data_2IH8 # _entry.id 2IH8 # _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 2IH8 RCSB RCSB039567 WWPDB D_1000039567 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 1GW0 'The crystal structure of Melanocarpus albomyces laccase in four copper form, determined at 2.40 angstrom resolution' unspecified PDB 2IH9 'The high-dose crystal structure of a recombinant Melanocarpus albomyces laccase, determined at 2.00 angstrom resolution' unspecified # _pdbx_database_status.entry_id 2IH8 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.recvd_initial_deposition_date 2006-09-26 _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.pdb_format_compatible Y _pdbx_database_status.status_code_cs ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Hakulinen, N.' 1 'Rouvinen, J.' 2 # _citation.id primary _citation.title ;A crystallographic and spectroscopic study on the effect of X-ray radiation on the crystal structure of Melanocarpus albomyces laccase. ; _citation.journal_abbrev Biochem.Biophys.Res.Commun. _citation.journal_volume 350 _citation.page_first 929 _citation.page_last 934 _citation.year 2006 _citation.journal_id_ASTM BBRCA9 _citation.country US _citation.journal_id_ISSN 0006-291X _citation.journal_id_CSD 0146 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 17045575 _citation.pdbx_database_id_DOI 10.1016/j.bbrc.2006.09.144 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Hakulinen, N.' 1 primary 'Kruus, K.' 2 primary 'Koivula, A.' 3 primary 'Rouvinen, J.' 4 # _cell.entry_id 2IH8 _cell.length_a 173.060 _cell.length_b 61.810 _cell.length_c 123.910 _cell.angle_alpha 90.00 _cell.angle_beta 96.36 _cell.angle_gamma 90.00 _cell.Z_PDB 8 _cell.pdbx_unique_axis ? _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.entry_id 2IH8 _symmetry.space_group_name_H-M 'C 1 2 1' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 5 _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 61845.441 2 1.10.3.2 ? ? ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 22 ? ? ? ? 3 non-polymer man BETA-D-MANNOSE 180.156 5 ? ? ? ? 4 non-polymer man ALPHA-D-MANNOSE 180.156 3 ? ? ? ? 5 non-polymer man '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' 221.208 1 ? ? ? ? 6 non-polymer syn 'COPPER (II) ION' 63.546 8 ? ? ? ? 7 non-polymer syn 'CHLORIDE ION' 35.453 2 ? ? ? ? 8 non-polymer syn 'SULFATE ION' 96.063 3 ? ? ? ? 9 non-polymer syn 'OXYGEN MOLECULE' 31.999 2 ? ? ? ? 10 water nat water 18.015 1156 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'Benzenediol:oxygen oxidoreductase, Urishiol oxidase, 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 LPAGGWLLLAFRTDNPGAWLFHCHIAWHVSGGLSVDFLERPADLRQRISQEDEDDFNRVCDEWRAYWPTNPYPKIDSGL ; _entity_poly.pdbx_seq_one_letter_code_can ;EPTCNTPSNRACWSDGFDINTDYEVSTPDTGVTQSYVFNLTEVDNWMGPDGVVKEKVMLINGNIMGPNIVANWGDTVEVT VINNLVTNGTSIHWHGIHQKDTNLHDGANGVTECPIPPKGGQRTYRWRARQYGTSWYHSHFSAQYGNGVVGTIQINGPAS LPYDIDLGVFPITDYYYRAADDLVHFTQNNAPPFSDNVLINGTAVNPNTGEGQYANVTLTPGKRHRLRILNTSTENHFQV SLVNHTMTVIAADMVPVNAMTVDSLFLAVGQRYDVVIDASRAPDNYWFNVTFGGQAACGGSLNPHPAAIFHYAGAPGGLP TDEGTPPVDHQCLDTLDVRPVVPRSVPVNSFVKRPDNTLPVALDLTGTPLFVWKVNGSDINVDWGKPIIDYILTGNTSYP VSDNIVQVDAVDQWTYWLIENDPEGPFSLPHPMHLHGHDFLVLGRSPDVPAASQQRFVFDPAVDLARLNGDNPPRRDTTM LPAGGWLLLAFRTDNPGAWLFHCHIAWHVSGGLSVDFLERPADLRQRISQEDEDDFNRVCDEWRAYWPTNPYPKIDSGL ; _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 LEU 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 Melanocarpus _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 'Hypocrea jecorina' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 51453 _entity_src_gen.host_org_genus Hypocrea _entity_src_gen.pdbx_host_org_gene ? _entity_src_gen.pdbx_host_org_organ ? _entity_src_gen.host_org_species ? _entity_src_gen.pdbx_host_org_tissue ? _entity_src_gen.pdbx_host_org_tissue_fraction ? _entity_src_gen.pdbx_host_org_strain ? _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line ? _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type ? _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name ? _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code LAC1_MELAO _struct_ref.pdbx_db_accession Q70KY3 _struct_ref.entity_id 1 _struct_ref.pdbx_align_begin 51 _struct_ref.pdbx_db_isoform ? _struct_ref.pdbx_seq_one_letter_code ? # 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 2IH8 A 1 ? 559 ? Q70KY3 51 ? 609 ? 1 559 2 1 2IH8 B 1 ? 559 ? Q70KY3 51 ? 609 ? 1 559 # 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 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 NDG D-saccharide . '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' ? '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 2IH8 _exptl.method 'X-RAY DIFFRACTION' # _exptl_crystal.id 1 _exptl_crystal.density_Matthews 2.66 _exptl_crystal.density_meas ? _exptl_crystal.density_percent_sol 53.77 _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 5.0 _exptl_crystal_grow.temp 295 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pdbx_details '17% PEG MME2000, 0.1M Ammonium sulfate, 0.1M Sodium acetate, pH 5.0, 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 'MAR CCD 165 mm' _diffrn_detector.pdbx_collection_date 2005-01-21 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.monochromator 'Si [111], horizontally focusing' _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 0.81000 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'EMBL/DESY, HAMBURG BEAMLINE X11' _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 0.81000 _diffrn_source.pdbx_synchrotron_site 'EMBL/DESY, Hamburg' _diffrn_source.pdbx_synchrotron_beamline X11 # _reflns.entry_id 2IH8 _reflns.observed_criterion_sigma_F ? _reflns.observed_criterion_sigma_I -3 _reflns.d_resolution_high 2.0 _reflns.d_resolution_low 25.0 _reflns.number_all ? _reflns.number_obs 88169 _reflns.percent_possible_obs 99.8 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rsym_value 0.074 _reflns.pdbx_netI_over_sigmaI 17.1 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 3.8 _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 2.0 _reflns_shell.d_res_low 2.1 _reflns_shell.percent_possible_obs ? _reflns_shell.percent_possible_all 100 _reflns_shell.Rmerge_I_obs ? _reflns_shell.meanI_over_sigI_obs 6.2 _reflns_shell.pdbx_Rsym_value 0.278 _reflns_shell.pdbx_redundancy 3.8 _reflns_shell.number_unique_all 11895 _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 # _refine.entry_id 2IH8 _refine.ls_d_res_high 2.000 _refine.ls_d_res_low 25.000 _refine.pdbx_ls_sigma_F 0.00 _refine.ls_percent_reflns_obs 99.900 _refine.ls_number_reflns_obs 88169 _refine.ls_R_factor_R_work 0.1827 _refine.ls_R_factor_R_free 0.2135 _refine.ls_percent_reflns_R_free 5.000 _refine.ls_number_reflns_R_free 4409 _refine.B_iso_mean 19.264 _refine.solvent_model_param_bsol 11.856 _refine.aniso_B[1][1] 1.080 _refine.aniso_B[2][2] -0.888 _refine.aniso_B[3][3] -0.192 _refine.aniso_B[1][2] 0.000 _refine.aniso_B[1][3] -0.097 _refine.aniso_B[2][3] 0.000 _refine.pdbx_ls_sigma_I ? _refine.ls_number_reflns_all 88169 _refine.ls_R_factor_all ? _refine.ls_R_factor_obs 0.1827 _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_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_starting_model 'PDB entry 1GW0' _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.occupancy_max ? _refine.occupancy_min ? _refine.pdbx_isotropic_thermal_model Isotropic _refine.details ? _refine.B_iso_min ? _refine.B_iso_max ? _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_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_overall_phase_error ? _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 8738 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 439 _refine_hist.number_atoms_solvent 1156 _refine_hist.number_atoms_total 10333 _refine_hist.d_res_high 2.000 _refine_hist.d_res_low 25.000 # 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 ? 0.011 ? ? 'X-RAY DIFFRACTION' ? c_angle_deg ? 1.575 ? ? 'X-RAY DIFFRACTION' ? c_mcbond_it ? 1.066 1.500 ? 'X-RAY DIFFRACTION' ? c_scbond_it ? 1.745 2.000 ? 'X-RAY DIFFRACTION' ? c_mcangle_it ? 1.585 2.000 ? 'X-RAY DIFFRACTION' ? c_scangle_it ? 2.500 2.500 ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.d_res_high 2.0 _refine_ls_shell.d_res_low 2.1 _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.number_reflns_R_free ? _refine_ls_shell.R_factor_R_work 0.227 _refine_ls_shell.R_factor_R_free 0.27 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_obs ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.pdbx_total_number_of_bins_used ? _refine_ls_shell.number_reflns_R_work ? _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.pdbx_refine_id '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 CNS_TOPPAR:protein.param CNS_TOPPAR:protein.top 'X-RAY DIFFRACTION' 2 CNS_TOPPAR:carbohydrate.param CNS_TOPPAR:carbohydrate.top 'X-RAY DIFFRACTION' 3 CNS_TOPPAR:water_rep.param CNS_TOPPAR:water.top 'X-RAY DIFFRACTION' 4 CNS_TOPPAR:ion.param CNS_TOPPAR:ion.top 'X-RAY DIFFRACTION' 5 ? CNS_TOPPAR:nina.top 'X-RAY DIFFRACTION' # _struct.entry_id 2IH8 _struct.title 'A low-dose crystal structure of a recombinant 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 2IH8 _struct_keywords.pdbx_keywords OXIDOREDUCTASE _struct_keywords.text 'laccase, multicopper oxidase, redox-enzyme, 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 4 ? I N N 2 ? J N N 2 ? K N N 3 ? L N N 2 ? M N N 2 ? N N N 3 ? O N N 2 ? P N N 2 ? Q N N 2 ? R N N 2 ? S N N 5 ? T N N 6 ? U N N 6 ? V N N 6 ? W N N 6 ? X N N 7 ? Y N N 8 ? Z N N 8 ? AA N N 9 ? BA N N 2 ? CA N N 2 ? DA N N 2 ? EA N N 3 ? FA N N 4 ? GA N N 2 ? HA N N 2 ? IA N N 2 ? JA N N 2 ? KA N N 3 ? LA N N 2 ? MA N N 2 ? NA N N 2 ? OA N N 2 ? PA N N 6 ? QA N N 6 ? RA N N 6 ? SA N N 6 ? TA N N 7 ? UA N N 8 ? VA N N 9 ? WA N N 10 ? XA N N 10 ? # _struct_biol.id 1 # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 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 GLY A 293 ? ALA A 297 ? GLY A 293 ALA A 297 5 ? 5 HELX_P HELX_P5 5 ARG A 354 ? ASP A 356 ? ARG A 354 ASP A 356 5 ? 3 HELX_P HELX_P6 6 PRO A 387 ? GLY A 395 ? PRO A 387 GLY A 395 1 ? 9 HELX_P HELX_P7 7 PRO A 400 ? ASP A 403 ? PRO A 400 ASP A 403 5 ? 4 HELX_P HELX_P8 8 ASP A 460 ? LEU A 465 ? ASP A 460 LEU A 465 1 ? 6 HELX_P HELX_P9 9 ALA A 466 ? LEU A 468 ? ALA A 466 LEU A 468 5 ? 3 HELX_P HELX_P10 10 ILE A 505 ? GLY A 511 ? ILE A 505 GLY A 511 1 ? 7 HELX_P HELX_P11 11 ARG A 520 ? ILE A 528 ? ARG A 520 ILE A 528 1 ? 9 HELX_P HELX_P12 12 SER A 529 ? TRP A 547 ? SER A 529 TRP A 547 1 ? 19 HELX_P HELX_P13 13 PRO A 548 ? ASN A 550 ? PRO A 548 ASN A 550 5 ? 3 HELX_P HELX_P14 14 THR B 102 ? ASP B 106 ? THR B 102 ASP B 106 5 ? 5 HELX_P HELX_P15 15 ALA B 143 ? GLY B 148 ? ALA B 143 GLY B 148 5 ? 6 HELX_P HELX_P16 16 ALA B 179 ? ASN B 190 ? ALA B 179 ASN B 190 1 ? 12 HELX_P HELX_P17 17 GLY B 293 ? ALA B 297 ? GLY B 293 ALA B 297 5 ? 5 HELX_P HELX_P18 18 ARG B 354 ? ASP B 356 ? ARG B 354 ASP B 356 5 ? 3 HELX_P HELX_P19 19 PRO B 387 ? THR B 394 ? PRO B 387 THR B 394 1 ? 8 HELX_P HELX_P20 20 PRO B 400 ? ASP B 403 ? PRO B 400 ASP B 403 5 ? 4 HELX_P HELX_P21 21 ASP B 460 ? LEU B 465 ? ASP B 460 LEU B 465 1 ? 6 HELX_P HELX_P22 22 ILE B 505 ? GLY B 511 ? ILE B 505 GLY B 511 1 ? 7 HELX_P HELX_P23 23 ARG B 520 ? ILE B 528 ? ARG B 520 ILE B 528 1 ? 9 HELX_P HELX_P24 24 SER B 529 ? TRP B 547 ? SER B 529 TRP B 547 1 ? 19 HELX_P HELX_P25 25 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 ? ? ? ? ? ? ? 2.029 ? disulf2 disulf ? ? A CYS 114 SG ? ? ? 1_555 A CYS 540 SG ? ? A CYS 114 A CYS 540 1_555 ? ? ? ? ? ? ? 2.033 ? disulf3 disulf ? ? A CYS 298 SG ? ? ? 1_555 A CYS 332 SG ? ? A CYS 298 A CYS 332 1_555 ? ? ? ? ? ? ? 2.029 ? disulf4 disulf ? ? B CYS 4 SG ? ? ? 1_555 B CYS 12 SG ? ? B CYS 4 B CYS 12 1_555 ? ? ? ? ? ? ? 2.029 ? disulf5 disulf ? ? B CYS 114 SG ? ? ? 1_555 B CYS 540 SG ? ? B CYS 114 B CYS 540 1_555 ? ? ? ? ? ? ? 2.027 ? disulf6 disulf ? ? B CYS 298 SG ? ? ? 1_555 B CYS 332 SG ? ? B CYS 298 B CYS 332 1_555 ? ? ? ? ? ? ? 2.026 ? covale1 covale ? ? A ASN 39 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 39 A NAG 700 1_555 ? ? ? ? ? ? ? 1.449 ? covale2 covale ? ? A ASN 201 ND2 ? ? ? 1_555 R NAG . C1 ? ? A ASN 201 A NAG 760 1_555 ? ? ? ? ? ? ? 1.452 ? covale3 covale ? ? A ASN 396 ND2 ? ? ? 1_555 Q NAG . C1 ? ? A ASN 396 A NAG 750 1_555 ? ? ? ? ? ? ? 1.450 ? covale4 covale ? ? B ASN 39 ND2 ? ? ? 1_555 BA NAG . C1 ? ? B ASN 39 B NAG 700 1_555 ? ? ? ? ? ? ? 1.449 ? covale5 covale ? ? B ASN 201 ND2 ? ? ? 1_555 OA NAG . C1 ? ? B ASN 201 B NAG 760 1_555 ? ? ? ? ? ? ? 1.452 ? covale6 covale ? ? B ASN 396 ND2 ? ? ? 1_555 NA NAG . C1 ? ? B ASN 396 B NAG 750 1_555 ? ? ? ? ? ? ? 1.448 ? covale7 covale ? ? A ASN 88 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 88 A NAG 710 1_555 ? ? ? ? ? ? ? 1.447 ? covale8 covale ? ? A ASN 216 ND2 ? ? ? 1_555 I NAG . C1 ? ? A ASN 216 A NAG 720 1_555 ? ? ? ? ? ? ? 1.446 ? covale9 covale ? ? A ASN 244 ND2 ? ? ? 1_555 S NDG . C1 ? ? A ASN 244 A NDG 770 1_555 ? ? ? ? ? ? ? 1.451 ? covale10 covale ? ? A ASN 289 ND2 ? ? ? 1_555 L NAG . C1 ? ? A ASN 289 A NAG 730 1_555 ? ? ? ? ? ? ? 1.448 ? covale11 covale ? ? A ASN 376 ND2 ? ? ? 1_555 O NAG . C1 ? ? A ASN 376 A NAG 740 1_555 ? ? ? ? ? ? ? 1.451 ? covale12 covale ? ? B ASN 88 ND2 ? ? ? 1_555 CA NAG . C1 ? ? B ASN 88 B NAG 710 1_555 ? ? ? ? ? ? ? 1.446 ? covale13 covale ? ? B ASN 216 ND2 ? ? ? 1_555 GA NAG . C1 ? ? B ASN 216 B NAG 720 1_555 ? ? ? ? ? ? ? 1.448 ? covale14 covale ? ? B ASN 289 ND2 ? ? ? 1_555 IA NAG . C1 ? ? B ASN 289 B NAG 730 1_555 ? ? ? ? ? ? ? 1.449 ? covale15 covale ? ? B ASN 376 ND2 ? ? ? 1_555 LA NAG . C1 ? ? B ASN 376 B NAG 740 1_555 ? ? ? ? ? ? ? 1.451 ? covale16 covale ? ? D NAG . O4 ? ? ? 1_555 E NAG . C1 ? ? A NAG 710 A NAG 711 1_555 ? ? ? ? ? ? ? 1.382 ? covale17 covale ? ? E NAG . O4 ? ? ? 1_555 F BMA . C1 ? ? A NAG 711 A BMA 712 1_555 ? ? ? ? ? ? ? 1.383 ? covale18 covale ? ? F BMA . O3 ? ? ? 1_555 G MAN . C1 ? ? A BMA 712 A MAN 713 1_555 ? ? ? ? ? ? ? 1.404 ? covale19 covale ? ? F BMA . O6 ? ? ? 1_555 H MAN . C1 ? ? A BMA 712 A MAN 714 1_555 ? ? ? ? ? ? ? 1.404 ? covale20 covale ? ? I NAG . O4 ? ? ? 1_555 J NAG . C1 ? ? A NAG 720 A NAG 721 1_555 ? ? ? ? ? ? ? 1.382 ? covale21 covale ? ? J NAG . O4 ? ? ? 1_555 K BMA . C1 ? ? A NAG 721 A BMA 722 1_555 ? ? ? ? ? ? ? 1.394 ? covale22 covale ? ? L NAG . O4 ? ? ? 1_555 M NAG . C1 ? ? A NAG 730 A NAG 731 1_555 ? ? ? ? ? ? ? 1.384 ? covale23 covale ? ? M NAG . O4 ? ? ? 1_555 N BMA . C1 ? ? A NAG 731 A BMA 732 1_555 ? ? ? ? ? ? ? 1.385 ? covale24 covale ? ? O NAG . O4 ? ? ? 1_555 P NAG . C1 ? ? A NAG 740 A NAG 741 1_555 ? ? ? ? ? ? ? 1.386 ? covale25 covale ? ? CA NAG . O4 ? ? ? 1_555 DA NAG . C1 ? ? B NAG 710 B NAG 711 1_555 ? ? ? ? ? ? ? 1.382 ? covale26 covale ? ? DA NAG . O4 ? ? ? 1_555 EA BMA . C1 ? ? B NAG 711 B BMA 712 1_555 ? ? ? ? ? ? ? 1.384 ? covale27 covale ? ? EA BMA . O6 ? ? ? 1_555 FA MAN . C1 ? ? B BMA 712 B MAN 714 1_555 ? ? ? ? ? ? ? 1.403 ? covale28 covale ? ? GA NAG . O4 ? ? ? 1_555 HA NAG . C1 ? ? B NAG 720 B NAG 721 1_555 ? ? ? ? ? ? ? 1.384 ? covale29 covale ? ? IA NAG . O4 ? ? ? 1_555 JA NAG . C1 ? ? B NAG 730 B NAG 731 1_555 ? ? ? ? ? ? ? 1.390 ? covale30 covale ? ? JA NAG . O4 ? ? ? 1_555 KA BMA . C1 ? ? B NAG 731 B BMA 732 1_555 ? ? ? ? ? ? ? 1.385 ? covale31 covale ? ? LA NAG . O4 ? ? ? 1_555 MA NAG . C1 ? ? B NAG 740 B NAG 741 1_555 ? ? ? ? ? ? ? 1.386 ? metalc1 metalc ? ? T CU . CU ? ? ? 1_555 A CYS 503 SG ? ? A CU 601 A CYS 503 1_555 ? ? ? ? ? ? ? 2.183 ? metalc2 metalc ? ? T CU . CU ? ? ? 1_555 A HIS 431 ND1 ? ? A CU 601 A HIS 431 1_555 ? ? ? ? ? ? ? 1.950 ? metalc3 metalc ? ? T CU . CU ? ? ? 1_555 A HIS 508 ND1 ? ? A CU 601 A HIS 508 1_555 ? ? ? ? ? ? ? 1.938 ? metalc4 metalc ? ? U CU . CU ? ? ? 1_555 A HIS 436 NE2 ? ? A CU 602 A HIS 436 1_555 ? ? ? ? ? ? ? 1.930 ? metalc5 metalc ? ? U CU . CU ? ? ? 1_555 A HIS 502 NE2 ? ? A CU 602 A HIS 502 1_555 ? ? ? ? ? ? ? 1.931 ? metalc6 metalc ? ? U CU . CU ? ? ? 1_555 A HIS 140 NE2 ? ? A CU 602 A HIS 140 1_555 ? ? ? ? ? ? ? 1.954 ? metalc7 metalc ? ? U CU . CU ? ? ? 1_555 AA OXY . O1 ? ? A CU 602 A OXY 620 1_555 ? ? ? ? ? ? ? 2.236 ? metalc8 metalc ? ? U CU . CU ? ? ? 1_555 AA OXY . O2 ? ? A CU 602 A OXY 620 1_555 ? ? ? ? ? ? ? 2.445 ? metalc9 metalc ? ? V CU . CU ? ? ? 1_555 A HIS 95 ND1 ? ? A CU 603 A HIS 95 1_555 ? ? ? ? ? ? ? 1.948 ? metalc10 metalc ? ? V CU . CU ? ? ? 1_555 A HIS 138 NE2 ? ? A CU 603 A HIS 138 1_555 ? ? ? ? ? ? ? 1.953 ? metalc11 metalc ? ? V CU . CU ? ? ? 1_555 A HIS 504 NE2 ? ? A CU 603 A HIS 504 1_555 ? ? ? ? ? ? ? 1.960 ? metalc12 metalc ? ? V CU . CU ? ? ? 1_555 AA OXY . O1 ? ? A CU 603 A OXY 620 1_555 ? ? ? ? ? ? ? 2.638 ? metalc13 metalc ? ? V CU . CU ? ? ? 1_555 AA OXY . O2 ? ? A CU 603 A OXY 620 1_555 ? ? ? ? ? ? ? 2.328 ? metalc14 metalc ? ? W CU . CU ? ? ? 1_555 A HIS 434 NE2 ? ? A CU 604 A HIS 434 1_555 ? ? ? ? ? ? ? 1.940 ? metalc15 metalc ? ? W CU . CU ? ? ? 1_555 A HIS 93 NE2 ? ? A CU 604 A HIS 93 1_555 ? ? ? ? ? ? ? 1.898 ? metalc16 metalc ? ? W CU . CU ? ? ? 1_555 X CL . CL ? ? A CU 604 A CL 610 1_555 ? ? ? ? ? ? ? 2.479 ? metalc17 metalc ? ? W CU . CU ? ? ? 1_555 AA OXY . O2 ? ? A CU 604 A OXY 620 1_555 ? ? ? ? ? ? ? 2.632 ? metalc18 metalc ? ? PA CU . CU ? ? ? 1_555 B HIS 508 ND1 ? ? B CU 601 B HIS 508 1_555 ? ? ? ? ? ? ? 1.946 ? metalc19 metalc ? ? PA CU . CU ? ? ? 1_555 B HIS 431 ND1 ? ? B CU 601 B HIS 431 1_555 ? ? ? ? ? ? ? 1.924 ? metalc20 metalc ? ? PA CU . CU ? ? ? 1_555 B CYS 503 SG ? ? B CU 601 B CYS 503 1_555 ? ? ? ? ? ? ? 2.180 ? metalc21 metalc ? ? QA CU . CU ? ? ? 1_555 B HIS 502 NE2 ? ? B CU 602 B HIS 502 1_555 ? ? ? ? ? ? ? 1.937 ? metalc22 metalc ? ? QA CU . CU ? ? ? 1_555 VA OXY . O2 ? ? B CU 602 B OXY 620 1_555 ? ? ? ? ? ? ? 2.511 ? metalc23 metalc ? ? QA CU . CU ? ? ? 1_555 VA OXY . O1 ? ? B CU 602 B OXY 620 1_555 ? ? ? ? ? ? ? 2.279 ? metalc24 metalc ? ? QA CU . CU ? ? ? 1_555 B HIS 436 NE2 ? ? B CU 602 B HIS 436 1_555 ? ? ? ? ? ? ? 1.918 ? metalc25 metalc ? ? QA CU . CU ? ? ? 1_555 B HIS 140 NE2 ? ? B CU 602 B HIS 140 1_555 ? ? ? ? ? ? ? 1.961 ? metalc26 metalc ? ? RA CU . CU ? ? ? 1_555 B HIS 95 ND1 ? ? B CU 603 B HIS 95 1_555 ? ? ? ? ? ? ? 1.938 ? metalc27 metalc ? ? RA CU . CU ? ? ? 1_555 VA OXY . O1 ? ? B CU 603 B OXY 620 1_555 ? ? ? ? ? ? ? 2.668 ? metalc28 metalc ? ? RA CU . CU ? ? ? 1_555 VA OXY . O2 ? ? B CU 603 B OXY 620 1_555 ? ? ? ? ? ? ? 2.290 ? metalc29 metalc ? ? RA CU . CU ? ? ? 1_555 B HIS 138 NE2 ? ? B CU 603 B HIS 138 1_555 ? ? ? ? ? ? ? 1.953 ? metalc30 metalc ? ? RA CU . CU ? ? ? 1_555 B HIS 504 NE2 ? ? B CU 603 B HIS 504 1_555 ? ? ? ? ? ? ? 1.962 ? metalc31 metalc ? ? SA CU . CU ? ? ? 1_555 VA OXY . O2 ? ? B CU 604 B OXY 620 1_555 ? ? ? ? ? ? ? 2.700 ? metalc32 metalc ? ? SA CU . CU ? ? ? 1_555 B HIS 93 NE2 ? ? B CU 604 B HIS 93 1_555 ? ? ? ? ? ? ? 1.899 ? metalc33 metalc ? ? SA CU . CU ? ? ? 1_555 TA CL . CL ? ? B CU 604 B CL 610 1_555 ? ? ? ? ? ? ? 2.575 ? metalc34 metalc ? ? SA CU . CU ? ? ? 1_555 B HIS 434 NE2 ? ? B CU 604 B HIS 434 1_555 ? ? ? ? ? ? ? 1.907 ? # 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 0.07 2 THR 368 B . ? THR 368 B PRO 369 B ? PRO 369 B 1 -0.43 # 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 84 ? THR A 76 ASN A 84 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 ? SER A 139 ? GLY A 133 SER A 139 C 4 ILE A 92 ? HIS A 95 ? ILE A 92 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 ALA A 215 ? LEU A 219 ? ALA A 215 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 ALA B 215 ? LEU B 219 ? ALA B 215 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 LEU B 265 ? LEU B 267 ? LEU B 265 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 LYS A 54 ? O LYS A 54 N TRP A 46 ? N TRP A 46 B 2 3 N PHE A 38 ? N PHE A 38 O ILE A 82 ? O ILE A 82 B 3 4 N VAL A 77 ? N VAL A 77 O TRP A 127 ? O TRP A 127 C 1 2 N ILE A 69 ? N ILE A 69 O GLN A 154 ? O GLN A 154 C 2 3 O ILE A 153 ? O ILE A 153 N SER A 135 ? N SER A 135 C 3 4 O HIS A 138 ? O HIS A 138 N HIS A 93 ? N HIS A 93 D 1 2 O LEU A 199 ? O LEU A 199 N THR A 173 ? N THR A 173 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 ALA A 252 ? N ALA A 252 O VAL A 255 ? O VAL A 255 E 1 2 N ALA A 215 ? N ALA A 215 O ILE A 309 ? O ILE A 309 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 LYS B 54 ? O LYS B 54 N TRP B 46 ? N TRP B 46 I 2 3 N PHE B 38 ? N PHE B 38 O ILE B 82 ? O ILE B 82 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 LEU B 227 ? N LEU B 227 O VAL B 275 ? O VAL B 275 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 ALA B 215 ? N ALA B 215 O ILE B 309 ? O ILE B 309 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 ALA B 490 ? O ALA B 490 N LEU B 441 ? N LEU B 441 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 ? ? ? ? 14 'BINDING SITE FOR RESIDUE NAG A 710' AC3 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE NAG A 711' AC4 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE BMA A 712' AC5 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE MAN A 713' AC6 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE MAN A 714' AC7 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE NAG A 720' AC8 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG A 721' AC9 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE BMA A 722' BC1 Software ? ? ? ? 11 'BINDING SITE FOR RESIDUE NAG A 730' BC2 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE NAG A 731' BC3 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE BMA A 732' BC4 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE NAG A 740' BC5 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG A 741' BC6 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE NAG A 750' BC7 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 760' BC8 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE NDG A 770' BC9 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG B 700' CC1 Software ? ? ? ? 13 'BINDING SITE FOR RESIDUE NAG B 710' CC2 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE NAG B 711' CC3 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE BMA B 712' CC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE MAN B 714' CC5 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE NAG B 720' CC6 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE NAG B 721' CC7 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE NAG B 730' CC8 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG B 731' CC9 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE BMA B 732' DC1 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE NAG B 740' DC2 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG B 741' DC3 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE NAG B 750' DC4 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE NAG B 760' DC5 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE CU A 601' DC6 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU A 602' DC7 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CU A 603' DC8 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE CU A 604' DC9 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CL A 610' EC1 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE SO4 A 800' EC2 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE SO4 A 801' EC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU B 601' EC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU B 602' EC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU B 603' EC6 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE CU B 604' EC7 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE CL B 610' EC8 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE SO4 B 800' EC9 Software ? ? ? ? 12 'BINDING SITE FOR RESIDUE OXY A 620' FC1 Software ? ? ? ? 12 'BINDING SITE FOR RESIDUE OXY B 620' # 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 ASN A 84 ? ASN A 84 . ? 1_555 ? 3 AC1 5 HOH WA . ? HOH A 1050 . ? 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 14 LYS A 56 ? LYS A 56 . ? 1_555 ? 7 AC2 14 MET A 58 ? MET A 58 . ? 1_555 ? 8 AC2 14 THR A 87 ? THR A 87 . ? 1_555 ? 9 AC2 14 ASN A 88 ? ASN A 88 . ? 1_555 ? 10 AC2 14 ASP A 181 ? ASP A 181 . ? 1_555 ? 11 AC2 14 ASN A 550 ? ASN A 550 . ? 1_555 ? 12 AC2 14 TYR A 552 ? TYR A 552 . ? 1_555 ? 13 AC2 14 NAG E . ? NAG A 711 . ? 1_555 ? 14 AC2 14 HOH WA . ? HOH A 832 . ? 1_555 ? 15 AC2 14 HOH WA . ? HOH A 884 . ? 1_555 ? 16 AC2 14 HOH WA . ? HOH A 905 . ? 1_555 ? 17 AC2 14 HOH WA . ? HOH A 926 . ? 1_555 ? 18 AC2 14 HOH WA . ? HOH A 1089 . ? 1_555 ? 19 AC2 14 HOH WA . ? HOH A 1337 . ? 1_555 ? 20 AC3 9 GLU A 55 ? GLU A 55 . ? 1_555 ? 21 AC3 9 LYS A 56 ? LYS A 56 . ? 1_555 ? 22 AC3 9 ALA A 179 ? ALA A 179 . ? 1_555 ? 23 AC3 9 ASP A 181 ? ASP A 181 . ? 1_555 ? 24 AC3 9 ASP A 182 ? ASP A 182 . ? 1_555 ? 25 AC3 9 NAG D . ? NAG A 710 . ? 1_555 ? 26 AC3 9 BMA F . ? BMA A 712 . ? 1_555 ? 27 AC3 9 HOH WA . ? HOH A 820 . ? 1_555 ? 28 AC3 9 HOH WA . ? HOH A 949 . ? 1_555 ? 29 AC4 3 NAG E . ? NAG A 711 . ? 1_555 ? 30 AC4 3 MAN G . ? MAN A 713 . ? 1_555 ? 31 AC4 3 MAN H . ? MAN A 714 . ? 1_555 ? 32 AC5 1 BMA F . ? BMA A 712 . ? 1_555 ? 33 AC6 4 GLU A 55 ? GLU A 55 . ? 1_555 ? 34 AC6 4 ASP A 182 ? ASP A 182 . ? 1_555 ? 35 AC6 4 BMA F . ? BMA A 712 . ? 1_555 ? 36 AC6 4 HOH WA . ? HOH A 949 . ? 1_555 ? 37 AC7 8 ASN A 216 ? ASN A 216 . ? 1_555 ? 38 AC7 8 THR A 218 ? THR A 218 . ? 1_555 ? 39 AC7 8 HIS A 311 ? HIS A 311 . ? 1_555 ? 40 AC7 8 GLY A 317 ? GLY A 317 . ? 1_555 ? 41 AC7 8 NAG J . ? NAG A 721 . ? 1_555 ? 42 AC7 8 HOH WA . ? HOH A 984 . ? 1_555 ? 43 AC7 8 HOH WA . ? HOH A 991 . ? 1_555 ? 44 AC7 8 HOH WA . ? HOH A 1396 . ? 1_555 ? 45 AC8 4 HIS A 311 ? HIS A 311 . ? 1_555 ? 46 AC8 4 GLY A 314 ? GLY A 314 . ? 1_555 ? 47 AC8 4 NAG I . ? NAG A 720 . ? 1_555 ? 48 AC8 4 BMA K . ? BMA A 722 . ? 1_555 ? 49 AC9 3 NAG J . ? NAG A 721 . ? 1_555 ? 50 AC9 3 HOH WA . ? HOH A 1327 . ? 1_555 ? 51 AC9 3 HOH WA . ? HOH A 1373 . ? 1_555 ? 52 BC1 11 TRP A 287 ? TRP A 287 . ? 1_555 ? 53 BC1 11 ASN A 289 ? ASN A 289 . ? 1_555 ? 54 BC1 11 THR A 291 ? THR A 291 . ? 1_555 ? 55 BC1 11 HIS A 305 ? HIS A 305 . ? 1_555 ? 56 BC1 11 ALA A 307 ? ALA A 307 . ? 1_555 ? 57 BC1 11 GLU A 323 ? GLU A 323 . ? 1_555 ? 58 BC1 11 THR A 325 ? THR A 325 . ? 1_555 ? 59 BC1 11 NAG M . ? NAG A 731 . ? 1_555 ? 60 BC1 11 HOH WA . ? HOH A 862 . ? 1_555 ? 61 BC1 11 HOH WA . ? HOH A 919 . ? 1_555 ? 62 BC1 11 HOH WA . ? HOH A 1223 . ? 1_555 ? 63 BC2 7 TYR A 214 ? TYR A 214 . ? 1_555 ? 64 BC2 7 TRP A 287 ? TRP A 287 . ? 1_555 ? 65 BC2 7 HIS A 305 ? HIS A 305 . ? 1_555 ? 66 BC2 7 GLU A 323 ? GLU A 323 . ? 1_555 ? 67 BC2 7 NAG L . ? NAG A 730 . ? 1_555 ? 68 BC2 7 BMA N . ? BMA A 732 . ? 1_555 ? 69 BC2 7 HOH WA . ? HOH A 1142 . ? 1_555 ? 70 BC3 1 NAG M . ? NAG A 731 . ? 1_555 ? 71 BC4 7 PRO A 355 ? PRO A 355 . ? 1_555 ? 72 BC4 7 ASP A 356 ? ASP A 356 . ? 1_555 ? 73 BC4 7 THR A 358 ? THR A 358 . ? 1_555 ? 74 BC4 7 ASN A 376 ? ASN A 376 . ? 1_555 ? 75 BC4 7 VAL A 406 ? VAL A 406 . ? 1_555 ? 76 BC4 7 NAG P . ? NAG A 741 . ? 1_555 ? 77 BC4 7 HOH WA . ? HOH A 1092 . ? 1_555 ? 78 BC5 1 NAG O . ? NAG A 740 . ? 1_555 ? 79 BC6 9 LYS A 386 ? LYS A 386 . ? 1_555 ? 80 BC6 9 TYR A 391 ? TYR A 391 . ? 1_555 ? 81 BC6 9 ASN A 396 ? ASN A 396 . ? 1_555 ? 82 BC6 9 HOH WA . ? HOH A 1132 . ? 1_555 ? 83 BC6 9 HOH WA . ? HOH A 1311 . ? 1_555 ? 84 BC6 9 HOH WA . ? HOH A 1323 . ? 1_555 ? 85 BC6 9 HOH WA . ? HOH A 1360 . ? 1_555 ? 86 BC6 9 GLN B 530 ? GLN B 530 . ? 2_555 ? 87 BC6 9 GLU B 533 ? GLU B 533 . ? 2_555 ? 88 BC7 5 LEU A 167 ? LEU A 167 . ? 1_555 ? 89 BC7 5 ASN A 201 ? ASN A 201 . ? 1_555 ? 90 BC7 5 VAL A 217 ? VAL A 217 . ? 1_555 ? 91 BC7 5 HOH WA . ? HOH A 836 . ? 1_555 ? 92 BC7 5 HOH WA . ? HOH A 1104 . ? 1_555 ? 93 BC8 9 ASN A 244 ? ASN A 244 . ? 1_555 ? 94 BC8 9 ALA A 282 ? ALA A 282 . ? 1_555 ? 95 BC8 9 ASP A 322 ? ASP A 322 . ? 1_555 ? 96 BC8 9 HOH WA . ? HOH A 1039 . ? 1_555 ? 97 BC8 9 HOH WA . ? HOH A 1120 . ? 1_555 ? 98 BC8 9 HOH WA . ? HOH A 1308 . ? 1_555 ? 99 BC8 9 HOH WA . ? HOH A 1387 . ? 1_555 ? 100 BC8 9 ARG B 281 ? ARG B 281 . ? 2_556 ? 101 BC8 9 HOH XA . ? HOH B 934 . ? 2_556 ? 102 BC9 4 GLU A 78 ? GLU A 78 . ? 3_545 ? 103 BC9 4 ARG A 126 ? ARG A 126 . ? 3_545 ? 104 BC9 4 ASN B 39 ? ASN B 39 . ? 1_555 ? 105 BC9 4 ASN B 84 ? ASN B 84 . ? 1_555 ? 106 CC1 13 LYS B 56 ? LYS B 56 . ? 1_555 ? 107 CC1 13 MET B 58 ? MET B 58 . ? 1_555 ? 108 CC1 13 THR B 87 ? THR B 87 . ? 1_555 ? 109 CC1 13 ASN B 88 ? ASN B 88 . ? 1_555 ? 110 CC1 13 ASP B 181 ? ASP B 181 . ? 1_555 ? 111 CC1 13 ASN B 550 ? ASN B 550 . ? 1_555 ? 112 CC1 13 TYR B 552 ? TYR B 552 . ? 1_555 ? 113 CC1 13 PRO B 553 ? PRO B 553 . ? 1_555 ? 114 CC1 13 NAG DA . ? NAG B 711 . ? 1_555 ? 115 CC1 13 HOH XA . ? HOH B 869 . ? 1_555 ? 116 CC1 13 HOH XA . ? HOH B 888 . ? 1_555 ? 117 CC1 13 HOH XA . ? HOH B 984 . ? 1_555 ? 118 CC1 13 HOH XA . ? HOH B 1167 . ? 1_555 ? 119 CC2 10 GLU B 55 ? GLU B 55 . ? 1_555 ? 120 CC2 10 ALA B 179 ? ALA B 179 . ? 1_555 ? 121 CC2 10 ASP B 181 ? ASP B 181 . ? 1_555 ? 122 CC2 10 ASP B 182 ? ASP B 182 . ? 1_555 ? 123 CC2 10 NAG CA . ? NAG B 710 . ? 1_555 ? 124 CC2 10 BMA EA . ? BMA B 712 . ? 1_555 ? 125 CC2 10 HOH XA . ? HOH B 853 . ? 1_555 ? 126 CC2 10 HOH XA . ? HOH B 965 . ? 1_555 ? 127 CC2 10 HOH XA . ? HOH B 1082 . ? 1_555 ? 128 CC2 10 HOH XA . ? HOH B 1298 . ? 1_555 ? 129 CC3 2 NAG DA . ? NAG B 711 . ? 1_555 ? 130 CC3 2 MAN FA . ? MAN B 714 . ? 1_555 ? 131 CC4 4 GLU B 55 ? GLU B 55 . ? 1_555 ? 132 CC4 4 ARG B 178 ? ARG B 178 . ? 1_555 ? 133 CC4 4 BMA EA . ? BMA B 712 . ? 1_555 ? 134 CC4 4 HOH XA . ? HOH B 965 . ? 1_555 ? 135 CC5 8 ASN B 216 ? ASN B 216 . ? 1_555 ? 136 CC5 8 THR B 218 ? THR B 218 . ? 1_555 ? 137 CC5 8 HIS B 311 ? HIS B 311 . ? 1_555 ? 138 CC5 8 GLY B 317 ? GLY B 317 . ? 1_555 ? 139 CC5 8 GLY B 318 ? GLY B 318 . ? 1_555 ? 140 CC5 8 NAG HA . ? NAG B 721 . ? 1_555 ? 141 CC5 8 HOH XA . ? HOH B 928 . ? 1_555 ? 142 CC5 8 HOH XA . ? HOH B 1103 . ? 1_555 ? 143 CC6 7 HIS B 311 ? HIS B 311 . ? 1_555 ? 144 CC6 7 GLY B 314 ? GLY B 314 . ? 1_555 ? 145 CC6 7 NAG GA . ? NAG B 720 . ? 1_555 ? 146 CC6 7 HOH XA . ? HOH B 943 . ? 1_555 ? 147 CC6 7 HOH XA . ? HOH B 1069 . ? 1_555 ? 148 CC6 7 HOH XA . ? HOH B 1150 . ? 1_555 ? 149 CC6 7 HOH XA . ? HOH B 1334 . ? 1_555 ? 150 CC7 10 TRP B 287 ? TRP B 287 . ? 1_555 ? 151 CC7 10 ASN B 289 ? ASN B 289 . ? 1_555 ? 152 CC7 10 THR B 291 ? THR B 291 . ? 1_555 ? 153 CC7 10 HIS B 305 ? HIS B 305 . ? 1_555 ? 154 CC7 10 ALA B 307 ? ALA B 307 . ? 1_555 ? 155 CC7 10 GLU B 323 ? GLU B 323 . ? 1_555 ? 156 CC7 10 THR B 325 ? THR B 325 . ? 1_555 ? 157 CC7 10 NAG JA . ? NAG B 731 . ? 1_555 ? 158 CC7 10 HOH XA . ? HOH B 913 . ? 1_555 ? 159 CC7 10 HOH XA . ? HOH B 1174 . ? 1_555 ? 160 CC8 6 TYR B 214 ? TYR B 214 . ? 1_555 ? 161 CC8 6 TRP B 287 ? TRP B 287 . ? 1_555 ? 162 CC8 6 HIS B 305 ? HIS B 305 . ? 1_555 ? 163 CC8 6 GLU B 323 ? GLU B 323 . ? 1_555 ? 164 CC8 6 NAG IA . ? NAG B 730 . ? 1_555 ? 165 CC8 6 BMA KA . ? BMA B 732 . ? 1_555 ? 166 CC9 3 NAG JA . ? NAG B 731 . ? 1_555 ? 167 CC9 3 HOH XA . ? HOH B 1148 . ? 1_555 ? 168 CC9 3 HOH XA . ? HOH B 1277 . ? 1_555 ? 169 DC1 7 PRO B 355 ? PRO B 355 . ? 1_555 ? 170 DC1 7 ASP B 356 ? ASP B 356 . ? 1_555 ? 171 DC1 7 THR B 358 ? THR B 358 . ? 1_555 ? 172 DC1 7 LEU B 359 ? LEU B 359 . ? 1_555 ? 173 DC1 7 ASN B 376 ? ASN B 376 . ? 1_555 ? 174 DC1 7 NAG MA . ? NAG B 741 . ? 1_555 ? 175 DC1 7 HOH XA . ? HOH B 1119 . ? 1_555 ? 176 DC2 2 ASP B 356 ? ASP B 356 . ? 1_555 ? 177 DC2 2 NAG LA . ? NAG B 740 . ? 1_555 ? 178 DC3 9 ASP A 379 ? ASP A 379 . ? 2_555 ? 179 DC3 9 ASN A 381 ? ASN A 381 . ? 2_555 ? 180 DC3 9 HOH WA . ? HOH A 1284 . ? 2_555 ? 181 DC3 9 HOH WA . ? HOH A 1325 . ? 2_555 ? 182 DC3 9 LYS B 386 ? LYS B 386 . ? 1_555 ? 183 DC3 9 TYR B 391 ? TYR B 391 . ? 1_555 ? 184 DC3 9 ASN B 396 ? ASN B 396 . ? 1_555 ? 185 DC3 9 HOH XA . ? HOH B 1217 . ? 1_555 ? 186 DC3 9 HOH XA . ? HOH B 1348 . ? 1_555 ? 187 DC4 8 LEU B 167 ? LEU B 167 . ? 1_555 ? 188 DC4 8 ASN B 201 ? ASN B 201 . ? 1_555 ? 189 DC4 8 VAL B 217 ? VAL B 217 . ? 1_555 ? 190 DC4 8 HOH XA . ? HOH B 985 . ? 1_555 ? 191 DC4 8 HOH XA . ? HOH B 987 . ? 1_555 ? 192 DC4 8 HOH XA . ? HOH B 1184 . ? 1_555 ? 193 DC4 8 HOH XA . ? HOH B 1232 . ? 1_555 ? 194 DC4 8 HOH XA . ? HOH B 1276 . ? 1_555 ? 195 DC5 3 HIS A 431 ? HIS A 431 . ? 1_555 ? 196 DC5 3 CYS A 503 ? CYS A 503 . ? 1_555 ? 197 DC5 3 HIS A 508 ? HIS A 508 . ? 1_555 ? 198 DC6 4 HIS A 140 ? HIS A 140 . ? 1_555 ? 199 DC6 4 HIS A 436 ? HIS A 436 . ? 1_555 ? 200 DC6 4 HIS A 502 ? HIS A 502 . ? 1_555 ? 201 DC6 4 OXY AA . ? OXY A 620 . ? 1_555 ? 202 DC7 5 HIS A 95 ? HIS A 95 . ? 1_555 ? 203 DC7 5 TRP A 136 ? TRP A 136 . ? 1_555 ? 204 DC7 5 HIS A 138 ? HIS A 138 . ? 1_555 ? 205 DC7 5 HIS A 504 ? HIS A 504 . ? 1_555 ? 206 DC7 5 OXY AA . ? OXY A 620 . ? 1_555 ? 207 DC8 6 HIS A 93 ? HIS A 93 . ? 1_555 ? 208 DC8 6 HIS A 95 ? HIS A 95 . ? 1_555 ? 209 DC8 6 HIS A 434 ? HIS A 434 . ? 1_555 ? 210 DC8 6 HIS A 436 ? HIS A 436 . ? 1_555 ? 211 DC8 6 CL X . ? CL A 610 . ? 1_555 ? 212 DC8 6 OXY AA . ? OXY A 620 . ? 1_555 ? 213 DC9 5 HIS A 93 ? HIS A 93 . ? 1_555 ? 214 DC9 5 HIS A 95 ? HIS A 95 . ? 1_555 ? 215 DC9 5 GLY A 96 ? GLY A 96 . ? 1_555 ? 216 DC9 5 HIS A 434 ? HIS A 434 . ? 1_555 ? 217 DC9 5 CU W . ? CU A 604 . ? 1_555 ? 218 EC1 3 ARG A 128 ? ARG A 128 . ? 1_555 ? 219 EC1 3 ARG A 130 ? ARG A 130 . ? 1_555 ? 220 EC1 3 ARG B 492 ? ARG B 492 . ? 3_445 ? 221 EC2 6 ARG A 520 ? ARG A 520 . ? 1_555 ? 222 EC2 6 ARG A 527 ? ARG A 527 . ? 1_555 ? 223 EC2 6 ARG B 520 ? ARG B 520 . ? 3_445 ? 224 EC2 6 ARG B 527 ? ARG B 527 . ? 3_445 ? 225 EC2 6 HOH XA . ? HOH B 825 . ? 3_445 ? 226 EC2 6 HOH XA . ? HOH B 981 . ? 3_445 ? 227 EC3 4 HIS B 431 ? HIS B 431 . ? 1_555 ? 228 EC3 4 CYS B 503 ? CYS B 503 . ? 1_555 ? 229 EC3 4 HIS B 508 ? HIS B 508 . ? 1_555 ? 230 EC3 4 LEU B 513 ? LEU B 513 . ? 1_555 ? 231 EC4 4 HIS B 140 ? HIS B 140 . ? 1_555 ? 232 EC4 4 HIS B 436 ? HIS B 436 . ? 1_555 ? 233 EC4 4 HIS B 502 ? HIS B 502 . ? 1_555 ? 234 EC4 4 OXY VA . ? OXY B 620 . ? 1_555 ? 235 EC5 4 HIS B 95 ? HIS B 95 . ? 1_555 ? 236 EC5 4 HIS B 138 ? HIS B 138 . ? 1_555 ? 237 EC5 4 HIS B 504 ? HIS B 504 . ? 1_555 ? 238 EC5 4 OXY VA . ? OXY B 620 . ? 1_555 ? 239 EC6 6 HIS B 93 ? HIS B 93 . ? 1_555 ? 240 EC6 6 HIS B 95 ? HIS B 95 . ? 1_555 ? 241 EC6 6 HIS B 434 ? HIS B 434 . ? 1_555 ? 242 EC6 6 HIS B 436 ? HIS B 436 . ? 1_555 ? 243 EC6 6 CL TA . ? CL B 610 . ? 1_555 ? 244 EC6 6 OXY VA . ? OXY B 620 . ? 1_555 ? 245 EC7 6 HIS B 93 ? HIS B 93 . ? 1_555 ? 246 EC7 6 HIS B 95 ? HIS B 95 . ? 1_555 ? 247 EC7 6 GLY B 96 ? GLY B 96 . ? 1_555 ? 248 EC7 6 HIS B 434 ? HIS B 434 . ? 1_555 ? 249 EC7 6 CU SA . ? CU B 604 . ? 1_555 ? 250 EC7 6 HOH XA . ? HOH B 831 . ? 1_555 ? 251 EC8 5 ARG A 492 ? ARG A 492 . ? 3_555 ? 252 EC8 5 HOH WA . ? HOH A 1345 . ? 3_555 ? 253 EC8 5 ARG B 128 ? ARG B 128 . ? 1_555 ? 254 EC8 5 ARG B 130 ? ARG B 130 . ? 1_555 ? 255 EC8 5 HOH XA . ? HOH B 1201 . ? 1_555 ? 256 EC9 12 HIS A 93 ? HIS A 93 . ? 1_555 ? 257 EC9 12 HIS A 95 ? HIS A 95 . ? 1_555 ? 258 EC9 12 HIS A 138 ? HIS A 138 . ? 1_555 ? 259 EC9 12 HIS A 140 ? HIS A 140 . ? 1_555 ? 260 EC9 12 HIS A 434 ? HIS A 434 . ? 1_555 ? 261 EC9 12 HIS A 436 ? HIS A 436 . ? 1_555 ? 262 EC9 12 HIS A 502 ? HIS A 502 . ? 1_555 ? 263 EC9 12 HIS A 504 ? HIS A 504 . ? 1_555 ? 264 EC9 12 CU U . ? CU A 602 . ? 1_555 ? 265 EC9 12 CU V . ? CU A 603 . ? 1_555 ? 266 EC9 12 CU W . ? CU A 604 . ? 1_555 ? 267 EC9 12 HOH WA . ? HOH A 1053 . ? 1_555 ? 268 FC1 12 HIS B 93 ? HIS B 93 . ? 1_555 ? 269 FC1 12 HIS B 95 ? HIS B 95 . ? 1_555 ? 270 FC1 12 HIS B 138 ? HIS B 138 . ? 1_555 ? 271 FC1 12 HIS B 140 ? HIS B 140 . ? 1_555 ? 272 FC1 12 HIS B 434 ? HIS B 434 . ? 1_555 ? 273 FC1 12 HIS B 436 ? HIS B 436 . ? 1_555 ? 274 FC1 12 HIS B 502 ? HIS B 502 . ? 1_555 ? 275 FC1 12 HIS B 504 ? HIS B 504 . ? 1_555 ? 276 FC1 12 CU QA . ? CU B 602 . ? 1_555 ? 277 FC1 12 CU RA . ? CU B 603 . ? 1_555 ? 278 FC1 12 CU SA . ? CU B 604 . ? 1_555 ? 279 FC1 12 HOH XA . ? HOH B 970 . ? 1_555 ? # _atom_sites.entry_id 2IH8 _atom_sites.fract_transf_matrix[1][1] 0.005778 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.000644 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.016179 _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] 0.008120 _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 . GLU A 1 1 ? -54.964 29.636 40.598 1.00 41.06 ? 1 GLU A N 1 ATOM 2 C CA . GLU A 1 1 ? -55.207 30.150 41.977 1.00 43.72 ? 1 GLU A CA 1 ATOM 3 C C . GLU A 1 1 ? -55.038 29.015 43.007 1.00 42.42 ? 1 GLU A C 1 ATOM 4 O O . GLU A 1 1 ? -55.677 27.962 42.881 1.00 41.89 ? 1 GLU A O 1 ATOM 5 C CB . GLU A 1 1 ? -56.617 30.767 42.063 1.00 45.71 ? 1 GLU A CB 1 ATOM 6 C CG . GLU A 1 1 ? -56.890 31.669 43.279 1.00 49.85 ? 1 GLU A CG 1 ATOM 7 C CD . GLU A 1 1 ? -56.031 32.929 43.308 1.00 52.15 ? 1 GLU A CD 1 ATOM 8 O OE1 . GLU A 1 1 ? -56.037 33.691 42.315 1.00 54.09 ? 1 GLU A OE1 1 ATOM 9 O OE2 . GLU A 1 1 ? -55.351 33.155 44.332 1.00 53.49 ? 1 GLU A OE2 1 ATOM 10 N N . PRO A 1 2 ? -54.142 29.199 44.011 1.00 41.30 ? 2 PRO A N 1 ATOM 11 C CA . PRO A 1 2 ? -53.898 28.186 45.052 1.00 39.90 ? 2 PRO A CA 1 ATOM 12 C C . PRO A 1 2 ? -54.948 28.129 46.167 1.00 38.52 ? 2 PRO A C 1 ATOM 13 O O . PRO A 1 2 ? -55.638 29.120 46.426 1.00 38.90 ? 2 PRO A O 1 ATOM 14 C CB . PRO A 1 2 ? -52.545 28.603 45.617 1.00 39.50 ? 2 PRO A CB 1 ATOM 15 C CG . PRO A 1 2 ? -52.566 30.092 45.499 1.00 40.01 ? 2 PRO A CG 1 ATOM 16 C CD . PRO A 1 2 ? -53.166 30.306 44.130 1.00 40.72 ? 2 PRO A CD 1 ATOM 17 N N . THR A 1 3 ? -55.071 26.958 46.801 1.00 36.58 ? 3 THR A N 1 ATOM 18 C CA . THR A 1 3 ? -56.007 26.745 47.915 1.00 34.36 ? 3 THR A CA 1 ATOM 19 C C . THR A 1 3 ? -55.355 26.036 49.114 1.00 32.52 ? 3 THR A C 1 ATOM 20 O O . THR A 1 3 ? -55.908 26.057 50.218 1.00 33.28 ? 3 THR A O 1 ATOM 21 C CB . THR A 1 3 ? -57.282 25.930 47.506 1.00 34.08 ? 3 THR A CB 1 ATOM 22 O OG1 . THR A 1 3 ? -56.900 24.683 46.916 1.00 33.37 ? 3 THR A OG1 1 ATOM 23 C CG2 . THR A 1 3 ? -58.179 26.716 46.545 1.00 33.57 ? 3 THR A CG2 1 ATOM 24 N N . CYS A 1 4 ? -54.180 25.436 48.904 1.00 29.22 ? 4 CYS A N 1 ATOM 25 C CA . CYS A 1 4 ? -53.479 24.704 49.969 1.00 25.94 ? 4 CYS A CA 1 ATOM 26 C C . CYS A 1 4 ? -51.952 24.868 49.996 1.00 24.14 ? 4 CYS A C 1 ATOM 27 O O . CYS A 1 4 ? -51.252 24.094 50.663 1.00 23.10 ? 4 CYS A O 1 ATOM 28 C CB . CYS A 1 4 ? -53.837 23.213 49.891 1.00 24.69 ? 4 CYS A CB 1 ATOM 29 S SG . CYS A 1 4 ? -53.388 22.457 48.299 1.00 23.27 ? 4 CYS A SG 1 ATOM 30 N N . ASN A 1 5 ? -51.442 25.868 49.278 1.00 22.21 ? 5 ASN A N 1 ATOM 31 C CA . ASN A 1 5 ? -50.001 26.139 49.230 1.00 20.95 ? 5 ASN A CA 1 ATOM 32 C C . ASN A 1 5 ? -49.628 27.037 50.410 1.00 20.75 ? 5 ASN A C 1 ATOM 33 O O . ASN A 1 5 ? -49.915 28.241 50.414 1.00 21.77 ? 5 ASN A O 1 ATOM 34 C CB . ASN A 1 5 ? -49.621 26.792 47.895 1.00 18.69 ? 5 ASN A CB 1 ATOM 35 C CG . ASN A 1 5 ? -48.115 26.855 47.674 1.00 18.45 ? 5 ASN A CG 1 ATOM 36 O OD1 . ASN A 1 5 ? -47.509 27.917 47.788 1.00 18.75 ? 5 ASN A OD1 1 ATOM 37 N ND2 . ASN A 1 5 ? -47.511 25.717 47.347 1.00 15.77 ? 5 ASN A ND2 1 ATOM 38 N N . THR A 1 6 ? -49.008 26.415 51.411 1.00 20.72 ? 6 THR A N 1 ATOM 39 C CA . THR A 1 6 ? -48.595 27.072 52.658 1.00 20.94 ? 6 THR A CA 1 ATOM 40 C C . THR A 1 6 ? -47.086 26.864 52.885 1.00 19.82 ? 6 THR A C 1 ATOM 41 O O . THR A 1 6 ? -46.496 26.000 52.233 1.00 16.48 ? 6 THR A O 1 ATOM 42 C CB . THR A 1 6 ? -49.351 26.429 53.869 1.00 20.69 ? 6 THR A CB 1 ATOM 43 O OG1 . THR A 1 6 ? -49.070 25.024 53.917 1.00 21.81 ? 6 THR A OG1 1 ATOM 44 C CG2 . THR A 1 6 ? -50.859 26.668 53.785 1.00 21.81 ? 6 THR A CG2 1 ATOM 45 N N . PRO A 1 7 ? -46.436 27.666 53.777 1.00 19.63 ? 7 PRO A N 1 ATOM 46 C CA . PRO A 1 7 ? -44.999 27.488 54.034 1.00 21.00 ? 7 PRO A CA 1 ATOM 47 C C . PRO A 1 7 ? -44.534 26.084 54.432 1.00 22.47 ? 7 PRO A C 1 ATOM 48 O O . PRO A 1 7 ? -43.471 25.650 54.002 1.00 22.33 ? 7 PRO A O 1 ATOM 49 C CB . PRO A 1 7 ? -44.736 28.497 55.142 1.00 21.31 ? 7 PRO A CB 1 ATOM 50 C CG . PRO A 1 7 ? -45.545 29.640 54.691 1.00 19.18 ? 7 PRO A CG 1 ATOM 51 C CD . PRO A 1 7 ? -46.859 28.980 54.318 1.00 19.60 ? 7 PRO A CD 1 ATOM 52 N N . SER A 1 8 ? -45.364 25.367 55.190 1.00 23.31 ? 8 SER A N 1 ATOM 53 C CA . SER A 1 8 ? -45.048 24.007 55.643 1.00 23.97 ? 8 SER A CA 1 ATOM 54 C C . SER A 1 8 ? -45.462 22.917 54.645 1.00 23.87 ? 8 SER A C 1 ATOM 55 O O . SER A 1 8 ? -44.963 21.789 54.705 1.00 23.74 ? 8 SER A O 1 ATOM 56 C CB . SER A 1 8 ? -45.674 23.744 57.017 1.00 23.56 ? 8 SER A CB 1 ATOM 57 O OG . SER A 1 8 ? -47.068 23.985 57.000 1.00 24.57 ? 8 SER A OG 1 ATOM 58 N N . ASN A 1 9 ? -46.366 23.264 53.730 1.00 23.28 ? 9 ASN A N 1 ATOM 59 C CA . ASN A 1 9 ? -46.840 22.333 52.711 1.00 23.16 ? 9 ASN A CA 1 ATOM 60 C C . ASN A 1 9 ? -46.836 23.034 51.347 1.00 22.63 ? 9 ASN A C 1 ATOM 61 O O . ASN A 1 9 ? -47.870 23.524 50.871 1.00 21.87 ? 9 ASN A O 1 ATOM 62 C CB . ASN A 1 9 ? -48.244 21.801 53.075 1.00 24.63 ? 9 ASN A CB 1 ATOM 63 C CG . ASN A 1 9 ? -48.674 20.595 52.229 1.00 26.06 ? 9 ASN A CG 1 ATOM 64 O OD1 . ASN A 1 9 ? -47.904 20.056 51.428 1.00 27.37 ? 9 ASN A OD1 1 ATOM 65 N ND2 . ASN A 1 9 ? -49.924 20.177 52.406 1.00 26.44 ? 9 ASN A ND2 1 ATOM 66 N N . ARG A 1 10 ? -45.647 23.121 50.749 1.00 20.86 ? 10 ARG A N 1 ATOM 67 C CA . ARG A 1 10 ? -45.485 23.740 49.434 1.00 19.11 ? 10 ARG A CA 1 ATOM 68 C C . ARG A 1 10 ? -45.754 22.730 48.329 1.00 17.93 ? 10 ARG A C 1 ATOM 69 O O . ARG A 1 10 ? -45.890 23.101 47.168 1.00 18.34 ? 10 ARG A O 1 ATOM 70 C CB . ARG A 1 10 ? -44.088 24.345 49.267 1.00 17.29 ? 10 ARG A CB 1 ATOM 71 C CG . ARG A 1 10 ? -43.828 25.578 50.115 1.00 16.05 ? 10 ARG A CG 1 ATOM 72 C CD . ARG A 1 10 ? -44.639 26.781 49.689 1.00 16.73 ? 10 ARG A CD 1 ATOM 73 N NE . ARG A 1 10 ? -44.232 27.965 50.441 1.00 16.88 ? 10 ARG A NE 1 ATOM 74 C CZ . ARG A 1 10 ? -44.877 29.129 50.446 1.00 17.69 ? 10 ARG A CZ 1 ATOM 75 N NH1 . ARG A 1 10 ? -45.986 29.298 49.736 1.00 19.09 ? 10 ARG A NH1 1 ATOM 76 N NH2 . ARG A 1 10 ? -44.396 30.134 51.163 1.00 18.48 ? 10 ARG A NH2 1 ATOM 77 N N . ALA A 1 11 ? -45.873 21.460 48.716 1.00 16.48 ? 11 ALA A N 1 ATOM 78 C CA . ALA A 1 11 ? -46.151 20.360 47.798 1.00 16.54 ? 11 ALA A CA 1 ATOM 79 C C . ALA A 1 11 ? -47.576 20.416 47.246 1.00 17.69 ? 11 ALA A C 1 ATOM 80 O O . ALA A 1 11 ? -47.827 20.001 46.113 1.00 16.77 ? 11 ALA A O 1 ATOM 81 C CB . ALA A 1 11 ? -45.910 19.025 48.495 1.00 16.73 ? 11 ALA A CB 1 ATOM 82 N N . CYS A 1 12 ? -48.480 20.989 48.038 1.00 17.29 ? 12 CYS A N 1 ATOM 83 C CA . CYS A 1 12 ? -49.893 21.121 47.689 1.00 19.07 ? 12 CYS A CA 1 ATOM 84 C C . CYS A 1 12 ? -50.157 22.412 46.917 1.00 18.86 ? 12 CYS A C 1 ATOM 85 O O . CYS A 1 12 ? -49.488 23.421 47.143 1.00 18.54 ? 12 CYS A O 1 ATOM 86 C CB . CYS A 1 12 ? -50.731 21.114 48.976 1.00 20.39 ? 12 CYS A CB 1 ATOM 87 S SG . CYS A 1 12 ? -52.498 20.701 48.789 1.00 23.71 ? 12 CYS A SG 1 ATOM 88 N N . TRP A 1 13 ? -51.110 22.366 45.986 1.00 18.74 ? 13 TRP A N 1 ATOM 89 C CA . TRP A 1 13 ? -51.477 23.554 45.215 1.00 19.03 ? 13 TRP A CA 1 ATOM 90 C C . TRP A 1 13 ? -52.985 23.771 45.249 1.00 19.41 ? 13 TRP A C 1 ATOM 91 O O . TRP A 1 13 ? -53.460 24.747 45.828 1.00 19.62 ? 13 TRP A O 1 ATOM 92 C CB . TRP A 1 13 ? -50.948 23.487 43.771 1.00 17.79 ? 13 TRP A CB 1 ATOM 93 C CG . TRP A 1 13 ? -51.120 24.782 42.984 1.00 16.22 ? 13 TRP A CG 1 ATOM 94 C CD1 . TRP A 1 13 ? -51.928 24.975 41.900 1.00 16.98 ? 13 TRP A CD1 1 ATOM 95 C CD2 . TRP A 1 13 ? -50.498 26.052 43.250 1.00 17.13 ? 13 TRP A CD2 1 ATOM 96 N NE1 . TRP A 1 13 ? -51.855 26.278 41.472 1.00 16.43 ? 13 TRP A NE1 1 ATOM 97 C CE2 . TRP A 1 13 ? -50.987 26.966 42.277 1.00 16.45 ? 13 TRP A CE2 1 ATOM 98 C CE3 . TRP A 1 13 ? -49.576 26.515 44.217 1.00 14.86 ? 13 TRP A CE3 1 ATOM 99 C CZ2 . TRP A 1 13 ? -50.585 28.323 42.236 1.00 17.96 ? 13 TRP A CZ2 1 ATOM 100 C CZ3 . TRP A 1 13 ? -49.171 27.879 44.182 1.00 16.32 ? 13 TRP A CZ3 1 ATOM 101 C CH2 . TRP A 1 13 ? -49.681 28.761 43.193 1.00 16.85 ? 13 TRP A CH2 1 ATOM 102 N N . SER A 1 14 ? -53.723 22.860 44.621 1.00 20.45 ? 14 SER A N 1 ATOM 103 C CA . SER A 1 14 ? -55.184 22.906 44.584 1.00 21.49 ? 14 SER A CA 1 ATOM 104 C C . SER A 1 14 ? -55.694 21.477 44.457 1.00 22.35 ? 14 SER A C 1 ATOM 105 O O . SER A 1 14 ? -54.892 20.539 44.408 1.00 22.06 ? 14 SER A O 1 ATOM 106 C CB . SER A 1 14 ? -55.690 23.789 43.427 1.00 20.90 ? 14 SER A CB 1 ATOM 107 O OG . SER A 1 14 ? -55.251 23.319 42.164 1.00 21.81 ? 14 SER A OG 1 ATOM 108 N N . ASP A 1 15 ? -57.018 21.309 44.408 1.00 23.86 ? 15 ASP A N 1 ATOM 109 C CA . ASP A 1 15 ? -57.636 19.986 44.286 1.00 25.19 ? 15 ASP A CA 1 ATOM 110 C C . ASP A 1 15 ? -57.276 19.309 42.957 1.00 23.55 ? 15 ASP A C 1 ATOM 111 O O . ASP A 1 15 ? -57.598 19.814 41.880 1.00 23.24 ? 15 ASP A O 1 ATOM 112 C CB . ASP A 1 15 ? -59.157 20.091 44.448 1.00 30.29 ? 15 ASP A CB 1 ATOM 113 C CG . ASP A 1 15 ? -59.801 18.757 44.788 1.00 36.31 ? 15 ASP A CG 1 ATOM 114 O OD1 . ASP A 1 15 ? -60.336 18.102 43.867 1.00 39.85 ? 15 ASP A OD1 1 ATOM 115 O OD2 . ASP A 1 15 ? -59.760 18.361 45.975 1.00 39.56 ? 15 ASP A OD2 1 ATOM 116 N N . GLY A 1 16 ? -56.541 18.203 43.066 1.00 23.16 ? 16 GLY A N 1 ATOM 117 C CA . GLY A 1 16 ? -56.108 17.442 41.905 1.00 22.71 ? 16 GLY A CA 1 ATOM 118 C C . GLY A 1 16 ? -54.784 17.895 41.328 1.00 22.03 ? 16 GLY A C 1 ATOM 119 O O . GLY A 1 16 ? -54.305 17.336 40.338 1.00 22.48 ? 16 GLY A O 1 ATOM 120 N N . PHE A 1 17 ? -54.211 18.939 41.928 1.00 20.47 ? 17 PHE A N 1 ATOM 121 C CA . PHE A 1 17 ? -52.948 19.508 41.470 1.00 18.38 ? 17 PHE A CA 1 ATOM 122 C C . PHE A 1 17 ? -51.943 19.704 42.592 1.00 18.18 ? 17 PHE A C 1 ATOM 123 O O . PHE A 1 17 ? -52.193 20.443 43.544 1.00 18.30 ? 17 PHE A O 1 ATOM 124 C CB . PHE A 1 17 ? -53.198 20.832 40.730 1.00 18.40 ? 17 PHE A CB 1 ATOM 125 C CG . PHE A 1 17 ? -54.060 20.685 39.506 1.00 18.18 ? 17 PHE A CG 1 ATOM 126 C CD1 . PHE A 1 17 ? -53.535 20.126 38.325 1.00 18.71 ? 17 PHE A CD1 1 ATOM 127 C CD2 . PHE A 1 17 ? -55.432 21.006 39.560 1.00 16.78 ? 17 PHE A CD2 1 ATOM 128 C CE1 . PHE A 1 17 ? -54.370 19.874 37.206 1.00 17.87 ? 17 PHE A CE1 1 ATOM 129 C CE2 . PHE A 1 17 ? -56.283 20.762 38.453 1.00 18.58 ? 17 PHE A CE2 1 ATOM 130 C CZ . PHE A 1 17 ? -55.749 20.190 37.272 1.00 18.86 ? 17 PHE A CZ 1 ATOM 131 N N . ASP A 1 18 ? -50.829 18.982 42.493 1.00 18.05 ? 18 ASP A N 1 ATOM 132 C CA . ASP A 1 18 ? -49.741 19.054 43.465 1.00 17.58 ? 18 ASP A CA 1 ATOM 133 C C . ASP A 1 18 ? -48.379 18.856 42.779 1.00 17.20 ? 18 ASP A C 1 ATOM 134 O O . ASP A 1 18 ? -48.304 18.856 41.550 1.00 15.54 ? 18 ASP A O 1 ATOM 135 C CB . ASP A 1 18 ? -49.965 18.078 44.653 1.00 18.69 ? 18 ASP A CB 1 ATOM 136 C CG . ASP A 1 18 ? -50.136 16.617 44.233 1.00 18.93 ? 18 ASP A CG 1 ATOM 137 O OD1 . ASP A 1 18 ? -49.432 16.139 43.322 1.00 17.89 ? 18 ASP A OD1 1 ATOM 138 O OD2 . ASP A 1 18 ? -50.962 15.924 44.865 1.00 20.83 ? 18 ASP A OD2 1 ATOM 139 N N . ILE A 1 19 ? -47.316 18.681 43.567 1.00 16.15 ? 19 ILE A N 1 ATOM 140 C CA . ILE A 1 19 ? -45.956 18.493 43.042 1.00 16.09 ? 19 ILE A CA 1 ATOM 141 C C . ILE A 1 19 ? -45.747 17.189 42.251 1.00 16.07 ? 19 ILE A C 1 ATOM 142 O O . ILE A 1 19 ? -44.864 17.104 41.396 1.00 16.42 ? 19 ILE A O 1 ATOM 143 C CB . ILE A 1 19 ? -44.889 18.643 44.194 1.00 14.38 ? 19 ILE A CB 1 ATOM 144 C CG1 . ILE A 1 19 ? -43.479 18.859 43.624 1.00 14.01 ? 19 ILE A CG1 1 ATOM 145 C CG2 . ILE A 1 19 ? -44.913 17.430 45.140 1.00 13.98 ? 19 ILE A CG2 1 ATOM 146 C CD1 . ILE A 1 19 ? -43.335 20.084 42.753 1.00 12.81 ? 19 ILE A CD1 1 ATOM 147 N N . ASN A 1 20 ? -46.610 16.212 42.510 1.00 17.50 ? 20 ASN A N 1 ATOM 148 C CA . ASN A 1 20 ? -46.540 14.909 41.861 1.00 17.59 ? 20 ASN A CA 1 ATOM 149 C C . ASN A 1 20 ? -47.386 14.804 40.592 1.00 16.73 ? 20 ASN A C 1 ATOM 150 O O . ASN A 1 20 ? -47.276 13.823 39.848 1.00 16.29 ? 20 ASN A O 1 ATOM 151 C CB . ASN A 1 20 ? -46.929 13.823 42.860 1.00 19.73 ? 20 ASN A CB 1 ATOM 152 C CG . ASN A 1 20 ? -45.998 13.768 44.057 1.00 21.94 ? 20 ASN A CG 1 ATOM 153 O OD1 . ASN A 1 20 ? -46.434 13.908 45.199 1.00 23.93 ? 20 ASN A OD1 1 ATOM 154 N ND2 . ASN A 1 20 ? -44.711 13.569 43.799 1.00 19.13 ? 20 ASN A ND2 1 ATOM 155 N N . THR A 1 21 ? -48.220 15.818 40.347 1.00 16.06 ? 21 THR A N 1 ATOM 156 C CA . THR A 1 21 ? -49.074 15.871 39.152 1.00 15.08 ? 21 THR A CA 1 ATOM 157 C C . THR A 1 21 ? -48.174 16.023 37.927 1.00 13.94 ? 21 THR A C 1 ATOM 158 O O . THR A 1 21 ? -47.205 16.784 37.954 1.00 11.99 ? 21 THR A O 1 ATOM 159 C CB . THR A 1 21 ? -50.041 17.095 39.188 1.00 14.36 ? 21 THR A CB 1 ATOM 160 O OG1 . THR A 1 21 ? -50.868 17.021 40.349 1.00 16.14 ? 21 THR A OG1 1 ATOM 161 C CG2 . THR A 1 21 ? -50.941 17.152 37.949 1.00 14.34 ? 21 THR A CG2 1 ATOM 162 N N . ASP A 1 22 ? -48.476 15.257 36.882 1.00 14.86 ? 22 ASP A N 1 ATOM 163 C CA . ASP A 1 22 ? -47.727 15.329 35.633 1.00 15.40 ? 22 ASP A CA 1 ATOM 164 C C . ASP A 1 22 ? -48.245 16.585 34.912 1.00 14.77 ? 22 ASP A C 1 ATOM 165 O O . ASP A 1 22 ? -49.280 16.555 34.245 1.00 14.88 ? 22 ASP A O 1 ATOM 166 C CB . ASP A 1 22 ? -47.953 14.055 34.801 1.00 15.18 ? 22 ASP A CB 1 ATOM 167 C CG . ASP A 1 22 ? -46.993 13.934 33.616 1.00 16.51 ? 22 ASP A CG 1 ATOM 168 O OD1 . ASP A 1 22 ? -46.422 14.954 33.170 1.00 14.88 ? 22 ASP A OD1 1 ATOM 169 O OD2 . ASP A 1 22 ? -46.822 12.802 33.116 1.00 16.92 ? 22 ASP A OD2 1 ATOM 170 N N . TYR A 1 23 ? -47.515 17.684 35.101 1.00 13.61 ? 23 TYR A N 1 ATOM 171 C CA . TYR A 1 23 ? -47.828 18.997 34.533 1.00 13.42 ? 23 TYR A CA 1 ATOM 172 C C . TYR A 1 23 ? -47.815 19.074 33.003 1.00 14.74 ? 23 TYR A C 1 ATOM 173 O O . TYR A 1 23 ? -48.399 19.989 32.423 1.00 15.88 ? 23 TYR A O 1 ATOM 174 C CB . TYR A 1 23 ? -46.885 20.063 35.129 1.00 12.00 ? 23 TYR A CB 1 ATOM 175 C CG . TYR A 1 23 ? -45.406 19.749 34.999 1.00 11.74 ? 23 TYR A CG 1 ATOM 176 C CD1 . TYR A 1 23 ? -44.696 20.094 33.831 1.00 11.26 ? 23 TYR A CD1 1 ATOM 177 C CD2 . TYR A 1 23 ? -44.713 19.068 36.025 1.00 11.81 ? 23 TYR A CD2 1 ATOM 178 C CE1 . TYR A 1 23 ? -43.332 19.765 33.676 1.00 11.35 ? 23 TYR A CE1 1 ATOM 179 C CE2 . TYR A 1 23 ? -43.335 18.734 35.880 1.00 11.83 ? 23 TYR A CE2 1 ATOM 180 C CZ . TYR A 1 23 ? -42.662 19.090 34.696 1.00 11.59 ? 23 TYR A CZ 1 ATOM 181 O OH . TYR A 1 23 ? -41.341 18.771 34.511 1.00 13.43 ? 23 TYR A OH 1 ATOM 182 N N . GLU A 1 24 ? -47.101 18.144 32.368 1.00 16.76 ? 24 GLU A N 1 ATOM 183 C CA . GLU A 1 24 ? -47.000 18.092 30.906 1.00 18.04 ? 24 GLU A CA 1 ATOM 184 C C . GLU A 1 24 ? -48.286 17.630 30.231 1.00 17.71 ? 24 GLU A C 1 ATOM 185 O O . GLU A 1 24 ? -48.487 17.882 29.043 1.00 16.75 ? 24 GLU A O 1 ATOM 186 C CB . GLU A 1 24 ? -45.841 17.192 30.468 1.00 20.12 ? 24 GLU A CB 1 ATOM 187 C CG . GLU A 1 24 ? -44.467 17.813 30.667 1.00 22.90 ? 24 GLU A CG 1 ATOM 188 C CD . GLU A 1 24 ? -43.330 17.032 30.024 1.00 24.80 ? 24 GLU A CD 1 ATOM 189 O OE1 . GLU A 1 24 ? -43.522 15.870 29.602 1.00 25.13 ? 24 GLU A OE1 1 ATOM 190 O OE2 . GLU A 1 24 ? -42.221 17.594 29.946 1.00 27.21 ? 24 GLU A OE2 1 ATOM 191 N N . VAL A 1 25 ? -49.145 16.948 30.991 1.00 17.39 ? 25 VAL A N 1 ATOM 192 C CA . VAL A 1 25 ? -50.414 16.445 30.467 1.00 17.71 ? 25 VAL A CA 1 ATOM 193 C C . VAL A 1 25 ? -51.671 16.911 31.228 1.00 18.45 ? 25 VAL A C 1 ATOM 194 O O . VAL A 1 25 ? -52.790 16.746 30.737 1.00 18.49 ? 25 VAL A O 1 ATOM 195 C CB . VAL A 1 25 ? -50.417 14.883 30.346 1.00 15.97 ? 25 VAL A CB 1 ATOM 196 C CG1 . VAL A 1 25 ? -49.417 14.402 29.305 1.00 16.53 ? 25 VAL A CG1 1 ATOM 197 C CG2 . VAL A 1 25 ? -50.175 14.222 31.694 1.00 15.35 ? 25 VAL A CG2 1 ATOM 198 N N . SER A 1 26 ? -51.483 17.487 32.417 1.00 17.87 ? 26 SER A N 1 ATOM 199 C CA . SER A 1 26 ? -52.597 17.967 33.243 1.00 17.89 ? 26 SER A CA 1 ATOM 200 C C . SER A 1 26 ? -52.348 19.416 33.673 1.00 17.36 ? 26 SER A C 1 ATOM 201 O O . SER A 1 26 ? -51.312 19.726 34.270 1.00 16.44 ? 26 SER A O 1 ATOM 202 C CB . SER A 1 26 ? -52.778 17.052 34.457 1.00 18.97 ? 26 SER A CB 1 ATOM 203 O OG . SER A 1 26 ? -53.966 17.360 35.152 1.00 20.76 ? 26 SER A OG 1 ATOM 204 N N . THR A 1 27 ? -53.327 20.281 33.399 1.00 16.01 ? 27 THR A N 1 ATOM 205 C CA . THR A 1 27 ? -53.234 21.717 33.676 1.00 16.68 ? 27 THR A CA 1 ATOM 206 C C . THR A 1 27 ? -54.511 22.287 34.334 1.00 17.50 ? 27 THR A C 1 ATOM 207 O O . THR A 1 27 ? -55.620 21.936 33.919 1.00 17.62 ? 27 THR A O 1 ATOM 208 C CB . THR A 1 27 ? -52.978 22.474 32.326 1.00 16.51 ? 27 THR A CB 1 ATOM 209 O OG1 . THR A 1 27 ? -51.880 21.866 31.634 1.00 16.06 ? 27 THR A OG1 1 ATOM 210 C CG2 . THR A 1 27 ? -52.647 23.933 32.551 1.00 15.53 ? 27 THR A CG2 1 ATOM 211 N N . PRO A 1 28 ? -54.370 23.147 35.384 1.00 17.17 ? 28 PRO A N 1 ATOM 212 C CA . PRO A 1 28 ? -55.521 23.754 36.069 1.00 19.03 ? 28 PRO A CA 1 ATOM 213 C C . PRO A 1 28 ? -56.302 24.704 35.177 1.00 19.68 ? 28 PRO A C 1 ATOM 214 O O . PRO A 1 28 ? -55.715 25.484 34.423 1.00 19.17 ? 28 PRO A O 1 ATOM 215 C CB . PRO A 1 28 ? -54.873 24.546 37.209 1.00 17.90 ? 28 PRO A CB 1 ATOM 216 C CG . PRO A 1 28 ? -53.668 23.808 37.505 1.00 17.53 ? 28 PRO A CG 1 ATOM 217 C CD . PRO A 1 28 ? -53.143 23.417 36.157 1.00 17.19 ? 28 PRO A CD 1 ATOM 218 N N . ASP A 1 29 ? -57.625 24.616 35.254 1.00 20.91 ? 29 ASP A N 1 ATOM 219 C CA . ASP A 1 29 ? -58.494 25.491 34.487 1.00 22.85 ? 29 ASP A CA 1 ATOM 220 C C . ASP A 1 29 ? -58.888 26.605 35.460 1.00 22.96 ? 29 ASP A C 1 ATOM 221 O O . ASP A 1 29 ? -59.865 26.484 36.207 1.00 23.93 ? 29 ASP A O 1 ATOM 222 C CB . ASP A 1 29 ? -59.724 24.719 33.978 1.00 26.40 ? 29 ASP A CB 1 ATOM 223 C CG . ASP A 1 29 ? -60.408 25.403 32.797 1.00 30.39 ? 29 ASP A CG 1 ATOM 224 O OD1 . ASP A 1 29 ? -60.459 26.651 32.755 1.00 31.61 ? 29 ASP A OD1 1 ATOM 225 O OD2 . ASP A 1 29 ? -60.901 24.681 31.901 1.00 35.92 ? 29 ASP A OD2 1 ATOM 226 N N . THR A 1 30 ? -58.073 27.659 35.486 1.00 20.72 ? 30 THR A N 1 ATOM 227 C CA . THR A 1 30 ? -58.295 28.806 36.370 1.00 19.40 ? 30 THR A CA 1 ATOM 228 C C . THR A 1 30 ? -59.208 29.854 35.735 1.00 18.47 ? 30 THR A C 1 ATOM 229 O O . THR A 1 30 ? -59.888 30.596 36.443 1.00 17.59 ? 30 THR A O 1 ATOM 230 C CB . THR A 1 30 ? -56.970 29.514 36.737 1.00 19.70 ? 30 THR A CB 1 ATOM 231 O OG1 . THR A 1 30 ? -56.419 30.130 35.567 1.00 16.81 ? 30 THR A OG1 1 ATOM 232 C CG2 . THR A 1 30 ? -55.950 28.531 37.315 1.00 18.20 ? 30 THR A CG2 1 ATOM 233 N N . GLY A 1 31 ? -59.137 29.955 34.404 1.00 18.77 ? 31 GLY A N 1 ATOM 234 C CA . GLY A 1 31 ? -59.932 30.916 33.647 1.00 19.21 ? 31 GLY A CA 1 ATOM 235 C C . GLY A 1 31 ? -59.417 32.346 33.740 1.00 18.70 ? 31 GLY A C 1 ATOM 236 O O . GLY A 1 31 ? -60.046 33.276 33.234 1.00 19.53 ? 31 GLY A O 1 ATOM 237 N N . VAL A 1 32 ? -58.263 32.508 34.387 1.00 19.15 ? 32 VAL A N 1 ATOM 238 C CA . VAL A 1 32 ? -57.632 33.809 34.593 1.00 17.55 ? 32 VAL A CA 1 ATOM 239 C C . VAL A 1 32 ? -56.580 34.103 33.521 1.00 17.30 ? 32 VAL A C 1 ATOM 240 O O . VAL A 1 32 ? -55.849 33.209 33.081 1.00 16.06 ? 32 VAL A O 1 ATOM 241 C CB . VAL A 1 32 ? -57.000 33.896 36.029 1.00 18.97 ? 32 VAL A CB 1 ATOM 242 C CG1 . VAL A 1 32 ? -56.319 35.251 36.279 1.00 20.46 ? 32 VAL A CG1 1 ATOM 243 C CG2 . VAL A 1 32 ? -58.078 33.674 37.093 1.00 21.16 ? 32 VAL A CG2 1 ATOM 244 N N . THR A 1 33 ? -56.545 35.362 33.091 1.00 15.67 ? 33 THR A N 1 ATOM 245 C CA . THR A 1 33 ? -55.590 35.836 32.103 1.00 16.44 ? 33 THR A CA 1 ATOM 246 C C . THR A 1 33 ? -54.821 37.016 32.690 1.00 17.07 ? 33 THR A C 1 ATOM 247 O O . THR A 1 33 ? -55.418 37.941 33.247 1.00 17.02 ? 33 THR A O 1 ATOM 248 C CB . THR A 1 33 ? -56.277 36.261 30.762 1.00 16.16 ? 33 THR A CB 1 ATOM 249 O OG1 . THR A 1 33 ? -56.884 35.120 30.147 1.00 17.97 ? 33 THR A OG1 1 ATOM 250 C CG2 . THR A 1 33 ? -55.265 36.838 29.775 1.00 15.03 ? 33 THR A CG2 1 ATOM 251 N N . GLN A 1 34 ? -53.493 36.923 32.630 1.00 16.98 ? 34 GLN A N 1 ATOM 252 C CA . GLN A 1 34 ? -52.610 37.990 33.096 1.00 17.56 ? 34 GLN A CA 1 ATOM 253 C C . GLN A 1 34 ? -52.058 38.675 31.857 1.00 17.59 ? 34 GLN A C 1 ATOM 254 O O . GLN A 1 34 ? -51.340 38.062 31.059 1.00 18.01 ? 34 GLN A O 1 ATOM 255 C CB . GLN A 1 34 ? -51.478 37.450 33.982 1.00 18.58 ? 34 GLN A CB 1 ATOM 256 C CG . GLN A 1 34 ? -51.929 36.928 35.355 1.00 21.50 ? 34 GLN A CG 1 ATOM 257 C CD . GLN A 1 34 ? -52.600 37.981 36.243 1.00 23.72 ? 34 GLN A CD 1 ATOM 258 O OE1 . GLN A 1 34 ? -52.266 39.171 36.199 1.00 21.20 ? 34 GLN A OE1 1 ATOM 259 N NE2 . GLN A 1 34 ? -53.543 37.533 37.067 1.00 23.52 ? 34 GLN A NE2 1 ATOM 260 N N . SER A 1 35 ? -52.437 39.940 31.697 1.00 17.18 ? 35 SER A N 1 ATOM 261 C CA . SER A 1 35 ? -52.054 40.756 30.551 1.00 17.40 ? 35 SER A CA 1 ATOM 262 C C . SER A 1 35 ? -50.959 41.778 30.792 1.00 15.22 ? 35 SER A C 1 ATOM 263 O O . SER A 1 35 ? -50.871 42.371 31.866 1.00 16.44 ? 35 SER A O 1 ATOM 264 C CB . SER A 1 35 ? -53.283 41.457 29.992 1.00 17.21 ? 35 SER A CB 1 ATOM 265 O OG . SER A 1 35 ? -54.206 40.507 29.490 1.00 23.46 ? 35 SER A OG 1 ATOM 266 N N . TYR A 1 36 ? -50.104 41.939 29.780 1.00 14.91 ? 36 TYR A N 1 ATOM 267 C CA . TYR A 1 36 ? -48.972 42.869 29.800 1.00 14.41 ? 36 TYR A CA 1 ATOM 268 C C . TYR A 1 36 ? -48.841 43.533 28.435 1.00 14.88 ? 36 TYR A C 1 ATOM 269 O O . TYR A 1 36 ? -49.318 43.002 27.430 1.00 15.05 ? 36 TYR A O 1 ATOM 270 C CB . TYR A 1 36 ? -47.651 42.127 30.091 1.00 15.54 ? 36 TYR A CB 1 ATOM 271 C CG . TYR A 1 36 ? -47.600 41.396 31.412 1.00 16.76 ? 36 TYR A CG 1 ATOM 272 C CD1 . TYR A 1 36 ? -48.041 40.058 31.509 1.00 16.01 ? 36 TYR A CD1 1 ATOM 273 C CD2 . TYR A 1 36 ? -47.177 42.049 32.589 1.00 16.50 ? 36 TYR A CD2 1 ATOM 274 C CE1 . TYR A 1 36 ? -48.077 39.386 32.751 1.00 17.71 ? 36 TYR A CE1 1 ATOM 275 C CE2 . TYR A 1 36 ? -47.203 41.382 33.848 1.00 18.12 ? 36 TYR A CE2 1 ATOM 276 C CZ . TYR A 1 36 ? -47.659 40.053 33.912 1.00 18.05 ? 36 TYR A CZ 1 ATOM 277 O OH . TYR A 1 36 ? -47.708 39.388 35.110 1.00 20.42 ? 36 TYR A OH 1 ATOM 278 N N . VAL A 1 37 ? -48.224 44.713 28.416 1.00 15.79 ? 37 VAL A N 1 ATOM 279 C CA . VAL A 1 37 ? -47.971 45.459 27.183 1.00 16.55 ? 37 VAL A CA 1 ATOM 280 C C . VAL A 1 37 ? -46.482 45.779 27.168 1.00 16.44 ? 37 VAL A C 1 ATOM 281 O O . VAL A 1 37 ? -45.960 46.395 28.101 1.00 18.24 ? 37 VAL A O 1 ATOM 282 C CB . VAL A 1 37 ? -48.828 46.775 27.071 1.00 19.63 ? 37 VAL A CB 1 ATOM 283 C CG1 . VAL A 1 37 ? -48.363 47.645 25.896 1.00 19.52 ? 37 VAL A CG1 1 ATOM 284 C CG2 . VAL A 1 37 ? -50.300 46.429 26.855 1.00 20.08 ? 37 VAL A CG2 1 ATOM 285 N N . PHE A 1 38 ? -45.796 45.278 26.143 1.00 15.79 ? 38 PHE A N 1 ATOM 286 C CA . PHE A 1 38 ? -44.362 45.504 25.967 1.00 14.92 ? 38 PHE A CA 1 ATOM 287 C C . PHE A 1 38 ? -44.140 46.582 24.922 1.00 15.35 ? 38 PHE A C 1 ATOM 288 O O . PHE A 1 38 ? -44.374 46.355 23.732 1.00 14.10 ? 38 PHE A O 1 ATOM 289 C CB . PHE A 1 38 ? -43.632 44.236 25.483 1.00 14.30 ? 38 PHE A CB 1 ATOM 290 C CG . PHE A 1 38 ? -43.482 43.144 26.510 1.00 13.13 ? 38 PHE A CG 1 ATOM 291 C CD1 . PHE A 1 38 ? -44.085 43.213 27.785 1.00 14.63 ? 38 PHE A CD1 1 ATOM 292 C CD2 . PHE A 1 38 ? -42.777 41.982 26.160 1.00 14.16 ? 38 PHE A CD2 1 ATOM 293 C CE1 . PHE A 1 38 ? -43.999 42.133 28.692 1.00 15.99 ? 38 PHE A CE1 1 ATOM 294 C CE2 . PHE A 1 38 ? -42.683 40.893 27.055 1.00 15.00 ? 38 PHE A CE2 1 ATOM 295 C CZ . PHE A 1 38 ? -43.299 40.968 28.325 1.00 14.62 ? 38 PHE A CZ 1 ATOM 296 N N . ASN A 1 39 ? -43.683 47.747 25.367 1.00 15.34 ? 39 ASN A N 1 ATOM 297 C CA . ASN A 1 39 ? -43.400 48.857 24.465 1.00 15.61 ? 39 ASN A CA 1 ATOM 298 C C . ASN A 1 39 ? -41.883 48.904 24.320 1.00 14.94 ? 39 ASN A C 1 ATOM 299 O O . ASN A 1 39 ? -41.175 49.322 25.239 1.00 13.44 ? 39 ASN A O 1 ATOM 300 C CB . ASN A 1 39 ? -43.953 50.172 25.042 1.00 17.12 ? 39 ASN A CB 1 ATOM 301 C CG . ASN A 1 39 ? -43.759 51.371 24.113 1.00 22.42 ? 39 ASN A CG 1 ATOM 302 O OD1 . ASN A 1 39 ? -43.152 51.283 23.037 1.00 20.23 ? 39 ASN A OD1 1 ATOM 303 N ND2 . ASN A 1 39 ? -44.291 52.506 24.552 1.00 25.17 ? 39 ASN A ND2 1 ATOM 304 N N . LEU A 1 40 ? -41.396 48.469 23.158 1.00 14.03 ? 40 LEU A N 1 ATOM 305 C CA . LEU A 1 40 ? -39.962 48.457 22.891 1.00 15.29 ? 40 LEU A CA 1 ATOM 306 C C . LEU A 1 40 ? -39.524 49.786 22.323 1.00 13.69 ? 40 LEU A C 1 ATOM 307 O O . LEU A 1 40 ? -40.060 50.211 21.317 1.00 14.22 ? 40 LEU A O 1 ATOM 308 C CB . LEU A 1 40 ? -39.574 47.363 21.887 1.00 13.85 ? 40 LEU A CB 1 ATOM 309 C CG . LEU A 1 40 ? -40.077 45.920 21.890 1.00 16.50 ? 40 LEU A CG 1 ATOM 310 C CD1 . LEU A 1 40 ? -38.949 45.091 21.331 1.00 14.11 ? 40 LEU A CD1 1 ATOM 311 C CD2 . LEU A 1 40 ? -40.458 45.396 23.252 1.00 15.60 ? 40 LEU A CD2 1 ATOM 312 N N . THR A 1 41 ? -38.584 50.456 22.988 1.00 13.41 ? 41 THR A N 1 ATOM 313 C CA . THR A 1 41 ? -38.071 51.741 22.501 1.00 13.53 ? 41 THR A CA 1 ATOM 314 C C . THR A 1 41 ? -36.567 51.658 22.325 1.00 14.47 ? 41 THR A C 1 ATOM 315 O O . THR A 1 41 ? -35.901 50.822 22.941 1.00 12.21 ? 41 THR A O 1 ATOM 316 C CB . THR A 1 41 ? -38.399 52.940 23.440 1.00 13.91 ? 41 THR A CB 1 ATOM 317 O OG1 . THR A 1 41 ? -37.934 52.669 24.768 1.00 11.67 ? 41 THR A OG1 1 ATOM 318 C CG2 . THR A 1 41 ? -39.891 53.233 23.457 1.00 14.45 ? 41 THR A CG2 1 ATOM 319 N N . GLU A 1 42 ? -36.052 52.498 21.435 1.00 14.20 ? 42 GLU A N 1 ATOM 320 C CA . GLU A 1 42 ? -34.631 52.559 21.148 1.00 15.49 ? 42 GLU A CA 1 ATOM 321 C C . GLU A 1 42 ? -34.111 53.818 21.828 1.00 16.16 ? 42 GLU A C 1 ATOM 322 O O . GLU A 1 42 ? -34.533 54.928 21.494 1.00 17.54 ? 42 GLU A O 1 ATOM 323 C CB . GLU A 1 42 ? -34.424 52.622 19.637 1.00 15.14 ? 42 GLU A CB 1 ATOM 324 C CG . GLU A 1 42 ? -33.038 52.248 19.170 1.00 15.41 ? 42 GLU A CG 1 ATOM 325 C CD . GLU A 1 42 ? -33.007 51.896 17.700 1.00 15.79 ? 42 GLU A CD 1 ATOM 326 O OE1 . GLU A 1 42 ? -33.951 51.232 17.225 1.00 14.55 ? 42 GLU A OE1 1 ATOM 327 O OE2 . GLU A 1 42 ? -32.041 52.282 17.015 1.00 17.72 ? 42 GLU A OE2 1 ATOM 328 N N . VAL A 1 43 ? -33.266 53.625 22.839 1.00 16.12 ? 43 VAL A N 1 ATOM 329 C CA . VAL A 1 43 ? -32.698 54.736 23.602 1.00 16.32 ? 43 VAL A CA 1 ATOM 330 C C . VAL A 1 43 ? -31.195 54.862 23.358 1.00 16.88 ? 43 VAL A C 1 ATOM 331 O O . VAL A 1 43 ? -30.431 53.912 23.561 1.00 15.80 ? 43 VAL A O 1 ATOM 332 C CB . VAL A 1 43 ? -32.970 54.590 25.145 1.00 16.96 ? 43 VAL A CB 1 ATOM 333 C CG1 . VAL A 1 43 ? -32.530 55.842 25.897 1.00 16.10 ? 43 VAL A CG1 1 ATOM 334 C CG2 . VAL A 1 43 ? -34.452 54.321 25.423 1.00 18.07 ? 43 VAL A CG2 1 ATOM 335 N N . ASP A 1 44 ? -30.787 56.051 22.919 1.00 16.49 ? 44 ASP A N 1 ATOM 336 C CA . ASP A 1 44 ? -29.383 56.343 22.671 1.00 15.78 ? 44 ASP A CA 1 ATOM 337 C C . ASP A 1 44 ? -28.804 57.029 23.898 1.00 15.91 ? 44 ASP A C 1 ATOM 338 O O . ASP A 1 44 ? -29.537 57.672 24.658 1.00 15.22 ? 44 ASP A O 1 ATOM 339 C CB . ASP A 1 44 ? -29.208 57.240 21.441 1.00 17.40 ? 44 ASP A CB 1 ATOM 340 C CG . ASP A 1 44 ? -29.649 56.567 20.149 1.00 19.29 ? 44 ASP A CG 1 ATOM 341 O OD1 . ASP A 1 44 ? -29.470 55.337 20.009 1.00 20.19 ? 44 ASP A OD1 1 ATOM 342 O OD2 . ASP A 1 44 ? -30.177 57.276 19.269 1.00 20.41 ? 44 ASP A OD2 1 ATOM 343 N N . ASN A 1 45 ? -27.500 56.835 24.110 1.00 15.53 ? 45 ASN A N 1 ATOM 344 C CA . ASN A 1 45 ? -26.743 57.423 25.225 1.00 16.08 ? 45 ASN A CA 1 ATOM 345 C C . ASN A 1 45 ? -27.432 57.248 26.579 1.00 16.84 ? 45 ASN A C 1 ATOM 346 O O . ASN A 1 45 ? -27.696 58.205 27.310 1.00 16.54 ? 45 ASN A O 1 ATOM 347 C CB . ASN A 1 45 ? -26.404 58.889 24.923 1.00 15.43 ? 45 ASN A CB 1 ATOM 348 C CG . ASN A 1 45 ? -25.734 59.050 23.578 1.00 15.46 ? 45 ASN A CG 1 ATOM 349 O OD1 . ASN A 1 45 ? -24.614 58.589 23.370 1.00 16.02 ? 45 ASN A OD1 1 ATOM 350 N ND2 . ASN A 1 45 ? -26.437 59.673 22.639 1.00 16.65 ? 45 ASN A ND2 1 ATOM 351 N N . TRP A 1 46 ? -27.730 55.987 26.875 1.00 17.97 ? 46 TRP A N 1 ATOM 352 C CA . TRP A 1 46 ? -28.419 55.585 28.089 1.00 18.11 ? 46 TRP A CA 1 ATOM 353 C C . TRP A 1 46 ? -27.456 55.313 29.230 1.00 17.87 ? 46 TRP A C 1 ATOM 354 O O . TRP A 1 46 ? -26.494 54.563 29.075 1.00 18.33 ? 46 TRP A O 1 ATOM 355 C CB . TRP A 1 46 ? -29.258 54.345 27.773 1.00 18.80 ? 46 TRP A CB 1 ATOM 356 C CG . TRP A 1 46 ? -30.025 53.723 28.912 1.00 18.77 ? 46 TRP A CG 1 ATOM 357 C CD1 . TRP A 1 46 ? -31.215 54.148 29.434 1.00 19.52 ? 46 TRP A CD1 1 ATOM 358 C CD2 . TRP A 1 46 ? -29.688 52.516 29.604 1.00 18.32 ? 46 TRP A CD2 1 ATOM 359 N NE1 . TRP A 1 46 ? -31.646 53.275 30.407 1.00 20.58 ? 46 TRP A NE1 1 ATOM 360 C CE2 . TRP A 1 46 ? -30.730 52.263 30.535 1.00 18.60 ? 46 TRP A CE2 1 ATOM 361 C CE3 . TRP A 1 46 ? -28.605 51.614 29.528 1.00 17.90 ? 46 TRP A CE3 1 ATOM 362 C CZ2 . TRP A 1 46 ? -30.726 51.139 31.393 1.00 17.22 ? 46 TRP A CZ2 1 ATOM 363 C CZ3 . TRP A 1 46 ? -28.598 50.484 30.381 1.00 17.87 ? 46 TRP A CZ3 1 ATOM 364 C CH2 . TRP A 1 46 ? -29.656 50.265 31.301 1.00 17.26 ? 46 TRP A CH2 1 ATOM 365 N N . MET A 1 47 ? -27.776 55.884 30.390 1.00 18.48 ? 47 MET A N 1 ATOM 366 C CA . MET A 1 47 ? -26.983 55.720 31.601 1.00 18.94 ? 47 MET A CA 1 ATOM 367 C C . MET A 1 47 ? -27.274 54.347 32.201 1.00 18.27 ? 47 MET A C 1 ATOM 368 O O . MET A 1 47 ? -28.401 54.065 32.622 1.00 17.53 ? 47 MET A O 1 ATOM 369 C CB . MET A 1 47 ? -27.298 56.836 32.612 1.00 21.18 ? 47 MET A CB 1 ATOM 370 C CG . MET A 1 47 ? -26.592 56.702 33.967 1.00 25.52 ? 47 MET A CG 1 ATOM 371 S SD . MET A 1 47 ? -24.810 56.557 33.807 1.00 31.34 ? 47 MET A SD 1 ATOM 372 C CE . MET A 1 47 ? -24.309 58.246 34.239 1.00 30.77 ? 47 MET A CE 1 ATOM 373 N N . GLY A 1 48 ? -26.252 53.495 32.176 1.00 17.63 ? 48 GLY A N 1 ATOM 374 C CA . GLY A 1 48 ? -26.357 52.152 32.715 1.00 17.03 ? 48 GLY A CA 1 ATOM 375 C C . GLY A 1 48 ? -26.190 52.089 34.224 1.00 17.38 ? 48 GLY A C 1 ATOM 376 O O . GLY A 1 48 ? -25.702 53.056 34.818 1.00 16.93 ? 48 GLY A O 1 ATOM 377 N N . PRO A 1 49 ? -26.530 50.949 34.867 1.00 16.87 ? 49 PRO A N 1 ATOM 378 C CA . PRO A 1 49 ? -26.425 50.770 36.322 1.00 18.07 ? 49 PRO A CA 1 ATOM 379 C C . PRO A 1 49 ? -25.045 50.880 36.967 1.00 17.70 ? 49 PRO A C 1 ATOM 380 O O . PRO A 1 49 ? -24.959 51.139 38.166 1.00 18.31 ? 49 PRO A O 1 ATOM 381 C CB . PRO A 1 49 ? -27.070 49.406 36.547 1.00 18.61 ? 49 PRO A CB 1 ATOM 382 C CG . PRO A 1 49 ? -26.812 48.694 35.272 1.00 17.90 ? 49 PRO A CG 1 ATOM 383 C CD . PRO A 1 49 ? -27.081 49.734 34.240 1.00 16.50 ? 49 PRO A CD 1 ATOM 384 N N . ASP A 1 50 ? -23.979 50.696 36.186 1.00 18.29 ? 50 ASP A N 1 ATOM 385 C CA . ASP A 1 50 ? -22.627 50.816 36.732 1.00 18.36 ? 50 ASP A CA 1 ATOM 386 C C . ASP A 1 50 ? -21.979 52.184 36.472 1.00 18.63 ? 50 ASP A C 1 ATOM 387 O O . ASP A 1 50 ? -20.777 52.362 36.670 1.00 19.70 ? 50 ASP A O 1 ATOM 388 C CB . ASP A 1 50 ? -21.724 49.626 36.321 1.00 16.15 ? 50 ASP A CB 1 ATOM 389 C CG . ASP A 1 50 ? -21.346 49.608 34.836 1.00 16.39 ? 50 ASP A CG 1 ATOM 390 O OD1 . ASP A 1 50 ? -21.784 50.472 34.046 1.00 15.30 ? 50 ASP A OD1 1 ATOM 391 O OD2 . ASP A 1 50 ? -20.586 48.691 34.464 1.00 18.25 ? 50 ASP A OD2 1 ATOM 392 N N . GLY A 1 51 ? -22.791 53.136 36.013 1.00 18.81 ? 51 GLY A N 1 ATOM 393 C CA . GLY A 1 51 ? -22.309 54.483 35.756 1.00 20.28 ? 51 GLY A CA 1 ATOM 394 C C . GLY A 1 51 ? -21.848 54.787 34.346 1.00 21.15 ? 51 GLY A C 1 ATOM 395 O O . GLY A 1 51 ? -21.724 55.958 33.982 1.00 22.28 ? 51 GLY A O 1 ATOM 396 N N . VAL A 1 52 ? -21.587 53.747 33.554 1.00 20.24 ? 52 VAL A N 1 ATOM 397 C CA . VAL A 1 52 ? -21.143 53.928 32.175 1.00 18.83 ? 52 VAL A CA 1 ATOM 398 C C . VAL A 1 52 ? -22.338 54.124 31.253 1.00 18.18 ? 52 VAL A C 1 ATOM 399 O O . VAL A 1 52 ? -23.367 53.455 31.380 1.00 16.62 ? 52 VAL A O 1 ATOM 400 C CB . VAL A 1 52 ? -20.255 52.750 31.693 1.00 19.61 ? 52 VAL A CB 1 ATOM 401 C CG1 . VAL A 1 52 ? -19.817 52.932 30.229 1.00 19.02 ? 52 VAL A CG1 1 ATOM 402 C CG2 . VAL A 1 52 ? -19.024 52.644 32.571 1.00 18.41 ? 52 VAL A CG2 1 ATOM 403 N N . VAL A 1 53 ? -22.172 55.066 30.334 1.00 17.09 ? 53 VAL A N 1 ATOM 404 C CA . VAL A 1 53 ? -23.191 55.422 29.362 1.00 17.19 ? 53 VAL A CA 1 ATOM 405 C C . VAL A 1 53 ? -23.014 54.560 28.110 1.00 16.88 ? 53 VAL A C 1 ATOM 406 O O . VAL A 1 53 ? -21.943 54.563 27.495 1.00 16.58 ? 53 VAL A O 1 ATOM 407 C CB . VAL A 1 53 ? -23.105 56.949 29.035 1.00 17.61 ? 53 VAL A CB 1 ATOM 408 C CG1 . VAL A 1 53 ? -24.111 57.345 27.988 1.00 18.11 ? 53 VAL A CG1 1 ATOM 409 C CG2 . VAL A 1 53 ? -23.345 57.770 30.297 1.00 16.92 ? 53 VAL A CG2 1 ATOM 410 N N . LYS A 1 54 ? -24.065 53.816 27.760 1.00 15.33 ? 54 LYS A N 1 ATOM 411 C CA . LYS A 1 54 ? -24.054 52.948 26.577 1.00 16.81 ? 54 LYS A CA 1 ATOM 412 C C . LYS A 1 54 ? -24.544 53.719 25.367 1.00 15.78 ? 54 LYS A C 1 ATOM 413 O O . LYS A 1 54 ? -25.522 54.458 25.462 1.00 14.00 ? 54 LYS A O 1 ATOM 414 C CB . LYS A 1 54 ? -24.974 51.738 26.757 1.00 17.29 ? 54 LYS A CB 1 ATOM 415 C CG . LYS A 1 54 ? -24.721 50.885 27.984 1.00 20.00 ? 54 LYS A CG 1 ATOM 416 C CD . LYS A 1 54 ? -24.488 49.406 27.658 1.00 19.58 ? 54 LYS A CD 1 ATOM 417 C CE . LYS A 1 54 ? -25.496 48.784 26.699 1.00 20.81 ? 54 LYS A CE 1 ATOM 418 N NZ . LYS A 1 54 ? -25.399 47.303 26.559 1.00 17.32 ? 54 LYS A NZ 1 ATOM 419 N N . GLU A 1 55 ? -23.908 53.464 24.224 1.00 16.13 ? 55 GLU A N 1 ATOM 420 C CA . GLU A 1 55 ? -24.223 54.095 22.937 1.00 16.12 ? 55 GLU A CA 1 ATOM 421 C C . GLU A 1 55 ? -25.698 53.931 22.546 1.00 15.75 ? 55 GLU A C 1 ATOM 422 O O . GLU A 1 55 ? -26.367 54.911 22.210 1.00 12.70 ? 55 GLU A O 1 ATOM 423 C CB . GLU A 1 55 ? -23.329 53.481 21.850 1.00 17.36 ? 55 GLU A CB 1 ATOM 424 C CG . GLU A 1 55 ? -23.458 54.090 20.453 1.00 22.11 ? 55 GLU A CG 1 ATOM 425 C CD . GLU A 1 55 ? -22.976 53.156 19.348 1.00 24.08 ? 55 GLU A CD 1 ATOM 426 O OE1 . GLU A 1 55 ? -22.045 52.351 19.584 1.00 25.23 ? 55 GLU A OE1 1 ATOM 427 O OE2 . GLU A 1 55 ? -23.535 53.230 18.232 1.00 24.67 ? 55 GLU A OE2 1 ATOM 428 N N . LYS A 1 56 ? -26.194 52.696 22.639 1.00 13.95 ? 56 LYS A N 1 ATOM 429 C CA . LYS A 1 56 ? -27.570 52.371 22.285 1.00 13.73 ? 56 LYS A CA 1 ATOM 430 C C . LYS A 1 56 ? -28.065 51.126 23.013 1.00 14.60 ? 56 LYS A C 1 ATOM 431 O O . LYS A 1 56 ? -27.309 50.177 23.232 1.00 15.85 ? 56 LYS A O 1 ATOM 432 C CB . LYS A 1 56 ? -27.676 52.145 20.767 1.00 13.04 ? 56 LYS A CB 1 ATOM 433 C CG . LYS A 1 56 ? -29.096 51.931 20.216 1.00 12.11 ? 56 LYS A CG 1 ATOM 434 C CD . LYS A 1 56 ? -29.076 51.551 18.741 1.00 11.28 ? 56 LYS A CD 1 ATOM 435 C CE . LYS A 1 56 ? -28.707 52.718 17.821 1.00 13.01 ? 56 LYS A CE 1 ATOM 436 N NZ . LYS A 1 56 ? -29.771 53.756 17.771 1.00 12.36 ? 56 LYS A NZ 1 ATOM 437 N N . VAL A 1 57 ? -29.331 51.178 23.429 1.00 14.25 ? 57 VAL A N 1 ATOM 438 C CA . VAL A 1 57 ? -30.020 50.072 24.086 1.00 13.04 ? 57 VAL A CA 1 ATOM 439 C C . VAL A 1 57 ? -31.434 49.993 23.517 1.00 14.10 ? 57 VAL A C 1 ATOM 440 O O . VAL A 1 57 ? -31.944 50.966 22.948 1.00 12.28 ? 57 VAL A O 1 ATOM 441 C CB . VAL A 1 57 ? -30.132 50.219 25.632 1.00 14.96 ? 57 VAL A CB 1 ATOM 442 C CG1 . VAL A 1 57 ? -28.805 50.023 26.295 1.00 14.74 ? 57 VAL A CG1 1 ATOM 443 C CG2 . VAL A 1 57 ? -30.726 51.545 26.010 1.00 13.32 ? 57 VAL A CG2 1 ATOM 444 N N . MET A 1 58 ? -32.046 48.820 23.652 1.00 12.47 ? 58 MET A N 1 ATOM 445 C CA . MET A 1 58 ? -33.407 48.572 23.183 1.00 12.41 ? 58 MET A CA 1 ATOM 446 C C . MET A 1 58 ? -34.123 48.039 24.408 1.00 12.41 ? 58 MET A C 1 ATOM 447 O O . MET A 1 58 ? -33.855 46.928 24.865 1.00 10.98 ? 58 MET A O 1 ATOM 448 C CB . MET A 1 58 ? -33.407 47.582 22.023 1.00 11.67 ? 58 MET A CB 1 ATOM 449 C CG . MET A 1 58 ? -32.717 48.136 20.781 1.00 11.86 ? 58 MET A CG 1 ATOM 450 S SD . MET A 1 58 ? -32.525 46.963 19.467 1.00 12.87 ? 58 MET A SD 1 ATOM 451 C CE . MET A 1 58 ? -31.510 47.922 18.330 1.00 10.58 ? 58 MET A CE 1 ATOM 452 N N . LEU A 1 59 ? -34.984 48.886 24.969 1.00 11.03 ? 59 LEU A N 1 ATOM 453 C CA . LEU A 1 59 ? -35.696 48.596 26.207 1.00 13.30 ? 59 LEU A CA 1 ATOM 454 C C . LEU A 1 59 ? -37.187 48.366 26.110 1.00 14.24 ? 59 LEU A C 1 ATOM 455 O O . LEU A 1 59 ? -37.863 48.926 25.257 1.00 14.18 ? 59 LEU A O 1 ATOM 456 C CB . LEU A 1 59 ? -35.478 49.746 27.201 1.00 12.97 ? 59 LEU A CB 1 ATOM 457 C CG . LEU A 1 59 ? -34.081 50.318 27.455 1.00 11.69 ? 59 LEU A CG 1 ATOM 458 C CD1 . LEU A 1 59 ? -34.165 51.520 28.362 1.00 12.36 ? 59 LEU A CD1 1 ATOM 459 C CD2 . LEU A 1 59 ? -33.164 49.261 28.040 1.00 12.95 ? 59 LEU A CD2 1 ATOM 460 N N . ILE A 1 60 ? -37.691 47.585 27.060 1.00 14.56 ? 60 ILE A N 1 ATOM 461 C CA . ILE A 1 60 ? -39.111 47.298 27.172 1.00 14.85 ? 60 ILE A CA 1 ATOM 462 C C . ILE A 1 60 ? -39.597 48.193 28.316 1.00 15.38 ? 60 ILE A C 1 ATOM 463 O O . ILE A 1 60 ? -39.045 48.150 29.426 1.00 13.90 ? 60 ILE A O 1 ATOM 464 C CB . ILE A 1 60 ? -39.379 45.820 27.535 1.00 15.09 ? 60 ILE A CB 1 ATOM 465 C CG1 . ILE A 1 60 ? -38.765 44.882 26.493 1.00 15.88 ? 60 ILE A CG1 1 ATOM 466 C CG2 . ILE A 1 60 ? -40.876 45.585 27.711 1.00 15.22 ? 60 ILE A CG2 1 ATOM 467 C CD1 . ILE A 1 60 ? -38.957 43.401 26.771 1.00 16.03 ? 60 ILE A CD1 1 ATOM 468 N N . ASN A 1 61 ? -40.601 49.022 28.016 1.00 14.45 ? 61 ASN A N 1 ATOM 469 C CA . ASN A 1 61 ? -41.222 49.959 28.963 1.00 16.79 ? 61 ASN A CA 1 ATOM 470 C C . ASN A 1 61 ? -40.247 50.911 29.692 1.00 16.90 ? 61 ASN A C 1 ATOM 471 O O . ASN A 1 61 ? -40.442 51.252 30.863 1.00 17.59 ? 61 ASN A O 1 ATOM 472 C CB . ASN A 1 61 ? -42.143 49.202 29.949 1.00 15.99 ? 61 ASN A CB 1 ATOM 473 C CG . ASN A 1 61 ? -43.254 48.422 29.239 1.00 16.83 ? 61 ASN A CG 1 ATOM 474 O OD1 . ASN A 1 61 ? -43.524 48.639 28.056 1.00 14.85 ? 61 ASN A OD1 1 ATOM 475 N ND2 . ASN A 1 61 ? -43.880 47.492 29.956 1.00 15.14 ? 61 ASN A ND2 1 ATOM 476 N N . GLY A 1 62 ? -39.174 51.280 28.986 1.00 16.05 ? 62 GLY A N 1 ATOM 477 C CA . GLY A 1 62 ? -38.160 52.193 29.503 1.00 17.37 ? 62 GLY A CA 1 ATOM 478 C C . GLY A 1 62 ? -37.221 51.720 30.602 1.00 16.72 ? 62 GLY A C 1 ATOM 479 O O . GLY A 1 62 ? -36.500 52.537 31.183 1.00 16.82 ? 62 GLY A O 1 ATOM 480 N N . ASN A 1 63 ? -37.215 50.417 30.884 1.00 15.27 ? 63 ASN A N 1 ATOM 481 C CA . ASN A 1 63 ? -36.361 49.849 31.933 1.00 16.48 ? 63 ASN A CA 1 ATOM 482 C C . ASN A 1 63 ? -35.336 48.872 31.362 1.00 16.20 ? 63 ASN A C 1 ATOM 483 O O . ASN A 1 63 ? -35.502 48.382 30.245 1.00 15.87 ? 63 ASN A O 1 ATOM 484 C CB . ASN A 1 63 ? -37.212 49.140 32.998 1.00 18.25 ? 63 ASN A CB 1 ATOM 485 C CG . ASN A 1 63 ? -38.243 50.056 33.639 1.00 19.34 ? 63 ASN A CG 1 ATOM 486 O OD1 . ASN A 1 63 ? -37.985 51.236 33.879 1.00 19.79 ? 63 ASN A OD1 1 ATOM 487 N ND2 . ASN A 1 63 ? -39.423 49.513 33.911 1.00 21.02 ? 63 ASN A ND2 1 ATOM 488 N N . ILE A 1 64 ? -34.307 48.560 32.157 1.00 16.12 ? 64 ILE A N 1 ATOM 489 C CA . ILE A 1 64 ? -33.223 47.643 31.771 1.00 14.68 ? 64 ILE A CA 1 ATOM 490 C C . ILE A 1 64 ? -33.757 46.263 31.347 1.00 13.89 ? 64 ILE A C 1 ATOM 491 O O . ILE A 1 64 ? -33.246 45.636 30.415 1.00 14.38 ? 64 ILE A O 1 ATOM 492 C CB . ILE A 1 64 ? -32.143 47.542 32.907 1.00 15.15 ? 64 ILE A CB 1 ATOM 493 C CG1 . ILE A 1 64 ? -30.927 46.746 32.422 1.00 16.19 ? 64 ILE A CG1 1 ATOM 494 C CG2 . ILE A 1 64 ? -32.739 46.980 34.217 1.00 13.16 ? 64 ILE A CG2 1 ATOM 495 C CD1 . ILE A 1 64 ? -29.699 46.989 33.230 1.00 16.15 ? 64 ILE A CD1 1 ATOM 496 N N . MET A 1 65 ? -34.812 45.832 32.028 1.00 13.96 ? 65 MET A N 1 ATOM 497 C CA . MET A 1 65 ? -35.479 44.574 31.734 1.00 13.79 ? 65 MET A CA 1 ATOM 498 C C . MET A 1 65 ? -36.958 44.866 31.614 1.00 13.16 ? 65 MET A C 1 ATOM 499 O O . MET A 1 65 ? -37.440 45.905 32.083 1.00 11.34 ? 65 MET A O 1 ATOM 500 C CB . MET A 1 65 ? -35.255 43.552 32.847 1.00 16.61 ? 65 MET A CB 1 ATOM 501 C CG . MET A 1 65 ? -33.964 42.768 32.736 1.00 21.17 ? 65 MET A CG 1 ATOM 502 S SD . MET A 1 65 ? -33.785 41.656 34.134 1.00 26.40 ? 65 MET A SD 1 ATOM 503 C CE . MET A 1 65 ? -33.187 42.832 35.387 1.00 22.75 ? 65 MET A CE 1 ATOM 504 N N . GLY A 1 66 ? -37.685 43.944 30.991 1.00 12.47 ? 66 GLY A N 1 ATOM 505 C CA . GLY A 1 66 ? -39.118 44.114 30.853 1.00 12.99 ? 66 GLY A CA 1 ATOM 506 C C . GLY A 1 66 ? -39.803 43.802 32.165 1.00 13.68 ? 66 GLY A C 1 ATOM 507 O O . GLY A 1 66 ? -39.106 43.490 33.137 1.00 10.72 ? 66 GLY A O 1 ATOM 508 N N . PRO A 1 67 ? -41.146 43.893 32.249 1.00 16.11 ? 67 PRO A N 1 ATOM 509 C CA . PRO A 1 67 ? -41.791 43.579 33.527 1.00 17.28 ? 67 PRO A CA 1 ATOM 510 C C . PRO A 1 67 ? -41.683 42.092 33.859 1.00 18.47 ? 67 PRO A C 1 ATOM 511 O O . PRO A 1 67 ? -41.478 41.257 32.967 1.00 17.39 ? 67 PRO A O 1 ATOM 512 C CB . PRO A 1 67 ? -43.240 44.015 33.300 1.00 19.45 ? 67 PRO A CB 1 ATOM 513 C CG . PRO A 1 67 ? -43.426 43.869 31.834 1.00 17.71 ? 67 PRO A CG 1 ATOM 514 C CD . PRO A 1 67 ? -42.135 44.393 31.275 1.00 17.28 ? 67 PRO A CD 1 ATOM 515 N N . ASN A 1 68 ? -41.706 41.792 35.154 1.00 18.68 ? 68 ASN A N 1 ATOM 516 C CA . ASN A 1 68 ? -41.637 40.420 35.632 1.00 19.54 ? 68 ASN A CA 1 ATOM 517 C C . ASN A 1 68 ? -43.019 39.809 35.452 1.00 19.58 ? 68 ASN A C 1 ATOM 518 O O . ASN A 1 68 ? -43.980 40.244 36.092 1.00 21.35 ? 68 ASN A O 1 ATOM 519 C CB . ASN A 1 68 ? -41.240 40.379 37.115 1.00 21.27 ? 68 ASN A CB 1 ATOM 520 C CG . ASN A 1 68 ? -39.891 41.034 37.388 1.00 23.48 ? 68 ASN A CG 1 ATOM 521 O OD1 . ASN A 1 68 ? -38.981 40.999 36.558 1.00 23.10 ? 68 ASN A OD1 1 ATOM 522 N ND2 . ASN A 1 68 ? -39.759 41.629 38.567 1.00 23.71 ? 68 ASN A ND2 1 ATOM 523 N N . ILE A 1 69 ? -43.130 38.881 34.502 1.00 17.71 ? 69 ILE A N 1 ATOM 524 C CA . ILE A 1 69 ? -44.393 38.196 34.241 1.00 16.55 ? 69 ILE A CA 1 ATOM 525 C C . ILE A 1 69 ? -44.668 37.271 35.419 1.00 15.24 ? 69 ILE A C 1 ATOM 526 O O . ILE A 1 69 ? -43.812 36.477 35.800 1.00 14.78 ? 69 ILE A O 1 ATOM 527 C CB . ILE A 1 69 ? -44.376 37.417 32.887 1.00 15.26 ? 69 ILE A CB 1 ATOM 528 C CG1 . ILE A 1 69 ? -44.384 38.417 31.726 1.00 15.65 ? 69 ILE A CG1 1 ATOM 529 C CG2 . ILE A 1 69 ? -45.565 36.440 32.784 1.00 16.08 ? 69 ILE A CG2 1 ATOM 530 C CD1 . ILE A 1 69 ? -44.319 37.788 30.350 1.00 12.21 ? 69 ILE A CD1 1 ATOM 531 N N . VAL A 1 70 ? -45.798 37.517 36.080 1.00 16.11 ? 70 VAL A N 1 ATOM 532 C CA . VAL A 1 70 ? -46.234 36.733 37.234 1.00 15.23 ? 70 VAL A CA 1 ATOM 533 C C . VAL A 1 70 ? -47.662 36.234 36.977 1.00 15.18 ? 70 VAL A C 1 ATOM 534 O O . VAL A 1 70 ? -48.558 37.015 36.645 1.00 14.96 ? 70 VAL A O 1 ATOM 535 C CB . VAL A 1 70 ? -46.191 37.556 38.574 1.00 15.68 ? 70 VAL A CB 1 ATOM 536 C CG1 . VAL A 1 70 ? -46.575 36.670 39.767 1.00 17.32 ? 70 VAL A CG1 1 ATOM 537 C CG2 . VAL A 1 70 ? -44.796 38.146 38.819 1.00 14.81 ? 70 VAL A CG2 1 ATOM 538 N N . ALA A 1 71 ? -47.840 34.923 37.104 1.00 13.32 ? 71 ALA A N 1 ATOM 539 C CA . ALA A 1 71 ? -49.133 34.263 36.926 1.00 14.38 ? 71 ALA A CA 1 ATOM 540 C C . ALA A 1 71 ? -49.114 32.947 37.692 1.00 14.54 ? 71 ALA A C 1 ATOM 541 O O . ALA A 1 71 ? -48.073 32.539 38.206 1.00 14.54 ? 71 ALA A O 1 ATOM 542 C CB . ALA A 1 71 ? -49.412 34.006 35.441 1.00 10.52 ? 71 ALA A CB 1 ATOM 543 N N . ASN A 1 72 ? -50.278 32.311 37.804 1.00 14.37 ? 72 ASN A N 1 ATOM 544 C CA . ASN A 1 72 ? -50.389 31.028 38.488 1.00 15.54 ? 72 ASN A CA 1 ATOM 545 C C . ASN A 1 72 ? -50.437 29.918 37.453 1.00 15.25 ? 72 ASN A C 1 ATOM 546 O O . ASN A 1 72 ? -50.695 30.164 36.274 1.00 15.90 ? 72 ASN A O 1 ATOM 547 C CB . ASN A 1 72 ? -51.652 30.975 39.359 1.00 16.34 ? 72 ASN A CB 1 ATOM 548 C CG . ASN A 1 72 ? -51.608 31.955 40.518 1.00 16.17 ? 72 ASN A CG 1 ATOM 549 O OD1 . ASN A 1 72 ? -50.608 32.045 41.228 1.00 18.82 ? 72 ASN A OD1 1 ATOM 550 N ND2 . ASN A 1 72 ? -52.697 32.690 40.716 1.00 14.46 ? 72 ASN A ND2 1 ATOM 551 N N . TRP A 1 73 ? -50.168 28.697 37.908 1.00 14.23 ? 73 TRP A N 1 ATOM 552 C CA . TRP A 1 73 ? -50.195 27.497 37.078 1.00 12.62 ? 73 TRP A CA 1 ATOM 553 C C . TRP A 1 73 ? -51.612 27.307 36.518 1.00 12.32 ? 73 TRP A C 1 ATOM 554 O O . TRP A 1 73 ? -52.588 27.302 37.266 1.00 11.14 ? 73 TRP A O 1 ATOM 555 C CB . TRP A 1 73 ? -49.763 26.309 37.946 1.00 12.22 ? 73 TRP A CB 1 ATOM 556 C CG . TRP A 1 73 ? -49.697 24.940 37.304 1.00 11.07 ? 73 TRP A CG 1 ATOM 557 C CD1 . TRP A 1 73 ? -49.535 24.633 35.974 1.00 9.61 ? 73 TRP A CD1 1 ATOM 558 C CD2 . TRP A 1 73 ? -49.759 23.697 37.994 1.00 10.95 ? 73 TRP A CD2 1 ATOM 559 N NE1 . TRP A 1 73 ? -49.495 23.272 35.802 1.00 9.90 ? 73 TRP A NE1 1 ATOM 560 C CE2 . TRP A 1 73 ? -49.628 22.668 37.023 1.00 11.13 ? 73 TRP A CE2 1 ATOM 561 C CE3 . TRP A 1 73 ? -49.904 23.342 39.349 1.00 13.68 ? 73 TRP A CE3 1 ATOM 562 C CZ2 . TRP A 1 73 ? -49.641 21.298 37.366 1.00 10.71 ? 73 TRP A CZ2 1 ATOM 563 C CZ3 . TRP A 1 73 ? -49.912 21.976 39.696 1.00 11.53 ? 73 TRP A CZ3 1 ATOM 564 C CH2 . TRP A 1 73 ? -49.781 20.972 38.699 1.00 13.09 ? 73 TRP A CH2 1 ATOM 565 N N . GLY A 1 74 ? -51.700 27.243 35.193 1.00 10.96 ? 74 GLY A N 1 ATOM 566 C CA . GLY A 1 74 ? -52.983 27.070 34.542 1.00 12.86 ? 74 GLY A CA 1 ATOM 567 C C . GLY A 1 74 ? -53.581 28.332 33.960 1.00 14.56 ? 74 GLY A C 1 ATOM 568 O O . GLY A 1 74 ? -54.555 28.260 33.199 1.00 15.34 ? 74 GLY A O 1 ATOM 569 N N . ASP A 1 75 ? -53.027 29.485 34.343 1.00 14.75 ? 75 ASP A N 1 ATOM 570 C CA . ASP A 1 75 ? -53.469 30.787 33.830 1.00 14.77 ? 75 ASP A CA 1 ATOM 571 C C . ASP A 1 75 ? -53.034 30.922 32.374 1.00 15.25 ? 75 ASP A C 1 ATOM 572 O O . ASP A 1 75 ? -52.260 30.109 31.858 1.00 15.07 ? 75 ASP A O 1 ATOM 573 C CB . ASP A 1 75 ? -52.794 31.952 34.579 1.00 14.51 ? 75 ASP A CB 1 ATOM 574 C CG . ASP A 1 75 ? -53.327 32.175 35.987 1.00 14.02 ? 75 ASP A CG 1 ATOM 575 O OD1 . ASP A 1 75 ? -54.282 31.504 36.415 1.00 12.52 ? 75 ASP A OD1 1 ATOM 576 O OD2 . ASP A 1 75 ? -52.768 33.057 36.673 1.00 13.40 ? 75 ASP A OD2 1 ATOM 577 N N . THR A 1 76 ? -53.557 31.948 31.719 1.00 15.48 ? 76 THR A N 1 ATOM 578 C CA . THR A 1 76 ? -53.172 32.253 30.358 1.00 15.09 ? 76 THR A CA 1 ATOM 579 C C . THR A 1 76 ? -52.421 33.575 30.483 1.00 14.94 ? 76 THR A C 1 ATOM 580 O O . THR A 1 76 ? -52.818 34.452 31.252 1.00 15.50 ? 76 THR A O 1 ATOM 581 C CB . THR A 1 76 ? -54.389 32.394 29.415 1.00 15.71 ? 76 THR A CB 1 ATOM 582 O OG1 . THR A 1 76 ? -55.065 31.135 29.313 1.00 14.12 ? 76 THR A OG1 1 ATOM 583 C CG2 . THR A 1 76 ? -53.941 32.802 28.023 1.00 17.53 ? 76 THR A CG2 1 ATOM 584 N N . VAL A 1 77 ? -51.259 33.650 29.846 1.00 14.07 ? 77 VAL A N 1 ATOM 585 C CA . VAL A 1 77 ? -50.476 34.873 29.857 1.00 13.27 ? 77 VAL A CA 1 ATOM 586 C C . VAL A 1 77 ? -50.641 35.476 28.466 1.00 14.54 ? 77 VAL A C 1 ATOM 587 O O . VAL A 1 77 ? -50.536 34.778 27.453 1.00 12.63 ? 77 VAL A O 1 ATOM 588 C CB . VAL A 1 77 ? -48.991 34.616 30.204 1.00 14.15 ? 77 VAL A CB 1 ATOM 589 C CG1 . VAL A 1 77 ? -48.178 35.908 30.134 1.00 12.15 ? 77 VAL A CG1 1 ATOM 590 C CG2 . VAL A 1 77 ? -48.875 34.023 31.602 1.00 14.16 ? 77 VAL A CG2 1 ATOM 591 N N . GLU A 1 78 ? -50.961 36.765 28.447 1.00 15.07 ? 78 GLU A N 1 ATOM 592 C CA . GLU A 1 78 ? -51.183 37.494 27.212 1.00 15.90 ? 78 GLU A CA 1 ATOM 593 C C . GLU A 1 78 ? -50.304 38.726 27.187 1.00 15.14 ? 78 GLU A C 1 ATOM 594 O O . GLU A 1 78 ? -50.320 39.533 28.115 1.00 15.34 ? 78 GLU A O 1 ATOM 595 C CB . GLU A 1 78 ? -52.658 37.876 27.101 1.00 16.04 ? 78 GLU A CB 1 ATOM 596 C CG . GLU A 1 78 ? -53.047 38.481 25.774 1.00 20.78 ? 78 GLU A CG 1 ATOM 597 C CD . GLU A 1 78 ? -54.528 38.399 25.484 1.00 22.37 ? 78 GLU A CD 1 ATOM 598 O OE1 . GLU A 1 78 ? -55.338 38.328 26.435 1.00 23.99 ? 78 GLU A OE1 1 ATOM 599 O OE2 . GLU A 1 78 ? -54.880 38.402 24.287 1.00 25.22 ? 78 GLU A OE2 1 ATOM 600 N N . VAL A 1 79 ? -49.516 38.855 26.125 1.00 14.40 ? 79 VAL A N 1 ATOM 601 C CA . VAL A 1 79 ? -48.608 39.982 25.987 1.00 12.93 ? 79 VAL A CA 1 ATOM 602 C C . VAL A 1 79 ? -48.697 40.669 24.626 1.00 13.90 ? 79 VAL A C 1 ATOM 603 O O . VAL A 1 79 ? -48.416 40.059 23.591 1.00 12.21 ? 79 VAL A O 1 ATOM 604 C CB . VAL A 1 79 ? -47.127 39.555 26.226 1.00 13.76 ? 79 VAL A CB 1 ATOM 605 C CG1 . VAL A 1 79 ? -46.212 40.730 26.028 1.00 12.29 ? 79 VAL A CG1 1 ATOM 606 C CG2 . VAL A 1 79 ? -46.914 38.993 27.638 1.00 13.12 ? 79 VAL A CG2 1 ATOM 607 N N . THR A 1 80 ? -49.026 41.959 24.650 1.00 13.91 ? 80 THR A N 1 ATOM 608 C CA . THR A 1 80 ? -49.092 42.756 23.427 1.00 13.59 ? 80 THR A CA 1 ATOM 609 C C . THR A 1 80 ? -47.737 43.429 23.281 1.00 12.39 ? 80 THR A C 1 ATOM 610 O O . THR A 1 80 ? -47.326 44.211 24.137 1.00 13.39 ? 80 THR A O 1 ATOM 611 C CB . THR A 1 80 ? -50.228 43.813 23.466 1.00 12.27 ? 80 THR A CB 1 ATOM 612 O OG1 . THR A 1 80 ? -51.482 43.145 23.617 1.00 14.93 ? 80 THR A OG1 1 ATOM 613 C CG2 . THR A 1 80 ? -50.263 44.640 22.163 1.00 11.63 ? 80 THR A CG2 1 ATOM 614 N N . VAL A 1 81 ? -47.024 43.071 22.220 1.00 12.50 ? 81 VAL A N 1 ATOM 615 C CA . VAL A 1 81 ? -45.708 43.646 21.967 1.00 12.48 ? 81 VAL A CA 1 ATOM 616 C C . VAL A 1 81 ? -45.817 44.707 20.894 1.00 11.64 ? 81 VAL A C 1 ATOM 617 O O . VAL A 1 81 ? -46.240 44.425 19.778 1.00 11.61 ? 81 VAL A O 1 ATOM 618 C CB . VAL A 1 81 ? -44.674 42.559 21.556 1.00 12.38 ? 81 VAL A CB 1 ATOM 619 C CG1 . VAL A 1 81 ? -43.301 43.177 21.301 1.00 12.36 ? 81 VAL A CG1 1 ATOM 620 C CG2 . VAL A 1 81 ? -44.575 41.515 22.643 1.00 9.55 ? 81 VAL A CG2 1 ATOM 621 N N . ILE A 1 82 ? -45.464 45.933 21.263 1.00 12.18 ? 82 ILE A N 1 ATOM 622 C CA . ILE A 1 82 ? -45.496 47.063 20.345 1.00 12.13 ? 82 ILE A CA 1 ATOM 623 C C . ILE A 1 82 ? -44.048 47.440 20.077 1.00 12.45 ? 82 ILE A C 1 ATOM 624 O O . ILE A 1 82 ? -43.318 47.854 20.984 1.00 13.06 ? 82 ILE A O 1 ATOM 625 C CB . ILE A 1 82 ? -46.289 48.278 20.923 1.00 12.49 ? 82 ILE A CB 1 ATOM 626 C CG1 . ILE A 1 82 ? -47.699 47.836 21.348 1.00 12.22 ? 82 ILE A CG1 1 ATOM 627 C CG2 . ILE A 1 82 ? -46.393 49.399 19.859 1.00 11.77 ? 82 ILE A CG2 1 ATOM 628 C CD1 . ILE A 1 82 ? -48.476 48.869 22.116 1.00 13.43 ? 82 ILE A CD1 1 ATOM 629 N N . ASN A 1 83 ? -43.642 47.268 18.823 1.00 11.33 ? 83 ASN A N 1 ATOM 630 C CA . ASN A 1 83 ? -42.286 47.567 18.399 1.00 12.05 ? 83 ASN A CA 1 ATOM 631 C C . ASN A 1 83 ? -42.115 49.021 17.949 1.00 11.30 ? 83 ASN A C 1 ATOM 632 O O . ASN A 1 83 ? -42.460 49.377 16.818 1.00 11.11 ? 83 ASN A O 1 ATOM 633 C CB . ASN A 1 83 ? -41.858 46.593 17.289 1.00 11.86 ? 83 ASN A CB 1 ATOM 634 C CG . ASN A 1 83 ? -40.390 46.745 16.894 1.00 13.40 ? 83 ASN A CG 1 ATOM 635 O OD1 . ASN A 1 83 ? -39.664 47.542 17.471 1.00 13.71 ? 83 ASN A OD1 1 ATOM 636 N ND2 . ASN A 1 83 ? -39.966 46.000 15.884 1.00 11.42 ? 83 ASN A ND2 1 ATOM 637 N N . ASN A 1 84 ? -41.505 49.821 18.821 1.00 12.02 ? 84 ASN A N 1 ATOM 638 C CA . ASN A 1 84 ? -41.241 51.230 18.535 1.00 13.02 ? 84 ASN A CA 1 ATOM 639 C C . ASN A 1 84 ? -39.750 51.506 18.347 1.00 14.05 ? 84 ASN A C 1 ATOM 640 O O . ASN A 1 84 ? -39.270 52.615 18.597 1.00 12.51 ? 84 ASN A O 1 ATOM 641 C CB . ASN A 1 84 ? -41.849 52.133 19.615 1.00 14.73 ? 84 ASN A CB 1 ATOM 642 C CG . ASN A 1 84 ? -43.343 52.302 19.451 1.00 15.09 ? 84 ASN A CG 1 ATOM 643 O OD1 . ASN A 1 84 ? -43.822 52.606 18.358 1.00 17.31 ? 84 ASN A OD1 1 ATOM 644 N ND2 . ASN A 1 84 ? -44.089 52.107 20.533 1.00 14.12 ? 84 ASN A ND2 1 ATOM 645 N N . LEU A 1 85 ? -39.017 50.482 17.900 1.00 13.52 ? 85 LEU A N 1 ATOM 646 C CA . LEU A 1 85 ? -37.584 50.622 17.608 1.00 13.81 ? 85 LEU A CA 1 ATOM 647 C C . LEU A 1 85 ? -37.522 51.377 16.273 1.00 13.93 ? 85 LEU A C 1 ATOM 648 O O . LEU A 1 85 ? -38.542 51.495 15.590 1.00 15.14 ? 85 LEU A O 1 ATOM 649 C CB . LEU A 1 85 ? -36.896 49.250 17.508 1.00 11.98 ? 85 LEU A CB 1 ATOM 650 C CG . LEU A 1 85 ? -36.943 48.363 18.763 1.00 13.94 ? 85 LEU A CG 1 ATOM 651 C CD1 . LEU A 1 85 ? -36.366 46.992 18.485 1.00 13.66 ? 85 LEU A CD1 1 ATOM 652 C CD2 . LEU A 1 85 ? -36.239 49.004 19.916 1.00 12.08 ? 85 LEU A CD2 1 ATOM 653 N N . VAL A 1 86 ? -36.363 51.915 15.914 1.00 15.29 ? 86 VAL A N 1 ATOM 654 C CA . VAL A 1 86 ? -36.253 52.683 14.672 1.00 16.26 ? 86 VAL A CA 1 ATOM 655 C C . VAL A 1 86 ? -36.194 51.825 13.407 1.00 15.85 ? 86 VAL A C 1 ATOM 656 O O . VAL A 1 86 ? -36.974 52.044 12.477 1.00 15.72 ? 86 VAL A O 1 ATOM 657 C CB . VAL A 1 86 ? -35.061 53.702 14.714 1.00 17.13 ? 86 VAL A CB 1 ATOM 658 C CG1 . VAL A 1 86 ? -35.089 54.637 13.491 1.00 16.00 ? 86 VAL A CG1 1 ATOM 659 C CG2 . VAL A 1 86 ? -35.128 54.541 15.989 1.00 16.83 ? 86 VAL A CG2 1 ATOM 660 N N . THR A 1 87 ? -35.314 50.823 13.397 1.00 16.52 ? 87 THR A N 1 ATOM 661 C CA . THR A 1 87 ? -35.137 49.972 12.219 1.00 15.24 ? 87 THR A CA 1 ATOM 662 C C . THR A 1 87 ? -35.452 48.497 12.398 1.00 16.18 ? 87 THR A C 1 ATOM 663 O O . THR A 1 87 ? -36.011 47.855 11.499 1.00 15.31 ? 87 THR A O 1 ATOM 664 C CB . THR A 1 87 ? -33.694 50.066 11.685 1.00 15.51 ? 87 THR A CB 1 ATOM 665 O OG1 . THR A 1 87 ? -32.772 49.663 12.710 1.00 15.75 ? 87 THR A OG1 1 ATOM 666 C CG2 . THR A 1 87 ? -33.376 51.481 11.225 1.00 14.37 ? 87 THR A CG2 1 ATOM 667 N N . ASN A 1 88 ? -35.067 47.970 13.556 1.00 13.83 ? 88 ASN A N 1 ATOM 668 C CA . ASN A 1 88 ? -35.241 46.567 13.902 1.00 13.11 ? 88 ASN A CA 1 ATOM 669 C C . ASN A 1 88 ? -36.653 46.041 14.030 1.00 12.36 ? 88 ASN A C 1 ATOM 670 O O . ASN A 1 88 ? -37.539 46.699 14.577 1.00 11.32 ? 88 ASN A O 1 ATOM 671 C CB . ASN A 1 88 ? -34.594 46.279 15.257 1.00 14.23 ? 88 ASN A CB 1 ATOM 672 C CG . ASN A 1 88 ? -33.104 46.103 15.192 1.00 16.13 ? 88 ASN A CG 1 ATOM 673 O OD1 . ASN A 1 88 ? -32.536 45.450 16.070 1.00 16.91 ? 88 ASN A OD1 1 ATOM 674 N ND2 . ASN A 1 88 ? -32.456 46.694 14.194 1.00 15.15 ? 88 ASN A ND2 1 ATOM 675 N N . GLY A 1 89 ? -36.821 44.801 13.587 1.00 10.87 ? 89 GLY A N 1 ATOM 676 C CA . GLY A 1 89 ? -38.078 44.113 13.784 1.00 9.76 ? 89 GLY A CA 1 ATOM 677 C C . GLY A 1 89 ? -37.859 43.440 15.136 1.00 10.17 ? 89 GLY A C 1 ATOM 678 O O . GLY A 1 89 ? -36.800 43.640 15.754 1.00 8.34 ? 89 GLY A O 1 ATOM 679 N N . THR A 1 90 ? -38.834 42.679 15.621 1.00 9.74 ? 90 THR A N 1 ATOM 680 C CA . THR A 1 90 ? -38.675 41.981 16.896 1.00 11.37 ? 90 THR A CA 1 ATOM 681 C C . THR A 1 90 ? -39.599 40.781 16.976 1.00 10.74 ? 90 THR A C 1 ATOM 682 O O . THR A 1 90 ? -40.535 40.665 16.198 1.00 10.14 ? 90 THR A O 1 ATOM 683 C CB . THR A 1 90 ? -38.898 42.926 18.134 1.00 11.02 ? 90 THR A CB 1 ATOM 684 O OG1 . THR A 1 90 ? -38.309 42.332 19.302 1.00 9.41 ? 90 THR A OG1 1 ATOM 685 C CG2 . THR A 1 90 ? -40.388 43.205 18.396 1.00 8.82 ? 90 THR A CG2 1 ATOM 686 N N . SER A 1 91 ? -39.291 39.879 17.899 1.00 14.14 ? 91 SER A N 1 ATOM 687 C CA . SER A 1 91 ? -40.092 38.686 18.149 1.00 15.28 ? 91 SER A CA 1 ATOM 688 C C . SER A 1 91 ? -39.691 38.221 19.532 1.00 17.05 ? 91 SER A C 1 ATOM 689 O O . SER A 1 91 ? -38.523 37.913 19.769 1.00 19.39 ? 91 SER A O 1 ATOM 690 C CB . SER A 1 91 ? -39.830 37.584 17.118 1.00 17.37 ? 91 SER A CB 1 ATOM 691 O OG . SER A 1 91 ? -38.529 37.040 17.247 1.00 23.27 ? 91 SER A OG 1 ATOM 692 N N . ILE A 1 92 ? -40.650 38.205 20.450 1.00 14.70 ? 92 ILE A N 1 ATOM 693 C CA . ILE A 1 92 ? -40.369 37.795 21.819 1.00 13.78 ? 92 ILE A CA 1 ATOM 694 C C . ILE A 1 92 ? -40.613 36.306 22.019 1.00 11.52 ? 92 ILE A C 1 ATOM 695 O O . ILE A 1 92 ? -41.718 35.803 21.803 1.00 10.63 ? 92 ILE A O 1 ATOM 696 C CB . ILE A 1 92 ? -41.176 38.632 22.856 1.00 13.99 ? 92 ILE A CB 1 ATOM 697 C CG1 . ILE A 1 92 ? -41.098 40.133 22.532 1.00 14.53 ? 92 ILE A CG1 1 ATOM 698 C CG2 . ILE A 1 92 ? -40.653 38.379 24.279 1.00 14.20 ? 92 ILE A CG2 1 ATOM 699 C CD1 . ILE A 1 92 ? -39.702 40.740 22.471 1.00 16.25 ? 92 ILE A CD1 1 ATOM 700 N N . HIS A 1 93 ? -39.541 35.617 22.397 1.00 10.28 ? 93 HIS A N 1 ATOM 701 C CA . HIS A 1 93 ? -39.559 34.190 22.656 1.00 10.28 ? 93 HIS A CA 1 ATOM 702 C C . HIS A 1 93 ? -39.712 33.964 24.148 1.00 10.31 ? 93 HIS A C 1 ATOM 703 O O . HIS A 1 93 ? -39.055 34.609 24.949 1.00 9.32 ? 93 HIS A O 1 ATOM 704 C CB . HIS A 1 93 ? -38.282 33.522 22.124 1.00 9.72 ? 93 HIS A CB 1 ATOM 705 C CG . HIS A 1 93 ? -38.138 32.080 22.515 1.00 7.81 ? 93 HIS A CG 1 ATOM 706 N ND1 . HIS A 1 93 ? -39.131 31.147 22.314 1.00 8.16 ? 93 HIS A ND1 1 ATOM 707 C CD2 . HIS A 1 93 ? -37.136 31.430 23.150 1.00 7.55 ? 93 HIS A CD2 1 ATOM 708 C CE1 . HIS A 1 93 ? -38.749 29.985 22.815 1.00 8.39 ? 93 HIS A CE1 1 ATOM 709 N NE2 . HIS A 1 93 ? -37.542 30.130 23.327 1.00 9.17 ? 93 HIS A NE2 1 ATOM 710 N N . TRP A 1 94 ? -40.566 33.010 24.493 1.00 10.84 ? 94 TRP A N 1 ATOM 711 C CA . TRP A 1 94 ? -40.852 32.666 25.877 1.00 11.37 ? 94 TRP A CA 1 ATOM 712 C C . TRP A 1 94 ? -40.077 31.391 26.192 1.00 11.38 ? 94 TRP A C 1 ATOM 713 O O . TRP A 1 94 ? -40.568 30.272 26.041 1.00 11.15 ? 94 TRP A O 1 ATOM 714 C CB . TRP A 1 94 ? -42.373 32.523 26.062 1.00 10.79 ? 94 TRP A CB 1 ATOM 715 C CG . TRP A 1 94 ? -43.137 33.573 25.302 1.00 14.19 ? 94 TRP A CG 1 ATOM 716 C CD1 . TRP A 1 94 ? -43.614 33.468 24.021 1.00 13.75 ? 94 TRP A CD1 1 ATOM 717 C CD2 . TRP A 1 94 ? -43.340 34.936 25.691 1.00 14.07 ? 94 TRP A CD2 1 ATOM 718 N NE1 . TRP A 1 94 ? -44.072 34.685 23.578 1.00 15.08 ? 94 TRP A NE1 1 ATOM 719 C CE2 . TRP A 1 94 ? -43.918 35.607 24.579 1.00 15.58 ? 94 TRP A CE2 1 ATOM 720 C CE3 . TRP A 1 94 ? -43.078 35.667 26.867 1.00 15.48 ? 94 TRP A CE3 1 ATOM 721 C CZ2 . TRP A 1 94 ? -44.234 36.981 24.607 1.00 16.47 ? 94 TRP A CZ2 1 ATOM 722 C CZ3 . TRP A 1 94 ? -43.392 37.041 26.894 1.00 15.61 ? 94 TRP A CZ3 1 ATOM 723 C CH2 . TRP A 1 94 ? -43.963 37.677 25.765 1.00 15.42 ? 94 TRP A CH2 1 ATOM 724 N N . HIS A 1 95 ? -38.822 31.603 26.578 1.00 12.05 ? 95 HIS A N 1 ATOM 725 C CA . HIS A 1 95 ? -37.865 30.549 26.905 1.00 12.36 ? 95 HIS A CA 1 ATOM 726 C C . HIS A 1 95 ? -38.315 29.692 28.090 1.00 12.21 ? 95 HIS A C 1 ATOM 727 O O . HIS A 1 95 ? -38.422 30.181 29.214 1.00 14.20 ? 95 HIS A O 1 ATOM 728 C CB . HIS A 1 95 ? -36.498 31.207 27.168 1.00 11.13 ? 95 HIS A CB 1 ATOM 729 C CG . HIS A 1 95 ? -35.354 30.248 27.309 1.00 11.76 ? 95 HIS A CG 1 ATOM 730 N ND1 . HIS A 1 95 ? -34.175 30.408 26.616 1.00 12.45 ? 95 HIS A ND1 1 ATOM 731 C CD2 . HIS A 1 95 ? -35.173 29.177 28.121 1.00 11.29 ? 95 HIS A CD2 1 ATOM 732 C CE1 . HIS A 1 95 ? -33.319 29.478 27.003 1.00 14.98 ? 95 HIS A CE1 1 ATOM 733 N NE2 . HIS A 1 95 ? -33.900 28.717 27.911 1.00 12.87 ? 95 HIS A NE2 1 ATOM 734 N N . GLY A 1 96 ? -38.465 28.396 27.827 1.00 11.36 ? 96 GLY A N 1 ATOM 735 C CA . GLY A 1 96 ? -38.888 27.456 28.852 1.00 13.00 ? 96 GLY A CA 1 ATOM 736 C C . GLY A 1 96 ? -40.360 27.120 28.755 1.00 12.85 ? 96 GLY A C 1 ATOM 737 O O . GLY A 1 96 ? -40.810 26.128 29.327 1.00 11.38 ? 96 GLY A O 1 ATOM 738 N N . ILE A 1 97 ? -41.114 27.972 28.060 1.00 12.91 ? 97 ILE A N 1 ATOM 739 C CA . ILE A 1 97 ? -42.547 27.768 27.868 1.00 14.11 ? 97 ILE A CA 1 ATOM 740 C C . ILE A 1 97 ? -42.699 26.894 26.633 1.00 15.24 ? 97 ILE A C 1 ATOM 741 O O . ILE A 1 97 ? -42.334 27.295 25.521 1.00 14.71 ? 97 ILE A O 1 ATOM 742 C CB . ILE A 1 97 ? -43.306 29.109 27.712 1.00 12.58 ? 97 ILE A CB 1 ATOM 743 C CG1 . ILE A 1 97 ? -42.970 30.062 28.878 1.00 12.91 ? 97 ILE A CG1 1 ATOM 744 C CG2 . ILE A 1 97 ? -44.808 28.871 27.558 1.00 13.11 ? 97 ILE A CG2 1 ATOM 745 C CD1 . ILE A 1 97 ? -43.216 29.535 30.282 1.00 12.42 ? 97 ILE A CD1 1 ATOM 746 N N . HIS A 1 98 ? -43.239 25.698 26.859 1.00 16.17 ? 98 HIS A N 1 ATOM 747 C CA . HIS A 1 98 ? -43.421 24.684 25.826 1.00 17.30 ? 98 HIS A CA 1 ATOM 748 C C . HIS A 1 98 ? -44.282 24.978 24.615 1.00 15.95 ? 98 HIS A C 1 ATOM 749 O O . HIS A 1 98 ? -44.095 24.358 23.563 1.00 15.40 ? 98 HIS A O 1 ATOM 750 C CB . HIS A 1 98 ? -43.861 23.366 26.462 1.00 20.27 ? 98 HIS A CB 1 ATOM 751 C CG . HIS A 1 98 ? -42.851 22.803 27.406 1.00 23.77 ? 98 HIS A CG 1 ATOM 752 N ND1 . HIS A 1 98 ? -41.572 23.307 27.495 1.00 24.21 ? 98 HIS A ND1 1 ATOM 753 C CD2 . HIS A 1 98 ? -42.929 21.804 28.315 1.00 23.10 ? 98 HIS A CD2 1 ATOM 754 C CE1 . HIS A 1 98 ? -40.907 22.646 28.420 1.00 24.84 ? 98 HIS A CE1 1 ATOM 755 N NE2 . HIS A 1 98 ? -41.706 21.727 28.934 1.00 21.77 ? 98 HIS A NE2 1 ATOM 756 N N . GLN A 1 99 ? -45.203 25.931 24.755 1.00 15.66 ? 99 GLN A N 1 ATOM 757 C CA . GLN A 1 99 ? -46.128 26.326 23.686 1.00 15.73 ? 99 GLN A CA 1 ATOM 758 C C . GLN A 1 99 ? -46.862 25.106 23.098 1.00 16.10 ? 99 GLN A C 1 ATOM 759 O O . GLN A 1 99 ? -46.873 24.885 21.877 1.00 14.30 ? 99 GLN A O 1 ATOM 760 C CB . GLN A 1 99 ? -45.403 27.127 22.580 1.00 16.85 ? 99 GLN A CB 1 ATOM 761 C CG . GLN A 1 99 ? -44.657 28.390 23.040 1.00 15.55 ? 99 GLN A CG 1 ATOM 762 C CD . GLN A 1 99 ? -45.557 29.554 23.439 1.00 17.04 ? 99 GLN A CD 1 ATOM 763 O OE1 . GLN A 1 99 ? -45.115 30.474 24.127 1.00 17.42 ? 99 GLN A OE1 1 ATOM 764 N NE2 . GLN A 1 99 ? -46.811 29.534 22.990 1.00 13.94 ? 99 GLN A NE2 1 ATOM 765 N N . LYS A 1 100 ? -47.416 24.295 24.004 1.00 16.54 ? 100 LYS A N 1 ATOM 766 C CA . LYS A 1 100 ? -48.147 23.069 23.670 1.00 18.01 ? 100 LYS A CA 1 ATOM 767 C C . LYS A 1 100 ? -49.337 23.376 22.764 1.00 16.86 ? 100 LYS A C 1 ATOM 768 O O . LYS A 1 100 ? -50.337 23.951 23.200 1.00 16.52 ? 100 LYS A O 1 ATOM 769 C CB . LYS A 1 100 ? -48.598 22.355 24.951 1.00 20.78 ? 100 LYS A CB 1 ATOM 770 C CG . LYS A 1 100 ? -48.993 20.888 24.791 1.00 25.46 ? 100 LYS A CG 1 ATOM 771 C CD . LYS A 1 100 ? -47.782 19.997 24.552 1.00 30.49 ? 100 LYS A CD 1 ATOM 772 C CE . LYS A 1 100 ? -48.077 18.549 24.899 1.00 31.44 ? 100 LYS A CE 1 ATOM 773 N NZ . LYS A 1 100 ? -48.218 18.343 26.360 1.00 34.84 ? 100 LYS A NZ 1 ATOM 774 N N . ASP A 1 101 ? -49.161 23.028 21.485 1.00 16.89 ? 101 ASP A N 1 ATOM 775 C CA . ASP A 1 101 ? -50.125 23.239 20.393 1.00 16.78 ? 101 ASP A CA 1 ATOM 776 C C . ASP A 1 101 ? -50.338 24.723 20.048 1.00 16.38 ? 101 ASP A C 1 ATOM 777 O O . ASP A 1 101 ? -51.323 25.092 19.399 1.00 15.99 ? 101 ASP A O 1 ATOM 778 C CB . ASP A 1 101 ? -51.451 22.490 20.634 1.00 18.96 ? 101 ASP A CB 1 ATOM 779 C CG . ASP A 1 101 ? -51.262 20.983 20.722 1.00 20.94 ? 101 ASP A CG 1 ATOM 780 O OD1 . ASP A 1 101 ? -50.781 20.381 19.743 1.00 22.34 ? 101 ASP A OD1 1 ATOM 781 O OD2 . ASP A 1 101 ? -51.571 20.408 21.786 1.00 25.12 ? 101 ASP A OD2 1 ATOM 782 N N . THR A 1 102 ? -49.404 25.567 20.503 1.00 15.16 ? 102 THR A N 1 ATOM 783 C CA . THR A 1 102 ? -49.427 27.010 20.231 1.00 14.51 ? 102 THR A CA 1 ATOM 784 C C . THR A 1 102 ? -48.066 27.451 19.663 1.00 14.74 ? 102 THR A C 1 ATOM 785 O O . THR A 1 102 ? -47.508 28.478 20.071 1.00 14.31 ? 102 THR A O 1 ATOM 786 C CB . THR A 1 102 ? -49.796 27.873 21.492 1.00 13.29 ? 102 THR A CB 1 ATOM 787 O OG1 . THR A 1 102 ? -48.870 27.618 22.552 1.00 14.15 ? 102 THR A OG1 1 ATOM 788 C CG2 . THR A 1 102 ? -51.210 27.594 21.977 1.00 14.38 ? 102 THR A CG2 1 ATOM 789 N N . ASN A 1 103 ? -47.566 26.683 18.686 1.00 15.15 ? 103 ASN A N 1 ATOM 790 C CA . ASN A 1 103 ? -46.277 26.932 18.011 1.00 13.78 ? 103 ASN A CA 1 ATOM 791 C C . ASN A 1 103 ? -46.111 28.348 17.448 1.00 13.55 ? 103 ASN A C 1 ATOM 792 O O . ASN A 1 103 ? -45.037 28.934 17.563 1.00 12.66 ? 103 ASN A O 1 ATOM 793 C CB . ASN A 1 103 ? -46.051 25.888 16.898 1.00 12.45 ? 103 ASN A CB 1 ATOM 794 C CG . ASN A 1 103 ? -44.670 25.998 16.230 1.00 12.56 ? 103 ASN A CG 1 ATOM 795 O OD1 . ASN A 1 103 ? -44.566 26.016 15.004 1.00 14.09 ? 103 ASN A OD1 1 ATOM 796 N ND2 . ASN A 1 103 ? -43.615 26.029 17.033 1.00 9.20 ? 103 ASN A ND2 1 ATOM 797 N N . LEU A 1 104 ? -47.195 28.916 16.925 1.00 11.29 ? 104 LEU A N 1 ATOM 798 C CA . LEU A 1 104 ? -47.170 30.262 16.339 1.00 12.26 ? 104 LEU A CA 1 ATOM 799 C C . LEU A 1 104 ? -46.957 31.412 17.325 1.00 10.65 ? 104 LEU A C 1 ATOM 800 O O . LEU A 1 104 ? -46.782 32.564 16.919 1.00 12.95 ? 104 LEU A O 1 ATOM 801 C CB . LEU A 1 104 ? -48.416 30.489 15.477 1.00 11.76 ? 104 LEU A CB 1 ATOM 802 C CG . LEU A 1 104 ? -48.287 29.959 14.042 1.00 13.25 ? 104 LEU A CG 1 ATOM 803 C CD1 . LEU A 1 104 ? -48.160 28.437 14.013 1.00 10.06 ? 104 LEU A CD1 1 ATOM 804 C CD2 . LEU A 1 104 ? -49.483 30.402 13.223 1.00 14.61 ? 104 LEU A CD2 1 ATOM 805 N N . HIS A 1 105 ? -46.916 31.075 18.613 1.00 10.34 ? 105 HIS A N 1 ATOM 806 C CA . HIS A 1 105 ? -46.691 32.048 19.679 1.00 11.96 ? 105 HIS A CA 1 ATOM 807 C C . HIS A 1 105 ? -45.297 31.904 20.306 1.00 10.88 ? 105 HIS A C 1 ATOM 808 O O . HIS A 1 105 ? -44.964 32.612 21.262 1.00 9.92 ? 