data_3DKH # _entry.id 3DKH # _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 3DKH RCSB RCSB048150 WWPDB D_1000048150 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 1GW0 MaL unspecified PDB 2IH8 'a low-dose structure of rMaL' unspecified PDB 2IH9 'a high-dose structure of rMaL' unspecified PDB 2Q9O 'a near atomic resolution structure of rMal' unspecified # _pdbx_database_status.entry_id 3DKH _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site PDBJ _pdbx_database_status.recvd_initial_deposition_date 2008-06-25 _pdbx_database_status.status_code REL _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.methods_development_category ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Hakulinen, N.' 1 'Rouvinen, J.' 2 # _citation.id primary _citation.title 'Essential role of the C-terminus in Melanocarpus albomyces laccase for enzyme production, catalytic properties and structure' _citation.journal_abbrev 'Febs J.' _citation.journal_volume 276 _citation.page_first 6285 _citation.page_last 6300 _citation.year 2009 _citation.journal_id_ASTM ? _citation.country UK _citation.journal_id_ISSN 1742-464X _citation.journal_id_CSD ? _citation.book_publisher ? _citation.pdbx_database_id_PubMed 19780817 _citation.pdbx_database_id_DOI 10.1111/j.1742-4658.2009.07336.x # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Andberg, M.' 1 primary 'Hakulinen, N.' 2 primary 'Auer, S.' 3 primary 'Saloheimo, M.' 4 primary 'Koivula, A.' 5 primary 'Rouvinen, J.' 6 primary 'Kruus, K.' 7 # _cell.length_a 173.510 _cell.length_b 62.020 _cell.length_c 125.670 _cell.angle_alpha 90.000 _cell.angle_beta 99.920 _cell.angle_gamma 90.000 _cell.entry_id 3DKH _cell.pdbx_unique_axis ? _cell.Z_PDB 8 _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.space_group_name_H-M 'C 1 2 1' _symmetry.entry_id 3DKH _symmetry.Int_Tables_number 5 _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.space_group_name_Hall ? # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer man Laccase-1 61803.363 2 1.10.3.2 L559A ? ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 24 ? ? ? ? 3 non-polymer man BETA-D-MANNOSE 180.156 5 ? ? ? ? 4 non-polymer man ALPHA-D-MANNOSE 180.156 1 ? ? ? ? 5 non-polymer syn 'COPPER (II) ION' 63.546 8 ? ? ? ? 6 non-polymer syn 'CHLORIDE ION' 35.453 1 ? ? ? ? 7 non-polymer syn 'SULFATE ION' 96.063 3 ? ? ? ? 8 non-polymer syn 'OXYGEN MOLECULE' 31.999 2 ? ? ? ? 9 non-polymer syn GLYCEROL 92.094 1 ? ? ? ? 10 water nat water 18.015 706 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'Benzenediol:oxygen oxidoreductase 1, Urishiol oxidase 1, Diphenol oxidase 1, Ligninolytic phenoloxidase' # _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 ;EPTCNTPSNRACWSDGFDINTDYEVSTPDTGVTQSYVFNLTEVDNWMGPDGVVKEKVMLINGNIMGPNIVANWGDTVEVT VINNLVTNGTSIHWHGIHQKDTNLHDGANGVTECPIPPKGGQRTYRWRARQYGTSWYHSHFSAQYGNGVVGTIQINGPAS LPYDIDLGVFPITDYYYRAADDLVHFTQNNAPPFSDNVLINGTAVNPNTGEGQYANVTLTPGKRHRLRILNTSTENHFQV SLVNHTMTVIAADMVPVNAMTVDSLFLAVGQRYDVVIDASRAPDNYWFNVTFGGQAACGGSLNPHPAAIFHYAGAPGGLP TDEGTPPVDHQCLDTLDVRPVVPRSVPVNSFVKRPDNTLPVALDLTGTPLFVWKVNGSDINVDWGKPIIDYILTGNTSYP VSDNIVQVDAVDQWTYWLIENDPEGPFSLPHPMHLHGHDFLVLGRSPDVPAASQQRFVFDPAVDLARLNGDNPPRRDTTM LPAGGWLLLAFRTDNPGAWLFHCHIAWHVSGGLSVDFLERPADLRQRISQEDEDDFNRVCDEWRAYWPTNPYPKIDSGA ; _entity_poly.pdbx_seq_one_letter_code_can ;EPTCNTPSNRACWSDGFDINTDYEVSTPDTGVTQSYVFNLTEVDNWMGPDGVVKEKVMLINGNIMGPNIVANWGDTVEVT VINNLVTNGTSIHWHGIHQKDTNLHDGANGVTECPIPPKGGQRTYRWRARQYGTSWYHSHFSAQYGNGVVGTIQINGPAS LPYDIDLGVFPITDYYYRAADDLVHFTQNNAPPFSDNVLINGTAVNPNTGEGQYANVTLTPGKRHRLRILNTSTENHFQV SLVNHTMTVIAADMVPVNAMTVDSLFLAVGQRYDVVIDASRAPDNYWFNVTFGGQAACGGSLNPHPAAIFHYAGAPGGLP TDEGTPPVDHQCLDTLDVRPVVPRSVPVNSFVKRPDNTLPVALDLTGTPLFVWKVNGSDINVDWGKPIIDYILTGNTSYP VSDNIVQVDAVDQWTYWLIENDPEGPFSLPHPMHLHGHDFLVLGRSPDVPAASQQRFVFDPAVDLARLNGDNPPRRDTTM LPAGGWLLLAFRTDNPGAWLFHCHIAWHVSGGLSVDFLERPADLRQRISQEDEDDFNRVCDEWRAYWPTNPYPKIDSGA ; _entity_poly.pdbx_strand_id A,B _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 GLU n 1 2 PRO n 1 3 THR n 1 4 CYS n 1 5 ASN n 1 6 THR n 1 7 PRO n 1 8 SER n 1 9 ASN n 1 10 ARG n 1 11 ALA n 1 12 CYS n 1 13 TRP n 1 14 SER n 1 15 ASP n 1 16 GLY n 1 17 PHE n 1 18 ASP n 1 19 ILE n 1 20 ASN n 1 21 THR n 1 22 ASP n 1 23 TYR n 1 24 GLU n 1 25 VAL n 1 26 SER n 1 27 THR n 1 28 PRO n 1 29 ASP n 1 30 THR n 1 31 GLY n 1 32 VAL n 1 33 THR n 1 34 GLN n 1 35 SER n 1 36 TYR n 1 37 VAL n 1 38 PHE n 1 39 ASN n 1 40 LEU n 1 41 THR n 1 42 GLU n 1 43 VAL n 1 44 ASP n 1 45 ASN n 1 46 TRP n 1 47 MET n 1 48 GLY n 1 49 PRO n 1 50 ASP n 1 51 GLY n 1 52 VAL n 1 53 VAL n 1 54 LYS n 1 55 GLU n 1 56 LYS n 1 57 VAL n 1 58 MET n 1 59 LEU n 1 60 ILE n 1 61 ASN n 1 62 GLY n 1 63 ASN n 1 64 ILE n 1 65 MET n 1 66 GLY n 1 67 PRO n 1 68 ASN n 1 69 ILE n 1 70 VAL n 1 71 ALA n 1 72 ASN n 1 73 TRP n 1 74 GLY n 1 75 ASP n 1 76 THR n 1 77 VAL n 1 78 GLU n 1 79 VAL n 1 80 THR n 1 81 VAL n 1 82 ILE n 1 83 ASN n 1 84 ASN n 1 85 LEU n 1 86 VAL n 1 87 THR n 1 88 ASN n 1 89 GLY n 1 90 THR n 1 91 SER n 1 92 ILE n 1 93 HIS n 1 94 TRP n 1 95 HIS n 1 96 GLY n 1 97 ILE n 1 98 HIS n 1 99 GLN n 1 100 LYS n 1 101 ASP n 1 102 THR n 1 103 ASN n 1 104 LEU n 1 105 HIS n 1 106 ASP n 1 107 GLY n 1 108 ALA n 1 109 ASN n 1 110 GLY n 1 111 VAL n 1 112 THR n 1 113 GLU n 1 114 CYS n 1 115 PRO n 1 116 ILE n 1 117 PRO n 1 118 PRO n 1 119 LYS n 1 120 GLY n 1 121 GLY n 1 122 GLN n 1 123 ARG n 1 124 THR n 1 125 TYR n 1 126 ARG n 1 127 TRP n 1 128 ARG n 1 129 ALA n 1 130 ARG n 1 131 GLN n 1 132 TYR n 1 133 GLY n 1 134 THR n 1 135 SER n 1 136 TRP n 1 137 TYR n 1 138 HIS n 1 139 SER n 1 140 HIS n 1 141 PHE n 1 142 SER n 1 143 ALA n 1 144 GLN n 1 145 TYR n 1 146 GLY n 1 147 ASN n 1 148 GLY n 1 149 VAL n 1 150 VAL n 1 151 GLY n 1 152 THR n 1 153 ILE n 1 154 GLN n 1 155 ILE n 1 156 ASN n 1 157 GLY n 1 158 PRO n 1 159 ALA n 1 160 SER n 1 161 LEU n 1 162 PRO n 1 163 TYR n 1 164 ASP n 1 165 ILE n 1 166 ASP n 1 167 LEU n 1 168 GLY n 1 169 VAL n 1 170 PHE n 1 171 PRO n 1 172 ILE n 1 173 THR n 1 174 ASP n 1 175 TYR n 1 176 TYR n 1 177 TYR n 1 178 ARG n 1 179 ALA n 1 180 ALA n 1 181 ASP n 1 182 ASP n 1 183 LEU n 1 184 VAL n 1 185 HIS n 1 186 PHE n 1 187 THR n 1 188 GLN n 1 189 ASN n 1 190 ASN n 1 191 ALA n 1 192 PRO n 1 193 PRO n 1 194 PHE n 1 195 SER n 1 196 ASP n 1 197 ASN n 1 198 VAL n 1 199 LEU n 1 200 ILE n 1 201 ASN n 1 202 GLY n 1 203 THR n 1 204 ALA n 1 205 VAL n 1 206 ASN n 1 207 PRO n 1 208 ASN n 1 209 THR n 1 210 GLY n 1 211 GLU n 1 212 GLY n 1 213 GLN n 1 214 TYR n 1 215 ALA n 1 216 ASN n 1 217 VAL n 1 218 THR n 1 219 LEU n 1 220 THR n 1 221 PRO n 1 222 GLY n 1 223 LYS n 1 224 ARG n 1 225 HIS n 1 226 ARG n 1 227 LEU n 1 228 ARG n 1 229 ILE n 1 230 LEU n 1 231 ASN n 1 232 THR n 1 233 SER n 1 234 THR n 1 235 GLU n 1 236 ASN n 1 237 HIS n 1 238 PHE n 1 239 GLN n 1 240 VAL n 1 241 SER n 1 242 LEU n 1 243 VAL n 1 244 ASN n 1 245 HIS n 1 246 THR n 1 247 MET n 1 248 THR n 1 249 VAL n 1 250 ILE n 1 251 ALA n 1 252 ALA n 1 253 ASP n 1 254 MET n 1 255 VAL n 1 256 PRO n 1 257 VAL n 1 258 ASN n 1 259 ALA n 1 260 MET n 1 261 THR n 1 262 VAL n 1 263 ASP n 1 264 SER n 1 265 LEU n 1 266 PHE n 1 267 LEU n 1 268 ALA n 1 269 VAL n 1 270 GLY n 1 271 GLN n 1 272 ARG n 1 273 TYR n 1 274 ASP n 1 275 VAL n 1 276 VAL n 1 277 ILE n 1 278 ASP n 1 279 ALA n 1 280 SER n 1 281 ARG n 1 282 ALA n 1 283 PRO n 1 284 ASP n 1 285 ASN n 1 286 TYR n 1 287 TRP n 1 288 PHE n 1 289 ASN n 1 290 VAL n 1 291 THR n 1 292 PHE n 1 293 GLY n 1 294 GLY n 1 295 GLN n 1 296 ALA n 1 297 ALA n 1 298 CYS n 1 299 GLY n 1 300 GLY n 1 301 SER n 1 302 LEU n 1 303 ASN n 1 304 PRO n 1 305 HIS n 1 306 PRO n 1 307 ALA n 1 308 ALA n 1 309 ILE n 1 310 PHE n 1 311 HIS n 1 312 TYR n 1 313 ALA n 1 314 GLY n 1 315 ALA n 1 316 PRO n 1 317 GLY n 1 318 GLY n 1 319 LEU n 1 320 PRO n 1 321 THR n 1 322 ASP n 1 323 GLU n 1 324 GLY n 1 325 THR n 1 326 PRO n 1 327 PRO n 1 328 VAL n 1 329 ASP n 1 330 HIS n 1 331 GLN n 1 332 CYS n 1 333 LEU n 1 334 ASP n 1 335 THR n 1 336 LEU n 1 337 ASP n 1 338 VAL n 1 339 ARG n 1 340 PRO n 1 341 VAL n 1 342 VAL n 1 343 PRO n 1 344 ARG n 1 345 SER n 1 346 VAL n 1 347 PRO n 1 348 VAL n 1 349 ASN n 1 350 SER n 1 351 PHE n 1 352 VAL n 1 353 LYS n 1 354 ARG n 1 355 PRO n 1 356 ASP n 1 357 ASN n 1 358 THR n 1 359 LEU n 1 360 PRO n 1 361 VAL n 1 362 ALA n 1 363 LEU n 1 364 ASP n 1 365 LEU n 1 366 THR n 1 367 GLY n 1 368 THR n 1 369 PRO n 1 370 LEU n 1 371 PHE n 1 372 VAL n 1 373 TRP n 1 374 LYS n 1 375 VAL n 1 376 ASN n 1 377 GLY n 1 378 SER n 1 379 ASP n 1 380 ILE n 1 381 ASN n 1 382 VAL n 1 383 ASP n 1 384 TRP n 1 385 GLY n 1 386 LYS n 1 387 PRO n 1 388 ILE n 1 389 ILE n 1 390 ASP n 1 391 TYR n 1 392 ILE n 1 393 LEU n 1 394 THR n 1 395 GLY n 1 396 ASN n 1 397 THR n 1 398 SER n 1 399 TYR n 1 400 PRO n 1 401 VAL n 1 402 SER n 1 403 ASP n 1 404 ASN n 1 405 ILE n 1 406 VAL n 1 407 GLN n 1 408 VAL n 1 409 ASP n 1 410 ALA n 1 411 VAL n 1 412 ASP n 1 413 GLN n 1 414 TRP n 1 415 THR n 1 416 TYR n 1 417 TRP n 1 418 LEU n 1 419 ILE n 1 420 GLU n 1 421 ASN n 1 422 ASP n 1 423 PRO n 1 424 GLU n 1 425 GLY n 1 426 PRO n 1 427 PHE n 1 428 SER n 1 429 LEU n 1 430 PRO n 1 431 HIS n 1 432 PRO n 1 433 MET n 1 434 HIS n 1 435 LEU n 1 436 HIS n 1 437 GLY n 1 438 HIS n 1 439 ASP n 1 440 PHE n 1 441 LEU n 1 442 VAL n 1 443 LEU n 1 444 GLY n 1 445 ARG n 1 446 SER n 1 447 PRO n 1 448 ASP n 1 449 VAL n 1 450 PRO n 1 451 ALA n 1 452 ALA n 1 453 SER n 1 454 GLN n 1 455 GLN n 1 456 ARG n 1 457 PHE n 1 458 VAL n 1 459 PHE n 1 460 ASP n 1 461 PRO n 1 462 ALA n 1 463 VAL n 1 464 ASP n 1 465 LEU n 1 466 ALA n 1 467 ARG n 1 468 LEU n 1 469 ASN n 1 470 GLY n 1 471 ASP n 1 472 ASN n 1 473 PRO n 1 474 PRO n 1 475 ARG n 1 476 ARG n 1 477 ASP n 1 478 THR n 1 479 THR n 1 480 MET n 1 481 LEU n 1 482 PRO n 1 483 ALA n 1 484 GLY n 1 485 GLY n 1 486 TRP n 1 487 LEU n 1 488 LEU n 1 489 LEU n 1 490 ALA n 1 491 PHE n 1 492 ARG n 1 493 THR n 1 494 ASP n 1 495 ASN n 1 496 PRO n 1 497 GLY n 1 498 ALA n 1 499 TRP n 1 500 LEU n 1 501 PHE n 1 502 HIS n 1 503 CYS n 1 504 HIS n 1 505 ILE n 1 506 ALA n 1 507 TRP n 1 508 HIS n 1 509 VAL n 1 510 SER n 1 511 GLY n 1 512 GLY n 1 513 LEU n 1 514 SER n 1 515 VAL n 1 516 ASP n 1 517 PHE n 1 518 LEU n 1 519 GLU n 1 520 ARG n 1 521 PRO n 1 522 ALA n 1 523 ASP n 1 524 LEU n 1 525 ARG n 1 526 GLN n 1 527 ARG n 1 528 ILE n 1 529 SER n 1 530 GLN n 1 531 GLU n 1 532 ASP n 1 533 GLU n 1 534 ASP n 1 535 ASP n 1 536 PHE n 1 537 ASN n 1 538 ARG n 1 539 VAL n 1 540 CYS n 1 541 ASP n 1 542 GLU n 1 543 TRP n 1 544 ARG n 1 545 ALA n 1 546 TYR n 1 547 TRP n 1 548 PRO n 1 549 THR n 1 550 ASN n 1 551 PRO n 1 552 TYR n 1 553 PRO n 1 554 LYS n 1 555 ILE n 1 556 ASP n 1 557 SER n 1 558 GLY n 1 559 ALA 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 ? _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene LAC1 _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain 'VTT D-96490' _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 'Melanocarpus albomyces' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 204285 _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 'Saccharomyces cerevisiae' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 4932 _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 INVSc1 _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line ? _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type 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 pMS175 _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code LAC1_MELAO _struct_ref.pdbx_db_accession Q70KY3 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;EPTCNTPSNRACWSDGFDINTDYEVSTPDTGVTQSYVFNLTEVDNWMGPDGVVKEKVMLINGNIMGPNIVANWGDTVEVT VINNLVTNGTSIHWHGIHQKDTNLHDGANGVTECPIPPKGGQRTYRWRARQYGTSWYHSHFSAQYGNGVVGTIQINGPAS LPYDIDLGVFPITDYYYRAADDLVHFTQNNAPPFSDNVLINGTAVNPNTGEGQYANVTLTPGKRHRLRILNTSTENHFQV SLVNHTMTVIAADMVPVNAMTVDSLFLAVGQRYDVVIDASRAPDNYWFNVTFGGQAACGGSLNPHPAAIFHYAGAPGGLP TDEGTPPVDHQCLDTLDVRPVVPRSVPVNSFVKRPDNTLPVALDLTGTPLFVWKVNGSDINVDWGKPIIDYILTGNTSYP VSDNIVQVDAVDQWTYWLIENDPEGPFSLPHPMHLHGHDFLVLGRSPDVPAASQQRFVFDPAVDLARLNGDNPPRRDTTM LPAGGWLLLAFRTDNPGAWLFHCHIAWHVSGGLSVDFLERPADLRQRISQEDEDDFNRVCDEWRAYWPTNPYPKIDSGL ; _struct_ref.pdbx_align_begin 51 _struct_ref.pdbx_db_isoform ? # loop_ _struct_ref_seq.align_id _struct_ref_seq.ref_id _struct_ref_seq.pdbx_PDB_id_code _struct_ref_seq.pdbx_strand_id _struct_ref_seq.seq_align_beg _struct_ref_seq.pdbx_seq_align_beg_ins_code _struct_ref_seq.seq_align_end _struct_ref_seq.pdbx_seq_align_end_ins_code _struct_ref_seq.pdbx_db_accession _struct_ref_seq.db_align_beg _struct_ref_seq.pdbx_db_align_beg_ins_code _struct_ref_seq.db_align_end _struct_ref_seq.pdbx_db_align_end_ins_code _struct_ref_seq.pdbx_auth_seq_align_beg _struct_ref_seq.pdbx_auth_seq_align_end 1 1 3DKH A 1 ? 559 ? Q70KY3 51 ? 609 ? 1 559 2 1 3DKH B 1 ? 559 ? Q70KY3 51 ? 609 ? 1 559 # 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 3DKH ALA A 559 ? UNP Q70KY3 LEU 609 'ENGINEERED MUTATION' 559 1 2 3DKH ALA B 559 ? UNP Q70KY3 LEU 609 'ENGINEERED MUTATION' 559 2 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 BMA D-saccharide . BETA-D-MANNOSE ? 'C6 H12 O6' 180.156 CL non-polymer . 'CHLORIDE ION' ? 'Cl -1' 35.453 CU non-polymer . 'COPPER (II) ION' ? 'Cu 2' 63.546 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 GOL non-polymer . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3' 92.094 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MAN D-saccharide . ALPHA-D-MANNOSE ? 'C6 H12 O6' 180.156 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 OXY non-polymer . 'OXYGEN MOLECULE' ? O2 31.999 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 SO4 non-polymer . 'SULFATE ION' ? 'O4 S -2' 96.063 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.crystals_number 1 _exptl.entry_id 3DKH _exptl.method 'X-RAY DIFFRACTION' # _exptl_crystal.id 1 _exptl_crystal.pdbx_mosaicity ? _exptl_crystal.pdbx_mosaicity_esd ? _exptl_crystal.density_Matthews 2.69 _exptl_crystal.density_diffrn ? _exptl_crystal.density_meas ? _exptl_crystal.density_meas_temp ? _exptl_crystal.density_percent_sol 54.35 _exptl_crystal.size_max ? _exptl_crystal.size_mid ? _exptl_crystal.size_min ? _exptl_crystal.size_rad ? _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.pH 4.5 _exptl_crystal_grow.temp 295 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pdbx_details '15% PEG MME 2000, 0.2M AMMONIUM SULPHATE, 0.1M SODIUM ACETATE, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K' _exptl_crystal_grow.pdbx_pH_range . # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'MARMOSAIC 300 mm CCD' _diffrn_detector.pdbx_collection_date 2006-02-21 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.monochromator 'Double crystal Si[111]' _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.365 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'EMBL/DESY, HAMBURG BEAMLINE X12' _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 1.365 _diffrn_source.pdbx_synchrotron_site 'EMBL/DESY, Hamburg' _diffrn_source.pdbx_synchrotron_beamline X12 # _reflns.entry_id 3DKH _reflns.d_resolution_high 2.400 _reflns.number_obs 50625 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_netI_over_sigmaI 9.050 _reflns.percent_possible_obs 97.400 _reflns.B_iso_Wilson_estimate 26.726 _reflns.observed_criterion_sigma_I -3.00 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 20.00 _reflns.number_all ? _reflns.pdbx_Rsym_value 0.118 _reflns.pdbx_redundancy 3.7 _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _reflns_shell.d_res_high 2.40 _reflns_shell.d_res_low 2.50 _reflns_shell.number_measured_obs 19653 _reflns_shell.number_measured_all ? _reflns_shell.number_unique_obs 5497 _reflns_shell.Rmerge_I_obs ? _reflns_shell.meanI_over_sigI_obs 4.0 _reflns_shell.pdbx_Rsym_value 0.323 _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_redundancy 3.6 _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all ? _reflns_shell.percent_possible_all 92.30 _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 # _refine.entry_id 3DKH _refine.ls_d_res_high 2.400 _refine.ls_d_res_low 19.82 _refine.pdbx_ls_sigma_F 0.00 _refine.ls_percent_reflns_obs 97.700 _refine.ls_number_reflns_obs 50625 _refine.ls_R_factor_R_work 0.224 _refine.ls_R_factor_R_free 0.282 _refine.ls_percent_reflns_R_free 4.900 _refine.ls_number_reflns_R_free 2532 _refine.B_iso_mean 21.120 _refine.solvent_model_param_bsol 10.000 _refine.aniso_B[1][1] 2.183 _refine.aniso_B[2][2] 9.889 _refine.aniso_B[3][3] -12.072 _refine.aniso_B[1][2] 0.000 _refine.aniso_B[1][3] -4.280 _refine.aniso_B[2][3] 0.000 _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.B_iso_max 85.10 _refine.B_iso_min 1.00 _refine.occupancy_max 1.00 _refine.occupancy_min 1.00 _refine.pdbx_ls_sigma_I ? _refine.ls_number_reflns_all ? _refine.ls_R_factor_all ? _refine.ls_R_factor_obs ? _refine.ls_redundancy_reflns_obs ? _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.pdbx_starting_model 'PDB ENTRY 2Q9O' _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_stereochemistry_target_values 'Engh & Huber' _refine.solvent_model_details ? _refine.solvent_model_param_ksol ? _refine.pdbx_isotropic_thermal_model ? _refine.details ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.pdbx_solvent_vdw_probe_radii ? _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.overall_SU_ML ? _refine.overall_SU_B ? _refine.pdbx_overall_ESU_R_Free ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.pdbx_overall_ESU_R ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_overall_phase_error ? _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 8714 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 436 _refine_hist.number_atoms_solvent 706 _refine_hist.number_atoms_total 9856 _refine_hist.d_res_high 2.400 _refine_hist.d_res_low 19.82 # loop_ _refine_ls_restr.type _refine_ls_restr.number _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function c_bond_d ? 0.012 ? ? 'X-RAY DIFFRACTION' ? c_angle_d ? 1.585 ? ? 'X-RAY DIFFRACTION' ? c_mcbond_it ? 1.245 1.500 ? 'X-RAY DIFFRACTION' ? c_scbond_it ? 1.763 2.000 ? 'X-RAY DIFFRACTION' ? c_mcangle_it ? 1.994 2.000 ? 'X-RAY DIFFRACTION' ? c_scangle_it ? 2.522 2.500 ? 'X-RAY DIFFRACTION' ? # loop_ _pdbx_xplor_file.serial_no _pdbx_xplor_file.param_file _pdbx_xplor_file.topol_file _pdbx_xplor_file.pdbx_refine_id 1 protein.param protein.top 'X-RAY DIFFRACTION' 2 carbohydrate.param carbohydrate.top 'X-RAY DIFFRACTION' 3 water_rep.param water.top 'X-RAY DIFFRACTION' 4 ion.param ion.top 'X-RAY DIFFRACTION' 5 gol.param nina.top 'X-RAY DIFFRACTION' # _struct.entry_id 3DKH _struct.title 'L559A mutant of Melanocarpus albomyces laccase' _struct.pdbx_descriptor 'Laccase-1 (E.C.1.10.3.2)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 3DKH _struct_keywords.pdbx_keywords OXIDOREDUCTASE _struct_keywords.text 'laccase, multicopper oxidase, C-terminal mutant, ascomycete, Glycoprotein, Lignin degradation, Metal-binding, Oxidoreductase' # 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 1 ? C N N 2 ? D N N 2 ? E N N 2 ? F N N 3 ? G N N 4 ? H N N 2 ? I N N 2 ? J N N 2 ? K N N 2 ? L N N 3 ? M N N 2 ? N N N 2 ? O N N 2 ? P N N 2 ? Q N N 2 ? R N N 5 ? S N N 5 ? T N N 5 ? U N N 5 ? V N N 6 ? W N N 7 ? X N N 7 ? Y N N 8 ? Z N N 2 ? AA N N 2 ? BA N N 2 ? CA N N 3 ? DA N N 2 ? EA N N 2 ? FA N N 3 ? GA N N 2 ? HA N N 2 ? IA N N 3 ? JA N N 2 ? KA N N 2 ? LA N N 2 ? MA N N 2 ? NA N N 2 ? OA N N 5 ? PA N N 5 ? QA N N 5 ? RA N N 5 ? SA N N 7 ? TA N N 8 ? UA N N 9 ? VA N N 10 ? WA N N 10 ? # _struct_biol.id 1 _struct_biol.details ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 THR A 102 ? ASP A 106 ? THR A 102 ASP A 106 5 ? 5 HELX_P HELX_P2 2 ALA A 143 ? GLY A 148 ? ALA A 143 GLY A 148 5 ? 6 HELX_P HELX_P3 3 ALA A 179 ? ASN A 190 ? ALA A 179 ASN A 190 1 ? 12 HELX_P HELX_P4 4 PRO A 387 ? THR A 394 ? PRO A 387 THR A 394 1 ? 8 HELX_P HELX_P5 5 PRO A 400 ? ASP A 403 ? PRO A 400 ASP A 403 5 ? 4 HELX_P HELX_P6 6 ASP A 460 ? LEU A 465 ? ASP A 460 LEU A 465 1 ? 6 HELX_P HELX_P7 7 ILE A 505 ? GLY A 512 ? ILE A 505 GLY A 512 1 ? 8 HELX_P HELX_P8 8 ARG A 520 ? ILE A 528 ? ARG A 520 ILE A 528 1 ? 9 HELX_P HELX_P9 9 SER A 529 ? TRP A 547 ? SER A 529 TRP A 547 1 ? 19 HELX_P HELX_P10 10 PRO A 548 ? ASN A 550 ? PRO A 548 ASN A 550 5 ? 3 HELX_P HELX_P11 11 THR B 102 ? ASP B 106 ? THR B 102 ASP B 106 5 ? 5 HELX_P HELX_P12 12 ALA B 143 ? ASN B 147 ? ALA B 143 ASN B 147 5 ? 5 HELX_P HELX_P13 13 ALA B 179 ? ASN B 190 ? ALA B 179 ASN B 190 1 ? 12 HELX_P HELX_P14 14 ARG B 354 ? ASP B 356 ? ARG B 354 ASP B 356 5 ? 3 HELX_P HELX_P15 15 PRO B 387 ? THR B 394 ? PRO B 387 THR B 394 1 ? 8 HELX_P HELX_P16 16 PRO B 400 ? ASP B 403 ? PRO B 400 ASP B 403 5 ? 4 HELX_P HELX_P17 17 ASP B 460 ? LEU B 465 ? ASP B 460 LEU B 465 1 ? 6 HELX_P HELX_P18 18 ILE B 505 ? GLY B 512 ? ILE B 505 GLY B 512 1 ? 8 HELX_P HELX_P19 19 ARG B 520 ? ILE B 528 ? ARG B 520 ILE B 528 1 ? 9 HELX_P HELX_P20 20 SER B 529 ? TRP B 547 ? SER B 529 TRP B 547 1 ? 19 HELX_P HELX_P21 21 PRO B 548 ? ASN B 550 ? PRO B 548 ASN B 550 5 ? 3 # _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 4 SG ? ? ? 1_555 A CYS 12 SG ? ? A CYS 4 A CYS 12 1_555 ? ? ? ? ? ? ? 2.038 ? disulf2 disulf ? ? A CYS 114 SG ? ? ? 1_555 A CYS 540 SG ? ? A CYS 114 A CYS 540 1_555 ? ? ? ? ? ? ? 2.037 ? disulf3 disulf ? ? A CYS 298 SG ? ? ? 1_555 A CYS 332 SG ? ? A CYS 298 A CYS 332 1_555 ? ? ? ? ? ? ? 2.028 ? disulf4 disulf ? ? B CYS 4 SG ? ? ? 1_555 B CYS 12 SG ? ? B CYS 4 B CYS 12 1_555 ? ? ? ? ? ? ? 2.035 ? disulf5 disulf ? ? B CYS 114 SG ? ? ? 1_555 B CYS 540 SG ? ? B CYS 114 B CYS 540 1_555 ? ? ? ? ? ? ? 2.035 ? disulf6 disulf ? ? B CYS 298 SG ? ? ? 1_555 B CYS 332 SG ? ? B CYS 298 B CYS 332 1_555 ? ? ? ? ? ? ? 2.029 ? covale1 covale ? ? A ASN 39 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 39 A NAG 700 1_555 ? ? ? ? ? ? ? 1.451 ? covale2 covale ? ? A ASN 88 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 88 A NAG 710 1_555 ? ? ? ? ? ? ? 1.448 ? metalc1 metalc ? ? A HIS 93 NE2 ? ? ? 1_555 U CU . CU ? ? A HIS 93 A CU 604 1_555 ? ? ? ? ? ? ? 2.027 ? metalc2 metalc ? ? A HIS 95 ND1 ? ? ? 1_555 T CU . CU ? ? A HIS 95 A CU 603 1_555 ? ? ? ? ? ? ? 2.185 ? metalc3 metalc ? ? A HIS 138 NE2 ? ? ? 1_555 T CU . CU ? ? A HIS 138 A CU 603 1_555 ? ? ? ? ? ? ? 2.278 ? metalc4 metalc ? ? A HIS 140 NE2 ? ? ? 1_555 S CU . CU ? ? A HIS 140 A CU 602 1_555 ? ? ? ? ? ? ? 2.188 ? covale3 covale ? ? A ASN 201 ND2 ? ? ? 1_555 P NAG . C1 ? ? A ASN 201 A NAG 760 1_555 ? ? ? ? ? ? ? 1.451 ? covale4 covale ? ? A ASN 216 ND2 ? ? ? 1_555 H NAG . C1 ? ? A ASN 216 A NAG 720 1_555 ? ? ? ? ? ? ? 1.449 ? covale5 covale ? ? A ASN 289 ND2 ? ? ? 1_555 J NAG . C1 ? ? A ASN 289 A NAG 730 1_555 ? ? ? ? ? ? ? 1.450 ? covale6 covale ? ? A ASN 376 ND2 ? ? ? 1_555 M NAG . C1 ? ? A ASN 376 A NAG 740 1_555 ? ? ? ? ? ? ? 1.450 ? covale7 covale ? ? A ASN 396 ND2 ? ? ? 1_555 O NAG . C1 ? ? A ASN 396 A NAG 750 1_555 ? ? ? ? ? ? ? 1.451 ? metalc5 metalc ? ? A HIS 431 ND1 ? ? ? 1_555 R CU . CU ? ? A HIS 431 A CU 601 1_555 ? ? ? ? ? ? ? 2.162 ? metalc6 metalc ? ? A HIS 434 NE2 ? ? ? 1_555 U CU . CU ? ? A HIS 434 A CU 604 1_555 ? ? ? ? ? ? ? 2.068 ? metalc7 metalc ? ? A HIS 436 NE2 ? ? ? 1_555 S CU . CU ? ? A HIS 436 A CU 602 1_555 ? ? ? ? ? ? ? 2.072 ? metalc8 metalc ? ? A HIS 502 NE2 ? ? ? 1_555 S CU . CU ? ? A HIS 502 A CU 602 1_555 ? ? ? ? ? ? ? 2.165 ? metalc9 metalc ? ? A HIS 504 NE2 ? ? ? 1_555 T CU . CU ? ? A HIS 504 A CU 603 1_555 ? ? ? ? ? ? ? 2.170 ? metalc10 metalc ? ? A HIS 508 ND1 ? ? ? 1_555 R CU . CU ? ? A HIS 508 A CU 601 1_555 ? ? ? ? ? ? ? 2.281 ? covale8 covale ? ? B ASN 39 ND2 ? ? ? 1_555 Z NAG . C1 ? ? B ASN 39 B NAG 700 1_555 ? ? ? ? ? ? ? 1.447 ? covale9 covale ? ? B ASN 88 ND2 ? ? ? 1_555 AA NAG . C1 ? ? B ASN 88 B NAG 710 1_555 ? ? ? ? ? ? ? 1.447 ? metalc11 metalc ? ? B HIS 93 NE2 ? ? ? 1_555 RA CU . CU ? ? B HIS 93 B CU 604 1_555 ? ? ? ? ? ? ? 2.009 ? metalc12 metalc ? ? B HIS 95 ND1 ? ? ? 1_555 QA CU . CU ? ? B HIS 95 B CU 603 1_555 ? ? ? ? ? ? ? 2.209 ? metalc13 metalc ? ? B HIS 138 NE2 ? ? ? 1_555 QA CU . CU ? ? B HIS 138 B CU 603 1_555 ? ? ? ? ? ? ? 2.222 ? metalc14 metalc ? ? B HIS 140 NE2 ? ? ? 1_555 PA CU . CU ? ? B HIS 140 B CU 602 1_555 ? ? ? ? ? ? ? 2.278 ? covale10 covale ? ? B ASN 201 ND2 ? ? ? 1_555 MA NAG . C1 ? ? B ASN 201 B NAG 760 1_555 ? ? ? ? ? ? ? 1.458 ? covale11 covale ? ? B ASN 216 ND2 ? ? ? 1_555 DA NAG . C1 ? ? B ASN 216 B NAG 720 1_555 ? ? ? ? ? ? ? 1.450 ? covale12 covale ? ? B ASN 244 ND2 ? ? ? 1_555 NA NAG . C1 ? ? B ASN 244 B NAG 770 1_555 ? ? ? ? ? ? ? 1.453 ? covale13 covale ? ? B ASN 289 ND2 ? ? ? 1_555 GA NAG . C1 ? ? B ASN 289 B NAG 730 1_555 ? ? ? ? ? ? ? 1.450 ? covale14 covale ? ? B ASN 376 ND2 ? ? ? 1_555 JA NAG . C1 ? ? B ASN 376 B NAG 740 1_555 ? ? ? ? ? ? ? 1.451 ? covale15 covale ? ? B ASN 396 ND2 ? ? ? 1_555 LA NAG . C1 ? ? B ASN 396 B NAG 750 1_555 ? ? ? ? ? ? ? 1.448 ? metalc15 metalc ? ? B HIS 431 ND1 ? ? ? 1_555 OA CU . CU ? ? B HIS 431 B CU 601 1_555 ? ? ? ? ? ? ? 2.136 ? metalc16 metalc ? ? B HIS 434 NE2 ? ? ? 1_555 RA CU . CU ? ? B HIS 434 B CU 604 1_555 ? ? ? ? ? ? ? 2.095 ? metalc17 metalc ? ? B HIS 436 NE2 ? ? ? 1_555 PA CU . CU ? ? B HIS 436 B CU 602 1_555 ? ? ? ? ? ? ? 2.084 ? metalc18 metalc ? ? B HIS 502 NE2 ? ? ? 1_555 PA CU . CU ? ? B HIS 502 B CU 602 1_555 ? ? ? ? ? ? ? 2.098 ? metalc19 metalc ? ? B HIS 504 NE2 ? ? ? 1_555 QA CU . CU ? ? B HIS 504 B CU 603 1_555 ? ? ? ? ? ? ? 2.145 ? metalc20 metalc ? ? B HIS 508 ND1 ? ? ? 1_555 OA CU . CU ? ? B HIS 508 B CU 601 1_555 ? ? ? ? ? ? ? 2.077 ? covale16 covale ? ? D NAG . O4 ? ? ? 1_555 E NAG . C1 ? ? A NAG 710 A NAG 711 1_555 ? ? ? ? ? ? ? 1.383 ? covale17 covale ? ? E NAG . O4 ? ? ? 1_555 F BMA . C1 ? ? A NAG 711 A BMA 712 1_555 ? ? ? ? ? ? ? 1.380 ? covale18 covale ? ? F BMA . O6 ? ? ? 1_555 G MAN . C1 ? ? A BMA 712 A MAN 714 1_555 ? ? ? ? ? ? ? 1.403 ? covale19 covale ? ? H NAG . O4 ? ? ? 1_555 I NAG . C1 ? ? A NAG 720 A NAG 721 1_555 ? ? ? ? ? ? ? 1.387 ? covale20 covale ? ? J NAG . O4 ? ? ? 1_555 K NAG . C1 ? ? A NAG 730 A NAG 731 1_555 ? ? ? ? ? ? ? 1.383 ? covale21 covale ? ? K NAG . O4 ? ? ? 1_555 L BMA . C1 ? ? A NAG 731 A BMA 732 1_555 ? ? ? ? ? ? ? 1.383 ? covale22 covale ? ? M NAG . O4 ? ? ? 1_555 N NAG . C1 ? ? A NAG 740 A NAG 741 1_555 ? ? ? ? ? ? ? 1.387 ? covale23 covale ? ? P NAG . O4 ? ? ? 1_555 Q NAG . C1 ? ? A NAG 760 A NAG 761 1_555 ? ? ? ? ? ? ? 1.388 ? covale24 covale ? ? AA NAG . O4 ? ? ? 1_555 BA NAG . C1 ? ? B NAG 710 B NAG 711 1_555 ? ? ? ? ? ? ? 1.381 ? covale25 covale ? ? BA NAG . O4 ? ? ? 1_555 CA BMA . C1 ? ? B NAG 711 B BMA 712 1_555 ? ? ? ? ? ? ? 1.380 ? covale26 covale ? ? DA NAG . O4 ? ? ? 1_555 EA NAG . C1 ? ? B NAG 720 B NAG 721 1_555 ? ? ? ? ? ? ? 1.382 ? covale27 covale ? ? EA NAG . O4 ? ? ? 1_555 FA BMA . C1 ? ? B NAG 721 B BMA 722 1_555 ? ? ? ? ? ? ? 1.390 ? covale28 covale ? ? GA NAG . O4 ? ? ? 1_555 HA NAG . C1 ? ? B NAG 730 B NAG 731 1_555 ? ? ? ? ? ? ? 1.382 ? covale29 covale ? ? HA NAG . O4 ? ? ? 1_555 IA BMA . C1 ? ? B NAG 731 B BMA 732 1_555 ? ? ? ? ? ? ? 1.385 ? covale30 covale ? ? JA NAG . O4 ? ? ? 1_555 KA NAG . C1 ? ? B NAG 740 B NAG 741 1_555 ? ? ? ? ? ? ? 1.388 ? metalc21 metalc ? ? B CYS 503 SG ? ? ? 1_555 OA CU . CU ? ? B CYS 503 B CU 601 1_555 ? ? ? ? ? ? ? 2.119 ? metalc22 metalc ? ? A CYS 503 SG ? ? ? 1_555 R CU . CU ? ? A CYS 503 A CU 601 1_555 ? ? ? ? ? ? ? 2.188 ? metalc23 metalc ? ? PA CU . CU ? ? ? 1_555 TA OXY . O1 ? ? B CU 602 B OXY 901 1_555 ? ? ? ? ? ? ? 2.473 ? metalc24 metalc ? ? T CU . CU ? ? ? 1_555 Y OXY . O2 ? ? A CU 603 A OXY 900 1_555 ? ? ? ? ? ? ? 2.488 ? metalc25 metalc ? ? S CU . CU ? ? ? 1_555 Y OXY . O1 ? ? A CU 602 A OXY 900 1_555 ? ? ? ? ? ? ? 2.590 ? metalc26 metalc ? ? PA CU . CU ? ? ? 1_555 TA OXY . O2 ? ? B CU 602 B OXY 901 1_555 ? ? ? ? ? ? ? 2.613 ? metalc27 metalc ? ? QA CU . CU ? ? ? 1_555 TA OXY . O2 ? ? B CU 603 B OXY 901 1_555 ? ? ? ? ? ? ? 2.669 ? metalc28 metalc ? ? S CU . CU ? ? ? 1_555 Y OXY . O2 ? ? A CU 602 A OXY 900 1_555 ? ? ? ? ? ? ? 2.672 ? # 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 THR 368 A . ? THR 368 A PRO 369 A ? PRO 369 A 1 -0.31 2 THR 368 B . ? THR 368 B PRO 369 B ? PRO 369 B 1 -0.42 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 2 ? B ? 4 ? C ? 4 ? D ? 6 ? E ? 5 ? F ? 6 ? G ? 5 ? H ? 2 ? I ? 4 ? J ? 4 ? K ? 6 ? L ? 5 ? M ? 6 ? N ? 5 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? anti-parallel B 1 2 ? anti-parallel B 2 3 ? parallel B 3 4 ? anti-parallel C 1 2 ? parallel C 2 3 ? anti-parallel C 3 4 ? anti-parallel D 1 2 ? anti-parallel D 2 3 ? parallel D 3 4 ? anti-parallel D 4 5 ? anti-parallel D 5 6 ? anti-parallel E 1 2 ? parallel E 2 3 ? anti-parallel E 3 4 ? anti-parallel E 4 5 ? anti-parallel F 1 2 ? anti-parallel F 2 3 ? parallel F 3 4 ? anti-parallel F 4 5 ? anti-parallel F 5 6 ? anti-parallel G 1 2 ? parallel G 2 3 ? anti-parallel G 3 4 ? anti-parallel G 4 5 ? anti-parallel H 1 2 ? anti-parallel I 1 2 ? anti-parallel I 2 3 ? parallel I 3 4 ? anti-parallel J 1 2 ? parallel J 2 3 ? anti-parallel J 3 4 ? anti-parallel K 1 2 ? anti-parallel K 2 3 ? parallel K 3 4 ? anti-parallel K 4 5 ? anti-parallel K 5 6 ? anti-parallel L 1 2 ? parallel L 2 3 ? anti-parallel L 3 4 ? anti-parallel L 4 5 ? anti-parallel M 1 2 ? anti-parallel M 2 3 ? parallel M 3 4 ? anti-parallel M 4 5 ? anti-parallel M 5 6 ? anti-parallel N 1 2 ? parallel N 2 3 ? anti-parallel N 3 4 ? anti-parallel N 4 5 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 CYS A 12 ? SER A 14 ? CYS A 12 SER A 14 A 2 PHE A 17 ? ASP A 18 ? PHE A 17 ASP A 18 B 1 VAL A 53 ? ILE A 60 ? VAL A 53 ILE A 60 B 2 THR A 33 ? MET A 47 ? THR A 33 MET A 47 B 3 THR A 76 ? ASN A 83 ? THR A 76 ASN A 83 B 4 GLY A 121 ? ARG A 128 ? GLY A 121 ARG A 128 C 1 ILE A 69 ? ASN A 72 ? ILE A 69 ASN A 72 C 2 VAL A 150 ? ASN A 156 ? VAL A 150 ASN A 156 C 3 GLY A 133 ? HIS A 138 ? GLY A 133 HIS A 138 C 4 HIS A 93 ? HIS A 95 ? HIS A 93 HIS A 95 D 1 ASN A 197 ? ILE A 200 ? ASN A 197 ILE A 200 D 2 ILE A 165 ? TYR A 175 ? ILE A 165 TYR A 175 D 3 ARG A 224 ? ASN A 231 ? ARG A 224 ASN A 231 D 4 ARG A 272 ? ASP A 278 ? ARG A 272 ASP A 278 D 5 MET A 247 ? ALA A 252 ? MET A 247 ALA A 252 D 6 VAL A 255 ? VAL A 262 ? VAL A 255 VAL A 262 E 1 ASN A 216 ? LEU A 219 ? ASN A 216 LEU A 219 E 2 ALA A 307 ? TYR A 312 ? ALA A 307 TYR A 312 E 3 ASN A 285 ? THR A 291 ? ASN A 285 THR A 291 E 4 PHE A 238 ? LEU A 242 ? PHE A 238 LEU A 242 E 5 SER A 264 ? LEU A 267 ? SER A 264 LEU A 267 F 1 VAL A 372 ? VAL A 375 ? VAL A 372 VAL A 375 F 2 THR A 358 ? ASP A 364 ? THR A 358 ASP A 364 F 3 TRP A 414 ? ASN A 421 ? TRP A 414 ASN A 421 F 4 TRP A 486 ? ARG A 492 ? TRP A 486 ARG A 492 F 5 PHE A 440 ? ARG A 445 ? PHE A 440 ARG A 445 F 6 ARG A 475 ? ARG A 476 ? ARG A 475 ARG A 476 G 1 ILE A 405 ? VAL A 408 ? ILE A 405 VAL A 408 G 2 SER A 514 ? GLU A 519 ? SER A 514 GLU A 519 G 3 GLY A 497 ? CYS A 503 ? GLY A 497 CYS A 503 G 4 HIS A 431 ? LEU A 435 ? HIS A 431 LEU A 435 G 5 THR A 478 ? LEU A 481 ? THR A 478 LEU A 481 H 1 CYS B 12 ? SER B 14 ? CYS B 12 SER B 14 H 2 PHE B 17 ? ASP B 18 ? PHE B 17 ASP B 18 I 1 VAL B 53 ? ILE B 60 ? VAL B 53 ILE B 60 I 2 THR B 33 ? MET B 47 ? THR B 33 MET B 47 I 3 THR B 76 ? ASN B 84 ? THR B 76 ASN B 84 I 4 GLY B 121 ? ARG B 128 ? GLY B 121 ARG B 128 J 1 ILE B 69 ? ASN B 72 ? ILE B 69 ASN B 72 J 2 VAL B 150 ? ASN B 156 ? VAL B 150 ASN B 156 J 3 GLY B 133 ? SER B 139 ? GLY B 133 SER B 139 J 4 ILE B 92 ? HIS B 95 ? ILE B 92 HIS B 95 K 1 ASN B 197 ? ILE B 200 ? ASN B 197 ILE B 200 K 2 ILE B 165 ? TYR B 175 ? ILE B 165 TYR B 175 K 3 ARG B 224 ? ASN B 231 ? ARG B 224 ASN B 231 K 4 ARG B 272 ? ASP B 278 ? ARG B 272 ASP B 278 K 5 MET B 247 ? ALA B 252 ? MET B 247 ALA B 252 K 6 VAL B 255 ? VAL B 262 ? VAL B 255 VAL B 262 L 1 ASN B 216 ? LEU B 219 ? ASN B 216 LEU B 219 L 2 ALA B 307 ? TYR B 312 ? ALA B 307 TYR B 312 L 3 ASN B 285 ? THR B 291 ? ASN B 285 THR B 291 L 4 PHE B 238 ? LEU B 242 ? PHE B 238 LEU B 242 L 5 SER B 264 ? LEU B 267 ? SER B 264 LEU B 267 M 1 VAL B 372 ? VAL B 375 ? VAL B 372 VAL B 375 M 2 THR B 358 ? ASP B 364 ? THR B 358 ASP B 364 M 3 TRP B 414 ? ASN B 421 ? TRP B 414 ASN B 421 M 4 TRP B 486 ? ARG B 492 ? TRP B 486 ARG B 492 M 5 PHE B 440 ? ARG B 445 ? PHE B 440 ARG B 445 M 6 ARG B 475 ? ARG B 476 ? ARG B 475 ARG B 476 N 1 ILE B 405 ? VAL B 408 ? ILE B 405 VAL B 408 N 2 SER B 514 ? GLU B 519 ? SER B 514 GLU B 519 N 3 GLY B 497 ? CYS B 503 ? GLY B 497 CYS B 503 N 4 HIS B 431 ? LEU B 435 ? HIS B 431 LEU B 435 N 5 THR B 478 ? LEU B 481 ? THR B 478 LEU B 481 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 N SER A 14 ? N SER A 14 O PHE A 17 ? O PHE A 17 B 1 2 O LEU A 59 ? O LEU A 59 N THR A 41 ? N THR A 41 B 2 3 N PHE A 38 ? N PHE A 38 O THR A 80 ? O THR A 80 B 3 4 N ASN A 83 ? N ASN A 83 O GLY A 121 ? O GLY A 121 C 1 2 N ALA A 71 ? N ALA A 71 O ASN A 156 ? O ASN A 156 C 2 3 O GLY A 151 ? O GLY A 151 N TYR A 137 ? N TYR A 137 C 3 4 O HIS A 138 ? O HIS A 138 N HIS A 93 ? N HIS A 93 D 1 2 O ASN A 197 ? O ASN A 197 N TYR A 175 ? N TYR A 175 D 2 3 N ILE A 165 ? N ILE A 165 O ARG A 226 ? O ARG A 226 D 3 4 N LEU A 227 ? N LEU A 227 O VAL A 275 ? O VAL A 275 D 4 5 O ASP A 274 ? O ASP A 274 N ILE A 250 ? N ILE A 250 D 5 6 N MET A 247 ? N MET A 247 O VAL A 262 ? O VAL A 262 E 1 2 N LEU A 219 ? N LEU A 219 O HIS A 311 ? O HIS A 311 E 2 3 O PHE A 310 ? O PHE A 310 N TYR A 286 ? N TYR A 286 E 3 4 O ASN A 289 ? O ASN A 289 N SER A 241 ? N SER A 241 E 4 5 N PHE A 238 ? N PHE A 238 O LEU A 267 ? O LEU A 267 F 1 2 O LYS A 374 ? O LYS A 374 N ALA A 362 ? N ALA A 362 F 2 3 N LEU A 359 ? N LEU A 359 O LEU A 418 ? O LEU A 418 F 3 4 N ILE A 419 ? N ILE A 419 O LEU A 487 ? O LEU A 487 F 4 5 O ALA A 490 ? O ALA A 490 N LEU A 441 ? N LEU A 441 F 5 6 N PHE A 440 ? N PHE A 440 O ARG A 476 ? O ARG A 476 G 1 2 N VAL A 406 ? N VAL A 406 O ASP A 516 ? O ASP A 516 G 2 3 O PHE A 517 ? O PHE A 517 N TRP A 499 ? N TRP A 499 G 3 4 O HIS A 502 ? O HIS A 502 N HIS A 434 ? N HIS A 434 G 4 5 N HIS A 431 ? N HIS A 431 O LEU A 481 ? O LEU A 481 H 1 2 N SER B 14 ? N SER B 14 O PHE B 17 ? O PHE B 17 I 1 2 O LEU B 59 ? O LEU B 59 N THR B 41 ? N THR B 41 I 2 3 N PHE B 38 ? N PHE B 38 O THR B 80 ? O THR B 80 I 3 4 N ASN B 83 ? N ASN B 83 O GLY B 121 ? O GLY B 121 J 1 2 N ILE B 69 ? N ILE B 69 O GLN B 154 ? O GLN B 154 J 2 3 O ILE B 153 ? O ILE B 153 N SER B 135 ? N SER B 135 J 3 4 O HIS B 138 ? O HIS B 138 N HIS B 93 ? N HIS B 93 K 1 2 O LEU B 199 ? O LEU B 199 N THR B 173 ? N THR B 173 K 2 3 N ILE B 165 ? N ILE B 165 O ARG B 226 ? O ARG B 226 K 3 4 N HIS B 225 ? N HIS B 225 O ILE B 277 ? O ILE B 277 K 4 5 O ASP B 274 ? O ASP B 274 N ILE B 250 ? N ILE B 250 K 5 6 N MET B 247 ? N MET B 247 O VAL B 262 ? O VAL B 262 L 1 2 N LEU B 219 ? N LEU B 219 O HIS B 311 ? O HIS B 311 L 2 3 O PHE B 310 ? O PHE B 310 N TYR B 286 ? N TYR B 286 L 3 4 O ASN B 289 ? O ASN B 289 N SER B 241 ? N SER B 241 L 4 5 N PHE B 238 ? N PHE B 238 O LEU B 267 ? O LEU B 267 M 1 2 O LYS B 374 ? O LYS B 374 N ALA B 362 ? N ALA B 362 M 2 3 N LEU B 359 ? N LEU B 359 O LEU B 418 ? O LEU B 418 M 3 4 N TRP B 417 ? N TRP B 417 O LEU B 489 ? O LEU B 489 M 4 5 O LEU B 488 ? O LEU B 488 N GLY B 444 ? N GLY B 444 M 5 6 N PHE B 440 ? N PHE B 440 O ARG B 476 ? O ARG B 476 N 1 2 N VAL B 406 ? N VAL B 406 O ASP B 516 ? O ASP B 516 N 2 3 O PHE B 517 ? O PHE B 517 N TRP B 499 ? N TRP B 499 N 3 4 O HIS B 502 ? O HIS B 502 N HIS B 434 ? N HIS B 434 N 4 5 N HIS B 431 ? N HIS B 431 O LEU B 481 ? O LEU B 481 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 700' AC2 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE NAG A 710' AC3 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE NAG A 711' AC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE BMA A 712' AC5 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE MAN A 714' AC6 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE NAG A 720' AC7 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 721' AC8 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE NAG A 730' AC9 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE NAG A 731' BC1 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE BMA A 732' BC2 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 740' BC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG A 741' BC4 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 750' BC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG A 760' BC6 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 761' BC7 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG B 700' BC8 Software ? ? ? ? 11 'BINDING SITE FOR RESIDUE NAG B 710' BC9 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE NAG B 711' CC1 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE BMA B 712' CC2 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG B 720' CC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG B 721' CC4 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE BMA B 722' CC5 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE NAG B 730' CC6 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG B 731' CC7 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE BMA B 732' CC8 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG B 740' CC9 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG B 741' DC1 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG B 750' DC2 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE NAG B 760' DC3 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE NAG B 770' DC4 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE CU A 601' DC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU A 602' DC6 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CU A 603' DC7 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CU A 604' DC8 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE CL A 610' DC9 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE CU B 601' EC1 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU B 602' EC2 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CU B 603' EC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU B 604' EC4 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE SO4 A 800' EC5 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE SO4 B 801' EC6 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE SO4 A 802' EC7 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE OXY A 900' EC8 Software ? ? ? ? 11 'BINDING SITE FOR RESIDUE OXY B 901' EC9 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE GOL B 810' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 5 ASN A 39 ? ASN A 39 . ? 1_555 ? 2 AC1 5 THR A 41 ? THR A 41 . ? 1_555 ? 3 AC1 5 ASN A 84 ? ASN A 84 . ? 1_555 ? 4 AC1 5 GLU B 78 ? GLU B 78 . ? 3_455 ? 5 AC1 5 ARG B 126 ? ARG B 126 . ? 3_455 ? 6 AC2 10 LYS A 56 ? LYS A 56 . ? 1_555 ? 7 AC2 10 THR A 87 ? THR A 87 . ? 1_555 ? 8 AC2 10 ASN A 88 ? ASN A 88 . ? 1_555 ? 9 AC2 10 ASP A 181 ? ASP A 181 . ? 1_555 ? 10 AC2 10 ASN A 550 ? ASN A 550 . ? 1_555 ? 11 AC2 10 TYR A 552 ? TYR A 552 . ? 1_555 ? 12 AC2 10 PRO A 553 ? PRO A 553 . ? 1_555 ? 13 AC2 10 NAG E . ? NAG A 711 . ? 1_555 ? 14 AC2 10 HOH VA . ? HOH A 964 . ? 1_555 ? 15 AC2 10 HOH VA . ? HOH A 979 . ? 1_555 ? 16 AC3 8 GLU A 55 ? GLU A 55 . ? 1_555 ? 17 AC3 8 ALA A 179 ? ALA A 179 . ? 1_555 ? 18 AC3 8 ASP A 181 ? ASP A 181 . ? 1_555 ? 19 AC3 8 ASP A 182 ? ASP A 182 . ? 1_555 ? 20 AC3 8 NAG D . ? NAG A 710 . ? 1_555 ? 21 AC3 8 BMA F . ? BMA A 712 . ? 1_555 ? 22 AC3 8 HOH VA . ? HOH A 1068 . ? 1_555 ? 23 AC3 8 HOH VA . ? HOH A 1140 . ? 1_555 ? 24 AC4 4 NAG E . ? NAG A 711 . ? 1_555 ? 25 AC4 4 MAN G . ? MAN A 714 . ? 1_555 ? 26 AC4 4 HOH VA . ? HOH A 1068 . ? 1_555 ? 27 AC4 4 HOH VA . ? HOH A 1217 . ? 1_555 ? 28 AC5 3 ARG A 178 ? ARG A 178 . ? 1_555 ? 29 AC5 3 BMA F . ? BMA A 712 . ? 1_555 ? 30 AC5 3 HOH VA . ? HOH A 1140 . ? 1_555 ? 31 AC6 8 ASN A 216 ? ASN A 216 . ? 1_555 ? 32 AC6 8 THR A 218 ? THR A 218 . ? 1_555 ? 33 AC6 8 HIS A 311 ? HIS A 311 . ? 1_555 ? 34 AC6 8 GLY A 317 ? GLY A 317 . ? 1_555 ? 35 AC6 8 GLY A 318 ? GLY A 318 . ? 1_555 ? 36 AC6 8 NAG I . ? NAG A 721 . ? 1_555 ? 37 AC6 8 HOH VA . ? HOH A 1075 . ? 1_555 ? 38 AC6 8 HOH VA . ? HOH A 1205 . ? 1_555 ? 39 AC7 5 HIS A 311 ? HIS A 311 . ? 1_555 ? 40 AC7 5 GLY A 314 ? GLY A 314 . ? 1_555 ? 41 AC7 5 GLY A 317 ? GLY A 317 . ? 1_555 ? 42 AC7 5 NAG H . ? NAG A 720 . ? 1_555 ? 43 AC7 5 HOH VA . ? HOH A 1232 . ? 1_555 ? 44 AC8 10 TRP A 287 ? TRP A 287 . ? 1_555 ? 45 AC8 10 ASN A 289 ? ASN A 289 . ? 1_555 ? 46 AC8 10 HIS A 305 ? HIS A 305 . ? 1_555 ? 47 AC8 10 ALA A 307 ? ALA A 307 . ? 1_555 ? 48 AC8 10 GLU A 323 ? GLU A 323 . ? 1_555 ? 49 AC8 10 THR A 325 ? THR A 325 . ? 1_555 ? 50 AC8 10 PRO A 326 ? PRO A 326 . ? 1_555 ? 51 AC8 10 NAG K . ? NAG A 731 . ? 1_555 ? 52 AC8 10 HOH VA . ? HOH A 904 . ? 1_555 ? 53 AC8 10 HOH VA . ? HOH A 1079 . ? 1_555 ? 54 AC9 7 TYR A 214 ? TYR A 214 . ? 1_555 ? 55 AC9 7 TRP A 287 ? TRP A 287 . ? 1_555 ? 56 AC9 7 HIS A 305 ? HIS A 305 . ? 1_555 ? 57 AC9 7 GLU A 323 ? GLU A 323 . ? 1_555 ? 58 AC9 7 NAG J . ? NAG A 730 . ? 1_555 ? 59 AC9 7 BMA L . ? BMA A 732 . ? 1_555 ? 60 AC9 7 HOH VA . ? HOH A 1206 . ? 1_555 ? 61 BC1 2 NAG K . ? NAG A 731 . ? 1_555 ? 62 BC1 2 HOH VA . ? HOH A 995 . ? 1_555 ? 63 BC2 5 PRO A 355 ? PRO A 355 . ? 1_555 ? 64 BC2 5 ASP A 356 ? ASP A 356 . ? 1_555 ? 65 BC2 5 ASN A 376 ? ASN A 376 . ? 1_555 ? 66 BC2 5 VAL A 406 ? VAL A 406 . ? 1_555 ? 67 BC2 5 NAG N . ? NAG A 741 . ? 1_555 ? 68 BC3 4 ASP A 356 ? ASP A 356 . ? 1_555 ? 69 BC3 4 NAG M . ? NAG A 740 . ? 1_555 ? 70 BC3 4 HOH VA . ? HOH A 1200 . ? 1_555 ? 71 BC3 4 HOH VA . ? HOH A 1234 . ? 1_555 ? 72 BC4 6 LYS A 386 ? LYS A 386 . ? 1_555 ? 73 BC4 6 TYR A 391 ? TYR A 391 . ? 1_555 ? 74 BC4 6 ASN A 396 ? ASN A 396 . ? 1_555 ? 75 BC4 6 HOH VA . ? HOH A 1156 . ? 1_555 ? 76 BC4 6 GLN B 530 ? GLN B 530 . ? 2_555 ? 77 BC4 6 GLU B 533 ? GLU B 533 . ? 2_555 ? 78 BC5 4 LEU A 167 ? LEU A 167 . ? 1_555 ? 79 BC5 4 ASN A 201 ? ASN A 201 . ? 1_555 ? 80 BC5 4 VAL A 217 ? VAL A 217 . ? 1_555 ? 81 BC5 4 NAG Q . ? NAG A 761 . ? 1_555 ? 82 BC6 2 NAG P . ? NAG A 760 . ? 1_555 ? 83 BC6 2 HOH VA . ? HOH A 1056 . ? 1_555 ? 84 BC7 6 GLU A 78 ? GLU A 78 . ? 3_545 ? 85 BC7 6 ARG A 126 ? ARG A 126 . ? 3_545 ? 86 BC7 6 ASN B 39 ? ASN B 39 . ? 1_555 ? 87 BC7 6 THR B 41 ? THR B 41 . ? 1_555 ? 88 BC7 6 ASN B 84 ? ASN B 84 . ? 1_555 ? 89 BC7 6 HOH WA . ? HOH B 992 . ? 1_555 ? 90 BC8 11 LYS B 56 ? LYS B 56 . ? 1_555 ? 91 BC8 11 THR B 87 ? THR B 87 . ? 1_555 ? 92 BC8 11 ASN B 88 ? ASN B 88 . ? 1_555 ? 93 BC8 11 ASP B 181 ? ASP B 181 . ? 1_555 ? 94 BC8 11 ASN B 550 ? ASN B 550 . ? 1_555 ? 95 BC8 11 TYR B 552 ? TYR B 552 . ? 1_555 ? 96 BC8 11 PRO B 553 ? PRO B 553 . ? 1_555 ? 97 BC8 11 NAG BA . ? NAG B 711 . ? 1_555 ? 98 BC8 11 HOH WA . ? HOH B 918 . ? 1_555 ? 99 BC8 11 HOH WA . ? HOH B 1119 . ? 1_555 ? 100 BC8 11 HOH WA . ? HOH B 1141 . ? 1_555 ? 101 BC9 8 GLU B 55 ? GLU B 55 . ? 1_555 ? 102 BC9 8 ALA B 179 ? ALA B 179 . ? 1_555 ? 103 BC9 8 ASP B 181 ? ASP B 181 . ? 1_555 ? 104 BC9 8 ASP B 182 ? ASP B 182 . ? 1_555 ? 105 BC9 8 NAG AA . ? NAG B 710 . ? 1_555 ? 106 BC9 8 BMA CA . ? BMA B 712 . ? 1_555 ? 107 BC9 8 HOH WA . ? HOH B 1065 . ? 1_555 ? 108 BC9 8 HOH WA . ? HOH B 1141 . ? 1_555 ? 109 CC1 3 ASP B 182 ? ASP B 182 . ? 1_555 ? 110 CC1 3 NAG BA . ? NAG B 711 . ? 1_555 ? 111 CC1 3 HOH WA . ? HOH B 1163 . ? 1_555 ? 112 CC2 6 ASN B 216 ? ASN B 216 . ? 1_555 ? 113 CC2 6 THR B 218 ? THR B 218 . ? 1_555 ? 114 CC2 6 ILE B 309 ? ILE B 309 . ? 1_555 ? 115 CC2 6 HIS B 311 ? HIS B 311 . ? 1_555 ? 116 CC2 6 NAG EA . ? NAG B 721 . ? 1_555 ? 117 CC2 6 HOH WA . ? HOH B 1093 . ? 1_555 ? 118 CC3 4 HIS B 311 ? HIS B 311 . ? 1_555 ? 119 CC3 4 GLY B 314 ? GLY B 314 . ? 1_555 ? 120 CC3 4 NAG DA . ? NAG B 720 . ? 1_555 ? 121 CC3 4 BMA FA . ? BMA B 722 . ? 1_555 ? 122 CC4 1 NAG EA . ? NAG B 721 . ? 1_555 ? 123 CC5 7 TRP B 287 ? TRP B 287 . ? 1_555 ? 124 CC5 7 ASN B 289 ? ASN B 289 . ? 1_555 ? 125 CC5 7 HIS B 305 ? HIS B 305 . ? 1_555 ? 126 CC5 7 ALA B 307 ? ALA B 307 . ? 1_555 ? 127 CC5 7 GLU B 323 ? GLU B 323 . ? 1_555 ? 128 CC5 7 NAG HA . ? NAG B 731 . ? 1_555 ? 129 CC5 7 HOH WA . ? HOH B 959 . ? 1_555 ? 130 CC6 6 TRP B 287 ? TRP B 287 . ? 1_555 ? 131 CC6 6 HIS B 305 ? HIS B 305 . ? 1_555 ? 132 CC6 6 GLU B 323 ? GLU B 323 . ? 1_555 ? 133 CC6 6 NAG GA . ? NAG B 730 . ? 1_555 ? 134 CC6 6 BMA IA . ? BMA B 732 . ? 1_555 ? 135 CC6 6 HOH WA . ? HOH B 1010 . ? 1_555 ? 136 CC7 1 NAG HA . ? NAG B 731 . ? 1_555 ? 137 CC8 6 PRO B 355 ? PRO B 355 . ? 1_555 ? 138 CC8 6 ASP B 356 ? ASP B 356 . ? 1_555 ? 139 CC8 6 ASN B 376 ? ASN B 376 . ? 1_555 ? 140 CC8 6 VAL B 406 ? VAL B 406 . ? 1_555 ? 141 CC8 6 NAG KA . ? NAG B 741 . ? 1_555 ? 142 CC8 6 HOH WA . ? HOH B 1017 . ? 1_555 ? 143 CC9 1 NAG JA . ? NAG B 740 . ? 1_555 ? 144 DC1 5 ASP A 379 ? ASP A 379 . ? 2_555 ? 145 DC1 5 ASN A 381 ? ASN A 381 . ? 2_555 ? 146 DC1 5 LYS B 386 ? LYS B 386 . ? 1_555 ? 147 DC1 5 TYR B 391 ? TYR B 391 . ? 1_555 ? 148 DC1 5 ASN B 396 ? ASN B 396 . ? 1_555 ? 149 DC2 7 LEU B 167 ? LEU B 167 . ? 1_555 ? 150 DC2 7 PHE B 170 ? PHE B 170 . ? 1_555 ? 151 DC2 7 ASN B 201 ? ASN B 201 . ? 1_555 ? 152 DC2 7 VAL B 217 ? VAL B 217 . ? 1_555 ? 153 DC2 7 HOH WA . ? HOH B 943 . ? 1_555 ? 154 DC2 7 HOH WA . ? HOH B 1001 . ? 1_555 ? 155 DC2 7 HOH WA . ? HOH B 1139 . ? 1_555 ? 156 DC3 7 ARG A 281 ? ARG A 281 . ? 2_556 ? 157 DC3 7 ASN B 244 ? ASN B 244 . ? 1_555 ? 158 DC3 7 ARG B 281 ? ARG B 281 . ? 1_555 ? 159 DC3 7 ALA B 282 ? ALA B 282 . ? 1_555 ? 160 DC3 7 TYR B 286 ? TYR B 286 . ? 1_555 ? 161 DC3 7 HOH WA . ? HOH B 912 . ? 1_555 ? 162 DC3 7 HOH WA . ? HOH B 1050 . ? 1_555 ? 163 DC4 3 HIS A 431 ? HIS A 431 . ? 1_555 ? 164 DC4 3 CYS A 503 ? CYS A 503 . ? 1_555 ? 165 DC4 3 HIS A 508 ? HIS A 508 . ? 1_555 ? 166 DC5 4 HIS A 140 ? HIS A 140 . ? 1_555 ? 167 DC5 4 HIS A 436 ? HIS A 436 . ? 1_555 ? 168 DC5 4 HIS A 502 ? HIS A 502 . ? 1_555 ? 169 DC5 4 OXY Y . ? OXY A 900 . ? 1_555 ? 170 DC6 5 HIS A 95 ? HIS A 95 . ? 1_555 ? 171 DC6 5 TRP A 136 ? TRP A 136 . ? 1_555 ? 172 DC6 5 HIS A 138 ? HIS A 138 . ? 1_555 ? 173 DC6 5 HIS A 504 ? HIS A 504 . ? 1_555 ? 174 DC6 5 OXY Y . ? OXY A 900 . ? 1_555 ? 175 DC7 5 HIS A 93 ? HIS A 93 . ? 1_555 ? 176 DC7 5 HIS A 434 ? HIS A 434 . ? 1_555 ? 177 DC7 5 HIS A 436 ? HIS A 436 . ? 1_555 ? 178 DC7 5 CL V . ? CL A 610 . ? 1_555 ? 179 DC7 5 OXY Y . ? OXY A 900 . ? 1_555 ? 180 DC8 7 HIS A 93 ? HIS A 93 . ? 1_555 ? 181 DC8 7 TRP A 94 ? TRP A 94 . ? 1_555 ? 182 DC8 7 HIS A 95 ? HIS A 95 . ? 1_555 ? 183 DC8 7 GLY A 96 ? GLY A 96 . ? 1_555 ? 184 DC8 7 HIS A 434 ? HIS A 434 . ? 1_555 ? 185 DC8 7 CU U . ? CU A 604 . ? 1_555 ? 186 DC8 7 HOH VA . ? HOH A 1022 . ? 1_555 ? 187 DC9 3 HIS B 431 ? HIS B 431 . ? 1_555 ? 188 DC9 3 CYS B 503 ? CYS B 503 . ? 1_555 ? 189 DC9 3 HIS B 508 ? HIS B 508 . ? 1_555 ? 190 EC1 4 HIS B 140 ? HIS B 140 . ? 1_555 ? 191 EC1 4 HIS B 436 ? HIS B 436 . ? 1_555 ? 192 EC1 4 HIS B 502 ? HIS B 502 . ? 1_555 ? 193 EC1 4 OXY TA . ? OXY B 901 . ? 1_555 ? 194 EC2 5 HIS B 95 ? HIS B 95 . ? 1_555 ? 195 EC2 5 TRP B 136 ? TRP B 136 . ? 1_555 ? 196 EC2 5 HIS B 138 ? HIS B 138 . ? 1_555 ? 197 EC2 5 HIS B 504 ? HIS B 504 . ? 1_555 ? 198 EC2 5 OXY TA . ? OXY B 901 . ? 1_555 ? 199 EC3 4 HIS B 93 ? HIS B 93 . ? 1_555 ? 200 EC3 4 HIS B 434 ? HIS B 434 . ? 1_555 ? 201 EC3 4 HIS B 436 ? HIS B 436 . ? 1_555 ? 202 EC3 4 OXY TA . ? OXY B 901 . ? 1_555 ? 203 EC4 6 ARG A 492 ? ARG A 492 . ? 1_555 ? 204 EC4 6 HOH VA . ? HOH A 1048 . ? 1_555 ? 205 EC4 6 HOH VA . ? HOH A 1163 . ? 1_555 ? 206 EC4 6 ARG B 128 ? ARG B 128 . ? 3_445 ? 207 EC4 6 ARG B 130 ? ARG B 130 . ? 3_445 ? 208 EC4 6 HOH WA . ? HOH B 1175 . ? 3_445 ? 209 EC5 3 ARG A 128 ? ARG A 128 . ? 3_555 ? 210 EC5 3 ARG A 130 ? ARG A 130 . ? 3_555 ? 211 EC5 3 ARG B 492 ? ARG B 492 . ? 1_555 ? 212 EC6 5 ARG A 520 ? ARG A 520 . ? 1_555 ? 213 EC6 5 ARG A 527 ? ARG A 527 . ? 1_555 ? 214 EC6 5 HOH VA . ? HOH A 1099 . ? 1_555 ? 215 EC6 5 ARG B 520 ? ARG B 520 . ? 3_445 ? 216 EC6 5 ARG B 527 ? ARG B 527 . ? 3_445 ? 217 EC7 10 HIS A 93 ? HIS A 93 . ? 1_555 ? 218 EC7 10 HIS A 138 ? HIS A 138 . ? 1_555 ? 219 EC7 10 HIS A 140 ? HIS A 140 . ? 1_555 ? 220 EC7 10 HIS A 434 ? HIS A 434 . ? 1_555 ? 221 EC7 10 HIS A 436 ? HIS A 436 . ? 1_555 ? 222 EC7 10 HIS A 502 ? HIS A 502 . ? 1_555 ? 223 EC7 10 HIS A 504 ? HIS A 504 . ? 1_555 ? 224 EC7 10 CU S . ? CU A 602 . ? 1_555 ? 225 EC7 10 CU T . ? CU A 603 . ? 1_555 ? 226 EC7 10 CU U . ? CU A 604 . ? 1_555 ? 227 EC8 11 HIS B 93 ? HIS B 93 . ? 1_555 ? 228 EC8 11 HIS B 138 ? HIS B 138 . ? 1_555 ? 229 EC8 11 HIS B 140 ? HIS B 140 . ? 1_555 ? 230 EC8 11 HIS B 434 ? HIS B 434 . ? 1_555 ? 231 EC8 11 HIS B 436 ? HIS B 436 . ? 1_555 ? 232 EC8 11 HIS B 502 ? HIS B 502 . ? 1_555 ? 233 EC8 11 HIS B 504 ? HIS B 504 . ? 1_555 ? 234 EC8 11 CU PA . ? CU B 602 . ? 1_555 ? 235 EC8 11 CU QA . ? CU B 603 . ? 1_555 ? 236 EC8 11 CU RA . ? CU B 604 . ? 1_555 ? 237 EC8 11 HOH WA . ? HOH B 1121 . ? 1_555 ? 238 EC9 3 PHE A 427 ? PHE A 427 . ? 1_555 ? 239 EC9 3 PHE B 427 ? PHE B 427 . ? 1_555 ? 240 EC9 3 HOH WA . ? HOH B 1219 . ? 1_555 ? # _atom_sites.entry_id 3DKH _atom_sites.fract_transf_matrix[1][1] 0.005763 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.001008 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.016124 _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] 0.008078 _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 CL CU 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 . PRO A 1 2 ? -54.286 -1.847 44.392 1.00 59.81 ? 2 PRO A N 1 ATOM 2 C CA . PRO A 1 2 ? -53.532 -2.109 45.643 1.00 59.18 ? 2 PRO A CA 1 ATOM 3 C C . PRO A 1 2 ? -54.431 -2.182 46.882 1.00 58.40 ? 2 PRO A C 1 ATOM 4 O O . PRO A 1 2 ? -54.908 -1.156 47.383 1.00 58.87 ? 2 PRO A O 1 ATOM 5 C CB . PRO A 1 2 ? -52.486 -1.006 45.784 1.00 59.82 ? 2 PRO A CB 1 ATOM 6 C CG . PRO A 1 2 ? -53.020 0.079 44.839 1.00 60.88 ? 2 PRO A CG 1 ATOM 7 C CD . PRO A 1 2 ? -53.729 -0.671 43.702 1.00 60.33 ? 2 PRO A CD 1 ATOM 8 N N . THR A 1 3 ? -54.666 -3.406 47.359 1.00 56.67 ? 3 THR A N 1 ATOM 9 C CA . THR A 1 3 ? -55.507 -3.649 48.535 1.00 54.12 ? 3 THR A CA 1 ATOM 10 C C . THR A 1 3 ? -54.742 -4.267 49.711 1.00 51.09 ? 3 THR A C 1 ATOM 11 O O . THR A 1 3 ? -54.695 -3.688 50.804 1.00 51.24 ? 3 THR A O 1 ATOM 12 C CB . THR A 1 3 ? -56.741 -4.544 48.192 1.00 54.80 ? 3 THR A CB 1 ATOM 13 O OG1 . THR A 1 3 ? -56.316 -5.726 47.503 1.00 55.02 ? 3 THR A OG1 1 ATOM 14 C CG2 . THR A 1 3 ? -57.748 -3.783 47.333 1.00 55.36 ? 3 THR A CG2 1 ATOM 15 N N . CYS A 1 4 ? -54.118 -5.419 49.462 1.00 46.64 ? 4 CYS A N 1 ATOM 16 C CA . CYS A 1 4 ? -53.366 -6.155 50.474 1.00 42.26 ? 4 CYS A CA 1 ATOM 17 C C . CYS A 1 4 ? -51.844 -5.972 50.418 1.00 39.39 ? 4 CYS A C 1 ATOM 18 O O . CYS A 1 4 ? -51.094 -6.798 50.949 1.00 39.37 ? 4 CYS A O 1 ATOM 19 C CB . CYS A 1 4 ? -53.739 -7.643 50.407 1.00 41.88 ? 4 CYS A CB 1 ATOM 20 S SG . CYS A 1 4 ? -53.449 -8.399 48.777 1.00 39.86 ? 4 CYS A SG 1 ATOM 21 N N . ASN A 1 5 ? -51.395 -4.881 49.796 1.00 36.02 ? 5 ASN A N 1 ATOM 22 C CA . ASN A 1 5 ? -49.967 -4.568 49.685 1.00 33.00 ? 5 ASN A CA 1 ATOM 23 C C . ASN A 1 5 ? -49.582 -3.625 50.827 1.00 32.66 ? 5 ASN A C 1 ATOM 24 O O . ASN A 1 5 ? -49.900 -2.433 50.803 1.00 33.53 ? 5 ASN A O 1 ATOM 25 C CB . ASN A 1 5 ? -49.659 -3.941 48.320 1.00 30.06 ? 5 ASN A CB 1 ATOM 26 C CG . ASN A 1 5 ? -48.172 -3.874 48.025 1.00 26.97 ? 5 ASN A CG 1 ATOM 27 O OD1 . ASN A 1 5 ? -47.579 -2.802 48.043 1.00 28.25 ? 5 ASN A OD1 1 ATOM 28 N ND2 . ASN A 1 5 ? -47.567 -5.020 47.739 1.00 24.41 ? 5 ASN A ND2 1 ATOM 29 N N . THR A 1 6 ? -48.939 -4.198 51.843 1.00 32.00 ? 6 THR A N 1 ATOM 30 C CA . THR A 1 6 ? -48.505 -3.490 53.052 1.00 31.37 ? 6 THR A CA 1 ATOM 31 C C . THR A 1 6 ? -47.002 -3.783 53.283 1.00 30.21 ? 6 THR A C 1 ATOM 32 O O . THR A 1 6 ? -46.454 -4.667 52.615 1.00 29.78 ? 6 THR A O 1 ATOM 33 C CB . THR A 1 6 ? -49.351 -3.983 54.291 1.00 31.83 ? 6 THR A CB 1 ATOM 34 O OG1 . THR A 1 6 ? -49.284 -5.408 54.387 1.00 35.19 ? 6 THR A OG1 1 ATOM 35 C CG2 . THR A 1 6 ? -50.812 -3.541 54.193 1.00 31.52 ? 6 THR A CG2 1 ATOM 36 N N . PRO A 1 7 ? -46.297 -3.003 54.157 1.00 29.01 ? 7 PRO A N 1 ATOM 37 C CA . PRO A 1 7 ? -44.869 -3.254 54.417 1.00 28.40 ? 7 PRO A CA 1 ATOM 38 C C . PRO A 1 7 ? -44.451 -4.649 54.881 1.00 28.71 ? 7 PRO A C 1 ATOM 39 O O . PRO A 1 7 ? -43.323 -5.065 54.624 1.00 30.01 ? 7 PRO A O 1 ATOM 40 C CB . PRO A 1 7 ? -44.536 -2.209 55.470 1.00 29.14 ? 7 PRO A CB 1 ATOM 41 C CG . PRO A 1 7 ? -45.276 -1.045 54.978 1.00 28.78 ? 7 PRO A CG 1 ATOM 42 C CD . PRO A 1 7 ? -46.635 -1.646 54.647 1.00 29.69 ? 7 PRO A CD 1 ATOM 43 N N . SER A 1 8 ? -45.354 -5.361 55.551 1.00 28.05 ? 8 SER A N 1 ATOM 44 C CA . SER A 1 8 ? -45.075 -6.713 56.040 1.00 28.27 ? 8 SER A CA 1 ATOM 45 C C . SER A 1 8 ? -45.487 -7.819 55.055 1.00 28.61 ? 8 SER A C 1 ATOM 46 O O . SER A 1 8 ? -45.043 -8.969 55.177 1.00 28.69 ? 8 SER A O 1 ATOM 47 C CB . SER A 1 8 ? -45.713 -6.929 57.421 1.00 28.41 ? 8 SER A CB 1 ATOM 48 O OG . SER A 1 8 ? -47.063 -6.496 57.455 1.00 26.10 ? 8 SER A OG 1 ATOM 49 N N . ASN A 1 9 ? -46.309 -7.457 54.070 1.00 28.58 ? 9 ASN A N 1 ATOM 50 C CA . ASN A 1 9 ? -46.773 -8.398 53.046 1.00 28.43 ? 9 ASN A CA 1 ATOM 51 C C . ASN A 1 9 ? -46.748 -7.725 51.668 1.00 27.92 ? 9 ASN A C 1 ATOM 52 O O . ASN A 1 9 ? -47.772 -7.243 51.172 1.00 29.47 ? 9 ASN A O 1 ATOM 53 C CB . ASN A 1 9 ? -48.185 -8.924 53.383 1.00 27.02 ? 9 ASN A CB 1 ATOM 54 C CG . ASN A 1 9 ? -48.610 -10.123 52.520 1.00 26.59 ? 9 ASN A CG 1 ATOM 55 O OD1 . ASN A 1 9 ? -47.843 -10.633 51.699 1.00 27.55 ? 9 ASN A OD1 1 ATOM 56 N ND2 . ASN A 1 9 ? -49.850 -10.567 52.706 1.00 26.02 ? 9 ASN A ND2 1 ATOM 57 N N . ARG A 1 10 ? -45.565 -7.689 51.060 1.00 26.68 ? 10 ARG A N 1 ATOM 58 C CA . ARG A 1 10 ? -45.410 -7.092 49.737 1.00 24.66 ? 10 ARG A CA 1 ATOM 59 C C . ARG A 1 10 ? -45.686 -8.110 48.643 1.00 23.56 ? 10 ARG A C 1 ATOM 60 O O . ARG A 1 10 ? -45.795 -7.751 47.480 1.00 22.41 ? 10 ARG A O 1 ATOM 61 C CB . ARG A 1 10 ? -44.014 -6.483 49.559 1.00 24.05 ? 10 ARG A CB 1 ATOM 62 C CG . ARG A 1 10 ? -43.768 -5.205 50.353 1.00 23.64 ? 10 ARG A CG 1 ATOM 63 C CD . ARG A 1 10 ? -44.634 -4.031 49.906 1.00 23.00 ? 10 ARG A CD 1 ATOM 64 N NE . ARG A 1 10 ? -44.236 -2.804 50.596 1.00 23.61 ? 10 ARG A NE 1 ATOM 65 C CZ . ARG A 1 10 ? -44.975 -1.698 50.697 1.00 23.77 ? 10 ARG A CZ 1 ATOM 66 N NH1 . ARG A 1 10 ? -46.187 -1.625 50.155 1.00 23.04 ? 10 ARG A NH1 1 ATOM 67 N NH2 . ARG A 1 10 ? -44.487 -0.648 51.345 1.00 24.33 ? 10 ARG A NH2 1 ATOM 68 N N . ALA A 1 11 ? -45.841 -9.372 49.042 1.00 24.39 ? 11 ALA A N 1 ATOM 69 C CA . ALA A 1 11 ? -46.114 -10.479 48.126 1.00 24.23 ? 11 ALA A CA 1 ATOM 70 C C . ALA A 1 11 ? -47.537 -10.442 47.575 1.00 24.46 ? 11 ALA A C 1 ATOM 71 O O . ALA A 1 11 ? -47.766 -10.826 46.433 1.00 24.46 ? 11 ALA A O 1 ATOM 72 C CB . ALA A 1 11 ? -45.841 -11.807 48.813 1.00 23.75 ? 11 ALA A CB 1 ATOM 73 N N . CYS A 1 12 ? -48.464 -9.926 48.381 1.00 25.29 ? 12 CYS A N 1 ATOM 74 C CA . CYS A 1 12 ? -49.879 -9.795 48.019 1.00 28.68 ? 12 CYS A CA 1 ATOM 75 C C . CYS A 1 12 ? -50.094 -8.465 47.274 1.00 27.44 ? 12 CYS A C 1 ATOM 76 O O . CYS A 1 12 ? -49.352 -7.504 47.487 1.00 25.43 ? 12 CYS A O 1 ATOM 77 C CB . CYS A 1 12 ? -50.736 -9.813 49.303 1.00 31.50 ? 12 CYS A CB 1 ATOM 78 S SG . CYS A 1 12 ? -52.533 -10.176 49.171 1.00 40.17 ? 12 CYS A SG 1 ATOM 79 N N . TRP A 1 13 ? -51.086 -8.429 46.384 1.00 27.72 ? 13 TRP A N 1 ATOM 80 C CA . TRP A 1 13 ? -51.422 -7.213 45.635 1.00 28.57 ? 13 TRP A CA 1 ATOM 81 C C . TRP A 1 13 ? -52.936 -6.982 45.626 1.00 28.70 ? 13 TRP A C 1 ATOM 82 O O . TRP A 1 13 ? -53.406 -5.969 46.143 1.00 28.94 ? 13 TRP A O 1 ATOM 83 C CB . TRP A 1 13 ? -50.848 -7.260 44.207 1.00 29.72 ? 13 TRP A CB 1 ATOM 84 C CG . TRP A 1 13 ? -51.052 -5.992 43.391 1.00 30.76 ? 13 TRP A CG 1 ATOM 85 C CD1 . TRP A 1 13 ? -51.854 -5.853 42.294 1.00 31.05 ? 13 TRP A CD1 1 ATOM 86 C CD2 . TRP A 1 13 ? -50.460 -4.700 43.620 1.00 31.17 ? 13 TRP A CD2 1 ATOM 87 N NE1 . TRP A 1 13 ? -51.802 -4.565 41.824 1.00 32.58 ? 13 TRP A NE1 1 ATOM 88 C CE2 . TRP A 1 13 ? -50.956 -3.832 42.612 1.00 30.39 ? 13 TRP A CE2 1 ATOM 89 C CE3 . TRP A 1 13 ? -49.556 -4.186 44.578 1.00 31.64 ? 13 TRP A CE3 1 ATOM 90 C CZ2 . TRP A 1 13 ? -50.580 -2.469 42.527 1.00 32.73 ? 13 TRP A CZ2 1 ATOM 91 C CZ3 . TRP A 1 13 ? -49.176 -2.816 44.500 1.00 32.47 ? 13 TRP A CZ3 1 ATOM 92 C CH2 . TRP A 1 13 ? -49.694 -1.979 43.474 1.00 33.50 ? 13 TRP A CH2 1 ATOM 93 N N . SER A 1 14 ? -53.675 -7.922 45.027 1.00 29.42 ? 14 SER A N 1 ATOM 94 C CA . SER A 1 14 ? -55.144 -7.896 44.937 1.00 29.56 ? 14 SER A CA 1 ATOM 95 C C . SER A 1 14 ? -55.657 -9.340 44.798 1.00 30.37 ? 14 SER A C 1 ATOM 96 O O . SER A 1 14 ? -54.861 -10.286 44.836 1.00 30.21 ? 14 SER A O 1 ATOM 97 C CB . SER A 1 14 ? -55.618 -7.026 43.751 1.00 29.17 ? 14 SER A CB 1 ATOM 98 O OG . SER A 1 14 ? -55.167 -7.520 42.498 1.00 26.15 ? 14 SER A OG 1 ATOM 99 N N . ASP A 1 15 ? -56.973 -9.506 44.633 1.00 30.96 ? 15 ASP A N 1 ATOM 100 C CA . ASP A 1 15 ? -57.595 -10.833 44.485 1.00 32.39 ? 15 ASP A CA 1 ATOM 101 C C . ASP A 1 15 ? -57.148 -11.560 43.204 1.00 31.11 ? 15 ASP A C 1 ATOM 102 O O . ASP A 1 15 ? -57.446 -11.127 42.085 1.00 30.29 ? 15 ASP A O 1 ATOM 103 C CB . ASP A 1 15 ? -59.129 -10.716 44.531 1.00 36.73 ? 15 ASP A CB 1 ATOM 104 C CG . ASP A 1 15 ? -59.828 -12.076 44.548 1.00 40.70 ? 15 ASP A CG 1 ATOM 105 O OD1 . ASP A 1 15 ? -60.603 -12.359 43.604 1.00 43.25 ? 15 ASP A OD1 1 ATOM 106 O OD2 . ASP A 1 15 ? -59.596 -12.857 45.499 1.00 42.03 ? 15 ASP A OD2 1 ATOM 107 N N . GLY A 1 16 ? -56.397 -12.643 43.400 1.00 29.81 ? 16 GLY A N 1 ATOM 108 C CA . GLY A 1 16 ? -55.891 -13.439 42.296 1.00 27.56 ? 16 GLY A CA 1 ATOM 109 C C . GLY A 1 16 ? -54.605 -12.927 41.691 1.00 26.38 ? 16 GLY A C 1 ATOM 110 O O . GLY A 1 16 ? -54.102 -13.497 40.720 1.00 27.90 ? 16 GLY A O 1 ATOM 111 N N . PHE A 1 17 ? -54.111 -11.811 42.220 1.00 23.55 ? 17 PHE A N 1 ATOM 112 C CA . PHE A 1 17 ? -52.885 -11.212 41.723 1.00 21.39 ? 17 PHE A CA 1 ATOM 113 C C . PHE A 1 17 ? -51.877 -11.010 42.834 1.00 20.91 ? 17 PHE A C 1 ATOM 114 O O . PHE A 1 17 ? -52.150 -10.327 43.813 1.00 21.23 ? 17 PHE A O 1 ATOM 115 C CB . PHE A 1 17 ? -53.181 -9.912 40.957 1.00 20.47 ? 17 PHE A CB 1 ATOM 116 C CG . PHE A 1 17 ? -53.959 -10.129 39.682 1.00 17.95 ? 17 PHE A CG 1 ATOM 117 C CD1 . PHE A 1 17 ? -53.323 -10.642 38.535 1.00 18.13 ? 17 PHE A CD1 1 ATOM 118 C CD2 . PHE A 1 17 ? -55.346 -9.897 39.645 1.00 16.45 ? 17 PHE A CD2 1 ATOM 119 C CE1 . PHE A 1 17 ? -54.061 -10.934 37.356 1.00 17.23 ? 17 PHE A CE1 1 ATOM 120 C CE2 . PHE A 1 17 ? -56.102 -10.181 38.479 1.00 17.84 ? 17 PHE A CE2 1 ATOM 121 C CZ . PHE A 1 17 ? -55.454 -10.706 37.328 1.00 18.10 ? 17 PHE A CZ 1 ATOM 122 N N . ASP A 1 18 ? -50.754 -11.716 42.707 1.00 20.98 ? 18 ASP A N 1 ATOM 123 C CA . ASP A 1 18 ? -49.650 -11.669 43.658 1.00 21.27 ? 18 ASP A CA 1 ATOM 124 C C . ASP A 1 18 ? -48.316 -11.870 42.935 1.00 20.42 ? 18 ASP A C 1 ATOM 125 O O . ASP A 1 18 ? -48.274 -11.901 41.709 1.00 21.10 ? 18 ASP A O 1 ATOM 126 C CB . ASP A 1 18 ? -49.844 -12.701 44.795 1.00 24.47 ? 18 ASP A CB 1 ATOM 127 C CG . ASP A 1 18 ? -50.116 -14.114 44.290 1.00 27.61 ? 18 ASP A CG 1 ATOM 128 O OD1 . ASP A 1 18 ? -49.189 -14.763 43.755 1.00 26.94 ? 18 ASP A OD1 1 ATOM 129 O OD2 . ASP A 1 18 ? -51.265 -14.579 44.444 1.00 30.86 ? 18 ASP A OD2 1 ATOM 130 N N . ILE A 1 19 ? -47.238 -12.015 43.702 1.00 19.49 ? 19 ILE A N 1 ATOM 131 C CA . ILE A 1 19 ? -45.887 -12.201 43.172 1.00 19.82 ? 19 ILE A CA 1 ATOM 132 C C . ILE A 1 19 ? -45.649 -13.509 42.404 1.00 21.48 ? 19 ILE A C 1 ATOM 133 O O . ILE A 1 19 ? -44.748 -13.588 41.566 1.00 22.77 ? 19 ILE A O 1 ATOM 134 C CB . ILE A 1 19 ? -44.834 -12.039 44.326 1.00 19.98 ? 19 ILE A CB 1 ATOM 135 C CG1 . ILE A 1 19 ? -43.426 -11.795 43.773 1.00 17.77 ? 19 ILE A CG1 1 ATOM 136 C CG2 . ILE A 1 19 ? -44.858 -13.240 45.282 1.00 18.76 ? 19 ILE A CG2 1 ATOM 137 C CD1 . ILE A 1 19 ? -43.312 -10.556 42.931 1.00 16.84 ? 19 ILE A CD1 1 ATOM 138 N N . ASN A 1 20 ? -46.480 -14.511 42.676 1.00 21.21 ? 20 ASN A N 1 ATOM 139 C CA . ASN A 1 20 ? -46.345 -15.821 42.054 1.00 20.29 ? 20 ASN A CA 1 ATOM 140 C C . ASN A 1 20 ? -47.146 -16.037 40.776 1.00 19.16 ? 20 ASN A C 1 ATOM 141 O O . ASN A 1 20 ? -46.875 -16.994 40.041 1.00 18.86 ? 20 ASN A O 1 ATOM 142 C CB . ASN A 1 20 ? -46.661 -16.915 43.072 1.00 21.22 ? 20 ASN A CB 1 ATOM 143 C CG . ASN A 1 20 ? -45.682 -16.945 44.222 1.00 22.54 ? 20 ASN A CG 1 ATOM 144 O OD1 . ASN A 1 20 ? -44.481 -17.152 44.031 1.00 24.75 ? 20 ASN A OD1 1 ATOM 145 N ND2 . ASN A 1 20 ? -46.189 -16.725 45.428 1.00 21.87 ? 20 ASN A ND2 1 ATOM 146 N N . THR A 1 21 ? -48.098 -15.140 40.504 1.00 16.41 ? 21 THR A N 1 ATOM 147 C CA . THR A 1 21 ? -48.941 -15.219 39.309 1.00 16.68 ? 21 THR A CA 1 ATOM 148 C C . THR A 1 21 ? -48.156 -14.876 38.045 1.00 16.56 ? 21 THR A C 1 ATOM 149 O O . THR A 1 21 ? -47.316 -13.972 38.055 1.00 17.58 ? 21 THR A O 1 ATOM 150 C CB . THR A 1 21 ? -50.145 -14.254 39.379 1.00 17.97 ? 21 THR A CB 1 ATOM 151 O OG1 . THR A 1 21 ? -49.688 -12.903 39.300 1.00 18.35 ? 21 THR A OG1 1 ATOM 152 C CG2 . THR A 1 21 ? -50.913 -14.441 40.668 1.00 18.81 ? 21 THR A CG2 1 ATOM 153 N N . ASP A 1 22 ? -48.442 -15.589 36.960 1.00 16.38 ? 22 ASP A N 1 ATOM 154 C CA . ASP A 1 22 ? -47.764 -15.346 35.693 1.00 16.42 ? 22 ASP A CA 1 ATOM 155 C C . ASP A 1 22 ? -48.279 -14.046 35.075 1.00 15.84 ? 22 ASP A C 1 ATOM 156 O O . ASP A 1 22 ? -49.379 -13.989 34.520 1.00 16.19 ? 22 ASP A O 1 ATOM 157 C CB . ASP A 1 22 ? -47.965 -16.526 34.744 1.00 16.83 ? 22 ASP A CB 1 ATOM 158 C CG . ASP A 1 22 ? -46.980 -16.531 33.578 1.00 17.88 ? 22 ASP A CG 1 ATOM 159 O OD1 . ASP A 1 22 ? -46.505 -15.455 33.156 1.00 18.89 ? 22 ASP A OD1 1 ATOM 160 O OD2 . ASP A 1 22 ? -46.694 -17.629 33.063 1.00 22.09 ? 22 ASP A OD2 1 ATOM 161 N N . TYR A 1 23 ? -47.459 -13.007 35.202 1.00 14.29 ? 23 TYR A N 1 ATOM 162 C CA . TYR A 1 23 ? -47.773 -11.679 34.686 1.00 13.84 ? 23 TYR A CA 1 ATOM 163 C C . TYR A 1 23 ? -47.765 -11.587 33.155 1.00 13.44 ? 23 TYR A C 1 ATOM 164 O O . TYR A 1 23 ? -48.362 -10.675 32.584 1.00 13.46 ? 23 TYR A O 1 ATOM 165 C CB . TYR A 1 23 ? -46.824 -10.634 35.297 1.00 11.52 ? 23 TYR A CB 1 ATOM 166 C CG . TYR A 1 23 ? -45.342 -10.958 35.187 1.00 10.71 ? 23 TYR A CG 1 ATOM 167 C CD1 . TYR A 1 23 ? -44.608 -10.612 34.034 1.00 8.12 ? 23 TYR A CD1 1 ATOM 168 C CD2 . TYR A 1 23 ? -44.665 -11.612 36.239 1.00 9.59 ? 23 TYR A CD2 1 ATOM 169 C CE1 . TYR A 1 23 ? -43.237 -10.910 33.923 1.00 8.59 ? 23 TYR A CE1 1 ATOM 170 C CE2 . TYR A 1 23 ? -43.284 -11.913 36.146 1.00 7.42 ? 23 TYR A CE2 1 ATOM 171 C CZ . TYR A 1 23 ? -42.584 -11.557 34.981 1.00 10.04 ? 23 TYR A CZ 1 ATOM 172 O OH . TYR A 1 23 ? -41.254 -11.830 34.865 1.00 8.46 ? 23 TYR A OH 1 ATOM 173 N N . GLU A 1 24 ? -47.091 -12.538 32.509 1.00 13.91 ? 24 GLU A N 1 ATOM 174 C CA . GLU A 1 24 ? -46.983 -12.570 31.049 1.00 16.42 ? 24 GLU A CA 1 ATOM 175 C C . GLU A 1 24 ? -48.245 -13.041 30.326 1.00 15.82 ? 24 GLU A C 1 ATOM 176 O O . GLU A 1 24 ? -48.359 -12.886 29.111 1.00 16.34 ? 24 GLU A O 1 ATOM 177 C CB . GLU A 1 24 ? -45.761 -13.401 30.611 1.00 17.30 ? 24 GLU A CB 1 ATOM 178 C CG . GLU A 1 24 ? -44.443 -12.636 30.710 1.00 20.04 ? 24 GLU A CG 1 ATOM 179 C CD . GLU A 1 24 ? -43.234 -13.364 30.129 1.00 23.16 ? 24 GLU A CD 1 ATOM 180 O OE1 . GLU A 1 24 ? -43.311 -14.580 29.859 1.00 27.22 ? 24 GLU A OE1 1 ATOM 181 O OE2 . GLU A 1 24 ? -42.185 -12.708 29.946 1.00 23.35 ? 24 GLU A OE2 1 ATOM 182 N N . VAL A 1 25 ? -49.185 -13.613 31.078 1.00 16.71 ? 25 VAL A N 1 ATOM 183 C CA . VAL A 1 25 ? -50.440 -14.119 30.518 1.00 17.69 ? 25 VAL A CA 1 ATOM 184 C C . VAL A 1 25 ? -51.709 -13.734 31.317 1.00 17.95 ? 25 VAL A C 1 ATOM 185 O O . VAL A 1 25 ? -52.829 -13.988 30.864 1.00 16.49 ? 25 VAL A O 1 ATOM 186 C CB . VAL A 1 25 ? -50.397 -15.685 30.321 1.00 18.69 ? 25 VAL A CB 1 ATOM 187 C CG1 . VAL A 1 25 ? -49.424 -16.099 29.218 1.00 18.15 ? 25 VAL A CG1 1 ATOM 188 C CG2 . VAL A 1 25 ? -50.066 -16.393 31.620 1.00 16.53 ? 25 VAL A CG2 1 ATOM 189 N N . SER A 1 26 ? -51.521 -13.141 32.502 1.00 18.49 ? 26 SER A N 1 ATOM 190 C CA . SER A 1 26 ? -52.625 -12.716 33.384 1.00 16.94 ? 26 SER A CA 1 ATOM 191 C C . SER A 1 26 ? -52.395 -11.260 33.821 1.00 15.33 ? 26 SER A C 1 ATOM 192 O O . SER A 1 26 ? -51.344 -10.940 34.366 1.00 14.69 ? 26 SER A O 1 ATOM 193 C CB . SER A 1 26 ? -52.711 -13.647 34.600 1.00 16.65 ? 26 SER A CB 1 ATOM 194 O OG . SER A 1 26 ? -53.989 -13.585 35.200 1.00 20.82 ? 26 SER A OG 1 ATOM 195 N N . THR A 1 27 ? -53.403 -10.403 33.628 1.00 14.65 ? 27 THR A N 1 ATOM 196 C CA . THR A 1 27 ? -53.302 -8.966 33.923 1.00 13.48 ? 27 THR A CA 1 ATOM 197 C C . THR A 1 27 ? -54.569 -8.398 34.590 1.00 14.22 ? 27 THR A C 1 ATOM 198 O O . THR A 1 27 ? -55.682 -8.723 34.162 1.00 13.93 ? 27 THR A O 1 ATOM 199 C CB . THR A 1 27 ? -53.036 -8.171 32.575 1.00 13.07 ? 27 THR A CB 1 ATOM 200 O OG1 . THR A 1 27 ? -51.888 -8.712 31.905 1.00 13.66 ? 27 THR A OG1 1 ATOM 201 C CG2 . THR A 1 27 ? -52.787 -6.694 32.819 1.00 10.09 ? 27 THR A CG2 1 ATOM 202 N N . PRO A 1 28 ? -54.418 -7.552 35.652 1.00 16.34 ? 28 PRO A N 1 ATOM 203 C CA . PRO A 1 28 ? -55.567 -6.948 36.353 1.00 18.80 ? 28 PRO A CA 1 ATOM 204 C C . PRO A 1 28 ? -56.352 -5.960 35.499 1.00 20.76 ? 28 PRO A C 1 ATOM 205 O O . PRO A 1 28 ? -55.775 -5.215 34.703 1.00 20.66 ? 28 PRO A O 1 ATOM 206 C CB . PRO A 1 28 ? -54.918 -6.210 37.529 1.00 17.37 ? 28 PRO A CB 1 ATOM 207 C CG . PRO A 1 28 ? -53.724 -6.977 37.800 1.00 15.96 ? 28 PRO A CG 1 ATOM 208 C CD . PRO A 1 28 ? -53.190 -7.311 36.435 1.00 15.75 ? 28 PRO A CD 1 ATOM 209 N N . ASP A 1 29 ? -57.669 -5.975 35.669 1.00 21.77 ? 29 ASP A N 1 ATOM 210 C CA . ASP A 1 29 ? -58.549 -5.078 34.940 1.00 23.34 ? 29 ASP A CA 1 ATOM 211 C C . ASP A 1 29 ? -58.971 -3.954 35.901 1.00 22.01 ? 29 ASP A C 1 ATOM 212 O O . ASP A 1 29 ? -59.966 -4.061 36.625 1.00 21.65 ? 29 ASP A O 1 ATOM 213 C CB . ASP A 1 29 ? -59.745 -5.869 34.379 1.00 26.03 ? 29 ASP A CB 1 ATOM 214 C CG . ASP A 1 29 ? -60.713 -5.008 33.594 1.00 28.42 ? 29 ASP A CG 1 ATOM 215 O OD1 . ASP A 1 29 ? -60.279 -4.010 32.975 1.00 31.01 ? 29 ASP A OD1 1 ATOM 216 O OD2 . ASP A 1 29 ? -61.918 -5.329 33.616 1.00 31.33 ? 29 ASP A OD2 1 ATOM 217 N N . THR A 1 30 ? -58.166 -2.898 35.918 1.00 20.32 ? 30 THR A N 1 ATOM 218 C CA . THR A 1 30 ? -58.404 -1.741 36.770 1.00 20.82 ? 30 THR A CA 1 ATOM 219 C C . THR A 1 30 ? -59.339 -0.732 36.104 1.00 20.17 ? 30 THR A C 1 ATOM 220 O O . THR A 1 30 ? -60.106 -0.050 36.785 1.00 20.12 ? 30 THR A O 1 ATOM 221 C CB . THR A 1 30 ? -57.074 -1.018 37.128 1.00 22.56 ? 30 THR A CB 1 ATOM 222 O OG1 . THR A 1 30 ? -56.517 -0.410 35.952 1.00 22.22 ? 30 THR A OG1 1 ATOM 223 C CG2 . THR A 1 30 ? -56.051 -1.999 37.715 1.00 22.86 ? 30 THR A CG2 1 ATOM 224 N N . GLY A 1 31 ? -59.230 -0.628 34.773 1.00 20.86 ? 31 GLY A N 1 ATOM 225 C CA . GLY A 1 31 ? -60.026 0.301 33.978 1.00 18.23 ? 31 GLY A CA 1 ATOM 226 C C . GLY A 1 31 ? -59.545 1.746 34.077 1.00 18.91 ? 31 GLY A C 1 ATOM 227 O O . GLY A 1 31 ? -60.217 2.660 33.592 1.00 19.77 ? 31 GLY A O 1 ATOM 228 N N . VAL A 1 32 ? -58.380 1.936 34.705 1.00 17.85 ? 32 VAL A N 1 ATOM 229 C CA . VAL A 1 32 ? -57.756 3.248 34.935 1.00 16.38 ? 32 VAL A CA 1 ATOM 230 C C . VAL A 1 32 ? -56.681 3.569 33.888 1.00 16.95 ? 32 VAL A C 1 ATOM 231 O O . VAL A 1 32 ? -55.954 2.683 33.417 1.00 17.29 ? 32 VAL A O 1 ATOM 232 C CB . VAL A 1 32 ? -57.120 3.315 36.386 1.00 14.66 ? 32 VAL A CB 1 ATOM 233 C CG1 . VAL A 1 32 ? -56.503 4.688 36.686 1.00 12.82 ? 32 VAL A CG1 1 ATOM 234 C CG2 . VAL A 1 32 ? -58.165 2.978 37.447 1.00 13.18 ? 32 VAL A CG2 1 ATOM 235 N N . THR A 1 33 ? -56.575 4.851 33.553 1.00 17.41 ? 33 THR A N 1 ATOM 236 C CA . THR A 1 33 ? -55.592 5.315 32.590 1.00 18.72 ? 33 THR A CA 1 ATOM 237 C C . THR A 1 33 ? -54.773 6.481 33.149 1.00 19.78 ? 33 THR A C 1 ATOM 238 O O . THR A 1 33 ? -55.304 7.347 33.844 1.00 20.10 ? 33 THR A O 1 ATOM 239 C CB . THR A 1 33 ? -56.266 5.669 31.224 1.00 17.61 ? 33 THR A CB 1 ATOM 240 O OG1 . THR A 1 33 ? -56.782 4.467 30.635 1.00 16.95 ? 33 THR A OG1 1 ATOM 241 C CG2 . THR A 1 33 ? -55.277 6.316 30.244 1.00 16.15 ? 33 THR A CG2 1 ATOM 242 N N . GLN A 1 34 ? -53.463 6.426 32.906 1.00 20.98 ? 34 GLN A N 1 ATOM 243 C CA . GLN A 1 34 ? -52.523 7.469 33.324 1.00 22.96 ? 34 GLN A CA 1 ATOM 244 C C . GLN A 1 34 ? -52.014 8.205 32.086 1.00 22.26 ? 34 GLN A C 1 ATOM 245 O O . GLN A 1 34 ? -51.317 7.629 31.244 1.00 22.05 ? 34 GLN A O 1 ATOM 246 C CB . GLN A 1 34 ? -51.354 6.874 34.118 1.00 24.81 ? 34 GLN A CB 1 ATOM 247 C CG . GLN A 1 34 ? -51.735 6.306 35.488 1.00 27.00 ? 34 GLN A CG 1 ATOM 248 C CD . GLN A 1 34 ? -52.197 7.358 36.475 1.00 27.75 ? 34 GLN A CD 1 ATOM 249 O OE1 . GLN A 1 34 ? -51.734 8.500 36.454 1.00 29.81 ? 34 GLN A OE1 1 ATOM 250 N NE2 . GLN A 1 34 ? -53.116 6.974 37.351 1.00 30.22 ? 34 GLN A NE2 1 ATOM 251 N N . SER A 1 35 ? -52.387 9.479 31.988 1.00 22.69 ? 35 SER A N 1 ATOM 252 C CA . SER A 1 35 ? -52.035 10.324 30.857 1.00 22.43 ? 35 SER A CA 1 ATOM 253 C C . SER A 1 35 ? -50.901 11.304 31.086 1.00 22.64 ? 35 SER A C 1 ATOM 254 O O . SER A 1 35 ? -50.730 11.833 32.193 1.00 24.65 ? 35 SER A O 1 ATOM 255 C CB . SER A 1 35 ? -53.273 11.056 30.370 1.00 23.40 ? 35 SER A CB 1 ATOM 256 O OG . SER A 1 35 ? -54.220 10.133 29.864 1.00 27.57 ? 35 SER A OG 1 ATOM 257 N N . TYR A 1 36 ? -50.084 11.474 30.043 1.00 20.01 ? 36 TYR A N 1 ATOM 258 C CA . TYR A 1 36 ? -48.917 12.365 30.042 1.00 19.66 ? 36 TYR A CA 1 ATOM 259 C C . TYR A 1 36 ? -48.737 13.008 28.662 1.00 19.94 ? 36 TYR A C 1 ATOM 260 O O . TYR A 1 36 ? -49.046 12.396 27.643 1.00 19.41 ? 36 TYR A O 1 ATOM 261 C CB . TYR A 1 36 ? -47.625 11.588 30.382 1.00 19.74 ? 36 TYR A CB 1 ATOM 262 C CG . TYR A 1 36 ? -47.591 10.950 31.751 1.00 19.20 ? 36 TYR A CG 1 ATOM 263 C CD1 . TYR A 1 36 ? -48.046 9.627 31.942 1.00 19.41 ? 36 TYR A CD1 1 ATOM 264 C CD2 . TYR A 1 36 ? -47.198 11.693 32.886 1.00 19.39 ? 36 TYR A CD2 1 ATOM 265 C CE1 . TYR A 1 36 ? -48.128 9.058 33.243 1.00 18.88 ? 36 TYR A CE1 1 ATOM 266 C CE2 . TYR A 1 36 ? -47.269 11.132 34.195 1.00 19.10 ? 36 TYR A CE2 1 ATOM 267 C CZ . TYR A 1 36 ? -47.739 9.817 34.359 1.00 19.36 ? 36 TYR A CZ 1 ATOM 268 O OH . TYR A 1 36 ? -47.826 9.268 35.621 1.00 20.65 ? 36 TYR A OH 1 ATOM 269 N N . VAL A 1 37 ? -48.274 14.257 28.641 1.00 19.90 ? 37 VAL A N 1 ATOM 270 C CA . VAL A 1 37 ? -48.013 14.980 27.398 1.00 20.08 ? 37 VAL A CA 1 ATOM 271 C C . VAL A 1 37 ? -46.531 15.319 27.403 1.00 19.49 ? 37 VAL A C 1 ATOM 272 O O . VAL A 1 37 ? -46.030 15.932 28.343 1.00 21.09 ? 37 VAL A O 1 ATOM 273 C CB . VAL A 1 37 ? -48.887 16.275 27.260 1.00 21.35 ? 37 VAL A CB 1 ATOM 274 C CG1 . VAL A 1 37 ? -48.446 17.123 26.064 1.00 22.24 ? 37 VAL A CG1 1 ATOM 275 C CG2 . VAL A 1 37 ? -50.353 15.902 27.067 1.00 21.16 ? 37 VAL A CG2 1 ATOM 276 N N . PHE A 1 38 ? -45.831 14.853 26.371 1.00 20.09 ? 38 PHE A N 1 ATOM 277 C CA . PHE A 1 38 ? -44.391 15.072 26.209 1.00 17.50 ? 38 PHE A CA 1 ATOM 278 C C . PHE A 1 38 ? -44.117 16.150 25.176 1.00 17.81 ? 38 PHE A C 1 ATOM 279 O O . PHE A 1 38 ? -44.335 15.939 23.981 1.00 16.97 ? 38 PHE A O 1 ATOM 280 C CB . PHE A 1 38 ? -43.683 13.786 25.752 1.00 16.66 ? 38 PHE A CB 1 ATOM 281 C CG . PHE A 1 38 ? -43.556 12.709 26.804 1.00 15.03 ? 38 PHE A CG 1 ATOM 282 C CD1 . PHE A 1 38 ? -44.152 12.818 28.086 1.00 16.85 ? 38 PHE A CD1 1 ATOM 283 C CD2 . PHE A 1 38 ? -42.838 11.545 26.495 1.00 14.76 ? 38 PHE A CD2 1 ATOM 284 C CE1 . PHE A 1 38 ? -44.035 11.777 29.038 1.00 14.25 ? 38 PHE A CE1 1 ATOM 285 C CE2 . PHE A 1 38 ? -42.712 10.503 27.428 1.00 12.68 ? 38 PHE A CE2 1 ATOM 286 C CZ . PHE A 1 38 ? -43.316 10.619 28.710 1.00 13.61 ? 38 PHE A CZ 1 ATOM 287 N N . ASN A 1 39 ? -43.621 17.292 25.643 1.00 17.99 ? 39 ASN A N 1 ATOM 288 C CA . ASN A 1 39 ? -43.298 18.415 24.776 1.00 18.19 ? 39 ASN A CA 1 ATOM 289 C C . ASN A 1 39 ? -41.786 18.444 24.586 1.00 18.34 ? 39 ASN A C 1 ATOM 290 O O . ASN A 1 39 ? -41.034 18.823 25.488 1.00 16.47 ? 39 ASN A O 1 ATOM 291 C CB . ASN A 1 39 ? -43.809 19.729 25.394 1.00 19.97 ? 39 ASN A CB 1 ATOM 292 C CG . ASN A 1 39 ? -43.776 20.908 24.423 1.00 22.18 ? 39 ASN A CG 1 ATOM 293 O OD1 . ASN A 1 39 ? -43.395 20.774 23.253 1.00 21.17 ? 39 ASN A OD1 1 ATOM 294 N ND2 . ASN A 1 39 ? -44.205 22.065 24.925 1.00 24.44 ? 39 ASN A ND2 1 ATOM 295 N N . LEU A 1 40 ? -41.354 18.051 23.391 1.00 19.27 ? 40 LEU A N 1 ATOM 296 C CA . LEU A 1 40 ? -39.937 18.019 23.071 1.00 20.67 ? 40 LEU A CA 1 ATOM 297 C C . LEU A 1 40 ? -39.464 19.342 22.508 1.00 20.69 ? 40 LEU A C 1 ATOM 298 O O . LEU A 1 40 ? -39.819 19.702 21.390 1.00 22.36 ? 40 LEU A O 1 ATOM 299 C CB . LEU A 1 40 ? -39.608 16.914 22.059 1.00 22.67 ? 40 LEU A CB 1 ATOM 300 C CG . LEU A 1 40 ? -40.055 15.452 22.105 1.00 21.14 ? 40 LEU A CG 1 ATOM 301 C CD1 . LEU A 1 40 ? -38.972 14.660 21.419 1.00 21.78 ? 40 LEU A CD1 1 ATOM 302 C CD2 . LEU A 1 40 ? -40.253 14.934 23.499 1.00 21.21 ? 40 LEU A CD2 1 ATOM 303 N N . THR A 1 41 ? -38.693 20.077 23.298 1.00 19.25 ? 41 THR A N 1 ATOM 304 C CA . THR A 1 41 ? -38.133 21.352 22.859 1.00 18.96 ? 41 THR A CA 1 ATOM 305 C C . THR A 1 41 ? -36.629 21.184 22.709 1.00 17.85 ? 41 THR A C 1 ATOM 306 O O . THR A 1 41 ? -36.034 20.299 23.332 1.00 15.40 ? 41 THR A O 1 ATOM 307 C CB . THR A 1 41 ? -38.403 22.499 23.856 1.00 18.34 ? 41 THR A CB 1 ATOM 308 O OG1 . THR A 1 41 ? -38.020 22.091 25.174 1.00 21.13 ? 41 THR A OG1 1 ATOM 309 C CG2 . THR A 1 41 ? -39.871 22.899 23.841 1.00 20.12 ? 41 THR A CG2 1 ATOM 310 N N . GLU A 1 42 ? -36.048 21.986 21.819 1.00 17.47 ? 42 GLU A N 1 ATOM 311 C CA . GLU A 1 42 ? -34.615 21.984 21.556 1.00 17.51 ? 42 GLU A CA 1 ATOM 312 C C . GLU A 1 42 ? -34.066 23.239 22.226 1.00 17.42 ? 42 GLU A C 1 ATOM 313 O O . GLU A 1 42 ? -34.467 24.362 21.898 1.00 19.14 ? 42 GLU A O 1 ATOM 314 C CB . GLU A 1 42 ? -34.367 22.013 20.047 1.00 19.50 ? 42 GLU A CB 1 ATOM 315 C CG . GLU A 1 42 ? -33.026 21.456 19.605 1.00 21.49 ? 42 GLU A CG 1 ATOM 316 C CD . GLU A 1 42 ? -32.965 21.210 18.105 1.00 23.54 ? 42 GLU A CD 1 ATOM 317 O OE1 . GLU A 1 42 ? -33.918 20.620 17.546 1.00 23.40 ? 42 GLU A OE1 1 ATOM 318 O OE2 . GLU A 1 42 ? -31.963 21.608 17.478 1.00 24.37 ? 42 GLU A OE2 1 ATOM 319 N N . VAL A 1 43 ? -33.204 23.042 23.217 1.00 17.69 ? 43 VAL A N 1 ATOM 320 C CA . VAL A 1 43 ? -32.633 24.166 23.950 1.00 17.77 ? 43 VAL A CA 1 ATOM 321 C C . VAL A 1 43 ? -31.143 24.350 23.672 1.00 17.46 ? 43 VAL A C 1 ATOM 322 O O . VAL A 1 43 ? -30.345 23.442 23.890 1.00 19.36 ? 43 VAL A O 1 ATOM 323 C CB . VAL A 1 43 ? -32.888 24.056 25.490 1.00 16.51 ? 43 VAL A CB 1 ATOM 324 C CG1 . VAL A 1 43 ? -32.628 25.398 26.170 1.00 17.02 ? 43 VAL A CG1 1 ATOM 325 C CG2 . VAL A 1 43 ? -34.314 23.592 25.785 1.00 14.99 ? 43 VAL A CG2 1 ATOM 326 N N . ASP A 1 44 ? -30.796 25.528 23.152 1.00 18.12 ? 44 ASP A N 1 ATOM 327 C CA . ASP A 1 44 ? -29.412 25.885 22.856 1.00 19.04 ? 44 ASP A CA 1 ATOM 328 C C . ASP A 1 44 ? -28.822 26.577 24.084 1.00 19.37 ? 44 ASP A C 1 ATOM 329 O O . ASP A 1 44 ? -29.540 27.269 24.821 1.00 19.61 ? 44 ASP A O 1 ATOM 330 C CB . ASP A 1 44 ? -29.321 26.826 21.641 1.00 19.29 ? 44 ASP A CB 1 ATOM 331 C CG . ASP A 1 44 ? -29.801 26.172 20.343 1.00 21.17 ? 44 ASP A CG 1 ATOM 332 O OD1 . ASP A 1 44 ? -29.235 25.136 19.936 1.00 22.34 ? 44 ASP A OD1 1 ATOM 333 O OD2 . ASP A 1 44 ? -30.747 26.700 19.722 1.00 20.23 ? 44 ASP A OD2 1 ATOM 334 N N . ASN A 1 45 ? -27.526 26.351 24.312 1.00 18.04 ? 45 ASN A N 1 ATOM 335 C CA . ASN A 1 45 ? -26.750 26.933 25.424 1.00 19.16 ? 45 ASN A CA 1 ATOM 336 C C . ASN A 1 45 ? -27.430 26.761 26.786 1.00 18.92 ? 45 ASN A C 1 ATOM 337 O O . ASN A 1 45 ? -27.690 27.719 27.520 1.00 19.16 ? 45 ASN A O 1 ATOM 338 C CB . ASN A 1 45 ? -26.400 28.400 25.127 1.00 17.35 ? 45 ASN A CB 1 ATOM 339 C CG . ASN A 1 45 ? -25.862 28.592 23.718 1.00 17.43 ? 45 ASN A CG 1 ATOM 340 O OD1 . ASN A 1 45 ? -24.724 28.237 23.419 1.00 18.15 ? 45 ASN A OD1 1 ATOM 341 N ND2 . ASN A 1 45 ? -26.691 29.139 22.841 1.00 17.90 ? 45 ASN A ND2 1 ATOM 342 N N . TRP A 1 46 ? -27.712 25.501 27.091 1.00 18.62 ? 46 TRP A N 1 ATOM 343 C CA . TRP A 1 46 ? -28.393 25.103 28.306 1.00 19.92 ? 46 TRP A CA 1 ATOM 344 C C . TRP A 1 46 ? -27.452 24.894 29.484 1.00 20.14 ? 46 TRP A C 1 ATOM 345 O O . TRP A 1 46 ? -26.383 24.308 29.339 1.00 21.31 ? 46 TRP A O 1 ATOM 346 C CB . TRP A 1 46 ? -29.202 23.832 28.012 1.00 19.93 ? 46 TRP A CB 1 ATOM 347 C CG . TRP A 1 46 ? -30.007 23.280 29.157 1.00 20.77 ? 46 TRP A CG 1 ATOM 348 C CD1 . TRP A 1 46 ? -31.132 23.827 29.719 1.00 20.89 ? 46 TRP A CD1 1 ATOM 349 C CD2 . TRP A 1 46 ? -29.729 22.086 29.893 1.00 20.95 ? 46 TRP A CD2 1 ATOM 350 N NE1 . TRP A 1 46 ? -31.569 23.045 30.766 1.00 21.73 ? 46 TRP A NE1 1 ATOM 351 C CE2 . TRP A 1 46 ? -30.731 21.971 30.898 1.00 20.36 ? 46 TRP A CE2 1 ATOM 352 C CE3 . TRP A 1 46 ? -28.727 21.094 29.808 1.00 21.69 ? 46 TRP A CE3 1 ATOM 353 C CZ2 . TRP A 1 46 ? -30.761 20.901 31.816 1.00 19.87 ? 46 TRP A CZ2 1 ATOM 354 C CZ3 . TRP A 1 46 ? -28.753 20.020 30.725 1.00 21.11 ? 46 TRP A CZ3 1 ATOM 355 C CH2 . TRP A 1 46 ? -29.771 19.940 31.717 1.00 19.45 ? 46 TRP A CH2 1 ATOM 356 N N . MET A 1 47 ? -27.894 25.344 30.656 1.00 21.62 ? 47 MET A N 1 ATOM 357 C CA . MET A 1 47 ? -27.127 25.203 31.890 1.00 23.63 ? 47 MET A CA 1 ATOM 358 C C . MET A 1 47 ? -27.322 23.814 32.504 1.00 23.75 ? 47 MET A C 1 ATOM 359 O O . MET A 1 47 ? -28.417 23.463 32.964 1.00 22.43 ? 47 MET A O 1 ATOM 360 C CB . MET A 1 47 ? -27.489 26.310 32.893 1.00 23.38 ? 47 MET A CB 1 ATOM 361 C CG . MET A 1 47 ? -26.702 26.260 34.205 1.00 26.70 ? 47 MET A CG 1 ATOM 362 S SD . MET A 1 47 ? -24.924 25.996 33.990 1.00 28.61 ? 47 MET A SD 1 ATOM 363 C CE . MET A 1 47 ? -24.318 27.687 34.041 1.00 28.94 ? 47 MET A CE 1 ATOM 364 N N . GLY A 1 48 ? -26.233 23.044 32.489 1.00 25.38 ? 48 GLY A N 1 ATOM 365 C CA . GLY A 1 48 ? -26.220 21.693 33.027 1.00 25.65 ? 48 GLY A CA 1 ATOM 366 C C . GLY A 1 48 ? -26.100 21.577 34.543 1.00 26.54 ? 48 GLY A C 1 ATOM 367 O O . GLY A 1 48 ? -25.681 22.535 35.203 1.00 26.61 ? 48 GLY A O 1 ATOM 368 N N . PRO A 1 49 ? -26.438 20.405 35.123 1.00 27.48 ? 49 PRO A N 1 ATOM 369 C CA . PRO A 1 49 ? -26.385 20.128 36.565 1.00 28.24 ? 49 PRO A CA 1 ATOM 370 C C . PRO A 1 49 ? -25.022 20.306 37.242 1.00 29.40 ? 49 PRO A C 1 ATOM 371 O O . PRO A 1 49 ? -24.960 20.580 38.450 1.00 30.27 ? 49 PRO A O 1 ATOM 372 C CB . PRO A 1 49 ? -26.851 18.680 36.639 1.00 27.96 ? 49 PRO A CB 1 ATOM 373 C CG . PRO A 1 49 ? -27.802 18.579 35.490 1.00 28.64 ? 49 PRO A CG 1 ATOM 374 C CD . PRO A 1 49 ? -27.019 19.248 34.412 1.00 28.31 ? 49 PRO A CD 1 ATOM 375 N N . ASP A 1 50 ? -23.947 20.152 36.464 1.00 28.65 ? 50 ASP A N 1 ATOM 376 C CA . ASP A 1 50 ? -22.583 20.295 36.978 1.00 28.26 ? 50 ASP A CA 1 ATOM 377 C C . ASP A 1 50 ? -21.971 21.685 36.738 1.00 28.42 ? 50 ASP A C 1 ATOM 378 O O . ASP A 1 50 ? -20.785 21.906 37.008 1.00 29.11 ? 50 ASP A O 1 ATOM 379 C CB . ASP A 1 50 ? -21.676 19.173 36.435 1.00 27.77 ? 50 ASP A CB 1 ATOM 380 C CG . ASP A 1 50 ? -21.427 19.263 34.925 1.00 28.42 ? 50 ASP A CG 1 ATOM 381 O OD1 . ASP A 1 50 ? -22.244 19.861 34.194 1.00 26.68 ? 50 ASP A OD1 1 ATOM 382 O OD2 . ASP A 1 50 ? -20.399 18.719 34.475 1.00 27.11 ? 50 ASP A OD2 1 ATOM 383 N N . GLY A 1 51 ? -22.782 22.601 36.210 1.00 26.63 ? 51 GLY A N 1 ATOM 384 C CA . GLY A 1 51 ? -22.323 23.959 35.957 1.00 26.54 ? 51 GLY A CA 1 ATOM 385 C C . GLY A 1 51 ? -21.890 24.266 34.532 1.00 26.39 ? 51 GLY A C 1 ATOM 386 O O . GLY A 1 51 ? -21.882 25.434 34.121 1.00 25.50 ? 51 GLY A O 1 ATOM 387 N N . VAL A 1 52 ? -21.533 23.229 33.775 1.00 23.96 ? 52 VAL A N 1 ATOM 388 C CA . VAL A 1 52 ? -21.101 23.404 32.392 1.00 22.83 ? 52 VAL A CA 1 ATOM 389 C C . VAL A 1 52 ? -22.285 23.672 31.461 1.00 20.89 ? 52 VAL A C 1 ATOM 390 O O . VAL A 1 52 ? -23.357 23.087 31.603 1.00 19.20 ? 52 VAL A O 1 ATOM 391 C CB . VAL A 1 52 ? -20.243 22.197 31.921 1.00 22.83 ? 52 VAL A CB 1 ATOM 392 C CG1 . VAL A 1 52 ? -19.880 22.295 30.429 1.00 24.05 ? 52 VAL A CG1 1 ATOM 393 C CG2 . VAL A 1 52 ? -18.964 22.143 32.737 1.00 24.10 ? 52 VAL A CG2 1 ATOM 394 N N . VAL A 1 53 ? -22.083 24.631 30.566 1.00 19.63 ? 53 VAL A N 1 ATOM 395 C CA . VAL A 1 53 ? -23.088 25.024 29.590 1.00 20.38 ? 53 VAL A CA 1 ATOM 396 C C . VAL A 1 53 ? -22.921 24.152 28.339 1.00 19.68 ? 53 VAL A C 1 ATOM 397 O O . VAL A 1 53 ? -21.849 24.133 27.724 1.00 19.57 ? 53 VAL A O 1 ATOM 398 C CB . VAL A 1 53 ? -22.962 26.537 29.230 1.00 21.52 ? 53 VAL A CB 1 ATOM 399 C CG1 . VAL A 1 53 ? -24.099 26.978 28.344 1.00 19.97 ? 53 VAL A CG1 1 ATOM 400 C CG2 . VAL A 1 53 ? -22.953 27.393 30.498 1.00 21.25 ? 53 VAL A CG2 1 ATOM 401 N N . LYS A 1 54 ? -23.978 23.408 28.008 1.00 17.84 ? 54 LYS A N 1 ATOM 402 C CA . LYS A 1 54 ? -23.995 22.527 26.839 1.00 17.05 ? 54 LYS A CA 1 ATOM 403 C C . LYS A 1 54 ? -24.522 23.236 25.602 1.00 15.84 ? 54 LYS A C 1 ATOM 404 O O . LYS A 1 54 ? -25.548 23.923 25.675 1.00 15.29 ? 54 LYS A O 1 ATOM 405 C CB . LYS A 1 54 ? -24.867 21.298 27.099 1.00 19.57 ? 54 LYS A CB 1 ATOM 406 C CG . LYS A 1 54 ? -24.194 20.188 27.888 1.00 20.37 ? 54 LYS A CG 1 ATOM 407 C CD . LYS A 1 54 ? -24.997 18.896 27.856 1.00 20.96 ? 54 LYS A CD 1 ATOM 408 C CE . LYS A 1 54 ? -25.039 18.270 26.467 1.00 22.18 ? 54 LYS A CE 1 ATOM 409 N NZ . LYS A 1 54 ? -25.584 16.884 26.499 1.00 22.86 ? 54 LYS A NZ 1 ATOM 410 N N . GLU A 1 55 ? -23.860 22.998 24.463 1.00 12.80 ? 55 GLU A N 1 ATOM 411 C CA . GLU A 1 55 ? -24.220 23.582 23.165 1.00 10.53 ? 55 GLU A CA 1 ATOM 412 C C . GLU A 1 55 ? -25.701 23.417 22.805 1.00 10.11 ? 55 GLU A C 1 ATOM 413 O O . GLU A 1 55 ? -26.371 24.396 22.473 1.00 10.10 ? 55 GLU A O 1 ATOM 414 C CB . GLU A 1 55 ? -23.377 22.950 22.047 1.00 11.11 ? 55 GLU A CB 1 ATOM 415 C CG . GLU A 1 55 ? -23.672 23.507 20.649 1.00 13.10 ? 55 GLU A CG 1 ATOM 416 C CD . GLU A 1 55 ? -23.372 22.541 19.515 1.00 18.03 ? 55 GLU A CD 1 ATOM 417 O OE1 . GLU A 1 55 ? -22.877 21.421 19.766 1.00 22.86 ? 55 GLU A OE1 1 ATOM 418 O OE2 . GLU A 1 55 ? -23.634 22.908 18.351 1.00 17.82 ? 55 GLU A OE2 1 ATOM 419 N N . LYS A 1 56 ? -26.188 22.175 22.891 1.00 8.91 ? 56 LYS A N 1 ATOM 420 C CA . LYS A 1 56 ? -27.563 21.835 22.548 1.00 8.69 ? 56 LYS A CA 1 ATOM 421 C C . LYS A 1 56 ? -28.056 20.590 23.288 1.00 8.12 ? 56 LYS A C 1 ATOM 422 O O . LYS A 1 56 ? -27.292 19.666 23.560 1.00 8.96 ? 56 LYS A O 1 ATOM 423 C CB . LYS A 1 56 ? -27.658 21.599 21.021 1.00 9.30 ? 56 LYS A CB 1 ATOM 424 C CG . LYS A 1 56 ? -29.059 21.312 20.457 1.00 8.50 ? 56 LYS A CG 1 ATOM 425 C CD . LYS A 1 56 ? -29.009 20.898 18.973 1.00 9.03 ? 56 LYS A CD 1 ATOM 426 C CE . LYS A 1 56 ? -28.690 22.067 18.035 1.00 7.39 ? 56 LYS A CE 1 ATOM 427 N NZ . LYS A 1 56 ? -29.740 23.130 18.084 1.00 8.44 ? 56 LYS A NZ 1 ATOM 428 N N . VAL A 1 57 ? -29.336 20.602 23.649 1.00 6.16 ? 57 VAL A N 1 ATOM 429 C CA . VAL A 1 57 ? -29.992 19.478 24.306 1.00 4.90 ? 57 VAL A CA 1 ATOM 430 C C . VAL A 1 57 ? -31.431 19.407 23.770 1.00 6.19 ? 57 VAL A C 1 ATOM 431 O O . VAL A 1 57 ? -31.976 20.409 23.292 1.00 4.35 ? 57 VAL A O 1 ATOM 432 C CB . VAL A 1 57 ? -30.036 19.604 25.880 1.00 5.32 ? 57 VAL A CB 1 ATOM 433 C CG1 . VAL A 1 57 ? -28.662 19.417 26.507 1.00 3.77 ? 57 VAL A CG1 1 ATOM 434 C CG2 . VAL A 1 57 ? -30.617 20.915 26.298 1.00 1.85 ? 57 VAL A CG2 1 ATOM 435 N N . MET A 1 58 ? -32.025 18.215 23.829 1.00 7.67 ? 58 MET A N 1 ATOM 436 C CA . MET A 1 58 ? -33.408 17.988 23.395 1.00 8.54 ? 58 MET A CA 1 ATOM 437 C C . MET A 1 58 ? -34.098 17.480 24.643 1.00 9.42 ? 58 MET A C 1 ATOM 438 O O . MET A 1 58 ? -33.686 16.475 25.205 1.00 10.65 ? 58 MET A O 1 ATOM 439 C CB . MET A 1 58 ? -33.454 16.970 22.259 1.00 7.37 ? 58 MET A CB 1 ATOM 440 C CG . MET A 1 58 ? -32.862 17.513 20.970 1.00 9.25 ? 58 MET A CG 1 ATOM 441 S SD . MET A 1 58 ? -32.636 16.324 19.682 1.00 6.33 ? 58 MET A SD 1 ATOM 442 C CE . MET A 1 58 ? -31.454 17.194 18.672 1.00 8.39 ? 58 MET A CE 1 ATOM 443 N N . LEU A 1 59 ? -35.092 18.226 25.125 1.00 12.10 ? 59 LEU A N 1 ATOM 444 C CA . LEU A 1 59 ? -35.778 17.879 26.372 1.00 14.63 ? 59 LEU A CA 1 ATOM 445 C C . LEU A 1 59 ? -37.293 17.766 26.342 1.00 15.81 ? 59 LEU A C 1 ATOM 446 O O . LEU A 1 59 ? -37.977 18.487 25.624 1.00 17.42 ? 59 LEU A O 1 ATOM 447 C CB . LEU A 1 59 ? -35.423 18.890 27.470 1.00 15.27 ? 59 LEU A CB 1 ATOM 448 C CG . LEU A 1 59 ? -33.987 19.307 27.780 1.00 16.82 ? 59 LEU A CG 1 ATOM 449 C CD1 . LEU A 1 59 ? -33.999 20.470 28.744 1.00 14.51 ? 59 LEU A CD1 1 ATOM 450 C CD2 . LEU A 1 59 ? -33.179 18.126 28.314 1.00 18.20 ? 59 LEU A CD2 1 ATOM 451 N N . ILE A 1 60 ? -37.796 16.918 27.233 1.00 15.28 ? 60 ILE A N 1 ATOM 452 C CA . ILE A 1 60 ? -39.220 16.678 27.405 1.00 14.22 ? 60 ILE A CA 1 ATOM 453 C C . ILE A 1 60 ? -39.672 17.598 28.548 1.00 15.56 ? 60 ILE A C 1 ATOM 454 O O . ILE A 1 60 ? -39.178 17.466 29.680 1.00 16.60 ? 60 ILE A O 1 ATOM 455 C CB . ILE A 1 60 ? -39.477 15.214 27.812 1.00 13.46 ? 60 ILE A CB 1 ATOM 456 C CG1 . ILE A 1 60 ? -38.892 14.249 26.784 1.00 12.79 ? 60 ILE A CG1 1 ATOM 457 C CG2 . ILE A 1 60 ? -40.951 14.975 28.030 1.00 12.90 ? 60 ILE A CG2 1 ATOM 458 C CD1 . ILE A 1 60 ? -38.789 12.811 27.268 1.00 12.44 ? 60 ILE A CD1 1 ATOM 459 N N . ASN A 1 61 ? -40.599 18.516 28.240 1.00 14.95 ? 61 ASN A N 1 ATOM 460 C CA . ASN A 1 61 ? -41.161 19.492 29.189 1.00 16.32 ? 61 ASN A CA 1 ATOM 461 C C . ASN A 1 61 ? -40.133 20.387 29.917 1.00 16.86 ? 61 ASN A C 1 ATOM 462 O O . ASN A 1 61 ? -40.276 20.687 31.109 1.00 17.15 ? 61 ASN A O 1 ATOM 463 C CB . ASN A 1 61 ? -42.118 18.806 30.197 1.00 15.09 ? 61 ASN A CB 1 ATOM 464 C CG . ASN A 1 61 ? -43.307 18.127 29.521 1.00 18.40 ? 61 ASN A CG 1 ATOM 465 O OD1 . ASN A 1 61 ? -43.612 18.381 28.347 1.00 17.06 ? 61 ASN A OD1 1 ATOM 466 N ND2 . ASN A 1 61 ? -43.974 17.247 30.259 1.00 15.05 ? 61 ASN A ND2 1 ATOM 467 N N . GLY A 1 62 ? -39.073 20.753 29.196 1.00 17.18 ? 62 GLY A N 1 ATOM 468 C CA . GLY A 1 62 ? -38.025 21.621 29.728 1.00 19.48 ? 62 GLY A CA 1 ATOM 469 C C . GLY A 1 62 ? -37.143 21.159 30.885 1.00 19.31 ? 62 GLY A C 1 ATOM 470 O O . GLY A 1 62 ? -36.506 21.998 31.526 1.00 19.40 ? 62 GLY A O 1 ATOM 471 N N . ASN A 1 63 ? -37.107 19.855 31.163 1.00 18.56 ? 63 ASN A N 1 ATOM 472 C CA . ASN A 1 63 ? -36.277 19.313 32.250 1.00 20.00 ? 63 ASN A CA 1 ATOM 473 C C . ASN A 1 63 ? -35.213 18.311 31.769 1.00 19.79 ? 63 ASN A C 1 ATOM 474 O O . ASN A 1 63 ? -35.279 17.837 30.631 1.00 15.79 ? 63 ASN A O 1 ATOM 475 C CB . ASN A 1 63 ? -37.155 18.692 33.346 1.00 20.51 ? 63 ASN A CB 1 ATOM 476 C CG . ASN A 1 63 ? -38.080 19.707 33.999 1.00 20.43 ? 63 ASN A CG 1 ATOM 477 O OD1 . ASN A 1 63 ? -37.647 20.784 34.420 1.00 21.36 ? 63 ASN A OD1 1 ATOM 478 N ND2 . ASN A 1 63 ? -39.364 19.384 34.053 1.00 21.11 ? 63 ASN A ND2 1 ATOM 479 N N . ILE A 1 64 ? -34.248 18.001 32.646 1.00 19.20 ? 64 ILE A N 1 ATOM 480 C CA . ILE A 1 64 ? -33.127 17.073 32.380 1.00 21.11 ? 64 ILE A CA 1 ATOM 481 C C . ILE A 1 64 ? -33.616 15.706 31.862 1.00 21.73 ? 64 ILE A C 1 ATOM 482 O O . ILE A 1 64 ? -33.007 15.106 30.971 1.00 22.07 ? 64 ILE A O 1 ATOM 483 C CB . ILE A 1 64 ? -32.182 16.944 33.664 1.00 21.63 ? 64 ILE A CB 1 ATOM 484 C CG1 . ILE A 1 64 ? -31.006 15.974 33.441 1.00 24.00 ? 64 ILE A CG1 1 ATOM 485 C CG2 . ILE A 1 64 ? -32.974 16.530 34.900 1.00 22.56 ? 64 ILE A CG2 1 ATOM 486 C CD1 . ILE A 1 64 ? -29.936 16.448 32.480 1.00 22.45 ? 64 ILE A CD1 1 ATOM 487 N N . MET A 1 65 ? -34.708 15.233 32.453 1.00 20.95 ? 65 MET A N 1 ATOM 488 C CA . MET A 1 65 ? -35.366 13.990 32.068 1.00 22.62 ? 65 MET A CA 1 ATOM 489 C C . MET A 1 65 ? -36.851 14.329 31.947 1.00 20.96 ? 65 MET A C 1 ATOM 490 O O . MET A 1 65 ? -37.280 15.423 32.335 1.00 19.40 ? 65 MET A O 1 ATOM 491 C CB . MET A 1 65 ? -35.181 12.881 33.122 1.00 24.73 ? 65 MET A CB 1 ATOM 492 C CG . MET A 1 65 ? -33.756 12.373 33.292 1.00 28.24 ? 65 MET A CG 1 ATOM 493 S SD . MET A 1 65 ? -33.646 10.757 34.069 1.00 31.88 ? 65 MET A SD 1 ATOM 494 C CE . MET A 1 65 ? -32.374 9.986 33.037 1.00 29.78 ? 65 MET A CE 1 ATOM 495 N N . GLY A 1 66 ? -37.629 13.396 31.402 1.00 20.65 ? 66 GLY A N 1 ATOM 496 C CA . GLY A 1 66 ? -39.061 13.595 31.268 1.00 20.47 ? 66 GLY A CA 1 ATOM 497 C C . GLY A 1 66 ? -39.778 13.291 32.573 1.00 22.09 ? 66 GLY A C 1 ATOM 498 O O . GLY A 1 66 ? -39.113 12.902 33.545 1.00 22.30 ? 66 GLY A O 1 ATOM 499 N N . PRO A 1 67 ? -41.123 13.432 32.642 1.00 22.87 ? 67 PRO A N 1 ATOM 500 C CA . PRO A 1 67 ? -41.812 13.138 33.904 1.00 23.05 ? 67 PRO A CA 1 ATOM 501 C C . PRO A 1 67 ? -41.792 11.653 34.272 1.00 23.84 ? 67 PRO A C 1 ATOM 502 O O . PRO A 1 67 ? -41.674 10.784 33.401 1.00 23.44 ? 67 PRO A O 1 ATOM 503 C CB . PRO A 1 67 ? -43.226 13.668 33.658 1.00 23.38 ? 67 PRO A CB 1 ATOM 504 C CG . PRO A 1 67 ? -43.403 13.529 32.192 1.00 22.30 ? 67 PRO A CG 1 ATOM 505 C CD . PRO A 1 67 ? -42.072 13.944 31.633 1.00 22.64 ? 67 PRO A CD 1 ATOM 506 N N . ASN A 1 68 ? -41.836 11.380 35.571 1.00 24.79 ? 68 ASN A N 1 ATOM 507 C CA . ASN A 1 68 ? -41.825 10.009 36.064 1.00 25.65 ? 68 ASN A CA 1 ATOM 508 C C . ASN A 1 68 ? -43.208 9.388 35.876 1.00 24.38 ? 68 ASN A C 1 ATOM 509 O O . ASN A 1 68 ? -44.170 9.783 36.539 1.00 25.84 ? 68 ASN A O 1 ATOM 510 C CB . ASN A 1 68 ? -41.398 9.967 37.540 1.00 28.09 ? 68 ASN A CB 1 ATOM 511 C CG . ASN A 1 68 ? -40.025 10.593 37.775 1.00 31.59 ? 68 ASN A CG 1 ATOM 512 O OD1 . ASN A 1 68 ? -38.992 9.938 37.617 1.00 32.45 ? 68 ASN A OD1 1 ATOM 513 N ND2 . ASN A 1 68 ? -40.012 11.870 38.150 1.00 34.55 ? 68 ASN A ND2 1 ATOM 514 N N . ILE A 1 69 ? -43.310 8.480 34.905 1.00 22.12 ? 69 ILE A N 1 ATOM 515 C CA . ILE A 1 69 ? -44.557 7.778 34.612 1.00 19.97 ? 69 ILE A CA 1 ATOM 516 C C . ILE A 1 69 ? -44.816 6.784 35.730 1.00 17.74 ? 69 ILE A C 1 ATOM 517 O O . ILE A 1 69 ? -44.047 5.836 35.912 1.00 19.71 ? 69 ILE A O 1 ATOM 518 C CB . ILE A 1 69 ? -44.518 7.053 33.230 1.00 19.82 ? 69 ILE A CB 1 ATOM 519 C CG1 . ILE A 1 69 ? -44.561 8.086 32.104 1.00 18.61 ? 69 ILE A CG1 1 ATOM 520 C CG2 . ILE A 1 69 ? -45.684 6.061 33.089 1.00 20.60 ? 69 ILE A CG2 1 ATOM 521 C CD1 . ILE A 1 69 ? -44.483 7.499 30.721 1.00 17.47 ? 69 ILE A CD1 1 ATOM 522 N N . VAL A 1 70 ? -45.842 7.072 36.526 1.00 14.16 ? 70 VAL A N 1 ATOM 523 C CA . VAL A 1 70 ? -46.222 6.214 37.644 1.00 12.09 ? 70 VAL A CA 1 ATOM 524 C C . VAL A 1 70 ? -47.662 5.706 37.455 1.00 12.69 ? 70 VAL A C 1 ATOM 525 O O . VAL A 1 70 ? -48.616 6.493 37.351 1.00 11.90 ? 70 VAL A O 1 ATOM 526 C CB . VAL A 1 70 ? -46.081 6.925 39.048 1.00 11.20 ? 70 VAL A CB 1 ATOM 527 C CG1 . VAL A 1 70 ? -45.960 5.884 40.153 1.00 11.02 ? 70 VAL A CG1 1 ATOM 528 C CG2 . VAL A 1 70 ? -44.879 7.853 39.105 1.00 7.11 ? 70 VAL A CG2 1 ATOM 529 N N . ALA A 1 71 ? -47.786 4.380 37.417 1.00 12.43 ? 71 ALA A N 1 ATOM 530 C CA . ALA A 1 71 ? -49.054 3.673 37.252 1.00 14.00 ? 71 ALA A CA 1 ATOM 531 C C . ALA A 1 71 ? -49.000 2.360 38.034 1.00 15.12 ? 71 ALA A C 1 ATOM 532 O O . ALA A 1 71 ? -47.945 1.986 38.549 1.00 16.96 ? 71 ALA A O 1 ATOM 533 C CB . ALA A 1 71 ? -49.290 3.377 35.779 1.00 11.96 ? 71 ALA A CB 1 ATOM 534 N N . ASN A 1 72 ? -50.143 1.686 38.158 1.00 14.46 ? 72 ASN A N 1 ATOM 535 C CA . ASN A 1 72 ? -50.197 0.396 38.841 1.00 14.58 ? 72 ASN A CA 1 ATOM 536 C C . ASN A 1 72 ? -50.268 -0.698 37.785 1.00 14.02 ? 72 ASN A C 1 ATOM 537 O O . ASN A 1 72 ? -50.418 -0.416 36.599 1.00 13.96 ? 72 ASN A O 1 ATOM 538 C CB . ASN A 1 72 ? -51.426 0.285 39.756 1.00 17.00 ? 72 ASN A CB 1 ATOM 539 C CG . ASN A 1 72 ? -51.395 1.261 40.912 1.00 18.57 ? 72 ASN A CG 1 ATOM 540 O OD1 . ASN A 1 72 ? -50.536 1.177 41.792 1.00 20.92 ? 72 ASN A OD1 1 ATOM 541 N ND2 . ASN A 1 72 ? -52.354 2.180 40.930 1.00 16.52 ? 72 ASN A ND2 1 ATOM 542 N N . TRP A 1 73 ? -50.130 -1.945 38.231 1.00 14.33 ? 73 TRP A N 1 ATOM 543 C CA . TRP A 1 73 ? -50.210 -3.131 37.385 1.00 15.06 ? 73 TRP A CA 1 ATOM 544 C C . TRP A 1 73 ? -51.658 -3.274 36.873 1.00 15.46 ? 73 TRP A C 1 ATOM 545 O O . TRP A 1 73 ? -52.600 -3.348 37.659 1.00 15.82 ? 73 TRP A O 1 ATOM 546 C CB . TRP A 1 73 ? -49.784 -4.343 38.223 1.00 13.76 ? 73 TRP A CB 1 ATOM 547 C CG . TRP A 1 73 ? -49.746 -5.702 37.560 1.00 13.08 ? 73 TRP A CG 1 ATOM 548 C CD1 . TRP A 1 73 ? -49.647 -5.990 36.219 1.00 14.25 ? 73 TRP A CD1 1 ATOM 549 C CD2 . TRP A 1 73 ? -49.747 -6.962 38.237 1.00 14.32 ? 73 TRP A CD2 1 ATOM 550 N NE1 . TRP A 1 73 ? -49.587 -7.349 36.027 1.00 12.89 ? 73 TRP A NE1 1 ATOM 551 C CE2 . TRP A 1 73 ? -49.643 -7.974 37.245 1.00 12.73 ? 73 TRP A CE2 1 ATOM 552 C CE3 . TRP A 1 73 ? -49.810 -7.340 39.597 1.00 13.51 ? 73 TRP A CE3 1 ATOM 553 C CZ2 . TRP A 1 73 ? -49.604 -9.349 37.567 1.00 13.24 ? 73 TRP A CZ2 1 ATOM 554 C CZ3 . TRP A 1 73 ? -49.767 -8.712 39.925 1.00 12.81 ? 73 TRP A CZ3 1 ATOM 555 C CH2 . TRP A 1 73 ? -49.665 -9.699 38.906 1.00 14.61 ? 73 TRP A CH2 1 ATOM 556 N N . GLY A 1 74 ? -51.807 -3.248 35.550 1.00 17.28 ? 74 GLY A N 1 ATOM 557 C CA . GLY A 1 74 ? -53.117 -3.369 34.933 1.00 17.45 ? 74 GLY A CA 1 ATOM 558 C C . GLY A 1 74 ? -53.631 -2.079 34.325 1.00 19.07 ? 74 GLY A C 1 ATOM 559 O O . GLY A 1 74 ? -54.527 -2.114 33.475 1.00 19.83 ? 74 GLY A O 1 ATOM 560 N N . ASP A 1 75 ? -53.079 -0.944 34.768 1.00 19.00 ? 75 ASP A N 1 ATOM 561 C CA . ASP A 1 75 ? -53.455 0.380 34.255 1.00 19.42 ? 75 ASP A CA 1 ATOM 562 C C . ASP A 1 75 ? -52.972 0.529 32.814 1.00 20.13 ? 75 ASP A C 1 ATOM 563 O O . ASP A 1 75 ? -52.109 -0.225 32.353 1.00 21.08 ? 75 ASP A O 1 ATOM 564 C CB . ASP A 1 75 ? -52.798 1.509 35.073 1.00 18.94 ? 75 ASP A CB 1 ATOM 565 C CG . ASP A 1 75 ? -53.340 1.638 36.495 1.00 19.66 ? 75 ASP A CG 1 ATOM 566 O OD1 . ASP A 1 75 ? -54.403 1.076 36.817 1.00 17.59 ? 75 ASP A OD1 1 ATOM 567 O OD2 . ASP A 1 75 ? -52.691 2.342 37.301 1.00 20.00 ? 75 ASP A OD2 1 ATOM 568 N N . THR A 1 76 ? -53.557 1.475 32.090 1.00 19.41 ? 76 THR A N 1 ATOM 569 C CA . THR A 1 76 ? -53.126 1.732 30.731 1.00 17.55 ? 76 THR A CA 1 ATOM 570 C C . THR A 1 76 ? -52.383 3.066 30.739 1.00 18.34 ? 76 THR A C 1 ATOM 571 O O . THR A 1 76 ? -52.835 4.035 31.349 1.00 18.80 ? 76 THR A O 1 ATOM 572 C CB . THR A 1 76 ? -54.304 1.757 29.743 1.00 19.42 ? 76 THR A CB 1 ATOM 573 O OG1 . THR A 1 76 ? -55.060 0.548 29.881 1.00 21.17 ? 76 THR A OG1 1 ATOM 574 C CG2 . THR A 1 76 ? -53.791 1.826 28.310 1.00 17.67 ? 76 THR A CG2 1 ATOM 575 N N . VAL A 1 77 ? -51.188 3.078 30.158 1.00 17.45 ? 77 VAL A N 1 ATOM 576 C CA . VAL A 1 77 ? -50.413 4.303 30.087 1.00 18.79 ? 77 VAL A CA 1 ATOM 577 C C . VAL A 1 77 ? -50.574 4.899 28.689 1.00 19.88 ? 77 VAL A C 1 ATOM 578 O O . VAL A 1 77 ? -50.343 4.233 27.668 1.00 17.25 ? 77 VAL A O 1 ATOM 579 C CB . VAL A 1 77 ? -48.926 4.078 30.436 1.00 19.40 ? 77 VAL A CB 1 ATOM 580 C CG1 . VAL A 1 77 ? -48.160 5.404 30.429 1.00 20.47 ? 77 VAL A CG1 1 ATOM 581 C CG2 . VAL A 1 77 ? -48.791 3.406 31.801 1.00 21.80 ? 77 VAL A CG2 1 ATOM 582 N N . GLU A 1 78 ? -51.023 6.152 28.678 1.00 21.00 ? 78 GLU A N 1 ATOM 583 C CA . GLU A 1 78 ? -51.245 6.899 27.460 1.00 20.55 ? 78 GLU A CA 1 ATOM 584 C C . GLU A 1 78 ? -50.359 8.129 27.469 1.00 20.27 ? 78 GLU A C 1 ATOM 585 O O . GLU A 1 78 ? -50.369 8.899 28.429 1.00 21.22 ? 78 GLU A O 1 ATOM 586 C CB . GLU A 1 78 ? -52.707 7.303 27.346 1.00 22.24 ? 78 GLU A CB 1 ATOM 587 C CG . GLU A 1 78 ? -53.132 7.531 25.918 1.00 26.30 ? 78 GLU A CG 1 ATOM 588 C CD . GLU A 1 78 ? -54.582 7.919 25.771 1.00 27.72 ? 78 GLU A CD 1 ATOM 589 O OE1 . GLU A 1 78 ? -55.416 7.490 26.594 1.00 30.53 ? 78 GLU A OE1 1 ATOM 590 O OE2 . GLU A 1 78 ? -54.892 8.642 24.805 1.00 29.36 ? 78 GLU A OE2 1 ATOM 591 N N . VAL A 1 79 ? -49.567 8.288 26.410 1.00 17.12 ? 79 VAL A N 1 ATOM 592 C CA . VAL A 1 79 ? -48.643 9.412 26.279 1.00 14.63 ? 79 VAL A CA 1 ATOM 593 C C . VAL A 1 79 ? -48.711 10.092 24.906 1.00 14.49 ? 79 VAL A C 1 ATOM 594 O O . VAL A 1 79 ? -48.535 9.447 23.873 1.00 16.09 ? 79 VAL A O 1 ATOM 595 C CB . VAL A 1 79 ? -47.179 8.959 26.560 1.00 13.00 ? 79 VAL A CB 1 ATOM 596 C CG1 . VAL A 1 79 ? -46.203 10.057 26.248 1.00 11.47 ? 79 VAL A CG1 1 ATOM 597 C CG2 . VAL A 1 79 ? -46.998 8.548 28.012 1.00 12.14 ? 79 VAL A CG2 1 ATOM 598 N N . THR A 1 80 ? -48.908 11.408 24.914 1.00 14.42 ? 80 THR A N 1 ATOM 599 C CA . THR A 1 80 ? -48.970 12.189 23.683 1.00 15.21 ? 80 THR A CA 1 ATOM 600 C C . THR A 1 80 ? -47.644 12.908 23.494 1.00 14.65 ? 80 THR A C 1 ATOM 601 O O . THR A 1 80 ? -47.286 13.809 24.254 1.00 13.45 ? 80 THR A O 1 ATOM 602 C CB . THR A 1 80 ? -50.179 13.169 23.680 1.00 16.23 ? 80 THR A CB 1 ATOM 603 O OG1 . THR A 1 80 ? -51.388 12.411 23.811 1.00 18.35 ? 80 THR A OG1 1 ATOM 604 C CG2 . THR A 1 80 ? -50.252 13.971 22.376 1.00 15.95 ? 80 THR A CG2 1 ATOM 605 N N . VAL A 1 81 ? -46.893 12.438 22.505 1.00 15.49 ? 81 VAL A N 1 ATOM 606 C CA . VAL A 1 81 ? -45.590 12.998 22.180 1.00 16.86 ? 81 VAL A CA 1 ATOM 607 C C . VAL A 1 81 ? -45.739 14.014 21.058 1.00 17.04 ? 81 VAL A C 1 ATOM 608 O O . VAL A 1 81 ? -46.124 13.676 19.940 1.00 19.46 ? 81 VAL A O 1 ATOM 609 C CB . VAL A 1 81 ? -44.559 11.880 21.807 1.00 18.13 ? 81 VAL A CB 1 ATOM 610 C CG1 . VAL A 1 81 ? -43.161 12.468 21.561 1.00 17.35 ? 81 VAL A CG1 1 ATOM 611 C CG2 . VAL A 1 81 ? -44.479 10.855 22.929 1.00 17.32 ? 81 VAL A CG2 1 ATOM 612 N N . ILE A 1 82 ? -45.524 15.275 21.420 1.00 17.39 ? 82 ILE A N 1 ATOM 613 C CA . ILE A 1 82 ? -45.583 16.402 20.504 1.00 17.56 ? 82 ILE A CA 1 ATOM 614 C C . ILE A 1 82 ? -44.122 16.775 20.245 1.00 17.81 ? 82 ILE A C 1 ATOM 615 O O . ILE A 1 82 ? -43.344 16.989 21.180 1.00 16.78 ? 82 ILE A O 1 ATOM 616 C CB . ILE A 1 82 ? -46.390 17.604 21.108 1.00 19.09 ? 82 ILE A CB 1 ATOM 617 C CG1 . ILE A 1 82 ? -47.810 17.155 21.484 1.00 19.27 ? 82 ILE A CG1 1 ATOM 618 C CG2 . ILE A 1 82 ? -46.488 18.753 20.095 1.00 19.30 ? 82 ILE A CG2 1 ATOM 619 C CD1 . ILE A 1 82 ? -48.549 18.106 22.370 1.00 21.83 ? 82 ILE A CD1 1 ATOM 620 N N . ASN A 1 83 ? -43.763 16.815 18.967 1.00 19.00 ? 83 ASN A N 1 ATOM 621 C CA . ASN A 1 83 ? -42.406 17.122 18.534 1.00 19.45 ? 83 ASN A CA 1 ATOM 622 C C . ASN A 1 83 ? -42.212 18.580 18.102 1.00 19.19 ? 83 ASN A C 1 ATOM 623 O O . ASN A 1 83 ? -42.536 18.954 16.970 1.00 19.89 ? 83 ASN A O 1 ATOM 624 C CB . ASN A 1 83 ? -42.014 16.158 17.402 1.00 19.76 ? 83 ASN A CB 1 ATOM 625 C CG . ASN A 1 83 ? -40.533 16.226 17.036 1.00 20.15 ? 83 ASN A CG 1 ATOM 626 O OD1 . ASN A 1 83 ? -39.780 17.036 17.564 1.00 20.36 ? 83 ASN A OD1 1 ATOM 627 N ND2 . ASN A 1 83 ? -40.121 15.375 16.108 1.00 19.48 ? 83 ASN A ND2 1 ATOM 628 N N . ASN A 1 84 ? -41.639 19.379 19.000 1.00 17.98 ? 84 ASN A N 1 ATOM 629 C CA . ASN A 1 84 ? -41.363 20.778 18.708 1.00 16.80 ? 84 ASN A CA 1 ATOM 630 C C . ASN A 1 84 ? -39.864 21.044 18.496 1.00 14.95 ? 84 ASN A C 1 ATOM 631 O O . ASN A 1 84 ? -39.392 22.176 18.652 1.00 16.45 ? 84 ASN A O 1 ATOM 632 C CB . ASN A 1 84 ? -41.974 21.702 19.774 1.00 16.34 ? 84 ASN A CB 1 ATOM 633 C CG . ASN A 1 84 ? -43.478 21.868 19.613 1.00 20.19 ? 84 ASN A CG 1 ATOM 634 O OD1 . ASN A 1 84 ? -43.970 22.202 18.528 1.00 22.33 ? 84 ASN A OD1 1 ATOM 635 N ND2 . ASN A 1 84 ? -44.218 21.638 20.692 1.00 20.13 ? 84 ASN A ND2 1 ATOM 636 N N . LEU A 1 85 ? -39.121 20.000 18.112 1.00 13.01 ? 85 LEU A N 1 ATOM 637 C CA . LEU A 1 85 ? -37.685 20.138 17.814 1.00 14.44 ? 85 LEU A CA 1 ATOM 638 C C . LEU A 1 85 ? -37.565 20.865 16.472 1.00 14.25 ? 85 LEU A C 1 ATOM 639 O O . LEU A 1 85 ? -38.559 21.033 15.765 1.00 14.55 ? 85 LEU A O 1 ATOM 640 C CB . LEU A 1 85 ? -36.970 18.773 17.759 1.00 12.56 ? 85 LEU A CB 1 ATOM 641 C CG . LEU A 1 85 ? -37.007 17.870 19.005 1.00 11.67 ? 85 LEU A CG 1 ATOM 642 C CD1 . LEU A 1 85 ? -36.273 16.567 18.760 1.00 10.60 ? 85 LEU A CD1 1 ATOM 643 C CD2 . LEU A 1 85 ? -36.439 18.564 20.210 1.00 10.37 ? 85 LEU A CD2 1 ATOM 644 N N . VAL A 1 86 ? -36.369 21.309 16.117 1.00 14.04 ? 86 VAL A N 1 ATOM 645 C CA . VAL A 1 86 ? -36.223 22.058 14.876 1.00 15.58 ? 86 VAL A CA 1 ATOM 646 C C . VAL A 1 86 ? -36.199 21.192 13.626 1.00 15.67 ? 86 VAL A C 1 ATOM 647 O O . VAL A 1 86 ? -37.080 21.306 12.772 1.00 16.06 ? 86 VAL A O 1 ATOM 648 C CB . VAL A 1 86 ? -34.984 23.017 14.899 1.00 15.40 ? 86 VAL A CB 1 ATOM 649 C CG1 . VAL A 1 86 ? -35.033 23.977 13.702 1.00 14.70 ? 86 VAL A CG1 1 ATOM 650 C CG2 . VAL A 1 86 ? -34.939 23.818 16.207 1.00 12.74 ? 86 VAL A CG2 1 ATOM 651 N N . THR A 1 87 ? -35.220 20.297 13.563 1.00 17.75 ? 87 THR A N 1 ATOM 652 C CA . THR A 1 87 ? -35.013 19.430 12.410 1.00 17.90 ? 87 THR A CA 1 ATOM 653 C C . THR A 1 87 ? -35.337 17.959 12.618 1.00 18.20 ? 87 THR A C 1 ATOM 654 O O . THR A 1 87 ? -35.933 17.320 11.746 1.00 17.97 ? 87 THR A O 1 ATOM 655 C CB . THR A 1 87 ? -33.560 19.543 11.944 1.00 19.57 ? 87 THR A CB 1 ATOM 656 O OG1 . THR A 1 87 ? -32.692 19.269 13.050 1.00 22.11 ? 87 THR A OG1 1 ATOM 657 C CG2 . THR A 1 87 ? -33.269 20.949 11.425 1.00 19.02 ? 87 THR A CG2 1 ATOM 658 N N . ASN A 1 88 ? -34.952 17.438 13.781 1.00 16.34 ? 88 ASN A N 1 ATOM 659 C CA . ASN A 1 88 ? -35.146 16.036 14.141 1.00 16.20 ? 88 ASN A CA 1 ATOM 660 C C . ASN A 1 88 ? -36.562 15.477 14.212 1.00 15.05 ? 88 ASN A C 1 ATOM 661 O O . ASN A 1 88 ? -37.494 16.141 14.666 1.00 16.08 ? 88 ASN A O 1 ATOM 662 C CB . ASN A 1 88 ? -34.508 15.752 15.502 1.00 18.49 ? 88 ASN A CB 1 ATOM 663 C CG . ASN A 1 88 ? -33.019 15.516 15.437 1.00 19.35 ? 88 ASN A CG 1 ATOM 664 O OD1 . ASN A 1 88 ? -32.466 14.910 16.352 1.00 18.32 ? 88 ASN A OD1 1 ATOM 665 N ND2 . ASN A 1 88 ? -32.359 16.010 14.394 1.00 19.46 ? 88 ASN A ND2 1 ATOM 666 N N . GLY A 1 89 ? -36.683 14.216 13.804 1.00 13.34 ? 89 GLY A N 1 ATOM 667 C CA . GLY A 1 89 ? -37.938 13.501 13.914 1.00 9.99 ? 89 GLY A CA 1 ATOM 668 C C . GLY A 1 89 ? -37.806 12.828 15.272 1.00 9.92 ? 89 GLY A C 1 ATOM 669 O O . GLY A 1 89 ? -36.771 13.012 15.939 1.00 7.70 ? 89 GLY A O 1 ATOM 670 N N . THR A 1 90 ? -38.817 12.076 15.701 1.00 7.98 ? 90 THR A N 1 ATOM 671 C CA . THR A 1 90 ? -38.749 11.398 16.994 1.00 10.01 ? 90 THR A CA 1 ATOM 672 C C . THR A 1 90 ? -39.736 10.251 17.169 1.00 10.37 ? 90 THR A C 1 ATOM 673 O O . THR A 1 90 ? -40.563 9.965 16.312 1.00 10.88 ? 90 THR A O 1 ATOM 674 C CB . THR A 1 90 ? -38.889 12.410 18.207 1.00 10.52 ? 90 THR A CB 1 ATOM 675 O OG1 . THR A 1 90 ? -38.389 11.807 19.404 1.00 11.39 ? 90 THR A OG1 1 ATOM 676 C CG2 . THR A 1 90 ? -40.340 12.834 18.437 1.00 12.84 ? 90 THR A CG2 1 ATOM 677 N N . SER A 1 91 ? -39.608 9.617 18.323 1.00 11.68 ? 91 SER A N 1 ATOM 678 C CA . SER A 1 91 ? -40.435 8.515 18.780 1.00 12.06 ? 91 SER A CA 1 ATOM 679 C C . SER A 1 91 ? -39.987 8.304 20.210 1.00 11.24 ? 91 SER A C 1 ATOM 680 O O . SER A 1 91 ? -39.000 8.896 20.635 1.00 14.49 ? 91 SER A O 1 ATOM 681 C CB . SER A 1 91 ? -40.173 7.244 17.970 1.00 11.53 ? 91 SER A CB 1 ATOM 682 O OG . SER A 1 91 ? -38.832 6.808 18.092 1.00 10.04 ? 91 SER A OG 1 ATOM 683 N N . ILE A 1 92 ? -40.777 7.587 20.991 1.00 10.28 ? 92 ILE A N 1 ATOM 684 C CA . ILE A 1 92 ? -40.377 7.276 22.351 1.00 12.29 ? 92 ILE A CA 1 ATOM 685 C C . ILE A 1 92 ? -40.579 5.777 22.505 1.00 13.76 ? 92 ILE A C 1 ATOM 686 O O . ILE A 1 92 ? -41.696 5.264 22.339 1.00 12.97 ? 92 ILE A O 1 ATOM 687 C CB . ILE A 1 92 ? -41.158 8.061 23.471 1.00 11.65 ? 92 ILE A CB 1 ATOM 688 C CG1 . ILE A 1 92 ? -40.891 9.573 23.414 1.00 10.41 ? 92 ILE A CG1 1 ATOM 689 C CG2 . ILE A 1 92 ? -40.728 7.565 24.855 1.00 9.83 ? 92 ILE A CG2 1 ATOM 690 C CD1 . ILE A 1 92 ? -39.445 9.996 23.665 1.00 12.85 ? 92 ILE A CD1 1 ATOM 691 N N . HIS A 1 93 ? -39.469 5.082 22.745 1.00 13.10 ? 93 HIS A N 1 ATOM 692 C CA . HIS A 1 93 ? -39.498 3.652 22.955 1.00 15.42 ? 93 HIS A CA 1 ATOM 693 C C . HIS A 1 93 ? -39.659 3.371 24.444 1.00 15.65 ? 93 HIS A C 1 ATOM 694 O O . HIS A 1 93 ? -38.934 3.913 25.274 1.00 13.89 ? 93 HIS A O 1 ATOM 695 C CB . HIS A 1 93 ? -38.236 2.972 22.411 1.00 16.39 ? 93 HIS A CB 1 ATOM 696 C CG . HIS A 1 93 ? -38.153 1.513 22.746 1.00 17.48 ? 93 HIS A CG 1 ATOM 697 N ND1 . HIS A 1 93 ? -39.162 0.623 22.444 1.00 20.04 ? 93 HIS A ND1 1 ATOM 698 C CD2 . HIS A 1 93 ? -37.253 0.821 23.482 1.00 18.58 ? 93 HIS A CD2 1 ATOM 699 C CE1 . HIS A 1 93 ? -38.896 -0.548 22.991 1.00 18.38 ? 93 HIS A CE1 1 ATOM 700 N NE2 . HIS A 1 93 ? -37.743 -0.455 23.626 1.00 18.98 ? 93 HIS A NE2 1 ATOM 701 N N . TRP A 1 94 ? -40.570 2.450 24.734 1.00 17.29 ? 94 TRP A N 1 ATOM 702 C CA . TRP A 1 94 ? -40.895 2.024 26.083 1.00 19.40 ? 94 TRP A CA 1 ATOM 703 C C . TRP A 1 94 ? -40.118 0.735 26.347 1.00 20.54 ? 94 TRP A C 1 ATOM 704 O O . TRP A 1 94 ? -40.538 -0.352 25.953 1.00 20.67 ? 94 TRP A O 1 ATOM 705 C CB . TRP A 1 94 ? -42.419 1.848 26.197 1.00 19.72 ? 94 TRP A CB 1 ATOM 706 C CG . TRP A 1 94 ? -43.168 2.955 25.479 1.00 22.13 ? 94 TRP A CG 1 ATOM 707 C CD1 . TRP A 1 94 ? -43.620 2.929 24.191 1.00 23.85 ? 94 TRP A CD1 1 ATOM 708 C CD2 . TRP A 1 94 ? -43.405 4.285 25.954 1.00 22.46 ? 94 TRP A CD2 1 ATOM 709 N NE1 . TRP A 1 94 ? -44.100 4.161 23.823 1.00 24.72 ? 94 TRP A NE1 1 ATOM 710 C CE2 . TRP A 1 94 ? -43.984 5.015 24.885 1.00 23.56 ? 94 TRP A CE2 1 ATOM 711 C CE3 . TRP A 1 94 ? -43.180 4.940 27.180 1.00 23.45 ? 94 TRP A CE3 1 ATOM 712 C CZ2 . TRP A 1 94 ? -44.339 6.374 25.001 1.00 24.29 ? 94 TRP A CZ2 1 ATOM 713 C CZ3 . TRP A 1 94 ? -43.534 6.300 27.299 1.00 23.66 ? 94 TRP A CZ3 1 ATOM 714 C CH2 . TRP A 1 94 ? -44.104 6.995 26.212 1.00 23.36 ? 94 TRP A CH2 1 ATOM 715 N N . HIS A 1 95 ? -38.930 0.910 26.935 1.00 21.90 ? 95 HIS A N 1 ATOM 716 C CA . HIS A 1 95 ? -37.985 -0.165 27.267 1.00 22.13 ? 95 HIS A CA 1 ATOM 717 C C . HIS A 1 95 ? -38.481 -1.048 28.412 1.00 21.54 ? 95 HIS A C 1 ATOM 718 O O . HIS A 1 95 ? -38.710 -0.571 29.518 1.00 21.14 ? 95 HIS A O 1 ATOM 719 C CB . HIS A 1 95 ? -36.616 0.466 27.609 1.00 21.40 ? 95 HIS A CB 1 ATOM 720 C CG . HIS A 1 95 ? -35.468 -0.503 27.714 1.00 22.24 ? 95 HIS A CG 1 ATOM 721 N ND1 . HIS A 1 95 ? -34.230 -0.227 27.180 1.00 23.57 ? 95 HIS A ND1 1 ATOM 722 C CD2 . HIS A 1 95 ? -35.340 -1.694 28.349 1.00 21.89 ? 95 HIS A CD2 1 ATOM 723 C CE1 . HIS A 1 95 ? -33.392 -1.203 27.479 1.00 24.06 ? 95 HIS A CE1 1 ATOM 724 N NE2 . HIS A 1 95 ? -34.041 -2.107 28.187 1.00 22.22 ? 95 HIS A NE2 1 ATOM 725 N N . GLY A 1 96 ? -38.530 -2.350 28.145 1.00 21.19 ? 96 GLY A N 1 ATOM 726 C CA . GLY A 1 96 ? -38.971 -3.316 29.133 1.00 25.06 ? 96 GLY A CA 1 ATOM 727 C C . GLY A 1 96 ? -40.421 -3.689 28.943 1.00 26.43 ? 96 GLY A C 1 ATOM 728 O O . GLY A 1 96 ? -40.852 -4.770 29.345 1.00 27.73 ? 96 GLY A O 1 ATOM 729 N N . ILE A 1 97 ? -41.172 -2.780 28.327 1.00 27.28 ? 97 ILE A N 1 ATOM 730 C CA . ILE A 1 97 ? -42.582 -2.991 28.057 1.00 28.54 ? 97 ILE A CA 1 ATOM 731 C C . ILE A 1 97 ? -42.722 -3.852 26.813 1.00 28.76 ? 97 ILE A C 1 ATOM 732 O O . ILE A 1 97 ? -42.349 -3.462 25.694 1.00 27.21 ? 97 ILE A O 1 ATOM 733 C CB . ILE A 1 97 ? -43.369 -1.657 27.958 1.00 29.63 ? 97 ILE A CB 1 ATOM 734 C CG1 . ILE A 1 97 ? -43.386 -0.967 29.327 1.00 31.60 ? 97 ILE A CG1 1 ATOM 735 C CG2 . ILE A 1 97 ? -44.833 -1.907 27.546 1.00 30.04 ? 97 ILE A CG2 1 ATOM 736 C CD1 . ILE A 1 97 ? -42.135 -0.211 29.690 1.00 33.42 ? 97 ILE A CD1 1 ATOM 737 N N . HIS A 1 98 ? -43.262 -5.040 27.061 1.00 28.84 ? 98 HIS A N 1 ATOM 738 C CA . HIS A 1 98 ? -43.473 -6.071 26.064 1.00 29.29 ? 98 HIS A CA 1 ATOM 739 C C . HIS A 1 98 ? -44.289 -5.708 24.840 1.00 28.14 ? 98 HIS A C 1 ATOM 740 O O . HIS A 1 98 ? -44.009 -6.196 23.745 1.00 26.88 ? 98 HIS A O 1 ATOM 741 C CB . HIS A 1 98 ? -44.070 -7.307 26.731 1.00 31.19 ? 98 HIS A CB 1 ATOM 742 C CG . HIS A 1 98 ? -43.131 -8.002 27.665 1.00 31.41 ? 98 HIS A CG 1 ATOM 743 N ND1 . HIS A 1 98 ? -43.513 -9.082 28.429 1.00 31.77 ? 98 HIS A ND1 1 ATOM 744 C CD2 . HIS A 1 98 ? -41.822 -7.791 27.939 1.00 30.85 ? 98 HIS A CD2 1 ATOM 745 C CE1 . HIS A 1 98 ? -42.480 -9.509 29.130 1.00 31.41 ? 98 HIS A CE1 1 ATOM 746 N NE2 . HIS A 1 98 ? -41.443 -8.741 28.852 1.00 32.52 ? 98 HIS A NE2 1 ATOM 747 N N . GLN A 1 99 ? -45.250 -4.802 25.026 1.00 28.20 ? 99 GLN A N 1 ATOM 748 C CA . GLN A 1 99 ? -46.165 -4.351 23.970 1.00 28.65 ? 99 GLN A CA 1 ATOM 749 C C . GLN A 1 99 ? -46.947 -5.544 23.371 1.00 28.31 ? 99 GLN A C 1 ATOM 750 O O . GLN A 1 99 ? -46.973 -5.741 22.148 1.00 28.63 ? 99 GLN A O 1 ATOM 751 C CB . GLN A 1 99 ? -45.431 -3.557 22.855 1.00 26.64 ? 99 GLN A CB 1 ATOM 752 C CG . GLN A 1 99 ? -44.599 -2.352 23.295 1.00 23.40 ? 99 GLN A CG 1 ATOM 753 C CD . GLN A 1 99 ? -45.391 -1.093 23.623 1.00 22.45 ? 99 GLN A CD 1 ATOM 754 O OE1 . GLN A 1 99 ? -44.808 -0.096 24.042 1.00 23.25 ? 99 GLN A OE1 1 ATOM 755 N NE2 . GLN A 1 99 ? -46.706 -1.121 23.424 1.00 19.91 ? 99 GLN A NE2 1 ATOM 756 N N . LYS A 1 100 ? -47.552 -6.342 24.258 1.00 28.05 ? 100 LYS A N 1 ATOM 757 C CA . LYS A 1 100 ? -48.330 -7.532 23.888 1.00 27.35 ? 100 LYS A CA 1 ATOM 758 C C . LYS A 1 100 ? -49.486 -7.185 22.951 1.00 24.88 ? 100 LYS A C 1 ATOM 759 O O . LYS A 1 100 ? -50.449 -6.528 23.352 1.00 23.82 ? 100 LYS A O 1 ATOM 760 C CB . LYS A 1 100 ? -48.839 -8.239 25.147 1.00 29.63 ? 100 LYS A CB 1 ATOM 761 C CG . LYS A 1 100 ? -48.984 -9.755 25.038 1.00 33.33 ? 100 LYS A CG 1 ATOM 762 C CD . LYS A 1 100 ? -47.633 -10.444 24.896 1.00 35.76 ? 100 LYS A CD 1 ATOM 763 C CE . LYS A 1 100 ? -47.766 -11.948 25.036 1.00 38.88 ? 100 LYS A CE 1 ATOM 764 N NZ . LYS A 1 100 ? -47.825 -12.391 26.457 1.00 40.12 ? 100 LYS A NZ 1 ATOM 765 N N . ASP A 1 101 ? -49.318 -7.576 21.682 1.00 23.90 ? 101 ASP A N 1 ATOM 766 C CA . ASP A 1 101 ? -50.257 -7.330 20.566 1.00 22.10 ? 101 ASP A CA 1 ATOM 767 C C . ASP A 1 101 ? -50.418 -5.837 20.212 1.00 18.69 ? 101 ASP A C 1 ATOM 768 O O . ASP A 1 101 ? -51.374 -5.445 19.544 1.00 18.09 ? 101 ASP A O 1 ATOM 769 C CB . ASP A 1 101 ? -51.632 -8.003 20.791 1.00 24.37 ? 101 ASP A CB 1 ATOM 770 C CG . ASP A 1 101 ? -51.550 -9.522 20.832 1.00 26.51 ? 101 ASP A CG 1 ATOM 771 O OD1 . ASP A 1 101 ? -51.082 -10.128 19.843 1.00 26.45 ? 101 ASP A OD1 1 ATOM 772 O OD2 . ASP A 1 101 ? -51.971 -10.106 21.856 1.00 27.62 ? 101 ASP A OD2 1 ATOM 773 N N . THR A 1 102 ? -49.490 -5.011 20.703 1.00 17.25 ? 102 THR A N 1 ATOM 774 C CA . THR A 1 102 ? -49.485 -3.567 20.440 1.00 14.09 ? 102 THR A CA 1 ATOM 775 C C . THR A 1 102 ? -48.125 -3.160 19.852 1.00 13.47 ? 102 THR A C 1 ATOM 776 O O . THR A 1 102 ? -47.543 -2.159 20.254 1.00 13.78 ? 102 THR A O 1 ATOM 777 C CB . THR A 1 102 ? -49.816 -2.708 21.724 1.00 12.58 ? 102 THR A CB 1 ATOM 778 O OG1 . THR A 1 102 ? -48.908 -3.017 22.791 1.00 10.26 ? 102 THR A OG1 1 ATOM 779 C CG2 . THR A 1 102 ? -51.256 -2.907 22.189 1.00 9.98 ? 102 THR A CG2 1 ATOM 780 N N . ASN A 1 103 ? -47.665 -3.909 18.844 1.00 14.88 ? 103 ASN A N 1 ATOM 781 C CA . ASN A 1 103 ? -46.368 -3.687 18.166 1.00 14.15 ? 103 ASN A CA 1 ATOM 782 C C . ASN A 1 103 ? -46.118 -2.268 17.622 1.00 12.92 ? 103 ASN A C 1 ATOM 783 O O . ASN A 1 103 ? -45.008 -1.753 17.729 1.00 11.30 ? 103 ASN A O 1 ATOM 784 C CB . ASN A 1 103 ? -46.175 -4.742 17.053 1.00 13.86 ? 103 ASN A CB 1 ATOM 785 C CG . ASN A 1 103 ? -44.751 -4.757 16.456 1.00 14.11 ? 103 ASN A CG 1 ATOM 786 O OD1 . ASN A 1 103 ? -44.577 -4.966 15.254 1.00 14.56 ? 103 ASN A OD1 1 ATOM 787 N ND2 . ASN A 1 103 ? -43.746 -4.561 17.292 1.00 11.25 ? 103 ASN A ND2 1 ATOM 788 N N . LEU A 1 104 ? -47.175 -1.622 17.133 1.00 13.80 ? 104 LEU A N 1 ATOM 789 C CA . LEU A 1 104 ? -47.095 -0.273 16.565 1.00 13.34 ? 104 LEU A CA 1 ATOM 790 C C . LEU A 1 104 ? -46.885 0.880 17.554 1.00 12.58 ? 104 LEU A C 1 ATOM 791 O O . LEU A 1 104 ? -46.734 2.031 17.152 1.00 11.62 ? 104 LEU A O 1 ATOM 792 C CB . LEU A 1 104 ? -48.292 -0.019 15.645 1.00 15.23 ? 104 LEU A CB 1 ATOM 793 C CG . LEU A 1 104 ? -48.143 -0.561 14.212 1.00 16.89 ? 104 LEU A CG 1 ATOM 794 C CD1 . LEU A 1 104 ? -48.095 -2.085 14.184 1.00 16.62 ? 104 LEU A CD1 1 ATOM 795 C CD2 . LEU A 1 104 ? -49.286 -0.053 13.350 1.00 15.86 ? 104 LEU A CD2 1 ATOM 796 N N . HIS A 1 105 ? -46.825 0.544 18.842 1.00 13.40 ? 105 HIS A N 1 ATOM 797 C CA . HIS A 1 105 ? -46.586 1.515 19.911 1.00 13.02 ? 105 HIS A CA 1 ATOM 798 C C . HIS A 1 105 ? -45.165 1.391 20.483 1.00 12.95 ? 105 HIS A C 1 ATOM 799 O O . HIS A 1 105 ? -44.798 2.129 21.400 1.00 15.77 ? 105 HIS A O 1 ATOM 800 C CB . HIS A 1 105 ? -47.611 1.338 21.036 1.00 12.76 ? 105 HIS A CB 1 ATOM 801 C CG . HIS A 1 105 ? -49.023 1.588 20.612 1.00 11.93 ? 105 HIS A CG 1 ATOM 802 N ND1 . HIS A 1 105 ? -49.588 2.846 20.613 1.00 10.37 ? 105 HIS A ND1 1 ATOM 803 C CD2 . HIS A 1 105 ? -49.979 0.745 20.158 1.00 9.72 ? 105 HIS A CD2 1 ATOM 804 C CE1 . HIS A 1 105 ? -50.833 2.765 20.177 1.00 11.71 ? 105 HIS A CE1 1 ATOM 805 N NE2 . HIS A 1 105 ? -51.095 1.501 19.896 1.00 11.70 ? 105 HIS A NE2 1 ATOM 806 N N . ASP A 1 106 ? -44.360 0.500 19.903 1.00 11.66 ? 106 ASP A N 1 ATOM 807 C CA . ASP A 1 106 ? -42.987 0.249 20.343 1.00 10.34 ? 106 ASP A CA 1 ATOM 808 C C . ASP A 1 106 ? -41.988 1.401 20.181 1.00 11.30 ? 106 ASP A C 1 ATOM 809 O O . ASP A 1 106 ? -40.985 1.451 20.890 1.00 10.76 ? 106 ASP A O 1 ATOM 810 C CB . ASP A 1 106 ? -42.449 -1.010 19.678 1.00 10.91 ? 106 ASP A CB 1 ATOM 811 C CG . ASP A 1 106 ? -41.263 -1.582 20.400 1.00 10.81 ? 106 ASP A CG 1 ATOM 812 O OD1 . ASP A 1 106 ? -41.405 -1.884 21.598 1.00 15.81 ? 106 ASP A OD1 1 ATOM 813 O OD2 . ASP A 1 106 ? -40.189 -1.700 19.786 1.00 9.91 ? 106 ASP A OD2 1 ATOM 814 N N . GLY A 1 107 ? -42.248 2.304 19.238 1.00 12.75 ? 107 GLY A N 1 ATOM 815 C CA . GLY A 1 107 ? -41.374 3.454 19.037 1.00 13.10 ? 107 GLY A CA 1 ATOM 816 C C . GLY A 1 107 ? -40.105 3.256 18.226 1.00 14.05 ? 107 GLY A C 1 ATOM 817 O O . GLY A 1 107 ? -39.283 4.170 18.123 1.00 12.96 ? 107 GLY A O 1 ATOM 818 N N . ALA A 1 108 ? -39.941 2.074 17.645 1.00 13.93 ? 108 ALA A N 1 ATOM 819 C CA . ALA A 1 108 ? -38.768 1.791 16.830 1.00 15.07 ? 108 ALA A CA 1 ATOM 820 C C . ALA A 1 108 ? -38.977 2.365 15.426 1.00 15.57 ? 108 ALA A C 1 ATOM 821 O O . ALA A 1 108 ? -39.808 1.879 14.653 1.00 15.47 ? 108 ALA A O 1 ATOM 822 C CB . ALA A 1 108 ? -38.499 0.291 16.782 1.00 13.48 ? 108 ALA A CB 1 ATOM 823 N N . ASN A 1 109 ? -38.254 3.449 15.150 1.00 15.41 ? 109 ASN A N 1 ATOM 824 C CA . ASN A 1 109 ? -38.306 4.149 13.871 1.00 16.43 ? 109 ASN A CA 1 ATOM 825 C C . ASN A 1 109 ? -37.766 3.315 12.729 1.00 16.97 ? 109 ASN A C 1 ATOM 826 O O . ASN A 1 109 ? -36.717 2.675 12.853 1.00 18.98 ? 109 ASN A O 1 ATOM 827 C CB . ASN A 1 109 ? -37.531 5.460 13.947 1.00 17.30 ? 109 ASN A CB 1 ATOM 828 C CG . ASN A 1 109 ? -38.192 6.468 14.846 1.00 15.89 ? 109 ASN A CG 1 ATOM 829 O OD1 . ASN A 1 109 ? -39.387 6.718 14.744 1.00 15.91 ? 109 ASN A OD1 1 ATOM 830 N ND2 . ASN A 1 109 ? -37.416 7.053 15.736 1.00 16.07 ? 109 ASN A ND2 1 ATOM 831 N N . GLY A 1 110 ? -38.514 3.309 11.628 1.00 16.79 ? 110 GLY A N 1 ATOM 832 C CA . GLY A 1 110 ? -38.136 2.536 10.461 1.00 14.49 ? 110 GLY A CA 1 ATOM 833 C C . GLY A 1 110 ? -38.453 1.061 10.630 1.00 14.04 ? 110 GLY A C 1 ATOM 834 O O . GLY A 1 110 ? -38.103 0.231 9.789 1.00 13.87 ? 110 GLY A O 1 ATOM 835 N N . VAL A 1 111 ? -39.126 0.742 11.731 1.00 13.38 ? 111 VAL A N 1 ATOM 836 C CA . VAL A 1 111 ? -39.516 -0.621 12.063 1.00 12.69 ? 111 VAL A CA 1 ATOM 837 C C . VAL A 1 111 ? -41.022 -0.653 12.375 1.00 13.61 ? 111 VAL A C 1 ATOM 838 O O . VAL A 1 111 ? -41.791 -1.253 11.620 1.00 13.65 ? 111 VAL A O 1 ATOM 839 C CB . VAL A 1 111 ? -38.683 -1.169 13.281 1.00 10.73 ? 111 VAL A CB 1 ATOM 840 C CG1 . VAL A 1 111 ? -39.034 -2.619 13.606 1.00 6.73 ? 111 VAL A CG1 1 ATOM 841 C CG2 . VAL A 1 111 ? -37.197 -1.051 13.015 1.00 7.98 ? 111 VAL A CG2 1 ATOM 842 N N . THR A 1 112 ? -41.432 0.010 13.463 1.00 13.61 ? 112 THR A N 1 ATOM 843 C CA . THR A 1 112 ? -42.841 0.023 13.884 1.00 14.21 ? 112 THR A CA 1 ATOM 844 C C . THR A 1 112 ? -43.599 1.287 13.521 1.00 14.70 ? 112 THR A C 1 ATOM 845 O O . THR A 1 112 ? -44.838 1.312 13.531 1.00 14.68 ? 112 THR A O 1 ATOM 846 C CB . THR A 1 112 ? -43.016 -0.273 15.414 1.00 13.47 ? 112 THR A CB 1 ATOM 847 O OG1 . THR A 1 112 ? -42.391 0.747 16.209 1.00 9.56 ? 112 THR A OG1 1 ATOM 848 C CG2 . THR A 1 112 ? -42.434 -1.633 15.772 1.00 12.10 ? 112 THR A CG2 1 ATOM 849 N N . GLU A 1 113 ? -42.844 2.332 13.198 1.00 15.59 ? 113 GLU A N 1 ATOM 850 C CA . GLU A 1 113 ? -43.416 3.626 12.838 1.00 16.32 ? 113 GLU A CA 1 ATOM 851 C C . GLU A 1 113 ? -42.423 4.484 12.081 1.00 16.14 ? 113 GLU A C 1 ATOM 852 O O . GLU A 1 113 ? -41.231 4.153 11.973 1.00 15.94 ? 113 GLU A O 1 ATOM 853 C CB . GLU A 1 113 ? -43.863 4.397 14.099 1.00 16.44 ? 113 GLU A CB 1 ATOM 854 C CG . GLU A 1 113 ? -42.726 4.828 15.039 1.00 17.84 ? 113 GLU A CG 1 ATOM 855 C CD . GLU A 1 113 ? -43.208 5.685 16.190 1.00 21.15 ? 113 GLU A CD 1 ATOM 856 O OE1 . GLU A 1 113 ? -43.553 5.112 17.242 1.00 19.45 ? 113 GLU A OE1 1 ATOM 857 O OE2 . GLU A 1 113 ? -43.231 6.929 16.052 1.00 23.77 ? 113 GLU A OE2 1 ATOM 858 N N . CYS A 1 114 ? -42.952 5.569 11.524 1.00 15.53 ? 114 CYS A N 1 ATOM 859 C CA . CYS A 1 114 ? -42.155 6.573 10.845 1.00 15.68 ? 114 CYS A CA 1 ATOM 860 C C . CYS A 1 114 ? -41.941 7.574 11.965 1.00 15.70 ? 114 CYS A C 1 ATOM 861 O O . CYS A 1 114 ? -42.743 7.616 12.912 1.00 16.76 ? 114 CYS A O 1 ATOM 862 C CB . CYS A 1 114 ? -42.947 7.260 9.740 1.00 15.51 ? 114 CYS A CB 1 ATOM 863 S SG . CYS A 1 114 ? -43.160 6.324 8.202 1.00 17.58 ? 114 CYS A SG 1 ATOM 864 N N . PRO A 1 115 ? -40.836 8.347 11.922 1.00 15.96 ? 115 PRO A N 1 ATOM 865 C CA . PRO A 1 115 ? -40.592 9.332 12.976 1.00 13.59 ? 115 PRO A CA 1 ATOM 866 C C . PRO A 1 115 ? -41.653 10.411 12.959 1.00 13.90 ? 115 PRO A C 1 ATOM 867 O O . PRO A 1 115 ? -42.149 10.782 11.886 1.00 12.23 ? 115 PRO A O 1 ATOM 868 C CB . PRO A 1 115 ? -39.246 9.921 12.583 1.00 14.06 ? 115 PRO A CB 1 ATOM 869 C CG . PRO A 1 115 ? -38.577 8.817 11.922 1.00 15.54 ? 115 PRO A CG 1 ATOM 870 C CD . PRO A 1 115 ? -39.641 8.219 11.071 1.00 16.04 ? 115 PRO A CD 1 ATOM 871 N N . ILE A 1 116 ? -42.048 10.842 14.157 1.00 10.55 ? 116 ILE A N 1 ATOM 872 C CA . ILE A 1 116 ? -43.022 11.905 14.329 1.00 12.00 ? 116 ILE A CA 1 ATOM 873 C C . ILE A 1 116 ? -42.289 13.166 13.835 1.00 12.80 ? 116 ILE A C 1 ATOM 874 O O . ILE A 1 116 ? -41.188 13.458 14.311 1.00 14.22 ? 116 ILE A O 1 ATOM 875 C CB . ILE A 1 116 ? -43.408 12.059 15.820 1.00 12.56 ? 116 ILE A CB 1 ATOM 876 C CG1 . ILE A 1 116 ? -43.841 10.711 16.397 1.00 12.55 ? 116 ILE A CG1 1 ATOM 877 C CG2 . ILE A 1 116 ? -44.526 13.051 15.968 1.00 8.64 ? 116 ILE A CG2 1 ATOM 878 C CD1 . ILE A 1 116 ? -43.762 10.646 17.902 1.00 13.10 ? 116 ILE A CD1 1 ATOM 879 N N . PRO A 1 117 ? -42.847 13.877 12.829 1.00 13.84 ? 117 PRO A N 1 ATOM 880 C CA . PRO A 1 117 ? -42.198 15.089 12.298 1.00 13.56 ? 117 PRO A CA 1 ATOM 881 C C . PRO A 1 117 ? -42.051 16.258 13.281 1.00 13.71 ? 117 PRO A C 1 ATOM 882 O O . PRO A 1 117 ? -42.779 16.329 14.271 1.00 14.69 ? 117 PRO A O 1 ATOM 883 C CB . PRO A 1 117 ? -43.104 15.459 11.118 1.00 12.99 ? 117 PRO A CB 1 ATOM 884 C CG . PRO A 1 117 ? -44.441 14.962 11.541 1.00 11.54 ? 117 PRO A CG 1 ATOM 885 C CD . PRO A 1 117 ? -44.094 13.605 12.085 1.00 12.95 ? 117 PRO A CD 1 ATOM 886 N N . PRO A 1 118 ? -41.044 17.134 13.075 1.00 14.12 ? 118 PRO A N 1 ATOM 887 C CA . PRO A 1 118 ? -40.865 18.282 13.972 1.00 13.37 ? 118 PRO A CA 1 ATOM 888 C C . PRO A 1 118 ? -41.846 19.413 13.704 1.00 12.05 ? 118 PRO A C 1 ATOM 889 O O . PRO A 1 118 ? -42.772 19.258 12.916 1.00 12.12 ? 118 PRO A O 1 ATOM 890 C CB . PRO A 1 118 ? -39.430 18.705 13.696 1.00 12.59 ? 118 PRO A CB 1 ATOM 891 C CG . PRO A 1 118 ? -39.236 18.343 12.314 1.00 12.57 ? 118 PRO A CG 1 ATOM 892 C CD . PRO A 1 118 ? -39.834 16.967 12.252 1.00 13.62 ? 118 PRO A CD 1 ATOM 893 N N . LYS A 1 119 ? -41.617 20.544 14.375 1.00 14.36 ? 119 LYS A N 1 ATOM 894 C CA . LYS A 1 119 ? -42.422 21.774 14.274 1.00 16.68 ? 119 LYS A CA 1 ATOM 895 C C . LYS A 1 119 ? -43.912 21.614 14.625 1.00 15.79 ? 119 LYS A C 1 ATOM 896 O O . LYS A 1 119 ? -44.778 22.251 14.025 1.00 16.97 ? 119 LYS A O 1 ATOM 897 C CB . LYS A 1 119 ? -42.244 22.455 12.897 1.00 20.98 ? 119 LYS A CB 1 ATOM 898 C CG . LYS A 1 119 ? -40.808 22.839 12.540 1.00 22.05 ? 119 LYS A CG 1 ATOM 899 C CD . LYS A 1 119 ? -40.748 23.456 11.146 1.00 25.01 ? 119 LYS A CD 1 ATOM 900 C CE . LYS A 1 119 ? -39.338 23.438 10.579 1.00 25.69 ? 119 LYS A CE 1 ATOM 901 N NZ . LYS A 1 119 ? -38.360 24.144 11.459 1.00 29.34 ? 119 LYS A NZ 1 ATOM 902 N N . GLY A 1 120 ? -44.193 20.747 15.594 1.00 15.83 ? 120 GLY A N 1 ATOM 903 C CA . GLY A 1 120 ? -45.559 20.527 16.028 1.00 15.40 ? 120 GLY A CA 1 ATOM 904 C C . GLY A 1 120 ? -46.176 19.189 15.691 1.00 14.43 ? 120 GLY A C 1 ATOM 905 O O . GLY A 1 120 ? -47.387 19.034 15.829 1.00 16.90 ? 120 GLY A O 1 ATOM 906 N N . GLY A 1 121 ? -45.358 18.228 15.258 1.00 16.67 ? 121 GLY A N 1 ATOM 907 C CA . GLY A 1 121 ? -45.852 16.894 14.921 1.00 16.64 ? 121 GLY A CA 1 ATOM 908 C C . GLY A 1 121 ? -46.242 16.119 16.169 1.00 17.44 ? 121 GLY A C 1 ATOM 909 O O . GLY A 1 121 ? -45.553 16.205 17.184 1.00 16.02 ? 121 GLY A O 1 ATOM 910 N N . GLN A 1 122 ? -47.359 15.399 16.113 1.00 17.93 ? 122 GLN A N 1 ATOM 911 C CA . GLN A 1 122 ? -47.815 14.634 17.260 1.00 18.58 ? 122 GLN A CA 1 ATOM 912 C C . GLN A 1 122 ? -48.250 13.211 16.990 1.00 18.65 ? 122 GLN A C 1 ATOM 913 O O . GLN A 1 122 ? -48.441 12.808 15.844 1.00 20.51 ? 122 GLN A O 1 ATOM 914 C CB . GLN A 1 122 ? -48.883 15.394 18.066 1.00 20.39 ? 122 GLN A CB 1 ATOM 915 C CG . GLN A 1 122 ? -50.065 15.968 17.302 1.00 22.85 ? 122 GLN A CG 1 ATOM 916 C CD . GLN A 1 122 ? -51.056 16.681 18.222 1.00 23.69 ? 122 GLN A CD 1 ATOM 917 O OE1 . GLN A 1 122 ? -51.927 16.048 18.825 1.00 23.90 ? 122 GLN A OE1 1 ATOM 918 N NE2 . GLN A 1 122 ? -50.927 17.999 18.330 1.00 25.02 ? 122 GLN A NE2 1 ATOM 919 N N . ARG A 1 123 ? -48.298 12.436 18.069 1.00 18.04 ? 123 ARG A N 1 ATOM 920 C CA . ARG A 1 123 ? -48.717 11.038 18.056 1.00 17.08 ? 123 ARG A CA 1 ATOM 921 C C . ARG A 1 123 ? -48.966 10.617 19.495 1.00 16.43 ? 123 ARG A C 1 ATOM 922 O O . ARG A 1 123 ? -48.238 11.006 20.405 1.00 16.39 ? 123 ARG A O 1 ATOM 923 C CB . ARG A 1 123 ? -47.646 10.126 17.448 1.00 16.68 ? 123 ARG A CB 1 ATOM 924 C CG . ARG A 1 123 ? -48.137 8.731 17.160 1.00 16.01 ? 123 ARG A CG 1 ATOM 925 C CD . ARG A 1 123 ? -47.337 7.684 17.900 1.00 17.69 ? 123 ARG A CD 1 ATOM 926 N NE . ARG A 1 123 ? -48.077 6.428 18.027 1.00 18.01 ? 123 ARG A NE 1 ATOM 927 C CZ . ARG A 1 123 ? -47.617 5.236 17.653 1.00 17.10 ? 123 ARG A CZ 1 ATOM 928 N NH1 . ARG A 1 123 ? -46.407 5.120 17.122 1.00 15.77 ? 123 ARG A NH1 1 ATOM 929 N NH2 . ARG A 1 123 ? -48.374 4.156 17.809 1.00 16.66 ? 123 ARG A NH2 1 ATOM 930 N N . THR A 1 124 ? -49.992 9.801 19.686 1.00 16.86 ? 124 THR A N 1 ATOM 931 C CA . THR A 1 124 ? -50.318 9.315 21.007 1.00 16.39 ? 124 THR A CA 1 ATOM 932 C C . THR A 1 124 ? -50.041 7.818 21.103 1.00 15.66 ? 124 THR A C 1 ATOM 933 O O . THR A 1 124 ? -50.440 7.039 20.235 1.00 16.12 ? 124 THR A O 1 ATOM 934 C CB . THR A 1 124 ? -51.771 9.674 21.400 1.00 16.81 ? 124 THR A CB 1 ATOM 935 O OG1 . THR A 1 124 ? -51.962 11.087 21.255 1.00 14.43 ? 124 THR A OG1 1 ATOM 936 C CG2 . THR A 1 124 ? -52.038 9.327 22.855 1.00 17.73 ? 124 THR A CG2 1 ATOM 937 N N . TYR A 1 125 ? -49.270 7.462 22.125 1.00 14.71 ? 125 TYR A N 1 ATOM 938 C CA . TYR A 1 125 ? -48.899 6.086 22.416 1.00 16.24 ? 125 TYR A CA 1 ATOM 939 C C . TYR A 1 125 ? -49.811 5.614 23.529 1.00 17.14 ? 125 TYR A C 1 ATOM 940 O O . TYR A 1 125 ? -50.076 6.367 24.465 1.00 17.66 ? 125 TYR A O 1 ATOM 941 C CB . TYR A 1 125 ? -47.456 6.002 22.906 1.00 15.59 ? 125 TYR A CB 1 ATOM 942 C CG . TYR A 1 125 ? -46.400 6.299 21.871 1.00 15.87 ? 125 TYR A CG 1 ATOM 943 C CD1 . TYR A 1 125 ? -45.909 7.609 21.693 1.00 15.05 ? 125 TYR A CD1 1 ATOM 944 C CD2 . TYR A 1 125 ? -45.838 5.265 21.096 1.00 15.62 ? 125 TYR A CD2 1 ATOM 945 C CE1 . TYR A 1 125 ? -44.871 7.883 20.763 1.00 12.40 ? 125 TYR A CE1 1 ATOM 946 C CE2 . TYR A 1 125 ? -44.800 5.526 20.162 1.00 12.99 ? 125 TYR A CE2 1 ATOM 947 C CZ . TYR A 1 125 ? -44.328 6.839 20.005 1.00 13.44 ? 125 TYR A CZ 1 ATOM 948 O OH . TYR A 1 125 ? -43.361 7.118 19.077 1.00 8.43 ? 125 TYR A OH 1 ATOM 949 N N . ARG A 1 126 ? -50.295 4.380 23.408 1.00 17.55 ? 126 ARG A N 1 ATOM 950 C CA . ARG A 1 126 ? -51.189 3.775 24.389 1.00 18.47 ? 126 ARG A CA 1 ATOM 951 C C . ARG A 1 126 ? -50.799 2.308 24.550 1.00 19.97 ? 126 ARG A C 1 ATOM 952 O O . ARG A 1 126 ? -50.755 1.550 23.564 1.00 19.86 ? 126 ARG A O 1 ATOM 953 C CB . ARG A 1 126 ? -52.657 3.918 23.942 1.00 19.14 ? 126 ARG A CB 1 ATOM 954 C CG . ARG A 1 126 ? -53.682 3.347 24.924 1.00 21.22 ? 126 ARG A CG 1 ATOM 955 C CD . ARG A 1 126 ? -55.122 3.543 24.466 1.00 23.07 ? 126 ARG A CD 1 ATOM 956 N NE . ARG A 1 126 ? -56.115 2.806 25.265 1.00 22.64 ? 126 ARG A NE 1 ATOM 957 C CZ . ARG A 1 126 ? -56.571 3.171 26.467 1.00 23.99 ? 126 ARG A CZ 1 ATOM 958 N NH1 . ARG A 1 126 ? -56.134 4.277 27.064 1.00 21.95 ? 126 ARG A NH1 1 ATOM 959 N NH2 . ARG A 1 126 ? -57.486 2.428 27.076 1.00 22.00 ? 126 ARG A NH2 1 ATOM 960 N N . TRP A 1 127 ? -50.459 1.935 25.787 1.00 19.28 ? 127 TRP A N 1 ATOM 961 C CA . TRP A 1 127 ? -50.052 0.569 26.117 1.00 20.74 ? 127 TRP A CA 1 ATOM 962 C C . TRP A 1 127 ? -50.467 0.135 27.516 1.00 21.50 ? 127 TRP A C 1 ATOM 963 O O . TRP A 1 127 ? -50.445 0.930 28.458 1.00 22.33 ? 127 TRP A O 1 ATOM 964 C CB . TRP A 1 127 ? -48.533 0.361 25.924 1.00 22.27 ? 127 TRP A CB 1 ATOM 965 C CG . TRP A 1 127 ? -47.625 1.434 26.496 1.00 23.42 ? 127 TRP A CG 1 ATOM 966 C CD1 . TRP A 1 127 ? -47.161 2.548 25.841 1.00 22.69 ? 127 TRP A CD1 1 ATOM 967 C CD2 . TRP A 1 127 ? -47.038 1.468 27.811 1.00 23.09 ? 127 TRP A CD2 1 ATOM 968 N NE1 . TRP A 1 127 ? -46.323 3.267 26.662 1.00 23.60 ? 127 TRP A NE1 1 ATOM 969 C CE2 . TRP A 1 127 ? -46.225 2.634 27.875 1.00 22.20 ? 127 TRP A CE2 1 ATOM 970 C CE3 . TRP A 1 127 ? -47.116 0.628 28.946 1.00 23.70 ? 127 TRP A CE3 1 ATOM 971 C CZ2 . TRP A 1 127 ? -45.485 2.987 29.037 1.00 21.44 ? 127 TRP A CZ2 1 ATOM 972 C CZ3 . TRP A 1 127 ? -46.373 0.981 30.116 1.00 21.64 ? 127 TRP A CZ3 1 ATOM 973 C CH2 . TRP A 1 127 ? -45.570 2.154 30.140 1.00 21.57 ? 127 TRP A CH2 1 ATOM 974 N N . ARG A 1 128 ? -50.805 -1.145 27.639 1.00 20.47 ? 128 ARG A N 1 ATOM 975 C CA . ARG A 1 128 ? -51.242 -1.729 28.896 1.00 19.45 ? 128 ARG A CA 1 ATOM 976 C C . ARG A 1 128 ? -50.055 -2.161 29.764 1.00 20.20 ? 128 ARG A C 1 ATOM 977 O O . ARG A 1 128 ? -49.069 -2.723 29.269 1.00 18.71 ? 128 ARG A O 1 ATOM 978 C CB . ARG A 1 128 ? -52.162 -2.919 28.612 1.00 18.21 ? 128 ARG A CB 1 ATOM 979 C CG . ARG A 1 128 ? -52.883 -3.493 29.833 1.00 18.22 ? 128 ARG A CG 1 ATOM 980 C CD . ARG A 1 128 ? -54.221 -2.819 30.125 1.00 17.36 ? 128 ARG A CD 1 ATOM 981 N NE . ARG A 1 128 ? -54.959 -3.552 31.159 1.00 17.99 ? 128 ARG A NE 1 ATOM 982 C CZ . ARG A 1 128 ? -55.612 -4.696 30.963 1.00 15.27 ? 128 ARG A CZ 1 ATOM 983 N NH1 . ARG A 1 128 ? -55.654 -5.252 29.761 1.00 17.20 ? 128 ARG A NH1 1 ATOM 984 N NH2 . ARG A 1 128 ? -56.140 -5.340 31.992 1.00 14.55 ? 128 ARG A NH2 1 ATOM 985 N N . ALA A 1 129 ? -50.180 -1.895 31.064 1.00 20.13 ? 129 ALA A N 1 ATOM 986 C CA . ALA A 1 129 ? -49.167 -2.244 32.060 1.00 20.44 ? 129 ALA A CA 1 ATOM 987 C C . ALA A 1 129 ? -49.314 -3.710 32.472 1.00 19.75 ? 129 ALA A C 1 ATOM 988 O O . ALA A 1 129 ? -49.797 -4.026 33.562 1.00 21.03 ? 129 ALA A O 1 ATOM 989 C CB . ALA A 1 129 ? -49.290 -1.321 33.272 1.00 19.56 ? 129 ALA A CB 1 ATOM 990 N N . ARG A 1 130 ? -48.885 -4.594 31.574 1.00 20.26 ? 130 ARG A N 1 ATOM 991 C CA . ARG A 1 130 ? -48.949 -6.045 31.765 1.00 21.22 ? 130 ARG A CA 1 ATOM 992 C C . ARG A 1 130 ? -47.784 -6.584 32.589 1.00 20.81 ? 130 ARG A C 1 ATOM 993 O O . ARG A 1 130 ? -47.723 -7.775 32.896 1.00 21.65 ? 130 ARG A O 1 ATOM 994 C CB . ARG A 1 130 ? -48.972 -6.765 30.405 1.00 21.88 ? 130 ARG A CB 1 ATOM 995 C CG . ARG A 1 130 ? -50.159 -6.444 29.522 1.00 20.63 ? 130 ARG A CG 1 ATOM 996 C CD . ARG A 1 130 ? -50.478 -7.608 28.590 1.00 21.59 ? 130 ARG A CD 1 ATOM 997 N NE . ARG A 1 130 ? -51.575 -7.301 27.673 1.00 20.59 ? 130 ARG A NE 1 ATOM 998 C CZ . ARG A 1 130 ? -52.872 -7.412 27.966 1.00 23.73 ? 130 ARG A CZ 1 ATOM 999 N NH1 . ARG A 1 130 ? -53.264 -7.836 29.165 1.00 23.39 ? 130 ARG A NH1 1 ATOM 1000 N NH2 . ARG A 1 130 ? -53.786 -7.053 27.071 1.00 21.55 ? 130 ARG A NH2 1 ATOM 1001 N N . GLN A 1 131 ? -46.866 -5.695 32.941 1.00 19.98 ? 131 GLN A N 1 ATOM 1002 C CA . GLN A 1 131 ? -45.689 -6.056 33.703 1.00 19.59 ? 131 GLN A CA 1 ATOM 1003 C C . GLN A 1 131 ? -45.488 -5.014 34.776 1.00 17.35 ? 131 GLN A C 1 ATOM 1004 O O . GLN A 1 131 ? -45.806 -3.849 34.567 1.00 19.40 ? 131 GLN A O 1 ATOM 1005 C CB . GLN A 1 131 ? -44.500 -6.061 32.760 1.00 21.82 ? 131 GLN A CB 1 ATOM 1006 C CG . GLN A 1 131 ? -43.466 -7.110 33.041 1.00 24.50 ? 131 GLN A CG 1 ATOM 1007 C CD . GLN A 1 131 ? -42.476 -7.261 31.900 1.00 29.15 ? 131 GLN A CD 1 ATOM 1008 O OE1 . GLN A 1 131 ? -42.644 -6.679 30.817 1.00 29.97 ? 131 GLN A OE1 1 ATOM 1009 N NE2 . GLN A 1 131 ? -41.437 -8.054 32.130 1.00 27.80 ? 131 GLN A NE2 1 ATOM 1010 N N . TYR A 1 132 ? -44.973 -5.439 35.925 1.00 15.84 ? 132 TYR A N 1 ATOM 1011 C CA . TYR A 1 132 ? -44.717 -4.530 37.045 1.00 13.43 ? 132 TYR A CA 1 ATOM 1012 C C . TYR A 1 132 ? -43.232 -4.498 37.425 1.00 13.27 ? 132 TYR A C 1 ATOM 1013 O O . TYR A 1 132 ? -42.532 -5.512 37.325 1.00 11.12 ? 132 TYR A O 1 ATOM 1014 C CB . TYR A 1 132 ? -45.600 -4.873 38.255 1.00 15.82 ? 132 TYR A CB 1 ATOM 1015 C CG . TYR A 1 132 ? -45.452 -6.291 38.784 1.00 19.66 ? 132 TYR A CG 1 ATOM 1016 C CD1 . TYR A 1 132 ? -46.204 -7.348 38.231 1.00 18.85 ? 132 TYR A CD1 1 ATOM 1017 C CD2 . TYR A 1 132 ? -44.515 -6.600 39.798 1.00 19.40 ? 132 TYR A CD2 1 ATOM 1018 C CE1 . TYR A 1 132 ? -46.025 -8.685 38.666 1.00 20.03 ? 132 TYR A CE1 1 ATOM 1019 C CE2 . TYR A 1 132 ? -44.327 -7.933 40.234 1.00 19.41 ? 132 TYR A CE2 1 ATOM 1020 C CZ . TYR A 1 132 ? -45.084 -8.966 39.661 1.00 19.51 ? 132 TYR A CZ 1 ATOM 1021 O OH . TYR A 1 132 ? -44.890 -10.265 40.060 1.00 21.86 ? 132 TYR A OH 1 ATOM 1022 N N . GLY A 1 133 ? -42.771 -3.339 37.883 1.00 10.34 ? 133 GLY A N 1 ATOM 1023 C CA . GLY A 1 133 ? -41.382 -3.186 38.255 1.00 12.12 ? 133 GLY A CA 1 ATOM 1024 C C . GLY A 1 133 ? -40.847 -1.894 37.686 1.00 13.46 ? 133 GLY A C 1 ATOM 1025 O O . GLY A 1 133 ? -41.616 -0.989 37.355 1.00 14.11 ? 133 GLY A O 1 ATOM 1026 N N . THR A 1 134 ? -39.532 -1.811 37.546 1.00 13.54 ? 134 THR A N 1 ATOM 1027 C CA . THR A 1 134 ? -38.927 -0.601 37.027 1.00 14.78 ? 134 THR A CA 1 ATOM 1028 C C . THR A 1 134 ? -38.467 -0.759 35.591 1.00 15.23 ? 134 THR A C 1 ATOM 1029 O O . THR A 1 134 ? -38.000 -1.817 35.183 1.00 17.97 ? 134 THR A O 1 ATOM 1030 C CB . THR A 1 134 ? -37.748 -0.159 37.896 1.00 14.54 ? 134 THR A CB 1 ATOM 1031 O OG1 . THR A 1 134 ? -38.097 -0.323 39.273 1.00 15.03 ? 134 THR A OG1 1 ATOM 1032 C CG2 . THR A 1 134 ? -37.417 1.310 37.652 1.00 16.78 ? 134 THR A CG2 1 ATOM 1033 N N . SER A 1 135 ? -38.656 0.310 34.831 1.00 15.89 ? 135 SER A N 1 ATOM 1034 C CA . SER A 1 135 ? -38.251 0.388 33.437 1.00 16.23 ? 135 SER A CA 1 ATOM 1035 C C . SER A 1 135 ? -37.949 1.839 33.097 1.00 15.24 ? 135 SER A C 1 ATOM 1036 O O . SER A 1 135 ? -37.860 2.682 33.990 1.00 17.53 ? 135 SER A O 1 ATOM 1037 C CB . SER A 1 135 ? -39.333 -0.175 32.524 1.00 14.37 ? 135 SER A CB 1 ATOM 1038 O OG . SER A 1 135 ? -38.982 -1.478 32.107 1.00 15.20 ? 135 SER A OG 1 ATOM 1039 N N . TRP A 1 136 ? -37.760 2.119 31.812 1.00 15.53 ? 136 TRP A N 1 ATOM 1040 C CA . TRP A 1 136 ? -37.469 3.468 31.343 1.00 14.26 ? 136 TRP A CA 1 ATOM 1041 C C . TRP A 1 136 ? -37.938 3.680 29.917 1.00 14.68 ? 136 TRP A C 1 ATOM 1042 O O . TRP A 1 136 ? -38.342 2.738 29.236 1.00 15.80 ? 136 TRP A O 1 ATOM 1043 C CB . TRP A 1 136 ? -35.965 3.796 31.468 1.00 13.35 ? 136 TRP A CB 1 ATOM 1044 C CG . TRP A 1 136 ? -35.009 2.955 30.644 1.00 13.19 ? 136 TRP A CG 1 ATOM 1045 C CD1 . TRP A 1 136 ? -34.852 1.597 30.689 1.00 13.43 ? 136 TRP A CD1 1 ATOM 1046 C CD2 . TRP A 1 136 ? -34.034 3.437 29.716 1.00 12.44 ? 136 TRP A CD2 1 ATOM 1047 N NE1 . TRP A 1 136 ? -33.834 1.203 29.854 1.00 13.68 ? 136 TRP A NE1 1 ATOM 1048 C CE2 . TRP A 1 136 ? -33.310 2.311 29.242 1.00 12.71 ? 136 TRP A CE2 1 ATOM 1049 C CE3 . TRP A 1 136 ? -33.688 4.717 29.240 1.00 13.51 ? 136 TRP A CE3 1 ATOM 1050 C CZ2 . TRP A 1 136 ? -32.247 2.425 28.309 1.00 9.73 ? 136 TRP A CZ2 1 ATOM 1051 C CZ3 . TRP A 1 136 ? -32.616 4.836 28.306 1.00 12.90 ? 136 TRP A CZ3 1 ATOM 1052 C CH2 . TRP A 1 136 ? -31.914 3.688 27.860 1.00 9.86 ? 136 TRP A CH2 1 ATOM 1053 N N . TYR A 1 137 ? -37.928 4.936 29.493 1.00 13.66 ? 137 TYR A N 1 ATOM 1054 C CA . TYR A 1 137 ? -38.308 5.277 28.138 1.00 12.50 ? 137 TYR A CA 1 ATOM 1055 C C . TYR A 1 137 ? -37.267 6.216 27.549 1.00 13.27 ? 137 TYR A C 1 ATOM 1056 O O . TYR A 1 137 ? -36.618 6.972 28.280 1.00 10.04 ? 137 TYR A O 1 ATOM 1057 C CB . TYR A 1 137 ? -39.732 5.865 28.068 1.00 9.58 ? 137 TYR A CB 1 ATOM 1058 C CG . TYR A 1 137 ? -39.977 7.149 28.829 1.00 10.68 ? 137 TYR A CG 1 ATOM 1059 C CD1 . TYR A 1 137 ? -39.627 8.398 28.277 1.00 12.24 ? 137 TYR A CD1 1 ATOM 1060 C CD2 . TYR A 1 137 ? -40.555 7.131 30.113 1.00 10.11 ? 137 TYR A CD2 1 ATOM 1061 C CE1 . TYR A 1 137 ? -39.836 9.595 28.985 1.00 11.43 ? 137 TYR A CE1 1 ATOM 1062 C CE2 . TYR A 1 137 ? -40.782 8.327 30.831 1.00 10.66 ? 137 TYR A CE2 1 ATOM 1063 C CZ . TYR A 1 137 ? -40.415 9.549 30.254 1.00 11.39 ? 137 TYR A CZ 1 ATOM 1064 O OH . TYR A 1 137 ? -40.602 10.721 30.923 1.00 12.48 ? 137 TYR A OH 1 ATOM 1065 N N . HIS A 1 138 ? -37.120 6.166 26.229 1.00 13.22 ? 138 HIS A N 1 ATOM 1066 C CA . HIS A 1 138 ? -36.159 7.014 25.537 1.00 15.04 ? 138 HIS A CA 1 ATOM 1067 C C . HIS A 1 138 ? -36.473 7.130 24.047 1.00 14.64 ? 138 HIS A C 1 ATOM 1068 O O . HIS A 1 138 ? -37.229 6.326 23.506 1.00 16.27 ? 138 HIS A O 1 ATOM 1069 C CB . HIS A 1 138 ? -34.734 6.474 25.747 1.00 15.94 ? 138 HIS A CB 1 ATOM 1070 C CG . HIS A 1 138 ? -34.478 5.150 25.095 1.00 20.74 ? 138 HIS A CG 1 ATOM 1071 N ND1 . HIS A 1 138 ? -33.913 5.044 23.844 1.00 20.84 ? 138 HIS A ND1 1 ATOM 1072 C CD2 . HIS A 1 138 ? -34.736 3.884 25.503 1.00 18.61 ? 138 HIS A CD2 1 ATOM 1073 C CE1 . HIS A 1 138 ? -33.832 3.772 23.508 1.00 20.85 ? 138 HIS A CE1 1 ATOM 1074 N NE2 . HIS A 1 138 ? -34.324 3.047 24.497 1.00 20.87 ? 138 HIS A NE2 1 ATOM 1075 N N . SER A 1 139 ? -35.860 8.115 23.394 1.00 14.80 ? 139 SER A N 1 ATOM 1076 C CA . SER A 1 139 ? -36.026 8.347 21.957 1.00 13.94 ? 139 SER A CA 1 ATOM 1077 C C . SER A 1 139 ? -35.355 7.234 21.169 1.00 14.70 ? 139 SER A C 1 ATOM 1078 O O . SER A 1 139 ? -34.400 6.620 21.653 1.00 13.57 ? 139 SER A O 1 ATOM 1079 C CB . SER A 1 139 ? -35.399 9.686 21.561 1.00 12.42 ? 139 SER A CB 1 ATOM 1080 O OG . SER A 1 139 ? -35.457 9.920 20.167 1.00 9.94 ? 139 SER A OG 1 ATOM 1081 N N . HIS A 1 140 ? -35.889 6.949 19.981 1.00 16.34 ? 140 HIS A N 1 ATOM 1082 C CA . HIS A 1 140 ? -35.310 5.920 19.129 1.00 17.24 ? 140 HIS A CA 1 ATOM 1083 C C . HIS A 1 140 ? -34.893 6.444 17.767 1.00 17.73 ? 140 HIS A C 1 ATOM 1084 O O . HIS A 1 140 ? -34.665 5.686 16.815 1.00 20.33 ? 140 HIS A O 1 ATOM 1085 C CB . HIS A 1 140 ? -36.213 4.698 19.022 1.00 17.26 ? 140 HIS A CB 1 ATOM 1086 C CG . HIS A 1 140 ? -35.467 3.415 19.180 1.00 17.29 ? 140 HIS A CG 1 ATOM 1087 N ND1 . HIS A 1 140 ? -34.710 2.873 18.167 1.00 16.25 ? 140 HIS A ND1 1 ATOM 1088 C CD2 . HIS A 1 140 ? -35.251 2.640 20.268 1.00 17.72 ? 140 HIS A CD2 1 ATOM 1089 C CE1 . HIS A 1 140 ? -34.051 1.825 18.626 1.00 20.10 ? 140 HIS A CE1 1 ATOM 1090 N NE2 . HIS A 1 140 ? -34.362 1.663 19.899 1.00 17.25 ? 140 HIS A NE2 1 ATOM 1091 N N . PHE A 1 141 ? -34.730 7.760 17.715 1.00 18.10 ? 141 PHE A N 1 ATOM 1092 C CA . PHE A 1 141 ? -34.308 8.457 16.513 1.00 16.50 ? 141 PHE A CA 1 ATOM 1093 C C . PHE A 1 141 ? -32.787 8.576 16.645 1.00 15.99 ? 141 PHE A C 1 ATOM 1094 O O . PHE A 1 141 ? -32.271 9.578 17.137 1.00 17.34 ? 141 PHE A O 1 ATOM 1095 C CB . PHE A 1 141 ? -34.995 9.831 16.458 1.00 13.88 ? 141 PHE A CB 1 ATOM 1096 C CG . PHE A 1 141 ? -34.831 10.539 15.147 1.00 11.33 ? 141 PHE A CG 1 ATOM 1097 C CD1 . PHE A 1 141 ? -35.620 10.185 14.046 1.00 6.45 ? 141 PHE A CD1 1 ATOM 1098 C CD2 . PHE A 1 141 ? -33.894 11.582 15.009 1.00 10.74 ? 141 PHE A CD2 1 ATOM 1099 C CE1 . PHE A 1 141 ? -35.483 10.865 12.816 1.00 9.68 ? 141 PHE A CE1 1 ATOM 1100 C CE2 . PHE A 1 141 ? -33.746 12.270 13.783 1.00 11.21 ? 141 PHE A CE2 1 ATOM 1101 C CZ . PHE A 1 141 ? -34.541 11.913 12.687 1.00 7.44 ? 141 PHE A CZ 1 ATOM 1102 N N . SER A 1 142 ? -32.086 7.525 16.213 1.00 14.84 ? 142 SER A N 1 ATOM 1103 C CA . SER A 1 142 ? -30.626 7.419 16.295 1.00 12.74 ? 142 SER A CA 1 ATOM 1104 C C . SER A 1 142 ? -30.202 7.497 17.765 1.00 10.56 ? 142 SER A C 1 ATOM 1105 O O . SER A 1 142 ? -30.782 6.808 18.601 1.00 10.44 ? 142 SER A O 1 ATOM 1106 C CB . SER A 1 142 ? -29.917 8.477 15.435 1.00 15.54 ? 142 SER A CB 1 ATOM 1107 O OG . SER A 1 142 ? -30.288 8.353 14.080 1.00 21.11 ? 142 SER A OG 1 ATOM 1108 N N . ALA A 1 143 ? -29.245 8.363 18.085 1.00 9.69 ? 143 ALA A N 1 ATOM 1109 C CA . ALA A 1 143 ? -28.770 8.506 19.459 1.00 10.20 ? 143 ALA A CA 1 ATOM 1110 C C . ALA A 1 143 ? -29.357 9.744 20.130 1.00 10.34 ? 143 ALA A C 1 ATOM 1111 O O . ALA A 1 143 ? -28.860 10.174 21.165 1.00 9.76 ? 143 ALA A O 1 ATOM 1112 C CB . ALA A 1 143 ? -27.240 8.539 19.491 1.00 7.99 ? 143 ALA A CB 1 ATOM 1113 N N . GLN A 1 144 ? -30.469 10.251 19.579 1.00 12.56 ? 144 GLN A N 1 ATOM 1114 C CA . GLN A 1 144 ? -31.179 11.442 20.081 1.00 11.77 ? 144 GLN A CA 1 ATOM 1115 C C . GLN A 1 144 ? -31.403 11.468 21.597 1.00 10.51 ? 144 GLN A C 1 ATOM 1116 O O . GLN A 1 144 ? -31.331 12.532 22.214 1.00 11.57 ? 144 GLN A O 1 ATOM 1117 C CB . GLN A 1 144 ? -32.520 11.599 19.366 1.00 12.47 ? 144 GLN A CB 1 ATOM 1118 C CG . GLN A 1 144 ? -33.249 12.903 19.638 1.00 13.88 ? 144 GLN A CG 1 ATOM 1119 C CD . GLN A 1 144 ? -34.596 12.960 18.980 1.00 14.74 ? 144 GLN A CD 1 ATOM 1120 O OE1 . GLN A 1 144 ? -35.615 12.602 19.575 1.00 15.24 ? 144 GLN A OE1 1 ATOM 1121 N NE2 . GLN A 1 144 ? -34.615 13.410 17.740 1.00 17.08 ? 144 GLN A NE2 1 ATOM 1122 N N . TYR A 1 145 ? -31.593 10.286 22.190 1.00 8.98 ? 145 TYR A N 1 ATOM 1123 C CA . TYR A 1 145 ? -31.804 10.149 23.630 1.00 6.36 ? 145 TYR A CA 1 ATOM 1124 C C . TYR A 1 145 ? -30.567 10.600 24.425 1.00 7.27 ? 145 TYR A C 1 ATOM 1125 O O . TYR A 1 145 ? -30.665 10.928 25.608 1.00 9.08 ? 145 TYR A O 1 ATOM 1126 C CB . TYR A 1 145 ? -32.288 8.724 23.986 1.00 4.04 ? 145 TYR A CB 1 ATOM 1127 C CG . TYR A 1 145 ? -31.252 7.629 24.268 1.00 3.32 ? 145 TYR A CG 1 ATOM 1128 C CD1 . TYR A 1 145 ? -30.788 7.386 25.595 1.00 1.77 ? 145 TYR A CD1 1 ATOM 1129 C CD2 . TYR A 1 145 ? -30.789 6.783 23.237 1.00 2.39 ? 145 TYR A CD2 1 ATOM 1130 C CE1 . TYR A 1 145 ? -29.890 6.317 25.881 1.00 1.93 ? 145 TYR A CE1 1 ATOM 1131 C CE2 . TYR A 1 145 ? -29.889 5.701 23.510 1.00 1.00 ? 145 TYR A CE2 1 ATOM 1132 C CZ . TYR A 1 145 ? -29.453 5.480 24.833 1.00 3.12 ? 145 TYR A CZ 1 ATOM 1133 O OH . TYR A 1 145 ? -28.618 4.419 25.109 1.00 3.04 ? 145 TYR A OH 1 ATOM 1134 N N . GLY A 1 146 ? -29.433 10.670 23.728 1.00 5.74 ? 146 GLY A N 1 ATOM 1135 C CA . GLY A 1 146 ? -28.182 11.132 24.308 1.00 8.20 ? 146 GLY A CA 1 ATOM 1136 C C . GLY A 1 146 ? -28.172 12.629 24.586 1.00 9.29 ? 146 GLY A C 1 ATOM 1137 O O . GLY A 1 146 ? -27.327 13.114 25.337 1.00 10.09 ? 146 GLY A O 1 ATOM 1138 N N . ASN A 1 147 ? -29.137 13.341 23.998 1.00 10.84 ? 147 ASN A N 1 ATOM 1139 C CA . ASN A 1 147 ? -29.303 14.783 24.179 1.00 12.62 ? 147 ASN A CA 1 ATOM 1140 C C . ASN A 1 147 ? -30.262 15.085 25.325 1.00 14.06 ? 147 ASN A C 1 ATOM 1141 O O . ASN A 1 147 ? -30.468 16.246 25.661 1.00 14.25 ? 147 ASN A O 1 ATOM 1142 C CB . ASN A 1 147 ? -29.811 15.452 22.894 1.00 11.83 ? 147 ASN A CB 1 ATOM 1143 C CG . ASN A 1 147 ? -28.801 15.405 21.768 1.00 12.11 ? 147 ASN A CG 1 ATOM 1144 O OD1 . ASN A 1 147 ? -27.603 15.585 21.982 1.00 10.69 ? 147 ASN A OD1 1 ATOM 1145 N ND2 . ASN A 1 147 ? -29.281 15.158 20.555 1.00 12.54 ? 147 ASN A ND2 1 ATOM 1146 N N . GLY A 1 148 ? -30.888 14.040 25.872 1.00 14.89 ? 148 GLY A N 1 ATOM 1147 C CA . GLY A 1 148 ? -31.789 14.218 26.997 1.00 16.91 ? 148 GLY A CA 1 ATOM 1148 C C . GLY A 1 148 ? -33.234 13.779 26.875 1.00 17.56 ? 148 GLY A C 1 ATOM 1149 O O . GLY A 1 148 ? -34.028 14.077 27.769 1.00 17.39 ? 148 GLY A O 1 ATOM 1150 N N . VAL A 1 149 ? -33.586 13.083 25.793 1.00 18.48 ? 149 VAL A N 1 ATOM 1151 C CA . VAL A 1 149 ? -34.962 12.609 25.589 1.00 18.32 ? 149 VAL A CA 1 ATOM 1152 C C . VAL A 1 149 ? -35.101 11.235 26.261 1.00 17.98 ? 149 VAL A C 1 ATOM 1153 O O . VAL A 1 149 ? -35.283 10.204 25.613 1.00 17.08 ? 149 VAL A O 1 ATOM 1154 C CB . VAL A 1 149 ? -35.342 12.535 24.084 1.00 19.34 ? 149 VAL A CB 1 ATOM 1155 C CG1 . VAL A 1 149 ? -36.837 12.664 23.910 1.00 19.71 ? 149 VAL A CG1 1 ATOM 1156 C CG2 . VAL A 1 149 ? -34.640 13.599 23.285 1.00 20.72 ? 149 VAL A CG2 1 ATOM 1157 N N . VAL A 1 150 ? -34.931 11.252 27.582 1.00 19.44 ? 150 VAL A N 1 ATOM 1158 C CA . VAL A 1 150 ? -34.983 10.074 28.438 1.00 19.55 ? 150 VAL A CA 1 ATOM 1159 C C . VAL A 1 150 ? -35.925 10.340 29.616 1.00 19.49 ? 150 VAL A C 1 ATOM 1160 O O . VAL A 1 150 ? -36.256 11.488 29.925 1.00 19.77 ? 150 VAL A O 1 ATOM 1161 C CB . VAL A 1 150 ? -33.572 9.737 29.049 1.00 20.83 ? 150 VAL A CB 1 ATOM 1162 C CG1 . VAL A 1 150 ? -33.563 8.346 29.641 1.00 22.54 ? 150 VAL A CG1 1 ATOM 1163 C CG2 . VAL A 1 150 ? -32.469 9.839 28.023 1.00 20.83 ? 150 VAL A CG2 1 ATOM 1164 N N . GLY A 1 151 ? -36.298 9.256 30.288 1.00 18.22 ? 151 GLY A N 1 ATOM 1165 C CA . GLY A 1 151 ? -37.155 9.311 31.450 1.00 15.93 ? 151 GLY A CA 1 ATOM 1166 C C . GLY A 1 151 ? -37.362 7.913 31.992 1.00 15.22 ? 151 GLY A C 1 ATOM 1167 O O . GLY A 1 151 ? -37.037 6.928 31.327 1.00 14.41 ? 151 GLY A O 1 ATOM 1168 N N . THR A 1 152 ? -37.974 7.840 33.172 1.00 13.36 ? 152 THR A N 1 ATOM 1169 C CA . THR A 1 152 ? -38.227 6.583 33.862 1.00 10.86 ? 152 THR A CA 1 ATOM 1170 C C . THR A 1 152 ? -39.696 6.142 33.911 1.00 10.38 ? 152 THR A C 1 ATOM 1171 O O . THR A 1 152 ? -40.614 6.952 33.772 1.00 8.22 ? 152 THR A O 1 ATOM 1172 C CB . THR A 1 152 ? -37.673 6.637 35.311 1.00 11.96 ? 152 THR A CB 1 ATOM 1173 O OG1 . THR A 1 152 ? -38.391 7.619 36.067 1.00 13.42 ? 152 THR A OG1 1 ATOM 1174 C CG2 . THR A 1 152 ? -36.191 7.007 35.328 1.00 7.60 ? 152 THR A CG2 1 ATOM 1175 N N . ILE A 1 153 ? -39.899 4.832 34.038 1.00 10.45 ? 153 ILE A N 1 ATOM 1176 C CA . ILE A 1 153 ? -41.237 4.239 34.149 1.00 11.76 ? 153 ILE A CA 1 ATOM 1177 C C . ILE A 1 153 ? -41.263 3.403 35.435 1.00 9.72 ? 153 ILE A C 1 ATOM 1178 O O . ILE A 1 153 ? -40.340 2.634 35.710 1.00 11.80 ? 153 ILE A O 1 ATOM 1179 C CB . ILE A 1 153 ? -41.608 3.329 32.926 1.00 10.79 ? 153 ILE A CB 1 ATOM 1180 C CG1 . ILE A 1 153 ? -41.715 4.159 31.647 1.00 14.17 ? 153 ILE A CG1 1 ATOM 1181 C CG2 . ILE A 1 153 ? -42.963 2.654 33.152 1.00 17.57 ? 153 ILE A CG2 1 ATOM 1182 C CD1 . ILE A 1 153 ? -41.834 3.380 30.355 1.00 9.04 ? 153 ILE A CD1 1 ATOM 1183 N N . GLN A 1 154 ? -42.309 3.587 36.223 1.00 9.14 ? 154 GLN A N 1 ATOM 1184 C CA . GLN A 1 154 ? -42.487 2.839 37.459 1.00 9.61 ? 154 GLN A CA 1 ATOM 1185 C C . GLN A 1 154 ? -43.915 2.280 37.518 1.00 9.30 ? 154 GLN A C 1 ATOM 1186 O O . GLN A 1 154 ? -44.871 3.014 37.763 1.00 9.10 ? 154 GLN A O 1 ATOM 1187 C CB . GLN A 1 154 ? -42.203 3.723 38.682 1.00 9.20 ? 154 GLN A CB 1 ATOM 1188 C CG . GLN A 1 154 ? -42.249 2.970 40.016 1.00 8.71 ? 154 GLN A CG 1 ATOM 1189 C CD . GLN A 1 154 ? -41.922 3.840 41.212 1.00 14.09 ? 154 GLN A CD 1 ATOM 1190 O OE1 . GLN A 1 154 ? -41.006 4.667 41.168 1.00 15.75 ? 154 GLN A OE1 1 ATOM 1191 N NE2 . GLN A 1 154 ? -42.646 3.629 42.306 1.00 15.02 ? 154 GLN A NE2 1 ATOM 1192 N N . ILE A 1 155 ? -44.055 0.990 37.232 1.00 10.19 ? 155 ILE A N 1 ATOM 1193 C CA . ILE A 1 155 ? -45.358 0.335 37.282 1.00 11.91 ? 155 ILE A CA 1 ATOM 1194 C C . ILE A 1 155 ? -45.393 -0.429 38.605 1.00 13.82 ? 155 ILE A C 1 ATOM 1195 O O . ILE A 1 155 ? -44.680 -1.416 38.783 1.00 14.68 ? 155 ILE A O 1 ATOM 1196 C CB . ILE A 1 155 ? -45.589 -0.632 36.080 1.00 10.65 ? 155 ILE A CB 1 ATOM 1197 C CG1 . ILE A 1 155 ? -45.439 0.091 34.732 1.00 11.78 ? 155 ILE A CG1 1 ATOM 1198 C CG2 . ILE A 1 155 ? -46.945 -1.310 36.197 1.00 11.07 ? 155 ILE A CG2 1 ATOM 1199 C CD1 . ILE A 1 155 ? -46.462 1.190 34.430 1.00 14.10 ? 155 ILE A CD1 1 ATOM 1200 N N . ASN A 1 156 ? -46.189 0.072 39.545 1.00 16.13 ? 156 ASN A N 1 ATOM 1201 C CA . ASN A 1 156 ? -46.318 -0.548 40.858 1.00 17.22 ? 156 ASN A CA 1 ATOM 1202 C C . ASN A 1 156 ? -47.018 -1.890 40.836 1.00 18.10 ? 156 ASN A C 1 ATOM 1203 O O . ASN A 1 156 ? -47.996 -2.088 40.119 1.00 20.14 ? 156 ASN A O 1 ATOM 1204 C CB . ASN A 1 156 ? -47.029 0.378 41.844 1.00 16.10 ? 156 ASN A CB 1 ATOM 1205 C CG . ASN A 1 156 ? -46.132 1.472 42.365 1.00 15.30 ? 156 ASN A CG 1 ATOM 1206 O OD1 . ASN A 1 156 ? -44.954 1.244 42.669 1.00 14.10 ? 156 ASN A OD1 1 ATOM 1207 N ND2 . ASN A 1 156 ? -46.685 2.673 42.482 1.00 14.73 ? 156 ASN A ND2 1 ATOM 1208 N N . GLY A 1 157 ? -46.482 -2.801 41.637 1.00 19.01 ? 157 GLY A N 1 ATOM 1209 C CA . GLY A 1 157 ? -47.017 -4.138 41.759 1.00 18.09 ? 157 GLY A CA 1 ATOM 1210 C C . GLY A 1 157 ? -46.395 -4.776 42.980 1.00 17.57 ? 157 GLY A C 1 ATOM 1211 O O . GLY A 1 157 ? -45.782 -4.065 43.778 1.00 18.69 ? 157 GLY A O 1 ATOM 1212 N N . PRO A 1 158 ? -46.554 -6.098 43.182 1.00 16.24 ? 158 PRO A N 1 ATOM 1213 C CA . PRO A 1 158 ? -45.974 -6.789 44.341 1.00 16.79 ? 158 PRO A CA 1 ATOM 1214 C C . PRO A 1 158 ? -44.457 -7.024 44.198 1.00 16.14 ? 158 PRO A C 1 ATOM 1215 O O . PRO A 1 158 ? -43.910 -6.880 43.098 1.00 15.54 ? 158 PRO A O 1 ATOM 1216 C CB . PRO A 1 158 ? -46.760 -8.098 44.369 1.00 16.66 ? 158 PRO A CB 1 ATOM 1217 C CG . PRO A 1 158 ? -47.034 -8.351 42.922 1.00 14.48 ? 158 PRO A CG 1 ATOM 1218 C CD . PRO A 1 158 ? -47.408 -7.010 42.401 1.00 13.94 ? 158 PRO A CD 1 ATOM 1219 N N . ALA A 1 159 ? -43.792 -7.357 45.307 1.00 15.07 ? 159 ALA A N 1 ATOM 1220 C CA . ALA A 1 159 ? -42.348 -7.614 45.309 1.00 15.41 ? 159 ALA A CA 1 ATOM 1221 C C . ALA A 1 159 ? -41.995 -8.948 45.981 1.00 15.86 ? 159 ALA A C 1 ATOM 1222 O O . ALA A 1 159 ? -42.859 -9.575 46.599 1.00 16.60 ? 159 ALA A O 1 ATOM 1223 C CB . ALA A 1 159 ? -41.611 -6.466 45.970 1.00 16.85 ? 159 ALA A CB 1 ATOM 1224 N N . SER A 1 160 ? -40.737 -9.383 45.858 1.00 14.61 ? 160 SER A N 1 ATOM 1225 C CA . SER A 1 160 ? -40.301 -10.664 46.432 1.00 15.96 ? 160 SER A CA 1 ATOM 1226 C C . SER A 1 160 ? -39.744 -10.627 47.863 1.00 16.88 ? 160 SER A C 1 ATOM 1227 O O . SER A 1 160 ? -39.300 -11.654 48.391 1.00 16.18 ? 160 SER A O 1 ATOM 1228 C CB . SER A 1 160 ? -39.296 -11.338 45.499 1.00 14.65 ? 160 SER A CB 1 ATOM 1229 O OG . SER A 1 160 ? -38.123 -10.556 45.366 1.00 17.90 ? 160 SER A OG 1 ATOM 1230 N N . LEU A 1 161 ? -39.798 -9.454 48.491 1.00 18.12 ? 161 LEU A N 1 ATOM 1231 C CA . LEU A 1 161 ? -39.291 -9.267 49.848 1.00 19.56 ? 161 LEU A CA 1 ATOM 1232 C C . LEU A 1 161 ? -39.975 -8.064 50.482 1.00 19.40 ? 161 LEU A C 1 ATOM 1233 O O . LEU A 1 161 ? -40.289 -7.101 49.778 1.00 20.46 ? 161 LEU A O 1 ATOM 1234 C CB . LEU A 1 161 ? -37.776 -9.001 49.801 1.00 19.54 ? 161 LEU A CB 1 ATOM 1235 C CG . LEU A 1 161 ? -36.827 -9.327 50.951 1.00 17.11 ? 161 LEU A CG 1 ATOM 1236 C CD1 . LEU A 1 161 ? -36.762 -10.829 51.159 1.00 17.88 ? 161 LEU A CD1 1 ATOM 1237 C CD2 . LEU A 1 161 ? -35.454 -8.768 50.637 1.00 16.55 ? 161 LEU A CD2 1 ATOM 1238 N N . PRO A 1 162 ? -40.269 -8.123 51.805 1.00 18.81 ? 162 PRO A N 1 ATOM 1239 C CA . PRO A 1 162 ? -40.914 -6.988 52.478 1.00 18.54 ? 162 PRO A CA 1 ATOM 1240 C C . PRO A 1 162 ? -39.991 -5.768 52.653 1.00 18.48 ? 162 PRO A C 1 ATOM 1241 O O . PRO A 1 162 ? -38.776 -5.919 52.833 1.00 20.01 ? 162 PRO A O 1 ATOM 1242 C CB . PRO A 1 162 ? -41.330 -7.584 53.827 1.00 19.09 ? 162 PRO A CB 1 ATOM 1243 C CG . PRO A 1 162 ? -40.348 -8.699 54.044 1.00 18.27 ? 162 PRO A CG 1 ATOM 1244 C CD . PRO A 1 162 ? -40.310 -9.312 52.681 1.00 18.82 ? 162 PRO A CD 1 ATOM 1245 N N . TYR A 1 163 ? -40.577 -4.577 52.511 1.00 17.25 ? 163 TYR A N 1 ATOM 1246 C CA . TYR A 1 163 ? -39.882 -3.292 52.666 1.00 17.80 ? 163 TYR A CA 1 ATOM 1247 C C . TYR A 1 163 ? -40.877 -2.244 53.157 1.00 18.21 ? 163 TYR A C 1 ATOM 1248 O O . TYR A 1 163 ? -42.075 -2.377 52.919 1.00 18.67 ? 163 TYR A O 1 ATOM 1249 C CB . TYR A 1 163 ? -39.189 -2.827 51.358 1.00 15.71 ? 163 TYR A CB 1 ATOM 1250 C CG . TYR A 1 163 ? -40.085 -2.688 50.151 1.00 14.05 ? 163 TYR A CG 1 ATOM 1251 C CD1 . TYR A 1 163 ? -40.809 -1.496 49.912 1.00 14.75 ? 163 TYR A CD1 1 ATOM 1252 C CD2 . TYR A 1 163 ? -40.241 -3.754 49.249 1.00 14.48 ? 163 TYR A CD2 1 ATOM 1253 C CE1 . TYR A 1 163 ? -41.678 -1.374 48.800 1.00 16.05 ? 163 TYR A CE1 1 ATOM 1254 C CE2 . TYR A 1 163 ? -41.108 -3.644 48.129 1.00 14.38 ? 163 TYR A CE2 1 ATOM 1255 C CZ . TYR A 1 163 ? -41.821 -2.456 47.915 1.00 16.17 ? 163 TYR A CZ 1 ATOM 1256 O OH . TYR A 1 163 ? -42.662 -2.346 46.832 1.00 16.78 ? 163 TYR A OH 1 ATOM 1257 N N . ASP A 1 164 ? -40.372 -1.163 53.741 1.00 18.69 ? 164 ASP A N 1 ATOM 1258 C CA . ASP A 1 164 ? -41.234 -0.109 54.268 1.00 20.88 ? 164 ASP A CA 1 ATOM 1259 C C . ASP A 1 164 ? -41.442 1.083 53.343 1.00 21.91 ? 164 ASP A C 1 ATOM 1260 O O . ASP A 1 164 ? -42.578 1.529 53.139 1.00 22.02 ? 164 ASP A O 1 ATOM 1261 C CB . ASP A 1 164 ? -40.709 0.376 55.623 1.00 22.17 ? 164 ASP A CB 1 ATOM 1262 C CG . ASP A 1 164 ? -40.603 -0.742 56.634 1.00 23.70 ? 164 ASP A CG 1 ATOM 1263 O OD1 . ASP A 1 164 ? -41.620 -1.050 57.292 1.00 24.38 ? 164 ASP A OD1 1 ATOM 1264 O OD2 . ASP A 1 164 ? -39.502 -1.318 56.755 1.00 24.18 ? 164 ASP A OD2 1 ATOM 1265 N N . ILE A 1 165 ? -40.334 1.626 52.837 1.00 21.18 ? 165 ILE A N 1 ATOM 1266 C CA . ILE A 1 165 ? -40.356 2.792 51.954 1.00 21.58 ? 165 ILE A CA 1 ATOM 1267 C C . ILE A 1 165 ? -39.854 2.458 50.535 1.00 21.96 ? 165 ILE A C 1 ATOM 1268 O O . ILE A 1 165 ? -38.913 1.680 50.355 1.00 22.06 ? 165 ILE A O 1 ATOM 1269 C CB . ILE A 1 165 ? -39.493 3.966 52.563 1.00 21.82 ? 165 ILE A CB 1 ATOM 1270 C CG1 . ILE A 1 165 ? -39.969 4.309 53.986 1.00 22.31 ? 165 ILE A CG1 1 ATOM 1271 C CG2 . ILE A 1 165 ? -39.558 5.221 51.681 1.00 19.73 ? 165 ILE A CG2 1 ATOM 1272 C CD1 . ILE A 1 165 ? -39.098 5.304 54.737 1.00 21.19 ? 165 ILE A CD1 1 ATOM 1273 N N . ASP A 1 166 ? -40.518 3.042 49.540 1.00 22.08 ? 166 ASP A N 1 ATOM 1274 C CA . ASP A 1 166 ? -40.152 2.885 48.132 1.00 20.74 ? 166 ASP A CA 1 ATOM 1275 C C . ASP A 1 166 ? -39.615 4.270 47.762 1.00 20.80 ? 166 ASP A C 1 ATOM 1276 O O . ASP A 1 166 ? -40.396 5.196 47.535 1.00 23.24 ? 166 ASP A O 1 ATOM 1277 C CB . ASP A 1 166 ? -41.397 2.526 47.295 1.00 18.91 ? 166 ASP A CB 1 ATOM 1278 C CG . ASP A 1 166 ? -41.081 2.224 45.821 1.00 18.88 ? 166 ASP A CG 1 ATOM 1279 O OD1 . ASP A 1 166 ? -40.085 2.738 45.262 1.00 18.00 ? 166 ASP A OD1 1 ATOM 1280 O OD2 . ASP A 1 166 ? -41.866 1.478 45.206 1.00 16.95 ? 166 ASP A OD2 1 ATOM 1281 N N . LEU A 1 167 ? -38.285 4.399 47.722 1.00 20.20 ? 167 LEU A N 1 ATOM 1282 C CA . LEU A 1 167 ? -37.593 5.654 47.392 1.00 19.34 ? 167 LEU A CA 1 ATOM 1283 C C . LEU A 1 167 ? -37.794 6.097 45.948 1.00 18.52 ? 167 LEU A C 1 ATOM 1284 O O . LEU A 1 167 ? -37.481 7.233 45.581 1.00 20.14 ? 167 LEU A O 1 ATOM 1285 C CB . LEU A 1 167 ? -36.095 5.524 47.670 1.00 20.08 ? 167 LEU A CB 1 ATOM 1286 C CG . LEU A 1 167 ? -35.635 5.397 49.124 1.00 23.46 ? 167 LEU A CG 1 ATOM 1287 C CD1 . LEU A 1 167 ? -34.221 4.860 49.135 1.00 20.93 ? 167 LEU A CD1 1 ATOM 1288 C CD2 . LEU A 1 167 ? -35.725 6.747 49.863 1.00 22.87 ? 167 LEU A CD2 1 ATOM 1289 N N . GLY A 1 168 ? -38.311 5.186 45.131 1.00 17.05 ? 168 GLY A N 1 ATOM 1290 C CA . GLY A 1 168 ? -38.560 5.496 43.739 1.00 14.88 ? 168 GLY A CA 1 ATOM 1291 C C . GLY A 1 168 ? -37.369 5.222 42.853 1.00 13.29 ? 168 GLY A C 1 ATOM 1292 O O . GLY A 1 168 ? -36.440 4.486 43.215 1.00 13.61 ? 168 GLY A O 1 ATOM 1293 N N . VAL A 1 169 ? -37.375 5.888 41.711 1.00 11.83 ? 169 VAL A N 1 ATOM 1294 C CA . VAL A 1 169 ? -36.343 5.729 40.698 1.00 9.55 ? 169 VAL A CA 1 ATOM 1295 C C . VAL A 1 169 ? -35.012 6.435 40.961 1.00 10.43 ? 169 VAL A C 1 ATOM 1296 O O . VAL A 1 169 ? -34.969 7.566 41.459 1.00 10.06 ? 169 VAL A O 1 ATOM 1297 C CB . VAL A 1 169 ? -36.915 6.069 39.301 1.00 6.83 ? 169 VAL A CB 1 ATOM 1298 C CG1 . VAL A 1 169 ? -38.058 5.096 38.972 1.00 2.86 ? 169 VAL A CG1 1 ATOM 1299 C CG2 . VAL A 1 169 ? -37.416 7.514 39.239 1.00 3.71 ? 169 VAL A CG2 1 ATOM 1300 N N . PHE A 1 170 ? -33.929 5.761 40.577 1.00 12.68 ? 170 PHE A N 1 ATOM 1301 C CA . PHE A 1 170 ? -32.564 6.272 40.754 1.00 14.64 ? 170 PHE A CA 1 ATOM 1302 C C . PHE A 1 170 ? -31.793 6.149 39.415 1.00 14.04 ? 170 PHE A C 1 ATOM 1303 O O . PHE A 1 170 ? -30.863 5.337 39.298 1.00 13.91 ? 170 PHE A O 1 ATOM 1304 C CB . PHE A 1 170 ? -31.889 5.449 41.867 1.00 14.38 ? 170 PHE A CB 1 ATOM 1305 C CG . PHE A 1 170 ? -30.838 6.188 42.650 1.00 15.35 ? 170 PHE A CG 1 ATOM 1306 C CD1 . PHE A 1 170 ? -31.071 7.492 43.131 1.00 14.88 ? 170 PHE A CD1 1 ATOM 1307 C CD2 . PHE A 1 170 ? -29.627 5.549 42.974 1.00 16.17 ? 170 PHE A CD2 1 ATOM 1308 C CE1 . PHE A 1 170 ? -30.114 8.155 43.931 1.00 15.68 ? 170 PHE A CE1 1 ATOM 1309 C CE2 . PHE A 1 170 ? -28.649 6.197 43.784 1.00 17.35 ? 170 PHE A CE2 1 ATOM 1310 C CZ . PHE A 1 170 ? -28.895 7.504 44.265 1.00 16.12 ? 170 PHE A CZ 1 ATOM 1311 N N . PRO A 1 171 ? -32.149 6.975 38.399 1.00 14.22 ? 171 PRO A N 1 ATOM 1312 C CA . PRO A 1 171 ? -31.461 6.899 37.100 1.00 15.25 ? 171 PRO A CA 1 ATOM 1313 C C . PRO A 1 171 ? -30.019 7.396 37.017 1.00 15.24 ? 171 PRO A C 1 ATOM 1314 O O . PRO A 1 171 ? -29.741 8.589 37.156 1.00 16.55 ? 171 PRO A O 1 ATOM 1315 C CB . PRO A 1 171 ? -32.396 7.677 36.175 1.00 14.70 ? 171 PRO A CB 1 ATOM 1316 C CG . PRO A 1 171 ? -32.946 8.724 37.052 1.00 15.56 ? 171 PRO A CG 1 ATOM 1317 C CD . PRO A 1 171 ? -33.222 7.989 38.346 1.00 15.16 ? 171 PRO A CD 1 ATOM 1318 N N . ILE A 1 172 ? -29.109 6.450 36.798 1.00 15.36 ? 172 ILE A N 1 ATOM 1319 C CA . ILE A 1 172 ? -27.687 6.750 36.667 1.00 15.80 ? 172 ILE A CA 1 ATOM 1320 C C . ILE A 1 172 ? -27.341 6.743 35.169 1.00 15.83 ? 172 ILE A C 1 ATOM 1321 O O . ILE A 1 172 ? -27.580 5.748 34.476 1.00 17.14 ? 172 ILE A O 1 ATOM 1322 C CB . ILE A 1 172 ? -26.793 5.732 37.457 1.00 15.39 ? 172 ILE A CB 1 ATOM 1323 C CG1 . ILE A 1 172 ? -27.342 5.513 38.878 1.00 15.77 ? 172 ILE A CG1 1 ATOM 1324 C CG2 . ILE A 1 172 ? -25.375 6.292 37.590 1.00 14.53 ? 172 ILE A CG2 1 ATOM 1325 C CD1 . ILE A 1 172 ? -26.588 4.497 39.709 1.00 14.90 ? 172 ILE A CD1 1 ATOM 1326 N N . THR A 1 173 ? -26.814 7.865 34.672 1.00 15.21 ? 173 THR A N 1 ATOM 1327 C CA . THR A 1 173 ? -26.444 7.994 33.257 1.00 15.62 ? 173 THR A CA 1 ATOM 1328 C C . THR A 1 173 ? -25.126 8.708 33.007 1.00 14.64 ? 173 THR A C 1 ATOM 1329 O O . THR A 1 173 ? -24.671 9.504 33.834 1.00 14.12 ? 173 THR A O 1 ATOM 1330 C CB . THR A 1 173 ? -27.560 8.728 32.426 1.00 16.08 ? 173 THR A CB 1 ATOM 1331 O OG1 . THR A 1 173 ? -27.219 8.729 31.029 1.00 16.44 ? 173 THR A OG1 1 ATOM 1332 C CG2 . THR A 1 173 ? -27.795 10.175 32.913 1.00 17.32 ? 173 THR A CG2 1 ATOM 1333 N N . ASP A 1 174 ? -24.522 8.424 31.851 1.00 13.00 ? 174 ASP A N 1 ATOM 1334 C CA . ASP A 1 174 ? -23.301 9.124 31.466 1.00 12.21 ? 174 ASP A CA 1 ATOM 1335 C C . ASP A 1 174 ? -23.721 10.503 30.969 1.00 10.18 ? 174 ASP A C 1 ATOM 1336 O O . ASP A 1 174 ? -24.845 10.674 30.483 1.00 9.15 ? 174 ASP A O 1 ATOM 1337 C CB . ASP A 1 174 ? -22.480 8.382 30.404 1.00 12.55 ? 174 ASP A CB 1 ATOM 1338 C CG . ASP A 1 174 ? -23.303 7.837 29.235 1.00 13.09 ? 174 ASP A CG 1 ATOM 1339 O OD1 . ASP A 1 174 ? -24.461 8.264 28.996 1.00 8.54 ? 174 ASP A OD1 1 ATOM 1340 O OD2 . ASP A 1 174 ? -22.742 6.964 28.534 1.00 12.10 ? 174 ASP A OD2 1 ATOM 1341 N N . TYR A 1 175 ? -22.836 11.474 31.142 1.00 9.45 ? 175 TYR A N 1 ATOM 1342 C CA . TYR A 1 175 ? -23.109 12.844 30.757 1.00 10.66 ? 175 TYR A CA 1 ATOM 1343 C C . TYR A 1 175 ? -21.975 13.382 29.904 1.00 9.40 ? 175 TYR A C 1 ATOM 1344 O O . TYR A 1 175 ? -20.821 13.351 30.313 1.00 10.46 ? 175 TYR A O 1 ATOM 1345 C CB . TYR A 1 175 ? -23.295 13.689 32.016 1.00 11.27 ? 175 TYR A CB 1 ATOM 1346 C CG . TYR A 1 175 ? -23.855 15.071 31.788 1.00 14.34 ? 175 TYR A CG 1 ATOM 1347 C CD1 . TYR A 1 175 ? -25.062 15.264 31.074 1.00 14.12 ? 175 TYR A CD1 1 ATOM 1348 C CD2 . TYR A 1 175 ? -23.185 16.203 32.297 1.00 14.39 ? 175 TYR A CD2 1 ATOM 1349 C CE1 . TYR A 1 175 ? -25.585 16.554 30.874 1.00 16.28 ? 175 TYR A CE1 1 ATOM 1350 C CE2 . TYR A 1 175 ? -23.699 17.496 32.105 1.00 15.74 ? 175 TYR A CE2 1 ATOM 1351 C CZ . TYR A 1 175 ? -24.894 17.664 31.396 1.00 17.31 ? 175 TYR A CZ 1 ATOM 1352 O OH . TYR A 1 175 ? -25.392 18.927 31.214 1.00 20.06 ? 175 TYR A OH 1 ATOM 1353 N N . TYR A 1 176 ? -22.334 13.818 28.698 1.00 10.30 ? 176 TYR A N 1 ATOM 1354 C CA . TYR A 1 176 ? -21.397 14.372 27.720 1.00 11.47 ? 176 TYR A CA 1 ATOM 1355 C C . TYR A 1 176 ? -21.739 15.809 27.429 1.00 12.81 ? 176 TYR A C 1 ATOM 1356 O O . TYR A 1 176 ? -22.913 16.154 27.300 1.00 14.29 ? 176 TYR A O 1 ATOM 1357 C CB . TYR A 1 176 ? -21.460 13.617 26.394 1.00 9.51 ? 176 TYR A CB 1 ATOM 1358 C CG . TYR A 1 176 ? -21.128 12.162 26.503 1.00 10.77 ? 176 TYR A CG 1 ATOM 1359 C CD1 . TYR A 1 176 ? -22.144 11.210 26.740 1.00 11.53 ? 176 TYR A CD1 1 ATOM 1360 C CD2 . TYR A 1 176 ? -19.796 11.718 26.424 1.00 7.96 ? 176 TYR A CD2 1 ATOM 1361 C CE1 . TYR A 1 176 ? -21.834 9.840 26.908 1.00 11.40 ? 176 TYR A CE1 1 ATOM 1362 C CE2 . TYR A 1 176 ? -19.478 10.343 26.586 1.00 10.96 ? 176 TYR A CE2 1 ATOM 1363 C CZ . TYR A 1 176 ? -20.500 9.415 26.837 1.00 9.54 ? 176 TYR A CZ 1 ATOM 1364 O OH . TYR A 1 176 ? -20.186 8.097 27.071 1.00 12.05 ? 176 TYR A OH 1 ATOM 1365 N N . TYR A 1 177 ? -20.701 16.630 27.286 1.00 13.23 ? 177 TYR A N 1 ATOM 1366 C CA . TYR A 1 177 ? -20.846 18.046 26.976 1.00 11.56 ? 177 TYR A CA 1 ATOM 1367 C C . TYR A 1 177 ? -21.133 18.215 25.487 1.00 12.75 ? 177 TYR A C 1 ATOM 1368 O O . TYR A 1 177 ? -21.843 19.144 25.086 1.00 15.35 ? 177 TYR A O 1 ATOM 1369 C CB . TYR A 1 177 ? -19.589 18.820 27.395 1.00 12.79 ? 177 TYR A CB 1 ATOM 1370 C CG . TYR A 1 177 ? -19.259 18.767 28.888 1.00 11.07 ? 177 TYR A CG 1 ATOM 1371 C CD1 . TYR A 1 177 ? -20.247 18.444 29.864 1.00 12.44 ? 177 TYR A CD1 1 ATOM 1372 C CD2 . TYR A 1 177 ? -17.948 19.018 29.337 1.00 11.83 ? 177 TYR A CD2 1 ATOM 1373 C CE1 . TYR A 1 177 ? -19.924 18.368 31.250 1.00 10.12 ? 177 TYR A CE1 1 ATOM 1374 C CE2 . TYR A 1 177 ? -17.612 18.948 30.729 1.00 11.48 ? 177 TYR A CE2 1 ATOM 1375 C CZ . TYR A 1 177 ? -18.604 18.620 31.664 1.00 10.29 ? 177 TYR A CZ 1 ATOM 1376 O OH . TYR A 1 177 ? -18.268 18.532 32.989 1.00 14.86 ? 177 TYR A OH 1 ATOM 1377 N N . ARG A 1 178 ? -20.616 17.285 24.682 1.00 11.65 ? 178 ARG A N 1 ATOM 1378 C CA . ARG A 1 178 ? -20.824 17.279 23.235 1.00 12.51 ? 178 ARG A CA 1 ATOM 1379 C C . ARG A 1 178 ? -22.132 16.548 22.914 1.00 13.31 ? 178 ARG A C 1 ATOM 1380 O O . ARG A 1 178 ? -22.461 15.541 23.553 1.00 13.44 ? 178 ARG A O 1 ATOM 1381 C CB . ARG A 1 178 ? -19.645 16.599 22.536 1.00 16.35 ? 178 ARG A CB 1 ATOM 1382 C CG . ARG A 1 178 ? -18.325 17.359 22.632 1.00 18.38 ? 178 ARG A CG 1 ATOM 1383 C CD . ARG A 1 178 ? -18.270 18.548 21.674 1.00 20.88 ? 178 ARG A CD 1 ATOM 1384 N NE . ARG A 1 178 ? -18.280 18.114 20.276 1.00 24.51 ? 178 ARG A NE 1 ATOM 1385 C CZ . ARG A 1 178 ? -18.285 18.927 19.219 1.00 25.59 ? 178 ARG A CZ 1 ATOM 1386 N NH1 . ARG A 1 178 ? -18.291 20.246 19.370 1.00 26.28 ? 178 ARG A NH1 1 ATOM 1387 N NH2 . ARG A 1 178 ? -18.250 18.412 17.996 1.00 26.11 ? 178 ARG A NH2 1 ATOM 1388 N N . ALA A 1 179 ? -22.876 17.063 21.934 1.00 11.47 ? 179 ALA A N 1 ATOM 1389 C CA . ALA A 1 179 ? -24.168 16.495 21.530 1.00 10.19 ? 179 ALA A CA 1 ATOM 1390 C C . ALA A 1 179 ? -24.056 15.109 20.902 1.00 9.98 ? 179 ALA A C 1 ATOM 1391 O O . ALA A 1 179 ? -22.978 14.720 20.451 1.00 10.23 ? 179 ALA A O 1 ATOM 1392 C CB . ALA A 1 179 ? -24.905 17.452 20.596 1.00 10.24 ? 179 ALA A CB 1 ATOM 1393 N N . ALA A 1 180 ? -25.178 14.385 20.886 1.00 8.58 ? 180 ALA A N 1 ATOM 1394 C CA . ALA A 1 180 ? -25.277 13.022 20.355 1.00 8.17 ? 180 ALA A CA 1 ATOM 1395 C C . ALA A 1 180 ? -24.899 12.811 18.895 1.00 10.61 ? 180 ALA A C 1 ATOM 1396 O O . ALA A 1 180 ? -24.189 11.849 18.584 1.00 12.27 ? 180 ALA A O 1 ATOM 1397 C CB . ALA A 1 180 ? -26.656 12.473 20.596 1.00 7.60 ? 180 ALA A CB 1 ATOM 1398 N N . ASP A 1 181 ? -25.347 13.704 18.012 1.00 12.15 ? 181 ASP A N 1 ATOM 1399 C CA . ASP A 1 181 ? -25.052 13.594 16.573 1.00 16.66 ? 181 ASP A CA 1 ATOM 1400 C C . ASP A 1 181 ? -23.588 13.834 16.249 1.00 17.90 ? 181 ASP A C 1 ATOM 1401 O O . ASP A 1 181 ? -23.071 13.305 15.265 1.00 20.32 ? 181 ASP A O 1 ATOM 1402 C CB . ASP A 1 181 ? -25.936 14.523 15.740 1.00 17.95 ? 181 ASP A CB 1 ATOM 1403 C CG . ASP A 1 181 ? -27.388 14.078 15.713 1.00 21.73 ? 181 ASP A CG 1 ATOM 1404 O OD1 . ASP A 1 181 ? -27.675 12.992 15.157 1.00 23.38 ? 181 ASP A OD1 1 ATOM 1405 O OD2 . ASP A 1 181 ? -28.242 14.818 16.247 1.00 23.24 ? 181 ASP A OD2 1 ATOM 1406 N N . ASP A 1 182 ? -22.919 14.592 17.117 1.00 18.07 ? 182 ASP A N 1 ATOM 1407 C CA . ASP A 1 182 ? -21.501 14.891 16.969 1.00 17.47 ? 182 ASP A CA 1 ATOM 1408 C C . ASP A 1 182 ? -20.677 13.709 17.477 1.00 16.71 ? 182 ASP A C 1 ATOM 1409 O O . ASP A 1 182 ? -19.609 13.404 16.939 1.00 18.22 ? 182 ASP A O 1 ATOM 1410 C CB . ASP A 1 182 ? -21.143 16.174 17.724 1.00 16.58 ? 182 ASP A CB 1 ATOM 1411 C CG . ASP A 1 182 ? -21.660 17.421 17.035 1.00 15.73 ? 182 ASP A CG 1 ATOM 1412 O OD1 . ASP A 1 182 ? -21.738 17.429 15.785 1.00 16.29 ? 182 ASP A OD1 1 ATOM 1413 O OD2 . ASP A 1 182 ? -21.978 18.400 17.742 1.00 15.87 ? 182 ASP A OD2 1 ATOM 1414 N N . LEU A 1 183 ? -21.233 13.009 18.464 1.00 14.88 ? 183 LEU A N 1 ATOM 1415 C CA . LEU A 1 183 ? -20.601 11.840 19.055 1.00 14.19 ? 183 LEU A CA 1 ATOM 1416 C C . LEU A 1 183 ? -20.780 10.608 18.178 1.00 14.33 ? 183 LEU A C 1 ATOM 1417 O O . LEU A 1 183 ? -19.936 9.720 18.192 1.00 13.47 ? 183 LEU A O 1 ATOM 1418 C CB . LEU A 1 183 ? -21.143 11.584 20.463 1.00 12.94 ? 183 LEU A CB 1 ATOM 1419 C CG . LEU A 1 183 ? -20.689 12.534 21.567 1.00 10.20 ? 183 LEU A CG 1 ATOM 1420 C CD1 . LEU A 1 183 ? -21.649 12.438 22.727 1.00 10.27 ? 183 LEU A CD1 1 ATOM 1421 C CD2 . LEU A 1 183 ? -19.279 12.234 22.006 1.00 10.88 ? 183 LEU A CD2 1 ATOM 1422 N N . VAL A 1 184 ? -21.872 10.561 17.413 1.00 14.90 ? 184 VAL A N 1 ATOM 1423 C CA . VAL A 1 184 ? -22.130 9.449 16.498 1.00 15.08 ? 184 VAL A CA 1 ATOM 1424 C C . VAL A 1 184 ? -21.120 9.591 15.363 1.00 16.83 ? 184 VAL A C 1 ATOM 1425 O O . VAL A 1 184 ? -20.500 8.611 14.954 1.00 17.78 ? 184 VAL A O 1 ATOM 1426 C CB . VAL A 1 184 ? -23.600 9.457 15.974 1.00 14.36 ? 184 VAL A CB 1 ATOM 1427 C CG1 . VAL A 1 184 ? -23.771 8.559 14.753 1.00 16.32 ? 184 VAL A CG1 1 ATOM 1428 C CG2 . VAL A 1 184 ? -24.517 8.950 17.047 1.00 10.69 ? 184 VAL A CG2 1 ATOM 1429 N N . HIS A 1 185 ? -20.911 10.839 14.939 1.00 18.56 ? 185 HIS A N 1 ATOM 1430 C CA . HIS A 1 185 ? -19.966 11.194 13.885 1.00 21.31 ? 185 HIS A CA 1 ATOM 1431 C C . HIS A 1 185 ? -18.512 10.914 14.325 1.00 22.21 ? 185 HIS A C 1 ATOM 1432 O O . HIS A 1 185 ? -17.692 10.468 13.513 1.00 21.40 ? 185 HIS A O 1 ATOM 1433 C CB . HIS A 1 185 ? -20.139 12.673 13.504 1.00 22.78 ? 185 HIS A CB 1 ATOM 1434 C CG . HIS A 1 185 ? -19.130 13.167 12.513 1.00 26.39 ? 185 HIS A CG 1 ATOM 1435 N ND1 . HIS A 1 185 ? -19.063 12.690 11.221 1.00 26.57 ? 185 HIS A ND1 1 ATOM 1436 C CD2 . HIS A 1 185 ? -18.112 14.052 12.641 1.00 27.48 ? 185 HIS A CD2 1 ATOM 1437 C CE1 . HIS A 1 185 ? -18.046 13.257 10.598 1.00 28.03 ? 185 HIS A CE1 1 ATOM 1438 N NE2 . HIS A 1 185 ? -17.452 14.087 11.437 1.00 29.15 ? 185 HIS A NE2 1 ATOM 1439 N N . PHE A 1 186 ? -18.208 11.189 15.600 1.00 21.98 ? 186 PHE A N 1 ATOM 1440 C CA . PHE A 1 186 ? -16.871 10.965 16.155 1.00 20.72 ? 186 PHE A CA 1 ATOM 1441 C C . PHE A 1 186 ? -16.583 9.465 16.253 1.00 19.85 ? 186 PHE A C 1 ATOM 1442 O O . PHE A 1 186 ? -15.570 8.999 15.737 1.00 19.70 ? 186 PHE A O 1 ATOM 1443 C CB . PHE A 1 186 ? -16.731 11.643 17.531 1.00 21.92 ? 186 PHE A CB 1 ATOM 1444 C CG . PHE A 1 186 ? -15.331 11.584 18.117 1.00 22.27 ? 186 PHE A CG 1 ATOM 1445 C CD1 . PHE A 1 186 ? -14.277 12.333 17.546 1.00 21.92 ? 186 PHE A CD1 1 ATOM 1446 C CD2 . PHE A 1 186 ? -15.063 10.783 19.249 1.00 22.43 ? 186 PHE A CD2 1 ATOM 1447 C CE1 . PHE A 1 186 ? -12.963 12.292 18.094 1.00 19.85 ? 186 PHE A CE1 1 ATOM 1448 C CE2 . PHE A 1 186 ? -13.758 10.726 19.814 1.00 22.58 ? 186 PHE A CE2 1 ATOM 1449 C CZ . PHE A 1 186 ? -12.704 11.486 19.232 1.00 20.95 ? 186 PHE A CZ 1 ATOM 1450 N N . THR A 1 187 ? -17.531 8.717 16.821 1.00 19.04 ? 187 THR A N 1 ATOM 1451 C CA . THR A 1 187 ? -17.407 7.269 17.004 1.00 16.97 ? 187 THR A CA 1 ATOM 1452 C C . THR A 1 187 ? -17.382 6.418 15.733 1.00 16.94 ? 187 THR A C 1 ATOM 1453 O O . THR A 1 187 ? -16.901 5.281 15.754 1.00 16.46 ? 187 THR A O 1 ATOM 1454 C CB . THR A 1 187 ? -18.456 6.721 17.983 1.00 16.35 ? 187 THR A CB 1 ATOM 1455 O OG1 . THR A 1 187 ? -19.779 7.004 17.505 1.00 14.71 ? 187 THR A OG1 1 ATOM 1456 C CG2 . THR A 1 187 ? -18.274 7.348 19.354 1.00 13.85 ? 187 THR A CG2 1 ATOM 1457 N N . GLN A 1 188 ? -17.863 6.986 14.628 1.00 18.31 ? 188 GLN A N 1 ATOM 1458 C CA . GLN A 1 188 ? -17.872 6.309 13.327 1.00 20.03 ? 188 GLN A CA 1 ATOM 1459 C C . GLN A 1 188 ? -16.452 6.026 12.837 1.00 20.12 ? 188 GLN A C 1 ATOM 1460 O O . GLN A 1 188 ? -16.207 5.007 12.195 1.00 21.46 ? 188 GLN A O 1 ATOM 1461 C CB . GLN A 1 188 ? -18.610 7.145 12.283 1.00 19.86 ? 188 GLN A CB 1 ATOM 1462 C CG . GLN A 1 188 ? -20.120 6.935 12.268 1.00 22.97 ? 188 GLN A CG 1 ATOM 1463 C CD . GLN A 1 188 ? -20.845 7.731 11.184 1.00 23.29 ? 188 GLN A CD 1 ATOM 1464 O OE1 . GLN A 1 188 ? -20.382 8.784 10.735 1.00 25.02 ? 188 GLN A OE1 1 ATOM 1465 N NE2 . GLN A 1 188 ? -22.002 7.229 10.769 1.00 24.55 ? 188 GLN A NE2 1 ATOM 1466 N N . ASN A 1 189 ? -15.523 6.913 13.197 1.00 19.92 ? 189 ASN A N 1 ATOM 1467 C CA . ASN A 1 189 ? -14.121 6.801 12.808 1.00 19.77 ? 189 ASN A CA 1 ATOM 1468 C C . ASN A 1 189 ? -13.141 6.793 13.977 1.00 19.69 ? 189 ASN A C 1 ATOM 1469 O O . ASN A 1 189 ? -11.939 6.623 13.767 1.00 20.35 ? 189 ASN A O 1 ATOM 1470 C CB . ASN A 1 189 ? -13.746 7.924 11.832 1.00 21.76 ? 189 ASN A CB 1 ATOM 1471 C CG . ASN A 1 189 ? -14.226 7.655 10.423 1.00 21.00 ? 189 ASN A CG 1 ATOM 1472 O OD1 . ASN A 1 189 ? -13.687 6.788 9.731 1.00 23.97 ? 189 ASN A OD1 1 ATOM 1473 N ND2 . ASN A 1 189 ? -15.251 8.390 9.991 1.00 18.30 ? 189 ASN A ND2 1 ATOM 1474 N N . ASN A 1 190 ? -13.640 7.016 15.193 1.00 19.02 ? 190 ASN A N 1 ATOM 1475 C CA . ASN A 1 190 ? -12.798 7.031 16.394 1.00 19.92 ? 190 ASN A CA 1 ATOM 1476 C C . ASN A 1 190 ? -13.386 6.188 17.505 1.00 17.72 ? 190 ASN A C 1 ATOM 1477 O O . ASN A 1 190 ? -14.574 5.869 17.502 1.00 18.64 ? 190 ASN A O 1 ATOM 1478 C CB . ASN A 1 190 ? -12.580 8.449 16.933 1.00 22.83 ? 190 ASN A CB 1 ATOM 1479 C CG . ASN A 1 190 ? -11.845 9.340 15.966 1.00 27.25 ? 190 ASN A CG 1 ATOM 1480 O OD1 . ASN A 1 190 ? -10.622 9.239 15.812 1.00 28.69 ? 190 ASN A OD1 1 ATOM 1481 N ND2 . ASN A 1 190 ? -12.591 10.217 15.290 1.00 27.71 ? 190 ASN A ND2 1 ATOM 1482 N N . ALA A 1 191 ? -12.522 5.791 18.432 1.00 16.47 ? 191 ALA A N 1 ATOM 1483 C CA . ALA A 1 191 ? -12.905 4.991 19.588 1.00 15.67 ? 191 ALA A CA 1 ATOM 1484 C C . ALA A 1 191 ? -13.724 5.876 20.524 1.00 14.90 ? 191 ALA A C 1 ATOM 1485 O O . ALA A 1 191 ? -13.399 7.052 20.700 1.00 14.52 ? 191 ALA A O 1 ATOM 1486 C CB . ALA A 1 191 ? -11.658 4.479 20.307 1.00 16.49 ? 191 ALA A CB 1 ATOM 1487 N N . PRO A 1 192 ? -14.832 5.348 21.078 1.00 16.14 ? 192 PRO A N 1 ATOM 1488 C CA . PRO A 1 192 ? -15.688 6.111 21.993 1.00 16.09 ? 192 PRO A CA 1 ATOM 1489 C C . PRO A 1 192 ? -14.939 6.757 23.164 1.00 16.68 ? 192 PRO A C 1 ATOM 1490 O O . PRO A 1 192 ? -14.062 6.130 23.768 1.00 16.83 ? 192 PRO A O 1 ATOM 1491 C CB . PRO A 1 192 ? -16.696 5.063 22.470 1.00 17.05 ? 192 PRO A CB 1 ATOM 1492 C CG . PRO A 1 192 ? -16.021 3.745 22.200 1.00 18.31 ? 192 PRO A CG 1 ATOM 1493 C CD . PRO A 1 192 ? -15.388 3.996 20.881 1.00 16.51 ? 192 PRO A CD 1 ATOM 1494 N N . PRO A 1 193 ? -15.211 8.051 23.431 1.00 16.47 ? 193 PRO A N 1 ATOM 1495 C CA . PRO A 1 193 ? -14.538 8.739 24.535 1.00 15.27 ? 193 PRO A CA 1 ATOM 1496 C C . PRO A 1 193 ? -15.174 8.413 25.888 1.00 14.30 ? 193 PRO A C 1 ATOM 1497 O O . PRO A 1 193 ? -16.278 7.843 25.956 1.00 12.03 ? 193 PRO A O 1 ATOM 1498 C CB . PRO A 1 193 ? -14.742 10.209 24.178 1.00 15.22 ? 193 PRO A CB 1 ATOM 1499 C CG . PRO A 1 193 ? -16.124 10.207 23.605 1.00 16.36 ? 193 PRO A CG 1 ATOM 1500 C CD . PRO A 1 193 ? -16.095 8.987 22.698 1.00 16.30 ? 193 PRO A CD 1 ATOM 1501 N N . PHE A 1 194 ? -14.469 8.791 26.950 1.00 11.67 ? 194 PHE A N 1 ATOM 1502 C CA . PHE A 1 194 ? -14.947 8.609 28.316 1.00 11.81 ? 194 PHE A CA 1 ATOM 1503 C C . PHE A 1 194 ? -15.987 9.691 28.551 1.00 12.82 ? 194 PHE A C 1 ATOM 1504 O O . PHE A 1 194 ? -15.975 10.719 27.863 1.00 11.97 ? 194 PHE A O 1 ATOM 1505 C CB . PHE A 1 194 ? -13.799 8.813 29.309 1.00 10.24 ? 194 PHE A CB 1 ATOM 1506 C CG . PHE A 1 194 ? -13.035 7.558 29.658 1.00 8.44 ? 194 PHE A CG 1 ATOM 1507 C CD1 . PHE A 1 194 ? -13.056 6.418 28.826 1.00 7.56 ? 194 PHE A CD1 1 ATOM 1508 C CD2 . PHE A 1 194 ? -12.295 7.510 30.860 1.00 7.81 ? 194 PHE A CD2 1 ATOM 1509 C CE1 . PHE A 1 194 ? -12.350 5.237 29.184 1.00 6.65 ? 194 PHE A CE1 1 ATOM 1510 C CE2 . PHE A 1 194 ? -11.585 6.340 31.239 1.00 8.12 ? 194 PHE A CE2 1 ATOM 1511 C CZ . PHE A 1 194 ? -11.613 5.198 30.396 1.00 6.27 ? 194 PHE A CZ 1 ATOM 1512 N N . SER A 1 195 ? -16.891 9.472 29.504 1.00 14.11 ? 195 SER A N 1 ATOM 1513 C CA . SER A 1 195 ? -17.894 10.487 29.789 1.00 15.48 ? 195 SER A CA 1 ATOM 1514 C C . SER A 1 195 ? -17.272 11.649 30.531 1.00 15.61 ? 195 SER A C 1 ATOM 1515 O O . SER A 1 195 ? -16.254 11.484 31.201 1.00 14.52 ? 195 SER A O 1 ATOM 1516 C CB . SER A 1 195 ? -19.094 9.913 30.535 1.00 18.58 ? 195 SER A CB 1 ATOM 1517 O OG . SER A 1 195 ? -18.738 9.343 31.775 1.00 22.19 ? 195 SER A OG 1 ATOM 1518 N N . ASP A 1 196 ? -17.834 12.836 30.324 1.00 15.36 ? 196 ASP A N 1 ATOM 1519 C CA . ASP A 1 196 ? -17.344 14.057 30.965 1.00 15.73 ? 196 ASP A CA 1 ATOM 1520 C C . ASP A 1 196 ? -17.693 14.055 32.452 1.00 16.57 ? 196 ASP A C 1 ATOM 1521 O O . ASP A 1 196 ? -16.954 14.587 33.284 1.00 17.07 ? 196 ASP A O 1 ATOM 1522 C CB . ASP A 1 196 ? -17.938 15.269 30.264 1.00 12.58 ? 196 ASP A CB 1 ATOM 1523 C CG . ASP A 1 196 ? -17.476 15.395 28.816 1.00 13.58 ? 196 ASP A CG 1 ATOM 1524 O OD1 . ASP A 1 196 ? -16.249 15.390 28.566 1.00 13.42 ? 196 ASP A OD1 1 ATOM 1525 O OD2 . ASP A 1 196 ? -18.340 15.520 27.925 1.00 9.54 ? 196 ASP A OD2 1 ATOM 1526 N N . ASN A 1 197 ? -18.810 13.400 32.758 1.00 17.07 ? 197 ASN A N 1 ATOM 1527 C CA . ASN A 1 197 ? -19.326 13.236 34.110 1.00 16.68 ? 197 ASN A CA 1 ATOM 1528 C C . ASN A 1 197 ? -20.396 12.158 34.058 1.00 15.99 ? 197 ASN A C 1 ATOM 1529 O O . ASN A 1 197 ? -20.728 11.647 32.987 1.00 17.19 ? 197 ASN A O 1 ATOM 1530 C CB . ASN A 1 197 ? -19.929 14.546 34.647 1.00 16.06 ? 197 ASN A CB 1 ATOM 1531 C CG . ASN A 1 197 ? -19.747 14.702 36.163 1.00 16.58 ? 197 ASN A CG 1 ATOM 1532 O OD1 . ASN A 1 197 ? -19.730 13.713 36.911 1.00 14.49 ? 197 ASN A OD1 1 ATOM 1533 N ND2 . ASN A 1 197 ? -19.616 15.948 36.618 1.00 11.91 ? 197 ASN A ND2 1 ATOM 1534 N N . VAL A 1 198 ? -20.875 11.766 35.232 1.00 16.08 ? 198 VAL A N 1 ATOM 1535 C CA . VAL A 1 198 ? -21.919 10.763 35.373 1.00 16.59 ? 198 VAL A CA 1 ATOM 1536 C C . VAL A 1 198 ? -22.959 11.337 36.332 1.00 16.56 ? 198 VAL A C 1 ATOM 1537 O O . VAL A 1 198 ? -22.659 11.618 37.492 1.00 18.32 ? 198 VAL A O 1 ATOM 1538 C CB . VAL A 1 198 ? -21.359 9.402 35.925 1.00 15.54 ? 198 VAL A CB 1 ATOM 1539 C CG1 . VAL A 1 198 ? -22.485 8.460 36.347 1.00 13.55 ? 198 VAL A CG1 1 ATOM 1540 C CG2 . VAL A 1 198 ? -20.476 8.713 34.896 1.00 15.07 ? 198 VAL A CG2 1 ATOM 1541 N N . LEU A 1 199 ? -24.175 11.517 35.829 1.00 18.43 ? 199 LEU A N 1 ATOM 1542 C CA . LEU A 1 199 ? -25.274 12.036 36.629 1.00 18.90 ? 199 LEU A CA 1 ATOM 1543 C C . LEU A 1 199 ? -25.965 10.912 37.379 1.00 19.79 ? 199 LEU A C 1 ATOM 1544 O O . LEU A 1 199 ? -26.152 9.823 36.843 1.00 19.78 ? 199 LEU A O 1 ATOM 1545 C CB . LEU A 1 199 ? -26.323 12.721 35.757 1.00 20.41 ? 199 LEU A CB 1 ATOM 1546 C CG . LEU A 1 199 ? -26.004 13.854 34.790 1.00 21.06 ? 199 LEU A CG 1 ATOM 1547 C CD1 . LEU A 1 199 ? -27.293 14.275 34.134 1.00 19.83 ? 199 LEU A CD1 1 ATOM 1548 C CD2 . LEU A 1 199 ? -25.329 15.036 35.483 1.00 22.78 ? 199 LEU A CD2 1 ATOM 1549 N N . ILE A 1 200 ? -26.238 11.154 38.656 1.00 20.54 ? 200 ILE A N 1 ATOM 1550 C CA . ILE A 1 200 ? -26.958 10.206 39.495 1.00 22.05 ? 200 ILE A CA 1 ATOM 1551 C C . ILE A 1 200 ? -28.207 10.995 39.903 1.00 24.58 ? 200 ILE A C 1 ATOM 1552 O O . ILE A 1 200 ? -28.107 11.990 40.630 1.00 25.67 ? 200 ILE A O 1 ATOM 1553 C CB . ILE A 1 200 ? -26.134 9.761 40.741 1.00 20.33 ? 200 ILE A CB 1 ATOM 1554 C CG1 . ILE A 1 200 ? -24.870 9.009 40.309 1.00 18.57 ? 200 ILE A CG1 1 ATOM 1555 C CG2 . ILE A 1 200 ? -26.969 8.838 41.621 1.00 17.89 ? 200 ILE A CG2 1 ATOM 1556 C CD1 . ILE A 1 200 ? -23.903 8.737 41.426 1.00 15.45 ? 200 ILE A CD1 1 ATOM 1557 N N . ASN A 1 201 ? -29.360 10.578 39.367 1.00 26.43 ? 201 ASN A N 1 ATOM 1558 C CA . ASN A 1 201 ? -30.676 11.202 39.599 1.00 29.81 ? 201 ASN A CA 1 ATOM 1559 C C . ASN A 1 201 ? -30.694 12.656 39.089 1.00 29.41 ? 201 ASN A C 1 ATOM 1560 O O . ASN A 1 201 ? -31.115 13.589 39.785 1.00 30.19 ? 201 ASN A O 1 ATOM 1561 C CB . ASN A 1 201 ? -31.105 11.082 41.085 1.00 33.57 ? 201 ASN A CB 1 ATOM 1562 C CG . ASN A 1 201 ? -32.629 11.113 41.285 1.00 37.80 ? 201 ASN A CG 1 ATOM 1563 O OD1 . ASN A 1 201 ? -33.411 10.744 40.396 1.00 37.74 ? 201 ASN A OD1 1 ATOM 1564 N ND2 . ASN A 1 201 ? -33.031 11.524 42.487 1.00 41.26 ? 201 ASN A ND2 1 ATOM 1565 N N . GLY A 1 202 ? -30.151 12.823 37.884 1.00 28.57 ? 202 GLY A N 1 ATOM 1566 C CA . GLY A 1 202 ? -30.089 14.116 37.224 1.00 28.26 ? 202 GLY A CA 1 ATOM 1567 C C . GLY A 1 202 ? -29.117 15.144 37.775 1.00 27.60 ? 202 GLY A C 1 ATOM 1568 O O . GLY A 1 202 ? -29.257 16.331 37.457 1.00 28.57 ? 202 GLY A O 1 ATOM 1569 N N . THR A 1 203 ? -28.139 14.705 38.576 1.00 26.10 ? 203 THR A N 1 ATOM 1570 C CA . THR A 1 203 ? -27.155 15.615 39.179 1.00 24.06 ? 203 THR A CA 1 ATOM 1571 C C . THR A 1 203 ? -25.778 15.006 39.485 1.00 23.59 ? 203 THR A C 1 ATOM 1572 O O . THR A 1 203 ? -25.638 13.795 39.657 1.00 22.25 ? 203 THR A O 1 ATOM 1573 C CB . THR A 1 203 ? -27.744 16.335 40.453 1.00 23.26 ? 203 THR A CB 1 ATOM 1574 O OG1 . THR A 1 203 ? -26.850 17.367 40.896 1.00 21.93 ? 203 THR A OG1 1 ATOM 1575 C CG2 . THR A 1 203 ? -28.027 15.344 41.586 1.00 20.06 ? 203 THR A CG2 1 ATOM 1576 N N . ALA A 1 204 ? -24.768 15.875 39.521 1.00 25.43 ? 204 ALA A N 1 ATOM 1577 C CA . ALA A 1 204 ? -23.375 15.507 39.809 1.00 27.18 ? 204 ALA A CA 1 ATOM 1578 C C . ALA A 1 204 ? -22.554 16.749 40.121 1.00 27.78 ? 204 ALA A C 1 ATOM 1579 O O . ALA A 1 204 ? -23.020 17.877 39.949 1.00 28.50 ? 204 ALA A O 1 ATOM 1580 C CB . ALA A 1 204 ? -22.744 14.770 38.626 1.00 27.02 ? 204 ALA A CB 1 ATOM 1581 N N . VAL A 1 205 ? -21.335 16.515 40.604 1.00 29.34 ? 205 VAL A N 1 ATOM 1582 C CA . VAL A 1 205 ? -20.378 17.566 40.933 1.00 29.29 ? 205 VAL A CA 1 ATOM 1583 C C . VAL A 1 205 ? -19.311 17.542 39.848 1.00 30.13 ? 205 VAL A C 1 ATOM 1584 O O . VAL A 1 205 ? -18.887 16.466 39.414 1.00 30.53 ? 205 VAL A O 1 ATOM 1585 C CB . VAL A 1 205 ? -19.724 17.314 42.328 1.00 29.99 ? 205 VAL A CB 1 ATOM 1586 C CG1 . VAL A 1 205 ? -18.606 18.327 42.628 1.00 30.12 ? 205 VAL A CG1 1 ATOM 1587 C CG2 . VAL A 1 205 ? -20.774 17.416 43.403 1.00 29.61 ? 205 VAL A CG2 1 ATOM 1588 N N . ASN A 1 206 ? -18.887 18.729 39.420 1.00 30.67 ? 206 ASN A N 1 ATOM 1589 C CA . ASN A 1 206 ? -17.851 18.887 38.400 1.00 31.46 ? 206 ASN A CA 1 ATOM 1590 C C . ASN A 1 206 ? -16.488 18.662 39.085 1.00 32.12 ? 206 ASN A C 1 ATOM 1591 O O . ASN A 1 206 ? -16.134 19.394 40.003 1.00 32.72 ? 206 ASN A O 1 ATOM 1592 C CB . ASN A 1 206 ? -17.942 20.296 37.801 1.00 30.93 ? 206 ASN A CB 1 ATOM 1593 C CG . ASN A 1 206 ? -17.185 20.437 36.490 1.00 29.86 ? 206 ASN A CG 1 ATOM 1594 O OD1 . ASN A 1 206 ? -15.966 20.567 36.475 1.00 27.99 ? 206 ASN A OD1 1 ATOM 1595 N ND2 . ASN A 1 206 ? -17.916 20.440 35.386 1.00 30.22 ? 206 ASN A ND2 1 ATOM 1596 N N . PRO A 1 207 ? -15.711 17.649 38.640 1.00 34.26 ? 207 PRO A N 1 ATOM 1597 C CA . PRO A 1 207 ? -14.392 17.315 39.207 1.00 35.45 ? 207 PRO A CA 1 ATOM 1598 C C . PRO A 1 207 ? -13.275 18.362 39.056 1.00 36.33 ? 207 PRO A C 1 ATOM 1599 O O . PRO A 1 207 ? -12.230 18.265 39.709 1.00 36.19 ? 207 PRO A O 1 ATOM 1600 C CB . PRO A 1 207 ? -14.040 16.020 38.480 1.00 34.86 ? 207 PRO A CB 1 ATOM 1601 C CG . PRO A 1 207 ? -14.648 16.229 37.136 1.00 35.65 ? 207 PRO A CG 1 ATOM 1602 C CD . PRO A 1 207 ? -16.010 16.759 37.500 1.00 35.47 ? 207 PRO A CD 1 ATOM 1603 N N . ASN A 1 208 ? -13.506 19.345 38.188 1.00 37.07 ? 208 ASN A N 1 ATOM 1604 C CA . ASN A 1 208 ? -12.544 20.412 37.933 1.00 38.25 ? 208 ASN A CA 1 ATOM 1605 C C . ASN A 1 208 ? -12.903 21.688 38.687 1.00 39.09 ? 208 ASN A C 1 ATOM 1606 O O . ASN A 1 208 ? -12.034 22.308 39.304 1.00 40.64 ? 208 ASN A O 1 ATOM 1607 C CB . ASN A 1 208 ? -12.451 20.699 36.430 1.00 38.06 ? 208 ASN A CB 1 ATOM 1608 C CG . ASN A 1 208 ? -12.121 19.460 35.616 1.00 39.48 ? 208 ASN A CG 1 ATOM 1609 O OD1 . ASN A 1 208 ? -11.130 18.775 35.875 1.00 39.12 ? 208 ASN A OD1 1 ATOM 1610 N ND2 . ASN A 1 208 ? -12.964 19.158 34.633 1.00 39.67 ? 208 ASN A ND2 1 ATOM 1611 N N . THR A 1 209 ? -14.183 22.061 38.654 1.00 39.91 ? 209 THR A N 1 ATOM 1612 C CA . THR A 1 209 ? -14.657 23.273 39.324 1.00 40.63 ? 209 THR A CA 1 ATOM 1613 C C . THR A 1 209 ? -15.176 23.044 40.743 1.00 40.53 ? 209 THR A C 1 ATOM 1614 O O . THR A 1 209 ? -14.726 23.696 41.686 1.00 42.48 ? 209 THR A O 1 ATOM 1615 C CB . THR A 1 209 ? -15.739 24.025 38.488 1.00 41.40 ? 209 THR A CB 1 ATOM 1616 O OG1 . THR A 1 209 ? -16.935 23.241 38.406 1.00 40.35 ? 209 THR A OG1 1 ATOM 1617 C CG2 . THR A 1 209 ? -15.231 24.331 37.075 1.00 41.14 ? 209 THR A CG2 1 ATOM 1618 N N . GLY A 1 210 ? -16.101 22.099 40.885 1.00 40.39 ? 210 GLY A N 1 ATOM 1619 C CA . GLY A 1 210 ? -16.689 21.805 42.181 1.00 39.52 ? 210 GLY A CA 1 ATOM 1620 C C . GLY A 1 210 ? -18.145 22.229 42.219 1.00 39.96 ? 210 GLY A C 1 ATOM 1621 O O . GLY A 1 210 ? -18.814 22.046 43.240 1.00 40.73 ? 210 GLY A O 1 ATOM 1622 N N . GLU A 1 211 ? -18.631 22.777 41.099 1.00 39.47 ? 211 GLU A N 1 ATOM 1623 C CA . GLU A 1 211 ? -20.013 23.245 40.946 1.00 38.78 ? 211 GLU A CA 1 ATOM 1624 C C . GLU A 1 211 ? -21.011 22.090 40.856 1.00 38.48 ? 211 GLU A C 1 ATOM 1625 O O . GLU A 1 211 ? -20.688 21.019 40.342 1.00 38.05 ? 211 GLU A O 1 ATOM 1626 C CB . GLU A 1 211 ? -20.143 24.137 39.708 1.00 39.68 ? 211 GLU A CB 1 ATOM 1627 C CG . GLU A 1 211 ? -19.464 25.498 39.826 1.00 40.89 ? 211 GLU A CG 1 ATOM 1628 C CD . GLU A 1 211 ? -19.459 26.280 38.517 1.00 41.16 ? 211 GLU A CD 1 ATOM 1629 O OE1 . GLU A 1 211 ? -20.523 26.405 37.873 1.00 41.92 ? 211 GLU A OE1 1 ATOM 1630 O OE2 . GLU A 1 211 ? -18.383 26.783 38.132 1.00 42.15 ? 211 GLU A OE2 1 ATOM 1631 N N . GLY A 1 212 ? -22.219 22.325 41.362 1.00 38.25 ? 212 GLY A N 1 ATOM 1632 C CA . GLY A 1 212 ? -23.251 21.306 41.360 1.00 38.68 ? 212 GLY A CA 1 ATOM 1633 C C . GLY A 1 212 ? -23.365 20.617 42.708 1.00 38.78 ? 212 GLY A C 1 ATOM 1634 O O . GLY A 1 212 ? -22.643 20.958 43.651 1.00 38.52 ? 212 GLY A O 1 ATOM 1635 N N . GLN A 1 213 ? -24.270 19.644 42.789 1.00 38.77 ? 213 GLN A N 1 ATOM 1636 C CA . GLN A 1 213 ? -24.525 18.883 44.014 1.00 39.29 ? 213 GLN A CA 1 ATOM 1637 C C . GLN A 1 213 ? -24.483 17.369 43.806 1.00 37.80 ? 213 GLN A C 1 ATOM 1638 O O . GLN A 1 213 ? -24.664 16.874 42.690 1.00 37.50 ? 213 GLN A O 1 ATOM 1639 C CB . GLN A 1 213 ? -25.916 19.226 44.574 1.00 42.27 ? 213 GLN A CB 1 ATOM 1640 C CG . GLN A 1 213 ? -26.009 20.448 45.485 1.00 47.47 ? 213 GLN A CG 1 ATOM 1641 C CD . GLN A 1 213 ? -27.355 20.520 46.203 1.00 50.64 ? 213 GLN A CD 1 ATOM 1642 O OE1 . GLN A 1 213 ? -28.348 21.000 45.647 1.00 51.11 ? 213 GLN A OE1 1 ATOM 1643 N NE2 . GLN A 1 213 ? -27.396 20.021 47.440 1.00 52.00 ? 213 GLN A NE2 1 ATOM 1644 N N . TYR A 1 214 ? -24.230 16.640 44.894 1.00 34.92 ? 214 TYR A N 1 ATOM 1645 C CA . TYR A 1 214 ? -24.240 15.176 44.876 1.00 32.26 ? 214 TYR A CA 1 ATOM 1646 C C . TYR A 1 214 ? -25.712 14.818 45.101 1.00 30.44 ? 214 TYR A C 1 ATOM 1647 O O . TYR A 1 214 ? -26.461 15.620 45.675 1.00 30.38 ? 214 TYR A O 1 ATOM 1648 C CB . TYR A 1 214 ? -23.430 14.598 46.047 1.00 32.21 ? 214 TYR A CB 1 ATOM 1649 C CG . TYR A 1 214 ? -21.931 14.812 46.007 1.00 32.11 ? 214 TYR A CG 1 ATOM 1650 C CD1 . TYR A 1 214 ? -21.102 13.981 45.226 1.00 31.68 ? 214 TYR A CD1 1 ATOM 1651 C CD2 . TYR A 1 214 ? -21.322 15.837 46.768 1.00 32.08 ? 214 TYR A CD2 1 ATOM 1652 C CE1 . TYR A 1 214 ? -19.682 14.163 45.196 1.00 31.84 ? 214 TYR A CE1 1 ATOM 1653 C CE2 . TYR A 1 214 ? -19.903 16.031 46.749 1.00 31.38 ? 214 TYR A CE2 1 ATOM 1654 C CZ . TYR A 1 214 ? -19.100 15.188 45.959 1.00 30.99 ? 214 TYR A CZ 1 ATOM 1655 O OH . TYR A 1 214 ? -17.741 15.366 45.925 1.00 31.38 ? 214 TYR A OH 1 ATOM 1656 N N . ALA A 1 215 ? -26.141 13.646 44.638 1.00 28.16 ? 215 ALA A N 1 ATOM 1657 C CA . ALA A 1 215 ? -27.524 13.211 44.848 1.00 26.80 ? 215 ALA A CA 1 ATOM 1658 C C . ALA A 1 215 ? -27.665 12.876 46.330 1.00 26.13 ? 215 ALA A C 1 ATOM 1659 O O . ALA A 1 215 ? -26.801 12.214 46.908 1.00 25.45 ? 215 ALA A O 1 ATOM 1660 C CB . ALA A 1 215 ? -27.850 12.003 43.984 1.00 26.79 ? 215 ALA A CB 1 ATOM 1661 N N . ASN A 1 216 ? -28.720 13.389 46.948 1.00 25.57 ? 216 ASN A N 1 ATOM 1662 C CA . ASN A 1 216 ? -28.934 13.178 48.369 1.00 24.85 ? 216 ASN A CA 1 ATOM 1663 C C . ASN A 1 216 ? -30.171 12.347 48.695 1.00 25.34 ? 216 ASN A C 1 ATOM 1664 O O . ASN A 1 216 ? -31.303 12.832 48.618 1.00 27.31 ? 216 ASN A O 1 ATOM 1665 C CB . ASN A 1 216 ? -28.992 14.538 49.062 1.00 23.80 ? 216 ASN A CB 1 ATOM 1666 C CG . ASN A 1 216 ? -28.781 14.460 50.563 1.00 24.58 ? 216 ASN A CG 1 ATOM 1667 O OD1 . ASN A 1 216 ? -28.474 13.405 51.138 1.00 20.28 ? 216 ASN A OD1 1 ATOM 1668 N ND2 . ASN A 1 216 ? -28.931 15.626 51.182 1.00 26.96 ? 216 ASN A ND2 1 ATOM 1669 N N . VAL A 1 217 ? -29.932 11.096 49.081 1.00 25.85 ? 217 VAL A N 1 ATOM 1670 C CA . VAL A 1 217 ? -31.000 10.174 49.452 1.00 27.88 ? 217 VAL A CA 1 ATOM 1671 C C . VAL A 1 217 ? -31.068 10.081 50.970 1.00 28.33 ? 217 VAL A C 1 ATOM 1672 O O . VAL A 1 217 ? -30.075 9.751 51.626 1.00 25.91 ? 217 VAL A O 1 ATOM 1673 C CB . VAL A 1 217 ? -30.771 8.755 48.868 1.00 28.70 ? 217 VAL A CB 1 ATOM 1674 C CG1 . VAL A 1 217 ? -31.928 7.827 49.218 1.00 27.34 ? 217 VAL A CG1 1 ATOM 1675 C CG2 . VAL A 1 217 ? -30.614 8.824 47.372 1.00 27.81 ? 217 VAL A CG2 1 ATOM 1676 N N . THR A 1 218 ? -32.252 10.363 51.511 1.00 29.08 ? 218 THR A N 1 ATOM 1677 C CA . THR A 1 218 ? -32.464 10.296 52.949 1.00 29.84 ? 218 THR A CA 1 ATOM 1678 C C . THR A 1 218 ? -33.017 8.928 53.352 1.00 28.68 ? 218 THR A C 1 ATOM 1679 O O . THR A 1 218 ? -34.078 8.499 52.881 1.00 27.31 ? 218 THR A O 1 ATOM 1680 C CB . THR A 1 218 ? -33.378 11.443 53.468 1.00 31.92 ? 218 THR A CB 1 ATOM 1681 O OG1 . THR A 1 218 ? -32.953 12.685 52.890 1.00 33.24 ? 218 THR A OG1 1 ATOM 1682 C CG2 . THR A 1 218 ? -33.280 11.568 55.009 1.00 30.97 ? 218 THR A CG2 1 ATOM 1683 N N . LEU A 1 219 ? -32.225 8.230 54.163 1.00 27.20 ? 219 LEU A N 1 ATOM 1684 C CA . LEU A 1 219 ? -32.568 6.917 54.697 1.00 27.18 ? 219 LEU A CA 1 ATOM 1685 C C . LEU A 1 219 ? -33.135 7.077 56.107 1.00 25.71 ? 219 LEU A C 1 ATOM 1686 O O . LEU A 1 219 ? -32.625 7.881 56.892 1.00 24.30 ? 219 LEU A O 1 ATOM 1687 C CB . LEU A 1 219 ? -31.325 6.020 54.768 1.00 28.22 ? 219 LEU A CB 1 ATOM 1688 C CG . LEU A 1 219 ? -30.638 5.533 53.492 1.00 27.98 ? 219 LEU A CG 1 ATOM 1689 C CD1 . LEU A 1 219 ? -29.328 4.874 53.853 1.00 28.59 ? 219 LEU A CD1 1 ATOM 1690 C CD2 . LEU A 1 219 ? -31.518 4.559 52.734 1.00 27.61 ? 219 LEU A CD2 1 ATOM 1691 N N . THR A 1 220 ? -34.207 6.340 56.403 1.00 24.61 ? 220 THR A N 1 ATOM 1692 C CA . THR A 1 220 ? -34.843 6.362 57.722 1.00 23.69 ? 220 THR A CA 1 ATOM 1693 C C . THR A 1 220 ? -34.269 5.174 58.514 1.00 24.07 ? 220 THR A C 1 ATOM 1694 O O . THR A 1 220 ? -34.391 4.026 58.068 1.00 21.74 ? 220 THR A O 1 ATOM 1695 C CB . THR A 1 220 ? -36.385 6.265 57.609 1.00 23.17 ? 220 THR A CB 1 ATOM 1696 O OG1 . THR A 1 220 ? -36.865 7.358 56.818 1.00 25.28 ? 220 THR A OG1 1 ATOM 1697 C CG2 . THR A 1 220 ? -37.052 6.344 58.989 1.00 23.30 ? 220 THR A CG2 1 ATOM 1698 N N . PRO A 1 221 ? -33.625 5.438 59.689 1.00 24.67 ? 221 PRO A N 1 ATOM 1699 C CA . PRO A 1 221 ? -33.018 4.414 60.559 1.00 23.58 ? 221 PRO A CA 1 ATOM 1700 C C . PRO A 1 221 ? -33.906 3.228 60.950 1.00 24.00 ? 221 PRO A C 1 ATOM 1701 O O . PRO A 1 221 ? -35.001 3.408 61.483 1.00 25.64 ? 221 PRO A O 1 ATOM 1702 C CB . PRO A 1 221 ? -32.600 5.222 61.785 1.00 23.59 ? 221 PRO A CB 1 ATOM 1703 C CG . PRO A 1 221 ? -32.234 6.528 61.209 1.00 23.55 ? 221 PRO A CG 1 ATOM 1704 C CD . PRO A 1 221 ? -33.378 6.781 60.261 1.00 24.51 ? 221 PRO A CD 1 ATOM 1705 N N . GLY A 1 222 ? -33.442 2.026 60.607 1.00 24.59 ? 222 GLY A N 1 ATOM 1706 C CA . GLY A 1 222 ? -34.159 0.802 60.926 1.00 25.09 ? 222 GLY A CA 1 ATOM 1707 C C . GLY A 1 222 ? -35.188 0.296 59.940 1.00 25.37 ? 222 GLY A C 1 ATOM 1708 O O . GLY A 1 222 ? -35.738 -0.799 60.113 1.00 24.85 ? 222 GLY A O 1 ATOM 1709 N N . LYS A 1 223 ? -35.443 1.086 58.903 1.00 25.89 ? 223 LYS A N 1 ATOM 1710 C CA . LYS A 1 223 ? -36.421 0.722 57.892 1.00 26.82 ? 223 LYS A CA 1 ATOM 1711 C C . LYS A 1 223 ? -35.782 0.201 56.601 1.00 27.74 ? 223 LYS A C 1 ATOM 1712 O O . LYS A 1 223 ? -34.696 0.630 56.207 1.00 28.10 ? 223 LYS A O 1 ATOM 1713 C CB . LYS A 1 223 ? -37.346 1.910 57.605 1.00 25.55 ? 223 LYS A CB 1 ATOM 1714 C CG . LYS A 1 223 ? -38.128 2.431 58.812 1.00 26.40 ? 223 LYS A CG 1 ATOM 1715 C CD . LYS A 1 223 ? -39.149 1.434 59.346 1.00 27.31 ? 223 LYS A CD 1 ATOM 1716 C CE . LYS A 1 223 ? -39.969 2.030 60.489 1.00 29.52 ? 223 LYS A CE 1 ATOM 1717 N NZ . LYS A 1 223 ? -41.158 1.195 60.845 1.00 29.88 ? 223 LYS A NZ 1 ATOM 1718 N N . ARG A 1 224 ? -36.462 -0.753 55.971 1.00 28.09 ? 224 ARG A N 1 ATOM 1719 C CA . ARG A 1 224 ? -36.012 -1.364 54.723 1.00 28.85 ? 224 ARG A CA 1 ATOM 1720 C C . ARG A 1 224 ? -36.489 -0.503 53.535 1.00 27.55 ? 224 ARG A C 1 ATOM 1721 O O . ARG A 1 224 ? -37.693 -0.329 53.319 1.00 29.20 ? 224 ARG A O 1 ATOM 1722 C CB . ARG A 1 224 ? -36.549 -2.800 54.636 1.00 31.24 ? 224 ARG A CB 1 ATOM 1723 C CG . ARG A 1 224 ? -36.263 -3.664 55.877 1.00 35.23 ? 224 ARG A CG 1 ATOM 1724 C CD . ARG A 1 224 ? -37.141 -4.915 55.955 1.00 38.94 ? 224 ARG A CD 1 ATOM 1725 N NE . ARG A 1 224 ? -38.571 -4.592 56.026 1.00 42.90 ? 224 ARG A NE 1 ATOM 1726 C CZ . ARG A 1 224 ? -39.504 -5.346 56.611 1.00 44.62 ? 224 ARG A CZ 1 ATOM 1727 N NH1 . ARG A 1 224 ? -40.770 -4.945 56.600 1.00 44.69 ? 224 ARG A NH1 1 ATOM 1728 N NH2 . ARG A 1 224 ? -39.185 -6.484 57.222 1.00 45.05 ? 224 ARG A NH2 1 ATOM 1729 N N . HIS A 1 225 ? -35.529 0.066 52.806 1.00 25.57 ? 225 HIS A N 1 ATOM 1730 C CA . HIS A 1 225 ? -35.799 0.940 51.656 1.00 24.21 ? 225 HIS A CA 1 ATOM 1731 C C . HIS A 1 225 ? -35.613 0.288 50.288 1.00 21.88 ? 225 HIS A C 1 ATOM 1732 O O . HIS A 1 225 ? -34.523 -0.197 49.986 1.00 21.23 ? 225 HIS A O 1 ATOM 1733 C CB . HIS A 1 225 ? -34.867 2.151 51.678 1.00 24.79 ? 225 HIS A CB 1 ATOM 1734 C CG . HIS A 1 225 ? -34.949 2.970 52.921 1.00 25.81 ? 225 HIS A CG 1 ATOM 1735 N ND1 . HIS A 1 225 ? -34.403 2.556 54.115 1.00 27.22 ? 225 HIS A ND1 1 ATOM 1736 C CD2 . HIS A 1 225 ? -35.468 4.199 53.146 1.00 26.61 ? 225 HIS A CD2 1 ATOM 1737 C CE1 . HIS A 1 225 ? -34.581 3.498 55.022 1.00 27.67 ? 225 HIS A CE1 1 ATOM 1738 N NE2 . HIS A 1 225 ? -35.224 4.505 54.461 1.00 27.81 ? 225 HIS A NE2 1 ATOM 1739 N N . ARG A 1 226 ? -36.649 0.330 49.447 1.00 20.66 ? 226 ARG A N 1 ATOM 1740 C CA . ARG A 1 226 ? -36.556 -0.215 48.085 1.00 18.89 ? 226 ARG A CA 1 ATOM 1741 C C . ARG A 1 226 ? -35.997 0.882 47.183 1.00 17.49 ? 226 ARG A C 1 ATOM 1742 O O . ARG A 1 226 ? -36.530 1.995 47.161 1.00 17.79 ? 226 ARG A O 1 ATOM 1743 C CB . ARG A 1 226 ? -37.921 -0.665 47.532 1.00 18.35 ? 226 ARG A CB 1 ATOM 1744 C CG . ARG A 1 226 ? -37.874 -1.297 46.107 1.00 17.93 ? 226 ARG A CG 1 ATOM 1745 C CD . ARG A 1 226 ? -39.267 -1.484 45.502 1.00 17.18 ? 226 ARG A CD 1 ATOM 1746 N NE . ARG A 1 226 ? -39.259 -2.219 44.235 1.00 16.02 ? 226 ARG A NE 1 ATOM 1747 C CZ . ARG A 1 226 ? -40.214 -3.063 43.834 1.00 17.24 ? 226 ARG A CZ 1 ATOM 1748 N NH1 . ARG A 1 226 ? -41.272 -3.301 44.598 1.00 13.02 ? 226 ARG A NH1 1 ATOM 1749 N NH2 . ARG A 1 226 ? -40.137 -3.640 42.636 1.00 16.12 ? 226 ARG A NH2 1 ATOM 1750 N N . LEU A 1 227 ? -34.906 0.569 46.483 1.00 14.60 ? 227 LEU A N 1 ATOM 1751 C CA . LEU A 1 227 ? -34.281 1.503 45.550 1.00 13.39 ? 227 LEU A CA 1 ATOM 1752 C C . LEU A 1 227 ? -34.299 0.905 44.140 1.00 12.51 ? 227 LEU A C 1 ATOM 1753 O O . LEU A 1 227 ? -33.850 -0.218 43.919 1.00 13.89 ? 227 LEU A O 1 ATOM 1754 C CB . LEU A 1 227 ? -32.850 1.845 45.980 1.00 10.35 ? 227 LEU A CB 1 ATOM 1755 C CG . LEU A 1 227 ? -32.162 3.012 45.261 1.00 7.20 ? 227 LEU A CG 1 ATOM 1756 C CD1 . LEU A 1 227 ? -32.841 4.331 45.579 1.00 5.88 ? 227 LEU A CD1 1 ATOM 1757 C CD2 . LEU A 1 227 ? -30.701 3.042 45.641 1.00 5.54 ? 227 LEU A CD2 1 ATOM 1758 N N . ARG A 1 228 ? -34.821 1.679 43.196 1.00 11.56 ? 228 ARG A N 1 ATOM 1759 C CA . ARG A 1 228 ? -34.954 1.260 41.799 1.00 11.88 ? 228 ARG A CA 1 ATOM 1760 C C . ARG A 1 228 ? -33.861 1.904 40.944 1.00 10.61 ? 228 ARG A C 1 ATOM 1761 O O . ARG A 1 228 ? -34.025 3.019 40.430 1.00 9.80 ? 228 ARG A O 1 ATOM 1762 C CB . ARG A 1 228 ? -36.354 1.638 41.304 1.00 12.75 ? 228 ARG A CB 1 ATOM 1763 C CG . ARG A 1 228 ? -37.484 1.116 42.197 1.00 10.57 ? 228 ARG A CG 1 ATOM 1764 C CD . ARG A 1 228 ? -38.797 1.770 41.857 1.00 12.55 ? 228 ARG A CD 1 ATOM 1765 N NE . ARG A 1 228 ? -39.889 1.219 42.646 1.00 12.60 ? 228 ARG A NE 1 ATOM 1766 C CZ . ARG A 1 228 ? -40.729 0.273 42.232 1.00 14.40 ? 228 ARG A CZ 1 ATOM 1767 N NH1 . ARG A 1 228 ? -40.633 -0.252 41.013 1.00 13.45 ? 228 ARG A NH1 1 ATOM 1768 N NH2 . ARG A 1 228 ? -41.656 -0.171 43.062 1.00 15.27 ? 228 ARG A NH2 1 ATOM 1769 N N . ILE A 1 229 ? -32.722 1.210 40.870 1.00 9.29 ? 229 ILE A N 1 ATOM 1770 C CA . ILE A 1 229 ? -31.532 1.648 40.132 1.00 8.06 ? 229 ILE A CA 1 ATOM 1771 C C . ILE A 1 229 ? -31.638 1.362 38.619 1.00 8.67 ? 229 ILE A C 1 ATOM 1772 O O . ILE A 1 229 ? -32.013 0.270 38.213 1.00 6.25 ? 229 ILE A O 1 ATOM 1773 C CB . ILE A 1 229 ? -30.256 0.974 40.714 1.00 7.23 ? 229 ILE A CB 1 ATOM 1774 C CG1 . ILE A 1 229 ? -30.252 1.108 42.249 1.00 6.93 ? 229 ILE A CG1 1 ATOM 1775 C CG2 . ILE A 1 229 ? -28.992 1.623 40.143 1.00 2.98 ? 229 ILE A CG2 1 ATOM 1776 C CD1 . ILE A 1 229 ? -29.209 0.271 42.956 1.00 5.69 ? 229 ILE A CD1 1 ATOM 1777 N N . LEU A 1 230 ? -31.354 2.379 37.808 1.00 10.52 ? 230 LEU A N 1 ATOM 1778 C CA . LEU A 1 230 ? -31.398 2.269 36.344 1.00 12.98 ? 230 LEU A CA 1 ATOM 1779 C C . LEU A 1 230 ? -30.124 2.815 35.721 1.00 12.66 ? 230 LEU A C 1 ATOM 1780 O O . LEU A 1 230 ? -29.501 3.740 36.250 1.00 14.03 ? 230 LEU A O 1 ATOM 1781 C CB . LEU A 1 230 ? -32.549 3.086 35.733 1.00 10.92 ? 230 LEU A CB 1 ATOM 1782 C CG . LEU A 1 230 ? -34.008 3.057 36.170 1.00 13.39 ? 230 LEU A CG 1 ATOM 1783 C CD1 . LEU A 1 230 ? -34.246 3.996 37.333 1.00 13.26 ? 230 LEU A CD1 1 ATOM 1784 C CD2 . LEU A 1 230 ? -34.862 3.455 34.991 1.00 13.33 ? 230 LEU A CD2 1 ATOM 1785 N N . ASN A 1 231 ? -29.756 2.228 34.590 1.00 12.87 ? 231 ASN A N 1 ATOM 1786 C CA . ASN A 1 231 ? -28.613 2.670 33.814 1.00 12.40 ? 231 ASN A CA 1 ATOM 1787 C C . ASN A 1 231 ? -29.233 3.175 32.507 1.00 12.62 ? 231 ASN A C 1 ATOM 1788 O O . ASN A 1 231 ? -29.599 2.384 31.633 1.00 10.20 ? 231 ASN A O 1 ATOM 1789 C CB . ASN A 1 231 ? -27.636 1.521 33.547 1.00 11.49 ? 231 ASN A CB 1 ATOM 1790 C CG . ASN A 1 231 ? -26.367 1.981 32.835 1.00 9.99 ? 231 ASN A CG 1 ATOM 1791 O OD1 . ASN A 1 231 ? -26.231 3.147 32.475 1.00 10.67 ? 231 ASN A OD1 1 ATOM 1792 N ND2 . ASN A 1 231 ? -25.425 1.067 32.654 1.00 9.94 ? 231 ASN A ND2 1 ATOM 1793 N N . THR A 1 232 ? -29.375 4.494 32.397 1.00 13.05 ? 232 THR A N 1 ATOM 1794 C CA . THR A 1 232 ? -29.969 5.094 31.206 1.00 12.37 ? 232 THR A CA 1 ATOM 1795 C C . THR A 1 232 ? -28.929 5.686 30.251 1.00 13.59 ? 232 THR A C 1 ATOM 1796 O O . THR A 1 232 ? -29.254 6.540 29.411 1.00 15.31 ? 232 THR A O 1 ATOM 1797 C CB . THR A 1 232 ? -31.042 6.155 31.574 1.00 12.12 ? 232 THR A CB 1 ATOM 1798 O OG1 . THR A 1 232 ? -30.426 7.295 32.174 1.00 12.42 ? 232 THR A OG1 1 ATOM 1799 C CG2 . THR A 1 232 ? -32.101 5.571 32.525 1.00 13.22 ? 232 THR A CG2 1 ATOM 1800 N N . SER A 1 233 ? -27.696 5.180 30.363 1.00 12.58 ? 233 SER A N 1 ATOM 1801 C CA . SER A 1 233 ? -26.542 5.603 29.560 1.00 13.26 ? 233 SER A CA 1 ATOM 1802 C C . SER A 1 233 ? -26.620 5.382 28.058 1.00 12.13 ? 233 SER A C 1 ATOM 1803 O O . SER A 1 233 ? -27.530 4.720 27.560 1.00 11.92 ? 233 SER A O 1 ATOM 1804 C CB . SER A 1 233 ? -25.281 4.893 30.045 1.00 14.41 ? 233 SER A CB 1 ATOM 1805 O OG . SER A 1 233 ? -24.849 5.363 31.310 1.00 18.91 ? 233 SER A OG 1 ATOM 1806 N N . THR A 1 234 ? -25.659 5.969 27.348 1.00 12.15 ? 234 THR A N 1 ATOM 1807 C CA . THR A 1 234 ? -25.542 5.814 25.901 1.00 10.88 ? 234 THR A CA 1 ATOM 1808 C C . THR A 1 234 ? -24.410 4.843 25.611 1.00 11.40 ? 234 THR A C 1 ATOM 1809 O O . THR A 1 234 ? -24.409 4.205 24.569 1.00 13.07 ? 234 THR A O 1 ATOM 1810 C CB . THR A 1 234 ? -25.274 7.145 25.156 1.00 9.85 ? 234 THR A CB 1 ATOM 1811 O OG1 . THR A 1 234 ? -24.205 7.870 25.777 1.00 10.03 ? 234 THR A OG1 1 ATOM 1812 C CG2 . THR A 1 234 ? -26.520 7.986 25.098 1.00 8.53 ? 234 THR A CG2 1 ATOM 1813 N N . GLU A 1 235 ? -23.455 4.736 26.540 1.00 11.37 ? 235 GLU A N 1 ATOM 1814 C CA . GLU A 1 235 ? -22.311 3.831 26.392 1.00 13.14 ? 235 GLU A CA 1 ATOM 1815 C C . GLU A 1 235 ? -21.844 3.271 27.725 1.00 11.90 ? 235 GLU A C 1 ATOM 1816 O O . GLU A 1 235 ? -21.570 2.083 27.815 1.00 12.72 ? 235 GLU A O 1 ATOM 1817 C CB . GLU A 1 235 ? -21.132 4.522 25.684 1.00 14.58 ? 235 GLU A CB 1 ATOM 1818 C CG . GLU A 1 235 ? -19.972 3.599 25.231 1.00 17.32 ? 235 GLU A CG 1 ATOM 1819 C CD . GLU A 1 235 ? -18.865 3.384 26.271 1.00 20.80 ? 235 GLU A CD 1 ATOM 1820 O OE1 . GLU A 1 235 ? -18.697 4.232 27.173 1.00 22.76 ? 235 GLU A OE1 1 ATOM 1821 O OE2 . GLU A 1 235 ? -18.167 2.349 26.194 1.00 22.78 ? 235 GLU A OE2 1 ATOM 1822 N N . ASN A 1 236 ? -21.692 4.129 28.730 1.00 10.86 ? 236 ASN A N 1 ATOM 1823 C CA . ASN A 1 236 ? -21.219 3.722 30.062 1.00 9.40 ? 236 ASN A CA 1 ATOM 1824 C C . ASN A 1 236 ? -21.980 2.596 30.783 1.00 8.76 ? 236 ASN A C 1 ATOM 1825 O O . ASN A 1 236 ? -23.207 2.621 30.872 1.00 6.33 ? 236 ASN A O 1 ATOM 1826 C CB . ASN A 1 236 ? -21.182 4.932 30.993 1.00 9.25 ? 236 ASN A CB 1 ATOM 1827 C CG . ASN A 1 236 ? -19.949 5.820 30.805 1.00 7.16 ? 236 ASN A CG 1 ATOM 1828 O OD1 . ASN A 1 236 ? -19.652 6.622 31.676 1.00 6.83 ? 236 ASN A OD1 1 ATOM 1829 N ND2 . ASN A 1 236 ? -19.278 5.727 29.664 1.00 8.53 ? 236 ASN A ND2 1 ATOM 1830 N N . HIS A 1 237 ? -21.226 1.590 31.238 1.00 8.94 ? 237 HIS A N 1 ATOM 1831 C CA . HIS A 1 237 ? -21.751 0.454 31.994 1.00 7.30 ? 237 HIS A CA 1 ATOM 1832 C C . HIS A 1 237 ? -21.202 0.625 33.408 1.00 8.71 ? 237 HIS A C 1 ATOM 1833 O O . HIS A 1 237 ? -19.985 0.719 33.619 1.00 7.62 ? 237 HIS A O 1 ATOM 1834 C CB . HIS A 1 237 ? -21.267 -0.860 31.426 1.00 5.41 ? 237 HIS A CB 1 ATOM 1835 C CG . HIS A 1 237 ? -21.682 -1.107 30.016 1.00 6.36 ? 237 HIS A CG 1 ATOM 1836 N ND1 . HIS A 1 237 ? -21.250 -0.328 28.968 1.00 4.70 ? 237 HIS A ND1 1 ATOM 1837 C CD2 . HIS A 1 237 ? -22.427 -2.093 29.469 1.00 6.91 ? 237 HIS A CD2 1 ATOM 1838 C CE1 . HIS A 1 237 ? -21.707 -0.831 27.837 1.00 6.95 ? 237 HIS A CE1 1 ATOM 1839 N NE2 . HIS A 1 237 ? -22.427 -1.899 28.115 1.00 6.68 ? 237 HIS A NE2 1 ATOM 1840 N N . PHE A 1 238 ? -22.111 0.621 34.372 1.00 9.28 ? 238 PHE A N 1 ATOM 1841 C CA . PHE A 1 238 ? -21.765 0.872 35.756 1.00 8.70 ? 238 PHE A CA 1 ATOM 1842 C C . PHE A 1 238 ? -21.714 -0.264 36.735 1.00 9.87 ? 238 PHE A C 1 ATOM 1843 O O . PHE A 1 238 ? -22.434 -1.254 36.614 1.00 10.94 ? 238 PHE A O 1 ATOM 1844 C CB . PHE A 1 238 ? -22.738 1.885 36.335 1.00 10.05 ? 238 PHE A CB 1 ATOM 1845 C CG . PHE A 1 238 ? -22.865 3.138 35.544 1.00 8.69 ? 238 PHE A CG 1 ATOM 1846 C CD1 . PHE A 1 238 ? -21.733 3.899 35.208 1.00 8.53 ? 238 PHE A CD1 1 ATOM 1847 C CD2 . PHE A 1 238 ? -24.129 3.592 35.167 1.00 7.73 ? 238 PHE A CD2 1 ATOM 1848 C CE1 . PHE A 1 238 ? -21.860 5.104 34.511 1.00 8.01 ? 238 PHE A CE1 1 ATOM 1849 C CE2 . PHE A 1 238 ? -24.278 4.801 34.464 1.00 10.12 ? 238 PHE A CE2 1 ATOM 1850 C CZ . PHE A 1 238 ? -23.140 5.562 34.136 1.00 10.36 ? 238 PHE A CZ 1 ATOM 1851 N N . GLN A 1 239 ? -20.869 -0.060 37.739 1.00 10.48 ? 239 GLN A N 1 ATOM 1852 C CA . GLN A 1 239 ? -20.708 -0.966 38.871 1.00 13.15 ? 239 GLN A CA 1 ATOM 1853 C C . GLN A 1 239 ? -21.147 -0.071 40.018 1.00 10.36 ? 239 GLN A C 1 ATOM 1854 O O . GLN A 1 239 ? -20.663 1.056 40.144 1.00 11.10 ? 239 GLN A O 1 ATOM 1855 C CB . GLN A 1 239 ? -19.253 -1.395 39.076 1.00 15.05 ? 239 GLN A CB 1 ATOM 1856 C CG . GLN A 1 239 ? -18.630 -2.103 37.881 1.00 18.08 ? 239 GLN A CG 1 ATOM 1857 C CD . GLN A 1 239 ? -17.283 -2.737 38.183 1.00 19.38 ? 239 GLN A CD 1 ATOM 1858 O OE1 . GLN A 1 239 ? -16.992 -3.830 37.699 1.00 19.60 ? 239 GLN A OE1 1 ATOM 1859 N NE2 . GLN A 1 239 ? -16.434 -2.034 38.935 1.00 19.38 ? 239 GLN A NE2 1 ATOM 1860 N N . VAL A 1 240 ? -22.153 -0.507 40.762 1.00 9.40 ? 240 VAL A N 1 ATOM 1861 C CA . VAL A 1 240 ? -22.649 0.288 41.881 1.00 12.32 ? 240 VAL A CA 1 ATOM 1862 C C . VAL A 1 240 ? -22.487 -0.397 43.235 1.00 12.73 ? 240 VAL A C 1 ATOM 1863 O O . VAL A 1 240 ? -22.635 -1.615 43.331 1.00 13.51 ? 240 VAL A O 1 ATOM 1864 C CB . VAL A 1 240 ? -24.122 0.763 41.665 1.00 11.46 ? 240 VAL A CB 1 ATOM 1865 C CG1 . VAL A 1 240 ? -24.212 1.704 40.487 1.00 10.55 ? 240 VAL A CG1 1 ATOM 1866 C CG2 . VAL A 1 240 ? -25.071 -0.396 41.485 1.00 12.68 ? 240 VAL A CG2 1 ATOM 1867 N N . SER A 1 241 ? -22.144 0.389 44.260 1.00 13.64 ? 241 SER A N 1 ATOM 1868 C CA . SER A 1 241 ? -21.951 -0.111 45.635 1.00 14.39 ? 241 SER A CA 1 ATOM 1869 C C . SER A 1 241 ? -22.153 0.988 46.661 1.00 13.98 ? 241 SER A C 1 ATOM 1870 O O . SER A 1 241 ? -21.860 2.153 46.390 1.00 15.34 ? 241 SER A O 1 ATOM 1871 C CB . SER A 1 241 ? -20.540 -0.698 45.827 1.00 15.71 ? 241 SER A CB 1 ATOM 1872 O OG . SER A 1 241 ? -19.527 0.296 45.706 1.00 17.75 ? 241 SER A OG 1 ATOM 1873 N N . LEU A 1 242 ? -22.635 0.606 47.840 1.00 13.35 ? 242 LEU A N 1 ATOM 1874 C CA . LEU A 1 242 ? -22.851 1.547 48.932 1.00 14.05 ? 242 LEU A CA 1 ATOM 1875 C C . LEU A 1 242 ? -21.887 1.174 50.047 1.00 12.77 ? 242 LEU A C 1 ATOM 1876 O O . LEU A 1 242 ? -21.840 0.018 50.464 1.00 12.85 ? 242 LEU A O 1 ATOM 1877 C CB . LEU A 1 242 ? -24.311 1.501 49.418 1.00 16.98 ? 242 LEU A CB 1 ATOM 1878 C CG . LEU A 1 242 ? -24.804 2.457 50.524 1.00 18.02 ? 242 LEU A CG 1 ATOM 1879 C CD1 . LEU A 1 242 ? -24.548 3.921 50.207 1.00 18.70 ? 242 LEU A CD1 1 ATOM 1880 C CD2 . LEU A 1 242 ? -26.281 2.240 50.727 1.00 18.26 ? 242 LEU A CD2 1 ATOM 1881 N N . VAL A 1 243 ? -21.086 2.148 50.477 1.00 13.29 ? 243 VAL A N 1 ATOM 1882 C CA . VAL A 1 243 ? -20.088 1.976 51.544 1.00 15.62 ? 243 VAL A CA 1 ATOM 1883 C C . VAL A 1 243 ? -20.743 1.489 52.848 1.00 17.20 ? 243 VAL A C 1 ATOM 1884 O O . VAL A 1 243 ? -21.752 2.042 53.287 1.00 17.51 ? 243 VAL A O 1 ATOM 1885 C CB . VAL A 1 243 ? -19.278 3.309 51.769 1.00 15.96 ? 243 VAL A CB 1 ATOM 1886 C CG1 . VAL A 1 243 ? -18.382 3.233 53.020 1.00 12.16 ? 243 VAL A CG1 1 ATOM 1887 C CG2 . VAL A 1 243 ? -18.417 3.607 50.541 1.00 12.78 ? 243 VAL A CG2 1 ATOM 1888 N N . ASN A 1 244 ? -20.193 0.398 53.388 1.00 20.66 ? 244 ASN A N 1 ATOM 1889 C CA . ASN A 1 244 ? -20.650 -0.269 54.619 1.00 23.60 ? 244 ASN A CA 1 ATOM 1890 C C . ASN A 1 244 ? -22.012 -0.975 54.577 1.00 22.86 ? 244 ASN A C 1 ATOM 1891 O O . ASN A 1 244 ? -22.500 -1.434 55.617 1.00 23.40 ? 244 ASN A O 1 ATOM 1892 C CB . ASN A 1 244 ? -20.569 0.668 55.842 1.00 26.76 ? 244 ASN A CB 1 ATOM 1893 C CG . ASN A 1 244 ? -19.247 0.559 56.587 1.00 32.41 ? 244 ASN A CG 1 ATOM 1894 O OD1 . ASN A 1 244 ? -19.081 1.167 57.653 1.00 35.00 ? 244 ASN A OD1 1 ATOM 1895 N ND2 . ASN A 1 244 ? -18.308 -0.217 56.049 1.00 33.70 ? 244 ASN A ND2 1 ATOM 1896 N N . HIS A 1 245 ? -22.619 -1.064 53.389 1.00 20.96 ? 245 HIS A N 1 ATOM 1897 C CA . HIS A 1 245 ? -23.922 -1.724 53.221 1.00 19.24 ? 245 HIS A CA 1 ATOM 1898 C C . HIS A 1 245 ? -23.950 -2.746 52.105 1.00 20.29 ? 245 HIS A C 1 ATOM 1899 O O . HIS A 1 245 ? -23.131 -2.717 51.180 1.00 21.78 ? 245 HIS A O 1 ATOM 1900 C CB . HIS A 1 245 ? -25.040 -0.736 52.885 1.00 17.13 ? 245 HIS A CB 1 ATOM 1901 C CG . HIS A 1 245 ? -25.263 0.324 53.909 1.00 16.43 ? 245 HIS A CG 1 ATOM 1902 N ND1 . HIS A 1 245 ? -24.350 1.326 54.148 1.00 14.65 ? 245 HIS A ND1 1 ATOM 1903 C CD2 . HIS A 1 245 ? -26.312 0.561 54.730 1.00 16.29 ? 245 HIS A CD2 1 ATOM 1904 C CE1 . HIS A 1 245 ? -24.828 2.137 55.074 1.00 14.53 ? 245 HIS A CE1 1 ATOM 1905 N NE2 . HIS A 1 245 ? -26.017 1.696 55.442 1.00 15.77 ? 245 HIS A NE2 1 ATOM 1906 N N . THR A 1 246 ? -24.952 -3.617 52.191 1.00 18.97 ? 246 THR A N 1 ATOM 1907 C CA . THR A 1 246 ? -25.207 -4.638 51.192 1.00 16.66 ? 246 THR A CA 1 ATOM 1908 C C . THR A 1 246 ? -26.487 -4.201 50.484 1.00 15.77 ? 246 THR A C 1 ATOM 1909 O O . THR A 1 246 ? -27.212 -3.322 50.969 1.00 13.26 ? 246 THR A O 1 ATOM 1910 C CB . THR A 1 246 ? -25.431 -6.047 51.815 1.00 17.87 ? 246 THR A CB 1 ATOM 1911 O OG1 . THR A 1 246 ? -26.521 -6.010 52.749 1.00 16.51 ? 246 THR A OG1 1 ATOM 1912 C CG2 . THR A 1 246 ? -24.168 -6.562 52.494 1.00 13.47 ? 246 THR A CG2 1 ATOM 1913 N N . MET A 1 247 ? -26.703 -4.748 49.289 1.00 15.58 ? 247 MET A N 1 ATOM 1914 C CA . MET A 1 247 ? -27.892 -4.462 48.491 1.00 13.34 ? 247 MET A CA 1 ATOM 1915 C C . MET A 1 247 ? -28.562 -5.808 48.224 1.00 12.14 ? 247 MET A C 1 ATOM 1916 O O . MET A 1 247 ? -27.883 -6.774 47.887 1.00 12.34 ? 247 MET A O 1 ATOM 1917 C CB . MET A 1 247 ? -27.501 -3.769 47.186 1.00 13.82 ? 247 MET A CB 1 ATOM 1918 C CG . MET A 1 247 ? -26.965 -2.354 47.369 1.00 14.25 ? 247 MET A CG 1 ATOM 1919 S SD . MET A 1 247 ? -26.685 -1.469 45.827 1.00 19.11 ? 247 MET A SD 1 ATOM 1920 C CE . MET A 1 247 ? -25.288 -2.370 45.165 1.00 16.12 ? 247 MET A CE 1 ATOM 1921 N N . THR A 1 248 ? -29.868 -5.891 48.474 1.00 11.99 ? 248 THR A N 1 ATOM 1922 C CA . THR A 1 248 ? -30.612 -7.128 48.264 1.00 11.18 ? 248 THR A CA 1 ATOM 1923 C C . THR A 1 248 ? -31.521 -6.977 47.063 1.00 11.54 ? 248 THR A C 1 ATOM 1924 O O . THR A 1 248 ? -32.580 -6.358 47.153 1.00 11.98 ? 248 THR A O 1 ATOM 1925 C CB . THR A 1 248 ? -31.437 -7.543 49.506 1.00 12.75 ? 248 THR A CB 1 ATOM 1926 O OG1 . THR A 1 248 ? -30.627 -7.444 50.688 1.00 15.13 ? 248 THR A OG1 1 ATOM 1927 C CG2 . THR A 1 248 ? -31.893 -8.988 49.365 1.00 13.23 ? 248 THR A CG2 1 ATOM 1928 N N . VAL A 1 249 ? -31.098 -7.573 45.950 1.00 11.61 ? 249 VAL A N 1 ATOM 1929 C CA . VAL A 1 249 ? -31.826 -7.524 44.684 1.00 12.97 ? 249 VAL A CA 1 ATOM 1930 C C . VAL A 1 249 ? -33.138 -8.300 44.742 1.00 14.08 ? 249 VAL A C 1 ATOM 1931 O O . VAL A 1 249 ? -33.167 -9.477 45.108 1.00 14.35 ? 249 VAL A O 1 ATOM 1932 C CB . VAL A 1 249 ? -30.965 -8.079 43.507 1.00 13.69 ? 249 VAL A CB 1 ATOM 1933 C CG1 . VAL A 1 249 ? -31.667 -7.892 42.176 1.00 13.78 ? 249 VAL A CG1 1 ATOM 1934 C CG2 . VAL A 1 249 ? -29.625 -7.395 43.469 1.00 16.58 ? 249 VAL A CG2 1 ATOM 1935 N N . ILE A 1 250 ? -34.224 -7.601 44.434 1.00 13.63 ? 250 ILE A N 1 ATOM 1936 C CA . ILE A 1 250 ? -35.543 -8.214 44.401 1.00 14.02 ? 250 ILE A CA 1 ATOM 1937 C C . ILE A 1 250 ? -36.117 -8.239 42.983 1.00 12.85 ? 250 ILE A C 1 ATOM 1938 O O . ILE A 1 250 ? -37.155 -8.855 42.760 1.00 13.91 ? 250 ILE A O 1 ATOM 1939 C CB . ILE A 1 250 ? -36.540 -7.559 45.394 1.00 12.79 ? 250 ILE A CB 1 ATOM 1940 C CG1 . ILE A 1 250 ? -36.579 -6.038 45.228 1.00 12.03 ? 250 ILE A CG1 1 ATOM 1941 C CG2 . ILE A 1 250 ? -36.170 -7.943 46.800 1.00 15.03 ? 250 ILE A CG2 1 ATOM 1942 C CD1 . ILE A 1 250 ? -37.851 -5.397 45.724 1.00 11.51 ? 250 ILE A CD1 1 ATOM 1943 N N . ALA A 1 251 ? -35.415 -7.593 42.039 1.00 13.38 ? 251 ALA A N 1 ATOM 1944 C CA . ALA A 1 251 ? -35.808 -7.529 40.619 1.00 13.08 ? 251 ALA A CA 1 ATOM 1945 C C . ALA A 1 251 ? -34.698 -7.171 39.634 1.00 14.24 ? 251 ALA A C 1 ATOM 1946 O O . ALA A 1 251 ? -33.953 -6.216 39.841 1.00 14.65 ? 251 ALA A O 1 ATOM 1947 C CB . ALA A 1 251 ? -36.982 -6.569 40.416 1.00 13.77 ? 251 ALA A CB 1 ATOM 1948 N N . ALA A 1 252 ? -34.615 -7.952 38.559 1.00 16.52 ? 252 ALA A N 1 ATOM 1949 C CA . ALA A 1 252 ? -33.657 -7.743 37.469 1.00 17.43 ? 252 ALA A CA 1 ATOM 1950 C C . ALA A 1 252 ? -34.525 -7.289 36.303 1.00 18.07 ? 252 ALA A C 1 ATOM 1951 O O . ALA A 1 252 ? -35.368 -8.055 35.822 1.00 17.27 ? 252 ALA A O 1 ATOM 1952 C CB . ALA A 1 252 ? -32.929 -9.042 37.127 1.00 18.34 ? 252 ALA A CB 1 ATOM 1953 N N . ASP A 1 253 ? -34.326 -6.038 35.875 1.00 18.00 ? 253 ASP A N 1 ATOM 1954 C CA . ASP A 1 253 ? -35.115 -5.388 34.812 1.00 19.04 ? 253 ASP A CA 1 ATOM 1955 C C . ASP A 1 253 ? -36.591 -5.339 35.249 1.00 18.80 ? 253 ASP A C 1 ATOM 1956 O O . ASP A 1 253 ? -36.867 -4.909 36.375 1.00 20.77 ? 253 ASP A O 1 ATOM 1957 C CB . ASP A 1 253 ? -34.890 -6.028 33.422 1.00 18.59 ? 253 ASP A CB 1 ATOM 1958 C CG . ASP A 1 253 ? -33.474 -5.802 32.893 1.00 19.45 ? 253 ASP A CG 1 ATOM 1959 O OD1 . ASP A 1 253 ? -32.760 -4.934 33.432 1.00 22.05 ? 253 ASP A OD1 1 ATOM 1960 O OD2 . ASP A 1 253 ? -33.056 -6.499 31.947 1.00 17.80 ? 253 ASP A OD2 1 ATOM 1961 N N . MET A 1 254 ? -37.526 -5.813 34.429 1.00 18.00 ? 254 MET A N 1 ATOM 1962 C CA . MET A 1 254 ? -38.929 -5.787 34.838 1.00 16.24 ? 254 MET A CA 1 ATOM 1963 C C . MET A 1 254 ? -39.418 -7.175 35.246 1.00 14.75 ? 254 MET A C 1 ATOM 1964 O O . MET A 1 254 ? -40.612 -7.472 35.212 1.00 14.12 ? 254 MET A O 1 ATOM 1965 C CB . MET A 1 254 ? -39.797 -5.164 33.750 1.00 19.20 ? 254 MET A CB 1 ATOM 1966 C CG . MET A 1 254 ? -40.869 -4.268 34.316 1.00 21.94 ? 254 MET A CG 1 ATOM 1967 S SD . MET A 1 254 ? -41.789 -3.400 33.073 1.00 29.72 ? 254 MET A SD 1 ATOM 1968 C CE . MET A 1 254 ? -42.300 -1.983 33.991 1.00 25.76 ? 254 MET A CE 1 ATOM 1969 N N . VAL A 1 255 ? -38.463 -8.009 35.661 1.00 12.94 ? 255 VAL A N 1 ATOM 1970 C CA . VAL A 1 255 ? -38.714 -9.380 36.095 1.00 9.28 ? 255 VAL A CA 1 ATOM 1971 C C . VAL A 1 255 ? -38.306 -9.533 37.573 1.00 10.21 ? 255 VAL A C 1 ATOM 1972 O O . VAL A 1 255 ? -37.134 -9.385 37.904 1.00 10.93 ? 255 VAL A O 1 ATOM 1973 C CB . VAL A 1 255 ? -37.897 -10.375 35.233 1.00 8.03 ? 255 VAL A CB 1 ATOM 1974 C CG1 . VAL A 1 255 ? -38.143 -11.811 35.663 1.00 5.13 ? 255 VAL A CG1 1 ATOM 1975 C CG2 . VAL A 1 255 ? -38.221 -10.197 33.758 1.00 7.11 ? 255 VAL A CG2 1 ATOM 1976 N N . PRO A 1 256 ? -39.272 -9.810 38.477 1.00 11.69 ? 256 PRO A N 1 ATOM 1977 C CA . PRO A 1 256 ? -38.976 -9.981 39.907 1.00 11.59 ? 256 PRO A CA 1 ATOM 1978 C C . PRO A 1 256 ? -38.216 -11.269 40.163 1.00 12.00 ? 256 PRO A C 1 ATOM 1979 O O . PRO A 1 256 ? -38.592 -12.325 39.651 1.00 11.80 ? 256 PRO A O 1 ATOM 1980 C CB . PRO A 1 256 ? -40.362 -10.031 40.538 1.00 13.18 ? 256 PRO A CB 1 ATOM 1981 C CG . PRO A 1 256 ? -41.168 -9.227 39.610 1.00 13.05 ? 256 PRO A CG 1 ATOM 1982 C CD . PRO A 1 256 ? -40.730 -9.722 38.283 1.00 11.52 ? 256 PRO A CD 1 ATOM 1983 N N . VAL A 1 257 ? -37.113 -11.160 40.904 1.00 12.45 ? 257 VAL A N 1 ATOM 1984 C CA . VAL A 1 257 ? -36.263 -12.312 41.226 1.00 12.68 ? 257 VAL A CA 1 ATOM 1985 C C . VAL A 1 257 ? -36.235 -12.654 42.716 1.00 13.05 ? 257 VAL A C 1 ATOM 1986 O O . VAL A 1 257 ? -36.563 -11.809 43.544 1.00 11.99 ? 257 VAL A O 1 ATOM 1987 C CB . VAL A 1 257 ? -34.782 -12.135 40.700 1.00 11.80 ? 257 VAL A CB 1 ATOM 1988 C CG1 . VAL A 1 257 ? -34.765 -11.902 39.196 1.00 11.47 ? 257 VAL A CG1 1 ATOM 1989 C CG2 . VAL A 1 257 ? -34.037 -11.014 41.431 1.00 11.09 ? 257 VAL A CG2 1 ATOM 1990 N N . ASN A 1 258 ? -35.825 -13.886 43.042 1.00 14.26 ? 258 ASN A N 1 ATOM 1991 C CA . ASN A 1 258 ? -35.700 -14.345 44.434 1.00 16.18 ? 258 ASN A CA 1 ATOM 1992 C C . ASN A 1 258 ? -34.570 -13.536 45.065 1.00 16.81 ? 258 ASN A C 1 ATOM 1993 O O . ASN A 1 258 ? -33.550 -13.287 44.401 1.00 17.74 ? 258 ASN A O 1 ATOM 1994 C CB . ASN A 1 258 ? -35.342 -15.839 44.503 1.00 17.05 ? 258 ASN A CB 1 ATOM 1995 C CG . ASN A 1 258 ? -36.486 -16.754 44.078 1.00 19.84 ? 258 ASN A CG 1 ATOM 1996 O OD1 . ASN A 1 258 ? -37.664 -16.384 44.121 1.00 22.79 ? 258 ASN A OD1 1 ATOM 1997 N ND2 . ASN A 1 258 ? -36.137 -17.970 43.675 1.00 21.93 ? 258 ASN A ND2 1 ATOM 1998 N N . ALA A 1 259 ? -34.768 -13.114 46.320 1.00 16.02 ? 259 ALA A N 1 ATOM 1999 C CA . ALA A 1 259 ? -33.802 -12.302 47.077 1.00 15.20 ? 259 ALA A CA 1 ATOM 2000 C C . ALA A 1 259 ? -32.352 -12.766 46.941 1.00 16.16 ? 259 ALA A C 1 ATOM 2001 O O . ALA A 1 259 ? -32.059 -13.956 47.073 1.00 16.65 ? 259 ALA A O 1 ATOM 2002 C CB . ALA A 1 259 ? -34.202 -12.237 48.541 1.00 17.10 ? 259 ALA A CB 1 ATOM 2003 N N . MET A 1 260 ? -31.484 -11.827 46.567 1.00 16.41 ? 260 MET A N 1 ATOM 2004 C CA . MET A 1 260 ? -30.064 -12.095 46.369 1.00 16.77 ? 260 MET A CA 1 ATOM 2005 C C . MET A 1 260 ? -29.241 -10.916 46.880 1.00 15.99 ? 260 MET A C 1 ATOM 2006 O O . MET A 1 260 ? -29.237 -9.827 46.291 1.00 16.63 ? 260 MET A O 1 ATOM 2007 C CB . MET A 1 260 ? -29.776 -12.358 44.884 1.00 17.78 ? 260 MET A CB 1 ATOM 2008 C CG . MET A 1 260 ? -28.452 -13.052 44.608 1.00 20.47 ? 260 MET A CG 1 ATOM 2009 S SD . MET A 1 260 ? -28.128 -13.209 42.845 1.00 23.07 ? 260 MET A SD 1 ATOM 2010 C CE . MET A 1 260 ? -27.586 -11.541 42.458 1.00 18.37 ? 260 MET A CE 1 ATOM 2011 N N . THR A 1 261 ? -28.589 -11.143 48.016 1.00 14.56 ? 261 THR A N 1 ATOM 2012 C CA . THR A 1 261 ? -27.745 -10.155 48.673 1.00 13.02 ? 261 THR A CA 1 ATOM 2013 C C . THR A 1 261 ? -26.354 -10.091 48.019 1.00 12.69 ? 261 THR A C 1 ATOM 2014 O O . THR A 1 261 ? -25.724 -11.129 47.762 1.00 11.87 ? 261 THR A O 1 ATOM 2015 C CB . THR A 1 261 ? -27.678 -10.448 50.208 1.00 12.02 ? 261 THR A CB 1 ATOM 2016 O OG1 . THR A 1 261 ? -28.932 -10.094 50.806 1.00 11.12 ? 261 THR A OG1 1 ATOM 2017 C CG2 . THR A 1 261 ? -26.552 -9.684 50.899 1.00 9.49 ? 261 THR A CG2 1 ATOM 2018 N N . VAL A 1 262 ? -25.930 -8.864 47.697 1.00 11.82 ? 262 VAL A N 1 ATOM 2019 C CA . VAL A 1 262 ? -24.633 -8.582 47.064 1.00 14.15 ? 262 VAL A CA 1 ATOM 2020 C C . VAL A 1 262 ? -23.976 -7.314 47.637 1.00 16.13 ? 262 VAL A C 1 ATOM 2021 O O . VAL A 1 262 ? -24.640 -6.500 48.277 1.00 17.38 ? 262 VAL A O 1 ATOM 2022 C CB . VAL A 1 262 ? -24.766 -8.403 45.503 1.00 12.23 ? 262 VAL A CB 1 ATOM 2023 C CG1 . VAL A 1 262 ? -25.151 -9.715 44.830 1.00 7.24 ? 262 VAL A CG1 1 ATOM 2024 C CG2 . VAL A 1 262 ? -25.781 -7.312 45.166 1.00 10.51 ? 262 VAL A CG2 1 ATOM 2025 N N . ASP A 1 263 ? -22.673 -7.159 47.403 1.00 19.34 ? 263 ASP A N 1 ATOM 2026 C CA . ASP A 1 263 ? -21.933 -5.980 47.853 1.00 22.82 ? 263 ASP A CA 1 ATOM 2027 C C . ASP A 1 263 ? -21.922 -4.947 46.734 1.00 22.91 ? 263 ASP A C 1 ATOM 2028 O O . ASP A 1 263 ? -21.915 -3.740 46.992 1.00 23.75 ? 263 ASP A O 1 ATOM 2029 C CB . ASP A 1 263 ? -20.492 -6.333 48.225 1.00 26.85 ? 263 ASP A CB 1 ATOM 2030 C CG . ASP A 1 263 ? -20.399 -7.136 49.504 1.00 32.82 ? 263 ASP A CG 1 ATOM 2031 O OD1 . ASP A 1 263 ? -20.845 -6.635 50.565 1.00 34.02 ? 263 ASP A OD1 1 ATOM 2032 O OD2 . ASP A 1 263 ? -19.872 -8.270 49.444 1.00 35.29 ? 263 ASP A OD2 1 ATOM 2033 N N . SER A 1 264 ? -21.921 -5.446 45.498 1.00 21.40 ? 264 SER A N 1 ATOM 2034 C CA . SER A 1 264 ? -21.909 -4.613 44.304 1.00 20.24 ? 264 SER A CA 1 ATOM 2035 C C . SER A 1 264 ? -22.729 -5.191 43.165 1.00 19.52 ? 264 SER A C 1 ATOM 2036 O O . SER A 1 264 ? -22.957 -6.400 43.093 1.00 19.07 ? 264 SER A O 1 ATOM 2037 C CB . SER A 1 264 ? -20.474 -4.345 43.834 1.00 21.92 ? 264 SER A CB 1 ATOM 2038 O OG . SER A 1 264 ? -19.741 -5.541 43.645 1.00 23.49 ? 264 SER A OG 1 ATOM 2039 N N . LEU A 1 265 ? -23.171 -4.307 42.277 1.00 18.90 ? 265 LEU A N 1 ATOM 2040 C CA . LEU A 1 265 ? -23.974 -4.691 41.125 1.00 18.72 ? 265 LEU A CA 1 ATOM 2041 C C . LEU A 1 265 ? -23.522 -4.096 39.824 1.00 17.64 ? 265 LEU A C 1 ATOM 2042 O O . LEU A 1 265 ? -23.281 -2.892 39.729 1.00 17.94 ? 265 LEU A O 1 ATOM 2043 C CB . LEU A 1 265 ? -25.419 -4.258 41.307 1.00 19.57 ? 265 LEU A CB 1 ATOM 2044 C CG . LEU A 1 265 ? -26.392 -5.158 42.032 1.00 23.16 ? 265 LEU A CG 1 ATOM 2045 C CD1 . LEU A 1 265 ? -27.628 -4.361 42.329 1.00 22.76 ? 265 LEU A CD1 1 ATOM 2046 C CD2 . LEU A 1 265 ? -26.702 -6.392 41.197 1.00 25.72 ? 265 LEU A CD2 1 ATOM 2047 N N . PHE A 1 266 ? -23.488 -4.936 38.798 1.00 17.67 ? 266 PHE A N 1 ATOM 2048 C CA . PHE A 1 266 ? -23.138 -4.481 37.467 1.00 14.49 ? 266 PHE A CA 1 ATOM 2049 C C . PHE A 1 266 ? -24.431 -4.131 36.747 1.00 13.01 ? 266 PHE A C 1 ATOM 2050 O O . PHE A 1 266 ? -25.389 -4.911 36.755 1.00 12.51 ? 266 PHE A O 1 ATOM 2051 C CB . PHE A 1 266 ? -22.391 -5.553 36.672 1.00 15.47 ? 266 PHE A CB 1 ATOM 2052 C CG . PHE A 1 266 ? -21.954 -5.092 35.308 1.00 15.59 ? 266 PHE A CG 1 ATOM 2053 C CD1 . PHE A 1 266 ? -20.837 -4.249 35.166 1.00 16.36 ? 266 PHE A CD1 1 ATOM 2054 C CD2 . PHE A 1 266 ? -22.697 -5.440 34.159 1.00 14.80 ? 266 PHE A CD2 1 ATOM 2055 C CE1 . PHE A 1 266 ? -20.472 -3.753 33.894 1.00 15.75 ? 266 PHE A CE1 1 ATOM 2056 C CE2 . PHE A 1 266 ? -22.347 -4.960 32.889 1.00 14.48 ? 266 PHE A CE2 1 ATOM 2057 C CZ . PHE A 1 266 ? -21.240 -4.116 32.750 1.00 13.35 ? 266 PHE A CZ 1 ATOM 2058 N N . LEU A 1 267 ? -24.451 -2.943 36.152 1.00 10.20 ? 267 LEU A N 1 ATOM 2059 C CA . LEU A 1 267 ? -25.595 -2.483 35.379 1.00 9.25 ? 267 LEU A CA 1 ATOM 2060 C C . LEU A 1 267 ? -25.142 -2.121 33.963 1.00 9.57 ? 267 LEU A C 1 ATOM 2061 O O . LEU A 1 267 ? -24.398 -1.153 33.755 1.00 8.57 ? 267 LEU A O 1 ATOM 2062 C CB . LEU A 1 267 ? -26.282 -1.274 36.033 1.00 9.70 ? 267 LEU A CB 1 ATOM 2063 C CG . LEU A 1 267 ? -27.339 -1.522 37.119 1.00 12.64 ? 267 LEU A CG 1 ATOM 2064 C CD1 . LEU A 1 267 ? -26.676 -1.589 38.482 1.00 10.28 ? 267 LEU A CD1 1 ATOM 2065 C CD2 . LEU A 1 267 ? -28.407 -0.446 37.106 1.00 8.98 ? 267 LEU A CD2 1 ATOM 2066 N N . ALA A 1 268 ? -25.541 -2.942 32.998 1.00 9.08 ? 268 ALA A N 1 ATOM 2067 C CA . ALA A 1 268 ? -25.226 -2.692 31.593 1.00 10.26 ? 268 ALA A CA 1 ATOM 2068 C C . ALA A 1 268 ? -26.163 -1.612 31.103 1.00 11.01 ? 268 ALA A C 1 ATOM 2069 O O . ALA A 1 268 ? -27.127 -1.281 31.796 1.00 14.00 ? 268 ALA A O 1 ATOM 2070 C CB . ALA A 1 268 ? -25.407 -3.944 30.772 1.00 7.19 ? 268 ALA A CB 1 ATOM 2071 N N . VAL A 1 269 ? -25.877 -1.051 29.930 1.00 14.16 ? 269 VAL A N 1 ATOM 2072 C CA . VAL A 1 269 ? -26.708 -0.006 29.327 1.00 13.97 ? 269 VAL A CA 1 ATOM 2073 C C . VAL A 1 269 ? -28.124 -0.532 29.106 1.00 14.40 ? 269 VAL A C 1 ATOM 2074 O O . VAL A 1 269 ? -28.339 -1.476 28.352 1.00 14.51 ? 269 VAL A O 1 ATOM 2075 C CB . VAL A 1 269 ? -26.108 0.486 27.991 1.00 15.14 ? 269 VAL A CB 1 ATOM 2076 C CG1 . VAL A 1 269 ? -26.990 1.556 27.343 1.00 13.99 ? 269 VAL A CG1 1 ATOM 2077 C CG2 . VAL A 1 269 ? -24.744 1.045 28.233 1.00 13.14 ? 269 VAL A CG2 1 ATOM 2078 N N . GLY A 1 270 ? -29.061 0.059 29.837 1.00 15.17 ? 270 GLY A N 1 ATOM 2079 C CA . GLY A 1 270 ? -30.448 -0.343 29.738 1.00 16.04 ? 270 GLY A CA 1 ATOM 2080 C C . GLY A 1 270 ? -30.909 -1.261 30.848 1.00 17.56 ? 270 GLY A C 1 ATOM 2081 O O . GLY A 1 270 ? -32.085 -1.618 30.897 1.00 17.51 ? 270 GLY A O 1 ATOM 2082 N N . GLN A 1 271 ? -29.989 -1.661 31.726 1.00 18.36 ? 271 GLN A N 1 ATOM 2083 C CA . GLN A 1 271 ? -30.334 -2.550 32.832 1.00 19.24 ? 271 GLN A CA 1 ATOM 2084 C C . GLN A 1 271 ? -30.884 -1.828 34.045 1.00 19.21 ? 271 GLN A C 1 ATOM 2085 O O . GLN A 1 271 ? -30.572 -0.653 34.293 1.00 20.83 ? 271 GLN A O 1 ATOM 2086 C CB . GLN A 1 271 ? -29.157 -3.448 33.236 1.00 16.34 ? 271 GLN A CB 1 ATOM 2087 C CG . GLN A 1 271 ? -29.002 -4.653 32.336 1.00 14.80 ? 271 GLN A CG 1 ATOM 2088 C CD . GLN A 1 271 ? -27.939 -5.651 32.778 1.00 15.59 ? 271 GLN A CD 1 ATOM 2089 O OE1 . GLN A 1 271 ? -27.000 -5.317 33.492 1.00 14.96 ? 271 GLN A OE1 1 ATOM 2090 N NE2 . GLN A 1 271 ? -28.078 -6.889 32.322 1.00 18.32 ? 271 GLN A NE2 1 ATOM 2091 N N . ARG A 1 272 ? -31.823 -2.500 34.701 1.00 17.61 ? 272 ARG A N 1 ATOM 2092 C CA . ARG A 1 272 ? -32.451 -1.991 35.910 1.00 17.25 ? 272 ARG A CA 1 ATOM 2093 C C . ARG A 1 272 ? -32.293 -3.026 37.000 1.00 16.08 ? 272 ARG A C 1 ATOM 2094 O O . ARG A 1 272 ? -32.146 -4.212 36.713 1.00 16.52 ? 272 ARG A O 1 ATOM 2095 C CB . ARG A 1 272 ? -33.950 -1.717 35.715 1.00 17.38 ? 272 ARG A CB 1 ATOM 2096 C CG . ARG A 1 272 ? -34.299 -0.528 34.854 1.00 16.53 ? 272 ARG A CG 1 ATOM 2097 C CD . ARG A 1 272 ? -34.312 -0.862 33.379 1.00 16.57 ? 272 ARG A CD 1 ATOM 2098 N NE . ARG A 1 272 ? -35.452 -1.696 33.026 1.00 16.26 ? 272 ARG A NE 1 ATOM 2099 C CZ . ARG A 1 272 ? -35.479 -2.568 32.024 1.00 16.76 ? 272 ARG A CZ 1 ATOM 2100 N NH1 . ARG A 1 272 ? -34.419 -2.743 31.250 1.00 14.94 ? 272 ARG A NH1 1 ATOM 2101 N NH2 . ARG A 1 272 ? -36.578 -3.280 31.802 1.00 17.25 ? 272 ARG A NH2 1 ATOM 2102 N N . TYR A 1 273 ? -32.313 -2.562 38.249 1.00 17.57 ? 273 TYR A N 1 ATOM 2103 C CA . TYR A 1 273 ? -32.213 -3.414 39.437 1.00 16.53 ? 273 TYR A CA 1 ATOM 2104 C C . TYR A 1 273 ? -32.960 -2.798 40.607 1.00 17.89 ? 273 TYR A C 1 ATOM 2105 O O . TYR A 1 273 ? -32.701 -1.654 40.983 1.00 18.06 ? 273 TYR A O 1 ATOM 2106 C CB . TYR A 1 273 ? -30.759 -3.671 39.845 1.00 14.23 ? 273 TYR A CB 1 ATOM 2107 C CG . TYR A 1 273 ? -30.093 -4.841 39.148 1.00 14.96 ? 273 TYR A CG 1 ATOM 2108 C CD1 . TYR A 1 273 ? -30.612 -6.149 39.253 1.00 14.70 ? 273 TYR A CD1 1 ATOM 2109 C CD2 . TYR A 1 273 ? -28.914 -4.657 38.409 1.00 14.84 ? 273 TYR A CD2 1 ATOM 2110 C CE1 . TYR A 1 273 ? -29.958 -7.255 38.639 1.00 14.23 ? 273 TYR A CE1 1 ATOM 2111 C CE2 . TYR A 1 273 ? -28.253 -5.746 37.792 1.00 15.15 ? 273 TYR A CE2 1 ATOM 2112 C CZ . TYR A 1 273 ? -28.780 -7.037 37.917 1.00 15.83 ? 273 TYR A CZ 1 ATOM 2113 O OH . TYR A 1 273 ? -28.118 -8.088 37.341 1.00 18.21 ? 273 TYR A OH 1 ATOM 2114 N N . ASP A 1 274 ? -33.948 -3.523 41.125 1.00 19.99 ? 274 ASP A N 1 ATOM 2115 C CA . ASP A 1 274 ? -34.696 -3.053 42.286 1.00 22.25 ? 274 ASP A CA 1 ATOM 2116 C C . ASP A 1 274 ? -34.018 -3.696 43.482 1.00 21.69 ? 274 ASP A C 1 ATOM 2117 O O . ASP A 1 274 ? -33.941 -4.923 43.565 1.00 21.43 ? 274 ASP A O 1 ATOM 2118 C CB . ASP A 1 274 ? -36.169 -3.468 42.234 1.00 25.24 ? 274 ASP A CB 1 ATOM 2119 C CG . ASP A 1 274 ? -36.933 -2.811 41.098 1.00 29.11 ? 274 ASP A CG 1 ATOM 2120 O OD1 . ASP A 1 274 ? -36.420 -2.782 39.965 1.00 32.81 ? 274 ASP A OD1 1 ATOM 2121 O OD2 . ASP A 1 274 ? -38.066 -2.339 41.328 1.00 32.11 ? 274 ASP A OD2 1 ATOM 2122 N N . VAL A 1 275 ? -33.406 -2.871 44.326 1.00 21.61 ? 275 VAL A N 1 ATOM 2123 C CA . VAL A 1 275 ? -32.726 -3.372 45.518 1.00 22.25 ? 275 VAL A CA 1 ATOM 2124 C C . VAL A 1 275 ? -33.372 -2.891 46.804 1.00 23.18 ? 275 VAL A C 1 ATOM 2125 O O . VAL A 1 275 ? -34.043 -1.863 46.815 1.00 23.23 ? 275 VAL A O 1 ATOM 2126 C CB . VAL A 1 275 ? -31.197 -3.016 45.553 1.00 21.85 ? 275 VAL A CB 1 ATOM 2127 C CG1 . VAL A 1 275 ? -30.501 -3.557 44.336 1.00 19.47 ? 275 VAL A CG1 1 ATOM 2128 C CG2 . VAL A 1 275 ? -30.960 -1.509 45.687 1.00 22.33 ? 275 VAL A CG2 1 ATOM 2129 N N . VAL A 1 276 ? -33.193 -3.676 47.866 1.00 24.19 ? 276 VAL A N 1 ATOM 2130 C CA . VAL A 1 276 ? -33.686 -3.349 49.200 1.00 23.58 ? 276 VAL A CA 1 ATOM 2131 C C . VAL A 1 276 ? -32.434 -3.055 50.033 1.00 24.70 ? 276 VAL A C 1 ATOM 2132 O O . VAL A 1 276 ? -31.542 -3.898 50.160 1.00 25.57 ? 276 VAL A O 1 ATOM 2133 C CB . VAL A 1 276 ? -34.533 -4.506 49.830 1.00 23.97 ? 276 VAL A CB 1 ATOM 2134 C CG1 . VAL A 1 276 ? -34.848 -4.227 51.299 1.00 22.05 ? 276 VAL A CG1 1 ATOM 2135 C CG2 . VAL A 1 276 ? -35.844 -4.673 49.071 1.00 22.94 ? 276 VAL A CG2 1 ATOM 2136 N N . ILE A 1 277 ? -32.334 -1.813 50.494 1.00 24.58 ? 277 ILE A N 1 ATOM 2137 C CA . ILE A 1 277 ? -31.220 -1.364 51.316 1.00 24.18 ? 277 ILE A CA 1 ATOM 2138 C C . ILE A 1 277 ? -31.743 -1.223 52.749 1.00 25.46 ? 277 ILE A C 1 ATOM 2139 O O . ILE A 1 277 ? -32.704 -0.489 53.003 1.00 25.61 ? 277 ILE A O 1 ATOM 2140 C CB . ILE A 1 277 ? -30.632 -0.016 50.780 1.00 22.77 ? 277 ILE A CB 1 ATOM 2141 C CG1 . ILE A 1 277 ? -29.990 -0.246 49.405 1.00 21.37 ? 277 ILE A CG1 1 ATOM 2142 C CG2 . ILE A 1 277 ? -29.627 0.592 51.785 1.00 22.81 ? 277 ILE A CG2 1 ATOM 2143 C CD1 . ILE A 1 277 ? -29.430 0.991 48.741 1.00 20.96 ? 277 ILE A CD1 1 ATOM 2144 N N . ASP A 1 278 ? -31.132 -1.969 53.666 1.00 27.14 ? 278 ASP A N 1 ATOM 2145 C CA . ASP A 1 278 ? -31.514 -1.938 55.074 1.00 28.68 ? 278 ASP A CA 1 ATOM 2146 C C . ASP A 1 278 ? -30.682 -0.889 55.789 1.00 28.97 ? 278 ASP A C 1 ATOM 2147 O O . ASP A 1 278 ? -29.451 -0.902 55.713 1.00 28.41 ? 278 ASP A O 1 ATOM 2148 C CB . ASP A 1 278 ? -31.309 -3.315 55.727 1.00 31.32 ? 278 ASP A CB 1 ATOM 2149 C CG . ASP A 1 278 ? -32.299 -4.373 55.226 1.00 33.72 ? 278 ASP A CG 1 ATOM 2150 O OD1 . ASP A 1 278 ? -33.228 -4.038 54.457 1.00 35.51 ? 278 ASP A OD1 1 ATOM 2151 O OD2 . ASP A 1 278 ? -32.147 -5.554 55.617 1.00 34.76 ? 278 ASP A OD2 1 ATOM 2152 N N . ALA A 1 279 ? -31.362 0.043 56.450 1.00 29.65 ? 279 ALA A N 1 ATOM 2153 C CA . ALA A 1 279 ? -30.695 1.113 57.186 1.00 30.81 ? 279 ALA A CA 1 ATOM 2154 C C . ALA A 1 279 ? -30.297 0.610 58.580 1.00 31.69 ? 279 ALA A C 1 ATOM 2155 O O . ALA A 1 279 ? -30.664 1.188 59.610 1.00 31.91 ? 279 ALA A O 1 ATOM 2156 C CB . ALA A 1 279 ? -31.599 2.334 57.269 1.00 31.01 ? 279 ALA A CB 1 ATOM 2157 N N . SER A 1 280 ? -29.492 -0.455 58.564 1.00 32.67 ? 280 SER A N 1 ATOM 2158 C CA . SER A 1 280 ? -29.009 -1.162 59.746 1.00 33.41 ? 280 SER A CA 1 ATOM 2159 C C . SER A 1 280 ? -27.597 -0.824 60.253 1.00 33.89 ? 280 SER A C 1 ATOM 2160 O O . SER A 1 280 ? -27.054 -1.524 61.123 1.00 32.42 ? 280 SER A O 1 ATOM 2161 C CB . SER A 1 280 ? -29.128 -2.667 59.490 1.00 33.49 ? 280 SER A CB 1 ATOM 2162 O OG . SER A 1 280 ? -28.394 -3.054 58.345 1.00 35.29 ? 280 SER A OG 1 ATOM 2163 N N . ARG A 1 281 ? -27.000 0.232 59.701 1.00 34.22 ? 281 ARG A N 1 ATOM 2164 C CA . ARG A 1 281 ? -25.661 0.665 60.099 1.00 34.20 ? 281 ARG A CA 1 ATOM 2165 C C . ARG A 1 281 ? -25.713 1.942 60.935 1.00 33.47 ? 281 ARG A C 1 ATOM 2166 O O . ARG A 1 281 ? -26.792 2.517 61.123 1.00 32.49 ? 281 ARG A O 1 ATOM 2167 C CB . ARG A 1 281 ? -24.768 0.857 58.866 1.00 35.36 ? 281 ARG A CB 1 ATOM 2168 C CG . ARG A 1 281 ? -24.580 -0.400 58.010 1.00 38.71 ? 281 ARG A CG 1 ATOM 2169 C CD . ARG A 1 281 ? -24.010 -1.592 58.780 1.00 41.51 ? 281 ARG A CD 1 ATOM 2170 N NE . ARG A 1 281 ? -22.700 -1.301 59.358 1.00 46.11 ? 281 ARG A NE 1 ATOM 2171 C CZ . ARG A 1 281 ? -21.585 -1.978 59.094 1.00 48.43 ? 281 ARG A CZ 1 ATOM 2172 N NH1 . ARG A 1 281 ? -21.599 -3.006 58.250 1.00 50.15 ? 281 ARG A NH1 1 ATOM 2173 N NH2 . ARG A 1 281 ? -20.448 -1.628 59.681 1.00 49.30 ? 281 ARG A NH2 1 ATOM 2174 N N . ALA A 1 282 ? -24.545 2.367 61.431 1.00 33.06 ? 282 ALA A N 1 ATOM 2175 C CA . ALA A 1 282 ? -24.381 3.569 62.267 1.00 34.18 ? 282 ALA A CA 1 ATOM 2176 C C . ALA A 1 282 ? -24.849 4.867 61.577 1.00 34.71 ? 282 ALA A C 1 ATOM 2177 O O . ALA A 1 282 ? -24.525 5.087 60.406 1.00 34.27 ? 282 ALA A O 1 ATOM 2178 C CB . ALA A 1 282 ? -22.917 3.701 62.711 1.00 33.59 ? 282 ALA A CB 1 ATOM 2179 N N . PRO A 1 283 ? -25.641 5.722 62.284 1.00 35.21 ? 283 PRO A N 1 ATOM 2180 C CA . PRO A 1 283 ? -26.160 6.993 61.747 1.00 34.51 ? 283 PRO A CA 1 ATOM 2181 C C . PRO A 1 283 ? -25.092 7.974 61.252 1.00 33.46 ? 283 PRO A C 1 ATOM 2182 O O . PRO A 1 283 ? -24.528 8.758 62.022 1.00 34.19 ? 283 PRO A O 1 ATOM 2183 C CB . PRO A 1 283 ? -26.974 7.549 62.917 1.00 36.06 ? 283 PRO A CB 1 ATOM 2184 C CG . PRO A 1 283 ? -27.475 6.306 63.581 1.00 36.29 ? 283 PRO A CG 1 ATOM 2185 C CD . PRO A 1 283 ? -26.219 5.478 63.623 1.00 35.34 ? 283 PRO A CD 1 ATOM 2186 N N . ASP A 1 284 ? -24.850 7.924 59.943 1.00 32.15 ? 284 ASP A N 1 ATOM 2187 C CA . ASP A 1 284 ? -23.841 8.750 59.288 1.00 30.69 ? 284 ASP A CA 1 ATOM 2188 C C . ASP A 1 284 ? -24.185 8.932 57.806 1.00 29.19 ? 284 ASP A C 1 ATOM 2189 O O . ASP A 1 284 ? -25.250 8.527 57.341 1.00 28.70 ? 284 ASP A O 1 ATOM 2190 C CB . ASP A 1 284 ? -22.470 8.056 59.435 1.00 31.15 ? 284 ASP A CB 1 ATOM 2191 C CG . ASP A 1 284 ? -21.295 9.011 59.358 1.00 31.71 ? 284 ASP A CG 1 ATOM 2192 O OD1 . ASP A 1 284 ? -21.487 10.244 59.440 1.00 33.09 ? 284 ASP A OD1 1 ATOM 2193 O OD2 . ASP A 1 284 ? -20.160 8.513 59.224 1.00 32.86 ? 284 ASP A OD2 1 ATOM 2194 N N . ASN A 1 285 ? -23.286 9.597 57.091 1.00 28.20 ? 285 ASN A N 1 ATOM 2195 C CA . ASN A 1 285 ? -23.417 9.836 55.663 1.00 26.80 ? 285 ASN A CA 1 ATOM 2196 C C . ASN A 1 285 ? -22.531 8.810 54.956 1.00 24.37 ? 285 ASN A C 1 ATOM 2197 O O . ASN A 1 285 ? -21.356 8.660 55.299 1.00 24.29 ? 285 ASN A O 1 ATOM 2198 C CB . ASN A 1 285 ? -22.948 11.250 55.328 1.00 28.34 ? 285 ASN A CB 1 ATOM 2199 C CG . ASN A 1 285 ? -23.878 12.315 55.852 1.00 30.70 ? 285 ASN A CG 1 ATOM 2200 O OD1 . ASN A 1 285 ? -25.005 12.444 55.389 1.00 30.40 ? 285 ASN A OD1 1 ATOM 2201 N ND2 . ASN A 1 285 ? -23.398 13.108 56.804 1.00 31.52 ? 285 ASN A ND2 1 ATOM 2202 N N . TYR A 1 286 ? -23.106 8.076 54.007 1.00 21.67 ? 286 TYR A N 1 ATOM 2203 C CA . TYR A 1 286 ? -22.366 7.058 53.259 1.00 19.99 ? 286 TYR A CA 1 ATOM 2204 C C . TYR A 1 286 ? -22.323 7.335 51.757 1.00 18.81 ? 286 TYR A C 1 ATOM 2205 O O . TYR A 1 286 ? -23.265 7.894 51.187 1.00 17.67 ? 286 TYR A O 1 ATOM 2206 C CB . TYR A 1 286 ? -22.941 5.660 53.532 1.00 21.26 ? 286 TYR A CB 1 ATOM 2207 C CG . TYR A 1 286 ? -22.791 5.213 54.974 1.00 21.44 ? 286 TYR A CG 1 ATOM 2208 C CD1 . TYR A 1 286 ? -21.619 4.566 55.415 1.00 20.22 ? 286 TYR A CD1 1 ATOM 2209 C CD2 . TYR A 1 286 ? -23.800 5.479 55.921 1.00 22.21 ? 286 TYR A CD2 1 ATOM 2210 C CE1 . TYR A 1 286 ? -21.450 4.199 56.779 1.00 21.20 ? 286 TYR A CE1 1 ATOM 2211 C CE2 . TYR A 1 286 ? -23.644 5.114 57.286 1.00 23.10 ? 286 TYR A CE2 1 ATOM 2212 C CZ . TYR A 1 286 ? -22.466 4.480 57.704 1.00 22.37 ? 286 TYR A CZ 1 ATOM 2213 O OH . TYR A 1 286 ? -22.302 4.158 59.029 1.00 23.78 ? 286 TYR A OH 1 ATOM 2214 N N . TRP A 1 287 ? -21.197 6.994 51.133 1.00 17.01 ? 287 TRP A N 1 ATOM 2215 C CA . TRP A 1 287 ? -21.020 7.187 49.693 1.00 16.31 ? 287 TRP A CA 1 ATOM 2216 C C . TRP A 1 287 ? -21.643 6.056 48.883 1.00 15.87 ? 287 TRP A C 1 ATOM 2217 O O . TRP A 1 287 ? -21.536 4.880 49.253 1.00 16.66 ? 287 TRP A O 1 ATOM 2218 C CB . TRP A 1 287 ? -19.534 7.231 49.284 1.00 15.79 ? 287 TRP A CB 1 ATOM 2219 C CG . TRP A 1 287 ? -18.693 8.452 49.609 1.00 13.26 ? 287 TRP A CG 1 ATOM 2220 C CD1 . TRP A 1 287 ? -17.530 8.450 50.319 1.00 12.57 ? 287 TRP A CD1 1 ATOM 2221 C CD2 . TRP A 1 287 ? -18.881 9.807 49.163 1.00 13.15 ? 287 TRP A CD2 1 ATOM 2222 N NE1 . TRP A 1 287 ? -16.974 9.702 50.350 1.00 12.94 ? 287 TRP A NE1 1 ATOM 2223 C CE2 . TRP A 1 287 ? -17.777 10.562 49.654 1.00 14.16 ? 287 TRP A CE2 1 ATOM 2224 C CE3 . TRP A 1 287 ? -19.872 10.467 48.399 1.00 14.85 ? 287 TRP A CE3 1 ATOM 2225 C CZ2 . TRP A 1 287 ? -17.630 11.955 49.410 1.00 14.87 ? 287 TRP A CZ2 1 ATOM 2226 C CZ3 . TRP A 1 287 ? -19.729 11.864 48.148 1.00 12.54 ? 287 TRP A CZ3 1 ATOM 2227 C CH2 . TRP A 1 287 ? -18.611 12.586 48.658 1.00 13.82 ? 287 TRP A CH2 1 ATOM 2228 N N . PHE A 1 288 ? -22.318 6.430 47.798 1.00 15.42 ? 288 PHE A N 1 ATOM 2229 C CA . PHE A 1 288 ? -22.897 5.476 46.859 1.00 14.84 ? 288 PHE A CA 1 ATOM 2230 C C . PHE A 1 288 ? -21.919 5.646 45.715 1.00 14.81 ? 288 PHE A C 1 ATOM 2231 O O . PHE A 1 288 ? -21.889 6.703 45.089 1.00 14.00 ? 288 PHE A O 1 ATOM 2232 C CB . PHE A 1 288 ? -24.298 5.901 46.413 1.00 14.52 ? 288 PHE A CB 1 ATOM 2233 C CG . PHE A 1 288 ? -24.962 4.930 45.469 1.00 12.76 ? 288 PHE A CG 1 ATOM 2234 C CD1 . PHE A 1 288 ? -24.806 5.063 44.069 1.00 13.84 ? 288 PHE A CD1 1 ATOM 2235 C CD2 . PHE A 1 288 ? -25.742 3.878 45.972 1.00 12.03 ? 288 PHE A CD2 1 ATOM 2236 C CE1 . PHE A 1 288 ? -25.423 4.156 43.177 1.00 14.50 ? 288 PHE A CE1 1 ATOM 2237 C CE2 . PHE A 1 288 ? -26.375 2.955 45.103 1.00 14.79 ? 288 PHE A CE2 1 ATOM 2238 C CZ . PHE A 1 288 ? -26.216 3.094 43.695 1.00 17.02 ? 288 PHE A CZ 1 ATOM 2239 N N . ASN A 1 289 ? -21.136 4.612 45.437 1.00 15.41 ? 289 ASN A N 1 ATOM 2240 C CA . ASN A 1 289 ? -20.130 4.703 44.386 1.00 17.33 ? 289 ASN A CA 1 ATOM 2241 C C . ASN A 1 289 ? -20.397 4.078 43.040 1.00 16.24 ? 289 ASN A C 1 ATOM 2242 O O . ASN A 1 289 ? -20.883 2.949 42.941 1.00 16.58 ? 289 ASN A O 1 ATOM 2243 C CB . ASN A 1 289 ? -18.788 4.208 44.906 1.00 18.97 ? 289 ASN A CB 1 ATOM 2244 C CG . ASN A 1 289 ? -18.230 5.105 45.965 1.00 21.30 ? 289 ASN A CG 1 ATOM 2245 O OD1 . ASN A 1 289 ? -18.374 4.833 47.161 1.00 21.92 ? 289 ASN A OD1 1 ATOM 2246 N ND2 . ASN A 1 289 ? -17.614 6.195 45.509 1.00 22.89 ? 289 ASN A ND2 1 ATOM 2247 N N . VAL A 1 290 ? -20.035 4.838 42.008 1.00 15.73 ? 290 VAL A N 1 ATOM 2248 C CA . VAL A 1 290 ? -20.143 4.425 40.616 1.00 12.88 ? 290 VAL A CA 1 ATOM 2249 C C . VAL A 1 290 ? -18.705 4.137 40.170 1.00 14.58 ? 290 VAL A C 1 ATOM 2250 O O . VAL A 1 290 ? -17.889 5.055 40.041 1.00 13.90 ? 290 VAL A O 1 ATOM 2251 C CB . VAL A 1 290 ? -20.796 5.542 39.756 1.00 12.60 ? 290 VAL A CB 1 ATOM 2252 C CG1 . VAL A 1 290 ? -20.624 5.281 38.267 1.00 12.27 ? 290 VAL A CG1 1 ATOM 2253 C CG2 . VAL A 1 290 ? -22.267 5.636 40.076 1.00 12.46 ? 290 VAL A CG2 1 ATOM 2254 N N . THR A 1 291 ? -18.383 2.853 40.024 1.00 14.81 ? 291 THR A N 1 ATOM 2255 C CA . THR A 1 291 ? -17.047 2.434 39.592 1.00 16.80 ? 291 THR A CA 1 ATOM 2256 C C . THR A 1 291 ? -17.038 1.817 38.197 1.00 17.30 ? 291 THR A C 1 ATOM 2257 O O . THR A 1 291 ? -18.094 1.525 37.619 1.00 18.06 ? 291 THR A O 1 ATOM 2258 C CB . THR A 1 291 ? -16.412 1.438 40.570 1.00 13.63 ? 291 THR A CB 1 ATOM 2259 O OG1 . THR A 1 291 ? -17.398 0.498 40.996 1.00 14.58 ? 291 THR A OG1 1 ATOM 2260 C CG2 . THR A 1 291 ? -15.846 2.156 41.767 1.00 17.56 ? 