105 HIS A O 1 ATOM 809 C CB . HIS A 1 105 ? -47.783 31.923 20.748 1.00 13.11 ? 105 HIS A CB 1 ATOM 810 C CG . HIS A 1 105 ? -49.139 32.340 20.270 1.00 13.92 ? 105 HIS A CG 1 ATOM 811 N ND1 . HIS A 1 105 ? -49.641 33.606 20.477 1.00 14.63 ? 105 HIS A ND1 1 ATOM 812 C CD2 . HIS A 1 105 ? -50.081 31.673 19.562 1.00 16.09 ? 105 HIS A CD2 1 ATOM 813 C CE1 . HIS A 1 105 ? -50.832 33.704 19.911 1.00 16.00 ? 105 HIS A CE1 1 ATOM 814 N NE2 . HIS A 1 105 ? -51.122 32.545 19.349 1.00 17.97 ? 105 HIS A NE2 1 ATOM 815 N N . ASP A 1 106 ? -44.461 31.050 19.708 1.00 9.86 ? 106 ASP A N 1 ATOM 816 C CA . ASP A 1 106 ? -43.103 30.789 20.196 1.00 9.59 ? 106 ASP A CA 1 ATOM 817 C C . ASP A 1 106 ? -42.151 31.988 20.118 1.00 9.73 ? 106 ASP A C 1 ATOM 818 O O . ASP A 1 106 ? -41.212 32.075 20.899 1.00 7.75 ? 106 ASP A O 1 ATOM 819 C CB . ASP A 1 106 ? -42.506 29.575 19.476 1.00 8.95 ? 106 ASP A CB 1 ATOM 820 C CG . ASP A 1 106 ? -41.255 29.040 20.155 1.00 11.18 ? 106 ASP A CG 1 ATOM 821 O OD1 . ASP A 1 106 ? -41.296 28.778 21.377 1.00 11.84 ? 106 ASP A OD1 1 ATOM 822 O OD2 . ASP A 1 106 ? -40.232 28.892 19.463 1.00 10.91 ? 106 ASP A OD2 1 ATOM 823 N N . GLY A 1 107 ? -42.404 32.909 19.192 1.00 9.80 ? 107 GLY A N 1 ATOM 824 C CA . GLY A 1 107 ? -41.558 34.085 19.066 1.00 11.42 ? 107 GLY A CA 1 ATOM 825 C C . GLY A 1 107 ? -40.243 33.872 18.351 1.00 12.06 ? 107 GLY A C 1 ATOM 826 O O . GLY A 1 107 ? -39.290 34.621 18.560 1.00 13.06 ? 107 GLY A O 1 ATOM 827 N N . ALA A 1 108 ? -40.188 32.837 17.520 1.00 12.51 ? 108 ALA A N 1 ATOM 828 C CA . ALA A 1 108 ? -38.984 32.526 16.763 1.00 11.46 ? 108 ALA A CA 1 ATOM 829 C C . ALA A 1 108 ? -39.161 33.072 15.349 1.00 11.79 ? 108 ALA A C 1 ATOM 830 O O . ALA A 1 108 ? -39.784 32.428 14.498 1.00 10.74 ? 108 ALA A O 1 ATOM 831 C CB . ALA A 1 108 ? -38.759 31.020 16.741 1.00 9.13 ? 108 ALA A CB 1 ATOM 832 N N . ASN A 1 109 ? -38.645 34.275 15.105 1.00 10.69 ? 109 ASN A N 1 ATOM 833 C CA . ASN A 1 109 ? -38.770 34.871 13.779 1.00 10.20 ? 109 ASN A CA 1 ATOM 834 C C . ASN A 1 109 ? -38.041 34.107 12.686 1.00 9.88 ? 109 ASN A C 1 ATOM 835 O O . ASN A 1 109 ? -36.924 33.632 12.886 1.00 9.22 ? 109 ASN A O 1 ATOM 836 C CB . ASN A 1 109 ? -38.407 36.354 13.760 1.00 9.12 ? 109 ASN A CB 1 ATOM 837 C CG . ASN A 1 109 ? -37.093 36.680 14.452 1.00 11.32 ? 109 ASN A CG 1 ATOM 838 O OD1 . ASN A 1 109 ? -36.951 37.776 14.979 1.00 12.23 ? 109 ASN A OD1 1 ATOM 839 N ND2 . ASN A 1 109 ? -36.130 35.760 14.436 1.00 9.73 ? 109 ASN A ND2 1 ATOM 840 N N . GLY A 1 110 ? -38.727 33.941 11.559 1.00 10.61 ? 110 GLY A N 1 ATOM 841 C CA . GLY A 1 110 ? -38.178 33.196 10.445 1.00 9.58 ? 110 GLY A CA 1 ATOM 842 C C . GLY A 1 110 ? -38.498 31.717 10.591 1.00 10.27 ? 110 GLY A C 1 ATOM 843 O O . GLY A 1 110 ? -38.183 30.916 9.712 1.00 12.66 ? 110 GLY A O 1 ATOM 844 N N . VAL A 1 111 ? -39.146 31.362 11.699 1.00 9.50 ? 111 VAL A N 1 ATOM 845 C CA . VAL A 1 111 ? -39.535 29.986 11.986 1.00 11.06 ? 111 VAL A CA 1 ATOM 846 C C . VAL A 1 111 ? -41.044 29.943 12.256 1.00 11.10 ? 111 VAL A C 1 ATOM 847 O O . VAL A 1 111 ? -41.806 29.428 11.434 1.00 11.63 ? 111 VAL A O 1 ATOM 848 C CB . VAL A 1 111 ? -38.721 29.401 13.198 1.00 11.70 ? 111 VAL A CB 1 ATOM 849 C CG1 . VAL A 1 111 ? -39.139 27.983 13.522 1.00 12.24 ? 111 VAL A CG1 1 ATOM 850 C CG2 . VAL A 1 111 ? -37.230 29.440 12.914 1.00 13.81 ? 111 VAL A CG2 1 ATOM 851 N N . THR A 1 112 ? -41.470 30.541 13.372 1.00 10.71 ? 112 THR A N 1 ATOM 852 C CA . THR A 1 112 ? -42.879 30.543 13.774 1.00 10.54 ? 112 THR A CA 1 ATOM 853 C C . THR A 1 112 ? -43.661 31.804 13.434 1.00 10.97 ? 112 THR A C 1 ATOM 854 O O . THR A 1 112 ? -44.884 31.856 13.607 1.00 10.06 ? 112 THR A O 1 ATOM 855 C CB . THR A 1 112 ? -43.031 30.258 15.288 1.00 9.53 ? 112 THR A CB 1 ATOM 856 O OG1 . THR A 1 112 ? -42.458 31.330 16.050 1.00 9.61 ? 112 THR A OG1 1 ATOM 857 C CG2 . THR A 1 112 ? -42.340 28.947 15.657 1.00 7.79 ? 112 THR A CG2 1 ATOM 858 N N . GLU A 1 113 ? -42.938 32.830 12.990 1.00 12.52 ? 113 GLU A N 1 ATOM 859 C CA . GLU A 1 113 ? -43.524 34.123 12.639 1.00 12.30 ? 113 GLU A CA 1 ATOM 860 C C . GLU A 1 113 ? -42.528 35.024 11.949 1.00 11.60 ? 113 GLU A C 1 ATOM 861 O O . GLU A 1 113 ? -41.339 34.718 11.878 1.00 10.52 ? 113 GLU A O 1 ATOM 862 C CB . GLU A 1 113 ? -44.014 34.854 13.894 1.00 14.11 ? 113 GLU A CB 1 ATOM 863 C CG . GLU A 1 113 ? -42.925 35.121 14.920 1.00 17.47 ? 113 GLU A CG 1 ATOM 864 C CD . GLU A 1 113 ? -43.483 35.166 16.298 1.00 20.95 ? 113 GLU A CD 1 ATOM 865 O OE1 . GLU A 1 113 ? -43.889 34.093 16.813 1.00 23.56 ? 113 GLU A OE1 1 ATOM 866 O OE2 . GLU A 1 113 ? -43.522 36.270 16.862 1.00 19.42 ? 113 GLU A OE2 1 ATOM 867 N N . CYS A 1 114 ? -43.045 36.114 11.394 1.00 10.84 ? 114 CYS A N 1 ATOM 868 C CA . CYS A 1 114 ? -42.210 37.131 10.778 1.00 10.84 ? 114 CYS A CA 1 ATOM 869 C C . CYS A 1 114 ? -41.987 38.128 11.912 1.00 10.83 ? 114 CYS A C 1 ATOM 870 O O . CYS A 1 114 ? -42.775 38.160 12.867 1.00 10.39 ? 114 CYS A O 1 ATOM 871 C CB . CYS A 1 114 ? -42.951 37.836 9.651 1.00 10.63 ? 114 CYS A CB 1 ATOM 872 S SG . CYS A 1 114 ? -43.151 36.886 8.119 1.00 12.05 ? 114 CYS A SG 1 ATOM 873 N N . PRO A 1 115 ? -40.894 38.922 11.860 1.00 10.77 ? 115 PRO A N 1 ATOM 874 C CA . PRO A 1 115 ? -40.657 39.896 12.926 1.00 10.06 ? 115 PRO A CA 1 ATOM 875 C C . PRO A 1 115 ? -41.731 40.968 12.917 1.00 10.74 ? 115 PRO A C 1 ATOM 876 O O . PRO A 1 115 ? -42.326 41.259 11.873 1.00 8.47 ? 115 PRO A O 1 ATOM 877 C CB . PRO A 1 115 ? -39.321 40.518 12.535 1.00 10.71 ? 115 PRO A CB 1 ATOM 878 C CG . PRO A 1 115 ? -38.648 39.465 11.821 1.00 10.84 ? 115 PRO A CG 1 ATOM 879 C CD . PRO A 1 115 ? -39.723 38.858 10.973 1.00 8.71 ? 115 PRO A CD 1 ATOM 880 N N . ILE A 1 116 ? -42.022 41.490 14.101 1.00 9.42 ? 116 ILE A N 1 ATOM 881 C CA . ILE A 1 116 ? -42.992 42.559 14.260 1.00 11.23 ? 116 ILE A CA 1 ATOM 882 C C . ILE A 1 116 ? -42.262 43.805 13.728 1.00 10.46 ? 116 ILE A C 1 ATOM 883 O O . ILE A 1 116 ? -41.171 44.116 14.202 1.00 13.33 ? 116 ILE A O 1 ATOM 884 C CB . ILE A 1 116 ? -43.350 42.736 15.748 1.00 10.77 ? 116 ILE A CB 1 ATOM 885 C CG1 . ILE A 1 116 ? -43.938 41.439 16.307 1.00 11.71 ? 116 ILE A CG1 1 ATOM 886 C CG2 . ILE A 1 116 ? -44.331 43.854 15.914 1.00 11.36 ? 116 ILE A CG2 1 ATOM 887 C CD1 . ILE A 1 116 ? -43.890 41.336 17.821 1.00 12.21 ? 116 ILE A CD1 1 ATOM 888 N N . PRO A 1 117 ? -42.817 44.484 12.698 1.00 12.34 ? 117 PRO A N 1 ATOM 889 C CA . PRO A 1 117 ? -42.156 45.679 12.152 1.00 11.67 ? 117 PRO A CA 1 ATOM 890 C C . PRO A 1 117 ? -42.006 46.846 13.139 1.00 11.95 ? 117 PRO A C 1 ATOM 891 O O . PRO A 1 117 ? -42.786 46.964 14.083 1.00 11.12 ? 117 PRO A O 1 ATOM 892 C CB . PRO A 1 117 ? -43.049 46.042 10.954 1.00 12.50 ? 117 PRO A CB 1 ATOM 893 C CG . PRO A 1 117 ? -44.394 45.523 11.350 1.00 12.91 ? 117 PRO A CG 1 ATOM 894 C CD . PRO A 1 117 ? -44.041 44.181 11.928 1.00 12.76 ? 117 PRO A CD 1 ATOM 895 N N . PRO A 1 118 ? -40.955 47.678 12.977 1.00 12.68 ? 118 PRO A N 1 ATOM 896 C CA . PRO A 1 118 ? -40.742 48.821 13.868 1.00 13.23 ? 118 PRO A CA 1 ATOM 897 C C . PRO A 1 118 ? -41.721 49.954 13.579 1.00 13.52 ? 118 PRO A C 1 ATOM 898 O O . PRO A 1 118 ? -42.663 49.774 12.809 1.00 13.93 ? 118 PRO A O 1 ATOM 899 C CB . PRO A 1 118 ? -39.303 49.215 13.558 1.00 13.51 ? 118 PRO A CB 1 ATOM 900 C CG . PRO A 1 118 ? -39.193 48.919 12.152 1.00 14.30 ? 118 PRO A CG 1 ATOM 901 C CD . PRO A 1 118 ? -39.808 47.552 12.063 1.00 13.33 ? 118 PRO A CD 1 ATOM 902 N N . LYS A 1 119 ? -41.488 51.108 14.208 1.00 17.55 ? 119 LYS A N 1 ATOM 903 C CA . LYS A 1 119 ? -42.314 52.314 14.051 1.00 18.14 ? 119 LYS A CA 1 ATOM 904 C C . LYS A 1 119 ? -43.804 52.137 14.416 1.00 17.73 ? 119 LYS A C 1 ATOM 905 O O . LYS A 1 119 ? -44.681 52.783 13.833 1.00 18.17 ? 119 LYS A O 1 ATOM 906 C CB . LYS A 1 119 ? -42.148 52.916 12.637 1.00 20.79 ? 119 LYS A CB 1 ATOM 907 C CG . LYS A 1 119 ? -40.712 53.291 12.255 1.00 21.93 ? 119 LYS A CG 1 ATOM 908 C CD . LYS A 1 119 ? -40.624 53.685 10.779 1.00 26.88 ? 119 LYS A CD 1 ATOM 909 C CE . LYS A 1 119 ? -39.179 53.845 10.315 1.00 27.68 ? 119 LYS A CE 1 ATOM 910 N NZ . LYS A 1 119 ? -38.441 54.891 11.088 1.00 29.98 ? 119 LYS A NZ 1 ATOM 911 N N . GLY A 1 120 ? -44.077 51.241 15.365 1.00 15.43 ? 120 GLY A N 1 ATOM 912 C CA . GLY A 1 120 ? -45.444 51.025 15.814 1.00 14.82 ? 120 GLY A CA 1 ATOM 913 C C . GLY A 1 120 ? -46.109 49.693 15.531 1.00 14.82 ? 120 GLY A C 1 ATOM 914 O O . GLY A 1 120 ? -47.278 49.522 15.877 1.00 14.49 ? 120 GLY A O 1 ATOM 915 N N . GLY A 1 121 ? -45.386 48.751 14.920 1.00 13.47 ? 121 GLY A N 1 ATOM 916 C CA . GLY A 1 121 ? -45.952 47.438 14.626 1.00 12.85 ? 121 GLY A CA 1 ATOM 917 C C . GLY A 1 121 ? -46.305 46.675 15.894 1.00 12.26 ? 121 GLY A C 1 ATOM 918 O O . GLY A 1 121 ? -45.638 46.836 16.917 1.00 11.03 ? 121 GLY A O 1 ATOM 919 N N . GLN A 1 122 ? -47.359 45.867 15.844 1.00 11.43 ? 122 GLN A N 1 ATOM 920 C CA . GLN A 1 122 ? -47.768 45.104 17.016 1.00 13.17 ? 122 GLN A CA 1 ATOM 921 C C . GLN A 1 122 ? -48.276 43.701 16.748 1.00 11.94 ? 122 GLN A C 1 ATOM 922 O O . GLN A 1 122 ? -48.706 43.377 15.640 1.00 12.71 ? 122 GLN A O 1 ATOM 923 C CB . GLN A 1 122 ? -48.787 45.880 17.859 1.00 14.66 ? 122 GLN A CB 1 ATOM 924 C CG . GLN A 1 122 ? -50.172 46.014 17.261 1.00 18.16 ? 122 GLN A CG 1 ATOM 925 C CD . GLN A 1 122 ? -51.050 46.902 18.098 1.00 20.59 ? 122 GLN A CD 1 ATOM 926 O OE1 . GLN A 1 122 ? -51.835 46.430 18.925 1.00 20.27 ? 122 GLN A OE1 1 ATOM 927 N NE2 . GLN A 1 122 ? -50.912 48.204 17.901 1.00 22.82 ? 122 GLN A NE2 1 ATOM 928 N N . ARG A 1 123 ? -48.203 42.885 17.795 1.00 13.21 ? 123 ARG A N 1 ATOM 929 C CA . ARG A 1 123 ? -48.665 41.503 17.790 1.00 14.57 ? 123 ARG A CA 1 ATOM 930 C C . ARG A 1 123 ? -48.919 41.117 19.239 1.00 13.12 ? 123 ARG A C 1 ATOM 931 O O . ARG A 1 123 ? -48.155 41.473 20.135 1.00 13.87 ? 123 ARG A O 1 ATOM 932 C CB . ARG A 1 123 ? -47.621 40.560 17.177 1.00 15.97 ? 123 ARG A CB 1 ATOM 933 C CG . ARG A 1 123 ? -48.125 39.146 16.912 1.00 18.79 ? 123 ARG A CG 1 ATOM 934 C CD . ARG A 1 123 ? -47.418 38.124 17.774 1.00 19.63 ? 123 ARG A CD 1 ATOM 935 N NE . ARG A 1 123 ? -48.196 36.894 17.877 1.00 22.18 ? 123 ARG A NE 1 ATOM 936 C CZ . ARG A 1 123 ? -47.766 35.688 17.521 1.00 20.74 ? 123 ARG A CZ 1 ATOM 937 N NH1 . ARG A 1 123 ? -46.544 35.521 17.036 1.00 17.37 ? 123 ARG A NH1 1 ATOM 938 N NH2 . ARG A 1 123 ? -48.585 34.649 17.611 1.00 21.02 ? 123 ARG A NH2 1 ATOM 939 N N . THR A 1 124 ? -49.973 40.340 19.445 1.00 13.08 ? 124 THR A N 1 ATOM 940 C CA . THR A 1 124 ? -50.334 39.886 20.770 1.00 13.89 ? 124 THR A CA 1 ATOM 941 C C . THR A 1 124 ? -50.086 38.391 20.916 1.00 14.00 ? 124 THR A C 1 ATOM 942 O O . THR A 1 124 ? -50.704 37.574 20.224 1.00 15.35 ? 124 THR A O 1 ATOM 943 C CB . THR A 1 124 ? -51.803 40.266 21.108 1.00 13.82 ? 124 THR A CB 1 ATOM 944 O OG1 . THR A 1 124 ? -51.939 41.693 21.087 1.00 13.94 ? 124 THR A OG1 1 ATOM 945 C CG2 . THR A 1 124 ? -52.191 39.783 22.492 1.00 14.65 ? 124 THR A CG2 1 ATOM 946 N N . TYR A 1 125 ? -49.146 38.055 21.800 1.00 12.79 ? 125 TYR A N 1 ATOM 947 C CA . TYR A 1 125 ? -48.807 36.665 22.095 1.00 13.11 ? 125 TYR A CA 1 ATOM 948 C C . TYR A 1 125 ? -49.743 36.191 23.183 1.00 14.21 ? 125 TYR A C 1 ATOM 949 O O . TYR A 1 125 ? -50.089 36.953 24.091 1.00 12.49 ? 125 TYR A O 1 ATOM 950 C CB . TYR A 1 125 ? -47.380 36.531 22.608 1.00 12.21 ? 125 TYR A CB 1 ATOM 951 C CG . TYR A 1 125 ? -46.314 36.871 21.607 1.00 10.73 ? 125 TYR A CG 1 ATOM 952 C CD1 . TYR A 1 125 ? -45.843 38.191 21.481 1.00 11.26 ? 125 TYR A CD1 1 ATOM 953 C CD2 . TYR A 1 125 ? -45.726 35.870 20.811 1.00 12.26 ? 125 TYR A CD2 1 ATOM 954 C CE1 . TYR A 1 125 ? -44.802 38.511 20.584 1.00 9.50 ? 125 TYR A CE1 1 ATOM 955 C CE2 . TYR A 1 125 ? -44.684 36.176 19.912 1.00 11.87 ? 125 TYR A CE2 1 ATOM 956 C CZ . TYR A 1 125 ? -44.231 37.502 19.810 1.00 11.47 ? 125 TYR A CZ 1 ATOM 957 O OH . TYR A 1 125 ? -43.220 37.823 18.954 1.00 13.10 ? 125 TYR A OH 1 ATOM 958 N N . ARG A 1 126 ? -50.141 34.929 23.086 1.00 14.39 ? 126 ARG A N 1 ATOM 959 C CA . ARG A 1 126 ? -51.044 34.333 24.054 1.00 16.20 ? 126 ARG A CA 1 ATOM 960 C C . ARG A 1 126 ? -50.615 32.889 24.260 1.00 15.90 ? 126 ARG A C 1 ATOM 961 O O . ARG A 1 126 ? -50.484 32.126 23.297 1.00 15.27 ? 126 ARG A O 1 ATOM 962 C CB . ARG A 1 126 ? -52.490 34.409 23.547 1.00 16.93 ? 126 ARG A CB 1 ATOM 963 C CG . ARG A 1 126 ? -53.535 34.347 24.645 1.00 20.30 ? 126 ARG A CG 1 ATOM 964 C CD . ARG A 1 126 ? -54.940 34.228 24.087 1.00 21.87 ? 126 ARG A CD 1 ATOM 965 N NE . ARG A 1 126 ? -55.937 34.078 25.148 1.00 25.59 ? 126 ARG A NE 1 ATOM 966 C CZ . ARG A 1 126 ? -56.522 32.929 25.491 1.00 27.48 ? 126 ARG A CZ 1 ATOM 967 N NH1 . ARG A 1 126 ? -56.226 31.799 24.855 1.00 28.02 ? 126 ARG A NH1 1 ATOM 968 N NH2 . ARG A 1 126 ? -57.374 32.904 26.509 1.00 24.73 ? 126 ARG A NH2 1 ATOM 969 N N . TRP A 1 127 ? -50.323 32.545 25.510 1.00 14.55 ? 127 TRP A N 1 ATOM 970 C CA . TRP A 1 127 ? -49.905 31.191 25.854 1.00 15.33 ? 127 TRP A CA 1 ATOM 971 C C . TRP A 1 127 ? -50.406 30.730 27.207 1.00 15.55 ? 127 TRP A C 1 ATOM 972 O O . TRP A 1 127 ? -50.535 31.520 28.147 1.00 16.40 ? 127 TRP A O 1 ATOM 973 C CB . TRP A 1 127 ? -48.376 31.011 25.748 1.00 15.66 ? 127 TRP A CB 1 ATOM 974 C CG . TRP A 1 127 ? -47.508 32.063 26.415 1.00 15.66 ? 127 TRP A CG 1 ATOM 975 C CD1 . TRP A 1 127 ? -46.986 33.184 25.825 1.00 16.60 ? 127 TRP A CD1 1 ATOM 976 C CD2 . TRP A 1 127 ? -46.998 32.043 27.758 1.00 16.34 ? 127 TRP A CD2 1 ATOM 977 N NE1 . TRP A 1 127 ? -46.175 33.857 26.710 1.00 16.30 ? 127 TRP A NE1 1 ATOM 978 C CE2 . TRP A 1 127 ? -46.157 33.183 27.902 1.00 16.31 ? 127 TRP A CE2 1 ATOM 979 C CE3 . TRP A 1 127 ? -47.162 31.172 28.857 1.00 15.73 ? 127 TRP A CE3 1 ATOM 980 C CZ2 . TRP A 1 127 ? -45.473 33.478 29.108 1.00 16.78 ? 127 TRP A CZ2 1 ATOM 981 C CZ3 . TRP A 1 127 ? -46.482 31.461 30.067 1.00 16.51 ? 127 TRP A CZ3 1 ATOM 982 C CH2 . TRP A 1 127 ? -45.646 32.611 30.175 1.00 15.81 ? 127 TRP A CH2 1 ATOM 983 N N . ARG A 1 128 ? -50.645 29.428 27.295 1.00 13.85 ? 128 ARG A N 1 ATOM 984 C CA . ARG A 1 128 ? -51.131 28.793 28.506 1.00 15.15 ? 128 ARG A CA 1 ATOM 985 C C . ARG A 1 128 ? -49.951 28.386 29.388 1.00 15.05 ? 128 ARG A C 1 ATOM 986 O O . ARG A 1 128 ? -48.970 27.808 28.905 1.00 14.06 ? 128 ARG A O 1 ATOM 987 C CB . ARG A 1 128 ? -51.973 27.570 28.130 1.00 15.28 ? 128 ARG A CB 1 ATOM 988 C CG . ARG A 1 128 ? -52.688 26.887 29.280 1.00 16.55 ? 128 ARG A CG 1 ATOM 989 C CD . ARG A 1 128 ? -53.901 27.647 29.787 1.00 16.70 ? 128 ARG A CD 1 ATOM 990 N NE . ARG A 1 128 ? -54.593 26.871 30.816 1.00 18.19 ? 128 ARG A NE 1 ATOM 991 C CZ . ARG A 1 128 ? -55.404 25.840 30.583 1.00 16.89 ? 128 ARG A CZ 1 ATOM 992 N NH1 . ARG A 1 128 ? -55.660 25.438 29.341 1.00 15.86 ? 128 ARG A NH1 1 ATOM 993 N NH2 . ARG A 1 128 ? -55.914 25.166 31.605 1.00 17.42 ? 128 ARG A NH2 1 ATOM 994 N N . ALA A 1 129 ? -50.059 28.709 30.677 1.00 14.12 ? 129 ALA A N 1 ATOM 995 C CA . ALA A 1 129 ? -49.034 28.383 31.666 1.00 12.96 ? 129 ALA A CA 1 ATOM 996 C C . ALA A 1 129 ? -49.200 26.934 32.139 1.00 13.04 ? 129 ALA A C 1 ATOM 997 O O . ALA A 1 129 ? -49.755 26.673 33.208 1.00 14.19 ? 129 ALA A O 1 ATOM 998 C CB . ALA A 1 129 ? -49.116 29.358 32.837 1.00 13.84 ? 129 ALA A CB 1 ATOM 999 N N . ARG A 1 130 ? -48.728 26.001 31.309 1.00 11.99 ? 130 ARG A N 1 ATOM 1000 C CA . ARG A 1 130 ? -48.805 24.560 31.579 1.00 12.97 ? 130 ARG A CA 1 ATOM 1001 C C . ARG A 1 130 ? -47.608 24.026 32.356 1.00 13.35 ? 130 ARG A C 1 ATOM 1002 O O . ARG A 1 130 ? -47.436 22.808 32.509 1.00 11.68 ? 130 ARG A O 1 ATOM 1003 C CB . ARG A 1 130 ? -48.939 23.778 30.268 1.00 13.72 ? 130 ARG A CB 1 ATOM 1004 C CG . ARG A 1 130 ? -50.163 24.132 29.472 1.00 14.37 ? 130 ARG A CG 1 ATOM 1005 C CD . ARG A 1 130 ? -50.396 23.168 28.338 1.00 18.01 ? 130 ARG A CD 1 ATOM 1006 N NE . ARG A 1 130 ? -51.529 23.562 27.498 1.00 18.71 ? 130 ARG A NE 1 ATOM 1007 C CZ . ARG A 1 130 ? -52.798 23.225 27.721 1.00 20.39 ? 130 ARG A CZ 1 ATOM 1008 N NH1 . ARG A 1 130 ? -53.130 22.485 28.772 1.00 20.13 ? 130 ARG A NH1 1 ATOM 1009 N NH2 . ARG A 1 130 ? -53.738 23.603 26.866 1.00 19.31 ? 130 ARG A NH2 1 ATOM 1010 N N . GLN A 1 131 ? -46.780 24.943 32.840 1.00 12.35 ? 131 GLN A N 1 ATOM 1011 C CA . GLN A 1 131 ? -45.595 24.574 33.594 1.00 13.81 ? 131 GLN A CA 1 ATOM 1012 C C . GLN A 1 131 ? -45.330 25.670 34.596 1.00 13.81 ? 131 GLN A C 1 ATOM 1013 O O . GLN A 1 131 ? -45.453 26.856 34.278 1.00 16.92 ? 131 GLN A O 1 ATOM 1014 C CB . GLN A 1 131 ? -44.404 24.412 32.646 1.00 15.90 ? 131 GLN A CB 1 ATOM 1015 C CG . GLN A 1 131 ? -43.253 23.593 33.211 1.00 22.10 ? 131 GLN A CG 1 ATOM 1016 C CD . GLN A 1 131 ? -42.233 23.176 32.163 1.00 24.61 ? 131 GLN A CD 1 ATOM 1017 O OE1 . GLN A 1 131 ? -42.278 23.623 31.016 1.00 30.21 ? 131 GLN A OE1 1 ATOM 1018 N NE2 . GLN A 1 131 ? -41.292 22.328 32.563 1.00 19.26 ? 131 GLN A NE2 1 ATOM 1019 N N . TYR A 1 132 ? -44.989 25.267 35.813 1.00 11.82 ? 132 TYR A N 1 ATOM 1020 C CA . TYR A 1 132 ? -44.701 26.210 36.875 1.00 10.74 ? 132 TYR A CA 1 ATOM 1021 C C . TYR A 1 132 ? -43.215 26.269 37.204 1.00 9.72 ? 132 TYR A C 1 ATOM 1022 O O . TYR A 1 132 ? -42.513 25.252 37.176 1.00 7.59 ? 132 TYR A O 1 ATOM 1023 C CB . TYR A 1 132 ? -45.541 25.910 38.124 1.00 12.60 ? 132 TYR A CB 1 ATOM 1024 C CG . TYR A 1 132 ? -45.429 24.493 38.636 1.00 11.04 ? 132 TYR A CG 1 ATOM 1025 C CD1 . TYR A 1 132 ? -46.195 23.461 38.067 1.00 12.71 ? 132 TYR A CD1 1 ATOM 1026 C CD2 . TYR A 1 132 ? -44.514 24.163 39.652 1.00 10.50 ? 132 TYR A CD2 1 ATOM 1027 C CE1 . TYR A 1 132 ? -46.051 22.119 38.491 1.00 13.13 ? 132 TYR A CE1 1 ATOM 1028 C CE2 . TYR A 1 132 ? -44.359 22.830 40.081 1.00 9.21 ? 132 TYR A CE2 1 ATOM 1029 C CZ . TYR A 1 132 ? -45.123 21.816 39.497 1.00 8.74 ? 132 TYR A CZ 1 ATOM 1030 O OH . TYR A 1 132 ? -44.943 20.513 39.887 1.00 9.46 ? 132 TYR A OH 1 ATOM 1031 N N . GLY A 1 133 ? -42.756 27.472 37.522 1.00 8.65 ? 133 GLY A N 1 ATOM 1032 C CA . GLY A 1 133 ? -41.364 27.664 37.861 1.00 9.17 ? 133 GLY A CA 1 ATOM 1033 C C . GLY A 1 133 ? -40.837 28.975 37.342 1.00 9.65 ? 133 GLY A C 1 ATOM 1034 O O . GLY A 1 133 ? -41.597 29.914 37.098 1.00 10.87 ? 133 GLY A O 1 ATOM 1035 N N . THR A 1 134 ? -39.532 28.994 37.104 1.00 9.62 ? 134 THR A N 1 ATOM 1036 C CA . THR A 1 134 ? -38.844 30.177 36.638 1.00 8.90 ? 134 THR A CA 1 ATOM 1037 C C . THR A 1 134 ? -38.333 30.037 35.219 1.00 9.70 ? 134 THR A C 1 ATOM 1038 O O . THR A 1 134 ? -37.560 29.135 34.898 1.00 10.22 ? 134 THR A O 1 ATOM 1039 C CB . THR A 1 134 ? -37.670 30.509 37.559 1.00 9.79 ? 134 THR A CB 1 ATOM 1040 O OG1 . THR A 1 134 ? -38.105 30.398 38.919 1.00 7.12 ? 134 THR A OG1 1 ATOM 1041 C CG2 . THR A 1 134 ? -37.172 31.931 37.312 1.00 6.40 ? 134 THR A CG2 1 ATOM 1042 N N . SER A 1 135 ? -38.771 30.969 34.387 1.00 10.62 ? 135 SER A N 1 ATOM 1043 C CA . SER A 1 135 ? -38.370 31.024 33.000 1.00 11.78 ? 135 SER A CA 1 ATOM 1044 C C . SER A 1 135 ? -38.082 32.473 32.664 1.00 10.61 ? 135 SER A C 1 ATOM 1045 O O . SER A 1 135 ? -38.078 33.338 33.549 1.00 11.91 ? 135 SER A O 1 ATOM 1046 C CB . SER A 1 135 ? -39.465 30.443 32.106 1.00 11.30 ? 135 SER A CB 1 ATOM 1047 O OG . SER A 1 135 ? -39.435 29.029 32.152 1.00 13.55 ? 135 SER A OG 1 ATOM 1048 N N . TRP A 1 136 ? -37.830 32.737 31.390 1.00 10.58 ? 136 TRP A N 1 ATOM 1049 C CA . TRP A 1 136 ? -37.543 34.084 30.942 1.00 10.78 ? 136 TRP A CA 1 ATOM 1050 C C . TRP A 1 136 ? -37.964 34.280 29.506 1.00 11.58 ? 136 TRP A C 1 ATOM 1051 O O . TRP A 1 136 ? -38.376 33.333 28.837 1.00 11.01 ? 136 TRP A O 1 ATOM 1052 C CB . TRP A 1 136 ? -36.053 34.431 31.135 1.00 10.01 ? 136 TRP A CB 1 ATOM 1053 C CG . TRP A 1 136 ? -35.043 33.627 30.342 1.00 9.33 ? 136 TRP A CG 1 ATOM 1054 C CD1 . TRP A 1 136 ? -34.856 32.272 30.369 1.00 10.43 ? 136 TRP A CD1 1 ATOM 1055 C CD2 . TRP A 1 136 ? -34.031 34.154 29.477 1.00 8.13 ? 136 TRP A CD2 1 ATOM 1056 N NE1 . TRP A 1 136 ? -33.783 31.921 29.581 1.00 9.71 ? 136 TRP A NE1 1 ATOM 1057 C CE2 . TRP A 1 136 ? -33.252 33.056 29.023 1.00 9.37 ? 136 TRP A CE2 1 ATOM 1058 C CE3 . TRP A 1 136 ? -33.695 35.453 29.046 1.00 6.23 ? 136 TRP A CE3 1 ATOM 1059 C CZ2 . TRP A 1 136 ? -32.147 33.215 28.156 1.00 5.40 ? 136 TRP A CZ2 1 ATOM 1060 C CZ3 . TRP A 1 136 ? -32.582 35.619 28.175 1.00 6.75 ? 136 TRP A CZ3 1 ATOM 1061 C CH2 . TRP A 1 136 ? -31.825 34.498 27.746 1.00 8.82 ? 136 TRP A CH2 1 ATOM 1062 N N . TYR A 1 137 ? -37.975 35.538 29.088 1.00 11.17 ? 137 TYR A N 1 ATOM 1063 C CA . TYR A 1 137 ? -38.313 35.874 27.725 1.00 11.10 ? 137 TYR A CA 1 ATOM 1064 C C . TYR A 1 137 ? -37.237 36.764 27.150 1.00 9.71 ? 137 TYR A C 1 ATOM 1065 O O . TYR A 1 137 ? -36.548 37.468 27.889 1.00 9.56 ? 137 TYR A O 1 ATOM 1066 C CB . TYR A 1 137 ? -39.700 36.522 27.609 1.00 10.47 ? 137 TYR A CB 1 ATOM 1067 C CG . TYR A 1 137 ? -39.917 37.799 28.387 1.00 11.06 ? 137 TYR A CG 1 ATOM 1068 C CD1 . TYR A 1 137 ? -39.524 39.047 27.858 1.00 9.97 ? 137 TYR A CD1 1 ATOM 1069 C CD2 . TYR A 1 137 ? -40.518 37.770 29.658 1.00 12.44 ? 137 TYR A CD2 1 ATOM 1070 C CE1 . TYR A 1 137 ? -39.719 40.236 28.578 1.00 9.60 ? 137 TYR A CE1 1 ATOM 1071 C CE2 . TYR A 1 137 ? -40.728 38.963 30.390 1.00 10.56 ? 137 TYR A CE2 1 ATOM 1072 C CZ . TYR A 1 137 ? -40.321 40.184 29.836 1.00 9.05 ? 137 TYR A CZ 1 ATOM 1073 O OH . TYR A 1 137 ? -40.516 41.344 30.520 1.00 9.36 ? 137 TYR A OH 1 ATOM 1074 N N . HIS A 1 138 ? -37.128 36.746 25.827 1.00 8.70 ? 138 HIS A N 1 ATOM 1075 C CA . HIS A 1 138 ? -36.145 37.548 25.125 1.00 9.55 ? 138 HIS A CA 1 ATOM 1076 C C . HIS A 1 138 ? -36.452 37.631 23.641 1.00 8.74 ? 138 HIS A C 1 ATOM 1077 O O . HIS A 1 138 ? -37.184 36.803 23.097 1.00 8.33 ? 138 HIS A O 1 ATOM 1078 C CB . HIS A 1 138 ? -34.729 36.967 25.338 1.00 10.08 ? 138 HIS A CB 1 ATOM 1079 C CG . HIS A 1 138 ? -34.543 35.570 24.820 1.00 10.37 ? 138 HIS A CG 1 ATOM 1080 N ND1 . HIS A 1 138 ? -34.263 35.302 23.499 1.00 11.14 ? 138 HIS A ND1 1 ATOM 1081 C CD2 . HIS A 1 138 ? -34.547 34.373 25.454 1.00 9.46 ? 138 HIS A CD2 1 ATOM 1082 C CE1 . HIS A 1 138 ? -34.095 34.003 23.342 1.00 11.29 ? 138 HIS A CE1 1 ATOM 1083 N NE2 . HIS A 1 138 ? -34.260 33.413 24.514 1.00 12.29 ? 138 HIS A NE2 1 ATOM 1084 N N . SER A 1 139 ? -35.849 38.614 22.980 1.00 9.30 ? 139 SER A N 1 ATOM 1085 C CA . SER A 1 139 ? -36.010 38.766 21.544 1.00 10.07 ? 139 SER A CA 1 ATOM 1086 C C . SER A 1 139 ? -35.214 37.665 20.857 1.00 9.53 ? 139 SER A C 1 ATOM 1087 O O . SER A 1 139 ? -34.200 37.199 21.395 1.00 8.27 ? 139 SER A O 1 ATOM 1088 C CB . SER A 1 139 ? -35.479 40.115 21.077 1.00 8.50 ? 139 SER A CB 1 ATOM 1089 O OG . SER A 1 139 ? -35.519 40.221 19.665 1.00 9.71 ? 139 SER A OG 1 ATOM 1090 N N . HIS A 1 140 ? -35.718 37.210 19.714 1.00 10.69 ? 140 HIS A N 1 ATOM 1091 C CA . HIS A 1 140 ? -35.025 36.203 18.919 1.00 10.70 ? 140 HIS A CA 1 ATOM 1092 C C . HIS A 1 140 ? -34.613 36.823 17.578 1.00 11.19 ? 140 HIS A C 1 ATOM 1093 O O . HIS A 1 140 ? -34.228 36.112 16.644 1.00 10.22 ? 140 HIS A O 1 ATOM 1094 C CB . HIS A 1 140 ? -35.884 34.946 18.726 1.00 12.55 ? 140 HIS A CB 1 ATOM 1095 C CG . HIS A 1 140 ? -35.161 33.670 19.045 1.00 13.70 ? 140 HIS A CG 1 ATOM 1096 N ND1 . HIS A 1 140 ? -33.921 33.364 18.526 1.00 13.20 ? 140 HIS A ND1 1 ATOM 1097 C CD2 . HIS A 1 140 ? -35.495 32.634 19.849 1.00 12.90 ? 140 HIS A CD2 1 ATOM 1098 C CE1 . HIS A 1 140 ? -33.523 32.196 18.999 1.00 13.66 ? 140 HIS A CE1 1 ATOM 1099 N NE2 . HIS A 1 140 ? -34.459 31.731 19.806 1.00 14.77 ? 140 HIS A NE2 1 ATOM 1100 N N . PHE A 1 141 ? -34.667 38.159 17.511 1.00 10.10 ? 141 PHE A N 1 ATOM 1101 C CA . PHE A 1 141 ? -34.285 38.922 16.315 1.00 10.52 ? 141 PHE A CA 1 ATOM 1102 C C . PHE A 1 141 ? -32.782 39.124 16.400 1.00 10.68 ? 141 PHE A C 1 ATOM 1103 O O . PHE A 1 141 ? -32.311 40.107 16.982 1.00 10.29 ? 141 PHE A O 1 ATOM 1104 C CB . PHE A 1 141 ? -35.023 40.276 16.281 1.00 11.02 ? 141 PHE A CB 1 ATOM 1105 C CG . PHE A 1 141 ? -34.837 41.052 14.999 1.00 10.24 ? 141 PHE A CG 1 ATOM 1106 C CD1 . PHE A 1 141 ? -35.682 40.822 13.903 1.00 9.96 ? 141 PHE A CD1 1 ATOM 1107 C CD2 . PHE A 1 141 ? -33.847 42.051 14.894 1.00 9.70 ? 141 PHE A CD2 1 ATOM 1108 C CE1 . PHE A 1 141 ? -35.554 41.583 12.711 1.00 10.83 ? 141 PHE A CE1 1 ATOM 1109 C CE2 . PHE A 1 141 ? -33.704 42.817 13.711 1.00 10.47 ? 141 PHE A CE2 1 ATOM 1110 C CZ . PHE A 1 141 ? -34.562 42.587 12.618 1.00 10.96 ? 141 PHE A CZ 1 ATOM 1111 N N . SER A 1 142 ? -32.033 38.203 15.792 1.00 9.72 ? 142 SER A N 1 ATOM 1112 C CA . SER A 1 142 ? -30.570 38.206 15.835 1.00 10.59 ? 142 SER A CA 1 ATOM 1113 C C . SER A 1 142 ? -30.150 38.208 17.316 1.00 10.23 ? 142 SER A C 1 ATOM 1114 O O . SER A 1 142 ? -30.746 37.473 18.114 1.00 8.72 ? 142 SER A O 1 ATOM 1115 C CB . SER A 1 142 ? -29.980 39.370 15.021 1.00 12.61 ? 142 SER A CB 1 ATOM 1116 O OG . SER A 1 142 ? -30.256 39.177 13.642 1.00 14.24 ? 142 SER A OG 1 ATOM 1117 N N . ALA A 1 143 ? -29.229 39.085 17.704 1.00 9.12 ? 143 ALA A N 1 ATOM 1118 C CA . ALA A 1 143 ? -28.782 39.147 19.090 1.00 8.83 ? 143 ALA A CA 1 ATOM 1119 C C . ALA A 1 143 ? -29.375 40.357 19.807 1.00 9.30 ? 143 ALA A C 1 ATOM 1120 O O . ALA A 1 143 ? -28.832 40.808 20.815 1.00 10.16 ? 143 ALA A O 1 ATOM 1121 C CB . ALA A 1 143 ? -27.264 39.185 19.142 1.00 6.63 ? 143 ALA A CB 1 ATOM 1122 N N . GLN A 1 144 ? -30.537 40.815 19.335 1.00 10.33 ? 144 GLN A N 1 ATOM 1123 C CA . GLN A 1 144 ? -31.242 41.989 19.876 1.00 9.84 ? 144 GLN A CA 1 ATOM 1124 C C . GLN A 1 144 ? -31.466 41.988 21.390 1.00 11.55 ? 144 GLN A C 1 ATOM 1125 O O . GLN A 1 144 ? -31.491 43.058 22.011 1.00 11.18 ? 144 GLN A O 1 ATOM 1126 C CB . GLN A 1 144 ? -32.578 42.173 19.153 1.00 8.72 ? 144 GLN A CB 1 ATOM 1127 C CG . GLN A 1 144 ? -33.288 43.501 19.393 1.00 9.40 ? 144 GLN A CG 1 ATOM 1128 C CD . GLN A 1 144 ? -34.649 43.537 18.742 1.00 11.76 ? 144 GLN A CD 1 ATOM 1129 O OE1 . GLN A 1 144 ? -34.828 44.133 17.688 1.00 11.19 ? 144 GLN A OE1 1 ATOM 1130 N NE2 . GLN A 1 144 ? -35.617 42.887 19.368 1.00 4.96 ? 144 GLN A NE2 1 ATOM 1131 N N . TYR A 1 145 ? -31.592 40.798 21.986 1.00 10.33 ? 145 TYR A N 1 ATOM 1132 C CA . TYR A 1 145 ? -31.793 40.704 23.432 1.00 10.54 ? 145 TYR A CA 1 ATOM 1133 C C . TYR A 1 145 ? -30.578 41.194 24.227 1.00 10.30 ? 145 TYR A C 1 ATOM 1134 O O . TYR A 1 145 ? -30.701 41.566 25.394 1.00 11.06 ? 145 TYR A O 1 ATOM 1135 C CB . TYR A 1 145 ? -32.286 39.308 23.850 1.00 8.09 ? 145 TYR A CB 1 ATOM 1136 C CG . TYR A 1 145 ? -31.279 38.200 24.123 1.00 10.11 ? 145 TYR A CG 1 ATOM 1137 C CD1 . TYR A 1 145 ? -30.686 38.052 25.403 1.00 10.91 ? 145 TYR A CD1 1 ATOM 1138 C CD2 . TYR A 1 145 ? -31.010 37.213 23.154 1.00 10.72 ? 145 TYR A CD2 1 ATOM 1139 C CE1 . TYR A 1 145 ? -29.856 36.945 25.717 1.00 9.74 ? 145 TYR A CE1 1 ATOM 1140 C CE2 . TYR A 1 145 ? -30.176 36.092 23.458 1.00 8.93 ? 145 TYR A CE2 1 ATOM 1141 C CZ . TYR A 1 145 ? -29.610 35.973 24.742 1.00 9.60 ? 145 TYR A CZ 1 ATOM 1142 O OH . TYR A 1 145 ? -28.807 34.902 25.055 1.00 9.46 ? 145 TYR A OH 1 ATOM 1143 N N . GLY A 1 146 ? -29.429 41.246 23.549 1.00 10.30 ? 146 GLY A N 1 ATOM 1144 C CA . GLY A 1 146 ? -28.194 41.737 24.144 1.00 11.73 ? 146 GLY A CA 1 ATOM 1145 C C . GLY A 1 146 ? -28.216 43.242 24.369 1.00 13.19 ? 146 GLY A C 1 ATOM 1146 O O . GLY A 1 146 ? -27.349 43.785 25.060 1.00 12.17 ? 146 GLY A O 1 ATOM 1147 N N . ASN A 1 147 ? -29.220 43.899 23.780 1.00 11.10 ? 147 ASN A N 1 ATOM 1148 C CA . ASN A 1 147 ? -29.427 45.342 23.911 1.00 12.05 ? 147 ASN A CA 1 ATOM 1149 C C . ASN A 1 147 ? -30.436 45.671 25.018 1.00 11.63 ? 147 ASN A C 1 ATOM 1150 O O . ASN A 1 147 ? -30.667 46.846 25.317 1.00 12.74 ? 147 ASN A O 1 ATOM 1151 C CB . ASN A 1 147 ? -29.903 45.946 22.585 1.00 11.32 ? 147 ASN A CB 1 ATOM 1152 C CG . ASN A 1 147 ? -28.821 45.989 21.534 1.00 11.34 ? 147 ASN A CG 1 ATOM 1153 O OD1 . ASN A 1 147 ? -27.633 46.076 21.848 1.00 11.75 ? 147 ASN A OD1 1 ATOM 1154 N ND2 . ASN A 1 147 ? -29.225 45.941 20.270 1.00 12.45 ? 147 ASN A ND2 1 ATOM 1155 N N . GLY A 1 148 ? -31.076 44.644 25.579 1.00 11.17 ? 148 GLY A N 1 ATOM 1156 C CA . GLY A 1 148 ? -32.025 44.867 26.661 1.00 10.53 ? 148 GLY A CA 1 ATOM 1157 C C . GLY A 1 148 ? -33.434 44.326 26.517 1.00 11.54 ? 148 GLY A C 1 ATOM 1158 O O . GLY A 1 148 ? -34.235 44.479 27.439 1.00 11.26 ? 148 GLY A O 1 ATOM 1159 N N . VAL A 1 149 ? -33.755 43.699 25.385 1.00 11.78 ? 149 VAL A N 1 ATOM 1160 C CA . VAL A 1 149 ? -35.097 43.138 25.187 1.00 12.00 ? 149 VAL A CA 1 ATOM 1161 C C . VAL A 1 149 ? -35.127 41.761 25.868 1.00 12.11 ? 149 VAL A C 1 ATOM 1162 O O . VAL A 1 149 ? -35.079 40.712 25.221 1.00 11.19 ? 149 VAL A O 1 ATOM 1163 C CB . VAL A 1 149 ? -35.486 43.043 23.684 1.00 12.27 ? 149 VAL A CB 1 ATOM 1164 C CG1 . VAL A 1 149 ? -36.966 42.730 23.545 1.00 10.68 ? 149 VAL A CG1 1 ATOM 1165 C CG2 . VAL A 1 149 ? -35.182 44.335 22.959 1.00 11.58 ? 149 VAL A CG2 1 ATOM 1166 N N . VAL A 1 150 ? -35.120 41.814 27.198 1.00 13.58 ? 150 VAL A N 1 ATOM 1167 C CA . VAL A 1 150 ? -35.114 40.653 28.084 1.00 13.66 ? 150 VAL A CA 1 ATOM 1168 C C . VAL A 1 150 ? -36.010 40.888 29.284 1.00 12.99 ? 150 VAL A C 1 ATOM 1169 O O . VAL A 1 150 ? -36.349 42.026 29.604 1.00 13.41 ? 150 VAL A O 1 ATOM 1170 C CB . VAL A 1 150 ? -33.692 40.345 28.668 1.00 15.06 ? 150 VAL A CB 1 ATOM 1171 C CG1 . VAL A 1 150 ? -32.876 39.564 27.700 1.00 17.93 ? 150 VAL A CG1 1 ATOM 1172 C CG2 . VAL A 1 150 ? -32.956 41.623 29.066 1.00 16.63 ? 150 VAL A CG2 1 ATOM 1173 N N . GLY A 1 151 ? -36.339 39.798 29.967 1.00 14.04 ? 151 GLY A N 1 ATOM 1174 C CA . GLY A 1 151 ? -37.160 39.868 31.160 1.00 13.54 ? 151 GLY A CA 1 ATOM 1175 C C . GLY A 1 151 ? -37.402 38.491 31.721 1.00 12.30 ? 151 GLY A C 1 ATOM 1176 O O . GLY A 1 151 ? -37.059 37.498 31.089 1.00 12.42 ? 151 GLY A O 1 ATOM 1177 N N . THR A 1 152 ? -38.086 38.439 32.861 1.00 12.29 ? 152 THR A N 1 ATOM 1178 C CA . THR A 1 152 ? -38.348 37.185 33.562 1.00 10.92 ? 152 THR A CA 1 ATOM 1179 C C . THR A 1 152 ? -39.804 36.726 33.613 1.00 11.66 ? 152 THR A C 1 ATOM 1180 O O . THR A 1 152 ? -40.731 37.522 33.451 1.00 12.56 ? 152 THR A O 1 ATOM 1181 C CB . THR A 1 152 ? -37.834 37.263 35.014 1.00 10.19 ? 152 THR A CB 1 ATOM 1182 O OG1 . THR A 1 152 ? -38.594 38.239 35.736 1.00 10.19 ? 152 THR A OG1 1 ATOM 1183 C CG2 . THR A 1 152 ? -36.354 37.651 35.064 1.00 9.61 ? 152 THR A CG2 1 ATOM 1184 N N . ILE A 1 153 ? -39.981 35.425 33.841 1.00 11.03 ? 153 ILE A N 1 ATOM 1185 C CA . ILE A 1 153 ? -41.296 34.799 33.956 1.00 11.32 ? 153 ILE A CA 1 ATOM 1186 C C . ILE A 1 153 ? -41.309 33.974 35.246 1.00 11.79 ? 153 ILE A C 1 ATOM 1187 O O . ILE A 1 153 ? -40.416 33.157 35.482 1.00 12.18 ? 153 ILE A O 1 ATOM 1188 C CB . ILE A 1 153 ? -41.622 33.834 32.749 1.00 9.94 ? 153 ILE A CB 1 ATOM 1189 C CG1 . ILE A 1 153 ? -41.638 34.582 31.414 1.00 9.76 ? 153 ILE A CG1 1 ATOM 1190 C CG2 . ILE A 1 153 ? -42.975 33.146 32.954 1.00 10.03 ? 153 ILE A CG2 1 ATOM 1191 C CD1 . ILE A 1 153 ? -41.671 33.684 30.173 1.00 9.31 ? 153 ILE A CD1 1 ATOM 1192 N N . GLN A 1 154 ? -42.323 34.208 36.072 1.00 11.42 ? 154 GLN A N 1 ATOM 1193 C CA . GLN A 1 154 ? -42.503 33.456 37.306 1.00 12.20 ? 154 GLN A CA 1 ATOM 1194 C C . GLN A 1 154 ? -43.927 32.922 37.317 1.00 11.33 ? 154 GLN A C 1 ATOM 1195 O O . GLN A 1 154 ? -44.881 33.679 37.506 1.00 10.77 ? 154 GLN A O 1 ATOM 1196 C CB . GLN A 1 154 ? -42.247 34.326 38.544 1.00 13.24 ? 154 GLN A CB 1 ATOM 1197 C CG . GLN A 1 154 ? -42.481 33.588 39.879 1.00 12.20 ? 154 GLN A CG 1 ATOM 1198 C CD . GLN A 1 154 ? -42.121 34.414 41.093 1.00 13.44 ? 154 GLN A CD 1 ATOM 1199 O OE1 . GLN A 1 154 ? -41.156 35.179 41.076 1.00 15.85 ? 154 GLN A OE1 1 ATOM 1200 N NE2 . GLN A 1 154 ? -42.872 34.233 42.172 1.00 13.74 ? 154 GLN A NE2 1 ATOM 1201 N N . ILE A 1 155 ? -44.071 31.633 37.021 1.00 12.86 ? 155 ILE A N 1 ATOM 1202 C CA . ILE A 1 155 ? -45.387 31.006 37.049 1.00 11.43 ? 155 ILE A CA 1 ATOM 1203 C C . ILE A 1 155 ? -45.434 30.258 38.380 1.00 12.74 ? 155 ILE A C 1 ATOM 1204 O O . ILE A 1 155 ? -44.733 29.259 38.572 1.00 12.38 ? 155 ILE A O 1 ATOM 1205 C CB . ILE A 1 155 ? -45.627 30.036 35.855 1.00 12.54 ? 155 ILE A CB 1 ATOM 1206 C CG1 . ILE A 1 155 ? -45.507 30.759 34.503 1.00 12.18 ? 155 ILE A CG1 1 ATOM 1207 C CG2 . ILE A 1 155 ? -46.991 29.342 35.993 1.00 11.08 ? 155 ILE A CG2 1 ATOM 1208 C CD1 . ILE A 1 155 ? -46.505 31.904 34.256 1.00 11.52 ? 155 ILE A CD1 1 ATOM 1209 N N . ASN A 1 156 ? -46.223 30.786 39.314 1.00 12.84 ? 156 ASN A N 1 ATOM 1210 C CA . ASN A 1 156 ? -46.353 30.184 40.637 1.00 13.57 ? 156 ASN A CA 1 ATOM 1211 C C . ASN A 1 156 ? -47.060 28.838 40.613 1.00 12.52 ? 156 ASN A C 1 ATOM 1212 O O . ASN A 1 156 ? -47.973 28.614 39.822 1.00 12.01 ? 156 ASN A O 1 ATOM 1213 C CB . ASN A 1 156 ? -47.023 31.149 41.618 1.00 12.93 ? 156 ASN A CB 1 ATOM 1214 C CG . ASN A 1 156 ? -46.120 32.308 41.995 1.00 14.41 ? 156 ASN A CG 1 ATOM 1215 O OD1 . ASN A 1 156 ? -44.986 32.107 42.447 1.00 15.21 ? 156 ASN A OD1 1 ATOM 1216 N ND2 . ASN A 1 156 ? -46.609 33.531 41.797 1.00 12.63 ? 156 ASN A ND2 1 ATOM 1217 N N . GLY A 1 157 ? -46.541 27.929 41.430 1.00 12.56 ? 157 GLY A N 1 ATOM 1218 C CA . GLY A 1 157 ? -47.070 26.587 41.529 1.00 12.70 ? 157 GLY A CA 1 ATOM 1219 C C . GLY A 1 157 ? -46.483 25.914 42.753 1.00 13.13 ? 157 GLY A C 1 ATOM 1220 O O . GLY A 1 157 ? -45.926 26.599 43.618 1.00 14.12 ? 157 GLY A O 1 ATOM 1221 N N . PRO A 1 158 ? -46.647 24.587 42.902 1.00 13.90 ? 158 PRO A N 1 ATOM 1222 C CA . PRO A 1 158 ? -46.098 23.878 44.060 1.00 13.70 ? 158 PRO A CA 1 ATOM 1223 C C . PRO A 1 158 ? -44.569 23.731 43.999 1.00 13.15 ? 158 PRO A C 1 ATOM 1224 O O . PRO A 1 158 ? -43.938 24.129 43.014 1.00 14.92 ? 158 PRO A O 1 ATOM 1225 C CB . PRO A 1 158 ? -46.823 22.534 44.009 1.00 13.77 ? 158 PRO A CB 1 ATOM 1226 C CG . PRO A 1 158 ? -47.061 22.331 42.564 1.00 14.39 ? 158 PRO A CG 1 ATOM 1227 C CD . PRO A 1 158 ? -47.476 23.684 42.086 1.00 13.03 ? 158 PRO A CD 1 ATOM 1228 N N . ALA A 1 159 ? -43.983 23.216 45.075 1.00 13.77 ? 159 ALA A N 1 ATOM 1229 C CA . ALA A 1 159 ? -42.537 23.020 45.152 1.00 13.08 ? 159 ALA A CA 1 ATOM 1230 C C . ALA A 1 159 ? -42.189 21.715 45.851 1.00 13.10 ? 159 ALA A C 1 ATOM 1231 O O . ALA A 1 159 ? -43.023 21.138 46.550 1.00 14.32 ? 159 ALA A O 1 ATOM 1232 C CB . ALA A 1 159 ? -41.881 24.189 45.848 1.00 14.49 ? 159 ALA A CB 1 ATOM 1233 N N . SER A 1 160 ? -40.959 21.251 45.639 1.00 11.94 ? 160 SER A N 1 ATOM 1234 C CA . SER A 1 160 ? -40.465 19.998 46.211 1.00 13.24 ? 160 SER A CA 1 ATOM 1235 C C . SER A 1 160 ? -39.864 20.104 47.612 1.00 13.43 ? 160 SER A C 1 ATOM 1236 O O . SER A 1 160 ? -39.298 19.138 48.128 1.00 13.77 ? 160 SER A O 1 ATOM 1237 C CB . SER A 1 160 ? -39.445 19.377 45.268 1.00 14.02 ? 160 SER A CB 1 ATOM 1238 O OG . SER A 1 160 ? -38.373 20.267 45.037 1.00 13.13 ? 160 SER A OG 1 ATOM 1239 N N . LEU A 1 161 ? -39.990 21.278 48.220 1.00 14.85 ? 161 LEU A N 1 ATOM 1240 C CA . LEU A 1 161 ? -39.467 21.510 49.563 1.00 16.70 ? 161 LEU A CA 1 ATOM 1241 C C . LEU A 1 161 ? -40.203 22.681 50.194 1.00 16.17 ? 161 LEU A C 1 ATOM 1242 O O . LEU A 1 161 ? -40.636 23.595 49.477 1.00 14.96 ? 161 LEU A O 1 ATOM 1243 C CB . LEU A 1 161 ? -37.969 21.837 49.494 1.00 17.96 ? 161 LEU A CB 1 ATOM 1244 C CG . LEU A 1 161 ? -37.021 21.555 50.660 1.00 21.10 ? 161 LEU A CG 1 ATOM 1245 C CD1 . LEU A 1 161 ? -36.933 20.055 50.931 1.00 21.06 ? 161 LEU A CD1 1 ATOM 1246 C CD2 . LEU A 1 161 ? -35.658 22.118 50.333 1.00 19.21 ? 161 LEU A CD2 1 ATOM 1247 N N . PRO A 1 162 ? -40.474 22.611 51.520 1.00 16.80 ? 162 PRO A N 1 ATOM 1248 C CA . PRO A 1 162 ? -41.161 23.728 52.170 1.00 16.41 ? 162 PRO A CA 1 ATOM 1249 C C . PRO A 1 162 ? -40.239 24.959 52.300 1.00 15.08 ? 162 PRO A C 1 ATOM 1250 O O . PRO A 1 162 ? -39.017 24.813 52.393 1.00 15.45 ? 162 PRO A O 1 ATOM 1251 C CB . PRO A 1 162 ? -41.540 23.142 53.539 1.00 15.89 ? 162 PRO A CB 1 ATOM 1252 C CG . PRO A 1 162 ? -40.533 22.066 53.765 1.00 18.27 ? 162 PRO A CG 1 ATOM 1253 C CD . PRO A 1 162 ? -40.484 21.432 52.413 1.00 17.07 ? 162 PRO A CD 1 ATOM 1254 N N . TYR A 1 163 ? -40.820 26.150 52.166 1.00 14.49 ? 163 TYR A N 1 ATOM 1255 C CA . TYR A 1 163 ? -40.086 27.414 52.307 1.00 15.34 ? 163 TYR A CA 1 ATOM 1256 C C . TYR A 1 163 ? -41.036 28.485 52.810 1.00 15.25 ? 163 TYR A C 1 ATOM 1257 O O . TYR A 1 163 ? -42.233 28.422 52.542 1.00 15.87 ? 163 TYR A O 1 ATOM 1258 C CB . TYR A 1 163 ? -39.371 27.859 51.004 1.00 15.13 ? 163 TYR A CB 1 ATOM 1259 C CG . TYR A 1 163 ? -40.260 28.066 49.791 1.00 15.21 ? 163 TYR A CG 1 ATOM 1260 C CD1 . TYR A 1 163 ? -40.914 29.299 49.563 1.00 15.64 ? 163 TYR A CD1 1 ATOM 1261 C CD2 . TYR A 1 163 ? -40.473 27.021 48.875 1.00 14.97 ? 163 TYR A CD2 1 ATOM 1262 C CE1 . TYR A 1 163 ? -41.775 29.479 48.446 1.00 17.26 ? 163 TYR A CE1 1 ATOM 1263 C CE2 . TYR A 1 163 ? -41.322 27.189 47.760 1.00 13.72 ? 163 TYR A CE2 1 ATOM 1264 C CZ . TYR A 1 163 ? -41.971 28.412 47.554 1.00 15.27 ? 163 TYR A CZ 1 ATOM 1265 O OH . TYR A 1 163 ? -42.821 28.554 46.483 1.00 17.26 ? 163 TYR A OH 1 ATOM 1266 N N . ASP A 1 164 ? -40.486 29.513 53.447 1.00 15.79 ? 164 ASP A N 1 ATOM 1267 C CA . ASP A 1 164 ? -41.298 30.589 54.007 1.00 16.52 ? 164 ASP A CA 1 ATOM 1268 C C . ASP A 1 164 ? -41.504 31.798 53.118 1.00 15.32 ? 164 ASP A C 1 ATOM 1269 O O . ASP A 1 164 ? -42.614 32.328 53.033 1.00 16.38 ? 164 ASP A O 1 ATOM 1270 C CB . ASP A 1 164 ? -40.709 31.053 55.341 1.00 16.54 ? 164 ASP A CB 1 ATOM 1271 C CG . ASP A 1 164 ? -40.406 29.905 56.271 1.00 17.08 ? 164 ASP A CG 1 ATOM 1272 O OD1 . ASP A 1 164 ? -41.350 29.215 56.705 1.00 15.89 ? 164 ASP A OD1 1 ATOM 1273 O OD2 . ASP A 1 164 ? -39.211 29.685 56.544 1.00 15.42 ? 164 ASP A OD2 1 ATOM 1274 N N . ILE A 1 165 ? -40.417 32.262 52.503 1.00 15.61 ? 165 ILE A N 1 ATOM 1275 C CA . ILE A 1 165 ? -40.434 33.455 51.657 1.00 14.44 ? 165 ILE A CA 1 ATOM 1276 C C . ILE A 1 165 ? -39.946 33.169 50.239 1.00 14.06 ? 165 ILE A C 1 ATOM 1277 O O . ILE A 1 165 ? -38.952 32.471 50.042 1.00 14.57 ? 165 ILE A O 1 ATOM 1278 C CB . ILE A 1 165 ? -39.535 34.586 52.285 1.00 14.76 ? 165 ILE A CB 1 ATOM 1279 C CG1 . ILE A 1 165 ? -40.013 34.927 53.702 1.00 16.09 ? 165 ILE A CG1 1 ATOM 1280 C CG2 . ILE A 1 165 ? -39.558 35.873 51.426 1.00 13.78 ? 165 ILE A CG2 1 ATOM 1281 C CD1 . ILE A 1 165 ? -38.972 35.576 54.558 1.00 17.45 ? 165 ILE A CD1 1 ATOM 1282 N N . ASP A 1 166 ? -40.661 33.729 49.267 1.00 13.94 ? 166 ASP A N 1 ATOM 1283 C CA . ASP A 1 166 ? -40.313 33.612 47.856 1.00 14.40 ? 166 ASP A CA 1 ATOM 1284 C C . ASP A 1 166 ? -39.697 34.976 47.522 1.00 14.76 ? 166 ASP A C 1 ATOM 1285 O O . ASP A 1 166 ? -40.412 35.977 47.392 1.00 16.41 ? 166 ASP A O 1 ATOM 1286 C CB . ASP A 1 166 ? -41.572 33.344 47.008 1.00 15.47 ? 166 ASP A CB 1 ATOM 1287 C CG . ASP A 1 166 ? -41.257 32.929 45.559 1.00 15.54 ? 166 ASP A CG 1 ATOM 1288 O OD1 . ASP A 1 166 ? -40.139 33.184 45.056 1.00 13.49 ? 166 ASP A OD1 1 ATOM 1289 O OD2 . ASP A 1 166 ? -42.151 32.339 44.916 1.00 17.56 ? 166 ASP A OD2 1 ATOM 1290 N N . LEU A 1 167 ? -38.366 35.010 47.436 1.00 14.61 ? 167 LEU A N 1 ATOM 1291 C CA . LEU A 1 167 ? -37.616 36.232 47.127 1.00 14.28 ? 167 LEU A CA 1 ATOM 1292 C C . LEU A 1 167 ? -37.761 36.674 45.679 1.00 14.23 ? 167 LEU A C 1 ATOM 1293 O O . LEU A 1 167 ? -37.317 37.760 45.301 1.00 14.80 ? 167 LEU A O 1 ATOM 1294 C CB . LEU A 1 167 ? -36.135 36.062 47.475 1.00 15.64 ? 167 LEU A CB 1 ATOM 1295 C CG . LEU A 1 167 ? -35.768 35.971 48.956 1.00 14.98 ? 167 LEU A CG 1 ATOM 1296 C CD1 . LEU A 1 167 ? -34.293 35.661 49.054 1.00 17.03 ? 167 LEU A CD1 1 ATOM 1297 C CD2 . LEU A 1 167 ? -36.101 37.263 49.707 1.00 17.99 ? 167 LEU A CD2 1 ATOM 1298 N N . GLY A 1 168 ? -38.385 35.813 44.879 1.00 13.40 ? 168 GLY A N 1 ATOM 1299 C CA . GLY A 1 168 ? -38.625 36.113 43.484 1.00 13.76 ? 168 GLY A CA 1 ATOM 1300 C C . GLY A 1 168 ? -37.442 35.862 42.580 1.00 13.72 ? 168 GLY A C 1 ATOM 1301 O O . GLY A 1 168 ? -36.523 35.107 42.916 1.00 12.82 ? 168 GLY A O 1 ATOM 1302 N N . VAL A 1 169 ? -37.452 36.555 41.449 1.00 12.50 ? 169 VAL A N 1 ATOM 1303 C CA . VAL A 1 169 ? -36.418 36.406 40.442 1.00 12.36 ? 169 VAL A CA 1 ATOM 1304 C C . VAL A 1 169 ? -35.105 37.104 40.745 1.00 12.17 ? 169 VAL A C 1 ATOM 1305 O O . VAL A 1 169 ? -35.069 38.176 41.358 1.00 11.44 ? 169 VAL A O 1 ATOM 1306 C CB . VAL A 1 169 ? -36.951 36.762 39.039 1.00 12.13 ? 169 VAL A CB 1 ATOM 1307 C CG1 . VAL A 1 169 ? -38.118 35.819 38.691 1.00 8.04 ? 169 VAL A CG1 1 ATOM 1308 C CG2 . VAL A 1 169 ? -37.376 38.238 38.953 1.00 10.80 ? 169 VAL A CG2 1 ATOM 1309 N N . PHE A 1 170 ? -34.028 36.475 40.289 1.00 11.14 ? 170 PHE A N 1 ATOM 1310 C CA . PHE A 1 170 ? -32.680 36.977 40.499 1.00 11.00 ? 170 PHE A CA 1 ATOM 1311 C C . PHE A 1 170 ? -31.886 36.751 39.205 1.00 10.06 ? 170 PHE A C 1 ATOM 1312 O O . PHE A 1 170 ? -31.059 35.829 39.131 1.00 9.54 ? 170 PHE A O 1 ATOM 1313 C CB . PHE A 1 170 ? -32.061 36.207 41.674 1.00 10.30 ? 170 PHE A CB 1 ATOM 1314 C CG . PHE A 1 170 ? -31.003 36.959 42.429 1.00 11.68 ? 170 PHE A CG 1 ATOM 1315 C CD1 . PHE A 1 170 ? -31.228 38.277 42.874 1.00 11.51 ? 170 PHE A CD1 1 ATOM 1316 C CD2 . PHE A 1 170 ? -29.793 36.324 42.759 1.00 9.78 ? 170 PHE A CD2 1 ATOM 1317 C CE1 . PHE A 1 170 ? -30.265 38.955 43.644 1.00 12.43 ? 170 PHE A CE1 1 ATOM 1318 C CE2 . PHE A 1 170 ? -28.813 36.985 43.534 1.00 11.71 ? 170 PHE A CE2 1 ATOM 1319 C CZ . PHE A 1 170 ? -29.051 38.309 43.982 1.00 11.34 ? 170 PHE A CZ 1 ATOM 1320 N N . PRO A 1 171 ? -32.166 37.554 38.147 1.00 11.45 ? 171 PRO A N 1 ATOM 1321 C CA . PRO A 1 171 ? -31.446 37.394 36.878 1.00 11.48 ? 171 PRO A CA 1 ATOM 1322 C C . PRO A 1 171 ? -30.007 37.884 36.921 1.00 11.20 ? 171 PRO A C 1 ATOM 1323 O O . PRO A 1 171 ? -29.725 38.964 37.435 1.00 12.05 ? 171 PRO A O 1 ATOM 1324 C CB . PRO A 1 171 ? -32.301 38.199 35.897 1.00 12.81 ? 171 PRO A CB 1 ATOM 1325 C CG . PRO A 1 171 ? -32.844 39.298 36.748 1.00 11.56 ? 171 PRO A CG 1 ATOM 1326 C CD . PRO A 1 171 ? -33.207 38.601 38.023 1.00 10.53 ? 171 PRO A CD 1 ATOM 1327 N N . ILE A 1 172 ? -29.097 37.023 36.478 1.00 10.35 ? 172 ILE A N 1 ATOM 1328 C CA . ILE A 1 172 ? -27.677 37.350 36.427 1.00 9.67 ? 172 ILE A CA 1 ATOM 1329 C C . ILE A 1 172 ? -27.309 37.351 34.949 1.00 9.41 ? 172 ILE A C 1 ATOM 1330 O O . ILE A 1 172 ? -27.540 36.367 34.245 1.00 11.33 ? 172 ILE A O 1 ATOM 1331 C CB . ILE A 1 172 ? -26.796 36.337 37.212 1.00 10.20 ? 172 ILE A CB 1 ATOM 1332 C CG1 . ILE A 1 172 ? -27.312 36.164 38.648 1.00 10.35 ? 172 ILE A CG1 1 ATOM 1333 C CG2 . ILE A 1 172 ? -25.358 36.855 37.288 1.00 9.64 ? 172 ILE A CG2 1 ATOM 1334 C CD1 . ILE A 1 172 ? -26.582 35.108 39.441 1.00 12.43 ? 172 ILE A CD1 1 ATOM 1335 N N . THR A 1 173 ? -26.735 38.455 34.485 1.00 8.67 ? 173 THR A N 1 ATOM 1336 C CA . THR A 1 173 ? -26.371 38.576 33.081 1.00 7.96 ? 173 THR A CA 1 ATOM 1337 C C . THR A 1 173 ? -25.065 39.290 32.833 1.00 8.88 ? 173 THR A C 1 ATOM 1338 O O . THR A 1 173 ? -24.663 40.162 33.610 1.00 9.02 ? 173 THR A O 1 ATOM 1339 C CB . THR A 1 173 ? -27.484 39.328 32.267 1.00 7.66 ? 173 THR A CB 1 ATOM 1340 O OG1 . THR A 1 173 ? -27.126 39.382 30.876 1.00 7.17 ? 173 THR A OG1 1 ATOM 1341 C CG2 . THR A 1 173 ? -27.730 40.759 32.795 1.00 6.74 ? 173 THR A CG2 1 ATOM 1342 N N . ASP A 1 174 ? -24.437 38.946 31.708 1.00 8.76 ? 174 ASP A N 1 ATOM 1343 C CA . ASP A 1 174 ? -23.230 39.630 31.283 1.00 10.23 ? 174 ASP A CA 1 ATOM 1344 C C . ASP A 1 174 ? -23.693 40.976 30.747 1.00 9.42 ? 174 ASP A C 1 ATOM 1345 O O . ASP A 1 174 ? -24.845 41.121 30.325 1.00 9.65 ? 174 ASP A O 1 ATOM 1346 C CB . ASP A 1 174 ? -22.422 38.858 30.226 1.00 8.27 ? 174 ASP A CB 1 ATOM 1347 C CG . ASP A 1 174 ? -23.244 38.308 29.074 1.00 9.32 ? 174 ASP A CG 1 ATOM 1348 O OD1 . ASP A 1 174 ? -24.426 38.670 28.891 1.00 8.03 ? 174 ASP A OD1 1 ATOM 1349 O OD2 . ASP A 1 174 ? -22.666 37.489 28.318 1.00 7.20 ? 174 ASP A OD2 1 ATOM 1350 N N . TYR A 1 175 ? -22.804 41.951 30.799 1.00 10.57 ? 175 TYR A N 1 ATOM 1351 C CA . TYR A 1 175 ? -23.130 43.297 30.379 1.00 12.08 ? 175 TYR A CA 1 ATOM 1352 C C . TYR A 1 175 ? -21.985 43.833 29.555 1.00 10.60 ? 175 TYR A C 1 ATOM 1353 O O . TYR A 1 175 ? -20.833 43.794 29.989 1.00 11.63 ? 175 TYR A O 1 ATOM 1354 C CB . TYR A 1 175 ? -23.344 44.141 31.639 1.00 11.49 ? 175 TYR A CB 1 ATOM 1355 C CG . TYR A 1 175 ? -23.844 45.549 31.436 1.00 13.94 ? 175 TYR A CG 1 ATOM 1356 C CD1 . TYR A 1 175 ? -25.037 45.805 30.730 1.00 12.92 ? 175 TYR A CD1 1 ATOM 1357 C CD2 . TYR A 1 175 ? -23.150 46.639 32.004 1.00 14.15 ? 175 TYR A CD2 1 ATOM 1358 C CE1 . TYR A 1 175 ? -25.536 47.126 30.597 1.00 14.81 ? 175 TYR A CE1 1 ATOM 1359 C CE2 . TYR A 1 175 ? -23.634 47.958 31.879 1.00 13.59 ? 175 TYR A CE2 1 ATOM 1360 C CZ . TYR A 1 175 ? -24.823 48.192 31.177 1.00 15.91 ? 175 TYR A CZ 1 ATOM 1361 O OH . TYR A 1 175 ? -25.285 49.476 31.043 1.00 16.04 ? 175 TYR A OH 1 ATOM 1362 N N . TYR A 1 176 ? -22.313 44.281 28.346 1.00 10.76 ? 176 TYR A N 1 ATOM 1363 C CA . TYR A 1 176 ? -21.333 44.839 27.415 1.00 11.22 ? 176 TYR A CA 1 ATOM 1364 C C . TYR A 1 176 ? -21.724 46.269 27.090 1.00 12.64 ? 176 TYR A C 1 ATOM 1365 O O . TYR A 1 176 ? -22.908 46.559 26.924 1.00 11.06 ? 176 TYR A O 1 ATOM 1366 C CB . TYR A 1 176 ? -21.301 44.049 26.103 1.00 11.42 ? 176 TYR A CB 1 ATOM 1367 C CG . TYR A 1 176 ? -21.047 42.570 26.254 1.00 10.35 ? 176 TYR A CG 1 ATOM 1368 C CD1 . TYR A 1 176 ? -22.106 41.688 26.542 1.00 11.04 ? 176 TYR A CD1 1 ATOM 1369 C CD2 . TYR A 1 176 ? -19.743 42.041 26.148 1.00 12.74 ? 176 TYR A CD2 1 ATOM 1370 C CE1 . TYR A 1 176 ? -21.873 40.310 26.736 1.00 11.21 ? 176 TYR A CE1 1 ATOM 1371 C CE2 . TYR A 1 176 ? -19.501 40.649 26.336 1.00 11.38 ? 176 TYR A CE2 1 ATOM 1372 C CZ . TYR A 1 176 ? -20.574 39.797 26.639 1.00 10.15 ? 176 TYR A CZ 1 ATOM 1373 O OH . TYR A 1 176 ? -20.355 38.460 26.892 1.00 10.21 ? 176 TYR A OH 1 ATOM 1374 N N . TYR A 1 177 ? -20.727 47.142 26.949 1.00 12.96 ? 177 TYR A N 1 ATOM 1375 C CA . TYR A 1 177 ? -20.967 48.548 26.620 1.00 13.72 ? 177 TYR A CA 1 ATOM 1376 C C . TYR A 1 177 ? -21.309 48.710 25.151 1.00 14.14 ? 177 TYR A C 1 ATOM 1377 O O . TYR A 1 177 ? -22.126 49.563 24.777 1.00 13.29 ? 177 TYR A O 1 ATOM 1378 C CB . TYR A 1 177 ? -19.777 49.423 27.037 1.00 14.42 ? 177 TYR A CB 1 ATOM 1379 C CG . TYR A 1 177 ? -19.487 49.370 28.531 1.00 15.35 ? 177 TYR A CG 1 ATOM 1380 C CD1 . TYR A 1 177 ? -20.524 49.131 29.471 1.00 14.21 ? 177 TYR A CD1 1 ATOM 1381 C CD2 . TYR A 1 177 ? -18.170 49.503 29.017 1.00 15.35 ? 177 TYR A CD2 1 ATOM 1382 C CE1 . TYR A 1 177 ? -20.252 49.010 30.857 1.00 14.46 ? 177 TYR A CE1 1 ATOM 1383 C CE2 . TYR A 1 177 ? -17.884 49.392 30.416 1.00 14.72 ? 177 TYR A CE2 1 ATOM 1384 C CZ . TYR A 1 177 ? -18.935 49.141 31.317 1.00 15.59 ? 177 TYR A CZ 1 ATOM 1385 O OH . TYR A 1 177 ? -18.685 49.004 32.663 1.00 15.60 ? 177 TYR A OH 1 ATOM 1386 N N . ARG A 1 178 ? -20.745 47.816 24.342 1.00 12.76 ? 178 ARG A N 1 ATOM 1387 C CA . ARG A 1 178 ? -20.983 47.792 22.910 1.00 14.57 ? 178 ARG A CA 1 ATOM 1388 C C . ARG A 1 178 ? -22.335 47.134 22.646 1.00 14.53 ? 178 ARG A C 1 ATOM 1389 O O . ARG A 1 178 ? -22.752 46.229 23.384 1.00 16.48 ? 178 ARG A O 1 ATOM 1390 C CB . ARG A 1 178 ? -19.863 47.031 22.201 1.00 15.91 ? 178 ARG A CB 1 ATOM 1391 C CG . ARG A 1 178 ? -18.507 47.720 22.281 1.00 20.33 ? 178 ARG A CG 1 ATOM 1392 C CD . ARG A 1 178 ? -17.396 46.855 21.705 1.00 26.16 ? 178 ARG A CD 1 ATOM 1393 N NE . ARG A 1 178 ? -17.569 46.605 20.273 1.00 31.22 ? 178 ARG A NE 1 ATOM 1394 C CZ . ARG A 1 178 ? -16.668 46.020 19.486 1.00 33.17 ? 178 ARG A CZ 1 ATOM 1395 N NH1 . ARG A 1 178 ? -15.503 45.606 19.977 1.00 33.69 ? 178 ARG A NH1 1 ATOM 1396 N NH2 . ARG A 1 178 ? -16.928 45.864 18.194 1.00 34.95 ? 178 ARG A NH2 1 ATOM 1397 N N . ALA A 1 179 ? -23.035 47.632 21.631 1.00 13.90 ? 179 ALA A N 1 ATOM 1398 C CA . ALA A 1 179 ? -24.350 47.116 21.249 1.00 14.16 ? 179 ALA A CA 1 ATOM 1399 C C . ALA A 1 179 ? -24.250 45.724 20.624 1.00 13.00 ? 179 ALA A C 1 ATOM 1400 O O . ALA A 1 179 ? -23.194 45.341 20.119 1.00 10.53 ? 179 ALA A O 1 ATOM 1401 C CB . ALA A 1 179 ? -25.038 48.084 20.302 1.00 13.83 ? 179 ALA A CB 1 ATOM 1402 N N . ALA A 1 180 ? -25.360 44.988 20.662 1.00 13.06 ? 180 ALA A N 1 ATOM 1403 C CA . ALA A 1 180 ? -25.447 43.620 20.147 1.00 11.95 ? 180 ALA A CA 1 ATOM 1404 C C . ALA A 1 180 ? -25.000 43.390 18.711 1.00 13.26 ? 180 ALA A C 1 ATOM 1405 O O . ALA A 1 180 ? -24.258 42.439 18.452 1.00 11.09 ? 180 ALA A O 1 ATOM 1406 C CB . ALA A 1 180 ? -26.837 43.084 20.340 1.00 11.92 ? 180 ALA A CB 1 ATOM 1407 N N . ASP A 1 181 ? -25.411 44.278 17.801 1.00 11.56 ? 181 ASP A N 1 ATOM 1408 C CA . ASP A 1 181 ? -25.053 44.166 16.381 1.00 12.53 ? 181 ASP A CA 1 ATOM 1409 C C . ASP A 1 181 ? -23.574 44.411 16.105 1.00 12.44 ? 181 ASP A C 1 ATOM 1410 O O . ASP A 1 181 ? -23.007 43.812 15.191 1.00 11.35 ? 181 ASP A O 1 ATOM 1411 C CB . ASP A 1 181 ? -25.923 45.082 15.518 1.00 12.98 ? 181 ASP A CB 1 ATOM 1412 C CG . ASP A 1 181 ? -27.374 44.636 15.488 1.00 14.78 ? 181 ASP A CG 1 ATOM 1413 O OD1 . ASP A 1 181 ? -27.665 43.615 14.834 1.00 16.49 ? 181 ASP A OD1 1 ATOM 1414 O OD2 . ASP A 1 181 ? -28.215 45.286 16.142 1.00 16.08 ? 181 ASP A OD2 1 ATOM 1415 N N . ASP A 1 182 ? -22.953 45.262 16.923 1.00 13.22 ? 182 ASP A N 1 ATOM 1416 C CA . ASP A 1 182 ? -21.524 45.561 16.802 1.00 14.68 ? 182 ASP A CA 1 ATOM 1417 C C . ASP A 1 182 ? -20.729 44.366 17.316 1.00 14.10 ? 182 ASP A C 1 ATOM 1418 O O . ASP A 1 182 ? -19.678 44.031 16.772 1.00 13.28 ? 182 ASP A O 1 ATOM 1419 C CB . ASP A 1 182 ? -21.159 46.818 17.589 1.00 16.63 ? 182 ASP A CB 1 ATOM 1420 C CG . ASP A 1 182 ? -21.655 48.092 16.924 1.00 21.30 ? 182 ASP A CG 1 ATOM 1421 O OD1 . ASP A 1 182 ? -21.608 48.181 15.674 1.00 20.29 ? 182 ASP A OD1 1 ATOM 1422 O OD2 . ASP A 1 182 ? -22.087 49.010 17.655 1.00 23.62 ? 182 ASP A OD2 1 ATOM 1423 N N . LEU A 1 183 ? -21.280 43.698 18.331 1.00 13.62 ? 183 LEU A N 1 ATOM 1424 C CA . LEU A 1 183 ? -20.665 42.512 18.915 1.00 14.63 ? 183 LEU A CA 1 ATOM 1425 C C . LEU A 1 183 ? -20.828 41.288 18.020 1.00 14.19 ? 183 LEU A C 1 ATOM 1426 O O . LEU A 1 183 ? -19.954 40.426 18.012 1.00 14.26 ? 183 LEU A O 1 ATOM 1427 C CB . LEU A 1 183 ? -21.219 42.236 20.306 1.00 15.30 ? 183 LEU A CB 1 ATOM 1428 C CG . LEU A 1 183 ? -20.734 43.147 21.429 1.00 14.65 ? 183 LEU A CG 1 ATOM 1429 C CD1 . LEU A 1 183 ? -21.631 42.949 22.609 1.00 11.80 ? 183 LEU A CD1 1 ATOM 1430 C CD2 . LEU A 1 183 ? -19.279 42.873 21.792 1.00 15.34 ? 183 LEU A CD2 1 ATOM 1431 N N . VAL A 1 184 ? -21.925 41.233 17.252 1.00 13.14 ? 184 VAL A N 1 ATOM 1432 C CA . VAL A 1 184 ? -22.171 40.131 16.310 1.00 13.37 ? 184 VAL A CA 1 ATOM 1433 C C . VAL A 1 184 ? -21.117 40.246 15.205 1.00 13.85 ? 184 VAL A C 1 ATOM 1434 O O . VAL A 1 184 ? -20.423 39.274 14.911 1.00 12.27 ? 184 VAL A O 1 ATOM 1435 C CB . VAL A 1 184 ? -23.616 40.168 15.712 1.00 13.61 ? 184 VAL A CB 1 ATOM 1436 C CG1 . VAL A 1 184 ? -23.743 39.253 14.476 1.00 12.36 ? 184 VAL A CG1 1 ATOM 1437 C CG2 . VAL A 1 184 ? -24.609 39.714 16.756 1.00 11.01 ? 184 VAL A CG2 1 ATOM 1438 N N . HIS A 1 185 ? -20.947 41.468 14.691 1.00 15.40 ? 185 HIS A N 1 ATOM 1439 C CA . HIS A 1 185 ? -19.966 41.783 13.648 1.00 15.83 ? 185 HIS A CA 1 ATOM 1440 C C . HIS A 1 185 ? -18.539 41.468 14.130 1.00 13.73 ? 185 HIS A C 1 ATOM 1441 O O . HIS A 1 185 ? -17.732 40.910 13.376 1.00 15.29 ? 185 HIS A O 1 ATOM 1442 C CB . HIS A 1 185 ? -20.088 43.266 13.247 1.00 18.70 ? 185 HIS A CB 1 ATOM 1443 C CG . HIS A 1 185 ? -19.136 43.688 12.169 1.00 22.71 ? 185 HIS A CG 1 ATOM 1444 N ND1 . HIS A 1 185 ? -19.300 43.325 10.850 1.00 25.15 ? 185 HIS A ND1 1 ATOM 1445 C CD2 . HIS A 1 185 ? -17.990 44.409 12.222 1.00 25.12 ? 185 HIS A CD2 1 ATOM 1446 C CE1 . HIS A 1 185 ? -18.292 43.800 10.138 1.00 27.67 ? 185 HIS A CE1 1 ATOM 1447 N NE2 . HIS A 1 185 ? -17.484 44.460 10.947 1.00 26.52 ? 185 HIS A NE2 1 ATOM 1448 N N . PHE A 1 186 ? -18.252 41.805 15.387 1.00 12.71 ? 186 PHE A N 1 ATOM 1449 C CA . PHE A 1 186 ? -16.939 41.563 15.997 1.00 12.50 ? 186 PHE A CA 1 ATOM 1450 C C . PHE A 1 186 ? -16.656 40.062 16.111 1.00 11.94 ? 186 PHE A C 1 ATOM 1451 O O . PHE A 1 186 ? -15.619 39.595 15.646 1.00 12.61 ? 186 PHE A O 1 ATOM 1452 C CB . PHE A 1 186 ? -16.865 42.229 17.385 1.00 12.32 ? 186 PHE A CB 1 ATOM 1453 C CG . PHE A 1 186 ? -15.520 42.101 18.069 1.00 14.07 ? 186 PHE A CG 1 ATOM 1454 C CD1 . PHE A 1 186 ? -14.422 42.874 17.640 1.00 14.63 ? 186 PHE A CD1 1 ATOM 1455 C CD2 . PHE A 1 186 ? -15.346 41.209 19.153 1.00 13.95 ? 186 PHE A CD2 1 ATOM 1456 C CE1 . PHE A 1 186 ? -13.154 42.766 18.282 1.00 16.57 ? 186 PHE A CE1 1 ATOM 1457 C CE2 . PHE A 1 186 ? -14.086 41.086 19.809 1.00 15.48 ? 186 PHE A CE2 1 ATOM 1458 C CZ . PHE A 1 186 ? -12.987 41.869 19.369 1.00 14.80 ? 186 PHE A CZ 1 ATOM 1459 N N . THR A 1 187 ? -17.608 39.318 16.676 1.00 10.75 ? 187 THR A N 1 ATOM 1460 C CA . THR A 1 187 ? -17.459 37.875 16.869 1.00 12.19 ? 187 THR A CA 1 ATOM 1461 C C . THR A 1 187 ? -17.458 37.030 15.600 1.00 13.05 ? 187 THR A C 1 ATOM 1462 O O . THR A 1 187 ? -17.087 35.854 15.630 1.00 11.91 ? 187 THR A O 1 ATOM 1463 C CB . THR A 1 187 ? -18.485 37.326 17.856 1.00 13.19 ? 187 THR A CB 1 ATOM 1464 O OG1 . THR A 1 187 ? -19.810 37.621 17.396 1.00 12.38 ? 187 THR A OG1 1 ATOM 1465 C CG2 . THR A 1 187 ? -18.273 37.947 19.233 1.00 12.18 ? 187 THR A CG2 1 ATOM 1466 N N . GLN A 1 188 ? -17.846 37.647 14.486 1.00 14.07 ? 188 GLN A N 1 ATOM 1467 C CA . GLN A 1 188 ? -17.857 36.977 13.189 1.00 15.95 ? 188 GLN A CA 1 ATOM 1468 C C . GLN A 1 188 ? -16.425 36.769 12.683 1.00 16.69 ? 188 GLN A C 1 ATOM 1469 O O . GLN A 1 188 ? -16.149 35.809 11.962 1.00 17.35 ? 188 GLN A O 1 ATOM 1470 C CB . GLN A 1 188 ? -18.674 37.785 12.176 1.00 16.53 ? 188 GLN A CB 1 ATOM 1471 C CG . GLN A 1 188 ? -20.182 37.523 12.256 1.00 16.98 ? 188 GLN A CG 1 ATOM 1472 C CD . GLN A 1 188 ? -21.008 38.276 11.213 1.00 17.69 ? 188 GLN A CD 1 ATOM 1473 O OE1 . GLN A 1 188 ? -20.476 38.970 10.341 1.00 19.56 ? 188 GLN A OE1 1 ATOM 1474 N NE2 . GLN A 1 188 ? -22.323 38.133 11.302 1.00 16.34 ? 188 GLN A NE2 1 ATOM 1475 N N . ASN A 1 189 ? -15.514 37.644 13.113 1.00 17.28 ? 189 ASN A N 1 ATOM 1476 C CA . ASN A 1 189 ? -14.109 37.570 12.707 1.00 18.03 ? 189 ASN A CA 1 ATOM 1477 C C . ASN A 1 189 ? -13.111 37.560 13.864 1.00 17.30 ? 189 ASN A C 1 ATOM 1478 O O . ASN A 1 189 ? -11.902 37.498 13.638 1.00 16.65 ? 189 ASN A O 1 ATOM 1479 C CB . ASN A 1 189 ? -13.775 38.699 11.718 1.00 18.95 ? 189 ASN A CB 1 ATOM 1480 C CG . ASN A 1 189 ? -14.433 38.497 10.357 1.00 19.72 ? 189 ASN A CG 1 ATOM 1481 O OD1 . ASN A 1 189 ? -14.142 37.530 9.651 1.00 20.38 ? 189 ASN A OD1 1 ATOM 1482 N ND2 . ASN A 1 189 ? -15.344 39.391 10.002 1.00 22.07 ? 189 ASN A ND2 1 ATOM 1483 N N . ASN A 1 190 ? -13.613 37.631 15.100 1.00 16.58 ? 190 ASN A N 1 ATOM 1484 C CA . ASN A 1 190 ? -12.762 37.626 16.294 1.00 17.62 ? 190 ASN A CA 1 ATOM 1485 C C . ASN A 1 190 ? -13.313 36.720 17.385 1.00 19.32 ? 190 ASN A C 1 ATOM 1486 O O . ASN A 1 190 ? -14.487 36.341 17.360 1.00 19.17 ? 190 ASN A O 1 ATOM 1487 C CB . ASN A 1 190 ? -12.607 39.036 16.880 1.00 17.97 ? 190 ASN A CB 1 ATOM 1488 C CG . ASN A 1 190 ? -11.960 40.005 15.923 1.00 18.78 ? 190 ASN A CG 1 ATOM 1489 O OD1 . ASN A 1 190 ? -10.738 40.125 15.876 1.00 22.89 ? 190 ASN A OD1 1 ATOM 1490 N ND2 . ASN A 1 190 ? -12.780 40.682 15.128 1.00 17.29 ? 190 ASN A ND2 1 ATOM 1491 N N . ALA A 1 191 ? -12.447 36.372 18.338 1.00 17.56 ? 191 ALA A N 1 ATOM 1492 C CA . ALA A 1 191 ? -12.821 35.547 19.487 1.00 19.46 ? 191 ALA A CA 1 ATOM 1493 C C . ALA A 1 191 ? -13.697 36.444 20.373 1.00 18.21 ? 191 ALA A C 1 ATOM 1494 O O . ALA A 1 191 ? -13.456 37.658 20.439 1.00 17.86 ? 191 ALA A O 1 ATOM 1495 C CB . ALA A 1 191 ? -11.568 35.103 20.250 1.00 20.38 ? 191 ALA A CB 1 ATOM 1496 N N . PRO A 1 192 ? -14.756 35.885 21.004 1.00 17.79 ? 192 PRO A N 1 ATOM 1497 C CA . PRO A 1 192 ? -15.642 36.684 21.866 1.00 17.77 ? 192 PRO A CA 1 ATOM 1498 C C . PRO A 1 192 ? -14.944 37.382 23.036 1.00 16.41 ? 192 PRO A C 1 ATOM 1499 O O . PRO A 1 192 ? -14.054 36.806 23.664 1.00 16.67 ? 192 PRO A O 1 ATOM 1500 C CB . PRO A 1 192 ? -16.684 35.663 22.336 1.00 18.66 ? 192 PRO A CB 1 ATOM 1501 C CG . PRO A 1 192 ? -15.974 34.355 22.234 1.00 20.02 ? 192 PRO A CG 1 ATOM 1502 C CD . PRO A 1 192 ? -15.237 34.492 20.938 1.00 17.60 ? 192 PRO A CD 1 ATOM 1503 N N . PRO A 1 193 ? -15.303 38.655 23.306 1.00 15.46 ? 193 PRO A N 1 ATOM 1504 C CA . PRO A 1 193 ? -14.663 39.368 24.414 1.00 13.52 ? 193 PRO A CA 1 ATOM 1505 C C . PRO A 1 193 ? -15.226 38.967 25.770 1.00 12.16 ? 193 PRO A C 1 ATOM 1506 O O . PRO A 1 193 ? -16.260 38.298 25.856 1.00 10.50 ? 193 PRO A O 1 ATOM 1507 C CB . PRO A 1 193 ? -15.001 40.827 24.107 1.00 14.04 ? 193 PRO A CB 1 ATOM 1508 C CG . PRO A 1 193 ? -16.394 40.726 23.545 1.00 14.33 ? 193 PRO A CG 1 ATOM 1509 C CD . PRO A 1 193 ? -16.270 39.533 22.609 1.00 16.83 ? 193 PRO A CD 1 ATOM 1510 N N . PHE A 1 194 ? -14.524 39.377 26.823 1.00 11.00 ? 194 PHE A N 1 ATOM 1511 C CA . PHE A 1 194 ? -14.979 39.151 28.183 1.00 10.51 ? 194 PHE A CA 1 ATOM 1512 C C . PHE A 1 194 ? -16.052 40.223 28.387 1.00 11.60 ? 194 PHE A C 1 ATOM 1513 O O . PHE A 1 194 ? -16.052 41.244 27.684 1.00 10.50 ? 194 PHE A O 1 ATOM 1514 C CB . PHE A 1 194 ? -13.838 39.394 29.178 1.00 11.10 ? 194 PHE A CB 1 ATOM 1515 C CG . PHE A 1 194 ? -13.080 38.147 29.602 1.00 10.64 ? 194 PHE A CG 1 ATOM 1516 C CD1 . PHE A 1 194 ? -13.085 36.969 28.826 1.00 9.59 ? 194 PHE A CD1 1 ATOM 1517 C CD2 . PHE A 1 194 ? -12.329 38.166 30.801 1.00 12.20 ? 194 PHE A CD2 1 ATOM 1518 C CE1 . PHE A 1 194 ? -12.348 35.815 29.234 1.00 11.80 ? 194 PHE A CE1 1 ATOM 1519 C CE2 . PHE A 1 194 ? -11.588 37.029 31.228 1.00 12.88 ? 194 PHE A CE2 1 ATOM 1520 C CZ . PHE A 1 194 ? -11.597 35.849 30.440 1.00 13.43 ? 194 PHE A CZ 1 ATOM 1521 N N . SER A 1 195 ? -16.990 39.979 29.299 1.00 11.34 ? 195 SER A N 1 ATOM 1522 C CA . SER A 1 195 ? -18.025 40.966 29.586 1.00 13.79 ? 195 SER A CA 1 ATOM 1523 C C . SER A 1 195 ? -17.432 42.139 30.332 1.00 14.02 ? 195 SER A C 1 ATOM 1524 O O . SER A 1 195 ? -16.455 41.978 31.058 1.00 15.01 ? 195 SER A O 1 ATOM 1525 C CB . SER A 1 195 ? -19.162 40.356 30.385 1.00 13.26 ? 195 SER A CB 1 ATOM 1526 O OG . SER A 1 195 ? -18.704 39.716 31.556 1.00 11.51 ? 195 SER A OG 1 ATOM 1527 N N . ASP A 1 196 ? -17.986 43.327 30.111 1.00 14.01 ? 196 ASP A N 1 ATOM 1528 C CA . ASP A 1 196 ? -17.494 44.523 30.780 1.00 13.84 ? 196 ASP A CA 1 ATOM 1529 C C . ASP A 1 196 ? -17.858 44.477 32.257 1.00 13.92 ? 196 ASP A C 1 ATOM 1530 O O . ASP A 1 196 ? -17.079 44.885 33.120 1.00 14.30 ? 196 ASP A O 1 ATOM 1531 C CB . ASP A 1 196 ? -18.046 45.762 30.099 1.00 14.98 ? 196 ASP A CB 1 ATOM 1532 C CG . ASP A 1 196 ? -17.464 45.969 28.712 1.00 16.82 ? 196 ASP A CG 1 ATOM 1533 O OD1 . ASP A 1 196 ? -16.222 45.997 28.581 1.00 16.86 ? 196 ASP A OD1 1 ATOM 1534 O OD2 . ASP A 1 196 ? -18.250 46.104 27.754 1.00 14.33 ? 196 ASP A OD2 1 ATOM 1535 N N . ASN A 1 197 ? -19.016 43.885 32.531 1.00 12.71 ? 197 ASN A N 1 ATOM 1536 C CA . ASN A 1 197 ? -19.509 43.712 33.882 1.00 12.71 ? 197 ASN A CA 1 ATOM 1537 C C . ASN A 1 197 ? -20.544 42.594 33.868 1.00 12.09 ? 197 ASN A C 1 ATOM 1538 O O . ASN A 1 197 ? -20.891 42.058 32.809 1.00 12.35 ? 197 ASN A O 1 ATOM 1539 C CB . ASN A 1 197 ? -20.133 45.015 34.418 1.00 12.85 ? 197 ASN A CB 1 ATOM 1540 C CG . ASN A 1 197 ? -19.899 45.204 35.914 1.00 14.75 ? 197 ASN A CG 1 ATOM 1541 O OD1 . ASN A 1 197 ? -19.757 44.233 36.663 1.00 16.23 ? 197 ASN A OD1 1 ATOM 1542 N ND2 . ASN A 1 197 ? -19.869 46.458 36.357 1.00 15.09 ? 197 ASN A ND2 1 ATOM 1543 N N . VAL A 1 198 ? -20.956 42.183 35.061 1.00 10.54 ? 198 VAL A N 1 ATOM 1544 C CA . VAL A 1 198 ? -21.968 41.153 35.232 1.00 10.23 ? 198 VAL A CA 1 ATOM 1545 C C . VAL A 1 198 ? -22.993 41.734 36.199 1.00 9.52 ? 198 VAL A C 1 ATOM 1546 O O . VAL A 1 198 ? -22.673 42.034 37.352 1.00 9.13 ? 198 VAL A O 1 ATOM 1547 C CB . VAL A 1 198 ? -21.370 39.822 35.771 1.00 8.99 ? 198 VAL A CB 1 ATOM 1548 C CG1 . VAL A 1 198 ? -22.468 38.869 36.248 1.00 11.50 ? 198 VAL A CG1 1 ATOM 1549 C CG2 . VAL A 1 198 ? -20.513 39.138 34.701 1.00 9.27 ? 198 VAL A CG2 1 ATOM 1550 N N . LEU A 1 199 ? -24.212 41.914 35.697 1.00 10.82 ? 199 LEU A N 1 ATOM 1551 C CA . LEU A 1 199 ? -25.311 42.463 36.481 1.00 10.91 ? 199 LEU A CA 1 ATOM 1552 C C . LEU A 1 199 ? -26.062 41.380 37.209 1.00 12.14 ? 199 LEU A C 1 ATOM 1553 O O . LEU A 1 199 ? -26.327 40.312 36.660 1.00 11.46 ? 199 LEU A O 1 ATOM 1554 C CB . LEU A 1 199 ? -26.297 43.218 35.595 1.00 11.56 ? 199 LEU A CB 1 ATOM 1555 C CG . LEU A 1 199 ? -25.769 44.299 34.671 1.00 11.30 ? 199 LEU A CG 1 ATOM 1556 C CD1 . LEU A 1 199 ? -26.910 44.812 33.846 1.00 13.55 ? 199 LEU A CD1 1 ATOM 1557 C CD2 . LEU A 1 199 ? -25.091 45.417 35.430 1.00 12.78 ? 199 LEU A CD2 1 ATOM 1558 N N . ILE A 1 200 ? -26.345 41.651 38.477 1.00 10.68 ? 200 ILE A N 1 ATOM 1559 C CA . ILE A 1 200 ? -27.087 40.740 39.323 1.00 11.91 ? 200 ILE A CA 1 ATOM 1560 C C . ILE A 1 200 ? -28.316 41.538 39.708 1.00 13.01 ? 200 ILE A C 1 ATOM 1561 O O . ILE A 1 200 ? -28.208 42.581 40.357 1.00 13.43 ? 200 ILE A O 1 ATOM 1562 C CB . ILE A 1 200 ? -26.280 40.324 40.571 1.00 11.37 ? 200 ILE A CB 1 ATOM 1563 C CG1 . ILE A 1 200 ? -24.976 39.640 40.150 1.00 12.90 ? 200 ILE A CG1 1 ATOM 1564 C CG2 . ILE A 1 200 ? -27.098 39.368 41.399 1.00 11.84 ? 200 ILE A CG2 1 ATOM 1565 C CD1 . ILE A 1 200 ? -24.076 39.258 41.268 1.00 10.54 ? 200 ILE A CD1 1 ATOM 1566 N N . ASN A 1 201 ? -29.473 41.057 39.251 1.00 14.97 ? 201 ASN A N 1 ATOM 1567 C CA . ASN A 1 201 ? -30.781 41.688 39.460 1.00 16.47 ? 201 ASN A CA 1 ATOM 1568 C C . ASN A 1 201 ? -30.787 43.123 38.910 1.00 14.84 ? 201 ASN A C 1 ATOM 1569 O O . ASN A 1 201 ? -31.268 44.055 39.555 1.00 15.55 ? 201 ASN A O 1 ATOM 1570 C CB . ASN A 1 201 ? -31.222 41.621 40.935 1.00 19.25 ? 201 ASN A CB 1 ATOM 1571 C CG . ASN A 1 201 ? -32.734 41.769 41.110 1.00 22.93 ? 201 ASN A CG 1 ATOM 1572 O OD1 . ASN A 1 201 ? -33.505 41.595 40.160 1.00 20.47 ? 201 ASN A OD1 1 ATOM 1573 N ND2 . ASN A 1 201 ? -33.145 42.097 42.331 1.00 25.93 ? 201 ASN A ND2 1 ATOM 1574 N N . GLY A 1 202 ? -30.144 43.277 37.752 1.00 13.19 ? 202 GLY A N 1 ATOM 1575 C CA . GLY A 1 202 ? -30.061 44.555 37.063 1.00 14.64 ? 202 GLY A CA 1 ATOM 1576 C C . GLY A 1 202 ? -29.077 45.594 37.565 1.00 14.77 ? 202 GLY A C 1 ATOM 1577 O O . GLY A 1 202 ? -29.129 46.738 37.115 1.00 16.06 ? 202 GLY A O 1 ATOM 1578 N N . THR A 1 203 ? -28.170 45.206 38.462 1.00 15.47 ? 203 THR A N 1 ATOM 1579 C CA . THR A 1 203 ? -27.188 46.146 38.997 1.00 14.98 ? 203 THR A CA 1 ATOM 1580 C C . THR A 1 203 ? -25.823 45.539 39.323 1.00 13.79 ? 203 THR A C 1 ATOM 1581 O O . THR A 1 203 ? -25.696 44.336 39.569 1.00 13.60 ? 203 THR A O 1 ATOM 1582 C CB . THR A 1 203 ? -27.758 46.936 40.228 1.00 16.78 ? 203 THR A CB 1 ATOM 1583 O OG1 . THR A 1 203 ? -26.846 47.978 40.604 1.00 20.74 ? 203 THR A OG1 1 ATOM 1584 C CG2 . THR A 1 203 ? -28.008 46.019 41.417 1.00 16.02 ? 203 THR A CG2 1 ATOM 1585 N N . ALA A 1 204 ? -24.808 46.398 39.279 1.00 13.90 ? 204 ALA A N 1 ATOM 1586 C CA . ALA A 1 204 ? -23.423 46.041 39.574 1.00 13.61 ? 204 ALA A CA 1 ATOM 1587 C C . ALA A 1 204 ? -22.616 47.302 39.847 1.00 14.40 ? 204 ALA A C 1 ATOM 1588 O O . ALA A 1 204 ? -23.060 48.419 39.563 1.00 12.63 ? 204 ALA A O 1 ATOM 1589 C CB . ALA A 1 204 ? -22.793 45.279 38.410 1.00 13.31 ? 204 ALA A CB 1 ATOM 1590 N N . VAL A 1 205 ? -21.450 47.102 40.451 1.00 15.87 ? 205 VAL A N 1 ATOM 1591 C CA . VAL A 1 205 ? -20.521 48.179 40.744 1.00 16.19 ? 205 VAL A CA 1 ATOM 1592 C C . VAL A 1 205 ? -19.480 48.125 39.635 1.00 16.53 ? 205 VAL A C 1 ATOM 1593 O O . VAL A 1 205 ? -19.105 47.038 39.180 1.00 16.17 ? 205 VAL A O 1 ATOM 1594 C CB . VAL A 1 205 ? -19.839 47.993 42.138 1.00 16.04 ? 205 VAL A CB 1 ATOM 1595 C CG1 . VAL A 1 205 ? -18.711 48.999 42.356 1.00 16.25 ? 205 VAL A CG1 1 ATOM 1596 C CG2 . VAL A 1 205 ? -20.853 48.192 43.227 1.00 16.01 ? 205 VAL A CG2 1 ATOM 1597 N N . ASN A 1 206 ? -19.069 49.303 39.171 1.00 17.81 ? 206 ASN A N 1 ATOM 1598 C CA . ASN A 1 206 ? -18.042 49.433 38.143 1.00 21.22 ? 206 ASN A CA 1 ATOM 1599 C C . ASN A 1 206 ? -16.715 49.124 38.852 1.00 22.03 ? 206 ASN A C 1 ATOM 1600 O O . ASN A 1 206 ? -16.394 49.766 39.852 1.00 24.30 ? 206 ASN A O 1 ATOM 1601 C CB . ASN A 1 206 ? -18.032 50.865 37.596 1.00 21.28 ? 206 ASN A CB 1 ATOM 1602 C CG . ASN A 1 206 ? -17.161 51.021 36.366 1.00 21.08 ? 206 ASN A CG 1 ATOM 1603 O OD1 . ASN A 1 206 ? -15.940 50.972 36.449 1.00 20.87 ? 206 ASN A OD1 1 ATOM 1604 N ND2 . ASN A 1 206 ? -17.791 51.211 35.217 1.00 24.13 ? 206 ASN A ND2 1 ATOM 1605 N N . PRO A 1 207 ? -15.934 48.145 38.344 1.00 24.48 ? 207 PRO A N 1 ATOM 1606 C CA . PRO A 1 207 ? -14.650 47.773 38.957 1.00 26.16 ? 207 PRO A CA 1 ATOM 1607 C C . PRO A 1 207 ? -13.539 48.832 38.872 1.00 28.29 ? 207 PRO A C 1 ATOM 1608 O O . PRO A 1 207 ? -12.540 48.742 39.591 1.00 29.81 ? 207 PRO A O 1 ATOM 1609 C CB . PRO A 1 207 ? -14.272 46.511 38.190 1.00 25.05 ? 207 PRO A CB 1 ATOM 1610 C CG . PRO A 1 207 ? -14.817 46.790 36.815 1.00 24.94 ? 207 PRO A CG 1 ATOM 1611 C CD . PRO A 1 207 ? -16.185 47.325 37.139 1.00 24.28 ? 207 PRO A CD 1 ATOM 1612 N N . ASN A 1 208 ? -13.736 49.827 38.005 1.00 28.56 ? 208 ASN A N 1 ATOM 1613 C CA . ASN A 1 208 ? -12.763 50.900 37.798 1.00 29.92 ? 208 ASN A CA 1 ATOM 1614 C C . ASN A 1 208 ? -13.088 52.198 38.543 1.00 29.28 ? 208 ASN A C 1 ATOM 1615 O O . ASN A 1 208 ? -12.205 52.788 39.170 1.00 30.64 ? 208 ASN A O 1 ATOM 1616 C CB . ASN A 1 208 ? -12.609 51.202 36.298 1.00 31.07 ? 208 ASN A CB 1 ATOM 1617 C CG . ASN A 1 208 ? -12.246 49.971 35.477 1.00 32.49 ? 208 ASN A CG 1 ATOM 1618 O OD1 . ASN A 1 208 ? -12.972 49.590 34.557 1.00 32.49 ? 208 ASN A OD1 1 ATOM 1619 N ND2 . ASN A 1 208 ? -11.117 49.352 35.802 1.00 33.02 ? 208 ASN A ND2 1 ATOM 1620 N N . THR A 1 209 ? -14.348 52.632 38.482 1.00 28.49 ? 209 THR A N 1 ATOM 1621 C CA . THR A 1 209 ? -14.773 53.885 39.124 1.00 27.48 ? 209 THR A CA 1 ATOM 1622 C C . THR A 1 209 ? -15.431 53.751 40.497 1.00 27.44 ? 209 THR A C 1 ATOM 1623 O O . THR A 1 209 ? -15.479 54.719 41.263 1.00 27.75 ? 209 THR A O 1 ATOM 1624 C CB . THR A 1 209 ? -15.736 54.695 38.216 1.00 27.17 ? 209 THR A CB 1 ATOM 1625 O OG1 . THR A 1 209 ? -16.967 53.979 38.056 1.00 24.36 ? 209 THR A OG1 1 ATOM 1626 C CG2 . THR A 1 209 ? -15.116 54.956 36.849 1.00 27.05 ? 209 THR A CG2 1 ATOM 1627 N N . GLY A 1 210 ? -15.984 52.572 40.779 1.00 27.09 ? 210 GLY A N 1 ATOM 1628 C CA . GLY A 1 210 ? -16.658 52.341 42.046 1.00 25.22 ? 210 GLY A CA 1 ATOM 1629 C C . GLY A 1 210 ? -18.113 52.788 42.035 1.00 24.93 ? 210 GLY A C 1 ATOM 1630 O O . GLY A 1 210 ? -18.799 52.689 43.057 1.00 24.90 ? 210 GLY A O 1 ATOM 1631 N N . GLU A 1 211 ? -18.581 53.266 40.877 1.00 24.14 ? 211 GLU A N 1 ATOM 1632 C CA . GLU A 1 211 ? -19.961 53.732 40.692 1.00 25.58 ? 211 GLU A CA 1 ATOM 1633 C C . GLU A 1 211 ? -20.936 52.562 40.602 1.00 25.19 ? 211 GLU A C 1 ATOM 1634 O O . GLU A 1 211 ? -20.538 51.446 40.269 1.00 24.33 ? 211 GLU A O 1 ATOM 1635 C CB . GLU A 1 211 ? -20.076 54.600 39.432 1.00 28.09 ? 211 GLU A CB 1 ATOM 1636 C CG . GLU A 1 211 ? -19.483 56.002 39.566 1.00 32.44 ? 211 GLU A CG 1 ATOM 1637 C CD . GLU A 1 211 ? -19.498 56.782 38.261 1.00 35.31 ? 211 GLU A CD 1 ATOM 1638 O OE1 . GLU A 1 211 ? -20.568 56.881 37.622 1.00 38.01 ? 211 GLU A OE1 1 ATOM 1639 O OE2 . GLU A 1 211 ? -18.433 57.305 37.872 1.00 38.46 ? 211 GLU A OE2 1 ATOM 1640 N N . GLY A 1 212 ? -22.207 52.836 40.891 1.00 25.30 ? 212 GLY A N 1 ATOM 1641 C CA . GLY A 1 212 ? -23.233 51.807 40.866 1.00 24.66 ? 212 GLY A CA 1 ATOM 1642 C C . GLY A 1 212 ? -23.406 51.172 42.235 1.00 24.85 ? 212 GLY A C 1 ATOM 1643 O O . GLY A 1 212 ? -22.749 51.578 43.201 1.00 23.04 ? 212 GLY A O 1 ATOM 1644 N N . GLN A 1 213 ? -24.283 50.172 42.325 1.00 24.82 ? 213 GLN A N 1 ATOM 1645 C CA . GLN A 1 213 ? -24.558 49.484 43.583 1.00 25.12 ? 213 GLN A CA 1 ATOM 1646 C C . GLN A 1 213 ? -24.615 47.970 43.415 1.00 23.93 ? 213 GLN A C 1 ATOM 1647 O O . GLN A 1 213 ? -24.903 47.467 42.331 1.00 20.86 ? 213 GLN A O 1 ATOM 1648 C CB . GLN A 1 213 ? -25.902 49.951 44.179 1.00 28.48 ? 213 GLN A CB 1 ATOM 1649 C CG . GLN A 1 213 ? -26.050 51.458 44.501 1.00 36.38 ? 213 GLN A CG 1 ATOM 1650 C CD . GLN A 1 213 ? -25.100 52.013 45.579 1.00 40.01 ? 213 GLN A CD 1 ATOM 1651 O OE1 . GLN A 1 213 ? -24.925 53.214 45.680 1.00 43.37 ? 213 GLN A OE1 1 ATOM 1652 N NE2 . GLN A 1 213 ? -24.514 51.137 46.397 1.00 42.16 ? 213 GLN A NE2 1 ATOM 1653 N N . TYR A 1 214 ? -24.299 47.246 44.488 1.00 21.41 ? 214 TYR A N 1 ATOM 1654 C CA . TYR A 1 214 ? -24.361 45.781 44.491 1.00 20.22 ? 214 TYR A CA 1 ATOM 1655 C C . TYR A 1 214 ? -25.826 45.419 44.727 1.00 19.59 ? 214 TYR A C 1 ATOM 1656 O O . TYR A 1 214 ? -26.557 46.193 45.361 1.00 18.90 ? 214 TYR A O 1 ATOM 1657 C CB . TYR A 1 214 ? -23.566 45.191 45.661 1.00 20.21 ? 214 TYR A CB 1 ATOM 1658 C CG . TYR A 1 214 ? -22.066 45.377 45.625 1.00 20.20 ? 214 TYR A CG 1 ATOM 1659 C CD1 . TYR A 1 214 ? -21.253 44.546 44.825 1.00 18.96 ? 214 TYR A CD1 1 ATOM 1660 C CD2 . TYR A 1 214 ? -21.435 46.351 46.433 1.00 20.33 ? 214 TYR A CD2 1 ATOM 1661 C CE1 . TYR A 1 214 ? -19.837 44.672 44.827 1.00 19.91 ? 214 TYR A CE1 1 ATOM 1662 C CE2 . TYR A 1 214 ? -20.011 46.490 46.442 1.00 18.88 ? 214 TYR A CE2 1 ATOM 1663 C CZ . TYR A 1 214 ? -19.230 45.646 45.639 1.00 18.44 ? 214 TYR A CZ 1 ATOM 1664 O OH . TYR A 1 214 ? -17.865 45.761 45.647 1.00 17.38 ? 214 TYR A OH 1 ATOM 1665 N N . ALA A 1 215 ? -26.257 44.259 44.223 1.00 19.20 ? 215 ALA A N 1 ATOM 1666 C CA . ALA A 1 215 ? -27.626 43.782 44.441 1.00 18.59 ? 215 ALA A CA 1 ATOM 1667 C C . ALA A 1 215 ? -27.711 43.453 45.927 1.00 18.80 ? 215 ALA A C 1 ATOM 1668 O O . ALA A 1 215 ? -26.801 42.838 46.490 1.00 19.43 ? 215 ALA A O 1 ATOM 1669 C CB . ALA A 1 215 ? -27.912 42.557 43.600 1.00 15.77 ? 215 ALA A CB 1 ATOM 1670 N N . ASN A 1 216 ? -28.750 43.971 46.569 1.00 18.96 ? 216 ASN A N 1 ATOM 1671 C CA . ASN A 1 216 ? -28.929 43.787 47.998 1.00 18.96 ? 216 ASN A CA 1 ATOM 1672 C C . ASN A 1 216 ? -30.176 42.979 48.338 1.00 17.95 ? 216 ASN A C 1 ATOM 1673 O O . ASN A 1 216 ? -31.306 43.459 48.210 1.00 18.64 ? 216 ASN A O 1 ATOM 1674 C CB . ASN A 1 216 ? -28.953 45.167 48.661 1.00 21.49 ? 216 ASN A CB 1 ATOM 1675 C CG . ASN A 1 216 ? -28.814 45.114 50.172 1.00 24.85 ? 216 ASN A CG 1 ATOM 1676 O OD1 . ASN A 1 216 ? -28.582 44.059 50.783 1.00 22.74 ? 216 ASN A OD1 1 ATOM 1677 N ND2 . ASN A 1 216 ? -28.950 46.291 50.768 1.00 27.14 ? 216 ASN A ND2 1 ATOM 1678 N N . VAL A 1 217 ? -29.948 41.749 48.792 1.00 16.10 ? 217 VAL A N 1 ATOM 1679 C CA . VAL A 1 217 ? -31.031 40.848 49.165 1.00 17.11 ? 217 VAL A CA 1 ATOM 1680 C C . VAL A 1 217 ? -31.128 40.743 50.680 1.00 17.18 ? 217 VAL A C 1 ATOM 1681 O O . VAL A 1 217 ? -30.177 40.336 51.346 1.00 16.62 ? 217 VAL A O 1 ATOM 1682 C CB . VAL A 1 217 ? -30.833 39.437 48.564 1.00 15.59 ? 217 VAL A CB 1 ATOM 1683 C CG1 . VAL A 1 217 ? -32.027 38.535 48.869 1.00 14.92 ? 217 VAL A CG1 1 ATOM 1684 C CG2 . VAL A 1 217 ? -30.647 39.531 47.080 1.00 16.35 ? 217 VAL A CG2 1 ATOM 1685 N N . THR A 1 218 ? -32.294 41.093 51.210 1.00 19.11 ? 218 THR A N 1 ATOM 1686 C CA . THR A 1 218 ? -32.524 41.019 52.642 1.00 21.54 ? 218 THR A CA 1 ATOM 1687 C C . THR A 1 218 ? -33.137 39.675 53.027 1.00 20.04 ? 218 THR A C 1 ATOM 1688 O O . THR A 1 218 ? -34.228 39.311 52.570 1.00 21.15 ? 218 THR A O 1 ATOM 1689 C CB . THR A 1 218 ? -33.375 42.214 53.157 1.00 22.57 ? 218 THR A CB 1 ATOM 1690 O OG1 . THR A 1 218 ? -32.685 43.434 52.868 1.00 26.36 ? 218 THR A OG1 1 ATOM 1691 C CG2 . THR A 1 218 ? -33.578 42.140 54.671 1.00 24.60 ? 218 THR A CG2 1 ATOM 1692 N N . LEU A 1 219 ? -32.369 38.919 53.808 1.00 18.68 ? 219 LEU A N 1 ATOM 1693 C CA . LEU A 1 219 ? -32.787 37.619 54.318 1.00 18.98 ? 219 LEU A CA 1 ATOM 1694 C C . LEU A 1 219 ? -33.347 37.825 55.724 1.00 19.85 ? 219 LEU A C 1 ATOM 1695 O O . LEU A 1 219 ? -32.802 38.610 56.506 1.00 18.09 ? 219 LEU A O 1 ATOM 1696 C CB . LEU A 1 219 ? -31.601 36.653 54.401 1.00 18.34 ? 219 LEU A CB 1 ATOM 1697 C CG . LEU A 1 219 ? -30.864 36.158 53.152 1.00 18.36 ? 219 LEU A CG 1 ATOM 1698 C CD1 . LEU A 1 219 ? -29.707 35.285 53.588 1.00 15.48 ? 219 LEU A CD1 1 ATOM 1699 C CD2 . LEU A 1 219 ? -31.785 35.367 52.230 1.00 15.73 ? 219 LEU A CD2 1 ATOM 1700 N N . THR A 1 220 ? -34.454 37.149 56.020 1.00 19.84 ? 220 THR A N 1 ATOM 1701 C CA . THR A 1 220 ? -35.087 37.221 57.336 1.00 20.66 ? 220 THR A CA 1 ATOM 1702 C C . THR A 1 220 ? -34.459 36.061 58.125 1.00 19.96 ? 220 THR A C 1 ATOM 1703 O O . THR A 1 220 ? -34.517 34.919 57.672 1.00 18.44 ? 220 THR A O 1 ATOM 1704 C CB . THR A 1 220 ? -36.620 37.031 57.222 1.00 20.81 ? 220 THR A CB 1 ATOM 1705 O OG1 . THR A 1 220 ? -37.123 37.867 56.175 1.00 21.62 ? 220 THR A OG1 1 ATOM 1706 C CG2 . THR A 1 220 ? -37.329 37.399 58.529 1.00 21.37 ? 220 THR A CG2 1 ATOM 1707 N N . PRO A 1 221 ? -33.831 36.341 59.295 1.00 21.00 ? 221 PRO A N 1 ATOM 1708 C CA . PRO A 1 221 ? -33.192 35.298 60.116 1.00 20.47 ? 221 PRO A CA 1 ATOM 1709 C C . PRO A 1 221 ? -34.074 34.114 60.518 1.00 19.89 ? 221 PRO A C 1 ATOM 1710 O O . PRO A 1 221 ? -35.241 34.290 60.883 1.00 21.10 ? 221 PRO A O 1 ATOM 1711 C CB . PRO A 1 221 ? -32.708 36.076 61.340 1.00 22.02 ? 221 PRO A CB 1 ATOM 1712 C CG . PRO A 1 221 ? -32.430 37.426 60.788 1.00 21.35 ? 221 PRO A CG 1 ATOM 1713 C CD . PRO A 1 221 ? -33.635 37.663 59.923 1.00 19.55 ? 221 PRO A CD 1 ATOM 1714 N N . GLY A 1 222 ? -33.517 32.912 60.363 1.00 20.63 ? 222 GLY A N 1 ATOM 1715 C CA . GLY A 1 222 ? -34.208 31.678 60.712 1.00 21.60 ? 222 GLY A CA 1 ATOM 1716 C C . GLY A 1 222 ? -35.265 31.188 59.735 1.00 21.88 ? 222 GLY A C 1 ATOM 1717 O O . GLY A 1 222 ? -35.979 30.225 60.029 1.00 22.95 ? 222 GLY A O 1 ATOM 1718 N N . LYS A 1 223 ? -35.372 31.843 58.580 1.00 22.16 ? 223 LYS A N 1 ATOM 1719 C CA . LYS A 1 223 ? -36.363 31.464 57.570 1.00 22.04 ? 223 LYS A CA 1 ATOM 1720 C C . LYS A 1 223 ? -35.751 30.821 56.324 1.00 22.03 ? 223 LYS A C 1 ATOM 1721 O O . LYS A 1 223 ? -34.564 31.004 56.027 1.00 21.86 ? 223 LYS A O 1 ATOM 1722 C CB . LYS A 1 223 ? -37.220 32.677 57.166 1.00 23.12 ? 223 LYS A CB 1 ATOM 1723 C CG . LYS A 1 223 ? -37.968 33.383 58.309 1.00 24.23 ? 223 LYS A CG 1 ATOM 1724 C CD . LYS A 1 223 ? -39.007 32.499 58.979 1.00 25.54 ? 223 LYS A CD 1 ATOM 1725 C CE . LYS A 1 223 ? -39.686 33.223 60.131 1.00 27.32 ? 223 LYS A CE 1 ATOM 1726 N NZ . LYS A 1 223 ? -40.726 32.369 60.765 1.00 29.63 ? 223 LYS A NZ 1 ATOM 1727 N N . ARG A 1 224 ? -36.571 30.046 55.616 1.00 20.83 ? 224 ARG A N 1 ATOM 1728 C CA . ARG A 1 224 ? -36.154 29.374 54.387 1.00 21.05 ? 224 ARG A CA 1 ATOM 1729 C C . ARG A 1 224 ? -36.634 30.240 53.227 1.00 19.73 ? 224 ARG A C 1 ATOM 1730 O O . ARG A 1 224 ? -37.832 30.515 53.098 1.00 19.41 ? 224 ARG A O 1 ATOM 1731 C CB . ARG A 1 224 ? -36.751 27.966 54.293 1.00 22.09 ? 224 ARG A CB 1 ATOM 1732 C CG . ARG A 1 224 ? -36.499 27.061 55.494 1.00 25.09 ? 224 ARG A CG 1 ATOM 1733 C CD . ARG A 1 224 ? -37.780 26.857 56.277 1.00 27.88 ? 224 ARG A CD 1 ATOM 1734 N NE . ARG A 1 224 ? -38.185 25.457 56.355 1.00 31.30 ? 224 ARG A NE 1 ATOM 1735 C CZ . ARG A 1 224 ? -39.437 25.039 56.531 1.00 31.50 ? 224 ARG A CZ 1 ATOM 1736 N NH1 . ARG A 1 224 ? -40.437 25.909 56.640 1.00 32.34 ? 224 ARG A NH1 1 ATOM 1737 N NH2 . ARG A 1 224 ? -39.684 23.742 56.641 1.00 32.33 ? 224 ARG A NH2 1 ATOM 1738 N N . HIS A 1 225 ? -35.684 30.683 52.405 1.00 18.54 ? 225 HIS A N 1 ATOM 1739 C CA . HIS A 1 225 ? -35.963 31.565 51.270 1.00 17.06 ? 225 HIS A CA 1 ATOM 1740 C C . HIS A 1 225 ? -35.809 30.917 49.901 1.00 14.96 ? 225 HIS A C 1 ATOM 1741 O O . HIS A 1 225 ? -34.784 30.306 49.620 1.00 14.69 ? 225 HIS A O 1 ATOM 1742 C CB . HIS A 1 225 ? -35.024 32.775 51.304 1.00 17.41 ? 225 HIS A CB 1 ATOM 1743 C CG . HIS A 1 225 ? -35.074 33.563 52.574 1.00 17.64 ? 225 HIS A CG 1 ATOM 1744 N ND1 . HIS A 1 225 ? -34.478 33.131 53.738 1.00 17.77 ? 225 HIS A ND1 1 ATOM 1745 C CD2 . HIS A 1 225 ? -35.612 34.774 52.852 1.00 17.36 ? 225 HIS A CD2 1 ATOM 1746 C CE1 . HIS A 1 225 ? -34.646 34.042 54.679 1.00 17.50 ? 225 HIS A CE1 1 ATOM 1747 N NE2 . HIS A 1 225 ? -35.332 35.048 54.168 1.00 18.02 ? 225 HIS A NE2 1 ATOM 1748 N N . ARG A 1 226 ? -36.808 31.087 49.038 1.00 14.69 ? 226 ARG A N 1 ATOM 1749 C CA . ARG A 1 226 ? -36.721 30.551 47.677 1.00 14.39 ? 226 ARG A CA 1 ATOM 1750 C C . ARG A 1 226 ? -36.138 31.654 46.801 1.00 12.84 ? 226 ARG A C 1 ATOM 1751 O O . ARG A 1 226 ? -36.645 32.777 46.793 1.00 13.24 ? 226 ARG A O 1 ATOM 1752 C CB . ARG A 1 226 ? -38.085 30.122 47.121 1.00 15.01 ? 226 ARG A CB 1 ATOM 1753 C CG . ARG A 1 226 ? -38.008 29.431 45.744 1.00 13.49 ? 226 ARG A CG 1 ATOM 1754 C CD . ARG A 1 226 ? -39.378 29.293 45.118 1.00 14.72 ? 226 ARG A CD 1 ATOM 1755 N NE . ARG A 1 226 ? -39.360 28.565 43.849 1.00 15.99 ? 226 ARG A NE 1 ATOM 1756 C CZ . ARG A 1 226 ? -40.294 27.695 43.462 1.00 17.00 ? 226 ARG A CZ 1 ATOM 1757 N NH1 . ARG A 1 226 ? -41.336 27.424 44.245 1.00 14.88 ? 226 ARG A NH1 1 ATOM 1758 N NH2 . ARG A 1 226 ? -40.202 27.111 42.273 1.00 14.49 ? 226 ARG A NH2 1 ATOM 1759 N N . LEU A 1 227 ? -35.039 31.338 46.122 1.00 11.74 ? 227 LEU A N 1 ATOM 1760 C CA . LEU A 1 227 ? -34.384 32.285 45.230 1.00 9.60 ? 227 LEU A CA 1 ATOM 1761 C C . LEU A 1 227 ? -34.373 31.678 43.837 1.00 9.29 ? 227 LEU A C 1 ATOM 1762 O O . LEU A 1 227 ? -33.908 30.552 43.636 1.00 9.08 ? 227 LEU A O 1 ATOM 1763 C CB . LEU A 1 227 ? -32.957 32.592 45.698 1.00 8.94 ? 227 LEU A CB 1 ATOM 1764 C CG . LEU A 1 227 ? -32.224 33.716 44.961 1.00 7.65 ? 227 LEU A CG 1 ATOM 1765 C CD1 . LEU A 1 227 ? -32.841 35.068 45.291 1.00 9.87 ? 227 LEU A CD1 1 ATOM 1766 C CD2 . LEU A 1 227 ? -30.762 33.684 45.341 1.00 8.12 ? 227 LEU A CD2 1 ATOM 1767 N N . ARG A 1 228 ? -34.904 32.438 42.886 1.00 8.70 ? 228 ARG A N 1 ATOM 1768 C CA . ARG A 1 228 ? -35.012 32.005 41.500 1.00 9.08 ? 228 ARG A CA 1 ATOM 1769 C C . ARG A 1 228 ? -33.901 32.626 40.664 1.00 8.20 ? 228 ARG A C 1 ATOM 1770 O O . ARG A 1 228 ? -34.041 33.724 40.117 1.00 8.31 ? 228 ARG A O 1 ATOM 1771 C CB . ARG A 1 228 ? -36.398 32.367 40.974 1.00 7.59 ? 228 ARG A CB 1 ATOM 1772 C CG . ARG A 1 228 ? -37.536 31.874 41.861 1.00 8.26 ? 228 ARG A CG 1 ATOM 1773 C CD . ARG A 1 228 ? -38.853 32.509 41.482 1.00 7.19 ? 228 ARG A CD 1 ATOM 1774 N NE . ARG A 1 228 ? -39.959 32.004 42.290 1.00 10.24 ? 228 ARG A NE 1 ATOM 1775 C CZ . ARG A 1 228 ? -40.762 31.005 41.929 1.00 12.99 ? 228 ARG A CZ 1 ATOM 1776 N NH1 . ARG A 1 228 ? -40.587 30.386 40.764 1.00 13.12 ? 228 ARG A NH1 1 ATOM 1777 N NH2 . ARG A 1 228 ? -41.757 30.634 42.726 1.00 10.87 ? 228 ARG A NH2 1 ATOM 1778 N N . ILE A 1 229 ? -32.787 31.900 40.586 1.00 8.67 ? 229 ILE A N 1 ATOM 1779 C CA . ILE A 1 229 ? -31.591 32.336 39.864 1.00 7.25 ? 229 ILE A CA 1 ATOM 1780 C C . ILE A 1 229 ? -31.680 32.032 38.372 1.00 8.11 ? 229 ILE A C 1 ATOM 1781 O O . ILE A 1 229 ? -31.983 30.908 37.978 1.00 8.27 ? 229 ILE A O 1 ATOM 1782 C CB . ILE A 1 229 ? -30.302 31.674 40.436 1.00 7.54 ? 229 ILE A CB 1 ATOM 1783 C CG1 . ILE A 1 229 ? -30.307 31.726 41.974 1.00 6.97 ? 229 ILE A CG1 1 ATOM 1784 C CG2 . ILE A 1 229 ? -29.054 32.389 39.893 1.00 7.76 ? 229 ILE A CG2 1 ATOM 1785 C CD1 . ILE A 1 229 ? -29.123 31.046 42.646 1.00 8.19 ? 229 ILE A CD1 1 ATOM 1786 N N . LEU A 1 230 ? -31.427 33.051 37.556 1.00 7.65 ? 230 LEU A N 1 ATOM 1787 C CA . LEU A 1 230 ? -31.454 32.905 36.102 1.00 9.41 ? 230 LEU A CA 1 ATOM 1788 C C . LEU A 1 230 ? -30.167 33.417 35.499 1.00 9.27 ? 230 LEU A C 1 ATOM 1789 O O . LEU A 1 230 ? -29.519 34.289 36.069 1.00 11.52 ? 230 LEU A O 1 ATOM 1790 C CB . LEU A 1 230 ? -32.580 33.732 35.463 1.00 8.25 ? 230 LEU A CB 1 ATOM 1791 C CG . LEU A 1 230 ? -34.030 33.711 35.936 1.00 8.71 ? 230 LEU A CG 1 ATOM 1792 C CD1 . LEU A 1 230 ? -34.261 34.763 36.990 1.00 7.81 ? 230 LEU A CD1 1 ATOM 1793 C CD2 . LEU A 1 230 ? -34.938 33.954 34.756 1.00 7.21 ? 230 LEU A CD2 1 ATOM 1794 N N . ASN A 1 231 ? -29.797 32.850 34.353 1.00 8.57 ? 231 ASN A N 1 ATOM 1795 C CA . ASN A 1 231 ? -28.644 33.317 33.601 1.00 8.05 ? 231 ASN A CA 1 ATOM 1796 C C . ASN A 1 231 ? -29.259 33.803 32.293 1.00 6.74 ? 231 ASN A C 1 ATOM 1797 O O . ASN A 1 231 ? -29.584 33.008 31.410 1.00 6.90 ? 231 ASN A O 1 ATOM 1798 C CB . ASN A 1 231 ? -27.584 32.225 33.355 1.00 7.47 ? 231 ASN A CB 1 ATOM 1799 C CG . ASN A 1 231 ? -26.386 32.744 32.548 1.00 7.56 ? 231 ASN A CG 1 ATOM 1800 O OD1 . ASN A 1 231 ? -26.353 33.908 32.155 1.00 6.81 ? 231 ASN A OD1 1 ATOM 1801 N ND2 . ASN A 1 231 ? -25.396 31.893 32.325 1.00 5.91 ? 231 ASN A ND2 1 ATOM 1802 N N . THR A 1 232 ? -29.415 35.123 32.193 1.00 8.22 ? 232 THR A N 1 ATOM 1803 C CA . THR A 1 232 ? -30.009 35.763 31.023 1.00 9.03 ? 232 THR A CA 1 ATOM 1804 C C . THR A 1 232 ? -28.968 36.349 30.067 1.00 8.78 ? 232 THR A C 1 ATOM 1805 O O . THR A 1 232 ? -29.275 37.220 29.238 1.00 8.55 ? 232 THR A O 1 ATOM 1806 C CB . THR A 1 232 ? -31.022 36.860 31.444 1.00 9.11 ? 232 THR A CB 1 ATOM 1807 O OG1 . THR A 1 232 ? -30.347 37.893 32.159 1.00 9.07 ? 232 THR A OG1 1 ATOM 1808 C CG2 . THR A 1 232 ? -32.115 36.272 32.328 1.00 10.23 ? 232 THR A CG2 1 ATOM 1809 N N . SER A 1 233 ? -27.749 35.824 30.162 1.00 7.49 ? 233 SER A N 1 ATOM 1810 C CA . SER A 1 233 ? -26.613 36.261 29.349 1.00 7.51 ? 233 SER A CA 1 ATOM 1811 C C . SER A 1 233 ? -26.701 36.012 27.862 1.00 7.19 ? 233 SER A C 1 ATOM 1812 O O . SER A 1 233 ? -27.582 35.298 27.392 1.00 8.04 ? 233 SER A O 1 ATOM 1813 C CB . SER A 1 233 ? -25.329 35.582 29.829 1.00 7.87 ? 233 SER A CB 1 ATOM 1814 O OG . SER A 1 233 ? -24.881 36.117 31.058 1.00 9.01 ? 233 SER A OG 1 ATOM 1815 N N . THR A 1 234 ? -25.780 36.641 27.135 1.00 9.39 ? 234 THR A N 1 ATOM 1816 C CA . THR A 1 234 ? -25.648 36.449 25.702 1.00 9.20 ? 234 THR A CA 1 ATOM 1817 C C . THR A 1 234 ? -24.506 35.459 25.478 1.00 9.42 ? 234 THR A C 1 ATOM 1818 O O . THR A 1 234 ? -24.506 34.750 24.484 1.00 10.12 ? 234 THR A O 1 ATOM 1819 C CB . THR A 1 234 ? -25.349 37.756 24.942 1.00 9.03 ? 234 THR A CB 1 ATOM 1820 O OG1 . THR A 1 234 ? -24.382 38.542 25.651 1.00 11.74 ? 234 THR A OG1 1 ATOM 1821 C CG2 . THR A 1 234 ? -26.615 38.545 24.748 1.00 9.85 ? 234 THR A CG2 1 ATOM 1822 N N . GLU A 1 235 ? -23.557 35.397 26.421 1.00 8.70 ? 235 GLU A N 1 ATOM 1823 C CA . GLU A 1 235 ? -22.413 34.484 26.309 1.00 9.47 ? 235 GLU A CA 1 ATOM 1824 C C . GLU A 1 235 ? -21.921 33.888 27.629 1.00 9.03 ? 235 GLU A C 1 ATOM 1825 O O . GLU A 1 235 ? -21.594 32.701 27.683 1.00 7.18 ? 235 GLU A O 1 ATOM 1826 C CB . GLU A 1 235 ? -21.238 35.170 25.573 1.00 7.04 ? 235 GLU A CB 1 ATOM 1827 C CG . GLU A 1 235 ? -20.032 34.257 25.179 1.00 10.28 ? 235 GLU A CG 1 ATOM 1828 C CD . GLU A 1 235 ? -18.996 34.075 26.293 1.00 12.11 ? 235 GLU A CD 1 ATOM 1829 O OE1 . GLU A 1 235 ? -18.973 34.899 27.228 1.00 11.71 ? 235 GLU A OE1 1 ATOM 1830 O OE2 . GLU A 1 235 ? -18.234 33.087 26.258 1.00 13.77 ? 235 GLU A OE2 1 ATOM 1831 N N . ASN A 1 236 ? -21.769 34.725 28.652 1.00 9.42 ? 236 ASN A N 1 ATOM 1832 C CA . ASN A 1 236 ? -21.251 34.290 29.948 1.00 9.08 ? 236 ASN A CA 1 ATOM 1833 C C . ASN A 1 236 ? -22.012 33.174 30.662 1.00 9.71 ? 236 ASN A C 1 ATOM 1834 O O . ASN A 1 236 ? -23.243 33.210 30.779 1.00 7.84 ? 236 ASN A O 1 ATOM 1835 C CB . ASN A 1 236 ? -21.161 35.465 30.909 1.00 8.77 ? 236 ASN A CB 1 ATOM 1836 C CG . ASN A 1 236 ? -19.934 36.343 30.711 1.00 10.29 ? 236 ASN A CG 1 ATOM 1837 O OD1 . ASN A 1 236 ? -19.684 37.217 31.542 1.00 12.06 ? 236 ASN A OD1 1 ATOM 1838 N ND2 . ASN A 1 236 ? -19.198 36.158 29.625 1.00 8.21 ? 236 ASN A ND2 1 ATOM 1839 N N . HIS A 1 237 ? -21.247 32.182 31.110 1.00 8.10 ? 237 HIS A N 1 ATOM 1840 C CA . HIS A 1 237 ? -21.764 31.042 31.867 1.00 8.92 ? 237 HIS A CA 1 ATOM 1841 C C . HIS A 1 237 ? -21.227 31.248 33.273 1.00 9.62 ? 237 HIS A C 1 ATOM 1842 O O . HIS A 1 237 ? -20.011 31.361 33.471 1.00 9.84 ? 237 HIS A O 1 ATOM 1843 C CB . HIS A 1 237 ? -21.223 29.737 31.325 1.00 6.89 ? 237 HIS A CB 1 ATOM 1844 C CG . HIS A 1 237 ? -21.693 29.399 29.949 1.00 8.74 ? 237 HIS A CG 1 ATOM 1845 N ND1 . HIS A 1 237 ? -21.511 30.239 28.874 1.00 8.08 ? 237 HIS A ND1 1 ATOM 1846 C CD2 . HIS A 1 237 ? -22.264 28.275 29.458 1.00 7.66 ? 237 HIS A CD2 1 ATOM 1847 C CE1 . HIS A 1 237 ? -21.947 29.643 27.779 1.00 9.80 ? 237 HIS A CE1 1 ATOM 1848 N NE2 . HIS A 1 237 ? -22.410 28.451 28.106 1.00 9.71 ? 237 HIS A NE2 1 ATOM 1849 N N . PHE A 1 238 ? -22.131 31.234 34.247 1.00 9.91 ? 238 PHE A N 1 ATOM 1850 C CA . PHE A 1 238 ? -21.774 31.504 35.631 1.00 10.00 ? 238 PHE A CA 1 ATOM 1851 C C . PHE A 1 238 ? -21.739 30.380 36.631 1.00 11.07 ? 238 PHE A C 1 ATOM 1852 O O . PHE A 1 238 ? -22.470 29.395 36.524 1.00 12.05 ? 238 PHE A O 1 ATOM 1853 C CB . PHE A 1 238 ? -22.735 32.543 36.224 1.00 10.58 ? 238 PHE A CB 1 ATOM 1854 C CG . PHE A 1 238 ? -22.909 33.763 35.391 1.00 9.05 ? 238 PHE A CG 1 ATOM 1855 C CD1 . PHE A 1 238 ? -21.814 34.581 35.074 1.00 9.43 ? 238 PHE A CD1 1 ATOM 1856 C CD2 . PHE A 1 238 ? -24.179 34.121 34.933 1.00 9.01 ? 238 PHE A CD2 1 ATOM 1857 C CE1 . PHE A 1 238 ? -21.983 35.748 34.314 1.00 8.14 ? 238 PHE A CE1 1 ATOM 1858 C CE2 . PHE A 1 238 ? -24.362 35.292 34.163 1.00 9.09 ? 238 PHE A CE2 1 ATOM 1859 C CZ . PHE A 1 238 ? -23.266 36.107 33.854 1.00 3.95 ? 238 PHE A CZ 1 ATOM 1860 N N . GLN A 1 239 ? -20.909 30.601 37.648 1.00 10.33 ? 239 GLN A N 1 ATOM 1861 C CA . GLN A 1 239 ? -20.794 29.721 38.798 1.00 11.44 ? 239 GLN A CA 1 ATOM 1862 C C . GLN A 1 239 ? -21.247 30.655 39.909 1.00 11.54 ? 239 GLN A C 1 ATOM 1863 O O . GLN A 1 239 ? -20.810 31.807 39.967 1.00 12.56 ? 239 GLN A O 1 ATOM 1864 C CB . GLN A 1 239 ? -19.357 29.272 39.055 1.00 9.51 ? 239 GLN A CB 1 ATOM 1865 C CG . GLN A 1 239 ? -18.775 28.424 37.950 1.00 10.90 ? 239 GLN A CG 1 ATOM 1866 C CD . GLN A 1 239 ? -17.401 27.861 38.259 1.00 10.64 ? 239 GLN A CD 1 ATOM 1867 O OE1 . GLN A 1 239 ? -16.970 26.916 37.610 1.00 10.70 ? 239 GLN A OE1 1 ATOM 1868 N NE2 . GLN A 1 239 ? -16.691 28.458 39.217 1.00 9.73 ? 239 GLN A NE2 1 ATOM 1869 N N . VAL A 1 240 ? -22.228 30.227 40.695 1.00 12.79 ? 240 VAL A N 1 ATOM 1870 C CA . VAL A 1 240 ? -22.712 31.059 41.794 1.00 12.57 ? 240 VAL A CA 1 ATOM 1871 C C . VAL A 1 240 ? -22.550 30.375 43.141 1.00 12.32 ? 240 VAL A C 1 ATOM 1872 O O . VAL A 1 240 ? -22.656 29.161 43.234 1.00 9.75 ? 240 VAL A O 1 ATOM 1873 C CB . VAL A 1 240 ? -24.182 31.537 41.603 1.00 12.25 ? 240 VAL A CB 1 ATOM 1874 C CG1 . VAL A 1 240 ? -24.306 32.396 40.354 1.00 9.33 ? 240 VAL A CG1 1 ATOM 1875 C CG2 . VAL A 1 240 ? -25.169 30.362 41.574 1.00 11.66 ? 240 VAL A CG2 1 ATOM 1876 N N . SER A 1 241 ? -22.277 31.172 44.170 1.00 13.16 ? 241 SER A N 1 ATOM 1877 C CA . SER A 1 241 ? -22.099 30.673 45.531 1.00 13.28 ? 241 SER A CA 1 ATOM 1878 C C . SER A 1 241 ? -22.360 31.781 46.524 1.00 13.47 ? 241 SER A C 1 ATOM 1879 O O . SER A 1 241 ? -22.186 32.961 46.212 1.00 13.26 ? 241 SER A O 1 ATOM 1880 C CB . SER A 1 241 ? -20.678 30.129 45.745 1.00 12.17 ? 241 SER A CB 1 ATOM 1881 O OG . SER A 1 241 ? -19.694 31.096 45.410 1.00 13.96 ? 241 SER A OG 1 ATOM 1882 N N . LEU A 1 242 ? -22.818 31.390 47.708 1.00 12.66 ? 242 LEU A N 1 ATOM 1883 C CA . LEU A 1 242 ? -23.070 32.333 48.783 1.00 12.44 ? 242 LEU A CA 1 ATOM 1884 C C . LEU A 1 242 ? -22.148 31.927 49.923 1.00 12.62 ? 242 LEU A C 1 ATOM 1885 O O . LEU A 1 242 ? -22.147 30.763 50.337 1.00 13.51 ? 242 LEU A O 1 ATOM 1886 C CB . LEU A 1 242 ? -24.543 32.304 49.213 1.00 11.76 ? 242 LEU A CB 1 ATOM 1887 C CG . LEU A 1 242 ? -25.033 33.235 50.337 1.00 13.03 ? 242 LEU A CG 1 ATOM 1888 C CD1 . LEU A 1 242 ? -24.692 34.682 50.088 1.00 12.83 ? 242 LEU A CD1 1 ATOM 1889 C CD2 . LEU A 1 242 ? -26.532 33.070 50.488 1.00 15.10 ? 242 LEU A CD2 1 ATOM 1890 N N . VAL A 1 243 ? -21.354 32.886 50.404 1.00 14.12 ? 243 VAL A N 1 ATOM 1891 C CA . VAL A 1 243 ? -20.401 32.670 51.502 1.00 15.23 ? 243 VAL A CA 1 ATOM 1892 C C . VAL A 1 243 ? -21.117 32.159 52.756 1.00 16.40 ? 243 VAL A C 1 ATOM 1893 O O . VAL A 1 243 ? -22.148 32.705 53.157 1.00 16.04 ? 243 VAL A O 1 ATOM 1894 C CB . VAL A 1 243 ? -19.580 33.973 51.814 1.00 14.56 ? 243 VAL A CB 1 ATOM 1895 C CG1 . VAL A 1 243 ? -18.632 33.767 53.011 1.00 14.66 ? 243 VAL A CG1 1 ATOM 1896 C CG2 . VAL A 1 243 ? -18.758 34.377 50.588 1.00 14.59 ? 243 VAL A CG2 1 ATOM 1897 N N . ASN A 1 244 ? -20.601 31.038 53.274 1.00 19.39 ? 244 ASN A N 1 ATOM 1898 C CA . ASN A 1 244 ? -21.087 30.330 54.469 1.00 22.15 ? 244 ASN A CA 1 ATOM 1899 C C . ASN A 1 244 ? -22.487 29.723 54.401 1.00 21.03 ? 244 ASN A C 1 ATOM 1900 O O . ASN A 1 244 ? -23.064 29.347 55.425 1.00 19.36 ? 244 ASN A O 1 ATOM 1901 C CB . ASN A 1 244 ? -20.909 31.182 55.742 1.00 27.35 ? 244 ASN A CB 1 ATOM 1902 C CG . ASN A 1 244 ? -19.489 31.128 56.285 1.00 34.78 ? 244 ASN A CG 1 ATOM 1903 O OD1 . ASN A 1 244 ? -18.548 30.789 55.558 1.00 34.12 ? 244 ASN A OD1 1 ATOM 1904 N ND2 . ASN A 1 244 ? -19.326 31.444 57.570 1.00 40.75 ? 244 ASN A ND2 1 ATOM 1905 N N . HIS A 1 245 ? -23.031 29.628 53.189 1.00 18.76 ? 245 HIS A N 1 ATOM 1906 C CA . HIS A 1 245 ? -24.359 29.057 52.991 1.00 17.53 ? 245 HIS A CA 1 ATOM 1907 C C . HIS A 1 245 ? -24.378 28.054 51.867 1.00 18.35 ? 245 HIS A C 1 ATOM 1908 O O . HIS A 1 245 ? -23.613 28.152 50.899 1.00 17.20 ? 245 HIS A O 1 ATOM 1909 C CB . HIS A 1 245 ? -25.401 30.117 52.637 1.00 17.50 ? 245 HIS A CB 1 ATOM 1910 C CG . HIS A 1 245 ? -25.658 31.124 53.712 1.00 17.81 ? 245 HIS A CG 1 ATOM 1911 N ND1 . HIS A 1 245 ? -24.751 32.109 54.038 1.00 18.44 ? 245 HIS A ND1 1 ATOM 1912 C CD2 . HIS A 1 245 ? -26.741 31.334 54.495 1.00 17.84 ? 245 HIS A CD2 1 ATOM 1913 C CE1 . HIS A 1 245 ? -25.268 32.883 54.974 1.00 18.50 ? 245 HIS A CE1 1 ATOM 1914 N NE2 . HIS A 1 245 ? -26.474 32.435 55.269 1.00 19.90 ? 245 HIS A NE2 1 ATOM 1915 N N . THR A 1 246 ? -25.283 27.093 52.004 1.00 16.26 ? 246 THR A N 1 ATOM 1916 C CA . THR A 1 246 ? -25.490 26.085 50.984 1.00 16.12 ? 246 THR A CA 1 ATOM 1917 C C . THR A 1 246 ? -26.753 26.522 50.248 1.00 14.87 ? 246 THR A C 1 ATOM 1918 O O . THR A 1 246 ? -27.470 27.426 50.701 1.00 13.73 ? 246 THR A O 1 ATOM 1919 C CB . THR A 1 246 ? -25.702 24.679 51.590 1.00 16.01 ? 246 THR A CB 1 ATOM 1920 O OG1 . THR A 1 246 ? -26.764 24.715 52.550 1.00 15.61 ? 246 THR A OG1 1 ATOM 1921 C CG2 . THR A 1 246 ? -24.426 24.163 52.242 1.00 17.71 ? 246 THR A CG2 1 ATOM 1922 N N . MET A 1 247 ? -26.969 25.951 49.071 1.00 14.92 ? 247 MET A N 1 ATOM 1923 C CA . MET A 1 247 ? -28.153 26.245 48.274 1.00 14.01 ? 247 MET A CA 1 ATOM 1924 C C . MET A 1 247 ? -28.789 24.904 47.976 1.00 13.24 ? 247 MET A C 1 ATOM 1925 O O . MET A 1 247 ? -28.105 23.969 47.556 1.00 14.36 ? 247 MET A O 1 ATOM 1926 C CB . MET A 1 247 ? -27.785 26.956 46.968 1.00 14.81 ? 247 MET A CB 1 ATOM 1927 C CG . MET A 1 247 ? -27.266 28.383 47.133 1.00 14.94 ? 247 MET A CG 1 ATOM 1928 S SD . MET A 1 247 ? -26.863 29.180 45.565 1.00 16.84 ? 247 MET A SD 1 ATOM 1929 C CE . MET A 1 247 ? -25.384 28.367 45.133 1.00 16.06 ? 247 MET A CE 1 ATOM 1930 N N . THR A 1 248 ? -30.081 24.790 48.257 1.00 12.77 ? 248 THR A N 1 ATOM 1931 C CA . THR A 1 248 ? -30.790 23.549 48.001 1.00 12.98 ? 248 THR A CA 1 ATOM 1932 C C . THR A 1 248 ? -31.664 23.716 46.768 1.00 11.46 ? 248 THR A C 1 ATOM 1933 O O . THR A 1 248 ? -32.679 24.407 46.804 1.00 13.49 ? 248 THR A O 1 ATOM 1934 C CB . THR A 1 248 ? -31.602 23.082 49.234 1.00 14.16 ? 248 THR A CB 1 ATOM 1935 O OG1 . THR A 1 248 ? -30.723 22.984 50.360 1.00 16.43 ? 248 THR A OG1 1 ATOM 1936 C CG2 . THR A 1 248 ? -32.211 21.703 48.994 1.00 13.76 ? 248 THR A CG2 1 ATOM 1937 N N . VAL A 1 249 ? -31.243 23.065 45.686 1.00 11.95 ? 249 VAL A N 1 ATOM 1938 C CA . VAL A 1 249 ? -31.934 23.105 44.397 1.00 11.36 ? 249 VAL A CA 1 ATOM 1939 C C . VAL A 1 249 ? -33.270 22.380 44.472 1.00 10.65 ? 249 VAL A C 1 ATOM 1940 O O . VAL A 1 249 ? -33.332 21.227 44.899 1.00 9.49 ? 249 VAL A O 1 ATOM 1941 C CB . VAL A 1 249 ? -31.072 22.454 43.286 1.00 11.99 ? 249 VAL A CB 1 ATOM 1942 C CG1 . VAL A 1 249 ? -31.756 22.563 41.935 1.00 9.99 ? 249 VAL A CG1 1 ATOM 1943 C CG2 . VAL A 1 249 ? -29.702 23.096 43.237 1.00 10.41 ? 249 VAL A CG2 1 ATOM 1944 N N . ILE A 1 250 ? -34.335 23.087 44.099 1.00 10.73 ? 250 ILE A N 1 ATOM 1945 C CA . ILE A 1 250 ? -35.675 22.509 44.087 1.00 11.08 ? 250 ILE A CA 1 ATOM 1946 C C . ILE A 1 250 ? -36.263 22.471 42.677 1.00 11.31 ? 250 ILE A C 1 ATOM 1947 O O . ILE A 1 250 ? -37.318 21.870 42.458 1.00 11.43 ? 250 ILE A O 1 ATOM 1948 C CB . ILE A 1 250 ? -36.637 23.199 45.085 1.00 11.40 ? 250 ILE A CB 1 ATOM 1949 C CG1 . ILE A 1 250 ? -36.769 24.698 44.797 1.00 9.88 ? 250 ILE A CG1 1 ATOM 1950 C CG2 . ILE A 1 250 ? -36.168 22.929 46.508 1.00 9.84 ? 250 ILE A CG2 1 ATOM 1951 C CD1 . ILE A 1 250 ? -37.986 25.341 45.437 1.00 9.74 ? 250 ILE A CD1 1 ATOM 1952 N N . ALA A 1 251 ? -35.559 23.111 41.738 1.00 10.54 ? 251 ALA A N 1 ATOM 1953 C CA . ALA A 1 251 ? -35.933 23.152 40.322 1.00 10.60 ? 251 ALA A CA 1 ATOM 1954 C C . ALA A 1 251 ? -34.745 23.457 39.409 1.00 9.99 ? 251 ALA A C 1 ATOM 1955 O O . ALA A 1 251 ? -33.856 24.221 39.775 1.00 11.44 ? 251 ALA A O 1 ATOM 1956 C CB . ALA A 1 251 ? -37.063 24.149 40.072 1.00 8.19 ? 251 ALA A CB 1 ATOM 1957 N N . ALA A 1 252 ? -34.720 22.796 38.251 1.00 9.52 ? 252 ALA A N 1 ATOM 1958 C CA . ALA A 1 252 ? -33.687 22.967 37.228 1.00 9.12 ? 252 ALA A CA 1 ATOM 1959 C C . ALA A 1 252 ? -34.492 23.464 36.042 1.00 9.68 ? 252 ALA A C 1 ATOM 1960 O O . ALA A 1 252 ? -35.387 22.765 35.567 1.00 8.24 ? 252 ALA A O 1 ATOM 1961 C CB . ALA A 1 252 ? -33.016 21.638 36.913 1.00 8.99 ? 252 ALA A CB 1 ATOM 1962 N N . ASP A 1 253 ? -34.191 24.684 35.593 1.00 10.86 ? 253 ASP A N 1 ATOM 1963 C CA . ASP A 1 253 ? -34.928 25.363 34.518 1.00 10.71 ? 253 ASP A CA 1 ATOM 1964 C C . ASP A 1 253 ? -36.385 25.469 34.992 1.00 11.61 ? 253 ASP A C 1 ATOM 1965 O O . ASP A 1 253 ? -36.617 25.951 36.107 1.00 11.80 ? 253 ASP A O 1 ATOM 1966 C CB . ASP A 1 253 ? -34.761 24.675 33.144 1.00 10.66 ? 253 ASP A CB 1 ATOM 1967 C CG . ASP A 1 253 ? -33.348 24.831 32.575 1.00 11.13 ? 253 ASP A CG 1 ATOM 1968 O OD1 . ASP A 1 253 ? -32.526 25.552 33.179 1.00 10.50 ? 253 ASP A OD1 1 ATOM 1969 O OD2 . ASP A 1 253 ? -33.051 24.220 31.527 1.00 11.53 ? 253 ASP A OD2 1 ATOM 1970 N N . MET A 1 254 ? -37.344 24.944 34.233 1.00 11.24 ? 254 MET A N 1 ATOM 1971 C CA . MET A 1 254 ? -38.735 25.007 34.670 1.00 13.01 ? 254 MET A CA 1 ATOM 1972 C C . MET A 1 254 ? -39.247 23.628 35.104 1.00 12.10 ? 254 MET A C 1 ATOM 1973 O O . MET A 1 254 ? -40.447 23.341 35.062 1.00 10.93 ? 254 MET A O 1 ATOM 1974 C CB . MET A 1 254 ? -39.613 25.615 33.579 1.00 14.07 ? 254 MET A CB 1 ATOM 1975 C CG . MET A 1 254 ? -40.663 26.549 34.140 1.00 14.96 ? 254 MET A CG 1 ATOM 1976 S SD . MET A 1 254 ? -41.734 27.195 32.879 1.00 18.04 ? 254 MET A SD 1 ATOM 1977 C CE . MET A 1 254 ? -42.514 28.480 33.802 1.00 14.41 ? 254 MET A CE 1 ATOM 1978 N N . VAL A 1 255 ? -38.319 22.790 35.555 1.00 10.69 ? 255 VAL A N 1 ATOM 1979 C CA . VAL A 1 255 ? -38.646 21.440 35.990 1.00 12.29 ? 255 VAL A CA 1 ATOM 1980 C C . VAL A 1 255 ? -38.308 21.227 37.462 1.00 10.56 ? 255 VAL A C 1 ATOM 1981 O O . VAL A 1 255 ? -37.141 21.290 37.843 1.00 11.59 ? 255 VAL A O 1 ATOM 1982 C CB . VAL A 1 255 ? -37.922 20.363 35.121 1.00 12.06 ? 255 VAL A CB 1 ATOM 1983 C CG1 . VAL A 1 255 ? -38.224 18.946 35.618 1.00 11.92 ? 255 VAL A CG1 1 ATOM 1984 C CG2 . VAL A 1 255 ? -38.355 20.476 33.669 1.00 13.72 ? 255 VAL A CG2 1 ATOM 1985 N N . PRO A 1 256 ? -39.329 20.939 38.300 1.00 12.07 ? 256 PRO A N 1 ATOM 1986 C CA . PRO A 1 256 ? -39.153 20.697 39.737 1.00 12.23 ? 256 PRO A CA 1 ATOM 1987 C C . PRO A 1 256 ? -38.347 19.425 39.963 1.00 11.40 ? 256 PRO A C 1 ATOM 1988 O O . PRO A 1 256 ? -38.613 18.400 39.334 1.00 11.56 ? 256 PRO A O 1 ATOM 1989 C CB . PRO A 1 256 ? -40.581 20.518 40.225 1.00 12.52 ? 256 PRO A CB 1 ATOM 1990 C CG . PRO A 1 256 ? -41.342 21.365 39.306 1.00 10.76 ? 256 PRO A CG 1 ATOM 1991 C CD . PRO A 1 256 ? -40.769 21.004 37.985 1.00 11.20 ? 256 PRO A CD 1 ATOM 1992 N N . VAL A 1 257 ? -37.302 19.534 40.779 1.00 11.63 ? 257 VAL A N 1 ATOM 1993 C CA . VAL A 1 257 ? -36.444 18.397 41.084 1.00 10.53 ? 257 VAL A CA 1 ATOM 1994 C C . VAL A 1 257 ? -36.445 18.111 42.576 1.00 11.62 ? 257 VAL A C 1 ATOM 1995 O O . VAL A 1 257 ? -36.840 18.965 43.367 1.00 9.81 ? 257 VAL A O 1 ATOM 1996 C CB . VAL A 1 257 ? -34.963 18.590 40.564 1.00 9.49 ? 257 VAL A CB 1 ATOM 1997 C CG1 . VAL A 1 257 ? -34.934 18.758 39.051 1.00 10.06 ? 257 VAL A CG1 1 ATOM 1998 C CG2 . VAL A 1 257 ? -34.265 19.756 41.244 1.00 10.90 ? 257 VAL A CG2 1 ATOM 1999 N N . ASN A 1 258 ? -36.030 16.899 42.953 1.00 13.37 ? 258 ASN A N 1 ATOM 2000 C CA . ASN A 1 258 ? -35.933 16.514 44.366 1.00 13.95 ? 258 ASN A CA 1 ATOM 2001 C C . ASN A 1 258 ? -34.817 17.368 44.968 1.00 14.97 ? 258 ASN A C 1 ATOM 2002 O O . ASN A 1 258 ? -33.852 17.713 44.266 1.00 13.43 ? 258 ASN A O 1 ATOM 2003 C CB . ASN A 1 258 ? -35.571 15.030 44.513 1.00 14.93 ? 258 ASN A CB 1 ATOM 2004 C CG . ASN A 1 258 ? -36.630 14.101 43.940 1.00 14.98 ? 258 ASN A CG 1 ATOM 2005 O OD1 . ASN A 1 258 ? -37.831 14.321 44.107 1.00 16.74 ? 258 ASN A OD1 1 ATOM 2006 N ND2 . ASN A 1 258 ? -36.183 13.050 43.265 1.00 15.10 ? 258 ASN A ND2 1 ATOM 2007 N N . ALA A 1 259 ? -34.984 17.746 46.237 1.00 14.92 ? 259 ALA A N 1 ATOM 2008 C CA . ALA A 1 259 ? -34.023 18.573 46.974 1.00 16.48 ? 259 ALA A CA 1 ATOM 2009 C C . ALA A 1 259 ? -32.572 18.109 46.826 1.00 16.68 ? 259 ALA A C 1 ATOM 2010 O O . ALA A 1 259 ? -32.265 16.935 47.047 1.00 18.31 ? 259 ALA A O 1 ATOM 2011 C CB . ALA A 1 259 ? -34.413 18.628 48.445 1.00 16.59 ? 259 ALA A CB 1 ATOM 2012 N N . MET A 1 260 ? -31.716 19.016 46.354 1.00 15.74 ? 260 MET A N 1 ATOM 2013 C CA . MET A 1 260 ? -30.300 18.722 46.153 1.00 17.52 ? 260 MET A CA 1 ATOM 2014 C C . MET A 1 260 ? -29.438 19.865 46.686 1.00 17.90 ? 260 MET A C 1 ATOM 2015 O O . MET A 1 260 ? -29.302 20.918 46.052 1.00 17.09 ? 260 MET A O 1 ATOM 2016 C CB . MET A 1 260 ? -30.008 18.457 44.670 1.00 17.09 ? 260 MET A CB 1 ATOM 2017 C CG . MET A 1 260 ? -28.629 17.872 44.405 1.00 17.81 ? 260 MET A CG 1 ATOM 2018 S SD . MET A 1 260 ? -28.277 17.745 42.659 1.00 22.36 ? 260 MET A SD 1 ATOM 2019 C CE . MET A 1 260 ? -27.795 19.397 42.300 1.00 17.37 ? 260 MET A CE 1 ATOM 2020 N N . THR A 1 261 ? -28.847 19.625 47.854 1.00 17.99 ? 261 THR A N 1 ATOM 2021 C CA . THR A 1 261 ? -27.998 20.590 48.545 1.00 17.84 ? 261 THR A CA 1 ATOM 2022 C C . THR A 1 261 ? -26.582 20.624 47.966 1.00 17.37 ? 261 THR A C 1 ATOM 2023 O O . THR A 1 261 ? -25.922 19.588 47.849 1.00 18.97 ? 261 THR A O 1 ATOM 2024 C CB . THR A 1 261 ? -27.996 20.291 50.069 1.00 18.61 ? 261 THR A CB 1 ATOM 2025 O OG1 . THR A 1 261 ? -29.346 20.316 50.551 1.00 17.38 ? 261 THR A OG1 1 ATOM 2026 C CG2 . THR A 1 261 ? -27.194 21.320 50.842 1.00 15.82 ? 261 THR A CG2 1 ATOM 2027 N N . VAL A 1 262 ? -26.164 21.822 47.547 1.00 16.87 ? 262 VAL A N 1 ATOM 2028 C CA . VAL A 1 262 ? -24.842 22.071 46.956 1.00 15.69 ? 262 VAL A CA 1 ATOM 2029 C C . VAL A 1 262 ? -24.180 23.328 47.537 1.00 14.78 ? 262 VAL A C 1 ATOM 2030 O O . VAL A 1 262 ? -24.851 24.173 48.131 1.00 14.19 ? 262 VAL A O 1 ATOM 2031 C CB . VAL A 1 262 ? -24.919 22.250 45.395 1.00 16.51 ? 262 VAL A CB 1 ATOM 2032 C CG1 . VAL A 1 262 ? -25.268 20.942 44.709 1.00 16.51 ? 262 VAL A CG1 1 ATOM 2033 C CG2 . VAL A 1 262 ? -25.924 23.332 45.023 1.00 15.27 ? 262 VAL A CG2 1 ATOM 2034 N N . ASP A 1 263 ? -22.873 23.459 47.313 1.00 13.70 ? 