291 THR A CG2 1 ATOM 2261 N N . PHE A 1 292 ? -15.837 1.679 37.649 1.00 16.79 ? 292 PHE A N 1 ATOM 2262 C CA . PHE A 1 292 ? -15.645 1.089 36.334 1.00 19.14 ? 292 PHE A CA 1 ATOM 2263 C C . PHE A 1 292 ? -14.684 -0.083 36.380 1.00 19.72 ? 292 PHE A C 1 ATOM 2264 O O . PHE A 1 292 ? -13.514 0.033 36.774 1.00 18.65 ? 292 PHE A O 1 ATOM 2265 C CB . PHE A 1 292 ? -15.165 2.123 35.310 1.00 19.02 ? 292 PHE A CB 1 ATOM 2266 C CG . PHE A 1 292 ? -16.210 3.121 34.929 1.00 20.40 ? 292 PHE A CG 1 ATOM 2267 C CD1 . PHE A 1 292 ? -17.170 2.811 33.952 1.00 22.86 ? 292 PHE A CD1 1 ATOM 2268 C CD2 . PHE A 1 292 ? -16.257 4.376 35.562 1.00 20.63 ? 292 PHE A CD2 1 ATOM 2269 C CE1 . PHE A 1 292 ? -18.183 3.751 33.603 1.00 24.12 ? 292 PHE A CE1 1 ATOM 2270 C CE2 . PHE A 1 292 ? -17.254 5.325 35.234 1.00 21.53 ? 292 PHE A CE2 1 ATOM 2271 C CZ . PHE A 1 292 ? -18.219 5.015 34.251 1.00 22.99 ? 292 PHE A CZ 1 ATOM 2272 N N . GLY A 1 293 ? -15.234 -1.234 36.032 1.00 21.08 ? 293 GLY A N 1 ATOM 2273 C CA . GLY A 1 293 ? -14.462 -2.448 35.974 1.00 22.81 ? 293 GLY A CA 1 ATOM 2274 C C . GLY A 1 293 ? -14.449 -2.851 34.524 1.00 23.31 ? 293 GLY A C 1 ATOM 2275 O O . GLY A 1 293 ? -15.064 -2.195 33.670 1.00 22.56 ? 293 GLY A O 1 ATOM 2276 N N . GLY A 1 294 ? -13.743 -3.937 34.245 1.00 24.05 ? 294 GLY A N 1 ATOM 2277 C CA . GLY A 1 294 ? -13.649 -4.424 32.888 1.00 25.33 ? 294 GLY A CA 1 ATOM 2278 C C . GLY A 1 294 ? -12.628 -3.654 32.108 1.00 25.73 ? 294 GLY A C 1 ATOM 2279 O O . GLY A 1 294 ? -12.683 -3.621 30.885 1.00 26.54 ? 294 GLY A O 1 ATOM 2280 N N . GLN A 1 295 ? -11.658 -3.098 32.839 1.00 26.39 ? 295 GLN A N 1 ATOM 2281 C CA . GLN A 1 295 ? -10.547 -2.307 32.313 1.00 24.16 ? 295 GLN A CA 1 ATOM 2282 C C . GLN A 1 295 ? -10.851 -1.482 31.047 1.00 21.75 ? 295 GLN A C 1 ATOM 2283 O O . GLN A 1 295 ? -10.251 -1.674 29.983 1.00 20.37 ? 295 GLN A O 1 ATOM 2284 C CB . GLN A 1 295 ? -9.263 -3.170 32.198 1.00 29.03 ? 295 GLN A CB 1 ATOM 2285 C CG . GLN A 1 295 ? -9.334 -4.521 31.449 1.00 33.21 ? 295 GLN A CG 1 ATOM 2286 C CD . GLN A 1 295 ? -9.745 -5.709 32.315 1.00 36.66 ? 295 GLN A CD 1 ATOM 2287 O OE1 . GLN A 1 295 ? -9.526 -5.724 33.531 1.00 39.23 ? 295 GLN A OE1 1 ATOM 2288 N NE2 . GLN A 1 295 ? -10.341 -6.717 31.682 1.00 35.94 ? 295 GLN A NE2 1 ATOM 2289 N N . ALA A 1 296 ? -11.857 -0.608 31.195 1.00 19.21 ? 296 ALA A N 1 ATOM 2290 C CA . ALA A 1 296 ? -12.388 0.301 30.164 1.00 16.95 ? 296 ALA A CA 1 ATOM 2291 C C . ALA A 1 296 ? -12.819 -0.334 28.842 1.00 14.95 ? 296 ALA A C 1 ATOM 2292 O O . ALA A 1 296 ? -12.730 0.282 27.776 1.00 15.78 ? 296 ALA A O 1 ATOM 2293 C CB . ALA A 1 296 ? -11.452 1.474 29.921 1.00 16.94 ? 296 ALA A CB 1 ATOM 2294 N N . ALA A 1 297 ? -13.294 -1.572 28.931 1.00 14.02 ? 297 ALA A N 1 ATOM 2295 C CA . ALA A 1 297 ? -13.780 -2.309 27.772 1.00 13.25 ? 297 ALA A CA 1 ATOM 2296 C C . ALA A 1 297 ? -15.234 -1.916 27.521 1.00 13.82 ? 297 ALA A C 1 ATOM 2297 O O . ALA A 1 297 ? -15.702 -1.920 26.381 1.00 14.81 ? 297 ALA A O 1 ATOM 2298 C CB . ALA A 1 297 ? -13.665 -3.779 28.016 1.00 11.21 ? 297 ALA A CB 1 ATOM 2299 N N . CYS A 1 298 ? -15.928 -1.544 28.593 1.00 14.02 ? 298 CYS A N 1 ATOM 2300 C CA . CYS A 1 298 ? -17.320 -1.123 28.496 1.00 15.67 ? 298 CYS A CA 1 ATOM 2301 C C . CYS A 1 298 ? -17.538 0.271 29.098 1.00 15.29 ? 298 CYS A C 1 ATOM 2302 O O . CYS A 1 298 ? -18.514 0.512 29.820 1.00 16.69 ? 298 CYS A O 1 ATOM 2303 C CB . CYS A 1 298 ? -18.256 -2.174 29.109 1.00 13.55 ? 298 CYS A CB 1 ATOM 2304 S SG . CYS A 1 298 ? -17.969 -2.561 30.869 1.00 17.13 ? 298 CYS A SG 1 ATOM 2305 N N . GLY A 1 299 ? -16.578 1.162 28.837 1.00 16.75 ? 299 GLY A N 1 ATOM 2306 C CA . GLY A 1 299 ? -16.668 2.540 29.300 1.00 15.50 ? 299 GLY A CA 1 ATOM 2307 C C . GLY A 1 299 ? -15.828 3.025 30.460 1.00 14.86 ? 299 GLY A C 1 ATOM 2308 O O . GLY A 1 299 ? -15.175 2.242 31.153 1.00 13.63 ? 299 GLY A O 1 ATOM 2309 N N . GLY A 1 300 ? -15.909 4.342 30.669 1.00 14.49 ? 300 GLY A N 1 ATOM 2310 C CA . GLY A 1 300 ? -15.207 5.043 31.734 1.00 13.54 ? 300 GLY A CA 1 ATOM 2311 C C . GLY A 1 300 ? -15.662 6.496 31.822 1.00 13.94 ? 300 GLY A C 1 ATOM 2312 O O . GLY A 1 300 ? -16.475 6.948 31.011 1.00 14.18 ? 300 GLY A O 1 ATOM 2313 N N . SER A 1 301 ? -15.121 7.243 32.784 1.00 14.78 ? 301 SER A N 1 ATOM 2314 C CA . SER A 1 301 ? -15.484 8.648 32.951 1.00 14.67 ? 301 SER A CA 1 ATOM 2315 C C . SER A 1 301 ? -14.323 9.536 33.339 1.00 14.70 ? 301 SER A C 1 ATOM 2316 O O . SER A 1 301 ? -13.415 9.105 34.049 1.00 15.93 ? 301 SER A O 1 ATOM 2317 C CB . SER A 1 301 ? -16.590 8.809 33.996 1.00 15.93 ? 301 SER A CB 1 ATOM 2318 O OG . SER A 1 301 ? -17.183 10.099 33.918 1.00 12.26 ? 301 SER A OG 1 ATOM 2319 N N . LEU A 1 302 ? -14.394 10.798 32.908 1.00 15.78 ? 302 LEU A N 1 ATOM 2320 C CA . LEU A 1 302 ? -13.381 11.805 33.231 1.00 16.34 ? 302 LEU A CA 1 ATOM 2321 C C . LEU A 1 302 ? -13.518 12.281 34.676 1.00 16.08 ? 302 LEU A C 1 ATOM 2322 O O . LEU A 1 302 ? -12.633 12.952 35.207 1.00 18.76 ? 302 LEU A O 1 ATOM 2323 C CB . LEU A 1 302 ? -13.407 12.968 32.239 1.00 15.79 ? 302 LEU A CB 1 ATOM 2324 C CG . LEU A 1 302 ? -13.012 12.579 30.808 1.00 14.31 ? 302 LEU A CG 1 ATOM 2325 C CD1 . LEU A 1 302 ? -13.077 13.788 29.899 1.00 13.75 ? 302 LEU A CD1 1 ATOM 2326 C CD2 . LEU A 1 302 ? -11.621 11.943 30.786 1.00 15.20 ? 302 LEU A CD2 1 ATOM 2327 N N . ASN A 1 303 ? -14.643 11.927 35.297 1.00 15.84 ? 303 ASN A N 1 ATOM 2328 C CA . ASN A 1 303 ? -14.882 12.205 36.708 1.00 15.70 ? 303 ASN A CA 1 ATOM 2329 C C . ASN A 1 303 ? -14.330 10.901 37.296 1.00 14.91 ? 303 ASN A C 1 ATOM 2330 O O . ASN A 1 303 ? -14.865 9.817 37.026 1.00 14.15 ? 303 ASN A O 1 ATOM 2331 C CB . ASN A 1 303 ? -16.384 12.371 37.030 1.00 14.10 ? 303 ASN A CB 1 ATOM 2332 C CG . ASN A 1 303 ? -16.660 12.622 38.533 1.00 14.97 ? 303 ASN A CG 1 ATOM 2333 O OD1 . ASN A 1 303 ? -15.803 12.397 39.388 1.00 15.30 ? 303 ASN A OD1 1 ATOM 2334 N ND2 . ASN A 1 303 ? -17.878 13.056 38.847 1.00 13.81 ? 303 ASN A ND2 1 ATOM 2335 N N . PRO A 1 304 ? -13.211 10.983 38.043 1.00 14.51 ? 304 PRO A N 1 ATOM 2336 C CA . PRO A 1 304 ? -12.656 9.751 38.612 1.00 14.14 ? 304 PRO A CA 1 ATOM 2337 C C . PRO A 1 304 ? -13.547 9.070 39.656 1.00 13.73 ? 304 PRO A C 1 ATOM 2338 O O . PRO A 1 304 ? -13.581 7.841 39.724 1.00 14.22 ? 304 PRO A O 1 ATOM 2339 C CB . PRO A 1 304 ? -11.314 10.214 39.187 1.00 13.17 ? 304 PRO A CB 1 ATOM 2340 C CG . PRO A 1 304 ? -11.597 11.637 39.605 1.00 14.05 ? 304 PRO A CG 1 ATOM 2341 C CD . PRO A 1 304 ? -12.400 12.156 38.431 1.00 13.61 ? 304 PRO A CD 1 ATOM 2342 N N . HIS A 1 305 ? -14.310 9.863 40.418 1.00 11.96 ? 305 HIS A N 1 ATOM 2343 C CA . HIS A 1 305 ? -15.169 9.318 41.471 1.00 13.25 ? 305 HIS A CA 1 ATOM 2344 C C . HIS A 1 305 ? -16.611 9.838 41.522 1.00 13.08 ? 305 HIS A C 1 ATOM 2345 O O . HIS A 1 305 ? -16.944 10.661 42.389 1.00 14.40 ? 305 HIS A O 1 ATOM 2346 C CB . HIS A 1 305 ? -14.504 9.486 42.859 1.00 13.31 ? 305 HIS A CB 1 ATOM 2347 C CG . HIS A 1 305 ? -13.109 8.952 42.932 1.00 12.86 ? 305 HIS A CG 1 ATOM 2348 N ND1 . HIS A 1 305 ? -12.820 7.609 42.814 1.00 14.88 ? 305 HIS A ND1 1 ATOM 2349 C CD2 . HIS A 1 305 ? -11.917 9.587 43.035 1.00 15.41 ? 305 HIS A CD2 1 ATOM 2350 C CE1 . HIS A 1 305 ? -11.509 7.441 42.839 1.00 17.21 ? 305 HIS A CE1 1 ATOM 2351 N NE2 . HIS A 1 305 ? -10.938 8.626 42.972 1.00 15.23 ? 305 HIS A NE2 1 ATOM 2352 N N . PRO A 1 306 ? -17.492 9.377 40.594 1.00 12.48 ? 306 PRO A N 1 ATOM 2353 C CA . PRO A 1 306 ? -18.895 9.831 40.601 1.00 12.15 ? 306 PRO A CA 1 ATOM 2354 C C . PRO A 1 306 ? -19.598 9.156 41.773 1.00 10.32 ? 306 PRO A C 1 ATOM 2355 O O . PRO A 1 306 ? -19.495 7.939 41.956 1.00 10.13 ? 306 PRO A O 1 ATOM 2356 C CB . PRO A 1 306 ? -19.436 9.319 39.266 1.00 13.31 ? 306 PRO A CB 1 ATOM 2357 C CG . PRO A 1 306 ? -18.198 9.121 38.421 1.00 15.24 ? 306 PRO A CG 1 ATOM 2358 C CD . PRO A 1 306 ? -17.243 8.542 39.407 1.00 13.88 ? 306 PRO A CD 1 ATOM 2359 N N . ALA A 1 307 ? -20.239 9.962 42.606 1.00 11.11 ? 307 ALA A N 1 ATOM 2360 C CA . ALA A 1 307 ? -20.899 9.440 43.784 1.00 10.59 ? 307 ALA A CA 1 ATOM 2361 C C . ALA A 1 307 ? -22.109 10.226 44.241 1.00 10.53 ? 307 ALA A C 1 ATOM 2362 O O . ALA A 1 307 ? -22.325 11.361 43.818 1.00 9.90 ? 307 ALA A O 1 ATOM 2363 C CB . ALA A 1 307 ? -19.890 9.312 44.931 1.00 11.62 ? 307 ALA A CB 1 ATOM 2364 N N . ALA A 1 308 ? -22.918 9.561 45.066 1.00 12.20 ? 308 ALA A N 1 ATOM 2365 C CA . ALA A 1 308 ? -24.127 10.113 45.668 1.00 13.86 ? 308 ALA A CA 1 ATOM 2366 C C . ALA A 1 308 ? -23.998 9.920 47.175 1.00 15.17 ? 308 ALA A C 1 ATOM 2367 O O . ALA A 1 308 ? -23.281 9.028 47.631 1.00 14.22 ? 308 ALA A O 1 ATOM 2368 C CB . ALA A 1 308 ? -25.354 9.381 45.162 1.00 12.85 ? 308 ALA A CB 1 ATOM 2369 N N . ILE A 1 309 ? -24.684 10.767 47.939 1.00 17.42 ? 309 ILE A N 1 ATOM 2370 C CA . ILE A 1 309 ? -24.662 10.695 49.399 1.00 19.13 ? 309 ILE A CA 1 ATOM 2371 C C . ILE A 1 309 ? -25.953 10.073 49.923 1.00 20.35 ? 309 ILE A C 1 ATOM 2372 O O . ILE A 1 309 ? -27.049 10.462 49.518 1.00 21.50 ? 309 ILE A O 1 ATOM 2373 C CB . ILE A 1 309 ? -24.510 12.106 50.065 1.00 19.15 ? 309 ILE A CB 1 ATOM 2374 C CG1 . ILE A 1 309 ? -23.290 12.845 49.503 1.00 20.65 ? 309 ILE A CG1 1 ATOM 2375 C CG2 . ILE A 1 309 ? -24.391 11.970 51.611 1.00 20.34 ? 309 ILE A CG2 1 ATOM 2376 C CD1 . ILE A 1 309 ? -23.139 14.292 49.974 1.00 20.45 ? 309 ILE A CD1 1 ATOM 2377 N N . PHE A 1 310 ? -25.802 9.091 50.808 1.00 21.02 ? 310 PHE A N 1 ATOM 2378 C CA . PHE A 1 310 ? -26.934 8.445 51.457 1.00 21.41 ? 310 PHE A CA 1 ATOM 2379 C C . PHE A 1 310 ? -26.915 8.880 52.926 1.00 22.33 ? 310 PHE A C 1 ATOM 2380 O O . PHE A 1 310 ? -26.115 8.397 53.737 1.00 20.56 ? 310 PHE A O 1 ATOM 2381 C CB . PHE A 1 310 ? -26.881 6.920 51.302 1.00 21.69 ? 310 PHE A CB 1 ATOM 2382 C CG . PHE A 1 310 ? -27.572 6.405 50.061 1.00 20.84 ? 310 PHE A CG 1 ATOM 2383 C CD1 . PHE A 1 310 ? -27.162 6.818 48.779 1.00 19.98 ? 310 PHE A CD1 1 ATOM 2384 C CD2 . PHE A 1 310 ? -28.636 5.496 50.168 1.00 21.09 ? 310 PHE A CD2 1 ATOM 2385 C CE1 . PHE A 1 310 ? -27.804 6.331 47.620 1.00 19.62 ? 310 PHE A CE1 1 ATOM 2386 C CE2 . PHE A 1 310 ? -29.292 4.994 49.019 1.00 19.84 ? 310 PHE A CE2 1 ATOM 2387 C CZ . PHE A 1 310 ? -28.871 5.416 47.737 1.00 19.69 ? 310 PHE A CZ 1 ATOM 2388 N N . HIS A 1 311 ? -27.758 9.867 53.222 1.00 22.99 ? 311 HIS A N 1 ATOM 2389 C CA . HIS A 1 311 ? -27.883 10.442 54.554 1.00 24.00 ? 311 HIS A CA 1 ATOM 2390 C C . HIS A 1 311 ? -28.928 9.746 55.430 1.00 24.75 ? 311 HIS A C 1 ATOM 2391 O O . HIS A 1 311 ? -30.067 9.547 55.016 1.00 23.95 ? 311 HIS A O 1 ATOM 2392 C CB . HIS A 1 311 ? -28.191 11.951 54.437 1.00 23.69 ? 311 HIS A CB 1 ATOM 2393 C CG . HIS A 1 311 ? -28.431 12.636 55.751 1.00 26.58 ? 311 HIS A CG 1 ATOM 2394 N ND1 . HIS A 1 311 ? -29.674 13.099 56.129 1.00 26.10 ? 311 HIS A ND1 1 ATOM 2395 C CD2 . HIS A 1 311 ? -27.602 12.900 56.789 1.00 25.06 ? 311 HIS A CD2 1 ATOM 2396 C CE1 . HIS A 1 311 ? -29.598 13.615 57.341 1.00 25.85 ? 311 HIS A CE1 1 ATOM 2397 N NE2 . HIS A 1 311 ? -28.353 13.505 57.765 1.00 24.97 ? 311 HIS A NE2 1 ATOM 2398 N N . TYR A 1 312 ? -28.514 9.387 56.645 1.00 25.85 ? 312 TYR A N 1 ATOM 2399 C CA . TYR A 1 312 ? -29.401 8.776 57.634 1.00 27.26 ? 312 TYR A CA 1 ATOM 2400 C C . TYR A 1 312 ? -30.073 9.935 58.344 1.00 27.03 ? 312 TYR A C 1 ATOM 2401 O O . TYR A 1 312 ? -29.386 10.856 58.771 1.00 27.56 ? 312 TYR A O 1 ATOM 2402 C CB . TYR A 1 312 ? -28.602 7.993 58.668 1.00 27.67 ? 312 TYR A CB 1 ATOM 2403 C CG . TYR A 1 312 ? -28.371 6.545 58.337 1.00 29.52 ? 312 TYR A CG 1 ATOM 2404 C CD1 . TYR A 1 312 ? -27.550 6.166 57.252 1.00 28.80 ? 312 TYR A CD1 1 ATOM 2405 C CD2 . TYR A 1 312 ? -28.950 5.530 59.130 1.00 29.09 ? 312 TYR A CD2 1 ATOM 2406 C CE1 . TYR A 1 312 ? -27.306 4.793 56.962 1.00 29.67 ? 312 TYR A CE1 1 ATOM 2407 C CE2 . TYR A 1 312 ? -28.715 4.154 58.852 1.00 30.10 ? 312 TYR A CE2 1 ATOM 2408 C CZ . TYR A 1 312 ? -27.891 3.798 57.764 1.00 29.15 ? 312 TYR A CZ 1 ATOM 2409 O OH . TYR A 1 312 ? -27.660 2.474 57.481 1.00 25.39 ? 312 TYR A OH 1 ATOM 2410 N N . ALA A 1 313 ? -31.402 9.908 58.445 1.00 28.32 ? 313 ALA A N 1 ATOM 2411 C CA . ALA A 1 313 ? -32.168 10.968 59.119 1.00 30.56 ? 313 ALA A CA 1 ATOM 2412 C C . ALA A 1 313 ? -31.775 11.107 60.599 1.00 32.37 ? 313 ALA A C 1 ATOM 2413 O O . ALA A 1 313 ? -31.747 10.117 61.340 1.00 32.30 ? 313 ALA A O 1 ATOM 2414 C CB . ALA A 1 313 ? -33.669 10.709 58.985 1.00 28.70 ? 313 ALA A CB 1 ATOM 2415 N N . GLY A 1 314 ? -31.401 12.328 60.985 1.00 34.51 ? 314 GLY A N 1 ATOM 2416 C CA . GLY A 1 314 ? -30.988 12.606 62.353 1.00 36.65 ? 314 GLY A CA 1 ATOM 2417 C C . GLY A 1 314 ? -29.478 12.671 62.522 1.00 37.77 ? 314 GLY A C 1 ATOM 2418 O O . GLY A 1 314 ? -28.977 13.023 63.596 1.00 38.34 ? 314 GLY A O 1 ATOM 2419 N N . ALA A 1 315 ? -28.757 12.325 61.457 1.00 37.54 ? 315 ALA A N 1 ATOM 2420 C CA . ALA A 1 315 ? -27.295 12.336 61.436 1.00 37.86 ? 315 ALA A CA 1 ATOM 2421 C C . ALA A 1 315 ? -26.809 13.720 60.979 1.00 38.16 ? 315 ALA A C 1 ATOM 2422 O O . ALA A 1 315 ? -27.607 14.491 60.431 1.00 37.89 ? 315 ALA A O 1 ATOM 2423 C CB . ALA A 1 315 ? -26.795 11.255 60.484 1.00 37.24 ? 315 ALA A CB 1 ATOM 2424 N N . PRO A 1 316 ? -25.523 14.087 61.255 1.00 38.50 ? 316 PRO A N 1 ATOM 2425 C CA . PRO A 1 316 ? -25.019 15.401 60.824 1.00 38.27 ? 316 PRO A CA 1 ATOM 2426 C C . PRO A 1 316 ? -24.924 15.504 59.303 1.00 38.74 ? 316 PRO A C 1 ATOM 2427 O O . PRO A 1 316 ? -24.895 14.483 58.609 1.00 38.32 ? 316 PRO A O 1 ATOM 2428 C CB . PRO A 1 316 ? -23.627 15.452 61.451 1.00 37.92 ? 316 PRO A CB 1 ATOM 2429 C CG . PRO A 1 316 ? -23.788 14.659 62.678 1.00 38.79 ? 316 PRO A CG 1 ATOM 2430 C CD . PRO A 1 316 ? -24.544 13.465 62.172 1.00 38.14 ? 316 PRO A CD 1 ATOM 2431 N N . GLY A 1 317 ? -24.867 16.737 58.800 1.00 39.12 ? 317 GLY A N 1 ATOM 2432 C CA . GLY A 1 317 ? -24.774 16.971 57.368 1.00 38.97 ? 317 GLY A CA 1 ATOM 2433 C C . GLY A 1 317 ? -23.380 16.786 56.795 1.00 38.89 ? 317 GLY A C 1 ATOM 2434 O O . GLY A 1 317 ? -22.569 16.023 57.333 1.00 39.55 ? 317 GLY A O 1 ATOM 2435 N N . GLY A 1 318 ? -23.122 17.461 55.678 1.00 38.57 ? 318 GLY A N 1 ATOM 2436 C CA . GLY A 1 318 ? -21.825 17.387 55.029 1.00 38.45 ? 318 GLY A CA 1 ATOM 2437 C C . GLY A 1 318 ? -21.562 16.164 54.167 1.00 37.61 ? 318 GLY A C 1 ATOM 2438 O O . GLY A 1 318 ? -22.454 15.352 53.897 1.00 36.60 ? 318 GLY A O 1 ATOM 2439 N N . LEU A 1 319 ? -20.304 16.041 53.756 1.00 36.95 ? 319 LEU A N 1 ATOM 2440 C CA . LEU A 1 319 ? -19.842 14.953 52.906 1.00 36.13 ? 319 LEU A CA 1 ATOM 2441 C C . LEU A 1 319 ? -19.371 13.748 53.730 1.00 36.24 ? 319 LEU A C 1 ATOM 2442 O O . LEU A 1 319 ? -18.957 13.918 54.882 1.00 37.20 ? 319 LEU A O 1 ATOM 2443 C CB . LEU A 1 319 ? -18.700 15.459 52.000 1.00 35.97 ? 319 LEU A CB 1 ATOM 2444 C CG . LEU A 1 319 ? -18.876 16.748 51.179 1.00 35.37 ? 319 LEU A CG 1 ATOM 2445 C CD1 . LEU A 1 319 ? -17.736 16.871 50.189 1.00 34.43 ? 319 LEU A CD1 1 ATOM 2446 C CD2 . LEU A 1 319 ? -20.208 16.768 50.442 1.00 34.12 ? 319 LEU A CD2 1 ATOM 2447 N N . PRO A 1 320 ? -19.527 12.508 53.196 1.00 35.82 ? 320 PRO A N 1 ATOM 2448 C CA . PRO A 1 320 ? -19.099 11.280 53.886 1.00 34.70 ? 320 PRO A CA 1 ATOM 2449 C C . PRO A 1 320 ? -17.588 11.261 54.044 1.00 33.24 ? 320 PRO A C 1 ATOM 2450 O O . PRO A 1 320 ? -16.857 11.644 53.128 1.00 32.61 ? 320 PRO A O 1 ATOM 2451 C CB . PRO A 1 320 ? -19.545 10.178 52.937 1.00 34.08 ? 320 PRO A CB 1 ATOM 2452 C CG . PRO A 1 320 ? -20.733 10.738 52.301 1.00 34.41 ? 320 PRO A CG 1 ATOM 2453 C CD . PRO A 1 320 ? -20.387 12.162 52.046 1.00 35.73 ? 320 PRO A CD 1 ATOM 2454 N N . THR A 1 321 ? -17.140 10.815 55.212 1.00 33.31 ? 321 THR A N 1 ATOM 2455 C CA . THR A 1 321 ? -15.723 10.767 55.548 1.00 33.67 ? 321 THR A CA 1 ATOM 2456 C C . THR A 1 321 ? -14.993 9.490 55.139 1.00 34.48 ? 321 THR A C 1 ATOM 2457 O O . THR A 1 321 ? -13.773 9.508 54.939 1.00 35.26 ? 321 THR A O 1 ATOM 2458 C CB . THR A 1 321 ? -15.528 11.023 57.051 1.00 34.26 ? 321 THR A CB 1 ATOM 2459 O OG1 . THR A 1 321 ? -16.351 10.118 57.799 1.00 34.69 ? 321 THR A OG1 1 ATOM 2460 C CG2 . THR A 1 321 ? -15.911 12.464 57.399 1.00 32.06 ? 321 THR A CG2 1 ATOM 2461 N N . ASP A 1 322 ? -15.742 8.395 55.011 1.00 33.97 ? 322 ASP A N 1 ATOM 2462 C CA . ASP A 1 322 ? -15.188 7.097 54.630 1.00 34.18 ? 322 ASP A CA 1 ATOM 2463 C C . ASP A 1 322 ? -15.252 6.928 53.108 1.00 34.82 ? 322 ASP A C 1 ATOM 2464 O O . ASP A 1 322 ? -16.331 6.744 52.544 1.00 35.29 ? 322 ASP A O 1 ATOM 2465 C CB . ASP A 1 322 ? -15.967 5.974 55.348 1.00 34.07 ? 322 ASP A CB 1 ATOM 2466 C CG . ASP A 1 322 ? -15.362 4.572 55.144 1.00 35.13 ? 322 ASP A CG 1 ATOM 2467 O OD1 . ASP A 1 322 ? -14.221 4.431 54.643 1.00 35.92 ? 322 ASP A OD1 1 ATOM 2468 O OD2 . ASP A 1 322 ? -16.051 3.594 55.500 1.00 33.47 ? 322 ASP A OD2 1 ATOM 2469 N N . GLU A 1 323 ? -14.085 6.965 52.460 1.00 35.10 ? 323 GLU A N 1 ATOM 2470 C CA . GLU A 1 323 ? -13.979 6.805 51.007 1.00 35.23 ? 323 GLU A CA 1 ATOM 2471 C C . GLU A 1 323 ? -14.317 5.384 50.570 1.00 35.60 ? 323 GLU A C 1 ATOM 2472 O O . GLU A 1 323 ? -14.794 5.172 49.457 1.00 35.89 ? 323 GLU A O 1 ATOM 2473 C CB . GLU A 1 323 ? -12.587 7.205 50.512 1.00 34.65 ? 323 GLU A CB 1 ATOM 2474 C CG . GLU A 1 323 ? -12.359 8.715 50.517 1.00 37.72 ? 323 GLU A CG 1 ATOM 2475 C CD . GLU A 1 323 ? -10.968 9.144 50.064 1.00 38.37 ? 323 GLU A CD 1 ATOM 2476 O OE1 . GLU A 1 323 ? -10.162 8.280 49.659 1.00 38.65 ? 323 GLU A OE1 1 ATOM 2477 O OE2 . GLU A 1 323 ? -10.685 10.364 50.107 1.00 38.25 ? 323 GLU A OE2 1 ATOM 2478 N N . GLY A 1 324 ? -14.102 4.431 51.478 1.00 35.87 ? 324 GLY A N 1 ATOM 2479 C CA . GLY A 1 324 ? -14.401 3.033 51.215 1.00 35.62 ? 324 GLY A CA 1 ATOM 2480 C C . GLY A 1 324 ? -13.353 2.226 50.474 1.00 36.12 ? 324 GLY A C 1 ATOM 2481 O O . GLY A 1 324 ? -12.283 2.728 50.108 1.00 35.48 ? 324 GLY A O 1 ATOM 2482 N N . THR A 1 325 ? -13.674 0.949 50.282 1.00 36.37 ? 325 THR A N 1 ATOM 2483 C CA . THR A 1 325 ? -12.817 -0.001 49.585 1.00 37.36 ? 325 THR A CA 1 ATOM 2484 C C . THR A 1 325 ? -13.383 -0.207 48.174 1.00 38.58 ? 325 THR A C 1 ATOM 2485 O O . THR A 1 325 ? -14.606 -0.344 48.023 1.00 38.47 ? 325 THR A O 1 ATOM 2486 C CB . THR A 1 325 ? -12.781 -1.363 50.334 1.00 37.73 ? 325 THR A CB 1 ATOM 2487 O OG1 . THR A 1 325 ? -14.117 -1.851 50.521 1.00 36.08 ? 325 THR A OG1 1 ATOM 2488 C CG2 . THR A 1 325 ? -12.108 -1.211 51.694 1.00 37.54 ? 325 THR A CG2 1 ATOM 2489 N N . PRO A 1 326 ? -12.523 -0.171 47.121 1.00 38.99 ? 326 PRO A N 1 ATOM 2490 C CA . PRO A 1 326 ? -13.007 -0.367 45.745 1.00 39.72 ? 326 PRO A CA 1 ATOM 2491 C C . PRO A 1 326 ? -13.634 -1.759 45.542 1.00 39.45 ? 326 PRO A C 1 ATOM 2492 O O . PRO A 1 326 ? -13.064 -2.767 45.972 1.00 39.66 ? 326 PRO A O 1 ATOM 2493 C CB . PRO A 1 326 ? -11.742 -0.155 44.898 1.00 40.70 ? 326 PRO A CB 1 ATOM 2494 C CG . PRO A 1 326 ? -10.619 -0.489 45.833 1.00 40.46 ? 326 PRO A CG 1 ATOM 2495 C CD . PRO A 1 326 ? -11.083 0.158 47.107 1.00 40.95 ? 326 PRO A CD 1 ATOM 2496 N N . PRO A 1 327 ? -14.851 -1.819 44.958 1.00 39.37 ? 327 PRO A N 1 ATOM 2497 C CA . PRO A 1 327 ? -15.543 -3.094 44.722 1.00 38.65 ? 327 PRO A CA 1 ATOM 2498 C C . PRO A 1 327 ? -14.911 -4.013 43.678 1.00 37.38 ? 327 PRO A C 1 ATOM 2499 O O . PRO A 1 327 ? -14.052 -3.591 42.893 1.00 36.54 ? 327 PRO A O 1 ATOM 2500 C CB . PRO A 1 327 ? -16.943 -2.646 44.309 1.00 39.52 ? 327 PRO A CB 1 ATOM 2501 C CG . PRO A 1 327 ? -16.689 -1.368 43.607 1.00 39.17 ? 327 PRO A CG 1 ATOM 2502 C CD . PRO A 1 327 ? -15.702 -0.693 44.524 1.00 40.05 ? 327 PRO A CD 1 ATOM 2503 N N . VAL A 1 328 ? -15.372 -5.264 43.679 1.00 35.49 ? 328 VAL A N 1 ATOM 2504 C CA . VAL A 1 328 ? -14.900 -6.308 42.769 1.00 33.89 ? 328 VAL A CA 1 ATOM 2505 C C . VAL A 1 328 ? -15.087 -5.965 41.289 1.00 32.25 ? 328 VAL A C 1 ATOM 2506 O O . VAL A 1 328 ? -16.076 -5.333 40.907 1.00 32.37 ? 328 VAL A O 1 ATOM 2507 C CB . VAL A 1 328 ? -15.575 -7.683 43.075 1.00 34.30 ? 328 VAL A CB 1 ATOM 2508 C CG1 . VAL A 1 328 ? -15.086 -8.224 44.404 1.00 35.42 ? 328 VAL A CG1 1 ATOM 2509 C CG2 . VAL A 1 328 ? -17.104 -7.563 43.090 1.00 34.99 ? 328 VAL A CG2 1 ATOM 2510 N N . ASP A 1 329 ? -14.105 -6.352 40.479 1.00 29.64 ? 329 ASP A N 1 ATOM 2511 C CA . ASP A 1 329 ? -14.134 -6.110 39.041 1.00 27.10 ? 329 ASP A CA 1 ATOM 2512 C C . ASP A 1 329 ? -15.137 -7.082 38.415 1.00 23.55 ? 329 ASP A C 1 ATOM 2513 O O . ASP A 1 329 ? -14.924 -8.298 38.427 1.00 23.60 ? 329 ASP A O 1 ATOM 2514 C CB . ASP A 1 329 ? -12.733 -6.307 38.446 1.00 27.33 ? 329 ASP A CB 1 ATOM 2515 C CG . ASP A 1 329 ? -12.523 -5.517 37.175 1.00 29.37 ? 329 ASP A CG 1 ATOM 2516 O OD1 . ASP A 1 329 ? -13.360 -5.624 36.261 1.00 30.20 ? 329 ASP A OD1 1 ATOM 2517 O OD2 . ASP A 1 329 ? -11.521 -4.780 37.085 1.00 33.94 ? 329 ASP A OD2 1 ATOM 2518 N N . HIS A 1 330 ? -16.251 -6.538 37.927 1.00 20.55 ? 330 HIS A N 1 ATOM 2519 C CA . HIS A 1 330 ? -17.307 -7.344 37.307 1.00 18.60 ? 330 HIS A CA 1 ATOM 2520 C C . HIS A 1 330 ? -16.994 -7.778 35.883 1.00 15.29 ? 330 HIS A C 1 ATOM 2521 O O . HIS A 1 330 ? -17.690 -8.619 35.319 1.00 15.81 ? 330 HIS A O 1 ATOM 2522 C CB . HIS A 1 330 ? -18.658 -6.633 37.379 1.00 18.92 ? 330 HIS A CB 1 ATOM 2523 C CG . HIS A 1 330 ? -19.283 -6.664 38.739 1.00 19.87 ? 330 HIS A CG 1 ATOM 2524 N ND1 . HIS A 1 330 ? -19.725 -7.828 39.326 1.00 21.91 ? 330 HIS A ND1 1 ATOM 2525 C CD2 . HIS A 1 330 ? -19.533 -5.676 39.630 1.00 21.10 ? 330 HIS A CD2 1 ATOM 2526 C CE1 . HIS A 1 330 ? -20.223 -7.556 40.519 1.00 22.54 ? 330 HIS A CE1 1 ATOM 2527 N NE2 . HIS A 1 330 ? -20.118 -6.256 40.728 1.00 19.45 ? 330 HIS A NE2 1 ATOM 2528 N N . GLN A 1 331 ? -15.898 -7.241 35.348 1.00 12.38 ? 331 GLN A N 1 ATOM 2529 C CA . GLN A 1 331 ? -15.389 -7.538 34.007 1.00 14.10 ? 331 GLN A CA 1 ATOM 2530 C C . GLN A 1 331 ? -16.398 -7.409 32.867 1.00 13.31 ? 331 GLN A C 1 ATOM 2531 O O . GLN A 1 331 ? -16.477 -8.262 31.978 1.00 14.44 ? 331 GLN A O 1 ATOM 2532 C CB . GLN A 1 331 ? -14.681 -8.903 33.981 1.00 13.97 ? 331 GLN A CB 1 ATOM 2533 C CG . GLN A 1 331 ? -13.522 -9.038 34.968 1.00 13.56 ? 331 GLN A CG 1 ATOM 2534 C CD . GLN A 1 331 ? -12.272 -8.250 34.582 1.00 13.88 ? 331 GLN A CD 1 ATOM 2535 O OE1 . GLN A 1 331 ? -12.180 -7.668 33.490 1.00 9.08 ? 331 GLN A OE1 1 ATOM 2536 N NE2 . GLN A 1 331 ? -11.283 -8.264 35.472 1.00 12.48 ? 331 GLN A NE2 1 ATOM 2537 N N . CYS A 1 332 ? -17.177 -6.329 32.933 1.00 12.91 ? 332 CYS A N 1 ATOM 2538 C CA . CYS A 1 332 ? -18.225 -5.999 31.972 1.00 12.13 ? 332 CYS A CA 1 ATOM 2539 C C . CYS A 1 332 ? -19.290 -7.085 31.790 1.00 11.69 ? 332 CYS A C 1 ATOM 2540 O O . CYS A 1 332 ? -19.800 -7.292 30.686 1.00 10.97 ? 332 CYS A O 1 ATOM 2541 C CB . CYS A 1 332 ? -17.629 -5.557 30.633 1.00 9.98 ? 332 CYS A CB 1 ATOM 2542 S SG . CYS A 1 332 ? -16.609 -4.061 30.754 1.00 12.01 ? 332 CYS A SG 1 ATOM 2543 N N . LEU A 1 333 ? -19.601 -7.788 32.885 1.00 12.48 ? 333 LEU A N 1 ATOM 2544 C CA . LEU A 1 333 ? -20.581 -8.877 32.871 1.00 13.76 ? 333 LEU A CA 1 ATOM 2545 C C . LEU A 1 333 ? -21.625 -8.762 33.961 1.00 14.77 ? 333 LEU A C 1 ATOM 2546 O O . LEU A 1 333 ? -21.296 -8.500 35.117 1.00 16.29 ? 333 LEU A O 1 ATOM 2547 C CB . LEU A 1 333 ? -19.888 -10.233 33.030 1.00 14.34 ? 333 LEU A CB 1 ATOM 2548 C CG . LEU A 1 333 ? -18.836 -10.670 32.018 1.00 15.08 ? 333 LEU A CG 1 ATOM 2549 C CD1 . LEU A 1 333 ? -17.854 -11.612 32.668 1.00 14.29 ? 333 LEU A CD1 1 ATOM 2550 C CD2 . LEU A 1 333 ? -19.489 -11.239 30.785 1.00 12.60 ? 333 LEU A CD2 1 ATOM 2551 N N . ASP A 1 334 ? -22.890 -8.927 33.577 1.00 17.10 ? 334 ASP A N 1 ATOM 2552 C CA . ASP A 1 334 ? -24.004 -8.899 34.529 1.00 16.56 ? 334 ASP A CA 1 ATOM 2553 C C . ASP A 1 334 ? -24.140 -10.263 35.177 1.00 16.55 ? 334 ASP A C 1 ATOM 2554 O O . ASP A 1 334 ? -23.819 -11.277 34.554 1.00 17.43 ? 334 ASP A O 1 ATOM 2555 C CB . ASP A 1 334 ? -25.319 -8.442 33.878 1.00 15.78 ? 334 ASP A CB 1 ATOM 2556 C CG . ASP A 1 334 ? -25.639 -9.165 32.571 1.00 17.62 ? 334 ASP A CG 1 ATOM 2557 O OD1 . ASP A 1 334 ? -24.715 -9.413 31.768 1.00 13.15 ? 334 ASP A OD1 1 ATOM 2558 O OD2 . ASP A 1 334 ? -26.835 -9.459 32.345 1.00 16.25 ? 334 ASP A OD2 1 ATOM 2559 N N . THR A 1 335 ? -24.543 -10.279 36.448 1.00 16.59 ? 335 THR A N 1 ATOM 2560 C CA . THR A 1 335 ? -24.681 -11.527 37.184 1.00 15.44 ? 335 THR A CA 1 ATOM 2561 C C . THR A 1 335 ? -25.819 -12.406 36.677 1.00 15.34 ? 335 THR A C 1 ATOM 2562 O O . THR A 1 335 ? -26.934 -11.932 36.400 1.00 11.87 ? 335 THR A O 1 ATOM 2563 C CB . THR A 1 335 ? -24.776 -11.301 38.729 1.00 16.74 ? 335 THR A CB 1 ATOM 2564 O OG1 . THR A 1 335 ? -24.685 -12.561 39.394 1.00 15.88 ? 335 THR A OG1 1 ATOM 2565 C CG2 . THR A 1 335 ? -26.090 -10.624 39.136 1.00 17.48 ? 335 THR A CG2 1 ATOM 2566 N N . LEU A 1 336 ? -25.479 -13.676 36.485 1.00 14.42 ? 336 LEU A N 1 ATOM 2567 C CA . LEU A 1 336 ? -26.432 -14.660 36.027 1.00 14.43 ? 336 LEU A CA 1 ATOM 2568 C C . LEU A 1 336 ? -26.929 -15.539 37.176 1.00 15.23 ? 336 LEU A C 1 ATOM 2569 O O . LEU A 1 336 ? -27.609 -16.549 36.952 1.00 16.53 ? 336 LEU A O 1 ATOM 2570 C CB . LEU A 1 336 ? -25.845 -15.499 34.882 1.00 14.62 ? 336 LEU A CB 1 ATOM 2571 C CG . LEU A 1 336 ? -25.501 -14.805 33.553 1.00 12.56 ? 336 LEU A CG 1 ATOM 2572 C CD1 . LEU A 1 336 ? -25.130 -15.842 32.515 1.00 11.68 ? 336 LEU A CD1 1 ATOM 2573 C CD2 . LEU A 1 336 ? -26.639 -13.951 33.053 1.00 11.96 ? 336 LEU A CD2 1 ATOM 2574 N N . ASP A 1 337 ? -26.643 -15.117 38.407 1.00 14.77 ? 337 ASP A N 1 ATOM 2575 C CA . ASP A 1 337 ? -27.074 -15.855 39.595 1.00 14.82 ? 337 ASP A CA 1 ATOM 2576 C C . ASP A 1 337 ? -28.556 -15.604 39.920 1.00 14.52 ? 337 ASP A C 1 ATOM 2577 O O . ASP A 1 337 ? -29.175 -16.397 40.633 1.00 16.52 ? 337 ASP A O 1 ATOM 2578 C CB . ASP A 1 337 ? -26.189 -15.518 40.802 1.00 16.15 ? 337 ASP A CB 1 ATOM 2579 C CG . ASP A 1 337 ? -24.751 -16.015 40.649 1.00 17.84 ? 337 ASP A CG 1 ATOM 2580 O OD1 . ASP A 1 337 ? -24.530 -17.128 40.120 1.00 19.54 ? 337 ASP A OD1 1 ATOM 2581 O OD2 . ASP A 1 337 ? -23.833 -15.288 41.076 1.00 18.08 ? 337 ASP A OD2 1 ATOM 2582 N N . VAL A 1 338 ? -29.121 -14.535 39.348 1.00 11.83 ? 338 VAL A N 1 ATOM 2583 C CA . VAL A 1 338 ? -30.532 -14.164 39.535 1.00 11.77 ? 338 VAL A CA 1 ATOM 2584 C C . VAL A 1 338 ? -31.534 -15.210 39.016 1.00 12.73 ? 338 VAL A C 1 ATOM 2585 O O . VAL A 1 338 ? -31.409 -15.718 37.889 1.00 11.10 ? 338 VAL A O 1 ATOM 2586 C CB . VAL A 1 338 ? -30.871 -12.770 38.923 1.00 11.26 ? 338 VAL A CB 1 ATOM 2587 C CG1 . VAL A 1 338 ? -30.373 -11.665 39.827 1.00 10.99 ? 338 VAL A CG1 1 ATOM 2588 C CG2 . VAL A 1 338 ? -30.276 -12.616 37.528 1.00 11.24 ? 338 VAL A CG2 1 ATOM 2589 N N . ARG A 1 339 ? -32.473 -15.580 39.888 1.00 11.90 ? 339 ARG A N 1 ATOM 2590 C CA . ARG A 1 339 ? -33.498 -16.577 39.581 1.00 12.96 ? 339 ARG A CA 1 ATOM 2591 C C . ARG A 1 339 ? -34.893 -15.969 39.727 1.00 13.02 ? 339 ARG A C 1 ATOM 2592 O O . ARG A 1 339 ? -35.297 -15.601 40.833 1.00 14.34 ? 339 ARG A O 1 ATOM 2593 C CB . ARG A 1 339 ? -33.379 -17.792 40.515 1.00 13.47 ? 339 ARG A CB 1 ATOM 2594 C CG . ARG A 1 339 ? -32.051 -18.539 40.482 1.00 17.41 ? 339 ARG A CG 1 ATOM 2595 C CD . ARG A 1 339 ? -31.980 -19.518 39.321 1.00 20.31 ? 339 ARG A CD 1 ATOM 2596 N NE . ARG A 1 339 ? -30.641 -20.083 39.133 1.00 21.17 ? 339 ARG A NE 1 ATOM 2597 C CZ . ARG A 1 339 ? -29.641 -19.478 38.490 1.00 21.00 ? 339 ARG A CZ 1 ATOM 2598 N NH1 . ARG A 1 339 ? -29.810 -18.269 37.957 1.00 17.94 ? 339 ARG A NH1 1 ATOM 2599 N NH2 . ARG A 1 339 ? -28.465 -20.090 38.383 1.00 17.89 ? 339 ARG A NH2 1 ATOM 2600 N N . PRO A 1 340 ? -35.643 -15.835 38.612 1.00 13.53 ? 340 PRO A N 1 ATOM 2601 C CA . PRO A 1 340 ? -37.007 -15.270 38.600 1.00 14.70 ? 340 PRO A CA 1 ATOM 2602 C C . PRO A 1 340 ? -37.970 -15.967 39.569 1.00 14.51 ? 340 PRO A C 1 ATOM 2603 O O . PRO A 1 340 ? -37.799 -17.158 39.856 1.00 14.83 ? 340 PRO A O 1 ATOM 2604 C CB . PRO A 1 340 ? -37.446 -15.486 37.151 1.00 14.37 ? 340 PRO A CB 1 ATOM 2605 C CG . PRO A 1 340 ? -36.170 -15.358 36.401 1.00 13.44 ? 340 PRO A CG 1 ATOM 2606 C CD . PRO A 1 340 ? -35.206 -16.151 37.237 1.00 12.19 ? 340 PRO A CD 1 ATOM 2607 N N . VAL A 1 341 ? -38.957 -15.222 40.081 1.00 14.07 ? 341 VAL A N 1 ATOM 2608 C CA . VAL A 1 341 ? -39.952 -15.775 41.012 1.00 14.51 ? 341 VAL A CA 1 ATOM 2609 C C . VAL A 1 341 ? -40.839 -16.755 40.247 1.00 13.49 ? 341 VAL A C 1 ATOM 2610 O O . VAL A 1 341 ? -40.960 -17.910 40.641 1.00 13.19 ? 341 VAL A O 1 ATOM 2611 C CB . VAL A 1 341 ? -40.804 -14.667 41.710 1.00 15.10 ? 341 VAL A CB 1 ATOM 2612 C CG1 . VAL A 1 341 ? -41.777 -15.286 42.724 1.00 15.99 ? 341 VAL A CG1 1 ATOM 2613 C CG2 . VAL A 1 341 ? -39.906 -13.699 42.438 1.00 13.57 ? 341 VAL A CG2 1 ATOM 2614 N N . VAL A 1 342 ? -41.386 -16.292 39.123 1.00 15.65 ? 342 VAL A N 1 ATOM 2615 C CA . VAL A 1 342 ? -42.216 -17.109 38.231 1.00 16.78 ? 342 VAL A CA 1 ATOM 2616 C C . VAL A 1 342 ? -41.209 -17.845 37.330 1.00 17.17 ? 342 VAL A C 1 ATOM 2617 O O . VAL A 1 342 ? -40.506 -17.210 36.551 1.00 18.85 ? 342 VAL A O 1 ATOM 2618 C CB . VAL A 1 342 ? -43.172 -16.227 37.365 1.00 17.28 ? 342 VAL A CB 1 ATOM 2619 C CG1 . VAL A 1 342 ? -44.076 -17.103 36.481 1.00 15.24 ? 342 VAL A CG1 1 ATOM 2620 C CG2 . VAL A 1 342 ? -44.015 -15.331 38.266 1.00 15.60 ? 342 VAL A CG2 1 ATOM 2621 N N . PRO A 1 343 ? -41.118 -19.187 37.442 1.00 18.14 ? 343 PRO A N 1 ATOM 2622 C CA . PRO A 1 343 ? -40.170 -19.947 36.623 1.00 19.44 ? 343 PRO A CA 1 ATOM 2623 C C . PRO A 1 343 ? -40.559 -20.280 35.187 1.00 20.07 ? 343 PRO A C 1 ATOM 2624 O O . PRO A 1 343 ? -41.727 -20.203 34.800 1.00 19.70 ? 343 PRO A O 1 ATOM 2625 C CB . PRO A 1 343 ? -39.967 -21.215 37.446 1.00 20.27 ? 343 PRO A CB 1 ATOM 2626 C CG . PRO A 1 343 ? -41.339 -21.470 37.986 1.00 20.09 ? 343 PRO A CG 1 ATOM 2627 C CD . PRO A 1 343 ? -41.834 -20.085 38.375 1.00 20.13 ? 343 PRO A CD 1 ATOM 2628 N N . ARG A 1 344 ? -39.536 -20.626 34.412 1.00 20.93 ? 344 ARG A N 1 ATOM 2629 C CA . ARG A 1 344 ? -39.652 -21.027 33.012 1.00 24.17 ? 344 ARG A CA 1 ATOM 2630 C C . ARG A 1 344 ? -38.670 -22.179 32.829 1.00 24.80 ? 344 ARG A C 1 ATOM 2631 O O . ARG A 1 344 ? -37.585 -22.166 33.409 1.00 26.41 ? 344 ARG A O 1 ATOM 2632 C CB . ARG A 1 344 ? -39.273 -19.880 32.055 1.00 24.02 ? 344 ARG A CB 1 ATOM 2633 C CG . ARG A 1 344 ? -40.259 -18.707 31.962 1.00 24.91 ? 344 ARG A CG 1 ATOM 2634 C CD . ARG A 1 344 ? -41.636 -19.131 31.449 1.00 24.64 ? 344 ARG A CD 1 ATOM 2635 N NE . ARG A 1 344 ? -42.526 -17.987 31.252 1.00 23.71 ? 344 ARG A NE 1 ATOM 2636 C CZ . ARG A 1 344 ? -43.511 -17.633 32.073 1.00 23.79 ? 344 ARG A CZ 1 ATOM 2637 N NH1 . ARG A 1 344 ? -43.769 -18.325 33.178 1.00 22.16 ? 344 ARG A NH1 1 ATOM 2638 N NH2 . ARG A 1 344 ? -44.237 -16.565 31.790 1.00 26.02 ? 344 ARG A NH2 1 ATOM 2639 N N . SER A 1 345 ? -39.068 -23.189 32.063 1.00 26.53 ? 345 SER A N 1 ATOM 2640 C CA . SER A 1 345 ? -38.215 -24.345 31.804 1.00 27.80 ? 345 SER A CA 1 ATOM 2641 C C . SER A 1 345 ? -38.065 -24.591 30.308 1.00 27.79 ? 345 SER A C 1 ATOM 2642 O O . SER A 1 345 ? -39.049 -24.540 29.559 1.00 26.26 ? 345 SER A O 1 ATOM 2643 C CB . SER A 1 345 ? -38.753 -25.593 32.510 1.00 29.58 ? 345 SER A CB 1 ATOM 2644 O OG . SER A 1 345 ? -38.632 -25.469 33.919 1.00 31.67 ? 345 SER A OG 1 ATOM 2645 N N . VAL A 1 346 ? -36.815 -24.791 29.880 1.00 27.47 ? 346 VAL A N 1 ATOM 2646 C CA . VAL A 1 346 ? -36.472 -25.034 28.473 1.00 27.99 ? 346 VAL A CA 1 ATOM 2647 C C . VAL A 1 346 ? -35.413 -26.113 28.268 1.00 27.34 ? 346 VAL A C 1 ATOM 2648 O O . VAL A 1 346 ? -34.473 -26.227 29.066 1.00 28.10 ? 346 VAL A O 1 ATOM 2649 C CB . VAL A 1 346 ? -35.934 -23.746 27.744 1.00 29.32 ? 346 VAL A CB 1 ATOM 2650 C CG1 . VAL A 1 346 ? -37.042 -22.787 27.476 1.00 27.54 ? 346 VAL A CG1 1 ATOM 2651 C CG2 . VAL A 1 346 ? -34.824 -23.076 28.534 1.00 29.02 ? 346 VAL A CG2 1 ATOM 2652 N N . PRO A 1 347 ? -35.565 -26.943 27.212 1.00 27.66 ? 347 PRO A N 1 ATOM 2653 C CA . PRO A 1 347 ? -34.547 -27.977 26.983 1.00 27.65 ? 347 PRO A CA 1 ATOM 2654 C C . PRO A 1 347 ? -33.292 -27.319 26.385 1.00 27.28 ? 347 PRO A C 1 ATOM 2655 O O . PRO A 1 347 ? -33.389 -26.577 25.400 1.00 26.50 ? 347 PRO A O 1 ATOM 2656 C CB . PRO A 1 347 ? -35.216 -28.902 25.955 1.00 27.61 ? 347 PRO A CB 1 ATOM 2657 C CG . PRO A 1 347 ? -36.681 -28.691 26.167 1.00 27.59 ? 347 PRO A CG 1 ATOM 2658 C CD . PRO A 1 347 ? -36.762 -27.210 26.380 1.00 27.80 ? 347 PRO A CD 1 ATOM 2659 N N . VAL A 1 348 ? -32.149 -27.515 27.043 1.00 26.80 ? 348 VAL A N 1 ATOM 2660 C CA . VAL A 1 348 ? -30.873 -26.969 26.571 1.00 26.28 ? 348 VAL A CA 1 ATOM 2661 C C . VAL A 1 348 ? -29.975 -28.033 25.953 1.00 26.31 ? 348 VAL A C 1 ATOM 2662 O O . VAL A 1 348 ? -28.995 -27.709 25.281 1.00 26.06 ? 348 VAL A O 1 ATOM 2663 C CB . VAL A 1 348 ? -30.088 -26.212 27.679 1.00 26.26 ? 348 VAL A CB 1 ATOM 2664 C CG1 . VAL A 1 348 ? -30.740 -24.872 27.961 1.00 26.10 ? 348 VAL A CG1 1 ATOM 2665 C CG2 . VAL A 1 348 ? -29.954 -27.054 28.957 1.00 26.34 ? 348 VAL A CG2 1 ATOM 2666 N N . ASN A 1 349 ? -30.322 -29.298 26.192 1.00 27.05 ? 349 ASN A N 1 ATOM 2667 C CA . ASN A 1 349 ? -29.579 -30.450 25.675 1.00 28.37 ? 349 ASN A CA 1 ATOM 2668 C C . ASN A 1 349 ? -29.806 -30.663 24.170 1.00 28.50 ? 349 ASN A C 1 ATOM 2669 O O . ASN A 1 349 ? -28.932 -31.167 23.463 1.00 28.81 ? 349 ASN A O 1 ATOM 2670 C CB . ASN A 1 349 ? -29.956 -31.718 26.467 1.00 29.22 ? 349 ASN A CB 1 ATOM 2671 C CG . ASN A 1 349 ? -31.462 -32.042 26.418 1.00 30.59 ? 349 ASN A CG 1 ATOM 2672 O OD1 . ASN A 1 349 ? -32.235 -31.597 27.269 1.00 31.73 ? 349 ASN A OD1 1 ATOM 2673 N ND2 . ASN A 1 349 ? -31.869 -32.829 25.422 1.00 28.92 ? 349 ASN A ND2 1 ATOM 2674 N N . SER A 1 350 ? -30.969 -30.209 23.703 1.00 28.11 ? 350 SER A N 1 ATOM 2675 C CA . SER A 1 350 ? -31.406 -30.331 22.315 1.00 28.58 ? 350 SER A CA 1 ATOM 2676 C C . SER A 1 350 ? -30.821 -29.286 21.359 1.00 27.56 ? 350 SER A C 1 ATOM 2677 O O . SER A 1 350 ? -31.055 -29.360 20.145 1.00 26.81 ? 350 SER A O 1 ATOM 2678 C CB . SER A 1 350 ? -32.941 -30.277 22.258 1.00 29.92 ? 350 SER A CB 1 ATOM 2679 O OG . SER A 1 350 ? -33.533 -31.137 23.223 1.00 31.53 ? 350 SER A OG 1 ATOM 2680 N N . PHE A 1 351 ? -30.043 -28.342 21.898 1.00 26.93 ? 351 PHE A N 1 ATOM 2681 C CA . PHE A 1 351 ? -29.443 -27.282 21.089 1.00 27.29 ? 351 PHE A CA 1 ATOM 2682 C C . PHE A 1 351 ? -28.341 -27.702 20.098 1.00 28.30 ? 351 PHE A C 1 ATOM 2683 O O . PHE A 1 351 ? -27.350 -28.350 20.457 1.00 26.80 ? 351 PHE A O 1 ATOM 2684 C CB . PHE A 1 351 ? -28.969 -26.101 21.963 1.00 25.72 ? 351 PHE A CB 1 ATOM 2685 C CG . PHE A 1 351 ? -28.474 -24.910 21.158 1.00 25.90 ? 351 PHE A CG 1 ATOM 2686 C CD1 . PHE A 1 351 ? -29.371 -24.144 20.387 1.00 25.50 ? 351 PHE A CD1 1 ATOM 2687 C CD2 . PHE A 1 351 ? -27.096 -24.617 21.081 1.00 24.17 ? 351 PHE A CD2 1 ATOM 2688 C CE1 . PHE A 1 351 ? -28.906 -23.109 19.533 1.00 25.81 ? 351 PHE A CE1 1 ATOM 2689 C CE2 . PHE A 1 351 ? -26.615 -23.589 20.238 1.00 24.52 ? 351 PHE A CE2 1 ATOM 2690 C CZ . PHE A 1 351 ? -27.524 -22.833 19.457 1.00 25.00 ? 351 PHE A CZ 1 ATOM 2691 N N . VAL A 1 352 ? -28.547 -27.291 18.847 1.00 30.25 ? 352 VAL A N 1 ATOM 2692 C CA . VAL A 1 352 ? -27.624 -27.545 17.740 1.00 32.71 ? 352 VAL A CA 1 ATOM 2693 C C . VAL A 1 352 ? -27.364 -26.190 17.059 1.00 33.61 ? 352 VAL A C 1 ATOM 2694 O O . VAL A 1 352 ? -28.309 -25.456 16.746 1.00 32.40 ? 352 VAL A O 1 ATOM 2695 C CB . VAL A 1 352 ? -28.217 -28.549 16.679 1.00 33.20 ? 352 VAL A CB 1 ATOM 2696 C CG1 . VAL A 1 352 ? -27.169 -28.903 15.625 1.00 33.01 ? 352 VAL A CG1 1 ATOM 2697 C CG2 . VAL A 1 352 ? -28.723 -29.835 17.343 1.00 34.06 ? 352 VAL A CG2 1 ATOM 2698 N N . LYS A 1 353 ? -26.080 -25.870 16.861 1.00 35.45 ? 353 LYS A N 1 ATOM 2699 C CA . LYS A 1 353 ? -25.635 -24.632 16.209 1.00 37.16 ? 353 LYS A CA 1 ATOM 2700 C C . LYS A 1 353 ? -25.839 -24.740 14.694 1.00 37.38 ? 353 LYS A C 1 ATOM 2701 O O . LYS A 1 353 ? -25.100 -25.440 13.997 1.00 38.24 ? 353 LYS A O 1 ATOM 2702 C CB . LYS A 1 353 ? -24.152 -24.357 16.530 1.00 38.29 ? 353 LYS A CB 1 ATOM 2703 C CG . LYS A 1 353 ? -23.556 -23.121 15.842 1.00 39.20 ? 353 LYS A CG 1 ATOM 2704 C CD . LYS A 1 353 ? -22.051 -23.029 16.016 1.00 41.51 ? 353 LYS A CD 1 ATOM 2705 C CE . LYS A 1 353 ? -21.496 -21.850 15.230 1.00 43.02 ? 353 LYS A CE 1 ATOM 2706 N NZ . LYS A 1 353 ? -20.018 -21.711 15.372 1.00 46.03 ? 353 LYS A NZ 1 ATOM 2707 N N . ARG A 1 354 ? -26.881 -24.073 14.213 1.00 38.32 ? 354 ARG A N 1 ATOM 2708 C CA . ARG A 1 354 ? -27.237 -24.053 12.794 1.00 39.58 ? 354 ARG A CA 1 ATOM 2709 C C . ARG A 1 354 ? -27.200 -22.593 12.314 1.00 38.50 ? 354 ARG A C 1 ATOM 2710 O O . ARG A 1 354 ? -27.405 -21.687 13.120 1.00 38.07 ? 354 ARG A O 1 ATOM 2711 C CB . ARG A 1 354 ? -28.645 -24.645 12.601 1.00 40.99 ? 354 ARG A CB 1 ATOM 2712 C CG . ARG A 1 354 ? -28.755 -26.153 12.845 1.00 43.85 ? 354 ARG A CG 1 ATOM 2713 C CD . ARG A 1 354 ? -30.186 -26.654 12.662 1.00 46.88 ? 354 ARG A CD 1 ATOM 2714 N NE . ARG A 1 354 ? -31.110 -26.051 13.624 1.00 49.60 ? 354 ARG A NE 1 ATOM 2715 C CZ . ARG A 1 354 ? -32.423 -25.914 13.441 1.00 50.64 ? 354 ARG A CZ 1 ATOM 2716 N NH1 . ARG A 1 354 ? -33.005 -26.337 12.322 1.00 50.92 ? 354 ARG A NH1 1 ATOM 2717 N NH2 . ARG A 1 354 ? -33.161 -25.350 14.388 1.00 50.49 ? 354 ARG A NH2 1 ATOM 2718 N N . PRO A 1 355 ? -26.889 -22.339 11.017 1.00 37.68 ? 355 PRO A N 1 ATOM 2719 C CA . PRO A 1 355 ? -26.845 -20.960 10.506 1.00 36.34 ? 355 PRO A CA 1 ATOM 2720 C C . PRO A 1 355 ? -28.097 -20.094 10.729 1.00 33.88 ? 355 PRO A C 1 ATOM 2721 O O . PRO A 1 355 ? -27.976 -18.881 10.933 1.00 34.48 ? 355 PRO A O 1 ATOM 2722 C CB . PRO A 1 355 ? -26.558 -21.167 9.018 1.00 36.10 ? 355 PRO A CB 1 ATOM 2723 C CG . PRO A 1 355 ? -25.635 -22.310 9.040 1.00 35.60 ? 355 PRO A CG 1 ATOM 2724 C CD . PRO A 1 355 ? -26.316 -23.258 10.007 1.00 37.28 ? 355 PRO A CD 1 ATOM 2725 N N . ASP A 1 356 ? -29.276 -20.722 10.763 1.00 31.48 ? 356 ASP A N 1 ATOM 2726 C CA . ASP A 1 356 ? -30.530 -19.984 10.959 1.00 29.08 ? 356 ASP A CA 1 ATOM 2727 C C . ASP A 1 356 ? -30.860 -19.627 12.412 1.00 26.79 ? 356 ASP A C 1 ATOM 2728 O O . ASP A 1 356 ? -31.914 -19.044 12.687 1.00 26.58 ? 356 ASP A O 1 ATOM 2729 C CB . ASP A 1 356 ? -31.723 -20.647 10.219 1.00 29.60 ? 356 ASP A CB 1 ATOM 2730 C CG . ASP A 1 356 ? -32.148 -21.995 10.808 1.00 30.86 ? 356 ASP A CG 1 ATOM 2731 O OD1 . ASP A 1 356 ? -31.358 -22.635 11.530 1.00 32.87 ? 356 ASP A OD1 1 ATOM 2732 O OD2 . ASP A 1 356 ? -33.295 -22.418 10.531 1.00 32.20 ? 356 ASP A OD2 1 ATOM 2733 N N . ASN A 1 357 ? -29.966 -20.011 13.329 1.00 24.16 ? 357 ASN A N 1 ATOM 2734 C CA . ASN A 1 357 ? -30.101 -19.690 14.751 1.00 21.75 ? 357 ASN A CA 1 ATOM 2735 C C . ASN A 1 357 ? -28.848 -18.969 15.274 1.00 19.57 ? 357 ASN A C 1 ATOM 2736 O O . ASN A 1 357 ? -28.785 -18.551 16.434 1.00 16.83 ? 357 ASN A O 1 ATOM 2737 C CB . ASN A 1 357 ? -30.489 -20.928 15.610 1.00 23.69 ? 357 ASN A CB 1 ATOM 2738 C CG . ASN A 1 357 ? -29.418 -22.042 15.648 1.00 26.13 ? 357 ASN A CG 1 ATOM 2739 O OD1 . ASN A 1 357 ? -28.208 -21.790 15.699 1.00 26.70 ? 357 ASN A OD1 1 ATOM 2740 N ND2 . ASN A 1 357 ? -29.886 -23.291 15.695 1.00 27.56 ? 357 ASN A ND2 1 ATOM 2741 N N . THR A 1 358 ? -27.870 -18.810 14.383 1.00 17.83 ? 358 THR A N 1 ATOM 2742 C CA . THR A 1 358 ? -26.596 -18.169 14.702 1.00 15.89 ? 358 THR A CA 1 ATOM 2743 C C . THR A 1 358 ? -26.523 -16.730 14.189 1.00 13.71 ? 358 THR A C 1 ATOM 2744 O O . THR A 1 358 ? -26.734 -16.478 12.998 1.00 15.70 ? 358 THR A O 1 ATOM 2745 C CB . THR A 1 358 ? -25.416 -19.023 14.152 1.00 15.95 ? 358 THR A CB 1 ATOM 2746 O OG1 . THR A 1 358 ? -25.518 -20.354 14.676 1.00 14.66 ? 358 THR A OG1 1 ATOM 2747 C CG2 . THR A 1 358 ? -24.065 -18.451 14.568 1.00 17.26 ? 358 THR A CG2 1 ATOM 2748 N N . LEU A 1 359 ? -26.236 -15.794 15.100 1.00 11.47 ? 359 LEU A N 1 ATOM 2749 C CA . LEU A 1 359 ? -26.111 -14.363 14.769 1.00 12.14 ? 359 LEU A CA 1 ATOM 2750 C C . LEU A 1 359 ? -24.683 -13.868 15.059 1.00 12.96 ? 359 LEU A C 1 ATOM 2751 O O . LEU A 1 359 ? -24.378 -13.467 16.184 1.00 11.96 ? 359 LEU A O 1 ATOM 2752 C CB . LEU A 1 359 ? -27.137 -13.501 15.540 1.00 8.82 ? 359 LEU A CB 1 ATOM 2753 C CG . LEU A 1 359 ? -28.653 -13.712 15.374 1.00 7.24 ? 359 LEU A CG 1 ATOM 2754 C CD1 . LEU A 1 359 ? -29.378 -12.793 16.333 1.00 5.14 ? 359 LEU A CD1 1 ATOM 2755 C CD2 . LEU A 1 359 ? -29.125 -13.460 13.926 1.00 3.58 ? 359 LEU A CD2 1 ATOM 2756 N N . PRO A 1 360 ? -23.783 -13.909 14.043 1.00 14.86 ? 360 PRO A N 1 ATOM 2757 C CA . PRO A 1 360 ? -22.387 -13.466 14.187 1.00 15.91 ? 360 PRO A CA 1 ATOM 2758 C C . PRO A 1 360 ? -22.230 -11.948 14.135 1.00 16.71 ? 360 PRO A C 1 ATOM 2759 O O . PRO A 1 360 ? -22.647 -11.312 13.172 1.00 18.87 ? 360 PRO A O 1 ATOM 2760 C CB . PRO A 1 360 ? -21.691 -14.101 12.977 1.00 15.15 ? 360 PRO A CB 1 ATOM 2761 C CG . PRO A 1 360 ? -22.626 -15.172 12.519 1.00 14.96 ? 360 PRO A CG 1 ATOM 2762 C CD . PRO A 1 360 ? -23.960 -14.544 12.727 1.00 12.69 ? 360 PRO A CD 1 ATOM 2763 N N . VAL A 1 361 ? -21.657 -11.385 15.195 1.00 16.30 ? 361 VAL A N 1 ATOM 2764 C CA . VAL A 1 361 ? -21.402 -9.953 15.296 1.00 15.22 ? 361 VAL A CA 1 ATOM 2765 C C . VAL A 1 361 ? -19.973 -9.754 14.805 1.00 16.08 ? 361 VAL A C 1 ATOM 2766 O O . VAL A 1 361 ? -19.052 -10.421 15.263 1.00 15.88 ? 361 VAL A O 1 ATOM 2767 C CB . VAL A 1 361 ? -21.520 -9.449 16.769 1.00 14.47 ? 361 VAL A CB 1 ATOM 2768 C CG1 . VAL A 1 361 ? -21.165 -7.978 16.883 1.00 14.91 ? 361 VAL A CG1 1 ATOM 2769 C CG2 . VAL A 1 361 ? -22.915 -9.678 17.282 1.00 16.90 ? 361 VAL A CG2 1 ATOM 2770 N N . ALA A 1 362 ? -19.807 -8.866 13.837 1.00 17.64 ? 362 ALA A N 1 ATOM 2771 C CA . ALA A 1 362 ? -18.494 -8.572 13.297 1.00 17.53 ? 362 ALA A CA 1 ATOM 2772 C C . ALA A 1 362 ? -18.317 -7.085 13.082 1.00 17.84 ? 362 ALA A C 1 ATOM 2773 O O . ALA A 1 362 ? -19.276 -6.353 12.823 1.00 18.40 ? 362 ALA A O 1 ATOM 2774 C CB . ALA A 1 362 ? -18.268 -9.328 11.990 1.00 17.85 ? 362 ALA A CB 1 ATOM 2775 N N . LEU A 1 363 ? -17.086 -6.633 13.262 1.00 17.19 ? 363 LEU A N 1 ATOM 2776 C CA . LEU A 1 363 ? -16.752 -5.249 13.042 1.00 15.46 ? 363 LEU A CA 1 ATOM 2777 C C . LEU A 1 363 ? -16.021 -5.215 11.704 1.00 16.92 ? 363 LEU A C 1 ATOM 2778 O O . LEU A 1 363 ? -15.039 -5.931 11.510 1.00 16.66 ? 363 LEU A O 1 ATOM 2779 C CB . LEU A 1 363 ? -15.863 -4.735 14.170 1.00 13.61 ? 363 LEU A CB 1 ATOM 2780 C CG . LEU A 1 363 ? -15.338 -3.298 14.080 1.00 13.72 ? 363 LEU A CG 1 ATOM 2781 C CD1 . LEU A 1 363 ? -16.458 -2.281 13.972 1.00 12.92 ? 363 LEU A CD1 1 ATOM 2782 C CD2 . LEU A 1 363 ? -14.506 -3.021 15.281 1.00 8.86 ? 363 LEU A CD2 1 ATOM 2783 N N . ASP A 1 364 ? -16.555 -4.443 10.764 1.00 18.51 ? 364 ASP A N 1 ATOM 2784 C CA . ASP A 1 364 ? -15.946 -4.304 9.446 1.00 20.90 ? 364 ASP A CA 1 ATOM 2785 C C . ASP A 1 364 ? -15.079 -3.036 9.480 1.00 21.88 ? 364 ASP A C 1 ATOM 2786 O O . ASP A 1 364 ? -15.550 -1.962 9.864 1.00 21.91 ? 364 ASP A O 1 ATOM 2787 C CB . ASP A 1 364 ? -17.040 -4.211 8.374 1.00 22.12 ? 364 ASP A CB 1 ATOM 2788 C CG . ASP A 1 364 ? -16.536 -4.543 6.970 1.00 24.34 ? 364 ASP A CG 1 ATOM 2789 O OD1 . ASP A 1 364 ? -15.340 -4.321 6.679 1.00 25.18 ? 364 ASP A OD1 1 ATOM 2790 O OD2 . ASP A 1 364 ? -17.357 -5.013 6.146 1.00 25.29 ? 364 ASP A OD2 1 ATOM 2791 N N . LEU A 1 365 ? -13.802 -3.195 9.130 1.00 24.05 ? 365 LEU A N 1 ATOM 2792 C CA . LEU A 1 365 ? -12.822 -2.104 9.123 1.00 25.56 ? 365 LEU A CA 1 ATOM 2793 C C . LEU A 1 365 ? -12.281 -1.799 7.731 1.00 27.31 ? 365 LEU A C 1 ATOM 2794 O O . LEU A 1 365 ? -11.324 -1.025 7.597 1.00 29.19 ? 365 LEU A O 1 ATOM 2795 C CB . LEU A 1 365 ? -11.630 -2.468 10.019 1.00 25.91 ? 365 LEU A CB 1 ATOM 2796 C CG . LEU A 1 365 ? -11.792 -2.782 11.504 1.00 27.15 ? 365 LEU A CG 1 ATOM 2797 C CD1 . LEU A 1 365 ? -10.476 -3.314 12.048 1.00 27.25 ? 365 LEU A CD1 1 ATOM 2798 C CD2 . LEU A 1 365 ? -12.229 -1.540 12.259 1.00 27.08 ? 365 LEU A CD2 1 ATOM 2799 N N . THR A 1 366 ? -12.869 -2.414 6.704 1.00 28.63 ? 366 THR A N 1 ATOM 2800 C CA . THR A 1 366 ? -12.412 -2.228 5.325 1.00 29.88 ? 366 THR A CA 1 ATOM 2801 C C . THR A 1 366 ? -13.027 -1.056 4.559 1.00 30.80 ? 366 THR A C 1 ATOM 2802 O O . THR A 1 366 ? -12.376 -0.489 3.678 1.00 32.73 ? 366 THR A O 1 ATOM 2803 C CB . THR A 1 366 ? -12.549 -3.532 4.487 1.00 30.14 ? 366 THR A CB 1 ATOM 2804 O OG1 . THR A 1 366 ? -13.926 -3.919 4.389 1.00 29.70 ? 366 THR A OG1 1 ATOM 2805 C CG2 . THR A 1 366 ? -11.748 -4.665 5.125 1.00 30.40 ? 366 THR A CG2 1 ATOM 2806 N N . GLY A 1 367 ? -14.259 -0.683 4.909 1.00 30.39 ? 367 GLY A N 1 ATOM 2807 C CA . GLY A 1 367 ? -14.936 0.415 4.232 1.00 30.68 ? 367 GLY A CA 1 ATOM 2808 C C . GLY A 1 367 ? -14.876 1.777 4.908 1.00 31.34 ? 367 GLY A C 1 ATOM 2809 O O . GLY A 1 367 ? -14.004 2.037 5.745 1.00 31.39 ? 367 GLY A O 1 ATOM 2810 N N . THR A 1 368 ? -15.772 2.662 4.473 1.00 30.94 ? 368 THR A N 1 ATOM 2811 C CA . THR A 1 368 ? -15.915 4.020 5.003 1.00 31.05 ? 368 THR A CA 1 ATOM 2812 C C . THR A 1 368 ? -17.353 4.142 5.538 1.00 28.44 ? 368 THR A C 1 ATOM 2813 O O . THR A 1 368 ? -18.301 3.854 4.798 1.00 29.57 ? 368 THR A O 1 ATOM 2814 C CB . THR A 1 368 ? -15.658 5.123 3.924 1.00 34.33 ? 368 THR A CB 1 ATOM 2815 O OG1 . THR A 1 368 ? -16.344 4.793 2.706 1.00 39.06 ? 368 THR A OG1 1 ATOM 2816 C CG2 . THR A 1 368 ? -14.158 5.300 3.662 1.00 35.16 ? 368 THR A CG2 1 ATOM 2817 N N . PRO A 1 369 ? -17.540 4.502 6.836 1.00 26.26 ? 369 PRO A N 1 ATOM 2818 C CA . PRO A 1 369 ? -16.574 4.814 7.905 1.00 23.88 ? 369 PRO A CA 1 ATOM 2819 C C . PRO A 1 369 ? -15.856 3.594 8.488 1.00 22.11 ? 369 PRO A C 1 ATOM 2820 O O . PRO A 1 369 ? -16.172 2.459 8.138 1.00 20.28 ? 369 PRO A O 1 ATOM 2821 C CB . PRO A 1 369 ? -17.441 5.519 8.942 1.00 24.73 ? 369 PRO A CB 1 ATOM 2822 C CG . PRO A 1 369 ? -18.766 4.860 8.789 1.00 24.82 ? 369 PRO A CG 1 ATOM 2823 C CD . PRO A 1 369 ? -18.915 4.792 7.295 1.00 25.29 ? 369 PRO A CD 1 ATOM 2824 N N . LEU A 1 370 ? -14.864 3.839 9.338 1.00 22.01 ? 370 LEU A N 1 ATOM 2825 C CA . LEU A 1 370 ? -14.085 2.766 9.945 1.00 20.49 ? 370 LEU A CA 1 ATOM 2826 C C . LEU A 1 370 ? -14.882 1.819 10.842 1.00 19.59 ? 370 LEU A C 1 ATOM 2827 O O . LEU A 1 370 ? -14.809 0.602 10.671 1.00 19.74 ? 370 LEU A O 1 ATOM 2828 C CB . LEU A 1 370 ? -12.902 3.348 10.711 1.00 21.05 ? 370 LEU A CB 1 ATOM 2829 C CG . LEU A 1 370 ? -11.786 2.393 11.132 1.00 20.83 ? 370 LEU A CG 1 ATOM 2830 C CD1 . LEU A 1 370 ? -11.056 1.787 9.931 1.00 22.41 ? 370 LEU A CD1 1 ATOM 2831 C CD2 . LEU A 1 370 ? -10.838 3.171 11.960 1.00 21.94 ? 370 LEU A CD2 1 ATOM 2832 N N . PHE A 1 371 ? -15.669 2.376 11.759 1.00 17.49 ? 371 PHE A N 1 ATOM 2833 C CA . PHE A 1 371 ? -16.462 1.559 12.670 1.00 17.48 ? 371 PHE A CA 1 ATOM 2834 C C . PHE A 1 371 ? -17.888 1.326 12.192 1.00 17.14 ? 371 PHE A C 1 ATOM 2835 O O . PHE A 1 371 ? -18.772 2.177 12.311 1.00 18.70 ? 371 PHE A O 1 ATOM 2836 C CB . PHE A 1 371 ? -16.380 2.104 14.104 1.00 17.71 ? 371 PHE A CB 1 ATOM 2837 C CG . PHE A 1 371 ? -14.979 2.122 14.649 1.00 20.26 ? 371 PHE A CG 1 ATOM 2838 C CD1 . PHE A 1 371 ? -14.233 0.926 14.743 1.00 23.29 ? 371 PHE A CD1 1 ATOM 2839 C CD2 . PHE A 1 371 ? -14.354 3.332 14.982 1.00 20.58 ? 371 PHE A CD2 1 ATOM 2840 C CE1 . PHE A 1 371 ? -12.869 0.939 15.156 1.00 25.32 ? 371 PHE A CE1 1 ATOM 2841 C CE2 . PHE A 1 371 ? -12.995 3.361 15.395 1.00 21.65 ? 371 PHE A CE2 1 ATOM 2842 C CZ . PHE A 1 371 ? -12.250 2.164 15.481 1.00 24.41 ? 371 PHE A CZ 1 ATOM 2843 N N . VAL A 1 372 ? -18.044 0.182 11.538 1.00 16.28 ? 372 VAL A N 1 ATOM 2844 C CA . VAL A 1 372 ? -19.302 -0.286 10.972 1.00 15.99 ? 372 VAL A CA 1 ATOM 2845 C C . VAL A 1 372 ? -19.522 -1.657 11.607 1.00 15.68 ? 372 VAL A C 1 ATOM 2846 O O . VAL A 1 372 ? -18.710 -2.572 11.416 1.00 17.50 ? 372 VAL A O 1 ATOM 2847 C CB . VAL A 1 372 ? -19.191 -0.404 9.400 1.00 17.05 ? 372 VAL A CB 1 ATOM 2848 C CG1 . VAL A 1 372 ? -20.397 -1.101 8.804 1.00 11.90 ? 372 VAL A CG1 1 ATOM 2849 C CG2 . VAL A 1 372 ? -19.033 0.977 8.768 1.00 11.48 ? 372 VAL A CG2 1 ATOM 2850 N N . TRP A 1 373 ? -20.598 -1.774 12.383 1.00 13.99 ? 373 TRP A N 1 ATOM 2851 C CA . TRP A 1 373 ? -20.943 -3.017 13.071 1.00 13.76 ? 373 TRP A CA 1 ATOM 2852 C C . TRP A 1 373 ? -21.915 -3.888 12.277 1.00 13.37 ? 373 TRP A C 1 ATOM 2853 O O . TRP A 1 373 ? -23.021 -3.465 11.967 1.00 14.52 ? 373 TRP A O 1 ATOM 2854 C CB . TRP A 1 373 ? -21.493 -2.706 14.460 1.00 12.89 ? 373 TRP A CB 1 ATOM 2855 C CG . TRP A 1 373 ? -20.465 -2.146 15.377 1.00 11.91 ? 373 TRP A CG 1 ATOM 2856 C CD1 . TRP A 1 373 ? -20.223 -0.828 15.620 1.00 12.12 ? 373 TRP A CD1 1 ATOM 2857 C CD2 . TRP A 1 373 ? -19.498 -2.884 16.140 1.00 11.30 ? 373 TRP A CD2 1 ATOM 2858 N NE1 . TRP A 1 373 ? -19.162 -0.689 16.477 1.00 13.57 ? 373 TRP A NE1 1 ATOM 2859 C CE2 . TRP A 1 373 ? -18.693 -1.932 16.817 1.00 12.11 ? 373 TRP A CE2 1 ATOM 2860 C CE3 . TRP A 1 373 ? -19.227 -4.261 16.318 1.00 10.78 ? 373 TRP A CE3 1 ATOM 2861 C CZ2 . TRP A 1 373 ? -17.621 -2.307 17.668 1.00 10.77 ? 373 TRP A CZ2 1 ATOM 2862 C CZ3 . TRP A 1 373 ? -18.159 -4.642 17.169 1.00 10.28 ? 373 TRP A CZ3 1 ATOM 2863 C CH2 . TRP A 1 373 ? -17.372 -3.659 17.830 1.00 10.78 ? 373 TRP A CH2 1 ATOM 2864 N N . LYS A 1 374 ? -21.495 -5.113 11.967 1.00 11.85 ? 374 LYS A N 1 ATOM 2865 C CA . LYS A 1 374 ? -22.298 -6.024 11.163 1.00 11.33 ? 374 LYS A CA 1 ATOM 2866 C C . LYS A 1 374 ? -22.781 -7.272 11.874 1.00 10.70 ? 374 LYS A C 1 ATOM 2867 O O . LYS A 1 374 ? -22.042 -7.879 12.634 1.00 12.26 ? 374 LYS A O 1 ATOM 2868 C CB . LYS A 1 374 ? -21.525 -6.430 9.894 1.00 12.54 ? 374 LYS A CB 1 ATOM 2869 C CG . LYS A 1 374 ? -21.148 -5.275 8.971 1.00 12.19 ? 374 LYS A CG 1 ATOM 2870 C CD . LYS A 1 374 ? -20.745 -5.749 7.587 1.00 16.74 ? 374 LYS A CD 1 ATOM 2871 C CE . LYS A 1 374 ? -20.738 -4.586 6.594 1.00 17.67 ? 374 LYS A CE 1 ATOM 2872 N NZ . LYS A 1 374 ? -20.595 -5.029 5.172 1.00 19.79 ? 374 LYS A NZ 1 ATOM 2873 N N . VAL A 1 375 ? -24.048 -7.616 11.671 1.00 9.86 ? 375 VAL A N 1 ATOM 2874 C CA . VAL A 1 375 ? -24.603 -8.825 12.267 1.00 11.22 ? 375 VAL A CA 1 ATOM 2875 C C . VAL A 1 375 ? -25.041 -9.710 11.109 1.00 12.92 ? 375 VAL A C 1 ATOM 2876 O O . VAL A 1 375 ? -25.964 -9.359 10.366 1.00 12.37 ? 375 VAL A O 1 ATOM 2877 C CB . VAL A 1 375 ? -25.791 -8.574 13.248 1.00 9.98 ? 375 VAL A CB 1 ATOM 2878 C CG1 . VAL A 1 375 ? -26.061 -9.849 14.057 1.00 7.98 ? 375 VAL A CG1 1 ATOM 2879 C CG2 . VAL A 1 375 ? -25.494 -7.429 14.202 1.00 6.86 ? 375 VAL A CG2 1 ATOM 2880 N N . ASN A 1 376 ? -24.343 -10.845 10.965 1.00 13.62 ? 376 ASN A N 1 ATOM 2881 C CA . ASN A 1 376 ? -24.543 -11.844 9.899 1.00 17.58 ? 376 ASN A CA 1 ATOM 2882 C C . ASN A 1 376 ? -24.165 -11.272 8.516 1.00 16.30 ? 376 ASN A C 1 ATOM 2883 O O . ASN A 1 376 ? -24.857 -11.479 7.517 1.00 17.56 ? 376 ASN A O 1 ATOM 2884 C CB . ASN A 1 376 ? -25.971 -12.449 9.925 1.00 21.31 ? 376 ASN A CB 1 ATOM 2885 C CG . ASN A 1 376 ? -26.011 -13.904 9.441 1.00 26.26 ? 376 ASN A CG 1 ATOM 2886 O OD1 . ASN A 1 376 ? -25.020 -14.639 9.561 1.00 28.00 ? 376 ASN A OD1 1 ATOM 2887 N ND2 . ASN A 1 376 ? -27.157 -14.325 8.908 1.00 27.29 ? 376 ASN A ND2 1 ATOM 2888 N N . GLY A 1 377 ? -23.056 -10.531 8.504 1.00 15.58 ? 377 GLY A N 1 ATOM 2889 C CA . GLY A 1 377 ? -22.532 -9.911 7.298 1.00 15.64 ? 377 GLY A CA 1 ATOM 2890 C C . GLY A 1 377 ? -23.233 -8.644 6.841 1.00 15.18 ? 377 GLY A C 1 ATOM 2891 O O . GLY A 1 377 ? -22.950 -8.153 5.744 1.00 15.77 ? 377 GLY A O 1 ATOM 2892 N N . SER A 1 378 ? -24.110 -8.094 7.683 1.00 13.57 ? 378 SER A N 1 ATOM 2893 C CA . SER A 1 378 ? -24.865 -6.894 7.330 1.00 12.35 ? 378 SER A CA 1 ATOM 2894 C C . SER A 1 378 ? -25.094 -5.912 8.472 1.00 12.50 ? 378 SER A C 1 ATOM 2895 O O . SER A 1 378 ? -25.513 -6.301 9.567 1.00 12.62 ? 378 SER A O 1 ATOM 2896 C CB . SER A 1 378 ? -26.216 -7.297 6.728 1.00 12.97 ? 378 SER A CB 1 ATOM 2897 O OG . SER A 1 378 ? -27.106 -6.200 6.608 1.00 13.02 ? 378 SER A OG 1 ATOM 2898 N N . ASP A 1 379 ? -24.793 -4.641 8.198 1.00 12.63 ? 379 ASP A N 1 ATOM 2899 C CA . ASP A 1 379 ? -24.994 -3.538 9.140 1.00 12.87 ? 379 ASP A CA 1 ATOM 2900 C C . ASP A 1 379 ? -26.382 -2.973 8.877 1.00 13.47 ? 379 ASP A C 1 ATOM 2901 O O . ASP A 1 379 ? -26.700 -2.621 7.733 1.00 11.80 ? 379 ASP A O 1 ATOM 2902 C CB . ASP A 1 379 ? -23.910 -2.445 9.003 1.00 12.00 ? 379 ASP A CB 1 ATOM 2903 C CG . ASP A 1 379 ? -23.717 -1.942 7.560 1.00 15.15 ? 379 ASP A CG 1 ATOM 2904 O OD1 . ASP A 1 379 ? -23.569 -2.767 6.627 1.00 15.55 ? 379 ASP A OD1 1 ATOM 2905 O OD2 . ASP A 1 379 ? -23.688 -0.707 7.371 1.00 13.56 ? 379 ASP A OD2 1 ATOM 2906 N N . ILE A 1 380 ? -27.212 -2.933 9.922 1.00 13.68 ? 380 ILE A N 1 ATOM 2907 C CA . ILE A 1 380 ? -28.586 -2.448 9.805 1.00 18.14 ? 380 ILE A CA 1 ATOM 2908 C C . ILE A 1 380 ? -28.719 -0.983 9.353 1.00 20.37 ? 380 ILE A C 1 ATOM 2909 O O . ILE A 1 380 ? -27.866 -0.145 9.662 1.00 23.26 ? 380 ILE A O 1 ATOM 2910 C CB . ILE A 1 380 ? -29.416 -2.713 11.121 1.00 17.77 ? 380 ILE A CB 1 ATOM 2911 C CG1 . ILE A 1 380 ? -30.882 -3.020 10.766 1.00 13.80 ? 380 ILE A CG1 1 ATOM 2912 C CG2 . ILE A 1 380 ? -29.306 -1.515 12.106 1.00 17.39 ? 380 ILE A CG2 1 ATOM 2913 C CD1 . ILE A 1 380 ? -31.750 -3.531 11.913 1.00 12.77 ? 380 ILE A CD1 1 ATOM 2914 N N . ASN A 1 381 ? -29.759 -0.726 8.564 1.00 22.65 ? 381 ASN A N 1 ATOM 2915 C CA . ASN A 1 381 ? -30.078 0.600 8.051 1.00 25.07 ? 381 ASN A CA 1 ATOM 2916 C C . ASN A 1 381 ? -31.567 0.596 7.730 1.00 25.03 ? 381 ASN A C 1 ATOM 2917 O O . ASN A 1 381 ? -31.990 0.166 6.649 1.00 24.46 ? 381 ASN A O 1 ATOM 2918 C CB . ASN A 1 381 ? -29.239 0.948 6.806 1.00 27.45 ? 381 ASN A CB 1 ATOM 2919 C CG . ASN A 1 381 ? -29.236 2.431 6.503 1.00 29.24 ? 381 ASN A CG 1 ATOM 2920 O OD1 . ASN A 1 381 ? -30.193 2.964 5.938 1.00 29.28 ? 381 ASN A OD1 1 ATOM 2921 N ND2 . ASN A 1 381 ? -28.155 3.110 6.882 1.00 31.13 ? 381 ASN A ND2 1 ATOM 2922 N N . VAL A 1 382 ? -32.349 1.052 8.708 1.00 25.19 ? 382 VAL A N 1 ATOM 2923 C CA . VAL A 1 382 ? -33.804 1.122 8.603 1.00 24.28 ? 382 VAL A CA 1 ATOM 2924 C C . VAL A 1 382 ? -34.252 2.305 7.754 1.00 23.95 ? 382 VAL A C 1 ATOM 2925 O O . VAL A 1 382 ? -33.541 3.307 7.649 1.00 23.61 ? 382 VAL A O 1 ATOM 2926 C CB . VAL A 1 382 ? -34.478 1.182 10.007 1.00 24.16 ? 382 VAL A CB 1 ATOM 2927 C CG1 . VAL A 1 382 ? -34.105 -0.043 10.824 1.00 24.28 ? 382 VAL A CG1 1 ATOM 2928 C CG2 . VAL A 1 382 ? -34.105 2.464 10.757 1.00 24.96 ? 382 VAL A CG2 1 ATOM 2929 N N . ASP A 1 383 ? -35.421 2.168 7.139 1.00 23.69 ? 383 ASP A N 1 ATOM 2930 C CA . ASP A 1 383 ? -35.975 3.221 6.300 1.00 23.42 ? 383 ASP A CA 1 ATOM 2931 C C . ASP A 1 383 ? -37.052 3.980 7.083 1.00 23.02 ? 383 ASP A C 1 ATOM 2932 O O . ASP A 1 383 ? -38.144 3.462 7.330 1.00 22.20 ? 383 ASP A O 1 ATOM 2933 C CB . ASP A 1 383 ? -36.541 2.617 5.000 1.00 24.97 ? 383 ASP A CB 1 ATOM 2934 C CG . ASP A 1 383 ? -36.800 3.658 3.902 1.00 26.12 ? 383 ASP A CG 1 ATOM 2935 O OD1 . ASP A 1 383 ? -36.872 4.877 4.187 1.00 26.30 ? 383 ASP A OD1 1 ATOM 2936 O OD2 . ASP A 1 383 ? -36.947 3.240 2.733 1.00 28.65 ? 383 ASP A OD2 1 ATOM 2937 N N . TRP A 1 384 ? -36.718 5.214 7.463 1.00 22.36 ? 384 TRP A N 1 ATOM 2938 C CA . TRP A 1 384 ? -37.607 6.120 8.194 1.00 20.66 ? 384 TRP A CA 1 ATOM 2939 C C . TRP A 1 384 ? -38.851 6.461 7.367 1.00 20.24 ? 384 TRP A C 1 ATOM 2940 O O . TRP A 1 384 ? -39.922 6.722 7.924 1.00 18.57 ? 384 TRP A O 1 ATOM 2941 C CB . TRP A 1 384 ? -36.866 7.419 8.531 1.00 21.97 ? 384 TRP A CB 1 ATOM 2942 C CG . TRP A 1 384 ? -35.813 7.341 9.624 1.00 22.14 ? 384 TRP A CG 1 ATOM 2943 C CD1 . TRP A 1 384 ? -35.705 6.400 10.622 1.00 23.03 ? 384 TRP A CD1 1 ATOM 2944 C CD2 . TRP A 1 384 ? -34.763 8.288 9.856 1.00 21.47 ? 384 TRP A CD2 1 ATOM 2945 N NE1 . TRP A 1 384 ? -34.660 6.712 11.462 1.00 20.51 ? 384 TRP A NE1 1 ATOM 2946 C CE2 . TRP A 1 384 ? -34.063 7.862 11.020 1.00 20.74 ? 384 TRP A CE2 1 ATOM 2947 C CE3 . TRP A 1 384 ? -34.341 9.463 9.194 1.00 20.66 ? 384 TRP A CE3 1 ATOM 2948 C CZ2 . TRP A 1 384 ? -32.955 8.574 11.544 1.00 20.12 ? 384 TRP A CZ2 1 ATOM 2949 C CZ3 . TRP A 1 384 ? -33.235 10.176 9.713 1.00 21.21 ? 384 TRP A CZ3 1 ATOM 2950 C CH2 . TRP A 1 384 ? -32.555 9.719 10.883 1.00 19.62 ? 384 TRP A CH2 1 ATOM 2951 N N . GLY A 1 385 ? -38.677 6.437 6.039 1.00 20.88 ? 385 GLY A N 1 ATOM 2952 C CA . GLY A 1 385 ? -39.743 6.712 5.082 1.00 20.60 ? 385 GLY A CA 1 ATOM 2953 C C . GLY A 1 385 ? -40.628 5.514 4.769 1.00 21.44 ? 385 GLY A C 1 ATOM 2954 O O . GLY A 1 385 ? -41.795 5.691 4.411 1.00 22.36 ? 385 GLY A O 1 ATOM 2955 N N . LYS A 1 386 ? -40.073 4.303 4.864 1.00 22.59 ? 386 LYS A N 1 ATOM 2956 C CA . LYS A 1 386 ? -40.831 3.072 4.616 1.00 22.94 ? 386 LYS A CA 1 ATOM 2957 C C . LYS A 1 386 ? -40.480 1.982 5.654 1.00 23.40 ? 386 LYS A C 1 ATOM 2958 O O . LYS A 1 386 ? -39.577 1.158 5.441 1.00 22.36 ? 386 LYS A O 1 ATOM 2959 C CB . LYS A 1 386 ? -40.634 2.566 3.177 1.00 23.62 ? 386 LYS A CB 1 ATOM 2960 C CG . LYS A 1 386 ? -41.731 1.599 2.741 1.00 25.36 ? 386 LYS A CG 1 ATOM 2961 C CD . LYS A 1 386 ? -41.551 1.095 1.326 1.00 27.84 ? 386 LYS A CD 1 ATOM 2962 C CE . LYS A 1 386 ? -42.672 0.122 0.973 1.00 29.12 ? 386 LYS A CE 1 ATOM 2963 N NZ . LYS A 1 386 ? -42.477 -0.526 -0.350 1.00 31.83 ? 386 LYS A NZ 1 ATOM 2964 N N . PRO A 1 387 ? -41.190 1.974 6.805 1.00 23.63 ? 387 PRO A N 1 ATOM 2965 C CA . PRO A 1 387 ? -40.977 1.006 7.892 1.00 22.83 ? 387 PRO A CA 1 ATOM 2966 C C . PRO A 1 387 ? -41.392 -0.415 7.550 1.00 21.46 ? 387 PRO A C 1 ATOM 2967 O O . PRO A 1 387 ? -42.112 -0.631 6.580 1.00 22.26 ? 387 PRO A O 1 ATOM 2968 C CB . PRO A 1 387 ? -41.859 1.553 9.016 1.00 23.63 ? 387 PRO A CB 1 ATOM 2969 C CG . PRO A 1 387 ? -41.962 2.992 8.706 1.00 25.23 ? 387 PRO A CG 1 ATOM 2970 C CD . PRO A 1 387 ? -42.180 2.977 7.230 1.00 24.10 ? 387 PRO A CD 1 ATOM 2971 N N . ILE A 1 388 ? -40.971 -1.367 8.384 1.00 19.63 ? 388 ILE A N 1 ATOM 2972 C CA . ILE A 1 388 ? -41.287 -2.784 8.198 1.00 17.38 ? 388 ILE A CA 1 ATOM 2973 C C . ILE A 1 388 ? -42.792 -3.060 8.274 1.00 18.27 ? 388 ILE A C 1 ATOM 2974 O O . ILE A 1 388 ? -43.311 -3.884 7.512 1.00 18.54 ? 388 ILE A O 1 ATOM 2975 C CB . ILE A 1 388 ? -40.439 -3.679 9.179 1.00 16.08 ? 388 ILE A CB 1 ATOM 2976 C CG1 . ILE A 1 388 ? -38.961 -3.650 8.744 1.00 15.00 ? 388 ILE A CG1 1 ATOM 2977 C CG2 . ILE A 1 388 ? -40.946 -5.141 9.243 1.00 12.26 ? 388 ILE A CG2 1 ATOM 2978 C CD1 . ILE A 1 388 ? -38.702 -4.141 7.314 1.00 10.13 ? 388 ILE A CD1 1 ATOM 2979 N N . ILE A 1 389 ? -43.495 -2.300 9.117 1.00 16.94 ? 389 ILE A N 1 ATOM 2980 C CA . ILE A 1 389 ? -44.938 -2.453 9.262 1.00 16.74 ? 389 ILE A CA 1 ATOM 2981 C C . ILE A 1 389 ? -45.671 -2.061 7.971 1.00 17.31 ? 389 ILE A C 1 ATOM 2982 O O . ILE A 1 389 ? -46.720 -2.623 7.663 1.00 18.45 ? 389 ILE A O 1 ATOM 2983 C CB . ILE A 1 389 ? -45.473 -1.718 10.527 1.00 13.88 ? 389 ILE A CB 1 ATOM 2984 C CG1 . ILE A 1 389 ? -44.938 -2.392 11.795 1.00 13.08 ? 389 ILE A CG1 1 ATOM 2985 C CG2 . ILE A 1 389 ? -46.999 -1.673 10.558 1.00 15.59 ? 389 ILE A CG2 1 ATOM 2986 C CD1 . ILE A 1 389 ? -45.224 -3.891 11.953 1.00 15.33 ? 389 ILE A CD1 1 ATOM 2987 N N . ASP A 1 390 ? -45.059 -1.188 7.170 1.00 18.17 ? 390 ASP A N 1 ATOM 2988 C CA . ASP A 1 390 ? -45.654 -0.776 5.896 1.00 18.63 ? 390 ASP A CA 1 ATOM 2989 C C . ASP A 1 390 ? -45.621 -1.943 4.913 1.00 16.80 ? 390 ASP A C 1 ATOM 2990 O O . ASP A 1 390 ? -46.585 -2.159 4.194 1.00 18.35 ? 390 ASP A O 1 ATOM 2991 C CB . ASP A 1 390 ? -44.950 0.451 5.312 1.00 20.26 ? 390 ASP A CB 1 ATOM 2992 C CG . ASP A 1 390 ? -45.779 1.142 4.253 1.00 20.94 ? 390 ASP A CG 1 ATOM 2993 O OD1 . ASP A 1 390 ? -46.889 1.624 4.581 1.00 25.15 ? 390 ASP A OD1 1 ATOM 2994 O OD2 . ASP A 1 390 ? -45.333 1.175 3.089 1.00 20.73 ? 390 ASP A OD2 1 ATOM 2995 N N . TYR A 1 391 ? -44.550 -2.736 4.970 1.00 16.43 ? 391 TYR A N 1 ATOM 2996 C CA . TYR A 1 391 ? -44.376 -3.927 4.131 1.00 16.14 ? 391 TYR A CA 1 ATOM 2997 C C . TYR A 1 391 ? -45.413 -4.997 4.514 1.00 16.81 ? 391 TYR A C 1 ATOM 2998 O O . TYR A 1 391 ? -45.951 -5.692 3.656 1.00 18.53 ? 391 TYR A O 1 ATOM 2999 C CB . TYR A 1 391 ? -42.967 -4.492 4.304 1.00 15.42 ? 391 TYR A CB 1 ATOM 3000 C CG . TYR A 1 391 ? -41.867 -3.736 3.588 1.00 16.68 ? 391 TYR A CG 1 ATOM 3001 C CD1 . TYR A 1 391 ? -41.161 -2.686 4.221 1.00 16.89 ? 391 TYR A CD1 1 ATOM 3002 C CD2 . TYR A 1 391 ? -41.507 -4.076 2.270 1.00 14.60 ? 391 TYR A CD2 1 ATOM 3003 C CE1 . TYR A 1 391 ? -40.110 -1.989 3.540 1.00 16.96 ? 391 TYR A CE1 1 ATOM 3004 C CE2 . TYR A 1 391 ? -40.472 -3.391 1.582 1.00 14.34 ? 391 TYR A CE2 1 ATOM 3005 C CZ . TYR A 1 391 ? -39.785 -2.357 2.218 1.00 15.86 ? 391 TYR A CZ 1 ATOM 3006 O OH . TYR A 1 391 ? -38.804 -1.699 1.519 1.00 15.39 ? 391 TYR A OH 1 ATOM 3007 N N . ILE A 1 392 ? -45.724 -5.063 5.808 1.00 16.55 ? 392 ILE A N 1 ATOM 3008 C CA . ILE A 1 392 ? -46.701 -5.993 6.376 1.00 15.14 ? 392 ILE A CA 1 ATOM 3009 C C . ILE A 1 392 ? -48.134 -5.619 5.963 1.00 15.80 ? 392 ILE A C 1 ATOM 3010 O O . ILE A 1 392 ? -48.917 -6.486 5.560 1.00 16.08 ? 392 ILE A O 1 ATOM 3011 C CB . ILE A 1 392 ? -46.544 -6.033 7.946 1.00 13.75 ? 392 ILE A CB 1 ATOM 3012 C CG1 . ILE A 1 392 ? -45.222 -6.720 8.332 1.00 13.43 ? 392 ILE A CG1 1 ATOM 3013 C CG2 . ILE A 1 392 ? -47.775 -6.637 8.656 1.00 13.19 ? 392 ILE A CG2 1 ATOM 3014 C CD1 . ILE A 1 392 ? -45.097 -8.188 7.903 1.00 13.45 ? 392 ILE A CD1 1 ATOM 3015 N N . LEU A 1 393 ? -48.445 -4.325 6.046 1.00 16.49 ? 393 LEU A N 1 ATOM 3016 C CA . LEU A 1 393 ? -49.764 -3.792 5.704 1.00 18.54 ? 393 LEU A CA 1 ATOM 3017 C C . LEU A 1 393 ? -50.081 -3.747 4.213 1.00 19.35 ? 393 LEU A C 1 ATOM 3018 O O . LEU A 1 393 ? -51.250 -3.678 3.830 1.00 20.12 ? 393 LEU A O 1 ATOM 3019 C CB . LEU A 1 393 ? -49.933 -2.390 6.290 1.00 18.62 ? 393 LEU A CB 1 ATOM 3020 C CG . LEU A 1 393 ? -50.035 -2.257 7.807 1.00 18.55 ? 393 LEU A CG 1 ATOM 3021 C CD1 . LEU A 1 393 ? -49.900 -0.794 8.154 1.00 16.98 ? 393 LEU A CD1 1 ATOM 3022 C CD2 . LEU A 1 393 ? -51.339 -2.848 8.337 1.00 17.49 ? 393 LEU A CD2 1 ATOM 3023 N N . THR A 1 394 ? -49.040 -3.743 3.386 1.00 20.98 ? 394 THR A N 1 ATOM 3024 C CA . THR A 1 394 ? -49.203 -3.705 1.939 1.00 23.20 ? 394 THR A CA 1 ATOM 3025 C C . THR A 1 394 ? -48.993 -5.076 1.289 1.00 24.88 ? 394 THR A C 1 ATOM 3026 O O . THR A 1 394 ? -49.115 -5.209 0.065 1.00 26.77 ? 394 THR A O 1 ATOM 3027 C CB . THR A 1 394 ? -48.284 -2.625 1.275 1.00 24.41 ? 394 THR A CB 1 ATOM 3028 O OG1 . THR A 1 394 ? -46.917 -2.823 1.664 1.00 21.41 ? 394 THR A OG1 1 ATOM 3029 C CG2 . THR A 1 394 ? -48.724 -1.208 1.676 1.00 25.15 ? 394 THR A CG2 1 ATOM 3030 N N . GLY A 1 395 ? -48.712 -6.089 2.118 1.00 25.10 ? 395 GLY A N 1 ATOM 3031 C CA . GLY A 1 395 ? -48.491 -7.454 1.644 1.00 25.11 ? 395 GLY A CA 1 ATOM 3032 C C . GLY A 1 395 ? -47.219 -7.665 0.835 1.00 26.63 ? 395 GLY A C 1 ATOM 3033 O O . GLY A 1 395 ? -47.143 -8.562 -0.010 1.00 27.35 ? 395 GLY A O 1 ATOM 3034 N N . ASN A 1 396 ? -46.222 -6.828 1.107 1.00 26.21 ? 396 ASN A N 1 ATOM 3035 C CA . ASN A 1 396 ? -44.930 -6.847 0.428 1.00 27.04 ? 396 ASN A CA 1 ATOM 3036 C C . ASN A 1 396 ? -43.922 -7.628 1.290 1.00 26.35 ? 396 ASN A C 1 ATOM 3037 O O . ASN A 1 396 ? -43.627 -7.232 2.421 1.00 26.42 ? 396 ASN A O 1 ATOM 3038 C CB . ASN A 1 396 ? -44.490 -5.383 0.222 1.00 28.08 ? 396 ASN A CB 1 ATOM 3039 C CG . ASN A 1 396 ? -43.297 -5.220 -0.717 1.00 30.55 ? 396 ASN A CG 1 ATOM 3040 O OD1 . ASN A 1 396 ? -42.467 -6.121 -0.885 1.00 30.46 ? 396 ASN A OD1 1 ATOM 3041 N ND2 . ASN A 1 396 ? -43.201 -4.018 -1.285 1.00 32.96 ? 396 ASN A ND2 1 ATOM 3042 N N . THR A 1 397 ? -43.410 -8.738 0.752 1.00 25.57 ? 397 THR A N 1 ATOM 3043 C CA . THR A 1 397 ? -42.441 -9.572 1.476 1.00 24.65 ? 397 THR A CA 1 ATOM 3044 C C . THR A 1 397 ? -40.984 -9.379 1.035 1.00 23.26 ? 397 THR A C 1 ATOM 3045 O O . THR A 1 397 ? -40.080 -10.044 1.545 1.00 22.82 ? 397 THR A O 1 ATOM 3046 C CB . THR A 1 397 ? -42.799 -11.077 1.419 1.00 23.56 ? 397 THR A CB 1 ATOM 3047 O OG1 . THR A 1 397 ? -42.899 -11.498 0.056 1.00 24.97 ? 397 THR A OG1 1 ATOM 3048 C CG2 . THR A 1 397 ? -44.105 -11.350 2.148 1.00 22.90 ? 397 THR A CG2 1 ATOM 3049 N N . SER A 1 398 ? -40.765 -8.452 0.104 1.00 22.18 ? 398 SER A N 1 ATOM 3050 C CA . SER A 1 398 ? -39.429 -8.154 -0.403 1.00 21.29 ? 398 SER A CA 1 ATOM 3051 C C . SER A 1 398 ? -38.744 -7.143 0.522 1.00 22.26 ? 398 SER A C 1 ATOM 3052 O O . SER A 1 398 ? -38.582 -5.965 0.178 1.00 20.98 ? 398 SER A O 1 ATOM 3053 C CB . SER A 1 398 ? -39.503 -7.639 -1.851 1.00 19.52 ? 398 SER A CB 1 ATOM 3054 O OG . SER A 1 398 ? -40.050 -8.622 -2.712 1.00 13.62 ? 398 SER A OG 1 ATOM 3055 N N . TYR A 1 399 ? -38.401 -7.621 1.725 1.00 22.61 ? 399 TYR A N 1 ATOM 3056 C CA . TYR A 1 399 ? -37.729 -6.819 2.752 1.00 21.54 ? 399 TYR A CA 1 ATOM 3057 C C . TYR A 1 399 ? -36.284 -6.609 2.306 1.00 21.29 ? 399 TYR A C 1 ATOM 3058 O O . TYR A 1 399 ? -35.651 -7.550 1.815 1.00 21.48 ? 399 TYR A O 1 ATOM 3059 C CB . TYR A 1 399 ? -37.729 -7.528 4.122 1.00 18.86 ? 399 TYR A CB 1 ATOM 3060 C CG . TYR A 1 399 ? -39.072 -8.055 4.581 1.00 16.58 ? 399 TYR A CG 1 ATOM 3061 C CD1 . TYR A 1 399 ? -40.147 -7.182 4.857 1.00 15.18 ? 399 TYR A CD1 1 ATOM 3062 C CD2 . TYR A 1 399 ? -39.302 -9.444 4.663 1.00 14.56 ? 399 TYR A CD2 1 ATOM 3063 C CE1 . TYR A 1 399 ? -41.436 -7.690 5.191 1.00 14.79 ? 399 TYR A CE1 1 ATOM 3064 C CE2 . TYR A 1 399 ? -40.571 -9.965 4.994 1.00 13.16 ? 399 TYR A CE2 1 ATOM 3065 C CZ . TYR A 1 399 ? -41.637 -9.084 5.250 1.00 15.98 ? 399 TYR A CZ 1 ATOM 3066 O OH . TYR A 1 399 ? -42.890 -9.594 5.516 1.00 15.92 ? 399 TYR A OH 1 ATOM 3067 N N . PRO A 1 400 ? -35.767 -5.363 2.406 1.00 22.15 ? 400 PRO A N 1 ATOM 3068 C CA . PRO A 1 400 ? -34.385 -5.053 2.007 1.00 21.59 ? 400 PRO A CA 1 ATOM 3069 C C . PRO A 1 400 ? -33.355 -5.759 2.881 1.00 20.56 ? 400 PRO A C 1 ATOM 3070 O O . PRO A 1 400 ? -33.633 -6.082 4.046 1.00 21.15 ? 400 PRO A O 1 ATOM 3071 C CB . PRO A 1 400 ? -34.303 -3.538 2.203 1.00 22.55 ? 400 PRO A CB 1 ATOM 3072 C CG . PRO A 1 400 ? -35.707 -3.086 1.986 1.00 22.79 ? 400 PRO A CG 1 ATOM 3073 C CD . PRO A 1 400 ? -36.486 -4.119 2.748 1.00 22.02 ? 400 PRO A CD 1 ATOM 3074 N N . VAL A 1 401 ? -32.172 -5.976 2.308 1.00 18.57 ? 401 VAL A N 1 ATOM 3075 C CA . VAL A 1 401 ? -31.046 -6.632 2.985 1.00 19.02 ? 401 VAL A CA 1 ATOM 3076 C C . VAL A 1 401 ? -30.631 -5.860 4.247 1.00 18.15 ? 401 VAL A C 1 ATOM 3077 O O . VAL A 1 401 ? -30.423 -6.465 5.302 1.00 18.52 ? 401 VAL A O 1 ATOM 3078 C CB . VAL A 1 401 ? -29.815 -6.778 2.026 1.00 17.82 ? 401 VAL A CB 1 ATOM 3079 C CG1 . VAL A 1 401 ? -28.688 -7.565 2.695 1.00 19.19 ? 401 VAL A CG1 1 ATOM 3080 C CG2 . VAL A 1 401 ? -30.226 -7.497 0.743 1.00 20.22 ? 401 VAL A CG2 1 ATOM 3081 N N . SER A 1 402 ? -30.618 -4.527 4.134 1.00 17.54 ? 402 SER A N 1 ATOM 3082 C CA . SER A 1 402 ? -30.240 -3.606 5.209 1.00 15.77 ? 402 SER A CA 1 ATOM 3083 C C . SER A 1 402 ? -31.174 -3.582 6.410 1.00 14.29 ? 402 SER A C 1 ATOM 3084 O O . SER A 1 402 ? -30.808 -3.062 7.456 1.00 11.76 ? 402 SER A O 1 ATOM 3085 C CB . SER A 1 402 ? -30.098 -2.184 4.671 1.00 16.73 ? 402 SER A CB 1 ATOM 3086 O OG . SER A 1 402 ? -28.998 -2.070 3.791 1.00 25.56 ? 402 SER A OG 1 ATOM 3087 N N . ASP A 1 403 ? -32.379 -4.127 6.250 1.00 14.16 ? 403 ASP A N 1 ATOM 3088 C CA . ASP A 1 403 ? -33.351 -4.164 7.338 1.00 14.18 ? 403 ASP A CA 1 ATOM 3089 C C . ASP A 1 403 ? -33.106 -5.304 8.323 1.00 13.85 ? 403 ASP A C 1 ATOM 3090 O O . ASP A 1 403 ? -33.691 -5.322 9.402 1.00 13.17 ? 403 ASP A O 1 ATOM 3091 C CB . ASP A 1 403 ? -34.777 -4.195 6.791 1.00 16.14 ? 403 ASP A CB 1 ATOM 3092 C CG . ASP A 1 403 ? -35.347 -2.803 6.575 1.00 17.47 ? 403 ASP A CG 1 ATOM 3093 O OD1 . ASP A 1 403 ? -35.623 -2.122 7.582 1.00 17.84 ? 403 ASP A OD1 1 ATOM 3094 O OD2 . ASP A 1 403 ? -35.529 -2.388 5.408 1.00 20.81 ? 403 ASP A OD2 1 ATOM 3095 N N . ASN A 1 404 ? -32.193 -6.209 7.949 1.00 13.76 ? 404 ASN A N 1 ATOM 3096 C CA . ASN A 1 404 ? -31.771 -7.376 8.733 1.00 14.63 ? 404 ASN A CA 1 ATOM 3097 C C . ASN A 1 404 ? -32.911 -8.190 9.362 1.00 15.08 ? 404 ASN A C 1 ATOM 3098 O O . ASN A 1 404 ? -32.955 -8.442 10.578 1.00 13.51 ? 404 ASN A O 1 ATOM 3099 C CB . ASN A 1 404 ? -30.720 -6.964 9.776 1.00 14.08 ? 404 ASN A CB 1 ATOM 3100 C CG . ASN A 1 404 ? -29.443 -6.444 9.151 1.00 15.62 ? 404 ASN A CG 1 ATOM 3101 O OD1 . ASN A 1 404 ? -29.377 -6.201 7.947 1.00 18.53 ? 404 ASN A OD1 1 ATOM 3102 N ND2 . ASN A 1 404 ? -28.423 -6.251 9.973 1.00 13.45 ? 404 ASN A ND2 1 ATOM 3103 N N . ILE A 1 405 ? -33.821 -8.608 8.490 1.00 15.21 ? 405 ILE A N 1 ATOM 3104 C CA . ILE A 1 405 ? -34.994 -9.377 8.863 1.00 15.78 ? 405 ILE A CA 1 ATOM 3105 C C . ILE A 1 405 ? -34.686 -10.846 9.107 1.00 17.47 ? 405 ILE A C 1 ATOM 3106 O O . ILE A 1 405 ? -34.248 -11.567 8.206 1.00 19.65 ? 405 ILE A O 1 ATOM 3107 C CB . ILE A 1 405 ? -36.120 -9.217 7.791 1.00 14.28 ? 405 ILE A CB 1 ATOM 3108 C CG1 . ILE A 1 405 ? -36.610 -7.762 7.760 1.00 15.49 ? 405 ILE A CG1 1 ATOM 3109 C CG2 . ILE A 1 405 ? -37.284 -10.222 8.007 1.00 15.93 ? 405 ILE A CG2 1 ATOM 3110 C CD1 . ILE A 1 405 ? -37.385 -7.297 8.983 1.00 15.27 ? 405 ILE A CD1 1 ATOM 3111 N N . VAL A 1 406 ? -34.869 -11.246 10.360 1.00 18.25 ? 406 VAL A N 1 ATOM 3112 C CA . VAL A 1 406 ? -34.698 -12.624 10.773 1.00 19.65 ? 406 VAL A CA 1 ATOM 3113 C C . VAL A 1 406 ? -36.136 -13.065 11.076 1.00 21.89 ? 406 VAL A C 1 ATOM 3114 O O . VAL A 1 406 ? -36.655 -12.857 12.186 1.00 21.51 ? 406 VAL A O 1 ATOM 3115 C CB . VAL A 1 406 ? -33.798 -12.753 12.023 1.00 19.73 ? 406 VAL A CB 1 ATOM 3116 C CG1 . VAL A 1 406 ? -33.653 -14.206 12.392 1.00 20.53 ? 406 VAL A CG1 1 ATOM 3117 C CG2 . VAL A 1 406 ? -32.418 -12.164 11.760 1.00 18.76 ? 406 VAL A CG2 1 ATOM 3118 N N . GLN A 1 407 ? -36.779 -13.623 10.049 1.00 22.32 ? 407 GLN A N 1 ATOM 3119 C CA . GLN A 1 407 ? -38.162 -14.082 10.126 1.00 23.40 ? 407 GLN A CA 1 ATOM 3120 C C . GLN A 1 407 ? -38.330 -15.381 10.907 1.00 23.69 ? 407 GLN A C 1 ATOM 3121 O O . GLN A 1 407 ? -37.764 -16.416 10.553 1.00 24.22 ? 407 GLN A O 1 ATOM 3122 C CB . GLN A 1 407 ? -38.752 -14.218 8.717 1.00 22.47 ? 407 GLN A CB 1 ATOM 3123 C CG . GLN A 1 407 ? -40.264 -14.346 8.672 1.00 22.54 ? 407 GLN A CG 1 ATOM 3124 C CD . GLN A 1 407 ? -40.811 -14.422 7.256 1.00 24.16 ? 407 GLN A CD 1 ATOM 3125 O OE1 . GLN A 1 407 ? -40.507 -13.579 6.409 1.00 24.46 ? 407 GLN A OE1 1 ATOM 3126 N NE2 . GLN A 1 407 ? -41.635 -15.429 6.999 1.00 21.47 ? 407 GLN A NE2 1 ATOM 3127 N N . VAL A 1 408 ? -39.103 -15.287 11.988 1.00 25.33 ? 408 VAL A N 1 ATOM 3128 C CA . VAL A 1 408 ? -39.398 -16.415 12.870 1.00 26.53 ? 408 VAL A CA 1 ATOM 3129 C C . VAL A 1 408 ? -40.882 -16.778 12.712 1.00 27.68 ? 408 VAL A C 1 ATOM 3130 O O . VAL A 1 408 ? -41.758 -16.068 13.223 1.00 29.05 ? 408 VAL A O 1 ATOM 3131 C CB . VAL A 1 408 ? -39.109 -16.069 14.361 1.00 25.59 ? 408 VAL A CB 1 ATOM 3132 C CG1 . VAL A 1 408 ? -39.111 -17.326 15.191 1.00 26.07 ? 408 VAL A CG1 1 ATOM 3133 C CG2 . VAL A 1 408 ? -37.784 -15.342 14.513 1.00 25.40 ? 408 VAL A CG2 1 ATOM 3134 N N . ASP A 1 409 ? -41.147 -17.875 12.000 1.00 28.54 ? 409 ASP A N 1 ATOM 3135 C CA . ASP A 1 409 ? -42.513 -18.354 11.753 1.00 28.53 ? 409 ASP A CA 1 ATOM 3136 C C . ASP A 1 409 ? -43.100 -19.186 12.886 1.00 28.52 ? 409 ASP A C 1 ATOM 3137 O O . ASP A 1 409 ? -44.317 -19.378 12.943 1.00 28.85 ? 409 ASP A O 1 ATOM 3138 C CB . ASP A 1 409 ? -42.585 -19.146 10.440 1.00 29.29 ? 409 ASP A CB 1 ATOM 3139 C CG . ASP A 1 409 ? -42.560 -18.254 9.210 1.00 29.90 ? 409 ASP A CG 1 ATOM 3140 O OD1 . ASP A 1 409 ? -43.232 -17.203 9.216 1.00 31.94 ? 409 ASP A OD1 1 ATOM 3141 O OD2 . ASP A 1 409 ? -41.877 -18.607 8.228 1.00 29.99 ? 409 ASP A OD2 1 ATOM 3142 N N . ALA A 1 410 ? -42.231 -19.646 13.790 1.00 29.20 ? 410 ALA A N 1 ATOM 3143 C CA . ALA A 1 410 ? -42.596 -20.464 14.955 1.00 29.19 ? 410 ALA A CA 1 ATOM 3144 C C . ALA A 1 410 ? -43.713 -19.816 15.770 1.00 29.17 ? 410 ALA A C 1 ATOM 3145 O O . ALA A 1 410 ? -43.613 -18.654 16.144 1.00 29.19 ? 410 ALA A O 1 ATOM 3146 C CB . ALA A 1 410 ? -41.362 -20.696 15.833 1.00 28.90 ? 410 ALA A CB 1 ATOM 3147 N N . VAL A 1 411 ? -44.801 -20.555 15.963 1.00 30.21 ? 411 VAL A N 1 ATOM 3148 C CA . VAL A 1 411 ? -45.968 -20.064 16.691 1.00 32.51 ? 411 VAL A CA 1 ATOM 3149 C C . VAL A 1 411 ? -46.005 -20.505 18.157 1.00 32.96 ? 411 VAL A C 1 ATOM 3150 O O . VAL A 1 411 ? -46.242 -21.679 18.457 1.00 34.33 ? 411 VAL A O 1 ATOM 3151 C CB . VAL A 1 411 ? -47.299 -20.471 15.961 1.00 33.74 ? 411 VAL A CB 1 ATOM 3152 C CG1 . VAL A 1 411 ? -48.520 -19.906 16.687 1.00 33.08 ? 411 VAL A CG1 1 ATOM 3153 C CG2 . VAL A 1 411 ? -47.288 -19.979 14.508 1.00 34.05 ? 411 VAL A CG2 1 ATOM 3154 N N . ASP A 1 412 ? -45.785 -19.538 19.052 1.00 32.90 ? 412 ASP A N 1 ATOM 3155 C CA . ASP A 1 412 ? -45.798 -19.720 20.512 1.00 33.29 ? 412 ASP A CA 1 ATOM 3156 C C . ASP A 1 412 ? -44.842 -20.809 21.032 1.00 31.89 ? 412 ASP A C 1 ATOM 3157 O O . ASP A 1 412 ? -45.145 -21.529 21.990 1.00 31.90 ? 412 ASP A O 1 ATOM 3158 C CB . ASP A 1 412 ? -47.253 -19.912 21.012 1.00 34.37 ? 412 ASP A CB 1 ATOM 3159 C CG . ASP A 1 412 ? -47.432 -19.590 22.497 1.00 35.11 ? 412 ASP A CG 1 ATOM 3160 O OD1 . ASP A 1 412 ? -46.675 -18.758 23.047 1.00 35.30 ? 412 ASP A OD1 1 ATOM 3161 O OD2 . ASP A 1 412 ? -48.343 -20.184 23.113 1.00 36.46 ? 412 ASP A OD2 1 ATOM 3162 N N . GLN A 1 413 ? -43.692 -20.922 20.369 1.00 29.96 ? 413 GLN A N 1 ATOM 3163 C CA . GLN A 1 413 ? -42.661 -21.896 20.735 1.00 29.59 ? 413 GLN A CA 1 ATOM 3164 C C . GLN A 1 413 ? -41.350 -21.192 21.085 1.00 27.61 ? 413 GLN A C 1 ATOM 3165 O O . GLN A 1 413 ? -41.092 -20.070 20.633 1.00 26.45 ? 413 GLN A O 1 ATOM 3166 C CB . GLN A 1 413 ? -42.413 -22.906 19.593 1.00 32.16 ? 413 GLN A CB 1 ATOM 3167 C CG . GLN A 1 413 ? -43.555 -23.887 19.271 1.00 35.15 ? 413 GLN A CG 1 ATOM 3168 C CD . GLN A 1 413 ? -43.862 -24.871 20.397 1.00 38.55 ? 413 GLN A CD 1 ATOM 3169 O OE1 . GLN A 1 413 ? -43.161 -25.871 20.582 1.00 37.96 ? 413 GLN A OE1 1 ATOM 3170 N NE2 . GLN A 1 413 ? -44.926 -24.596 21.147 1.00 41.19 ? 413 GLN A NE2 1 ATOM 3171 N N . TRP A 1 414 ? -40.527 -21.864 21.889 1.00 25.87 ? 414 TRP A N 1 ATOM 3172 C CA . TRP A 1 414 ? -39.227 -21.337 22.302 1.00 25.80 ? 414 TRP A CA 1 ATOM 3173 C C . TRP A 1 414 ? -38.230 -21.365 21.150 1.00 24.84 ? 414 TRP A C 1 ATOM 3174 O O . TRP A 1 414 ? -38.118 -22.370 20.437 1.00 24.50 ? 414 TRP A O 1 ATOM 3175 C CB . TRP A 1 414 ? -38.656 -22.122 23.493 1.00 27.32 ? 414 TRP A CB 1 ATOM 3176 C CG . TRP A 1 414 ? -39.428 -21.966 24.785 1.00 27.23 ? 414 TRP A CG 1 ATOM 3177 C CD1 . TRP A 1 414 ? -40.307 -22.862 25.322 1.00 28.16 ? 414 TRP A CD1 1 ATOM 3178 C CD2 . TRP A 1 414 ? -39.379 -20.859 25.695 1.00 26.21 ? 414 TRP A CD2 1 ATOM 3179 N NE1 . TRP A 1 414 ? -40.816 -22.385 26.508 1.00 28.92 ? 414 TRP A NE1 1 ATOM 3180 C CE2 . TRP A 1 414 ? -40.269 -21.158 26.765 1.00 26.87 ? 414 TRP A CE2 1 ATOM 3181 C CE3 . TRP A 1 414 ? -38.670 -19.641 25.718 1.00 25.14 ? 414 TRP A CE3 1 ATOM 3182 C CZ2 . TRP A 1 414 ? -40.475 -20.280 27.850 1.00 26.34 ? 414 TRP A CZ2 1 ATOM 3183 C CZ3 . TRP A 1 414 ? -38.874 -18.756 26.799 1.00 24.76 ? 414 TRP A CZ3 1 ATOM 3184 C CH2 . TRP A 1 414 ? -39.775 -19.088 27.851 1.00 27.18 ? 414 TRP A CH2 1 ATOM 3185 N N . THR A 1 415 ? -37.579 -20.222 20.928 1.00 23.03 ? 415 THR A N 1 ATOM 3186 C CA . THR A 1 415 ? -36.585 -20.072 19.869 1.00 22.40 ? 415 THR A CA 1 ATOM 3187 C C . THR A 1 415 ? -35.236 -19.727 20.484 1.00 21.03 ? 415 THR A C 1 ATOM 3188 O O . THR A 1 415 ? -35.124 -18.806 21.288 1.00 23.27 ? 415 THR A O 1 ATOM 3189 C CB . THR A 1 415 ? -37.001 -19.012 18.841 1.00 22.77 ? 415 THR A CB 1 ATOM 3190 O OG1 . THR A 1 415 ? -37.243 -17.765 19.501 1.00 24.69 ? 415 THR A OG1 1 ATOM 3191 C CG2 . THR A 1 415 ? -38.251 -19.452 18.100 1.00 23.35 ? 415 THR A CG2 1 ATOM 3192 N N . TYR A 1 416 ? -34.221 -20.480 20.085 1.00 18.43 ? 416 TYR A N 1 ATOM 3193 C CA . TYR A 1 416 ? -32.867 -20.340 20.609 1.00 17.49 ? 416 TYR A CA 1 ATOM 3194 C C . TYR A 1 416 ? -31.971 -19.575 19.660 1.00 14.96 ? 416 TYR A C 1 ATOM 3195 O O . TYR A 1 416 ? -31.989 -19.806 18.451 1.00 15.34 ? 416 TYR A O 1 ATOM 3196 C CB . TYR A 1 416 ? -32.276 -21.727 20.888 1.00 19.92 ? 416 TYR A CB 1 ATOM 3197 C CG . TYR A 1 416 ? -33.151 -22.618 21.744 1.00 18.15 ? 416 TYR A CG 1 ATOM 3198 C CD1 . TYR A 1 416 ? -34.117 -23.471 21.158 1.00 19.57 ? 416 TYR A CD1 1 ATOM 3199 C CD2 . TYR A 1 416 ? -33.027 -22.611 23.145 1.00 18.05 ? 416 TYR A CD2 1 ATOM 3200 C CE1 . TYR A 1 416 ? -34.949 -24.307 21.967 1.00 20.26 ? 416 TYR A CE1 1 ATOM 3201 C CE2 . TYR A 1 416 ? -33.846 -23.433 23.962 1.00 19.25 ? 416 TYR A CE2 1 ATOM 3202 C CZ . TYR A 1 416 ? -34.798 -24.275 23.367 1.00 19.49 ? 416 TYR A CZ 1 ATOM 3203 O OH . TYR A 1 416 ? -35.568 -25.076 24.168 1.00 20.84 ? 416 TYR A OH 1 ATOM 3204 N N . TRP A 1 417 ? -31.236 -18.607 20.206 1.00 11.35 ? 417 TRP A N 1 ATOM 3205 C CA . TRP A 1 417 ? -30.350 -17.766 19.399 1.00 9.72 ? 417 TRP A CA 1 ATOM 3206 C C . TRP A 1 417 ? -28.969 -17.671 19.979 1.00 7.50 ? 417 TRP A C 1 ATOM 3207 O O . TRP A 1 417 ? -28.785 -17.296 21.142 1.00 8.94 ? 417 TRP A O 1 ATOM 3208 C CB . TRP A 1 417 ? -30.929 -16.344 19.217 1.00 8.55 ? 417 TRP A CB 1 ATOM 3209 C CG . TRP A 1 417 ? -32.314 -16.373 18.702 1.00 6.50 ? 417 TRP A CG 1 ATOM 3210 C CD1 . TRP A 1 417 ? -33.449 -16.466 19.449 1.00 5.59 ? 417 TRP A CD1 1 ATOM 3211 C CD2 . TRP A 1 417 ? -32.718 -16.524 17.334 1.00 8.24 ? 417 TRP A CD2 1 ATOM 3212 N NE1 . TRP A 1 417 ? -34.534 -16.699 18.644 1.00 8.43 ? 417 TRP A NE1 1 ATOM 3213 C CE2 . TRP A 1 417 ? -34.120 -16.738 17.338 1.00 8.29 ? 417 TRP A CE2 1 ATOM 3214 C CE3 . TRP A 1 417 ? -32.030 -16.510 16.099 1.00 7.61 ? 417 TRP A CE3 1 ATOM 3215 C CZ2 . TRP A 1 417 ? -34.861 -16.943 16.148 1.00 8.88 ? 417 TRP A CZ2 1 ATOM 3216 C CZ3 . TRP A 1 417 ? -32.765 -16.715 14.909 1.00 6.11 ? 417 TRP A CZ3 1 ATOM 3217 C CH2 . TRP A 1 417 ? -34.170 -16.929 14.948 1.00 7.27 ? 417 TRP A CH2 1 ATOM 3218 N N . LEU A 1 418 ? -28.000 -18.057 19.165 1.00 6.58 ? 418 LEU A N 1 ATOM 3219 C CA . LEU A 1 418 ? -26.608 -18.002 19.556 1.00 5.03 ? 418 LEU A CA 1 ATOM 3220 C C . LEU A 1 418 ? -26.015 -16.750 18.936 1.00 4.58 ? 418 LEU A C 1 ATOM 3221 O O . LEU A 1 418 ? -26.025 -16.591 17.718 1.00 7.95 ? 418 LEU A O 1 ATOM 3222 C CB . LEU A 1 418 ? -25.866 -19.261 19.090 1.00 3.09 ? 418 LEU A CB 1 ATOM 3223 C CG . LEU A 1 418 ? -24.371 -19.401 19.405 1.00 3.81 ? 418 LEU A CG 1 ATOM 3224 C CD1 . LEU A 1 418 ? -24.123 -19.580 20.898 1.00 2.00 ? 418 LEU A CD1 1 ATOM 3225 C CD2 . LEU A 1 418 ? -23.840 -20.588 18.655 1.00 4.06 ? 418 LEU A CD2 1 ATOM 3226 N N . ILE A 1 419 ? -25.586 -15.823 19.784 1.00 4.89 ? 419 ILE A N 1 ATOM 3227 C CA . ILE A 1 419 ? -24.971 -14.582 19.315 1.00 6.00 ? 419 ILE A CA 1 ATOM 3228 C C . ILE A 1 419 ? -23.464 -14.705 19.545 1.00 7.04 ? 419 ILE A C 1 ATOM 3229 O O . ILE A 1 419 ? -23.044 -14.913 20.680 1.00 7.60 ? 419 ILE A O 1 ATOM 3230 C CB . ILE A 1 419 ? -25.527 -13.329 20.058 1.00 5.28 ? 419 ILE A CB 1 ATOM 3231 C CG1 . ILE A 1 419 ? -27.048 -13.263 19.945 1.00 4.48 ? 419 ILE A CG1 1 ATOM 3232 C CG2 . ILE A 1 419 ? -25.021 -12.056 19.406 1.00 5.83 ? 419 ILE A CG2 1 ATOM 3233 C CD1 . ILE A 1 419 ? -27.778 -13.971 21.013 1.00 3.41 ? 419 ILE A CD1 1 ATOM 3234 N N . GLU A 1 420 ? -22.677 -14.639 18.465 1.00 8.31 ? 420 GLU A N 1 ATOM 3235 C CA . GLU A 1 420 ? -21.202 -14.734 18.531 1.00 9.92 ? 420 GLU A CA 1 ATOM 3236 C C . GLU A 1 420 ? -20.572 -13.338 18.478 1.00 10.56 ? 420 GLU A C 1 ATOM 3237 O O . GLU A 1 420 ? -20.972 -12.524 17.653 1.00 12.58 ? 420 GLU A O 1 ATOM 3238 C CB . GLU A 1 420 ? -20.645 -15.563 17.368 1.00 7.23 ? 420 GLU A CB 1 ATOM 3239 C CG . GLU A 1 420 ? -21.272 -16.925 17.192 1.00 8.07 ? 420 GLU A CG 1 ATOM 3240 C CD . GLU A 1 420 ? -20.638 -17.730 16.069 1.00 11.41 ? 420 GLU A CD 1 ATOM 3241 O OE1 . GLU A 1 420 ? -20.673 -17.284 14.892 1.00 11.32 ? 420 GLU A OE1 1 ATOM 3242 O OE2 . GLU A 1 420 ? -20.112 -18.825 16.371 1.00 13.42 ? 420 GLU A OE2 1 ATOM 3243 N N . ASN A 1 421 ? -19.539 -13.107 19.296 1.00 11.72 ? 421 ASN A N 1 ATOM 3244 C CA . ASN A 1 421 ? -18.851 -11.808 19.385 1.00 10.97 ? 421 ASN A CA 1 ATOM 3245 C C . ASN A 1 421 ? -17.493 -11.686 18.688 1.00 11.03 ? 421 ASN A C 1 ATOM 3246 O O . ASN A 1 421 ? -16.458 -11.599 19.363 1.00 9.30 ? 421 ASN A O 1 ATOM 3247 C CB . ASN A 1 421 ? -18.680 -11.417 20.858 1.00 9.62 ? 421 ASN A CB 1 ATOM 3248 C CG . ASN A 1 421 ? -18.556 -9.918 21.064 1.00 9.69 ? 421 ASN A CG 1 ATOM 3249 O OD1 . ASN A 1 421 ? -18.459 -9.145 20.111 1.00 7.35 ? 421 ASN A OD1 1 ATOM 3250 N ND2 . ASN A 1 421 ? -18.592 -9.499 22.321 1.00 10.68 ? 421 ASN A ND2 1 ATOM 3251 N N . ASP A 1 422 ? -17.509 -11.631 17.348 1.00 12.53 ? 422 ASP A N 1 ATOM 3252 C CA . ASP A 1 422 ? -16.310 -11.476 16.497 1.00 12.30 ? 422 ASP A CA 1 ATOM 3253 C C . ASP A 1 422 ? -15.113 -12.313 16.975 1.00 15.58 ? 422 ASP A C 1 ATOM 3254 O O . ASP A 1 422 ? -14.088 -11.756 17.392 1.00 15.20 ? 422 ASP A O 1 ATOM 3255 C CB . ASP A 1 422 ? -15.937 -9.984 16.430 1.00 11.78 ? 422 ASP A CB 1 ATOM 3256 C CG . ASP A 1 422 ? -15.367 -9.569 15.086 1.00 11.38 ? 422 ASP A CG 1 ATOM 3257 O OD1 . ASP A 1 422 ? -15.150 -10.431 14.203 1.00 14.66 ? 422 ASP A OD1 1 ATOM 3258 O OD2 . ASP A 1 422 ? -15.159 -8.354 14.904 1.00 9.58 ? 422 ASP A OD2 1 ATOM 3259 N N . PRO A 1 423 ? -15.239 -13.660 16.951 1.00 18.70 ? 423 PRO A N 1 ATOM 3260 C CA . PRO A 1 423 ? -14.142 -14.525 17.405 1.00 21.75 ? 423 PRO A CA 1 ATOM 3261 C C . PRO A 1 423 ? -12.870 -14.471 16.554 1.00 24.04 ? 423 PRO A C 1 ATOM 3262 O O . PRO A 1 423 ? -11.765 -14.553 17.096 1.00 26.61 ? 423 PRO A O 1 ATOM 3263 C CB . PRO A 1 423 ? -14.768 -15.921 17.373 1.00 21.79 ? 423 PRO A CB 1 ATOM 3264 C CG . PRO A 1 423 ? -16.254 -15.665 17.386 1.00 21.50 ? 423 PRO A CG 1 ATOM 3265 C CD . PRO A 1 423 ? -16.371 -14.485 16.493 1.00 19.02 ? 423 PRO A CD 1 ATOM 3266 N N . GLU A 1 424 ? -13.043 -14.291 15.240 1.00 25.51 ? 424 GLU A N 1 ATOM 3267 C CA . GLU A 1 424 ? -11.936 -14.236 14.278 1.00 25.38 ? 424 GLU A CA 1 ATOM 3268 C C . GLU A 1 424 ? -11.447 -12.818 13.940 1.00 24.62 ? 424 GLU A C 1 ATOM 3269 O O . GLU A 1 424 ? -10.607 -12.645 13.046 1.00 24.23 ? 424 GLU A O 1 ATOM 3270 C CB . GLU A 1 424 ? -12.330 -14.959 12.977 1.00 26.66 ? 424 GLU A CB 1 ATOM 3271 C CG . GLU A 1 424 ? -12.947 -16.360 13.134 1.00 31.16 ? 424 GLU A CG 1 ATOM 3272 C CD . GLU A 1 424 ? -12.033 -17.365 13.821 1.00 32.45 ? 424 GLU A CD 1 ATOM 3273 O OE1 . GLU A 1 424 ? -10.993 -17.739 13.234 1.00 33.33 ? 424 GLU A OE1 1 ATOM 3274 O OE2 . GLU A 1 424 ? -12.367 -17.783 14.951 1.00 34.06 ? 424 GLU A OE2 1 ATOM 3275 N N . GLY A 1 425 ? -11.970 -11.815 14.652 1.00 22.39 ? 425 GLY A N 1 ATOM 3276 C CA . GLY A 1 425 ? -11.584 -10.431 14.413 1.00 19.44 ? 425 GLY A CA 1 ATOM 3277 C C . GLY A 1 425 ? -10.350 -9.964 15.172 1.00 17.94 ? 425 GLY A C 1 ATOM 3278 O O . GLY A 1 425 ? -9.864 -10.698 16.037 1.00 16.74 ? 425 GLY A O 1 ATOM 3279 N N . PRO A 1 426 ? -9.777 -8.782 14.836 1.00 17.41 ? 426 PRO A N 1 ATOM 3280 C CA . PRO A 1 426 ? -8.588 -8.244 15.515 1.00 16.83 ? 426 PRO A CA 1 ATOM 3281 C C . PRO A 1 426 ? -8.789 -8.001 17.011 1.00 17.29 ? 426 PRO A C 1 ATOM 3282 O O . PRO A 1 426 ? -7.940 -8.369 17.829 1.00 17.90 ? 426 PRO A O 1 ATOM 3283 C CB . PRO A 1 426 ? -8.310 -6.946 14.756 1.00 15.07 ? 426 PRO A CB 1 ATOM 3284 C CG . PRO A 1 426 ? -9.629 -6.604 14.114 1.00 14.65 ? 426 PRO A CG 1 ATOM 3285 C CD . PRO A 1 426 ? -10.097 -7.947 13.665 1.00 16.64 ? 426 PRO A CD 1 ATOM 3286 N N . PHE A 1 427 ? -9.922 -7.392 17.347 1.00 17.01 ? 427 PHE A N 1 ATOM 3287 C CA . PHE A 1 427 ? -10.294 -7.123 18.729 1.00 17.45 ? 427 PHE A CA 1 ATOM 3288 C C . PHE A 1 427 ? -11.813 -7.245 18.873 1.00 14.81 ? 427 PHE A C 1 ATOM 3289 O O . PHE A 1 427 ? -12.561 -7.155 17.882 1.00 12.43 ? 427 PHE A O 1 ATOM 3290 C CB . PHE A 1 427 ? -9.769 -5.750 19.221 1.00 20.85 ? 427 PHE A CB 1 ATOM 3291 C CG . PHE A 1 427 ? -10.479 -4.563 18.628 1.00 23.16 ? 427 PHE A CG 1 ATOM 3292 C CD1 . PHE A 1 427 ? -10.239 -4.179 17.291 1.00 24.47 ? 427 PHE A CD1 1 ATOM 3293 C CD2 . PHE A 1 427 ? -11.442 -3.861 19.386 1.00 23.94 ? 427 PHE A CD2 1 ATOM 3294 C CE1 . PHE A 1 427 ? -10.958 -3.107 16.695 1.00 25.03 ? 427 PHE A CE1 1 ATOM 3295 C CE2 . PHE A 1 427 ? -12.174 -2.791 18.817 1.00 25.88 ? 427 PHE A CE2 1 ATOM 3296 C CZ . PHE A 1 427 ? -11.930 -2.411 17.459 1.00 24.99 ? 427 PHE A CZ 1 ATOM 3297 N N . SER A 1 428 ? -12.249 -7.436 20.114 1.00 11.51 ? 428 SER A N 1 ATOM 3298 C CA . SER A 1 428 ? -13.659 -7.576 20.427 1.00 9.21 ? 428 SER A CA 1 ATOM 3299 C C . SER A 1 428 ? -13.987 -6.850 21.731 1.00 10.57 ? 428 SER A C 1 ATOM 3300 O O . SER A 1 428 ? -13.224 -6.910 22.706 1.00 7.83 ? 428 SER A O 1 ATOM 3301 C CB . SER A 1 428 ? -14.024 -9.058 20.515 1.00 8.25 ? 428 SER A CB 1 ATOM 3302 O OG . SER A 1 428 ? -15.424 -9.262 20.519 1.00 7.55 ? 428 SER A OG 1 ATOM 3303 N N . LEU A 1 429 ? -15.119 -6.141 21.700 1.00 10.82 ? 429 LEU A N 1 ATOM 3304 C CA . LEU A 1 429 ? -15.637 -5.349 22.807 1.00 7.87 ? 429 LEU A CA 1 ATOM 3305 C C . LEU A 1 429 ? -16.923 -5.970 23.359 1.00 8.31 ? 429 LEU A C 1 ATOM 3306 O O . LEU A 1 429 ? -17.618 -6.681 22.631 1.00 9.96 ? 429 LEU A O 1 ATOM 3307 C CB . LEU A 1 429 ? -15.930 -3.924 22.306 1.00 11.66 ? 429 LEU A CB 1 ATOM 3308 C CG . LEU A 1 429 ? -14.762 -2.966 22.028 1.00 11.17 ? 429 LEU A CG 1 ATOM 3309 C CD1 . LEU A 1 429 ? -15.255 -1.757 21.251 1.00 12.09 ? 429 LEU A CD1 1 ATOM 3310 C CD2 . LEU A 1 429 ? -14.107 -2.523 23.334 1.00 12.42 ? 429 LEU A CD2 1 ATOM 3311 N N . PRO A 1 430 ? -17.230 -5.762 24.670 1.00 6.79 ? 430 PRO A N 1 ATOM 3312 C CA . PRO A 1 430 ? -18.452 -6.308 25.282 1.00 6.57 ? 430 PRO A CA 1 ATOM 3313 C C . PRO A 1 430 ? -19.702 -5.592 24.738 1.00 8.62 ? 430 PRO A C 1 ATOM 3314 O O . PRO A 1 430 ? -19.662 -4.385 24.469 1.00 9.06 ? 430 PRO A O 1 ATOM 3315 C CB . PRO A 1 430 ? -18.249 -6.007 26.770 1.00 8.11 ? 430 PRO A CB 1 ATOM 3316 C CG . PRO A 1 430 ? -16.794 -5.969 26.929 1.00 6.10 ? 430 PRO A CG 1 ATOM 3317 C CD . PRO A 1 430 ? -16.373 -5.182 25.720 1.00 5.92 ? 430 PRO A CD 1 ATOM 3318 N N . HIS A 1 431 ? -20.790 -6.336 24.538 1.00 6.40 ? 431 HIS A N 1 ATOM 3319 C CA . HIS A 1 431 ? -22.015 -5.755 23.990 1.00 8.93 ? 431 HIS A CA 1 ATOM 3320 C C . HIS A 1 431 ? -23.288 -6.021 24.801 1.00 8.56 ? 431 HIS A C 1 ATOM 3321 O O . HIS A 1 431 ? -23.670 -7.174 24.985 1.00 11.22 ? 431 HIS A O 1 ATOM 3322 C CB . HIS A 1 431 ? -22.268 -6.236 22.538 1.00 8.35 ? 431 HIS A CB 1 ATOM 3323 C CG . HIS A 1 431 ? -21.193 -5.861 21.560 1.00 10.16 ? 431 HIS A CG 1 ATOM 3324 N ND1 . HIS A 1 431 ? -20.716 -4.576 21.427 1.00 9.38 ? 431 HIS A ND1 1 ATOM 3325 C CD2 . HIS A 1 431 ? -20.501 -6.609 20.667 1.00 11.49 ? 431 HIS A CD2 1 ATOM 3326 C CE1 . HIS A 1 431 ? -19.776 -4.546 20.500 1.00 8.80 ? 431 HIS A CE1 1 ATOM 3327 N NE2 . HIS A 1 431 ? -19.627 -5.767 20.022 1.00 11.21 ? 431 HIS A NE2 1 ATOM 3328 N N . PRO A 1 432 ? -23.947 -4.959 25.315 1.00 7.37 ? 432 PRO A N 1 ATOM 3329 C CA . PRO A 1 432 ? -25.186 -5.112 26.085 1.00 8.31 ? 432 PRO A CA 1 ATOM 3330 C C . PRO A 1 432 ? -26.347 -5.386 25.117 1.00 8.83 ? 432 PRO A C 1 ATOM 3331 O O . PRO A 1 432 ? -26.909 -4.476 24.515 1.00 11.44 ? 432 PRO A O 1 ATOM 3332 C CB . PRO A 1 432 ? -25.309 -3.761 26.794 1.00 8.99 ? 432 PRO A CB 1 ATOM 3333 C CG . PRO A 1 432 ? -24.667 -2.809 25.826 1.00 6.00 ? 432 PRO A CG 1 ATOM 3334 C CD . PRO A 1 432 ? -23.451 -3.571 25.411 1.00 8.42 ? 432 PRO A CD 1 ATOM 3335 N N . MET A 1 433 ? -26.613 -6.663 24.880 1.00 10.32 ? 433 MET A N 1 ATOM 3336 C CA . MET A 1 433 ? -27.678 -7.063 23.969 1.00 10.85 ? 433 MET A CA 1 ATOM 3337 C C . MET A 1 433 ? -29.069 -6.896 24.567 1.00 10.32 ? 433 MET A C 1 ATOM 3338 O O . MET A 1 433 ? -29.358 -7.363 25.671 1.00 9.43 ? 433 MET A O 1 ATOM 3339 C CB . MET A 1 433 ? -27.448 -8.481 23.455 1.00 11.06 ? 433 MET A CB 1 ATOM 3340 C CG . MET A 1 433 ? -26.185 -8.634 22.634 1.00 11.14 ? 433 MET A CG 1 ATOM 3341 S SD . MET A 1 433 ? -25.939 -7.395 21.328 1.00 19.92 ? 433 MET A SD 1 ATOM 3342 C CE . MET A 1 433 ? -26.842 -8.096 20.004 1.00 13.22 ? 433 MET A CE 1 ATOM 3343 N N . HIS A 1 434 ? -29.903 -6.181 23.823 1.00 10.53 ? 434 HIS A N 1 ATOM 3344 C CA . HIS A 1 434 ? -31.256 -5.877 24.233 1.00 10.00 ? 434 HIS A CA 1 ATOM 3345 C C . HIS A 1 434 ? -32.294 -6.270 23.177 1.00 10.42 ? 434 HIS A C 1 ATOM 3346 O O . HIS A 1 434 ? -32.127 -5.956 21.991 1.00 8.20 ? 434 HIS A O 1 ATOM 3347 C CB . HIS A 1 434 ? -31.342 -4.379 24.576 1.00 10.89 ? 434 HIS A CB 1 ATOM 3348 C CG . HIS A 1 434 ? -32.738 -3.891 24.774 1.00 12.53 ? 434 HIS A CG 1 ATOM 3349 N ND1 . HIS A 1 434 ? -33.578 -4.426 25.725 1.00 13.88 ? 434 HIS A ND1 1 ATOM 3350 C CD2 . HIS A 1 434 ? -33.486 -3.025 24.053 1.00 13.20 ? 434 HIS A CD2 1 ATOM 3351 C CE1 . HIS A 1 434 ? -34.787 -3.920 25.572 1.00 13.73 ? 434 HIS A CE1 1 ATOM 3352 N NE2 . HIS A 1 434 ? -34.757 -3.068 24.566 1.00 13.41 ? 434 HIS A NE2 1 ATOM 3353 N N . LEU A 1 435 ? -33.386 -6.888 23.649 1.00 9.10 ? 435 LEU A N 1 ATOM 3354 C CA . LEU A 1 435 ? -34.504 -7.332 22.804 1.00 9.08 ? 435 LEU A CA 1 ATOM 3355 C C . LEU A 1 435 ? -35.804 -6.580 23.089 1.00 9.22 ? 435 LEU A C 1 ATOM 3356 O O . LEU A 1 435 ? -36.201 -6.404 24.252 1.00 7.46 ? 435 LEU A O 1 ATOM 3357 C CB . LEU A 1 435 ? -34.757 -8.835 22.983 1.00 6.79 ? 435 LEU A CB 1 ATOM 3358 C CG . LEU A 1 435 ? -35.837 -9.583 22.191 1.00 6.09 ? 435 LEU A CG 1 ATOM 3359 C CD1 . LEU A 1 435 ? -35.601 -9.454 20.698 1.00 5.20 ? 435 LEU A CD1 1 ATOM 3360 C CD2 . LEU A 1 435 ? -35.851 -11.039 22.587 1.00 4.80 ? 435 LEU A CD2 1 ATOM 3361 N N . HIS A 1 436 ? -36.484 -6.208 22.004 1.00 8.65 ? 436 HIS A N 1 ATOM 3362 C CA . HIS A 1 436 ? -37.757 -5.496 22.063 1.00 8.91 ? 436 HIS A CA 1 ATOM 3363 C C . HIS A 1 436 ? -38.906 -6.488 22.143 1.00 9.93 ? 436 HIS A C 1 ATOM 3364 O O . HIS A 1 436 ? -38.815 -7.603 21.616 1.00 9.80 ? 436 HIS A O 1 ATOM 3365 C CB . HIS A 1 436 ? -37.962 -4.627 20.812 1.00 7.62 ? 436 HIS A CB 1 ATOM 3366 C CG . HIS A 1 436 ? -37.129 -3.383 20.774 1.00 3.96 ? 436 HIS A CG 1 ATOM 3367 N ND1 . HIS A 1 436 ? -37.645 -2.166 20.394 1.00 1.00 ? 436 HIS A ND1 1 ATOM 3368 C CD2 . HIS A 1 436 ? -35.808 -3.178 20.993 1.00 3.90 ? 436 HIS A CD2 1 ATOM 3369 C CE1 . HIS A 1 436 ? -36.681 -1.267 20.374 1.00 1.00 ? 436 HIS A CE1 1 ATOM 3370 N NE2 . HIS A 1 436 ? -35.556 -1.855 20.734 1.00 1.00 ? 436 HIS A NE2 1 ATOM 3371 N N . GLY A 1 437 ? -39.971 -6.072 22.830 1.00 10.63 ? 437 GLY A N 1 ATOM 3372 C CA . GLY A 1 437 ? -41.168 -6.879 22.968 1.00 11.27 ? 437 GLY A CA 1 ATOM 3373 C C . GLY A 1 437 ? -41.158 -8.172 23.748 1.00 13.51 ? 437 GLY A C 1 ATOM 3374 O O . GLY A 1 437 ? -42.183 -8.853 23.822 1.00 12.61 ? 437 GLY A O 1 ATOM 3375 N N . HIS A 1 438 ? -40.002 -8.533 24.298 1.00 14.57 ? 438 HIS A N 1 ATOM 3376 C CA . HIS A 1 438 ? -39.861 -9.766 25.064 1.00 15.46 ? 438 HIS A CA 1 ATOM 3377 C C . HIS A 1 438 ? -38.903 -9.616 26.242 1.00 14.84 ? 438 HIS A C 1 ATOM 3378 O O . HIS A 1 438 ? -38.308 -8.563 26.472 1.00 15.04 ? 438 HIS A O 1 ATOM 3379 C CB . HIS A 1 438 ? -39.286 -10.892 24.174 1.00 16.91 ? 438 HIS A CB 1 ATOM 3380 C CG . HIS A 1 438 ? -40.186 -11.347 23.068 1.00 18.76 ? 438 HIS A CG 1 ATOM 3381 N ND1 . HIS A 1 438 ? -41.177 -12.288 23.254 1.00 20.43 ? 438 HIS A ND1 1 ATOM 3382 C CD2 . HIS A 1 438 ? -40.229 -11.008 21.758 1.00 18.63 ? 438 HIS A CD2 1 ATOM 3383 C CE1 . HIS A 1 438 ? -41.791 -12.508 22.105 1.00 18.97 ? 438 HIS A CE1 1 ATOM 3384 N NE2 . HIS A 1 438 ? -41.235 -11.743 21.183 1.00 20.56 ? 438 HIS A NE2 1 ATOM 3385 N N . ASP A 1 439 ? -38.824 -10.700 27.003 1.00 14.22 ? 439 ASP A N 1 ATOM 3386 C CA . ASP A 1 439 ? -37.896 -10.871 28.106 1.00 14.83 ? 439 ASP A CA 1 ATOM 3387 C C . ASP A 1 439 ? -37.319 -12.228 27.718 1.00 15.67 ? 439 ASP A C 1 ATOM 3388 O O . ASP A 1 439 ? -38.071 -13.205 27.577 1.00 19.03 ? 439 ASP A O 1 ATOM 3389 C CB . ASP A 1 439 ? -38.592 -10.976 29.462 1.00 13.30 ? 439 ASP A CB 1 ATOM 3390 C CG . ASP A 1 439 ? -38.723 -9.648 30.166 1.00 10.93 ? 439 ASP A CG 1 ATOM 3391 O OD1 . ASP A 1 439 ? -37.930 -8.719 29.934 1.00 13.65 ? 439 ASP A OD1 1 ATOM 3392 O OD2 . ASP A 1 439 ? -39.649 -9.538 30.977 1.00 11.89 ? 439 ASP A OD2 1 ATOM 3393 N N . PHE A 1 440 ? -36.019 -12.266 27.431 1.00 14.95 ? 440 PHE A N 1 ATOM 3394 C CA . PHE A 1 440 ? -35.371 -13.517 27.035 1.00 15.71 ? 440 PHE A CA 1 ATOM 3395 C C . PHE A 1 440 ? -34.795 -14.320 28.194 1.00 16.42 ? 440 PHE A C 1 ATOM 3396 O O . PHE A 1 440 ? -34.627 -13.799 29.291 1.00 18.01 ? 440 PHE A O 1 ATOM 3397 C CB . PHE A 1 440 ? -34.295 -13.288 25.944 1.00 12.39 ? 440 PHE A CB 1 ATOM 3398 C CG . PHE A 1 440 ? -33.313 -12.155 26.231 1.00 13.03 ? 440 PHE A CG 1 ATOM 3399 C CD1 . PHE A 1 440 ? -32.448 -12.176 27.353 1.00 12.08 ? 440 PHE A CD1 1 ATOM 3400 C CD2 . PHE A 1 440 ? -33.210 -11.075 25.338 1.00 13.16 ? 440 PHE A CD2 1 ATOM 3401 C CE1 . PHE A 1 440 ? -31.499 -11.140 27.573 1.00 7.37 ? 440 PHE A CE1 1 ATOM 3402 C CE2 . PHE A 1 440 ? -32.252 -10.027 25.548 1.00 11.21 ? 440 PHE A CE2 1 ATOM 3403 C CZ . PHE A 1 440 ? -31.401 -10.072 26.670 1.00 6.10 ? 440 PHE A CZ 1 ATOM 3404 N N . LEU A 1 441 ? -34.500 -15.589 27.933 1.00 16.59 ? 441 LEU A N 1 ATOM 3405 C CA . LEU A 1 441 ? -33.883 -16.464 28.918 1.00 16.81 ? 441 LEU A CA 1 ATOM 3406 C C . LEU A 1 441 ? -32.399 -16.543 28.560 1.00 16.93 ? 441 LEU A C 1 ATOM 3407 O O . LEU A 1 441 ? -32.046 -16.850 27.417 1.00 12.92 ? 441 LEU A O 1 ATOM 3408 C CB . LEU A 1 441 ? -34.494 -17.864 28.865 1.00 17.42 ? 441 LEU A CB 1 ATOM 3409 C CG . LEU A 1 441 ? -35.967 -18.092 29.187 1.00 17.44 ? 441 LEU A CG 1 ATOM 3410 C CD1 . LEU A 1 441 ? -36.181 -19.585 29.214 1.00 14.18 ? 441 LEU A CD1 1 ATOM 3411 C CD2 . LEU A 1 441 ? -36.347 -17.507 30.525 1.00 16.79 ? 441 LEU A CD2 1 ATOM 3412 N N . VAL A 1 442 ? -31.542 -16.211 29.525 1.00 17.58 ? 442 VAL A N 1 ATOM 3413 C CA . VAL A 1 442 ? -30.095 -16.247 29.323 1.00 18.90 ? 442 VAL A CA 1 ATOM 3414 C C . VAL A 1 442 ? -29.639 -17.649 29.723 1.00 18.50 ? 442 VAL A C 1 ATOM 3415 O O . VAL A 1 442 ? -29.480 -17.958 30.910 1.00 20.85 ? 442 VAL A O 1 ATOM 3416 C CB . VAL A 1 442 ? -29.357 -15.144 30.151 1.00 19.92 ? 442 VAL A CB 1 ATOM 3417 C CG1 . VAL A 1 442 ? -27.962 -14.904 29.585 1.00 19.41 ? 442 VAL A CG1 1 ATOM 3418 C CG2 . VAL A 1 442 ? -30.146 -13.839 30.146 1.00 19.85 ? 442 VAL A CG2 1 ATOM 3419 N N . LEU A 1 443 ? -29.482 -18.499 28.714 1.00 18.28 ? 443 LEU A N 1 ATOM 3420 C CA . LEU A 1 443 ? -29.096 -19.894 28.906 1.00 18.50 ? 443 LEU A CA 1 ATOM 3421 C C . LEU A 1 443 ? -27.633 -20.071 29.245 1.00 18.46 ? 443 LEU A C 1 ATOM 3422 O O . LEU A 1 443 ? -27.275 -20.924 30.058 1.00 18.05 ? 443 LEU A O 1 ATOM 3423 C CB . LEU A 1 443 ? -29.460 -20.716 27.667 1.00 20.13 ? 443 LEU A CB 1 ATOM 3424 C CG . LEU A 1 443 ? -30.899 -20.573 27.147 1.00 20.32 ? 443 LEU A CG 1 ATOM 3425 C CD1 . LEU A 1 443 ? -31.101 -21.477 25.967 1.00 19.84 ? 443 LEU A CD1 1 ATOM 3426 C CD2 . LEU A 1 443 ? -31.921 -20.913 28.226 1.00 21.12 ? 443 LEU A CD2 1 ATOM 3427 N N . GLY A 1 444 ? -26.802 -19.223 28.654 1.00 18.70 ? 444 GLY A N 1 ATOM 3428 C CA . GLY A 1 444 ? -25.383 -19.298 28.910 1.00 17.22 ? 444 GLY A CA 1 ATOM 3429 C C . GLY A 1 444 ? -24.571 -18.334 28.088 1.00 17.02 ? 444 GLY A C 1 ATOM 3430 O O . GLY A 1 444 ? -25.088 -17.635 27.216 1.00 17.00 ? 444 GLY A O 1 ATOM 3431 N N . ARG A 1 445 ? -23.284 -18.292 28.411 1.00 16.44 ? 445 ARG A N 1 ATOM 3432 C CA . ARG A 1 445 ? -22.313 -17.437 27.746 1.00 16.67 ? 445 ARG A CA 1 ATOM 3433 C C . ARG A 1 445 ? -20.947 -18.106 27.840 1.00 16.22 ? 445 ARG A C 1 ATOM 3434 O O . ARG A 1 445 ? -20.795 -19.125 28.516 1.00 16.77 ? 445 ARG A O 1 ATOM 3435 C CB . ARG A 1 445 ? -22.288 -16.029 28.376 1.00 17.00 ? 445 ARG A CB 1 ATOM 3436 C CG . ARG A 1 445 ? -22.080 -15.981 29.889 1.00 17.95 ? 445 ARG A CG 1 ATOM 3437 C CD . ARG A 1 445 ? -22.088 -14.554 30.401 1.00 19.38 ? 445 ARG A CD 1 ATOM 3438 N NE . ARG A 1 445 ? -21.710 -14.498 31.811 1.00 20.59 ? 445 ARG A NE 1 ATOM 3439 C CZ . ARG A 1 445 ? -22.078 -13.543 32.657 1.00 21.16 ? 445 ARG A CZ 1 ATOM 3440 N NH1 . ARG A 1 445 ? -22.850 -12.540 32.249 1.00 21.82 ? 445 ARG A NH1 1 ATOM 3441 N NH2 . ARG A 1 445 ? -21.691 -13.605 33.923 1.00 19.43 ? 445 ARG A NH2 1 ATOM 3442 N N . SER A 1 446 ? -19.966 -17.547 27.138 1.00 14.73 ? 446 SER A N 1 ATOM 3443 C CA . SER A 1 446 ? -18.594 -18.048 27.156 1.00 13.95 ? 446 SER A CA 1 ATOM 3444 C C . SER A 1 446 ? -17.988 -17.869 28.564 1.00 13.80 ? 446 SER A C 1 ATOM 3445 O O . SER A 1 446 ? -18.456 -17.002 29.316 1.00 12.48 ? 446 SER A O 1 ATOM 3446 C CB . SER A 1 446 ? -17.789 -17.305 26.095 1.00 12.62 ? 446 SER A CB 1 ATOM 3447 O OG . SER A 1 446 ? -18.051 -15.921 26.126 1.00 13.38 ? 446 SER A OG 1 ATOM 3448 N N . PRO A 1 447 ? -16.993 -18.709 28.960 1.00 13.45 ? 447 PRO A N 1 ATOM 3449 C CA . PRO A 1 447 ? -16.379 -18.594 30.295 1.00 14.07 ? 447 PRO A CA 1 ATOM 3450 C C . PRO A 1 447 ? -15.937 -17.187 30.710 1.00 15.56 ? 447 PRO A C 1 ATOM 3451 O O . PRO A 1 447 ? -15.232 -16.502 29.956 1.00 15.54 ? 447 PRO A O 1 ATOM 3452 C CB . PRO A 1 447 ? -15.193 -19.552 30.204 1.00 13.90 ? 447 PRO A CB 1 ATOM 3453 C CG . PRO A 1 447 ? -15.716 -20.636 29.345 1.00 14.28 ? 447 PRO A CG 1 ATOM 3454 C CD . PRO A 1 447 ? -16.397 -19.853 28.234 1.00 13.58 ? 447 PRO A CD 1 ATOM 3455 N N . ASP A 1 448 ? -16.406 -16.761 31.889 1.00 15.91 ? 448 ASP A N 1 ATOM 3456 C CA . ASP A 1 448 ? -16.100 -15.445 32.459 1.00 17.71 ? 448 ASP A CA 1 ATOM 3457 C C . ASP A 1 448 ? -14.592 -15.242 32.638 1.00 19.36 ? 448 ASP A C 1 ATOM 3458 O O . ASP A 1 448 ? -13.935 -15.963 33.395 1.00 21.04 ? 448 ASP A O 1 ATOM 3459 C CB . ASP A 1 448 ? -16.858 -15.238 33.783 1.00 17.97 ? 448 ASP A CB 1 ATOM 3460 C CG . ASP A 1 448 ? -18.383 -15.080 33.589 1.00 19.56 ? 448 ASP A CG 1 ATOM 3461 O OD1 . ASP A 1 448 ? -18.875 -15.073 32.436 1.00 19.44 ? 448 ASP A OD1 1 ATOM 3462 O OD2 . ASP A 1 448 ? -19.100 -14.940 34.601 1.00 20.20 ? 448 ASP A OD2 1 ATOM 3463 N N . VAL A 1 449 ? -14.054 -14.332 31.822 1.00 19.24 ? 449 VAL A N 1 ATOM 3464 C CA . VAL A 1 449 ? -12.628 -13.988 31.770 1.00 18.47 ? 449 VAL A CA 1 ATOM 3465 C C . VAL A 1 449 ? -12.455 -12.445 31.770 1.00 17.80 ? 449 VAL A C 1 ATOM 3466 O O . VAL A 1 449 ? -13.461 -11.736 31.723 1.00 16.52 ? 449 VAL A O 1 ATOM 3467 C CB . VAL A 1 449 ? -11.980 -14.605 30.455 1.00 20.18 ? 449 VAL A CB 1 ATOM 3468 C CG1 . VAL A 1 449 ? -11.860 -16.136 30.555 1.00 19.61 ? 449 VAL A CG1 1 ATOM 3469 C CG2 . VAL A 1 449 ? -12.762 -14.195 29.201 1.00 19.33 ? 449 VAL A CG2 1 ATOM 3470 N N . PRO A 1 450 ? -11.207 -11.908 31.954 1.00 18.72 ? 450 PRO A N 1 ATOM 3471 C CA . PRO A 1 450 ? -11.063 -10.444 31.927 1.00 19.15 ? 450 PRO A CA 1 ATOM 3472 C C . PRO A 1 450 ? -11.483 -9.811 30.597 1.00 19.20 ? 450 PRO A C 1 ATOM 3473 O O . PRO A 1 450 ? -11.047 -10.235 29.532 1.00 20.17 ? 450 PRO A O 1 ATOM 3474 C CB . PRO A 1 450 ? -9.586 -10.244 32.235 1.00 17.61 ? 450 PRO A CB 1 ATOM 3475 C CG . PRO A 1 450 ? -9.368 -11.259 33.256 1.00 18.86 ? 450 PRO A CG 1 ATOM 3476 C CD . PRO A 1 450 ? -10.021 -12.482 32.630 1.00 19.32 ? 450 PRO A CD 1 ATOM 3477 N N . ALA A 1 451 ? -12.355 -8.810 30.689 1.00 19.45 ? 451 ALA A N 1 ATOM 3478 C CA . ALA A 1 451 ? -12.935 -8.123 29.537 1.00 19.92 ? 451 ALA A CA 1 ATOM 3479 C C . ALA A 1 451 ? -12.033 -7.686 28.390 1.00 20.98 ? 451 ALA A C 1 ATOM 3480 O O . ALA A 1 451 ? -12.428 -7.805 27.235 1.00 24.15 ? 451 ALA A O 1 ATOM 3481 C CB . ALA A 1 451 ? -13.806 -6.977 29.999 1.00 18.06 ? 451 ALA A CB 1 ATOM 3482 N N . ALA A 1 452 ? -10.828 -7.213 28.696 1.00 22.19 ? 452 ALA A N 1 ATOM 3483 C CA . ALA A 1 452 ? -9.900 -6.783 27.656 1.00 22.06 ? 452 ALA A CA 1 ATOM 3484 C C . ALA A 1 452 ? -8.702 -7.721 27.541 1.00 21.24 ? 452 ALA A C 1 ATOM 3485 O O . ALA A 1 452 ? -7.612 -7.311 27.134 1.00 21.50 ? 452 ALA A O 1 ATOM 3486 C CB . ALA A 1 452 ? -9.454 -5.345 27.896 1.00 24.07 ? 452 ALA A CB 1 ATOM 3487 N N . SER A 1 453 ? -8.924 -8.994 27.863 1.00 21.55 ? 453 SER A N 1 ATOM 3488 C CA . SER A 1 453 ? -7.865 -10.001 27.791 1.00 23.85 ? 453 SER A CA 1 ATOM 3489 C C . SER A 1 453 ? -7.605 -10.514 26.387 1.00 25.57 ? 453 SER A C 1 ATOM 3490 O O . SER A 1 453 ? -6.508 -10.989 26.082 1.00 27.45 ? 453 SER A O 1 ATOM 3491 C CB . SER A 1 453 ? -8.138 -11.177 28.735 1.00 20.44 ? 453 SER A CB 1 ATOM 3492 O OG . SER A 1 453 ? -9.372 -11.808 28.457 1.00 20.68 ? 453 SER A OG 1 ATOM 3493 N N . GLN A 1 454 ? -8.619 -10.351 25.537 1.00 27.26 ? 454 GLN A N 1 ATOM 3494 C CA . GLN A 1 454 ? -8.634 -10.789 24.140 1.00 29.07 ? 454 GLN A CA 1 ATOM 3495 C C . GLN A 1 454 ? -8.630 -12.316 23.962 1.00 28.84 ? 454 GLN A C 1 ATOM 3496 O O . GLN A 1 454 ? -8.094 -12.855 22.988 1.00 29.17 ? 454 GLN A O 1 ATOM 3497 C CB . GLN A 1 454 ? -7.565 -10.063 23.292 1.00 29.89 ? 454 GLN A CB 1 ATOM 3498 C CG . GLN A 1 454 ? -7.826 -8.556 23.106 1.00 30.14 ? 454 GLN A CG 1 ATOM 3499 C CD . GLN A 1 454 ? -9.166 -8.248 22.441 1.00 31.57 ? 454 GLN A CD 1 ATOM 3500 O OE1 . GLN A 1 454 ? -9.570 -8.914 21.483 1.00 31.76 ? 454 GLN A OE1 1 ATOM 3501 N NE2 . GLN A 1 454 ? -9.870 -7.248 22.965 1.00 31.53 ? 454 GLN A NE2 1 ATOM 3502 N N . GLN A 1 455 ? -9.239 -12.994 24.938 1.00 28.77 ? 455 GLN A N 1 ATOM 3503 C CA . GLN A 1 455 ? -9.390 -14.447 24.938 1.00 27.51 ? 455 GLN A CA 1 ATOM 3504 C C . GLN A 1 455 ? -10.638 -14.712 24.125 1.00 26.97 ? 455 GLN A C 1 ATOM 3505 O O . GLN A 1 455 ? -11.635 -13.994 24.252 1.00 26.04 ? 455 GLN A O 1 ATOM 3506 C CB . GLN A 1 455 ? -9.565 -14.996 26.353 1.00 26.89 ? 455 GLN A CB 1 ATOM 3507 C CG . GLN A 1 455 ? -8.265 -15.206 27.081 1.00 26.10 ? 455 GLN A CG 1 ATOM 3508 C CD . GLN A 1 455 ? -8.454 -15.897 28.405 1.00 25.38 ? 455 GLN A CD 1 ATOM 3509 O OE1 . GLN A 1 455 ? -8.313 -17.113 28.510 1.00 25.04 ? 455 GLN A OE1 1 ATOM 3510 N NE2 . GLN A 1 455 ? -8.767 -15.124 29.430 1.00 25.51 ? 455 GLN A NE2 1 ATOM 3511 N N . ARG A 1 456 ? -10.538 -15.692 23.234 1.00 26.18 ? 456 ARG A N 1 ATOM 3512 C CA . ARG A 1 456 ? -11.626 -16.042 22.338 1.00 25.78 ? 456 ARG A CA 1 ATOM 3513 C C . ARG A 1 456 ? -12.213 -17.411 22.613 1.00 24.77 ? 456 ARG A C 1 ATOM 3514 O O . ARG A 1 456 ? -11.504 -18.346 23.004 1.00 22.74 ? 456 ARG A O 1 ATOM 3515 C CB . ARG A 1 456 ? -11.152 -15.985 20.876 1.00 27.80 ? 456 ARG A CB 1 ATOM 3516 C CG . ARG A 1 456 ? -10.343 -14.752 20.485 1.00 29.63 ? 456 ARG A CG 1 ATOM 3517 C CD . ARG A 1 456 ? -11.130 -13.460 20.624 1.00 32.56 ? 456 ARG A CD 1 ATOM 3518 N NE . ARG A 1 456 ? -10.288 -12.305 20.325 1.00 36.48 ? 456 ARG A NE 1 ATOM 3519 C CZ . ARG A 1 456 ? -10.381 -11.563 19.224 1.00 38.09 ? 456 ARG A CZ 1 ATOM 3520 N NH1 . ARG A 1 456 ? -11.294 -11.832 18.298 1.00 37.34 ? 456 ARG A NH1 1 ATOM 3521 N NH2 . ARG A 1 456 ? -9.512 -10.580 19.021 1.00 39.65 ? 456 ARG A NH2 1 ATOM 3522 N N . PHE A 1 457 ? -13.531 -17.500 22.438 1.00 24.20 ? 457 PHE A N 1 ATOM 3523 C CA . PHE A 1 457 ? -14.284 -18.739 22.621 1.00 24.16 ? 457 PHE A CA 1 ATOM 3524 C C . PHE A 1 457 ? -15.348 -18.871 21.528 1.00 22.78 ? 457 PHE A C 1 ATOM 3525 O O . PHE A 1 457 ? -16.072 -17.918 21.229 1.00 21.33 ? 457 PHE A O 1 ATOM 3526 C CB . PHE A 1 457 ? -14.991 -18.786 23.993 1.00 26.07 ? 457 PHE A CB 1 ATOM 3527 C CG . PHE A 1 457 ? -14.065 -18.696 25.182 1.00 26.95 ? 457 PHE A CG 1 ATOM 3528 C CD1 . PHE A 1 457 ? -13.337 -19.820 25.614 1.00 26.08 ? 457 PHE A CD1 1 ATOM 3529 C CD2 . PHE A 1 457 ? -13.911 -17.479 25.874 1.00 25.63 ? 457 PHE A CD2 1 ATOM 3530 C CE1 . PHE A 1 457 ? -12.460 -19.732 26.730 1.00 26.99 ? 457 PHE A CE1 1 ATOM 3531 C CE2 . PHE A 1 457 ? -13.040 -17.374 26.988 1.00 25.36 ? 457 PHE A CE2 1 ATOM 3532 C CZ . PHE A 1 457 ? -12.313 -18.500 27.417 1.00 24.89 ? 457 PHE A CZ 1 ATOM 3533 N N . VAL A 1 458 ? -15.377 -20.038 20.890 1.00 21.64 ? 458 VAL A N 1 ATOM 3534 C CA . VAL A 1 458 ? -16.366 -20.373 19.862 1.00 21.80 ? 458 VAL A CA 1 ATOM 3535 C C . VAL A 1 458 ? -17.141 -21.517 20.518 1.00 22.33 ? 458 VAL A C 1 ATOM 3536 O O . VAL A 1 458 ? -16.558 -22.299 21.273 1.00 23.53 ? 458 VAL A O 1 ATOM 3537 C CB . VAL A 1 458 ? -15.697 -20.869 18.528 1.00 21.13 ? 458 VAL A CB 1 ATOM 3538 C CG1 . VAL A 1 458 ? -16.753 -21.277 17.489 1.00 18.24 ? 458 VAL A CG1 1 ATOM 3539 C CG2 . VAL A 1 458 ? -14.815 -19.782 17.940 1.00 18.17 ? 458 VAL A CG2 1 ATOM 3540 N N . PHE A 1 459 ? -18.441 -21.607 20.243 1.00 23.35 ? 459 PHE A N 1 ATOM 3541 C CA . PHE A 1 459 ? -19.293 -22.657 20.810 1.00 24.90 ? 459 PHE A CA 1 ATOM 3542 C C . PHE A 1 459 ? -18.816 -24.057 20.396 1.00 25.12 ? 459 PHE A C 1 ATOM 3543 O O . PHE A 1 459 ? -18.788 -24.395 19.207 1.00 25.70 ? 459 PHE A O 1 ATOM 3544 C CB . PHE A 1 459 ? -20.763 -22.430 20.400 1.00 25.63 ? 459 PHE A CB 1 ATOM 3545 C CG . PHE A 1 459 ? -21.763 -23.277 21.163 1.00 27.14 ? 459 PHE A CG 1 ATOM 3546 C CD1 . PHE A 1 459 ? -22.296 -22.822 22.382 1.00 28.11 ? 459 PHE A CD1 1 ATOM 3547 C CD2 . PHE A 1 459 ? -22.190 -24.531 20.660 1.00 27.41 ? 459 PHE A CD2 1 ATOM 3548 C CE1 . PHE A 1 459 ? -23.244 -23.603 23.100 1.00 28.63 ? 459 PHE A CE1 1 ATOM 3549 C CE2 . PHE A 1 459 ? -23.132 -25.323 21.363 1.00 26.57 ? 459 PHE A CE2 1 ATOM 3550 C CZ . PHE A 1 459 ? -23.660 -24.859 22.585 1.00 28.48 ? 459 PHE A CZ 1 ATOM 3551 N N . ASP A 1 460 ? -18.389 -24.819 21.399 1.00 26.14 ? 460 ASP A N 1 ATOM 3552 C CA . ASP A 1 460 ? -17.908 -26.193 21.242 1.00 27.70 ? 460 ASP A CA 1 ATOM 3553 C C . ASP A 1 460 ? -18.921 -27.037 22.022 1.00 27.29 ? 460 ASP A C 1 ATOM 3554 O O . ASP A 1 460 ? -18.946 -26.985 23.250 1.00 26.25 ? 460 ASP A O 1 ATOM 3555 C CB . ASP A 1 460 ? -16.486 -26.334 21.831 1.00 29.27 ? 460 ASP A CB 1 ATOM 3556 C CG . ASP A 1 460 ? -15.886 -27.744 21.665 1.00 31.67 ? 460 ASP A CG 1 ATOM 3557 O OD1 . ASP A 1 460 ? -16.283 -28.499 20.743 1.00 33.80 ? 460 ASP A OD1 1 ATOM 3558 O OD2 . ASP A 1 460 ? -14.992 -28.091 22.468 1.00 32.32 ? 460 ASP A OD2 1 ATOM 3559 N N . PRO A 1 461 ? -19.774 -27.816 21.317 1.00 27.95 ? 461 PRO A N 1 ATOM 3560 C CA . PRO A 1 461 ? -20.799 -28.669 21.939 1.00 29.09 ? 461 PRO A CA 1 ATOM 3561 C C . PRO A 1 461 ? -20.299 -29.635 23.028 1.00 31.17 ? 461 PRO A C 1 ATOM 3562 O O . PRO A 1 461 ? -21.010 -29.889 24.007 1.00 30.90 ? 461 PRO A O 1 ATOM 3563 C CB . PRO A 1 461 ? -21.375 -29.431 20.743 1.00 28.38 ? 461 PRO A CB 1 ATOM 3564 C CG . PRO A 1 461 ? -21.222 -28.470 19.622 1.00 27.47 ? 461 PRO A CG 1 ATOM 3565 C CD . PRO A 1 461 ? -19.828 -27.952 19.847 1.00 27.73 ? 461 PRO A CD 1 ATOM 3566 N N . ALA A 1 462 ? -19.049 -30.085 22.877 1.00 31.76 ? 462 ALA A N 1 ATOM 3567 C CA . ALA A 1 462 ? -18.388 -31.028 23.785 1.00 34.25 ? 462 ALA A CA 1 ATOM 3568 C C . ALA A 1 462 ? -18.143 -30.534 25.216 1.00 35.71 ? 462 ALA A C 1 ATOM 3569 O O . ALA A 1 462 ? -18.094 -31.338 26.155 1.00 36.95 ? 462 ALA A O 1 ATOM 3570 C CB . ALA A 1 462 ? -17.074 -31.509 23.164 1.00 34.95 ? 462 ALA A CB 1 ATOM 3571 N N . VAL A 1 463 ? -17.970 -29.223 25.376 1.00 36.37 ? 463 VAL A N 1 ATOM 3572 C CA . VAL A 1 463 ? -17.737 -28.629 26.693 1.00 35.99 ? 463 VAL A CA 1 ATOM 3573 C C . VAL A 1 463 ? -18.793 -27.603 27.099 1.00 34.34 ? 463 VAL A C 1 ATOM 3574 O O . VAL A 1 463 ? -18.985 -27.366 28.290 1.00 34.69 ? 463 VAL A O 1 ATOM 3575 C CB . VAL A 1 463 ? -16.323 -27.958 26.804 1.00 37.80 ? 463 VAL A CB 1 ATOM 3576 C CG1 . VAL A 1 463 ? -15.217 -29.014 26.867 1.00 38.67 ? 463 VAL A CG1 1 ATOM 3577 C CG2 . VAL A 1 463 ? -16.076 -27.008 25.639 1.00 38.99 ? 463 VAL A CG2 1 ATOM 3578 N N . ASP A 1 464 ? -19.504 -27.046 26.115 1.00 33.29 ? 464 ASP A N 1 ATOM 3579 C CA . ASP A 1 464 ? -20.510 -25.997 26.352 1.00 32.79 ? 464 ASP A CA 1 ATOM 3580 C C . ASP A 1 464 ? -21.973 -26.358 26.608 1.00 32.39 ? 464 ASP A C 1 ATOM 3581 O O . ASP A 1 464 ? -22.669 -25.607 27.296 1.00 31.40 ? 464 ASP A O 1 ATOM 3582 C CB . ASP A 1 464 ? -20.443 -24.947 25.247 1.00 32.29 ? 464 ASP A CB 1 ATOM 3583 C CG . ASP A 1 464 ? -19.091 -24.259 25.170 1.00 33.23 ? 464 ASP A CG 1 ATOM 3584 O OD1 . ASP A 1 464 ? -18.524 -23.922 26.233 1.00 31.79 ? 464 ASP A OD1 1 ATOM 3585 O OD2 . ASP A 1 464 ? -18.614 -24.027 24.037 1.00 33.36 ? 464 ASP A OD2 1 ATOM 3586 N N . LEU A 1 465 ? -22.444 -27.477 26.052 1.00 32.67 ? 465 LEU A N 1 ATOM 3587 C CA . LEU A 1 465 ? -23.832 -27.925 26.237 1.00 33.05 ? 465 LEU A CA 1 ATOM 3588 C C . LEU A 1 465 ? -24.173 -28.243 27.688 1.00 33.05 ? 465 LEU A C 1 ATOM 3589 O O . LEU A 1 465 ? -25.337 -28.161 28.094 1.00 33.95 ? 465 LEU A O 1 ATOM 3590 C CB . LEU A 1 465 ? -24.149 -29.131 25.352 1.00 33.92 ? 465 LEU A CB 1 ATOM 3591 C CG . LEU A 1 465 ? -24.498 -28.860 23.882 1.00 34.94 ? 465 LEU A CG 1 ATOM 3592 C CD1 . LEU A 1 465 ? -24.462 -30.158 23.110 1.00 34.24 ? 465 LEU A CD1 1 ATOM 3593 C CD2 . LEU A 1 465 ? -25.859 -28.194 23.744 1.00 35.23 ? 465 LEU A CD2 1 ATOM 3594 N N . ALA A 1 466 ? -23.131 -28.556 28.459 1.00 31.93 ? 466 ALA A N 1 ATOM 3595 C CA . ALA A 1 466 ? -23.233 -28.873 29.880 1.00 31.55 ? 466 ALA A CA 1 ATOM 3596 C C . ALA A 1 466 ? -23.261 -27.589 30.716 1.00 31.08 ? 466 ALA A C 1 ATOM 3597 O O . ALA A 1 466 ? -23.891 -27.543 31.777 1.00 32.11 ? 466 ALA A O 1 ATOM 3598 C CB . ALA A 1 466 ? -22.056 -29.753 30.298 1.00 31.43 ? 466 ALA A CB 1 ATOM 3599 N N . ARG A 1 467 ? -22.618 -26.543 30.192 1.00 30.21 ? 467 ARG A N 1 ATOM 3600 C CA . ARG A 1 467 ? -22.527 -25.231 30.837 1.00 29.46 ? 467 ARG A CA 1 ATOM 3601 C C . ARG A 1 467 ? -23.804 -24.388 30.789 1.00 29.64 ? 467 ARG A C 1 ATOM 3602 O O . ARG A 1 467 ? -23.918 -23.378 31.490 1.00 30.86 ? 467 ARG A O 1 ATOM 3603 C CB . ARG A 1 467 ? -21.375 -24.434 30.233 1.00 28.89 ? 467 ARG A CB 1 ATOM 3604 C CG . ARG A 1 467 ? -19.987 -24.901 30.640 1.00 28.26 ? 467 ARG A CG 1 ATOM 3605 C CD . ARG A 1 467 ? -18.892 -23.957 30.149 1.00 28.61 ? 467 ARG A CD 1 ATOM 3606 N NE . ARG A 1 467 ? -18.962 -22.634 30.779 1.00 28.23 ? 467 ARG A NE 1 ATOM 3607 C CZ . ARG A 1 467 ? -19.349 -21.516 30.167 1.00 28.42 ? 467 ARG A CZ 1 ATOM 3608 N NH1 . ARG A 1 467 ? -19.708 -21.537 28.885 1.00 26.64 ? 467 ARG A NH1 1 ATOM 3609 N NH2 . ARG A 1 467 ? -19.414 -20.380 30.849 1.00 29.25 ? 467 ARG A NH2 1 ATOM 3610 N N . LEU A 1 468 ? -24.763 -24.817 29.972 1.00 29.32 ? 468 LEU A N 1 ATOM 3611 C CA . LEU A 1 468 ? -26.040 -24.125 29.814 1.00 26.82 ? 468 LEU A CA 1 ATOM 3612 C C . LEU A 1 468 ? -27.030 -24.490 30.908 1.00 27.20 ? 468 LEU A C 1 ATOM 3613 O O . LEU A 1 468 ? -26.929 -25.559 31.517 1.00 27.23 ? 468 LEU A O 1 ATOM 3614 C CB . LEU A 1 468 ? -26.657 -24.462 28.462 1.00 24.25 ? 468 LEU A CB 1 ATOM 3615 C CG . LEU A 1 468 ? -25.805 -24.287 27.212 1.00 23.78 ? 468 LEU A CG 1 ATOM 3616 C CD1 . LEU A 1 468 ? -26.496 -24.954 26.046 1.00 25.36 ? 468 LEU A CD1 1 ATOM 3617 C CD2 . LEU A 1 468 ? -25.522 -22.820 26.941 1.00 23.74 ? 468 LEU A CD2 1 ATOM 3618 N N . ASN A 1 469 ? -27.984 -23.595 31.149 1.00 26.91 ? 469 ASN A N 1 ATOM 3619 C CA . ASN A 1 469 ? -29.007 -23.811 32.157 1.00 27.59 ? 469 ASN A CA 1 ATOM 3620 C C . ASN A 1 469 ? -30.385 -23.486 31.594 1.00 27.81 ? 469 ASN A C 1 ATOM 3621 O O . ASN A 1 469 ? -30.603 -22.408 31.034 1.00 28.27 ? 469 ASN A O 1 ATOM 3622 C CB . ASN A 1 469 ? -28.724 -22.970 33.411 1.00 29.65 ? 469 ASN A CB 1 ATOM 3623 C CG . ASN A 1 469 ? -29.655 -23.305 34.571 1.00 30.09 ? 469 ASN A CG 1 ATOM 3624 O OD1 . ASN A 1 469 ? -29.905 -24.474 34.866 1.00 31.67 ? 469 ASN A OD1 1 ATOM 3625 N ND2 . ASN A 1 469 ? -30.176 -22.273 35.226 1.00 31.40 ? 469 ASN A ND2 1 ATOM 3626 N N . GLY A 1 470 ? -31.298 -24.441 31.757 1.00 27.00 ? 470 GLY A N 1 ATOM 3627 C CA . GLY A 1 470 ? -32.665 -24.288 31.298 1.00 24.97 ? 470 GLY A CA 1 ATOM 3628 C C . GLY A 1 470 ? -33.678 -24.409 32.417 1.00 23.46 ? 470 GLY A C 1 ATOM 3629 O O . GLY A 1 470 ? -34.875 -24.497 32.155 1.00 25.21 ? 470 GLY A O 1 ATOM 3630 N N . ASP A 1 471 ? -33.188 -24.424 33.655 1.00 22.74 ? 471 ASP A N 1 ATOM 3631 C CA . ASP A 1 471 ? -34.021 -24.527 34.849 1.00 21.51 ? 471 ASP A CA 1 ATOM 3632 C C . ASP A 1 471 ? -33.983 -23.182 35.572 1.00 19.95 ? 471 ASP A C 1 ATOM 3633 O O . ASP A 1 471 ? -33.045 -22.877 36.321 1.00 18.50 ? 471 ASP A O 1 ATOM 3634 C CB . ASP A 1 471 ? -33.529 -25.664 35.754 1.00 24.58 ? 471 ASP A CB 1 ATOM 3635 C CG . ASP A 1 471 ? -34.449 -25.914 36.945 1.00 27.11 ? 471 ASP A CG 1 ATOM 3636 O OD1 . ASP A 1 471 ? -35.677 -25.715 36.807 1.00 30.70 ? 471 ASP A OD1 1 ATOM 3637 O OD2 . ASP A 1 471 ? -33.942 -26.306 38.019 1.00 27.97 ? 471 ASP A OD2 1 ATOM 3638 N N . ASN A 1 472 ? -35.038 -22.403 35.323 1.00 18.46 ? 472 ASN A N 1 ATOM 3639 C CA . ASN A 1 472 ? -35.257 -21.046 35.832 1.00 16.07 ? 472 ASN A CA 1 ATOM 3640 C C . ASN A 1 472 ? -34.056 -20.115 35.605 1.00 15.51 ? 472 ASN A C 1 ATOM 3641 O O . ASN A 1 472 ? -33.508 -19.550 36.558 1.00 13.50 ? 472 ASN A O 1 ATOM 3642 C CB . ASN A 1 472 ? -35.728 -21.043 37.299 1.00 19.25 ? 472 ASN A CB 1 ATOM 3643 C CG . ASN A 1 472 ? -36.464 -19.750 37.679 1.00 21.01 ? 472 ASN A CG 1 ATOM 3644 O OD1 . ASN A 1 472 ? -36.935 -19.009 36.808 1.00 20.15 ? 472 ASN A OD1 1 ATOM 3645 N ND2 . ASN A 1 472 ? -36.572 -19.482 38.978 1.00 20.14 ? 472 ASN A ND2 1 ATOM 3646 N N . PRO A 1 473 ? -33.642 -19.930 34.325 1.00 14.80 ? 473 PRO A N 1 ATOM 3647 C CA . PRO A 1 473 ? -32.504 -19.058 34.042 1.00 13.05 ? 473 PRO A CA 1 ATOM 3648 C C . PRO A 1 473 ? -32.901 -17.575 34.130 1.00 13.12 ? 473 PRO A C 1 ATOM 3649 O O . PRO A 1 473 ? -34.106 -17.263 34.201 1.00 13.17 ? 473 PRO A O 1 ATOM 3650 C CB . PRO A 1 473 ? -32.130 -19.476 32.618 1.00 13.18 ? 473 PRO A CB 1 ATOM 3651 C CG . PRO A 1 473 ? -33.410 -19.767 32.006 1.00 12.47 ? 473 PRO A CG 1 ATOM 3652 C CD . PRO A 1 473 ? -34.176 -20.495 33.062 1.00 15.03 ? 473 PRO A CD 1 ATOM 3653 N N . PRO A 1 474 ? -31.909 -16.654 34.209 1.00 11.23 ? 474 PRO A N 1 ATOM 3654 C CA . PRO A 1 474 ? -32.209 -15.220 34.279 1.00 12.38 ? 474 PRO A CA 1 ATOM 3655 C C . PRO A 1 474 ? -33.096 -14.783 33.117 1.00 14.54 ? 474 PRO A C 1 ATOM 3656 O O . PRO A 1 474 ? -32.828 -15.120 31.959 1.00 16.72 ? 474 PRO A O 1 ATOM 3657 C CB . PRO A 1 474 ? -30.831 -14.583 34.149 1.00 12.17 ? 474 PRO A CB 1 ATOM 3658 C CG . PRO A 1 474 ? -29.985 -15.531 34.847 1.00 13.01 ? 474 PRO A CG 1 ATOM 3659 C CD . PRO A 1 474 ? -30.461 -16.875 34.413 1.00 11.69 ? 474 PRO A CD 1 ATOM 3660 N N . ARG A 1 475 ? -34.206 -14.143 33.454 1.00 14.78 ? 475 ARG A N 1 ATOM 3661 C CA . ARG A 1 475 ? -35.137 -13.656 32.459 1.00 15.24 ? 475 ARG A CA 1 ATOM 3662 C C . ARG A 1 475 ? -35.112 -12.139 32.524 1.00 14.80 ? 475 ARG A C 1 ATOM 3663 O O . ARG A 1 475 ? -35.323 -11.559 33.583 1.00 14.72 ? 475 ARG A O 1 ATOM 3664 C CB . ARG A 1 475 ? -36.545 -14.211 32.708 1.00 14.82 ? 475 ARG A CB 1 ATOM 3665 C CG . ARG A 1 475 ? -37.516 -14.054 31.536 1.00 14.55 ? 475 ARG A CG 1 ATOM 3666 C CD . ARG A 1 475 ? -38.847 -14.786 31.745 1.00 11.80 ? 475 ARG A CD 1 ATOM 3667 N NE . ARG A 1 475 ? -39.611 -14.297 32.895 1.00 13.04 ? 475 ARG A NE 1 ATOM 3668 C CZ . ARG A 1 475 ? -39.786 -14.972 34.033 1.00 13.64 ? 475 ARG A CZ 1 ATOM 3669 N NH1 . ARG A 1 475 ? -39.252 -16.176 34.197 1.00 11.42 ? 475 ARG A NH1 1 ATOM 3670 N NH2 . ARG A 1 475 ? -40.491 -14.434 35.016 1.00 16.06 ? 475 ARG A NH2 1 ATOM 3671 N N . ARG A 1 476 ? -34.738 -11.515 31.409 1.00 13.60 ? 