263 ASP A N 1 ATOM 2035 C CA . ASP A 1 263 ? -22.093 24.614 47.778 1.00 14.58 ? 263 ASP A CA 1 ATOM 2036 C C . ASP A 1 263 ? -22.074 25.705 46.712 1.00 13.87 ? 263 ASP A C 1 ATOM 2037 O O . ASP A 1 263 ? -21.969 26.898 47.020 1.00 13.09 ? 263 ASP A O 1 ATOM 2038 C CB . ASP A 1 263 ? -20.643 24.204 48.080 1.00 16.81 ? 263 ASP A CB 1 ATOM 2039 C CG . ASP A 1 263 ? -20.527 23.274 49.276 1.00 17.97 ? 263 ASP A CG 1 ATOM 2040 O OD1 . ASP A 1 263 ? -21.277 23.454 50.261 1.00 17.21 ? 263 ASP A OD1 1 ATOM 2041 O OD2 . ASP A 1 263 ? -19.668 22.368 49.228 1.00 21.05 ? 263 ASP A OD2 1 ATOM 2042 N N . SER A 1 264 ? -22.128 25.266 45.456 1.00 13.80 ? 264 SER A N 1 ATOM 2043 C CA . SER A 1 264 ? -22.113 26.152 44.300 1.00 14.95 ? 264 SER A CA 1 ATOM 2044 C C . SER A 1 264 ? -22.869 25.547 43.130 1.00 15.21 ? 264 SER A C 1 ATOM 2045 O O . SER A 1 264 ? -23.047 24.328 43.060 1.00 14.29 ? 264 SER A O 1 ATOM 2046 C CB . SER A 1 264 ? -20.677 26.466 43.873 1.00 15.54 ? 264 SER A CB 1 ATOM 2047 O OG . SER A 1 264 ? -19.961 25.293 43.540 1.00 17.01 ? 264 SER A OG 1 ATOM 2048 N N . LEU A 1 265 ? -23.308 26.411 42.215 1.00 14.38 ? 265 LEU A N 1 ATOM 2049 C CA . LEU A 1 265 ? -24.054 25.991 41.036 1.00 13.78 ? 265 LEU A CA 1 ATOM 2050 C C . LEU A 1 265 ? -23.546 26.589 39.753 1.00 13.74 ? 265 LEU A C 1 ATOM 2051 O O . LEU A 1 265 ? -23.174 27.760 39.713 1.00 14.30 ? 265 LEU A O 1 ATOM 2052 C CB . LEU A 1 265 ? -25.519 26.396 41.153 1.00 14.91 ? 265 LEU A CB 1 ATOM 2053 C CG . LEU A 1 265 ? -26.485 25.504 41.910 1.00 16.42 ? 265 LEU A CG 1 ATOM 2054 C CD1 . LEU A 1 265 ? -27.772 26.262 42.091 1.00 16.70 ? 265 LEU A CD1 1 ATOM 2055 C CD2 . LEU A 1 265 ? -26.697 24.188 41.173 1.00 17.80 ? 265 LEU A CD2 1 ATOM 2056 N N . PHE A 1 266 ? -23.570 25.784 38.697 1.00 12.54 ? 266 PHE A N 1 ATOM 2057 C CA . PHE A 1 266 ? -23.184 26.251 37.377 1.00 11.39 ? 266 PHE A CA 1 ATOM 2058 C C . PHE A 1 266 ? -24.464 26.543 36.601 1.00 11.88 ? 266 PHE A C 1 ATOM 2059 O O . PHE A 1 266 ? -25.334 25.672 36.473 1.00 11.89 ? 266 PHE A O 1 ATOM 2060 C CB . PHE A 1 266 ? -22.362 25.203 36.615 1.00 11.37 ? 266 PHE A CB 1 ATOM 2061 C CG . PHE A 1 266 ? -21.961 25.640 35.229 1.00 10.60 ? 266 PHE A CG 1 ATOM 2062 C CD1 . PHE A 1 266 ? -20.885 26.523 35.043 1.00 8.30 ? 266 PHE A CD1 1 ATOM 2063 C CD2 . PHE A 1 266 ? -22.696 25.217 34.103 1.00 9.59 ? 266 PHE A CD2 1 ATOM 2064 C CE1 . PHE A 1 266 ? -20.551 26.981 33.756 1.00 9.25 ? 266 PHE A CE1 1 ATOM 2065 C CE2 . PHE A 1 266 ? -22.375 25.663 32.812 1.00 10.20 ? 266 PHE A CE2 1 ATOM 2066 C CZ . PHE A 1 266 ? -21.306 26.545 32.636 1.00 7.79 ? 266 PHE A CZ 1 ATOM 2067 N N . LEU A 1 267 ? -24.543 27.754 36.055 1.00 11.23 ? 267 LEU A N 1 ATOM 2068 C CA . LEU A 1 267 ? -25.678 28.161 35.237 1.00 10.85 ? 267 LEU A CA 1 ATOM 2069 C C . LEU A 1 267 ? -25.212 28.513 33.838 1.00 9.49 ? 267 LEU A C 1 ATOM 2070 O O . LEU A 1 267 ? -24.516 29.508 33.633 1.00 11.06 ? 267 LEU A O 1 ATOM 2071 C CB . LEU A 1 267 ? -26.417 29.370 35.823 1.00 10.10 ? 267 LEU A CB 1 ATOM 2072 C CG . LEU A 1 267 ? -27.332 29.172 37.024 1.00 10.11 ? 267 LEU A CG 1 ATOM 2073 C CD1 . LEU A 1 267 ? -26.579 29.548 38.282 1.00 9.65 ? 267 LEU A CD1 1 ATOM 2074 C CD2 . LEU A 1 267 ? -28.571 30.022 36.874 1.00 8.07 ? 267 LEU A CD2 1 ATOM 2075 N N . ALA A 1 268 ? -25.583 27.673 32.875 1.00 9.80 ? 268 ALA A N 1 ATOM 2076 C CA . ALA A 1 268 ? -25.270 27.918 31.468 1.00 8.27 ? 268 ALA A CA 1 ATOM 2077 C C . ALA A 1 268 ? -26.164 29.055 30.990 1.00 7.76 ? 268 ALA A C 1 ATOM 2078 O O . ALA A 1 268 ? -27.086 29.451 31.707 1.00 6.34 ? 268 ALA A O 1 ATOM 2079 C CB . ALA A 1 268 ? -25.549 26.683 30.647 1.00 8.63 ? 268 ALA A CB 1 ATOM 2080 N N . VAL A 1 269 ? -25.888 29.591 29.802 1.00 8.91 ? 269 VAL A N 1 ATOM 2081 C CA . VAL A 1 269 ? -26.713 30.666 29.236 1.00 8.92 ? 269 VAL A CA 1 ATOM 2082 C C . VAL A 1 269 ? -28.126 30.120 29.036 1.00 8.11 ? 269 VAL A C 1 ATOM 2083 O O . VAL A 1 269 ? -28.310 29.057 28.442 1.00 9.84 ? 269 VAL A O 1 ATOM 2084 C CB . VAL A 1 269 ? -26.155 31.177 27.890 1.00 8.57 ? 269 VAL A CB 1 ATOM 2085 C CG1 . VAL A 1 269 ? -27.062 32.248 27.289 1.00 6.52 ? 269 VAL A CG1 1 ATOM 2086 C CG2 . VAL A 1 269 ? -24.792 31.757 28.102 1.00 8.14 ? 269 VAL A CG2 1 ATOM 2087 N N . GLY A 1 270 ? -29.089 30.801 29.644 1.00 6.86 ? 270 GLY A N 1 ATOM 2088 C CA . GLY A 1 270 ? -30.474 30.388 29.532 1.00 9.08 ? 270 GLY A CA 1 ATOM 2089 C C . GLY A 1 270 ? -30.966 29.479 30.637 1.00 10.10 ? 270 GLY A C 1 ATOM 2090 O O . GLY A 1 270 ? -32.171 29.245 30.738 1.00 10.81 ? 270 GLY A O 1 ATOM 2091 N N . GLN A 1 271 ? -30.042 28.947 31.439 1.00 8.89 ? 271 GLN A N 1 ATOM 2092 C CA . GLN A 1 271 ? -30.399 28.063 32.545 1.00 10.54 ? 271 GLN A CA 1 ATOM 2093 C C . GLN A 1 271 ? -30.921 28.806 33.760 1.00 10.05 ? 271 GLN A C 1 ATOM 2094 O O . GLN A 1 271 ? -30.699 30.013 33.912 1.00 8.99 ? 271 GLN A O 1 ATOM 2095 C CB . GLN A 1 271 ? -29.232 27.164 32.961 1.00 11.32 ? 271 GLN A CB 1 ATOM 2096 C CG . GLN A 1 271 ? -29.143 25.875 32.170 1.00 8.66 ? 271 GLN A CG 1 ATOM 2097 C CD . GLN A 1 271 ? -28.063 24.922 32.650 1.00 8.32 ? 271 GLN A CD 1 ATOM 2098 O OE1 . GLN A 1 271 ? -27.142 25.304 33.368 1.00 8.58 ? 271 GLN A OE1 1 ATOM 2099 N NE2 . GLN A 1 271 ? -28.168 23.663 32.233 1.00 6.03 ? 271 GLN A NE2 1 ATOM 2100 N N . ARG A 1 272 ? -31.736 28.095 34.537 1.00 8.58 ? 272 ARG A N 1 ATOM 2101 C CA . ARG A 1 272 ? -32.323 28.611 35.765 1.00 10.59 ? 272 ARG A CA 1 ATOM 2102 C C . ARG A 1 272 ? -32.238 27.550 36.848 1.00 11.26 ? 272 ARG A C 1 ATOM 2103 O O . ARG A 1 272 ? -32.176 26.350 36.562 1.00 9.50 ? 272 ARG A O 1 ATOM 2104 C CB . ARG A 1 272 ? -33.814 28.974 35.611 1.00 10.58 ? 272 ARG A CB 1 ATOM 2105 C CG . ARG A 1 272 ? -34.165 30.159 34.737 1.00 10.57 ? 272 ARG A CG 1 ATOM 2106 C CD . ARG A 1 272 ? -34.315 29.809 33.270 1.00 7.02 ? 272 ARG A CD 1 ATOM 2107 N NE . ARG A 1 272 ? -35.524 29.044 32.995 1.00 10.21 ? 272 ARG A NE 1 ATOM 2108 C CZ . ARG A 1 272 ? -35.650 28.161 32.010 1.00 10.18 ? 272 ARG A CZ 1 ATOM 2109 N NH1 . ARG A 1 272 ? -34.630 27.914 31.191 1.00 8.23 ? 272 ARG A NH1 1 ATOM 2110 N NH2 . ARG A 1 272 ? -36.794 27.503 31.858 1.00 8.67 ? 272 ARG A NH2 1 ATOM 2111 N N . TYR A 1 273 ? -32.216 28.018 38.091 1.00 11.63 ? 273 TYR A N 1 ATOM 2112 C CA . TYR A 1 273 ? -32.203 27.159 39.270 1.00 12.05 ? 273 TYR A CA 1 ATOM 2113 C C . TYR A 1 273 ? -32.977 27.841 40.375 1.00 12.79 ? 273 TYR A C 1 ATOM 2114 O O . TYR A 1 273 ? -32.709 29.002 40.703 1.00 13.40 ? 273 TYR A O 1 ATOM 2115 C CB . TYR A 1 273 ? -30.787 26.862 39.777 1.00 11.04 ? 273 TYR A CB 1 ATOM 2116 C CG . TYR A 1 273 ? -30.077 25.739 39.063 1.00 11.04 ? 273 TYR A CG 1 ATOM 2117 C CD1 . TYR A 1 273 ? -30.573 24.418 39.101 1.00 10.01 ? 273 TYR A CD1 1 ATOM 2118 C CD2 . TYR A 1 273 ? -28.910 25.989 38.325 1.00 10.08 ? 273 TYR A CD2 1 ATOM 2119 C CE1 . TYR A 1 273 ? -29.912 23.364 38.410 1.00 7.52 ? 273 TYR A CE1 1 ATOM 2120 C CE2 . TYR A 1 273 ? -28.242 24.950 37.632 1.00 9.77 ? 273 TYR A CE2 1 ATOM 2121 C CZ . TYR A 1 273 ? -28.751 23.645 37.683 1.00 9.44 ? 273 TYR A CZ 1 ATOM 2122 O OH . TYR A 1 273 ? -28.094 22.644 37.021 1.00 9.05 ? 273 TYR A OH 1 ATOM 2123 N N . ASP A 1 274 ? -34.002 27.151 40.873 1.00 12.48 ? 274 ASP A N 1 ATOM 2124 C CA . ASP A 1 274 ? -34.791 27.649 41.993 1.00 12.20 ? 274 ASP A CA 1 ATOM 2125 C C . ASP A 1 274 ? -34.130 26.997 43.188 1.00 11.70 ? 274 ASP A C 1 ATOM 2126 O O . ASP A 1 274 ? -34.006 25.768 43.240 1.00 10.83 ? 274 ASP A O 1 ATOM 2127 C CB . ASP A 1 274 ? -36.247 27.199 41.916 1.00 14.85 ? 274 ASP A CB 1 ATOM 2128 C CG . ASP A 1 274 ? -37.048 27.974 40.904 1.00 18.27 ? 274 ASP A CG 1 ATOM 2129 O OD1 . ASP A 1 274 ? -38.029 28.620 41.310 1.00 22.61 ? 274 ASP A OD1 1 ATOM 2130 O OD2 . ASP A 1 274 ? -36.713 27.932 39.708 1.00 21.54 ? 274 ASP A OD2 1 ATOM 2131 N N . VAL A 1 275 ? -33.602 27.819 44.085 1.00 11.79 ? 275 VAL A N 1 ATOM 2132 C CA . VAL A 1 275 ? -32.930 27.300 45.268 1.00 11.87 ? 275 VAL A CA 1 ATOM 2133 C C . VAL A 1 275 ? -33.579 27.745 46.557 1.00 12.22 ? 275 VAL A C 1 ATOM 2134 O O . VAL A 1 275 ? -34.307 28.728 46.577 1.00 12.31 ? 275 VAL A O 1 ATOM 2135 C CB . VAL A 1 275 ? -31.418 27.680 45.315 1.00 12.28 ? 275 VAL A CB 1 ATOM 2136 C CG1 . VAL A 1 275 ? -30.677 27.066 44.149 1.00 10.14 ? 275 VAL A CG1 1 ATOM 2137 C CG2 . VAL A 1 275 ? -31.219 29.192 45.348 1.00 7.75 ? 275 VAL A CG2 1 ATOM 2138 N N . VAL A 1 276 ? -33.339 26.979 47.618 1.00 12.53 ? 276 VAL A N 1 ATOM 2139 C CA . VAL A 1 276 ? -33.840 27.310 48.945 1.00 12.30 ? 276 VAL A CA 1 ATOM 2140 C C . VAL A 1 276 ? -32.604 27.574 49.797 1.00 12.26 ? 276 VAL A C 1 ATOM 2141 O O . VAL A 1 276 ? -31.710 26.736 49.893 1.00 11.19 ? 276 VAL A O 1 ATOM 2142 C CB . VAL A 1 276 ? -34.744 26.198 49.561 1.00 12.57 ? 276 VAL A CB 1 ATOM 2143 C CG1 . VAL A 1 276 ? -35.131 26.550 50.999 1.00 12.90 ? 276 VAL A CG1 1 ATOM 2144 C CG2 . VAL A 1 276 ? -36.028 26.058 48.746 1.00 12.26 ? 276 VAL A CG2 1 ATOM 2145 N N . ILE A 1 277 ? -32.529 28.798 50.312 1.00 13.53 ? 277 ILE A N 1 ATOM 2146 C CA . ILE A 1 277 ? -31.434 29.245 51.162 1.00 15.10 ? 277 ILE A CA 1 ATOM 2147 C C . ILE A 1 277 ? -31.993 29.442 52.569 1.00 17.47 ? 277 ILE A C 1 ATOM 2148 O O . ILE A 1 277 ? -32.947 30.199 52.773 1.00 17.91 ? 277 ILE A O 1 ATOM 2149 C CB . ILE A 1 277 ? -30.796 30.578 50.629 1.00 13.73 ? 277 ILE A CB 1 ATOM 2150 C CG1 . ILE A 1 277 ? -30.185 30.347 49.235 1.00 15.05 ? 277 ILE A CG1 1 ATOM 2151 C CG2 . ILE A 1 277 ? -29.703 31.090 51.593 1.00 14.20 ? 277 ILE A CG2 1 ATOM 2152 C CD1 . ILE A 1 277 ? -29.757 31.613 48.500 1.00 15.02 ? 277 ILE A CD1 1 ATOM 2153 N N . ASP A 1 278 ? -31.406 28.727 53.522 1.00 19.93 ? 278 ASP A N 1 ATOM 2154 C CA . ASP A 1 278 ? -31.808 28.812 54.919 1.00 21.99 ? 278 ASP A CA 1 ATOM 2155 C C . ASP A 1 278 ? -30.953 29.870 55.588 1.00 21.88 ? 278 ASP A C 1 ATOM 2156 O O . ASP A 1 278 ? -29.720 29.797 55.545 1.00 22.28 ? 278 ASP A O 1 ATOM 2157 C CB . ASP A 1 278 ? -31.606 27.467 55.635 1.00 24.39 ? 278 ASP A CB 1 ATOM 2158 C CG . ASP A 1 278 ? -32.494 26.356 55.091 1.00 27.53 ? 278 ASP A CG 1 ATOM 2159 O OD1 . ASP A 1 278 ? -33.379 26.631 54.252 1.00 29.09 ? 278 ASP A OD1 1 ATOM 2160 O OD2 . ASP A 1 278 ? -32.302 25.193 55.513 1.00 30.38 ? 278 ASP A OD2 1 ATOM 2161 N N . ALA A 1 279 ? -31.610 30.860 56.189 1.00 22.13 ? 279 ALA A N 1 ATOM 2162 C CA . ALA A 1 279 ? -30.919 31.935 56.898 1.00 23.52 ? 279 ALA A CA 1 ATOM 2163 C C . ALA A 1 279 ? -30.558 31.408 58.296 1.00 23.98 ? 279 ALA A C 1 ATOM 2164 O O . ALA A 1 279 ? -30.969 31.947 59.328 1.00 23.61 ? 279 ALA A O 1 ATOM 2165 C CB . ALA A 1 279 ? -31.804 33.172 56.974 1.00 23.73 ? 279 ALA A CB 1 ATOM 2166 N N . SER A 1 280 ? -29.762 30.341 58.274 1.00 25.32 ? 280 SER A N 1 ATOM 2167 C CA . SER A 1 280 ? -29.305 29.602 59.442 1.00 26.42 ? 280 SER A CA 1 ATOM 2168 C C . SER A 1 280 ? -28.021 30.093 60.107 1.00 25.74 ? 280 SER A C 1 ATOM 2169 O O . SER A 1 280 ? -27.711 29.686 61.229 1.00 25.65 ? 280 SER A O 1 ATOM 2170 C CB . SER A 1 280 ? -29.150 28.123 59.060 1.00 26.00 ? 280 SER A CB 1 ATOM 2171 O OG . SER A 1 280 ? -28.195 27.941 58.028 1.00 31.32 ? 280 SER A OG 1 ATOM 2172 N N . ARG A 1 281 ? -27.274 30.945 59.411 1.00 25.81 ? 281 ARG A N 1 ATOM 2173 C CA . ARG A 1 281 ? -26.015 31.471 59.930 1.00 25.83 ? 281 ARG A CA 1 ATOM 2174 C C . ARG A 1 281 ? -26.164 32.727 60.782 1.00 24.63 ? 281 ARG A C 1 ATOM 2175 O O . ARG A 1 281 ? -27.276 33.218 60.997 1.00 24.29 ? 281 ARG A O 1 ATOM 2176 C CB . ARG A 1 281 ? -25.015 31.696 58.788 1.00 27.95 ? 281 ARG A CB 1 ATOM 2177 C CG . ARG A 1 281 ? -24.582 30.425 58.052 1.00 31.80 ? 281 ARG A CG 1 ATOM 2178 C CD . ARG A 1 281 ? -23.924 29.405 58.982 1.00 36.93 ? 281 ARG A CD 1 ATOM 2179 N NE . ARG A 1 281 ? -22.993 28.512 58.292 1.00 41.23 ? 281 ARG A NE 1 ATOM 2180 C CZ . ARG A 1 281 ? -21.745 28.266 58.690 1.00 42.73 ? 281 ARG A CZ 1 ATOM 2181 N NH1 . ARG A 1 281 ? -21.258 28.840 59.784 1.00 42.02 ? 281 ARG A NH1 1 ATOM 2182 N NH2 . ARG A 1 281 ? -20.973 27.451 57.981 1.00 44.55 ? 281 ARG A NH2 1 ATOM 2183 N N . ALA A 1 282 ? -25.034 33.207 61.300 1.00 24.84 ? 282 ALA A N 1 ATOM 2184 C CA . ALA A 1 282 ? -24.968 34.395 62.149 1.00 24.79 ? 282 ALA A CA 1 ATOM 2185 C C . ALA A 1 282 ? -25.352 35.670 61.394 1.00 25.40 ? 282 ALA A C 1 ATOM 2186 O O . ALA A 1 282 ? -25.001 35.811 60.216 1.00 24.99 ? 282 ALA A O 1 ATOM 2187 C CB . ALA A 1 282 ? -23.563 34.529 62.733 1.00 26.59 ? 282 ALA A CB 1 ATOM 2188 N N . PRO A 1 283 ? -26.135 36.578 62.033 1.00 25.36 ? 283 PRO A N 1 ATOM 2189 C CA . PRO A 1 283 ? -26.553 37.836 61.399 1.00 25.30 ? 283 PRO A CA 1 ATOM 2190 C C . PRO A 1 283 ? -25.367 38.682 60.938 1.00 25.04 ? 283 PRO A C 1 ATOM 2191 O O . PRO A 1 283 ? -24.587 39.189 61.750 1.00 26.16 ? 283 PRO A O 1 ATOM 2192 C CB . PRO A 1 283 ? -27.371 38.513 62.496 1.00 26.61 ? 283 PRO A CB 1 ATOM 2193 C CG . PRO A 1 283 ? -28.015 37.354 63.167 1.00 26.01 ? 283 PRO A CG 1 ATOM 2194 C CD . PRO A 1 283 ? -26.846 36.409 63.318 1.00 25.77 ? 283 PRO A CD 1 ATOM 2195 N N . ASP A 1 284 ? -25.218 38.763 59.615 1.00 22.68 ? 284 ASP A N 1 ATOM 2196 C CA . ASP A 1 284 ? -24.121 39.485 58.974 1.00 20.80 ? 284 ASP A CA 1 ATOM 2197 C C . ASP A 1 284 ? -24.495 39.731 57.506 1.00 19.85 ? 284 ASP A C 1 ATOM 2198 O O . ASP A 1 284 ? -25.606 39.423 57.068 1.00 18.21 ? 284 ASP A O 1 ATOM 2199 C CB . ASP A 1 284 ? -22.849 38.609 59.044 1.00 20.66 ? 284 ASP A CB 1 ATOM 2200 C CG . ASP A 1 284 ? -21.550 39.401 58.976 1.00 20.67 ? 284 ASP A CG 1 ATOM 2201 O OD1 . ASP A 1 284 ? -21.547 40.577 58.555 1.00 20.19 ? 284 ASP A OD1 1 ATOM 2202 O OD2 . ASP A 1 284 ? -20.509 38.811 59.336 1.00 22.84 ? 284 ASP A OD2 1 ATOM 2203 N N . ASN A 1 285 ? -23.562 40.338 56.779 1.00 19.13 ? 285 ASN A N 1 ATOM 2204 C CA . ASN A 1 285 ? -23.696 40.622 55.360 1.00 19.65 ? 285 ASN A CA 1 ATOM 2205 C C . ASN A 1 285 ? -22.773 39.610 54.687 1.00 19.38 ? 285 ASN A C 1 ATOM 2206 O O . ASN A 1 285 ? -21.599 39.497 55.054 1.00 18.39 ? 285 ASN A O 1 ATOM 2207 C CB . ASN A 1 285 ? -23.235 42.049 55.054 1.00 20.30 ? 285 ASN A CB 1 ATOM 2208 C CG . ASN A 1 285 ? -24.109 43.099 55.698 1.00 20.73 ? 285 ASN A CG 1 ATOM 2209 O OD1 . ASN A 1 285 ? -25.302 43.180 55.422 1.00 20.33 ? 285 ASN A OD1 1 ATOM 2210 N ND2 . ASN A 1 285 ? -23.515 43.919 56.553 1.00 21.30 ? 285 ASN A ND2 1 ATOM 2211 N N . TYR A 1 286 ? -23.312 38.840 53.742 1.00 18.45 ? 286 TYR A N 1 ATOM 2212 C CA . TYR A 1 286 ? -22.529 37.819 53.039 1.00 17.66 ? 286 TYR A CA 1 ATOM 2213 C C . TYR A 1 286 ? -22.476 38.043 51.533 1.00 16.31 ? 286 TYR A C 1 ATOM 2214 O O . TYR A 1 286 ? -23.467 38.464 50.934 1.00 16.79 ? 286 TYR A O 1 ATOM 2215 C CB . TYR A 1 286 ? -23.090 36.424 53.325 1.00 17.18 ? 286 TYR A CB 1 ATOM 2216 C CG . TYR A 1 286 ? -23.016 35.997 54.773 1.00 17.17 ? 286 TYR A CG 1 ATOM 2217 C CD1 . TYR A 1 286 ? -21.875 35.335 55.276 1.00 17.75 ? 286 TYR A CD1 1 ATOM 2218 C CD2 . TYR A 1 286 ? -24.097 36.226 55.649 1.00 16.83 ? 286 TYR A CD2 1 ATOM 2219 C CE1 . TYR A 1 286 ? -21.811 34.902 56.629 1.00 18.20 ? 286 TYR A CE1 1 ATOM 2220 C CE2 . TYR A 1 286 ? -24.047 35.796 57.005 1.00 15.77 ? 286 TYR A CE2 1 ATOM 2221 C CZ . TYR A 1 286 ? -22.904 35.136 57.482 1.00 17.29 ? 286 TYR A CZ 1 ATOM 2222 O OH . TYR A 1 286 ? -22.857 34.712 58.789 1.00 18.42 ? 286 TYR A OH 1 ATOM 2223 N N . TRP A 1 287 ? -21.320 37.760 50.928 1.00 14.90 ? 287 TRP A N 1 ATOM 2224 C CA . TRP A 1 287 ? -21.153 37.918 49.479 1.00 15.84 ? 287 TRP A CA 1 ATOM 2225 C C . TRP A 1 287 ? -21.767 36.774 48.686 1.00 14.42 ? 287 TRP A C 1 ATOM 2226 O O . TRP A 1 287 ? -21.614 35.604 49.040 1.00 12.91 ? 287 TRP A O 1 ATOM 2227 C CB . TRP A 1 287 ? -19.674 37.980 49.050 1.00 14.80 ? 287 TRP A CB 1 ATOM 2228 C CG . TRP A 1 287 ? -18.859 39.205 49.393 1.00 15.24 ? 287 TRP A CG 1 ATOM 2229 C CD1 . TRP A 1 287 ? -17.707 39.216 50.128 1.00 13.61 ? 287 TRP A CD1 1 ATOM 2230 C CD2 . TRP A 1 287 ? -19.062 40.560 48.953 1.00 15.10 ? 287 TRP A CD2 1 ATOM 2231 N NE1 . TRP A 1 287 ? -17.176 40.478 50.175 1.00 14.82 ? 287 TRP A NE1 1 ATOM 2232 C CE2 . TRP A 1 287 ? -17.980 41.329 49.467 1.00 16.06 ? 287 TRP A CE2 1 ATOM 2233 C CE3 . TRP A 1 287 ? -20.049 41.207 48.174 1.00 16.86 ? 287 TRP A CE3 1 ATOM 2234 C CZ2 . TRP A 1 287 ? -17.850 42.718 49.231 1.00 16.36 ? 287 TRP A CZ2 1 ATOM 2235 C CZ3 . TRP A 1 287 ? -19.923 42.598 47.936 1.00 16.79 ? 287 TRP A CZ3 1 ATOM 2236 C CH2 . TRP A 1 287 ? -18.826 43.333 48.468 1.00 17.90 ? 287 TRP A CH2 1 ATOM 2237 N N . PHE A 1 288 ? -22.498 37.137 47.636 1.00 14.91 ? 288 PHE A N 1 ATOM 2238 C CA . PHE A 1 288 ? -23.075 36.169 46.712 1.00 13.50 ? 288 PHE A CA 1 ATOM 2239 C C . PHE A 1 288 ? -22.096 36.341 45.565 1.00 13.92 ? 288 PHE A C 1 ATOM 2240 O O . PHE A 1 288 ? -22.071 37.388 44.920 1.00 14.72 ? 288 PHE A O 1 ATOM 2241 C CB . PHE A 1 288 ? -24.483 36.573 46.282 1.00 14.76 ? 288 PHE A CB 1 ATOM 2242 C CG . PHE A 1 288 ? -25.127 35.623 45.300 1.00 14.45 ? 288 PHE A CG 1 ATOM 2243 C CD1 . PHE A 1 288 ? -25.818 34.481 45.755 1.00 13.89 ? 288 PHE A CD1 1 ATOM 2244 C CD2 . PHE A 1 288 ? -25.071 35.880 43.913 1.00 14.63 ? 288 PHE A CD2 1 ATOM 2245 C CE1 . PHE A 1 288 ? -26.454 33.604 44.842 1.00 14.51 ? 288 PHE A CE1 1 ATOM 2246 C CE2 . PHE A 1 288 ? -25.696 35.016 42.988 1.00 13.50 ? 288 PHE A CE2 1 ATOM 2247 C CZ . PHE A 1 288 ? -26.394 33.873 43.452 1.00 14.80 ? 288 PHE A CZ 1 ATOM 2248 N N . ASN A 1 289 ? -21.280 35.324 45.336 1.00 12.20 ? 289 ASN A N 1 ATOM 2249 C CA . ASN A 1 289 ? -20.263 35.397 44.305 1.00 13.45 ? 289 ASN A CA 1 ATOM 2250 C C . ASN A 1 289 ? -20.541 34.775 42.963 1.00 12.88 ? 289 ASN A C 1 ATOM 2251 O O . ASN A 1 289 ? -20.993 33.636 42.870 1.00 11.55 ? 289 ASN A O 1 ATOM 2252 C CB . ASN A 1 289 ? -18.953 34.844 44.845 1.00 13.16 ? 289 ASN A CB 1 ATOM 2253 C CG . ASN A 1 289 ? -18.347 35.747 45.876 1.00 15.17 ? 289 ASN A CG 1 ATOM 2254 O OD1 . ASN A 1 289 ? -18.470 35.517 47.077 1.00 14.64 ? 289 ASN A OD1 1 ATOM 2255 N ND2 . ASN A 1 289 ? -17.689 36.788 45.379 1.00 16.05 ? 289 ASN A ND2 1 ATOM 2256 N N . VAL A 1 290 ? -20.240 35.548 41.925 1.00 12.45 ? 290 VAL A N 1 ATOM 2257 C CA . VAL A 1 290 ? -20.369 35.091 40.552 1.00 11.47 ? 290 VAL A CA 1 ATOM 2258 C C . VAL A 1 290 ? -18.927 34.865 40.103 1.00 10.72 ? 290 VAL A C 1 ATOM 2259 O O . VAL A 1 290 ? -18.121 35.802 40.075 1.00 12.33 ? 290 VAL A O 1 ATOM 2260 C CB . VAL A 1 290 ? -21.105 36.120 39.659 1.00 10.47 ? 290 VAL A CB 1 ATOM 2261 C CG1 . VAL A 1 290 ? -20.938 35.777 38.199 1.00 13.47 ? 290 VAL A CG1 1 ATOM 2262 C CG2 . VAL A 1 290 ? -22.593 36.131 39.994 1.00 11.14 ? 290 VAL A CG2 1 ATOM 2263 N N . THR A 1 291 ? -18.593 33.602 39.842 1.00 9.82 ? 291 THR A N 1 ATOM 2264 C CA . THR A 1 291 ? -17.251 33.225 39.406 1.00 9.32 ? 291 THR A CA 1 ATOM 2265 C C . THR A 1 291 ? -17.281 32.468 38.084 1.00 10.46 ? 291 THR A C 1 ATOM 2266 O O . THR A 1 291 ? -18.348 32.059 37.610 1.00 8.52 ? 291 THR A O 1 ATOM 2267 C CB . THR A 1 291 ? -16.513 32.354 40.464 1.00 11.60 ? 291 THR A CB 1 ATOM 2268 O OG1 . THR A 1 291 ? -17.307 31.206 40.780 1.00 10.31 ? 291 THR A OG1 1 ATOM 2269 C CG2 . THR A 1 291 ? -16.232 33.144 41.743 1.00 10.18 ? 291 THR A CG2 1 ATOM 2270 N N . PHE A 1 292 ? -16.101 32.313 37.484 1.00 9.92 ? 292 PHE A N 1 ATOM 2271 C CA . PHE A 1 292 ? -15.950 31.611 36.218 1.00 11.82 ? 292 PHE A CA 1 ATOM 2272 C C . PHE A 1 292 ? -14.985 30.452 36.349 1.00 14.19 ? 292 PHE A C 1 ATOM 2273 O O . PHE A 1 292 ? -13.958 30.544 37.032 1.00 14.84 ? 292 PHE A O 1 ATOM 2274 C CB . PHE A 1 292 ? -15.446 32.563 35.122 1.00 11.87 ? 292 PHE A CB 1 ATOM 2275 C CG . PHE A 1 292 ? -16.417 33.648 34.774 1.00 12.57 ? 292 PHE A CG 1 ATOM 2276 C CD1 . PHE A 1 292 ? -17.462 33.405 33.861 1.00 12.08 ? 292 PHE A CD1 1 ATOM 2277 C CD2 . PHE A 1 292 ? -16.319 34.910 35.383 1.00 9.18 ? 292 PHE A CD2 1 ATOM 2278 C CE1 . PHE A 1 292 ? -18.406 34.409 33.559 1.00 11.35 ? 292 PHE A CE1 1 ATOM 2279 C CE2 . PHE A 1 292 ? -17.257 35.931 35.097 1.00 11.27 ? 292 PHE A CE2 1 ATOM 2280 C CZ . PHE A 1 292 ? -18.303 35.684 34.183 1.00 12.50 ? 292 PHE A CZ 1 ATOM 2281 N N . GLY A 1 293 ? -15.348 29.353 35.703 1.00 14.15 ? 293 GLY A N 1 ATOM 2282 C CA . GLY A 1 293 ? -14.517 28.171 35.702 1.00 16.01 ? 293 GLY A CA 1 ATOM 2283 C C . GLY A 1 293 ? -14.337 27.754 34.262 1.00 17.27 ? 293 GLY A C 1 ATOM 2284 O O . GLY A 1 293 ? -14.660 28.522 33.352 1.00 17.47 ? 293 GLY A O 1 ATOM 2285 N N . GLY A 1 294 ? -13.815 26.548 34.053 1.00 17.03 ? 294 GLY A N 1 ATOM 2286 C CA . GLY A 1 294 ? -13.592 26.047 32.706 1.00 17.98 ? 294 GLY A CA 1 ATOM 2287 C C . GLY A 1 294 ? -12.492 26.757 31.962 1.00 18.59 ? 294 GLY A C 1 ATOM 2288 O O . GLY A 1 294 ? -12.431 26.699 30.737 1.00 18.46 ? 294 GLY A O 1 ATOM 2289 N N . GLN A 1 295 ? -11.649 27.456 32.723 1.00 20.30 ? 295 GLN A N 1 ATOM 2290 C CA . GLN A 1 295 ? -10.517 28.230 32.216 1.00 23.57 ? 295 GLN A CA 1 ATOM 2291 C C . GLN A 1 295 ? -10.887 29.165 31.044 1.00 22.56 ? 295 GLN A C 1 ATOM 2292 O O . GLN A 1 295 ? -10.266 29.134 29.974 1.00 22.82 ? 295 GLN A O 1 ATOM 2293 C CB . GLN A 1 295 ? -9.347 27.293 31.859 1.00 27.98 ? 295 GLN A CB 1 ATOM 2294 C CG . GLN A 1 295 ? -8.880 26.307 32.959 1.00 34.75 ? 295 GLN A CG 1 ATOM 2295 C CD . GLN A 1 295 ? -8.350 26.963 34.232 1.00 39.35 ? 295 GLN A CD 1 ATOM 2296 O OE1 . GLN A 1 295 ? -7.833 28.082 34.215 1.00 43.42 ? 295 GLN A OE1 1 ATOM 2297 N NE2 . GLN A 1 295 ? -8.460 26.244 35.345 1.00 41.29 ? 295 GLN A NE2 1 ATOM 2298 N N . ALA A 1 296 ? -11.942 29.957 31.265 1.00 21.32 ? 296 ALA A N 1 ATOM 2299 C CA . ALA A 1 296 ? -12.512 30.925 30.306 1.00 20.79 ? 296 ALA A CA 1 ATOM 2300 C C . ALA A 1 296 ? -13.086 30.366 28.994 1.00 18.29 ? 296 ALA A C 1 ATOM 2301 O O . ALA A 1 296 ? -13.367 31.126 28.061 1.00 20.64 ? 296 ALA A O 1 ATOM 2302 C CB . ALA A 1 296 ? -11.533 32.063 30.014 1.00 19.89 ? 296 ALA A CB 1 ATOM 2303 N N . ALA A 1 297 ? -13.316 29.053 28.951 1.00 15.13 ? 297 ALA A N 1 ATOM 2304 C CA . ALA A 1 297 ? -13.858 28.390 27.764 1.00 13.35 ? 297 ALA A CA 1 ATOM 2305 C C . ALA A 1 297 ? -15.330 28.725 27.537 1.00 10.80 ? 297 ALA A C 1 ATOM 2306 O O . ALA A 1 297 ? -15.838 28.584 26.423 1.00 9.74 ? 297 ALA A O 1 ATOM 2307 C CB . ALA A 1 297 ? -13.664 26.889 27.857 1.00 14.04 ? 297 ALA A CB 1 ATOM 2308 N N . CYS A 1 298 ? -16.005 29.164 28.597 1.00 9.49 ? 298 CYS A N 1 ATOM 2309 C CA . CYS A 1 298 ? -17.407 29.552 28.495 1.00 10.23 ? 298 CYS A CA 1 ATOM 2310 C C . CYS A 1 298 ? -17.680 30.930 29.093 1.00 10.86 ? 298 CYS A C 1 ATOM 2311 O O . CYS A 1 298 ? -18.733 31.175 29.700 1.00 10.34 ? 298 CYS A O 1 ATOM 2312 C CB . CYS A 1 298 ? -18.327 28.473 29.073 1.00 9.51 ? 298 CYS A CB 1 ATOM 2313 S SG . CYS A 1 298 ? -18.048 28.033 30.812 1.00 12.50 ? 298 CYS A SG 1 ATOM 2314 N N . GLY A 1 299 ? -16.704 31.821 28.917 1.00 10.17 ? 299 GLY A N 1 ATOM 2315 C CA . GLY A 1 299 ? -16.834 33.187 29.387 1.00 9.18 ? 299 GLY A CA 1 ATOM 2316 C C . GLY A 1 299 ? -15.949 33.680 30.506 1.00 9.14 ? 299 GLY A C 1 ATOM 2317 O O . GLY A 1 299 ? -15.309 32.908 31.229 1.00 7.44 ? 299 GLY A O 1 ATOM 2318 N N . GLY A 1 300 ? -15.972 35.002 30.654 1.00 8.22 ? 300 GLY A N 1 ATOM 2319 C CA . GLY A 1 300 ? -15.219 35.692 31.681 1.00 9.31 ? 300 GLY A CA 1 ATOM 2320 C C . GLY A 1 300 ? -15.682 37.133 31.720 1.00 8.08 ? 300 GLY A C 1 ATOM 2321 O O . GLY A 1 300 ? -16.397 37.577 30.814 1.00 9.29 ? 300 GLY A O 1 ATOM 2322 N N . SER A 1 301 ? -15.266 37.866 32.749 1.00 9.30 ? 301 SER A N 1 ATOM 2323 C CA . SER A 1 301 ? -15.635 39.273 32.897 1.00 10.18 ? 301 SER A CA 1 ATOM 2324 C C . SER A 1 301 ? -14.443 40.150 33.223 1.00 11.67 ? 301 SER A C 1 ATOM 2325 O O . SER A 1 301 ? -13.472 39.685 33.831 1.00 11.37 ? 301 SER A O 1 ATOM 2326 C CB . SER A 1 301 ? -16.691 39.453 33.988 1.00 9.85 ? 301 SER A CB 1 ATOM 2327 O OG . SER A 1 301 ? -17.266 40.751 33.936 1.00 12.46 ? 301 SER A OG 1 ATOM 2328 N N . LEU A 1 302 ? -14.534 41.422 32.814 1.00 12.25 ? 302 LEU A N 1 ATOM 2329 C CA . LEU A 1 302 ? -13.498 42.418 33.083 1.00 11.89 ? 302 LEU A CA 1 ATOM 2330 C C . LEU A 1 302 ? -13.640 42.894 34.527 1.00 12.38 ? 302 LEU A C 1 ATOM 2331 O O . LEU A 1 302 ? -12.765 43.580 35.047 1.00 14.25 ? 302 LEU A O 1 ATOM 2332 C CB . LEU A 1 302 ? -13.536 43.580 32.078 1.00 12.00 ? 302 LEU A CB 1 ATOM 2333 C CG . LEU A 1 302 ? -13.157 43.242 30.623 1.00 13.16 ? 302 LEU A CG 1 ATOM 2334 C CD1 . LEU A 1 302 ? -13.146 44.506 29.772 1.00 13.15 ? 302 LEU A CD1 1 ATOM 2335 C CD2 . LEU A 1 302 ? -11.795 42.549 30.553 1.00 12.76 ? 302 LEU A CD2 1 ATOM 2336 N N . ASN A 1 303 ? -14.779 42.550 35.142 1.00 12.58 ? 303 ASN A N 1 ATOM 2337 C CA . ASN A 1 303 ? -15.034 42.805 36.560 1.00 11.89 ? 303 ASN A CA 1 ATOM 2338 C C . ASN A 1 303 ? -14.523 41.470 37.131 1.00 12.83 ? 303 ASN A C 1 ATOM 2339 O O . ASN A 1 303 ? -15.129 40.419 36.882 1.00 10.47 ? 303 ASN A O 1 ATOM 2340 C CB . ASN A 1 303 ? -16.537 42.990 36.859 1.00 11.80 ? 303 ASN A CB 1 ATOM 2341 C CG . ASN A 1 303 ? -16.837 43.202 38.365 1.00 12.72 ? 303 ASN A CG 1 ATOM 2342 O OD1 . ASN A 1 303 ? -16.018 42.899 39.235 1.00 10.90 ? 303 ASN A OD1 1 ATOM 2343 N ND2 . ASN A 1 303 ? -18.031 43.695 38.662 1.00 10.40 ? 303 ASN A ND2 1 ATOM 2344 N N . PRO A 1 304 ? -13.388 41.491 37.869 1.00 12.60 ? 304 PRO A N 1 ATOM 2345 C CA . PRO A 1 304 ? -12.817 40.265 38.443 1.00 12.45 ? 304 PRO A CA 1 ATOM 2346 C C . PRO A 1 304 ? -13.630 39.575 39.531 1.00 13.16 ? 304 PRO A C 1 ATOM 2347 O O . PRO A 1 304 ? -13.496 38.363 39.736 1.00 13.40 ? 304 PRO A O 1 ATOM 2348 C CB . PRO A 1 304 ? -11.453 40.737 38.959 1.00 13.56 ? 304 PRO A CB 1 ATOM 2349 C CG . PRO A 1 304 ? -11.726 42.149 39.384 1.00 14.51 ? 304 PRO A CG 1 ATOM 2350 C CD . PRO A 1 304 ? -12.578 42.670 38.250 1.00 13.78 ? 304 PRO A CD 1 ATOM 2351 N N . HIS A 1 305 ? -14.464 40.345 40.235 1.00 12.25 ? 305 HIS A N 1 ATOM 2352 C CA . HIS A 1 305 ? -15.276 39.804 41.326 1.00 13.64 ? 305 HIS A CA 1 ATOM 2353 C C . HIS A 1 305 ? -16.730 40.299 41.331 1.00 12.40 ? 305 HIS A C 1 ATOM 2354 O O . HIS A 1 305 ? -17.126 41.043 42.229 1.00 12.40 ? 305 HIS A O 1 ATOM 2355 C CB . HIS A 1 305 ? -14.614 40.101 42.690 1.00 13.77 ? 305 HIS A CB 1 ATOM 2356 C CG . HIS A 1 305 ? -13.202 39.619 42.800 1.00 15.87 ? 305 HIS A CG 1 ATOM 2357 N ND1 . HIS A 1 305 ? -12.862 38.288 42.699 1.00 16.36 ? 305 HIS A ND1 1 ATOM 2358 C CD2 . HIS A 1 305 ? -12.038 40.295 42.937 1.00 16.27 ? 305 HIS A CD2 1 ATOM 2359 C CE1 . HIS A 1 305 ? -11.548 38.164 42.767 1.00 16.37 ? 305 HIS A CE1 1 ATOM 2360 N NE2 . HIS A 1 305 ? -11.025 39.368 42.910 1.00 16.91 ? 305 HIS A NE2 1 ATOM 2361 N N . PRO A 1 306 ? -17.553 39.887 40.332 1.00 12.97 ? 306 PRO A N 1 ATOM 2362 C CA . PRO A 1 306 ? -18.960 40.319 40.285 1.00 13.65 ? 306 PRO A CA 1 ATOM 2363 C C . PRO A 1 306 ? -19.672 39.710 41.488 1.00 12.86 ? 306 PRO A C 1 ATOM 2364 O O . PRO A 1 306 ? -19.510 38.515 41.763 1.00 13.00 ? 306 PRO A O 1 ATOM 2365 C CB . PRO A 1 306 ? -19.467 39.694 38.992 1.00 13.33 ? 306 PRO A CB 1 ATOM 2366 C CG . PRO A 1 306 ? -18.217 39.447 38.184 1.00 16.11 ? 306 PRO A CG 1 ATOM 2367 C CD . PRO A 1 306 ? -17.271 38.968 39.216 1.00 12.81 ? 306 PRO A CD 1 ATOM 2368 N N . ALA A 1 307 ? -20.382 40.543 42.242 1.00 12.24 ? 307 ALA A N 1 ATOM 2369 C CA . ALA A 1 307 ? -21.050 40.073 43.447 1.00 13.78 ? 307 ALA A CA 1 ATOM 2370 C C . ALA A 1 307 ? -22.278 40.852 43.873 1.00 13.84 ? 307 ALA A C 1 ATOM 2371 O O . ALA A 1 307 ? -22.560 41.935 43.362 1.00 17.40 ? 307 ALA A O 1 ATOM 2372 C CB . ALA A 1 307 ? -20.049 40.014 44.608 1.00 13.01 ? 307 ALA A CB 1 ATOM 2373 N N . ALA A 1 308 ? -23.039 40.229 44.767 1.00 14.21 ? 308 ALA A N 1 ATOM 2374 C CA . ALA A 1 308 ? -24.242 40.800 45.354 1.00 14.20 ? 308 ALA A CA 1 ATOM 2375 C C . ALA A 1 308 ? -24.081 40.638 46.864 1.00 14.62 ? 308 ALA A C 1 ATOM 2376 O O . ALA A 1 308 ? -23.250 39.845 47.316 1.00 13.61 ? 308 ALA A O 1 ATOM 2377 C CB . ALA A 1 308 ? -25.480 40.052 44.878 1.00 11.24 ? 308 ALA A CB 1 ATOM 2378 N N . ILE A 1 309 ? -24.861 41.401 47.630 1.00 15.78 ? 309 ILE A N 1 ATOM 2379 C CA . ILE A 1 309 ? -24.827 41.355 49.096 1.00 15.76 ? 309 ILE A CA 1 ATOM 2380 C C . ILE A 1 309 ? -26.096 40.694 49.633 1.00 16.04 ? 309 ILE A C 1 ATOM 2381 O O . ILE A 1 309 ? -27.205 41.035 49.217 1.00 18.24 ? 309 ILE A O 1 ATOM 2382 C CB . ILE A 1 309 ? -24.733 42.796 49.728 1.00 16.80 ? 309 ILE A CB 1 ATOM 2383 C CG1 . ILE A 1 309 ? -23.498 43.538 49.210 1.00 16.51 ? 309 ILE A CG1 1 ATOM 2384 C CG2 . ILE A 1 309 ? -24.689 42.724 51.276 1.00 16.04 ? 309 ILE A CG2 1 ATOM 2385 C CD1 . ILE A 1 309 ? -23.445 45.025 49.574 1.00 16.04 ? 309 ILE A CD1 1 ATOM 2386 N N . PHE A 1 310 ? -25.916 39.704 50.503 1.00 15.56 ? 310 PHE A N 1 ATOM 2387 C CA . PHE A 1 310 ? -27.035 39.040 51.159 1.00 15.86 ? 310 PHE A CA 1 ATOM 2388 C C . PHE A 1 310 ? -26.978 39.490 52.610 1.00 16.42 ? 310 PHE A C 1 ATOM 2389 O O . PHE A 1 310 ? -26.118 39.065 53.390 1.00 15.10 ? 310 PHE A O 1 ATOM 2390 C CB . PHE A 1 310 ? -26.975 37.518 51.014 1.00 15.48 ? 310 PHE A CB 1 ATOM 2391 C CG . PHE A 1 310 ? -27.686 37.001 49.788 1.00 14.61 ? 310 PHE A CG 1 ATOM 2392 C CD1 . PHE A 1 310 ? -27.282 37.397 48.499 1.00 14.68 ? 310 PHE A CD1 1 ATOM 2393 C CD2 . PHE A 1 310 ? -28.775 36.128 49.915 1.00 16.33 ? 310 PHE A CD2 1 ATOM 2394 C CE1 . PHE A 1 310 ? -27.958 36.928 47.344 1.00 13.57 ? 310 PHE A CE1 1 ATOM 2395 C CE2 . PHE A 1 310 ? -29.466 35.643 48.770 1.00 16.94 ? 310 PHE A CE2 1 ATOM 2396 C CZ . PHE A 1 310 ? -29.049 36.050 47.480 1.00 15.49 ? 310 PHE A CZ 1 ATOM 2397 N N . HIS A 1 311 ? -27.858 40.438 52.908 1.00 16.42 ? 311 HIS A N 1 ATOM 2398 C CA . HIS A 1 311 ? -27.986 41.068 54.213 1.00 19.16 ? 311 HIS A CA 1 ATOM 2399 C C . HIS A 1 311 ? -29.032 40.402 55.100 1.00 18.98 ? 311 HIS A C 1 ATOM 2400 O O . HIS A 1 311 ? -30.167 40.209 54.687 1.00 19.20 ? 311 HIS A O 1 ATOM 2401 C CB . HIS A 1 311 ? -28.335 42.554 53.986 1.00 21.34 ? 311 HIS A CB 1 ATOM 2402 C CG . HIS A 1 311 ? -28.687 43.312 55.230 1.00 22.17 ? 311 HIS A CG 1 ATOM 2403 N ND1 . HIS A 1 311 ? -27.744 43.702 56.154 1.00 23.51 ? 311 HIS A ND1 1 ATOM 2404 C CD2 . HIS A 1 311 ? -29.878 43.759 55.694 1.00 21.97 ? 311 HIS A CD2 1 ATOM 2405 C CE1 . HIS A 1 311 ? -28.339 44.357 57.134 1.00 24.47 ? 311 HIS A CE1 1 ATOM 2406 N NE2 . HIS A 1 311 ? -29.633 44.405 56.880 1.00 23.79 ? 311 HIS A NE2 1 ATOM 2407 N N . TYR A 1 312 ? -28.647 40.084 56.333 1.00 19.73 ? 312 TYR A N 1 ATOM 2408 C CA . TYR A 1 312 ? -29.582 39.512 57.300 1.00 20.56 ? 312 TYR A CA 1 ATOM 2409 C C . TYR A 1 312 ? -30.280 40.707 57.944 1.00 20.61 ? 312 TYR A C 1 ATOM 2410 O O . TYR A 1 312 ? -29.615 41.677 58.298 1.00 20.55 ? 312 TYR A O 1 ATOM 2411 C CB . TYR A 1 312 ? -28.842 38.730 58.378 1.00 19.14 ? 312 TYR A CB 1 ATOM 2412 C CG . TYR A 1 312 ? -28.619 37.265 58.084 1.00 18.82 ? 312 TYR A CG 1 ATOM 2413 C CD1 . TYR A 1 312 ? -27.835 36.846 56.986 1.00 16.99 ? 312 TYR A CD1 1 ATOM 2414 C CD2 . TYR A 1 312 ? -29.149 36.279 58.942 1.00 17.22 ? 312 TYR A CD2 1 ATOM 2415 C CE1 . TYR A 1 312 ? -27.580 35.467 56.754 1.00 17.18 ? 312 TYR A CE1 1 ATOM 2416 C CE2 . TYR A 1 312 ? -28.897 34.906 58.725 1.00 15.76 ? 312 TYR A CE2 1 ATOM 2417 C CZ . TYR A 1 312 ? -28.113 34.508 57.632 1.00 16.45 ? 312 TYR A CZ 1 ATOM 2418 O OH . TYR A 1 312 ? -27.860 33.172 57.430 1.00 13.52 ? 312 TYR A OH 1 ATOM 2419 N N . ALA A 1 313 ? -31.609 40.656 58.049 1.00 21.71 ? 313 ALA A N 1 ATOM 2420 C CA . ALA A 1 313 ? -32.397 41.738 58.654 1.00 23.85 ? 313 ALA A CA 1 ATOM 2421 C C . ALA A 1 313 ? -32.038 41.924 60.131 1.00 24.70 ? 313 ALA A C 1 ATOM 2422 O O . ALA A 1 313 ? -31.951 40.946 60.880 1.00 24.93 ? 313 ALA A O 1 ATOM 2423 C CB . ALA A 1 313 ? -33.888 41.457 58.503 1.00 23.35 ? 313 ALA A CB 1 ATOM 2424 N N . GLY A 1 314 ? -31.761 43.171 60.514 1.00 25.76 ? 314 GLY A N 1 ATOM 2425 C CA . GLY A 1 314 ? -31.395 43.478 61.892 1.00 26.82 ? 314 GLY A CA 1 ATOM 2426 C C . GLY A 1 314 ? -29.893 43.561 62.105 1.00 27.33 ? 314 GLY A C 1 ATOM 2427 O O . GLY A 1 314 ? -29.428 44.071 63.128 1.00 29.16 ? 314 GLY A O 1 ATOM 2428 N N . ALA A 1 315 ? -29.137 43.037 61.140 1.00 26.91 ? 315 ALA A N 1 ATOM 2429 C CA . ALA A 1 315 ? -27.674 43.044 61.164 1.00 26.43 ? 315 ALA A CA 1 ATOM 2430 C C . ALA A 1 315 ? -27.190 44.415 60.671 1.00 25.66 ? 315 ALA A C 1 ATOM 2431 O O . ALA A 1 315 ? -27.984 45.171 60.101 1.00 25.59 ? 315 ALA A O 1 ATOM 2432 C CB . ALA A 1 315 ? -27.146 41.937 60.260 1.00 27.06 ? 315 ALA A CB 1 ATOM 2433 N N . PRO A 1 316 ? -25.913 44.790 60.938 1.00 26.52 ? 316 PRO A N 1 ATOM 2434 C CA . PRO A 1 316 ? -25.468 46.104 60.451 1.00 26.41 ? 316 PRO A CA 1 ATOM 2435 C C . PRO A 1 316 ? -25.326 46.196 58.930 1.00 27.05 ? 316 PRO A C 1 ATOM 2436 O O . PRO A 1 316 ? -25.303 45.173 58.232 1.00 26.53 ? 316 PRO A O 1 ATOM 2437 C CB . PRO A 1 316 ? -24.126 46.302 61.162 1.00 26.48 ? 316 PRO A CB 1 ATOM 2438 C CG . PRO A 1 316 ? -23.660 44.917 61.448 1.00 27.71 ? 316 PRO A CG 1 ATOM 2439 C CD . PRO A 1 316 ? -24.917 44.231 61.876 1.00 26.83 ? 316 PRO A CD 1 ATOM 2440 N N . GLY A 1 317 ? -25.270 47.429 58.431 1.00 26.54 ? 317 GLY A N 1 ATOM 2441 C CA . GLY A 1 317 ? -25.125 47.668 57.005 1.00 26.79 ? 317 GLY A CA 1 ATOM 2442 C C . GLY A 1 317 ? -23.688 47.547 56.539 1.00 26.52 ? 317 GLY A C 1 ATOM 2443 O O . GLY A 1 317 ? -22.852 46.933 57.211 1.00 27.26 ? 317 GLY A O 1 ATOM 2444 N N . GLY A 1 318 ? -23.405 48.131 55.380 1.00 26.10 ? 318 GLY A N 1 ATOM 2445 C CA . GLY A 1 318 ? -22.064 48.088 54.829 1.00 26.14 ? 318 GLY A CA 1 ATOM 2446 C C . GLY A 1 318 ? -21.771 46.854 53.997 1.00 26.58 ? 318 GLY A C 1 ATOM 2447 O O . GLY A 1 318 ? -22.628 45.984 53.806 1.00 26.13 ? 318 GLY A O 1 ATOM 2448 N N . LEU A 1 319 ? -20.528 46.777 53.534 1.00 26.61 ? 319 LEU A N 1 ATOM 2449 C CA . LEU A 1 319 ? -20.049 45.685 52.700 1.00 26.51 ? 319 LEU A CA 1 ATOM 2450 C C . LEU A 1 319 ? -19.582 44.476 53.516 1.00 26.04 ? 319 LEU A C 1 ATOM 2451 O O . LEU A 1 319 ? -19.097 44.639 54.639 1.00 26.86 ? 319 LEU A O 1 ATOM 2452 C CB . LEU A 1 319 ? -18.890 46.183 51.819 1.00 27.49 ? 319 LEU A CB 1 ATOM 2453 C CG . LEU A 1 319 ? -19.069 47.427 50.942 1.00 27.77 ? 319 LEU A CG 1 ATOM 2454 C CD1 . LEU A 1 319 ? -17.835 47.584 50.069 1.00 27.55 ? 319 LEU A CD1 1 ATOM 2455 C CD2 . LEU A 1 319 ? -20.320 47.325 50.078 1.00 27.73 ? 319 LEU A CD2 1 ATOM 2456 N N . PRO A 1 320 ? -19.786 43.241 52.993 1.00 24.91 ? 320 PRO A N 1 ATOM 2457 C CA . PRO A 1 320 ? -19.366 42.008 53.677 1.00 24.04 ? 320 PRO A CA 1 ATOM 2458 C C . PRO A 1 320 ? -17.846 41.992 53.846 1.00 23.63 ? 320 PRO A C 1 ATOM 2459 O O . PRO A 1 320 ? -17.121 42.486 52.976 1.00 23.33 ? 320 PRO A O 1 ATOM 2460 C CB . PRO A 1 320 ? -19.799 40.920 52.706 1.00 23.06 ? 320 PRO A CB 1 ATOM 2461 C CG . PRO A 1 320 ? -20.993 41.494 52.056 1.00 22.16 ? 320 PRO A CG 1 ATOM 2462 C CD . PRO A 1 320 ? -20.641 42.920 51.832 1.00 22.56 ? 320 PRO A CD 1 ATOM 2463 N N . THR A 1 321 ? -17.381 41.446 54.967 1.00 23.64 ? 321 THR A N 1 ATOM 2464 C CA . THR A 1 321 ? -15.951 41.391 55.279 1.00 24.06 ? 321 THR A CA 1 ATOM 2465 C C . THR A 1 321 ? -15.248 40.080 54.930 1.00 24.77 ? 321 THR A C 1 ATOM 2466 O O . THR A 1 321 ? -14.017 40.035 54.860 1.00 25.84 ? 321 THR A O 1 ATOM 2467 C CB . THR A 1 321 ? -15.695 41.718 56.772 1.00 24.82 ? 321 THR A CB 1 ATOM 2468 O OG1 . THR A 1 321 ? -16.446 40.820 57.601 1.00 24.45 ? 321 THR A OG1 1 ATOM 2469 C CG2 . THR A 1 321 ? -16.097 43.156 57.086 1.00 25.53 ? 321 THR A CG2 1 ATOM 2470 N N . ASP A 1 322 ? -16.026 39.017 54.729 1.00 23.01 ? 322 ASP A N 1 ATOM 2471 C CA . ASP A 1 322 ? -15.473 37.705 54.397 1.00 23.12 ? 322 ASP A CA 1 ATOM 2472 C C . ASP A 1 322 ? -15.520 37.455 52.886 1.00 23.33 ? 322 ASP A C 1 ATOM 2473 O O . ASP A 1 322 ? -16.593 37.236 52.317 1.00 22.64 ? 322 ASP A O 1 ATOM 2474 C CB . ASP A 1 322 ? -16.236 36.606 55.158 1.00 22.39 ? 322 ASP A CB 1 ATOM 2475 C CG . ASP A 1 322 ? -15.555 35.231 55.094 1.00 22.59 ? 322 ASP A CG 1 ATOM 2476 O OD1 . ASP A 1 322 ? -14.536 35.057 54.384 1.00 22.22 ? 322 ASP A OD1 1 ATOM 2477 O OD2 . ASP A 1 322 ? -16.059 34.310 55.767 1.00 21.59 ? 322 ASP A OD2 1 ATOM 2478 N N . GLU A 1 323 ? -14.340 37.427 52.265 1.00 22.70 ? 323 GLU A N 1 ATOM 2479 C CA . GLU A 1 323 ? -14.203 37.192 50.824 1.00 23.86 ? 323 GLU A CA 1 ATOM 2480 C C . GLU A 1 323 ? -14.542 35.754 50.441 1.00 23.36 ? 323 GLU A C 1 ATOM 2481 O O . GLU A 1 323 ? -14.906 35.474 49.299 1.00 23.97 ? 323 GLU A O 1 ATOM 2482 C CB . GLU A 1 323 ? -12.793 37.560 50.351 1.00 23.02 ? 323 GLU A CB 1 ATOM 2483 C CG . GLU A 1 323 ? -12.493 39.060 50.439 1.00 26.07 ? 323 GLU A CG 1 ATOM 2484 C CD . GLU A 1 323 ? -11.094 39.451 49.962 1.00 27.34 ? 323 GLU A CD 1 ATOM 2485 O OE1 . GLU A 1 323 ? -10.300 38.572 49.558 1.00 27.86 ? 323 GLU A OE1 1 ATOM 2486 O OE2 . GLU A 1 323 ? -10.791 40.663 49.982 1.00 29.05 ? 323 GLU A OE2 1 ATOM 2487 N N . GLY A 1 324 ? -14.443 34.857 51.422 1.00 23.86 ? 324 GLY A N 1 ATOM 2488 C CA . GLY A 1 324 ? -14.749 33.452 51.219 1.00 23.71 ? 324 GLY A CA 1 ATOM 2489 C C . GLY A 1 324 ? -13.691 32.680 50.459 1.00 24.53 ? 324 GLY A C 1 ATOM 2490 O O . GLY A 1 324 ? -12.633 33.211 50.117 1.00 24.68 ? 324 GLY A O 1 ATOM 2491 N N . THR A 1 325 ? -13.985 31.408 50.218 1.00 25.70 ? 325 THR A N 1 ATOM 2492 C CA . THR A 1 325 ? -13.092 30.516 49.495 1.00 27.40 ? 325 THR A CA 1 ATOM 2493 C C . THR A 1 325 ? -13.646 30.335 48.078 1.00 27.24 ? 325 THR A C 1 ATOM 2494 O O . THR A 1 325 ? -14.873 30.318 47.895 1.00 26.03 ? 325 THR A O 1 ATOM 2495 C CB . THR A 1 325 ? -12.984 29.130 50.212 1.00 29.57 ? 325 THR A CB 1 ATOM 2496 O OG1 . THR A 1 325 ? -14.288 28.557 50.372 1.00 31.97 ? 325 THR A OG1 1 ATOM 2497 C CG2 . THR A 1 325 ? -12.321 29.277 51.580 1.00 31.30 ? 325 THR A CG2 1 ATOM 2498 N N . PRO A 1 326 ? -12.765 30.270 47.048 1.00 27.55 ? 326 PRO A N 1 ATOM 2499 C CA . PRO A 1 326 ? -13.265 30.087 45.679 1.00 26.68 ? 326 PRO A CA 1 ATOM 2500 C C . PRO A 1 326 ? -13.981 28.734 45.528 1.00 25.84 ? 326 PRO A C 1 ATOM 2501 O O . PRO A 1 326 ? -13.538 27.726 46.099 1.00 25.83 ? 326 PRO A O 1 ATOM 2502 C CB . PRO A 1 326 ? -11.988 30.168 44.830 1.00 28.53 ? 326 PRO A CB 1 ATOM 2503 C CG . PRO A 1 326 ? -10.905 29.750 45.769 1.00 29.54 ? 326 PRO A CG 1 ATOM 2504 C CD . PRO A 1 326 ? -11.301 30.472 47.025 1.00 29.61 ? 326 PRO A CD 1 ATOM 2505 N N . PRO A 1 327 ? -15.140 28.711 44.831 1.00 23.52 ? 327 PRO A N 1 ATOM 2506 C CA . PRO A 1 327 ? -15.873 27.453 44.651 1.00 21.91 ? 327 PRO A CA 1 ATOM 2507 C C . PRO A 1 327 ? -15.146 26.492 43.716 1.00 20.29 ? 327 PRO A C 1 ATOM 2508 O O . PRO A 1 327 ? -14.155 26.871 43.083 1.00 19.55 ? 327 PRO A O 1 ATOM 2509 C CB . PRO A 1 327 ? -17.200 27.923 44.060 1.00 22.42 ? 327 PRO A CB 1 ATOM 2510 C CG . PRO A 1 327 ? -16.815 29.124 43.267 1.00 22.76 ? 327 PRO A CG 1 ATOM 2511 C CD . PRO A 1 327 ? -15.872 29.831 44.203 1.00 23.30 ? 327 PRO A CD 1 ATOM 2512 N N . VAL A 1 328 ? -15.624 25.251 43.651 1.00 19.78 ? 328 VAL A N 1 ATOM 2513 C CA . VAL A 1 328 ? -15.027 24.248 42.774 1.00 20.07 ? 328 VAL A CA 1 ATOM 2514 C C . VAL A 1 328 ? -15.224 24.661 41.312 1.00 18.54 ? 328 VAL A C 1 ATOM 2515 O O . VAL A 1 328 ? -16.190 25.360 40.978 1.00 18.48 ? 328 VAL A O 1 ATOM 2516 C CB . VAL A 1 328 ? -15.609 22.814 43.018 1.00 22.01 ? 328 VAL A CB 1 ATOM 2517 C CG1 . VAL A 1 328 ? -15.310 22.366 44.443 1.00 25.62 ? 328 VAL A CG1 1 ATOM 2518 C CG2 . VAL A 1 328 ? -17.124 22.758 42.745 1.00 25.06 ? 328 VAL A CG2 1 ATOM 2519 N N . ASP A 1 329 ? -14.244 24.324 40.483 1.00 16.13 ? 329 ASP A N 1 ATOM 2520 C CA . ASP A 1 329 ? -14.290 24.627 39.062 1.00 15.68 ? 329 ASP A CA 1 ATOM 2521 C C . ASP A 1 329 ? -15.286 23.642 38.433 1.00 14.47 ? 329 ASP A C 1 ATOM 2522 O O . ASP A 1 329 ? -15.050 22.434 38.415 1.00 12.27 ? 329 ASP A O 1 ATOM 2523 C CB . ASP A 1 329 ? -12.888 24.461 38.456 1.00 16.37 ? 329 ASP A CB 1 ATOM 2524 C CG . ASP A 1 329 ? -12.753 25.101 37.085 1.00 15.27 ? 329 ASP A CG 1 ATOM 2525 O OD1 . ASP A 1 329 ? -13.707 25.044 36.279 1.00 14.63 ? 329 ASP A OD1 1 ATOM 2526 O OD2 . ASP A 1 329 ? -11.675 25.651 36.798 1.00 17.21 ? 329 ASP A OD2 1 ATOM 2527 N N . HIS A 1 330 ? -16.408 24.173 37.947 1.00 13.02 ? 330 HIS A N 1 ATOM 2528 C CA . HIS A 1 330 ? -17.457 23.352 37.329 1.00 12.07 ? 330 HIS A CA 1 ATOM 2529 C C . HIS A 1 330 ? -17.155 22.918 35.898 1.00 12.28 ? 330 HIS A C 1 ATOM 2530 O O . HIS A 1 330 ? -17.913 22.149 35.297 1.00 12.42 ? 330 HIS A O 1 ATOM 2531 C CB . HIS A 1 330 ? -18.799 24.076 37.399 1.00 11.61 ? 330 HIS A CB 1 ATOM 2532 C CG . HIS A 1 330 ? -19.358 24.168 38.784 1.00 11.95 ? 330 HIS A CG 1 ATOM 2533 N ND1 . HIS A 1 330 ? -20.359 23.339 39.236 1.00 12.34 ? 330 HIS A ND1 1 ATOM 2534 C CD2 . HIS A 1 330 ? -19.050 24.985 39.819 1.00 11.33 ? 330 HIS A CD2 1 ATOM 2535 C CE1 . HIS A 1 330 ? -20.645 23.640 40.490 1.00 11.84 ? 330 HIS A CE1 1 ATOM 2536 N NE2 . HIS A 1 330 ? -19.864 24.635 40.867 1.00 12.75 ? 330 HIS A NE2 1 ATOM 2537 N N . GLN A 1 331 ? -16.027 23.409 35.379 1.00 11.68 ? 331 GLN A N 1 ATOM 2538 C CA . GLN A 1 331 ? -15.520 23.110 34.038 1.00 12.60 ? 331 GLN A CA 1 ATOM 2539 C C . GLN A 1 331 ? -16.507 23.269 32.875 1.00 11.62 ? 331 GLN A C 1 ATOM 2540 O O . GLN A 1 331 ? -16.555 22.444 31.965 1.00 10.64 ? 331 GLN A O 1 ATOM 2541 C CB . GLN A 1 331 ? -14.826 21.735 34.013 1.00 12.48 ? 331 GLN A CB 1 ATOM 2542 C CG . GLN A 1 331 ? -13.622 21.595 34.976 1.00 13.77 ? 331 GLN A CG 1 ATOM 2543 C CD . GLN A 1 331 ? -12.384 22.402 34.570 1.00 14.23 ? 331 GLN A CD 1 ATOM 2544 O OE1 . GLN A 1 331 ? -12.301 22.949 33.465 1.00 14.71 ? 331 GLN A OE1 1 ATOM 2545 N NE2 . GLN A 1 331 ? -11.400 22.444 35.459 1.00 13.15 ? 331 GLN A NE2 1 ATOM 2546 N N . CYS A 1 332 ? -17.273 24.364 32.911 1.00 10.99 ? 332 CYS A N 1 ATOM 2547 C CA . CYS A 1 332 ? -18.286 24.688 31.898 1.00 10.82 ? 332 CYS A CA 1 ATOM 2548 C C . CYS A 1 332 ? -19.326 23.585 31.684 1.00 9.17 ? 332 CYS A C 1 ATOM 2549 O O . CYS A 1 332 ? -19.766 23.329 30.563 1.00 7.83 ? 332 CYS A O 1 ATOM 2550 C CB . CYS A 1 332 ? -17.637 25.070 30.568 1.00 9.44 ? 332 CYS A CB 1 ATOM 2551 S SG . CYS A 1 332 ? -16.646 26.578 30.630 1.00 10.91 ? 332 CYS A SG 1 ATOM 2552 N N . LEU A 1 333 ? -19.651 22.886 32.768 1.00 9.73 ? 333 LEU A N 1 ATOM 2553 C CA . LEU A 1 333 ? -20.608 21.785 32.730 1.00 10.28 ? 333 LEU A CA 1 ATOM 2554 C C . LEU A 1 333 ? -21.647 21.926 33.815 1.00 10.51 ? 333 LEU A C 1 ATOM 2555 O O . LEU A 1 333 ? -21.319 22.262 34.957 1.00 11.00 ? 333 LEU A O 1 ATOM 2556 C CB . LEU A 1 333 ? -19.895 20.442 32.931 1.00 11.94 ? 333 LEU A CB 1 ATOM 2557 C CG . LEU A 1 333 ? -18.836 19.987 31.928 1.00 14.26 ? 333 LEU A CG 1 ATOM 2558 C CD1 . LEU A 1 333 ? -17.973 18.923 32.552 1.00 13.35 ? 333 LEU A CD1 1 ATOM 2559 C CD2 . LEU A 1 333 ? -19.467 19.543 30.622 1.00 13.43 ? 333 LEU A CD2 1 ATOM 2560 N N . ASP A 1 334 ? -22.909 21.723 33.443 1.00 9.73 ? 334 ASP A N 1 ATOM 2561 C CA . ASP A 1 334 ? -24.002 21.763 34.406 1.00 9.69 ? 334 ASP A CA 1 ATOM 2562 C C . ASP A 1 334 ? -24.067 20.397 35.076 1.00 10.24 ? 334 ASP A C 1 ATOM 2563 O O . ASP A 1 334 ? -23.513 19.424 34.558 1.00 10.17 ? 334 ASP A O 1 ATOM 2564 C CB . ASP A 1 334 ? -25.342 22.177 33.757 1.00 10.54 ? 334 ASP A CB 1 ATOM 2565 C CG . ASP A 1 334 ? -25.733 21.326 32.545 1.00 9.41 ? 334 ASP A CG 1 ATOM 2566 O OD1 . ASP A 1 334 ? -24.861 20.978 31.723 1.00 9.66 ? 334 ASP A OD1 1 ATOM 2567 O OD2 . ASP A 1 334 ? -26.941 21.039 32.403 1.00 6.99 ? 334 ASP A OD2 1 ATOM 2568 N N . THR A 1 335 ? -24.677 20.339 36.253 1.00 10.92 ? 335 THR A N 1 ATOM 2569 C CA . THR A 1 335 ? -24.775 19.085 36.989 1.00 11.19 ? 335 THR A CA 1 ATOM 2570 C C . THR A 1 335 ? -25.823 18.128 36.429 1.00 11.73 ? 335 THR A C 1 ATOM 2571 O O . THR A 1 335 ? -26.914 18.548 36.037 1.00 12.06 ? 335 THR A O 1 ATOM 2572 C CB . THR A 1 335 ? -25.016 19.334 38.506 1.00 12.02 ? 335 THR A CB 1 ATOM 2573 O OG1 . THR A 1 335 ? -25.137 18.077 39.186 1.00 11.89 ? 335 THR A OG1 1 ATOM 2574 C CG2 . THR A 1 335 ? -26.275 20.184 38.749 1.00 10.19 ? 335 THR A CG2 1 ATOM 2575 N N . LEU A 1 336 ? -25.449 16.853 36.338 1.00 10.20 ? 336 LEU A N 1 ATOM 2576 C CA . LEU A 1 336 ? -26.357 15.816 35.867 1.00 12.28 ? 336 LEU A CA 1 ATOM 2577 C C . LEU A 1 336 ? -26.908 15.008 37.042 1.00 12.23 ? 336 LEU A C 1 ATOM 2578 O O . LEU A 1 336 ? -27.494 13.937 36.851 1.00 12.04 ? 336 LEU A O 1 ATOM 2579 C CB . LEU A 1 336 ? -25.681 14.883 34.850 1.00 12.83 ? 336 LEU A CB 1 ATOM 2580 C CG . LEU A 1 336 ? -25.126 15.470 33.548 1.00 14.69 ? 336 LEU A CG 1 ATOM 2581 C CD1 . LEU A 1 336 ? -24.711 14.337 32.624 1.00 16.05 ? 336 LEU A CD1 1 ATOM 2582 C CD2 . LEU A 1 336 ? -26.133 16.382 32.858 1.00 14.31 ? 336 LEU A CD2 1 ATOM 2583 N N . ASP A 1 337 ? -26.753 15.558 38.247 1.00 12.32 ? 337 ASP A N 1 ATOM 2584 C CA . ASP A 1 337 ? -27.211 14.921 39.478 1.00 13.78 ? 337 ASP A CA 1 ATOM 2585 C C . ASP A 1 337 ? -28.666 15.243 39.827 1.00 14.26 ? 337 ASP A C 1 ATOM 2586 O O . ASP A 1 337 ? -29.242 14.592 40.703 1.00 14.97 ? 337 ASP A O 1 ATOM 2587 C CB . ASP A 1 337 ? -26.301 15.299 40.661 1.00 15.12 ? 337 ASP A CB 1 ATOM 2588 C CG . ASP A 1 337 ? -24.887 14.723 40.542 1.00 17.65 ? 337 ASP A CG 1 ATOM 2589 O OD1 . ASP A 1 337 ? -24.679 13.737 39.801 1.00 18.61 ? 337 ASP A OD1 1 ATOM 2590 O OD2 . ASP A 1 337 ? -23.976 15.262 41.209 1.00 20.13 ? 337 ASP A OD2 1 ATOM 2591 N N . VAL A 1 338 ? -29.256 16.240 39.156 1.00 13.12 ? 338 VAL A N 1 ATOM 2592 C CA . VAL A 1 338 ? -30.656 16.619 39.412 1.00 13.78 ? 338 VAL A CA 1 ATOM 2593 C C . VAL A 1 338 ? -31.633 15.537 38.943 1.00 12.89 ? 338 VAL A C 1 ATOM 2594 O O . VAL A 1 338 ? -31.441 14.926 37.891 1.00 12.19 ? 338 VAL A O 1 ATOM 2595 C CB . VAL A 1 338 ? -31.040 18.013 38.807 1.00 14.16 ? 338 VAL A CB 1 ATOM 2596 C CG1 . VAL A 1 338 ? -30.274 19.121 39.508 1.00 12.08 ? 338 VAL A CG1 1 ATOM 2597 C CG2 . VAL A 1 338 ? -30.802 18.067 37.305 1.00 13.26 ? 338 VAL A CG2 1 ATOM 2598 N N . ARG A 1 339 ? -32.616 15.241 39.788 1.00 14.37 ? 339 ARG A N 1 ATOM 2599 C CA . ARG A 1 339 ? -33.610 14.211 39.502 1.00 13.93 ? 339 ARG A CA 1 ATOM 2600 C C . ARG A 1 339 ? -35.018 14.787 39.620 1.00 14.08 ? 339 ARG A C 1 ATOM 2601 O O . ARG A 1 339 ? -35.457 15.109 40.724 1.00 13.75 ? 339 ARG A O 1 ATOM 2602 C CB . ARG A 1 339 ? -33.467 13.032 40.486 1.00 14.08 ? 339 ARG A CB 1 ATOM 2603 C CG . ARG A 1 339 ? -32.141 12.258 40.439 1.00 15.28 ? 339 ARG A CG 1 ATOM 2604 C CD . ARG A 1 339 ? -32.033 11.393 39.191 1.00 17.83 ? 339 ARG A CD 1 ATOM 2605 N NE . ARG A 1 339 ? -30.740 10.718 39.074 1.00 19.01 ? 339 ARG A NE 1 ATOM 2606 C CZ . ARG A 1 339 ? -29.672 11.217 38.454 1.00 20.52 ? 339 ARG A CZ 1 ATOM 2607 N NH1 . ARG A 1 339 ? -29.723 12.414 37.876 1.00 17.97 ? 339 ARG A NH1 1 ATOM 2608 N NH2 . ARG A 1 339 ? -28.542 10.519 38.422 1.00 20.55 ? 339 ARG A NH2 1 ATOM 2609 N N . PRO A 1 340 ? -35.736 14.953 38.483 1.00 13.50 ? 340 PRO A N 1 ATOM 2610 C CA . PRO A 1 340 ? -37.103 15.495 38.512 1.00 14.09 ? 340 PRO A CA 1 ATOM 2611 C C . PRO A 1 340 ? -38.092 14.740 39.398 1.00 14.43 ? 340 PRO A C 1 ATOM 2612 O O . PRO A 1 340 ? -37.986 13.517 39.543 1.00 12.77 ? 340 PRO A O 1 ATOM 2613 C CB . PRO A 1 340 ? -37.521 15.506 37.040 1.00 14.68 ? 340 PRO A CB 1 ATOM 2614 C CG . PRO A 1 340 ? -36.453 14.759 36.313 1.00 15.60 ? 340 PRO A CG 1 ATOM 2615 C CD . PRO A 1 340 ? -35.220 14.938 37.104 1.00 13.58 ? 340 PRO A CD 1 ATOM 2616 N N . VAL A 1 341 ? -38.987 15.494 40.049 1.00 14.00 ? 341 VAL A N 1 ATOM 2617 C CA . VAL A 1 341 ? -40.018 14.939 40.941 1.00 15.06 ? 341 VAL A CA 1 ATOM 2618 C C . VAL A 1 341 ? -40.934 14.000 40.159 1.00 15.35 ? 341 VAL A C 1 ATOM 2619 O O . VAL A 1 341 ? -41.157 12.868 40.580 1.00 16.31 ? 341 VAL A O 1 ATOM 2620 C CB . VAL A 1 341 ? -40.859 16.054 41.625 1.00 15.55 ? 341 VAL A CB 1 ATOM 2621 C CG1 . VAL A 1 341 ? -41.920 15.451 42.566 1.00 15.57 ? 341 VAL A CG1 1 ATOM 2622 C CG2 . VAL A 1 341 ? -39.960 16.958 42.418 1.00 15.69 ? 341 VAL A CG2 1 ATOM 2623 N N . VAL A 1 342 ? -41.459 14.489 39.035 1.00 14.36 ? 342 VAL A N 1 ATOM 2624 C CA . VAL A 1 342 ? -42.308 13.690 38.148 1.00 14.69 ? 342 VAL A CA 1 ATOM 2625 C C . VAL A 1 342 ? -41.302 12.943 37.256 1.00 15.32 ? 342 VAL A C 1 ATOM 2626 O O . VAL A 1 342 ? -40.606 13.568 36.452 1.00 14.93 ? 342 VAL A O 1 ATOM 2627 C CB . VAL A 1 342 ? -43.261 14.584 37.307 1.00 15.37 ? 342 VAL A CB 1 ATOM 2628 C CG1 . VAL A 1 342 ? -44.045 13.742 36.302 1.00 15.59 ? 342 VAL A CG1 1 ATOM 2629 C CG2 . VAL A 1 342 ? -44.226 15.313 38.227 1.00 14.46 ? 342 VAL A CG2 1 ATOM 2630 N N . PRO A 1 343 ? -41.218 11.599 37.391 1.00 15.28 ? 343 PRO A N 1 ATOM 2631 C CA . PRO A 1 343 ? -40.272 10.817 36.592 1.00 15.02 ? 343 PRO A CA 1 ATOM 2632 C C . PRO A 1 343 ? -40.580 10.516 35.128 1.00 15.26 ? 343 PRO A C 1 ATOM 2633 O O . PRO A 1 343 ? -41.716 10.644 34.674 1.00 14.11 ? 343 PRO A O 1 ATOM 2634 C CB . PRO A 1 343 ? -40.140 9.531 37.408 1.00 15.98 ? 343 PRO A CB 1 ATOM 2635 C CG . PRO A 1 343 ? -41.538 9.315 37.898 1.00 16.95 ? 343 PRO A CG 1 ATOM 2636 C CD . PRO A 1 343 ? -41.974 10.715 38.308 1.00 15.30 ? 343 PRO A CD 1 ATOM 2637 N N . ARG A 1 344 ? -39.516 10.194 34.394 1.00 14.65 ? 344 ARG A N 1 ATOM 2638 C CA . ARG A 1 344 ? -39.572 9.797 32.988 1.00 15.82 ? 344 ARG A CA 1 ATOM 2639 C C . ARG A 1 344 ? -38.599 8.634 32.863 1.00 17.99 ? 344 ARG A C 1 ATOM 2640 O O . ARG A 1 344 ? -37.553 8.633 33.504 1.00 17.61 ? 344 ARG A O 1 ATOM 2641 C CB . ARG A 1 344 ? -39.146 10.927 32.040 1.00 16.02 ? 344 ARG A CB 1 ATOM 2642 C CG . ARG A 1 344 ? -40.125 12.099 31.898 1.00 16.13 ? 344 ARG A CG 1 ATOM 2643 C CD . ARG A 1 344 ? -41.494 11.683 31.368 1.00 16.06 ? 344 ARG A CD 1 ATOM 2644 N NE . ARG A 1 344 ? -42.375 12.842 31.228 1.00 17.95 ? 344 ARG A NE 1 ATOM 2645 C CZ . ARG A 1 344 ? -43.489 13.045 31.926 1.00 17.52 ? 344 ARG A CZ 1 ATOM 2646 N NH1 . ARG A 1 344 ? -43.894 12.166 32.836 1.00 16.91 ? 344 ARG A NH1 1 ATOM 2647 N NH2 . ARG A 1 344 ? -44.198 14.146 31.718 1.00 17.86 ? 344 ARG A NH2 1 ATOM 2648 N N . SER A 1 345 ? -38.971 7.622 32.086 1.00 19.30 ? 345 SER A N 1 ATOM 2649 C CA . SER A 1 345 ? -38.132 6.443 31.887 1.00 21.16 ? 345 SER A CA 1 ATOM 2650 C C . SER A 1 345 ? -38.034 6.136 30.401 1.00 20.14 ? 345 SER A C 1 ATOM 2651 O O . SER A 1 345 ? -39.051 6.089 29.710 1.00 20.39 ? 345 SER A O 1 ATOM 2652 C CB . SER A 1 345 ? -38.714 5.238 32.643 1.00 23.85 ? 345 SER A CB 1 ATOM 2653 O OG . SER A 1 345 ? -37.919 4.075 32.466 1.00 27.31 ? 345 SER A OG 1 ATOM 2654 N N . VAL A 1 346 ? -36.801 5.987 29.911 1.00 19.26 ? 346 VAL A N 1 ATOM 2655 C CA . VAL A 1 346 ? -36.525 5.678 28.501 1.00 20.18 ? 346 VAL A CA 1 ATOM 2656 C C . VAL A 1 346 ? -35.426 4.628 28.336 1.00 20.59 ? 346 VAL A C 1 ATOM 2657 O O . VAL A 1 346 ? -34.489 4.588 29.142 1.00 20.06 ? 346 VAL A O 1 ATOM 2658 C CB . VAL A 1 346 ? -36.056 6.931 27.680 1.00 21.29 ? 346 VAL A CB 1 ATOM 2659 C CG1 . VAL A 1 346 ? -37.163 7.881 27.510 1.00 21.33 ? 346 VAL A CG1 1 ATOM 2660 C CG2 . VAL A 1 346 ? -34.880 7.620 28.334 1.00 21.79 ? 346 VAL A CG2 1 ATOM 2661 N N . PRO A 1 347 ? -35.549 3.733 27.324 1.00 21.27 ? 347 PRO A N 1 ATOM 2662 C CA . PRO A 1 347 ? -34.487 2.733 27.142 1.00 21.95 ? 347 PRO A CA 1 ATOM 2663 C C . PRO A 1 347 ? -33.258 3.388 26.494 1.00 21.96 ? 347 PRO A C 1 ATOM 2664 O O . PRO A 1 347 ? -33.392 4.247 25.615 1.00 23.31 ? 347 PRO A O 1 ATOM 2665 C CB . PRO A 1 347 ? -35.141 1.695 26.222 1.00 23.21 ? 347 PRO A CB 1 ATOM 2666 C CG . PRO A 1 347 ? -36.167 2.481 25.456 1.00 22.82 ? 347 PRO A CG 1 ATOM 2667 C CD . PRO A 1 347 ? -36.744 3.365 26.530 1.00 22.29 ? 347 PRO A CD 1 ATOM 2668 N N . VAL A 1 348 ? -32.078 3.066 27.013 1.00 21.13 ? 348 VAL A N 1 ATOM 2669 C CA . VAL A 1 348 ? -30.825 3.613 26.493 1.00 21.11 ? 348 VAL A CA 1 ATOM 2670 C C . VAL A 1 348 ? -29.931 2.556 25.842 1.00 21.52 ? 348 VAL A C 1 ATOM 2671 O O . VAL A 1 348 ? -29.000 2.889 25.106 1.00 19.79 ? 348 VAL A O 1 ATOM 2672 C CB . VAL A 1 348 ? -30.027 4.384 27.585 1.00 20.21 ? 348 VAL A CB 1 ATOM 2673 C CG1 . VAL A 1 348 ? -30.695 5.715 27.880 1.00 20.68 ? 348 VAL A CG1 1 ATOM 2674 C CG2 . VAL A 1 348 ? -29.887 3.557 28.868 1.00 21.77 ? 348 VAL A CG2 1 ATOM 2675 N N . ASN A 1 349 ? -30.255 1.286 26.093 1.00 21.45 ? 349 ASN A N 1 ATOM 2676 C CA . ASN A 1 349 ? -29.517 0.134 25.564 1.00 22.00 ? 349 ASN A CA 1 ATOM 2677 C C . ASN A 1 349 ? -29.677 -0.048 24.048 1.00 21.59 ? 349 ASN A C 1 ATOM 2678 O O . ASN A 1 349 ? -28.786 -0.565 23.375 1.00 21.30 ? 349 ASN A O 1 ATOM 2679 C CB . ASN A 1 349 ? -29.974 -1.147 26.288 1.00 23.20 ? 349 ASN A CB 1 ATOM 2680 C CG . ASN A 1 349 ? -31.460 -1.457 26.070 1.00 25.25 ? 349 ASN A CG 1 ATOM 2681 O OD1 . ASN A 1 349 ? -32.332 -0.830 26.671 1.00 27.96 ? 349 ASN A OD1 1 ATOM 2682 N ND2 . ASN A 1 349 ? -31.745 -2.403 25.181 1.00 25.76 ? 349 ASN A ND2 1 ATOM 2683 N N . SER A 1 350 ? -30.819 0.405 23.536 1.00 20.83 ? 350 SER A N 1 ATOM 2684 C CA . SER A 1 350 ? -31.181 0.290 22.125 1.00 22.10 ? 350 SER A CA 1 ATOM 2685 C C . SER A 1 350 ? -30.665 1.378 21.178 1.00 20.65 ? 350 SER A C 1 ATOM 2686 O O . SER A 1 350 ? -30.856 1.271 19.963 1.00 18.64 ? 350 SER A O 1 ATOM 2687 C CB . SER A 1 350 ? -32.707 0.172 22.007 1.00 23.05 ? 350 SER A CB 1 ATOM 2688 O OG . SER A 1 350 ? -33.351 1.127 22.838 1.00 24.03 ? 350 SER A OG 1 ATOM 2689 N N . PHE A 1 351 ? -29.996 2.398 21.722 1.00 21.03 ? 351 PHE A N 1 ATOM 2690 C CA . PHE A 1 351 ? -29.462 3.495 20.909 1.00 20.66 ? 351 PHE A CA 1 ATOM 2691 C C . PHE A 1 351 ? -28.325 3.082 19.967 1.00 21.11 ? 351 PHE A C 1 ATOM 2692 O O . PHE A 1 351 ? -27.351 2.451 20.381 1.00 21.98 ? 351 PHE A O 1 ATOM 2693 C CB . PHE A 1 351 ? -29.017 4.694 21.782 1.00 20.62 ? 351 PHE A CB 1 ATOM 2694 C CG . PHE A 1 351 ? -28.451 5.859 20.984 1.00 17.33 ? 351 PHE A CG 1 ATOM 2695 C CD1 . PHE A 1 351 ? -29.288 6.629 20.154 1.00 18.44 ? 351 PHE A CD1 1 ATOM 2696 C CD2 . PHE A 1 351 ? -27.065 6.119 20.975 1.00 18.01 ? 351 PHE A CD2 1 ATOM 2697 C CE1 . PHE A 1 351 ? -28.758 7.638 19.308 1.00 17.60 ? 351 PHE A CE1 1 ATOM 2698 C CE2 . PHE A 1 351 ? -26.514 7.124 20.134 1.00 18.52 ? 351 PHE A CE2 1 ATOM 2699 C CZ . PHE A 1 351 ? -27.369 7.885 19.294 1.00 18.76 ? 351 PHE A CZ 1 ATOM 2700 N N . VAL A 1 352 ? -28.478 3.472 18.700 1.00 19.78 ? 352 VAL A N 1 ATOM 2701 C CA . VAL A 1 352 ? -27.498 3.216 17.645 1.00 21.79 ? 352 VAL A CA 1 ATOM 2702 C C . VAL A 1 352 ? -27.261 4.557 16.938 1.00 21.89 ? 352 VAL A C 1 ATOM 2703 O O . VAL A 1 352 ? -28.220 5.227 16.529 1.00 21.90 ? 352 VAL A O 1 ATOM 2704 C CB . VAL A 1 352 ? -28.008 2.173 16.575 1.00 20.65 ? 352 VAL A CB 1 ATOM 2705 C CG1 . VAL A 1 352 ? -26.877 1.789 15.612 1.00 22.29 ? 352 VAL A CG1 1 ATOM 2706 C CG2 . VAL A 1 352 ? -28.561 0.916 17.236 1.00 22.75 ? 352 VAL A CG2 1 ATOM 2707 N N . LYS A 1 353 ? -25.987 4.938 16.809 1.00 22.03 ? 353 LYS A N 1 ATOM 2708 C CA . LYS A 1 353 ? -25.581 6.174 16.130 1.00 23.41 ? 353 LYS A CA 1 ATOM 2709 C C . LYS A 1 353 ? -25.788 6.011 14.617 1.00 23.72 ? 353 LYS A C 1 ATOM 2710 O O . LYS A 1 353 ? -25.223 5.107 13.999 1.00 23.74 ? 353 LYS A O 1 ATOM 2711 C CB . LYS A 1 353 ? -24.108 6.495 16.439 1.00 24.99 ? 353 LYS A CB 1 ATOM 2712 C CG . LYS A 1 353 ? -23.532 7.687 15.676 1.00 25.86 ? 353 LYS A CG 1 ATOM 2713 C CD . LYS A 1 353 ? -22.030 7.809 15.857 1.00 27.88 ? 353 LYS A CD 1 ATOM 2714 C CE . LYS A 1 353 ? -21.476 8.885 14.931 1.00 29.69 ? 353 LYS A CE 1 ATOM 2715 N NZ . LYS A 1 353 ? -20.011 9.091 15.106 1.00 31.99 ? 353 LYS A NZ 1 ATOM 2716 N N . ARG A 1 354 ? -26.659 6.852 14.059 1.00 23.25 ? 354 ARG A N 1 ATOM 2717 C CA . ARG A 1 354 ? -26.995 6.854 12.629 1.00 23.69 ? 354 ARG A CA 1 ATOM 2718 C C . ARG A 1 354 ? -26.972 8.313 12.150 1.00 22.23 ? 354 ARG A C 1 ATOM 2719 O O . ARG A 1 354 ? -27.100 9.223 12.976 1.00 19.93 ? 354 ARG A O 1 ATOM 2720 C CB . ARG A 1 354 ? -28.420 6.308 12.406 1.00 26.77 ? 354 ARG A CB 1 ATOM 2721 C CG . ARG A 1 354 ? -28.679 4.846 12.763 1.00 32.39 ? 354 ARG A CG 1 ATOM 2722 C CD . ARG A 1 354 ? -30.095 4.417 12.353 1.00 37.14 ? 354 ARG A CD 1 ATOM 2723 N NE . ARG A 1 354 ? -31.143 5.341 12.806 1.00 40.63 ? 354 ARG A NE 1 ATOM 2724 C CZ . ARG A 1 354 ? -31.706 5.337 14.016 1.00 43.45 ? 354 ARG A CZ 1 ATOM 2725 N NH1 . ARG A 1 354 ? -31.337 4.452 14.937 1.00 43.91 ? 354 ARG A NH1 1 ATOM 2726 N NH2 . ARG A 1 354 ? -32.640 6.235 14.306 1.00 43.92 ? 354 ARG A NH2 1 ATOM 2727 N N . PRO A 1 355 ? -26.796 8.565 10.824 1.00 20.67 ? 355 PRO A N 1 ATOM 2728 C CA . PRO A 1 355 ? -26.785 9.957 10.350 1.00 19.39 ? 355 PRO A CA 1 ATOM 2729 C C . PRO A 1 355 ? -28.074 10.732 10.662 1.00 18.74 ? 355 PRO A C 1 ATOM 2730 O O . PRO A 1 355 ? -28.014 11.925 10.972 1.00 17.36 ? 355 PRO A O 1 ATOM 2731 C CB . PRO A 1 355 ? -26.590 9.796 8.844 1.00 19.37 ? 355 PRO A CB 1 ATOM 2732 C CG . PRO A 1 355 ? -25.693 8.626 8.762 1.00 21.19 ? 355 PRO A CG 1 ATOM 2733 C CD . PRO A 1 355 ? -26.331 7.667 9.742 1.00 21.22 ? 355 PRO A CD 1 ATOM 2734 N N . ASP A 1 356 ? -29.211 10.026 10.682 1.00 17.41 ? 356 ASP A N 1 ATOM 2735 C CA . ASP A 1 356 ? -30.512 10.650 10.952 1.00 18.76 ? 356 ASP A CA 1 ATOM 2736 C C . ASP A 1 356 ? -30.819 11.017 12.415 1.00 17.05 ? 356 ASP A C 1 ATOM 2737 O O . ASP A 1 356 ? -31.879 11.581 12.706 1.00 17.79 ? 356 ASP A O 1 ATOM 2738 C CB . ASP A 1 356 ? -31.672 9.861 10.291 1.00 19.72 ? 356 ASP A CB 1 ATOM 2739 C CG . ASP A 1 356 ? -31.946 8.494 10.936 1.00 22.42 ? 356 ASP A CG 1 ATOM 2740 O OD1 . ASP A 1 356 ? -31.280 8.108 11.923 1.00 21.04 ? 356 ASP A OD1 1 ATOM 2741 O OD2 . ASP A 1 356 ? -32.859 7.800 10.436 1.00 24.98 ? 356 ASP A OD2 1 ATOM 2742 N N . ASN A 1 357 ? -29.919 10.642 13.325 1.00 15.25 ? 357 ASN A N 1 ATOM 2743 C CA . ASN A 1 357 ? -30.068 10.974 14.741 1.00 14.32 ? 357 ASN A CA 1 ATOM 2744 C C . ASN A 1 357 ? -28.835 11.703 15.289 1.00 12.98 ? 357 ASN A C 1 ATOM 2745 O O . ASN A 1 357 ? -28.742 11.987 16.484 1.00 12.91 ? 357 ASN A O 1 ATOM 2746 C CB . ASN A 1 357 ? -30.464 9.744 15.598 1.00 14.69 ? 357 ASN A CB 1 ATOM 2747 C CG . ASN A 1 357 ? -29.372 8.671 15.705 1.00 15.21 ? 357 ASN A CG 1 ATOM 2748 O OD1 . ASN A 1 357 ? -28.181 8.928 15.535 1.00 13.44 ? 357 ASN A OD1 1 ATOM 2749 N ND2 . ASN A 1 357 ? -29.794 7.461 16.046 1.00 16.00 ? 357 ASN A ND2 1 ATOM 2750 N N . THR A 1 358 ? -27.890 11.979 14.394 1.00 13.16 ? 358 THR A N 1 ATOM 2751 C CA . THR A 1 358 ? -26.648 12.651 14.745 1.00 13.80 ? 358 THR A CA 1 ATOM 2752 C C . THR A 1 358 ? -26.601 14.078 14.207 1.00 13.17 ? 358 THR A C 1 ATOM 2753 O O . THR A 1 358 ? -26.931 14.338 13.042 1.00 11.58 ? 358 THR A O 1 ATOM 2754 C CB . THR A 1 358 ? -25.424 11.833 14.268 1.00 15.39 ? 358 THR A CB 1 ATOM 2755 O OG1 . THR A 1 358 ? -25.481 10.525 14.853 1.00 15.50 ? 358 THR A OG1 1 ATOM 2756 C CG2 . THR A 1 358 ? -24.113 12.481 14.688 1.00 15.36 ? 358 THR A CG2 1 ATOM 2757 N N . LEU A 1 359 ? -26.201 14.995 15.089 1.00 12.46 ? 359 LEU A N 1 ATOM 2758 C CA . LEU A 1 359 ? -26.078 16.421 14.776 1.00 12.43 ? 359 LEU A CA 1 ATOM 2759 C C . LEU A 1 359 ? -24.629 16.898 15.000 1.00 12.70 ? 359 LEU A C 1 ATOM 2760 O O . LEU A 1 359 ? -24.260 17.277 16.118 1.00 11.96 ? 359 LEU A O 1 ATOM 2761 C CB . LEU A 1 359 ? -27.078 17.242 15.618 1.00 12.01 ? 359 LEU A CB 1 ATOM 2762 C CG . LEU A 1 359 ? -28.580 16.999 15.371 1.00 11.53 ? 359 LEU A CG 1 ATOM 2763 C CD1 . LEU A 1 359 ? -29.427 17.690 16.423 1.00 11.57 ? 359 LEU A CD1 1 ATOM 2764 C CD2 . LEU A 1 359 ? -28.960 17.454 13.966 1.00 12.10 ? 359 LEU A CD2 1 ATOM 2765 N N . PRO A 1 360 ? -23.768 16.810 13.955 1.00 12.48 ? 360 PRO A N 1 ATOM 2766 C CA . PRO A 1 360 ? -22.368 17.240 14.063 1.00 13.55 ? 360 PRO A CA 1 ATOM 2767 C C . PRO A 1 360 ? -22.232 18.757 14.011 1.00 13.25 ? 360 PRO A C 1 ATOM 2768 O O . PRO A 1 360 ? -22.610 19.387 13.018 1.00 13.50 ? 360 PRO A O 1 ATOM 2769 C CB . PRO A 1 360 ? -21.713 16.611 12.825 1.00 14.40 ? 360 PRO A CB 1 ATOM 2770 C CG . PRO A 1 360 ? -22.630 15.490 12.450 1.00 15.98 ? 360 PRO A CG 1 ATOM 2771 C CD . PRO A 1 360 ? -23.969 16.110 12.675 1.00 13.67 ? 360 PRO A CD 1 ATOM 2772 N N . VAL A 1 361 ? -21.733 19.330 15.105 1.00 11.88 ? 361 VAL A N 1 ATOM 2773 C CA . VAL A 1 361 ? -21.497 20.769 15.213 1.00 11.84 ? 361 VAL A CA 1 ATOM 2774 C C . VAL A 1 361 ? -20.072 20.956 14.708 1.00 13.16 ? 361 VAL A C 1 ATOM 2775 O O . VAL A 1 361 ? -19.202 20.136 14.998 1.00 12.12 ? 361 VAL A O 1 ATOM 2776 C CB . VAL A 1 361 ? -21.634 21.260 16.691 1.00 11.48 ? 361 VAL A CB 1 ATOM 2777 C CG1 . VAL A 1 361 ? -21.190 22.719 16.846 1.00 14.17 ? 361 VAL A CG1 1 ATOM 2778 C CG2 . VAL A 1 361 ? -23.071 21.121 17.147 1.00 12.06 ? 361 VAL A CG2 1 ATOM 2779 N N . ALA A 1 362 ? -19.859 21.992 13.901 1.00 13.34 ? 362 ALA A N 1 ATOM 2780 C CA . ALA A 1 362 ? -18.539 22.263 13.351 1.00 13.62 ? 362 ALA A CA 1 ATOM 2781 C C . ALA A 1 362 ? -18.281 23.730 13.104 1.00 13.58 ? 362 ALA A C 1 ATOM 2782 O O . ALA A 1 362 ? -19.175 24.467 12.694 1.00 13.84 ? 362 ALA A O 1 ATOM 2783 C CB . ALA A 1 362 ? -18.319 21.475 12.054 1.00 14.42 ? 362 ALA A CB 1 ATOM 2784 N N . LEU A 1 363 ? -17.055 24.151 13.395 1.00 14.23 ? 363 LEU A N 1 ATOM 2785 C CA . LEU A 1 363 ? -16.633 25.521 13.152 1.00 14.07 ? 363 LEU A CA 1 ATOM 2786 C C . LEU A 1 363 ? -15.933 25.518 11.799 1.00 15.12 ? 363 LEU A C 1 ATOM 2787 O O . LEU A 1 363 ? -14.922 24.830 11.609 1.00 16.06 ? 363 LEU A O 1 ATOM 2788 C CB . LEU A 1 363 ? -15.683 26.018 14.244 1.00 14.00 ? 363 LEU A CB 1 ATOM 2789 C CG . LEU A 1 363 ? -15.153 27.456 14.146 1.00 14.56 ? 363 LEU A CG 1 ATOM 2790 C CD1 . LEU A 1 363 ? -16.287 28.478 14.059 1.00 15.26 ? 363 LEU A CD1 1 ATOM 2791 C CD2 . LEU A 1 363 ? -14.265 27.737 15.334 1.00 14.74 ? 363 LEU A CD2 1 ATOM 2792 N N . ASP A 1 364 ? -16.516 26.256 10.860 1.00 15.73 ? 364 ASP A N 1 ATOM 2793 C CA . ASP A 1 364 ? -15.988 26.376 9.511 1.00 18.36 ? 364 ASP A CA 1 ATOM 2794 C C . ASP A 1 364 ? -15.225 27.692 9.412 1.00 19.20 ? 364 ASP A C 1 ATOM 2795 O O . ASP A 1 364 ? -15.814 28.770 9.495 1.00 18.85 ? 364 ASP A O 1 ATOM 2796 C CB . ASP A 1 364 ? -17.136 26.324 8.487 1.00 19.46 ? 364 ASP A CB 1 ATOM 2797 C CG . ASP A 1 364 ? -16.650 26.132 7.051 1.00 21.26 ? 364 ASP A CG 1 ATOM 2798 O OD1 . ASP A 1 364 ? -15.470 26.413 6.758 1.00 22.12 ? 364 ASP A OD1 1 ATOM 2799 O OD2 . ASP A 1 364 ? -17.458 25.696 6.209 1.00 24.76 ? 364 ASP A OD2 1 ATOM 2800 N N . LEU A 1 365 ? -13.913 27.575 9.210 1.00 21.56 ? 365 LEU A N 1 ATOM 2801 C CA . LEU A 1 365 ? -13.009 28.722 9.097 1.00 23.95 ? 365 LEU A CA 1 ATOM 2802 C C . LEU A 1 365 ? -12.634 29.067 7.649 1.00 24.90 ? 365 LEU A C 1 ATOM 2803 O O . LEU A 1 365 ? -11.933 30.057 7.412 1.00 25.50 ? 365 LEU A O 1 ATOM 2804 C CB . LEU A 1 365 ? -11.725 28.450 9.898 1.00 23.83 ? 365 LEU A CB 1 ATOM 2805 C CG . LEU A 1 365 ? -11.829 28.092 11.388 1.00 24.31 ? 365 LEU A CG 1 ATOM 2806 C CD1 . LEU A 1 365 ? -10.521 27.492 11.870 1.00 26.23 ? 365 LEU A CD1 1 ATOM 2807 C CD2 . LEU A 1 365 ? -12.208 29.315 12.216 1.00 23.23 ? 365 LEU A CD2 1 ATOM 2808 N N . THR A 1 366 ? -13.141 28.289 6.692 1.00 25.69 ? 366 THR A N 1 ATOM 2809 C CA . THR A 1 366 ? -12.823 28.471 5.269 1.00 27.98 ? 366 THR A CA 1 ATOM 2810 C C . THR A 1 366 ? -13.554 29.568 4.487 1.00 29.47 ? 366 THR A C 1 ATOM 2811 O O . THR A 1 366 ? -13.037 30.048 3.470 1.00 31.20 ? 366 THR A O 1 ATOM 2812 C CB . THR A 1 366 ? -12.970 27.140 4.479 1.00 27.84 ? 366 THR A CB 1 ATOM 2813 O OG1 . THR A 1 366 ? -14.353 26.766 4.405 1.00 27.95 ? 366 THR A OG1 1 ATOM 2814 C CG2 . THR A 1 366 ? -12.186 26.020 5.152 1.00 27.62 ? 366 THR A CG2 1 ATOM 2815 N N . GLY A 1 367 ? -14.742 29.955 4.948 1.00 29.69 ? 367 GLY A N 1 ATOM 2816 C CA . GLY A 1 367 ? -15.522 30.969 4.251 1.00 29.38 ? 367 GLY A CA 1 ATOM 2817 C C . GLY A 1 367 ? -15.389 32.404 4.722 1.00 29.14 ? 367 GLY A C 1 ATOM 2818 O O . GLY A 1 367 ? -14.367 32.807 5.283 1.00 29.55 ? 367 GLY A O 1 ATOM 2819 N N . THR A 1 368 ? -16.433 33.179 4.440 1.00 29.93 ? 368 THR A N 1 ATOM 2820 C CA . THR A 1 368 ? -16.527 34.589 4.808 1.00 29.64 ? 368 THR A CA 1 ATOM 2821 C C . THR A 1 368 ? -17.895 34.753 5.493 1.00 28.09 ? 368 THR A C 1 ATOM 2822 O O . THR A 1 368 ? -18.927 34.440 4.884 1.00 29.57 ? 368 THR A O 1 ATOM 2823 C CB . THR A 1 368 ? -16.388 35.519 3.562 1.00 31.36 ? 368 THR A CB 1 ATOM 2824 O OG1 . THR A 1 368 ? -15.107 35.303 2.956 1.00 33.28 ? 368 THR A OG1 1 ATOM 2825 C CG2 . THR A 1 368 ? -16.492 37.004 3.952 1.00 33.03 ? 368 THR A CG2 1 ATOM 2826 N N . PRO A 1 369 ? -17.920 35.156 6.792 1.00 25.27 ? 369 PRO A N 1 ATOM 2827 C CA . PRO A 1 369 ? -16.835 35.490 7.737 1.00 23.09 ? 369 PRO A CA 1 ATOM 2828 C C . PRO A 1 369 ? -16.052 34.280 8.275 1.00 20.65 ? 369 PRO A C 1 ATOM 2829 O O . PRO A 1 369 ? -16.346 33.142 7.905 1.00 19.88 ? 369 PRO A O 1 ATOM 2830 C CB . PRO A 1 369 ? -17.576 36.217 8.848 1.00 23.34 ? 369 PRO A CB 1 ATOM 2831 C CG . PRO A 1 369 ? -18.902 35.524 8.869 1.00 23.08 ? 369 PRO A CG 1 ATOM 2832 C CD . PRO A 1 369 ? -19.232 35.450 7.407 1.00 24.63 ? 369 PRO A CD 1 ATOM 2833 N N . LEU A 1 370 ? -15.057 34.536 9.123 1.00 18.64 ? 370 LEU A N 1 ATOM 2834 C CA . LEU A 1 370 ? -14.224 33.466 9.676 1.00 18.25 ? 370 LEU A CA 1 ATOM 2835 C C . LEU A 1 370 ? -14.942 32.495 10.617 1.00 15.73 ? 370 LEU A C 1 ATOM 2836 O O . LEU A 1 370 ? -14.808 31.283 10.471 1.00 16.55 ? 370 LEU A O 1 ATOM 2837 C CB . LEU A 1 370 ? -12.988 34.046 10.372 1.00 18.87 ? 370 LEU A CB 1 ATOM 2838 C CG . LEU A 1 370 ? -11.886 33.032 10.697 1.00 20.34 ? 370 LEU A CG 1 ATOM 2839 C CD1 . LEU A 1 370 ? -11.115 32.645 9.444 1.00 21.93 ? 370 LEU A CD1 1 ATOM 2840 C CD2 . LEU A 1 370 ? -10.965 33.612 11.714 1.00 21.12 ? 370 LEU A CD2 1 ATOM 2841 N N . PHE A 1 371 ? -15.694 33.034 11.573 1.00 14.18 ? 371 PHE A N 1 ATOM 2842 C CA . PHE A 1 371 ? -16.415 32.206 12.534 1.00 15.06 ? 371 PHE A CA 1 ATOM 2843 C C . PHE A 1 371 ? -17.836 31.896 12.085 1.00 13.51 ? 371 PHE A C 1 ATOM 2844 O O . PHE A 1 371 ? -18.762 32.688 12.273 1.00 14.66 ? 371 PHE A O 1 ATOM 2845 C CB . PHE A 1 371 ? -16.386 32.836 13.935 1.00 15.98 ? 371 PHE A CB 1 ATOM 2846 C CG . PHE A 1 371 ? -15.029 32.800 14.585 1.00 20.50 ? 371 PHE A CG 1 ATOM 2847 C CD1 . PHE A 1 371 ? -14.614 31.666 15.310 1.00 23.34 ? 371 PHE A CD1 1 ATOM 2848 C CD2 . PHE A 1 371 ? -14.148 33.887 14.465 1.00 21.13 ? 371 PHE A CD2 1 ATOM 2849 C CE1 . PHE A 1 371 ? -13.325 31.613 15.912 1.00 25.39 ? 371 PHE A CE1 1 ATOM 2850 C CE2 . PHE A 1 371 ? -12.855 33.853 15.060 1.00 21.80 ? 371 PHE A CE2 1 ATOM 2851 C CZ . PHE A 1 371 ? -12.443 32.716 15.783 1.00 23.43 ? 371 PHE A CZ 1 ATOM 2852 N N . VAL A 1 372 ? -17.970 30.761 11.408 1.00 13.59 ? 372 VAL A N 1 ATOM 2853 C CA . VAL A 1 372 ? -19.256 30.290 10.907 1.00 13.26 ? 372 VAL A CA 1 ATOM 2854 C C . VAL A 1 372 ? -19.478 28.915 11.530 1.00 13.96 ? 372 VAL A C 1 ATOM 2855 O O . VAL A 1 372 ? -18.666 28.002 11.354 1.00 14.44 ? 372 VAL A O 1 ATOM 2856 C CB . VAL A 1 372 ? -19.275 30.221 9.342 1.00 13.43 ? 372 VAL A CB 1 ATOM 2857 C CG1 . VAL A 1 372 ? -20.574 29.632 8.842 1.00 14.22 ? 372 VAL A CG1 1 ATOM 2858 C CG2 . VAL A 1 372 ? -19.119 31.614 8.746 1.00 13.58 ? 372 VAL A CG2 1 ATOM 2859 N N . TRP A 1 373 ? -20.574 28.795 12.274 1.00 12.52 ? 373 TRP A N 1 ATOM 2860 C CA . TRP A 1 373 ? -20.931 27.553 12.953 1.00 13.02 ? 373 TRP A CA 1 ATOM 2861 C C . TRP A 1 373 ? -21.923 26.749 12.140 1.00 12.74 ? 373 TRP A C 1 ATOM 2862 O O . TRP A 1 373 ? -23.000 27.237 11.810 1.00 11.90 ? 373 TRP A O 1 ATOM 2863 C CB . TRP A 1 373 ? -21.498 27.858 14.334 1.00 11.41 ? 373 TRP A CB 1 ATOM 2864 C CG . TRP A 1 373 ? -20.488 28.421 15.283 1.00 12.27 ? 373 TRP A CG 1 ATOM 2865 C CD1 . TRP A 1 373 ? -20.274 29.741 15.560 1.00 11.41 ? 373 TRP A CD1 1 ATOM 2866 C CD2 . TRP A 1 373 ? -19.530 27.684 16.053 1.00 11.18 ? 373 TRP A CD2 1 ATOM 2867 N NE1 . TRP A 1 373 ? -19.240 29.877 16.455 1.00 11.49 ? 373 TRP A NE1 1 ATOM 2868 C CE2 . TRP A 1 373 ? -18.762 28.634 16.777 1.00 11.21 ? 373 TRP A CE2 1 ATOM 2869 C CE3 . TRP A 1 373 ? -19.237 26.308 16.202 1.00 9.76 ? 373 TRP A CE3 1 ATOM 2870 C CZ2 . TRP A 1 373 ? -17.706 28.256 17.645 1.00 9.78 ? 373 TRP A CZ2 1 ATOM 2871 C CZ3 . TRP A 1 373 ? -18.184 25.927 17.066 1.00 9.16 ? 373 TRP A CZ3 1 ATOM 2872 C CH2 . TRP A 1 373 ? -17.433 26.906 17.775 1.00 8.82 ? 373 TRP A CH2 1 ATOM 2873 N N . LYS A 1 374 ? -21.545 25.513 11.822 1.00 12.54 ? 374 LYS A N 1 ATOM 2874 C CA . LYS A 1 374 ? -22.369 24.628 11.009 1.00 15.08 ? 374 LYS A CA 1 ATOM 2875 C C . LYS A 1 374 ? -22.847 23.371 11.713 1.00 15.25 ? 374 LYS A C 1 ATOM 2876 O O . LYS A 1 374 ? -22.095 22.744 12.456 1.00 16.75 ? 374 LYS A O 1 ATOM 2877 C CB . LYS A 1 374 ? -21.620 24.244 9.721 1.00 15.23 ? 374 LYS A CB 1 ATOM 2878 C CG . LYS A 1 374 ? -21.253 25.438 8.841 1.00 17.73 ? 374 LYS A CG 1 ATOM 2879 C CD . LYS A 1 374 ? -20.881 25.045 7.429 1.00 18.10 ? 374 LYS A CD 1 ATOM 2880 C CE . LYS A 1 374 ? -20.682 26.286 6.573 1.00 17.54 ? 374 LYS A CE 1 ATOM 2881 N NZ . LYS A 1 374 ? -20.284 25.924 5.188 1.00 21.69 ? 374 LYS A NZ 1 ATOM 2882 N N . VAL A 1 375 ? -24.124 23.043 11.525 1.00 15.49 ? 375 VAL A N 1 ATOM 2883 C CA . VAL A 1 375 ? -24.696 21.832 12.108 1.00 14.49 ? 375 VAL A CA 1 ATOM 2884 C C . VAL A 1 375 ? -25.113 20.942 10.943 1.00 14.47 ? 375 VAL A C 1 ATOM 2885 O O . VAL A 1 375 ? -25.957 21.325 10.128 1.00 12.80 ? 375 VAL A O 1 ATOM 2886 C CB . VAL A 1 375 ? -25.901 22.094 13.046 1.00 13.98 ? 375 VAL A CB 1 ATOM 2887 C CG1 . VAL A 1 375 ? -26.195 20.835 13.861 1.00 14.46 ? 375 VAL A CG1 1 ATOM 2888 C CG2 . VAL A 1 375 ? -25.623 23.255 13.994 1.00 13.27 ? 375 VAL A CG2 1 ATOM 2889 N N . ASN A 1 376 ? -24.480 19.767 10.872 1.00 15.52 ? 376 ASN A N 1 ATOM 2890 C CA . ASN A 1 376 ? -24.678 18.764 9.820 1.00 16.15 ? 376 ASN A CA 1 ATOM 2891 C C . ASN A 1 376 ? -24.315 19.335 8.437 1.00 15.80 ? 376 ASN A C 1 ATOM 2892 O O . ASN A 1 376 ? -24.986 19.075 7.435 1.00 17.30 ? 376 ASN A O 1 ATOM 2893 C CB . ASN A 1 376 ? -26.102 18.162 9.862 1.00 16.99 ? 376 ASN A CB 1 ATOM 2894 C CG . ASN A 1 376 ? -26.145 16.705 9.399 1.00 19.97 ? 376 ASN A CG 1 ATOM 2895 O OD1 . ASN A 1 376 ? -25.196 15.938 9.612 1.00 15.86 ? 376 ASN A OD1 1 ATOM 2896 N ND2 . ASN A 1 376 ? -27.253 16.323 8.773 1.00 20.88 ? 376 ASN A ND2 1 ATOM 2897 N N . GLY A 1 377 ? -23.266 20.161 8.433 1.00 15.50 ? 377 GLY A N 1 ATOM 2898 C CA . GLY A 1 377 ? -22.759 20.784 7.218 1.00 15.33 ? 377 GLY A CA 1 ATOM 2899 C C . GLY A 1 377 ? -23.405 22.094 6.796 1.00 15.00 ? 377 GLY A C 1 ATOM 2900 O O . GLY A 1 377 ? -23.066 22.629 5.737 1.00 15.11 ? 377 GLY A O 1 ATOM 2901 N N . SER A 1 378 ? -24.285 22.643 7.633 1.00 14.27 ? 378 SER A N 1 ATOM 2902 C CA . SER A 1 378 ? -24.978 23.887 7.291 1.00 14.08 ? 378 SER A CA 1 ATOM 2903 C C . SER A 1 378 ? -25.216 24.850 8.448 1.00 13.99 ? 378 SER A C 1 ATOM 2904 O O . SER A 1 378 ? -25.667 24.447 9.528 1.00 12.58 ? 378 SER A O 1 ATOM 2905 C CB . SER A 1 378 ? -26.321 23.562 6.617 1.00 14.00 ? 378 SER A CB 1 ATOM 2906 O OG . SER A 1 378 ? -27.080 24.730 6.346 1.00 13.40 ? 378 SER A OG 1 ATOM 2907 N N . ASP A 1 379 ? -24.866 26.118 8.218 1.00 12.24 ? 379 ASP A N 1 ATOM 2908 C CA . ASP A 1 379 ? -25.097 27.184 9.190 1.00 11.31 ? 379 ASP A CA 1 ATOM 2909 C C . ASP A 1 379 ? -26.512 27.683 8.952 1.00 11.59 ? 379 ASP A C 1 ATOM 2910 O O . ASP A 1 379 ? -26.870 28.008 7.814 1.00 11.30 ? 379 ASP A O 1 ATOM 2911 C CB . ASP A 1 379 ? -24.079 28.335 9.063 1.00 10.62 ? 379 ASP A CB 1 ATOM 2912 C CG . ASP A 1 379 ? -23.959 28.898 7.651 1.00 13.72 ? 379 ASP A CG 1 ATOM 2913 O OD1 . ASP A 1 379 ? -23.687 28.127 6.709 1.00 12.27 ? 379 ASP A OD1 1 ATOM 2914 O OD2 . ASP A 1 379 ? -24.115 30.127 7.499 1.00 13.72 ? 379 ASP A OD2 1 ATOM 2915 N N . ILE A 1 380 ? -27.322 27.712 10.009 1.00 8.91 ? 380 ILE A N 1 ATOM 2916 C CA . ILE A 1 380 ? -28.707 28.157 9.875 1.00 10.65 ? 380 ILE A CA 1 ATOM 2917 C C . ILE A 1 380 ? -28.791 29.621 9.429 1.00 10.08 ? 380 ILE A C 1 ATOM 2918 O O . ILE A 1 380 ? -27.919 30.423 9.753 1.00 9.29 ? 380 ILE A O 1 ATOM 2919 C CB . ILE A 1 380 ? -29.545 27.895 11.176 1.00 10.87 ? 380 ILE A CB 1 ATOM 2920 C CG1 . ILE A 1 380 ? -31.031 27.712 10.819 1.00 10.69 ? 380 ILE A CG1 1 ATOM 2921 C CG2 . ILE A 1 380 ? -29.361 29.043 12.197 1.00 9.93 ? 380 ILE A CG2 1 ATOM 2922 C CD1 . ILE A 1 380 ? -31.917 27.177 11.941 1.00 9.08 ? 380 ILE A CD1 1 ATOM 2923 N N . ASN A 1 381 ? -29.771 29.901 8.580 1.00 10.90 ? 381 ASN A N 1 ATOM 2924 C CA . ASN A 1 381 ? -30.029 31.239 8.070 1.00 10.43 ? 381 ASN A CA 1 ATOM 2925 C C . ASN A 1 381 ? -31.486 31.193 7.665 1.00 10.53 ? 381 ASN A C 1 ATOM 2926 O O . ASN A 1 381 ? -31.840 30.589 6.653 1.00 10.05 ? 381 ASN A O 1 ATOM 2927 C CB . ASN A 1 381 ? -29.132 31.577 6.869 1.00 11.99 ? 381 ASN A CB 1 ATOM 2928 C CG . ASN A 1 381 ? -29.038 33.069 6.619 1.00 14.65 ? 381 ASN A CG 1 ATOM 2929 O OD1 . ASN A 1 381 ? -29.976 33.684 6.111 1.00 16.19 ? 381 ASN A OD1 1 ATOM 2930 N ND2 . ASN A 1 381 ? -27.903 33.665 6.988 1.00 17.32 ? 381 ASN A ND2 1 ATOM 2931 N N . VAL A 1 382 ? -32.331 31.776 8.510 1.00 8.21 ? 382 VAL A N 1 ATOM 2932 C CA . VAL A 1 382 ? -33.769 31.798 8.277 1.00 9.50 ? 382 VAL A CA 1 ATOM 2933 C C . VAL A 1 382 ? -34.204 32.981 7.423 1.00 10.58 ? 382 VAL A C 1 ATOM 2934 O O . VAL A 1 382 ? -33.447 33.938 7.233 1.00 11.51 ? 382 VAL A O 1 ATOM 2935 C CB . VAL A 1 382 ? -34.563 31.799 9.615 1.00 10.21 ? 382 VAL A CB 1 ATOM 2936 C CG1 . VAL A 1 382 ? -34.265 30.538 10.406 1.00 10.30 ? 382 VAL A CG1 1 ATOM 2937 C CG2 . VAL A 1 382 ? -34.257 33.063 10.443 1.00 7.77 ? 382 VAL A CG2 1 ATOM 2938 N N . ASP A 1 383 ? -35.418 32.890 6.893 1.00 11.27 ? 383 ASP A N 1 ATOM 2939 C CA . ASP A 1 383 ? -35.968 33.964 6.086 1.00 13.04 ? 383 ASP A CA 1 ATOM 2940 C C . ASP A 1 383 ? -37.041 34.632 6.931 1.00 13.64 ? 383 ASP A C 1 ATOM 2941 O O . ASP A 1 383 ? -38.121 34.074 7.139 1.00 14.64 ? 383 ASP A O 1 ATOM 2942 C CB . ASP A 1 383 ? -36.559 33.426 4.772 1.00 14.30 ? 383 ASP A CB 1 ATOM 2943 C CG . ASP A 1 383 ? -36.878 34.534 3.762 1.00 15.21 ? 383 ASP A CG 1 ATOM 2944 O OD1 . ASP A 1 383 ? -37.028 35.717 4.157 1.00 15.98 ? 383 ASP A OD1 1 ATOM 2945 O OD2 . ASP A 1 383 ? -36.982 34.212 2.559 1.00 16.59 ? 383 ASP A OD2 1 ATOM 2946 N N . TRP A 1 384 ? -36.726 35.835 7.408 1.00 14.06 ? 384 TRP A N 1 ATOM 2947 C CA . TRP A 1 384 ? -37.635 36.642 8.219 1.00 14.04 ? 384 TRP A CA 1 ATOM 2948 C C . TRP A 1 384 ? -38.950 36.903 7.483 1.00 13.63 ? 384 TRP A C 1 ATOM 2949 O O . TRP A 1 384 ? -40.014 36.918 8.098 1.00 11.57 ? 384 TRP A O 1 ATOM 2950 C CB . TRP A 1 384 ? -36.981 37.979 8.563 1.00 14.30 ? 384 TRP A CB 1 ATOM 2951 C CG . TRP A 1 384 ? -35.941 37.954 9.668 1.00 14.38 ? 384 TRP A CG 1 ATOM 2952 C CD1 . TRP A 1 384 ? -35.831 37.050 10.701 1.00 15.21 ? 384 TRP A CD1 1 ATOM 2953 C CD2 . TRP A 1 384 ? -34.886 38.902 9.854 1.00 13.41 ? 384 TRP A CD2 1 ATOM 2954 N NE1 . TRP A 1 384 ? -34.771 37.382 11.513 1.00 13.00 ? 384 TRP A NE1 1 ATOM 2955 C CE2 . TRP A 1 384 ? -34.171 38.512 11.021 1.00 12.97 ? 384 TRP A CE2 1 ATOM 2956 C CE3 . TRP A 1 384 ? -34.467 40.052 9.147 1.00 11.92 ? 384 TRP A CE3 1 ATOM 2957 C CZ2 . TRP A 1 384 ? -33.048 39.234 11.501 1.00 13.69 ? 384 TRP A CZ2 1 ATOM 2958 C CZ3 . TRP A 1 384 ? -33.349 40.773 9.621 1.00 12.01 ? 384 TRP A CZ3 1 ATOM 2959 C CH2 . TRP A 1 384 ? -32.651 40.354 10.792 1.00 10.86 ? 384 TRP A CH2 1 ATOM 2960 N N . GLY A 1 385 ? -38.846 37.015 6.155 1.00 13.37 ? 385 GLY A N 1 ATOM 2961 C CA . GLY A 1 385 ? -39.985 37.260 5.286 1.00 13.82 ? 385 GLY A CA 1 ATOM 2962 C C . GLY A 1 385 ? -40.743 36.020 4.846 1.00 15.80 ? 385 GLY A C 1 ATOM 2963 O O . GLY A 1 385 ? -41.841 36.143 4.302 1.00 15.30 ? 385 GLY A O 1 ATOM 2964 N N . LYS A 1 386 ? -40.150 34.836 5.029 1.00 15.17 ? 386 LYS A N 1 ATOM 2965 C CA . LYS A 1 386 ? -40.820 33.579 4.677 1.00 16.28 ? 386 LYS A CA 1 ATOM 2966 C C . LYS A 1 386 ? -40.502 32.492 5.714 1.00 15.90 ? 386 LYS A C 1 ATOM 2967 O O . LYS A 1 386 ? -39.632 31.632 5.502 1.00 14.14 ? 386 LYS A O 1 ATOM 2968 C CB . LYS A 1 386 ? -40.493 33.114 3.246 1.00 18.76 ? 386 LYS A CB 1 ATOM 2969 C CG . LYS A 1 386 ? -41.534 32.123 2.703 1.00 20.75 ? 386 LYS A CG 1 ATOM 2970 C CD . LYS A 1 386 ? -41.262 31.668 1.275 1.00 24.58 ? 386 LYS A CD 1 ATOM 2971 C CE . LYS A 1 386 ? -42.350 30.693 0.822 1.00 26.61 ? 386 LYS A CE 1 ATOM 2972 N NZ . LYS A 1 386 ? -42.046 30.038 -0.482 1.00 30.29 ? 386 LYS A NZ 1 ATOM 2973 N N . PRO A 1 387 ? -41.206 32.527 6.867 1.00 15.21 ? 387 PRO A N 1 ATOM 2974 C CA . PRO A 1 387 ? -41.025 31.565 7.960 1.00 14.66 ? 387 PRO A CA 1 ATOM 2975 C C . PRO A 1 387 ? -41.449 30.158 7.588 1.00 13.77 ? 387 PRO A C 1 ATOM 2976 O O . PRO A 1 387 ? -42.231 29.981 6.655 1.00 12.03 ? 387 PRO A O 1 ATOM 2977 C CB . PRO A 1 387 ? -41.935 32.122 9.058 1.00 13.55 ? 387 PRO A CB 1 ATOM 2978 C CG . PRO A 1 387 ? -42.031 33.565 8.721 1.00 16.63 ? 387 PRO A CG 1 ATOM 2979 C CD . PRO A 1 387 ? -42.215 33.526 7.256 1.00 15.66 ? 387 PRO A CD 1 ATOM 2980 N N . ILE A 1 388 ? -40.956 29.173 8.343 1.00 14.60 ? 388 ILE A N 1 ATOM 2981 C CA . ILE A 1 388 ? -41.275 27.758 8.122 1.00 13.93 ? 388 ILE A CA 1 ATOM 2982 C C . ILE A 1 388 ? -42.783 27.503 8.181 1.00 13.64 ? 388 ILE A C 1 ATOM 2983 O O . ILE A 1 388 ? -43.307 26.690 7.417 1.00 13.81 ? 388 ILE A O 1 ATOM 2984 C CB . ILE A 1 388 ? -40.488 26.847 9.117 1.00 14.69 ? 388 ILE A CB 1 ATOM 2985 C CG1 . ILE A 1 388 ? -38.984 26.980 8.850 1.00 15.49 ? 388 ILE A CG1 1 ATOM 2986 C CG2 . ILE A 1 388 ? -40.929 25.372 9.024 1.00 14.08 ? 388 ILE A CG2 1 ATOM 2987 C CD1 . ILE A 1 388 ? -38.552 26.630 7.423 1.00 15.80 ? 388 ILE A CD1 1 ATOM 2988 N N . ILE A 1 389 ? -43.472 28.273 9.022 1.00 14.06 ? 389 ILE A N 1 ATOM 2989 C CA . ILE A 1 389 ? -44.923 28.178 9.162 1.00 13.17 ? 389 ILE A CA 1 ATOM 2990 C C . ILE A 1 389 ? -45.650 28.602 7.875 1.00 14.17 ? 389 ILE A C 1 ATOM 2991 O O . ILE A 1 389 ? -46.745 28.103 7.604 1.00 13.70 ? 389 ILE A O 1 ATOM 2992 C CB . ILE A 1 389 ? -45.421 28.930 10.442 1.00 12.78 ? 389 ILE A CB 1 ATOM 2993 C CG1 . ILE A 1 389 ? -45.028 28.133 11.698 1.00 12.66 ? 389 ILE A CG1 1 ATOM 2994 C CG2 . ILE A 1 389 ? -46.941 29.199 10.418 1.00 11.61 ? 389 ILE A CG2 1 ATOM 2995 C CD1 . ILE A 1 389 ? -45.508 26.684 11.758 1.00 12.71 ? 389 ILE A CD1 1 ATOM 2996 N N . ASP A 1 390 ? -45.012 29.447 7.056 1.00 14.76 ? 390 ASP A N 1 ATOM 2997 C CA . ASP A 1 390 ? -45.603 29.879 5.778 1.00 15.25 ? 390 ASP A CA 1 ATOM 2998 C C . ASP A 1 390 ? -45.591 28.709 4.807 1.00 15.38 ? 390 ASP A C 1 ATOM 2999 O O . ASP A 1 390 ? -46.549 28.516 4.058 1.00 14.06 ? 390 ASP A O 1 ATOM 3000 C CB . ASP A 1 390 ? -44.866 31.079 5.170 1.00 15.26 ? 390 ASP A CB 1 ATOM 3001 C CG . ASP A 1 390 ? -45.591 31.657 3.959 1.00 18.81 ? 390 ASP A CG 1 ATOM 3002 O OD1 . ASP A 1 390 ? -46.793 31.985 4.079 1.00 19.67 ? 390 ASP A OD1 1 ATOM 3003 O OD2 . ASP A 1 390 ? -44.968 31.748 2.883 1.00 19.37 ? 390 ASP A OD2 1 ATOM 3004 N N . TYR A 1 391 ? -44.517 27.916 4.863 1.00 15.90 ? 391 TYR A N 1 ATOM 3005 C CA . TYR A 1 391 ? -44.364 26.722 4.031 1.00 16.27 ? 391 TYR A CA 1 ATOM 3006 C C . TYR A 1 391 ? -45.427 25.688 4.405 1.00 16.02 ? 391 TYR A C 1 ATOM 3007 O O . TYR A 1 391 ? -46.001 25.042 3.532 1.00 18.13 ? 391 TYR A O 1 ATOM 3008 C CB . TYR A 1 391 ? -42.976 26.105 4.221 1.00 15.61 ? 391 TYR A CB 1 ATOM 3009 C CG . TYR A 1 391 ? -41.848 26.859 3.561 1.00 15.82 ? 391 TYR A CG 1 ATOM 3010 C CD1 . TYR A 1 391 ? -41.240 27.957 4.200 1.00 16.74 ? 391 TYR A CD1 1 ATOM 3011 C CD2 . TYR A 1 391 ? -41.373 26.479 2.289 1.00 14.80 ? 391 TYR A CD2 1 ATOM 3012 C CE1 . TYR A 1 391 ? -40.174 28.668 3.586 1.00 16.59 ? 391 TYR A CE1 1 ATOM 3013 C CE2 . TYR A 1 391 ? -40.310 27.184 1.661 1.00 16.55 ? 391 TYR A CE2 1 ATOM 3014 C CZ . TYR A 1 391 ? -39.722 28.274 2.319 1.00 16.50 ? 391 TYR A CZ 1 ATOM 3015 O OH . TYR A 1 391 ? -38.707 28.972 1.716 1.00 18.57 ? 391 TYR A OH 1 ATOM 3016 N N . ILE A 1 392 ? -45.727 25.606 5.703 1.00 16.53 ? 392 ILE A N 1 ATOM 3017 C CA . ILE A 1 392 ? -46.726 24.678 6.253 1.00 17.10 ? 392 ILE A CA 1 ATOM 3018 C C . ILE A 1 392 ? -48.148 25.081 5.834 1.00 17.22 ? 392 ILE A C 1 ATOM 3019 O O . ILE A 1 392 ? -48.930 24.231 5.406 1.00 18.03 ? 392 ILE A O 1 ATOM 3020 C CB . ILE A 1 392 ? -46.607 24.588 7.823 1.00 16.44 ? 392 ILE A CB 1 ATOM 3021 C CG1 . ILE A 1 392 ? -45.243 24.003 8.231 1.00 16.76 ? 392 ILE A CG1 1 ATOM 3022 C CG2 . ILE A 1 392 ? -47.769 23.788 8.448 1.00 16.68 ? 392 ILE A CG2 1 ATOM 3023 C CD1 . ILE A 1 392 ? -45.014 22.526 7.869 1.00 15.08 ? 392 ILE A CD1 1 ATOM 3024 N N . LEU A 1 393 ? -48.446 26.379 5.913 1.00 16.95 ? 393 LEU A N 1 ATOM 3025 C CA . LEU A 1 393 ? -49.764 26.913 5.551 1.00 19.48 ? 393 LEU A CA 1 ATOM 3026 C C . LEU A 1 393 ? -50.070 26.909 4.054 1.00 20.31 ? 393 LEU A C 1 ATOM 3027 O O . LEU A 1 393 ? -51.240 26.890 3.665 1.00 21.71 ? 393 LEU A O 1 ATOM 3028 C CB . LEU A 1 393 ? -49.955 28.323 6.123 1.00 18.83 ? 393 LEU A CB 1 ATOM 3029 C CG . LEU A 1 393 ? -50.076 28.456 7.648 1.00 20.96 ? 393 LEU A CG 1 ATOM 3030 C CD1 . LEU A 1 393 ? -50.037 29.923 8.029 1.00 20.21 ? 393 LEU A CD1 1 ATOM 3031 C CD2 . LEU A 1 393 ? -51.346 27.788 8.172 1.00 20.60 ? 393 LEU A CD2 1 ATOM 3032 N N . THR A 1 394 ? -49.022 26.929 3.228 1.00 20.76 ? 394 THR A N 1 ATOM 3033 C CA . THR A 1 394 ? -49.172 26.907 1.768 1.00 22.63 ? 394 THR A CA 1 ATOM 3034 C C . THR A 1 394 ? -48.965 25.508 1.174 1.00 23.60 ? 394 THR A C 1 ATOM 3035 O O . THR A 1 394 ? -49.177 25.303 -0.027 1.00 24.98 ? 394 THR A O 1 ATOM 3036 C CB . THR A 1 394 ? -48.213 27.904 1.058 1.00 23.57 ? 394 THR A CB 1 ATOM 3037 O OG1 . THR A 1 394 ? -46.851 27.595 1.387 1.00 22.88 ? 394 THR A OG1 1 ATOM 3038 C CG2 . THR A 1 394 ? -48.526 29.345 1.458 1.00 23.39 ? 394 THR A CG2 1 ATOM 3039 N N . GLY A 1 395 ? -48.547 24.558 2.015 1.00 23.08 ? 395 GLY A N 1 ATOM 3040 C CA . GLY A 1 395 ? -48.314 23.185 1.575 1.00 23.68 ? 395 GLY A CA 1 ATOM 3041 C C . GLY A 1 395 ? -47.040 22.992 0.768 1.00 24.13 ? 395 GLY A C 1 ATOM 3042 O O . GLY A 1 395 ? -46.941 22.074 -0.051 1.00 24.70 ? 395 GLY A O 1 ATOM 3043 N N . ASN A 1 396 ? -46.075 23.880 0.997 1.00 23.96 ? 396 ASN A N 1 ATOM 3044 C CA . ASN A 1 396 ? -44.782 23.861 0.320 1.00 23.83 ? 396 ASN A CA 1 ATOM 3045 C C . ASN A 1 396 ? -43.791 23.090 1.198 1.00 22.69 ? 396 ASN A C 1 ATOM 3046 O O . ASN A 1 396 ? -43.565 23.461 2.352 1.00 23.74 ? 396 ASN A O 1 ATOM 3047 C CB . ASN A 1 396 ? -44.314 25.310 0.115 1.00 26.18 ? 396 ASN A CB 1 ATOM 3048 C CG . ASN A 1 396 ? -43.180 25.446 -0.892 1.00 29.38 ? 396 ASN A CG 1 ATOM 3049 O OD1 . ASN A 1 396 ? -42.277 24.610 -0.969 1.00 27.72 ? 396 ASN A OD1 1 ATOM 3050 N ND2 . ASN A 1 396 ? -43.221 26.544 -1.642 1.00 33.49 ? 396 ASN A ND2 1 ATOM 3051 N N . THR A 1 397 ? -43.225 22.013 0.654 1.00 20.29 ? 397 THR A N 1 ATOM 3052 C CA . THR A 1 397 ? -42.259 21.192 1.389 1.00 19.44 ? 397 THR A CA 1 ATOM 3053 C C . THR A 1 397 ? -40.821 21.375 0.902 1.00 19.49 ? 397 THR A C 1 ATOM 3054 O O . THR A 1 397 ? -39.915 20.659 1.343 1.00 20.12 ? 397 THR A O 1 ATOM 3055 C CB . THR A 1 397 ? -42.620 19.677 1.360 1.00 19.03 ? 397 THR A CB 1 ATOM 3056 O OG1 . THR A 1 397 ? -42.670 19.219 0.004 1.00 16.12 ? 397 THR A OG1 1 ATOM 3057 C CG2 . THR A 1 397 ? -43.961 19.414 2.062 1.00 16.90 ? 397 THR A CG2 1 ATOM 3058 N N . SER A 1 398 ? -40.614 22.351 0.017 1.00 19.26 ? 398 SER A N 1 ATOM 3059 C CA . SER A 1 398 ? -39.291 22.642 -0.536 1.00 20.08 ? 398 SER A CA 1 ATOM 3060 C C . SER A 1 398 ? -38.553 23.638 0.364 1.00 20.68 ? 398 SER A C 1 ATOM 3061 O O . SER A 1 398 ? -38.327 24.796 -0.005 1.00 21.62 ? 398 SER A O 1 ATOM 3062 C CB . SER A 1 398 ? -39.416 23.177 -1.970 1.00 21.43 ? 398 SER A CB 1 ATOM 3063 O OG . SER A 1 398 ? -40.173 22.295 -2.779 1.00 21.19 ? 398 SER A OG 1 ATOM 3064 N N . TYR A 1 399 ? -38.198 23.168 1.561 1.00 19.66 ? 399 TYR A N 1 ATOM 3065 C CA . TYR A 1 399 ? -37.494 23.979 2.553 1.00 18.60 ? 399 TYR A CA 1 ATOM 3066 C C . TYR A 1 399 ? -36.045 24.179 2.125 1.00 18.07 ? 399 TYR A C 1 ATOM 3067 O O . TYR A 1 399 ? -35.370 23.204 1.783 1.00 15.41 ? 399 TYR A O 1 ATOM 3068 C CB . TYR A 1 399 ? -37.494 23.289 3.927 1.00 17.42 ? 399 TYR A CB 1 ATOM 3069 C CG . TYR A 1 399 ? -38.812 22.687 4.352 1.00 16.72 ? 399 TYR A CG 1 ATOM 3070 C CD1 . TYR A 1 399 ? -39.933 23.501 4.618 1.00 17.73 ? 399 TYR A CD1 1 ATOM 3071 C CD2 . TYR A 1 399 ? -38.954 21.288 4.482 1.00 18.27 ? 399 TYR A CD2 1 ATOM 3072 C CE1 . TYR A 1 399 ? -41.177 22.933 5.002 1.00 18.37 ? 399 TYR A CE1 1 ATOM 3073 C CE2 . TYR A 1 399 ? -40.194 20.706 4.866 1.00 16.45 ? 399 TYR A CE2 1 ATOM 3074 C CZ . TYR A 1 399 ? -41.296 21.542 5.121 1.00 17.31 ? 399 TYR A CZ 1 ATOM 3075 O OH . TYR A 1 399 ? -42.506 21.001 5.481 1.00 18.52 ? 399 TYR A OH 1 ATOM 3076 N N . PRO A 1 400 ? -35.569 25.445 2.056 1.00 18.63 ? 400 PRO A N 1 ATOM 3077 C CA . PRO A 1 400 ? -34.172 25.659 1.659 1.00 18.55 ? 400 PRO A CA 1 ATOM 3078 C C . PRO A 1 400 ? -33.207 25.057 2.681 1.00 17.96 ? 400 PRO A C 1 ATOM 3079 O O . PRO A 1 400 ? -33.555 24.904 3.864 1.00 16.93 ? 400 PRO A O 1 ATOM 3080 C CB . PRO A 1 400 ? -34.054 27.187 1.557 1.00 20.16 ? 400 PRO A CB 1 ATOM 3081 C CG . PRO A 1 400 ? -35.191 27.712 2.324 1.00 21.16 ? 400 PRO A CG 1 ATOM 3082 C CD . PRO A 1 400 ? -36.294 26.726 2.091 1.00 20.27 ? 400 PRO A CD 1 ATOM 3083 N N . VAL A 1 401 ? -32.041 24.647 2.182 1.00 16.34 ? 401 VAL A N 1 ATOM 3084 C CA . VAL A 1 401 ? -30.968 24.016 2.958 1.00 16.77 ? 401 VAL A CA 1 ATOM 3085 C C . VAL A 1 401 ? -30.600 24.776 4.237 1.00 16.45 ? 401 VAL A C 1 ATOM 3086 O O . VAL A 1 401 ? -30.449 24.168 5.300 1.00 16.68 ? 401 VAL A O 1 ATOM 3087 C CB . VAL A 1 401 ? -29.700 23.812 2.063 1.00 17.76 ? 401 VAL A CB 1 ATOM 3088 C CG1 . VAL A 1 401 ? -28.586 23.059 2.815 1.00 18.09 ? 401 VAL A CG1 1 ATOM 3089 C CG2 . VAL A 1 401 ? -30.077 23.037 0.796 1.00 17.35 ? 401 VAL A CG2 1 ATOM 3090 N N . SER A 1 402 ? -30.568 26.104 4.131 1.00 14.96 ? 402 SER A N 1 ATOM 3091 C CA . SER A 1 402 ? -30.212 26.995 5.232 1.00 15.73 ? 402 SER A CA 1 ATOM 3092 C C . SER A 1 402 ? -31.172 27.040 6.414 1.00 14.18 ? 402 SER A C 1 ATOM 3093 O O . SER A 1 402 ? -30.834 27.579 7.461 1.00 13.56 ? 402 SER A O 1 ATOM 3094 C CB . SER A 1 402 ? -29.968 28.403 4.701 1.00 15.13 ? 402 SER A CB 1 ATOM 3095 O OG . SER A 1 402 ? -28.857 28.401 3.824 1.00 20.81 ? 402 SER A OG 1 ATOM 3096 N N . ASP A 1 403 ? -32.364 26.477 6.247 1.00 12.88 ? 403 ASP A N 1 ATOM 3097 C CA . ASP A 1 403 ? -33.340 26.440 7.328 1.00 14.10 ? 403 ASP A CA 1 ATOM 3098 C C . ASP A 1 403 ? -33.066 25.292 8.293 1.00 12.28 ? 403 ASP A C 1 ATOM 3099 O O . ASP A 1 403 ? -33.690 25.213 9.349 1.00 11.92 ? 403 ASP A O 1 ATOM 3100 C CB . ASP A 1 403 ? -34.760 26.350 6.774 1.00 16.40 ? 403 ASP A CB 1 ATOM 3101 C CG . ASP A 1 403 ? -35.233 27.655 6.153 1.00 20.42 ? 403 ASP A CG 1 ATOM 3102 O OD1 . ASP A 1 403 ? -34.712 28.735 6.507 1.00 23.25 ? 403 ASP A OD1 1 ATOM 3103 O OD2 . ASP A 1 403 ? -36.162 27.602 5.325 1.00 24.38 ? 403 ASP A OD2 1 ATOM 3104 N N . ASN A 1 404 ? -32.117 24.423 7.919 1.00 11.75 ? 404 ASN A N 1 ATOM 3105 C CA . ASN A 1 404 ? -31.685 23.256 8.704 1.00 12.10 ? 404 ASN A CA 1 ATOM 3106 C C . ASN A 1 404 ? -32.824 22.428 9.294 1.00 11.42 ? 404 ASN A C 1 ATOM 3107 O O . ASN A 1 404 ? -32.836 22.097 10.488 1.00 10.69 ? 404 ASN A O 1 ATOM 3108 C CB . ASN A 1 404 ? -30.705 23.680 9.810 1.00 10.69 ? 404 ASN A CB 1 ATOM 3109 C CG . ASN A 1 404 ? -29.390 24.183 9.271 1.00 10.65 ? 404 ASN A CG 1 ATOM 3110 O OD1 . ASN A 1 404 ? -29.198 24.289 8.063 1.00 10.77 ? 404 ASN A OD1 1 ATOM 3111 N ND2 . ASN A 1 404 ? -28.472 24.501 10.172 1.00 8.98 ? 404 ASN A ND2 1 ATOM 3112 N N . ILE A 1 405 ? -33.802 22.145 8.441 1.00 12.50 ? 405 ILE A N 1 ATOM 3113 C CA . ILE A 1 405 ? -34.973 21.370 8.818 1.00 13.06 ? 405 ILE A CA 1 ATOM 3114 C C . ILE A 1 405 ? -34.642 19.904 9.079 1.00 13.12 ? 405 ILE A C 1 ATOM 3115 O O . ILE A 1 405 ? -34.059 19.225 8.237 1.00 12.53 ? 405 ILE A O 1 ATOM 3116 C CB . ILE A 1 405 ? -36.102 21.485 7.735 1.00 13.13 ? 405 ILE A CB 1 ATOM 3117 C CG1 . ILE A 1 405 ? -36.636 22.922 7.674 1.00 13.59 ? 405 ILE A CG1 1 ATOM 3118 C CG2 . ILE A 1 405 ? -37.245 20.466 7.986 1.00 12.43 ? 405 ILE A CG2 1 ATOM 3119 C CD1 . ILE A 1 405 ? -37.400 23.388 8.904 1.00 13.42 ? 405 ILE A CD1 1 ATOM 3120 N N . VAL A 1 406 ? -34.953 19.465 10.294 1.00 12.90 ? 406 VAL A N 1 ATOM 3121 C CA . VAL A 1 406 ? -34.777 18.073 10.685 1.00 13.95 ? 406 VAL A CA 1 ATOM 3122 C C . VAL A 1 406 ? -36.222 17.641 10.946 1.00 14.49 ? 406 VAL A C 1 ATOM 3123 O O . VAL A 1 406 ? -36.804 17.950 11.991 1.00 12.62 ? 406 VAL A O 1 ATOM 3124 C CB . VAL A 1 406 ? -33.884 17.914 11.948 1.00 13.24 ? 406 VAL A CB 1 ATOM 3125 C CG1 . VAL A 1 406 ? -33.708 16.439 12.286 1.00 12.42 ? 406 VAL A CG1 1 ATOM 3126 C CG2 . VAL A 1 406 ? -32.512 18.535 11.715 1.00 10.51 ? 406 VAL A CG2 1 ATOM 3127 N N . GLN A 1 407 ? -36.819 17.008 9.938 1.00 14.80 ? 407 GLN A N 1 ATOM 3128 C CA . GLN A 1 407 ? -38.203 16.558 10.018 1.00 16.43 ? 407 GLN A CA 1 ATOM 3129 C C . GLN A 1 407 ? -38.367 15.298 10.861 1.00 15.77 ? 407 GLN A C 1 ATOM 3130 O O . GLN A 1 407 ? -37.744 14.271 10.591 1.00 15.99 ? 407 GLN A O 1 ATOM 3131 C CB . GLN A 1 407 ? -38.793 16.359 8.619 1.00 16.70 ? 407 GLN A CB 1 ATOM 3132 C CG . GLN A 1 407 ? -40.318 16.306 8.607 1.00 18.43 ? 407 GLN A CG 1 ATOM 3133 C CD . GLN A 1 407 ? -40.891 16.260 7.210 1.00 21.05 ? 407 GLN A CD 1 ATOM 3134 O OE1 . GLN A 1 407 ? -40.562 17.091 6.365 1.00 23.16 ? 407 GLN A OE1 1 ATOM 3135 N NE2 . GLN A 1 407 ? -41.765 15.290 6.960 1.00 20.91 ? 407 GLN A NE2 1 ATOM 3136 N N . VAL A 1 408 ? -39.184 15.418 11.906 1.00 15.72 ? 408 VAL A N 1 ATOM 3137 C CA . VAL A 1 408 ? -39.463 14.319 12.836 1.00 16.91 ? 408 VAL A CA 1 ATOM 3138 C C . VAL A 1 408 ? -40.949 13.962 12.733 1.00 16.64 ? 408 VAL A C 1 ATOM 3139 O O . VAL A 1 408 ? -41.801 14.632 13.325 1.00 16.31 ? 408 VAL A O 1 ATOM 3140 C CB . VAL A 1 408 ? -39.122 14.709 14.307 1.00 16.26 ? 408 VAL A CB 1 ATOM 3141 C CG1 . VAL A 1 408 ? -39.104 13.474 15.172 1.00 15.85 ? 408 VAL A CG1 1 ATOM 3142 C CG2 . VAL A 1 408 ? -37.777 15.424 14.394 1.00 15.44 ? 408 VAL A CG2 1 ATOM 3143 N N . ASP A 1 409 ? -41.240 12.884 12.007 1.00 17.86 ? 409 ASP A N 1 ATOM 3144 C CA . ASP A 1 409 ? -42.615 12.428 11.784 1.00 19.30 ? 409 ASP A CA 1 ATOM 3145 C C . ASP A 1 409 ? -43.227 11.561 12.876 1.00 18.50 ? 409 ASP A C 1 ATOM 3146 O O . ASP A 1 409 ? -44.451 11.452 12.950 1.00 18.38 ? 409 ASP A O 1 ATOM 3147 C CB . ASP A 1 409 ? -42.731 11.723 10.425 1.00 21.24 ? 409 ASP A CB 1 ATOM 3148 C CG . ASP A 1 409 ? -42.530 12.673 9.248 1.00 23.90 ? 409 ASP A CG 1 ATOM 3149 O OD1 . ASP A 1 409 ? -43.060 13.804 9.285 1.00 24.25 ? 409 ASP A OD1 1 ATOM 3150 O OD2 . ASP A 1 409 ? -41.841 12.285 8.282 1.00 26.80 ? 409 ASP A OD2 1 ATOM 3151 N N . ALA A 1 410 ? -42.380 10.973 13.729 1.00 18.95 ? 410 ALA A N 1 ATOM 3152 C CA . ALA A 1 410 ? -42.810 10.104 14.842 1.00 18.52 ? 410 ALA A CA 1 ATOM 3153 C C . ALA A 1 410 ? -43.871 10.764 15.726 1.00 17.69 ? 410 ALA A C 1 ATOM 3154 O O . ALA A 1 410 ? -43.740 11.930 16.093 1.00 15.49 ? 410 ALA A O 1 ATOM 3155 C CB . ALA A 1 410 ? -41.606 9.696 15.683 1.00 19.26 ? 410 ALA A CB 1 ATOM 3156 N N . VAL A 1 411 ? -44.948 10.030 16.000 1.00 18.23 ? 411 VAL A N 1 ATOM 3157 C CA . VAL A 1 411 ? -46.061 10.538 16.806 1.00 19.52 ? 411 VAL A CA 1 ATOM 3158 C C . VAL A 1 411 ? -45.977 10.101 18.263 1.00 19.58 ? 411 VAL A C 1 ATOM 3159 O O . VAL A 1 411 ? -46.125 8.914 18.567 1.00 19.16 ? 411 VAL A O 1 ATOM 3160 C CB . VAL A 1 411 ? -47.446 10.110 16.204 1.00 20.04 ? 411 VAL A CB 1 ATOM 3161 C CG1 . VAL A 1 411 ? -48.600 10.720 17.000 1.00 18.89 ? 411 VAL A CG1 1 ATOM 3162 C CG2 . VAL A 1 411 ? -47.549 10.543 14.748 1.00 19.18 ? 411 VAL A CG2 1 ATOM 3163 N N . ASP A 1 412 ? -45.776 11.083 19.151 1.00 20.05 ? 412 ASP A N 1 ATOM 3164 C CA . ASP A 1 412 ? -45.681 10.893 20.610 1.00 21.35 ? 412 ASP A CA 1 ATOM 3165 C C . ASP A 1 412 ? -44.684 9.797 21.029 1.00 21.40 ? 412 ASP A C 1 ATOM 3166 O O . ASP A 1 412 ? -44.939 8.997 21.943 1.00 21.94 ? 412 ASP A O 1 ATOM 3167 C CB . ASP A 1 412 ? -47.087 10.678 21.216 1.00 22.51 ? 412 ASP A CB 1 ATOM 3168 C CG . ASP A 1 412 ? -47.150 10.983 22.715 1.00 24.03 ? 412 ASP A CG 1 ATOM 3169 O OD1 . ASP A 1 412 ? -46.378 11.836 23.204 1.00 24.54 ? 412 ASP A OD1 1 ATOM 3170 O OD2 . ASP A 1 412 ? -47.985 10.362 23.405 1.00 25.40 ? 412 ASP A OD2 1 ATOM 3171 N N . GLN A 1 413 ? -43.564 9.752 20.310 1.00 19.84 ? 413 GLN A N 1 ATOM 3172 C CA . GLN A 1 413 ? -42.506 8.781 20.569 1.00 20.89 ? 413 GLN A CA 1 ATOM 3173 C C . GLN A 1 413 ? -41.232 9.488 20.991 1.00 20.28 ? 413 GLN A C 1 ATOM 3174 O O . GLN A 1 413 ? -41.021 10.666 20.666 1.00 18.93 ? 413 GLN A O 1 ATOM 3175 C CB . GLN A 1 413 ? -42.216 7.929 19.325 1.00 23.73 ? 413 GLN A CB 1 ATOM 3176 C CG . GLN A 1 413 ? -43.331 6.968 18.915 1.00 29.48 ? 413 GLN A CG 1 ATOM 3177 C CD . GLN A 1 413 ? -42.929 6.038 17.779 1.00 33.18 ? 413 GLN A CD 1 ATOM 3178 O OE1 . GLN A 1 413 ? -42.272 6.448 16.819 1.00 34.80 ? 413 GLN A OE1 1 ATOM 3179 N NE2 . GLN A 1 413 ? -43.329 4.775 17.885 1.00 34.88 ? 413 GLN A NE2 1 ATOM 3180 N N . TRP A 1 414 ? -40.392 8.765 21.729 1.00 19.20 ? 414 TRP A N 1 ATOM 3181 C CA . TRP A 1 414 ? -39.107 9.285 22.185 1.00 18.84 ? 414 TRP A CA 1 ATOM 3182 C C . TRP A 1 414 ? -38.109 9.240 21.035 1.00 18.01 ? 414 TRP A C 1 ATOM 3183 O O . TRP A 1 414 ? -37.954 8.211 20.372 1.00 18.54 ? 414 TRP A O 1 ATOM 3184 C CB . TRP A 1 414 ? -38.577 8.481 23.377 1.00 18.06 ? 414 TRP A CB 1 ATOM 3185 C CG . TRP A 1 414 ? -39.354 8.692 24.653 1.00 19.89 ? 414 TRP A CG 1 ATOM 3186 C CD1 . TRP A 1 414 ? -40.282 7.845 25.195 1.00 19.60 ? 414 TRP A CD1 1 ATOM 3187 C CD2 . TRP A 1 414 ? -39.270 9.817 25.542 1.00 19.33 ? 414 TRP A CD2 1 ATOM 3188 N NE1 . TRP A 1 414 ? -40.784 8.370 26.363 1.00 22.33 ? 414 TRP A NE1 1 ATOM 3189 C CE2 . TRP A 1 414 ? -40.186 9.579 26.605 1.00 20.17 ? 414 TRP A CE2 1 ATOM 3190 C CE3 . TRP A 1 414 ? -38.508 11.007 25.552 1.00 19.83 ? 414 TRP A CE3 1 ATOM 3191 C CZ2 . TRP A 1 414 ? -40.369 10.492 27.673 1.00 20.72 ? 414 TRP A CZ2 1 ATOM 3192 C CZ3 . TRP A 1 414 ? -38.691 11.926 26.619 1.00 19.55 ? 414 TRP A CZ3 1 ATOM 3193 C CH2 . TRP A 1 414 ? -39.618 11.655 27.663 1.00 20.22 ? 414 TRP A CH2 1 ATOM 3194 N N . THR A 1 415 ? -37.534 10.400 20.728 1.00 17.19 ? 415 THR A N 1 ATOM 3195 C CA . THR A 1 415 ? -36.545 10.516 19.659 1.00 15.13 ? 415 THR A CA 1 ATOM 3196 C C . THR A 1 415 ? -35.207 10.840 20.298 1.00 14.38 ? 415 THR A C 1 ATOM 3197 O O . THR A 1 415 ? -35.130 11.686 21.185 1.00 13.11 ? 415 THR A O 1 ATOM 3198 C CB . THR A 1 415 ? -36.940 11.582 18.625 1.00 14.25 ? 415 THR A CB 1 ATOM 3199 O OG1 . THR A 1 415 ? -37.151 12.839 19.278 1.00 13.65 ? 415 THR A OG1 1 ATOM 3200 C CG2 . THR A 1 415 ? -38.207 11.161 17.888 1.00 15.38 ? 415 THR A CG2 1 ATOM 3201 N N . TYR A 1 416 ? -34.168 10.142 19.847 1.00 13.81 ? 416 TYR A N 1 ATOM 3202 C CA . TYR A 1 416 ? -32.816 10.267 20.386 1.00 14.03 ? 416 TYR A CA 1 ATOM 3203 C C . TYR A 1 416 ? -31.902 11.084 19.489 1.00 13.60 ? 416 TYR A C 1 ATOM 3204 O O . TYR A 1 416 ? -31.914 10.922 18.268 1.00 13.43 ? 416 TYR A O 1 ATOM 3205 C CB . TYR A 1 416 ? -32.238 8.870 20.625 1.00 16.05 ? 416 TYR A CB 1 ATOM 3206 C CG . TYR A 1 416 ? -33.067 8.011 21.561 1.00 18.88 ? 416 TYR A CG 1 ATOM 3207 C CD1 . TYR A 1 416 ? -34.210 7.312 21.098 1.00 20.62 ? 416 TYR A CD1 1 ATOM 3208 C CD2 . TYR A 1 416 ? -32.740 7.915 22.924 1.00 20.74 ? 416 TYR A CD2 1 ATOM 3209 C CE1 . TYR A 1 416 ? -35.013 6.539 21.990 1.00 21.98 ? 416 TYR A CE1 1 ATOM 3210 C CE2 . TYR A 1 416 ? -33.532 7.144 23.826 1.00 20.95 ? 416 TYR A CE2 1 ATOM 3211 C CZ . TYR A 1 416 ? -34.660 6.466 23.349 1.00 21.71 ? 416 TYR A CZ 1 ATOM 3212 O OH . TYR A 1 416 ? -35.421 5.737 24.226 1.00 24.26 ? 416 TYR A OH 1 ATOM 3213 N N . TRP A 1 417 ? -31.161 12.014 20.095 1.00 11.25 ? 417 TRP A N 1 ATOM 3214 C CA . TRP A 1 417 ? -30.272 12.911 19.348 1.00 11.57 ? 417 TRP A CA 1 ATOM 3215 C C . TRP A 1 417 ? -28.866 13.016 19.901 1.00 9.93 ? 417 TRP A C 1 ATOM 3216 O O . TRP A 1 417 ? -28.660 13.418 21.045 1.00 11.54 ? 417 TRP A O 1 ATOM 3217 C CB . TRP A 1 417 ? -30.883 14.324 19.224 1.00 10.19 ? 417 TRP A CB 1 ATOM 3218 C CG . TRP A 1 417 ? -32.280 14.315 18.682 1.00 11.18 ? 417 TRP A CG 1 ATOM 3219 C CD1 . TRP A 1 417 ? -33.434 14.279 19.417 1.00 12.35 ? 417 TRP A CD1 1 ATOM 3220 C CD2 . TRP A 1 417 ? -32.673 14.157 17.312 1.00 11.72 ? 417 TRP A CD2 1 ATOM 3221 N NE1 . TRP A 1 417 ? -34.516 14.080 18.597 1.00 11.43 ? 417 TRP A NE1 1 ATOM 3222 C CE2 . TRP A 1 417 ? -34.085 14.002 17.300 1.00 12.60 ? 417 TRP A CE2 1 ATOM 3223 C CE3 . TRP A 1 417 ? -31.970 14.121 16.087 1.00 12.57 ? 417 TRP A CE3 1 ATOM 3224 C CZ2 . TRP A 1 417 ? -34.818 13.808 16.105 1.00 11.84 ? 417 TRP A CZ2 1 ATOM 3225 C CZ3 . TRP A 1 417 ? -32.704 13.925 14.886 1.00 13.41 ? 417 TRP A CZ3 1 ATOM 3226 C CH2 . TRP A 1 417 ? -34.115 13.770 14.915 1.00 10.58 ? 417 TRP A CH2 1 ATOM 3227 N N . LEU A 1 418 ? -27.902 12.612 19.082 1.00 9.71 ? 418 LEU A N 1 ATOM 3228 C CA . LEU A 1 418 ? -26.500 12.679 19.454 1.00 8.60 ? 418 LEU A CA 1 ATOM 3229 C C . LEU A 1 418 ? -25.897 13.934 18.845 1.00 8.38 ? 418 LEU A C 1 ATOM 3230 O O . LEU A 1 418 ? -25.855 14.086 17.627 1.00 8.18 ? 418 LEU A O 1 ATOM 3231 C CB . LEU A 1 418 ? -25.745 11.431 18.982 1.00 8.06 ? 418 LEU A CB 1 ATOM 3232 C CG . LEU A 1 418 ? -24.240 11.363 19.275 1.00 6.85 ? 418 LEU A CG 1 ATOM 3233 C CD1 . LEU A 1 418 ? -23.984 11.239 20.766 1.00 4.48 ? 418 LEU A CD1 1 ATOM 3234 C CD2 . LEU A 1 418 ? -23.651 10.192 18.539 1.00 9.64 ? 418 LEU A CD2 1 ATOM 3235 N N . ILE A 1 419 ? -25.468 14.849 19.709 1.00 9.80 ? 419 ILE A N 1 ATOM 3236 C CA . ILE A 1 419 ? -24.853 16.096 19.263 1.00 9.15 ? 419 ILE A CA 1 ATOM 3237 C C . ILE A 1 419 ? -23.359 15.955 19.501 1.00 9.97 ? 419 ILE A C 1 ATOM 3238 O O . ILE A 1 419 ? -22.935 15.704 20.625 1.00 9.80 ? 419 ILE A O 1 ATOM 3239 C CB . ILE A 1 419 ? -25.406 17.335 20.022 1.00 9.92 ? 419 ILE A CB 1 ATOM 3240 C CG1 . ILE A 1 419 ? -26.932 17.356 19.974 1.00 10.04 ? 419 ILE A CG1 1 ATOM 3241 C CG2 . ILE A 1 419 ? -24.915 18.621 19.374 1.00 8.83 ? 419 ILE A CG2 1 ATOM 3242 C CD1 . ILE A 1 419 ? -27.575 16.766 21.187 1.00 8.88 ? 419 ILE A CD1 1 ATOM 3243 N N . GLU A 1 420 ? -22.579 16.078 18.427 1.00 10.46 ? 420 GLU A N 1 ATOM 3244 C CA . GLU A 1 420 ? -21.120 15.951 18.482 1.00 11.82 ? 420 GLU A CA 1 ATOM 3245 C C . GLU A 1 420 ? -20.482 17.325 18.380 1.00 11.09 ? 420 GLU A C 1 ATOM 3246 O O . GLU A 1 420 ? -20.797 18.084 17.466 1.00 11.61 ? 420 GLU A O 1 ATOM 3247 C CB . GLU A 1 420 ? -20.629 15.051 17.343 1.00 11.81 ? 420 GLU A CB 1 ATOM 3248 C CG . GLU A 1 420 ? -21.290 13.677 17.327 1.00 13.02 ? 420 GLU A CG 1 ATOM 3249 C CD . GLU A 1 420 ? -20.819 12.807 16.190 1.00 13.33 ? 420 GLU A CD 1 ATOM 3250 O OE1 . GLU A 1 420 ? -20.831 13.276 15.036 1.00 17.99 ? 420 GLU A OE1 1 ATOM 3251 O OE2 . GLU A 1 420 ? -20.455 11.644 16.449 1.00 15.45 ? 420 GLU A OE2 1 ATOM 3252 N N . ASN A 1 421 ? -19.556 17.620 19.292 1.00 11.98 ? 421 ASN A N 1 ATOM 3253 C CA . ASN A 1 421 ? -18.897 18.927 19.338 1.00 11.90 ? 421 ASN A CA 1 ATOM 3254 C C . ASN A 1 421 ? -17.556 19.039 18.624 1.00 11.73 ? 421 ASN A C 1 ATOM 3255 O O . ASN A 1 421 ? -16.504 19.032 19.277 1.00 12.93 ? 421 ASN A O 1 ATOM 3256 C CB . ASN A 1 421 ? -18.728 19.380 20.793 1.00 9.97 ? 421 ASN A CB 1 ATOM 3257 C CG . ASN A 1 421 ? -18.569 20.891 20.932 1.00 10.01 ? 421 ASN A CG 1 ATOM 3258 O OD1 . ASN A 1 421 ? -18.459 21.622 19.944 1.00 9.64 ? 421 ASN A OD1 1 ATOM 3259 N ND2 . ASN A 1 421 ? -18.567 21.362 22.166 1.00 9.31 ? 421 ASN A ND2 1 ATOM 3260 N N . ASP A 1 422 ? -17.606 19.168 17.293 1.00 12.23 ? 422 ASP A N 1 ATOM 3261 C CA . ASP A 1 422 ? -16.422 19.318 16.416 1.00 14.78 ? 