476 ARG A N 1 ATOM 3672 C CA . ARG A 1 476 ? -34.661 -10.063 31.316 1.00 13.04 ? 476 ARG A CA 1 ATOM 3673 C C . ARG A 1 476 ? -34.614 -9.604 29.862 1.00 13.28 ? 476 ARG A C 1 ATOM 3674 O O . ARG A 1 476 ? -34.584 -10.427 28.947 1.00 13.03 ? 476 ARG A O 1 ATOM 3675 C CB . ARG A 1 476 ? -33.469 -9.523 32.130 1.00 12.03 ? 476 ARG A CB 1 ATOM 3676 C CG . ARG A 1 476 ? -32.086 -10.057 31.790 1.00 9.29 ? 476 ARG A CG 1 ATOM 3677 C CD . ARG A 1 476 ? -31.122 -9.814 32.945 1.00 9.13 ? 476 ARG A CD 1 ATOM 3678 N NE . ARG A 1 476 ? -31.191 -8.432 33.440 1.00 10.34 ? 476 ARG A NE 1 ATOM 3679 C CZ . ARG A 1 476 ? -30.367 -7.890 34.335 1.00 6.68 ? 476 ARG A CZ 1 ATOM 3680 N NH1 . ARG A 1 476 ? -29.372 -8.588 34.864 1.00 9.24 ? 476 ARG A NH1 1 ATOM 3681 N NH2 . ARG A 1 476 ? -30.553 -6.640 34.720 1.00 8.10 ? 476 ARG A NH2 1 ATOM 3682 N N . ASP A 1 477 ? -34.646 -8.291 29.657 1.00 12.40 ? 477 ASP A N 1 ATOM 3683 C CA . ASP A 1 477 ? -34.631 -7.725 28.320 1.00 11.74 ? 477 ASP A CA 1 ATOM 3684 C C . ASP A 1 477 ? -33.257 -7.264 27.873 1.00 10.45 ? 477 ASP A C 1 ATOM 3685 O O . ASP A 1 477 ? -33.076 -6.935 26.701 1.00 11.63 ? 477 ASP A O 1 ATOM 3686 C CB . ASP A 1 477 ? -35.671 -6.589 28.190 1.00 13.15 ? 477 ASP A CB 1 ATOM 3687 C CG . ASP A 1 477 ? -35.462 -5.458 29.198 1.00 14.00 ? 477 ASP A CG 1 ATOM 3688 O OD1 . ASP A 1 477 ? -34.446 -4.735 29.120 1.00 13.81 ? 477 ASP A OD1 1 ATOM 3689 O OD2 . ASP A 1 477 ? -36.336 -5.275 30.059 1.00 17.40 ? 477 ASP A OD2 1 ATOM 3690 N N . THR A 1 478 ? -32.300 -7.245 28.805 1.00 9.54 ? 478 THR A N 1 ATOM 3691 C CA . THR A 1 478 ? -30.923 -6.818 28.526 1.00 8.50 ? 478 THR A CA 1 ATOM 3692 C C . THR A 1 478 ? -29.885 -7.643 29.281 1.00 7.00 ? 478 THR A C 1 ATOM 3693 O O . THR A 1 478 ? -30.003 -7.848 30.493 1.00 5.74 ? 478 THR A O 1 ATOM 3694 C CB . THR A 1 478 ? -30.704 -5.326 28.879 1.00 9.83 ? 478 THR A CB 1 ATOM 3695 O OG1 . THR A 1 478 ? -31.834 -4.557 28.458 1.00 15.09 ? 478 THR A OG1 1 ATOM 3696 C CG2 . THR A 1 478 ? -29.463 -4.776 28.190 1.00 11.44 ? 478 THR A CG2 1 ATOM 3697 N N . THR A 1 479 ? -28.847 -8.066 28.558 1.00 5.22 ? 479 THR A N 1 ATOM 3698 C CA . THR A 1 479 ? -27.739 -8.846 29.120 1.00 3.80 ? 479 THR A CA 1 ATOM 3699 C C . THR A 1 479 ? -26.472 -8.643 28.284 1.00 6.66 ? 479 THR A C 1 ATOM 3700 O O . THR A 1 479 ? -26.545 -8.229 27.120 1.00 7.86 ? 479 THR A O 1 ATOM 3701 C CB . THR A 1 479 ? -28.087 -10.379 29.263 1.00 4.80 ? 479 THR A CB 1 ATOM 3702 O OG1 . THR A 1 479 ? -27.206 -10.987 30.218 1.00 6.08 ? 479 THR A OG1 1 ATOM 3703 C CG2 . THR A 1 479 ? -27.973 -11.129 27.933 1.00 1.26 ? 479 THR A CG2 1 ATOM 3704 N N . MET A 1 480 ? -25.329 -9.038 28.842 1.00 6.05 ? 480 MET A N 1 ATOM 3705 C CA . MET A 1 480 ? -24.045 -8.874 28.175 1.00 6.75 ? 480 MET A CA 1 ATOM 3706 C C . MET A 1 480 ? -23.568 -9.967 27.247 1.00 9.90 ? 480 MET A C 1 ATOM 3707 O O . MET A 1 480 ? -23.605 -11.149 27.588 1.00 12.53 ? 480 MET A O 1 ATOM 3708 C CB . MET A 1 480 ? -22.929 -8.625 29.200 1.00 8.56 ? 480 MET A CB 1 ATOM 3709 C CG . MET A 1 480 ? -23.035 -7.318 29.968 1.00 6.97 ? 480 MET A CG 1 ATOM 3710 S SD . MET A 1 480 ? -23.187 -5.890 28.916 1.00 11.09 ? 480 MET A SD 1 ATOM 3711 C CE . MET A 1 480 ? -21.534 -5.714 28.352 1.00 6.55 ? 480 MET A CE 1 ATOM 3712 N N . LEU A 1 481 ? -23.129 -9.557 26.061 1.00 8.95 ? 481 LEU A N 1 ATOM 3713 C CA . LEU A 1 481 ? -22.533 -10.469 25.099 1.00 10.61 ? 481 LEU A CA 1 ATOM 3714 C C . LEU A 1 481 ? -21.059 -10.213 25.423 1.00 10.70 ? 481 LEU A C 1 ATOM 3715 O O . LEU A 1 481 ? -20.549 -9.105 25.222 1.00 13.43 ? 481 LEU A O 1 ATOM 3716 C CB . LEU A 1 481 ? -22.885 -10.086 23.658 1.00 12.10 ? 481 LEU A CB 1 ATOM 3717 C CG . LEU A 1 481 ? -22.099 -10.655 22.471 1.00 14.63 ? 481 LEU A CG 1 ATOM 3718 C CD1 . LEU A 1 481 ? -22.228 -12.152 22.334 1.00 13.97 ? 481 LEU A CD1 1 ATOM 3719 C CD2 . LEU A 1 481 ? -22.529 -9.970 21.202 1.00 16.00 ? 481 LEU A CD2 1 ATOM 3720 N N . PRO A 1 482 ? -20.385 -11.200 26.028 1.00 10.13 ? 482 PRO A N 1 ATOM 3721 C CA . PRO A 1 482 ? -18.973 -11.033 26.386 1.00 9.85 ? 482 PRO A CA 1 ATOM 3722 C C . PRO A 1 482 ? -18.006 -10.838 25.228 1.00 10.32 ? 482 PRO A C 1 ATOM 3723 O O . PRO A 1 482 ? -18.201 -11.397 24.138 1.00 9.94 ? 482 PRO A O 1 ATOM 3724 C CB . PRO A 1 482 ? -18.671 -12.304 27.163 1.00 12.03 ? 482 PRO A CB 1 ATOM 3725 C CG . PRO A 1 482 ? -19.603 -13.307 26.553 1.00 10.45 ? 482 PRO A CG 1 ATOM 3726 C CD . PRO A 1 482 ? -20.864 -12.551 26.375 1.00 9.97 ? 482 PRO A CD 1 ATOM 3727 N N . ALA A 1 483 ? -16.978 -10.024 25.475 1.00 8.35 ? 483 ALA A N 1 ATOM 3728 C CA . ALA A 1 483 ? -15.937 -9.743 24.493 1.00 8.63 ? 483 ALA A CA 1 ATOM 3729 C C . ALA A 1 483 ? -15.251 -11.035 24.063 1.00 9.60 ? 483 ALA A C 1 ATOM 3730 O O . ALA A 1 483 ? -14.879 -11.851 24.917 1.00 7.43 ? 483 ALA A O 1 ATOM 3731 C CB . ALA A 1 483 ? -14.918 -8.798 25.077 1.00 10.32 ? 483 ALA A CB 1 ATOM 3732 N N . GLY A 1 484 ? -15.229 -11.254 22.743 1.00 9.16 ? 484 GLY A N 1 ATOM 3733 C CA . GLY A 1 484 ? -14.594 -12.415 22.135 1.00 7.50 ? 484 GLY A CA 1 ATOM 3734 C C . GLY A 1 484 ? -15.308 -13.744 22.239 1.00 8.94 ? 484 GLY A C 1 ATOM 3735 O O . GLY A 1 484 ? -14.833 -14.742 21.707 1.00 8.61 ? 484 GLY A O 1 ATOM 3736 N N . GLY A 1 485 ? -16.473 -13.743 22.873 1.00 10.97 ? 485 GLY A N 1 ATOM 3737 C CA . GLY A 1 485 ? -17.201 -14.979 23.063 1.00 12.13 ? 485 GLY A CA 1 ATOM 3738 C C . GLY A 1 485 ? -18.530 -15.178 22.384 1.00 12.82 ? 485 GLY A C 1 ATOM 3739 O O . GLY A 1 485 ? -18.697 -14.868 21.202 1.00 11.80 ? 485 GLY A O 1 ATOM 3740 N N . TRP A 1 486 ? -19.447 -15.777 23.140 1.00 13.39 ? 486 TRP A N 1 ATOM 3741 C CA . TRP A 1 486 ? -20.792 -16.083 22.673 1.00 14.08 ? 486 TRP A CA 1 ATOM 3742 C C . TRP A 1 486 ? -21.869 -15.904 23.744 1.00 14.43 ? 486 TRP A C 1 ATOM 3743 O O . TRP A 1 486 ? -21.571 -15.805 24.939 1.00 14.93 ? 486 TRP A O 1 ATOM 3744 C CB . TRP A 1 486 ? -20.856 -17.503 22.068 1.00 14.69 ? 486 TRP A CB 1 ATOM 3745 C CG . TRP A 1 486 ? -20.321 -18.610 22.940 1.00 15.36 ? 486 TRP A CG 1 ATOM 3746 C CD1 . TRP A 1 486 ? -19.036 -19.053 22.991 1.00 14.90 ? 486 TRP A CD1 1 ATOM 3747 C CD2 . TRP A 1 486 ? -21.053 -19.383 23.905 1.00 16.58 ? 486 TRP A CD2 1 ATOM 3748 N NE1 . TRP A 1 486 ? -18.908 -20.045 23.937 1.00 17.00 ? 486 TRP A NE1 1 ATOM 3749 C CE2 . TRP A 1 486 ? -20.129 -20.268 24.515 1.00 17.19 ? 486 TRP A CE2 1 ATOM 3750 C CE3 . TRP A 1 486 ? -22.402 -19.412 24.322 1.00 17.72 ? 486 TRP A CE3 1 ATOM 3751 C CZ2 . TRP A 1 486 ? -20.506 -21.176 25.532 1.00 17.58 ? 486 TRP A CZ2 1 ATOM 3752 C CZ3 . TRP A 1 486 ? -22.784 -20.326 25.341 1.00 18.96 ? 486 TRP A CZ3 1 ATOM 3753 C CH2 . TRP A 1 486 ? -21.829 -21.193 25.931 1.00 16.81 ? 486 TRP A CH2 1 ATOM 3754 N N . LEU A 1 487 ? -23.121 -15.888 23.298 1.00 14.43 ? 487 LEU A N 1 ATOM 3755 C CA . LEU A 1 487 ? -24.276 -15.732 24.181 1.00 14.85 ? 487 LEU A CA 1 ATOM 3756 C C . LEU A 1 487 ? -25.454 -16.529 23.637 1.00 12.56 ? 487 LEU A C 1 ATOM 3757 O O . LEU A 1 487 ? -25.826 -16.356 22.471 1.00 11.67 ? 487 LEU A O 1 ATOM 3758 C CB . LEU A 1 487 ? -24.659 -14.251 24.282 1.00 14.23 ? 487 LEU A CB 1 ATOM 3759 C CG . LEU A 1 487 ? -25.749 -13.801 25.244 1.00 14.71 ? 487 LEU A CG 1 ATOM 3760 C CD1 . LEU A 1 487 ? -25.362 -14.060 26.695 1.00 13.33 ? 487 LEU A CD1 1 ATOM 3761 C CD2 . LEU A 1 487 ? -26.010 -12.326 24.998 1.00 16.22 ? 487 LEU A CD2 1 ATOM 3762 N N . LEU A 1 488 ? -26.009 -17.414 24.472 1.00 12.06 ? 488 LEU A N 1 ATOM 3763 C CA . LEU A 1 488 ? -27.169 -18.225 24.078 1.00 11.95 ? 488 LEU A CA 1 ATOM 3764 C C . LEU A 1 488 ? -28.444 -17.725 24.760 1.00 10.46 ? 488 LEU A C 1 ATOM 3765 O O . LEU A 1 488 ? -28.590 -17.792 25.993 1.00 10.69 ? 488 LEU A O 1 ATOM 3766 C CB . LEU A 1 488 ? -26.947 -19.734 24.330 1.00 11.87 ? 488 LEU A CB 1 ATOM 3767 C CG . LEU A 1 488 ? -28.016 -20.665 23.719 1.00 14.32 ? 488 LEU A CG 1 ATOM 3768 C CD1 . LEU A 1 488 ? -28.068 -20.544 22.217 1.00 15.47 ? 488 LEU A CD1 1 ATOM 3769 C CD2 . LEU A 1 488 ? -27.784 -22.097 24.078 1.00 15.28 ? 488 LEU A CD2 1 ATOM 3770 N N . LEU A 1 489 ? -29.339 -17.177 23.940 1.00 8.80 ? 489 LEU A N 1 ATOM 3771 C CA . LEU A 1 489 ? -30.611 -16.631 24.412 1.00 7.96 ? 489 LEU A CA 1 ATOM 3772 C C . LEU A 1 489 ? -31.803 -17.443 23.942 1.00 8.10 ? 489 LEU A C 1 ATOM 3773 O O . LEU A 1 489 ? -31.671 -18.250 23.026 1.00 9.12 ? 489 LEU A O 1 ATOM 3774 C CB . LEU A 1 489 ? -30.777 -15.174 23.964 1.00 6.63 ? 489 LEU A CB 1 ATOM 3775 C CG . LEU A 1 489 ? -29.721 -14.161 24.432 1.00 6.83 ? 489 LEU A CG 1 ATOM 3776 C CD1 . LEU A 1 489 ? -30.037 -12.805 23.886 1.00 2.78 ? 489 LEU A CD1 1 ATOM 3777 C CD2 . LEU A 1 489 ? -29.616 -14.115 25.964 1.00 5.79 ? 489 LEU A CD2 1 ATOM 3778 N N . ALA A 1 490 ? -32.959 -17.224 24.575 1.00 6.86 ? 490 ALA A N 1 ATOM 3779 C CA . ALA A 1 490 ? -34.186 -17.921 24.216 1.00 8.34 ? 490 ALA A CA 1 ATOM 3780 C C . ALA A 1 490 ? -35.428 -17.128 24.551 1.00 8.59 ? 490 ALA A C 1 ATOM 3781 O O . ALA A 1 490 ? -35.543 -16.594 25.641 1.00 11.13 ? 490 ALA A O 1 ATOM 3782 C CB . ALA A 1 490 ? -34.252 -19.289 24.886 1.00 7.49 ? 490 ALA A CB 1 ATOM 3783 N N . PHE A 1 491 ? -36.352 -17.040 23.598 1.00 11.01 ? 491 PHE A N 1 ATOM 3784 C CA . PHE A 1 491 ? -37.612 -16.339 23.813 1.00 10.25 ? 491 PHE A CA 1 ATOM 3785 C C . PHE A 1 491 ? -38.796 -17.067 23.184 1.00 12.04 ? 491 PHE A C 1 ATOM 3786 O O . PHE A 1 491 ? -38.685 -17.628 22.087 1.00 12.63 ? 491 PHE A O 1 ATOM 3787 C CB . PHE A 1 491 ? -37.539 -14.851 23.397 1.00 9.40 ? 491 PHE A CB 1 ATOM 3788 C CG . PHE A 1 491 ? -37.429 -14.600 21.903 1.00 11.10 ? 491 PHE A CG 1 ATOM 3789 C CD1 . PHE A 1 491 ? -36.176 -14.571 21.268 1.00 10.60 ? 491 PHE A CD1 1 ATOM 3790 C CD2 . PHE A 1 491 ? -38.583 -14.320 21.135 1.00 8.23 ? 491 PHE A CD2 1 ATOM 3791 C CE1 . PHE A 1 491 ? -36.074 -14.260 19.877 1.00 10.61 ? 491 PHE A CE1 1 ATOM 3792 C CE2 . PHE A 1 491 ? -38.494 -14.012 19.751 1.00 9.01 ? 491 PHE A CE2 1 ATOM 3793 C CZ . PHE A 1 491 ? -37.235 -13.981 19.121 1.00 9.37 ? 491 PHE A CZ 1 ATOM 3794 N N . ARG A 1 492 ? -39.916 -17.089 23.903 1.00 13.53 ? 492 ARG A N 1 ATOM 3795 C CA . ARG A 1 492 ? -41.131 -17.733 23.408 1.00 16.66 ? 492 ARG A CA 1 ATOM 3796 C C . ARG A 1 492 ? -41.807 -16.766 22.450 1.00 14.88 ? 492 ARG A C 1 ATOM 3797 O O . ARG A 1 492 ? -42.025 -15.612 22.797 1.00 15.38 ? 492 ARG A O 1 ATOM 3798 C CB . ARG A 1 492 ? -42.066 -18.106 24.568 1.00 19.40 ? 492 ARG A CB 1 ATOM 3799 C CG . ARG A 1 492 ? -43.161 -19.079 24.172 1.00 24.68 ? 492 ARG A CG 1 ATOM 3800 C CD . ARG A 1 492 ? -43.793 -19.757 25.368 1.00 29.28 ? 492 ARG A CD 1 ATOM 3801 N NE . ARG A 1 492 ? -44.755 -20.764 24.927 1.00 33.50 ? 492 ARG A NE 1 ATOM 3802 C CZ . ARG A 1 492 ? -45.289 -21.709 25.698 1.00 36.01 ? 492 ARG A CZ 1 ATOM 3803 N NH1 . ARG A 1 492 ? -44.964 -21.806 26.985 1.00 36.43 ? 492 ARG A NH1 1 ATOM 3804 N NH2 . ARG A 1 492 ? -46.160 -22.561 25.172 1.00 36.17 ? 492 ARG A NH2 1 ATOM 3805 N N . THR A 1 493 ? -42.103 -17.235 21.241 1.00 14.61 ? 493 THR A N 1 ATOM 3806 C CA . THR A 1 493 ? -42.738 -16.408 20.218 1.00 13.13 ? 493 THR A CA 1 ATOM 3807 C C . THR A 1 493 ? -44.226 -16.135 20.487 1.00 14.39 ? 493 THR A C 1 ATOM 3808 O O . THR A 1 493 ? -45.089 -16.562 19.724 1.00 16.28 ? 493 THR A O 1 ATOM 3809 C CB . THR A 1 493 ? -42.563 -17.018 18.812 1.00 11.49 ? 493 THR A CB 1 ATOM 3810 O OG1 . THR A 1 493 ? -43.020 -18.374 18.805 1.00 13.21 ? 493 THR A OG1 1 ATOM 3811 C CG2 . THR A 1 493 ? -41.135 -16.963 18.383 1.00 9.04 ? 493 THR A CG2 1 ATOM 3812 N N . ASP A 1 494 ? -44.508 -15.372 21.542 1.00 15.33 ? 494 ASP A N 1 ATOM 3813 C CA . ASP A 1 494 ? -45.881 -15.072 21.936 1.00 17.73 ? 494 ASP A CA 1 ATOM 3814 C C . ASP A 1 494 ? -46.416 -13.679 21.599 1.00 18.09 ? 494 ASP A C 1 ATOM 3815 O O . ASP A 1 494 ? -47.552 -13.344 21.951 1.00 18.09 ? 494 ASP A O 1 ATOM 3816 C CB . ASP A 1 494 ? -46.104 -15.413 23.433 1.00 18.14 ? 494 ASP A CB 1 ATOM 3817 C CG . ASP A 1 494 ? -45.171 -14.654 24.394 1.00 19.78 ? 494 ASP A CG 1 ATOM 3818 O OD1 . ASP A 1 494 ? -44.547 -13.639 24.022 1.00 19.03 ? 494 ASP A OD1 1 ATOM 3819 O OD2 . ASP A 1 494 ? -45.087 -15.075 25.565 1.00 23.72 ? 494 ASP A OD2 1 ATOM 3820 N N . ASN A 1 495 ? -45.628 -12.898 20.866 1.00 18.79 ? 495 ASN A N 1 ATOM 3821 C CA . ASN A 1 495 ? -46.024 -11.535 20.513 1.00 19.17 ? 495 ASN A CA 1 ATOM 3822 C C . ASN A 1 495 ? -45.664 -11.203 19.054 1.00 18.57 ? 495 ASN A C 1 ATOM 3823 O O . ASN A 1 495 ? -44.569 -10.704 18.786 1.00 18.00 ? 495 ASN A O 1 ATOM 3824 C CB . ASN A 1 495 ? -45.345 -10.559 21.487 1.00 18.58 ? 495 ASN A CB 1 ATOM 3825 C CG . ASN A 1 495 ? -45.926 -9.156 21.434 1.00 21.17 ? 495 ASN A CG 1 ATOM 3826 O OD1 . ASN A 1 495 ? -46.930 -8.885 20.758 1.00 20.44 ? 495 ASN A OD1 1 ATOM 3827 N ND2 . ASN A 1 495 ? -45.278 -8.242 22.147 1.00 19.57 ? 495 ASN A ND2 1 ATOM 3828 N N . PRO A 1 496 ? -46.593 -11.446 18.097 1.00 18.27 ? 496 PRO A N 1 ATOM 3829 C CA . PRO A 1 496 ? -46.375 -11.177 16.667 1.00 17.91 ? 496 PRO A CA 1 ATOM 3830 C C . PRO A 1 496 ? -45.978 -9.729 16.376 1.00 16.25 ? 496 PRO A C 1 ATOM 3831 O O . PRO A 1 496 ? -46.642 -8.786 16.832 1.00 16.31 ? 496 PRO A O 1 ATOM 3832 C CB . PRO A 1 496 ? -47.735 -11.498 16.050 1.00 18.95 ? 496 PRO A CB 1 ATOM 3833 C CG . PRO A 1 496 ? -48.276 -12.515 16.947 1.00 19.36 ? 496 PRO A CG 1 ATOM 3834 C CD . PRO A 1 496 ? -47.957 -11.964 18.298 1.00 18.34 ? 496 PRO A CD 1 ATOM 3835 N N . GLY A 1 497 ? -44.855 -9.566 15.685 1.00 13.54 ? 497 GLY A N 1 ATOM 3836 C CA . GLY A 1 497 ? -44.399 -8.231 15.370 1.00 10.78 ? 497 GLY A CA 1 ATOM 3837 C C . GLY A 1 497 ? -42.972 -8.098 14.936 1.00 9.92 ? 497 GLY A C 1 ATOM 3838 O O . GLY A 1 497 ? -42.229 -9.077 14.936 1.00 13.37 ? 497 GLY A O 1 ATOM 3839 N N . ALA A 1 498 ? -42.597 -6.885 14.534 1.00 7.50 ? 498 ALA A N 1 ATOM 3840 C CA . ALA A 1 498 ? -41.226 -6.611 14.116 1.00 7.49 ? 498 ALA A CA 1 ATOM 3841 C C . ALA A 1 498 ? -40.529 -6.076 15.342 1.00 5.95 ? 498 ALA A C 1 ATOM 3842 O O . ALA A 1 498 ? -40.920 -5.035 15.877 1.00 6.91 ? 498 ALA A O 1 ATOM 3843 C CB . ALA A 1 498 ? -41.183 -5.607 12.973 1.00 3.76 ? 498 ALA A CB 1 ATOM 3844 N N . TRP A 1 499 ? -39.552 -6.837 15.832 1.00 6.99 ? 499 TRP A N 1 ATOM 3845 C CA . TRP A 1 499 ? -38.808 -6.457 17.040 1.00 8.78 ? 499 TRP A CA 1 ATOM 3846 C C . TRP A 1 499 ? -37.329 -6.340 16.853 1.00 8.15 ? 499 TRP A C 1 ATOM 3847 O O . TRP A 1 499 ? -36.684 -7.277 16.389 1.00 10.69 ? 499 TRP A O 1 ATOM 3848 C CB . TRP A 1 499 ? -39.049 -7.449 18.182 1.00 5.90 ? 499 TRP A CB 1 ATOM 3849 C CG . TRP A 1 499 ? -40.472 -7.755 18.420 1.00 7.32 ? 499 TRP A CG 1 ATOM 3850 C CD1 . TRP A 1 499 ? -41.119 -8.907 18.078 1.00 6.89 ? 499 TRP A CD1 1 ATOM 3851 C CD2 . TRP A 1 499 ? -41.452 -6.907 19.034 1.00 6.57 ? 499 TRP A CD2 1 ATOM 3852 N NE1 . TRP A 1 499 ? -42.441 -8.836 18.439 1.00 5.14 ? 499 TRP A NE1 1 ATOM 3853 C CE2 . TRP A 1 499 ? -42.679 -7.624 19.030 1.00 5.33 ? 499 TRP A CE2 1 ATOM 3854 C CE3 . TRP A 1 499 ? -41.422 -5.613 19.595 1.00 4.50 ? 499 TRP A CE3 1 ATOM 3855 C CZ2 . TRP A 1 499 ? -43.870 -7.093 19.569 1.00 2.05 ? 499 TRP A CZ2 1 ATOM 3856 C CZ3 . TRP A 1 499 ? -42.622 -5.079 20.145 1.00 2.81 ? 499 TRP A CZ3 1 ATOM 3857 C CH2 . TRP A 1 499 ? -43.824 -5.829 20.123 1.00 1.69 ? 499 TRP A CH2 1 ATOM 3858 N N . LEU A 1 500 ? -36.784 -5.210 17.296 1.00 9.68 ? 500 LEU A N 1 ATOM 3859 C CA . LEU A 1 500 ? -35.350 -4.967 17.212 1.00 9.12 ? 500 LEU A CA 1 ATOM 3860 C C . LEU A 1 500 ? -34.580 -5.711 18.293 1.00 9.99 ? 500 LEU A C 1 ATOM 3861 O O . LEU A 1 500 ? -35.035 -5.840 19.440 1.00 12.97 ? 500 LEU A O 1 ATOM 3862 C CB . LEU A 1 500 ? -35.028 -3.473 17.305 1.00 7.48 ? 500 LEU A CB 1 ATOM 3863 C CG . LEU A 1 500 ? -35.273 -2.569 16.096 1.00 11.02 ? 500 LEU A CG 1 ATOM 3864 C CD1 . LEU A 1 500 ? -34.748 -1.170 16.401 1.00 9.10 ? 500 LEU A CD1 1 ATOM 3865 C CD2 . LEU A 1 500 ? -34.575 -3.126 14.856 1.00 9.94 ? 500 LEU A CD2 1 ATOM 3866 N N . PHE A 1 501 ? -33.456 -6.274 17.881 1.00 7.16 ? 501 PHE A N 1 ATOM 3867 C CA . PHE A 1 501 ? -32.566 -6.977 18.775 1.00 7.60 ? 501 PHE A CA 1 ATOM 3868 C C . PHE A 1 501 ? -31.262 -6.295 18.466 1.00 9.33 ? 501 PHE A C 1 ATOM 3869 O O . PHE A 1 501 ? -30.676 -6.497 17.397 1.00 12.39 ? 501 PHE A O 1 ATOM 3870 C CB . PHE A 1 501 ? -32.514 -8.473 18.464 1.00 3.81 ? 501 PHE A CB 1 ATOM 3871 C CG . PHE A 1 501 ? -31.540 -9.237 19.312 1.00 2.38 ? 501 PHE A CG 1 ATOM 3872 C CD1 . PHE A 1 501 ? -31.668 -9.262 20.726 1.00 2.82 ? 501 PHE A CD1 1 ATOM 3873 C CD2 . PHE A 1 501 ? -30.450 -9.893 18.715 1.00 1.00 ? 501 PHE A CD2 1 ATOM 3874 C CE1 . PHE A 1 501 ? -30.711 -9.928 21.539 1.00 1.48 ? 501 PHE A CE1 1 ATOM 3875 C CE2 . PHE A 1 501 ? -29.492 -10.558 19.503 1.00 1.00 ? 501 PHE A CE2 1 ATOM 3876 C CZ . PHE A 1 501 ? -29.620 -10.576 20.930 1.00 1.00 ? 501 PHE A CZ 1 ATOM 3877 N N . HIS A 1 502 ? -30.814 -5.479 19.409 1.00 8.47 ? 502 HIS A N 1 ATOM 3878 C CA . HIS A 1 502 ? -29.615 -4.706 19.201 1.00 8.73 ? 502 HIS A CA 1 ATOM 3879 C C . HIS A 1 502 ? -28.762 -4.469 20.425 1.00 8.48 ? 502 HIS A C 1 ATOM 3880 O O . HIS A 1 502 ? -29.187 -4.693 21.559 1.00 6.00 ? 502 HIS A O 1 ATOM 3881 C CB . HIS A 1 502 ? -30.007 -3.342 18.605 1.00 10.24 ? 502 HIS A CB 1 ATOM 3882 C CG . HIS A 1 502 ? -30.752 -2.443 19.544 1.00 14.18 ? 502 HIS A CG 1 ATOM 3883 N ND1 . HIS A 1 502 ? -30.133 -1.426 20.240 1.00 14.15 ? 502 HIS A ND1 1 ATOM 3884 C CD2 . HIS A 1 502 ? -32.057 -2.407 19.902 1.00 13.07 ? 502 HIS A CD2 1 ATOM 3885 C CE1 . HIS A 1 502 ? -31.025 -0.804 20.988 1.00 14.46 ? 502 HIS A CE1 1 ATOM 3886 N NE2 . HIS A 1 502 ? -32.199 -1.380 20.801 1.00 13.53 ? 502 HIS A NE2 1 ATOM 3887 N N . CYS A 1 503 ? -27.571 -3.938 20.153 1.00 6.61 ? 503 CYS A N 1 ATOM 3888 C CA . CYS A 1 503 ? -26.631 -3.555 21.186 1.00 6.73 ? 503 CYS A CA 1 ATOM 3889 C C . CYS A 1 503 ? -27.169 -2.206 21.631 1.00 6.17 ? 503 CYS A C 1 ATOM 3890 O O . CYS A 1 503 ? -27.561 -1.380 20.786 1.00 1.50 ? 503 CYS A O 1 ATOM 3891 C CB . CYS A 1 503 ? -25.227 -3.369 20.623 1.00 6.06 ? 503 CYS A CB 1 ATOM 3892 S SG . CYS A 1 503 ? -24.106 -2.741 21.857 1.00 13.35 ? 503 CYS A SG 1 ATOM 3893 N N . HIS A 1 504 ? -27.216 -2.000 22.949 1.00 4.31 ? 504 HIS A N 1 ATOM 3894 C CA . HIS A 1 504 ? -27.730 -0.753 23.472 1.00 2.80 ? 504 HIS A CA 1 ATOM 3895 C C . HIS A 1 504 ? -26.729 0.406 23.614 1.00 3.24 ? 504 HIS A C 1 ATOM 3896 O O . HIS A 1 504 ? -27.101 1.505 24.049 1.00 3.61 ? 504 HIS A O 1 ATOM 3897 C CB . HIS A 1 504 ? -28.565 -0.985 24.722 1.00 2.99 ? 504 HIS A CB 1 ATOM 3898 C CG . HIS A 1 504 ? -29.719 -0.045 24.836 1.00 1.08 ? 504 HIS A CG 1 ATOM 3899 N ND1 . HIS A 1 504 ? -29.556 1.315 24.996 1.00 1.95 ? 504 HIS A ND1 1 ATOM 3900 C CD2 . HIS A 1 504 ? -31.051 -0.261 24.783 1.00 2.68 ? 504 HIS A CD2 1 ATOM 3901 C CE1 . HIS A 1 504 ? -30.738 1.897 25.035 1.00 2.09 ? 504 HIS A CE1 1 ATOM 3902 N NE2 . HIS A 1 504 ? -31.663 0.963 24.910 1.00 7.66 ? 504 HIS A NE2 1 ATOM 3903 N N . ILE A 1 505 ? -25.465 0.171 23.250 1.00 3.15 ? 505 ILE A N 1 ATOM 3904 C CA . ILE A 1 505 ? -24.465 1.254 23.227 1.00 5.28 ? 505 ILE A CA 1 ATOM 3905 C C . ILE A 1 505 ? -24.925 2.029 21.984 1.00 6.95 ? 505 ILE A C 1 ATOM 3906 O O . ILE A 1 505 ? -25.017 1.451 20.887 1.00 5.76 ? 505 ILE A O 1 ATOM 3907 C CB . ILE A 1 505 ? -22.995 0.743 23.036 1.00 4.67 ? 505 ILE A CB 1 ATOM 3908 C CG1 . ILE A 1 505 ? -22.468 0.168 24.354 1.00 2.42 ? 505 ILE A CG1 1 ATOM 3909 C CG2 . ILE A 1 505 ? -22.066 1.883 22.542 1.00 1.28 ? 505 ILE A CG2 1 ATOM 3910 C CD1 . ILE A 1 505 ? -21.192 -0.662 24.230 1.00 1.00 ? 505 ILE A CD1 1 ATOM 3911 N N . ALA A 1 506 ? -25.327 3.285 22.205 1.00 9.43 ? 506 ALA A N 1 ATOM 3912 C CA . ALA A 1 506 ? -25.851 4.168 21.161 1.00 12.07 ? 506 ALA A CA 1 ATOM 3913 C C . ALA A 1 506 ? -25.020 4.232 19.899 1.00 14.22 ? 506 ALA A C 1 ATOM 3914 O O . ALA A 1 506 ? -25.548 4.092 18.797 1.00 14.89 ? 506 ALA A O 1 ATOM 3915 C CB . ALA A 1 506 ? -26.065 5.548 21.705 1.00 14.58 ? 506 ALA A CB 1 ATOM 3916 N N . TRP A 1 507 ? -23.706 4.309 20.089 1.00 15.81 ? 507 TRP A N 1 ATOM 3917 C CA . TRP A 1 507 ? -22.754 4.389 18.986 1.00 17.00 ? 507 TRP A CA 1 ATOM 3918 C C . TRP A 1 507 ? -22.684 3.107 18.156 1.00 16.76 ? 507 TRP A C 1 ATOM 3919 O O . TRP A 1 507 ? -22.525 3.163 16.932 1.00 15.93 ? 507 TRP A O 1 ATOM 3920 C CB . TRP A 1 507 ? -21.359 4.752 19.512 1.00 18.02 ? 507 TRP A CB 1 ATOM 3921 C CG . TRP A 1 507 ? -21.267 5.608 20.792 1.00 19.27 ? 507 TRP A CG 1 ATOM 3922 C CD1 . TRP A 1 507 ? -20.428 5.371 21.840 1.00 20.71 ? 507 TRP A CD1 1 ATOM 3923 C CD2 . TRP A 1 507 ? -22.016 6.796 21.147 1.00 20.15 ? 507 TRP A CD2 1 ATOM 3924 N NE1 . TRP A 1 507 ? -20.594 6.313 22.823 1.00 21.04 ? 507 TRP A NE1 1 ATOM 3925 C CE2 . TRP A 1 507 ? -21.562 7.200 22.435 1.00 22.17 ? 507 TRP A CE2 1 ATOM 3926 C CE3 . TRP A 1 507 ? -23.029 7.556 20.514 1.00 22.30 ? 507 TRP A CE3 1 ATOM 3927 C CZ2 . TRP A 1 507 ? -22.087 8.333 23.110 1.00 21.51 ? 507 TRP A CZ2 1 ATOM 3928 C CZ3 . TRP A 1 507 ? -23.558 8.685 21.185 1.00 22.48 ? 507 TRP A CZ3 1 ATOM 3929 C CH2 . TRP A 1 507 ? -23.080 9.057 22.475 1.00 23.59 ? 507 TRP A CH2 1 ATOM 3930 N N . HIS A 1 508 ? -22.862 1.966 18.822 1.00 16.96 ? 508 HIS A N 1 ATOM 3931 C CA . HIS A 1 508 ? -22.815 0.666 18.160 1.00 16.98 ? 508 HIS A CA 1 ATOM 3932 C C . HIS A 1 508 ? -24.058 0.326 17.337 1.00 17.34 ? 508 HIS A C 1 ATOM 3933 O O . HIS A 1 508 ? -23.927 -0.199 16.224 1.00 18.42 ? 508 HIS A O 1 ATOM 3934 C CB . HIS A 1 508 ? -22.461 -0.439 19.157 1.00 16.70 ? 508 HIS A CB 1 ATOM 3935 C CG . HIS A 1 508 ? -21.081 -0.312 19.736 1.00 14.95 ? 508 HIS A CG 1 ATOM 3936 N ND1 . HIS A 1 508 ? -20.629 -1.110 20.762 1.00 11.75 ? 508 HIS A ND1 1 ATOM 3937 C CD2 . HIS A 1 508 ? -20.060 0.527 19.440 1.00 14.69 ? 508 HIS A CD2 1 ATOM 3938 C CE1 . HIS A 1 508 ? -19.392 -0.771 21.072 1.00 12.86 ? 508 HIS A CE1 1 ATOM 3939 N NE2 . HIS A 1 508 ? -19.024 0.221 20.285 1.00 13.00 ? 508 HIS A NE2 1 ATOM 3940 N N . VAL A 1 509 ? -25.245 0.683 17.843 1.00 15.45 ? 509 VAL A N 1 ATOM 3941 C CA . VAL A 1 509 ? -26.497 0.450 17.110 1.00 14.22 ? 509 VAL A CA 1 ATOM 3942 C C . VAL A 1 509 ? -26.543 1.413 15.914 1.00 15.29 ? 509 VAL A C 1 ATOM 3943 O O . VAL A 1 509 ? -27.097 1.082 14.862 1.00 17.19 ? 509 VAL A O 1 ATOM 3944 C CB . VAL A 1 509 ? -27.779 0.542 18.026 1.00 14.12 ? 509 VAL A CB 1 ATOM 3945 C CG1 . VAL A 1 509 ? -27.965 1.915 18.630 1.00 10.47 ? 509 VAL A CG1 1 ATOM 3946 C CG2 . VAL A 1 509 ? -29.025 0.114 17.261 1.00 15.05 ? 509 VAL A CG2 1 ATOM 3947 N N . SER A 1 510 ? -25.866 2.556 16.065 1.00 16.03 ? 510 SER A N 1 ATOM 3948 C CA . SER A 1 510 ? -25.748 3.564 15.006 1.00 15.71 ? 510 SER A CA 1 ATOM 3949 C C . SER A 1 510 ? -24.781 3.060 13.934 1.00 14.85 ? 510 SER A C 1 ATOM 3950 O O . SER A 1 510 ? -24.917 3.398 12.763 1.00 13.90 ? 510 SER A O 1 ATOM 3951 C CB . SER A 1 510 ? -25.251 4.892 15.570 1.00 14.12 ? 510 SER A CB 1 ATOM 3952 O OG . SER A 1 510 ? -26.290 5.553 16.251 1.00 17.42 ? 510 SER A OG 1 ATOM 3953 N N . GLY A 1 511 ? -23.815 2.243 14.366 1.00 16.31 ? 511 GLY A N 1 ATOM 3954 C CA . GLY A 1 511 ? -22.825 1.648 13.479 1.00 17.12 ? 511 GLY A CA 1 ATOM 3955 C C . GLY A 1 511 ? -23.430 0.498 12.694 1.00 17.68 ? 511 GLY A C 1 ATOM 3956 O O . GLY A 1 511 ? -22.919 0.121 11.638 1.00 19.23 ? 511 GLY A O 1 ATOM 3957 N N . GLY A 1 512 ? -24.514 -0.063 13.228 1.00 18.41 ? 512 GLY A N 1 ATOM 3958 C CA . GLY A 1 512 ? -25.216 -1.138 12.557 1.00 17.69 ? 512 GLY A CA 1 ATOM 3959 C C . GLY A 1 512 ? -25.500 -2.400 13.339 1.00 17.32 ? 512 GLY A C 1 ATOM 3960 O O . GLY A 1 512 ? -26.084 -3.329 12.779 1.00 17.71 ? 512 GLY A O 1 ATOM 3961 N N . LEU A 1 513 ? -25.118 -2.436 14.616 1.00 17.28 ? 513 LEU A N 1 ATOM 3962 C CA . LEU A 1 513 ? -25.324 -3.616 15.461 1.00 15.98 ? 513 LEU A CA 1 ATOM 3963 C C . LEU A 1 513 ? -26.771 -3.838 15.862 1.00 13.98 ? 513 LEU A C 1 ATOM 3964 O O . LEU A 1 513 ? -27.183 -3.491 16.975 1.00 13.38 ? 513 LEU A O 1 ATOM 3965 C CB . LEU A 1 513 ? -24.426 -3.576 16.703 1.00 16.04 ? 513 LEU A CB 1 ATOM 3966 C CG . LEU A 1 513 ? -23.662 -4.867 17.042 1.00 15.93 ? 513 LEU A CG 1 ATOM 3967 C CD1 . LEU A 1 513 ? -22.501 -4.502 17.924 1.00 13.90 ? 513 LEU A CD1 1 ATOM 3968 C CD2 . LEU A 1 513 ? -24.541 -5.925 17.714 1.00 16.47 ? 513 LEU A CD2 1 ATOM 3969 N N . SER A 1 514 ? -27.506 -4.479 14.951 1.00 13.14 ? 514 SER A N 1 ATOM 3970 C CA . SER A 1 514 ? -28.910 -4.798 15.136 1.00 11.52 ? 514 SER A CA 1 ATOM 3971 C C . SER A 1 514 ? -29.449 -5.758 14.090 1.00 12.87 ? 514 SER A C 1 ATOM 3972 O O . SER A 1 514 ? -28.889 -5.890 12.997 1.00 14.35 ? 514 SER A O 1 ATOM 3973 C CB . SER A 1 514 ? -29.749 -3.503 15.086 1.00 10.45 ? 514 SER A CB 1 ATOM 3974 O OG . SER A 1 514 ? -31.099 -3.707 15.460 1.00 10.79 ? 514 SER A OG 1 ATOM 3975 N N . VAL A 1 515 ? -30.479 -6.500 14.493 1.00 11.75 ? 515 VAL A N 1 ATOM 3976 C CA . VAL A 1 515 ? -31.231 -7.384 13.603 1.00 12.34 ? 515 VAL A CA 1 ATOM 3977 C C . VAL A 1 515 ? -32.681 -7.033 13.903 1.00 13.80 ? 515 VAL A C 1 ATOM 3978 O O . VAL A 1 515 ? -32.964 -6.301 14.862 1.00 14.39 ? 515 VAL A O 1 ATOM 3979 C CB . VAL A 1 515 ? -31.001 -8.943 13.776 1.00 11.94 ? 515 VAL A CB 1 ATOM 3980 C CG1 . VAL A 1 515 ? -29.608 -9.333 13.402 1.00 10.94 ? 515 VAL A CG1 1 ATOM 3981 C CG2 . VAL A 1 515 ? -31.376 -9.444 15.153 1.00 10.34 ? 515 VAL A CG2 1 ATOM 3982 N N . ASP A 1 516 ? -33.591 -7.546 13.087 1.00 15.22 ? 516 ASP A N 1 ATOM 3983 C CA . ASP A 1 516 ? -35.009 -7.289 13.277 1.00 17.04 ? 516 ASP A CA 1 ATOM 3984 C C . ASP A 1 516 ? -35.739 -8.612 13.219 1.00 18.02 ? 516 ASP A C 1 ATOM 3985 O O . ASP A 1 516 ? -35.813 -9.253 12.167 1.00 20.08 ? 516 ASP A O 1 ATOM 3986 C CB . ASP A 1 516 ? -35.526 -6.306 12.208 1.00 16.18 ? 516 ASP A CB 1 ATOM 3987 C CG . ASP A 1 516 ? -36.978 -5.865 12.426 1.00 14.59 ? 516 ASP A CG 1 ATOM 3988 O OD1 . ASP A 1 516 ? -37.665 -6.352 13.352 1.00 15.52 ? 516 ASP A OD1 1 ATOM 3989 O OD2 . ASP A 1 516 ? -37.435 -5.014 11.633 1.00 13.69 ? 516 ASP A OD2 1 ATOM 3990 N N . PHE A 1 517 ? -36.241 -9.025 14.381 1.00 18.99 ? 517 PHE A N 1 ATOM 3991 C CA . PHE A 1 517 ? -37.009 -10.255 14.508 1.00 18.10 ? 517 PHE A CA 1 ATOM 3992 C C . PHE A 1 517 ? -38.434 -10.015 14.051 1.00 17.70 ? 517 PHE A C 1 ATOM 3993 O O . PHE A 1 517 ? -39.238 -9.408 14.779 1.00 17.29 ? 517 PHE A O 1 ATOM 3994 C CB . PHE A 1 517 ? -37.025 -10.774 15.957 1.00 18.00 ? 517 PHE A CB 1 ATOM 3995 C CG . PHE A 1 517 ? -35.776 -11.505 16.364 1.00 18.38 ? 517 PHE A CG 1 ATOM 3996 C CD1 . PHE A 1 517 ? -35.303 -12.601 15.619 1.00 15.95 ? 517 PHE A CD1 1 ATOM 3997 C CD2 . PHE A 1 517 ? -35.058 -11.100 17.501 1.00 17.90 ? 517 PHE A CD2 1 ATOM 3998 C CE1 . PHE A 1 517 ? -34.129 -13.282 15.995 1.00 17.33 ? 517 PHE A CE1 1 ATOM 3999 C CE2 . PHE A 1 517 ? -33.870 -11.779 17.900 1.00 16.98 ? 517 PHE A CE2 1 ATOM 4000 C CZ . PHE A 1 517 ? -33.405 -12.868 17.144 1.00 18.57 ? 517 PHE A CZ 1 ATOM 4001 N N . LEU A 1 518 ? -38.715 -10.415 12.811 1.00 16.22 ? 518 LEU A N 1 ATOM 4002 C CA . LEU A 1 518 ? -40.062 -10.296 12.271 1.00 16.67 ? 518 LEU A CA 1 ATOM 4003 C C . LEU A 1 518 ? -40.784 -11.591 12.651 1.00 16.92 ? 518 LEU A C 1 ATOM 4004 O O . LEU A 1 518 ? -40.739 -12.612 11.950 1.00 15.91 ? 518 LEU A O 1 ATOM 4005 C CB . LEU A 1 518 ? -40.056 -10.040 10.766 1.00 16.32 ? 518 LEU A CB 1 ATOM 4006 C CG . LEU A 1 518 ? -41.429 -9.801 10.127 1.00 17.18 ? 518 LEU A CG 1 ATOM 4007 C CD1 . LEU A 1 518 ? -42.201 -8.629 10.729 1.00 17.80 ? 518 LEU A CD1 1 ATOM 4008 C CD2 . LEU A 1 518 ? -41.227 -9.608 8.666 1.00 17.76 ? 518 LEU A CD2 1 ATOM 4009 N N . GLU A 1 519 ? -41.375 -11.520 13.838 1.00 16.10 ? 519 GLU A N 1 ATOM 4010 C CA . GLU A 1 519 ? -42.093 -12.604 14.474 1.00 17.29 ? 519 GLU A CA 1 ATOM 4011 C C . GLU A 1 519 ? -43.532 -12.722 13.995 1.00 18.39 ? 519 GLU A C 1 ATOM 4012 O O . GLU A 1 519 ? -44.305 -11.758 14.041 1.00 19.02 ? 519 GLU A O 1 ATOM 4013 C CB . GLU A 1 519 ? -42.036 -12.382 15.988 1.00 18.62 ? 519 GLU A CB 1 ATOM 4014 C CG . GLU A 1 519 ? -42.695 -13.425 16.871 1.00 18.45 ? 519 GLU A CG 1 ATOM 4015 C CD . GLU A 1 519 ? -42.530 -13.105 18.353 1.00 20.40 ? 519 GLU A CD 1 ATOM 4016 O OE1 . GLU A 1 519 ? -41.474 -12.564 18.747 1.00 19.38 ? 519 GLU A OE1 1 ATOM 4017 O OE2 . GLU A 1 519 ? -43.456 -13.399 19.135 1.00 17.26 ? 519 GLU A OE2 1 ATOM 4018 N N . ARG A 1 520 ? -43.852 -13.918 13.508 1.00 18.44 ? 520 ARG A N 1 ATOM 4019 C CA . ARG A 1 520 ? -45.175 -14.301 13.012 1.00 20.10 ? 520 ARG A CA 1 ATOM 4020 C C . ARG A 1 520 ? -45.888 -13.268 12.112 1.00 21.33 ? 520 ARG A C 1 ATOM 4021 O O . ARG A 1 520 ? -46.897 -12.680 12.518 1.00 21.84 ? 520 ARG A O 1 ATOM 4022 C CB . ARG A 1 520 ? -46.053 -14.718 14.200 1.00 19.61 ? 520 ARG A CB 1 ATOM 4023 C CG . ARG A 1 520 ? -45.491 -15.875 15.011 1.00 15.86 ? 520 ARG A CG 1 ATOM 4024 C CD . ARG A 1 520 ? -46.061 -15.900 16.421 1.00 17.84 ? 520 ARG A CD 1 ATOM 4025 N NE . ARG A 1 520 ? -47.507 -16.117 16.440 1.00 16.49 ? 520 ARG A NE 1 ATOM 4026 C CZ . ARG A 1 520 ? -48.242 -16.254 17.539 1.00 15.61 ? 520 ARG A CZ 1 ATOM 4027 N NH1 . ARG A 1 520 ? -47.690 -16.205 18.741 1.00 15.45 ? 520 ARG A NH1 1 ATOM 4028 N NH2 . ARG A 1 520 ? -49.548 -16.416 17.430 1.00 17.33 ? 520 ARG A NH2 1 ATOM 4029 N N . PRO A 1 521 ? -45.350 -13.020 10.889 1.00 23.05 ? 521 PRO A N 1 ATOM 4030 C CA . PRO A 1 521 ? -45.888 -12.070 9.903 1.00 24.80 ? 521 PRO A CA 1 ATOM 4031 C C . PRO A 1 521 ? -47.361 -12.211 9.545 1.00 26.48 ? 521 PRO A C 1 ATOM 4032 O O . PRO A 1 521 ? -48.093 -11.214 9.510 1.00 27.59 ? 521 PRO A O 1 ATOM 4033 C CB . PRO A 1 521 ? -45.014 -12.324 8.683 1.00 25.67 ? 521 PRO A CB 1 ATOM 4034 C CG . PRO A 1 521 ? -43.734 -12.669 9.271 1.00 23.87 ? 521 PRO A CG 1 ATOM 4035 C CD . PRO A 1 521 ? -44.091 -13.597 10.376 1.00 22.94 ? 521 PRO A CD 1 ATOM 4036 N N . ALA A 1 522 ? -47.788 -13.449 9.294 1.00 28.75 ? 522 ALA A N 1 ATOM 4037 C CA . ALA A 1 522 ? -49.177 -13.757 8.938 1.00 29.48 ? 522 ALA A CA 1 ATOM 4038 C C . ALA A 1 522 ? -50.164 -13.380 10.054 1.00 30.82 ? 522 ALA A C 1 ATOM 4039 O O . ALA A 1 522 ? -51.232 -12.816 9.782 1.00 32.23 ? 522 ALA A O 1 ATOM 4040 C CB . ALA A 1 522 ? -49.309 -15.231 8.585 1.00 29.74 ? 522 ALA A CB 1 ATOM 4041 N N . ASP A 1 523 ? -49.752 -13.615 11.304 1.00 30.16 ? 523 ASP A N 1 ATOM 4042 C CA . ASP A 1 523 ? -50.566 -13.313 12.484 1.00 29.68 ? 523 ASP A CA 1 ATOM 4043 C C . ASP A 1 523 ? -50.600 -11.824 12.798 1.00 30.03 ? 523 ASP A C 1 ATOM 4044 O O . ASP A 1 523 ? -51.585 -11.335 13.349 1.00 27.62 ? 523 ASP A O 1 ATOM 4045 C CB . ASP A 1 523 ? -50.033 -14.034 13.729 1.00 29.76 ? 523 ASP A CB 1 ATOM 4046 C CG . ASP A 1 523 ? -50.025 -15.547 13.602 1.00 28.58 ? 523 ASP A CG 1 ATOM 4047 O OD1 . ASP A 1 523 ? -50.847 -16.120 12.861 1.00 31.46 ? 523 ASP A OD1 1 ATOM 4048 O OD2 . ASP A 1 523 ? -49.192 -16.170 14.279 1.00 25.99 ? 523 ASP A OD2 1 ATOM 4049 N N . LEU A 1 524 ? -49.520 -11.123 12.431 1.00 30.72 ? 524 LEU A N 1 ATOM 4050 C CA . LEU A 1 524 ? -49.355 -9.688 12.674 1.00 31.21 ? 524 LEU A CA 1 ATOM 4051 C C . LEU A 1 524 ? -50.302 -8.745 11.937 1.00 31.39 ? 524 LEU A C 1 ATOM 4052 O O . LEU A 1 524 ? -50.861 -7.850 12.572 1.00 31.73 ? 524 LEU A O 1 ATOM 4053 C CB . LEU A 1 524 ? -47.889 -9.266 12.444 1.00 32.34 ? 524 LEU A CB 1 ATOM 4054 C CG . LEU A 1 524 ? -47.430 -7.794 12.508 1.00 32.11 ? 524 LEU A CG 1 ATOM 4055 C CD1 . LEU A 1 524 ? -47.631 -7.190 13.890 1.00 31.99 ? 524 LEU A CD1 1 ATOM 4056 C CD2 . LEU A 1 524 ? -45.985 -7.687 12.074 1.00 30.92 ? 524 LEU A CD2 1 ATOM 4057 N N . ARG A 1 525 ? -50.485 -8.943 10.627 1.00 31.80 ? 525 ARG A N 1 ATOM 4058 C CA . ARG A 1 525 ? -51.362 -8.088 9.809 1.00 32.77 ? 525 ARG A CA 1 ATOM 4059 C C . ARG A 1 525 ? -52.811 -8.061 10.299 1.00 32.27 ? 525 ARG A C 1 ATOM 4060 O O . ARG A 1 525 ? -53.435 -6.997 10.344 1.00 31.70 ? 525 ARG A O 1 ATOM 4061 C CB . ARG A 1 525 ? -51.309 -8.496 8.326 1.00 34.77 ? 525 ARG A CB 1 ATOM 4062 C CG . ARG A 1 525 ? -52.040 -7.532 7.382 1.00 37.76 ? 525 ARG A CG 1 ATOM 4063 C CD . ARG A 1 525 ? -51.994 -7.982 5.934 1.00 42.23 ? 525 ARG A CD 1 ATOM 4064 N NE . ARG A 1 525 ? -52.668 -7.025 5.050 1.00 45.82 ? 525 ARG A NE 1 ATOM 4065 C CZ . ARG A 1 525 ? -52.527 -6.979 3.724 1.00 48.25 ? 525 ARG A CZ 1 ATOM 4066 N NH1 . ARG A 1 525 ? -51.732 -7.839 3.092 1.00 48.66 ? 525 ARG A NH1 1 ATOM 4067 N NH2 . ARG A 1 525 ? -53.175 -6.056 3.020 1.00 49.01 ? 525 ARG A NH2 1 ATOM 4068 N N . GLN A 1 526 ? -53.294 -9.221 10.738 1.00 31.88 ? 526 GLN A N 1 ATOM 4069 C CA . GLN A 1 526 ? -54.655 -9.376 11.238 1.00 33.71 ? 526 GLN A CA 1 ATOM 4070 C C . GLN A 1 526 ? -54.887 -8.869 12.671 1.00 32.92 ? 526 GLN A C 1 ATOM 4071 O O . GLN A 1 526 ? -56.036 -8.671 13.079 1.00 31.97 ? 526 GLN A O 1 ATOM 4072 C CB . GLN A 1 526 ? -55.099 -10.839 11.093 1.00 36.49 ? 526 GLN A CB 1 ATOM 4073 C CG . GLN A 1 526 ? -55.677 -11.216 9.701 1.00 41.43 ? 526 GLN A CG 1 ATOM 4074 C CD . GLN A 1 526 ? -54.673 -11.108 8.544 1.00 42.95 ? 526 GLN A CD 1 ATOM 4075 O OE1 . GLN A 1 526 ? -54.848 -10.302 7.629 1.00 43.66 ? 526 GLN A OE1 1 ATOM 4076 N NE2 . GLN A 1 526 ? -53.623 -11.925 8.585 1.00 44.53 ? 526 GLN A NE2 1 ATOM 4077 N N . ARG A 1 527 ? -53.801 -8.616 13.406 1.00 32.13 ? 527 ARG A N 1 ATOM 4078 C CA . ARG A 1 527 ? -53.885 -8.130 14.793 1.00 31.98 ? 527 ARG A CA 1 ATOM 4079 C C . ARG A 1 527 ? -53.746 -6.616 14.962 1.00 30.60 ? 527 ARG A C 1 ATOM 4080 O O . ARG A 1 527 ? -53.900 -6.091 16.074 1.00 30.48 ? 527 ARG A O 1 ATOM 4081 C CB . ARG A 1 527 ? -52.875 -8.861 15.684 1.00 32.15 ? 527 ARG A CB 1 ATOM 4082 C CG . ARG A 1 527 ? -53.262 -10.297 15.955 1.00 34.25 ? 527 ARG A CG 1 ATOM 4083 C CD . ARG A 1 527 ? -52.169 -11.072 16.655 1.00 35.84 ? 527 ARG A CD 1 ATOM 4084 N NE . ARG A 1 527 ? -52.253 -12.490 16.313 1.00 37.65 ? 527 ARG A NE 1 ATOM 4085 C CZ . ARG A 1 527 ? -51.906 -13.496 17.113 1.00 39.56 ? 527 ARG A CZ 1 ATOM 4086 N NH1 . ARG A 1 527 ? -51.440 -13.266 18.341 1.00 39.91 ? 527 ARG A NH1 1 ATOM 4087 N NH2 . ARG A 1 527 ? -52.002 -14.744 16.667 1.00 39.07 ? 527 ARG A NH2 1 ATOM 4088 N N . ILE A 1 528 ? -53.475 -5.923 13.856 1.00 29.64 ? 528 ILE A N 1 ATOM 4089 C CA . ILE A 1 528 ? -53.323 -4.466 13.849 1.00 29.40 ? 528 ILE A CA 1 ATOM 4090 C C . ILE A 1 528 ? -54.696 -3.804 13.705 1.00 29.39 ? 528 ILE A C 1 ATOM 4091 O O . ILE A 1 528 ? -55.375 -3.982 12.684 1.00 29.75 ? 528 ILE A O 1 ATOM 4092 C CB . ILE A 1 528 ? -52.368 -4.001 12.699 1.00 29.48 ? 528 ILE A CB 1 ATOM 4093 C CG1 . ILE A 1 528 ? -50.963 -4.577 12.923 1.00 27.32 ? 528 ILE A CG1 1 ATOM 4094 C CG2 . ILE A 1 528 ? -52.298 -2.455 12.619 1.00 29.32 ? 528 ILE A CG2 1 ATOM 4095 C CD1 . ILE A 1 528 ? -50.048 -4.492 11.719 1.00 25.54 ? 528 ILE A CD1 1 ATOM 4096 N N . SER A 1 529 ? -55.081 -3.037 14.729 1.00 28.05 ? 529 SER A N 1 ATOM 4097 C CA . SER A 1 529 ? -56.363 -2.320 14.761 1.00 28.64 ? 529 SER A CA 1 ATOM 4098 C C . SER A 1 529 ? -56.429 -1.205 13.710 1.00 28.16 ? 529 SER A C 1 ATOM 4099 O O . SER A 1 529 ? -55.394 -0.668 13.306 1.00 27.28 ? 529 SER A O 1 ATOM 4100 C CB . SER A 1 529 ? -56.623 -1.737 16.160 1.00 27.86 ? 529 SER A CB 1 ATOM 4101 O OG . SER A 1 529 ? -55.674 -0.739 16.508 1.00 25.33 ? 529 SER A OG 1 ATOM 4102 N N . GLN A 1 530 ? -57.649 -0.853 13.295 1.00 28.77 ? 530 GLN A N 1 ATOM 4103 C CA . GLN A 1 530 ? -57.887 0.192 12.290 1.00 29.32 ? 530 GLN A CA 1 ATOM 4104 C C . GLN A 1 530 ? -57.354 1.564 12.747 1.00 28.30 ? 530 GLN A C 1 ATOM 4105 O O . GLN A 1 530 ? -56.882 2.348 11.925 1.00 27.49 ? 530 GLN A O 1 ATOM 4106 C CB . GLN A 1 530 ? -59.388 0.264 11.945 1.00 31.07 ? 530 GLN A CB 1 ATOM 4107 C CG . GLN A 1 530 ? -59.747 0.948 10.603 1.00 33.94 ? 530 GLN A CG 1 ATOM 4108 C CD . GLN A 1 530 ? -59.225 0.205 9.369 1.00 35.52 ? 530 GLN A CD 1 ATOM 4109 O OE1 . GLN A 1 530 ? -59.559 -0.959 9.136 1.00 36.67 ? 530 GLN A OE1 1 ATOM 4110 N NE2 . GLN A 1 530 ? -58.404 0.885 8.574 1.00 35.27 ? 530 GLN A NE2 1 ATOM 4111 N N . GLU A 1 531 ? -57.346 1.786 14.065 1.00 26.21 ? 531 GLU A N 1 ATOM 4112 C CA . GLU A 1 531 ? -56.858 3.022 14.675 1.00 26.17 ? 531 GLU A CA 1 ATOM 4113 C C . GLU A 1 531 ? -55.337 3.137 14.603 1.00 25.12 ? 531 GLU A C 1 ATOM 4114 O O . GLU A 1 531 ? -54.806 4.212 14.317 1.00 24.01 ? 531 GLU A O 1 ATOM 4115 C CB . GLU A 1 531 ? -57.314 3.122 16.137 1.00 28.94 ? 531 GLU A CB 1 ATOM 4116 C CG . GLU A 1 531 ? -58.786 3.507 16.318 1.00 34.05 ? 531 GLU A CG 1 ATOM 4117 C CD . GLU A 1 531 ? -59.737 2.317 16.466 1.00 36.01 ? 531 GLU A CD 1 ATOM 4118 O OE1 . GLU A 1 531 ? -59.645 1.337 15.686 1.00 36.84 ? 531 GLU A OE1 1 ATOM 4119 O OE2 . GLU A 1 531 ? -60.600 2.380 17.370 1.00 37.20 ? 531 GLU A OE2 1 ATOM 4120 N N . ASP A 1 532 ? -54.655 2.012 14.832 1.00 24.54 ? 532 ASP A N 1 ATOM 4121 C CA . ASP A 1 532 ? -53.194 1.939 14.802 1.00 23.78 ? 532 ASP A CA 1 ATOM 4122 C C . ASP A 1 532 ? -52.657 2.005 13.383 1.00 23.04 ? 532 ASP A C 1 ATOM 4123 O O . ASP A 1 532 ? -51.587 2.567 13.154 1.00 22.58 ? 532 ASP A O 1 ATOM 4124 C CB . ASP A 1 532 ? -52.690 0.664 15.492 1.00 25.61 ? 532 ASP A CB 1 ATOM 4125 C CG . ASP A 1 532 ? -52.863 0.696 17.009 1.00 26.51 ? 532 ASP A CG 1 ATOM 4126 O OD1 . ASP A 1 532 ? -53.125 1.779 17.583 1.00 25.85 ? 532 ASP A OD1 1 ATOM 4127 O OD2 . ASP A 1 532 ? -52.734 -0.382 17.630 1.00 27.74 ? 532 ASP A OD2 1 ATOM 4128 N N . GLU A 1 533 ? -53.427 1.453 12.441 1.00 23.39 ? 533 GLU A N 1 ATOM 4129 C CA . GLU A 1 533 ? -53.081 1.450 11.019 1.00 23.94 ? 533 GLU A CA 1 ATOM 4130 C C . GLU A 1 533 ? -53.188 2.865 10.447 1.00 23.55 ? 533 GLU A C 1 ATOM 4131 O O . GLU A 1 533 ? -52.305 3.297 9.701 1.00 22.71 ? 533 GLU A O 1 ATOM 4132 C CB . GLU A 1 533 ? -53.988 0.491 10.236 1.00 25.33 ? 533 GLU A CB 1 ATOM 4133 C CG . GLU A 1 533 ? -53.643 0.380 8.738 1.00 28.59 ? 533 GLU A CG 1 ATOM 4134 C CD . GLU A 1 533 ? -54.469 -0.643 7.979 1.00 30.16 ? 533 GLU A CD 1 ATOM 4135 O OE1 . GLU A 1 533 ? -55.542 -1.062 8.467 1.00 31.26 ? 533 GLU A OE1 1 ATOM 4136 O OE2 . GLU A 1 533 ? -54.034 -1.024 6.871 1.00 32.03 ? 533 GLU A OE2 1 ATOM 4137 N N . ASP A 1 534 ? -54.245 3.582 10.841 1.00 23.41 ? 534 ASP A N 1 ATOM 4138 C CA . ASP A 1 534 ? -54.482 4.958 10.395 1.00 24.83 ? 534 ASP A CA 1 ATOM 4139 C C . ASP A 1 534 ? -53.455 5.929 10.970 1.00 23.67 ? 534 ASP A C 1 ATOM 4140 O O . ASP A 1 534 ? -52.939 6.776 10.248 1.00 25.27 ? 534 ASP A O 1 ATOM 4141 C CB . ASP A 1 534 ? -55.899 5.432 10.757 1.00 26.06 ? 534 ASP A CB 1 ATOM 4142 C CG . ASP A 1 534 ? -56.983 4.685 10.008 1.00 28.53 ? 534 ASP A CG 1 ATOM 4143 O OD1 . ASP A 1 534 ? -56.675 3.993 9.011 1.00 30.73 ? 534 ASP A OD1 1 ATOM 4144 O OD2 . ASP A 1 534 ? -58.151 4.773 10.438 1.00 30.19 ? 534 ASP A OD2 1 ATOM 4145 N N . ASP A 1 535 ? -53.136 5.765 12.252 1.00 22.78 ? 535 ASP A N 1 ATOM 4146 C CA . ASP A 1 535 ? -52.157 6.604 12.945 1.00 22.85 ? 535 ASP A CA 1 ATOM 4147 C C . ASP A 1 535 ? -50.787 6.424 12.290 1.00 21.15 ? 535 ASP A C 1 ATOM 4148 O O . ASP A 1 535 ? -50.107 7.402 12.006 1.00 20.28 ? 535 ASP A O 1 ATOM 4149 C CB . ASP A 1 535 ? -52.102 6.241 14.441 1.00 24.21 ? 535 ASP A CB 1 ATOM 4150 C CG . ASP A 1 535 ? -51.105 7.096 15.225 1.00 25.67 ? 535 ASP A CG 1 ATOM 4151 O OD1 . ASP A 1 535 ? -51.510 8.152 15.763 1.00 25.62 ? 535 ASP A OD1 1 ATOM 4152 O OD2 . ASP A 1 535 ? -49.917 6.700 15.290 1.00 23.10 ? 535 ASP A OD2 1 ATOM 4153 N N . PHE A 1 536 ? -50.442 5.166 12.006 1.00 19.69 ? 536 PHE A N 1 ATOM 4154 C CA . PHE A 1 536 ? -49.187 4.788 11.365 1.00 20.09 ? 536 PHE A CA 1 ATOM 4155 C C . PHE A 1 536 ? -49.045 5.488 10.005 1.00 21.24 ? 536 PHE A C 1 ATOM 4156 O O . PHE A 1 536 ? -47.996 6.060 9.710 1.00 22.08 ? 536 PHE A O 1 ATOM 4157 C CB . PHE A 1 536 ? -49.136 3.249 11.206 1.00 18.42 ? 536 PHE A CB 1 ATOM 4158 C CG . PHE A 1 536 ? -47.983 2.743 10.376 1.00 16.47 ? 536 PHE A CG 1 ATOM 4159 C CD1 . PHE A 1 536 ? -48.117 2.588 8.972 1.00 14.99 ? 536 PHE A CD1 1 ATOM 4160 C CD2 . PHE A 1 536 ? -46.750 2.469 10.974 1.00 13.54 ? 536 PHE A CD2 1 ATOM 4161 C CE1 . PHE A 1 536 ? -47.036 2.180 8.181 1.00 13.14 ? 536 PHE A CE1 1 ATOM 4162 C CE2 . PHE A 1 536 ? -45.652 2.054 10.193 1.00 14.17 ? 536 PHE A CE2 1 ATOM 4163 C CZ . PHE A 1 536 ? -45.794 1.911 8.793 1.00 14.95 ? 536 PHE A CZ 1 ATOM 4164 N N . ASN A 1 537 ? -50.095 5.390 9.183 1.00 21.40 ? 537 ASN A N 1 ATOM 4165 C CA . ASN A 1 537 ? -50.123 5.988 7.848 1.00 20.75 ? 537 ASN A CA 1 ATOM 4166 C C . ASN A 1 537 ? -50.158 7.505 7.893 1.00 21.29 ? 537 ASN A C 1 ATOM 4167 O O . ASN A 1 537 ? -49.499 8.155 7.081 1.00 23.46 ? 537 ASN A O 1 ATOM 4168 C CB . ASN A 1 537 ? -51.292 5.440 7.018 1.00 19.79 ? 537 ASN A CB 1 ATOM 4169 C CG . ASN A 1 537 ? -51.092 3.982 6.608 1.00 18.17 ? 537 ASN A CG 1 ATOM 4170 O OD1 . ASN A 1 537 ? -50.019 3.596 6.141 1.00 15.99 ? 537 ASN A OD1 1 ATOM 4171 N ND2 . ASN A 1 537 ? -52.131 3.174 6.772 1.00 16.30 ? 537 ASN A ND2 1 ATOM 4172 N N . ARG A 1 538 ? -50.857 8.055 8.891 1.00 19.68 ? 538 ARG A N 1 ATOM 4173 C CA . ARG A 1 538 ? -50.964 9.506 9.093 1.00 19.63 ? 538 ARG A CA 1 ATOM 4174 C C . ARG A 1 538 ? -49.578 10.100 9.416 1.00 18.23 ? 538 ARG A C 1 ATOM 4175 O O . ARG A 1 538 ? -49.137 11.041 8.751 1.00 17.02 ? 538 ARG A O 1 ATOM 4176 C CB . ARG A 1 538 ? -51.954 9.808 10.230 1.00 19.75 ? 538 ARG A CB 1 ATOM 4177 C CG . ARG A 1 538 ? -52.190 11.282 10.538 1.00 18.62 ? 538 ARG A CG 1 ATOM 4178 C CD . ARG A 1 538 ? -52.950 11.459 11.849 1.00 19.67 ? 538 ARG A CD 1 ATOM 4179 N NE . ARG A 1 538 ? -52.212 10.965 13.013 1.00 17.74 ? 538 ARG A NE 1 ATOM 4180 C CZ . ARG A 1 538 ? -51.306 11.662 13.699 1.00 18.42 ? 538 ARG A CZ 1 ATOM 4181 N NH1 . ARG A 1 538 ? -50.995 12.908 13.353 1.00 19.40 ? 538 ARG A NH1 1 ATOM 4182 N NH2 . ARG A 1 538 ? -50.714 11.111 14.747 1.00 17.49 ? 538 ARG A NH2 1 ATOM 4183 N N . VAL A 1 539 ? -48.880 9.475 10.371 1.00 16.98 ? 539 VAL A N 1 ATOM 4184 C CA . VAL A 1 539 ? -47.539 9.893 10.804 1.00 16.82 ? 539 VAL A CA 1 ATOM 4185 C C . VAL A 1 539 ? -46.521 9.659 9.681 1.00 17.04 ? 539 VAL A C 1 ATOM 4186 O O . VAL A 1 539 ? -45.550 10.408 9.555 1.00 19.70 ? 539 VAL A O 1 ATOM 4187 C CB . VAL A 1 539 ? -47.090 9.162 12.120 1.00 14.09 ? 539 VAL A CB 1 ATOM 4188 C CG1 . VAL A 1 539 ? -45.720 9.639 12.578 1.00 13.41 ? 539 VAL A CG1 1 ATOM 4189 C CG2 . VAL A 1 539 ? -48.078 9.434 13.232 1.00 12.16 ? 539 VAL A CG2 1 ATOM 4190 N N . CYS A 1 540 ? -46.752 8.636 8.862 1.00 17.09 ? 540 CYS A N 1 ATOM 4191 C CA . CYS A 1 540 ? -45.858 8.354 7.743 1.00 16.32 ? 540 CYS A CA 1 ATOM 4192 C C . CYS A 1 540 ? -46.021 9.353 6.601 1.00 15.84 ? 540 CYS A C 1 ATOM 4193 O O . CYS A 1 540 ? -45.032 9.730 5.983 1.00 15.57 ? 540 CYS A O 1 ATOM 4194 C CB . CYS A 1 540 ? -45.985 6.904 7.261 1.00 17.28 ? 540 CYS A CB 1 ATOM 4195 S SG . CYS A 1 540 ? -45.095 5.694 8.303 1.00 18.58 ? 540 CYS A SG 1 ATOM 4196 N N . ASP A 1 541 ? -47.248 9.845 6.396 1.00 15.29 ? 541 ASP A N 1 ATOM 4197 C CA . ASP A 1 541 ? -47.537 10.841 5.349 1.00 15.87 ? 541 ASP A CA 1 ATOM 4198 C C . ASP A 1 541 ? -46.973 12.219 5.718 1.00 13.90 ? 541 ASP A C 1 ATOM 4199 O O . ASP A 1 541 ? -46.412 12.915 4.872 1.00 12.88 ? 541 ASP A O 1 ATOM 4200 C CB . ASP A 1 541 ? -49.050 10.949 5.085 1.00 16.86 ? 541 ASP A CB 1 ATOM 4201 C CG . ASP A 1 541 ? -49.621 9.731 4.347 1.00 20.26 ? 541 ASP A CG 1 ATOM 4202 O OD1 . ASP A 1 541 ? -48.853 8.912 3.785 1.00 21.42 ? 541 ASP A OD1 1 ATOM 4203 O OD2 . ASP A 1 541 ? -50.862 9.592 4.335 1.00 22.12 ? 541 ASP A OD2 1 ATOM 4204 N N . GLU A 1 542 ? -47.066 12.556 7.006 1.00 13.10 ? 542 GLU A N 1 ATOM 4205 C CA . GLU A 1 542 ? -46.578 13.825 7.547 1.00 11.90 ? 542 GLU A CA 1 ATOM 4206 C C . GLU A 1 542 ? -45.045 13.883 7.588 1.00 10.50 ? 542 GLU A C 1 ATOM 4207 O O . GLU A 1 542 ? -44.460 14.955 7.419 1.00 10.11 ? 542 GLU A O 1 ATOM 4208 C CB . GLU A 1 542 ? -47.153 14.055 8.950 1.00 14.94 ? 542 GLU A CB 1 ATOM 4209 C CG . GLU A 1 542 ? -48.633 14.430 9.006 1.00 16.27 ? 542 GLU A CG 1 ATOM 4210 C CD . GLU A 1 542 ? -49.184 14.488 10.436 1.00 19.55 ? 542 GLU A CD 1 ATOM 4211 O OE1 . GLU A 1 542 ? -48.445 14.879 11.370 1.00 20.94 ? 542 GLU A OE1 1 ATOM 4212 O OE2 . GLU A 1 542 ? -50.376 14.158 10.624 1.00 21.60 ? 542 GLU A OE2 1 ATOM 4213 N N . TRP A 1 543 ? -44.417 12.723 7.809 1.00 7.94 ? 543 TRP A N 1 ATOM 4214 C CA . TRP A 1 543 ? -42.965 12.587 7.860 1.00 7.24 ? 543 TRP A CA 1 ATOM 4215 C C . TRP A 1 543 ? -42.369 12.607 6.457 1.00 9.15 ? 543 TRP A C 1 ATOM 4216 O O . TRP A 1 543 ? -41.324 13.227 6.244 1.00 11.15 ? 543 TRP A O 1 ATOM 4217 C CB . TRP A 1 543 ? -42.546 11.299 8.613 1.00 7.69 ? 543 TRP A CB 1 ATOM 4218 C CG . TRP A 1 543 ? -41.050 10.955 8.547 1.00 8.29 ? 543 TRP A CG 1 ATOM 4219 C CD1 . TRP A 1 543 ? -40.470 9.957 7.799 1.00 10.17 ? 543 TRP A CD1 1 ATOM 4220 C CD2 . TRP A 1 543 ? -39.961 11.676 9.158 1.00 11.12 ? 543 TRP A CD2 1 ATOM 4221 N NE1 . TRP A 1 543 ? -39.097 10.023 7.891 1.00 11.65 ? 543 TRP A NE1 1 ATOM 4222 C CE2 . TRP A 1 543 ? -38.753 11.062 8.716 1.00 10.18 ? 543 TRP A CE2 1 ATOM 4223 C CE3 . TRP A 1 543 ? -39.882 12.788 10.031 1.00 9.69 ? 543 TRP A CE3 1 ATOM 4224 C CZ2 . TRP A 1 543 ? -37.480 11.518 9.119 1.00 11.02 ? 543 TRP A CZ2 1 ATOM 4225 C CZ3 . TRP A 1 543 ? -38.610 13.247 10.434 1.00 9.77 ? 543 TRP A CZ3 1 ATOM 4226 C CH2 . TRP A 1 543 ? -37.427 12.608 9.975 1.00 12.16 ? 543 TRP A CH2 1 ATOM 4227 N N . ARG A 1 544 ? -43.004 11.894 5.524 1.00 10.43 ? 544 ARG A N 1 ATOM 4228 C CA . ARG A 1 544 ? -42.535 11.844 4.139 1.00 13.04 ? 544 ARG A CA 1 ATOM 4229 C C . ARG A 1 544 ? -42.656 13.198 3.449 1.00 13.77 ? 544 ARG A C 1 ATOM 4230 O O . ARG A 1 544 ? -41.838 13.521 2.593 1.00 15.08 ? 544 ARG A O 1 ATOM 4231 C CB . ARG A 1 544 ? -43.238 10.741 3.340 1.00 14.97 ? 544 ARG A CB 1 ATOM 4232 C CG . ARG A 1 544 ? -42.673 9.329 3.613 1.00 17.51 ? 544 ARG A CG 1 ATOM 4233 C CD . ARG A 1 544 ? -43.162 8.271 2.618 1.00 19.47 ? 544 ARG A CD 1 ATOM 4234 N NE . ARG A 1 544 ? -44.612 8.082 2.672 1.00 22.64 ? 544 ARG A NE 1 ATOM 4235 C CZ . ARG A 1 544 ? -45.240 7.152 3.391 1.00 24.85 ? 544 ARG A CZ 1 ATOM 4236 N NH1 . ARG A 1 544 ? -44.562 6.284 4.139 1.00 22.95 ? 544 ARG A NH1 1 ATOM 4237 N NH2 . ARG A 1 544 ? -46.565 7.119 3.388 1.00 27.41 ? 544 ARG A NH2 1 ATOM 4238 N N . ALA A 1 545 ? -43.624 14.007 3.894 1.00 15.14 ? 545 ALA A N 1 ATOM 4239 C CA . ALA A 1 545 ? -43.843 15.363 3.372 1.00 14.99 ? 545 ALA A CA 1 ATOM 4240 C C . ALA A 1 545 ? -42.786 16.327 3.947 1.00 16.48 ? 545 ALA A C 1 ATOM 4241 O O . ALA A 1 545 ? -42.283 17.207 3.235 1.00 15.11 ? 545 ALA A O 1 ATOM 4242 C CB . ALA A 1 545 ? -45.240 15.847 3.720 1.00 14.31 ? 545 ALA A CB 1 ATOM 4243 N N . TYR A 1 546 ? -42.431 16.123 5.223 1.00 15.71 ? 546 TYR A N 1 ATOM 4244 C CA . TYR A 1 546 ? -41.426 16.938 5.904 1.00 14.66 ? 546 TYR A CA 1 ATOM 4245 C C . TYR A 1 546 ? -39.988 16.671 5.421 1.00 16.01 ? 546 TYR A C 1 ATOM 4246 O O . TYR A 1 546 ? -39.226 17.618 5.234 1.00 16.54 ? 546 TYR A O 1 ATOM 4247 C CB . TYR A 1 546 ? -41.498 16.770 7.455 1.00 12.63 ? 546 TYR A CB 1 ATOM 4248 C CG . TYR A 1 546 ? -40.289 17.368 8.174 1.00 9.95 ? 546 TYR A CG 1 ATOM 4249 C CD1 . TYR A 1 546 ? -40.135 18.770 8.285 1.00 7.10 ? 546 TYR A CD1 1 ATOM 4250 C CD2 . TYR A 1 546 ? -39.187 16.548 8.526 1.00 8.34 ? 546 TYR A CD2 1 ATOM 4251 C CE1 . TYR A 1 546 ? -38.906 19.342 8.698 1.00 7.75 ? 546 TYR A CE1 1 ATOM 4252 C CE2 . TYR A 1 546 ? -37.958 17.108 8.933 1.00 8.46 ? 546 TYR A CE2 1 ATOM 4253 C CZ . TYR A 1 546 ? -37.825 18.502 9.013 1.00 8.76 ? 546 TYR A CZ 1 ATOM 4254 O OH . TYR A 1 546 ? -36.617 19.036 9.393 1.00 8.81 ? 546 TYR A OH 1 ATOM 4255 N N . TRP A 1 547 ? -39.614 15.393 5.301 1.00 17.22 ? 547 TRP A N 1 ATOM 4256 C CA . TRP A 1 547 ? -38.255 14.977 4.918 1.00 19.43 ? 547 TRP A CA 1 ATOM 4257 C C . TRP A 1 547 ? -37.474 15.723 3.798 1.00 20.81 ? 547 TRP A C 1 ATOM 4258 O O . TRP A 1 547 ? -36.288 16.017 4.002 1.00 21.50 ? 547 TRP A O 1 ATOM 4259 C CB . TRP A 1 547 ? -38.164 13.430 4.797 1.00 19.63 ? 547 TRP A CB 1 ATOM 4260 C CG . TRP A 1 547 ? -36.762 12.854 4.538 1.00 22.37 ? 547 TRP A CG 1 ATOM 4261 C CD1 . TRP A 1 547 ? -36.317 12.284 3.371 1.00 23.95 ? 547 TRP A CD1 1 ATOM 4262 C CD2 . TRP A 1 547 ? -35.637 12.846 5.437 1.00 23.44 ? 547 TRP A CD2 1 ATOM 4263 N NE1 . TRP A 1 547 ? -34.993 11.935 3.481 1.00 23.81 ? 547 TRP A NE1 1 ATOM 4264 C CE2 . TRP A 1 547 ? -34.545 12.264 4.732 1.00 23.55 ? 547 TRP A CE2 1 ATOM 4265 C CE3 . TRP A 1 547 ? -35.437 13.276 6.769 1.00 23.47 ? 547 TRP A CE3 1 ATOM 4266 C CZ2 . TRP A 1 547 ? -33.263 12.100 5.313 1.00 22.59 ? 547 TRP A CZ2 1 ATOM 4267 C CZ3 . TRP A 1 547 ? -34.157 13.114 7.353 1.00 23.57 ? 547 TRP A CZ3 1 ATOM 4268 C CH2 . TRP A 1 547 ? -33.088 12.529 6.615 1.00 22.33 ? 547 TRP A CH2 1 ATOM 4269 N N . PRO A 1 548 ? -38.105 16.064 2.640 1.00 20.20 ? 548 PRO A N 1 ATOM 4270 C CA . PRO A 1 548 ? -37.320 16.775 1.614 1.00 21.63 ? 548 PRO A CA 1 ATOM 4271 C C . PRO A 1 548 ? -36.854 18.187 2.008 1.00 22.95 ? 548 PRO A C 1 ATOM 4272 O O . PRO A 1 548 ? -35.926 18.727 1.396 1.00 21.99 ? 548 PRO A O 1 ATOM 4273 C CB . PRO A 1 548 ? -38.285 16.830 0.434 1.00 21.87 ? 548 PRO A CB 1 ATOM 4274 C CG . PRO A 1 548 ? -39.081 15.597 0.604 1.00 22.28 ? 548 PRO A CG 1 ATOM 4275 C CD . PRO A 1 548 ? -39.396 15.651 2.062 1.00 20.27 ? 548 PRO A CD 1 ATOM 4276 N N . THR A 1 549 ? -37.476 18.734 3.062 1.00 24.24 ? 549 THR A N 1 ATOM 4277 C CA . THR A 1 549 ? -37.177 20.074 3.588 1.00 23.98 ? 549 THR A CA 1 ATOM 4278 C C . THR A 1 549 ? -36.118 20.067 4.693 1.00 23.93 ? 549 THR A C 1 ATOM 4279 O O . THR A 1 549 ? -35.633 21.136 5.089 1.00 23.55 ? 549 THR A O 1 ATOM 4280 C CB . THR A 1 549 ? -38.459 20.810 4.136 1.00 25.36 ? 549 THR A CB 1 ATOM 4281 O OG1 . THR A 1 549 ? -38.881 20.224 5.379 1.00 24.80 ? 549 THR A OG1 1 ATOM 4282 C CG2 . THR A 1 549 ? -39.613 20.753 3.125 1.00 22.10 ? 549 THR A CG2 1 ATOM 4283 N N . ASN A 1 550 ? -35.793 18.871 5.201 1.00 23.69 ? 550 ASN A N 1 ATOM 4284 C CA . ASN A 1 550 ? -34.790 18.684 6.257 1.00 22.76 ? 550 ASN A CA 1 ATOM 4285 C C . ASN A 1 550 ? -33.408 19.043 5.684 1.00 23.83 ? 550 ASN A C 1 ATOM 4286 O O . ASN A 1 550 ? -33.023 18.514 4.638 1.00 25.53 ? 550 ASN A O 1 ATOM 4287 C CB . ASN A 1 550 ? -34.806 17.229 6.755 1.00 21.79 ? 550 ASN A CB 1 ATOM 4288 C CG . ASN A 1 550 ? -34.080 17.045 8.093 1.00 22.20 ? 550 ASN A CG 1 ATOM 4289 O OD1 . ASN A 1 550 ? -33.091 16.314 8.186 1.00 20.77 ? 550 ASN A OD1 1 ATOM 4290 N ND2 . ASN A 1 550 ? -34.573 17.707 9.126 1.00 19.01 ? 550 ASN A ND2 1 ATOM 4291 N N . PRO A 1 551 ? -32.670 19.975 6.337 1.00 24.43 ? 551 PRO A N 1 ATOM 4292 C CA . PRO A 1 551 ? -31.341 20.394 5.866 1.00 24.37 ? 551 PRO A CA 1 ATOM 4293 C C . PRO A 1 551 ? -30.179 19.449 6.184 1.00 24.34 ? 551 PRO A C 1 ATOM 4294 O O . PRO A 1 551 ? -29.036 19.708 5.785 1.00 24.94 ? 551 PRO A O 1 ATOM 4295 C CB . PRO A 1 551 ? -31.160 21.748 6.554 1.00 24.88 ? 551 PRO A CB 1 ATOM 4296 C CG . PRO A 1 551 ? -31.821 21.533 7.872 1.00 24.16 ? 551 PRO A CG 1 ATOM 4297 C CD . PRO A 1 551 ? -33.089 20.801 7.492 1.00 24.18 ? 551 PRO A CD 1 ATOM 4298 N N . TYR A 1 552 ? -30.475 18.380 6.923 1.00 23.60 ? 552 TYR A N 1 ATOM 4299 C CA . TYR A 1 552 ? -29.467 17.398 7.327 1.00 23.99 ? 552 TYR A CA 1 ATOM 4300 C C . TYR A 1 552 ? -29.766 15.994 6.788 1.00 23.35 ? 552 TYR A C 1 ATOM 4301 O O . TYR A 1 552 ? -30.938 15.642 6.607 1.00 22.75 ? 552 TYR A O 1 ATOM 4302 C CB . TYR A 1 552 ? -29.369 17.327 8.870 1.00 21.89 ? 552 TYR A CB 1 ATOM 4303 C CG . TYR A 1 552 ? -29.041 18.632 9.585 1.00 21.68 ? 552 TYR A CG 1 ATOM 4304 C CD1 . TYR A 1 552 ? -27.969 19.460 9.161 1.00 20.94 ? 552 TYR A CD1 1 ATOM 4305 C CD2 . TYR A 1 552 ? -29.802 19.049 10.695 1.00 19.94 ? 552 TYR A CD2 1 ATOM 4306 C CE1 . TYR A 1 552 ? -27.672 20.679 9.831 1.00 20.09 ? 552 TYR A CE1 1 ATOM 4307 C CE2 . TYR A 1 552 ? -29.512 20.264 11.376 1.00 19.98 ? 552 TYR A CE2 1 ATOM 4308 C CZ . TYR A 1 552 ? -28.452 21.069 10.935 1.00 20.95 ? 552 TYR A CZ 1 ATOM 4309 O OH . TYR A 1 552 ? -28.190 22.254 11.581 1.00 22.62 ? 552 TYR A OH 1 ATOM 4310 N N . PRO A 1 553 ? -28.714 15.214 6.429 1.00 24.19 ? 553 PRO A N 1 ATOM 4311 C CA . PRO A 1 553 ? -28.922 13.846 5.919 1.00 24.95 ? 553 PRO A CA 1 ATOM 4312 C C . PRO A 1 553 ? -28.912 12.810 7.062 1.00 25.54 ? 553 PRO A C 1 ATOM 4313 O O . PRO A 1 553 ? -28.736 13.161 8.233 1.00 23.95 ? 553 PRO A O 1 ATOM 4314 C CB . PRO A 1 553 ? -27.725 13.652 4.990 1.00 24.35 ? 553 PRO A CB 1 ATOM 4315 C CG . PRO A 1 553 ? -26.638 14.397 5.698 1.00 23.43 ? 553 PRO A CG 1 ATOM 4316 C CD . PRO A 1 553 ? -27.337 15.670 6.122 1.00 23.72 ? 553 PRO A CD 1 ATOM 4317 N N . LYS A 1 554 ? -29.102 11.543 6.707 1.00 27.64 ? 554 LYS A N 1 ATOM 4318 C CA . LYS A 1 554 ? -29.080 10.437 7.668 1.00 28.63 ? 554 LYS A CA 1 ATOM 4319 C C . LYS A 1 554 ? -27.680 9.831 7.535 1.00 29.80 ? 554 LYS A C 1 ATOM 4320 O O . LYS A 1 554 ? -27.360 9.213 6.512 1.00 31.02 ? 554 LYS A O 1 ATOM 4321 C CB . LYS A 1 554 ? -30.172 9.426 7.297 1.00 28.90 ? 554 LYS A CB 1 ATOM 4322 C CG . LYS A 1 554 ? -30.276 8.151 8.135 1.00 25.79 ? 554 LYS A CG 1 ATOM 4323 C CD . LYS A 1 554 ? -31.475 7.373 7.619 1.00 24.48 ? 554 LYS A CD 1 ATOM 4324 C CE . LYS A 1 554 ? -31.670 6.033 8.272 1.00 20.59 ? 554 LYS A CE 1 ATOM 4325 N NZ . LYS A 1 554 ? -30.794 4.990 7.705 1.00 17.65 ? 554 LYS A NZ 1 ATOM 4326 N N . ILE A 1 555 ? -26.836 10.077 8.538 1.00 30.37 ? 555 ILE A N 1 ATOM 4327 C CA . ILE A 1 555 ? -25.452 9.583 8.543 1.00 30.52 ? 555 ILE A CA 1 ATOM 4328 C C . ILE A 1 555 ? -25.236 8.203 9.169 1.00 29.05 ? 555 ILE A C 1 ATOM 4329 O O . ILE A 1 555 ? -24.176 7.601 8.983 1.00 28.69 ? 555 ILE A O 1 ATOM 4330 C CB . ILE A 1 555 ? -24.464 10.604 9.198 1.00 31.64 ? 555 ILE A CB 1 ATOM 4331 C CG1 . ILE A 1 555 ? -24.909 10.965 10.631 1.00 34.10 ? 555 ILE A CG1 1 ATOM 4332 C CG2 . ILE A 1 555 ? -24.335 11.838 8.309 1.00 32.38 ? 555 ILE A CG2 1 ATOM 4333 C CD1 . ILE A 1 555 ? -23.818 11.572 11.515 1.00 33.76 ? 555 ILE A CD1 1 ATOM 4334 N N . ASP A 1 556 ? -26.229 7.716 9.913 1.00 27.41 ? 556 ASP A N 1 ATOM 4335 C CA . ASP A 1 556 ? -26.132 6.415 10.563 1.00 27.11 ? 556 ASP A CA 1 ATOM 4336 C C . ASP A 1 556 ? -27.239 5.429 10.185 1.00 26.86 ? 556 ASP A C 1 ATOM 4337 O O . ASP A 1 556 ? -27.945 5.637 9.199 1.00 28.42 ? 556 ASP A O 1 ATOM 4338 C CB . ASP A 1 556 ? -25.991 6.575 12.097 1.00 28.29 ? 556 ASP A CB 1 ATOM 4339 C CG . ASP A 1 556 ? -27.140 7.352 12.753 1.00 29.83 ? 556 ASP A CG 1 ATOM 4340 O OD1 . ASP A 1 556 ? -28.192 7.597 12.118 1.00 31.75 ? 556 ASP A OD1 1 ATOM 4341 O OD2 . ASP A 1 556 ? -26.984 7.713 13.938 1.00 29.07 ? 556 ASP A OD2 1 ATOM 4342 N N . SER A 1 557 ? -27.395 4.378 10.994 1.00 25.93 ? 557 SER A N 1 ATOM 4343 C CA . SER A 1 557 ? -28.389 3.321 10.796 1.00 25.28 ? 557 SER A CA 1 ATOM 4344 C C . SER A 1 557 ? -29.837 3.785 10.864 1.00 25.90 ? 557 SER A C 1 ATOM 4345 O O . SER A 1 557 ? -30.684 3.320 10.102 1.00 25.09 ? 557 SER A O 1 ATOM 4346 C CB . SER A 1 557 ? -28.197 2.226 11.842 1.00 24.88 ? 557 SER A CB 1 ATOM 4347 O OG . SER A 1 557 ? -28.524 2.687 13.144 1.00 23.99 ? 557 SER A OG 1 ATOM 4348 N N . GLY A 1 558 ? -30.104 4.679 11.812 1.00 26.78 ? 558 GLY A N 1 ATOM 4349 C CA . GLY A 1 558 ? -31.444 5.190 12.012 1.00 26.70 ? 558 GLY A CA 1 ATOM 4350 C C . GLY A 1 558 ? -32.054 4.597 13.259 1.00 26.57 ? 558 GLY A C 1 ATOM 4351 O O . GLY A 1 558 ? -33.128 5.016 13.696 1.00 27.00 ? 558 GLY A O 1 ATOM 4352 N N . ALA A 1 559 ? -31.367 3.596 13.806 1.00 26.42 ? 559 ALA A N 1 ATOM 4353 C CA . ALA A 1 559 ? -31.779 2.914 15.025 1.00 26.52 ? 559 ALA A CA 1 ATOM 4354 C C . ALA A 1 559 ? -30.854 3.308 16.185 1.00 28.02 ? 559 ALA A C 1 ATOM 4355 O O . ALA A 1 559 ? -29.797 3.923 15.903 1.00 29.27 ? 559 ALA A O 1 ATOM 4356 C CB . ALA A 1 559 ? -31.768 1.413 14.807 1.00 25.64 ? 559 ALA A CB 1 ATOM 4357 O OXT . ALA A 1 559 ? -31.198 3.023 17.357 1.00 27.89 ? 559 ALA A OXT 1 ATOM 4358 N N . PRO B 1 2 ? 36.429 0.133 44.718 1.00 63.29 ? 2 PRO B N 1 ATOM 4359 C CA . PRO B 1 2 ? 35.648 -0.337 45.887 1.00 62.92 ? 2 PRO B CA 1 ATOM 4360 C C . PRO B 1 2 ? 36.443 -0.210 47.198 1.00 62.88 ? 2 PRO B C 1 ATOM 4361 O O . PRO B 1 2 ? 36.496 -1.144 48.011 1.00 63.21 ? 2 PRO B O 1 ATOM 4362 C CB . PRO B 1 2 ? 35.259 -1.785 45.594 1.00 63.33 ? 2 PRO B CB 1 ATOM 4363 C CG . PRO B 1 2 ? 36.344 -2.206 44.592 1.00 63.63 ? 2 PRO B CG 1 ATOM 4364 C CD . PRO B 1 2 ? 36.581 -0.959 43.738 1.00 63.14 ? 2 PRO B CD 1 ATOM 4365 N N . THR B 1 3 ? 37.033 0.969 47.400 1.00 61.87 ? 3 THR B N 1 ATOM 4366 C CA . THR B 1 3 ? 37.838 1.254 48.590 1.00 60.09 ? 3 THR B CA 1 ATOM 4367 C C . THR B 1 3 ? 37.071 1.901 49.753 1.00 57.73 ? 3 THR B C 1 ATOM 4368 O O . THR B 1 3 ? 36.929 1.287 50.813 1.00 57.93 ? 3 THR B O 1 ATOM 4369 C CB . THR B 1 3 ? 39.103 2.107 48.239 1.00 61.16 ? 3 THR B CB 1 ATOM 4370 O OG1 . THR B 1 3 ? 38.728 3.241 47.444 1.00 61.33 ? 3 THR B OG1 1 ATOM 4371 C CG2 . THR B 1 3 ? 40.131 1.272 47.480 1.00 60.87 ? 3 THR B CG2 1 ATOM 4372 N N . CYS B 1 4 ? 36.552 3.113 49.528 1.00 54.66 ? 4 CYS B N 1 ATOM 4373 C CA . CYS B 1 4 ? 35.814 3.884 50.540 1.00 50.84 ? 4 CYS B CA 1 ATOM 4374 C C . CYS B 1 4 ? 34.285 3.705 50.564 1.00 48.31 ? 4 CYS B C 1 ATOM 4375 O O . CYS B 1 4 ? 33.570 4.506 51.183 1.00 47.13 ? 4 CYS B O 1 ATOM 4376 C CB . CYS B 1 4 ? 36.177 5.375 50.418 1.00 49.92 ? 4 CYS B CB 1 ATOM 4377 S SG . CYS B 1 4 ? 35.846 6.089 48.774 1.00 48.08 ? 4 CYS B SG 1 ATOM 4378 N N . ASN B 1 5 ? 33.796 2.644 49.916 1.00 45.26 ? 5 ASN B N 1 ATOM 4379 C CA . ASN B 1 5 ? 32.361 2.342 49.862 1.00 42.64 ? 5 ASN B CA 1 ATOM 4380 C C . ASN B 1 5 ? 31.977 1.431 51.029 1.00 40.84 ? 5 ASN B C 1 ATOM 4381 O O . ASN B 1 5 ? 32.272 0.232 51.028 1.00 40.65 ? 5 ASN B O 1 ATOM 4382 C CB . ASN B 1 5 ? 31.985 1.700 48.516 1.00 40.92 ? 5 ASN B CB 1 ATOM 4383 C CG . ASN B 1 5 ? 30.491 1.786 48.213 1.00 38.80 ? 5 ASN B CG 1 ATOM 4384 O OD1 . ASN B 1 5 ? 29.780 0.786 48.252 1.00 38.36 ? 5 ASN B OD1 1 ATOM 4385 N ND2 . ASN B 1 5 ? 30.022 2.978 47.881 1.00 37.27 ? 5 ASN B ND2 1 ATOM 4386 N N . THR B 1 6 ? 31.356 2.046 52.034 1.00 39.50 ? 6 THR B N 1 ATOM 4387 C CA . THR B 1 6 ? 30.906 1.386 53.265 1.00 37.31 ? 6 THR B CA 1 ATOM 4388 C C . THR B 1 6 ? 29.385 1.591 53.398 1.00 34.94 ? 6 THR B C 1 ATOM 4389 O O . THR B 1 6 ? 28.828 2.434 52.691 1.00 33.26 ? 6 THR B O 1 ATOM 4390 C CB . THR B 1 6 ? 31.631 2.012 54.519 1.00 37.68 ? 6 THR B CB 1 ATOM 4391 O OG1 . THR B 1 6 ? 31.471 3.439 54.522 1.00 39.78 ? 6 THR B OG1 1 ATOM 4392 C CG2 . THR B 1 6 ? 33.110 1.660 54.534 1.00 38.86 ? 6 THR B CG2 1 ATOM 4393 N N . PRO B 1 7 ? 28.679 0.776 54.230 1.00 33.57 ? 7 PRO B N 1 ATOM 4394 C CA . PRO B 1 7 ? 27.231 0.967 54.382 1.00 33.11 ? 7 PRO B CA 1 ATOM 4395 C C . PRO B 1 7 ? 26.812 2.372 54.818 1.00 33.03 ? 7 PRO B C 1 ATOM 4396 O O . PRO B 1 7 ? 25.775 2.875 54.384 1.00 33.57 ? 7 PRO B O 1 ATOM 4397 C CB . PRO B 1 7 ? 26.872 -0.075 55.429 1.00 33.17 ? 7 PRO B CB 1 ATOM 4398 C CG . PRO B 1 7 ? 27.696 -1.205 55.014 1.00 32.43 ? 7 PRO B CG 1 ATOM 4399 C CD . PRO B 1 7 ? 29.045 -0.549 54.781 1.00 33.80 ? 7 PRO B CD 1 ATOM 4400 N N . SER B 1 8 ? 27.666 3.011 55.615 1.00 32.08 ? 8 SER B N 1 ATOM 4401 C CA . SER B 1 8 ? 27.438 4.365 56.113 1.00 32.11 ? 8 SER B CA 1 ATOM 4402 C C . SER B 1 8 ? 27.804 5.448 55.085 1.00 31.81 ? 8 SER B C 1 ATOM 4403 O O . SER B 1 8 ? 27.256 6.555 55.114 1.00 32.41 ? 8 SER B O 1 ATOM 4404 C CB . SER B 1 8 ? 28.214 4.579 57.414 1.00 31.92 ? 8 SER B CB 1 ATOM 4405 O OG . SER B 1 8 ? 29.573 4.211 57.266 1.00 31.69 ? 8 SER B OG 1 ATOM 4406 N N . ASN B 1 9 ? 28.718 5.119 54.176 1.00 31.22 ? 9 ASN B N 1 ATOM 4407 C CA . ASN B 1 9 ? 29.147 6.054 53.141 1.00 31.16 ? 9 ASN B CA 1 ATOM 4408 C C . ASN B 1 9 ? 29.144 5.370 51.774 1.00 30.72 ? 9 ASN B C 1 ATOM 4409 O O . ASN B 1 9 ? 30.158 4.828 51.317 1.00 31.64 ? 9 ASN B O 1 ATOM 4410 C CB . ASN B 1 9 ? 30.530 6.642 53.475 1.00 31.22 ? 9 ASN B CB 1 ATOM 4411 C CG . ASN B 1 9 ? 30.936 7.795 52.548 1.00 31.51 ? 9 ASN B CG 1 ATOM 4412 O OD1 . ASN B 1 9 ? 30.095 8.433 51.905 1.00 31.94 ? 9 ASN B OD1 1 ATOM 4413 N ND2 . ASN B 1 9 ? 32.235 8.062 52.483 1.00 30.48 ? 9 ASN B ND2 1 ATOM 4414 N N . ARG B 1 10 ? 27.972 5.369 51.148 1.00 29.56 ? 10 ARG B N 1 ATOM 4415 C CA . ARG B 1 10 ? 27.789 4.774 49.831 1.00 27.76 ? 10 ARG B CA 1 ATOM 4416 C C . ARG B 1 10 ? 28.045 5.790 48.734 1.00 26.82 ? 10 ARG B C 1 ATOM 4417 O O . ARG B 1 10 ? 28.112 5.435 47.565 1.00 25.61 ? 10 ARG B O 1 ATOM 4418 C CB . ARG B 1 10 ? 26.382 4.196 49.695 1.00 26.70 ? 10 ARG B CB 1 ATOM 4419 C CG . ARG B 1 10 ? 26.150 2.942 50.495 1.00 24.73 ? 10 ARG B CG 1 ATOM 4420 C CD . ARG B 1 10 ? 26.953 1.775 49.971 1.00 23.08 ? 10 ARG B CD 1 ATOM 4421 N NE . ARG B 1 10 ? 26.549 0.545 50.635 1.00 22.31 ? 10 ARG B NE 1 ATOM 4422 C CZ . ARG B 1 10 ? 27.245 -0.586 50.635 1.00 23.07 ? 10 ARG B CZ 1 ATOM 4423 N NH1 . ARG B 1 10 ? 28.408 -0.672 50.004 1.00 20.56 ? 10 ARG B NH1 1 ATOM 4424 N NH2 . ARG B 1 10 ? 26.759 -1.645 51.269 1.00 25.59 ? 10 ARG B NH2 1 ATOM 4425 N N . ALA B 1 11 ? 28.215 7.048 49.139 1.00 28.34 ? 11 ALA B N 1 ATOM 4426 C CA . ALA B 1 11 ? 28.486 8.164 48.237 1.00 29.75 ? 11 ALA B CA 1 ATOM 4427 C C . ALA B 1 11 ? 29.904 8.119 47.650 1.00 30.76 ? 11 ALA B C 1 ATOM 4428 O O . ALA B 1 11 ? 30.117 8.568 46.528 1.00 32.19 ? 11 ALA B O 1 ATOM 4429 C CB . ALA B 1 11 ? 28.253 9.490 48.964 1.00 28.68 ? 11 ALA B CB 1 ATOM 4430 N N . CYS B 1 12 ? 30.836 7.516 48.395 1.00 31.83 ? 12 CYS B N 1 ATOM 4431 C CA . CYS B 1 12 ? 32.253 7.379 48.023 1.00 33.42 ? 12 CYS B CA 1 ATOM 4432 C C . CYS B 1 12 ? 32.524 6.073 47.271 1.00 31.73 ? 12 CYS B C 1 ATOM 4433 O O . CYS B 1 12 ? 31.825 5.081 47.479 1.00 31.33 ? 12 CYS B O 1 ATOM 4434 C CB . CYS B 1 12 ? 33.105 7.398 49.303 1.00 37.51 ? 12 CYS B CB 1 ATOM 4435 S SG . CYS B 1 12 ? 34.871 7.836 49.146 1.00 46.10 ? 12 CYS B SG 1 ATOM 4436 N N . TRP B 1 13 ? 33.557 6.071 46.425 1.00 29.97 ? 13 TRP B N 1 ATOM 4437 C CA . TRP B 1 13 ? 33.936 4.876 45.662 1.00 29.04 ? 13 TRP B CA 1 ATOM 4438 C C . TRP B 1 13 ? 35.461 4.653 45.640 1.00 29.58 ? 13 TRP B C 1 ATOM 4439 O O . TRP B 1 13 ? 35.943 3.605 46.083 1.00 28.70 ? 13 TRP B O 1 ATOM 4440 C CB . TRP B 1 13 ? 33.324 4.918 44.242 1.00 27.25 ? 13 TRP B CB 1 ATOM 4441 C CG . TRP B 1 13 ? 33.444 3.631 43.462 1.00 23.60 ? 13 TRP B CG 1 ATOM 4442 C CD1 . TRP B 1 13 ? 34.211 3.426 42.355 1.00 24.45 ? 13 TRP B CD1 1 ATOM 4443 C CD2 . TRP B 1 13 ? 32.828 2.368 43.761 1.00 21.32 ? 13 TRP B CD2 1 ATOM 4444 N NE1 . TRP B 1 13 ? 34.126 2.117 41.949 1.00 24.66 ? 13 TRP B NE1 1 ATOM 4445 C CE2 . TRP B 1 13 ? 33.284 1.442 42.791 1.00 21.53 ? 13 TRP B CE2 1 ATOM 4446 C CE3 . TRP B 1 13 ? 31.938 1.921 44.758 1.00 20.93 ? 13 TRP B CE3 1 ATOM 4447 C CZ2 . TRP B 1 13 ? 32.882 0.088 42.784 1.00 21.44 ? 13 TRP B CZ2 1 ATOM 4448 C CZ3 . TRP B 1 13 ? 31.533 0.561 44.755 1.00 19.65 ? 13 TRP B CZ3 1 ATOM 4449 C CH2 . TRP B 1 13 ? 32.009 -0.332 43.771 1.00 18.70 ? 13 TRP B CH2 1 ATOM 4450 N N . SER B 1 14 ? 36.199 5.639 45.129 1.00 30.86 ? 14 SER B N 1 ATOM 4451 C CA . SER B 1 14 ? 37.669 5.621 45.057 1.00 31.95 ? 14 SER B CA 1 ATOM 4452 C C . SER B 1 14 ? 38.161 7.061 44.859 1.00 33.68 ? 14 SER B C 1 ATOM 4453 O O . SER B 1 14 ? 37.341 7.992 44.849 1.00 35.16 ? 14 SER B O 1 ATOM 4454 C CB . SER B 1 14 ? 38.168 4.695 43.931 1.00 30.26 ? 14 SER B CB 1 ATOM 4455 O OG . SER B 1 14 ? 37.520 4.960 42.702 1.00 29.47 ? 14 SER B OG 1 ATOM 4456 N N . ASP B 1 15 ? 39.477 7.251 44.718 1.00 34.77 ? 15 ASP B N 1 ATOM 4457 C CA . ASP B 1 15 ? 40.065 8.586 44.521 1.00 37.48 ? 15 ASP B CA 1 ATOM 4458 C C . ASP B 1 15 ? 39.651 9.219 43.183 1.00 37.76 ? 15 ASP B C 1 ATOM 4459 O O . ASP B 1 15 ? 39.984 8.710 42.108 1.00 38.74 ? 15 ASP B O 1 ATOM 4460 C CB . ASP B 1 15 ? 41.600 8.537 44.636 1.00 40.72 ? 15 ASP B CB 1 ATOM 4461 C CG . ASP B 1 15 ? 42.231 9.929 44.777 1.00 44.17 ? 15 ASP B CG 1 ATOM 4462 O OD1 . ASP B 1 15 ? 42.601 10.538 43.744 1.00 44.95 ? 15 ASP B OD1 1 ATOM 4463 O OD2 . ASP B 1 15 ? 42.348 10.413 45.927 1.00 45.94 ? 15 ASP B OD2 1 ATOM 4464 N N . GLY B 1 16 ? 38.910 10.323 43.287 1.00 37.83 ? 16 GLY B N 1 ATOM 4465 C CA . GLY B 1 16 ? 38.422 11.051 42.129 1.00 35.52 ? 16 GLY B CA 1 ATOM 4466 C C . GLY B 1 16 ? 37.071 10.580 41.638 1.00 35.20 ? 16 GLY B C 1 ATOM 4467 O O . GLY B 1 16 ? 36.499 11.168 40.713 1.00 35.28 ? 16 GLY B O 1 ATOM 4468 N N . PHE B 1 17 ? 36.565 9.508 42.251 1.00 32.02 ? 17 PHE B N 1 ATOM 4469 C CA . PHE B 1 17 ? 35.296 8.919 41.848 1.00 30.10 ? 17 PHE B CA 1 ATOM 4470 C C . PHE B 1 17 ? 34.300 8.707 42.980 1.00 29.37 ? 17 PHE B C 1 ATOM 4471 O O . PHE B 1 17 ? 34.520 7.900 43.880 1.00 28.46 ? 17 PHE B O 1 ATOM 4472 C CB . PHE B 1 17 ? 35.547 7.608 41.079 1.00 28.56 ? 17 PHE B CB 1 ATOM 4473 C CG . PHE B 1 17 ? 36.366 7.787 39.829 1.00 26.62 ? 17 PHE B CG 1 ATOM 4474 C CD1 . PHE B 1 17 ? 35.791 8.342 38.668 1.00 27.63 ? 17 PHE B CD1 1 ATOM 4475 C CD2 . PHE B 1 17 ? 37.742 7.486 39.831 1.00 25.85 ? 17 PHE B CD2 1 ATOM 4476 C CE1 . PHE B 1 17 ? 36.578 8.607 37.517 1.00 26.21 ? 17 PHE B CE1 1 ATOM 4477 C CE2 . PHE B 1 17 ? 38.550 7.744 38.693 1.00 25.57 ? 17 PHE B CE2 1 ATOM 4478 C CZ . PHE B 1 17 ? 37.965 8.309 37.532 1.00 27.59 ? 17 PHE B CZ 1 ATOM 4479 N N . ASP B 1 18 ? 33.234 9.505 42.937 1.00 28.89 ? 18 ASP B N 1 ATOM 4480 C CA . ASP B 1 18 ? 32.133 9.461 43.895 1.00 28.21 ? 18 ASP B CA 1 ATOM 4481 C C . ASP B 1 18 ? 30.801 9.584 43.138 1.00 26.60 ? 18 ASP B C 1 ATOM 4482 O O . ASP B 1 18 ? 30.785 9.525 41.908 1.00 26.93 ? 18 ASP B O 1 ATOM 4483 C CB . ASP B 1 18 ? 32.285 10.532 45.012 1.00 29.97 ? 18 ASP B CB 1 ATOM 4484 C CG . ASP B 1 18 ? 32.669 11.922 44.490 1.00 31.29 ? 18 ASP B CG 1 ATOM 4485 O OD1 . ASP B 1 18 ? 32.102 12.390 43.478 1.00 31.68 ? 18 ASP B OD1 1 ATOM 4486 O OD2 . ASP B 1 18 ? 33.535 12.561 45.126 1.00 32.63 ? 18 ASP B OD2 1 ATOM 4487 N N . ILE B 1 19 ? 29.696 9.746 43.863 1.00 24.63 ? 19 ILE B N 1 ATOM 4488 C CA . ILE B 1 19 ? 28.359 9.852 43.272 1.00 23.77 ? 19 ILE B CA 1 ATOM 4489 C C . ILE B 1 19 ? 28.111 11.137 42.459 1.00 25.19 ? 19 ILE B C 1 ATOM 4490 O O . ILE B 1 19 ? 27.243 11.172 41.579 1.00 25.12 ? 19 ILE B O 1 ATOM 4491 C CB . ILE B 1 19 ? 27.262 9.645 44.386 1.00 22.90 ? 19 ILE B CB 1 ATOM 4492 C CG1 . ILE B 1 19 ? 25.865 9.439 43.783 1.00 21.27 ? 19 ILE B CG1 1 ATOM 4493 C CG2 . ILE B 1 19 ? 27.270 10.796 45.396 1.00 21.83 ? 19 ILE B CG2 1 ATOM 4494 C CD1 . ILE B 1 19 ? 25.731 8.204 42.941 1.00 18.00 ? 19 ILE B CD1 1 ATOM 4495 N N . ASN B 1 20 ? 28.925 12.155 42.719 1.00 25.84 ? 20 ASN B N 1 ATOM 4496 C CA . ASN B 1 20 ? 28.805 13.450 42.058 1.00 25.30 ? 20 ASN B CA 1 ATOM 4497 C C . ASN B 1 20 ? 29.684 13.621 40.821 1.00 24.58 ? 20 ASN B C 1 ATOM 4498 O O . ASN B 1 20 ? 29.596 14.633 40.116 1.00 26.22 ? 20 ASN B O 1 ATOM 4499 C CB . ASN B 1 20 ? 29.065 14.556 43.073 1.00 26.48 ? 20 ASN B CB 1 ATOM 4500 C CG . ASN B 1 20 ? 28.053 14.559 44.200 1.00 26.90 ? 20 ASN B CG 1 ATOM 4501 O OD1 . ASN B 1 20 ? 26.856 14.715 43.968 1.00 27.58 ? 20 ASN B OD1 1 ATOM 4502 N ND2 . ASN B 1 20 ? 28.527 14.365 45.425 1.00 26.91 ? 20 ASN B ND2 1 ATOM 4503 N N . THR B 1 21 ? 30.512 12.614 40.550 1.00 22.71 ? 21 THR B N 1 ATOM 4504 C CA . THR B 1 21 ? 31.400 12.604 39.388 1.00 20.90 ? 21 THR B CA 1 ATOM 4505 C C . THR B 1 21 ? 30.561 12.394 38.126 1.00 19.94 ? 21 THR B C 1 ATOM 4506 O O . THR B 1 21 ? 29.632 11.579 38.118 1.00 20.03 ? 21 THR B O 1 ATOM 4507 C CB . THR B 1 21 ? 32.435 11.458 39.508 1.00 20.29 ? 21 THR B CB 1 ATOM 4508 O OG1 . THR B 1 21 ? 33.210 11.651 40.695 1.00 17.00 ? 21 THR B OG1 1 ATOM 4509 C CG2 . THR B 1 21 ? 33.370 11.403 38.292 1.00 19.04 ? 21 THR B CG2 1 ATOM 4510 N N . ASP B 1 22 ? 30.863 13.170 37.089 1.00 20.08 ? 22 ASP B N 1 ATOM 4511 C CA . ASP B 1 22 ? 30.162 13.073 35.810 1.00 20.64 ? 22 ASP B CA 1 ATOM 4512 C C . ASP B 1 22 ? 30.678 11.803 35.113 1.00 20.68 ? 22 ASP B C 1 ATOM 4513 O O . ASP B 1 22 ? 31.779 11.789 34.538 1.00 19.67 ? 22 ASP B O 1 ATOM 4514 C CB . ASP B 1 22 ? 30.427 14.333 34.978 1.00 22.13 ? 22 ASP B CB 1 ATOM 4515 C CG . ASP B 1 22 ? 29.436 14.514 33.830 1.00 24.36 ? 22 ASP B CG 1 ATOM 4516 O OD1 . ASP B 1 22 ? 29.108 13.525 33.148 1.00 26.48 ? 22 ASP B OD1 1 ATOM 4517 O OD2 . ASP B 1 22 ? 29.002 15.662 33.590 1.00 27.28 ? 22 ASP B OD2 1 ATOM 4518 N N . TYR B 1 23 ? 29.894 10.729 35.251 1.00 19.20 ? 23 TYR B N 1 ATOM 4519 C CA . TYR B 1 23 ? 30.212 9.408 34.694 1.00 20.04 ? 23 TYR B CA 1 ATOM 4520 C C . TYR B 1 23 ? 30.228 9.298 33.165 1.00 20.23 ? 23 TYR B C 1 ATOM 4521 O O . TYR B 1 23 ? 30.790 8.350 32.618 1.00 20.27 ? 23 TYR B O 1 ATOM 4522 C CB . TYR B 1 23 ? 29.288 8.330 35.293 1.00 18.83 ? 23 TYR B CB 1 ATOM 4523 C CG . TYR B 1 23 ? 27.799 8.612 35.180 1.00 17.74 ? 23 TYR B CG 1 ATOM 4524 C CD1 . TYR B 1 23 ? 27.109 8.402 33.969 1.00 11.96 ? 23 TYR B CD1 1 ATOM 4525 C CD2 . TYR B 1 23 ? 27.078 9.121 36.282 1.00 16.39 ? 23 TYR B CD2 1 ATOM 4526 C CE1 . TYR B 1 23 ? 25.739 8.697 33.847 1.00 14.34 ? 23 TYR B CE1 1 ATOM 4527 C CE2 . TYR B 1 23 ? 25.692 9.417 36.173 1.00 16.59 ? 23 TYR B CE2 1 ATOM 4528 C CZ . TYR B 1 23 ? 25.036 9.203 34.946 1.00 14.47 ? 23 TYR B CZ 1 ATOM 4529 O OH . TYR B 1 23 ? 23.700 9.496 34.810 1.00 16.04 ? 23 TYR B OH 1 ATOM 4530 N N . GLU B 1 24 ? 29.570 10.245 32.496 1.00 21.21 ? 24 GLU B N 1 ATOM 4531 C CA . GLU B 1 24 ? 29.502 10.278 31.034 1.00 23.82 ? 24 GLU B CA 1 ATOM 4532 C C . GLU B 1 24 ? 30.806 10.761 30.396 1.00 23.38 ? 24 GLU B C 1 ATOM 4533 O O . GLU B 1 24 ? 31.019 10.585 29.192 1.00 24.01 ? 24 GLU B O 1 ATOM 4534 C CB . GLU B 1 24 ? 28.315 11.140 30.563 1.00 24.99 ? 24 GLU B CB 1 ATOM 4535 C CG . GLU B 1 24 ? 26.967 10.406 30.594 1.00 28.06 ? 24 GLU B CG 1 ATOM 4536 C CD . GLU B 1 24 ? 25.762 11.268 30.204 1.00 31.97 ? 24 GLU B CD 1 ATOM 4537 O OE1 . GLU B 1 24 ? 25.938 12.361 29.619 1.00 34.22 ? 24 GLU B OE1 1 ATOM 4538 O OE2 . GLU B 1 24 ? 24.618 10.842 30.480 1.00 33.28 ? 24 GLU B OE2 1 ATOM 4539 N N . VAL B 1 25 ? 31.679 11.356 31.213 1.00 23.37 ? 25 VAL B N 1 ATOM 4540 C CA . VAL B 1 25 ? 32.967 11.869 30.737 1.00 22.26 ? 25 VAL B CA 1 ATOM 4541 C C . VAL B 1 25 ? 34.213 11.348 31.494 1.00 21.99 ? 25 VAL B C 1 ATOM 4542 O O . VAL B 1 25 ? 35.335 11.443 30.983 1.00 22.92 ? 25 VAL B O 1 ATOM 4543 C CB . VAL B 1 25 ? 32.983 13.443 30.680 1.00 21.62 ? 25 VAL B CB 1 ATOM 4544 C CG1 . VAL B 1 25 ? 32.043 13.983 29.612 1.00 18.21 ? 25 VAL B CG1 1 ATOM 4545 C CG2 . VAL B 1 25 ? 32.665 14.050 32.026 1.00 20.32 ? 25 VAL B CG2 1 ATOM 4546 N N . SER B 1 26 ? 34.013 10.802 32.696 1.00 21.54 ? 26 SER B N 1 ATOM 4547 C CA . SER B 1 26 ? 35.108 10.275 33.522 1.00 20.20 ? 26 SER B CA 1 ATOM 4548 C C . SER B 1 26 ? 34.806 8.834 33.949 1.00 20.79 ? 26 SER B C 1 ATOM 4549 O O . SER B 1 26 ? 33.731 8.546 34.475 1.00 20.90 ? 26 SER B O 1 ATOM 4550 C CB . SER B 1 26 ? 35.336 11.175 34.743 1.00 19.38 ? 26 SER B CB 1 ATOM 4551 O OG . SER B 1 26 ? 36.696 11.154 35.149 1.00 16.63 ? 26 SER B OG 1 ATOM 4552 N N . THR B 1 27 ? 35.786 7.950 33.764 1.00 20.70 ? 27 THR B N 1 ATOM 4553 C CA . THR B 1 27 ? 35.638 6.520 34.054 1.00 21.05 ? 27 THR B CA 1 ATOM 4554 C C . THR B 1 27 ? 36.895 5.940 34.743 1.00 23.18 ? 27 THR B C 1 ATOM 4555 O O . THR B 1 27 ? 38.015 6.219 34.297 1.00 25.21 ? 27 THR B O 1 ATOM 4556 C CB . THR B 1 27 ? 35.381 5.752 32.699 1.00 19.44 ? 27 THR B CB 1 ATOM 4557 O OG1 . THR B 1 27 ? 34.266 6.341 32.012 1.00 18.05 ? 27 THR B OG1 1 ATOM 4558 C CG2 . THR B 1 27 ? 35.088 4.287 32.926 1.00 16.37 ? 27 THR B CG2 1 ATOM 4559 N N . PRO B 1 28 ? 36.727 5.137 35.834 1.00 22.70 ? 28 PRO B N 1 ATOM 4560 C CA . PRO B 1 28 ? 37.845 4.523 36.567 1.00 24.46 ? 28 PRO B CA 1 ATOM 4561 C C . PRO B 1 28 ? 38.688 3.550 35.751 1.00 26.30 ? 28 PRO B C 1 ATOM 4562 O O . PRO B 1 28 ? 38.159 2.642 35.100 1.00 26.68 ? 28 PRO B O 1 ATOM 4563 C CB . PRO B 1 28 ? 37.147 3.780 37.710 1.00 22.68 ? 28 PRO B CB 1 ATOM 4564 C CG . PRO B 1 28 ? 35.982 4.586 37.975 1.00 21.40 ? 28 PRO B CG 1 ATOM 4565 C CD . PRO B 1 28 ? 35.482 4.937 36.597 1.00 23.07 ? 28 PRO B CD 1 ATOM 4566 N N . ASP B 1 29 ? 40.002 3.753 35.795 1.00 27.39 ? 29 ASP B N 1 ATOM 4567 C CA . ASP B 1 29 ? 40.940 2.896 35.091 1.00 29.02 ? 29 ASP B CA 1 ATOM 4568 C C . ASP B 1 29 ? 41.283 1.716 36.021 1.00 28.95 ? 29 ASP B C 1 ATOM 4569 O O . ASP B 1 29 ? 42.205 1.794 36.837 1.00 29.72 ? 29 ASP B O 1 ATOM 4570 C CB . ASP B 1 29 ? 42.187 3.705 34.697 1.00 31.80 ? 29 ASP B CB 1 ATOM 4571 C CG . ASP B 1 29 ? 43.010 3.026 33.618 1.00 34.17 ? 29 ASP B CG 1 ATOM 4572 O OD1 . ASP B 1 29 ? 42.433 2.670 32.566 1.00 36.76 ? 29 ASP B OD1 1 ATOM 4573 O OD2 . ASP B 1 29 ? 44.231 2.847 33.821 1.00 35.39 ? 29 ASP B OD2 1 ATOM 4574 N N . THR B 1 30 ? 40.481 0.657 35.933 1.00 28.24 ? 30 THR B N 1 ATOM 4575 C CA . THR B 1 30 ? 40.677 -0.538 36.752 1.00 28.86 ? 30 THR B CA 1 ATOM 4576 C C . THR B 1 30 ? 41.572 -1.549 36.050 1.00 29.02 ? 30 THR B C 1 ATOM 4577 O O . THR B 1 30 ? 42.412 -2.182 36.690 1.00 30.11 ? 30 THR B O 1 ATOM 4578 C CB . THR B 1 30 ? 39.342 -1.249 37.092 1.00 28.23 ? 30 THR B CB 1 ATOM 4579 O OG1 . THR B 1 30 ? 38.729 -1.717 35.887 1.00 28.78 ? 30 THR B OG1 1 ATOM 4580 C CG2 . THR B 1 30 ? 38.380 -0.323 37.829 1.00 28.35 ? 30 THR B CG2 1 ATOM 4581 N N . GLY B 1 31 ? 41.355 -1.709 34.742 1.00 28.91 ? 31 GLY B N 1 ATOM 4582 C CA . GLY B 1 31 ? 42.120 -2.655 33.941 1.00 28.21 ? 31 GLY B CA 1 ATOM 4583 C C . GLY B 1 31 ? 41.712 -4.102 34.183 1.00 27.17 ? 31 GLY B C 1 ATOM 4584 O O . GLY B 1 31 ? 42.520 -5.015 33.996 1.00 28.53 ? 31 GLY B O 1 ATOM 4585 N N . VAL B 1 32 ? 40.482 -4.294 34.662 1.00 25.43 ? 32 VAL B N 1 ATOM 4586 C CA . VAL B 1 32 ? 39.916 -5.615 34.951 1.00 23.50 ? 32 VAL B CA 1 ATOM 4587 C C . VAL B 1 32 ? 38.887 -5.952 33.875 1.00 23.03 ? 32 VAL B C 1 ATOM 4588 O O . VAL B 1 32 ? 38.132 -5.083 33.423 1.00 22.80 ? 32 VAL B O 1 ATOM 4589 C CB . VAL B 1 32 ? 39.224 -5.654 36.367 1.00 23.19 ? 32 VAL B CB 1 ATOM 4590 C CG1 . VAL B 1 32 ? 38.516 -6.996 36.630 1.00 21.73 ? 32 VAL B CG1 1 ATOM 4591 C CG2 . VAL B 1 32 ? 40.247 -5.408 37.463 1.00 24.21 ? 32 VAL B CG2 1 ATOM 4592 N N . THR B 1 33 ? 38.884 -7.215 33.463 1.00 22.70 ? 33 THR B N 1 ATOM 4593 C CA . THR B 1 33 ? 37.949 -7.706 32.469 1.00 21.75 ? 33 THR B CA 1 ATOM 4594 C C . THR B 1 33 ? 37.161 -8.867 33.067 1.00 23.43 ? 33 THR B C 1 ATOM 4595 O O . THR B 1 33 ? 37.741 -9.789 33.641 1.00 24.58 ? 33 THR B O 1 ATOM 4596 C CB . THR B 1 33 ? 38.674 -8.120 31.152 1.00 20.79 ? 33 THR B CB 1 ATOM 4597 O OG1 . THR B 1 33 ? 39.227 -6.955 30.532 1.00 21.82 ? 33 THR B OG1 1 ATOM 4598 C CG2 . THR B 1 33 ? 37.724 -8.769 30.163 1.00 20.18 ? 33 THR B CG2 1 ATOM 4599 N N . GLN B 1 34 ? 35.833 -8.767 32.983 1.00 24.99 ? 34 GLN B N 1 ATOM 4600 C CA . GLN B 1 34 ? 34.918 -9.803 33.462 1.00 25.83 ? 34 GLN B CA 1 ATOM 4601 C C . GLN B 1 34 ? 34.360 -10.513 32.236 1.00 25.49 ? 34 GLN B C 1 ATOM 4602 O O . GLN B 1 34 ? 33.578 -9.945 31.467 1.00 25.09 ? 34 GLN B O 1 ATOM 4603 C CB . GLN B 1 34 ? 33.794 -9.200 34.317 1.00 28.20 ? 34 GLN B CB 1 ATOM 4604 C CG . GLN B 1 34 ? 34.235 -8.718 35.710 1.00 29.76 ? 34 GLN B CG 1 ATOM 4605 C CD . GLN B 1 34 ? 34.611 -9.858 36.646 1.00 29.91 ? 34 GLN B CD 1 ATOM 4606 O OE1 . GLN B 1 34 ? 33.797 -10.738 36.931 1.00 31.67 ? 34 GLN B OE1 1 ATOM 4607 N NE2 . GLN B 1 34 ? 35.850 -9.847 37.122 1.00 31.26 ? 34 GLN B NE2 1 ATOM 4608 N N . SER B 1 35 ? 34.834 -11.742 32.046 1.00 26.24 ? 35 SER B N 1 ATOM 4609 C CA . SER B 1 35 ? 34.466 -12.589 30.919 1.00 24.56 ? 35 SER B CA 1 ATOM 4610 C C . SER B 1 35 ? 33.361 -13.589 31.183 1.00 23.89 ? 35 SER B C 1 ATOM 4611 O O . SER B 1 35 ? 33.253 -14.149 32.277 1.00 25.16 ? 35 SER B O 1 ATOM 4612 C CB . SER B 1 35 ? 35.697 -13.313 30.392 1.00 23.67 ? 35 SER B CB 1 ATOM 4613 O OG . SER B 1 35 ? 36.612 -12.395 29.835 1.00 24.04 ? 35 SER B OG 1 ATOM 4614 N N . TYR B 1 36 ? 32.502 -13.750 30.176 1.00 22.80 ? 36 TYR B N 1 ATOM 4615 C CA . TYR B 1 36 ? 31.358 -14.664 30.208 1.00 21.75 ? 36 TYR B CA 1 ATOM 4616 C C . TYR B 1 36 ? 31.213 -15.322 28.836 1.00 21.57 ? 36 TYR B C 1 ATOM 4617 O O . TYR B 1 36 ? 31.752 -14.827 27.842 1.00 22.80 ? 36 TYR B O 1 ATOM 4618 C CB . TYR B 1 36 ? 30.048 -13.909 30.530 1.00 19.68 ? 36 TYR B CB 1 ATOM 4619 C CG . TYR B 1 36 ? 30.023 -13.179 31.854 1.00 18.89 ? 36 TYR B CG 1 ATOM 4620 C CD1 . TYR B 1 36 ? 30.397 -11.818 31.939 1.00 19.40 ? 36 TYR B CD1 1 ATOM 4621 C CD2 . TYR B 1 36 ? 29.696 -13.855 33.046 1.00 19.78 ? 36 TYR B CD2 1 ATOM 4622 C CE1 . TYR B 1 36 ? 30.459 -11.149 33.195 1.00 18.25 ? 36 TYR B CE1 1 ATOM 4623 C CE2 . TYR B 1 36 ? 29.749 -13.193 34.310 1.00 20.00 ? 36 TYR B CE2 1 ATOM 4624 C CZ . TYR B 1 36 ? 30.135 -11.847 34.368 1.00 18.11 ? 36 TYR B CZ 1 ATOM 4625 O OH . TYR B 1 36 ? 30.205 -11.220 35.587 1.00 18.49 ? 36 TYR B OH 1 ATOM 4626 N N . VAL B 1 37 ? 30.576 -16.492 28.808 1.00 21.60 ? 37 VAL B N 1 ATOM 4627 C CA . VAL B 1 37 ? 30.306 -17.211 27.562 1.00 21.03 ? 37 VAL B CA 1 ATOM 4628 C C . VAL B 1 37 ? 28.828 -17.549 27.553 1.00 19.69 ? 37 VAL B C 1 ATOM 4629 O O . VAL B 1 37 ? 28.269 -18.014 28.557 1.00 18.94 ? 37 VAL B O 1 ATOM 4630 C CB . VAL B 1 37 ? 31.164 -18.503 27.376 1.00 21.84 ? 37 VAL B CB 1 ATOM 4631 C CG1 . VAL B 1 37 ? 30.670 -19.332 26.179 1.00 23.15 ? 37 VAL B CG1 1 ATOM 4632 C CG2 . VAL B 1 37 ? 32.605 -18.128 27.112 1.00 24.01 ? 37 VAL B CG2 1 ATOM 4633 N N . PHE B 1 38 ? 28.191 -17.201 26.439 1.00 18.33 ? 38 PHE B N 1 ATOM 4634 C CA . PHE B 1 38 ? 26.771 -17.446 26.227 1.00 19.07 ? 38 PHE B CA 1 ATOM 4635 C C . PHE B 1 38 ? 26.624 -18.547 25.206 1.00 19.28 ? 38 PHE B C 1 ATOM 4636 O O . PHE B 1 38 ? 27.229 -18.494 24.131 1.00 19.73 ? 38 PHE B O 1 ATOM 4637 C CB . PHE B 1 38 ? 26.045 -16.196 25.703 1.00 16.30 ? 38 PHE B CB 1 ATOM 4638 C CG . PHE B 1 38 ? 25.864 -15.085 26.716 1.00 16.17 ? 38 PHE B CG 1 ATOM 4639 C CD1 . PHE B 1 38 ? 26.421 -15.147 28.018 1.00 14.71 ? 38 PHE B CD1 1 ATOM 4640 C CD2 . PHE B 1 38 ? 25.180 -13.923 26.334 1.00 15.19 ? 38 PHE B CD2 1 ATOM 4641 C CE1 . PHE B 1 38 ? 26.311 -14.069 28.912 1.00 14.91 ? 38 PHE B CE1 1 ATOM 4642 C CE2 . PHE B 1 38 ? 25.058 -12.834 27.215 1.00 17.25 ? 38 PHE B CE2 1 ATOM 4643 C CZ . PHE B 1 38 ? 25.631 -12.907 28.513 1.00 15.58 ? 38 PHE B CZ 1 ATOM 4644 N N . ASN B 1 39 ? 25.835 -19.549 25.563 1.00 19.79 ? 39 ASN B N 1 ATOM 4645 C CA . ASN B 1 39 ? 25.579 -20.673 24.690 1.00 21.17 ? 39 ASN B CA 1 ATOM 4646 C C . ASN B 1 39 ? 24.077 -20.719 24.486 1.00 21.75 ? 39 ASN B C 1 ATOM 4647 O O . ASN B 1 39 ? 23.326 -21.180 25.354 1.00 19.82 ? 39 ASN B O 1 ATOM 4648 C CB . ASN B 1 39 ? 26.101 -21.970 25.319 1.00 23.85 ? 39 ASN B CB 1 ATOM 4649 C CG . ASN B 1 39 ? 26.122 -23.142 24.345 1.00 25.34 ? 39 ASN B CG 1 ATOM 4650 O OD1 . ASN B 1 39 ? 25.698 -23.044 23.189 1.00 26.72 ? 39 ASN B OD1 1 ATOM 4651 N ND2 . ASN B 1 39 ? 26.623 -24.266 24.834 1.00 27.19 ? 39 ASN B ND2 1 ATOM 4652 N N . LEU B 1 40 ? 23.654 -20.208 23.331 1.00 22.53 ? 40 LEU B N 1 ATOM 4653 C CA . LEU B 1 40 ? 22.246 -20.158 22.980 1.00 21.31 ? 40 LEU B CA 1 ATOM 4654 C C . LEU B 1 40 ? 21.842 -21.483 22.391 1.00 21.55 ? 40 LEU B C 1 ATOM 4655 O O . LEU B 1 40 ? 22.351 -21.885 21.349 1.00 21.62 ? 40 LEU B O 1 ATOM 4656 C CB . LEU B 1 40 ? 21.948 -19.047 21.969 1.00 22.01 ? 40 LEU B CB 1 ATOM 4657 C CG . LEU B 1 40 ? 22.418 -17.594 22.068 1.00 22.29 ? 40 LEU B CG 1 ATOM 4658 C CD1 . LEU B 1 40 ? 21.305 -16.730 21.527 1.00 22.86 ? 40 LEU B CD1 1 ATOM 4659 C CD2 . LEU B 1 40 ? 22.746 -17.163 23.465 1.00 23.58 ? 40 LEU B CD2 1 ATOM 4660 N N . THR B 1 41 ? 20.986 -22.193 23.113 1.00 21.22 ? 41 THR B N 1 ATOM 4661 C CA . THR B 1 41 ? 20.488 -23.485 22.665 1.00 21.91 ? 41 THR B CA 1 ATOM 4662 C C . THR B 1 41 ? 18.967 -23.453 22.583 1.00 21.34 ? 41 THR B C 1 ATOM 4663 O O . THR B 1 41 ? 18.309 -22.759 23.367 1.00 19.30 ? 41 THR B O 1 ATOM 4664 C CB . THR B 1 41 ? 20.938 -24.646 23.598 1.00 22.29 ? 41 THR B CB 1 ATOM 4665 O OG1 . THR B 1 41 ? 20.554 -24.362 24.950 1.00 23.00 ? 41 THR B OG1 1 ATOM 4666 C CG2 . THR B 1 41 ? 22.451 -24.853 23.525 1.00 22.01 ? 41 THR B CG2 1 ATOM 4667 N N . GLU B 1 42 ? 18.435 -24.165 21.586 1.00 21.26 ? 42 GLU B N 1 ATOM 4668 C CA . GLU B 1 42 ? 16.999 -24.278 21.353 1.00 20.49 ? 42 GLU B CA 1 ATOM 4669 C C . GLU B 1 42 ? 16.511 -25.540 22.054 1.00 20.24 ? 42 GLU B C 1 ATOM 4670 O O . GLU B 1 42 ? 16.983 -26.644 21.768 1.00 21.52 ? 42 GLU B O 1 ATOM 4671 C CB . GLU B 1 42 ? 16.712 -24.351 19.850 1.00 19.95 ? 42 GLU B CB 1 ATOM 4672 C CG . GLU B 1 42 ? 15.311 -23.906 19.452 1.00 18.58 ? 42 GLU B CG 1 ATOM 4673 C CD . GLU B 1 42 ? 15.231 -23.464 18.000 1.00 20.44 ? 42 GLU B CD 1 ATOM 4674 O OE1 . GLU B 1 42 ? 16.151 -22.757 17.532 1.00 22.03 ? 42 GLU B OE1 1 ATOM 4675 O OE2 . GLU B 1 42 ? 14.250 -23.817 17.318 1.00 20.41 ? 42 GLU B OE2 1 ATOM 4676 N N . VAL B 1 43 ? 15.621 -25.356 23.028 1.00 21.28 ? 43 VAL B N 1 ATOM 4677 C CA . VAL B 1 43 ? 15.071 -26.471 23.798 1.00 21.08 ? 43 VAL B CA 1 ATOM 4678 C C . VAL B 1 43 ? 13.572 -26.579 23.549 1.00 21.12 ? 43 VAL B C 1 ATOM 4679 O O . VAL B 1 43 ? 12.831 -25.614 23.726 1.00 21.63 ? 43 VAL B O 1 ATOM 4680 C CB . VAL B 1 43 ? 15.343 -26.326 25.337 1.00 19.67 ? 43 VAL B CB 1 ATOM 4681 C CG1 . VAL B 1 43 ? 14.953 -27.606 26.079 1.00 21.82 ? 43 VAL B CG1 1 ATOM 4682 C CG2 . VAL B 1 43 ? 16.811 -26.007 25.610 1.00 20.17 ? 43 VAL B CG2 1 ATOM 4683 N N . ASP B 1 44 ? 13.153 -27.757 23.094 1.00 22.22 ? 44 ASP B N 1 ATOM 4684 C CA . ASP B 1 44 ? 11.747 -28.045 22.826 1.00 22.96 ? 44 ASP B CA 1 ATOM 4685 C C . ASP B 1 44 ? 11.142 -28.770 24.026 1.00 23.45 ? 44 ASP B C 1 ATOM 4686 O O . ASP B 1 44 ? 11.839 -29.517 24.721 1.00 23.16 ? 44 ASP B O 1 ATOM 4687 C CB . ASP B 1 44 ? 11.590 -28.898 21.559 1.00 23.27 ? 44 ASP B CB 1 ATOM 4688 C CG . ASP B 1 44 ? 12.000 -28.160 20.283 1.00 23.64 ? 44 ASP B CG 1 ATOM 4689 O OD1 . ASP B 1 44 ? 12.010 -26.910 20.261 1.00 22.95 ? 44 ASP B OD1 1 ATOM 4690 O OD2 . ASP B 1 44 ? 12.303 -28.843 19.286 1.00 24.06 ? 44 ASP B OD2 1 ATOM 4691 N N . ASN B 1 45 ? 9.858 -28.511 24.281 1.00 23.52 ? 45 ASN B N 1 ATOM 4692 C CA . ASN B 1 45 ? 9.093 -29.112 25.385 1.00 25.32 ? 45 ASN B CA 1 ATOM 4693 C C . ASN B 1 45 ? 9.778 -29.016 26.760 1.00 25.81 ? 45 ASN B C 1 ATOM 4694 O O . ASN B 1 45 ? 9.941 -29.997 27.494 1.00 25.57 ? 45 ASN B O 1 ATOM 4695 C CB . ASN B 1 45 ? 8.665 -30.538 25.028 1.00 23.81 ? 45 ASN B CB 1 ATOM 4696 C CG . ASN B 1 45 ? 7.899 -30.591 23.724 1.00 25.73 ? 45 ASN B CG 1 ATOM 4697 O OD1 . ASN B 1 45 ? 6.680 -30.415 23.691 1.00 26.94 ? 45 ASN B OD1 1 ATOM 4698 N ND2 . ASN B 1 45 ? 8.617 -30.817 22.632 1.00 27.14 ? 45 ASN B ND2 1 ATOM 4699 N N . TRP B 1 46 ? 10.156 -27.782 27.072 1.00 26.03 ? 46 TRP B N 1 ATOM 4700 C CA . TRP B 1 46 ? 10.849 -27.394 28.289 1.00 26.64 ? 46 TRP B CA 1 ATOM 4701 C C . TRP B 1 46 ? 9.852 -27.170 29.420 1.00 27.08 ? 46 TRP B C 1 ATOM 4702 O O . TRP B 1 46 ? 8.780 -26.603 29.205 1.00 28.64 ? 46 TRP B O 1 ATOM 4703 C CB . TRP B 1 46 ? 11.633 -26.114 27.974 1.00 26.53 ? 46 TRP B CB 1 ATOM 4704 C CG . TRP B 1 46 ? 12.397 -25.456 29.089 1.00 27.56 ? 46 TRP B CG 1 ATOM 4705 C CD1 . TRP B 1 46 ? 13.625 -25.813 29.568 1.00 28.23 ? 46 TRP B CD1 1 ATOM 4706 C CD2 . TRP B 1 46 ? 12.018 -24.271 29.797 1.00 28.27 ? 46 TRP B CD2 1 ATOM 4707 N NE1 . TRP B 1 46 ? 14.042 -24.919 30.528 1.00 28.83 ? 46 TRP B NE1 1 ATOM 4708 C CE2 . TRP B 1 46 ? 13.077 -23.962 30.691 1.00 27.50 ? 46 TRP B CE2 1 ATOM 4709 C CE3 . TRP B 1 46 ? 10.885 -23.430 29.760 1.00 28.42 ? 46 TRP B CE3 1 ATOM 4710 C CZ2 . TRP B 1 46 ? 13.042 -22.844 31.548 1.00 27.38 ? 46 TRP B CZ2 1 ATOM 4711 C CZ3 . TRP B 1 46 ? 10.845 -22.308 30.614 1.00 27.61 ? 46 TRP B CZ3 1 ATOM 4712 C CH2 . TRP B 1 46 ? 11.923 -22.031 31.496 1.00 28.05 ? 46 TRP B CH2 1 ATOM 4713 N N . MET B 1 47 ? 10.217 -27.626 30.616 1.00 27.38 ? 47 MET B N 1 ATOM 4714 C CA . MET B 1 47 ? 9.374 -27.468 31.796 1.00 28.00 ? 47 MET B CA 1 ATOM 4715 C C . MET B 1 47 ? 9.574 -26.074 32.383 1.00 28.21 ? 47 MET B C 1 ATOM 4716 O O . MET B 1 47 ? 10.683 -25.705 32.789 1.00 28.58 ? 47 MET B O 1 ATOM 4717 C CB . MET B 1 47 ? 9.667 -28.564 32.838 1.00 27.58 ? 47 MET B CB 1 ATOM 4718 C CG . MET B 1 47 ? 8.867 -28.460 34.149 1.00 29.37 ? 47 MET B CG 1 ATOM 4719 S SD . MET B 1 47 ? 7.083 -28.245 33.917 1.00 31.06 ? 47 MET B SD 1 ATOM 4720 C CE . MET B 1 47 ? 6.476 -29.885 34.322 1.00 31.58 ? 47 MET B CE 1 ATOM 4721 N N . GLY B 1 48 ? 8.489 -25.302 32.371 1.00 27.98 ? 48 GLY B N 1 ATOM 4722 C CA . GLY B 1 48 ? 8.502 -23.951 32.896 1.00 27.90 ? 48 GLY B CA 1 ATOM 4723 C C . GLY B 1 48 ? 8.475 -23.855 34.415 1.00 28.27 ? 48 GLY B C 1 ATOM 4724 O O . GLY B 1 48 ? 8.231 -24.861 35.093 1.00 26.82 ? 48 GLY B O 1 ATOM 4725 N N . PRO B 1 49 ? 8.725 -22.657 34.984 1.00 28.17 ? 49 PRO B N 1 ATOM 4726 C CA . PRO B 1 49 ? 8.727 -22.436 36.435 1.00 29.02 ? 49 PRO B CA 1 ATOM 4727 C C . PRO B 1 49 ? 7.376 -22.661 37.129 1.00 29.56 ? 49 PRO B C 1 ATOM 4728 O O . PRO B 1 49 ? 7.348 -23.028 38.313 1.00 30.43 ? 49 PRO B O 1 ATOM 4729 C CB . PRO B 1 49 ? 9.165 -20.977 36.552 1.00 28.79 ? 49 PRO B CB 1 ATOM 4730 C CG . PRO B 1 49 ? 10.008 -20.777 35.347 1.00 29.67 ? 49 PRO B CG 1 ATOM 4731 C CD . PRO B 1 49 ? 9.192 -21.443 34.290 1.00 28.66 ? 49 PRO B CD 1 ATOM 4732 N N . ASP B 1 50 ? 6.281 -22.478 36.379 1.00 28.27 ? 50 ASP B N 1 ATOM 4733 C CA . ASP B 1 50 ? 4.912 -22.630 36.891 1.00 28.52 ? 50 ASP B CA 1 ATOM 4734 C C . ASP B 1 50 ? 4.245 -23.999 36.655 1.00 29.14 ? 50 ASP B C 1 ATOM 4735 O O . ASP B 1 50 ? 3.022 -24.145 36.814 1.00 29.32 ? 50 ASP B O 1 ATOM 4736 C CB . ASP B 1 50 ? 4.017 -21.471 36.393 1.00 28.23 ? 50 ASP B CB 1 ATOM 4737 C CG . ASP B 1 50 ? 3.770 -21.488 34.879 1.00 27.19 ? 50 ASP B CG 1 ATOM 4738 O OD1 . ASP B 1 50 ? 4.569 -22.080 34.123 1.00 25.12 ? 50 ASP B OD1 1 ATOM 4739 O OD2 . ASP B 1 50 ? 2.759 -20.890 34.450 1.00 27.34 ? 50 ASP B OD2 1 ATOM 4740 N N . GLY B 1 51 ? 5.057 -24.987 36.277 1.00 27.80 ? 51 GLY B N 1 ATOM 4741 C CA . GLY B 1 51 ? 4.563 -26.332 36.035 1.00 27.20 ? 51 GLY B CA 1 ATOM 4742 C C . GLY B 1 51 ? 4.005 -26.581 34.645 1.00 26.92 ? 51 GLY B C 1 ATOM 4743 O O . GLY B 1 51 ? 3.608 -27.706 34.338 1.00 28.44 ? 51 GLY B O 1 ATOM 4744 N N . VAL B 1 52 ? 3.967 -25.540 33.813 1.00 25.23 ? 52 VAL B N 1 ATOM 4745 C CA . VAL B 1 52 ? 3.452 -25.654 32.450 1.00 23.39 ? 52 VAL B CA 1 ATOM 4746 C C . VAL B 1 52 ? 4.587 -25.851 31.457 1.00 22.69 ? 52 VAL B C 1 ATOM 4747 O O . VAL B 1 52 ? 5.601 -25.151 31.491 1.00 22.57 ? 52 VAL B O 1 ATOM 4748 C CB . VAL B 1 52 ? 2.595 -24.429 32.050 1.00 22.86 ? 52 VAL B CB 1 ATOM 4749 C CG1 . VAL B 1 52 ? 2.078 -24.561 30.609 1.00 24.07 ? 52 VAL B CG1 1 ATOM 4750 C CG2 . VAL B 1 52 ? 1.424 -24.284 32.996 1.00 21.13 ? 52 VAL B CG2 1 ATOM 4751 N N . VAL B 1 53 ? 4.380 -26.810 30.563 1.00 21.44 ? 53 VAL B N 1 ATOM 4752 C CA . VAL B 1 53 ? 5.354 -27.153 29.543 1.00 20.83 ? 53 VAL B CA 1 ATOM 4753 C C . VAL B 1 53 ? 5.160 -26.289 28.302 1.00 18.75 ? 53 VAL B C 1 ATOM 4754 O O . VAL B 1 53 ? 4.066 -26.225 27.743 1.00 17.05 ? 53 VAL B O 1 ATOM 4755 C CB . VAL B 1 53 ? 5.287 -28.676 29.216 1.00 21.81 ? 53 VAL B CB 1 ATOM 4756 C CG1 . VAL B 1 53 ? 6.272 -29.053 28.120 1.00 20.06 ? 53 VAL B CG1 1 ATOM 4757 C CG2 . VAL B 1 53 ? 5.606 -29.484 30.468 1.00 20.39 ? 53 VAL B CG2 1 ATOM 4758 N N . LYS B 1 54 ? 6.237 -25.600 27.921 1.00 18.26 ? 54 LYS B N 1 ATOM 4759 C CA . LYS B 1 54 ? 6.264 -24.723 26.750 1.00 18.26 ? 54 LYS B CA 1 ATOM 4760 C C . LYS B 1 54 ? 6.796 -25.449 25.527 1.00 17.17 ? 54 LYS B C 1 ATOM 4761 O O . LYS B 1 54 ? 7.800 -26.167 25.621 1.00 17.28 ? 54 LYS B O 1 ATOM 4762 C CB . LYS B 1 54 ? 7.140 -23.494 27.011 1.00 19.77 ? 54 LYS B CB 1 ATOM 4763 C CG . LYS B 1 54 ? 6.435 -22.362 27.740 1.00 20.66 ? 54 LYS B CG 1 ATOM 4764 C CD . LYS B 1 54 ? 7.266 -21.076 27.781 1.00 21.45 ? 54 LYS B CD 1 ATOM 4765 C CE . LYS B 1 54 ? 7.388 -20.396 26.429 1.00 21.48 ? 54 LYS B CE 1 ATOM 4766 N NZ . LYS B 1 54 ? 8.017 -19.045 26.522 1.00 19.03 ? 54 LYS B NZ 1 ATOM 4767 N N . GLU B 1 55 ? 6.165 -25.193 24.376 1.00 15.65 ? 55 GLU B N 1 ATOM 4768 C CA . GLU B 1 55 ? 6.538 -25.800 23.091 1.00 14.07 ? 55 GLU B CA 1 ATOM 4769 C C . GLU B 1 55 ? 8.021 -25.625 22.728 1.00 12.52 ? 55 GLU B C 1 ATOM 4770 O O . GLU B 1 55 ? 8.714 -26.606 22.473 1.00 11.14 ? 55 GLU B O 1 ATOM 4771 C CB . GLU B 1 55 ? 5.672 -25.227 21.954 1.00 13.62 ? 55 GLU B CB 1 ATOM 4772 C CG . GLU B 1 55 ? 5.858 -25.945 20.617 1.00 16.56 ? 55 GLU B CG 1 ATOM 4773 C CD . GLU B 1 55 ? 5.489 -25.109 19.399 1.00 19.75 ? 55 GLU B CD 1 ATOM 4774 O OE1 . GLU B 1 55 ? 4.303 -24.754 19.234 1.00 21.33 ? 55 GLU B OE1 1 ATOM 4775 O OE2 . GLU B 1 55 ? 6.389 -24.845 18.574 1.00 22.07 ? 55 GLU B OE2 1 ATOM 4776 N N . LYS B 1 56 ? 8.489 -24.377 22.735 1.00 13.51 ? 56 LYS B N 1 ATOM 4777 C CA . LYS B 1 56 ? 9.868 -24.046 22.370 1.00 13.62 ? 56 LYS B CA 1 ATOM 4778 C C . LYS B 1 56 ? 10.386 -22.818 23.104 1.00 12.91 ? 56 LYS B C 1 ATOM 4779 O O . LYS B 1 56 ? 9.658 -21.848 23.320 1.00 12.78 ? 56 LYS B O 1 ATOM 4780 C CB . LYS B 1 56 ? 9.949 -23.786 20.858 1.00 14.04 ? 56 LYS B CB 1 ATOM 4781 C CG . LYS B 1 56 ? 11.352 -23.612 20.283 1.00 16.81 ? 56 LYS B CG 1 ATOM 4782 C CD . LYS B 1 56 ? 11.305 -23.176 18.818 1.00 20.90 ? 56 LYS B CD 1 ATOM 4783 C CE . LYS B 1 56 ? 10.859 -24.289 17.854 1.00 23.71 ? 56 LYS B CE 1 ATOM 4784 N NZ . LYS B 1 56 ? 11.857 -25.397 17.703 1.00 26.22 ? 56 LYS B NZ 1 ATOM 4785 N N . VAL B 1 57 ? 11.646 -22.890 23.518 1.00 11.86 ? 57 VAL B N 1 ATOM 4786 C CA . VAL B 1 57 ? 12.317 -21.779 24.191 1.00 12.10 ? 57 VAL B CA 1 ATOM 4787 C C . VAL B 1 57 ? 13.739 -21.691 23.650 1.00 11.10 ? 57 VAL B C 1 ATOM 4788 O O . VAL B 1 57 ? 14.271 -22.670 23.119 1.00 12.30 ? 57 VAL B O 1 ATOM 4789 C CB . VAL B 1 57 ? 12.377 -21.930 25.758 1.00 11.41 ? 57 VAL B CB 1 ATOM 4790 C CG1 . VAL B 1 57 ? 11.001 -21.771 26.396 1.00 10.07 ? 57 VAL B CG1 1 ATOM 4791 C CG2 . VAL B 1 57 ? 13.001 -23.241 26.152 1.00 11.73 ? 57 VAL B CG2 1 ATOM 4792 N N . MET B 1 58 ? 14.333 -20.506 23.761 1.00 11.61 ? 58 MET B N 1 ATOM 4793 C CA . MET B 1 58 ? 15.706 -20.259 23.327 1.00 11.64 ? 58 MET B CA 1 ATOM 4794 C C . MET B 1 58 ? 16.383 -19.824 24.605 1.00 13.06 ? 58 MET B C 1 ATOM 4795 O O . MET B 1 58 ? 15.928 -18.885 25.246 1.00 13.20 ? 58 MET B O 1 ATOM 4796 C CB . MET B 1 58 ? 15.739 -19.184 22.244 1.00 8.84 ? 58 MET B CB 1 ATOM 4797 C CG . MET B 1 58 ? 15.127 -19.689 20.947 1.00 11.25 ? 58 MET B CG 1 ATOM 4798 S SD . MET B 1 58 ? 14.948 -18.546 19.598 1.00 10.57 ? 58 MET B SD 1 ATOM 4799 C CE . MET B 1 58 ? 13.904 -19.543 18.546 1.00 8.99 ? 58 MET B CE 1 ATOM 4800 N N . LEU B 1 59 ? 17.391 -20.588 25.037 1.00 15.37 ? 59 LEU B N 1 ATOM 4801 C CA . LEU B 1 59 ? 18.073 -20.325 26.306 1.00 16.80 ? 59 LEU B CA 1 ATOM 4802 C C . LEU B 1 59 ? 19.578 -20.148 26.262 1.00 18.08 ? 59 LEU B C 1 ATOM 4803 O O . LEU B 1 59 ? 20.269 -20.801 25.487 1.00 19.56 ? 59 LEU B O 1 ATOM 4804 C CB . LEU B 1 59 ? 17.778 -21.456 27.302 1.00 17.83 ? 59 LEU B CB 1 ATOM 4805 C CG . LEU B 1 59 ? 16.360 -21.943 27.600 1.00 18.37 ? 59 LEU B CG 1 ATOM 4806 C CD1 . LEU B 1 59 ? 16.407 -23.084 28.591 1.00 19.93 ? 59 LEU B CD1 1 ATOM 4807 C CD2 . LEU B 1 59 ? 15.489 -20.796 28.117 1.00 21.27 ? 59 LEU B CD2 1 ATOM 4808 N N . ILE B 1 60 ? 20.068 -19.322 27.187 1.00 17.28 ? 60 ILE B N 1 ATOM 4809 C CA . ILE B 1 60 ? 21.486 -19.023 27.360 1.00 15.75 ? 60 ILE B CA 1 ATOM 4810 C C . ILE B 1 60 ? 21.978 -19.907 28.516 1.00 16.93 ? 60 ILE B C 1 ATOM 4811 O O . ILE B 1 60 ? 21.491 -19.779 29.652 1.00 16.01 ? 60 ILE B O 1 ATOM 4812 C CB . ILE B 1 60 ? 21.704 -17.547 27.765 1.00 14.67 ? 60 ILE B CB 1 ATOM 4813 C CG1 . ILE B 1 60 ? 21.068 -16.593 26.756 1.00 16.12 ? 60 ILE B CG1 1 ATOM 4814 C CG2 . ILE B 1 60 ? 23.176 -17.261 27.933 1.00 14.71 ? 60 ILE B CG2 1 ATOM 4815 C CD1 . ILE B 1 60 ? 21.033 -15.135 27.210 1.00 15.46 ? 60 ILE B CD1 1 ATOM 4816 N N . ASN B 1 61 ? 22.953 -20.777 28.223 1.00 16.58 ? 61 ASN B N 1 ATOM 4817 C CA . ASN B 1 61 ? 23.547 -21.715 29.194 1.00 17.16 ? 61 ASN B CA 1 ATOM 4818 C C . ASN B 1 61 ? 22.507 -22.628 29.893 1.00 17.57 ? 61 ASN B C 1 ATOM 4819 O O . ASN B 1 61 ? 22.600 -22.907 31.098 1.00 17.23 ? 61 ASN B O 1 ATOM 4820 C CB . ASN B 1 61 ? 24.436 -20.971 30.228 1.00 17.31 ? 61 ASN B CB 1 ATOM 4821 C CG . ASN B 1 61 ? 25.585 -20.179 29.581 1.00 16.51 ? 61 ASN B CG 1 ATOM 4822 O OD1 . ASN B 1 61 ? 25.868 -20.307 28.385 1.00 16.48 ? 61 ASN B OD1 1 ATOM 4823 N ND2 . ASN B 1 61 ? 26.234 -19.346 30.378 1.00 14.60 ? 61 ASN B ND2 1 ATOM 4824 N N . GLY B 1 62 ? 21.479 -23.007 29.127 1.00 16.85 ? 62 GLY B N 1 ATOM 4825 C CA . GLY B 1 62 ? 20.415 -23.889 29.595 1.00 18.09 ? 62 GLY B CA 1 ATOM 4826 C C . GLY B 1 62 ? 19.486 -23.418 30.704 1.00 17.99 ? 62 GLY B C 1 ATOM 4827 O O . GLY B 1 62 ? 18.738 -24.223 31.261 1.00 16.20 ? 62 GLY B O 1 ATOM 4828 N N . ASN B 1 63 ? 19.534 -22.129 31.033 1.00 17.60 ? 63 ASN B N 1 ATOM 4829 C CA . ASN B 1 63 ? 18.676 -21.576 32.080 1.00 19.16 ? 63 ASN B CA 1 ATOM 4830 C C . ASN B 1 63 ? 17.596 -20.635 31.542 1.00 19.18 ? 63 ASN B C 1 ATOM 4831 O O . ASN B 1 63 ? 17.646 -20.233 30.382 1.00 17.46 ? 63 ASN B O 1 ATOM 4832 C CB . ASN B 1 63 ? 19.521 -20.899 33.163 1.00 18.82 ? 63 ASN B CB 1 ATOM 4833 C CG . ASN B 1 63 ? 20.438 -21.870 33.869 1.00 19.91 ? 63 ASN B CG 1 ATOM 4834 O OD1 . ASN B 1 63 ? 20.052 -23.004 34.163 1.00 21.19 ? 63 ASN B OD1 1 ATOM 4835 N ND2 . ASN B 1 63 ? 21.669 -21.447 34.118 1.00 22.42 ? 63 ASN B ND2 1 ATOM 4836 N N . ILE B 1 64 ? 16.619 -20.310 32.394 1.00 20.13 ? 64 ILE B N 1 ATOM 4837 C CA . ILE B 1 64 ? 15.483 -19.430 32.066 1.00 20.79 ? 64 ILE B CA 1 ATOM 4838 C C . ILE B 1 64 ? 15.978 -18.042 31.625 1.00 22.02 ? 64 ILE B C 1 ATOM 4839 O O . ILE B 1 64 ? 15.369 -17.388 30.771 1.00 22.41 ? 64 ILE B O 1 ATOM 4840 C CB . ILE B 1 64 ? 14.480 -19.356 33.293 1.00 21.58 ? 64 ILE B CB 1 ATOM 4841 C CG1 . ILE B 1 64 ? 13.113 -18.758 32.884 1.00 22.92 ? 64 ILE B CG1 1 ATOM 4842 C CG2 . ILE B 1 64 ? 15.158 -18.744 34.535 1.00 18.59 ? 64 ILE B CG2 1 ATOM 4843 C CD1 . ILE B 1 64 ? 12.894 -17.276 33.157 1.00 27.11 ? 64 ILE B CD1 1 ATOM 4844 N N . MET B 1 65 ? 17.074 -17.616 32.252 1.00 20.94 ? 65 MET B N 1 ATOM 4845 C CA . MET B 1 65 ? 17.740 -16.353 31.980 1.00 20.34 ? 65 MET B CA 1 ATOM 4846 C C . MET B 1 65 ? 19.228 -16.648 31.918 1.00 20.90 ? 65 MET B C 1 ATOM 4847 O O . MET B 1 65 ? 19.690 -17.673 32.431 1.00 20.59 ? 65 MET B O 1 ATOM 4848 C CB . MET B 1 65 ? 17.479 -15.324 33.089 1.00 21.11 ? 65 MET B CB 1 ATOM 4849 C CG . MET B 1 65 ? 16.120 -14.652 33.036 1.00 22.27 ? 65 MET B CG 1 ATOM 4850 S SD . MET B 1 65 ? 15.925 -13.428 34.330 1.00 27.45 ? 65 MET B SD 1 ATOM 4851 C CE . MET B 1 65 ? 15.670 -14.525 35.774 1.00 23.70 ? 65 MET B CE 1 ATOM 4852 N N . GLY B 1 66 ? 19.983 -15.732 31.314 1.00 21.41 ? 66 GLY B N 1 ATOM 4853 C CA . GLY B 1 66 ? 21.419 -15.898 31.208 1.00 20.38 ? 66 GLY B CA 1 ATOM 4854 C C . GLY B 1 66 ? 22.150 -15.541 32.486 1.00 22.08 ? 66 GLY B C 1 ATOM 4855 O O . GLY B 1 66 ? 21.491 -15.292 33.502 1.00 21.40 ? 66 GLY B O 1 ATOM 4856 N N . PRO B 1 67 ? 23.508 -15.520 32.481 1.00 23.13 ? 67 PRO B N 1 ATOM 4857 C CA . PRO B 1 67 ? 24.322 -15.185 33.657 1.00 22.64 ? 67 PRO B CA 1 ATOM 4858 C C . PRO B 1 67 ? 24.088 -13.762 34.146 1.00 23.22 ? 67 PRO B C 1 ATOM 4859 O O . PRO B 1 67 ? 23.789 -12.866 33.347 1.00 21.59 ? 67 PRO B O 1 ATOM 4860 C CB . PRO B 1 67 ? 25.753 -15.314 33.130 1.00 23.59 ? 67 PRO B CB 1 ATOM 4861 C CG . PRO B 1 67 ? 25.645 -16.353 32.101 1.00 23.87 ? 67 PRO B CG 1 ATOM 4862 C CD . PRO B 1 67 ? 24.383 -15.968 31.379 1.00 22.25 ? 67 PRO B CD 1 ATOM 4863 N N . ASN B 1 68 ? 24.174 -13.576 35.463 1.00 23.74 ? 68 ASN B N 1 ATOM 4864 C CA . ASN B 1 68 ? 24.028 -12.254 36.060 1.00 23.72 ? 68 ASN B CA 1 ATOM 4865 C C . ASN B 1 68 ? 25.412 -11.619 35.954 1.00 23.26 ? 68 ASN B C 1 ATOM 4866 O O . ASN B 1 68 ? 26.355 -12.035 36.643 1.00 23.99 ? 68 ASN B O 1 ATOM 4867 C CB . ASN B 1 68 ? 23.580 -12.345 37.526 1.00 26.28 ? 68 ASN B CB 1 ATOM 4868 C CG . ASN B 1 68 ? 22.135 -12.820 37.677 1.00 28.76 ? 68 ASN B CG 1 ATOM 4869 O OD1 . ASN B 1 68 ? 21.239 -12.389 36.945 1.00 28.52 ? 68 ASN B OD1 1 ATOM 4870 N ND2 . ASN B 1 68 ? 21.905 -13.703 38.644 1.00 28.93 ? 68 ASN B ND2 1 ATOM 4871 N N . ILE B 1 69 ? 25.547 -10.709 34.985 1.00 21.16 ? 69 ILE B N 1 ATOM 4872 C CA . ILE B 1 69 ? 26.795 -9.993 34.732 1.00 17.68 ? 69 ILE B CA 1 ATOM 4873 C C . ILE B 1 69 ? 27.069 -9.019 35.862 1.00 16.09 ? 69 ILE B C 1 ATOM 4874 O O . ILE B 1 69 ? 26.272 -8.113 36.120 1.00 16.14 ? 69 ILE B O 1 ATOM 4875 C CB . ILE B 1 69 ? 26.790 -9.250 33.355 1.00 14.89 ? 69 ILE B CB 1 ATOM 4876 C CG1 . ILE B 1 69 ? 26.794 -10.276 32.217 1.00 14.15 ? 69 ILE B CG1 1 ATOM 4877 C CG2 . ILE B 1 69 ? 27.986 -8.284 33.245 1.00 15.06 ? 69 ILE B CG2 1 ATOM 4878 C CD1 . ILE B 1 69 ? 26.848 -9.692 30.825 1.00 8.99 ? 69 ILE B CD1 1 ATOM 4879 N N . VAL B 1 70 ? 28.172 -9.276 36.562 1.00 14.04 ? 70 VAL B N 1 ATOM 4880 C CA . VAL B 1 70 ? 28.618 -8.456 37.679 1.00 13.37 ? 70 VAL B CA 1 ATOM 4881 C C . VAL B 1 70 ? 30.041 -7.953 37.398 1.00 13.00 ? 70 VAL B C 1 ATOM 4882 O O . VAL B 1 70 ? 30.964 -8.737 37.132 1.00 13.20 ? 70 VAL B O 1 ATOM 4883 C CB . VAL B 1 70 ? 28.571 -9.238 39.049 1.00 13.39 ? 70 VAL B CB 1 ATOM 4884 C CG1 . VAL B 1 70 ? 28.815 -8.289 40.235 1.00 14.43 ? 70 VAL B CG1 1 ATOM 4885 C CG2 . VAL B 1 70 ? 27.243 -9.943 39.235 1.00 11.33 ? 70 VAL B CG2 1 ATOM 4886 N N . ALA B 1 71 ? 30.185 -6.631 37.423 1.00 12.86 ? 71 ALA B N 1 ATOM 4887 C CA . ALA B 1 71 ? 31.457 -5.946 37.212 1.00 13.48 ? 71 ALA B CA 1 ATOM 4888 C C . ALA B 1 71 ? 31.423 -4.654 38.023 1.00 14.59 ? 71 ALA B C 1 ATOM 4889 O O . ALA B 1 71 ? 30.402 -4.334 38.628 1.00 16.66 ? 71 ALA B O 1 ATOM 4890 C CB . ALA B 1 71 ? 31.657 -5.636 35.737 1.00 13.42 ? 71 ALA B CB 1 ATOM 4891 N N . ASN B 1 72 ? 32.549 -3.945 38.083 1.00 15.67 ? 72 ASN B N 1 ATOM 4892 C CA . ASN B 1 72 ? 32.620 -2.677 38.806 1.00 14.37 ? 72 ASN B CA 1 ATOM 4893 C C . ASN B 1 72 ? 32.700 -1.550 37.803 1.00 14.42 ? 72 ASN B C 1 ATOM 4894 O O . ASN B 1 72 ? 32.935 -1.787 36.616 1.00 14.32 ? 72 ASN B O 1 ATOM 4895 C CB . ASN B 1 72 ? 33.849 -2.622 39.716 1.00 17.10 ? 72 ASN B CB 1 ATOM 4896 C CG . ASN B 1 72 ? 33.757 -3.569 40.888 1.00 18.18 ? 72 ASN B CG 1 ATOM 4897 O OD1 . ASN B 1 72 ? 32.773 -3.565 41.626 1.00 20.86 ? 72 ASN B OD1 1 ATOM 4898 N ND2 . ASN B 1 72 ? 34.794 -4.373 41.079 1.00 17.18 ? 72 ASN B ND2 1 ATOM 4899 N N . TRP B 1 73 ? 32.474 -0.326 38.287 1.00 13.90 ? 73 TRP B N 1 ATOM 4900 C CA . TRP B 1 73 ? 32.536 0.893 37.479 1.00 12.70 ? 73 TRP B CA 1 ATOM 4901 C C . TRP B 1 73 ? 33.963 1.066 36.954 1.00 13.31 ? 73 TRP B C 1 ATOM 4902 O O . TRP B 1 73 ? 34.916 1.170 37.733 1.00 13.65 ? 73 TRP B O 1 ATOM 4903 C CB . TRP B 1 73 ? 32.116 2.082 38.347 1.00 11.20 ? 73 TRP B CB 1 ATOM 4904 C CG . TRP B 1 73 ? 32.043 3.443 37.692 1.00 11.15 ? 73 TRP B CG 1 ATOM 4905 C CD1 . TRP B 1 73 ? 31.893 3.737 36.351 1.00 11.05 ? 73 TRP B CD1 1 ATOM 4906 C CD2 . TRP B 1 73 ? 32.107 4.699 38.369 1.00 10.63 ? 73 TRP B CD2 1 ATOM 4907 N NE1 . TRP B 1 73 ? 31.872 5.100 36.164 1.00 10.29 ? 73 TRP B NE1 1 ATOM 4908 C CE2 . TRP B 1 73 ? 31.998 5.718 37.380 1.00 10.31 ? 73 TRP B CE2 1 ATOM 4909 C CE3 . TRP B 1 73 ? 32.235 5.071 39.724 1.00 9.51 ? 73 TRP B CE3 1 ATOM 4910 C CZ2 . TRP B 1 73 ? 32.018 7.093 37.706 1.00 11.30 ? 73 TRP B CZ2 1 ATOM 4911 C CZ3 . TRP B 1 73 ? 32.251 6.442 40.054 1.00 7.22 ? 73 TRP B CZ3 1 ATOM 4912 C CH2 . TRP B 1 73 ? 32.143 7.435 39.043 1.00 10.06 ? 73 TRP B CH2 1 ATOM 4913 N N . GLY B 1 74 ? 34.091 1.021 35.631 1.00 14.12 ? 74 GLY B N 1 ATOM 4914 C CA . GLY B 1 74 ? 35.391 1.155 35.001 1.00 16.92 ? 74 GLY B CA 1 ATOM 4915 C C . GLY B 1 74 ? 35.978 -0.135 34.462 1.00 19.50 ? 74 GLY B C 1 ATOM 4916 O O . GLY B 1 74 ? 37.022 -0.109 33.799 1.00 21.42 ? 74 GLY B O 1 ATOM 4917 N N . ASP B 1 75 ? 35.327 -1.261 34.768 1.00 20.98 ? 75 ASP B N 1 ATOM 4918 C CA . ASP B 1 75 ? 35.745 -2.585 34.292 1.00 21.89 ? 75 ASP B CA 1 ATOM 4919 C C . ASP B 1 75 ? 35.328 -2.742 32.826 1.00 22.41 ? 75 ASP B C 1 ATOM 4920 O O . ASP B 1 75 ? 34.576 -1.921 32.285 1.00 22.74 ? 75 ASP B O 1 ATOM 4921 C CB . ASP B 1 75 ? 35.062 -3.712 35.095 1.00 22.27 ? 75 ASP B CB 1 ATOM 4922 C CG . ASP B 1 75 ? 35.639 -3.911 36.501 1.00 22.89 ? 75 ASP B CG 1 ATOM 4923 O OD1 . ASP B 1 75 ? 36.633 -3.261 36.886 1.00 21.11 ? 75 ASP B OD1 1 ATOM 4924 O OD2 . ASP B 1 75 ? 35.078 -4.752 37.236 1.00 21.44 ? 75 ASP B OD2 1 ATOM 4925 N N . THR B 1 76 ? 35.825 -3.799 32.191 1.00 21.58 ? 76 THR B N 1 ATOM 4926 C CA . THR B 1 76 ? 35.480 -4.097 30.811 1.00 19.80 ? 76 THR B CA 1 ATOM 4927 C C . THR B 1 76 ? 34.734 -5.432 30.808 1.00 18.94 ? 76 THR B C 1 ATOM 4928 O O . THR B 1 76 ? 35.180 -6.386 31.437 1.00 19.30 ? 76 THR B O 1 ATOM 4929 C CB . THR B 1 76 ? 36.730 -4.189 29.931 1.00 19.32 ? 76 THR B CB 1 ATOM 4930 O OG1 . THR B 1 76 ? 37.581 -3.073 30.200 1.00 23.60 ? 76 THR B OG1 1 ATOM 4931 C CG2 . THR B 1 76 ? 36.350 -4.135 28.479 1.00 22.28 ? 76 THR B CG2 1 ATOM 4932 N N . VAL B 1 77 ? 33.554 -5.471 30.189 1.00 17.48 ? 77 VAL B N 1 ATOM 4933 C CA . VAL B 1 77 ? 32.794 -6.715 30.118 1.00 16.71 ? 77 VAL B CA 1 ATOM 4934 C C . VAL B 1 77 ? 32.913 -7.322 28.721 1.00 16.13 ? 77 VAL B C 1 ATOM 4935 O O . VAL B 1 77 ? 32.542 -6.714 27.715 1.00 12.52 ? 77 VAL B O 1 ATOM 4936 C CB . VAL B 1 77 ? 31.314 -6.546 30.533 1.00 17.16 ? 77 VAL B CB 1 ATOM 4937 C CG1 . VAL B 1 77 ? 30.589 -7.906 30.530 1.00 18.80 ? 77 VAL B CG1 1 ATOM 4938 C CG2 . VAL B 1 77 ? 31.214 -5.921 31.915 1.00 19.82 ? 77 VAL B CG2 1 ATOM 4939 N N . GLU B 1 78 ? 33.440 -8.542 28.703 1.00 17.69 ? 78 GLU B N 1 ATOM 4940 C CA . GLU B 1 78 ? 33.662 -9.305 27.489 1.00 17.36 ? 78 GLU B CA 1 ATOM 4941 C C . GLU B 1 78 ? 32.775 -10.531 27.515 1.00 16.34 ? 78 GLU B C 1 ATOM 4942 O O . GLU B 1 78 ? 32.703 -11.217 28.532 1.00 17.11 ? 78 GLU B O 1 ATOM 4943 C CB . GLU B 1 78 ? 35.126 -9.717 27.410 1.00 18.50 ? 78 GLU B CB 1 ATOM 4944 C CG . GLU B 1 78 ? 35.591 -10.088 26.021 1.00 21.86 ? 78 GLU B CG 1 ATOM 4945 C CD . GLU B 1 78 ? 37.106 -10.089 25.861 1.00 22.25 ? 78 GLU B CD 1 ATOM 4946 O OE1 . GLU B 1 78 ? 37.835 -9.611 26.762 1.00 22.27 ? 78 GLU B OE1 1 ATOM 4947 O OE2 . GLU B 1 78 ? 37.572 -10.548 24.799 1.00 25.67 ? 78 GLU B OE2 1 ATOM 4948 N N . VAL B 1 79 ? 32.041 -10.755 26.426 1.00 13.30 ? 79 VAL B N 1 ATOM 4949 C CA . VAL B 1 79 ? 31.138 -11.898 26.307 1.00 11.88 ? 79 VAL B CA 1 ATOM 4950 C C . VAL B 1 79 ? 31.209 -12.542 24.916 1.00 12.87 ? 79 VAL B C 1 ATOM 4951 O O . VAL B 1 79 ? 31.008 -11.876 23.899 1.00 12.14 ? 79 VAL B O 1 ATOM 4952 C CB . VAL B 1 79 ? 29.648 -11.506 26.584 1.00 11.91 ? 79 VAL B CB 1 ATOM 4953 C CG1 . VAL B 1 79 ? 28.734 -12.677 26.348 1.00 11.10 ? 79 VAL B CG1 1 ATOM 4954 C CG2 . VAL B 1 79 ? 29.440 -11.031 28.005 1.00 12.30 ? 79 VAL B CG2 1 ATOM 4955 N N . THR B 1 80 ? 31.430 -13.858 24.902 1.00 13.85 ? 80 THR B N 1 ATOM 4956 C CA . THR B 1 80 ? 31.480 -14.645 23.673 1.00 13.86 ? 80 THR B CA 1 ATOM 4957 C C . THR B 1 80 ? 30.103 -15.286 23.519 1.00 14.47 ? 80 THR B C 1 ATOM 4958 O O . THR B 1 80 ? 29.661 -16.039 24.389 1.00 14.16 ? 80 THR B O 1 ATOM 4959 C CB . THR B 1 80 ? 32.609 -15.713 23.734 1.00 12.54 ? 80 THR B CB 1 ATOM 4960 O OG1 . THR B 1 80 ? 33.861 -15.044 23.927 1.00 11.46 ? 80 THR B OG1 1 ATOM 4961 C CG2 . THR B 1 80 ? 32.678 -16.537 22.439 1.00 11.26 ? 80 THR B CG2 1 ATOM 4962 N N . VAL B 1 81 ? 29.413 -14.930 22.438 1.00 14.65 ? 81 VAL B N 1 ATOM 4963 C CA . VAL B 1 81 ? 28.071 -15.445 22.168 1.00 16.57 ? 81 VAL B CA 1 ATOM 4964 C C . VAL B 1 81 ? 28.111 -16.490 21.064 1.00 17.31 ? 81 VAL B C 1 ATOM 4965 O O . VAL B 1 81 ? 28.297 -16.164 19.887 1.00 19.35 ? 81 VAL B O 1 ATOM 4966 C CB . VAL B 1 81 ? 27.061 -14.294 21.798 1.00 16.91 ? 81 VAL B CB 1 ATOM 4967 C CG1 . VAL B 1 81 ? 25.629 -14.832 21.635 1.00 14.34 ? 81 VAL B CG1 1 ATOM 4968 C CG2 . VAL B 1 81 ? 27.071 -13.222 22.872 1.00 16.58 ? 81 VAL B CG2 1 ATOM 4969 N N . ILE B 1 82 ? 27.951 -17.750 21.463 1.00 16.99 ? 82 ILE B N 1 ATOM 4970 C CA . ILE B 1 82 ? 27.942 -18.863 20.526 1.00 16.02 ? 82 ILE B CA 1 ATOM 4971 C C . ILE B 1 82 ? 26.494 -19.260 20.245 1.00 16.33 ? 82 ILE B C 1 ATOM 4972 O O . ILE B 1 82 ? 25.741 -19.657 21.146 1.00 13.68 ? 82 ILE B O 1 ATOM 4973 C CB . ILE B 1 82 ? 28.782 -20.078 21.027 1.00 16.92 ? 82 ILE B CB 1 ATOM 4974 C CG1 . ILE B 1 82 ? 30.199 -19.616 21.403 1.00 15.66 ? 82 ILE B CG1 1 ATOM 4975 C CG2 . ILE B 1 82 ? 28.889 -21.129 19.907 1.00 15.32 ? 82 ILE B CG2 1 ATOM 4976 C CD1 . ILE B 1 82 ? 31.007 -20.619 22.152 1.00 17.41 ? 82 ILE B CD1 1 ATOM 4977 N N . ASN B 1 83 ? 26.126 -19.141 18.972 1.00 16.65 ? 83 ASN B N 1 ATOM 4978 C CA . ASN B 1 83 ? 24.785 -19.453 18.521 1.00 16.60 ? 83 ASN B CA 1 ATOM 4979 C C . ASN B 1 83 ? 24.618 -20.890 18.053 1.00 17.30 ? 83 ASN B C 1 ATOM 4980 O O . ASN B 1 83 ? 25.013 -21.251 16.935 1.00 15.89 ? 83 ASN B O 1 ATOM 4981 C CB . ASN B 1 83 ? 24.362 -18.483 17.420 1.00 16.27 ? 83 ASN B CB 1 ATOM 4982 C CG . ASN B 1 83 ? 22.872 -18.500 17.175 1.00 16.05 ? 83 ASN B CG 1 ATOM 4983 O OD1 . ASN B 1 83 ? 22.102 -18.872 18.050 1.00 15.36 ? 83 ASN B OD1 1 ATOM 4984 N ND2 . ASN B 1 83 ? 22.457 -18.064 15.995 1.00 15.79 ? 83 ASN B ND2 1 ATOM 4985 N N . ASN B 1 84 ? 23.995 -21.690 18.917 1.00 17.36 ? 84 ASN B N 1 ATOM 4986 C CA . ASN B 1 84 ? 23.733 -23.090 18.626 1.00 17.97 ? 84 ASN B CA 1 ATOM 4987 C C . ASN B 1 84 ? 22.247 -23.362 18.394 1.00 18.03 ? 84 ASN B C 1 ATOM 4988 O O . ASN B 1 84 ? 21.782 -24.499 18.527 1.00 19.60 ? 84 ASN B O 1 ATOM 4989 C CB . ASN B 1 84 ? 24.320 -23.991 19.723 1.00 16.80 ? 84 ASN B CB 1 ATOM 4990 C CG . ASN B 1 84 ? 25.840 -24.108 19.640 1.00 16.35 ? 84 ASN B CG 1 ATOM 4991 O OD1 . ASN B 1 84 ? 26.413 -24.210 18.551 1.00 15.67 ? 84 ASN B OD1 1 ATOM 4992 N ND2 . ASN B 1 84 ? 26.495 -24.120 20.794 1.00 16.24 ? 84 ASN B ND2 1 ATOM 4993 N N . LEU B 1 85 ? 21.509 -22.312 18.020 1.00 18.83 ? 85 LEU B N 1 ATOM 4994 C CA . LEU B 1 85 ? 20.077 -22.423 17.704 1.00 19.31 ? 85 LEU B CA 1 ATOM 4995 C C . LEU B 1 85 ? 19.970 -23.101 16.340 1.00 19.31 ? 85 LEU B C 1 ATOM 4996 O O . LEU B 1 85 ? 20.952 -23.142 15.600 1.00 20.13 ? 85 LEU B O 1 ATOM 4997 C CB . LEU B 1 85 ? 19.395 -21.049 17.648 1.00 18.87 ? 85 LEU B CB 1 ATOM 4998 C CG . LEU B 1 85 ? 19.344 -20.173 18.905 1.00 17.63 ? 85 LEU B CG 1 ATOM 4999 C CD1 . LEU B 1 85 ? 18.773 -18.824 18.549 1.00 16.62 ? 85 LEU B CD1 1 ATOM 5000 C CD2 . LEU B 1 85 ? 18.552 -20.807 20.011 1.00 17.85 ? 85 LEU B CD2 1 ATOM 5001 N N . VAL B 1 86 ? 18.793 -23.636 16.020 1.00 18.87 ? 86 VAL B N 1 ATOM 5002 C CA . VAL B 1 86 ? 18.580 -24.350 14.761 1.00 18.94 ? 86 VAL B CA 1 ATOM 5003 C C . VAL B 1 86 ? 18.576 -23.450 13.528 1.00 18.21 ? 86 VAL B C 1 ATOM 5004 O O . VAL B 1 86 ? 19.445 -23.583 12.665 1.00 16.29 ? 86 VAL B O 1 ATOM 5005 C CB . VAL B 1 86 ? 17.279 -25.220 14.807 1.00 19.46 ? 86 VAL B CB 1 ATOM 5006 C CG1 . VAL B 1 86 ? 17.177 -26.127 13.579 1.00 19.15 ? 86 VAL B CG1 1 ATOM 5007 C CG2 . VAL B 1 86 ? 17.254 -26.076 16.072 1.00 18.92 ? 86 VAL B CG2 1 ATOM 5008 N N . THR B 1 87 ? 17.628 -22.513 13.479 1.00 20.37 ? 87 THR B N 1 ATOM 5009 C CA . THR B 1 87 ? 17.483 -21.605 12.333 1.00 19.95 ? 87 THR B CA 1 ATOM 5010 C C . THR B 1 87 ? 17.793 -20.127 12.565 1.00 18.42 ? 87 THR B C 1 ATOM 5011 O O . THR B 1 87 ? 18.427 -19.481 11.726 1.00 18.44 ? 87 THR B O 1 ATOM 5012 C CB . THR B 1 87 ? 16.061 -21.687 11.738 1.00 20.27 ? 87 THR B CB 1 ATOM 5013 O OG1 . THR B 1 87 ? 15.106 -21.293 12.729 1.00 22.62 ? 87 THR B OG1 1 ATOM 5014 C CG2 . THR B 1 87 ? 15.743 -23.093 11.270 1.00 20.43 ? 87 THR B CG2 1 ATOM 5015 N N . ASN B 1 88 ? 17.320 -19.600 13.693 1.00 16.97 ? 88 ASN B N 1 ATOM 5016 C CA . ASN B 1 88 ? 17.486 -18.195 14.067 1.00 14.61 ? 88 ASN B CA 1 ATOM 5017 C C . ASN B 1 88 ? 18.891 -17.631 14.153 1.00 14.50 ? 88 ASN B C 1 ATOM 5018 O O . ASN B 1 88 ? 19.827 -18.301 14.600 1.00 15.60 ? 88 ASN B O 1 ATOM 5019 C CB . ASN B 1 88 ? 16.862 -17.934 15.431 1.00 14.07 ? 88 ASN B CB 1 ATOM 5020 C CG . ASN B 1 88 ? 15.371 -17.816 15.399 1.00 14.98 ? 88 ASN B CG 1 ATOM 5021 O OD1 . ASN B 1 88 ? 14.792 -17.344 16.371 1.00 10.62 ? 88 ASN B OD1 1 ATOM 5022 N ND2 . ASN B 1 88 ? 14.728 -18.260 14.326 1.00 16.98 ? 88 ASN B ND2 1 ATOM 5023 N N . GLY B 1 89 ? 19.009 -16.366 13.762 1.00 13.77 ? 89 GLY B N 1 ATOM 5024 C CA . GLY B 1 89 ? 20.265 -15.651 13.898 1.00 10.88 ? 89 GLY B CA 1 ATOM 5025 C C . GLY B 1 89 ? 20.151 -15.010 15.274 1.00 10.93 ? 89 GLY B C 1 ATOM 5026 O O . GLY B 1 89 ? 19.128 -15.205 15.957 1.00 7.75 ? 89 GLY B O 1 ATOM 5027 N N . THR B 1 90 ? 21.164 -14.266 15.702 1.00 8.66 ? 90 THR B N 1 ATOM 5028 C CA . THR B 1 90 ? 21.106 -13.628 17.008 1.00 9.01 ? 90 THR B CA 1 ATOM 5029 C C . THR B 1 90 ? 22.096 -12.484 17.178 1.00 11.96 ? 90 THR B C 1 ATOM 5030 O O . THR B 1 90 ? 22.914 -12.205 16.306 1.00 12.46 ? 90 THR B O 1 ATOM 5031 C CB . THR B 1 90 ? 21.267 -14.666 18.166 1.00 7.12 ? 90 THR B CB 1 ATOM 5032 O OG1 . THR B 1 90 ? 20.805 -14.094 19.397 1.00 10.68 ? 90 THR B OG1 1 ATOM 5033 C CG2 . THR B 1 90 ? 22.702 -15.124 18.313 1.00 6.96 ? 90 THR B CG2 1 ATOM 5034 N N . SER B 1 91 ? 21.985 -11.838 18.332 1.00 12.82 ? 91 SER B N 1 ATOM 5035 C CA . SER B 1 91 ? 22.821 -10.728 18.750 1.00 13.81 ? 91 SER B CA 1 ATOM 5036 C C . SER B 1 91 ? 22.415 -10.475 20.180 1.00 14.95 ? 91 SER B C 1 ATOM 5037 O O . SER B 1 91 ? 21.383 -10.974 20.625 1.00 16.55 ? 91 SER B O 1 ATOM 5038 C CB . SER B 1 91 ? 22.530 -9.473 17.925 1.00 13.52 ? 91 SER B CB 1 ATOM 5039 O OG . SER B 1 91 ? 21.169 -9.096 18.021 1.00 12.08 ? 91 SER B OG 1 ATOM 5040 N N . ILE B 1 92 ? 23.268 -9.807 20.942 1.00 15.38 ? 92 ILE B N 1 ATOM 5041 C CA . ILE B 1 92 ? 22.896 -9.472 22.304 1.00 16.77 ? 92 ILE B CA 1 ATOM 5042 C C . ILE B 1 92 ? 23.043 -7.971 22.435 1.00 16.59 ? 92 ILE B C 1 ATOM 5043 O O . ILE B 1 92 ? 24.131 -7.421 22.238 1.00 16.06 ? 92 ILE B O 1 ATOM 5044 C CB . ILE B 1 92 ? 23.743 -10.186 23.405 1.00 17.70 ? 92 ILE B CB 1 ATOM 5045 C CG1 . ILE B 1 92 ? 23.650 -11.715 23.305 1.00 18.62 ? 92 ILE B CG1 1 ATOM 5046 C CG2 . ILE B 1 92 ? 23.262 -9.746 24.802 1.00 18.99 ? 92 ILE B CG2 1 ATOM 5047 C CD1 . ILE B 1 92 ? 22.302 -12.323 23.642 1.00 20.69 ? 92 ILE B CD1 1 ATOM 5048 N N . HIS B 1 93 ? 21.916 -7.319 22.707 1.00 17.12 ? 93 HIS B N 1 ATOM 5049 C CA . HIS B 1 93 ? 21.878 -5.885 22.915 1.00 18.33 ? 93 HIS B CA 1 ATOM 5050 C C . HIS B 1 93 ? 22.025 -5.611 24.421 1.00 18.24 ? 93 HIS B C 1 ATOM 5051 O O . HIS B 1 93 ? 21.337 -6.207 25.240 1.00 17.98 ? 93 HIS B O 1 ATOM 5052 C CB . HIS B 1 93 ? 20.589 -5.272 22.346 1.00 17.60 ? 93 HIS B CB 1 ATOM 5053 C CG . HIS B 1 93 ? 20.431 -3.815 22.660 1.00 20.12 ? 93 HIS B CG 1 ATOM 5054 N ND1 . HIS B 1 93 ? 21.439 -2.898 22.445 1.00 21.45 ? 93 HIS B ND1 1 ATOM 5055 C CD2 . HIS B 1 93 ? 19.452 -3.148 23.315 1.00 19.92 ? 93 HIS B CD2 1 ATOM 5056 C CE1 . HIS B 1 93 ? 21.097 -1.737 22.971 1.00 19.17 ? 93 HIS B CE1 1 ATOM 5057 N NE2 . HIS B 1 93 ? 19.895 -1.863 23.503 1.00 19.66 ? 93 HIS B NE2 1 ATOM 5058 N N . TRP B 1 94 ? 22.912 -4.679 24.751 1.00 20.32 ? 94 TRP B N 1 ATOM 5059 C CA . TRP B 1 94 ? 23.210 -4.308 26.132 1.00 21.28 ? 94 TRP B CA 1 ATOM 5060 C C . TRP B 1 94 ? 22.508 -2.989 26.485 1.00 21.58 ? 94 TRP B C 1 ATOM 5061 O O . TRP B 1 94 ? 23.095 -1.909 26.412 1.00 21.14 ? 94 TRP B O 1 ATOM 5062 C CB . TRP B 1 94 ? 24.736 -4.224 26.316 1.00 22.02 ? 94 TRP B CB 1 ATOM 5063 C CG . TRP B 1 94 ? 25.508 -5.312 25.591 1.00 24.64 ? 94 TRP B CG 1 ATOM 5064 C CD1 . TRP B 1 94 ? 26.032 -5.240 24.330 1.00 24.58 ? 94 TRP B CD1 1 ATOM 5065 C CD2 . TRP B 1 94 ? 25.781 -6.641 26.061 1.00 26.07 ? 94 TRP B CD2 1 ATOM 5066 N NE1 . TRP B 1 94 ? 26.605 -6.440 23.979 1.00 25.58 ? 94 TRP B NE1 1 ATOM 5067 C CE2 . TRP B 1 94 ? 26.469 -7.320 25.019 1.00 25.52 ? 94 TRP B CE2 1 ATOM 5068 C CE3 . TRP B 1 94 ? 25.512 -7.331 27.263 1.00 26.56 ? 94 TRP B CE3 1 ATOM 5069 C CZ2 . TRP B 1 94 ? 26.890 -8.665 25.138 1.00 26.04 ? 94 TRP B CZ2 1 ATOM 5070 C CZ3 . TRP B 1 94 ? 25.932 -8.678 27.384 1.00 25.61 ? 94 TRP B CZ3 1 ATOM 5071 C CH2 . TRP B 1 94 ? 26.612 -9.323 26.321 1.00 25.56 ? 94 TRP B CH2 1 ATOM 5072 N N . HIS B 1 95 ? 21.222 -3.117 26.821 1.00 23.37 ? 95 HIS B N 1 ATOM 5073 C CA . HIS B 1 95 ? 20.305 -2.028 27.193 1.00 23.19 ? 95 HIS B CA 1 ATOM 5074 C C . HIS B 1 95 ? 20.834 -1.323 28.438 1.00 23.51 ? 95 HIS B C 1 ATOM 5075 O O . HIS B 1 95 ? 21.032 -1.953 29.476 1.00 22.31 ? 95 HIS B O 1 ATOM 5076 C CB . HIS B 1 95 ? 18.913 -2.654 27.449 1.00 24.84 ? 95 HIS B CB 1 ATOM 5077 C CG . HIS B 1 95 ? 17.790 -1.682 27.690 1.00 25.87 ? 95 HIS B CG 1 ATOM 5078 N ND1 . HIS B 1 95 ? 16.544 -1.856 27.128 1.00 26.67 ? 95 HIS B ND1 1 ATOM 5079 C CD2 . HIS B 1 95 ? 17.682 -0.603 28.504 1.00 26.79 ? 95 HIS B CD2 1 ATOM 5080 C CE1 . HIS B 1 95 ? 15.719 -0.932 27.587 1.00 27.17 ? 95 HIS B CE1 1 ATOM 5081 N NE2 . HIS B 1 95 ? 16.384 -0.158 28.423 1.00 26.79 ? 95 HIS B NE2 1 ATOM 5082 N N . GLY B 1 96 ? 21.023 -0.010 28.320 1.00 23.36 ? 96 GLY B N 1 ATOM 5083 C CA . GLY B 1 96 ? 21.525 0.778 29.433 1.00 25.63 ? 96 GLY B CA 1 ATOM 5084 C C . GLY B 1 96 ? 23.015 1.026 29.357 1.00 27.00 ? 96 GLY B C 1 ATOM 5085 O O . GLY B 1 96 ? 23.589 1.735 30.192 1.00 29.18 ? 96 GLY B O 1 ATOM 5086 N N . ILE B 1 97 ? 23.661 0.369 28.399 1.00 26.63 ? 97 ILE B N 1 ATOM 5087 C CA . ILE B 1 97 ? 25.086 0.546 28.197 1.00 25.18 ? 97 ILE B CA 1 ATOM 5088 C C . ILE B 1 97 ? 25.195 1.448 26.984 1.00 24.74 ? 97 ILE B C 1 ATOM 5089 O O . ILE B 1 97 ? 24.767 1.099 25.880 1.00 23.45 ? 97 ILE B O 1 ATOM 5090 C CB . ILE B 1 97 ? 25.845 -0.796 28.016 1.00 23.28 ? 97 ILE B CB 1 ATOM 5091 C CG1 . ILE B 1 97 ? 25.534 -1.760 29.177 1.00 24.55 ? 97 ILE B CG1 1 ATOM 5092 C CG2 . ILE B 1 97 ? 27.342 -0.546 27.900 1.00 24.38 ? 97 ILE B CG2 1 ATOM 5093 C CD1 . ILE B 1 97 ? 25.780 -1.226 30.614 1.00 22.02 ? 97 ILE B CD1 1 ATOM 5094 N N . HIS B 1 98 ? 25.709 2.645 27.250 1.00 24.73 ? 98 HIS B N 1 ATOM 5095 C CA . HIS B 1 98 ? 25.888 3.701 26.271 1.00 25.28 ? 98 HIS B CA 1 ATOM 5096 C C . HIS B 1 98 ? 26.669 3.333 25.023 1.00 24.12 ? 98 HIS B C 1 ATOM 5097 O O . HIS B 1 98 ? 26.362 3.813 23.934 1.00 22.61 ? 98 HIS B O 1 ATOM 5098 C CB . HIS B 1 98 ? 26.544 4.911 26.943 1.00 28.69 ? 98 HIS B CB 1 ATOM 5099 C CG . HIS B 1 98 ? 25.626 5.690 27.832 1.00 31.00 ? 98 HIS B CG 1 ATOM 5100 N ND1 . HIS B 1 98 ? 26.049 6.792 28.543 1.00 32.36 ? 98 HIS B ND1 1 ATOM 5101 C CD2 . HIS B 1 98 ? 24.302 5.561 28.089 1.00 31.89 ? 98 HIS B CD2 1 ATOM 5102 C CE1 . HIS B 1 98 ? 25.024 7.311 29.194 1.00 31.62 ? 98 HIS B CE1 1 ATOM 5103 N NE2 . HIS B 1 98 ? 23.953 6.582 28.936 1.00 31.99 ? 98 HIS B NE2 1 ATOM 5104 N N . GLN B 1 99 ? 27.652 2.449 25.191 1.00 23.97 ? 99 GLN B N 1 ATOM 5105 C CA . GLN B 1 99 ? 28.529 1.992 24.115 1.00 24.98 ? 99 GLN B CA 1 ATOM 5106 C C . GLN B 1 99 ? 29.293 3.177 23.496 1.00 25.13 ? 99 GLN B C 1 ATOM 5107 O O . GLN B 1 99 ? 29.264 3.381 22.275 1.00 25.68 ? 99 GLN B O 1 ATOM 5108 C CB . GLN B 1 99 ? 27.752 1.202 23.027 1.00 26.28 ? 99 GLN B CB 1 ATOM 5109 C CG . GLN B 1 99 ? 27.017 -0.068 23.485 1.00 25.92 ? 99 GLN B CG 1 ATOM 5110 C CD . GLN B 1 99 ? 27.928 -1.257 23.781 1.00 26.53 ? 99 GLN B CD 1 ATOM 5111 O OE1 . GLN B 1 99 ? 27.486 -2.239 24.374 1.00 28.73 ? 99 GLN B OE1 1 ATOM 5112 N NE2 . GLN B 1 99 ? 29.189 -1.182 23.359 1.00 25.02 ? 99 GLN B NE2 1 ATOM 5113 N N . LYS B 1 100 ? 29.943 3.963 24.363 1.00 24.86 ? 100 LYS B N 1 ATOM 5114 C CA . LYS B 1 100 ? 30.726 5.146 23.973 1.00 24.09 ? 100 LYS B CA 1 ATOM 5115 C C . LYS B 1 100 ? 31.881 4.792 23.030 1.00 23.02 ? 100 LYS B C 1 ATOM 5116 O O . LYS B 1 100 ? 32.831 4.092 23.411 1.00 21.85 ? 100 LYS B O 1 ATOM 5117 C CB . LYS B 1 100 ? 31.228 5.899 25.218 1.00 24.79 ? 100 LYS B CB 1 ATOM 5118 C CG . LYS B 1 100 ? 31.864 7.290 24.970 1.00 25.83 ? 100 LYS B CG 1 ATOM 5119 C CD . LYS B 1 100 ? 30.855 8.375 24.573 1.00 26.12 ? 100 LYS B CD 1 ATOM 5120 C CE . LYS B 1 100 ? 30.266 9.113 25.772 1.00 28.22 ? 100 LYS B CE 1 ATOM 5121 N NZ . LYS B 1 100 ? 29.394 8.266 26.630 1.00 28.45 ? 100 LYS B NZ 1 ATOM 5122 N N . ASP B 1 101 ? 31.726 5.245 21.780 1.00 23.16 ? 101 ASP B N 1 ATOM 5123 C CA . ASP B 1 101 ? 32.659 5.034 20.656 1.00 24.43 ? 101 ASP B CA 1 ATOM 5124 C C . ASP B 1 101 ? 32.870 3.555 20.292 1.00 21.79 ? 101 ASP B C 1 ATOM 5125 O O . ASP B 1 101 ? 33.849 3.194 19.644 1.00 21.82 ? 101 ASP B O 1 ATOM 5126 C CB . ASP B 1 101 ? 34.003 5.761 20.880 1.00 27.76 ? 101 ASP B CB 1 ATOM 5127 C CG . ASP B 1 101 ? 33.836 7.260 21.049 1.00 29.90 ? 101 ASP B CG 1 ATOM 5128 O OD1 . ASP B 1 101 ? 33.464 7.933 20.062 1.00 28.68 ? 101 ASP B OD1 1 ATOM 5129 O OD2 . ASP B 1 101 ? 34.067 7.756 22.177 1.00 31.76 ? 101 ASP B OD2 1 ATOM 5130 N N . THR B 1 102 ? 31.936 2.714 20.743 1.00 20.43 ? 102 THR B N 1 ATOM 5131 C CA . THR B 1 102 ? 31.938 1.272 20.494 1.00 17.86 ? 102 THR B CA 1 ATOM 5132 C C . THR B 1 102 ? 30.571 0.856 19.906 1.00 17.48 ? 102 THR B C 1 ATOM 5133 O O . THR B 1 102 ? 30.015 -0.194 20.260 1.00 15.78 ? 102 THR B O 1 ATOM 5134 C CB . THR B 1 102 ? 32.260 0.444 21.792 1.00 16.94 ? 102 THR B CB 1 ATOM 5135 O OG1 . THR B 1 102 ? 31.390 0.833 22.862 1.00 14.50 ? 102 THR B OG1 1 ATOM 5136 C CG2 . THR B 1 102 ? 33.713 0.620 22.226 1.00 16.52 ? 102 THR B CG2 1 ATOM 5137 N N . ASN B 1 103 ? 30.076 1.668 18.963 1.00 16.88 ? 103 ASN B N 1 ATOM 5138 C CA . ASN B 1 103 ? 28.787 1.465 18.270 1.00 16.41 ? 103 ASN B CA 1 ATOM 5139 C C . ASN B 1 103 ? 28.545 0.055 17.715 1.00 16.52 ? 103 ASN B C 1 ATOM 5140 O O . ASN B 1 103 ? 27.439 -0.470 17.818 1.00 16.30 ? 103 ASN B O 1 ATOM 5141 C CB . ASN B 1 103 ? 28.631 2.506 17.146 1.00 13.62 ? 103 ASN B CB 1 ATOM 5142 C CG . ASN B 1 103 ? 27.273 2.437 16.438 1.00 11.76 ? 103 ASN B CG 1 ATOM 5143 O OD1 . ASN B 1 103 ? 27.203 2.492 15.208 1.00 11.24 ? 103 ASN B OD1 1 ATOM 5144 N ND2 . ASN B 1 103 ? 26.198 2.330 17.209 1.00 6.70 ? 103 ASN B ND2 1 ATOM 5145 N N . LEU B 1 104 ? 29.604 -0.569 17.201 1.00 16.74 ? 104 LEU B N 1 ATOM 5146 C CA . LEU B 1 104 ? 29.529 -1.906 16.624 1.00 16.52 ? 104 LEU B CA 1 ATOM 5147 C C . LEU B 1 104 ? 29.344 -3.057 17.615 1.00 16.76 ? 104 LEU B C 1 ATOM 5148 O O . LEU B 1 104 ? 29.246 -4.221 17.213 1.00 18.20 ? 104 LEU B O 1 ATOM 5149 C CB . LEU B 1 104 ? 30.727 -2.143 15.715 1.00 17.29 ? 104 LEU B CB 1 ATOM 5150 C CG . LEU B 1 104 ? 30.612 -1.502 14.328 1.00 18.43 ? 104 LEU B CG 1 ATOM 5151 C CD1 . LEU B 1 104 ? 30.712 0.026 14.370 1.00 18.30 ? 104 LEU B CD1 1 ATOM 5152 C CD2 . LEU B 1 104 ? 31.698 -2.078 13.459 1.00 16.91 ? 104 LEU B CD2 1 ATOM 5153 N N . HIS B 1 105 ? 29.275 -2.718 18.903 1.00 16.04 ? 105 HIS B N 1 ATOM 5154 C CA . HIS B 1 105 ? 29.060 -3.688 19.972 1.00 15.12 ? 105 HIS B CA 1 ATOM 5155 C C . HIS B 1 105 ? 27.650 -3.564 20.565 1.00 15.19 ? 105 HIS B C 1 ATOM 5156 O O . HIS B 1 105 ? 27.327 -4.250 21.534 1.00 18.19 ? 105 HIS B O 1 ATOM 5157 C CB . HIS B 1 105 ? 30.109 -3.515 21.073 1.00 15.03 ? 105 HIS B CB 1 ATOM 5158 C CG . HIS B 1 105 ? 31.491 -3.930 20.669 1.00 15.45 ? 105 HIS B CG 1 ATOM 5159 N ND1 . HIS B 1 105 ? 31.892 -5.249 20.633 1.00 13.47 ? 105 HIS B ND1 1 ATOM 5160 C CD2 . HIS B 1 105 ? 32.568 -3.200 20.299 1.00 14.96 ? 105 HIS B CD2 1 ATOM 5161 C CE1 . HIS B 1 105 ? 33.157 -5.313 20.261 1.00 15.12 ? 105 HIS B CE1 1 ATOM 5162 N NE2 . HIS B 1 105 ? 33.592 -4.083 20.053 1.00 17.54 ? 105 HIS B NE2 1 ATOM 5163 N N . ASP B 1 106 ? 26.805 -2.733 19.946 1.00 13.50 ? 106 ASP B N 1 ATOM 5164 C CA . ASP B 1 106 ? 25.427 -2.484 20.396 1.00 12.04 ? 106 ASP B CA 1 ATOM 5165 C C . ASP B 1 106 ? 24.452 -3.668 20.258 1.00 12.14 ? 106 ASP B C 1 ATOM 5166 O O . ASP B 1 106 ? 23.510 -3.785 21.041 1.00 10.82 ? 106 ASP B O 1 ATOM 5167 C CB . ASP B 1 106 ? 24.862 -1.228 19.706 1.00 11.63 ? 106 ASP B CB 1 ATOM 5168 C CG . ASP B 1 106 ? 23.714 -0.583 20.483 1.00 11.73 ? 106 ASP B CG 1 ATOM 5169 O OD1 . ASP B 1 106 ? 23.821 -0.460 21.723 1.00 16.06 ? 106 ASP B OD1 1 ATOM 5170 O OD2 . ASP B 1 106 ? 22.706 -0.194 19.858 1.00 7.86 ? 106 ASP B OD2 1 ATOM 5171 N N . GLY B 1 107 ? 24.672 -4.523 19.261 1.00 12.77 ? 107 GLY B N 1 ATOM 5172 C CA . GLY B 1 107 ? 23.824 -5.690 19.066 1.00 12.42 ? 107 GLY B CA 1 ATOM 5173 C C . GLY B 1 107 ? 22.526 -5.496 18.300 1.00 12.89 ? 107 GLY B C 1 ATOM 5174 O O . GLY B 1 107 ? 21.675 -6.385 18.277 1.00 11.30 ? 107 GLY B O 1 ATOM 5175 N N . ALA B 1 108 ? 22.370 -4.341 17.667 1.00 12.13 ? 108 ALA B N 1 ATOM 5176 C CA . ALA B 1 108 ? 21.168 -4.069 16.899 1.00 13.84 ? 108 ALA B CA 1 ATOM 5177 C C . ALA B 1 108 ? 21.333 -4.627 15.479 1.00 14.82 ? 108 ALA B C 1 ATOM 5178 O O . ALA B 1 108 ? 22.137 -4.139 14.687 1.00 17.74 ? 108 ALA B O 1 ATOM 5179 C CB . ALA B 1 108 ? 20.871 -2.575 16.893 1.00 12.22 ? 108 ALA B CB 1 ATOM 5180 N N . ASN B 1 109 ? 20.605 -5.707 15.210 1.00 15.17 ? 109 ASN B N 1 ATOM 5181 C CA . ASN B 1 109 ? 20.611 -6.404 13.927 1.00 16.10 ? 109 ASN B CA 1 ATOM 5182 C C . ASN B 1 109 ? 20.112 -5.552 12.776 1.00 16.45 ? 109 ASN B C 1 ATOM 5183 O O . ASN B 1 109 ? 19.043 -4.940 12.863 1.00 16.99 ? 109 ASN B O 1 ATOM 5184 C CB . ASN B 1 109 ? 19.765 -7.674 14.016 1.00 16.41 ? 109 ASN B CB 1 ATOM 5185 C CG . ASN B 1 109 ? 20.422 -8.752 14.841 1.00 15.67 ? 109 ASN B CG 1 ATOM 5186 O OD1 . ASN B 1 109 ? 21.599 -9.056 14.658 1.00 14.01 ? 109 ASN B OD1 1 ATOM 5187 N ND2 . ASN B 1 109 ? 19.664 -9.345 15.749 1.00 14.49 ? 109 ASN B ND2 1 ATOM 5188 N N . GLY B 1 110 ? 20.911 -5.522 11.709 1.00 15.46 ? 110 GLY B N 1 ATOM 5189 C CA . GLY B 1 110 ? 20.593 -4.742 10.528 1.00 14.85 ? 110 GLY B CA 1 ATOM 5190 C C . GLY B 1 110 ? 20.928 -3.269 10.700 1.00 15.17 ? 110 GLY B C 1 ATOM 5191 O O . GLY B 1 110 ? 20.578 -2.430 9.869 1.00 14.29 ? 110 GLY B O 1 ATOM 5192 N N . VAL B 1 111 ? 21.638 -2.969 11.784 1.00 15.03 ? 111 VAL B N 1 ATOM 5193 C CA . VAL B 1 111 ? 22.035 -1.612 12.134 1.00 14.40 ? 111 VAL B CA 1 ATOM 5194 C C . VAL B 1 111 ? 23.537 -1.578 12.427 1.00 14.08 ? 111 VAL B C 1 ATOM 5195 O O . VAL B 1 111 ? 24.304 -1.008 11.648 1.00 14.51 ? 111 VAL B O 1 ATOM 5196 C CB . VAL B 1 111 ? 21.215 -1.105 13.384 1.00 13.94 ? 111 VAL B CB 1 ATOM 5197 C CG1 . VAL B 1 111 ? 21.623 0.306 13.812 1.00 11.94 ? 111 VAL B CG1 1 ATOM 5198 C CG2 . VAL B 1 111 ? 19.723 -1.155 13.101 1.00 12.72 ? 111 VAL B CG2 1 ATOM 5199 N N . THR B 1 112 ? 23.943 -2.229 13.522 1.00 11.98 ? 112 THR B N 1 ATOM 5200 C CA . THR B 1 112 ? 25.341 -2.255 13.969 1.00 10.80 ? 112 THR B CA 1 ATOM 5201 C C . THR B 1 112 ? 26.091 -3.532 13.637 1.00 11.87 ? 112 THR B C 1 ATOM 5202 O O . THR B 1 112 ? 27.327 -3.584 13.727 1.00 10.27 ? 112 THR B O 1 ATOM 5203 C CB . THR B 1 112 ? 25.453 -1.987 15.492 1.00 9.39 ? 112 THR B CB 1 ATOM 5204 O OG1 . THR B 1 112 ? 24.716 -2.979 16.222 1.00 8.00 ? 112 THR B OG1 1 ATOM 5205 C CG2 . THR B 1 112 ? 24.924 -0.601 15.830 1.00 6.17 ? 112 THR B CG2 1 ATOM 5206 N N . GLU B 1 113 ? 25.325 -4.561 13.280 1.00 13.35 ? 113 GLU B N 1 ATOM 5207 C CA . GLU B 1 113 ? 25.855 -5.874 12.922 1.00 13.62 ? 113 GLU B CA 1 ATOM 5208 C C . GLU B 1 113 ? 24.833 -6.708 12.177 1.00 14.72 ? 113 GLU B C 1 ATOM 5209 O O . GLU B 1 113 ? 23.646 -6.353 12.101 1.00 14.65 ? 113 GLU B O 1 ATOM 5210 C CB . GLU B 1 113 ? 26.298 -6.652 14.167 1.00 13.91 ? 113 GLU B CB 1 ATOM 5211 C CG . GLU B 1 113 ? 25.190 -6.977 15.156 1.00 14.80 ? 113 GLU B CG 1 ATOM 5212 C CD . GLU B 1 113 ? 25.629 -7.999 16.158 1.00 18.90 ? 113 GLU B CD 1 ATOM 5213 O OE1 . GLU B 1 113 ? 25.907 -7.604 17.307 1.00 17.63 ? 113 GLU B OE1 1 ATOM 5214 O OE2 . GLU B 1 113 ? 25.705 -9.196 15.792 1.00 22.54 ? 113 GLU B OE2 1 ATOM 5215 N N . CYS B 1 114 ? 25.327 -7.789 11.580 1.00 14.46 ? 114 CYS B N 1 ATOM 5216 C CA . CYS B 1 114 ? 24.479 -8.757 10.903 1.00 16.03 ? 114 CYS B CA 1 ATOM 5217 C C . CYS B 1 114 ? 24.251 -9.789 12.005 1.00 16.04 ? 114 CYS B C 1 ATOM 5218 O O . CYS B 1 114 ? 25.048 -9.856 12.952 1.00 18.13 ? 114 CYS B O 1 ATOM 5219 C CB . CYS B 1 114 ? 25.211 -9.432 9.739 1.00 16.06 ? 114 CYS B CB 1 ATOM 5220 S SG . CYS B 1 114 ? 25.469 -8.439 8.235 1.00 14.95 ? 114 CYS B SG 1 ATOM 5221 N N . PRO B 1 115 ? 23.153 -10.575 11.934 1.00 15.73 ? 115 PRO B N 1 ATOM 5222 C CA . PRO B 1 115 ? 22.913 -11.580 12.975 1.00 15.63 ? 115 PRO B CA 1 ATOM 5223 C C . PRO B 1 115 ? 23.960 -12.672 12.957 1.00 15.19 ? 115 PRO B C 1 ATOM 5224 O O . PRO B 1 115 ? 24.441 -13.069 11.890 1.00 15.29 ? 115 PRO B O 1 ATOM 5225 C CB . PRO B 1 115 ? 21.555 -12.153 12.594 1.00 17.46 ? 115 PRO B CB 1 ATOM 5226 C CG . PRO B 1 115 ? 20.890 -11.036 11.923 1.00 17.12 ? 115 PRO B CG 1 ATOM 5227 C CD . PRO B 1 115 ? 21.967 -10.456 11.070 1.00 16.28 ? 115 PRO B CD 1 ATOM 5228 N N . ILE B 1 116 ? 24.348 -13.108 14.149 1.00 14.59 ? 116 ILE B N 1 ATOM 5229 C CA . ILE B 1 116 ? 25.324 -14.178 14.308 1.00 16.19 ? 116 ILE B CA 1 ATOM 5230 C C . ILE B 1 116 ? 24.622 -15.444 13.775 1.00 16.08 ? 116 ILE B C 1 ATOM 5231 O O . ILE B 1 116 ? 23.514 -15.766 14.215 1.00 16.16 ? 116 ILE B O 1 ATOM 5232 C CB . ILE B 1 116 ? 25.721 -14.346 15.811 1.00 16.69 ? 116 ILE B CB 1 ATOM 5233 C CG1 . ILE B 1 116 ? 26.296 -13.040 16.366 1.00 16.38 ? 116 ILE B CG1 1 ATOM 5234 C CG2 . ILE B 1 116 ? 26.750 -15.432 15.970 1.00 14.47 ? 116 ILE B CG2 1 ATOM 5235 C CD1 . ILE B 1 116 ? 26.268 -12.952 17.885 1.00 17.04 ? 116 ILE B CD1 1 ATOM 5236 N N . PRO B 1 117 ? 25.209 -16.117 12.760 1.00 17.17 ? 117 PRO B N 1 ATOM 5237 C CA . PRO B 1 117 ? 24.571 -17.328 12.220 1.00 17.63 ? 117 PRO B CA 1 ATOM 5238 C C . PRO B 1 117 ? 24.435 -18.494 13.214 1.00 16.23 ? 117 PRO B C 1 ATOM 5239 O O . PRO B 1 117 ? 25.188 -18.570 14.185 1.00 17.10 ? 117 PRO B O 1 ATOM 5240 C CB . PRO B 1 117 ? 25.476 -17.685 11.026 1.00 15.64 ? 117 PRO B CB 1 ATOM 5241 C CG . PRO B 1 117 ? 26.796 -17.162 11.423 1.00 15.99 ? 117 PRO B CG 1 ATOM 5242 C CD . PRO B 1 117 ? 26.448 -15.819 12.013 1.00 17.15 ? 117 PRO B CD 1 ATOM 5243 N N . PRO B 1 118 ? 23.409 -19.357 13.039 1.00 15.75 ? 118 PRO B N 1 ATOM 5244 C CA . PRO B 1 118 ? 23.219 -20.504 13.931 1.00 15.73 ? 118 PRO B CA 1 ATOM 5245 C C . PRO B 1 118 ? 24.230 -21.628 13.669 1.00 15.90 ? 118 PRO B C 1 ATOM 5246 O O . PRO B 1 118 ? 25.241 -21.414 12.991 1.00 14.62 ? 118 PRO B O 1 ATOM 5247 C CB . PRO B 1 118 ? 21.788 -20.935 13.611 1.00 14.36 ? 118 PRO B CB 1 ATOM 5248 C CG . PRO B 1 118 ? 21.647 -20.603 12.217 1.00 13.97 ? 118 PRO B CG 1 ATOM 5249 C CD . PRO B 1 118 ? 22.234 -19.221 12.162 1.00 15.18 ? 118 PRO B CD 1 ATOM 5250 N N . LYS B 1 119 ? 23.928 -22.821 14.193 1.00 18.40 ? 119 LYS B N 1 ATOM 5251 C CA . LYS B 1 119 ? 24.755 -24.027 14.048 1.00 20.45 ? 119 LYS B CA 1 ATOM 5252 C C . LYS B 1 119 ? 26.240 -23.794 14.424 1.00 19.64 ? 119 LYS B C 1 ATOM 5253 O O . LYS B 1 119 ? 27.151 -24.209 13.699 1.00 21.54 ? 119 LYS B O 1 ATOM 5254 C CB . LYS B 1 119 ? 24.640 -24.592 12.617 1.00 24.58 ? 119 LYS B CB 1 ATOM 5255 C CG . LYS B 1 119 ? 23.229 -24.881 12.097 1.00 28.64 ? 119 LYS B CG 1 ATOM 5256 C CD . LYS B 1 119 ? 23.286 -25.089 10.574 1.00 32.46 ? 119 LYS B CD 1 ATOM 5257 C CE . LYS B 1 119 ? 21.911 -25.255 9.928 1.00 34.98 ? 119 LYS B CE 1 ATOM 5258 N NZ . LYS B 1 119 ? 21.291 -26.585 10.181 1.00 36.68 ? 119 LYS B NZ 1 ATOM 5259 N N . GLY B 1 120 ? 26.462 -23.045 15.506 1.00 18.38 ? 120 GLY B N 1 ATOM 5260 C CA . GLY B 1 120 ? 27.813 -22.763 15.970 1.00 17.46 ? 120 GLY B CA 1 ATOM 5261 C C . GLY B 1 120 ? 28.472 -21.426 15.657 1.00 16.42 ? 120 GLY B C 1 ATOM 5262 O O . GLY B 1 120 ? 29.669 -21.283 15.915 1.00 17.84 ? 120 GLY B O 1 ATOM 5263 N N . GLY B 1 121 ? 27.723 -20.452 15.127 1.00 16.98 ? 121 GLY B N 1 ATOM 5264 C CA . GLY B 1 121 ? 28.287 -19.140 14.814 1.00 15.88 ? 121 GLY B CA 1 ATOM 5265 C C . GLY B 1 121 ? 28.664 -18.380 16.077 1.00 17.36 ? 121 GLY B C 1 ATOM 5266 O O . GLY B 1 121 ? 28.011 -18.541 17.108 1.00 16.93 ? 121 GLY B O 1 ATOM 5267 N N . GLN B 1 122 ? 29.719 -17.570 16.013 1.00 18.74 ? 122 GLN B N 1 ATOM 5268 C CA . GLN B 1 122 ? 30.155 -16.811 17.180 1.00 19.40 ? 122 GLN B CA 1 ATOM 5269 C C . GLN B 1 122 ? 30.657 -15.396 16.936 1.00 18.56 ? 122 GLN B C 1 ATOM 5270 O O . GLN B 1 122 ? 30.997 -15.019 15.816 1.00 19.42 ? 122 GLN B O 1 ATOM 5271 C CB . GLN B 1 122 ? 31.177 -17.603 18.007 1.00 21.93 ? 122 GLN B CB 1 ATOM 5272 C CG . GLN B 1 122 ? 32.488 -17.939 17.317 1.00 25.79 ? 122 GLN B CG 1 ATOM 5273 C CD . GLN B 1 122 ? 33.465 -18.613 18.262 1.00 27.77 ? 122 GLN B CD 1 ATOM 5274 O OE1 . GLN B 1 122 ? 34.077 -17.957 19.110 1.00 28.84 ? 122 GLN B OE1 1 ATOM 5275 N NE2 . GLN B 1 122 ? 33.609 -19.929 18.129 1.00 28.07 ? 122 GLN B NE2 1 ATOM 5276 N N . ARG B 1 123 ? 30.648 -14.615 18.012 1.00 17.74 ? 123 ARG B N 1 ATOM 5277 C CA . ARG B 1 123 ? 31.106 -13.228 18.019 1.00 19.25 ? 123 ARG B CA 1 ATOM 5278 C C . ARG B 1 123 ? 31.374 -12.849 19.473 1.00 17.46 ? 123 ARG B C 1 ATOM 5279 O O . ARG B 1 123 ? 30.623 -13.215 20.373 1.00 19.79 ? 123 ARG B O 1 ATOM 5280 C CB . ARG B 1 123 ? 30.048 -12.293 17.409 1.00 17.11 ? 123 ARG B CB 1 ATOM 5281 C CG . ARG B 1 123 ? 30.528 -10.895 17.110 1.00 17.35 ? 123 ARG B CG 1 ATOM 5282 C CD . ARG B 1 123 ? 29.875 -9.878 18.028 1.00 17.47 ? 123 ARG B CD 1 ATOM 5283 N NE . ARG B 1 123 ? 30.661 -8.649 18.115 1.00 16.50 ? 123 ARG B NE 1 ATOM 5284 C CZ . ARG B 1 123 ? 30.169 -7.433 17.918 1.00 17.53 ? 123 ARG B CZ 1 ATOM 5285 N NH1 . ARG B 1 123 ? 28.884 -7.266 17.622 1.00 15.15 ? 123 ARG B NH1 1 ATOM 5286 N NH2 . ARG B 1 123 ? 30.966 -6.381 18.008 1.00 16.54 ? 123 ARG B NH2 1 ATOM 5287 N N . THR B 1 124 ? 32.438 -12.093 19.689 1.00 18.34 ? 124 THR B N 1 ATOM 5288 C CA . THR B 1 124 ? 32.795 -11.667 21.028 1.00 18.46 ? 124 THR B CA 1 ATOM 5289 C C . THR B 1 124 ? 32.603 -10.159 21.197 1.00 19.17 ? 124 THR B C 1 ATOM 5290 O O . THR B 1 124 ? 33.197 -9.357 20.474 1.00 20.56 ? 124 THR B O 1 ATOM 5291 C CB . THR B 1 124 ? 34.241 -12.134 21.395 1.00 18.84 ? 124 THR B CB 1 ATOM 5292 O OG1 . THR B 1 124 ? 34.340 -13.555 21.209 1.00 15.36 ? 124 THR B OG1 1 ATOM 5293 C CG2 . THR B 1 124 ? 34.570 -11.834 22.857 1.00 18.12 ? 124 THR B CG2 1 ATOM 5294 N N . TYR B 1 125 ? 31.719 -9.806 22.128 1.00 19.73 ? 125 TYR B N 1 ATOM 5295 C CA . TYR B 1 125 ? 31.394 -8.423 22.467 1.00 21.50 ? 125 TYR B CA 1 ATOM 5296 C C . TYR B 1 125 ? 32.307 -7.978 23.585 1.00 23.07 ? 125 TYR B C 1 ATOM 5297 O O . TYR B 1 125 ? 32.543 -8.735 24.521 1.00 24.05 ? 125 TYR B O 1 ATOM 5298 C CB . TYR B 1 125 ? 29.966 -8.301 22.999 1.00 20.90 ? 125 TYR B CB 1 ATOM 5299 C CG . TYR B 1 125 ? 28.864 -8.540 22.002 1.00 23.09 ? 125 TYR B CG 1 ATOM 5300 C CD1 . TYR B 1 125 ? 28.425 -9.848 21.705 1.00 21.62 ? 125 TYR B CD1 1 ATOM 5301 C CD2 . TYR B 1 125 ? 28.208 -7.459 21.384 1.00 23.21 ? 125 TYR B CD2 1 ATOM 5302 C CE1 . TYR B 1 125 ? 27.348 -10.074 20.815 1.00 21.63 ? 125 TYR B CE1 1 ATOM 5303 C CE2 . TYR B 1 125 ? 27.128 -7.670 20.487 1.00 24.02 ? 125 TYR B CE2 1 ATOM 5304 C CZ . TYR B 1 125 ? 26.709 -8.981 20.213 1.00 23.81 ? 125 TYR B CZ 1 ATOM 5305 O OH . TYR B 1 125 ? 25.676 -9.197 19.345 1.00 21.81 ? 125 TYR B OH 1 ATOM 5306 N N . ARG B 1 126 ? 32.798 -6.747 23.489 1.00 23.97 ? 126 ARG B N 1 ATOM 5307 C CA . ARG B 1 126 ? 33.666 -6.169 24.505 1.00 24.57 ? 126 ARG B CA 1 ATOM 5308 C C . ARG B 1 126 ? 33.287 -4.707 24.632 1.00 24.35 ? 126 ARG B C 1 ATOM 5309 O O . ARG B 1 126 ? 33.271 -3.978 23.636 1.00 24.80 ? 126 ARG B O 1 ATOM 5310 C CB . ARG B 1 126 ? 35.151 -6.309 24.128 1.00 25.30 ? 126 ARG B CB 1 ATOM 5311 C CG . ARG B 1 126 ? 36.114 -5.853 25.229 1.00 27.29 ? 126 ARG B CG 1 ATOM 5312 C CD . ARG B 1 126 ? 37.547 -5.768 24.741 1.00 29.56 ? 126 ARG B CD 1 ATOM 5313 N NE . ARG B 1 126 ? 38.442 -5.026 25.634 1.00 31.88 ? 126 ARG B NE 1 ATOM 5314 C CZ . ARG B 1 126 ? 39.105 -5.542 26.670 1.00 33.82 ? 126 ARG B CZ 1 ATOM 5315 N NH1 . ARG B 1 126 ? 38.989 -6.827 26.993 1.00 35.25 ? 126 ARG B NH1 1 ATOM 5316 N NH2 . ARG B 1 126 ? 39.911 -4.764 27.378 1.00 33.80 ? 126 ARG B NH2 1 ATOM 5317 N N . TRP B 1 127 ? 32.937 -4.302 25.850 1.00 24.38 ? 127 TRP B N 1 ATOM 5318 C CA . TRP B 1 127 ? 32.555 -2.917 26.133 1.00 25.29 ? 127 TRP B CA 1 ATOM 5319 C C . TRP B 1 127 ? 33.013 -2.430 27.492 1.00 24.92 ? 127 TRP B C 1 ATOM 5320 O O . TRP B 1 127 ? 33.175 -3.219 28.423 1.00 25.64 ? 127 TRP B O 1 ATOM 5321 C CB . TRP B 1 127 ? 31.035 -2.693 25.992 1.00 26.88 ? 127 TRP B CB 1 ATOM 5322 C CG . TRP B 1 127 ? 30.123 -3.736 26.609 1.00 26.83 ? 127 TRP B CG 1 ATOM 5323 C CD1 . TRP B 1 127 ? 29.583 -4.814 25.972 1.00 26.88 ? 127 TRP B CD1 1 ATOM 5324 C CD2 . TRP B 1 127 ? 29.567 -3.733 27.935 1.00 27.31 ? 127 TRP B CD2 1 ATOM 5325 N NE1 . TRP B 1 127 ? 28.714 -5.476 26.805 1.00 28.79 ? 127 TRP B NE1 1 ATOM 5326 C CE2 . TRP B 1 127 ? 28.681 -4.840 28.017 1.00 27.67 ? 127 TRP B CE2 1 ATOM 5327 C CE3 . TRP B 1 127 ? 29.724 -2.900 29.067 1.00 28.36 ? 127 TRP B CE3 1 ATOM 5328 C CZ2 . TRP B 1 127 ? 27.944 -5.144 29.194 1.00 28.33 ? 127 TRP B CZ2 1 ATOM 5329 C CZ3 . TRP B 1 127 ? 28.986 -3.201 30.253 1.00 26.05 ? 127 TRP B CZ3 1 ATOM 5330 C CH2 . TRP B 1 127 ? 28.108 -4.317 30.295 1.00 26.39 ? 127 TRP B CH2 1 ATOM 5331 N N . ARG B 1 128 ? 33.196 -1.120 27.603 1.00 22.81 ? 128 ARG B N 1 ATOM 5332 C CA . ARG B 1 128 ? 33.616 -0.518 28.855 1.00 22.15 ? 128 ARG B CA 1 ATOM 5333 C C . ARG B 1 128 ? 32.373 -0.120 29.665 1.00 21.32 ? 128 ARG B C 1 ATOM 5334 O O . ARG B 1 128 ? 31.373 0.347 29.106 1.00 19.16 ? 128 ARG B O 1 ATOM 5335 C CB . ARG B 1 128 ? 34.511 0.695 28.584 1.00 20.58 ? 128 ARG B CB 1 ATOM 5336 C CG . ARG B 1 128 ? 35.235 1.231 29.816 1.00 21.87 ? 128 ARG B CG 1 ATOM 5337 C CD . ARG B 1 128 ? 36.571 0.533 30.073 1.00 24.13 ? 128 ARG B CD 1 ATOM 5338 N NE . ARG B 1 128 ? 37.308 1.114 31.203 1.00 26.00 ? 128 ARG B NE 1 ATOM 5339 C CZ . ARG B 1 128 ? 37.883 2.320 31.218 1.00 26.15 ? 128 ARG B CZ 1 ATOM 5340 N NH1 . ARG B 1 128 ? 37.827 3.124 30.162 1.00 26.15 ? 128 ARG B NH1 1 ATOM 5341 N NH2 . ARG B 1 128 ? 38.514 2.735 32.308 1.00 26.83 ? 128 ARG B NH2 1 ATOM 5342 N N . ALA B 1 129 ? 32.447 -0.356 30.975 1.00 20.51 ? 129 ALA B N 1 ATOM 5343 C CA . ALA B 1 129 ? 31.379 -0.037 31.921 1.00 18.61 ? 129 ALA B CA 1 ATOM 5344 C C . ALA B 1 129 ? 31.568 1.392 32.444 1.00 19.64 ? 129 ALA B C 1 ATOM 5345 O O . ALA B 1 129 ? 32.055 1.615 33.561 1.00 21.03 ? 129 ALA B O 1 ATOM 5346 C CB . ALA B 1 129 ? 31.397 -1.035 33.054 1.00 15.67 ? 129 ALA B CB 1 ATOM 5347 N N . ARG B 1 130 ? 31.190 2.356 31.608 1.00 20.04 ? 130 ARG B N 1 ATOM 5348 C CA . ARG B 1 130 ? 31.312 3.787 31.915 1.00 19.97 ? 130 ARG B CA 1 ATOM 5349 C C . ARG B 1 130 ? 30.125 4.319 32.716 1.00 20.38 ? 130 ARG B C 1 ATOM 5350 O O . ARG B 1 130 ? 30.018 5.517 32.997 1.00 18.97 ? 130 ARG B O 1 ATOM 5351 C CB . ARG B 1 130 ? 31.481 4.589 30.614 1.00 19.61 ? 130 ARG B CB 1 ATOM 5352 C CG . ARG B 1 130 ? 32.651 4.125 29.772 1.00 18.22 ? 130 ARG B CG 1 ATOM 5353 C CD . ARG B 1 130 ? 32.974 5.058 28.624 1.00 17.70 ? 130 ARG B CD 1 ATOM 5354 N NE . ARG B 1 130 ? 34.152 4.598 27.885 1.00 18.28 ? 130 ARG B NE 1 ATOM 5355 C CZ . ARG B 1 130 ? 35.409 4.956 28.147 1.00 18.72 ? 130 ARG B CZ 1 ATOM 5356 N NH1 . ARG B 1 130 ? 35.683 5.802 29.136 1.00 19.30 ? 130 ARG B NH1 1 ATOM 5357 N NH2 . ARG B 1 130 ? 36.405 4.423 27.452 1.00 17.86 ? 130 ARG B NH2 1 ATOM 5358 N N . GLN B 1 131 ? 29.236 3.405 33.082 1.00 21.83 ? 131 GLN B N 1 ATOM 5359 C CA . GLN B 1 131 ? 28.055 3.746 33.842 1.00 21.71 ? 131 GLN B CA 1 ATOM 5360 C C . GLN B 1 131 ? 27.828 2.669 34.880 1.00 20.26 ? 131 GLN B C 1 ATOM 5361 O O . GLN B 1 131 ? 28.055 1.490 34.620 1.00 21.90 ? 131 GLN B O 1 ATOM 5362 C CB . GLN B 1 131 ? 26.861 3.853 32.903 1.00 22.29 ? 131 GLN B CB 1 ATOM 5363 C CG . GLN B 1 131 ? 25.831 4.845 33.363 1.00 25.48 ? 131 GLN B CG 1 ATOM 5364 C CD . GLN B 1 131 ? 24.814 5.198 32.297 1.00 30.02 ? 131 GLN B CD 1 ATOM 5365 O OE1 . GLN B 1 131 ? 24.912 4.761 31.144 1.00 31.69 ? 131 GLN B OE1 1 ATOM 5366 N NE2 . GLN B 1 131 ? 23.815 5.990 32.682 1.00 29.12 ? 131 GLN B NE2 1 ATOM 5367 N N . TYR B 1 132 ? 27.422 3.094 36.070 1.00 19.68 ? 132 TYR B N 1 ATOM 5368 C CA . TYR B 1 132 ? 27.150 2.181 37.175 1.00 15.97 ? 132 TYR B CA 1 ATOM 5369 C C . TYR B 1 132 ? 25.661 2.113 37.522 1.00 14.48 ? 132 TYR B C 1 ATOM 5370 O O . TYR B 1 132 ? 24.935 3.114 37.442 1.00 13.00 ? 132 TYR B O 1 ATOM 5371 C CB . TYR B 1 132 ? 27.999 2.538 38.405 1.00 14.63 ? 132 TYR B CB 1 ATOM 5372 C CG . TYR B 1 132 ? 27.859 3.966 38.893 1.00 17.83 ? 132 TYR B CG 1 ATOM 5373 C CD1 . TYR B 1 132 ? 28.584 5.010 38.288 1.00 17.11 ? 132 TYR B CD1 1 ATOM 5374 C CD2 . TYR B 1 132 ? 26.966 4.295 39.937 1.00 18.49 ? 132 TYR B CD2 1 ATOM 5375 C CE1 . TYR B 1 132 ? 28.426 6.358 38.702 1.00 17.32 ? 132 TYR B CE1 1 ATOM 5376 C CE2 . TYR B 1 132 ? 26.796 5.639 40.354 1.00 18.08 ? 132 TYR B CE2 1 ATOM 5377 C CZ . TYR B 1 132 ? 27.528 6.662 39.727 1.00 17.17 ? 132 TYR B CZ 1 ATOM 5378 O OH . TYR B 1 132 ? 27.338 7.970 40.098 1.00 16.28 ? 132 TYR B OH 1 ATOM 5379 N N . GLY B 1 133 ? 25.220 0.926 37.906 1.00 11.55 ? 133 GLY B N 1 ATOM 5380 C CA . GLY B 1 133 ? 23.832 0.750 38.259 1.00 12.70 ? 133 GLY B CA 1 ATOM 5381 C C . GLY B 1 133 ? 23.332 -0.599 37.829 1.00 12.58 ? 133 GLY B C 1 ATOM 5382 O O . GLY B 1 133 ? 24.090 -1.572 37.823 1.00 11.69 ? 133 GLY B O 1 ATOM 5383 N N . THR B 1 134 ? 22.050 -0.645 37.474 1.00 13.73 ? 134 THR B N 1 ATOM 5384 C CA . THR B 1 134 ? 21.405 -1.875 37.034 1.00 14.15 ? 134 THR B CA 1 ATOM 5385 C C . THR B 1 134 ? 20.912 -1.712 35.615 1.00 15.37 ? 134 THR B C 1 ATOM 5386 O O . THR B 1 134 ? 20.302 -0.699 35.263 1.00 17.38 ? 134 THR B O 1 ATOM 5387 C CB . THR B 1 134 ? 20.211 -2.234 37.913 1.00 13.97 ? 134 THR B CB 1 ATOM 5388 O OG1 . THR B 1 134 ? 20.589 -2.113 39.288 1.00 14.92 ? 134 THR B OG1 1 ATOM 5389 C CG2 . THR B 1 134 ? 19.757 -3.667 37.648 1.00 14.99 ? 134 THR B CG2 1 ATOM 5390 N N . SER B 1 135 ? 21.188 -2.731 34.813 1.00 15.76 ? 135 SER B N 1 ATOM 5391 C CA . SER B 1 135 ? 20.777 -2.772 33.423 1.00 17.12 ? 135 SER B CA 1 ATOM 5392 C C . SER B 1 135 ? 20.446 -4.203 33.042 1.00 16.20 ? 135 SER B C 1 ATOM 5393 O O . SER B 1 135 ? 20.430 -5.088 33.903 1.00 17.76 ? 135 SER B O 1 ATOM 5394 C CB . SER B 1 135 ? 21.866 -2.187 32.524 1.00 17.97 ? 135 SER B CB 1 ATOM 5395 O OG . SER B 1 135 ? 21.677 -0.791 32.392 1.00 23.19 ? 135 SER B OG 1 ATOM 5396 N N . TRP B 1 136 ? 20.144 -4.416 31.766 1.00 14.87 ? 136 TRP B N 1 ATOM 5397 C CA . TRP B 1 136 ? 19.805 -5.735 31.267 1.00 12.92 ? 136 TRP B CA 1 ATOM 5398 C C . TRP B 1 136 ? 20.221 -5.950 29.825 1.00 13.64 ? 136 TRP B C 1 ATOM 5399 O O . TRP B 1 136 ? 20.466 -4.997 29.077 1.00 12.58 ? 136 TRP B O 1 ATOM 5400 C CB . TRP B 1 136 ? 18.298 -6.038 31.445 1.00 12.10 ? 136 TRP B CB 1 ATOM 5401 C CG . TRP B 1 136 ? 17.326 -5.218 30.627 1.00 10.88 ? 136 TRP B CG 1 ATOM 5402 C CD1 . TRP B 1 136 ? 17.168 -3.855 30.643 1.00 11.19 ? 136 TRP B CD1 1 ATOM 5403 C CD2 . TRP B 1 136 ? 16.335 -5.723 29.725 1.00 8.44 ? 136 TRP B CD2 1 ATOM 5404 N NE1 . TRP B 1 136 ? 16.132 -3.486 29.816 1.00 11.31 ? 136 TRP B NE1 1 ATOM 5405 C CE2 . TRP B 1 136 ? 15.603 -4.608 29.237 1.00 7.75 ? 136 TRP B CE2 1 ATOM 5406 C CE3 . TRP B 1 136 ? 15.987 -7.015 29.280 1.00 10.89 ? 136 TRP B CE3 1 ATOM 5407 C CZ2 . TRP B 1 136 ? 14.537 -4.742 28.320 1.00 8.24 ? 136 TRP B CZ2 1 ATOM 5408 C CZ3 . TRP B 1 136 ? 14.912 -7.157 28.358 1.00 9.89 ? 136 TRP B CZ3 1 ATOM 5409 C CH2 . TRP B 1 136 ? 14.204 -6.015 27.894 1.00 9.09 ? 136 TRP B CH2 1 ATOM 5410 N N . TYR B 1 137 ? 20.338 -7.222 29.463 1.00 13.38 ? 137 TYR B N 1 ATOM 5411 C CA . TYR B 1 137 ? 20.690 -7.596 28.110 1.00 12.58 ? 137 TYR B CA 1 ATOM 5412 C C . TYR B 1 137 ? 19.636 -8.529 27.559 1.00 10.20 ? 137 TYR B C 1 ATOM 5413 O O . TYR B 1 137 ? 18.969 -9.234 28.314 1.00 8.98 ? 137 TYR B O 1 ATOM 5414 C CB . TYR B 1 137 ? 22.095 -8.220 28.028 1.00 11.23 ? 137 TYR B CB 1 ATOM 5415 C CG . TYR B 1 137 ? 22.314 -9.510 28.787 1.00 11.37 ? 137 TYR B CG 1 ATOM 5416 C CD1 . TYR B 1 137 ? 21.954 -10.758 28.227 1.00 12.48 ? 137 TYR B CD1 1 ATOM 5417 C CD2 . TYR B 1 137 ? 22.906 -9.497 30.067 1.00 12.57 ? 137 TYR B CD2 1 ATOM 5418 C CE1 . TYR B 1 137 ? 22.171 -11.955 28.919 1.00 12.77 ? 137 TYR B CE1 1 ATOM 5419 C CE2 . TYR B 1 137 ? 23.141 -10.691 30.774 1.00 13.43 ? 137 TYR B CE2 1 ATOM 5420 C CZ . TYR B 1 137 ? 22.768 -11.912 30.191 1.00 13.65 ? 137 TYR B CZ 1 ATOM 5421 O OH . TYR B 1 137 ? 22.982 -13.069 30.864 1.00 12.72 ? 137 TYR B OH 1 ATOM 5422 N N . HIS B 1 138 ? 19.539 -8.561 26.236 1.00 8.32 ? 138 HIS B N 1 ATOM 5423 C CA . HIS B 1 138 ? 18.578 -9.399 25.554 1.00 10.50 ? 138 HIS B CA 1 ATOM 5424 C C . HIS B 1 138 ? 18.910 -9.454 24.080 1.00 10.78 ? 138 HIS B C 1 ATOM 5425 O O . HIS B 1 138 ? 19.665 -8.621 23.580 1.00 9.76 ? 138 HIS B O 1 ATOM 5426 C CB . HIS B 1 138 ? 17.156 -8.843 25.749 1.00 12.00 ? 138 HIS B CB 1 ATOM 5427 C CG . HIS B 1 138 ? 16.952 -7.473 25.178 1.00 15.14 ? 138 HIS B CG 1 ATOM 5428 N ND1 . HIS B 1 138 ? 16.544 -7.270 23.877 1.00 16.40 ? 138 HIS B ND1 1 ATOM 5429 C CD2 . HIS B 1 138 ? 17.140 -6.243 25.711 1.00 12.24 ? 138 HIS B CD2 1 ATOM 5430 C CE1 . HIS B 1 138 ? 16.494 -5.975 23.633 1.00 15.91 ? 138 HIS B CE1 1 ATOM 5431 N NE2 . HIS B 1 138 ? 16.850 -5.330 24.730 1.00 14.60 ? 138 HIS B NE2 1 ATOM 5432 N N . SER B 1 139 ? 18.301 -10.408 23.384 1.00 12.88 ? 139 SER B N 1 ATOM 5433 C CA . SER B 1 139 ? 18.480 -10.555 21.941 1.00 15.53 ? 139 SER B CA 1 ATOM 5434 C C . SER B 1 139 ? 17.788 -9.425 21.198 1.00 17.19 ? 139 SER B C 1 ATOM 5435 O O . SER B 1 139 ? 16.824 -8.831 21.706 1.00 14.94 ? 139 SER B O 1 ATOM 5436 C CB . SER B 1 139 ? 17.882 -11.872 21.448 1.00 13.80 ? 139 SER B CB 1 ATOM 5437 O OG . SER B 1 139 ? 17.962 -11.989 20.040 1.00 12.24 ? 139 SER B OG 1 ATOM 5438 N N . HIS B 1 140 ? 18.277 -9.159 19.987 1.00 20.04 ? 140 HIS B N 1 ATOM 5439 C CA . HIS B 1 140 ? 17.690 -8.134 19.140 1.00 21.51 ? 140 HIS B CA 1 ATOM 5440 C C . HIS B 1 140 ? 17.335 -8.708 17.767 1.00 21.03 ? 140 HIS B C 1 ATOM 5441 O O . HIS B 1 140 ? 17.348 -8.005 16.753 1.00 24.22 ? 140 HIS B O 1 ATOM 5442 C CB . HIS B 1 140 ? 18.613 -6.919 19.040 1.00 24.70 ? 140 HIS B CB 1 ATOM 5443 C CG . HIS B 1 140 ? 17.882 -5.615 19.075 1.00 26.87 ? 140 HIS B CG 1 ATOM 5444 N ND1 . HIS B 1 140 ? 17.330 -5.045 17.950 1.00 27.42 ? 140 HIS B ND1 1 ATOM 5445 C CD2 . HIS B 1 140 ? 17.545 -4.810 20.109 1.00 28.35 ? 140 HIS B CD2 1 ATOM 5446 C CE1 . HIS B 1 140 ? 16.676 -3.950 18.292 1.00 29.00 ? 140 HIS B CE1 1 ATOM 5447 N NE2 . HIS B 1 140 ? 16.791 -3.785 19.596 1.00 28.67 ? 140 HIS B NE2 1 ATOM 5448 N N . PHE B 1 141 ? 17.043 -10.007 17.746 1.00 19.81 ? 141 PHE B N 1 ATOM 5449 C CA . PHE B 1 141 ? 16.649 -10.715 16.529 1.00 16.86 ? 141 PHE B CA 1 ATOM 5450 C C . PHE B 1 141 ? 15.122 -10.836 16.610 1.00 15.71 ? 141 PHE B C 1 ATOM 5451 O O . PHE B 1 141 ? 14.592 -11.847 17.078 1.00 14.08 ? 141 PHE B O 1 ATOM 5452 C CB . PHE B 1 141 ? 17.327 -12.091 16.476 1.00 14.53 ? 141 PHE B CB 1 ATOM 5453 C CG . PHE B 1 141 ? 17.168 -12.803 15.155 1.00 12.37 ? 141 PHE B CG 1 ATOM 5454 C CD1 . PHE B 1 141 ? 17.946 -12.432 14.045 1.00 10.16 ? 141 PHE B CD1 1 ATOM 5455 C CD2 . PHE B 1 141 ? 16.258 -13.867 15.021 1.00 9.50 ? 141 PHE B CD2 1 ATOM 5456 C CE1 . PHE B 1 141 ? 17.825 -13.123 12.805 1.00 9.24 ? 141 PHE B CE1 1 ATOM 5457 C CE2 . PHE B 1 141 ? 16.124 -14.558 13.797 1.00 10.29 ? 141 PHE B CE2 1 ATOM 5458 C CZ . PHE B 1 141 ? 16.911 -14.190 12.685 1.00 8.81 ? 141 PHE B CZ 1 ATOM 5459 N N . SER B 1 142 ? 14.437 -9.797 16.118 1.00 15.05 ? 142 SER B N 1 ATOM 5460 C CA . SER B 1 142 ? 12.972 -9.661 16.151 1.00 14.50 ? 142 SER B CA 1 ATOM 5461 C C . SER B 1 142 ? 12.575 -9.685 17.634 1.00 12.58 ? 142 SER B C 1 ATOM 5462 O O . SER B 1 142 ? 13.144 -8.923 18.419 1.00 11.21 ? 142 SER B O 1 ATOM 5463 C CB . SER B 1 142 ? 12.247 -10.748 15.329 1.00 15.74 ? 142 SER B CB 1 ATOM 5464 O OG . SER B 1 142 ? 12.568 -10.648 13.955 1.00 21.65 ? 142 SER B OG 1 ATOM 5465 N N . ALA B 1 143 ? 11.686 -10.603 18.020 1.00 11.03 ? 143 ALA B N 1 ATOM 5466 C CA . ALA B 1 143 ? 11.240 -10.733 19.406 1.00 11.24 ? 143 ALA B CA 1 ATOM 5467 C C . ALA B 1 143 ? 11.788 -12.017 20.028 1.00 11.91 ? 143 ALA B C 1 ATOM 5468 O O . ALA B 1 143 ? 11.187 -12.568 20.942 1.00 12.55 ? 143 ALA B O 1 ATOM 5469 C CB . ALA B 1 143 ? 9.714 -10.707 19.472 1.00 8.68 ? 143 ALA B CB 1 ATOM 5470 N N . GLN B 1 144 ? 12.981 -12.428 19.586 1.00 14.03 ? 144 GLN B N 1 ATOM 5471 C CA . GLN B 1 144 ? 13.654 -13.647 20.052 1.00 14.31 ? 144 GLN B CA 1 ATOM 5472 C C . GLN B 1 144 ? 13.842 -13.719 21.569 1.00 13.65 ? 144 GLN B C 1 ATOM 5473 O O . GLN B 1 144 ? 13.833 -14.811 22.147 1.00 13.86 ? 144 GLN B O 1 ATOM 5474 C CB . GLN B 1 144 ? 15.012 -13.785 19.370 1.00 14.32 ? 144 GLN B CB 1 ATOM 5475 C CG . GLN B 1 144 ? 15.695 -15.112 19.580 1.00 16.85 ? 144 GLN B CG 1 ATOM 5476 C CD . GLN B 1 144 ? 17.109 -15.125 19.084 1.00 17.73 ? 144 GLN B CD 1 ATOM 5477 O OE1 . GLN B 1 144 ? 18.050 -14.849 19.831 1.00 19.12 ? 144 GLN B OE1 1 ATOM 5478 N NE2 . GLN B 1 144 ? 17.275 -15.447 17.816 1.00 18.20 ? 144 GLN B NE2 1 ATOM 5479 N N . TYR B 1 145 ? 13.956 -12.554 22.209 1.00 12.82 ? 145 TYR B N 1 ATOM 5480 C CA . TYR B 1 145 ? 14.141 -12.494 23.652 1.00 11.21 ? 145 TYR B CA 1 ATOM 5481 C C . TYR B 1 145 ? 12.898 -12.892 24.448 1.00 12.42 ? 145 TYR B C 1 ATOM 5482 O O . TYR B 1 145 ? 12.955 -13.019 25.674 1.00 14.49 ? 145 TYR B O 1 ATOM 5483 C CB . TYR B 1 145 ? 14.730 -11.144 24.078 1.00 9.16 ? 145 TYR B CB 1 ATOM 5484 C CG . TYR B 1 145 ? 13.780 -9.998 24.349 1.00 7.55 ? 145 TYR B CG 1 ATOM 5485 C CD1 . TYR B 1 145 ? 13.306 -9.748 25.662 1.00 4.88 ? 145 TYR B CD1 1 ATOM 5486 C CD2 . TYR B 1 145 ? 13.390 -9.125 23.317 1.00 4.72 ? 145 TYR B CD2 1 ATOM 5487 C CE1 . TYR B 1 145 ? 12.457 -8.647 25.938 1.00 6.42 ? 145 TYR B CE1 1 ATOM 5488 C CE2 . TYR B 1 145 ? 12.544 -8.014 23.582 1.00 6.64 ? 145 TYR B CE2 1 ATOM 5489 C CZ . TYR B 1 145 ? 12.086 -7.786 24.895 1.00 5.33 ? 145 TYR B CZ 1 ATOM 5490 O OH . TYR B 1 145 ? 11.281 -6.708 25.164 1.00 6.23 ? 145 TYR B OH 1 ATOM 5491 N N . GLY B 1 146 ? 11.790 -13.092 23.730 1.00 11.38 ? 146 GLY B N 1 ATOM 5492 C CA . GLY B 1 146 ? 10.542 -13.527 24.337 1.00 12.03 ? 146 GLY B CA 1 ATOM 5493 C C . GLY B 1 146 ? 10.507 -15.034 24.520 1.00 12.15 ? 146 GLY B C 1 ATOM 5494 O O . GLY B 1 146 ? 9.597 -15.572 25.152 1.00 11.93 ? 146 GLY B O 1 ATOM 5495 N N . ASN B 1 147 ? 11.502 -15.711 23.948 1.00 14.16 ? 147 ASN B N 1 ATOM 5496 C CA . ASN B 1 147 ? 11.631 -17.166 24.047 1.00 17.22 ? 147 ASN B CA 1 ATOM 5497 C C . ASN B 1 147 ? 12.522 -17.515 25.237 1.00 17.36 ? 147 ASN B C 1 ATOM 5498 O O . ASN B 1 147 ? 12.450 -18.622 25.762 1.00 16.59 ? 147 ASN B O 1 ATOM 5499 C CB . ASN B 1 147 ? 12.199 -17.762 22.750 1.00 15.95 ? 147 ASN B CB 1 ATOM 5500 C CG . ASN B 1 147 ? 11.242 -17.632 21.563 1.00 18.68 ? 147 ASN B CG 1 ATOM 5501 O OD1 . ASN B 1 147 ? 10.017 -17.608 21.727 1.00 18.07 ? 147 ASN B OD1 1 ATOM 5502 N ND2 . ASN B 1 147 ? 11.803 -17.559 20.358 1.00 18.15 ? 147 ASN B ND2 1 ATOM 5503 N N . GLY B 1 148 ? 13.343 -16.549 25.656 1.00 18.42 ? 148 GLY B N 1 ATOM 5504 C CA . GLY B 1 148 ? 14.217 -16.739 26.800 1.00 18.93 ? 148 GLY B CA 1 ATOM 5505 C C . GLY B 1 148 ? 15.617 -16.148 26.733 1.00 19.95 ? 148 GLY B C 1 ATOM 5506 O O . GLY B 1 148 ? 16.350 -16.263 27.715 1.00 21.57 ? 148 GLY B O 1 ATOM 5507 N N . VAL B 1 149 ? 16.009 -15.547 25.602 1.00 19.74 ? 149 VAL B N 1 ATOM 5508 C CA . VAL B 1 149 ? 17.350 -14.951 25.452 1.00 18.14 ? 149 VAL B CA 1 ATOM 5509 C C . VAL B 1 149 ? 17.385 -13.587 26.171 1.00 18.98 ? 149 VAL B C 1 ATOM 5510 O O . VAL B 1 149 ? 17.382 -12.519 25.545 1.00 19.75 ? 149 VAL B O 1 ATOM 5511 C CB . VAL B 1 149 ? 17.774 -14.790 23.948 1.00 18.26 ? 149 VAL B CB 1 ATOM 5512 C CG1 . VAL B 1 149 ? 19.266 -14.525 23.831 1.00 18.47 ? 149 VAL B CG1 1 ATOM 5513 C CG2 . VAL B 1 149 ? 17.443 -16.007 23.142 1.00 19.36 ? 149 VAL B CG2 1 ATOM 5514 N N . VAL B 1 150 ? 17.443 -13.648 27.498 1.00 18.59 ? 150 VAL B N 1 ATOM 5515 C CA . VAL B 1 150 ? 17.439 -12.455 28.340 1.00 17.63 ? 150 VAL B CA 1 ATOM 5516 C C . VAL B 1 150 ? 18.272 -12.656 29.609 1.00 15.68 ? 150 VAL B C 1 ATOM 5517 O O . VAL B 1 150 ? 18.485 -13.783 30.046 1.00 14.94 ? 150 VAL B O 1 ATOM 5518 C CB . VAL B 1 150 ? 15.948 -12.053 28.692 1.00 18.89 ? 150 VAL B CB 1 ATOM 5519 C CG1 . VAL B 1 150 ? 15.227 -13.181 29.435 1.00 20.61 ? 150 VAL B CG1 1 ATOM 5520 C CG2 . VAL B 1 150 ? 15.889 -10.759 29.483 1.00 19.04 ? 150 VAL B CG2 1 ATOM 5521 N N . GLY B 1 151 ? 18.722 -11.547 30.190 1.00 14.79 ? 151 GLY B N 1 ATOM 5522 C CA . GLY B 1 151 ? 19.496 -11.584 31.412 1.00 12.39 ? 151 GLY B CA 1 ATOM 5523 C C . GLY B 1 151 ? 19.708 -10.203 31.989 1.00 11.80 ? 151 GLY B C 1 ATOM 5524 O O . GLY B 1 151 ? 19.255 -9.224 31.412 1.00 11.05 ? 151 GLY B O 1 ATOM 5525 N N . THR B 1 152 ? 20.423 -10.136 33.116 1.00 11.16 ? 152 THR B N 1 ATOM 5526 C CA . THR B 1 152 ? 20.686 -8.884 33.824 1.00 9.22 ? 152 THR B CA 1 ATOM 5527 C C . THR B 1 152 ? 22.167 -8.456 33.894 1.00 9.66 ? 152 THR B C 1 ATOM 5528 O O . THR B 1 152 ? 23.079 -9.280 33.747 1.00 8.39 ? 152 THR B O 1 ATOM 5529 C CB . THR B 1 152 ? 20.097 -8.920 35.275 1.00 9.93 ? 152 THR B CB 1 ATOM 5530 O OG1 . THR B 1 152 ? 20.911 -9.744 36.117 1.00 8.37 ? 152 THR B OG1 1 ATOM 5531 C CG2 . THR B 1 152 ? 18.658 -9.473 35.296 1.00 8.25 ? 152 THR B CG2 1 ATOM 5532 N N . ILE B 1 153 ? 22.376 -7.145 34.047 1.00 8.65 ? 153 ILE B N 1 ATOM 5533 C CA . ILE B 1 153 ? 23.708 -6.525 34.165 1.00 10.98 ? 153 ILE B CA 1 ATOM 5534 C C . ILE B 1 153 ? 23.749 -5.680 35.453 1.00 9.82 ? 153 ILE B C 1 ATOM 5535 O O . ILE B 1 153 ? 22.919 -4.794 35.651 1.00 11.50 ? 153 ILE B O 1 ATOM 5536 C CB . ILE B 1 153 ? 24.045 -5.569 32.956 1.00 11.33 ? 153 ILE B CB 1 ATOM 5537 C CG1 . ILE B 1 153 ? 23.997 -6.309 31.616 1.00 13.60 ? 153 ILE B CG1 1 ATOM 5538 C CG2 . ILE B 1 153 ? 25.435 -4.960 33.129 1.00 15.94 ? 153 ILE B CG2 1 ATOM 5539 C CD1 . ILE B 1 153 ? 23.991 -5.404 30.391 1.00 12.42 ? 153 ILE B CD1 1 ATOM 5540 N N . GLN B 1 154 ? 24.703 -5.970 36.325 1.00 10.83 ? 154 GLN B N 1 ATOM 5541 C CA . GLN B 1 154 ? 24.871 -5.215 37.562 1.00 11.13 ? 154 GLN B CA 1 ATOM 5542 C C . GLN B 1 154 ? 26.296 -4.635 37.625 1.00 10.41 ? 154 GLN B C 1 ATOM 5543 O O . GLN B 1 154 ? 27.270 -5.355 37.871 1.00 9.96 ? 154 GLN B O 1 ATOM 5544 C CB . GLN B 1 154 ? 24.570 -6.092 38.789 1.00 12.37 ? 154 GLN B CB 1 ATOM 5545 C CG . GLN B 1 154 ? 24.800 -5.390 40.149 1.00 14.85 ? 154 GLN B CG 1 ATOM 5546 C CD . GLN B 1 154 ? 24.336 -6.192 41.356 1.00 19.01 ? 154 GLN B CD 1 ATOM 5547 O OE1 . GLN B 1 154 ? 23.738 -7.257 41.226 1.00 20.41 ? 154 GLN B OE1 1 ATOM 5548 N NE2 . GLN B 1 154 ? 24.592 -5.658 42.546 1.00 20.31 ? 154 GLN B NE2 1 ATOM 5549 N N . ILE B 1 155 ? 26.415 -3.346 37.332 1.00 10.92 ? 155 ILE B N 1 ATOM 5550 C CA . ILE B 1 155 ? 27.708 -2.667 37.395 1.00 12.70 ? 155 ILE B CA 1 ATOM 5551 C C . ILE B 1 155 ? 27.721 -1.925 38.732 1.00 14.28 ? 155 ILE B C 1 ATOM 5552 O O . ILE B 1 155 ? 26.965 -0.966 38.931 1.00 13.09 ? 155 ILE B O 1 ATOM 5553 C CB . ILE B 1 155 ? 27.942 -1.674 36.214 1.00 11.51 ? 155 ILE B CB 1 ATOM 5554 C CG1 . ILE B 1 155 ? 27.777 -2.353 34.836 1.00 12.45 ? 155 ILE B CG1 1 ATOM 5555 C CG2 . ILE B 1 155 ? 29.320 -1.035 36.340 1.00 13.01 ? 155 ILE B CG2 1 ATOM 5556 C CD1 . ILE B 1 155 ? 28.778 -3.466 34.493 1.00 12.51 ? 155 ILE B CD1 1 ATOM 5557 N N . ASN B 1 156 ? 28.544 -2.423 39.659 1.00 16.67 ? 156 ASN B N 1 ATOM 5558 C CA . ASN B 1 156 ? 28.673 -1.842 40.998 1.00 18.31 ? 156 ASN B CA 1 ATOM 5559 C C . ASN B 1 156 ? 29.352 -0.489 40.982 1.00 19.07 ? 156 ASN B C 1 ATOM 5560 O O . ASN B 1 156 ? 30.283 -0.256 40.211 1.00 19.92 ? 156 ASN B O 1 ATOM 5561 C CB . ASN B 1 156 ? 29.416 -2.784 41.952 1.00 16.16 ? 156 ASN B CB 1 ATOM 5562 C CG . ASN B 1 156 ? 28.560 -3.953 42.417 1.00 14.80 ? 156 ASN B CG 1 ATOM 5563 O OD1 . ASN B 1 156 ? 27.357 -3.812 42.652 1.00 12.96 ? 156 ASN B OD1 1 ATOM 5564 N ND2 . ASN B 1 156 ? 29.185 -5.116 42.562 1.00 13.46 ? 156 ASN B ND2 1 ATOM 5565 N N . GLY B 1 157 ? 28.826 0.406 41.809 1.00 20.64 ? 157 GLY B N 1 ATOM 5566 C CA . GLY B 1 157 ? 29.351 1.752 41.915 1.00 20.97 ? 157 GLY B CA 1 ATOM 5567 C C . GLY B 1 157 ? 28.766 2.440 43.131 1.00 21.07 ? 157 GLY B C 1 ATOM 5568 O O . GLY B 1 157 ? 28.162 1.767 43.974 1.00 22.29 ? 157 GLY B O 1 ATOM 5569 N N . PRO B 1 158 ? 28.954 3.765 43.284 1.00 20.28 ? 158 PRO B N 1 ATOM 5570 C CA . PRO B 1 158 ? 28.409 4.489 44.436 1.00 20.14 ? 158 PRO B CA 1 ATOM 5571 C C . PRO B 1 158 ? 26.882 4.671 44.380 1.00 20.01 ? 158 PRO B C 1 ATOM 5572 O O . PRO B 1 158 ? 26.246 4.312 43.378 1.00 18.82 ? 158 PRO B O 1 ATOM 5573 C CB . PRO B 1 158 ? 29.165 5.816 44.387 1.00 20.76 ? 158 PRO B CB 1 ATOM 5574 C CG . PRO B 1 158 ? 29.424 6.002 42.941 1.00 18.47 ? 158 PRO B CG 1 ATOM 5575 C CD . PRO B 1 158 ? 29.824 4.644 42.484 1.00 18.24 ? 158 PRO B CD 1 ATOM 5576 N N . ALA B 1 159 ? 26.308 5.184 45.470 1.00 19.20 ? 159 ALA B N 1 ATOM 5577 C CA . ALA B 1 159 ? 24.864 5.403 45.560 1.00 20.08 ? 159 ALA B CA 1 ATOM 5578 C C . ALA B 1 159 ? 24.497 6.744 46.173 1.00 18.95 ? 159 ALA B C 1 ATOM 5579 O O . ALA B 1 159 ? 25.342 7.431 46.741 1.00 19.60 ? 159 ALA B O 1 ATOM 5580 C CB . ALA B 1 159 ? 24.195 4.275 46.329 1.00 21.81 ? 159 ALA B CB 1 ATOM 5581 N N . SER B 1 160 ? 23.229 7.116 46.022 1.00 17.91 ? 160 SER B N 1 ATOM 5582 C CA . SER B 1 160 ? 22.716 8.375 46.536 1.00 18.13 ? 160 SER B CA 1 ATOM 5583 C C . SER B 1 160 ? 22.067 8.257 47.915 1.00 18.76 ? 160 SER B C 1 ATOM 5584 O O . SER B 1 160 ? 21.468 9.217 48.400 1.00 18.32 ? 160 SER B O 1 ATOM 5585 C CB . SER B 1 160 ? 21.730 8.971 45.535 1.00 17.95 ? 160 SER B CB 1 ATOM 5586 O OG . SER B 1 160 ? 20.654 8.085 45.284 1.00 19.66 ? 160 SER B OG 1 ATOM 5587 N N . LEU B 1 161 ? 22.185 7.082 48.535 1.00 19.84 ? 161 LEU B N 1 ATOM 5588 C CA . LEU B 1 161 ? 21.616 6.835 49.858 1.00 22.10 ? 161 LEU B CA 1 ATOM 5589 C C . LEU B 1 161 ? 22.340 5.672 50.525 1.00 22.65 ? 161 LEU B C 1 ATOM 5590 O O . LEU B 1 161 ? 22.774 4.750 49.830 1.00 23.28 ? 161 LEU B O 1 ATOM 5591 C CB . LEU B 1 161 ? 20.123 6.489 49.747 1.00 21.55 ? 161 LEU B CB 1 ATOM 5592 C CG . LEU B 1 161 ? 19.191 6.688 50.945 1.00 22.09 ? 161 LEU B CG 1 ATOM 5593 C CD1 . LEU B 1 161 ? 18.969 8.181 51.210 1.00 22.42 ? 161 LEU B CD1 1 ATOM 5594 C CD2 . LEU B 1 161 ? 17.885 6.009 50.682 1.00 22.73 ? 161 LEU B CD2 1 ATOM 5595 N N . PRO B 1 162 ? 22.549 5.735 51.866 1.00 22.94 ? 162 PRO B N 1 ATOM 5596 C CA . PRO B 1 162 ? 23.226 4.641 52.573 1.00 23.28 ? 162 PRO B CA 1 ATOM 5597 C C . PRO B 1 162 ? 22.352 3.375 52.704 1.00 23.02 ? 162 PRO B C 1 ATOM 5598 O O . PRO B 1 162 ? 21.142 3.461 52.958 1.00 22.86 ? 162 PRO B O 1 ATOM 5599 C CB . PRO B 1 162 ? 23.508 5.253 53.947 1.00 24.17 ? 162 PRO B CB 1 ATOM 5600 C CG . PRO B 1 162 ? 23.656 6.690 53.663 1.00 24.23 ? 162 PRO B CG 1 ATOM 5601 C CD . PRO B 1 162 ? 22.512 6.933 52.735 1.00 23.40 ? 162 PRO B CD 1 ATOM 5602 N N . TYR B 1 163 ? 22.973 2.217 52.478 1.00 21.78 ? 163 TYR B N 1 ATOM 5603 C CA . TYR B 1 163 ? 22.306 0.921 52.582 1.00 22.06 ? 163 TYR B CA 1 ATOM 5604 C C . TYR B 1 163 ? 23.290 -0.128 53.082 1.00 21.85 ? 163 TYR B C 1 ATOM 5605 O O . TYR B 1 163 ? 24.485 -0.018 52.817 1.00 21.44 ? 163 TYR B O 1 ATOM 5606 C CB . TYR B 1 163 ? 21.653 0.492 51.242 1.00 21.59 ? 163 TYR B CB 1 ATOM 5607 C CG . TYR B 1 163 ? 22.582 0.325 50.049 1.00 19.85 ? 163 TYR B CG 1 ATOM 5608 C CD1 . TYR B 1 163 ? 23.233 -0.908 49.799 1.00 22.02 ? 163 TYR B CD1 1 ATOM 5609 C CD2 . TYR B 1 163 ? 22.808 1.383 49.158 1.00 17.68 ? 163 TYR B CD2 1 ATOM 5610 C CE1 . TYR B 1 163 ? 24.099 -1.080 48.683 1.00 20.48 ? 163 TYR B CE1 1 ATOM 5611 C CE2 . TYR B 1 163 ? 23.669 1.224 48.035 1.00 19.11 ? 163 TYR B CE2 1 ATOM 5612 C CZ . TYR B 1 163 ? 24.311 -0.007 47.808 1.00 20.75 ? 163 TYR B CZ 1 ATOM 5613 O OH . TYR B 1 163 ? 25.163 -0.168 46.732 1.00 19.94 ? 163 TYR B OH 1 ATOM 5614 N N . ASP B 1 164 ? 22.775 -1.178 53.722 1.00 21.53 ? 164 ASP B N 1 ATOM 5615 C CA . ASP B 1 164 ? 23.622 -2.243 54.266 1.00 21.75 ? 164 ASP B CA 1 ATOM 5616 C C . ASP B 1 164 ? 23.796 -3.438 53.343 1.00 21.95 ? 164 ASP B C 1 ATOM 5617 O O . ASP B 1 164 ? 24.924 -3.853 53.068 1.00 20.80 ? 164 ASP B O 1 ATOM 5618 C CB . ASP B 1 164 ? 23.090 -2.721 55.621 1.00 21.61 ? 164 ASP B CB 1 ATOM 5619 C CG . ASP B 1 164 ? 22.777 -1.582 56.552 1.00 21.64 ? 164 ASP B CG 1 ATOM 5620 O OD1 . ASP B 1 164 ? 23.725 -0.883 56.970 1.00 22.57 ? 164 ASP B OD1 1 ATOM 5621 O OD2 . ASP B 1 164 ? 21.578 -1.380 56.843 1.00 18.25 ? 164 ASP B OD2 1 ATOM 5622 N N . ILE B 1 165 ? 22.671 -4.019 52.924 1.00 22.20 ? 165 ILE B N 1 ATOM 5623 C CA . ILE B 1 165 ? 22.656 -5.182 52.042 1.00 21.91 ? 165 ILE B CA 1 ATOM 5624 C C . ILE B 1 165 ? 22.137 -4.828 50.645 1.00 21.40 ? 165 ILE B C 1 ATOM 5625 O O . ILE B 1 165 ? 21.210 -4.027 50.483 1.00 20.61 ? 165 ILE B O 1 ATOM 5626 C CB . ILE B 1 165 ? 21.799 -6.349 52.658 1.00 22.64 ? 165 ILE B CB 1 ATOM 5627 C CG1 . ILE B 1 165 ? 22.426 -6.843 53.962 1.00 24.40 ? 165 ILE B CG1 1 ATOM 5628 C CG2 . ILE B 1 165 ? 21.693 -7.559 51.713 1.00 23.01 ? 165 ILE B CG2 1 ATOM 5629 C CD1 . ILE B 1 165 ? 21.708 -6.378 55.184 1.00 25.07 ? 165 ILE B CD1 1 ATOM 5630 N N . ASP B 1 166 ? 22.782 -5.418 49.644 1.00 20.46 ? 166 ASP B N 1 ATOM 5631 C CA . ASP B 1 166 ? 22.409 -5.255 48.250 1.00 19.99 ? 166 ASP B CA 1 ATOM 5632 C C . ASP B 1 166 ? 21.839 -6.633 47.886 1.00 19.93 ? 166 ASP B C 1 ATOM 5633 O O . ASP B 1 166 ? 22.584 -7.609 47.761 1.00 21.37 ? 166 ASP B O 1 ATOM 5634 C CB . ASP B 1 166 ? 23.650 -4.922 47.404 1.00 19.60 ? 166 ASP B CB 1 ATOM 5635 C CG . ASP B 1 166 ? 23.310 -4.440 45.988 1.00 21.16 ? 166 ASP B CG 1 ATOM 5636 O OD1 . ASP B 1 166 ? 22.171 -4.631 45.504 1.00 18.75 ? 166 ASP B OD1 1 ATOM 5637 O OD2 . ASP B 1 166 ? 24.211 -3.858 45.350 1.00 22.01 ? 166 ASP B OD2 1 ATOM 5638 N N . LEU B 1 167 ? 20.513 -6.711 47.766 1.00 17.97 ? 167 LEU B N 1 ATOM 5639 C CA . LEU B 1 167 ? 19.819 -7.951 47.418 1.00 17.95 ? 167 LEU B CA 1 ATOM 5640 C C . LEU B 1 167 ? 20.033 -8.357 45.952 1.00 18.03 ? 167 LEU B C 1 ATOM 5641 O O . LEU B 1 167 ? 19.628 -9.447 45.529 1.00 19.45 ? 167 LEU B O 1 ATOM 5642 C CB . LEU B 1 167 ? 18.325 -7.819 47.722 1.00 18.11 ? 167 LEU B CB 1 ATOM 5643 C CG . LEU B 1 167 ? 17.911 -7.522 49.169 1.00 19.75 ? 167 LEU B CG 1 ATOM 5644 C CD1 . LEU B 1 167 ? 16.464 -7.082 49.194 1.00 19.04 ? 167 LEU B CD1 1 ATOM 5645 C CD2 . LEU B 1 167 ? 18.132 -8.734 50.086 1.00 21.15 ? 167 LEU B CD2 1 ATOM 5646 N N . GLY B 1 168 ? 20.681 -7.473 45.193 1.00 16.82 ? 168 GLY B N 1 ATOM 5647 C CA . GLY B 1 168 ? 20.972 -7.733 43.795 1.00 15.86 ? 168 GLY B CA 1 ATOM 5648 C C . GLY B 1 168 ? 19.811 -7.540 42.844 1.00 15.68 ? 168 GLY B C 1 ATOM 5649 O O . GLY B 1 168 ? 18.855 -6.802 43.128 1.00 14.86 ? 168 GLY B O 1 ATOM 5650 N N . VAL B 1 169 ? 19.873 -8.262 41.733 1.00 14.57 ? 169 VAL B N 1 ATOM 5651 C CA . VAL B 1 169 ? 18.854 -8.179 40.685 1.00 14.22 ? 169 VAL B CA 1 ATOM 5652 C C . VAL B 1 169 ? 17.502 -8.819 41.007 1.00 13.61 ? 169 VAL B C 1 ATOM 5653 O O . VAL B 1 169 ? 17.440 -9.867 41.648 1.00 15.28 ? 169 VAL B O 1 ATOM 5654 C CB . VAL B 1 169 ? 19.414 -8.688 39.329 1.00 11.17 ? 169 VAL B CB 1 ATOM 5655 C CG1 . VAL B 1 169 ? 20.608 -7.838 38.929 1.00 10.01 ? 169 VAL B CG1 1 ATOM 5656 C CG2 . VAL B 1 169 ? 19.815 -10.151 39.401 1.00 6.63 ? 169 VAL B CG2 1 ATOM 5657 N N . PHE B 1 170 ? 16.432 -8.165 40.552 1.00 14.89 ? 170 PHE B N 1 ATOM 5658 C CA . PHE B 1 170 ? 15.056 -8.621 40.764 1.00 15.55 ? 170 PHE B CA 1 ATOM 5659 C C . PHE B 1 170 ? 14.216 -8.398 39.487 1.00 16.54 ? 170 PHE B C 1 ATOM 5660 O O . PHE B 1 170 ? 13.308 -7.548 39.468 1.00 17.55 ? 170 PHE B O 1 ATOM 5661 C CB . PHE B 1 170 ? 14.462 -7.843 41.940 1.00 16.76 ? 170 PHE B CB 1 ATOM 5662 C CG . PHE B 1 170 ? 13.324 -8.534 42.634 1.00 17.72 ? 170 PHE B CG 1 ATOM 5663 C CD1 . PHE B 1 170 ? 13.433 -9.880 43.041 1.00 18.24 ? 170 PHE B CD1 1 ATOM 5664 C CD2 . PHE B 1 170 ? 12.167 -7.810 42.970 1.00 16.84 ? 170 PHE B CD2 1 ATOM 5665 C CE1 . PHE B 1 170 ? 12.406 -10.498 43.785 1.00 17.67 ? 170 PHE B CE1 1 ATOM 5666 C CE2 . PHE B 1 170 ? 11.128 -8.410 43.718 1.00 18.39 ? 170 PHE B CE2 1 ATOM 5667 C CZ . PHE B 1 170 ? 11.248 -9.758 44.129 1.00 18.74 ? 170 PHE B CZ 1 ATOM 5668 N N . PRO B 1 171 ? 14.467 -9.195 38.419 1.00 15.89 ? 171 PRO B N 1 ATOM 5669 C CA . PRO B 1 171 ? 13.714 -9.036 37.168 1.00 17.08 ? 171 PRO B CA 1 ATOM 5670 C C . PRO B 1 171 ? 12.261 -9.509 37.193 1.00 18.31 ? 171 PRO B C 1 ATOM 5671 O O . PRO B 1 171 ? 11.957 -10.606 37.664 1.00 21.31 ? 171 PRO B O 1 ATOM 5672 C CB . PRO B 1 171 ? 14.554 -9.819 36.169 1.00 15.57 ? 171 PRO B CB 1 ATOM 5673 C CG . PRO B 1 171 ? 15.080 -10.942 36.989 1.00 15.70 ? 171 PRO B CG 1 ATOM 5674 C CD . PRO B 1 171 ? 15.442 -10.301 38.299 1.00 15.99 ? 171 PRO B CD 1 ATOM 5675 N N . ILE B 1 172 ? 11.363 -8.626 36.767 1.00 17.80 ? 172 ILE B N 1 ATOM 5676 C CA . ILE B 1 172 ? 9.943 -8.941 36.701 1.00 17.56 ? 172 ILE B CA 1 ATOM 5677 C C . ILE B 1 172 ? 9.597 -8.935 35.212 1.00 17.31 ? 172 ILE B C 1 ATOM 5678 O O . ILE B 1 172 ? 9.789 -7.926 34.531 1.00 19.07 ? 172 ILE B O 1 ATOM 5679 C CB . ILE B 1 172 ? 9.077 -7.932 37.526 1.00 16.89 ? 172 ILE B CB 1 ATOM 5680 C CG1 . ILE B 1 172 ? 9.561 -7.891 38.988 1.00 17.36 ? 172 ILE B CG1 1 ATOM 5681 C CG2 . ILE B 1 172 ? 7.623 -8.386 37.540 1.00 17.06 ? 172 ILE B CG2 1 ATOM 5682 C CD1 . ILE B 1 172 ? 8.838 -6.916 39.880 1.00 15.67 ? 172 ILE B CD1 1 ATOM 5683 N N . THR B 1 173 ? 9.139 -10.080 34.706 1.00 17.39 ? 173 THR B N 1 ATOM 5684 C CA . THR B 1 173 ? 8.796 -10.223 33.285 1.00 16.55 ? 173 THR B CA 1 ATOM 5685 C C . THR B 1 173 ? 7.458 -10.900 33.002 1.00 15.77 ? 173 THR B C 1 ATOM 5686 O O . THR B 1 173 ? 6.942 -11.641 33.836 1.00 13.82 ? 173 THR B O 1 ATOM 5687 C CB . THR B 1 173 ? 9.914 -11.016 32.510 1.00 15.72 ? 173 THR B CB 1 ATOM 5688 O OG1 . THR B 1 173 ? 9.629 -11.034 31.102 1.00 15.35 ? 173 THR B OG1 1 ATOM 5689 C CG2 . THR B 1 173 ? 10.059 -12.448 33.021 1.00 14.60 ? 173 THR B CG2 1 ATOM 5690 N N . ASP B 1 174 ? 6.912 -10.645 31.809 1.00 15.07 ? 174 ASP B N 1 ATOM 5691 C CA . ASP B 1 174 ? 5.688 -11.317 31.391 1.00 14.87 ? 174 ASP B CA 1 ATOM 5692 C C . ASP B 1 174 ? 6.096 -12.697 30.874 1.00 14.95 ? 174 ASP B C 1 ATOM 5693 O O . ASP B 1 174 ? 7.250 -12.895 30.459 1.00 13.35 ? 174 ASP B O 1 ATOM 5694 C CB . ASP B 1 174 ? 4.872 -10.534 30.346 1.00 13.66 ? 174 ASP B CB 1 ATOM 5695 C CG . ASP B 1 174 ? 5.705 -9.938 29.195 1.00 12.65 ? 174 ASP B CG 1 ATOM 5696 O OD1 . ASP B 1 174 ? 6.823 -10.413 28.872 1.00 4.74 ? 174 ASP B OD1 1 ATOM 5697 O OD2 . ASP B 1 174 ? 5.190 -8.968 28.594 1.00 7.90 ? 174 ASP B OD2 1 ATOM 5698 N N . TYR B 1 175 ? 5.168 -13.644 30.951 1.00 15.08 ? 175 TYR B N 1 ATOM 5699 C CA . TYR B 1 175 ? 5.425 -15.016 30.538 1.00 15.30 ? 175 TYR B CA 1 ATOM 5700 C C . TYR B 1 175 ? 4.266 -15.534 29.718 1.00 14.75 ? 175 TYR B C 1 ATOM 5701 O O . TYR B 1 175 ? 3.116 -15.484 30.158 1.00 17.15 ? 175 TYR B O 1 ATOM 5702 C CB . TYR B 1 175 ? 5.632 -15.880 31.785 1.00 15.67 ? 175 TYR B CB 1 ATOM 5703 C CG . TYR B 1 175 ? 6.186 -17.268 31.556 1.00 16.55 ? 175 TYR B CG 1 ATOM 5704 C CD1 . TYR B 1 175 ? 7.454 -17.461 30.968 1.00 15.83 ? 175 TYR B CD1 1 ATOM 5705 C CD2 . TYR B 1 175 ? 5.469 -18.404 31.994 1.00 17.48 ? 175 TYR B CD2 1 ATOM 5706 C CE1 . TYR B 1 175 ? 8.002 -18.767 30.828 1.00 19.02 ? 175 TYR B CE1 1 ATOM 5707 C CE2 . TYR B 1 175 ? 6.003 -19.709 31.858 1.00 17.28 ? 175 TYR B CE2 1 ATOM 5708 C CZ . TYR B 1 175 ? 7.261 -19.879 31.278 1.00 18.94 ? 175 TYR B CZ 1 ATOM 5709 O OH . TYR B 1 175 ? 7.764 -21.148 31.142 1.00 22.89 ? 175 TYR B OH 1 ATOM 5710 N N . TYR B 1 176 ? 4.595 -16.009 28.516 1.00 15.24 ? 176 TYR B N 1 ATOM 5711 C CA . TYR B 1 176 ? 3.627 -16.551 27.561 1.00 14.68 ? 176 TYR B CA 1 ATOM 5712 C C . TYR B 1 176 ? 3.984 -17.983 27.218 1.00 15.96 ? 176 TYR B C 1 ATOM 5713 O O . TYR B 1 176 ? 5.153 -18.283 26.989 1.00 17.60 ? 176 TYR B O 1 ATOM 5714 C CB . TYR B 1 176 ? 3.632 -15.758 26.253 1.00 12.92 ? 176 TYR B CB 1 ATOM 5715 C CG . TYR B 1 176 ? 3.398 -14.282 26.400 1.00 12.98 ? 176 TYR B CG 1 ATOM 5716 C CD1 . TYR B 1 176 ? 4.473 -13.408 26.669 1.00 11.15 ? 176 TYR B CD1 1 ATOM 5717 C CD2 . TYR B 1 176 ? 2.099 -13.739 26.296 1.00 10.47 ? 176 TYR B CD2 1 ATOM 5718 C CE1 . TYR B 1 176 ? 4.257 -12.024 26.842 1.00 13.07 ? 176 TYR B CE1 1 ATOM 5719 C CE2 . TYR B 1 176 ? 1.877 -12.348 26.461 1.00 11.02 ? 176 TYR B CE2 1 ATOM 5720 C CZ . TYR B 1 176 ? 2.959 -11.505 26.739 1.00 10.54 ? 176 TYR B CZ 1 ATOM 5721 O OH . TYR B 1 176 ? 2.756 -10.166 26.932 1.00 14.90 ? 176 TYR B OH 1 ATOM 5722 N N . TYR B 1 177 ? 2.970 -18.841 27.106 1.00 15.94 ? 177 TYR B N 1 ATOM 5723 C CA . TYR B 1 177 ? 3.183 -20.244 26.768 1.00 15.82 ? 177 TYR B CA 1 ATOM 5724 C C . TYR B 1 177 ? 3.509 -20.389 25.280 1.00 16.54 ? 177 TYR B C 1 ATOM 5725 O O . TYR B 1 177 ? 4.315 -21.241 24.897 1.00 15.89 ? 177 TYR B O 1 ATOM 5726 C CB . TYR B 1 177 ? 1.977 -21.096 27.175 1.00 18.08 ? 177 TYR B CB 1 ATOM 5727 C CG . TYR B 1 177 ? 1.616 -21.044 28.661 1.00 20.21 ? 177 TYR B CG 1 ATOM 5728 C CD1 . TYR B 1 177 ? 2.585 -20.736 29.652 1.00 21.13 ? 177 TYR B CD1 1 ATOM 5729 C CD2 . TYR B 1 177 ? 0.290 -21.276 29.083 1.00 21.83 ? 177 TYR B CD2 1 ATOM 5730 C CE1 . TYR B 1 177 ? 2.237 -20.651 31.035 1.00 21.43 ? 177 TYR B CE1 1 ATOM 5731 C CE2 . TYR B 1 177 ? -0.075 -21.197 30.472 1.00 22.10 ? 177 TYR B CE2 1 ATOM 5732 C CZ . TYR B 1 177 ? 0.904 -20.880 31.433 1.00 21.44 ? 177 TYR B CZ 1 ATOM 5733 O OH . TYR B 1 177 ? 0.554 -20.761 32.763 1.00 21.55 ? 177 TYR B OH 1 ATOM 5734 N N . ARG B 1 178 ? 2.943 -19.494 24.468 1.00 16.23 ? 178 ARG B N 1 ATOM 5735 C CA . ARG B 1 178 ? 3.177 -19.466 23.022 1.00 18.56 ? 178 ARG B CA 1 ATOM 5736 C C . ARG B 1 178 ? 4.517 -18.778 22.745 1.00 18.44 ? 178 ARG B C 1 ATOM 5737 O O . ARG B 1 178 ? 4.875 -17.807 23.423 1.00 18.68 ? 178 ARG B O 1 ATOM 5738 C CB . ARG B 1 178 ? 2.052 -18.709 22.310 1.00 21.78 ? 178 ARG B CB 1 ATOM 5739 C CG . ARG B 1 178 ? 0.683 -19.382 22.338 1.00 26.94 ? 178 ARG B CG 1 ATOM 5740 C CD . ARG B 1 178 ? 0.475 -20.318 21.148 1.00 29.86 ? 178 ARG B CD 1 ATOM 5741 N NE . ARG B 1 178 ? 0.376 -19.585 19.884 1.00 35.27 ? 178 ARG B NE 1 ATOM 5742 C CZ . ARG B 1 178 ? 0.210 -20.140 18.683 1.00 36.86 ? 178 ARG B CZ 1 ATOM 5743 N NH1 . ARG B 1 178 ? 0.120 -21.458 18.545 1.00 37.09 ? 178 ARG B NH1 1 ATOM 5744 N NH2 . ARG B 1 178 ? 0.125 -19.366 17.608 1.00 38.89 ? 178 ARG B NH2 1 ATOM 5745 N N . ALA B 1 179 ? 5.256 -19.296 21.764 1.00 18.06 ? 179 ALA B N 1 ATOM 5746 C CA . ALA B 1 179 ? 6.567 -18.764 21.380 1.00 18.05 ? 179 ALA B CA 1 ATOM 5747 C C . ALA B 1 179 ? 6.460 -17.390 20.729 1.00 19.27 ? 179 ALA B C 1 ATOM 5748 O O . ALA B 1 179 ? 5.420 -17.048 20.165 1.00 20.44 ? 179 ALA B O 1 ATOM 5749 C CB . ALA B 1 179 ? 7.287 -19.734 20.463 1.00 16.28 ? 179 ALA B CB 1 ATOM 5750 N N . ALA B 1 180 ? 7.544 -16.617 20.814 1.00 19.90 ? 180 ALA B N 1 ATOM 5751 C CA . ALA B 1 180 ? 7.612 -15.250 20.290 1.00 21.00 ? 180 ALA B CA 1 ATOM 5752 C C . ALA B 1 180 ? 7.298 -15.032 18.818 1.00 22.16 ? 180 ALA B C 1 ATOM 5753 O O . ALA B 1 180 ? 6.609 -14.065 18.492 1.00 22.32 ? 180 ALA B O 1 ATOM 5754 C CB . ALA B 1 180 ? 8.948 -14.625 20.629 1.00 21.65 ? 180 ALA B CB 1 ATOM 5755 N N . ASP B 1 181 ? 7.782 -15.922 17.944 1.00 21.66 ? 181 ASP B N 1 ATOM 5756 C CA . ASP B 1 181 ? 7.539 -15.812 16.500 1.00 23.21 ? 181 ASP B CA 1 ATOM 5757 C C . ASP B 1 181 ? 6.086 -16.059 16.130 1.00 23.00 ? 181 ASP B C 1 ATOM 5758 O O . ASP B 1 181 ? 5.598 -15.510 15.139 1.00 23.96 ? 181 ASP B O 1 ATOM 5759 C CB . ASP B 1 181 ? 8.459 -16.736 15.700 1.00 24.49 ? 181 ASP B CB 1 ATOM 5760 C CG . ASP B 1 181 ? 9.906 -16.273 15.716 1.00 26.29 ? 181 ASP B CG 1 ATOM 5761 O OD1 . ASP B 1 181 ? 10.179 -15.141 15.253 1.00 26.08 ? 181 ASP B OD1 1 ATOM 5762 O OD2 . ASP B 1 181 ? 10.768 -17.038 16.200 1.00 26.95 ? 181 ASP B OD2 1 ATOM 5763 N N . ASP B 1 182 ? 5.395 -16.846 16.961 1.00 22.61 ? 182 ASP B N 1 ATOM 5764 C CA . ASP B 1 182 ? 3.971 -17.144 16.770 1.00 22.13 ? 182 ASP B CA 1 ATOM 5765 C C . ASP B 1 182 ? 3.136 -15.952 17.247 1.00 20.85 ? 182 ASP B C 1 ATOM 5766 O O . ASP B 1 182 ? 2.129 -15.606 16.631 1.00 21.77 ? 182 ASP B O 1 ATOM 5767 C CB . ASP B 1 182 ? 3.558 -18.418 17.523 1.00 21.41 ? 182 ASP B CB 1 ATOM 5768 C CG . ASP B 1 182 ? 3.860 -19.696 16.743 1.00 23.49 ? 182 ASP B CG 1 ATOM 5769 O OD1 . ASP B 1 182 ? 3.638 -19.722 15.508 1.00 21.83 ? 182 ASP B OD1 1 ATOM 5770 O OD2 . ASP B 1 182 ? 4.307 -20.685 17.373 1.00 22.44 ? 182 ASP B OD2 1 ATOM 5771 N N . LEU B 1 183 ? 3.615 -15.296 18.304 1.00 19.63 ? 183 LEU B N 1 ATOM 5772 C CA . LEU B 1 183 ? 2.964 -14.130 18.892 1.00 19.05 ? 183 LEU B CA 1 ATOM 5773 C C . LEU B 1 183 ? 3.147 -12.858 18.065 1.00 19.78 ? 183 LEU B C 1 ATOM 5774 O O . LEU B 1 183 ? 2.305 -11.967 18.117 1.00 20.84 ? 183 LEU B O 1 ATOM 5775 C CB . LEU B 1 183 ? 3.452 -13.910 20.323 1.00 16.87 ? 183 LEU B CB 1 ATOM 5776 C CG . LEU B 1 183 ? 2.978 -14.887 21.400 1.00 14.06 ? 183 LEU B CG 1 ATOM 5777 C CD1 . LEU B 1 183 ? 3.794 -14.685 22.654 1.00 13.11 ? 183 LEU B CD1 1 ATOM 5778 C CD2 . LEU B 1 183 ? 1.489 -14.715 21.688 1.00 14.06 ? 183 LEU B CD2 1 ATOM 5779 N N . VAL B 1 184 ? 4.239 -12.787 17.300 1.00 20.05 ? 184 VAL B N 1 ATOM 5780 C CA . VAL B 1 184 ? 4.520 -11.643 16.421 1.00 19.72 ? 184 VAL B CA 1 ATOM 5781 C C . VAL B 1 184 ? 3.543 -11.753 15.248 1.00 18.85 ? 184 VAL B C 1 ATOM 5782 O O . VAL B 1 184 ? 2.997 -10.747 14.806 1.00 17.14 ? 184 VAL B O 1 ATOM 5783 C CB . VAL B 1 184 ? 6.019 -11.625 15.932 1.00 18.90 ? 184 VAL B CB 1 ATOM 5784 C CG1 . VAL B 1 184 ? 6.222 -10.679 14.752 1.00 17.73 ? 184 VAL B CG1 1 ATOM 5785 C CG2 . VAL B 1 184 ? 6.923 -11.173 17.057 1.00 17.01 ? 184 VAL B CG2 1 ATOM 5786 N N . HIS B 1 185 ? 3.286 -12.992 14.815 1.00 20.04 ? 185 HIS B N 1 ATOM 5787 C CA . HIS B 1 185 ? 2.350 -13.283 13.728 1.00 21.40 ? 185 HIS B CA 1 ATOM 5788 C C . HIS B 1 185 ? 0.911 -13.010 14.180 1.00 20.21 ? 185 HIS B C 1 ATOM 5789 O O . HIS B 1 185 ? 0.091 -12.551 13.387 1.00 20.77 ? 185 HIS B O 1 ATOM 5790 C CB . HIS B 1 185 ? 2.486 -14.739 13.251 1.00 23.71 ? 185 HIS B CB 1 ATOM 5791 C CG . HIS B 1 185 ? 1.469 -15.130 12.218 1.00 28.19 ? 185 HIS B CG 1 ATOM 5792 N ND1 . HIS B 1 185 ? 1.294 -14.428 11.045 1.00 29.33 ? 185 HIS B ND1 1 ATOM 5793 C CD2 . HIS B 1 185 ? 0.515 -16.092 12.226 1.00 29.51 ? 185 HIS B CD2 1 ATOM 5794 C CE1 . HIS B 1 185 ? 0.274 -14.935 10.378 1.00 30.53 ? 185 HIS B CE1 1 ATOM 5795 N NE2 . HIS B 1 185 ? -0.217 -15.946 11.073 1.00 30.57 ? 185 HIS B NE2 1 ATOM 5796 N N . PHE B 1 186 ? 0.624 -13.317 15.448 1.00 19.20 ? 186 PHE B N 1 ATOM 5797 C CA . PHE B 1 186 ? -0.691 -13.102 16.042 1.00 18.09 ? 186 PHE B CA 1 ATOM 5798 C C . PHE B 1 186 ? -0.967 -11.602 16.188 1.00 17.42 ? 186 PHE B C 1 ATOM 5799 O O . PHE B 1 186 ? -1.967 -11.109 15.665 1.00 17.44 ? 186 PHE B O 1 ATOM 5800 C CB . PHE B 1 186 ? -0.782 -13.810 17.405 1.00 19.23 ? 186 PHE B CB 1 ATOM 5801 C CG . PHE B 1 186 ? -2.133 -13.707 18.072 1.00 20.04 ? 186 PHE B CG 1 ATOM 5802 C CD1 . PHE B 1 186 ? -3.241 -14.412 17.559 1.00 19.26 ? 186 PHE B CD1 1 ATOM 5803 C CD2 . PHE B 1 186 ? -2.303 -12.906 19.225 1.00 21.05 ? 186 PHE B CD2 1 ATOM 5804 C CE1 . PHE B 1 186 ? -4.509 -14.325 18.182 1.00 20.66 ? 186 PHE B CE1 1 ATOM 5805 C CE2 . PHE B 1 186 ? -3.565 -12.806 19.865 1.00 21.46 ? 186 PHE B CE2 1 ATOM 5806 C CZ . PHE B 1 186 ? -4.673 -13.518 19.342 1.00 21.72 ? 186 PHE B CZ 1 ATOM 5807 N N . THR B 1 187 ? -0.042 -10.878 16.821 1.00 16.24 ? 187 THR B N 1 ATOM 5808 C CA . THR B 1 187 ? -0.201 -9.437 17.034 1.00 17.56 ? 187 THR B CA 1 ATOM 5809 C C . THR B 1 187 ? -0.210 -8.551 15.788 1.00 19.06 ? 187 THR B C 1 ATOM 5810 O O . THR B 1 187 ? -0.661 -7.400 15.841 1.00 18.49 ? 187 THR B O 1 ATOM 5811 C CB . THR B 1 187 ? 0.793 -8.886 18.048 1.00 17.51 ? 187 THR B CB 1 ATOM 5812 O OG1 . THR B 1 187 ? 2.133 -9.122 17.601 1.00 17.11 ? 187 THR B OG1 1 ATOM 5813 C CG2 . THR B 1 187 ? 0.576 -9.536 19.409 1.00 16.27 ? 187 THR B CG2 1 ATOM 5814 N N . GLN B 1 188 ? 0.239 -9.113 14.665 1.00 21.11 ? 188 GLN B N 1 ATOM 5815 C CA . GLN B 1 188 ? 0.256 -8.407 13.382 1.00 22.92 ? 188 GLN B CA 1 ATOM 5816 C C . GLN B 1 188 ? -1.166 -8.175 12.886 1.00 22.12 ? 188 GLN B C 1 ATOM 5817 O O . GLN B 1 188 ? -1.450 -7.156 12.259 1.00 22.09 ? 188 GLN B O 1 ATOM 5818 C CB . GLN B 1 188 ? 1.026 -9.205 12.326 1.00 24.48 ? 188 GLN B CB 1 ATOM 5819 C CG . GLN B 1 188 ? 2.519 -8.922 12.291 1.00 29.07 ? 188 GLN B CG 1 ATOM 5820 C CD . GLN B 1 188 ? 3.230 -9.534 11.086 1.00 30.29 ? 188 GLN B CD 1 ATOM 5821 O OE1 . GLN B 1 188 ? 3.104 -10.729 10.806 1.00 29.83 ? 188 GLN B OE1 1 ATOM 5822 N NE2 . GLN B 1 188 ? 3.989 -8.706 10.370 1.00 31.35 ? 188 GLN B NE2 1 ATOM 5823 N N . ASN B 1 189 ? -2.055 -9.116 13.203 1.00 22.19 ? 189 ASN B N 1 ATOM 5824 C CA . ASN B 1 189 ? -3.452 -9.046 12.788 1.00 21.02 ? 189 ASN B CA 1 ATOM 5825 C C . ASN B 1 189 ? -4.435 -8.963 13.938 1.00 20.86 ? 189 ASN B C 1 ATOM 5826 O O . ASN B 1 189 ? -5.629 -8.782 13.713 1.00 22.10 ? 189 ASN B O 1 ATOM 5827 C CB . ASN B 1 189 ? -3.805 -10.234 11.891 1.00 20.72 ? 189 ASN B CB 1 ATOM 5828 C CG . ASN B 1 189 ? -3.166 -10.140 10.526 1.00 19.21 ? 189 ASN B CG 1 ATOM 5829 O OD1 . ASN B 1 189 ? -3.572 -9.331 9.697 1.00 21.54 ? 189 ASN B OD1 1 ATOM 5830 N ND2 . ASN B 1 189 ? -2.148 -10.956 10.291 1.00 19.59 ? 189 ASN B ND2 1 ATOM 5831 N N . ASN B 1 190 ? -3.940 -9.130 15.162 1.00 20.06 ? 190 ASN B N 1 ATOM 5832 C CA . ASN B 1 190 ? -4.784 -9.077 16.358 1.00 19.70 ? 190 ASN B CA 1 ATOM 5833 C C . ASN B 1 190 ? -4.236 -8.163 17.439 1.00 17.59 ? 190 ASN B C 1 ATOM 5834 O O . ASN B 1 190 ? -3.062 -7.801 17.426 1.00 18.62 ? 190 ASN B O 1 ATOM 5835 C CB . ASN B 1 190 ? -5.000 -10.480 16.953 1.00 21.26 ? 190 ASN B CB 1 ATOM 5836 C CG . ASN B 1 190 ? -5.823 -11.385 16.056 1.00 23.96 ? 190 ASN B CG 1 ATOM 5837 O OD1 . ASN B 1 190 ? -7.017 -11.611 16.297 1.00 26.81 ? 190 ASN B OD1 1 ATOM 5838 N ND2 . ASN B 1 190 ? -5.188 -11.914 15.017 1.00 22.30 ? 190 ASN B ND2 1 ATOM 5839 N N . ALA B 1 191 ? -5.105 -7.782 18.370 1.00 15.15 ? 191 ALA B N 1 ATOM 5840 C CA . ALA B 1 191 ? -4.722 -6.936 19.495 1.00 14.34 ? 191 ALA B CA 1 ATOM 5841 C C . ALA B 1 191 ? -3.867 -7.786 20.449 1.00 13.54 ? 191 ALA B C 1 ATOM 5842 O O . ALA B 1 191 ? -4.098 -8.991 20.566 1.00 14.35 ? 191 ALA B O 1 ATOM 5843 C CB . ALA B 1 191 ? -5.973 -6.422 20.211 1.00 14.27 ? 191 ALA B CB 1 ATOM 5844 N N . PRO B 1 192 ? -2.830 -7.196 21.085 1.00 13.68 ? 192 PRO B N 1 ATOM 5845 C CA . PRO B 1 192 ? -1.983 -7.961 22.009 1.00 15.08 ? 192 PRO B CA 1 ATOM 5846 C C . PRO B 1 192 ? -2.741 -8.724 23.112 1.00 17.03 ? 192 PRO B C 1 ATOM 5847 O O . PRO B 1 192 ? -3.717 -8.208 23.680 1.00 18.19 ? 192 PRO B O 1 ATOM 5848 C CB . PRO B 1 192 ? -1.038 -6.891 22.580 1.00 14.25 ? 192 PRO B CB 1 ATOM 5849 C CG . PRO B 1 192 ? -1.768 -5.604 22.357 1.00 15.98 ? 192 PRO B CG 1 ATOM 5850 C CD . PRO B 1 192 ? -2.334 -5.814 20.985 1.00 14.16 ? 192 PRO B CD 1 ATOM 5851 N N . PRO B 1 193 ? -2.379 -10.010 23.331 1.00 17.61 ? 193 PRO B N 1 ATOM 5852 C CA . PRO B 1 193 ? -3.043 -10.813 24.366 1.00 16.84 ? 193 PRO B CA 1 ATOM 5853 C C . PRO B 1 193 ? -2.465 -10.516 25.752 1.00 16.57 ? 193 PRO B C 1 ATOM 5854 O O . PRO B 1 193 ? -1.440 -9.827 25.869 1.00 16.09 ? 193 PRO B O 1 ATOM 5855 C CB . PRO B 1 193 ? -2.710 -12.239 23.938 1.00 17.91 ? 193 PRO B CB 1 ATOM 5856 C CG . PRO B 1 193 ? -1.310 -12.101 23.386 1.00 17.15 ? 193 PRO B CG 1 ATOM 5857 C CD . PRO B 1 193 ? -1.423 -10.836 22.557 1.00 16.70 ? 193 PRO B CD 1 ATOM 5858 N N . PHE B 1 194 ? -3.135 -11.011 26.792 1.00 14.83 ? 194 PHE B N 1 ATOM 5859 C CA . PHE B 1 194 ? -2.643 -10.845 28.162 1.00 12.68 ? 194 PHE B CA 1 ATOM 5860 C C . PHE B 1 194 ? -1.608 -11.927 28.388 1.00 12.26 ? 194 PHE B C 1 ATOM 5861 O O . PHE B 1 194 ? -1.603 -12.947 27.688 1.00 10.34 ? 194 PHE B O 1 ATOM 5862 C CB . PHE B 1 194 ? -3.758 -11.062 29.177 1.00 12.53 ? 194 PHE B CB 1 ATOM 5863 C CG . PHE B 1 194 ? -4.491 -9.817 29.588 1.00 14.40 ? 194 PHE B CG 1 ATOM 5864 C CD1 . PHE B 1 194 ? -4.446 -8.633 28.815 1.00 16.99 ? 194 PHE B CD1 1 ATOM 5865 C CD2 . PHE B 1 194 ? -5.266 -9.831 30.765 1.00 13.66 ? 194 PHE B CD2 1 ATOM 5866 C CE1 . PHE B 1 194 ? -5.169 -7.476 29.215 1.00 17.20 ? 194 PHE B CE1 1 ATOM 5867 C CE2 . PHE B 1 194 ? -5.993 -8.688 31.181 1.00 14.44 ? 194 PHE B CE2 1 ATOM 5868 C CZ . PHE B 1 194 ? -5.947 -7.507 30.405 1.00 15.18 ? 194 PHE B CZ 1 ATOM 5869 N N . SER B 1 195 ? -0.725 -11.708 29.356 1.00 12.67 ? 195 SER B N 1 ATOM 5870 C CA . SER B 1 195 ? 0.276 -12.712 29.678 1.00 13.90 ? 195 SER B CA 1 ATOM 5871 C C . SER B 1 195 ? -0.372 -13.853 30.433 1.00 13.34 ? 195 SER B C 1 ATOM 5872 O O . SER B 1 195 ? -1.441 -13.685 31.020 1.00 11.75 ? 195 SER B O 1 ATOM 5873 C CB . SER B 1 195 ? 1.417 -12.120 30.486 1.00 15.33 ? 195 SER B CB 1 ATOM 5874 O OG . SER B 1 195 ? 0.941 -11.504 31.655 1.00 14.73 ? 195 SER B OG 1 ATOM 5875 N N . ASP B 1 196 ? 0.246 -15.025 30.349 1.00 13.43 ? 196 ASP B N 1 ATOM 5876 C CA . ASP B 1 196 ? -0.260 -16.210 31.032 1.00 13.33 ? 196 ASP B CA 1 ATOM 5877 C C . ASP B 1 196 ? 0.154 -16.158 32.504 1.00 14.87 ? 196 ASP B C 1 ATOM 5878 O O . ASP B 1 196 ? -0.556 -16.651 33.385 1.00 16.05 ? 196 ASP B O 1 ATOM 5879 C CB . ASP B 1 196 ? 0.276 -17.463 30.356 1.00 9.48 ? 196 ASP B CB 1 ATOM 5880 C CG . ASP B 1 196 ? -0.201 -17.611 28.910 1.00 9.21 ? 196 ASP B CG 1 ATOM 5881 O OD1 . ASP B 1 196 ? -1.430 -17.586 28.652 1.00 8.31 ? 196 ASP B OD1 1 ATOM 5882 O OD2 . ASP B 1 196 ? 0.663 -17.778 28.028 1.00 5.08 ? 196 ASP B OD2 1 ATOM 5883 N N . ASN B 1 197 ? 1.306 -15.538 32.749 1.00 15.65 ? 197 ASN B N 1 ATOM 5884 C CA . ASN B 1 197 ? 1.844 -15.366 34.091 1.00 15.64 ? 197 ASN B CA 1 ATOM 5885 C C . ASN B 1 197 ? 2.871 -14.250 34.072 1.00 14.93 ? 197 ASN B C 1 ATOM 5886 O O . ASN B 1 197 ? 3.226 -13.730 33.012 1.00 14.91 ? 197 ASN B O 1 ATOM 5887 C CB . ASN B 1 197 ? 2.492 -16.665 34.614 1.00 15.72 ? 197 ASN B CB 1 ATOM 5888 C CG . ASN B 1 197 ? 2.190 -16.920 36.100 1.00 19.35 ? 197 ASN B CG 1 ATOM 5889 O OD1 . ASN B 1 197 ? 2.193 -15.991 36.920 1.00 19.28 ? 197 ASN B OD1 1 ATOM 5890 N ND2 . ASN B 1 197 ? 1.925 -18.180 36.448 1.00 17.18 ? 197 ASN B ND2 1 ATOM 5891 N N . VAL B 1 198 ? 3.264 -13.820 35.264 1.00 15.27 ? 198 VAL B N 1 ATOM 5892 C CA . VAL B 1 198 ? 4.277 -12.791 35.433 1.00 15.30 ? 198 VAL B CA 1 ATOM 5893 C C . VAL B 1 198 ? 5.318 -13.391 36.368 1.00 15.50 ? 198 VAL B C 1 ATOM 5894 O O . VAL B 1 198 ? 5.029 -13.672 37.540 1.00 16.74 ? 198 VAL B O 1 ATOM 5895 C CB . VAL B 1 198 ? 3.696 -11.463 36.009 1.00 15.16 ? 198 VAL B CB 1 ATOM 5896 C CG1 . VAL B 1 198 ? 4.806 -10.486 36.384 1.00 13.74 ? 198 VAL B CG1 1 ATOM 5897 C CG2 . VAL B 1 198 ? 2.762 -10.806 35.012 1.00 17.69 ? 198 VAL B CG2 1 ATOM 5898 N N . LEU B 1 199 ? 6.512 -13.610 35.822 1.00 15.74 ? 199 LEU B N 1 ATOM 5899 C CA . LEU B 1 199 ? 7.638 -14.176 36.559 1.00 17.20 ? 199 LEU B CA 1 ATOM 5900 C C . LEU B 1 199 ? 8.403 -13.120 37.336 1.00 17.90 ? 199 LEU B C 1 ATOM 5901 O O . LEU B 1 199 ? 8.697 -12.044 36.815 1.00 19.29 ? 199 LEU B O 1 ATOM 5902 C CB . LEU B 1 199 ? 8.617 -14.868 35.622 1.00 16.47 ? 199 LEU B CB 1 ATOM 5903 C CG . LEU B 1 199 ? 8.212 -16.079 34.798 1.00 17.08 ? 199 LEU B CG 1 ATOM 5904 C CD1 . LEU B 1 199 ? 9.351 -16.409 33.878 1.00 17.16 ? 199 LEU B CD1 1 ATOM 5905 C CD2 . LEU B 1 199 ? 7.869 -17.261 35.665 1.00 18.97 ? 199 LEU B CD2 1 ATOM 5906 N N . ILE B 1 200 ? 8.666 -13.424 38.606 1.00 16.48 ? 200 ILE B N 1 ATOM 5907 C CA . ILE B 1 200 ? 9.410 -12.545 39.496 1.00 14.34 ? 200 ILE B CA 1 ATOM 5908 C C . ILE B 1 200 ? 10.640 -13.352 39.904 1.00 16.03 ? 200 ILE B C 1 ATOM 5909 O O . ILE B 1 200 ? 10.513 -14.402 40.532 1.00 17.31 ? 200 ILE B O 1 ATOM 5910 C CB . ILE B 1 200 ? 8.565 -12.132 40.733 1.00 11.88 ? 200 ILE B CB 1 ATOM 5911 C CG1 . ILE B 1 200 ? 7.241 -11.500 40.285 1.00 9.64 ? 200 ILE B CG1 1 ATOM 5912 C CG2 . ILE B 1 200 ? 9.316 -11.097 41.546 1.00 10.52 ? 200 ILE B CG2 1 ATOM 5913 C CD1 . ILE B 1 200 ? 6.256 -11.270 41.369 1.00 4.40 ? 200 ILE B CD1 1 ATOM 5914 N N . ASN B 1 201 ? 11.815 -12.866 39.491 1.00 17.71 ? 201 ASN B N 1 ATOM 5915 C CA . ASN B 1 201 ? 13.132 -13.488 39.720 1.00 20.85 ? 201 ASN B CA 1 ATOM 5916 C C . ASN B 1 201 ? 13.155 -14.908 39.138 1.00 20.39 ? 201 ASN B C 1 ATOM 5917 O O . ASN B 1 201 ? 13.735 -15.831 39.717 1.00 22.02 ? 201 ASN B O 1 ATOM 5918 C CB . ASN B 1 201 ? 13.540 -13.454 41.215 1.00 25.50 ? 201 ASN B CB 1 ATOM 5919 C CG . ASN B 1 201 ? 15.066 -13.507 41.426 1.00 30.45 ? 201 ASN B CG 1 ATOM 5920 O OD1 . ASN B 1 201 ? 15.846 -13.332 40.479 1.00 30.16 ? 201 ASN B OD1 1 ATOM 5921 N ND2 . ASN B 1 201 ? 15.477 -13.747 42.673 1.00 35.53 ? 201 ASN B ND2 1 ATOM 5922 N N . GLY B 1 202 ? 12.457 -15.059 38.009 1.00 19.31 ? 202 GLY B N 1 ATOM 5923 C CA . GLY B 1 202 ? 12.353 -16.328 37.307 1.00 19.40 ? 202 GLY B CA 1 ATOM 5924 C C . GLY B 1 202 ? 11.334 -17.344 37.811 1.00 19.07 ? 202 GLY B C 1 ATOM 5925 O O . GLY B 1 202 ? 11.293 -18.461 37.297 1.00 19.40 ? 202 GLY B O 1 ATOM 5926 N N . THR B 1 203 ? 10.545 -16.988 38.827 1.00 19.46 ? 203 THR B N 1 ATOM 5927 C CA . THR B 1 203 ? 9.537 -17.892 39.401 1.00 19.55 ? 203 THR B CA 1 ATOM 5928 C C . THR B 1 203 ? 8.144 -17.257 39.538 1.00 17.98 ? 203 THR B C 1 ATOM 5929 O O . THR B 1 203 ? 8.017 -16.039 39.632 1.00 19.16 ? 203 THR B O 1 ATOM 5930 C CB . THR B 1 203 ? 9.967 -18.438 40.805 1.00 20.42 ? 203 THR B CB 1 ATOM 5931 O OG1 . THR B 1 203 ? 10.136 -17.355 41.725 1.00 21.72 ? 203 THR B OG1 1 ATOM 5932 C CG2 . THR B 1 203 ? 11.268 -19.229 40.732 1.00 22.97 ? 203 THR B CG2 1 ATOM 5933 N N . ALA B 1 204 ? 7.110 -18.099 39.528 1.00 18.77 ? 204 ALA B N 1 ATOM 5934 C CA . ALA B 1 204 ? 5.703 -17.683 39.677 1.00 19.88 ? 204 ALA B CA 1 ATOM 5935 C C . ALA B 1 204 ? 4.821 -18.892 39.928 1.00 21.14 ? 204 ALA B C 1 ATOM 5936 O O . ALA B 1 204 ? 5.190 -20.022 39.596 1.00 19.81 ? 204 ALA B O 1 ATOM 5937 C CB . ALA B 1 204 ? 5.200 -16.953 38.430 1.00 20.41 ? 204 ALA B CB 1 ATOM 5938 N N . VAL B 1 205 ? 3.648 -18.638 40.508 1.00 22.81 ? 205 VAL B N 1 ATOM 5939 C CA . VAL B 1 205 ? 2.667 -19.683 40.788 1.00 24.59 ? 205 VAL B CA 1 ATOM 5940 C C . VAL B 1 205 ? 1.588 -19.647 39.712 1.00 26.66 ? 205 VAL B C 1 ATOM 5941 O O . VAL B 1 205 ? 1.182 -18.571 39.259 1.00 27.65 ? 205 VAL B O 1 ATOM 5942 C CB . VAL B 1 205 ? 2.030 -19.507 42.206 1.00 24.71 ? 205 VAL B CB 1 ATOM 5943 C CG1 . VAL B 1 205 ? 0.894 -20.513 42.462 1.00 23.76 ? 205 VAL B CG1 1 ATOM 5944 C CG2 . VAL B 1 205 ? 3.084 -19.724 43.256 1.00 25.22 ? 205 VAL B CG2 1 ATOM 5945 N N . ASN B 1 206 ? 1.141 -20.837 39.307 1.00 28.14 ? 206 ASN B N 1 ATOM 5946 C CA . ASN B 1 206 ? 0.087 -20.996 38.310 1.00 30.07 ? 206 ASN B CA 1 ATOM 5947 C C . ASN B 1 206 ? -1.262 -20.735 39.010 1.00 32.15 ? 206 ASN B C 1 ATOM 5948 O O . ASN B 1 206 ? -1.529 -21.322 40.061 1.00 32.74 ? 206 ASN B O 1 ATOM 5949 C CB . ASN B 1 206 ? 0.126 -22.417 37.748 1.00 28.35 ? 206 ASN B CB 1 ATOM 5950 C CG . ASN B 1 206 ? -0.623 -22.553 36.443 1.00 27.59 ? 206 ASN B CG 1 ATOM 5951 O OD1 . ASN B 1 206 ? -1.778 -22.971 36.414 1.00 26.26 ? 206 ASN B OD1 1 ATOM 5952 N ND2 . ASN B 1 206 ? 0.038 -22.207 35.351 1.00 29.86 ? 206 ASN B ND2 1 ATOM 5953 N N . PRO B 1 207 ? -2.097 -19.812 38.470 1.00 33.48 ? 207 PRO B N 1 ATOM 5954 C CA . PRO B 1 207 ? -3.405 -19.494 39.067 1.00 34.26 ? 207 PRO B CA 1 ATOM 5955 C C . PRO B 1 207 ? -4.490 -20.573 38.904 1.00 35.25 ? 207 PRO B C 1 ATOM 5956 O O . PRO B 1 207 ? -5.505 -20.550 39.607 1.00 35.96 ? 207 PRO B O 1 ATOM 5957 C CB . PRO B 1 207 ? -3.790 -18.195 38.357 1.00 34.22 ? 207 PRO B CB 1 ATOM 5958 C CG . PRO B 1 207 ? -3.193 -18.369 37.003 1.00 34.27 ? 207 PRO B CG 1 ATOM 5959 C CD . PRO B 1 207 ? -1.824 -18.910 37.331 1.00 34.33 ? 207 PRO B CD 1 ATOM 5960 N N . ASN B 1 208 ? -4.250 -21.517 37.995 1.00 35.58 ? 208 ASN B N 1 ATOM 5961 C CA . ASN B 1 208 ? -5.186 -22.607 37.716 1.00 36.64 ? 208 ASN B CA 1 ATOM 5962 C C . ASN B 1 208 ? -4.864 -23.903 38.467 1.00 36.89 ? 208 ASN B C 1 ATOM 5963 O O . ASN B 1 208 ? -5.755 -24.519 39.062 1.00 38.18 ? 208 ASN B O 1 ATOM 5964 C CB . ASN B 1 208 ? -5.240 -22.893 36.207 1.00 36.08 ? 208 ASN B CB 1 ATOM 5965 C CG . ASN B 1 208 ? -5.503 -21.643 35.381 1.00 35.75 ? 208 ASN B CG 1 ATOM 5966 O OD1 . ASN B 1 208 ? -6.554 -21.016 35.500 1.00 33.93 ? 208 ASN B OD1 1 ATOM 5967 N ND2 . ASN B 1 208 ? -4.532 -21.268 34.551 1.00 35.24 ? 208 ASN B ND2 1 ATOM 5968 N N . THR B 1 209 ? -3.591 -24.303 38.444 1.00 36.21 ? 209 THR B N 1 ATOM 5969 C CA . THR B 1 209 ? -3.141 -25.539 39.091 1.00 34.74 ? 209 THR B CA 1 ATOM 5970 C C . THR B 1 209 ? -2.588 -25.356 40.508 1.00 34.69 ? 209 THR B C 1 ATOM 5971 O O . THR B 1 209 ? -2.824 -26.191 41.386 1.00 33.56 ? 209 THR B O 1 ATOM 5972 C CB . THR B 1 209 ? -2.089 -26.269 38.222 1.00 34.44 ? 209 THR B CB 1 ATOM 5973 O OG1 . THR B 1 209 ? -0.882 -25.499 38.168 1.00 32.53 ? 209 THR B OG1 1 ATOM 5974 C CG2 . THR B 1 209 ? -2.618 -26.482 36.800 1.00 33.86 ? 209 THR B CG2 1 ATOM 5975 N N . GLY B 1 210 ? -1.839 -24.272 40.707 1.00 34.37 ? 210 GLY B N 1 ATOM 5976 C CA . GLY B 1 210 ? -1.243 -23.978 42.002 1.00 34.20 ? 210 GLY B CA 1 ATOM 5977 C C . GLY B 1 210 ? 0.224 -24.354 42.095 1.00 33.41 ? 210 GLY B C 1 ATOM 5978 O O . GLY B 1 210 ? 0.871 -24.086 43.111 1.00 33.63 ? 210 GLY B O 1 ATOM 5979 N N . GLU B 1 211 ? 0.754 -24.927 41.013 1.00 33.58 ? 211 GLU B N 1 ATOM 5980 C CA . GLU B 1 211 ? 2.146 -25.371 40.934 1.00 33.43 ? 211 GLU B CA 1 ATOM 5981 C C . GLU B 1 211 ? 3.163 -24.248 40.853 1.00 32.84 ? 211 GLU B C 1 ATOM 5982 O O . GLU B 1 211 ? 2.830 -23.127 40.471 1.00 31.54 ? 211 GLU B O 1 ATOM 5983 C CB . GLU B 1 211 ? 2.337 -26.307 39.749 1.00 35.44 ? 211 GLU B CB 1 ATOM 5984 C CG . GLU B 1 211 ? 1.559 -27.599 39.846 1.00 38.72 ? 211 GLU B CG 1 ATOM 5985 C CD . GLU B 1 211 ? 1.834 -28.502 38.674 1.00 40.77 ? 211 GLU B CD 1 ATOM 5986 O OE1 . GLU B 1 211 ? 2.862 -29.209 38.711 1.00 42.85 ? 211 GLU B OE1 1 ATOM 5987 O OE2 . GLU B 1 211 ? 1.039 -28.489 37.710 1.00 41.29 ? 211 GLU B OE2 1 ATOM 5988 N N . GLY B 1 212 ? 4.404 -24.578 41.201 1.00 33.79 ? 212 GLY B N 1 ATOM 5989 C CA . GLY B 1 212 ? 5.490 -23.613 41.197 1.00 35.32 ? 212 GLY B CA 1 ATOM 5990 C C . GLY B 1 212 ? 5.717 -23.026 42.580 1.00 36.75 ? 212 GLY B C 1 ATOM 5991 O O . GLY B 1 212 ? 5.266 -23.588 43.587 1.00 37.05 ? 212 GLY B O 1 ATOM 5992 N N . GLN B 1 213 ? 6.423 -21.898 42.629 1.00 37.18 ? 213 GLN B N 1 ATOM 5993 C CA . GLN B 1 213 ? 6.716 -21.216 43.887 1.00 37.18 ? 213 GLN B CA 1 ATOM 5994 C C . GLN B 1 213 ? 6.791 -19.700 43.720 1.00 36.07 ? 213 GLN B C 1 ATOM 5995 O O . GLN B 1 213 ? 7.092 -19.204 42.629 1.00 35.88 ? 213 GLN B O 1 ATOM 5996 C CB . GLN B 1 213 ? 8.016 -21.758 44.522 1.00 39.45 ? 213 GLN B CB 1 ATOM 5997 C CG . GLN B 1 213 ? 9.290 -21.668 43.668 1.00 41.75 ? 213 GLN B CG 1 ATOM 5998 C CD . GLN B 1 213 ? 10.527 -22.266 44.351 1.00 43.88 ? 213 GLN B CD 1 ATOM 5999 O OE1 . GLN B 1 213 ? 11.367 -22.886 43.693 1.00 44.43 ? 213 GLN B OE1 1 ATOM 6000 N NE2 . GLN B 1 213 ? 10.649 -22.070 45.666 1.00 42.82 ? 213 GLN B NE2 1 ATOM 6001 N N . TYR B 1 214 ? 6.445 -18.973 44.786 1.00 33.57 ? 214 TYR B N 1 ATOM 6002 C CA . TYR B 1 214 ? 6.518 -17.510 44.791 1.00 31.60 ? 214 TYR B CA 1 ATOM 6003 C C . TYR B 1 214 ? 7.985 -17.157 45.060 1.00 30.58 ? 214 TYR B C 1 ATOM 6004 O O . TYR B 1 214 ? 8.704 -17.941 45.693 1.00 29.94 ? 214 TYR B O 1 ATOM 6005 C CB . TYR B 1 214 ? 5.666 -16.905 45.915 1.00 31.59 ? 214 TYR B CB 1 ATOM 6006 C CG . TYR B 1 214 ? 4.165 -17.125 45.841 1.00 31.73 ? 214 TYR B CG 1 ATOM 6007 C CD1 . TYR B 1 214 ? 3.348 -16.310 45.025 1.00 32.05 ? 214 TYR B CD1 1 ATOM 6008 C CD2 . TYR B 1 214 ? 3.540 -18.121 46.626 1.00 31.94 ? 214 TYR B CD2 1 ATOM 6009 C CE1 . TYR B 1 214 ? 1.921 -16.480 44.990 1.00 30.91 ? 214 TYR B CE1 1 ATOM 6010 C CE2 . TYR B 1 214 ? 2.120 -18.305 46.598 1.00 31.12 ? 214 TYR B CE2 1 ATOM 6011 C CZ . TYR B 1 214 ? 1.323 -17.481 45.780 1.00 31.03 ? 214 TYR B CZ 1 ATOM 6012 O OH . TYR B 1 214 ? -0.043 -17.665 45.748 1.00 29.57 ? 214 TYR B OH 1 ATOM 6013 N N . ALA B 1 215 ? 8.431 -16.001 44.568 1.00 29.44 ? 215 ALA B N 1 ATOM 6014 C CA . ALA B 1 215 ? 9.810 -15.544 44.781 1.00 29.29 ? 215 ALA B CA 1 ATOM 6015 C C . ALA B 1 215 ? 10.002 -15.224 46.269 1.00 28.73 ? 215 ALA B C 1 ATOM 6016 O O . ALA B 1 215 ? 9.123 -14.631 46.901 1.00 28.28 ? 215 ALA B O 1 ATOM 6017 C CB . ALA B 1 215 ? 10.107 -14.325 43.920 1.00 28.82 ? 215 ALA B CB 1 ATOM 6018 N N . ASN B 1 216 ? 11.125 -15.666 46.827 1.00 28.41 ? 216 ASN B N 1 ATOM 6019 C CA . ASN B 1 216 ? 11.399 -15.471 48.243 1.00 27.29 ? 216 ASN B CA 1 ATOM 6020 C C . ASN B 1 216 ? 12.621 -14.610 48.546 1.00 26.60 ? 216 ASN B C 1 ATOM 6021 O O . ASN B 1 216 ? 13.764 -15.059 48.407 1.00 26.80 ? 216 ASN B O 1 ATOM 6022 C CB . ASN B 1 216 ? 11.537 -16.837 48.913 1.00 29.90 ? 216 ASN B CB 1 ATOM 6023 C CG . ASN B 1 216 ? 11.192 -16.816 50.388 1.00 32.75 ? 216 ASN B CG 1 ATOM 6024 O OD1 . ASN B 1 216 ? 11.137 -15.764 51.033 1.00 29.75 ? 216 ASN B OD1 1 ATOM 6025 N ND2 . ASN B 1 216 ? 10.962 -18.012 50.919 1.00 37.96 ? 216 ASN B ND2 1 ATOM 6026 N N . VAL B 1 217 ? 12.354 -13.393 49.023 1.00 24.98 ? 217 VAL B N 1 ATOM 6027 C CA . VAL B 1 217 ? 13.395 -12.430 49.388 1.00 25.87 ? 217 VAL B CA 1 ATOM 6028 C C . VAL B 1 217 ? 13.460 -12.295 50.911 1.00 25.20 ? 217 VAL B C 1 ATOM 6029 O O . VAL B 1 217 ? 12.520 -11.804 51.538 1.00 24.46 ? 217 VAL B O 1 ATOM 6030 C CB . VAL B 1 217 ? 13.117 -11.024 48.792 1.00 25.59 ? 217 VAL B CB 1 ATOM 6031 C CG1 . VAL B 1 217 ? 14.325 -10.129 48.964 1.00 27.23 ? 217 VAL B CG1 1 ATOM 6032 C CG2 . VAL B 1 217 ? 12.741 -11.118 47.337 1.00 23.85 ? 217 VAL B CG2 1 ATOM 6033 N N . THR B 1 218 ? 14.581 -12.708 51.498 1.00 25.07 ? 218 THR B N 1 ATOM 6034 C CA . THR B 1 218 ? 14.745 -12.613 52.942 1.00 24.49 ? 218 THR B CA 1 ATOM 6035 C C . THR B 1 218 ? 15.360 -11.275 53.376 1.00 24.25 ? 218 THR B C 1 ATOM 6036 O O . THR B 1 218 ? 16.491 -10.940 53.017 1.00 23.34 ? 218 THR B O 1 ATOM 6037 C CB . THR B 1 218 ? 15.519 -13.829 53.529 1.00 25.28 ? 218 THR B CB 1 ATOM 6038 O OG1 . THR B 1 218 ? 14.861 -15.039 53.133 1.00 26.07 ? 218 THR B OG1 1 ATOM 6039 C CG2 . THR B 1 218 ? 15.525 -13.791 55.061 1.00 25.49 ? 218 THR B CG2 1 ATOM 6040 N N . LEU B 1 219 ? 14.559 -10.500 54.104 1.00 24.05 ? 219 LEU B N 1 ATOM 6041 C CA . LEU B 1 219 ? 14.962 -9.203 54.636 1.00 25.42 ? 219 LEU B CA 1 ATOM 6042 C C . LEU B 1 219 ? 15.473 -9.366 56.067 1.00 26.66 ? 219 LEU B C 1 ATOM 6043 O O . LEU B 1 219 ? 14.861 -10.074 56.874 1.00 25.97 ? 219 LEU B O 1 ATOM 6044 C CB . LEU B 1 219 ? 13.775 -8.233 54.650 1.00 24.88 ? 219 LEU B CB 1 ATOM 6045 C CG . LEU B 1 219 ? 13.075 -7.833 53.355 1.00 24.65 ? 219 LEU B CG 1 ATOM 6046 C CD1 . LEU B 1 219 ? 11.777 -7.126 53.692 1.00 25.36 ? 219 LEU B CD1 1 ATOM 6047 C CD2 . LEU B 1 219 ? 13.967 -6.953 52.501 1.00 23.95 ? 219 LEU B CD2 1 ATOM 6048 N N . THR B 1 220 ? 16.600 -8.718 56.366 1.00 28.43 ? 220 THR B N 1 ATOM 6049 C CA . THR B 1 220 ? 17.211 -8.745 57.700 1.00 29.11 ? 220 THR B CA 1 ATOM 6050 C C . THR B 1 220 ? 16.566 -7.587 58.486 1.00 29.71 ? 220 THR B C 1 ATOM 6051 O O . THR B 1 220 ? 16.685 -6.428 58.080 1.00 29.14 ? 220 THR B O 1 ATOM 6052 C CB . THR B 1 220 ? 18.758 -8.543 57.613 1.00 28.97 ? 220 THR B CB 1 ATOM 6053 O OG1 . THR B 1 220 ? 19.294 -9.406 56.603 1.00 28.87 ? 220 THR B OG1 1 ATOM 6054 C CG2 . THR B 1 220 ? 19.441 -8.864 58.956 1.00 27.12 ? 220 THR B CG2 1 ATOM 6055 N N . PRO B 1 221 ? 15.862 -7.887 59.607 1.00 31.64 ? 221 PRO B N 1 ATOM 6056 C CA . PRO B 1 221 ? 15.206 -6.845 60.418 1.00 32.34 ? 221 PRO B CA 1 ATOM 6057 C C . PRO B 1 221 ? 16.069 -5.682 60.950 1.00 33.01 ? 221 PRO B C 1 ATOM 6058 O O . PRO B 1 221 ? 17.067 -5.900 61.645 1.00 33.91 ? 221 PRO B O 1 ATOM 6059 C CB . PRO B 1 221 ? 14.536 -7.652 61.540 1.00 32.72 ? 221 PRO B CB 1 ATOM 6060 C CG . PRO B 1 221 ? 15.347 -8.927 61.606 1.00 32.26 ? 221 PRO B CG 1 ATOM 6061 C CD . PRO B 1 221 ? 15.574 -9.225 60.163 1.00 30.29 ? 221 PRO B CD 1 ATOM 6062 N N . GLY B 1 222 ? 15.693 -4.462 60.548 1.00 32.90 ? 222 GLY B N 1 ATOM 6063 C CA . GLY B 1 222 ? 16.382 -3.246 60.963 1.00 34.40 ? 222 GLY B CA 1 ATOM 6064 C C . GLY B 1 222 ? 17.428 -2.688 60.010 1.00 35.59 ? 222 GLY B C 1 ATOM 6065 O O . GLY B 1 222 ? 17.958 -1.589 60.226 1.00 36.22 ? 222 GLY B O 1 ATOM 6066 N N . LYS B 1 223 ? 17.718 -3.440 58.951 1.00 35.53 ? 223 LYS B N 1 ATOM 6067 C CA . LYS B 1 223 ? 18.714 -3.049 57.952 1.00 35.31 ? 223 LYS B CA 1 ATOM 6068 C C . LYS B 1 223 ? 18.095 -2.471 56.672 1.00 33.24 ? 223 LYS B C 1 ATOM 6069 O O . LYS B 1 223 ? 16.986 -2.852 56.294 1.00 34.14 ? 223 LYS B O 1 ATOM 6070 C CB . LYS B 1 223 ? 19.599 -4.259 57.605 1.00 36.21 ? 223 LYS B CB 1 ATOM 6071 C CG . LYS B 1 223 ? 20.394 -4.865 58.777 1.00 36.81 ? 223 LYS B CG 1 ATOM 6072 C CD . LYS B 1 223 ? 21.553 -3.979 59.217 1.00 38.70 ? 223 LYS B CD 1 ATOM 6073 C CE . LYS B 1 223 ? 22.336 -4.590 60.370 1.00 39.88 ? 223 LYS B CE 1 ATOM 6074 N NZ . LYS B 1 223 ? 23.567 -3.805 60.678 1.00 39.60 ? 223 LYS B NZ 1 ATOM 6075 N N . ARG B 1 224 ? 18.794 -1.525 56.038 1.00 31.23 ? 224 ARG B N 1 ATOM 6076 C CA . ARG B 1 224 ? 18.330 -0.915 54.783 1.00 29.76 ? 224 ARG B CA 1 ATOM 6077 C C . ARG B 1 224 ? 18.794 -1.839 53.652 1.00 28.72 ? 224 ARG B C 1 ATOM 6078 O O . ARG B 1 224 ? 19.985 -2.169 53.561 1.00 29.60 ? 224 ARG B O 1 ATOM 6079 C CB . ARG B 1 224 ? 18.920 0.488 54.547 1.00 29.68 ? 224 ARG B CB 1 ATOM 6080 C CG . ARG B 1 224 ? 18.814 1.515 55.663 1.00 29.07 ? 224 ARG B CG 1 ATOM 6081 C CD . ARG B 1 224 ? 20.155 1.619 56.360 1.00 31.63 ? 224 ARG B CD 1 ATOM 6082 N NE . ARG B 1 224 ? 20.532 2.977 56.741 1.00 31.63 ? 224 ARG B NE 1 ATOM 6083 C CZ . ARG B 1 224 ? 21.788 3.411 56.815 1.00 31.94 ? 224 ARG B CZ 1 ATOM 6084 N NH1 . ARG B 1 224 ? 22.805 2.601 56.526 1.00 31.78 ? 224 ARG B NH1 1 ATOM 6085 N NH2 . ARG B 1 224 ? 22.033 4.657 57.199 1.00 32.61 ? 224 ARG B NH2 1 ATOM 6086 N N . HIS B 1 225 ? 17.854 -2.258 52.807 1.00 25.78 ? 225 HIS B N 1 ATOM 6087 C CA . HIS B 1 225 ? 18.148 -3.170 51.702 1.00 24.89 ? 225 HIS B CA 1 ATOM 6088 C C . HIS B 1 225 ? 18.004 -2.524 50.340 1.00 23.60 ? 225 HIS B C 1 ATOM 6089 O O . HIS B 1 225 ? 16.991 -1.882 50.071 1.00 24.30 ? 225 HIS B O 1 ATOM 6090 C CB . HIS B 1 225 ? 17.191 -4.363 51.719 1.00 24.81 ? 225 HIS B CB 1 ATOM 6091 C CG . HIS B 1 225 ? 17.202 -5.145 52.990 1.00 24.73 ? 225 HIS B CG 1 ATOM 6092 N ND1 . HIS B 1 225 ? 16.457 -4.780 54.089 1.00 23.42 ? 225 HIS B ND1 1 ATOM 6093 C CD2 . HIS B 1 225 ? 17.845 -6.287 53.330 1.00 24.96 ? 225 HIS B CD2 1 ATOM 6094 C CE1 . HIS B 1 225 ? 16.643 -5.663 55.052 1.00 24.32 ? 225 HIS B CE1 1 ATOM 6095 N NE2 . HIS B 1 225 ? 17.480 -6.587 54.619 1.00 25.00 ? 225 HIS B NE2 1 ATOM 6096 N N . ARG B 1 226 ? 18.999 -2.715 49.474 1.00 21.14 ? 226 ARG B N 1 ATOM 6097 C CA . ARG B 1 226 ? 18.918 -2.189 48.114 1.00 17.52 ? 226 ARG B CA 1 ATOM 6098 C C . ARG B 1 226 ? 18.372 -3.302 47.230 1.00 15.40 ? 226 ARG B C 1 ATOM 6099 O O . ARG B 1 226 ? 18.862 -4.427 47.271 1.00 14.75 ? 226 ARG B O 1 ATOM 6100 C CB . ARG B 1 226 ? 20.271 -1.716 47.578 1.00 18.35 ? 226 ARG B CB 1 ATOM 6101 C CG . ARG B 1 226 ? 20.198 -1.133 46.163 1.00 16.72 ? 226 ARG B CG 1 ATOM 6102 C CD . ARG B 1 226 ? 21.566 -0.828 45.607 1.00 17.85 ? 226 ARG B CD 1 ATOM 6103 N NE . ARG B 1 226 ? 21.509 -0.151 44.313 1.00 18.14 ? 226 ARG B NE 1 ATOM 6104 C CZ . ARG B 1 226 ? 22.486 0.591 43.804 1.00 17.61 ? 226 ARG B CZ 1 ATOM 6105 N NH1 . ARG B 1 226 ? 23.616 0.770 44.474 1.00 17.84 ? 226 ARG B NH1 1 ATOM 6106 N NH2 . ARG B 1 226 ? 22.343 1.139 42.604 1.00 18.32 ? 226 ARG B NH2 1 ATOM 6107 N N . LEU B 1 227 ? 17.336 -2.974 46.464 1.00 13.53 ? 227 LEU B N 1 ATOM 6108 C CA . LEU B 1 227 ? 16.699 -3.910 45.550 1.00 10.01 ? 227 LEU B CA 1 ATOM 6109 C C . LEU B 1 227 ? 16.661 -3.312 44.144 1.00 9.04 ? 227 LEU B C 1 ATOM 6110 O O . LEU B 1 227 ? 16.137 -2.219 43.921 1.00 9.03 ? 227 LEU B O 1 ATOM 6111 C CB . LEU B 1 227 ? 15.291 -4.232 46.037 1.00 8.47 ? 227 LEU B CB 1 ATOM 6112 C CG . LEU B 1 227 ? 14.527 -5.324 45.304 1.00 4.92 ? 227 LEU B CG 1 ATOM 6113 C CD1 . LEU B 1 227 ? 15.073 -6.681 45.660 1.00 3.41 ? 227 LEU B CD1 1 ATOM 6114 C CD2 . LEU B 1 227 ? 13.067 -5.203 45.661 1.00 6.83 ? 227 LEU B CD2 1 ATOM 6115 N N . ARG B 1 228 ? 17.185 -4.073 43.195 1.00 8.16 ? 228 ARG B N 1 ATOM 6116 C CA . ARG B 1 228 ? 17.275 -3.654 41.803 1.00 7.75 ? 228 ARG B CA 1 ATOM 6117 C C . ARG B 1 228 ? 16.168 -4.283 40.952 1.00 8.39 ? 228 ARG B C 1 ATOM 6118 O O . ARG B 1 228 ? 16.320 -5.392 40.427 1.00 7.10 ? 228 ARG B O 1 ATOM 6119 C CB . ARG B 1 228 ? 18.671 -4.012 41.291 1.00 8.62 ? 228 ARG B CB 1 ATOM 6120 C CG . ARG B 1 228 ? 19.786 -3.475 42.188 1.00 6.49 ? 228 ARG B CG 1 ATOM 6121 C CD . ARG B 1 228 ? 21.123 -4.038 41.825 1.00 7.57 ? 228 ARG B CD 1 ATOM 6122 N NE . ARG B 1 228 ? 22.186 -3.476 42.649 1.00 8.05 ? 228 ARG B NE 1 ATOM 6123 C CZ . ARG B 1 228 ? 23.143 -2.661 42.208 1.00 10.31 ? 228 ARG B CZ 1 ATOM 6124 N NH1 . ARG B 1 228 ? 23.192 -2.288 40.930 1.00 8.73 ? 228 ARG B NH1 1 ATOM 6125 N NH2 . ARG B 1 228 ? 24.084 -2.246 43.047 1.00 8.56 ? 228 ARG B NH2 1 ATOM 6126 N N . ILE B 1 229 ? 15.041 -3.566 40.859 1.00 9.00 ? 229 ILE B N 1 ATOM 6127 C CA . ILE B 1 229 ? 13.849 -4.002 40.114 1.00 10.66 ? 229 ILE B CA 1 ATOM 6128 C C . ILE B 1 229 ? 13.941 -3.674 38.618 1.00 11.41 ? 229 ILE B C 1 ATOM 6129 O O . ILE B 1 229 ? 14.098 -2.518 38.235 1.00 11.48 ? 229 ILE B O 1 ATOM 6130 C CB . ILE B 1 229 ? 12.544 -3.357 40.697 1.00 10.87 ? 229 ILE B CB 1 ATOM 6131 C CG1 . ILE B 1 229 ? 12.470 -3.581 42.213 1.00 11.03 ? 229 ILE B CG1 1 ATOM 6132 C CG2 . ILE B 1 229 ? 11.284 -3.952 40.036 1.00 8.63 ? 229 ILE B CG2 1 ATOM 6133 C CD1 . ILE B 1 229 ? 11.420 -2.742 42.908 1.00 7.57 ? 229 ILE B CD1 1 ATOM 6134 N N . LEU B 1 230 ? 13.818 -4.706 37.790 1.00 12.84 ? 230 LEU B N 1 ATOM 6135 C CA . LEU B 1 230 ? 13.876 -4.557 36.338 1.00 14.61 ? 230 LEU B CA 1 ATOM 6136 C C . LEU B 1 230 ? 12.611 -5.068 35.675 1.00 16.10 ? 230 LEU B C 1 ATOM 6137 O O . LEU B 1 230 ? 11.929 -5.962 36.189 1.00 15.27 ? 230 LEU B O 1 ATOM 6138 C CB . LEU B 1 230 ? 15.028 -5.356 35.736 1.00 14.71 ? 230 LEU B CB 1 ATOM 6139 C CG . LEU B 1 230 ? 16.459 -5.358 36.241 1.00 17.17 ? 230 LEU B CG 1 ATOM 6140 C CD1 . LEU B 1 230 ? 16.655 -6.356 37.359 1.00 16.24 ? 230 LEU B CD1 1 ATOM 6141 C CD2 . LEU B 1 230 ? 17.335 -5.718 35.056 1.00 20.73 ? 230 LEU B CD2 1 ATOM 6142 N N . ASN B 1 231 ? 12.328 -4.510 34.505 1.00 16.99 ? 231 ASN B N 1 ATOM 6143 C CA . ASN B 1 231 ? 11.190 -4.924 33.717 1.00 17.56 ? 231 ASN B CA 1 ATOM 6144 C C . ASN B 1 231 ? 11.777 -5.474 32.420 1.00 18.02 ? 231 ASN B C 1 ATOM 6145 O O . ASN B 1 231 ? 12.079 -4.729 31.482 1.00 17.34 ? 231 ASN B O 1 ATOM 6146 C CB . ASN B 1 231 ? 10.232 -3.759 33.464 1.00 16.26 ? 231 ASN B CB 1 ATOM 6147 C CG . ASN B 1 231 ? 8.900 -4.217 32.907 1.00 14.72 ? 231 ASN B CG 1 ATOM 6148 O OD1 . ASN B 1 231 ? 8.722 -5.388 32.586 1.00 16.86 ? 231 ASN B OD1 1 ATOM 6149 N ND2 . ASN B 1 231 ? 7.957 -3.297 32.794 1.00 16.81 ? 231 ASN B ND2 1 ATOM 6150 N N . THR B 1 232 ? 11.925 -6.797 32.392 1.00 19.62 ? 232 THR B N 1 ATOM 6151 C CA . THR B 1 232 ? 12.512 -7.508 31.258 1.00 17.76 ? 232 THR B CA 1 ATOM 6152 C C . THR B 1 232 ? 11.512 -8.001 30.206 1.00 17.12 ? 232 THR B C 1 ATOM 6153 O O . THR B 1 232 ? 11.891 -8.643 29.211 1.00 17.68 ? 232 THR B O 1 ATOM 6154 C CB . THR B 1 232 ? 13.426 -8.674 31.757 1.00 18.88 ? 232 THR B CB 1 ATOM 6155 O OG1 . THR B 1 232 ? 12.665 -9.602 32.534 1.00 16.21 ? 232 THR B OG1 1 ATOM 6156 C CG2 . THR B 1 232 ? 14.573 -8.131 32.623 1.00 15.77 ? 232 THR B CG2 1 ATOM 6157 N N . SER B 1 233 ? 10.262 -7.577 30.384 1.00 14.58 ? 233 SER B N 1 ATOM 6158 C CA . SER B 1 233 ? 9.123 -7.929 29.537 1.00 13.78 ? 233 SER B CA 1 ATOM 6159 C C . SER B 1 233 ? 9.174 -7.651 28.036 1.00 13.21 ? 233 SER B C 1 ATOM 6160 O O . SER B 1 233 ? 10.044 -6.937 27.547 1.00 15.33 ? 233 SER B O 1 ATOM 6161 C CB . SER B 1 233 ? 7.881 -7.247 30.089 1.00 13.43 ? 233 SER B CB 1 ATOM 6162 O OG . SER B 1 233 ? 7.587 -7.709 31.388 1.00 17.01 ? 233 SER B OG 1 ATOM 6163 N N . THR B 1 234 ? 8.213 -8.228 27.323 1.00 12.13 ? 234 THR B N 1 ATOM 6164 C CA . THR B 1 234 ? 8.057 -8.033 25.885 1.00 11.88 ? 234 THR B CA 1 ATOM 6165 C C . THR B 1 234 ? 6.908 -7.055 25.617 1.00 11.28 ? 234 THR B C 1 ATOM 6166 O O . THR B 1 234 ? 6.920 -6.368 24.605 1.00 11.96 ? 234 THR B O 1 ATOM 6167 C CB . THR B 1 234 ? 7.748 -9.357 25.134 1.00 11.96 ? 234 THR B CB 1 ATOM 6168 O OG1 . THR B 1 234 ? 6.693 -10.072 25.794 1.00 7.53 ? 234 THR B OG1 1 ATOM 6169 C CG2 . THR B 1 234 ? 8.990 -10.211 25.017 1.00 9.14 ? 234 THR B CG2 1 ATOM 6170 N N . GLU B 1 235 ? 5.925 -7.010 26.523 1.00 11.40 ? 235 GLU B N 1 ATOM 6171 C CA . GLU B 1 235 ? 4.757 -6.122 26.393 1.00 12.79 ? 235 GLU B CA 1 ATOM 6172 C C . GLU B 1 235 ? 4.261 -5.519 27.716 1.00 10.06 ? 235 GLU B C 1 ATOM 6173 O O . GLU B 1 235 ? 4.004 -4.320 27.778 1.00 9.01 ? 235 GLU B O 1 ATOM 6174 C CB . GLU B 1 235 ? 3.591 -6.853 25.696 1.00 13.80 ? 235 GLU B CB 1 ATOM 6175 C CG . GLU B 1 235 ? 2.376 -5.982 25.271 1.00 17.65 ? 235 GLU B CG 1 ATOM 6176 C CD . GLU B 1 235 ? 1.318 -5.767 26.366 1.00 20.18 ? 235 GLU B CD 1 ATOM 6177 O OE1 . GLU B 1 235 ? 1.225 -6.613 27.281 1.00 20.04 ? 235 GLU B OE1 1 ATOM 6178 O OE2 . GLU B 1 235 ? 0.599 -4.739 26.321 1.00 20.17 ? 235 GLU B OE2 1 ATOM 6179 N N . ASN B 1 236 ? 4.038 -6.356 28.726 1.00 8.53 ? 236 ASN B N 1 ATOM 6180 C CA . ASN B 1 236 ? 3.516 -5.908 30.030 1.00 8.35 ? 236 ASN B CA 1 ATOM 6181 C C . ASN B 1 236 ? 4.242 -4.791 30.785 1.00 7.91 ? 236 ASN B C 1 ATOM 6182 O O . ASN B 1 236 ? 5.466 -4.832 30.953 1.00 9.53 ? 236 ASN B O 1 ATOM 6183 C CB . ASN B 1 236 ? 3.400 -7.085 30.983 1.00 6.15 ? 236 ASN B CB 1 ATOM 6184 C CG . ASN B 1 236 ? 2.183 -7.955 30.733 1.00 5.95 ? 236 ASN B CG 1 ATOM 6185 O OD1 . ASN B 1 236 ? 2.092 -9.035 31.293 1.00 6.27 ? 236 ASN B OD1 1 ATOM 6186 N ND2 . ASN B 1 236 ? 1.238 -7.485 29.939 1.00 6.17 ? 236 ASN B ND2 1 ATOM 6187 N N . HIS B 1 237 ? 3.482 -3.777 31.195 1.00 7.04 ? 237 HIS B N 1 ATOM 6188 C CA . HIS B 1 237 ? 4.018 -2.673 31.988 1.00 7.88 ? 237 HIS B CA 1 ATOM 6189 C C . HIS B 1 237 ? 3.477 -2.896 33.402 1.00 9.17 ? 237 HIS B C 1 ATOM 6190 O O . HIS B 1 237 ? 2.273 -3.082 33.610 1.00 8.29 ? 237 HIS B O 1 ATOM 6191 C CB . HIS B 1 237 ? 3.560 -1.334 31.464 1.00 7.24 ? 237 HIS B CB 1 ATOM 6192 C CG . HIS B 1 237 ? 4.032 -1.021 30.084 1.00 8.33 ? 237 HIS B CG 1 ATOM 6193 N ND1 . HIS B 1 237 ? 3.759 -1.829 29.002 1.00 7.21 ? 237 HIS B ND1 1 ATOM 6194 C CD2 . HIS B 1 237 ? 4.704 0.046 29.597 1.00 8.35 ? 237 HIS B CD2 1 ATOM 6195 C CE1 . HIS B 1 237 ? 4.242 -1.267 27.910 1.00 8.55 ? 237 HIS B CE1 1 ATOM 6196 N NE2 . HIS B 1 237 ? 4.822 -0.129 28.243 1.00 7.87 ? 237 HIS B NE2 1 ATOM 6197 N N . PHE B 1 238 ? 4.380 -2.847 34.369 1.00 9.44 ? 238 PHE B N 1 ATOM 6198 C CA . PHE B 1 238 ? 4.045 -3.139 35.746 1.00 9.31 ? 238 PHE B CA 1 ATOM 6199 C C . PHE B 1 238 ? 3.989 -2.034 36.756 1.00 9.65 ? 238 PHE B C 1 ATOM 6200 O O . PHE B 1 238 ? 4.722 -1.042 36.685 1.00 9.53 ? 238 PHE B O 1 ATOM 6201 C CB . PHE B 1 238 ? 5.035 -4.160 36.296 1.00 9.71 ? 238 PHE B CB 1 ATOM 6202 C CG . PHE B 1 238 ? 5.154 -5.400 35.480 1.00 8.13 ? 238 PHE B CG 1 ATOM 6203 C CD1 . PHE B 1 238 ? 4.020 -6.167 35.160 1.00 8.31 ? 238 PHE B CD1 1 ATOM 6204 C CD2 . PHE B 1 238 ? 6.413 -5.839 35.064 1.00 8.25 ? 238 PHE B CD2 1 ATOM 6205 C CE1 . PHE B 1 238 ? 4.141 -7.361 34.443 1.00 5.77 ? 238 PHE B CE1 1 ATOM 6206 C CE2 . PHE B 1 238 ? 6.552 -7.035 34.338 1.00 8.60 ? 238 PHE B CE2 1 ATOM 6207 C CZ . PHE B 1 238 ? 5.412 -7.801 34.028 1.00 8.50 ? 238 PHE B CZ 1 ATOM 6208 N N . GLN B 1 239 ? 3.127 -2.267 37.734 1.00 8.41 ? 239 GLN B N 1 ATOM 6209 C CA . GLN B 1 239 ? 2.973 -1.385 38.877 1.00 9.66 ? 239 GLN B CA 1 ATOM 6210 C C . GLN B 1 239 ? 3.403 -2.294 40.011 1.00 7.47 ? 239 GLN B C 1 ATOM 6211 O O . GLN B 1 239 ? 2.962 -3.441 40.098 1.00 5.28 ? 239 GLN B O 1 ATOM 6212 C CB . GLN B 1 239 ? 1.523 -0.935 39.072 1.00 11.07 ? 239 GLN B CB 1 ATOM 6213 C CG . GLN B 1 239 ? 1.049 0.111 38.081 1.00 5.84 ? 239 GLN B CG 1 ATOM 6214 C CD . GLN B 1 239 ? -0.390 0.572 38.305 1.00 10.16 ? 239 GLN B CD 1 ATOM 6215 O OE1 . GLN B 1 239 ? -0.800 1.594 37.750 1.00 9.83 ? 239 GLN B OE1 1 ATOM 6216 N NE2 . GLN B 1 239 ? -1.174 -0.192 39.081 1.00 7.09 ? 239 GLN B NE2 1 ATOM 6217 N N . VAL B 1 240 ? 4.396 -1.852 40.762 1.00 8.37 ? 240 VAL B N 1 ATOM 6218 C CA . VAL B 1 240 ? 4.884 -2.642 41.881 1.00 10.86 ? 240 VAL B CA 1 ATOM 6219 C C . VAL B 1 240 ? 4.708 -1.949 43.226 1.00 10.81 ? 240 VAL B C 1 ATOM 6220 O O . VAL B 1 240 ? 4.908 -0.738 43.341 1.00 11.56 ? 240 VAL B O 1 ATOM 6221 C CB . VAL B 1 240 ? 6.356 -3.096 41.692 1.00 10.58 ? 240 VAL B CB 1 ATOM 6222 C CG1 . VAL B 1 240 ? 6.460 -4.084 40.556 1.00 9.86 ? 240 VAL B CG1 1 ATOM 6223 C CG2 . VAL B 1 240 ? 7.278 -1.915 41.467 1.00 9.24 ? 240 VAL B CG2 1 ATOM 6224 N N . SER B 1 241 ? 4.333 -2.738 44.229 1.00 11.90 ? 241 SER B N 1 ATOM 6225 C CA . SER B 1 241 ? 4.124 -2.265 45.594 1.00 11.88 ? 241 SER B CA 1 ATOM 6226 C C . SER B 1 241 ? 4.435 -3.391 46.570 1.00 14.80 ? 241 SER B C 1 ATOM 6227 O O . SER B 1 241 ? 4.300 -4.565 46.218 1.00 14.29 ? 241 SER B O 1 ATOM 6228 C CB . SER B 1 241 ? 2.672 -1.808 45.801 1.00 11.78 ? 241 SER B CB 1 ATOM 6229 O OG . SER B 1 241 ? 1.746 -2.871 45.608 1.00 9.71 ? 241 SER B OG 1 ATOM 6230 N N . LEU B 1 242 ? 4.853 -3.010 47.781 1.00 13.98 ? 242 LEU B N 1 ATOM 6231 C CA . LEU B 1 242 ? 5.170 -3.936 48.859 1.00 15.60 ? 242 LEU B CA 1 ATOM 6232 C C . LEU B 1 242 ? 4.300 -3.545 50.042 1.00 15.68 ? 242 LEU B C 1 ATOM 6233 O O . LEU B 1 242 ? 4.351 -2.404 50.511 1.00 15.08 ? 242 LEU B O 1 ATOM 6234 C CB . LEU B 1 242 ? 6.662 -3.854 49.241 1.00 19.86 ? 242 LEU B CB 1 ATOM 6235 C CG . LEU B 1 242 ? 7.216 -4.726 50.384 1.00 17.82 ? 242 LEU B CG 1 ATOM 6236 C CD1 . LEU B 1 242 ? 6.999 -6.199 50.128 1.00 19.05 ? 242 LEU B CD1 1 ATOM 6237 C CD2 . LEU B 1 242 ? 8.686 -4.447 50.560 1.00 19.86 ? 242 LEU B CD2 1 ATOM 6238 N N . VAL B 1 243 ? 3.498 -4.503 50.499 1.00 16.03 ? 243 VAL B N 1 ATOM 6239 C CA . VAL B 1 243 ? 2.565 -4.338 51.622 1.00 18.50 ? 243 VAL B CA 1 ATOM 6240 C C . VAL B 1 243 ? 3.236 -3.787 52.895 1.00 19.20 ? 243 VAL B C 1 ATOM 6241 O O . VAL B 1 243 ? 4.274 -4.296 53.334 1.00 18.31 ? 243 VAL B O 1 ATOM 6242 C CB . VAL B 1 243 ? 1.827 -5.694 51.913 1.00 18.56 ? 243 VAL B CB 1 ATOM 6243 C CG1 . VAL B 1 243 ? 0.912 -5.607 53.144 1.00 15.94 ? 243 VAL B CG1 1 ATOM 6244 C CG2 . VAL B 1 243 ? 1.010 -6.103 50.701 1.00 16.80 ? 243 VAL B CG2 1 ATOM 6245 N N . ASN B 1 244 ? 2.651 -2.701 53.410 1.00 22.41 ? 244 ASN B N 1 ATOM 6246 C CA . ASN B 1 244 ? 3.081 -1.970 54.619 1.00 26.85 ? 244 ASN B CA 1 ATOM 6247 C C . ASN B 1 244 ? 4.494 -1.365 54.588 1.00 26.11 ? 244 ASN B C 1 ATOM 6248 O O . ASN B 1 244 ? 5.074 -1.034 55.633 1.00 22.98 ? 244 ASN B O 1 ATOM 6249 C CB . ASN B 1 244 ? 2.849 -2.813 55.895 1.00 31.82 ? 244 ASN B CB 1 ATOM 6250 C CG . ASN B 1 244 ? 1.367 -3.079 56.171 1.00 38.43 ? 244 ASN B CG 1 ATOM 6251 O OD1 . ASN B 1 244 ? 0.485 -2.454 55.575 1.00 39.32 ? 244 ASN B OD1 1 ATOM 6252 N ND2 . ASN B 1 244 ? 1.087 -4.023 57.066 1.00 44.92 ? 244 ASN B ND2 1 ATOM 6253 N N . HIS B 1 245 ? 5.030 -1.213 53.376 1.00 24.66 ? 245 HIS B N 1 ATOM 6254 C CA . HIS B 1 245 ? 6.359 -0.645 53.176 1.00 24.44 ? 245 HIS B CA 1 ATOM 6255 C C . HIS B 1 245 ? 6.398 0.379 52.054 1.00 23.58 ? 245 HIS B C 1 ATOM 6256 O O . HIS B 1 245 ? 5.621 0.322 51.089 1.00 22.57 ? 245 HIS B O 1 ATOM 6257 C CB . HIS B 1 245 ? 7.397 -1.712 52.821 1.00 25.28 ? 245 HIS B CB 1 ATOM 6258 C CG . HIS B 1 245 ? 7.769 -2.635 53.940 1.00 27.73 ? 245 HIS B CG 1 ATOM 6259 N ND1 . HIS B 1 245 ? 6.977 -3.695 54.324 1.00 28.25 ? 245 HIS B ND1 1 ATOM 6260 C CD2 . HIS B 1 245 ? 8.896 -2.718 54.687 1.00 27.92 ? 245 HIS B CD2 1 ATOM 6261 C CE1 . HIS B 1 245 ? 7.603 -4.394 55.254 1.00 27.71 ? 245 HIS B CE1 1 ATOM 6262 N NE2 . HIS B 1 245 ? 8.769 -3.822 55.491 1.00 28.13 ? 245 HIS B NE2 1 ATOM 6263 N N . THR B 1 246 ? 7.347 1.299 52.198 1.00 22.58 ? 246 THR B N 1 ATOM 6264 C CA . THR B 1 246 ? 7.615 2.340 51.223 1.00 21.55 ? 246 THR B CA 1 ATOM 6265 C C . THR B 1 246 ? 8.927 1.924 50.564 1.00 20.48 ? 246 THR B C 1 ATOM 6266 O O . THR B 1 246 ? 9.695 1.149 51.134 1.00 21.09 ? 246 THR B O 1 ATOM 6267 C CB . THR B 1 246 ? 7.810 3.733 51.881 1.00 21.77 ? 246 THR B CB 1 ATOM 6268 O OG1 . THR B 1 246 ? 8.916 3.700 52.794 1.00 22.39 ? 246 THR B OG1 1 ATOM 6269 C CG2 . THR B 1 246 ? 6.554 4.196 52.601 1.00 19.17 ? 246 THR B CG2 1 ATOM 6270 N N . MET B 1 247 ? 9.140 2.378 49.335 1.00 19.84 ? 247 MET B N 1 ATOM 6271 C CA . MET B 1 247 ? 10.357 2.078 48.587 1.00 18.24 ? 247 MET B CA 1 ATOM 6272 C C . MET B 1 247 ? 11.006 3.417 48.274 1.00 17.96 ? 247 MET B C 1 ATOM 6273 O O . MET B 1 247 ? 10.317 4.346 47.854 1.00 19.42 ? 247 MET B O 1 ATOM 6274 C CB . MET B 1 247 ? 10.022 1.353 47.280 1.00 18.06 ? 247 MET B CB 1 ATOM 6275 C CG . MET B 1 247 ? 9.249 0.052 47.447 1.00 18.42 ? 247 MET B CG 1 ATOM 6276 S SD . MET B 1 247 ? 8.933 -0.784 45.901 1.00 19.88 ? 247 MET B SD 1 ATOM 6277 C CE . MET B 1 247 ? 7.708 0.307 45.193 1.00 17.03 ? 247 MET B CE 1 ATOM 6278 N N . THR B 1 248 ? 12.309 3.537 48.523 1.00 18.70 ? 248 THR B N 1 ATOM 6279 C CA . THR B 1 248 ? 13.021 4.781 48.243 1.00 16.46 ? 248 THR B CA 1 ATOM 6280 C C . THR B 1 248 ? 13.902 4.622 47.012 1.00 16.42 ? 248 THR B C 1 ATOM 6281 O O . THR B 1 248 ? 14.920 3.923 47.048 1.00 16.92 ? 248 THR B O 1 ATOM 6282 C CB . THR B 1 248 ? 13.837 5.276 49.464 1.00 16.22 ? 248 THR B CB 1 ATOM 6283 O OG1 . THR B 1 248 ? 12.967 5.384 50.596 1.00 20.41 ? 248 THR B OG1 1 ATOM 6284 C CG2 . THR B 1 248 ? 14.439 6.662 49.195 1.00 15.73 ? 248 THR B CG2 1 ATOM 6285 N N . VAL B 1 249 ? 13.508 5.302 45.936 1.00 14.54 ? 249 VAL B N 1 ATOM 6286 C CA . VAL B 1 249 ? 14.232 5.262 44.667 1.00 13.88 ? 249 VAL B CA 1 ATOM 6287 C C . VAL B 1 249 ? 15.564 6.003 44.754 1.00 13.70 ? 249 VAL B C 1 ATOM 6288 O O . VAL B 1 249 ? 15.611 7.174 45.140 1.00 13.15 ? 249 VAL B O 1 ATOM 6289 C CB . VAL B 1 249 ? 13.398 5.883 43.509 1.00 12.72 ? 249 VAL B CB 1 ATOM 6290 C CG1 . VAL B 1 249 ? 14.092 5.683 42.177 1.00 11.85 ? 249 VAL B CG1 1 ATOM 6291 C CG2 . VAL B 1 249 ? 12.010 5.290 43.472 1.00 12.26 ? 249 VAL B CG2 1 ATOM 6292 N N . ILE B 1 250 ? 16.643 5.276 44.465 1.00 12.94 ? 250 ILE B N 1 ATOM 6293 C CA . ILE B 1 250 ? 17.979 5.851 44.453 1.00 13.52 ? 250 ILE B CA 1 ATOM 6294 C C . ILE B 1 250 ? 18.545 5.894 43.040 1.00 12.17 ? 250 ILE B C 1 ATOM 6295 O O . ILE B 1 250 ? 19.576 6.520 42.811 1.00 13.73 ? 250 ILE B O 1 ATOM 6296 C CB . ILE B 1 250 ? 18.956 5.149 45.421 1.00 14.74 ? 250 ILE B CB 1 ATOM 6297 C CG1 . ILE B 1 250 ? 19.132 3.673 45.074 1.00 14.86 ? 250 ILE B CG1 1 ATOM 6298 C CG2 . ILE B 1 250 ? 18.460 5.326 46.825 1.00 16.14 ? 250 ILE B CG2 1 ATOM 6299 C CD1 . ILE B 1 250 ? 20.399 3.069 45.610 1.00 15.81 ? 250 ILE B CD1 1 ATOM 6300 N N . ALA B 1 251 ? 17.842 5.254 42.103 1.00 10.99 ? 251 ALA B N 1 ATOM 6301 C CA . ALA B 1 251 ? 18.220 5.209 40.685 1.00 10.22 ? 251 ALA B CA 1 ATOM 6302 C C . ALA B 1 251 ? 17.058 4.851 39.768 1.00 11.88 ? 251 ALA B C 1 ATOM 6303 O O . ALA B 1 251 ? 16.219 4.008 40.096 1.00 13.19 ? 251 ALA B O 1 ATOM 6304 C CB . ALA B 1 251 ? 19.367 4.238 40.452 1.00 9.07 ? 251 ALA B CB 1 ATOM 6305 N N . ALA B 1 252 ? 17.013 5.540 38.632 1.00 14.41 ? 252 ALA B N 1 ATOM 6306 C CA . ALA B 1 252 ? 16.018 5.343 37.576 1.00 15.14 ? 252 ALA B CA 1 ATOM 6307 C C . ALA B 1 252 ? 16.895 4.939 36.400 1.00 16.34 ? 252 ALA B C 1 ATOM 6308 O O . ALA B 1 252 ? 17.789 5.703 35.994 1.00 16.96 ? 252 ALA B O 1 ATOM 6309 C CB . ALA B 1 252 ? 15.275 6.652 37.286 1.00 15.43 ? 252 ALA B CB 1 ATOM 6310 N N . ASP B 1 253 ? 16.667 3.725 35.889 1.00 15.49 ? 253 ASP B N 1 ATOM 6311 C CA . ASP B 1 253 ? 17.472 3.119 34.817 1.00 15.39 ? 253 ASP B CA 1 ATOM 6312 C C . ASP B 1 253 ? 18.932 3.082 35.305 1.00 13.44 ? 253 ASP B C 1 ATOM 6313 O O . ASP B 1 253 ? 19.164 2.649 36.428 1.00 13.16 ? 253 ASP B O 1 ATOM 6314 C CB . ASP B 1 253 ? 17.270 3.801 33.446 1.00 16.29 ? 253 ASP B CB 1 ATOM 6315 C CG . ASP B 1 253 ? 15.869 3.571 32.874 1.00 19.51 ? 253 ASP B CG 1 ATOM 6316 O OD1 . ASP B 1 253 ? 15.067 2.839 33.501 1.00 19.69 ? 253 ASP B OD1 1 ATOM 6317 O OD2 . ASP B 1 253 ? 15.558 4.141 31.803 1.00 18.03 ? 253 ASP B OD2 1 ATOM 6318 N N . MET B 1 254 ? 19.893 3.595 34.545 1.00 12.89 ? 254 MET B N 1 ATOM 6319 C CA . MET B 1 254 ? 21.274 3.573 35.018 1.00 13.82 ? 254 MET B CA 1 ATOM 6320 C C . MET B 1 254 ? 21.758 4.949 35.437 1.00 12.77 ? 254 MET B C 1 ATOM 6321 O O . MET B 1 254 ? 22.957 5.210 35.505 1.00 14.03 ? 254 MET B O 1 ATOM 6322 C CB . MET B 1 254 ? 22.197 2.948 33.981 1.00 16.01 ? 254 MET B CB 1 ATOM 6323 C CG . MET B 1 254 ? 22.717 1.591 34.388 1.00 16.63 ? 254 MET B CG 1 ATOM 6324 S SD . MET B 1 254 ? 24.053 1.051 33.320 1.00 22.58 ? 254 MET B SD 1 ATOM 6325 C CE . MET B 1 254 ? 24.863 -0.016 34.356 1.00 17.76 ? 254 MET B CE 1 ATOM 6326 N N . VAL B 1 255 ? 20.801 5.816 35.756 1.00 13.02 ? 255 VAL B N 1 ATOM 6327 C CA . VAL B 1 255 ? 21.064 7.190 36.174 1.00 11.88 ? 255 VAL B CA 1 ATOM 6328 C C . VAL B 1 255 ? 20.676 7.379 37.651 1.00 14.16 ? 255 VAL B C 1 ATOM 6329 O O . VAL B 1 255 ? 19.486 7.366 37.983 1.00 15.83 ? 255 VAL B O 1 ATOM 6330 C CB . VAL B 1 255 ? 20.248 8.187 35.306 1.00 11.85 ? 255 VAL B CB 1 ATOM 6331 C CG1 . VAL B 1 255 ? 20.506 9.624 35.732 1.00 12.91 ? 255 VAL B CG1 1 ATOM 6332 C CG2 . VAL B 1 255 ? 20.564 7.999 33.824 1.00 9.69 ? 255 VAL B CG2 1 ATOM 6333 N N . PRO B 1 256 ? 21.673 7.541 38.558 1.00 15.61 ? 256 PRO B N 1 ATOM 6334 C CA . PRO B 1 256 ? 21.389 7.737 39.989 1.00 15.49 ? 256 PRO B CA 1 ATOM 6335 C C . PRO B 1 256 ? 20.626 9.037 40.235 1.00 15.87 ? 256 PRO B C 1 ATOM 6336 O O . PRO B 1 256 ? 21.017 10.097 39.738 1.00 15.91 ? 256 PRO B O 1 ATOM 6337 C CB . PRO B 1 256 ? 22.783 7.797 40.610 1.00 14.95 ? 256 PRO B CB 1 ATOM 6338 C CG . PRO B 1 256 ? 23.583 6.959 39.709 1.00 15.90 ? 256 PRO B CG 1 ATOM 6339 C CD . PRO B 1 256 ? 23.127 7.396 38.352 1.00 13.54 ? 256 PRO B CD 1 ATOM 6340 N N . VAL B 1 257 ? 19.489 8.918 40.916 1.00 16.61 ? 257 VAL B N 1 ATOM 6341 C CA . VAL B 1 257 ? 18.643 10.062 41.235 1.00 17.14 ? 257 VAL B CA 1 ATOM 6342 C C . VAL B 1 257 ? 18.647 10.389 42.724 1.00 17.91 ? 257 VAL B C 1 ATOM 6343 O O . VAL B 1 257 ? 19.142 9.594 43.530 1.00 18.83 ? 257 VAL B O 1 ATOM 6344 C CB . VAL B 1 257 ? 17.164 9.874 40.726 1.00 16.92 ? 257 VAL B CB 1 ATOM 6345 C CG1 . VAL B 1 257 ? 17.140 9.729 39.201 1.00 18.02 ? 257 VAL B CG1 1 ATOM 6346 C CG2 . VAL B 1 257 ? 16.469 8.684 41.402 1.00 16.10 ? 257 VAL B CG2 1 ATOM 6347 N N . ASN B 1 258 ? 18.106 11.561 43.079 1.00 17.07 ? 258 ASN B N 1 ATOM 6348 C CA . ASN B 1 258 ? 17.997 11.984 44.485 1.00 16.44 ? 258 ASN B CA 1 ATOM 6349 C C . ASN B 1 258 ? 16.937 11.094 45.129 1.00 15.97 ? 258 ASN B C 1 ATOM 6350 O O . ASN B 1 258 ? 16.018 10.638 44.435 1.00 15.66 ? 258 ASN B O 1 ATOM 6351 C CB . ASN B 1 258 ? 17.556 13.452 44.602 1.00 14.09 ? 258 ASN B CB 1 ATOM 6352 C CG . ASN B 1 258 ? 18.604 14.431 44.107 1.00 13.32 ? 258 ASN B CG 1 ATOM 6353 O OD1 . ASN B 1 258 ? 19.805 14.254 44.311 1.00 9.85 ? 258 ASN B OD1 1 ATOM 6354 N ND2 . ASN B 1 258 ? 18.143 15.487 43.457 1.00 17.09 ? 258 ASN B ND2 1 ATOM 6355 N N . ALA B 1 259 ? 17.071 10.853 46.435 1.00 15.45 ? 259 ALA B N 1 ATOM 6356 C CA . ALA B 1 259 ? 16.149 10.007 47.204 1.00 15.88 ? 259 ALA B CA 1 ATOM 6357 C C . ALA B 1 259 ? 14.694 10.424 47.047 1.00 16.16 ? 259 ALA B C 1 ATOM 6358 O O . ALA B 1 259 ? 14.351 11.587 47.257 1.00 18.17 ? 259 ALA B O 1 ATOM 6359 C CB . ALA B 1 259 ? 16.541 10.004 48.683 1.00 17.64 ? 259 ALA B CB 1 ATOM 6360 N N . MET B 1 260 ? 13.873 9.481 46.588 1.00 16.42 ? 260 MET B N 1 ATOM 6361 C CA . MET B 1 260 ? 12.448 9.714 46.372 1.00 16.59 ? 260 MET B CA 1 ATOM 6362 C C . MET B 1 260 ? 11.636 8.532 46.892 1.00 16.51 ? 260 MET B C 1 ATOM 6363 O O . MET B 1 260 ? 11.507 7.487 46.232 1.00 16.15 ? 260 MET B O 1 ATOM 6364 C CB . MET B 1 260 ? 12.157 9.958 44.883 1.00 16.74 ? 260 MET B CB 1 ATOM 6365 C CG . MET B 1 260 ? 10.802 10.611 44.601 1.00 18.51 ? 260 MET B CG 1 ATOM 6366 S SD . MET B 1 260 ? 10.497 10.826 42.831 1.00 21.38 ? 260 MET B SD 1 ATOM 6367 C CE . MET B 1 260 ? 9.751 9.289 42.442 1.00 14.68 ? 260 MET B CE 1 ATOM 6368 N N . THR B 1 261 ? 11.082 8.730 48.083 1.00 15.38 ? 261 THR B N 1 ATOM 6369 C CA . THR B 1 261 ? 10.261 7.742 48.768 1.00 14.46 ? 261 THR B CA 1 ATOM 6370 C C . THR B 1 261 ? 8.819 7.736 48.219 1.00 15.35 ? 261 THR B C 1 ATOM 6371 O O . THR B 1 261 ? 8.136 8.770 48.221 1.00 15.56 ? 261 THR B O 1 ATOM 6372 C CB . THR B 1 261 ? 10.310 8.006 50.296 1.00 14.66 ? 261 THR B CB 1 ATOM 6373 O OG1 . THR B 1 261 ? 11.678 8.002 50.727 1.00 11.85 ? 261 THR B OG1 1 ATOM 6374 C CG2 . THR B 1 261 ? 9.556 6.950 51.064 1.00 11.28 ? 261 THR B CG2 1 ATOM 6375 N N . VAL B 1 262 ? 8.408 6.571 47.702 1.00 15.36 ? 262 VAL B N 1 ATOM 6376 C CA . VAL B 1 262 ? 7.076 6.336 47.106 1.00 16.48 ? 262 VAL B CA 1 ATOM 6377 C C . VAL B 1 262 ? 6.423 5.061 47.666 1.00 16.67 ? 262 VAL B C 1 ATOM 6378 O O . VAL B 1 262 ? 7.117 4.204 48.221 1.00 16.68 ? 262 VAL B O 1 ATOM 6379 C CB . VAL B 1 262 ? 7.151 6.194 45.525 1.00 16.15 ? 262 VAL B CB 1 ATOM 6380 C CG1 . VAL B 1 262 ? 7.562 7.498 44.884 1.00 15.47 ? 262 VAL B CG1 1 ATOM 6381 C CG2 . VAL B 1 262 ? 8.125 5.095 45.111 1.00 13.43 ? 262 VAL B CG2 1 ATOM 6382 N N . ASP B 1 263 ? 5.106 4.933 47.486 1.00 17.17 ? 263 ASP B N 1 ATOM 6383 C CA . ASP B 1 263 ? 4.343 3.759 47.944 1.00 19.73 ? 263 ASP B CA 1 ATOM 6384 C C . ASP B 1 263 ? 4.321 2.688 46.858 1.00 21.17 ? 263 ASP B C 1 ATOM 6385 O O . ASP B 1 263 ? 4.167 1.492 47.144 1.00 21.27 ? 263 ASP B O 1 ATOM 6386 C CB . ASP B 1 263 ? 2.889 4.128 48.270 1.00 19.64 ? 263 ASP B CB 1 ATOM 6387 C CG . ASP B 1 263 ? 2.747 4.886 49.577 1.00 25.72 ? 263 ASP B CG 1 ATOM 6388 O OD1 . ASP B 1 263 ? 3.191 4.373 50.636 1.00 27.14 ? 263 ASP B OD1 1 ATOM 6389 O OD2 . ASP B 1 263 ? 2.164 5.993 49.547 1.00 26.80 ? 263 ASP B OD2 1 ATOM 6390 N N . SER B 1 264 ? 4.423 3.148 45.610 1.00 21.55 ? 264 SER B N 1 ATOM 6391 C CA . SER B 1 264 ? 4.400 2.290 44.435 1.00 22.08 ? 264 SER B CA 1 ATOM 6392 C C . SER B 1 264 ? 5.215 2.859 43.280 1.00 21.94 ? 264 SER B C 1 ATOM 6393 O O . SER B 1 264 ? 5.410 4.074 43.178 1.00 22.56 ? 264 SER B O 1 ATOM 6394 C CB . SER B 1 264 ? 2.954 2.029 43.981 1.00 22.79 ? 264 SER B CB 1 ATOM 6395 O OG . SER B 1 264 ? 2.251 3.239 43.742 1.00 25.27 ? 264 SER B OG 1 ATOM 6396 N N . LEU B 1 265 ? 5.683 1.963 42.413 1.00 20.30 ? 265 LEU B N 1 ATOM 6397 C CA . LEU B 1 265 ? 6.482 2.331 41.247 1.00 18.21 ? 265 LEU B CA 1 ATOM 6398 C C . LEU B 1 265 ? 5.973 1.768 39.950 1.00 16.40 ? 265 LEU B C 1 ATOM 6399 O O . LEU B 1 265 ? 5.573 0.610 39.883 1.00 19.05 ? 265 LEU B O 1 ATOM 6400 C CB . LEU B 1 265 ? 7.915 1.847 41.404 1.00 17.18 ? 265 LEU B CB 1 ATOM 6401 C CG . LEU B 1 265 ? 8.900 2.764 42.099 1.00 19.01 ? 265 LEU B CG 1 ATOM 6402 C CD1 . LEU B 1 265 ? 10.162 1.992 42.325 1.00 17.80 ? 265 LEU B CD1 1 ATOM 6403 C CD2 . LEU B 1 265 ? 9.136 4.022 41.276 1.00 15.90 ? 265 LEU B CD2 1 ATOM 6404 N N . PHE B 1 266 ? 5.993 2.596 38.915 1.00 15.51 ? 266 PHE B N 1 ATOM 6405 C CA . PHE B 1 266 ? 5.587 2.156 37.592 1.00 12.54 ? 266 PHE B CA 1 ATOM 6406 C C . PHE B 1 266 ? 6.839 1.817 36.810 1.00 12.08 ? 266 PHE B C 1 ATOM 6407 O O . PHE B 1 266 ? 7.739 2.652 36.675 1.00 12.26 ? 266 PHE B O 1 ATOM 6408 C CB . PHE B 1 266 ? 4.795 3.227 36.831 1.00 10.06 ? 266 PHE B CB 1 ATOM 6409 C CG . PHE B 1 266 ? 4.376 2.797 35.445 1.00 5.34 ? 266 PHE B CG 1 ATOM 6410 C CD1 . PHE B 1 266 ? 3.321 1.882 35.270 1.00 7.14 ? 266 PHE B CD1 1 ATOM 6411 C CD2 . PHE B 1 266 ? 5.076 3.251 34.309 1.00 5.32 ? 266 PHE B CD2 1 ATOM 6412 C CE1 . PHE B 1 266 ? 2.969 1.418 33.969 1.00 6.92 ? 266 PHE B CE1 1 ATOM 6413 C CE2 . PHE B 1 266 ? 4.745 2.804 33.009 1.00 6.26 ? 266 PHE B CE2 1 ATOM 6414 C CZ . PHE B 1 266 ? 3.692 1.886 32.836 1.00 3.29 ? 266 PHE B CZ 1 ATOM 6415 N N . LEU B 1 267 ? 6.862 0.600 36.274 1.00 11.61 ? 267 LEU B N 1 ATOM 6416 C CA . LEU B 1 267 ? 7.965 0.129 35.452 1.00 12.18 ? 267 LEU B CA 1 ATOM 6417 C C . LEU B 1 267 ? 7.464 -0.169 34.056 1.00 12.99 ? 267 LEU B C 1 ATOM 6418 O O . LEU B 1 267 ? 6.583 -1.009 33.872 1.00 13.85 ? 267 LEU B O 1 ATOM 6419 C CB . LEU B 1 267 ? 8.605 -1.136 36.025 1.00 10.05 ? 267 LEU B CB 1 ATOM 6420 C CG . LEU B 1 267 ? 9.664 -0.864 37.087 1.00 13.01 ? 267 LEU B CG 1 ATOM 6421 C CD1 . LEU B 1 267 ? 9.041 -0.944 38.461 1.00 9.15 ? 267 LEU B CD1 1 ATOM 6422 C CD2 . LEU B 1 267 ? 10.835 -1.819 36.952 1.00 10.37 ? 267 LEU B CD2 1 ATOM 6423 N N . ALA B 1 268 ? 7.976 0.577 33.085 1.00 12.93 ? 268 ALA B N 1 ATOM 6424 C CA . ALA B 1 268 ? 7.636 0.350 31.688 1.00 11.90 ? 268 ALA B CA 1 ATOM 6425 C C . ALA B 1 268 ? 8.574 -0.727 31.182 1.00 12.63 ? 268 ALA B C 1 ATOM 6426 O O . ALA B 1 268 ? 9.577 -1.036 31.836 1.00 13.30 ? 268 ALA B O 1 ATOM 6427 C CB . ALA B 1 268 ? 7.813 1.616 30.872 1.00 11.23 ? 268 ALA B CB 1 ATOM 6428 N N . VAL B 1 269 ? 8.238 -1.321 30.039 1.00 14.43 ? 269 VAL B N 1 ATOM 6429 C CA . VAL B 1 269 ? 9.066 -2.356 29.413 1.00 13.93 ? 269 VAL B CA 1 ATOM 6430 C C . VAL B 1 269 ? 10.464 -1.782 29.160 1.00 13.10 ? 269 VAL B C 1 ATOM 6431 O O . VAL B 1 269 ? 10.613 -0.790 28.447 1.00 11.28 ? 269 VAL B O 1 ATOM 6432 C CB . VAL B 1 269 ? 8.424 -2.857 28.089 1.00 14.02 ? 269 VAL B CB 1 ATOM 6433 C CG1 . VAL B 1 269 ? 9.331 -3.843 27.349 1.00 12.43 ? 269 VAL B CG1 1 ATOM 6434 C CG2 . VAL B 1 269 ? 7.133 -3.521 28.402 1.00 12.82 ? 269 VAL B CG2 1 ATOM 6435 N N . GLY B 1 270 ? 11.442 -2.354 29.863 1.00 14.22 ? 270 GLY B N 1 ATOM 6436 C CA . GLY B 1 270 ? 12.823 -1.923 29.738 1.00 14.34 ? 270 GLY B CA 1 ATOM 6437 C C . GLY B 1 270 ? 13.338 -1.062 30.874 1.00 14.26 ? 270 GLY B C 1 ATOM 6438 O O . GLY B 1 270 ? 14.544 -0.877 30.997 1.00 14.65 ? 270 GLY B O 1 ATOM 6439 N N . GLN B 1 271 ? 12.426 -0.526 31.686 1.00 16.03 ? 271 GLN B N 1 ATOM 6440 C CA . GLN B 1 271 ? 12.775 0.336 32.818 1.00 16.33 ? 271 GLN B CA 1 ATOM 6441 C C . GLN B 1 271 ? 13.280 -0.407 34.039 1.00 17.42 ? 271 GLN B C 1 ATOM 6442 O O . GLN B 1 271 ? 12.867 -1.537 34.321 1.00 18.02 ? 271 GLN B O 1 ATOM 6443 C CB . GLN B 1 271 ? 11.592 1.221 33.235 1.00 15.36 ? 271 GLN B CB 1 ATOM 6444 C CG . GLN B 1 271 ? 11.291 2.345 32.271 1.00 13.56 ? 271 GLN B CG 1 ATOM 6445 C CD . GLN B 1 271 ? 10.358 3.404 32.833 1.00 13.18 ? 271 GLN B CD 1 ATOM 6446 O OE1 . GLN B 1 271 ? 9.385 3.102 33.528 1.00 12.13 ? 271 GLN B OE1 1 ATOM 6447 N NE2 . GLN B 1 271 ? 10.637 4.662 32.499 1.00 13.00 ? 271 GLN B NE2 1 ATOM 6448 N N . ARG B 1 272 ? 14.233 0.224 34.716 1.00 17.07 ? 272 ARG B N 1 ATOM 6449 C CA . ARG B 1 272 ? 14.819 -0.319 35.930 1.00 15.78 ? 272 ARG B CA 1 ATOM 6450 C C . ARG B 1 272 ? 14.649 0.693 37.048 1.00 13.81 ? 272 ARG B C 1 ATOM 6451 O O . ARG B 1 272 ? 14.493 1.892 36.801 1.00 11.24 ? 272 ARG B O 1 ATOM 6452 C CB . ARG B 1 272 ? 16.314 -0.604 35.760 1.00 18.38 ? 272 ARG B CB 1 ATOM 6453 C CG . ARG B 1 272 ? 16.671 -1.791 34.907 1.00 20.07 ? 272 ARG B CG 1 ATOM 6454 C CD . ARG B 1 272 ? 16.827 -1.438 33.454 1.00 21.30 ? 272 ARG B CD 1 ATOM 6455 N NE . ARG B 1 272 ? 18.034 -0.660 33.211 1.00 20.12 ? 272 ARG B NE 1 ATOM 6456 C CZ . ARG B 1 272 ? 18.170 0.218 32.227 1.00 21.58 ? 272 ARG B CZ 1 ATOM 6457 N NH1 . ARG B 1 272 ? 17.169 0.443 31.386 1.00 22.27 ? 272 ARG B NH1 1 ATOM 6458 N NH2 . ARG B 1 272 ? 19.311 0.876 32.087 1.00 22.92 ? 272 ARG B NH2 1 ATOM 6459 N N . TYR B 1 273 ? 14.685 0.202 38.280 1.00 14.09 ? 273 TYR B N 1 ATOM 6460 C CA . TYR B 1 273 ? 14.566 1.055 39.458 1.00 14.72 ? 273 TYR B CA 1 ATOM 6461 C C . TYR B 1 273 ? 15.300 0.429 40.622 1.00 14.56 ? 273 TYR B C 1 ATOM 6462 O O . TYR B 1 273 ? 15.018 -0.706 40.999 1.00 14.00 ? 273 TYR B O 1 ATOM 6463 C CB . TYR B 1 273 ? 13.097 1.303 39.846 1.00 14.85 ? 273 TYR B CB 1 ATOM 6464 C CG . TYR B 1 273 ? 12.396 2.466 39.143 1.00 14.36 ? 273 TYR B CG 1 ATOM 6465 C CD1 . TYR B 1 273 ? 12.911 3.782 39.194 1.00 15.18 ? 273 TYR B CD1 1 ATOM 6466 C CD2 . TYR B 1 273 ? 11.190 2.263 38.459 1.00 15.19 ? 273 TYR B CD2 1 ATOM 6467 C CE1 . TYR B 1 273 ? 12.225 4.872 38.573 1.00 13.73 ? 273 TYR B CE1 1 ATOM 6468 C CE2 . TYR B 1 273 ? 10.494 3.338 37.833 1.00 15.14 ? 273 TYR B CE2 1 ATOM 6469 C CZ . TYR B 1 273 ? 11.019 4.634 37.895 1.00 15.60 ? 273 TYR B CZ 1 ATOM 6470 O OH . TYR B 1 273 ? 10.350 5.661 37.263 1.00 13.45 ? 273 TYR B OH 1 ATOM 6471 N N . ASP B 1 274 ? 16.320 1.133 41.110 1.00 16.38 ? 274 ASP B N 1 ATOM 6472 C CA . ASP B 1 274 ? 17.084 0.689 42.269 1.00 16.50 ? 274 ASP B CA 1 ATOM 6473 C C . ASP B 1 274 ? 16.427 1.331 43.482 1.00 16.68 ? 274 ASP B C 1 ATOM 6474 O O . ASP B 1 274 ? 16.308 2.555 43.555 1.00 16.62 ? 274 ASP B O 1 ATOM 6475 C CB . ASP B 1 274 ? 18.552 1.105 42.172 1.00 19.55 ? 274 ASP B CB 1 ATOM 6476 C CG . ASP B 1 274 ? 19.316 0.342 41.103 1.00 21.86 ? 274 ASP B CG 1 ATOM 6477 O OD1 . ASP B 1 274 ? 18.773 -0.625 40.542 1.00 25.54 ? 274 ASP B OD1 1 ATOM 6478 O OD2 . ASP B 1 274 ? 20.476 0.702 40.821 1.00 24.29 ? 274 ASP B OD2 1 ATOM 6479 N N . VAL B 1 275 ? 15.899 0.498 44.373 1.00 16.27 ? 275 VAL B N 1 ATOM 6480 C CA . VAL B 1 275 ? 15.224 0.990 45.568 1.00 16.39 ? 275 VAL B CA 1 ATOM 6481 C C . VAL B 1 275 ? 15.855 0.571 46.890 1.00 17.39 ? 275 VAL B C 1 ATOM 6482 O O . VAL B 1 275 ? 16.523 -0.451 46.960 1.00 17.35 ? 275 VAL B O 1 ATOM 6483 C CB . VAL B 1 275 ? 13.712 0.596 45.590 1.00 16.50 ? 275 VAL B CB 1 ATOM 6484 C CG1 . VAL B 1 275 ? 13.004 1.169 44.403 1.00 17.38 ? 275 VAL B CG1 1 ATOM 6485 C CG2 . VAL B 1 275 ? 13.518 -0.905 45.624 1.00 14.85 ? 275 VAL B CG2 1 ATOM 6486 N N . VAL B 1 276 ? 15.662 1.399 47.917 1.00 18.52 ? 276 VAL B N 1 ATOM 6487 C CA . VAL B 1 276 ? 16.137 1.113 49.269 1.00 20.24 ? 276 VAL B CA 1 ATOM 6488 C C . VAL B 1 276 ? 14.879 0.838 50.091 1.00 20.96 ? 276 VAL B C 1 ATOM 6489 O O . VAL B 1 276 ? 13.967 1.668 50.145 1.00 21.05 ? 276 VAL B O 1 ATOM 6490 C CB . VAL B 1 276 ? 16.987 2.282 49.885 1.00 20.98 ? 276 VAL B CB 1 ATOM 6491 C CG1 . VAL B 1 276 ? 17.217 2.074 51.386 1.00 20.61 ? 276 VAL B CG1 1 ATOM 6492 C CG2 . VAL B 1 276 ? 18.355 2.355 49.210 1.00 20.73 ? 276 VAL B CG2 1 ATOM 6493 N N . ILE B 1 277 ? 14.799 -0.383 50.618 1.00 21.66 ? 277 ILE B N 1 ATOM 6494 C CA . ILE B 1 277 ? 13.681 -0.832 51.437 1.00 22.98 ? 277 ILE B CA 1 ATOM 6495 C C . ILE B 1 277 ? 14.164 -1.097 52.877 1.00 25.50 ? 277 ILE B C 1 ATOM 6496 O O . ILE B 1 277 ? 15.007 -1.965 53.117 1.00 26.68 ? 277 ILE B O 1 ATOM 6497 C CB . ILE B 1 277 ? 12.998 -2.096 50.808 1.00 22.02 ? 277 ILE B CB 1 ATOM 6498 C CG1 . ILE B 1 277 ? 12.317 -1.712 49.481 1.00 22.69 ? 277 ILE B CG1 1 ATOM 6499 C CG2 . ILE B 1 277 ? 11.973 -2.717 51.777 1.00 22.77 ? 277 ILE B CG2 1 ATOM 6500 C CD1 . ILE B 1 277 ? 11.693 -2.855 48.692 1.00 19.79 ? 277 ILE B CD1 1 ATOM 6501 N N . ASP B 1 278 ? 13.631 -0.319 53.816 1.00 28.16 ? 278 ASP B N 1 ATOM 6502 C CA . ASP B 1 278 ? 13.962 -0.442 55.236 1.00 30.59 ? 278 ASP B CA 1 ATOM 6503 C C . ASP B 1 278 ? 13.072 -1.490 55.879 1.00 30.90 ? 278 ASP B C 1 ATOM 6504 O O . ASP B 1 278 ? 11.840 -1.369 55.857 1.00 29.50 ? 278 ASP B O 1 ATOM 6505 C CB . ASP B 1 278 ? 13.760 0.891 55.978 1.00 32.88 ? 278 ASP B CB 1 ATOM 6506 C CG . ASP B 1 278 ? 14.743 1.976 55.552 1.00 35.99 ? 278 ASP B CG 1 ATOM 6507 O OD1 . ASP B 1 278 ? 15.601 1.735 54.674 1.00 39.96 ? 278 ASP B OD1 1 ATOM 6508 O OD2 . ASP B 1 278 ? 14.651 3.091 56.106 1.00 37.25 ? 278 ASP B OD2 1 ATOM 6509 N N . ALA B 1 279 ? 13.697 -2.518 56.453 1.00 32.11 ? 279 ALA B N 1 ATOM 6510 C CA . ALA B 1 279 ? 12.969 -3.587 57.137 1.00 34.47 ? 279 ALA B CA 1 ATOM 6511 C C . ALA B 1 279 ? 12.596 -3.059 58.534 1.00 35.40 ? 279 ALA B C 1 ATOM 6512 O O . ALA B 1 279 ? 13.003 -3.594 59.571 1.00 34.30 ? 279 ALA B O 1 ATOM 6513 C CB . ALA B 1 279 ? 13.822 -4.833 57.221 1.00 33.98 ? 279 ALA B CB 1 ATOM 6514 N N . SER B 1 280 ? 11.791 -1.996 58.498 1.00 36.84 ? 280 SER B N 1 ATOM 6515 C CA . SER B 1 280 ? 11.313 -1.245 59.648 1.00 37.51 ? 280 SER B CA 1 ATOM 6516 C C . SER B 1 280 ? 10.019 -1.714 60.305 1.00 37.88 ? 280 SER B C 1 ATOM 6517 O O . SER B 1 280 ? 9.674 -1.238 61.391 1.00 37.76 ? 280 SER B O 1 ATOM 6518 C CB . SER B 1 280 ? 11.159 0.222 59.236 1.00 38.75 ? 280 SER B CB 1 ATOM 6519 O OG . SER B 1 280 ? 10.225 0.358 58.172 1.00 42.07 ? 280 SER B OG 1 ATOM 6520 N N . ARG B 1 281 ? 9.296 -2.619 59.645 1.00 37.93 ? 281 ARG B N 1 ATOM 6521 C CA . ARG B 1 281 ? 8.025 -3.121 60.172 1.00 37.05 ? 281 ARG B CA 1 ATOM 6522 C C . ARG B 1 281 ? 8.136 -4.412 60.989 1.00 35.59 ? 281 ARG B C 1 ATOM 6523 O O . ARG B 1 281 ? 9.237 -4.918 61.223 1.00 32.93 ? 281 ARG B O 1 ATOM 6524 C CB . ARG B 1 281 ? 7.000 -3.264 59.039 1.00 39.29 ? 281 ARG B CB 1 ATOM 6525 C CG . ARG B 1 281 ? 6.760 -1.976 58.246 1.00 42.76 ? 281 ARG B CG 1 ATOM 6526 C CD . ARG B 1 281 ? 6.058 -0.882 59.052 1.00 44.71 ? 281 ARG B CD 1 ATOM 6527 N NE . ARG B 1 281 ? 4.649 -1.193 59.306 1.00 47.50 ? 281 ARG B NE 1 ATOM 6528 C CZ . ARG B 1 281 ? 3.644 -0.324 59.191 1.00 48.64 ? 281 ARG B CZ 1 ATOM 6529 N NH1 . ARG B 1 281 ? 3.869 0.933 58.822 1.00 49.68 ? 281 ARG B NH1 1 ATOM 6530 N NH2 . ARG B 1 281 ? 2.402 -0.716 59.446 1.00 49.13 ? 281 ARG B NH2 1 ATOM 6531 N N . ALA B 1 282 ? 6.983 -4.908 61.444 1.00 35.94 ? 282 ALA B N 1 ATOM 6532 C CA . ALA B 1 282 ? 6.871 -6.119 62.265 1.00 36.48 ? 282 ALA B CA 1 ATOM 6533 C C . ALA B 1 282 ? 7.323 -7.414 61.575 1.00 36.59 ? 282 ALA B C 1 ATOM 6534 O O . ALA B 1 282 ? 7.124 -7.567 60.368 1.00 35.58 ? 282 ALA B O 1 ATOM 6535 C CB . ALA B 1 282 ? 5.434 -6.268 62.771 1.00 36.49 ? 282 ALA B CB 1 ATOM 6536 N N . PRO B 1 283 ? 8.028 -8.315 62.314 1.00 37.53 ? 283 PRO B N 1 ATOM 6537 C CA . PRO B 1 283 ? 8.507 -9.598 61.776 1.00 36.90 ? 283 PRO B CA 1 ATOM 6538 C C . PRO B 1 283 ? 7.361 -10.467 61.247 1.00 35.55 ? 283 PRO B C 1 ATOM 6539 O O . PRO B 1 283 ? 6.636 -11.120 62.007 1.00 35.68 ? 283 PRO B O 1 ATOM 6540 C CB . PRO B 1 283 ? 9.210 -10.225 62.979 1.00 36.79 ? 283 PRO B CB 1 ATOM 6541 C CG . PRO B 1 283 ? 9.814 -9.040 63.628 1.00 37.33 ? 283 PRO B CG 1 ATOM 6542 C CD . PRO B 1 283 ? 8.662 -8.063 63.627 1.00 37.55 ? 283 PRO B CD 1 ATOM 6543 N N . ASP B 1 284 ? 7.198 -10.414 59.926 1.00 33.67 ? 284 ASP B N 1 ATOM 6544 C CA . ASP B 1 284 ? 6.147 -11.126 59.210 1.00 32.20 ? 284 ASP B CA 1 ATOM 6545 C C . ASP B 1 284 ? 6.530 -11.238 57.730 1.00 30.80 ? 284 ASP B C 1 ATOM 6546 O O . ASP B 1 284 ? 7.587 -10.769 57.294 1.00 31.41 ? 284 ASP B O 1 ATOM 6547 C CB . ASP B 1 284 ? 4.827 -10.333 59.357 1.00 32.38 ? 284 ASP B CB 1 ATOM 6548 C CG . ASP B 1 284 ? 3.587 -11.135 58.977 1.00 32.30 ? 