422 ASP A CA 1 ATOM 3262 C C . ASP A 1 422 ? -15.225 18.473 16.902 1.00 16.30 ? 422 ASP A C 1 ATOM 3263 O O . ASP A 1 422 ? -14.151 19.019 17.173 1.00 17.67 ? 422 ASP A O 1 ATOM 3264 C CB . ASP A 1 422 ? -16.055 20.819 16.345 1.00 12.24 ? 422 ASP A CB 1 ATOM 3265 C CG . ASP A 1 422 ? -15.408 21.222 15.028 1.00 12.74 ? 422 ASP A CG 1 ATOM 3266 O OD1 . ASP A 1 422 ? -15.233 20.367 14.130 1.00 12.11 ? 422 ASP A OD1 1 ATOM 3267 O OD2 . ASP A 1 422 ? -15.098 22.426 14.882 1.00 13.09 ? 422 ASP A OD2 1 ATOM 3268 N N . PRO A 1 423 ? -15.403 17.129 17.016 1.00 20.21 ? 423 PRO A N 1 ATOM 3269 C CA . PRO A 1 423 ? -14.350 16.215 17.490 1.00 21.50 ? 423 PRO A CA 1 ATOM 3270 C C . PRO A 1 423 ? -13.050 16.213 16.700 1.00 22.83 ? 423 PRO A C 1 ATOM 3271 O O . PRO A 1 423 ? -11.969 16.095 17.281 1.00 24.04 ? 423 PRO A O 1 ATOM 3272 C CB . PRO A 1 423 ? -15.020 14.837 17.413 1.00 21.95 ? 423 PRO A CB 1 ATOM 3273 C CG . PRO A 1 423 ? -16.477 15.127 17.333 1.00 22.94 ? 423 PRO A CG 1 ATOM 3274 C CD . PRO A 1 423 ? -16.529 16.337 16.482 1.00 20.61 ? 423 PRO A CD 1 ATOM 3275 N N . GLU A 1 424 ? -13.173 16.358 15.381 1.00 23.56 ? 424 GLU A N 1 ATOM 3276 C CA . GLU A 1 424 ? -12.027 16.357 14.475 1.00 25.06 ? 424 GLU A CA 1 ATOM 3277 C C . GLU A 1 424 ? -11.568 17.771 14.121 1.00 23.88 ? 424 GLU A C 1 ATOM 3278 O O . GLU A 1 424 ? -10.657 17.948 13.304 1.00 23.15 ? 424 GLU A O 1 ATOM 3279 C CB . GLU A 1 424 ? -12.361 15.579 13.187 1.00 28.71 ? 424 GLU A CB 1 ATOM 3280 C CG . GLU A 1 424 ? -13.093 14.226 13.362 1.00 34.75 ? 424 GLU A CG 1 ATOM 3281 C CD . GLU A 1 424 ? -12.345 13.200 14.219 1.00 37.85 ? 424 GLU A CD 1 ATOM 3282 O OE1 . GLU A 1 424 ? -11.097 13.123 14.151 1.00 40.64 ? 424 GLU A OE1 1 ATOM 3283 O OE2 . GLU A 1 424 ? -13.024 12.453 14.957 1.00 39.88 ? 424 GLU A OE2 1 ATOM 3284 N N . GLY A 1 425 ? -12.189 18.768 14.752 1.00 20.80 ? 425 GLY A N 1 ATOM 3285 C CA . GLY A 1 425 ? -11.851 20.159 14.494 1.00 19.22 ? 425 GLY A CA 1 ATOM 3286 C C . GLY A 1 425 ? -10.608 20.664 15.209 1.00 18.86 ? 425 GLY A C 1 ATOM 3287 O O . GLY A 1 425 ? -10.141 20.002 16.142 1.00 17.27 ? 425 GLY A O 1 ATOM 3288 N N . PRO A 1 426 ? -10.032 21.818 14.785 1.00 18.80 ? 426 PRO A N 1 ATOM 3289 C CA . PRO A 1 426 ? -8.831 22.414 15.391 1.00 19.60 ? 426 PRO A CA 1 ATOM 3290 C C . PRO A 1 426 ? -8.963 22.726 16.881 1.00 19.10 ? 426 PRO A C 1 ATOM 3291 O O . PRO A 1 426 ? -8.042 22.479 17.661 1.00 19.08 ? 426 PRO A O 1 ATOM 3292 C CB . PRO A 1 426 ? -8.614 23.677 14.556 1.00 20.10 ? 426 PRO A CB 1 ATOM 3293 C CG . PRO A 1 426 ? -9.961 23.968 13.963 1.00 19.20 ? 426 PRO A CG 1 ATOM 3294 C CD . PRO A 1 426 ? -10.436 22.599 13.602 1.00 18.47 ? 426 PRO A CD 1 ATOM 3295 N N . PHE A 1 427 ? -10.103 23.300 17.252 1.00 19.94 ? 427 PHE A N 1 ATOM 3296 C CA . PHE A 1 427 ? -10.411 23.612 18.638 1.00 21.54 ? 427 PHE A CA 1 ATOM 3297 C C . PHE A 1 427 ? -11.914 23.545 18.848 1.00 20.97 ? 427 PHE A C 1 ATOM 3298 O O . PHE A 1 427 ? -12.691 23.768 17.916 1.00 20.47 ? 427 PHE A O 1 ATOM 3299 C CB . PHE A 1 427 ? -9.781 24.945 19.125 1.00 26.45 ? 427 PHE A CB 1 ATOM 3300 C CG . PHE A 1 427 ? -10.417 26.202 18.579 1.00 30.98 ? 427 PHE A CG 1 ATOM 3301 C CD1 . PHE A 1 427 ? -10.127 26.653 17.275 1.00 33.74 ? 427 PHE A CD1 1 ATOM 3302 C CD2 . PHE A 1 427 ? -11.253 26.988 19.407 1.00 33.49 ? 427 PHE A CD2 1 ATOM 3303 C CE1 . PHE A 1 427 ? -10.661 27.886 16.790 1.00 35.99 ? 427 PHE A CE1 1 ATOM 3304 C CE2 . PHE A 1 427 ? -11.796 28.219 18.947 1.00 36.52 ? 427 PHE A CE2 1 ATOM 3305 C CZ . PHE A 1 427 ? -11.498 28.672 17.634 1.00 36.63 ? 427 PHE A CZ 1 ATOM 3306 N N . SER A 1 428 ? -12.312 23.193 20.064 1.00 18.70 ? 428 SER A N 1 ATOM 3307 C CA . SER A 1 428 ? -13.719 23.085 20.393 1.00 17.03 ? 428 SER A CA 1 ATOM 3308 C C . SER A 1 428 ? -14.040 23.811 21.684 1.00 17.27 ? 428 SER A C 1 ATOM 3309 O O . SER A 1 428 ? -13.250 23.820 22.634 1.00 16.10 ? 428 SER A O 1 ATOM 3310 C CB . SER A 1 428 ? -14.126 21.623 20.473 1.00 17.58 ? 428 SER A CB 1 ATOM 3311 O OG . SER A 1 428 ? -15.528 21.488 20.610 1.00 15.27 ? 428 SER A OG 1 ATOM 3312 N N . LEU A 1 429 ? -15.214 24.435 21.685 1.00 16.25 ? 429 LEU A N 1 ATOM 3313 C CA . LEU A 1 429 ? -15.702 25.222 22.805 1.00 15.70 ? 429 LEU A CA 1 ATOM 3314 C C . LEU A 1 429 ? -16.982 24.610 23.348 1.00 13.35 ? 429 LEU A C 1 ATOM 3315 O O . LEU A 1 429 ? -17.699 23.936 22.606 1.00 13.44 ? 429 LEU A O 1 ATOM 3316 C CB . LEU A 1 429 ? -16.021 26.652 22.324 1.00 16.09 ? 429 LEU A CB 1 ATOM 3317 C CG . LEU A 1 429 ? -14.960 27.525 21.656 1.00 19.90 ? 429 LEU A CG 1 ATOM 3318 C CD1 . LEU A 1 429 ? -15.618 28.798 21.149 1.00 20.83 ? 429 LEU A CD1 1 ATOM 3319 C CD2 . LEU A 1 429 ? -13.834 27.848 22.631 1.00 22.26 ? 429 LEU A CD2 1 ATOM 3320 N N . PRO A 1 430 ? -17.279 24.806 24.656 1.00 12.63 ? 430 PRO A N 1 ATOM 3321 C CA . PRO A 1 430 ? -18.513 24.258 25.234 1.00 11.10 ? 430 PRO A CA 1 ATOM 3322 C C . PRO A 1 430 ? -19.707 25.039 24.656 1.00 11.22 ? 430 PRO A C 1 ATOM 3323 O O . PRO A 1 430 ? -19.561 26.216 24.303 1.00 10.43 ? 430 PRO A O 1 ATOM 3324 C CB . PRO A 1 430 ? -18.349 24.555 26.720 1.00 10.49 ? 430 PRO A CB 1 ATOM 3325 C CG . PRO A 1 430 ? -16.882 24.589 26.912 1.00 13.36 ? 430 PRO A CG 1 ATOM 3326 C CD . PRO A 1 430 ? -16.433 25.365 25.727 1.00 12.20 ? 430 PRO A CD 1 ATOM 3327 N N . HIS A 1 431 ? -20.844 24.366 24.481 1.00 9.49 ? 431 HIS A N 1 ATOM 3328 C CA . HIS A 1 431 ? -22.041 25.005 23.929 1.00 10.13 ? 431 HIS A CA 1 ATOM 3329 C C . HIS A 1 431 ? -23.307 24.729 24.735 1.00 9.65 ? 431 HIS A C 1 ATOM 3330 O O . HIS A 1 431 ? -23.639 23.570 24.980 1.00 9.72 ? 431 HIS A O 1 ATOM 3331 C CB . HIS A 1 431 ? -22.316 24.552 22.482 1.00 9.62 ? 431 HIS A CB 1 ATOM 3332 C CG . HIS A 1 431 ? -21.254 24.933 21.505 1.00 11.04 ? 431 HIS A CG 1 ATOM 3333 N ND1 . HIS A 1 431 ? -21.045 26.234 21.095 1.00 11.75 ? 431 HIS A ND1 1 ATOM 3334 C CD2 . HIS A 1 431 ? -20.305 24.186 20.894 1.00 11.81 ? 431 HIS A CD2 1 ATOM 3335 C CE1 . HIS A 1 431 ? -20.002 26.268 20.284 1.00 11.76 ? 431 HIS A CE1 1 ATOM 3336 N NE2 . HIS A 1 431 ? -19.535 25.041 20.146 1.00 14.79 ? 431 HIS A NE2 1 ATOM 3337 N N . PRO A 1 432 ? -24.002 25.790 25.202 1.00 9.24 ? 432 PRO A N 1 ATOM 3338 C CA . PRO A 1 432 ? -25.242 25.621 25.968 1.00 8.97 ? 432 PRO A CA 1 ATOM 3339 C C . PRO A 1 432 ? -26.386 25.351 24.981 1.00 9.93 ? 432 PRO A C 1 ATOM 3340 O O . PRO A 1 432 ? -26.942 26.272 24.375 1.00 11.21 ? 432 PRO A O 1 ATOM 3341 C CB . PRO A 1 432 ? -25.391 26.965 26.687 1.00 8.56 ? 432 PRO A CB 1 ATOM 3342 C CG . PRO A 1 432 ? -24.756 27.933 25.747 1.00 8.33 ? 432 PRO A CG 1 ATOM 3343 C CD . PRO A 1 432 ? -23.528 27.186 25.290 1.00 8.02 ? 432 PRO A CD 1 ATOM 3344 N N . MET A 1 433 ? -26.680 24.073 24.777 1.00 9.38 ? 433 MET A N 1 ATOM 3345 C CA . MET A 1 433 ? -27.727 23.665 23.845 1.00 9.28 ? 433 MET A CA 1 ATOM 3346 C C . MET A 1 433 ? -29.117 23.809 24.431 1.00 8.13 ? 433 MET A C 1 ATOM 3347 O O . MET A 1 433 ? -29.406 23.286 25.508 1.00 9.36 ? 433 MET A O 1 ATOM 3348 C CB . MET A 1 433 ? -27.485 22.237 23.352 1.00 7.50 ? 433 MET A CB 1 ATOM 3349 C CG . MET A 1 433 ? -26.158 22.046 22.622 1.00 10.20 ? 433 MET A CG 1 ATOM 3350 S SD . MET A 1 433 ? -25.837 23.217 21.267 1.00 12.02 ? 433 MET A SD 1 ATOM 3351 C CE . MET A 1 433 ? -27.033 22.668 20.034 1.00 8.75 ? 433 MET A CE 1 ATOM 3352 N N . HIS A 1 434 ? -29.960 24.550 23.716 1.00 7.88 ? 434 HIS A N 1 ATOM 3353 C CA . HIS A 1 434 ? -31.327 24.814 24.133 1.00 6.86 ? 434 HIS A CA 1 ATOM 3354 C C . HIS A 1 434 ? -32.343 24.334 23.099 1.00 8.40 ? 434 HIS A C 1 ATOM 3355 O O . HIS A 1 434 ? -32.146 24.524 21.902 1.00 7.95 ? 434 HIS A O 1 ATOM 3356 C CB . HIS A 1 434 ? -31.495 26.320 24.404 1.00 8.13 ? 434 HIS A CB 1 ATOM 3357 C CG . HIS A 1 434 ? -32.914 26.741 24.622 1.00 8.66 ? 434 HIS A CG 1 ATOM 3358 N ND1 . HIS A 1 434 ? -33.711 26.196 25.606 1.00 8.45 ? 434 HIS A ND1 1 ATOM 3359 C CD2 . HIS A 1 434 ? -33.695 27.611 23.942 1.00 8.04 ? 434 HIS A CD2 1 ATOM 3360 C CE1 . HIS A 1 434 ? -34.924 26.711 25.517 1.00 8.31 ? 434 HIS A CE1 1 ATOM 3361 N NE2 . HIS A 1 434 ? -34.941 27.574 24.517 1.00 11.76 ? 434 HIS A NE2 1 ATOM 3362 N N . LEU A 1 435 ? -33.455 23.780 23.583 1.00 7.49 ? 435 LEU A N 1 ATOM 3363 C CA . LEU A 1 435 ? -34.525 23.285 22.720 1.00 8.30 ? 435 LEU A CA 1 ATOM 3364 C C . LEU A 1 435 ? -35.835 24.006 22.985 1.00 7.37 ? 435 LEU A C 1 ATOM 3365 O O . LEU A 1 435 ? -36.281 24.101 24.126 1.00 8.58 ? 435 LEU A O 1 ATOM 3366 C CB . LEU A 1 435 ? -34.735 21.777 22.920 1.00 7.65 ? 435 LEU A CB 1 ATOM 3367 C CG . LEU A 1 435 ? -35.880 21.016 22.233 1.00 9.24 ? 435 LEU A CG 1 ATOM 3368 C CD1 . LEU A 1 435 ? -35.723 21.027 20.722 1.00 9.85 ? 435 LEU A CD1 1 ATOM 3369 C CD2 . LEU A 1 435 ? -35.920 19.596 22.743 1.00 9.61 ? 435 LEU A CD2 1 ATOM 3370 N N . HIS A 1 436 ? -36.466 24.462 21.906 1.00 9.01 ? 436 HIS A N 1 ATOM 3371 C CA . HIS A 1 436 ? -37.752 25.144 21.986 1.00 10.58 ? 436 HIS A CA 1 ATOM 3372 C C . HIS A 1 436 ? -38.857 24.094 22.030 1.00 10.64 ? 436 HIS A C 1 ATOM 3373 O O . HIS A 1 436 ? -38.699 22.983 21.500 1.00 10.12 ? 436 HIS A O 1 ATOM 3374 C CB . HIS A 1 436 ? -37.991 26.017 20.745 1.00 10.69 ? 436 HIS A CB 1 ATOM 3375 C CG . HIS A 1 436 ? -37.171 27.271 20.682 1.00 11.68 ? 436 HIS A CG 1 ATOM 3376 N ND1 . HIS A 1 436 ? -37.627 28.409 20.053 1.00 12.63 ? 436 HIS A ND1 1 ATOM 3377 C CD2 . HIS A 1 436 ? -35.914 27.556 21.103 1.00 10.24 ? 436 HIS A CD2 1 ATOM 3378 C CE1 . HIS A 1 436 ? -36.686 29.336 20.082 1.00 10.99 ? 436 HIS A CE1 1 ATOM 3379 N NE2 . HIS A 1 436 ? -35.637 28.845 20.716 1.00 12.57 ? 436 HIS A NE2 1 ATOM 3380 N N . GLY A 1 437 ? -39.958 24.452 22.686 1.00 11.02 ? 437 GLY A N 1 ATOM 3381 C CA . GLY A 1 437 ? -41.126 23.595 22.766 1.00 12.10 ? 437 GLY A CA 1 ATOM 3382 C C . GLY A 1 437 ? -41.178 22.349 23.612 1.00 13.92 ? 437 GLY A C 1 ATOM 3383 O O . GLY A 1 437 ? -42.249 21.740 23.722 1.00 13.16 ? 437 GLY A O 1 ATOM 3384 N N . HIS A 1 438 ? -40.028 21.914 24.122 1.00 12.74 ? 438 HIS A N 1 ATOM 3385 C CA . HIS A 1 438 ? -39.949 20.715 24.957 1.00 11.44 ? 438 HIS A CA 1 ATOM 3386 C C . HIS A 1 438 ? -38.847 20.840 25.981 1.00 11.08 ? 438 HIS A C 1 ATOM 3387 O O . HIS A 1 438 ? -37.963 21.697 25.889 1.00 10.27 ? 438 HIS A O 1 ATOM 3388 C CB . HIS A 1 438 ? -39.511 19.469 24.159 1.00 12.15 ? 438 HIS A CB 1 ATOM 3389 C CG . HIS A 1 438 ? -40.344 19.146 22.967 1.00 14.48 ? 438 HIS A CG 1 ATOM 3390 N ND1 . HIS A 1 438 ? -41.368 18.227 23.009 1.00 14.13 ? 438 HIS A ND1 1 ATOM 3391 C CD2 . HIS A 1 438 ? -40.265 19.568 21.684 1.00 14.04 ? 438 HIS A CD2 1 ATOM 3392 C CE1 . HIS A 1 438 ? -41.882 18.093 21.802 1.00 13.15 ? 438 HIS A CE1 1 ATOM 3393 N NE2 . HIS A 1 438 ? -41.232 18.895 20.980 1.00 15.07 ? 438 HIS A NE2 1 ATOM 3394 N N . ASP A 1 439 ? -38.908 19.926 26.943 1.00 10.49 ? 439 ASP A N 1 ATOM 3395 C CA . ASP A 1 439 ? -37.854 19.756 27.919 1.00 10.16 ? 439 ASP A CA 1 ATOM 3396 C C . ASP A 1 439 ? -37.282 18.441 27.404 1.00 11.80 ? 439 ASP A C 1 ATOM 3397 O O . ASP A 1 439 ? -38.042 17.560 26.968 1.00 13.22 ? 439 ASP A O 1 ATOM 3398 C CB . ASP A 1 439 ? -38.385 19.533 29.331 1.00 10.13 ? 439 ASP A CB 1 ATOM 3399 C CG . ASP A 1 439 ? -38.683 20.814 30.052 1.00 10.04 ? 439 ASP A CG 1 ATOM 3400 O OD1 . ASP A 1 439 ? -37.927 21.798 29.908 1.00 10.20 ? 439 ASP A OD1 1 ATOM 3401 O OD2 . ASP A 1 439 ? -39.707 20.849 30.753 1.00 12.92 ? 439 ASP A OD2 1 ATOM 3402 N N . PHE A 1 440 ? -35.962 18.339 27.342 1.00 8.35 ? 440 PHE A N 1 ATOM 3403 C CA . PHE A 1 440 ? -35.353 17.096 26.896 1.00 9.63 ? 440 PHE A CA 1 ATOM 3404 C C . PHE A 1 440 ? -34.780 16.332 28.076 1.00 10.00 ? 440 PHE A C 1 ATOM 3405 O O . PHE A 1 440 ? -34.587 16.901 29.155 1.00 9.83 ? 440 PHE A O 1 ATOM 3406 C CB . PHE A 1 440 ? -34.259 17.337 25.832 1.00 8.30 ? 440 PHE A CB 1 ATOM 3407 C CG . PHE A 1 440 ? -33.289 18.454 26.164 1.00 8.42 ? 440 PHE A CG 1 ATOM 3408 C CD1 . PHE A 1 440 ? -32.411 18.371 27.264 1.00 7.12 ? 440 PHE A CD1 1 ATOM 3409 C CD2 . PHE A 1 440 ? -33.231 19.588 25.348 1.00 8.47 ? 440 PHE A CD2 1 ATOM 3410 C CE1 . PHE A 1 440 ? -31.496 19.399 27.542 1.00 6.49 ? 440 PHE A CE1 1 ATOM 3411 C CE2 . PHE A 1 440 ? -32.315 20.628 25.609 1.00 4.57 ? 440 PHE A CE2 1 ATOM 3412 C CZ . PHE A 1 440 ? -31.445 20.528 26.710 1.00 6.68 ? 440 PHE A CZ 1 ATOM 3413 N N . LEU A 1 441 ? -34.489 15.057 27.857 1.00 8.91 ? 441 LEU A N 1 ATOM 3414 C CA . LEU A 1 441 ? -33.862 14.232 28.876 1.00 11.11 ? 441 LEU A CA 1 ATOM 3415 C C . LEU A 1 441 ? -32.379 14.215 28.539 1.00 10.12 ? 441 LEU A C 1 ATOM 3416 O O . LEU A 1 441 ? -32.019 14.013 27.377 1.00 11.71 ? 441 LEU A O 1 ATOM 3417 C CB . LEU A 1 441 ? -34.398 12.806 28.825 1.00 11.33 ? 441 LEU A CB 1 ATOM 3418 C CG . LEU A 1 441 ? -35.863 12.547 29.160 1.00 13.10 ? 441 LEU A CG 1 ATOM 3419 C CD1 . LEU A 1 441 ? -36.088 11.062 29.076 1.00 11.81 ? 441 LEU A CD1 1 ATOM 3420 C CD2 . LEU A 1 441 ? -36.215 13.040 30.551 1.00 12.62 ? 441 LEU A CD2 1 ATOM 3421 N N . VAL A 1 442 ? -31.527 14.470 29.532 1.00 8.76 ? 442 VAL A N 1 ATOM 3422 C CA . VAL A 1 442 ? -30.083 14.444 29.316 1.00 9.98 ? 442 VAL A CA 1 ATOM 3423 C C . VAL A 1 442 ? -29.637 13.024 29.657 1.00 10.67 ? 442 VAL A C 1 ATOM 3424 O O . VAL A 1 442 ? -29.404 12.687 30.822 1.00 11.39 ? 442 VAL A O 1 ATOM 3425 C CB . VAL A 1 442 ? -29.324 15.493 30.172 1.00 10.00 ? 442 VAL A CB 1 ATOM 3426 C CG1 . VAL A 1 442 ? -27.881 15.602 29.698 1.00 7.66 ? 442 VAL A CG1 1 ATOM 3427 C CG2 . VAL A 1 442 ? -30.000 16.852 30.075 1.00 8.73 ? 442 VAL A CG2 1 ATOM 3428 N N . LEU A 1 443 ? -29.546 12.198 28.619 1.00 10.72 ? 443 LEU A N 1 ATOM 3429 C CA . LEU A 1 443 ? -29.181 10.788 28.757 1.00 12.09 ? 443 LEU A CA 1 ATOM 3430 C C . LEU A 1 443 ? -27.734 10.543 29.104 1.00 13.76 ? 443 LEU A C 1 ATOM 3431 O O . LEU A 1 443 ? -27.413 9.560 29.764 1.00 14.04 ? 443 LEU A O 1 ATOM 3432 C CB . LEU A 1 443 ? -29.550 10.016 27.494 1.00 11.21 ? 443 LEU A CB 1 ATOM 3433 C CG . LEU A 1 443 ? -31.016 10.122 27.074 1.00 12.28 ? 443 LEU A CG 1 ATOM 3434 C CD1 . LEU A 1 443 ? -31.216 9.341 25.813 1.00 12.81 ? 443 LEU A CD1 1 ATOM 3435 C CD2 . LEU A 1 443 ? -31.930 9.616 28.162 1.00 11.65 ? 443 LEU A CD2 1 ATOM 3436 N N . GLY A 1 444 ? -26.872 11.450 28.663 1.00 13.64 ? 444 GLY A N 1 ATOM 3437 C CA . GLY A 1 444 ? -25.460 11.322 28.951 1.00 12.97 ? 444 GLY A CA 1 ATOM 3438 C C . GLY A 1 444 ? -24.631 12.249 28.108 1.00 12.72 ? 444 GLY A C 1 ATOM 3439 O O . GLY A 1 444 ? -25.128 12.898 27.184 1.00 11.01 ? 444 GLY A O 1 ATOM 3440 N N . ARG A 1 445 ? -23.355 12.321 28.459 1.00 12.24 ? 445 ARG A N 1 ATOM 3441 C CA . ARG A 1 445 ? -22.399 13.149 27.751 1.00 13.41 ? 445 ARG A CA 1 ATOM 3442 C C . ARG A 1 445 ? -21.033 12.505 27.869 1.00 13.22 ? 445 ARG A C 1 ATOM 3443 O O . ARG A 1 445 ? -20.859 11.543 28.618 1.00 11.48 ? 445 ARG A O 1 ATOM 3444 C CB . ARG A 1 445 ? -22.391 14.588 28.296 1.00 12.62 ? 445 ARG A CB 1 ATOM 3445 C CG . ARG A 1 445 ? -21.969 14.756 29.744 1.00 12.06 ? 445 ARG A CG 1 ATOM 3446 C CD . ARG A 1 445 ? -22.134 16.201 30.172 1.00 11.20 ? 445 ARG A CD 1 ATOM 3447 N NE . ARG A 1 445 ? -21.679 16.410 31.544 1.00 12.27 ? 445 ARG A NE 1 ATOM 3448 C CZ . ARG A 1 445 ? -22.172 17.323 32.373 1.00 11.70 ? 445 ARG A CZ 1 ATOM 3449 N NH1 . ARG A 1 445 ? -23.149 18.139 31.982 1.00 8.56 ? 445 ARG A NH1 1 ATOM 3450 N NH2 . ARG A 1 445 ? -21.733 17.377 33.626 1.00 12.22 ? 445 ARG A NH2 1 ATOM 3451 N N . SER A 1 446 ? -20.079 13.029 27.106 1.00 13.30 ? 446 SER A N 1 ATOM 3452 C CA . SER A 1 446 ? -18.695 12.564 27.111 1.00 14.14 ? 446 SER A CA 1 ATOM 3453 C C . SER A 1 446 ? -18.089 12.779 28.507 1.00 14.48 ? 446 SER A C 1 ATOM 3454 O O . SER A 1 446 ? -18.612 13.603 29.263 1.00 13.95 ? 446 SER A O 1 ATOM 3455 C CB . SER A 1 446 ? -17.924 13.325 26.032 1.00 14.51 ? 446 SER A CB 1 ATOM 3456 O OG . SER A 1 446 ? -18.271 14.696 26.005 1.00 15.43 ? 446 SER A OG 1 ATOM 3457 N N . PRO A 1 447 ? -17.037 12.006 28.896 1.00 15.49 ? 447 PRO A N 1 ATOM 3458 C CA . PRO A 1 447 ? -16.428 12.177 30.227 1.00 15.06 ? 447 PRO A CA 1 ATOM 3459 C C . PRO A 1 447 ? -16.105 13.619 30.624 1.00 14.65 ? 447 PRO A C 1 ATOM 3460 O O . PRO A 1 447 ? -15.638 14.411 29.796 1.00 14.71 ? 447 PRO A O 1 ATOM 3461 C CB . PRO A 1 447 ? -15.163 11.330 30.127 1.00 17.63 ? 447 PRO A CB 1 ATOM 3462 C CG . PRO A 1 447 ? -15.610 10.190 29.295 1.00 17.42 ? 447 PRO A CG 1 ATOM 3463 C CD . PRO A 1 447 ? -16.386 10.881 28.189 1.00 15.66 ? 447 PRO A CD 1 ATOM 3464 N N . ASP A 1 448 ? -16.438 13.960 31.872 1.00 14.71 ? 448 ASP A N 1 ATOM 3465 C CA . ASP A 1 448 ? -16.200 15.296 32.428 1.00 15.86 ? 448 ASP A CA 1 ATOM 3466 C C . ASP A 1 448 ? -14.693 15.507 32.593 1.00 16.34 ? 448 ASP A C 1 ATOM 3467 O O . ASP A 1 448 ? -14.050 14.852 33.414 1.00 17.76 ? 448 ASP A O 1 ATOM 3468 C CB . ASP A 1 448 ? -16.922 15.459 33.776 1.00 15.24 ? 448 ASP A CB 1 ATOM 3469 C CG . ASP A 1 448 ? -18.453 15.446 33.654 1.00 16.55 ? 448 ASP A CG 1 ATOM 3470 O OD1 . ASP A 1 448 ? -19.003 15.374 32.529 1.00 15.21 ? 448 ASP A OD1 1 ATOM 3471 O OD2 . ASP A 1 448 ? -19.115 15.521 34.708 1.00 17.39 ? 448 ASP A OD2 1 ATOM 3472 N N . VAL A 1 449 ? -14.137 16.343 31.719 1.00 14.91 ? 449 VAL A N 1 ATOM 3473 C CA . VAL A 1 449 ? -12.703 16.662 31.682 1.00 15.41 ? 449 VAL A CA 1 ATOM 3474 C C . VAL A 1 449 ? -12.547 18.195 31.678 1.00 15.31 ? 449 VAL A C 1 ATOM 3475 O O . VAL A 1 449 ? -13.561 18.899 31.533 1.00 16.28 ? 449 VAL A O 1 ATOM 3476 C CB . VAL A 1 449 ? -12.037 16.045 30.381 1.00 15.70 ? 449 VAL A CB 1 ATOM 3477 C CG1 . VAL A 1 449 ? -11.999 14.520 30.462 1.00 18.57 ? 449 VAL A CG1 1 ATOM 3478 C CG2 . VAL A 1 449 ? -12.757 16.507 29.106 1.00 19.15 ? 449 VAL A CG2 1 ATOM 3479 N N . PRO A 1 450 ? -11.317 18.740 31.918 1.00 15.20 ? 450 PRO A N 1 ATOM 3480 C CA . PRO A 1 450 ? -11.202 20.207 31.889 1.00 13.83 ? 450 PRO A CA 1 ATOM 3481 C C . PRO A 1 450 ? -11.621 20.800 30.541 1.00 13.26 ? 450 PRO A C 1 ATOM 3482 O O . PRO A 1 450 ? -11.202 20.320 29.489 1.00 11.61 ? 450 PRO A O 1 ATOM 3483 C CB . PRO A 1 450 ? -9.726 20.436 32.200 1.00 16.17 ? 450 PRO A CB 1 ATOM 3484 C CG . PRO A 1 450 ? -9.451 19.362 33.190 1.00 14.76 ? 450 PRO A CG 1 ATOM 3485 C CD . PRO A 1 450 ? -10.096 18.166 32.534 1.00 14.68 ? 450 PRO A CD 1 ATOM 3486 N N . ALA A 1 451 ? -12.530 21.777 30.598 1.00 13.52 ? 451 ALA A N 1 ATOM 3487 C CA . ALA A 1 451 ? -13.100 22.442 29.418 1.00 12.81 ? 451 ALA A CA 1 ATOM 3488 C C . ALA A 1 451 ? -12.122 23.003 28.394 1.00 12.24 ? 451 ALA A C 1 ATOM 3489 O O . ALA A 1 451 ? -12.431 23.044 27.205 1.00 12.44 ? 451 ALA A O 1 ATOM 3490 C CB . ALA A 1 451 ? -14.083 23.525 29.850 1.00 11.77 ? 451 ALA A CB 1 ATOM 3491 N N . ALA A 1 452 ? -10.945 23.416 28.858 1.00 13.61 ? 452 ALA A N 1 ATOM 3492 C CA . ALA A 1 452 ? -9.923 23.965 27.973 1.00 13.24 ? 452 ALA A CA 1 ATOM 3493 C C . ALA A 1 452 ? -8.829 22.956 27.608 1.00 13.45 ? 452 ALA A C 1 ATOM 3494 O O . ALA A 1 452 ? -7.888 23.303 26.894 1.00 13.29 ? 452 ALA A O 1 ATOM 3495 C CB . ALA A 1 452 ? -9.310 25.204 28.595 1.00 13.34 ? 452 ALA A CB 1 ATOM 3496 N N . SER A 1 453 ? -8.985 21.703 28.041 1.00 15.79 ? 453 SER A N 1 ATOM 3497 C CA . SER A 1 453 ? -7.996 20.650 27.771 1.00 18.73 ? 453 SER A CA 1 ATOM 3498 C C . SER A 1 453 ? -7.818 20.230 26.324 1.00 20.88 ? 453 SER A C 1 ATOM 3499 O O . SER A 1 453 ? -6.749 19.750 25.942 1.00 22.00 ? 453 SER A O 1 ATOM 3500 C CB . SER A 1 453 ? -8.254 19.404 28.626 1.00 18.47 ? 453 SER A CB 1 ATOM 3501 O OG . SER A 1 453 ? -9.420 18.717 28.212 1.00 19.78 ? 453 SER A OG 1 ATOM 3502 N N . GLN A 1 454 ? -8.862 20.462 25.528 1.00 22.33 ? 454 GLN A N 1 ATOM 3503 C CA . GLN A 1 454 ? -8.936 20.097 24.111 1.00 23.77 ? 454 GLN A CA 1 ATOM 3504 C C . GLN A 1 454 ? -8.936 18.577 23.890 1.00 23.45 ? 454 GLN A C 1 ATOM 3505 O O . GLN A 1 454 ? -8.583 18.089 22.814 1.00 24.21 ? 454 GLN A O 1 ATOM 3506 C CB . GLN A 1 454 ? -7.889 20.838 23.245 1.00 26.32 ? 454 GLN A CB 1 ATOM 3507 C CG . GLN A 1 454 ? -8.082 22.368 23.156 1.00 27.45 ? 454 GLN A CG 1 ATOM 3508 C CD . GLN A 1 454 ? -9.431 22.793 22.565 1.00 30.32 ? 454 GLN A CD 1 ATOM 3509 O OE1 . GLN A 1 454 ? -9.949 22.168 21.635 1.00 30.14 ? 454 GLN A OE1 1 ATOM 3510 N NE2 . GLN A 1 454 ? -10.004 23.860 23.115 1.00 30.80 ? 454 GLN A NE2 1 ATOM 3511 N N . GLN A 1 455 ? -9.348 17.844 24.932 1.00 23.71 ? 455 GLN A N 1 ATOM 3512 C CA . GLN A 1 455 ? -9.471 16.383 24.897 1.00 23.45 ? 455 GLN A CA 1 ATOM 3513 C C . GLN A 1 455 ? -10.736 16.063 24.113 1.00 23.86 ? 455 GLN A C 1 ATOM 3514 O O . GLN A 1 455 ? -11.806 16.616 24.398 1.00 23.02 ? 455 GLN A O 1 ATOM 3515 C CB . GLN A 1 455 ? -9.606 15.800 26.301 1.00 24.41 ? 455 GLN A CB 1 ATOM 3516 C CG . GLN A 1 455 ? -8.306 15.552 27.018 1.00 26.95 ? 455 GLN A CG 1 ATOM 3517 C CD . GLN A 1 455 ? -8.512 14.725 28.264 1.00 27.82 ? 455 GLN A CD 1 ATOM 3518 O OE1 . GLN A 1 455 ? -8.439 13.499 28.227 1.00 30.75 ? 455 GLN A OE1 1 ATOM 3519 N NE2 . GLN A 1 455 ? -8.798 15.391 29.371 1.00 29.00 ? 455 GLN A NE2 1 ATOM 3520 N N . ARG A 1 456 ? -10.593 15.191 23.117 1.00 23.18 ? 456 ARG A N 1 ATOM 3521 C CA . ARG A 1 456 ? -11.692 14.809 22.233 1.00 23.59 ? 456 ARG A CA 1 ATOM 3522 C C . ARG A 1 456 ? -12.302 13.450 22.531 1.00 22.35 ? 456 ARG A C 1 ATOM 3523 O O . ARG A 1 456 ? -11.605 12.513 22.922 1.00 21.37 ? 456 ARG A O 1 ATOM 3524 C CB . ARG A 1 456 ? -11.227 14.824 20.767 1.00 26.58 ? 456 ARG A CB 1 ATOM 3525 C CG . ARG A 1 456 ? -10.366 16.018 20.355 1.00 30.97 ? 456 ARG A CG 1 ATOM 3526 C CD . ARG A 1 456 ? -11.111 17.336 20.459 1.00 35.66 ? 456 ARG A CD 1 ATOM 3527 N NE . ARG A 1 456 ? -10.210 18.463 20.239 1.00 39.98 ? 456 ARG A NE 1 ATOM 3528 C CZ . ARG A 1 456 ? -10.393 19.416 19.331 1.00 40.80 ? 456 ARG A CZ 1 ATOM 3529 N NH1 . ARG A 1 456 ? -11.459 19.406 18.537 1.00 41.02 ? 456 ARG A NH1 1 ATOM 3530 N NH2 . ARG A 1 456 ? -9.478 20.363 19.189 1.00 40.95 ? 456 ARG A NH2 1 ATOM 3531 N N . PHE A 1 457 ? -13.618 13.359 22.342 1.00 22.00 ? 457 PHE A N 1 ATOM 3532 C CA . PHE A 1 457 ? -14.363 12.118 22.549 1.00 21.15 ? 457 PHE A CA 1 ATOM 3533 C C . PHE A 1 457 ? -15.403 11.920 21.452 1.00 20.63 ? 457 PHE A C 1 ATOM 3534 O O . PHE A 1 457 ? -16.157 12.843 21.113 1.00 18.94 ? 457 PHE A O 1 ATOM 3535 C CB . PHE A 1 457 ? -15.088 12.102 23.904 1.00 22.43 ? 457 PHE A CB 1 ATOM 3536 C CG . PHE A 1 457 ? -14.179 12.032 25.100 1.00 23.72 ? 457 PHE A CG 1 ATOM 3537 C CD1 . PHE A 1 457 ? -13.532 10.827 25.444 1.00 23.68 ? 457 PHE A CD1 1 ATOM 3538 C CD2 . PHE A 1 457 ? -13.964 13.174 25.893 1.00 23.03 ? 457 PHE A CD2 1 ATOM 3539 C CE1 . PHE A 1 457 ? -12.672 10.759 26.573 1.00 24.20 ? 457 PHE A CE1 1 ATOM 3540 C CE2 . PHE A 1 457 ? -13.109 13.126 27.024 1.00 23.04 ? 457 PHE A CE2 1 ATOM 3541 C CZ . PHE A 1 457 ? -12.459 11.914 27.366 1.00 23.31 ? 457 PHE A CZ 1 ATOM 3542 N N . VAL A 1 458 ? -15.387 10.733 20.852 1.00 18.55 ? 458 VAL A N 1 ATOM 3543 C CA . VAL A 1 458 ? -16.359 10.358 19.827 1.00 19.83 ? 458 VAL A CA 1 ATOM 3544 C C . VAL A 1 458 ? -17.133 9.218 20.483 1.00 18.90 ? 458 VAL A C 1 ATOM 3545 O O . VAL A 1 458 ? -16.535 8.374 21.166 1.00 19.66 ? 458 VAL A O 1 ATOM 3546 C CB . VAL A 1 458 ? -15.690 9.869 18.499 1.00 18.90 ? 458 VAL A CB 1 ATOM 3547 C CG1 . VAL A 1 458 ? -16.759 9.492 17.458 1.00 19.18 ? 458 VAL A CG1 1 ATOM 3548 C CG2 . VAL A 1 458 ? -14.792 10.959 17.919 1.00 19.51 ? 458 VAL A CG2 1 ATOM 3549 N N . PHE A 1 459 ? -18.455 9.218 20.298 1.00 18.33 ? 459 PHE A N 1 ATOM 3550 C CA . PHE A 1 459 ? -19.341 8.198 20.866 1.00 18.27 ? 459 PHE A CA 1 ATOM 3551 C C . PHE A 1 459 ? -18.908 6.789 20.449 1.00 18.35 ? 459 PHE A C 1 ATOM 3552 O O . PHE A 1 459 ? -18.879 6.452 19.262 1.00 18.77 ? 459 PHE A O 1 ATOM 3553 C CB . PHE A 1 459 ? -20.805 8.465 20.464 1.00 17.14 ? 459 PHE A CB 1 ATOM 3554 C CG . PHE A 1 459 ? -21.814 7.589 21.178 1.00 18.11 ? 459 PHE A CG 1 ATOM 3555 C CD1 . PHE A 1 459 ? -22.253 7.917 22.470 1.00 18.71 ? 459 PHE A CD1 1 ATOM 3556 C CD2 . PHE A 1 459 ? -22.323 6.423 20.567 1.00 19.92 ? 459 PHE A CD2 1 ATOM 3557 C CE1 . PHE A 1 459 ? -23.190 7.098 23.165 1.00 19.87 ? 459 PHE A CE1 1 ATOM 3558 C CE2 . PHE A 1 459 ? -23.256 5.590 21.245 1.00 21.80 ? 459 PHE A CE2 1 ATOM 3559 C CZ . PHE A 1 459 ? -23.689 5.930 22.549 1.00 20.28 ? 459 PHE A CZ 1 ATOM 3560 N N . ASP A 1 460 ? -18.522 6.016 21.458 1.00 19.33 ? 460 ASP A N 1 ATOM 3561 C CA . ASP A 1 460 ? -18.071 4.640 21.304 1.00 21.74 ? 460 ASP A CA 1 ATOM 3562 C C . ASP A 1 460 ? -19.068 3.791 22.101 1.00 22.12 ? 460 ASP A C 1 ATOM 3563 O O . ASP A 1 460 ? -19.040 3.801 23.329 1.00 21.29 ? 460 ASP A O 1 ATOM 3564 C CB . ASP A 1 460 ? -16.636 4.507 21.857 1.00 23.89 ? 460 ASP A CB 1 ATOM 3565 C CG . ASP A 1 460 ? -16.068 3.080 21.766 1.00 25.54 ? 460 ASP A CG 1 ATOM 3566 O OD1 . ASP A 1 460 ? -16.663 2.199 21.108 1.00 27.22 ? 460 ASP A OD1 1 ATOM 3567 O OD2 . ASP A 1 460 ? -15.002 2.851 22.373 1.00 27.14 ? 460 ASP A OD2 1 ATOM 3568 N N . PRO A 1 461 ? -19.945 3.031 21.408 1.00 22.85 ? 461 PRO A N 1 ATOM 3569 C CA . PRO A 1 461 ? -20.962 2.169 22.032 1.00 24.47 ? 461 PRO A CA 1 ATOM 3570 C C . PRO A 1 461 ? -20.447 1.169 23.079 1.00 25.82 ? 461 PRO A C 1 ATOM 3571 O O . PRO A 1 461 ? -21.143 0.878 24.058 1.00 26.35 ? 461 PRO A O 1 ATOM 3572 C CB . PRO A 1 461 ? -21.560 1.431 20.834 1.00 24.27 ? 461 PRO A CB 1 ATOM 3573 C CG . PRO A 1 461 ? -21.409 2.402 19.728 1.00 24.99 ? 461 PRO A CG 1 ATOM 3574 C CD . PRO A 1 461 ? -20.015 2.912 19.938 1.00 23.89 ? 461 PRO A CD 1 ATOM 3575 N N . ALA A 1 462 ? -19.209 0.704 22.888 1.00 26.99 ? 462 ALA A N 1 ATOM 3576 C CA . ALA A 1 462 ? -18.547 -0.270 23.770 1.00 28.88 ? 462 ALA A CA 1 ATOM 3577 C C . ALA A 1 462 ? -18.260 0.205 25.199 1.00 29.99 ? 462 ALA A C 1 ATOM 3578 O O . ALA A 1 462 ? -18.161 -0.613 26.117 1.00 31.06 ? 462 ALA A O 1 ATOM 3579 C CB . ALA A 1 462 ? -17.261 -0.772 23.115 1.00 28.84 ? 462 ALA A CB 1 ATOM 3580 N N . VAL A 1 463 ? -18.091 1.516 25.378 1.00 29.94 ? 463 VAL A N 1 ATOM 3581 C CA . VAL A 1 463 ? -17.826 2.089 26.704 1.00 29.52 ? 463 VAL A CA 1 ATOM 3582 C C . VAL A 1 463 ? -18.864 3.133 27.120 1.00 28.58 ? 463 VAL A C 1 ATOM 3583 O O . VAL A 1 463 ? -19.084 3.353 28.313 1.00 29.08 ? 463 VAL A O 1 ATOM 3584 C CB . VAL A 1 463 ? -16.393 2.731 26.814 1.00 31.32 ? 463 VAL A CB 1 ATOM 3585 C CG1 . VAL A 1 463 ? -15.310 1.656 26.792 1.00 30.77 ? 463 VAL A CG1 1 ATOM 3586 C CG2 . VAL A 1 463 ? -16.150 3.748 25.701 1.00 31.68 ? 463 VAL A CG2 1 ATOM 3587 N N . ASP A 1 464 ? -19.524 3.736 26.132 1.00 26.18 ? 464 ASP A N 1 ATOM 3588 C CA . ASP A 1 464 ? -20.504 4.792 26.379 1.00 24.06 ? 464 ASP A CA 1 ATOM 3589 C C . ASP A 1 464 ? -21.959 4.433 26.624 1.00 23.02 ? 464 ASP A C 1 ATOM 3590 O O . ASP A 1 464 ? -22.658 5.201 27.280 1.00 21.68 ? 464 ASP A O 1 ATOM 3591 C CB . ASP A 1 464 ? -20.397 5.865 25.302 1.00 22.38 ? 464 ASP A CB 1 ATOM 3592 C CG . ASP A 1 464 ? -19.070 6.599 25.345 1.00 20.33 ? 464 ASP A CG 1 ATOM 3593 O OD1 . ASP A 1 464 ? -18.634 6.971 26.455 1.00 20.52 ? 464 ASP A OD1 1 ATOM 3594 O OD2 . ASP A 1 464 ? -18.482 6.833 24.272 1.00 21.28 ? 464 ASP A OD2 1 ATOM 3595 N N . LEU A 1 465 ? -22.419 3.285 26.120 1.00 22.99 ? 465 LEU A N 1 ATOM 3596 C CA . LEU A 1 465 ? -23.809 2.858 26.341 1.00 23.89 ? 465 LEU A CA 1 ATOM 3597 C C . LEU A 1 465 ? -24.102 2.599 27.821 1.00 23.89 ? 465 LEU A C 1 ATOM 3598 O O . LEU A 1 465 ? -25.192 2.914 28.307 1.00 23.69 ? 465 LEU A O 1 ATOM 3599 C CB . LEU A 1 465 ? -24.162 1.629 25.499 1.00 24.45 ? 465 LEU A CB 1 ATOM 3600 C CG . LEU A 1 465 ? -24.558 1.897 24.041 1.00 25.22 ? 465 LEU A CG 1 ATOM 3601 C CD1 . LEU A 1 465 ? -24.542 0.603 23.271 1.00 25.96 ? 465 LEU A CD1 1 ATOM 3602 C CD2 . LEU A 1 465 ? -25.918 2.560 23.934 1.00 24.03 ? 465 LEU A CD2 1 ATOM 3603 N N . ALA A 1 466 ? -23.069 2.153 28.540 1.00 23.34 ? 466 ALA A N 1 ATOM 3604 C CA . ALA A 1 466 ? -23.140 1.859 29.973 1.00 24.70 ? 466 ALA A CA 1 ATOM 3605 C C . ALA A 1 466 ? -23.091 3.131 30.821 1.00 24.35 ? 466 ALA A C 1 ATOM 3606 O O . ALA A 1 466 ? -23.442 3.116 32.004 1.00 25.39 ? 466 ALA A O 1 ATOM 3607 C CB . ALA A 1 466 ? -22.003 0.918 30.368 1.00 26.13 ? 466 ALA A CB 1 ATOM 3608 N N . ARG A 1 467 ? -22.655 4.225 30.199 1.00 22.96 ? 467 ARG A N 1 ATOM 3609 C CA . ARG A 1 467 ? -22.550 5.525 30.857 1.00 22.18 ? 467 ARG A CA 1 ATOM 3610 C C . ARG A 1 467 ? -23.846 6.337 30.774 1.00 21.26 ? 467 ARG A C 1 ATOM 3611 O O . ARG A 1 467 ? -24.006 7.334 31.485 1.00 21.42 ? 467 ARG A O 1 ATOM 3612 C CB . ARG A 1 467 ? -21.400 6.322 30.252 1.00 22.24 ? 467 ARG A CB 1 ATOM 3613 C CG . ARG A 1 467 ? -20.012 5.761 30.547 1.00 21.94 ? 467 ARG A CG 1 ATOM 3614 C CD . ARG A 1 467 ? -18.906 6.665 30.015 1.00 23.75 ? 467 ARG A CD 1 ATOM 3615 N NE . ARG A 1 467 ? -18.901 7.978 30.667 1.00 24.08 ? 467 ARG A NE 1 ATOM 3616 C CZ . ARG A 1 467 ? -19.277 9.116 30.087 1.00 23.34 ? 467 ARG A CZ 1 ATOM 3617 N NH1 . ARG A 1 467 ? -19.684 9.121 28.823 1.00 22.88 ? 467 ARG A NH1 1 ATOM 3618 N NH2 . ARG A 1 467 ? -19.314 10.237 30.795 1.00 21.56 ? 467 ARG A NH2 1 ATOM 3619 N N . LEU A 1 468 ? -24.770 5.898 29.918 1.00 19.26 ? 468 LEU A N 1 ATOM 3620 C CA . LEU A 1 468 ? -26.055 6.577 29.742 1.00 19.24 ? 468 LEU A CA 1 ATOM 3621 C C . LEU A 1 468 ? -27.066 6.233 30.829 1.00 19.82 ? 468 LEU A C 1 ATOM 3622 O O . LEU A 1 468 ? -27.064 5.117 31.361 1.00 21.14 ? 468 LEU A O 1 ATOM 3623 C CB . LEU A 1 468 ? -26.652 6.262 28.372 1.00 17.71 ? 468 LEU A CB 1 ATOM 3624 C CG . LEU A 1 468 ? -25.782 6.501 27.140 1.00 17.55 ? 468 LEU A CG 1 ATOM 3625 C CD1 . LEU A 1 468 ? -26.460 5.888 25.934 1.00 17.28 ? 468 LEU A CD1 1 ATOM 3626 C CD2 . LEU A 1 468 ? -25.490 7.984 26.937 1.00 13.78 ? 468 LEU A CD2 1 ATOM 3627 N N . ASN A 1 469 ? -27.905 7.211 31.167 1.00 19.14 ? 469 ASN A N 1 ATOM 3628 C CA . ASN A 1 469 ? -28.942 7.054 32.184 1.00 19.83 ? 469 ASN A CA 1 ATOM 3629 C C . ASN A 1 469 ? -30.317 7.350 31.595 1.00 18.64 ? 469 ASN A C 1 ATOM 3630 O O . ASN A 1 469 ? -30.576 8.454 31.110 1.00 16.41 ? 469 ASN A O 1 ATOM 3631 C CB . ASN A 1 469 ? -28.666 7.971 33.397 1.00 20.89 ? 469 ASN A CB 1 ATOM 3632 C CG . ASN A 1 469 ? -29.750 7.880 34.488 1.00 21.76 ? 469 ASN A CG 1 ATOM 3633 O OD1 . ASN A 1 469 ? -30.413 6.853 34.647 1.00 20.11 ? 469 ASN A OD1 1 ATOM 3634 N ND2 . ASN A 1 469 ? -29.928 8.970 35.236 1.00 21.34 ? 469 ASN A ND2 1 ATOM 3635 N N . GLY A 1 470 ? -31.188 6.347 31.671 1.00 18.13 ? 470 GLY A N 1 ATOM 3636 C CA . GLY A 1 470 ? -32.549 6.468 31.189 1.00 17.60 ? 470 GLY A CA 1 ATOM 3637 C C . GLY A 1 470 ? -33.563 6.373 32.315 1.00 18.33 ? 470 GLY A C 1 ATOM 3638 O O . GLY A 1 470 ? -34.766 6.483 32.072 1.00 18.40 ? 470 GLY A O 1 ATOM 3639 N N . ASP A 1 471 ? -33.070 6.182 33.541 1.00 17.96 ? 471 ASP A N 1 ATOM 3640 C CA . ASP A 1 471 ? -33.898 6.068 34.747 1.00 19.18 ? 471 ASP A CA 1 ATOM 3641 C C . ASP A 1 471 ? -33.972 7.453 35.403 1.00 17.01 ? 471 ASP A C 1 ATOM 3642 O O . ASP A 1 471 ? -33.124 7.821 36.224 1.00 14.93 ? 471 ASP A O 1 ATOM 3643 C CB . ASP A 1 471 ? -33.290 5.013 35.698 1.00 22.98 ? 471 ASP A CB 1 ATOM 3644 C CG . ASP A 1 471 ? -34.113 4.796 36.976 1.00 27.38 ? 471 ASP A CG 1 ATOM 3645 O OD1 . ASP A 1 471 ? -35.344 5.023 36.970 1.00 28.51 ? 471 ASP A OD1 1 ATOM 3646 O OD2 . ASP A 1 471 ? -33.511 4.393 37.995 1.00 30.74 ? 471 ASP A OD2 1 ATOM 3647 N N . ASN A 1 472 ? -35.008 8.203 35.016 1.00 14.86 ? 472 ASN A N 1 ATOM 3648 C CA . ASN A 1 472 ? -35.276 9.579 35.467 1.00 13.87 ? 472 ASN A CA 1 ATOM 3649 C C . ASN A 1 472 ? -34.060 10.525 35.389 1.00 13.01 ? 472 ASN A C 1 ATOM 3650 O O . ASN A 1 472 ? -33.655 11.117 36.392 1.00 13.68 ? 472 ASN A O 1 ATOM 3651 C CB . ASN A 1 472 ? -35.943 9.609 36.852 1.00 12.96 ? 472 ASN A CB 1 ATOM 3652 C CG . ASN A 1 472 ? -36.585 10.957 37.160 1.00 14.27 ? 472 ASN A CG 1 ATOM 3653 O OD1 . ASN A 1 472 ? -37.113 11.623 36.263 1.00 12.68 ? 472 ASN A OD1 1 ATOM 3654 N ND2 . ASN A 1 472 ? -36.539 11.364 38.419 1.00 9.44 ? 472 ASN A ND2 1 ATOM 3655 N N . PRO A 1 473 ? -33.476 10.690 34.181 1.00 13.39 ? 473 PRO A N 1 ATOM 3656 C CA . PRO A 1 473 ? -32.313 11.566 34.003 1.00 13.63 ? 473 PRO A CA 1 ATOM 3657 C C . PRO A 1 473 ? -32.719 13.049 34.088 1.00 13.03 ? 473 PRO A C 1 ATOM 3658 O O . PRO A 1 473 ? -33.919 13.344 34.216 1.00 12.90 ? 473 PRO A O 1 ATOM 3659 C CB . PRO A 1 473 ? -31.839 11.175 32.598 1.00 13.21 ? 473 PRO A CB 1 ATOM 3660 C CG . PRO A 1 473 ? -33.082 10.926 31.889 1.00 13.19 ? 473 PRO A CG 1 ATOM 3661 C CD . PRO A 1 473 ? -33.907 10.146 32.873 1.00 13.83 ? 473 PRO A CD 1 ATOM 3662 N N . PRO A 1 474 ? -31.741 13.993 34.091 1.00 13.27 ? 474 PRO A N 1 ATOM 3663 C CA . PRO A 1 474 ? -32.100 15.417 34.156 1.00 12.90 ? 474 PRO A CA 1 ATOM 3664 C C . PRO A 1 474 ? -33.012 15.807 33.006 1.00 13.01 ? 474 PRO A C 1 ATOM 3665 O O . PRO A 1 474 ? -32.771 15.417 31.865 1.00 13.76 ? 474 PRO A O 1 ATOM 3666 C CB . PRO A 1 474 ? -30.754 16.107 34.009 1.00 11.85 ? 474 PRO A CB 1 ATOM 3667 C CG . PRO A 1 474 ? -29.882 15.210 34.743 1.00 13.82 ? 474 PRO A CG 1 ATOM 3668 C CD . PRO A 1 474 ? -30.282 13.845 34.284 1.00 13.31 ? 474 PRO A CD 1 ATOM 3669 N N . ARG A 1 475 ? -34.115 16.462 33.350 1.00 12.72 ? 475 ARG A N 1 ATOM 3670 C CA . ARG A 1 475 ? -35.088 16.917 32.374 1.00 12.38 ? 475 ARG A CA 1 ATOM 3671 C C . ARG A 1 475 ? -35.123 18.426 32.476 1.00 11.86 ? 475 ARG A C 1 ATOM 3672 O O . ARG A 1 475 ? -35.437 18.963 33.530 1.00 11.88 ? 475 ARG A O 1 ATOM 3673 C CB . ARG A 1 475 ? -36.470 16.331 32.664 1.00 10.92 ? 475 ARG A CB 1 ATOM 3674 C CG . ARG A 1 475 ? -37.501 16.646 31.592 1.00 10.87 ? 475 ARG A CG 1 ATOM 3675 C CD . ARG A 1 475 ? -38.794 15.878 31.762 1.00 11.49 ? 475 ARG A CD 1 ATOM 3676 N NE . ARG A 1 475 ? -39.591 16.330 32.901 1.00 11.18 ? 475 ARG A NE 1 ATOM 3677 C CZ . ARG A 1 475 ? -39.770 15.627 34.015 1.00 11.98 ? 475 ARG A CZ 1 ATOM 3678 N NH1 . ARG A 1 475 ? -39.199 14.433 34.152 1.00 9.21 ? 475 ARG A NH1 1 ATOM 3679 N NH2 . ARG A 1 475 ? -40.526 16.112 34.989 1.00 10.33 ? 475 ARG A NH2 1 ATOM 3680 N N . ARG A 1 476 ? -34.749 19.094 31.387 1.00 11.08 ? 476 ARG A N 1 ATOM 3681 C CA . ARG A 1 476 ? -34.705 20.554 31.334 1.00 12.24 ? 476 ARG A CA 1 ATOM 3682 C C . ARG A 1 476 ? -34.674 21.043 29.884 1.00 12.27 ? 476 ARG A C 1 ATOM 3683 O O . ARG A 1 476 ? -34.679 20.227 28.961 1.00 11.03 ? 476 ARG A O 1 ATOM 3684 C CB . ARG A 1 476 ? -33.489 21.066 32.124 1.00 11.40 ? 476 ARG A CB 1 ATOM 3685 C CG . ARG A 1 476 ? -32.118 20.569 31.647 1.00 11.19 ? 476 ARG A CG 1 ATOM 3686 C CD . ARG A 1 476 ? -31.052 20.837 32.702 1.00 10.08 ? 476 ARG A CD 1 ATOM 3687 N NE . ARG A 1 476 ? -31.120 22.206 33.210 1.00 8.49 ? 476 ARG A NE 1 ATOM 3688 C CZ . ARG A 1 476 ? -30.451 22.657 34.265 1.00 7.87 ? 476 ARG A CZ 1 ATOM 3689 N NH1 . ARG A 1 476 ? -29.642 21.854 34.944 1.00 7.79 ? 476 ARG A NH1 1 ATOM 3690 N NH2 . ARG A 1 476 ? -30.584 23.924 34.633 1.00 7.29 ? 476 ARG A NH2 1 ATOM 3691 N N . ASP A 1 477 ? -34.635 22.361 29.688 1.00 12.07 ? 477 ASP A N 1 ATOM 3692 C CA . ASP A 1 477 ? -34.615 22.931 28.339 1.00 11.21 ? 477 ASP A CA 1 ATOM 3693 C C . ASP A 1 477 ? -33.232 23.351 27.828 1.00 10.22 ? 477 ASP A C 1 ATOM 3694 O O . ASP A 1 477 ? -33.069 23.603 26.634 1.00 10.25 ? 477 ASP A O 1 ATOM 3695 C CB . ASP A 1 477 ? -35.630 24.081 28.211 1.00 9.97 ? 477 ASP A CB 1 ATOM 3696 C CG . ASP A 1 477 ? -35.296 25.277 29.087 1.00 10.05 ? 477 ASP A CG 1 ATOM 3697 O OD1 . ASP A 1 477 ? -34.249 25.922 28.860 1.00 9.96 ? 477 ASP A OD1 1 ATOM 3698 O OD2 . ASP A 1 477 ? -36.097 25.591 29.987 1.00 14.38 ? 477 ASP A OD2 1 ATOM 3699 N N . THR A 1 478 ? -32.256 23.441 28.732 1.00 9.67 ? 478 THR A N 1 ATOM 3700 C CA . THR A 1 478 ? -30.887 23.820 28.380 1.00 8.79 ? 478 THR A CA 1 ATOM 3701 C C . THR A 1 478 ? -29.854 22.958 29.123 1.00 9.76 ? 478 THR A C 1 ATOM 3702 O O . THR A 1 478 ? -29.984 22.727 30.319 1.00 8.89 ? 478 THR A O 1 ATOM 3703 C CB . THR A 1 478 ? -30.599 25.318 28.700 1.00 9.59 ? 478 THR A CB 1 ATOM 3704 O OG1 . THR A 1 478 ? -31.599 26.150 28.107 1.00 9.07 ? 478 THR A OG1 1 ATOM 3705 C CG2 . THR A 1 478 ? -29.218 25.746 28.175 1.00 10.23 ? 478 THR A CG2 1 ATOM 3706 N N . THR A 1 479 ? -28.840 22.490 28.397 1.00 9.83 ? 479 THR A N 1 ATOM 3707 C CA . THR A 1 479 ? -27.749 21.710 28.983 1.00 10.00 ? 479 THR A CA 1 ATOM 3708 C C . THR A 1 479 ? -26.478 21.920 28.168 1.00 10.41 ? 479 THR A C 1 ATOM 3709 O O . THR A 1 479 ? -26.536 22.310 27.001 1.00 10.59 ? 479 THR A O 1 ATOM 3710 C CB . THR A 1 479 ? -28.082 20.181 29.134 1.00 9.77 ? 479 THR A CB 1 ATOM 3711 O OG1 . THR A 1 479 ? -27.193 19.593 30.089 1.00 8.77 ? 479 THR A OG1 1 ATOM 3712 C CG2 . THR A 1 479 ? -27.945 19.430 27.817 1.00 7.21 ? 479 THR A CG2 1 ATOM 3713 N N . MET A 1 480 ? -25.340 21.604 28.777 1.00 9.63 ? 480 MET A N 1 ATOM 3714 C CA . MET A 1 480 ? -24.053 21.776 28.126 1.00 9.41 ? 480 MET A CA 1 ATOM 3715 C C . MET A 1 480 ? -23.572 20.663 27.218 1.00 10.15 ? 480 MET A C 1 ATOM 3716 O O . MET A 1 480 ? -23.655 19.479 27.550 1.00 7.15 ? 480 MET A O 1 ATOM 3717 C CB . MET A 1 480 ? -22.958 22.052 29.160 1.00 10.91 ? 480 MET A CB 1 ATOM 3718 C CG . MET A 1 480 ? -23.151 23.324 29.958 1.00 8.76 ? 480 MET A CG 1 ATOM 3719 S SD . MET A 1 480 ? -23.284 24.794 28.940 1.00 9.62 ? 480 MET A SD 1 ATOM 3720 C CE . MET A 1 480 ? -21.650 24.923 28.259 1.00 7.18 ? 480 MET A CE 1 ATOM 3721 N N . LEU A 1 481 ? -23.082 21.079 26.054 1.00 10.06 ? 481 LEU A N 1 ATOM 3722 C CA . LEU A 1 481 ? -22.475 20.184 25.081 1.00 10.37 ? 481 LEU A CA 1 ATOM 3723 C C . LEU A 1 481 ? -20.991 20.368 25.441 1.00 10.69 ? 481 LEU A C 1 ATOM 3724 O O . LEU A 1 481 ? -20.456 21.471 25.294 1.00 10.31 ? 481 LEU A O 1 ATOM 3725 C CB . LEU A 1 481 ? -22.764 20.671 23.654 1.00 11.54 ? 481 LEU A CB 1 ATOM 3726 C CG . LEU A 1 481 ? -22.037 20.052 22.458 1.00 12.53 ? 481 LEU A CG 1 ATOM 3727 C CD1 . LEU A 1 481 ? -22.315 18.568 22.322 1.00 11.92 ? 481 LEU A CD1 1 ATOM 3728 C CD2 . LEU A 1 481 ? -22.413 20.784 21.187 1.00 13.51 ? 481 LEU A CD2 1 ATOM 3729 N N . PRO A 1 482 ? -20.331 19.317 25.983 1.00 10.20 ? 482 PRO A N 1 ATOM 3730 C CA . PRO A 1 482 ? -18.913 19.399 26.368 1.00 11.48 ? 482 PRO A CA 1 ATOM 3731 C C . PRO A 1 482 ? -17.985 19.741 25.215 1.00 11.96 ? 482 PRO A C 1 ATOM 3732 O O . PRO A 1 482 ? -18.224 19.325 24.078 1.00 11.26 ? 482 PRO A O 1 ATOM 3733 C CB . PRO A 1 482 ? -18.607 17.987 26.875 1.00 12.15 ? 482 PRO A CB 1 ATOM 3734 C CG . PRO A 1 482 ? -19.913 17.475 27.307 1.00 9.51 ? 482 PRO A CG 1 ATOM 3735 C CD . PRO A 1 482 ? -20.841 17.958 26.233 1.00 10.60 ? 482 PRO A CD 1 ATOM 3736 N N . ALA A 1 483 ? -16.932 20.500 25.519 1.00 13.36 ? 483 ALA A N 1 ATOM 3737 C CA . ALA A 1 483 ? -15.930 20.889 24.528 1.00 13.97 ? 483 ALA A CA 1 ATOM 3738 C C . ALA A 1 483 ? -15.239 19.631 24.009 1.00 14.30 ? 483 ALA A C 1 ATOM 3739 O O . ALA A 1 483 ? -14.836 18.775 24.801 1.00 16.52 ? 483 ALA A O 1 ATOM 3740 C CB . ALA A 1 483 ? -14.910 21.815 25.154 1.00 13.16 ? 483 ALA A CB 1 ATOM 3741 N N . GLY A 1 484 ? -15.245 19.473 22.684 1.00 13.91 ? 484 GLY A N 1 ATOM 3742 C CA . GLY A 1 484 ? -14.613 18.335 22.027 1.00 12.89 ? 484 GLY A CA 1 ATOM 3743 C C . GLY A 1 484 ? -15.280 16.988 22.177 1.00 12.84 ? 484 GLY A C 1 ATOM 3744 O O . GLY A 1 484 ? -14.805 16.000 21.618 1.00 12.74 ? 484 GLY A O 1 ATOM 3745 N N . GLY A 1 485 ? -16.396 16.958 22.900 1.00 12.33 ? 485 GLY A N 1 ATOM 3746 C CA . GLY A 1 485 ? -17.085 15.709 23.132 1.00 12.45 ? 485 GLY A CA 1 ATOM 3747 C C . GLY A 1 485 ? -18.406 15.524 22.427 1.00 12.42 ? 485 GLY A C 1 ATOM 3748 O O . GLY A 1 485 ? -18.560 15.851 21.246 1.00 12.08 ? 485 GLY A O 1 ATOM 3749 N N . TRP A 1 486 ? -19.351 14.952 23.165 1.00 13.03 ? 486 TRP A N 1 ATOM 3750 C CA . TRP A 1 486 ? -20.684 14.677 22.653 1.00 12.43 ? 486 TRP A CA 1 ATOM 3751 C C . TRP A 1 486 ? -21.738 14.810 23.741 1.00 12.75 ? 486 TRP A C 1 ATOM 3752 O O . TRP A 1 486 ? -21.412 14.882 24.928 1.00 12.00 ? 486 TRP A O 1 ATOM 3753 C CB . TRP A 1 486 ? -20.755 13.283 21.976 1.00 12.36 ? 486 TRP A CB 1 ATOM 3754 C CG . TRP A 1 486 ? -20.297 12.122 22.827 1.00 14.30 ? 486 TRP A CG 1 ATOM 3755 C CD1 . TRP A 1 486 ? -19.030 11.623 22.905 1.00 15.40 ? 486 TRP A CD1 1 ATOM 3756 C CD2 . TRP A 1 486 ? -21.082 11.376 23.772 1.00 14.07 ? 486 TRP A CD2 1 ATOM 3757 N NE1 . TRP A 1 486 ? -18.965 10.628 23.855 1.00 14.97 ? 486 TRP A NE1 1 ATOM 3758 C CE2 . TRP A 1 486 ? -20.208 10.455 24.404 1.00 15.42 ? 486 TRP A CE2 1 ATOM 3759 C CE3 . TRP A 1 486 ? -22.442 11.398 24.158 1.00 15.16 ? 486 TRP A CE3 1 ATOM 3760 C CZ2 . TRP A 1 486 ? -20.645 9.566 25.411 1.00 13.86 ? 486 TRP A CZ2 1 ATOM 3761 C CZ3 . TRP A 1 486 ? -22.883 10.505 25.164 1.00 14.15 ? 486 TRP A CZ3 1 ATOM 3762 C CH2 . TRP A 1 486 ? -21.977 9.603 25.778 1.00 12.59 ? 486 TRP A CH2 1 ATOM 3763 N N . LEU A 1 487 ? -22.999 14.747 23.323 1.00 12.99 ? 487 LEU A N 1 ATOM 3764 C CA . LEU A 1 487 ? -24.147 14.864 24.216 1.00 13.49 ? 487 LEU A CA 1 ATOM 3765 C C . LEU A 1 487 ? -25.314 14.083 23.619 1.00 13.04 ? 487 LEU A C 1 ATOM 3766 O O . LEU A 1 487 ? -25.622 14.236 22.436 1.00 12.59 ? 487 LEU A O 1 ATOM 3767 C CB . LEU A 1 487 ? -24.528 16.343 24.363 1.00 13.53 ? 487 LEU A CB 1 ATOM 3768 C CG . LEU A 1 487 ? -25.730 16.788 25.189 1.00 12.65 ? 487 LEU A CG 1 ATOM 3769 C CD1 . LEU A 1 487 ? -25.491 16.555 26.678 1.00 14.07 ? 487 LEU A CD1 1 ATOM 3770 C CD2 . LEU A 1 487 ? -25.998 18.260 24.900 1.00 13.39 ? 487 LEU A CD2 1 ATOM 3771 N N . LEU A 1 488 ? -25.948 13.247 24.438 1.00 11.31 ? 488 LEU A N 1 ATOM 3772 C CA . LEU A 1 488 ? -27.093 12.464 23.990 1.00 12.28 ? 488 LEU A CA 1 ATOM 3773 C C . LEU A 1 488 ? -28.366 12.931 24.689 1.00 11.97 ? 488 LEU A C 1 ATOM 3774 O O . LEU A 1 488 ? -28.476 12.874 25.921 1.00 10.55 ? 488 LEU A O 1 ATOM 3775 C CB . LEU A 1 488 ? -26.873 10.957 24.201 1.00 11.20 ? 488 LEU A CB 1 ATOM 3776 C CG . LEU A 1 488 ? -27.961 10.044 23.596 1.00 13.49 ? 488 LEU A CG 1 ATOM 3777 C CD1 . LEU A 1 488 ? -28.016 10.165 22.094 1.00 9.48 ? 488 LEU A CD1 1 ATOM 3778 C CD2 . LEU A 1 488 ? -27.714 8.613 23.964 1.00 12.30 ? 488 LEU A CD2 1 ATOM 3779 N N . LEU A 1 489 ? -29.294 13.454 23.885 1.00 9.56 ? 489 LEU A N 1 ATOM 3780 C CA . LEU A 1 489 ? -30.573 13.954 24.373 1.00 10.72 ? 489 LEU A CA 1 ATOM 3781 C C . LEU A 1 489 ? -31.749 13.180 23.807 1.00 12.06 ? 489 LEU A C 1 ATOM 3782 O O . LEU A 1 489 ? -31.627 12.491 22.792 1.00 11.16 ? 489 LEU A O 1 ATOM 3783 C CB . LEU A 1 489 ? -30.756 15.441 24.023 1.00 10.90 ? 489 LEU A CB 1 ATOM 3784 C CG . LEU A 1 489 ? -29.693 16.444 24.476 1.00 12.44 ? 489 LEU A CG 1 ATOM 3785 C CD1 . LEU A 1 489 ? -30.048 17.842 24.012 1.00 11.52 ? 489 LEU A CD1 1 ATOM 3786 C CD2 . LEU A 1 489 ? -29.509 16.407 25.983 1.00 9.98 ? 489 LEU A CD2 1 ATOM 3787 N N . ALA A 1 490 ? -32.886 13.290 24.487 1.00 11.96 ? 490 ALA A N 1 ATOM 3788 C CA . ALA A 1 490 ? -34.111 12.646 24.047 1.00 11.60 ? 490 ALA A CA 1 ATOM 3789 C C . ALA A 1 490 ? -35.305 13.507 24.395 1.00 12.55 ? 490 ALA A C 1 ATOM 3790 O O . ALA A 1 490 ? -35.329 14.133 25.451 1.00 11.56 ? 490 ALA A O 1 ATOM 3791 C CB . ALA A 1 490 ? -34.265 11.267 24.673 1.00 12.35 ? 490 ALA A CB 1 ATOM 3792 N N . PHE A 1 491 ? -36.245 13.608 23.459 1.00 11.23 ? 491 PHE A N 1 ATOM 3793 C CA . PHE A 1 491 ? -37.481 14.346 23.687 1.00 12.68 ? 491 PHE A CA 1 ATOM 3794 C C . PHE A 1 491 ? -38.629 13.598 23.028 1.00 12.41 ? 491 PHE A C 1 ATOM 3795 O O . PHE A 1 491 ? -38.451 12.975 21.977 1.00 11.52 ? 491 PHE A O 1 ATOM 3796 C CB . PHE A 1 491 ? -37.399 15.841 23.270 1.00 10.22 ? 491 PHE A CB 1 ATOM 3797 C CG . PHE A 1 491 ? -37.404 16.103 21.776 1.00 12.76 ? 491 PHE A CG 1 ATOM 3798 C CD1 . PHE A 1 491 ? -36.199 16.200 21.061 1.00 12.05 ? 491 PHE A CD1 1 ATOM 3799 C CD2 . PHE A 1 491 ? -38.617 16.344 21.094 1.00 10.51 ? 491 PHE A CD2 1 ATOM 3800 C CE1 . PHE A 1 491 ? -36.198 16.541 19.681 1.00 11.12 ? 491 PHE A CE1 1 ATOM 3801 C CE2 . PHE A 1 491 ? -38.633 16.682 19.722 1.00 11.36 ? 491 PHE A CE2 1 ATOM 3802 C CZ . PHE A 1 491 ? -37.417 16.782 19.013 1.00 13.47 ? 491 PHE A CZ 1 ATOM 3803 N N . ARG A 1 492 ? -39.787 13.630 23.682 1.00 13.98 ? 492 ARG A N 1 ATOM 3804 C CA . ARG A 1 492 ? -40.986 12.968 23.185 1.00 15.65 ? 492 ARG A CA 1 ATOM 3805 C C . ARG A 1 492 ? -41.701 13.913 22.239 1.00 13.34 ? 492 ARG A C 1 ATOM 3806 O O . ARG A 1 492 ? -41.898 15.086 22.556 1.00 14.12 ? 492 ARG A O 1 ATOM 3807 C CB . ARG A 1 492 ? -41.897 12.555 24.346 1.00 18.33 ? 492 ARG A CB 1 ATOM 3808 C CG . ARG A 1 492 ? -42.929 11.506 23.973 1.00 24.08 ? 492 ARG A CG 1 ATOM 3809 C CD . ARG A 1 492 ? -43.623 10.935 25.196 1.00 26.87 ? 492 ARG A CD 1 ATOM 3810 N NE . ARG A 1 492 ? -44.547 9.864 24.826 1.00 33.01 ? 492 ARG A NE 1 ATOM 3811 C CZ . ARG A 1 492 ? -44.974 8.903 25.645 1.00 35.03 ? 492 ARG A CZ 1 ATOM 3812 N NH1 . ARG A 1 492 ? -44.567 8.853 26.908 1.00 36.13 ? 492 ARG A NH1 1 ATOM 3813 N NH2 . ARG A 1 492 ? -45.815 7.982 25.194 1.00 37.27 ? 492 ARG A NH2 1 ATOM 3814 N N . THR A 1 493 ? -42.068 13.392 21.073 1.00 12.54 ? 493 THR A N 1 ATOM 3815 C CA . THR A 1 493 ? -42.743 14.169 20.042 1.00 11.91 ? 493 THR A CA 1 ATOM 3816 C C . THR A 1 493 ? -44.232 14.432 20.314 1.00 11.91 ? 493 THR A C 1 ATOM 3817 O O . THR A 1 493 ? -45.103 14.056 19.530 1.00 12.83 ? 493 THR A O 1 ATOM 3818 C CB . THR A 1 493 ? -42.526 13.532 18.659 1.00 12.17 ? 493 THR A CB 1 ATOM 3819 O OG1 . THR A 1 493 ? -42.891 12.147 18.692 1.00 12.28 ? 493 THR A OG1 1 ATOM 3820 C CG2 . THR A 1 493 ? -41.081 13.655 18.251 1.00 11.27 ? 493 THR A CG2 1 ATOM 3821 N N . ASP A 1 494 ? -44.491 15.136 21.413 1.00 11.75 ? 494 ASP A N 1 ATOM 3822 C CA . ASP A 1 494 ? -45.842 15.461 21.879 1.00 14.15 ? 494 ASP A CA 1 ATOM 3823 C C . ASP A 1 494 ? -46.330 16.868 21.529 1.00 12.88 ? 494 ASP A C 1 ATOM 3824 O O . ASP A 1 494 ? -47.387 17.293 21.995 1.00 11.87 ? 494 ASP A O 1 ATOM 3825 C CB . ASP A 1 494 ? -45.905 15.269 23.415 1.00 16.29 ? 494 ASP A CB 1 ATOM 3826 C CG . ASP A 1 494 ? -44.866 16.124 24.190 1.00 20.04 ? 494 ASP A CG 1 ATOM 3827 O OD1 . ASP A 1 494 ? -44.307 17.105 23.640 1.00 16.79 ? 494 ASP A OD1 1 ATOM 3828 O OD2 . ASP A 1 494 ? -44.617 15.813 25.375 1.00 24.37 ? 494 ASP A OD2 1 ATOM 3829 N N . ASN A 1 495 ? -45.582 17.573 20.686 1.00 13.16 ? 495 ASN A N 1 ATOM 3830 C CA . ASN A 1 495 ? -45.919 18.955 20.376 1.00 12.17 ? 495 ASN A CA 1 ATOM 3831 C C . ASN A 1 495 ? -45.602 19.328 18.925 1.00 11.83 ? 495 ASN A C 1 ATOM 3832 O O . ASN A 1 495 ? -44.507 19.820 18.640 1.00 10.36 ? 495 ASN A O 1 ATOM 3833 C CB . ASN A 1 495 ? -45.133 19.839 21.362 1.00 12.63 ? 495 ASN A CB 1 ATOM 3834 C CG . ASN A 1 495 ? -45.601 21.274 21.401 1.00 13.55 ? 495 ASN A CG 1 ATOM 3835 O OD1 . ASN A 1 495 ? -46.622 21.648 20.819 1.00 14.94 ? 495 ASN A OD1 1 ATOM 3836 N ND2 . ASN A 1 495 ? -44.839 22.099 22.103 1.00 10.66 ? 495 ASN A ND2 1 ATOM 3837 N N . PRO A 1 496 ? -46.569 19.136 17.995 1.00 11.30 ? 496 PRO A N 1 ATOM 3838 C CA . PRO A 1 496 ? -46.368 19.463 16.579 1.00 10.82 ? 496 PRO A CA 1 ATOM 3839 C C . PRO A 1 496 ? -45.997 20.926 16.366 1.00 11.43 ? 496 PRO A C 1 ATOM 3840 O O . PRO A 1 496 ? -46.659 21.833 16.891 1.00 12.41 ? 496 PRO A O 1 ATOM 3841 C CB . PRO A 1 496 ? -47.729 19.151 15.962 1.00 12.30 ? 496 PRO A CB 1 ATOM 3842 C CG . PRO A 1 496 ? -48.242 18.070 16.814 1.00 10.65 ? 496 PRO A CG 1 ATOM 3843 C CD . PRO A 1 496 ? -47.909 18.553 18.190 1.00 11.28 ? 496 PRO A CD 1 ATOM 3844 N N . GLY A 1 497 ? -44.897 21.135 15.649 1.00 11.07 ? 497 GLY A N 1 ATOM 3845 C CA . GLY A 1 497 ? -44.434 22.481 15.387 1.00 11.32 ? 497 GLY A CA 1 ATOM 3846 C C . GLY A 1 497 ? -43.023 22.560 14.870 1.00 10.28 ? 497 GLY A C 1 ATOM 3847 O O . GLY A 1 497 ? -42.352 21.544 14.748 1.00 11.66 ? 497 GLY A O 1 ATOM 3848 N N . ALA A 1 498 ? -42.596 23.774 14.528 1.00 10.17 ? 498 ALA A N 1 ATOM 3849 C CA . ALA A 1 498 ? -41.245 24.024 14.040 1.00 9.66 ? 498 ALA A CA 1 ATOM 3850 C C . ALA A 1 498 ? -40.490 24.543 15.261 1.00 9.45 ? 498 ALA A C 1 ATOM 3851 O O . ALA A 1 498 ? -40.771 25.638 15.762 1.00 9.59 ? 498 ALA A O 1 ATOM 3852 C CB . ALA A 1 498 ? -41.269 25.055 12.918 1.00 8.22 ? 498 ALA A CB 1 ATOM 3853 N N . TRP A 1 499 ? -39.585 23.709 15.770 1.00 9.45 ? 499 TRP A N 1 ATOM 3854 C CA . TRP A 1 499 ? -38.818 24.018 16.977 1.00 9.32 ? 499 TRP A CA 1 ATOM 3855 C C . TRP A 1 499 ? -37.315 24.149 16.834 1.00 8.36 ? 499 TRP A C 1 ATOM 3856 O O . TRP A 1 499 ? -36.626 23.197 16.467 1.00 8.57 ? 499 TRP A O 1 ATOM 3857 C CB . TRP A 1 499 ? -39.113 22.977 18.069 1.00 9.18 ? 499 TRP A CB 1 ATOM 3858 C CG . TRP A 1 499 ? -40.571 22.733 18.324 1.00 9.93 ? 499 TRP A CG 1 ATOM 3859 C CD1 . TRP A 1 499 ? -41.272 21.606 18.006 1.00 10.04 ? 499 TRP A CD1 1 ATOM 3860 C CD2 . TRP A 1 499 ? -41.513 23.636 18.924 1.00 9.68 ? 499 TRP A CD2 1 ATOM 3861 N NE1 . TRP A 1 499 ? -42.589 21.744 18.364 1.00 9.75 ? 499 TRP A NE1 1 ATOM 3862 C CE2 . TRP A 1 499 ? -42.771 22.978 18.931 1.00 10.09 ? 499 TRP A CE2 1 ATOM 3863 C CE3 . TRP A 1 499 ? -41.421 24.939 19.464 1.00 8.60 ? 499 TRP A CE3 1 ATOM 3864 C CZ2 . TRP A 1 499 ? -43.936 23.576 19.457 1.00 8.87 ? 499 TRP A CZ2 1 ATOM 3865 C CZ3 . TRP A 1 499 ? -42.585 25.538 19.997 1.00 7.26 ? 499 TRP A CZ3 1 ATOM 3866 C CH2 . TRP A 1 499 ? -43.824 24.848 19.988 1.00 8.67 ? 499 TRP A CH2 1 ATOM 3867 N N . LEU A 1 500 ? -36.803 25.315 17.212 1.00 8.46 ? 500 LEU A N 1 ATOM 3868 C CA . LEU A 1 500 ? -35.372 25.563 17.161 1.00 8.03 ? 500 LEU A CA 1 ATOM 3869 C C . LEU A 1 500 ? -34.625 24.828 18.257 1.00 7.15 ? 500 LEU A C 1 ATOM 3870 O O . LEU A 1 500 ? -35.125 24.666 19.375 1.00 7.10 ? 500 LEU A O 1 ATOM 3871 C CB . LEU A 1 500 ? -35.063 27.054 17.279 1.00 7.62 ? 500 LEU A CB 1 ATOM 3872 C CG . LEU A 1 500 ? -35.425 27.964 16.115 1.00 9.19 ? 500 LEU A CG 1 ATOM 3873 C CD1 . LEU A 1 500 ? -35.105 29.390 16.509 1.00 11.87 ? 500 LEU A CD1 1 ATOM 3874 C CD2 . LEU A 1 500 ? -34.660 27.557 14.857 1.00 8.51 ? 500 LEU A CD2 1 ATOM 3875 N N . PHE A 1 501 ? -33.474 24.292 17.875 1.00 7.46 ? 501 PHE A N 1 ATOM 3876 C CA . PHE A 1 501 ? -32.579 23.602 18.787 1.00 8.77 ? 501 PHE A CA 1 ATOM 3877 C C . PHE A 1 501 ? -31.269 24.281 18.468 1.00 9.07 ? 501 PHE A C 1 ATOM 3878 O O . PHE A 1 501 ? -30.669 24.035 17.420 1.00 9.15 ? 501 PHE A O 1 ATOM 3879 C CB . PHE A 1 501 ? -32.526 22.102 18.507 1.00 8.43 ? 501 PHE A CB 1 ATOM 3880 C CG . PHE A 1 501 ? -31.540 21.347 19.369 1.00 10.94 ? 501 PHE A CG 1 ATOM 3881 C CD1 . PHE A 1 501 ? -31.628 21.379 20.772 1.00 10.79 ? 501 PHE A CD1 1 ATOM 3882 C CD2 . PHE A 1 501 ? -30.509 20.602 18.771 1.00 11.86 ? 501 PHE A CD2 1 ATOM 3883 C CE1 . PHE A 1 501 ? -30.698 20.677 21.580 1.00 11.89 ? 501 PHE A CE1 1 ATOM 3884 C CE2 . PHE A 1 501 ? -29.574 19.897 19.557 1.00 11.46 ? 501 PHE A CE2 1 ATOM 3885 C CZ . PHE A 1 501 ? -29.668 19.934 20.968 1.00 12.05 ? 501 PHE A CZ 1 ATOM 3886 N N . HIS A 1 502 ? -30.833 25.125 19.396 1.00 10.35 ? 502 HIS A N 1 ATOM 3887 C CA . HIS A 1 502 ? -29.638 25.916 19.196 1.00 11.19 ? 502 HIS A CA 1 ATOM 3888 C C . HIS A 1 502 ? -28.771 26.165 20.402 1.00 10.46 ? 502 HIS A C 1 ATOM 3889 O O . HIS A 1 502 ? -29.189 25.961 21.536 1.00 11.16 ? 502 HIS A O 1 ATOM 3890 C CB . HIS A 1 502 ? -30.044 27.283 18.622 1.00 11.09 ? 502 HIS A CB 1 ATOM 3891 C CG . HIS A 1 502 ? -30.933 28.101 19.510 1.00 12.73 ? 502 HIS A CG 1 ATOM 3892 N ND1 . HIS A 1 502 ? -30.442 29.085 20.340 1.00 13.94 ? 502 HIS A ND1 1 ATOM 3893 C CD2 . HIS A 1 502 ? -32.278 28.112 19.669 1.00 12.99 ? 502 HIS A CD2 1 ATOM 3894 C CE1 . HIS A 1 502 ? -31.446 29.668 20.969 1.00 12.41 ? 502 HIS A CE1 1 ATOM 3895 N NE2 . HIS A 1 502 ? -32.572 29.097 20.579 1.00 13.52 ? 502 HIS A NE2 1 ATOM 3896 N N . CYS A 1 503 ? -27.565 26.659 20.127 1.00 10.66 ? 503 CYS A N 1 ATOM 3897 C CA . CYS A 1 503 ? -26.644 27.055 21.176 1.00 9.83 ? 503 CYS A CA 1 ATOM 3898 C C . CYS A 1 503 ? -27.180 28.417 21.605 1.00 9.36 ? 503 CYS A C 1 ATOM 3899 O O . CYS A 1 503 ? -27.530 29.238 20.750 1.00 10.05 ? 503 CYS A O 1 ATOM 3900 C CB . CYS A 1 503 ? -25.230 27.223 20.643 1.00 9.50 ? 503 CYS A CB 1 ATOM 3901 S SG . CYS A 1 503 ? -24.167 27.985 21.870 1.00 11.99 ? 503 CYS A SG 1 ATOM 3902 N N . HIS A 1 504 ? -27.262 28.650 22.912 1.00 10.07 ? 504 HIS A N 1 ATOM 3903 C CA . HIS A 1 504 ? -27.780 29.916 23.398 1.00 10.25 ? 504 HIS A CA 1 ATOM 3904 C C . HIS A 1 504 ? -26.770 31.058 23.476 1.00 9.41 ? 504 HIS A C 1 ATOM 3905 O O . HIS A 1 504 ? -27.116 32.166 23.902 1.00 12.81 ? 504 HIS A O 1 ATOM 3906 C CB . HIS A 1 504 ? -28.545 29.746 24.703 1.00 8.93 ? 504 HIS A CB 1 ATOM 3907 C CG . HIS A 1 504 ? -29.770 30.599 24.781 1.00 11.37 ? 504 HIS A CG 1 ATOM 3908 N ND1 . HIS A 1 504 ? -29.719 31.973 24.884 1.00 9.87 ? 504 HIS A ND1 1 ATOM 3909 C CD2 . HIS A 1 504 ? -31.081 30.274 24.737 1.00 10.07 ? 504 HIS A CD2 1 ATOM 3910 C CE1 . HIS A 1 504 ? -30.949 32.454 24.904 1.00 11.16 ? 504 HIS A CE1 1 ATOM 3911 N NE2 . HIS A 1 504 ? -31.796 31.444 24.821 1.00 13.29 ? 504 HIS A NE2 1 ATOM 3912 N N . ILE A 1 505 ? -25.523 30.793 23.084 1.00 9.27 ? 505 ILE A N 1 ATOM 3913 C CA . ILE A 1 505 ? -24.519 31.861 23.028 1.00 8.72 ? 505 ILE A CA 1 ATOM 3914 C C . ILE A 1 505 ? -24.948 32.628 21.781 1.00 8.85 ? 505 ILE A C 1 ATOM 3915 O O . ILE A 1 505 ? -24.987 32.064 20.685 1.00 9.03 ? 505 ILE A O 1 ATOM 3916 C CB . ILE A 1 505 ? -23.061 31.341 22.889 1.00 9.62 ? 505 ILE A CB 1 ATOM 3917 C CG1 . ILE A 1 505 ? -22.597 30.752 24.221 1.00 8.73 ? 505 ILE A CG1 1 ATOM 3918 C CG2 . ILE A 1 505 ? -22.101 32.486 22.477 1.00 5.99 ? 505 ILE A CG2 1 ATOM 3919 C CD1 . ILE A 1 505 ? -21.254 30.015 24.174 1.00 8.37 ? 505 ILE A CD1 1 ATOM 3920 N N . ALA A 1 506 ? -25.361 33.880 21.991 1.00 10.96 ? 506 ALA A N 1 ATOM 3921 C CA . ALA A 1 506 ? -25.850 34.757 20.926 1.00 10.16 ? 506 ALA A CA 1 ATOM 3922 C C . ALA A 1 506 ? -24.976 34.796 19.686 1.00 9.68 ? 506 ALA A C 1 ATOM 3923 O O . ALA A 1 506 ? -25.471 34.624 18.577 1.00 11.44 ? 506 ALA A O 1 ATOM 3924 C CB . ALA A 1 506 ? -26.082 36.161 21.456 1.00 8.44 ? 506 ALA A CB 1 ATOM 3925 N N . TRP A 1 507 ? -23.666 34.875 19.903 1.00 11.86 ? 507 TRP A N 1 ATOM 3926 C CA . TRP A 1 507 ? -22.679 34.933 18.829 1.00 10.76 ? 507 TRP A CA 1 ATOM 3927 C C . TRP A 1 507 ? -22.639 33.665 17.990 1.00 10.95 ? 507 TRP A C 1 ATOM 3928 O O . TRP A 1 507 ? -22.425 33.728 16.778 1.00 10.33 ? 507 TRP A O 1 ATOM 3929 C CB . TRP A 1 507 ? -21.287 35.230 19.398 1.00 11.38 ? 507 TRP A CB 1 ATOM 3930 C CG . TRP A 1 507 ? -21.193 36.147 20.642 1.00 12.27 ? 507 TRP A CG 1 ATOM 3931 C CD1 . TRP A 1 507 ? -20.360 35.952 21.709 1.00 11.84 ? 507 TRP A CD1 1 ATOM 3932 C CD2 . TRP A 1 507 ? -21.953 37.341 20.948 1.00 11.28 ? 507 TRP A CD2 1 ATOM 3933 N NE1 . TRP A 1 507 ? -20.551 36.925 22.659 1.00 13.21 ? 507 TRP A NE1 1 ATOM 3934 C CE2 . TRP A 1 507 ? -21.522 37.789 22.229 1.00 12.52 ? 507 TRP A CE2 1 ATOM 3935 C CE3 . TRP A 1 507 ? -22.965 38.073 20.278 1.00 10.89 ? 507 TRP A CE3 1 ATOM 3936 C CZ2 . TRP A 1 507 ? -22.069 38.929 22.860 1.00 13.07 ? 507 TRP A CZ2 1 ATOM 3937 C CZ3 . TRP A 1 507 ? -23.516 39.207 20.906 1.00 11.71 ? 507 TRP A CZ3 1 ATOM 3938 C CH2 . TRP A 1 507 ? -23.062 39.620 22.190 1.00 11.41 ? 507 TRP A CH2 1 ATOM 3939 N N . HIS A 1 508 ? -22.921 32.530 18.632 1.00 10.36 ? 508 HIS A N 1 ATOM 3940 C CA . HIS A 1 508 ? -22.929 31.235 17.954 1.00 10.81 ? 508 HIS A CA 1 ATOM 3941 C C . HIS A 1 508 ? -24.199 30.975 17.154 1.00 10.04 ? 508 HIS A C 1 ATOM 3942 O O . HIS A 1 508 ? -24.114 30.475 16.030 1.00 11.44 ? 508 HIS A O 1 ATOM 3943 C CB . HIS A 1 508 ? -22.657 30.090 18.936 1.00 9.65 ? 508 HIS A CB 1 ATOM 3944 C CG . HIS A 1 508 ? -21.305 30.153 19.584 1.00 10.03 ? 508 HIS A CG 1 ATOM 3945 N ND1 . HIS A 1 508 ? -20.929 29.298 20.597 1.00 10.24 ? 508 HIS A ND1 1 ATOM 3946 C CD2 . HIS A 1 508 ? -20.256 30.989 19.389 1.00 11.89 ? 508 HIS A CD2 1 ATOM 3947 C CE1 . HIS A 1 508 ? -19.708 29.611 20.999 1.00 11.70 ? 508 HIS A CE1 1 ATOM 3948 N NE2 . HIS A 1 508 ? -19.279 30.632 20.283 1.00 10.66 ? 508 HIS A NE2 1 ATOM 3949 N N . VAL A 1 509 ? -25.364 31.327 17.712 1.00 10.08 ? 509 VAL A N 1 ATOM 3950 C CA . VAL A 1 509 ? -26.639 31.142 17.001 1.00 10.97 ? 509 VAL A CA 1 ATOM 3951 C C . VAL A 1 509 ? -26.738 32.149 15.851 1.00 10.59 ? 509 VAL A C 1 ATOM 3952 O O . VAL A 1 509 ? -27.290 31.837 14.792 1.00 9.01 ? 509 VAL A O 1 ATOM 3953 C CB . VAL A 1 509 ? -27.895 31.150 17.947 1.00 9.97 ? 509 VAL A CB 1 ATOM 3954 C CG1 . VAL A 1 509 ? -28.109 32.497 18.630 1.00 12.14 ? 509 VAL A CG1 1 ATOM 3955 C CG2 . VAL A 1 509 ? -29.140 30.714 17.179 1.00 10.09 ? 509 VAL A CG2 1 ATOM 3956 N N . SER A 1 510 ? -26.117 33.317 16.043 1.00 11.59 ? 510 SER A N 1 ATOM 3957 C CA . SER A 1 510 ? -26.039 34.358 15.012 1.00 11.70 ? 510 SER A CA 1 ATOM 3958 C C . SER A 1 510 ? -25.139 33.801 13.907 1.00 11.08 ? 510 SER A C 1 ATOM 3959 O O . SER A 1 510 ? -25.420 33.967 12.717 1.00 10.77 ? 510 SER A O 1 ATOM 3960 C CB . SER A 1 510 ? -25.399 35.637 15.561 1.00 10.89 ? 510 SER A CB 1 ATOM 3961 O OG . SER A 1 510 ? -26.296 36.356 16.377 1.00 15.83 ? 510 SER A OG 1 ATOM 3962 N N . GLY A 1 511 ? -24.098 33.082 14.341 1.00 10.64 ? 511 GLY A N 1 ATOM 3963 C CA . GLY A 1 511 ? -23.135 32.456 13.445 1.00 10.58 ? 511 GLY A CA 1 ATOM 3964 C C . GLY A 1 511 ? -23.643 31.203 12.753 1.00 11.77 ? 511 GLY A C 1 ATOM 3965 O O . GLY A 1 511 ? -22.912 30.592 11.968 1.00 12.02 ? 511 GLY A O 1 ATOM 3966 N N . GLY A 1 512 ? -24.868 30.793 13.095 1.00 10.75 ? 512 GLY A N 1 ATOM 3967 C CA . GLY A 1 512 ? -25.486 29.640 12.468 1.00 10.17 ? 512 GLY A CA 1 ATOM 3968 C C . GLY A 1 512 ? -25.676 28.347 13.236 1.00 11.05 ? 512 GLY A C 1 ATOM 3969 O O . GLY A 1 512 ? -26.224 27.400 12.668 1.00 10.34 ? 512 GLY A O 1 ATOM 3970 N N . LEU A 1 513 ? -25.266 28.299 14.506 1.00 9.10 ? 513 LEU A N 1 ATOM 3971 C CA . LEU A 1 513 ? -25.394 27.082 15.313 1.00 10.28 ? 513 LEU A CA 1 ATOM 3972 C C . LEU A 1 513 ? -26.817 26.793 15.762 1.00 9.93 ? 513 LEU A C 1 ATOM 3973 O O . LEU A 1 513 ? -27.203 27.108 16.897 1.00 9.34 ? 513 LEU A O 1 ATOM 3974 C CB . LEU A 1 513 ? -24.460 27.111 16.529 1.00 8.25 ? 513 LEU A CB 1 ATOM 3975 C CG . LEU A 1 513 ? -23.784 25.786 16.924 1.00 9.38 ? 513 LEU A CG 1 ATOM 3976 C CD1 . LEU A 1 513 ? -22.692 26.104 17.918 1.00 8.53 ? 513 LEU A CD1 1 ATOM 3977 C CD2 . LEU A 1 513 ? -24.733 24.738 17.502 1.00 6.36 ? 513 LEU A CD2 1 ATOM 3978 N N . SER A 1 514 ? -27.555 26.127 14.876 1.00 10.52 ? 514 SER A N 1 ATOM 3979 C CA . SER A 1 514 ? -28.940 25.746 15.119 1.00 9.76 ? 514 SER A CA 1 ATOM 3980 C C . SER A 1 514 ? -29.487 24.826 14.055 1.00 10.57 ? 514 SER A C 1 ATOM 3981 O O . SER A 1 514 ? -28.950 24.732 12.950 1.00 9.75 ? 514 SER A O 1 ATOM 3982 C CB . SER A 1 514 ? -29.848 26.988 15.151 1.00 11.09 ? 514 SER A CB 1 ATOM 3983 O OG . SER A 1 514 ? -31.200 26.660 15.445 1.00 9.88 ? 514 SER A OG 1 ATOM 3984 N N . VAL A 1 515 ? -30.523 24.095 14.452 1.00 10.37 ? 515 VAL A N 1 ATOM 3985 C CA . VAL A 1 515 ? -31.292 23.248 13.560 1.00 12.38 ? 515 VAL A CA 1 ATOM 3986 C C . VAL A 1 515 ? -32.730 23.600 13.886 1.00 12.10 ? 515 VAL A C 1 ATOM 3987 O O . VAL A 1 515 ? -33.001 24.304 14.868 1.00 12.89 ? 515 VAL A O 1 ATOM 3988 C CB . VAL A 1 515 ? -31.065 21.706 13.706 1.00 11.18 ? 515 VAL A CB 1 ATOM 3989 C CG1 . VAL A 1 515 ? -29.729 21.310 13.138 1.00 12.81 ? 515 VAL A CG1 1 ATOM 3990 C CG2 . VAL A 1 515 ? -31.233 21.231 15.128 1.00 13.04 ? 515 VAL A CG2 1 ATOM 3991 N N . ASP A 1 516 ? -33.642 23.135 13.049 1.00 12.48 ? 516 ASP A N 1 ATOM 3992 C CA . ASP A 1 516 ? -35.052 23.389 13.256 1.00 12.36 ? 516 ASP A CA 1 ATOM 3993 C C . ASP A 1 516 ? -35.757 22.046 13.182 1.00 11.62 ? 516 ASP A C 1 ATOM 3994 O O . ASP A 1 516 ? -35.846 21.438 12.114 1.00 12.81 ? 516 ASP A O 1 ATOM 3995 C CB . ASP A 1 516 ? -35.567 24.359 12.182 1.00 12.31 ? 516 ASP A CB 1 ATOM 3996 C CG . ASP A 1 516 ? -37.024 24.787 12.391 1.00 12.66 ? 516 ASP A CG 1 ATOM 3997 O OD1 . ASP A 1 516 ? -37.757 24.180 13.207 1.00 12.05 ? 516 ASP A OD1 1 ATOM 3998 O OD2 . ASP A 1 516 ? -37.441 25.740 11.700 1.00 13.59 ? 516 ASP A OD2 1 ATOM 3999 N N . PHE A 1 517 ? -36.240 21.586 14.333 1.00 10.77 ? 517 PHE A N 1 ATOM 4000 C CA . PHE A 1 517 ? -36.969 20.331 14.407 1.00 10.12 ? 517 PHE A CA 1 ATOM 4001 C C . PHE A 1 517 ? -38.393 20.564 13.917 1.00 9.98 ? 517 PHE A C 1 ATOM 4002 O O . PHE A 1 517 ? -39.188 21.212 14.600 1.00 10.24 ? 517 PHE A O 1 ATOM 4003 C CB . PHE A 1 517 ? -37.015 19.789 15.848 1.00 9.90 ? 517 PHE A CB 1 ATOM 4004 C CG . PHE A 1 517 ? -35.746 19.122 16.300 1.00 11.75 ? 517 PHE A CG 1 ATOM 4005 C CD1 . PHE A 1 517 ? -35.202 18.041 15.582 1.00 11.53 ? 517 PHE A CD1 1 ATOM 4006 C CD2 . PHE A 1 517 ? -35.093 19.557 17.459 1.00 11.45 ? 517 PHE A CD2 1 ATOM 4007 C CE1 . PHE A 1 517 ? -34.015 17.400 16.015 1.00 11.65 ? 517 PHE A CE1 1 ATOM 4008 C CE2 . PHE A 1 517 ? -33.898 18.918 17.910 1.00 10.63 ? 517 PHE A CE2 1 ATOM 4009 C CZ . PHE A 1 517 ? -33.362 17.841 17.184 1.00 10.96 ? 517 PHE A CZ 1 ATOM 4010 N N . LEU A 1 518 ? -38.679 20.123 12.693 1.00 10.75 ? 518 LEU A N 1 ATOM 4011 C CA . LEU A 1 518 ? -40.025 20.242 12.153 1.00 10.84 ? 518 LEU A CA 1 ATOM 4012 C C . LEU A 1 518 ? -40.735 18.975 12.616 1.00 11.76 ? 518 LEU A C 1 ATOM 4013 O O . LEU A 1 518 ? -40.649 17.906 12.003 1.00 10.36 ? 518 LEU A O 1 ATOM 4014 C CB . LEU A 1 518 ? -40.029 20.378 10.632 1.00 10.35 ? 518 LEU A CB 1 ATOM 4015 C CG . LEU A 1 518 ? -41.407 20.634 10.011 1.00 11.55 ? 518 LEU A CG 1 ATOM 4016 C CD1 . LEU A 1 518 ? -42.035 21.939 10.483 1.00 12.86 ? 518 LEU A CD1 1 ATOM 4017 C CD2 . LEU A 1 518 ? -41.266 20.618 8.528 1.00 11.74 ? 518 LEU A CD2 1 ATOM 4018 N N . GLU A 1 519 ? -41.393 19.125 13.755 1.00 12.82 ? 519 GLU A N 1 ATOM 4019 C CA . GLU A 1 519 ? -42.093 18.044 14.419 1.00 13.70 ? 519 GLU A CA 1 ATOM 4020 C C . GLU A 1 519 ? -43.512 17.858 13.938 1.00 12.90 ? 519 GLU A C 1 ATOM 4021 O O . GLU A 1 519 ? -44.330 18.775 14.028 1.00 12.71 ? 519 GLU A O 1 ATOM 4022 C CB . GLU A 1 519 ? -42.087 18.328 15.908 1.00 13.51 ? 519 GLU A CB 1 ATOM 4023 C CG . GLU A 1 519 ? -42.544 17.205 16.783 1.00 15.23 ? 519 GLU A CG 1 ATOM 4024 C CD . GLU A 1 519 ? -42.430 17.574 18.233 1.00 16.18 ? 519 GLU A CD 1 ATOM 4025 O OE1 . GLU A 1 519 ? -41.507 18.333 18.589 1.00 15.94 ? 519 GLU A OE1 1 ATOM 4026 O OE2 . GLU A 1 519 ? -43.280 17.130 19.023 1.00 15.86 ? 519 GLU A OE2 1 ATOM 4027 N N . ARG A 1 520 ? -43.786 16.648 13.439 1.00 14.61 ? 520 ARG A N 1 ATOM 4028 C CA . ARG A 1 520 ? -45.105 16.235 12.936 1.00 15.04 ? 520 ARG A CA 1 ATOM 4029 C C . ARG A 1 520 ? -45.795 17.315 12.083 1.00 15.94 ? 520 ARG A C 1 ATOM 4030 O O . ARG A 1 520 ? -46.860 17.815 12.463 1.00 16.02 ? 520 ARG A O 1 ATOM 4031 C CB . ARG A 1 520 ? -45.992 15.827 14.118 1.00 14.16 ? 520 ARG A CB 1 ATOM 4032 C CG . ARG A 1 520 ? -45.442 14.674 14.936 1.00 15.42 ? 520 ARG A CG 1 ATOM 4033 C CD . ARG A 1 520 ? -46.052 14.647 16.320 1.00 16.04 ? 520 ARG A CD 1 ATOM 4034 N NE . ARG A 1 520 ? -47.506 14.489 16.293 1.00 15.29 ? 520 ARG A NE 1 ATOM 4035 C CZ . ARG A 1 520 ? -48.286 14.496 17.371 1.00 17.46 ? 520 ARG A CZ 1 ATOM 4036 N NH1 . ARG A 1 520 ? -47.763 14.650 18.581 1.00 15.96 ? 520 ARG A NH1 1 ATOM 4037 N NH2 . ARG A 1 520 ? -49.601 14.382 17.233 1.00 17.55 ? 520 ARG A NH2 1 ATOM 4038 N N . PRO A 1 521 ? -45.188 17.697 10.929 1.00 16.86 ? 521 PRO A N 1 ATOM 4039 C CA . PRO A 1 521 ? -45.760 18.729 10.051 1.00 18.44 ? 521 PRO A CA 1 ATOM 4040 C C . PRO A 1 521 ? -47.206 18.550 9.606 1.00 20.27 ? 521 PRO A C 1 ATOM 4041 O O . PRO A 1 521 ? -47.945 19.534 9.517 1.00 21.45 ? 521 PRO A O 1 ATOM 4042 C CB . PRO A 1 521 ? -44.790 18.755 8.867 1.00 17.40 ? 521 PRO A CB 1 ATOM 4043 C CG . PRO A 1 521 ? -44.204 17.407 8.854 1.00 19.59 ? 521 PRO A CG 1 ATOM 4044 C CD . PRO A 1 521 ? -43.965 17.145 10.310 1.00 16.91 ? 521 PRO A CD 1 ATOM 4045 N N . ALA A 1 522 ? -47.611 17.295 9.396 1.00 22.92 ? 522 ALA A N 1 ATOM 4046 C CA . ALA A 1 522 ? -48.973 16.946 8.975 1.00 24.27 ? 522 ALA A CA 1 ATOM 4047 C C . ALA A 1 522 ? -50.002 17.286 10.055 1.00 23.95 ? 522 ALA A C 1 ATOM 4048 O O . ALA A 1 522 ? -51.097 17.766 9.751 1.00 26.55 ? 522 ALA A O 1 ATOM 4049 C CB . ALA A 1 522 ? -49.049 15.462 8.615 1.00 24.28 ? 522 ALA A CB 1 ATOM 4050 N N . ASP A 1 523 ? -49.614 17.087 11.314 1.00 22.57 ? 523 ASP A N 1 ATOM 4051 C CA . ASP A 1 523 ? -50.471 17.372 12.466 1.00 22.84 ? 523 ASP A CA 1 ATOM 4052 C C . ASP A 1 523 ? -50.513 18.863 12.785 1.00 22.11 ? 523 ASP A C 1 ATOM 4053 O O . ASP A 1 523 ? -51.535 19.370 13.241 1.00 21.73 ? 523 ASP A O 1 ATOM 4054 C CB . ASP A 1 523 ? -49.993 16.602 13.702 1.00 23.42 ? 523 ASP A CB 1 ATOM 4055 C CG . ASP A 1 523 ? -50.161 15.096 13.567 1.00 25.57 ? 523 ASP A CG 1 ATOM 4056 O OD1 . ASP A 1 523 ? -51.135 14.655 12.924 1.00 26.26 ? 523 ASP A OD1 1 ATOM 4057 O OD2 . ASP A 1 523 ? -49.326 14.351 14.121 1.00 23.21 ? 523 ASP A OD2 1 ATOM 4058 N N . LEU A 1 524 ? -49.407 19.556 12.504 1.00 22.58 ? 524 LEU A N 1 ATOM 4059 C CA . LEU A 1 524 ? -49.267 20.995 12.753 1.00 22.17 ? 524 LEU A CA 1 ATOM 4060 C C . LEU A 1 524 ? -50.254 21.864 11.974 1.00 22.91 ? 524 LEU A C 1 ATOM 4061 O O . LEU A 1 524 ? -50.864 22.758 12.558 1.00 22.07 ? 524 LEU A O 1 ATOM 4062 C CB . LEU A 1 524 ? -47.818 21.441 12.491 1.00 20.25 ? 524 LEU A CB 1 ATOM 4063 C CG . LEU A 1 524 ? -47.403 22.921 12.485 1.00 19.48 ? 524 LEU A CG 1 ATOM 4064 C CD1 . LEU A 1 524 ? -47.626 23.595 13.844 1.00 17.14 ? 524 LEU A CD1 1 ATOM 4065 C CD2 . LEU A 1 524 ? -45.957 23.008 12.057 1.00 17.62 ? 524 LEU A CD2 1 ATOM 4066 N N . ARG A 1 525 ? -50.449 21.558 10.690 1.00 25.04 ? 525 ARG A N 1 ATOM 4067 C CA . ARG A 1 525 ? -51.364 22.315 9.832 1.00 28.17 ? 525 ARG A CA 1 ATOM 4068 C C . ARG A 1 525 ? -52.817 22.258 10.321 1.00 27.86 ? 525 ARG A C 1 ATOM 4069 O O . ARG A 1 525 ? -53.521 23.273 10.295 1.00 28.64 ? 525 ARG A O 1 ATOM 4070 C CB . ARG A 1 525 ? -51.263 21.832 8.383 1.00 31.22 ? 525 ARG A CB 1 ATOM 4071 C CG . ARG A 1 525 ? -51.749 22.851 7.360 1.00 35.59 ? 525 ARG A CG 1 ATOM 4072 C CD . ARG A 1 525 ? -51.659 22.305 5.954 1.00 40.78 ? 525 ARG A CD 1 ATOM 4073 N NE . ARG A 1 525 ? -52.060 23.300 4.959 1.00 44.80 ? 525 ARG A NE 1 ATOM 4074 C CZ . ARG A 1 525 ? -51.843 23.191 3.649 1.00 47.10 ? 525 ARG A CZ 1 ATOM 4075 N NH1 . ARG A 1 525 ? -51.222 22.124 3.152 1.00 46.34 ? 525 ARG A NH1 1 ATOM 4076 N NH2 . ARG A 1 525 ? -52.250 24.154 2.829 1.00 47.79 ? 525 ARG A NH2 1 ATOM 4077 N N . GLN A 1 526 ? -53.219 21.093 10.836 1.00 28.11 ? 526 GLN A N 1 ATOM 4078 C CA . GLN A 1 526 ? -54.569 20.864 11.368 1.00 29.03 ? 526 GLN A CA 1 ATOM 4079 C C . GLN A 1 526 ? -54.824 21.628 12.670 1.00 27.83 ? 526 GLN A C 1 ATOM 4080 O O . GLN A 1 526 ? -55.952 22.051 12.940 1.00 27.11 ? 526 GLN A O 1 ATOM 4081 C CB . GLN A 1 526 ? -54.795 19.377 11.657 1.00 31.45 ? 526 GLN A CB 1 ATOM 4082 C CG . GLN A 1 526 ? -54.869 18.455 10.453 1.00 37.22 ? 526 GLN A CG 1 ATOM 4083 C CD . GLN A 1 526 ? -55.377 17.066 10.834 1.00 39.47 ? 526 GLN A CD 1 ATOM 4084 O OE1 . GLN A 1 526 ? -54.650 16.261 11.422 1.00 39.82 ? 526 GLN A OE1 1 ATOM 4085 N NE2 . GLN A 1 526 ? -56.640 16.791 10.516 1.00 40.66 ? 526 GLN A NE2 1 ATOM 4086 N N . ARG A 1 527 ? -53.762 21.807 13.458 1.00 26.20 ? 527 ARG A N 1 ATOM 4087 C CA . ARG A 1 527 ? -53.833 22.485 14.754 1.00 25.51 ? 527 ARG A CA 1 ATOM 4088 C C . ARG A 1 527 ? -53.702 24.006 14.761 1.00 24.11 ? 527 ARG A C 1 ATOM 4089 O O . ARG A 1 527 ? -53.913 24.640 15.801 1.00 24.29 ? 527 ARG A O 1 ATOM 4090 C CB . ARG A 1 527 ? -52.831 21.856 15.719 1.00 26.51 ? 527 ARG A CB 1 ATOM 4091 C CG . ARG A 1 527 ? -53.197 20.438 16.077 1.00 28.07 ? 527 ARG A CG 1 ATOM 4092 C CD . ARG A 1 527 ? -52.016 19.658 16.593 1.00 29.15 ? 527 ARG A CD 1 ATOM 4093 N NE . ARG A 1 527 ? -52.172 18.242 16.270 1.00 29.93 ? 527 ARG A NE 1 ATOM 4094 C CZ . ARG A 1 527 ? -52.010 17.238 17.126 1.00 31.46 ? 527 ARG A CZ 1 ATOM 4095 N NH1 . ARG A 1 527 ? -51.677 17.465 18.395 1.00 30.89 ? 527 ARG A NH1 1 ATOM 4096 N NH2 . ARG A 1 527 ? -52.208 15.995 16.708 1.00 31.30 ? 527 ARG A NH2 1 ATOM 4097 N N . ILE A 1 528 ? -53.371 24.590 13.610 1.00 22.24 ? 528 ILE A N 1 ATOM 4098 C CA . ILE A 1 528 ? -53.243 26.044 13.500 1.00 20.81 ? 528 ILE A CA 1 ATOM 4099 C C . ILE A 1 528 ? -54.636 26.663 13.334 1.00 21.67 ? 528 ILE A C 1 ATOM 4100 O O . ILE A 1 528 ? -55.326 26.423 12.332 1.00 20.15 ? 528 ILE A O 1 ATOM 4101 C CB . ILE A 1 528 ? -52.298 26.465 12.329 1.00 19.29 ? 528 ILE A CB 1 ATOM 4102 C CG1 . ILE A 1 528 ? -50.878 25.946 12.590 1.00 16.29 ? 528 ILE A CG1 1 ATOM 4103 C CG2 . ILE A 1 528 ? -52.255 28.010 12.189 1.00 17.92 ? 528 ILE A CG2 1 ATOM 4104 C CD1 . ILE A 1 528 ? -49.922 26.077 11.412 1.00 13.95 ? 528 ILE A CD1 1 ATOM 4105 N N . SER A 1 529 ? -55.032 27.452 14.335 1.00 21.68 ? 529 SER A N 1 ATOM 4106 C CA . SER A 1 529 ? -56.329 28.132 14.358 1.00 22.59 ? 529 SER A CA 1 ATOM 4107 C C . SER A 1 529 ? -56.392 29.243 13.312 1.00 22.52 ? 529 SER A C 1 ATOM 4108 O O . SER A 1 529 ? -55.353 29.764 12.898 1.00 18.69 ? 529 SER A O 1 ATOM 4109 C CB . SER A 1 529 ? -56.609 28.714 15.751 1.00 23.10 ? 529 SER A CB 1 ATOM 4110 O OG . SER A 1 529 ? -55.739 29.794 16.054 1.00 22.87 ? 529 SER A OG 1 ATOM 4111 N N . GLN A 1 530 ? -57.611 29.614 12.913 1.00 23.46 ? 530 GLN A N 1 ATOM 4112 C CA . GLN A 1 530 ? -57.820 30.661 11.914 1.00 24.72 ? 530 GLN A CA 1 ATOM 4113 C C . GLN A 1 530 ? -57.286 32.011 12.395 1.00 23.07 ? 530 GLN A C 1 ATOM 4114 O O . GLN A 1 530 ? -56.693 32.743 11.607 1.00 21.45 ? 530 GLN A O 1 ATOM 4115 C CB . GLN A 1 530 ? -59.303 30.763 11.517 1.00 25.92 ? 530 GLN A CB 1 ATOM 4116 C CG . GLN A 1 530 ? -59.581 31.536 10.205 1.00 26.69 ? 530 GLN A CG 1 ATOM 4117 C CD . GLN A 1 530 ? -58.947 30.894 8.969 1.00 28.79 ? 530 GLN A CD 1 ATOM 4118 O OE1 . GLN A 1 530 ? -59.257 29.756 8.616 1.00 30.50 ? 530 GLN A OE1 1 ATOM 4119 N NE2 . GLN A 1 530 ? -58.049 31.626 8.315 1.00 28.03 ? 530 GLN A NE2 1 ATOM 4120 N N . GLU A 1 531 ? -57.415 32.276 13.701 1.00 23.08 ? 531 GLU A N 1 ATOM 4121 C CA . GLU A 1 531 ? -56.935 33.520 14.319 1.00 23.31 ? 531 GLU A CA 1 ATOM 4122 C C . GLU A 1 531 ? -55.411 33.594 14.261 1.00 21.35 ? 531 GLU A C 1 ATOM 4123 O O . GLU A 1 531 ? -54.858 34.643 13.934 1.00 21.42 ? 531 GLU A O 1 ATOM 4124 C CB . GLU A 1 531 ? -57.407 33.648 15.777 1.00 26.76 ? 531 GLU A CB 1 ATOM 4125 C CG . GLU A 1 531 ? -58.920 33.803 15.963 1.00 32.91 ? 531 GLU A CG 1 ATOM 4126 C CD . GLU A 1 531 ? -59.634 32.482 16.224 1.00 36.16 ? 531 GLU A CD 1 ATOM 4127 O OE1 . GLU A 1 531 ? -60.109 32.285 17.363 1.00 39.37 ? 531 GLU A OE1 1 ATOM 4128 O OE2 . GLU A 1 531 ? -59.727 31.644 15.298 1.00 37.62 ? 531 GLU A OE2 1 ATOM 4129 N N . ASP A 1 532 ? -54.753 32.458 14.519 1.00 18.27 ? 532 ASP A N 1 ATOM 4130 C CA . ASP A 1 532 ? -53.292 32.368 14.481 1.00 17.38 ? 532 ASP A CA 1 ATOM 4131 C C . ASP A 1 532 ? -52.768 32.482 13.054 1.00 15.58 ? 532 ASP A C 1 ATOM 4132 O O . ASP A 1 532 ? -51.787 33.177 12.817 1.00 14.54 ? 532 ASP A O 1 ATOM 4133 C CB . ASP A 1 532 ? -52.801 31.071 15.134 1.00 17.81 ? 532 ASP A CB 1 ATOM 4134 C CG . ASP A 1 532 ? -52.693 31.173 16.652 1.00 18.34 ? 532 ASP A CG 1 ATOM 4135 O OD1 . ASP A 1 532 ? -53.061 32.219 17.234 1.00 17.88 ? 532 ASP A OD1 1 ATOM 4136 O OD2 . ASP A 1 532 ? -52.220 30.195 17.269 1.00 19.11 ? 532 ASP A OD2 1 ATOM 4137 N N . GLU A 1 533 ? -53.482 31.867 12.108 1.00 16.10 ? 533 GLU A N 1 ATOM 4138 C CA . GLU A 1 533 ? -53.131 31.904 10.686 1.00 16.37 ? 533 GLU A CA 1 ATOM 4139 C C . GLU A 1 533 ? -53.282 33.322 10.114 1.00 15.59 ? 533 GLU A C 1 ATOM 4140 O O . GLU A 1 533 ? -52.364 33.820 9.458 1.00 14.31 ? 533 GLU A O 1 ATOM 4141 C CB . GLU A 1 533 ? -53.993 30.911 9.890 1.00 15.73 ? 533 GLU A CB 1 ATOM 4142 C CG . GLU A 1 533 ? -53.783 30.953 8.367 1.00 18.58 ? 533 GLU A CG 1 ATOM 4143 C CD . GLU A 1 533 ? -54.477 29.835 7.613 1.00 20.37 ? 533 GLU A CD 1 ATOM 4144 O OE1 . GLU A 1 533 ? -55.381 29.176 8.172 1.00 23.61 ? 533 GLU A OE1 1 ATOM 4145 O OE2 . GLU A 1 533 ? -54.100 29.613 6.443 1.00 22.76 ? 533 GLU A OE2 1 ATOM 4146 N N . ASP A 1 534 ? -54.424 33.962 10.394 1.00 16.33 ? 534 ASP A N 1 ATOM 4147 C CA . ASP A 1 534 ? -54.713 35.326 9.925 1.00 15.76 ? 534 ASP A CA 1 ATOM 4148 C C . ASP A 1 534 ? -53.726 36.347 10.472 1.00 15.59 ? 534 ASP A C 1 ATOM 4149 O O . ASP A 1 534 ? -53.254 37.212 9.730 1.00 15.66 ? 534 ASP A O 1 ATOM 4150 C CB . ASP A 1 534 ? -56.132 35.773 10.317 1.00 16.83 ? 534 ASP A CB 1 ATOM 4151 C CG . ASP A 1 534 ? -57.225 35.045 9.549 1.00 18.39 ? 534 ASP A CG 1 ATOM 4152 O OD1 . ASP A 1 534 ? -56.931 34.384 8.533 1.00 19.42 ? 534 ASP A OD1 1 ATOM 4153 O OD2 . ASP A 1 534 ? -58.394 35.138 9.975 1.00 20.72 ? 534 ASP A OD2 1 ATOM 4154 N N . ASP A 1 535 ? -53.392 36.214 11.757 1.00 15.50 ? 535 ASP A N 1 ATOM 4155 C CA . ASP A 1 535 ? -52.467 37.137 12.407 1.00 15.08 ? 535 ASP A CA 1 ATOM 4156 C C . ASP A 1 535 ? -51.025 36.942 11.952 1.00 14.21 ? 535 ASP A C 1 ATOM 4157 O O . ASP A 1 535 ? -50.291 37.918 11.800 1.00 13.40 ? 535 ASP A O 1 ATOM 4158 C CB . ASP A 1 535 ? -52.582 37.068 13.924 1.00 17.61 ? 535 ASP A CB 1 ATOM 4159 C CG . ASP A 1 535 ? -52.252 38.394 14.582 1.00 21.18 ? 535 ASP A CG 1 ATOM 4160 O OD1 . ASP A 1 535 ? -53.007 39.366 14.360 1.00 20.43 ? 535 ASP A OD1 1 ATOM 4161 O OD2 . ASP A 1 535 ? -51.227 38.469 15.290 1.00 20.95 ? 535 ASP A OD2 1 ATOM 4162 N N . PHE A 1 536 ? -50.654 35.687 11.688 1.00 13.35 ? 536 PHE A N 1 ATOM 4163 C CA . PHE A 1 536 ? -49.322 35.324 11.190 1.00 14.18 ? 536 PHE A CA 1 ATOM 4164 C C . PHE A 1 536 ? -49.143 36.037 9.844 1.00 13.62 ? 536 PHE A C 1 ATOM 4165 O O . PHE A 1 536 ? -48.117 36.666 9.601 1.00 13.05 ? 536 PHE A O 1 ATOM 4166 C CB . PHE A 1 536 ? -49.235 33.788 11.004 1.00 14.04 ? 536 PHE A CB 1 ATOM 4167 C CG . PHE A 1 536 ? -48.054 33.322 10.185 1.00 14.80 ? 536 PHE A CG 1 ATOM 4168 C CD1 . PHE A 1 536 ? -46.807 33.118 10.787 1.00 14.09 ? 536 PHE A CD1 1 ATOM 4169 C CD2 . PHE A 1 536 ? -48.181 33.117 8.790 1.00 15.31 ? 536 PHE A CD2 1 ATOM 4170 C CE1 . PHE A 1 536 ? -45.691 32.720 10.014 1.00 14.24 ? 536 PHE A CE1 1 ATOM 4171 C CE2 . PHE A 1 536 ? -47.083 32.724 8.008 1.00 13.91 ? 536 PHE A CE2 1 ATOM 4172 C CZ . PHE A 1 536 ? -45.827 32.524 8.621 1.00 14.50 ? 536 PHE A CZ 1 ATOM 4173 N N . ASN A 1 537 ? -50.167 35.912 8.996 1.00 14.02 ? 537 ASN A N 1 ATOM 4174 C CA . ASN A 1 537 ? -50.195 36.511 7.665 1.00 14.76 ? 537 ASN A CA 1 ATOM 4175 C C . ASN A 1 537 ? -50.207 38.032 7.713 1.00 13.95 ? 537 ASN A C 1 ATOM 4176 O O . ASN A 1 537 ? -49.513 38.667 6.924 1.00 15.16 ? 537 ASN A O 1 ATOM 4177 C CB . ASN A 1 537 ? -51.386 35.978 6.853 1.00 14.91 ? 537 ASN A CB 1 ATOM 4178 C CG . ASN A 1 537 ? -51.178 34.548 6.378 1.00 15.68 ? 537 ASN A CG 1 ATOM 4179 O OD1 . ASN A 1 537 ? -50.063 34.145 6.050 1.00 17.34 ? 537 ASN A OD1 1 ATOM 4180 N ND2 . ASN A 1 537 ? -52.257 33.776 6.333 1.00 18.34 ? 537 ASN A ND2 1 ATOM 4181 N N . ARG A 1 538 ? -50.936 38.600 8.681 1.00 13.86 ? 538 ARG A N 1 ATOM 4182 C CA . ARG A 1 538 ? -51.014 40.057 8.871 1.00 13.30 ? 538 ARG A CA 1 ATOM 4183 C C . ARG A 1 538 ? -49.624 40.623 9.191 1.00 13.35 ? 538 ARG A C 1 ATOM 4184 O O . ARG A 1 538 ? -49.153 41.527 8.499 1.00 13.41 ? 538 ARG A O 1 ATOM 4185 C CB . ARG A 1 538 ? -51.987 40.411 10.007 1.00 13.82 ? 538 ARG A CB 1 ATOM 4186 C CG . ARG A 1 538 ? -52.101 41.909 10.302 1.00 13.12 ? 538 ARG A CG 1 ATOM 4187 C CD . ARG A 1 538 ? -52.853 42.199 11.591 1.00 13.66 ? 538 ARG A CD 1 ATOM 4188 N NE . ARG A 1 538 ? -52.200 41.694 12.800 1.00 13.98 ? 538 ARG A NE 1 ATOM 4189 C CZ . ARG A 1 538 ? -51.267 42.334 13.506 1.00 13.59 ? 538 ARG A CZ 1 ATOM 4190 N NH1 . ARG A 1 538 ? -50.822 43.533 13.139 1.00 13.61 ? 538 ARG A NH1 1 ATOM 4191 N NH2 . ARG A 1 538 ? -50.833 41.800 14.639 1.00 12.34 ? 538 ARG A NH2 1 ATOM 4192 N N . VAL A 1 539 ? -48.962 40.040 10.198 1.00 12.65 ? 539 VAL A N 1 ATOM 4193 C CA . VAL A 1 539 ? -47.625 40.471 10.623 1.00 11.93 ? 539 VAL A CA 1 ATOM 4194 C C . VAL A 1 539 ? -46.614 40.271 9.497 1.00 10.53 ? 539 VAL A C 1 ATOM 4195 O O . VAL A 1 539 ? -45.784 41.145 9.260 1.00 9.43 ? 539 VAL A O 1 ATOM 4196 C CB . VAL A 1 539 ? -47.160 39.751 11.927 1.00 13.12 ? 539 VAL A CB 1 ATOM 4197 C CG1 . VAL A 1 539 ? -45.772 40.241 12.362 1.00 11.97 ? 539 VAL A CG1 1 ATOM 4198 C CG2 . VAL A 1 539 ? -48.148 40.028 13.048 1.00 11.38 ? 539 VAL A CG2 1 ATOM 4199 N N . CYS A 1 540 ? -46.736 39.155 8.775 1.00 11.06 ? 540 CYS A N 1 ATOM 4200 C CA . CYS A 1 540 ? -45.850 38.864 7.648 1.00 12.14 ? 540 CYS A CA 1 ATOM 4201 C C . CYS A 1 540 ? -46.021 39.839 6.483 1.00 13.00 ? 540 CYS A C 1 ATOM 4202 O O . CYS A 1 540 ? -45.032 40.252 5.878 1.00 11.96 ? 540 CYS A O 1 ATOM 4203 C CB . CYS A 1 540 ? -45.984 37.409 7.183 1.00 11.65 ? 540 CYS A CB 1 ATOM 4204 S SG . CYS A 1 540 ? -45.064 36.202 8.206 1.00 11.51 ? 540 CYS A SG 1 ATOM 4205 N N . ASP A 1 541 ? -47.260 40.260 6.227 1.00 13.24 ? 541 ASP A N 1 ATOM 4206 C CA . ASP A 1 541 ? -47.545 41.224 5.157 1.00 14.47 ? 541 ASP A CA 1 ATOM 4207 C C . ASP A 1 541 ? -46.994 42.597 5.544 1.00 13.88 ? 541 ASP A C 1 ATOM 4208 O O . ASP A 1 541 ? -46.394 43.285 4.717 1.00 12.78 ? 541 ASP A O 1 ATOM 4209 C CB . ASP A 1 541 ? -49.052 41.311 4.864 1.00 16.62 ? 541 ASP A CB 1 ATOM 4210 C CG . ASP A 1 541 ? -49.580 40.104 4.082 1.00 19.21 ? 541 ASP A CG 1 ATOM 4211 O OD1 . ASP A 1 541 ? -48.792 39.417 3.396 1.00 20.36 ? 541 ASP A OD1 1 ATOM 4212 O OD2 . ASP A 1 541 ? -50.799 39.845 4.150 1.00 21.11 ? 541 ASP A OD2 1 ATOM 4213 N N . GLU A 1 542 ? -47.124 42.938 6.829 1.00 13.37 ? 542 GLU A N 1 ATOM 4214 C CA . GLU A 1 542 ? -46.626 44.209 7.365 1.00 12.82 ? 542 GLU A CA 1 ATOM 4215 C C . GLU A 1 542 ? -45.097 44.226 7.385 1.00 11.76 ? 542 GLU A C 1 ATOM 4216 O O . GLU A 1 542 ? -44.483 45.248 7.089 1.00 12.41 ? 542 GLU A O 1 ATOM 4217 C CB . GLU A 1 542 ? -47.166 44.452 8.774 1.00 13.24 ? 542 GLU A CB 1 ATOM 4218 C CG . GLU A 1 542 ? -48.656 44.800 8.845 1.00 11.72 ? 542 GLU A CG 1 ATOM 4219 C CD . GLU A 1 542 ? -49.156 44.964 10.273 1.00 12.84 ? 542 GLU A CD 1 ATOM 4220 O OE1 . GLU A 1 542 ? -48.351 45.300 11.171 1.00 13.61 ? 542 GLU A OE1 1 ATOM 4221 O OE2 . GLU A 1 542 ? -50.366 44.759 10.503 1.00 13.41 ? 542 GLU A OE2 1 ATOM 4222 N N . TRP A 1 543 ? -44.494 43.077 7.693 1.00 11.61 ? 543 TRP A N 1 ATOM 4223 C CA . TRP A 1 543 ? -43.038 42.952 7.720 1.00 11.53 ? 543 TRP A CA 1 ATOM 4224 C C . TRP A 1 543 ? -42.452 43.023 6.312 1.00 11.73 ? 543 TRP A C 1 ATOM 4225 O O . TRP A 1 543 ? -41.433 43.682 6.105 1.00 10.24 ? 543 TRP A O 1 ATOM 4226 C CB . TRP A 1 543 ? -42.589 41.652 8.421 1.00 12.18 ? 543 TRP A CB 1 ATOM 4227 C CG . TRP A 1 543 ? -41.088 41.415 8.362 1.00 13.56 ? 543 TRP A CG 1 ATOM 4228 C CD1 . TRP A 1 543 ? -40.433 40.500 7.577 1.00 14.43 ? 543 TRP A CD1 1 ATOM 4229 C CD2 . TRP A 1 543 ? -40.066 42.182 9.017 1.00 13.53 ? 543 TRP A CD2 1 ATOM 4230 N NE1 . TRP A 1 543 ? -39.073 40.661 7.687 1.00 15.36 ? 543 TRP A NE1 1 ATOM 4231 C CE2 . TRP A 1 543 ? -38.814 41.682 8.563 1.00 13.76 ? 543 TRP A CE2 1 ATOM 4232 C CE3 . TRP A 1 543 ? -40.079 43.251 9.938 1.00 13.40 ? 543 TRP A CE3 1 ATOM 4233 C CZ2 . TRP A 1 543 ? -37.582 42.214 9.000 1.00 14.68 ? 543 TRP A CZ2 1 ATOM 4234 C CZ3 . TRP A 1 543 ? -38.849 43.789 10.374 1.00 13.05 ? 543 TRP A CZ3 1 ATOM 4235 C CH2 . TRP A 1 543 ? -37.616 43.264 9.902 1.00 13.52 ? 543 TRP A CH2 1 ATOM 4236 N N . ARG A 1 544 ? -43.074 42.309 5.373 1.00 13.57 ? 544 ARG A N 1 ATOM 4237 C CA . ARG A 1 544 ? -42.622 42.286 3.980 1.00 16.30 ? 544 ARG A CA 1 ATOM 4238 C C . ARG A 1 544 ? -42.738 43.649 3.306 1.00 16.49 ? 544 ARG A C 1 ATOM 4239 O O . ARG A 1 544 ? -41.906 43.994 2.473 1.00 17.37 ? 544 ARG A O 1 ATOM 4240 C CB . ARG A 1 544 ? -43.355 41.212 3.177 1.00 16.55 ? 544 ARG A CB 1 ATOM 4241 C CG . ARG A 1 544 ? -42.813 39.809 3.418 1.00 20.31 ? 544 ARG A CG 1 ATOM 4242 C CD . ARG A 1 544 ? -43.411 38.787 2.459 1.00 22.23 ? 544 ARG A CD 1 ATOM 4243 N NE . ARG A 1 544 ? -44.834 38.565 2.708 1.00 22.66 ? 544 ARG A NE 1 ATOM 4244 C CZ . ARG A 1 544 ? -45.336 37.525 3.370 1.00 26.01 ? 544 ARG A CZ 1 ATOM 4245 N NH1 . ARG A 1 544 ? -44.537 36.581 3.865 1.00 23.64 ? 544 ARG A NH1 1 ATOM 4246 N NH2 . ARG A 1 544 ? -46.646 37.438 3.559 1.00 25.06 ? 544 ARG A NH2 1 ATOM 4247 N N . ALA A 1 545 ? -43.732 44.436 3.728 1.00 15.99 ? 545 ALA A N 1 ATOM 4248 C CA . ALA A 1 545 ? -43.949 45.786 3.212 1.00 16.15 ? 545 ALA A CA 1 ATOM 4249 C C . ALA A 1 545 ? -42.894 46.712 3.817 1.00 15.76 ? 545 ALA A C 1 ATOM 4250 O O . ALA A 1 545 ? -42.393 47.612 3.146 1.00 15.57 ? 545 ALA A O 1 ATOM 4251 C CB . ALA A 1 545 ? -45.343 46.276 3.564 1.00 16.10 ? 545 ALA A CB 1 ATOM 4252 N N . TYR A 1 546 ? -42.525 46.447 5.073 1.00 15.34 ? 546 TYR A N 1 ATOM 4253 C CA . TYR A 1 546 ? -41.514 47.243 5.754 1.00 14.85 ? 546 TYR A CA 1 ATOM 4254 C C . TYR A 1 546 ? -40.081 46.983 5.267 1.00 14.79 ? 546 TYR A C 1 ATOM 4255 O O . TYR A 1 546 ? -39.345 47.939 5.025 1.00 14.83 ? 546 TYR A O 1 ATOM 4256 C CB . TYR A 1 546 ? -41.567 47.067 7.299 1.00 14.55 ? 546 TYR A CB 1 ATOM 4257 C CG . TYR A 1 546 ? -40.376 47.713 8.000 1.00 13.11 ? 546 TYR A CG 1 ATOM 4258 C CD1 . TYR A 1 546 ? -40.262 49.120 8.066 1.00 10.85 ? 546 TYR A CD1 1 ATOM 4259 C CD2 . TYR A 1 546 ? -39.251 46.935 8.391 1.00 11.24 ? 546 TYR A CD2 1 ATOM 4260 C CE1 . TYR A 1 546 ? -39.058 49.740 8.474 1.00 11.80 ? 546 TYR A CE1 1 ATOM 4261 C CE2 . TYR A 1 546 ? -38.043 47.549 8.794 1.00 12.00 ? 546 TYR A CE2 1 ATOM 4262 C CZ . TYR A 1 546 ? -37.960 48.950 8.828 1.00 11.24 ? 546 TYR A CZ 1 ATOM 4263 O OH . TYR A 1 546 ? -36.793 49.560 9.206 1.00 14.62 ? 546 TYR A OH 1 ATOM 4264 N N . TRP A 1 547 ? -39.681 45.710 5.196 1.00 13.86 ? 547 TRP A N 1 ATOM 4265 C CA . TRP A 1 547 ? -38.305 45.326 4.839 1.00 15.20 ? 547 TRP A CA 1 ATOM 4266 C C . TRP A 1 547 ? -37.517 46.085 3.748 1.00 16.18 ? 547 TRP A C 1 ATOM 4267 O O . TRP A 1 547 ? -36.373 46.466 4.014 1.00 15.54 ? 547 TRP A O 1 ATOM 4268 C CB . TRP A 1 547 ? -38.139 43.785 4.743 1.00 13.73 ? 547 TRP A CB 1 ATOM 4269 C CG . TRP A 1 547 ? -36.701 43.303 4.528 1.00 16.09 ? 547 TRP A CG 1 ATOM 4270 C CD1 . TRP A 1 547 ? -36.197 42.719 3.394 1.00 16.78 ? 547 TRP A CD1 1 ATOM 4271 C CD2 . TRP A 1 547 ? -35.594 43.414 5.444 1.00 17.29 ? 547 TRP A CD2 1 ATOM 4272 N NE1 . TRP A 1 547 ? -34.853 42.470 3.538 1.00 17.20 ? 547 TRP A NE1 1 ATOM 4273 C CE2 . TRP A 1 547 ? -34.451 42.883 4.782 1.00 17.38 ? 547 TRP A CE2 1 ATOM 4274 C CE3 . TRP A 1 547 ? -35.450 43.912 6.760 1.00 17.94 ? 547 TRP A CE3 1 ATOM 4275 C CZ2 . TRP A 1 547 ? -33.172 42.833 5.391 1.00 16.89 ? 547 TRP A CZ2 1 ATOM 4276 C CZ3 . TRP A 1 547 ? -34.170 43.862 7.375 1.00 19.22 ? 547 TRP A CZ3 1 ATOM 4277 C CH2 . TRP A 1 547 ? -33.049 43.323 6.679 1.00 15.44 ? 547 TRP A CH2 1 ATOM 4278 N N . PRO A 1 548 ? -38.102 46.341 2.543 1.00 17.10 ? 548 PRO A N 1 ATOM 4279 C CA . PRO A 1 548 ? -37.319 47.075 1.532 1.00 17.45 ? 548 PRO A CA 1 ATOM 4280 C C . PRO A 1 548 ? -36.896 48.498 1.936 1.00 18.28 ? 548 PRO A C 1 ATOM 4281 O O . PRO A 1 548 ? -35.926 49.028 1.395 1.00 19.09 ? 548 PRO A O 1 ATOM 4282 C CB . PRO A 1 548 ? -38.258 47.093 0.326 1.00 18.07 ? 548 PRO A CB 1 ATOM 4283 C CG . PRO A 1 548 ? -38.988 45.796 0.459 1.00 19.12 ? 548 PRO A CG 1 ATOM 4284 C CD . PRO A 1 548 ? -39.341 45.823 1.924 1.00 17.26 ? 548 PRO A CD 1 ATOM 4285 N N . THR A 1 549 ? -37.581 49.070 2.932 1.00 18.14 ? 549 THR A N 1 ATOM 4286 C CA . THR A 1 549 ? -37.282 50.423 3.421 1.00 17.58 ? 549 THR A CA 1 ATOM 4287 C C . THR A 1 549 ? -36.199 50.457 4.506 1.00 18.24 ? 549 THR A C 1 ATOM 4288 O O . THR A 1 549 ? -35.717 51.536 4.863 1.00 18.04 ? 549 THR A O 1 ATOM 4289 C CB . THR A 1 549 ? -38.549 51.167 3.960 1.00 18.10 ? 549 THR A CB 1 ATOM 4290 O OG1 . THR A 1 549 ? -38.958 50.605 5.215 1.00 17.73 ? 549 THR A OG1 1 ATOM 4291 C CG2 . THR A 1 549 ? -39.699 51.077 2.971 1.00 17.58 ? 549 THR A CG2 1 ATOM 4292 N N . ASN A 1 550 ? -35.832 49.282 5.028 1.00 17.63 ? 550 ASN A N 1 ATOM 4293 C CA . ASN A 1 550 ? -34.808 49.161 6.075 1.00 16.21 ? 550 ASN A CA 1 ATOM 4294 C C . ASN A 1 550 ? -33.428 49.517 5.502 1.00 17.22 ? 550 ASN A C 1 ATOM 4295 O O . ASN A 1 550 ? -33.014 48.941 4.492 1.00 18.68 ? 550 ASN A O 1 ATOM 4296 C CB . ASN A 1 550 ? -34.798 47.739 6.655 1.00 17.56 ? 550 ASN A CB 1 ATOM 4297 C CG . ASN A 1 550 ? -34.070 47.651 7.995 1.00 17.84 ? 550 ASN A CG 1 ATOM 4298 O OD1 . ASN A 1 550 ? -34.504 48.224 8.984 1.00 18.38 ? 550 ASN A OD1 1 ATOM 4299 N ND2 . ASN A 1 550 ? -32.963 46.935 8.022 1.00 18.35 ? 550 ASN A ND2 1 ATOM 4300 N N . PRO A 1 551 ? -32.722 50.494 6.119 1.00 18.00 ? 551 PRO A N 1 ATOM 4301 C CA . PRO A 1 551 ? -31.396 50.920 5.657 1.00 18.32 ? 551 PRO A CA 1 ATOM 4302 C C . PRO A 1 551 ? -30.231 49.996 6.021 1.00 18.44 ? 551 PRO A C 1 ATOM 4303 O O . PRO A 1 551 ? -29.101 50.225 5.588 1.00 18.35 ? 551 PRO A O 1 ATOM 4304 C CB . PRO A 1 551 ? -31.242 52.290 6.318 1.00 19.10 ? 551 PRO A CB 1 ATOM 4305 C CG . PRO A 1 551 ? -31.921 52.100 7.625 1.00 20.01 ? 551 PRO A CG 1 ATOM 4306 C CD . PRO A 1 551 ? -33.180 51.364 7.227 1.00 18.94 ? 551 PRO A CD 1 ATOM 4307 N N . TYR A 1 552 ? -30.517 48.968 6.820 1.00 18.68 ? 552 TYR A N 1 ATOM 4308 C CA . TYR A 1 552 ? -29.504 48.017 7.277 1.00 19.65 ? 552 TYR A CA 1 ATOM 4309 C C . TYR A 1 552 ? -29.726 46.585 6.784 1.00 20.28 ? 552 TYR A C 1 ATOM 4310 O O . TYR A 1 552 ? -30.867 46.123 6.705 1.00 20.69 ? 552 TYR A O 1 ATOM 4311 C CB . TYR A 1 552 ? -29.445 47.996 8.816 1.00 19.16 ? 552 TYR A CB 1 ATOM 4312 C CG . TYR A 1 552 ? -29.142 49.322 9.484 1.00 20.17 ? 552 TYR A CG 1 ATOM 4313 C CD1 . TYR A 1 552 ? -28.069 50.140 9.051 1.00 20.66 ? 552 TYR A CD1 1 ATOM 4314 C CD2 . TYR A 1 552 ? -29.923 49.768 10.565 1.00 19.19 ? 552 TYR A CD2 1 ATOM 4315 C CE1 . TYR A 1 552 ? -27.787 51.381 9.691 1.00 21.29 ? 552 TYR A CE1 1 ATOM 4316 C CE2 . TYR A 1 552 ? -29.651 51.002 11.214 1.00 19.99 ? 552 TYR A CE2 1 ATOM 4317 C CZ . TYR A 1 552 ? -28.585 51.798 10.769 1.00 20.49 ? 552 TYR A CZ 1 ATOM 4318 O OH . TYR A 1 552 ? -28.328 52.990 11.398 1.00 23.23 ? 552 TYR A OH 1 ATOM 4319 N N . PRO A 1 553 ? -28.638 45.876 6.408 1.00 20.38 ? 553 PRO A N 1 ATOM 4320 C CA . PRO A 1 553 ? -28.814 44.497 5.943 1.00 20.88 ? 553 PRO A CA 1 ATOM 4321 C C . PRO A 1 553 ? -28.818 43.499 7.113 1.00 19.97 ? 553 PRO A C 1 ATOM 4322 O O . PRO A 1 553 ? -28.489 43.854 8.248 1.00 18.76 ? 553 PRO A O 1 ATOM 4323 C CB . PRO A 1 553 ? -27.596 44.292 5.044 1.00 22.20 ? 553 PRO A CB 1 ATOM 4324 C CG . PRO A 1 553 ? -26.531 45.087 5.742 1.00 22.53 ? 553 PRO A CG 1 ATOM 4325 C CD . PRO A 1 553 ? -27.267 46.355 6.119 1.00 21.74 ? 553 PRO A CD 1 ATOM 4326 N N . LYS A 1 554 ? -29.246 42.275 6.826 1.00 19.46 ? 554 LYS A N 1 ATOM 4327 C CA . LYS A 1 554 ? -29.257 41.180 7.794 1.00 19.81 ? 554 LYS A CA 1 ATOM 4328 C C . LYS A 1 554 ? -27.827 40.623 7.700 1.00 19.82 ? 554 LYS A C 1 ATOM 4329 O O . LYS A 1 554 ? -27.419 40.119 6.644 1.00 19.68 ? 554 LYS A O 1 ATOM 4330 C CB . LYS A 1 554 ? -30.300 40.147 7.359 1.00 20.40 ? 554 LYS A CB 1 ATOM 4331 C CG . LYS A 1 554 ? -30.362 38.844 8.138 1.00 19.16 ? 554 LYS A CG 1 ATOM 4332 C CD . LYS A 1 554 ? -31.553 38.061 7.616 1.00 23.28 ? 554 LYS A CD 1 ATOM 4333 C CE . LYS A 1 554 ? -31.626 36.661 8.152 1.00 22.59 ? 554 LYS A CE 1 ATOM 4334 N NZ . LYS A 1 554 ? -30.579 35.820 7.549 1.00 26.52 ? 554 LYS A NZ 1 ATOM 4335 N N . ILE A 1 555 ? -27.055 40.814 8.770 1.00 20.50 ? 555 ILE A N 1 ATOM 4336 C CA . ILE A 1 555 ? -25.655 40.380 8.827 1.00 22.11 ? 555 ILE A CA 1 ATOM 4337 C C . ILE A 1 555 ? -25.398 38.973 9.375 1.00 20.82 ? 555 ILE A C 1 ATOM 4338 O O . ILE A 1 555 ? -24.274 38.464 9.267 1.00 20.70 ? 555 ILE A O 1 ATOM 4339 C CB . ILE A 1 555 ? -24.764 41.402 9.613 1.00 24.35 ? 555 ILE A CB 1 ATOM 4340 C CG1 . ILE A 1 555 ? -25.318 41.640 11.030 1.00 26.47 ? 555 ILE A CG1 1 ATOM 4341 C CG2 . ILE A 1 555 ? -24.639 42.707 8.819 1.00 25.91 ? 555 ILE A CG2 1 ATOM 4342 C CD1 . ILE A 1 555 ? -24.367 42.381 11.977 1.00 29.31 ? 555 ILE A CD1 1 ATOM 4343 N N . ASP A 1 556 ? -26.430 38.345 9.938 1.00 16.70 ? 556 ASP A N 1 ATOM 4344 C CA . ASP A 1 556 ? -26.279 37.008 10.513 1.00 13.50 ? 556 ASP A CA 1 ATOM 4345 C C . ASP A 1 556 ? -27.384 36.006 10.152 1.00 11.63 ? 556 ASP A C 1 ATOM 4346 O O . ASP A 1 556 ? -28.096 36.195 9.166 1.00 12.24 ? 556 ASP A O 1 ATOM 4347 C CB . ASP A 1 556 ? -26.078 37.121 12.040 1.00 12.53 ? 556 ASP A CB 1 ATOM 4348 C CG . ASP A 1 556 ? -27.291 37.692 12.791 1.00 14.39 ? 556 ASP A CG 1 ATOM 4349 O OD1 . ASP A 1 556 ? -28.383 37.875 12.205 1.00 14.09 ? 556 ASP A OD1 1 ATOM 4350 O OD2 . ASP A 1 556 ? -27.146 37.947 14.007 1.00 14.35 ? 556 ASP A OD2 1 ATOM 4351 N N . SER A 1 557 ? -27.550 34.970 10.979 1.00 8.51 ? 557 SER A N 1 ATOM 4352 C CA . SER A 1 557 ? -28.573 33.939 10.768 1.00 9.33 ? 557 SER A CA 1 ATOM 4353 C C . SER A 1 557 ? -29.992 34.476 10.917 1.00 9.06 ? 557 SER A C 1 ATOM 4354 O O . SER A 1 557 ? -30.933 33.947 10.326 1.00 9.01 ? 557 SER A O 1 ATOM 4355 C CB . SER A 1 557 ? -28.393 32.798 11.767 1.00 7.82 ? 557 SER A CB 1 ATOM 4356 O OG . SER A 1 557 ? -28.719 33.218 13.079 1.00 7.63 ? 557 SER A OG 1 ATOM 4357 N N . GLY A 1 558 ? -30.123 35.514 11.738 1.00 10.61 ? 558 GLY A N 1 ATOM 4358 C CA . GLY A 1 558 ? -31.414 36.116 12.002 1.00 10.90 ? 558 GLY A CA 1 ATOM 4359 C C . GLY A 1 558 ? -32.028 35.612 13.291 1.00 11.94 ? 558 GLY A C 1 ATOM 4360 O O . GLY A 1 558 ? -33.108 36.058 13.686 1.00 11.70 ? 558 GLY A O 1 ATOM 4361 N N . LEU A 1 559 ? -31.329 34.679 13.942 1.00 12.12 ? 559 LEU A N 1 ATOM 4362 C CA . LEU A 1 559 ? -31.773 34.076 15.200 1.00 12.56 ? 559 LEU A CA 1 ATOM 4363 C C . LEU A 1 559 ? -30.865 34.435 16.376 1.00 14.30 ? 559 LEU A C 1 ATOM 4364 O O . LEU A 1 559 ? -29.722 34.870 16.123 1.00 14.87 ? 559 LEU A O 1 ATOM 4365 C CB . LEU A 1 559 ? -31.853 32.555 15.062 1.00 10.68 ? 559 LEU A CB 1 ATOM 4366 C CG . LEU A 1 559 ? -32.797 31.979 14.003 1.00 11.14 ? 559 LEU A CG 1 ATOM 4367 C CD1 . LEU A 1 559 ? -32.557 30.502 13.860 1.00 7.34 ? 559 LEU A CD1 1 ATOM 4368 C CD2 . LEU A 1 559 ? -34.255 32.280 14.330 1.00 9.76 ? 559 LEU A CD2 1 ATOM 4369 O OXT . LEU A 1 559 ? -31.312 34.294 17.539 1.00 13.70 ? 559 LEU A OXT 1 ATOM 4370 N N . GLU B 1 1 ? 37.167 29.162 40.722 1.00 45.69 ? 1 GLU B N 1 ATOM 4371 C CA . GLU B 1 1 ? 37.351 28.647 42.111 1.00 47.11 ? 1 GLU B CA 1 ATOM 4372 C C . GLU B 1 1 ? 37.203 29.798 43.127 1.00 45.93 ? 1 GLU B C 1 ATOM 4373 O O . GLU B 1 1 ? 37.860 30.837 42.988 1.00 45.52 ? 1 GLU B O 1 ATOM 4374 C CB . GLU B 1 1 ? 38.729 27.962 42.234 1.00 49.03 ? 1 GLU B CB 1 ATOM 4375 C CG . GLU B 1 1 ? 38.991 27.165 43.531 1.00 52.40 ? 1 GLU B CG 1 ATOM 4376 C CD . GLU B 1 1 ? 38.055 25.971 43.726 1.00 54.29 ? 1 GLU B CD 1 ATOM 4377 O OE1 . GLU B 1 1 ? 37.916 25.147 42.795 1.00 55.16 ? 1 GLU B OE1 1 ATOM 4378 O OE2 . GLU B 1 1 ? 37.458 25.861 44.821 1.00 54.65 ? 1 GLU B OE2 1 ATOM 4379 N N . PRO B 1 2 ? 36.297 29.647 44.128 1.00 44.85 ? 2 PRO B N 1 ATOM 4380 C CA . PRO B 1 2 ? 36.074 30.677 45.156 1.00 43.78 ? 2 PRO B CA 1 ATOM 4381 C C . PRO B 1 2 ? 37.118 30.730 46.277 1.00 42.53 ? 2 PRO B C 1 ATOM 4382 O O . PRO B 1 2 ? 37.728 29.710 46.612 1.00 43.42 ? 2 PRO B O 1 ATOM 4383 C CB . PRO B 1 2 ? 34.706 30.302 45.714 1.00 43.71 ? 2 PRO B CB 1 ATOM 4384 C CG . PRO B 1 2 ? 34.687 28.813 45.607 1.00 44.22 ? 2 PRO B CG 1 ATOM 4385 C CD . PRO B 1 2 ? 35.274 28.583 44.239 1.00 44.55 ? 2 PRO B CD 1 ATOM 4386 N N . THR B 1 3 ? 37.318 31.926 46.838 1.00 40.94 ? 3 THR B N 1 ATOM 4387 C CA . THR B 1 3 ? 38.261 32.141 47.942 1.00 38.92 ? 3 THR B CA 1 ATOM 4388 C C . THR B 1 3 ? 37.599 32.834 49.145 1.00 37.63 ? 3 THR B C 1 ATOM 4389 O O . THR B 1 3 ? 38.126 32.771 50.260 1.00 38.97 ? 3 THR B O 1 ATOM 4390 C CB . THR B 1 3 ? 39.512 32.986 47.522 1.00 39.34 ? 3 THR B CB 1 ATOM 4391 O OG1 . THR B 1 3 ? 39.099 34.266 47.028 1.00 38.73 ? 3 THR B OG1 1 ATOM 4392 C CG2 . THR B 1 3 ? 40.355 32.269 46.468 1.00 38.03 ? 3 THR B CG2 1 ATOM 4393 N N . CYS B 1 4 ? 36.445 33.470 48.920 1.00 34.09 ? 4 CYS B N 1 ATOM 4394 C CA . CYS B 1 4 ? 35.731 34.194 49.979 1.00 30.29 ? 4 CYS B CA 1 ATOM 4395 C C . CYS B 1 4 ? 34.204 34.017 50.023 1.00 28.59 ? 4 CYS B C 1 ATOM 4396 O O . CYS B 1 4 ? 33.511 34.748 50.745 1.00 26.88 ? 4 CYS B O 1 ATOM 4397 C CB . CYS B 1 4 ? 36.083 35.686 49.906 1.00 29.64 ? 4 CYS B CB 1 ATOM 4398 S SG . CYS B 1 4 ? 35.652 36.472 48.321 1.00 28.02 ? 4 CYS B SG 1 ATOM 4399 N N . ASN B 1 5 ? 33.682 33.057 49.258 1.00 25.50 ? 5 ASN B N 1 ATOM 4400 C CA . ASN B 1 5 ? 32.240 32.781 49.219 1.00 24.08 ? 5 ASN B CA 1 ATOM 4401 C C . ASN B 1 5 ? 31.862 31.872 50.394 1.00 24.01 ? 5 ASN B C 1 ATOM 4402 O O . ASN B 1 5 ? 32.109 30.662 50.371 1.00 24.21 ? 5 ASN B O 1 ATOM 4403 C CB . ASN B 1 5 ? 31.858 32.140 47.879 1.00 22.09 ? 5 ASN B CB 1 ATOM 4404 C CG . ASN B 1 5 ? 30.355 32.089 47.653 1.00 19.10 ? 5 ASN B CG 1 ATOM 4405 O OD1 . ASN B 1 5 ? 29.740 31.034 47.764 1.00 19.09 ? 5 ASN B OD1 1 ATOM 4406 N ND2 . ASN B 1 5 ? 29.765 33.229 47.313 1.00 20.11 ? 5 ASN B ND2 1 ATOM 4407 N N . THR B 1 6 ? 31.299 32.494 51.429 1.00 23.80 ? 6 THR B N 1 ATOM 4408 C CA . THR B 1 6 ? 30.893 31.823 52.668 1.00 24.65 ? 6 THR B CA 1 ATOM 4409 C C . THR B 1 6 ? 29.377 32.002 52.875 1.00 24.35 ? 6 THR B C 1 ATOM 4410 O O . THR B 1 6 ? 28.777 32.848 52.206 1.00 22.52 ? 6 THR B O 1 ATOM 4411 C CB . THR B 1 6 ? 31.639 32.464 53.894 1.00 25.86 ? 6 THR B CB 1 ATOM 4412 O OG1 . THR B 1 6 ? 31.320 33.858 53.977 1.00 27.23 ? 6 THR B OG1 1 ATOM 4413 C CG2 . THR B 1 6 ? 33.156 32.279 53.792 1.00 27.32 ? 6 THR B CG2 1 ATOM 4414 N N . PRO B 1 7 ? 28.728 31.184 53.756 1.00 24.22 ? 7 PRO B N 1 ATOM 4415 C CA . PRO B 1 7 ? 27.282 31.349 53.982 1.00 24.29 ? 7 PRO B CA 1 ATOM 4416 C C . PRO B 1 7 ? 26.823 32.754 54.397 1.00 24.63 ? 7 PRO B C 1 ATOM 4417 O O . PRO B 1 7 ? 25.763 33.209 53.971 1.00 23.77 ? 7 PRO B O 1 ATOM 4418 C CB . PRO B 1 7 ? 27.000 30.326 55.074 1.00 24.33 ? 7 PRO B CB 1 ATOM 4419 C CG . PRO B 1 7 ? 27.843 29.192 54.643 1.00 23.47 ? 7 PRO B CG 1 ATOM 4420 C CD . PRO B 1 7 ? 29.156 29.871 54.297 1.00 24.33 ? 7 PRO B CD 1 ATOM 4421 N N . SER B 1 8 ? 27.668 33.451 55.159 1.00 24.17 ? 8 SER B N 1 ATOM 4422 C CA . SER B 1 8 ? 27.384 34.807 55.635 1.00 24.25 ? 8 SER B CA 1 ATOM 4423 C C . SER B 1 8 ? 27.785 35.901 54.634 1.00 24.53 ? 8 SER B C 1 ATOM 4424 O O . SER B 1 8 ? 27.304 37.036 54.716 1.00 24.59 ? 8 SER B O 1 ATOM 4425 C CB . SER B 1 8 ? 28.079 35.046 56.979 1.00 25.39 ? 8 SER B CB 1 ATOM 4426 O OG . SER B 1 8 ? 29.472 34.790 56.890 1.00 26.35 ? 8 SER B OG 1 ATOM 4427 N N . ASN B 1 9 ? 28.688 35.561 53.716 1.00 23.43 ? 9 ASN B N 1 ATOM 4428 C CA . ASN B 1 9 ? 29.150 36.505 52.701 1.00 23.50 ? 9 ASN B CA 1 ATOM 4429 C C . ASN B 1 9 ? 29.130 35.823 51.331 1.00 22.64 ? 9 ASN B C 1 ATOM 4430 O O . ASN B 1 9 ? 30.158 35.352 50.827 1.00 21.32 ? 9 ASN B O 1 ATOM 4431 C CB . ASN B 1 9 ? 30.555 37.044 53.050 1.00 25.26 ? 9 ASN B CB 1 ATOM 4432 C CG . ASN B 1 9 ? 30.940 38.301 52.250 1.00 26.28 ? 9 ASN B CG 1 ATOM 4433 O OD1 . ASN B 1 9 ? 30.283 38.677 51.274 1.00 27.82 ? 9 ASN B OD1 1 ATOM 4434 N ND2 . ASN B 1 9 ? 32.031 38.938 52.658 1.00 27.46 ? 9 ASN B ND2 1 ATOM 4435 N N . ARG B 1 10 ? 27.932 35.742 50.756 1.00 20.76 ? 10 ARG B N 1 ATOM 4436 C CA . ARG B 1 10 ? 27.746 35.138 49.441 1.00 19.83 ? 10 ARG B CA 1 ATOM 4437 C C . ARG B 1 10 ? 28.006 36.155 48.343 1.00 19.31 ? 10 ARG B C 1 ATOM 4438 O O . ARG B 1 10 ? 28.141 35.787 47.185 1.00 17.80 ? 10 ARG B O 1 ATOM 4439 C CB . ARG B 1 10 ? 26.342 34.550 49.297 1.00 18.81 ? 10 ARG B CB 1 ATOM 4440 C CG . ARG B 1 10 ? 26.093 33.303 50.130 1.00 19.57 ? 10 ARG B CG 1 ATOM 4441 C CD . ARG B 1 10 ? 26.886 32.103 49.651 1.00 19.96 ? 10 ARG B CD 1 ATOM 4442 N NE . ARG B 1 10 ? 26.434 30.882 50.314 1.00 21.12 ? 10 ARG B NE 1 ATOM 4443 C CZ . ARG B 1 10 ? 27.111 29.736 50.349 1.00 23.05 ? 10 ARG B CZ 1 ATOM 4444 N NH1 . ARG B 1 10 ? 28.297 29.630 49.759 1.00 22.51 ? 10 ARG B NH1 1 ATOM 4445 N NH2 . ARG B 1 10 ? 26.585 28.686 50.968 1.00 22.90 ? 10 ARG B NH2 1 ATOM 4446 N N . ALA B 1 11 ? 28.117 37.426 48.735 1.00 18.37 ? 11 ALA B N 1 ATOM 4447 C CA . ALA B 1 11 ? 28.382 38.536 47.820 1.00 19.85 ? 11 ALA B CA 1 ATOM 4448 C C . ALA B 1 11 ? 29.807 38.492 47.269 1.00 21.53 ? 11 ALA B C 1 ATOM 4449 O O . ALA B 1 11 ? 30.057 38.925 46.145 1.00 22.36 ? 11 ALA B O 1 ATOM 4450 C CB . ALA B 1 11 ? 28.133 39.861 48.522 1.00 19.24 ? 11 ALA B CB 1 ATOM 4451 N N . CYS B 1 12 ? 30.716 37.917 48.057 1.00 22.41 ? 12 CYS B N 1 ATOM 4452 C CA . CYS B 1 12 ? 32.128 37.782 47.709 1.00 21.69 ? 12 CYS B CA 1 ATOM 4453 C C . CYS B 1 12 ? 32.367 36.493 46.923 1.00 20.85 ? 12 CYS B C 1 ATOM 4454 O O . CYS B 1 12 ? 31.638 35.515 47.101 1.00 20.02 ? 12 CYS B O 1 ATOM 4455 C CB . CYS B 1 12 ? 32.958 37.749 49.000 1.00 24.17 ? 12 CYS B CB 1 ATOM 4456 S SG . CYS B 1 12 ? 34.719 38.197 48.843 1.00 25.88 ? 12 CYS B SG 1 ATOM 4457 N N . TRP B 1 13 ? 33.356 36.512 46.028 1.00 20.22 ? 13 TRP B N 1 ATOM 4458 C CA . TRP B 1 13 ? 33.716 35.326 45.246 1.00 20.24 ? 13 TRP B CA 1 ATOM 4459 C C . TRP B 1 13 ? 35.227 35.098 45.264 1.00 21.52 ? 13 TRP B C 1 ATOM 4460 O O . TRP B 1 13 ? 35.694 34.088 45.797 1.00 22.56 ? 13 TRP B O 1 ATOM 4461 C CB . TRP B 1 13 ? 33.177 35.401 43.806 1.00 18.55 ? 13 TRP B CB 1 ATOM 4462 C CG . TRP B 1 13 ? 33.361 34.117 43.008 1.00 17.47 ? 13 TRP B CG 1 ATOM 4463 C CD1 . TRP B 1 13 ? 34.187 33.934 41.933 1.00 16.84 ? 13 TRP B CD1 1 ATOM 4464 C CD2 . TRP B 1 13 ? 32.731 32.846 43.248 1.00 16.61 ? 13 TRP B CD2 1 ATOM 4465 N NE1 . TRP B 1 13 ? 34.118 32.635 41.490 1.00 15.29 ? 13 TRP B NE1 1 ATOM 4466 C CE2 . TRP B 1 13 ? 33.234 31.942 42.272 1.00 16.23 ? 13 TRP B CE2 1 ATOM 4467 C CE3 . TRP B 1 13 ? 31.792 32.376 44.192 1.00 15.92 ? 13 TRP B CE3 1 ATOM 4468 C CZ2 . TRP B 1 13 ? 32.827 30.588 42.209 1.00 17.86 ? 13 TRP B CZ2 1 ATOM 4469 C CZ3 . TRP B 1 13 ? 31.382 31.013 44.134 1.00 15.39 ? 13 TRP B CZ3 1 ATOM 4470 C CH2 . TRP B 1 13 ? 31.904 30.144 43.145 1.00 17.42 ? 13 TRP B CH2 1 ATOM 4471 N N . SER B 1 14 ? 35.972 36.028 44.665 1.00 23.30 ? 14 SER B N 1 ATOM 4472 C CA . SER B 1 14 ? 37.439 35.987 44.610 1.00 24.72 ? 14 SER B CA 1 ATOM 4473 C C . SER B 1 14 ? 37.967 37.414 44.459 1.00 25.61 ? 14 SER B C 1 ATOM 4474 O O . SER B 1 14 ? 37.174 38.357 44.358 1.00 24.47 ? 14 SER B O 1 ATOM 4475 C CB . SER B 1 14 ? 37.934 35.092 43.461 1.00 24.73 ? 14 SER B CB 1 ATOM 4476 O OG . SER B 1 14 ? 37.477 35.546 42.200 1.00 26.50 ? 14 SER B OG 1 ATOM 4477 N N . ASP B 1 15 ? 39.295 37.569 44.444 1.00 27.13 ? 15 ASP B N 1 ATOM 4478 C CA . ASP B 1 15 ? 39.944 38.882 44.310 1.00 28.39 ? 15 ASP B CA 1 ATOM 4479 C C . ASP B 1 15 ? 39.585 39.576 42.998 1.00 27.28 ? 15 ASP B C 1 ATOM 4480 O O . ASP B 1 15 ? 39.926 39.099 41.911 1.00 27.12 ? 15 ASP B O 1 ATOM 4481 C CB . ASP B 1 15 ? 41.473 38.758 44.435 1.00 31.88 ? 15 ASP B CB 1 ATOM 4482 C CG . ASP B 1 15 ? 41.924 38.292 45.818 1.00 35.95 ? 15 ASP B CG 1 ATOM 4483 O OD1 . ASP B 1 15 ? 41.341 38.736 46.836 1.00 37.01 ? 15 ASP B OD1 1 ATOM 4484 O OD2 . ASP B 1 15 ? 42.877 37.483 45.884 1.00 38.59 ? 15 ASP B OD2 1 ATOM 4485 N N . GLY B 1 16 ? 38.824 40.662 43.123 1.00 25.81 ? 16 GLY B N 1 ATOM 4486 C CA . GLY B 1 16 ? 38.389 41.433 41.972 1.00 24.65 ? 16 GLY B CA 1 ATOM 4487 C C . GLY B 1 16 ? 37.062 40.997 41.391 1.00 24.03 ? 16 GLY B C 1 ATOM 4488 O O . GLY B 1 16 ? 36.574 41.589 40.422 1.00 24.44 ? 16 GLY B O 1 ATOM 4489 N N . PHE B 1 17 ? 36.495 39.934 41.960 1.00 21.68 ? 17 PHE B N 1 ATOM 4490 C CA . PHE B 1 17 ? 35.232 39.384 41.486 1.00 19.92 ? 17 PHE B CA 1 ATOM 4491 C C . PHE B 1 17 ? 34.211 39.174 42.588 1.00 18.93 ? 17 PHE B C 1 ATOM 4492 O O . PHE B 1 17 ? 34.434 38.406 43.521 1.00 17.11 ? 17 PHE B O 1 ATOM 4493 C CB . PHE B 1 17 ? 35.481 38.077 40.718 1.00 20.33 ? 17 PHE B CB 1 ATOM 4494 C CG . PHE B 1 17 ? 36.324 38.258 39.489 1.00 20.73 ? 