284 ASP B CG 1 ATOM 6549 O OD1 . ASP B 1 284 ? 3.643 -12.384 58.957 1.00 33.23 ? 284 ASP B OD1 1 ATOM 6550 O OD2 . ASP B 1 284 ? 2.549 -10.498 58.699 1.00 31.88 ? 284 ASP B OD2 1 ATOM 6551 N N . ASN B 1 285 ? 5.673 -11.916 56.978 1.00 29.20 ? 285 ASN B N 1 ATOM 6552 C CA . ASN B 1 285 ? 5.840 -12.095 55.545 1.00 27.22 ? 285 ASN B CA 1 ATOM 6553 C C . ASN B 1 285 ? 4.915 -11.080 54.896 1.00 25.79 ? 285 ASN B C 1 ATOM 6554 O O . ASN B 1 285 ? 3.758 -10.943 55.302 1.00 27.45 ? 285 ASN B O 1 ATOM 6555 C CB . ASN B 1 285 ? 5.435 -13.508 55.138 1.00 25.08 ? 285 ASN B CB 1 ATOM 6556 C CG . ASN B 1 285 ? 6.310 -14.560 55.755 1.00 24.94 ? 285 ASN B CG 1 ATOM 6557 O OD1 . ASN B 1 285 ? 7.500 -14.602 55.497 1.00 22.47 ? 285 ASN B OD1 1 ATOM 6558 N ND2 . ASN B 1 285 ? 5.724 -15.417 56.583 1.00 26.43 ? 285 ASN B ND2 1 ATOM 6559 N N . TYR B 1 286 ? 5.433 -10.330 53.932 1.00 24.37 ? 286 TYR B N 1 ATOM 6560 C CA . TYR B 1 286 ? 4.639 -9.314 53.242 1.00 23.59 ? 286 TYR B CA 1 ATOM 6561 C C . TYR B 1 286 ? 4.639 -9.548 51.732 1.00 21.60 ? 286 TYR B C 1 ATOM 6562 O O . TYR B 1 286 ? 5.667 -9.922 51.156 1.00 20.29 ? 286 TYR B O 1 ATOM 6563 C CB . TYR B 1 286 ? 5.176 -7.911 53.556 1.00 26.87 ? 286 TYR B CB 1 ATOM 6564 C CG . TYR B 1 286 ? 5.072 -7.499 55.011 1.00 30.68 ? 286 TYR B CG 1 ATOM 6565 C CD1 . TYR B 1 286 ? 3.940 -6.807 55.491 1.00 32.05 ? 286 TYR B CD1 1 ATOM 6566 C CD2 . TYR B 1 286 ? 6.114 -7.782 55.920 1.00 32.07 ? 286 TYR B CD2 1 ATOM 6567 C CE1 . TYR B 1 286 ? 3.846 -6.398 56.856 1.00 35.02 ? 286 TYR B CE1 1 ATOM 6568 C CE2 . TYR B 1 286 ? 6.032 -7.378 57.284 1.00 34.37 ? 286 TYR B CE2 1 ATOM 6569 C CZ . TYR B 1 286 ? 4.899 -6.688 57.739 1.00 33.80 ? 286 TYR B CZ 1 ATOM 6570 O OH . TYR B 1 286 ? 4.831 -6.279 59.048 1.00 33.19 ? 286 TYR B OH 1 ATOM 6571 N N . TRP B 1 287 ? 3.481 -9.341 51.101 1.00 19.23 ? 287 TRP B N 1 ATOM 6572 C CA . TRP B 1 287 ? 3.339 -9.520 49.649 1.00 16.47 ? 287 TRP B CA 1 ATOM 6573 C C . TRP B 1 287 ? 3.945 -8.368 48.861 1.00 14.80 ? 287 TRP B C 1 ATOM 6574 O O . TRP B 1 287 ? 3.833 -7.210 49.258 1.00 16.24 ? 287 TRP B O 1 ATOM 6575 C CB . TRP B 1 287 ? 1.865 -9.599 49.205 1.00 13.30 ? 287 TRP B CB 1 ATOM 6576 C CG . TRP B 1 287 ? 1.031 -10.827 49.530 1.00 10.80 ? 287 TRP B CG 1 ATOM 6577 C CD1 . TRP B 1 287 ? -0.162 -10.827 50.188 1.00 8.73 ? 287 TRP B CD1 1 ATOM 6578 C CD2 . TRP B 1 287 ? 1.261 -12.191 49.124 1.00 10.18 ? 287 TRP B CD2 1 ATOM 6579 N NE1 . TRP B 1 287 ? -0.699 -12.087 50.220 1.00 10.45 ? 287 TRP B NE1 1 ATOM 6580 C CE2 . TRP B 1 287 ? 0.145 -12.951 49.581 1.00 10.07 ? 287 TRP B CE2 1 ATOM 6581 C CE3 . TRP B 1 287 ? 2.295 -12.852 48.419 1.00 9.92 ? 287 TRP B CE3 1 ATOM 6582 C CZ2 . TRP B 1 287 ? 0.026 -14.346 49.358 1.00 10.78 ? 287 TRP B CZ2 1 ATOM 6583 C CZ3 . TRP B 1 287 ? 2.183 -14.249 48.190 1.00 9.14 ? 287 TRP B CZ3 1 ATOM 6584 C CH2 . TRP B 1 287 ? 1.049 -14.976 48.662 1.00 10.83 ? 287 TRP B CH2 1 ATOM 6585 N N . PHE B 1 288 ? 4.610 -8.713 47.764 1.00 16.17 ? 288 PHE B N 1 ATOM 6586 C CA . PHE B 1 288 ? 5.181 -7.742 46.827 1.00 16.89 ? 288 PHE B CA 1 ATOM 6587 C C . PHE B 1 288 ? 4.234 -7.934 45.660 1.00 15.67 ? 288 PHE B C 1 ATOM 6588 O O . PHE B 1 288 ? 4.239 -8.995 45.030 1.00 16.88 ? 288 PHE B O 1 ATOM 6589 C CB . PHE B 1 288 ? 6.606 -8.127 46.412 1.00 18.38 ? 288 PHE B CB 1 ATOM 6590 C CG . PHE B 1 288 ? 7.288 -7.113 45.514 1.00 19.49 ? 288 PHE B CG 1 ATOM 6591 C CD1 . PHE B 1 288 ? 7.355 -7.320 44.117 1.00 20.35 ? 288 PHE B CD1 1 ATOM 6592 C CD2 . PHE B 1 288 ? 7.887 -5.959 46.061 1.00 18.56 ? 288 PHE B CD2 1 ATOM 6593 C CE1 . PHE B 1 288 ? 8.015 -6.389 43.277 1.00 20.81 ? 288 PHE B CE1 1 ATOM 6594 C CE2 . PHE B 1 288 ? 8.554 -5.016 45.237 1.00 20.12 ? 288 PHE B CE2 1 ATOM 6595 C CZ . PHE B 1 288 ? 8.621 -5.231 43.838 1.00 21.28 ? 288 PHE B CZ 1 ATOM 6596 N N . ASN B 1 289 ? 3.399 -6.936 45.394 1.00 14.76 ? 289 ASN B N 1 ATOM 6597 C CA . ASN B 1 289 ? 2.421 -7.058 44.318 1.00 12.14 ? 289 ASN B CA 1 ATOM 6598 C C . ASN B 1 289 ? 2.729 -6.388 43.005 1.00 11.65 ? 289 ASN B C 1 ATOM 6599 O O . ASN B 1 289 ? 3.277 -5.284 42.953 1.00 8.46 ? 289 ASN B O 1 ATOM 6600 C CB . ASN B 1 289 ? 1.041 -6.625 44.792 1.00 11.26 ? 289 ASN B CB 1 ATOM 6601 C CG . ASN B 1 289 ? 0.487 -7.543 45.832 1.00 13.94 ? 289 ASN B CG 1 ATOM 6602 O OD1 . ASN B 1 289 ? 0.663 -7.313 47.031 1.00 14.16 ? 289 ASN B OD1 1 ATOM 6603 N ND2 . ASN B 1 289 ? -0.171 -8.601 45.363 1.00 17.45 ? 289 ASN B ND2 1 ATOM 6604 N N . VAL B 1 290 ? 2.358 -7.104 41.945 1.00 12.06 ? 290 VAL B N 1 ATOM 6605 C CA . VAL B 1 290 ? 2.501 -6.662 40.570 1.00 9.04 ? 290 VAL B CA 1 ATOM 6606 C C . VAL B 1 290 ? 1.059 -6.452 40.099 1.00 10.11 ? 290 VAL B C 1 ATOM 6607 O O . VAL B 1 290 ? 0.309 -7.413 39.929 1.00 11.17 ? 290 VAL B O 1 ATOM 6608 C CB . VAL B 1 290 ? 3.235 -7.726 39.712 1.00 10.13 ? 290 VAL B CB 1 ATOM 6609 C CG1 . VAL B 1 290 ? 3.130 -7.402 38.244 1.00 9.63 ? 290 VAL B CG1 1 ATOM 6610 C CG2 . VAL B 1 290 ? 4.704 -7.809 40.110 1.00 10.33 ? 290 VAL B CG2 1 ATOM 6611 N N . THR B 1 291 ? 0.653 -5.189 40.003 1.00 9.91 ? 291 THR B N 1 ATOM 6612 C CA . THR B 1 291 ? -0.695 -4.836 39.555 1.00 11.30 ? 291 THR B CA 1 ATOM 6613 C C . THR B 1 291 ? -0.688 -4.203 38.167 1.00 11.77 ? 291 THR B C 1 ATOM 6614 O O . THR B 1 291 ? 0.373 -4.028 37.561 1.00 12.34 ? 291 THR B O 1 ATOM 6615 C CB . THR B 1 291 ? -1.403 -3.883 40.540 1.00 9.60 ? 291 THR B CB 1 ATOM 6616 O OG1 . THR B 1 291 ? -0.520 -2.822 40.909 1.00 10.85 ? 291 THR B OG1 1 ATOM 6617 C CG2 . THR B 1 291 ? -1.852 -4.626 41.771 1.00 12.28 ? 291 THR B CG2 1 ATOM 6618 N N . PHE B 1 292 ? -1.887 -3.946 37.644 1.00 13.23 ? 292 PHE B N 1 ATOM 6619 C CA . PHE B 1 292 ? -2.072 -3.321 36.335 1.00 14.67 ? 292 PHE B CA 1 ATOM 6620 C C . PHE B 1 292 ? -3.058 -2.170 36.389 1.00 15.44 ? 292 PHE B C 1 ATOM 6621 O O . PHE B 1 292 ? -4.218 -2.323 36.803 1.00 15.50 ? 292 PHE B O 1 ATOM 6622 C CB . PHE B 1 292 ? -2.538 -4.332 35.273 1.00 13.78 ? 292 PHE B CB 1 ATOM 6623 C CG . PHE B 1 292 ? -1.489 -5.311 34.877 1.00 14.88 ? 292 PHE B CG 1 ATOM 6624 C CD1 . PHE B 1 292 ? -0.483 -4.950 33.966 1.00 18.08 ? 292 PHE B CD1 1 ATOM 6625 C CD2 . PHE B 1 292 ? -1.467 -6.589 35.449 1.00 15.95 ? 292 PHE B CD2 1 ATOM 6626 C CE1 . PHE B 1 292 ? 0.548 -5.856 33.628 1.00 18.42 ? 292 PHE B CE1 1 ATOM 6627 C CE2 . PHE B 1 292 ? -0.448 -7.509 35.129 1.00 17.19 ? 292 PHE B CE2 1 ATOM 6628 C CZ . PHE B 1 292 ? 0.562 -7.147 34.217 1.00 18.91 ? 292 PHE B CZ 1 ATOM 6629 N N . GLY B 1 293 ? -2.560 -1.012 35.981 1.00 16.26 ? 293 GLY B N 1 ATOM 6630 C CA . GLY B 1 293 ? -3.369 0.179 35.914 1.00 18.65 ? 293 GLY B CA 1 ATOM 6631 C C . GLY B 1 293 ? -3.353 0.609 34.464 1.00 21.34 ? 293 GLY B C 1 ATOM 6632 O O . GLY B 1 293 ? -2.727 -0.052 33.623 1.00 21.05 ? 293 GLY B O 1 ATOM 6633 N N . GLY B 1 294 ? -4.013 1.729 34.178 1.00 23.36 ? 294 GLY B N 1 ATOM 6634 C CA . GLY B 1 294 ? -4.077 2.254 32.824 1.00 25.24 ? 294 GLY B CA 1 ATOM 6635 C C . GLY B 1 294 ? -5.234 1.702 32.029 1.00 26.94 ? 294 GLY B C 1 ATOM 6636 O O . GLY B 1 294 ? -5.448 2.094 30.883 1.00 28.24 ? 294 GLY B O 1 ATOM 6637 N N . GLN B 1 295 ? -6.001 0.825 32.678 1.00 27.74 ? 295 GLN B N 1 ATOM 6638 C CA . GLN B 1 295 ? -7.168 0.144 32.118 1.00 27.80 ? 295 GLN B CA 1 ATOM 6639 C C . GLN B 1 295 ? -6.812 -0.674 30.867 1.00 26.15 ? 295 GLN B C 1 ATOM 6640 O O . GLN B 1 295 ? -7.353 -0.459 29.773 1.00 27.09 ? 295 GLN B O 1 ATOM 6641 C CB . GLN B 1 295 ? -8.336 1.125 31.886 1.00 31.29 ? 295 GLN B CB 1 ATOM 6642 C CG . GLN B 1 295 ? -8.781 1.978 33.111 1.00 37.38 ? 295 GLN B CG 1 ATOM 6643 C CD . GLN B 1 295 ? -9.337 1.176 34.291 1.00 40.24 ? 295 GLN B CD 1 ATOM 6644 O OE1 . GLN B 1 295 ? -10.556 1.104 34.487 1.00 43.05 ? 295 GLN B OE1 1 ATOM 6645 N NE2 . GLN B 1 295 ? -8.443 0.619 35.114 1.00 41.21 ? 295 GLN B NE2 1 ATOM 6646 N N . ALA B 1 296 ? -5.838 -1.574 31.063 1.00 23.67 ? 296 ALA B N 1 ATOM 6647 C CA . ALA B 1 296 ? -5.278 -2.492 30.052 1.00 21.34 ? 296 ALA B CA 1 ATOM 6648 C C . ALA B 1 296 ? -4.650 -1.847 28.820 1.00 19.85 ? 296 ALA B C 1 ATOM 6649 O O . ALA B 1 296 ? -4.396 -2.523 27.821 1.00 21.17 ? 296 ALA B O 1 ATOM 6650 C CB . ALA B 1 296 ? -6.303 -3.555 29.632 1.00 20.08 ? 296 ALA B CB 1 ATOM 6651 N N . ALA B 1 297 ? -4.355 -0.552 28.916 1.00 18.44 ? 297 ALA B N 1 ATOM 6652 C CA . ALA B 1 297 ? -3.756 0.193 27.820 1.00 16.63 ? 297 ALA B CA 1 ATOM 6653 C C . ALA B 1 297 ? -2.291 -0.154 27.609 1.00 16.46 ? 297 ALA B C 1 ATOM 6654 O O . ALA B 1 297 ? -1.754 0.037 26.519 1.00 16.63 ? 297 ALA B O 1 ATOM 6655 C CB . ALA B 1 297 ? -3.917 1.655 28.049 1.00 17.05 ? 297 ALA B CB 1 ATOM 6656 N N . CYS B 1 298 ? -1.666 -0.703 28.642 1.00 15.03 ? 298 CYS B N 1 ATOM 6657 C CA . CYS B 1 298 ? -0.263 -1.091 28.566 1.00 14.98 ? 298 CYS B CA 1 ATOM 6658 C C . CYS B 1 298 ? -0.004 -2.491 29.134 1.00 14.67 ? 298 CYS B C 1 ATOM 6659 O O . CYS B 1 298 ? 1.039 -2.751 29.752 1.00 16.14 ? 298 CYS B O 1 ATOM 6660 C CB . CYS B 1 298 ? 0.618 -0.037 29.237 1.00 12.68 ? 298 CYS B CB 1 ATOM 6661 S SG . CYS B 1 298 ? 0.194 0.322 30.970 1.00 13.41 ? 298 CYS B SG 1 ATOM 6662 N N . GLY B 1 299 ? -0.971 -3.383 28.927 1.00 13.57 ? 299 GLY B N 1 ATOM 6663 C CA . GLY B 1 299 ? -0.828 -4.751 29.387 1.00 12.44 ? 299 GLY B CA 1 ATOM 6664 C C . GLY B 1 299 ? -1.750 -5.266 30.467 1.00 12.57 ? 299 GLY B C 1 ATOM 6665 O O . GLY B 1 299 ? -2.532 -4.531 31.072 1.00 10.03 ? 299 GLY B O 1 ATOM 6666 N N . GLY B 1 300 ? -1.622 -6.569 30.694 1.00 13.84 ? 300 GLY B N 1 ATOM 6667 C CA . GLY B 1 300 ? -2.398 -7.272 31.693 1.00 14.07 ? 300 GLY B CA 1 ATOM 6668 C C . GLY B 1 300 ? -1.922 -8.702 31.760 1.00 15.25 ? 300 GLY B C 1 ATOM 6669 O O . GLY B 1 300 ? -1.141 -9.136 30.913 1.00 17.64 ? 300 GLY B O 1 ATOM 6670 N N . SER B 1 301 ? -2.413 -9.440 32.751 1.00 17.26 ? 301 SER B N 1 ATOM 6671 C CA . SER B 1 301 ? -2.047 -10.838 32.934 1.00 17.75 ? 301 SER B CA 1 ATOM 6672 C C . SER B 1 301 ? -3.247 -11.665 33.316 1.00 17.09 ? 301 SER B C 1 ATOM 6673 O O . SER B 1 301 ? -4.137 -11.180 34.016 1.00 20.25 ? 301 SER B O 1 ATOM 6674 C CB . SER B 1 301 ? -0.987 -10.989 34.021 1.00 17.30 ? 301 SER B CB 1 ATOM 6675 O OG . SER B 1 301 ? -0.398 -12.278 33.976 1.00 16.31 ? 301 SER B OG 1 ATOM 6676 N N . LEU B 1 302 ? -3.238 -12.927 32.884 1.00 16.88 ? 302 LEU B N 1 ATOM 6677 C CA . LEU B 1 302 ? -4.306 -13.873 33.190 1.00 15.56 ? 302 LEU B CA 1 ATOM 6678 C C . LEU B 1 302 ? -4.171 -14.353 34.633 1.00 15.39 ? 302 LEU B C 1 ATOM 6679 O O . LEU B 1 302 ? -5.104 -14.920 35.195 1.00 15.01 ? 302 LEU B O 1 ATOM 6680 C CB . LEU B 1 302 ? -4.324 -15.030 32.196 1.00 14.74 ? 302 LEU B CB 1 ATOM 6681 C CG . LEU B 1 302 ? -4.684 -14.654 30.752 1.00 14.93 ? 302 LEU B CG 1 ATOM 6682 C CD1 . LEU B 1 302 ? -4.633 -15.885 29.881 1.00 13.65 ? 302 LEU B CD1 1 ATOM 6683 C CD2 . LEU B 1 302 ? -6.057 -13.969 30.669 1.00 14.63 ? 302 LEU B CD2 1 ATOM 6684 N N . ASN B 1 303 ? -2.993 -14.106 35.214 1.00 15.36 ? 303 ASN B N 1 ATOM 6685 C CA . ASN B 1 303 ? -2.721 -14.391 36.619 1.00 12.61 ? 303 ASN B CA 1 ATOM 6686 C C . ASN B 1 303 ? -3.262 -13.086 37.210 1.00 11.56 ? 303 ASN B C 1 ATOM 6687 O O . ASN B 1 303 ? -2.735 -12.003 36.927 1.00 9.61 ? 303 ASN B O 1 ATOM 6688 C CB . ASN B 1 303 ? -1.217 -14.557 36.898 1.00 12.69 ? 303 ASN B CB 1 ATOM 6689 C CG . ASN B 1 303 ? -0.908 -14.829 38.387 1.00 13.35 ? 303 ASN B CG 1 ATOM 6690 O OD1 . ASN B 1 303 ? -1.765 -14.683 39.249 1.00 12.61 ? 303 ASN B OD1 1 ATOM 6691 N ND2 . ASN B 1 303 ? 0.332 -15.197 38.679 1.00 15.12 ? 303 ASN B ND2 1 ATOM 6692 N N . PRO B 1 304 ? -4.364 -13.171 37.983 1.00 11.67 ? 304 PRO B N 1 ATOM 6693 C CA . PRO B 1 304 ? -4.937 -11.955 38.557 1.00 11.73 ? 304 PRO B CA 1 ATOM 6694 C C . PRO B 1 304 ? -4.133 -11.262 39.652 1.00 12.23 ? 304 PRO B C 1 ATOM 6695 O O . PRO B 1 304 ? -4.212 -10.040 39.794 1.00 13.49 ? 304 PRO B O 1 ATOM 6696 C CB . PRO B 1 304 ? -6.317 -12.418 39.011 1.00 9.65 ? 304 PRO B CB 1 ATOM 6697 C CG . PRO B 1 304 ? -6.082 -13.821 39.417 1.00 12.48 ? 304 PRO B CG 1 ATOM 6698 C CD . PRO B 1 304 ? -5.156 -14.358 38.363 1.00 10.26 ? 304 PRO B CD 1 ATOM 6699 N N . HIS B 1 305 ? -3.345 -12.033 40.404 1.00 11.81 ? 305 HIS B N 1 ATOM 6700 C CA . HIS B 1 305 ? -2.536 -11.478 41.496 1.00 13.25 ? 305 HIS B CA 1 ATOM 6701 C C . HIS B 1 305 ? -1.099 -12.020 41.491 1.00 13.20 ? 305 HIS B C 1 ATOM 6702 O O . HIS B 1 305 ? -0.755 -12.873 42.313 1.00 14.34 ? 305 HIS B O 1 ATOM 6703 C CB . HIS B 1 305 ? -3.201 -11.744 42.868 1.00 14.83 ? 305 HIS B CB 1 ATOM 6704 C CG . HIS B 1 305 ? -4.649 -11.367 42.932 1.00 16.07 ? 305 HIS B CG 1 ATOM 6705 N ND1 . HIS B 1 305 ? -5.083 -10.061 42.839 1.00 19.54 ? 305 HIS B ND1 1 ATOM 6706 C CD2 . HIS B 1 305 ? -5.765 -12.129 43.005 1.00 18.70 ? 305 HIS B CD2 1 ATOM 6707 C CE1 . HIS B 1 305 ? -6.404 -10.036 42.847 1.00 20.05 ? 305 HIS B CE1 1 ATOM 6708 N NE2 . HIS B 1 305 ? -6.843 -11.279 42.946 1.00 21.14 ? 305 HIS B NE2 1 ATOM 6709 N N . PRO B 1 306 ? -0.247 -11.569 40.536 1.00 14.21 ? 306 PRO B N 1 ATOM 6710 C CA . PRO B 1 306 ? 1.142 -12.053 40.495 1.00 14.84 ? 306 PRO B CA 1 ATOM 6711 C C . PRO B 1 306 ? 1.857 -11.420 41.665 1.00 14.73 ? 306 PRO B C 1 ATOM 6712 O O . PRO B 1 306 ? 1.820 -10.200 41.826 1.00 14.84 ? 306 PRO B O 1 ATOM 6713 C CB . PRO B 1 306 ? 1.669 -11.487 39.180 1.00 14.73 ? 306 PRO B CB 1 ATOM 6714 C CG . PRO B 1 306 ? 0.438 -11.194 38.382 1.00 16.73 ? 306 PRO B CG 1 ATOM 6715 C CD . PRO B 1 306 ? -0.491 -10.657 39.405 1.00 15.14 ? 306 PRO B CD 1 ATOM 6716 N N . ALA B 1 307 ? 2.435 -12.255 42.519 1.00 17.12 ? 307 ALA B N 1 ATOM 6717 C CA . ALA B 1 307 ? 3.106 -11.764 43.707 1.00 15.09 ? 307 ALA B CA 1 ATOM 6718 C C . ALA B 1 307 ? 4.367 -12.514 44.082 1.00 16.07 ? 307 ALA B C 1 ATOM 6719 O O . ALA B 1 307 ? 4.661 -13.580 43.533 1.00 15.74 ? 307 ALA B O 1 ATOM 6720 C CB . ALA B 1 307 ? 2.129 -11.766 44.875 1.00 16.87 ? 307 ALA B CB 1 ATOM 6721 N N . ALA B 1 308 ? 5.139 -11.885 44.967 1.00 16.96 ? 308 ALA B N 1 ATOM 6722 C CA . ALA B 1 308 ? 6.387 -12.416 45.515 1.00 17.56 ? 308 ALA B CA 1 ATOM 6723 C C . ALA B 1 308 ? 6.295 -12.248 47.028 1.00 18.42 ? 308 ALA B C 1 ATOM 6724 O O . ALA B 1 308 ? 5.532 -11.411 47.516 1.00 18.33 ? 308 ALA B O 1 ATOM 6725 C CB . ALA B 1 308 ? 7.579 -11.639 44.979 1.00 17.03 ? 308 ALA B CB 1 ATOM 6726 N N . ILE B 1 309 ? 7.045 -13.061 47.770 1.00 20.09 ? 309 ILE B N 1 ATOM 6727 C CA . ILE B 1 309 ? 7.036 -12.989 49.236 1.00 19.82 ? 309 ILE B CA 1 ATOM 6728 C C . ILE B 1 309 ? 8.318 -12.355 49.740 1.00 19.75 ? 309 ILE B C 1 ATOM 6729 O O . ILE B 1 309 ? 9.417 -12.686 49.287 1.00 21.47 ? 309 ILE B O 1 ATOM 6730 C CB . ILE B 1 309 ? 6.919 -14.399 49.913 1.00 20.08 ? 309 ILE B CB 1 ATOM 6731 C CG1 . ILE B 1 309 ? 5.678 -15.141 49.421 1.00 20.51 ? 309 ILE B CG1 1 ATOM 6732 C CG2 . ILE B 1 309 ? 6.849 -14.266 51.454 1.00 20.89 ? 309 ILE B CG2 1 ATOM 6733 C CD1 . ILE B 1 309 ? 5.603 -16.606 49.863 1.00 22.51 ? 309 ILE B CD1 1 ATOM 6734 N N . PHE B 1 310 ? 8.153 -11.407 50.652 1.00 19.46 ? 310 PHE B N 1 ATOM 6735 C CA . PHE B 1 310 ? 9.272 -10.754 51.300 1.00 19.33 ? 310 PHE B CA 1 ATOM 6736 C C . PHE B 1 310 ? 9.176 -11.256 52.736 1.00 20.55 ? 310 PHE B C 1 ATOM 6737 O O . PHE B 1 310 ? 8.197 -10.997 53.456 1.00 17.01 ? 310 PHE B O 1 ATOM 6738 C CB . PHE B 1 310 ? 9.183 -9.226 51.189 1.00 19.11 ? 310 PHE B CB 1 ATOM 6739 C CG . PHE B 1 310 ? 9.863 -8.659 49.957 1.00 19.88 ? 310 PHE B CG 1 ATOM 6740 C CD1 . PHE B 1 310 ? 9.459 -9.038 48.663 1.00 17.93 ? 310 PHE B CD1 1 ATOM 6741 C CD2 . PHE B 1 310 ? 10.913 -7.734 50.085 1.00 21.54 ? 310 PHE B CD2 1 ATOM 6742 C CE1 . PHE B 1 310 ? 10.094 -8.503 47.513 1.00 18.51 ? 310 PHE B CE1 1 ATOM 6743 C CE2 . PHE B 1 310 ? 11.562 -7.184 48.938 1.00 20.47 ? 310 PHE B CE2 1 ATOM 6744 C CZ . PHE B 1 310 ? 11.144 -7.576 47.650 1.00 18.26 ? 310 PHE B CZ 1 ATOM 6745 N N . HIS B 1 311 ? 10.152 -12.087 53.084 1.00 21.58 ? 311 HIS B N 1 ATOM 6746 C CA . HIS B 1 311 ? 10.233 -12.716 54.393 1.00 23.30 ? 311 HIS B CA 1 ATOM 6747 C C . HIS B 1 311 ? 11.247 -12.045 55.311 1.00 23.69 ? 311 HIS B C 1 ATOM 6748 O O . HIS B 1 311 ? 12.372 -11.780 54.911 1.00 23.40 ? 311 HIS B O 1 ATOM 6749 C CB . HIS B 1 311 ? 10.570 -14.207 54.196 1.00 23.62 ? 311 HIS B CB 1 ATOM 6750 C CG . HIS B 1 311 ? 10.874 -14.951 55.460 1.00 25.34 ? 311 HIS B CG 1 ATOM 6751 N ND1 . HIS B 1 311 ? 12.145 -15.374 55.777 1.00 25.69 ? 311 HIS B ND1 1 ATOM 6752 C CD2 . HIS B 1 311 ? 10.077 -15.359 56.476 1.00 24.98 ? 311 HIS B CD2 1 ATOM 6753 C CE1 . HIS B 1 311 ? 12.116 -16.015 56.930 1.00 27.26 ? 311 HIS B CE1 1 ATOM 6754 N NE2 . HIS B 1 311 ? 10.873 -16.019 57.377 1.00 25.88 ? 311 HIS B NE2 1 ATOM 6755 N N . TYR B 1 312 ? 10.826 -11.779 56.546 1.00 24.18 ? 312 TYR B N 1 ATOM 6756 C CA . TYR B 1 312 ? 11.709 -11.196 57.550 1.00 25.05 ? 312 TYR B CA 1 ATOM 6757 C C . TYR B 1 312 ? 12.445 -12.350 58.203 1.00 25.02 ? 312 TYR B C 1 ATOM 6758 O O . TYR B 1 312 ? 11.827 -13.361 58.531 1.00 26.01 ? 312 TYR B O 1 ATOM 6759 C CB . TYR B 1 312 ? 10.914 -10.458 58.616 1.00 24.54 ? 312 TYR B CB 1 ATOM 6760 C CG . TYR B 1 312 ? 10.676 -8.996 58.350 1.00 24.40 ? 312 TYR B CG 1 ATOM 6761 C CD1 . TYR B 1 312 ? 9.885 -8.568 57.262 1.00 22.34 ? 312 TYR B CD1 1 ATOM 6762 C CD2 . TYR B 1 312 ? 11.186 -8.020 59.232 1.00 22.98 ? 312 TYR B CD2 1 ATOM 6763 C CE1 . TYR B 1 312 ? 9.600 -7.194 57.063 1.00 22.59 ? 312 TYR B CE1 1 ATOM 6764 C CE2 . TYR B 1 312 ? 10.902 -6.642 59.043 1.00 22.54 ? 312 TYR B CE2 1 ATOM 6765 C CZ . TYR B 1 312 ? 10.106 -6.242 57.955 1.00 21.15 ? 312 TYR B CZ 1 ATOM 6766 O OH . TYR B 1 312 ? 9.820 -4.910 57.777 1.00 17.16 ? 312 TYR B OH 1 ATOM 6767 N N . ALA B 1 313 ? 13.759 -12.209 58.365 1.00 26.22 ? 313 ALA B N 1 ATOM 6768 C CA . ALA B 1 313 ? 14.590 -13.243 58.979 1.00 27.38 ? 313 ALA B CA 1 ATOM 6769 C C . ALA B 1 313 ? 14.227 -13.484 60.448 1.00 28.94 ? 313 ALA B C 1 ATOM 6770 O O . ALA B 1 313 ? 14.059 -12.534 61.227 1.00 28.15 ? 313 ALA B O 1 ATOM 6771 C CB . ALA B 1 313 ? 16.058 -12.877 58.846 1.00 28.26 ? 313 ALA B CB 1 ATOM 6772 N N . GLY B 1 314 ? 14.023 -14.760 60.777 1.00 29.55 ? 314 GLY B N 1 ATOM 6773 C CA . GLY B 1 314 ? 13.672 -15.161 62.130 1.00 30.10 ? 314 GLY B CA 1 ATOM 6774 C C . GLY B 1 314 ? 12.179 -15.269 62.359 1.00 30.93 ? 314 GLY B C 1 ATOM 6775 O O . GLY B 1 314 ? 11.739 -15.861 63.351 1.00 31.27 ? 314 GLY B O 1 ATOM 6776 N N . ALA B 1 315 ? 11.406 -14.695 61.437 1.00 30.53 ? 315 ALA B N 1 ATOM 6777 C CA . ALA B 1 315 ? 9.943 -14.693 61.491 1.00 29.79 ? 315 ALA B CA 1 ATOM 6778 C C . ALA B 1 315 ? 9.403 -16.023 60.959 1.00 28.48 ? 315 ALA B C 1 ATOM 6779 O O . ALA B 1 315 ? 10.136 -16.739 60.273 1.00 28.61 ? 315 ALA B O 1 ATOM 6780 C CB . ALA B 1 315 ? 9.403 -13.531 60.664 1.00 30.09 ? 315 ALA B CB 1 ATOM 6781 N N . PRO B 1 316 ? 8.148 -16.405 61.319 1.00 27.86 ? 316 PRO B N 1 ATOM 6782 C CA . PRO B 1 316 ? 7.598 -17.676 60.820 1.00 27.99 ? 316 PRO B CA 1 ATOM 6783 C C . PRO B 1 316 ? 7.385 -17.709 59.299 1.00 28.63 ? 316 PRO B C 1 ATOM 6784 O O . PRO B 1 316 ? 7.227 -16.665 58.660 1.00 28.68 ? 316 PRO B O 1 ATOM 6785 C CB . PRO B 1 316 ? 6.286 -17.811 61.599 1.00 27.14 ? 316 PRO B CB 1 ATOM 6786 C CG . PRO B 1 316 ? 5.921 -16.394 61.925 1.00 27.60 ? 316 PRO B CG 1 ATOM 6787 C CD . PRO B 1 316 ? 7.240 -15.830 62.333 1.00 27.35 ? 316 PRO B CD 1 ATOM 6788 N N . GLY B 1 317 ? 7.423 -18.913 58.736 1.00 29.27 ? 317 GLY B N 1 ATOM 6789 C CA . GLY B 1 317 ? 7.261 -19.085 57.303 1.00 31.12 ? 317 GLY B CA 1 ATOM 6790 C C . GLY B 1 317 ? 5.838 -19.147 56.783 1.00 32.46 ? 317 GLY B C 1 ATOM 6791 O O . GLY B 1 317 ? 4.869 -18.923 57.519 1.00 33.13 ? 317 GLY B O 1 ATOM 6792 N N . GLY B 1 318 ? 5.729 -19.451 55.492 1.00 32.70 ? 318 GLY B N 1 ATOM 6793 C CA . GLY B 1 318 ? 4.435 -19.549 54.848 1.00 32.15 ? 318 GLY B CA 1 ATOM 6794 C C . GLY B 1 318 ? 4.025 -18.303 54.091 1.00 31.22 ? 318 GLY B C 1 ATOM 6795 O O . GLY B 1 318 ? 4.787 -17.345 53.963 1.00 30.30 ? 318 GLY B O 1 ATOM 6796 N N . LEU B 1 319 ? 2.784 -18.327 53.620 1.00 30.74 ? 319 LEU B N 1 ATOM 6797 C CA . LEU B 1 319 ? 2.190 -17.247 52.848 1.00 31.55 ? 319 LEU B CA 1 ATOM 6798 C C . LEU B 1 319 ? 1.742 -16.047 53.701 1.00 32.67 ? 319 LEU B C 1 ATOM 6799 O O . LEU B 1 319 ? 1.325 -16.230 54.849 1.00 34.78 ? 319 LEU B O 1 ATOM 6800 C CB . LEU B 1 319 ? 0.983 -17.795 52.074 1.00 29.54 ? 319 LEU B CB 1 ATOM 6801 C CG . LEU B 1 319 ? 1.136 -19.109 51.303 1.00 28.00 ? 319 LEU B CG 1 ATOM 6802 C CD1 . LEU B 1 319 ? -0.207 -19.482 50.706 1.00 26.88 ? 319 LEU B CD1 1 ATOM 6803 C CD2 . LEU B 1 319 ? 2.210 -18.997 50.225 1.00 27.13 ? 319 LEU B CD2 1 ATOM 6804 N N . PRO B 1 320 ? 1.906 -14.801 53.185 1.00 32.93 ? 320 PRO B N 1 ATOM 6805 C CA . PRO B 1 320 ? 1.498 -13.572 53.892 1.00 32.48 ? 320 PRO B CA 1 ATOM 6806 C C . PRO B 1 320 ? -0.024 -13.554 54.063 1.00 32.40 ? 320 PRO B C 1 ATOM 6807 O O . PRO B 1 320 ? -0.760 -13.982 53.165 1.00 33.38 ? 320 PRO B O 1 ATOM 6808 C CB . PRO B 1 320 ? 1.929 -12.465 52.937 1.00 32.14 ? 320 PRO B CB 1 ATOM 6809 C CG . PRO B 1 320 ? 3.106 -13.033 52.265 1.00 31.98 ? 320 PRO B CG 1 ATOM 6810 C CD . PRO B 1 320 ? 2.761 -14.464 52.028 1.00 31.99 ? 320 PRO B CD 1 ATOM 6811 N N . THR B 1 321 ? -0.478 -13.060 55.210 1.00 31.61 ? 321 THR B N 1 ATOM 6812 C CA . THR B 1 321 ? -1.898 -13.009 55.545 1.00 30.95 ? 321 THR B CA 1 ATOM 6813 C C . THR B 1 321 ? -2.617 -11.732 55.125 1.00 31.28 ? 321 THR B C 1 ATOM 6814 O O . THR B 1 321 ? -3.838 -11.732 54.959 1.00 31.73 ? 321 THR B O 1 ATOM 6815 C CB . THR B 1 321 ? -2.093 -13.216 57.056 1.00 32.12 ? 321 THR B CB 1 ATOM 6816 O OG1 . THR B 1 321 ? -1.210 -12.341 57.775 1.00 30.63 ? 321 THR B OG1 1 ATOM 6817 C CG2 . THR B 1 321 ? -1.799 -14.671 57.439 1.00 31.40 ? 321 THR B CG2 1 ATOM 6818 N N . ASP B 1 322 ? -1.853 -10.655 54.954 1.00 30.93 ? 322 ASP B N 1 ATOM 6819 C CA . ASP B 1 322 ? -2.386 -9.347 54.570 1.00 30.61 ? 322 ASP B CA 1 ATOM 6820 C C . ASP B 1 322 ? -2.399 -9.182 53.040 1.00 30.58 ? 322 ASP B C 1 ATOM 6821 O O . ASP B 1 322 ? -1.344 -9.018 52.421 1.00 31.21 ? 322 ASP B O 1 ATOM 6822 C CB . ASP B 1 322 ? -1.542 -8.249 55.247 1.00 30.51 ? 322 ASP B CB 1 ATOM 6823 C CG . ASP B 1 322 ? -2.236 -6.885 55.297 1.00 32.12 ? 322 ASP B CG 1 ATOM 6824 O OD1 . ASP B 1 322 ? -3.338 -6.708 54.721 1.00 32.44 ? 322 ASP B OD1 1 ATOM 6825 O OD2 . ASP B 1 322 ? -1.654 -5.974 55.926 1.00 32.21 ? 322 ASP B OD2 1 ATOM 6826 N N . GLU B 1 323 ? -3.599 -9.196 52.449 1.00 30.47 ? 323 GLU B N 1 ATOM 6827 C CA . GLU B 1 323 ? -3.784 -9.056 50.994 1.00 29.31 ? 323 GLU B CA 1 ATOM 6828 C C . GLU B 1 323 ? -3.467 -7.658 50.458 1.00 29.24 ? 323 GLU B C 1 ATOM 6829 O O . GLU B 1 323 ? -3.372 -7.453 49.242 1.00 27.56 ? 323 GLU B O 1 ATOM 6830 C CB . GLU B 1 323 ? -5.201 -9.461 50.576 1.00 28.45 ? 323 GLU B CB 1 ATOM 6831 C CG . GLU B 1 323 ? -5.451 -10.969 50.534 1.00 28.77 ? 323 GLU B CG 1 ATOM 6832 C CD . GLU B 1 323 ? -6.835 -11.352 50.011 1.00 28.10 ? 323 GLU B CD 1 ATOM 6833 O OE1 . GLU B 1 323 ? -7.587 -10.467 49.548 1.00 26.50 ? 323 GLU B OE1 1 ATOM 6834 O OE2 . GLU B 1 323 ? -7.170 -12.558 50.051 1.00 29.45 ? 323 GLU B OE2 1 ATOM 6835 N N . GLY B 1 324 ? -3.331 -6.706 51.383 1.00 29.37 ? 324 GLY B N 1 ATOM 6836 C CA . GLY B 1 324 ? -2.999 -5.331 51.044 1.00 29.52 ? 324 GLY B CA 1 ATOM 6837 C C . GLY B 1 324 ? -4.061 -4.437 50.427 1.00 28.84 ? 324 GLY B C 1 ATOM 6838 O O . GLY B 1 324 ? -5.193 -4.847 50.161 1.00 27.77 ? 324 GLY B O 1 ATOM 6839 N N . THR B 1 325 ? -3.667 -3.184 50.226 1.00 29.55 ? 325 THR B N 1 ATOM 6840 C CA . THR B 1 325 ? -4.510 -2.154 49.639 1.00 30.30 ? 325 THR B CA 1 ATOM 6841 C C . THR B 1 325 ? -4.033 -1.933 48.196 1.00 30.20 ? 325 THR B C 1 ATOM 6842 O O . THR B 1 325 ? -2.823 -1.814 47.965 1.00 29.41 ? 325 THR B O 1 ATOM 6843 C CB . THR B 1 325 ? -4.408 -0.837 50.455 1.00 30.69 ? 325 THR B CB 1 ATOM 6844 O OG1 . THR B 1 325 ? -3.032 -0.535 50.712 1.00 32.68 ? 325 THR B OG1 1 ATOM 6845 C CG2 . THR B 1 325 ? -5.150 -0.969 51.786 1.00 33.02 ? 325 THR B CG2 1 ATOM 6846 N N . PRO B 1 326 ? -4.966 -1.912 47.204 1.00 30.85 ? 326 PRO B N 1 ATOM 6847 C CA . PRO B 1 326 ? -4.602 -1.706 45.791 1.00 30.25 ? 326 PRO B CA 1 ATOM 6848 C C . PRO B 1 326 ? -3.870 -0.373 45.600 1.00 29.72 ? 326 PRO B C 1 ATOM 6849 O O . PRO B 1 326 ? -4.271 0.648 46.175 1.00 29.26 ? 326 PRO B O 1 ATOM 6850 C CB . PRO B 1 326 ? -5.962 -1.697 45.083 1.00 31.66 ? 326 PRO B CB 1 ATOM 6851 C CG . PRO B 1 326 ? -6.805 -2.570 45.941 1.00 31.07 ? 326 PRO B CG 1 ATOM 6852 C CD . PRO B 1 326 ? -6.430 -2.098 47.322 1.00 31.76 ? 326 PRO B CD 1 ATOM 6853 N N . PRO B 1 327 ? -2.755 -0.375 44.846 1.00 29.22 ? 327 PRO B N 1 ATOM 6854 C CA . PRO B 1 327 ? -2.016 0.874 44.638 1.00 29.35 ? 327 PRO B CA 1 ATOM 6855 C C . PRO B 1 327 ? -2.708 1.887 43.723 1.00 28.31 ? 327 PRO B C 1 ATOM 6856 O O . PRO B 1 327 ? -3.752 1.602 43.114 1.00 27.36 ? 327 PRO B O 1 ATOM 6857 C CB . PRO B 1 327 ? -0.694 0.386 44.050 1.00 28.32 ? 327 PRO B CB 1 ATOM 6858 C CG . PRO B 1 327 ? -1.108 -0.790 43.262 1.00 28.08 ? 327 PRO B CG 1 ATOM 6859 C CD . PRO B 1 327 ? -2.047 -1.499 44.205 1.00 29.47 ? 327 PRO B CD 1 ATOM 6860 N N . VAL B 1 328 ? -2.102 3.069 43.644 1.00 26.69 ? 328 VAL B N 1 ATOM 6861 C CA . VAL B 1 328 ? -2.597 4.158 42.815 1.00 26.05 ? 328 VAL B CA 1 ATOM 6862 C C . VAL B 1 328 ? -2.415 3.768 41.342 1.00 24.14 ? 328 VAL B C 1 ATOM 6863 O O . VAL B 1 328 ? -1.417 3.139 40.969 1.00 23.26 ? 328 VAL B O 1 ATOM 6864 C CB . VAL B 1 328 ? -1.829 5.475 43.112 1.00 26.46 ? 328 VAL B CB 1 ATOM 6865 C CG1 . VAL B 1 328 ? -2.493 6.660 42.403 1.00 30.75 ? 328 VAL B CG1 1 ATOM 6866 C CG2 . VAL B 1 328 ? -1.774 5.732 44.607 1.00 28.00 ? 328 VAL B CG2 1 ATOM 6867 N N . ASP B 1 329 ? -3.434 4.072 40.543 1.00 22.06 ? 329 ASP B N 1 ATOM 6868 C CA . ASP B 1 329 ? -3.432 3.798 39.111 1.00 20.19 ? 329 ASP B CA 1 ATOM 6869 C C . ASP B 1 329 ? -2.447 4.791 38.483 1.00 16.85 ? 329 ASP B C 1 ATOM 6870 O O . ASP B 1 329 ? -2.702 5.994 38.456 1.00 17.21 ? 329 ASP B O 1 ATOM 6871 C CB . ASP B 1 329 ? -4.852 3.992 38.547 1.00 21.09 ? 329 ASP B CB 1 ATOM 6872 C CG . ASP B 1 329 ? -5.032 3.400 37.152 1.00 22.29 ? 329 ASP B CG 1 ATOM 6873 O OD1 . ASP B 1 329 ? -4.052 3.334 36.382 1.00 18.77 ? 329 ASP B OD1 1 ATOM 6874 O OD2 . ASP B 1 329 ? -6.175 3.019 36.816 1.00 23.10 ? 329 ASP B OD2 1 ATOM 6875 N N . HIS B 1 330 ? -1.306 4.276 38.028 1.00 14.19 ? 330 HIS B N 1 ATOM 6876 C CA . HIS B 1 330 ? -0.266 5.099 37.410 1.00 13.40 ? 330 HIS B CA 1 ATOM 6877 C C . HIS B 1 330 ? -0.595 5.530 35.984 1.00 12.60 ? 330 HIS B C 1 ATOM 6878 O O . HIS B 1 330 ? 0.112 6.357 35.409 1.00 15.37 ? 330 HIS B O 1 ATOM 6879 C CB . HIS B 1 330 ? 1.092 4.391 37.456 1.00 11.55 ? 330 HIS B CB 1 ATOM 6880 C CG . HIS B 1 330 ? 1.732 4.391 38.811 1.00 12.09 ? 330 HIS B CG 1 ATOM 6881 N ND1 . HIS B 1 330 ? 2.841 5.154 39.107 1.00 12.82 ? 330 HIS B ND1 1 ATOM 6882 C CD2 . HIS B 1 330 ? 1.440 3.700 39.940 1.00 10.20 ? 330 HIS B CD2 1 ATOM 6883 C CE1 . HIS B 1 330 ? 3.207 4.928 40.356 1.00 9.81 ? 330 HIS B CE1 1 ATOM 6884 N NE2 . HIS B 1 330 ? 2.374 4.050 40.882 1.00 9.11 ? 330 HIS B NE2 1 ATOM 6885 N N . GLN B 1 331 ? -1.695 4.990 35.451 1.00 9.36 ? 331 GLN B N 1 ATOM 6886 C CA . GLN B 1 331 ? -2.212 5.282 34.108 1.00 11.84 ? 331 GLN B CA 1 ATOM 6887 C C . GLN B 1 331 ? -1.215 5.161 32.953 1.00 10.81 ? 331 GLN B C 1 ATOM 6888 O O . GLN B 1 331 ? -1.161 6.022 32.075 1.00 13.35 ? 331 GLN B O 1 ATOM 6889 C CB . GLN B 1 331 ? -2.929 6.646 34.073 1.00 11.62 ? 331 GLN B CB 1 ATOM 6890 C CG . GLN B 1 331 ? -4.052 6.819 35.094 1.00 12.55 ? 331 GLN B CG 1 ATOM 6891 C CD . GLN B 1 331 ? -5.350 6.124 34.730 1.00 12.00 ? 331 GLN B CD 1 ATOM 6892 O OE1 . GLN B 1 331 ? -5.447 5.418 33.729 1.00 15.97 ? 331 GLN B OE1 1 ATOM 6893 N NE2 . GLN B 1 331 ? -6.374 6.360 35.529 1.00 14.88 ? 331 GLN B NE2 1 ATOM 6894 N N . CYS B 1 332 ? -0.439 4.075 32.979 1.00 11.03 ? 332 CYS B N 1 ATOM 6895 C CA . CYS B 1 332 ? 0.594 3.749 31.988 1.00 11.84 ? 332 CYS B CA 1 ATOM 6896 C C . CYS B 1 332 ? 1.641 4.845 31.765 1.00 11.95 ? 332 CYS B C 1 ATOM 6897 O O . CYS B 1 332 ? 2.042 5.106 30.628 1.00 12.33 ? 332 CYS B O 1 ATOM 6898 C CB . CYS B 1 332 ? -0.031 3.321 30.658 1.00 8.92 ? 332 CYS B CB 1 ATOM 6899 S SG . CYS B 1 332 ? -1.107 1.865 30.760 1.00 12.54 ? 332 CYS B SG 1 ATOM 6900 N N . LEU B 1 333 ? 2.032 5.511 32.858 1.00 12.41 ? 333 LEU B N 1 ATOM 6901 C CA . LEU B 1 333 ? 3.007 6.617 32.836 1.00 14.23 ? 333 LEU B CA 1 ATOM 6902 C C . LEU B 1 333 ? 4.067 6.525 33.923 1.00 13.86 ? 333 LEU B C 1 ATOM 6903 O O . LEU B 1 333 ? 3.754 6.242 35.079 1.00 15.05 ? 333 LEU B O 1 ATOM 6904 C CB . LEU B 1 333 ? 2.296 7.966 33.015 1.00 14.60 ? 333 LEU B CB 1 ATOM 6905 C CG . LEU B 1 333 ? 1.260 8.461 32.010 1.00 14.85 ? 333 LEU B CG 1 ATOM 6906 C CD1 . LEU B 1 333 ? 0.387 9.474 32.675 1.00 15.24 ? 333 LEU B CD1 1 ATOM 6907 C CD2 . LEU B 1 333 ? 1.921 9.005 30.762 1.00 15.18 ? 333 LEU B CD2 1 ATOM 6908 N N . ASP B 1 334 ? 5.324 6.754 33.546 1.00 15.78 ? 334 ASP B N 1 ATOM 6909 C CA . ASP B 1 334 ? 6.434 6.746 34.508 1.00 17.91 ? 334 ASP B CA 1 ATOM 6910 C C . ASP B 1 334 ? 6.531 8.114 35.169 1.00 19.57 ? 334 ASP B C 1 ATOM 6911 O O . ASP B 1 334 ? 6.180 9.126 34.553 1.00 19.62 ? 334 ASP B O 1 ATOM 6912 C CB . ASP B 1 334 ? 7.772 6.325 33.859 1.00 16.09 ? 334 ASP B CB 1 ATOM 6913 C CG . ASP B 1 334 ? 8.159 7.174 32.654 1.00 16.41 ? 334 ASP B CG 1 ATOM 6914 O OD1 . ASP B 1 334 ? 7.294 7.457 31.803 1.00 14.90 ? 334 ASP B OD1 1 ATOM 6915 O OD2 . ASP B 1 334 ? 9.344 7.559 32.562 1.00 16.98 ? 334 ASP B OD2 1 ATOM 6916 N N . THR B 1 335 ? 6.951 8.135 36.433 1.00 21.07 ? 335 THR B N 1 ATOM 6917 C CA . THR B 1 335 ? 7.076 9.381 37.185 1.00 21.33 ? 335 THR B CA 1 ATOM 6918 C C . THR B 1 335 ? 8.181 10.288 36.656 1.00 21.94 ? 335 THR B C 1 ATOM 6919 O O . THR B 1 335 ? 9.289 9.833 36.337 1.00 20.97 ? 335 THR B O 1 ATOM 6920 C CB . THR B 1 335 ? 7.261 9.133 38.718 1.00 22.45 ? 335 THR B CB 1 ATOM 6921 O OG1 . THR B 1 335 ? 7.389 10.387 39.397 1.00 24.23 ? 335 THR B OG1 1 ATOM 6922 C CG2 . THR B 1 335 ? 8.493 8.274 39.016 1.00 23.77 ? 335 THR B CG2 1 ATOM 6923 N N . LEU B 1 336 ? 7.831 11.559 36.489 1.00 21.96 ? 336 LEU B N 1 ATOM 6924 C CA . LEU B 1 336 ? 8.781 12.548 36.023 1.00 21.76 ? 336 LEU B CA 1 ATOM 6925 C C . LEU B 1 336 ? 9.254 13.434 37.171 1.00 22.64 ? 336 LEU B C 1 ATOM 6926 O O . LEU B 1 336 ? 9.801 14.520 36.954 1.00 24.24 ? 336 LEU B O 1 ATOM 6927 C CB . LEU B 1 336 ? 8.214 13.377 34.861 1.00 21.98 ? 336 LEU B CB 1 ATOM 6928 C CG . LEU B 1 336 ? 7.847 12.646 33.559 1.00 21.08 ? 336 LEU B CG 1 ATOM 6929 C CD1 . LEU B 1 336 ? 7.522 13.666 32.490 1.00 21.30 ? 336 LEU B CD1 1 ATOM 6930 C CD2 . LEU B 1 336 ? 8.943 11.701 33.090 1.00 18.40 ? 336 LEU B CD2 1 ATOM 6931 N N . ASP B 1 337 ? 9.089 12.930 38.393 1.00 22.61 ? 337 ASP B N 1 ATOM 6932 C CA . ASP B 1 337 ? 9.510 13.650 39.593 1.00 22.91 ? 337 ASP B CA 1 ATOM 6933 C C . ASP B 1 337 ? 10.978 13.385 39.926 1.00 21.76 ? 337 ASP B C 1 ATOM 6934 O O . ASP B 1 337 ? 11.612 14.199 40.601 1.00 21.74 ? 337 ASP B O 1 ATOM 6935 C CB . ASP B 1 337 ? 8.615 13.304 40.789 1.00 23.18 ? 337 ASP B CB 1 ATOM 6936 C CG . ASP B 1 337 ? 7.206 13.827 40.634 1.00 24.91 ? 337 ASP B CG 1 ATOM 6937 O OD1 . ASP B 1 337 ? 7.032 15.035 40.361 1.00 28.67 ? 337 ASP B OD1 1 ATOM 6938 O OD2 . ASP B 1 337 ? 6.264 13.030 40.789 1.00 26.95 ? 337 ASP B OD2 1 ATOM 6939 N N . VAL B 1 338 ? 11.524 12.284 39.397 1.00 20.65 ? 338 VAL B N 1 ATOM 6940 C CA . VAL B 1 338 ? 12.931 11.908 39.625 1.00 20.12 ? 338 VAL B CA 1 ATOM 6941 C C . VAL B 1 338 ? 13.937 12.944 39.105 1.00 19.93 ? 338 VAL B C 1 ATOM 6942 O O . VAL B 1 338 ? 13.840 13.419 37.967 1.00 20.15 ? 338 VAL B O 1 ATOM 6943 C CB . VAL B 1 338 ? 13.281 10.483 39.077 1.00 17.13 ? 338 VAL B CB 1 ATOM 6944 C CG1 . VAL B 1 338 ? 12.646 9.418 39.947 1.00 15.94 ? 338 VAL B CG1 1 ATOM 6945 C CG2 . VAL B 1 338 ? 12.848 10.315 37.623 1.00 17.56 ? 338 VAL B CG2 1 ATOM 6946 N N . ARG B 1 339 ? 14.818 13.368 40.007 1.00 19.49 ? 339 ARG B N 1 ATOM 6947 C CA . ARG B 1 339 ? 15.840 14.365 39.716 1.00 19.03 ? 339 ARG B CA 1 ATOM 6948 C C . ARG B 1 339 ? 17.226 13.747 39.902 1.00 18.56 ? 339 ARG B C 1 ATOM 6949 O O . ARG B 1 339 ? 17.591 13.386 41.027 1.00 18.58 ? 339 ARG B O 1 ATOM 6950 C CB . ARG B 1 339 ? 15.701 15.578 40.656 1.00 19.64 ? 339 ARG B CB 1 ATOM 6951 C CG . ARG B 1 339 ? 14.378 16.327 40.608 1.00 22.48 ? 339 ARG B CG 1 ATOM 6952 C CD . ARG B 1 339 ? 14.233 17.137 39.332 1.00 26.95 ? 339 ARG B CD 1 ATOM 6953 N NE . ARG B 1 339 ? 12.956 17.853 39.252 1.00 30.83 ? 339 ARG B NE 1 ATOM 6954 C CZ . ARG B 1 339 ? 11.833 17.365 38.723 1.00 31.64 ? 339 ARG B CZ 1 ATOM 6955 N NH1 . ARG B 1 339 ? 11.797 16.139 38.208 1.00 32.94 ? 339 ARG B NH1 1 ATOM 6956 N NH2 . ARG B 1 339 ? 10.735 18.108 38.717 1.00 33.11 ? 339 ARG B NH2 1 ATOM 6957 N N . PRO B 1 340 ? 18.009 13.602 38.806 1.00 18.06 ? 340 PRO B N 1 ATOM 6958 C CA . PRO B 1 340 ? 19.369 13.036 38.797 1.00 18.89 ? 340 PRO B CA 1 ATOM 6959 C C . PRO B 1 340 ? 20.344 13.718 39.762 1.00 19.68 ? 340 PRO B C 1 ATOM 6960 O O . PRO B 1 340 ? 20.210 14.917 40.028 1.00 20.49 ? 340 PRO B O 1 ATOM 6961 C CB . PRO B 1 340 ? 19.805 13.235 37.350 1.00 19.01 ? 340 PRO B CB 1 ATOM 6962 C CG . PRO B 1 340 ? 18.544 13.068 36.608 1.00 17.02 ? 340 PRO B CG 1 ATOM 6963 C CD . PRO B 1 340 ? 17.570 13.868 37.421 1.00 17.92 ? 340 PRO B CD 1 ATOM 6964 N N . VAL B 1 341 ? 21.293 12.945 40.302 1.00 20.53 ? 341 VAL B N 1 ATOM 6965 C CA . VAL B 1 341 ? 22.307 13.464 41.233 1.00 22.84 ? 341 VAL B CA 1 ATOM 6966 C C . VAL B 1 341 ? 23.242 14.397 40.468 1.00 22.90 ? 341 VAL B C 1 ATOM 6967 O O . VAL B 1 341 ? 23.531 15.500 40.929 1.00 23.67 ? 341 VAL B O 1 ATOM 6968 C CB . VAL B 1 341 ? 23.134 12.328 41.915 1.00 24.60 ? 341 VAL B CB 1 ATOM 6969 C CG1 . VAL B 1 341 ? 24.137 12.912 42.921 1.00 25.04 ? 341 VAL B CG1 1 ATOM 6970 C CG2 . VAL B 1 341 ? 22.222 11.375 42.646 1.00 23.87 ? 341 VAL B CG2 1 ATOM 6971 N N . VAL B 1 342 ? 23.698 13.938 39.303 1.00 24.79 ? 342 VAL B N 1 ATOM 6972 C CA . VAL B 1 342 ? 24.566 14.723 38.419 1.00 25.47 ? 342 VAL B CA 1 ATOM 6973 C C . VAL B 1 342 ? 23.599 15.473 37.483 1.00 25.05 ? 342 VAL B C 1 ATOM 6974 O O . VAL B 1 342 ? 22.894 14.840 36.692 1.00 24.13 ? 342 VAL B O 1 ATOM 6975 C CB . VAL B 1 342 ? 25.549 13.811 37.624 1.00 25.67 ? 342 VAL B CB 1 ATOM 6976 C CG1 . VAL B 1 342 ? 26.463 14.640 36.726 1.00 24.26 ? 342 VAL B CG1 1 ATOM 6977 C CG2 . VAL B 1 342 ? 26.396 13.007 38.594 1.00 26.51 ? 342 VAL B CG2 1 ATOM 6978 N N . PRO B 1 343 ? 23.531 16.823 37.598 1.00 25.96 ? 343 PRO B N 1 ATOM 6979 C CA . PRO B 1 343 ? 22.638 17.642 36.771 1.00 27.14 ? 343 PRO B CA 1 ATOM 6980 C C . PRO B 1 343 ? 23.042 17.990 35.336 1.00 28.06 ? 343 PRO B C 1 ATOM 6981 O O . PRO B 1 343 ? 24.213 17.912 34.961 1.00 27.97 ? 343 PRO B O 1 ATOM 6982 C CB . PRO B 1 343 ? 22.457 18.895 37.626 1.00 26.71 ? 343 PRO B CB 1 ATOM 6983 C CG . PRO B 1 343 ? 23.801 19.082 38.216 1.00 26.62 ? 343 PRO B CG 1 ATOM 6984 C CD . PRO B 1 343 ? 24.222 17.673 38.594 1.00 26.56 ? 343 PRO B CD 1 ATOM 6985 N N . ARG B 1 344 ? 22.028 18.339 34.546 1.00 28.96 ? 344 ARG B N 1 ATOM 6986 C CA . ARG B 1 344 ? 22.155 18.750 33.143 1.00 31.27 ? 344 ARG B CA 1 ATOM 6987 C C . ARG B 1 344 ? 21.188 19.924 32.940 1.00 32.84 ? 344 ARG B C 1 ATOM 6988 O O . ARG B 1 344 ? 20.138 19.975 33.584 1.00 34.37 ? 344 ARG B O 1 ATOM 6989 C CB . ARG B 1 344 ? 21.759 17.609 32.189 1.00 30.96 ? 344 ARG B CB 1 ATOM 6990 C CG . ARG B 1 344 ? 22.699 16.400 32.132 1.00 30.34 ? 344 ARG B CG 1 ATOM 6991 C CD . ARG B 1 344 ? 24.075 16.735 31.559 1.00 29.64 ? 344 ARG B CD 1 ATOM 6992 N NE . ARG B 1 344 ? 24.902 15.536 31.407 1.00 29.08 ? 344 ARG B NE 1 ATOM 6993 C CZ . ARG B 1 344 ? 25.875 15.163 32.238 1.00 29.09 ? 344 ARG B CZ 1 ATOM 6994 N NH1 . ARG B 1 344 ? 26.176 15.894 33.310 1.00 30.07 ? 344 ARG B NH1 1 ATOM 6995 N NH2 . ARG B 1 344 ? 26.540 14.040 32.003 1.00 25.22 ? 344 ARG B NH2 1 ATOM 6996 N N . SER B 1 345 ? 21.540 20.867 32.065 1.00 34.57 ? 345 SER B N 1 ATOM 6997 C CA . SER B 1 345 ? 20.680 22.027 31.793 1.00 36.47 ? 345 SER B CA 1 ATOM 6998 C C . SER B 1 345 ? 20.520 22.333 30.308 1.00 36.98 ? 345 SER B C 1 ATOM 6999 O O . SER B 1 345 ? 21.501 22.345 29.553 1.00 37.11 ? 345 SER B O 1 ATOM 7000 C CB . SER B 1 345 ? 21.177 23.270 32.537 1.00 36.74 ? 345 SER B CB 1 ATOM 7001 O OG . SER B 1 345 ? 20.926 23.159 33.925 1.00 38.47 ? 345 SER B OG 1 ATOM 7002 N N . VAL B 1 346 ? 19.266 22.539 29.895 1.00 37.64 ? 346 VAL B N 1 ATOM 7003 C CA . VAL B 1 346 ? 18.913 22.843 28.500 1.00 38.34 ? 346 VAL B CA 1 ATOM 7004 C C . VAL B 1 346 ? 17.872 23.967 28.372 1.00 38.41 ? 346 VAL B C 1 ATOM 7005 O O . VAL B 1 346 ? 16.954 24.057 29.200 1.00 37.94 ? 346 VAL B O 1 ATOM 7006 C CB . VAL B 1 346 ? 18.337 21.587 27.733 1.00 38.82 ? 346 VAL B CB 1 ATOM 7007 C CG1 . VAL B 1 346 ? 19.384 20.531 27.562 1.00 39.64 ? 346 VAL B CG1 1 ATOM 7008 C CG2 . VAL B 1 346 ? 17.125 21.011 28.428 1.00 38.52 ? 346 VAL B CG2 1 ATOM 7009 N N . PRO B 1 347 ? 18.029 24.866 27.366 1.00 38.69 ? 347 PRO B N 1 ATOM 7010 C CA . PRO B 1 347 ? 17.048 25.949 27.192 1.00 38.88 ? 347 PRO B CA 1 ATOM 7011 C C . PRO B 1 347 ? 15.773 25.382 26.546 1.00 38.60 ? 347 PRO B C 1 ATOM 7012 O O . PRO B 1 347 ? 15.817 24.836 25.436 1.00 38.86 ? 347 PRO B O 1 ATOM 7013 C CB . PRO B 1 347 ? 17.768 26.918 26.246 1.00 39.34 ? 347 PRO B CB 1 ATOM 7014 C CG . PRO B 1 347 ? 19.216 26.666 26.522 1.00 39.83 ? 347 PRO B CG 1 ATOM 7015 C CD . PRO B 1 347 ? 19.248 25.167 26.587 1.00 39.14 ? 347 PRO B CD 1 ATOM 7016 N N . VAL B 1 348 ? 14.662 25.458 27.274 1.00 37.09 ? 348 VAL B N 1 ATOM 7017 C CA . VAL B 1 348 ? 13.386 24.940 26.783 1.00 36.61 ? 348 VAL B CA 1 ATOM 7018 C C . VAL B 1 348 ? 12.462 25.970 26.146 1.00 36.29 ? 348 VAL B C 1 ATOM 7019 O O . VAL B 1 348 ? 11.557 25.611 25.388 1.00 35.34 ? 348 VAL B O 1 ATOM 7020 C CB . VAL B 1 348 ? 12.616 24.150 27.871 1.00 36.66 ? 348 VAL B CB 1 ATOM 7021 C CG1 . VAL B 1 348 ? 13.259 22.785 28.067 1.00 36.38 ? 348 VAL B CG1 1 ATOM 7022 C CG2 . VAL B 1 348 ? 12.544 24.931 29.191 1.00 36.82 ? 348 VAL B CG2 1 ATOM 7023 N N . ASN B 1 349 ? 12.705 27.243 26.456 1.00 35.86 ? 349 ASN B N 1 ATOM 7024 C CA . ASN B 1 349 ? 11.920 28.363 25.929 1.00 35.28 ? 349 ASN B CA 1 ATOM 7025 C C . ASN B 1 349 ? 12.129 28.555 24.416 1.00 34.88 ? 349 ASN B C 1 ATOM 7026 O O . ASN B 1 349 ? 11.219 28.975 23.693 1.00 32.59 ? 349 ASN B O 1 ATOM 7027 C CB . ASN B 1 349 ? 12.266 29.657 26.697 1.00 35.53 ? 349 ASN B CB 1 ATOM 7028 C CG . ASN B 1 349 ? 13.770 29.989 26.687 1.00 35.61 ? 349 ASN B CG 1 ATOM 7029 O OD1 . ASN B 1 349 ? 14.526 29.526 27.542 1.00 35.32 ? 349 ASN B OD1 1 ATOM 7030 N ND2 . ASN B 1 349 ? 14.193 30.807 25.726 1.00 34.46 ? 349 ASN B ND2 1 ATOM 7031 N N . SER B 1 350 ? 13.314 28.142 23.964 1.00 34.75 ? 350 SER B N 1 ATOM 7032 C CA . SER B 1 350 ? 13.767 28.243 22.579 1.00 35.55 ? 350 SER B CA 1 ATOM 7033 C C . SER B 1 350 ? 13.206 27.215 21.593 1.00 35.13 ? 350 SER B C 1 ATOM 7034 O O . SER B 1 350 ? 13.432 27.334 20.385 1.00 34.96 ? 350 SER B O 1 ATOM 7035 C CB . SER B 1 350 ? 15.296 28.187 22.560 1.00 35.51 ? 350 SER B CB 1 ATOM 7036 O OG . SER B 1 350 ? 15.759 27.023 23.225 1.00 37.30 ? 350 SER B OG 1 ATOM 7037 N N . PHE B 1 351 ? 12.477 26.222 22.104 1.00 35.46 ? 351 PHE B N 1 ATOM 7038 C CA . PHE B 1 351 ? 11.901 25.165 21.273 1.00 35.02 ? 351 PHE B CA 1 ATOM 7039 C C . PHE B 1 351 ? 10.787 25.613 20.316 1.00 35.31 ? 351 PHE B C 1 ATOM 7040 O O . PHE B 1 351 ? 9.863 26.333 20.698 1.00 35.00 ? 351 PHE B O 1 ATOM 7041 C CB . PHE B 1 351 ? 11.426 23.978 22.139 1.00 34.55 ? 351 PHE B CB 1 ATOM 7042 C CG . PHE B 1 351 ? 10.904 22.803 21.336 1.00 33.17 ? 351 PHE B CG 1 ATOM 7043 C CD1 . PHE B 1 351 ? 11.784 22.003 20.589 1.00 32.45 ? 351 PHE B CD1 1 ATOM 7044 C CD2 . PHE B 1 351 ? 9.519 22.550 21.255 1.00 33.18 ? 351 PHE B CD2 1 ATOM 7045 C CE1 . PHE B 1 351 ? 11.297 20.966 19.754 1.00 33.80 ? 351 PHE B CE1 1 ATOM 7046 C CE2 . PHE B 1 351 ? 9.011 21.521 20.429 1.00 32.63 ? 351 PHE B CE2 1 ATOM 7047 C CZ . PHE B 1 351 ? 9.904 20.725 19.672 1.00 33.47 ? 351 PHE B CZ 1 ATOM 7048 N N . VAL B 1 352 ? 10.910 25.152 19.070 1.00 35.46 ? 352 VAL B N 1 ATOM 7049 C CA . VAL B 1 352 ? 9.960 25.419 17.991 1.00 35.70 ? 352 VAL B CA 1 ATOM 7050 C C . VAL B 1 352 ? 9.711 24.072 17.287 1.00 35.87 ? 352 VAL B C 1 ATOM 7051 O O . VAL B 1 352 ? 10.659 23.362 16.936 1.00 35.35 ? 352 VAL B O 1 ATOM 7052 C CB . VAL B 1 352 ? 10.522 26.459 16.941 1.00 36.41 ? 352 VAL B CB 1 ATOM 7053 C CG1 . VAL B 1 352 ? 9.474 26.774 15.866 1.00 35.80 ? 352 VAL B CG1 1 ATOM 7054 C CG2 . VAL B 1 352 ? 10.958 27.763 17.615 1.00 36.12 ? 352 VAL B CG2 1 ATOM 7055 N N . LYS B 1 353 ? 8.430 23.739 17.102 1.00 36.56 ? 353 LYS B N 1 ATOM 7056 C CA . LYS B 1 353 ? 7.971 22.515 16.433 1.00 36.28 ? 353 LYS B CA 1 ATOM 7057 C C . LYS B 1 353 ? 8.199 22.631 14.916 1.00 36.89 ? 353 LYS B C 1 ATOM 7058 O O . LYS B 1 353 ? 7.587 23.467 14.247 1.00 37.37 ? 353 LYS B O 1 ATOM 7059 C CB . LYS B 1 353 ? 6.479 22.301 16.733 1.00 37.34 ? 353 LYS B CB 1 ATOM 7060 C CG . LYS B 1 353 ? 5.821 21.116 16.023 1.00 39.49 ? 353 LYS B CG 1 ATOM 7061 C CD . LYS B 1 353 ? 4.319 21.131 16.215 1.00 40.90 ? 353 LYS B CD 1 ATOM 7062 C CE . LYS B 1 353 ? 3.665 19.975 15.490 1.00 41.37 ? 353 LYS B CE 1 ATOM 7063 N NZ . LYS B 1 353 ? 2.188 20.014 15.655 1.00 42.73 ? 353 LYS B NZ 1 ATOM 7064 N N . ARG B 1 354 ? 9.110 21.809 14.402 1.00 36.69 ? 354 ARG B N 1 ATOM 7065 C CA . ARG B 1 354 ? 9.477 21.778 12.978 1.00 37.55 ? 354 ARG B CA 1 ATOM 7066 C C . ARG B 1 354 ? 9.494 20.315 12.487 1.00 35.95 ? 354 ARG B C 1 ATOM 7067 O O . ARG B 1 354 ? 9.660 19.403 13.299 1.00 34.43 ? 354 ARG B O 1 ATOM 7068 C CB . ARG B 1 354 ? 10.886 22.380 12.787 1.00 39.54 ? 354 ARG B CB 1 ATOM 7069 C CG . ARG B 1 354 ? 11.036 23.875 13.057 1.00 42.16 ? 354 ARG B CG 1 ATOM 7070 C CD . ARG B 1 354 ? 12.494 24.304 12.971 1.00 45.89 ? 354 ARG B CD 1 ATOM 7071 N NE . ARG B 1 354 ? 13.343 23.578 13.922 1.00 49.54 ? 354 ARG B NE 1 ATOM 7072 C CZ . ARG B 1 354 ? 14.556 23.093 13.647 1.00 50.21 ? 354 ARG B CZ 1 ATOM 7073 N NH1 . ARG B 1 354 ? 15.092 23.249 12.441 1.00 50.93 ? 354 ARG B NH1 1 ATOM 7074 N NH2 . ARG B 1 354 ? 15.222 22.417 14.575 1.00 49.82 ? 354 ARG B NH2 1 ATOM 7075 N N . PRO B 1 355 ? 9.319 20.068 11.160 1.00 35.24 ? 355 PRO B N 1 ATOM 7076 C CA . PRO B 1 355 ? 9.335 18.694 10.630 1.00 34.01 ? 355 PRO B CA 1 ATOM 7077 C C . PRO B 1 355 ? 10.595 17.867 10.922 1.00 33.13 ? 355 PRO B C 1 ATOM 7078 O O . PRO B 1 355 ? 10.483 16.686 11.266 1.00 33.45 ? 355 PRO B O 1 ATOM 7079 C CB . PRO B 1 355 ? 9.155 18.914 9.131 1.00 34.36 ? 355 PRO B CB 1 ATOM 7080 C CG . PRO B 1 355 ? 8.219 20.049 9.098 1.00 34.36 ? 355 PRO B CG 1 ATOM 7081 C CD . PRO B 1 355 ? 8.833 20.991 10.110 1.00 35.64 ? 355 PRO B CD 1 ATOM 7082 N N . ASP B 1 356 ? 11.772 18.500 10.864 1.00 31.75 ? 356 ASP B N 1 ATOM 7083 C CA . ASP B 1 356 ? 13.037 17.802 11.117 1.00 30.85 ? 356 ASP B CA 1 ATOM 7084 C C . ASP B 1 356 ? 13.369 17.485 12.582 1.00 29.69 ? 356 ASP B C 1 ATOM 7085 O O . ASP B 1 356 ? 14.451 16.965 12.880 1.00 30.31 ? 356 ASP B O 1 ATOM 7086 C CB . ASP B 1 356 ? 14.224 18.465 10.378 1.00 31.99 ? 356 ASP B CB 1 ATOM 7087 C CG . ASP B 1 356 ? 14.523 19.888 10.844 1.00 33.61 ? 356 ASP B CG 1 ATOM 7088 O OD1 . ASP B 1 356 ? 13.754 20.457 11.651 1.00 34.79 ? 356 ASP B OD1 1 ATOM 7089 O OD2 . ASP B 1 356 ? 15.550 20.439 10.385 1.00 33.40 ? 356 ASP B OD2 1 ATOM 7090 N N . ASN B 1 357 ? 12.446 17.828 13.483 1.00 28.76 ? 357 ASN B N 1 ATOM 7091 C CA . ASN B 1 357 ? 12.582 17.525 14.909 1.00 25.85 ? 357 ASN B CA 1 ATOM 7092 C C . ASN B 1 357 ? 11.337 16.793 15.428 1.00 25.30 ? 357 ASN B C 1 ATOM 7093 O O . ASN B 1 357 ? 11.243 16.465 16.612 1.00 24.97 ? 357 ASN B O 1 ATOM 7094 C CB . ASN B 1 357 ? 12.947 18.768 15.762 1.00 26.28 ? 357 ASN B CB 1 ATOM 7095 C CG . ASN B 1 357 ? 11.855 19.851 15.798 1.00 26.71 ? 357 ASN B CG 1 ATOM 7096 O OD1 . ASN B 1 357 ? 10.665 19.573 15.962 1.00 27.16 ? 357 ASN B OD1 1 ATOM 7097 N ND2 . ASN B 1 357 ? 12.283 21.102 15.711 1.00 27.40 ? 357 ASN B ND2 1 ATOM 7098 N N . THR B 1 358 ? 10.397 16.533 14.517 1.00 25.07 ? 358 THR B N 1 ATOM 7099 C CA . THR B 1 358 ? 9.141 15.857 14.845 1.00 24.75 ? 358 THR B CA 1 ATOM 7100 C C . THR B 1 358 ? 9.075 14.425 14.331 1.00 23.96 ? 358 THR B C 1 ATOM 7101 O O . THR B 1 358 ? 9.308 14.154 13.145 1.00 23.33 ? 358 THR B O 1 ATOM 7102 C CB . THR B 1 358 ? 7.908 16.655 14.332 1.00 24.69 ? 358 THR B CB 1 ATOM 7103 O OG1 . THR B 1 358 ? 7.984 17.999 14.817 1.00 25.60 ? 358 THR B OG1 1 ATOM 7104 C CG2 . THR B 1 358 ? 6.605 16.051 14.845 1.00 26.12 ? 358 THR B CG2 1 ATOM 7105 N N . LEU B 1 359 ? 8.737 13.514 15.245 1.00 21.57 ? 359 LEU B N 1 ATOM 7106 C CA . LEU B 1 359 ? 8.612 12.100 14.929 1.00 20.26 ? 359 LEU B CA 1 ATOM 7107 C C . LEU B 1 359 ? 7.174 11.641 15.218 1.00 20.55 ? 359 LEU B C 1 ATOM 7108 O O . LEU B 1 359 ? 6.832 11.336 16.361 1.00 19.44 ? 359 LEU B O 1 ATOM 7109 C CB . LEU B 1 359 ? 9.641 11.267 15.720 1.00 19.42 ? 359 LEU B CB 1 ATOM 7110 C CG . LEU B 1 359 ? 11.151 11.493 15.505 1.00 18.68 ? 359 LEU B CG 1 ATOM 7111 C CD1 . LEU B 1 359 ? 11.942 10.603 16.436 1.00 19.01 ? 359 LEU B CD1 1 ATOM 7112 C CD2 . LEU B 1 359 ? 11.556 11.228 14.053 1.00 18.29 ? 359 LEU B CD2 1 ATOM 7113 N N . PRO B 1 360 ? 6.287 11.676 14.197 1.00 20.91 ? 360 PRO B N 1 ATOM 7114 C CA . PRO B 1 360 ? 4.896 11.250 14.388 1.00 22.06 ? 360 PRO B CA 1 ATOM 7115 C C . PRO B 1 360 ? 4.728 9.732 14.325 1.00 21.99 ? 360 PRO B C 1 ATOM 7116 O O . PRO B 1 360 ? 5.110 9.099 13.343 1.00 22.22 ? 360 PRO B O 1 ATOM 7117 C CB . PRO B 1 360 ? 4.163 11.911 13.213 1.00 22.96 ? 360 PRO B CB 1 ATOM 7118 C CG . PRO B 1 360 ? 5.092 13.005 12.756 1.00 22.04 ? 360 PRO B CG 1 ATOM 7119 C CD . PRO B 1 360 ? 6.423 12.361 12.900 1.00 21.10 ? 360 PRO B CD 1 ATOM 7120 N N . VAL B 1 361 ? 4.180 9.163 15.394 1.00 22.41 ? 361 VAL B N 1 ATOM 7121 C CA . VAL B 1 361 ? 3.911 7.732 15.477 1.00 21.68 ? 361 VAL B CA 1 ATOM 7122 C C . VAL B 1 361 ? 2.483 7.550 14.971 1.00 22.70 ? 361 VAL B C 1 ATOM 7123 O O . VAL B 1 361 ? 1.549 8.107 15.538 1.00 24.08 ? 361 VAL B O 1 ATOM 7124 C CB . VAL B 1 361 ? 4.023 7.216 16.938 1.00 21.95 ? 361 VAL B CB 1 ATOM 7125 C CG1 . VAL B 1 361 ? 3.650 5.742 17.025 1.00 24.47 ? 361 VAL B CG1 1 ATOM 7126 C CG2 . VAL B 1 361 ? 5.428 7.409 17.456 1.00 22.35 ? 361 VAL B CG2 1 ATOM 7127 N N . ALA B 1 362 ? 2.329 6.809 13.879 1.00 23.66 ? 362 ALA B N 1 ATOM 7128 C CA . ALA B 1 362 ? 1.014 6.554 13.302 1.00 24.37 ? 362 ALA B CA 1 ATOM 7129 C C . ALA B 1 362 ? 0.782 5.069 13.093 1.00 24.26 ? 362 ALA B C 1 ATOM 7130 O O . ALA B 1 362 ? 1.733 4.314 12.880 1.00 24.21 ? 362 ALA B O 1 ATOM 7131 C CB . ALA B 1 362 ? 0.856 7.306 11.974 1.00 24.88 ? 362 ALA B CB 1 ATOM 7132 N N . LEU B 1 363 ? -0.479 4.652 13.228 1.00 24.23 ? 363 LEU B N 1 ATOM 7133 C CA . LEU B 1 363 ? -0.876 3.266 13.012 1.00 22.55 ? 363 LEU B CA 1 ATOM 7134 C C . LEU B 1 363 ? -1.639 3.183 11.696 1.00 22.76 ? 363 LEU B C 1 ATOM 7135 O O . LEU B 1 363 ? -2.721 3.757 11.549 1.00 23.21 ? 363 LEU B O 1 ATOM 7136 C CB . LEU B 1 363 ? -1.743 2.738 14.163 1.00 22.88 ? 363 LEU B CB 1 ATOM 7137 C CG . LEU B 1 363 ? -2.319 1.309 14.042 1.00 22.00 ? 363 LEU B CG 1 ATOM 7138 C CD1 . LEU B 1 363 ? -1.226 0.244 13.946 1.00 19.80 ? 363 LEU B CD1 1 ATOM 7139 C CD2 . LEU B 1 363 ? -3.226 1.027 15.209 1.00 19.53 ? 363 LEU B CD2 1 ATOM 7140 N N . ASP B 1 364 ? -1.057 2.453 10.751 1.00 23.32 ? 364 ASP B N 1 ATOM 7141 C CA . ASP B 1 364 ? -1.638 2.256 9.435 1.00 23.03 ? 364 ASP B CA 1 ATOM 7142 C C . ASP B 1 364 ? -2.464 0.971 9.432 1.00 23.64 ? 364 ASP B C 1 ATOM 7143 O O . ASP B 1 364 ? -1.937 -0.112 9.689 1.00 23.31 ? 364 ASP B O 1 ATOM 7144 C CB . ASP B 1 364 ? -0.524 2.186 8.385 1.00 24.85 ? 364 ASP B CB 1 ATOM 7145 C CG . ASP B 1 364 ? -1.026 2.418 6.968 1.00 25.85 ? 364 ASP B CG 1 ATOM 7146 O OD1 . ASP B 1 364 ? -2.205 2.791 6.787 1.00 26.89 ? 364 ASP B OD1 1 ATOM 7147 O OD2 . ASP B 1 364 ? -0.228 2.232 6.029 1.00 28.40 ? 364 ASP B OD2 1 ATOM 7148 N N . LEU B 1 365 ? -3.762 1.115 9.158 1.00 24.61 ? 365 LEU B N 1 ATOM 7149 C CA . LEU B 1 365 ? -4.703 -0.006 9.114 1.00 25.56 ? 365 LEU B CA 1 ATOM 7150 C C . LEU B 1 365 ? -5.192 -0.287 7.687 1.00 27.42 ? 365 LEU B C 1 ATOM 7151 O O . LEU B 1 365 ? -6.157 -1.039 7.491 1.00 28.15 ? 365 LEU B O 1 ATOM 7152 C CB . LEU B 1 365 ? -5.908 0.283 10.025 1.00 24.97 ? 365 LEU B CB 1 ATOM 7153 C CG . LEU B 1 365 ? -5.723 0.567 11.522 1.00 25.08 ? 365 LEU B CG 1 ATOM 7154 C CD1 . LEU B 1 365 ? -7.019 1.122 12.108 1.00 24.86 ? 365 LEU B CD1 1 ATOM 7155 C CD2 . LEU B 1 365 ? -5.291 -0.686 12.260 1.00 22.19 ? 365 LEU B CD2 1 ATOM 7156 N N . THR B 1 366 ? -4.524 0.315 6.699 1.00 27.70 ? 366 THR B N 1 ATOM 7157 C CA . THR B 1 366 ? -4.891 0.150 5.289 1.00 28.14 ? 366 THR B CA 1 ATOM 7158 C C . THR B 1 366 ? -4.194 -0.990 4.533 1.00 28.78 ? 366 THR B C 1 ATOM 7159 O O . THR B 1 366 ? -4.732 -1.472 3.535 1.00 30.16 ? 366 THR B O 1 ATOM 7160 C CB . THR B 1 366 ? -4.724 1.474 4.477 1.00 27.24 ? 366 THR B CB 1 ATOM 7161 O OG1 . THR B 1 366 ? -3.344 1.852 4.416 1.00 25.91 ? 366 THR B OG1 1 ATOM 7162 C CG2 . THR B 1 366 ? -5.528 2.607 5.108 1.00 28.15 ? 366 THR B CG2 1 ATOM 7163 N N . GLY B 1 367 ? -3.030 -1.435 5.016 1.00 28.91 ? 367 GLY B N 1 ATOM 7164 C CA . GLY B 1 367 ? -2.291 -2.501 4.341 1.00 29.69 ? 367 GLY B CA 1 ATOM 7165 C C . GLY B 1 367 ? -2.362 -3.923 4.891 1.00 31.00 ? 367 GLY B C 1 ATOM 7166 O O . GLY B 1 367 ? -3.275 -4.276 5.654 1.00 32.00 ? 367 GLY B O 1 ATOM 7167 N N . THR B 1 368 ? -1.423 -4.757 4.432 1.00 29.98 ? 368 THR B N 1 ATOM 7168 C CA . THR B 1 368 ? -1.298 -6.157 4.858 1.00 28.53 ? 368 THR B CA 1 ATOM 7169 C C . THR B 1 368 ? 0.074 -6.316 5.552 1.00 27.39 ? 368 THR B C 1 ATOM 7170 O O . THR B 1 368 ? 1.104 -6.009 4.939 1.00 26.57 ? 368 THR B O 1 ATOM 7171 C CB . THR B 1 368 ? -1.416 -7.181 3.668 1.00 30.52 ? 368 THR B CB 1 ATOM 7172 O OG1 . THR B 1 368 ? -0.399 -6.923 2.688 1.00 30.03 ? 368 THR B OG1 1 ATOM 7173 C CG2 . THR B 1 368 ? -2.809 -7.126 3.019 1.00 28.75 ? 368 THR B CG2 1 ATOM 7174 N N . PRO B 1 369 ? 0.107 -6.701 6.858 1.00 25.77 ? 369 PRO B N 1 ATOM 7175 C CA . PRO B 1 369 ? -0.958 -7.015 7.827 1.00 23.36 ? 369 PRO B CA 1 ATOM 7176 C C . PRO B 1 369 ? -1.694 -5.781 8.358 1.00 23.00 ? 369 PRO B C 1 ATOM 7177 O O . PRO B 1 369 ? -1.396 -4.659 7.939 1.00 23.59 ? 369 PRO B O 1 ATOM 7178 C CB . PRO B 1 369 ? -0.194 -7.725 8.936 1.00 24.36 ? 369 PRO B CB 1 ATOM 7179 C CG . PRO B 1 369 ? 1.134 -7.043 8.918 1.00 24.00 ? 369 PRO B CG 1 ATOM 7180 C CD . PRO B 1 369 ? 1.430 -6.993 7.451 1.00 24.45 ? 369 PRO B CD 1 ATOM 7181 N N . LEU B 1 370 ? -2.643 -5.993 9.268 1.00 21.99 ? 370 LEU B N 1 ATOM 7182 C CA . LEU B 1 370 ? -3.434 -4.905 9.847 1.00 20.65 ? 370 LEU B CA 1 ATOM 7183 C C . LEU B 1 370 ? -2.663 -3.957 10.775 1.00 19.43 ? 370 LEU B C 1 ATOM 7184 O O . LEU B 1 370 ? -2.793 -2.737 10.653 1.00 18.61 ? 370 LEU B O 1 ATOM 7185 C CB . LEU B 1 370 ? -4.668 -5.462 10.573 1.00 21.48 ? 370 LEU B CB 1 ATOM 7186 C CG . LEU B 1 370 ? -5.800 -4.463 10.852 1.00 21.43 ? 370 LEU B CG 1 ATOM 7187 C CD1 . LEU B 1 370 ? -6.482 -4.051 9.546 1.00 23.37 ? 370 LEU B CD1 1 ATOM 7188 C CD2 . LEU B 1 370 ? -6.803 -5.068 11.788 1.00 22.04 ? 370 LEU B CD2 1 ATOM 7189 N N . PHE B 1 371 ? -1.870 -4.518 11.688 1.00 17.53 ? 371 PHE B N 1 ATOM 7190 C CA . PHE B 1 371 ? -1.090 -3.716 12.625 1.00 18.31 ? 371 PHE B CA 1 ATOM 7191 C C . PHE B 1 371 ? 0.307 -3.396 12.092 1.00 17.55 ? 371 PHE B C 1 ATOM 7192 O O . PHE B 1 371 ? 1.240 -4.206 12.180 1.00 19.29 ? 371 PHE B O 1 ATOM 7193 C CB . PHE B 1 371 ? -1.019 -4.390 14.009 1.00 20.14 ? 371 PHE B CB 1 ATOM 7194 C CG . PHE B 1 371 ? -2.319 -4.374 14.762 1.00 21.46 ? 371 PHE B CG 1 ATOM 7195 C CD1 . PHE B 1 371 ? -2.510 -3.479 15.832 1.00 25.85 ? 371 PHE B CD1 1 ATOM 7196 C CD2 . PHE B 1 371 ? -3.376 -5.234 14.397 1.00 24.28 ? 371 PHE B CD2 1 ATOM 7197 C CE1 . PHE B 1 371 ? -3.751 -3.433 16.535 1.00 23.79 ? 371 PHE B CE1 1 ATOM 7198 C CE2 . PHE B 1 371 ? -4.621 -5.207 15.079 1.00 22.23 ? 371 PHE B CE2 1 ATOM 7199 C CZ . PHE B 1 371 ? -4.809 -4.304 16.151 1.00 25.05 ? 371 PHE B CZ 1 ATOM 7200 N N . VAL B 1 372 ? 0.411 -2.231 11.462 1.00 15.62 ? 372 VAL B N 1 ATOM 7201 C CA . VAL B 1 372 ? 1.666 -1.736 10.900 1.00 14.54 ? 372 VAL B CA 1 ATOM 7202 C C . VAL B 1 372 ? 1.881 -0.369 11.540 1.00 15.65 ? 372 VAL B C 1 ATOM 7203 O O . VAL B 1 372 ? 1.058 0.542 11.375 1.00 14.83 ? 372 VAL B O 1 ATOM 7204 C CB . VAL B 1 372 ? 1.607 -1.618 9.329 1.00 13.41 ? 372 VAL B CB 1 ATOM 7205 C CG1 . VAL B 1 372 ? 2.836 -0.929 8.783 1.00 7.11 ? 372 VAL B CG1 1 ATOM 7206 C CG2 . VAL B 1 372 ? 1.497 -2.993 8.694 1.00 12.66 ? 372 VAL B CG2 1 ATOM 7207 N N . TRP B 1 373 ? 2.966 -0.257 12.303 1.00 16.05 ? 373 TRP B N 1 ATOM 7208 C CA . TRP B 1 373 ? 3.319 0.979 12.989 1.00 17.73 ? 373 TRP B CA 1 ATOM 7209 C C . TRP B 1 373 ? 4.317 1.813 12.194 1.00 19.16 ? 373 TRP B C 1 ATOM 7210 O O . TRP B 1 373 ? 5.413 1.356 11.867 1.00 19.92 ? 373 TRP B O 1 ATOM 7211 C CB . TRP B 1 373 ? 3.863 0.684 14.387 1.00 16.91 ? 373 TRP B CB 1 ATOM 7212 C CG . TRP B 1 373 ? 2.829 0.202 15.352 1.00 16.96 ? 373 TRP B CG 1 ATOM 7213 C CD1 . TRP B 1 373 ? 2.559 -1.097 15.682 1.00 17.05 ? 373 TRP B CD1 1 ATOM 7214 C CD2 . TRP B 1 373 ? 1.929 1.009 16.123 1.00 16.67 ? 373 TRP B CD2 1 ATOM 7215 N NE1 . TRP B 1 373 ? 1.550 -1.153 16.612 1.00 17.00 ? 373 TRP B NE1 1 ATOM 7216 C CE2 . TRP B 1 373 ? 1.140 0.123 16.904 1.00 16.48 ? 373 TRP B CE2 1 ATOM 7217 C CE3 . TRP B 1 373 ? 1.707 2.400 16.233 1.00 15.62 ? 373 TRP B CE3 1 ATOM 7218 C CZ2 . TRP B 1 373 ? 0.134 0.580 17.792 1.00 17.12 ? 373 TRP B CZ2 1 ATOM 7219 C CZ3 . TRP B 1 373 ? 0.700 2.862 17.123 1.00 17.60 ? 373 TRP B CZ3 1 ATOM 7220 C CH2 . TRP B 1 373 ? -0.070 1.946 17.888 1.00 15.85 ? 373 TRP B CH2 1 ATOM 7221 N N . LYS B 1 374 ? 3.922 3.046 11.890 1.00 18.25 ? 374 LYS B N 1 ATOM 7222 C CA . LYS B 1 374 ? 4.755 3.946 11.114 1.00 17.72 ? 374 LYS B CA 1 ATOM 7223 C C . LYS B 1 374 ? 5.228 5.150 11.906 1.00 17.43 ? 374 LYS B C 1 ATOM 7224 O O . LYS B 1 374 ? 4.498 5.681 12.734 1.00 17.45 ? 374 LYS B O 1 ATOM 7225 C CB . LYS B 1 374 ? 4.015 4.392 9.845 1.00 19.02 ? 374 LYS B CB 1 ATOM 7226 C CG . LYS B 1 374 ? 3.723 3.256 8.853 1.00 18.22 ? 374 LYS B CG 1 ATOM 7227 C CD . LYS B 1 374 ? 3.177 3.760 7.525 1.00 22.37 ? 374 LYS B CD 1 ATOM 7228 C CE . LYS B 1 374 ? 3.170 2.654 6.479 1.00 21.39 ? 374 LYS B CE 1 ATOM 7229 N NZ . LYS B 1 374 ? 2.709 3.127 5.151 1.00 25.03 ? 374 LYS B NZ 1 ATOM 7230 N N . VAL B 1 375 ? 6.506 5.485 11.739 1.00 17.91 ? 375 VAL B N 1 ATOM 7231 C CA . VAL B 1 375 ? 7.093 6.647 12.397 1.00 16.63 ? 375 VAL B CA 1 ATOM 7232 C C . VAL B 1 375 ? 7.535 7.539 11.247 1.00 16.54 ? 375 VAL B C 1 ATOM 7233 O O . VAL B 1 375 ? 8.402 7.155 10.450 1.00 15.46 ? 375 VAL B O 1 ATOM 7234 C CB . VAL B 1 375 ? 8.286 6.312 13.329 1.00 15.67 ? 375 VAL B CB 1 ATOM 7235 C CG1 . VAL B 1 375 ? 8.671 7.554 14.138 1.00 13.77 ? 375 VAL B CG1 1 ATOM 7236 C CG2 . VAL B 1 375 ? 7.930 5.189 14.280 1.00 14.98 ? 375 VAL B CG2 1 ATOM 7237 N N . ASN B 1 376 ? 6.872 8.697 11.151 1.00 16.70 ? 376 ASN B N 1 ATOM 7238 C CA . ASN B 1 376 ? 7.063 9.716 10.107 1.00 20.13 ? 376 ASN B CA 1 ATOM 7239 C C . ASN B 1 376 ? 6.623 9.206 8.722 1.00 18.31 ? 376 ASN B C 1 ATOM 7240 O O . ASN B 1 376 ? 7.235 9.511 7.692 1.00 20.12 ? 376 ASN B O 1 ATOM 7241 C CB . ASN B 1 376 ? 8.503 10.285 10.099 1.00 24.27 ? 376 ASN B CB 1 ATOM 7242 C CG . ASN B 1 376 ? 8.558 11.749 9.663 1.00 29.79 ? 376 ASN B CG 1 ATOM 7243 O OD1 . ASN B 1 376 ? 7.553 12.469 9.738 1.00 28.57 ? 376 ASN B OD1 1 ATOM 7244 N ND2 . ASN B 1 376 ? 9.731 12.185 9.210 1.00 34.22 ? 376 ASN B ND2 1 ATOM 7245 N N . GLY B 1 377 ? 5.544 8.424 8.734 1.00 16.52 ? 377 GLY B N 1 ATOM 7246 C CA . GLY B 1 377 ? 4.978 7.847 7.525 1.00 16.93 ? 377 GLY B CA 1 ATOM 7247 C C . GLY B 1 377 ? 5.707 6.644 6.951 1.00 16.45 ? 377 GLY B C 1 ATOM 7248 O O . GLY B 1 377 ? 5.494 6.307 5.781 1.00 16.96 ? 377 GLY B O 1 ATOM 7249 N N . SER B 1 378 ? 6.528 5.981 7.772 1.00 15.50 ? 378 SER B N 1 ATOM 7250 C CA . SER B 1 378 ? 7.310 4.815 7.345 1.00 14.82 ? 378 SER B CA 1 ATOM 7251 C C . SER B 1 378 ? 7.592 3.803 8.456 1.00 15.34 ? 378 SER B C 1 ATOM 7252 O O . SER B 1 378 ? 8.107 4.159 9.535 1.00 13.42 ? 378 SER B O 1 ATOM 7253 C CB . SER B 1 378 ? 8.646 5.261 6.734 1.00 14.69 ? 378 SER B CB 1 ATOM 7254 O OG . SER B 1 378 ? 9.495 4.153 6.456 1.00 16.16 ? 378 SER B OG 1 ATOM 7255 N N . ASP B 1 379 ? 7.237 2.547 8.182 1.00 13.69 ? 379 ASP B N 1 ATOM 7256 C CA . ASP B 1 379 ? 7.485 1.446 9.115 1.00 14.44 ? 379 ASP B CA 1 ATOM 7257 C C . ASP B 1 379 ? 8.891 0.921 8.857 1.00 14.24 ? 379 ASP B C 1 ATOM 7258 O O . ASP B 1 379 ? 9.260 0.660 7.700 1.00 15.57 ? 379 ASP B O 1 ATOM 7259 C CB . ASP B 1 379 ? 6.432 0.323 8.993 1.00 12.90 ? 379 ASP B CB 1 ATOM 7260 C CG . ASP B 1 379 ? 6.209 -0.150 7.560 1.00 14.96 ? 379 ASP B CG 1 ATOM 7261 O OD1 . ASP B 1 379 ? 5.861 0.682 6.697 1.00 14.76 ? 379 ASP B OD1 1 ATOM 7262 O OD2 . ASP B 1 379 ? 6.361 -1.364 7.308 1.00 17.07 ? 379 ASP B OD2 1 ATOM 7263 N N . ILE B 1 380 ? 9.685 0.820 9.921 1.00 12.65 ? 380 ILE B N 1 ATOM 7264 C CA . ILE B 1 380 ? 11.064 0.354 9.804 1.00 14.61 ? 380 ILE B CA 1 ATOM 7265 C C . ILE B 1 380 ? 11.201 -1.105 9.331 1.00 15.94 ? 380 ILE B C 1 ATOM 7266 O O . ILE B 1 380 ? 10.375 -1.962 9.656 1.00 16.59 ? 380 ILE B O 1 ATOM 7267 C CB . ILE B 1 380 ? 11.884 0.612 11.125 1.00 13.88 ? 380 ILE B CB 1 ATOM 7268 C CG1 . ILE B 1 380 ? 13.375 0.806 10.800 1.00 12.23 ? 380 ILE B CG1 1 ATOM 7269 C CG2 . ILE B 1 380 ? 11.680 -0.534 12.143 1.00 12.81 ? 380 ILE B CG2 1 ATOM 7270 C CD1 . ILE B 1 380 ? 14.210 1.370 11.924 1.00 8.26 ? 380 ILE B CD1 1 ATOM 7271 N N . ASN B 1 381 ? 12.198 -1.335 8.485 1.00 17.61 ? 381 ASN B N 1 ATOM 7272 C CA . ASN B 1 381 ? 12.500 -2.657 7.967 1.00 19.92 ? 381 ASN B CA 1 ATOM 7273 C C . ASN B 1 381 ? 13.997 -2.689 7.677 1.00 19.43 ? 381 ASN B C 1 ATOM 7274 O O . ASN B 1 381 ? 14.436 -2.368 6.567 1.00 19.34 ? 381 ASN B O 1 ATOM 7275 C CB . ASN B 1 381 ? 11.664 -2.974 6.712 1.00 20.92 ? 381 ASN B CB 1 ATOM 7276 C CG . ASN B 1 381 ? 11.623 -4.464 6.400 1.00 21.35 ? 381 ASN B CG 1 ATOM 7277 O OD1 . ASN B 1 381 ? 12.423 -4.965 5.610 1.00 22.24 ? 381 ASN B OD1 1 ATOM 7278 N ND2 . ASN B 1 381 ? 10.695 -5.177 7.033 1.00 21.76 ? 381 ASN B ND2 1 ATOM 7279 N N . VAL B 1 382 ? 14.769 -3.054 8.705 1.00 18.96 ? 382 VAL B N 1 ATOM 7280 C CA . VAL B 1 382 ? 16.230 -3.142 8.624 1.00 18.52 ? 382 VAL B CA 1 ATOM 7281 C C . VAL B 1 382 ? 16.680 -4.343 7.802 1.00 17.71 ? 382 VAL B C 1 ATOM 7282 O O . VAL B 1 382 ? 15.963 -5.342 7.729 1.00 19.10 ? 382 VAL B O 1 ATOM 7283 C CB . VAL B 1 382 ? 16.891 -3.169 10.036 1.00 18.79 ? 382 VAL B CB 1 ATOM 7284 C CG1 . VAL B 1 382 ? 16.565 -1.884 10.793 1.00 19.66 ? 382 VAL B CG1 1 ATOM 7285 C CG2 . VAL B 1 382 ? 16.456 -4.390 10.839 1.00 19.15 ? 382 VAL B CG2 1 ATOM 7286 N N . ASP B 1 383 ? 17.844 -4.224 7.166 1.00 17.62 ? 383 ASP B N 1 ATOM 7287 C CA . ASP B 1 383 ? 18.392 -5.292 6.329 1.00 17.07 ? 383 ASP B CA 1 ATOM 7288 C C . ASP B 1 383 ? 19.465 -6.067 7.093 1.00 17.26 ? 383 ASP B C 1 ATOM 7289 O O . ASP B 1 383 ? 20.562 -5.558 7.349 1.00 17.28 ? 383 ASP B O 1 ATOM 7290 C CB . ASP B 1 383 ? 18.942 -4.698 5.009 1.00 18.17 ? 383 ASP B CB 1 ATOM 7291 C CG . ASP B 1 383 ? 19.342 -5.764 3.961 1.00 17.48 ? 383 ASP B CG 1 ATOM 7292 O OD1 . ASP B 1 383 ? 19.267 -6.985 4.218 1.00 16.41 ? 383 ASP B OD1 1 ATOM 7293 O OD2 . ASP B 1 383 ? 19.753 -5.357 2.853 1.00 18.71 ? 383 ASP B OD2 1 ATOM 7294 N N . TRP B 1 384 ? 19.126 -7.312 7.435 1.00 17.57 ? 384 TRP B N 1 ATOM 7295 C CA . TRP B 1 384 ? 20.002 -8.241 8.154 1.00 15.09 ? 384 TRP B CA 1 ATOM 7296 C C . TRP B 1 384 ? 21.251 -8.579 7.350 1.00 16.50 ? 384 TRP B C 1 ATOM 7297 O O . TRP B 1 384 ? 22.306 -8.860 7.922 1.00 16.97 ? 384 TRP B O 1 ATOM 7298 C CB . TRP B 1 384 ? 19.249 -9.537 8.467 1.00 14.37 ? 384 TRP B CB 1 ATOM 7299 C CG . TRP B 1 384 ? 18.272 -9.460 9.627 1.00 15.13 ? 384 TRP B CG 1 ATOM 7300 C CD1 . TRP B 1 384 ? 18.261 -8.541 10.646 1.00 14.78 ? 384 TRP B CD1 1 ATOM 7301 C CD2 . TRP B 1 384 ? 17.198 -10.370 9.902 1.00 14.33 ? 384 TRP B CD2 1 ATOM 7302 N NE1 . TRP B 1 384 ? 17.256 -8.824 11.536 1.00 14.74 ? 384 TRP B NE1 1 ATOM 7303 C CE2 . TRP B 1 384 ? 16.584 -9.939 11.111 1.00 15.08 ? 384 TRP B CE2 1 ATOM 7304 C CE3 . TRP B 1 384 ? 16.690 -11.509 9.247 1.00 12.88 ? 384 TRP B CE3 1 ATOM 7305 C CZ2 . TRP B 1 384 ? 15.473 -10.614 11.687 1.00 14.51 ? 384 TRP B CZ2 1 ATOM 7306 C CZ3 . TRP B 1 384 ? 15.580 -12.185 9.814 1.00 15.33 ? 384 TRP B CZ3 1 ATOM 7307 C CH2 . TRP B 1 384 ? 14.985 -11.725 11.029 1.00 14.48 ? 384 TRP B CH2 1 ATOM 7308 N N . GLY B 1 385 ? 21.108 -8.534 6.023 1.00 16.38 ? 385 GLY B N 1 ATOM 7309 C CA . GLY B 1 385 ? 22.198 -8.817 5.100 1.00 16.84 ? 385 GLY B CA 1 ATOM 7310 C C . GLY B 1 385 ? 23.115 -7.631 4.850 1.00 17.46 ? 385 GLY B C 1 ATOM 7311 O O . GLY B 1 385 ? 24.306 -7.820 4.590 1.00 18.15 ? 385 GLY B O 1 ATOM 7312 N N . LYS B 1 386 ? 22.564 -6.417 4.922 1.00 18.38 ? 386 LYS B N 1 ATOM 7313 C CA . LYS B 1 386 ? 23.339 -5.187 4.725 1.00 20.01 ? 386 LYS B CA 1 ATOM 7314 C C . LYS B 1 386 ? 22.959 -4.104 5.763 1.00 20.14 ? 386 LYS B C 1 ATOM 7315 O O . LYS B 1 386 ? 22.035 -3.301 5.553 1.00 19.68 ? 386 LYS B O 1 ATOM 7316 C CB . LYS B 1 386 ? 23.198 -4.664 3.288 1.00 20.61 ? 386 LYS B CB 1 ATOM 7317 C CG . LYS B 1 386 ? 24.212 -3.576 2.915 1.00 22.90 ? 386 LYS B CG 1 ATOM 7318 C CD . LYS B 1 386 ? 23.998 -3.080 1.489 1.00 26.01 ? 386 LYS B CD 1 ATOM 7319 C CE . LYS B 1 386 ? 24.954 -1.954 1.135 1.00 24.28 ? 386 LYS B CE 1 ATOM 7320 N NZ . LYS B 1 386 ? 26.356 -2.399 1.062 1.00 26.36 ? 386 LYS B NZ 1 ATOM 7321 N N . PRO B 1 387 ? 23.653 -4.097 6.920 1.00 20.69 ? 387 PRO B N 1 ATOM 7322 C CA . PRO B 1 387 ? 23.421 -3.138 8.007 1.00 20.42 ? 387 PRO B CA 1 ATOM 7323 C C . PRO B 1 387 ? 23.800 -1.709 7.659 1.00 20.44 ? 387 PRO B C 1 ATOM 7324 O O . PRO B 1 387 ? 24.464 -1.470 6.653 1.00 20.48 ? 387 PRO B O 1 ATOM 7325 C CB . PRO B 1 387 ? 24.318 -3.673 9.119 1.00 21.13 ? 387 PRO B CB 1 ATOM 7326 C CG . PRO B 1 387 ? 24.360 -5.113 8.849 1.00 20.77 ? 387 PRO B CG 1 ATOM 7327 C CD . PRO B 1 387 ? 24.594 -5.132 7.378 1.00 20.44 ? 387 PRO B CD 1 ATOM 7328 N N . ILE B 1 388 ? 23.396 -0.770 8.515 1.00 20.14 ? 388 ILE B N 1 ATOM 7329 C CA . ILE B 1 388 ? 23.682 0.653 8.320 1.00 20.44 ? 388 ILE B CA 1 ATOM 7330 C C . ILE B 1 388 ? 25.180 0.956 8.418 1.00 21.33 ? 388 ILE B C 1 ATOM 7331 O O . ILE B 1 388 ? 25.684 1.838 7.719 1.00 22.15 ? 388 ILE B O 1 ATOM 7332 C CB . ILE B 1 388 ? 22.792 1.542 9.270 1.00 19.89 ? 388 ILE B CB 1 ATOM 7333 C CG1 . ILE B 1 388 ? 21.329 1.494 8.789 1.00 19.81 ? 388 ILE B CG1 1 ATOM 7334 C CG2 . ILE B 1 388 ? 23.275 3.009 9.341 1.00 18.56 ? 388 ILE B CG2 1 ATOM 7335 C CD1 . ILE B 1 388 ? 21.112 1.902 7.317 1.00 16.54 ? 388 ILE B CD1 1 ATOM 7336 N N . ILE B 1 389 ? 25.891 0.143 9.201 1.00 21.07 ? 389 ILE B N 1 ATOM 7337 C CA . ILE B 1 389 ? 27.329 0.290 9.378 1.00 20.45 ? 389 ILE B CA 1 ATOM 7338 C C . ILE B 1 389 ? 28.085 -0.153 8.116 1.00 20.93 ? 389 ILE B C 1 ATOM 7339 O O . ILE B 1 389 ? 29.168 0.356 7.845 1.00 22.97 ? 389 ILE B O 1 ATOM 7340 C CB . ILE B 1 389 ? 27.829 -0.403 10.704 1.00 18.69 ? 389 ILE B CB 1 ATOM 7341 C CG1 . ILE B 1 389 ? 27.337 0.377 11.939 1.00 18.08 ? 389 ILE B CG1 1 ATOM 7342 C CG2 . ILE B 1 389 ? 29.351 -0.536 10.752 1.00 20.24 ? 389 ILE B CG2 1 ATOM 7343 C CD1 . ILE B 1 389 ? 27.663 1.881 11.979 1.00 17.32 ? 389 ILE B CD1 1 ATOM 7344 N N . ASP B 1 390 ? 27.477 -1.022 7.302 1.00 20.43 ? 390 ASP B N 1 ATOM 7345 C CA . ASP B 1 390 ? 28.111 -1.473 6.056 1.00 20.18 ? 390 ASP B CA 1 ATOM 7346 C C . ASP B 1 390 ? 28.119 -0.307 5.074 1.00 17.05 ? 390 ASP B C 1 ATOM 7347 O O . ASP B 1 390 ? 29.098 -0.099 4.367 1.00 17.08 ? 390 ASP B O 1 ATOM 7348 C CB . ASP B 1 390 ? 27.395 -2.694 5.457 1.00 24.01 ? 390 ASP B CB 1 ATOM 7349 C CG . ASP B 1 390 ? 28.284 -3.486 4.503 1.00 25.16 ? 390 ASP B CG 1 ATOM 7350 O OD1 . ASP B 1 390 ? 29.411 -3.851 4.896 1.00 27.58 ? 390 ASP B OD1 1 ATOM 7351 O OD2 . ASP B 1 390 ? 27.859 -3.744 3.360 1.00 26.15 ? 390 ASP B OD2 1 ATOM 7352 N N . TYR B 1 391 ? 27.067 0.507 5.143 1.00 14.57 ? 391 TYR B N 1 ATOM 7353 C CA . TYR B 1 391 ? 26.922 1.700 4.318 1.00 14.03 ? 391 TYR B CA 1 ATOM 7354 C C . TYR B 1 391 ? 27.990 2.734 4.696 1.00 13.16 ? 391 TYR B C 1 ATOM 7355 O O . TYR B 1 391 ? 28.623 3.325 3.827 1.00 15.03 ? 391 TYR B O 1 ATOM 7356 C CB . TYR B 1 391 ? 25.533 2.306 4.497 1.00 14.58 ? 391 TYR B CB 1 ATOM 7357 C CG . TYR B 1 391 ? 24.415 1.575 3.798 1.00 16.89 ? 391 TYR B CG 1 ATOM 7358 C CD1 . TYR B 1 391 ? 23.680 0.581 4.459 1.00 18.83 ? 391 TYR B CD1 1 ATOM 7359 C CD2 . TYR B 1 391 ? 24.048 1.906 2.479 1.00 17.53 ? 391 TYR B CD2 1 ATOM 7360 C CE1 . TYR B 1 391 ? 22.588 -0.075 3.824 1.00 20.17 ? 391 TYR B CE1 1 ATOM 7361 C CE2 . TYR B 1 391 ? 22.965 1.262 1.827 1.00 17.68 ? 391 TYR B CE2 1 ATOM 7362 C CZ . TYR B 1 391 ? 22.242 0.273 2.511 1.00 19.11 ? 391 TYR B CZ 1 ATOM 7363 O OH . TYR B 1 391 ? 21.197 -0.369 1.892 1.00 19.83 ? 391 TYR B OH 1 ATOM 7364 N N . ILE B 1 392 ? 28.229 2.869 6.000 1.00 12.48 ? 392 ILE B N 1 ATOM 7365 C CA . ILE B 1 392 ? 29.220 3.779 6.573 1.00 11.09 ? 392 ILE B CA 1 ATOM 7366 C C . ILE B 1 392 ? 30.642 3.361 6.173 1.00 11.81 ? 392 ILE B C 1 ATOM 7367 O O . ILE B 1 392 ? 31.480 4.210 5.858 1.00 12.35 ? 392 ILE B O 1 ATOM 7368 C CB . ILE B 1 392 ? 29.095 3.793 8.149 1.00 11.11 ? 392 ILE B CB 1 ATOM 7369 C CG1 . ILE B 1 392 ? 27.720 4.336 8.586 1.00 11.24 ? 392 ILE B CG1 1 ATOM 7370 C CG2 . ILE B 1 392 ? 30.268 4.537 8.815 1.00 9.45 ? 392 ILE B CG2 1 ATOM 7371 C CD1 . ILE B 1 392 ? 27.431 5.789 8.203 1.00 9.59 ? 392 ILE B CD1 1 ATOM 7372 N N . LEU B 1 393 ? 30.892 2.053 6.188 1.00 12.59 ? 393 LEU B N 1 ATOM 7373 C CA . LEU B 1 393 ? 32.198 1.501 5.856 1.00 15.22 ? 393 LEU B CA 1 ATOM 7374 C C . LEU B 1 393 ? 32.530 1.464 4.373 1.00 15.12 ? 393 LEU B C 1 ATOM 7375 O O . LEU B 1 393 ? 33.692 1.328 4.009 1.00 16.05 ? 393 LEU B O 1 ATOM 7376 C CB . LEU B 1 393 ? 32.348 0.115 6.470 1.00 16.78 ? 393 LEU B CB 1 ATOM 7377 C CG . LEU B 1 393 ? 32.414 0.091 7.996 1.00 18.57 ? 393 LEU B CG 1 ATOM 7378 C CD1 . LEU B 1 393 ? 32.252 -1.335 8.448 1.00 21.33 ? 393 LEU B CD1 1 ATOM 7379 C CD2 . LEU B 1 393 ? 33.707 0.691 8.524 1.00 19.98 ? 393 LEU B CD2 1 ATOM 7380 N N . THR B 1 394 ? 31.509 1.579 3.527 1.00 17.11 ? 394 THR B N 1 ATOM 7381 C CA . THR B 1 394 ? 31.699 1.586 2.075 1.00 17.96 ? 394 THR B CA 1 ATOM 7382 C C . THR B 1 394 ? 31.447 2.970 1.460 1.00 18.84 ? 394 THR B C 1 ATOM 7383 O O . THR B 1 394 ? 31.433 3.119 0.233 1.00 18.71 ? 394 THR B O 1 ATOM 7384 C CB . THR B 1 394 ? 30.831 0.510 1.366 1.00 18.27 ? 394 THR B CB 1 ATOM 7385 O OG1 . THR B 1 394 ? 29.463 0.630 1.775 1.00 15.35 ? 394 THR B OG1 1 ATOM 7386 C CG2 . THR B 1 394 ? 31.349 -0.908 1.676 1.00 17.34 ? 394 THR B CG2 1 ATOM 7387 N N . GLY B 1 395 ? 31.266 3.973 2.328 1.00 19.68 ? 395 GLY B N 1 ATOM 7388 C CA . GLY B 1 395 ? 31.026 5.355 1.906 1.00 21.30 ? 395 GLY B CA 1 ATOM 7389 C C . GLY B 1 395 ? 29.707 5.587 1.189 1.00 22.16 ? 395 GLY B C 1 ATOM 7390 O O . GLY B 1 395 ? 29.533 6.565 0.455 1.00 22.32 ? 395 GLY B O 1 ATOM 7391 N N . ASN B 1 396 ? 28.773 4.674 1.435 1.00 22.03 ? 396 ASN B N 1 ATOM 7392 C CA . ASN B 1 396 ? 27.456 4.682 0.828 1.00 22.22 ? 396 ASN B CA 1 ATOM 7393 C C . ASN B 1 396 ? 26.442 5.455 1.672 1.00 21.95 ? 396 ASN B C 1 ATOM 7394 O O . ASN B 1 396 ? 26.139 5.075 2.805 1.00 23.16 ? 396 ASN B O 1 ATOM 7395 C CB . ASN B 1 396 ? 27.037 3.227 0.645 1.00 22.51 ? 396 ASN B CB 1 ATOM 7396 C CG . ASN B 1 396 ? 25.874 3.045 -0.301 1.00 22.77 ? 396 ASN B CG 1 ATOM 7397 O OD1 . ASN B 1 396 ? 25.121 3.973 -0.629 1.00 23.59 ? 396 ASN B OD1 1 ATOM 7398 N ND2 . ASN B 1 396 ? 25.736 1.793 -0.720 1.00 21.94 ? 396 ASN B ND2 1 ATOM 7399 N N . THR B 1 397 ? 25.892 6.511 1.081 1.00 21.40 ? 397 THR B N 1 ATOM 7400 C CA . THR B 1 397 ? 24.913 7.366 1.753 1.00 20.95 ? 397 THR B CA 1 ATOM 7401 C C . THR B 1 397 ? 23.469 7.134 1.312 1.00 21.51 ? 397 THR B C 1 ATOM 7402 O O . THR B 1 397 ? 22.544 7.709 1.891 1.00 20.65 ? 397 THR B O 1 ATOM 7403 C CB . THR B 1 397 ? 25.249 8.868 1.570 1.00 20.58 ? 397 THR B CB 1 ATOM 7404 O OG1 . THR B 1 397 ? 25.569 9.127 0.196 1.00 21.29 ? 397 THR B OG1 1 ATOM 7405 C CG2 . THR B 1 397 ? 26.414 9.280 2.461 1.00 18.73 ? 397 THR B CG2 1 ATOM 7406 N N . SER B 1 398 ? 23.277 6.273 0.312 1.00 21.78 ? 398 SER B N 1 ATOM 7407 C CA . SER B 1 398 ? 21.948 5.975 -0.226 1.00 20.99 ? 398 SER B CA 1 ATOM 7408 C C . SER B 1 398 ? 21.131 5.007 0.647 1.00 21.26 ? 398 SER B C 1 ATOM 7409 O O . SER B 1 398 ? 20.758 3.915 0.207 1.00 21.88 ? 398 SER B O 1 ATOM 7410 C CB . SER B 1 398 ? 22.065 5.455 -1.669 1.00 20.25 ? 398 SER B CB 1 ATOM 7411 O OG . SER B 1 398 ? 22.721 6.391 -2.511 1.00 18.47 ? 398 SER B OG 1 ATOM 7412 N N . TYR B 1 399 ? 20.820 5.449 1.871 1.00 21.38 ? 399 TYR B N 1 ATOM 7413 C CA . TYR B 1 399 ? 20.049 4.661 2.845 1.00 21.07 ? 399 TYR B CA 1 ATOM 7414 C C . TYR B 1 399 ? 18.594 4.497 2.384 1.00 21.30 ? 399 TYR B C 1 ATOM 7415 O O . TYR B 1 399 ? 17.976 5.469 1.940 1.00 21.75 ? 399 TYR B O 1 ATOM 7416 C CB . TYR B 1 399 ? 20.048 5.326 4.234 1.00 19.29 ? 399 TYR B CB 1 ATOM 7417 C CG . TYR B 1 399 ? 21.375 5.897 4.697 1.00 18.27 ? 399 TYR B CG 1 ATOM 7418 C CD1 . TYR B 1 399 ? 22.484 5.063 4.956 1.00 18.02 ? 399 TYR B CD1 1 ATOM 7419 C CD2 . TYR B 1 399 ? 21.542 7.288 4.838 1.00 16.21 ? 399 TYR B CD2 1 ATOM 7420 C CE1 . TYR B 1 399 ? 23.739 5.612 5.335 1.00 15.21 ? 399 TYR B CE1 1 ATOM 7421 C CE2 . TYR B 1 399 ? 22.781 7.842 5.213 1.00 14.11 ? 399 TYR B CE2 1 ATOM 7422 C CZ . TYR B 1 399 ? 23.871 7.000 5.453 1.00 14.61 ? 399 TYR B CZ 1 ATOM 7423 O OH . TYR B 1 399 ? 25.086 7.554 5.777 1.00 16.32 ? 399 TYR B OH 1 ATOM 7424 N N . PRO B 1 400 ? 18.052 3.255 2.426 1.00 22.40 ? 400 PRO B N 1 ATOM 7425 C CA . PRO B 1 400 ? 16.668 2.974 2.015 1.00 22.88 ? 400 PRO B CA 1 ATOM 7426 C C . PRO B 1 400 ? 15.665 3.651 2.933 1.00 24.16 ? 400 PRO B C 1 ATOM 7427 O O . PRO B 1 400 ? 15.915 3.786 4.135 1.00 27.37 ? 400 PRO B O 1 ATOM 7428 C CB . PRO B 1 400 ? 16.576 1.456 2.147 1.00 23.03 ? 400 PRO B CB 1 ATOM 7429 C CG . PRO B 1 400 ? 17.967 1.009 1.883 1.00 21.85 ? 400 PRO B CG 1 ATOM 7430 C CD . PRO B 1 400 ? 18.759 1.988 2.693 1.00 22.20 ? 400 PRO B CD 1 ATOM 7431 N N . VAL B 1 401 ? 14.538 4.067 2.358 1.00 25.56 ? 401 VAL B N 1 ATOM 7432 C CA . VAL B 1 401 ? 13.445 4.749 3.076 1.00 26.70 ? 401 VAL B CA 1 ATOM 7433 C C . VAL B 1 401 ? 12.996 3.944 4.298 1.00 26.07 ? 401 VAL B C 1 ATOM 7434 O O . VAL B 1 401 ? 12.730 4.515 5.361 1.00 26.75 ? 401 VAL B O 1 ATOM 7435 C CB . VAL B 1 401 ? 12.220 4.993 2.133 1.00 26.49 ? 401 VAL B CB 1 ATOM 7436 C CG1 . VAL B 1 401 ? 11.133 5.830 2.835 1.00 25.62 ? 401 VAL B CG1 1 ATOM 7437 C CG2 . VAL B 1 401 ? 12.678 5.694 0.851 1.00 26.94 ? 401 VAL B CG2 1 ATOM 7438 N N . SER B 1 402 ? 13.022 2.617 4.142 1.00 25.09 ? 402 SER B N 1 ATOM 7439 C CA . SER B 1 402 ? 12.641 1.657 5.180 1.00 22.98 ? 402 SER B CA 1 ATOM 7440 C C . SER B 1 402 ? 13.546 1.633 6.405 1.00 20.18 ? 402 SER B C 1 ATOM 7441 O O . SER B 1 402 ? 13.113 1.221 7.471 1.00 17.57 ? 402 SER B O 1 ATOM 7442 C CB . SER B 1 402 ? 12.558 0.250 4.593 1.00 23.59 ? 402 SER B CB 1 ATOM 7443 O OG . SER B 1 402 ? 11.230 -0.057 4.210 1.00 29.22 ? 402 SER B OG 1 ATOM 7444 N N . ASP B 1 403 ? 14.785 2.098 6.257 1.00 20.63 ? 403 ASP B N 1 ATOM 7445 C CA . ASP B 1 403 ? 15.739 2.118 7.369 1.00 21.03 ? 403 ASP B CA 1 ATOM 7446 C C . ASP B 1 403 ? 15.508 3.241 8.369 1.00 19.42 ? 403 ASP B C 1 ATOM 7447 O O . ASP B 1 403 ? 16.103 3.245 9.446 1.00 19.40 ? 403 ASP B O 1 ATOM 7448 C CB . ASP B 1 403 ? 17.188 2.097 6.864 1.00 23.08 ? 403 ASP B CB 1 ATOM 7449 C CG . ASP B 1 403 ? 17.704 0.681 6.652 1.00 24.45 ? 403 ASP B CG 1 ATOM 7450 O OD1 . ASP B 1 403 ? 17.926 -0.028 7.657 1.00 24.56 ? 403 ASP B OD1 1 ATOM 7451 O OD2 . ASP B 1 403 ? 17.882 0.268 5.485 1.00 26.94 ? 403 ASP B OD2 1 ATOM 7452 N N . ASN B 1 404 ? 14.611 4.162 8.002 1.00 19.17 ? 404 ASN B N 1 ATOM 7453 C CA . ASN B 1 404 ? 14.193 5.306 8.816 1.00 17.90 ? 404 ASN B CA 1 ATOM 7454 C C . ASN B 1 404 ? 15.320 6.106 9.462 1.00 17.72 ? 404 ASN B C 1 ATOM 7455 O O . ASN B 1 404 ? 15.290 6.421 10.659 1.00 16.81 ? 404 ASN B O 1 ATOM 7456 C CB . ASN B 1 404 ? 13.177 4.848 9.869 1.00 16.32 ? 404 ASN B CB 1 ATOM 7457 C CG . ASN B 1 404 ? 11.856 4.454 9.275 1.00 14.71 ? 404 ASN B CG 1 ATOM 7458 O OD1 . ASN B 1 404 ? 11.706 4.378 8.055 1.00 15.46 ? 404 ASN B OD1 1 ATOM 7459 N ND2 . ASN B 1 404 ? 10.876 4.201 10.139 1.00 11.23 ? 404 ASN B ND2 1 ATOM 7460 N N . ILE B 1 405 ? 16.300 6.440 8.631 1.00 18.50 ? 405 ILE B N 1 ATOM 7461 C CA . ILE B 1 405 ? 17.481 7.191 9.031 1.00 18.75 ? 405 ILE B CA 1 ATOM 7462 C C . ILE B 1 405 ? 17.192 8.676 9.278 1.00 20.00 ? 405 ILE B C 1 ATOM 7463 O O . ILE B 1 405 ? 16.709 9.399 8.396 1.00 20.50 ? 405 ILE B O 1 ATOM 7464 C CB . ILE B 1 405 ? 18.615 7.011 7.976 1.00 18.57 ? 405 ILE B CB 1 ATOM 7465 C CG1 . ILE B 1 405 ? 19.066 5.544 7.939 1.00 17.74 ? 405 ILE B CG1 1 ATOM 7466 C CG2 . ILE B 1 405 ? 19.787 7.993 8.209 1.00 17.18 ? 405 ILE B CG2 1 ATOM 7467 C CD1 . ILE B 1 405 ? 19.983 5.108 9.051 1.00 18.63 ? 405 ILE B CD1 1 ATOM 7468 N N . VAL B 1 406 ? 17.438 9.085 10.519 1.00 20.12 ? 406 VAL B N 1 ATOM 7469 C CA . VAL B 1 406 ? 17.288 10.470 10.941 1.00 20.45 ? 406 VAL B CA 1 ATOM 7470 C C . VAL B 1 406 ? 18.740 10.894 11.229 1.00 20.96 ? 406 VAL B C 1 ATOM 7471 O O . VAL B 1 406 ? 19.302 10.608 12.300 1.00 18.72 ? 406 VAL B O 1 ATOM 7472 C CB . VAL B 1 406 ? 16.375 10.614 12.194 1.00 19.28 ? 406 VAL B CB 1 ATOM 7473 C CG1 . VAL B 1 406 ? 16.179 12.062 12.526 1.00 20.06 ? 406 VAL B CG1 1 ATOM 7474 C CG2 . VAL B 1 406 ? 15.018 9.973 11.958 1.00 18.41 ? 406 VAL B CG2 1 ATOM 7475 N N . GLN B 1 407 ? 19.352 11.502 10.212 1.00 21.58 ? 407 GLN B N 1 ATOM 7476 C CA . GLN B 1 407 ? 20.740 11.956 10.269 1.00 22.67 ? 407 GLN B CA 1 ATOM 7477 C C . GLN B 1 407 ? 20.901 13.230 11.081 1.00 21.80 ? 407 GLN B C 1 ATOM 7478 O O . GLN B 1 407 ? 20.315 14.265 10.767 1.00 23.48 ? 407 GLN B O 1 ATOM 7479 C CB . GLN B 1 407 ? 21.294 12.148 8.858 1.00 21.80 ? 407 GLN B CB 1 ATOM 7480 C CG . GLN B 1 407 ? 22.772 11.853 8.730 1.00 21.00 ? 407 GLN B CG 1 ATOM 7481 C CD . GLN B 1 407 ? 23.283 12.049 7.312 1.00 24.31 ? 407 GLN B CD 1 ATOM 7482 O OE1 . GLN B 1 407 ? 22.856 11.364 6.380 1.00 23.67 ? 407 GLN B OE1 1 ATOM 7483 N NE2 . GLN B 1 407 ? 24.198 12.994 7.142 1.00 25.27 ? 407 GLN B NE2 1 ATOM 7484 N N . VAL B 1 408 ? 21.663 13.104 12.162 1.00 23.13 ? 408 VAL B N 1 ATOM 7485 C CA . VAL B 1 408 ? 21.946 14.198 13.087 1.00 24.05 ? 408 VAL B CA 1 ATOM 7486 C C . VAL B 1 408 ? 23.435 14.529 12.949 1.00 25.41 ? 408 VAL B C 1 ATOM 7487 O O . VAL B 1 408 ? 24.291 13.797 13.458 1.00 26.04 ? 408 VAL B O 1 ATOM 7488 C CB . VAL B 1 408 ? 21.622 13.785 14.553 1.00 21.51 ? 408 VAL B CB 1 ATOM 7489 C CG1 . VAL B 1 408 ? 21.683 14.981 15.462 1.00 22.50 ? 408 VAL B CG1 1 ATOM 7490 C CG2 . VAL B 1 408 ? 20.257 13.144 14.642 1.00 20.89 ? 408 VAL B CG2 1 ATOM 7491 N N . ASP B 1 409 ? 23.728 15.625 12.249 1.00 27.09 ? 409 ASP B N 1 ATOM 7492 C CA . ASP B 1 409 ? 25.104 16.060 12.005 1.00 28.64 ? 409 ASP B CA 1 ATOM 7493 C C . ASP B 1 409 ? 25.724 16.939 13.079 1.00 29.13 ? 409 ASP B C 1 ATOM 7494 O O . ASP B 1 409 ? 26.948 17.125 13.091 1.00 27.84 ? 409 ASP B O 1 ATOM 7495 C CB . ASP B 1 409 ? 25.214 16.740 10.639 1.00 29.86 ? 409 ASP B CB 1 ATOM 7496 C CG . ASP B 1 409 ? 25.062 15.760 9.494 1.00 32.21 ? 409 ASP B CG 1 ATOM 7497 O OD1 . ASP B 1 409 ? 25.843 14.788 9.439 1.00 34.89 ? 409 ASP B OD1 1 ATOM 7498 O OD2 . ASP B 1 409 ? 24.152 15.949 8.660 1.00 32.82 ? 409 ASP B OD2 1 ATOM 7499 N N . ALA B 1 410 ? 24.881 17.445 13.986 1.00 29.90 ? 410 ALA B N 1 ATOM 7500 C CA . ALA B 1 410 ? 25.294 18.314 15.098 1.00 30.69 ? 410 ALA B CA 1 ATOM 7501 C C . ALA B 1 410 ? 26.353 17.644 15.976 1.00 31.15 ? 410 ALA B C 1 ATOM 7502 O O . ALA B 1 410 ? 26.218 16.469 16.331 1.00 30.45 ? 410 ALA B O 1 ATOM 7503 C CB . ALA B 1 410 ? 24.082 18.706 15.939 1.00 31.37 ? 410 ALA B CB 1 ATOM 7504 N N . VAL B 1 411 ? 27.434 18.378 16.244 1.00 30.76 ? 411 VAL B N 1 ATOM 7505 C CA . VAL B 1 411 ? 28.554 17.881 17.047 1.00 30.25 ? 411 VAL B CA 1 ATOM 7506 C C . VAL B 1 411 ? 28.503 18.335 18.508 1.00 30.12 ? 411 VAL B C 1 ATOM 7507 O O . VAL B 1 411 ? 28.624 19.528 18.792 1.00 30.49 ? 411 VAL B O 1 ATOM 7508 C CB . VAL B 1 411 ? 29.923 18.293 16.415 1.00 29.16 ? 411 VAL B CB 1 ATOM 7509 C CG1 . VAL B 1 411 ? 31.083 17.738 17.220 1.00 28.17 ? 411 VAL B CG1 1 ATOM 7510 C CG2 . VAL B 1 411 ? 30.019 17.804 14.972 1.00 29.00 ? 411 VAL B CG2 1 ATOM 7511 N N . ASP B 1 412 ? 28.353 17.363 19.415 1.00 30.88 ? 412 ASP B N 1 ATOM 7512 C CA . ASP B 1 412 ? 28.306 17.560 20.882 1.00 32.37 ? 412 ASP B CA 1 ATOM 7513 C C . ASP B 1 412 ? 27.276 18.606 21.366 1.00 32.72 ? 412 ASP B C 1 ATOM 7514 O O . ASP B 1 412 ? 27.455 19.257 22.404 1.00 32.48 ? 412 ASP B O 1 ATOM 7515 C CB . ASP B 1 412 ? 29.733 17.846 21.418 1.00 32.88 ? 412 ASP B CB 1 ATOM 7516 C CG . ASP B 1 412 ? 29.910 17.484 22.892 1.00 33.13 ? 412 ASP B CG 1 ATOM 7517 O OD1 . ASP B 1 412 ? 29.258 16.536 23.375 1.00 33.72 ? 412 ASP B OD1 1 ATOM 7518 O OD2 . ASP B 1 412 ? 30.717 18.157 23.569 1.00 33.72 ? 412 ASP B OD2 1 ATOM 7519 N N . GLN B 1 413 ? 26.203 18.759 20.587 1.00 32.32 ? 413 GLN B N 1 ATOM 7520 C CA . GLN B 1 413 ? 25.128 19.699 20.894 1.00 32.16 ? 413 GLN B CA 1 ATOM 7521 C C . GLN B 1 413 ? 23.843 18.949 21.234 1.00 30.84 ? 413 GLN B C 1 ATOM 7522 O O . GLN B 1 413 ? 23.660 17.792 20.834 1.00 29.56 ? 413 GLN B O 1 ATOM 7523 C CB . GLN B 1 413 ? 24.863 20.644 19.706 1.00 35.16 ? 413 GLN B CB 1 ATOM 7524 C CG . GLN B 1 413 ? 26.060 21.475 19.196 1.00 38.68 ? 413 GLN B CG 1 ATOM 7525 C CD . GLN B 1 413 ? 26.656 22.405 20.248 1.00 40.72 ? 413 GLN B CD 1 ATOM 7526 O OE1 . GLN B 1 413 ? 26.114 23.477 20.528 1.00 42.83 ? 413 GLN B OE1 1 ATOM 7527 N NE2 . GLN B 1 413 ? 27.784 21.999 20.824 1.00 40.55 ? 413 GLN B NE2 1 ATOM 7528 N N . TRP B 1 414 ? 22.963 19.619 21.977 1.00 28.90 ? 414 TRP B N 1 ATOM 7529 C CA . TRP B 1 414 ? 21.674 19.059 22.374 1.00 27.87 ? 414 TRP B CA 1 ATOM 7530 C C . TRP B 1 414 ? 20.695 19.126 21.207 1.00 27.01 ? 414 TRP B C 1 ATOM 7531 O O . TRP B 1 414 ? 20.656 20.122 20.471 1.00 25.71 ? 414 TRP B O 1 ATOM 7532 C CB . TRP B 1 414 ? 21.095 19.809 23.583 1.00 28.85 ? 414 TRP B CB 1 ATOM 7533 C CG . TRP B 1 414 ? 21.913 19.698 24.844 1.00 28.66 ? 414 TRP B CG 1 ATOM 7534 C CD1 . TRP B 1 414 ? 22.848 20.587 25.293 1.00 29.44 ? 414 TRP B CD1 1 ATOM 7535 C CD2 . TRP B 1 414 ? 21.869 18.642 25.810 1.00 29.42 ? 414 TRP B CD2 1 ATOM 7536 N NE1 . TRP B 1 414 ? 23.397 20.153 26.476 1.00 31.24 ? 414 TRP B NE1 1 ATOM 7537 C CE2 . TRP B 1 414 ? 22.818 18.962 26.822 1.00 29.81 ? 414 TRP B CE2 1 ATOM 7538 C CE3 . TRP B 1 414 ? 21.119 17.452 25.927 1.00 28.73 ? 414 TRP B CE3 1 ATOM 7539 C CZ2 . TRP B 1 414 ? 23.043 18.133 27.942 1.00 29.19 ? 414 TRP B CZ2 1 ATOM 7540 C CZ3 . TRP B 1 414 ? 21.340 16.617 27.047 1.00 29.03 ? 414 TRP B CZ3 1 ATOM 7541 C CH2 . TRP B 1 414 ? 22.299 16.970 28.039 1.00 30.37 ? 414 TRP B CH2 1 ATOM 7542 N N . THR B 1 415 ? 19.964 18.030 21.007 1.00 25.11 ? 415 THR B N 1 ATOM 7543 C CA . THR B 1 415 ? 18.979 17.922 19.934 1.00 23.78 ? 415 THR B CA 1 ATOM 7544 C C . THR B 1 415 ? 17.614 17.588 20.516 1.00 22.55 ? 415 THR B C 1 ATOM 7545 O O . THR B 1 415 ? 17.460 16.610 21.244 1.00 24.18 ? 415 THR B O 1 ATOM 7546 C CB . THR B 1 415 ? 19.392 16.873 18.908 1.00 23.64 ? 415 THR B CB 1 ATOM 7547 O OG1 . THR B 1 415 ? 19.741 15.656 19.580 1.00 25.35 ? 415 THR B OG1 1 ATOM 7548 C CG2 . THR B 1 415 ? 20.568 17.371 18.094 1.00 24.69 ? 415 THR B CG2 1 ATOM 7549 N N . TYR B 1 416 ? 16.627 18.403 20.162 1.00 21.09 ? 416 TYR B N 1 ATOM 7550 C CA . TYR B 1 416 ? 15.261 18.285 20.674 1.00 20.63 ? 416 TYR B CA 1 ATOM 7551 C C . TYR B 1 416 ? 14.330 17.485 19.777 1.00 18.89 ? 416 TYR B C 1 ATOM 7552 O O . TYR B 1 416 ? 14.276 17.721 18.570 1.00 20.34 ? 416 TYR B O 1 ATOM 7553 C CB . TYR B 1 416 ? 14.696 19.686 20.922 1.00 23.15 ? 416 TYR B CB 1 ATOM 7554 C CG . TYR B 1 416 ? 15.555 20.547 21.827 1.00 23.97 ? 416 TYR B CG 1 ATOM 7555 C CD1 . TYR B 1 416 ? 16.691 21.227 21.325 1.00 26.25 ? 416 TYR B CD1 1 ATOM 7556 C CD2 . TYR B 1 416 ? 15.264 20.659 23.199 1.00 24.95 ? 416 TYR B CD2 1 ATOM 7557 C CE1 . TYR B 1 416 ? 17.528 21.999 22.185 1.00 28.15 ? 416 TYR B CE1 1 ATOM 7558 C CE2 . TYR B 1 416 ? 16.088 21.427 24.067 1.00 27.71 ? 416 TYR B CE2 1 ATOM 7559 C CZ . TYR B 1 416 ? 17.214 22.088 23.552 1.00 27.17 ? 416 TYR B CZ 1 ATOM 7560 O OH . TYR B 1 416 ? 18.018 22.815 24.395 1.00 29.89 ? 416 TYR B OH 1 ATOM 7561 N N . TRP B 1 417 ? 13.638 16.505 20.364 1.00 16.17 ? 417 TRP B N 1 ATOM 7562 C CA . TRP B 1 417 ? 12.725 15.627 19.615 1.00 14.65 ? 417 TRP B CA 1 ATOM 7563 C C . TRP B 1 417 ? 11.295 15.551 20.131 1.00 11.74 ? 417 TRP B C 1 ATOM 7564 O O . TRP B 1 417 ? 11.054 15.231 21.296 1.00 11.17 ? 417 TRP B O 1 ATOM 7565 C CB . TRP B 1 417 ? 13.318 14.205 19.488 1.00 15.18 ? 417 TRP B CB 1 ATOM 7566 C CG . TRP B 1 417 ? 14.688 14.229 18.895 1.00 15.49 ? 417 TRP B CG 1 ATOM 7567 C CD1 . TRP B 1 417 ? 15.864 14.352 19.582 1.00 16.00 ? 417 TRP B CD1 1 ATOM 7568 C CD2 . TRP B 1 417 ? 15.021 14.367 17.506 1.00 15.56 ? 417 TRP B CD2 1 ATOM 7569 N NE1 . TRP B 1 417 ? 16.901 14.598 18.719 1.00 15.24 ? 417 TRP B NE1 1 ATOM 7570 C CE2 . TRP B 1 417 ? 16.421 14.612 17.437 1.00 14.79 ? 417 TRP B CE2 1 ATOM 7571 C CE3 . TRP B 1 417 ? 14.274 14.318 16.307 1.00 14.22 ? 417 TRP B CE3 1 ATOM 7572 C CZ2 . TRP B 1 417 ? 17.101 14.816 16.207 1.00 15.31 ? 417 TRP B CZ2 1 ATOM 7573 C CZ3 . TRP B 1 417 ? 14.947 14.520 15.078 1.00 15.94 ? 417 TRP B CZ3 1 ATOM 7574 C CH2 . TRP B 1 417 ? 16.354 14.769 15.045 1.00 14.49 ? 417 TRP B CH2 1 ATOM 7575 N N . LEU B 1 418 ? 10.350 15.880 19.255 1.00 11.45 ? 418 LEU B N 1 ATOM 7576 C CA . LEU B 1 418 ? 8.930 15.833 19.590 1.00 11.41 ? 418 LEU B CA 1 ATOM 7577 C C . LEU B 1 418 ? 8.303 14.587 18.981 1.00 11.39 ? 418 LEU B C 1 ATOM 7578 O O . LEU B 1 418 ? 8.208 14.462 17.758 1.00 12.52 ? 418 LEU B O 1 ATOM 7579 C CB . LEU B 1 418 ? 8.195 17.092 19.107 1.00 9.89 ? 418 LEU B CB 1 ATOM 7580 C CG . LEU B 1 418 ? 6.706 17.182 19.477 1.00 9.41 ? 418 LEU B CG 1 ATOM 7581 C CD1 . LEU B 1 418 ? 6.525 17.610 20.931 1.00 8.06 ? 418 LEU B CD1 1 ATOM 7582 C CD2 . LEU B 1 418 ? 6.024 18.154 18.557 1.00 9.20 ? 418 LEU B CD2 1 ATOM 7583 N N . ILE B 1 419 ? 7.912 13.654 19.847 1.00 10.75 ? 419 ILE B N 1 ATOM 7584 C CA . ILE B 1 419 ? 7.292 12.407 19.413 1.00 10.31 ? 419 ILE B CA 1 ATOM 7585 C C . ILE B 1 419 ? 5.791 12.517 19.676 1.00 11.49 ? 419 ILE B C 1 ATOM 7586 O O . ILE B 1 419 ? 5.373 12.673 20.821 1.00 11.41 ? 419 ILE B O 1 ATOM 7587 C CB . ILE B 1 419 ? 7.879 11.159 20.149 1.00 10.56 ? 419 ILE B CB 1 ATOM 7588 C CG1 . ILE B 1 419 ? 9.413 11.170 20.144 1.00 6.63 ? 419 ILE B CG1 1 ATOM 7589 C CG2 . ILE B 1 419 ? 7.436 9.878 19.451 1.00 9.46 ? 419 ILE B CG2 1 ATOM 7590 C CD1 . ILE B 1 419 ? 10.034 11.951 21.248 1.00 4.84 ? 419 ILE B CD1 1 ATOM 7591 N N . GLU B 1 420 ? 5.000 12.471 18.601 1.00 12.18 ? 420 GLU B N 1 ATOM 7592 C CA . GLU B 1 420 ? 3.536 12.578 18.670 1.00 12.56 ? 420 GLU B CA 1 ATOM 7593 C C . GLU B 1 420 ? 2.872 11.199 18.610 1.00 12.93 ? 420 GLU B C 1 ATOM 7594 O O . GLU B 1 420 ? 3.127 10.425 17.686 1.00 13.56 ? 420 GLU B O 1 ATOM 7595 C CB . GLU B 1 420 ? 3.016 13.448 17.512 1.00 12.37 ? 420 GLU B CB 1 ATOM 7596 C CG . GLU B 1 420 ? 3.686 14.814 17.373 1.00 12.36 ? 420 GLU B CG 1 ATOM 7597 C CD . GLU B 1 420 ? 3.122 15.642 16.229 1.00 14.27 ? 420 GLU B CD 1 ATOM 7598 O OE1 . GLU B 1 420 ? 3.060 15.133 15.086 1.00 18.30 ? 420 GLU B OE1 1 ATOM 7599 O OE2 . GLU B 1 420 ? 2.741 16.807 16.468 1.00 13.94 ? 420 GLU B OE2 1 ATOM 7600 N N . ASN B 1 421 ? 1.965 10.928 19.547 1.00 14.20 ? 421 ASN B N 1 ATOM 7601 C CA . ASN B 1 421 ? 1.279 9.635 19.611 1.00 15.30 ? 421 ASN B CA 1 ATOM 7602 C C . ASN B 1 421 ? -0.079 9.540 18.901 1.00 15.77 ? 421 ASN B C 1 ATOM 7603 O O . ASN B 1 421 ? -1.115 9.427 19.565 1.00 14.50 ? 421 ASN B O 1 ATOM 7604 C CB . ASN B 1 421 ? 1.129 9.192 21.074 1.00 14.73 ? 421 ASN B CB 1 ATOM 7605 C CG . ASN B 1 421 ? 1.034 7.669 21.237 1.00 16.00 ? 421 ASN B CG 1 ATOM 7606 O OD1 . ASN B 1 421 ? 0.873 6.929 20.267 1.00 17.55 ? 421 ASN B OD1 1 ATOM 7607 N ND2 . ASN B 1 421 ? 1.154 7.202 22.474 1.00 13.68 ? 421 ASN B ND2 1 ATOM 7608 N N . ASP B 1 422 ? -0.059 9.558 17.560 1.00 17.81 ? 422 ASP B N 1 ATOM 7609 C CA . ASP B 1 422 ? -1.258 9.424 16.700 1.00 18.67 ? 422 ASP B CA 1 ATOM 7610 C C . ASP B 1 422 ? -2.468 10.268 17.190 1.00 20.76 ? 422 ASP B C 1 ATOM 7611 O O . ASP B 1 422 ? -3.495 9.704 17.583 1.00 22.08 ? 422 ASP B O 1 ATOM 7612 C CB . ASP B 1 422 ? -1.632 7.919 16.630 1.00 18.36 ? 422 ASP B CB 1 ATOM 7613 C CG . ASP B 1 422 ? -2.223 7.491 15.283 1.00 18.80 ? 422 ASP B CG 1 ATOM 7614 O OD1 . ASP B 1 422 ? -2.525 8.351 14.420 1.00 18.32 ? 422 ASP B OD1 1 ATOM 7615 O OD2 . ASP B 1 422 ? -2.386 6.264 15.096 1.00 16.70 ? 422 ASP B OD2 1 ATOM 7616 N N . PRO B 1 423 ? -2.364 11.620 17.165 1.00 21.27 ? 423 PRO B N 1 ATOM 7617 C CA . PRO B 1 423 ? -3.467 12.477 17.629 1.00 22.60 ? 423 PRO B CA 1 ATOM 7618 C C . PRO B 1 423 ? -4.747 12.405 16.802 1.00 23.90 ? 423 PRO B C 1 ATOM 7619 O O . PRO B 1 423 ? -5.843 12.481 17.355 1.00 24.75 ? 423 PRO B O 1 ATOM 7620 C CB . PRO B 1 423 ? -2.871 13.884 17.548 1.00 22.88 ? 423 PRO B CB 1 ATOM 7621 C CG . PRO B 1 423 ? -1.396 13.669 17.462 1.00 23.23 ? 423 PRO B CG 1 ATOM 7622 C CD . PRO B 1 423 ? -1.284 12.457 16.618 1.00 21.91 ? 423 PRO B CD 1 ATOM 7623 N N . GLU B 1 424 ? -4.585 12.247 15.486 1.00 25.29 ? 424 GLU B N 1 ATOM 7624 C CA . GLU B 1 424 ? -5.697 12.183 14.535 1.00 26.27 ? 424 GLU B CA 1 ATOM 7625 C C . GLU B 1 424 ? -6.152 10.754 14.200 1.00 25.18 ? 424 GLU B C 1 ATOM 7626 O O . GLU B 1 424 ? -7.123 10.563 13.454 1.00 24.18 ? 424 GLU B O 1 ATOM 7627 C CB . GLU B 1 424 ? -5.319 12.921 13.239 1.00 29.38 ? 424 GLU B CB 1 ATOM 7628 C CG . GLU B 1 424 ? -4.764 14.351 13.408 1.00 36.31 ? 424 GLU B CG 1 ATOM 7629 C CD . GLU B 1 424 ? -5.751 15.329 14.043 1.00 39.32 ? 424 GLU B CD 1 ATOM 7630 O OE1 . GLU B 1 424 ? -6.859 15.523 13.488 1.00 42.92 ? 424 GLU B OE1 1 ATOM 7631 O OE2 . GLU B 1 424 ? -5.409 15.910 15.097 1.00 40.16 ? 424 GLU B OE2 1 ATOM 7632 N N . GLY B 1 425 ? -5.468 9.764 14.779 1.00 24.75 ? 425 GLY B N 1 ATOM 7633 C CA . GLY B 1 425 ? -5.792 8.360 14.548 1.00 23.85 ? 425 GLY B CA 1 ATOM 7634 C C . GLY B 1 425 ? -7.058 7.818 15.204 1.00 23.82 ? 425 GLY B C 1 ATOM 7635 O O . GLY B 1 425 ? -7.631 8.497 16.060 1.00 22.76 ? 425 GLY B O 1 ATOM 7636 N N . PRO B 1 426 ? -7.503 6.586 14.848 1.00 24.44 ? 426 PRO B N 1 ATOM 7637 C CA . PRO B 1 426 ? -8.703 5.910 15.369 1.00 24.54 ? 426 PRO B CA 1 ATOM 7638 C C . PRO B 1 426 ? -8.663 5.772 16.890 1.00 24.51 ? 426 PRO B C 1 ATOM 7639 O O . PRO B 1 426 ? -9.607 6.137 17.593 1.00 24.35 ? 426 PRO B O 1 ATOM 7640 C CB . PRO B 1 426 ? -8.637 4.536 14.696 1.00 24.34 ? 426 PRO B CB 1 ATOM 7641 C CG . PRO B 1 426 ? -7.862 4.797 13.454 1.00 24.07 ? 426 PRO B CG 1 ATOM 7642 C CD . PRO B 1 426 ? -6.773 5.669 13.954 1.00 25.81 ? 426 PRO B CD 1 ATOM 7643 N N . PHE B 1 427 ? -7.545 5.250 17.374 1.00 23.81 ? 427 PHE B N 1 ATOM 7644 C CA . PHE B 1 427 ? -7.313 5.085 18.794 1.00 24.46 ? 427 PHE B CA 1 ATOM 7645 C C . PHE B 1 427 ? -5.807 5.167 19.004 1.00 22.70 ? 427 PHE B C 1 ATOM 7646 O O . PHE B 1 427 ? -5.028 5.050 18.044 1.00 21.08 ? 427 PHE B O 1 ATOM 7647 C CB . PHE B 1 427 ? -7.937 3.767 19.329 1.00 28.40 ? 427 PHE B CB 1 ATOM 7648 C CG . PHE B 1 427 ? -7.098 2.539 19.107 1.00 32.15 ? 427 PHE B CG 1 ATOM 7649 C CD1 . PHE B 1 427 ? -6.855 2.053 17.799 1.00 34.01 ? 427 PHE B CD1 1 ATOM 7650 C CD2 . PHE B 1 427 ? -6.506 1.887 20.206 1.00 32.87 ? 427 PHE B CD2 1 ATOM 7651 C CE1 . PHE B 1 427 ? -6.021 0.932 17.582 1.00 34.22 ? 427 PHE B CE1 1 ATOM 7652 C CE2 . PHE B 1 427 ? -5.670 0.767 20.011 1.00 35.12 ? 427 PHE B CE2 1 ATOM 7653 C CZ . PHE B 1 427 ? -5.420 0.283 18.695 1.00 35.28 ? 427 PHE B CZ 1 ATOM 7654 N N . SER B 1 428 ? -5.412 5.345 20.258 1.00 19.72 ? 428 SER B N 1 ATOM 7655 C CA . SER B 1 428 ? -4.009 5.444 20.585 1.00 18.09 ? 428 SER B CA 1 ATOM 7656 C C . SER B 1 428 ? -3.626 4.603 21.796 1.00 16.94 ? 428 SER B C 1 ATOM 7657 O O . SER B 1 428 ? -4.417 4.425 22.731 1.00 13.88 ? 428 SER B O 1 ATOM 7658 C CB . SER B 1 428 ? -3.625 6.907 20.789 1.00 17.25 ? 428 SER B CB 1 ATOM 7659 O OG . SER B 1 428 ? -2.214 7.090 20.745 1.00 16.20 ? 428 SER B OG 1 ATOM 7660 N N . LEU B 1 429 ? -2.406 4.067 21.726 1.00 15.34 ? 429 LEU B N 1 ATOM 7661 C CA . LEU B 1 429 ? -1.823 3.223 22.761 1.00 12.25 ? 429 LEU B CA 1 ATOM 7662 C C . LEU B 1 429 ? -0.547 3.857 23.320 1.00 10.35 ? 429 LEU B C 1 ATOM 7663 O O . LEU B 1 429 ? 0.172 4.540 22.585 1.00 11.35 ? 429 LEU B O 1 ATOM 7664 C CB . LEU B 1 429 ? -1.457 1.851 22.173 1.00 13.98 ? 429 LEU B CB 1 ATOM 7665 C CG . LEU B 1 429 ? -2.542 0.838 21.835 1.00 12.46 ? 429 LEU B CG 1 ATOM 7666 C CD1 . LEU B 1 429 ? -1.891 -0.399 21.262 1.00 14.20 ? 429 LEU B CD1 1 ATOM 7667 C CD2 . LEU B 1 429 ? -3.373 0.494 23.064 1.00 14.03 ? 429 LEU B CD2 1 ATOM 7668 N N . PRO B 1 430 ? -0.262 3.662 24.632 1.00 6.35 ? 430 PRO B N 1 ATOM 7669 C CA . PRO B 1 430 ? 0.938 4.209 25.262 1.00 5.92 ? 430 PRO B CA 1 ATOM 7670 C C . PRO B 1 430 ? 2.164 3.432 24.768 1.00 7.73 ? 430 PRO B C 1 ATOM 7671 O O . PRO B 1 430 ? 2.080 2.224 24.527 1.00 10.62 ? 430 PRO B O 1 ATOM 7672 C CB . PRO B 1 430 ? 0.694 3.930 26.741 1.00 7.50 ? 430 PRO B CB 1 ATOM 7673 C CG . PRO B 1 430 ? -0.742 3.821 26.866 1.00 5.89 ? 430 PRO B CG 1 ATOM 7674 C CD . PRO B 1 430 ? -1.121 3.052 25.658 1.00 6.06 ? 430 PRO B CD 1 ATOM 7675 N N . HIS B 1 431 ? 3.283 4.117 24.575 1.00 6.34 ? 431 HIS B N 1 ATOM 7676 C CA . HIS B 1 431 ? 4.487 3.448 24.090 1.00 7.35 ? 431 HIS B CA 1 ATOM 7677 C C . HIS B 1 431 ? 5.739 3.664 24.929 1.00 6.12 ? 431 HIS B C 1 ATOM 7678 O O . HIS B 1 431 ? 6.035 4.787 25.309 1.00 7.64 ? 431 HIS B O 1 ATOM 7679 C CB . HIS B 1 431 ? 4.815 3.871 22.649 1.00 7.34 ? 431 HIS B CB 1 ATOM 7680 C CG . HIS B 1 431 ? 3.720 3.599 21.669 1.00 8.60 ? 431 HIS B CG 1 ATOM 7681 N ND1 . HIS B 1 431 ? 3.235 2.332 21.427 1.00 7.43 ? 431 HIS B ND1 1 ATOM 7682 C CD2 . HIS B 1 431 ? 3.006 4.434 20.881 1.00 8.74 ? 431 HIS B CD2 1 ATOM 7683 C CE1 . HIS B 1 431 ? 2.268 2.399 20.532 1.00 8.79 ? 431 HIS B CE1 1 ATOM 7684 N NE2 . HIS B 1 431 ? 2.110 3.663 20.183 1.00 10.99 ? 431 HIS B NE2 1 ATOM 7685 N N . PRO B 1 432 ? 6.448 2.574 25.290 1.00 6.66 ? 432 PRO B N 1 ATOM 7686 C CA . PRO B 1 432 ? 7.683 2.682 26.074 1.00 8.97 ? 432 PRO B CA 1 ATOM 7687 C C . PRO B 1 432 ? 8.854 3.041 25.134 1.00 11.43 ? 432 PRO B C 1 ATOM 7688 O O . PRO B 1 432 ? 9.512 2.157 24.579 1.00 15.27 ? 432 PRO B O 1 ATOM 7689 C CB . PRO B 1 432 ? 7.817 1.283 26.685 1.00 8.86 ? 432 PRO B CB 1 ATOM 7690 C CG . PRO B 1 432 ? 7.172 0.409 25.682 1.00 6.50 ? 432 PRO B CG 1 ATOM 7691 C CD . PRO B 1 432 ? 5.955 1.183 25.303 1.00 5.58 ? 432 PRO B CD 1 ATOM 7692 N N . MET B 1 433 ? 9.049 4.340 24.903 1.00 11.65 ? 433 MET B N 1 ATOM 7693 C CA . MET B 1 433 ? 10.111 4.830 24.024 1.00 12.72 ? 433 MET B CA 1 ATOM 7694 C C . MET B 1 433 ? 11.507 4.665 24.592 1.00 12.55 ? 433 MET B C 1 ATOM 7695 O O . MET B 1 433 ? 11.812 5.157 25.673 1.00 12.05 ? 433 MET B O 1 ATOM 7696 C CB . MET B 1 433 ? 9.869 6.283 23.618 1.00 12.89 ? 433 MET B CB 1 ATOM 7697 C CG . MET B 1 433 ? 8.685 6.476 22.716 1.00 12.07 ? 433 MET B CG 1 ATOM 7698 S SD . MET B 1 433 ? 8.485 5.206 21.448 1.00 17.85 ? 433 MET B SD 1 ATOM 7699 C CE . MET B 1 433 ? 9.571 5.767 20.175 1.00 11.01 ? 433 MET B CE 1 ATOM 7700 N N . HIS B 1 434 ? 12.355 4.008 23.806 1.00 13.82 ? 434 HIS B N 1 ATOM 7701 C CA . HIS B 1 434 ? 13.721 3.703 24.197 1.00 13.71 ? 434 HIS B CA 1 ATOM 7702 C C . HIS B 1 434 ? 14.757 4.140 23.164 1.00 13.82 ? 434 HIS B C 1 ATOM 7703 O O . HIS B 1 434 ? 14.558 3.960 21.964 1.00 13.05 ? 434 HIS B O 1 ATOM 7704 C CB . HIS B 1 434 ? 13.830 2.190 24.459 1.00 14.83 ? 434 HIS B CB 1 ATOM 7705 C CG . HIS B 1 434 ? 15.211 1.732 24.796 1.00 16.50 ? 434 HIS B CG 1 ATOM 7706 N ND1 . HIS B 1 434 ? 15.954 2.297 25.809 1.00 18.37 ? 434 HIS B ND1 1 ATOM 7707 C CD2 . HIS B 1 434 ? 16.015 0.822 24.201 1.00 16.63 ? 434 HIS B CD2 1 ATOM 7708 C CE1 . HIS B 1 434 ? 17.158 1.757 25.820 1.00 16.39 ? 434 HIS B CE1 1 ATOM 7709 N NE2 . HIS B 1 434 ? 17.219 0.859 24.857 1.00 16.28 ? 434 HIS B NE2 1 ATOM 7710 N N . LEU B 1 435 ? 15.881 4.656 23.665 1.00 12.03 ? 435 LEU B N 1 ATOM 7711 C CA . LEU B 1 435 ? 16.996 5.101 22.836 1.00 12.22 ? 435 LEU B CA 1 ATOM 7712 C C . LEU B 1 435 ? 18.259 4.299 23.126 1.00 11.52 ? 435 LEU B C 1 ATOM 7713 O O . LEU B 1 435 ? 18.609 4.046 24.288 1.00 10.76 ? 435 LEU B O 1 ATOM 7714 C CB . LEU B 1 435 ? 17.285 6.594 23.063 1.00 12.74 ? 435 LEU B CB 1 ATOM 7715 C CG . LEU B 1 435 ? 18.398 7.367 22.339 1.00 11.56 ? 435 LEU B CG 1 ATOM 7716 C CD1 . LEU B 1 435 ? 18.242 7.299 20.832 1.00 12.53 ? 435 LEU B CD1 1 ATOM 7717 C CD2 . LEU B 1 435 ? 18.362 8.804 22.785 1.00 13.01 ? 435 LEU B CD2 1 ATOM 7718 N N . HIS B 1 436 ? 18.937 3.920 22.049 1.00 10.78 ? 436 HIS B N 1 ATOM 7719 C CA . HIS B 1 436 ? 20.194 3.185 22.122 1.00 11.24 ? 436 HIS B CA 1 ATOM 7720 C C . HIS B 1 436 ? 21.304 4.223 22.210 1.00 11.03 ? 436 HIS B C 1 ATOM 7721 O O . HIS B 1 436 ? 21.174 5.327 21.665 1.00 11.39 ? 436 HIS B O 1 ATOM 7722 C CB . HIS B 1 436 ? 20.419 2.362 20.841 1.00 11.25 ? 436 HIS B CB 1 ATOM 7723 C CG . HIS B 1 436 ? 19.586 1.119 20.735 1.00 12.81 ? 436 HIS B CG 1 ATOM 7724 N ND1 . HIS B 1 436 ? 20.084 -0.059 20.220 1.00 11.91 ? 436 HIS B ND1 1 ATOM 7725 C CD2 . HIS B 1 436 ? 18.290 0.872 21.043 1.00 12.77 ? 436 HIS B CD2 1 ATOM 7726 C CE1 . HIS B 1 436 ? 19.135 -0.975 20.215 1.00 8.52 ? 436 HIS B CE1 1 ATOM 7727 N NE2 . HIS B 1 436 ? 18.037 -0.436 20.709 1.00 10.07 ? 436 HIS B NE2 1 ATOM 7728 N N . GLY B 1 437 ? 22.372 3.865 22.919 1.00 12.22 ? 437 GLY B N 1 ATOM 7729 C CA . GLY B 1 437 ? 23.545 4.711 23.049 1.00 10.50 ? 437 GLY B CA 1 ATOM 7730 C C . GLY B 1 437 ? 23.539 5.996 23.838 1.00 13.44 ? 437 GLY B C 1 ATOM 7731 O O . GLY B 1 437 ? 24.577 6.669 23.907 1.00 12.61 ? 437 GLY B O 1 ATOM 7732 N N . HIS B 1 438 ? 22.377 6.379 24.372 1.00 14.07 ? 438 HIS B N 1 ATOM 7733 C CA . HIS B 1 438 ? 22.243 7.611 25.149 1.00 13.79 ? 438 HIS B CA 1 ATOM 7734 C C . HIS B 1 438 ? 21.184 7.508 26.232 1.00 14.42 ? 438 HIS B C 1 ATOM 7735 O O . HIS B 1 438 ? 20.320 6.620 26.210 1.00 13.65 ? 438 HIS B O 1 ATOM 7736 C CB . HIS B 1 438 ? 21.793 8.789 24.258 1.00 14.91 ? 438 HIS B CB 1 ATOM 7737 C CG . HIS B 1 438 ? 22.790 9.226 23.230 1.00 17.44 ? 438 HIS B CG 1 ATOM 7738 N ND1 . HIS B 1 438 ? 23.780 10.148 23.496 1.00 18.62 ? 438 HIS B ND1 1 ATOM 7739 C CD2 . HIS B 1 438 ? 22.925 8.894 21.923 1.00 17.59 ? 438 HIS B CD2 1 ATOM 7740 C CE1 . HIS B 1 438 ? 24.481 10.366 22.396 1.00 17.28 ? 438 HIS B CE1 1 ATOM 7741 N NE2 . HIS B 1 438 ? 23.983 9.618 21.429 1.00 16.87 ? 438 HIS B NE2 1 ATOM 7742 N N . ASP B 1 439 ? 21.289 8.432 27.185 1.00 12.31 ? 439 ASP B N 1 ATOM 7743 C CA . ASP B 1 439 ? 20.302 8.621 28.240 1.00 12.32 ? 439 ASP B CA 1 ATOM 7744 C C . ASP B 1 439 ? 19.726 9.982 27.816 1.00 13.31 ? 439 ASP B C 1 ATOM 7745 O O . ASP B 1 439 ? 20.480 10.949 27.601 1.00 14.53 ? 439 ASP B O 1 ATOM 7746 C CB . ASP B 1 439 ? 20.937 8.748 29.624 1.00 10.80 ? 439 ASP B CB 1 ATOM 7747 C CG . ASP B 1 439 ? 21.097 7.423 30.325 1.00 11.81 ? 439 ASP B CG 1 ATOM 7748 O OD1 . ASP B 1 439 ? 20.146 6.614 30.365 1.00 12.35 ? 439 ASP B OD1 1 ATOM 7749 O OD2 . ASP B 1 439 ? 22.181 7.203 30.887 1.00 12.45 ? 439 ASP B OD2 1 ATOM 7750 N N . PHE B 1 440 ? 18.419 10.035 27.587 1.00 12.90 ? 440 PHE B N 1 ATOM 7751 C CA . PHE B 1 440 ? 17.800 11.285 27.172 1.00 13.76 ? 440 PHE B CA 1 ATOM 7752 C C . PHE B 1 440 ? 17.195 12.073 28.323 1.00 14.29 ? 440 PHE B C 1 ATOM 7753 O O . PHE B 1 440 ? 17.019 11.549 29.425 1.00 14.69 ? 440 PHE B O 1 ATOM 7754 C CB . PHE B 1 440 ? 16.769 11.074 26.037 1.00 12.04 ? 440 PHE B CB 1 ATOM 7755 C CG . PHE B 1 440 ? 15.771 9.960 26.283 1.00 13.30 ? 440 PHE B CG 1 ATOM 7756 C CD1 . PHE B 1 440 ? 14.822 10.033 27.320 1.00 13.11 ? 440 PHE B CD1 1 ATOM 7757 C CD2 . PHE B 1 440 ? 15.755 8.838 25.445 1.00 14.35 ? 440 PHE B CD2 1 ATOM 7758 C CE1 . PHE B 1 440 ? 13.878 9.009 27.516 1.00 11.81 ? 440 PHE B CE1 1 ATOM 7759 C CE2 . PHE B 1 440 ? 14.805 7.797 25.626 1.00 13.43 ? 440 PHE B CE2 1 ATOM 7760 C CZ . PHE B 1 440 ? 13.865 7.890 26.668 1.00 12.74 ? 440 PHE B CZ 1 ATOM 7761 N N . LEU B 1 441 ? 16.880 13.331 28.047 1.00 13.53 ? 441 LEU B N 1 ATOM 7762 C CA . LEU B 1 441 ? 16.252 14.199 29.018 1.00 13.01 ? 441 LEU B CA 1 ATOM 7763 C C . LEU B 1 441 ? 14.774 14.289 28.662 1.00 12.50 ? 441 LEU B C 1 ATOM 7764 O O . LEU B 1 441 ? 14.420 14.650 27.532 1.00 10.34 ? 441 LEU B O 1 ATOM 7765 C CB . LEU B 1 441 ? 16.891 15.587 29.000 1.00 13.99 ? 441 LEU B CB 1 ATOM 7766 C CG . LEU B 1 441 ? 18.313 15.793 29.507 1.00 12.40 ? 441 LEU B CG 1 ATOM 7767 C CD1 . LEU B 1 441 ? 18.594 17.280 29.526 1.00 12.43 ? 441 LEU B CD1 1 ATOM 7768 C CD2 . LEU B 1 441 ? 18.454 15.248 30.905 1.00 15.32 ? 441 LEU B CD2 1 ATOM 7769 N N . VAL B 1 442 ? 13.924 13.887 29.609 1.00 12.51 ? 442 VAL B N 1 ATOM 7770 C CA . VAL B 1 442 ? 12.476 13.921 29.425 1.00 14.43 ? 442 VAL B CA 1 ATOM 7771 C C . VAL B 1 442 ? 12.037 15.336 29.820 1.00 16.14 ? 442 VAL B C 1 ATOM 7772 O O . VAL B 1 442 ? 11.790 15.629 30.997 1.00 17.24 ? 442 VAL B O 1 ATOM 7773 C CB . VAL B 1 442 ? 11.751 12.857 30.296 1.00 15.16 ? 442 VAL B CB 1 ATOM 7774 C CG1 . VAL B 1 442 ? 10.341 12.628 29.773 1.00 13.68 ? 442 VAL B CG1 1 ATOM 7775 C CG2 . VAL B 1 442 ? 12.530 11.547 30.324 1.00 15.68 ? 442 VAL B CG2 1 ATOM 7776 N N . LEU B 1 443 ? 11.980 16.208 28.816 1.00 16.15 ? 443 LEU B N 1 ATOM 7777 C CA . LEU B 1 443 ? 11.630 17.615 28.993 1.00 17.23 ? 443 LEU B CA 1 ATOM 7778 C C . LEU B 1 443 ? 10.166 17.848 29.300 1.00 17.71 ? 443 LEU B C 1 ATOM 7779 O O . LEU B 1 443 ? 9.825 18.725 30.093 1.00 19.64 ? 443 LEU B O 1 ATOM 7780 C CB . LEU B 1 443 ? 12.035 18.411 27.755 1.00 18.95 ? 443 LEU B CB 1 ATOM 7781 C CG . LEU B 1 443 ? 13.435 18.140 27.197 1.00 17.54 ? 443 LEU B CG 1 ATOM 7782 C CD1 . LEU B 1 443 ? 13.628 18.946 25.954 1.00 17.25 ? 443 LEU B CD1 1 ATOM 7783 C CD2 . LEU B 1 443 ? 14.495 18.479 28.209 1.00 19.33 ? 443 LEU B CD2 1 ATOM 7784 N N . GLY B 1 444 ? 9.312 17.038 28.691 1.00 17.58 ? 444 GLY B N 1 ATOM 7785 C CA . GLY B 1 444 ? 7.890 17.163 28.926 1.00 16.81 ? 444 GLY B CA 1 ATOM 7786 C C . GLY B 1 444 ? 7.059 16.164 28.159 1.00 16.41 ? 444 GLY B C 1 ATOM 7787 O O . GLY B 1 444 ? 7.563 15.441 27.296 1.00 16.08 ? 444 GLY B O 1 ATOM 7788 N N . ARG B 1 445 ? 5.783 16.107 28.523 1.00 15.63 ? 445 ARG B N 1 ATOM 7789 C CA . ARG B 1 445 ? 4.814 15.230 27.889 1.00 18.37 ? 445 ARG B CA 1 ATOM 7790 C C . ARG B 1 445 ? 3.441 15.857 27.998 1.00 18.35 ? 445 ARG B C 1 ATOM 7791 O O . ARG B 1 445 ? 3.246 16.798 28.759 1.00 19.19 ? 445 ARG B O 1 ATOM 7792 C CB . ARG B 1 445 ? 4.814 13.824 28.519 1.00 19.11 ? 445 ARG B CB 1 ATOM 7793 C CG . ARG B 1 445 ? 4.392 13.747 29.972 1.00 20.43 ? 445 ARG B CG 1 ATOM 7794 C CD . ARG B 1 445 ? 4.404 12.320 30.454 1.00 21.32 ? 445 ARG B CD 1 ATOM 7795 N NE . ARG B 1 445 ? 4.042 12.247 31.865 1.00 21.99 ? 445 ARG B NE 1 ATOM 7796 C CZ . ARG B 1 445 ? 4.485 11.323 32.709 1.00 22.57 ? 445 ARG B CZ 1 ATOM 7797 N NH1 . ARG B 1 445 ? 5.315 10.370 32.292 1.00 21.91 ? 445 ARG B NH1 1 ATOM 7798 N NH2 . ARG B 1 445 ? 4.145 11.386 33.992 1.00 23.19 ? 445 ARG B NH2 1 ATOM 7799 N N . SER B 1 446 ? 2.497 15.335 27.222 1.00 19.21 ? 446 SER B N 1 ATOM 7800 C CA . SER B 1 446 ? 1.115 15.797 27.237 1.00 19.61 ? 446 SER B CA 1 ATOM 7801 C C . SER B 1 446 ? 0.512 15.558 28.639 1.00 19.34 ? 446 SER B C 1 ATOM 7802 O O . SER B 1 446 ? 0.958 14.636 29.333 1.00 19.66 ? 446 SER B O 1 ATOM 7803 C CB . SER B 1 446 ? 0.343 15.055 26.155 1.00 19.40 ? 446 SER B CB 1 ATOM 7804 O OG . SER B 1 446 ? 0.663 13.683 26.146 1.00 17.49 ? 446 SER B OG 1 ATOM 7805 N N . PRO B 1 447 ? -0.465 16.395 29.084 1.00 18.70 ? 447 PRO B N 1 ATOM 7806 C CA . PRO B 1 447 ? -1.087 16.246 30.413 1.00 19.65 ? 447 PRO B CA 1 ATOM 7807 C C . PRO B 1 447 ? -1.497 14.834 30.843 1.00 20.86 ? 447 PRO B C 1 ATOM 7808 O O . PRO B 1 447 ? -2.135 14.093 30.070 1.00 20.34 ? 447 PRO B O 1 ATOM 7809 C CB . PRO B 1 447 ? -2.307 17.163 30.322 1.00 19.50 ? 447 PRO B CB 1 ATOM 7810 C CG . PRO B 1 447 ? -1.830 18.258 29.464 1.00 20.15 ? 447 PRO B CG 1 ATOM 7811 C CD . PRO B 1 447 ? -1.104 17.517 28.361 1.00 18.77 ? 447 PRO B CD 1 ATOM 7812 N N . ASP B 1 448 ? -1.082 14.466 32.061 1.00 19.00 ? 448 ASP B N 1 ATOM 7813 C CA . ASP B 1 448 ? -1.394 13.165 32.653 1.00 19.05 ? 448 ASP B CA 1 ATOM 7814 C C . ASP B 1 448 ? -2.907 12.989 32.783 1.00 20.10 ? 448 ASP B C 1 ATOM 7815 O O . ASP B 1 448 ? -3.556 13.661 33.576 1.00 20.88 ? 448 ASP B O 1 ATOM 7816 C CB . ASP B 1 448 ? -0.742 13.022 34.037 1.00 17.95 ? 448 ASP B CB 1 ATOM 7817 C CG . ASP B 1 448 ? 0.773 12.866 33.978 1.00 15.72 ? 448 ASP B CG 1 ATOM 7818 O OD1 . ASP B 1 448 ? 1.349 12.833 32.868 1.00 9.64 ? 448 ASP B OD1 1 ATOM 7819 O OD2 . ASP B 1 448 ? 1.383 12.755 35.070 1.00 16.83 ? 448 ASP B OD2 1 ATOM 7820 N N . VAL B 1 449 ? -3.457 12.172 31.891 1.00 22.21 ? 449 VAL B N 1 ATOM 7821 C CA . VAL B 1 449 ? -4.887 11.856 31.832 1.00 23.15 ? 449 VAL B CA 1 ATOM 7822 C C . VAL B 1 449 ? -4.991 10.318 31.796 1.00 23.40 ? 449 VAL B C 1 ATOM 7823 O O . VAL B 1 449 ? -3.953 9.656 31.660 1.00 24.48 ? 449 VAL B O 1 ATOM 7824 C CB . VAL B 1 449 ? -5.547 12.483 30.532 1.00 24.90 ? 449 VAL B CB 1 ATOM 7825 C CG1 . VAL B 1 449 ? -5.598 14.006 30.623 1.00 25.97 ? 449 VAL B CG1 1 ATOM 7826 C CG2 . VAL B 1 449 ? -4.833 12.026 29.249 1.00 24.53 ? 449 VAL B CG2 1 ATOM 7827 N N . PRO B 1 450 ? -6.203 9.724 32.012 1.00 22.99 ? 450 PRO B N 1 ATOM 7828 C CA . PRO B 1 450 ? -6.258 8.255 31.949 1.00 23.09 ? 450 PRO B CA 1 ATOM 7829 C C . PRO B 1 450 ? -5.884 7.686 30.574 1.00 24.20 ? 450 PRO B C 1 ATOM 7830 O O . PRO B 1 450 ? -6.258 8.242 29.544 1.00 22.97 ? 450 PRO B O 1 ATOM 7831 C CB . PRO B 1 450 ? -7.696 7.954 32.344 1.00 23.96 ? 450 PRO B CB 1 ATOM 7832 C CG . PRO B 1 450 ? -7.955 8.990 33.360 1.00 23.45 ? 450 PRO B CG 1 ATOM 7833 C CD . PRO B 1 450 ? -7.419 10.227 32.686 1.00 22.21 ? 450 PRO B CD 1 ATOM 7834 N N . ALA B 1 451 ? -5.096 6.611 30.582 1.00 24.29 ? 451 ALA B N 1 ATOM 7835 C CA . ALA B 1 451 ? -4.584 5.976 29.367 1.00 25.32 ? 451 ALA B CA 1 ATOM 7836 C C . ALA B 1 451 ? -5.594 5.491 28.330 1.00 26.37 ? 451 ALA B C 1 ATOM 7837 O O . ALA B 1 451 ? -5.337 5.581 27.125 1.00 28.24 ? 451 ALA B O 1 ATOM 7838 C CB . ALA B 1 451 ? -3.626 4.863 29.739 1.00 26.73 ? 451 ALA B CB 1 ATOM 7839 N N . ALA B 1 452 ? -6.745 5.011 28.797 1.00 26.75 ? 452 ALA B N 1 ATOM 7840 C CA . ALA B 1 452 ? -7.800 4.519 27.913 1.00 26.42 ? 452 ALA B CA 1 ATOM 7841 C C . ALA B 1 452 ? -8.863 5.574 27.635 1.00 26.40 ? 452 ALA B C 1 ATOM 7842 O O . ALA B 1 452 ? -9.901 5.265 27.041 1.00 27.77 ? 452 ALA B O 1 ATOM 7843 C CB . ALA B 1 452 ? -8.435 3.268 28.496 1.00 26.62 ? 452 ALA B CB 1 ATOM 7844 N N . SER B 1 453 ? -8.589 6.817 28.043 1.00 26.90 ? 453 SER B N 1 ATOM 7845 C CA . SER B 1 453 ? -9.505 7.947 27.847 1.00 28.44 ? 453 SER B CA 1 ATOM 7846 C C . SER B 1 453 ? -9.674 8.357 26.400 1.00 30.29 ? 453 SER B C 1 ATOM 7847 O O . SER B 1 453 ? -10.724 8.888 26.024 1.00 31.75 ? 453 SER B O 1 ATOM 7848 C CB . SER B 1 453 ? -9.053 9.180 28.630 1.00 26.58 ? 453 SER B CB 1 ATOM 7849 O OG . SER B 1 453 ? -9.449 9.103 29.982 1.00 27.45 ? 453 SER B OG 1 ATOM 7850 N N . GLN B 1 454 ? -8.635 8.092 25.602 1.00 31.08 ? 454 GLN B N 1 ATOM 7851 C CA . GLN B 1 454 ? -8.563 8.437 24.178 1.00 31.82 ? 454 GLN B CA 1 ATOM 7852 C C . GLN B 1 454 ? -8.656 9.955 23.958 1.00 30.95 ? 454 GLN B C 1 ATOM 7853 O O . GLN B 1 454 ? -9.194 10.434 22.953 1.00 30.59 ? 454 GLN B O 1 ATOM 7854 C CB . GLN B 1 454 ? -9.589 7.645 23.328 1.00 33.03 ? 454 GLN B CB 1 ATOM 7855 C CG . GLN B 1 454 ? -9.430 6.107 23.352 1.00 33.57 ? 454 GLN B CG 1 ATOM 7856 C CD . GLN B 1 454 ? -8.051 5.618 22.915 1.00 36.05 ? 454 GLN B CD 1 ATOM 7857 O OE1 . GLN B 1 454 ? -7.461 6.137 21.965 1.00 37.68 ? 454 GLN B OE1 1 ATOM 7858 N NE2 . GLN B 1 454 ? -7.533 4.614 23.614 1.00 36.52 ? 454 GLN B NE2 1 ATOM 7859 N N . GLN B 1 455 ? -8.164 10.690 24.962 1.00 30.98 ? 455 GLN B N 1 ATOM 7860 C CA . GLN B 1 455 ? -8.102 12.150 24.962 1.00 30.16 ? 455 GLN B CA 1 ATOM 7861 C C . GLN B 1 455 ? -6.844 12.510 24.199 1.00 29.93 ? 455 GLN B C 1 ATOM 7862 O O . GLN B 1 455 ? -5.777 11.938 24.441 1.00 30.29 ? 455 GLN B O 1 ATOM 7863 C CB . GLN B 1 455 ? -8.019 12.710 26.385 1.00 28.75 ? 455 GLN B CB 1 ATOM 7864 C CG . GLN B 1 455 ? -9.369 12.931 27.038 1.00 29.14 ? 455 GLN B CG 1 ATOM 7865 C CD . GLN B 1 455 ? -9.267 13.559 28.414 1.00 28.63 ? 455 GLN B CD 1 ATOM 7866 O OE1 . GLN B 1 455 ? -9.786 14.648 28.652 1.00 29.29 ? 455 GLN B OE1 1 ATOM 7867 N NE2 . GLN B 1 455 ? -8.625 12.860 29.336 1.00 26.49 ? 455 GLN B NE2 1 ATOM 7868 N N . ARG B 1 456 ? -6.998 13.418 23.238 1.00 29.65 ? 456 ARG B N 1 ATOM 7869 C CA . ARG B 1 456 ? -5.905 13.850 22.379 1.00 28.10 ? 456 ARG B CA 1 ATOM 7870 C C . ARG B 1 456 ? -5.317 15.203 22.736 1.00 25.66 ? 456 ARG B C 1 ATOM 7871 O O . ARG B 1 456 ? -6.001 16.080 23.255 1.00 24.52 ? 456 ARG B O 1 ATOM 7872 C CB . ARG B 1 456 ? -6.355 13.863 20.910 1.00 29.85 ? 456 ARG B CB 1 ATOM 7873 C CG . ARG B 1 456 ? -7.179 12.655 20.467 1.00 31.96 ? 456 ARG B CG 1 ATOM 7874 C CD . ARG B 1 456 ? -6.406 11.355 20.566 1.00 33.82 ? 456 ARG B CD 1 ATOM 7875 N NE . ARG B 1 456 ? -7.260 10.206 20.301 1.00 38.53 ? 456 ARG B NE 1 ATOM 7876 C CZ . ARG B 1 456 ? -7.208 9.462 19.200 1.00 40.25 ? 456 ARG B CZ 1 ATOM 7877 N NH1 . ARG B 1 456 ? -6.328 9.731 18.243 1.00 39.43 ? 456 ARG B NH1 1 ATOM 7878 N NH2 . ARG B 1 456 ? -8.075 8.472 19.038 1.00 40.68 ? 456 ARG B NH2 1 ATOM 7879 N N . PHE B 1 457 ? -4.014 15.324 22.505 1.00 25.26 ? 457 PHE B N 1 ATOM 7880 C CA . PHE B 1 457 ? -3.253 16.548 22.745 1.00 25.21 ? 457 PHE B CA 1 ATOM 7881 C C . PHE B 1 457 ? -2.205 16.671 21.648 1.00 24.69 ? 457 PHE B C 1 ATOM 7882 O O . PHE B 1 457 ? -1.532 15.697 21.314 1.00 23.69 ? 457 PHE B O 1 ATOM 7883 C CB . PHE B 1 457 ? -2.499 16.510 24.087 1.00 24.91 ? 457 PHE B CB 1 ATOM 7884 C CG . PHE B 1 457 ? -3.380 16.462 25.300 1.00 26.61 ? 457 PHE B CG 1 ATOM 7885 C CD1 . PHE B 1 457 ? -4.051 17.616 25.746 1.00 26.03 ? 457 PHE B CD1 1 ATOM 7886 C CD2 . PHE B 1 457 ? -3.541 15.258 26.013 1.00 26.21 ? 457 PHE B CD2 1 ATOM 7887 C CE1 . PHE B 1 457 ? -4.882 17.572 26.900 1.00 28.70 ? 457 PHE B CE1 1 ATOM 7888 C CE2 . PHE B 1 457 ? -4.364 15.194 27.162 1.00 26.79 ? 457 PHE B CE2 1 ATOM 7889 C CZ . PHE B 1 457 ? -5.039 16.356 27.609 1.00 27.20 ? 457 PHE B CZ 1 ATOM 7890 N N . VAL B 1 458 ? -2.129 17.854 21.047 1.00 25.72 ? 458 VAL B N 1 ATOM 7891 C CA . VAL B 1 458 ? -1.136 18.183 20.020 1.00 25.54 ? 458 VAL B CA 1 ATOM 7892 C C . VAL B 1 458 ? -0.326 19.291 20.700 1.00 25.71 ? 458 VAL B C 1 ATOM 7893 O O . VAL B 1 458 ? -0.870 20.026 21.534 1.00 27.65 ? 458 VAL B O 1 ATOM 7894 C CB . VAL B 1 458 ? -1.797 18.717 18.713 1.00 24.98 ? 458 VAL B CB 1 ATOM 7895 C CG1 . VAL B 1 458 ? -0.742 19.093 17.668 1.00 26.18 ? 458 VAL B CG1 1 ATOM 7896 C CG2 . VAL B 1 458 ? -2.724 17.677 18.129 1.00 24.64 ? 458 VAL B CG2 1 ATOM 7897 N N . PHE B 1 459 ? 0.967 19.385 20.382 1.00 26.68 ? 459 PHE B N 1 ATOM 7898 C CA . PHE B 1 459 ? 1.844 20.403 20.972 1.00 27.56 ? 459 PHE B CA 1 ATOM 7899 C C . PHE B 1 459 ? 1.417 21.806 20.572 1.00 28.01 ? 459 PHE B C 1 ATOM 7900 O O . PHE B 1 459 ? 1.461 22.172 19.398 1.00 27.76 ? 459 PHE B O 1 ATOM 7901 C CB . PHE B 1 459 ? 3.316 20.167 20.585 1.00 28.10 ? 459 PHE B CB 1 ATOM 7902 C CG . PHE B 1 459 ? 4.308 21.007 21.370 1.00 29.33 ? 459 PHE B CG 1 ATOM 7903 C CD1 . PHE B 1 459 ? 4.734 20.600 22.647 1.00 28.90 ? 459 PHE B CD1 1 ATOM 7904 C CD2 . PHE B 1 459 ? 4.812 22.220 20.844 1.00 30.21 ? 459 PHE B CD2 1 ATOM 7905 C CE1 . PHE B 1 459 ? 5.650 21.383 23.405 1.00 28.25 ? 459 PHE B CE1 1 ATOM 7906 C CE2 . PHE B 1 459 ? 5.727 23.016 21.590 1.00 30.34 ? 459 PHE B CE2 1 ATOM 7907 C CZ . PHE B 1 459 ? 6.145 22.592 22.876 1.00 29.65 ? 459 PHE B CZ 1 ATOM 7908 N N . ASP B 1 460 ? 0.984 22.560 21.576 1.00 31.18 ? 460 ASP B N 1 ATOM 7909 C CA . ASP B 1 460 ? 0.550 23.943 21.409 1.00 34.52 ? 460 ASP B CA 1 ATOM 7910 C C . ASP B 1 460 ? 1.496 24.786 22.268 1.00 34.50 ? 460 ASP B C 1 ATOM 7911 O O . ASP B 1 460 ? 1.412 24.757 23.495 1.00 33.85 ? 460 ASP B O 1 ATOM 7912 C CB . ASP B 1 460 ? -0.921 24.111 21.852 1.00 36.58 ? 460 ASP B CB 1 ATOM 7913 C CG . ASP B 1 460 ? -1.449 25.544 21.676 1.00 38.82 ? 460 ASP B CG 1 ATOM 7914 O OD1 . ASP B 1 460 ? -1.021 26.247 20.731 1.00 40.40 ? 460 ASP B OD1 1 ATOM 7915 O OD2 . ASP B 1 460 ? -2.301 25.962 22.492 1.00 39.45 ? 460 ASP B OD2 1 ATOM 7916 N N . PRO B 1 461 ? 2.411 25.549 21.631 1.00 35.84 ? 461 PRO B N 1 ATOM 7917 C CA . PRO B 1 461 ? 3.373 26.399 22.348 1.00 36.64 ? 461 PRO B CA 1 ATOM 7918 C C . PRO B 1 461 ? 2.756 27.452 23.283 1.00 37.85 ? 461 PRO B C 1 ATOM 7919 O O . PRO B 1 461 ? 3.399 27.895 24.241 1.00 38.47 ? 461 PRO B O 1 ATOM 7920 C CB . PRO B 1 461 ? 4.180 27.031 21.212 1.00 36.88 ? 461 PRO B CB 1 ATOM 7921 C CG . PRO B 1 461 ? 3.238 27.023 20.054 1.00 38.22 ? 461 PRO B CG 1 ATOM 7922 C CD . PRO B 1 461 ? 2.605 25.674 20.173 1.00 36.60 ? 461 PRO B CD 1 ATOM 7923 N N . ALA B 1 462 ? 1.474 27.749 23.045 1.00 38.67 ? 462 ALA B N 1 ATOM 7924 C CA . ALA B 1 462 ? 0.689 28.721 23.811 1.00 39.47 ? 462 ALA B CA 1 ATOM 7925 C C . ALA B 1 462 ? 0.335 28.278 25.236 1.00 38.98 ? 462 ALA B C 1 ATOM 7926 O O . ALA B 1 462 ? -0.028 29.107 26.075 1.00 39.85 ? 462 ALA B O 1 ATOM 7927 C CB . ALA B 1 462 ? -0.585 29.086 23.040 1.00 39.55 ? 462 ALA B CB 1 ATOM 7928 N N . VAL B 1 463 ? 0.399 26.973 25.487 1.00 38.40 ? 463 VAL B N 1 ATOM 7929 C CA . VAL B 1 463 ? 0.105 26.414 26.809 1.00 37.81 ? 463 VAL B CA 1 ATOM 7930 C C . VAL B 1 463 ? 1.202 25.466 27.288 1.00 37.37 ? 463 VAL B C 1 ATOM 7931 O O . VAL B 1 463 ? 1.496 25.408 28.487 1.00 36.86 ? 463 VAL B O 1 ATOM 7932 C CB . VAL B 1 463 ? -1.272 25.642 26.859 1.00 37.98 ? 463 VAL B CB 1 ATOM 7933 C CG1 . VAL B 1 463 ? -2.445 26.613 26.944 1.00 38.20 ? 463 VAL B CG1 1 ATOM 7934 C CG2 . VAL B 1 463 ? -1.443 24.731 25.649 1.00 37.72 ? 463 VAL B CG2 1 ATOM 7935 N N . ASP B 1 464 ? 1.857 24.805 26.332 1.00 36.10 ? 464 ASP B N 1 ATOM 7936 C CA . ASP B 1 464 ? 2.878 23.796 26.619 1.00 36.57 ? 464 ASP B CA 1 ATOM 7937 C C . ASP B 1 464 ? 4.356 24.147 26.817 1.00 35.94 ? 464 ASP B C 1 ATOM 7938 O O . ASP B 1 464 ? 5.095 23.340 27.394 1.00 34.89 ? 464 ASP B O 1 ATOM 7939 C CB . ASP B 1 464 ? 2.742 22.640 25.623 1.00 36.71 ? 464 ASP B CB 1 ATOM 7940 C CG . ASP B 1 464 ? 1.395 21.913 25.732 1.00 37.13 ? 464 ASP B CG 1 ATOM 7941 O OD1 . ASP B 1 464 ? 0.947 21.617 26.864 1.00 37.29 ? 464 ASP B OD1 1 ATOM 7942 O OD2 . ASP B 1 464 ? 0.810 21.587 24.676 1.00 37.79 ? 464 ASP B OD2 1 ATOM 7943 N N . LEU B 1 465 ? 4.794 25.324 26.364 1.00 35.66 ? 465 LEU B N 1 ATOM 7944 C CA . LEU B 1 465 ? 6.197 25.739 26.535 1.00 35.13 ? 465 LEU B CA 1 ATOM 7945 C C . LEU B 1 465 ? 6.532 26.021 27.998 1.00 35.18 ? 465 LEU B C 1 ATOM 7946 O O . LEU B 1 465 ? 7.689 25.902 28.427 1.00 36.28 ? 465 LEU B O 1 ATOM 7947 C CB . LEU B 1 465 ? 6.535 26.953 25.665 1.00 34.27 ? 465 LEU B CB 1 ATOM 7948 C CG . LEU B 1 465 ? 7.029 26.677 24.238 1.00 34.54 ? 465 LEU B CG 1 ATOM 7949 C CD1 . LEU B 1 465 ? 7.088 27.973 23.489 1.00 34.28 ? 465 LEU B CD1 1 ATOM 7950 C CD2 . LEU B 1 465 ? 8.395 26.010 24.210 1.00 33.62 ? 465 LEU B CD2 1 ATOM 7951 N N . ALA B 1 466 ? 5.481 26.323 28.757 1.00 33.35 ? 466 ALA B N 1 ATOM 7952 C CA . ALA B 1 466 ? 5.562 26.609 30.181 1.00 32.24 ? 466 ALA B CA 1 ATOM 7953 C C . ALA B 1 466 ? 5.508 25.306 30.982 1.00 31.14 ? 466 ALA B C 1 ATOM 7954 O O . ALA B 1 466 ? 5.892 25.272 32.153 1.00 31.03 ? 466 ALA B O 1 ATOM 7955 C CB . ALA B 1 466 ? 4.413 27.524 30.582 1.00 31.56 ? 466 ALA B CB 1 ATOM 7956 N N . ARG B 1 467 ? 5.035 24.240 30.333 1.00 29.56 ? 467 ARG B N 1 ATOM 7957 C CA . ARG B 1 467 ? 4.922 22.920 30.953 1.00 28.67 ? 467 ARG B CA 1 ATOM 7958 C C . ARG B 1 467 ? 6.206 22.094 30.889 1.00 28.66 ? 467 ARG B C 1 ATOM 7959 O O . ARG B 1 467 ? 6.278 21.000 31.451 1.00 30.10 ? 467 ARG B O 1 ATOM 7960 C CB . ARG B 1 467 ? 3.766 22.134 30.336 1.00 26.16 ? 467 ARG B CB 1 ATOM 7961 C CG . ARG B 1 467 ? 2.381 22.596 30.774 1.00 24.55 ? 467 ARG B CG 1 ATOM 7962 C CD . ARG B 1 467 ? 1.294 21.618 30.358 1.00 23.74 ? 467 ARG B CD 1 ATOM 7963 N NE . ARG B 1 467 ? 1.417 20.336 31.057 1.00 24.82 ? 467 ARG B NE 1 ATOM 7964 C CZ . ARG B 1 467 ? 1.801 19.191 30.495 1.00 23.90 ? 467 ARG B CZ 1 ATOM 7965 N NH1 . ARG B 1 467 ? 2.107 19.152 29.200 1.00 23.73 ? 467 ARG B NH1 1 ATOM 7966 N NH2 . ARG B 1 467 ? 1.903 18.092 31.237 1.00 22.21 ? 467 ARG B NH2 1 ATOM 7967 N N . LEU B 1 468 ? 7.220 22.633 30.216 1.00 28.56 ? 468 LEU B N 1 ATOM 7968 C CA . LEU B 1 468 ? 8.512 21.966 30.078 1.00 27.53 ? 468 LEU B CA 1 ATOM 7969 C C . LEU B 1 468 ? 9.460 22.326 31.227 1.00 26.61 ? 468 LEU B C 1 ATOM 7970 O O . LEU B 1 468 ? 9.278 23.346 31.892 1.00 27.58 ? 468 LEU B O 1 ATOM 7971 C CB . LEU B 1 468 ? 9.148 22.338 28.732 1.00 26.07 ? 468 LEU B CB 1 ATOM 7972 C CG . LEU B 1 468 ? 8.309 22.138 27.463 1.00 25.57 ? 468 LEU B CG 1 ATOM 7973 C CD1 . LEU B 1 468 ? 8.959 22.811 26.287 1.00 22.67 ? 468 LEU B CD1 1 ATOM 7974 C CD2 . LEU B 1 468 ? 8.076 20.666 27.189 1.00 26.29 ? 468 LEU B CD2 1 ATOM 7975 N N . ASN B 1 469 ? 10.441 21.461 31.473 1.00 26.50 ? 469 ASN B N 1 ATOM 7976 C CA . ASN B 1 469 ? 11.441 21.667 32.520 1.00 27.15 ? 469 ASN B CA 1 ATOM 7977 C C . ASN B 1 469 ? 12.819 21.336 31.959 1.00 26.63 ? 469 ASN B C 1 ATOM 7978 O O . ASN B 1 469 ? 13.112 20.185 31.643 1.00 26.92 ? 469 ASN B O 1 ATOM 7979 C CB . ASN B 1 469 ? 11.133 20.802 33.760 1.00 28.95 ? 469 ASN B CB 1 ATOM 7980 C CG . ASN B 1 469 ? 12.194 20.929 34.869 1.00 30.41 ? 469 ASN B CG 1 ATOM 7981 O OD1 . ASN B 1 469 ? 12.751 22.006 35.110 1.00 32.59 ? 469 ASN B OD1 1 ATOM 7982 N ND2 . ASN B 1 469 ? 12.475 19.818 35.536 1.00 30.21 ? 469 ASN B ND2 1 ATOM 7983 N N . GLY B 1 470 ? 13.654 22.364 31.847 1.00 26.68 ? 470 GLY B N 1 ATOM 7984 C CA . GLY B 1 470 ? 15.002 22.191 31.347 1.00 25.71 ? 470 GLY B CA 1 ATOM 7985 C C . GLY B 1 470 ? 16.029 22.183 32.456 1.00 25.93 ? 470 GLY B C 1 ATOM 7986 O O . GLY B 1 470 ? 17.216 22.001 32.190 1.00 26.55 ? 470 GLY B O 1 ATOM 7987 N N . ASP B 1 471 ? 15.569 22.398 33.691 1.00 26.88 ? 471 ASP B N 1 ATOM 7988 C CA . ASP B 1 471 ? 16.436 22.422 34.868 1.00 26.86 ? 471 ASP B CA 1 ATOM 7989 C C . ASP B 1 471 ? 16.372 21.055 35.538 1.00 25.14 ? 471 ASP B C 1 ATOM 7990 O O . ASP B 1 471 ? 15.375 20.703 36.177 1.00 25.84 ? 471 ASP B O 1 ATOM 7991 C CB . ASP B 1 471 ? 16.008 23.540 35.826 1.00 30.91 ? 471 ASP B CB 1 ATOM 7992 C CG . ASP B 1 471 ? 17.121 23.960 36.784 1.00 35.32 ? 471 ASP B CG 1 ATOM 7993 O OD1 . ASP B 1 471 ? 18.309 23.967 36.383 1.00 39.17 ? 471 ASP B OD1 1 ATOM 7994 O OD2 . ASP B 1 471 ? 16.803 24.302 37.943 1.00 38.99 ? 471 ASP B OD2 1 ATOM 7995 N N . ASN B 1 472 ? 17.443 20.283 35.322 1.00 23.05 ? 472 ASN B N 1 ATOM 7996 C CA . ASN B 1 472 ? 17.639 18.906 35.803 1.00 19.33 ? 472 ASN B CA 1 ATOM 7997 C C . ASN B 1 472 ? 16.417 17.965 35.672 1.00 18.03 ? 472 ASN B C 1 ATOM 7998 O O . ASN B 1 472 ? 15.922 17.417 36.670 1.00 18.66 ? 472 ASN B O 1 ATOM 7999 C CB . ASN B 1 472 ? 18.244 18.876 37.218 1.00 19.01 ? 472 ASN B CB 1 ATOM 8000 C CG . ASN B 1 472 ? 18.910 17.538 37.542 1.00 19.69 ? 472 ASN B CG 1 ATOM 8001 O OD1 . ASN B 1 472 ? 19.394 16.842 36.644 1.00 17.29 ? 472 ASN B OD1 1 ATOM 8002 N ND2 . ASN B 1 472 ? 18.933 17.175 38.823 1.00 18.73 ? 472 ASN B ND2 1 ATOM 8003 N N . PRO B 1 473 ? 15.946 17.733 34.423 1.00 14.88 ? 473 PRO B N 1 ATOM 8004 C CA . PRO B 1 473 ? 14.795 16.859 34.205 1.00 12.75 ? 473 PRO B CA 1 ATOM 8005 C C . PRO B 1 473 ? 15.197 15.375 34.294 1.00 11.67 ? 473 PRO B C 1 ATOM 8006 O O . PRO B 1 473 ? 16.391 15.070 34.447 1.00 11.12 ? 473 PRO B O 1 ATOM 8007 C CB . PRO B 1 473 ? 14.345 17.273 32.801 1.00 14.92 ? 473 PRO B CB 1 ATOM 8008 C CG . PRO B 1 473 ? 15.594 17.539 32.113 1.00 14.19 ? 473 PRO B CG 1 ATOM 8009 C CD . PRO B 1 473 ? 16.461 18.235 33.129 1.00 14.02 ? 473 PRO B CD 1 ATOM 8010 N N . PRO B 1 474 ? 14.214 14.443 34.305 1.00 11.51 ? 474 PRO B N 1 ATOM 8011 C CA . PRO B 1 474 ? 14.587 13.025 34.375 1.00 11.28 ? 474 PRO B CA 1 ATOM 8012 C C . PRO B 1 474 ? 15.474 12.632 33.199 1.00 12.55 ? 474 PRO B C 1 ATOM 8013 O O . PRO B 1 474 ? 15.222 13.029 32.056 1.00 13.67 ? 474 PRO B O 1 ATOM 8014 C CB . PRO B 1 474 ? 13.238 12.318 34.276 1.00 11.61 ? 474 PRO B CB 1 ATOM 8015 C CG . PRO B 1 474 ? 12.345 13.242 34.949 1.00 10.40 ? 474 PRO B CG 1 ATOM 8016 C CD . PRO B 1 474 ? 12.747 14.584 34.449 1.00 10.79 ? 474 PRO B CD 1 ATOM 8017 N N . ARG B 1 475 ? 16.572 11.961 33.518 1.00 13.53 ? 475 ARG B N 1 ATOM 8018 C CA . ARG B 1 475 ? 17.508 11.496 32.513 1.00 14.57 ? 475 ARG B CA 1 ATOM 8019 C C . ARG B 1 475 ? 17.474 9.976 32.576 1.00 14.61 ? 475 ARG B C 1 ATOM 8020 O O . ARG B 1 475 ? 17.754 9.405 33.622 1.00 14.39 ? 475 ARG B O 1 ATOM 8021 C CB . ARG B 1 475 ? 18.913 12.034 32.798 1.00 15.01 ? 475 ARG B CB 1 ATOM 8022 C CG . ARG B 1 475 ? 19.948 11.743 31.715 1.00 14.68 ? 475 ARG B CG 1 ATOM 8023 C CD . ARG B 1 475 ? 21.259 12.473 31.950 1.00 14.40 ? 475 ARG B CD 1 ATOM 8024 N NE . ARG B 1 475 ? 21.998 11.989 33.114 1.00 14.03 ? 475 ARG B NE 1 ATOM 8025 C CZ . ARG B 1 475 ? 22.150 12.666 34.252 1.00 13.52 ? 475 ARG B CZ 1 ATOM 8026 N NH1 . ARG B 1 475 ? 21.605 13.870 34.405 1.00 12.79 ? 475 ARG B NH1 1 ATOM 8027 N NH2 . ARG B 1 475 ? 22.856 12.139 35.237 1.00 10.63 ? 475 ARG B NH2 1 ATOM 8028 N N . ARG B 1 476 ? 17.039 9.342 31.486 1.00 13.76 ? 476 ARG B N 1 ATOM 8029 C CA . ARG B 1 476 ? 16.945 7.880 31.408 1.00 14.19 ? 476 ARG B CA 1 ATOM 8030 C C . ARG B 1 476 ? 16.913 7.355 29.973 1.00 14.60 ? 476 ARG B C 1 ATOM 8031 O O . ARG B 1 476 ? 16.799 8.134 29.028 1.00 16.72 ? 476 ARG B O 1 ATOM 8032 C CB . ARG B 1 476 ? 15.744 7.358 32.219 1.00 14.22 ? 476 ARG B CB 1 ATOM 8033 C CG . ARG B 1 476 ? 14.350 7.839 31.815 1.00 12.01 ? 476 ARG B CG 1 ATOM 8034 C CD . ARG B 1 476 ? 13.333 7.526 32.919 1.00 12.63 ? 476 ARG B CD 1 ATOM 8035 N NE . ARG B 1 476 ? 13.423 6.140 33.406 1.00 14.44 ? 476 ARG B NE 1 ATOM 8036 C CZ . ARG B 1 476 ? 12.876 5.691 34.536 1.00 13.33 ? 476 ARG B CZ 1 ATOM 8037 N NH1 . ARG B 1 476 ? 12.179 6.507 35.319 1.00 15.99 ? 476 ARG B NH1 1 ATOM 8038 N NH2 . ARG B 1 476 ? 13.055 4.429 34.905 1.00 9.06 ? 476 ARG B NH2 1 ATOM 8039 N N . ASP B 1 477 ? 17.047 6.039 29.813 1.00 15.17 ? 477 ASP B N 1 ATOM 8040 C CA . ASP B 1 477 ? 17.052 5.431 28.487 1.00 13.47 ? 477 ASP B CA 1 ATOM 8041 C C . ASP B 1 477 ? 15.680 5.000 27.974 1.00 11.98 ? 477 ASP B C 1 ATOM 8042 O O . ASP B 1 477 ? 15.515 4.785 26.768 1.00 12.06 ? 477 ASP B O 1 ATOM 8043 C CB . ASP B 1 477 ? 18.091 4.290 28.391 1.00 14.35 ? 477 ASP B CB 1 ATOM 8044 C CG . ASP B 1 477 ? 17.863 3.160 29.402 1.00 15.86 ? 477 ASP B CG 1 ATOM 8045 O OD1 . ASP B 1 477 ? 16.716 2.699 29.590 1.00 17.91 ? 477 ASP B OD1 1 ATOM 8046 O OD2 . ASP B 1 477 ? 18.860 2.690 29.979 1.00 15.76 ? 477 ASP B OD2 1 ATOM 8047 N N . THR B 1 478 ? 14.705 4.899 28.881 1.00 7.89 ? 478 THR B N 1 ATOM 8048 C CA . THR B 1 478 ? 13.343 4.509 28.518 1.00 9.18 ? 478 THR B CA 1 ATOM 8049 C C . THR B 1 478 ? 12.278 5.321 29.263 1.00 9.15 ? 478 THR B C 1 ATOM 8050 O O . THR B 1 478 ? 12.367 5.514 30.480 1.00 8.54 ? 478 THR B O 1 ATOM 8051 C CB . THR B 1 478 ? 13.104 2.994 28.748 1.00 10.13 ? 478 THR B CB 1 ATOM 8052 O OG1 . THR B 1 478 ? 14.227 2.254 28.258 1.00 11.67 ? 478 THR B OG1 1 ATOM 8053 C CG2 . THR B 1 478 ? 11.855 2.513 28.000 1.00 14.08 ? 478 THR B CG2 1 ATOM 8054 N N . THR B 1 479 ? 11.279 5.798 28.524 1.00 7.31 ? 479 THR B N 1 ATOM 8055 C CA . THR B 1 479 ? 10.173 6.572 29.109 1.00 7.23 ? 479 THR B CA 1 ATOM 8056 C C . THR B 1 479 ? 8.899 6.379 28.299 1.00 6.52 ? 479 THR B C 1 ATOM 8057 O O . THR B 1 479 ? 8.943 6.027 27.118 1.00 6.34 ? 479 THR B O 1 ATOM 8058 C CB . THR B 1 479 ? 10.502 8.117 29.261 1.00 6.84 ? 479 THR B CB 1 ATOM 8059 O OG1 . THR B 1 479 ? 9.590 8.718 30.194 1.00 7.94 ? 479 THR B OG1 1 ATOM 8060 C CG2 . THR B 1 479 ? 10.392 8.866 27.933 1.00 4.80 ? 479 THR B CG2 1 ATOM 8061 N N . MET B 1 480 ? 7.776 6.707 28.921 1.00 6.90 ? 480 MET B N 1 ATOM 8062 C CA . MET B 1 480 ? 6.478 6.566 28.288 1.00 7.57 ? 480 MET B CA 1 ATOM 8063 C C . MET B 1 480 ? 6.033 7.679 27.360 1.00 9.99 ? 480 MET B C 1 ATOM 8064 O O . MET B 1 480 ? 6.242 8.870 27.625 1.00 10.03 ? 480 MET B O 1 ATOM 8065 C CB . MET B 1 480 ? 5.397 6.321 29.339 1.00 8.72 ? 480 MET B CB 1 ATOM 8066 C CG . MET B 1 480 ? 5.521 4.980 30.029 1.00 7.48 ? 480 MET B CG 1 ATOM 8067 S SD . MET B 1 480 ? 5.594 3.643 28.828 1.00 11.66 ? 480 MET B SD 1 ATOM 8068 C CE . MET B 1 480 ? 3.892 3.425 28.428 1.00 3.49 ? 480 MET B CE 1 ATOM 8069 N N . LEU B 1 481 ? 5.468 7.255 26.233 1.00 10.67 ? 481 LEU B N 1 ATOM 8070 C CA . LEU B 1 481 ? 4.901 8.149 25.239 1.00 12.45 ? 481 LEU B CA 1 ATOM 8071 C C . LEU B 1 481 ? 3.402 7.974 25.517 1.00 13.35 ? 481 LEU B C 1 ATOM 8072 O O . LEU B 1 481 ? 2.822 6.950 25.157 1.00 15.37 ? 481 LEU B O 1 ATOM 8073 C CB . LEU B 1 481 ? 5.279 7.693 23.820 1.00 11.75 ? 481 LEU B CB 1 ATOM 8074 C CG . LEU B 1 481 ? 4.589 8.309 22.593 1.00 13.77 ? 481 LEU B CG 1 ATOM 8075 C CD1 . LEU B 1 481 ? 4.799 9.818 22.497 1.00 13.11 ? 481 LEU B CD1 1 ATOM 8076 C CD2 . LEU B 1 481 ? 5.036 7.613 21.333 1.00 10.57 ? 481 LEU B CD2 1 ATOM 8077 N N . PRO B 1 482 ? 2.770 8.946 26.210 1.00 14.42 ? 482 PRO B N 1 ATOM 8078 C CA . PRO B 1 482 ? 1.337 8.879 26.544 1.00 15.28 ? 482 PRO B CA 1 ATOM 8079 C C . PRO B 1 482 ? 0.372 8.746 25.365 1.00 15.97 ? 482 PRO B C 1 ATOM 8080 O O . PRO B 1 482 ? 0.565 9.379 24.319 1.00 15.11 ? 482 PRO B O 1 ATOM 8081 C CB . PRO B 1 482 ? 1.102 10.176 27.317 1.00 14.14 ? 482 PRO B CB 1 ATOM 8082 C CG . PRO B 1 482 ? 2.124 11.092 26.758 1.00 14.50 ? 482 PRO B CG 1 ATOM 8083 C CD . PRO B 1 482 ? 3.334 10.243 26.632 1.00 14.91 ? 482 PRO B CD 1 ATOM 8084 N N . ALA B 1 483 ? -0.648 7.903 25.554 1.00 16.10 ? 483 ALA B N 1 ATOM 8085 C CA . ALA B 1 483 ? -1.689 7.648 24.558 1.00 16.95 ? 483 ALA B CA 1 ATOM 8086 C C . ALA B 1 483 ? -2.400 8.938 24.154 1.00 17.76 ? 483 ALA B C 1 ATOM 8087 O O . ALA B 1 483 ? -2.740 9.761 25.017 1.00 17.02 ? 483 ALA B O 1 ATOM 8088 C CB . ALA B 1 483 ? -2.694 6.661 25.103 1.00 17.34 ? 483 ALA B CB 1 ATOM 8089 N N . GLY B 1 484 ? -2.512 9.145 22.840 1.00 16.29 ? 484 GLY B N 1 ATOM 8090 C CA . GLY B 1 484 ? -3.174 10.318 22.293 1.00 15.77 ? 484 GLY B CA 1 ATOM 8091 C C . GLY B 1 484 ? -2.423 11.633 22.356 1.00 17.89 ? 484 GLY B C 1 ATOM 8092 O O . GLY B 1 484 ? -2.846 12.608 21.731 1.00 20.37 ? 484 GLY B O 1 ATOM 8093 N N . GLY B 1 485 ? -1.289 11.649 23.057 1.00 16.82 ? 485 GLY B N 1 ATOM 8094 C CA . GLY B 1 485 ? -0.528 12.874 23.208 1.00 15.92 ? 485 GLY B CA 1 ATOM 8095 C C . GLY B 1 485 ? 0.828 13.015 22.550 1.00 15.40 ? 485 GLY B C 1 ATOM 8096 O O . GLY B 1 485 ? 1.033 12.622 21.400 1.00 14.03 ? 485 GLY B O 1 ATOM 8097 N N . TRP B 1 486 ? 1.738 13.644 23.288 1.00 14.54 ? 486 TRP B N 1 ATOM 8098 C CA . TRP B 1 486 ? 3.098 13.900 22.822 1.00 15.06 ? 486 TRP B CA 1 ATOM 8099 C C . TRP B 1 486 ? 4.152 13.752 23.918 1.00 14.08 ? 486 TRP B C 1 ATOM 8100 O O . TRP B 1 486 ? 3.830 13.655 25.105 1.00 14.04 ? 486 TRP B O 1 ATOM 8101 C CB . TRP B 1 486 ? 3.201 15.292 22.149 1.00 15.00 ? 486 TRP B CB 1 ATOM 8102 C CG . TRP B 1 486 ? 2.711 16.448 22.990 1.00 15.33 ? 486 TRP B CG 1 ATOM 8103 C CD1 . TRP B 1 486 ? 1.436 16.920 23.059 1.00 15.00 ? 486 TRP B CD1 1 ATOM 8104 C CD2 . TRP B 1 486 ? 3.471 17.204 23.947 1.00 16.67 ? 486 TRP B CD2 1 ATOM 8105 N NE1 . TRP B 1 486 ? 1.340 17.906 24.010 1.00 14.94 ? 486 TRP B NE1 1 ATOM 8106 C CE2 . TRP B 1 486 ? 2.574 18.099 24.575 1.00 17.36 ? 486 TRP B CE2 1 ATOM 8107 C CE3 . TRP B 1 486 ? 4.827 17.205 24.347 1.00 16.52 ? 486 TRP B CE3 1 ATOM 8108 C CZ2 . TRP B 1 486 ? 2.984 18.986 25.594 1.00 15.96 ? 486 TRP B CZ2 1 ATOM 8109 C CZ3 . TRP B 1 486 ? 5.239 18.094 25.361 1.00 15.94 ? 486 TRP B CZ3 1 ATOM 8110 C CH2 . TRP B 1 486 ? 4.311 18.971 25.973 1.00 14.47 ? 486 TRP B CH2 1 ATOM 8111 N N . LEU B 1 487 ? 5.410 13.793 23.497 1.00 13.09 ? 487 LEU B N 1 ATOM 8112 C CA . LEU B 1 487 ? 6.555 13.667 24.387 1.00 13.91 ? 487 LEU B CA 1 ATOM 8113 C C . LEU B 1 487 ? 7.715 14.475 23.825 1.00 12.00 ? 487 LEU B C 1 ATOM 8114 O O . LEU B 1 487 ? 7.974 14.437 22.618 1.00 12.97 ? 487 LEU B O 1 ATOM 8115 C CB . LEU B 1 487 ? 6.951 12.193 24.507 1.00 13.68 ? 487 LEU B CB 1 ATOM 8116 C CG . LEU B 1 487 ? 8.116 11.710 25.361 1.00 13.66 ? 487 LEU B CG 1 ATOM 8117 C CD1 . LEU B 1 487 ? 7.844 11.908 26.843 1.00 13.46 ? 487 LEU B CD1 1 ATOM 8118 C CD2 . LEU B 1 487 ? 8.339 10.238 25.059 1.00 15.72 ? 487 LEU B CD2 1 ATOM 8119 N N . LEU B 1 488 ? 8.392 15.223 24.695 1.00 10.75 ? 488 LEU B N 1 ATOM 8120 C CA . LEU B 1 488 ? 9.545 16.013 24.269 1.00 10.42 ? 488 LEU B CA 1 ATOM 8121 C C . LEU B 1 488 ? 10.815 15.461 24.897 1.00 8.74 ? 488 LEU B C 1 ATOM 8122 O O . LEU B 1 488 ? 10.914 15.343 26.118 1.00 9.92 ? 488 LEU B O 1 ATOM 8123 C CB . LEU B 1 488 ? 9.366 17.510 24.586 1.00 8.03 ? 488 LEU B CB 1 ATOM 8124 C CG . LEU B 1 488 ? 10.350 18.461 23.879 1.00 12.06 ? 488 LEU B CG 1 ATOM 8125 C CD1 . LEU B 1 488 ? 10.300 18.303 22.378 1.00 14.07 ? 488 LEU B CD1 1 ATOM 8126 C CD2 . LEU B 1 488 ? 10.086 19.896 24.224 1.00 12.05 ? 488 LEU B CD2 1 ATOM 8127 N N . LEU B 1 489 ? 11.756 15.060 24.046 1.00 7.95 ? 489 LEU B N 1 ATOM 8128 C CA . LEU B 1 489 ? 13.034 14.500 24.498 1.00 8.39 ? 489 LEU B CA 1 ATOM 8129 C C . LEU B 1 489 ? 14.221 15.293 23.999 1.00 9.45 ? 489 LEU B C 1 ATOM 8130 O O . LEU B 1 489 ? 14.081 16.113 23.093 1.00 10.86 ? 489 LEU B O 1 ATOM 8131 C CB . LEU B 1 489 ? 13.200 13.038 24.054 1.00 5.80 ? 489 LEU B CB 1 ATOM 8132 C CG . LEU B 1 489 ? 12.204 11.952 24.484 1.00 6.14 ? 489 LEU B CG 1 ATOM 8133 C CD1 . LEU B 1 489 ? 12.694 10.622 24.000 1.00 5.03 ? 489 LEU B CD1 1 ATOM 8134 C CD2 . LEU B 1 489 ? 11.997 11.916 26.001 1.00 7.61 ? 489 LEU B CD2 1 ATOM 8135 N N . ALA B 1 490 ? 15.377 15.061 24.626 1.00 11.37 ? 490 ALA B N 1 ATOM 8136 C CA . ALA B 1 490 ? 16.639 15.704 24.256 1.00 13.99 ? 490 ALA B CA 1 ATOM 8137 C C . ALA B 1 490 ? 17.863 14.899 24.670 1.00 15.36 ? 490 ALA B C 1 ATOM 8138 O O . ALA B 1 490 ? 17.939 14.397 25.792 1.00 16.92 ? 490 ALA B O 1 ATOM 8139 C CB . ALA B 1 490 ? 16.733 17.116 24.825 1.00 14.10 ? 490 ALA B CB 1 ATOM 8140 N N . PHE B 1 491 ? 18.802 14.766 23.736 1.00 15.61 ? 491 PHE B N 1 ATOM 8141 C CA . PHE B 1 491 ? 20.057 14.067 23.966 1.00 15.62 ? 491 PHE B CA 1 ATOM 8142 C C . PHE B 1 491 ? 21.223 14.817 23.316 1.00 16.18 ? 491 PHE B C 1 ATOM 8143 O O . PHE B 1 491 ? 21.070 15.430 22.253 1.00 15.55 ? 491 PHE B O 1 ATOM 8144 C CB . PHE B 1 491 ? 19.990 12.576 23.535 1.00 16.41 ? 491 PHE B CB 1 ATOM 8145 C CG . PHE B 1 491 ? 19.874 12.332 22.033 1.00 17.23 ? 491 PHE B CG 1 ATOM 8146 C CD1 . PHE B 1 491 ? 18.620 12.343 21.394 1.00 18.21 ? 491 PHE B CD1 1 ATOM 8147 C CD2 . PHE B 1 491 ? 21.011 11.987 21.275 1.00 16.03 ? 491 PHE B CD2 1 ATOM 8148 C CE1 . PHE B 1 491 ? 18.495 12.005 20.013 1.00 17.40 ? 491 PHE B CE1 1 ATOM 8149 C CE2 . PHE B 1 491 ? 20.905 11.650 19.897 1.00 17.39 ? 491 PHE B CE2 1 ATOM 8150 C CZ . PHE B 1 491 ? 19.638 11.657 19.265 1.00 16.97 ? 491 PHE B CZ 1 ATOM 8151 N N . ARG B 1 492 ? 22.366 14.813 23.998 1.00 18.42 ? 492 ARG B N 1 ATOM 8152 C CA . ARG B 1 492 ? 23.575 15.478 23.507 1.00 18.75 ? 492 ARG B CA 1 ATOM 8153 C C . ARG B 1 492 ? 24.310 14.510 22.595 1.00 17.78 ? 492 ARG B C 1 ATOM 8154 O O . ARG B 1 492 ? 24.570 13.376 22.982 1.00 17.61 ? 492 ARG B O 1 ATOM 8155 C CB . ARG B 1 492 ? 24.476 15.903 24.671 1.00 19.23 ? 492 ARG B CB 1 ATOM 8156 C CG . ARG B 1 492 ? 25.471 16.996 24.309 1.00 22.21 ? 492 ARG B CG 1 ATOM 8157 C CD . ARG B 1 492 ? 26.280 17.456 25.504 1.00 24.26 ? 492 ARG B CD 1 ATOM 8158 N NE . ARG B 1 492 ? 27.176 18.554 25.149 1.00 25.71 ? 492 ARG B NE 1 ATOM 8159 C CZ . ARG B 1 492 ? 27.704 19.419 26.015 1.00 28.97 ? 492 ARG B CZ 1 ATOM 8160 N NH1 . ARG B 1 492 ? 27.431 19.335 27.318 1.00 27.06 ? 492 ARG B NH1 1 ATOM 8161 N NH2 . ARG B 1 492 ? 28.526 20.368 25.575 1.00 29.63 ? 492 ARG B NH2 1 ATOM 8162 N N . THR B 1 493 ? 24.632 14.968 21.387 1.00 17.16 ? 493 THR B N 1 ATOM 8163 C CA . THR B 1 493 ? 25.325 14.148 20.396 1.00 16.60 ? 493 THR B CA 1 ATOM 8164 C C . THR B 1 493 ? 26.829 13.913 20.668 1.00 17.39 ? 493 THR B C 1 ATOM 8165 O O . THR B 1 493 ? 27.691 14.360 19.910 1.00 17.30 ? 493 THR B O 1 ATOM 8166 C CB . THR B 1 493 ? 25.090 14.698 18.970 1.00 14.88 ? 493 THR B CB 1 ATOM 8167 O OG1 . THR B 1 493 ? 25.447 16.083 18.912 1.00 14.97 ? 493 THR B OG1 1 ATOM 8168 C CG2 . THR B 1 493 ? 23.642 14.539 18.573 1.00 14.50 ? 493 THR B CG2 1 ATOM 8169 N N . ASP B 1 494 ? 27.117 13.166 21.735 1.00 18.00 ? 494 ASP B N 1 ATOM 8170 C CA . ASP B 1 494 ? 28.485 12.869 22.160 1.00 19.38 ? 494 ASP B CA 1 ATOM 8171 C C . ASP B 1 494 ? 28.947 11.439 21.869 1.00 20.23 ? 494 ASP B C 1 ATOM 8172 O O . ASP B 1 494 ? 29.997 11.004 22.368 1.00 21.39 ? 494 ASP B O 1 ATOM 8173 C CB . ASP B 1 494 ? 28.663 13.205 23.663 1.00 19.69 ? 494 ASP B CB 1 ATOM 8174 C CG . ASP B 1 494 ? 27.750 12.381 24.601 1.00 21.48 ? 494 ASP B CG 1 ATOM 8175 O OD1 . ASP B 1 494 ? 26.867 11.630 24.129 1.00 21.16 ? 494 ASP B OD1 1 ATOM 8176 O OD2 . ASP B 1 494 ? 27.923 12.497 25.838 1.00 23.22 ? 494 ASP B OD2 1 ATOM 8177 N N . ASN B 1 495 ? 28.184 10.727 21.040 1.00 20.35 ? 495 ASN B N 1 ATOM 8178 C CA . ASN B 1 495 ? 28.493 9.336 20.714 1.00 19.33 ? 495 ASN B CA 1 ATOM 8179 C C . ASN B 1 495 ? 28.126 8.963 19.263 1.00 18.70 ? 495 ASN B C 1 ATOM 8180 O O . ASN B 1 495 ? 27.030 8.456 19.014 1.00 17.93 ? 495 ASN B O 1 ATOM 8181 C CB . ASN B 1 495 ? 27.779 8.414 21.724 1.00 19.53 ? 495 ASN B CB 1 ATOM 8182 C CG . ASN B 1 495 ? 28.296 6.982 21.700 1.00 20.26 ? 495 ASN B CG 1 ATOM 8183 O OD1 . ASN B 1 495 ? 29.363 6.693 21.157 1.00 20.00 ? 495 ASN B OD1 1 ATOM 8184 N ND2 . ASN B 1 495 ? 27.535 6.077 22.302 1.00 20.88 ? 495 ASN B ND2 1 ATOM 8185 N N . PRO B 1 496 ? 29.041 9.208 18.292 1.00 18.46 ? 496 PRO B N 1 ATOM 8186 C CA . PRO B 1 496 ? 28.854 8.911 16.866 1.00 18.06 ? 496 PRO B CA 1 ATOM 8187 C C . PRO B 1 496 ? 28.486 7.459 16.562 1.00 18.34 ? 496 PRO B C 1 ATOM 8188 O O . PRO B 1 496 ? 29.209 6.527 16.947 1.00 19.41 ? 496 PRO B O 1 ATOM 8189 C CB . PRO B 1 496 ? 30.214 9.250 16.277 1.00 19.21 ? 496 PRO B CB 1 ATOM 8190 C CG . PRO B 1 496 ? 30.647 10.374 17.102 1.00 18.94 ? 496 PRO B CG 1 ATOM 8191 C CD . PRO B 1 496 ? 30.317 9.923 18.485 1.00 19.18 ? 496 PRO B CD 1 ATOM 8192 N N . GLY B 1 497 ? 27.342 7.283 15.903 1.00 16.05 ? 497 GLY B N 1 ATOM 8193 C CA . GLY B 1 497 ? 26.885 5.954 15.557 1.00 14.55 ? 497 GLY B CA 1 ATOM 8194 C C . GLY B 1 497 ? 25.458 5.860 15.089 1.00 14.86 ? 497 GLY B C 1 ATOM 8195 O O . GLY B 1 497 ? 24.738 6.857 15.071 1.00 17.26 ? 497 GLY B O 1 ATOM 8196 N N . ALA B 1 498 ? 25.061 4.659 14.673 1.00 13.82 ? 498 ALA B N 1 ATOM 8197 C CA . ALA B 1 498 ? 23.692 4.399 14.228 1.00 12.87 ? 498 ALA B CA 1 ATOM 8198 C C . ALA B 1 498 ? 22.954 3.842 15.440 1.00 10.43 ? 498 ALA B C 1 ATOM 8199 O O . ALA B 1 498 ? 23.268 2.752 15.913 1.00 11.83 ? 498 ALA B O 1 ATOM 8200 C CB . ALA B 1 498 ? 23.681 3.405 13.072 1.00 12.74 ? 498 ALA B CB 1 ATOM 8201 N N . TRP B 1 499 ? 22.015 4.622 15.967 1.00 9.69 ? 499 TRP B N 1 ATOM 8202 C CA . TRP B 1 499 ? 21.259 4.230 17.161 1.00 10.00 ? 499 TRP B CA 1 ATOM 8203 C C . TRP B 1 499 ? 19.763 4.128 16.970 1.00 8.65 ? 499 TRP B C 1 ATOM 8204 O O . TRP B 1 499 ? 19.130 5.072 16.509 1.00 11.23 ? 499 TRP B O 1 ATOM 8205 C CB . TRP B 1 499 ? 21.533 5.202 18.319 1.00 8.27 ? 499 TRP B CB 1 ATOM 8206 C CG . TRP B 1 499 ? 22.976 5.491 18.550 1.00 7.61 ? 499 TRP B CG 1 ATOM 8207 C CD1 . TRP B 1 499 ? 23.649 6.623 18.175 1.00 7.92 ? 499 TRP B CD1 1 ATOM 8208 C CD2 . TRP B 1 499 ? 23.946 4.626 19.153 1.00 6.49 ? 499 TRP B CD2 1 ATOM 8209 N NE1 . TRP B 1 499 ? 24.985 6.515 18.498 1.00 7.33 ? 499 TRP B NE1 1 ATOM 8210 C CE2 . TRP B 1 499 ? 25.199 5.303 19.100 1.00 5.85 ? 499 TRP B CE2 1 ATOM 8211 C CE3 . TRP B 1 499 ? 23.890 3.344 19.741 1.00 4.66 ? 499 TRP B CE3 1 ATOM 8212 C CZ2 . TRP B 1 499 ? 26.391 4.738 19.615 1.00 5.62 ? 499 TRP B CZ2 1 ATOM 8213 C CZ3 . TRP B 1 499 ? 25.089 2.777 20.265 1.00 3.54 ? 499 TRP B CZ3 1 ATOM 8214 C CH2 . TRP B 1 499 ? 26.315 3.483 20.194 1.00 1.42 ? 499 TRP B CH2 1 ATOM 8215 N N . LEU B 1 500 ? 19.192 2.997 17.375 1.00 8.39 ? 500 LEU B N 1 ATOM 8216 C CA . LEU B 1 500 ? 17.750 2.800 17.265 1.00 7.92 ? 500 LEU B CA 1 ATOM 8217 C C . LEU B 1 500 ? 17.005 3.535 18.372 1.00 8.97 ? 500 LEU B C 1 ATOM 8218 O O . LEU B 1 500 ? 17.499 3.685 19.496 1.00 10.84 ? 500 LEU B O 1 ATOM 8219 C CB . LEU B 1 500 ? 17.365 1.309 17.284 1.00 8.30 ? 500 LEU B CB 1 ATOM 8220 C CG . LEU B 1 500 ? 17.653 0.389 16.090 1.00 9.84 ? 500 LEU B CG 1 ATOM 8221 C CD1 . LEU B 1 500 ? 17.124 -0.975 16.393 1.00 11.35 ? 500 LEU B CD1 1 ATOM 8222 C CD2 . LEU B 1 500 ? 17.003 0.889 14.814 1.00 10.66 ? 500 LEU B CD2 1 ATOM 8223 N N . PHE B 1 501 ? 15.854 4.071 17.994 1.00 8.41 ? 501 PHE B N 1 ATOM 8224 C CA . PHE B 1 501 ? 14.971 4.784 18.888 1.00 8.75 ? 501 PHE B CA 1 ATOM 8225 C C . PHE B 1 501 ? 13.667 4.111 18.563 1.00 9.89 ? 501 PHE B C 1 ATOM 8226 O O . PHE B 1 501 ? 13.133 4.248 17.461 1.00 10.35 ? 501 PHE B O 1 ATOM 8227 C CB . PHE B 1 501 ? 14.947 6.283 18.585 1.00 7.18 ? 501 PHE B CB 1 ATOM 8228 C CG . PHE B 1 501 ? 14.009 7.070 19.458 1.00 8.36 ? 501 PHE B CG 1 ATOM 8229 C CD1 . PHE B 1 501 ? 14.203 7.131 20.854 1.00 7.94 ? 501 PHE B CD1 1 ATOM 8230 C CD2 . PHE B 1 501 ? 12.896 7.727 18.895 1.00 6.91 ? 501 PHE B CD2 1 ATOM 8231 C CE1 . PHE B 1 501 ? 13.301 7.829 21.687 1.00 8.06 ? 501 PHE B CE1 1 ATOM 8232 C CE2 . PHE B 1 501 ? 11.983 8.431 19.708 1.00 6.90 ? 501 PHE B CE2 1 ATOM 8233 C CZ . PHE B 1 501 ? 12.181 8.484 21.112 1.00 7.00 ? 501 PHE B CZ 1 ATOM 8234 N N . HIS B 1 502 ? 13.178 3.348 19.531 1.00 11.59 ? 502 HIS B N 1 ATOM 8235 C CA . HIS B 1 502 ? 11.981 2.573 19.321 1.00 11.06 ? 502 HIS B CA 1 ATOM 8236 C C . HIS B 1 502 ? 11.155 2.286 20.540 1.00 10.62 ? 502 HIS B C 1 ATOM 8237 O O . HIS B 1 502 ? 11.607 2.428 21.674 1.00 13.26 ? 502 HIS B O 1 ATOM 8238 C CB . HIS B 1 502 ? 12.361 1.230 18.677 1.00 10.82 ? 502 HIS B CB 1 ATOM 8239 C CG . HIS B 1 502 ? 13.155 0.316 19.557 1.00 12.13 ? 502 HIS B CG 1 ATOM 8240 N ND1 . HIS B 1 502 ? 12.576 -0.721 20.257 1.00 13.56 ? 502 HIS B ND1 1 ATOM 8241 C CD2 . HIS B 1 502 ? 14.479 0.263 19.829 1.00 11.96 ? 502 HIS B CD2 1 ATOM 8242 C CE1 . HIS B 1 502 ? 13.511 -1.377 20.920 1.00 14.04 ? 502 HIS B CE1 1 ATOM 8243 N NE2 . HIS B 1 502 ? 14.674 -0.799 20.677 1.00 12.39 ? 502 HIS B NE2 1 ATOM 8244 N N . CYS B 1 503 ? 9.961 1.782 20.259 1.00 8.12 ? 503 CYS B N 1 ATOM 8245 C CA . CYS B 1 503 ? 9.026 1.357 21.268 1.00 8.08 ? 503 CYS B CA 1 ATOM 8246 C C . CYS B 1 503 ? 9.561 0.003 21.690 1.00 7.73 ? 503 CYS B C 1 ATOM 8247 O O . CYS B 1 503 ? 9.928 -0.821 20.829 1.00 4.69 ? 503 CYS B O 1 ATOM 8248 C CB . CYS B 1 503 ? 7.643 1.181 20.668 1.00 8.53 ? 503 CYS B CB 1 ATOM 8249 S SG . CYS B 1 503 ? 6.504 0.466 21.815 1.00 14.21 ? 503 CYS B SG 1 ATOM 8250 N N . HIS B 1 504 ? 9.602 -0.224 23.002 1.00 5.00 ? 504 HIS B N 1 ATOM 8251 C CA . HIS B 1 504 ? 10.118 -1.473 23.508 1.00 4.22 ? 504 HIS B CA 1 ATOM 8252 C C . HIS B 1 504 ? 9.118 -2.615 23.623 1.00 4.36 ? 504 HIS B C 1 ATOM 8253 O O . HIS B 1 504 ? 9.462 -3.694 24.114 1.00 6.94 ? 504 HIS B O 1 ATOM 8254 C CB . HIS B 1 504 ? 10.920 -1.269 24.786 1.00 7.21 ? 504 HIS B CB 1 ATOM 8255 C CG . HIS B 1 504 ? 12.122 -2.152 24.870 1.00 6.75 ? 504 HIS B CG 1 ATOM 8256 N ND1 . HIS B 1 504 ? 12.042 -3.526 24.796 1.00 7.78 ? 504 HIS B ND1 1 ATOM 8257 C CD2 . HIS B 1 504 ? 13.433 -1.861 25.011 1.00 8.91 ? 504 HIS B CD2 1 ATOM 8258 C CE1 . HIS B 1 504 ? 13.251 -4.043 24.891 1.00 7.10 ? 504 HIS B CE1 1 ATOM 8259 N NE2 . HIS B 1 504 ? 14.113 -3.054 25.024 1.00 11.24 ? 504 HIS B NE2 1 ATOM 8260 N N . ILE B 1 505 ? 7.874 -2.382 23.204 1.00 3.47 ? 505 ILE B N 1 ATOM 8261 C CA . ILE B 1 505 ? 6.894 -3.471 23.165 1.00 4.32 ? 505 ILE B CA 1 ATOM 8262 C C . ILE B 1 505 ? 7.327 -4.230 21.904 1.00 5.79 ? 505 ILE B C 1 ATOM 8263 O O . ILE B 1 505 ? 7.377 -3.663 20.796 1.00 5.67 ? 505 ILE B O 1 ATOM 8264 C CB . ILE B 1 505 ? 5.400 -2.993 23.045 1.00 4.66 ? 505 ILE B CB 1 ATOM 8265 C CG1 . ILE B 1 505 ? 4.889 -2.487 24.399 1.00 3.37 ? 505 ILE B CG1 1 ATOM 8266 C CG2 . ILE B 1 505 ? 4.489 -4.161 22.586 1.00 1.67 ? 505 ILE B CG2 1 ATOM 8267 C CD1 . ILE B 1 505 ? 3.607 -1.643 24.331 1.00 3.11 ? 505 ILE B CD1 1 ATOM 8268 N N . ALA B 1 506 ? 7.736 -5.477 22.123 1.00 6.47 ? 506 ALA B N 1 ATOM 8269 C CA . ALA B 1 506 ? 8.219 -6.379 21.083 1.00 7.84 ? 506 ALA B CA 1 ATOM 8270 C C . ALA B 1 506 ? 7.347 -6.468 19.836 1.00 8.85 ? 506 ALA B C 1 ATOM 8271 O O . ALA B 1 506 ? 7.862 -6.461 18.722 1.00 9.12 ? 506 ALA B O 1 ATOM 8272 C CB . ALA B 1 506 ? 8.461 -7.757 21.667 1.00 5.96 ? 506 ALA B CB 1 ATOM 8273 N N . TRP B 1 507 ? 6.030 -6.415 20.038 1.00 12.32 ? 507 TRP B N 1 ATOM 8274 C CA . TRP B 1 507 ? 5.054 -6.510 18.950 1.00 13.95 ? 507 TRP B CA 1 ATOM 8275 C C . TRP B 1 507 ? 4.978 -5.251 18.113 1.00 13.38 ? 507 TRP B C 1 ATOM 8276 O O . TRP B 1 507 ? 4.804 -5.313 16.895 1.00 14.52 ? 507 TRP B O 1 ATOM 8277 C CB . TRP B 1 507 ? 3.662 -6.852 19.495 1.00 15.48 ? 507 TRP B CB 1 ATOM 8278 C CG . TRP B 1 507 ? 3.589 -7.770 20.726 1.00 16.65 ? 507 TRP B CG 1 ATOM 8279 C CD1 . TRP B 1 507 ? 2.824 -7.549 21.836 1.00 17.41 ? 507 TRP B CD1 1 ATOM 8280 C CD2 . TRP B 1 507 ? 4.329 -8.984 20.992 1.00 16.08 ? 507 TRP B CD2 1 ATOM 8281 N NE1 . TRP B 1 507 ? 3.042 -8.521 22.777 1.00 16.64 ? 507 TRP B NE1 1 ATOM 8282 C CE2 . TRP B 1 507 ? 3.962 -9.413 22.296 1.00 17.85 ? 507 TRP B CE2 1 ATOM 8283 C CE3 . TRP B 1 507 ? 5.276 -9.745 20.267 1.00 17.84 ? 507 TRP B CE3 1 ATOM 8284 C CZ2 . TRP B 1 507 ? 4.511 -10.570 22.899 1.00 17.78 ? 507 TRP B CZ2 1 ATOM 8285 C CZ3 . TRP B 1 507 ? 5.827 -10.895 20.864 1.00 17.27 ? 507 TRP B CZ3 1 ATOM 8286 C CH2 . TRP B 1 507 ? 5.439 -11.292 22.174 1.00 19.15 ? 507 TRP B CH2 1 ATOM 8287 N N . HIS B 1 508 ? 5.162 -4.116 18.779 1.00 14.03 ? 508 HIS B N 1 ATOM 8288 C CA . HIS B 1 508 ? 5.126 -2.811 18.136 1.00 13.57 ? 508 HIS B CA 1 ATOM 8289 C C . HIS B 1 508 ? 6.398 -2.521 17.327 1.00 12.75 ? 508 HIS B C 1 ATOM 8290 O O . HIS B 1 508 ? 6.312 -1.992 16.211 1.00 11.76 ? 508 HIS B O 1 ATOM 8291 C CB . HIS B 1 508 ? 4.862 -1.716 19.178 1.00 15.66 ? 508 HIS B CB 1 ATOM 8292 C CG . HIS B 1 508 ? 3.482 -1.748 19.772 1.00 13.63 ? 508 HIS B CG 1 ATOM 8293 N ND1 . HIS B 1 508 ? 3.102 -0.920 20.806 1.00 12.93 ? 508 HIS B ND1 1 ATOM 8294 C CD2 . HIS B 1 508 ? 2.389 -2.488 19.470 1.00 14.54 ? 508 HIS B CD2 1 ATOM 8295 C CE1 . HIS B 1 508 ? 1.839 -1.145 21.113 1.00 12.46 ? 508 HIS B CE1 1 ATOM 8296 N NE2 . HIS B 1 508 ? 1.383 -2.092 20.317 1.00 14.57 ? 508 HIS B NE2 1 ATOM 8297 N N . VAL B 1 509 ? 7.559 -2.928 17.854 1.00 11.15 ? 509 VAL B N 1 ATOM 8298 C CA . VAL B 1 509 ? 8.835 -2.728 17.157 1.00 10.69 ? 509 VAL B CA 1 ATOM 8299 C C . VAL B 1 509 ? 8.940 -3.699 15.969 1.00 10.37 ? 509 VAL B C 1 ATOM 8300 O O . VAL B 1 509 ? 9.645 -3.430 14.998 1.00 10.63 ? 509 VAL B O 1 ATOM 8301 C CB . VAL B 1 509 ? 10.081 -2.819 18.112 1.00 10.85 ? 509 VAL B CB 1 ATOM 8302 C CG1 . VAL B 1 509 ? 10.318 -4.234 18.621 1.00 6.07 ? 509 VAL B CG1 1 ATOM 8303 C CG2 . VAL B 1 509 ? 11.329 -2.273 17.415 1.00 10.96 ? 509 VAL B CG2 1 ATOM 8304 N N . SER B 1 510 ? 8.216 -4.812 16.072 1.00 10.28 ? 510 SER B N 1 ATOM 8305 C CA . SER B 1 510 ? 8.145 -5.814 15.020 1.00 12.06 ? 510 SER B CA 1 ATOM 8306 C C . SER B 1 510 ? 7.241 -5.273 13.919 1.00 13.29 ? 510 SER B C 1 ATOM 8307 O O . SER B 1 510 ? 7.497 -5.494 12.730 1.00 13.46 ? 510 SER B O 1 ATOM 8308 C CB . SER B 1 510 ? 7.563 -7.109 15.561 1.00 11.81 ? 510 SER B CB 1 ATOM 8309 O OG . SER B 1 510 ? 8.518 -7.777 16.347 1.00 14.50 ? 510 SER B OG 1 ATOM 8310 N N . GLY B 1 511 ? 6.204 -4.543 14.347 1.00 13.91 ? 511 GLY B N 1 ATOM 8311 C CA . GLY B 1 511 ? 5.254 -3.913 13.439 1.00 16.18 ? 511 GLY B CA 1 ATOM 8312 C C . GLY B 1 511 ? 5.839 -2.714 12.694 1.00 15.91 ? 511 GLY B C 1 ATOM 8313 O O . GLY B 1 511 ? 5.270 -2.273 11.689 1.00 15.92 ? 511 GLY B O 1 ATOM 8314 N N . GLY B 1 512 ? 6.943 -2.168 13.217 1.00 14.44 ? 512 GLY B N 1 ATOM 8315 C CA . GLY B 1 512 ? 7.617 -1.051 12.578 1.00 12.99 ? 512 GLY B CA 1 ATOM 8316 C C . GLY B 1 512 ? 7.917 0.213 13.367 1.00 13.29 ? 512 GLY B C 1 ATOM 8317 O O . GLY B 1 512 ? 8.527 1.132 12.801 1.00 12.47 ? 512 GLY B O 1 ATOM 8318 N N . LEU B 1 513 ? 7.544 0.256 14.653 1.00 12.38 ? 513 LEU B N 1 ATOM 8319 C CA . LEU B 1 513 ? 7.754 1.433 15.508 1.00 12.18 ? 513 LEU B CA 1 ATOM 8320 C C . LEU B 1 513 ? 9.200 1.702 15.905 1.00 12.60 ? 513 LEU B C 1 ATOM 8321 O O . LEU B 1 513 ? 9.600 1.504 17.063 1.00 13.50 ? 513 LEU B O 1 ATOM 8322 C CB . LEU B 1 513 ? 6.859 1.388 16.757 1.00 12.07 ? 513 LEU B CB 1 ATOM 8323 C CG . LEU B 1 513 ? 6.108 2.677 17.142 1.00 12.76 ? 513 LEU B CG 1 ATOM 8324 C CD1 . LEU B 1 513 ? 4.988 2.302 18.081 1.00 13.99 ? 513 LEU B CD1 1 ATOM 8325 C CD2 . LEU B 1 513 ? 6.999 3.756 17.769 1.00 9.52 ? 513 LEU B CD2 1 ATOM 8326 N N . SER B 1 514 ? 9.943 2.252 14.950 1.00 11.12 ? 514 SER B N 1 ATOM 8327 C CA . SER B 1 514 ? 11.335 2.573 15.148 1.00 11.12 ? 514 SER B CA 1 ATOM 8328 C C . SER B 1 514 ? 11.896 3.519 14.113 1.00 12.38 ? 514 SER B C 1 ATOM 8329 O O . SER B 1 514 ? 11.329 3.711 13.036 1.00 12.37 ? 514 SER B O 1 ATOM 8330 C CB . SER B 1 514 ? 12.173 1.287 15.150 1.00 11.68 ? 514 SER B CB 1 ATOM 8331 O OG . SER B 1 514 ? 13.515 1.519 15.536 1.00 13.50 ? 514 SER B OG 1 ATOM 8332 N N . VAL B 1 515 ? 12.971 4.181 14.524 1.00 12.98 ? 515 VAL B N 1 ATOM 8333 C CA . VAL B 1 515 ? 13.751 5.074 13.680 1.00 14.46 ? 515 VAL B CA 1 ATOM 8334 C C . VAL B 1 515 ? 15.184 4.728 14.014 1.00 14.82 ? 515 VAL B C 1 ATOM 8335 O O . VAL B 1 515 ? 15.445 3.984 14.970 1.00 13.12 ? 515 VAL B O 1 ATOM 8336 C CB . VAL B 1 515 ? 13.504 6.602 13.896 1.00 15.44 ? 515 VAL B CB 1 ATOM 8337 C CG1 . VAL B 1 515 ? 12.238 7.033 13.205 1.00 13.59 ? 515 VAL B CG1 1 ATOM 8338 C CG2 . VAL B 1 515 ? 13.473 6.966 15.358 1.00 16.09 ? 515 VAL B CG2 1 ATOM 8339 N N . ASP B 1 516 ? 16.098 5.234 13.196 1.00 14.64 ? 516 ASP B N 1 ATOM 8340 C CA . ASP B 1 516 ? 17.516 4.993 13.369 1.00 15.26 ? 516 ASP B CA 1 ATOM 8341 C C . ASP B 1 516 ? 18.200 6.352 13.331 1.00 16.17 ? 516 ASP B C 1 ATOM 8342 O O . ASP B 1 516 ? 18.259 6.999 12.286 1.00 18.30 ? 516 ASP B O 1 ATOM 8343 C CB . ASP B 1 516 ? 18.027 4.060 12.244 1.00 13.24 ? 516 ASP B CB 1 ATOM 8344 C CG . ASP B 1 516 ? 19.500 3.655 12.393 1.00 9.70 ? 516 ASP B CG 1 ATOM 8345 O OD1 . ASP B 1 516 ? 20.288 4.366 13.053 1.00 13.86 ? 516 ASP B OD1 1 ATOM 8346 O OD2 . ASP B 1 516 ? 19.884 2.622 11.801 1.00 8.24 ? 516 ASP B OD2 1 ATOM 8347 N N . PHE B 1 517 ? 18.684 6.785 14.491 1.00 16.20 ? 517 PHE B N 1 ATOM 8348 C CA . PHE B 1 517 ? 19.410 8.041 14.604 1.00 16.55 ? 517 PHE B CA 1 ATOM 8349 C C . PHE B 1 517 ? 20.855 7.831 14.149 1.00 16.47 ? 517 PHE B C 1 ATOM 8350 O O . PHE B 1 517 ? 21.658 7.248 14.884 1.00 17.74 ? 517 PHE B O 1 ATOM 8351 C CB . PHE B 1 517 ? 19.419 8.560 16.052 1.00 14.73 ? 517 PHE B CB 1 ATOM 8352 C CG . PHE B 1 517 ? 18.175 9.307 16.456 1.00 14.98 ? 517 PHE B CG 1 ATOM 8353 C CD1 . PHE B 1 517 ? 17.748 10.440 15.744 1.00 13.56 ? 517 PHE B CD1 1 ATOM 8354 C CD2 . PHE B 1 517 ? 17.444 8.903 17.579 1.00 13.71 ? 517 PHE B CD2 1 ATOM 8355 C CE1 . PHE B 1 517 ? 16.604 11.162 16.146 1.00 13.77 ? 517 PHE B CE1 1 ATOM 8356 C CE2 . PHE B 1 517 ? 16.286 9.625 18.002 1.00 13.97 ? 517 PHE B CE2 1 ATOM 8357 C CZ . PHE B 1 517 ? 15.868 10.753 17.283 1.00 13.61 ? 517 PHE B CZ 1 ATOM 8358 N N . LEU B 1 518 ? 21.166 8.238 12.919 1.00 14.90 ? 518 LEU B N 1 ATOM 8359 C CA . LEU B 1 518 ? 22.533 8.133 12.426 1.00 16.34 ? 518 LEU B CA 1 ATOM 8360 C C . LEU B 1 518 ? 23.277 9.395 12.874 1.00 18.94 ? 518 LEU B C 1 ATOM 8361 O O . LEU B 1 518 ? 23.355 10.413 12.168 1.00 19.06 ? 518 LEU B O 1 ATOM 8362 C CB . LEU B 1 518 ? 22.583 7.942 10.913 1.00 13.12 ? 518 LEU B CB 1 ATOM 8363 C CG . LEU B 1 518 ? 23.973 7.694 10.324 1.00 10.07 ? 518 LEU B CG 1 ATOM 8364 C CD1 . LEU B 1 518 ? 24.603 6.411 10.831 1.00 11.06 ? 518 LEU B CD1 1 ATOM 8365 C CD2 . LEU B 1 518 ? 23.855 7.661 8.843 1.00 6.76 ? 518 LEU B CD2 1 ATOM 8366 N N . GLU B 1 519 ? 23.772 9.306 14.100 1.00 20.71 ? 519 GLU B N 1 ATOM 8367 C CA . GLU B 1 519 ? 24.491 10.374 14.766 1.00 23.93 ? 519 GLU B CA 1 ATOM 8368 C C . GLU B 1 519 ? 25.926 10.519 14.279 1.00 25.60 ? 519 GLU B C 1 ATOM 8369 O O . GLU B 1 519 ? 26.691 9.545 14.285 1.00 26.93 ? 519 GLU B O 1 ATOM 8370 C CB . GLU B 1 519 ? 24.468 10.092 16.260 1.00 24.67 ? 519 GLU B CB 1 ATOM 8371 C CG . GLU B 1 519 ? 25.136 11.114 17.137 1.00 23.77 ? 519 GLU B CG 1 ATOM 8372 C CD . GLU B 1 519 ? 24.963 10.784 18.597 1.00 24.60 ? 519 GLU B CD 1 ATOM 8373 O OE1 . GLU B 1 519 ? 23.918 10.199 18.966 1.00 22.24 ? 519 GLU B OE1 1 ATOM 8374 O OE2 . GLU B 1 519 ? 25.878 11.113 19.379 1.00 22.60 ? 519 GLU B OE2 1 ATOM 8375 N N . ARG B 1 520 ? 26.260 11.746 13.858 1.00 26.12 ? 520 ARG B N 1 ATOM 8376 C CA . ARG B 1 520 ? 27.587 12.143 13.356 1.00 26.74 ? 520 ARG B CA 1 ATOM 8377 C C . ARG B 1 520 ? 28.269 11.090 12.449 1.00 27.66 ? 520 ARG B C 1 ATOM 8378 O O . ARG B 1 520 ? 29.325 10.551 12.806 1.00 29.08 ? 520 ARG B O 1 ATOM 8379 C CB . ARG B 1 520 ? 28.486 12.522 14.543 1.00 25.89 ? 520 ARG B CB 1 ATOM 8380 C CG . ARG B 1 520 ? 28.033 13.751 15.321 1.00 25.11 ? 520 ARG B CG 1 ATOM 8381 C CD . ARG B 1 520 ? 28.668 13.827 16.716 1.00 24.74 ? 520 ARG B CD 1 ATOM 8382 N NE . ARG B 1 520 ? 30.132 13.821 16.667 1.00 25.22 ? 520 ARG B NE 1 ATOM 8383 C CZ . ARG B 1 520 ? 30.940 14.034 17.702 1.00 22.55 ? 520 ARG B CZ 1 ATOM 8384 N NH1 . ARG B 1 520 ? 30.456 14.292 18.910 1.00 21.77 ? 520 ARG B NH1 1 ATOM 8385 N NH2 . ARG B 1 520 ? 32.246 13.926 17.533 1.00 23.17 ? 520 ARG B NH2 1 ATOM 8386 N N . PRO B 1 521 ? 27.655 10.764 11.281 1.00 28.43 ? 521 PRO B N 1 ATOM 8387 C CA . PRO B 1 521 ? 28.210 9.768 10.352 1.00 29.43 ? 521 PRO B CA 1 ATOM 8388 C C . PRO B 1 521 ? 29.622 10.039 9.854 1.00 30.53 ? 521 PRO B C 1 ATOM 8389 O O . PRO B 1 521 ? 30.433 9.115 9.751 1.00 31.40 ? 521 PRO B O 1 ATOM 8390 C CB . PRO B 1 521 ? 27.196 9.762 9.209 1.00 29.93 ? 521 PRO B CB 1 ATOM 8391 C CG . PRO B 1 521 ? 26.625 11.132 9.241 1.00 29.01 ? 521 PRO B CG 1 ATOM 8392 C CD . PRO B 1 521 ? 26.429 11.353 10.704 1.00 28.16 ? 521 PRO B CD 1 ATOM 8393 N N . ALA B 1 522 ? 29.915 11.319 9.621 1.00 31.38 ? 522 ALA B N 1 ATOM 8394 C CA . ALA B 1 522 ? 31.221 11.775 9.152 1.00 31.83 ? 522 ALA B CA 1 ATOM 8395 C C . ALA B 1 522 ? 32.326 11.529 10.177 1.00 32.61 ? 522 ALA B C 1 ATOM 8396 O O . ALA B 1 522 ? 33.483 11.372 9.803 1.00 34.75 ? 522 ALA B O 1 ATOM 8397 C CB . ALA B 1 522 ? 31.157 13.245 8.801 1.00 32.65 ? 522 ALA B CB 1 ATOM 8398 N N . ASP B 1 523 ? 31.951 11.475 11.458 1.00 32.71 ? 523 ASP B N 1 ATOM 8399 C CA . ASP B 1 523 ? 32.884 11.238 12.567 1.00 32.88 ? 523 ASP B CA 1 ATOM 8400 C C . ASP B 1 523 ? 33.017 9.750 12.882 1.00 32.80 ? 523 ASP B C 1 ATOM 8401 O O . ASP B 1 523 ? 34.067 9.296 13.346 1.00 31.73 ? 523 ASP B O 1 ATOM 8402 C CB . ASP B 1 523 ? 32.412 11.954 13.846 1.00 32.91 ? 523 ASP B CB 1 ATOM 8403 C CG . ASP B 1 523 ? 32.563 13.467 13.782 1.00 33.71 ? 523 ASP B CG 1 ATOM 8404 O OD1 . ASP B 1 523 ? 33.696 13.965 13.964 1.00 35.02 ? 523 ASP B OD1 1 ATOM 8405 O OD2 . ASP B 1 523 ? 31.541 14.159 13.589 1.00 32.59 ? 523 ASP B OD2 1 ATOM 8406 N N . LEU B 1 524 ? 31.943 9.007 12.607 1.00 33.14 ? 524 LEU B N 1 ATOM 8407 C CA . LEU B 1 524 ? 31.840 7.568 12.872 1.00 32.27 ? 524 LEU B CA 1 ATOM 8408 C C . LEU B 1 524 ? 32.844 6.641 12.194 1.00 30.90 ? 524 LEU B C 1 ATOM 8409 O O . LEU B 1 524 ? 33.397 5.768 12.851 1.00 29.79 ? 524 LEU B O 1 ATOM 8410 C CB . LEU B 1 524 ? 30.402 7.109 12.591 1.00 34.05 ? 524 LEU B CB 1 ATOM 8411 C CG . LEU B 1 524 ? 29.945 5.648 12.642 1.00 34.95 ? 524 LEU B CG 1 ATOM 8412 C CD1 . LEU B 1 524 ? 30.143 5.041 14.020 1.00 36.13 ? 524 LEU B CD1 1 ATOM 8413 C CD2 . LEU B 1 524 ? 28.496 5.580 12.213 1.00 36.06 ? 524 LEU B CD2 1 ATOM 8414 N N . ARG B 1 525 ? 33.086 6.854 10.902 1.00 31.21 ? 525 ARG B N 1 ATOM 8415 C CA . ARG B 1 525 ? 34.007 6.040 10.098 1.00 32.13 ? 525 ARG B CA 1 ATOM 8416 C C . ARG B 1 525 ? 35.438 5.925 10.645 1.00 33.76 ? 525 ARG B C 1 ATOM 8417 O O . ARG B 1 525 ? 35.986 4.817 10.711 1.00 32.79 ? 525 ARG B O 1 ATOM 8418 C CB . ARG B 1 525 ? 34.030 6.573 8.662 1.00 31.43 ? 525 ARG B CB 1 ATOM 8419 C CG . ARG B 1 525 ? 34.629 5.648 7.616 1.00 31.97 ? 525 ARG B CG 1 ATOM 8420 C CD . ARG B 1 525 ? 34.480 6.277 6.251 1.00 34.63 ? 525 ARG B CD 1 ATOM 8421 N NE . ARG B 1 525 ? 34.911 5.395 5.168 1.00 38.21 ? 525 ARG B NE 1 ATOM 8422 C CZ . ARG B 1 525 ? 34.599 5.568 3.883 1.00 40.70 ? 525 ARG B CZ 1 ATOM 8423 N NH1 . ARG B 1 525 ? 33.839 6.592 3.497 1.00 40.19 ? 525 ARG B NH1 1 ATOM 8424 N NH2 . ARG B 1 525 ? 35.072 4.728 2.969 1.00 41.75 ? 525 ARG B NH2 1 ATOM 8425 N N . GLN B 1 526 ? 35.998 7.052 11.095 1.00 35.92 ? 526 GLN B N 1 ATOM 8426 C CA . GLN B 1 526 ? 37.367 7.117 11.636 1.00 38.50 ? 526 GLN B CA 1 ATOM 8427 C C . GLN B 1 526 ? 37.521 6.473 13.009 1.00 37.57 ? 526 GLN B C 1 ATOM 8428 O O . GLN B 1 526 ? 38.606 5.992 13.356 1.00 38.42 ? 526 GLN B O 1 ATOM 8429 C CB . GLN B 1 526 ? 37.860 8.568 11.746 1.00 41.39 ? 526 GLN B CB 1 ATOM 8430 C CG . GLN B 1 526 ? 37.693 9.425 10.508 1.00 45.54 ? 526 GLN B CG 1 ATOM 8431 C CD . GLN B 1 526 ? 36.373 10.173 10.504 1.00 49.36 ? 526 GLN B CD 1 ATOM 8432 O OE1 . GLN B 1 526 ? 35.326 9.609 10.157 1.00 49.81 ? 526 GLN B OE1 1 ATOM 8433 N NE2 . GLN B 1 526 ? 36.408 11.446 10.907 1.00 49.37 ? 526 GLN B NE2 1 ATOM 8434 N N . ARG B 1 527 ? 36.428 6.465 13.770 1.00 35.80 ? 527 ARG B N 1 ATOM 8435 C CA . ARG B 1 527 ? 36.408 5.917 15.125 1.00 34.47 ? 527 ARG B CA 1 ATOM 8436 C C . ARG B 1 527 ? 36.279 4.398 15.215 1.00 32.78 ? 527 ARG B C 1 ATOM 8437 O O . ARG B 1 527 ? 36.506 3.818 16.287 1.00 33.10 ? 527 ARG B O 1 ATOM 8438 C CB . ARG B 1 527 ? 35.314 6.601 15.945 1.00 35.17 ? 527 ARG B CB 1 ATOM 8439 C CG . ARG B 1 527 ? 35.528 8.093 16.094 1.00 35.91 ? 527 ARG B CG 1 ATOM 8440 C CD . ARG B 1 527 ? 34.329 8.757 16.717 1.00 37.55 ? 527 ARG B CD 1 ATOM 8441 N NE . ARG B 1 527 ? 34.465 10.211 16.737 1.00 39.64 ? 527 ARG B NE 1 ATOM 8442 C CZ . ARG B 1 527 ? 34.712 10.937 17.826 1.00 41.63 ? 527 ARG B CZ 1 ATOM 8443 N NH1 . ARG B 1 527 ? 34.857 10.355 19.014 1.00 41.70 ? 527 ARG B NH1 1 ATOM 8444 N NH2 . ARG B 1 527 ? 34.824 12.254 17.720 1.00 41.51 ? 527 ARG B NH2 1 ATOM 8445 N N . ILE B 1 528 ? 35.940 3.761 14.090 1.00 29.72 ? 528 ILE B N 1 ATOM 8446 C CA . ILE B 1 528 ? 35.792 2.303 14.025 1.00 26.69 ? 528 ILE B CA 1 ATOM 8447 C C . ILE B 1 528 ? 37.158 1.645 13.788 1.00 25.17 ? 528 ILE B C 1 ATOM 8448 O O . ILE B 1 528 ? 37.784 1.833 12.737 1.00 24.87 ? 528 ILE B O 1 ATOM 8449 C CB . ILE B 1 528 ? 34.787 1.856 12.912 1.00 25.48 ? 528 ILE B CB 1 ATOM 8450 C CG1 . ILE B 1 528 ? 33.428 2.532 13.106 1.00 23.96 ? 528 ILE B CG1 1 ATOM 8451 C CG2 . ILE B 1 528 ? 34.576 0.334 12.962 1.00 24.78 ? 528 ILE B CG2 1 ATOM 8452 C CD1 . ILE B 1 528 ? 32.517 2.449 11.887 1.00 21.98 ? 528 ILE B CD1 1 ATOM 8453 N N . SER B 1 529 ? 37.587 0.860 14.776 1.00 23.25 ? 529 SER B N 1 ATOM 8454 C CA . SER B 1 529 ? 38.863 0.136 14.752 1.00 22.40 ? 529 SER B CA 1 ATOM 8455 C C . SER B 1 529 ? 38.879 -0.966 13.693 1.00 22.19 ? 529 SER B C 1 ATOM 8456 O O . SER B 1 529 ? 37.821 -1.439 13.271 1.00 23.23 ? 529 SER B O 1 ATOM 8457 C CB . SER B 1 529 ? 39.114 -0.492 16.118 1.00 20.70 ? 529 SER B CB 1 ATOM 8458 O OG . SER B 1 529 ? 38.081 -1.415 16.423 1.00 18.33 ? 529 SER B OG 1 ATOM 8459 N N . GLN B 1 530 ? 40.079 -1.400 13.306 1.00 22.29 ? 530 GLN B N 1 ATOM 8460 C CA . GLN B 1 530 ? 40.247 -2.454 12.305 1.00 22.16 ? 530 GLN B CA 1 ATOM 8461 C C . GLN B 1 530 ? 39.703 -3.788 12.839 1.00 22.36 ? 530 GLN B C 1 ATOM 8462 O O . GLN B 1 530 ? 39.099 -4.547 12.086 1.00 22.82 ? 530 GLN B O 1 ATOM 8463 C CB . GLN B 1 530 ? 41.723 -2.584 11.900 1.00 20.34 ? 530 GLN B CB 1 ATOM 8464 C CG . GLN B 1 530 ? 41.980 -3.352 10.596 1.00 23.29 ? 530 GLN B CG 1 ATOM 8465 C CD . GLN B 1 530 ? 41.715 -2.535 9.328 1.00 22.66 ? 530 GLN B CD 1 ATOM 8466 O OE1 . GLN B 1 530 ? 42.592 -1.827 8.847 1.00 22.79 ? 530 GLN B OE1 1 ATOM 8467 N NE2 . GLN B 1 530 ? 40.512 -2.661 8.772 1.00 23.85 ? 530 GLN B NE2 1 ATOM 8468 N N . GLU B 1 531 ? 39.826 -3.993 14.157 1.00 22.36 ? 531 GLU B N 1 ATOM 8469 C CA . GLU B 1 531 ? 39.359 -5.201 14.860 1.00 22.29 ? 531 GLU B CA 1 ATOM 8470 C C . GLU B 1 531 ? 37.839 -5.344 14.767 1.00 20.86 ? 531 GLU B C 1 ATOM 8471 O O . GLU B 1 531 ? 37.327 -6.430 14.483 1.00 20.32 ? 531 GLU B O 1 ATOM 8472 C CB . GLU B 1 531 ? 39.776 -5.180 16.345 1.00 24.43 ? 531 GLU B CB 1 ATOM 8473 C CG . GLU B 1 531 ? 41.291 -5.110 16.625 1.00 28.55 ? 531 GLU B CG 1 ATOM 8474 C CD . GLU B 1 531 ? 41.870 -3.698 16.494 1.00 31.16 ? 531 GLU B CD 1 ATOM 8475 O OE1 . GLU B 1 531 ? 41.650 -2.870 17.405 1.00 31.45 ? 531 GLU B OE1 1 ATOM 8476 O OE2 . GLU B 1 531 ? 42.537 -3.414 15.474 1.00 32.56 ? 531 GLU B OE2 1 ATOM 8477 N N . ASP B 1 532 ? 37.140 -4.223 14.954 1.00 20.29 ? 532 ASP B N 1 ATOM 8478 C CA . ASP B 1 532 ? 35.681 -4.169 14.885 1.00 18.45 ? 532 ASP B CA 1 ATOM 8479 C C . ASP B 1 532 ? 35.159 -4.286 13.460 1.00 18.52 ? 532 ASP B C 1 ATOM 8480 O O . ASP B 1 532 ? 34.168 -4.989 13.224 1.00 17.41 ? 532 ASP B O 1 ATOM 8481 C CB . ASP B 1 532 ? 35.152 -2.888 15.533 1.00 16.51 ? 532 ASP B CB 1 ATOM 8482 C CG . ASP B 1 532 ? 35.128 -2.956 17.055 1.00 16.01 ? 532 ASP B CG 1 ATOM 8483 O OD1 . ASP B 1 532 ? 35.324 -4.055 17.631 1.00 12.64 ? 532 ASP B OD1 1 ATOM 8484 O OD2 . ASP B 1 532 ? 34.897 -1.893 17.676 1.00 16.01 ? 532 ASP B OD2 1 ATOM 8485 N N . GLU B 1 533 ? 35.855 -3.635 12.522 1.00 17.95 ? 533 GLU B N 1 ATOM 8486 C CA . GLU B 1 533 ? 35.504 -3.654 11.095 1.00 20.46 ? 533 GLU B CA 1 ATOM 8487 C C . GLU B 1 533 ? 35.649 -5.064 10.504 1.00 20.07 ? 533 GLU B C 1 ATOM 8488 O O . GLU B 1 533 ? 34.720 -5.559 9.850 1.00 18.63 ? 533 GLU B O 1 ATOM 8489 C CB . GLU B 1 533 ? 36.374 -2.667 10.297 1.00 21.73 ? 533 GLU B CB 1 ATOM 8490 C CG . GLU B 1 533 ? 36.024 -2.599 8.794 1.00 25.24 ? 533 GLU B CG 1 ATOM 8491 C CD . GLU B 1 533 ? 36.957 -1.727 7.955 1.00 29.97 ? 533 GLU B CD 1 ATOM 8492 O OE1 . GLU B 1 533 ? 38.076 -1.373 8.413 1.00 29.66 ? 533 GLU B OE1 1 ATOM 8493 O OE2 . GLU B 1 533 ? 36.556 -1.411 6.809 1.00 30.15 ? 533 GLU B OE2 1 ATOM 8494 N N . ASP B 1 534 ? 36.803 -5.695 10.764 1.00 19.26 ? 534 ASP B N 1 ATOM 8495 C CA . ASP B 1 534 ? 37.111 -7.050 10.283 1.00 20.50 ? 534 ASP B CA 1 ATOM 8496 C C . ASP B 1 534 ? 36.086 -8.040 10.796 1.00 19.69 ? 534 ASP B C 1 ATOM 8497 O O . ASP B 1 534 ? 35.529 -8.817 10.023 1.00 20.31 ? 534 ASP B O 1 ATOM 8498 C CB . ASP B 1 534 ? 38.502 -7.523 10.742 1.00 20.81 ? 534 ASP B CB 1 ATOM 8499 C CG . ASP B 1 534 ? 39.646 -6.769 10.084 1.00 23.33 ? 534 ASP B CG 1 ATOM 8500 O OD1 . ASP B 1 534 ? 39.413 -5.801 9.326 1.00 25.12 ? 534 ASP B OD1 1 ATOM 8501 O OD2 . ASP B 1 534 ? 40.805 -7.142 10.354 1.00 25.56 ? 534 ASP B OD2 1 ATOM 8502 N N . ASP B 1 535 ? 35.781 -7.926 12.088 1.00 18.72 ? 535 ASP B N 1 ATOM 8503 C CA . ASP B 1 535 ? 34.827 -8.805 12.736 1.00 18.68 ? 535 ASP B CA 1 ATOM 8504 C C . ASP B 1 535 ? 33.392 -8.574 12.273 1.00 17.81 ? 535 ASP B C 1 ATOM 8505 O O . ASP B 1 535 ? 32.619 -9.525 12.192 1.00 19.09 ? 535 ASP B O 1 ATOM 8506 C CB . ASP B 1 535 ? 34.932 -8.707 14.252 1.00 18.68 ? 535 ASP B CB 1 ATOM 8507 C CG . ASP B 1 535 ? 34.538 -9.988 14.921 1.00 19.95 ? 535 ASP B CG 1 ATOM 8508 O OD1 . ASP B 1 535 ? 35.237 -10.999 14.698 1.00 22.28 ? 535 ASP B OD1 1 ATOM 8509 O OD2 . ASP B 1 535 ? 33.515 -9.998 15.628 1.00 20.55 ? 535 ASP B OD2 1 ATOM 8510 N N . PHE B 1 536 ? 33.065 -7.320 11.946 1.00 15.09 ? 536 PHE B N 1 ATOM 8511 C CA . PHE B 1 536 ? 31.746 -6.940 11.451 1.00 14.90 ? 536 PHE B CA 1 ATOM 8512 C C . PHE B 1 536 ? 31.554 -7.615 10.091 1.00 16.00 ? 536 PHE B C 1 ATOM 8513 O O . PHE B 1 536 ? 30.471 -8.122 9.798 1.00 16.93 ? 536 PHE B O 1 ATOM 8514 C CB . PHE B 1 536 ? 31.651 -5.401 11.318 1.00 13.47 ? 536 PHE B CB 1 ATOM 8515 C CG . PHE B 1 536 ? 30.450 -4.912 10.539 1.00 11.43 ? 536 PHE B CG 1 ATOM 8516 C CD1 . PHE B 1 536 ? 30.531 -4.706 9.139 1.00 11.54 ? 536 PHE B CD1 1 ATOM 8517 C CD2 . PHE B 1 536 ? 29.225 -4.689 11.183 1.00 8.12 ? 536 PHE B CD2 1 ATOM 8518 C CE1 . PHE B 1 536 ? 29.408 -4.293 8.394 1.00 7.89 ? 536 PHE B CE1 1 ATOM 8519 C CE2 . PHE B 1 536 ? 28.091 -4.270 10.450 1.00 7.21 ? 536 PHE B CE2 1 ATOM 8520 C CZ . PHE B 1 536 ? 28.182 -4.074 9.051 1.00 8.33 ? 536 PHE B CZ 1 ATOM 8521 N N . ASN B 1 537 ? 32.592 -7.525 9.256 1.00 15.42 ? 537 ASN B N 1 ATOM 8522 C CA . ASN B 1 537 ? 32.605 -8.116 7.923 1.00 14.87 ? 537 ASN B CA 1 ATOM 8523 C C . ASN B 1 537 ? 32.664 -9.635 7.953 1.00 15.84 ? 537 ASN B C 1 ATOM 8524 O O . ASN B 1 537 ? 32.090 -10.285 7.086 1.00 17.65 ? 537 ASN B O 1 ATOM 8525 C CB . ASN B 1 537 ? 33.767 -7.566 7.104 1.00 14.30 ? 537 ASN B CB 1 ATOM 8526 C CG . ASN B 1 537 ? 33.500 -6.169 6.588 1.00 14.72 ? 537 ASN B CG 1 ATOM 8527 O OD1 . ASN B 1 537 ? 32.396 -5.870 6.116 1.00 15.92 ? 537 ASN B OD1 1 ATOM 8528 N ND2 . ASN B 1 537 ? 34.509 -5.304 6.667 1.00 8.51 ? 537 ASN B ND2 1 ATOM 8529 N N . ARG B 1 538 ? 33.309 -10.192 8.979 1.00 15.25 ? 538 ARG B N 1 ATOM 8530 C CA . ARG B 1 538 ? 33.419 -11.642 9.147 1.00 14.97 ? 538 ARG B CA 1 ATOM 8531 C C . ARG B 1 538 ? 32.041 -12.238 9.444 1.00 15.03 ? 538 ARG B C 1 ATOM 8532 O O . ARG B 1 538 ? 31.628 -13.191 8.789 1.00 15.15 ? 538 ARG B O 1 ATOM 8533 C CB . ARG B 1 538 ? 34.390 -11.986 10.288 1.00 15.41 ? 538 ARG B CB 1 ATOM 8534 C CG . ARG B 1 538 ? 34.557 -13.477 10.581 1.00 13.98 ? 538 ARG B CG 1 ATOM 8535 C CD . ARG B 1 538 ? 35.298 -13.732 11.891 1.00 15.82 ? 538 ARG B CD 1 ATOM 8536 N NE . ARG B 1 538 ? 34.568 -13.260 13.068 1.00 13.83 ? 538 ARG B NE 1 ATOM 8537 C CZ . ARG B 1 538 ? 33.597 -13.926 13.693 1.00 15.63 ? 538 ARG B CZ 1 ATOM 8538 N NH1 . ARG B 1 538 ? 33.202 -15.125 13.270 1.00 13.18 ? 538 ARG B NH1 1 ATOM 8539 N NH2 . ARG B 1 538 ? 33.016 -13.383 14.756 1.00 16.43 ? 538 ARG B NH2 1 ATOM 8540 N N . VAL B 1 539 ? 31.323 -11.622 10.387 1.00 15.14 ? 539 VAL B N 1 ATOM 8541 C CA . VAL B 1 539 ? 29.992 -12.078 10.799 1.00 14.31 ? 539 VAL B CA 1 ATOM 8542 C C . VAL B 1 539 ? 28.973 -11.883 9.684 1.00 14.06 ? 539 VAL B C 1 ATOM 8543 O O . VAL B 1 539 ? 28.101 -12.729 9.493 1.00 16.09 ? 539 VAL B O 1 ATOM 8544 C CB . VAL B 1 539 ? 29.522 -11.386 12.119 1.00 12.22 ? 539 VAL B CB 1 ATOM 8545 C CG1 . VAL B 1 539 ? 28.181 -11.931 12.578 1.00 8.35 ? 539 VAL B CG1 1 ATOM 8546 C CG2 . VAL B 1 539 ? 30.535 -11.635 13.221 1.00 11.50 ? 539 VAL B CG2 1 ATOM 8547 N N . CYS B 1 540 ? 29.120 -10.804 8.920 1.00 14.35 ? 540 CYS B N 1 ATOM 8548 C CA . CYS B 1 540 ? 28.204 -10.539 7.814 1.00 15.58 ? 540 CYS B CA 1 ATOM 8549 C C . CYS B 1 540 ? 28.368 -11.528 6.675 1.00 13.97 ? 540 CYS B C 1 ATOM 8550 O O . CYS B 1 540 ? 27.376 -11.969 6.113 1.00 14.15 ? 540 CYS B O 1 ATOM 8551 C CB . CYS B 1 540 ? 28.301 -9.093 7.317 1.00 16.69 ? 540 CYS B CB 1 ATOM 8552 S SG . CYS B 1 540 ? 27.424 -7.890 8.372 1.00 21.01 ? 540 CYS B SG 1 ATOM 8553 N N . ASP B 1 541 ? 29.610 -11.945 6.426 1.00 12.78 ? 541 ASP B N 1 ATOM 8554 C CA . ASP B 1 541 ? 29.928 -12.910 5.377 1.00 14.17 ? 541 ASP B CA 1 ATOM 8555 C C . ASP B 1 541 ? 29.386 -14.294 5.715 1.00 14.94 ? 541 ASP B C 1 ATOM 8556 O O . ASP B 1 541 ? 28.787 -14.956 4.864 1.00 15.32 ? 541 ASP B O 1 ATOM 8557 C CB . ASP B 1 541 ? 31.442 -12.975 5.148 1.00 14.84 ? 541 ASP B CB 1 ATOM 8558 C CG . ASP B 1 541 ? 31.992 -11.714 4.489 1.00 16.70 ? 541 ASP B CG 1 ATOM 8559 O OD1 . ASP B 1 541 ? 31.214 -10.772 4.199 1.00 16.49 ? 541 ASP B OD1 1 ATOM 8560 O OD2 . ASP B 1 541 ? 33.219 -11.647 4.288 1.00 18.85 ? 541 ASP B OD2 1 ATOM 8561 N N . GLU B 1 542 ? 29.507 -14.662 6.992 1.00 15.10 ? 542 GLU B N 1 ATOM 8562 C CA . GLU B 1 542 ? 29.042 -15.946 7.511 1.00 14.92 ? 542 GLU B CA 1 ATOM 8563 C C . GLU B 1 542 ? 27.510 -16.030 7.507 1.00 14.05 ? 542 GLU B C 1 ATOM 8564 O O . GLU B 1 542 ? 26.937 -17.097 7.244 1.00 12.66 ? 542 GLU B O 1 ATOM 8565 C CB . GLU B 1 542 ? 29.593 -16.172 8.927 1.00 17.84 ? 542 GLU B CB 1 ATOM 8566 C CG . GLU B 1 542 ? 31.110 -16.461 9.013 1.00 19.48 ? 542 GLU B CG 1 ATOM 8567 C CD . GLU B 1 542 ? 31.624 -16.574 10.453 1.00 22.56 ? 542 GLU B CD 1 ATOM 8568 O OE1 . GLU B 1 542 ? 30.805 -16.751 11.384 1.00 25.05 ? 542 GLU B OE1 1 ATOM 8569 O OE2 . GLU B 1 542 ? 32.856 -16.494 10.658 1.00 23.66 ? 542 GLU B OE2 1 ATOM 8570 N N . TRP B 1 543 ? 26.873 -14.880 7.738 1.00 12.49 ? 543 TRP B N 1 ATOM 8571 C CA . TRP B 1 543 ? 25.422 -14.751 7.764 1.00 11.12 ? 543 TRP B CA 1 ATOM 8572 C C . TRP B 1 543 ? 24.842 -14.726 6.352 1.00 13.43 ? 543 TRP B C 1 ATOM 8573 O O . TRP B 1 543 ? 23.767 -15.283 6.110 1.00 13.19 ? 543 TRP B O 1 ATOM 8574 C CB . TRP B 1 543 ? 25.010 -13.486 8.547 1.00 11.46 ? 543 TRP B CB 1 ATOM 8575 C CG . TRP B 1 543 ? 23.531 -13.190 8.536 1.00 10.11 ? 543 TRP B CG 1 ATOM 8576 C CD1 . TRP B 1 543 ? 22.905 -12.196 7.839 1.00 12.18 ? 543 TRP B CD1 1 ATOM 8577 C CD2 . TRP B 1 543 ? 22.495 -13.941 9.178 1.00 10.55 ? 543 TRP B CD2 1 ATOM 8578 N NE1 . TRP B 1 543 ? 21.545 -12.282 7.998 1.00 11.27 ? 543 TRP B NE1 1 ATOM 8579 C CE2 . TRP B 1 543 ? 21.261 -13.342 8.816 1.00 11.42 ? 543 TRP B CE2 1 ATOM 8580 C CE3 . TRP B 1 543 ? 22.481 -15.068 10.023 1.00 10.07 ? 543 TRP B CE3 1 ATOM 8581 C CZ2 . TRP B 1 543 ? 20.019 -13.830 9.277 1.00 12.05 ? 543 TRP B CZ2 1 ATOM 8582 C CZ3 . TRP B 1 543 ? 21.243 -15.560 10.481 1.00 8.97 ? 543 TRP B CZ3 1 ATOM 8583 C CH2 . TRP B 1 543 ? 20.030 -14.938 10.107 1.00 9.61 ? 543 TRP B CH2 1 ATOM 8584 N N . ARG B 1 544 ? 25.537 -14.046 5.439 1.00 15.67 ? 544 ARG B N 1 ATOM 8585 C CA . ARG B 1 544 ? 25.104 -13.952 4.048 1.00 16.73 ? 544 ARG B CA 1 ATOM 8586 C C . ARG B 1 544 ? 25.214 -15.285 3.332 1.00 16.55 ? 544 ARG B C 1 ATOM 8587 O O . ARG B 1 544 ? 24.517 -15.520 2.348 1.00 18.77 ? 544 ARG B O 1 ATOM 8588 C CB . ARG B 1 544 ? 25.858 -12.852 3.304 1.00 18.03 ? 544 ARG B CB 1 ATOM 8589 C CG . ARG B 1 544 ? 25.183 -11.489 3.444 1.00 21.00 ? 544 ARG B CG 1 ATOM 8590 C CD . ARG B 1 544 ? 25.825 -10.425 2.564 1.00 25.60 ? 544 ARG B CD 1 ATOM 8591 N NE . ARG B 1 544 ? 27.181 -10.106 3.003 1.00 28.28 ? 544 ARG B NE 1 ATOM 8592 C CZ . ARG B 1 544 ? 27.586 -8.907 3.413 1.00 29.22 ? 544 ARG B CZ 1 ATOM 8593 N NH1 . ARG B 1 544 ? 26.745 -7.879 3.439 1.00 28.45 ? 544 ARG B NH1 1 ATOM 8594 N NH2 . ARG B 1 544 ? 28.832 -8.749 3.846 1.00 31.44 ? 544 ARG B NH2 1 ATOM 8595 N N . ALA B 1 545 ? 26.063 -16.161 3.878 1.00 17.28 ? 545 ALA B N 1 ATOM 8596 C CA . ALA B 1 545 ? 26.280 -17.519 3.379 1.00 15.52 ? 545 ALA B CA 1 ATOM 8597 C C . ALA B 1 545 ? 25.162 -18.418 3.923 1.00 15.75 ? 545 ALA B C 1 ATOM 8598 O O . ALA B 1 545 ? 24.592 -19.224 3.180 1.00 15.85 ? 545 ALA B O 1 ATOM 8599 C CB . ALA B 1 545 ? 27.633 -18.039 3.833 1.00 14.27 ? 545 ALA B CB 1 ATOM 8600 N N . TYR B 1 546 ? 24.826 -18.224 5.205 1.00 14.56 ? 546 TYR B N 1 ATOM 8601 C CA . TYR B 1 546 ? 23.774 -18.983 5.878 1.00 12.26 ? 546 TYR B CA 1 ATOM 8602 C C . TYR B 1 546 ? 22.340 -18.653 5.426 1.00 14.15 ? 546 TYR B C 1 ATOM 8603 O O . TYR B 1 546 ? 21.535 -19.572 5.293 1.00 15.95 ? 546 TYR B O 1 ATOM 8604 C CB . TYR B 1 546 ? 23.875 -18.884 7.437 1.00 7.77 ? 546 TYR B CB 1 ATOM 8605 C CG . TYR B 1 546 ? 22.662 -19.509 8.144 1.00 5.76 ? 546 TYR B CG 1 ATOM 8606 C CD1 . TYR B 1 546 ? 22.518 -20.910 8.222 1.00 1.00 ? 546 TYR B CD1 1 ATOM 8607 C CD2 . TYR B 1 546 ? 21.539 -18.707 8.494 1.00 4.89 ? 546 TYR B CD2 1 ATOM 8608 C CE1 . TYR B 1 546 ? 21.286 -21.501 8.594 1.00 2.62 ? 546 TYR B CE1 1 ATOM 8609 C CE2 . TYR B 1 546 ? 20.303 -19.284 8.860 1.00 5.91 ? 546 TYR B CE2 1 ATOM 8610 C CZ . TYR B 1 546 ? 20.181 -20.680 8.904 1.00 6.83 ? 546 TYR B CZ 1 ATOM 8611 O OH . TYR B 1 546 ? 18.964 -21.238 9.235 1.00 5.99 ? 546 TYR B OH 1 ATOM 8612 N N . TRP B 1 547 ? 21.997 -17.369 5.276 1.00 15.81 ? 547 TRP B N 1 ATOM 8613 C CA . TRP B 1 547 ? 20.627 -16.971 4.908 1.00 18.70 ? 547 TRP B CA 1 ATOM 8614 C C . TRP B 1 547 ? 19.890 -17.717 3.764 1.00 20.82 ? 547 TRP B C 1 ATOM 8615 O O . TRP B 1 547 ? 18.705 -18.034 3.929 1.00 21.33 ? 547 TRP B O 1 ATOM 8616 C CB . TRP B 1 547 ? 20.475 -15.429 4.826 1.00 17.10 ? 547 TRP B CB 1 ATOM 8617 C CG . TRP B 1 547 ? 19.036 -14.922 4.663 1.00 16.74 ? 547 TRP B CG 1 ATOM 8618 C CD1 . TRP B 1 547 ? 18.484 -14.385 3.532 1.00 17.25 ? 547 TRP B CD1 1 ATOM 8619 C CD2 . TRP B 1 547 ? 17.979 -14.960 5.638 1.00 18.08 ? 547 TRP B CD2 1 ATOM 8620 N NE1 . TRP B 1 547 ? 17.157 -14.099 3.732 1.00 16.34 ? 547 TRP B NE1 1 ATOM 8621 C CE2 . TRP B 1 547 ? 16.814 -14.440 5.012 1.00 16.60 ? 547 TRP B CE2 1 ATOM 8622 C CE3 . TRP B 1 547 ? 17.896 -15.387 6.983 1.00 18.89 ? 547 TRP B CE3 1 ATOM 8623 C CZ2 . TRP B 1 547 ? 15.571 -14.335 5.682 1.00 17.95 ? 547 TRP B CZ2 1 ATOM 8624 C CZ3 . TRP B 1 547 ? 16.655 -15.284 7.659 1.00 18.66 ? 547 TRP B CZ3 1 ATOM 8625 C CH2 . TRP B 1 547 ? 15.510 -14.761 6.998 1.00 18.34 ? 547 TRP B CH2 1 ATOM 8626 N N . PRO B 1 548 ? 20.556 -18.015 2.614 1.00 23.09 ? 548 PRO B N 1 ATOM 8627 C CA . PRO B 1 548 ? 19.817 -18.736 1.559 1.00 24.70 ? 548 PRO B CA 1 ATOM 8628 C C . PRO B 1 548 ? 19.373 -20.169 1.926 1.00 26.84 ? 548 PRO B C 1 ATOM 8629 O O . PRO B 1 548 ? 18.518 -20.744 1.245 1.00 28.89 ? 548 PRO B O 1 ATOM 8630 C CB . PRO B 1 548 ? 20.812 -18.744 0.401 1.00 23.17 ? 548 PRO B CB 1 ATOM 8631 C CG . PRO B 1 548 ? 21.504 -17.445 0.563 1.00 22.43 ? 548 PRO B CG 1 ATOM 8632 C CD . PRO B 1 548 ? 21.797 -17.450 2.041 1.00 23.01 ? 548 PRO B CD 1 ATOM 8633 N N . THR B 1 549 ? 19.930 -20.710 3.016 1.00 27.37 ? 549 THR B N 1 ATOM 8634 C CA . THR B 1 549 ? 19.609 -22.062 3.494 1.00 27.93 ? 549 THR B CA 1 ATOM 8635 C C . THR B 1 549 ? 18.534 -22.071 4.579 1.00 28.96 ? 549 THR B C 1 ATOM 8636 O O . THR B 1 549 ? 18.104 -23.142 5.015 1.00 29.85 ? 549 THR B O 1 ATOM 8637 C CB . THR B 1 549 ? 20.864 -22.828 4.041 1.00 27.84 ? 549 THR B CB 1 ATOM 8638 O OG1 . THR B 1 549 ? 21.334 -22.216 5.253 1.00 24.41 ? 549 THR B OG1 1 ATOM 8639 C CG2 . THR B 1 549 ? 21.988 -22.855 3.005 1.00 26.06 ? 549 THR B CG2 1 ATOM 8640 N N . ASN B 1 550 ? 18.126 -20.881 5.028 1.00 29.07 ? 550 ASN B N 1 ATOM 8641 C CA . ASN B 1 550 ? 17.095 -20.739 6.058 1.00 28.82 ? 550 ASN B CA 1 ATOM 8642 C C . ASN B 1 550 ? 15.735 -21.146 5.469 1.00 28.56 ? 550 ASN B C 1 ATOM 8643 O O . ASN B 1 550 ? 15.353 -20.651 4.406 1.00 28.33 ? 550 ASN B O 1 ATOM 8644 C CB . ASN B 1 550 ? 17.048 -19.296 6.582 1.00 28.12 ? 550 ASN B CB 1 ATOM 8645 C CG . ASN B 1 550 ? 16.316 -19.175 7.914 1.00 27.73 ? 550 ASN B CG 1 ATOM 8646 O OD1 . ASN B 1 550 ? 15.378 -18.388 8.059 1.00 26.38 ? 550 ASN B OD1 1 ATOM 8647 N ND2 . ASN B 1 550 ? 16.744 -19.960 8.893 1.00 26.84 ? 550 ASN B ND2 1 ATOM 8648 N N . PRO B 1 551 ? 15.018 -22.090 6.127 1.00 28.71 ? 551 PRO B N 1 ATOM 8649 C CA . PRO B 1 551 ? 13.709 -22.547 5.639 1.00 29.14 ? 551 PRO B CA 1 ATOM 8650 C C . PRO B 1 551 ? 12.543 -21.606 5.950 1.00 28.19 ? 551 PRO B C 1 ATOM 8651 O O . PRO B 1 551 ? 11.416 -21.830 5.495 1.00 29.33 ? 551 PRO B O 1 ATOM 8652 C CB . PRO B 1 551 ? 13.549 -23.897 6.343 1.00 29.76 ? 551 PRO B CB 1 ATOM 8653 C CG . PRO B 1 551 ? 14.187 -23.652 7.673 1.00 29.40 ? 551 PRO B CG 1 ATOM 8654 C CD . PRO B 1 551 ? 15.446 -22.903 7.288 1.00 29.62 ? 551 PRO B CD 1 ATOM 8655 N N . TYR B 1 552 ? 12.839 -20.558 6.717 1.00 26.90 ? 552 TYR B N 1 ATOM 8656 C CA . TYR B 1 552 ? 11.857 -19.565 7.145 1.00 25.98 ? 552 TYR B CA 1 ATOM 8657 C C . TYR B 1 552 ? 12.133 -18.153 6.611 1.00 25.52 ? 552 TYR B C 1 ATOM 8658 O O . TYR B 1 552 ? 13.292 -17.800 6.349 1.00 25.91 ? 552 TYR B O 1 ATOM 8659 C CB . TYR B 1 552 ? 11.833 -19.481 8.684 1.00 23.85 ? 552 TYR B CB 1 ATOM 8660 C CG . TYR B 1 552 ? 11.554 -20.769 9.440 1.00 23.56 ? 552 TYR B CG 1 ATOM 8661 C CD1 . TYR B 1 552 ? 10.468 -21.613 9.096 1.00 23.81 ? 552 TYR B CD1 1 ATOM 8662 C CD2 . TYR B 1 552 ? 12.331 -21.112 10.564 1.00 22.73 ? 552 TYR B CD2 1 ATOM 8663 C CE1 . TYR B 1 552 ? 10.162 -22.771 9.871 1.00 22.82 ? 552 TYR B CE1 1 ATOM 8664 C CE2 . TYR B 1 552 ? 12.036 -22.257 11.344 1.00 21.85 ? 552 TYR B CE2 1 ATOM 8665 C CZ . TYR B 1 552 ? 10.954 -23.077 10.994 1.00 23.38 ? 552 TYR B CZ 1 ATOM 8666 O OH . TYR B 1 552 ? 10.673 -24.177 11.769 1.00 25.88 ? 552 TYR B OH 1 ATOM 8667 N N . PRO B 1 553 ? 11.064 -17.360 6.355 1.00 24.81 ? 553 PRO B N 1 ATOM 8668 C CA . PRO B 1 553 ? 11.265 -15.988 5.863 1.00 24.79 ? 553 PRO B CA 1 ATOM 8669 C C . PRO B 1 553 ? 11.308 -14.965 7.020 1.00 24.35 ? 553 PRO B C 1 ATOM 8670 O O . PRO B 1 553 ? 11.201 -15.332 8.195 1.00 23.86 ? 553 PRO B O 1 ATOM 8671 C CB . PRO B 1 553 ? 10.047 -15.773 4.966 1.00 24.04 ? 553 PRO B CB 1 ATOM 8672 C CG . PRO B 1 553 ? 8.975 -16.531 5.674 1.00 22.84 ? 553 PRO B CG 1 ATOM 8673 C CD . PRO B 1 553 ? 9.681 -17.810 6.069 1.00 24.12 ? 553 PRO B CD 1 ATOM 8674 N N . LYS B 1 554 ? 11.473 -13.693 6.666 1.00 25.76 ? 554 LYS B N 1 ATOM 8675 C CA . LYS B 1 554 ? 11.509 -12.577 7.617 1.00 26.32 ? 554 LYS B CA 1 ATOM 8676 C C . LYS B 1 554 ? 10.118 -11.934 7.548 1.00 26.14 ? 554 LYS B C 1 ATOM 8677 O O . LYS B 1 554 ? 9.796 -11.243 6.581 1.00 26.27 ? 554 LYS B O 1 ATOM 8678 C CB . LYS B 1 554 ? 12.610 -11.595 7.188 1.00 26.96 ? 554 LYS B CB 1 ATOM 8679 C CG . LYS B 1 554 ? 12.769 -10.311 8.000 1.00 27.19 ? 554 LYS B CG 1 ATOM 8680 C CD . LYS B 1 554 ? 13.926 -9.510 7.405 1.00 27.11 ? 554 LYS B CD 1 ATOM 8681 C CE . LYS B 1 554 ? 14.164 -8.194 8.107 1.00 25.07 ? 554 LYS B CE 1 ATOM 8682 N NZ . LYS B 1 554 ? 13.058 -7.231 7.873 1.00 27.96 ? 554 LYS B NZ 1 ATOM 8683 N N . ILE B 1 555 ? 9.292 -12.195 8.562 1.00 28.18 ? 555 ILE B N 1 ATOM 8684 C CA . ILE B 1 555 ? 7.920 -11.673 8.601 1.00 29.24 ? 555 ILE B CA 1 ATOM 8685 C C . ILE B 1 555 ? 7.753 -10.256 9.148 1.00 28.51 ? 555 ILE B C 1 ATOM 8686 O O . ILE B 1 555 ? 6.736 -9.602 8.882 1.00 30.03 ? 555 ILE B O 1 ATOM 8687 C CB . ILE B 1 555 ? 6.940 -12.632 9.358 1.00 30.88 ? 555 ILE B CB 1 ATOM 8688 C CG1 . ILE B 1 555 ? 7.359 -12.818 10.828 1.00 32.64 ? 555 ILE B CG1 1 ATOM 8689 C CG2 . ILE B 1 555 ? 6.846 -13.963 8.625 1.00 31.03 ? 555 ILE B CG2 1 ATOM 8690 C CD1 . ILE B 1 555 ? 6.247 -13.341 11.740 1.00 33.34 ? 555 ILE B CD1 1 ATOM 8691 N N . ASP B 1 556 ? 8.747 -9.788 9.895 1.00 26.14 ? 556 ASP B N 1 ATOM 8692 C CA . ASP B 1 556 ? 8.679 -8.462 10.484 1.00 25.43 ? 556 ASP B CA 1 ATOM 8693 C C . ASP B 1 556 ? 9.820 -7.515 10.107 1.00 25.33 ? 556 ASP B C 1 ATOM 8694 O O . ASP B 1 556 ? 10.506 -7.733 9.102 1.00 27.13 ? 556 ASP B O 1 ATOM 8695 C CB . ASP B 1 556 ? 8.484 -8.565 12.012 1.00 26.27 ? 556 ASP B CB 1 ATOM 8696 C CG . ASP B 1 556 ? 9.563 -9.389 12.723 1.00 25.38 ? 556 ASP B CG 1 ATOM 8697 O OD1 . ASP B 1 556 ? 10.606 -9.729 12.128 1.00 26.67 ? 556 ASP B OD1 1 ATOM 8698 O OD2 . ASP B 1 556 ? 9.358 -9.689 13.912 1.00 26.25 ? 556 ASP B OD2 1 ATOM 8699 N N . SER B 1 557 ? 9.989 -6.461 10.912 1.00 23.31 ? 557 SER B N 1 ATOM 8700 C CA . SER B 1 557 ? 11.015 -5.426 10.734 1.00 21.85 ? 557 SER B CA 1 ATOM 8701 C C . SER B 1 557 ? 12.450 -5.925 10.886 1.00 21.11 ? 557 SER B C 1 ATOM 8702 O O . SER B 1 557 ? 13.355 -5.433 10.224 1.00 21.34 ? 557 SER B O 1 ATOM 8703 C CB . SER B 1 557 ? 10.791 -4.290 11.740 1.00 19.82 ? 557 SER B CB 1 ATOM 8704 O OG . SER B 1 557 ? 11.029 -4.706 13.074 1.00 17.30 ? 557 SER B OG 1 ATOM 8705 N N . GLY B 1 558 ? 12.639 -6.890 11.779 1.00 22.21 ? 558 GLY B N 1 ATOM 8706 C CA . GLY B 1 558 ? 13.959 -7.426 12.033 1.00 22.18 ? 558 GLY B CA 1 ATOM 8707 C C . GLY B 1 558 ? 14.516 -6.883 13.329 1.00 22.84 ? 558 GLY B C 1 ATOM 8708 O O . GLY B 1 558 ? 15.413 -7.477 13.935 1.00 23.33 ? 558 GLY B O 1 ATOM 8709 N N . ALA B 1 559 ? 13.954 -5.749 13.745 1.00 22.80 ? 559 ALA B N 1 ATOM 8710 C CA . ALA B 1 559 ? 14.322 -5.051 14.971 1.00 22.62 ? 559 ALA B CA 1 ATOM 8711 C C . ALA B 1 559 ? 13.469 -5.540 16.147 1.00 23.64 ? 559 ALA B C 1 ATOM 8712 O O . ALA B 1 559 ? 12.530 -6.329 15.902 1.00 24.39 ? 559 ALA B O 1 ATOM 8713 C CB . ALA B 1 559 ? 14.152 -3.551 14.773 1.00 20.22 ? 559 ALA B CB 1 ATOM 8714 O OXT . ALA B 1 559 ? 13.750 -5.138 17.302 1.00 25.21 ? 559 ALA B OXT 1 HETATM 8715 C C1 . NAG C 2 . ? -43.846 23.320 24.292 1.00 24.13 ? 700 NAG A C1 1 HETATM 8716 C C2 . NAG C 2 . ? -45.106 24.069 23.856 1.00 25.53 ? 700 NAG A C2 1 HETATM 8717 C C3 . NAG C 2 . ? -44.728 25.407 23.203 1.00 26.47 ? 700 NAG A C3 1 HETATM 8718 C C4 . NAG C 2 . ? -43.766 26.208 24.094 1.00 26.56 ? 700 NAG A C4 1 HETATM 8719 C C5 . NAG C 2 . ? -42.594 25.331 24.554 1.00 26.30 ? 700 NAG A C5 1 HETATM 8720 C C6 . NAG C 2 . ? -41.699 26.023 25.566 1.00 26.21 ? 700 NAG A C6 1 HETATM 8721 C C7 . NAG C 2 . ? -46.999 22.681 23.315 1.00 26.29 ? 700 NAG A C7 1 HETATM 8722 C C8 . NAG C 2 . ? -48.101 22.519 22.277 1.00 24.48 ? 700 NAG A C8 1 HETATM 8723 N N2 . NAG C 2 . ? -45.864 23.252 22.923 1.00 25.10 ? 700 NAG A N2 1 HETATM 8724 O O3 . NAG C 2 . ? -45.904 26.170 22.972 1.00 22.36 ? 700 NAG A O3 1 HETATM 8725 O O4 . NAG C 2 . ? -43.265 27.323 23.369 1.00 29.64 ? 700 NAG A O4 1 HETATM 8726 O O5 . NAG C 2 . ? -43.087 24.133 25.184 1.00 25.65 ? 700 NAG A O5 1 HETATM 8727 O O6 . NAG C 2 . ? -42.363 26.194 26.813 1.00 25.49 ? 700 NAG A O6 1 HETATM 8728 O O7 . NAG C 2 . ? -47.198 22.330 24.483 1.00 25.68 ? 700 NAG A O7 1 HETATM 8729 C C1 . NAG D 2 . ? -30.930 16.225 14.484 1.00 19.11 ? 710 NAG A C1 1 HETATM 8730 C C2 . NAG D 2 . ? -30.295 16.134 13.108 1.00 18.82 ? 710 NAG A C2 1 HETATM 8731 C C3 . NAG D 2 . ? -28.782 16.213 13.271 1.00 19.99 ? 710 NAG A C3 1 HETATM 8732 C C4 . NAG D 2 . ? -28.409 17.490 14.037 1.00 20.43 ? 710 NAG A C4 1 HETATM 8733 C C5 . NAG D 2 . ? -29.235 17.666 15.326 1.00 21.20 ? 710 NAG A C5 1 HETATM 8734 C C6 . NAG D 2 . ? -29.061 19.034 15.968 1.00 20.75 ? 710 NAG A C6 1 HETATM 8735 C C7 . NAG D 2 . ? -31.433 14.899 11.375 1.00 13.94 ? 710 NAG A C7 1 HETATM 8736 C C8 . NAG D 2 . ? -31.282 13.710 10.446 1.00 13.99 ? 710 NAG A C8 1 HETATM 8737 N N2 . NAG D 2 . ? -30.675 14.893 12.468 1.00 18.14 ? 710 NAG A N2 1 HETATM 8738 O O3 . NAG D 2 . ? -28.176 16.235 11.985 1.00 20.01 ? 710 NAG A O3 1 HETATM 8739 O O4 . NAG D 2 . ? -27.018 17.455 14.385 1.00 20.72 ? 710 NAG A O4 1 HETATM 8740 O O5 . NAG D 2 . ? -30.643 17.499 15.060 1.00 21.23 ? 710 NAG A O5 1 HETATM 8741 O O6 . NAG D 2 . ? -28.979 20.072 14.996 1.00 22.86 ? 710 NAG A O6 1 HETATM 8742 O O7 . NAG D 2 . ? -32.233 15.798 11.106 1.00 11.71 ? 710 NAG A O7 1 HETATM 8743 C C1 . NAG E 2 . ? -26.197 18.306 13.668 1.00 21.79 ? 711 NAG A C1 1 HETATM 8744 C C2 . NAG E 2 . ? -24.958 18.637 14.501 1.00 21.98 ? 711 NAG A C2 1 HETATM 8745 C C3 . NAG E 2 . ? -23.958 19.445 13.661 1.00 24.72 ? 711 NAG A C3 1 HETATM 8746 C C4 . NAG E 2 . ? -23.674 18.725 12.341 1.00 27.19 ? 711 NAG A C4 1 HETATM 8747 C C5 . NAG E 2 . ? -24.976 18.435 11.604 1.00 26.26 ? 711 NAG A C5 1 HETATM 8748 C C6 . NAG E 2 . ? -24.750 17.646 10.323 1.00 24.70 ? 711 NAG A C6 1 HETATM 8749 C C7 . NAG E 2 . ? -25.430 18.865 16.878 1.00 20.54 ? 711 NAG A C7 1 HETATM 8750 C C8 . NAG E 2 . ? -25.561 19.829 18.051 1.00 19.98 ? 711 NAG A C8 1 HETATM 8751 N N2 . NAG E 2 . ? -25.367 19.411 15.663 1.00 21.88 ? 711 NAG A N2 1 HETATM 8752 O O3 . NAG E 2 . ? -22.744 19.604 14.382 1.00 22.91 ? 711 NAG A O3 1 HETATM 8753 O O4 . NAG E 2 . ? -22.819 19.525 11.512 1.00 32.22 ? 711 NAG A O4 1 HETATM 8754 O O5 . NAG E 2 . ? -25.843 17.646 12.442 1.00 24.02 ? 711 NAG A O5 1 HETATM 8755 O O6 . NAG E 2 . ? -24.226 16.352 10.595 1.00 26.00 ? 711 NAG A O6 1 HETATM 8756 O O7 . NAG E 2 . ? -25.396 17.650 17.084 1.00 19.47 ? 711 NAG A O7 1 HETATM 8757 C C1 . BMA F 3 . ? -21.626 18.923 11.169 1.00 38.32 ? 712 BMA A C1 1 HETATM 8758 C C2 . BMA F 3 . ? -21.063 19.567 9.907 1.00 39.81 ? 712 BMA A C2 1 HETATM 8759 C C3 . BMA F 3 . ? -19.738 18.882 9.568 1.00 42.67 ? 712 BMA A C3 1 HETATM 8760 C C4 . BMA F 3 . ? -18.768 19.003 10.761 1.00 44.65 ? 712 BMA A C4 1 HETATM 8761 C C5 . BMA F 3 . ? -19.432 18.462 12.045 1.00 44.52 ? 712 BMA A C5 1 HETATM 8762 C C6 . BMA F 3 . ? -18.595 18.717 13.296 1.00 46.70 ? 712 BMA A C6 1 HETATM 8763 O O2 . BMA F 3 . ? -20.850 20.953 10.141 1.00 38.56 ? 712 BMA A O2 1 HETATM 8764 O O3 . BMA F 3 . ? -19.163 19.482 8.390 1.00 42.08 ? 712 BMA A O3 1 HETATM 8765 O O4 . BMA F 3 . ? -17.572 18.278 10.494 1.00 46.06 ? 712 BMA A O4 1 HETATM 8766 O O5 . BMA F 3 . ? -20.715 19.101 12.261 1.00 41.61 ? 712 BMA A O5 1 HETATM 8767 O O6 . BMA F 3 . ? -18.724 20.099 13.693 1.00 48.81 ? 712 BMA A O6 1 HETATM 8768 C C1 . MAN G 4 . ? -18.848 20.258 15.081 1.00 49.56 ? 714 MAN A C1 1 HETATM 8769 C C2 . MAN G 4 . ? -19.567 21.577 15.388 1.00 49.59 ? 714 MAN A C2 1 HETATM 8770 C C3 . MAN G 4 . ? -18.705 22.764 14.941 1.00 49.77 ? 714 MAN A C3 1 HETATM 8771 C C4 . MAN G 4 . ? -17.280 22.672 15.510 1.00 49.96 ? 714 MAN A C4 1 HETATM 8772 C C5 . MAN G 4 . ? -16.666 21.268 15.319 1.00 49.37 ? 714 MAN A C5 1 HETATM 8773 C C6 . MAN G 4 . ? -15.384 21.072 16.117 1.00 48.43 ? 714 MAN A C6 1 HETATM 8774 O O2 . MAN G 4 . ? -19.835 21.667 16.782 1.00 49.51 ? 714 MAN A O2 1 HETATM 8775 O O3 . MAN G 4 . ? -19.308 23.988 15.354 1.00 48.57 ? 714 MAN A O3 1 HETATM 8776 O O4 . MAN G 4 . ? -16.462 23.629 14.848 1.00 50.78 ? 714 MAN A O4 1 HETATM 8777 O O5 . MAN G 4 . ? -17.588 20.236 15.743 1.00 49.82 ? 714 MAN A O5 1 HETATM 8778 O O6 . MAN G 4 . ? -15.646 20.896 17.503 1.00 45.98 ? 714 MAN A O6 1 HETATM 8779 C C1 . NAG H 2 . ? -29.098 15.687 52.620 1.00 27.23 ? 720 NAG A C1 1 HETATM 8780 C C2 . NAG H 2 . ? -28.157 16.733 53.189 1.00 28.49 ? 720 NAG A C2 1 HETATM 8781 C C3 . NAG H 2 . ? -28.268 16.724 54.704 1.00 29.97 ? 720 NAG A C3 1 HETATM 8782 C C4 . NAG H 2 . ? -29.729 16.986 55.110 1.00 29.81 ? 720 NAG A C4 1 HETATM 8783 C C5 . NAG H 2 . ? -30.705 16.050 54.369 1.00 29.12 ? 720 NAG A C5 1 HETATM 8784 C C6 . NAG H 2 . ? -32.145 16.518 54.540 1.00 28.24 ? 720 NAG A C6 1 HETATM 8785 C C7 . NAG H 2 . ? -26.206 17.314 51.888 1.00 30.53 ? 720 NAG A C7 1 HETATM 8786 C C8 . NAG H 2 . ? -24.695 17.257 51.778 1.00 29.32 ? 720 NAG A C8 1 HETATM 8787 N N2 . NAG H 2 . ? -26.790 16.489 52.760 1.00 30.09 ? 720 NAG A N2 1 HETATM 8788 O O3 . NAG H 2 . ? -27.425 17.737 55.234 1.00 29.35 ? 720 NAG A O3 1 HETATM 8789 O O4 . NAG H 2 . ? -29.884 16.784 56.527 1.00 32.01 ? 720 NAG A O4 1 HETATM 8790 O O5 . NAG H 2 . ? -30.445 16.040 52.947 1.00 27.56 ? 720 NAG A O5 1 HETATM 8791 O O6 . NAG H 2 . ? -33.058 15.433 54.467 1.00 26.80 ? 720 NAG A O6 1 HETATM 8792 O O7 . NAG H 2 . ? -26.834 18.112 51.189 1.00 31.99 ? 720 NAG A O7 1 HETATM 8793 C C1 . NAG I 2 . ? -30.212 17.885 57.304 1.00 33.99 ? 721 NAG A C1 1 HETATM 8794 C C2 . NAG I 2 . ? -30.717 17.375 58.671 1.00 35.00 ? 721 NAG A C2 1 HETATM 8795 C C3 . NAG I 2 . ? -30.659 18.433 59.787 1.00 35.82 ? 721 NAG A C3 1 HETATM 8796 C C4 . NAG I 2 . ? -29.367 19.245 59.754 1.00 36.57 ? 721 NAG A C4 1 HETATM 8797 C C5 . NAG I 2 . ? -29.160 19.781 58.343 1.00 36.75 ? 721 NAG A C5 1 HETATM 8798 C C6 . NAG I 2 . ? -27.921 20.657 58.197 1.00 38.12 ? 721 NAG A C6 1 HETATM 8799 C C7 . NAG I 2 . ? -32.394 15.632 58.464 1.00 34.66 ? 721 NAG A C7 1 HETATM 8800 C C8 . NAG I 2 . ? -33.274 15.193 57.315 1.00 35.35 ? 721 NAG A C8 1 HETATM 8801 N N2 . NAG I 2 . ? -32.095 16.928 58.540 1.00 36.34 ? 721 NAG A N2 1 HETATM 8802 O O3 . NAG I 2 . ? -30.759 17.780 61.043 1.00 37.31 ? 721 NAG A O3 1 HETATM 8803 O O4 . NAG I 2 . ? -29.450 20.335 60.696 1.00 37.45 ? 721 NAG A O4 1 HETATM 8804 O O5 . NAG I 2 . ? -29.017 18.674 57.436 1.00 35.57 ? 721 NAG A O5 1 HETATM 8805 O O6 . NAG I 2 . ? -26.733 19.883 58.083 1.00 39.28 ? 721 NAG A O6 1 HETATM 8806 O O7 . NAG I 2 . ? -31.980 14.797 59.264 1.00 36.41 ? 721 NAG A O7 1 HETATM 8807 C C1 . NAG J 2 . ? -16.836 7.040 46.394 1.00 23.39 ? 730 NAG A C1 1 HETATM 8808 C C2 . NAG J 2 . ? -15.354 6.634 46.323 1.00 24.95 ? 730 NAG A C2 1 HETATM 8809 C C3 . NAG J 2 . ? -14.460 7.593 47.112 1.00 26.09 ? 730 NAG A C3 1 HETATM 8810 C C4 . NAG J 2 . ? -14.762 9.047 46.736 1.00 27.52 ? 730 NAG A C4 1 HETATM 8811 C C5 . NAG J 2 . ? -16.261 9.317 46.869 1.00 26.76 ? 730 NAG A C5 1 HETATM 8812 C C6 . NAG J 2 . ? -16.647 10.725 46.462 1.00 24.96 ? 730 NAG A C6 1 HETATM 8813 C C7 . NAG J 2 . ? -14.716 4.317 46.085 1.00 24.93 ? 730 NAG A C7 1 HETATM 8814 C C8 . NAG J 2 . ? -14.133 3.112 46.807 1.00 25.56 ? 730 NAG A C8 1 HETATM 8815 N N2 . NAG J 2 . ? -15.193 5.293 46.850 1.00 23.85 ? 730 NAG A N2 1 HETATM 8816 O O3 . NAG J 2 . ? -13.101 7.295 46.825 1.00 24.82 ? 730 NAG A O3 1 HETATM 8817 O O4 . NAG J 2 . ? -14.042 9.943 47.599 1.00 30.98 ? 730 NAG A O4 1 HETATM 8818 O O5 . NAG J 2 . ? -16.999 8.415 46.025 1.00 25.91 ? 730 NAG A O5 1 HETATM 8819 O O6 . NAG J 2 . ? -16.341 10.976 45.103 1.00 25.21 ? 730 NAG A O6 1 HETATM 8820 O O7 . NAG J 2 . ? -14.743 4.351 44.850 1.00 24.47 ? 730 NAG A O7 1 HETATM 8821 C C1 . NAG K 2 . ? -13.030 10.674 47.004 1.00 32.10 ? 731 NAG A C1 1 HETATM 8822 C C2 . NAG K 2 . ? -12.773 11.952 47.815 1.00 33.65 ? 731 NAG A C2 1 HETATM 8823 C C3 . NAG K 2 . ? -11.522 12.681 47.307 1.00 35.48 ? 731 NAG A C3 1 HETATM 8824 C C4 . NAG K 2 . ? -10.327 11.737 47.096 1.00 37.89 ? 731 NAG A C4 1 HETATM 8825 C C5 . NAG K 2 . ? -10.757 10.496 46.311 1.00 35.82 ? 731 NAG A C5 1 HETATM 8826 C C6 . NAG K 2 . ? -9.642 9.474 46.176 1.00 35.40 ? 731 NAG A C6 1 HETATM 8827 C C7 . NAG K 2 . ? -14.432 13.470 48.738 1.00 32.79 ? 731 NAG A C7 1 HETATM 8828 C C8 . NAG K 2 . ? -15.214 14.748 48.464 1.00 31.98 ? 731 NAG A C8 1 HETATM 8829 N N2 . NAG K 2 . ? -13.928 12.828 47.684 1.00 33.16 ? 731 NAG A N2 1 HETATM 8830 O O3 . NAG K 2 . ? -11.154 13.686 48.236 1.00 36.28 ? 731 NAG A O3 1 HETATM 8831 O O4 . NAG K 2 . ? -9.312 12.431 46.345 1.00 42.54 ? 731 NAG A O4 1 HETATM 8832 O O5 . NAG K 2 . ? -11.862 9.853 46.968 1.00 33.16 ? 731 NAG A O5 1 HETATM 8833 O O6 . NAG K 2 . ? -9.942 8.267 46.860 1.00 35.38 ? 731 NAG A O6 1 HETATM 8834 O O7 . NAG K 2 . ? -14.310 13.069 49.896 1.00 33.36 ? 731 NAG A O7 1 HETATM 8835 C C1 . BMA L 3 . ? -8.007 12.325 46.789 1.00 46.66 ? 732 BMA A C1 1 HETATM 8836 C C2 . BMA L 3 . ? -7.062 12.298 45.583 1.00 48.60 ? 732 BMA A C2 1 HETATM 8837 C C3 . BMA L 3 . ? -5.604 12.263 46.066 1.00 49.97 ? 732 BMA A C3 1 HETATM 8838 C C4 . BMA L 3 . ? -5.329 13.401 47.059 1.00 50.61 ? 732 BMA A C4 1 HETATM 8839 C C5 . BMA L 3 . ? -6.400 13.444 48.169 1.00 50.89 ? 732 BMA A C5 1 HETATM 8840 C C6 . BMA L 3 . ? -6.270 14.683 49.042 1.00 51.90 ? 732 BMA A C6 1 HETATM 8841 O O2 . BMA L 3 . ? -7.287 13.445 44.770 1.00 48.86 ? 732 BMA A O2 1 HETATM 8842 O O3 . BMA L 3 . ? -4.713 12.365 44.959 1.00 49.15 ? 732 BMA A O3 1 HETATM 8843 O O4 . BMA L 3 . ? -4.048 13.209 47.644 1.00 51.05 ? 732 BMA A O4 1 HETATM 8844 O O5 . BMA L 3 . ? -7.728 13.473 47.597 1.00 49.03 ? 732 BMA A O5 1 HETATM 8845 O O6 . BMA L 3 . ? -7.415 14.865 49.867 1.00 53.26 ? 732 BMA A O6 1 HETATM 8846 C C1 . NAG M 2 . ? -27.246 -15.663 8.356 1.00 29.35 ? 740 NAG A C1 1 HETATM 8847 C C2 . NAG M 2 . ? -28.653 -16.233 8.542 1.00 31.06 ? 740 NAG A C2 1 HETATM 8848 C C3 . NAG M 2 . ? -28.702 -17.660 7.976 1.00 32.82 ? 740 NAG A C3 1 HETATM 8849 C C4 . NAG M 2 . ? -28.114 -17.755 6.552 1.00 35.05 ? 740 NAG A C4 1 HETATM 8850 C C5 . NAG M 2 . ? -26.775 -17.002 6.446 1.00 33.78 ? 740 NAG A C5 1 HETATM 8851 C C6 . NAG M 2 . ? -26.289 -16.868 5.012 1.00 33.75 ? 740 NAG A C6 1 HETATM 8852 C C7 . NAG M 2 . ? -29.941 -15.480 10.450 1.00 30.74 ? 740 NAG A C7 1 HETATM 8853 C C8 . NAG M 2 . ? -30.676 -16.002 11.672 1.00 32.18 ? 740 NAG A C8 1 HETATM 8854 N N2 . NAG M 2 . ? -28.979 -16.255 9.958 1.00 31.30 ? 740 NAG A N2 1 HETATM 8855 O O3 . NAG M 2 . ? -30.046 -18.113 7.957 1.00 31.62 ? 740 NAG A O3 1 HETATM 8856 O O4 . NAG M 2 . ? -27.881 -19.145 6.233 1.00 39.28 ? 740 NAG A O4 1 HETATM 8857 O O5 . NAG M 2 . ? -26.897 -15.666 6.974 1.00 31.42 ? 740 NAG A O5 1 HETATM 8858 O O6 . NAG M 2 . ? -27.103 -15.969 4.272 1.00 34.01 ? 740 NAG A O6 1 HETATM 8859 O O7 . NAG M 2 . ? -30.244 -14.386 9.972 1.00 31.49 ? 740 NAG A O7 1 HETATM 8860 C C1 . NAG N 2 . ? -28.723 -19.759 5.318 1.00 41.17 ? 741 NAG A C1 1 HETATM 8861 C C2 . NAG N 2 . ? -28.058 -21.036 4.812 1.00 42.02 ? 741 NAG A C2 1 HETATM 8862 C C3 . NAG N 2 . ? -28.989 -21.733 3.829 1.00 43.34 ? 741 NAG A C3 1 HETATM 8863 C C4 . NAG N 2 . ? -30.327 -22.029 4.514 1.00 43.18 ? 741 NAG A C4 1 HETATM 8864 C C5 . NAG N 2 . ? -30.913 -20.751 5.146 1.00 42.21 ? 741 NAG A C5 1 HETATM 8865 C C6 . NAG N 2 . ? -32.122 -21.049 6.017 1.00 42.22 ? 741 NAG A C6 1 HETATM 8866 C C7 . NAG N 2 . ? -25.659 -21.129 4.769 1.00 43.64 ? 741 NAG A C7 1 HETATM 8867 C C8 . NAG N 2 . ? -24.620 -20.054 5.051 1.00 44.21 ? 741 NAG A C8 1 HETATM 8868 N N2 . NAG N 2 . ? -26.787 -20.745 4.181 1.00 42.31 ? 741 NAG A N2 1 HETATM 8869 O O3 . NAG N 2 . ? -28.392 -22.943 3.387 1.00 43.85 ? 741 NAG A O3 1 HETATM 8870 O O4 . NAG N 2 . ? -31.244 -22.557 3.565 1.00 43.77 ? 741 NAG A O4 1 HETATM 8871 O O5 . NAG N 2 . ? -29.941 -20.099 5.999 1.00 41.93 ? 741 NAG A O5 1 HETATM 8872 O O6 . NAG N 2 . ? -31.815 -21.993 7.037 1.00 40.53 ? 741 NAG A O6 1 HETATM 8873 O O7 . NAG N 2 . ? -25.449 -22.293 5.117 1.00 43.68 ? 741 NAG A O7 1 HETATM 8874 C C1 . NAG O 2 . ? -42.150 -3.739 -2.245 1.00 34.30 ? 750 NAG A C1 1 HETATM 8875 C C2 . NAG O 2 . ? -42.707 -2.942 -3.434 1.00 35.36 ? 750 NAG A C2 1 HETATM 8876 C C3 . NAG O 2 . ? -41.582 -2.735 -4.454 1.00 35.21 ? 750 NAG A C3 1 HETATM 8877 C C4 . NAG O 2 . ? -40.372 -2.071 -3.781 1.00 35.07 ? 750 NAG A C4 1 HETATM 8878 C C5 . NAG O 2 . ? -39.952 -2.855 -2.522 1.00 34.81 ? 750 NAG A C5 1 HETATM 8879 C C6 . NAG O 2 . ? -38.854 -2.174 -1.728 1.00 34.16 ? 750 NAG A C6 1 HETATM 8880 C C7 . NAG O 2 . ? -45.008 -3.064 -4.184 1.00 37.90 ? 750 NAG A C7 1 HETATM 8881 C C8 . NAG O 2 . ? -45.685 -3.200 -5.538 1.00 38.85 ? 750 NAG A C8 1 HETATM 8882 N N2 . NAG O 2 . ? -43.823 -3.656 -4.035 1.00 36.70 ? 750 NAG A N2 1 HETATM 8883 O O3 . NAG O 2 . ? -42.044 -1.920 -5.522 1.00 35.87 ? 750 NAG A O3 1 HETATM 8884 O O4 . NAG O 2 . ? -39.285 -2.020 -4.696 1.00 35.47 ? 750 NAG A O4 1 HETATM 8885 O O5 . NAG O 2 . ? -41.077 -3.012 -1.633 1.00 34.33 ? 750 NAG A O5 1 HETATM 8886 O O6 . NAG O 2 . ? -39.255 -0.880 -1.302 1.00 33.21 ? 750 NAG A O6 1 HETATM 8887 O O7 . NAG O 2 . ? -45.562 -2.425 -3.286 1.00 38.91 ? 750 NAG A O7 1 HETATM 8888 C C1 . NAG P 2 . ? -34.378 12.019 42.700 1.00 45.43 ? 760 NAG A C1 1 HETATM 8889 C C2 . NAG P 2 . ? -34.883 11.586 44.079 1.00 46.65 ? 760 NAG A C2 1 HETATM 8890 C C3 . NAG P 2 . ? -36.304 12.096 44.290 1.00 49.53 ? 760 NAG A C3 1 HETATM 8891 C C4 . NAG P 2 . ? -36.376 13.607 44.048 1.00 51.75 ? 760 NAG A C4 1 HETATM 8892 C C5 . NAG P 2 . ? -35.753 13.966 42.689 1.00 50.75 ? 760 NAG A C5 1 HETATM 8893 C C6 . NAG P 2 . ? -35.658 15.464 42.459 1.00 51.61 ? 760 NAG A C6 1 HETATM 8894 C C7 . NAG P 2 . ? -34.170 9.562 45.175 1.00 43.00 ? 760 NAG A C7 1 HETATM 8895 C C8 . NAG P 2 . ? -34.781 8.329 45.809 1.00 42.88 ? 760 NAG A C8 1 HETATM 8896 N N2 . NAG P 2 . ? -34.851 10.141 44.192 1.00 45.31 ? 760 NAG A N2 1 HETATM 8897 O O3 . NAG P 2 . ? -36.718 11.805 45.616 1.00 50.78 ? 760 NAG A O3 1 HETATM 8898 O O4 . NAG P 2 . ? -37.755 14.029 44.075 1.00 56.47 ? 760 NAG A O4 1 HETATM 8899 O O5 . NAG P 2 . ? -34.412 13.445 42.605 1.00 47.29 ? 760 NAG A O5 1 HETATM 8900 O O6 . NAG P 2 . ? -35.632 15.774 41.072 1.00 53.02 ? 760 NAG A O6 1 HETATM 8901 O O7 . NAG P 2 . ? -33.092 9.985 45.582 1.00 42.57 ? 760 NAG A O7 1 HETATM 8902 C C1 . NAG Q 2 . ? -38.058 15.119 44.879 1.00 60.45 ? 761 NAG A C1 1 HETATM 8903 C C2 . NAG Q 2 . ? -39.503 15.573 44.628 1.00 62.15 ? 761 NAG A C2 1 HETATM 8904 C C3 . NAG Q 2 . ? -39.873 16.705 45.597 1.00 63.46 ? 761 NAG A C3 1 HETATM 8905 C C4 . NAG Q 2 . ? -39.566 16.322 47.048 1.00 64.13 ? 761 NAG A C4 1 HETATM 8906 C C5 . NAG Q 2 . ? -38.127 15.794 47.175 1.00 64.48 ? 761 NAG A C5 1 HETATM 8907 C C6 . NAG Q 2 . ? -37.817 15.254 48.563 1.00 66.31 ? 761 NAG A C6 1 HETATM 8908 C C7 . NAG Q 2 . ? -40.151 15.220 42.322 1.00 62.51 ? 761 NAG A C7 1 HETATM 8909 C C8 . NAG Q 2 . ? -39.292 14.990 41.089 1.00 62.35 ? 761 NAG A C8 1 HETATM 8910 N N2 . NAG Q 2 . ? -39.661 16.032 43.258 1.00 62.15 ? 761 NAG A N2 1 HETATM 8911 O O3 . NAG Q 2 . ? -41.256 17.004 45.476 1.00 64.02 ? 761 NAG A O3 1 HETATM 8912 O O4 . NAG Q 2 . ? -39.733 17.463 47.881 1.00 63.52 ? 761 NAG A O4 1 HETATM 8913 O O5 . NAG Q 2 . ? -37.906 14.712 46.244 1.00 62.14 ? 761 NAG A O5 1 HETATM 8914 O O6 . NAG Q 2 . ? -38.375 13.959 48.759 1.00 68.12 ? 761 NAG A O6 1 HETATM 8915 O O7 . NAG Q 2 . ? -41.240 14.651 42.427 1.00 62.58 ? 761 NAG A O7 1 HETATM 8916 CU CU . CU R 5 . ? -22.016 -2.861 21.222 1.00 16.90 ? 601 CU A CU 1 HETATM 8917 CU CU . CU S 5 . ? -34.110 -0.373 20.661 1.00 26.02 ? 602 CU A CU 1 HETATM 8918 CU CU . CU T 5 . ? -33.747 1.085 25.501 1.00 15.48 ? 603 CU A CU 1 HETATM 8919 CU CU . CU U 5 . ? -36.184 -1.716 23.924 1.00 47.97 ? 604 CU A CU 1 HETATM 8920 CL CL . CL V 6 . ? -38.376 -3.244 25.362 1.00 49.94 ? 610 CL A CL 1 HETATM 8921 S S . SO4 W 7 . ? -47.187 -24.607 29.024 1.00 84.96 ? 800 SO4 A S 1 HETATM 8922 O O1 . SO4 W 7 . ? -47.736 -24.344 27.682 1.00 84.84 ? 800 SO4 A O1 1 HETATM 8923 O O2 . SO4 W 7 . ? -48.138 -24.132 30.046 1.00 85.10 ? 800 SO4 A O2 1 HETATM 8924 O O3 . SO4 W 7 . ? -45.899 -23.904 29.182 1.00 85.10 ? 800 SO4 A O3 1 HETATM 8925 O O4 . SO4 W 7 . ? -46.975 -26.055 29.184 1.00 85.07 ? 800 SO4 A O4 1 HETATM 8926 S S . SO4 X 7 . ? -51.793 -16.430 20.518 1.00 60.69 ? 802 SO4 A S 1 HETATM 8927 O O1 . SO4 X 7 . ? -51.964 -15.057 21.030 1.00 61.21 ? 802 SO4 A O1 1 HETATM 8928 O O2 . SO4 X 7 . ? -51.608 -16.381 19.062 1.00 59.74 ? 802 SO4 A O2 1 HETATM 8929 O O3 . SO4 X 7 . ? -52.996 -17.230 20.825 1.00 60.51 ? 802 SO4 A O3 1 HETATM 8930 O O4 . SO4 X 7 . ? -50.607 -17.045 21.147 1.00 60.47 ? 802 SO4 A O4 1 HETATM 8931 O O1 . OXY Y 8 . ? -33.553 0.991 22.791 1.00 1.00 ? 900 OXY A O1 1 HETATM 8932 O O2 . OXY Y 8 . ? -34.166 -0.012 23.308 1.00 1.11 ? 900 OXY A O2 1 HETATM 8933 C C1 . NAG Z 2 . ? 26.282 -25.537 24.232 1.00 26.85 ? 700 NAG B C1 1 HETATM 8934 C C2 . NAG Z 2 . ? 27.565 -26.309 23.926 1.00 28.13 ? 700 NAG B C2 1 HETATM 8935 C C3 . NAG Z 2 . ? 27.256 -27.728 23.432 1.00 30.30 ? 700 NAG B C3 1 HETATM 8936 C C4 . NAG Z 2 . ? 26.264 -28.432 24.370 1.00 30.16 ? 700 NAG B C4 1 HETATM 8937 C C5 . NAG Z 2 . ? 25.028 -27.549 24.559 1.00 30.57 ? 700 NAG B C5 1 HETATM 8938 C C6 . NAG Z 2 . ? 23.992 -28.131 25.508 1.00 28.83 ? 700 NAG B C6 1 HETATM 8939 C C7 . NAG Z 2 . ? 29.395 -24.892 23.225 1.00 25.85 ? 700 NAG B C7 1 HETATM 8940 C C8 . NAG Z 2 . ? 30.497 -24.813 22.180 1.00 26.05 ? 700 NAG B C8 1 HETATM 8941 N N2 . NAG Z 2 . ? 28.308 -25.588 22.907 1.00 26.29 ? 700 NAG B N2 1 HETATM 8942 O O3 . NAG Z 2 . ? 28.465 -28.474 23.363 1.00 30.19 ? 700 NAG B O3 1 HETATM 8943 O O4 . NAG Z 2 . ? 25.882 -29.681 23.816 1.00 34.37 ? 700 NAG B O4 1 HETATM 8944 O O5 . NAG Z 2 . ? 25.426 -26.277 25.103 1.00 29.71 ? 700 NAG B O5 1 HETATM 8945 O O6 . NAG Z 2 . ? 24.510 -28.256 26.826 1.00 30.45 ? 700 NAG B O6 1 HETATM 8946 O O7 . NAG Z 2 . ? 29.554 -24.358 24.321 1.00 24.93 ? 700 NAG B O7 1 HETATM 8947 C C1 . NAG AA 2 . ? 13.301 -18.491 14.400 1.00 18.14 ? 710 NAG B C1 1 HETATM 8948 C C2 . NAG AA 2 . ? 12.673 -18.368 13.029 1.00 19.74 ? 710 NAG B C2 1 HETATM 8949 C C3 . NAG AA 2 . ? 11.160 -18.513 13.167 1.00 19.76 ? 710 NAG B C3 1 HETATM 8950 C C4 . NAG AA 2 . ? 10.779 -19.759 13.982 1.00 20.24 ? 710 NAG B C4 1 HETATM 8951 C C5 . NAG AA 2 . ? 11.621 -19.913 15.255 1.00 20.05 ? 710 NAG B C5 1 HETATM 8952 C C6 . NAG AA 2 . ? 11.450 -21.255 15.944 1.00 21.19 ? 710 NAG B C6 1 HETATM 8953 C C7 . NAG AA 2 . ? 13.802 -16.987 11.406 1.00 18.83 ? 710 NAG B C7 1 HETATM 8954 C C8 . NAG AA 2 . ? 13.537 -15.836 10.453 1.00 17.61 ? 710 NAG B C8 1 HETATM 8955 N N2 . NAG AA 2 . ? 13.005 -17.073 12.467 1.00 20.86 ? 710 NAG B N2 1 HETATM 8956 O O3 . NAG AA 2 . ? 10.596 -18.622 11.871 1.00 19.99 ? 710 NAG B O3 1 HETATM 8957 O O4 . NAG AA 2 . ? 9.396 -19.675 14.351 1.00 22.26 ? 710 NAG B O4 1 HETATM 8958 O O5 . NAG AA 2 . ? 13.017 -19.775 14.949 1.00 19.22 ? 710 NAG B O5 1 HETATM 8959 O O6 . NAG AA 2 . ? 11.458 -22.335 15.021 1.00 24.15 ? 710 NAG B O6 1 HETATM 8960 O O7 . NAG AA 2 . ? 14.714 -17.785 11.177 1.00 18.36 ? 710 NAG B O7 1 HETATM 8961 C C1 . NAG BA 2 . ? 8.529 -20.460 13.617 1.00 25.22 ? 711 NAG B C1 1 HETATM 8962 C C2 . NAG BA 2 . ? 7.283 -20.739 14.441 1.00 25.65 ? 711 NAG B C2 1 HETATM 8963 C C3 . NAG BA 2 . ? 6.274 -21.518 13.599 1.00 29.31 ? 711 NAG B C3 1 HETATM 8964 C C4 . NAG BA 2 . ? 6.011 -20.805 12.265 1.00 30.70 ? 711 NAG B C4 1 HETATM 8965 C C5 . NAG BA 2 . ? 7.335 -20.522 11.558 1.00 29.52 ? 711 NAG B C5 1 HETATM 8966 C C6 . NAG BA 2 . ? 7.168 -19.734 10.274 1.00 28.49 ? 711 NAG B C6 1 HETATM 8967 C C7 . NAG BA 2 . ? 7.589 -21.031 16.824 1.00 22.81 ? 711 NAG B C7 1 HETATM 8968 C C8 . NAG BA 2 . ? 7.578 -22.047 17.955 1.00 21.60 ? 711 NAG B C8 1 HETATM 8969 N N2 . NAG BA 2 . ? 7.666 -21.528 15.594 1.00 24.86 ? 711 NAG B N2 1 HETATM 8970 O O3 . NAG BA 2 . ? 5.060 -21.651 14.320 1.00 28.90 ? 711 NAG B O3 1 HETATM 8971 O O4 . NAG BA 2 . ? 5.192 -21.634 11.427 1.00 33.95 ? 711 NAG B O4 1 HETATM 8972 O O5 . NAG BA 2 . ? 8.190 -19.753 12.423 1.00 27.26 ? 711 NAG B O5 1 HETATM 8973 O O6 . NAG BA 2 . ? 6.829 -18.382 10.545 1.00 28.66 ? 711 NAG B O6 1 HETATM 8974 O O7 . NAG BA 2 . ? 7.525 -19.824 17.072 1.00 22.30 ? 711 NAG B O7 1 HETATM 8975 C C1 . BMA CA 3 . ? 3.903 -21.186 11.224 1.00 37.87 ? 712 BMA B C1 1 HETATM 8976 C C2 . BMA CA 3 . ? 3.487 -21.455 9.771 1.00 39.76 ? 712 BMA B C2 1 HETATM 8977 C C3 . BMA CA 3 . ? 2.006 -21.093 9.570 1.00 40.63 ? 712 BMA B C3 1 HETATM 8978 C C4 . BMA CA 3 . ? 1.121 -21.760 10.639 1.00 40.43 ? 712 BMA B C4 1 HETATM 8979 C C5 . BMA CA 3 . ? 1.671 -21.458 12.043 1.00 39.57 ? 712 BMA B C5 1 HETATM 8980 C C6 . BMA CA 3 . ? 0.903 -22.170 13.145 1.00 38.09 ? 712 BMA B C6 1 HETATM 8981 O O2 . BMA CA 3 . ? 3.713 -22.819 9.438 1.00 38.78 ? 712 BMA B O2 1 HETATM 8982 O O3 . BMA CA 3 . ? 1.582 -21.490 8.272 1.00 39.90 ? 712 BMA B O3 1 HETATM 8983 O O4 . BMA CA 3 . ? -0.211 -21.272 10.532 1.00 41.83 ? 712 BMA B O4 1 HETATM 8984 O O5 . BMA CA 3 . ? 3.047 -21.890 12.134 1.00 39.40 ? 712 BMA B O5 1 HETATM 8985 O O6 . BMA CA 3 . ? 1.114 -21.500 14.401 1.00 35.69 ? 712 BMA B O6 1 HETATM 8986 C C1 . NAG DA 2 . ? 11.156 -18.234 52.339 1.00 39.17 ? 720 NAG B C1 1 HETATM 8987 C C2 . NAG DA 2 . ? 10.286 -19.391 52.810 1.00 40.99 ? 720 NAG B C2 1 HETATM 8988 C C3 . NAG DA 2 . ? 10.401 -19.488 54.333 1.00 42.67 ? 720 NAG B C3 1 HETATM 8989 C C4 . NAG DA 2 . ? 11.878 -19.544 54.791 1.00 44.37 ? 720 NAG B C4 1 HETATM 8990 C C5 . NAG DA 2 . ? 12.784 -18.535 54.050 1.00 43.46 ? 720 NAG B C5 1 HETATM 8991 C C6 . NAG DA 2 . ? 14.252 -18.879 54.224 1.00 43.81 ? 720 NAG B C6 1 HETATM 8992 C C7 . NAG DA 2 . ? 8.276 -20.054 51.622 1.00 39.24 ? 720 NAG B C7 1 HETATM 8993 C C8 . NAG DA 2 . ? 6.811 -19.779 51.320 1.00 37.14 ? 720 NAG B C8 1 HETATM 8994 N N2 . NAG DA 2 . ? 8.903 -19.178 52.408 1.00 40.49 ? 720 NAG B N2 1 HETATM 8995 O O3 . NAG DA 2 . ? 9.718 -20.650 54.782 1.00 41.62 ? 720 NAG B O3 1 HETATM 8996 O O4 . NAG DA 2 . ? 11.947 -19.245 56.198 1.00 47.70 ? 720 NAG B O4 1 HETATM 8997 O O5 . NAG DA 2 . ? 12.522 -18.531 52.630 1.00 40.23 ? 720 NAG B O5 1 HETATM 8998 O O6 . NAG DA 2 . ? 15.088 -17.873 53.675 1.00 44.79 ? 720 NAG B O6 1 HETATM 8999 O O7 . NAG DA 2 . ? 8.820 -21.058 51.155 1.00 39.45 ? 720 NAG B O7 1 HETATM 9000 C C1 . NAG EA 2 . ? 12.215 -20.295 57.055 1.00 51.43 ? 721 NAG B C1 1 HETATM 9001 C C2 . NAG EA 2 . ? 12.965 -19.770 58.284 1.00 52.34 ? 721 NAG B C2 1 HETATM 9002 C C3 . NAG EA 2 . ? 13.100 -20.862 59.361 1.00 55.13 ? 721 NAG B C3 1 HETATM 9003 C C4 . NAG EA 2 . ? 11.770 -21.595 59.624 1.00 56.43 ? 721 NAG B C4 1 HETATM 9004 C C5 . NAG EA 2 . ? 11.123 -22.010 58.293 1.00 55.74 ? 721 NAG B C5 1 HETATM 9005 C C6 . NAG EA 2 . ? 9.750 -22.642 58.446 1.00 55.82 ? 721 NAG B C6 1 HETATM 9006 C C7 . NAG EA 2 . ? 14.756 -18.134 58.273 1.00 48.99 ? 721 NAG B C7 1 HETATM 9007 C C8 . NAG EA 2 . ? 16.174 -17.782 57.858 1.00 49.09 ? 721 NAG B C8 1 HETATM 9008 N N2 . NAG EA 2 . ? 14.286 -19.317 57.880 1.00 50.52 ? 721 NAG B N2 1 HETATM 9009 O O3 . NAG EA 2 . ? 13.562 -20.276 60.571 1.00 54.35 ? 721 NAG B O3 1 HETATM 9010 O O4 . NAG EA 2 . ? 12.028 -22.773 60.418 1.00 60.24 ? 721 NAG B O4 1 HETATM 9011 O O5 . NAG EA 2 . ? 10.962 -20.859 57.446 1.00 53.71 ? 721 NAG B O5 1 HETATM 9012 O O6 . NAG EA 2 . ? 9.115 -22.807 57.183 1.00 55.44 ? 721 NAG B O6 1 HETATM 9013 O O7 . NAG EA 2 . ? 14.103 -17.337 58.946 1.00 48.05 ? 721 NAG B O7 1 HETATM 9014 C C1 . BMA FA 3 . ? 11.146 -23.059 61.453 1.00 62.89 ? 722 BMA B C1 1 HETATM 9015 C C2 . BMA FA 3 . ? 11.016 -24.585 61.610 1.00 64.17 ? 722 BMA B C2 1 HETATM 9016 C C3 . BMA FA 3 . ? 10.149 -24.926 62.828 1.00 65.13 ? 722 BMA B C3 1 HETATM 9017 C C4 . BMA FA 3 . ? 10.692 -24.217 64.076 1.00 65.65 ? 722 BMA B C4 1 HETATM 9018 C C5 . BMA FA 3 . ? 10.818 -22.709 63.807 1.00 65.50 ? 722 BMA B C5 1 HETATM 9019 C C6 . BMA FA 3 . ? 11.405 -21.928 64.977 1.00 66.03 ? 722 BMA B C6 1 HETATM 9020 O O2 . BMA FA 3 . ? 12.302 -25.174 61.754 1.00 65.14 ? 722 BMA B O2 1 HETATM 9021 O O3 . BMA FA 3 . ? 10.134 -26.334 63.034 1.00 64.41 ? 722 BMA B O3 1 HETATM 9022 O O4 . BMA FA 3 . ? 9.817 -24.438 65.174 1.00 66.22 ? 722 BMA B O4 1 HETATM 9023 O O5 . BMA FA 3 . ? 11.667 -22.474 62.659 1.00 63.73 ? 722 BMA B O5 1 HETATM 9024 O O6 . BMA FA 3 . ? 12.626 -22.497 65.434 1.00 66.59 ? 722 BMA B O6 1 HETATM 9025 C C1 . NAG GA 2 . ? -0.967 -9.431 46.246 1.00 17.42 ? 730 NAG B C1 1 HETATM 9026 C C2 . NAG GA 2 . ? -2.443 -9.018 46.155 1.00 19.30 ? 730 NAG B C2 1 HETATM 9027 C C3 . NAG GA 2 . ? -3.338 -9.961 46.957 1.00 20.86 ? 730 NAG B C3 1 HETATM 9028 C C4 . NAG GA 2 . ? -3.041 -11.425 46.633 1.00 20.51 ? 730 NAG B C4 1 HETATM 9029 C C5 . NAG GA 2 . ? -1.546 -11.687 46.777 1.00 18.86 ? 730 NAG B C5 1 HETATM 9030 C C6 . NAG GA 2 . ? -1.136 -13.111 46.445 1.00 14.59 ? 730 NAG B C6 1 HETATM 9031 C C7 . NAG GA 2 . ? -3.002 -6.690 45.886 1.00 18.15 ? 730 NAG B C7 1 HETATM 9032 C C8 . NAG GA 2 . ? -3.443 -5.398 46.561 1.00 17.09 ? 730 NAG B C8 1 HETATM 9033 N N2 . NAG GA 2 . ? -2.596 -7.675 46.676 1.00 17.62 ? 730 NAG B N2 1 HETATM 9034 O O3 . NAG GA 2 . ? -4.695 -9.677 46.659 1.00 23.72 ? 730 NAG B O3 1 HETATM 9035 O O4 . NAG GA 2 . ? -3.766 -12.269 47.543 1.00 24.67 ? 730 NAG B O4 1 HETATM 9036 O O5 . NAG GA 2 . ? -0.818 -10.812 45.895 1.00 19.74 ? 730 NAG B O5 1 HETATM 9037 O O6 . NAG GA 2 . ? -1.246 -13.370 45.056 1.00 12.90 ? 730 NAG B O6 1 HETATM 9038 O O7 . NAG GA 2 . ? -3.014 -6.779 44.662 1.00 19.81 ? 730 NAG B O7 1 HETATM 9039 C C1 . NAG HA 2 . ? -4.841 -12.957 47.012 1.00 29.00 ? 731 NAG B C1 1 HETATM 9040 C C2 . NAG HA 2 . ? -5.137 -14.180 47.866 1.00 31.95 ? 731 NAG B C2 1 HETATM 9041 C C3 . NAG HA 2 . ? -6.299 -14.934 47.224 1.00 34.11 ? 731 NAG B C3 1 HETATM 9042 C C4 . NAG HA 2 . ? -7.522 -14.014 47.085 1.00 35.80 ? 731 NAG B C4 1 HETATM 9043 C C5 . NAG HA 2 . ? -7.154 -12.678 46.398 1.00 33.21 ? 731 NAG B C5 1 HETATM 9044 C C6 . NAG HA 2 . ? -8.285 -11.664 46.525 1.00 31.91 ? 731 NAG B C6 1 HETATM 9045 C C7 . NAG HA 2 . ? -3.603 -15.580 49.116 1.00 34.17 ? 731 NAG B C7 1 HETATM 9046 C C8 . NAG HA 2 . ? -2.675 -16.783 49.039 1.00 34.80 ? 731 NAG B C8 1 HETATM 9047 N N2 . NAG HA 2 . ? -3.956 -15.023 47.957 1.00 33.47 ? 731 NAG B N2 1 HETATM 9048 O O3 . NAG HA 2 . ? -6.636 -16.061 48.016 1.00 33.85 ? 731 NAG B O3 1 HETATM 9049 O O4 . NAG HA 2 . ? -8.537 -14.688 46.308 1.00 40.23 ? 731 NAG B O4 1 HETATM 9050 O O5 . NAG HA 2 . ? -5.979 -12.084 47.008 1.00 31.50 ? 731 NAG B O5 1 HETATM 9051 O O6 . NAG HA 2 . ? -7.849 -10.339 46.258 1.00 29.08 ? 731 NAG B O6 1 HETATM 9052 O O7 . NAG HA 2 . ? -4.002 -15.178 50.216 1.00 34.33 ? 731 NAG B O7 1 HETATM 9053 C C1 . BMA IA 3 . ? -9.850 -14.481 46.698 1.00 43.44 ? 732 BMA B C1 1 HETATM 9054 C C2 . BMA IA 3 . ? -10.804 -14.728 45.522 1.00 44.95 ? 732 BMA B C2 1 HETATM 9055 C C3 . BMA IA 3 . ? -12.243 -14.492 45.996 1.00 45.18 ? 732 BMA B C3 1 HETATM 9056 C C4 . BMA IA 3 . ? -12.553 -15.348 47.240 1.00 45.48 ? 732 BMA B C4 1 HETATM 9057 C C5 . BMA IA 3 . ? -11.476 -15.135 48.320 1.00 45.70 ? 732 BMA B C5 1 HETATM 9058 C C6 . BMA IA 3 . ? -11.640 -16.054 49.516 1.00 46.43 ? 732 BMA B C6 1 HETATM 9059 O O2 . BMA IA 3 . ? -10.656 -16.061 45.043 1.00 43.89 ? 732 BMA B O2 1 HETATM 9060 O O3 . BMA IA 3 . ? -13.154 -14.797 44.948 1.00 44.99 ? 732 BMA B O3 1 HETATM 9061 O O4 . BMA IA 3 . ? -13.826 -14.992 47.765 1.00 44.93 ? 732 BMA B O4 1 HETATM 9062 O O5 . BMA IA 3 . ? -10.158 -15.378 47.775 1.00 44.08 ? 732 BMA B O5 1 HETATM 9063 O O6 . BMA IA 3 . ? -11.173 -15.434 50.705 1.00 46.61 ? 732 BMA B O6 1 HETATM 9064 C C1 . NAG JA 2 . ? 9.826 13.480 8.562 1.00 36.07 ? 740 NAG B C1 1 HETATM 9065 C C2 . NAG JA 2 . ? 11.217 14.060 8.742 1.00 38.59 ? 740 NAG B C2 1 HETATM 9066 C C3 . NAG JA 2 . ? 11.259 15.464 8.140 1.00 41.08 ? 740 NAG B C3 1 HETATM 9067 C C4 . NAG JA 2 . ? 10.709 15.502 6.699 1.00 42.61 ? 740 NAG B C4 1 HETATM 9068 C C5 . NAG JA 2 . ? 9.426 14.658 6.528 1.00 40.60 ? 740 NAG B C5 1 HETATM 9069 C C6 . NAG JA 2 . ? 9.135 14.381 5.065 1.00 40.39 ? 740 NAG B C6 1 HETATM 9070 C C7 . NAG JA 2 . ? 12.573 13.377 10.614 1.00 41.05 ? 740 NAG B C7 1 HETATM 9071 C C8 . NAG JA 2 . ? 13.522 14.063 11.579 1.00 42.96 ? 740 NAG B C8 1 HETATM 9072 N N2 . NAG JA 2 . ? 11.557 14.100 10.152 1.00 40.20 ? 740 NAG B N2 1 HETATM 9073 O O3 . NAG JA 2 . ? 12.601 15.921 8.132 1.00 41.11 ? 740 NAG B O3 1 HETATM 9074 O O4 . NAG JA 2 . ? 10.398 16.871 6.352 1.00 46.52 ? 740 NAG B O4 1 HETATM 9075 O O5 . NAG JA 2 . ? 9.548 13.371 7.169 1.00 38.07 ? 740 NAG B O5 1 HETATM 9076 O O6 . NAG JA 2 . ? 10.065 13.452 4.522 1.00 39.92 ? 740 NAG B O6 1 HETATM 9077 O O7 . NAG JA 2 . ? 12.774 12.206 10.283 1.00 40.74 ? 740 NAG B O7 1 HETATM 9078 C C1 . NAG KA 2 . ? 11.237 17.548 5.477 1.00 49.28 ? 741 NAG B C1 1 HETATM 9079 C C2 . NAG KA 2 . ? 10.513 18.803 4.963 1.00 50.15 ? 741 NAG B C2 1 HETATM 9080 C C3 . NAG KA 2 . ? 11.458 19.675 4.121 1.00 51.12 ? 741 NAG B C3 1 HETATM 9081 C C4 . NAG KA 2 . ? 12.759 19.954 4.883 1.00 52.00 ? 741 NAG B C4 1 HETATM 9082 C C5 . NAG KA 2 . ? 13.373 18.638 5.386 1.00 51.47 ? 741 NAG B C5 1 HETATM 9083 C C6 . NAG KA 2 . ? 14.602 18.858 6.246 1.00 51.68 ? 741 NAG B C6 1 HETATM 9084 C C7 . NAG KA 2 . ? 8.207 19.054 4.294 1.00 50.20 ? 741 NAG B C7 1 HETATM 9085 C C8 . NAG KA 2 . ? 7.705 19.793 3.064 1.00 50.82 ? 741 NAG B C8 1 HETATM 9086 N N2 . NAG KA 2 . ? 9.361 18.406 4.174 1.00 50.38 ? 741 NAG B N2 1 HETATM 9087 O O3 . NAG KA 2 . ? 10.823 20.909 3.805 1.00 51.02 ? 741 NAG B O3 1 HETATM 9088 O O4 . NAG KA 2 . ? 13.680 20.628 4.032 1.00 51.93 ? 741 NAG B O4 1 HETATM 9089 O O5 . NAG KA 2 . ? 12.418 17.922 6.199 1.00 50.61 ? 741 NAG B O5 1 HETATM 9090 O O6 . NAG KA 2 . ? 15.271 17.632 6.505 1.00 52.21 ? 741 NAG B O6 1 HETATM 9091 O O7 . NAG KA 2 . ? 7.561 19.089 5.343 1.00 49.57 ? 741 NAG B O7 1 HETATM 9092 C C1 . NAG LA 2 . ? 24.791 1.458 -1.765 1.00 22.20 ? 750 NAG B C1 1 HETATM 9093 C C2 . NAG LA 2 . ? 25.552 1.199 -3.082 1.00 22.98 ? 750 NAG B C2 1 HETATM 9094 C C3 . NAG LA 2 . ? 24.603 0.691 -4.177 1.00 21.40 ? 750 NAG B C3 1 HETATM 9095 C C4 . NAG LA 2 . ? 23.786 -0.499 -3.656 1.00 22.12 ? 750 NAG B C4 1 HETATM 9096 C C5 . NAG LA 2 . ? 23.070 -0.097 -2.362 1.00 22.36 ? 750 NAG B C5 1 HETATM 9097 C C6 . NAG LA 2 . ? 22.243 -1.213 -1.743 1.00 19.85 ? 750 NAG B C6 1 HETATM 9098 C C7 . NAG LA 2 . ? 27.519 2.614 -3.292 1.00 26.33 ? 750 NAG B C7 1 HETATM 9099 C C8 . NAG LA 2 . ? 27.988 4.063 -3.241 1.00 25.52 ? 750 NAG B C8 1 HETATM 9100 N N2 . NAG LA 2 . ? 26.222 2.413 -3.533 1.00 25.20 ? 750 NAG B N2 1 HETATM 9101 O O3 . NAG LA 2 . ? 25.366 0.296 -5.308 1.00 22.15 ? 750 NAG B O3 1 HETATM 9102 O O4 . NAG LA 2 . ? 22.834 -0.914 -4.623 1.00 22.06 ? 750 NAG B O4 1 HETATM 9103 O O5 . NAG LA 2 . ? 24.039 0.301 -1.380 1.00 21.01 ? 750 NAG B O5 1 HETATM 9104 O O6 . NAG LA 2 . ? 22.973 -2.432 -1.685 1.00 22.84 ? 750 NAG B O6 1 HETATM 9105 O O7 . NAG LA 2 . ? 28.322 1.696 -3.072 1.00 26.78 ? 750 NAG B O7 1 HETATM 9106 C C1 . NAG MA 2 . ? 16.847 -14.169 42.941 1.00 42.31 ? 760 NAG B C1 1 HETATM 9107 C C2 . NAG MA 2 . ? 17.228 -13.865 44.406 1.00 43.93 ? 760 NAG B C2 1 HETATM 9108 C C3 . NAG MA 2 . ? 18.636 -14.389 44.729 1.00 45.48 ? 760 NAG B C3 1 HETATM 9109 C C4 . NAG MA 2 . ? 18.765 -15.866 44.338 1.00 45.53 ? 760 NAG B C4 1 HETATM 9110 C C5 . NAG MA 2 . ? 18.375 -16.023 42.866 1.00 46.72 ? 760 NAG B C5 1 HETATM 9111 C C6 . NAG MA 2 . ? 18.448 -17.460 42.385 1.00 48.80 ? 760 NAG B C6 1 HETATM 9112 C C7 . NAG MA 2 . ? 16.398 -11.940 45.589 1.00 44.72 ? 760 NAG B C7 1 HETATM 9113 C C8 . NAG MA 2 . ? 17.033 -11.628 46.935 1.00 46.33 ? 760 NAG B C8 1 HETATM 9114 N N2 . NAG MA 2 . ? 17.182 -12.435 44.640 1.00 44.32 ? 760 NAG B N2 1 HETATM 9115 O O3 . NAG MA 2 . ? 18.898 -14.233 46.118 1.00 47.03 ? 760 NAG B O3 1 HETATM 9116 O O4 . NAG MA 2 . ? 20.100 -16.316 44.541 1.00 44.01 ? 760 NAG B O4 1 HETATM 9117 O O5 . NAG MA 2 . ? 17.015 -15.569 42.663 1.00 44.38 ? 760 NAG B O5 1 HETATM 9118 O O6 . NAG MA 2 . ? 19.294 -17.578 41.250 1.00 51.55 ? 760 NAG B O6 1 HETATM 9119 O O7 . NAG MA 2 . ? 15.203 -11.737 45.417 1.00 45.82 ? 760 NAG B O7 1 HETATM 9120 C C1 . NAG NA 2 . ? 1.080 -3.730 58.489 1.00 49.70 ? 770 NAG B C1 1 HETATM 9121 C C2 . NAG NA 2 . ? -0.330 -3.250 58.922 1.00 51.04 ? 770 NAG B C2 1 HETATM 9122 C C3 . NAG NA 2 . ? -0.460 -3.182 60.459 1.00 53.69 ? 770 NAG B C3 1 HETATM 9123 C C4 . NAG NA 2 . ? 0.025 -4.482 61.099 1.00 54.73 ? 770 NAG B C4 1 HETATM 9124 C C5 . NAG NA 2 . ? 1.460 -4.738 60.646 1.00 54.27 ? 770 NAG B C5 1 HETATM 9125 C C6 . NAG NA 2 . ? 2.097 -5.976 61.264 1.00 55.84 ? 770 NAG B C6 1 HETATM 9126 C C7 . NAG NA 2 . ? -1.798 -1.594 57.933 1.00 51.54 ? 770 NAG B C7 1 HETATM 9127 C C8 . NAG NA 2 . ? -2.015 -1.513 56.430 1.00 52.09 ? 770 NAG B C8 1 HETATM 9128 N N2 . NAG NA 2 . ? -0.585 -1.931 58.364 1.00 51.06 ? 770 NAG B N2 1 HETATM 9129 O O3 . NAG NA 2 . ? -1.815 -2.955 60.823 1.00 54.43 ? 770 NAG B O3 1 HETATM 9130 O O4 . NAG NA 2 . ? -0.036 -4.388 62.516 1.00 56.13 ? 770 NAG B O4 1 HETATM 9131 O O5 . NAG NA 2 . ? 1.484 -4.908 59.215 1.00 53.00 ? 770 NAG B O5 1 HETATM 9132 O O6 . NAG NA 2 . ? 1.171 -7.049 61.388 1.00 56.83 ? 770 NAG B O6 1 HETATM 9133 O O7 . NAG NA 2 . ? -2.730 -1.343 58.697 1.00 51.34 ? 770 NAG B O7 1 HETATM 9134 CU CU . CU OA 5 . ? 4.449 0.578 21.312 1.00 14.39 ? 601 CU B CU 1 HETATM 9135 CU CU . CU PA 5 . ? 16.496 -1.838 20.741 1.00 22.95 ? 602 CU B CU 1 HETATM 9136 CU CU . CU QA 5 . ? 16.134 -3.432 25.636 1.00 25.91 ? 603 CU B CU 1 HETATM 9137 CU CU . CU RA 5 . ? 18.803 -0.288 24.107 1.00 58.09 ? 604 CU B CU 1 HETATM 9138 S S . SO4 SA 7 . ? 29.910 22.190 28.963 1.00 77.95 ? 801 SO4 B S 1 HETATM 9139 O O1 . SO4 SA 7 . ? 30.077 22.722 27.595 1.00 77.51 ? 801 SO4 B O1 1 HETATM 9140 O O2 . SO4 SA 7 . ? 29.594 23.290 29.893 1.00 77.66 ? 801 SO4 B O2 1 HETATM 9141 O O3 . SO4 SA 7 . ? 31.157 21.532 29.393 1.00 77.89 ? 801 SO4 B O3 1 HETATM 9142 O O4 . SO4 SA 7 . ? 28.809 21.208 28.978 1.00 77.90 ? 801 SO4 B O4 1 HETATM 9143 O O1 . OXY TA 8 . ? 16.028 -3.195 22.755 1.00 9.88 ? 901 OXY B O1 1 HETATM 9144 O O2 . OXY TA 8 . ? 16.348 -2.094 23.337 1.00 8.29 ? 901 OXY B O2 1 HETATM 9145 C C1 . GOL UA 9 . ? -10.157 0.283 19.836 1.00 43.77 ? 810 GOL B C1 1 HETATM 9146 O O1 . GOL UA 9 . ? -11.217 0.834 19.047 1.00 45.64 ? 810 GOL B O1 1 HETATM 9147 C C2 . GOL UA 9 . ? -9.454 -0.802 19.023 1.00 43.66 ? 810 GOL B C2 1 HETATM 9148 O O2 . GOL UA 9 . ? -8.948 -0.279 17.787 1.00 42.34 ? 810 GOL B O2 1 HETATM 9149 C C3 . GOL UA 9 . ? -8.334 -1.442 19.825 1.00 42.34 ? 810 GOL B C3 1 HETATM 9150 O O3 . GOL UA 9 . ? -7.715 -2.450 19.022 1.00 41.84 ? 810 GOL B O3 1 HETATM 9151 O O . HOH VA 10 . ? -39.591 -8.204 43.354 1.00 1.00 ? 901 HOH A O 1 HETATM 9152 O O . HOH VA 10 . ? -16.069 3.574 17.766 1.00 23.47 ? 902 HOH A O 1 HETATM 9153 O O . HOH VA 10 . ? -39.457 20.660 26.500 1.00 2.40 ? 903 HOH A O 1 HETATM 9154 O O . HOH VA 10 . ? -14.382 4.852 41.989 1.00 16.62 ? 904 HOH A O 1 HETATM 9155 O O . HOH VA 10 . ? -8.280 -11.643 13.647 1.00 2.12 ? 905 HOH A O 1 HETATM 9156 O O . HOH VA 10 . ? -18.157 -2.037 25.253 1.00 3.54 ? 906 HOH A O 1 HETATM 9157 O O . HOH VA 10 . ? -12.588 -12.295 34.906 1.00 9.44 ? 907 HOH A O 1 HETATM 9158 O O . HOH VA 10 . ? -35.498 -3.458 9.906 1.00 1.00 ? 908 HOH A O 1 HETATM 9159 O O . HOH VA 10 . ? -17.301 -3.698 34.822 1.00 6.43 ? 909 HOH A O 1 HETATM 9160 O O . HOH VA 10 . ? -29.393 10.978 36.208 1.00 4.89 ? 910 HOH A O 1 HETATM 9161 O O . HOH VA 10 . ? -39.853 16.955 32.583 1.00 14.41 ? 911 HOH A O 1 HETATM 9162 O O . HOH VA 10 . ? -16.785 -9.152 28.062 1.00 4.96 ? 912 HOH A O 1 HETATM 9163 O O . HOH VA 10 . ? -36.783 -18.043 33.624 1.00 6.81 ? 913 HOH A O 1 HETATM 9164 O O . HOH VA 10 . ? -48.983 3.701 41.247 1.00 20.22 ? 914 HOH A O 1 HETATM 9165 O O . HOH VA 10 . ? -24.572 19.910 23.595 1.00 1.00 ? 915 HOH A O 1 HETATM 9166 O O . HOH VA 10 . ? -41.278 -12.043 27.319 1.00 5.81 ? 916 HOH A O 1 HETATM 9167 O O . HOH VA 10 . ? -18.056 -16.983 19.682 1.00 3.22 ? 917 HOH A O 1 HETATM 9168 O O . HOH VA 10 . ? -45.751 5.833 11.385 1.00 1.00 ? 918 HOH A O 1 HETATM 9169 O O . HOH VA 10 . ? -52.741 -1.690 49.605 1.00 25.99 ? 919 HOH A O 1 HETATM 9170 O O . HOH VA 10 . ? -43.400 -7.727 36.262 1.00 4.63 ? 920 HOH A O 1 HETATM 9171 O O . HOH VA 10 . ? -47.105 -6.123 27.476 1.00 7.13 ? 921 HOH A O 1 HETATM 9172 O O . HOH VA 10 . ? -25.298 -7.508 37.139 1.00 20.14 ? 922 HOH A O 1 HETATM 9173 O O . HOH VA 10 . ? -40.853 6.698 37.242 1.00 6.75 ? 923 HOH A O 1 HETATM 9174 O O . HOH VA 10 . ? -23.687 -7.562 39.122 1.00 1.00 ? 924 HOH A O 1 HETATM 9175 O O . HOH VA 10 . ? -34.754 -21.324 40.637 1.00 20.09 ? 925 HOH A O 1 HETATM 9176 O O . HOH VA 10 . ? -27.807 15.798 18.540 1.00 4.16 ? 926 HOH A O 1 HETATM 9177 O O . HOH VA 10 . ? -33.479 18.669 16.022 1.00 13.93 ? 927 HOH A O 1 HETATM 9178 O O . HOH VA 10 . ? -52.824 -14.277 28.009 1.00 9.48 ? 928 HOH A O 1 HETATM 9179 O O . HOH VA 10 . ? -15.602 -6.513 17.332 1.00 25.34 ? 929 HOH A O 1 HETATM 9180 O O . HOH VA 10 . ? -45.571 -16.236 10.075 1.00 14.77 ? 930 HOH A O 1 HETATM 9181 O O . HOH VA 10 . ? -50.061 3.492 15.183 1.00 6.46 ? 931 HOH A O 1 HETATM 9182 O O . HOH VA 10 . ? -46.404 6.086 14.513 1.00 18.74 ? 932 HOH A O 1 HETATM 9183 O O . HOH VA 10 . ? -30.137 14.314 17.702 1.00 11.68 ? 933 HOH A O 1 HETATM 9184 O O . HOH VA 10 . ? -25.305 10.220 27.565 1.00 12.77 ? 934 HOH A O 1 HETATM 9185 O O . HOH VA 10 . ? -21.335 5.185 15.603 1.00 15.90 ? 935 HOH A O 1 HETATM 9186 O O . HOH VA 10 . ? -49.890 -8.725 33.760 1.00 13.55 ? 936 HOH A O 1 HETATM 9187 O O . HOH VA 10 . ? -35.128 -3.901 38.151 1.00 3.08 ? 937 HOH A O 1 HETATM 9188 O O . HOH VA 10 . ? -57.834 -2.069 33.095 1.00 18.56 ? 938 HOH A O 1 HETATM 9189 O O . HOH VA 10 . ? -15.566 -0.678 31.383 1.00 10.85 ? 939 HOH A O 1 HETATM 9190 O O . HOH VA 10 . ? -5.385 -13.705 26.891 1.00 11.52 ? 940 HOH A O 1 HETATM 9191 O O . HOH VA 10 . ? -18.928 6.774 53.035 1.00 16.93 ? 941 HOH A O 1 HETATM 9192 O O . HOH VA 10 . ? -33.915 -8.679 5.390 1.00 7.48 ? 942 HOH A O 1 HETATM 9193 O O . HOH VA 10 . ? -34.030 -20.173 15.799 1.00 26.08 ? 943 HOH A O 1 HETATM 9194 O O . HOH VA 10 . ? -19.683 2.570 14.839 1.00 4.26 ? 944 HOH A O 1 HETATM 9195 O O . HOH VA 10 . ? -11.696 -9.627 22.888 1.00 14.56 ? 945 HOH A O 1 HETATM 9196 O O . HOH VA 10 . ? -35.945 15.419 28.961 1.00 14.40 ? 946 HOH A O 1 HETATM 9197 O O . HOH VA 10 . ? -11.907 -8.026 41.880 1.00 18.53 ? 947 HOH A O 1 HETATM 9198 O O . HOH VA 10 . ? -23.518 -1.835 48.372 1.00 6.70 ? 948 HOH A O 1 HETATM 9199 O O . HOH VA 10 . ? -24.350 12.670 42.415 1.00 20.30 ? 949 HOH A O 1 HETATM 9200 O O . HOH VA 10 . ? -47.874 -3.953 57.543 1.00 17.19 ? 950 HOH A O 1 HETATM 9201 O O . HOH VA 10 . ? -17.593 -1.061 34.095 1.00 26.04 ? 951 HOH A O 1 HETATM 9202 O O . HOH VA 10 . ? -55.008 1.671 39.366 1.00 2.89 ? 952 HOH A O 1 HETATM 9203 O O . HOH VA 10 . ? -41.612 -16.041 28.922 1.00 23.07 ? 953 HOH A O 1 HETATM 9204 O O . HOH VA 10 . ? -31.622 3.946 20.369 1.00 19.44 ? 954 HOH A O 1 HETATM 9205 O O . HOH VA 10 . ? -29.007 -13.896 48.999 1.00 15.17 ? 955 HOH A O 1 HETATM 9206 O O . HOH VA 10 . ? -19.593 -18.987 19.207 1.00 8.70 ? 956 HOH A O 1 HETATM 9207 O O . HOH VA 10 . ? -44.774 -8.129 4.601 1.00 20.60 ? 957 HOH A O 1 HETATM 9208 O O . HOH VA 10 . ? -58.069 -3.207 50.895 1.00 26.59 ? 958 HOH A O 1 HETATM 9209 O O . HOH VA 10 . ? -38.595 -3.039 17.494 1.00 24.95 ? 959 HOH A O 1 HETATM 9210 O O . HOH VA 10 . ? -32.202 8.065 20.640 1.00 17.96 ? 960 HOH A O 1 HETATM 9211 O O . HOH VA 10 . ? -12.701 -7.024 15.155 1.00 3.84 ? 961 HOH A O 1 HETATM 9212 O O . HOH VA 10 . ? -18.047 -6.371 45.872 1.00 12.62 ? 962 HOH A O 1 HETATM 9213 O O . HOH VA 10 . ? -42.871 -2.145 41.072 1.00 10.01 ? 963 HOH A O 1 HETATM 9214 O O . HOH VA 10 . ? -31.690 20.942 14.789 1.00 1.52 ? 964 HOH A O 1 HETATM 9215 O O . HOH VA 10 . ? -57.457 -4.056 43.824 1.00 27.20 ? 965 HOH A O 1 HETATM 9216 O O . HOH VA 10 . ? -41.859 -13.799 25.427 1.00 20.85 ? 966 HOH A O 1 HETATM 9217 O O . HOH VA 10 . ? -8.636 -16.278 31.916 1.00 8.37 ? 967 HOH A O 1 HETATM 9218 O O . HOH VA 10 . ? -17.091 27.671 40.854 1.00 18.49 ? 968 HOH A O 1 HETATM 9219 O O . HOH VA 10 . ? -15.240 -13.418 13.600 1.00 12.48 ? 969 HOH A O 1 HETATM 9220 O O . HOH VA 10 . ? -35.866 19.589 -1.534 1.00 22.88 ? 970 HOH A O 1 HETATM 9221 O O . HOH VA 10 . ? -47.375 3.060 14.469 1.00 13.71 ? 971 HOH A O 1 HETATM 9222 O O . HOH VA 10 . ? -32.972 -19.029 43.546 1.00 15.86 ? 972 HOH A O 1 HETATM 9223 O O . HOH VA 10 . ? -31.218 14.969 45.325 1.00 20.70 ? 973 HOH A O 1 HETATM 9224 O O . HOH VA 10 . ? -18.869 6.846 25.193 1.00 9.21 ? 974 HOH A O 1 HETATM 9225 O O . HOH VA 10 . ? -21.064 -30.104 26.982 1.00 13.17 ? 975 HOH A O 1 HETATM 9226 O O . HOH VA 10 . ? -16.606 1.093 20.427 1.00 12.89 ? 976 HOH A O 1 HETATM 9227 O O . HOH VA 10 . ? -30.712 25.256 33.595 1.00 22.98 ? 977 HOH A O 1 HETATM 9228 O O . HOH VA 10 . ? -18.001 15.512 25.370 1.00 5.80 ? 978 HOH A O 1 HETATM 9229 O O . HOH VA 10 . ? -34.732 14.541 11.105 1.00 3.17 ? 979 HOH A O 1 HETATM 9230 O O . HOH VA 10 . ? -14.817 10.228 51.794 1.00 13.40 ? 980 HOH A O 1 HETATM 9231 O O . HOH VA 10 . ? -49.534 -3.204 25.432 1.00 8.86 ? 981 HOH A O 1 HETATM 9232 O O . HOH VA 10 . ? -49.111 15.446 13.881 1.00 1.28 ? 982 HOH A O 1 HETATM 9233 O O . HOH VA 10 . ? -30.526 12.747 30.538 1.00 31.81 ? 983 HOH A O 1 HETATM 9234 O O . HOH VA 10 . ? -54.381 7.954 8.126 1.00 20.97 ? 984 HOH A O 1 HETATM 9235 O O . HOH VA 10 . ? -51.502 -16.946 37.000 1.00 15.13 ? 985 HOH A O 1 HETATM 9236 O O . HOH VA 10 . ? -46.722 12.886 2.290 1.00 7.31 ? 986 HOH A O 1 HETATM 9237 O O . HOH VA 10 . ? -32.267 -14.441 42.438 1.00 5.16 ? 987 HOH A O 1 HETATM 9238 O O . HOH VA 10 . ? -20.981 -10.451 10.581 1.00 33.17 ? 988 HOH A O 1 HETATM 9239 O O . HOH VA 10 . ? -17.723 9.952 10.280 1.00 21.44 ? 989 HOH A O 1 HETATM 9240 O O . HOH VA 10 . ? -44.799 -13.041 27.360 1.00 12.58 ? 990 HOH A O 1 HETATM 9241 O O . HOH VA 10 . ? -49.560 -8.860 17.625 1.00 22.82 ? 991 HOH A O 1 HETATM 9242 O O . HOH VA 10 . ? -24.013 -8.527 41.870 1.00 35.10 ? 992 HOH A O 1 HETATM 9243 O O . HOH VA 10 . ? -43.693 -9.021 -2.118 1.00 8.12 ? 993 HOH A O 1 HETATM 9244 O O . HOH VA 10 . ? -40.134 -6.210 39.399 1.00 10.34 ? 994 HOH A O 1 HETATM 9245 O O . HOH VA 10 . ? -8.615 12.596 50.761 1.00 24.19 ? 995 HOH A O 1 HETATM 9246 O O . HOH VA 10 . ? -43.828 19.946 4.558 1.00 27.89 ? 996 HOH A O 1 HETATM 9247 O O . HOH VA 10 . ? -16.488 5.553 27.884 1.00 10.22 ? 997 HOH A O 1 HETATM 9248 O O . HOH VA 10 . ? -46.210 2.222 51.533 1.00 26.56 ? 998 HOH A O 1 HETATM 9249 O O . HOH VA 10 . ? -10.370 -1.857 27.439 1.00 24.16 ? 999 HOH A O 1 HETATM 9250 O O . HOH VA 10 . ? -41.149 -13.600 38.479 1.00 46.93 ? 1000 HOH A O 1 HETATM 9251 O O . HOH VA 10 . ? -44.645 -4.337 46.538 1.00 3.47 ? 1001 HOH A O 1 HETATM 9252 O O . HOH VA 10 . ? -44.855 -19.404 39.796 1.00 25.60 ? 1002 HOH A O 1 HETATM 9253 O O . HOH VA 10 . ? -14.607 13.160 41.686 1.00 11.93 ? 1003 HOH A O 1 HETATM 9254 O O . HOH VA 10 . ? -33.720 26.081 19.615 1.00 17.21 ? 1004 HOH A O 1 HETATM 9255 O O . HOH VA 10 . ? -36.655 21.540 9.632 1.00 25.04 ? 1005 HOH A O 1 HETATM 9256 O O . HOH VA 10 . ? -31.217 15.533 4.006 1.00 10.59 ? 1006 HOH A O 1 HETATM 9257 O O . HOH VA 10 . ? -42.135 17.574 0.561 1.00 6.97 ? 1007 HOH A O 1 HETATM 9258 O O . HOH VA 10 . ? -18.249 18.021 54.647 1.00 14.39 ? 1008 HOH A O 1 HETATM 9259 O O . HOH VA 10 . ? -13.852 18.870 20.154 1.00 17.06 ? 1009 HOH A O 1 HETATM 9260 O O . HOH VA 10 . ? -15.872 -0.987 55.223 1.00 16.70 ? 1010 HOH A O 1 HETATM 9261 O O . HOH VA 10 . ? -34.448 -27.418 18.476 1.00 36.86 ? 1011 HOH A O 1 HETATM 9262 O O . HOH VA 10 . ? -28.939 10.922 17.224 1.00 20.70 ? 1012 HOH A O 1 HETATM 9263 O O . HOH VA 10 . ? -39.343 -20.124 10.772 1.00 25.28 ? 1013 HOH A O 1 HETATM 9264 O O . HOH VA 10 . ? -43.331 -3.588 43.012 1.00 17.49 ? 1014 HOH A O 1 HETATM 9265 O O . HOH VA 10 . ? -47.009 -11.902 39.533 1.00 11.71 ? 1015 HOH A O 1 HETATM 9266 O O . HOH VA 10 . ? -19.643 26.598 30.110 1.00 26.50 ? 1016 HOH A O 1 HETATM 9267 O O . HOH VA 10 . ? -29.640 9.892 30.055 1.00 11.00 ? 1017 HOH A O 1 HETATM 9268 O O . HOH VA 10 . ? -37.511 24.247 19.996 1.00 9.95 ? 1018 HOH A O 1 HETATM 9269 O O . HOH VA 10 . ? -47.374 -11.825 2.203 1.00 20.79 ? 1019 HOH A O 1 HETATM 9270 O O . HOH VA 10 . ? -13.853 3.997 38.484 1.00 20.13 ? 1020 HOH A O 1 HETATM 9271 O O . HOH VA 10 . ? -60.191 -7.594 48.270 1.00 11.58 ? 1021 HOH A O 1 HETATM 9272 O O . HOH VA 10 . ? -40.205 -3.435 23.420 1.00 20.77 ? 1022 HOH A O 1 HETATM 9273 O O . HOH VA 10 . ? -21.738 19.022 20.388 1.00 2.41 ? 1023 HOH A O 1 HETATM 9274 O O . HOH VA 10 . ? -34.363 -12.552 36.095 1.00 1.00 ? 1024 HOH A O 1 HETATM 9275 O O . HOH VA 10 . ? -11.671 7.038 53.878 1.00 22.08 ? 1025 HOH A O 1 HETATM 9276 O O . HOH VA 10 . ? -59.483 -7.322 45.505 1.00 18.39 ? 1026 HOH A O 1 HETATM 9277 O O . HOH VA 10 . ? -24.883 13.204 27.647 1.00 16.23 ? 1027 HOH A O 1 HETATM 9278 O O . HOH VA 10 . ? -18.919 -2.853 56.212 1.00 29.95 ? 1028 HOH A O 1 HETATM 9279 O O . HOH VA 10 . ? -14.939 7.468 58.476 1.00 20.87 ? 1029 HOH A O 1 HETATM 9280 O O . HOH VA 10 . ? -44.023 2.462 17.173 1.00 23.63 ? 1030 HOH A O 1 HETATM 9281 O O . HOH VA 10 . ? -25.449 22.826 11.664 1.00 22.78 ? 1031 HOH A O 1 HETATM 9282 O O . HOH VA 10 . ? -22.047 -13.569 39.734 1.00 22.07 ? 1032 HOH A O 1 HETATM 9283 O O . HOH VA 10 . ? -10.578 6.793 11.302 1.00 10.06 ? 1033 HOH A O 1 HETATM 9284 O O . HOH VA 10 . ? -17.222 15.585 56.953 1.00 71.02 ? 1034 HOH A O 1 HETATM 9285 O O . HOH VA 10 . ? -42.128 -0.388 23.729 1.00 22.80 ? 1035 HOH A O 1 HETATM 9286 O O . HOH VA 10 . ? -34.909 2.748 15.479 1.00 13.13 ? 1036 HOH A O 1 HETATM 9287 O O . HOH VA 10 . ? -22.052 -14.075 36.937 1.00 13.85 ? 1037 HOH A O 1 HETATM 9288 O O . HOH VA 10 . ? -45.321 -3.952 59.920 1.00 24.84 ? 1038 HOH A O 1 HETATM 9289 O O . HOH VA 10 . ? -43.054 -12.147 39.678 1.00 1.00 ? 1039 HOH A O 1 HETATM 9290 O O . HOH VA 10 . ? -9.928 12.380 34.233 1.00 17.80 ? 1040 HOH A O 1 HETATM 9291 O O . HOH VA 10 . ? -20.670 25.496 43.825 1.00 21.92 ? 1041 HOH A O 1 HETATM 9292 O O . HOH VA 10 . ? -45.574 -16.342 6.866 1.00 19.71 ? 1042 HOH A O 1 HETATM 9293 O O . HOH VA 10 . ? -24.539 -12.312 29.943 1.00 8.71 ? 1043 HOH A O 1 HETATM 9294 O O . HOH VA 10 . ? -56.870 10.162 32.089 1.00 12.35 ? 1044 HOH A O 1 HETATM 9295 O O . HOH VA 10 . ? -17.421 -6.881 19.326 1.00 1.00 ? 1045 HOH A O 1 HETATM 9296 O O . HOH VA 10 . ? -12.899 0.019 33.602 1.00 17.88 ? 1046 HOH A O 1 HETATM 9297 O O . HOH VA 10 . ? -28.208 -29.812 28.676 1.00 21.41 ? 1047 HOH A O 1 HETATM 9298 O O . HOH VA 10 . ? -45.023 -27.759 30.024 1.00 23.97 ? 1048 HOH A O 1 HETATM 9299 O O . HOH VA 10 . ? -28.387 4.911 17.925 1.00 1.00 ? 1049 HOH A O 1 HETATM 9300 O O . HOH VA 10 . ? -28.080 -19.629 35.290 1.00 30.85 ? 1050 HOH A O 1 HETATM 9301 O O . HOH VA 10 . ? -32.627 -2.529 58.661 1.00 34.72 ? 1051 HOH A O 1 HETATM 9302 O O . HOH VA 10 . ? -52.384 -16.814 11.002 1.00 32.66 ? 1052 HOH A O 1 HETATM 9303 O O . HOH VA 10 . ? -13.819 -2.320 40.164 1.00 23.61 ? 1053 HOH A O 1 HETATM 9304 O O . HOH VA 10 . ? -14.939 -8.536 12.124 1.00 5.28 ? 1054 HOH A O 1 HETATM 9305 O O . HOH VA 10 . ? -19.066 10.624 57.740 1.00 25.38 ? 1055 HOH A O 1 HETATM 9306 O O . HOH VA 10 . ? -37.763 13.114 39.675 1.00 61.58 ? 1056 HOH A O 1 HETATM 9307 O O . HOH VA 10 . ? -45.870 -15.673 28.055 1.00 20.47 ? 1057 HOH A O 1 HETATM 9308 O O . HOH VA 10 . ? -17.988 -28.502 30.877 1.00 14.63 ? 1058 HOH A O 1 HETATM 9309 O O . HOH VA 10 . ? -18.609 7.396 1.342 1.00 18.07 ? 1059 HOH A O 1 HETATM 9310 O O . HOH VA 10 . ? -24.569 2.980 10.148 1.00 3.37 ? 1060 HOH A O 1 HETATM 9311 O O . HOH VA 10 . ? -29.494 22.127 34.909 1.00 25.22 ? 1061 HOH A O 1 HETATM 9312 O O . HOH VA 10 . ? -46.391 -12.754 5.804 1.00 12.78 ? 1062 HOH A O 1 HETATM 9313 O O . HOH VA 10 . ? -12.045 3.671 1.904 1.00 30.58 ? 1063 HOH A O 1 HETATM 9314 O O . HOH VA 10 . ? -16.739 -0.609 52.511 1.00 23.22 ? 1064 HOH A O 1 HETATM 9315 O O . HOH VA 10 . ? -46.125 -9.261 30.482 1.00 10.62 ? 1065 HOH A O 1 HETATM 9316 O O . HOH VA 10 . ? -29.393 11.435 13.149 1.00 24.47 ? 1066 HOH A O 1 HETATM 9317 O O . HOH VA 10 . ? -31.395 -13.269 50.633 1.00 28.08 ? 1067 HOH A O 1 HETATM 9318 O O . HOH VA 10 . ? -21.811 16.459 13.055 1.00 24.76 ? 1068 HOH A O 1 HETATM 9319 O O . HOH VA 10 . ? -18.793 7.606 55.651 1.00 20.13 ? 1069 HOH A O 1 HETATM 9320 O O . HOH VA 10 . ? -24.996 13.904 24.319 1.00 6.13 ? 1070 HOH A O 1 HETATM 9321 O O . HOH VA 10 . ? -50.001 -0.318 53.031 1.00 23.42 ? 1071 HOH A O 1 HETATM 9322 O O . HOH VA 10 . ? -15.045 6.988 37.171 1.00 2.95 ? 1072 HOH A O 1 HETATM 9323 O O . HOH VA 10 . ? -23.227 20.508 32.063 1.00 23.54 ? 1073 HOH A O 1 HETATM 9324 O O . HOH VA 10 . ? -10.751 8.730 35.827 1.00 8.32 ? 1074 HOH A O 1 HETATM 9325 O O . HOH VA 10 . ? -25.429 15.011 54.629 1.00 29.07 ? 1075 HOH A O 1 HETATM 9326 O O . HOH VA 10 . ? -32.922 -34.310 23.226 1.00 47.93 ? 1076 HOH A O 1 HETATM 9327 O O . HOH VA 10 . ? -21.744 26.400 24.843 1.00 20.22 ? 1077 HOH A O 1 HETATM 9328 O O . HOH VA 10 . ? -29.406 10.666 27.657 1.00 17.82 ? 1078 HOH A O 1 HETATM 9329 O O . HOH VA 10 . ? -15.152 13.246 44.578 1.00 26.51 ? 1079 HOH A O 1 HETATM 9330 O O . HOH VA 10 . ? -12.584 6.551 34.794 1.00 12.80 ? 1080 HOH A O 1 HETATM 9331 O O . HOH VA 10 . ? -37.123 26.461 18.769 1.00 30.15 ? 1081 HOH A O 1 HETATM 9332 O O . HOH VA 10 . ? -18.792 2.124 17.196 1.00 4.33 ? 1082 HOH A O 1 HETATM 9333 O O . HOH VA 10 . ? -16.158 -22.666 26.459 1.00 15.95 ? 1083 HOH A O 1 HETATM 9334 O O . HOH VA 10 . ? -48.732 21.367 17.655 1.00 8.49 ? 1084 HOH A O 1 HETATM 9335 O O . HOH VA 10 . ? -16.022 -14.662 27.617 1.00 30.58 ? 1085 HOH A O 1 HETATM 9336 O O . HOH VA 10 . ? -16.371 -7.040 4.268 1.00 25.18 ? 1086 HOH A O 1 HETATM 9337 O O . HOH VA 10 . ? -16.063 17.535 34.090 1.00 28.80 ? 1087 HOH A O 1 HETATM 9338 O O . HOH VA 10 . ? -15.509 5.782 39.664 1.00 9.58 ? 1088 HOH A O 1 HETATM 9339 O O . HOH VA 10 . ? -33.869 20.127 34.774 1.00 18.83 ? 1089 HOH A O 1 HETATM 9340 O O . HOH VA 10 . ? -21.301 -13.513 8.326 1.00 39.32 ? 1090 HOH A O 1 HETATM 9341 O O . HOH VA 10 . ? -18.338 12.959 42.074 1.00 15.31 ? 1091 HOH A O 1 HETATM 9342 O O . HOH VA 10 . ? -12.610 -21.980 21.055 1.00 8.14 ? 1092 HOH A O 1 HETATM 9343 O O . HOH VA 10 . ? -18.831 -14.514 29.830 1.00 13.74 ? 1093 HOH A O 1 HETATM 9344 O O . HOH VA 10 . ? -28.364 -9.754 9.218 1.00 13.46 ? 1094 HOH A O 1 HETATM 9345 O O . HOH VA 10 . ? -55.065 -13.578 45.760 1.00 21.62 ? 1095 HOH A O 1 HETATM 9346 O O . HOH VA 10 . ? -23.046 -19.120 31.649 1.00 20.92 ? 1096 HOH A O 1 HETATM 9347 O O . HOH VA 10 . ? -45.886 20.935 28.925 1.00 8.26 ? 1097 HOH A O 1 HETATM 9348 O O . HOH VA 10 . ? -26.216 -10.243 5.456 1.00 33.62 ? 1098 HOH A O 1 HETATM 9349 O O . HOH VA 10 . ? -53.210 -12.293 20.398 1.00 14.84 ? 1099 HOH A O 1 HETATM 9350 O O . HOH VA 10 . ? -17.084 17.716 46.699 1.00 28.64 ? 1100 HOH A O 1 HETATM 9351 O O . HOH VA 10 . ? -53.422 -13.789 14.076 1.00 49.41 ? 1101 HOH A O 1 HETATM 9352 O O . HOH VA 10 . ? -11.018 -9.228 25.627 1.00 13.72 ? 1102 HOH A O 1 HETATM 9353 O O . HOH VA 10 . ? -56.318 6.360 13.996 1.00 24.60 ? 1103 HOH A O 1 HETATM 9354 O O . HOH VA 10 . ? -15.771 -0.049 7.592 1.00 8.44 ? 1104 HOH A O 1 HETATM 9355 O O . HOH VA 10 . ? -39.160 -12.599 2.359 1.00 3.18 ? 1105 HOH A O 1 HETATM 9356 O O . HOH VA 10 . ? -26.723 22.536 14.670 1.00 14.09 ? 1106 HOH A O 1 HETATM 9357 O O . HOH VA 10 . ? -10.238 -3.409 25.385 1.00 29.55 ? 1107 HOH A O 1 HETATM 9358 O O . HOH VA 10 . ? -46.207 24.800 20.202 1.00 27.87 ? 1108 HOH A O 1 HETATM 9359 O O . HOH VA 10 . ? -29.239 4.861 20.334 1.00 1.00 ? 1109 HOH A O 1 HETATM 9360 O O . HOH VA 10 . ? -50.668 10.665 35.379 1.00 10.92 ? 1110 HOH A O 1 HETATM 9361 O O . HOH VA 10 . ? -16.448 -25.238 33.664 1.00 18.74 ? 1111 HOH A O 1 HETATM 9362 O O . HOH VA 10 . ? -59.569 0.138 39.730 1.00 22.81 ? 1112 HOH A O 1 HETATM 9363 O O . HOH VA 10 . ? -34.534 -6.880 53.509 1.00 60.57 ? 1113 HOH A O 1 HETATM 9364 O O . HOH VA 10 . ? -46.180 -1.077 45.720 1.00 20.39 ? 1114 HOH A O 1 HETATM 9365 O O . HOH VA 10 . ? -21.765 19.536 51.489 1.00 17.59 ? 1115 HOH A O 1 HETATM 9366 O O . HOH VA 10 . ? -22.676 5.961 7.687 1.00 7.37 ? 1116 HOH A O 1 HETATM 9367 O O . HOH VA 10 . ? -11.280 6.456 38.286 1.00 34.84 ? 1117 HOH A O 1 HETATM 9368 O O . HOH VA 10 . ? -33.803 -26.960 21.011 1.00 54.17 ? 1118 HOH A O 1 HETATM 9369 O O . HOH VA 10 . ? -17.174 6.760 43.040 1.00 26.60 ? 1119 HOH A O 1 HETATM 9370 O O . HOH VA 10 . ? -25.730 1.359 8.459 1.00 36.94 ? 1120 HOH A O 1 HETATM 9371 O O . HOH VA 10 . ? -11.141 -10.528 10.592 1.00 23.47 ? 1121 HOH A O 1 HETATM 9372 O O . HOH VA 10 . ? -35.035 13.628 38.588 1.00 50.42 ? 1122 HOH A O 1 HETATM 9373 O O . HOH VA 10 . ? -46.721 22.699 19.055 1.00 14.99 ? 1123 HOH A O 1 HETATM 9374 O O . HOH VA 10 . ? -21.948 -9.102 38.052 1.00 9.61 ? 1124 HOH A O 1 HETATM 9375 O O . HOH VA 10 . ? -42.780 23.803 16.734 1.00 18.21 ? 1125 HOH A O 1 HETATM 9376 O O . HOH VA 10 . ? -14.732 -11.556 27.530 1.00 14.04 ? 1126 HOH A O 1 HETATM 9377 O O . HOH VA 10 . ? -27.790 -18.384 42.237 1.00 26.89 ? 1127 HOH A O 1 HETATM 9378 O O . HOH VA 10 . ? -38.209 -19.244 42.042 1.00 23.11 ? 1128 HOH A O 1 HETATM 9379 O O . HOH VA 10 . ? -45.598 -0.167 58.308 1.00 35.17 ? 1129 HOH A O 1 HETATM 9380 O O . HOH VA 10 . ? -48.131 15.506 31.200 1.00 32.05 ? 1130 HOH A O 1 HETATM 9381 O O . HOH VA 10 . ? -14.195 -23.634 25.201 1.00 18.07 ? 1131 HOH A O 1 HETATM 9382 O O . HOH VA 10 . ? -29.356 -23.125 8.931 1.00 38.67 ? 1132 HOH A O 1 HETATM 9383 O O . HOH VA 10 . ? -42.522 20.789 33.539 1.00 21.21 ? 1133 HOH A O 1 HETATM 9384 O O . HOH VA 10 . ? -11.278 18.085 20.397 1.00 14.51 ? 1134 HOH A O 1 HETATM 9385 O O . HOH VA 10 . ? -27.241 -12.829 4.834 1.00 27.47 ? 1135 HOH A O 1 HETATM 9386 O O . HOH VA 10 . ? -16.836 -0.266 58.372 1.00 15.35 ? 1136 HOH A O 1 HETATM 9387 O O . HOH VA 10 . ? -55.087 -4.019 26.957 1.00 21.11 ? 1137 HOH A O 1 HETATM 9388 O O . HOH VA 10 . ? -30.380 -2.762 1.552 1.00 16.72 ? 1138 HOH A O 1 HETATM 9389 O O . HOH VA 10 . ? -52.597 -10.844 46.258 1.00 17.22 ? 1139 HOH A O 1 HETATM 9390 O O . HOH VA 10 . ? -22.496 20.705 16.790 1.00 19.38 ? 1140 HOH A O 1 HETATM 9391 O O . HOH VA 10 . ? -30.560 -15.841 46.031 1.00 28.12 ? 1141 HOH A O 1 HETATM 9392 O O . HOH VA 10 . ? -16.218 13.647 24.127 1.00 20.90 ? 1142 HOH A O 1 HETATM 9393 O O . HOH VA 10 . ? -15.488 20.173 33.579 1.00 20.00 ? 1143 HOH A O 1 HETATM 9394 O O . HOH VA 10 . ? -22.653 11.919 40.154 1.00 32.62 ? 1144 HOH A O 1 HETATM 9395 O O . HOH VA 10 . ? -8.575 -7.689 35.217 1.00 8.94 ? 1145 HOH A O 1 HETATM 9396 O O . HOH VA 10 . ? -15.532 21.012 20.810 1.00 12.48 ? 1146 HOH A O 1 HETATM 9397 O O . HOH VA 10 . ? -55.689 -5.375 3.458 1.00 31.31 ? 1147 HOH A O 1 HETATM 9398 O O . HOH VA 10 . ? -27.512 13.263 28.386 1.00 24.79 ? 1148 HOH A O 1 HETATM 9399 O O . HOH VA 10 . ? -45.291 5.182 43.313 1.00 13.43 ? 1149 HOH A O 1 HETATM 9400 O O . HOH VA 10 . ? -41.529 6.938 40.061 1.00 18.31 ? 1150 HOH A O 1 HETATM 9401 O O . HOH VA 10 . ? -51.926 14.055 29.363 1.00 34.89 ? 1151 HOH A O 1 HETATM 9402 O O . HOH VA 10 . ? -10.804 -2.395 36.062 1.00 14.95 ? 1152 HOH A O 1 HETATM 9403 O O . HOH VA 10 . ? -44.205 0.325 46.952 1.00 16.66 ? 1153 HOH A O 1 HETATM 9404 O O . HOH VA 10 . ? -39.098 -6.568 28.420 1.00 28.85 ? 1154 HOH A O 1 HETATM 9405 O O . HOH VA 10 . ? -38.160 10.140 34.374 1.00 16.78 ? 1155 HOH A O 1 HETATM 9406 O O . HOH VA 10 . ? -45.215 -1.979 -0.385 1.00 48.75 ? 1156 HOH A O 1 HETATM 9407 O O . HOH VA 10 . ? -42.502 -11.012 49.443 1.00 13.31 ? 1157 HOH A O 1 HETATM 9408 O O . HOH VA 10 . ? -49.682 1.525 44.715 1.00 11.72 ? 1158 HOH A O 1 HETATM 9409 O O . HOH VA 10 . ? -11.642 -11.733 26.594 1.00 20.18 ? 1159 HOH A O 1 HETATM 9410 O O . HOH VA 10 . ? -12.960 -7.514 12.607 1.00 4.11 ? 1160 HOH A O 1 HETATM 9411 O O . HOH VA 10 . ? -34.327 6.509 6.451 1.00 9.12 ? 1161 HOH A O 1 HETATM 9412 O O . HOH VA 10 . ? -32.637 -5.951 -0.851 1.00 23.61 ? 1162 HOH A O 1 HETATM 9413 O O . HOH VA 10 . ? -49.042 -22.341 26.297 1.00 13.22 ? 