17 PHE B CG 1 ATOM 4495 C CD1 . PHE B 1 17 ? 35.767 38.803 38.317 1.00 19.88 ? 17 PHE B CD1 1 ATOM 4496 C CD2 . PHE B 1 17 ? 37.707 37.979 39.525 1.00 21.01 ? 17 PHE B CD2 1 ATOM 4497 C CE1 . PHE B 1 17 ? 36.578 39.080 37.191 1.00 20.74 ? 17 PHE B CE1 1 ATOM 4498 C CE2 . PHE B 1 17 ? 38.536 38.251 38.407 1.00 21.15 ? 17 PHE B CE2 1 ATOM 4499 C CZ . PHE B 1 17 ? 37.969 38.806 37.235 1.00 21.14 ? 17 PHE B CZ 1 ATOM 4500 N N . ASP B 1 18 ? 33.112 39.919 42.491 1.00 17.93 ? 18 ASP B N 1 ATOM 4501 C CA . ASP B 1 18 ? 32.011 39.837 43.446 1.00 17.87 ? 18 ASP B CA 1 ATOM 4502 C C . ASP B 1 18 ? 30.667 40.029 42.735 1.00 17.17 ? 18 ASP B C 1 ATOM 4503 O O . ASP B 1 18 ? 30.612 40.040 41.500 1.00 16.73 ? 18 ASP B O 1 ATOM 4504 C CB . ASP B 1 18 ? 32.205 40.814 44.637 1.00 18.55 ? 18 ASP B CB 1 ATOM 4505 C CG . ASP B 1 18 ? 32.427 42.268 44.216 1.00 19.57 ? 18 ASP B CG 1 ATOM 4506 O OD1 . ASP B 1 18 ? 31.758 42.763 43.285 1.00 20.99 ? 18 ASP B OD1 1 ATOM 4507 O OD2 . ASP B 1 18 ? 33.261 42.936 44.859 1.00 20.74 ? 18 ASP B OD2 1 ATOM 4508 N N . ILE B 1 19 ? 29.596 40.181 43.512 1.00 16.45 ? 19 ILE B N 1 ATOM 4509 C CA . ILE B 1 19 ? 28.239 40.360 42.987 1.00 15.92 ? 19 ILE B CA 1 ATOM 4510 C C . ILE B 1 19 ? 28.043 41.668 42.206 1.00 16.99 ? 19 ILE B C 1 ATOM 4511 O O . ILE B 1 19 ? 27.207 41.743 41.304 1.00 16.78 ? 19 ILE B O 1 ATOM 4512 C CB . ILE B 1 19 ? 27.187 40.219 44.146 1.00 16.11 ? 19 ILE B CB 1 ATOM 4513 C CG1 . ILE B 1 19 ? 25.769 40.004 43.597 1.00 14.90 ? 19 ILE B CG1 1 ATOM 4514 C CG2 . ILE B 1 19 ? 27.224 41.441 45.089 1.00 14.60 ? 19 ILE B CG2 1 ATOM 4515 C CD1 . ILE B 1 19 ? 25.598 38.747 42.791 1.00 15.63 ? 19 ILE B CD1 1 ATOM 4516 N N . ASN B 1 20 ? 28.871 42.661 42.525 1.00 17.44 ? 20 ASN B N 1 ATOM 4517 C CA . ASN B 1 20 ? 28.798 43.976 41.896 1.00 18.23 ? 20 ASN B CA 1 ATOM 4518 C C . ASN B 1 20 ? 29.645 44.141 40.638 1.00 17.73 ? 20 ASN B C 1 ATOM 4519 O O . ASN B 1 20 ? 29.535 45.152 39.938 1.00 18.39 ? 20 ASN B O 1 ATOM 4520 C CB . ASN B 1 20 ? 29.134 45.050 42.926 1.00 18.84 ? 20 ASN B CB 1 ATOM 4521 C CG . ASN B 1 20 ? 28.101 45.140 44.022 1.00 18.29 ? 20 ASN B CG 1 ATOM 4522 O OD1 . ASN B 1 20 ? 26.904 45.227 43.752 1.00 19.31 ? 20 ASN B OD1 1 ATOM 4523 N ND2 . ASN B 1 20 ? 28.553 45.101 45.268 1.00 18.49 ? 20 ASN B ND2 1 ATOM 4524 N N . THR B 1 21 ? 30.471 43.135 40.351 1.00 17.05 ? 21 THR B N 1 ATOM 4525 C CA . THR B 1 21 ? 31.329 43.115 39.163 1.00 17.02 ? 21 THR B CA 1 ATOM 4526 C C . THR B 1 21 ? 30.439 42.963 37.927 1.00 16.81 ? 21 THR B C 1 ATOM 4527 O O . THR B 1 21 ? 29.449 42.225 37.953 1.00 15.43 ? 21 THR B O 1 ATOM 4528 C CB . THR B 1 21 ? 32.303 41.902 39.200 1.00 17.68 ? 21 THR B CB 1 ATOM 4529 O OG1 . THR B 1 21 ? 33.087 41.952 40.394 1.00 17.67 ? 21 THR B OG1 1 ATOM 4530 C CG2 . THR B 1 21 ? 33.244 41.886 37.988 1.00 18.56 ? 21 THR B CG2 1 ATOM 4531 N N . ASP B 1 22 ? 30.774 43.692 36.866 1.00 16.14 ? 22 ASP B N 1 ATOM 4532 C CA . ASP B 1 22 ? 30.023 43.597 35.621 1.00 17.20 ? 22 ASP B CA 1 ATOM 4533 C C . ASP B 1 22 ? 30.526 42.339 34.897 1.00 16.72 ? 22 ASP B C 1 ATOM 4534 O O . ASP B 1 22 ? 31.536 42.368 34.190 1.00 15.96 ? 22 ASP B O 1 ATOM 4535 C CB . ASP B 1 22 ? 30.214 44.865 34.776 1.00 16.72 ? 22 ASP B CB 1 ATOM 4536 C CG . ASP B 1 22 ? 29.235 44.954 33.602 1.00 17.40 ? 22 ASP B CG 1 ATOM 4537 O OD1 . ASP B 1 22 ? 28.689 43.918 33.169 1.00 17.49 ? 22 ASP B OD1 1 ATOM 4538 O OD2 . ASP B 1 22 ? 29.024 46.072 33.094 1.00 19.04 ? 22 ASP B OD2 1 ATOM 4539 N N . TYR B 1 23 ? 29.794 41.243 35.102 1.00 16.18 ? 23 TYR B N 1 ATOM 4540 C CA . TYR B 1 23 ? 30.097 39.927 34.530 1.00 17.33 ? 23 TYR B CA 1 ATOM 4541 C C . TYR B 1 23 ? 30.073 39.855 33.000 1.00 17.81 ? 23 TYR B C 1 ATOM 4542 O O . TYR B 1 23 ? 30.683 38.960 32.414 1.00 19.87 ? 23 TYR B O 1 ATOM 4543 C CB . TYR B 1 23 ? 29.166 38.852 35.136 1.00 15.55 ? 23 TYR B CB 1 ATOM 4544 C CG . TYR B 1 23 ? 27.685 39.155 35.024 1.00 16.62 ? 23 TYR B CG 1 ATOM 4545 C CD1 . TYR B 1 23 ? 26.967 38.831 33.853 1.00 15.19 ? 23 TYR B CD1 1 ATOM 4546 C CD2 . TYR B 1 23 ? 27.000 39.825 36.063 1.00 16.52 ? 23 TYR B CD2 1 ATOM 4547 C CE1 . TYR B 1 23 ? 25.605 39.177 33.708 1.00 16.39 ? 23 TYR B CE1 1 ATOM 4548 C CE2 . TYR B 1 23 ? 25.626 40.170 35.930 1.00 15.01 ? 23 TYR B CE2 1 ATOM 4549 C CZ . TYR B 1 23 ? 24.946 39.842 34.744 1.00 15.60 ? 23 TYR B CZ 1 ATOM 4550 O OH . TYR B 1 23 ? 23.629 40.173 34.569 1.00 16.96 ? 23 TYR B OH 1 ATOM 4551 N N . GLU B 1 24 ? 29.338 40.777 32.372 1.00 19.38 ? 24 GLU B N 1 ATOM 4552 C CA . GLU B 1 24 ? 29.227 40.841 30.909 1.00 20.88 ? 24 GLU B CA 1 ATOM 4553 C C . GLU B 1 24 ? 30.510 41.298 30.220 1.00 21.20 ? 24 GLU B C 1 ATOM 4554 O O . GLU B 1 24 ? 30.661 41.123 29.007 1.00 20.84 ? 24 GLU B O 1 ATOM 4555 C CB . GLU B 1 24 ? 28.067 41.747 30.481 1.00 22.90 ? 24 GLU B CB 1 ATOM 4556 C CG . GLU B 1 24 ? 26.699 41.088 30.594 1.00 25.62 ? 24 GLU B CG 1 ATOM 4557 C CD . GLU B 1 24 ? 25.568 41.891 29.974 1.00 26.62 ? 24 GLU B CD 1 ATOM 4558 O OE1 . GLU B 1 24 ? 25.788 43.032 29.509 1.00 29.37 ? 24 GLU B OE1 1 ATOM 4559 O OE2 . GLU B 1 24 ? 24.438 41.367 29.952 1.00 29.27 ? 24 GLU B OE2 1 ATOM 4560 N N . VAL B 1 25 ? 31.415 41.906 30.990 1.00 20.85 ? 25 VAL B N 1 ATOM 4561 C CA . VAL B 1 25 ? 32.688 42.392 30.458 1.00 19.67 ? 25 VAL B CA 1 ATOM 4562 C C . VAL B 1 25 ? 33.937 41.904 31.219 1.00 20.16 ? 25 VAL B C 1 ATOM 4563 O O . VAL B 1 25 ? 35.052 41.974 30.694 1.00 20.13 ? 25 VAL B O 1 ATOM 4564 C CB . VAL B 1 25 ? 32.715 43.955 30.339 1.00 19.42 ? 25 VAL B CB 1 ATOM 4565 C CG1 . VAL B 1 25 ? 31.770 44.451 29.257 1.00 19.21 ? 25 VAL B CG1 1 ATOM 4566 C CG2 . VAL B 1 25 ? 32.414 44.618 31.672 1.00 18.32 ? 25 VAL B CG2 1 ATOM 4567 N N . SER B 1 26 ? 33.747 41.418 32.447 1.00 18.88 ? 26 SER B N 1 ATOM 4568 C CA . SER B 1 26 ? 34.851 40.929 33.279 1.00 18.27 ? 26 SER B CA 1 ATOM 4569 C C . SER B 1 26 ? 34.589 39.482 33.703 1.00 17.85 ? 26 SER B C 1 ATOM 4570 O O . SER B 1 26 ? 33.535 39.174 34.269 1.00 16.12 ? 26 SER B O 1 ATOM 4571 C CB . SER B 1 26 ? 35.031 41.840 34.496 1.00 18.68 ? 26 SER B CB 1 ATOM 4572 O OG . SER B 1 26 ? 36.215 41.528 35.199 1.00 21.05 ? 26 SER B OG 1 ATOM 4573 N N . THR B 1 27 ? 35.577 38.616 33.462 1.00 16.75 ? 27 THR B N 1 ATOM 4574 C CA . THR B 1 27 ? 35.473 37.180 33.742 1.00 18.10 ? 27 THR B CA 1 ATOM 4575 C C . THR B 1 27 ? 36.743 36.619 34.417 1.00 19.17 ? 27 THR B C 1 ATOM 4576 O O . THR B 1 27 ? 37.856 36.984 34.024 1.00 17.76 ? 27 THR B O 1 ATOM 4577 C CB . THR B 1 27 ? 35.242 36.410 32.388 1.00 19.05 ? 27 THR B CB 1 ATOM 4578 O OG1 . THR B 1 27 ? 34.172 37.026 31.658 1.00 18.45 ? 27 THR B OG1 1 ATOM 4579 C CG2 . THR B 1 27 ? 34.885 34.952 32.619 1.00 19.11 ? 27 THR B CG2 1 ATOM 4580 N N . PRO B 1 28 ? 36.595 35.750 35.458 1.00 18.84 ? 28 PRO B N 1 ATOM 4581 C CA . PRO B 1 28 ? 37.753 35.158 36.146 1.00 19.97 ? 28 PRO B CA 1 ATOM 4582 C C . PRO B 1 28 ? 38.517 34.208 35.240 1.00 20.10 ? 28 PRO B C 1 ATOM 4583 O O . PRO B 1 28 ? 37.909 33.482 34.454 1.00 18.09 ? 28 PRO B O 1 ATOM 4584 C CB . PRO B 1 28 ? 37.115 34.371 37.292 1.00 19.19 ? 28 PRO B CB 1 ATOM 4585 C CG . PRO B 1 28 ? 35.904 35.110 37.588 1.00 19.84 ? 28 PRO B CG 1 ATOM 4586 C CD . PRO B 1 28 ? 35.371 35.463 36.228 1.00 19.65 ? 28 PRO B CD 1 ATOM 4587 N N . ASP B 1 29 ? 39.843 34.262 35.316 1.00 21.22 ? 29 ASP B N 1 ATOM 4588 C CA . ASP B 1 29 ? 40.696 33.386 34.526 1.00 23.07 ? 29 ASP B CA 1 ATOM 4589 C C . ASP B 1 29 ? 41.106 32.248 35.465 1.00 23.35 ? 29 ASP B C 1 ATOM 4590 O O . ASP B 1 29 ? 42.153 32.306 36.120 1.00 24.24 ? 29 ASP B O 1 ATOM 4591 C CB . ASP B 1 29 ? 41.922 34.155 33.997 1.00 26.57 ? 29 ASP B CB 1 ATOM 4592 C CG . ASP B 1 29 ? 42.648 33.417 32.872 1.00 29.88 ? 29 ASP B CG 1 ATOM 4593 O OD1 . ASP B 1 29 ? 42.824 32.181 32.955 1.00 31.94 ? 29 ASP B OD1 1 ATOM 4594 O OD2 . ASP B 1 29 ? 43.048 34.083 31.894 1.00 36.70 ? 29 ASP B OD2 1 ATOM 4595 N N . THR B 1 30 ? 40.259 31.225 35.532 1.00 20.95 ? 30 THR B N 1 ATOM 4596 C CA . THR B 1 30 ? 40.500 30.070 36.397 1.00 22.16 ? 30 THR B CA 1 ATOM 4597 C C . THR B 1 30 ? 41.420 29.033 35.753 1.00 22.07 ? 30 THR B C 1 ATOM 4598 O O . THR B 1 30 ? 42.111 28.289 36.455 1.00 23.70 ? 30 THR B O 1 ATOM 4599 C CB . THR B 1 30 ? 39.184 29.359 36.774 1.00 21.45 ? 30 THR B CB 1 ATOM 4600 O OG1 . THR B 1 30 ? 38.620 28.752 35.605 1.00 21.08 ? 30 THR B OG1 1 ATOM 4601 C CG2 . THR B 1 30 ? 38.174 30.344 37.373 1.00 21.41 ? 30 THR B CG2 1 ATOM 4602 N N . GLY B 1 31 ? 41.355 28.949 34.421 1.00 22.29 ? 31 GLY B N 1 ATOM 4603 C CA . GLY B 1 31 ? 42.154 27.999 33.658 1.00 21.83 ? 31 GLY B CA 1 ATOM 4604 C C . GLY B 1 31 ? 41.650 26.569 33.772 1.00 21.64 ? 31 GLY B C 1 ATOM 4605 O O . GLY B 1 31 ? 42.302 25.640 33.296 1.00 21.99 ? 31 GLY B O 1 ATOM 4606 N N . VAL B 1 32 ? 40.490 26.402 34.410 1.00 21.47 ? 32 VAL B N 1 ATOM 4607 C CA . VAL B 1 32 ? 39.871 25.092 34.624 1.00 19.91 ? 32 VAL B CA 1 ATOM 4608 C C . VAL B 1 32 ? 38.809 24.803 33.558 1.00 19.82 ? 32 VAL B C 1 ATOM 4609 O O . VAL B 1 32 ? 38.094 25.703 33.107 1.00 18.94 ? 32 VAL B O 1 ATOM 4610 C CB . VAL B 1 32 ? 39.235 24.991 36.059 1.00 20.94 ? 32 VAL B CB 1 ATOM 4611 C CG1 . VAL B 1 32 ? 38.656 23.594 36.329 1.00 21.83 ? 32 VAL B CG1 1 ATOM 4612 C CG2 . VAL B 1 32 ? 40.275 25.318 37.129 1.00 22.72 ? 32 VAL B CG2 1 ATOM 4613 N N . THR B 1 33 ? 38.744 23.537 33.158 1.00 18.47 ? 33 THR B N 1 ATOM 4614 C CA . THR B 1 33 ? 37.786 23.054 32.177 1.00 18.21 ? 33 THR B CA 1 ATOM 4615 C C . THR B 1 33 ? 37.007 21.883 32.773 1.00 17.68 ? 33 THR B C 1 ATOM 4616 O O . THR B 1 33 ? 37.597 20.954 33.330 1.00 17.91 ? 33 THR B O 1 ATOM 4617 C CB . THR B 1 33 ? 38.493 22.618 30.853 1.00 17.66 ? 33 THR B CB 1 ATOM 4618 O OG1 . THR B 1 33 ? 39.064 23.767 30.222 1.00 16.66 ? 33 THR B OG1 1 ATOM 4619 C CG2 . THR B 1 33 ? 37.521 21.969 29.870 1.00 17.91 ? 33 THR B CG2 1 ATOM 4620 N N . GLN B 1 34 ? 35.679 21.975 32.707 1.00 18.07 ? 34 GLN B N 1 ATOM 4621 C CA . GLN B 1 34 ? 34.805 20.905 33.181 1.00 18.71 ? 34 GLN B CA 1 ATOM 4622 C C . GLN B 1 34 ? 34.247 20.236 31.936 1.00 19.46 ? 34 GLN B C 1 ATOM 4623 O O . GLN B 1 34 ? 33.496 20.847 31.164 1.00 21.13 ? 34 GLN B O 1 ATOM 4624 C CB . GLN B 1 34 ? 33.678 21.433 34.084 1.00 19.71 ? 34 GLN B CB 1 ATOM 4625 C CG . GLN B 1 34 ? 34.133 21.937 35.466 1.00 21.16 ? 34 GLN B CG 1 ATOM 4626 C CD . GLN B 1 34 ? 34.707 20.854 36.385 1.00 23.57 ? 34 GLN B CD 1 ATOM 4627 O OE1 . GLN B 1 34 ? 34.372 19.668 36.282 1.00 23.52 ? 34 GLN B OE1 1 ATOM 4628 N NE2 . GLN B 1 34 ? 35.566 21.273 37.308 1.00 23.91 ? 34 GLN B NE2 1 ATOM 4629 N N . SER B 1 35 ? 34.678 18.995 31.726 1.00 18.91 ? 35 SER B N 1 ATOM 4630 C CA . SER B 1 35 ? 34.293 18.198 30.570 1.00 18.60 ? 35 SER B CA 1 ATOM 4631 C C . SER B 1 35 ? 33.191 17.178 30.815 1.00 17.13 ? 35 SER B C 1 ATOM 4632 O O . SER B 1 35 ? 33.062 16.638 31.919 1.00 15.62 ? 35 SER B O 1 ATOM 4633 C CB . SER B 1 35 ? 35.523 17.505 30.001 1.00 19.46 ? 35 SER B CB 1 ATOM 4634 O OG . SER B 1 35 ? 36.454 18.458 29.517 1.00 25.22 ? 35 SER B OG 1 ATOM 4635 N N . TYR B 1 36 ? 32.363 16.975 29.785 1.00 14.78 ? 36 TYR B N 1 ATOM 4636 C CA . TYR B 1 36 ? 31.231 16.040 29.811 1.00 15.08 ? 36 TYR B CA 1 ATOM 4637 C C . TYR B 1 36 ? 31.098 15.371 28.446 1.00 14.75 ? 36 TYR B C 1 ATOM 4638 O O . TYR B 1 36 ? 31.588 15.893 27.444 1.00 15.29 ? 36 TYR B O 1 ATOM 4639 C CB . TYR B 1 36 ? 29.895 16.769 30.094 1.00 15.54 ? 36 TYR B CB 1 ATOM 4640 C CG . TYR B 1 36 ? 29.815 17.524 31.404 1.00 15.63 ? 36 TYR B CG 1 ATOM 4641 C CD1 . TYR B 1 36 ? 30.266 18.855 31.490 1.00 17.04 ? 36 TYR B CD1 1 ATOM 4642 C CD2 . TYR B 1 36 ? 29.353 16.897 32.581 1.00 15.37 ? 36 TYR B CD2 1 ATOM 4643 C CE1 . TYR B 1 36 ? 30.277 19.549 32.719 1.00 18.66 ? 36 TYR B CE1 1 ATOM 4644 C CE2 . TYR B 1 36 ? 29.353 17.588 33.826 1.00 18.29 ? 36 TYR B CE2 1 ATOM 4645 C CZ . TYR B 1 36 ? 29.822 18.913 33.876 1.00 17.60 ? 36 TYR B CZ 1 ATOM 4646 O OH . TYR B 1 36 ? 29.848 19.609 35.060 1.00 20.77 ? 36 TYR B OH 1 ATOM 4647 N N . VAL B 1 37 ? 30.467 14.199 28.421 1.00 15.11 ? 37 VAL B N 1 ATOM 4648 C CA . VAL B 1 37 ? 30.212 13.468 27.179 1.00 16.61 ? 37 VAL B CA 1 ATOM 4649 C C . VAL B 1 37 ? 28.721 13.131 27.172 1.00 18.36 ? 37 VAL B C 1 ATOM 4650 O O . VAL B 1 37 ? 28.192 12.566 28.136 1.00 19.50 ? 37 VAL B O 1 ATOM 4651 C CB . VAL B 1 37 ? 31.097 12.174 27.019 1.00 18.44 ? 37 VAL B CB 1 ATOM 4652 C CG1 . VAL B 1 37 ? 30.698 11.382 25.766 1.00 17.29 ? 37 VAL B CG1 1 ATOM 4653 C CG2 . VAL B 1 37 ? 32.576 12.548 26.884 1.00 18.55 ? 37 VAL B CG2 1 ATOM 4654 N N . PHE B 1 38 ? 28.039 13.585 26.123 1.00 17.85 ? 38 PHE B N 1 ATOM 4655 C CA . PHE B 1 38 ? 26.608 13.356 25.945 1.00 18.09 ? 38 PHE B CA 1 ATOM 4656 C C . PHE B 1 38 ? 26.377 12.280 24.897 1.00 19.28 ? 38 PHE B C 1 ATOM 4657 O O . PHE B 1 38 ? 26.668 12.483 23.715 1.00 19.46 ? 38 PHE B O 1 ATOM 4658 C CB . PHE B 1 38 ? 25.889 14.629 25.458 1.00 17.56 ? 38 PHE B CB 1 ATOM 4659 C CG . PHE B 1 38 ? 25.712 15.713 26.493 1.00 16.26 ? 38 PHE B CG 1 ATOM 4660 C CD1 . PHE B 1 38 ? 26.313 15.652 27.773 1.00 16.52 ? 38 PHE B CD1 1 ATOM 4661 C CD2 . PHE B 1 38 ? 24.972 16.857 26.150 1.00 15.82 ? 38 PHE B CD2 1 ATOM 4662 C CE1 . PHE B 1 38 ? 26.187 16.725 28.689 1.00 16.31 ? 38 PHE B CE1 1 ATOM 4663 C CE2 . PHE B 1 38 ? 24.838 17.931 27.050 1.00 14.82 ? 38 PHE B CE2 1 ATOM 4664 C CZ . PHE B 1 38 ? 25.451 17.866 28.326 1.00 14.35 ? 38 PHE B CZ 1 ATOM 4665 N N . ASN B 1 39 ? 25.855 11.140 25.333 1.00 19.96 ? 39 ASN B N 1 ATOM 4666 C CA . ASN B 1 39 ? 25.551 10.042 24.429 1.00 20.52 ? 39 ASN B CA 1 ATOM 4667 C C . ASN B 1 39 ? 24.030 10.027 24.271 1.00 20.49 ? 39 ASN B C 1 ATOM 4668 O O . ASN B 1 39 ? 23.302 9.646 25.194 1.00 18.36 ? 39 ASN B O 1 ATOM 4669 C CB . ASN B 1 39 ? 26.068 8.713 25.006 1.00 23.95 ? 39 ASN B CB 1 ATOM 4670 C CG . ASN B 1 39 ? 25.908 7.534 24.047 1.00 27.13 ? 39 ASN B CG 1 ATOM 4671 O OD1 . ASN B 1 39 ? 25.267 7.630 22.993 1.00 24.58 ? 39 ASN B OD1 1 ATOM 4672 N ND2 . ASN B 1 39 ? 26.499 6.410 24.432 1.00 29.88 ? 39 ASN B ND2 1 ATOM 4673 N N . LEU B 1 40 ? 23.565 10.457 23.098 1.00 19.38 ? 40 LEU B N 1 ATOM 4674 C CA . LEU B 1 40 ? 22.138 10.496 22.797 1.00 18.68 ? 40 LEU B CA 1 ATOM 4675 C C . LEU B 1 40 ? 21.692 9.152 22.259 1.00 18.27 ? 40 LEU B C 1 ATOM 4676 O O . LEU B 1 40 ? 22.221 8.693 21.256 1.00 16.25 ? 40 LEU B O 1 ATOM 4677 C CB . LEU B 1 40 ? 21.813 11.562 21.746 1.00 18.29 ? 40 LEU B CB 1 ATOM 4678 C CG . LEU B 1 40 ? 22.173 13.049 21.792 1.00 19.33 ? 40 LEU B CG 1 ATOM 4679 C CD1 . LEU B 1 40 ? 20.950 13.788 21.318 1.00 16.82 ? 40 LEU B CD1 1 ATOM 4680 C CD2 . LEU B 1 40 ? 22.584 13.553 23.153 1.00 18.92 ? 40 LEU B CD2 1 ATOM 4681 N N . THR B 1 41 ? 20.755 8.504 22.947 1.00 16.57 ? 41 THR B N 1 ATOM 4682 C CA . THR B 1 41 ? 20.240 7.207 22.502 1.00 16.82 ? 41 THR B CA 1 ATOM 4683 C C . THR B 1 41 ? 18.732 7.276 22.309 1.00 16.85 ? 41 THR B C 1 ATOM 4684 O O . THR B 1 41 ? 18.051 8.082 22.949 1.00 16.48 ? 41 THR B O 1 ATOM 4685 C CB . THR B 1 41 ? 20.558 6.057 23.498 1.00 15.15 ? 41 THR B CB 1 ATOM 4686 O OG1 . THR B 1 41 ? 20.046 6.384 24.796 1.00 16.37 ? 41 THR B OG1 1 ATOM 4687 C CG2 . THR B 1 41 ? 22.058 5.796 23.583 1.00 15.05 ? 41 THR B CG2 1 ATOM 4688 N N . GLU B 1 42 ? 18.230 6.448 21.398 1.00 16.63 ? 42 GLU B N 1 ATOM 4689 C CA . GLU B 1 42 ? 16.804 6.376 21.103 1.00 18.84 ? 42 GLU B CA 1 ATOM 4690 C C . GLU B 1 42 ? 16.261 5.127 21.781 1.00 19.02 ? 42 GLU B C 1 ATOM 4691 O O . GLU B 1 42 ? 16.623 4.005 21.415 1.00 21.03 ? 42 GLU B O 1 ATOM 4692 C CB . GLU B 1 42 ? 16.589 6.309 19.592 1.00 17.67 ? 42 GLU B CB 1 ATOM 4693 C CG . GLU B 1 42 ? 15.194 6.686 19.139 1.00 18.04 ? 42 GLU B CG 1 ATOM 4694 C CD . GLU B 1 42 ? 15.167 7.148 17.698 1.00 18.04 ? 42 GLU B CD 1 ATOM 4695 O OE1 . GLU B 1 42 ? 16.073 7.912 17.302 1.00 17.58 ? 42 GLU B OE1 1 ATOM 4696 O OE2 . GLU B 1 42 ? 14.247 6.747 16.956 1.00 17.21 ? 42 GLU B OE2 1 ATOM 4697 N N . VAL B 1 43 ? 15.436 5.333 22.805 1.00 18.92 ? 43 VAL B N 1 ATOM 4698 C CA . VAL B 1 43 ? 14.853 4.232 23.567 1.00 18.68 ? 43 VAL B CA 1 ATOM 4699 C C . VAL B 1 43 ? 13.352 4.114 23.313 1.00 19.95 ? 43 VAL B C 1 ATOM 4700 O O . VAL B 1 43 ? 12.593 5.070 23.513 1.00 20.00 ? 43 VAL B O 1 ATOM 4701 C CB . VAL B 1 43 ? 15.120 4.381 25.106 1.00 18.36 ? 43 VAL B CB 1 ATOM 4702 C CG1 . VAL B 1 43 ? 14.682 3.118 25.854 1.00 16.87 ? 43 VAL B CG1 1 ATOM 4703 C CG2 . VAL B 1 43 ? 16.603 4.660 25.386 1.00 17.79 ? 43 VAL B CG2 1 ATOM 4704 N N . ASP B 1 44 ? 12.945 2.931 22.857 1.00 20.09 ? 44 ASP B N 1 ATOM 4705 C CA . ASP B 1 44 ? 11.545 2.627 22.582 1.00 19.48 ? 44 ASP B CA 1 ATOM 4706 C C . ASP B 1 44 ? 10.941 1.917 23.786 1.00 20.27 ? 44 ASP B C 1 ATOM 4707 O O . ASP B 1 44 ? 11.642 1.200 24.505 1.00 19.26 ? 44 ASP B O 1 ATOM 4708 C CB . ASP B 1 44 ? 11.402 1.739 21.338 1.00 20.49 ? 44 ASP B CB 1 ATOM 4709 C CG . ASP B 1 44 ? 11.894 2.417 20.067 1.00 23.45 ? 44 ASP B CG 1 ATOM 4710 O OD1 . ASP B 1 44 ? 11.728 3.647 19.929 1.00 23.15 ? 44 ASP B OD1 1 ATOM 4711 O OD2 . ASP B 1 44 ? 12.450 1.710 19.201 1.00 23.29 ? 44 ASP B OD2 1 ATOM 4712 N N . ASN B 1 45 ? 9.642 2.144 24.003 1.00 19.67 ? 45 ASN B N 1 ATOM 4713 C CA . ASN B 1 45 ? 8.865 1.558 25.105 1.00 20.13 ? 45 ASN B CA 1 ATOM 4714 C C . ASN B 1 45 ? 9.547 1.721 26.475 1.00 21.09 ? 45 ASN B C 1 ATOM 4715 O O . ASN B 1 45 ? 9.763 0.762 27.219 1.00 20.01 ? 45 ASN B O 1 ATOM 4716 C CB . ASN B 1 45 ? 8.502 0.100 24.790 1.00 19.58 ? 45 ASN B CB 1 ATOM 4717 C CG . ASN B 1 45 ? 7.866 -0.049 23.422 1.00 19.56 ? 45 ASN B CG 1 ATOM 4718 O OD1 . ASN B 1 45 ? 6.709 0.317 23.217 1.00 19.95 ? 45 ASN B OD1 1 ATOM 4719 N ND2 . ASN B 1 45 ? 8.642 -0.543 22.463 1.00 19.68 ? 45 ASN B ND2 1 ATOM 4720 N N . TRP B 1 46 ? 9.882 2.974 26.772 1.00 22.31 ? 46 TRP B N 1 ATOM 4721 C CA . TRP B 1 46 ? 10.568 3.366 27.996 1.00 22.18 ? 46 TRP B CA 1 ATOM 4722 C C . TRP B 1 46 ? 9.617 3.660 29.150 1.00 23.33 ? 46 TRP B C 1 ATOM 4723 O O . TRP B 1 46 ? 8.690 4.466 29.019 1.00 23.81 ? 46 TRP B O 1 ATOM 4724 C CB . TRP B 1 46 ? 11.447 4.581 27.684 1.00 22.40 ? 46 TRP B CB 1 ATOM 4725 C CG . TRP B 1 46 ? 12.216 5.195 28.832 1.00 23.02 ? 46 TRP B CG 1 ATOM 4726 C CD1 . TRP B 1 46 ? 13.401 4.756 29.361 1.00 23.35 ? 46 TRP B CD1 1 ATOM 4727 C CD2 . TRP B 1 46 ? 11.888 6.403 29.528 1.00 22.89 ? 46 TRP B CD2 1 ATOM 4728 N NE1 . TRP B 1 46 ? 13.836 5.623 30.339 1.00 24.63 ? 46 TRP B NE1 1 ATOM 4729 C CE2 . TRP B 1 46 ? 12.930 6.643 30.466 1.00 22.57 ? 46 TRP B CE2 1 ATOM 4730 C CE3 . TRP B 1 46 ? 10.813 7.316 29.450 1.00 22.48 ? 46 TRP B CE3 1 ATOM 4731 C CZ2 . TRP B 1 46 ? 12.934 7.765 31.328 1.00 22.73 ? 46 TRP B CZ2 1 ATOM 4732 C CZ3 . TRP B 1 46 ? 10.811 8.444 30.309 1.00 23.15 ? 46 TRP B CZ3 1 ATOM 4733 C CH2 . TRP B 1 46 ? 11.871 8.650 31.235 1.00 22.75 ? 46 TRP B CH2 1 ATOM 4734 N N . MET B 1 47 ? 9.922 3.055 30.296 1.00 23.66 ? 47 MET B N 1 ATOM 4735 C CA . MET B 1 47 ? 9.145 3.220 31.520 1.00 24.81 ? 47 MET B CA 1 ATOM 4736 C C . MET B 1 47 ? 9.438 4.586 32.142 1.00 23.71 ? 47 MET B C 1 ATOM 4737 O O . MET B 1 47 ? 10.559 4.856 32.594 1.00 22.82 ? 47 MET B O 1 ATOM 4738 C CB . MET B 1 47 ? 9.464 2.085 32.509 1.00 27.35 ? 47 MET B CB 1 ATOM 4739 C CG . MET B 1 47 ? 8.781 2.187 33.877 1.00 31.57 ? 47 MET B CG 1 ATOM 4740 S SD . MET B 1 47 ? 6.991 2.302 33.761 1.00 36.51 ? 47 MET B SD 1 ATOM 4741 C CE . MET B 1 47 ? 6.536 0.579 34.027 1.00 34.52 ? 47 MET B CE 1 ATOM 4742 N N . GLY B 1 48 ? 8.415 5.438 32.133 1.00 22.67 ? 48 GLY B N 1 ATOM 4743 C CA . GLY B 1 48 ? 8.523 6.774 32.689 1.00 22.09 ? 48 GLY B CA 1 ATOM 4744 C C . GLY B 1 48 ? 8.375 6.829 34.201 1.00 21.49 ? 48 GLY B C 1 ATOM 4745 O O . GLY B 1 48 ? 7.958 5.837 34.807 1.00 21.74 ? 48 GLY B O 1 ATOM 4746 N N . PRO B 1 49 ? 8.676 7.982 34.837 1.00 20.83 ? 49 PRO B N 1 ATOM 4747 C CA . PRO B 1 49 ? 8.581 8.163 36.291 1.00 20.84 ? 49 PRO B CA 1 ATOM 4748 C C . PRO B 1 49 ? 7.194 8.088 36.924 1.00 21.16 ? 49 PRO B C 1 ATOM 4749 O O . PRO B 1 49 ? 7.088 7.915 38.139 1.00 20.11 ? 49 PRO B O 1 ATOM 4750 C CB . PRO B 1 49 ? 9.236 9.523 36.508 1.00 21.15 ? 49 PRO B CB 1 ATOM 4751 C CG . PRO B 1 49 ? 8.949 10.240 35.241 1.00 21.29 ? 49 PRO B CG 1 ATOM 4752 C CD . PRO B 1 49 ? 9.217 9.200 34.206 1.00 19.91 ? 49 PRO B CD 1 ATOM 4753 N N . ASP B 1 50 ? 6.144 8.236 36.114 1.00 22.06 ? 50 ASP B N 1 ATOM 4754 C CA . ASP B 1 50 ? 4.780 8.154 36.633 1.00 22.72 ? 50 ASP B CA 1 ATOM 4755 C C . ASP B 1 50 ? 4.114 6.792 36.368 1.00 23.06 ? 50 ASP B C 1 ATOM 4756 O O . ASP B 1 50 ? 2.899 6.643 36.500 1.00 23.12 ? 50 ASP B O 1 ATOM 4757 C CB . ASP B 1 50 ? 3.918 9.354 36.167 1.00 22.93 ? 50 ASP B CB 1 ATOM 4758 C CG . ASP B 1 50 ? 3.556 9.321 34.678 1.00 22.06 ? 50 ASP B CG 1 ATOM 4759 O OD1 . ASP B 1 50 ? 4.124 8.528 33.903 1.00 19.39 ? 50 ASP B OD1 1 ATOM 4760 O OD2 . ASP B 1 50 ? 2.681 10.118 34.287 1.00 24.19 ? 50 ASP B OD2 1 ATOM 4761 N N . GLY B 1 51 ? 4.929 5.811 35.982 1.00 22.77 ? 51 GLY B N 1 ATOM 4762 C CA . GLY B 1 51 ? 4.436 4.466 35.722 1.00 23.96 ? 51 GLY B CA 1 ATOM 4763 C C . GLY B 1 51 ? 3.996 4.158 34.304 1.00 23.16 ? 51 GLY B C 1 ATOM 4764 O O . GLY B 1 51 ? 3.890 2.987 33.935 1.00 24.25 ? 51 GLY B O 1 ATOM 4765 N N . VAL B 1 52 ? 3.738 5.196 33.509 1.00 22.51 ? 52 VAL B N 1 ATOM 4766 C CA . VAL B 1 52 ? 3.302 5.020 32.125 1.00 20.80 ? 52 VAL B CA 1 ATOM 4767 C C . VAL B 1 52 ? 4.504 4.801 31.210 1.00 21.18 ? 52 VAL B C 1 ATOM 4768 O O . VAL B 1 52 ? 5.554 5.423 31.377 1.00 22.22 ? 52 VAL B O 1 ATOM 4769 C CB . VAL B 1 52 ? 2.443 6.224 31.643 1.00 21.36 ? 52 VAL B CB 1 ATOM 4770 C CG1 . VAL B 1 52 ? 2.000 6.060 30.185 1.00 20.07 ? 52 VAL B CG1 1 ATOM 4771 C CG2 . VAL B 1 52 ? 1.214 6.367 32.524 1.00 20.77 ? 52 VAL B CG2 1 ATOM 4772 N N . VAL B 1 53 ? 4.328 3.882 30.267 1.00 20.25 ? 53 VAL B N 1 ATOM 4773 C CA . VAL B 1 53 ? 5.349 3.517 29.296 1.00 19.87 ? 53 VAL B CA 1 ATOM 4774 C C . VAL B 1 53 ? 5.178 4.374 28.035 1.00 20.55 ? 53 VAL B C 1 ATOM 4775 O O . VAL B 1 53 ? 4.103 4.397 27.433 1.00 20.86 ? 53 VAL B O 1 ATOM 4776 C CB . VAL B 1 53 ? 5.256 1.990 28.971 1.00 20.54 ? 53 VAL B CB 1 ATOM 4777 C CG1 . VAL B 1 53 ? 6.265 1.582 27.934 1.00 20.35 ? 53 VAL B CG1 1 ATOM 4778 C CG2 . VAL B 1 53 ? 5.478 1.165 30.234 1.00 20.27 ? 53 VAL B CG2 1 ATOM 4779 N N . LYS B 1 54 ? 6.238 5.096 27.669 1.00 19.96 ? 54 LYS B N 1 ATOM 4780 C CA . LYS B 1 54 ? 6.234 5.958 26.483 1.00 19.58 ? 54 LYS B CA 1 ATOM 4781 C C . LYS B 1 54 ? 6.735 5.245 25.243 1.00 19.25 ? 54 LYS B C 1 ATOM 4782 O O . LYS B 1 54 ? 7.734 4.534 25.302 1.00 18.25 ? 54 LYS B O 1 ATOM 4783 C CB . LYS B 1 54 ? 7.094 7.199 26.706 1.00 18.03 ? 54 LYS B CB 1 ATOM 4784 C CG . LYS B 1 54 ? 6.436 8.266 27.549 1.00 17.35 ? 54 LYS B CG 1 ATOM 4785 C CD . LYS B 1 54 ? 7.244 9.552 27.561 1.00 17.00 ? 54 LYS B CD 1 ATOM 4786 C CE . LYS B 1 54 ? 7.277 10.242 26.206 1.00 14.91 ? 54 LYS B CE 1 ATOM 4787 N NZ . LYS B 1 54 ? 7.823 11.613 26.329 1.00 16.21 ? 54 LYS B NZ 1 ATOM 4788 N N . GLU B 1 55 ? 6.076 5.515 24.115 1.00 19.76 ? 55 GLU B N 1 ATOM 4789 C CA . GLU B 1 55 ? 6.400 4.942 22.802 1.00 20.68 ? 55 GLU B CA 1 ATOM 4790 C C . GLU B 1 55 ? 7.879 5.121 22.428 1.00 20.83 ? 55 GLU B C 1 ATOM 4791 O O . GLU B 1 55 ? 8.580 4.141 22.168 1.00 20.36 ? 55 GLU B O 1 ATOM 4792 C CB . GLU B 1 55 ? 5.515 5.597 21.731 1.00 21.57 ? 55 GLU B CB 1 ATOM 4793 C CG . GLU B 1 55 ? 5.662 5.033 20.317 1.00 25.84 ? 55 GLU B CG 1 ATOM 4794 C CD . GLU B 1 55 ? 5.065 5.932 19.239 1.00 26.79 ? 55 GLU B CD 1 ATOM 4795 O OE1 . GLU B 1 55 ? 4.095 6.670 19.516 1.00 26.56 ? 55 GLU B OE1 1 ATOM 4796 O OE2 . GLU B 1 55 ? 5.573 5.891 18.100 1.00 29.64 ? 55 GLU B OE2 1 ATOM 4797 N N . LYS B 1 56 ? 8.346 6.370 22.467 1.00 20.25 ? 56 LYS B N 1 ATOM 4798 C CA . LYS B 1 56 ? 9.723 6.695 22.115 1.00 19.85 ? 56 LYS B CA 1 ATOM 4799 C C . LYS B 1 56 ? 10.236 7.930 22.851 1.00 20.45 ? 56 LYS B C 1 ATOM 4800 O O . LYS B 1 56 ? 9.509 8.911 23.038 1.00 18.85 ? 56 LYS B O 1 ATOM 4801 C CB . LYS B 1 56 ? 9.828 6.917 20.598 1.00 19.59 ? 56 LYS B CB 1 ATOM 4802 C CG . LYS B 1 56 ? 11.249 7.087 20.061 1.00 19.64 ? 56 LYS B CG 1 ATOM 4803 C CD . LYS B 1 56 ? 11.256 7.455 18.585 1.00 18.46 ? 56 LYS B CD 1 ATOM 4804 C CE . LYS B 1 56 ? 10.938 6.271 17.676 1.00 20.92 ? 56 LYS B CE 1 ATOM 4805 N NZ . LYS B 1 56 ? 11.984 5.212 17.748 1.00 20.77 ? 56 LYS B NZ 1 ATOM 4806 N N . VAL B 1 57 ? 11.480 7.834 23.316 1.00 19.72 ? 57 VAL B N 1 ATOM 4807 C CA . VAL B 1 57 ? 12.173 8.923 23.998 1.00 18.30 ? 57 VAL B CA 1 ATOM 4808 C C . VAL B 1 57 ? 13.599 8.986 23.456 1.00 18.63 ? 57 VAL B C 1 ATOM 4809 O O . VAL B 1 57 ? 14.111 8.008 22.902 1.00 17.53 ? 57 VAL B O 1 ATOM 4810 C CB . VAL B 1 57 ? 12.230 8.759 25.554 1.00 19.49 ? 57 VAL B CB 1 ATOM 4811 C CG1 . VAL B 1 57 ? 10.863 8.926 26.179 1.00 14.88 ? 57 VAL B CG1 1 ATOM 4812 C CG2 . VAL B 1 57 ? 12.829 7.435 25.940 1.00 18.36 ? 57 VAL B CG2 1 ATOM 4813 N N . MET B 1 58 ? 14.218 10.156 23.587 1.00 17.82 ? 58 MET B N 1 ATOM 4814 C CA . MET B 1 58 ? 15.587 10.387 23.133 1.00 17.65 ? 58 MET B CA 1 ATOM 4815 C C . MET B 1 58 ? 16.326 10.925 24.349 1.00 18.31 ? 58 MET B C 1 ATOM 4816 O O . MET B 1 58 ? 16.133 12.070 24.760 1.00 18.17 ? 58 MET B O 1 ATOM 4817 C CB . MET B 1 58 ? 15.595 11.359 21.952 1.00 15.80 ? 58 MET B CB 1 ATOM 4818 C CG . MET B 1 58 ? 14.917 10.785 20.712 1.00 14.57 ? 58 MET B CG 1 ATOM 4819 S SD . MET B 1 58 ? 14.656 11.948 19.400 1.00 15.23 ? 58 MET B SD 1 ATOM 4820 C CE . MET B 1 58 ? 13.671 10.949 18.260 1.00 11.17 ? 58 MET B CE 1 ATOM 4821 N N . LEU B 1 59 ? 17.130 10.051 24.953 1.00 17.75 ? 59 LEU B N 1 ATOM 4822 C CA . LEU B 1 59 ? 17.847 10.358 26.187 1.00 16.47 ? 59 LEU B CA 1 ATOM 4823 C C . LEU B 1 59 ? 19.340 10.574 26.087 1.00 17.18 ? 59 LEU B C 1 ATOM 4824 O O . LEU B 1 59 ? 20.009 9.997 25.234 1.00 16.01 ? 59 LEU B O 1 ATOM 4825 C CB . LEU B 1 59 ? 17.609 9.238 27.208 1.00 15.17 ? 59 LEU B CB 1 ATOM 4826 C CG . LEU B 1 59 ? 16.199 8.694 27.442 1.00 16.53 ? 59 LEU B CG 1 ATOM 4827 C CD1 . LEU B 1 59 ? 16.248 7.492 28.370 1.00 14.07 ? 59 LEU B CD1 1 ATOM 4828 C CD2 . LEU B 1 59 ? 15.287 9.778 27.989 1.00 15.63 ? 59 LEU B CD2 1 ATOM 4829 N N . ILE B 1 60 ? 19.849 11.373 27.023 1.00 16.09 ? 60 ILE B N 1 ATOM 4830 C CA . ILE B 1 60 ? 21.272 11.666 27.136 1.00 16.56 ? 60 ILE B CA 1 ATOM 4831 C C . ILE B 1 60 ? 21.788 10.800 28.293 1.00 18.10 ? 60 ILE B C 1 ATOM 4832 O O . ILE B 1 60 ? 21.296 10.910 29.427 1.00 16.22 ? 60 ILE B O 1 ATOM 4833 C CB . ILE B 1 60 ? 21.527 13.153 27.471 1.00 17.24 ? 60 ILE B CB 1 ATOM 4834 C CG1 . ILE B 1 60 ? 20.897 14.071 26.424 1.00 16.53 ? 60 ILE B CG1 1 ATOM 4835 C CG2 . ILE B 1 60 ? 23.021 13.413 27.621 1.00 18.55 ? 60 ILE B CG2 1 ATOM 4836 C CD1 . ILE B 1 60 ? 20.951 15.543 26.780 1.00 17.45 ? 60 ILE B CD1 1 ATOM 4837 N N . ASN B 1 61 ? 22.772 9.947 27.987 1.00 17.12 ? 61 ASN B N 1 ATOM 4838 C CA . ASN B 1 61 ? 23.412 9.022 28.941 1.00 18.56 ? 61 ASN B CA 1 ATOM 4839 C C . ASN B 1 61 ? 22.444 8.066 29.667 1.00 18.48 ? 61 ASN B C 1 ATOM 4840 O O . ASN B 1 61 ? 22.623 7.745 30.847 1.00 17.96 ? 61 ASN B O 1 ATOM 4841 C CB . ASN B 1 61 ? 24.321 9.784 29.932 1.00 17.21 ? 61 ASN B CB 1 ATOM 4842 C CG . ASN B 1 61 ? 25.448 10.548 29.236 1.00 17.27 ? 61 ASN B CG 1 ATOM 4843 O OD1 . ASN B 1 61 ? 25.746 10.319 28.062 1.00 16.06 ? 61 ASN B OD1 1 ATOM 4844 N ND2 . ASN B 1 61 ? 26.071 11.467 29.963 1.00 15.05 ? 61 ASN B ND2 1 ATOM 4845 N N . GLY B 1 62 ? 21.393 7.668 28.947 1.00 18.50 ? 62 GLY B N 1 ATOM 4846 C CA . GLY B 1 62 ? 20.386 6.748 29.460 1.00 19.10 ? 62 GLY B CA 1 ATOM 4847 C C . GLY B 1 62 ? 19.434 7.214 30.549 1.00 18.83 ? 62 GLY B C 1 ATOM 4848 O O . GLY B 1 62 ? 18.704 6.390 31.105 1.00 17.57 ? 62 GLY B O 1 ATOM 4849 N N . ASN B 1 63 ? 19.436 8.512 30.862 1.00 17.88 ? 63 ASN B N 1 ATOM 4850 C CA . ASN B 1 63 ? 18.555 9.060 31.901 1.00 19.73 ? 63 ASN B CA 1 ATOM 4851 C C . ASN B 1 63 ? 17.529 10.042 31.338 1.00 19.60 ? 63 ASN B C 1 ATOM 4852 O O . ASN B 1 63 ? 17.695 10.538 30.225 1.00 18.93 ? 63 ASN B O 1 ATOM 4853 C CB . ASN B 1 63 ? 19.376 9.736 33.007 1.00 21.63 ? 63 ASN B CB 1 ATOM 4854 C CG . ASN B 1 63 ? 20.333 8.781 33.695 1.00 23.55 ? 63 ASN B CG 1 ATOM 4855 O OD1 . ASN B 1 63 ? 19.969 7.651 34.031 1.00 24.96 ? 63 ASN B OD1 1 ATOM 4856 N ND2 . ASN B 1 63 ? 21.569 9.226 33.894 1.00 23.97 ? 63 ASN B ND2 1 ATOM 4857 N N . ILE B 1 64 ? 16.503 10.352 32.137 1.00 19.13 ? 64 ILE B N 1 ATOM 4858 C CA . ILE B 1 64 ? 15.419 11.270 31.759 1.00 18.83 ? 64 ILE B CA 1 ATOM 4859 C C . ILE B 1 64 ? 15.947 12.654 31.348 1.00 17.27 ? 64 ILE B C 1 ATOM 4860 O O . ILE B 1 64 ? 15.426 13.287 30.428 1.00 19.29 ? 64 ILE B O 1 ATOM 4861 C CB . ILE B 1 64 ? 14.337 11.359 32.889 1.00 19.17 ? 64 ILE B CB 1 ATOM 4862 C CG1 . ILE B 1 64 ? 13.098 12.108 32.387 1.00 22.00 ? 64 ILE B CG1 1 ATOM 4863 C CG2 . ILE B 1 64 ? 14.921 11.959 34.185 1.00 19.16 ? 64 ILE B CG2 1 ATOM 4864 C CD1 . ILE B 1 64 ? 11.889 11.937 33.259 1.00 21.24 ? 64 ILE B CD1 1 ATOM 4865 N N . MET B 1 65 ? 17.000 13.088 32.034 1.00 16.14 ? 65 MET B N 1 ATOM 4866 C CA . MET B 1 65 ? 17.666 14.350 31.752 1.00 16.98 ? 65 MET B CA 1 ATOM 4867 C C . MET B 1 65 ? 19.154 14.066 31.662 1.00 16.51 ? 65 MET B C 1 ATOM 4868 O O . MET B 1 65 ? 19.642 13.080 32.227 1.00 15.05 ? 65 MET B O 1 ATOM 4869 C CB . MET B 1 65 ? 17.414 15.384 32.852 1.00 18.34 ? 65 MET B CB 1 ATOM 4870 C CG . MET B 1 65 ? 16.042 16.035 32.822 1.00 22.55 ? 65 MET B CG 1 ATOM 4871 S SD . MET B 1 65 ? 15.934 17.345 34.045 1.00 27.92 ? 65 MET B SD 1 ATOM 4872 C CE . MET B 1 65 ? 16.168 18.753 33.013 1.00 26.74 ? 65 MET B CE 1 ATOM 4873 N N . GLY B 1 66 ? 19.878 14.940 30.966 1.00 16.96 ? 66 GLY B N 1 ATOM 4874 C CA . GLY B 1 66 ? 21.316 14.781 30.844 1.00 17.26 ? 66 GLY B CA 1 ATOM 4875 C C . GLY B 1 66 ? 22.013 15.141 32.142 1.00 18.45 ? 66 GLY B C 1 ATOM 4876 O O . GLY B 1 66 ? 21.329 15.547 33.090 1.00 16.44 ? 66 GLY B O 1 ATOM 4877 N N . PRO B 1 67 ? 23.357 15.022 32.231 1.00 20.01 ? 67 PRO B N 1 ATOM 4878 C CA . PRO B 1 67 ? 24.019 15.376 33.490 1.00 20.68 ? 67 PRO B CA 1 ATOM 4879 C C . PRO B 1 67 ? 23.906 16.856 33.840 1.00 20.65 ? 67 PRO B C 1 ATOM 4880 O O . PRO B 1 67 ? 23.763 17.707 32.954 1.00 19.81 ? 67 PRO B O 1 ATOM 4881 C CB . PRO B 1 67 ? 25.472 14.951 33.254 1.00 21.99 ? 67 PRO B CB 1 ATOM 4882 C CG . PRO B 1 67 ? 25.629 15.029 31.788 1.00 20.71 ? 67 PRO B CG 1 ATOM 4883 C CD . PRO B 1 67 ? 24.332 14.476 31.270 1.00 19.80 ? 67 PRO B CD 1 ATOM 4884 N N . ASN B 1 68 ? 23.862 17.128 35.142 1.00 20.39 ? 68 ASN B N 1 ATOM 4885 C CA . ASN B 1 68 ? 23.782 18.488 35.656 1.00 21.27 ? 68 ASN B CA 1 ATOM 4886 C C . ASN B 1 68 ? 25.174 19.093 35.498 1.00 21.20 ? 68 ASN B C 1 ATOM 4887 O O . ASN B 1 68 ? 26.130 18.646 36.142 1.00 21.90 ? 68 ASN B O 1 ATOM 4888 C CB . ASN B 1 68 ? 23.373 18.490 37.138 1.00 22.26 ? 68 ASN B CB 1 ATOM 4889 C CG . ASN B 1 68 ? 22.006 17.860 37.383 1.00 25.36 ? 68 ASN B CG 1 ATOM 4890 O OD1 . ASN B 1 68 ? 21.079 18.002 36.581 1.00 24.76 ? 68 ASN B OD1 1 ATOM 4891 N ND2 . ASN B 1 68 ? 21.874 17.174 38.513 1.00 26.23 ? 68 ASN B ND2 1 ATOM 4892 N N . ILE B 1 69 ? 25.295 20.030 34.560 1.00 19.86 ? 69 ILE B N 1 ATOM 4893 C CA . ILE B 1 69 ? 26.562 20.707 34.301 1.00 19.04 ? 69 ILE B CA 1 ATOM 4894 C C . ILE B 1 69 ? 26.868 21.652 35.457 1.00 19.28 ? 69 ILE B C 1 ATOM 4895 O O . ILE B 1 69 ? 26.061 22.517 35.786 1.00 18.78 ? 69 ILE B O 1 ATOM 4896 C CB . ILE B 1 69 ? 26.557 21.451 32.925 1.00 17.33 ? 69 ILE B CB 1 ATOM 4897 C CG1 . ILE B 1 69 ? 26.577 20.425 31.784 1.00 18.46 ? 69 ILE B CG1 1 ATOM 4898 C CG2 . ILE B 1 69 ? 27.739 22.432 32.809 1.00 18.54 ? 69 ILE B CG2 1 ATOM 4899 C CD1 . ILE B 1 69 ? 26.537 21.023 30.388 1.00 16.36 ? 69 ILE B CD1 1 ATOM 4900 N N . VAL B 1 70 ? 27.978 21.378 36.140 1.00 18.93 ? 70 VAL B N 1 ATOM 4901 C CA . VAL B 1 70 ? 28.424 22.187 37.273 1.00 18.61 ? 70 VAL B CA 1 ATOM 4902 C C . VAL B 1 70 ? 29.848 22.681 37.006 1.00 18.54 ? 70 VAL B C 1 ATOM 4903 O O . VAL B 1 70 ? 30.747 21.890 36.704 1.00 18.25 ? 70 VAL B O 1 ATOM 4904 C CB . VAL B 1 70 ? 28.388 21.399 38.633 1.00 19.32 ? 70 VAL B CB 1 ATOM 4905 C CG1 . VAL B 1 70 ? 28.728 22.330 39.802 1.00 20.38 ? 70 VAL B CG1 1 ATOM 4906 C CG2 . VAL B 1 70 ? 27.013 20.773 38.880 1.00 19.42 ? 70 VAL B CG2 1 ATOM 4907 N N . ALA B 1 71 ? 30.021 23.999 37.102 1.00 17.37 ? 71 ALA B N 1 ATOM 4908 C CA . ALA B 1 71 ? 31.306 24.665 36.912 1.00 17.79 ? 71 ALA B CA 1 ATOM 4909 C C . ALA B 1 71 ? 31.296 25.986 37.678 1.00 18.28 ? 71 ALA B C 1 ATOM 4910 O O . ALA B 1 71 ? 30.257 26.401 38.196 1.00 17.95 ? 71 ALA B O 1 ATOM 4911 C CB . ALA B 1 71 ? 31.572 24.917 35.421 1.00 16.06 ? 71 ALA B CB 1 ATOM 4912 N N . ASN B 1 72 ? 32.465 26.612 37.794 1.00 17.47 ? 72 ASN B N 1 ATOM 4913 C CA . ASN B 1 72 ? 32.594 27.892 38.485 1.00 18.14 ? 72 ASN B CA 1 ATOM 4914 C C . ASN B 1 72 ? 32.660 29.013 37.466 1.00 17.14 ? 72 ASN B C 1 ATOM 4915 O O . ASN B 1 72 ? 32.971 28.781 36.297 1.00 15.83 ? 72 ASN B O 1 ATOM 4916 C CB . ASN B 1 72 ? 33.862 27.925 39.346 1.00 21.18 ? 72 ASN B CB 1 ATOM 4917 C CG . ASN B 1 72 ? 33.778 27.010 40.552 1.00 21.57 ? 72 ASN B CG 1 ATOM 4918 O OD1 . ASN B 1 72 ? 34.683 26.213 40.804 1.00 23.76 ? 72 ASN B OD1 1 ATOM 4919 N ND2 . ASN B 1 72 ? 32.697 27.127 41.309 1.00 22.25 ? 72 ASN B ND2 1 ATOM 4920 N N . TRP B 1 73 ? 32.370 30.228 37.925 1.00 16.13 ? 73 TRP B N 1 ATOM 4921 C CA . TRP B 1 73 ? 32.412 31.434 37.101 1.00 17.06 ? 73 TRP B CA 1 ATOM 4922 C C . TRP B 1 73 ? 33.847 31.619 36.595 1.00 17.90 ? 73 TRP B C 1 ATOM 4923 O O . TRP B 1 73 ? 34.792 31.675 37.381 1.00 18.09 ? 73 TRP B O 1 ATOM 4924 C CB . TRP B 1 73 ? 31.953 32.625 37.951 1.00 15.67 ? 73 TRP B CB 1 ATOM 4925 C CG . TRP B 1 73 ? 31.917 33.989 37.305 1.00 14.87 ? 73 TRP B CG 1 ATOM 4926 C CD1 . TRP B 1 73 ? 31.780 34.293 35.969 1.00 14.87 ? 73 TRP B CD1 1 ATOM 4927 C CD2 . TRP B 1 73 ? 31.988 35.239 37.992 1.00 14.93 ? 73 TRP B CD2 1 ATOM 4928 N NE1 . TRP B 1 73 ? 31.765 35.653 35.792 1.00 15.76 ? 73 TRP B NE1 1 ATOM 4929 C CE2 . TRP B 1 73 ? 31.889 36.264 37.012 1.00 15.00 ? 73 TRP B CE2 1 ATOM 4930 C CE3 . TRP B 1 73 ? 32.117 35.601 39.349 1.00 15.87 ? 73 TRP B CE3 1 ATOM 4931 C CZ2 . TRP B 1 73 ? 31.919 37.637 37.348 1.00 14.96 ? 73 TRP B CZ2 1 ATOM 4932 C CZ3 . TRP B 1 73 ? 32.141 36.971 39.690 1.00 13.55 ? 73 TRP B CZ3 1 ATOM 4933 C CH2 . TRP B 1 73 ? 32.044 37.970 38.686 1.00 15.57 ? 73 TRP B CH2 1 ATOM 4934 N N . GLY B 1 74 ? 33.986 31.613 35.273 1.00 17.51 ? 74 GLY B N 1 ATOM 4935 C CA . GLY B 1 74 ? 35.291 31.761 34.665 1.00 16.95 ? 74 GLY B CA 1 ATOM 4936 C C . GLY B 1 74 ? 35.833 30.488 34.054 1.00 17.27 ? 74 GLY B C 1 ATOM 4937 O O . GLY B 1 74 ? 36.795 30.543 33.283 1.00 17.59 ? 74 GLY B O 1 ATOM 4938 N N . ASP B 1 75 ? 35.238 29.347 34.413 1.00 16.24 ? 75 ASP B N 1 ATOM 4939 C CA . ASP B 1 75 ? 35.641 28.045 33.871 1.00 16.37 ? 75 ASP B CA 1 ATOM 4940 C C . ASP B 1 75 ? 35.188 27.916 32.424 1.00 17.05 ? 75 ASP B C 1 ATOM 4941 O O . ASP B 1 75 ? 34.395 28.722 31.924 1.00 17.01 ? 75 ASP B O 1 ATOM 4942 C CB . ASP B 1 75 ? 34.987 26.877 34.629 1.00 15.83 ? 75 ASP B CB 1 ATOM 4943 C CG . ASP B 1 75 ? 35.521 26.683 36.030 1.00 14.53 ? 75 ASP B CG 1 ATOM 4944 O OD1 . ASP B 1 75 ? 36.504 27.338 36.427 1.00 16.03 ? 75 ASP B OD1 1 ATOM 4945 O OD2 . ASP B 1 75 ? 34.933 25.848 36.746 1.00 13.32 ? 75 ASP B OD2 1 ATOM 4946 N N . THR B 1 76 ? 35.701 26.884 31.770 1.00 17.65 ? 76 THR B N 1 ATOM 4947 C CA . THR B 1 76 ? 35.329 26.572 30.405 1.00 17.13 ? 76 THR B CA 1 ATOM 4948 C C . THR B 1 76 ? 34.562 25.262 30.503 1.00 16.51 ? 76 THR B C 1 ATOM 4949 O O . THR B 1 76 ? 34.972 24.347 31.218 1.00 15.92 ? 76 THR B O 1 ATOM 4950 C CB . THR B 1 76 ? 36.571 26.400 29.492 1.00 19.07 ? 76 THR B CB 1 ATOM 4951 O OG1 . THR B 1 76 ? 37.298 27.633 29.436 1.00 19.19 ? 76 THR B OG1 1 ATOM 4952 C CG2 . THR B 1 76 ? 36.151 26.036 28.081 1.00 19.81 ? 76 THR B CG2 1 ATOM 4953 N N . VAL B 1 77 ? 33.391 25.217 29.875 1.00 15.65 ? 77 VAL B N 1 ATOM 4954 C CA . VAL B 1 77 ? 32.600 23.997 29.866 1.00 16.07 ? 77 VAL B CA 1 ATOM 4955 C C . VAL B 1 77 ? 32.769 23.381 28.480 1.00 16.55 ? 77 VAL B C 1 ATOM 4956 O O . VAL B 1 77 ? 32.573 24.044 27.460 1.00 16.39 ? 77 VAL B O 1 ATOM 4957 C CB . VAL B 1 77 ? 31.121 24.258 30.200 1.00 17.34 ? 77 VAL B CB 1 ATOM 4958 C CG1 . VAL B 1 77 ? 30.295 22.974 30.083 1.00 16.73 ? 77 VAL B CG1 1 ATOM 4959 C CG2 . VAL B 1 77 ? 30.996 24.830 31.610 1.00 18.24 ? 77 VAL B CG2 1 ATOM 4960 N N . GLU B 1 78 ? 33.175 22.118 28.474 1.00 16.92 ? 78 GLU B N 1 ATOM 4961 C CA . GLU B 1 78 ? 33.410 21.375 27.251 1.00 17.14 ? 78 GLU B CA 1 ATOM 4962 C C . GLU B 1 78 ? 32.510 20.158 27.220 1.00 15.52 ? 78 GLU B C 1 ATOM 4963 O O . GLU B 1 78 ? 32.461 19.395 28.176 1.00 15.26 ? 78 GLU B O 1 ATOM 4964 C CB . GLU B 1 78 ? 34.872 20.961 27.183 1.00 17.13 ? 78 GLU B CB 1 ATOM 4965 C CG . GLU B 1 78 ? 35.298 20.425 25.847 1.00 20.31 ? 78 GLU B CG 1 ATOM 4966 C CD . GLU B 1 78 ? 36.787 20.516 25.610 1.00 21.24 ? 78 GLU B CD 1 ATOM 4967 O OE1 . GLU B 1 78 ? 37.520 21.041 26.474 1.00 21.48 ? 78 GLU B OE1 1 ATOM 4968 O OE2 . GLU B 1 78 ? 37.223 20.074 24.530 1.00 24.91 ? 78 GLU B OE2 1 ATOM 4969 N N . VAL B 1 79 ? 31.755 20.011 26.135 1.00 15.89 ? 79 VAL B N 1 ATOM 4970 C CA . VAL B 1 79 ? 30.836 18.893 25.999 1.00 14.98 ? 79 VAL B CA 1 ATOM 4971 C C . VAL B 1 79 ? 30.915 18.202 24.638 1.00 15.59 ? 79 VAL B C 1 ATOM 4972 O O . VAL B 1 79 ? 30.626 18.812 23.607 1.00 15.14 ? 79 VAL B O 1 ATOM 4973 C CB . VAL B 1 79 ? 29.354 19.326 26.234 1.00 16.46 ? 79 VAL B CB 1 ATOM 4974 C CG1 . VAL B 1 79 ? 28.453 18.127 26.145 1.00 16.03 ? 79 VAL B CG1 1 ATOM 4975 C CG2 . VAL B 1 79 ? 29.151 19.995 27.593 1.00 16.71 ? 79 VAL B CG2 1 ATOM 4976 N N . THR B 1 80 ? 31.248 16.913 24.657 1.00 16.05 ? 80 THR B N 1 ATOM 4977 C CA . THR B 1 80 ? 31.301 16.110 23.437 1.00 13.93 ? 80 THR B CA 1 ATOM 4978 C C . THR B 1 80 ? 29.935 15.454 23.282 1.00 12.78 ? 80 THR B C 1 ATOM 4979 O O . THR B 1 80 ? 29.515 14.662 24.126 1.00 12.86 ? 80 THR B O 1 ATOM 4980 C CB . THR B 1 80 ? 32.413 15.031 23.483 1.00 14.43 ? 80 THR B CB 1 ATOM 4981 O OG1 . THR B 1 80 ? 33.686 15.670 23.614 1.00 15.99 ? 80 THR B OG1 1 ATOM 4982 C CG2 . THR B 1 80 ? 32.410 14.176 22.198 1.00 12.74 ? 80 THR B CG2 1 ATOM 4983 N N . VAL B 1 81 ? 29.232 15.821 22.217 1.00 12.46 ? 81 VAL B N 1 ATOM 4984 C CA . VAL B 1 81 ? 27.913 15.263 21.951 1.00 12.59 ? 81 VAL B CA 1 ATOM 4985 C C . VAL B 1 81 ? 28.014 14.209 20.864 1.00 12.64 ? 81 VAL B C 1 ATOM 4986 O O . VAL B 1 81 ? 28.399 14.509 19.737 1.00 13.09 ? 81 VAL B O 1 ATOM 4987 C CB . VAL B 1 81 ? 26.887 16.365 21.560 1.00 12.43 ? 81 VAL B CB 1 ATOM 4988 C CG1 . VAL B 1 81 ? 25.505 15.763 21.306 1.00 11.32 ? 81 VAL B CG1 1 ATOM 4989 C CG2 . VAL B 1 81 ? 26.789 17.398 22.672 1.00 13.33 ? 81 VAL B CG2 1 ATOM 4990 N N . ILE B 1 82 ? 27.686 12.973 21.231 1.00 12.62 ? 82 ILE B N 1 ATOM 4991 C CA . ILE B 1 82 ? 27.710 11.842 20.308 1.00 13.76 ? 82 ILE B CA 1 ATOM 4992 C C . ILE B 1 82 ? 26.255 11.467 20.046 1.00 14.14 ? 82 ILE B C 1 ATOM 4993 O O . ILE B 1 82 ? 25.531 11.036 20.947 1.00 14.39 ? 82 ILE B O 1 ATOM 4994 C CB . ILE B 1 82 ? 28.504 10.625 20.878 1.00 14.83 ? 82 ILE B CB 1 ATOM 4995 C CG1 . ILE B 1 82 ? 29.930 11.056 21.259 1.00 14.93 ? 82 ILE B CG1 1 ATOM 4996 C CG2 . ILE B 1 82 ? 28.569 9.489 19.831 1.00 15.66 ? 82 ILE B CG2 1 ATOM 4997 C CD1 . ILE B 1 82 ? 30.695 10.051 22.088 1.00 17.11 ? 82 ILE B CD1 1 ATOM 4998 N N . ASN B 1 83 ? 25.844 11.657 18.798 1.00 13.89 ? 83 ASN B N 1 ATOM 4999 C CA . ASN B 1 83 ? 24.486 11.379 18.367 1.00 14.06 ? 83 ASN B CA 1 ATOM 5000 C C . ASN B 1 83 ? 24.317 9.933 17.897 1.00 14.45 ? 83 ASN B C 1 ATOM 5001 O O . ASN B 1 83 ? 24.655 9.596 16.757 1.00 13.15 ? 83 ASN B O 1 ATOM 5002 C CB . ASN B 1 83 ? 24.092 12.378 17.266 1.00 14.01 ? 83 ASN B CB 1 ATOM 5003 C CG . ASN B 1 83 ? 22.622 12.283 16.859 1.00 16.36 ? 83 ASN B CG 1 ATOM 5004 O OD1 . ASN B 1 83 ? 21.887 11.429 17.338 1.00 16.19 ? 83 ASN B OD1 1 ATOM 5005 N ND2 . ASN B 1 83 ? 22.208 13.140 15.934 1.00 14.67 ? 83 ASN B ND2 1 ATOM 5006 N N . ASN B 1 84 ? 23.756 9.104 18.776 1.00 14.13 ? 84 ASN B N 1 ATOM 5007 C CA . ASN B 1 84 ? 23.497 7.702 18.462 1.00 15.48 ? 84 ASN B CA 1 ATOM 5008 C C . ASN B 1 84 ? 22.008 7.431 18.263 1.00 16.00 ? 84 ASN B C 1 ATOM 5009 O O . ASN B 1 84 ? 21.524 6.321 18.504 1.00 15.78 ? 84 ASN B O 1 ATOM 5010 C CB . ASN B 1 84 ? 24.100 6.776 19.522 1.00 17.18 ? 84 ASN B CB 1 ATOM 5011 C CG . ASN B 1 84 ? 25.600 6.653 19.396 1.00 17.30 ? 84 ASN B CG 1 ATOM 5012 O OD1 . ASN B 1 84 ? 26.118 6.362 18.319 1.00 21.26 ? 84 ASN B OD1 1 ATOM 5013 N ND2 . ASN B 1 84 ? 26.308 6.884 20.491 1.00 16.49 ? 84 ASN B ND2 1 ATOM 5014 N N . LEU B 1 85 ? 21.278 8.463 17.827 1.00 15.14 ? 85 LEU B N 1 ATOM 5015 C CA . LEU B 1 85 ? 19.851 8.331 17.525 1.00 15.21 ? 85 LEU B CA 1 ATOM 5016 C C . LEU B 1 85 ? 19.765 7.594 16.186 1.00 14.45 ? 85 LEU B C 1 ATOM 5017 O O . LEU B 1 85 ? 20.770 7.469 15.483 1.00 14.66 ? 85 LEU B O 1 ATOM 5018 C CB . LEU B 1 85 ? 19.163 9.704 17.436 1.00 15.29 ? 85 LEU B CB 1 ATOM 5019 C CG . LEU B 1 85 ? 19.163 10.569 18.706 1.00 17.47 ? 85 LEU B CG 1 ATOM 5020 C CD1 . LEU B 1 85 ? 18.591 11.940 18.426 1.00 18.34 ? 85 LEU B CD1 1 ATOM 5021 C CD2 . LEU B 1 85 ? 18.412 9.906 19.816 1.00 15.74 ? 85 LEU B CD2 1 ATOM 5022 N N . VAL B 1 86 ? 18.582 7.104 15.836 1.00 15.52 ? 86 VAL B N 1 ATOM 5023 C CA . VAL B 1 86 ? 18.418 6.349 14.596 1.00 15.05 ? 86 VAL B CA 1 ATOM 5024 C C . VAL B 1 86 ? 18.379 7.212 13.334 1.00 14.78 ? 86 VAL B C 1 ATOM 5025 O O . VAL B 1 86 ? 19.179 7.001 12.422 1.00 13.32 ? 86 VAL B O 1 ATOM 5026 C CB . VAL B 1 86 ? 17.188 5.384 14.669 1.00 14.82 ? 86 VAL B CB 1 ATOM 5027 C CG1 . VAL B 1 86 ? 17.153 4.429 13.461 1.00 16.15 ? 86 VAL B CG1 1 ATOM 5028 C CG2 . VAL B 1 86 ? 17.240 4.566 15.953 1.00 16.19 ? 86 VAL B CG2 1 ATOM 5029 N N . THR B 1 87 ? 17.503 8.219 13.314 1.00 15.21 ? 87 THR B N 1 ATOM 5030 C CA . THR B 1 87 ? 17.347 9.079 12.136 1.00 13.95 ? 87 THR B CA 1 ATOM 5031 C C . THR B 1 87 ? 17.664 10.552 12.342 1.00 15.29 ? 87 THR B C 1 ATOM 5032 O O . THR B 1 87 ? 18.224 11.215 11.462 1.00 14.13 ? 87 THR B O 1 ATOM 5033 C CB . THR B 1 87 ? 15.909 8.988 11.579 1.00 14.18 ? 87 THR B CB 1 ATOM 5034 O OG1 . THR B 1 87 ? 14.977 9.409 12.585 1.00 16.83 ? 87 THR B OG1 1 ATOM 5035 C CG2 . THR B 1 87 ? 15.583 7.563 11.148 1.00 13.84 ? 87 THR B CG2 1 ATOM 5036 N N . ASN B 1 88 ? 17.276 11.055 13.508 1.00 14.05 ? 88 ASN B N 1 ATOM 5037 C CA . ASN B 1 88 ? 17.454 12.445 13.877 1.00 13.90 ? 88 ASN B CA 1 ATOM 5038 C C . ASN B 1 88 ? 18.865 12.967 14.003 1.00 12.39 ? 88 ASN B C 1 ATOM 5039 O O . ASN B 1 88 ? 19.751 12.301 14.536 1.00 12.99 ? 88 ASN B O 1 ATOM 5040 C CB . ASN B 1 88 ? 16.798 12.713 15.233 1.00 15.23 ? 88 ASN B CB 1 ATOM 5041 C CG . ASN B 1 88 ? 15.313 12.906 15.153 1.00 15.12 ? 88 ASN B CG 1 ATOM 5042 O OD1 . ASN B 1 88 ? 14.744 13.585 16.010 1.00 14.84 ? 88 ASN B OD1 1 ATOM 5043 N ND2 . ASN B 1 88 ? 14.674 12.319 14.147 1.00 14.90 ? 88 ASN B ND2 1 ATOM 5044 N N . GLY B 1 89 ? 19.039 14.203 13.549 1.00 10.57 ? 89 GLY B N 1 ATOM 5045 C CA . GLY B 1 89 ? 20.296 14.888 13.740 1.00 10.95 ? 89 GLY B CA 1 ATOM 5046 C C . GLY B 1 89 ? 20.089 15.564 15.090 1.00 11.52 ? 89 GLY B C 1 ATOM 5047 O O . GLY B 1 89 ? 19.007 15.423 15.682 1.00 10.17 ? 89 GLY B O 1 ATOM 5048 N N . THR B 1 90 ? 21.098 16.263 15.603 1.00 12.63 ? 90 THR B N 1 ATOM 5049 C CA . THR B 1 90 ? 20.951 16.950 16.883 1.00 13.28 ? 90 THR B CA 1 ATOM 5050 C C . THR B 1 90 ? 21.874 18.155 16.985 1.00 13.82 ? 90 THR B C 1 ATOM 5051 O O . THR B 1 90 ? 22.825 18.285 16.223 1.00 13.06 ? 90 THR B O 1 ATOM 5052 C CB . THR B 1 90 ? 21.154 15.978 18.109 1.00 11.92 ? 90 THR B CB 1 ATOM 5053 O OG1 . THR B 1 90 ? 20.541 16.539 19.278 1.00 11.87 ? 90 THR B OG1 1 ATOM 5054 C CG2 . THR B 1 90 ? 22.629 15.711 18.404 1.00 9.27 ? 90 THR B CG2 1 ATOM 5055 N N . SER B 1 91 ? 21.546 19.048 17.910 1.00 15.64 ? 91 SER B N 1 ATOM 5056 C CA . SER B 1 91 ? 22.330 20.244 18.182 1.00 17.45 ? 91 SER B CA 1 ATOM 5057 C C . SER B 1 91 ? 21.913 20.687 19.566 1.00 18.66 ? 91 SER B C 1 ATOM 5058 O O . SER B 1 91 ? 20.727 20.904 19.813 1.00 20.84 ? 91 SER B O 1 ATOM 5059 C CB . SER B 1 91 ? 22.054 21.353 17.162 1.00 19.97 ? 91 SER B CB 1 ATOM 5060 O OG . SER B 1 91 ? 20.712 21.796 17.226 1.00 23.15 ? 91 SER B OG 1 ATOM 5061 N N . ILE B 1 92 ? 22.877 20.786 20.473 1.00 16.58 ? 92 ILE B N 1 ATOM 5062 C CA . ILE B 1 92 ? 22.584 21.186 21.843 1.00 15.28 ? 92 ILE B CA 1 ATOM 5063 C C . ILE B 1 92 ? 22.818 22.673 22.057 1.00 14.75 ? 92 ILE B C 1 ATOM 5064 O O . ILE B 1 92 ? 23.934 23.176 21.886 1.00 14.04 ? 92 ILE B O 1 ATOM 5065 C CB . ILE B 1 92 ? 23.399 20.360 22.883 1.00 15.38 ? 92 ILE B CB 1 ATOM 5066 C CG1 . ILE B 1 92 ? 23.303 18.856 22.587 1.00 16.31 ? 92 ILE B CG1 1 ATOM 5067 C CG2 . ILE B 1 92 ? 22.892 20.639 24.307 1.00 15.39 ? 92 ILE B CG2 1 ATOM 5068 C CD1 . ILE B 1 92 ? 21.894 18.268 22.580 1.00 17.19 ? 92 ILE B CD1 1 ATOM 5069 N N . HIS B 1 93 ? 21.734 23.363 22.403 1.00 13.31 ? 93 HIS B N 1 ATOM 5070 C CA . HIS B 1 93 ? 21.762 24.791 22.670 1.00 13.35 ? 93 HIS B CA 1 ATOM 5071 C C . HIS B 1 93 ? 21.883 24.997 24.170 1.00 12.79 ? 93 HIS B C 1 ATOM 5072 O O . HIS B 1 93 ? 21.187 24.358 24.945 1.00 12.32 ? 93 HIS B O 1 ATOM 5073 C CB . HIS B 1 93 ? 20.502 25.475 22.122 1.00 13.58 ? 93 HIS B CB 1 ATOM 5074 C CG . HIS B 1 93 ? 20.360 26.910 22.538 1.00 14.01 ? 93 HIS B CG 1 ATOM 5075 N ND1 . HIS B 1 93 ? 21.377 27.831 22.404 1.00 13.97 ? 93 HIS B ND1 1 ATOM 5076 C CD2 . HIS B 1 93 ? 19.340 27.563 23.143 1.00 14.59 ? 93 HIS B CD2 1 ATOM 5077 C CE1 . HIS B 1 93 ? 20.992 28.988 22.915 1.00 13.26 ? 93 HIS B CE1 1 ATOM 5078 N NE2 . HIS B 1 93 ? 19.760 28.853 23.368 1.00 15.37 ? 93 HIS B NE2 1 ATOM 5079 N N . TRP B 1 94 ? 22.755 25.927 24.542 1.00 12.99 ? 94 TRP B N 1 ATOM 5080 C CA . TRP B 1 94 ? 23.031 26.270 25.930 1.00 14.57 ? 94 TRP B CA 1 ATOM 5081 C C . TRP B 1 94 ? 22.262 27.555 26.244 1.00 14.62 ? 94 TRP B C 1 ATOM 5082 O O . TRP B 1 94 ? 22.768 28.672 26.101 1.00 15.98 ? 94 TRP B O 1 ATOM 5083 C CB . TRP B 1 94 ? 24.556 26.415 26.123 1.00 14.28 ? 94 TRP B CB 1 ATOM 5084 C CG . TRP B 1 94 ? 25.336 25.371 25.367 1.00 15.79 ? 94 TRP B CG 1 ATOM 5085 C CD1 . TRP B 1 94 ? 25.840 25.488 24.096 1.00 16.59 ? 94 TRP B CD1 1 ATOM 5086 C CD2 . TRP B 1 94 ? 25.535 24.005 25.747 1.00 14.93 ? 94 TRP B CD2 1 ATOM 5087 N NE1 . TRP B 1 94 ? 26.310 24.275 23.653 1.00 16.13 ? 94 TRP B NE1 1 ATOM 5088 C CE2 . TRP B 1 94 ? 26.138 23.345 24.642 1.00 15.94 ? 94 TRP B CE2 1 ATOM 5089 C CE3 . TRP B 1 94 ? 25.252 23.262 26.911 1.00 16.13 ? 94 TRP B CE3 1 ATOM 5090 C CZ2 . TRP B 1 94 ? 26.461 21.970 24.667 1.00 14.97 ? 94 TRP B CZ2 1 ATOM 5091 C CZ3 . TRP B 1 94 ? 25.571 21.888 26.935 1.00 13.50 ? 94 TRP B CZ3 1 ATOM 5092 C CH2 . TRP B 1 94 ? 26.168 21.263 25.814 1.00 14.72 ? 94 TRP B CH2 1 ATOM 5093 N N . HIS B 1 95 ? 20.993 27.360 26.596 1.00 15.98 ? 95 HIS B N 1 ATOM 5094 C CA . HIS B 1 95 ? 20.042 28.426 26.915 1.00 15.43 ? 95 HIS B CA 1 ATOM 5095 C C . HIS B 1 95 ? 20.496 29.242 28.125 1.00 17.37 ? 95 HIS B C 1 ATOM 5096 O O . HIS B 1 95 ? 20.614 28.713 29.228 1.00 20.20 ? 95 HIS B O 1 ATOM 5097 C CB . HIS B 1 95 ? 18.662 27.780 27.147 1.00 14.83 ? 95 HIS B CB 1 ATOM 5098 C CG . HIS B 1 95 ? 17.527 28.746 27.322 1.00 15.47 ? 95 HIS B CG 1 ATOM 5099 N ND1 . HIS B 1 95 ? 16.334 28.601 26.647 1.00 14.40 ? 95 HIS B ND1 1 ATOM 5100 C CD2 . HIS B 1 95 ? 17.359 29.799 28.162 1.00 14.66 ? 95 HIS B CD2 1 ATOM 5101 C CE1 . HIS B 1 95 ? 15.484 29.520 27.071 1.00 15.80 ? 95 HIS B CE1 1 ATOM 5102 N NE2 . HIS B 1 95 ? 16.080 30.260 27.987 1.00 15.57 ? 95 HIS B NE2 1 ATOM 5103 N N . GLY B 1 96 ? 20.666 30.544 27.902 1.00 16.77 ? 96 GLY B N 1 ATOM 5104 C CA . GLY B 1 96 ? 21.092 31.447 28.955 1.00 18.00 ? 96 GLY B CA 1 ATOM 5105 C C . GLY B 1 96 ? 22.545 31.838 28.818 1.00 18.53 ? 96 GLY B C 1 ATOM 5106 O O . GLY B 1 96 ? 22.957 32.888 29.317 1.00 18.17 ? 96 GLY B O 1 ATOM 5107 N N . ILE B 1 97 ? 23.321 30.986 28.146 1.00 17.62 ? 97 ILE B N 1 ATOM 5108 C CA . ILE B 1 97 ? 24.745 31.230 27.924 1.00 17.83 ? 97 ILE B CA 1 ATOM 5109 C C . ILE B 1 97 ? 24.894 32.116 26.691 1.00 17.99 ? 97 ILE B C 1 ATOM 5110 O O . ILE B 1 97 ? 24.499 31.735 25.584 1.00 17.50 ? 97 ILE B O 1 ATOM 5111 C CB . ILE B 1 97 ? 25.541 29.907 27.758 1.00 18.27 ? 97 ILE B CB 1 ATOM 5112 C CG1 . ILE B 1 97 ? 25.210 28.920 28.897 1.00 18.06 ? 97 ILE B CG1 1 ATOM 5113 C CG2 . ILE B 1 97 ? 27.044 30.192 27.670 1.00 18.53 ? 97 ILE B CG2 1 ATOM 5114 C CD1 . ILE B 1 97 ? 25.479 29.405 30.316 1.00 18.03 ? 97 ILE B CD1 1 ATOM 5115 N N . HIS B 1 98 ? 25.492 33.287 26.909 1.00 17.50 ? 98 HIS B N 1 ATOM 5116 C CA . HIS B 1 98 ? 25.682 34.301 25.875 1.00 18.78 ? 98 HIS B CA 1 ATOM 5117 C C . HIS B 1 98 ? 26.537 33.982 24.678 1.00 17.02 ? 98 HIS B C 1 ATOM 5118 O O . HIS B 1 98 ? 26.317 34.537 23.599 1.00 16.42 ? 98 HIS B O 1 ATOM 5119 C CB . HIS B 1 98 ? 26.140 35.618 26.497 1.00 21.71 ? 98 HIS B CB 1 ATOM 5120 C CG . HIS B 1 98 ? 25.128 36.214 27.415 1.00 26.15 ? 98 HIS B CG 1 ATOM 5121 N ND1 . HIS B 1 98 ? 23.911 35.612 27.650 1.00 27.47 ? 98 HIS B ND1 1 ATOM 5122 C CD2 . HIS B 1 98 ? 25.150 37.335 28.171 1.00 27.38 ? 98 HIS B CD2 1 ATOM 5123 C CE1 . HIS B 1 98 ? 23.230 36.334 28.515 1.00 27.02 ? 98 HIS B CE1 1 ATOM 5124 N NE2 . HIS B 1 98 ? 23.957 37.385 28.848 1.00 26.82 ? 98 HIS B NE2 1 ATOM 5125 N N . GLN B 1 99 ? 27.490 33.069 24.859 1.00 16.63 ? 99 GLN B N 1 ATOM 5126 C CA . GLN B 1 99 ? 28.412 32.658 23.799 1.00 16.49 ? 99 GLN B CA 1 ATOM 5127 C C . GLN B 1 99 ? 29.152 33.873 23.215 1.00 16.46 ? 99 GLN B C 1 ATOM 5128 O O . GLN B 1 99 ? 29.147 34.102 21.995 1.00 15.92 ? 99 GLN B O 1 ATOM 5129 C CB . GLN B 1 99 ? 27.677 31.866 22.691 1.00 16.28 ? 99 GLN B CB 1 ATOM 5130 C CG . GLN B 1 99 ? 26.900 30.620 23.151 1.00 15.77 ? 99 GLN B CG 1 ATOM 5131 C CD . GLN B 1 99 ? 27.777 29.437 23.537 1.00 17.80 ? 99 GLN B CD 1 ATOM 5132 O OE1 . GLN B 1 99 ? 27.302 28.493 24.167 1.00 18.13 ? 99 GLN B OE1 1 ATOM 5133 N NE2 . GLN B 1 99 ? 29.053 29.475 23.156 1.00 13.00 ? 99 GLN B NE2 1 ATOM 5134 N N . LYS B 1 100 ? 29.726 34.676 24.116 1.00 16.98 ? 100 LYS B N 1 ATOM 5135 C CA . LYS B 1 100 ? 30.472 35.890 23.764 1.00 18.29 ? 100 LYS B CA 1 ATOM 5136 C C . LYS B 1 100 ? 31.631 35.554 22.832 1.00 16.36 ? 100 LYS B C 1 ATOM 5137 O O . LYS B 1 100 ? 32.612 34.919 23.234 1.00 14.59 ? 100 LYS B O 1 ATOM 5138 C CB . LYS B 1 100 ? 30.964 36.614 25.027 1.00 21.22 ? 100 LYS B CB 1 ATOM 5139 C CG . LYS B 1 100 ? 31.699 37.951 24.794 1.00 26.59 ? 100 LYS B CG 1 ATOM 5140 C CD . LYS B 1 100 ? 30.765 39.100 24.419 1.00 30.67 ? 100 LYS B CD 1 ATOM 5141 C CE . LYS B 1 100 ? 30.004 39.622 25.629 1.00 35.16 ? 100 LYS B CE 1 ATOM 5142 N NZ . LYS B 1 100 ? 29.087 40.727 25.264 1.00 38.09 ? 100 LYS B NZ 1 ATOM 5143 N N . ASP B 1 101 ? 31.438 35.933 21.566 1.00 16.82 ? 101 ASP B N 1 ATOM 5144 C CA . ASP B 1 101 ? 32.375 35.714 20.457 1.00 18.53 ? 101 ASP B CA 1 ATOM 5145 C C . ASP B 1 101 ? 32.616 34.233 20.125 1.00 17.23 ? 101 ASP B C 1 ATOM 5146 O O . ASP B 1 101 ? 33.633 33.868 19.528 1.00 17.42 ? 101 ASP B O 1 ATOM 5147 C CB . ASP B 1 101 ? 33.685 36.504 20.655 1.00 21.63 ? 101 ASP B CB 1 ATOM 5148 C CG . ASP B 1 101 ? 33.445 38.003 20.751 1.00 23.58 ? 101 ASP B CG 1 ATOM 5149 O OD1 . ASP B 1 101 ? 32.951 38.593 19.769 1.00 22.61 ? 101 ASP B OD1 1 ATOM 5150 O OD2 . ASP B 1 101 ? 33.716 38.580 21.823 1.00 26.95 ? 101 ASP B OD2 1 ATOM 5151 N N . THR B 1 102 ? 31.677 33.386 20.558 1.00 16.05 ? 102 THR B N 1 ATOM 5152 C CA . THR B 1 102 ? 31.712 31.942 20.298 1.00 14.81 ? 102 THR B CA 1 ATOM 5153 C C . THR B 1 102 ? 30.350 31.506 19.734 1.00 14.57 ? 102 THR B C 1 ATOM 5154 O O . THR B 1 102 ? 29.784 30.490 20.151 1.00 15.33 ? 102 THR B O 1 ATOM 5155 C CB . THR B 1 102 ? 32.072 31.086 21.568 1.00 13.24 ? 102 THR B CB 1 ATOM 5156 O OG1 . THR B 1 102 ? 31.115 31.321 22.606 1.00 13.58 ? 102 THR B OG1 1 ATOM 5157 C CG2 . THR B 1 102 ? 33.468 31.399 22.085 1.00 12.02 ? 102 THR B CG2 1 ATOM 5158 N N . ASN B 1 103 ? 29.855 32.274 18.758 1.00 15.24 ? 103 ASN B N 1 ATOM 5159 C CA . ASN B 1 103 ? 28.570 32.033 18.077 1.00 15.14 ? 103 ASN B CA 1 ATOM 5160 C C . ASN B 1 103 ? 28.395 30.613 17.523 1.00 13.96 ? 103 ASN B C 1 ATOM 5161 O O . ASN B 1 103 ? 27.326 30.023 17.668 1.00 13.19 ? 103 ASN B O 1 ATOM 5162 C CB . ASN B 1 103 ? 28.377 33.066 16.951 1.00 14.80 ? 103 ASN B CB 1 ATOM 5163 C CG . ASN B 1 103 ? 26.999 32.985 16.274 1.00 15.77 ? 103 ASN B CG 1 ATOM 5164 O OD1 . ASN B 1 103 ? 26.903 32.978 15.046 1.00 16.14 ? 103 ASN B OD1 1 ATOM 5165 N ND2 . ASN B 1 103 ? 25.939 32.979 17.069 1.00 14.64 ? 103 ASN B ND2 1 ATOM 5166 N N . LEU B 1 104 ? 29.474 30.044 16.984 1.00 12.84 ? 104 LEU B N 1 ATOM 5167 C CA . LEU B 1 104 ? 29.452 28.698 16.393 1.00 13.26 ? 104 LEU B CA 1 ATOM 5168 C C . LEU B 1 104 ? 29.224 27.545 17.376 1.00 11.75 ? 104 LEU B C 1 ATOM 5169 O O . LEU B 1 104 ? 29.068 26.392 16.964 1.00 11.64 ? 104 LEU B O 1 ATOM 5170 C CB . LEU B 1 104 ? 30.728 28.439 15.578 1.00 13.50 ? 104 LEU B CB 1 ATOM 5171 C CG . LEU B 1 104 ? 31.239 29.351 14.450 1.00 18.61 ? 104 LEU B CG 1 ATOM 5172 C CD1 . LEU B 1 104 ? 31.590 28.492 13.250 1.00 16.45 ? 104 LEU B CD1 1 ATOM 5173 C CD2 . LEU B 1 104 ? 30.271 30.449 14.058 1.00 15.46 ? 104 LEU B CD2 1 ATOM 5174 N N . HIS B 1 105 ? 29.199 27.872 18.668 1.00 11.25 ? 105 HIS B N 1 ATOM 5175 C CA . HIS B 1 105 ? 28.967 26.896 19.732 1.00 12.20 ? 105 HIS B CA 1 ATOM 5176 C C . HIS B 1 105 ? 27.570 27.051 20.358 1.00 12.64 ? 105 HIS B C 1 ATOM 5177 O O . HIS B 1 105 ? 27.246 26.380 21.345 1.00 9.85 ? 105 HIS B O 1 ATOM 5178 C CB . HIS B 1 105 ? 30.053 27.027 20.812 1.00 13.89 ? 105 HIS B CB 1 ATOM 5179 C CG . HIS B 1 105 ? 31.422 26.654 20.337 1.00 14.65 ? 105 HIS B CG 1 ATOM 5180 N ND1 . HIS B 1 105 ? 31.972 25.411 20.561 1.00 16.62 ? 105 HIS B ND1 1 ATOM 5181 C CD2 . HIS B 1 105 ? 32.337 27.345 19.615 1.00 14.92 ? 105 HIS B CD2 1 ATOM 5182 C CE1 . HIS B 1 105 ? 33.164 25.349 19.993 1.00 16.85 ? 105 HIS B CE1 1 ATOM 5183 N NE2 . HIS B 1 105 ? 33.408 26.510 19.412 1.00 14.46 ? 105 HIS B NE2 1 ATOM 5184 N N . ASP B 1 106 ? 26.731 27.890 19.742 1.00 12.34 ? 106 ASP B N 1 ATOM 5185 C CA . ASP B 1 106 ? 25.370 28.156 20.228 1.00 12.24 ? 106 ASP B CA 1 ATOM 5186 C C . ASP B 1 106 ? 24.411 26.969 20.125 1.00 12.76 ? 106 ASP B C 1 ATOM 5187 O O . ASP B 1 106 ? 23.440 26.895 20.873 1.00 12.32 ? 106 ASP B O 1 ATOM 5188 C CB . ASP B 1 106 ? 24.786 29.388 19.523 1.00 10.70 ? 106 ASP B CB 1 ATOM 5189 C CG . ASP B 1 106 ? 23.530 29.919 20.192 1.00 12.35 ? 106 ASP B CG 1 ATOM 5190 O OD1 . ASP B 1 106 ? 23.544 30.100 21.427 1.00 12.50 ? 106 ASP B OD1 1 ATOM 5191 O OD2 . ASP B 1 106 ? 22.536 30.154 19.479 1.00 9.94 ? 106 ASP B OD2 1 ATOM 5192 N N . GLY B 1 107 ? 24.685 26.048 19.204 1.00 13.72 ? 107 GLY B N 1 ATOM 5193 C CA . GLY B 1 107 ? 23.840 24.872 19.048 1.00 12.92 ? 107 GLY B CA 1 ATOM 5194 C C . GLY B 1 107 ? 22.498 25.082 18.375 1.00 12.16 ? 107 GLY B C 1 ATOM 5195 O O . GLY B 1 107 ? 21.567 24.307 18.587 1.00 14.11 ? 107 GLY B O 1 ATOM 5196 N N . ALA B 1 108 ? 22.399 26.134 17.572 1.00 10.86 ? 108 ALA B N 1 ATOM 5197 C CA . ALA B 1 108 ? 21.170 26.443 16.856 1.00 12.12 ? 108 ALA B CA 1 ATOM 5198 C C . ALA B 1 108 ? 21.341 25.935 15.431 1.00 10.76 ? 108 ALA B C 1 ATOM 5199 O O . ALA B 1 108 ? 21.939 26.611 14.592 1.00 9.92 ? 108 ALA B O 1 ATOM 5200 C CB . ALA B 1 108 ? 20.916 27.950 16.873 1.00 9.59 ? 108 ALA B CB 1 ATOM 5201 N N . ASN B 1 109 ? 20.865 24.717 15.173 1.00 12.01 ? 109 ASN B N 1 ATOM 5202 C CA . ASN B 1 109 ? 20.984 24.134 13.839 1.00 11.87 ? 109 ASN B CA 1 ATOM 5203 C C . ASN B 1 109 ? 20.265 24.903 12.744 1.00 13.13 ? 109 ASN B C 1 ATOM 5204 O O . ASN B 1 109 ? 19.127 25.358 12.926 1.00 12.18 ? 109 ASN B O 1 ATOM 5205 C CB . ASN B 1 109 ? 20.624 22.649 13.799 1.00 11.45 ? 109 ASN B CB 1 ATOM 5206 C CG . ASN B 1 109 ? 19.313 22.310 14.490 1.00 13.71 ? 109 ASN B CG 1 ATOM 5207 O OD1 . ASN B 1 109 ? 19.189 21.222 15.038 1.00 15.81 ? 109 ASN B OD1 1 ATOM 5208 N ND2 . ASN B 1 109 ? 18.336 23.214 14.459 1.00 13.94 ? 109 ASN B ND2 1 ATOM 5209 N N . GLY B 1 110 ? 20.978 25.090 11.635 1.00 12.36 ? 110 GLY B N 1 ATOM 5210 C CA . GLY B 1 110 ? 20.455 25.842 10.515 1.00 10.53 ? 110 GLY B CA 1 ATOM 5211 C C . GLY B 1 110 ? 20.808 27.312 10.667 1.00 10.78 ? 110 GLY B C 1 ATOM 5212 O O . GLY B 1 110 ? 20.544 28.127 9.780 1.00 10.60 ? 110 GLY B O 1 ATOM 5213 N N . VAL B 1 111 ? 21.441 27.647 11.789 1.00 10.24 ? 111 VAL B N 1 ATOM 5214 C CA . VAL B 1 111 ? 21.848 29.017 12.072 1.00 10.27 ? 111 VAL B CA 1 ATOM 5215 C C . VAL B 1 111 ? 23.351 29.045 12.360 1.00 10.48 ? 111 VAL B C 1 ATOM 5216 O O . VAL B 1 111 ? 24.122 29.557 11.554 1.00 11.84 ? 111 VAL B O 1 ATOM 5217 C CB . VAL B 1 111 ? 21.014 29.625 13.259 1.00 10.93 ? 111 VAL B CB 1 ATOM 5218 C CG1 . VAL B 1 111 ? 21.483 31.020 13.625 1.00 10.83 ? 111 VAL B CG1 1 ATOM 5219 C CG2 . VAL B 1 111 ? 19.537 29.672 12.898 1.00 10.78 ? 111 VAL B CG2 1 ATOM 5220 N N . THR B 1 112 ? 23.757 28.442 13.476 1.00 10.75 ? 112 THR B N 1 ATOM 5221 C CA . THR B 1 112 ? 25.160 28.426 13.895 1.00 11.45 ? 112 THR B CA 1 ATOM 5222 C C . THR B 1 112 ? 25.946 27.164 13.549 1.00 11.80 ? 112 THR B C 1 ATOM 5223 O O . THR B 1 112 ? 27.175 27.127 13.702 1.00 12.58 ? 112 THR B O 1 ATOM 5224 C CB . THR B 1 112 ? 25.285 28.679 15.402 1.00 10.39 ? 112 THR B CB 1 ATOM 5225 O OG1 . THR B 1 112 ? 24.651 27.616 16.125 1.00 9.83 ? 112 THR B OG1 1 ATOM 5226 C CG2 . THR B 1 112 ? 24.636 30.005 15.779 1.00 10.08 ? 112 THR B CG2 1 ATOM 5227 N N . GLU B 1 113 ? 25.223 26.133 13.122 1.00 11.50 ? 113 GLU B N 1 ATOM 5228 C CA . GLU B 1 113 ? 25.802 24.836 12.770 1.00 13.19 ? 113 GLU B CA 1 ATOM 5229 C C . GLU B 1 113 ? 24.806 23.950 12.049 1.00 11.66 ? 113 GLU B C 1 ATOM 5230 O O . GLU B 1 113 ? 23.619 24.253 11.997 1.00 10.95 ? 113 GLU B O 1 ATOM 5231 C CB . GLU B 1 113 ? 26.261 24.091 14.034 1.00 15.33 ? 113 GLU B CB 1 ATOM 5232 C CG . GLU B 1 113 ? 25.139 23.765 15.015 1.00 19.32 ? 113 GLU B CG 1 ATOM 5233 C CD . GLU B 1 113 ? 25.659 23.284 16.333 1.00 22.02 ? 113 GLU B CD 1 ATOM 5234 O OE1 . GLU B 1 113 ? 26.278 24.092 17.055 1.00 27.45 ? 113 GLU B OE1 1 ATOM 5235 O OE2 . GLU B 1 113 ? 25.442 22.105 16.650 1.00 26.25 ? 113 GLU B OE2 1 ATOM 5236 N N . CYS B 1 114 ? 25.318 22.885 11.440 1.00 11.84 ? 114 CYS B N 1 ATOM 5237 C CA . CYS B 1 114 ? 24.482 21.884 10.795 1.00 11.93 ? 114 CYS B CA 1 ATOM 5238 C C . CYS B 1 114 ? 24.254 20.886 11.920 1.00 11.44 ? 114 CYS B C 1 ATOM 5239 O O . CYS B 1 114 ? 25.055 20.841 12.864 1.00 12.25 ? 114 CYS B O 1 ATOM 5240 C CB . CYS B 1 114 ? 25.238 21.172 9.681 1.00 12.19 ? 114 CYS B CB 1 ATOM 5241 S SG . CYS B 1 114 ? 25.454 22.115 8.149 1.00 13.00 ? 114 CYS B SG 1 ATOM 5242 N N . PRO B 1 115 ? 23.156 20.100 11.870 1.00 11.42 ? 115 PRO B N 1 ATOM 5243 C CA . PRO B 1 115 ? 22.919 19.125 12.936 1.00 12.28 ? 115 PRO B CA 1 ATOM 5244 C C . PRO B 1 115 ? 23.984 18.043 12.923 1.00 12.85 ? 115 PRO B C 1 ATOM 5245 O O . PRO B 1 115 ? 24.565 17.744 11.878 1.00 10.38 ? 115 PRO B O 1 ATOM 5246 C CB . PRO B 1 115 ? 21.577 18.510 12.553 1.00 12.63 ? 115 PRO B CB 1 ATOM 5247 C CG . PRO B 1 115 ? 20.908 19.560 11.820 1.00 13.46 ? 115 PRO B CG 1 ATOM 5248 C CD . PRO B 1 115 ? 21.983 20.163 10.980 1.00 11.50 ? 115 PRO B CD 1 ATOM 5249 N N . ILE B 1 116 ? 24.265 17.504 14.103 1.00 13.70 ? 116 ILE B N 1 ATOM 5250 C CA . ILE B 1 116 ? 25.231 16.431 14.260 1.00 15.39 ? 116 ILE B CA 1 ATOM 5251 C C . ILE B 1 116 ? 24.499 15.200 13.708 1.00 15.77 ? 116 ILE B C 1 ATOM 5252 O O . ILE B 1 116 ? 23.399 14.890 14.168 1.00 16.56 ? 116 ILE B O 1 ATOM 5253 C CB . ILE B 1 116 ? 25.584 16.241 15.754 1.00 16.02 ? 116 ILE B CB 1 ATOM 5254 C CG1 . ILE B 1 116 ? 26.118 17.550 16.340 1.00 16.54 ? 116 ILE B CG1 1 ATOM 5255 C CG2 . ILE B 1 116 ? 26.613 15.174 15.909 1.00 16.28 ? 116 ILE B CG2 1 ATOM 5256 C CD1 . ILE B 1 116 ? 26.077 17.617 17.848 1.00 18.19 ? 116 ILE B CD1 1 ATOM 5257 N N . PRO B 1 117 ? 25.060 14.533 12.671 1.00 15.62 ? 117 PRO B N 1 ATOM 5258 C CA . PRO B 1 117 ? 24.399 13.351 12.102 1.00 14.36 ? 117 PRO B CA 1 ATOM 5259 C C . PRO B 1 117 ? 24.230 12.187 13.084 1.00 15.38 ? 117 PRO B C 1 ATOM 5260 O O . PRO B 1 117 ? 24.996 12.069 14.045 1.00 15.63 ? 117 PRO B O 1 ATOM 5261 C CB . PRO B 1 117 ? 25.305 12.992 10.914 1.00 14.72 ? 117 PRO B CB 1 ATOM 5262 C CG . PRO B 1 117 ? 26.653 13.470 11.349 1.00 15.25 ? 117 PRO B CG 1 ATOM 5263 C CD . PRO B 1 117 ? 26.323 14.809 11.954 1.00 14.84 ? 117 PRO B CD 1 ATOM 5264 N N . PRO B 1 118 ? 23.165 11.373 12.915 1.00 15.33 ? 118 PRO B N 1 ATOM 5265 C CA . PRO B 1 118 ? 22.938 10.231 13.807 1.00 16.00 ? 118 PRO B CA 1 ATOM 5266 C C . PRO B 1 118 ? 23.917 9.089 13.524 1.00 16.48 ? 118 PRO B C 1 ATOM 5267 O O . PRO B 1 118 ? 24.870 9.267 12.763 1.00 15.19 ? 118 PRO B O 1 ATOM 5268 C CB . PRO B 1 118 ? 21.500 9.839 13.482 1.00 15.24 ? 118 PRO B CB 1 ATOM 5269 C CG . PRO B 1 118 ? 21.400 10.146 12.064 1.00 15.74 ? 118 PRO B CG 1 ATOM 5270 C CD . PRO B 1 118 ? 22.033 11.504 11.981 1.00 14.74 ? 118 PRO B CD 1 ATOM 5271 N N . LYS B 1 119 ? 23.672 7.934 14.146 1.00 18.26 ? 119 LYS B N 1 ATOM 5272 C CA . LYS B 1 119 ? 24.494 6.729 13.991 1.00 21.90 ? 119 LYS B CA 1 ATOM 5273 C C . LYS B 1 119 ? 25.989 6.893 14.344 1.00 20.93 ? 119 LYS B C 1 ATOM 5274 O O . LYS B 1 119 ? 26.857 6.311 13.691 1.00 22.17 ? 119 LYS B O 1 ATOM 5275 C CB . LYS B 1 119 ? 24.315 6.122 12.579 1.00 24.38 ? 119 LYS B CB 1 ATOM 5276 C CG . LYS B 1 119 ? 22.881 5.701 12.205 1.00 28.95 ? 119 LYS B CG 1 ATOM 5277 C CD . LYS B 1 119 ? 22.348 4.589 13.101 1.00 33.74 ? 119 LYS B CD 1 ATOM 5278 C CE . LYS B 1 119 ? 21.059 4.000 12.553 1.00 36.51 ? 119 LYS B CE 1 ATOM 5279 N NZ . LYS B 1 119 ? 20.456 3.036 13.519 1.00 38.91 ? 119 LYS B NZ 1 ATOM 5280 N N . GLY B 1 120 ? 26.275 7.729 15.344 1.00 19.09 ? 120 GLY B N 1 ATOM 5281 C CA . GLY B 1 120 ? 27.648 7.926 15.788 1.00 17.24 ? 120 GLY B CA 1 ATOM 5282 C C . GLY B 1 120 ? 28.336 9.248 15.509 1.00 16.63 ? 120 GLY B C 1 ATOM 5283 O O . GLY B 1 120 ? 29.516 9.400 15.844 1.00 16.06 ? 120 GLY B O 1 ATOM 5284 N N . GLY B 1 121 ? 27.617 10.196 14.903 1.00 16.13 ? 121 GLY B N 1 ATOM 5285 C CA . GLY B 1 121 ? 28.180 11.507 14.602 1.00 14.67 ? 121 GLY B CA 1 ATOM 5286 C C . GLY B 1 121 ? 28.487 12.275 15.874 1.00 15.16 ? 121 GLY B C 1 ATOM 5287 O O . GLY B 1 121 ? 27.746 12.158 16.858 1.00 14.96 ? 121 GLY B O 1 ATOM 5288 N N . GLN B 1 122 ? 29.574 13.046 15.867 1.00 15.13 ? 122 GLN B N 1 ATOM 5289 C CA . GLN B 1 122 ? 29.967 13.811 17.042 1.00 15.31 ? 122 GLN B CA 1 ATOM 5290 C C . GLN B 1 122 ? 30.470 15.223 16.781 1.00 15.49 ? 122 GLN B C 1 ATOM 5291 O O . GLN B 1 122 ? 30.890 15.558 15.674 1.00 14.21 ? 122 GLN B O 1 ATOM 5292 C CB . GLN B 1 122 ? 30.990 13.038 17.884 1.00 17.91 ? 122 GLN B CB 1 ATOM 5293 C CG . GLN B 1 122 ? 32.393 12.924 17.298 1.00 19.67 ? 122 GLN B CG 1 ATOM 5294 C CD . GLN B 1 122 ? 33.262 11.994 18.107 1.00 22.38 ? 122 GLN B CD 1 ATOM 5295 O OE1 . GLN B 1 122 ? 33.220 10.781 17.915 1.00 24.05 ? 122 GLN B OE1 1 ATOM 5296 N NE2 . GLN B 1 122 ? 34.044 12.552 19.029 1.00 17.73 ? 122 GLN B NE2 1 ATOM 5297 N N . ARG B 1 123 ? 30.403 16.036 17.831 1.00 14.80 ? 123 ARG B N 1 ATOM 5298 C CA . ARG B 1 123 ? 30.865 17.418 17.820 1.00 15.90 ? 123 ARG B CA 1 ATOM 5299 C C . ARG B 1 123 ? 31.095 17.796 19.272 1.00 15.18 ? 123 ARG B C 1 ATOM 5300 O O . ARG B 1 123 ? 30.303 17.449 20.148 1.00 16.38 ? 123 ARG B O 1 ATOM 5301 C CB . ARG B 1 123 ? 29.825 18.361 17.192 1.00 17.58 ? 123 ARG B CB 1 ATOM 5302 C CG . ARG B 1 123 ? 30.314 19.791 16.943 1.00 19.58 ? 123 ARG B CG 1 ATOM 5303 C CD . ARG B 1 123 ? 29.686 20.785 17.903 1.00 20.29 ? 123 ARG B CD 1 ATOM 5304 N NE . ARG B 1 123 ? 30.466 22.019 17.989 1.00 21.32 ? 123 ARG B NE 1 ATOM 5305 C CZ . ARG B 1 123 ? 30.042 23.216 17.594 1.00 19.64 ? 123 ARG B CZ 1 ATOM 5306 N NH1 . ARG B 1 123 ? 30.839 24.267 17.712 1.00 20.26 ? 123 ARG B NH1 1 ATOM 5307 N NH2 . ARG B 1 123 ? 28.828 23.369 17.090 1.00 18.50 ? 123 ARG B NH2 1 ATOM 5308 N N . THR B 1 124 ? 32.170 18.536 19.502 1.00 15.48 ? 124 THR B N 1 ATOM 5309 C CA . THR B 1 124 ? 32.528 18.993 20.827 1.00 15.97 ? 124 THR B CA 1 ATOM 5310 C C . THR B 1 124 ? 32.288 20.492 20.954 1.00 16.06 ? 124 THR B C 1 ATOM 5311 O O . THR B 1 124 ? 32.889 21.291 20.227 1.00 15.77 ? 124 THR B O 1 ATOM 5312 C CB . THR B 1 124 ? 33.998 18.634 21.169 1.00 16.22 ? 124 THR B CB 1 ATOM 5313 O OG1 . THR B 1 124 ? 34.167 17.212 21.105 1.00 14.72 ? 124 THR B OG1 1 ATOM 5314 C CG2 . THR B 1 124 ? 34.352 19.080 22.576 1.00 15.80 ? 124 THR B CG2 1 ATOM 5315 N N . TYR B 1 125 ? 31.381 20.849 21.865 1.00 15.10 ? 125 TYR B N 1 ATOM 5316 C CA . TYR B 1 125 ? 31.046 22.244 22.145 1.00 15.88 ? 125 TYR B CA 1 ATOM 5317 C C . TYR B 1 125 ? 31.989 22.715 23.228 1.00 15.86 ? 125 TYR B C 1 ATOM 5318 O O . TYR B 1 125 ? 32.315 21.954 24.143 1.00 14.01 ? 125 TYR B O 1 ATOM 5319 C CB . TYR B 1 125 ? 29.620 22.391 22.664 1.00 15.03 ? 125 TYR B CB 1 ATOM 5320 C CG . TYR B 1 125 ? 28.541 22.079 21.667 1.00 14.98 ? 125 TYR B CG 1 ATOM 5321 C CD1 . TYR B 1 125 ? 28.033 20.772 21.543 1.00 14.09 ? 125 TYR B CD1 1 ATOM 5322 C CD2 . TYR B 1 125 ? 27.983 23.094 20.866 1.00 15.30 ? 125 TYR B CD2 1 ATOM 5323 C CE1 . TYR B 1 125 ? 26.985 20.475 20.642 1.00 14.73 ? 125 TYR B CE1 1 ATOM 5324 C CE2 . TYR B 1 125 ? 26.932 22.813 19.959 1.00 14.95 ? 125 TYR B CE2 1 ATOM 5325 C CZ . TYR B 1 125 ? 26.442 21.499 19.859 1.00 16.27 ? 125 TYR B CZ 1 ATOM 5326 O OH . TYR B 1 125 ? 25.422 21.205 19.001 1.00 14.18 ? 125 TYR B OH 1 ATOM 5327 N N . ARG B 1 126 ? 32.411 23.970 23.127 1.00 16.32 ? 126 ARG B N 1 ATOM 5328 C CA . ARG B 1 126 ? 33.328 24.549 24.094 1.00 18.65 ? 126 ARG B CA 1 ATOM 5329 C C . ARG B 1 126 ? 32.964 26.013 24.309 1.00 17.05 ? 126 ARG B C 1 ATOM 5330 O O . ARG B 1 126 ? 32.992 26.814 23.373 1.00 18.60 ? 126 ARG B O 1 ATOM 5331 C CB . ARG B 1 126 ? 34.771 24.414 23.592 1.00 19.49 ? 126 ARG B CB 1 ATOM 5332 C CG . ARG B 1 126 ? 35.810 24.517 24.683 1.00 23.08 ? 126 ARG B CG 1 ATOM 5333 C CD . ARG B 1 126 ? 37.206 24.664 24.117 1.00 24.41 ? 126 ARG B CD 1 ATOM 5334 N NE . ARG B 1 126 ? 38.203 24.863 25.170 1.00 26.20 ? 126 ARG B NE 1 ATOM 5335 C CZ . ARG B 1 126 ? 38.727 26.039 25.512 1.00 27.88 ? 126 ARG B CZ 1 ATOM 5336 N NH1 . ARG B 1 126 ? 38.359 27.155 24.889 1.00 30.43 ? 126 ARG B NH1 1 ATOM 5337 N NH2 . ARG B 1 126 ? 39.621 26.103 26.491 1.00 26.45 ? 126 ARG B NH2 1 ATOM 5338 N N . TRP B 1 127 ? 32.590 26.345 25.542 1.00 17.02 ? 127 TRP B N 1 ATOM 5339 C CA . TRP B 1 127 ? 32.214 27.714 25.882 1.00 16.85 ? 127 TRP B CA 1 ATOM 5340 C C . TRP B 1 127 ? 32.707 28.184 27.237 1.00 17.04 ? 127 TRP B C 1 ATOM 5341 O O . TRP B 1 127 ? 32.845 27.394 28.171 1.00 16.37 ? 127 TRP B O 1 ATOM 5342 C CB . TRP B 1 127 ? 30.694 27.939 25.755 1.00 17.90 ? 127 TRP B CB 1 ATOM 5343 C CG . TRP B 1 127 ? 29.795 26.895 26.373 1.00 17.70 ? 127 TRP B CG 1 ATOM 5344 C CD1 . TRP B 1 127 ? 29.275 25.794 25.749 1.00 18.22 ? 127 TRP B CD1 1 ATOM 5345 C CD2 . TRP B 1 127 ? 29.252 26.896 27.703 1.00 18.59 ? 127 TRP B CD2 1 ATOM 5346 N NE1 . TRP B 1 127 ? 28.436 25.113 26.599 1.00 18.36 ? 127 TRP B NE1 1 ATOM 5347 C CE2 . TRP B 1 127 ? 28.397 25.761 27.804 1.00 17.92 ? 127 TRP B CE2 1 ATOM 5348 C CE3 . TRP B 1 127 ? 29.398 27.745 28.823 1.00 18.66 ? 127 TRP B CE3 1 ATOM 5349 C CZ2 . TRP B 1 127 ? 27.681 25.449 28.988 1.00 18.86 ? 127 TRP B CZ2 1 ATOM 5350 C CZ3 . TRP B 1 127 ? 28.683 27.438 30.013 1.00 17.82 ? 127 TRP B CZ3 1 ATOM 5351 C CH2 . TRP B 1 127 ? 27.835 26.293 30.077 1.00 18.72 ? 127 TRP B CH2 1 ATOM 5352 N N . ARG B 1 128 ? 32.937 29.490 27.329 1.00 15.59 ? 128 ARG B N 1 ATOM 5353 C CA . ARG B 1 128 ? 33.415 30.122 28.546 1.00 15.20 ? 128 ARG B CA 1 ATOM 5354 C C . ARG B 1 128 ? 32.218 30.545 29.396 1.00 15.47 ? 128 ARG B C 1 ATOM 5355 O O . ARG B 1 128 ? 31.232 31.078 28.877 1.00 15.43 ? 128 ARG B O 1 ATOM 5356 C CB . ARG B 1 128 ? 34.291 31.328 28.185 1.00 15.58 ? 128 ARG B CB 1 ATOM 5357 C CG . ARG B 1 128 ? 35.000 32.002 29.355 1.00 17.24 ? 128 ARG B CG 1 ATOM 5358 C CD . ARG B 1 128 ? 36.211 31.241 29.875 1.00 18.24 ? 128 ARG B CD 1 ATOM 5359 N NE . ARG B 1 128 ? 36.897 32.015 30.916 1.00 19.11 ? 128 ARG B NE 1 ATOM 5360 C CZ . ARG B 1 128 ? 37.721 33.038 30.691 1.00 17.50 ? 128 ARG B CZ 1 ATOM 5361 N NH1 . ARG B 1 128 ? 37.999 33.428 29.451 1.00 19.75 ? 128 ARG B NH1 1 ATOM 5362 N NH2 . ARG B 1 128 ? 38.207 33.727 31.713 1.00 18.06 ? 128 ARG B NH2 1 ATOM 5363 N N . ALA B 1 129 ? 32.301 30.255 30.693 1.00 15.32 ? 129 ALA B N 1 ATOM 5364 C CA . ALA B 1 129 ? 31.248 30.599 31.646 1.00 15.40 ? 129 ALA B CA 1 ATOM 5365 C C . ALA B 1 129 ? 31.438 32.042 32.126 1.00 14.51 ? 129 ALA B C 1 ATOM 5366 O O . ALA B 1 129 ? 32.020 32.294 33.184 1.00 15.26 ? 129 ALA B O 1 ATOM 5367 C CB . ALA B 1 129 ? 31.264 29.619 32.813 1.00 13.30 ? 129 ALA B CB 1 ATOM 5368 N N . ARG B 1 130 ? 30.965 32.982 31.306 1.00 14.89 ? 130 ARG B N 1 ATOM 5369 C CA . ARG B 1 130 ? 31.064 34.421 31.582 1.00 16.09 ? 130 ARG B CA 1 ATOM 5370 C C . ARG B 1 130 ? 29.873 34.948 32.373 1.00 15.41 ? 130 ARG B C 1 ATOM 5371 O O . ARG B 1 130 ? 29.688 36.163 32.529 1.00 14.59 ? 130 ARG B O 1 ATOM 5372 C CB . ARG B 1 130 ? 31.200 35.211 30.272 1.00 15.52 ? 130 ARG B CB 1 ATOM 5373 C CG . ARG B 1 130 ? 32.387 34.801 29.440 1.00 18.21 ? 130 ARG B CG 1 ATOM 5374 C CD . ARG B 1 130 ? 32.714 35.821 28.373 1.00 18.11 ? 130 ARG B CD 1 ATOM 5375 N NE . ARG B 1 130 ? 33.829 35.380 27.538 1.00 19.03 ? 130 ARG B NE 1 ATOM 5376 C CZ . ARG B 1 130 ? 35.114 35.627 27.791 1.00 21.11 ? 130 ARG B CZ 1 ATOM 5377 N NH1 . ARG B 1 130 ? 35.471 36.322 28.866 1.00 17.88 ? 130 ARG B NH1 1 ATOM 5378 N NH2 . ARG B 1 130 ? 36.047 35.156 26.974 1.00 20.98 ? 130 ARG B NH2 1 ATOM 5379 N N . GLN B 1 131 ? 29.073 34.018 32.876 1.00 14.35 ? 131 GLN B N 1 ATOM 5380 C CA . GLN B 1 131 ? 27.890 34.352 33.638 1.00 15.95 ? 131 GLN B CA 1 ATOM 5381 C C . GLN B 1 131 ? 27.665 33.258 34.653 1.00 15.99 ? 131 GLN B C 1 ATOM 5382 O O . GLN B 1 131 ? 27.936 32.084 34.384 1.00 19.80 ? 131 GLN B O 1 ATOM 5383 C CB . GLN B 1 131 ? 26.690 34.462 32.696 1.00 17.01 ? 131 GLN B CB 1 ATOM 5384 C CG . GLN B 1 131 ? 25.523 35.265 33.250 1.00 21.78 ? 131 GLN B CG 1 ATOM 5385 C CD . GLN B 1 131 ? 24.750 36.018 32.181 1.00 23.19 ? 131 GLN B CD 1 ATOM 5386 O OE1 . GLN B 1 131 ? 25.226 36.185 31.061 1.00 27.17 ? 131 GLN B OE1 1 ATOM 5387 N NE2 . GLN B 1 131 ? 23.570 36.512 32.538 1.00 18.02 ? 131 GLN B NE2 1 ATOM 5388 N N . TYR B 1 132 ? 27.191 33.657 35.826 1.00 13.47 ? 132 TYR B N 1 ATOM 5389 C CA . TYR B 1 132 ? 26.914 32.725 36.901 1.00 12.29 ? 132 TYR B CA 1 ATOM 5390 C C . TYR B 1 132 ? 25.431 32.687 37.237 1.00 12.01 ? 132 TYR B C 1 ATOM 5391 O O . TYR B 1 132 ? 24.739 33.712 37.198 1.00 11.84 ? 132 TYR B O 1 ATOM 5392 C CB . TYR B 1 132 ? 27.758 33.043 38.144 1.00 12.51 ? 132 TYR B CB 1 ATOM 5393 C CG . TYR B 1 132 ? 27.663 34.472 38.639 1.00 12.24 ? 132 TYR B CG 1 ATOM 5394 C CD1 . TYR B 1 132 ? 28.438 35.490 38.053 1.00 12.52 ? 132 TYR B CD1 1 ATOM 5395 C CD2 . TYR B 1 132 ? 26.767 34.824 39.664 1.00 11.10 ? 132 TYR B CD2 1 ATOM 5396 C CE1 . TYR B 1 132 ? 28.321 36.838 38.472 1.00 13.63 ? 132 TYR B CE1 1 ATOM 5397 C CE2 . TYR B 1 132 ? 26.639 36.164 40.089 1.00 10.89 ? 132 TYR B CE2 1 ATOM 5398 C CZ . TYR B 1 132 ? 27.414 37.162 39.488 1.00 10.48 ? 132 TYR B CZ 1 ATOM 5399 O OH . TYR B 1 132 ? 27.270 38.463 39.886 1.00 13.47 ? 132 TYR B OH 1 ATOM 5400 N N . GLY B 1 133 ? 24.965 31.499 37.589 1.00 10.78 ? 133 GLY B N 1 ATOM 5401 C CA . GLY B 1 133 ? 23.574 31.323 37.932 1.00 12.67 ? 133 GLY B CA 1 ATOM 5402 C C . GLY B 1 133 ? 23.053 30.024 37.381 1.00 12.57 ? 133 GLY B C 1 ATOM 5403 O O . GLY B 1 133 ? 23.824 29.095 37.112 1.00 13.79 ? 133 GLY B O 1 ATOM 5404 N N . THR B 1 134 ? 21.747 29.992 37.145 1.00 12.23 ? 134 THR B N 1 ATOM 5405 C CA . THR B 1 134 ? 21.088 28.801 36.650 1.00 10.55 ? 134 THR B CA 1 ATOM 5406 C C . THR B 1 134 ? 20.565 28.966 35.238 1.00 10.84 ? 134 THR B C 1 ATOM 5407 O O . THR B 1 134 ? 19.849 29.917 34.917 1.00 11.56 ? 134 THR B O 1 ATOM 5408 C CB . THR B 1 134 ? 19.939 28.387 37.577 1.00 11.27 ? 134 THR B CB 1 ATOM 5409 O OG1 . THR B 1 134 ? 20.368 28.522 38.935 1.00 10.32 ? 134 THR B OG1 1 ATOM 5410 C CG2 . THR B 1 134 ? 19.546 26.940 37.341 1.00 10.77 ? 134 THR B CG2 1 ATOM 5411 N N . SER B 1 135 ? 20.962 28.018 34.405 1.00 11.00 ? 135 SER B N 1 ATOM 5412 C CA . SER B 1 135 ? 20.565 27.959 33.015 1.00 10.98 ? 135 SER B CA 1 ATOM 5413 C C . SER B 1 135 ? 20.281 26.501 32.699 1.00 10.76 ? 135 SER B C 1 ATOM 5414 O O . SER B 1 135 ? 20.254 25.657 33.601 1.00 9.26 ? 135 SER B O 1 ATOM 5415 C CB . SER B 1 135 ? 21.670 28.518 32.122 1.00 12.77 ? 135 SER B CB 1 ATOM 5416 O OG . SER B 1 135 ? 21.649 29.935 32.135 1.00 17.66 ? 135 SER B OG 1 ATOM 5417 N N . TRP B 1 136 ? 20.049 26.211 31.426 1.00 9.63 ? 136 TRP B N 1 ATOM 5418 C CA . TRP B 1 136 ? 19.764 24.858 30.992 1.00 10.30 ? 136 TRP B CA 1 ATOM 5419 C C . TRP B 1 136 ? 20.172 24.663 29.551 1.00 10.70 ? 136 TRP B C 1 ATOM 5420 O O . TRP B 1 136 ? 20.578 25.611 28.873 1.00 12.84 ? 136 TRP B O 1 ATOM 5421 C CB . TRP B 1 136 ? 18.276 24.504 31.198 1.00 8.81 ? 136 TRP B CB 1 ATOM 5422 C CG . TRP B 1 136 ? 17.277 25.309 30.412 1.00 9.36 ? 136 TRP B CG 1 ATOM 5423 C CD1 . TRP B 1 136 ? 17.112 26.669 30.421 1.00 9.90 ? 136 TRP B CD1 1 ATOM 5424 C CD2 . TRP B 1 136 ? 16.266 24.789 29.547 1.00 7.67 ? 136 TRP B CD2 1 ATOM 5425 N NE1 . TRP B 1 136 ? 16.055 27.027 29.620 1.00 9.59 ? 136 TRP B NE1 1 ATOM 5426 C CE2 . TRP B 1 136 ? 15.513 25.894 29.071 1.00 8.02 ? 136 TRP B CE2 1 ATOM 5427 C CE3 . TRP B 1 136 ? 15.912 23.490 29.129 1.00 7.68 ? 136 TRP B CE3 1 ATOM 5428 C CZ2 . TRP B 1 136 ? 14.416 25.742 28.194 1.00 5.98 ? 136 TRP B CZ2 1 ATOM 5429 C CZ3 . TRP B 1 136 ? 14.809 23.332 28.251 1.00 6.66 ? 136 TRP B CZ3 1 ATOM 5430 C CH2 . TRP B 1 136 ? 14.076 24.461 27.799 1.00 9.73 ? 136 TRP B CH2 1 ATOM 5431 N N . TYR B 1 137 ? 20.154 23.410 29.125 1.00 12.87 ? 137 TYR B N 1 ATOM 5432 C CA . TYR B 1 137 ? 20.484 23.077 27.760 1.00 11.98 ? 137 TYR B CA 1 ATOM 5433 C C . TYR B 1 137 ? 19.410 22.187 27.185 1.00 12.03 ? 137 TYR B C 1 ATOM 5434 O O . TYR B 1 137 ? 18.741 21.453 27.919 1.00 11.38 ? 137 TYR B O 1 ATOM 5435 C CB . TYR B 1 137 ? 21.872 22.434 27.637 1.00 13.14 ? 137 TYR B CB 1 ATOM 5436 C CG . TYR B 1 137 ? 22.093 21.140 28.388 1.00 12.63 ? 137 TYR B CG 1 ATOM 5437 C CD1 . TYR B 1 137 ? 21.682 19.905 27.846 1.00 12.03 ? 137 TYR B CD1 1 ATOM 5438 C CD2 . TYR B 1 137 ? 22.717 21.142 29.649 1.00 13.46 ? 137 TYR B CD2 1 ATOM 5439 C CE1 . TYR B 1 137 ? 21.878 18.705 28.541 1.00 13.67 ? 137 TYR B CE1 1 ATOM 5440 C CE2 . TYR B 1 137 ? 22.930 19.939 30.358 1.00 11.90 ? 137 TYR B CE2 1 ATOM 5441 C CZ . TYR B 1 137 ? 22.504 18.733 29.795 1.00 12.90 ? 137 TYR B CZ 1 ATOM 5442 O OH . TYR B 1 137 ? 22.686 17.561 30.470 1.00 13.05 ? 137 TYR B OH 1 ATOM 5443 N N . HIS B 1 138 ? 19.293 22.225 25.864 1.00 9.92 ? 138 HIS B N 1 ATOM 5444 C CA . HIS B 1 138 ? 18.305 21.433 25.161 1.00 10.36 ? 138 HIS B CA 1 ATOM 5445 C C . HIS B 1 138 ? 18.627 21.356 23.683 1.00 10.59 ? 138 HIS B C 1 ATOM 5446 O O . HIS B 1 138 ? 19.366 22.190 23.154 1.00 8.97 ? 138 HIS B O 1 ATOM 5447 C CB . HIS B 1 138 ? 16.899 22.028 25.364 1.00 10.15 ? 138 HIS B CB 1 ATOM 5448 C CG . HIS B 1 138 ? 16.743 23.437 24.873 1.00 11.69 ? 138 HIS B CG 1 ATOM 5449 N ND1 . HIS B 1 138 ? 16.468 23.735 23.558 1.00 13.20 ? 138 HIS B ND1 1 ATOM 5450 C CD2 . HIS B 1 138 ? 16.789 24.623 25.526 1.00 12.04 ? 138 HIS B CD2 1 ATOM 5451 C CE1 . HIS B 1 138 ? 16.343 25.042 23.422 1.00 12.46 ? 138 HIS B CE1 1 ATOM 5452 N NE2 . HIS B 1 138 ? 16.532 25.606 24.603 1.00 15.45 ? 138 HIS B NE2 1 ATOM 5453 N N . SER B 1 139 ? 18.029 20.377 23.012 1.00 11.90 ? 139 SER B N 1 ATOM 5454 C CA . SER B 1 139 ? 18.206 20.225 21.573 1.00 13.10 ? 139 SER B CA 1 ATOM 5455 C C . SER B 1 139 ? 17.422 21.324 20.868 1.00 12.47 ? 139 SER B C 1 ATOM 5456 O O . SER B 1 139 ? 16.412 21.799 21.397 1.00 12.19 ? 139 SER B O 1 ATOM 5457 C CB . SER B 1 139 ? 17.684 18.875 21.101 1.00 12.13 ? 139 SER B CB 1 ATOM 5458 O OG . SER B 1 139 ? 17.809 18.747 19.696 1.00 14.17 ? 139 SER B OG 1 ATOM 5459 N N . HIS B 1 140 ? 17.923 21.753 19.710 1.00 13.96 ? 140 HIS B N 1 ATOM 5460 C CA . HIS B 1 140 ? 17.248 22.766 18.908 1.00 12.90 ? 140 HIS B CA 1 ATOM 5461 C C . HIS B 1 140 ? 16.822 22.177 17.566 1.00 12.45 ? 140 HIS B C 1 ATOM 5462 O O . HIS B 1 140 ? 16.413 22.905 16.661 1.00 11.69 ? 140 HIS B O 1 ATOM 5463 C CB . HIS B 1 140 ? 18.115 24.019 18.721 1.00 15.28 ? 140 HIS B CB 1 ATOM 5464 C CG . HIS B 1 140 ? 17.398 25.296 19.039 1.00 14.96 ? 140 HIS B CG 1 ATOM 5465 N ND1 . HIS B 1 140 ? 16.135 25.583 18.567 1.00 16.32 ? 140 HIS B ND1 1 ATOM 5466 C CD2 . HIS B 1 140 ? 17.753 26.348 19.814 1.00 16.76 ? 140 HIS B CD2 1 ATOM 5467 C CE1 . HIS B 1 140 ? 15.743 26.754 19.040 1.00 16.93 ? 140 HIS B CE1 1 ATOM 5468 N NE2 . HIS B 1 140 ? 16.707 27.240 19.801 1.00 17.04 ? 140 HIS B NE2 1 ATOM 5469 N N . PHE B 1 141 ? 16.888 20.845 17.468 1.00 11.45 ? 141 PHE B N 1 ATOM 5470 C CA . PHE B 1 141 ? 16.498 20.096 16.265 1.00 12.12 ? 141 PHE B CA 1 ATOM 5471 C C . PHE B 1 141 ? 14.996 19.915 16.356 1.00 12.05 ? 141 PHE B C 1 ATOM 5472 O O . PHE B 1 141 ? 14.520 18.931 16.930 1.00 10.27 ? 141 PHE B O 1 ATOM 5473 C CB . PHE B 1 141 ? 17.217 18.735 16.239 1.00 12.20 ? 141 PHE B CB 1 ATOM 5474 C CG . PHE B 1 141 ? 17.031 17.953 14.958 1.00 13.78 ? 141 PHE B CG 1 ATOM 5475 C CD1 . PHE B 1 141 ? 17.872 18.181 13.857 1.00 12.96 ? 141 PHE B CD1 1 ATOM 5476 C CD2 . PHE B 1 141 ? 16.057 16.930 14.871 1.00 14.45 ? 141 PHE B CD2 1 ATOM 5477 C CE1 . PHE B 1 141 ? 17.761 17.393 12.676 1.00 14.12 ? 141 PHE B CE1 1 ATOM 5478 C CE2 . PHE B 1 141 ? 15.930 16.137 13.696 1.00 15.00 ? 141 PHE B CE2 1 ATOM 5479 C CZ . PHE B 1 141 ? 16.785 16.365 12.601 1.00 12.90 ? 141 PHE B CZ 1 ATOM 5480 N N . SER B 1 142 ? 14.258 20.866 15.778 1.00 11.93 ? 142 SER B N 1 ATOM 5481 C CA . SER B 1 142 ? 12.790 20.886 15.824 1.00 12.74 ? 142 SER B CA 1 ATOM 5482 C C . SER B 1 142 ? 12.366 20.868 17.303 1.00 12.43 ? 142 SER B C 1 ATOM 5483 O O . SER B 1 142 ? 12.939 21.620 18.098 1.00 13.10 ? 142 SER B O 1 ATOM 5484 C CB . SER B 1 142 ? 12.178 19.753 14.987 1.00 15.03 ? 142 SER B CB 1 ATOM 5485 O OG . SER B 1 142 ? 12.502 19.943 13.620 1.00 15.75 ? 142 SER B OG 1 ATOM 5486 N N . ALA B 1 143 ? 11.453 19.981 17.689 1.00 11.14 ? 143 ALA B N 1 ATOM 5487 C CA . ALA B 1 143 ? 11.010 19.897 19.078 1.00 10.52 ? 143 ALA B CA 1 ATOM 5488 C C . ALA B 1 143 ? 11.587 18.665 19.782 1.00 10.94 ? 143 ALA B C 1 ATOM 5489 O O . ALA B 1 143 ? 11.018 18.184 20.761 1.00 9.92 ? 143 ALA B O 1 ATOM 5490 C CB . ALA B 1 143 ? 9.490 19.879 19.133 1.00 10.88 ? 143 ALA B CB 1 ATOM 5491 N N . GLN B 1 144 ? 12.754 18.208 19.321 1.00 10.93 ? 144 GLN B N 1 ATOM 5492 C CA . GLN B 1 144 ? 13.438 17.022 19.856 1.00 11.53 ? 144 GLN B CA 1 ATOM 5493 C C . GLN B 1 144 ? 13.651 17.008 21.371 1.00 12.69 ? 144 GLN B C 1 ATOM 5494 O O . GLN B 1 144 ? 13.612 15.937 21.985 1.00 10.71 ? 144 GLN B O 1 ATOM 5495 C CB . GLN B 1 144 ? 14.774 16.825 19.141 1.00 10.90 ? 144 GLN B CB 1 ATOM 5496 C CG . GLN B 1 144 ? 15.463 15.493 19.382 1.00 11.39 ? 144 GLN B CG 1 ATOM 5497 C CD . GLN B 1 144 ? 16.820 15.444 18.737 1.00 11.43 ? 144 GLN B CD 1 ATOM 5498 O OE1 . GLN B 1 144 ? 17.008 14.816 17.706 1.00 13.63 ? 144 GLN B OE1 1 ATOM 5499 N NE2 . GLN B 1 144 ? 17.777 16.122 19.340 1.00 7.83 ? 144 GLN B NE2 1 ATOM 5500 N N . TYR B 1 145 ? 13.806 18.189 21.981 1.00 13.04 ? 145 TYR B N 1 ATOM 5501 C CA . TYR B 1 145 ? 14.006 18.255 23.432 1.00 13.07 ? 145 TYR B CA 1 ATOM 5502 C C . TYR B 1 145 ? 12.794 17.753 24.220 1.00 13.23 ? 145 TYR B C 1 ATOM 5503 O O . TYR B 1 145 ? 12.915 17.358 25.383 1.00 14.73 ? 145 TYR B O 1 ATOM 5504 C CB . TYR B 1 145 ? 14.513 19.637 23.884 1.00 11.30 ? 145 TYR B CB 1 ATOM 5505 C CG . TYR B 1 145 ? 13.519 20.755 24.164 1.00 11.74 ? 145 TYR B CG 1 ATOM 5506 C CD1 . TYR B 1 145 ? 12.900 20.875 25.432 1.00 9.54 ? 145 TYR B CD1 1 ATOM 5507 C CD2 . TYR B 1 145 ? 13.279 21.765 23.209 1.00 11.72 ? 145 TYR B CD2 1 ATOM 5508 C CE1 . TYR B 1 145 ? 12.069 21.979 25.747 1.00 9.89 ? 145 TYR B CE1 1 ATOM 5509 C CE2 . TYR B 1 145 ? 12.447 22.881 23.513 1.00 10.78 ? 145 TYR B CE2 1 ATOM 5510 C CZ . TYR B 1 145 ? 11.851 22.976 24.786 1.00 10.20 ? 145 TYR B CZ 1 ATOM 5511 O OH . TYR B 1 145 ? 11.052 24.049 25.104 1.00 8.55 ? 145 TYR B OH 1 ATOM 5512 N N . GLY B 1 146 ? 11.647 17.718 23.538 1.00 12.59 ? 146 GLY B N 1 ATOM 5513 C CA . GLY B 1 146 ? 10.411 17.222 24.121 1.00 14.68 ? 146 GLY B CA 1 ATOM 5514 C C . GLY B 1 146 ? 10.438 15.716 24.313 1.00 14.53 ? 146 GLY B C 1 ATOM 5515 O O . GLY B 1 146 ? 9.569 15.160 24.986 1.00 14.87 ? 146 GLY B O 1 ATOM 5516 N N . ASN B 1 147 ? 11.453 15.075 23.724 1.00 14.24 ? 147 ASN B N 1 ATOM 5517 C CA . ASN B 1 147 ? 11.664 13.633 23.825 1.00 14.81 ? 147 ASN B CA 1 ATOM 5518 C C . ASN B 1 147 ? 12.667 13.292 24.935 1.00 16.25 ? 147 ASN B C 1 ATOM 5519 O O . ASN B 1 147 ? 12.924 12.113 25.206 1.00 15.41 ? 147 ASN B O 1 ATOM 5520 C CB . ASN B 1 147 ? 12.142 13.059 22.480 1.00 13.87 ? 147 ASN B CB 1 ATOM 5521 C CG . ASN B 1 147 ? 11.049 13.026 21.430 1.00 11.27 ? 147 ASN B CG 1 ATOM 5522 O OD1 . ASN B 1 147 ? 9.864 13.029 21.753 1.00 10.84 ? 147 ASN B OD1 1 ATOM 5523 N ND2 . ASN B 1 147 ? 11.444 12.971 20.163 1.00 11.43 ? 147 ASN B ND2 1 ATOM 5524 N N . GLY B 1 148 ? 13.253 14.322 25.550 1.00 15.24 ? 148 GLY B N 1 ATOM 5525 C CA . GLY B 1 148 ? 14.194 14.095 26.637 1.00 14.35 ? 148 GLY B CA 1 ATOM 5526 C C . GLY B 1 148 ? 15.601 14.638 26.496 1.00 14.85 ? 148 GLY B C 1 ATOM 5527 O O . GLY B 1 148 ? 16.388 14.520 27.435 1.00 15.75 ? 148 GLY B O 1 ATOM 5528 N N . VAL B 1 149 ? 15.931 15.235 25.350 1.00 14.48 ? 149 VAL B N 1 ATOM 5529 C CA . VAL B 1 149 ? 17.273 15.797 25.141 1.00 14.92 ? 149 VAL B CA 1 ATOM 5530 C C . VAL B 1 149 ? 17.297 17.171 25.827 1.00 14.48 ? 149 VAL B C 1 ATOM 5531 O O . VAL B 1 149 ? 17.261 18.225 25.183 1.00 13.20 ? 149 VAL B O 1 ATOM 5532 C CB . VAL B 1 149 ? 17.641 15.902 23.638 1.00 13.85 ? 149 VAL B CB 1 ATOM 5533 C CG1 . VAL B 1 149 ? 19.119 16.173 23.483 1.00 14.63 ? 149 VAL B CG1 1 ATOM 5534 C CG2 . VAL B 1 149 ? 17.278 14.634 22.895 1.00 15.96 ? 149 VAL B CG2 1 ATOM 5535 N N . VAL B 1 150 ? 17.362 17.115 27.155 1.00 15.13 ? 150 VAL B N 1 ATOM 5536 C CA . VAL B 1 150 ? 17.325 18.287 28.017 1.00 14.75 ? 150 VAL B CA 1 ATOM 5537 C C . VAL B 1 150 ? 18.156 18.057 29.287 1.00 14.49 ? 150 VAL B C 1 ATOM 5538 O O . VAL B 1 150 ? 18.370 16.922 29.695 1.00 13.39 ? 150 VAL B O 1 ATOM 5539 C CB . VAL B 1 150 ? 15.820 18.620 28.384 1.00 17.02 ? 150 VAL B CB 1 ATOM 5540 C CG1 . VAL B 1 150 ? 15.147 17.447 29.095 1.00 18.33 ? 150 VAL B CG1 1 ATOM 5541 C CG2 . VAL B 1 150 ? 15.709 19.870 29.226 1.00 19.19 ? 150 VAL B CG2 1 ATOM 5542 N N . GLY B 1 151 ? 18.617 19.151 29.891 1.00 13.92 ? 151 GLY B N 1 ATOM 5543 C CA . GLY B 1 151 ? 19.380 19.077 31.120 1.00 12.81 ? 151 GLY B CA 1 ATOM 5544 C C . GLY B 1 151 ? 19.595 20.447 31.715 1.00 11.79 ? 151 GLY B C 1 ATOM 5545 O O . GLY B 1 151 ? 19.176 21.439 31.133 1.00 11.54 ? 151 GLY B O 1 ATOM 5546 N N . THR B 1 152 ? 20.304 20.503 32.843 1.00 11.75 ? 152 THR B N 1 ATOM 5547 C CA . THR B 1 152 ? 20.548 21.761 33.548 1.00 11.74 ? 152 THR B CA 1 ATOM 5548 C C . THR B 1 152 ? 22.002 22.221 33.605 1.00 12.52 ? 152 THR B C 1 ATOM 5549 O O . THR B 1 152 ? 22.928 21.429 33.416 1.00 12.91 ? 152 THR B O 1 ATOM 5550 C CB . THR B 1 152 ? 20.027 21.691 34.998 1.00 11.10 ? 152 THR B CB 1 ATOM 5551 O OG1 . THR B 1 152 ? 20.794 20.732 35.740 1.00 10.85 ? 152 THR B OG1 1 ATOM 5552 C CG2 . THR B 1 152 ? 18.547 21.296 35.041 1.00 8.64 ? 152 THR B CG2 1 ATOM 5553 N N . ILE B 1 153 ? 22.183 23.521 33.853 1.00 12.84 ? 153 ILE B N 1 ATOM 5554 C CA . ILE B 1 153 ? 23.505 24.140 33.976 1.00 12.20 ? 153 ILE B CA 1 ATOM 5555 C C . ILE B 1 153 ? 23.534 24.989 35.254 1.00 11.82 ? 153 ILE B C 1 ATOM 5556 O O . ILE B 1 153 ? 22.673 25.848 35.469 1.00 10.64 ? 153 ILE B O 1 ATOM 5557 C CB . ILE B 1 153 ? 23.871 25.065 32.752 1.00 12.37 ? 153 ILE B CB 1 ATOM 5558 C CG1 . ILE B 1 153 ? 23.859 24.290 31.428 1.00 13.31 ? 153 ILE B CG1 1 ATOM 5559 C CG2 . ILE B 1 153 ? 25.263 25.667 32.935 1.00 12.23 ? 153 ILE B CG2 1 ATOM 5560 C CD1 . ILE B 1 153 ? 23.896 25.165 30.180 1.00 14.37 ? 153 ILE B CD1 1 ATOM 5561 N N . GLN B 1 154 ? 24.524 24.727 36.098 1.00 12.51 ? 154 GLN B N 1 ATOM 5562 C CA . GLN B 1 154 ? 24.716 25.477 37.333 1.00 13.51 ? 154 GLN B CA 1 ATOM 5563 C C . GLN B 1 154 ? 26.144 26.007 37.334 1.00 12.56 ? 154 GLN B C 1 ATOM 5564 O O . GLN B 1 154 ? 27.097 25.251 37.526 1.00 13.77 ? 154 GLN B O 1 ATOM 5565 C CB . GLN B 1 154 ? 24.459 24.604 38.575 1.00 13.79 ? 154 GLN B CB 1 ATOM 5566 C CG . GLN B 1 154 ? 24.714 25.333 39.913 1.00 13.17 ? 154 GLN B CG 1 ATOM 5567 C CD . GLN B 1 154 ? 24.377 24.517 41.149 1.00 15.66 ? 154 GLN B CD 1 ATOM 5568 O OE1 . GLN B 1 154 ? 23.569 23.588 41.107 1.00 17.73 ? 154 GLN B OE1 1 ATOM 5569 N NE2 . GLN B 1 154 ? 24.968 24.899 42.276 1.00 16.52 ? 154 GLN B NE2 1 ATOM 5570 N N . ILE B 1 155 ? 26.290 27.291 37.027 1.00 13.38 ? 155 ILE B N 1 ATOM 5571 C CA . ILE B 1 155 ? 27.601 27.925 37.041 1.00 13.13 ? 155 ILE B CA 1 ATOM 5572 C C . ILE B 1 155 ? 27.640 28.685 38.363 1.00 14.88 ? 155 ILE B C 1 ATOM 5573 O O . ILE B 1 155 ? 26.939 29.688 38.540 1.00 14.84 ? 155 ILE B O 1 ATOM 5574 C CB . ILE B 1 155 ? 27.830 28.887 35.840 1.00 14.17 ? 155 ILE B CB 1 ATOM 5575 C CG1 . ILE B 1 155 ? 27.672 28.160 34.493 1.00 11.13 ? 155 ILE B CG1 1 ATOM 5576 C CG2 . ILE B 1 155 ? 29.203 29.547 35.944 1.00 13.01 ? 155 ILE B CG2 1 ATOM 5577 C CD1 . ILE B 1 155 ? 28.640 27.009 34.227 1.00 9.67 ? 155 ILE B CD1 1 ATOM 5578 N N . ASN B 1 156 ? 28.418 28.158 39.303 1.00 14.51 ? 156 ASN B N 1 ATOM 5579 C CA . ASN B 1 156 ? 28.548 28.754 40.626 1.00 14.68 ? 156 ASN B CA 1 ATOM 5580 C C . ASN B 1 156 ? 29.260 30.092 40.601 1.00 14.82 ? 156 ASN B C 1 ATOM 5581 O O . ASN B 1 156 ? 30.184 30.321 39.815 1.00 15.04 ? 156 ASN B O 1 ATOM 5582 C CB . ASN B 1 156 ? 29.214 27.788 41.609 1.00 15.21 ? 156 ASN B CB 1 ATOM 5583 C CG . ASN B 1 156 ? 28.297 26.642 42.015 1.00 14.91 ? 156 ASN B CG 1 ATOM 5584 O OD1 . ASN B 1 156 ? 27.145 26.855 42.412 1.00 18.16 ? 156 ASN B OD1 1 ATOM 5585 N ND2 . ASN B 1 156 ? 28.807 25.420 41.925 1.00 13.58 ? 156 ASN B ND2 1 ATOM 5586 N N . GLY B 1 157 ? 28.750 30.992 41.426 1.00 14.30 ? 157 GLY B N 1 ATOM 5587 C CA . GLY B 1 157 ? 29.286 32.329 41.524 1.00 13.61 ? 157 GLY B CA 1 ATOM 5588 C C . GLY B 1 157 ? 28.694 32.987 42.747 1.00 13.80 ? 157 GLY B C 1 ATOM 5589 O O . GLY B 1 157 ? 28.097 32.298 43.581 1.00 14.82 ? 157 GLY B O 1 ATOM 5590 N N . PRO B 1 158 ? 28.880 34.306 42.919 1.00 14.60 ? 158 PRO B N 1 ATOM 5591 C CA . PRO B 1 158 ? 28.329 35.000 44.083 1.00 13.94 ? 158 PRO B CA 1 ATOM 5592 C C . PRO B 1 158 ? 26.803 35.178 44.001 1.00 13.58 ? 158 PRO B C 1 ATOM 5593 O O . PRO B 1 158 ? 26.187 34.868 42.973 1.00 13.38 ? 158 PRO B O 1 ATOM 5594 C CB . PRO B 1 158 ? 29.087 36.324 44.072 1.00 15.14 ? 158 PRO B CB 1 ATOM 5595 C CG . PRO B 1 158 ? 29.322 36.559 42.635 1.00 14.74 ? 158 PRO B CG 1 ATOM 5596 C CD . PRO B 1 158 ? 29.704 35.220 42.109 1.00 13.17 ? 158 PRO B CD 1 ATOM 5597 N N . ALA B 1 159 ? 26.202 35.612 45.103 1.00 13.03 ? 159 ALA B N 1 ATOM 5598 C CA . ALA B 1 159 ? 24.759 35.814 45.165 1.00 14.40 ? 159 ALA B CA 1 ATOM 5599 C C . ALA B 1 159 ? 24.413 37.130 45.856 1.00 14.12 ? 159 ALA B C 1 ATOM 5600 O O . ALA B 1 159 ? 25.234 37.685 46.587 1.00 13.90 ? 159 ALA B O 1 ATOM 5601 C CB . ALA B 1 159 ? 24.099 34.650 45.867 1.00 14.05 ? 159 ALA B CB 1 ATOM 5602 N N . SER B 1 160 ? 23.202 37.624 45.603 1.00 13.38 ? 160 SER B N 1 ATOM 5603 C CA . SER B 1 160 ? 22.717 38.888 46.168 1.00 15.38 ? 160 SER B CA 1 ATOM 5604 C C . SER B 1 160 ? 22.134 38.810 47.581 1.00 15.49 ? 160 SER B C 1 ATOM 5605 O O . SER B 1 160 ? 21.623 39.807 48.103 1.00 15.25 ? 160 SER B O 1 ATOM 5606 C CB . SER B 1 160 ? 21.687 39.510 45.232 1.00 16.13 ? 160 SER B CB 1 ATOM 5607 O OG . SER B 1 160 ? 20.597 38.633 45.035 1.00 16.33 ? 160 SER B OG 1 ATOM 5608 N N . LEU B 1 161 ? 22.207 37.629 48.188 1.00 15.91 ? 161 LEU B N 1 ATOM 5609 C CA . LEU B 1 161 ? 21.698 37.423 49.539 1.00 17.52 ? 161 LEU B CA 1 ATOM 5610 C C . LEU B 1 161 ? 22.427 36.250 50.184 1.00 17.90 ? 161 LEU B C 1 ATOM 5611 O O . LEU B 1 161 ? 22.864 35.334 49.475 1.00 16.39 ? 161 LEU B O 1 ATOM 5612 C CB . LEU B 1 161 ? 20.193 37.118 49.491 1.00 19.08 ? 161 LEU B CB 1 ATOM 5613 C CG . LEU B 1 161 ? 19.241 37.464 50.634 1.00 22.67 ? 161 LEU B CG 1 ATOM 5614 C CD1 . LEU B 1 161 ? 19.185 38.970 50.866 1.00 20.79 ? 161 LEU B CD1 1 ATOM 5615 C CD2 . LEU B 1 161 ? 17.867 36.919 50.303 1.00 22.99 ? 161 LEU B CD2 1 ATOM 5616 N N . PRO B 1 162 ? 22.687 36.320 51.515 1.00 18.72 ? 162 PRO B N 1 ATOM 5617 C CA . PRO B 1 162 ? 23.366 35.194 52.163 1.00 18.06 ? 162 PRO B CA 1 ATOM 5618 C C . PRO B 1 162 ? 22.429 33.984 52.290 1.00 17.64 ? 162 PRO B C 1 ATOM 5619 O O . PRO B 1 162 ? 21.205 34.140 52.329 1.00 18.84 ? 162 PRO B O 1 ATOM 5620 C CB . PRO B 1 162 ? 23.750 35.765 53.537 1.00 18.74 ? 162 PRO B CB 1 ATOM 5621 C CG . PRO B 1 162 ? 22.768 36.881 53.759 1.00 19.10 ? 162 PRO B CG 1 ATOM 5622 C CD . PRO B 1 162 ? 22.724 37.505 52.400 1.00 19.05 ? 162 PRO B CD 1 ATOM 5623 N N . TYR B 1 163 ? 23.009 32.789 52.238 1.00 17.16 ? 163 TYR B N 1 ATOM 5624 C CA . TYR B 1 163 ? 22.268 31.536 52.381 1.00 16.37 ? 163 TYR B CA 1 ATOM 5625 C C . TYR B 1 163 ? 23.225 30.468 52.872 1.00 16.75 ? 163 TYR B C 1 ATOM 5626 O O . TYR B 1 163 ? 24.420 30.529 52.590 1.00 16.60 ? 163 TYR B O 1 ATOM 5627 C CB . TYR B 1 163 ? 21.553 31.105 51.073 1.00 16.10 ? 163 TYR B CB 1 ATOM 5628 C CG . TYR B 1 163 ? 22.440 30.893 49.863 1.00 15.36 ? 163 TYR B CG 1 ATOM 5629 C CD1 . TYR B 1 163 ? 23.051 29.641 49.617 1.00 15.55 ? 163 TYR B CD1 1 ATOM 5630 C CD2 . TYR B 1 163 ? 22.679 31.942 48.955 1.00 15.14 ? 163 TYR B CD2 1 ATOM 5631 C CE1 . TYR B 1 163 ? 23.889 29.441 48.494 1.00 15.88 ? 163 TYR B CE1 1 ATOM 5632 C CE2 . TYR B 1 163 ? 23.513 31.748 47.825 1.00 14.49 ? 163 TYR B CE2 1 ATOM 5633 C CZ . TYR B 1 163 ? 24.113 30.500 47.608 1.00 14.44 ? 163 TYR B CZ 1 ATOM 5634 O OH . TYR B 1 163 ? 24.930 30.316 46.523 1.00 16.19 ? 163 TYR B OH 1 ATOM 5635 N N . ASP B 1 164 ? 22.678 29.444 53.514 1.00 17.17 ? 164 ASP B N 1 ATOM 5636 C CA . ASP B 1 164 ? 23.485 28.368 54.073 1.00 17.47 ? 164 ASP B CA 1 ATOM 5637 C C . ASP B 1 164 ? 23.677 27.163 53.167 1.00 17.75 ? 164 ASP B C 1 ATOM 5638 O O . ASP B 1 164 ? 24.792 26.654 53.036 1.00 18.06 ? 164 ASP B O 1 ATOM 5639 C CB . ASP B 1 164 ? 22.882 27.918 55.409 1.00 17.85 ? 164 ASP B CB 1 ATOM 5640 C CG . ASP B 1 164 ? 22.597 29.083 56.337 1.00 19.50 ? 164 ASP B CG 1 ATOM 5641 O OD1 . ASP B 1 164 ? 23.566 29.727 56.795 1.00 21.81 ? 164 ASP B OD1 1 ATOM 5642 O OD2 . ASP B 1 164 ? 21.406 29.372 56.581 1.00 16.48 ? 164 ASP B OD2 1 ATOM 5643 N N . ILE B 1 165 ? 22.579 26.698 52.568 1.00 17.86 ? 165 ILE B N 1 ATOM 5644 C CA . ILE B 1 165 ? 22.584 25.511 51.710 1.00 17.70 ? 165 ILE B CA 1 ATOM 5645 C C . ILE B 1 165 ? 22.112 25.804 50.281 1.00 17.15 ? 165 ILE B C 1 ATOM 5646 O O . ILE B 1 165 ? 21.166 26.558 50.075 1.00 17.05 ? 165 ILE B O 1 ATOM 5647 C CB . ILE B 1 165 ? 21.674 24.384 52.334 1.00 17.76 ? 165 ILE B CB 1 ATOM 5648 C CG1 . ILE B 1 165 ? 22.143 24.042 53.758 1.00 19.77 ? 165 ILE B CG1 1 ATOM 5649 C CG2 . ILE B 1 165 ? 21.681 23.102 51.469 1.00 17.87 ? 165 ILE B CG2 1 ATOM 5650 C CD1 . ILE B 1 165 ? 21.187 23.189 54.542 1.00 19.70 ? 165 ILE B CD1 1 ATOM 5651 N N . ASP B 1 166 ? 22.790 25.197 49.308 1.00 16.45 ? 166 ASP B N 1 ATOM 5652 C CA . ASP B 1 166 ? 22.431 25.324 47.898 1.00 16.09 ? 166 ASP B CA 1 ATOM 5653 C C . ASP B 1 166 ? 21.851 23.959 47.537 1.00 16.20 ? 166 ASP B C 1 ATOM 5654 O O . ASP B 1 166 ? 22.597 22.989 47.355 1.00 15.09 ? 166 ASP B O 1 ATOM 5655 C CB . ASP B 1 166 ? 23.671 25.645 47.034 1.00 17.78 ? 166 ASP B CB 1 ATOM 5656 C CG . ASP B 1 166 ? 23.317 26.076 45.592 1.00 16.84 ? 166 ASP B CG 1 ATOM 5657 O OD1 . ASP B 1 166 ? 22.163 25.893 45.139 1.00 16.78 ? 166 ASP B OD1 1 ATOM 5658 O OD2 . ASP B 1 166 ? 24.211 26.614 44.907 1.00 18.19 ? 166 ASP B OD2 1 ATOM 5659 N N . LEU B 1 167 ? 20.518 23.888 47.477 1.00 14.87 ? 167 LEU B N 1 ATOM 5660 C CA . LEU B 1 167 ? 19.794 22.654 47.146 1.00 14.65 ? 167 LEU B CA 1 ATOM 5661 C C . LEU B 1 167 ? 19.988 22.225 45.696 1.00 14.05 ? 167 LEU B C 1 ATOM 5662 O O . LEU B 1 167 ? 19.677 21.090 45.322 1.00 15.50 ? 167 LEU B O 1 ATOM 5663 C CB . LEU B 1 167 ? 18.302 22.813 47.435 1.00 15.13 ? 167 LEU B CB 1 ATOM 5664 C CG . LEU B 1 167 ? 17.895 22.977 48.897 1.00 18.67 ? 167 LEU B CG 1 ATOM 5665 C CD1 . LEU B 1 167 ? 16.440 23.377 48.944 1.00 16.27 ? 167 LEU B CD1 1 ATOM 5666 C CD2 . LEU B 1 167 ? 18.140 21.693 49.694 1.00 20.74 ? 167 LEU B CD2 1 ATOM 5667 N N . GLY B 1 168 ? 20.498 23.151 44.892 1.00 12.81 ? 168 GLY B N 1 ATOM 5668 C CA . GLY B 1 168 ? 20.765 22.871 43.498 1.00 13.47 ? 168 GLY B CA 1 ATOM 5669 C C . GLY B 1 168 ? 19.581 23.089 42.586 1.00 12.42 ? 168 GLY B C 1 ATOM 5670 O O . GLY B 1 168 ? 18.633 23.808 42.927 1.00 11.38 ? 168 GLY B O 1 ATOM 5671 N N . VAL B 1 169 ? 19.630 22.419 41.440 1.00 11.31 ? 169 VAL B N 1 ATOM 5672 C CA . VAL B 1 169 ? 18.597 22.533 40.418 1.00 11.29 ? 169 VAL B CA 1 ATOM 5673 C C . VAL B 1 169 ? 17.274 21.854 40.732 1.00 12.46 ? 169 VAL B C 1 ATOM 5674 O O . VAL B 1 169 ? 17.228 20.795 41.365 1.00 13.25 ? 169 VAL B O 1 ATOM 5675 C CB . VAL B 1 169 ? 19.131 22.110 39.027 1.00 11.05 ? 169 VAL B CB 1 ATOM 5676 C CG1 . VAL B 1 169 ? 20.337 22.979 38.668 1.00 8.43 ? 169 VAL B CG1 1 ATOM 5677 C CG2 . VAL B 1 169 ? 19.495 20.612 38.984 1.00 10.77 ? 169 VAL B CG2 1 ATOM 5678 N N . PHE B 1 170 ? 16.201 22.487 40.268 1.00 13.11 ? 170 PHE B N 1 ATOM 5679 C CA . PHE B 1 170 ? 14.851 22.000 40.478 1.00 13.11 ? 170 PHE B CA 1 ATOM 5680 C C . PHE B 1 170 ? 14.069 22.224 39.177 1.00 13.84 ? 170 PHE B C 1 ATOM 5681 O O . PHE B 1 170 ? 13.257 23.163 39.087 1.00 12.79 ? 170 PHE B O 1 ATOM 5682 C CB . PHE B 1 170 ? 14.224 22.779 41.648 1.00 13.17 ? 170 PHE B CB 1 ATOM 5683 C CG . PHE B 1 170 ? 13.181 22.016 42.418 1.00 13.11 ? 170 PHE B CG 1 ATOM 5684 C CD1 . PHE B 1 170 ? 13.421 20.698 42.858 1.00 13.44 ? 170 PHE B CD1 1 ATOM 5685 C CD2 . PHE B 1 170 ? 11.960 22.636 42.754 1.00 11.42 ? 170 PHE B CD2 1 ATOM 5686 C CE1 . PHE B 1 170 ? 12.457 20.002 43.629 1.00 14.60 ? 170 PHE B CE1 1 ATOM 5687 C CE2 . PHE B 1 170 ? 10.985 21.957 43.527 1.00 12.58 ? 170 PHE B CE2 1 ATOM 5688 C CZ . PHE B 1 170 ? 11.234 20.634 43.969 1.00 11.96 ? 170 PHE B CZ 1 ATOM 5689 N N . PRO B 1 171 ? 14.343 21.400 38.131 1.00 12.61 ? 171 PRO B N 1 ATOM 5690 C CA . PRO B 1 171 ? 13.629 21.564 36.860 1.00 11.92 ? 171 PRO B CA 1 ATOM 5691 C C . PRO B 1 171 ? 12.194 21.068 36.892 1.00 12.04 ? 171 PRO B C 1 ATOM 5692 O O . PRO B 1 171 ? 11.906 19.984 37.403 1.00 12.26 ? 171 PRO B O 1 ATOM 5693 C CB . PRO B 1 171 ? 14.490 20.774 35.878 1.00 12.58 ? 171 PRO B CB 1 ATOM 5694 C CG . PRO B 1 171 ? 15.038 19.663 36.719 1.00 11.40 ? 171 PRO B CG 1 ATOM 5695 C CD . PRO B 1 171 ? 15.394 20.364 38.000 1.00 11.48 ? 171 PRO B CD 1 ATOM 5696 N N . ILE B 1 172 ? 11.290 21.928 36.436 1.00 10.61 ? 172 ILE B N 1 ATOM 5697 C CA . ILE B 1 172 ? 9.874 21.598 36.379 1.00 10.52 ? 172 ILE B CA 1 ATOM 5698 C C . ILE B 1 172 ? 9.527 21.596 34.894 1.00 10.26 ? 172 ILE B C 1 ATOM 5699 O O . ILE B 1 172 ? 9.829 22.545 34.178 1.00 11.21 ? 172 ILE B O 1 ATOM 5700 C CB . ILE B 1 172 ? 8.999 22.606 37.178 1.00 9.76 ? 172 ILE B CB 1 ATOM 5701 C CG1 . ILE B 1 172 ? 9.547 22.790 38.601 1.00 9.39 ? 172 ILE B CG1 1 ATOM 5702 C CG2 . ILE B 1 172 ? 7.569 22.081 37.278 1.00 9.24 ? 172 ILE B CG2 1 ATOM 5703 C CD1 . ILE B 1 172 ? 8.851 23.850 39.410 1.00 12.85 ? 172 ILE B CD1 1 ATOM 5704 N N . THR B 1 173 ? 8.924 20.508 34.432 1.00 11.27 ? 173 THR B N 1 ATOM 5705 C CA . THR B 1 173 ? 8.578 20.377 33.024 1.00 11.50 ? 173 THR B CA 1 ATOM 5706 C C . THR B 1 173 ? 7.259 19.684 32.770 1.00 12.86 ? 173 THR B C 1 ATOM 5707 O O . THR B 1 173 ? 6.819 18.852 33.567 1.00 11.97 ? 173 THR B O 1 ATOM 5708 C CB . THR B 1 173 ? 9.690 19.593 32.240 1.00 11.69 ? 173 THR B CB 1 ATOM 5709 O OG1 . THR B 1 173 ? 9.365 19.539 30.843 1.00 9.52 ? 173 THR B OG1 1 ATOM 5710 C CG2 . THR B 1 173 ? 9.894 18.171 32.784 1.00 10.09 ? 173 THR B CG2 1 ATOM 5711 N N . ASP B 1 174 ? 6.652 20.009 31.628 1.00 12.92 ? 174 ASP B N 1 ATOM 5712 C CA . ASP B 1 174 ? 5.431 19.338 31.216 1.00 12.64 ? 174 ASP B CA 1 ATOM 5713 C C . ASP B 1 174 ? 5.875 17.977 30.692 1.00 12.49 ? 174 ASP B C 1 ATOM 5714 O O . ASP B 1 174 ? 7.030 17.812 30.283 1.00 12.23 ? 174 ASP B O 1 ATOM 5715 C CB . ASP B 1 174 ? 4.641 20.119 30.157 1.00 10.30 ? 174 ASP B CB 1 ATOM 5716 C CG . ASP B 1 174 ? 5.478 20.634 28.997 1.00 11.51 ? 174 ASP B CG 1 ATOM 5717 O OD1 . ASP B 1 174 ? 6.626 20.194 28.771 1.00 10.18 ? 174 ASP B OD1 1 ATOM 5718 O OD2 . ASP B 1 174 ? 4.946 21.507 28.277 1.00 10.70 ? 174 ASP B OD2 1 ATOM 5719 N N . TYR B 1 175 ? 4.972 17.011 30.739 1.00 13.76 ? 175 TYR B N 1 ATOM 5720 C CA . TYR B 1 175 ? 5.282 15.659 30.321 1.00 12.89 ? 175 TYR B CA 1 ATOM 5721 C C . TYR B 1 175 ? 4.139 15.129 29.481 1.00 12.42 ? 175 TYR B C 1 ATOM 5722 O O . TYR B 1 175 ? 2.985 15.152 29.905 1.00 12.46 ? 175 TYR B O 1 ATOM 5723 C CB . TYR B 1 175 ? 5.482 14.813 31.580 1.00 15.06 ? 175 TYR B CB 1 ATOM 5724 C CG . TYR B 1 175 ? 5.989 13.405 31.388 1.00 16.77 ? 175 TYR B CG 1 ATOM 5725 C CD1 . TYR B 1 175 ? 7.200 13.147 30.703 1.00 15.86 ? 175 TYR B CD1 1 ATOM 5726 C CD2 . TYR B 1 175 ? 5.283 12.317 31.936 1.00 16.31 ? 175 TYR B CD2 1 ATOM 5727 C CE1 . TYR B 1 175 ? 7.698 11.824 30.575 1.00 18.26 ? 175 TYR B CE1 1 ATOM 5728 C CE2 . TYR B 1 175 ? 5.767 10.995 31.815 1.00 17.39 ? 175 TYR B CE2 1 ATOM 5729 C CZ . TYR B 1 175 ? 6.971 10.758 31.136 1.00 18.39 ? 175 TYR B CZ 1 ATOM 5730 O OH . TYR B 1 175 ? 7.435 9.471 31.016 1.00 17.65 ? 175 TYR B OH 1 ATOM 5731 N N . TYR B 1 176 ? 4.475 14.718 28.263 1.00 11.50 ? 176 TYR B N 1 ATOM 5732 C CA . TYR B 1 176 ? 3.510 14.167 27.316 1.00 12.68 ? 176 TYR B CA 1 ATOM 5733 C C . TYR B 1 176 ? 3.906 12.737 27.001 1.00 13.26 ? 176 TYR B C 1 ATOM 5734 O O . TYR B 1 176 ? 5.091 12.450 26.847 1.00 12.96 ? 176 TYR B O 1 ATOM 5735 C CB . TYR B 1 176 ? 3.512 14.961 26.008 1.00 10.73 ? 176 TYR B CB 1 ATOM 5736 C CG . TYR B 1 176 ? 3.227 16.436 26.159 1.00 11.32 ? 176 TYR B CG 1 ATOM 5737 C CD1 . TYR B 1 176 ? 4.255 17.331 26.511 1.00 10.72 ? 176 TYR B CD1 1 ATOM 5738 C CD2 . TYR B 1 176 ? 1.920 16.946 25.994 1.00 11.47 ? 176 TYR B CD2 1 ATOM 5739 C CE1 . TYR B 1 176 ? 3.991 18.699 26.713 1.00 11.43 ? 176 TYR B CE1 1 ATOM 5740 C CE2 . TYR B 1 176 ? 1.646 18.327 26.187 1.00 10.61 ? 176 TYR B CE2 1 ATOM 5741 C CZ . TYR B 1 176 ? 2.691 19.192 26.559 1.00 11.54 ? 176 TYR B CZ 1 ATOM 5742 O OH . TYR B 1 176 ? 2.442 20.511 26.851 1.00 12.84 ? 176 TYR B OH 1 ATOM 5743 N N . TYR B 1 177 ? 2.917 11.852 26.884 1.00 14.10 ? 177 TYR B N 1 ATOM 5744 C CA . TYR B 1 177 ? 3.171 10.445 26.561 1.00 15.40 ? 177 TYR B CA 1 ATOM 5745 C C . TYR B 1 177 ? 3.493 10.292 25.077 1.00 16.75 ? 177 TYR B C 1 ATOM 5746 O O . TYR B 1 177 ? 4.287 9.430 24.688 1.00 15.89 ? 177 TYR B O 1 ATOM 5747 C CB . TYR B 1 177 ? 1.992 9.550 26.978 1.00 16.14 ? 177 TYR B CB 1 ATOM 5748 C CG . TYR B 1 177 ? 1.650 9.619 28.463 1.00 17.87 ? 177 TYR B CG 1 ATOM 5749 C CD1 . TYR B 1 177 ? 2.651 9.858 29.442 1.00 18.16 ? 177 TYR B CD1 1 ATOM 5750 C CD2 . TYR B 1 177 ? 0.315 9.495 28.900 1.00 17.27 ? 177 TYR B CD2 1 ATOM 5751 C CE1 . TYR B 1 177 ? 2.324 9.982 30.822 1.00 18.05 ? 177 TYR B CE1 1 ATOM 5752 C CE2 . TYR B 1 177 ? -0.024 9.612 30.284 1.00 17.02 ? 177 TYR B CE2 1 ATOM 5753 C CZ . TYR B 1 177 ? 0.987 9.859 31.229 1.00 17.42 ? 177 TYR B CZ 1 ATOM 5754 O OH . TYR B 1 177 ? 0.669 10.004 32.562 1.00 19.00 ? 177 TYR B OH 1 ATOM 5755 N N . ARG B 1 178 ? 2.933 11.195 24.272 1.00 16.65 ? 178 ARG B N 1 ATOM 5756 C CA . ARG B 1 178 ? 3.162 11.217 22.833 1.00 18.67 ? 178 ARG B CA 1 ATOM 5757 C C . ARG B 1 178 ? 4.515 11.877 22.562 1.00 18.31 ? 178 ARG B C 1 ATOM 5758 O O . ARG B 1 178 ? 4.929 12.787 23.291 1.00 19.33 ? 178 ARG B O 1 ATOM 5759 C CB . ARG B 1 178 ? 2.046 11.990 22.121 1.00 20.93 ? 178 ARG B CB 1 ATOM 5760 C CG . ARG B 1 178 ? 0.664 11.354 22.208 1.00 25.15 ? 178 ARG B CG 1 ATOM 5761 C CD . ARG B 1 178 ? 0.482 10.254 21.179 1.00 31.36 ? 178 ARG B CD 1 ATOM 5762 N NE . ARG B 1 178 ? 0.356 10.791 19.822 1.00 35.00 ? 178 ARG B NE 1 ATOM 5763 C CZ . ARG B 1 178 ? 0.414 10.064 18.706 1.00 35.57 ? 178 ARG B CZ 1 ATOM 5764 N NH1 . ARG B 1 178 ? 0.605 8.750 18.758 1.00 36.01 ? 178 ARG B NH1 1 ATOM 5765 N NH2 . ARG B 1 178 ? 0.264 10.657 17.529 1.00 35.96 ? 178 ARG B NH2 1 ATOM 5766 N N . ALA B 1 179 ? 5.203 11.387 21.531 1.00 16.60 ? 179 ALA B N 1 ATOM 5767 C CA . ALA B 1 179 ? 6.514 11.894 21.128 1.00 15.25 ? 179 ALA B CA 1 ATOM 5768 C C . ALA B 1 179 ? 6.418 13.299 20.531 1.00 14.08 ? 179 ALA B C 1 ATOM 5769 O O . ALA B 1 179 ? 5.364 13.696 20.036 1.00 12.40 ? 179 ALA B O 1 ATOM 5770 C CB . ALA B 1 179 ? 7.160 10.940 20.145 1.00 15.30 ? 179 ALA B CB 1 ATOM 5771 N N . ALA B 1 180 ? 7.532 14.028 20.577 1.00 13.56 ? 180 ALA B N 1 ATOM 5772 C CA . ALA B 1 180 ? 7.623 15.404 20.087 1.00 14.80 ? 180 ALA B CA 1 ATOM 5773 C C . ALA B 1 180 ? 7.213 15.634 18.640 1.00 15.61 ? 180 ALA B C 1 ATOM 5774 O O . ALA B 1 180 ? 6.496 16.593 18.359 1.00 16.28 ? 180 ALA B O 1 ATOM 5775 C CB . ALA B 1 180 ? 9.006 15.940 20.316 1.00 13.15 ? 180 ALA B CB 1 ATOM 5776 N N . ASP B 1 181 ? 7.634 14.738 17.743 1.00 14.11 ? 181 ASP B N 1 ATOM 5777 C CA . ASP B 1 181 ? 7.309 14.852 16.320 1.00 16.40 ? 181 ASP B CA 1 ATOM 5778 C C . ASP B 1 181 ? 5.826 14.658 16.026 1.00 15.89 ? 181 ASP B C 1 ATOM 5779 O O . ASP B 1 181 ? 5.271 15.339 15.160 1.00 14.73 ? 181 ASP B O 1 ATOM 5780 C CB . ASP B 1 181 ? 8.154 13.893 15.484 1.00 16.98 ? 181 ASP B CB 1 ATOM 5781 C CG . ASP B 1 181 ? 9.605 14.323 15.402 1.00 19.17 ? 181 ASP B CG 1 ATOM 5782 O OD1 . ASP B 1 181 ? 9.897 15.294 14.673 1.00 22.38 ? 181 ASP B OD1 1 ATOM 5783 O OD2 . ASP B 1 181 ? 10.449 13.699 16.073 1.00 18.79 ? 181 ASP B OD2 1 ATOM 5784 N N . ASP B 1 182 ? 5.184 13.781 16.801 1.00 16.17 ? 182 ASP B N 1 ATOM 5785 C CA . ASP B 1 182 ? 3.751 13.506 16.661 1.00 17.08 ? 182 ASP B CA 1 ATOM 5786 C C . ASP B 1 182 ? 2.947 14.698 17.169 1.00 16.71 ? 182 ASP B C 1 ATOM 5787 O O . ASP B 1 182 ? 1.890 15.027 16.624 1.00 15.17 ? 182 ASP B O 1 ATOM 5788 C CB . ASP B 1 182 ? 3.363 12.246 17.436 1.00 18.79 ? 182 ASP B CB 1 ATOM 5789 C CG . ASP B 1 182 ? 3.900 10.971 16.799 1.00 23.13 ? 182 ASP B CG 1 ATOM 5790 O OD1 . ASP B 1 182 ? 4.031 10.918 15.552 1.00 22.06 ? 182 ASP B OD1 1 ATOM 5791 O OD2 . ASP B 1 182 ? 4.189 10.015 17.551 1.00 25.24 ? 182 ASP B OD2 1 ATOM 5792 N N . LEU B 1 183 ? 3.494 15.365 18.186 1.00 15.91 ? 183 LEU B N 1 ATOM 5793 C CA . LEU B 1 183 ? 2.872 16.543 18.779 1.00 16.75 ? 183 LEU B CA 1 ATOM 5794 C C . LEU B 1 183 ? 3.064 17.791 17.918 1.00 16.64 ? 183 LEU B C 1 ATOM 5795 O O . LEU B 1 183 ? 2.216 18.677 17.940 1.00 17.05 ? 183 LEU B O 1 ATOM 5796 C CB . LEU B 1 183 ? 3.391 16.776 20.193 1.00 16.66 ? 183 LEU B CB 1 ATOM 5797 C CG . LEU B 1 183 ? 2.914 15.833 21.296 1.00 15.95 ? 183 LEU B CG 1 ATOM 5798 C CD1 . LEU B 1 183 ? 3.835 15.969 22.473 1.00 15.28 ? 183 LEU B CD1 1 ATOM 5799 C CD2 . LEU B 1 183 ? 1.472 16.102 21.694 1.00 15.67 ? 183 LEU B CD2 1 ATOM 5800 N N . VAL B 1 184 ? 4.163 17.850 17.153 1.00 15.78 ? 184 VAL B N 1 ATOM 5801 C CA . VAL B 1 184 ? 4.428 18.980 16.243 1.00 15.70 ? 184 VAL B CA 1 ATOM 5802 C C . VAL B 1 184 ? 3.393 18.880 15.117 1.00 16.10 ? 184 VAL B C 1 ATOM 5803 O O . VAL B 1 184 ? 2.720 19.864 14.805 1.00 14.61 ? 184 VAL B O 1 ATOM 5804 C CB . VAL B 1 184 ? 5.883 18.948 15.656 1.00 15.10 ? 184 VAL B CB 1 ATOM 5805 C CG1 . VAL B 1 184 ? 6.034 19.898 14.454 1.00 16.17 ? 184 VAL B CG1 1 ATOM 5806 C CG2 . VAL B 1 184 ? 6.869 19.355 16.716 1.00 13.98 ? 184 VAL B CG2 1 ATOM 5807 N N . HIS B 1 185 ? 3.228 17.659 14.596 1.00 17.15 ? 185 HIS B N 1 ATOM 5808 C CA . HIS B 1 185 ? 2.275 17.333 13.529 1.00 17.72 ? 185 HIS B CA 1 ATOM 5809 C C . HIS B 1 185 ? 0.839 17.647 13.973 1.00 17.09 ? 185 HIS B C 1 ATOM 5810 O O . HIS B 1 185 ? 0.064 18.228 13.207 1.00 17.61 ? 185 HIS B O 1 ATOM 5811 C CB . HIS B 1 185 ? 2.408 15.846 13.150 1.00 21.32 ? 185 HIS B CB 1 ATOM 5812 C CG . HIS B 1 185 ? 1.468 15.402 12.069 1.00 25.06 ? 185 HIS B CG 1 ATOM 5813 N ND1 . HIS B 1 185 ? 1.517 15.906 10.787 1.00 28.05 ? 185 HIS B ND1 1 ATOM 5814 C CD2 . HIS B 1 185 ? 0.433 14.527 12.090 1.00 28.04 ? 185 HIS B CD2 1 ATOM 5815 C CE1 . HIS B 1 185 ? 0.550 15.364 10.066 1.00 29.92 ? 185 HIS B CE1 1 ATOM 5816 N NE2 . HIS B 1 185 ? -0.122 14.524 10.833 1.00 30.00 ? 185 HIS B NE2 1 ATOM 5817 N N . PHE B 1 186 ? 0.520 17.290 15.221 1.00 15.96 ? 186 PHE B N 1 ATOM 5818 C CA . PHE B 1 186 ? -0.802 17.515 15.814 1.00 15.82 ? 186 PHE B CA 1 ATOM 5819 C C . PHE B 1 186 ? -1.085 19.010 15.966 1.00 14.54 ? 186 PHE B C 1 ATOM 5820 O O . PHE B 1 186 ? -2.127 19.486 15.522 1.00 14.30 ? 186 PHE B O 1 ATOM 5821 C CB . PHE B 1 186 ? -0.908 16.805 17.182 1.00 14.41 ? 186 PHE B CB 1 ATOM 5822 C CG . PHE B 1 186 ? -2.260 16.943 17.858 1.00 17.35 ? 186 PHE B CG 1 ATOM 5823 C CD1 . PHE B 1 186 ? -3.377 16.221 17.387 1.00 17.56 ? 186 PHE B CD1 1 ATOM 5824 C CD2 . PHE B 1 186 ? -2.421 17.797 18.973 1.00 18.36 ? 186 PHE B CD2 1 ATOM 5825 C CE1 . PHE B 1 186 ? -4.649 16.343 18.017 1.00 18.76 ? 186 PHE B CE1 1 ATOM 5826 C CE2 . PHE B 1 186 ? -3.684 17.934 19.618 1.00 20.36 ? 186 PHE B CE2 1 ATOM 5827 C CZ . PHE B 1 186 ? -4.804 17.202 19.136 1.00 19.03 ? 186 PHE B CZ 1 ATOM 5828 N N . THR B 1 187 ? -0.129 19.742 16.541 1.00 13.52 ? 187 THR B N 1 ATOM 5829 C CA . THR B 1 187 ? -0.277 21.183 16.767 1.00 13.74 ? 187 THR B CA 1 ATOM 5830 C C . THR B 1 187 ? -0.248 22.052 15.519 1.00 15.05 ? 187 THR B C 1 ATOM 5831 O O . THR B 1 187 ? -0.592 23.238 15.568 1.00 14.94 ? 187 THR B O 1 ATOM 5832 C CB . THR B 1 187 ? 0.728 21.715 17.779 1.00 14.19 ? 187 THR B CB 1 ATOM 5833 O OG1 . THR B 1 187 ? 2.062 21.472 17.313 1.00 14.69 ? 187 THR B OG1 1 ATOM 5834 C CG2 . THR B 1 187 ? 0.518 21.046 19.138 1.00 13.47 ? 187 THR B CG2 1 ATOM 5835 N N . GLN B 1 188 ? 0.147 21.450 14.401 1.00 15.51 ? 188 GLN B N 1 ATOM 5836 C CA . GLN B 1 188 ? 0.184 22.144 13.116 1.00 18.31 ? 188 GLN B CA 1 ATOM 5837 C C . GLN B 1 188 ? -1.249 22.360 12.616 1.00 18.79 ? 188 GLN B C 1 ATOM 5838 O O . GLN B 1 188 ? -1.535 23.348 11.937 1.00 19.81 ? 188 GLN B O 1 ATOM 5839 C CB . GLN B 1 188 ? 0.989 21.336 12.096 1.00 17.17 ? 188 GLN B CB 1 ATOM 5840 C CG . GLN B 1 188 ? 2.496 21.599 12.147 1.00 18.25 ? 188 GLN B CG 1 ATOM 5841 C CD . GLN B 1 188 ? 3.293 20.852 11.085 1.00 18.62 ? 188 GLN B CD 1 ATOM 5842 O OE1 . GLN B 1 188 ? 2.753 20.056 10.310 1.00 20.96 ? 188 GLN B OE1 1 ATOM 5843 N NE2 . GLN B 1 188 ? 4.595 21.109 11.049 1.00 18.63 ? 188 GLN B NE2 1 ATOM 5844 N N . ASN B 1 189 ? -2.154 21.465 13.019 1.00 18.88 ? 189 ASN B N 1 ATOM 5845 C CA . ASN B 1 189 ? -3.556 21.544 12.614 1.00 20.46 ? 189 ASN B CA 1 ATOM 5846 C C . ASN B 1 189 ? -4.550 21.607 13.769 1.00 20.61 ? 189 ASN B C 1 ATOM 5847 O O . ASN B 1 189 ? -5.746 21.812 13.545 1.00 21.35 ? 189 ASN B O 1 ATOM 5848 C CB . ASN B 1 189 ? -3.907 20.386 11.667 1.00 21.37 ? 189 ASN B CB 1 ATOM 5849 C CG . ASN B 1 189 ? -3.170 20.474 10.341 1.00 21.78 ? 189 ASN B CG 1 ATOM 5850 O OD1 . ASN B 1 189 ? -3.365 21.413 9.569 1.00 23.07 ? 189 ASN B OD1 1 ATOM 5851 N ND2 . ASN B 1 189 ? -2.289 19.517 10.090 1.00 24.65 ? 189 ASN B ND2 1 ATOM 5852 N N . ASN B 1 190 ? -4.062 21.441 15.001 1.00 19.16 ? 190 ASN B N 1 ATOM 5853 C CA . ASN B 1 190 ? -4.919 21.472 16.193 1.00 18.37 ? 190 ASN B CA 1 ATOM 5854 C C . ASN B 1 190 ? -4.360 22.337 17.315 1.00 18.86 ? 190 ASN B C 1 ATOM 5855 O O . ASN B 1 190 ? -3.163 22.620 17.357 1.00 17.43 ? 190 ASN B O 1 ATOM 5856 C CB . ASN B 1 190 ? -5.142 20.065 16.756 1.00 18.59 ? 190 ASN B CB 1 ATOM 5857 C CG . ASN B 1 190 ? -5.777 19.122 15.761 1.00 20.25 ? 190 ASN B CG 1 ATOM 5858 O OD1 . ASN B 1 190 ? -7.000 19.013 15.684 1.00 22.71 ? 190 ASN B OD1 1 ATOM 5859 N ND2 . ASN B 1 190 ? -4.943 18.449 14.974 1.00 18.56 ? 190 ASN B ND2 1 ATOM 5860 N N . ALA B 1 191 ? -5.241 22.733 18.236 1.00 17.78 ? 191 ALA B N 1 ATOM 5861 C CA . ALA B 1 191 ? -4.868 23.534 19.403 1.00 18.80 ? 191 ALA B CA 1 ATOM 5862 C C . ALA B 1 191 ? -4.020 22.637 20.313 1.00 18.53 ? 191 ALA B C 1 ATOM 5863 O O . ALA B 1 191 ? -4.278 21.430 20.395 1.00 17.87 ? 191 ALA B O 1 ATOM 5864 C CB . ALA B 1 191 ? -6.120 24.004 20.143 1.00 19.25 ? 191 ALA B CB 1 ATOM 5865 N N . PRO B 1 192 ? -2.965 23.194 20.952 1.00 18.47 ? 192 PRO B N 1 ATOM 5866 C CA . PRO B 1 192 ? -2.088 22.422 21.844 1.00 18.68 ? 192 PRO B CA 1 ATOM 5867 C C . PRO B 1 192 ? -2.794 21.705 22.999 1.00 17.25 ? 192 PRO B C 1 ATOM 5868 O O . PRO B 1 192 ? -3.706 22.262 23.613 1.00 18.53 ? 192 PRO B O 1 ATOM 5869 C CB . PRO B 1 192 ? -1.096 23.476 22.349 1.00 18.25 ? 192 PRO B CB 1 ATOM 5870 C CG . PRO B 1 192 ? -1.825 24.765 22.181 1.00 21.24 ? 192 PRO B CG 1 ATOM 5871 C CD . PRO B 1 192 ? -2.470 24.579 20.850 1.00 19.25 ? 192 PRO B CD 1 ATOM 5872 N N . PRO B 1 193 ? -2.423 20.436 23.263 1.00 16.10 ? 193 PRO B N 1 ATOM 5873 C CA . PRO B 1 193 ? -3.072 19.716 24.362 1.00 14.45 ? 193 PRO B CA 1 ATOM 5874 C C . PRO B 1 193 ? -2.504 20.103 25.725 1.00 13.39 ? 193 PRO B C 1 ATOM 5875 O O . PRO B 1 193 ? -1.463 20.766 25.817 1.00 12.28 ? 193 PRO B O 1 ATOM 5876 C CB . PRO B 1 193 ? -2.751 18.258 24.040 1.00 14.77 ? 193 PRO B CB 1 ATOM 5877 C CG . PRO B 1 193 ? -1.374 18.346 23.444 1.00 17.23 ? 193 PRO B CG 1 ATOM 5878 C CD . PRO B 1 193 ? -1.500 19.545 22.525 1.00 15.85 ? 193 PRO B CD 1 ATOM 5879 N N . PHE B 1 194 ? -3.214 19.698 26.774 1.00 11.02 ? 194 PHE B N 1 ATOM 5880 C CA . PHE B 1 194 ? -2.768 19.908 28.141 1.00 11.48 ? 194 PHE B CA 1 ATOM 5881 C C . PHE B 1 194 ? -1.719 18.812 28.341 1.00 13.02 ? 194 PHE B C 1 ATOM 5882 O O . PHE B 1 194 ? -1.751 17.786 27.644 1.00 12.58 ? 194 PHE B O 1 ATOM 5883 C CB . PHE B 1 194 ? -3.921 19.661 29.126 1.00 12.23 ? 194 PHE B CB 1 ATOM 5884 C CG . PHE B 1 194 ? -4.673 20.906 29.561 1.00 10.30 ? 194 PHE B CG 1 ATOM 5885 C CD1 . PHE B 1 194 ? -4.641 22.103 28.808 1.00 11.17 ? 194 PHE B CD1 1 ATOM 5886 C CD2 . PHE B 1 194 ? -5.452 20.868 30.742 1.00 12.85 ? 194 PHE B CD2 1 ATOM 5887 C CE1 . PHE B 1 194 ? -5.380 23.254 29.225 1.00 10.98 ? 194 PHE B CE1 1 ATOM 5888 C CE2 . PHE B 1 194 ? -6.199 22.008 31.176 1.00 13.24 ? 194 PHE B CE2 1 ATOM 5889 C CZ . PHE B 1 194 ? -6.161 23.202 30.413 1.00 13.22 ? 194 PHE B CZ 1 ATOM 5890 N N . SER B 1 195 ? -0.768 19.034 29.243 1.00 12.14 ? 195 SER B N 1 ATOM 5891 C CA . SER B 1 195 ? 0.239 18.011 29.509 1.00 13.27 ? 195 SER B CA 1 ATOM 5892 C C . SER B 1 195 ? -0.377 16.855 30.261 1.00 12.85 ? 195 SER B C 1 ATOM 5893 O O . SER B 1 195 ? -1.367 17.030 30.963 1.00 13.81 ? 195 SER B O 1 ATOM 5894 C CB . SER B 1 195 ? 1.419 18.578 30.283 1.00 12.29 ? 195 SER B CB 1 ATOM 5895 O OG . SER B 1 195 ? 1.021 19.183 31.493 1.00 14.47 ? 195 SER B OG 1 ATOM 5896 N N . ASP B 1 196 ? 0.177 15.665 30.066 1.00 13.61 ? 196 ASP B N 1 ATOM 5897 C CA . ASP B 1 196 ? -0.323 14.474 30.740 1.00 14.14 ? 196 ASP B CA 1 ATOM 5898 C C . ASP B 1 196 ? 0.054 14.507 32.216 1.00 13.82 ? 196 ASP B C 1 ATOM 5899 O O . ASP B 1 196 ? -0.697 14.038 33.072 1.00 15.54 ? 196 ASP B O 1 ATOM 5900 C CB . ASP B 1 196 ? 0.206 13.233 30.045 1.00 12.95 ? 196 ASP B CB 1 ATOM 5901 C CG . ASP B 1 196 ? -0.367 13.064 28.650 1.00 15.51 ? 196 ASP B CG 1 ATOM 5902 O OD1 . ASP B 1 196 ? -1.605 12.978 28.513 1.00 16.01 ? 196 ASP B OD1 1 ATOM 5903 O OD2 . ASP B 1 196 ? 0.420 13.020 27.686 1.00 16.10 ? 196 ASP B OD2 1 ATOM 5904 N N . ASN B 1 197 ? 1.196 15.132 32.494 1.00 13.05 ? 197 ASN B N 1 ATOM 5905 C CA . ASN B 1 197 ? 1.695 15.309 33.848 1.00 13.45 ? 197 ASN B CA 1 ATOM 5906 C C . ASN B 1 197 ? 2.730 16.426 33.844 1.00 13.04 ? 197 ASN B C 1 ATOM 5907 O O . ASN B 1 197 ? 3.044 16.997 32.796 1.00 11.67 ? 197 ASN B O 1 ATOM 5908 C CB . ASN B 1 197 ? 2.316 14.010 34.393 1.00 15.19 ? 197 ASN B CB 1 ATOM 5909 C CG . ASN B 1 197 ? 2.037 13.800 35.882 1.00 15.50 ? 197 ASN B CG 1 ATOM 5910 O OD1 . ASN B 1 197 ? 1.951 14.756 36.658 1.00 15.20 ? 197 ASN B OD1 1 ATOM 5911 N ND2 . ASN B 1 197 ? 1.901 12.541 36.284 1.00 16.29 ? 197 ASN B ND2 1 ATOM 5912 N N . VAL B 1 198 ? 3.161 16.811 35.040 1.00 12.62 ? 198 VAL B N 1 ATOM 5913 C CA . VAL B 1 198 ? 4.182 17.830 35.218 1.00 13.55 ? 198 VAL B CA 1 ATOM 5914 C C . VAL B 1 198 ? 5.202 17.218 36.171 1.00 13.98 ? 198 VAL B C 1 ATOM 5915 O O . VAL B 1 198 ? 4.886 16.920 37.327 1.00 13.31 ? 198 VAL B O 1 ATOM 5916 C CB . VAL B 1 198 ? 3.612 19.157 35.799 1.00 12.71 ? 198 VAL B CB 1 ATOM 5917 C CG1 . VAL B 1 198 ? 4.729 20.093 36.233 1.00 12.21 ? 198 VAL B CG1 1 ATOM 5918 C CG2 . VAL B 1 198 ? 2.708 19.858 34.792 1.00 11.28 ? 198 VAL B CG2 1 ATOM 5919 N N . LEU B 1 199 ? 6.411 17.003 35.657 1.00 14.04 ? 199 LEU B N 1 ATOM 5920 C CA . LEU B 1 199 ? 7.501 16.434 36.438 1.00 14.69 ? 199 LEU B CA 1 ATOM 5921 C C . LEU B 1 199 ? 8.254 17.517 37.165 1.00 15.88 ? 199 LEU B C 1 ATOM 5922 O O . LEU B 1 199 ? 8.508 18.585 36.613 1.00 16.28 ? 199 LEU B O 1 ATOM 5923 C CB . LEU B 1 199 ? 8.489 15.689 35.546 1.00 14.28 ? 199 LEU B CB 1 ATOM 5924 C CG . LEU B 1 199 ? 7.951 14.651 34.575 1.00 16.23 ? 199 LEU B CG 1 ATOM 5925 C CD1 . LEU B 1 199 ? 9.090 14.125 33.758 1.00 15.55 ? 199 LEU B CD1 1 ATOM 5926 C CD2 . LEU B 1 199 ? 7.215 13.534 35.284 1.00 16.71 ? 199 LEU B CD2 1 ATOM 5927 N N . ILE B 1 200 ? 8.525 17.266 38.440 1.00 15.02 ? 200 ILE B N 1 ATOM 5928 C CA . ILE B 1 200 ? 9.280 18.192 39.268 1.00 15.60 ? 200 ILE B CA 1 ATOM 5929 C C . ILE B 1 200 ? 10.507 17.389 39.668 1.00 17.05 ? 200 ILE B C 1 ATOM 5930 O O . ILE B 1 200 ? 10.393 16.328 40.297 1.00 17.55 ? 200 ILE B O 1 ATOM 5931 C CB . ILE B 1 200 ? 8.483 18.669 40.504 1.00 16.07 ? 200 ILE B CB 1 ATOM 5932 C CG1 . ILE B 1 200 ? 7.179 19.348 40.064 1.00 15.09 ? 200 ILE B CG1 1 ATOM 5933 C CG2 . ILE B 1 200 ? 9.298 19.684 41.267 1.00 12.89 ? 200 ILE B CG2 1 ATOM 5934 C CD1 . ILE B 1 200 ? 6.222 19.619 41.171 1.00 14.42 ? 200 ILE B CD1 1 ATOM 5935 N N . ASN B 1 201 ? 11.663 17.867 39.208 1.00 18.99 ? 201 ASN B N 1 ATOM 5936 C CA . ASN B 1 201 ? 12.975 17.246 39.421 1.00 20.56 ? 201 ASN B CA 1 ATOM 5937 C C . ASN B 1 201 ? 12.995 15.796 38.901 1.00 19.84 ? 201 ASN B C 1 ATOM 5938 O O . ASN B 1 201 ? 13.477 14.873 39.566 1.00 19.63 ? 201 ASN B O 1 ATOM 5939 C CB . ASN B 1 201 ? 13.427 17.357 40.888 1.00 23.13 ? 201 ASN B CB 1 ATOM 5940 C CG . ASN B 1 201 ? 14.937 17.204 41.057 1.00 25.46 ? 201 ASN B CG 1 ATOM 5941 O OD1 . ASN B 1 201 ? 15.710 17.400 40.111 1.00 22.66 ? 201 ASN B OD1 1 ATOM 5942 N ND2 . ASN B 1 201 ? 15.347 16.848 42.270 1.00 28.93 ? 201 ASN B ND2 1 ATOM 5943 N N . GLY B 1 202 ? 12.374 15.620 37.734 1.00 18.72 ? 202 GLY B N 1 ATOM 5944 C CA . GLY B 1 202 ? 12.310 14.329 37.074 1.00 18.62 ? 202 GLY B CA 1 ATOM 5945 C C . GLY B 1 202 ? 11.249 13.336 37.512 1.00 18.45 ? 202 GLY B C 1 ATOM 5946 O O . GLY B 1 202 ? 11.196 12.240 36.959 1.00 17.76 ? 202 GLY B O 1 ATOM 5947 N N . THR B 1 203 ? 10.395 13.705 38.468 1.00 19.96 ? 203 THR B N 1 ATOM 5948 C CA . THR B 1 203 ? 9.359 12.786 38.938 1.00 19.21 ? 203 THR B CA 1 ATOM 5949 C C . THR B 1 203 ? 8.006 13.423 39.272 1.00 19.06 ? 203 THR B C 1 ATOM 5950 O O . THR B 1 203 ? 7.902 14.635 39.482 1.00 16.93 ? 203 THR B O 1 ATOM 5951 C CB . THR B 1 203 ? 9.885 11.901 40.124 1.00 23.21 ? 203 THR B CB 1 ATOM 5952 O OG1 . THR B 1 203 ? 8.909 10.907 40.468 1.00 25.08 ? 203 THR B OG1 1 ATOM 5953 C CG2 . THR B 1 203 ? 10.226 12.750 41.348 1.00 23.13 ? 203 THR B CG2 1 ATOM 5954 N N . ALA B 1 204 ? 6.970 12.585 39.263 1.00 17.51 ? 204 ALA B N 1 ATOM 5955 C CA . ALA B 1 204 ? 5.595 12.983 39.567 1.00 19.75 ? 204 ALA B CA 1 ATOM 5956 C C . ALA B 1 204 ? 4.749 11.742 39.783 1.00 20.13 ? 204 ALA B C 1 ATOM 5957 O O . ALA B 1 204 ? 5.132 10.637 39.385 1.00 20.26 ? 204 ALA B O 1 ATOM 5958 C CB . ALA B 1 204 ? 4.996 13.813 38.430 1.00 17.09 ? 204 ALA B CB 1 ATOM 5959 N N . VAL B 1 205 ? 3.607 11.940 40.435 1.00 21.74 ? 205 VAL B N 1 ATOM 5960 C CA . VAL B 1 205 ? 2.648 10.874 40.702 1.00 21.93 ? 205 VAL B CA 1 ATOM 5961 C C . VAL B 1 205 ? 1.586 10.905 39.606 1.00 22.93 ? 205 VAL B C 1 ATOM 5962 O O . VAL B 1 205 ? 1.146 11.980 39.181 1.00 22.50 ? 205 VAL B O 1 ATOM 5963 C CB . VAL B 1 205 ? 1.985 11.047 42.106 1.00 22.58 ? 205 VAL B CB 1 ATOM 5964 C CG1 . VAL B 1 205 ? 0.876 10.013 42.346 1.00 21.85 ? 205 VAL B CG1 1 ATOM 5965 C CG2 . VAL B 1 205 ? 3.027 10.886 43.173 1.00 21.86 ? 205 VAL B CG2 1 ATOM 5966 N N . ASN B 1 206 ? 1.206 9.715 39.141 1.00 23.92 ? 206 ASN B N 1 ATOM 5967 C CA . ASN B 1 206 ? 0.180 9.545 38.118 1.00 25.49 ? 206 ASN B CA 1 ATOM 5968 C C . ASN B 1 206 ? -1.168 9.840 38.796 1.00 27.36 ? 206 ASN B C 1 ATOM 5969 O O . ASN B 1 206 ? -1.516 9.189 39.783 1.00 26.83 ? 206 ASN B O 1 ATOM 5970 C CB . ASN B 1 206 ? 0.211 8.107 37.593 1.00 26.34 ? 206 ASN B CB 1 ATOM 5971 C CG . ASN B 1 206 ? -0.582 7.930 36.317 1.00 26.14 ? 206 ASN B CG 1 ATOM 5972 O OD1 . ASN B 1 206 ? -1.808 7.931 36.329 1.00 27.31 ? 206 ASN B OD1 1 ATOM 5973 N ND2 . ASN B 1 206 ? 0.120 7.775 35.205 1.00 28.04 ? 206 ASN B ND2 1 ATOM 5974 N N . PRO B 1 207 ? -1.935 10.828 38.276 1.00 29.64 ? 207 PRO B N 1 ATOM 5975 C CA . PRO B 1 207 ? -3.239 11.209 38.841 1.00 31.93 ? 207 PRO B CA 1 ATOM 5976 C C . PRO B 1 207 ? -4.346 10.147 38.791 1.00 33.34 ? 207 PRO B C 1 ATOM 5977 O O . PRO B 1 207 ? -5.340 10.251 39.517 1.00 34.47 ? 207 PRO B O 1 ATOM 5978 C CB . PRO B 1 207 ? -3.612 12.436 38.014 1.00 30.43 ? 207 PRO B CB 1 ATOM 5979 C CG . PRO B 1 207 ? -3.015 12.125 36.676 1.00 31.73 ? 207 PRO B CG 1 ATOM 5980 C CD . PRO B 1 207 ? -1.649 11.633 37.070 1.00 29.83 ? 207 PRO B CD 1 ATOM 5981 N N . ASN B 1 208 ? -4.150 9.129 37.952 1.00 34.16 ? 208 ASN B N 1 ATOM 5982 C CA . ASN B 1 208 ? -5.123 8.052 37.776 1.00 35.05 ? 208 ASN B CA 1 ATOM 5983 C C . ASN B 1 208 ? -4.798 6.761 38.529 1.00 34.48 ? 208 ASN B C 1 ATOM 5984 O O . ASN B 1 208 ? -5.660 6.220 39.225 1.00 34.99 ? 208 ASN B O 1 ATOM 5985 C CB . ASN B 1 208 ? -5.308 7.739 36.284 1.00 36.11 ? 208 ASN B CB 1 ATOM 5986 C CG . ASN B 1 208 ? -5.786 8.940 35.484 1.00 37.92 ? 208 ASN B CG 1 ATOM 5987 O OD1 . ASN B 1 208 ? -5.073 9.442 34.614 1.00 39.25 ? 208 ASN B OD1 1 ATOM 5988 N ND2 . ASN B 1 208 ? -6.994 9.407 35.778 1.00 37.66 ? 208 ASN B ND2 1 ATOM 5989 N N . THR B 1 209 ? -3.560 6.282 38.394 1.00 33.86 ? 209 THR B N 1 ATOM 5990 C CA . THR B 1 209 ? -3.121 5.032 39.027 1.00 33.86 ? 209 THR B CA 1 ATOM 5991 C C . THR B 1 209 ? -2.456 5.164 40.398 1.00 33.99 ? 209 THR B C 1 ATOM 5992 O O . THR B 1 209 ? -2.430 4.201 41.172 1.00 34.76 ? 209 THR B O 1 ATOM 5993 C CB . THR B 1 209 ? -2.157 4.242 38.108 1.00 34.09 ? 209 THR B CB 1 ATOM 5994 O OG1 . THR B 1 209 ? -0.973 5.015 37.875 1.00 32.81 ? 209 THR B OG1 1 ATOM 5995 C CG2 . THR B 1 209 ? -2.820 3.906 36.773 1.00 34.25 ? 209 THR B CG2 1 ATOM 5996 N N . GLY B 1 210 ? -1.881 6.335 40.670 1.00 33.34 ? 210 GLY B N 1 ATOM 5997 C CA . GLY B 1 210 ? -1.205 6.571 41.936 1.00 32.99 ? 210 GLY B CA 1 ATOM 5998 C C . GLY B 1 210 ? 0.257 6.153 41.923 1.00 33.01 ? 210 GLY B C 1 ATOM 5999 O O . GLY B 1 210 ? 0.942 6.257 42.945 1.00 33.67 ? 210 GLY B O 1 ATOM 6000 N N . GLU B 1 211 ? 0.732 5.693 40.763 1.00 32.23 ? 211 GLU B N 1 ATOM 6001 C CA . GLU B 1 211 ? 2.118 5.256 40.577 1.00 32.17 ? 211 GLU B CA 1 ATOM 6002 C C . GLU B 1 211 ? 3.078 6.436 40.488 1.00 32.05 ? 211 GLU B C 1 ATOM 6003 O O . GLU B 1 211 ? 2.681 7.540 40.113 1.00 31.61 ? 211 GLU B O 1 ATOM 6004 C CB . GLU B 1 211 ? 2.251 4.407 39.314 1.00 34.64 ? 211 GLU B CB 1 ATOM 6005 C CG . GLU B 1 211 ? 1.618 3.029 39.402 1.00 38.39 ? 211 GLU B CG 1 ATOM 6006 C CD . GLU B 1 211 ? 1.812 2.229 38.132 1.00 40.67 ? 211 GLU B CD 1 ATOM 6007 O OE1 . GLU B 1 211 ? 2.970 1.877 37.823 1.00 43.45 ? 211 GLU B OE1 1 ATOM 6008 O OE2 . GLU B 1 211 ? 0.809 1.953 37.440 1.00 43.07 ? 211 GLU B OE2 1 ATOM 6009 N N . GLY B 1 212 ? 4.340 6.182 40.825 1.00 30.78 ? 212 GLY B N 1 ATOM 6010 C CA . GLY B 1 212 ? 5.357 7.216 40.796 1.00 30.17 ? 212 GLY B CA 1 ATOM 6011 C C . GLY B 1 212 ? 5.610 7.796 42.169 1.00 30.07 ? 212 GLY B C 1 ATOM 6012 O O . GLY B 1 212 ? 5.089 7.287 43.165 1.00 29.65 ? 212 GLY B O 1 ATOM 6013 N N . GLN B 1 213 ? 6.396 8.869 42.222 1.00 28.46 ? 213 GLN B N 1 ATOM 6014 C CA . GLN B 1 213 ? 6.721 9.511 43.489 1.00 27.89 ? 213 GLN B CA 1 ATOM 6015 C C . GLN B 1 213 ? 6.823 11.025 43.357 1.00 26.74 ? 213 GLN B C 1 ATOM 6016 O O . GLN B 1 213 ? 7.126 11.547 42.284 1.00 24.35 ? 213 GLN B O 1 ATOM 6017 C CB . GLN B 1 213 ? 8.033 8.930 44.055 1.00 31.07 ? 213 GLN B CB 1 ATOM 6018 C CG . GLN B 1 213 ? 8.265 9.151 45.565 1.00 36.63 ? 213 GLN B CG 1 ATOM 6019 C CD . GLN B 1 213 ? 7.128 8.619 46.440 1.00 39.71 ? 213 GLN B CD 1 ATOM 6020 O OE1 . GLN B 1 213 ? 6.939 7.407 46.567 1.00 41.67 ? 213 GLN B OE1 1 ATOM 6021 N NE2 . GLN B 1 213 ? 6.364 9.533 47.040 1.00 39.12 ? 213 GLN B NE2 1 ATOM 6022 N N . TYR B 1 214 ? 6.511 11.723 44.449 1.00 24.96 ? 214 TYR B N 1 ATOM 6023 C CA . TYR B 1 214 ? 6.599 13.178 44.504 1.00 24.35 ? 214 TYR B CA 1 ATOM 6024 C C . TYR B 1 214 ? 8.067 13.532 44.721 1.00 23.85 ? 214 TYR B C 1 ATOM 6025 O O . TYR B 1 214 ? 8.810 12.744 45.324 1.00 22.32 ? 214 TYR B O 1 ATOM 6026 C CB . TYR B 1 214 ? 5.811 13.728 45.700 1.00 24.08 ? 214 TYR B CB 1 ATOM 6027 C CG . TYR B 1 214 ? 4.308 13.562 45.653 1.00 24.06 ? 214 TYR B CG 1 ATOM 6028 C CD1 . TYR B 1 214 ? 3.515 14.393 44.835 1.00 22.69 ? 214 TYR B CD1 1 ATOM 6029 C CD2 . TYR B 1 214 ? 3.657 12.598 46.456 1.00 22.81 ? 214 TYR B CD2 1 ATOM 6030 C CE1 . TYR B 1 214 ? 2.100 14.275 44.815 1.00 23.42 ? 214 TYR B CE1 1 ATOM 6031 C CE2 . TYR B 1 214 ? 2.234 12.469 46.446 1.00 22.26 ? 214 TYR B CE2 1 ATOM 6032 C CZ . TYR B 1 214 ? 1.471 13.313 45.623 1.00 21.70 ? 214 TYR B CZ 1 ATOM 6033 O OH . TYR B 1 214 ? 0.102 13.213 45.601 1.00 21.08 ? 214 TYR B OH 1 ATOM 6034 N N . ALA B 1 215 ? 8.488 14.696 44.217 1.00 22.36 ? 215 ALA B N 1 ATOM 6035 C CA . ALA B 1 215 ? 9.859 15.174 44.417 1.00 21.12 ? 215 ALA B CA 1 ATOM 6036 C C . ALA B 1 215 ? 9.945 15.494 45.908 1.00 21.06 ? 215 ALA B C 1 ATOM 6037 O O . ALA B 1 215 ? 9.026 16.097 46.471 1.00 19.79 ? 215 ALA B O 1 ATOM 6038 C CB . ALA B 1 215 ? 10.130 16.410 43.583 1.00 20.21 ? 215 ALA B CB 1 ATOM 6039 N N . ASN B 1 216 ? 10.991 14.990 46.552 1.00 20.84 ? 216 ASN B N 1 ATOM 6040 C CA . ASN B 1 216 ? 11.162 15.164 47.985 1.00 21.55 ? 216 ASN B CA 1 ATOM 6041 C C . ASN B 1 216 ? 12.411 15.960 48.343 1.00 21.58 ? 216 ASN B C 1 ATOM 6042 O O . ASN B 1 216 ? 13.536 15.465 48.236 1.00 21.44 ? 216 ASN B O 1 ATOM 6043 C CB . ASN B 1 216 ? 11.173 13.780 48.649 1.00 24.11 ? 216 ASN B CB 1 ATOM 6044 C CG . ASN B 1 216 ? 10.968 13.830 50.155 1.00 26.72 ? 216 ASN B CG 1 ATOM 6045 O OD1 . ASN B 1 216 ? 10.756 14.889 50.762 1.00 26.58 ? 216 ASN B OD1 1 ATOM 6046 N ND2 . ASN B 1 216 ? 11.029 12.649 50.756 1.00 29.25 ? 216 ASN B ND2 1 ATOM 6047 N N . VAL B 1 217 ? 12.186 17.197 48.779 1.00 20.83 ? 217 VAL B N 1 ATOM 6048 C CA . VAL B 1 217 ? 13.266 18.094 49.175 1.00 21.32 ? 217 VAL B CA 1 ATOM 6049 C C . VAL B 1 217 ? 13.317 18.175 50.692 1.00 20.80 ? 217 VAL B C 1 ATOM 6050 O O . VAL B 1 217 ? 12.320 18.492 51.336 1.00 20.33 ? 217 VAL B O 1 ATOM 6051 C CB . VAL B 1 217 ? 13.069 19.519 48.600 1.00 21.11 ? 217 VAL B CB 1 ATOM 6052 C CG1 . VAL B 1 217 ? 14.254 20.408 48.931 1.00 20.68 ? 217 VAL B CG1 1 ATOM 6053 C CG2 . VAL B 1 217 ? 12.891 19.458 47.108 1.00 21.85 ? 217 VAL B CG2 1 ATOM 6054 N N . THR B 1 218 ? 14.491 17.893 51.246 1.00 22.12 ? 218 THR B N 1 ATOM 6055 C CA . THR B 1 218 ? 14.689 17.955 52.682 1.00 22.71 ? 218 THR B CA 1 ATOM 6056 C C . THR B 1 218 ? 15.304 19.294 53.066 1.00 22.02 ? 218 THR B C 1 ATOM 6057 O O . THR B 1 218 ? 16.407 19.643 52.629 1.00 22.75 ? 218 THR B O 1 ATOM 6058 C CB . THR B 1 218 ? 15.538 16.765 53.209 1.00 24.10 ? 218 THR B CB 1 ATOM 6059 O OG1 . THR B 1 218 ? 14.871 15.537 52.891 1.00 23.83 ? 218 THR B OG1 1 ATOM 6060 C CG2 . THR B 1 218 ? 15.712 16.839 54.733 1.00 24.36 ? 218 THR B CG2 1 ATOM 6061 N N . LEU B 1 219 ? 14.532 20.060 53.830 1.00 20.25 ? 219 LEU B N 1 ATOM 6062 C CA . LEU B 1 219 ? 14.956 21.360 54.331 1.00 20.14 ? 219 LEU B CA 1 ATOM 6063 C C . LEU B 1 219 ? 15.496 21.167 55.741 1.00 20.78 ? 219 LEU B C 1 ATOM 6064 O O . LEU B 1 219 ? 14.958 20.366 56.512 1.00 21.15 ? 219 LEU B O 1 ATOM 6065 C CB . LEU B 1 219 ? 13.776 22.338 54.384 1.00 19.30 ? 219 LEU B CB 1 ATOM 6066 C CG . LEU B 1 219 ? 13.049 22.776 53.111 1.00 20.62 ? 219 LEU B CG 1 ATOM 6067 C CD1 . LEU B 1 219 ? 11.924 23.725 53.493 1.00 19.34 ? 219 LEU B CD1 1 ATOM 6068 C CD2 . LEU B 1 219 ? 13.998 23.465 52.139 1.00 18.80 ? 219 LEU B CD2 1 ATOM 6069 N N . THR B 1 220 ? 16.573 21.877 56.061 1.00 20.63 ? 220 THR B N 1 ATOM 6070 C CA . THR B 1 220 ? 17.184 21.813 57.385 1.00 20.81 ? 220 THR B CA 1 ATOM 6071 C C . THR B 1 220 ? 16.559 22.969 58.184 1.00 21.09 ? 220 THR B C 1 ATOM 6072 O O . THR B 1 220 ? 16.674 24.127 57.773 1.00 19.05 ? 220 THR B O 1 ATOM 6073 C CB . THR B 1 220 ? 18.725 21.965 57.291 1.00 20.55 ? 220 THR B CB 1 ATOM 6074 O OG1 . THR B 1 220 ? 19.237 21.033 56.331 1.00 19.01 ? 220 THR B OG1 1 ATOM 6075 C CG2 . THR B 1 220 ? 19.397 21.698 58.641 1.00 20.30 ? 220 THR B CG2 1 ATOM 6076 N N . PRO B 1 221 ? 15.863 22.667 59.312 1.00 21.68 ? 221 PRO B N 1 ATOM 6077 C CA . PRO B 1 221 ? 15.214 23.682 60.157 1.00 21.38 ? 221 PRO B CA 1 ATOM 6078 C C . PRO B 1 221 ? 16.085 24.874 60.544 1.00 22.64 ? 221 PRO B C 1 ATOM 6079 O O . PRO B 1 221 ? 17.220 24.708 61.005 1.00 24.26 ? 221 PRO B O 1 ATOM 6080 C CB . PRO B 1 221 ? 14.780 22.877 61.382 1.00 22.03 ? 221 PRO B CB 1 ATOM 6081 C CG . PRO B 1 221 ? 14.454 21.558 60.801 1.00 20.69 ? 221 PRO B CG 1 ATOM 6082 C CD . PRO B 1 221 ? 15.628 21.323 59.881 1.00 20.87 ? 221 PRO B CD 1 ATOM 6083 N N . GLY B 1 222 ? 15.572 26.066 60.246 1.00 22.49 ? 222 GLY B N 1 ATOM 6084 C CA . GLY B 1 222 ? 16.270 27.303 60.552 1.00 23.67 ? 222 GLY B CA 1 ATOM 6085 C C . GLY B 1 222 ? 17.276 27.824 59.545 1.00 23.74 ? 222 GLY B C 1 ATOM 6086 O O . GLY B 1 222 ? 17.744 28.964 59.672 1.00 24.62 ? 222 GLY B O 1 ATOM 6087 N N . LYS B 1 223 ? 17.612 27.003 58.553 1.00 22.75 ? 223 LYS B N 1 ATOM 6088 C CA . LYS B 1 223 ? 18.575 27.397 57.532 1.00 21.81 ? 223 LYS B CA 1 ATOM 6089 C C . LYS B 1 223 ? 17.938 28.044 56.306 1.00 20.67 ? 223 LYS B C 1 ATOM 6090 O O . LYS B 1 223 ? 16.749 27.853 56.023 1.00 20.16 ? 223 LYS B O 1 ATOM 6091 C CB . LYS B 1 223 ? 19.457 26.208 57.127 1.00 23.29 ? 223 LYS B CB 1 ATOM 6092 C CG . LYS B 1 223 ? 20.235 25.557 58.283 1.00 25.65 ? 223 LYS B CG 1 ATOM 6093 C CD . LYS B 1 223 ? 21.228 26.499 58.948 1.00 27.53 ? 223 LYS B CD 1 ATOM 6094 C CE . LYS B 1 223 ? 21.880 25.847 60.155 1.00 29.39 ? 223 LYS B CE 1 ATOM 6095 N NZ . LYS B 1 223 ? 22.841 26.772 60.815 1.00 31.62 ? 223 LYS B NZ 1 ATOM 6096 N N . ARG B 1 224 ? 18.738 28.856 55.621 1.00 19.59 ? 224 ARG B N 1 ATOM 6097 C CA . ARG B 1 224 ? 18.329 29.570 54.414 1.00 21.23 ? 224 ARG B CA 1 ATOM 6098 C C . ARG B 1 224 ? 18.825 28.738 53.228 1.00 20.74 ? 224 ARG B C 1 ATOM 6099 O O . ARG B 1 224 ? 20.034 28.524 53.065 1.00 20.43 ? 224 ARG B O 1 ATOM 6100 C CB . ARG B 1 224 ? 18.942 30.974 54.413 1.00 22.87 ? 224 ARG B CB 1 ATOM 6101 C CG . ARG B 1 224 ? 18.673 31.783 55.692 1.00 25.53 ? 224 ARG B CG 1 ATOM 6102 C CD . ARG B 1 224 ? 19.669 32.921 55.883 1.00 28.74 ? 224 ARG B CD 1 ATOM 6103 N NE . ARG B 1 224 ? 21.049 32.435 55.947 1.00 30.94 ? 224 ARG B NE 1 ATOM 6104 C CZ . ARG B 1 224 ? 22.107 33.181 56.256 1.00 32.47 ? 224 ARG B CZ 1 ATOM 6105 N NH1 . ARG B 1 224 ? 21.969 34.472 56.547 1.00 32.54 ? 224 ARG B NH1 1 ATOM 6106 N NH2 . ARG B 1 224 ? 23.319 32.640 56.235 1.00 31.79 ? 224 ARG B NH2 1 ATOM 6107 N N . HIS B 1 225 ? 17.878 28.255 52.425 1.00 18.53 ? 225 HIS B N 1 ATOM 6108 C CA . HIS B 1 225 ? 18.165 27.385 51.281 1.00 17.89 ? 225 HIS B CA 1 ATOM 6109 C C . HIS B 1 225 ? 18.008 28.017 49.907 1.00 17.29 ? 225 HIS B C 1 ATOM 6110 O O . HIS B 1 225 ? 16.958 28.579 49.608 1.00 17.58 ? 225 HIS B O 1 ATOM 6111 C CB . HIS B 1 225 ? 17.229 26.172 51.298 1.00 19.12 ? 225 HIS B CB 1 ATOM 6112 C CG . HIS B 1 225 ? 17.230 25.402 52.578 1.00 20.49 ? 225 HIS B CG 1 ATOM 6113 N ND1 . HIS B 1 225 ? 16.612 25.861 53.721 1.00 21.40 ? 225 HIS B ND1 1 ATOM 6114 C CD2 . HIS B 1 225 ? 17.724 24.178 52.881 1.00 21.71 ? 225 HIS B CD2 1 ATOM 6115 C CE1 . HIS B 1 225 ? 16.723 24.949 54.670 1.00 21.77 ? 225 HIS B CE1 1 ATOM 6116 N NE2 . HIS B 1 225 ? 17.393 23.919 54.187 1.00 21.04 ? 225 HIS B NE2 1 ATOM 6117 N N . ARG B 1 226 ? 19.016 27.855 49.049 1.00 16.64 ? 226 ARG B N 1 ATOM 6118 C CA . ARG B 1 226 ? 18.931 28.367 47.683 1.00 16.33 ? 226 ARG B CA 1 ATOM 6119 C C . ARG B 1 226 ? 18.337 27.251 46.832 1.00 15.24 ? 226 ARG B C 1 ATOM 6120 O O . ARG B 1 226 ? 18.841 26.128 46.841 1.00 14.88 ? 226 ARG B O 1 ATOM 6121 C CB . ARG B 1 226 ? 20.296 28.769 47.115 1.00 16.65 ? 226 ARG B CB 1 ATOM 6122 C CG . ARG B 1 226 ? 20.227 29.424 45.722 1.00 14.20 ? 226 ARG B CG 1 ATOM 6123 C CD . ARG B 1 226 ? 21.610 29.623 45.116 1.00 13.39 ? 226 ARG B CD 1 ATOM 6124 N NE . ARG B 1 226 ? 21.574 30.383 43.868 1.00 12.59 ? 226 ARG B NE 1 ATOM 6125 C CZ . ARG B 1 226 ? 22.542 31.191 43.438 1.00 13.50 ? 226 ARG B CZ 1 ATOM 6126 N NH1 . ARG B 1 226 ? 23.650 31.363 44.153 1.00 13.41 ? 226 ARG B NH1 1 ATOM 6127 N NH2 . ARG B 1 226 ? 22.412 31.816 42.276 1.00 11.18 ? 226 ARG B NH2 1 ATOM 6128 N N . LEU B 1 227 ? 17.228 27.556 46.165 1.00 13.75 ? 227 LEU B N 1 ATOM 6129 C CA . LEU B 1 227 ? 16.558 26.606 45.290 1.00 12.54 ? 227 LEU B CA 1 ATOM 6130 C C . LEU B 1 227 ? 16.540 27.218 43.895 1.00 11.69 ? 227 LEU B C 1 ATOM 6131 O O . LEU B 1 227 ? 16.033 28.321 43.693 1.00 12.36 ? 227 LEU B O 1 ATOM 6132 C CB . LEU B 1 227 ? 15.135 26.308 45.783 1.00 11.46 ? 227 LEU B CB 1 ATOM 6133 C CG . LEU B 1 227 ? 14.364 25.236 45.005 1.00 11.49 ? 227 LEU B CG 1 ATOM 6134 C CD1 . LEU B 1 227 ? 14.870 23.849 45.363 1.00 14.30 ? 227 LEU B CD1 1 ATOM 6135 C CD2 . LEU B 1 227 ? 12.884 25.359 45.297 1.00 12.80 ? 227 LEU B CD2 1 ATOM 6136 N N . ARG B 1 228 ? 17.107 26.487 42.940 1.00 11.80 ? 228 ARG B N 1 ATOM 6137 C CA . ARG B 1 228 ? 17.200 26.940 41.558 1.00 11.34 ? 228 ARG B CA 1 ATOM 6138 C C . ARG B 1 228 ? 16.077 26.343 40.707 1.00 12.22 ? 228 ARG B C 1 ATOM 6139 O O . ARG B 1 228 ? 16.206 25.249 40.150 1.00 12.62 ? 228 ARG B O 1 ATOM 6140 C CB . ARG B 1 228 ? 18.585 26.593 41.017 1.00 11.53 ? 228 ARG B CB 1 ATOM 6141 C CG . ARG B 1 228 ? 19.735 27.092 41.902 1.00 10.60 ? 228 ARG B CG 1 ATOM 6142 C CD . ARG B 1 228 ? 21.034 26.400 41.549 1.00 11.63 ? 228 ARG B CD 1 ATOM 6143 N NE . ARG B 1 228 ? 22.175 26.920 42.300 1.00 10.49 ? 228 ARG B NE 1 ATOM 6144 C CZ . ARG B 1 228 ? 22.934 27.940 41.903 1.00 14.15 ? 228 ARG B CZ 1 ATOM 6145 N NH1 . ARG B 1 228 ? 22.680 28.566 40.759 1.00 11.58 ? 228 ARG B NH1 1 ATOM 6146 N NH2 . ARG B 1 228 ? 23.970 28.324 42.640 1.00 11.27 ? 228 ARG B NH2 1 ATOM 6147 N N . ILE B 1 229 ? 14.972 27.086 40.621 1.00 11.71 ? 229 ILE B N 1 ATOM 6148 C CA . ILE B 1 229 ? 13.775 26.669 39.882 1.00 12.51 ? 229 ILE B CA 1 ATOM 6149 C C . ILE B 1 229 ? 13.894 26.932 38.382 1.00 10.64 ? 229 ILE B C 1 ATOM 6150 O O . ILE B 1 229 ? 14.296 28.009 37.969 1.00 11.18 ? 229 ILE B O 1 ATOM 6151 C CB . ILE B 1 229 ? 12.493 27.377 40.422 1.00 12.29 ? 229 ILE B CB 1 ATOM 6152 C CG1 . ILE B 1 229 ? 12.475 27.353 41.962 1.00 11.56 ? 229 ILE B CG1 1 ATOM 6153 C CG2 . ILE B 1 229 ? 11.233 26.670 39.888 1.00 11.84 ? 229 ILE B CG2 1 ATOM 6154 C CD1 . ILE B 1 229 ? 11.334 28.135 42.605 1.00 13.08 ? 229 ILE B CD1 1 ATOM 6155 N N . LEU B 1 230 ? 13.570 25.920 37.580 1.00 11.18 ? 230 LEU B N 1 ATOM 6156 C CA . LEU B 1 230 ? 13.625 26.035 36.123 1.00 10.79 ? 230 LEU B CA 1 ATOM 6157 C C . LEU B 1 230 ? 12.340 25.538 35.496 1.00 11.09 ? 230 LEU B C 1 ATOM 6158 O O . LEU B 1 230 ? 11.664 24.675 36.059 1.00 11.92 ? 230 LEU B O 1 ATOM 6159 C CB . LEU B 1 230 ? 14.756 25.188 35.519 1.00 11.42 ? 230 LEU B CB 1 ATOM 6160 C CG . LEU B 1 230 ? 16.214 25.240 35.972 1.00 11.68 ? 230 LEU B CG 1 ATOM 6161 C CD1 . LEU B 1 230 ? 16.462 24.252 37.065 1.00 11.18 ? 230 LEU B CD1 1 ATOM 6162 C CD2 . LEU B 1 230 ? 17.113 24.952 34.796 1.00 11.36 ? 230 LEU B CD2 1 ATOM 6163 N N . ASN B 1 231 ? 11.995 26.120 34.350 1.00 9.32 ? 231 ASN B N 1 ATOM 6164 C CA . ASN B 1 231 ? 10.843 25.672 33.581 1.00 9.82 ? 231 ASN B CA 1 ATOM 6165 C C . ASN B 1 231 ? 11.461 25.152 32.288 1.00 7.95 ? 231 ASN B C 1 ATOM 6166 O O . ASN B 1 231 ? 11.794 25.919 31.386 1.00 6.69 ? 231 ASN B O 1 ATOM 6167 C CB . ASN B 1 231 ? 9.820 26.787 33.307 1.00 9.03 ? 231 ASN B CB 1 ATOM 6168 C CG . ASN B 1 231 ? 8.567 26.271 32.578 1.00 11.00 ? 231 ASN B CG 1 ATOM 6169 O OD1 . ASN B 1 231 ? 8.518 25.117 32.154 1.00 9.41 ? 231 ASN B OD1 1 ATOM 6170 N ND2 . ASN B 1 231 ? 7.549 27.116 32.457 1.00 7.62 ? 231 ASN B ND2 1 ATOM 6171 N N . THR B 1 232 ? 11.611 23.831 32.222 1.00 10.74 ? 232 THR B N 1 ATOM 6172 C CA . THR B 1 232 ? 12.212 23.170 31.068 1.00 10.47 ? 232 THR B CA 1 ATOM 6173 C C . THR B 1 232 ? 11.186 22.613 30.080 1.00 9.61 ? 232 THR B C 1 ATOM 6174 O O . THR B 1 232 ? 11.518 21.794 29.211 1.00 10.60 ? 232 THR B O 1 ATOM 6175 C CB . THR B 1 232 ? 13.202 22.053 31.517 1.00 10.83 ? 232 THR B CB 1 ATOM 6176 O OG1 . THR B 1 232 ? 12.509 21.056 32.272 1.00 12.31 ? 232 THR B OG1 1 ATOM 6177 C CG2 . THR B 1 232 ? 14.324 22.635 32.371 1.00 10.82 ? 232 THR B CG2 1 ATOM 6178 N N . SER B 1 233 ? 9.955 23.116 30.185 1.00 8.33 ? 233 SER B N 1 ATOM 6179 C CA . SER B 1 233 ? 8.829 22.694 29.341 1.00 7.18 ? 233 SER B CA 1 ATOM 6180 C C . SER B 1 233 ? 8.921 22.964 27.851 1.00 7.33 ? 233 SER B C 1 ATOM 6181 O O . SER B 1 233 ? 9.779 23.715 27.396 1.00 8.96 ? 233 SER B O 1 ATOM 6182 C CB . SER B 1 233 ? 7.538 23.359 29.814 1.00 6.62 ? 233 SER B CB 1 ATOM 6183 O OG . SER B 1 233 ? 7.144 22.896 31.084 1.00 9.87 ? 233 SER B OG 1 ATOM 6184 N N . THR B 1 234 ? 8.018 22.324 27.108 1.00 7.89 ? 234 THR B N 1 ATOM 6185 C CA . THR B 1 234 ? 7.885 22.525 25.676 1.00 8.92 ? 234 THR B CA 1 ATOM 6186 C C . THR B 1 234 ? 6.749 23.520 25.456 1.00 8.76 ? 234 THR B C 1 ATOM 6187 O O . THR B 1 234 ? 6.741 24.221 24.452 1.00 10.31 ? 234 THR B O 1 ATOM 6188 C CB . THR B 1 234 ? 7.562 21.224 24.904 1.00 9.22 ? 234 THR B CB 1 ATOM 6189 O OG1 . THR B 1 234 ? 6.588 20.447 25.613 1.00 11.40 ? 234 THR B OG1 1 ATOM 6190 C CG2 . THR B 1 234 ? 8.810 20.423 24.680 1.00 9.01 ? 234 THR B CG2 1 ATOM 6191 N N . GLU B 1 235 ? 5.797 23.582 26.396 1.00 8.48 ? 235 GLU B N 1 ATOM 6192 C CA . GLU B 1 235 ? 4.660 24.501 26.277 1.00 9.53 ? 235 GLU B CA 1 ATOM 6193 C C . GLU B 1 235 ? 4.166 25.113 27.587 1.00 10.84 ? 235 GLU B C 1 ATOM 6194 O O . GLU B 1 235 ? 3.891 26.311 27.637 1.00 9.09 ? 235 GLU B O 1 ATOM 6195 C CB . GLU B 1 235 ? 3.480 23.827 25.538 1.00 7.48 ? 235 GLU B CB 1 ATOM 6196 C CG . GLU B 1 235 ? 2.278 24.756 25.153 1.00 10.02 ? 235 GLU B CG 1 ATOM 6197 C CD . GLU B 1 235 ? 1.231 24.938 26.257 1.00 13.17 ? 235 GLU B CD 1 ATOM 6198 O OE1 . GLU B 1 235 ? 1.208 24.118 27.197 1.00 12.29 ? 235 GLU B OE1 1 ATOM 6199 O OE2 . GLU B 1 235 ? 0.455 25.920 26.206 1.00 15.02 ? 235 GLU B OE2 1 ATOM 6200 N N . ASN B 1 236 ? 3.955 24.281 28.603 1.00 10.95 ? 236 ASN B N 1 ATOM 6201 C CA . ASN B 1 236 ? 3.437 24.735 29.893 1.00 11.04 ? 236 ASN B CA 1 ATOM 6202 C C . ASN B 1 236 ? 4.207 25.845 30.606 1.00 11.75 ? 236 ASN B C 1 ATOM 6203 O O . ASN B 1 236 ? 5.436 25.806 30.723 1.00 10.58 ? 236 ASN B O 1 ATOM 6204 C CB . ASN B 1 236 ? 3.325 23.569 30.864 1.00 11.01 ? 236 ASN B CB 1 ATOM 6205 C CG . ASN B 1 236 ? 2.115 22.682 30.627 1.00 11.22 ? 236 ASN B CG 1 ATOM 6206 O OD1 . ASN B 1 236 ? 1.393 22.799 29.637 1.00 13.08 ? 236 ASN B OD1 1 ATOM 6207 N ND2 . ASN B 1 236 ? 1.915 21.748 31.547 1.00 9.59 ? 236 ASN B ND2 1 ATOM 6208 N N . HIS B 1 237 ? 3.448 26.833 31.067 1.00 9.81 ? 237 HIS B N 1 ATOM 6209 C CA . HIS B 1 237 ? 3.975 27.957 31.823 1.00 10.21 ? 237 HIS B CA 1 ATOM 6210 C C . HIS B 1 237 ? 3.444 27.727 33.229 1.00 11.68 ? 237 HIS B C 1 ATOM 6211 O O . HIS B 1 237 ? 2.234 27.571 33.421 1.00 11.79 ? 237 HIS B O 1 ATOM 6212 C CB . HIS B 1 237 ? 3.431 29.263 31.288 1.00 9.55 ? 237 HIS B CB 1 ATOM 6213 C CG . HIS B 1 237 ? 3.908 29.610 29.917 1.00 11.58 ? 237 HIS B CG 1 ATOM 6214 N ND1 . HIS B 1 237 ? 3.782 28.755 28.846 1.00 11.08 ? 237 HIS B ND1 1 ATOM 6215 C CD2 . HIS B 1 237 ? 4.463 30.743 29.431 1.00 12.37 ? 237 HIS B CD2 1 ATOM 6216 C CE1 . HIS B 1 237 ? 4.241 29.349 27.760 1.00 12.78 ? 237 HIS B CE1 1 ATOM 6217 N NE2 . HIS B 1 237 ? 4.662 30.555 28.088 1.00 11.99 ? 237 HIS B NE2 1 ATOM 6218 N N . PHE B 1 238 ? 4.348 27.731 34.205 1.00 11.63 ? 238 PHE B N 1 ATOM 6219 C CA . PHE B 1 238 ? 3.990 27.451 35.591 1.00 12.73 ? 238 PHE B CA 1 ATOM 6220 C C . PHE B 1 238 ? 3.938 28.587 36.584 1.00 13.49 ? 238 PHE B C 1 ATOM 6221 O O . PHE B 1 238 ? 4.598 29.610 36.423 1.00 15.33 ? 238 PHE B O 1 ATOM 6222 C CB . PHE B 1 238 ? 4.965 26.424 36.173 1.00 13.59 ? 238 PHE B CB 1 ATOM 6223 C CG . PHE B 1 238 ? 5.111 25.186 35.354 1.00 11.99 ? 238 PHE B CG 1 ATOM 6224 C CD1 . PHE B 1 238 ? 3.991 24.412 35.014 1.00 11.16 ? 238 PHE B CD1 1 ATOM 6225 C CD2 . PHE B 1 238 ? 6.375 24.778 34.923 1.00 11.80 ? 238 PHE B CD2 1 ATOM 6226 C CE1 . PHE B 1 238 ? 4.129 23.240 34.256 1.00 10.54 ? 238 PHE B CE1 1 ATOM 6227 C CE2 . PHE B 1 238 ? 6.529 23.604 34.156 1.00 12.40 ? 238 PHE B CE2 1 ATOM 6228 C CZ . PHE B 1 238 ? 5.406 22.833 33.823 1.00 11.52 ? 238 PHE B CZ 1 ATOM 6229 N N . GLN B 1 239 ? 3.140 28.364 37.627 1.00 13.26 ? 239 GLN B N 1 ATOM 6230 C CA . GLN B 1 239 ? 3.025 29.265 38.766 1.00 12.61 ? 239 GLN B CA 1 ATOM 6231 C C . GLN B 1 239 ? 3.477 28.354 39.896 1.00 12.66 ? 239 GLN B C 1 ATOM 6232 O O . GLN B 1 239 ? 2.986 27.228 40.015 1.00 13.09 ? 239 GLN B O 1 ATOM 6233 C CB . GLN B 1 239 ? 1.589 29.717 39.028 1.00 12.14 ? 239 GLN B CB 1 ATOM 6234 C CG . GLN B 1 239 ? 0.969 30.549 37.924 1.00 12.63 ? 239 GLN B CG 1 ATOM 6235 C CD . GLN B 1 239 ? -0.386 31.118 38.293 1.00 12.92 ? 239 GLN B CD 1 ATOM 6236 O OE1 . GLN B 1 239 ? -0.844 32.069 37.671 1.00 15.03 ? 239 GLN B OE1 1 ATOM 6237 N NE2 . GLN B 1 239 ? -1.042 30.532 39.295 1.00 14.25 ? 239 GLN B NE2 1 ATOM 6238 N N . VAL B 1 240 ? 4.483 28.785 40.651 1.00 12.80 ? 240 VAL B N 1 ATOM 6239 C CA . VAL B 1 240 ? 4.991 27.981 41.761 1.00 13.00 ? 240 VAL B CA 1 ATOM 6240 C C . VAL B 1 240 ? 4.816 28.660 43.112 1.00 13.29 ? 240 VAL B C 1 ATOM 6241 O O . VAL B 1 240 ? 4.940 29.878 43.224 1.00 11.55 ? 240 VAL B O 1 ATOM 6242 C CB . VAL B 1 240 ? 6.474 27.548 41.557 1.00 14.09 ? 240 VAL B CB 1 ATOM 6243 C CG1 . VAL B 1 240 ? 6.622 26.726 40.278 1.00 11.84 ? 240 VAL B CG1 1 ATOM 6244 C CG2 . VAL B 1 240 ? 7.418 28.742 41.542 1.00 13.31 ? 240 VAL B CG2 1 ATOM 6245 N N . SER B 1 241 ? 4.515 27.855 44.125 1.00 14.40 ? 241 SER B N 1 ATOM 6246 C CA . SER B 1 241 ? 4.318 28.339 45.488 1.00 14.34 ? 241 SER B CA 1 ATOM 6247 C C . SER B 1 241 ? 4.550 27.215 46.477 1.00 13.94 ? 241 SER B C 1 ATOM 6248 O O . SER B 1 241 ? 4.333 26.045 46.160 1.00 14.49 ? 241 SER B O 1 ATOM 6249 C CB . SER B 1 241 ? 2.896 28.895 45.676 1.00 13.22 ? 241 SER B CB 1 ATOM 6250 O OG . SER B 1 241 ? 1.915 27.950 45.282 1.00 16.79 ? 241 SER B OG 1 ATOM 6251 N N . LEU B 1 242 ? 5.036 27.580 47.658 1.00 13.58 ? 242 LEU B N 1 ATOM 6252 C CA . LEU B 1 242 ? 5.274 26.622 48.729 1.00 13.33 ? 242 LEU B CA 1 ATOM 6253 C C . LEU B 1 242 ? 4.333 27.024 49.855 1.00 14.21 ? 242 LEU B C 1 ATOM 6254 O O . LEU B 1 242 ? 4.393 28.158 50.342 1.00 14.69 ? 242 LEU B O 1 ATOM 6255 C CB . LEU B 1 242 ? 6.739 26.654 49.186 1.00 12.80 ? 242 LEU B CB 1 ATOM 6256 C CG . LEU B 1 242 ? 7.206 25.734 50.328 1.00 13.26 ? 242 LEU B CG 1 ATOM 6257 C CD1 . LEU B 1 242 ? 6.895 24.279 50.062 1.00 14.10 ? 242 LEU B CD1 1 ATOM 6258 C CD2 . LEU B 1 242 ? 8.692 25.920 50.538 1.00 15.40 ? 242 LEU B CD2 1 ATOM 6259 N N . VAL B 1 243 ? 3.456 26.096 50.243 1.00 14.62 ? 243 VAL B N 1 ATOM 6260 C CA . VAL B 1 243 ? 2.468 26.321 51.305 1.00 17.85 ? 243 VAL B CA 1 ATOM 6261 C C . VAL B 1 243 ? 3.116 26.814 52.605 1.00 18.51 ? 243 VAL B C 1 ATOM 6262 O O . VAL B 1 243 ? 4.147 26.281 53.034 1.00 20.02 ? 243 VAL B O 1 ATOM 6263 C CB . VAL B 1 243 ? 1.616 25.033 51.587 1.00 16.79 ? 243 VAL B CB 1 ATOM 6264 C CG1 . VAL B 1 243 ? 0.555 25.293 52.661 1.00 16.37 ? 243 VAL B CG1 1 ATOM 6265 C CG2 . VAL B 1 243 ? 0.931 24.562 50.317 1.00 17.72 ? 243 VAL B CG2 1 ATOM 6266 N N . ASN B 1 244 ? 2.561 27.912 53.131 1.00 19.80 ? 244 ASN B N 1 ATOM 6267 C CA . ASN B 1 244 ? 2.985 28.558 54.382 1.00 20.83 ? 244 ASN B CA 1 ATOM 6268 C C . ASN B 1 244 ? 4.348 29.284 54.340 1.00 20.18 ? 244 ASN B C 1 ATOM 6269 O O . ASN B 1 244 ? 4.767 29.859 55.345 1.00 19.11 ? 244 ASN B O 1 ATOM 6270 C CB . ASN B 1 244 ? 2.922 27.544 55.550 1.00 23.00 ? 244 ASN B CB 1 ATOM 6271 C CG . ASN B 1 244 ? 2.418 28.152 56.846 1.00 26.81 ? 244 ASN B CG 1 ATOM 6272 O OD1 . ASN B 1 244 ? 3.087 28.073 57.876 1.00 26.77 ? 244 ASN B OD1 1 ATOM 6273 N ND2 . ASN B 1 244 ? 1.209 28.702 56.816 1.00 28.41 ? 244 ASN B ND2 1 ATOM 6274 N N . HIS B 1 245 ? 5.018 29.273 53.181 1.00 19.00 ? 245 HIS B N 1 ATOM 6275 C CA . HIS B 1 245 ? 6.319 29.943 53.017 1.00 18.10 ? 245 HIS B CA 1 ATOM 6276 C C . HIS B 1 245 ? 6.305 30.984 51.918 1.00 19.20 ? 245 HIS B C 1 ATOM 6277 O O . HIS B 1 245 ? 5.471 30.954 51.006 1.00 19.06 ? 245 HIS B O 1 ATOM 6278 C CB . HIS B 1 245 ? 7.439 28.978 52.616 1.00 17.49 ? 245 HIS B CB 1 ATOM 6279 C CG . HIS B 1 245 ? 7.727 27.899 53.605 1.00 17.16 ? 245 HIS B CG 1 ATOM 6280 N ND1 . HIS B 1 245 ? 6.827 26.896 53.889 1.00 19.36 ? 245 HIS B ND1 1 ATOM 6281 C CD2 . HIS B 1 245 ? 8.852 27.606 54.297 1.00 17.03 ? 245 HIS B CD2 1 ATOM 6282 C CE1 . HIS B 1 245 ? 7.389 26.026 54.708 1.00 18.96 ? 245 HIS B CE1 1 ATOM 6283 N NE2 . HIS B 1 245 ? 8.617 26.433 54.972 1.00 18.58 ? 245 HIS B NE2 1 ATOM 6284 N N . THR B 1 246 ? 7.299 31.863 51.990 1.00 18.37 ? 246 THR B N 1 ATOM 6285 C CA . THR B 1 246 ? 7.521 32.896 50.997 1.00 18.22 ? 246 THR B CA 1 ATOM 6286 C C . THR B 1 246 ? 8.808 32.470 50.282 1.00 17.59 ? 246 THR B C 1 ATOM 6287 O O . THR B 1 246 ? 9.506 31.557 50.735 1.00 16.44 ? 246 THR B O 1 ATOM 6288 C CB . THR B 1 246 ? 7.718 34.287 51.641 1.00 19.13 ? 246 THR B CB 1 ATOM 6289 O OG1 . THR B 1 246 ? 8.790 34.242 52.592 1.00 18.33 ? 246 THR B OG1 1 ATOM 6290 C CG2 . THR B 1 246 ? 6.432 34.766 52.322 1.00 21.13 ? 246 THR B CG2 1 ATOM 6291 N N . MET B 1 247 ? 9.071 33.063 49.122 1.00 17.75 ? 247 MET B N 1 ATOM 6292 C CA . MET B 1 247 ? 10.280 32.766 48.356 1.00 16.54 ? 247 MET B CA 1 ATOM 6293 C C . MET B 1 247 ? 10.939 34.092 48.045 1.00 15.69 ? 247 MET B C 1 ATOM 6294 O O . MET B 1 247 ? 10.267 35.036 47.627 1.00 15.12 ? 247 MET B O 1 ATOM 6295 C CB . MET B 1 247 ? 9.949 32.034 47.050 1.00 16.32 ? 247 MET B CB 1 ATOM 6296 C CG . MET B 1 247 ? 9.377 30.630 47.219 1.00 17.84 ? 247 MET B CG 1 ATOM 6297 S SD . MET B 1 247 ? 9.050 29.809 45.648 1.00 18.79 ? 247 MET B SD 1 ATOM 6298 C CE . MET B 1 247 ? 7.673 30.761 45.051 1.00 17.35 ? 247 MET B CE 1 ATOM 6299 N N . THR B 1 248 ? 12.242 34.182 48.297 1.00 15.89 ? 248 THR B N 1 ATOM 6300 C CA . THR B 1 248 ? 12.976 35.409 48.024 1.00 16.09 ? 248 THR B CA 1 ATOM 6301 C C . THR B 1 248 ? 13.851 35.229 46.789 1.00 15.21 ? 248 THR B C 1 ATOM 6302 O O . THR B 1 248 ? 14.839 34.493 46.814 1.00 16.63 ? 248 THR B O 1 ATOM 6303 C CB . THR B 1 248 ? 13.800 35.878 49.250 1.00 16.35 ? 248 THR B CB 1 ATOM 6304 O OG1 . THR B 1 248 ? 12.957 35.906 50.407 1.00 18.18 ? 248 THR B OG1 1 ATOM 6305 C CG2 . THR B 1 248 ? 14.327 37.282 49.031 1.00 16.55 ? 248 THR B CG2 1 ATOM 6306 N N . VAL B 1 249 ? 13.458 35.905 45.710 1.00 15.06 ? 249 VAL B N 1 ATOM 6307 C CA . VAL B 1 249 ? 14.161 35.857 44.427 1.00 14.39 ? 249 VAL B CA 1 ATOM 6308 C C . VAL B 1 249 ? 15.510 36.566 44.517 1.00 13.27 ? 249 VAL B C 1 ATOM 6309 O O . VAL B 1 249 ? 15.596 37.683 45.017 1.00 12.85 ? 249 VAL B O 1 ATOM 6310 C CB . VAL B 1 249 ? 13.310 36.522 43.291 1.00 15.12 ? 249 VAL B CB 1 ATOM 6311 C CG1 . VAL B 1 249 ? 14.011 36.425 41.939 1.00 13.50 ? 249 VAL B CG1 1 ATOM 6312 C CG2 . VAL B 1 249 ? 11.948 35.873 43.207 1.00 13.72 ? 249 VAL B CG2 1 ATOM 6313 N N . ILE B 1 250 ? 16.561 35.871 44.093 1.00 12.54 ? 250 ILE B N 1 ATOM 6314 C CA . ILE B 1 250 ? 17.908 36.438 44.079 1.00 12.15 ? 250 ILE B CA 1 ATOM 6315 C C . ILE B 1 250 ? 18.471 36.475 42.656 1.00 12.25 ? 250 ILE B C 1 ATOM 6316 O O . ILE B 1 250 ? 19.496 37.110 42.405 1.00 13.14 ? 250 ILE B O 1 ATOM 6317 C CB . ILE B 1 250 ? 18.886 35.713 45.047 1.00 11.04 ? 250 ILE B CB 1 ATOM 6318 C CG1 . ILE B 1 250 ? 18.965 34.210 44.758 1.00 11.48 ? 250 ILE B CG1 1 ATOM 6319 C CG2 . ILE B 1 250 ? 18.483 35.998 46.480 1.00 11.82 ? 250 ILE B CG2 1 ATOM 6320 C CD1 . ILE B 1 250 ? 20.169 33.513 45.388 1.00 13.01 ? 250 ILE B CD1 1 ATOM 6321 N N . ALA B 1 251 ? 17.779 35.799 41.735 1.00 11.35 ? 251 ALA B N 1 ATOM 6322 C CA . ALA B 1 251 ? 18.157 35.752 40.319 1.00 10.86 ? 251 ALA B CA 1 ATOM 6323 C C . ALA B 1 251 ? 16.981 35.423 39.411 1.00 9.99 ? 251 ALA B C 1 ATOM 6324 O O . ALA B 1 251 ? 16.127 34.606 39.762 1.00 11.50 ? 251 ALA B O 1 ATOM 6325 C CB . ALA B 1 251 ? 19.297 34.763 40.080 1.00 9.02 ? 251 ALA B CB 1 ATOM 6326 N N . ALA B 1 252 ? 16.928 36.120 38.276 1.00 9.97 ? 252 ALA B N 1 ATOM 6327 C CA . ALA B 1 252 ? 15.909 35.947 37.239 1.00 9.66 ? 252 ALA B CA 1 ATOM 6328 C C . ALA B 1 252 ? 16.723 35.479 36.036 1.00 10.65 ? 252 ALA B C 1 ATOM 6329 O O . ALA B 1 252 ? 17.576 36.218 35.529 1.00 11.24 ? 252 ALA B O 1 ATOM 6330 C CB . ALA B 1 252 ? 15.217 37.269 36.946 1.00 8.57 ? 252 ALA B CB 1 ATOM 6331 N N . ASP B 1 253 ? 16.480 34.233 35.622 1.00 11.91 ? 253 ASP B N 1 ATOM 6332 C CA . ASP B 1 253 ? 17.212 33.558 34.538 1.00 11.94 ? 253 ASP B CA 1 ATOM 6333 C C . ASP B 1 253 ? 18.673 33.454 35.001 1.00 12.98 ? 253 ASP B C 1 ATOM 6334 O O . ASP B 1 253 ? 18.917 32.954 36.104 1.00 13.24 ? 253 ASP B O 1 ATOM 6335 C CB . ASP B 1 253 ? 17.030 34.245 33.164 1.00 9.99 ? 253 ASP B CB 1 ATOM 6336 C CG . ASP B 1 253 ? 15.613 34.088 32.606 1.00 9.63 ? 253 ASP B CG 1 ATOM 6337 O OD1 . ASP B 1 253 ? 14.799 33.357 33.209 1.00 10.53 ? 253 ASP B OD1 1 ATOM 6338 O OD2 . ASP B 1 253 ? 15.308 34.699 31.559 1.00 9.65 ? 253 ASP B OD2 1 ATOM 6339 N N . MET B 1 254 ? 19.618 33.999 34.244 1.00 12.96 ? 254 MET B N 1 ATOM 6340 C CA . MET B 1 254 ? 21.010 33.944 34.669 1.00 15.22 ? 254 MET B CA 1 ATOM 6341 C C . MET B 1 254 ? 21.531 35.320 35.096 1.00 14.37 ? 254 MET B C 1 ATOM 6342 O O . MET B 1 254 ? 22.732 35.589 35.051 1.00 13.74 ? 254 MET B O 1 ATOM 6343 C CB . MET B 1 254 ? 21.882 33.322 33.581 1.00 16.91 ? 254 MET B CB 1 ATOM 6344 C CG . MET B 1 254 ? 22.895 32.367 34.162 1.00 16.53 ? 254 MET B CG 1 ATOM 6345 S SD . MET B 1 254 ? 24.024 31.734 32.957 1.00 21.12 ? 254 MET B SD 1 ATOM 6346 C CE . MET B 1 254 ? 24.652 30.363 33.865 1.00 14.86 ? 254 MET B CE 1 ATOM 6347 N N . VAL B 1 255 ? 20.611 36.172 35.546 1.00 14.38 ? 255 VAL B N 1 ATOM 6348 C CA . VAL B 1 255 ? 20.935 37.527 35.984 1.00 14.21 ? 255 VAL B CA 1 ATOM 6349 C C . VAL B 1 255 ? 20.596 37.714 37.464 1.00 14.31 ? 255 VAL B C 1 ATOM 6350 O O . VAL B 1 255 ? 19.437 37.575 37.855 1.00 14.47 ? 255 VAL B O 1 ATOM 6351 C CB . VAL B 1 255 ? 20.174 38.602 35.144 1.00 14.87 ? 255 VAL B CB 1 ATOM 6352 C CG1 . VAL B 1 255 ? 20.452 40.026 35.659 1.00 12.22 ? 255 VAL B CG1 1 ATOM 6353 C CG2 . VAL B 1 255 ? 20.576 38.516 33.695 1.00 14.08 ? 255 VAL B CG2 1 ATOM 6354 N N . PRO B 1 256 ? 21.611 38.019 38.304 1.00 15.06 ? 256 PRO B N 1 ATOM 6355 C CA . PRO B 1 256 ? 21.397 38.232 39.740 1.00 14.19 ? 256 PRO B CA 1 ATOM 6356 C C . PRO B 1 256 ? 20.595 39.501 39.971 1.00 13.43 ? 256 PRO B C 1 ATOM 6357 O O . PRO B 1 256 ? 20.868 40.540 39.363 1.00 13.11 ? 256 PRO B O 1 ATOM 6358 C CB . PRO B 1 256 ? 22.814 38.375 40.276 1.00 12.81 ? 256 PRO B CB 1 ATOM 6359 C CG . PRO B 1 256 ? 23.580 37.527 39.362 1.00 13.13 ? 256 PRO B CG 1 ATOM 6360 C CD . PRO B 1 256 ? 23.057 37.934 38.030 1.00 13.52 ? 256 PRO B CD 1 ATOM 6361 N N . VAL B 1 257 ? 19.547 39.377 40.778 1.00 13.50 ? 257 VAL B N 1 ATOM 6362 C CA . VAL B 1 257 ? 18.686 40.506 41.089 1.00 13.39 ? 257 VAL B CA 1 ATOM 6363 C C . VAL B 1 257 ? 18.667 40.774 42.585 1.00 13.45 ? 257 VAL B C 1 ATOM 6364 O O . VAL B 1 257 ? 18.996 39.889 43.376 1.00 11.07 ? 257 VAL B O 1 ATOM 6365 C CB . VAL B 1 257 ? 17.213 40.312 40.544 1.00 14.80 ? 257 VAL B CB 1 ATOM 6366 C CG1 . VAL B 1 257 ? 17.212 40.112 39.028 1.00 14.94 ? 257 VAL B CG1 1 ATOM 6367 C CG2 . VAL B 1 257 ? 16.491 39.170 41.237 1.00 12.49 ? 257 VAL B CG2 1 ATOM 6368 N N . ASN B 1 258 ? 18.284 41.995 42.966 1.00 15.08 ? 258 ASN B N 1 ATOM 6369 C CA . ASN B 1 258 ? 18.179 42.380 44.377 1.00 16.08 ? 258 ASN B CA 1 ATOM 6370 C C . ASN B 1 258 ? 17.049 41.548 44.975 1.00 16.66 ? 258 ASN B C 1 ATOM 6371 O O . ASN B 1 258 ? 16.067 41.257 44.280 1.00 14.50 ? 258 ASN B O 1 ATOM 6372 C CB . ASN B 1 258 ? 17.831 43.868 44.524 1.00 17.18 ? 258 ASN B CB 1 ATOM 6373 C CG . ASN B 1 258 ? 18.901 44.785 43.962 1.00 17.68 ? 258 ASN B CG 1 ATOM 6374 O OD1 . ASN B 1 258 ? 20.092 44.592 44.200 1.00 18.35 ? 258 ASN B OD1 1 ATOM 6375 N ND2 . ASN B 1 258 ? 18.476 45.794 43.214 1.00 20.41 ? 258 ASN B ND2 1 ATOM 6376 N N . ALA B 1 259 ? 17.222 41.139 46.233 1.00 16.45 ? 259 ALA B N 1 ATOM 6377 C CA . ALA B 1 259 ? 16.250 40.327 46.971 1.00 17.14 ? 259 ALA B CA 1 ATOM 6378 C C . ALA B 1 259 ? 14.808 40.810 46.821 1.00 17.28 ? 259 ALA B C 1 ATOM 6379 O O . ALA B 1 259 ? 14.514 41.987 47.041 1.00 16.55 ? 259 ALA B O 1 ATOM 6380 C CB . ALA B 1 259 ? 16.630 40.272 48.440 1.00 17.74 ? 259 ALA B CB 1 ATOM 6381 N N . MET B 1 260 ? 13.946 39.914 46.342 1.00 17.67 ? 260 MET B N 1 ATOM 6382 C CA . MET B 1 260 ? 12.535 40.225 46.142 1.00 18.48 ? 260 MET B CA 1 ATOM 6383 C C . MET B 1 260 ? 11.674 39.083 46.674 1.00 18.39 ? 260 MET B C 1 ATOM 6384 O O . MET B 1 260 ? 11.580 38.015 46.062 1.00 15.96 ? 260 MET B O 1 ATOM 6385 C CB . MET B 1 260 ? 12.244 40.485 44.661 1.00 18.97 ? 260 MET B CB 1 ATOM 6386 C CG . MET B 1 260 ? 10.877 41.104 44.396 1.00 20.91 ? 260 MET B CG 1 ATOM 6387 S SD . MET B 1 260 ? 10.492 41.133 42.653 1.00 23.57 ? 260 MET B SD 1 ATOM 6388 C CE . MET B 1 260 ? 9.996 39.445 42.400 1.00 22.58 ? 260 MET B CE 1 ATOM 6389 N N . THR B 1 261 ? 11.042 39.335 47.818 1.00 18.18 ? 261 THR B N 1 ATOM 6390 C CA . THR B 1 261 ? 10.193 38.356 48.494 1.00 18.36 ? 261 THR B CA 1 ATOM 6391 C C . THR B 1 261 ? 8.767 38.328 47.943 1.00 18.01 ? 261 THR B C 1 ATOM 6392 O O . THR B 1 261 ? 8.107 39.366 47.848 1.00 19.93 ? 261 THR B O 1 ATOM 6393 C CB . THR B 1 261 ? 10.215 38.594 50.026 1.00 18.28 ? 261 THR B CB 1 ATOM 6394 O OG1 . THR B 1 261 ? 11.576 38.646 50.467 1.00 16.83 ? 261 THR B OG1 1 ATOM 6395 C CG2 . THR B 1 261 ? 9.534 37.461 50.769 1.00 15.80 ? 261 THR B CG2 1 ATOM 6396 N N . VAL B 1 262 ? 8.334 37.134 47.532 1.00 16.46 ? 262 VAL B N 1 ATOM 6397 C CA . VAL B 1 262 ? 7.000 36.892 46.966 1.00 17.41 ? 262 VAL B CA 1 ATOM 6398 C C . VAL B 1 262 ? 6.352 35.625 47.538 1.00 17.01 ? 262 VAL B C 1 ATOM 6399 O O . VAL B 1 262 ? 7.029 34.786 48.131 1.00 16.45 ? 262 VAL B O 1 ATOM 6400 C CB . VAL B 1 262 ? 7.039 36.740 45.402 1.00 17.34 ? 262 VAL B CB 1 ATOM 6401 C CG1 . VAL B 1 262 ? 7.291 38.081 44.726 1.00 18.59 ? 262 VAL B CG1 1 ATOM 6402 C CG2 . VAL B 1 262 ? 8.103 35.721 44.981 1.00 18.19 ? 262 VAL B CG2 1 ATOM 6403 N N . ASP B 1 263 ? 5.045 35.484 47.314 1.00 17.56 ? 263 ASP B N 1 ATOM 6404 C CA . ASP B 1 263 ? 4.279 34.322 47.770 1.00 17.86 ? 263 ASP B CA 1 ATOM 6405 C C . ASP B 1 263 ? 4.260 33.262 46.671 1.00 16.53 ? 263 ASP B C 1 ATOM 6406 O O . ASP B 1 263 ? 4.196 32.062 46.949 1.00 15.50 ? 263 ASP B O 1 ATOM 6407 C CB . ASP B 1 263 ? 2.844 34.728 48.123 1.00 20.79 ? 263 ASP B CB 1 ATOM 6408 C CG . ASP B 1 263 ? 2.781 35.763 49.240 1.00 24.10 ? 263 ASP B CG 1 ATOM 6409 O OD1 . ASP B 1 263 ? 3.548 35.644 50.222 1.00 25.08 ? 263 ASP B OD1 1 ATOM 6410 O OD2 . ASP B 1 263 ? 1.959 36.697 49.131 1.00 25.01 ? 263 ASP B OD2 1 ATOM 6411 N N . SER B 1 264 ? 4.303 33.731 45.424 1.00 16.17 ? 264 SER B N 1 ATOM 6412 C CA . SER B 1 264 ? 4.300 32.870 44.244 1.00 15.27 ? 264 SER B CA 1 ATOM 6413 C C . SER B 1 264 ? 5.090 33.477 43.089 1.00 14.84 ? 264 SER B C 1 ATOM 6414 O O . SER B 1 264 ? 5.313 34.690 43.041 1.00 13.95 ? 264 SER B O 1 ATOM 6415 C CB . SER B 1 264 ? 2.872 32.552 43.791 1.00 15.55 ? 264 SER B CB 1 ATOM 6416 O OG . SER B 1 264 ? 2.156 33.722 43.456 1.00 15.67 ? 264 SER B OG 1 ATOM 6417 N N . LEU B 1 265 ? 5.519 32.616 42.172 1.00 13.20 ? 265 LEU B N 1 ATOM 6418 C CA . LEU B 1 265 ? 6.292 33.023 41.009 1.00 13.45 ? 265 LEU B CA 1 ATOM 6419 C C . LEU B 1 265 ? 5.790 32.398 39.738 1.00 13.45 ? 265 LEU B C 1 ATOM 6420 O O . LEU B 1 265 ? 5.427 31.225 39.718 1.00 14.75 ? 265 LEU B O 1 ATOM 6421 C CB . LEU B 1 265 ? 7.749 32.595 41.151 1.00 14.82 ? 265 LEU B CB 1 ATOM 6422 C CG . LEU B 1 265 ? 8.756 33.455 41.885 1.00 15.99 ? 265 LEU B CG 1 ATOM 6423 C CD1 . LEU B 1 265 ? 10.010 32.640 42.061 1.00 16.80 ? 265 LEU B CD1 1 ATOM 6424 C CD2 . LEU B 1 265 ? 9.022 34.736 41.115 1.00 16.58 ? 265 LEU B CD2 1 ATOM 6425 N N . PHE B 1 266 ? 5.830 33.178 38.666 1.00 13.50 ? 266 PHE B N 1 ATOM 6426 C CA . PHE B 1 266 ? 5.437 32.695 37.358 1.00 12.36 ? 266 PHE B CA 1 ATOM 6427 C C . PHE B 1 266 ? 6.704 32.368 36.575 1.00 12.09 ? 266 PHE B C 1 ATOM 6428 O O . PHE B 1 266 ? 7.576 33.222 36.411 1.00 10.90 ? 266 PHE B O 1 ATOM 6429 C CB . PHE B 1 266 ? 4.633 33.750 36.589 1.00 11.18 ? 266 PHE B CB 1 ATOM 6430 C CG . PHE B 1 266 ? 4.241 33.320 35.196 1.00 11.31 ? 266 PHE B CG 1 ATOM 6431 C CD1 . PHE B 1 266 ? 3.151 32.459 34.998 1.00 9.42 ? 266 PHE B CD1 1 ATOM 6432 C CD2 . PHE B 1 266 ? 4.991 33.742 34.077 1.00 10.15 ? 266 PHE B CD2 1 ATOM 6433 C CE1 . PHE B 1 266 ? 2.813 32.022 33.706 1.00 10.90 ? 266 PHE B CE1 1 ATOM 6434 C CE2 . PHE B 1 266 ? 4.667 33.317 32.781 1.00 9.13 ? 266 PHE B CE2 1 ATOM 6435 C CZ . PHE B 1 266 ? 3.583 32.458 32.592 1.00 8.88 ? 266 PHE B CZ 1 ATOM 6436 N N . LEU B 1 267 ? 6.758 31.152 36.042 1.00 11.54 ? 267 LEU B N 1 ATOM 6437 C CA . LEU B 1 267 ? 7.879 30.733 35.220 1.00 12.42 ? 267 LEU B CA 1 ATOM 6438 C C . LEU B 1 267 ? 7.397 30.403 33.826 1.00 10.33 ? 267 LEU B C 1 ATOM 6439 O O . LEU B 1 267 ? 6.660 29.437 33.623 1.00 9.86 ? 267 LEU B O 1 ATOM 6440 C CB . LEU B 1 267 ? 8.611 29.517 35.801 1.00 12.91 ? 267 LEU B CB 1 ATOM 6441 C CG . LEU B 1 267 ? 9.572 29.760 36.956 1.00 12.60 ? 267 LEU B CG 1 ATOM 6442 C CD1 . LEU B 1 267 ? 8.864 29.476 38.257 1.00 15.05 ? 267 LEU B CD1 1 ATOM 6443 C CD2 . LEU B 1 267 ? 10.796 28.883 36.817 1.00 12.32 ? 267 LEU B CD2 1 ATOM 6444 N N . ALA B 1 268 ? 7.786 31.243 32.871 1.00 9.41 ? 268 ALA B N 1 ATOM 6445 C CA . ALA B 1 268 ? 7.467 31.022 31.463 1.00 8.50 ? 268 ALA B CA 1 ATOM 6446 C C . ALA B 1 268 ? 8.380 29.904 30.978 1.00 8.78 ? 268 ALA B C 1 ATOM 6447 O O . ALA B 1 268 ? 9.318 29.525 31.688 1.00 8.63 ? 268 ALA B O 1 ATOM 6448 C CB . ALA B 1 268 ? 7.736 32.280 30.658 1.00 9.09 ? 268 ALA B CB 1 ATOM 6449 N N . VAL B 1 269 ? 8.106 29.363 29.792 1.00 9.43 ? 269 VAL B N 1 ATOM 6450 C CA . VAL B 1 269 ? 8.952 28.308 29.228 1.00 9.97 ? 269 VAL B CA 1 ATOM 6451 C C . VAL B 1 269 ? 10.365 28.873 29.027 1.00 10.57 ? 269 VAL B C 1 ATOM 6452 O O . VAL B 1 269 ? 10.539 29.942 28.434 1.00 10.72 ? 269 VAL B O 1 ATOM 6453 C CB . VAL B 1 269 ? 8.388 27.783 27.887 1.00 11.41 ? 269 VAL B CB 1 ATOM 6454 C CG1 . VAL B 1 269 ? 9.301 26.728 27.285 1.00 10.33 ? 269 VAL B CG1 1 ATOM 6455 C CG2 . VAL B 1 269 ? 7.041 27.177 28.114 1.00 9.79 ? 269 VAL B CG2 1 ATOM 6456 N N . GLY B 1 270 ? 11.339 28.197 29.625 1.00 10.77 ? 270 GLY B N 1 ATOM 6457 C CA . GLY B 1 270 ? 12.718 28.628 29.513 1.00 11.52 ? 270 GLY B CA 1 ATOM 6458 C C . GLY B 1 270 ? 13.202 29.512 30.640 1.00 10.87 ? 270 GLY B C 1 ATOM 6459 O O . GLY B 1 270 ? 14.408 29.704 30.789 1.00 11.81 ? 270 GLY B O 1 ATOM 6460 N N . GLN B 1 271 ? 12.269 30.038 31.434 1.00 8.76 ? 271 GLN B N 1 ATOM 6461 C CA . GLN B 1 271 ? 12.610 30.908 32.557 1.00 9.73 ? 271 GLN B CA 1 ATOM 6462 C C . GLN B 1 271 ? 13.119 30.163 33.772 1.00 10.50 ? 271 GLN B C 1 ATOM 6463 O O . GLN B 1 271 ? 12.826 28.977 33.966 1.00 11.74 ? 271 GLN B O 1 ATOM 6464 C CB . GLN B 1 271 ? 11.430 31.790 32.975 1.00 8.99 ? 271 GLN B CB 1 ATOM 6465 C CG . GLN B 1 271 ? 11.290 33.037 32.138 1.00 8.83 ? 271 GLN B CG 1 ATOM 6466 C CD . GLN B 1 271 ? 10.261 34.011 32.659 1.00 9.35 ? 271 GLN B CD 1 ATOM 6467 O OE1 . GLN B 1 271 ? 9.345 33.645 33.397 1.00 9.02 ? 271 GLN B OE1 1 ATOM 6468 N NE2 . GLN B 1 271 ? 10.397 35.269 32.256 1.00 7.73 ? 271 GLN B NE2 1 ATOM 6469 N N . ARG B 1 272 ? 13.979 30.850 34.517 1.00 10.05 ? 272 ARG B N 1 ATOM 6470 C CA . ARG B 1 272 ? 14.559 30.332 35.746 1.00 12.06 ? 272 ARG B CA 1 ATOM 6471 C C . ARG B 1 272 ? 14.470 31.385 36.835 1.00 12.05 ? 272 ARG B C 1 ATOM 6472 O O . ARG B 1 272 ? 14.409 32.590 36.558 1.00 12.16 ? 272 ARG B O 1 ATOM 6473 C CB . ARG B 1 272 ? 16.042 29.962 35.587 1.00 13.30 ? 272 ARG B CB 1 ATOM 6474 C CG . ARG B 1 272 ? 16.365 28.768 34.721 1.00 13.30 ? 272 ARG B CG 1 ATOM 6475 C CD . ARG B 1 272 ? 16.517 29.111 33.259 1.00 11.34 ? 272 ARG B CD 1 ATOM 6476 N NE . ARG B 1 272 ? 17.719 29.896 32.999 1.00 12.24 ? 272 ARG B NE 1 ATOM 6477 C CZ . ARG B 1 272 ? 17.861 30.748 31.991 1.00 12.23 ? 272 ARG B CZ 1 ATOM 6478 N NH1 . ARG B 1 272 ? 16.870 30.953 31.130 1.00 13.02 ? 272 ARG B NH1 1 ATOM 6479 N NH2 . ARG B 1 272 ? 19.010 31.392 31.835 1.00 9.38 ? 272 ARG B NH2 1 ATOM 6480 N N . TYR B 1 273 ? 14.413 30.909 38.073 1.00 12.10 ? 273 TYR B N 1 ATOM 6481 C CA . TYR B 1 273 ? 14.391 31.759 39.253 1.00 11.97 ? 273 TYR B CA 1 ATOM 6482 C C . TYR B 1 273 ? 15.173 31.073 40.355 1.00 12.30 ? 273 TYR B C 1 ATOM 6483 O O . TYR B 1 273 ? 14.924 29.909 40.662 1.00 11.39 ? 273 TYR B O 1 ATOM 6484 C CB . TYR B 1 273 ? 12.966 32.041 39.748 1.00 12.12 ? 273 TYR B CB 1 ATOM 6485 C CG . TYR B 1 273 ? 12.261 33.178 39.040 1.00 11.48 ? 273 TYR B CG 1 ATOM 6486 C CD1 . TYR B 1 273 ? 12.737 34.502 39.134 1.00 11.90 ? 273 TYR B CD1 1 ATOM 6487 C CD2 . TYR B 1 273 ? 11.121 32.937 38.256 1.00 11.61 ? 273 TYR B CD2 1 ATOM 6488 C CE1 . TYR B 1 273 ? 12.085 35.572 38.456 1.00 13.05 ? 273 TYR B CE1 1 ATOM 6489 C CE2 . TYR B 1 273 ? 10.458 33.990 37.571 1.00 12.17 ? 273 TYR B CE2 1 ATOM 6490 C CZ . TYR B 1 273 ? 10.945 35.300 37.680 1.00 11.66 ? 273 TYR B CZ 1 ATOM 6491 O OH . TYR B 1 273 ? 10.292 36.322 37.035 1.00 11.52 ? 273 TYR B OH 1 ATOM 6492 N N . ASP B 1 274 ? 16.185 31.764 40.873 1.00 12.77 ? 274 ASP B N 1 ATOM 6493 C CA . ASP B 1 274 ? 16.966 31.251 41.992 1.00 14.56 ? 274 ASP B CA 1 ATOM 6494 C C . ASP B 1 274 ? 16.335 31.901 43.203 1.00 14.20 ? 274 ASP B C 1 ATOM 6495 O O . ASP B 1 274 ? 16.230 33.131 43.265 1.00 13.44 ? 274 ASP B O 1 ATOM 6496 C CB . ASP B 1 274 ? 18.440 31.642 41.894 1.00 17.89 ? 274 ASP B CB 1 ATOM 6497 C CG . ASP B 1 274 ? 19.164 30.927 40.776 1.00 20.98 ? 274 ASP B CG 1 ATOM 6498 O OD1 . ASP B 1 274 ? 18.552 30.070 40.107 1.00 25.50 ? 274 ASP B OD1 1 ATOM 6499 O OD2 . ASP B 1 274 ? 20.353 31.221 40.566 1.00 24.71 ? 274 ASP B OD2 1 ATOM 6500 N N . VAL B 1 275 ? 15.797 31.075 44.097 1.00 13.39 ? 275 VAL B N 1 ATOM 6501 C CA . VAL B 1 275 ? 15.154 31.589 45.300 1.00 13.35 ? 275 VAL B CA 1 ATOM 6502 C C . VAL B 1 275 ? 15.817 31.136 46.585 1.00 13.13 ? 275 VAL B C 1 ATOM 6503 O O . VAL B 1 275 ? 16.493 30.118 46.609 1.00 13.57 ? 275 VAL B O 1 ATOM 6504 C CB . VAL B 1 275 ? 13.630 31.236 45.375 1.00 12.87 ? 275 VAL B CB 1 ATOM 6505 C CG1 . VAL B 1 275 ? 12.876 31.892 44.249 1.00 11.69 ? 275 VAL B CG1 1 ATOM 6506 C CG2 . VAL B 1 275 ? 13.397 29.731 45.375 1.00 13.40 ? 275 VAL B CG2 1 ATOM 6507 N N . VAL B 1 276 ? 15.644 31.935 47.634 1.00 14.07 ? 276 VAL B N 1 ATOM 6508 C CA . VAL B 1 276 ? 16.156 31.619 48.960 1.00 16.06 ? 276 VAL B CA 1 ATOM 6509 C C . VAL B 1 276 ? 14.917 31.358 49.822 1.00 16.31 ? 276 VAL B C 1 ATOM 6510 O O . VAL B 1 276 ? 14.053 32.225 49.969 1.00 16.39 ? 276 VAL B O 1 ATOM 6511 C CB . VAL B 1 276 ? 17.058 32.757 49.546 1.00 15.91 ? 276 VAL B CB 1 ATOM 6512 C CG1 . VAL B 1 276 ? 17.409 32.482 51.015 1.00 16.03 ? 276 VAL B CG1 1 ATOM 6513 C CG2 . VAL B 1 276 ? 18.354 32.844 48.755 1.00 12.52 ? 276 VAL B CG2 1 ATOM 6514 N N . ILE B 1 277 ? 14.788 30.113 50.273 1.00 17.70 ? 277 ILE B N 1 ATOM 6515 C CA . ILE B 1 277 ? 13.673 29.693 51.116 1.00 17.13 ? 277 ILE B CA 1 ATOM 6516 C C . ILE B 1 277 ? 14.194 29.471 52.535 1.00 19.14 ? 277 ILE B C 1 ATOM 6517 O O . ILE B 1 277 ? 15.107 28.672 52.757 1.00 17.22 ? 277 ILE B O 1 ATOM 6518 C CB . ILE B 1 277 ? 12.990 28.390 50.567 1.00 16.58 ? 277 ILE B CB 1 ATOM 6519 C CG1 . ILE B 1 277 ? 12.340 28.679 49.204 1.00 16.53 ? 277 ILE B CG1 1 ATOM 6520 C CG2 . ILE B 1 277 ? 11.934 27.851 51.560 1.00 15.53 ? 277 ILE B CG2 1 ATOM 6521 C CD1 . ILE B 1 277 ? 11.833 27.456 48.467 1.00 16.92 ? 277 ILE B CD1 1 ATOM 6522 N N . ASP B 1 278 ? 13.617 30.214 53.475 1.00 21.16 ? 278 ASP B N 1 ATOM 6523 C CA . ASP B 1 278 ? 13.970 30.112 54.885 1.00 22.30 ? 278 ASP B CA 1 ATOM 6524 C C . ASP B 1 278 ? 13.083 29.059 55.523 1.00 22.22 ? 278 ASP B C 1 ATOM 6525 O O . ASP B 1 278 ? 11.851 29.119 55.408 1.00 23.07 ? 278 ASP B O 1 ATOM 6526 C CB . ASP B 1 278 ? 13.763 31.453 55.602 1.00 25.78 ? 278 ASP B CB 1 ATOM 6527 C CG . ASP B 1 278 ? 14.660 32.561 55.067 1.00 27.65 ? 278 ASP B CG 1 ATOM 6528 O OD1 . ASP B 1 278 ? 15.664 32.262 54.384 1.00 28.06 ? 278 ASP B OD1 1 ATOM 6529 O OD2 . ASP B 1 278 ? 14.358 33.743 55.341 1.00 30.62 ? 278 ASP B OD2 1 ATOM 6530 N N . ALA B 1 279 ? 13.711 28.070 56.154 1.00 20.56 ? 279 ALA B N 1 ATOM 6531 C CA . ALA B 1 279 ? 12.986 27.002 56.836 1.00 21.26 ? 279 ALA B CA 1 ATOM 6532 C C . ALA B 1 279 ? 12.651 27.512 58.245 1.00 21.44 ? 279 ALA B C 1 ATOM 6533 O O . ALA B 1 279 ? 13.089 26.962 59.260 1.00 19.72 ? 279 ALA B O 1 ATOM 6534 C CB . ALA B 1 279 ? 13.828 25.733 56.882 1.00 18.41 ? 279 ALA B CB 1 ATOM 6535 N N . SER B 1 280 ? 11.845 28.572 58.264 1.00 22.74 ? 280 SER B N 1 ATOM 6536 C CA . SER B 1 280 ? 11.437 29.266 59.478 1.00 23.34 ? 280 SER B CA 1 ATOM 6537 C C . SER B 1 280 ? 10.056 28.913 60.024 1.00 24.23 ? 280 SER B C 1 ATOM 6538 O O . SER B 1 280 ? 9.611 29.499 61.010 1.00 23.63 ? 280 SER B O 1 ATOM 6539 C CB . SER B 1 280 ? 11.534 30.772 59.237 1.00 22.71 ? 280 SER B CB 1 ATOM 6540 O OG . SER B 1 280 ? 10.653 31.192 58.209 1.00 24.66 ? 280 SER B OG 1 ATOM 6541 N N . ARG B 1 281 ? 9.379 27.964 59.383 1.00 26.54 ? 281 ARG B N 1 ATOM 6542 C CA . ARG B 1 281 ? 8.044 27.550 59.815 1.00 28.05 ? 281 ARG B CA 1 ATOM 6543 C C . ARG B 1 281 ? 8.111 26.326 60.724 1.00 28.68 ? 281 ARG B C 1 ATOM 6544 O O . ARG B 1 281 ? 9.200 25.805 60.991 1.00 27.76 ? 281 ARG B O 1 ATOM 6545 C CB . ARG B 1 281 ? 7.145 27.274 58.600 1.00 29.10 ? 281 ARG B CB 1 ATOM 6546 C CG . ARG B 1 281 ? 7.133 28.385 57.539 1.00 31.28 ? 281 ARG B CG 1 ATOM 6547 C CD . ARG B 1 281 ? 6.696 29.734 58.069 1.00 32.98 ? 281 ARG B CD 1 ATOM 6548 N NE . ARG B 1 281 ? 5.312 29.706 58.525 1.00 36.77 ? 281 ARG B NE 1 ATOM 6549 C CZ . ARG B 1 281 ? 4.755 30.628 59.302 1.00 37.12 ? 281 ARG B CZ 1 ATOM 6550 N NH1 . ARG B 1 281 ? 5.464 31.668 59.723 1.00 36.94 ? 281 ARG B NH1 1 ATOM 6551 N NH2 . ARG B 1 281 ? 3.482 30.510 59.656 1.00 37.11 ? 281 ARG B NH2 1 ATOM 6552 N N . ALA B 1 282 ? 6.946 25.878 61.197 1.00 28.67 ? 282 ALA B N 1 ATOM 6553 C CA . ALA B 1 282 ? 6.836 24.714 62.080 1.00 29.97 ? 282 ALA B CA 1 ATOM 6554 C C . ALA B 1 282 ? 7.281 23.434 61.362 1.00 30.63 ? 282 ALA B C 1 ATOM 6555 O O . ALA B 1 282 ? 6.965 23.257 60.181 1.00 29.77 ? 282 ALA B O 1 ATOM 6556 C CB . ALA B 1 282 ? 5.393 24.568 62.578 1.00 30.07 ? 282 ALA B CB 1 ATOM 6557 N N . PRO B 1 283 ? 8.106 22.582 62.028 1.00 31.50 ? 283 PRO B N 1 ATOM 6558 C CA . PRO B 1 283 ? 8.587 21.325 61.434 1.00 30.78 ? 283 PRO B CA 1 ATOM 6559 C C . PRO B 1 283 ? 7.450 20.423 60.951 1.00 30.56 ? 283 PRO B C 1 ATOM 6560 O O . PRO B 1 283 ? 6.716 19.835 61.751 1.00 30.36 ? 283 PRO B O 1 ATOM 6561 C CB . PRO B 1 283 ? 9.397 20.703 62.572 1.00 32.14 ? 283 PRO B CB 1 ATOM 6562 C CG . PRO B 1 283 ? 10.001 21.900 63.213 1.00 32.89 ? 283 PRO B CG 1 ATOM 6563 C CD . PRO B 1 283 ? 8.806 22.831 63.306 1.00 32.39 ? 283 PRO B CD 1 ATOM 6564 N N . ASP B 1 284 ? 7.296 20.374 59.626 1.00 28.47 ? 284 ASP B N 1 ATOM 6565 C CA . ASP B 1 284 ? 6.236 19.609 58.967 1.00 27.98 ? 284 ASP B CA 1 ATOM 6566 C C . ASP B 1 284 ? 6.614 19.359 57.499 1.00 27.89 ? 284 ASP B C 1 ATOM 6567 O O . ASP B 1 284 ? 7.702 19.723 57.044 1.00 28.54 ? 284 ASP B O 1 ATOM 6568 C CB . ASP B 1 284 ? 4.933 20.439 59.030 1.00 28.18 ? 284 ASP B CB 1 ATOM 6569 C CG . ASP B 1 284 ? 3.664 19.599 58.981 1.00 27.26 ? 284 ASP B CG 1 ATOM 6570 O OD1 . ASP B 1 284 ? 3.702 18.413 58.588 1.00 27.57 ? 284 ASP B OD1 1 ATOM 6571 O OD2 . ASP B 1 284 ? 2.606 20.158 59.333 1.00 28.50 ? 284 ASP B OD2 1 ATOM 6572 N N . ASN B 1 285 ? 5.708 18.699 56.785 1.00 27.88 ? 285 ASN B N 1 ATOM 6573 C CA . ASN B 1 285 ? 5.851 18.406 55.365 1.00 27.03 ? 285 ASN B CA 1 ATOM 6574 C C . ASN B 1 285 ? 4.923 19.407 54.681 1.00 26.28 ? 285 ASN B C 1 ATOM 6575 O O . ASN B 1 285 ? 3.754 19.526 55.060 1.00 26.03 ? 285 ASN B O 1 ATOM 6576 C CB . ASN B 1 285 ? 5.386 16.980 55.064 1.00 27.88 ? 285 ASN B CB 1 ATOM 6577 C CG . ASN B 1 285 ? 6.210 15.932 55.768 1.00 29.01 ? 285 ASN B CG 1 ATOM 6578 O OD1 . ASN B 1 285 ? 7.385 15.746 55.465 1.00 29.55 ? 285 ASN B OD1 1 ATOM 6579 N ND2 . ASN B 1 285 ? 5.593 15.229 56.708 1.00 29.43 ? 285 ASN B ND2 1 ATOM 6580 N N . TYR B 1 286 ? 5.450 20.157 53.713 1.00 24.59 ? 286 TYR B N 1 ATOM 6581 C CA . TYR B 1 286 ? 4.660 21.161 52.995 1.00 23.02 ? 286 TYR B CA 1 ATOM 6582 C C . TYR B 1 286 ? 4.643 20.920 51.490 1.00 21.23 ? 286 TYR B C 1 ATOM 6583 O O . TYR B 1 286 ? 5.639 20.466 50.922 1.00 21.03 ? 286 TYR B O 1 ATOM 6584 C CB . TYR B 1 286 ? 5.194 22.571 53.271 1.00 23.87 ? 286 TYR B CB 1 ATOM 6585 C CG . TYR B 1 286 ? 5.099 23.018 54.712 1.00 24.63 ? 286 TYR B CG 1 ATOM 6586 C CD1 . TYR B 1 286 ? 3.944 23.668 55.195 1.00 24.97 ? 286 TYR B CD1 1 ATOM 6587 C CD2 . TYR B 1 286 ? 6.177 22.827 55.600 1.00 24.60 ? 286 TYR B CD2 1 ATOM 6588 C CE1 . TYR B 1 286 ? 3.865 24.127 56.543 1.00 25.57 ? 286 TYR B CE1 1 ATOM 6589 C CE2 . TYR B 1 286 ? 6.113 23.285 56.948 1.00 25.89 ? 286 TYR B CE2 1 ATOM 6590 C CZ . TYR B 1 286 ? 4.956 23.934 57.406 1.00 26.89 ? 286 TYR B CZ 1 ATOM 6591 O OH . TYR B 1 286 ? 4.903 24.400 58.698 1.00 27.27 ? 286 TYR B OH 1 ATOM 6592 N N . TRP B 1 287 ? 3.501 21.196 50.856 1.00 19.84 ? 287 TRP B N 1 ATOM 6593 C CA . TRP B 1 287 ? 3.364 21.037 49.404 1.00 18.28 ? 287 TRP B CA 1 ATOM 6594 C C . TRP B 1 287 ? 3.987 22.200 48.646 1.00 17.86 ? 287 TRP B C 1 ATOM 6595 O O . TRP B 1 287 ? 3.862 23.361 49.053 1.00 17.11 ? 287 TRP B O 1 ATOM 6596 C CB . TRP B 1 287 ? 1.894 20.983 48.938 1.00 17.47 ? 287 TRP B CB 1 ATOM 6597 C CG . TRP B 1 287 ? 1.038 19.801 49.324 1.00 16.09 ? 287 TRP B CG 1 ATOM 6598 C CD1 . TRP B 1 287 ? -0.116 19.854 50.055 1.00 16.87 ? 287 TRP B CD1 1 ATOM 6599 C CD2 . TRP B 1 287 ? 1.195 18.426 48.928 1.00 16.79 ? 287 TRP B CD2 1 ATOM 6600 N NE1 . TRP B 1 287 ? -0.692 18.611 50.142 1.00 18.36 ? 287 TRP B NE1 1 ATOM 6601 C CE2 . TRP B 1 287 ? 0.084 17.710 49.463 1.00 17.87 ? 287 TRP B CE2 1 ATOM 6602 C CE3 . TRP B 1 287 ? 2.161 17.721 48.177 1.00 16.99 ? 287 TRP B CE3 1 ATOM 6603 C CZ2 . TRP B 1 287 ? -0.092 16.319 49.271 1.00 17.61 ? 287 TRP B CZ2 1 ATOM 6604 C CZ3 . TRP B 1 287 ? 1.990 16.325 47.981 1.00 17.91 ? 287 TRP B CZ3 1 ATOM 6605 C CH2 . TRP B 1 287 ? 0.866 15.645 48.532 1.00 17.87 ? 287 TRP B CH2 1 ATOM 6606 N N . PHE B 1 288 ? 4.699 21.862 47.574 1.00 17.21 ? 288 PHE B N 1 ATOM 6607 C CA . PHE B 1 288 ? 5.284 22.842 46.665 1.00 16.76 ? 288 PHE B CA 1 ATOM 6608 C C . PHE B 1 288 ? 4.319 22.641 45.513 1.00 17.24 ? 288 PHE B C 1 ATOM 6609 O O . PHE B 1 288 ? 4.337 21.596 44.867 1.00 18.02 ? 288 PHE B O 1 ATOM 6610 C CB . PHE B 1 288 ? 6.699 22.449 46.240 1.00 17.35 ? 288 PHE B CB 1 ATOM 6611 C CG . PHE B 1 288 ? 7.338 23.396 45.244 1.00 16.10 ? 288 PHE B CG 1 ATOM 6612 C CD1 . PHE B 1 288 ? 8.094 24.496 45.690 1.00 17.10 ? 288 PHE B CD1 1 ATOM 6613 C CD2 . PHE B 1 288 ? 7.234 23.159 43.855 1.00 16.94 ? 288 PHE B CD2 1 ATOM 6614 C CE1 . PHE B 1 288 ? 8.752 25.354 44.771 1.00 16.96 ? 288 PHE B CE1 1 ATOM 6615 C CE2 . PHE B 1 288 ? 7.881 24.002 42.920 1.00 17.81 ? 288 PHE B CE2 1 ATOM 6616 C CZ . PHE B 1 288 ? 8.646 25.104 43.380 1.00 16.34 ? 288 PHE B CZ 1 ATOM 6617 N N . ASN B 1 289 ? 3.469 23.629 45.281 1.00 15.70 ? 289 ASN B N 1 ATOM 6618 C CA . ASN B 1 289 ? 2.466 23.530 44.236 1.00 15.74 ? 289 ASN B CA 1 ATOM 6619 C C . ASN B 1 289 ? 2.783 24.162 42.908 1.00 15.46 ? 289 ASN B C 1 ATOM 6620 O O . ASN B 1 289 ? 3.310 25.273 42.844 1.00 14.20 ? 289 ASN B O 1 ATOM 6621 C CB . ASN B 1 289 ? 1.147 24.101 44.737 1.00 17.15 ? 289 ASN B CB 1 ATOM 6622 C CG . ASN B 1 289 ? 0.507 23.229 45.774 1.00 17.30 ? 289 ASN B CG 1 ATOM 6623 O OD1 . ASN B 1 289 ? 0.626 23.477 46.976 1.00 17.78 ? 289 ASN B OD1 1 ATOM 6624 N ND2 . ASN B 1 289 ? -0.195 22.213 45.286 1.00 17.93 ? 289 ASN B ND2 1 ATOM 6625 N N . VAL B 1 290 ? 2.449 23.424 41.854 1.00 14.01 ? 290 VAL B N 1 ATOM 6626 C CA . VAL B 1 290 ? 2.592 23.881 40.481 1.00 12.96 ? 290 VAL B CA 1 ATOM 6627 C C . VAL B 1 290 ? 1.141 24.109 40.054 1.00 13.14 ? 290 VAL B C 1 ATOM 6628 O O . VAL B 1 290 ? 0.323 23.181 40.083 1.00 12.85 ? 290 VAL B O 1 ATOM 6629 C CB . VAL B 1 290 ? 3.292 22.827 39.581 1.00 13.31 ? 290 VAL B CB 1 ATOM 6630 C CG1 . VAL B 1 290 ? 3.050 23.117 38.109 1.00 13.13 ? 290 VAL B CG1 1 ATOM 6631 C CG2 . VAL B 1 290 ? 4.786 22.822 39.850 1.00 12.11 ? 290 VAL B CG2 1 ATOM 6632 N N . THR B 1 291 ? 0.811 25.369 39.779 1.00 12.46 ? 291 THR B N 1 ATOM 6633 C CA . THR B 1 291 ? -0.539 25.753 39.359 1.00 13.05 ? 291 THR B CA 1 ATOM 6634 C C . THR B 1 291 ? -0.513 26.515 38.040 1.00 13.20 ? 291 THR B C 1 ATOM 6635 O O . THR B 1 291 ? 0.554 26.906 37.548 1.00 12.39 ? 291 THR B O 1 ATOM 6636 C CB . THR B 1 291 ? -1.263 26.623 40.428 1.00 12.52 ? 291 THR B CB 1 ATOM 6637 O OG1 . THR B 1 291 ? -0.443 27.742 40.773 1.00 11.29 ? 291 THR B OG1 1 ATOM 6638 C CG2 . THR B 1 291 ? -1.574 25.814 41.685 1.00 12.77 ? 291 THR B CG2 1 ATOM 6639 N N . PHE B 1 292 ? -1.693 26.680 37.450 1.00 13.08 ? 292 PHE B N 1 ATOM 6640 C CA . PHE B 1 292 ? -1.840 27.385 36.188 1.00 13.85 ? 292 PHE B CA 1 ATOM 6641 C C . PHE B 1 292 ? -2.771 28.570 36.322 1.00 15.72 ? 292 PHE B C 1 ATOM 6642 O O . PHE B 1 292 ? -3.768 28.528 37.048 1.00 15.09 ? 292 PHE B O 1 ATOM 6643 C CB . PHE B 1 292 ? -2.357 26.441 35.097 1.00 14.04 ? 292 PHE B CB 1 ATOM 6644 C CG . PHE B 1 292 ? -1.410 25.327 34.770 1.00 12.73 ? 292 PHE B CG 1 ATOM 6645 C CD1 . PHE B 1 292 ? -0.349 25.536 33.872 1.00 11.76 ? 292 PHE B CD1 1 ATOM 6646 C CD2 . PHE B 1 292 ? -1.549 24.072 35.391 1.00 11.26 ? 292 PHE B CD2 1 ATOM 6647 C CE1 . PHE B 1 292 ? 0.575 24.501 33.590 1.00 12.11 ? 292 PHE B CE1 1 ATOM 6648 C CE2 . PHE B 1 292 ? -0.636 23.024 35.127 1.00 12.92 ? 292 PHE B CE2 1 ATOM 6649 C CZ . PHE B 1 292 ? 0.432 23.236 34.222 1.00 11.61 ? 292 PHE B CZ 1 ATOM 6650 N N . GLY B 1 293 ? -2.404 29.639 35.632 1.00 16.84 ? 293 GLY B N 1 ATOM 6651 C CA . GLY B 1 293 ? -3.198 30.845 35.635 1.00 18.77 ? 293 GLY B CA 1 ATOM 6652 C C . GLY B 1 293 ? -3.399 31.240 34.196 1.00 19.66 ? 293 GLY B C 1 ATOM 6653 O O . GLY B 1 293 ? -3.135 30.442 33.290 1.00 18.68 ? 293 GLY B O 1 ATOM 6654 N N . GLY B 1 294 ? -3.884 32.461 33.985 1.00 19.85 ? 294 GLY B N 1 ATOM 6655 C CA . GLY B 1 294 ? -4.120 32.957 32.641 1.00 21.13 ? 294 GLY B CA 1 ATOM 6656 C C . GLY B 1 294 ? -5.247 32.275 31.912 1.00 21.07 ? 294 GLY B C 1 ATOM 6657 O O . GLY B 1 294 ? -5.376 32.411 30.699 1.00 22.41 ? 294 GLY B O 1 ATOM 6658 N N . GLN B 1 295 ? -6.044 31.523 32.672 1.00 23.43 ? 295 GLN B N 1 ATOM 6659 C CA . GLN B 1 295 ? -7.194 30.770 32.177 1.00 24.59 ? 295 GLN B CA 1 ATOM 6660 C C . GLN B 1 295 ? -6.844 29.858 30.981 1.00 22.91 ? 295 GLN B C 1 ATOM 6661 O O . GLN B 1 295 ? -7.475 29.918 29.919 1.00 22.91 ? 295 GLN B O 1 ATOM 6662 C CB . GLN B 1 295 ? -8.364 31.725 31.854 1.00 28.40 ? 295 GLN B CB 1 ATOM 6663 C CG . GLN B 1 295 ? -8.798 32.710 32.974 1.00 33.75 ? 295 GLN B CG 1 ATOM 6664 C CD . GLN B 1 295 ? -9.408 32.063 34.218 1.00 37.27 ? 295 GLN B CD 1 ATOM 6665 O OE1 . GLN B 1 295 ? -9.875 30.923 34.194 1.00 41.02 ? 295 GLN B OE1 1 ATOM 6666 N NE2 . GLN B 1 295 ? -9.424 32.816 35.312 1.00 39.74 ? 295 GLN B NE2 1 ATOM 6667 N N . ALA B 1 296 ? -5.795 29.050 31.176 1.00 21.29 ? 296 ALA B N 1 ATOM 6668 C CA . ALA B 1 296 ? -5.250 28.096 30.192 1.00 19.27 ? 296 ALA B CA 1 ATOM 6669 C C . ALA B 1 296 ? -4.669 28.683 28.901 1.00 17.63 ? 296 ALA B C 1 ATOM 6670 O O . ALA B 1 296 ? -4.398 27.947 27.944 1.00 18.22 ? 296 ALA B O 1 ATOM 6671 C CB . ALA B 1 296 ? -6.257 27.003 29.863 1.00 20.60 ? 296 ALA B CB 1 ATOM 6672 N N . ALA B 1 297 ? -4.441 29.996 28.893 1.00 13.85 ? 297 ALA B N 1 ATOM 6673 C CA . ALA B 1 297 ? -3.884 30.687 27.730 1.00 13.22 ? 297 ALA B CA 1 ATOM 6674 C C . ALA B 1 297 ? -2.419 30.318 27.507 1.00 12.52 ? 297 ALA B C 1 ATOM 6675 O O . ALA B 1 297 ? -1.905 30.440 26.394 1.00 13.94 ? 297 ALA B O 1 ATOM 6676 C CB . ALA B 1 297 ? -4.032 32.180 27.886 1.00 14.72 ? 297 ALA B CB 1 ATOM 6677 N N . CYS B 1 298 ? -1.758 29.864 28.570 1.00 11.49 ? 298 CYS B N 1 ATOM 6678 C CA . CYS B 1 298 ? -0.364 29.451 28.472 1.00 10.83 ? 298 CYS B CA 1 ATOM 6679 C C . CYS B 1 298 ? -0.109 28.072 29.081 1.00 10.08 ? 298 CYS B C 1 ATOM 6680 O O . CYS B 1 298 ? 0.919 27.822 29.728 1.00 9.70 ? 298 CYS B O 1 ATOM 6681 C CB . CYS B 1 298 ? 0.567 30.533 29.025 1.00 9.86 ? 298 CYS B CB 1 ATOM 6682 S SG . CYS B 1 298 ? 0.333 30.980 30.768 1.00 13.03 ? 298 CYS B SG 1 ATOM 6683 N N . GLY B 1 299 ? -1.081 27.188 28.872 1.00 8.25 ? 299 GLY B N 1 ATOM 6684 C CA . GLY B 1 299 ? -0.975 25.817 29.334 1.00 9.16 ? 299 GLY B CA 1 ATOM 6685 C C . GLY B 1 299 ? -1.827 25.323 30.478 1.00 9.47 ? 299 GLY B C 1 ATOM 6686 O O . GLY B 1 299 ? -2.440 26.095 31.214 1.00 9.11 ? 299 GLY B O 1 ATOM 6687 N N . GLY B 1 300 ? -1.832 23.999 30.607 1.00 9.01 ? 300 GLY B N 1 ATOM 6688 C CA . GLY B 1 300 ? -2.552 23.310 31.659 1.00 10.25 ? 300 GLY B CA 1 ATOM 6689 C C . GLY B 1 300 ? -2.074 21.872 31.712 1.00 11.95 ? 300 GLY B C 1 ATOM 6690 O O . GLY B 1 300 ? -1.318 21.433 30.836 1.00 11.91 ? 300 GLY B O 1 ATOM 6691 N N . SER B 1 301 ? -2.532 21.126 32.713 1.00 12.89 ? 301 SER B N 1 ATOM 6692 C CA . SER B 1 301 ? -2.147 19.725 32.854 1.00 13.89 ? 301 SER B CA 1 ATOM 6693 C C . SER B 1 301 ? -3.326 18.838 33.196 1.00 13.51 ? 301 SER B C 1 ATOM 6694 O O . SER B 1 301 ? -4.273 19.282 33.845 1.00 12.48 ? 301 SER B O 1 ATOM 6695 C CB . SER B 1 301 ? -1.066 19.556 33.925 1.00 13.69 ? 301 SER B CB 1 ATOM 6696 O OG . SER B 1 301 ? -0.500 18.250 33.879 1.00 11.49 ? 301 SER B OG 1 ATOM 6697 N N . LEU B 1 302 ? -3.242 17.572 32.776 1.00 15.11 ? 302 LEU B N 1 ATOM 6698 C CA . LEU B 1 302 ? -4.282 16.581 33.061 1.00 15.62 ? 302 LEU B CA 1 ATOM 6699 C C . LEU B 1 302 ? -4.170 16.095 34.503 1.00 15.08 ? 302 LEU B C 1 ATOM 6700 O O . LEU B 1 302 ? -5.078 15.447 35.027 1.00 17.10 ? 302 LEU B O 1 ATOM 6701 C CB . LEU B 1 302 ? -4.259 15.433 32.048 1.00 15.48 ? 302 LEU B CB 1 ATOM 6702 C CG . LEU B 1 302 ? -4.650 15.844 30.619 1.00 15.67 ? 302 LEU B CG 1 ATOM 6703 C CD1 . LEU B 1 302 ? -4.658 14.623 29.709 1.00 16.94 ? 302 LEU B CD1 1 ATOM 6704 C CD2 . LEU B 1 302 ? -6.018 16.529 30.600 1.00 13.18 ? 302 LEU B CD2 1 ATOM 6705 N N . ASN B 1 303 ? -3.031 16.412 35.125 1.00 15.25 ? 303 ASN B N 1 ATOM 6706 C CA . ASN B 1 303 ? -2.791 16.141 36.539 1.00 13.45 ? 303 ASN B CA 1 ATOM 6707 C C . ASN B 1 303 ? -3.291 17.479 37.112 1.00 14.96 ? 303 ASN B C 1 ATOM 6708 O O . ASN B 1 303 ? -2.654 18.516 36.895 1.00 12.76 ? 303 ASN B O 1 ATOM 6709 C CB . ASN B 1 303 ? -1.290 15.929 36.833 1.00 12.40 ? 303 ASN B CB 1 ATOM 6710 C CG . ASN B 1 303 ? -0.986 15.730 38.333 1.00 12.96 ? 303 ASN B CG 1 ATOM 6711 O OD1 . ASN B 1 303 ? -1.801 16.052 39.200 1.00 12.26 ? 303 ASN B OD1 1 ATOM 6712 N ND2 . ASN B 1 303 ? 0.210 15.229 38.635 1.00 12.17 ? 303 ASN B ND2 1 ATOM 6713 N N . PRO B 1 304 ? -4.438 17.470 37.836 1.00 15.45 ? 304 PRO B N 1 ATOM 6714 C CA . PRO B 1 304 ? -5.005 18.697 38.412 1.00 15.50 ? 304 PRO B CA 1 ATOM 6715 C C . PRO B 1 304 ? -4.187 19.394 39.493 1.00 15.23 ? 304 PRO B C 1 ATOM 6716 O O . PRO B 1 304 ? -4.326 20.603 39.694 1.00 16.48 ? 304 PRO B O 1 ATOM 6717 C CB . PRO B 1 304 ? -6.357 18.222 38.947 1.00 16.97 ? 304 PRO B CB 1 ATOM 6718 C CG . PRO B 1 304 ? -6.060 16.818 39.390 1.00 18.71 ? 304 PRO B CG 1 ATOM 6719 C CD . PRO B 1 304 ? -5.237 16.292 38.242 1.00 16.34 ? 304 PRO B CD 1 ATOM 6720 N N . HIS B 1 305 ? -3.351 18.627 40.199 1.00 15.64 ? 305 HIS B N 1 ATOM 6721 C CA . HIS B 1 305 ? -2.532 19.165 41.286 1.00 15.86 ? 305 HIS B CA 1 ATOM 6722 C C . HIS B 1 305 ? -1.077 18.650 41.317 1.00 16.05 ? 305 HIS B C 1 ATOM 6723 O O . HIS B 1 305 ? -0.699 17.898 42.226 1.00 15.70 ? 305 HIS B O 1 ATOM 6724 C CB . HIS B 1 305 ? -3.207 18.902 42.649 1.00 15.42 ? 305 HIS B CB 1 ATOM 6725 C CG . HIS B 1 305 ? -4.594 19.450 42.763 1.00 16.52 ? 305 HIS B CG 1 ATOM 6726 N ND1 . HIS B 1 305 ? -4.866 20.800 42.717 1.00 18.07 ? 305 HIS B ND1 1 ATOM 6727 C CD2 . HIS B 1 305 ? -5.793 18.827 42.863 1.00 18.80 ? 305 HIS B CD2 1 ATOM 6728 C CE1 . HIS B 1 305 ? -6.173 20.986 42.781 1.00 19.67 ? 305 HIS B CE1 1 ATOM 6729 N NE2 . HIS B 1 305 ? -6.758 19.805 42.869 1.00 18.03 ? 305 HIS B NE2 1 ATOM 6730 N N . PRO B 1 306 ? -0.235 19.053 40.330 1.00 15.59 ? 306 PRO B N 1 ATOM 6731 C CA . PRO B 1 306 ? 1.167 18.609 40.305 1.00 15.37 ? 306 PRO B CA 1 ATOM 6732 C C . PRO B 1 306 ? 1.876 19.242 41.497 1.00 15.03 ? 306 PRO B C 1 ATOM 6733 O O . PRO B 1 306 ? 1.729 20.446 41.749 1.00 15.95 ? 306 PRO B O 1 ATOM 6734 C CB . PRO B 1 306 ? 1.688 19.190 38.999 1.00 14.87 ? 306 PRO B CB 1 ATOM 6735 C CG . PRO B 1 306 ? 0.457 19.422 38.180 1.00 16.00 ? 306 PRO B CG 1 ATOM 6736 C CD . PRO B 1 306 ? -0.498 19.940 39.183 1.00 15.74 ? 306 PRO B CD 1 ATOM 6737 N N . ALA B 1 307 ? 2.570 18.417 42.270 1.00 15.27 ? 307 ALA B N 1 ATOM 6738 C CA . ALA B 1 307 ? 3.233 18.898 43.465 1.00 16.22 ? 307 ALA B CA 1 ATOM 6739 C C . ALA B 1 307 ? 4.464 18.118 43.876 1.00 17.77 ? 307 ALA B C 1 ATOM 6740 O O . ALA B 1 307 ? 4.752 17.045 43.340 1.00 20.04 ? 307 ALA B O 1 ATOM 6741 C CB . ALA B 1 307 ? 2.236 18.948 44.626 1.00 14.50 ? 307 ALA B CB 1 ATOM 6742 N N . ALA B 1 308 ? 5.219 18.732 44.783 1.00 18.36 ? 308 ALA B N 1 ATOM 6743 C CA . ALA B 1 308 ? 6.431 18.171 45.358 1.00 17.44 ? 308 ALA B CA 1 ATOM 6744 C C . ALA B 1 308 ? 6.301 18.347 46.868 1.00 18.11 ? 308 ALA B C 1 ATOM 6745 O O . ALA B 1 308 ? 5.489 19.149 47.334 1.00 17.06 ? 308 ALA B O 1 ATOM 6746 C CB . ALA B 1 308 ? 7.653 18.914 44.849 1.00 15.73 ? 308 ALA B CB 1 ATOM 6747 N N . ILE B 1 309 ? 7.085 17.583 47.624 1.00 19.40 ? 309 ILE B N 1 ATOM 6748 C CA . ILE B 1 309 ? 7.070 17.645 49.087 1.00 19.41 ? 309 ILE B CA 1 ATOM 6749 C C . ILE B 1 309 ? 8.340 18.304 49.617 1.00 19.51 ? 309 ILE B C 1 ATOM 6750 O O . ILE B 1 309 ? 9.447 17.988 49.178 1.00 20.06 ? 309 ILE B O 1 ATOM 6751 C CB . ILE B 1 309 ? 6.936 16.217 49.733 1.00 19.43 ? 309 ILE B CB 1 ATOM 6752 C CG1 . ILE B 1 309 ? 5.656 15.525 49.244 1.00 20.63 ? 309 ILE B CG1 1 ATOM 6753 C CG2 . ILE B 1 309 ? 6.910 16.309 51.276 1.00 18.86 ? 309 ILE B CG2 1 ATOM 6754 C CD1 . ILE B 1 309 ? 5.552 14.047 49.604 1.00 19.64 ? 309 ILE B CD1 1 ATOM 6755 N N . PHE B 1 310 ? 8.155 19.266 50.516 1.00 19.24 ? 310 PHE B N 1 ATOM 6756 C CA . PHE B 1 310 ? 9.262 19.946 51.172 1.00 19.82 ? 310 PHE B CA 1 ATOM 6757 C C . PHE B 1 310 ? 9.205 19.505 52.626 1.00 20.36 ? 310 PHE B C 1 ATOM 6758 O O . PHE B 1 310 ? 8.364 19.959 53.410 1.00 19.54 ? 310 PHE B O 1 ATOM 6759 C CB . PHE B 1 310 ? 9.171 21.467 51.019 1.00 18.76 ? 310 PHE B CB 1 ATOM 6760 C CG . PHE B 1 310 ? 9.860 21.998 49.783 1.00 18.96 ? 310 PHE B CG 1 ATOM 6761 C CD1 . PHE B 1 310 ? 9.509 21.533 48.501 1.00 17.83 ? 310 PHE B CD1 1 ATOM 6762 C CD2 . PHE B 1 310 ? 10.886 22.949 49.895 1.00 19.05 ? 310 PHE B CD2 1 ATOM 6763 C CE1 . PHE B 1 310 ? 10.176 22.006 47.342 1.00 16.21 ? 310 PHE B CE1 1 ATOM 6764 C CE2 . PHE B 1 310 ? 11.566 23.437 48.744 1.00 19.00 ? 310 PHE B CE2 1 ATOM 6765 C CZ . PHE B 1 310 ? 11.205 22.959 47.465 1.00 17.39 ? 310 PHE B CZ 1 ATOM 6766 N N . HIS B 1 311 ? 10.053 18.527 52.925 1.00 20.89 ? 311 HIS B N 1 ATOM 6767 C CA . HIS B 1 311 ? 10.161 17.910 54.240 1.00 22.21 ? 311 HIS B CA 1 ATOM 6768 C C . HIS B 1 311 ? 11.194 18.585 55.144 1.00 21.61 ? 311 HIS B C 1 ATOM 6769 O O . HIS B 1 311 ? 12.340 18.778 54.753 1.00 21.32 ? 311 HIS B O 1 ATOM 6770 C CB . HIS B 1 311 ? 10.499 16.417 54.042 1.00 23.83 ? 311 HIS B CB 1 ATOM 6771 C CG . HIS B 1 311 ? 10.790 15.668 55.307 1.00 25.38 ? 311 HIS B CG 1 ATOM 6772 N ND1 . HIS B 1 311 ? 9.820 15.375 56.240 1.00 25.83 ? 311 HIS B ND1 1 ATOM 6773 C CD2 . HIS B 1 311 ? 11.943 15.139 55.784 1.00 26.46 ? 311 HIS B CD2 1 ATOM 6774 C CE1 . HIS B 1 311 ? 10.361 14.697 57.236 1.00 26.88 ? 311 HIS B CE1 1 ATOM 6775 N NE2 . HIS B 1 311 ? 11.648 14.541 56.985 1.00 27.28 ? 311 HIS B NE2 1 ATOM 6776 N N . TYR B 1 312 ? 10.779 18.921 56.362 1.00 22.12 ? 312 TYR B N 1 ATOM 6777 C CA . TYR B 1 312 ? 11.688 19.504 57.348 1.00 22.97 ? 312 TYR B CA 1 ATOM 6778 C C . TYR B 1 312 ? 12.382 18.321 58.012 1.00 23.58 ? 312 TYR B C 1 ATOM 6779 O O . TYR B 1 312 ? 11.717 17.357 58.395 1.00 23.10 ? 312 TYR B O 1 ATOM 6780 C CB . TYR B 1 312 ? 10.923 20.288 58.408 1.00 21.86 ? 312 TYR B CB 1 ATOM 6781 C CG . TYR B 1 312 ? 10.673 21.741 58.081 1.00 21.36 ? 312 TYR B CG 1 ATOM 6782 C CD1 . TYR B 1 312 ? 9.917 22.116 56.948 1.00 19.29 ? 312 TYR B CD1 1 ATOM 6783 C CD2 . TYR B 1 312 ? 11.157 22.758 58.929 1.00 19.04 ? 312 TYR B CD2 1 ATOM 6784 C CE1 . TYR B 1 312 ? 9.649 23.478 56.669 1.00 18.90 ? 312 TYR B CE1 1 ATOM 6785 C CE2 . TYR B 1 312 ? 10.887 24.123 58.663 1.00 18.97 ? 312 TYR B CE2 1 ATOM 6786 C CZ . TYR B 1 312 ? 10.133 24.471 57.529 1.00 18.67 ? 312 TYR B CZ 1 ATOM 6787 O OH . TYR B 1 312 ? 9.870 25.792 57.252 1.00 16.37 ? 312 TYR B OH 1 ATOM 6788 N N . ALA B 1 313 ? 13.712 18.375 58.094 1.00 25.72 ? 313 ALA B N 1 ATOM 6789 C CA . ALA B 1 313 ? 14.511 17.309 58.709 1.00 27.89 ? 313 ALA B CA 1 ATOM 6790 C C . ALA B 1 313 ? 14.169 17.114 60.192 1.00 28.53 ? 313 ALA B C 1 ATOM 6791 O O . ALA B 1 313 ? 14.124 18.082 60.955 1.00 28.65 ? 313 ALA B O 1 ATOM 6792 C CB . ALA B 1 313 ? 15.999 17.605 58.543 1.00 27.20 ? 313 ALA B CB 1 ATOM 6793 N N . GLY B 1 314 ? 13.856 15.869 60.558 1.00 30.55 ? 314 GLY B N 1 ATOM 6794 C CA . GLY B 1 314 ? 13.511 15.540 61.936 1.00 32.25 ? 314 GLY B CA 1 ATOM 6795 C C . GLY B 1 314 ? 12.019 15.395 62.180 1.00 33.00 ? 314 GLY B C 1 ATOM 6796 O O . GLY B 1 314 ? 11.600 14.725 63.129 1.00 34.00 ? 314 GLY B O 1 ATOM 6797 N N . ALA B 1 315 ? 11.227 16.022 61.308 1.00 32.60 ? 315 ALA B N 1 ATOM 6798 C CA . ALA B 1 315 ? 9.760 16.006 61.358 1.00 31.29 ? 315 ALA B CA 1 ATOM 6799 C C . ALA B 1 315 ? 9.224 14.653 60.844 1.00 30.70 ? 315 ALA B C 1 ATOM 6800 O O . ALA B 1 315 ? 9.991 13.883 60.257 1.00 29.83 ? 315 ALA B O 1 ATOM 6801 C CB . ALA B 1 315 ? 9.224 17.157 60.500 1.00 31.55 ? 315 ALA B CB 1 ATOM 6802 N N . PRO B 1 316 ? 7.925 14.322 61.089 1.00 30.92 ? 316 PRO B N 1 ATOM 6803 C CA . PRO B 1 316 ? 7.403 13.035 60.595 1.00 30.99 ? 316 PRO B CA 1 ATOM 6804 C C . PRO B 1 316 ? 7.365 12.944 59.066 1.00 31.16 ? 316 PRO B C 1 ATOM 6805 O O . PRO B 1 316 ? 7.370 13.969 58.375 1.00 30.38 ? 316 PRO B O 1 ATOM 6806 C CB . PRO B 1 316 ? 5.987 13.003 61.166 1.00 31.21 ? 316 PRO B CB 1 ATOM 6807 C CG . PRO B 1 316 ? 6.121 13.760 62.433 1.00 31.09 ? 316 PRO B CG 1 ATOM 6808 C CD . PRO B 1 316 ? 6.933 14.940 61.995 1.00 31.06 ? 316 PRO B CD 1 ATOM 6809 N N . GLY B 1 317 ? 7.338 11.714 58.554 1.00 30.63 ? 317 GLY B N 1 ATOM 6810 C CA . GLY B 1 317 ? 7.285 11.488 57.119 1.00 31.05 ? 317 GLY B CA 1 ATOM 6811 C C . GLY B 1 317 ? 5.869 11.584 56.577 1.00 30.82 ? 317 GLY B C 1 ATOM 6812 O O . GLY B 1 317 ? 5.004 12.233 57.182 1.00 30.84 ? 317 GLY B O 1 ATOM 6813 N N . GLY B 1 318 ? 5.639 10.958 55.426 1.00 30.23 ? 318 GLY B N 1 ATOM 6814 C CA . GLY B 1 318 ? 4.322 10.965 54.811 1.00 30.23 ? 318 GLY B CA 1 ATOM 6815 C C . GLY B 1 318 ? 3.986 12.189 53.978 1.00 29.96 ? 318 GLY B C 1 ATOM 6816 O O . GLY B 1 318 ? 4.836 13.047 53.724 1.00 31.01 ? 318 GLY B O 1 ATOM 6817 N N . LEU B 1 319 ? 2.718 12.275 53.588 1.00 28.73 ? 319 LEU B N 1 ATOM 6818 C CA . LEU B 1 319 ? 2.213 13.364 52.763 1.00 27.33 ? 319 LEU B CA 1 ATOM 6819 C C . LEU B 1 319 ? 1.753 14.586 53.570 1.00 26.50 ? 319 LEU B C 1 ATOM 6820 O O . LEU B 1 319 ? 1.318 14.446 54.713 1.00 25.66 ? 319 LEU B O 1 ATOM 6821 C CB . LEU B 1 319 ? 1.053 12.858 51.882 1.00 28.06 ? 319 LEU B CB 1 ATOM 6822 C CG . LEU B 1 319 ? 1.234 11.645 50.959 1.00 27.58 ? 319 LEU B CG 1 ATOM 6823 C CD1 . LEU B 1 319 ? 0.016 11.538 50.060 1.00 27.30 ? 319 LEU B CD1 1 ATOM 6824 C CD2 . LEU B 1 319 ? 2.494 11.755 50.113 1.00 27.85 ? 319 LEU B CD2 1 ATOM 6825 N N . PRO B 1 320 ? 1.920 15.810 53.014 1.00 26.34 ? 320 PRO B N 1 ATOM 6826 C CA . PRO B 1 320 ? 1.505 17.057 53.679 1.00 25.12 ? 320 PRO B CA 1 ATOM 6827 C C . PRO B 1 320 ? -0.015 17.092 53.873 1.00 25.62 ? 320 PRO B C 1 ATOM 6828 O O . PRO B 1 320 ? -0.758 16.528 53.063 1.00 25.91 ? 320 PRO B O 1 ATOM 6829 C CB . PRO B 1 320 ? 1.935 18.125 52.687 1.00 24.91 ? 320 PRO B CB 1 ATOM 6830 C CG . PRO B 1 320 ? 3.124 17.537 52.045 1.00 24.23 ? 320 PRO B CG 1 ATOM 6831 C CD . PRO B 1 320 ? 2.763 16.113 51.840 1.00 25.26 ? 320 PRO B CD 1 ATOM 6832 N N . THR B 1 321 ? -0.456 17.751 54.944 1.00 26.02 ? 321 THR B N 1 ATOM 6833 C CA . THR B 1 321 ? -1.875 17.849 55.291 1.00 26.81 ? 321 THR B CA 1 ATOM 6834 C C . THR B 1 321 ? -2.560 19.147 54.862 1.00 26.57 ? 321 THR B C 1 ATOM 6835 O O . THR B 1 321 ? -3.773 19.160 54.623 1.00 28.09 ? 321 THR B O 1 ATOM 6836 C CB . THR B 1 321 ? -2.091 17.653 56.815 1.00 27.65 ? 321 THR B CB 1 ATOM 6837 O OG1 . THR B 1 321 ? -1.294 18.597 57.541 1.00 28.82 ? 321 THR B OG1 1 ATOM 6838 C CG2 . THR B 1 321 ? -1.712 16.238 57.239 1.00 28.67 ? 321 THR B CG2 1 ATOM 6839 N N . ASP B 1 322 ? -1.786 20.230 54.782 1.00 24.63 ? 322 ASP B N 1 ATOM 6840 C CA . ASP B 1 322 ? -2.297 21.544 54.395 1.00 24.48 ? 322 ASP B CA 1 ATOM 6841 C C . ASP B 1 322 ? -2.252 21.736 52.872 1.00 24.21 ? 322 ASP B C 1 ATOM 6842 O O . ASP B 1 322 ? -1.183 21.950 52.295 1.00 23.30 ? 322 ASP B O 1 ATOM 6843 C CB . ASP B 1 322 ? -1.491 22.648 55.113 1.00 24.46 ? 322 ASP B CB 1 ATOM 6844 C CG . ASP B 1 322 ? -2.142 24.042 55.029 1.00 25.54 ? 322 ASP B CG 1 ATOM 6845 O OD1 . ASP B 1 322 ? -3.195 24.219 54.371 1.00 24.78 ? 322 ASP B OD1 1 ATOM 6846 O OD2 . ASP B 1 322 ? -1.573 24.980 55.628 1.00 25.13 ? 322 ASP B OD2 1 ATOM 6847 N N . GLU B 1 323 ? -3.431 21.710 52.246 1.00 23.73 ? 323 GLU B N 1 ATOM 6848 C CA . GLU B 1 323 ? -3.576 21.891 50.797 1.00 22.82 ? 323 GLU B CA 1 ATOM 6849 C C . GLU B 1 323 ? -3.295 23.337 50.381 1.00 23.03 ? 323 GLU B C 1 ATOM 6850 O O . GLU B 1 323 ? -2.991 23.616 49.218 1.00 20.10 ? 323 GLU B O 1 ATOM 6851 C CB . GLU B 1 323 ? -4.974 21.461 50.346 1.00 24.08 ? 323 GLU B CB 1 ATOM 6852 C CG . GLU B 1 323 ? -5.220 19.954 50.474 1.00 24.14 ? 323 GLU B CG 1 ATOM 6853 C CD . GLU B 1 323 ? -6.631 19.521 50.097 1.00 27.11 ? 323 GLU B CD 1 ATOM 6854 O OE1 . GLU B 1 323 ? -7.405 20.332 49.540 1.00 27.53 ? 323 GLU B OE1 1 ATOM 6855 O OE2 . GLU B 1 323 ? -6.966 18.346 50.354 1.00 27.97 ? 323 GLU B OE2 1 ATOM 6856 N N . GLY B 1 324 ? -3.398 24.241 51.356 1.00 22.47 ? 324 GLY B N 1 ATOM 6857 C CA . GLY B 1 324 ? -3.139 25.653 51.141 1.00 23.68 ? 324 GLY B CA 1 ATOM 6858 C C . GLY B 1 324 ? -4.180 26.433 50.368 1.00 25.38 ? 324 GLY B C 1 ATOM 6859 O O . GLY B 1 324 ? -5.226 25.911 49.966 1.00 23.02 ? 324 GLY B O 1 ATOM 6860 N N . THR B 1 325 ? -3.866 27.709 50.179 1.00 27.67 ? 325 THR B N 1 ATOM 6861 C CA . THR B 1 325 ? -4.714 28.644 49.455 1.00 30.36 ? 325 THR B CA 1 ATOM 6862 C C . THR B 1 325 ? -4.180 28.758 48.017 1.00 30.07 ? 325 THR B C 1 ATOM 6863 O O . THR B 1 325 ? -2.960 28.666 47.805 1.00 28.05 ? 325 THR B O 1 ATOM 6864 C CB . THR B 1 325 ? -4.742 30.046 50.180 1.00 33.31 ? 325 THR B CB 1 ATOM 6865 O OG1 . THR B 1 325 ? -5.553 30.966 49.437 1.00 38.58 ? 325 THR B OG1 1 ATOM 6866 C CG2 . THR B 1 325 ? -3.333 30.632 50.361 1.00 33.94 ? 325 THR B CG2 1 ATOM 6867 N N . PRO B 1 326 ? -5.082 28.840 47.005 1.00 29.64 ? 326 PRO B N 1 ATOM 6868 C CA . PRO B 1 326 ? -4.594 28.964 45.625 1.00 28.81 ? 326 PRO B CA 1 ATOM 6869 C C . PRO B 1 326 ? -3.867 30.309 45.442 1.00 26.27 ? 326 PRO B C 1 ATOM 6870 O O . PRO B 1 326 ? -4.315 31.336 45.970 1.00 26.43 ? 326 PRO B O 1 ATOM 6871 C CB . PRO B 1 326 ? -5.880 28.868 44.789 1.00 30.86 ? 326 PRO B CB 1 ATOM 6872 C CG . PRO B 1 326 ? -6.961 29.304 45.737 1.00 32.16 ? 326 PRO B CG 1 ATOM 6873 C CD . PRO B 1 326 ? -6.545 28.631 47.010 1.00 31.69 ? 326 PRO B CD 1 ATOM 6874 N N . PRO B 1 327 ? -2.701 30.307 44.761 1.00 23.82 ? 327 PRO B N 1 ATOM 6875 C CA . PRO B 1 327 ? -1.958 31.557 44.558 1.00 23.08 ? 327 PRO B CA 1 ATOM 6876 C C . PRO B 1 327 ? -2.670 32.541 43.638 1.00 20.68 ? 327 PRO B C 1 ATOM 6877 O O . PRO B 1 327 ? -3.636 32.172 42.967 1.00 19.78 ? 327 PRO B O 1 ATOM 6878 C CB . PRO B 1 327 ? -0.650 31.070 43.945 1.00 23.41 ? 327 PRO B CB 1 ATOM 6879 C CG . PRO B 1 327 ? -1.066 29.878 43.159 1.00 23.43 ? 327 PRO B CG 1 ATOM 6880 C CD . PRO B 1 327 ? -1.993 29.178 44.124 1.00 25.62 ? 327 PRO B CD 1 ATOM 6881 N N . VAL B 1 328 ? -2.195 33.786 43.620 1.00 20.98 ? 328 VAL B N 1 ATOM 6882 C CA . VAL B 1 328 ? -2.766 34.819 42.757 1.00 21.97 ? 328 VAL B CA 1 ATOM 6883 C C . VAL B 1 328 ? -2.559 34.426 41.294 1.00 21.04 ? 328 VAL B C 1 ATOM 6884 O O . VAL B 1 328 ? -1.567 33.767 40.959 1.00 20.90 ? 328 VAL B O 1 ATOM 6885 C CB . VAL B 1 328 ? -2.151 36.235 43.023 1.00 23.87 ? 328 VAL B CB 1 ATOM 6886 C CG1 . VAL B 1 328 ? -2.558 36.733 44.406 1.00 25.46 ? 328 VAL B CG1 1 ATOM 6887 C CG2 . VAL B 1 328 ? -0.615 36.224 42.886 1.00 25.72 ? 328 VAL B CG2 1 ATOM 6888 N N . ASP B 1 329 ? -3.549 34.731 40.459 1.00 19.91 ? 329 ASP B N 1 ATOM 6889 C CA . ASP B 1 329 ? -3.483 34.428 39.034 1.00 19.25 ? 329 ASP B CA 1 ATOM 6890 C C . ASP B 1 329 ? -2.470 35.396 38.408 1.00 18.66 ? 329 ASP B C 1 ATOM 6891 O O . ASP B 1 329 ? -2.675 36.612 38.416 1.00 19.39 ? 329 ASP B O 1 ATOM 6892 C CB . ASP B 1 329 ? -4.871 34.593 38.400 1.00 20.14 ? 329 ASP B CB 1 ATOM 6893 C CG . ASP B 1 329 ? -5.005 33.867 37.072 1.00 20.09 ? 329 ASP B CG 1 ATOM 6894 O OD1 . ASP B 1 329 ? -4.122 34.012 36.204 1.00 19.57 ? 329 ASP B OD1 1 ATOM 6895 O OD2 . ASP B 1 329 ? -6.011 33.156 36.886 1.00 22.18 ? 329 ASP B OD2 1 ATOM 6896 N N . HIS B 1 330 ? -1.357 34.842 37.923 1.00 16.63 ? 330 HIS B N 1 ATOM 6897 C CA . HIS B 1 330 ? -0.288 35.633 37.309 1.00 14.88 ? 330 HIS B CA 1 ATOM 6898 C C . HIS B 1 330 ? -0.592 36.062 35.880 1.00 14.09 ? 330 HIS B C 1 ATOM 6899 O O . HIS B 1 330 ? 0.167 36.826 35.281 1.00 11.24 ? 330 HIS B O 1 ATOM 6900 C CB . HIS B 1 330 ? 1.042 34.885 37.372 1.00 14.21 ? 330 HIS B CB 1 ATOM 6901 C CG . HIS B 1 330 ? 1.634 34.821 38.746 1.00 14.12 ? 330 HIS B CG 1 ATOM 6902 N ND1 . HIS B 1 330 ? 2.669 35.638 39.145 1.00 11.75 ? 330 HIS B ND1 1 ATOM 6903 C CD2 . HIS B 1 330 ? 1.337 34.040 39.812 1.00 11.99 ? 330 HIS B CD2 1 ATOM 6904 C CE1 . HIS B 1 330 ? 2.983 35.363 40.398 1.00 12.32 ? 330 HIS B CE1 1 ATOM 6905 N NE2 . HIS B 1 330 ? 2.191 34.397 40.826 1.00 11.63 ? 330 HIS B NE2 1 ATOM 6906 N N . GLN B 1 331 ? -1.720 35.567 35.360 1.00 12.77 ? 331 GLN B N 1 ATOM 6907 C CA . GLN B 1 331 ? -2.230 35.869 34.025 1.00 12.94 ? 331 GLN B CA 1 ATOM 6908 C C . GLN B 1 331 ? -1.249 35.715 32.860 1.00 12.09 ? 331 GLN B C 1 ATOM 6909 O O . GLN B 1 331 ? -1.208 36.545 31.947 1.00 12.58 ? 331 GLN B O 1 ATOM 6910 C CB . GLN B 1 331 ? -2.918 37.252 34.010 1.00 13.43 ? 331 GLN B CB 1 ATOM 6911 C CG . GLN B 1 331 ? -4.126 37.388 34.960 1.00 14.23 ? 331 GLN B CG 1 ATOM 6912 C CD . GLN B 1 331 ? -5.357 36.574 34.552 1.00 15.82 ? 331 GLN B CD 1 ATOM 6913 O OE1 . GLN B 1 331 ? -5.438 36.029 33.447 1.00 15.76 ? 331 GLN B OE1 1 ATOM 6914 N NE2 . GLN B 1 331 ? -6.344 36.525 35.442 1.00 17.75 ? 331 GLN B NE2 1 ATOM 6915 N N . CYS B 1 332 ? -0.483 34.621 32.894 1.00 11.22 ? 332 CYS B N 1 ATOM 6916 C CA . CYS B 1 332 ? 0.529 34.300 31.882 1.00 10.69 ? 332 CYS B CA 1 ATOM 6917 C C . CYS B 1 332 ? 1.579 35.403 31.682 1.00 10.74 ? 332 CYS B C 1 ATOM 6918 O O . CYS B 1 332 ? 2.025 35.673 30.565 1.00 10.99 ? 332 CYS B O 1 ATOM 6919 C CB . CYS B 1 332 ? -0.125 33.917 30.558 1.00 10.37 ? 332 CYS B CB 1 ATOM 6920 S SG . CYS B 1 332 ? -1.107 32.401 30.655 1.00 13.37 ? 332 CYS B SG 1 ATOM 6921 N N . LEU B 1 333 ? 1.913 36.079 32.780 1.00 10.42 ? 333 LEU B N 1 ATOM 6922 C CA . LEU B 1 333 ? 2.878 37.175 32.756 1.00 12.47 ? 333 LEU B CA 1 ATOM 6923 C C . LEU B 1 333 ? 3.915 37.031 33.841 1.00 12.20 ? 333 LEU B C 1 ATOM 6924 O O . LEU B 1 333 ? 3.591 36.670 34.974 1.00 13.18 ? 333 LEU B O 1 ATOM 6925 C CB . LEU B 1 333 ? 2.179 38.525 32.953 1.00 12.47 ? 333 LEU B CB 1 ATOM 6926 C CG . LEU B 1 333 ? 1.088 38.986 31.988 1.00 12.32 ? 333 LEU B CG 1 ATOM 6927 C CD1 . LEU B 1 333 ? 0.240 40.027 32.666 1.00 12.54 ? 333 LEU B CD1 1 ATOM 6928 C CD2 . LEU B 1 333 ? 1.669 39.480 30.677 1.00 14.42 ? 333 LEU B CD2 1 ATOM 6929 N N . ASP B 1 334 ? 5.171 37.268 33.472 1.00 11.51 ? 334 ASP B N 1 ATOM 6930 C CA . ASP B 1 334 ? 6.274 37.230 34.425 1.00 11.88 ? 334 ASP B CA 1 ATOM 6931 C C . ASP B 1 334 ? 6.369 38.608 35.065 1.00 13.23 ? 334 ASP B C 1 ATOM 6932 O O . ASP B 1 334 ? 5.914 39.596 34.481 1.00 14.30 ? 334 ASP B O 1 ATOM 6933 C CB . ASP B 1 334 ? 7.600 36.798 33.762 1.00 11.61 ? 334 ASP B CB 1 ATOM 6934 C CG . ASP B 1 334 ? 7.983 37.645 32.551 1.00 9.83 ? 334 ASP B CG 1 ATOM 6935 O OD1 . ASP B 1 334 ? 7.106 37.982 31.727 1.00 9.48 ? 334 ASP B OD1 1 ATOM 6936 O OD2 . ASP B 1 334 ? 9.184 37.955 32.415 1.00 9.17 ? 334 ASP B OD2 1 ATOM 6937 N N . THR B 1 335 ? 6.910 38.662 36.278 1.00 14.00 ? 335 THR B N 1 ATOM 6938 C CA . THR B 1 335 ? 7.032 39.918 37.009 1.00 15.67 ? 335 THR B CA 1 ATOM 6939 C C . THR B 1 335 ? 8.086 40.872 36.461 1.00 16.57 ? 335 THR B C 1 ATOM 6940 O O . THR B 1 335 ? 9.179 40.451 36.071 1.00 16.96 ? 335 THR B O 1 ATOM 6941 C CB . THR B 1 335 ? 7.258 39.678 38.536 1.00 14.85 ? 335 THR B CB 1 ATOM 6942 O OG1 . THR B 1 335 ? 7.403 40.938 39.201 1.00 15.50 ? 335 THR B OG1 1 ATOM 6943 C CG2 . THR B 1 335 ? 8.500 38.812 38.800 1.00 16.05 ? 335 THR B CG2 1 ATOM 6944 N N . LEU B 1 336 ? 7.713 42.149 36.381 1.00 16.10 ? 336 LEU B N 1 ATOM 6945 C CA . LEU B 1 336 ? 8.623 43.187 35.919 1.00 17.13 ? 336 LEU B CA 1 ATOM 6946 C C . LEU B 1 336 ? 9.155 44.012 37.093 1.00 17.54 ? 336 LEU B C 1 ATOM 6947 O O . LEU B 1 336 ? 9.673 45.120 36.907 1.00 18.29 ? 336 LEU B O 1 ATOM 6948 C CB . LEU B 1 336 ? 7.962 44.098 34.873 1.00 19.26 ? 336 LEU B CB 1 ATOM 6949 C CG . LEU B 1 336 ? 7.458 43.500 33.555 1.00 19.51 ? 336 LEU B CG 1 ATOM 6950 C CD1 . LEU B 1 336 ? 7.069 44.626 32.614 1.00 19.63 ? 336 LEU B CD1 1 ATOM 6951 C CD2 . LEU B 1 336 ? 8.496 42.601 32.913 1.00 18.97 ? 336 LEU B CD2 1 ATOM 6952 N N . ASP B 1 337 ? 9.080 43.430 38.289 1.00 16.50 ? 337 ASP B N 1 ATOM 6953 C CA . ASP B 1 337 ? 9.534 44.082 39.516 1.00 17.85 ? 337 ASP B CA 1 ATOM 6954 C C . ASP B 1 337 ? 10.980 43.763 39.874 1.00 17.74 ? 337 ASP B C 1 ATOM 6955 O O . ASP B 1 337 ? 11.559 44.425 40.739 1.00 18.24 ? 337 ASP B O 1 ATOM 6956 C CB . ASP B 1 337 ? 8.633 43.707 40.698 1.00 19.45 ? 337 ASP B CB 1 ATOM 6957 C CG . ASP B 1 337 ? 7.209 44.209 40.547 1.00 21.67 ? 337 ASP B CG 1 ATOM 6958 O OD1 . ASP B 1 337 ? 6.981 45.235 39.865 1.00 23.99 ? 337 ASP B OD1 1 ATOM 6959 O OD2 . ASP B 1 337 ? 6.313 43.574 41.137 1.00 24.82 ? 337 ASP B OD2 1 ATOM 6960 N N . VAL B 1 338 ? 11.553 42.747 39.221 1.00 17.21 ? 338 VAL B N 1 ATOM 6961 C CA . VAL B 1 338 ? 12.940 42.346 39.474 1.00 17.29 ? 338 VAL B CA 1 ATOM 6962 C C . VAL B 1 338 ? 13.937 43.411 39.008 1.00 16.62 ? 338 VAL B C 1 ATOM 6963 O O . VAL B 1 338 ? 13.788 44.004 37.933 1.00 16.13 ? 338 VAL B O 1 ATOM 6964 C CB . VAL B 1 338 ? 13.286 40.936 38.880 1.00 17.38 ? 338 VAL B CB 1 ATOM 6965 C CG1 . VAL B 1 338 ? 12.491 39.863 39.587 1.00 16.84 ? 338 VAL B CG1 1 ATOM 6966 C CG2 . VAL B 1 338 ? 13.027 40.869 37.384 1.00 16.34 ? 338 VAL B CG2 1 ATOM 6967 N N . ARG B 1 339 ? 14.885 43.721 39.885 1.00 16.37 ? 339 ARG B N 1 ATOM 6968 C CA . ARG B 1 339 ? 15.892 44.737 39.612 1.00 15.97 ? 339 ARG B CA 1 ATOM 6969 C C . ARG B 1 339 ? 17.293 44.134 39.697 1.00 14.55 ? 339 ARG B C 1 ATOM 6970 O O . ARG B 1 339 ? 17.716 43.711 40.771 1.00 13.44 ? 339 ARG B O 1 ATOM 6971 C CB . ARG B 1 339 ? 15.758 45.904 40.610 1.00 16.88 ? 339 ARG B CB 1 ATOM 6972 C CG . ARG B 1 339 ? 14.434 46.684 40.552 1.00 20.46 ? 339 ARG B CG 1 ATOM 6973 C CD . ARG B 1 339 ? 14.304 47.489 39.265 1.00 20.57 ? 339 ARG B CD 1 ATOM 6974 N NE . ARG B 1 339 ? 13.013 48.167 39.147 1.00 24.03 ? 339 ARG B NE 1 ATOM 6975 C CZ . ARG B 1 339 ? 11.953 47.682 38.502 1.00 24.98 ? 339 ARG B CZ 1 ATOM 6976 N NH1 . ARG B 1 339 ? 12.007 46.498 37.900 1.00 23.93 ? 339 ARG B NH1 1 ATOM 6977 N NH2 . ARG B 1 339 ? 10.829 48.386 38.460 1.00 24.60 ? 339 ARG B NH2 1 ATOM 6978 N N . PRO B 1 340 ? 18.018 44.054 38.557 1.00 13.39 ? 340 PRO B N 1 ATOM 6979 C CA . PRO B 1 340 ? 19.379 43.498 38.508 1.00 13.81 ? 340 PRO B CA 1 ATOM 6980 C C . PRO B 1 340 ? 20.360 44.202 39.443 1.00 14.46 ? 340 PRO B C 1 ATOM 6981 O O . PRO B 1 340 ? 20.256 45.420 39.642 1.00 14.44 ? 340 PRO B O 1 ATOM 6982 C CB . PRO B 1 340 ? 19.769 43.697 37.051 1.00 13.31 ? 340 PRO B CB 1 ATOM 6983 C CG . PRO B 1 340 ? 18.470 43.534 36.350 1.00 14.28 ? 340 PRO B CG 1 ATOM 6984 C CD . PRO B 1 340 ? 17.538 44.344 37.192 1.00 12.15 ? 340 PRO B CD 1 ATOM 6985 N N . VAL B 1 341 ? 21.264 43.425 40.052 1.00 14.76 ? 341 VAL B N 1 ATOM 6986 C CA . VAL B 1 341 ? 22.291 43.952 40.968 1.00 17.11 ? 341 VAL B CA 1 ATOM 6987 C C . VAL B 1 341 ? 23.211 44.908 40.198 1.00 17.16 ? 341 VAL B C 1 ATOM 6988 O O . VAL B 1 341 ? 23.470 46.021 40.656 1.00 18.19 ? 341 VAL B O 1 ATOM 6989 C CB . VAL B 1 341 ? 23.142 42.815 41.614 1.00 16.81 ? 341 VAL B CB 1 ATOM 6990 C CG1 . VAL B 1 341 ? 24.181 43.389 42.588 1.00 17.22 ? 341 VAL B CG1 1 ATOM 6991 C CG2 . VAL B 1 341 ? 22.254 41.866 42.356 1.00 18.24 ? 341 VAL B CG2 1 ATOM 6992 N N . VAL B 1 342 ? 23.699 44.454 39.040 1.00 17.60 ? 342 VAL B N 1 ATOM 6993 C CA . VAL B 1 342 ? 24.549 45.266 38.162 1.00 16.96 ? 342 VAL B CA 1 ATOM 6994 C C . VAL B 1 342 ? 23.548 46.022 37.269 1.00 17.66 ? 342 VAL B C 1 ATOM 6995 O O . VAL B 1 342 ? 22.833 45.404 36.471 1.00 15.93 ? 342 VAL B O 1 ATOM 6996 C CB . VAL B 1 342 ? 25.519 44.386 37.321 1.00 18.19 ? 342 VAL B CB 1 ATOM 6997 C CG1 . VAL B 1 342 ? 