1163 HOH A O 1 HETATM 9414 O O . HOH VA 10 . ? -37.399 -26.340 22.627 1.00 20.99 ? 1164 HOH A O 1 HETATM 9415 O O . HOH VA 10 . ? -45.855 15.726 32.391 1.00 26.56 ? 1165 HOH A O 1 HETATM 9416 O O . HOH VA 10 . ? -41.595 3.273 57.741 1.00 27.79 ? 1166 HOH A O 1 HETATM 9417 O O . HOH VA 10 . ? -22.696 -10.517 43.133 1.00 21.04 ? 1167 HOH A O 1 HETATM 9418 O O . HOH VA 10 . ? -25.850 24.210 38.063 1.00 21.86 ? 1168 HOH A O 1 HETATM 9419 O O . HOH VA 10 . ? -30.912 13.055 2.416 1.00 31.09 ? 1169 HOH A O 1 HETATM 9420 O O . HOH VA 10 . ? -52.182 -5.810 0.103 1.00 29.50 ? 1170 HOH A O 1 HETATM 9421 O O . HOH VA 10 . ? -41.967 -24.544 22.891 1.00 12.91 ? 1171 HOH A O 1 HETATM 9422 O O . HOH VA 10 . ? -43.299 19.314 10.287 1.00 13.75 ? 1172 HOH A O 1 HETATM 9423 O O . HOH VA 10 . ? -23.219 -12.614 46.953 1.00 23.26 ? 1173 HOH A O 1 HETATM 9424 O O . HOH VA 10 . ? -15.311 22.773 33.322 1.00 20.78 ? 1174 HOH A O 1 HETATM 9425 O O . HOH VA 10 . ? -28.570 16.062 28.401 1.00 25.51 ? 1175 HOH A O 1 HETATM 9426 O O . HOH VA 10 . ? -16.008 -12.878 29.616 1.00 10.31 ? 1176 HOH A O 1 HETATM 9427 O O . HOH VA 10 . ? -15.418 13.969 21.591 1.00 18.87 ? 1177 HOH A O 1 HETATM 9428 O O . HOH VA 10 . ? -48.608 0.650 56.028 1.00 26.30 ? 1178 HOH A O 1 HETATM 9429 O O . HOH VA 10 . ? -31.730 -26.880 17.818 1.00 22.71 ? 1179 HOH A O 1 HETATM 9430 O O . HOH VA 10 . ? -17.524 0.865 23.907 1.00 38.41 ? 1180 HOH A O 1 HETATM 9431 O O . HOH VA 10 . ? -48.014 4.820 5.020 1.00 27.01 ? 1181 HOH A O 1 HETATM 9432 O O . HOH VA 10 . ? -39.675 2.977 -1.067 1.00 21.44 ? 1182 HOH A O 1 HETATM 9433 O O . HOH VA 10 . ? -58.607 -3.162 30.957 1.00 24.61 ? 1183 HOH A O 1 HETATM 9434 O O . HOH VA 10 . ? -62.775 -7.994 48.449 1.00 24.31 ? 1184 HOH A O 1 HETATM 9435 O O . HOH VA 10 . ? -9.316 11.558 16.469 1.00 27.45 ? 1185 HOH A O 1 HETATM 9436 O O . HOH VA 10 . ? -49.460 14.069 33.783 1.00 36.28 ? 1186 HOH A O 1 HETATM 9437 O O . HOH VA 10 . ? -53.432 -4.149 25.051 1.00 8.05 ? 1187 HOH A O 1 HETATM 9438 O O . HOH VA 10 . ? -16.087 -22.299 23.949 1.00 21.52 ? 1188 HOH A O 1 HETATM 9439 O O . HOH VA 10 . ? -54.224 -3.842 40.470 1.00 26.13 ? 1189 HOH A O 1 HETATM 9440 O O . HOH VA 10 . ? -51.797 14.277 32.379 1.00 50.68 ? 1190 HOH A O 1 HETATM 9441 O O . HOH VA 10 . ? -40.966 -11.839 31.938 1.00 9.55 ? 1191 HOH A O 1 HETATM 9442 O O . HOH VA 10 . ? -44.594 -5.175 29.742 1.00 27.09 ? 1192 HOH A O 1 HETATM 9443 O O . HOH VA 10 . ? -50.832 -5.372 26.092 1.00 15.62 ? 1193 HOH A O 1 HETATM 9444 O O . HOH VA 10 . ? -20.192 12.802 57.284 1.00 10.98 ? 1194 HOH A O 1 HETATM 9445 O O . HOH VA 10 . ? -14.752 -14.451 25.471 1.00 48.75 ? 1195 HOH A O 1 HETATM 9446 O O . HOH VA 10 . ? -35.020 18.562 36.725 1.00 31.39 ? 1196 HOH A O 1 HETATM 9447 O O . HOH VA 10 . ? -44.942 -6.791 61.095 1.00 35.63 ? 1197 HOH A O 1 HETATM 9448 O O . HOH VA 10 . ? -29.200 -8.859 5.996 1.00 18.10 ? 1198 HOH A O 1 HETATM 9449 O O . HOH VA 10 . ? -37.398 9.476 5.737 1.00 21.24 ? 1199 HOH A O 1 HETATM 9450 O O . HOH VA 10 . ? -33.944 -23.637 3.145 1.00 34.74 ? 1200 HOH A O 1 HETATM 9451 O O . HOH VA 10 . ? -37.411 -0.017 7.029 1.00 14.05 ? 1201 HOH A O 1 HETATM 9452 O O . HOH VA 10 . ? -22.851 5.341 13.116 1.00 8.49 ? 1202 HOH A O 1 HETATM 9453 O O . HOH VA 10 . ? -58.530 1.958 41.051 1.00 14.49 ? 1203 HOH A O 1 HETATM 9454 O O . HOH VA 10 . ? -34.095 -13.823 51.933 1.00 25.84 ? 1204 HOH A O 1 HETATM 9455 O O . HOH VA 10 . ? -25.058 18.865 54.500 1.00 11.42 ? 1205 HOH A O 1 HETATM 9456 O O . HOH VA 10 . ? -11.753 13.581 44.626 1.00 16.35 ? 1206 HOH A O 1 HETATM 9457 O O . HOH VA 10 . ? -45.247 -16.768 47.853 1.00 11.67 ? 1207 HOH A O 1 HETATM 9458 O O . HOH VA 10 . ? -54.320 10.639 34.055 1.00 18.22 ? 1208 HOH A O 1 HETATM 9459 O O . HOH VA 10 . ? -18.106 -1.299 60.984 1.00 28.80 ? 1209 HOH A O 1 HETATM 9460 O O . HOH VA 10 . ? -35.203 -33.839 24.468 1.00 22.10 ? 1210 HOH A O 1 HETATM 9461 O O . HOH VA 10 . ? -12.682 13.100 23.206 1.00 13.21 ? 1211 HOH A O 1 HETATM 9462 O O . HOH VA 10 . ? -12.843 -6.240 25.075 1.00 25.93 ? 1212 HOH A O 1 HETATM 9463 O O . HOH VA 10 . ? -14.924 -12.589 11.216 1.00 15.61 ? 1213 HOH A O 1 HETATM 9464 O O . HOH VA 10 . ? -58.581 -7.342 38.211 1.00 38.38 ? 1214 HOH A O 1 HETATM 9465 O O . HOH VA 10 . ? -19.377 0.723 42.833 1.00 18.73 ? 1215 HOH A O 1 HETATM 9466 O O . HOH VA 10 . ? -34.144 -3.180 -1.124 1.00 23.71 ? 1216 HOH A O 1 HETATM 9467 O O . HOH VA 10 . ? -19.221 19.748 5.817 1.00 35.52 ? 1217 HOH A O 1 HETATM 9468 O O . HOH VA 10 . ? -18.658 -15.427 14.179 1.00 34.23 ? 1218 HOH A O 1 HETATM 9469 O O . HOH VA 10 . ? -20.942 -18.072 12.058 1.00 24.25 ? 1219 HOH A O 1 HETATM 9470 O O . HOH VA 10 . ? -26.948 -15.700 0.243 1.00 35.43 ? 1220 HOH A O 1 HETATM 9471 O O . HOH VA 10 . ? -16.189 -17.466 37.204 1.00 21.09 ? 1221 HOH A O 1 HETATM 9472 O O . HOH VA 10 . ? -31.146 -9.922 5.285 1.00 18.53 ? 1222 HOH A O 1 HETATM 9473 O O . HOH VA 10 . ? -32.587 2.754 4.780 1.00 20.14 ? 1223 HOH A O 1 HETATM 9474 O O . HOH VA 10 . ? -20.944 21.762 23.987 1.00 21.65 ? 1224 HOH A O 1 HETATM 9475 O O . HOH VA 10 . ? -27.021 10.557 13.845 1.00 24.46 ? 1225 HOH A O 1 HETATM 9476 O O . HOH VA 10 . ? -53.514 -0.422 20.238 1.00 34.05 ? 1226 HOH A O 1 HETATM 9477 O O . HOH VA 10 . ? -18.361 -10.802 36.938 1.00 27.03 ? 1227 HOH A O 1 HETATM 9478 O O . HOH VA 10 . ? -52.527 0.390 4.932 1.00 26.09 ? 1228 HOH A O 1 HETATM 9479 O O . HOH VA 10 . ? -8.787 18.916 39.120 1.00 23.20 ? 1229 HOH A O 1 HETATM 9480 O O . HOH VA 10 . ? -28.101 -11.119 33.981 1.00 25.79 ? 1230 HOH A O 1 HETATM 9481 O O . HOH VA 10 . ? -9.647 8.962 13.107 1.00 29.74 ? 1231 HOH A O 1 HETATM 9482 O O . HOH VA 10 . ? -29.841 19.748 63.392 1.00 39.28 ? 1232 HOH A O 1 HETATM 9483 O O . HOH VA 10 . ? -50.525 -5.413 16.952 1.00 15.70 ? 1233 HOH A O 1 HETATM 9484 O O . HOH VA 10 . ? -31.593 -25.485 3.383 1.00 46.83 ? 1234 HOH A O 1 HETATM 9485 O O . HOH VA 10 . ? -31.521 24.065 14.071 1.00 18.24 ? 1235 HOH A O 1 HETATM 9486 O O . HOH VA 10 . ? -30.393 19.213 48.387 1.00 45.91 ? 1236 HOH A O 1 HETATM 9487 O O . HOH VA 10 . ? -20.851 25.329 20.955 1.00 12.28 ? 1237 HOH A O 1 HETATM 9488 O O . HOH VA 10 . ? -9.710 -11.588 37.282 1.00 21.70 ? 1238 HOH A O 1 HETATM 9489 O O . HOH VA 10 . ? -43.369 -17.794 28.481 1.00 15.29 ? 1239 HOH A O 1 HETATM 9490 O O . HOH VA 10 . ? -42.699 -11.249 53.774 1.00 23.33 ? 1240 HOH A O 1 HETATM 9491 O O . HOH VA 10 . ? -58.873 -12.941 39.536 1.00 27.66 ? 1241 HOH A O 1 HETATM 9492 O O . HOH VA 10 . ? -47.249 -18.698 37.549 1.00 34.95 ? 1242 HOH A O 1 HETATM 9493 O O . HOH VA 10 . ? -38.320 -32.910 24.558 1.00 30.63 ? 1243 HOH A O 1 HETATM 9494 O O . HOH VA 10 . ? -28.745 26.094 36.515 1.00 35.80 ? 1244 HOH A O 1 HETATM 9495 O O . HOH VA 10 . ? -40.849 26.704 11.835 1.00 21.79 ? 1245 HOH A O 1 HETATM 9496 O O . HOH VA 10 . ? -38.591 -15.363 46.432 1.00 6.59 ? 1246 HOH A O 1 HETATM 9497 O O . HOH VA 10 . ? -12.470 13.620 25.876 1.00 28.21 ? 1247 HOH A O 1 HETATM 9498 O O . HOH VA 10 . ? -15.902 13.305 26.907 1.00 12.88 ? 1248 HOH A O 1 HETATM 9499 O O . HOH VA 10 . ? -53.660 -2.973 17.386 1.00 38.96 ? 1249 HOH A O 1 HETATM 9500 O O . HOH VA 10 . ? -58.492 -1.151 6.045 1.00 35.23 ? 1250 HOH A O 1 HETATM 9501 O O . HOH VA 10 . ? -51.421 6.931 3.716 1.00 29.35 ? 1251 HOH A O 1 HETATM 9502 O O . HOH VA 10 . ? -47.249 8.971 1.217 1.00 17.39 ? 1252 HOH A O 1 HETATM 9503 O O . HOH VA 10 . ? -27.554 6.207 6.454 1.00 33.40 ? 1253 HOH A O 1 HETATM 9504 O O . HOH VA 10 . ? -42.170 -23.855 32.387 1.00 34.98 ? 1254 HOH A O 1 HETATM 9505 O O . HOH VA 10 . ? -25.917 8.030 4.328 1.00 38.48 ? 1255 HOH A O 1 HETATM 9506 O O . HOH VA 10 . ? -55.629 2.003 45.256 1.00 16.65 ? 1256 HOH A O 1 HETATM 9507 O O . HOH VA 10 . ? -10.563 -19.950 30.340 1.00 20.17 ? 1257 HOH A O 1 HETATM 9508 O O . HOH VA 10 . ? -36.188 14.022 55.996 1.00 22.11 ? 1258 HOH A O 1 HETATM 9509 O O . HOH VA 10 . ? -26.516 -3.623 55.107 1.00 23.25 ? 1259 HOH A O 1 HETATM 9510 O O . HOH VA 10 . ? -28.869 -13.834 52.294 1.00 19.83 ? 1260 HOH A O 1 HETATM 9511 O O . HOH VA 10 . ? -20.352 -8.330 44.992 1.00 25.43 ? 1261 HOH A O 1 HETATM 9512 O O . HOH VA 10 . ? -40.714 -18.445 44.173 1.00 28.49 ? 1262 HOH A O 1 HETATM 9513 O O . HOH VA 10 . ? -17.559 -19.382 33.789 1.00 15.57 ? 1263 HOH A O 1 HETATM 9514 O O . HOH VA 10 . ? -51.254 11.967 26.676 1.00 34.43 ? 1264 HOH A O 1 HETATM 9515 O O . HOH VA 10 . ? -15.599 2.499 1.222 1.00 24.17 ? 1265 HOH A O 1 HETATM 9516 O O . HOH VA 10 . ? -29.732 2.259 62.519 1.00 28.62 ? 1266 HOH A O 1 HETATM 9517 O O . HOH VA 10 . ? -32.194 -0.228 1.806 1.00 12.21 ? 1267 HOH A O 1 HETATM 9518 O O . HOH VA 10 . ? -40.138 -13.515 50.690 1.00 26.14 ? 1268 HOH A O 1 HETATM 9519 O O . HOH WA 10 . ? 33.079 -7.948 3.781 1.00 46.21 ? 902 HOH B O 1 HETATM 9520 O O . HOH WA 10 . ? 2.096 16.728 19.269 1.00 6.14 ? 903 HOH B O 1 HETATM 9521 O O . HOH WA 10 . ? 4.687 -13.615 40.190 1.00 4.85 ? 904 HOH B O 1 HETATM 9522 O O . HOH WA 10 . ? 26.366 3.162 29.820 1.00 10.35 ? 905 HOH B O 1 HETATM 9523 O O . HOH WA 10 . ? 23.350 -8.913 37.131 1.00 3.02 ? 906 HOH B O 1 HETATM 9524 O O . HOH WA 10 . ? 11.661 -13.220 36.275 1.00 13.48 ? 907 HOH B O 1 HETATM 9525 O O . HOH WA 10 . ? 14.495 12.160 42.695 1.00 12.42 ? 908 HOH B O 1 HETATM 9526 O O . HOH WA 10 . ? 0.589 14.657 19.593 1.00 11.79 ? 909 HOH B O 1 HETATM 9527 O O . HOH WA 10 . ? 2.606 -27.697 15.300 1.00 19.44 ? 910 HOH B O 1 HETATM 9528 O O . HOH WA 10 . ? 18.840 -23.744 9.426 1.00 18.89 ? 911 HOH B O 1 HETATM 9529 O O . HOH WA 10 . ? -4.470 -0.121 56.091 1.00 34.59 ? 912 HOH B O 1 HETATM 9530 O O . HOH WA 10 . ? 3.679 -23.831 24.237 1.00 4.07 ? 913 HOH B O 1 HETATM 9531 O O . HOH WA 10 . ? -2.459 11.388 13.939 1.00 4.62 ? 914 HOH B O 1 HETATM 9532 O O . HOH WA 10 . ? -0.897 -3.234 20.336 1.00 10.65 ? 915 HOH B O 1 HETATM 9533 O O . HOH WA 10 . ? 16.879 10.325 35.965 1.00 13.45 ? 916 HOH B O 1 HETATM 9534 O O . HOH WA 10 . ? -8.385 13.496 32.631 1.00 8.84 ? 917 HOH B O 1 HETATM 9535 O O . HOH WA 10 . ? 17.515 -16.944 11.004 1.00 12.47 ? 918 HOH B O 1 HETATM 9536 O O . HOH WA 10 . ? 31.913 -5.735 15.300 1.00 7.75 ? 919 HOH B O 1 HETATM 9537 O O . HOH WA 10 . ? 0.674 -17.863 25.445 1.00 3.66 ? 920 HOH B O 1 HETATM 9538 O O . HOH WA 10 . ? 0.295 3.654 45.851 1.00 15.14 ? 921 HOH B O 1 HETATM 9539 O O . HOH WA 10 . ? -1.308 6.764 28.112 1.00 3.10 ? 922 HOH B O 1 HETATM 9540 O O . HOH WA 10 . ? 7.757 -12.549 27.645 1.00 5.83 ? 923 HOH B O 1 HETATM 9541 O O . HOH WA 10 . ? 28.234 -7.966 11.551 1.00 1.00 ? 924 HOH B O 1 HETATM 9542 O O . HOH WA 10 . ? 14.407 -10.133 20.509 1.00 5.46 ? 925 HOH B O 1 HETATM 9543 O O . HOH WA 10 . ? 27.127 1.757 46.526 1.00 5.71 ? 926 HOH B O 1 HETATM 9544 O O . HOH WA 10 . ? 2.354 -5.170 14.883 1.00 1.02 ? 927 HOH B O 1 HETATM 9545 O O . HOH WA 10 . ? 21.985 5.935 43.559 1.00 27.14 ? 928 HOH B O 1 HETATM 9546 O O . HOH WA 10 . ? 27.039 5.954 5.004 1.00 10.59 ? 929 HOH B O 1 HETATM 9547 O O . HOH WA 10 . ? 7.218 -16.748 24.646 1.00 6.52 ? 930 HOH B O 1 HETATM 9548 O O . HOH WA 10 . ? 1.067 -9.227 24.863 1.00 4.11 ? 931 HOH B O 1 HETATM 9549 O O . HOH WA 10 . ? -3.458 5.181 7.498 1.00 16.96 ? 932 HOH B O 1 HETATM 9550 O O . HOH WA 10 . ? 31.363 -5.626 41.251 1.00 17.24 ? 933 HOH B O 1 HETATM 9551 O O . HOH WA 10 . ? -5.748 9.406 26.643 1.00 8.18 ? 934 HOH B O 1 HETATM 9552 O O . HOH WA 10 . ? 29.362 9.430 39.697 1.00 23.35 ? 935 HOH B O 1 HETATM 9553 O O . HOH WA 10 . ? 7.735 5.432 37.197 1.00 8.75 ? 936 HOH B O 1 HETATM 9554 O O . HOH WA 10 . ? 0.833 0.317 25.695 1.00 12.61 ? 937 HOH B O 1 HETATM 9555 O O . HOH WA 10 . ? 22.902 9.686 32.154 1.00 10.62 ? 938 HOH B O 1 HETATM 9556 O O . HOH WA 10 . ? -7.146 4.454 31.839 1.00 29.16 ? 939 HOH B O 1 HETATM 9557 O O . HOH WA 10 . ? 32.295 6.526 33.772 1.00 12.05 ? 940 HOH B O 1 HETATM 9558 O O . HOH WA 10 . ? 17.483 19.220 40.456 1.00 28.70 ? 941 HOH B O 1 HETATM 9559 O O . HOH WA 10 . ? 15.831 6.272 5.419 1.00 12.58 ? 942 HOH B O 1 HETATM 9560 O O . HOH WA 10 . ? 19.190 -11.309 43.663 1.00 8.71 ? 943 HOH B O 1 HETATM 9561 O O . HOH WA 10 . ? 11.528 -18.191 28.541 1.00 12.54 ? 944 HOH B O 1 HETATM 9562 O O . HOH WA 10 . ? -1.784 -1.724 31.540 1.00 14.96 ? 945 HOH B O 1 HETATM 9563 O O . HOH WA 10 . ? 0.651 10.556 13.689 1.00 17.38 ? 946 HOH B O 1 HETATM 9564 O O . HOH WA 10 . ? 12.771 -15.318 30.502 1.00 25.39 ? 947 HOH B O 1 HETATM 9565 O O . HOH WA 10 . ? 35.370 11.812 28.217 1.00 21.11 ? 948 HOH B O 1 HETATM 9566 O O . HOH WA 10 . ? 8.847 -19.317 23.951 1.00 35.43 ? 949 HOH B O 1 HETATM 9567 O O . HOH WA 10 . ? 39.422 -1.207 32.483 1.00 15.42 ? 950 HOH B O 1 HETATM 9568 O O . HOH WA 10 . ? 21.764 -22.983 26.544 1.00 3.99 ? 951 HOH B O 1 HETATM 9569 O O . HOH WA 10 . ? 22.554 13.248 26.331 1.00 21.49 ? 952 HOH B O 1 HETATM 9570 O O . HOH WA 10 . ? 38.884 -1.133 51.097 1.00 26.65 ? 953 HOH B O 1 HETATM 9571 O O . HOH WA 10 . ? 36.407 -13.208 33.858 1.00 26.03 ? 954 HOH B O 1 HETATM 9572 O O . HOH WA 10 . ? 37.184 -3.679 39.313 1.00 17.87 ? 955 HOH B O 1 HETATM 9573 O O . HOH WA 10 . ? 29.964 -18.572 31.035 1.00 34.56 ? 956 HOH B O 1 HETATM 9574 O O . HOH WA 10 . ? 10.726 -7.315 17.848 1.00 6.76 ? 957 HOH B O 1 HETATM 9575 O O . HOH WA 10 . ? -0.031 -3.092 24.068 1.00 34.66 ? 958 HOH B O 1 HETATM 9576 O O . HOH WA 10 . ? -2.841 -7.593 42.151 1.00 2.18 ? 959 HOH B O 1 HETATM 9577 O O . HOH WA 10 . ? 23.496 9.937 27.729 1.00 7.05 ? 960 HOH B O 1 HETATM 9578 O O . HOH WA 10 . ? 5.003 -7.326 12.786 1.00 17.24 ? 961 HOH B O 1 HETATM 9579 O O . HOH WA 10 . ? -7.258 18.527 24.031 1.00 35.02 ? 962 HOH B O 1 HETATM 9580 O O . HOH WA 10 . ? -1.080 -7.808 27.745 1.00 3.15 ? 963 HOH B O 1 HETATM 9581 O O . HOH WA 10 . ? 21.446 0.856 17.310 1.00 13.32 ? 964 HOH B O 1 HETATM 9582 O O . HOH WA 10 . ? 25.852 5.509 36.405 1.00 11.43 ? 965 HOH B O 1 HETATM 9583 O O . HOH WA 10 . ? 31.108 -23.371 17.749 1.00 18.00 ? 966 HOH B O 1 HETATM 9584 O O . HOH WA 10 . ? 23.518 11.174 38.583 1.00 16.57 ? 967 HOH B O 1 HETATM 9585 O O . HOH WA 10 . ? 19.172 15.643 33.944 1.00 14.18 ? 968 HOH B O 1 HETATM 9586 O O . HOH WA 10 . ? 19.916 -1.250 4.611 1.00 19.79 ? 969 HOH B O 1 HETATM 9587 O O . HOH WA 10 . ? 25.285 -0.119 40.976 1.00 11.15 ? 970 HOH B O 1 HETATM 9588 O O . HOH WA 10 . ? -0.301 -1.057 33.894 1.00 8.14 ? 971 HOH B O 1 HETATM 9589 O O . HOH WA 10 . ? 34.829 -16.745 3.907 1.00 19.72 ? 972 HOH B O 1 HETATM 9590 O O . HOH WA 10 . ? -3.733 0.294 40.135 1.00 12.77 ? 973 HOH B O 1 HETATM 9591 O O . HOH WA 10 . ? 4.192 11.962 39.690 1.00 14.95 ? 974 HOH B O 1 HETATM 9592 O O . HOH WA 10 . ? 3.961 -21.326 20.337 1.00 8.16 ? 975 HOH B O 1 HETATM 9593 O O . HOH WA 10 . ? -2.142 4.225 17.291 1.00 19.47 ? 976 HOH B O 1 HETATM 9594 O O . HOH WA 10 . ? 20.931 3.893 26.312 1.00 14.13 ? 977 HOH B O 1 HETATM 9595 O O . HOH WA 10 . ? -2.528 22.183 29.869 1.00 42.28 ? 978 HOH B O 1 HETATM 9596 O O . HOH WA 10 . ? 27.752 -0.160 -0.005 1.00 18.45 ? 979 HOH B O 1 HETATM 9597 O O . HOH WA 10 . ? -0.195 4.645 19.799 1.00 4.73 ? 980 HOH B O 1 HETATM 9598 O O . HOH WA 10 . ? -2.868 -12.634 51.729 1.00 11.58 ? 981 HOH B O 1 HETATM 9599 O O . HOH WA 10 . ? 11.240 27.784 30.445 1.00 13.03 ? 982 HOH B O 1 HETATM 9600 O O . HOH WA 10 . ? 18.814 -28.154 19.119 1.00 27.16 ? 983 HOH B O 1 HETATM 9601 O O . HOH WA 10 . ? 26.582 -0.818 43.688 1.00 16.05 ? 984 HOH B O 1 HETATM 9602 O O . HOH WA 10 . ? 41.311 5.229 38.495 1.00 14.88 ? 985 HOH B O 1 HETATM 9603 O O . HOH WA 10 . ? 35.699 1.145 25.220 1.00 16.19 ? 986 HOH B O 1 HETATM 9604 O O . HOH WA 10 . ? 21.127 20.484 16.434 1.00 33.73 ? 987 HOH B O 1 HETATM 9605 O O . HOH WA 10 . ? -5.014 3.387 25.145 1.00 11.33 ? 988 HOH B O 1 HETATM 9606 O O . HOH WA 10 . ? 3.185 16.613 13.120 1.00 11.02 ? 989 HOH B O 1 HETATM 9607 O O . HOH WA 10 . ? -1.617 -2.065 7.707 1.00 15.16 ? 990 HOH B O 1 HETATM 9608 O O . HOH WA 10 . ? 6.589 -23.859 46.499 1.00 37.00 ? 991 HOH B O 1 HETATM 9609 O O . HOH WA 10 . ? 24.467 -27.027 21.769 1.00 35.59 ? 992 HOH B O 1 HETATM 9610 O O . HOH WA 10 . ? 28.381 -4.395 51.298 1.00 20.63 ? 993 HOH B O 1 HETATM 9611 O O . HOH WA 10 . ? 12.739 -15.749 17.251 1.00 19.66 ? 994 HOH B O 1 HETATM 9612 O O . HOH WA 10 . ? -5.123 10.866 35.340 1.00 8.18 ? 995 HOH B O 1 HETATM 9613 O O . HOH WA 10 . ? 17.674 1.265 10.087 1.00 13.66 ? 996 HOH B O 1 HETATM 9614 O O . HOH WA 10 . ? 8.136 18.730 32.857 1.00 8.16 ? 997 HOH B O 1 HETATM 9615 O O . HOH WA 10 . ? -8.439 3.926 37.702 1.00 10.02 ? 998 HOH B O 1 HETATM 9616 O O . HOH WA 10 . ? 7.521 -16.154 27.417 1.00 11.93 ? 999 HOH B O 1 HETATM 9617 O O . HOH WA 10 . ? 17.643 -5.337 15.179 1.00 33.30 ? 1000 HOH B O 1 HETATM 9618 O O . HOH WA 10 . ? 20.169 -16.819 38.844 1.00 25.16 ? 1001 HOH B O 1 HETATM 9619 O O . HOH WA 10 . ? -4.295 -2.927 19.573 1.00 49.83 ? 1002 HOH B O 1 HETATM 9620 O O . HOH WA 10 . ? 17.800 12.405 7.959 1.00 11.75 ? 1003 HOH B O 1 HETATM 9621 O O . HOH WA 10 . ? 25.278 -19.391 33.407 1.00 9.92 ? 1004 HOH B O 1 HETATM 9622 O O . HOH WA 10 . ? -8.661 -2.360 7.564 1.00 21.18 ? 1005 HOH B O 1 HETATM 9623 O O . HOH WA 10 . ? -9.278 -12.238 42.007 1.00 18.92 ? 1006 HOH B O 1 HETATM 9624 O O . HOH WA 10 . ? 10.423 7.607 8.798 1.00 5.02 ? 1007 HOH B O 1 HETATM 9625 O O . HOH WA 10 . ? 21.894 -19.090 32.155 1.00 33.72 ? 1008 HOH B O 1 HETATM 9626 O O . HOH WA 10 . ? 11.699 -14.223 13.383 1.00 29.30 ? 1009 HOH B O 1 HETATM 9627 O O . HOH WA 10 . ? -4.349 -16.023 45.284 1.00 33.88 ? 1010 HOH B O 1 HETATM 9628 O O . HOH WA 10 . ? 8.869 -24.794 14.446 1.00 28.63 ? 1011 HOH B O 1 HETATM 9629 O O . HOH WA 10 . ? 18.848 -18.157 35.437 1.00 13.10 ? 1012 HOH B O 1 HETATM 9630 O O . HOH WA 10 . ? 1.171 12.297 30.042 1.00 13.55 ? 1013 HOH B O 1 HETATM 9631 O O . HOH WA 10 . ? 29.269 -25.228 18.521 1.00 20.57 ? 1014 HOH B O 1 HETATM 9632 O O . HOH WA 10 . ? -2.528 -9.295 37.189 1.00 5.04 ? 1015 HOH B O 1 HETATM 9633 O O . HOH WA 10 . ? 20.848 1.570 38.088 1.00 30.67 ? 1016 HOH B O 1 HETATM 9634 O O . HOH WA 10 . ? 8.325 14.861 10.779 1.00 24.28 ? 1017 HOH B O 1 HETATM 9635 O O . HOH WA 10 . ? 16.231 -21.582 56.682 1.00 16.48 ? 1018 HOH B O 1 HETATM 9636 O O . HOH WA 10 . ? 41.022 -3.994 30.763 1.00 15.04 ? 1019 HOH B O 1 HETATM 9637 O O . HOH WA 10 . ? 4.329 -4.272 7.043 1.00 17.48 ? 1020 HOH B O 1 HETATM 9638 O O . HOH WA 10 . ? 37.327 -5.823 7.234 1.00 26.38 ? 1021 HOH B O 1 HETATM 9639 O O . HOH WA 10 . ? 29.118 16.495 30.778 1.00 20.42 ? 1022 HOH B O 1 HETATM 9640 O O . HOH WA 10 . ? 15.293 16.127 44.129 1.00 10.69 ? 1023 HOH B O 1 HETATM 9641 O O . HOH WA 10 . ? 30.350 1.407 57.713 1.00 29.62 ? 1024 HOH B O 1 HETATM 9642 O O . HOH WA 10 . ? 7.103 9.693 30.104 1.00 8.95 ? 1025 HOH B O 1 HETATM 9643 O O . HOH WA 10 . ? 36.181 1.682 53.269 1.00 26.48 ? 1026 HOH B O 1 HETATM 9644 O O . HOH WA 10 . ? 17.486 1.806 38.118 1.00 17.94 ? 1027 HOH B O 1 HETATM 9645 O O . HOH WA 10 . ? 7.060 -21.994 23.469 1.00 6.21 ? 1028 HOH B O 1 HETATM 9646 O O . HOH WA 10 . ? 29.837 16.935 26.676 1.00 19.71 ? 1029 HOH B O 1 HETATM 9647 O O . HOH WA 10 . ? 28.394 -27.281 20.152 1.00 31.17 ? 1030 HOH B O 1 HETATM 9648 O O . HOH WA 10 . ? 26.484 7.173 -1.509 1.00 15.71 ? 1031 HOH B O 1 HETATM 9649 O O . HOH WA 10 . ? 31.167 7.722 28.744 1.00 28.20 ? 1032 HOH B O 1 HETATM 9650 O O . HOH WA 10 . ? 31.823 -3.283 44.758 1.00 13.75 ? 1033 HOH B O 1 HETATM 9651 O O . HOH WA 10 . ? 2.524 -15.276 57.038 1.00 7.15 ? 1034 HOH B O 1 HETATM 9652 O O . HOH WA 10 . ? 11.646 3.742 59.217 1.00 33.13 ? 1035 HOH B O 1 HETATM 9653 O O . HOH WA 10 . ? 38.189 2.435 41.285 1.00 15.99 ? 1036 HOH B O 1 HETATM 9654 O O . HOH WA 10 . ? 8.863 1.945 55.210 1.00 28.96 ? 1037 HOH B O 1 HETATM 9655 O O . HOH WA 10 . ? 3.940 -7.026 15.305 1.00 12.68 ? 1038 HOH B O 1 HETATM 9656 O O . HOH WA 10 . ? -0.488 1.441 34.279 1.00 10.74 ? 1039 HOH B O 1 HETATM 9657 O O . HOH WA 10 . ? 15.794 24.457 21.240 1.00 29.80 ? 1040 HOH B O 1 HETATM 9658 O O . HOH WA 10 . ? -5.606 -13.753 52.800 1.00 29.31 ? 1041 HOH B O 1 HETATM 9659 O O . HOH WA 10 . ? 15.136 -4.793 32.649 1.00 12.10 ? 1042 HOH B O 1 HETATM 9660 O O . HOH WA 10 . ? 29.113 -8.343 14.274 1.00 7.42 ? 1043 HOH B O 1 HETATM 9661 O O . HOH WA 10 . ? -0.791 16.412 14.082 1.00 9.16 ? 1044 HOH B O 1 HETATM 9662 O O . HOH WA 10 . ? 29.398 3.845 27.509 1.00 15.83 ? 1045 HOH B O 1 HETATM 9663 O O . HOH WA 10 . ? 26.126 -21.255 10.184 1.00 10.98 ? 1046 HOH B O 1 HETATM 9664 O O . HOH WA 10 . ? -7.530 -9.055 11.547 1.00 20.00 ? 1047 HOH B O 1 HETATM 9665 O O . HOH WA 10 . ? 28.523 -22.157 28.060 1.00 22.84 ? 1048 HOH B O 1 HETATM 9666 O O . HOH WA 10 . ? -8.963 -2.801 4.666 1.00 10.03 ? 1049 HOH B O 1 HETATM 9667 O O . HOH WA 10 . ? 3.981 -3.690 61.585 1.00 58.06 ? 1050 HOH B O 1 HETATM 9668 O O . HOH WA 10 . ? 28.348 -0.518 46.072 1.00 10.07 ? 1051 HOH B O 1 HETATM 9669 O O . HOH WA 10 . ? 28.391 1.772 30.522 1.00 6.27 ? 1052 HOH B O 1 HETATM 9670 O O . HOH WA 10 . ? 31.622 -8.332 15.049 1.00 24.96 ? 1053 HOH B O 1 HETATM 9671 O O . HOH WA 10 . ? 34.341 -14.721 7.413 1.00 16.22 ? 1054 HOH B O 1 HETATM 9672 O O . HOH WA 10 . ? -6.009 4.180 41.556 1.00 32.61 ? 1055 HOH B O 1 HETATM 9673 O O . HOH WA 10 . ? 38.451 -1.764 19.493 1.00 21.80 ? 1056 HOH B O 1 HETATM 9674 O O . HOH WA 10 . ? 40.349 7.423 33.345 1.00 30.22 ? 1057 HOH B O 1 HETATM 9675 O O . HOH WA 10 . ? 29.325 -14.815 2.387 1.00 9.82 ? 1058 HOH B O 1 HETATM 9676 O O . HOH WA 10 . ? -2.406 -8.066 39.755 1.00 1.00 ? 1059 HOH B O 1 HETATM 9677 O O . HOH WA 10 . ? -5.397 -2.374 34.142 1.00 14.16 ? 1060 HOH B O 1 HETATM 9678 O O . HOH WA 10 . ? 8.533 -26.636 17.848 1.00 11.88 ? 1061 HOH B O 1 HETATM 9679 O O . HOH WA 10 . ? 22.614 -13.428 1.882 1.00 29.54 ? 1062 HOH B O 1 HETATM 9680 O O . HOH WA 10 . ? 4.809 -29.684 17.197 1.00 27.35 ? 1063 HOH B O 1 HETATM 9681 O O . HOH WA 10 . ? 25.696 1.630 42.842 1.00 7.25 ? 1064 HOH B O 1 HETATM 9682 O O . HOH WA 10 . ? 4.499 -23.272 16.527 1.00 31.18 ? 1065 HOH B O 1 HETATM 9683 O O . HOH WA 10 . ? 14.979 -29.861 22.701 1.00 4.98 ? 1066 HOH B O 1 HETATM 9684 O O . HOH WA 10 . ? 12.196 -12.751 4.059 1.00 27.96 ? 1067 HOH B O 1 HETATM 9685 O O . HOH WA 10 . ? 34.948 5.280 54.016 1.00 13.76 ? 1068 HOH B O 1 HETATM 9686 O O . HOH WA 10 . ? 20.479 4.193 31.648 1.00 16.69 ? 1069 HOH B O 1 HETATM 9687 O O . HOH WA 10 . ? 5.415 -25.903 15.275 1.00 25.54 ? 1070 HOH B O 1 HETATM 9688 O O . HOH WA 10 . ? 8.052 -3.025 8.882 1.00 20.25 ? 1071 HOH B O 1 HETATM 9689 O O . HOH WA 10 . ? 8.413 -28.272 20.281 1.00 31.30 ? 1072 HOH B O 1 HETATM 9690 O O . HOH WA 10 . ? 14.831 -6.957 4.745 1.00 19.08 ? 1073 HOH B O 1 HETATM 9691 O O . HOH WA 10 . ? 26.126 7.236 51.495 1.00 21.68 ? 1074 HOH B O 1 HETATM 9692 O O . HOH WA 10 . ? 20.969 -12.661 33.958 1.00 15.74 ? 1075 HOH B O 1 HETATM 9693 O O . HOH WA 10 . ? 9.044 22.308 35.578 1.00 45.30 ? 1076 HOH B O 1 HETATM 9694 O O . HOH WA 10 . ? 10.568 -22.430 40.422 1.00 40.02 ? 1077 HOH B O 1 HETATM 9695 O O . HOH WA 10 . ? 24.899 -22.678 33.461 1.00 20.50 ? 1078 HOH B O 1 HETATM 9696 O O . HOH WA 10 . ? 23.545 11.422 3.636 1.00 21.14 ? 1079 HOH B O 1 HETATM 9697 O O . HOH WA 10 . ? 24.718 -18.963 -0.197 1.00 18.87 ? 1080 HOH B O 1 HETATM 9698 O O . HOH WA 10 . ? 39.422 10.429 34.238 1.00 24.51 ? 1081 HOH B O 1 HETATM 9699 O O . HOH WA 10 . ? -3.292 9.178 27.568 1.00 15.85 ? 1082 HOH B O 1 HETATM 9700 O O . HOH WA 10 . ? 6.951 -14.677 42.294 1.00 15.27 ? 1083 HOH B O 1 HETATM 9701 O O . HOH WA 10 . ? 1.834 -30.461 41.552 1.00 70.39 ? 1084 HOH B O 1 HETATM 9702 O O . HOH WA 10 . ? 33.201 3.342 16.869 1.00 16.03 ? 1085 HOH B O 1 HETATM 9703 O O . HOH WA 10 . ? 41.810 5.099 45.257 1.00 36.81 ? 1086 HOH B O 1 HETATM 9704 O O . HOH WA 10 . ? -1.741 -5.617 17.741 1.00 19.48 ? 1087 HOH B O 1 HETATM 9705 O O . HOH WA 10 . ? 20.336 -16.393 36.242 1.00 16.89 ? 1088 HOH B O 1 HETATM 9706 O O . HOH WA 10 . ? -4.685 19.788 21.297 1.00 11.41 ? 1089 HOH B O 1 HETATM 9707 O O . HOH WA 10 . ? 11.663 -24.642 35.115 1.00 17.90 ? 1090 HOH B O 1 HETATM 9708 O O . HOH WA 10 . ? -0.105 27.762 18.743 1.00 35.51 ? 1091 HOH B O 1 HETATM 9709 O O . HOH WA 10 . ? 29.746 -11.186 1.485 1.00 27.10 ? 1092 HOH B O 1 HETATM 9710 O O . HOH WA 10 . ? 7.386 -17.437 54.358 1.00 10.58 ? 1093 HOH B O 1 HETATM 9711 O O . HOH WA 10 . ? 6.326 5.447 39.328 1.00 17.12 ? 1094 HOH B O 1 HETATM 9712 O O . HOH WA 10 . ? 29.246 -5.550 14.788 1.00 13.38 ? 1095 HOH B O 1 HETATM 9713 O O . HOH WA 10 . ? -3.047 22.184 20.172 1.00 15.54 ? 1096 HOH B O 1 HETATM 9714 O O . HOH WA 10 . ? 38.214 -9.158 14.425 1.00 27.13 ? 1097 HOH B O 1 HETATM 9715 O O . HOH WA 10 . ? -0.285 -16.891 18.939 1.00 10.65 ? 1098 HOH B O 1 HETATM 9716 O O . HOH WA 10 . ? 40.302 -2.084 47.620 1.00 65.89 ? 1099 HOH B O 1 HETATM 9717 O O . HOH WA 10 . ? -5.684 -5.023 33.021 1.00 33.62 ? 1100 HOH B O 1 HETATM 9718 O O . HOH WA 10 . ? 18.887 5.850 54.470 1.00 29.71 ? 1101 HOH B O 1 HETATM 9719 O O . HOH WA 10 . ? 36.689 -10.380 8.268 1.00 20.46 ? 1102 HOH B O 1 HETATM 9720 O O . HOH WA 10 . ? -4.973 -21.836 42.801 1.00 15.98 ? 1103 HOH B O 1 HETATM 9721 O O . HOH WA 10 . ? 1.702 -3.165 42.738 1.00 9.59 ? 1104 HOH B O 1 HETATM 9722 O O . HOH WA 10 . ? -5.634 7.302 38.062 1.00 35.02 ? 1105 HOH B O 1 HETATM 9723 O O . HOH WA 10 . ? 11.521 -27.922 16.747 1.00 19.38 ? 1106 HOH B O 1 HETATM 9724 O O . HOH WA 10 . ? 19.252 -8.196 62.439 1.00 21.76 ? 1107 HOH B O 1 HETATM 9725 O O . HOH WA 10 . ? -7.174 -5.730 52.824 1.00 9.62 ? 1108 HOH B O 1 HETATM 9726 O O . HOH WA 10 . ? -2.882 -19.602 30.724 1.00 16.77 ? 1109 HOH B O 1 HETATM 9727 O O . HOH WA 10 . ? 19.706 1.552 59.680 1.00 28.46 ? 1110 HOH B O 1 HETATM 9728 O O . HOH WA 10 . ? 21.120 13.568 46.573 1.00 18.46 ? 1111 HOH B O 1 HETATM 9729 O O . HOH WA 10 . ? 14.544 27.516 29.388 1.00 17.44 ? 1112 HOH B O 1 HETATM 9730 O O . HOH WA 10 . ? 12.247 -19.201 3.012 1.00 35.14 ? 1113 HOH B O 1 HETATM 9731 O O . HOH WA 10 . ? -12.511 10.718 26.726 1.00 20.41 ? 1114 HOH B O 1 HETATM 9732 O O . HOH WA 10 . ? -3.858 -25.785 33.598 1.00 14.71 ? 1115 HOH B O 1 HETATM 9733 O O . HOH WA 10 . ? 32.065 -20.460 15.130 1.00 20.35 ? 1116 HOH B O 1 HETATM 9734 O O . HOH WA 10 . ? -1.203 10.894 29.908 1.00 9.19 ? 1117 HOH B O 1 HETATM 9735 O O . HOH WA 10 . ? 16.671 18.824 15.685 1.00 37.32 ? 1118 HOH B O 1 HETATM 9736 O O . HOH WA 10 . ? 15.620 -21.100 15.291 1.00 17.31 ? 1119 HOH B O 1 HETATM 9737 O O . HOH WA 10 . ? 42.851 -5.441 13.438 1.00 22.59 ? 1120 HOH B O 1 HETATM 9738 O O . HOH WA 10 . ? 13.568 -4.646 21.618 1.00 23.45 ? 1121 HOH B O 1 HETATM 9739 O O . HOH WA 10 . ? 27.757 -19.665 6.919 1.00 31.46 ? 1122 HOH B O 1 HETATM 9740 O O . HOH WA 10 . ? 11.716 -25.215 37.913 1.00 22.35 ? 1123 HOH B O 1 HETATM 9741 O O . HOH WA 10 . ? 0.604 -11.899 10.042 1.00 7.82 ? 1124 HOH B O 1 HETATM 9742 O O . HOH WA 10 . ? 18.377 -17.613 28.968 1.00 1.85 ? 1125 HOH B O 1 HETATM 9743 O O . HOH WA 10 . ? 27.253 18.650 30.950 1.00 32.38 ? 1126 HOH B O 1 HETATM 9744 O O . HOH WA 10 . ? -7.557 15.862 33.023 1.00 22.87 ? 1127 HOH B O 1 HETATM 9745 O O . HOH WA 10 . ? 43.214 -6.791 9.446 1.00 28.26 ? 1128 HOH B O 1 HETATM 9746 O O . HOH WA 10 . ? 33.703 16.348 24.336 1.00 38.68 ? 1129 HOH B O 1 HETATM 9747 O O . HOH WA 10 . ? 2.920 23.917 17.443 1.00 54.37 ? 1130 HOH B O 1 HETATM 9748 O O . HOH WA 10 . ? -7.172 -1.779 2.458 1.00 43.58 ? 1131 HOH B O 1 HETATM 9749 O O . HOH WA 10 . ? 31.308 -2.464 48.174 1.00 16.20 ? 1132 HOH B O 1 HETATM 9750 O O . HOH WA 10 . ? 39.192 -6.942 45.168 1.00 26.26 ? 1133 HOH B O 1 HETATM 9751 O O . HOH WA 10 . ? 18.502 -9.361 53.763 1.00 11.88 ? 1134 HOH B O 1 HETATM 9752 O O . HOH WA 10 . ? -3.410 -22.252 30.861 1.00 13.45 ? 1135 HOH B O 1 HETATM 9753 O O . HOH WA 10 . ? -3.372 2.608 47.697 1.00 20.07 ? 1136 HOH B O 1 HETATM 9754 O O . HOH WA 10 . ? 5.984 -0.023 48.326 1.00 17.94 ? 1137 HOH B O 1 HETATM 9755 O O . HOH WA 10 . ? -1.687 12.576 27.399 1.00 19.64 ? 1138 HOH B O 1 HETATM 9756 O O . HOH WA 10 . ? 13.761 -14.217 45.264 1.00 18.10 ? 1139 HOH B O 1 HETATM 9757 O O . HOH WA 10 . ? 21.638 -30.404 25.099 1.00 20.51 ? 1140 HOH B O 1 HETATM 9758 O O . HOH WA 10 . ? 9.048 -16.470 10.938 1.00 24.39 ? 1141 HOH B O 1 HETATM 9759 O O . HOH WA 10 . ? 7.237 26.435 20.524 1.00 53.16 ? 1142 HOH B O 1 HETATM 9760 O O . HOH WA 10 . ? 20.183 -27.219 25.787 1.00 18.69 ? 1143 HOH B O 1 HETATM 9761 O O . HOH WA 10 . ? 17.148 4.378 57.371 1.00 24.66 ? 1144 HOH B O 1 HETATM 9762 O O . HOH WA 10 . ? 3.029 6.650 4.551 1.00 15.69 ? 1145 HOH B O 1 HETATM 9763 O O . HOH WA 10 . ? 2.306 13.571 39.828 1.00 27.37 ? 1146 HOH B O 1 HETATM 9764 O O . HOH WA 10 . ? -0.835 -16.372 24.217 1.00 6.65 ? 1147 HOH B O 1 HETATM 9765 O O . HOH WA 10 . ? -2.467 -2.147 53.327 1.00 19.34 ? 1148 HOH B O 1 HETATM 9766 O O . HOH WA 10 . ? 41.193 3.703 12.852 1.00 18.13 ? 1149 HOH B O 1 HETATM 9767 O O . HOH WA 10 . ? 34.337 8.661 29.117 1.00 51.03 ? 1150 HOH B O 1 HETATM 9768 O O . HOH WA 10 . ? 31.022 -3.173 51.027 1.00 22.82 ? 1151 HOH B O 1 HETATM 9769 O O . HOH WA 10 . ? 0.773 13.682 14.254 1.00 17.54 ? 1152 HOH B O 1 HETATM 9770 O O . HOH WA 10 . ? 16.123 21.650 40.014 1.00 25.51 ? 1153 HOH B O 1 HETATM 9771 O O . HOH WA 10 . ? 1.286 17.754 14.382 1.00 33.20 ? 1154 HOH B O 1 HETATM 9772 O O . HOH WA 10 . ? 9.141 -30.769 19.958 1.00 18.77 ? 1155 HOH B O 1 HETATM 9773 O O . HOH WA 10 . ? 17.506 -30.473 23.649 1.00 16.11 ? 1156 HOH B O 1 HETATM 9774 O O . HOH WA 10 . ? 4.211 6.961 37.869 1.00 15.56 ? 1157 HOH B O 1 HETATM 9775 O O . HOH WA 10 . ? 29.578 -3.176 45.659 1.00 25.36 ? 1158 HOH B O 1 HETATM 9776 O O . HOH WA 10 . ? 12.285 20.283 8.376 1.00 44.56 ? 1159 HOH B O 1 HETATM 9777 O O . HOH WA 10 . ? 19.705 26.447 29.833 1.00 23.89 ? 1160 HOH B O 1 HETATM 9778 O O . HOH WA 10 . ? 14.044 -21.256 51.260 1.00 21.43 ? 1161 HOH B O 1 HETATM 9779 O O . HOH WA 10 . ? 27.117 -26.738 12.849 1.00 13.51 ? 1162 HOH B O 1 HETATM 9780 O O . HOH WA 10 . ? 1.638 -21.284 5.611 1.00 34.43 ? 1163 HOH B O 1 HETATM 9781 O O . HOH WA 10 . ? 12.832 13.648 46.399 1.00 32.52 ? 1164 HOH B O 1 HETATM 9782 O O . HOH WA 10 . ? 0.607 2.892 2.803 1.00 24.05 ? 1165 HOH B O 1 HETATM 9783 O O . HOH WA 10 . ? 9.930 17.146 32.508 1.00 49.33 ? 1166 HOH B O 1 HETATM 9784 O O . HOH WA 10 . ? -0.156 -17.066 15.752 1.00 10.40 ? 1167 HOH B O 1 HETATM 9785 O O . HOH WA 10 . ? -9.524 5.626 35.389 1.00 23.00 ? 1168 HOH B O 1 HETATM 9786 O O . HOH WA 10 . ? -0.477 -1.132 52.482 1.00 17.68 ? 1169 HOH B O 1 HETATM 9787 O O . HOH WA 10 . ? 36.085 1.099 40.510 1.00 19.06 ? 1170 HOH B O 1 HETATM 9788 O O . HOH WA 10 . ? 10.833 -13.272 16.893 1.00 15.18 ? 1171 HOH B O 1 HETATM 9789 O O . HOH WA 10 . ? 22.617 3.831 39.103 1.00 8.78 ? 1172 HOH B O 1 HETATM 9790 O O . HOH WA 10 . ? 24.975 8.500 49.510 1.00 14.92 ? 1173 HOH B O 1 HETATM 9791 O O . HOH WA 10 . ? 31.740 -16.252 33.180 1.00 35.63 ? 1174 HOH B O 1 HETATM 9792 O O . HOH WA 10 . ? 38.216 8.618 32.251 1.00 30.96 ? 1175 HOH B O 1 HETATM 9793 O O . HOH WA 10 . ? 33.120 -13.060 35.219 1.00 21.44 ? 1176 HOH B O 1 HETATM 9794 O O . HOH WA 10 . ? 38.893 -3.714 50.220 1.00 23.17 ? 1177 HOH B O 1 HETATM 9795 O O . HOH WA 10 . ? 20.056 -26.169 20.456 1.00 14.84 ? 1178 HOH B O 1 HETATM 9796 O O . HOH WA 10 . ? 3.298 15.392 10.872 1.00 24.73 ? 1179 HOH B O 1 HETATM 9797 O O . HOH WA 10 . ? 29.195 7.130 4.549 1.00 31.27 ? 1180 HOH B O 1 HETATM 9798 O O . HOH WA 10 . ? 33.361 -5.724 44.949 1.00 27.80 ? 1181 HOH B O 1 HETATM 9799 O O . HOH WA 10 . ? 34.837 13.649 40.272 1.00 16.90 ? 1182 HOH B O 1 HETATM 9800 O O . HOH WA 10 . ? 6.423 -20.282 47.303 1.00 21.92 ? 1183 HOH B O 1 HETATM 9801 O O . HOH WA 10 . ? 34.586 -10.521 17.984 1.00 25.24 ? 1184 HOH B O 1 HETATM 9802 O O . HOH WA 10 . ? 31.420 1.027 26.183 1.00 39.20 ? 1185 HOH B O 1 HETATM 9803 O O . HOH WA 10 . ? 14.536 -23.278 14.633 1.00 12.76 ? 1186 HOH B O 1 HETATM 9804 O O . HOH WA 10 . ? 35.293 -2.698 22.058 1.00 24.40 ? 1187 HOH B O 1 HETATM 9805 O O . HOH WA 10 . ? -2.361 -13.203 12.315 1.00 17.11 ? 1188 HOH B O 1 HETATM 9806 O O . HOH WA 10 . ? 5.415 -0.298 4.421 1.00 10.30 ? 1189 HOH B O 1 HETATM 9807 O O . HOH WA 10 . ? 20.032 -1.933 7.039 1.00 25.68 ? 1190 HOH B O 1 HETATM 9808 O O . HOH WA 10 . ? 22.085 5.650 -5.153 1.00 25.37 ? 1191 HOH B O 1 HETATM 9809 O O . HOH WA 10 . ? 8.573 18.928 35.835 1.00 18.30 ? 1192 HOH B O 1 HETATM 9810 O O . HOH WA 10 . ? 19.067 -27.433 11.062 1.00 20.79 ? 1193 HOH B O 1 HETATM 9811 O O . HOH WA 10 . ? 4.717 -7.339 7.995 1.00 14.38 ? 1194 HOH B O 1 HETATM 9812 O O . HOH WA 10 . ? 23.869 14.061 28.965 1.00 33.61 ? 1195 HOH B O 1 HETATM 9813 O O . HOH WA 10 . ? -4.664 -19.163 42.303 1.00 16.89 ? 1196 HOH B O 1 HETATM 9814 O O . HOH WA 10 . ? 4.067 -22.273 5.525 1.00 29.04 ? 1197 HOH B O 1 HETATM 9815 O O . HOH WA 10 . ? 20.180 16.670 42.230 1.00 17.01 ? 1198 HOH B O 1 HETATM 9816 O O . HOH WA 10 . ? 23.016 3.662 41.745 1.00 11.91 ? 1199 HOH B O 1 HETATM 9817 O O . HOH WA 10 . ? 24.698 20.679 31.428 1.00 36.35 ? 1200 HOH B O 1 HETATM 9818 O O . HOH WA 10 . ? 4.207 -30.853 25.535 1.00 24.00 ? 1201 HOH B O 1 HETATM 9819 O O . HOH WA 10 . ? 23.858 -9.370 39.911 1.00 6.30 ? 1202 HOH B O 1 HETATM 9820 O O . HOH WA 10 . ? 41.084 5.471 41.126 1.00 11.88 ? 1203 HOH B O 1 HETATM 9821 O O . HOH WA 10 . ? 14.416 -27.910 17.920 1.00 23.77 ? 1204 HOH B O 1 HETATM 9822 O O . HOH WA 10 . ? -6.333 10.328 10.867 1.00 32.15 ? 1205 HOH B O 1 HETATM 9823 O O . HOH WA 10 . ? 18.629 -20.422 57.543 1.00 22.62 ? 1206 HOH B O 1 HETATM 9824 O O . HOH WA 10 . ? 37.023 11.721 38.088 1.00 23.04 ? 1207 HOH B O 1 HETATM 9825 O O . HOH WA 10 . ? 20.004 24.007 23.217 1.00 20.15 ? 1208 HOH B O 1 HETATM 9826 O O . HOH WA 10 . ? 13.850 24.302 18.011 1.00 31.84 ? 1209 HOH B O 1 HETATM 9827 O O . HOH WA 10 . ? 0.281 3.003 50.757 1.00 26.18 ? 1210 HOH B O 1 HETATM 9828 O O . HOH WA 10 . ? 41.335 10.818 35.929 1.00 56.22 ? 1211 HOH B O 1 HETATM 9829 O O . HOH WA 10 . ? -8.228 -14.531 53.001 1.00 33.26 ? 1212 HOH B O 1 HETATM 9830 O O . HOH WA 10 . ? 14.234 -6.312 19.918 1.00 20.50 ? 1213 HOH B O 1 HETATM 9831 O O . HOH WA 10 . ? 10.740 -4.486 21.839 1.00 30.53 ? 1214 HOH B O 1 HETATM 9832 O O . HOH WA 10 . ? 31.540 -17.806 13.700 1.00 6.69 ? 1215 HOH B O 1 HETATM 9833 O O . HOH WA 10 . ? -7.102 0.641 26.471 1.00 26.62 ? 1216 HOH B O 1 HETATM 9834 O O . HOH WA 10 . ? -6.583 -11.543 35.352 1.00 12.79 ? 1217 HOH B O 1 HETATM 9835 O O . HOH WA 10 . ? 13.248 -25.563 13.324 1.00 24.86 ? 1218 HOH B O 1 HETATM 9836 O O . HOH WA 10 . ? -13.850 1.112 19.194 1.00 23.50 ? 1219 HOH B O 1 HETATM 9837 O O . HOH WA 10 . ? 9.745 -17.944 18.701 1.00 16.75 ? 1220 HOH B O 1 HETATM 9838 O O . HOH WA 10 . ? 23.789 11.774 46.621 1.00 23.03 ? 1221 HOH B O 1 HETATM 9839 O O . HOH WA 10 . ? 20.377 11.372 47.678 1.00 20.44 ? 1222 HOH B O 1 HETATM 9840 O O . HOH WA 10 . ? 18.545 12.854 49.610 1.00 22.28 ? 1223 HOH B O 1 HETATM 9841 O O . HOH WA 10 . ? -3.252 -6.214 26.501 1.00 16.79 ? 1224 HOH B O 1 HETATM 9842 O O . HOH WA 10 . ? 2.079 0.615 50.218 1.00 21.61 ? 1225 HOH B O 1 HETATM 9843 O O . HOH WA 10 . ? 14.968 11.265 51.612 1.00 23.22 ? 1226 HOH B O 1 HETATM 9844 O O . HOH WA 10 . ? -5.684 -14.370 56.548 1.00 20.19 ? 1227 HOH B O 1 HETATM 9845 O O . HOH WA 10 . ? 4.765 18.282 32.027 1.00 32.52 ? 1228 HOH B O 1 HETATM 9846 O O . HOH WA 10 . ? 39.729 6.430 16.366 1.00 27.77 ? 1229 HOH B O 1 HETATM 9847 O O . HOH WA 10 . ? 31.808 -3.150 5.153 1.00 19.71 ? 1230 HOH B O 1 HETATM 9848 O O . HOH WA 10 . ? 26.520 -22.241 3.497 1.00 16.29 ? 1231 HOH B O 1 HETATM 9849 O O . HOH WA 10 . ? 8.461 -8.556 5.809 1.00 19.18 ? 1232 HOH B O 1 HETATM 9850 O O . HOH WA 10 . ? 11.672 -6.917 20.164 1.00 25.65 ? 1233 HOH B O 1 HETATM 9851 O O . HOH WA 10 . ? -7.297 7.109 7.588 1.00 18.30 ? 1234 HOH B O 1 HETATM 9852 O O . HOH WA 10 . ? 4.235 -7.455 5.016 1.00 20.70 ? 1235 HOH B O 1 HETATM 9853 O O . HOH WA 10 . ? -7.962 17.100 29.082 1.00 30.40 ? 1236 HOH B O 1 HETATM 9854 O O . HOH WA 10 . ? 24.635 10.948 25.871 1.00 35.15 ? 1237 HOH B O 1 HETATM 9855 O O . HOH WA 10 . ? 21.546 4.451 28.749 1.00 15.07 ? 1238 HOH B O 1 HETATM 9856 O O . HOH WA 10 . ? 0.524 17.261 34.074 1.00 18.40 ? 1239 HOH B O 1 # 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 GLU 1 1 ? ? ? A . n A 1 2 PRO 2 2 2 PRO PRO A . n A 1 3 THR 3 3 3 THR THR A . n A 1 4 CYS 4 4 4 CYS CYS A . n A 1 5 ASN 5 5 5 ASN ASN A . n A 1 6 THR 6 6 6 THR THR A . n A 1 7 PRO 7 7 7 PRO PRO A . n A 1 8 SER 8 8 8 SER SER A . n A 1 9 ASN 9 9 9 ASN ASN A . n A 1 10 ARG 10 10 10 ARG ARG A . n A 1 11 ALA 11 11 11 ALA ALA A . n A 1 12 CYS 12 12 12 CYS CYS A . n A 1 13 TRP 13 13 13 TRP TRP A . n A 1 14 SER 14 14 14 SER SER A . n A 1 15 ASP 15 15 15 ASP ASP A . n A 1 16 GLY 16 16 16 GLY GLY A . n A 1 17 PHE 17 17 17 PHE PHE A . n A 1 18 ASP 18 18 18 ASP ASP A . n A 1 19 ILE 19 19 19 ILE ILE A . n A 1 20 ASN 20 20 20 ASN ASN A . n A 1 21 THR 21 21 21 THR THR A . n A 1 22 ASP 22 22 22 ASP ASP A . n A 1 23 TYR 23 23 23 TYR TYR A . n A 1 24 GLU 24 24 24 GLU GLU A . n A 1 25 VAL 25 25 25 VAL VAL A . n A 1 26 SER 26 26 26 SER SER A . n A 1 27 THR 27 27 27 THR THR A . n A 1 28 PRO 28 28 28 PRO PRO A . n A 1 29 ASP 29 29 29 ASP ASP A . n A 1 30 THR 30 30 30 THR THR A . n A 1 31 GLY 31 31 31 GLY GLY A . n A 1 32 VAL 32 32 32 VAL VAL A . n A 1 33 THR 33 33 33 THR THR A . n A 1 34 GLN 34 34 34 GLN GLN A . n A 1 35 SER 35 35 35 SER SER A . n A 1 36 TYR 36 36 36 TYR TYR A . n A 1 37 VAL 37 37 37 VAL VAL A . n A 1 38 PHE 38 38 38 PHE PHE A . n A 1 39 ASN 39 39 39 ASN ASN A . n A 1 40 LEU 40 40 40 LEU LEU A . n A 1 41 THR 41 41 41 THR THR A . n A 1 42 GLU 42 42 42 GLU GLU A . n A 1 43 VAL 43 43 43 VAL VAL A . n A 1 44 ASP 44 44 44 ASP ASP A . n A 1 45 ASN 45 45 45 ASN ASN A . n A 1 46 TRP 46 46 46 TRP TRP A . n A 1 47 MET 47 47 47 MET MET A . n A 1 48 GLY 48 48 48 GLY GLY A . n A 1 49 PRO 49 49 49 PRO PRO A . n A 1 50 ASP 50 50 50 ASP ASP A . n A 1 51 GLY 51 51 51 GLY GLY A . n A 1 52 VAL 52 52 52 VAL VAL A . n A 1 53 VAL 53 53 53 VAL VAL A . n A 1 54 LYS 54 54 54 LYS LYS A . n A 1 55 GLU 55 55 55 GLU GLU A . n A 1 56 LYS 56 56 56 LYS LYS A . n A 1 57 VAL 57 57 57 VAL VAL A . n A 1 58 MET 58 58 58 MET MET A . n A 1 59 LEU 59 59 59 LEU LEU A . n A 1 60 ILE 60 60 60 ILE ILE A . n A 1 61 ASN 61 61 61 ASN ASN A . n A 1 62 GLY 62 62 62 GLY GLY A . n A 1 63 ASN 63 63 63 ASN ASN A . n A 1 64 ILE 64 64 64 ILE ILE A . n A 1 65 MET 65 65 65 MET MET A . n A 1 66 GLY 66 66 66 GLY GLY A . n A 1 67 PRO 67 67 67 PRO PRO A . n A 1 68 ASN 68 68 68 ASN ASN A . n A 1 69 ILE 69 69 69 ILE ILE A . n A 1 70 VAL 70 70 70 VAL VAL A . n A 1 71 ALA 71 71 71 ALA ALA A . n A 1 72 ASN 72 72 72 ASN ASN A . n A 1 73 TRP 73 73 73 TRP TRP A . n A 1 74 GLY 74 74 74 GLY GLY A . n A 1 75 ASP 75 75 75 ASP ASP A . n A 1 76 THR 76 76 76 THR THR A . n A 1 77 VAL 77 77 77 VAL VAL A . n A 1 78 GLU 78 78 78 GLU GLU A . n A 1 79 VAL 79 79 79 VAL VAL A . n A 1 80 THR 80 80 80 THR THR A . n A 1 81 VAL 81 81 81 VAL VAL A . n A 1 82 ILE 82 82 82 ILE ILE A . n A 1 83 ASN 83 83 83 ASN ASN A . n A 1 84 ASN 84 84 84 ASN ASN A . n A 1 85 LEU 85 85 85 LEU LEU A . n A 1 86 VAL 86 86 86 VAL VAL A . n A 1 87 THR 87 87 87 THR THR A . n A 1 88 ASN 88 88 88 ASN ASN A . n A 1 89 GLY 89 89 89 GLY GLY A . n A 1 90 THR 90 90 90 THR THR A . n A 1 91 SER 91 91 91 SER SER A . n A 1 92 ILE 92 92 92 ILE ILE A . n A 1 93 HIS 93 93 93 HIS HIS A . n A 1 94 TRP 94 94 94 TRP TRP A . n A 1 95 HIS 95 95 95 HIS HIS A . n A 1 96 GLY 96 96 96 GLY GLY A . n A 1 97 ILE 97 97 97 ILE ILE A . n A 1 98 HIS 98 98 98 HIS HIS A . n A 1 99 GLN 99 99 99 GLN GLN A . n A 1 100 LYS 100 100 100 LYS LYS A . n A 1 101 ASP 101 101 101 ASP ASP A . n A 1 102 THR 102 102 102 THR THR A . n A 1 103 ASN 103 103 103 ASN ASN A . n A 1 104 LEU 104 104 104 LEU LEU A . n A 1 105 HIS 105 105 105 HIS HIS A . n A 1 106 ASP 106 106 106 ASP ASP A . n A 1 107 GLY 107 107 107 GLY GLY A . n A 1 108 ALA 108 108 108 ALA ALA A . n A 1 109 ASN 109 109 109 ASN ASN A . n A 1 110 GLY 110 110 110 GLY GLY A . n A 1 111 VAL 111 111 111 VAL VAL A . n A 1 112 THR 112 112 112 THR THR A . n A 1 113 GLU 113 113 113 GLU GLU A . n A 1 114 CYS 114 114 114 CYS CYS A . n A 1 115 PRO 115 115 115 PRO PRO A . n A 1 116 ILE 116 116 116 ILE ILE A . n A 1 117 PRO 117 117 117 PRO PRO A . n A 1 118 PRO 118 118 118 PRO PRO A . n A 1 119 LYS 119 119 119 LYS LYS A . n A 1 120 GLY 120 120 120 GLY GLY A . n A 1 121 GLY 121 121 121 GLY GLY A . n A 1 122 GLN 122 122 122 GLN GLN A . n A 1 123 ARG 123 123 123 ARG ARG A . n A 1 124 THR 124 124 124 THR THR A . n A 1 125 TYR 125 125 125 TYR TYR A . n A 1 126 ARG 126 126 126 ARG ARG A . n A 1 127 TRP 127 127 127 TRP TRP A . n A 1 128 ARG 128 128 128 ARG ARG A . n A 1 129 ALA 129 129 129 ALA ALA A . n A 1 130 ARG 130 130 130 ARG ARG A . n A 1 131 GLN 131 131 131 GLN GLN A . n A 1 132 TYR 132 132 132 TYR TYR A . n A 1 133 GLY 133 133 133 GLY GLY A . n A 1 134 THR 134 134 134 THR THR A . n A 1 135 SER 135 135 135 SER SER A . n A 1 136 TRP 136 136 136 TRP TRP A . n A 1 137 TYR 137 137 137 TYR TYR A . n A 1 138 HIS 138 138 138 HIS HIS A . n A 1 139 SER 139 139 139 SER SER A . n A 1 140 HIS 140 140 140 HIS HIS A . n A 1 141 PHE 141 141 141 PHE PHE A . n A 1 142 SER 142 142 142 SER SER A . n A 1 143 ALA 143 143 143 ALA ALA A . n A 1 144 GLN 144 144 144 GLN GLN A . n A 1 145 TYR 145 145 145 TYR TYR A . n A 1 146 GLY 146 146 146 GLY GLY A . n A 1 147 ASN 147 147 147 ASN ASN A . n A 1 148 GLY 148 148 148 GLY GLY A . n A 1 149 VAL 149 149 149 VAL VAL A . n A 1 150 VAL 150 150 150 VAL VAL A . n A 1 151 GLY 151 151 151 GLY GLY A . n A 1 152 THR 152 152 152 THR THR A . n A 1 153 ILE 153 153 153 ILE ILE A . n A 1 154 GLN 154 154 154 GLN GLN A . n A 1 155 ILE 155 155 155 ILE ILE A . n A 1 156 ASN 156 156 156 ASN ASN A . n A 1 157 GLY 157 157 157 GLY GLY A . n A 1 158 PRO 158 158 158 PRO PRO A . n A 1 159 ALA 159 159 159 ALA ALA A . n A 1 160 SER 160 160 160 SER SER A . n A 1 161 LEU 161 161 161 LEU LEU A . n A 1 162 PRO 162 162 162 PRO PRO A . n A 1 163 TYR 163 163 163 TYR TYR A . n A 1 164 ASP 164 164 164 ASP ASP A . n A 1 165 ILE 165 165 165 ILE ILE A . n A 1 166 ASP 166 166 166 ASP ASP A . n A 1 167 LEU 167 167 167 LEU LEU A . n A 1 168 GLY 168 168 168 GLY GLY A . n A 1 169 VAL 169 169 169 VAL VAL A . n A 1 170 PHE 170 170 170 PHE PHE A . n A 1 171 PRO 171 171 171 PRO PRO A . n A 1 172 ILE 172 172 172 ILE ILE A . n A 1 173 THR 173 173 173 THR THR A . n A 1 174 ASP 174 174 174 ASP ASP A . n A 1 175 TYR 175 175 175 TYR TYR A . n A 1 176 TYR 176 176 176 TYR TYR A . n A 1 177 TYR 177 177 177 TYR TYR A . n A 1 178 ARG 178 178 178 ARG ARG A . n A 1 179 ALA 179 179 179 ALA ALA A . n A 1 180 ALA 180 180 180 ALA ALA A . n A 1 181 ASP 181 181 181 ASP ASP A . n A 1 182 ASP 182 182 182 ASP ASP A . n A 1 183 LEU 183 183 183 LEU LEU A . n A 1 184 VAL 184 184 184 VAL VAL A . n A 1 185 HIS 185 185 185 HIS HIS A . n A 1 186 PHE 186 186 186 PHE PHE A . n A 1 187 THR 187 187 187 THR THR A . n A 1 188 GLN 188 188 188 GLN GLN A . n A 1 189 ASN 189 189 189 ASN ASN A . n A 1 190 ASN 190 190 190 ASN ASN A . n A 1 191 ALA 191 191 191 ALA ALA A . n A 1 192 PRO 192 192 192 PRO PRO A . n A 1 193 PRO 193 193 193 PRO PRO A . n A 1 194 PHE 194 194 194 PHE PHE A . n A 1 195 SER 195 195 195 SER SER A . n A 1 196 ASP 196 196 196 ASP ASP A . n A 1 197 ASN 197 197 197 ASN ASN A . n A 1 198 VAL 198 198 198 VAL VAL A . n A 1 199 LEU 199 199 199 LEU LEU A . n A 1 200 ILE 200 200 200 ILE ILE A . n A 1 201 ASN 201 201 201 ASN ASN A . n A 1 202 GLY 202 202 202 GLY GLY A . n A 1 203 THR 203 203 203 THR THR A . n A 1 204 ALA 204 204 204 ALA ALA A . n A 1 205 VAL 205 205 205 VAL VAL A . n A 1 206 ASN 206 206 206 ASN ASN A . n A 1 207 PRO 207 207 207 PRO PRO A . n A 1 208 ASN 208 208 208 ASN ASN A . n A 1 209 THR 209 209 209 THR THR A . n A 1 210 GLY 210 210 210 GLY GLY A . n A 1 211 GLU 211 211 211 GLU GLU A . n A 1 212 GLY 212 212 212 GLY GLY A . n A 1 213 GLN 213 213 213 GLN GLN A . n A 1 214 TYR 214 214 214 TYR TYR A . n A 1 215 ALA 215 215 215 ALA ALA A . n A 1 216 ASN 216 216 216 ASN ASN A . n A 1 217 VAL 217 217 217 VAL VAL A . n A 1 218 THR 218 218 218 THR THR A . n A 1 219 LEU 219 219 219 LEU LEU A . n A 1 220 THR 220 220 220 THR THR A . n A 1 221 PRO 221 221 221 PRO PRO A . n A 1 222 GLY 222 222 222 GLY GLY A . n A 1 223 LYS 223 223 223 LYS LYS A . n A 1 224 ARG 224 224 224 ARG ARG A . n A 1 225 HIS 225 225 225 HIS HIS A . n A 1 226 ARG 226 226 226 ARG ARG A . n A 1 227 LEU 227 227 227 LEU LEU A . n A 1 228 ARG 228 228 228 ARG ARG A . n A 1 229 ILE 229 229 229 ILE ILE A . n A 1 230 LEU 230 230 230 LEU LEU A . n A 1 231 ASN 231 231 231 ASN ASN A . n A 1 232 THR 232 232 232 THR THR A . n A 1 233 SER 233 233 233 SER SER A . n A 1 234 THR 234 234 234 THR THR A . n A 1 235 GLU 235 235 235 GLU GLU A . n A 1 236 ASN 236 236 236 ASN ASN A . n A 1 237 HIS 237 237 237 HIS HIS A . n A 1 238 PHE 238 238 238 PHE PHE A . n A 1 239 GLN 239 239 239 GLN GLN A . n A 1 240 VAL 240 240 240 VAL VAL A . n A 1 241 SER 241 241 241 SER SER A . n A 1 242 LEU 242 242 242 LEU LEU A . n A 1 243 VAL 243 243 243 VAL VAL A . n A 1 244 ASN 244 244 244 ASN ASN A . n A 1 245 HIS 245 245 245 HIS HIS A . n A 1 246 THR 246 246 246 THR THR A . n A 1 247 MET 247 247 247 MET MET A . n A 1 248 THR 248 248 248 THR THR A . n A 1 249 VAL 249 249 249 VAL VAL A . n A 1 250 ILE 250 250 250 ILE ILE A . n A 1 251 ALA 251 251 251 ALA ALA A . n A 1 252 ALA 252 252 252 ALA ALA A . n A 1 253 ASP 253 253 253 ASP ASP A . n A 1 254 MET 254 254 254 MET MET A . n A 1 255 VAL 255 255 255 VAL VAL A . n A 1 256 PRO 256 256 256 PRO PRO A . n A 1 257 VAL 257 257 257 VAL VAL A . n A 1 258 ASN 258 258 258 ASN ASN A . n A 1 259 ALA 259 259 259 ALA ALA A . n A 1 260 MET 260 260 260 MET MET A . n A 1 261 THR 261 261 261 THR THR A . n A 1 262 VAL 262 262 262 VAL VAL A . n A 1 263 ASP 263 263 263 ASP ASP A . n A 1 264 SER 264 264 264 SER SER A . n A 1 265 LEU 265 265 265 LEU LEU A . n A 1 266 PHE 266 266 266 PHE PHE A . n A 1 267 LEU 267 267 267 LEU LEU A . n A 1 268 ALA 268 268 268 ALA ALA A . n A 1 269 VAL 269 269 269 VAL VAL A . n A 1 270 GLY 270 270 270 GLY GLY A . n A 1 271 GLN 271 271 271 GLN GLN A . n A 1 272 ARG 272 272 272 ARG ARG A . n A 1 273 TYR 273 273 273 TYR TYR A . n A 1 274 ASP 274 274 274 ASP ASP A . n A 1 275 VAL 275 275 275 VAL VAL A . n A 1 276 VAL 276 276 276 VAL VAL A . n A 1 277 ILE 277 277 277 ILE ILE A . n A 1 278 ASP 278 278 278 ASP ASP A . n A 1 279 ALA 279 279 279 ALA ALA A . n A 1 280 SER 280 280 280 SER SER A . n A 1 281 ARG 281 281 281 ARG ARG A . n A 1 282 ALA 282 282 282 ALA ALA A . n A 1 283 PRO 283 283 283 PRO PRO A . n A 1 284 ASP 284 284 284 ASP ASP A . n A 1 285 ASN 285 285 285 ASN ASN A . n A 1 286 TYR 286 286 286 TYR TYR A . n A 1 287 TRP 287 287 287 TRP TRP A . n A 1 288 PHE 288 288 288 PHE PHE A . n A 1 289 ASN 289 289 289 ASN ASN A . n A 1 290 VAL 290 290 290 VAL VAL A . n A 1 291 THR 291 291 291 THR THR A . n A 1 292 PHE 292 292 292 PHE PHE A . n A 1 293 GLY 293 293 293 GLY GLY A . n A 1 294 GLY 294 294 294 GLY GLY A . n A 1 295 GLN 295 295 295 GLN GLN A . n A 1 296 ALA 296 296 296 ALA ALA A . n A 1 297 ALA 297 297 297 ALA ALA A . n A 1 298 CYS 298 298 298 CYS CYS A . n A 1 299 GLY 299 299 299 GLY GLY A . n A 1 300 GLY 300 300 300 GLY GLY A . n A 1 301 SER 301 301 301 SER SER A . n A 1 302 LEU 302 302 302 LEU LEU A . n A 1 303 ASN 303 303 303 ASN ASN A . n A 1 304 PRO 304 304 304 PRO PRO A . n A 1 305 HIS 305 305 305 HIS HIS A . n A 1 306 PRO 306 306 306 PRO PRO A . n A 1 307 ALA 307 307 307 ALA ALA A . n A 1 308 ALA 308 308 308 ALA ALA A . n A 1 309 ILE 309 309 309 ILE ILE A . n A 1 310 PHE 310 310 310 PHE PHE A . n A 1 311 HIS 311 311 311 HIS HIS A . n A 1 312 TYR 312 312 312 TYR TYR A . n A 1 313 ALA 313 313 313 ALA ALA A . n A 1 314 GLY 314 314 314 GLY GLY A . n A 1 315 ALA 315 315 315 ALA ALA A . n A 1 316 PRO 316 316 316 PRO PRO A . n A 1 317 GLY 317 317 317 GLY GLY A . n A 1 318 GLY 318 318 318 GLY GLY A . n A 1 319 LEU 319 319 319 LEU LEU A . n A 1 320 PRO 320 320 320 PRO PRO A . n A 1 321 THR 321 321 321 THR THR A . n A 1 322 ASP 322 322 322 ASP ASP A . n A 1 323 GLU 323 323 323 GLU GLU A . n A 1 324 GLY 324 324 324 GLY GLY A . n A 1 325 THR 325 325 325 THR THR A . n A 1 326 PRO 326 326 326 PRO PRO A . n A 1 327 PRO 327 327 327 PRO PRO A . n A 1 328 VAL 328 328 328 VAL VAL A . n A 1 329 ASP 329 329 329 ASP ASP A . n A 1 330 HIS 330 330 330 HIS HIS A . n A 1 331 GLN 331 331 331 GLN GLN A . n A 1 332 CYS 332 332 332 CYS CYS A . n A 1 333 LEU 333 333 333 LEU LEU A . n A 1 334 ASP 334 334 334 ASP ASP A . n A 1 335 THR 335 335 335 THR THR A . n A 1 336 LEU 336 336 336 LEU LEU A . n A 1 337 ASP 337 337 337 ASP ASP A . n A 1 338 VAL 338 338 338 VAL VAL A . n A 1 339 ARG 339 339 339 ARG ARG A . n A 1 340 PRO 340 340 340 PRO PRO A . n A 1 341 VAL 341 341 341 VAL VAL A . n A 1 342 VAL 342 342 342 VAL VAL A . n A 1 343 PRO 343 343 343 PRO PRO A . n A 1 344 ARG 344 344 344 ARG ARG A . n A 1 345 SER 345 345 345 SER SER A . n A 1 346 VAL 346 346 346 VAL VAL A . n A 1 347 PRO 347 347 347 PRO PRO A . n A 1 348 VAL 348 348 348 VAL VAL A . n A 1 349 ASN 349 349 349 ASN ASN A . n A 1 350 SER 350 350 350 SER SER A . n A 1 351 PHE 351 351 351 PHE PHE A . n A 1 352 VAL 352 352 352 VAL VAL A . n A 1 353 LYS 353 353 353 LYS LYS A . n A 1 354 ARG 354 354 354 ARG ARG A . n A 1 355 PRO 355 355 355 PRO PRO A . n A 1 356 ASP 356 356 356 ASP ASP A . n A 1 357 ASN 357 357 357 ASN ASN A . n A 1 358 THR 358 358 358 THR THR A . n A 1 359 LEU 359 359 359 LEU LEU A . n A 1 360 PRO 360 360 360 PRO PRO A . n A 1 361 VAL 361 361 361 VAL VAL A . n A 1 362 ALA 362 362 362 ALA ALA A . n A 1 363 LEU 363 363 363 LEU LEU A . n A 1 364 ASP 364 364 364 ASP ASP A . n A 1 365 LEU 365 365 365 LEU LEU A . n A 1 366 THR 366 366 366 THR THR A . n A 1 367 GLY 367 367 367 GLY GLY A . n A 1 368 THR 368 368 368 THR THR A . n A 1 369 PRO 369 369 369 PRO PRO A . n A 1 370 LEU 370 370 370 LEU LEU A . n A 1 371 PHE 371 371 371 PHE PHE A . n A 1 372 VAL 372 372 372 VAL VAL A . n A 1 373 TRP 373 373 373 TRP TRP A . n A 1 374 LYS 374 374 374 LYS LYS A . n A 1 375 VAL 375 375 375 VAL VAL A . n A 1 376 ASN 376 376 376 ASN ASN A . n A 1 377 GLY 377 377 377 GLY GLY A . n A 1 378 SER 378 378 378 SER SER A . n A 1 379 ASP 379 379 379 ASP ASP A . n A 1 380 ILE 380 380 380 ILE ILE A . n A 1 381 ASN 381 381 381 ASN ASN A . n A 1 382 VAL 382 382 382 VAL VAL A . n A 1 383 ASP 383 383 383 ASP ASP A . n A 1 384 TRP 384 384 384 TRP TRP A . n A 1 385 GLY 385 385 385 GLY GLY A . n A 1 386 LYS 386 386 386 LYS LYS A . n A 1 387 PRO 387 387 387 PRO PRO A . n A 1 388 ILE 388 388 388 ILE ILE A . n A 1 389 ILE 389 389 389 ILE ILE A . n A 1 390 ASP 390 390 390 ASP ASP A . n A 1 391 TYR 391 391 391 TYR TYR A . n A 1 392 ILE 392 392 392 ILE ILE A . n A 1 393 LEU 393 393 393 LEU LEU A . n A 1 394 THR 394 394 394 THR THR A . n A 1 395 GLY 395 395 395 GLY GLY A . n A 1 396 ASN 396 396 396 ASN ASN A . n A 1 397 THR 397 397 397 THR THR A . n A 1 398 SER 398 398 398 SER SER A . n A 1 399 TYR 399 399 399 TYR TYR A . n A 1 400 PRO 400 400 400 PRO PRO A . n A 1 401 VAL 401 401 401 VAL VAL A . n A 1 402 SER 402 402 402 SER SER A . n A 1 403 ASP 403 403 403 ASP ASP A . n A 1 404 ASN 404 404 404 ASN ASN A . n A 1 405 ILE 405 405 405 ILE ILE A . n A 1 406 VAL 406 406 406 VAL VAL A . n A 1 407 GLN 407 407 407 GLN GLN A . n A 1 408 VAL 408 408 408 VAL VAL A . n A 1 409 ASP 409 409 409 ASP ASP A . n A 1 410 ALA 410 410 410 ALA ALA A . n A 1 411 VAL 411 411 411 VAL VAL A . n A 1 412 ASP 412 412 412 ASP ASP A . n A 1 413 GLN 413 413 413 GLN GLN A . n A 1 414 TRP 414 414 414 TRP TRP A . n A 1 415 THR 415 415 415 THR THR A . n A 1 416 TYR 416 416 416 TYR TYR A . n A 1 417 TRP 417 417 417 TRP TRP A . n A 1 418 LEU 418 418 418 LEU LEU A . n A 1 419 ILE 419 419 419 ILE ILE A . n A 1 420 GLU 420 420 420 GLU GLU A . n A 1 421 ASN 421 421 421 ASN ASN A . n A 1 422 ASP 422 422 422 ASP ASP A . n A 1 423 PRO 423 423 423 PRO PRO A . n A 1 424 GLU 424 424 424 GLU GLU A . n A 1 425 GLY 425 425 425 GLY GLY A . n A 1 426 PRO 426 426 426 PRO PRO A . n A 1 427 PHE 427 427 427 PHE PHE A . n A 1 428 SER 428 428 428 SER SER A . n A 1 429 LEU 429 429 429 LEU LEU A . n A 1 430 PRO 430 430 430 PRO PRO A . n A 1 431 HIS 431 431 431 HIS HIS A . n A 1 432 PRO 432 432 432 PRO PRO A . n A 1 433 MET 433 433 433 MET MET A . n A 1 434 HIS 434 434 434 HIS HIS A . n A 1 435 LEU 435 435 435 LEU LEU A . n A 1 436 HIS 436 436 436 HIS HIS A . n A 1 437 GLY 437 437 437 GLY GLY A . n A 1 438 HIS 438 438 438 HIS HIS A . n A 1 439 ASP 439 439 439 ASP ASP A . n A 1 440 PHE 440 440 440 PHE PHE A . n A 1 441 LEU 441 441 441 LEU LEU A . n A 1 442 VAL 442 442 442 VAL VAL A . n A 1 443 LEU 443 443 443 LEU LEU A . n A 1 444 GLY 444 444 444 GLY GLY A . n A 1 445 ARG 445 445 445 ARG ARG A . n A 1 446 SER 446 446 446 SER SER A . n A 1 447 PRO 447 447 447 PRO PRO A . n A 1 448 ASP 448 448 448 ASP ASP A . n A 1 449 VAL 449 449 449 VAL VAL A . n A 1 450 PRO 450 450 450 PRO PRO A . n A 1 451 ALA 451 451 451 ALA ALA A . n A 1 452 ALA 452 452 452 ALA ALA A . n A 1 453 SER 453 453 453 SER SER A . n A 1 454 GLN 454 454 454 GLN GLN A . n A 1 455 GLN 455 455 455 GLN GLN A . n A 1 456 ARG 456 456 456 ARG ARG A . n A 1 457 PHE 457 457 457 PHE PHE A . n A 1 458 VAL 458 458 458 VAL VAL A . n A 1 459 PHE 459 459 459 PHE PHE A . n A 1 460 ASP 460 460 460 ASP ASP A . n A 1 461 PRO 461 461 461 PRO PRO A . n A 1 462 ALA 462 462 462 ALA ALA A . n A 1 463 VAL 463 463 463 VAL VAL A . n A 1 464 ASP 464 464 464 ASP ASP A . n A 1 465 LEU 465 465 465 LEU LEU A . n A 1 466 ALA 466 466 466 ALA ALA A . n A 1 467 ARG 467 467 467 ARG ARG A . n A 1 468 LEU 468 468 468 LEU LEU A . n A 1 469 ASN 469 469 469 ASN ASN A . n A 1 470 GLY 470 470 470 GLY GLY A . n A 1 471 ASP 471 471 471 ASP ASP A . n A 1 472 ASN 472 472 472 ASN ASN A . n A 1 473 PRO 473 473 473 PRO PRO A . n A 1 474 PRO 474 474 474 PRO PRO A . n A 1 475 ARG 475 475 475 ARG ARG A . n A 1 476 ARG 476 476 476 ARG ARG A . n A 1 477 ASP 477 477 477 ASP ASP A . n A 1 478 THR 478 478 478 THR THR A . n A 1 479 THR 479 479 479 THR THR A . n A 1 480 MET 480 480 480 MET MET A . n A 1 481 LEU 481 481 481 LEU LEU A . n A 1 482 PRO 482 482 482 PRO PRO A . n A 1 483 ALA 483 483 483 ALA ALA A . n A 1 484 GLY 484 484 484 GLY GLY A . n A 1 485 GLY 485 485 485 GLY GLY A . n A 1 486 TRP 486 486 486 TRP TRP A . n A 1 487 LEU 487 487 487 LEU LEU A . n A 1 488 LEU 488 488 488 LEU LEU A . n A 1 489 LEU 489 489 489 LEU LEU A . n A 1 490 ALA 490 490 490 ALA ALA A . n A 1 491 PHE 491 491 491 PHE PHE A . n A 1 492 ARG 492 492 492 ARG ARG A . n A 1 493 THR 493 493 493 THR THR A . n A 1 494 ASP 494 494 494 ASP ASP A . n A 1 495 ASN 495 495 495 ASN ASN A . n A 1 496 PRO 496 496 496 PRO PRO A . n A 1 497 GLY 497 497 497 GLY GLY A . n A 1 498 ALA 498 498 498 ALA ALA A . n A 1 499 TRP 499 499 499 TRP TRP A . n A 1 500 LEU 500 500 500 LEU LEU A . n A 1 501 PHE 501 501 501 PHE PHE A . n A 1 502 HIS 502 502 502 HIS HIS A . n A 1 503 CYS 503 503 503 CYS CYS A . n A 1 504 HIS 504 504 504 HIS HIS A . n A 1 505 ILE 505 505 505 ILE ILE A . n A 1 506 ALA 506 506 506 ALA ALA A . n A 1 507 TRP 507 507 507 TRP TRP A . n A 1 508 HIS 508 508 508 HIS HIS A . n A 1 509 VAL 509 509 509 VAL VAL A . n A 1 510 SER 510 510 510 SER SER A . n A 1 511 GLY 511 511 511 GLY GLY A . n A 1 512 GLY 512 512 512 GLY GLY A . n A 1 513 LEU 513 513 513 LEU LEU A . n A 1 514 SER 514 514 514 SER SER A . n A 1 515 VAL 515 515 515 VAL VAL A . n A 1 516 ASP 516 516 516 ASP ASP A . n A 1 517 PHE 517 517 517 PHE PHE A . n A 1 518 LEU 518 518 518 LEU LEU A . n A 1 519 GLU 519 519 519 GLU GLU A . n A 1 520 ARG 520 520 520 ARG ARG A . n A 1 521 PRO 521 521 521 PRO PRO A . n A 1 522 ALA 522 522 522 ALA ALA A . n A 1 523 ASP 523 523 523 ASP ASP A . n A 1 524 LEU 524 524 524 LEU LEU A . n A 1 525 ARG 525 525 525 ARG ARG A . n A 1 526 GLN 526 526 526 GLN GLN A . n A 1 527 ARG 527 527 527 ARG ARG A . n A 1 528 ILE 528 528 528 ILE ILE A . n A 1 529 SER 529 529 529 SER SER A . n A 1 530 GLN 530 530 530 GLN GLN A . n A 1 531 GLU 531 531 531 GLU GLU A . n A 1 532 ASP 532 532 532 ASP ASP A . n A 1 533 GLU 533 533 533 GLU GLU A . n A 1 534 ASP 534 534 534 ASP ASP A . n A 1 535 ASP 535 535 535 ASP ASP A . n A 1 536 PHE 536 536 536 PHE PHE A . n A 1 537 ASN 537 537 537 ASN ASN A . n A 1 538 ARG 538 538 538 ARG ARG A . n A 1 539 VAL 539 539 539 VAL VAL A . n A 1 540 CYS 540 540 540 CYS CYS A . n A 1 541 ASP 541 541 541 ASP ASP A . n A 1 542 GLU 542 542 542 GLU GLU A . n A 1 543 TRP 543 543 543 TRP TRP A . n A 1 544 ARG 544 544 544 ARG ARG A . n A 1 545 ALA 545 545 545 ALA ALA A . n A 1 546 TYR 546 546 546 TYR TYR A . n A 1 547 TRP 547 547 547 TRP TRP A . n A 1 548 PRO 548 548 548 PRO PRO A . n A 1 549 THR 549 549 549 THR THR A . n A 1 550 ASN 550 550 550 ASN ASN A . n A 1 551 PRO 551 551 551 PRO PRO A . n A 1 552 TYR 552 552 552 TYR TYR A . n A 1 553 PRO 553 553 553 PRO PRO A . n A 1 554 LYS 554 554 554 LYS LYS A . n A 1 555 ILE 555 555 555 ILE ILE A . n A 1 556 ASP 556 556 556 ASP ASP A . n A 1 557 SER 557 557 557 SER SER A . n A 1 558 GLY 558 558 558 GLY GLY A . n A 1 559 ALA 559 559 559 ALA ALA A . n B 1 1 GLU 1 1 ? ? ? B . n B 1 2 PRO 2 2 2 PRO PRO B . n B 1 3 THR 3 3 3 THR THR B . n B 1 4 CYS 4 4 4 CYS CYS B . n B 1 5 ASN 5 5 5 ASN ASN B . n B 1 6 THR 6 6 6 THR THR B . n B 1 7 PRO 7 7 7 PRO PRO B . n B 1 8 SER 8 8 8 SER SER B . n B 1 9 ASN 9 9 9 ASN ASN B . n B 1 10 ARG 10 10 10 ARG ARG B . n B 1 11 ALA 11 11 11 ALA ALA B . n B 1 12 CYS 12 12 12 CYS CYS B . n B 1 13 TRP 13 13 13 TRP TRP B . n B 1 14 SER 14 14 14 SER SER B . n B 1 15 ASP 15 15 15 ASP ASP B . n B 1 16 GLY 16 16 16 GLY GLY B . n B 1 17 PHE 17 17 17 PHE PHE B . n B 1 18 ASP 18 18 18 ASP ASP B . n B 1 19 ILE 19 19 19 ILE ILE B . n B 1 20 ASN 20 20 20 ASN ASN B . n B 1 21 THR 21 21 21 THR THR B . n B 1 22 ASP 22 22 22 ASP ASP B . n B 1 23 TYR 23 23 23 TYR TYR B . n B 1 24 GLU 24 24 24 GLU GLU B . n B 1 25 VAL 25 25 25 VAL VAL B . n B 1 26 SER 26 26 26 SER SER B . n B 1 27 THR 27 27 27 THR THR B . n B 1 28 PRO 28 28 28 PRO PRO B . n B 1 29 ASP 29 29 29 ASP ASP B . n B 1 30 THR 30 30 30 THR THR B . n B 1 31 GLY 31 31 31 GLY GLY B . n B 1 32 VAL 32 32 32 VAL VAL B . n B 1 33 THR 33 33 33 THR THR B . n B 1 34 GLN 34 34 34 GLN GLN B . n B 1 35 SER 35 35 35 SER SER B . n B 1 36 TYR 36 36 36 TYR TYR B . n B 1 37 VAL 37 37 37 VAL VAL B . n B 1 38 PHE 38 38 38 PHE PHE B . n B 1 39 ASN 39 39 39 ASN ASN B . n B 1 40 LEU 40 40 40 LEU LEU B . n B 1 41 THR 41 41 41 THR THR B . n B 1 42 GLU 42 42 42 GLU GLU B . n B 1 43 VAL 43 43 43 VAL VAL B . n B 1 44 ASP 44 44 44 ASP ASP B . n B 1 45 ASN 45 45 45 ASN ASN B . n B 1 46 TRP 46 46 46 TRP TRP B . n B 1 47 MET 47 47 47 MET MET B . n B 1 48 GLY 48 48 48 GLY GLY B . n B 1 49 PRO 49 49 49 PRO PRO B . n B 1 50 ASP 50 50 50 ASP ASP B . n B 1 51 GLY 51 51 51 GLY GLY B . n B 1 52 VAL 52 52 52 VAL VAL B . n B 1 53 VAL 53 53 53 VAL VAL B . n B 1 54 LYS 54 54 54 LYS LYS B . n B 1 55 GLU 55 55 55 GLU GLU B . n B 1 56 LYS 56 56 56 LYS LYS B . n B 1 57 VAL 57 57 57 VAL VAL B . n B 1 58 MET 58 58 58 MET MET B . n B 1 59 LEU 59 59 59 LEU LEU B . n B 1 60 ILE 60 60 60 ILE ILE B . n B 1 61 ASN 61 61 61 ASN ASN B . n B 1 62 GLY 62 62 62 GLY GLY B . n B 1 63 ASN 63 63 63 ASN ASN B . n B 1 64 ILE 64 64 64 ILE ILE B . n B 1 65 MET 65 65 65 MET MET B . n B 1 66 GLY 66 66 66 GLY GLY B . n B 1 67 PRO 67 67 67 PRO PRO B . n B 1 68 ASN 68 68 68 ASN ASN B . n B 1 69 ILE 69 69 69 ILE ILE B . n B 1 70 VAL 70 70 70 VAL VAL B . n B 1 71 ALA 71 71 71 ALA ALA B . n B 1 72 ASN 72 72 72 ASN ASN B . n B 1 73 TRP 73 73 73 TRP TRP B . n B 1 74 GLY 74 74 74 GLY GLY B . n B 1 75 ASP 75 75 75 ASP ASP B . n B 1 76 THR 76 76 76 THR THR B . n B 1 77 VAL 77 77 77 VAL VAL B . n B 1 78 GLU 78 78 78 GLU GLU B . n B 1 79 VAL 79 79 79 VAL VAL B . n B 1 80 THR 80 80 80 THR THR B . n B 1 81 VAL 81 81 81 VAL VAL B . n B 1 82 ILE 82 82 82 ILE ILE B . n B 1 83 ASN 83 83 83 ASN ASN B . n B 1 84 ASN 84 84 84 ASN ASN B . n B 1 85 LEU 85 85 85 LEU LEU B . n B 1 86 VAL 86 86 86 VAL VAL B . n B 1 87 THR 87 87 87 THR THR B . n B 1 88 ASN 88 88 88 ASN ASN B . n B 1 89 GLY 89 89 89 GLY GLY B . n B 1 90 THR 90 90 90 THR THR B . n B 1 91 SER 91 91 91 SER SER B . n B 1 92 ILE 92 92 92 ILE ILE B . n B 1 93 HIS 93 93 93 HIS HIS B . n B 1 94 TRP 94 94 94 TRP TRP B . n B 1 95 HIS 95 95 95 HIS HIS B . n B 1 96 GLY 96 96 96 GLY GLY B . n B 1 97 ILE 97 97 97 ILE ILE B . n B 1 98 HIS 98 98 98 HIS HIS B . n B 1 99 GLN 99 99 99 GLN GLN B . n B 1 100 LYS 100 100 100 LYS LYS B . n B 1 101 ASP 101 101 101 ASP ASP B . n B 1 102 THR 102 102 102 THR THR B . n B 1 103 ASN 103 103 103 ASN ASN B . n B 1 104 LEU 104 104 104 LEU LEU B . n B 1 105 HIS 105 105 105 HIS HIS B . n B 1 106 ASP 106 106 106 ASP ASP B . n B 1 107 GLY 107 107 107 GLY GLY B . n B 1 108 ALA 108 108 108 ALA ALA B . n B 1 109 ASN 109 109 109 ASN ASN B . n B 1 110 GLY 110 110 110 GLY GLY B . n B 1 111 VAL 111 111 111 VAL VAL B . n B 1 112 THR 112 112 112 THR THR B . n B 1 113 GLU 113 113 113 GLU GLU B . n B 1 114 CYS 114 114 114 CYS CYS B . n B 1 115 PRO 115 115 115 PRO PRO B . n B 1 116 ILE 116 116 116 ILE ILE B . n B 1 117 PRO 117 117 117 PRO PRO B . n B 1 118 PRO 118 118 118 PRO PRO B . n B 1 119 LYS 119 119 119 LYS LYS B . n B 1 120 GLY 120 120 120 GLY GLY B . n B 1 121 GLY 121 121 121 GLY GLY B . n B 1 122 GLN 122 122 122 GLN GLN B . n B 1 123 ARG 123 123 123 ARG ARG B . n B 1 124 THR 124 124 124 THR THR B . n B 1 125 TYR 125 125 125 TYR TYR B . n B 1 126 ARG 126 126 126 ARG ARG B . n B 1 127 TRP 127 127 127 TRP TRP B . n B 1 128 ARG 128 128 128 ARG ARG B . n B 1 129 ALA 129 129 129 ALA ALA B . n B 1 130 ARG 130 130 130 ARG ARG B . n B 1 131 GLN 131 131 131 GLN GLN B . n B 1 132 TYR 132 132 132 TYR TYR B . n B 1 133 GLY 133 133 133 GLY GLY B . n B 1 134 THR 134 134 134 THR THR B . n B 1 135 SER 135 135 135 SER SER B . n B 1 136 TRP 136 136 136 TRP TRP B . n B 1 137 TYR 137 137 137 TYR TYR B . n B 1 138 HIS 138 138 138 HIS HIS B . n B 1 139 SER 139 139 139 SER SER B . n B 1 140 HIS 140 140 140 HIS HIS B . n B 1 141 PHE 141 141 141 PHE PHE B . n B 1 142 SER 142 142 142 SER SER B . n B 1 143 ALA 143 143 143 ALA ALA B . n B 1 144 GLN 144 144 144 GLN GLN B . n B 1 145 TYR 145 145 145 TYR TYR B . n B 1 146 GLY 146 146 146 GLY GLY B . n B 1 147 ASN 147 147 147 ASN ASN B . n B 1 148 GLY 148 148 148 GLY GLY B . n B 1 149 VAL 149 149 149 VAL VAL B . n B 1 150 VAL 150 150 150 VAL VAL B . n B 1 151 GLY 151 151 151 GLY GLY B . n B 1 152 THR 152 152 152 THR THR B . n B 1 153 ILE 153 153 153 ILE ILE B . n B 1 154 GLN 154 154 154 GLN GLN B . n B 1 155 ILE 155 155 155 ILE ILE B . n B 1 156 ASN 156 156 156 ASN ASN B . n B 1 157 GLY 157 157 157 GLY GLY B . n B 1 158 PRO 158 158 158 PRO PRO B . n B 1 159 ALA 159 159 159 ALA ALA B . n B 1 160 SER 160 160 160 SER SER B . n B 1 161 LEU 161 161 161 LEU LEU B . n B 1 162 PRO 162 162 162 PRO PRO B . n B 1 163 TYR 163 163 163 TYR TYR B . n B 1 164 ASP 164 164 164 ASP ASP B . n B 1 165 ILE 165 165 165 ILE ILE B . n B 1 166 ASP 166 166 166 ASP ASP B . n B 1 167 LEU 167 167 167 LEU LEU B . n B 1 168 GLY 168 168 168 GLY GLY B . n B 1 169 VAL 169 169 169 VAL VAL B . n B 1 170 PHE 170 170 170 PHE PHE B . n B 1 171 PRO 171 171 171 PRO PRO B . n B 1 172 ILE 172 172 172 ILE ILE B . n B 1 173 THR 173 173 173 THR THR B . n B 1 174 ASP 174 174 174 ASP ASP B . n B 1 175 TYR 175 175 175 TYR TYR B . n B 1 176 TYR 176 176 176 TYR TYR B . n B 1 177 TYR 177 177 177 TYR TYR B . n B 1 178 ARG 178 178 178 ARG ARG B . n B 1 179 ALA 179 179 179 ALA ALA B . n B 1 180 ALA 180 180 180 ALA ALA B . n B 1 181 ASP 181 181 181 ASP ASP B . n B 1 182 ASP 182 182 182 ASP ASP B . n B 1 183 LEU 183 183 183 LEU LEU B . n B 1 184 VAL 184 184 184 VAL VAL B . n B 1 185 HIS 185 185 185 HIS HIS B . n B 1 186 PHE 186 186 186 PHE PHE B . n B 1 187 THR 187 187 187 THR THR B . n B 1 188 GLN 188 188 188 GLN GLN B . n B 1 189 ASN 189 189 189 ASN ASN B . n B 1 190 ASN 190 190 190 ASN ASN B . n B 1 191 ALA 191 191 191 ALA ALA B . n B 1 192 PRO 192 192 192 PRO PRO B . n B 1 193 PRO 193 193 193 PRO PRO B . n B 1 194 PHE 194 194 194 PHE PHE B . n B 1 195 SER 195 195 195 SER SER B . n B 1 196 ASP 196 196 196 ASP ASP B . n B 1 197 ASN 197 197 197 ASN ASN B . n B 1 198 VAL 198 198 198 VAL VAL B . n B 1 199 LEU 199 199 199 LEU LEU B . n B 1 200 ILE 200 200 200 ILE ILE B . n B 1 201 ASN 201 201 201 ASN ASN B . n B 1 202 GLY 202 202 202 GLY GLY B . n B 1 203 THR 203 203 203 THR THR B . n B 1 204 ALA 204 204 204 ALA ALA B . n B 1 205 VAL 205 205 205 VAL VAL B . n B 1 206 ASN 206 206 206 ASN ASN B . n B 1 207 PRO 207 207 207 PRO PRO B . n B 1 208 ASN 208 208 208 ASN ASN B . n B 1 209 THR 209 209 209 THR THR B . n B 1 210 GLY 210 210 210 GLY GLY B . n B 1 211 GLU 211 211 211 GLU GLU B . n B 1 212 GLY 212 212 212 GLY GLY B . n B 1 213 GLN 213 213 213 GLN GLN B . n B 1 214 TYR 214 214 214 TYR TYR B . n B 1 215 ALA 215 215 215 ALA ALA B . n B 1 216 ASN 216 216 216 ASN ASN B . n B 1 217 VAL 217 217 217 VAL VAL B . n B 1 218 THR 218 218 218 THR THR B . n B 1 219 LEU 219 219 219 LEU LEU B . n B 1 220 THR 220 220 220 THR THR B . n B 1 221 PRO 221 221 221 PRO PRO B . n B 1 222 GLY 222 222 222 GLY GLY B . n B 1 223 LYS 223 223 223 LYS LYS B . n B 1 224 ARG 224 224 224 ARG ARG B . n B 1 225 HIS 225 225 225 HIS HIS B . n B 1 226 ARG 226 226 226 ARG ARG B . n B 1 227 LEU 227 227 227 LEU LEU B . n B 1 228 ARG 228 228 228 ARG ARG B . n B 1 229 ILE 229 229 229 ILE ILE B . n B 1 230 LEU 230 230 230 LEU LEU B . n B 1 231 ASN 231 231 231 ASN ASN B . n B 1 232 THR 232 232 232 THR THR B . n B 1 233 SER 233 233 233 SER SER B . n B 1 234 THR 234 234 234 THR THR B . n B 1 235 GLU 235 235 235 GLU GLU B . n B 1 236 ASN 236 236 236 ASN ASN B . n B 1 237 HIS 237 237 237 HIS HIS B . n B 1 238 PHE 238 238 238 PHE PHE B . n B 1 239 GLN 239 239 239 GLN GLN B . n B 1 240 VAL 240 240 240 VAL VAL B . n B 1 241 SER 241 241 241 SER SER B . n B 1 242 LEU 242 242 242 LEU LEU B . n B 1 243 VAL 243 243 243 VAL VAL B . n B 1 244 ASN 244 244 244 ASN ASN B . n B 1 245 HIS 245 245 245 HIS HIS B . n B 1 246 THR 246 246 246 THR THR B . n B 1 247 MET 247 247 247 MET MET B . n B 1 248 THR 248 248 248 THR THR B . n B 1 249 VAL 249 249 249 VAL VAL B . n B 1 250 ILE 250 250 250 ILE ILE B . n B 1 251 ALA 251 251 251 ALA ALA B . n B 1 252 ALA 252 252 252 ALA ALA B . n B 1 253 ASP 253 253 253 ASP ASP B . n B 1 254 MET 254 254 254 MET MET B . n B 1 255 VAL 255 255 255 VAL VAL B . n B 1 256 PRO 256 256 256 PRO PRO B . n B 1 257 VAL 257 257 257 VAL VAL B . n B 1 258 ASN 258 258 258 ASN ASN B . n B 1 259 ALA 259 259 259 ALA ALA B . n B 1 260 MET 260 260 260 MET MET B . n B 1 261 THR 261 261 261 THR THR B . n B 1 262 VAL 262 262 262 VAL VAL B . n B 1 263 ASP 263 263 263 ASP ASP B . n B 1 264 SER 264 264 264 SER SER B . n B 1 265 LEU 265 265 265 LEU LEU B . n B 1 266 PHE 266 266 266 PHE PHE B . n B 1 267 LEU 267 267 267 LEU LEU B . n B 1 268 ALA 268 268 268 ALA ALA B . n B 1 269 VAL 269 269 269 VAL VAL B . n B 1 270 GLY 270 270 270 GLY GLY B . n B 1 271 GLN 271 271 271 GLN GLN B . n B 1 272 ARG 272 272 272 ARG ARG B . n B 1 273 TYR 273 273 273 TYR TYR B . n B 1 274 ASP 274 274 274 ASP ASP B . n B 1 275 VAL 275 275 275 VAL VAL B . n B 1 276 VAL 276 276 276 VAL VAL B . n B 1 277 ILE 277 277 277 ILE ILE B . n B 1 278 ASP 278 278 278 ASP ASP B . n B 1 279 ALA 279 279 279 ALA ALA B . n B 1 280 SER 280 280 280 SER SER B . n B 1 281 ARG 281 281 281 ARG ARG B . n B 1 282 ALA 282 282 282 ALA ALA B . n B 1 283 PRO 283 283 283 PRO PRO B . n B 1 284 ASP 284 284 284 ASP ASP B . n B 1 285 ASN 285 285 285 ASN ASN B . n B 1 286 TYR 286 286 286 TYR TYR B . n B 1 287 TRP 287 287 287 TRP TRP B . n B 1 288 PHE 288 288 288 PHE PHE B . n B 1 289 ASN 289 289 289 ASN ASN B . n B 1 290 VAL 290 290 290 VAL VAL B . n B 1 291 THR 291 291 291 THR THR B . n B 1 292 PHE 292 292 292 PHE PHE B . n B 1 293 GLY 293 293 293 GLY GLY B . n B 1 294 GLY 294 294 294 GLY GLY B . n B 1 295 GLN 295 295 295 GLN GLN B . n B 1 296 ALA 296 296 296 ALA ALA B . n B 1 297 ALA 297 297 297 ALA ALA B . n B 1 298 CYS 298 298 298 CYS CYS B . n B 1 299 GLY 299 299 299 GLY GLY B . n B 1 300 GLY 300 300 300 GLY GLY B . n B 1 301 SER 301 301 301 SER SER B . n B 1 302 LEU 302 302 302 LEU LEU B . n B 1 303 ASN 303 303 303 ASN ASN B . n B 1 304 PRO 304 304 304 PRO PRO B . n B 1 305 HIS 305 305 305 HIS HIS B . n B 1 306 PRO 306 306 306 PRO PRO B . n B 1 307 ALA 307 307 307 ALA ALA B . n B 1 308 ALA 308 308 308 ALA ALA B . n B 1 309 ILE 309 309 309 ILE ILE B . n B 1 310 PHE 310 310 310 PHE PHE B . n B 1 311 HIS 311 311 311 HIS HIS B . n B 1 312 TYR 312 312 312 TYR TYR B . n B 1 313 ALA 313 313 313 ALA ALA B . n B 1 314 GLY 314 314 314 GLY GLY B . n B 1 315 ALA 315 315 315 ALA ALA B . n B 1 316 PRO 316 316 316 PRO PRO B . n B 1 317 GLY 317 317 317 GLY GLY B . n B 1 318 GLY 318 318 318 GLY GLY B . n B 1 319 LEU 319 319 319 LEU LEU B . n B 1 320 PRO 320 320 320 PRO PRO B . n B 1 321 THR 321 321 321 THR THR B . n B 1 322 ASP 322 322 322 ASP ASP B . n B 1 323 GLU 323 323 323 GLU GLU B . n B 1 324 GLY 324 324 324 GLY GLY B . n B 1 325 THR 325 325 325 THR THR B . n B 1 326 PRO 326 326 326 PRO PRO B . n B 1 327 PRO 327 327 327 PRO PRO B . n B 1 328 VAL 328 328 328 VAL VAL B . n B 1 329 ASP 329 329 329 ASP ASP B . n B 1 330 HIS 330 330 330 HIS HIS B . n B 1 331 GLN 331 331 331 GLN GLN B . n B 1 332 CYS 332 332 332 CYS CYS B . n B 1 333 LEU 333 333 333 LEU LEU B . n B 1 334 ASP 334 334 334 ASP ASP B . n B 1 335 THR 335 335 335 THR THR B . n B 1 336 LEU 336 336 336 LEU LEU B . n B 1 337 ASP 337 337 337 ASP ASP B . n B 1 338 VAL 338 338 338 VAL VAL B . n B 1 339 ARG 339 339 339 ARG ARG B . n B 1 340 PRO 340 340 340 PRO PRO B . n B 1 341 VAL 341 341 341 VAL VAL B . n B 1 342 VAL 342 342 342 VAL VAL B . n B 1 343 PRO 343 343 343 PRO PRO B . n B 1 344 ARG 344 344 344 ARG ARG B . n B 1 345 SER 345 345 345 SER SER B . n B 1 346 VAL 346 346 346 VAL VAL B . n B 1 347 PRO 347 347 347 PRO PRO B . n B 1 348 VAL 348 348 348 VAL VAL B . n B 1 349 ASN 349 349 349 ASN ASN B . n B 1 350 SER 350 350 350 SER SER B . n B 1 351 PHE 351 351 351 PHE PHE B . n B 1 352 VAL 352 352 352 VAL VAL B . n B 1 353 LYS 353 353 353 LYS LYS B . n B 1 354 ARG 354 354 354 ARG ARG B . n B 1 355 PRO 355 355 355 PRO PRO B . n B 1 356 ASP 356 356 356 ASP ASP B . n B 1 357 ASN 357 357 357 ASN ASN B . n B 1 358 THR 358 358 358 THR THR B . n B 1 359 LEU 359 359 359 LEU LEU B . n B 1 360 PRO 360 360 360 PRO PRO B . n B 1 361 VAL 361 361 361 VAL VAL B . n B 1 362 ALA 362 362 362 ALA ALA B . n B 1 363 LEU 363 363 363 LEU LEU B . n B 1 364 ASP 364 364 364 ASP ASP B . n B 1 365 LEU 365 365 365 LEU LEU B . n B 1 366 THR 366 366 366 THR THR B . n B 1 367 GLY 367 367 367 GLY GLY B . n B 1 368 THR 368 368 368 THR THR B . n B 1 369 PRO 369 369 369 PRO PRO B . n B 1 370 LEU 370 370 370 LEU LEU B . n B 1 371 PHE 371 371 371 PHE PHE B . n B 1 372 VAL 372 372 372 VAL VAL B . n B 1 373 TRP 373 373 373 TRP TRP B . n B 1 374 LYS 374 374 374 LYS LYS B . n B 1 375 VAL 375 375 375 VAL VAL B . n B 1 376 ASN 376 376 376 ASN ASN B . n B 1 377 GLY 377 377 377 GLY GLY B . n B 1 378 SER 378 378 378 SER SER B . n B 1 379 ASP 379 379 379 ASP ASP B . n B 1 380 ILE 380 380 380 ILE ILE B . n B 1 381 ASN 381 381 381 ASN ASN B . n B 1 382 VAL 382 382 382 VAL VAL B . n B 1 383 ASP 383 383 383 ASP ASP B . n B 1 384 TRP 384 384 384 TRP TRP B . n B 1 385 GLY 385 385 385 GLY GLY B . n B 1 386 LYS 386 386 386 LYS LYS B . n B 1 387 PRO 387 387 387 PRO PRO B . n B 1 388 ILE 388 388 388 ILE ILE B . n B 1 389 ILE 389 389 389 ILE ILE B . n B 1 390 ASP 390 390 390 ASP ASP B . n B 1 391 TYR 391 391 391 TYR TYR B . n B 1 392 ILE 392 392 392 ILE ILE B . n B 1 393 LEU 393 393 393 LEU LEU B . n B 1 394 THR 394 394 394 THR THR B . n B 1 395 GLY 395 395 395 GLY GLY B . n B 1 396 ASN 396 396 396 ASN ASN B . n B 1 397 THR 397 397 397 THR THR B . n B 1 398 SER 398 398 398 SER SER B . n B 1 399 TYR 399 399 399 TYR TYR B . n B 1 400 PRO 400 400 400 PRO PRO B . n B 1 401 VAL 401 401 401 VAL VAL B . n B 1 402 SER 402 402 402 SER SER B . n B 1 403 ASP 403 403 403 ASP ASP B . n B 1 404 ASN 404 404 404 ASN ASN B . n B 1 405 ILE 405 405 405 ILE ILE B . n B 1 406 VAL 406 406 406 VAL VAL B . n B 1 407 GLN 407 407 407 GLN GLN B . n B 1 408 VAL 408 408 408 VAL VAL B . n B 1 409 ASP 409 409 409 ASP ASP B . n B 1 410 ALA 410 410 410 ALA ALA B . n B 1 411 VAL 411 411 411 VAL VAL B . n B 1 412 ASP 412 412 412 ASP ASP B . n B 1 413 GLN 413 413 413 GLN GLN B . n B 1 414 TRP 414 414 414 TRP TRP B . n B 1 415 THR 415 415 415 THR THR B . n B 1 416 TYR 416 416 416 TYR TYR B . n B 1 417 TRP 417 417 417 TRP TRP B . n B 1 418 LEU 418 418 418 LEU LEU B . n B 1 419 ILE 419 419 419 ILE ILE B . n B 1 420 GLU 420 420 420 GLU GLU B . n B 1 421 ASN 421 421 421 ASN ASN B . n B 1 422 ASP 422 422 422 ASP ASP B . n B 1 423 PRO 423 423 423 PRO PRO B . n B 1 424 GLU 424 424 424 GLU GLU B . n B 1 425 GLY 425 425 425 GLY GLY B . n B 1 426 PRO 426 426 426 PRO PRO B . n B 1 427 PHE 427 427 427 PHE PHE B . n B 1 428 SER 428 428 428 SER SER B . n B 1 429 LEU 429 429 429 LEU LEU B . n B 1 430 PRO 430 430 430 PRO PRO B . n B 1 431 HIS 431 431 431 HIS HIS B . n B 1 432 PRO 432 432 432 PRO PRO B . n B 1 433 MET 433 433 433 MET MET B . n B 1 434 HIS 434 434 434 HIS HIS B . n B 1 435 LEU 435 435 435 LEU LEU B . n B 1 436 HIS 436 436 436 HIS HIS B . n B 1 437 GLY 437 437 437 GLY GLY B . n B 1 438 HIS 438 438 438 HIS HIS B . n B 1 439 ASP 439 439 439 ASP ASP B . n B 1 440 PHE 440 440 440 PHE PHE B . n B 1 441 LEU 441 441 441 LEU LEU B . n B 1 442 VAL 442 442 442 VAL VAL B . n B 1 443 LEU 443 443 443 LEU LEU B . n B 1 444 GLY 444 444 444 GLY GLY B . n B 1 445 ARG 445 445 445 ARG ARG B . n B 1 446 SER 446 446 446 SER SER B . n B 1 447 PRO 447 447 447 PRO PRO B . n B 1 448 ASP 448 448 448 ASP ASP B . n B 1 449 VAL 449 449 449 VAL VAL B . n B 1 450 PRO 450 450 450 PRO PRO B . n B 1 451 ALA 451 451 451 ALA ALA B . n B 1 452 ALA 452 452 452 ALA ALA B . n B 1 453 SER 453 453 453 SER SER B . n B 1 454 GLN 454 454 454 GLN GLN B . n B 1 455 GLN 455 455 455 GLN GLN B . n B 1 456 ARG 456 456 456 ARG ARG B . n B 1 457 PHE 457 457 457 PHE PHE B . n B 1 458 VAL 458 458 458 VAL VAL B . n B 1 459 PHE 459 459 459 PHE PHE B . n B 1 460 ASP 460 460 460 ASP ASP B . n B 1 461 PRO 461 461 461 PRO PRO B . n B 1 462 ALA 462 462 462 ALA ALA B . n B 1 463 VAL 463 463 463 VAL VAL B . n B 1 464 ASP 464 464 464 ASP ASP B . n B 1 465 LEU 465 465 465 LEU LEU B . n B 1 466 ALA 466 466 466 ALA ALA B . n B 1 467 ARG 467 467 467 ARG ARG B . n B 1 468 LEU 468 468 468 LEU LEU B . n B 1 469 ASN 469 469 469 ASN ASN B . n B 1 470 GLY 470 470 470 GLY GLY B . n B 1 471 ASP 471 471 471 ASP ASP B . n B 1 472 ASN 472 472 472 ASN ASN B . n B 1 473 PRO 473 473 473 PRO PRO B . n B 1 474 PRO 474 474 474 PRO PRO B . n B 1 475 ARG 475 475 475 ARG ARG B . n B 1 476 ARG 476 476 476 ARG ARG B . n B 1 477 ASP 477 477 477 ASP ASP B . n B 1 478 THR 478 478 478 THR THR B . n B 1 479 THR 479 479 479 THR THR B . n B 1 480 MET 480 480 480 MET MET B . n B 1 481 LEU 481 481 481 LEU LEU B . n B 1 482 PRO 482 482 482 PRO PRO B . n B 1 483 ALA 483 483 483 ALA ALA B . n B 1 484 GLY 484 484 484 GLY GLY B . n B 1 485 GLY 485 485 485 GLY GLY B . n B 1 486 TRP 486 486 486 TRP TRP B . n B 1 487 LEU 487 487 487 LEU LEU B . n B 1 488 LEU 488 488 488 LEU LEU B . n B 1 489 LEU 489 489 489 LEU LEU B . n B 1 490 ALA 490 490 490 ALA ALA B . n B 1 491 PHE 491 491 491 PHE PHE B . n B 1 492 ARG 492 492 492 ARG ARG B . n B 1 493 THR 493 493 493 THR THR B . n B 1 494 ASP 494 494 494 ASP ASP B . n B 1 495 ASN 495 495 495 ASN ASN B . n B 1 496 PRO 496 496 496 PRO PRO B . n B 1 497 GLY 497 497 497 GLY GLY B . n B 1 498 ALA 498 498 498 ALA ALA B . n B 1 499 TRP 499 499 499 TRP TRP B . n B 1 500 LEU 500 500 500 LEU LEU B . n B 1 501 PHE 501 501 501 PHE PHE B . n B 1 502 HIS 502 502 502 HIS HIS B . n B 1 503 CYS 503 503 503 CYS CYS B . n B 1 504 HIS 504 504 504 HIS HIS B . n B 1 505 ILE 505 505 505 ILE ILE B . n B 1 506 ALA 506 506 506 ALA ALA B . n B 1 507 TRP 507 507 507 TRP TRP B . n B 1 508 HIS 508 508 508 HIS HIS B . n B 1 509 VAL 509 509 509 VAL VAL B . n B 1 510 SER 510 510 510 SER SER B . n B 1 511 GLY 511 511 511 GLY GLY B . n B 1 512 GLY 512 512 512 GLY GLY B . n B 1 513 LEU 513 513 513 LEU LEU B . n B 1 514 SER 514 514 514 SER SER B . n B 1 515 VAL 515 515 515 VAL VAL B . n B 1 516 ASP 516 516 516 ASP ASP B . n B 1 517 PHE 517 517 517 PHE PHE B . n B 1 518 LEU 518 518 518 LEU LEU B . n B 1 519 GLU 519 519 519 GLU GLU B . n B 1 520 ARG 520 520 520 ARG ARG B . n B 1 521 PRO 521 521 521 PRO PRO B . n B 1 522 ALA 522 522 522 ALA ALA B . n B 1 523 ASP 523 523 523 ASP ASP B . n B 1 524 LEU 524 524 524 LEU LEU B . n B 1 525 ARG 525 525 525 ARG ARG B . n B 1 526 GLN 526 526 526 GLN GLN B . n B 1 527 ARG 527 527 527 ARG ARG B . n B 1 528 ILE 528 528 528 ILE ILE B . n B 1 529 SER 529 529 529 SER SER B . n B 1 530 GLN 530 530 530 GLN GLN B . n B 1 531 GLU 531 531 531 GLU GLU B . n B 1 532 ASP 532 532 532 ASP ASP B . n B 1 533 GLU 533 533 533 GLU GLU B . n B 1 534 ASP 534 534 534 ASP ASP B . n B 1 535 ASP 535 535 535 ASP ASP B . n B 1 536 PHE 536 536 536 PHE PHE B . n B 1 537 ASN 537 537 537 ASN ASN B . n B 1 538 ARG 538 538 538 ARG ARG B . n B 1 539 VAL 539 539 539 VAL VAL B . n B 1 540 CYS 540 540 540 CYS CYS B . n B 1 541 ASP 541 541 541 ASP ASP B . n B 1 542 GLU 542 542 542 GLU GLU B . n B 1 543 TRP 543 543 543 TRP TRP B . n B 1 544 ARG 544 544 544 ARG ARG B . n B 1 545 ALA 545 545 545 ALA ALA B . n B 1 546 TYR 546 546 546 TYR TYR B . n B 1 547 TRP 547 547 547 TRP TRP B . n B 1 548 PRO 548 548 548 PRO PRO B . n B 1 549 THR 549 549 549 THR THR B . n B 1 550 ASN 550 550 550 ASN ASN B . n B 1 551 PRO 551 551 551 PRO PRO B . n B 1 552 TYR 552 552 552 TYR TYR B . n B 1 553 PRO 553 553 553 PRO PRO B . n B 1 554 LYS 554 554 554 LYS LYS B . n B 1 555 ILE 555 555 555 ILE ILE B . n B 1 556 ASP 556 556 556 ASP ASP B . n B 1 557 SER 557 557 557 SER SER B . n B 1 558 GLY 558 558 558 GLY GLY B . n B 1 559 ALA 559 559 559 ALA ALA B . 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 C 2 NAG 1 700 700 NAG NAG A . D 2 NAG 1 710 710 NAG NAG A . E 2 NAG 2 711 711 NAG NAG A . F 3 BMA 3 712 712 BMA BMA A . G 4 MAN 4 714 714 MAN MAN A . H 2 NAG 1 720 720 NAG NAG A . I 2 NAG 2 721 721 NAG NAG A . J 2 NAG 1 730 730 NAG NAG A . K 2 NAG 2 731 731 NAG NAG A . L 3 BMA 3 732 732 BMA BMA A . M 2 NAG 1 740 740 NAG NAG A . N 2 NAG 2 741 741 NAG NAG A . O 2 NAG 1 750 750 NAG NAG A . P 2 NAG 1 760 760 NAG NAG A . Q 2 NAG 2 761 761 NAG NAG A . R 5 CU 1 601 601 CU CU A . S 5 CU 1 602 602 CU CU A . T 5 CU 1 603 603 CU CU A . U 5 CU 1 604 604 CU CU A . V 6 CL 1 610 610 CL CL A . W 7 SO4 1 800 800 SO4 SO4 A . X 7 SO4 1 802 802 SO4 SO4 A . Y 8 OXY 1 900 900 OXY O2 A . Z 2 NAG 1 700 700 NAG NAG B . AA 2 NAG 1 710 710 NAG NAG B . BA 2 NAG 2 711 711 NAG NAG B . CA 3 BMA 3 712 712 BMA BMA B . DA 2 NAG 1 720 720 NAG NAG B . EA 2 NAG 2 721 721 NAG NAG B . FA 3 BMA 3 722 722 BMA BMA B . GA 2 NAG 1 730 730 NAG NAG B . HA 2 NAG 2 731 731 NAG NAG B . IA 3 BMA 3 732 732 BMA BMA B . JA 2 NAG 1 740 740 NAG NAG B . KA 2 NAG 2 741 741 NAG NAG B . LA 2 NAG 1 750 750 NAG NAG B . MA 2 NAG 1 760 760 NAG NAG B . NA 2 NAG 1 770 770 NAG NAG B . OA 5 CU 1 601 601 CU CU B . PA 5 CU 1 602 602 CU CU B . QA 5 CU 1 603 603 CU CU B . RA 5 CU 1 604 604 CU CU B . SA 7 SO4 1 801 801 SO4 SO4 B . TA 8 OXY 1 901 901 OXY O2 B . UA 9 GOL 1 810 810 GOL GOL B . VA 10 HOH 1 901 5 HOH HOH A . VA 10 HOH 2 902 6 HOH HOH A . VA 10 HOH 3 903 7 HOH HOH A . VA 10 HOH 4 904 15 HOH HOH A . VA 10 HOH 5 905 16 HOH HOH A . VA 10 HOH 6 906 20 HOH HOH A . VA 10 HOH 7 907 23 HOH HOH A . VA 10 HOH 8 908 24 HOH HOH A . VA 10 HOH 9 909 25 HOH HOH A . VA 10 HOH 10 910 26 HOH HOH A . VA 10 HOH 11 911 30 HOH HOH A . VA 10 HOH 12 912 31 HOH HOH A . VA 10 HOH 13 913 32 HOH HOH A . VA 10 HOH 14 914 33 HOH HOH A . VA 10 HOH 15 915 34 HOH HOH A . VA 10 HOH 16 916 35 HOH HOH A . VA 10 HOH 17 917 36 HOH HOH A . VA 10 HOH 18 918 39 HOH HOH A . VA 10 HOH 19 919 45 HOH HOH A . VA 10 HOH 20 920 46 HOH HOH A . VA 10 HOH 21 921 47 HOH HOH A . VA 10 HOH 22 922 48 HOH HOH A . VA 10 HOH 23 923 49 HOH HOH A . VA 10 HOH 24 924 50 HOH HOH A . VA 10 HOH 25 925 53 HOH HOH A . VA 10 HOH 26 926 54 HOH HOH A . VA 10 HOH 27 927 55 HOH HOH A . VA 10 HOH 28 928 57 HOH HOH A . VA 10 HOH 29 929 58 HOH HOH A . VA 10 HOH 30 930 67 HOH HOH A . VA 10 HOH 31 931 69 HOH HOH A . VA 10 HOH 32 932 71 HOH HOH A . VA 10 HOH 33 933 72 HOH HOH A . VA 10 HOH 34 934 73 HOH HOH A . VA 10 HOH 35 935 75 HOH HOH A . VA 10 HOH 36 936 77 HOH HOH A . VA 10 HOH 37 937 78 HOH HOH A . VA 10 HOH 38 938 79 HOH HOH A . VA 10 HOH 39 939 81 HOH HOH A . VA 10 HOH 40 940 83 HOH HOH A . VA 10 HOH 41 941 84 HOH HOH A . VA 10 HOH 42 942 86 HOH HOH A . VA 10 HOH 43 943 89 HOH HOH A . VA 10 HOH 44 944 90 HOH HOH A . VA 10 HOH 45 945 91 HOH HOH A . VA 10 HOH 46 946 93 HOH HOH A . VA 10 HOH 47 947 94 HOH HOH A . VA 10 HOH 48 948 96 HOH HOH A . VA 10 HOH 49 949 98 HOH HOH A . VA 10 HOH 50 950 99 HOH HOH A . VA 10 HOH 51 951 100 HOH HOH A . VA 10 HOH 52 952 101 HOH HOH A . VA 10 HOH 53 953 102 HOH HOH A . VA 10 HOH 54 954 103 HOH HOH A . VA 10 HOH 55 955 104 HOH HOH A . VA 10 HOH 56 956 106 HOH HOH A . VA 10 HOH 57 957 109 HOH HOH A . VA 10 HOH 58 958 110 HOH HOH A . VA 10 HOH 59 959 111 HOH HOH A . VA 10 HOH 60 960 113 HOH HOH A . VA 10 HOH 61 961 119 HOH HOH A . VA 10 HOH 62 962 120 HOH HOH A . VA 10 HOH 63 963 125 HOH HOH A . VA 10 HOH 64 964 126 HOH HOH A . VA 10 HOH 65 965 127 HOH HOH A . VA 10 HOH 66 966 128 HOH HOH A . VA 10 HOH 67 967 129 HOH HOH A . VA 10 HOH 68 968 130 HOH HOH A . VA 10 HOH 69 969 132 HOH HOH A . VA 10 HOH 70 970 133 HOH HOH A . VA 10 HOH 71 971 137 HOH HOH A . VA 10 HOH 72 972 138 HOH HOH A . VA 10 HOH 73 973 139 HOH HOH A . VA 10 HOH 74 974 140 HOH HOH A . VA 10 HOH 75 975 141 HOH HOH A . VA 10 HOH 76 976 143 HOH HOH A . VA 10 HOH 77 977 144 HOH HOH A . VA 10 HOH 78 978 145 HOH HOH A . VA 10 HOH 79 979 147 HOH HOH A . VA 10 HOH 80 980 152 HOH HOH A . VA 10 HOH 81 981 155 HOH HOH A . VA 10 HOH 82 982 159 HOH HOH A . VA 10 HOH 83 983 160 HOH HOH A . VA 10 HOH 84 984 162 HOH HOH A . VA 10 HOH 85 985 163 HOH HOH A . VA 10 HOH 86 986 170 HOH HOH A . VA 10 HOH 87 987 172 HOH HOH A . VA 10 HOH 88 988 173 HOH HOH A . VA 10 HOH 89 989 174 HOH HOH A . VA 10 HOH 90 990 176 HOH HOH A . VA 10 HOH 91 991 177 HOH HOH A . VA 10 HOH 92 992 179 HOH HOH A . VA 10 HOH 93 993 181 HOH HOH A . VA 10 HOH 94 994 185 HOH HOH A . VA 10 HOH 95 995 187 HOH HOH A . VA 10 HOH 96 996 189 HOH HOH A . VA 10 HOH 97 997 190 HOH HOH A . VA 10 HOH 98 998 191 HOH HOH A . VA 10 HOH 99 999 192 HOH HOH A . VA 10 HOH 100 1000 193 HOH HOH A . VA 10 HOH 101 1001 201 HOH HOH A . VA 10 HOH 102 1002 203 HOH HOH A . VA 10 HOH 103 1003 204 HOH HOH A . VA 10 HOH 104 1004 205 HOH HOH A . VA 10 HOH 105 1005 206 HOH HOH A . VA 10 HOH 106 1006 209 HOH HOH A . VA 10 HOH 107 1007 211 HOH HOH A . VA 10 HOH 108 1008 215 HOH HOH A . VA 10 HOH 109 1009 216 HOH HOH A . VA 10 HOH 110 1010 217 HOH HOH A . VA 10 HOH 111 1011 219 HOH HOH A . VA 10 HOH 112 1012 220 HOH HOH A . VA 10 HOH 113 1013 223 HOH HOH A . VA 10 HOH 114 1014 226 HOH HOH A . VA 10 HOH 115 1015 230 HOH HOH A . VA 10 HOH 116 1016 231 HOH HOH A . VA 10 HOH 117 1017 234 HOH HOH A . VA 10 HOH 118 1018 235 HOH HOH A . VA 10 HOH 119 1019 237 HOH HOH A . VA 10 HOH 120 1020 240 HOH HOH A . VA 10 HOH 121 1021 244 HOH HOH A . VA 10 HOH 122 1022 245 HOH HOH A . VA 10 HOH 123 1023 246 HOH HOH A . VA 10 HOH 124 1024 247 HOH HOH A . VA 10 HOH 125 1025 249 HOH HOH A . VA 10 HOH 126 1026 250 HOH HOH A . VA 10 HOH 127 1027 251 HOH HOH A . VA 10 HOH 128 1028 253 HOH HOH A . VA 10 HOH 129 1029 257 HOH HOH A . VA 10 HOH 130 1030 258 HOH HOH A . VA 10 HOH 131 1031 259 HOH HOH A . VA 10 HOH 132 1032 262 HOH HOH A . VA 10 HOH 133 1033 263 HOH HOH A . VA 10 HOH 134 1034 266 HOH HOH A . VA 10 HOH 135 1035 267 HOH HOH A . VA 10 HOH 136 1036 269 HOH HOH A . VA 10 HOH 137 1037 272 HOH HOH A . VA 10 HOH 138 1038 274 HOH HOH A . VA 10 HOH 139 1039 276 HOH HOH A . VA 10 HOH 140 1040 284 HOH HOH A . VA 10 HOH 141 1041 285 HOH HOH A . VA 10 HOH 142 1042 286 HOH HOH A . VA 10 HOH 143 1043 288 HOH HOH A . VA 10 HOH 144 1044 290 HOH HOH A . VA 10 HOH 145 1045 291 HOH HOH A . VA 10 HOH 146 1046 293 HOH HOH A . VA 10 HOH 147 1047 295 HOH HOH A . VA 10 HOH 148 1048 298 HOH HOH A . VA 10 HOH 149 1049 300 HOH HOH A . VA 10 HOH 150 1050 301 HOH HOH A . VA 10 HOH 151 1051 307 HOH HOH A . VA 10 HOH 152 1052 310 HOH HOH A . VA 10 HOH 153 1053 311 HOH HOH A . VA 10 HOH 154 1054 312 HOH HOH A . VA 10 HOH 155 1055 313 HOH HOH A . VA 10 HOH 156 1056 317 HOH HOH A . VA 10 HOH 157 1057 319 HOH HOH A . VA 10 HOH 158 1058 325 HOH HOH A . VA 10 HOH 159 1059 326 HOH HOH A . VA 10 HOH 160 1060 327 HOH HOH A . VA 10 HOH 161 1061 332 HOH HOH A . VA 10 HOH 162 1062 334 HOH HOH A . VA 10 HOH 163 1063 335 HOH HOH A . VA 10 HOH 164 1064 336 HOH HOH A . VA 10 HOH 165 1065 338 HOH HOH A . VA 10 HOH 166 1066 339 HOH HOH A . VA 10 HOH 167 1067 341 HOH HOH A . VA 10 HOH 168 1068 343 HOH HOH A . VA 10 HOH 169 1069 345 HOH HOH A . VA 10 HOH 170 1070 346 HOH HOH A . VA 10 HOH 171 1071 347 HOH HOH A . VA 10 HOH 172 1072 349 HOH HOH A . VA 10 HOH 173 1073 350 HOH HOH A . VA 10 HOH 174 1074 351 HOH HOH A . VA 10 HOH 175 1075 352 HOH HOH A . VA 10 HOH 176 1076 353 HOH HOH A . VA 10 HOH 177 1077 356 HOH HOH A . VA 10 HOH 178 1078 358 HOH HOH A . VA 10 HOH 179 1079 359 HOH HOH A . VA 10 HOH 180 1080 360 HOH HOH A . VA 10 HOH 181 1081 361 HOH HOH A . VA 10 HOH 182 1082 363 HOH HOH A . VA 10 HOH 183 1083 365 HOH HOH A . VA 10 HOH 184 1084 367 HOH HOH A . VA 10 HOH 185 1085 370 HOH HOH A . VA 10 HOH 186 1086 371 HOH HOH A . VA 10 HOH 187 1087 376 HOH HOH A . VA 10 HOH 188 1088 378 HOH HOH A . VA 10 HOH 189 1089 381 HOH HOH A . VA 10 HOH 190 1090 384 HOH HOH A . VA 10 HOH 191 1091 388 HOH HOH A . VA 10 HOH 192 1092 389 HOH HOH A . VA 10 HOH 193 1093 390 HOH HOH A . VA 10 HOH 194 1094 391 HOH HOH A . VA 10 HOH 195 1095 392 HOH HOH A . VA 10 HOH 196 1096 393 HOH HOH A . VA 10 HOH 197 1097 394 HOH HOH A . VA 10 HOH 198 1098 395 HOH HOH A . VA 10 HOH 199 1099 399 HOH HOH A . VA 10 HOH 200 1100 400 HOH HOH A . VA 10 HOH 201 1101 414 HOH HOH A . VA 10 HOH 202 1102 415 HOH HOH A . VA 10 HOH 203 1103 419 HOH HOH A . VA 10 HOH 204 1104 420 HOH HOH A . VA 10 HOH 205 1105 421 HOH HOH A . VA 10 HOH 206 1106 422 HOH HOH A . VA 10 HOH 207 1107 425 HOH HOH A . VA 10 HOH 208 1108 426 HOH HOH A . VA 10 HOH 209 1109 427 HOH HOH A . VA 10 HOH 210 1110 433 HOH HOH A . VA 10 HOH 211 1111 434 HOH HOH A . VA 10 HOH 212 1112 436 HOH HOH A . VA 10 HOH 213 1113 437 HOH HOH A . VA 10 HOH 214 1114 439 HOH HOH A . VA 10 HOH 215 1115 443 HOH HOH A . VA 10 HOH 216 1116 444 HOH HOH A . VA 10 HOH 217 1117 449 HOH HOH A . VA 10 HOH 218 1118 450 HOH HOH A . VA 10 HOH 219 1119 451 HOH HOH A . VA 10 HOH 220 1120 453 HOH HOH A . VA 10 HOH 221 1121 455 HOH HOH A . VA 10 HOH 222 1122 456 HOH HOH A . VA 10 HOH 223 1123 458 HOH HOH A . VA 10 HOH 224 1124 460 HOH HOH A . VA 10 HOH 225 1125 462 HOH HOH A . VA 10 HOH 226 1126 465 HOH HOH A . VA 10 HOH 227 1127 468 HOH HOH A . VA 10 HOH 228 1128 472 HOH HOH A . VA 10 HOH 229 1129 474 HOH HOH A . VA 10 HOH 230 1130 476 HOH HOH A . VA 10 HOH 231 1131 478 HOH HOH A . VA 10 HOH 232 1132 482 HOH HOH A . VA 10 HOH 233 1133 484 HOH HOH A . VA 10 HOH 234 1134 485 HOH HOH A . VA 10 HOH 235 1135 488 HOH HOH A . VA 10 HOH 236 1136 489 HOH HOH A . VA 10 HOH 237 1137 490 HOH HOH A . VA 10 HOH 238 1138 492 HOH HOH A . VA 10 HOH 239 1139 493 HOH HOH A . VA 10 HOH 240 1140 498 HOH HOH A . VA 10 HOH 241 1141 499 HOH HOH A . VA 10 HOH 242 1142 502 HOH HOH A . VA 10 HOH 243 1143 503 HOH HOH A . VA 10 HOH 244 1144 505 HOH HOH A . VA 10 HOH 245 1145 506 HOH HOH A . VA 10 HOH 246 1146 509 HOH HOH A . VA 10 HOH 247 1147 511 HOH HOH A . VA 10 HOH 248 1148 512 HOH HOH A . VA 10 HOH 249 1149 513 HOH HOH A . VA 10 HOH 250 1150 519 HOH HOH A . VA 10 HOH 251 1151 522 HOH HOH A . VA 10 HOH 252 1152 523 HOH HOH A . VA 10 HOH 253 1153 524 HOH HOH A . VA 10 HOH 254 1154 526 HOH HOH A . VA 10 HOH 255 1155 528 HOH HOH A . VA 10 HOH 256 1156 529 HOH HOH A . VA 10 HOH 257 1157 531 HOH HOH A . VA 10 HOH 258 1158 535 HOH HOH A . VA 10 HOH 259 1159 537 HOH HOH A . VA 10 HOH 260 1160 538 HOH HOH A . VA 10 HOH 261 1161 539 HOH HOH A . VA 10 HOH 262 1162 542 HOH HOH A . VA 10 HOH 263 1163 544 HOH HOH A . VA 10 HOH 264 1164 545 HOH HOH A . VA 10 HOH 265 1165 547 HOH HOH A . VA 10 HOH 266 1166 554 HOH HOH A . VA 10 HOH 267 1167 555 HOH HOH A . VA 10 HOH 268 1168 557 HOH HOH A . VA 10 HOH 269 1169 563 HOH HOH A . VA 10 HOH 270 1170 564 HOH HOH A . VA 10 HOH 271 1171 565 HOH HOH A . VA 10 HOH 272 1172 572 HOH HOH A . VA 10 HOH 273 1173 573 HOH HOH A . VA 10 HOH 274 1174 574 HOH HOH A . VA 10 HOH 275 1175 581 HOH HOH A . VA 10 HOH 276 1176 587 HOH HOH A . VA 10 HOH 277 1177 588 HOH HOH A . VA 10 HOH 278 1178 589 HOH HOH A . VA 10 HOH 279 1179 593 HOH HOH A . VA 10 HOH 280 1180 596 HOH HOH A . VA 10 HOH 281 1181 609 HOH HOH A . VA 10 HOH 282 1182 614 HOH HOH A . VA 10 HOH 283 1183 617 HOH HOH A . VA 10 HOH 284 1184 618 HOH HOH A . VA 10 HOH 285 1185 620 HOH HOH A . VA 10 HOH 286 1186 623 HOH HOH A . VA 10 HOH 287 1187 625 HOH HOH A . VA 10 HOH 288 1188 628 HOH HOH A . VA 10 HOH 289 1189 631 HOH HOH A . VA 10 HOH 290 1190 632 HOH HOH A . VA 10 HOH 291 1191 634 HOH HOH A . VA 10 HOH 292 1192 635 HOH HOH A . VA 10 HOH 293 1193 636 HOH HOH A . VA 10 HOH 294 1194 638 HOH HOH A . VA 10 HOH 295 1195 639 HOH HOH A . VA 10 HOH 296 1196 643 HOH HOH A . VA 10 HOH 297 1197 647 HOH HOH A . VA 10 HOH 298 1198 654 HOH HOH A . VA 10 HOH 299 1199 660 HOH HOH A . VA 10 HOH 300 1200 661 HOH HOH A . VA 10 HOH 301 1201 662 HOH HOH A . VA 10 HOH 302 1202 670 HOH HOH A . VA 10 HOH 303 1203 672 HOH HOH A . VA 10 HOH 304 1204 678 HOH HOH A . VA 10 HOH 305 1205 680 HOH HOH A . VA 10 HOH 306 1206 681 HOH HOH A . VA 10 HOH 307 1207 682 HOH HOH A . VA 10 HOH 308 1208 685 HOH HOH A . VA 10 HOH 309 1209 686 HOH HOH A . VA 10 HOH 310 1210 692 HOH HOH A . VA 10 HOH 311 1211 693 HOH HOH A . VA 10 HOH 312 1212 695 HOH HOH A . VA 10 HOH 313 1213 697 HOH HOH A . VA 10 HOH 314 1214 699 HOH HOH A . VA 10 HOH 315 1215 702 HOH HOH A . VA 10 HOH 316 1216 707 HOH HOH A . VA 10 HOH 317 1217 710 HOH HOH A . VA 10 HOH 318 1218 711 HOH HOH A . VA 10 HOH 319 1219 713 HOH HOH A . VA 10 HOH 320 1220 714 HOH HOH A . VA 10 HOH 321 1221 715 HOH HOH A . VA 10 HOH 322 1222 716 HOH HOH A . VA 10 HOH 323 1223 717 HOH HOH A . VA 10 HOH 324 1224 718 HOH HOH A . VA 10 HOH 325 1225 719 HOH HOH A . VA 10 HOH 326 1226 720 HOH HOH A . VA 10 HOH 327 1227 721 HOH HOH A . VA 10 HOH 328 1228 722 HOH HOH A . VA 10 HOH 329 1229 724 HOH HOH A . VA 10 HOH 330 1230 725 HOH HOH A . VA 10 HOH 331 1231 726 HOH HOH A . VA 10 HOH 332 1232 728 HOH HOH A . VA 10 HOH 333 1233 729 HOH HOH A . VA 10 HOH 334 1234 730 HOH HOH A . VA 10 HOH 335 1235 732 HOH HOH A . VA 10 HOH 336 1236 733 HOH HOH A . VA 10 HOH 337 1237 740 HOH HOH A . VA 10 HOH 338 1238 742 HOH HOH A . VA 10 HOH 339 1239 743 HOH HOH A . VA 10 HOH 340 1240 762 HOH HOH A . VA 10 HOH 341 1241 763 HOH HOH A . VA 10 HOH 342 1242 764 HOH HOH A . VA 10 HOH 343 1243 765 HOH HOH A . VA 10 HOH 344 1244 766 HOH HOH A . VA 10 HOH 345 1245 767 HOH HOH A . VA 10 HOH 346 1246 768 HOH HOH A . VA 10 HOH 347 1247 770 HOH HOH A . VA 10 HOH 348 1248 771 HOH HOH A . VA 10 HOH 349 1249 772 HOH HOH A . VA 10 HOH 350 1250 773 HOH HOH A . VA 10 HOH 351 1251 774 HOH HOH A . VA 10 HOH 352 1252 775 HOH HOH A . VA 10 HOH 353 1253 776 HOH HOH A . VA 10 HOH 354 1254 777 HOH HOH A . VA 10 HOH 355 1255 780 HOH HOH A . VA 10 HOH 356 1256 781 HOH HOH A . VA 10 HOH 357 1257 782 HOH HOH A . VA 10 HOH 358 1258 783 HOH HOH A . VA 10 HOH 359 1259 784 HOH HOH A . VA 10 HOH 360 1260 785 HOH HOH A . VA 10 HOH 361 1261 786 HOH HOH A . VA 10 HOH 362 1262 787 HOH HOH A . VA 10 HOH 363 1263 790 HOH HOH A . VA 10 HOH 364 1264 114 HOH HOH A . VA 10 HOH 365 1265 198 HOH HOH A . VA 10 HOH 366 1266 241 HOH HOH A . VA 10 HOH 367 1267 527 HOH HOH A . VA 10 HOH 368 1268 530 HOH HOH A . WA 10 HOH 1 902 214 HOH HOH B . WA 10 HOH 2 903 8 HOH HOH B . WA 10 HOH 3 904 9 HOH HOH B . WA 10 HOH 4 905 10 HOH HOH B . WA 10 HOH 5 906 11 HOH HOH B . WA 10 HOH 6 907 12 HOH HOH B . WA 10 HOH 7 908 13 HOH HOH B . WA 10 HOH 8 909 14 HOH HOH B . WA 10 HOH 9 910 17 HOH HOH B . WA 10 HOH 10 911 18 HOH HOH B . WA 10 HOH 11 912 19 HOH HOH B . WA 10 HOH 12 913 21 HOH HOH B . WA 10 HOH 13 914 22 HOH HOH B . WA 10 HOH 14 915 27 HOH HOH B . WA 10 HOH 15 916 28 HOH HOH B . WA 10 HOH 16 917 29 HOH HOH B . WA 10 HOH 17 918 37 HOH HOH B . WA 10 HOH 18 919 38 HOH HOH B . WA 10 HOH 19 920 40 HOH HOH B . WA 10 HOH 20 921 41 HOH HOH B . WA 10 HOH 21 922 51 HOH HOH B . WA 10 HOH 22 923 52 HOH HOH B . WA 10 HOH 23 924 56 HOH HOH B . WA 10 HOH 24 925 59 HOH HOH B . WA 10 HOH 25 926 60 HOH HOH B . WA 10 HOH 26 927 61 HOH HOH B . WA 10 HOH 27 928 62 HOH HOH B . WA 10 HOH 28 929 63 HOH HOH B . WA 10 HOH 29 930 64 HOH HOH B . WA 10 HOH 30 931 65 HOH HOH B . WA 10 HOH 31 932 66 HOH HOH B . WA 10 HOH 32 933 68 HOH HOH B . WA 10 HOH 33 934 70 HOH HOH B . WA 10 HOH 34 935 74 HOH HOH B . WA 10 HOH 35 936 76 HOH HOH B . WA 10 HOH 36 937 80 HOH HOH B . WA 10 HOH 37 938 82 HOH HOH B . WA 10 HOH 38 939 85 HOH HOH B . WA 10 HOH 39 940 87 HOH HOH B . WA 10 HOH 40 941 88 HOH HOH B . WA 10 HOH 41 942 92 HOH HOH B . WA 10 HOH 42 943 95 HOH HOH B . WA 10 HOH 43 944 97 HOH HOH B . WA 10 HOH 44 945 105 HOH HOH B . WA 10 HOH 45 946 107 HOH HOH B . WA 10 HOH 46 947 108 HOH HOH B . WA 10 HOH 47 948 112 HOH HOH B . WA 10 HOH 48 949 115 HOH HOH B . WA 10 HOH 49 950 116 HOH HOH B . WA 10 HOH 50 951 117 HOH HOH B . WA 10 HOH 51 952 118 HOH HOH B . WA 10 HOH 52 953 121 HOH HOH B . WA 10 HOH 53 954 122 HOH HOH B . WA 10 HOH 54 955 123 HOH HOH B . WA 10 HOH 55 956 124 HOH HOH B . WA 10 HOH 56 957 131 HOH HOH B . WA 10 HOH 57 958 134 HOH HOH B . WA 10 HOH 58 959 135 HOH HOH B . WA 10 HOH 59 960 136 HOH HOH B . WA 10 HOH 60 961 142 HOH HOH B . WA 10 HOH 61 962 146 HOH HOH B . WA 10 HOH 62 963 148 HOH HOH B . WA 10 HOH 63 964 149 HOH HOH B . WA 10 HOH 64 965 151 HOH HOH B . WA 10 HOH 65 966 153 HOH HOH B . WA 10 HOH 66 967 154 HOH HOH B . WA 10 HOH 67 968 156 HOH HOH B . WA 10 HOH 68 969 158 HOH HOH B . WA 10 HOH 69 970 164 HOH HOH B . WA 10 HOH 70 971 166 HOH HOH B . WA 10 HOH 71 972 168 HOH HOH B . WA 10 HOH 72 973 169 HOH HOH B . WA 10 HOH 73 974 171 HOH HOH B . WA 10 HOH 74 975 175 HOH HOH B . WA 10 HOH 75 976 178 HOH HOH B . WA 10 HOH 76 977 180 HOH HOH B . WA 10 HOH 77 978 182 HOH HOH B . WA 10 HOH 78 979 183 HOH HOH B . WA 10 HOH 79 980 186 HOH HOH B . WA 10 HOH 80 981 188 HOH HOH B . WA 10 HOH 81 982 195 HOH HOH B . WA 10 HOH 82 983 196 HOH HOH B . WA 10 HOH 83 984 197 HOH HOH B . WA 10 HOH 84 985 199 HOH HOH B . WA 10 HOH 85 986 207 HOH HOH B . WA 10 HOH 86 987 208 HOH HOH B . WA 10 HOH 87 988 210 HOH HOH B . WA 10 HOH 88 989 212 HOH HOH B . WA 10 HOH 89 990 221 HOH HOH B . WA 10 HOH 90 991 222 HOH HOH B . WA 10 HOH 91 992 224 HOH HOH B . WA 10 HOH 92 993 225 HOH HOH B . WA 10 HOH 93 994 227 HOH HOH B . WA 10 HOH 94 995 228 HOH HOH B . WA 10 HOH 95 996 229 HOH HOH B . WA 10 HOH 96 997 232 HOH HOH B . WA 10 HOH 97 998 233 HOH HOH B . WA 10 HOH 98 999 236 HOH HOH B . WA 10 HOH 99 1000 238 HOH HOH B . WA 10 HOH 100 1001 239 HOH HOH B . WA 10 HOH 101 1002 242 HOH HOH B . WA 10 HOH 102 1003 243 HOH HOH B . WA 10 HOH 103 1004 248 HOH HOH B . WA 10 HOH 104 1005 252 HOH HOH B . WA 10 HOH 105 1006 254 HOH HOH B . WA 10 HOH 106 1007 256 HOH HOH B . WA 10 HOH 107 1008 261 HOH HOH B . WA 10 HOH 108 1009 264 HOH HOH B . WA 10 HOH 109 1010 265 HOH HOH B . WA 10 HOH 110 1011 268 HOH HOH B . WA 10 HOH 111 1012 270 HOH HOH B . WA 10 HOH 112 1013 271 HOH HOH B . WA 10 HOH 113 1014 273 HOH HOH B . WA 10 HOH 114 1015 275 HOH HOH B . WA 10 HOH 115 1016 277 HOH HOH B . WA 10 HOH 116 1017 280 HOH HOH B . WA 10 HOH 117 1018 281 HOH HOH B . WA 10 HOH 118 1019 282 HOH HOH B . WA 10 HOH 119 1020 283 HOH HOH B . WA 10 HOH 120 1021 287 HOH HOH B . WA 10 HOH 121 1022 289 HOH HOH B . WA 10 HOH 122 1023 292 HOH HOH B . WA 10 HOH 123 1024 294 HOH HOH B . WA 10 HOH 124 1025 296 HOH HOH B . WA 10 HOH 125 1026 297 HOH HOH B . WA 10 HOH 126 1027 299 HOH HOH B . WA 10 HOH 127 1028 302 HOH HOH B . WA 10 HOH 128 1029 303 HOH HOH B . WA 10 HOH 129 1030 304 HOH HOH B . WA 10 HOH 130 1031 305 HOH HOH B . WA 10 HOH 131 1032 308 HOH HOH B . WA 10 HOH 132 1033 314 HOH HOH B . WA 10 HOH 133 1034 315 HOH HOH B . WA 10 HOH 134 1035 316 HOH HOH B . WA 10 HOH 135 1036 318 HOH HOH B . WA 10 HOH 136 1037 320 HOH HOH B . WA 10 HOH 137 1038 322 HOH HOH B . WA 10 HOH 138 1039 323 HOH HOH B . WA 10 HOH 139 1040 324 HOH HOH B . WA 10 HOH 140 1041 328 HOH HOH B . WA 10 HOH 141 1042 329 HOH HOH B . WA 10 HOH 142 1043 330 HOH HOH B . WA 10 HOH 143 1044 333 HOH HOH B . WA 10 HOH 144 1045 337 HOH HOH B . WA 10 HOH 145 1046 340 HOH HOH B . WA 10 HOH 146 1047 342 HOH HOH B . WA 10 HOH 147 1048 348 HOH HOH B . WA 10 HOH 148 1049 354 HOH HOH B . WA 10 HOH 149 1050 357 HOH HOH B . WA 10 HOH 150 1051 362 HOH HOH B . WA 10 HOH 151 1052 368 HOH HOH B . WA 10 HOH 152 1053 372 HOH HOH B . WA 10 HOH 153 1054 373 HOH HOH B . WA 10 HOH 154 1055 374 HOH HOH B . WA 10 HOH 155 1056 379 HOH HOH B . WA 10 HOH 156 1057 380 HOH HOH B . WA 10 HOH 157 1058 382 HOH HOH B . WA 10 HOH 158 1059 383 HOH HOH B . WA 10 HOH 159 1060 386 HOH HOH B . WA 10 HOH 160 1061 387 HOH HOH B . WA 10 HOH 161 1062 396 HOH HOH B . WA 10 HOH 162 1063 401 HOH HOH B . WA 10 HOH 163 1064 402 HOH HOH B . WA 10 HOH 164 1065 403 HOH HOH B . WA 10 HOH 165 1066 406 HOH HOH B . WA 10 HOH 166 1067 407 HOH HOH B . WA 10 HOH 167 1068 408 HOH HOH B . WA 10 HOH 168 1069 410 HOH HOH B . WA 10 HOH 169 1070 411 HOH HOH B . WA 10 HOH 170 1071 412 HOH HOH B . WA 10 HOH 171 1072 413 HOH HOH B . WA 10 HOH 172 1073 416 HOH HOH B . WA 10 HOH 173 1074 417 HOH HOH B . WA 10 HOH 174 1075 423 HOH HOH B . WA 10 HOH 175 1076 424 HOH HOH B . WA 10 HOH 176 1077 428 HOH HOH B . WA 10 HOH 177 1078 429 HOH HOH B . WA 10 HOH 178 1079 431 HOH HOH B . WA 10 HOH 179 1080 432 HOH HOH B . WA 10 HOH 180 1081 435 HOH HOH B . WA 10 HOH 181 1082 438 HOH HOH B . WA 10 HOH 182 1083 440 HOH HOH B . WA 10 HOH 183 1084 441 HOH HOH B . WA 10 HOH 184 1085 442 HOH HOH B . WA 10 HOH 185 1086 445 HOH HOH B . WA 10 HOH 186 1087 447 HOH HOH B . WA 10 HOH 187 1088 448 HOH HOH B . WA 10 HOH 188 1089 457 HOH HOH B . WA 10 HOH 189 1090 459 HOH HOH B . WA 10 HOH 190 1091 464 HOH HOH B . WA 10 HOH 191 1092 466 HOH HOH B . WA 10 HOH 192 1093 470 HOH HOH B . WA 10 HOH 193 1094 471 HOH HOH B . WA 10 HOH 194 1095 473 HOH HOH B . WA 10 HOH 195 1096 475 HOH HOH B . WA 10 HOH 196 1097 479 HOH HOH B . WA 10 HOH 197 1098 483 HOH HOH B . WA 10 HOH 198 1099 487 HOH HOH B . WA 10 HOH 199 1100 491 HOH HOH B . WA 10 HOH 200 1101 494 HOH HOH B . WA 10 HOH 201 1102 496 HOH HOH B . WA 10 HOH 202 1103 497 HOH HOH B . WA 10 HOH 203 1104 501 HOH HOH B . WA 10 HOH 204 1105 504 HOH HOH B . WA 10 HOH 205 1106 510 HOH HOH B . WA 10 HOH 206 1107 514 HOH HOH B . WA 10 HOH 207 1108 515 HOH HOH B . WA 10 HOH 208 1109 516 HOH HOH B . WA 10 HOH 209 1110 517 HOH HOH B . WA 10 HOH 210 1111 518 HOH HOH B . WA 10 HOH 211 1112 520 HOH HOH B . WA 10 HOH 212 1113 521 HOH HOH B . WA 10 HOH 213 1114 525 HOH HOH B . WA 10 HOH 214 1115 533 HOH HOH B . WA 10 HOH 215 1116 536 HOH HOH B . WA 10 HOH 216 1117 540 HOH HOH B . WA 10 HOH 217 1118 541 HOH HOH B . WA 10 HOH 218 1119 543 HOH HOH B . WA 10 HOH 219 1120 546 HOH HOH B . WA 10 HOH 220 1121 548 HOH HOH B . WA 10 HOH 221 1122 549 HOH HOH B . WA 10 HOH 222 1123 552 HOH HOH B . WA 10 HOH 223 1124 553 HOH HOH B . WA 10 HOH 224 1125 556 HOH HOH B . WA 10 HOH 225 1126 558 HOH HOH B . WA 10 HOH 226 1127 560 HOH HOH B . WA 10 HOH 227 1128 561 HOH HOH B . WA 10 HOH 228 1129 562 HOH HOH B . WA 10 HOH 229 1130 566 HOH HOH B . WA 10 HOH 230 1131 567 HOH HOH B . WA 10 HOH 231 1132 568 HOH HOH B . WA 10 HOH 232 1133 570 HOH HOH B . WA 10 HOH 233 1134 571 HOH HOH B . WA 10 HOH 234 1135 575 HOH HOH B . WA 10 HOH 235 1136 576 HOH HOH B . WA 10 HOH 236 1137 577 HOH HOH B . WA 10 HOH 237 1138 578 HOH HOH B . WA 10 HOH 238 1139 579 HOH HOH B . WA 10 HOH 239 1140 580 HOH HOH B . WA 10 HOH 240 1141 582 HOH HOH B . WA 10 HOH 241 1142 584 HOH HOH B . WA 10 HOH 242 1143 585 HOH HOH B . WA 10 HOH 243 1144 586 HOH HOH B . WA 10 HOH 244 1145 594 HOH HOH B . WA 10 HOH 245 1146 595 HOH HOH B . WA 10 HOH 246 1147 597 HOH HOH B . WA 10 HOH 247 1148 598 HOH HOH B . WA 10 HOH 248 1149 601 HOH HOH B . WA 10 HOH 249 1150 602 HOH HOH B . WA 10 HOH 250 1151 603 HOH HOH B . WA 10 HOH 251 1152 604 HOH HOH B . WA 10 HOH 252 1153 605 HOH HOH B . WA 10 HOH 253 1154 606 HOH HOH B . WA 10 HOH 254 1155 607 HOH HOH B . WA 10 HOH 255 1156 608 HOH HOH B . WA 10 HOH 256 1157 610 HOH HOH B . WA 10 HOH 257 1158 612 HOH HOH B . WA 10 HOH 258 1159 613 HOH HOH B . WA 10 HOH 259 1160 615 HOH HOH B . WA 10 HOH 260 1161 616 HOH HOH B . WA 10 HOH 261 1162 622 HOH HOH B . WA 10 HOH 262 1163 624 HOH HOH B . WA 10 HOH 263 1164 626 HOH HOH B . WA 10 HOH 264 1165 627 HOH HOH B . WA 10 HOH 265 1166 630 HOH HOH B . WA 10 HOH 266 1167 633 HOH HOH B . WA 10 HOH 267 1168 637 HOH HOH B . WA 10 HOH 268 1169 640 HOH HOH B . WA 10 HOH 269 1170 641 HOH HOH B . WA 10 HOH 270 1171 642 HOH HOH B . WA 10 HOH 271 1172 644 HOH HOH B . WA 10 HOH 272 1173 646 HOH HOH B . WA 10 HOH 273 1174 648 HOH HOH B . WA 10 HOH 274 1175 649 HOH HOH B . WA 10 HOH 275 1176 650 HOH HOH B . WA 10 HOH 276 1177 652 HOH HOH B . WA 10 HOH 277 1178 653 HOH HOH B . WA 10 HOH 278 1179 655 HOH HOH B . WA 10 HOH 279 1180 656 HOH HOH B . WA 10 HOH 280 1181 657 HOH HOH B . WA 10 HOH 281 1182 658 HOH HOH B . WA 10 HOH 282 1183 659 HOH HOH B . WA 10 HOH 283 1184 664 HOH HOH B . WA 10 HOH 284 1185 665 HOH HOH B . WA 10 HOH 285 1186 666 HOH HOH B . WA 10 HOH 286 1187 667 HOH HOH B . WA 10 HOH 287 1188 668 HOH HOH B . WA 10 HOH 288 1189 669 HOH HOH B . WA 10 HOH 289 1190 671 HOH HOH B . WA 10 HOH 290 1191 674 HOH HOH B . WA 10 HOH 291 1192 675 HOH HOH B . WA 10 HOH 292 1193 676 HOH HOH B . WA 10 HOH 293 1194 677 HOH HOH B . WA 10 HOH 294 1195 679 HOH HOH B . WA 10 HOH 295 1196 683 HOH HOH B . WA 10 HOH 296 1197 684 HOH HOH B . WA 10 HOH 297 1198 687 HOH HOH B . WA 10 HOH 298 1199 694 HOH HOH B . WA 10 HOH 299 1200 696 HOH HOH B . WA 10 HOH 300 1201 698 HOH HOH B . WA 10 HOH 301 1202 700 HOH HOH B . WA 10 HOH 302 1203 701 HOH HOH B . WA 10 HOH 303 1204 703 HOH HOH B . WA 10 HOH 304 1205 704 HOH HOH B . WA 10 HOH 305 1206 705 HOH HOH B . WA 10 HOH 306 1207 708 HOH HOH B . WA 10 HOH 307 1208 709 HOH HOH B . WA 10 HOH 308 1209 712 HOH HOH B . WA 10 HOH 309 1210 723 HOH HOH B . WA 10 HOH 310 1211 727 HOH HOH B . WA 10 HOH 311 1212 731 HOH HOH B . WA 10 HOH 312 1213 734 HOH HOH B . WA 10 HOH 313 1214 735 HOH HOH B . WA 10 HOH 314 1215 736 HOH HOH B . WA 10 HOH 315 1216 737 HOH HOH B . WA 10 HOH 316 1217 738 HOH HOH B . WA 10 HOH 317 1218 739 HOH HOH B . WA 10 HOH 318 1219 741 HOH HOH B . WA 10 HOH 319 1220 744 HOH HOH B . WA 10 HOH 320 1221 745 HOH HOH B . WA 10 HOH 321 1222 746 HOH HOH B . WA 10 HOH 322 1223 747 HOH HOH B . WA 10 HOH 323 1224 748 HOH HOH B . WA 10 HOH 324 1225 750 HOH HOH B . WA 10 HOH 325 1226 751 HOH HOH B . WA 10 HOH 326 1227 753 HOH HOH B . WA 10 HOH 327 1228 754 HOH HOH B . WA 10 HOH 328 1229 755 HOH HOH B . WA 10 HOH 329 1230 756 HOH HOH B . WA 10 HOH 330 1231 758 HOH HOH B . WA 10 HOH 331 1232 759 HOH HOH B . WA 10 HOH 332 1233 761 HOH HOH B . WA 10 HOH 333 1234 769 HOH HOH B . WA 10 HOH 334 1235 778 HOH HOH B . WA 10 HOH 335 1236 779 HOH HOH B . WA 10 HOH 336 1237 788 HOH HOH B . WA 10 HOH 337 1238 789 HOH HOH B . WA 10 HOH 338 1239 791 HOH HOH B . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 39 A ASN 39 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 88 A ASN 88 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 201 A ASN 201 ? ASN 'GLYCOSYLATION SITE' 4 A ASN 216 A ASN 216 ? ASN 'GLYCOSYLATION SITE' 5 A ASN 289 A ASN 289 ? ASN 'GLYCOSYLATION SITE' 6 A ASN 376 A ASN 376 ? ASN 'GLYCOSYLATION SITE' 7 A ASN 396 A ASN 396 ? ASN 'GLYCOSYLATION SITE' 8 B ASN 39 B ASN 39 ? ASN 'GLYCOSYLATION SITE' 9 B ASN 88 B ASN 88 ? ASN 'GLYCOSYLATION SITE' 10 B ASN 201 B ASN 201 ? ASN 'GLYCOSYLATION SITE' 11 B ASN 216 B ASN 216 ? ASN 'GLYCOSYLATION SITE' 12 B ASN 244 B ASN 244 ? ASN 'GLYCOSYLATION SITE' 13 B ASN 289 B ASN 289 ? ASN 'GLYCOSYLATION SITE' 14 B ASN 376 B ASN 376 ? ASN 'GLYCOSYLATION SITE' 15 B ASN 396 B ASN 396 ? ASN 'GLYCOSYLATION SITE' # loop_ _pdbx_struct_assembly.id _pdbx_struct_assembly.details _pdbx_struct_assembly.method_details _pdbx_struct_assembly.oligomeric_details _pdbx_struct_assembly.oligomeric_count 1 author_and_software_defined_assembly PISA dimeric 2 2 software_defined_assembly PISA dimeric 2 # loop_ _pdbx_struct_assembly_gen.assembly_id _pdbx_struct_assembly_gen.oper_expression _pdbx_struct_assembly_gen.asym_id_list 1 1 A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA,GA,HA,IA,JA,KA,LA,MA,NA,OA,PA,QA,RA,SA,TA,UA,VA,WA 2 1 A,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,VA 2 2 B,Z,AA,BA,CA,DA,EA,FA,GA,HA,IA,JA,KA,LA,MA,NA,OA,PA,QA,RA,SA,TA,UA,WA # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 1 'ABSA (A^2)' 13100 ? 1 MORE -28 ? 1 'SSA (A^2)' 38710 ? 2 'ABSA (A^2)' 12660 ? 2 MORE -32 ? 2 'SSA (A^2)' 39160 ? # loop_ _pdbx_struct_oper_list.id _pdbx_struct_oper_list.type _pdbx_struct_oper_list.name _pdbx_struct_oper_list.symmetry_operation _pdbx_struct_oper_list.matrix[1][1] _pdbx_struct_oper_list.matrix[1][2] _pdbx_struct_oper_list.matrix[1][3] _pdbx_struct_oper_list.vector[1] _pdbx_struct_oper_list.matrix[2][1] _pdbx_struct_oper_list.matrix[2][2] _pdbx_struct_oper_list.matrix[2][3] _pdbx_struct_oper_list.vector[2] _pdbx_struct_oper_list.matrix[3][1] _pdbx_struct_oper_list.matrix[3][2] _pdbx_struct_oper_list.matrix[3][3] _pdbx_struct_oper_list.vector[3] 1 'identity operation' 1_555 x,y,z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 2 'crystal symmetry operation' 3_445 x-1/2,y-1/2,z 1.0000000000 0.0000000000 0.0000000000 -86.7550000000 0.0000000000 1.0000000000 0.0000000000 -31.0100000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 # loop_ _pdbx_struct_conn_angle.id _pdbx_struct_conn_angle.ptnr1_label_atom_id _pdbx_struct_conn_angle.ptnr1_label_alt_id _pdbx_struct_conn_angle.ptnr1_label_asym_id _pdbx_struct_conn_angle.ptnr1_label_comp_id _pdbx_struct_conn_angle.ptnr1_label_seq_id _pdbx_struct_conn_angle.ptnr1_auth_atom_id _pdbx_struct_conn_angle.ptnr1_auth_asym_id _pdbx_struct_conn_angle.ptnr1_auth_comp_id _pdbx_struct_conn_angle.ptnr1_auth_seq_id _pdbx_struct_conn_angle.ptnr1_PDB_ins_code _pdbx_struct_conn_angle.ptnr1_symmetry _pdbx_struct_conn_angle.ptnr2_label_atom_id _pdbx_struct_conn_angle.ptnr2_label_alt_id _pdbx_struct_conn_angle.ptnr2_label_asym_id _pdbx_struct_conn_angle.ptnr2_label_comp_id _pdbx_struct_conn_angle.ptnr2_label_seq_id _pdbx_struct_conn_angle.ptnr2_auth_atom_id _pdbx_struct_conn_angle.ptnr2_auth_asym_id _pdbx_struct_conn_angle.ptnr2_auth_comp_id _pdbx_struct_conn_angle.ptnr2_auth_seq_id _pdbx_struct_conn_angle.ptnr2_PDB_ins_code _pdbx_struct_conn_angle.ptnr2_symmetry _pdbx_struct_conn_angle.ptnr3_label_atom_id _pdbx_struct_conn_angle.ptnr3_label_alt_id _pdbx_struct_conn_angle.ptnr3_label_asym_id _pdbx_struct_conn_angle.ptnr3_label_comp_id _pdbx_struct_conn_angle.ptnr3_label_seq_id _pdbx_struct_conn_angle.ptnr3_auth_atom_id _pdbx_struct_conn_angle.ptnr3_auth_asym_id _pdbx_struct_conn_angle.ptnr3_auth_comp_id _pdbx_struct_conn_angle.ptnr3_auth_seq_id _pdbx_struct_conn_angle.ptnr3_PDB_ins_code _pdbx_struct_conn_angle.ptnr3_symmetry _pdbx_struct_conn_angle.value _pdbx_struct_conn_angle.value_esd 1 NE2 ? A HIS 93 ? A HIS 93 ? 1_555 CU ? U CU . ? A CU 604 ? 1_555 NE2 ? A HIS 434 ? A HIS 434 ? 1_555 169.4 ? 2 ND1 ? A HIS 95 ? A HIS 95 ? 1_555 CU ? T CU . ? A CU 603 ? 1_555 NE2 ? A HIS 138 ? A HIS 138 ? 1_555 143.1 ? 3 ND1 ? A HIS 95 ? A HIS 95 ? 1_555 CU ? T CU . ? A CU 603 ? 1_555 NE2 ? A HIS 504 ? A HIS 504 ? 1_555 112.8 ? 4 NE2 ? A HIS 138 ? A HIS 138 ? 1_555 CU ? T CU . ? A CU 603 ? 1_555 NE2 ? A HIS 504 ? A HIS 504 ? 1_555 99.9 ? 5 ND1 ? A HIS 95 ? A HIS 95 ? 1_555 CU ? T CU . ? A CU 603 ? 1_555 O2 ? Y OXY . ? A OXY 900 ? 1_555 112.0 ? 6 NE2 ? A HIS 138 ? A HIS 138 ? 1_555 CU ? T CU . ? A CU 603 ? 1_555 O2 ? Y OXY . ? A OXY 900 ? 1_555 87.1 ? 7 NE2 ? A HIS 504 ? A HIS 504 ? 1_555 CU ? T CU . ? A CU 603 ? 1_555 O2 ? Y OXY . ? A OXY 900 ? 1_555 84.1 ? 8 NE2 ? A HIS 140 ? A HIS 140 ? 1_555 CU ? S CU . ? A CU 602 ? 1_555 NE2 ? A HIS 436 ? A HIS 436 ? 1_555 126.7 ? 9 NE2 ? A HIS 140 ? A HIS 140 ? 1_555 CU ? S CU . ? A CU 602 ? 1_555 NE2 ? A HIS 502 ? A HIS 502 ? 1_555 123.8 ? 10 NE2 ? A HIS 436 ? A HIS 436 ? 1_555 CU ? S CU . ? A CU 602 ? 1_555 NE2 ? A HIS 502 ? A HIS 502 ? 1_555 106.3 ? 11 NE2 ? A HIS 140 ? A HIS 140 ? 1_555 CU ? S CU . ? A CU 602 ? 1_555 O1 ? Y OXY . ? A OXY 900 ? 1_555 79.7 ? 12 NE2 ? A HIS 436 ? A HIS 436 ? 1_555 CU ? S CU . ? A CU 602 ? 1_555 O1 ? Y OXY . ? A OXY 900 ? 1_555 119.9 ? 13 NE2 ? A HIS 502 ? A HIS 502 ? 1_555 CU ? S CU . ? A CU 602 ? 1_555 O1 ? Y OXY . ? A OXY 900 ? 1_555 90.1 ? 14 NE2 ? A HIS 140 ? A HIS 140 ? 1_555 CU ? S CU . ? A CU 602 ? 1_555 O2 ? Y OXY . ? A OXY 900 ? 1_555 102.5 ? 15 NE2 ? A HIS 436 ? A HIS 436 ? 1_555 CU ? S CU . ? A CU 602 ? 1_555 O2 ? Y OXY . ? A OXY 900 ? 1_555 92.7 ? 16 NE2 ? A HIS 502 ? A HIS 502 ? 1_555 CU ? S CU . ? A CU 602 ? 1_555 O2 ? Y OXY . ? A OXY 900 ? 1_555 91.0 ? 17 O1 ? Y OXY . ? A OXY 900 ? 1_555 CU ? S CU . ? A CU 602 ? 1_555 O2 ? Y OXY . ? A OXY 900 ? 1_555 28.2 ? 18 ND1 ? A HIS 431 ? A HIS 431 ? 1_555 CU ? R CU . ? A CU 601 ? 1_555 ND1 ? A HIS 508 ? A HIS 508 ? 1_555 105.2 ? 19 ND1 ? A HIS 431 ? A HIS 431 ? 1_555 CU ? R CU . ? A CU 601 ? 1_555 SG ? A CYS 503 ? A CYS 503 ? 1_555 126.2 ? 20 ND1 ? A HIS 508 ? A HIS 508 ? 1_555 CU ? R CU . ? A CU 601 ? 1_555 SG ? A CYS 503 ? A CYS 503 ? 1_555 126.7 ? 21 NE2 ? B HIS 93 ? B HIS 93 ? 1_555 CU ? RA CU . ? B CU 604 ? 1_555 NE2 ? B HIS 434 ? B HIS 434 ? 1_555 161.4 ? 22 ND1 ? B HIS 95 ? B HIS 95 ? 1_555 CU ? QA CU . ? B CU 603 ? 1_555 NE2 ? B HIS 138 ? B HIS 138 ? 1_555 145.6 ? 23 ND1 ? B HIS 95 ? B HIS 95 ? 1_555 CU ? QA CU . ? B CU 603 ? 1_555 NE2 ? B HIS 504 ? B HIS 504 ? 1_555 104.0 ? 24 NE2 ? B HIS 138 ? B HIS 138 ? 1_555 CU ? QA CU . ? B CU 603 ? 1_555 NE2 ? B HIS 504 ? B HIS 504 ? 1_555 109.7 ? 25 ND1 ? B HIS 95 ? B HIS 95 ? 1_555 CU ? QA CU . ? B CU 603 ? 1_555 O2 ? TA OXY . ? B OXY 901 ? 1_555 102.1 ? 26 NE2 ? B HIS 138 ? B HIS 138 ? 1_555 CU ? QA CU . ? B CU 603 ? 1_555 O2 ? TA OXY . ? B OXY 901 ? 1_555 92.9 ? 27 NE2 ? B HIS 504 ? B HIS 504 ? 1_555 CU ? QA CU . ? B CU 603 ? 1_555 O2 ? TA OXY . ? B OXY 901 ? 1_555 75.0 ? 28 NE2 ? B HIS 140 ? B HIS 140 ? 1_555 CU ? PA CU . ? B CU 602 ? 1_555 NE2 ? B HIS 436 ? B HIS 436 ? 1_555 118.1 ? 29 NE2 ? B HIS 140 ? B HIS 140 ? 1_555 CU ? PA CU . ? B CU 602 ? 1_555 NE2 ? B HIS 502 ? B HIS 502 ? 1_555 121.4 ? 30 NE2 ? B HIS 436 ? B HIS 436 ? 1_555 CU ? PA CU . ? B CU 602 ? 1_555 NE2 ? B HIS 502 ? B HIS 502 ? 1_555 108.0 ? 31 NE2 ? B HIS 140 ? B HIS 140 ? 1_555 CU ? PA CU . ? B CU 602 ? 1_555 O1 ? TA OXY . ? B OXY 901 ? 1_555 88.0 ? 32 NE2 ? B HIS 436 ? B HIS 436 ? 1_555 CU ? PA CU . ? B CU 602 ? 1_555 O1 ? TA OXY . ? B OXY 901 ? 1_555 121.4 ? 33 NE2 ? B HIS 502 ? B HIS 502 ? 1_555 CU ? PA CU . ? B CU 602 ? 1_555 O1 ? TA OXY . ? B OXY 901 ? 1_555 97.6 ? 34 NE2 ? B HIS 140 ? B HIS 140 ? 1_555 CU ? PA CU . ? B CU 602 ? 1_555 O2 ? TA OXY . ? B OXY 901 ? 1_555 115.0 ? 35 NE2 ? B HIS 436 ? B HIS 436 ? 1_555 CU ? PA CU . ? B CU 602 ? 1_555 O2 ? TA OXY . ? B OXY 901 ? 1_555 97.1 ? 36 NE2 ? B HIS 502 ? B HIS 502 ? 1_555 CU ? PA CU . ? B CU 602 ? 1_555 O2 ? TA OXY . ? B OXY 901 ? 1_555 91.7 ? 37 O1 ? TA OXY . ? B OXY 901 ? 1_555 CU ? PA CU . ? B CU 602 ? 1_555 O2 ? TA OXY . ? B OXY 901 ? 1_555 29.1 ? 38 ND1 ? B HIS 431 ? B HIS 431 ? 1_555 CU ? OA CU . ? B CU 601 ? 1_555 ND1 ? B HIS 508 ? B HIS 508 ? 1_555 103.7 ? 39 ND1 ? B HIS 431 ? B HIS 431 ? 1_555 CU ? OA CU . ? B CU 601 ? 1_555 SG ? B CYS 503 ? B CYS 503 ? 1_555 125.6 ? 40 ND1 ? B HIS 508 ? B HIS 508 ? 1_555 CU ? OA CU . ? B CU 601 ? 1_555 SG ? B CYS 503 ? B CYS 503 ? 1_555 130.4 ? # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2009-07-07 2 'Structure model' 1 1 2011-07-13 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Non-polymer description' 2 2 'Structure model' 'Version format compliance' # loop_ _software.name _software.version _software.date _software.type _software.contact_author _software.contact_author_email _software.classification _software.location _software.language _software.citation_id _software.pdbx_ordinal XSCALE . ? package 'Wolfgang Kabsch' ? 'data processing' http://www.mpimf-heidelberg.mpg.de/~kabsch/xds/html_doc/xscale_program.html ? ? 1 CNS . ? package 'Axel T. Brunger' axel.brunger@yale.edu refinement http://cns-online.org/ Fortran_77 ? 2 PDB_EXTRACT 3.006 'June 11, 2008' package PDB help@deposit.rcsb.org 'data extraction' http://sw-tools.pdb.org/apps/PDB_EXTRACT/ C++ ? 3 XDS . ? ? ? ? 'data reduction' ? ? ? 4 XSCALE . ? ? ? ? 'data scaling' ? ? ? 5 MOLREP . ? ? ? ? phasing ? ? ? 6 # 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 TRP A 13 ? ? -134.51 -62.72 2 1 LYS A 100 ? ? -58.26 107.47 3 1 VAL A 111 ? ? -128.23 -65.77 4 1 SER A 142 ? ? 60.26 -129.43 5 1 GLU A 235 ? ? -147.09 -47.07 6 1 ASP A 253 ? ? 60.49 -127.74 7 1 PRO A 283 ? ? -57.25 95.83 8 1 GLN A 295 ? ? 31.90 58.15 9 1 ASN A 421 ? ? -103.14 72.87 10 1 ASP A 556 ? ? -122.68 -163.21 11 1 THR B 3 ? ? -92.90 -63.38 12 1 TRP B 13 ? ? -136.94 -58.71 13 1 VAL B 111 ? ? -129.54 -67.56 14 1 PRO B 118 ? ? -74.59 -163.94 15 1 SER B 142 ? ? 59.97 -124.10 16 1 GLU B 235 ? ? -142.74 -51.21 17 1 ASP B 253 ? ? 57.29 -127.62 18 1 PRO B 283 ? ? -58.46 99.06 19 1 ALA B 296 ? ? 59.33 16.61 20 1 ASN B 381 ? ? -151.11 88.03 21 1 ASP B 556 ? ? -122.52 -161.49 # loop_ _pdbx_validate_planes.id _pdbx_validate_planes.PDB_model_num _pdbx_validate_planes.auth_comp_id _pdbx_validate_planes.auth_asym_id _pdbx_validate_planes.auth_seq_id _pdbx_validate_planes.PDB_ins_code _pdbx_validate_planes.label_alt_id _pdbx_validate_planes.rmsd _pdbx_validate_planes.type 1 1 TYR A 546 ? ? 0.080 'SIDE CHAIN' 2 1 TYR B 546 ? ? 0.090 'SIDE CHAIN' # 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 GLU 1 ? A GLU 1 2 1 Y 1 B GLU 1 ? B GLU 1 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 BETA-D-MANNOSE BMA 4 ALPHA-D-MANNOSE MAN 5 'COPPER (II) ION' CU 6 'CHLORIDE ION' CL 7 'SULFATE ION' SO4 8 'OXYGEN MOLECULE' OXY 9 GLYCEROL GOL 10 water HOH #