26.375 45.251 36.395 1.00 17.56 ? 342 VAL B CG1 1 ATOM 6998 C CG2 . VAL B 1 342 ? 26.419 43.578 38.246 1.00 16.05 ? 342 VAL B CG2 1 ATOM 6999 N N . PRO B 1 343 ? 23.471 47.365 37.412 1.00 17.74 ? 343 PRO B N 1 ATOM 7000 C CA . PRO B 1 343 ? 22.536 48.167 36.619 1.00 17.22 ? 343 PRO B CA 1 ATOM 7001 C C . PRO B 1 343 ? 22.846 48.484 35.161 1.00 16.26 ? 343 PRO B C 1 ATOM 7002 O O . PRO B 1 343 ? 23.990 48.395 34.720 1.00 15.19 ? 343 PRO B O 1 ATOM 7003 C CB . PRO B 1 343 ? 22.420 49.445 37.446 1.00 17.86 ? 343 PRO B CB 1 ATOM 7004 C CG . PRO B 1 343 ? 23.804 49.626 37.952 1.00 18.61 ? 343 PRO B CG 1 ATOM 7005 C CD . PRO B 1 343 ? 24.192 48.227 38.376 1.00 17.92 ? 343 PRO B CD 1 ATOM 7006 N N . ARG B 1 344 ? 21.781 48.793 34.419 1.00 15.00 ? 344 ARG B N 1 ATOM 7007 C CA . ARG B 1 344 ? 21.847 49.206 33.015 1.00 16.64 ? 344 ARG B CA 1 ATOM 7008 C C . ARG B 1 344 ? 20.877 50.374 32.879 1.00 19.29 ? 344 ARG B C 1 ATOM 7009 O O . ARG B 1 344 ? 19.790 50.348 33.450 1.00 19.44 ? 344 ARG B O 1 ATOM 7010 C CB . ARG B 1 344 ? 21.430 48.087 32.047 1.00 16.05 ? 344 ARG B CB 1 ATOM 7011 C CG . ARG B 1 344 ? 22.397 46.906 31.921 1.00 15.11 ? 344 ARG B CG 1 ATOM 7012 C CD . ARG B 1 344 ? 23.776 47.300 31.406 1.00 16.70 ? 344 ARG B CD 1 ATOM 7013 N NE . ARG B 1 344 ? 24.639 46.125 31.308 1.00 17.94 ? 344 ARG B NE 1 ATOM 7014 C CZ . ARG B 1 344 ? 25.774 45.946 31.980 1.00 17.87 ? 344 ARG B CZ 1 ATOM 7015 N NH1 . ARG B 1 344 ? 26.232 46.869 32.822 1.00 16.91 ? 344 ARG B NH1 1 ATOM 7016 N NH2 . ARG B 1 344 ? 26.435 44.809 31.836 1.00 16.79 ? 344 ARG B NH2 1 ATOM 7017 N N . SER B 1 345 ? 21.284 51.408 32.153 1.00 21.17 ? 345 SER B N 1 ATOM 7018 C CA . SER B 1 345 ? 20.442 52.581 31.952 1.00 23.25 ? 345 SER B CA 1 ATOM 7019 C C . SER B 1 345 ? 20.334 52.887 30.466 1.00 23.11 ? 345 SER B C 1 ATOM 7020 O O . SER B 1 345 ? 21.342 52.892 29.757 1.00 23.01 ? 345 SER B O 1 ATOM 7021 C CB . SER B 1 345 ? 21.014 53.787 32.711 1.00 24.96 ? 345 SER B CB 1 ATOM 7022 O OG . SER B 1 345 ? 20.166 54.919 32.598 1.00 28.96 ? 345 SER B OG 1 ATOM 7023 N N . VAL B 1 346 ? 19.098 53.066 29.994 1.00 23.05 ? 346 VAL B N 1 ATOM 7024 C CA . VAL B 1 346 ? 18.808 53.377 28.586 1.00 23.35 ? 346 VAL B CA 1 ATOM 7025 C C . VAL B 1 346 ? 17.713 54.437 28.429 1.00 23.56 ? 346 VAL B C 1 ATOM 7026 O O . VAL B 1 346 ? 16.784 54.485 29.242 1.00 22.23 ? 346 VAL B O 1 ATOM 7027 C CB . VAL B 1 346 ? 18.324 52.121 27.765 1.00 24.20 ? 346 VAL B CB 1 ATOM 7028 C CG1 . VAL B 1 346 ? 19.430 51.154 27.577 1.00 25.83 ? 346 VAL B CG1 1 ATOM 7029 C CG2 . VAL B 1 346 ? 17.149 51.440 28.426 1.00 24.21 ? 346 VAL B CG2 1 ATOM 7030 N N . PRO B 1 347 ? 17.834 55.332 27.416 1.00 24.22 ? 347 PRO B N 1 ATOM 7031 C CA . PRO B 1 347 ? 16.779 56.337 27.243 1.00 26.02 ? 347 PRO B CA 1 ATOM 7032 C C . PRO B 1 347 ? 15.553 55.686 26.585 1.00 26.57 ? 347 PRO B C 1 ATOM 7033 O O . PRO B 1 347 ? 15.688 54.826 25.703 1.00 25.77 ? 347 PRO B O 1 ATOM 7034 C CB . PRO B 1 347 ? 17.437 57.378 26.331 1.00 25.22 ? 347 PRO B CB 1 ATOM 7035 C CG . PRO B 1 347 ? 18.449 56.583 25.551 1.00 25.35 ? 347 PRO B CG 1 ATOM 7036 C CD . PRO B 1 347 ? 19.027 55.700 26.621 1.00 24.79 ? 347 PRO B CD 1 ATOM 7037 N N . VAL B 1 348 ? 14.373 56.013 27.099 1.00 26.79 ? 348 VAL B N 1 ATOM 7038 C CA . VAL B 1 348 ? 13.131 55.469 26.560 1.00 28.03 ? 348 VAL B CA 1 ATOM 7039 C C . VAL B 1 348 ? 12.271 56.545 25.904 1.00 28.59 ? 348 VAL B C 1 ATOM 7040 O O . VAL B 1 348 ? 11.385 56.234 25.107 1.00 27.93 ? 348 VAL B O 1 ATOM 7041 C CB . VAL B 1 348 ? 12.313 54.690 27.632 1.00 27.89 ? 348 VAL B CB 1 ATOM 7042 C CG1 . VAL B 1 348 ? 12.979 53.348 27.928 1.00 27.08 ? 348 VAL B CG1 1 ATOM 7043 C CG2 . VAL B 1 348 ? 12.154 55.507 28.920 1.00 28.97 ? 348 VAL B CG2 1 ATOM 7044 N N . ASN B 1 349 ? 12.592 57.806 26.199 1.00 29.21 ? 349 ASN B N 1 ATOM 7045 C CA . ASN B 1 349 ? 11.877 58.969 25.668 1.00 30.25 ? 349 ASN B CA 1 ATOM 7046 C C . ASN B 1 349 ? 12.015 59.157 24.149 1.00 29.95 ? 349 ASN B C 1 ATOM 7047 O O . ASN B 1 349 ? 11.092 59.633 23.487 1.00 28.98 ? 349 ASN B O 1 ATOM 7048 C CB . ASN B 1 349 ? 12.312 60.248 26.408 1.00 31.30 ? 349 ASN B CB 1 ATOM 7049 C CG . ASN B 1 349 ? 13.800 60.542 26.261 1.00 32.86 ? 349 ASN B CG 1 ATOM 7050 O OD1 . ASN B 1 349 ? 14.630 59.958 26.954 1.00 34.45 ? 349 ASN B OD1 1 ATOM 7051 N ND2 . ASN B 1 349 ? 14.138 61.434 25.335 1.00 33.27 ? 349 ASN B ND2 1 ATOM 7052 N N . SER B 1 350 ? 13.153 58.714 23.615 1.00 29.97 ? 350 SER B N 1 ATOM 7053 C CA . SER B 1 350 ? 13.479 58.837 22.196 1.00 30.12 ? 350 SER B CA 1 ATOM 7054 C C . SER B 1 350 ? 13.011 57.712 21.262 1.00 29.09 ? 350 SER B C 1 ATOM 7055 O O . SER B 1 350 ? 13.268 57.772 20.052 1.00 28.45 ? 350 SER B O 1 ATOM 7056 C CB . SER B 1 350 ? 14.989 59.068 22.041 1.00 30.27 ? 350 SER B CB 1 ATOM 7057 O OG . SER B 1 350 ? 15.728 58.137 22.813 1.00 32.54 ? 350 SER B OG 1 ATOM 7058 N N . PHE B 1 351 ? 12.308 56.713 21.806 1.00 28.29 ? 351 PHE B N 1 ATOM 7059 C CA . PHE B 1 351 ? 11.812 55.593 20.998 1.00 26.78 ? 351 PHE B CA 1 ATOM 7060 C C . PHE B 1 351 ? 10.671 55.998 20.056 1.00 27.29 ? 351 PHE B C 1 ATOM 7061 O O . PHE B 1 351 ? 9.682 56.606 20.475 1.00 25.12 ? 351 PHE B O 1 ATOM 7062 C CB . PHE B 1 351 ? 11.383 54.395 21.876 1.00 26.99 ? 351 PHE B CB 1 ATOM 7063 C CG . PHE B 1 351 ? 10.841 53.217 21.080 1.00 26.59 ? 351 PHE B CG 1 ATOM 7064 C CD1 . PHE B 1 351 ? 11.695 52.451 20.265 1.00 27.19 ? 351 PHE B CD1 1 ATOM 7065 C CD2 . PHE B 1 351 ? 9.458 52.943 21.055 1.00 25.95 ? 351 PHE B CD2 1 ATOM 7066 C CE1 . PHE B 1 351 ? 11.182 51.429 19.420 1.00 25.57 ? 351 PHE B CE1 1 ATOM 7067 C CE2 . PHE B 1 351 ? 8.927 51.927 20.216 1.00 26.82 ? 351 PHE B CE2 1 ATOM 7068 C CZ . PHE B 1 351 ? 9.796 51.170 19.393 1.00 25.28 ? 351 PHE B CZ 1 ATOM 7069 N N . VAL B 1 352 ? 10.839 55.634 18.783 1.00 27.61 ? 352 VAL B N 1 ATOM 7070 C CA . VAL B 1 352 ? 9.861 55.900 17.727 1.00 29.39 ? 352 VAL B CA 1 ATOM 7071 C C . VAL B 1 352 ? 9.587 54.567 17.015 1.00 29.65 ? 352 VAL B C 1 ATOM 7072 O O . VAL B 1 352 ? 10.526 53.884 16.588 1.00 30.27 ? 352 VAL B O 1 ATOM 7073 C CB . VAL B 1 352 ? 10.390 56.946 16.671 1.00 29.83 ? 352 VAL B CB 1 ATOM 7074 C CG1 . VAL B 1 352 ? 9.306 57.271 15.637 1.00 31.84 ? 352 VAL B CG1 1 ATOM 7075 C CG2 . VAL B 1 352 ? 10.853 58.240 17.345 1.00 31.53 ? 352 VAL B CG2 1 ATOM 7076 N N . LYS B 1 353 ? 8.303 54.214 16.894 1.00 29.82 ? 353 LYS B N 1 ATOM 7077 C CA . LYS B 1 353 ? 7.860 52.988 16.220 1.00 30.44 ? 353 LYS B CA 1 ATOM 7078 C C . LYS B 1 353 ? 8.077 53.124 14.706 1.00 30.46 ? 353 LYS B C 1 ATOM 7079 O O . LYS B 1 353 ? 7.470 53.978 14.051 1.00 29.07 ? 353 LYS B O 1 ATOM 7080 C CB . LYS B 1 353 ? 6.379 52.703 16.530 1.00 31.68 ? 353 LYS B CB 1 ATOM 7081 C CG . LYS B 1 353 ? 5.795 51.490 15.803 1.00 33.63 ? 353 LYS B CG 1 ATOM 7082 C CD . LYS B 1 353 ? 4.294 51.363 15.998 1.00 35.64 ? 353 LYS B CD 1 ATOM 7083 C CE . LYS B 1 353 ? 3.742 50.257 15.114 1.00 36.17 ? 353 LYS B CE 1 ATOM 7084 N NZ . LYS B 1 353 ? 2.289 50.014 15.335 1.00 39.08 ? 353 LYS B NZ 1 ATOM 7085 N N . ARG B 1 354 ? 8.998 52.313 14.188 1.00 29.40 ? 354 ARG B N 1 ATOM 7086 C CA . ARG B 1 354 ? 9.362 52.292 12.766 1.00 30.73 ? 354 ARG B CA 1 ATOM 7087 C C . ARG B 1 354 ? 9.375 50.829 12.288 1.00 28.32 ? 354 ARG B C 1 ATOM 7088 O O . ARG B 1 354 ? 9.586 49.928 13.103 1.00 27.51 ? 354 ARG B O 1 ATOM 7089 C CB . ARG B 1 354 ? 10.762 52.916 12.579 1.00 33.27 ? 354 ARG B CB 1 ATOM 7090 C CG . ARG B 1 354 ? 10.814 54.429 12.767 1.00 40.02 ? 354 ARG B CG 1 ATOM 7091 C CD . ARG B 1 354 ? 12.229 54.951 12.898 1.00 44.41 ? 354 ARG B CD 1 ATOM 7092 N NE . ARG B 1 354 ? 12.227 56.341 13.356 1.00 49.48 ? 354 ARG B NE 1 ATOM 7093 C CZ . ARG B 1 354 ? 12.990 57.312 12.860 1.00 51.76 ? 354 ARG B CZ 1 ATOM 7094 N NH1 . ARG B 1 354 ? 13.844 57.070 11.870 1.00 53.17 ? 354 ARG B NH1 1 ATOM 7095 N NH2 . ARG B 1 354 ? 12.890 58.540 13.353 1.00 52.58 ? 354 ARG B NH2 1 ATOM 7096 N N . PRO B 1 355 ? 9.132 50.568 10.976 1.00 26.08 ? 355 PRO B N 1 ATOM 7097 C CA . PRO B 1 355 ? 9.141 49.184 10.472 1.00 24.46 ? 355 PRO B CA 1 ATOM 7098 C C . PRO B 1 355 ? 10.430 48.386 10.742 1.00 23.67 ? 355 PRO B C 1 ATOM 7099 O O . PRO B 1 355 ? 10.365 47.177 10.976 1.00 21.59 ? 355 PRO B O 1 ATOM 7100 C CB . PRO B 1 355 ? 8.907 49.372 8.975 1.00 24.53 ? 355 PRO B CB 1 ATOM 7101 C CG . PRO B 1 355 ? 7.981 50.529 8.943 1.00 25.51 ? 355 PRO B CG 1 ATOM 7102 C CD . PRO B 1 355 ? 8.633 51.479 9.921 1.00 25.03 ? 355 PRO B CD 1 ATOM 7103 N N . ASP B 1 356 ? 11.573 49.077 10.788 1.00 21.67 ? 356 ASP B N 1 ATOM 7104 C CA . ASP B 1 356 ? 12.862 48.421 11.029 1.00 22.44 ? 356 ASP B CA 1 ATOM 7105 C C . ASP B 1 356 ? 13.158 48.023 12.483 1.00 21.05 ? 356 ASP B C 1 ATOM 7106 O O . ASP B 1 356 ? 14.164 47.365 12.754 1.00 21.76 ? 356 ASP B O 1 ATOM 7107 C CB . ASP B 1 356 ? 14.035 49.202 10.383 1.00 23.60 ? 356 ASP B CB 1 ATOM 7108 C CG . ASP B 1 356 ? 14.286 50.580 11.007 1.00 24.97 ? 356 ASP B CG 1 ATOM 7109 O OD1 . ASP B 1 356 ? 13.572 50.997 11.946 1.00 23.35 ? 356 ASP B OD1 1 ATOM 7110 O OD2 . ASP B 1 356 ? 15.231 51.254 10.540 1.00 26.93 ? 356 ASP B OD2 1 ATOM 7111 N N . ASN B 1 357 ? 12.293 48.447 13.406 1.00 19.23 ? 357 ASN B N 1 ATOM 7112 C CA . ASN B 1 357 ? 12.440 48.095 14.819 1.00 17.15 ? 357 ASN B CA 1 ATOM 7113 C C . ASN B 1 357 ? 11.195 47.375 15.361 1.00 15.45 ? 357 ASN B C 1 ATOM 7114 O O . ASN B 1 357 ? 11.091 47.096 16.556 1.00 13.44 ? 357 ASN B O 1 ATOM 7115 C CB . ASN B 1 357 ? 12.844 49.319 15.682 1.00 16.80 ? 357 ASN B CB 1 ATOM 7116 C CG . ASN B 1 357 ? 11.762 50.406 15.776 1.00 17.00 ? 357 ASN B CG 1 ATOM 7117 O OD1 . ASN B 1 357 ? 10.562 50.144 15.664 1.00 13.73 ? 357 ASN B OD1 1 ATOM 7118 N ND2 . ASN B 1 357 ? 12.200 51.633 16.032 1.00 16.13 ? 357 ASN B ND2 1 ATOM 7119 N N . THR B 1 358 ? 10.256 47.096 14.460 1.00 14.72 ? 358 THR B N 1 ATOM 7120 C CA . THR B 1 358 ? 8.997 46.441 14.803 1.00 14.97 ? 358 THR B CA 1 ATOM 7121 C C . THR B 1 358 ? 8.919 45.019 14.252 1.00 15.22 ? 358 THR B C 1 ATOM 7122 O O . THR B 1 358 ? 9.184 44.770 13.073 1.00 15.59 ? 358 THR B O 1 ATOM 7123 C CB . THR B 1 358 ? 7.793 47.302 14.336 1.00 14.76 ? 358 THR B CB 1 ATOM 7124 O OG1 . THR B 1 358 ? 7.880 48.589 14.957 1.00 13.74 ? 358 THR B OG1 1 ATOM 7125 C CG2 . THR B 1 358 ? 6.447 46.677 14.713 1.00 16.58 ? 358 THR B CG2 1 ATOM 7126 N N . LEU B 1 359 ? 8.566 44.088 15.138 1.00 15.01 ? 359 LEU B N 1 ATOM 7127 C CA . LEU B 1 359 ? 8.438 42.674 14.798 1.00 15.93 ? 359 LEU B CA 1 ATOM 7128 C C . LEU B 1 359 ? 7.007 42.192 15.063 1.00 16.36 ? 359 LEU B C 1 ATOM 7129 O O . LEU B 1 359 ? 6.694 41.754 16.176 1.00 15.23 ? 359 LEU B O 1 ATOM 7130 C CB . LEU B 1 359 ? 9.450 41.837 15.606 1.00 16.09 ? 359 LEU B CB 1 ATOM 7131 C CG . LEU B 1 359 ? 10.953 42.048 15.379 1.00 17.21 ? 359 LEU B CG 1 ATOM 7132 C CD1 . LEU B 1 359 ? 11.750 41.263 16.408 1.00 17.34 ? 359 LEU B CD1 1 ATOM 7133 C CD2 . LEU B 1 359 ? 11.334 41.643 13.964 1.00 17.00 ? 359 LEU B CD2 1 ATOM 7134 N N . PRO B 1 360 ? 6.099 42.324 14.065 1.00 17.15 ? 360 PRO B N 1 ATOM 7135 C CA . PRO B 1 360 ? 4.733 41.859 14.320 1.00 17.45 ? 360 PRO B CA 1 ATOM 7136 C C . PRO B 1 360 ? 4.561 40.346 14.160 1.00 17.34 ? 360 PRO B C 1 ATOM 7137 O O . PRO B 1 360 ? 4.939 39.767 13.143 1.00 16.48 ? 360 PRO B O 1 ATOM 7138 C CB . PRO B 1 360 ? 3.898 42.667 13.323 1.00 17.76 ? 360 PRO B CB 1 ATOM 7139 C CG . PRO B 1 360 ? 4.808 42.856 12.172 1.00 19.67 ? 360 PRO B CG 1 ATOM 7140 C CD . PRO B 1 360 ? 6.163 43.097 12.806 1.00 17.34 ? 360 PRO B CD 1 ATOM 7141 N N . VAL B 1 361 ? 4.071 39.718 15.226 1.00 16.67 ? 361 VAL B N 1 ATOM 7142 C CA . VAL B 1 361 ? 3.806 38.280 15.263 1.00 16.20 ? 361 VAL B CA 1 ATOM 7143 C C . VAL B 1 361 ? 2.392 38.124 14.715 1.00 15.92 ? 361 VAL B C 1 ATOM 7144 O O . VAL B 1 361 ? 1.517 38.916 15.043 1.00 16.39 ? 361 VAL B O 1 ATOM 7145 C CB . VAL B 1 361 ? 3.889 37.735 16.723 1.00 15.06 ? 361 VAL B CB 1 ATOM 7146 C CG1 . VAL B 1 361 ? 3.419 36.281 16.814 1.00 16.70 ? 361 VAL B CG1 1 ATOM 7147 C CG2 . VAL B 1 361 ? 5.309 37.850 17.235 1.00 16.05 ? 361 VAL B CG2 1 ATOM 7148 N N . ALA B 1 362 ? 2.186 37.139 13.847 1.00 17.63 ? 362 ALA B N 1 ATOM 7149 C CA . ALA B 1 362 ? 0.866 36.908 13.275 1.00 17.63 ? 362 ALA B CA 1 ATOM 7150 C C . ALA B 1 362 ? 0.596 35.450 12.998 1.00 19.04 ? 362 ALA B C 1 ATOM 7151 O O . ALA B 1 362 ? 1.466 34.730 12.507 1.00 19.62 ? 362 ALA B O 1 ATOM 7152 C CB . ALA B 1 362 ? 0.677 37.730 11.992 1.00 17.64 ? 362 ALA B CB 1 ATOM 7153 N N . LEU B 1 363 ? -0.612 35.014 13.345 1.00 18.87 ? 363 LEU B N 1 ATOM 7154 C CA . LEU B 1 363 ? -1.036 33.648 13.091 1.00 18.22 ? 363 LEU B CA 1 ATOM 7155 C C . LEU B 1 363 ? -1.758 33.642 11.744 1.00 19.47 ? 363 LEU B C 1 ATOM 7156 O O . LEU B 1 363 ? -2.766 34.333 11.565 1.00 19.29 ? 363 LEU B O 1 ATOM 7157 C CB . LEU B 1 363 ? -1.961 33.142 14.206 1.00 18.02 ? 363 LEU B CB 1 ATOM 7158 C CG . LEU B 1 363 ? -2.519 31.715 14.081 1.00 16.56 ? 363 LEU B CG 1 ATOM 7159 C CD1 . LEU B 1 363 ? -1.402 30.689 13.972 1.00 14.99 ? 363 LEU B CD1 1 ATOM 7160 C CD2 . LEU B 1 363 ? -3.409 31.419 15.262 1.00 15.30 ? 363 LEU B CD2 1 ATOM 7161 N N . ASP B 1 364 ? -1.204 32.885 10.801 1.00 20.00 ? 364 ASP B N 1 ATOM 7162 C CA . ASP B 1 364 ? -1.756 32.760 9.459 1.00 20.84 ? 364 ASP B CA 1 ATOM 7163 C C . ASP B 1 364 ? -2.517 31.439 9.361 1.00 21.38 ? 364 ASP B C 1 ATOM 7164 O O . ASP B 1 364 ? -1.932 30.360 9.494 1.00 20.04 ? 364 ASP B O 1 ATOM 7165 C CB . ASP B 1 364 ? -0.627 32.828 8.412 1.00 22.28 ? 364 ASP B CB 1 ATOM 7166 C CG . ASP B 1 364 ? -1.143 32.949 6.970 1.00 24.00 ? 364 ASP B CG 1 ATOM 7167 O OD1 . ASP B 1 364 ? -2.370 33.032 6.754 1.00 25.28 ? 364 ASP B OD1 1 ATOM 7168 O OD2 . ASP B 1 364 ? -0.308 32.963 6.043 1.00 27.51 ? 364 ASP B OD2 1 ATOM 7169 N N . LEU B 1 365 ? -3.823 31.554 9.119 1.00 21.77 ? 365 LEU B N 1 ATOM 7170 C CA . LEU B 1 365 ? -4.727 30.410 9.001 1.00 23.49 ? 365 LEU B CA 1 ATOM 7171 C C . LEU B 1 365 ? -5.120 30.103 7.551 1.00 24.97 ? 365 LEU B C 1 ATOM 7172 O O . LEU B 1 365 ? -5.912 29.188 7.306 1.00 26.14 ? 365 LEU B O 1 ATOM 7173 C CB . LEU B 1 365 ? -5.997 30.663 9.833 1.00 22.78 ? 365 LEU B CB 1 ATOM 7174 C CG . LEU B 1 365 ? -5.890 30.972 11.335 1.00 21.83 ? 365 LEU B CG 1 ATOM 7175 C CD1 . LEU B 1 365 ? -7.224 31.494 11.858 1.00 23.67 ? 365 LEU B CD1 1 ATOM 7176 C CD2 . LEU B 1 365 ? -5.452 29.746 12.116 1.00 21.50 ? 365 LEU B CD2 1 ATOM 7177 N N . THR B 1 366 ? -4.532 30.830 6.598 1.00 25.80 ? 366 THR B N 1 ATOM 7178 C CA . THR B 1 366 ? -4.852 30.667 5.174 1.00 27.73 ? 366 THR B CA 1 ATOM 7179 C C . THR B 1 366 ? -4.061 29.631 4.359 1.00 28.64 ? 366 THR B C 1 ATOM 7180 O O . THR B 1 366 ? -4.469 29.290 3.243 1.00 31.56 ? 366 THR B O 1 ATOM 7181 C CB . THR B 1 366 ? -4.812 32.033 4.418 1.00 28.05 ? 366 THR B CB 1 ATOM 7182 O OG1 . THR B 1 366 ? -3.470 32.535 4.378 1.00 27.42 ? 366 THR B OG1 1 ATOM 7183 C CG2 . THR B 1 366 ? -5.716 33.058 5.097 1.00 27.81 ? 366 THR B CG2 1 ATOM 7184 N N . GLY B 1 367 ? -2.957 29.123 4.906 1.00 27.99 ? 367 GLY B N 1 ATOM 7185 C CA . GLY B 1 367 ? -2.150 28.152 4.179 1.00 27.58 ? 367 GLY B CA 1 ATOM 7186 C C . GLY B 1 367 ? -2.220 26.709 4.648 1.00 27.32 ? 367 GLY B C 1 ATOM 7187 O O . GLY B 1 367 ? -3.220 26.270 5.219 1.00 28.08 ? 367 GLY B O 1 ATOM 7188 N N . THR B 1 368 ? -1.152 25.966 4.359 1.00 26.52 ? 368 THR B N 1 ATOM 7189 C CA . THR B 1 368 ? -1.013 24.560 4.732 1.00 25.36 ? 368 THR B CA 1 ATOM 7190 C C . THR B 1 368 ? 0.319 24.436 5.500 1.00 24.31 ? 368 THR B C 1 ATOM 7191 O O . THR B 1 368 ? 1.373 24.800 4.967 1.00 25.01 ? 368 THR B O 1 ATOM 7192 C CB . THR B 1 368 ? -1.035 23.622 3.480 1.00 26.84 ? 368 THR B CB 1 ATOM 7193 O OG1 . THR B 1 368 ? -2.229 23.866 2.726 1.00 27.15 ? 368 THR B OG1 1 ATOM 7194 C CG2 . THR B 1 368 ? -1.020 22.140 3.892 1.00 27.00 ? 368 THR B CG2 1 ATOM 7195 N N . PRO B 1 369 ? 0.278 24.017 6.789 1.00 22.82 ? 369 PRO B N 1 ATOM 7196 C CA . PRO B 1 369 ? -0.850 23.640 7.662 1.00 21.39 ? 369 PRO B CA 1 ATOM 7197 C C . PRO B 1 369 ? -1.652 24.835 8.203 1.00 19.31 ? 369 PRO B C 1 ATOM 7198 O O . PRO B 1 369 ? -1.368 25.980 7.847 1.00 18.19 ? 369 PRO B O 1 ATOM 7199 C CB . PRO B 1 369 ? -0.159 22.869 8.778 1.00 21.16 ? 369 PRO B CB 1 ATOM 7200 C CG . PRO B 1 369 ? 1.155 23.576 8.895 1.00 22.20 ? 369 PRO B CG 1 ATOM 7201 C CD . PRO B 1 369 ? 1.560 23.714 7.460 1.00 23.76 ? 369 PRO B CD 1 ATOM 7202 N N . LEU B 1 370 ? -2.658 24.561 9.032 1.00 18.76 ? 370 LEU B N 1 ATOM 7203 C CA . LEU B 1 370 ? -3.509 25.609 9.600 1.00 18.75 ? 370 LEU B CA 1 ATOM 7204 C C . LEU B 1 370 ? -2.783 26.602 10.513 1.00 18.33 ? 370 LEU B C 1 ATOM 7205 O O . LEU B 1 370 ? -2.930 27.813 10.347 1.00 19.27 ? 370 LEU B O 1 ATOM 7206 C CB . LEU B 1 370 ? -4.701 24.983 10.336 1.00 19.18 ? 370 LEU B CB 1 ATOM 7207 C CG . LEU B 1 370 ? -5.828 25.887 10.855 1.00 19.49 ? 370 LEU B CG 1 ATOM 7208 C CD1 . LEU B 1 370 ? -6.550 26.618 9.714 1.00 20.42 ? 370 LEU B CD1 1 ATOM 7209 C CD2 . LEU B 1 370 ? -6.803 25.034 11.617 1.00 19.62 ? 370 LEU B CD2 1 ATOM 7210 N N . PHE B 1 371 ? -1.988 26.085 11.448 1.00 16.90 ? 371 PHE B N 1 ATOM 7211 C CA . PHE B 1 371 ? -1.253 26.931 12.383 1.00 16.94 ? 371 PHE B CA 1 ATOM 7212 C C . PHE B 1 371 ? 0.170 27.239 11.930 1.00 16.23 ? 371 PHE B C 1 ATOM 7213 O O . PHE B 1 371 ? 1.093 26.442 12.112 1.00 13.53 ? 371 PHE B O 1 ATOM 7214 C CB . PHE B 1 371 ? -1.286 26.338 13.800 1.00 19.29 ? 371 PHE B CB 1 ATOM 7215 C CG . PHE B 1 371 ? -2.661 26.335 14.420 1.00 23.70 ? 371 PHE B CG 1 ATOM 7216 C CD1 . PHE B 1 371 ? -3.179 27.500 15.019 1.00 25.34 ? 371 PHE B CD1 1 ATOM 7217 C CD2 . PHE B 1 371 ? -3.466 25.182 14.372 1.00 22.90 ? 371 PHE B CD2 1 ATOM 7218 C CE1 . PHE B 1 371 ? -4.493 27.524 15.563 1.00 27.31 ? 371 PHE B CE1 1 ATOM 7219 C CE2 . PHE B 1 371 ? -4.785 25.186 14.912 1.00 24.41 ? 371 PHE B CE2 1 ATOM 7220 C CZ . PHE B 1 371 ? -5.300 26.360 15.508 1.00 26.00 ? 371 PHE B CZ 1 ATOM 7221 N N . VAL B 1 372 ? 0.299 28.374 11.247 1.00 14.93 ? 372 VAL B N 1 ATOM 7222 C CA . VAL B 1 372 ? 1.576 28.862 10.744 1.00 15.29 ? 372 VAL B CA 1 ATOM 7223 C C . VAL B 1 372 ? 1.800 30.223 11.412 1.00 15.84 ? 372 VAL B C 1 ATOM 7224 O O . VAL B 1 372 ? 0.984 31.144 11.274 1.00 13.17 ? 372 VAL B O 1 ATOM 7225 C CB . VAL B 1 372 ? 1.576 28.979 9.186 1.00 16.54 ? 372 VAL B CB 1 ATOM 7226 C CG1 . VAL B 1 372 ? 2.889 29.528 8.685 1.00 18.03 ? 372 VAL B CG1 1 ATOM 7227 C CG2 . VAL B 1 372 ? 1.356 27.608 8.541 1.00 16.92 ? 372 VAL B CG2 1 ATOM 7228 N N . TRP B 1 373 ? 2.880 30.311 12.183 1.00 13.82 ? 373 TRP B N 1 ATOM 7229 C CA . TRP B 1 373 ? 3.234 31.532 12.893 1.00 14.66 ? 373 TRP B CA 1 ATOM 7230 C C . TRP B 1 373 ? 4.234 32.351 12.098 1.00 15.24 ? 373 TRP B C 1 ATOM 7231 O O . TRP B 1 373 ? 5.286 31.851 11.709 1.00 14.56 ? 373 TRP B O 1 ATOM 7232 C CB . TRP B 1 373 ? 3.789 31.197 14.275 1.00 13.67 ? 373 TRP B CB 1 ATOM 7233 C CG . TRP B 1 373 ? 2.768 30.637 15.222 1.00 12.99 ? 373 TRP B CG 1 ATOM 7234 C CD1 . TRP B 1 373 ? 2.534 29.316 15.483 1.00 11.93 ? 373 TRP B CD1 1 ATOM 7235 C CD2 . TRP B 1 373 ? 1.835 31.377 16.022 1.00 11.09 ? 373 TRP B CD2 1 ATOM 7236 N NE1 . TRP B 1 373 ? 1.515 29.181 16.396 1.00 13.02 ? 373 TRP B NE1 1 ATOM 7237 C CE2 . TRP B 1 373 ? 1.063 30.427 16.747 1.00 13.50 ? 373 TRP B CE2 1 ATOM 7238 C CE3 . TRP B 1 373 ? 1.567 32.754 16.197 1.00 12.57 ? 373 TRP B CE3 1 ATOM 7239 C CZ2 . TRP B 1 373 ? 0.029 30.807 17.642 1.00 13.26 ? 373 TRP B CZ2 1 ATOM 7240 C CZ3 . TRP B 1 373 ? 0.535 33.142 17.090 1.00 11.34 ? 373 TRP B CZ3 1 ATOM 7241 C CH2 . TRP B 1 373 ? -0.221 32.162 17.800 1.00 12.50 ? 373 TRP B CH2 1 ATOM 7242 N N . LYS B 1 374 ? 3.882 33.608 11.842 1.00 14.70 ? 374 LYS B N 1 ATOM 7243 C CA . LYS B 1 374 ? 4.726 34.507 11.061 1.00 16.18 ? 374 LYS B CA 1 ATOM 7244 C C . LYS B 1 374 ? 5.210 35.726 11.829 1.00 16.51 ? 374 LYS B C 1 ATOM 7245 O O . LYS B 1 374 ? 4.483 36.274 12.656 1.00 16.61 ? 374 LYS B O 1 ATOM 7246 C CB . LYS B 1 374 ? 3.985 34.967 9.793 1.00 17.04 ? 374 LYS B CB 1 ATOM 7247 C CG . LYS B 1 374 ? 3.645 33.846 8.812 1.00 19.42 ? 374 LYS B CG 1 ATOM 7248 C CD . LYS B 1 374 ? 3.073 34.359 7.506 1.00 19.84 ? 374 LYS B CD 1 ATOM 7249 C CE . LYS B 1 374 ? 2.980 33.227 6.492 1.00 21.98 ? 374 LYS B CE 1 ATOM 7250 N NZ . LYS B 1 374 ? 2.405 33.687 5.195 1.00 23.64 ? 374 LYS B NZ 1 ATOM 7251 N N . VAL B 1 375 ? 6.475 36.088 11.616 1.00 16.79 ? 375 VAL B N 1 ATOM 7252 C CA . VAL B 1 375 ? 7.050 37.279 12.241 1.00 16.37 ? 375 VAL B CA 1 ATOM 7253 C C . VAL B 1 375 ? 7.478 38.172 11.082 1.00 16.65 ? 375 VAL B C 1 ATOM 7254 O O . VAL B 1 375 ? 8.322 37.789 10.264 1.00 13.89 ? 375 VAL B O 1 ATOM 7255 C CB . VAL B 1 375 ? 8.255 36.992 13.172 1.00 17.01 ? 375 VAL B CB 1 ATOM 7256 C CG1 . VAL B 1 375 ? 8.588 38.250 13.979 1.00 17.33 ? 375 VAL B CG1 1 ATOM 7257 C CG2 . VAL B 1 375 ? 7.951 35.849 14.131 1.00 16.84 ? 375 VAL B CG2 1 ATOM 7258 N N . ASN B 1 376 ? 6.850 39.348 11.013 1.00 17.51 ? 376 ASN B N 1 ATOM 7259 C CA . ASN B 1 376 ? 7.063 40.358 9.966 1.00 18.73 ? 376 ASN B CA 1 ATOM 7260 C C . ASN B 1 376 ? 6.678 39.832 8.573 1.00 18.61 ? 376 ASN B C 1 ATOM 7261 O O . ASN B 1 376 ? 7.315 40.143 7.559 1.00 19.84 ? 376 ASN B O 1 ATOM 7262 C CB . ASN B 1 376 ? 8.491 40.949 10.008 1.00 19.04 ? 376 ASN B CB 1 ATOM 7263 C CG . ASN B 1 376 ? 8.540 42.396 9.523 1.00 23.34 ? 376 ASN B CG 1 ATOM 7264 O OD1 . ASN B 1 376 ? 7.565 43.143 9.677 1.00 19.69 ? 376 ASN B OD1 1 ATOM 7265 N ND2 . ASN B 1 376 ? 9.666 42.787 8.929 1.00 25.62 ? 376 ASN B ND2 1 ATOM 7266 N N . GLY B 1 377 ? 5.629 39.010 8.565 1.00 18.09 ? 377 GLY B N 1 ATOM 7267 C CA . GLY B 1 377 ? 5.100 38.418 7.345 1.00 17.88 ? 377 GLY B CA 1 ATOM 7268 C C . GLY B 1 377 ? 5.739 37.117 6.895 1.00 17.39 ? 377 GLY B C 1 ATOM 7269 O O . GLY B 1 377 ? 5.365 36.585 5.845 1.00 17.06 ? 377 GLY B O 1 ATOM 7270 N N . SER B 1 378 ? 6.658 36.575 7.696 1.00 16.40 ? 378 SER B N 1 ATOM 7271 C CA . SER B 1 378 ? 7.351 35.342 7.324 1.00 15.73 ? 378 SER B CA 1 ATOM 7272 C C . SER B 1 378 ? 7.554 34.330 8.450 1.00 15.69 ? 378 SER B C 1 ATOM 7273 O O . SER B 1 378 ? 7.950 34.687 9.565 1.00 14.07 ? 378 SER B O 1 ATOM 7274 C CB . SER B 1 378 ? 8.705 35.688 6.685 1.00 15.38 ? 378 SER B CB 1 ATOM 7275 O OG . SER B 1 378 ? 9.500 34.533 6.451 1.00 15.99 ? 378 SER B OG 1 ATOM 7276 N N . ASP B 1 379 ? 7.230 33.072 8.150 1.00 13.86 ? 379 ASP B N 1 ATOM 7277 C CA . ASP B 1 379 ? 7.420 31.969 9.088 1.00 12.72 ? 379 ASP B CA 1 ATOM 7278 C C . ASP B 1 379 ? 8.831 31.449 8.869 1.00 12.70 ? 379 ASP B C 1 ATOM 7279 O O . ASP B 1 379 ? 9.220 31.169 7.727 1.00 12.64 ? 379 ASP B O 1 ATOM 7280 C CB . ASP B 1 379 ? 6.375 30.850 8.898 1.00 13.02 ? 379 ASP B CB 1 ATOM 7281 C CG . ASP B 1 379 ? 6.255 30.354 7.455 1.00 15.47 ? 379 ASP B CG 1 ATOM 7282 O OD1 . ASP B 1 379 ? 5.904 31.162 6.567 1.00 13.22 ? 379 ASP B OD1 1 ATOM 7283 O OD2 . ASP B 1 379 ? 6.476 29.142 7.229 1.00 14.89 ? 379 ASP B OD2 1 ATOM 7284 N N . ILE B 1 380 ? 9.607 31.356 9.946 1.00 12.00 ? 380 ILE B N 1 ATOM 7285 C CA . ILE B 1 380 ? 10.986 30.891 9.827 1.00 11.27 ? 380 ILE B CA 1 ATOM 7286 C C . ILE B 1 380 ? 11.091 29.426 9.377 1.00 12.33 ? 380 ILE B C 1 ATOM 7287 O O . ILE B 1 380 ? 10.244 28.597 9.717 1.00 12.58 ? 380 ILE B O 1 ATOM 7288 C CB . ILE B 1 380 ? 11.825 31.176 11.125 1.00 11.01 ? 380 ILE B CB 1 ATOM 7289 C CG1 . ILE B 1 380 ? 13.323 31.295 10.775 1.00 11.15 ? 380 ILE B CG1 1 ATOM 7290 C CG2 . ILE B 1 380 ? 11.603 30.077 12.175 1.00 10.52 ? 380 ILE B CG2 1 ATOM 7291 C CD1 . ILE B 1 380 ? 14.211 31.906 11.861 1.00 8.23 ? 380 ILE B CD1 1 ATOM 7292 N N . ASN B 1 381 ? 12.051 29.177 8.494 1.00 14.04 ? 381 ASN B N 1 ATOM 7293 C CA . ASN B 1 381 ? 12.339 27.844 7.976 1.00 16.00 ? 381 ASN B CA 1 ATOM 7294 C C . ASN B 1 381 ? 13.817 27.893 7.628 1.00 15.81 ? 381 ASN B C 1 ATOM 7295 O O . ASN B 1 381 ? 14.209 28.495 6.628 1.00 15.59 ? 381 ASN B O 1 ATOM 7296 C CB . ASN B 1 381 ? 11.483 27.504 6.742 1.00 17.87 ? 381 ASN B CB 1 ATOM 7297 C CG . ASN B 1 381 ? 11.567 26.033 6.362 1.00 21.57 ? 381 ASN B CG 1 ATOM 7298 O OD1 . ASN B 1 381 ? 11.083 25.166 7.086 1.00 27.21 ? 381 ASN B OD1 1 ATOM 7299 N ND2 . ASN B 1 381 ? 12.193 25.748 5.227 1.00 23.62 ? 381 ASN B ND2 1 ATOM 7300 N N . VAL B 1 382 ? 14.633 27.321 8.509 1.00 14.39 ? 382 VAL B N 1 ATOM 7301 C CA . VAL B 1 382 ? 16.081 27.309 8.320 1.00 14.39 ? 382 VAL B CA 1 ATOM 7302 C C . VAL B 1 382 ? 16.527 26.116 7.486 1.00 13.46 ? 382 VAL B C 1 ATOM 7303 O O . VAL B 1 382 ? 15.789 25.135 7.348 1.00 13.76 ? 382 VAL B O 1 ATOM 7304 C CB . VAL B 1 382 ? 16.838 27.326 9.687 1.00 14.04 ? 382 VAL B CB 1 ATOM 7305 C CG1 . VAL B 1 382 ? 16.466 28.566 10.483 1.00 14.65 ? 382 VAL B CG1 1 ATOM 7306 C CG2 . VAL B 1 382 ? 16.558 26.053 10.502 1.00 12.04 ? 382 VAL B CG2 1 ATOM 7307 N N . ASP B 1 383 ? 17.723 26.218 6.916 1.00 12.59 ? 383 ASP B N 1 ATOM 7308 C CA . ASP B 1 383 ? 18.274 25.132 6.121 1.00 12.86 ? 383 ASP B CA 1 ATOM 7309 C C . ASP B 1 383 ? 19.329 24.439 6.974 1.00 13.75 ? 383 ASP B C 1 ATOM 7310 O O . ASP B 1 383 ? 20.414 24.986 7.218 1.00 14.58 ? 383 ASP B O 1 ATOM 7311 C CB . ASP B 1 383 ? 18.874 25.656 4.805 1.00 14.72 ? 383 ASP B CB 1 ATOM 7312 C CG . ASP B 1 383 ? 19.237 24.535 3.816 1.00 17.40 ? 383 ASP B CG 1 ATOM 7313 O OD1 . ASP B 1 383 ? 19.316 23.346 4.207 1.00 15.83 ? 383 ASP B OD1 1 ATOM 7314 O OD2 . ASP B 1 383 ? 19.452 24.857 2.628 1.00 21.57 ? 383 ASP B OD2 1 ATOM 7315 N N . TRP B 1 384 ? 18.994 23.227 7.416 1.00 13.68 ? 384 TRP B N 1 ATOM 7316 C CA . TRP B 1 384 ? 19.876 22.392 8.232 1.00 14.39 ? 384 TRP B CA 1 ATOM 7317 C C . TRP B 1 384 ? 21.204 22.125 7.514 1.00 13.67 ? 384 TRP B C 1 ATOM 7318 O O . TRP B 1 384 ? 22.258 22.088 8.150 1.00 14.01 ? 384 TRP B O 1 ATOM 7319 C CB . TRP B 1 384 ? 19.195 21.053 8.550 1.00 13.79 ? 384 TRP B CB 1 ATOM 7320 C CG . TRP B 1 384 ? 18.157 21.067 9.668 1.00 14.56 ? 384 TRP B CG 1 ATOM 7321 C CD1 . TRP B 1 384 ? 18.060 21.956 10.714 1.00 15.49 ? 384 TRP B CD1 1 ATOM 7322 C CD2 . TRP B 1 384 ? 17.097 20.118 9.856 1.00 14.33 ? 384 TRP B CD2 1 ATOM 7323 N NE1 . TRP B 1 384 ? 17.007 21.614 11.537 1.00 15.47 ? 384 TRP B NE1 1 ATOM 7324 C CE2 . TRP B 1 384 ? 16.398 20.493 11.037 1.00 13.71 ? 384 TRP B CE2 1 ATOM 7325 C CE3 . TRP B 1 384 ? 16.666 18.980 9.140 1.00 14.42 ? 384 TRP B CE3 1 ATOM 7326 C CZ2 . TRP B 1 384 ? 15.276 19.765 11.523 1.00 14.04 ? 384 TRP B CZ2 1 ATOM 7327 C CZ3 . TRP B 1 384 ? 15.544 18.249 9.626 1.00 15.65 ? 384 TRP B CZ3 1 ATOM 7328 C CH2 . TRP B 1 384 ? 14.867 18.655 10.807 1.00 13.87 ? 384 TRP B CH2 1 ATOM 7329 N N . GLY B 1 385 ? 21.125 22.017 6.183 1.00 13.29 ? 385 GLY B N 1 ATOM 7330 C CA . GLY B 1 385 ? 22.279 21.761 5.332 1.00 12.36 ? 385 GLY B CA 1 ATOM 7331 C C . GLY B 1 385 ? 23.067 22.989 4.908 1.00 15.16 ? 385 GLY B C 1 ATOM 7332 O O . GLY B 1 385 ? 24.154 22.849 4.338 1.00 14.97 ? 385 GLY B O 1 ATOM 7333 N N . LYS B 1 386 ? 22.498 24.179 5.113 1.00 12.54 ? 386 LYS B N 1 ATOM 7334 C CA . LYS B 1 386 ? 23.184 25.435 4.789 1.00 14.67 ? 386 LYS B CA 1 ATOM 7335 C C . LYS B 1 386 ? 22.844 26.516 5.823 1.00 14.14 ? 386 LYS B C 1 ATOM 7336 O O . LYS B 1 386 ? 21.958 27.358 5.608 1.00 14.33 ? 386 LYS B O 1 ATOM 7337 C CB . LYS B 1 386 ? 22.891 25.927 3.365 1.00 15.39 ? 386 LYS B CB 1 ATOM 7338 C CG . LYS B 1 386 ? 23.979 26.871 2.853 1.00 18.58 ? 386 LYS B CG 1 ATOM 7339 C CD . LYS B 1 386 ? 23.668 27.437 1.483 1.00 21.29 ? 386 LYS B CD 1 ATOM 7340 C CE . LYS B 1 386 ? 24.701 28.480 1.074 1.00 21.49 ? 386 LYS B CE 1 ATOM 7341 N NZ . LYS B 1 386 ? 26.014 27.903 0.691 1.00 22.54 ? 386 LYS B NZ 1 ATOM 7342 N N . PRO B 1 387 ? 23.541 26.492 6.977 1.00 14.77 ? 387 PRO B N 1 ATOM 7343 C CA . PRO B 1 387 ? 23.338 27.453 8.063 1.00 12.81 ? 387 PRO B CA 1 ATOM 7344 C C . PRO B 1 387 ? 23.751 28.862 7.695 1.00 11.45 ? 387 PRO B C 1 ATOM 7345 O O . PRO B 1 387 ? 24.528 29.049 6.764 1.00 10.71 ? 387 PRO B O 1 ATOM 7346 C CB . PRO B 1 387 ? 24.233 26.901 9.172 1.00 12.36 ? 387 PRO B CB 1 ATOM 7347 C CG . PRO B 1 387 ? 24.263 25.459 8.879 1.00 14.10 ? 387 PRO B CG 1 ATOM 7348 C CD . PRO B 1 387 ? 24.488 25.454 7.415 1.00 14.78 ? 387 PRO B CD 1 ATOM 7349 N N . ILE B 1 388 ? 23.241 29.844 8.441 1.00 11.55 ? 388 ILE B N 1 ATOM 7350 C CA . ILE B 1 388 ? 23.562 31.262 8.221 1.00 11.22 ? 388 ILE B CA 1 ATOM 7351 C C . ILE B 1 388 ? 25.072 31.495 8.304 1.00 11.96 ? 388 ILE B C 1 ATOM 7352 O O . ILE B 1 388 ? 25.626 32.305 7.555 1.00 13.85 ? 388 ILE B O 1 ATOM 7353 C CB . ILE B 1 388 ? 22.768 32.171 9.208 1.00 11.67 ? 388 ILE B CB 1 ATOM 7354 C CG1 . ILE B 1 388 ? 21.266 32.050 8.908 1.00 12.71 ? 388 ILE B CG1 1 ATOM 7355 C CG2 . ILE B 1 388 ? 23.215 33.651 9.124 1.00 8.56 ? 388 ILE B CG2 1 ATOM 7356 C CD1 . ILE B 1 388 ? 20.866 32.451 7.477 1.00 13.98 ? 388 ILE B CD1 1 ATOM 7357 N N . ILE B 1 389 ? 25.734 30.702 9.144 1.00 12.42 ? 389 ILE B N 1 ATOM 7358 C CA . ILE B 1 389 ? 27.183 30.782 9.303 1.00 13.41 ? 389 ILE B CA 1 ATOM 7359 C C . ILE B 1 389 ? 27.912 30.344 8.020 1.00 13.03 ? 389 ILE B C 1 ATOM 7360 O O . ILE B 1 389 ? 28.978 30.877 7.719 1.00 13.05 ? 389 ILE B O 1 ATOM 7361 C CB . ILE B 1 389 ? 27.645 30.036 10.590 1.00 12.23 ? 389 ILE B CB 1 ATOM 7362 C CG1 . ILE B 1 389 ? 27.242 30.856 11.827 1.00 14.83 ? 389 ILE B CG1 1 ATOM 7363 C CG2 . ILE B 1 389 ? 29.149 29.746 10.591 1.00 13.67 ? 389 ILE B CG2 1 ATOM 7364 C CD1 . ILE B 1 389 ? 27.792 32.291 11.897 1.00 14.47 ? 389 ILE B CD1 1 ATOM 7365 N N . ASP B 1 390 ? 27.290 29.460 7.229 1.00 13.14 ? 390 ASP B N 1 ATOM 7366 C CA . ASP B 1 390 ? 27.877 29.016 5.952 1.00 14.39 ? 390 ASP B CA 1 ATOM 7367 C C . ASP B 1 390 ? 27.872 30.187 4.974 1.00 13.47 ? 390 ASP B C 1 ATOM 7368 O O . ASP B 1 390 ? 28.839 30.382 4.233 1.00 13.08 ? 390 ASP B O 1 ATOM 7369 C CB . ASP B 1 390 ? 27.123 27.819 5.358 1.00 14.91 ? 390 ASP B CB 1 ATOM 7370 C CG . ASP B 1 390 ? 27.885 27.153 4.221 1.00 18.15 ? 390 ASP B CG 1 ATOM 7371 O OD1 . ASP B 1 390 ? 29.000 26.642 4.463 1.00 20.45 ? 390 ASP B OD1 1 ATOM 7372 O OD2 . ASP B 1 390 ? 27.373 27.150 3.087 1.00 18.67 ? 390 ASP B OD2 1 ATOM 7373 N N . TYR B 1 391 ? 26.812 30.997 5.038 1.00 12.30 ? 391 TYR B N 1 ATOM 7374 C CA . TYR B 1 391 ? 26.676 32.188 4.201 1.00 13.44 ? 391 TYR B CA 1 ATOM 7375 C C . TYR B 1 391 ? 27.753 33.215 4.583 1.00 13.84 ? 391 TYR B C 1 ATOM 7376 O O . TYR B 1 391 ? 28.399 33.796 3.712 1.00 15.15 ? 391 TYR B O 1 ATOM 7377 C CB . TYR B 1 391 ? 25.293 32.824 4.369 1.00 14.15 ? 391 TYR B CB 1 ATOM 7378 C CG . TYR B 1 391 ? 24.148 32.085 3.712 1.00 15.41 ? 391 TYR B CG 1 ATOM 7379 C CD1 . TYR B 1 391 ? 23.526 30.997 4.352 1.00 15.26 ? 391 TYR B CD1 1 ATOM 7380 C CD2 . TYR B 1 391 ? 23.658 32.484 2.453 1.00 12.79 ? 391 TYR B CD2 1 ATOM 7381 C CE1 . TYR B 1 391 ? 22.431 30.319 3.753 1.00 16.08 ? 391 TYR B CE1 1 ATOM 7382 C CE2 . TYR B 1 391 ? 22.568 31.813 1.837 1.00 15.59 ? 391 TYR B CE2 1 ATOM 7383 C CZ . TYR B 1 391 ? 21.965 30.734 2.498 1.00 14.69 ? 391 TYR B CZ 1 ATOM 7384 O OH . TYR B 1 391 ? 20.926 30.058 1.908 1.00 16.93 ? 391 TYR B OH 1 ATOM 7385 N N . ILE B 1 392 ? 27.982 33.364 5.890 1.00 13.28 ? 392 ILE B N 1 ATOM 7386 C CA . ILE B 1 392 ? 28.983 34.288 6.440 1.00 15.68 ? 392 ILE B CA 1 ATOM 7387 C C . ILE B 1 392 ? 30.404 33.892 6.014 1.00 15.76 ? 392 ILE B C 1 ATOM 7388 O O . ILE B 1 392 ? 31.167 34.735 5.539 1.00 16.96 ? 392 ILE B O 1 ATOM 7389 C CB . ILE B 1 392 ? 28.861 34.364 8.008 1.00 14.64 ? 392 ILE B CB 1 ATOM 7390 C CG1 . ILE B 1 392 ? 27.568 35.095 8.406 1.00 14.70 ? 392 ILE B CG1 1 ATOM 7391 C CG2 . ILE B 1 392 ? 30.114 34.981 8.671 1.00 15.56 ? 392 ILE B CG2 1 ATOM 7392 C CD1 . ILE B 1 392 ? 27.510 36.581 8.039 1.00 13.19 ? 392 ILE B CD1 1 ATOM 7393 N N . LEU B 1 393 ? 30.718 32.602 6.141 1.00 16.64 ? 393 LEU B N 1 ATOM 7394 C CA . LEU B 1 393 ? 32.038 32.066 5.787 1.00 18.12 ? 393 LEU B CA 1 ATOM 7395 C C . LEU B 1 393 ? 32.352 32.029 4.291 1.00 18.12 ? 393 LEU B C 1 ATOM 7396 O O . LEU B 1 393 ? 33.518 31.926 3.905 1.00 20.67 ? 393 LEU B O 1 ATOM 7397 C CB . LEU B 1 393 ? 32.231 30.679 6.402 1.00 17.20 ? 393 LEU B CB 1 ATOM 7398 C CG . LEU B 1 393 ? 32.376 30.649 7.928 1.00 18.66 ? 393 LEU B CG 1 ATOM 7399 C CD1 . LEU B 1 393 ? 32.292 29.217 8.408 1.00 18.91 ? 393 LEU B CD1 1 ATOM 7400 C CD2 . LEU B 1 393 ? 33.683 31.313 8.376 1.00 16.76 ? 393 LEU B CD2 1 ATOM 7401 N N . THR B 1 394 ? 31.313 32.118 3.463 1.00 17.56 ? 394 THR B N 1 ATOM 7402 C CA . THR B 1 394 ? 31.473 32.112 2.009 1.00 17.64 ? 394 THR B CA 1 ATOM 7403 C C . THR B 1 394 ? 31.228 33.491 1.381 1.00 18.99 ? 394 THR B C 1 ATOM 7404 O O . THR B 1 394 ? 31.260 33.629 0.153 1.00 19.35 ? 394 THR B O 1 ATOM 7405 C CB . THR B 1 394 ? 30.558 31.059 1.328 1.00 17.60 ? 394 THR B CB 1 ATOM 7406 O OG1 . THR B 1 394 ? 29.196 31.288 1.701 1.00 16.81 ? 394 THR B OG1 1 ATOM 7407 C CG2 . THR B 1 394 ? 30.965 29.635 1.726 1.00 15.93 ? 394 THR B CG2 1 ATOM 7408 N N . GLY B 1 395 ? 30.975 34.497 2.227 1.00 18.57 ? 395 GLY B N 1 ATOM 7409 C CA . GLY B 1 395 ? 30.730 35.864 1.770 1.00 19.15 ? 395 GLY B CA 1 ATOM 7410 C C . GLY B 1 395 ? 29.457 36.035 0.962 1.00 20.83 ? 395 GLY B C 1 ATOM 7411 O O . GLY B 1 395 ? 29.384 36.850 0.037 1.00 21.97 ? 395 GLY B O 1 ATOM 7412 N N . ASN B 1 396 ? 28.459 35.239 1.326 1.00 20.86 ? 396 ASN B N 1 ATOM 7413 C CA . ASN B 1 396 ? 27.160 35.218 0.676 1.00 21.18 ? 396 ASN B CA 1 ATOM 7414 C C . ASN B 1 396 ? 26.167 36.025 1.519 1.00 22.04 ? 396 ASN B C 1 ATOM 7415 O O . ASN B 1 396 ? 25.916 35.698 2.684 1.00 21.51 ? 396 ASN B O 1 ATOM 7416 C CB . ASN B 1 396 ? 26.732 33.755 0.568 1.00 21.01 ? 396 ASN B CB 1 ATOM 7417 C CG . ASN B 1 396 ? 25.562 33.527 -0.360 1.00 20.78 ? 396 ASN B CG 1 ATOM 7418 O OD1 . ASN B 1 396 ? 24.782 34.423 -0.692 1.00 19.89 ? 396 ASN B OD1 1 ATOM 7419 N ND2 . ASN B 1 396 ? 25.449 32.266 -0.759 1.00 20.35 ? 396 ASN B ND2 1 ATOM 7420 N N . THR B 1 397 ? 25.626 37.085 0.921 1.00 21.18 ? 397 THR B N 1 ATOM 7421 C CA . THR B 1 397 ? 24.662 37.956 1.588 1.00 20.41 ? 397 THR B CA 1 ATOM 7422 C C . THR B 1 397 ? 23.224 37.706 1.127 1.00 20.53 ? 397 THR B C 1 ATOM 7423 O O . THR B 1 397 ? 22.290 38.338 1.630 1.00 20.71 ? 397 THR B O 1 ATOM 7424 C CB . THR B 1 397 ? 25.004 39.459 1.396 1.00 20.42 ? 397 THR B CB 1 ATOM 7425 O OG1 . THR B 1 397 ? 25.073 39.765 -0.002 1.00 19.09 ? 397 THR B OG1 1 ATOM 7426 C CG2 . THR B 1 397 ? 26.332 39.810 2.071 1.00 22.43 ? 397 THR B CG2 1 ATOM 7427 N N . SER B 1 398 ? 23.055 36.769 0.192 1.00 19.59 ? 398 SER B N 1 ATOM 7428 C CA . SER B 1 398 ? 21.740 36.427 -0.357 1.00 20.47 ? 398 SER B CA 1 ATOM 7429 C C . SER B 1 398 ? 20.991 35.425 0.526 1.00 20.27 ? 398 SER B C 1 ATOM 7430 O O . SER B 1 398 ? 20.732 34.282 0.132 1.00 20.55 ? 398 SER B O 1 ATOM 7431 C CB . SER B 1 398 ? 21.875 35.906 -1.796 1.00 21.21 ? 398 SER B CB 1 ATOM 7432 O OG . SER B 1 398 ? 22.446 36.888 -2.643 1.00 25.37 ? 398 SER B OG 1 ATOM 7433 N N . TYR B 1 399 ? 20.639 35.884 1.728 1.00 19.46 ? 399 TYR B N 1 ATOM 7434 C CA . TYR B 1 399 ? 19.914 35.076 2.712 1.00 19.09 ? 399 TYR B CA 1 ATOM 7435 C C . TYR B 1 399 ? 18.461 34.937 2.269 1.00 18.30 ? 399 TYR B C 1 ATOM 7436 O O . TYR B 1 399 ? 17.830 35.944 1.933 1.00 18.75 ? 399 TYR B O 1 ATOM 7437 C CB . TYR B 1 399 ? 19.920 35.758 4.087 1.00 18.57 ? 399 TYR B CB 1 ATOM 7438 C CG . TYR B 1 399 ? 21.242 36.349 4.517 1.00 18.41 ? 399 TYR B CG 1 ATOM 7439 C CD1 . TYR B 1 399 ? 22.367 35.528 4.742 1.00 18.30 ? 399 TYR B CD1 1 ATOM 7440 C CD2 . TYR B 1 399 ? 21.383 37.739 4.685 1.00 17.67 ? 399 TYR B CD2 1 ATOM 7441 C CE1 . TYR B 1 399 ? 23.615 36.085 5.123 1.00 17.12 ? 399 TYR B CE1 1 ATOM 7442 C CE2 . TYR B 1 399 ? 22.626 38.310 5.065 1.00 17.59 ? 399 TYR B CE2 1 ATOM 7443 C CZ . TYR B 1 399 ? 23.734 37.469 5.279 1.00 16.05 ? 399 TYR B CZ 1 ATOM 7444 O OH . TYR B 1 399 ? 24.947 38.004 5.633 1.00 17.42 ? 399 TYR B OH 1 ATOM 7445 N N . PRO B 1 400 ? 17.923 33.695 2.212 1.00 18.07 ? 400 PRO B N 1 ATOM 7446 C CA . PRO B 1 400 ? 16.522 33.540 1.798 1.00 18.43 ? 400 PRO B CA 1 ATOM 7447 C C . PRO B 1 400 ? 15.564 34.171 2.801 1.00 18.05 ? 400 PRO B C 1 ATOM 7448 O O . PRO B 1 400 ? 15.912 34.345 3.979 1.00 16.81 ? 400 PRO B O 1 ATOM 7449 C CB . PRO B 1 400 ? 16.344 32.021 1.689 1.00 20.20 ? 400 PRO B CB 1 ATOM 7450 C CG . PRO B 1 400 ? 17.407 31.457 2.532 1.00 20.64 ? 400 PRO B CG 1 ATOM 7451 C CD . PRO B 1 400 ? 18.575 32.378 2.327 1.00 18.54 ? 400 PRO B CD 1 ATOM 7452 N N . VAL B 1 401 ? 14.387 34.554 2.307 1.00 17.39 ? 401 VAL B N 1 ATOM 7453 C CA . VAL B 1 401 ? 13.339 35.206 3.102 1.00 18.68 ? 401 VAL B CA 1 ATOM 7454 C C . VAL B 1 401 ? 12.930 34.388 4.328 1.00 18.22 ? 401 VAL B C 1 ATOM 7455 O O . VAL B 1 401 ? 12.779 34.945 5.419 1.00 16.77 ? 401 VAL B O 1 ATOM 7456 C CB . VAL B 1 401 ? 12.083 35.514 2.229 1.00 20.37 ? 401 VAL B CB 1 ATOM 7457 C CG1 . VAL B 1 401 ? 11.064 36.369 3.004 1.00 20.71 ? 401 VAL B CG1 1 ATOM 7458 C CG2 . VAL B 1 401 ? 12.499 36.242 0.945 1.00 22.43 ? 401 VAL B CG2 1 ATOM 7459 N N . SER B 1 402 ? 12.870 33.066 4.153 1.00 17.49 ? 402 SER B N 1 ATOM 7460 C CA . SER B 1 402 ? 12.480 32.127 5.206 1.00 18.80 ? 402 SER B CA 1 ATOM 7461 C C . SER B 1 402 ? 13.416 32.096 6.421 1.00 17.20 ? 402 SER B C 1 ATOM 7462 O O . SER B 1 402 ? 13.032 31.619 7.475 1.00 17.36 ? 402 SER B O 1 ATOM 7463 C CB . SER B 1 402 ? 12.308 30.718 4.629 1.00 19.06 ? 402 SER B CB 1 ATOM 7464 O OG . SER B 1 402 ? 13.553 30.147 4.266 1.00 23.54 ? 402 SER B OG 1 ATOM 7465 N N . ASP B 1 403 ? 14.630 32.624 6.275 1.00 16.81 ? 403 ASP B N 1 ATOM 7466 C CA . ASP B 1 403 ? 15.580 32.664 7.386 1.00 17.15 ? 403 ASP B CA 1 ATOM 7467 C C . ASP B 1 403 ? 15.333 33.816 8.354 1.00 15.31 ? 403 ASP B C 1 ATOM 7468 O O . ASP B 1 403 ? 15.951 33.876 9.421 1.00 15.29 ? 403 ASP B O 1 ATOM 7469 C CB . ASP B 1 403 ? 17.017 32.689 6.877 1.00 18.22 ? 403 ASP B CB 1 ATOM 7470 C CG . ASP B 1 403 ? 17.570 31.299 6.655 1.00 20.12 ? 403 ASP B CG 1 ATOM 7471 O OD1 . ASP B 1 403 ? 17.653 30.522 7.629 1.00 21.22 ? 403 ASP B OD1 1 ATOM 7472 O OD2 . ASP B 1 403 ? 17.951 30.989 5.516 1.00 20.26 ? 403 ASP B OD2 1 ATOM 7473 N N . ASN B 1 404 ? 14.406 34.705 7.977 1.00 15.07 ? 404 ASN B N 1 ATOM 7474 C CA . ASN B 1 404 ? 13.994 35.883 8.760 1.00 13.44 ? 404 ASN B CA 1 ATOM 7475 C C . ASN B 1 404 ? 15.157 36.664 9.354 1.00 13.54 ? 404 ASN B C 1 ATOM 7476 O O . ASN B 1 404 ? 15.235 36.887 10.567 1.00 13.77 ? 404 ASN B O 1 ATOM 7477 C CB . ASN B 1 404 ? 12.995 35.486 9.859 1.00 12.15 ? 404 ASN B CB 1 ATOM 7478 C CG . ASN B 1 404 ? 11.694 34.953 9.309 1.00 10.84 ? 404 ASN B CG 1 ATOM 7479 O OD1 . ASN B 1 404 ? 11.524 34.829 8.103 1.00 13.42 ? 404 ASN B OD1 1 ATOM 7480 N ND2 . ASN B 1 404 ? 10.772 34.612 10.201 1.00 11.44 ? 404 ASN B ND2 1 ATOM 7481 N N . ILE B 1 405 ? 16.094 37.019 8.484 1.00 14.09 ? 405 ILE B N 1 ATOM 7482 C CA . ILE B 1 405 ? 17.274 37.764 8.882 1.00 14.63 ? 405 ILE B CA 1 ATOM 7483 C C . ILE B 1 405 ? 16.954 39.232 9.148 1.00 15.80 ? 405 ILE B C 1 ATOM 7484 O O . ILE B 1 405 ? 16.354 39.920 8.315 1.00 16.16 ? 405 ILE B O 1 ATOM 7485 C CB . ILE B 1 405 ? 18.413 37.625 7.818 1.00 14.33 ? 405 ILE B CB 1 ATOM 7486 C CG1 . ILE B 1 405 ? 18.915 36.172 7.770 1.00 11.85 ? 405 ILE B CG1 1 ATOM 7487 C CG2 . ILE B 1 405 ? 19.563 38.621 8.076 1.00 12.57 ? 405 ILE B CG2 1 ATOM 7488 C CD1 . ILE B 1 405 ? 19.713 35.714 8.972 1.00 11.46 ? 405 ILE B CD1 1 ATOM 7489 N N . VAL B 1 406 ? 17.280 39.660 10.362 1.00 14.93 ? 406 VAL B N 1 ATOM 7490 C CA . VAL B 1 406 ? 17.120 41.049 10.773 1.00 13.82 ? 406 VAL B CA 1 ATOM 7491 C C . VAL B 1 406 ? 18.567 41.461 11.031 1.00 14.75 ? 406 VAL B C 1 ATOM 7492 O O . VAL B 1 406 ? 19.153 41.135 12.071 1.00 13.69 ? 406 VAL B O 1 ATOM 7493 C CB . VAL B 1 406 ? 16.249 41.204 12.047 1.00 12.29 ? 406 VAL B CB 1 ATOM 7494 C CG1 . VAL B 1 406 ? 16.056 42.679 12.369 1.00 13.12 ? 406 VAL B CG1 1 ATOM 7495 C CG2 . VAL B 1 406 ? 14.894 40.558 11.855 1.00 8.77 ? 406 VAL B CG2 1 ATOM 7496 N N . GLN B 1 407 ? 19.166 42.090 10.023 1.00 16.07 ? 407 GLN B N 1 ATOM 7497 C CA . GLN B 1 407 ? 20.555 42.522 10.102 1.00 17.10 ? 407 GLN B CA 1 ATOM 7498 C C . GLN B 1 407 ? 20.718 43.779 10.944 1.00 17.61 ? 407 GLN B C 1 ATOM 7499 O O . GLN B 1 407 ? 20.077 44.800 10.688 1.00 18.15 ? 407 GLN B O 1 ATOM 7500 C CB . GLN B 1 407 ? 21.133 42.722 8.703 1.00 17.55 ? 407 GLN B CB 1 ATOM 7501 C CG . GLN B 1 407 ? 22.654 42.749 8.664 1.00 18.67 ? 407 GLN B CG 1 ATOM 7502 C CD . GLN B 1 407 ? 23.198 42.758 7.252 1.00 20.79 ? 407 GLN B CD 1 ATOM 7503 O OE1 . GLN B 1 407 ? 22.812 41.935 6.418 1.00 22.05 ? 407 GLN B OE1 1 ATOM 7504 N NE2 . GLN B 1 407 ? 24.101 43.689 6.975 1.00 20.00 ? 407 GLN B NE2 1 ATOM 7505 N N . VAL B 1 408 ? 21.535 43.655 11.990 1.00 17.68 ? 408 VAL B N 1 ATOM 7506 C CA . VAL B 1 408 ? 21.818 44.751 12.913 1.00 18.69 ? 408 VAL B CA 1 ATOM 7507 C C . VAL B 1 408 ? 23.314 45.075 12.818 1.00 19.60 ? 408 VAL B C 1 ATOM 7508 O O . VAL B 1 408 ? 24.150 44.377 13.405 1.00 19.28 ? 408 VAL B O 1 ATOM 7509 C CB . VAL B 1 408 ? 21.442 44.390 14.387 1.00 18.68 ? 408 VAL B CB 1 ATOM 7510 C CG1 . VAL B 1 408 ? 21.382 45.643 15.220 1.00 18.96 ? 408 VAL B CG1 1 ATOM 7511 C CG2 . VAL B 1 408 ? 20.101 43.658 14.461 1.00 18.89 ? 408 VAL B CG2 1 ATOM 7512 N N . ASP B 1 409 ? 23.634 46.140 12.082 1.00 20.71 ? 409 ASP B N 1 ATOM 7513 C CA . ASP B 1 409 ? 25.017 46.571 11.868 1.00 23.86 ? 409 ASP B CA 1 ATOM 7514 C C . ASP B 1 409 ? 25.598 47.480 12.946 1.00 24.11 ? 409 ASP B C 1 ATOM 7515 O O . ASP B 1 409 ? 26.819 47.679 12.992 1.00 24.71 ? 409 ASP B O 1 ATOM 7516 C CB . ASP B 1 409 ? 25.165 47.228 10.489 1.00 26.71 ? 409 ASP B CB 1 ATOM 7517 C CG . ASP B 1 409 ? 25.009 46.237 9.348 1.00 29.28 ? 409 ASP B CG 1 ATOM 7518 O OD1 . ASP B 1 409 ? 25.704 45.201 9.354 1.00 30.87 ? 409 ASP B OD1 1 ATOM 7519 O OD2 . ASP B 1 409 ? 24.189 46.497 8.442 1.00 31.79 ? 409 ASP B OD2 1 ATOM 7520 N N . ALA B 1 410 ? 24.730 47.999 13.824 1.00 23.97 ? 410 ALA B N 1 ATOM 7521 C CA . ALA B 1 410 ? 25.119 48.890 14.932 1.00 22.46 ? 410 ALA B CA 1 ATOM 7522 C C . ALA B 1 410 ? 26.192 48.242 15.805 1.00 21.85 ? 410 ALA B C 1 ATOM 7523 O O . ALA B 1 410 ? 26.074 47.072 16.166 1.00 19.23 ? 410 ALA B O 1 ATOM 7524 C CB . ALA B 1 410 ? 23.898 49.244 15.772 1.00 24.28 ? 410 ALA B CB 1 ATOM 7525 N N . VAL B 1 411 ? 27.268 48.982 16.066 1.00 21.63 ? 411 VAL B N 1 ATOM 7526 C CA . VAL B 1 411 ? 28.392 48.479 16.858 1.00 21.63 ? 411 VAL B CA 1 ATOM 7527 C C . VAL B 1 411 ? 28.336 48.920 18.320 1.00 21.59 ? 411 VAL B C 1 ATOM 7528 O O . VAL B 1 411 ? 28.505 50.104 18.623 1.00 22.54 ? 411 VAL B O 1 ATOM 7529 C CB . VAL B 1 411 ? 29.762 48.890 16.224 1.00 21.04 ? 411 VAL B CB 1 ATOM 7530 C CG1 . VAL B 1 411 ? 30.914 48.236 16.965 1.00 19.33 ? 411 VAL B CG1 1 ATOM 7531 C CG2 . VAL B 1 411 ? 29.819 48.494 14.755 1.00 20.97 ? 411 VAL B CG2 1 ATOM 7532 N N . ASP B 1 412 ? 28.119 47.944 19.209 1.00 21.78 ? 412 ASP B N 1 ATOM 7533 C CA . ASP B 1 412 ? 28.032 48.127 20.672 1.00 23.11 ? 412 ASP B CA 1 ATOM 7534 C C . ASP B 1 412 ? 27.018 49.209 21.094 1.00 23.12 ? 412 ASP B C 1 ATOM 7535 O O . ASP B 1 412 ? 27.230 49.970 22.049 1.00 23.61 ? 412 ASP B O 1 ATOM 7536 C CB . ASP B 1 412 ? 29.439 48.357 21.275 1.00 25.90 ? 412 ASP B CB 1 ATOM 7537 C CG . ASP B 1 412 ? 29.506 48.064 22.777 1.00 29.54 ? 412 ASP B CG 1 ATOM 7538 O OD1 . ASP B 1 412 ? 28.816 47.134 23.254 1.00 29.29 ? 412 ASP B OD1 1 ATOM 7539 O OD2 . ASP B 1 412 ? 30.253 48.776 23.481 1.00 31.86 ? 412 ASP B OD2 1 ATOM 7540 N N . GLN B 1 413 ? 25.915 49.265 20.352 1.00 21.29 ? 413 GLN B N 1 ATOM 7541 C CA . GLN B 1 413 ? 24.847 50.229 20.599 1.00 22.42 ? 413 GLN B CA 1 ATOM 7542 C C . GLN B 1 413 ? 23.568 49.534 21.039 1.00 20.80 ? 413 GLN B C 1 ATOM 7543 O O . GLN B 1 413 ? 23.326 48.369 20.694 1.00 16.66 ? 413 GLN B O 1 ATOM 7544 C CB . GLN B 1 413 ? 24.551 51.047 19.336 1.00 25.48 ? 413 GLN B CB 1 ATOM 7545 C CG . GLN B 1 413 ? 25.626 52.047 18.932 1.00 31.83 ? 413 GLN B CG 1 ATOM 7546 C CD . GLN B 1 413 ? 25.336 52.706 17.592 1.00 35.49 ? 413 GLN B CD 1 ATOM 7547 O OE1 . GLN B 1 413 ? 24.238 53.221 17.358 1.00 38.01 ? 413 GLN B OE1 1 ATOM 7548 N NE2 . GLN B 1 413 ? 26.323 52.691 16.701 1.00 37.89 ? 413 GLN B NE2 1 ATOM 7549 N N . TRP B 1 414 ? 22.754 50.264 21.801 1.00 19.64 ? 414 TRP B N 1 ATOM 7550 C CA . TRP B 1 414 ? 21.472 49.763 22.278 1.00 19.78 ? 414 TRP B CA 1 ATOM 7551 C C . TRP B 1 414 ? 20.467 49.791 21.140 1.00 19.31 ? 414 TRP B C 1 ATOM 7552 O O . TRP B 1 414 ? 20.330 50.803 20.444 1.00 20.05 ? 414 TRP B O 1 ATOM 7553 C CB . TRP B 1 414 ? 20.957 50.596 23.458 1.00 20.23 ? 414 TRP B CB 1 ATOM 7554 C CG . TRP B 1 414 ? 21.714 50.367 24.737 1.00 19.64 ? 414 TRP B CG 1 ATOM 7555 C CD1 . TRP B 1 414 ? 22.646 51.199 25.296 1.00 21.03 ? 414 TRP B CD1 1 ATOM 7556 C CD2 . TRP B 1 414 ? 21.605 49.237 25.617 1.00 20.85 ? 414 TRP B CD2 1 ATOM 7557 N NE1 . TRP B 1 414 ? 23.127 50.660 26.469 1.00 22.71 ? 414 TRP B NE1 1 ATOM 7558 C CE2 . TRP B 1 414 ? 22.510 49.457 26.694 1.00 20.58 ? 414 TRP B CE2 1 ATOM 7559 C CE3 . TRP B 1 414 ? 20.829 48.055 25.609 1.00 20.51 ? 414 TRP B CE3 1 ATOM 7560 C CZ2 . TRP B 1 414 ? 22.665 48.536 27.758 1.00 19.41 ? 414 TRP B CZ2 1 ATOM 7561 C CZ3 . TRP B 1 414 ? 20.984 47.129 26.672 1.00 19.26 ? 414 TRP B CZ3 1 ATOM 7562 C CH2 . TRP B 1 414 ? 21.900 47.383 27.730 1.00 19.27 ? 414 TRP B CH2 1 ATOM 7563 N N . THR B 1 415 ? 19.863 48.635 20.880 1.00 17.34 ? 415 THR B N 1 ATOM 7564 C CA . THR B 1 415 ? 18.867 48.509 19.823 1.00 15.91 ? 415 THR B CA 1 ATOM 7565 C C . THR B 1 415 ? 17.525 48.193 20.453 1.00 16.65 ? 415 THR B C 1 ATOM 7566 O O . THR B 1 415 ? 17.438 47.352 21.341 1.00 14.37 ? 415 THR B O 1 ATOM 7567 C CB . THR B 1 415 ? 19.254 47.444 18.782 1.00 15.61 ? 415 THR B CB 1 ATOM 7568 O OG1 . THR B 1 415 ? 19.483 46.183 19.426 1.00 14.52 ? 415 THR B OG1 1 ATOM 7569 C CG2 . THR B 1 415 ? 20.493 47.877 18.016 1.00 15.27 ? 415 THR B CG2 1 ATOM 7570 N N . TYR B 1 416 ? 16.496 48.899 19.993 1.00 16.63 ? 416 TYR B N 1 ATOM 7571 C CA . TYR B 1 416 ? 15.136 48.779 20.512 1.00 16.98 ? 416 TYR B CA 1 ATOM 7572 C C . TYR B 1 416 ? 14.241 47.974 19.588 1.00 15.25 ? 416 TYR B C 1 ATOM 7573 O O . TYR B 1 416 ? 14.279 48.147 18.369 1.00 16.11 ? 416 TYR B O 1 ATOM 7574 C CB . TYR B 1 416 ? 14.557 50.175 20.746 1.00 18.54 ? 416 TYR B CB 1 ATOM 7575 C CG . TYR B 1 416 ? 15.395 51.039 21.665 1.00 21.98 ? 416 TYR B CG 1 ATOM 7576 C CD1 . TYR B 1 416 ? 16.500 51.775 21.171 1.00 23.38 ? 416 TYR B CD1 1 ATOM 7577 C CD2 . TYR B 1 416 ? 15.117 51.100 23.042 1.00 22.04 ? 416 TYR B CD2 1 ATOM 7578 C CE1 . TYR B 1 416 ? 17.317 52.550 22.043 1.00 24.32 ? 416 TYR B CE1 1 ATOM 7579 C CE2 . TYR B 1 416 ? 15.922 51.869 23.922 1.00 24.70 ? 416 TYR B CE2 1 ATOM 7580 C CZ . TYR B 1 416 ? 17.016 52.586 23.415 1.00 24.70 ? 416 TYR B CZ 1 ATOM 7581 O OH . TYR B 1 416 ? 17.799 53.316 24.274 1.00 26.22 ? 416 TYR B OH 1 ATOM 7582 N N . TRP B 1 417 ? 13.503 47.027 20.168 1.00 14.35 ? 417 TRP B N 1 ATOM 7583 C CA . TRP B 1 417 ? 12.619 46.141 19.405 1.00 12.59 ? 417 TRP B CA 1 ATOM 7584 C C . TRP B 1 417 ? 11.213 46.042 19.954 1.00 12.30 ? 417 TRP B C 1 ATOM 7585 O O . TRP B 1 417 ? 11.005 45.664 21.108 1.00 11.82 ? 417 TRP B O 1 ATOM 7586 C CB . TRP B 1 417 ? 13.227 44.726 19.281 1.00 13.17 ? 417 TRP B CB 1 ATOM 7587 C CG . TRP B 1 417 ? 14.618 44.750 18.748 1.00 12.59 ? 417 TRP B CG 1 ATOM 7588 C CD1 . TRP B 1 417 ? 15.765 44.808 19.488 1.00 12.63 ? 417 TRP B CD1 1 ATOM 7589 C CD2 . TRP B 1 417 ? 15.012 44.927 17.381 1.00 13.54 ? 417 TRP B CD2 1 ATOM 7590 N NE1 . TRP B 1 417 ? 16.847 45.043 18.676 1.00 13.16 ? 417 TRP B NE1 1 ATOM 7591 C CE2 . TRP B 1 417 ? 16.421 45.120 17.377 1.00 14.06 ? 417 TRP B CE2 1 ATOM 7592 C CE3 . TRP B 1 417 ? 14.315 44.955 16.154 1.00 13.45 ? 417 TRP B CE3 1 ATOM 7593 C CZ2 . TRP B 1 417 ? 17.155 45.343 16.189 1.00 12.12 ? 417 TRP B CZ2 1 ATOM 7594 C CZ3 . TRP B 1 417 ? 15.046 45.179 14.963 1.00 13.85 ? 417 TRP B CZ3 1 ATOM 7595 C CH2 . TRP B 1 417 ? 16.456 45.371 14.998 1.00 12.66 ? 417 TRP B CH2 1 ATOM 7596 N N . LEU B 1 418 ? 10.249 46.403 19.112 1.00 12.01 ? 418 LEU B N 1 ATOM 7597 C CA . LEU B 1 418 ? 8.842 46.344 19.476 1.00 11.82 ? 418 LEU B CA 1 ATOM 7598 C C . LEU B 1 418 ? 8.206 45.101 18.869 1.00 10.38 ? 418 LEU B C 1 ATOM 7599 O O . LEU B 1 418 ? 8.109 44.970 17.649 1.00 10.64 ? 418 LEU B O 1 ATOM 7600 C CB . LEU B 1 418 ? 8.104 47.614 19.024 1.00 10.22 ? 418 LEU B CB 1 ATOM 7601 C CG . LEU B 1 418 ? 6.604 47.705 19.341 1.00 12.30 ? 418 LEU B CG 1 ATOM 7602 C CD1 . LEU B 1 418 ? 6.357 47.814 20.833 1.00 9.94 ? 418 LEU B CD1 1 ATOM 7603 C CD2 . LEU B 1 418 ? 6.014 48.887 18.619 1.00 14.44 ? 418 LEU B CD2 1 ATOM 7604 N N . ILE B 1 419 ? 7.798 44.179 19.736 1.00 11.53 ? 419 ILE B N 1 ATOM 7605 C CA . ILE B 1 419 ? 7.162 42.943 19.295 1.00 10.84 ? 419 ILE B CA 1 ATOM 7606 C C . ILE B 1 419 ? 5.661 43.098 19.528 1.00 11.08 ? 419 ILE B C 1 ATOM 7607 O O . ILE B 1 419 ? 5.236 43.403 20.635 1.00 10.50 ? 419 ILE B O 1 ATOM 7608 C CB . ILE B 1 419 ? 7.713 41.692 20.046 1.00 10.90 ? 419 ILE B CB 1 ATOM 7609 C CG1 . ILE B 1 419 ? 9.240 41.654 19.988 1.00 10.67 ? 419 ILE B CG1 1 ATOM 7610 C CG2 . ILE B 1 419 ? 7.217 40.413 19.389 1.00 10.83 ? 419 ILE B CG2 1 ATOM 7611 C CD1 . ILE B 1 419 ? 9.907 42.233 21.199 1.00 11.61 ? 419 ILE B CD1 1 ATOM 7612 N N . GLU B 1 420 ? 4.877 42.922 18.467 1.00 12.13 ? 420 GLU B N 1 ATOM 7613 C CA . GLU B 1 420 ? 3.423 43.059 18.538 1.00 12.89 ? 420 GLU B CA 1 ATOM 7614 C C . GLU B 1 420 ? 2.765 41.698 18.403 1.00 13.95 ? 420 GLU B C 1 ATOM 7615 O O . GLU B 1 420 ? 3.058 40.957 17.465 1.00 14.74 ? 420 GLU B O 1 ATOM 7616 C CB . GLU B 1 420 ? 2.926 43.993 17.435 1.00 14.08 ? 420 GLU B CB 1 ATOM 7617 C CG . GLU B 1 420 ? 3.609 45.351 17.417 1.00 13.48 ? 420 GLU B CG 1 ATOM 7618 C CD . GLU B 1 420 ? 3.115 46.236 16.299 1.00 16.07 ? 420 GLU B CD 1 ATOM 7619 O OE1 . GLU B 1 420 ? 3.112 45.785 15.135 1.00 16.08 ? 420 GLU B OE1 1 ATOM 7620 O OE2 . GLU B 1 420 ? 2.740 47.392 16.586 1.00 18.75 ? 420 GLU B OE2 1 ATOM 7621 N N . ASN B 1 421 ? 1.846 41.398 19.319 1.00 14.19 ? 421 ASN B N 1 ATOM 7622 C CA . ASN B 1 421 ? 1.159 40.110 19.341 1.00 14.24 ? 421 ASN B CA 1 ATOM 7623 C C . ASN B 1 421 ? -0.179 40.041 18.616 1.00 14.80 ? 421 ASN B C 1 ATOM 7624 O O . ASN B 1 421 ? -1.235 40.082 19.259 1.00 13.51 ? 421 ASN B O 1 ATOM 7625 C CB . ASN B 1 421 ? 0.968 39.645 20.789 1.00 13.80 ? 421 ASN B CB 1 ATOM 7626 C CG . ASN B 1 421 ? 0.816 38.133 20.912 1.00 13.03 ? 421 ASN B CG 1 ATOM 7627 O OD1 . ASN B 1 421 ? 0.785 37.406 19.913 1.00 13.22 ? 421 ASN B OD1 1 ATOM 7628 N ND2 . ASN B 1 421 ? 0.740 37.655 22.144 1.00 11.93 ? 421 ASN B ND2 1 ATOM 7629 N N . ASP B 1 422 ? -0.126 39.918 17.285 1.00 16.18 ? 422 ASP B N 1 ATOM 7630 C CA . ASP B 1 422 ? -1.314 39.792 16.413 1.00 18.50 ? 422 ASP B CA 1 ATOM 7631 C C . ASP B 1 422 ? -2.523 40.636 16.895 1.00 19.75 ? 422 ASP B C 1 ATOM 7632 O O . ASP B 1 422 ? -3.590 40.083 17.177 1.00 21.67 ? 422 ASP B O 1 ATOM 7633 C CB . ASP B 1 422 ? -1.682 38.297 16.331 1.00 18.17 ? 422 ASP B CB 1 ATOM 7634 C CG . ASP B 1 422 ? -2.285 37.894 14.996 1.00 18.31 ? 422 ASP B CG 1 ATOM 7635 O OD1 . ASP B 1 422 ? -2.512 38.759 14.118 1.00 18.75 ? 422 ASP B OD1 1 ATOM 7636 O OD2 . ASP B 1 422 ? -2.514 36.679 14.824 1.00 17.79 ? 422 ASP B OD2 1 ATOM 7637 N N . PRO B 1 423 ? -2.360 41.981 17.003 1.00 22.02 ? 423 PRO B N 1 ATOM 7638 C CA . PRO B 1 423 ? -3.430 42.881 17.467 1.00 24.55 ? 423 PRO B CA 1 ATOM 7639 C C . PRO B 1 423 ? -4.717 42.865 16.650 1.00 26.31 ? 423 PRO B C 1 ATOM 7640 O O . PRO B 1 423 ? -5.810 42.966 17.211 1.00 27.35 ? 423 PRO B O 1 ATOM 7641 C CB . PRO B 1 423 ? -2.776 44.266 17.394 1.00 24.42 ? 423 PRO B CB 1 ATOM 7642 C CG . PRO B 1 423 ? -1.322 43.991 17.392 1.00 23.47 ? 423 PRO B CG 1 ATOM 7643 C CD . PRO B 1 423 ? -1.219 42.785 16.529 1.00 22.45 ? 423 PRO B CD 1 ATOM 7644 N N . GLU B 1 424 ? -4.568 42.721 15.333 1.00 26.88 ? 424 GLU B N 1 ATOM 7645 C CA . GLU B 1 424 ? -5.691 42.702 14.399 1.00 28.77 ? 424 GLU B CA 1 ATOM 7646 C C . GLU B 1 424 ? -6.173 41.288 14.078 1.00 27.36 ? 424 GLU B C 1 ATOM 7647 O O . GLU B 1 424 ? -7.100 41.107 13.282 1.00 26.63 ? 424 GLU B O 1 ATOM 7648 C CB . GLU B 1 424 ? -5.307 43.427 13.095 1.00 32.62 ? 424 GLU B CB 1 ATOM 7649 C CG . GLU B 1 424 ? -4.643 44.810 13.257 1.00 37.90 ? 424 GLU B CG 1 ATOM 7650 C CD . GLU B 1 424 ? -5.457 45.786 14.096 1.00 41.57 ? 424 GLU B CD 1 ATOM 7651 O OE1 . GLU B 1 424 ? -6.622 46.073 13.735 1.00 44.50 ? 424 GLU B OE1 1 ATOM 7652 O OE2 . GLU B 1 424 ? -4.923 46.262 15.123 1.00 42.80 ? 424 GLU B OE2 1 ATOM 7653 N N . GLY B 1 425 ? -5.547 40.297 14.714 1.00 25.38 ? 425 GLY B N 1 ATOM 7654 C CA . GLY B 1 425 ? -5.894 38.903 14.489 1.00 23.69 ? 425 GLY B CA 1 ATOM 7655 C C . GLY B 1 425 ? -7.138 38.388 15.202 1.00 23.38 ? 425 GLY B C 1 ATOM 7656 O O . GLY B 1 425 ? -7.634 39.058 16.110 1.00 21.53 ? 425 GLY B O 1 ATOM 7657 N N . PRO B 1 426 ? -7.672 37.209 14.800 1.00 23.84 ? 426 PRO B N 1 ATOM 7658 C CA . PRO B 1 426 ? -8.862 36.539 15.354 1.00 23.69 ? 426 PRO B CA 1 ATOM 7659 C C . PRO B 1 426 ? -8.743 36.285 16.856 1.00 24.22 ? 426 PRO B C 1 ATOM 7660 O O . PRO B 1 426 ? -9.654 36.599 17.629 1.00 22.72 ? 426 PRO B O 1 ATOM 7661 C CB . PRO B 1 426 ? -8.890 35.221 14.588 1.00 24.14 ? 426 PRO B CB 1 ATOM 7662 C CG . PRO B 1 426 ? -8.318 35.591 13.282 1.00 25.54 ? 426 PRO B CG 1 ATOM 7663 C CD . PRO B 1 426 ? -7.159 36.448 13.644 1.00 23.10 ? 426 PRO B CD 1 ATOM 7664 N N . PHE B 1 427 ? -7.617 35.690 17.243 1.00 23.84 ? 427 PHE B N 1 ATOM 7665 C CA . PHE B 1 427 ? -7.307 35.408 18.638 1.00 24.95 ? 427 PHE B CA 1 ATOM 7666 C C . PHE B 1 427 ? -5.803 35.504 18.849 1.00 22.90 ? 427 PHE B C 1 ATOM 7667 O O . PHE B 1 427 ? -5.020 35.279 17.922 1.00 21.79 ? 427 PHE B O 1 ATOM 7668 C CB . PHE B 1 427 ? -7.904 34.065 19.134 1.00 28.45 ? 427 PHE B CB 1 ATOM 7669 C CG . PHE B 1 427 ? -7.317 32.826 18.501 1.00 33.14 ? 427 PHE B CG 1 ATOM 7670 C CD1 . PHE B 1 427 ? -7.634 32.469 17.172 1.00 35.29 ? 427 PHE B CD1 1 ATOM 7671 C CD2 . PHE B 1 427 ? -6.487 31.971 19.258 1.00 35.36 ? 427 PHE B CD2 1 ATOM 7672 C CE1 . PHE B 1 427 ? -7.135 31.266 16.596 1.00 37.10 ? 427 PHE B CE1 1 ATOM 7673 C CE2 . PHE B 1 427 ? -5.977 30.765 18.705 1.00 38.29 ? 427 PHE B CE2 1 ATOM 7674 C CZ . PHE B 1 427 ? -6.303 30.410 17.368 1.00 38.76 ? 427 PHE B CZ 1 ATOM 7675 N N . SER B 1 428 ? -5.412 35.885 20.058 1.00 21.08 ? 428 SER B N 1 ATOM 7676 C CA . SER B 1 428 ? -4.005 36.033 20.384 1.00 19.31 ? 428 SER B CA 1 ATOM 7677 C C . SER B 1 428 ? -3.657 35.278 21.659 1.00 18.92 ? 428 SER B C 1 ATOM 7678 O O . SER B 1 428 ? -4.436 35.249 22.619 1.00 17.76 ? 428 SER B O 1 ATOM 7679 C CB . SER B 1 428 ? -3.667 37.514 20.497 1.00 19.13 ? 428 SER B CB 1 ATOM 7680 O OG . SER B 1 428 ? -2.277 37.727 20.646 1.00 18.94 ? 428 SER B OG 1 ATOM 7681 N N . LEU B 1 429 ? -2.496 34.627 21.622 1.00 17.22 ? 429 LEU B N 1 ATOM 7682 C CA . LEU B 1 429 ? -1.987 33.820 22.726 1.00 16.74 ? 429 LEU B CA 1 ATOM 7683 C C . LEU B 1 429 ? -0.710 34.419 23.304 1.00 15.22 ? 429 LEU B C 1 ATOM 7684 O O . LEU B 1 429 ? 0.016 35.116 22.593 1.00 13.37 ? 429 LEU B O 1 ATOM 7685 C CB . LEU B 1 429 ? -1.653 32.404 22.216 1.00 18.22 ? 429 LEU B CB 1 ATOM 7686 C CG . LEU B 1 429 ? -2.710 31.487 21.601 1.00 21.08 ? 429 LEU B CG 1 ATOM 7687 C CD1 . LEU B 1 429 ? -2.026 30.208 21.153 1.00 19.87 ? 429 LEU B CD1 1 ATOM 7688 C CD2 . LEU B 1 429 ? -3.820 31.182 22.600 1.00 21.94 ? 429 LEU B CD2 1 ATOM 7689 N N . PRO B 1 430 ? -0.435 34.194 24.613 1.00 14.21 ? 430 PRO B N 1 ATOM 7690 C CA . PRO B 1 430 ? 0.788 34.722 25.234 1.00 13.24 ? 430 PRO B CA 1 ATOM 7691 C C . PRO B 1 430 ? 1.988 33.935 24.683 1.00 12.36 ? 430 PRO B C 1 ATOM 7692 O O . PRO B 1 430 ? 1.852 32.746 24.375 1.00 12.15 ? 430 PRO B O 1 ATOM 7693 C CB . PRO B 1 430 ? 0.576 34.406 26.711 1.00 13.35 ? 430 PRO B CB 1 ATOM 7694 C CG . PRO B 1 430 ? -0.897 34.422 26.863 1.00 15.91 ? 430 PRO B CG 1 ATOM 7695 C CD . PRO B 1 430 ? -1.335 33.664 25.656 1.00 13.12 ? 430 PRO B CD 1 ATOM 7696 N N . HIS B 1 431 ? 3.119 34.614 24.481 1.00 11.77 ? 431 HIS B N 1 ATOM 7697 C CA . HIS B 1 431 ? 4.327 33.977 23.950 1.00 11.88 ? 431 HIS B CA 1 ATOM 7698 C C . HIS B 1 431 ? 5.585 34.256 24.771 1.00 11.55 ? 431 HIS B C 1 ATOM 7699 O O . HIS B 1 431 ? 5.906 35.415 25.031 1.00 12.45 ? 431 HIS B O 1 ATOM 7700 C CB . HIS B 1 431 ? 4.617 34.431 22.506 1.00 12.14 ? 431 HIS B CB 1 ATOM 7701 C CG . HIS B 1 431 ? 3.539 34.097 21.529 1.00 12.37 ? 431 HIS B CG 1 ATOM 7702 N ND1 . HIS B 1 431 ? 3.260 32.806 21.137 1.00 12.47 ? 431 HIS B ND1 1 ATOM 7703 C CD2 . HIS B 1 431 ? 2.646 34.888 20.891 1.00 13.66 ? 431 HIS B CD2 1 ATOM 7704 C CE1 . HIS B 1 431 ? 2.235 32.819 20.304 1.00 12.35 ? 431 HIS B CE1 1 ATOM 7705 N NE2 . HIS B 1 431 ? 1.843 34.069 20.138 1.00 13.81 ? 431 HIS B NE2 1 ATOM 7706 N N . PRO B 1 432 ? 6.293 33.197 25.223 1.00 11.81 ? 432 PRO B N 1 ATOM 7707 C CA . PRO B 1 432 ? 7.526 33.367 26.002 1.00 11.78 ? 432 PRO B CA 1 ATOM 7708 C C . PRO B 1 432 ? 8.686 33.640 25.027 1.00 11.68 ? 432 PRO B C 1 ATOM 7709 O O . PRO B 1 432 ? 9.274 32.716 24.466 1.00 13.19 ? 432 PRO B O 1 ATOM 7710 C CB . PRO B 1 432 ? 7.660 32.022 26.728 1.00 11.17 ? 432 PRO B CB 1 ATOM 7711 C CG . PRO B 1 432 ? 7.052 31.050 25.780 1.00 11.04 ? 432 PRO B CG 1 ATOM 7712 C CD . PRO B 1 432 ? 5.835 31.796 25.274 1.00 10.47 ? 432 PRO B CD 1 ATOM 7713 N N . MET B 1 433 ? 8.940 34.920 24.766 1.00 12.00 ? 433 MET B N 1 ATOM 7714 C CA . MET B 1 433 ? 10.000 35.333 23.841 1.00 11.22 ? 433 MET B CA 1 ATOM 7715 C C . MET B 1 433 ? 11.388 35.174 24.428 1.00 11.11 ? 433 MET B C 1 ATOM 7716 O O . MET B 1 433 ? 11.670 35.669 25.516 1.00 9.77 ? 433 MET B O 1 ATOM 7717 C CB . MET B 1 433 ? 9.782 36.770 23.359 1.00 11.60 ? 433 MET B CB 1 ATOM 7718 C CG . MET B 1 433 ? 8.466 36.994 22.618 1.00 12.84 ? 433 MET B CG 1 ATOM 7719 S SD . MET B 1 433 ? 8.128 35.794 21.298 1.00 14.22 ? 433 MET B SD 1 ATOM 7720 C CE . MET B 1 433 ? 9.272 36.345 20.030 1.00 12.72 ? 433 MET B CE 1 ATOM 7721 N N . HIS B 1 434 ? 12.247 34.481 23.684 1.00 10.43 ? 434 HIS B N 1 ATOM 7722 C CA . HIS B 1 434 ? 13.611 34.205 24.112 1.00 11.92 ? 434 HIS B CA 1 ATOM 7723 C C . HIS B 1 434 ? 14.663 34.656 23.101 1.00 11.28 ? 434 HIS B C 1 ATOM 7724 O O . HIS B 1 434 ? 14.521 34.419 21.906 1.00 9.40 ? 434 HIS B O 1 ATOM 7725 C CB . HIS B 1 434 ? 13.749 32.702 24.422 1.00 12.96 ? 434 HIS B CB 1 ATOM 7726 C CG . HIS B 1 434 ? 15.159 32.250 24.646 1.00 14.09 ? 434 HIS B CG 1 ATOM 7727 N ND1 . HIS B 1 434 ? 15.966 32.780 25.629 1.00 14.63 ? 434 HIS B ND1 1 ATOM 7728 C CD2 . HIS B 1 434 ? 15.921 31.355 23.976 1.00 11.98 ? 434 HIS B CD2 1 ATOM 7729 C CE1 . HIS B 1 434 ? 17.167 32.235 25.548 1.00 12.75 ? 434 HIS B CE1 1 ATOM 7730 N NE2 . HIS B 1 434 ? 17.164 31.365 24.555 1.00 13.88 ? 434 HIS B NE2 1 ATOM 7731 N N . LEU B 1 435 ? 15.740 35.254 23.609 1.00 11.89 ? 435 LEU B N 1 ATOM 7732 C CA . LEU B 1 435 ? 16.838 35.719 22.768 1.00 11.96 ? 435 LEU B CA 1 ATOM 7733 C C . LEU B 1 435 ? 18.132 34.977 23.048 1.00 11.14 ? 435 LEU B C 1 ATOM 7734 O O . LEU B 1 435 ? 18.549 34.830 24.199 1.00 9.65 ? 435 LEU B O 1 ATOM 7735 C CB . LEU B 1 435 ? 17.063 37.225 22.942 1.00 12.07 ? 435 LEU B CB 1 ATOM 7736 C CG . LEU B 1 435 ? 18.198 37.973 22.226 1.00 12.91 ? 435 LEU B CG 1 ATOM 7737 C CD1 . LEU B 1 435 ? 18.051 37.879 20.717 1.00 11.21 ? 435 LEU B CD1 1 ATOM 7738 C CD2 . LEU B 1 435 ? 18.201 39.417 22.661 1.00 12.99 ? 435 LEU B CD2 1 ATOM 7739 N N . HIS B 1 436 ? 18.768 34.539 21.967 1.00 10.03 ? 436 HIS B N 1 ATOM 7740 C CA . HIS B 1 436 ? 20.043 33.840 22.032 1.00 11.49 ? 436 HIS B CA 1 ATOM 7741 C C . HIS B 1 436 ? 21.146 34.890 22.073 1.00 11.37 ? 436 HIS B C 1 ATOM 7742 O O . HIS B 1 436 ? 20.980 35.999 21.544 1.00 11.72 ? 436 HIS B O 1 ATOM 7743 C CB . HIS B 1 436 ? 20.256 32.974 20.784 1.00 10.99 ? 436 HIS B CB 1 ATOM 7744 C CG . HIS B 1 436 ? 19.436 31.719 20.737 1.00 12.89 ? 436 HIS B CG 1 ATOM 7745 N ND1 . HIS B 1 436 ? 19.885 30.577 20.109 1.00 12.69 ? 436 HIS B ND1 1 ATOM 7746 C CD2 . HIS B 1 436 ? 18.185 31.437 21.177 1.00 10.89 ? 436 HIS B CD2 1 ATOM 7747 C CE1 . HIS B 1 436 ? 18.947 29.649 20.160 1.00 11.66 ? 436 HIS B CE1 1 ATOM 7748 N NE2 . HIS B 1 436 ? 17.906 30.144 20.803 1.00 15.64 ? 436 HIS B NE2 1 ATOM 7749 N N . GLY B 1 437 ? 22.240 34.547 22.749 1.00 11.96 ? 437 GLY B N 1 ATOM 7750 C CA . GLY B 1 437 ? 23.406 35.410 22.834 1.00 13.52 ? 437 GLY B CA 1 ATOM 7751 C C . GLY B 1 437 ? 23.436 36.656 23.684 1.00 15.29 ? 437 GLY B C 1 ATOM 7752 O O . GLY B 1 437 ? 24.492 37.294 23.795 1.00 14.28 ? 437 GLY B O 1 ATOM 7753 N N . HIS B 1 438 ? 22.280 37.053 24.209 1.00 14.40 ? 438 HIS B N 1 ATOM 7754 C CA . HIS B 1 438 ? 22.170 38.252 25.038 1.00 13.80 ? 438 HIS B CA 1 ATOM 7755 C C . HIS B 1 438 ? 21.094 38.103 26.082 1.00 13.66 ? 438 HIS B C 1 ATOM 7756 O O . HIS B 1 438 ? 20.260 37.192 26.041 1.00 14.41 ? 438 HIS B O 1 ATOM 7757 C CB . HIS B 1 438 ? 21.692 39.476 24.227 1.00 14.77 ? 438 HIS B CB 1 ATOM 7758 C CG . HIS B 1 438 ? 22.543 39.838 23.056 1.00 15.54 ? 438 HIS B CG 1 ATOM 7759 N ND1 . HIS B 1 438 ? 23.589 40.728 23.149 1.00 14.66 ? 438 HIS B ND1 1 ATOM 7760 C CD2 . HIS B 1 438 ? 22.482 39.456 21.760 1.00 14.76 ? 438 HIS B CD2 1 ATOM 7761 C CE1 . HIS B 1 438 ? 24.137 40.878 21.959 1.00 15.82 ? 438 HIS B CE1 1 ATOM 7762 N NE2 . HIS B 1 438 ? 23.484 40.118 21.099 1.00 15.77 ? 438 HIS B NE2 1 ATOM 7763 N N . ASP B 1 439 ? 21.134 39.048 27.013 1.00 13.67 ? 439 ASP B N 1 ATOM 7764 C CA . ASP B 1 439 ? 20.115 39.219 28.022 1.00 13.04 ? 439 ASP B CA 1 ATOM 7765 C C . ASP B 1 439 ? 19.555 40.552 27.538 1.00 14.88 ? 439 ASP B C 1 ATOM 7766 O O . ASP B 1 439 ? 20.325 41.465 27.202 1.00 16.04 ? 439 ASP B O 1 ATOM 7767 C CB . ASP B 1 439 ? 20.696 39.401 29.419 1.00 12.48 ? 439 ASP B CB 1 ATOM 7768 C CG . ASP B 1 439 ? 20.942 38.097 30.128 1.00 11.18 ? 439 ASP B CG 1 ATOM 7769 O OD1 . ASP B 1 439 ? 20.157 37.139 29.968 1.00 10.57 ? 439 ASP B OD1 1 ATOM 7770 O OD2 . ASP B 1 439 ? 21.955 38.020 30.845 1.00 12.37 ? 439 ASP B OD2 1 ATOM 7771 N N . PHE B 1 440 ? 18.240 40.637 27.385 1.00 12.94 ? 440 PHE B N 1 ATOM 7772 C CA . PHE B 1 440 ? 17.643 41.887 26.945 1.00 12.77 ? 440 PHE B CA 1 ATOM 7773 C C . PHE B 1 440 ? 17.063 42.660 28.114 1.00 13.60 ? 440 PHE B C 1 ATOM 7774 O O . PHE B 1 440 ? 16.889 42.112 29.199 1.00 12.64 ? 440 PHE B O 1 ATOM 7775 C CB . PHE B 1 440 ? 16.570 41.666 25.860 1.00 10.38 ? 440 PHE B CB 1 ATOM 7776 C CG . PHE B 1 440 ? 15.594 40.547 26.156 1.00 11.92 ? 440 PHE B CG 1 ATOM 7777 C CD1 . PHE B 1 440 ? 14.723 40.599 27.265 1.00 9.83 ? 440 PHE B CD1 1 ATOM 7778 C CD2 . PHE B 1 440 ? 15.533 39.438 25.305 1.00 9.20 ? 440 PHE B CD2 1 ATOM 7779 C CE1 . PHE B 1 440 ? 13.812 39.566 27.521 1.00 11.42 ? 440 PHE B CE1 1 ATOM 7780 C CE2 . PHE B 1 440 ? 14.616 38.386 25.544 1.00 10.30 ? 440 PHE B CE2 1 ATOM 7781 C CZ . PHE B 1 440 ? 13.755 38.454 26.656 1.00 11.59 ? 440 PHE B CZ 1 ATOM 7782 N N . LEU B 1 441 ? 16.745 43.923 27.872 1.00 13.40 ? 441 LEU B N 1 ATOM 7783 C CA . LEU B 1 441 ? 16.123 44.757 28.880 1.00 14.47 ? 441 LEU B CA 1 ATOM 7784 C C . LEU B 1 441 ? 14.638 44.780 28.557 1.00 14.50 ? 441 LEU B C 1 ATOM 7785 O O . LEU B 1 441 ? 14.265 44.974 27.397 1.00 14.34 ? 441 LEU B O 1 ATOM 7786 C CB . LEU B 1 441 ? 16.684 46.178 28.831 1.00 14.56 ? 441 LEU B CB 1 ATOM 7787 C CG . LEU B 1 441 ? 18.150 46.425 29.183 1.00 15.87 ? 441 LEU B CG 1 ATOM 7788 C CD1 . LEU B 1 441 ? 18.384 47.921 29.215 1.00 14.86 ? 441 LEU B CD1 1 ATOM 7789 C CD2 . LEU B 1 441 ? 18.498 45.833 30.529 1.00 15.30 ? 441 LEU B CD2 1 ATOM 7790 N N . VAL B 1 442 ? 13.800 44.502 29.556 1.00 14.35 ? 442 VAL B N 1 ATOM 7791 C CA . VAL B 1 442 ? 12.351 44.530 29.360 1.00 15.94 ? 442 VAL B CA 1 ATOM 7792 C C . VAL B 1 442 ? 11.911 45.948 29.723 1.00 16.39 ? 442 VAL B C 1 ATOM 7793 O O . VAL B 1 442 ? 11.656 46.262 30.891 1.00 16.62 ? 442 VAL B O 1 ATOM 7794 C CB . VAL B 1 442 ? 11.603 43.473 30.214 1.00 16.19 ? 442 VAL B CB 1 ATOM 7795 C CG1 . VAL B 1 442 ? 10.163 43.345 29.731 1.00 17.33 ? 442 VAL B CG1 1 ATOM 7796 C CG2 . VAL B 1 442 ? 12.296 42.120 30.119 1.00 16.69 ? 442 VAL B CG2 1 ATOM 7797 N N . LEU B 1 443 ? 11.858 46.797 28.699 1.00 15.82 ? 443 LEU B N 1 ATOM 7798 C CA . LEU B 1 443 ? 11.500 48.208 28.850 1.00 17.73 ? 443 LEU B CA 1 ATOM 7799 C C . LEU B 1 443 ? 10.054 48.459 29.195 1.00 18.16 ? 443 LEU B C 1 ATOM 7800 O O . LEU B 1 443 ? 9.738 49.421 29.888 1.00 18.57 ? 443 LEU B O 1 ATOM 7801 C CB . LEU B 1 443 ? 11.868 48.986 27.588 1.00 17.42 ? 443 LEU B CB 1 ATOM 7802 C CG . LEU B 1 443 ? 13.313 48.847 27.110 1.00 18.38 ? 443 LEU B CG 1 ATOM 7803 C CD1 . LEU B 1 443 ? 13.492 49.677 25.881 1.00 18.75 ? 443 LEU B CD1 1 ATOM 7804 C CD2 . LEU B 1 443 ? 14.286 49.274 28.180 1.00 18.17 ? 443 LEU B CD2 1 ATOM 7805 N N . GLY B 1 444 ? 9.185 47.578 28.716 1.00 17.62 ? 444 GLY B N 1 ATOM 7806 C CA . GLY B 1 444 ? 7.774 47.708 28.994 1.00 17.53 ? 444 GLY B CA 1 ATOM 7807 C C . GLY B 1 444 ? 6.941 46.812 28.121 1.00 17.12 ? 444 GLY B C 1 ATOM 7808 O O . GLY B 1 444 ? 7.425 46.215 27.150 1.00 16.61 ? 444 GLY B O 1 ATOM 7809 N N . ARG B 1 445 ? 5.677 46.705 28.497 1.00 15.06 ? 445 ARG B N 1 ATOM 7810 C CA . ARG B 1 445 ? 4.717 45.895 27.778 1.00 16.32 ? 445 ARG B CA 1 ATOM 7811 C C . ARG B 1 445 ? 3.355 46.551 27.884 1.00 15.77 ? 445 ARG B C 1 ATOM 7812 O O . ARG B 1 445 ? 3.193 47.536 28.602 1.00 15.62 ? 445 ARG B O 1 ATOM 7813 C CB . ARG B 1 445 ? 4.691 44.456 28.326 1.00 16.12 ? 445 ARG B CB 1 ATOM 7814 C CG . ARG B 1 445 ? 4.274 44.293 29.783 1.00 16.91 ? 445 ARG B CG 1 ATOM 7815 C CD . ARG B 1 445 ? 4.417 42.843 30.211 1.00 16.04 ? 445 ARG B CD 1 ATOM 7816 N NE . ARG B 1 445 ? 3.961 42.625 31.582 1.00 16.81 ? 445 ARG B NE 1 ATOM 7817 C CZ . ARG B 1 445 ? 4.423 41.675 32.388 1.00 17.25 ? 445 ARG B CZ 1 ATOM 7818 N NH1 . ARG B 1 445 ? 5.366 40.836 31.972 1.00 16.32 ? 445 ARG B NH1 1 ATOM 7819 N NH2 . ARG B 1 445 ? 3.974 41.590 33.634 1.00 17.19 ? 445 ARG B NH2 1 ATOM 7820 N N . SER B 1 446 ? 2.393 46.018 27.134 1.00 16.90 ? 446 SER B N 1 ATOM 7821 C CA . SER B 1 446 ? 1.007 46.484 27.140 1.00 15.97 ? 446 SER B CA 1 ATOM 7822 C C . SER B 1 446 ? 0.417 46.231 28.536 1.00 16.90 ? 446 SER B C 1 ATOM 7823 O O . SER B 1 446 ? 0.909 45.340 29.241 1.00 15.46 ? 446 SER B O 1 ATOM 7824 C CB . SER B 1 446 ? 0.226 45.738 26.053 1.00 16.61 ? 446 SER B CB 1 ATOM 7825 O OG . SER B 1 446 ? 0.528 44.358 26.025 1.00 15.15 ? 446 SER B OG 1 ATOM 7826 N N . PRO B 1 447 ? -0.602 47.024 28.975 1.00 16.78 ? 447 PRO B N 1 ATOM 7827 C CA . PRO B 1 447 ? -1.203 46.837 30.305 1.00 17.05 ? 447 PRO B CA 1 ATOM 7828 C C . PRO B 1 447 ? -1.560 45.401 30.683 1.00 16.67 ? 447 PRO B C 1 ATOM 7829 O O . PRO B 1 447 ? -2.071 44.644 29.854 1.00 17.48 ? 447 PRO B O 1 ATOM 7830 C CB . PRO B 1 447 ? -2.450 47.718 30.240 1.00 18.18 ? 447 PRO B CB 1 ATOM 7831 C CG . PRO B 1 447 ? -2.004 48.850 29.410 1.00 16.70 ? 447 PRO B CG 1 ATOM 7832 C CD . PRO B 1 447 ? -1.273 48.146 28.280 1.00 17.77 ? 447 PRO B CD 1 ATOM 7833 N N . ASP B 1 448 ? -1.204 45.031 31.914 1.00 16.03 ? 448 ASP B N 1 ATOM 7834 C CA . ASP B 1 448 ? -1.463 43.701 32.470 1.00 17.85 ? 448 ASP B CA 1 ATOM 7835 C C . ASP B 1 448 ? -2.969 43.489 32.648 1.00 19.53 ? 448 ASP B C 1 ATOM 7836 O O . ASP B 1 448 ? -3.590 44.051 33.553 1.00 20.05 ? 448 ASP B O 1 ATOM 7837 C CB . ASP B 1 448 ? -0.727 43.526 33.810 1.00 17.17 ? 448 ASP B CB 1 ATOM 7838 C CG . ASP B 1 448 ? 0.803 43.517 33.663 1.00 17.80 ? 448 ASP B CG 1 ATOM 7839 O OD1 . ASP B 1 448 ? 1.329 43.599 32.529 1.00 16.61 ? 448 ASP B OD1 1 ATOM 7840 O OD2 . ASP B 1 448 ? 1.486 43.409 34.701 1.00 19.34 ? 448 ASP B OD2 1 ATOM 7841 N N . VAL B 1 449 ? -3.544 42.739 31.710 1.00 18.58 ? 449 VAL B N 1 ATOM 7842 C CA . VAL B 1 449 ? -4.975 42.422 31.668 1.00 19.81 ? 449 VAL B CA 1 ATOM 7843 C C . VAL B 1 449 ? -5.133 40.888 31.697 1.00 19.38 ? 449 VAL B C 1 ATOM 7844 O O . VAL B 1 449 ? -4.115 40.184 31.636 1.00 20.49 ? 449 VAL B O 1 ATOM 7845 C CB . VAL B 1 449 ? -5.626 43.019 30.356 1.00 19.25 ? 449 VAL B CB 1 ATOM 7846 C CG1 . VAL B 1 449 ? -5.672 44.544 30.422 1.00 20.80 ? 449 VAL B CG1 1 ATOM 7847 C CG2 . VAL B 1 449 ? -4.895 42.544 29.100 1.00 20.29 ? 449 VAL B CG2 1 ATOM 7848 N N . PRO B 1 450 ? -6.373 40.349 31.892 1.00 19.23 ? 450 PRO B N 1 ATOM 7849 C CA . PRO B 1 450 ? -6.479 38.880 31.894 1.00 18.49 ? 450 PRO B CA 1 ATOM 7850 C C . PRO B 1 450 ? -6.072 38.265 30.552 1.00 17.59 ? 450 PRO B C 1 ATOM 7851 O O . PRO B 1 450 ? -6.482 38.742 29.497 1.00 16.57 ? 450 PRO B O 1 ATOM 7852 C CB . PRO B 1 450 ? -7.950 38.646 32.224 1.00 20.46 ? 450 PRO B CB 1 ATOM 7853 C CG . PRO B 1 450 ? -8.221 39.734 33.192 1.00 20.35 ? 450 PRO B CG 1 ATOM 7854 C CD . PRO B 1 450 ? -7.599 40.924 32.498 1.00 19.62 ? 450 PRO B CD 1 ATOM 7855 N N . ALA B 1 451 ? -5.202 37.257 30.613 1.00 17.87 ? 451 ALA B N 1 ATOM 7856 C CA . ALA B 1 451 ? -4.655 36.583 29.431 1.00 17.05 ? 451 ALA B CA 1 ATOM 7857 C C . ALA B 1 451 ? -5.641 36.072 28.388 1.00 15.90 ? 451 ALA B C 1 ATOM 7858 O O . ALA B 1 451 ? -5.352 36.116 27.192 1.00 15.27 ? 451 ALA B O 1 ATOM 7859 C CB . ALA B 1 451 ? -3.716 35.471 29.856 1.00 16.11 ? 451 ALA B CB 1 ATOM 7860 N N . ALA B 1 452 ? -6.805 35.611 28.842 1.00 16.12 ? 452 ALA B N 1 ATOM 7861 C CA . ALA B 1 452 ? -7.836 35.098 27.942 1.00 17.26 ? 452 ALA B CA 1 ATOM 7862 C C . ALA B 1 452 ? -8.923 36.124 27.605 1.00 17.52 ? 452 ALA B C 1 ATOM 7863 O O . ALA B 1 452 ? -9.881 35.798 26.896 1.00 18.39 ? 452 ALA B O 1 ATOM 7864 C CB . ALA B 1 452 ? -8.457 33.832 28.528 1.00 16.72 ? 452 ALA B CB 1 ATOM 7865 N N . SER B 1 453 ? -8.746 37.368 28.061 1.00 18.95 ? 453 SER B N 1 ATOM 7866 C CA . SER B 1 453 ? -9.722 38.441 27.818 1.00 21.57 ? 453 SER B CA 1 ATOM 7867 C C . SER B 1 453 ? -9.871 38.906 26.380 1.00 22.99 ? 453 SER B C 1 ATOM 7868 O O . SER B 1 453 ? -10.905 39.470 26.013 1.00 24.89 ? 453 SER B O 1 ATOM 7869 C CB . SER B 1 453 ? -9.465 39.656 28.718 1.00 20.05 ? 453 SER B CB 1 ATOM 7870 O OG . SER B 1 453 ? -8.289 40.356 28.345 1.00 21.13 ? 453 SER B OG 1 ATOM 7871 N N . GLN B 1 454 ? -8.841 38.632 25.580 1.00 24.57 ? 454 GLN B N 1 ATOM 7872 C CA . GLN B 1 454 ? -8.751 39.006 24.165 1.00 27.28 ? 454 GLN B CA 1 ATOM 7873 C C . GLN B 1 454 ? -8.761 40.519 23.919 1.00 27.20 ? 454 GLN B C 1 ATOM 7874 O O . GLN B 1 454 ? -9.167 40.992 22.855 1.00 28.62 ? 454 GLN B O 1 ATOM 7875 C CB . GLN B 1 454 ? -9.775 38.245 23.291 1.00 28.52 ? 454 GLN B CB 1 ATOM 7876 C CG . GLN B 1 454 ? -9.528 36.726 23.173 1.00 28.98 ? 454 GLN B CG 1 ATOM 7877 C CD . GLN B 1 454 ? -8.164 36.359 22.579 1.00 30.94 ? 454 GLN B CD 1 ATOM 7878 O OE1 . GLN B 1 454 ? -7.684 36.995 21.637 1.00 30.17 ? 454 GLN B OE1 1 ATOM 7879 N NE2 . GLN B 1 454 ? -7.536 35.329 23.138 1.00 30.17 ? 454 GLN B NE2 1 ATOM 7880 N N . GLN B 1 455 ? -8.293 41.262 24.927 1.00 27.82 ? 455 GLN B N 1 ATOM 7881 C CA . GLN B 1 455 ? -8.180 42.719 24.871 1.00 28.96 ? 455 GLN B CA 1 ATOM 7882 C C . GLN B 1 455 ? -6.933 43.054 24.063 1.00 28.82 ? 455 GLN B C 1 ATOM 7883 O O . GLN B 1 455 ? -5.847 42.532 24.337 1.00 29.19 ? 455 GLN B O 1 ATOM 7884 C CB . GLN B 1 455 ? -8.060 43.322 26.271 1.00 29.54 ? 455 GLN B CB 1 ATOM 7885 C CG . GLN B 1 455 ? -9.369 43.433 27.017 1.00 32.70 ? 455 GLN B CG 1 ATOM 7886 C CD . GLN B 1 455 ? -9.218 44.180 28.320 1.00 34.01 ? 455 GLN B CD 1 ATOM 7887 O OE1 . GLN B 1 455 ? -9.421 45.393 28.382 1.00 35.95 ? 455 GLN B OE1 1 ATOM 7888 N NE2 . GLN B 1 455 ? -8.861 43.461 29.374 1.00 33.69 ? 455 GLN B NE2 1 ATOM 7889 N N . ARG B 1 456 ? -7.119 43.888 23.045 1.00 28.14 ? 456 ARG B N 1 ATOM 7890 C CA . ARG B 1 456 ? -6.047 44.291 22.140 1.00 27.60 ? 456 ARG B CA 1 ATOM 7891 C C . ARG B 1 456 ? -5.434 45.639 22.488 1.00 26.01 ? 456 ARG B C 1 ATOM 7892 O O . ARG B 1 456 ? -6.130 46.558 22.924 1.00 24.68 ? 456 ARG B O 1 ATOM 7893 C CB . ARG B 1 456 ? -6.558 44.339 20.692 1.00 30.58 ? 456 ARG B CB 1 ATOM 7894 C CG . ARG B 1 456 ? -7.449 43.173 20.261 1.00 34.90 ? 456 ARG B CG 1 ATOM 7895 C CD . ARG B 1 456 ? -6.711 41.847 20.263 1.00 39.76 ? 456 ARG B CD 1 ATOM 7896 N NE . ARG B 1 456 ? -7.610 40.750 19.926 1.00 44.70 ? 456 ARG B NE 1 ATOM 7897 C CZ . ARG B 1 456 ? -7.265 39.670 19.232 1.00 46.70 ? 456 ARG B CZ 1 ATOM 7898 N NH1 . ARG B 1 456 ? -6.025 39.512 18.782 1.00 47.60 ? 456 ARG B NH1 1 ATOM 7899 N NH2 . ARG B 1 456 ? -8.179 38.749 18.968 1.00 48.60 ? 456 ARG B NH2 1 ATOM 7900 N N . PHE B 1 457 ? -4.116 45.728 22.324 1.00 24.40 ? 457 PHE B N 1 ATOM 7901 C CA . PHE B 1 457 ? -3.359 46.956 22.572 1.00 23.85 ? 457 PHE B CA 1 ATOM 7902 C C . PHE B 1 457 ? -2.311 47.132 21.479 1.00 22.48 ? 457 PHE B C 1 ATOM 7903 O O . PHE B 1 457 ? -1.579 46.195 21.149 1.00 20.87 ? 457 PHE B O 1 ATOM 7904 C CB . PHE B 1 457 ? -2.631 46.924 23.925 1.00 24.51 ? 457 PHE B CB 1 ATOM 7905 C CG . PHE B 1 457 ? -3.536 46.959 25.125 1.00 26.91 ? 457 PHE B CG 1 ATOM 7906 C CD1 . PHE B 1 457 ? -4.137 48.166 25.541 1.00 27.12 ? 457 PHE B CD1 1 ATOM 7907 C CD2 . PHE B 1 457 ? -3.788 45.785 25.857 1.00 25.58 ? 457 PHE B CD2 1 ATOM 7908 C CE1 . PHE B 1 457 ? -4.988 48.204 26.681 1.00 27.73 ? 457 PHE B CE1 1 ATOM 7909 C CE2 . PHE B 1 457 ? -4.633 45.800 26.997 1.00 26.64 ? 457 PHE B CE2 1 ATOM 7910 C CZ . PHE B 1 457 ? -5.237 47.016 27.412 1.00 26.51 ? 457 PHE B CZ 1 ATOM 7911 N N . VAL B 1 458 ? -2.295 48.320 20.882 1.00 21.00 ? 458 VAL B N 1 ATOM 7912 C CA . VAL B 1 458 ? -1.323 48.682 19.851 1.00 22.21 ? 458 VAL B CA 1 ATOM 7913 C C . VAL B 1 458 ? -0.545 49.831 20.498 1.00 21.80 ? 458 VAL B C 1 ATOM 7914 O O . VAL B 1 458 ? -1.144 50.678 21.169 1.00 20.67 ? 458 VAL B O 1 ATOM 7915 C CB . VAL B 1 458 ? -2.001 49.175 18.528 1.00 22.63 ? 458 VAL B CB 1 ATOM 7916 C CG1 . VAL B 1 458 ? -0.950 49.456 17.448 1.00 23.58 ? 458 VAL B CG1 1 ATOM 7917 C CG2 . VAL B 1 458 ? -2.994 48.145 18.010 1.00 24.95 ? 458 VAL B CG2 1 ATOM 7918 N N . PHE B 1 459 ? 0.778 49.837 20.313 1.00 20.95 ? 459 PHE B N 1 ATOM 7919 C CA . PHE B 1 459 ? 1.666 50.863 20.873 1.00 22.07 ? 459 PHE B CA 1 ATOM 7920 C C . PHE B 1 459 ? 1.222 52.279 20.486 1.00 22.69 ? 459 PHE B C 1 ATOM 7921 O O . PHE B 1 459 ? 1.153 52.628 19.303 1.00 23.19 ? 459 PHE B O 1 ATOM 7922 C CB . PHE B 1 459 ? 3.121 50.609 20.435 1.00 21.28 ? 459 PHE B CB 1 ATOM 7923 C CG . PHE B 1 459 ? 4.145 51.432 21.180 1.00 21.66 ? 459 PHE B CG 1 ATOM 7924 C CD1 . PHE B 1 459 ? 4.587 51.033 22.451 1.00 20.96 ? 459 PHE B CD1 1 ATOM 7925 C CD2 . PHE B 1 459 ? 4.659 52.625 20.626 1.00 22.25 ? 459 PHE B CD2 1 ATOM 7926 C CE1 . PHE B 1 459 ? 5.529 51.805 23.180 1.00 20.56 ? 459 PHE B CE1 1 ATOM 7927 C CE2 . PHE B 1 459 ? 5.600 53.414 21.338 1.00 21.83 ? 459 PHE B CE2 1 ATOM 7928 C CZ . PHE B 1 459 ? 6.035 52.999 22.624 1.00 23.24 ? 459 PHE B CZ 1 ATOM 7929 N N . ASP B 1 460 ? 0.873 53.050 21.511 1.00 23.98 ? 460 ASP B N 1 ATOM 7930 C CA . ASP B 1 460 ? 0.419 54.430 21.363 1.00 26.13 ? 460 ASP B CA 1 ATOM 7931 C C . ASP B 1 460 ? 1.375 55.305 22.187 1.00 26.06 ? 460 ASP B C 1 ATOM 7932 O O . ASP B 1 460 ? 1.298 55.313 23.416 1.00 25.56 ? 460 ASP B O 1 ATOM 7933 C CB . ASP B 1 460 ? -1.039 54.542 21.861 1.00 28.59 ? 460 ASP B CB 1 ATOM 7934 C CG . ASP B 1 460 ? -1.622 55.961 21.754 1.00 31.31 ? 460 ASP B CG 1 ATOM 7935 O OD1 . ASP B 1 460 ? -1.108 56.803 20.981 1.00 33.80 ? 460 ASP B OD1 1 ATOM 7936 O OD2 . ASP B 1 460 ? -2.620 56.224 22.458 1.00 32.93 ? 460 ASP B OD2 1 ATOM 7937 N N . PRO B 1 461 ? 2.264 56.078 21.518 1.00 27.46 ? 461 PRO B N 1 ATOM 7938 C CA . PRO B 1 461 ? 3.238 56.963 22.180 1.00 29.45 ? 461 PRO B CA 1 ATOM 7939 C C . PRO B 1 461 ? 2.666 57.958 23.197 1.00 31.12 ? 461 PRO B C 1 ATOM 7940 O O . PRO B 1 461 ? 3.354 58.339 24.147 1.00 31.05 ? 461 PRO B O 1 ATOM 7941 C CB . PRO B 1 461 ? 3.879 57.701 21.004 1.00 29.69 ? 461 PRO B CB 1 ATOM 7942 C CG . PRO B 1 461 ? 3.822 56.698 19.912 1.00 30.26 ? 461 PRO B CG 1 ATOM 7943 C CD . PRO B 1 461 ? 2.421 56.165 20.052 1.00 28.89 ? 461 PRO B CD 1 ATOM 7944 N N . ALA B 1 462 ? 1.395 58.323 23.013 1.00 32.31 ? 462 ALA B N 1 ATOM 7945 C CA . ALA B 1 462 ? 0.684 59.274 23.875 1.00 33.59 ? 462 ALA B CA 1 ATOM 7946 C C . ALA B 1 462 ? 0.442 58.784 25.305 1.00 34.21 ? 462 ALA B C 1 ATOM 7947 O O . ALA B 1 462 ? 0.372 59.594 26.234 1.00 34.34 ? 462 ALA B O 1 ATOM 7948 C CB . ALA B 1 462 ? -0.642 59.677 23.225 1.00 34.16 ? 462 ALA B CB 1 ATOM 7949 N N . VAL B 1 463 ? 0.303 57.466 25.469 1.00 34.14 ? 463 VAL B N 1 ATOM 7950 C CA . VAL B 1 463 ? 0.072 56.857 26.782 1.00 33.98 ? 463 VAL B CA 1 ATOM 7951 C C . VAL B 1 463 ? 1.136 55.834 27.189 1.00 33.36 ? 463 VAL B C 1 ATOM 7952 O O . VAL B 1 463 ? 1.425 55.675 28.377 1.00 33.68 ? 463 VAL B O 1 ATOM 7953 C CB . VAL B 1 463 ? -1.342 56.178 26.888 1.00 36.18 ? 463 VAL B CB 1 ATOM 7954 C CG1 . VAL B 1 463 ? -2.446 57.233 26.968 1.00 36.67 ? 463 VAL B CG1 1 ATOM 7955 C CG2 . VAL B 1 463 ? -1.600 55.235 25.708 1.00 36.10 ? 463 VAL B CG2 1 ATOM 7956 N N . ASP B 1 464 ? 1.750 55.189 26.197 1.00 31.50 ? 464 ASP B N 1 ATOM 7957 C CA . ASP B 1 464 ? 2.749 54.146 26.431 1.00 30.45 ? 464 ASP B CA 1 ATOM 7958 C C . ASP B 1 464 ? 4.198 54.538 26.677 1.00 31.23 ? 464 ASP B C 1 ATOM 7959 O O . ASP B 1 464 ? 4.943 53.764 27.278 1.00 30.95 ? 464 ASP B O 1 ATOM 7960 C CB . ASP B 1 464 ? 2.678 53.105 25.319 1.00 27.35 ? 464 ASP B CB 1 ATOM 7961 C CG . ASP B 1 464 ? 1.351 52.364 25.299 1.00 26.66 ? 464 ASP B CG 1 ATOM 7962 O OD1 . ASP B 1 464 ? 0.876 51.956 26.381 1.00 23.67 ? 464 ASP B OD1 1 ATOM 7963 O OD2 . ASP B 1 464 ? 0.800 52.162 24.199 1.00 25.75 ? 464 ASP B OD2 1 ATOM 7964 N N . LEU B 1 465 ? 4.593 55.731 26.229 1.00 31.88 ? 465 LEU B N 1 ATOM 7965 C CA . LEU B 1 465 ? 5.963 56.229 26.405 1.00 33.67 ? 465 LEU B CA 1 ATOM 7966 C C . LEU B 1 465 ? 6.327 56.458 27.876 1.00 33.48 ? 465 LEU B C 1 ATOM 7967 O O . LEU B 1 465 ? 7.444 56.146 28.301 1.00 33.93 ? 465 LEU B O 1 ATOM 7968 C CB . LEU B 1 465 ? 6.162 57.520 25.600 1.00 35.33 ? 465 LEU B CB 1 ATOM 7969 C CG . LEU B 1 465 ? 7.150 57.588 24.425 1.00 37.41 ? 465 LEU B CG 1 ATOM 7970 C CD1 . LEU B 1 465 ? 8.533 57.474 24.956 1.00 39.69 ? 465 LEU B CD1 1 ATOM 7971 C CD2 . LEU B 1 465 ? 6.920 56.518 23.387 1.00 37.31 ? 465 LEU B CD2 1 ATOM 7972 N N . ALA B 1 466 ? 5.348 56.940 28.645 1.00 32.89 ? 466 ALA B N 1 ATOM 7973 C CA . ALA B 1 466 ? 5.493 57.220 30.076 1.00 31.94 ? 466 ALA B CA 1 ATOM 7974 C C . ALA B 1 466 ? 5.422 55.946 30.928 1.00 30.93 ? 466 ALA B C 1 ATOM 7975 O O . ALA B 1 466 ? 5.766 55.956 32.115 1.00 31.38 ? 466 ALA B O 1 ATOM 7976 C CB . ALA B 1 466 ? 4.416 58.206 30.519 1.00 32.79 ? 466 ALA B CB 1 ATOM 7977 N N . ARG B 1 467 ? 4.978 54.858 30.305 1.00 28.98 ? 467 ARG B N 1 ATOM 7978 C CA . ARG B 1 467 ? 4.850 53.562 30.965 1.00 28.64 ? 467 ARG B CA 1 ATOM 7979 C C . ARG B 1 467 ? 6.120 52.716 30.864 1.00 28.78 ? 467 ARG B C 1 ATOM 7980 O O . ARG B 1 467 ? 6.239 51.680 31.528 1.00 29.30 ? 467 ARG B O 1 ATOM 7981 C CB . ARG B 1 467 ? 3.680 52.787 30.370 1.00 27.66 ? 467 ARG B CB 1 ATOM 7982 C CG . ARG B 1 467 ? 2.298 53.328 30.715 1.00 27.01 ? 467 ARG B CG 1 ATOM 7983 C CD . ARG B 1 467 ? 1.199 52.412 30.180 1.00 27.06 ? 467 ARG B CD 1 ATOM 7984 N NE . ARG B 1 467 ? 1.273 51.074 30.772 1.00 25.55 ? 467 ARG B NE 1 ATOM 7985 C CZ . ARG B 1 467 ? 1.603 49.964 30.115 1.00 24.93 ? 467 ARG B CZ 1 ATOM 7986 N NH1 . ARG B 1 467 ? 1.891 50.007 28.817 1.00 22.23 ? 467 ARG B NH1 1 ATOM 7987 N NH2 . ARG B 1 467 ? 1.699 48.818 30.772 1.00 23.33 ? 467 ARG B NH2 1 ATOM 7988 N N . LEU B 1 468 ? 7.058 53.157 30.026 1.00 27.33 ? 468 LEU B N 1 ATOM 7989 C CA . LEU B 1 468 ? 8.325 52.455 29.832 1.00 26.32 ? 468 LEU B CA 1 ATOM 7990 C C . LEU B 1 468 ? 9.330 52.760 30.934 1.00 26.08 ? 468 LEU B C 1 ATOM 7991 O O . LEU B 1 468 ? 9.318 53.853 31.508 1.00 27.19 ? 468 LEU B O 1 ATOM 7992 C CB . LEU B 1 468 ? 8.935 52.808 28.479 1.00 25.62 ? 468 LEU B CB 1 ATOM 7993 C CG . LEU B 1 468 ? 8.087 52.595 27.230 1.00 25.41 ? 468 LEU B CG 1 ATOM 7994 C CD1 . LEU B 1 468 ? 8.766 53.250 26.047 1.00 24.68 ? 468 LEU B CD1 1 ATOM 7995 C CD2 . LEU B 1 468 ? 7.819 51.114 26.994 1.00 22.80 ? 468 LEU B CD2 1 ATOM 7996 N N . ASN B 1 469 ? 10.178 51.778 31.231 1.00 24.79 ? 469 ASN B N 1 ATOM 7997 C CA . ASN B 1 469 ? 11.206 51.905 32.258 1.00 24.18 ? 469 ASN B CA 1 ATOM 7998 C C . ASN B 1 469 ? 12.588 51.651 31.664 1.00 23.20 ? 469 ASN B C 1 ATOM 7999 O O . ASN B 1 469 ? 12.870 50.562 31.157 1.00 20.83 ? 469 ASN B O 1 ATOM 8000 C CB . ASN B 1 469 ? 10.932 50.937 33.428 1.00 25.17 ? 469 ASN B CB 1 ATOM 8001 C CG . ASN B 1 469 ? 11.963 51.054 34.561 1.00 26.34 ? 469 ASN B CG 1 ATOM 8002 O OD1 . ASN B 1 469 ? 12.574 52.107 34.766 1.00 26.45 ? 469 ASN B OD1 1 ATOM 8003 N ND2 . ASN B 1 469 ? 12.160 49.961 35.291 1.00 28.35 ? 469 ASN B ND2 1 ATOM 8004 N N . GLY B 1 470 ? 13.438 52.671 31.757 1.00 22.22 ? 470 GLY B N 1 ATOM 8005 C CA . GLY B 1 470 ? 14.799 52.589 31.262 1.00 20.85 ? 470 GLY B CA 1 ATOM 8006 C C . GLY B 1 470 ? 15.828 52.657 32.374 1.00 21.23 ? 470 GLY B C 1 ATOM 8007 O O . GLY B 1 470 ? 17.029 52.587 32.109 1.00 21.77 ? 470 GLY B O 1 ATOM 8008 N N . ASP B 1 471 ? 15.353 52.794 33.613 1.00 21.23 ? 471 ASP B N 1 ATOM 8009 C CA . ASP B 1 471 ? 16.206 52.877 34.799 1.00 22.07 ? 471 ASP B CA 1 ATOM 8010 C C . ASP B 1 471 ? 16.259 51.496 35.459 1.00 21.42 ? 471 ASP B C 1 ATOM 8011 O O . ASP B 1 471 ? 15.405 51.141 36.282 1.00 21.12 ? 471 ASP B O 1 ATOM 8012 C CB . ASP B 1 471 ? 15.665 53.949 35.768 1.00 24.92 ? 471 ASP B CB 1 ATOM 8013 C CG . ASP B 1 471 ? 16.603 54.226 36.949 1.00 28.61 ? 471 ASP B CG 1 ATOM 8014 O OD1 . ASP B 1 471 ? 17.817 53.932 36.862 1.00 31.25 ? 471 ASP B OD1 1 ATOM 8015 O OD2 . ASP B 1 471 ? 16.115 54.752 37.973 1.00 31.80 ? 471 ASP B OD2 1 ATOM 8016 N N . ASN B 1 472 ? 17.285 50.735 35.071 1.00 18.65 ? 472 ASN B N 1 ATOM 8017 C CA . ASN B 1 472 ? 17.546 49.362 35.526 1.00 17.92 ? 472 ASN B CA 1 ATOM 8018 C C . ASN B 1 472 ? 16.324 48.420 35.431 1.00 16.49 ? 472 ASN B C 1 ATOM 8019 O O . ASN B 1 472 ? 15.906 47.824 36.429 1.00 16.18 ? 472 ASN B O 1 ATOM 8020 C CB . ASN B 1 472 ? 18.192 49.342 36.928 1.00 15.81 ? 472 ASN B CB 1 ATOM 8021 C CG . ASN B 1 472 ? 18.814 47.991 37.266 1.00 15.36 ? 472 ASN B CG 1 ATOM 8022 O OD1 . ASN B 1 472 ? 19.353 47.313 36.389 1.00 14.60 ? 472 ASN B OD1 1 ATOM 8023 N ND2 . ASN B 1 472 ? 18.726 47.588 38.528 1.00 12.46 ? 472 ASN B ND2 1 ATOM 8024 N N . PRO B 1 473 ? 15.746 48.266 34.215 1.00 15.55 ? 473 PRO B N 1 ATOM 8025 C CA . PRO B 1 473 ? 14.582 47.393 34.040 1.00 15.06 ? 473 PRO B CA 1 ATOM 8026 C C . PRO B 1 473 ? 14.990 45.906 34.127 1.00 15.02 ? 473 PRO B C 1 ATOM 8027 O O . PRO B 1 473 ? 16.191 45.611 34.228 1.00 13.43 ? 473 PRO B O 1 ATOM 8028 C CB . PRO B 1 473 ? 14.102 47.788 32.640 1.00 15.22 ? 473 PRO B CB 1 ATOM 8029 C CG . PRO B 1 473 ? 15.340 48.030 31.928 1.00 14.11 ? 473 PRO B CG 1 ATOM 8030 C CD . PRO B 1 473 ? 16.165 48.817 32.907 1.00 15.69 ? 473 PRO B CD 1 ATOM 8031 N N . PRO B 1 474 ? 14.014 44.964 34.167 1.00 14.56 ? 474 PRO B N 1 ATOM 8032 C CA . PRO B 1 474 ? 14.384 43.542 34.236 1.00 14.99 ? 474 PRO B CA 1 ATOM 8033 C C . PRO B 1 474 ? 15.271 43.126 33.073 1.00 14.85 ? 474 PRO B C 1 ATOM 8034 O O . PRO B 1 474 ? 15.006 43.479 31.920 1.00 16.42 ? 474 PRO B O 1 ATOM 8035 C CB . PRO B 1 474 ? 13.039 42.845 34.148 1.00 14.61 ? 474 PRO B CB 1 ATOM 8036 C CG . PRO B 1 474 ? 12.189 43.755 34.900 1.00 16.50 ? 474 PRO B CG 1 ATOM 8037 C CD . PRO B 1 474 ? 12.561 45.106 34.387 1.00 15.20 ? 474 PRO B CD 1 ATOM 8038 N N . ARG B 1 475 ? 16.385 42.492 33.413 1.00 14.65 ? 475 ARG B N 1 ATOM 8039 C CA . ARG B 1 475 ? 17.337 42.017 32.425 1.00 15.11 ? 475 ARG B CA 1 ATOM 8040 C C . ARG B 1 475 ? 17.354 40.506 32.537 1.00 13.70 ? 475 ARG B C 1 ATOM 8041 O O . ARG B 1 475 ? 17.625 39.965 33.604 1.00 14.82 ? 475 ARG B O 1 ATOM 8042 C CB . ARG B 1 475 ? 18.727 42.604 32.683 1.00 14.45 ? 475 ARG B CB 1 ATOM 8043 C CG . ARG B 1 475 ? 19.725 42.362 31.563 1.00 13.94 ? 475 ARG B CG 1 ATOM 8044 C CD . ARG B 1 475 ? 21.042 43.080 31.786 1.00 14.26 ? 475 ARG B CD 1 ATOM 8045 N NE . ARG B 1 475 ? 21.781 42.577 32.943 1.00 13.50 ? 475 ARG B NE 1 ATOM 8046 C CZ . ARG B 1 475 ? 22.035 43.285 34.042 1.00 15.16 ? 475 ARG B CZ 1 ATOM 8047 N NH1 . ARG B 1 475 ? 21.603 44.539 34.155 1.00 12.89 ? 475 ARG B NH1 1 ATOM 8048 N NH2 . ARG B 1 475 ? 22.712 42.734 35.040 1.00 14.49 ? 475 ARG B NH2 1 ATOM 8049 N N . ARG B 1 476 ? 16.984 39.839 31.445 1.00 12.50 ? 476 ARG B N 1 ATOM 8050 C CA . ARG B 1 476 ? 16.921 38.376 31.392 1.00 11.16 ? 476 ARG B CA 1 ATOM 8051 C C . ARG B 1 476 ? 16.905 37.895 29.943 1.00 10.03 ? 476 ARG B C 1 ATOM 8052 O O . ARG B 1 476 ? 16.965 38.714 29.029 1.00 10.24 ? 476 ARG B O 1 ATOM 8053 C CB . ARG B 1 476 ? 15.690 37.871 32.162 1.00 9.75 ? 476 ARG B CB 1 ATOM 8054 C CG . ARG B 1 476 ? 14.331 38.381 31.687 1.00 9.14 ? 476 ARG B CG 1 ATOM 8055 C CD . ARG B 1 476 ? 13.266 38.098 32.735 1.00 7.32 ? 476 ARG B CD 1 ATOM 8056 N NE . ARG B 1 476 ? 13.329 36.720 33.230 1.00 7.46 ? 476 ARG B NE 1 ATOM 8057 C CZ . ARG B 1 476 ? 12.665 36.268 34.290 1.00 7.09 ? 476 ARG B CZ 1 ATOM 8058 N NH1 . ARG B 1 476 ? 11.864 37.077 34.977 1.00 7.58 ? 476 ARG B NH1 1 ATOM 8059 N NH2 . ARG B 1 476 ? 12.821 35.010 34.681 1.00 4.70 ? 476 ARG B NH2 1 ATOM 8060 N N . ASP B 1 477 ? 16.835 36.580 29.735 1.00 11.11 ? 477 ASP B N 1 ATOM 8061 C CA . ASP B 1 477 ? 16.836 36.031 28.381 1.00 9.69 ? 477 ASP B CA 1 ATOM 8062 C C . ASP B 1 477 ? 15.468 35.616 27.844 1.00 8.90 ? 477 ASP B C 1 ATOM 8063 O O . ASP B 1 477 ? 15.328 35.380 26.647 1.00 9.09 ? 477 ASP B O 1 ATOM 8064 C CB . ASP B 1 477 ? 17.863 34.882 28.247 1.00 10.18 ? 477 ASP B CB 1 ATOM 8065 C CG . ASP B 1 477 ? 17.513 33.653 29.080 1.00 11.98 ? 477 ASP B CG 1 ATOM 8066 O OD1 . ASP B 1 477 ? 16.429 33.059 28.873 1.00 10.30 ? 477 ASP B OD1 1 ATOM 8067 O OD2 . ASP B 1 477 ? 18.343 33.258 29.921 1.00 14.77 ? 477 ASP B OD2 1 ATOM 8068 N N . THR B 1 478 ? 14.482 35.508 28.735 1.00 8.54 ? 478 THR B N 1 ATOM 8069 C CA . THR B 1 478 ? 13.119 35.119 28.370 1.00 9.15 ? 478 THR B CA 1 ATOM 8070 C C . THR B 1 478 ? 12.100 35.968 29.125 1.00 10.78 ? 478 THR B C 1 ATOM 8071 O O . THR B 1 478 ? 12.230 36.161 30.331 1.00 11.59 ? 478 THR B O 1 ATOM 8072 C CB . THR B 1 478 ? 12.830 33.624 28.692 1.00 9.91 ? 478 THR B CB 1 ATOM 8073 O OG1 . THR B 1 478 ? 13.837 32.787 28.111 1.00 10.20 ? 478 THR B OG1 1 ATOM 8074 C CG2 . THR B 1 478 ? 11.446 33.197 28.156 1.00 8.61 ? 478 THR B CG2 1 ATOM 8075 N N . THR B 1 479 ? 11.091 36.457 28.404 1.00 10.40 ? 479 THR B N 1 ATOM 8076 C CA . THR B 1 479 ? 10.008 37.252 28.989 1.00 9.78 ? 479 THR B CA 1 ATOM 8077 C C . THR B 1 479 ? 8.729 37.065 28.175 1.00 8.74 ? 479 THR B C 1 ATOM 8078 O O . THR B 1 479 ? 8.775 36.640 27.021 1.00 8.80 ? 479 THR B O 1 ATOM 8079 C CB . THR B 1 479 ? 10.372 38.770 29.143 1.00 10.79 ? 479 THR B CB 1 ATOM 8080 O OG1 . THR B 1 479 ? 9.462 39.390 30.059 1.00 11.63 ? 479 THR B OG1 1 ATOM 8081 C CG2 . THR B 1 479 ? 10.299 39.509 27.826 1.00 9.91 ? 479 THR B CG2 1 ATOM 8082 N N . MET B 1 480 ? 7.603 37.441 28.767 1.00 8.91 ? 480 MET B N 1 ATOM 8083 C CA . MET B 1 480 ? 6.307 37.287 28.120 1.00 8.70 ? 480 MET B CA 1 ATOM 8084 C C . MET B 1 480 ? 5.808 38.390 27.208 1.00 9.55 ? 480 MET B C 1 ATOM 8085 O O . MET B 1 480 ? 5.841 39.581 27.547 1.00 7.75 ? 480 MET B O 1 ATOM 8086 C CB . MET B 1 480 ? 5.218 36.999 29.159 1.00 9.32 ? 480 MET B CB 1 ATOM 8087 C CG . MET B 1 480 ? 5.402 35.703 29.938 1.00 6.53 ? 480 MET B CG 1 ATOM 8088 S SD . MET B 1 480 ? 5.529 34.220 28.923 1.00 10.42 ? 480 MET B SD 1 ATOM 8089 C CE . MET B 1 480 ? 3.891 34.108 28.219 1.00 7.88 ? 480 MET B CE 1 ATOM 8090 N N . LEU B 1 481 ? 5.355 37.959 26.032 1.00 9.53 ? 481 LEU B N 1 ATOM 8091 C CA . LEU B 1 481 ? 4.734 38.826 25.046 1.00 9.81 ? 481 LEU B CA 1 ATOM 8092 C C . LEU B 1 481 ? 3.256 38.631 25.426 1.00 10.84 ? 481 LEU B C 1 ATOM 8093 O O . LEU B 1 481 ? 2.732 37.518 25.315 1.00 11.85 ? 481 LEU B O 1 ATOM 8094 C CB . LEU B 1 481 ? 5.015 38.314 23.626 1.00 9.72 ? 481 LEU B CB 1 ATOM 8095 C CG . LEU B 1 481 ? 4.303 38.955 22.432 1.00 11.39 ? 481 LEU B CG 1 ATOM 8096 C CD1 . LEU B 1 481 ? 4.608 40.433 22.315 1.00 9.86 ? 481 LEU B CD1 1 ATOM 8097 C CD2 . LEU B 1 481 ? 4.659 38.226 21.151 1.00 8.95 ? 481 LEU B CD2 1 ATOM 8098 N N . PRO B 1 482 ? 2.591 39.686 25.951 1.00 11.57 ? 482 PRO B N 1 ATOM 8099 C CA . PRO B 1 482 ? 1.182 39.588 26.354 1.00 13.32 ? 482 PRO B CA 1 ATOM 8100 C C . PRO B 1 482 ? 0.246 39.302 25.195 1.00 14.67 ? 482 PRO B C 1 ATOM 8101 O O . PRO B 1 482 ? 0.480 39.770 24.076 1.00 13.59 ? 482 PRO B O 1 ATOM 8102 C CB . PRO B 1 482 ? 0.885 40.978 26.927 1.00 13.73 ? 482 PRO B CB 1 ATOM 8103 C CG . PRO B 1 482 ? 2.212 41.514 27.289 1.00 11.46 ? 482 PRO B CG 1 ATOM 8104 C CD . PRO B 1 482 ? 3.078 41.060 26.164 1.00 11.78 ? 482 PRO B CD 1 ATOM 8105 N N . ALA B 1 483 ? -0.807 38.534 25.477 1.00 15.07 ? 483 ALA B N 1 ATOM 8106 C CA . ALA B 1 483 ? -1.822 38.196 24.484 1.00 16.73 ? 483 ALA B CA 1 ATOM 8107 C C . ALA B 1 483 ? -2.516 39.471 24.010 1.00 16.08 ? 483 ALA B C 1 ATOM 8108 O O . ALA B 1 483 ? -2.899 40.313 24.829 1.00 17.28 ? 483 ALA B O 1 ATOM 8109 C CB . ALA B 1 483 ? -2.845 37.243 25.080 1.00 16.02 ? 483 ALA B CB 1 ATOM 8110 N N . GLY B 1 484 ? -2.561 39.643 22.690 1.00 16.77 ? 484 GLY B N 1 ATOM 8111 C CA . GLY B 1 484 ? -3.205 40.792 22.066 1.00 14.76 ? 484 GLY B CA 1 ATOM 8112 C C . GLY B 1 484 ? -2.494 42.121 22.156 1.00 16.34 ? 484 GLY B C 1 ATOM 8113 O O . GLY B 1 484 ? -2.964 43.104 21.579 1.00 15.82 ? 484 GLY B O 1 ATOM 8114 N N . GLY B 1 485 ? -1.346 42.141 22.833 1.00 15.37 ? 485 GLY B N 1 ATOM 8115 C CA . GLY B 1 485 ? -0.623 43.381 23.014 1.00 14.58 ? 485 GLY B CA 1 ATOM 8116 C C . GLY B 1 485 ? 0.733 43.519 22.371 1.00 13.65 ? 485 GLY B C 1 ATOM 8117 O O . GLY B 1 485 ? 0.943 43.133 21.218 1.00 11.96 ? 485 GLY B O 1 ATOM 8118 N N . TRP B 1 486 ? 1.648 44.107 23.134 1.00 12.50 ? 486 TRP B N 1 ATOM 8119 C CA . TRP B 1 486 ? 3.002 44.353 22.672 1.00 12.77 ? 486 TRP B CA 1 ATOM 8120 C C . TRP B 1 486 ? 4.038 44.226 23.778 1.00 13.46 ? 486 TRP B C 1 ATOM 8121 O O . TRP B 1 486 ? 3.702 44.241 24.966 1.00 13.13 ? 486 TRP B O 1 ATOM 8122 C CB . TRP B 1 486 ? 3.109 45.739 21.990 1.00 13.84 ? 486 TRP B CB 1 ATOM 8123 C CG . TRP B 1 486 ? 2.656 46.902 22.845 1.00 13.72 ? 486 TRP B CG 1 ATOM 8124 C CD1 . TRP B 1 486 ? 1.393 47.415 22.921 1.00 14.78 ? 486 TRP B CD1 1 ATOM 8125 C CD2 . TRP B 1 486 ? 3.447 47.638 23.793 1.00 15.16 ? 486 TRP B CD2 1 ATOM 8126 N NE1 . TRP B 1 486 ? 1.339 48.412 23.870 1.00 14.24 ? 486 TRP B NE1 1 ATOM 8127 C CE2 . TRP B 1 486 ? 2.583 48.569 24.422 1.00 15.74 ? 486 TRP B CE2 1 ATOM 8128 C CE3 . TRP B 1 486 ? 4.807 47.599 24.180 1.00 15.24 ? 486 TRP B CE3 1 ATOM 8129 C CZ2 . TRP B 1 486 ? 3.032 49.454 25.430 1.00 13.56 ? 486 TRP B CZ2 1 ATOM 8130 C CZ3 . TRP B 1 486 ? 5.259 48.488 25.181 1.00 15.25 ? 486 TRP B CZ3 1 ATOM 8131 C CH2 . TRP B 1 486 ? 4.366 49.402 25.795 1.00 14.07 ? 486 TRP B CH2 1 ATOM 8132 N N . LEU B 1 487 ? 5.301 44.221 23.363 1.00 12.94 ? 487 LEU B N 1 ATOM 8133 C CA . LEU B 1 487 ? 6.440 44.108 24.264 1.00 13.90 ? 487 LEU B CA 1 ATOM 8134 C C . LEU B 1 487 ? 7.596 44.908 23.674 1.00 12.94 ? 487 LEU B C 1 ATOM 8135 O O . LEU B 1 487 ? 7.900 44.776 22.488 1.00 13.55 ? 487 LEU B O 1 ATOM 8136 C CB . LEU B 1 487 ? 6.834 42.633 24.399 1.00 13.78 ? 487 LEU B CB 1 ATOM 8137 C CG . LEU B 1 487 ? 8.033 42.204 25.232 1.00 12.63 ? 487 LEU B CG 1 ATOM 8138 C CD1 . LEU B 1 487 ? 7.765 42.404 26.720 1.00 13.71 ? 487 LEU B CD1 1 ATOM 8139 C CD2 . LEU B 1 487 ? 8.340 40.746 24.912 1.00 14.36 ? 487 LEU B CD2 1 ATOM 8140 N N . LEU B 1 488 ? 8.219 45.753 24.492 1.00 13.70 ? 488 LEU B N 1 ATOM 8141 C CA . LEU B 1 488 ? 9.359 46.545 24.035 1.00 12.37 ? 488 LEU B CA 1 ATOM 8142 C C . LEU B 1 488 ? 10.630 46.077 24.737 1.00 11.62 ? 488 LEU B C 1 ATOM 8143 O O . LEU B 1 488 ? 10.736 46.121 25.966 1.00 11.06 ? 488 LEU B O 1 ATOM 8144 C CB . LEU B 1 488 ? 9.134 48.052 24.239 1.00 11.00 ? 488 LEU B CB 1 ATOM 8145 C CG . LEU B 1 488 ? 10.233 48.981 23.689 1.00 12.55 ? 488 LEU B CG 1 ATOM 8146 C CD1 . LEU B 1 488 ? 10.377 48.868 22.194 1.00 10.16 ? 488 LEU B CD1 1 ATOM 8147 C CD2 . LEU B 1 488 ? 9.943 50.407 24.049 1.00 14.17 ? 488 LEU B CD2 1 ATOM 8148 N N . LEU B 1 489 ? 11.564 45.575 23.932 1.00 10.75 ? 489 LEU B N 1 ATOM 8149 C CA . LEU B 1 489 ? 12.840 45.067 24.418 1.00 11.40 ? 489 LEU B CA 1 ATOM 8150 C C . LEU B 1 489 ? 14.019 45.845 23.866 1.00 13.36 ? 489 LEU B C 1 ATOM 8151 O O . LEU B 1 489 ? 13.909 46.503 22.828 1.00 13.92 ? 489 LEU B O 1 ATOM 8152 C CB . LEU B 1 489 ? 13.024 43.590 24.035 1.00 11.14 ? 489 LEU B CB 1 ATOM 8153 C CG . LEU B 1 489 ? 12.005 42.550 24.491 1.00 10.79 ? 489 LEU B CG 1 ATOM 8154 C CD1 . LEU B 1 489 ? 12.419 41.191 23.996 1.00 10.69 ? 489 LEU B CD1 1 ATOM 8155 C CD2 . LEU B 1 489 ? 11.839 42.554 25.997 1.00 9.33 ? 489 LEU B CD2 1 ATOM 8156 N N . ALA B 1 490 ? 15.149 45.740 24.565 1.00 11.78 ? 490 ALA B N 1 ATOM 8157 C CA . ALA B 1 490 ? 16.389 46.381 24.155 1.00 14.99 ? 490 ALA B CA 1 ATOM 8158 C C . ALA B 1 490 ? 17.598 45.525 24.492 1.00 15.82 ? 490 ALA B C 1 ATOM 8159 O O . ALA B 1 490 ? 17.635 44.896 25.546 1.00 15.25 ? 490 ALA B O 1 ATOM 8160 C CB . ALA B 1 490 ? 16.537 47.756 24.797 1.00 16.40 ? 490 ALA B CB 1 ATOM 8161 N N . PHE B 1 491 ? 18.540 45.436 23.553 1.00 15.42 ? 491 PHE B N 1 ATOM 8162 C CA . PHE B 1 491 ? 19.788 44.709 23.777 1.00 15.30 ? 491 PHE B CA 1 ATOM 8163 C C . PHE B 1 491 ? 20.953 45.446 23.127 1.00 15.96 ? 491 PHE B C 1 ATOM 8164 O O . PHE B 1 491 ? 20.787 46.082 22.085 1.00 14.31 ? 491 PHE B O 1 ATOM 8165 C CB . PHE B 1 491 ? 19.718 43.214 23.365 1.00 12.80 ? 491 PHE B CB 1 ATOM 8166 C CG . PHE B 1 491 ? 19.697 42.953 21.876 1.00 14.24 ? 491 PHE B CG 1 ATOM 8167 C CD1 . PHE B 1 491 ? 18.476 42.849 21.185 1.00 12.74 ? 491 PHE B CD1 1 ATOM 8168 C CD2 . PHE B 1 491 ? 20.898 42.711 21.172 1.00 14.41 ? 491 PHE B CD2 1 ATOM 8169 C CE1 . PHE B 1 491 ? 18.450 42.500 19.811 1.00 12.21 ? 491 PHE B CE1 1 ATOM 8170 C CE2 . PHE B 1 491 ? 20.888 42.364 19.798 1.00 16.10 ? 491 PHE B CE2 1 ATOM 8171 C CZ . PHE B 1 491 ? 19.657 42.256 19.116 1.00 15.83 ? 491 PHE B CZ 1 ATOM 8172 N N . ARG B 1 492 ? 22.119 45.368 23.769 1.00 17.27 ? 492 ARG B N 1 ATOM 8173 C CA . ARG B 1 492 ? 23.327 46.011 23.271 1.00 18.51 ? 492 ARG B CA 1 ATOM 8174 C C . ARG B 1 492 ? 24.044 45.063 22.323 1.00 17.90 ? 492 ARG B C 1 ATOM 8175 O O . ARG B 1 492 ? 24.248 43.889 22.642 1.00 18.00 ? 492 ARG B O 1 ATOM 8176 C CB . ARG B 1 492 ? 24.241 46.421 24.430 1.00 21.77 ? 492 ARG B CB 1 ATOM 8177 C CG . ARG B 1 492 ? 25.222 47.515 24.054 1.00 26.79 ? 492 ARG B CG 1 ATOM 8178 C CD . ARG B 1 492 ? 25.955 48.082 25.246 1.00 29.20 ? 492 ARG B CD 1 ATOM 8179 N NE . ARG B 1 492 ? 26.799 49.207 24.842 1.00 33.78 ? 492 ARG B NE 1 ATOM 8180 C CZ . ARG B 1 492 ? 27.286 50.132 25.666 1.00 37.29 ? 492 ARG B CZ 1 ATOM 8181 N NH1 . ARG B 1 492 ? 27.024 50.089 26.968 1.00 38.45 ? 492 ARG B NH1 1 ATOM 8182 N NH2 . ARG B 1 492 ? 28.041 51.110 25.181 1.00 38.59 ? 492 ARG B NH2 1 ATOM 8183 N N . THR B 1 493 ? 24.414 45.584 21.157 1.00 17.02 ? 493 THR B N 1 ATOM 8184 C CA . THR B 1 493 ? 25.095 44.803 20.129 1.00 15.14 ? 493 THR B CA 1 ATOM 8185 C C . THR B 1 493 ? 26.591 44.564 20.394 1.00 15.35 ? 493 THR B C 1 ATOM 8186 O O . THR B 1 493 ? 27.457 44.959 19.607 1.00 15.37 ? 493 THR B O 1 ATOM 8187 C CB . THR B 1 493 ? 24.858 45.413 18.731 1.00 14.63 ? 493 THR B CB 1 ATOM 8188 O OG1 . THR B 1 493 ? 25.256 46.788 18.726 1.00 13.23 ? 493 THR B OG1 1 ATOM 8189 C CG2 . THR B 1 493 ? 23.388 45.317 18.352 1.00 13.62 ? 493 THR B CG2 1 ATOM 8190 N N . ASP B 1 494 ? 26.864 43.855 21.487 1.00 15.00 ? 494 ASP B N 1 ATOM 8191 C CA . ASP B 1 494 ? 28.221 43.544 21.949 1.00 16.08 ? 494 ASP B CA 1 ATOM 8192 C C . ASP B 1 494 ? 28.689 42.115 21.646 1.00 15.40 ? 494 ASP B C 1 ATOM 8193 O O . ASP B 1 494 ? 29.704 41.661 22.183 1.00 14.39 ? 494 ASP B O 1 ATOM 8194 C CB . ASP B 1 494 ? 28.304 43.799 23.474 1.00 17.92 ? 494 ASP B CB 1 ATOM 8195 C CG . ASP B 1 494 ? 27.249 43.013 24.291 1.00 22.59 ? 494 ASP B CG 1 ATOM 8196 O OD1 . ASP B 1 494 ? 26.605 42.076 23.759 1.00 22.20 ? 494 ASP B OD1 1 ATOM 8197 O OD2 . ASP B 1 494 ? 27.082 43.325 25.491 1.00 26.54 ? 494 ASP B OD2 1 ATOM 8198 N N . ASN B 1 495 ? 27.951 41.409 20.797 1.00 15.17 ? 495 ASN B N 1 ATOM 8199 C CA . ASN B 1 495 ? 28.272 40.013 20.509 1.00 15.61 ? 495 ASN B CA 1 ATOM 8200 C C . ASN B 1 495 ? 27.948 39.650 19.057 1.00 15.24 ? 495 ASN B C 1 ATOM 8201 O O . ASN B 1 495 ? 26.842 39.179 18.771 1.00 14.83 ? 495 ASN B O 1 ATOM 8202 C CB . ASN B 1 495 ? 27.466 39.141 21.494 1.00 15.10 ? 495 ASN B CB 1 ATOM 8203 C CG . ASN B 1 495 ? 27.914 37.694 21.539 1.00 17.32 ? 495 ASN B CG 1 ATOM 8204 O OD1 . ASN B 1 495 ? 28.895 37.294 20.908 1.00 16.11 ? 495 ASN B OD1 1 ATOM 8205 N ND2 . ASN B 1 495 ? 27.170 36.887 22.289 1.00 14.26 ? 495 ASN B ND2 1 ATOM 8206 N N . PRO B 1 496 ? 28.911 39.839 18.124 1.00 14.64 ? 496 PRO B N 1 ATOM 8207 C CA . PRO B 1 496 ? 28.691 39.517 16.707 1.00 14.72 ? 496 PRO B CA 1 ATOM 8208 C C . PRO B 1 496 ? 28.301 38.053 16.486 1.00 14.88 ? 496 PRO B C 1 ATOM 8209 O O . PRO B 1 496 ? 28.947 37.138 17.012 1.00 13.37 ? 496 PRO B O 1 ATOM 8210 C CB . PRO B 1 496 ? 30.044 39.827 16.071 1.00 14.76 ? 496 PRO B CB 1 ATOM 8211 C CG . PRO B 1 496 ? 30.588 40.890 16.941 1.00 15.82 ? 496 PRO B CG 1 ATOM 8212 C CD . PRO B 1 496 ? 30.264 40.393 18.313 1.00 15.51 ? 496 PRO B CD 1 ATOM 8213 N N . GLY B 1 497 ? 27.190 37.858 15.782 1.00 13.86 ? 497 GLY B N 1 ATOM 8214 C CA . GLY B 1 497 ? 26.710 36.519 15.519 1.00 13.70 ? 497 GLY B CA 1 ATOM 8215 C C . GLY B 1 497 ? 25.297 36.444 15.003 1.00 12.99 ? 497 GLY B C 1 ATOM 8216 O O . GLY B 1 497 ? 24.615 37.464 14.908 1.00 15.05 ? 497 GLY B O 1 ATOM 8217 N N . ALA B 1 498 ? 24.882 35.234 14.634 1.00 11.51 ? 498 ALA B N 1 ATOM 8218 C CA . ALA B 1 498 ? 23.531 34.968 14.143 1.00 11.01 ? 498 ALA B CA 1 ATOM 8219 C C . ALA B 1 498 ? 22.750 34.447 15.350 1.00 11.04 ? 498 ALA B C 1 ATOM 8220 O O . ALA B 1 498 ? 22.987 33.335 15.830 1.00 11.83 ? 498 ALA B O 1 ATOM 8221 C CB . ALA B 1 498 ? 23.569 33.945 13.021 1.00 10.14 ? 498 ALA B CB 1 ATOM 8222 N N . TRP B 1 499 ? 21.872 35.298 15.878 1.00 10.48 ? 499 TRP B N 1 ATOM 8223 C CA . TRP B 1 499 ? 21.103 34.971 17.075 1.00 9.90 ? 499 TRP B CA 1 ATOM 8224 C C . TRP B 1 499 ? 19.609 34.845 16.910 1.00 10.11 ? 499 TRP B C 1 ATOM 8225 O O . TRP B 1 499 ? 18.934 35.796 16.516 1.00 10.47 ? 499 TRP B O 1 ATOM 8226 C CB . TRP B 1 499 ? 21.384 35.996 18.180 1.00 10.09 ? 499 TRP B CB 1 ATOM 8227 C CG . TRP B 1 499 ? 22.842 36.253 18.437 1.00 9.45 ? 499 TRP B CG 1 ATOM 8228 C CD1 . TRP B 1 499 ? 23.530 37.402 18.149 1.00 11.79 ? 499 TRP B CD1 1 ATOM 8229 C CD2 . TRP B 1 499 ? 23.789 35.352 19.022 1.00 9.42 ? 499 TRP B CD2 1 ATOM 8230 N NE1 . TRP B 1 499 ? 24.847 37.274 18.519 1.00 11.71 ? 499 TRP B NE1 1 ATOM 8231 C CE2 . TRP B 1 499 ? 25.037 36.030 19.059 1.00 10.57 ? 499 TRP B CE2 1 ATOM 8232 C CE3 . TRP B 1 499 ? 23.711 34.032 19.529 1.00 9.13 ? 499 TRP B CE3 1 ATOM 8233 C CZ2 . TRP B 1 499 ? 26.204 35.435 19.586 1.00 9.72 ? 499 TRP B CZ2 1 ATOM 8234 C CZ3 . TRP B 1 499 ? 24.874 33.441 20.060 1.00 5.96 ? 499 TRP B CZ3 1 ATOM 8235 C CH2 . TRP B 1 499 ? 26.104 34.150 20.083 1.00 9.50 ? 499 TRP B CH2 1 ATOM 8236 N N . LEU B 1 500 ? 19.088 33.678 17.277 1.00 10.96 ? 500 LEU B N 1 ATOM 8237 C CA . LEU B 1 500 ? 17.655 33.436 17.204 1.00 10.03 ? 500 LEU B CA 1 ATOM 8238 C C . LEU B 1 500 ? 16.909 34.168 18.299 1.00 9.98 ? 500 LEU B C 1 ATOM 8239 O O . LEU B 1 500 ? 17.401 34.305 19.422 1.00 8.01 ? 500 LEU B O 1 ATOM 8240 C CB . LEU B 1 500 ? 17.342 31.949 17.325 1.00 10.86 ? 500 LEU B CB 1 ATOM 8241 C CG . LEU B 1 500 ? 17.706 31.047 16.157 1.00 11.37 ? 500 LEU B CG 1 ATOM 8242 C CD1 . LEU B 1 500 ? 17.414 29.622 16.559 1.00 12.89 ? 500 LEU B CD1 1 ATOM 8243 C CD2 . LEU B 1 500 ? 16.917 31.439 14.915 1.00 11.68 ? 500 LEU B CD2 1 ATOM 8244 N N . PHE B 1 501 ? 15.765 34.719 17.914 1.00 9.64 ? 501 PHE B N 1 ATOM 8245 C CA . PHE B 1 501 ? 14.875 35.406 18.826 1.00 10.38 ? 501 PHE B CA 1 ATOM 8246 C C . PHE B 1 501 ? 13.567 34.729 18.488 1.00 11.23 ? 501 PHE B C 1 ATOM 8247 O O . PHE B 1 501 ? 12.991 34.949 17.416 1.00 9.51 ? 501 PHE B O 1 ATOM 8248 C CB . PHE B 1 501 ? 14.835 36.907 18.558 1.00 10.79 ? 501 PHE B CB 1 ATOM 8249 C CG . PHE B 1 501 ? 13.859 37.659 19.424 1.00 12.00 ? 501 PHE B CG 1 ATOM 8250 C CD1 . PHE B 1 501 ? 13.975 37.644 20.825 1.00 11.34 ? 501 PHE B CD1 1 ATOM 8251 C CD2 . PHE B 1 501 ? 12.797 38.373 18.836 1.00 12.70 ? 501 PHE B CD2 1 ATOM 8252 C CE1 . PHE B 1 501 ? 13.048 38.325 21.641 1.00 11.10 ? 501 PHE B CE1 1 ATOM 8253 C CE2 . PHE B 1 501 ? 11.861 39.060 19.631 1.00 13.05 ? 501 PHE B CE2 1 ATOM 8254 C CZ . PHE B 1 501 ? 11.986 39.036 21.043 1.00 11.58 ? 501 PHE B CZ 1 ATOM 8255 N N . HIS B 1 502 ? 13.129 33.879 19.409 1.00 11.18 ? 502 HIS B N 1 ATOM 8256 C CA . HIS B 1 502 ? 11.937 33.090 19.196 1.00 12.30 ? 502 HIS B CA 1 ATOM 8257 C C . HIS B 1 502 ? 11.061 32.853 20.397 1.00 12.24 ? 502 HIS B C 1 ATOM 8258 O O . HIS B 1 502 ? 11.467 33.076 21.531 1.00 13.12 ? 502 HIS B O 1 ATOM 8259 C CB . HIS B 1 502 ? 12.349 31.722 18.628 1.00 13.36 ? 502 HIS B CB 1 ATOM 8260 C CG . HIS B 1 502 ? 13.179 30.882 19.551 1.00 14.74 ? 502 HIS B CG 1 ATOM 8261 N ND1 . HIS B 1 502 ? 12.622 29.954 20.402 1.00 15.83 ? 502 HIS B ND1 1 ATOM 8262 C CD2 . HIS B 1 502 ? 14.520 30.791 19.719 1.00 16.43 ? 502 HIS B CD2 1 ATOM 8263 C CE1 . HIS B 1 502 ? 13.584 29.323 21.050 1.00 16.76 ? 502 HIS B CE1 1 ATOM 8264 N NE2 . HIS B 1 502 ? 14.746 29.811 20.655 1.00 17.57 ? 502 HIS B NE2 1 ATOM 8265 N N . CYS B 1 503 ? 9.856 32.357 20.120 1.00 12.10 ? 503 CYS B N 1 ATOM 8266 C CA . CYS B 1 503 ? 8.924 31.977 21.168 1.00 12.05 ? 503 CYS B CA 1 ATOM 8267 C C . CYS B 1 503 ? 9.430 30.596 21.586 1.00 10.26 ? 503 CYS B C 1 ATOM 8268 O O . CYS B 1 503 ? 9.769 29.776 20.726 1.00 10.78 ? 503 CYS B O 1 ATOM 8269 C CB . CYS B 1 503 ? 7.505 31.859 20.633 1.00 11.24 ? 503 CYS B CB 1 ATOM 8270 S SG . CYS B 1 503 ? 6.420 31.010 21.786 1.00 14.41 ? 503 CYS B SG 1 ATOM 8271 N N . HIS B 1 504 ? 9.488 30.348 22.889 1.00 9.61 ? 504 HIS B N 1 ATOM 8272 C CA . HIS B 1 504 ? 9.985 29.073 23.377 1.00 10.17 ? 504 HIS B CA 1 ATOM 8273 C C . HIS B 1 504 ? 8.965 27.942 23.453 1.00 9.60 ? 504 HIS B C 1 ATOM 8274 O O . HIS B 1 504 ? 9.293 26.835 23.888 1.00 11.32 ? 504 HIS B O 1 ATOM 8275 C CB . HIS B 1 504 ? 10.754 29.244 24.683 1.00 10.54 ? 504 HIS B CB 1 ATOM 8276 C CG . HIS B 1 504 ? 11.979 28.389 24.764 1.00 10.41 ? 504 HIS B CG 1 ATOM 8277 N ND1 . HIS B 1 504 ? 11.926 27.018 24.891 1.00 10.05 ? 504 HIS B ND1 1 ATOM 8278 C CD2 . HIS B 1 504 ? 13.291 28.713 24.728 1.00 10.00 ? 504 HIS B CD2 1 ATOM 8279 C CE1 . HIS B 1 504 ? 13.156 26.536 24.934 1.00 8.71 ? 504 HIS B CE1 1 ATOM 8280 N NE2 . HIS B 1 504 ? 14.005 27.543 24.841 1.00 12.11 ? 504 HIS B NE2 1 ATOM 8281 N N . ILE B 1 505 ? 7.721 28.214 23.050 1.00 10.67 ? 505 ILE B N 1 ATOM 8282 C CA . ILE B 1 505 ? 6.720 27.145 23.001 1.00 10.45 ? 505 ILE B CA 1 ATOM 8283 C C . ILE B 1 505 ? 7.143 26.398 21.738 1.00 11.29 ? 505 ILE B C 1 ATOM 8284 O O . ILE B 1 505 ? 7.162 26.977 20.649 1.00 10.89 ? 505 ILE B O 1 ATOM 8285 C CB . ILE B 1 505 ? 5.262 27.660 22.876 1.00 11.06 ? 505 ILE B CB 1 ATOM 8286 C CG1 . ILE B 1 505 ? 4.815 28.267 24.205 1.00 9.47 ? 505 ILE B CG1 1 ATOM 8287 C CG2 . ILE B 1 505 ? 4.308 26.508 22.481 1.00 8.00 ? 505 ILE B CG2 1 ATOM 8288 C CD1 . ILE B 1 505 ? 3.480 29.002 24.154 1.00 10.47 ? 505 ILE B CD1 1 ATOM 8289 N N . ALA B 1 506 ? 7.586 25.154 21.930 1.00 11.84 ? 506 ALA B N 1 ATOM 8290 C CA . ALA B 1 506 ? 8.074 24.291 20.852 1.00 12.87 ? 506 ALA B CA 1 ATOM 8291 C C . ALA B 1 506 ? 7.182 24.229 19.620 1.00 12.45 ? 506 ALA B C 1 ATOM 8292 O O . ALA B 1 506 ? 7.673 24.300 18.500 1.00 13.16 ? 506 ALA B O 1 ATOM 8293 C CB . ALA B 1 506 ? 8.334 22.892 21.377 1.00 10.53 ? 506 ALA B CB 1 ATOM 8294 N N . TRP B 1 507 ? 5.870 24.210 19.845 1.00 12.85 ? 507 TRP B N 1 ATOM 8295 C CA . TRP B 1 507 ? 4.887 24.134 18.766 1.00 11.94 ? 507 TRP B CA 1 ATOM 8296 C C . TRP B 1 507 ? 4.846 25.389 17.906 1.00 12.45 ? 507 TRP B C 1 ATOM 8297 O O . TRP B 1 507 ? 4.598 25.315 16.693 1.00 12.99 ? 507 TRP B O 1 ATOM 8298 C CB . TRP B 1 507 ? 3.495 23.845 19.339 1.00 13.16 ? 507 TRP B CB 1 ATOM 8299 C CG . TRP B 1 507 ? 3.405 22.929 20.581 1.00 13.87 ? 507 TRP B CG 1 ATOM 8300 C CD1 . TRP B 1 507 ? 2.584 23.129 21.653 1.00 13.52 ? 507 TRP B CD1 1 ATOM 8301 C CD2 . TRP B 1 507 ? 4.141 21.712 20.868 1.00 13.87 ? 507 TRP B CD2 1 ATOM 8302 N NE1 . TRP B 1 507 ? 2.754 22.135 22.590 1.00 13.67 ? 507 TRP B NE1 1 ATOM 8303 C CE2 . TRP B 1 507 ? 3.701 21.254 22.143 1.00 15.08 ? 507 TRP B CE2 1 ATOM 8304 C CE3 . TRP B 1 507 ? 5.131 20.966 20.184 1.00 13.66 ? 507 TRP B CE3 1 ATOM 8305 C CZ2 . TRP B 1 507 ? 4.217 20.086 22.753 1.00 15.36 ? 507 TRP B CZ2 1 ATOM 8306 C CZ3 . TRP B 1 507 ? 5.651 19.801 20.790 1.00 14.89 ? 507 TRP B CZ3 1 ATOM 8307 C CH2 . TRP B 1 507 ? 5.188 19.379 22.066 1.00 16.16 ? 507 TRP B CH2 1 ATOM 8308 N N . HIS B 1 508 ? 5.155 26.520 18.540 1.00 10.50 ? 508 HIS B N 1 ATOM 8309 C CA . HIS B 1 508 ? 5.166 27.825 17.891 1.00 12.62 ? 508 HIS B CA 1 ATOM 8310 C C . HIS B 1 508 ? 6.435 28.092 17.095 1.00 11.89 ? 508 HIS B C 1 ATOM 8311 O O . HIS B 1 508 ? 6.348 28.586 15.970 1.00 12.82 ? 508 HIS B O 1 ATOM 8312 C CB . HIS B 1 508 ? 4.921 28.946 18.913 1.00 11.66 ? 508 HIS B CB 1 ATOM 8313 C CG . HIS B 1 508 ? 3.574 28.889 19.574 1.00 13.83 ? 508 HIS B CG 1 ATOM 8314 N ND1 . HIS B 1 508 ? 3.212 29.743 20.595 1.00 13.23 ? 508 HIS B ND1 1 ATOM 8315 C CD2 . HIS B 1 508 ? 2.509 28.076 19.370 1.00 13.78 ? 508 HIS B CD2 1 ATOM 8316 C CE1 . HIS B 1 508 ? 1.983 29.455 20.988 1.00 14.79 ? 508 HIS B CE1 1 ATOM 8317 N NE2 . HIS B 1 508 ? 1.535 28.448 20.262 1.00 13.51 ? 508 HIS B NE2 1 ATOM 8318 N N . VAL B 1 509 ? 7.602 27.755 17.658 1.00 12.96 ? 509 VAL B N 1 ATOM 8319 C CA . VAL B 1 509 ? 8.875 27.956 16.949 1.00 12.78 ? 509 VAL B CA 1 ATOM 8320 C C . VAL B 1 509 ? 8.966 26.968 15.780 1.00 13.08 ? 509 VAL B C 1 ATOM 8321 O O . VAL B 1 509 ? 9.521 27.294 14.729 1.00 12.80 ? 509 VAL B O 1 ATOM 8322 C CB . VAL B 1 509 ? 10.131 27.923 17.895 1.00 12.90 ? 509 VAL B CB 1 ATOM 8323 C CG1 . VAL B 1 509 ? 10.337 26.555 18.544 1.00 11.49 ? 509 VAL B CG1 1 ATOM 8324 C CG2 . VAL B 1 509 ? 11.381 28.376 17.136 1.00 10.94 ? 509 VAL B CG2 1 ATOM 8325 N N . SER B 1 510 ? 8.327 25.806 15.953 1.00 13.88 ? 510 SER B N 1 ATOM 8326 C CA . SER B 1 510 ? 8.241 24.775 14.914 1.00 14.01 ? 510 SER B CA 1 ATOM 8327 C C . SER B 1 510 ? 7.372 25.349 13.794 1.00 11.56 ? 510 SER B C 1 ATOM 8328 O O . SER B 1 510 ? 7.703 25.227 12.614 1.00 10.70 ? 510 SER B O 1 ATOM 8329 C CB . SER B 1 510 ? 7.569 23.503 15.445 1.00 15.06 ? 510 SER B CB 1 ATOM 8330 O OG . SER B 1 510 ? 8.461 22.714 16.204 1.00 18.38 ? 510 SER B OG 1 ATOM 8331 N N . GLY B 1 511 ? 6.308 26.044 14.205 1.00 11.00 ? 511 GLY B N 1 ATOM 8332 C CA . GLY B 1 511 ? 5.373 26.673 13.285 1.00 9.07 ? 511 GLY B CA 1 ATOM 8333 C C . GLY B 1 511 ? 5.887 27.953 12.647 1.00 10.37 ? 511 GLY B C 1 ATOM 8334 O O . GLY B 1 511 ? 5.154 28.602 11.896 1.00 9.49 ? 511 GLY B O 1 ATOM 8335 N N . GLY B 1 512 ? 7.120 28.335 12.989 1.00 10.20 ? 512 GLY B N 1 ATOM 8336 C CA . GLY B 1 512 ? 7.742 29.514 12.409 1.00 10.66 ? 512 GLY B CA 1 ATOM 8337 C C . GLY B 1 512 ? 7.924 30.786 13.217 1.00 9.88 ? 512 GLY B C 1 ATOM 8338 O O . GLY B 1 512 ? 8.453 31.759 12.670 1.00 11.97 ? 512 GLY B O 1 ATOM 8339 N N . LEU B 1 513 ? 7.550 30.790 14.498 1.00 9.37 ? 513 LEU B N 1 ATOM 8340 C CA . LEU B 1 513 ? 7.679 31.995 15.327 1.00 9.41 ? 513 LEU B CA 1 ATOM 8341 C C . LEU B 1 513 ? 9.103 32.308 15.769 1.00 9.50 ? 513 LEU B C 1 ATOM 8342 O O . LEU B 1 513 ? 9.475 32.078 16.927 1.00 9.49 ? 513 LEU B O 1 ATOM 8343 C CB . LEU B 1 513 ? 6.754 31.941 16.546 1.00 9.84 ? 513 LEU B CB 1 ATOM 8344 C CG . LEU B 1 513 ? 6.027 33.238 16.923 1.00 9.07 ? 513 LEU B CG 1 ATOM 8345 C CD1 . LEU B 1 513 ? 4.922 32.883 17.878 1.00 9.14 ? 513 LEU B CD1 1 ATOM 8346 C CD2 . LEU B 1 513 ? 6.929 34.296 17.538 1.00 7.84 ? 513 LEU B CD2 1 ATOM 8347 N N . SER B 1 514 ? 9.852 32.920 14.857 1.00 8.58 ? 514 SER B N 1 ATOM 8348 C CA . SER B 1 514 ? 11.233 33.296 15.106 1.00 8.43 ? 514 SER B CA 1 ATOM 8349 C C . SER B 1 514 ? 11.796 34.233 14.062 1.00 10.46 ? 514 SER B C 1 ATOM 8350 O O . SER B 1 514 ? 11.268 34.355 12.955 1.00 9.85 ? 514 SER B O 1 ATOM 8351 C CB . SER B 1 514 ? 12.133 32.045 15.139 1.00 8.14 ? 514 SER B CB 1 ATOM 8352 O OG . SER B 1 514 ? 13.482 32.347 15.479 1.00 7.97 ? 514 SER B OG 1 ATOM 8353 N N . VAL B 1 515 ? 12.828 34.957 14.484 1.00 10.33 ? 515 VAL B N 1 ATOM 8354 C CA . VAL B 1 515 ? 13.610 35.815 13.614 1.00 10.35 ? 515 VAL B CA 1 ATOM 8355 C C . VAL B 1 515 ? 15.038 35.425 13.939 1.00 10.65 ? 515 VAL B C 1 ATOM 8356 O O . VAL B 1 515 ? 15.279 34.650 14.875 1.00 9.54 ? 515 VAL B O 1 ATOM 8357 C CB . VAL B 1 515 ? 13.410 37.351 13.802 1.00 10.07 ? 515 VAL B CB 1 ATOM 8358 C CG1 . VAL B 1 515 ? 12.113 37.795 13.165 1.00 12.42 ? 515 VAL B CG1 1 ATOM 8359 C CG2 . VAL B 1 515 ? 13.487 37.761 15.242 1.00 12.61 ? 515 VAL B CG2 1 ATOM 8360 N N . ASP B 1 516 ? 15.970 35.925 13.143 1.00 10.07 ? 516 ASP B N 1 ATOM 8361 C CA . ASP B 1 516 ? 17.378 35.640 13.341 1.00 11.63 ? 516 ASP B CA 1 ATOM 8362 C C . ASP B 1 516 ? 18.104 36.971 13.257 1.00 10.79 ? 516 ASP B C 1 ATOM 8363 O O . ASP B 1 516 ? 18.235 37.551 12.174 1.00 10.75 ? 516 ASP B O 1 ATOM 8364 C CB . ASP B 1 516 ? 17.866 34.654 12.260 1.00 11.35 ? 516 ASP B CB 1 ATOM 8365 C CG . ASP B 1 516 ? 19.330 34.229 12.427 1.00 14.04 ? 516 ASP B CG 1 ATOM 8366 O OD1 . ASP B 1 516 ? 20.071 34.809 13.255 1.00 12.01 ? 516 ASP B OD1 1 ATOM 8367 O OD2 . ASP B 1 516 ? 19.747 33.306 11.687 1.00 14.51 ? 516 ASP B OD2 1 ATOM 8368 N N . PHE B 1 517 ? 18.549 37.455 14.416 1.00 9.41 ? 517 PHE B N 1 ATOM 8369 C CA . PHE B 1 517 ? 19.292 38.703 14.499 1.00 10.67 ? 517 PHE B CA 1 ATOM 8370 C C . PHE B 1 517 ? 20.721 38.464 14.032 1.00 10.41 ? 517 PHE B C 1 ATOM 8371 O O . PHE B 1 517 ? 21.516 37.827 14.733 1.00 11.05 ? 517 PHE B O 1 ATOM 8372 C CB . PHE B 1 517 ? 19.322 39.258 15.937 1.00 10.95 ? 517 PHE B CB 1 ATOM 8373 C CG . PHE B 1 517 ? 18.046 39.935 16.370 1.00 12.40 ? 517 PHE B CG 1 ATOM 8374 C CD1 . PHE B 1 517 ? 17.529 41.030 15.654 1.00 11.60 ? 517 PHE B CD1 1 ATOM 8375 C CD2 . PHE B 1 517 ? 17.366 39.499 17.517 1.00 11.98 ? 517 PHE B CD2 1 ATOM 8376 C CE1 . PHE B 1 517 ? 16.346 41.685 16.074 1.00 12.97 ? 517 PHE B CE1 1 ATOM 8377 C CE2 . PHE B 1 517 ? 16.172 40.151 17.957 1.00 12.44 ? 517 PHE B CE2 1 ATOM 8378 C CZ . PHE B 1 517 ? 15.664 41.243 17.232 1.00 13.36 ? 517 PHE B CZ 1 ATOM 8379 N N . LEU B 1 518 ? 21.019 38.912 12.816 1.00 11.54 ? 518 LEU B N 1 ATOM 8380 C CA . LEU B 1 518 ? 22.366 38.792 12.284 1.00 12.42 ? 518 LEU B CA 1 ATOM 8381 C C . LEU B 1 518 ? 23.079 40.057 12.742 1.00 12.29 ? 518 LEU B C 1 ATOM 8382 O O . LEU B 1 518 ? 23.000 41.123 12.123 1.00 12.38 ? 518 LEU B O 1 ATOM 8383 C CB . LEU B 1 518 ? 22.371 38.640 10.765 1.00 11.42 ? 518 LEU B CB 1 ATOM 8384 C CG . LEU B 1 518 ? 23.748 38.380 10.143 1.00 11.12 ? 518 LEU B CG 1 ATOM 8385 C CD1 . LEU B 1 518 ? 24.380 37.079 10.620 1.00 11.37 ? 518 LEU B CD1 1 ATOM 8386 C CD2 . LEU B 1 518 ? 23.586 38.372 8.664 1.00 11.05 ? 518 LEU B CD2 1 ATOM 8387 N N . GLU B 1 519 ? 23.716 39.914 13.893 1.00 12.55 ? 519 GLU B N 1 ATOM 8388 C CA . GLU B 1 519 ? 24.429 40.986 14.562 1.00 13.92 ? 519 GLU B CA 1 ATOM 8389 C C . GLU B 1 519 ? 25.851 41.152 14.069 1.00 13.73 ? 519 GLU B C 1 ATOM 8390 O O . GLU B 1 519 ? 26.660 40.223 14.159 1.00 12.20 ? 519 GLU B O 1 ATOM 8391 C CB . GLU B 1 519 ? 24.429 40.683 16.050 1.00 12.82 ? 519 GLU B CB 1 ATOM 8392 C CG . GLU B 1 519 ? 24.954 41.758 16.944 1.00 14.83 ? 519 GLU B CG 1 ATOM 8393 C CD . GLU B 1 519 ? 24.768 41.391 18.390 1.00 15.50 ? 519 GLU B CD 1 ATOM 8394 O OE1 . GLU B 1 519 ? 23.798 40.678 18.712 1.00 16.67 ? 519 GLU B OE1 1 ATOM 8395 O OE2 . GLU B 1 519 ? 25.603 41.794 19.214 1.00 15.14 ? 519 GLU B OE2 1 ATOM 8396 N N . ARG B 1 520 ? 26.137 42.355 13.562 1.00 14.20 ? 520 ARG B N 1 ATOM 8397 C CA . ARG B 1 520 ? 27.453 42.752 13.041 1.00 15.01 ? 520 ARG B CA 1 ATOM 8398 C C . ARG B 1 520 ? 28.127 41.672 12.159 1.00 15.74 ? 520 ARG B C 1 ATOM 8399 O O . ARG B 1 520 ? 29.191 41.147 12.520 1.00 14.78 ? 520 ARG B O 1 ATOM 8400 C CB . ARG B 1 520 ? 28.359 43.161 14.215 1.00 15.23 ? 520 ARG B CB 1 ATOM 8401 C CG . ARG B 1 520 ? 27.832 44.342 15.031 1.00 16.85 ? 520 ARG B CG 1 ATOM 8402 C CD . ARG B 1 520 ? 28.417 44.367 16.440 1.00 17.08 ? 520 ARG B CD 1 ATOM 8403 N NE . ARG B 1 520 ? 29.872 44.517 16.442 1.00 18.66 ? 520 ARG B NE 1 ATOM 8404 C CZ . ARG B 1 520 ? 30.638 44.523 17.532 1.00 18.60 ? 520 ARG B CZ 1 ATOM 8405 N NH1 . ARG B 1 520 ? 30.111 44.396 18.745 1.00 17.66 ? 520 ARG B NH1 1 ATOM 8406 N NH2 . ARG B 1 520 ? 31.954 44.600 17.400 1.00 18.44 ? 520 ARG B NH2 1 ATOM 8407 N N . PRO B 1 521 ? 27.515 41.331 10.995 1.00 16.77 ? 521 PRO B N 1 ATOM 8408 C CA . PRO B 1 521 ? 28.048 40.311 10.076 1.00 19.03 ? 521 PRO B CA 1 ATOM 8409 C C . PRO B 1 521 ? 29.502 40.439 9.623 1.00 21.18 ? 521 PRO B C 1 ATOM 8410 O O . PRO B 1 521 ? 30.185 39.426 9.456 1.00 22.53 ? 521 PRO B O 1 ATOM 8411 C CB . PRO B 1 521 ? 27.076 40.368 8.892 1.00 19.99 ? 521 PRO B CB 1 ATOM 8412 C CG . PRO B 1 521 ? 26.541 41.745 8.936 1.00 19.67 ? 521 PRO B CG 1 ATOM 8413 C CD . PRO B 1 521 ? 26.310 41.943 10.402 1.00 16.99 ? 521 PRO B CD 1 ATOM 8414 N N . ALA B 1 522 ? 29.971 41.680 9.473 1.00 24.24 ? 522 ALA B N 1 ATOM 8415 C CA . ALA B 1 522 ? 31.345 41.972 9.049 1.00 25.94 ? 522 ALA B CA 1 ATOM 8416 C C . ALA B 1 522 ? 32.363 41.612 10.135 1.00 26.94 ? 522 ALA B C 1 ATOM 8417 O O . ALA B 1 522 ? 33.432 41.066 9.838 1.00 28.89 ? 522 ALA B O 1 ATOM 8418 C CB . ALA B 1 522 ? 31.473 43.437 8.666 1.00 26.53 ? 522 ALA B CB 1 ATOM 8419 N N . ASP B 1 523 ? 31.991 41.872 11.391 1.00 25.21 ? 523 ASP B N 1 ATOM 8420 C CA . ASP B 1 523 ? 32.836 41.585 12.552 1.00 25.42 ? 523 ASP B CA 1 ATOM 8421 C C . ASP B 1 523 ? 32.844 40.097 12.898 1.00 24.96 ? 523 ASP B C 1 ATOM 8422 O O . ASP B 1 523 ? 33.850 39.575 13.376 1.00 24.27 ? 523 ASP B O 1 ATOM 8423 C CB . ASP B 1 523 ? 32.373 42.394 13.774 1.00 25.49 ? 523 ASP B CB 1 ATOM 8424 C CG . ASP B 1 523 ? 32.445 43.904 13.555 1.00 27.32 ? 523 ASP B CG 1 ATOM 8425 O OD1 . ASP B 1 523 ? 33.067 44.351 12.570 1.00 27.38 ? 523 ASP B OD1 1 ATOM 8426 O OD2 . ASP B 1 523 ? 31.872 44.650 14.375 1.00 25.95 ? 523 ASP B OD2 1 ATOM 8427 N N . LEU B 1 524 ? 31.729 39.422 12.617 1.00 24.17 ? 524 LEU B N 1 ATOM 8428 C CA . LEU B 1 524 ? 31.566 37.992 12.882 1.00 24.15 ? 524 LEU B CA 1 ATOM 8429 C C . LEU B 1 524 ? 32.537 37.108 12.101 1.00 23.40 ? 524 LEU B C 1 ATOM 8430 O O . LEU B 1 524 ? 33.150 36.214 12.683 1.00 22.49 ? 524 LEU B O 1 ATOM 8431 C CB . LEU B 1 524 ? 30.114 37.567 12.604 1.00 22.30 ? 524 LEU B CB 1 ATOM 8432 C CG . LEU B 1 524 ? 29.682 36.091 12.601 1.00 21.38 ? 524 LEU B CG 1 ATOM 8433 C CD1 . LEU B 1 524 ? 29.897 35.420 13.958 1.00 20.91 ? 524 LEU B CD1 1 ATOM 8434 C CD2 . LEU B 1 524 ? 28.231 36.019 12.183 1.00 19.65 ? 524 LEU B CD2 1 ATOM 8435 N N . ARG B 1 525 ? 32.701 37.403 10.810 1.00 25.03 ? 525 ARG B N 1 ATOM 8436 C CA . ARG B 1 525 ? 33.576 36.645 9.913 1.00 27.47 ? 525 ARG B CA 1 ATOM 8437 C C . ARG B 1 525 ? 35.043 36.574 10.356 1.00 27.97 ? 525 ARG B C 1 ATOM 8438 O O . ARG B 1 525 ? 35.637 35.491 10.350 1.00 27.77 ? 525 ARG B O 1 ATOM 8439 C CB . ARG B 1 525 ? 33.479 37.201 8.491 1.00 30.40 ? 525 ARG B CB 1 ATOM 8440 C CG . ARG B 1 525 ? 33.952 36.234 7.422 1.00 34.52 ? 525 ARG B CG 1 ATOM 8441 C CD . ARG B 1 525 ? 33.927 36.871 6.056 1.00 39.13 ? 525 ARG B CD 1 ATOM 8442 N NE . ARG B 1 525 ? 34.312 35.919 5.017 1.00 41.25 ? 525 ARG B NE 1 ATOM 8443 C CZ . ARG B 1 525 ? 34.124 36.108 3.714 1.00 42.86 ? 525 ARG B CZ 1 ATOM 8444 N NH1 . ARG B 1 525 ? 33.553 37.223 3.268 1.00 43.53 ? 525 ARG B NH1 1 ATOM 8445 N NH2 . ARG B 1 525 ? 34.502 35.174 2.851 1.00 44.24 ? 525 ARG B NH2 1 ATOM 8446 N N . GLN B 1 526 ? 35.596 37.709 10.785 1.00 28.13 ? 526 GLN B N 1 ATOM 8447 C CA . GLN B 1 526 ? 36.988 37.762 11.240 1.00 29.53 ? 526 GLN B CA 1 ATOM 8448 C C . GLN B 1 526 ? 37.215 37.237 12.664 1.00 27.39 ? 526 GLN B C 1 ATOM 8449 O O . GLN B 1 526 ? 38.351 36.946 13.045 1.00 28.03 ? 526 GLN B O 1 ATOM 8450 C CB . GLN B 1 526 ? 37.590 39.165 11.045 1.00 31.37 ? 526 GLN B CB 1 ATOM 8451 C CG . GLN B 1 526 ? 36.777 40.335 11.593 1.00 35.52 ? 526 GLN B CG 1 ATOM 8452 C CD . GLN B 1 526 ? 37.403 41.706 11.307 1.00 38.56 ? 526 GLN B CD 1 ATOM 8453 O OE1 . GLN B 1 526 ? 36.744 42.737 11.455 1.00 38.75 ? 526 GLN B OE1 1 ATOM 8454 N NE2 . GLN B 1 526 ? 38.679 41.720 10.916 1.00 40.49 ? 526 GLN B NE2 1 ATOM 8455 N N . ARG B 1 527 ? 36.128 37.060 13.417 1.00 26.72 ? 527 ARG B N 1 ATOM 8456 C CA . ARG B 1 527 ? 36.197 36.544 14.790 1.00 26.60 ? 527 ARG B CA 1 ATOM 8457 C C . ARG B 1 527 ? 36.039 35.027 14.877 1.00 25.74 ? 527 ARG B C 1 ATOM 8458 O O . ARG B 1 527 ? 36.198 34.443 15.954 1.00 26.95 ? 527 ARG B O 1 ATOM 8459 C CB . ARG B 1 527 ? 35.172 37.235 15.687 1.00 27.65 ? 527 ARG B CB 1 ATOM 8460 C CG . ARG B 1 527 ? 35.530 38.662 16.004 1.00 29.79 ? 527 ARG B CG 1 ATOM 8461 C CD . ARG B 1 527 ? 34.451 39.346 16.806 1.00 32.80 ? 527 ARG B CD 1 ATOM 8462 N NE . ARG B 1 527 ? 34.581 40.798 16.723 1.00 33.58 ? 527 ARG B NE 1 ATOM 8463 C CZ . ARG B 1 527 ? 34.253 41.652 17.688 1.00 34.81 ? 527 ARG B CZ 1 ATOM 8464 N NH1 . ARG B 1 527 ? 33.764 41.220 18.846 1.00 34.46 ? 527 ARG B NH1 1 ATOM 8465 N NH2 . ARG B 1 527 ? 34.409 42.950 17.484 1.00 34.83 ? 527 ARG B NH2 1 ATOM 8466 N N . ILE B 1 528 ? 35.712 34.397 13.745 1.00 24.76 ? 528 ILE B N 1 ATOM 8467 C CA . ILE B 1 528 ? 35.558 32.943 13.675 1.00 22.48 ? 528 ILE B CA 1 ATOM 8468 C C . ILE B 1 528 ? 36.949 32.324 13.492 1.00 22.13 ? 528 ILE B C 1 ATOM 8469 O O . ILE B 1 528 ? 37.629 32.584 12.492 1.00 20.81 ? 528 ILE B O 1 ATOM 8470 C CB . ILE B 1 528 ? 34.597 32.511 12.511 1.00 22.52 ? 528 ILE B CB 1 ATOM 8471 C CG1 . ILE B 1 528 ? 33.168 32.978 12.814 1.00 21.67 ? 528 ILE B CG1 1 ATOM 8472 C CG2 . ILE B 1 528 ? 34.598 30.970 12.328 1.00 21.64 ? 528 ILE B CG2 1 ATOM 8473 C CD1 . ILE B 1 528 ? 32.207 32.901 11.635 1.00 20.80 ? 528 ILE B CD1 1 ATOM 8474 N N . SER B 1 529 ? 37.354 31.519 14.475 1.00 21.20 ? 529 SER B N 1 ATOM 8475 C CA . SER B 1 529 ? 38.649 30.832 14.476 1.00 21.94 ? 529 SER B CA 1 ATOM 8476 C C . SER B 1 529 ? 38.699 29.743 13.404 1.00 22.95 ? 529 SER B C 1 ATOM 8477 O O . SER B 1 529 ? 37.651 29.268 12.946 1.00 21.65 ? 529 SER B O 1 ATOM 8478 C CB . SER B 1 529 ? 38.909 30.198 15.847 1.00 21.88 ? 529 SER B CB 1 ATOM 8479 O OG . SER B 1 529 ? 37.980 29.154 16.122 1.00 19.90 ? 529 SER B OG 1 ATOM 8480 N N . GLN B 1 530 ? 39.914 29.335 13.034 1.00 22.79 ? 530 GLN B N 1 ATOM 8481 C CA . GLN B 1 530 ? 40.125 28.293 12.025 1.00 24.02 ? 530 GLN B CA 1 ATOM 8482 C C . GLN B 1 530 ? 39.567 26.947 12.508 1.00 21.65 ? 530 GLN B C 1 ATOM 8483 O O . GLN B 1 530 ? 38.986 26.205 11.722 1.00 20.02 ? 530 GLN B O 1 ATOM 8484 C CB . GLN B 1 530 ? 41.616 28.172 11.675 1.00 25.64 ? 530 GLN B CB 1 ATOM 8485 C CG . GLN B 1 530 ? 41.922 27.456 10.345 1.00 30.50 ? 530 GLN B CG 1 ATOM 8486 C CD . GLN B 1 530 ? 41.373 28.185 9.119 1.00 32.54 ? 530 GLN B CD 1 ATOM 8487 O OE1 . GLN B 1 530 ? 41.697 29.349 8.872 1.00 34.84 ? 530 GLN B OE1 1 ATOM 8488 N NE2 . GLN B 1 530 ? 40.536 27.497 8.348 1.00 32.82 ? 530 GLN B NE2 1 ATOM 8489 N N . GLU B 1 531 ? 39.676 26.695 13.817 1.00 21.12 ? 531 GLU B N 1 ATOM 8490 C CA . GLU B 1 531 ? 39.174 25.470 14.450 1.00 20.97 ? 531 GLU B CA 1 ATOM 8491 C C . GLU B 1 531 ? 37.641 25.393 14.387 1.00 19.80 ? 531 GLU B C 1 ATOM 8492 O O . GLU B 1 531 ? 37.085 24.329 14.125 1.00 16.73 ? 531 GLU B O 1 ATOM 8493 C CB . GLU B 1 531 ? 39.629 25.382 15.914 1.00 23.49 ? 531 GLU B CB 1 ATOM 8494 C CG . GLU B 1 531 ? 41.131 25.129 16.134 1.00 28.31 ? 531 GLU B CG 1 ATOM 8495 C CD . GLU B 1 531 ? 42.006 26.393 16.124 1.00 31.46 ? 531 GLU B CD 1 ATOM 8496 O OE1 . GLU B 1 531 ? 43.236 26.250 16.298 1.00 33.55 ? 531 GLU B OE1 1 ATOM 8497 O OE2 . GLU B 1 531 ? 41.491 27.521 15.955 1.00 32.03 ? 531 GLU B OE2 1 ATOM 8498 N N . ASP B 1 532 ? 36.978 26.531 14.609 1.00 17.69 ? 532 ASP B N 1 ATOM 8499 C CA . ASP B 1 532 ? 35.516 26.610 14.566 1.00 17.19 ? 532 ASP B CA 1 ATOM 8500 C C . ASP B 1 532 ? 34.989 26.518 13.140 1.00 15.84 ? 532 ASP B C 1 ATOM 8501 O O . ASP B 1 532 ? 33.945 25.924 12.911 1.00 14.18 ? 532 ASP B O 1 ATOM 8502 C CB . ASP B 1 532 ? 35.013 27.896 15.230 1.00 17.56 ? 532 ASP B CB 1 ATOM 8503 C CG . ASP B 1 532 ? 34.906 27.780 16.745 1.00 18.87 ? 532 ASP B CG 1 ATOM 8504 O OD1 . ASP B 1 532 ? 35.173 26.692 17.304 1.00 18.85 ? 532 ASP B OD1 1 ATOM 8505 O OD2 . ASP B 1 532 ? 34.544 28.790 17.384 1.00 18.24 ? 532 ASP B OD2 1 ATOM 8506 N N . GLU B 1 533 ? 35.744 27.071 12.190 1.00 17.06 ? 533 GLU B N 1 ATOM 8507 C CA . GLU B 1 533 ? 35.378 27.044 10.772 1.00 17.60 ? 533 GLU B CA 1 ATOM 8508 C C . GLU B 1 533 ? 35.543 25.635 10.197 1.00 17.38 ? 533 GLU B C 1 ATOM 8509 O O . GLU B 1 533 ? 34.638 25.140 9.524 1.00 17.74 ? 533 GLU B O 1 ATOM 8510 C CB . GLU B 1 533 ? 36.222 28.051 9.977 1.00 19.63 ? 533 GLU B CB 1 ATOM 8511 C CG . GLU B 1 533 ? 36.025 28.006 8.450 1.00 20.47 ? 533 GLU B CG 1 ATOM 8512 C CD . GLU B 1 533 ? 36.701 29.147 7.705 1.00 21.86 ? 533 GLU B CD 1 ATOM 8513 O OE1 . GLU B 1 533 ? 37.605 29.804 8.268 1.00 23.65 ? 533 GLU B OE1 1 ATOM 8514 O OE2 . GLU B 1 533 ? 36.313 29.386 6.542 1.00 22.70 ? 533 GLU B OE2 1 ATOM 8515 N N . ASP B 1 534 ? 36.684 24.998 10.486 1.00 17.56 ? 534 ASP B N 1 ATOM 8516 C CA . ASP B 1 534 ? 36.977 23.645 10.002 1.00 17.89 ? 534 ASP B CA 1 ATOM 8517 C C . ASP B 1 534 ? 35.997 22.621 10.556 1.00 16.67 ? 534 ASP B C 1 ATOM 8518 O O . ASP B 1 534 ? 35.498 21.777 9.813 1.00 18.01 ? 534 ASP B O 1 ATOM 8519 C CB . ASP B 1 534 ? 38.411 23.212 10.352 1.00 18.23 ? 534 ASP B CB 1 ATOM 8520 C CG . ASP B 1 534 ? 39.475 23.975 9.573 1.00 19.39 ? 534 ASP B CG 1 ATOM 8521 O OD1 . ASP B 1 534 ? 39.158 24.610 8.546 1.00 20.07 ? 534 ASP B OD1 1 ATOM 8522 O OD2 . ASP B 1 534 ? 40.648 23.943 10.002 1.00 19.81 ? 534 ASP B OD2 1 ATOM 8523 N N . ASP B 1 535 ? 35.680 22.741 11.846 1.00 15.42 ? 535 ASP B N 1 ATOM 8524 C CA . ASP B 1 535 ? 34.756 21.818 12.499 1.00 14.52 ? 535 ASP B CA 1 ATOM 8525 C C . ASP B 1 535 ? 33.314 22.028 12.027 1.00 13.64 ? 535 ASP B C 1 ATOM 8526 O O . ASP B 1 535 ? 32.561 21.066 11.891 1.00 15.36 ? 535 ASP B O 1 ATOM 8527 C CB . ASP B 1 535 ? 34.861 21.920 14.020 1.00 15.03 ? 535 ASP B CB 1 ATOM 8528 C CG . ASP B 1 535 ? 34.501 20.621 14.712 1.00 18.18 ? 535 ASP B CG 1 ATOM 8529 O OD1 . ASP B 1 535 ? 35.060 19.569 14.333 1.00 16.55 ? 535 ASP B OD1 1 ATOM 8530 O OD2 . ASP B 1 535 ? 33.657 20.651 15.627 1.00 20.66 ? 535 ASP B OD2 1 ATOM 8531 N N . PHE B 1 536 ? 32.970 23.282 11.727 1.00 13.74 ? 536 PHE B N 1 ATOM 8532 C CA . PHE B 1 536 ? 31.646 23.655 11.221 1.00 14.06 ? 536 PHE B CA 1 ATOM 8533 C C . PHE B 1 536 ? 31.455 22.972 9.860 1.00 13.44 ? 536 PHE B C 1 ATOM 8534 O O . PHE B 1 536 ? 30.412 22.370 9.605 1.00 13.35 ? 536 PHE B O 1 ATOM 8535 C CB . PHE B 1 536 ? 31.544 25.193 11.077 1.00 12.30 ? 536 PHE B CB 1 ATOM 8536 C CG . PHE B 1 536 ? 30.344 25.664 10.289 1.00 14.18 ? 536 PHE B CG 1 ATOM 8537 C CD1 . PHE B 1 536 ? 29.094 25.796 10.909 1.00 13.12 ? 536 PHE B CD1 1 ATOM 8538 C CD2 . PHE B 1 536 ? 30.446 25.899 8.899 1.00 14.06 ? 536 PHE B CD2 1 ATOM 8539 C CE1 . PHE B 1 536 ? 27.950 26.145 10.152 1.00 13.28 ? 536 PHE B CE1 1 ATOM 8540 C CE2 . PHE B 1 536 ? 29.319 26.241 8.140 1.00 14.15 ? 536 PHE B CE2 1 ATOM 8541 C CZ . PHE B 1 536 ? 28.062 26.364 8.771 1.00 14.14 ? 536 PHE B CZ 1 ATOM 8542 N N . ASN B 1 537 ? 32.472 23.099 9.002 1.00 13.00 ? 537 ASN B N 1 ATOM 8543 C CA . ASN B 1 537 ? 32.467 22.513 7.663 1.00 14.75 ? 537 ASN B CA 1 ATOM 8544 C C . ASN B 1 537 ? 32.472 20.989 7.704 1.00 15.38 ? 537 ASN B C 1 ATOM 8545 O O . ASN B 1 537 ? 31.818 20.354 6.880 1.00 15.23 ? 537 ASN B O 1 ATOM 8546 C CB . ASN B 1 537 ? 33.652 23.021 6.831 1.00 14.67 ? 537 ASN B CB 1 ATOM 8547 C CG . ASN B 1 537 ? 33.505 24.479 6.417 1.00 14.19 ? 537 ASN B CG 1 ATOM 8548 O OD1 . ASN B 1 537 ? 32.416 24.937 6.080 1.00 15.43 ? 537 ASN B OD1 1 ATOM 8549 N ND2 . ASN B 1 537 ? 34.613 25.209 6.428 1.00 14.50 ? 537 ASN B ND2 1 ATOM 8550 N N . ARG B 1 538 ? 33.150 20.423 8.709 1.00 15.93 ? 538 ARG B N 1 ATOM 8551 C CA . ARG B 1 538 ? 33.242 18.970 8.903 1.00 14.75 ? 538 ARG B CA 1 ATOM 8552 C C . ARG B 1 538 ? 31.863 18.379 9.215 1.00 13.81 ? 538 ARG B C 1 ATOM 8553 O O . ARG B 1 538 ? 31.418 17.453 8.536 1.00 11.78 ? 538 ARG B O 1 ATOM 8554 C CB . ARG B 1 538 ? 34.224 18.638 10.038 1.00 15.03 ? 538 ARG B CB 1 ATOM 8555 C CG . ARG B 1 538 ? 34.381 17.146 10.328 1.00 16.85 ? 538 ARG B CG 1 ATOM 8556 C CD . ARG B 1 538 ? 35.109 16.875 11.643 1.00 15.18 ? 538 ARG B CD 1 ATOM 8557 N NE . ARG B 1 538 ? 34.387 17.310 12.840 1.00 12.56 ? 538 ARG B NE 1 ATOM 8558 C CZ . ARG B 1 538 ? 33.457 16.607 13.490 1.00 12.82 ? 538 ARG B CZ 1 ATOM 8559 N NH1 . ARG B 1 538 ? 33.076 15.402 13.071 1.00 8.69 ? 538 ARG B NH1 1 ATOM 8560 N NH2 . ARG B 1 538 ? 32.969 17.079 14.628 1.00 10.20 ? 538 ARG B NH2 1 ATOM 8561 N N . VAL B 1 539 ? 31.190 18.952 10.218 1.00 13.42 ? 539 VAL B N 1 ATOM 8562 C CA . VAL B 1 539 ? 29.856 18.518 10.643 1.00 11.85 ? 539 VAL B CA 1 ATOM 8563 C C . VAL B 1 539 ? 28.851 18.743 9.508 1.00 10.82 ? 539 VAL B C 1 ATOM 8564 O O . VAL B 1 539 ? 27.992 17.902 9.280 1.00 11.89 ? 539 VAL B O 1 ATOM 8565 C CB . VAL B 1 539 ? 29.399 19.246 11.944 1.00 13.28 ? 539 VAL B CB 1 ATOM 8566 C CG1 . VAL B 1 539 ? 28.019 18.758 12.397 1.00 12.64 ? 539 VAL B CG1 1 ATOM 8567 C CG2 . VAL B 1 539 ? 30.404 18.992 13.061 1.00 14.61 ? 539 VAL B CG2 1 ATOM 8568 N N . CYS B 1 540 ? 29.010 19.846 8.770 1.00 11.86 ? 540 CYS B N 1 ATOM 8569 C CA . CYS B 1 540 ? 28.131 20.149 7.638 1.00 12.76 ? 540 CYS B CA 1 ATOM 8570 C C . CYS B 1 540 ? 28.297 19.180 6.473 1.00 13.18 ? 540 CYS B C 1 ATOM 8571 O O . CYS B 1 540 ? 27.303 18.766 5.877 1.00 13.06 ? 540 CYS B O 1 ATOM 8572 C CB . CYS B 1 540 ? 28.271 21.603 7.184 1.00 11.39 ? 540 CYS B CB 1 ATOM 8573 S SG . CYS B 1 540 ? 27.366 22.781 8.249 1.00 13.15 ? 540 CYS B SG 1 ATOM 8574 N N . ASP B 1 541 ? 29.541 18.772 6.205 1.00 14.06 ? 541 ASP B N 1 ATOM 8575 C CA . ASP B 1 541 ? 29.839 17.804 5.142 1.00 15.08 ? 541 ASP B CA 1 ATOM 8576 C C . ASP B 1 541 ? 29.243 16.444 5.504 1.00 14.76 ? 541 ASP B C 1 ATOM 8577 O O . ASP B 1 541 ? 28.618 15.792 4.665 1.00 15.50 ? 541 ASP B O 1 ATOM 8578 C CB . ASP B 1 541 ? 31.350 17.660 4.923 1.00 19.21 ? 541 ASP B CB 1 ATOM 8579 C CG . ASP B 1 541 ? 31.949 18.816 4.136 1.00 21.51 ? 541 ASP B CG 1 ATOM 8580 O OD1 . ASP B 1 541 ? 31.238 19.438 3.316 1.00 25.95 ? 541 ASP B OD1 1 ATOM 8581 O OD2 . ASP B 1 541 ? 33.145 19.099 4.338 1.00 24.92 ? 541 ASP B OD2 1 ATOM 8582 N N . GLU B 1 542 ? 29.373 16.073 6.781 1.00 13.97 ? 542 GLU B N 1 ATOM 8583 C CA . GLU B 1 542 ? 28.849 14.809 7.308 1.00 13.17 ? 542 GLU B CA 1 ATOM 8584 C C . GLU B 1 542 ? 27.319 14.808 7.316 1.00 13.06 ? 542 GLU B C 1 ATOM 8585 O O . GLU B 1 542 ? 26.694 13.789 7.003 1.00 12.46 ? 542 GLU B O 1 ATOM 8586 C CB . GLU B 1 542 ? 29.373 14.560 8.724 1.00 14.63 ? 542 GLU B CB 1 ATOM 8587 C CG . GLU B 1 542 ? 30.862 14.236 8.814 1.00 13.85 ? 542 GLU B CG 1 ATOM 8588 C CD . GLU B 1 542 ? 31.360 14.115 10.248 1.00 15.80 ? 542 GLU B CD 1 ATOM 8589 O OE1 . GLU B 1 542 ? 30.556 13.802 11.154 1.00 16.69 ? 542 GLU B OE1 1 ATOM 8590 O OE2 . GLU B 1 542 ? 32.570 14.320 10.471 1.00 13.72 ? 542 GLU B OE2 1 ATOM 8591 N N . TRP B 1 543 ? 26.723 15.961 7.634 1.00 11.47 ? 543 TRP B N 1 ATOM 8592 C CA . TRP B 1 543 ? 25.267 16.088 7.652 1.00 11.87 ? 543 TRP B CA 1 ATOM 8593 C C . TRP B 1 543 ? 24.694 16.024 6.239 1.00 12.07 ? 543 TRP B C 1 ATOM 8594 O O . TRP B 1 543 ? 23.696 15.334 6.006 1.00 12.49 ? 543 TRP B O 1 ATOM 8595 C CB . TRP B 1 543 ? 24.809 17.387 8.346 1.00 13.10 ? 543 TRP B CB 1 ATOM 8596 C CG . TRP B 1 543 ? 23.297 17.609 8.290 1.00 12.40 ? 543 TRP B CG 1 ATOM 8597 C CD1 . TRP B 1 543 ? 22.631 18.525 7.518 1.00 14.61 ? 543 TRP B CD1 1 ATOM 8598 C CD2 . TRP B 1 543 ? 22.286 16.841 8.958 1.00 14.12 ? 543 TRP B CD2 1 ATOM 8599 N NE1 . TRP B 1 543 ? 21.272 18.368 7.649 1.00 13.27 ? 543 TRP B NE1 1 ATOM 8600 C CE2 . TRP B 1 543 ? 21.027 17.345 8.527 1.00 13.81 ? 543 TRP B CE2 1 ATOM 8601 C CE3 . TRP B 1 543 ? 22.315 15.768 9.876 1.00 13.57 ? 543 TRP B CE3 1 ATOM 8602 C CZ2 . TRP B 1 543 ? 19.802 16.814 8.985 1.00 12.88 ? 543 TRP B CZ2 1 ATOM 8603 C CZ3 . TRP B 1 543 ? 21.092 15.233 10.332 1.00 13.98 ? 543 TRP B CZ3 1 ATOM 8604 C CH2 . TRP B 1 543 ? 19.851 15.762 9.883 1.00 14.56 ? 543 TRP B CH2 1 ATOM 8605 N N . ARG B 1 544 ? 25.315 16.767 5.324 1.00 14.53 ? 544 ARG B N 1 ATOM 8606 C CA . ARG B 1 544 ? 24.888 16.814 3.925 1.00 17.41 ? 544 ARG B CA 1 ATOM 8607 C C . ARG B 1 544 ? 25.023 15.475 3.213 1.00 18.30 ? 544 ARG B C 1 ATOM 8608 O O . ARG B 1 544 ? 24.283 15.197 2.273 1.00 19.88 ? 544 ARG B O 1 ATOM 8609 C CB . ARG B 1 544 ? 25.630 17.908 3.164 1.00 19.01 ? 544 ARG B CB 1 ATOM 8610 C CG . ARG B 1 544 ? 25.066 19.297 3.415 1.00 22.13 ? 544 ARG B CG 1 ATOM 8611 C CD . ARG B 1 544 ? 25.698 20.324 2.490 1.00 24.43 ? 544 ARG B CD 1 ATOM 8612 N NE . ARG B 1 544 ? 27.113 20.533 2.783 1.00 25.84 ? 544 ARG B NE 1 ATOM 8613 C CZ . ARG B 1 544 ? 27.630 21.675 3.231 1.00 29.07 ? 544 ARG B CZ 1 ATOM 8614 N NH1 . ARG B 1 544 ? 26.852 22.733 3.443 1.00 27.95 ? 544 ARG B NH1 1 ATOM 8615 N NH2 . ARG B 1 544 ? 28.932 21.757 3.477 1.00 29.19 ? 544 ARG B NH2 1 ATOM 8616 N N . ALA B 1 545 ? 25.946 14.642 3.697 1.00 18.91 ? 545 ALA B N 1 ATOM 8617 C CA . ALA B 1 545 ? 26.164 13.303 3.156 1.00 18.90 ? 545 ALA B CA 1 ATOM 8618 C C . ALA B 1 545 ? 25.108 12.369 3.760 1.00 18.77 ? 545 ALA B C 1 ATOM 8619 O O . ALA B 1 545 ? 24.670 11.414 3.114 1.00 19.08 ? 545 ALA B O 1 ATOM 8620 C CB . ALA B 1 545 ? 27.567 12.809 3.494 1.00 17.90 ? 545 ALA B CB 1 ATOM 8621 N N . TYR B 1 546 ? 24.677 12.675 4.985 1.00 17.09 ? 546 TYR B N 1 ATOM 8622 C CA . TYR B 1 546 ? 23.660 11.874 5.653 1.00 15.10 ? 546 TYR B CA 1 ATOM 8623 C C . TYR B 1 546 ? 22.235 12.170 5.177 1.00 14.93 ? 546 TYR B C 1 ATOM 8624 O O . TYR B 1 546 ? 21.473 11.234 4.960 1.00 13.57 ? 546 TYR B O 1 ATOM 8625 C CB . TYR B 1 546 ? 23.721 12.003 7.199 1.00 13.74 ? 546 TYR B CB 1 ATOM 8626 C CG . TYR B 1 546 ? 22.532 11.342 7.888 1.00 14.20 ? 546 TYR B CG 1 ATOM 8627 C CD1 . TYR B 1 546 ? 22.431 9.934 7.956 1.00 13.92 ? 546 TYR B CD1 1 ATOM 8628 C CD2 . TYR B 1 546 ? 21.405 12.111 8.281 1.00 12.38 ? 546 TYR B CD2 1 ATOM 8629 C CE1 . TYR B 1 546 ? 21.229 9.304 8.375 1.00 14.44 ? 546 TYR B CE1 1 ATOM 8630 C CE2 . TYR B 1 546 ? 20.205 11.495 8.691 1.00 14.24 ? 546 TYR B CE2 1 ATOM 8631 C CZ . TYR B 1 546 ? 20.127 10.094 8.733 1.00 14.51 ? 546 TYR B CZ 1 ATOM 8632 O OH . TYR B 1 546 ? 18.962 9.497 9.130 1.00 15.56 ? 546 TYR B OH 1 ATOM 8633 N N . TRP B 1 547 ? 21.861 13.450 5.102 1.00 15.56 ? 547 TRP B N 1 ATOM 8634 C CA . TRP B 1 547 ? 20.491 13.848 4.741 1.00 18.58 ? 547 TRP B CA 1 ATOM 8635 C C . TRP B 1 547 ? 19.713 13.117 3.621 1.00 19.42 ? 547 TRP B C 1 ATOM 8636 O O . TRP B 1 547 ? 18.558 12.753 3.856 1.00 20.35 ? 547 TRP B O 1 ATOM 8637 C CB . TRP B 1 547 ? 20.337 15.391 4.668 1.00 17.54 ? 547 TRP B CB 1 ATOM 8638 C CG . TRP B 1 547 ? 18.898 15.883 4.490 1.00 19.08 ? 547 TRP B CG 1 ATOM 8639 C CD1 . TRP B 1 547 ? 18.378 16.501 3.382 1.00 20.55 ? 547 TRP B CD1 1 ATOM 8640 C CD2 . TRP B 1 547 ? 17.802 15.740 5.416 1.00 20.40 ? 547 TRP B CD2 1 ATOM 8641 N NE1 . TRP B 1 547 ? 17.035 16.741 3.552 1.00 20.67 ? 547 TRP B NE1 1 ATOM 8642 C CE2 . TRP B 1 547 ? 16.651 16.289 4.787 1.00 20.76 ? 547 TRP B CE2 1 ATOM 8643 C CE3 . TRP B 1 547 ? 17.675 15.199 6.716 1.00 19.99 ? 547 TRP B CE3 1 ATOM 8644 C CZ2 . TRP B 1 547 ? 15.380 16.314 5.413 1.00 20.93 ? 547 TRP B CZ2 1 ATOM 8645 C CZ3 . TRP B 1 547 ? 16.408 15.222 7.345 1.00 20.92 ? 547 TRP B CZ3 1 ATOM 8646 C CH2 . TRP B 1 547 ? 15.277 15.778 6.684 1.00 20.69 ? 547 TRP B CH2 1 ATOM 8647 N N . PRO B 1 548 ? 20.318 12.870 2.425 1.00 21.68 ? 548 PRO B N 1 ATOM 8648 C CA . PRO B 1 548 ? 19.546 12.164 1.386 1.00 22.56 ? 548 PRO B CA 1 ATOM 8649 C C . PRO B 1 548 ? 19.132 10.726 1.747 1.00 22.49 ? 548 PRO B C 1 ATOM 8650 O O . PRO B 1 548 ? 18.212 10.176 1.141 1.00 22.43 ? 548 PRO B O 1 ATOM 8651 C CB . PRO B 1 548 ? 20.496 12.182 0.188 1.00 22.98 ? 548 PRO B CB 1 ATOM 8652 C CG . PRO B 1 548 ? 21.250 13.453 0.379 1.00 23.59 ? 548 PRO B CG 1 ATOM 8653 C CD . PRO B 1 548 ? 21.582 13.366 1.843 1.00 21.36 ? 548 PRO B CD 1 ATOM 8654 N N . THR B 1 549 ? 19.784 10.156 2.766 1.00 23.67 ? 549 THR B N 1 ATOM 8655 C CA . THR B 1 549 ? 19.508 8.787 3.229 1.00 22.76 ? 549 THR B CA 1 ATOM 8656 C C . THR B 1 549 ? 18.444 8.716 4.336 1.00 23.57 ? 549 THR B C 1 ATOM 8657 O O . THR B 1 549 ? 18.022 7.617 4.716 1.00 22.70 ? 549 THR B O 1 ATOM 8658 C CB . THR B 1 549 ? 20.799 8.058 3.736 1.00 23.55 ? 549 THR B CB 1 ATOM 8659 O OG1 . THR B 1 549 ? 21.208 8.603 4.999 1.00 22.78 ? 549 THR B OG1 1 ATOM 8660 C CG2 . THR B 1 549 ? 21.949 8.194 2.734 1.00 21.78 ? 549 THR B CG2 1 ATOM 8661 N N . ASN B 1 550 ? 18.040 9.879 4.861 1.00 22.90 ? 550 ASN B N 1 ATOM 8662 C CA . ASN B 1 550 ? 17.030 9.967 5.928 1.00 22.42 ? 550 ASN B CA 1 ATOM 8663 C C . ASN B 1 550 ? 15.643 9.579 5.386 1.00 22.19 ? 550 ASN B C 1 ATOM 8664 O O . ASN B 1 550 ? 15.192 10.136 4.379 1.00 20.04 ? 550 ASN B O 1 ATOM 8665 C CB . ASN B 1 550 ? 16.996 11.387 6.520 1.00 20.89 ? 550 ASN B CB 1 ATOM 8666 C CG . ASN B 1 550 ? 16.276 11.455 7.866 1.00 21.67 ? 550 ASN B CG 1 ATOM 8667 O OD1 . ASN B 1 550 ? 16.669 10.803 8.827 1.00 21.34 ? 550 ASN B OD1 1 ATOM 8668 N ND2 . ASN B 1 550 ? 15.223 12.251 7.933 1.00 21.50 ? 550 ASN B ND2 1 ATOM 8669 N N . PRO B 1 551 ? 14.965 8.604 6.036 1.00 22.92 ? 551 PRO B N 1 ATOM 8670 C CA . PRO B 1 551 ? 13.635 8.163 5.591 1.00 22.41 ? 551 PRO B CA 1 ATOM 8671 C C . PRO B 1 551 ? 12.472 9.106 5.915 1.00 22.88 ? 551 PRO B C 1 ATOM 8672 O O . PRO B 1 551 ? 11.367 8.934 5.392 1.00 22.31 ? 551 PRO B O 1 ATOM 8673 C CB . PRO B 1 551 ? 13.478 6.813 6.294 1.00 22.75 ? 551 PRO B CB 1 ATOM 8674 C CG . PRO B 1 551 ? 14.208 7.016 7.575 1.00 22.61 ? 551 PRO B CG 1 ATOM 8675 C CD . PRO B 1 551 ? 15.459 7.727 7.122 1.00 23.52 ? 551 PRO B CD 1 ATOM 8676 N N . TYR B 1 552 ? 12.735 10.100 6.763 1.00 22.50 ? 552 TYR B N 1 ATOM 8677 C CA . TYR B 1 552 ? 11.713 11.057 7.189 1.00 23.11 ? 552 TYR B CA 1 ATOM 8678 C C . TYR B 1 552 ? 11.951 12.483 6.675 1.00 22.59 ? 552 TYR B C 1 ATOM 8679 O O . TYR B 1 552 ? 13.098 12.924 6.572 1.00 22.13 ? 552 TYR B O 1 ATOM 8680 C CB . TYR B 1 552 ? 11.619 11.077 8.726 1.00 23.49 ? 552 TYR B CB 1 ATOM 8681 C CG . TYR B 1 552 ? 11.306 9.743 9.388 1.00 25.00 ? 552 TYR B CG 1 ATOM 8682 C CD1 . TYR B 1 552 ? 10.204 8.955 8.977 1.00 27.18 ? 552 TYR B CD1 1 ATOM 8683 C CD2 . TYR B 1 552 ? 12.105 9.268 10.445 1.00 25.05 ? 552 TYR B CD2 1 ATOM 8684 C CE1 . TYR B 1 552 ? 9.908 7.711 9.616 1.00 28.32 ? 552 TYR B CE1 1 ATOM 8685 C CE2 . TYR B 1 552 ? 11.822 8.034 11.091 1.00 27.71 ? 552 TYR B CE2 1 ATOM 8686 C CZ . TYR B 1 552 ? 10.727 7.265 10.672 1.00 28.35 ? 552 TYR B CZ 1 ATOM 8687 O OH . TYR B 1 552 ? 10.460 6.074 11.304 1.00 30.32 ? 552 TYR B OH 1 ATOM 8688 N N . PRO B 1 553 ? 10.870 13.208 6.301 1.00 22.86 ? 553 PRO B N 1 ATOM 8689 C CA . PRO B 1 553 ? 11.067 14.579 5.815 1.00 23.01 ? 553 PRO B CA 1 ATOM 8690 C C . PRO B 1 553 ? 11.109 15.608 6.957 1.00 21.79 ? 553 PRO B C 1 ATOM 8691 O O . PRO B 1 553 ? 10.868 15.275 8.123 1.00 20.13 ? 553 PRO B O 1 ATOM 8692 C CB . PRO B 1 553 ? 9.850 14.792 4.916 1.00 23.71 ? 553 PRO B CB 1 ATOM 8693 C CG . PRO B 1 553 ? 8.771 14.026 5.631 1.00 23.93 ? 553 PRO B CG 1 ATOM 8694 C CD . PRO B 1 553 ? 9.484 12.753 6.037 1.00 24.06 ? 553 PRO B CD 1 ATOM 8695 N N . LYS B 1 554 ? 11.466 16.839 6.608 1.00 22.47 ? 554 LYS B N 1 ATOM 8696 C CA . LYS B 1 554 ? 11.507 17.957 7.548 1.00 23.10 ? 554 LYS B CA 1 ATOM 8697 C C . LYS B 1 554 ? 10.085 18.529 7.475 1.00 22.43 ? 554 LYS B C 1 ATOM 8698 O O . LYS B 1 554 ? 9.682 19.057 6.438 1.00 22.65 ? 554 LYS B O 1 ATOM 8699 C CB . LYS B 1 554 ? 12.543 18.980 7.075 1.00 24.28 ? 554 LYS B CB 1 ATOM 8700 C CG . LYS B 1 554 ? 12.712 20.211 7.943 1.00 26.40 ? 554 LYS B CG 1 ATOM 8701 C CD . LYS B 1 554 ? 13.868 21.034 7.410 1.00 28.16 ? 554 LYS B CD 1 ATOM 8702 C CE . LYS B 1 554 ? 14.065 22.313 8.185 1.00 27.19 ? 554 LYS B CE 1 ATOM 8703 N NZ . LYS B 1 554 ? 13.006 23.300 7.886 1.00 29.38 ? 554 LYS B NZ 1 ATOM 8704 N N . ILE B 1 555 ? 9.317 18.343 8.549 1.00 23.30 ? 555 ILE B N 1 ATOM 8705 C CA . ILE B 1 555 ? 7.925 18.802 8.607 1.00 24.15 ? 555 ILE B CA 1 ATOM 8706 C C . ILE B 1 555 ? 7.682 20.196 9.197 1.00 21.87 ? 555 ILE B C 1 ATOM 8707 O O . ILE B 1 555 ? 6.562 20.710 9.118 1.00 21.93 ? 555 ILE B O 1 ATOM 8708 C CB . ILE B 1 555 ? 7.002 17.768 9.334 1.00 25.78 ? 555 ILE B CB 1 ATOM 8709 C CG1 . ILE B 1 555 ? 7.526 17.455 10.745 1.00 28.78 ? 555 ILE B CG1 1 ATOM 8710 C CG2 . ILE B 1 555 ? 6.862 16.501 8.483 1.00 28.02 ? 555 ILE B CG2 1 ATOM 8711 C CD1 . ILE B 1 555 ? 6.507 16.781 11.665 1.00 31.11 ? 555 ILE B CD1 1 ATOM 8712 N N . ASP B 1 556 ? 8.723 20.804 9.766 1.00 18.83 ? 556 ASP B N 1 ATOM 8713 C CA . ASP B 1 556 ? 8.596 22.129 10.375 1.00 15.18 ? 556 ASP B CA 1 ATOM 8714 C C . ASP B 1 556 ? 9.744 23.103 10.060 1.00 14.19 ? 556 ASP B C 1 ATOM 8715 O O . ASP B 1 556 ? 10.499 22.889 9.109 1.00 15.34 ? 556 ASP B O 1 ATOM 8716 C CB . ASP B 1 556 ? 8.354 21.983 11.897 1.00 14.81 ? 556 ASP B CB 1 ATOM 8717 C CG . ASP B 1 556 ? 9.552 21.401 12.668 1.00 16.44 ? 556 ASP B CG 1 ATOM 8718 O OD1 . ASP B 1 556 ? 10.640 21.169 12.091 1.00 16.28 ? 556 ASP B OD1 1 ATOM 8719 O OD2 . ASP B 1 556 ? 9.398 21.195 13.891 1.00 16.15 ? 556 ASP B OD2 1 ATOM 8720 N N . SER B 1 557 ? 9.888 24.141 10.891 1.00 11.79 ? 557 SER B N 1 ATOM 8721 C CA . SER B 1 557 ? 10.925 25.169 10.743 1.00 11.52 ? 557 SER B CA 1 ATOM 8722 C C . SER B 1 557 ? 12.344 24.637 10.904 1.00 10.84 ? 557 SER B C 1 ATOM 8723 O O . SER B 1 557 ? 13.294 25.184 10.339 1.00 10.92 ? 557 SER B O 1 ATOM 8724 C CB . SER B 1 557 ? 10.721 26.275 11.779 1.00 11.02 ? 557 SER B CB 1 ATOM 8725 O OG . SER B 1 557 ? 10.970 25.794 13.089 1.00 8.36 ? 557 SER B OG 1 ATOM 8726 N N . GLY B 1 558 ? 12.459 23.592 11.719 1.00 10.95 ? 558 GLY B N 1 ATOM 8727 C CA . GLY B 1 558 ? 13.738 22.980 12.010 1.00 11.40 ? 558 GLY B CA 1 ATOM 8728 C C . GLY B 1 558 ? 14.308 23.460 13.326 1.00 10.34 ? 558 GLY B C 1 ATOM 8729 O O . GLY B 1 558 ? 15.369 23.002 13.753 1.00 11.28 ? 558 GLY B O 1 ATOM 8730 N N . LEU B 1 559 ? 13.580 24.368 13.979 1.00 10.98 ? 559 LEU B N 1 ATOM 8731 C CA . LEU B 1 559 ? 13.994 24.958 15.253 1.00 10.76 ? 559 LEU B CA 1 ATOM 8732 C C . LEU B 1 559 ? 13.093 24.596 16.430 1.00 11.91 ? 559 LEU B C 1 ATOM 8733 O O . LEU B 1 559 ? 13.562 24.704 17.585 1.00 12.16 ? 559 LEU B O 1 ATOM 8734 C CB . LEU B 1 559 ? 14.077 26.480 15.123 1.00 10.13 ? 559 LEU B CB 1 ATOM 8735 C CG . LEU B 1 559 ? 15.008 27.080 14.067 1.00 10.11 ? 559 LEU B CG 1 ATOM 8736 C CD1 . LEU B 1 559 ? 14.767 28.571 13.995 1.00 8.37 ? 559 LEU B CD1 1 ATOM 8737 C CD2 . LEU B 1 559 ? 16.479 26.759 14.361 1.00 8.43 ? 559 LEU B CD2 1 ATOM 8738 O OXT . LEU B 1 559 ? 11.938 24.187 16.191 1.00 11.79 ? 559 LEU B OXT 1 HETATM 8739 C C1 . NAG C 2 . ? -43.935 53.768 23.935 1.00 26.26 ? 700 NAG A C1 1 HETATM 8740 C C2 . NAG C 2 . ? -45.210 54.543 23.565 1.00 28.22 ? 700 NAG A C2 1 HETATM 8741 C C3 . NAG C 2 . ? -44.860 55.934 23.016 1.00 29.58 ? 700 NAG A C3 1 HETATM 8742 C C4 . NAG C 2 . ? -43.889 56.669 23.948 1.00 30.07 ? 700 NAG A C4 1 HETATM 8743 C C5 . NAG C 2 . ? -42.675 55.777 24.227 1.00 30.27 ? 700 NAG A C5 1 HETATM 8744 C C6 . NAG C 2 . ? -41.660 56.396 25.173 1.00 28.49 ? 700 NAG A C6 1 HETATM 8745 C C7 . NAG C 2 . ? -46.951 52.995 22.895 1.00 27.27 ? 700 NAG A C7 1 HETATM 8746 C C8 . NAG C 2 . ? -47.962 52.657 21.813 1.00 27.17 ? 700 NAG A C8 1 HETATM 8747 N N2 . NAG C 2 . ? -45.948 53.801 22.556 1.00 27.37 ? 700 NAG A N2 1 HETATM 8748 O O3 . NAG C 2 . ? -46.046 56.700 22.863 1.00 29.85 ? 700 NAG A O3 1 HETATM 8749 O O4 . NAG C 2 . ? -43.467 57.877 23.331 1.00 33.87 ? 700 NAG A O4 1 HETATM 8750 O O5 . NAG C 2 . ? -43.109 54.537 24.817 1.00 27.76 ? 700 NAG A O5 1 HETATM 8751 O O6 . NAG C 2 . ? -42.160 56.457 26.502 1.00 31.37 ? 700 NAG A O6 1 HETATM 8752 O O7 . NAG C 2 . ? -47.090 52.535 24.029 1.00 29.22 ? 700 NAG A O7 1 HETATM 8753 C C1 . NAG D 2 . ? -31.028 46.905 14.296 1.00 14.26 ? 710 NAG A C1 1 HETATM 8754 C C2 . NAG D 2 . ? -30.370 46.758 12.935 1.00 15.07 ? 710 NAG A C2 1 HETATM 8755 C C3 . NAG D 2 . ? -28.862 46.887 13.108 1.00 15.17 ? 710 NAG A C3 1 HETATM 8756 C C4 . NAG D 2 . ? -28.508 48.178 13.869 1.00 16.11 ? 710 NAG A C4 1 HETATM 8757 C C5 . NAG D 2 . ? -29.345 48.327 15.147 1.00 15.48 ? 710 NAG A C5 1 HETATM 8758 C C6 . NAG D 2 . ? -29.170 49.675 15.820 1.00 13.60 ? 710 NAG A C6 1 HETATM 8759 C C7 . NAG D 2 . ? -31.478 45.361 11.306 1.00 12.05 ? 710 NAG A C7 1 HETATM 8760 C C8 . NAG D 2 . ? -31.512 44.014 10.600 1.00 10.39 ? 710 NAG A C8 1 HETATM 8761 N N2 . NAG D 2 . ? -30.694 45.459 12.375 1.00 12.41 ? 710 NAG A N2 1 HETATM 8762 O O3 . NAG D 2 . ? -28.249 46.900 11.828 1.00 18.65 ? 710 NAG A O3 1 HETATM 8763 O O4 . NAG D 2 . ? -27.122 48.156 14.238 1.00 17.80 ? 710 NAG A O4 1 HETATM 8764 O O5 . NAG D 2 . ? -30.741 48.186 14.845 1.00 13.92 ? 710 NAG A O5 1 HETATM 8765 O O6 . NAG D 2 . ? -29.222 50.735 14.879 1.00 11.13 ? 710 NAG A O6 1 HETATM 8766 O O7 . NAG D 2 . ? -32.173 46.292 10.891 1.00 13.14 ? 710 NAG A O7 1 HETATM 8767 C C1 . NAG E 2 . ? -26.276 48.940 13.477 1.00 20.16 ? 711 NAG A C1 1 HETATM 8768 C C2 . NAG E 2 . ? -24.977 49.188 14.250 1.00 21.35 ? 711 NAG A C2 1 HETATM 8769 C C3 . NAG E 2 . ? -23.989 49.947 13.364 1.00 26.07 ? 711 NAG A C3 1 HETATM 8770 C C4 . NAG E 2 . ? -23.797 49.235 12.016 1.00 29.33 ? 711 NAG A C4 1 HETATM 8771 C C5 . NAG E 2 . ? -25.156 48.976 11.358 1.00 27.40 ? 711 NAG A C5 1 HETATM 8772 C C6 . NAG E 2 . ? -25.038 48.163 10.081 1.00 27.27 ? 711 NAG A C6 1 HETATM 8773 C C7 . NAG E 2 . ? -25.360 49.404 16.644 1.00 19.08 ? 711 NAG A C7 1 HETATM 8774 C C8 . NAG E 2 . ? -25.729 50.334 17.789 1.00 16.62 ? 711 NAG A C8 1 HETATM 8775 N N2 . NAG E 2 . ? -25.257 49.971 15.441 1.00 18.78 ? 711 NAG A N2 1 HETATM 8776 O O3 . NAG E 2 . ? -22.741 50.060 14.032 1.00 24.89 ? 711 NAG A O3 1 HETATM 8777 O O4 . NAG E 2 . ? -23.007 50.060 11.142 1.00 37.99 ? 711 NAG A O4 1 HETATM 8778 O O5 . NAG E 2 . ? -26.009 48.238 12.254 1.00 23.13 ? 711 NAG A O5 1 HETATM 8779 O O6 . NAG E 2 . ? -24.515 46.867 10.340 1.00 30.41 ? 711 NAG A O6 1 HETATM 8780 O O7 . NAG E 2 . ? -25.180 48.197 16.860 1.00 15.99 ? 711 NAG A O7 1 HETATM 8781 C C1 . BMA F 3 . ? -21.767 49.574 10.769 1.00 47.30 ? 712 BMA A C1 1 HETATM 8782 C C2 . BMA F 3 . ? -21.255 50.375 9.567 1.00 51.27 ? 712 BMA A C2 1 HETATM 8783 C C3 . BMA F 3 . ? -19.816 49.977 9.218 1.00 56.19 ? 712 BMA A C3 1 HETATM 8784 C C4 . BMA F 3 . ? -18.919 50.041 10.467 1.00 56.92 ? 712 BMA A C4 1 HETATM 8785 C C5 . BMA F 3 . ? -19.551 49.254 11.626 1.00 56.31 ? 712 BMA A C5 1 HETATM 8786 C C6 . BMA F 3 . ? -18.773 49.371 12.933 1.00 59.03 ? 712 BMA A C6 1 HETATM 8787 O O2 . BMA F 3 . ? -21.317 51.768 9.850 1.00 49.17 ? 712 BMA A O2 1 HETATM 8788 O O3 . BMA F 3 . ? -19.304 50.874 8.207 1.00 61.62 ? 712 BMA A O3 1 HETATM 8789 O O4 . BMA F 3 . ? -17.638 49.504 10.167 1.00 58.18 ? 712 BMA A O4 1 HETATM 8790 O O5 . BMA F 3 . ? -20.885 49.738 11.886 1.00 51.57 ? 712 BMA A O5 1 HETATM 8791 O O6 . BMA F 3 . ? -18.941 50.692 13.496 1.00 63.15 ? 712 BMA A O6 1 HETATM 8792 C C1 . MAN G 4 . ? -19.403 50.446 6.873 1.00 66.13 ? 713 MAN A C1 1 HETATM 8793 C C2 . MAN G 4 . ? -18.773 51.492 5.943 1.00 67.74 ? 713 MAN A C2 1 HETATM 8794 C C3 . MAN G 4 . ? -19.638 52.760 5.913 1.00 69.19 ? 713 MAN A C3 1 HETATM 8795 C C4 . MAN G 4 . ? -21.087 52.420 5.541 1.00 69.41 ? 713 MAN A C4 1 HETATM 8796 C C5 . MAN G 4 . ? -21.629 51.328 6.474 1.00 69.11 ? 713 MAN A C5 1 HETATM 8797 C C6 . MAN G 4 . ? -23.011 50.837 6.072 1.00 69.95 ? 713 MAN A C6 1 HETATM 8798 O O2 . MAN G 4 . ? -18.649 50.956 4.633 1.00 67.92 ? 713 MAN A O2 1 HETATM 8799 O O3 . MAN G 4 . ? -19.106 53.690 4.978 1.00 69.67 ? 713 MAN A O3 1 HETATM 8800 O O4 . MAN G 4 . ? -21.894 53.585 5.650 1.00 70.25 ? 713 MAN A O4 1 HETATM 8801 O O5 . MAN G 4 . ? -20.750 50.179 6.471 1.00 67.78 ? 713 MAN A O5 1 HETATM 8802 O O6 . MAN G 4 . ? -23.018 50.329 4.744 1.00 70.14 ? 713 MAN A O6 1 HETATM 8803 C C1 . MAN H 4 . ? -19.042 50.679 14.896 1.00 64.76 ? 714 MAN A C1 1 HETATM 8804 C C2 . MAN H 4 . ? -19.507 52.053 15.403 1.00 65.41 ? 714 MAN A C2 1 HETATM 8805 C C3 . MAN H 4 . ? -18.404 53.098 15.194 1.00 66.15 ? 714 MAN A C3 1 HETATM 8806 C C4 . MAN H 4 . ? -17.095 52.629 15.839 1.00 66.76 ? 714 MAN A C4 1 HETATM 8807 C C5 . MAN H 4 . ? -16.722 51.229 15.325 1.00 66.91 ? 714 MAN A C5 1 HETATM 8808 C C6 . MAN H 4 . ? -15.501 50.638 16.014 1.00 66.80 ? 714 MAN A C6 1 HETATM 8809 O O2 . MAN H 4 . ? -19.833 51.970 16.785 1.00 65.06 ? 714 MAN A O2 1 HETATM 8810 O O3 . MAN H 4 . ? -18.802 54.341 15.759 1.00 65.37 ? 714 MAN A O3 1 HETATM 8811 O O4 . MAN H 4 . ? -16.055 53.547 15.527 1.00 68.29 ? 714 MAN A O4 1 HETATM 8812 O O5 . MAN H 4 . ? -17.818 50.309 15.534 1.00 65.99 ? 714 MAN A O5 1 HETATM 8813 O O6 . MAN H 4 . ? -15.696 50.519 17.417 1.00 66.59 ? 714 MAN A O6 1 HETATM 8814 C C1 . NAG I 2 . ? -29.129 46.367 52.201 1.00 28.30 ? 720 NAG A C1 1 HETATM 8815 C C2 . NAG I 2 . ? -28.283 47.501 52.768 1.00 29.28 ? 720 NAG A C2 1 HETATM 8816 C C3 . NAG I 2 . ? -28.442 47.534 54.285 1.00 31.33 ? 720 NAG A C3 1 HETATM 8817 C C4 . NAG I 2 . ? -29.933 47.583 54.677 1.00 32.64 ? 720 NAG A C4 1 HETATM 8818 C C5 . NAG I 2 . ? -30.749 46.510 53.938 1.00 32.46 ? 720 NAG A C5 1 HETATM 8819 C C6 . NAG I 2 . ? -32.247 46.663 54.133 1.00 32.27 ? 720 NAG A C6 1 HETATM 8820 C C7 . NAG I 2 . ? -26.285 48.117 51.541 1.00 27.48 ? 720 NAG A C7 1 HETATM 8821 C C8 . NAG I 2 . ? -24.781 47.969 51.394 1.00 26.47 ? 720 NAG A C8 1 HETATM 8822 N N2 . NAG I 2 . ? -26.887 47.308 52.412 1.00 27.60 ? 720 NAG A N2 1 HETATM 8823 O O3 . NAG I 2 . ? -27.769 48.679 54.792 1.00 31.52 ? 720 NAG A O3 1 HETATM 8824 O O4 . NAG I 2 . ? -30.068 47.370 56.094 1.00 36.73 ? 720 NAG A O4 1 HETATM 8825 O O5 . NAG I 2 . ? -30.503 46.576 52.522 1.00 29.39 ? 720 NAG A O5 1 HETATM 8826 O O6 . NAG I 2 . ? -32.730 47.853 53.521 1.00 34.23 ? 720 NAG A O6 1 HETATM 8827 O O7 . NAG I 2 . ? -26.885 48.958 50.869 1.00 27.31 ? 720 NAG A O7 1 HETATM 8828 C C1 . NAG J 2 . ? -30.259 48.501 56.865 1.00 38.13 ? 721 NAG A C1 1 HETATM 8829 C C2 . NAG J 2 . ? -31.009 48.136 58.147 1.00 38.85 ? 721 NAG A C2 1 HETATM 8830 C C3 . NAG J 2 . ? -31.149 49.382 59.037 1.00 42.17 ? 721 NAG A C3 1 HETATM 8831 C C4 . NAG J 2 . ? -29.787 50.078 59.243 1.00 44.72 ? 721 NAG A C4 1 HETATM 8832 C C5 . NAG J 2 . ? -29.064 50.278 57.901 1.00 42.75 ? 721 NAG A C5 1 HETATM 8833 C C6 . NAG J 2 . ? -27.647 50.800 58.061 1.00 41.45 ? 721 NAG A C6 1 HETATM 8834 C C7 . NAG J 2 . ? -32.616 46.327 58.029 1.00 32.73 ? 721 NAG A C7 1 HETATM 8835 C C8 . NAG J 2 . ? -34.080 45.933 57.927 1.00 33.30 ? 721 NAG A C8 1 HETATM 8836 N N2 . NAG J 2 . ? -32.320 47.607 57.813 1.00 34.73 ? 721 NAG A N2 1 HETATM 8837 O O3 . NAG J 2 . ? -31.685 49.000 60.297 1.00 42.08 ? 721 NAG A O3 1 HETATM 8838 O O4 . NAG J 2 . ? -29.983 51.375 59.855 1.00 51.61 ? 721 NAG A O4 1 HETATM 8839 O O5 . NAG J 2 . ? -28.973 49.030 57.190 1.00 39.87 ? 721 NAG A O5 1 HETATM 8840 O O6 . NAG J 2 . ? -27.076 51.129 56.803 1.00 39.03 ? 721 NAG A O6 1 HETATM 8841 O O7 . NAG J 2 . ? -31.771 45.472 58.304 1.00 30.43 ? 721 NAG A O7 1 HETATM 8842 C C1 . BMA K 3 . ? -29.901 51.517 61.239 1.00 57.44 ? 722 BMA A C1 1 HETATM 8843 C C2 . BMA K 3 . ? -28.819 50.596 61.834 1.00 59.74 ? 722 BMA A C2 1 HETATM 8844 C C3 . BMA K 3 . ? -28.702 50.859 63.337 1.00 61.28 ? 722 BMA A C3 1 HETATM 8845 C C4 . BMA K 3 . ? -28.404 52.339 63.583 1.00 61.26 ? 722 BMA A C4 1 HETATM 8846 C C5 . BMA K 3 . ? -29.491 53.199 62.920 1.00 61.08 ? 722 BMA A C5 1 HETATM 8847 C C6 . BMA K 3 . ? -29.217 54.691 63.036 1.00 61.36 ? 722 BMA A C6 1 HETATM 8848 O O2 . BMA K 3 . ? -27.570 50.838 61.197 1.00 62.07 ? 722 BMA A O2 1 HETATM 8849 O O3 . BMA K 3 . ? -27.670 50.056 63.895 1.00 62.35 ? 722 BMA A O3 1 HETATM 8850 O O4 . BMA K 3 . ? -28.364 52.595 64.980 1.00 62.13 ? 722 BMA A O4 1 HETATM 8851 O O5 . BMA K 3 . ? -29.583 52.894 61.508 1.00 58.93 ? 722 BMA A O5 1 HETATM 8852 O O6 . BMA K 3 . ? -28.049 55.067 62.317 1.00 61.85 ? 722 BMA A O6 1 HETATM 8853 C C1 . NAG L 2 . ? -16.870 37.626 46.229 1.00 14.60 ? 730 NAG A C1 1 HETATM 8854 C C2 . NAG L 2 . ? -15.385 37.216 46.093 1.00 16.03 ? 730 NAG A C2 1 HETATM 8855 C C3 . NAG L 2 . ? -14.480 38.197 46.848 1.00 16.80 ? 730 NAG A C3 1 HETATM 8856 C C4 . NAG L 2 . ? -14.806 39.651 46.483 1.00 16.42 ? 730 NAG A C4 1 HETATM 8857 C C5 . NAG L 2 . ? -16.295 39.906 46.680 1.00 17.06 ? 730 NAG A C5 1 HETATM 8858 C C6 . NAG L 2 . ? -16.733 41.316 46.319 1.00 14.07 ? 730 NAG A C6 1 HETATM 8859 C C7 . NAG L 2 . ? -15.047 34.810 45.851 1.00 16.54 ? 730 NAG A C7 1 HETATM 8860 C C8 . NAG L 2 . ? -14.890 33.469 46.553 1.00 16.98 ? 730 NAG A C8 1 HETATM 8861 N N2 . NAG L 2 . ? -15.181 35.880 46.637 1.00 15.23 ? 730 NAG A N2 1 HETATM 8862 O O3 . NAG L 2 . ? -13.122 37.920 46.537 1.00 14.46 ? 730 NAG A O3 1 HETATM 8863 O O4 . NAG L 2 . ? -14.062 40.548 47.327 1.00 19.68 ? 730 NAG A O4 1 HETATM 8864 O O5 . NAG L 2 . ? -17.055 39.000 45.866 1.00 16.28 ? 730 NAG A O5 1 HETATM 8865 O O6 . NAG L 2 . ? -16.411 41.642 44.977 1.00 15.53 ? 730 NAG A O6 1 HETATM 8866 O O7 . NAG L 2 . ? -15.097 34.853 44.620 1.00 16.97 ? 730 NAG A O7 1 HETATM 8867 C C1 . NAG M 2 . ? -12.967 41.165 46.747 1.00 20.40 ? 731 NAG A C1 1 HETATM 8868 C C2 . NAG M 2 . ? -12.703 42.496 47.442 1.00 23.00 ? 731 NAG A C2 1 HETATM 8869 C C3 . NAG M 2 . ? -11.461 43.148 46.827 1.00 25.52 ? 731 NAG A C3 1 HETATM 8870 C C4 . NAG M 2 . ? -10.265 42.186 46.806 1.00 28.22 ? 731 NAG A C4 1 HETATM 8871 C C5 . NAG M 2 . ? -10.650 40.803 46.253 1.00 26.09 ? 731 NAG A C5 1 HETATM 8872 C C6 . NAG M 2 . ? -9.546 39.787 46.504 1.00 26.32 ? 731 NAG A C6 1 HETATM 8873 C C7 . NAG M 2 . ? -14.432 43.954 48.319 1.00 21.64 ? 731 NAG A C7 1 HETATM 8874 C C8 . NAG M 2 . ? -15.263 45.196 48.031 1.00 19.88 ? 731 NAG A C8 1 HETATM 8875 N N2 . NAG M 2 . ? -13.860 43.359 47.272 1.00 21.75 ? 731 NAG A N2 1 HETATM 8876 O O3 . NAG M 2 . ? -11.114 44.304 47.575 1.00 25.76 ? 731 NAG A O3 1 HETATM 8877 O O4 . NAG M 2 . ? -9.232 42.746 45.972 1.00 36.31 ? 731 NAG A O4 1 HETATM 8878 O O5 . NAG M 2 . ? -11.837 40.302 46.907 1.00 23.00 ? 731 NAG A O5 1 HETATM 8879 O O6 . NAG M 2 . ? -9.936 38.483 46.105 1.00 28.31 ? 731 NAG A O6 1 HETATM 8880 O O7 . NAG M 2 . ? -14.323 43.543 49.477 1.00 21.21 ? 731 NAG A O7 1 HETATM 8881 C C1 . BMA N 3 . ? -7.927 42.641 46.424 1.00 41.90 ? 732 BMA A C1 1 HETATM 8882 C C2 . BMA N 3 . ? -6.964 42.678 45.227 1.00 44.37 ? 732 BMA A C2 1 HETATM 8883 C C3 . BMA N 3 . ? -5.508 42.682 45.720 1.00 46.66 ? 732 BMA A C3 1 HETATM 8884 C C4 . BMA N 3 . ? -5.286 43.800 46.748 1.00 46.88 ? 732 BMA A C4 1 HETATM 8885 C C5 . BMA N 3 . ? -6.338 43.711 47.865 1.00 46.39 ? 732 BMA A C5 1 HETATM 8886 C C6 . BMA N 3 . ? -6.242 44.857 48.854 1.00 46.92 ? 732 BMA A C6 1 HETATM 8887 O O2 . BMA N 3 . ? -7.219 43.830 44.431 1.00 45.08 ? 732 BMA A O2 1 HETATM 8888 O O3 . BMA N 3 . ? -4.621 42.853 44.621 1.00 47.54 ? 732 BMA A O3 1 HETATM 8889 O O4 . BMA N 3 . ? -3.983 43.678 47.304 1.00 48.21 ? 732 BMA A O4 1 HETATM 8890 O O5 . BMA N 3 . ? -7.670 43.746 47.304 1.00 44.00 ? 732 BMA A O5 1 HETATM 8891 O O6 . BMA N 3 . ? -5.792 44.404 50.123 1.00 47.68 ? 732 BMA A O6 1 HETATM 8892 C C1 . NAG O 2 . ? -27.347 14.987 8.215 1.00 22.99 ? 740 NAG A C1 1 HETATM 8893 C C2 . NAG O 2 . ? -28.716 14.376 8.529 1.00 22.84 ? 740 NAG A C2 1 HETATM 8894 C C3 . NAG O 2 . ? -28.819 12.971 7.924 1.00 26.25 ? 740 NAG A C3 1 HETATM 8895 C C4 . NAG O 2 . ? -28.338 12.909 6.461 1.00 29.68 ? 740 NAG A C4 1 HETATM 8896 C C5 . NAG O 2 . ? -27.032 13.692 6.245 1.00 29.45 ? 740 NAG A C5 1 HETATM 8897 C C6 . NAG O 2 . ? -26.709 13.862 4.772 1.00 30.24 ? 740 NAG A C6 1 HETATM 8898 C C7 . NAG O 2 . ? -29.806 15.028 10.595 1.00 21.76 ? 740 NAG A C7 1 HETATM 8899 C C8 . NAG O 2 . ? -30.358 14.474 11.897 1.00 21.97 ? 740 NAG A C8 1 HETATM 8900 N N2 . NAG O 2 . ? -28.887 14.295 9.968 1.00 22.39 ? 740 NAG A N2 1 HETATM 8901 O O3 . NAG O 2 . ? -30.170 12.541 7.984 1.00 24.97 ? 740 NAG A O3 1 HETATM 8902 O O4 . NAG O 2 . ? -28.102 11.532 6.111 1.00 36.33 ? 740 NAG A O4 1 HETATM 8903 O O5 . NAG O 2 . ? -27.134 15.015 6.804 1.00 24.75 ? 740 NAG A O5 1 HETATM 8904 O O6 . NAG O 2 . ? -25.312 14.009 4.567 1.00 34.87 ? 740 NAG A O6 1 HETATM 8905 O O7 . NAG O 2 . ? -30.197 16.117 10.180 1.00 21.09 ? 740 NAG A O7 1 HETATM 8906 C C1 . NAG P 2 . ? -28.994 10.907 5.254 1.00 40.72 ? 741 NAG A C1 1 HETATM 8907 C C2 . NAG P 2 . ? -28.377 9.588 4.780 1.00 43.87 ? 741 NAG A C2 1 HETATM 8908 C C3 . NAG P 2 . ? -29.376 8.806 3.926 1.00 45.47 ? 741 NAG A C3 1 HETATM 8909 C C4 . NAG P 2 . ? -30.684 8.615 4.696 1.00 45.98 ? 741 NAG A C4 1 HETATM 8910 C C5 . NAG P 2 . ? -31.208 9.970 5.199 1.00 45.64 ? 741 NAG A C5 1 HETATM 8911 C C6 . NAG P 2 . ? -32.428 9.815 6.087 1.00 46.24 ? 741 NAG A C6 1 HETATM 8912 C C7 . NAG P 2 . ? -25.978 9.614 4.587 1.00 46.90 ? 741 NAG A C7 1 HETATM 8913 C C8 . NAG P 2 . ? -25.091 10.823 4.836 1.00 47.94 ? 741 NAG A C8 1 HETATM 8914 N N2 . NAG P 2 . ? -27.162 9.834 4.025 1.00 45.19 ? 741 NAG A N2 1 HETATM 8915 O O3 . NAG P 2 . ? -28.827 7.537 3.597 1.00 44.61 ? 741 NAG A O3 1 HETATM 8916 O O4 . NAG P 2 . ? -31.652 8.006 3.849 1.00 47.88 ? 741 NAG A O4 1 HETATM 8917 O O5 . NAG P 2 . ? -30.199 10.641 5.990 1.00 42.32 ? 741 NAG A O5 1 HETATM 8918 O O6 . NAG P 2 . ? -33.272 10.954 6.002 1.00 49.06 ? 741 NAG A O6 1 HETATM 8919 O O7 . NAG P 2 . ? -25.601 8.495 4.936 1.00 48.99 ? 741 NAG A O7 1 HETATM 8920 C C1 . NAG Q 2 . ? -42.103 26.896 -2.495 1.00 34.99 ? 750 NAG A C1 1 HETATM 8921 C C2 . NAG Q 2 . ? -42.548 27.926 -3.533 1.00 37.92 ? 750 NAG A C2 1 HETATM 8922 C C3 . NAG Q 2 . ? -41.375 28.282 -4.443 1.00 38.89 ? 750 NAG A C3 1 HETATM 8923 C C4 . NAG Q 2 . ? -40.180 28.742 -3.605 1.00 38.88 ? 750 NAG A C4 1 HETATM 8924 C C5 . NAG Q 2 . ? -39.849 27.707 -2.515 1.00 37.78 ? 750 NAG A C5 1 HETATM 8925 C C6 . NAG Q 2 . ? -38.779 28.195 -1.557 1.00 37.71 ? 750 NAG A C6 1 HETATM 8926 C C7 . NAG Q 2 . ? -44.810 28.052 -4.339 1.00 41.91 ? 750 NAG A C7 1 HETATM 8927 C C8 . NAG Q 2 . ? -45.051 29.008 -5.497 1.00 43.37 ? 750 NAG A C8 1 HETATM 8928 N N2 . NAG Q 2 . ? -43.650 27.404 -4.316 1.00 39.78 ? 750 NAG A N2 1 HETATM 8929 O O3 . NAG Q 2 . ? -41.762 29.321 -5.330 1.00 40.12 ? 750 NAG A O3 1 HETATM 8930 O O4 . NAG Q 2 . ? -39.053 28.929 -4.451 1.00 40.70 ? 750 NAG A O4 1 HETATM 8931 O O5 . NAG Q 2 . ? -41.020 27.424 -1.718 1.00 35.68 ? 750 NAG A O5 1 HETATM 8932 O O6 . NAG Q 2 . ? -39.167 29.411 -0.934 1.00 37.28 ? 750 NAG A O6 1 HETATM 8933 O O7 . NAG Q 2 . ? -45.668 27.915 -3.468 1.00 44.17 ? 750 NAG A O7 1 HETATM 8934 C C1 . NAG R 2 . ? -34.517 42.511 42.564 1.00 30.18 ? 760 NAG A C1 1 HETATM 8935 C C2 . NAG R 2 . ? -34.884 42.263 44.035 1.00 31.15 ? 760 NAG A C2 1 HETATM 8936 C C3 . NAG R 2 . ? -36.302 42.774 44.337 1.00 33.32 ? 760 NAG A C3 1 HETATM 8937 C C4 . NAG R 2 . ? -36.459 44.230 43.875 1.00 32.85 ? 760 NAG A C4 1 HETATM 8938 C C5 . NAG R 2 . ? -36.065 44.332 42.396 1.00 33.99 ? 760 NAG A C5 1 HETATM 8939 C C6 . NAG R 2 . ? -36.179 45.736 41.819 1.00 33.80 ? 760 NAG A C6 1 HETATM 8940 C C7 . NAG R 2 . ? -34.048 40.389 45.319 1.00 31.94 ? 760 NAG A C7 1 HETATM 8941 C C8 . NAG R 2 . ? -34.127 38.902 45.622 1.00 31.30 ? 760 NAG A C8 1 HETATM 8942 N N2 . NAG R 2 . ? -34.803 40.841 44.321 1.00 32.08 ? 760 NAG A N2 1 HETATM 8943 O O3 . NAG R 2 . ? -36.559 42.681 45.732 1.00 33.63 ? 760 NAG A O3 1 HETATM 8944 O O4 . NAG R 2 . ? -37.804 44.657 44.056 1.00 32.71 ? 760 NAG A O4 1 HETATM 8945 O O5 . NAG R 2 . ? -34.695 43.895 42.224 1.00 30.47 ? 760 NAG A O5 1 HETATM 8946 O O6 . NAG R 2 . ? -35.160 46.591 42.321 1.00 36.59 ? 760 NAG A O6 1 HETATM 8947 O O7 . NAG R 2 . ? -33.309 41.113 45.990 1.00 33.89 ? 760 NAG A O7 1 HETATM 8948 C C1 . NDG S 5 . ? -18.212 32.285 57.966 1.00 43.13 ? 770 NDG A C1 1 HETATM 8949 C C2 . NDG S 5 . ? -17.041 31.447 58.578 1.00 45.45 ? 770 NDG A C2 1 HETATM 8950 C C3 . NDG S 5 . ? -16.956 31.470 60.120 1.00 46.56 ? 770 NDG A C3 1 HETATM 8951 C C4 . NDG S 5 . ? -17.286 32.850 60.646 1.00 47.25 ? 770 NDG A C4 1 HETATM 8952 C C5 . NDG S 5 . ? -18.693 33.152 60.171 1.00 46.76 ? 770 NDG A C5 1 HETATM 8953 C C6 . NDG S 5 . ? -19.338 34.353 60.836 1.00 46.91 ? 770 NDG A C6 1 HETATM 8954 C C7 . NDG S 5 . ? -16.065 29.318 57.964 1.00 47.20 ? 770 NDG A C7 1 HETATM 8955 C C8 . NDG S 5 . ? -15.833 28.203 58.970 1.00 47.55 ? 770 NDG A C8 1 HETATM 8956 O O . NDG S 5 . ? -18.648 33.411 58.761 1.00 45.41 ? 770 NDG A O 1 HETATM 8957 O O3 . NDG S 5 . ? -15.647 31.108 60.536 1.00 47.36 ? 770 NDG A O3 1 HETATM 8958 O O4 . NDG S 5 . ? -17.201 32.878 62.062 1.00 47.61 ? 770 NDG A O4 1 HETATM 8959 O O6 . NDG S 5 . ? -20.267 33.943 61.828 1.00 48.43 ? 770 NDG A O6 1 HETATM 8960 O O7 . NDG S 5 . ? -15.260 29.500 57.049 1.00 49.57 ? 770 NDG A O7 1 HETATM 8961 N N2 . NDG S 5 . ? -17.151 30.067 58.134 1.00 45.79 ? 770 NDG A N2 1 HETATM 8962 CU CU . CU T 6 . ? -22.116 27.863 21.133 1.00 15.84 ? 601 CU A CU 1 HETATM 8963 CU CU . CU U 6 . ? -34.189 30.112 20.866 1.00 18.57 ? 602 CU A CU 1 HETATM 8964 CU CU . CU V 6 . ? -33.701 31.679 25.218 1.00 15.93 ? 603 CU A CU 1 HETATM 8965 CU CU . CU W 6 . ? -36.226 28.916 23.958 1.00 15.61 ? 604 CU A CU 1 HETATM 8966 CL CL . CL X 7 . ? -38.033 27.484 24.868 1.00 22.72 ? 610 CL A CL 1 HETATM 8967 S S . SO4 Y 8 . ? -56.912 22.072 28.667 1.00 62.09 ? 800 SO4 A S 1 HETATM 8968 O O1 . SO4 Y 8 . ? -55.710 21.287 29.001 1.00 62.62 ? 800 SO4 A O1 1 HETATM 8969 O O2 . SO4 Y 8 . ? -56.680 22.841 27.431 1.00 62.10 ? 800 SO4 A O2 1 HETATM 8970 O O3 . SO4 Y 8 . ? -57.219 22.998 29.774 1.00 63.34 ? 800 SO4 A O3 1 HETATM 8971 O O4 . SO4 Y 8 . ? -58.050 21.157 28.469 1.00 63.71 ? 800 SO4 A O4 1 HETATM 8972 S S . SO4 Z 8 . ? -51.797 14.281 20.202 1.00 74.29 ? 801 SO4 A S 1 HETATM 8973 O O1 . SO4 Z 8 . ? -52.064 15.553 20.899 1.00 74.68 ? 801 SO4 A O1 1 HETATM 8974 O O2 . SO4 Z 8 . ? -52.258 14.384 18.812 1.00 74.62 ? 801 SO4 A O2 1 HETATM 8975 O O3 . SO4 Z 8 . ? -52.523 13.184 20.867 1.00 74.96 ? 801 SO4 A O3 1 HETATM 8976 O O4 . SO4 Z 8 . ? -50.349 14.005 20.215 1.00 74.64 ? 801 SO4 A O4 1 HETATM 8977 O O1 . OXY AA 9 . ? -33.435 31.266 22.626 1.00 33.25 ? 620 OXY A O1 1 HETATM 8978 O O2 . OXY AA 9 . ? -34.253 30.519 23.276 1.00 32.02 ? 620 OXY A O2 1 HETATM 8979 C C1 . NAG BA 2 . ? 26.116 5.145 23.837 1.00 30.82 ? 700 NAG B C1 1 HETATM 8980 C C2 . NAG BA 2 . ? 27.374 4.350 23.445 1.00 32.40 ? 700 NAG B C2 1 HETATM 8981 C C3 . NAG BA 2 . ? 27.002 2.954 22.928 1.00 32.96 ? 700 NAG B C3 1 HETATM 8982 C C4 . NAG BA 2 . ? 26.040 2.246 23.888 1.00 33.37 ? 700 NAG B C4 1 HETATM 8983 C C5 . NAG BA 2 . ? 24.838 3.154 24.164 1.00 33.89 ? 700 NAG B C5 1 HETATM 8984 C C6 . NAG BA 2 . ? 23.821 2.552 25.121 1.00 33.54 ? 700 NAG B C6 1 HETATM 8985 C C7 . NAG BA 2 . ? 29.159 5.803 22.689 1.00 32.29 ? 700 NAG B C7 1 HETATM 8986 C C8 . NAG BA 2 . ? 30.252 5.878 21.634 1.00 32.85 ? 700 NAG B C8 1 HETATM 8987 N N2 . NAG BA 2 . ? 28.086 5.069 22.402 1.00 32.15 ? 700 NAG B N2 1 HETATM 8988 O O3 . NAG BA 2 . ? 28.181 2.177 22.770 1.00 33.65 ? 700 NAG B O3 1 HETATM 8989 O O4 . NAG BA 2 . ? 25.599 1.028 23.307 1.00 34.84 ? 700 NAG B O4 1 HETATM 8990 O O5 . NAG BA 2 . ? 25.292 4.396 24.738 1.00 31.76 ? 700 NAG B O5 1 HETATM 8991 O O6 . NAG BA 2 . ? 24.253 2.651 26.471 1.00 35.17 ? 700 NAG B O6 1 HETATM 8992 O O7 . NAG BA 2 . ? 29.299 6.397 23.756 1.00 30.77 ? 700 NAG B O7 1 HETATM 8993 C C1 . NAG CA 2 . ? 13.244 12.117 14.226 1.00 14.69 ? 710 NAG B C1 1 HETATM 8994 C C2 . NAG CA 2 . ? 12.610 12.281 12.853 1.00 15.95 ? 710 NAG B C2 1 HETATM 8995 C C3 . NAG CA 2 . ? 11.094 12.149 12.999 1.00 16.81 ? 710 NAG B C3 1 HETATM 8996 C C4 . NAG CA 2 . ? 10.719 10.861 13.753 1.00 18.32 ? 710 NAG B C4 1 HETATM 8997 C C5 . NAG CA 2 . ? 11.540 10.685 15.040 1.00 16.72 ? 710 NAG B C5 1 HETATM 8998 C C6 . NAG CA 2 . ? 11.354 9.317 15.670 1.00 18.73 ? 710 NAG B C6 1 HETATM 8999 C C7 . NAG CA 2 . ? 13.664 13.711 11.209 1.00 16.54 ? 710 NAG B C7 1 HETATM 9000 C C8 . NAG CA 2 . ? 13.555 15.040 10.478 1.00 14.50 ? 710 NAG B C8 1 HETATM 9001 N N2 . NAG CA 2 . ? 12.949 13.588 12.325 1.00 14.79 ? 710 NAG B N2 1 HETATM 9002 O O3 . NAG CA 2 . ? 10.497 12.132 11.711 1.00 17.85 ? 710 NAG B O3 1 HETATM 9003 O O4 . NAG CA 2 . ? 9.324 10.902 14.100 1.00 23.32 ? 710 NAG B O4 1 HETATM 9004 O O5 . NAG CA 2 . ? 12.941 10.829 14.765 1.00 13.98 ? 710 NAG B O5 1 HETATM 9005 O O6 . NAG CA 2 . ? 11.488 8.277 14.710 1.00 16.84 ? 710 NAG B O6 1 HETATM 9006 O O7 . NAG CA 2 . ? 14.399 12.822 10.769 1.00 15.89 ? 710 NAG B O7 1 HETATM 9007 C C1 . NAG DA 2 . ? 8.477 10.127 13.331 1.00 25.95 ? 711 NAG B C1 1 HETATM 9008 C C2 . NAG DA 2 . ? 7.220 9.802 14.139 1.00 27.93 ? 711 NAG B C2 1 HETATM 9009 C C3 . NAG DA 2 . ? 6.227 9.036 13.266 1.00 31.73 ? 711 NAG B C3 1 HETATM 9010 C C4 . NAG DA 2 . ? 5.951 9.811 11.972 1.00 34.31 ? 711 NAG B C4 1 HETATM 9011 C C5 . NAG DA 2 . ? 7.266 10.159 11.265 1.00 33.26 ? 711 NAG B C5 1 HETATM 9012 C C6 . NAG DA 2 . ? 7.064 11.035 10.038 1.00 32.57 ? 711 NAG B C6 1 HETATM 9013 C C7 . NAG DA 2 . ? 7.461 9.507 16.526 1.00 25.19 ? 711 NAG B C7 1 HETATM 9014 C C8 . NAG DA 2 . ? 7.360 8.502 17.662 1.00 24.75 ? 711 NAG B C8 1 HETATM 9015 N N2 . NAG DA 2 . ? 7.582 9.009 15.299 1.00 25.83 ? 711 NAG B N2 1 HETATM 9016 O O3 . NAG DA 2 . ? 5.016 8.847 13.983 1.00 32.64 ? 711 NAG B O3 1 HETATM 9017 O O4 . NAG DA 2 . ? 5.135 9.017 11.095 1.00 41.43 ? 711 NAG B O4 1 HETATM 9018 O O5 . NAG DA 2 . ? 8.136 10.880 12.161 1.00 28.85 ? 711 NAG B O5 1 HETATM 9019 O O6 . NAG DA 2 . ? 6.524 12.303 10.390 1.00 34.30 ? 711 NAG B O6 1 HETATM 9020 O O7 . NAG DA 2 . ? 7.423 10.718 16.768 1.00 22.82 ? 711 NAG B O7 1 HETATM 9021 C C1 . BMA EA 3 . ? 3.889 9.536 10.791 1.00 48.40 ? 712 BMA B C1 1 HETATM 9022 C C2 . BMA EA 3 . ? 3.332 8.845 9.543 1.00 50.26 ? 712 BMA B C2 1 HETATM 9023 C C3 . BMA EA 3 . ? 1.907 9.340 9.266 1.00 53.02 ? 712 BMA B C3 1 HETATM 9024 C C4 . BMA EA 3 . ? 1.026 9.181 10.518 1.00 54.92 ? 712 BMA B C4 1 HETATM 9025 C C5 . BMA EA 3 . ? 1.704 9.854 11.720 1.00 55.59 ? 712 BMA B C5 1 HETATM 9026 C C6 . BMA EA 3 . ? 0.942 9.681 13.027 1.00 59.06 ? 712 BMA B C6 1 HETATM 9027 O O2 . BMA EA 3 . ? 3.333 7.436 9.732 1.00 49.49 ? 712 BMA B O2 1 HETATM 9028 O O3 . BMA EA 3 . ? 1.349 8.614 8.178 1.00 53.06 ? 712 BMA B O3 1 HETATM 9029 O O4 . BMA EA 3 . ? -0.247 9.771 10.292 1.00 55.47 ? 712 BMA B O4 1 HETATM 9030 O O5 . BMA EA 3 . ? 3.026 9.304 11.914 1.00 51.81 ? 712 BMA B O5 1 HETATM 9031 O O6 . BMA EA 3 . ? 1.061 8.321 13.496 1.00 63.85 ? 712 BMA B O6 1 HETATM 9032 C C1 . MAN FA 4 . ? 1.111 8.246 14.896 1.00 66.01 ? 714 MAN B C1 1 HETATM 9033 C C2 . MAN FA 4 . ? 1.508 6.829 15.330 1.00 67.07 ? 714 MAN B C2 1 HETATM 9034 C C3 . MAN FA 4 . ? 0.375 5.841 15.018 1.00 68.09 ? 714 MAN B C3 1 HETATM 9035 C C4 . MAN FA 4 . ? -0.947 6.318 15.629 1.00 68.62 ? 714 MAN B C4 1 HETATM 9036 C C5 . MAN FA 4 . ? -1.244 7.763 15.198 1.00 68.79 ? 714 MAN B C5 1 HETATM 9037 C C6 . MAN FA 4 . ? -2.467 8.353 15.885 1.00 68.81 ? 714 MAN B C6 1 HETATM 9038 O O2 . MAN FA 4 . ? 1.795 6.817 16.723 1.00 66.65 ? 714 MAN B O2 1 HETATM 9039 O O3 . MAN FA 4 . ? 0.700 4.553 15.526 1.00 67.55 ? 714 MAN B O3 1 HETATM 9040 O O4 . MAN FA 4 . ? -2.001 5.467 15.203 1.00 69.50 ? 714 MAN B O4 1 HETATM 9041 O O5 . MAN FA 4 . ? -0.123 8.622 15.510 1.00 67.67 ? 714 MAN B O5 1 HETATM 9042 O O6 . MAN FA 4 . ? -2.363 8.276 17.302 1.00 68.31 ? 714 MAN B O6 1 HETATM 9043 C C1 . NAG GA 2 . ? 11.217 12.575 52.190 1.00 30.55 ? 720 NAG B C1 1 HETATM 9044 C C2 . NAG GA 2 . ? 10.367 11.452 52.771 1.00 31.58 ? 720 NAG B C2 1 HETATM 9045 C C3 . NAG GA 2 . ? 10.538 11.426 54.290 1.00 33.18 ? 720 NAG B C3 1 HETATM 9046 C C4 . NAG GA 2 . ? 12.033 11.387 54.684 1.00 33.99 ? 720 NAG B C4 1 HETATM 9047 C C5 . NAG GA 2 . ? 12.838 12.456 53.924 1.00 34.48 ? 720 NAG B C5 1 HETATM 9048 C C6 . NAG GA 2 . ? 14.339 12.340 54.125 1.00 34.08 ? 720 NAG B C6 1 HETATM 9049 C C7 . NAG GA 2 . ? 8.337 10.825 51.607 1.00 29.18 ? 720 NAG B C7 1 HETATM 9050 C C8 . NAG GA 2 . ? 6.835 11.001 51.473 1.00 28.69 ? 720 NAG B C8 1 HETATM 9051 N N2 . NAG GA 2 . ? 8.971 11.664 52.425 1.00 30.82 ? 720 NAG B N2 1 HETATM 9052 O O3 . NAG GA 2 . ? 9.868 10.288 54.811 1.00 32.58 ? 720 NAG B O3 1 HETATM 9053 O O4 . NAG GA 2 . ? 12.166 11.635 56.097 1.00 36.41 ? 720 NAG B O4 1 HETATM 9054 O O5 . NAG GA 2 . ? 12.592 12.364 52.509 1.00 31.88 ? 720 NAG B O5 1 HETATM 9055 O O6 . NAG GA 2 . ? 14.828 11.088 53.665 1.00 36.00 ? 720 NAG B O6 1 HETATM 9056 O O7 . NAG GA 2 . ? 8.908 9.932 50.977 1.00 30.23 ? 720 NAG B O7 1 HETATM 9057 C C1 . NAG HA 2 . ? 12.409 10.537 56.904 1.00 37.76 ? 721 NAG B C1 1 HETATM 9058 C C2 . NAG HA 2 . ? 13.138 10.989 58.171 1.00 37.91 ? 721 NAG B C2 1 HETATM 9059 C C3 . NAG HA 2 . ? 13.319 9.798 59.119 1.00 39.49 ? 721 NAG B C3 1 HETATM 9060 C C4 . NAG HA 2 . ? 11.978 9.092 59.372 1.00 40.60 ? 721 NAG B C4 1 HETATM 9061 C C5 . NAG HA 2 . ? 11.279 8.765 58.044 1.00 39.95 ? 721 NAG B C5 1 HETATM 9062 C C6 . NAG HA 2 . ? 9.880 8.207 58.240 1.00 40.75 ? 721 NAG B C6 1 HETATM 9063 C C7 . NAG HA 2 . ? 14.731 12.815 58.124 1.00 36.49 ? 721 NAG B C7 1 HETATM 9064 C C8 . NAG HA 2 . ? 16.201 13.197 58.097 1.00 34.19 ? 721 NAG B C8 1 HETATM 9065 N N2 . NAG HA 2 . ? 14.430 11.553 57.819 1.00 36.47 ? 721 NAG B N2 1 HETATM 9066 O O3 . NAG HA 2 . ? 13.855 10.253 60.353 1.00 39.70 ? 721 NAG B O3 1 HETATM 9067 O O4 . NAG HA 2 . ? 12.199 7.892 60.103 1.00 42.67 ? 721 NAG B O4 1 HETATM 9068 O O5 . NAG HA 2 . ? 11.145 9.959 57.247 1.00 38.42 ? 721 NAG B O5 1 HETATM 9069 O O6 . NAG HA 2 . ? 9.220 8.014 56.995 1.00 39.80 ? 721 NAG B O6 1 HETATM 9070 O O7 . NAG HA 2 . ? 13.883 13.663 58.419 1.00 36.05 ? 721 NAG B O7 1 HETATM 9071 C C1 . NAG IA 2 . ? -0.985 21.368 46.159 1.00 18.30 ? 730 NAG B C1 1 HETATM 9072 C C2 . NAG IA 2 . ? -2.466 21.781 46.071 1.00 18.93 ? 730 NAG B C2 1 HETATM 9073 C C3 . NAG IA 2 . ? -3.361 20.798 46.837 1.00 19.33 ? 730 NAG B C3 1 HETATM 9074 C C4 . NAG IA 2 . ? -3.057 19.344 46.426 1.00 21.60 ? 730 NAG B C4 1 HETATM 9075 C C5 . NAG IA 2 . ? -1.565 19.090 46.612 1.00 20.65 ? 730 NAG B C5 1 HETATM 9076 C C6 . NAG IA 2 . ? -1.133 17.680 46.246 1.00 19.26 ? 730 NAG B C6 1 HETATM 9077 C C7 . NAG IA 2 . ? -2.845 24.176 45.824 1.00 18.33 ? 730 NAG B C7 1 HETATM 9078 C C8 . NAG IA 2 . ? -3.227 25.483 46.507 1.00 17.55 ? 730 NAG B C8 1 HETATM 9079 N N2 . NAG IA 2 . ? -2.642 23.121 46.615 1.00 17.52 ? 730 NAG B N2 1 HETATM 9080 O O3 . NAG IA 2 . ? -4.717 21.106 46.561 1.00 17.98 ? 730 NAG B O3 1 HETATM 9081 O O4 . NAG IA 2 . ? -3.799 18.416 47.242 1.00 24.35 ? 730 NAG B O4 1 HETATM 9082 O O5 . NAG IA 2 . ? -0.816 19.993 45.786 1.00 19.24 ? 730 NAG B O5 1 HETATM 9083 O O6 . NAG IA 2 . ? -1.525 17.340 44.927 1.00 17.82 ? 730 NAG B O6 1 HETATM 9084 O O7 . NAG IA 2 . ? -2.694 24.149 44.599 1.00 18.55 ? 730 NAG B O7 1 HETATM 9085 C C1 . NAG JA 2 . ? -4.930 17.828 46.689 1.00 29.41 ? 731 NAG B C1 1 HETATM 9086 C C2 . NAG JA 2 . ? -5.246 16.532 47.488 1.00 32.10 ? 731 NAG B C2 1 HETATM 9087 C C3 . NAG JA 2 . ? -6.679 16.025 47.263 1.00 35.17 ? 731 NAG B C3 1 HETATM 9088 C C4 . NAG JA 2 . ? -7.567 17.198 47.610 1.00 37.84 ? 731 NAG B C4 1 HETATM 9089 C C5 . NAG JA 2 . ? -7.314 18.276 46.568 1.00 34.14 ? 731 NAG B C5 1 HETATM 9090 C C6 . NAG JA 2 . ? -8.292 19.441 46.650 1.00 31.41 ? 731 NAG B C6 1 HETATM 9091 C C7 . NAG JA 2 . ? -3.480 14.991 48.090 1.00 33.41 ? 731 NAG B C7 1 HETATM 9092 C C8 . NAG JA 2 . ? -2.447 13.973 47.632 1.00 33.60 ? 731 NAG B C8 1 HETATM 9093 N N2 . NAG JA 2 . ? -4.293 15.487 47.157 1.00 32.94 ? 731 NAG B N2 1 HETATM 9094 O O3 . NAG JA 2 . ? -6.941 14.924 48.121 1.00 35.13 ? 731 NAG B O3 1 HETATM 9095 O O4 . NAG JA 2 . ? -8.974 16.887 47.749 1.00 46.22 ? 731 NAG B O4 1 HETATM 9096 O O5 . NAG JA 2 . ? -5.990 18.807 46.784 1.00 28.25 ? 731 NAG B O5 1 HETATM 9097 O O6 . NAG JA 2 . ? -7.775 20.593 46.002 1.00 34.70 ? 731 NAG B O6 1 HETATM 9098 O O7 . NAG JA 2 . ? -3.529 15.321 49.277 1.00 32.67 ? 731 NAG B O7 1 HETATM 9099 C C1 . BMA KA 3 . ? -9.571 15.749 47.233 1.00 51.60 ? 732 BMA B C1 1 HETATM 9100 C C2 . BMA KA 3 . ? -10.922 15.574 47.950 1.00 54.33 ? 732 BMA B C2 1 HETATM 9101 C C3 . BMA KA 3 . ? -11.777 14.489 47.297 1.00 56.37 ? 732 BMA B C3 1 HETATM 9102 C C4 . BMA KA 3 . ? -11.897 14.751 45.793 1.00 56.84 ? 732 BMA B C4 1 HETATM 9103 C C5 . BMA KA 3 . ? -10.491 14.901 45.187 1.00 56.73 ? 732 BMA B C5 1 HETATM 9104 C C6 . BMA KA 3 . ? -10.498 15.221 43.708 1.00 57.41 ? 732 BMA B C6 1 HETATM 9105 O O2 . BMA KA 3 . ? -11.631 16.806 47.942 1.00 55.46 ? 732 BMA B O2 1 HETATM 9106 O O3 . BMA KA 3 . ? -13.068 14.479 47.893 1.00 56.82 ? 732 BMA B O3 1 HETATM 9107 O O4 . BMA KA 3 . ? -12.584 13.671 45.173 1.00 58.71 ? 732 BMA B O4 1 HETATM 9108 O O5 . BMA KA 3 . ? -9.777 15.975 45.833 1.00 54.22 ? 732 BMA B O5 1 HETATM 9109 O O6 . BMA KA 3 . ? -9.174 15.282 43.205 1.00 58.80 ? 732 BMA B O6 1 HETATM 9110 C C1 . NAG LA 2 . ? 9.749 44.108 8.334 1.00 27.46 ? 740 NAG B C1 1 HETATM 9111 C C2 . NAG LA 2 . ? 11.111 44.737 8.615 1.00 27.95 ? 740 NAG B C2 1 HETATM 9112 C C3 . NAG LA 2 . ? 11.162 46.142 8.006 1.00 30.90 ? 740 NAG B C3 1 HETATM 9113 C C4 . NAG LA 2 . ? 10.669 46.181 6.545 1.00 34.02 ? 740 NAG B C4 1 HETATM 9114 C C5 . NAG LA 2 . ? 9.381 45.361 6.349 1.00 33.23 ? 740 NAG B C5 1 HETATM 9115 C C6 . NAG LA 2 . ? 9.016 45.168 4.885 1.00 33.62 ? 740 NAG B C6 1 HETATM 9116 C C7 . NAG LA 2 . ? 12.202 44.040 10.669 1.00 26.44 ? 740 NAG B C7 1 HETATM 9117 C C8 . NAG LA 2 . ? 12.610 44.446 12.073 1.00 23.90 ? 740 NAG B C8 1 HETATM 9118 N N2 . NAG LA 2 . ? 11.321 44.824 10.050 1.00 26.83 ? 740 NAG B N2 1 HETATM 9119 O O3 . NAG LA 2 . ? 12.497 46.620 8.057 1.00 29.78 ? 740 NAG B O3 1 HETATM 9120 O O4 . NAG LA 2 . ? 10.397 47.550 6.182 1.00 39.53 ? 740 NAG B O4 1 HETATM 9121 O O5 . NAG LA 2 . ? 9.524 44.048 6.926 1.00 29.42 ? 740 NAG B O5 1 HETATM 9122 O O6 . NAG LA 2 . ? 10.122 44.681 4.134 1.00 35.52 ? 740 NAG B O6 1 HETATM 9123 O O7 . NAG LA 2 . ? 12.670 43.017 10.168 1.00 26.89 ? 740 NAG B O7 1 HETATM 9124 C C1 . NAG MA 2 . ? 11.229 48.149 5.249 1.00 44.99 ? 741 NAG B C1 1 HETATM 9125 C C2 . NAG MA 2 . ? 10.519 49.374 4.659 1.00 47.25 ? 741 NAG B C2 1 HETATM 9126 C C3 . NAG MA 2 . ? 11.464 50.147 3.732 1.00 48.67 ? 741 NAG B C3 1 HETATM 9127 C C4 . NAG MA 2 . ? 12.779 50.466 4.449 1.00 48.59 ? 741 NAG B C4 1 HETATM 9128 C C5 . NAG MA 2 . ? 13.383 49.183 5.039 1.00 48.06 ? 741 NAG B C5 1 HETATM 9129 C C6 . NAG MA 2 . ? 14.641 49.441 5.851 1.00 48.18 ? 741 NAG B C6 1 HETATM 9130 C C7 . NAG MA 2 . ? 8.148 49.447 4.206 1.00 50.78 ? 741 NAG B C7 1 HETATM 9131 C C8 . NAG MA 2 . ? 7.403 50.131 3.071 1.00 52.55 ? 741 NAG B C8 1 HETATM 9132 N N2 . NAG MA 2 . ? 9.345 48.941 3.923 1.00 48.97 ? 741 NAG B N2 1 HETATM 9133 O O3 . NAG MA 2 . ? 10.844 51.358 3.321 1.00 49.52 ? 741 NAG B O3 1 HETATM 9134 O O4 . NAG MA 2 . ? 13.694 51.054 3.533 1.00 49.71 ? 741 NAG B O4 1 HETATM 9135 O O5 . NAG MA 2 . ? 12.432 48.548 5.922 1.00 46.13 ? 741 NAG B O5 1 HETATM 9136 O O6 . NAG MA 2 . ? 14.377 50.285 6.964 1.00 48.98 ? 741 NAG B O6 1 HETATM 9137 O O7 . NAG MA 2 . ? 7.639 49.387 5.326 1.00 52.07 ? 741 NAG B O7 1 HETATM 9138 C C1 . NAG NA 2 . ? 24.503 31.897 -1.791 1.00 22.52 ? 750 NAG B C1 1 HETATM 9139 C C2 . NAG NA 2 . ? 25.251 31.713 -3.127 1.00 23.58 ? 750 NAG B C2 1 HETATM 9140 C C3 . NAG NA 2 . ? 24.346 31.115 -4.208 1.00 24.09 ? 750 NAG B C3 1 HETATM 9141 C C4 . NAG NA 2 . ? 23.610 29.878 -3.680 1.00 24.30 ? 750 NAG B C4 1 HETATM 9142 C C5 . NAG NA 2 . ? 22.876 30.245 -2.394 1.00 25.17 ? 750 NAG B C5 1 HETATM 9143 C C6 . NAG NA 2 . ? 22.110 29.081 -1.783 1.00 25.21 ? 750 NAG B C6 1 HETATM 9144 C C7 . NAG NA 2 . ? 27.056 33.307 -3.453 1.00 25.50 ? 750 NAG B C7 1 HETATM 9145 C C8 . NAG NA 2 . ? 27.433 34.763 -3.676 1.00 25.81 ? 750 NAG B C8 1 HETATM 9146 N N2 . NAG NA 2 . ? 25.770 32.989 -3.599 1.00 24.77 ? 750 NAG B N2 1 HETATM 9147 O O3 . NAG NA 2 . ? 25.148 30.757 -5.321 1.00 25.19 ? 750 NAG B O3 1 HETATM 9148 O O4 . NAG NA 2 . ? 22.676 29.410 -4.642 1.00 22.95 ? 750 NAG B O4 1 HETATM 9149 O O5 . NAG NA 2 . ? 23.827 30.689 -1.415 1.00 23.33 ? 750 NAG B O5 1 HETATM 9150 O O6 . NAG NA 2 . ? 22.904 27.903 -1.743 1.00 26.00 ? 750 NAG B O6 1 HETATM 9151 O O7 . NAG NA 2 . ? 27.918 32.497 -3.108 1.00 26.97 ? 750 NAG B O7 1 HETATM 9152 C C1 . NAG OA 2 . ? 16.728 16.462 42.497 1.00 34.00 ? 760 NAG B C1 1 HETATM 9153 C C2 . NAG OA 2 . ? 17.111 16.758 43.952 1.00 34.02 ? 760 NAG B C2 1 HETATM 9154 C C3 . NAG OA 2 . ? 18.530 16.261 44.268 1.00 36.66 ? 760 NAG B C3 1 HETATM 9155 C C4 . NAG OA 2 . ? 18.734 14.812 43.796 1.00 36.86 ? 760 NAG B C4 1 HETATM 9156 C C5 . NAG OA 2 . ? 18.297 14.671 42.333 1.00 38.08 ? 760 NAG B C5 1 HETATM 9157 C C6 . NAG OA 2 . ? 18.412 13.255 41.792 1.00 38.04 ? 760 NAG B C6 1 HETATM 9158 C C7 . NAG OA 2 . ? 16.279 18.681 45.161 1.00 32.59 ? 760 NAG B C7 1 HETATM 9159 C C8 . NAG OA 2 . ? 16.384 20.172 45.423 1.00 32.53 ? 760 NAG B C8 1 HETATM 9160 N N2 . NAG OA 2 . ? 17.037 18.189 44.185 1.00 33.51 ? 760 NAG B N2 1 HETATM 9161 O O3 . NAG OA 2 . ? 18.752 16.336 45.670 1.00 35.94 ? 760 NAG B O3 1 HETATM 9162 O O4 . NAG OA 2 . ? 20.105 14.454 43.926 1.00 38.44 ? 760 NAG B O4 1 HETATM 9163 O O5 . NAG OA 2 . ? 16.919 15.074 42.196 1.00 35.32 ? 760 NAG B O5 1 HETATM 9164 O O6 . NAG OA 2 . ? 17.585 12.354 42.516 1.00 40.80 ? 760 NAG B O6 1 HETATM 9165 O O7 . NAG OA 2 . ? 15.519 17.989 45.841 1.00 34.26 ? 760 NAG B O7 1 HETATM 9166 CU CU . CU PA 6 . ? 4.362 31.229 21.100 1.00 15.62 ? 601 CU B CU 1 HETATM 9167 CU CU . CU QA 6 . ? 16.447 28.899 20.814 1.00 22.53 ? 602 CU B CU 1 HETATM 9168 CU CU . CU RA 6 . ? 15.920 27.354 25.222 1.00 17.04 ? 603 CU B CU 1 HETATM 9169 CU CU . CU SA 6 . ? 18.467 30.077 24.027 1.00 20.08 ? 604 CU B CU 1 HETATM 9170 CL CL . CL TA 7 . ? 20.315 31.569 25.022 1.00 27.01 ? 610 CL B CL 1 HETATM 9171 S S . SO4 UA 8 . ? 39.139 37.082 28.491 1.00 71.95 ? 800 SO4 B S 1 HETATM 9172 O O1 . SO4 UA 8 . ? 38.992 36.352 27.218 1.00 71.67 ? 800 SO4 B O1 1 HETATM 9173 O O2 . SO4 UA 8 . ? 40.377 37.882 28.458 1.00 71.96 ? 800 SO4 B O2 1 HETATM 9174 O O3 . SO4 UA 8 . ? 39.205 36.118 29.606 1.00 71.58 ? 800 SO4 B O3 1 HETATM 9175 O O4 . SO4 UA 8 . ? 37.984 37.977 28.686 1.00 71.98 ? 800 SO4 B O4 1 HETATM 9176 O O1 . OXY VA 9 . ? 15.630 27.740 22.598 1.00 28.22 ? 620 OXY B O1 1 HETATM 9177 O O2 . OXY VA 9 . ? 16.426 28.472 23.288 1.00 27.81 ? 620 OXY B O2 1 HETATM 9178 O O . HOH WA 10 . ? -23.615 51.054 32.439 1.00 13.87 ? 802 HOH A O 1 HETATM 9179 O O . HOH WA 10 . ? -38.418 26.601 38.048 1.00 6.38 ? 803 HOH A O 1 HETATM 9180 O O . HOH WA 10 . ? -40.802 18.704 31.874 1.00 12.37 ? 804 HOH A O 1 HETATM 9181 O O . HOH WA 10 . ? -25.468 23.172 37.080 1.00 8.00 ? 805 HOH A O 1 HETATM 9182 O O . HOH WA 10 . ? -40.570 24.724 39.080 1.00 7.56 ? 806 HOH A O 1 HETATM 9183 O O . HOH WA 10 . ? -25.814 31.783 8.876 1.00 13.76 ? 807 HOH A O 1 HETATM 9184 O O . HOH WA 10 . ? -43.389 26.922 42.530 1.00 11.10 ? 808 HOH A O 1 HETATM 9185 O O . HOH WA 10 . ? -28.232 35.874 18.031 1.00 10.03 ? 809 HOH A O 1 HETATM 9186 O O . HOH WA 10 . ? -21.857 21.634 37.538 1.00 9.08 ? 810 HOH A O 1 HETATM 9187 O O . HOH WA 10 . ? -22.761 35.854 13.193 1.00 10.05 ? 811 HOH A O 1 HETATM 9188 O O . HOH WA 10 . ? -17.312 26.799 34.703 1.00 11.47 ? 812 HOH A O 1 HETATM 9189 O O . HOH WA 10 . ? -37.565 17.311 47.559 1.00 12.01 ? 813 HOH A O 1 HETATM 9190 O O . HOH WA 10 . ? -19.849 33.511 14.687 1.00 10.16 ? 814 HOH A O 1 HETATM 9191 O O . HOH WA 10 . ? -49.095 46.034 13.619 1.00 10.14 ? 815 HOH A O 1 HETATM 9192 O O . HOH WA 10 . ? -41.913 16.960 25.460 1.00 13.57 ? 816 HOH A O 1 HETATM 9193 O O . HOH WA 10 . ? -35.633 26.852 10.182 1.00 6.91 ? 817 HOH A O 1 HETATM 9194 O O . HOH WA 10 . ? -25.060 43.810 27.258 1.00 11.75 ? 818 HOH A O 1 HETATM 9195 O O . HOH WA 10 . ? -38.122 24.497 26.032 1.00 8.46 ? 819 HOH A O 1 HETATM 9196 O O . HOH WA 10 . ? -27.400 46.741 18.182 1.00 8.77 ? 820 HOH A O 1 HETATM 9197 O O . HOH WA 10 . ? -15.349 23.928 17.265 1.00 12.74 ? 821 HOH A O 1 HETATM 9198 O O . HOH WA 10 . ? -19.283 31.640 42.547 1.00 12.98 ? 822 HOH A O 1 HETATM 9199 O O . HOH WA 10 . ? -43.224 18.433 39.607 1.00 11.06 ? 823 HOH A O 1 HETATM 9200 O O . HOH WA 10 . ? -21.260 35.844 15.468 1.00 11.02 ? 824 HOH A O 1 HETATM 9201 O O . HOH WA 10 . ? -15.640 30.194 31.394 1.00 12.57 ? 825 HOH A O 1 HETATM 9202 O O . HOH WA 10 . ? -28.458 19.609 34.045 1.00 13.66 ? 826 HOH A O 1 HETATM 9203 O O . HOH WA 10 . ? -30.402 44.366 17.490 1.00 11.16 ? 827 HOH A O 1 HETATM 9204 O O . HOH WA 10 . ? -52.103 44.930 8.632 1.00 11.77 ? 828 HOH A O 1 HETATM 9205 O O . HOH WA 10 . ? -24.696 18.281 29.680 1.00 10.37 ? 829 HOH A O 1 HETATM 9206 O O . HOH WA 10 . ? -19.592 11.450 18.992 1.00 16.58 ? 830 HOH A O 1 HETATM 9207 O O . HOH WA 10 . ? -42.011 30.208 23.689 1.00 14.96 ? 831 HOH A O 1 HETATM 9208 O O . HOH WA 10 . ? -33.521 49.204 15.689 1.00 7.58 ? 832 HOH A O 1 HETATM 9209 O O . HOH WA 10 . ? -16.142 15.559 27.299 1.00 10.76 ? 833 HOH A O 1 HETATM 9210 O O . HOH WA 10 . ? -42.840 28.733 40.575 1.00 14.38 ? 834 HOH A O 1 HETATM 9211 O O . HOH WA 10 . ? -39.796 22.675 43.313 1.00 11.03 ? 835 HOH A O 1 HETATM 9212 O O . HOH WA 10 . ? -31.532 42.594 44.439 1.00 16.37 ? 836 HOH A O 1 HETATM 9213 O O . HOH WA 10 . ? -25.827 40.816 27.438 1.00 12.26 ? 837 HOH A O 1 HETATM 9214 O O . HOH WA 10 . ? -39.417 51.247 26.242 1.00 15.40 ? 838 HOH A O 1 HETATM 9215 O O . HOH WA 10 . ? -18.719 37.440 24.863 1.00 9.42 ? 839 HOH A O 1 HETATM 9216 O O . HOH WA 10 . ? -46.953 24.303 27.194 1.00 15.18 ? 840 HOH A O 1 HETATM 9217 O O . HOH WA 10 . ? -31.908 30.184 2.036 1.00 14.69 ? 841 HOH A O 1 HETATM 9218 O O . HOH WA 10 . ? -45.799 36.541 11.372 1.00 11.31 ? 842 HOH A O 1 HETATM 9219 O O . HOH WA 10 . ? -32.098 38.329 20.258 1.00 12.17 ? 843 HOH A O 1 HETATM 9220 O O . HOH WA 10 . ? -49.400 36.662 14.846 1.00 17.85 ? 844 HOH A O 1 HETATM 9221 O O . HOH WA 10 . ? -23.792 22.066 41.663 1.00 10.85 ? 845 HOH A O 1 HETATM 9222 O O . HOH WA 10 . ? -49.839 21.944 33.445 1.00 11.88 ? 846 HOH A O 1 HETATM 9223 O O . HOH WA 10 . ? -41.254 24.536 41.651 1.00 9.48 ? 847 HOH A O 1 HETATM 9224 O O . HOH WA 10 . ? -43.619 25.062 29.605 1.00 18.85 ? 848 HOH A O 1 HETATM 9225 O O . HOH WA 10 . ? -21.537 49.570 20.190 1.00 14.26 ? 849 HOH A O 1 HETATM 9226 O O . HOH WA 10 . ? -16.774 31.626 20.423 1.00 15.83 ? 850 HOH A O 1 HETATM 9227 O O . HOH WA 10 . ? -35.145 26.825 37.970 1.00 13.13 ? 851 HOH A O 1 HETATM 9228 O O . HOH WA 10 . ? -46.915 19.045 39.218 1.00 9.64 ? 852 HOH A O 1 HETATM 9229 O O . HOH WA 10 . ? -17.125 23.753 19.402 1.00 12.07 ? 853 HOH A O 1 HETATM 9230 O O . HOH WA 10 . ? -18.799 32.797 17.008 1.00 12.89 ? 854 HOH A O 1 HETATM 9231 O O . HOH WA 10 . ? -38.201 41.155 33.932 1.00 11.16 ? 855 HOH A O 1 HETATM 9232 O O . HOH WA 10 . ? -40.734 26.871 23.399 1.00 18.44 ? 856 HOH A O 1 HETATM 9233 O O . HOH WA 10 . ? -51.112 25.427 25.293 1.00 14.48 ? 857 HOH A O 1 HETATM 9234 O O . HOH WA 10 . ? -26.715 47.598 23.992 1.00 10.17 ? 858 HOH A O 1 HETATM 9235 O O . HOH WA 10 . ? -18.224 46.211 25.199 1.00 16.13 ? 859 HOH A O 1 HETATM 9236 O O . HOH WA 10 . ? -36.004 46.105 28.738 1.00 14.62 ? 860 HOH A O 1 HETATM 9237 O O . HOH WA 10 . ? -44.689 22.368 4.475 1.00 17.44 ? 861 HOH A O 1 HETATM 9238 O O . HOH WA 10 . ? -14.286 36.021 42.216 1.00 16.46 ? 862 HOH A O 1 HETATM 9239 O O . HOH WA 10 . ? -24.544 50.182 23.259 1.00 13.24 ? 863 HOH A O 1 HETATM 9240 O O . HOH WA 10 . ? -15.656 20.409 30.514 1.00 11.78 ? 864 HOH A O 1 HETATM 9241 O O . HOH WA 10 . ? -11.492 21.188 25.704 1.00 15.11 ? 865 HOH A O 1 HETATM 9242 O O . HOH WA 10 . ? -44.791 38.221 14.996 1.00 13.65 ? 866 HOH A O 1 HETATM 9243 O O . HOH WA 10 . ? -32.627 16.435 42.291 1.00 18.55 ? 867 HOH A O 1 HETATM 9244 O O . HOH WA 10 . ? -23.760 22.902 39.032 1.00 10.14 ? 868 HOH A O 1 HETATM 9245 O O . HOH WA 10 . ? -19.170 37.278 52.914 1.00 14.34 ? 869 HOH A O 1 HETATM 9246 O O . HOH WA 10 . ? -34.245 18.296 35.843 1.00 9.22 ? 870 HOH A O 1 HETATM 9247 O O . HOH WA 10 . ? -44.118 9.856 35.371 1.00 16.38 ? 871 HOH A O 1 HETATM 9248 O O . HOH WA 10 . ? -49.210 30.283 47.744 1.00 27.25 ? 872 HOH A O 1 HETATM 9249 O O . HOH WA 10 . ? -16.795 36.215 27.670 1.00 11.65 ? 873 HOH A O 1 HETATM 9250 O O . HOH WA 10 . ? -40.918 37.256 36.856 1.00 15.58 ? 874 HOH A O 1 HETATM 9251 O O . HOH WA 10 . ? -44.705 26.519 46.173 1.00 17.67 ? 875 HOH A O 1 HETATM 9252 O O . HOH WA 10 . ? -15.008 37.748 36.882 1.00 14.09 ? 876 HOH A O 1 HETATM 9253 O O . HOH WA 10 . ? -17.479 29.547 33.825 1.00 14.13 ? 877 HOH A O 1 HETATM 9254 O O . HOH WA 10 . ? -16.062 17.864 29.810 1.00 8.62 ? 878 HOH A O 1 HETATM 9255 O O . HOH WA 10 . ? -36.721 12.758 33.708 1.00 14.74 ? 879 HOH A O 1 HETATM 9256 O O . HOH WA 10 . ? -20.891 44.461 41.485 1.00 18.61 ? 880 HOH A O 1 HETATM 9257 O O . HOH WA 10 . ? -57.272 28.892 32.535 1.00 17.83 ? 881 HOH A O 1 HETATM 9258 O O . HOH WA 10 . ? -50.799 13.572 36.755 1.00 14.28 ? 882 HOH A O 1 HETATM 9259 O O . HOH WA 10 . ? -33.193 12.610 43.868 1.00 25.10 ? 883 HOH A O 1 HETATM 9260 O O . HOH WA 10 . ? -31.788 51.529 14.519 1.00 15.96 ? 884 HOH A O 1 HETATM 9261 O O . HOH WA 10 . ? -42.554 18.393 5.296 1.00 13.76 ? 885 HOH A O 1 HETATM 9262 O O . HOH WA 10 . ? -45.997 29.454 45.852 1.00 18.15 ? 886 HOH A O 1 HETATM 9263 O O . HOH WA 10 . ? -18.147 13.785 19.563 1.00 13.94 ? 887 HOH A O 1 HETATM 9264 O O . HOH WA 10 . ? -49.573 48.537 14.652 1.00 15.49 ? 888 HOH A O 1 HETATM 9265 O O . HOH WA 10 . ? -12.775 24.883 25.132 1.00 20.38 ? 889 HOH A O 1 HETATM 9266 O O . HOH WA 10 . ? -21.417 51.931 24.173 1.00 15.21 ? 890 HOH A O 1 HETATM 9267 O O . HOH WA 10 . ? -36.929 23.708 53.370 1.00 24.66 ? 891 HOH A O 1 HETATM 9268 O O . HOH WA 10 . ? -43.852 21.116 51.156 1.00 17.95 ? 892 HOH A O 1 HETATM 9269 O O . HOH WA 10 . ? -40.909 17.459 38.249 1.00 12.03 ? 893 HOH A O 1 HETATM 9270 O O . HOH WA 10 . ? -14.334 16.245 25.273 1.00 20.27 ? 894 HOH A O 1 HETATM 9271 O O . HOH WA 10 . ? -8.899 14.599 31.995 1.00 26.52 ? 895 HOH A O 1 HETATM 9272 O O . HOH WA 10 . ? -44.587 29.354 43.391 1.00 12.65 ? 896 HOH A O 1 HETATM 9273 O O . HOH WA 10 . ? -55.099 32.039 38.838 1.00 12.62 ? 897 HOH A O 1 HETATM 9274 O O . HOH WA 10 . ? -28.480 21.126 9.005 1.00 16.62 ? 898 HOH A O 1 HETATM 9275 O O . HOH WA 10 . ? -36.968 40.147 5.642 1.00 13.52 ? 899 HOH A O 1 HETATM 9276 O O . HOH WA 10 . ? -39.022 27.534 17.289 1.00 10.82 ? 900 HOH A O 1 HETATM 9277 O O . HOH WA 10 . ? -15.898 30.659 7.558 1.00 17.21 ? 901 HOH A O 1 HETATM 9278 O O . HOH WA 10 . ? -36.551 38.017 53.497 1.00 16.56 ? 902 HOH A O 1 HETATM 9279 O O . HOH WA 10 . ? -23.597 28.749 48.149 1.00 15.98 ? 903 HOH A O 1 HETATM 9280 O O . HOH WA 10 . ? -47.144 33.975 14.363 1.00 14.65 ? 904 HOH A O 1 HETATM 9281 O O . HOH WA 10 . ? -27.410 44.831 10.453 1.00 27.46 ? 905 HOH A O 1 HETATM 9282 O O . HOH WA 10 . ? -53.030 16.201 28.156 1.00 24.83 ? 906 HOH A O 1 HETATM 9283 O O . HOH WA 10 . ? -18.279 16.407 29.926 1.00 16.27 ? 907 HOH A O 1 HETATM 9284 O O . HOH WA 10 . ? -24.762 44.402 24.730 1.00 17.52 ? 908 HOH A O 1 HETATM 9285 O O . HOH WA 10 . ? -33.684 30.539 4.492 1.00 28.93 ? 909 HOH A O 1 HETATM 9286 O O . HOH WA 10 . ? -11.062 27.945 35.738 1.00 19.41 ? 910 HOH A O 1 HETATM 9287 O O . HOH WA 10 . ? -41.591 18.608 27.544 1.00 16.98 ? 911 HOH A O 1 HETATM 9288 O O . HOH WA 10 . ? -49.570 27.614 25.128 1.00 11.98 ? 912 HOH A O 1 HETATM 9289 O O . HOH WA 10 . ? -15.762 43.761 26.767 1.00 12.00 ? 913 HOH A O 1 HETATM 9290 O O . HOH WA 10 . ? -18.368 31.334 24.343 1.00 11.46 ? 914 HOH A O 1 HETATM 9291 O O . HOH WA 10 . ? -59.410 34.855 12.474 1.00 19.89 ? 915 HOH A O 1 HETATM 9292 O O . HOH WA 10 . ? -52.429 30.746 22.153 1.00 22.43 ? 916 HOH A O 1 HETATM 9293 O O . HOH WA 10 . ? -37.620 54.196 19.892 1.00 19.77 ? 917 HOH A O 1 HETATM 9294 O O . HOH WA 10 . ? -54.864 41.243 14.629 1.00 21.28 ? 918 HOH A O 1 HETATM 9295 O O . HOH WA 10 . ? -16.284 44.118 43.932 1.00 35.34 ? 919 HOH A O 1 HETATM 9296 O O . HOH WA 10 . ? -19.033 32.865 47.400 1.00 15.32 ? 920 HOH A O 1 HETATM 9297 O O . HOH WA 10 . ? -46.585 12.382 30.448 1.00 19.10 ? 921 HOH A O 1 HETATM 9298 O O . HOH WA 10 . ? -46.711 42.987 2.140 1.00 14.96 ? 922 HOH A O 1 HETATM 9299 O O . HOH WA 10 . ? -5.329 17.625 26.428 1.00 25.18 ? 923 HOH A O 1 HETATM 9300 O O . HOH WA 10 . ? -30.707 27.783 1.628 1.00 15.88 ? 924 HOH A O 1 HETATM 9301 O O . HOH WA 10 . ? -49.083 34.193 41.041 1.00 20.79 ? 925 HOH A O 1 HETATM 9302 O O . HOH WA 10 . ? -34.815 45.451 10.654 1.00 15.06 ? 926 HOH A O 1 HETATM 9303 O O . HOH WA 10 . ? -21.077 0.600 26.850 1.00 22.16 ? 927 HOH A O 1 HETATM 9304 O O . HOH WA 10 . ? -49.988 34.062 14.790 1.00 19.82 ? 928 HOH A O 1 HETATM 9305 O O . HOH WA 10 . ? -11.912 18.665 26.528 1.00 19.11 ? 929 HOH A O 1 HETATM 9306 O O . HOH WA 10 . ? -20.483 43.673 56.859 1.00 19.63 ? 930 HOH A O 1 HETATM 9307 O O . HOH WA 10 . ? -37.282 30.709 6.938 1.00 15.91 ? 931 HOH A O 1 HETATM 9308 O O . HOH WA 10 . ? -43.080 35.008 49.855 1.00 18.14 ? 932 HOH A O 1 HETATM 9309 O O . HOH WA 10 . ? -43.311 47.375 32.701 1.00 27.12 ? 933 HOH A O 1 HETATM 9310 O O . HOH WA 10 . ? -43.861 30.883 46.451 1.00 17.80 ? 934 HOH A O 1 HETATM 9311 O O . HOH WA 10 . ? -15.074 44.454 22.276 1.00 27.82 ? 935 HOH A O 1 HETATM 9312 O O . HOH WA 10 . ? -59.315 34.731 30.958 1.00 18.73 ? 936 HOH A O 1 HETATM 9313 O O . HOH WA 10 . ? -41.382 37.505 39.576 1.00 21.27 ? 937 HOH A O 1 HETATM 9314 O O . HOH WA 10 . ? -18.560 17.665 13.614 1.00 26.30 ? 938 HOH A O 1 HETATM 9315 O O . HOH WA 10 . ? -42.567 20.079 49.047 1.00 16.54 ? 939 HOH A O 1 HETATM 9316 O O . HOH WA 10 . ? -11.242 40.224 35.220 1.00 19.00 ? 940 HOH A O 1 HETATM 9317 O O . HOH WA 10 . ? -31.939 55.967 17.856 1.00 18.40 ? 941 HOH A O 1 HETATM 9318 O O . HOH WA 10 . ? -55.270 26.641 26.788 1.00 16.62 ? 942 HOH A O 1 HETATM 9319 O O . HOH WA 10 . ? -28.526 41.800 16.876 1.00 18.77 ? 943 HOH A O 1 HETATM 9320 O O . HOH WA 10 . ? -17.173 37.225 42.602 1.00 11.14 ? 944 HOH A O 1 HETATM 9321 O O . HOH WA 10 . ? -18.049 24.622 45.245 1.00 18.22 ? 945 HOH A O 1 HETATM 9322 O O . HOH WA 10 . ? -29.333 41.238 36.127 1.00 17.59 ? 946 HOH A O 1 HETATM 9323 O O . HOH WA 10 . ? -33.421 12.944 10.996 1.00 24.40 ? 947 HOH A O 1 HETATM 9324 O O . HOH WA 10 . ? -55.486 25.751 40.550 1.00 17.99 ? 948 HOH A O 1 HETATM 9325 O O . HOH WA 10 . ? -22.359 51.537 16.552 1.00 25.13 ? 949 HOH A O 1 HETATM 9326 O O . HOH WA 10 . ? -21.535 20.614 10.585 1.00 14.78 ? 950 HOH A O 1 HETATM 9327 O O . HOH WA 10 . ? -55.051 34.363 6.536 1.00 22.49 ? 951 HOH A O 1 HETATM 9328 O O . HOH WA 10 . ? -27.964 11.192 35.165 1.00 27.73 ? 952 HOH A O 1 HETATM 9329 O O . HOH WA 10 . ? -47.797 45.882 30.985 1.00 17.40 ? 953 HOH A O 1 HETATM 9330 O O . HOH WA 10 . ? -49.833 17.861 21.247 1.00 19.11 ? 954 HOH A O 1 HETATM 9331 O O . HOH WA 10 . ? -39.047 15.594 46.168 1.00 17.95 ? 955 HOH A O 1 HETATM 9332 O O . HOH WA 10 . ? -19.648 56.551 29.983 1.00 20.92 ? 956 HOH A O 1 HETATM 9333 O O . HOH WA 10 . ? -22.847 15.943 37.047 1.00 21.39 ? 957 HOH A O 1 HETATM 9334 O O . HOH WA 10 . ? -43.463 22.767 36.196 1.00 25.50 ? 958 HOH A O 1 HETATM 9335 O O . HOH WA 10 . ? -31.698 35.427 20.117 1.00 14.10 ? 959 HOH A O 1 HETATM 9336 O O . HOH WA 10 . ? -34.951 15.907 7.716 1.00 20.97 ? 960 HOH A O 1 HETATM 9337 O O . HOH WA 10 . ? -45.700 14.425 9.448 1.00 40.10 ? 961 HOH A O 1 HETATM 9338 O O . HOH WA 10 . ? -53.128 35.125 38.430 1.00 19.56 ? 962 HOH A O 1 HETATM 9339 O O . HOH WA 10 . ? -58.771 23.327 45.276 1.00 27.13 ? 963 HOH A O 1 HETATM 9340 O O . HOH WA 10 . ? -34.005 46.101 2.862 1.00 32.67 ? 964 HOH A O 1 HETATM 9341 O O . HOH WA 10 . ? -12.651 24.945 8.911 1.00 23.50 ? 965 HOH A O 1 HETATM 9342 O O . HOH WA 10 . ? -29.960 57.657 30.581 1.00 26.86 ? 966 HOH A O 1 HETATM 9343 O O . HOH WA 10 . ? -20.887 34.352 11.346 1.00 12.66 ? 967 HOH A O 1 HETATM 9344 O O . HOH WA 10 . ? -17.398 31.207 49.035 1.00 29.31 ? 968 HOH A O 1 HETATM 9345 O O . HOH WA 10 . ? -46.082 26.133 29.559 1.00 17.52 ? 969 HOH A O 1 HETATM 9346 O O . HOH WA 10 . ? -19.076 38.616 55.395 1.00 20.85 ? 970 HOH A O 1 HETATM 9347 O O . HOH WA 10 . ? -29.912 41.770 4.078 1.00 21.19 ? 971 HOH A O 1 HETATM 9348 O O . HOH WA 10 . ? -29.204 21.883 6.407 1.00 21.60 ? 972 HOH A O 1 HETATM 9349 O O . HOH WA 10 . ? -37.788 23.956 31.376 1.00 11.57 ? 973 HOH A O 1 HETATM 9350 O O . HOH WA 10 . ? -10.301 42.832 34.595 1.00 16.95 ? 974 HOH A O 1 HETATM 9351 O O . HOH WA 10 . ? -29.466 40.045 29.631 1.00 26.20 ? 975 HOH A O 1 HETATM 9352 O O . HOH WA 10 . ? -22.801 11.278 31.100 1.00 23.48 ? 976 HOH A O 1 HETATM 9353 O O . HOH WA 10 . ? -13.505 36.818 34.786 1.00 13.26 ? 977 HOH A O 1 HETATM 9354 O O . HOH WA 10 . ? -41.221 14.651 29.173 1.00 22.62 ? 978 HOH A O 1 HETATM 9355 O O . HOH WA 10 . ? -13.017 33.460 32.973 1.00 19.80 ? 979 HOH A O 1 HETATM 9356 O O . HOH WA 10 . ? -45.794 50.503 28.338 1.00 19.08 ? 980 HOH A O 1 HETATM 9357 O O . HOH WA 10 . ? -29.505 7.655 8.937 1.00 23.96 ? 981 HOH A O 1 HETATM 9358 O O . HOH WA 10 . ? -13.163 8.903 21.216 1.00 35.34 ? 982 HOH A O 1 HETATM 9359 O O . HOH WA 10 . ? -11.943 37.760 53.695 1.00 28.39 ? 983 HOH A O 1 HETATM 9360 O O . HOH WA 10 . ? -25.157 49.781 54.075 1.00 19.76 ? 984 HOH A O 1 HETATM 9361 O O . HOH WA 10 . ? -39.657 38.636 56.087 1.00 26.61 ? 985 HOH A O 1 HETATM 9362 O O . HOH WA 10 . ? -46.831 36.693 14.088 1.00 10.38 ? 986 HOH A O 1 HETATM 9363 O O . HOH WA 10 . ? -22.336 34.203 9.005 1.00 18.10 ? 987 HOH A O 1 HETATM 9364 O O . HOH WA 10 . ? -53.425 26.576 24.707 1.00 18.43 ? 988 HOH A O 1 HETATM 9365 O O . HOH WA 10 . ? -16.854 44.170 24.283 1.00 15.86 ? 989 HOH A O 1 HETATM 9366 O O . HOH WA 10 . ? -53.708 27.475 39.715 1.00 15.02 ? 990 HOH A O 1 HETATM 9367 O O . HOH WA 10 . ? -25.413 45.542 54.053 1.00 19.92 ? 991 HOH A O 1 HETATM 9368 O O . HOH WA 10 . ? -24.599 43.152 42.117 1.00 14.84 ? 992 HOH A O 1 HETATM 9369 O O . HOH WA 10 . ? -31.988 1.105 29.137 1.00 17.97 ? 993 HOH A O 1 HETATM 9370 O O . HOH WA 10 . ? -47.505 27.098 26.776 1.00 15.55 ? 994 HOH A O 1 HETATM 9371 O O . HOH WA 10 . ? -24.642 33.791 10.117 1.00 15.84 ? 995 HOH A O 1 HETATM 9372 O O . HOH WA 10 . ? -18.294 29.590 52.054 1.00 27.13 ? 996 HOH A O 1 HETATM 9373 O O . HOH WA 10 . ? -43.609 12.226 41.824 1.00 18.03 ? 997 HOH A O 1 HETATM 9374 O O . HOH WA 10 . ? -33.590 22.451 5.438 1.00 17.65 ? 998 HOH A O 1 HETATM 9375 O O . HOH WA 10 . ? -18.280 28.561 25.102 1.00 22.01 ? 999 HOH A O 1 HETATM 9376 O O . HOH WA 10 . ? -42.549 17.431 48.509 1.00 18.82 ? 1000 HOH A O 1 HETATM 9377 O O . HOH WA 10 . ? -53.028 29.685 19.797 1.00 27.68 ? 1001 HOH A O 1 HETATM 9378 O O . HOH WA 10 . ? -8.167 13.859 22.900 1.00 20.74 ? 1002 HOH A O 1 HETATM 9379 O O . HOH WA 10 . ? -14.551 43.671 41.516 1.00 27.41 ? 1003 HOH A O 1 HETATM 9380 O O . HOH WA 10 . ? -35.962 46.400 34.902 1.00 18.54 ? 1004 HOH A O 1 HETATM 9381 O O . HOH WA 10 . ? -41.500 16.575 46.152 1.00 19.80 ? 1005 HOH A O 1 HETATM 9382 O O . HOH WA 10 . ? -34.628 41.640 49.294 1.00 24.08 ? 1006 HOH A O 1 HETATM 9383 O O . HOH WA 10 . ? -45.352 47.648 7.057 1.00 21.86 ? 1007 HOH A O 1 HETATM 9384 O O . HOH WA 10 . ? -17.966 29.527 6.177 1.00 21.86 ? 1008 HOH A O 1 HETATM 9385 O O . HOH WA 10 . ? -15.214 17.635 13.684 1.00 18.56 ? 1009 HOH A O 1 HETATM 9386 O O . HOH WA 10 . ? -16.857 21.462 28.251 1.00 16.82 ? 1010 HOH A O 1 HETATM 9387 O O . HOH WA 10 . ? -29.105 41.513 27.498 1.00 18.83 ? 1011 HOH A O 1 HETATM 9388 O O . HOH WA 10 . ? -48.037 31.645 45.243 1.00 24.76 ? 1012 HOH A O 1 HETATM 9389 O O . HOH WA 10 . ? -53.002 27.859 16.582 1.00 21.58 ? 1013 HOH A O 1 HETATM 9390 O O . HOH WA 10 . ? -31.351 53.978 13.071 1.00 18.15 ? 1014 HOH A O 1 HETATM 9391 O O . HOH WA 10 . ? -13.941 34.026 38.592 1.00 18.50 ? 1015 HOH A O 1 HETATM 9392 O O . HOH WA 10 . ? -56.146 17.373 33.851 1.00 18.51 ? 1016 HOH A O 1 HETATM 9393 O O . HOH WA 10 . ? -23.880 48.742 46.893 1.00 18.42 ? 1017 HOH A O 1 HETATM 9394 O O . HOH WA 10 . ? -30.991 45.162 44.972 1.00 22.42 ? 1018 HOH A O 1 HETATM 9395 O O . HOH WA 10 . ? -34.638 8.500 17.549 1.00 19.93 ? 1019 HOH A O 1 HETATM 9396 O O . HOH WA 10 . ? -32.392 7.067 17.028 1.00 22.29 ? 1020 HOH A O 1 HETATM 9397 O O . HOH WA 10 . ? -14.979 41.169 51.556 1.00 21.61 ? 1021 HOH A O 1 HETATM 9398 O O . HOH WA 10 . ? -15.392 36.129 39.338 1.00 19.06 ? 1022 HOH A O 1 HETATM 9399 O O . HOH WA 10 . ? -29.472 52.468 34.641 1.00 22.56 ? 1023 HOH A O 1 HETATM 9400 O O . HOH WA 10 . ? -29.292 17.191 49.290 1.00 30.12 ? 1024 HOH A O 1 HETATM 9401 O O . HOH WA 10 . ? -50.917 35.790 39.731 1.00 16.73 ? 1025 HOH A O 1 HETATM 9402 O O . HOH WA 10 . ? -33.913 14.914 47.892 1.00 25.61 ? 1026 HOH A O 1 HETATM 9403 O O . HOH WA 10 . ? -58.546 37.083 33.984 1.00 22.25 ? 1027 HOH A O 1 HETATM 9404 O O . HOH WA 10 . ? -47.906 35.108 5.005 1.00 25.87 ? 1028 HOH A O 1 HETATM 9405 O O . HOH WA 10 . ? -22.636 36.500 7.663 1.00 24.63 ? 1029 HOH A O 1 HETATM 9406 O O . HOH WA 10 . ? -26.267 26.780 55.016 1.00 31.79 ? 1030 HOH A O 1 HETATM 9407 O O . HOH WA 10 . ? -39.863 47.184 32.176 1.00 29.62 ? 1031 HOH A O 1 HETATM 9408 O O . HOH WA 10 . ? -46.685 53.073 18.427 1.00 23.89 ? 1032 HOH A O 1 HETATM 9409 O O . HOH WA 10 . ? -56.997 31.011 31.168 1.00 18.44 ? 1033 HOH A O 1 HETATM 9410 O O . HOH WA 10 . ? -47.246 23.640 19.005 1.00 20.92 ? 1034 HOH A O 1 HETATM 9411 O O . HOH WA 10 . ? -52.380 17.261 46.862 1.00 21.07 ? 1035 HOH A O 1 HETATM 9412 O O . HOH WA 10 . ? -25.211 10.235 32.469 1.00 20.00 ? 1036 HOH A O 1 HETATM 9413 O O . HOH WA 10 . ? -32.590 -3.627 22.350 1.00 23.50 ? 1037 HOH A O 1 HETATM 9414 O O . HOH WA 10 . ? -29.074 27.366 52.963 1.00 23.34 ? 1038 HOH A O 1 HETATM 9415 O O . HOH WA 10 . ? -18.426 35.210 57.192 1.00 24.44 ? 1039 HOH A O 1 HETATM 9416 O O . HOH WA 10 . ? -28.419 46.715 28.343 1.00 19.91 ? 1040 HOH A O 1 HETATM 9417 O O . HOH WA 10 . ? -49.323 13.807 45.802 1.00 25.20 ? 1041 HOH A O 1 HETATM 9418 O O . HOH WA 10 . ? -30.753 48.597 37.224 1.00 23.80 ? 1042 HOH A O 1 HETATM 9419 O O . HOH WA 10 . ? -18.344 43.453 41.766 1.00 16.69 ? 1043 HOH A O 1 HETATM 9420 O O . HOH WA 10 . ? -29.575 41.125 11.790 1.00 23.38 ? 1044 HOH A O 1 HETATM 9421 O O . HOH WA 10 . ? -16.213 34.283 17.703 1.00 21.35 ? 1045 HOH A O 1 HETATM 9422 O O . HOH WA 10 . ? -39.892 15.292 26.221 1.00 21.16 ? 1046 HOH A O 1 HETATM 9423 O O . HOH WA 10 . ? -45.556 14.275 28.729 1.00 21.80 ? 1047 HOH A O 1 HETATM 9424 O O . HOH WA 10 . ? -54.426 38.359 7.591 1.00 26.63 ? 1048 HOH A O 1 HETATM 9425 O O . HOH WA 10 . ? -9.537 39.886 13.453 1.00 34.19 ? 1049 HOH A O 1 HETATM 9426 O O . HOH WA 10 . ? -41.621 52.717 26.717 1.00 24.19 ? 1050 HOH A O 1 HETATM 9427 O O . HOH WA 10 . ? -45.296 17.527 5.419 1.00 31.73 ? 1051 HOH A O 1 HETATM 9428 O O . HOH WA 10 . ? -11.499 36.914 38.712 1.00 22.29 ? 1052 HOH A O 1 HETATM 9429 O O . HOH WA 10 . ? -31.262 33.038 21.517 1.00 23.63 ? 1053 HOH A O 1 HETATM 9430 O O . HOH WA 10 . ? -30.428 28.301 26.969 1.00 21.59 ? 1054 HOH A O 1 HETATM 9431 O O . HOH WA 10 . ? -14.831 32.103 18.691 1.00 37.32 ? 1055 HOH A O 1 HETATM 9432 O O . HOH WA 10 . ? -38.289 39.538 51.946 1.00 26.23 ? 1056 HOH A O 1 HETATM 9433 O O . HOH WA 10 . ? -43.552 19.564 24.843 1.00 18.73 ? 1057 HOH A O 1 HETATM 9434 O O . HOH WA 10 . ? -41.256 6.147 22.528 1.00 24.21 ? 1058 HOH A O 1 HETATM 9435 O O . HOH WA 10 . ? -50.005 27.785 17.023 1.00 19.19 ? 1059 HOH A O 1 HETATM 9436 O O . HOH WA 10 . ? -42.539 54.402 16.647 1.00 25.70 ? 1060 HOH A O 1 HETATM 9437 O O . HOH WA 10 . ? -35.088 9.596 40.389 1.00 27.15 ? 1061 HOH A O 1 HETATM 9438 O O . HOH WA 10 . ? -16.083 7.521 27.002 1.00 29.90 ? 1062 HOH A O 1 HETATM 9439 O O . HOH WA 10 . ? -22.053 42.251 40.089 1.00 19.20 ? 1063 HOH A O 1 HETATM 9440 O O . HOH WA 10 . ? -39.024 11.417 10.527 1.00 28.65 ? 1064 HOH A O 1 HETATM 9441 O O . HOH WA 10 . ? -20.739 12.250 12.653 1.00 14.31 ? 1065 HOH A O 1 HETATM 9442 O O . HOH WA 10 . ? -18.295 49.016 18.493 1.00 27.67 ? 1066 HOH A O 1 HETATM 9443 O O . HOH WA 10 . ? -35.999 12.585 12.047 1.00 30.94 ? 1067 HOH A O 1 HETATM 9444 O O . HOH WA 10 . ? -56.171 37.067 13.906 1.00 26.24 ? 1068 HOH A O 1 HETATM 9445 O O . HOH WA 10 . ? -36.430 40.455 56.472 1.00 37.04 ? 1069 HOH A O 1 HETATM 9446 O O . HOH WA 10 . ? -20.140 12.740 31.635 1.00 29.62 ? 1070 HOH A O 1 HETATM 9447 O O . HOH WA 10 . ? -43.584 10.786 28.380 1.00 27.26 ? 1071 HOH A O 1 HETATM 9448 O O . HOH WA 10 . ? -51.752 39.736 17.473 1.00 19.51 ? 1072 HOH A O 1 HETATM 9449 O O . HOH WA 10 . ? -14.515 19.118 27.777 1.00 22.62 ? 1073 HOH A O 1 HETATM 9450 O O . HOH WA 10 . ? -34.382 37.195 6.257 1.00 20.12 ? 1074 HOH A O 1 HETATM 9451 O O . HOH WA 10 . ? -41.597 7.679 31.150 1.00 23.62 ? 1075 HOH A O 1 HETATM 9452 O O . HOH WA 10 . ? -51.572 36.109 17.723 1.00 25.33 ? 1076 HOH A O 1 HETATM 9453 O O . HOH WA 10 . ? -33.785 50.590 34.209 1.00 24.06 ? 1077 HOH A O 1 HETATM 9454 O O . HOH WA 10 . ? -12.230 20.345 23.195 1.00 30.71 ? 1078 HOH A O 1 HETATM 9455 O O . HOH WA 10 . ? -33.715 10.650 16.216 1.00 22.41 ? 1079 HOH A O 1 HETATM 9456 O O . HOH WA 10 . ? -31.573 45.678 4.088 1.00 25.15 ? 1080 HOH A O 1 HETATM 9457 O O . HOH WA 10 . ? -30.169 14.997 46.022 1.00 26.32 ? 1081 HOH A O 1 HETATM 9458 O O . HOH WA 10 . ? -36.721 56.366 18.616 1.00 20.05 ? 1082 HOH A O 1 HETATM 9459 O O . HOH WA 10 . ? -38.266 17.592 5.166 1.00 21.88 ? 1083 HOH A O 1 HETATM 9460 O O . HOH WA 10 . ? -21.175 21.887 45.463 1.00 26.00 ? 1084 HOH A O 1 HETATM 9461 O O . HOH WA 10 . ? -37.521 4.476 23.005 1.00 26.08 ? 1085 HOH A O 1 HETATM 9462 O O . HOH WA 10 . ? -41.999 43.993 36.928 1.00 22.17 ? 1086 HOH A O 1 HETATM 9463 O O . HOH WA 10 . ? -38.531 5.512 20.515 1.00 26.29 ? 1087 HOH A O 1 HETATM 9464 O O . HOH WA 10 . ? -16.775 8.929 24.178 1.00 27.95 ? 1088 HOH A O 1 HETATM 9465 O O . HOH WA 10 . ? -27.123 52.773 14.444 1.00 44.82 ? 1089 HOH A O 1 HETATM 9466 O O . HOH WA 10 . ? -31.628 26.337 -0.505 1.00 34.85 ? 1090 HOH A O 1 HETATM 9467 O O . HOH WA 10 . ? -36.342 16.088 49.715 1.00 31.62 ? 1091 HOH A O 1 HETATM 9468 O O . HOH WA 10 . ? -29.600 18.512 9.039 1.00 25.77 ? 1092 HOH A O 1 HETATM 9469 O O . HOH WA 10 . ? -43.646 50.323 3.734 1.00 31.44 ? 1093 HOH A O 1 HETATM 9470 O O . HOH WA 10 . ? -32.310 33.087 4.473 1.00 26.72 ? 1094 HOH A O 1 HETATM 9471 O O . HOH WA 10 . ? -38.301 45.159 35.166 1.00 30.44 ? 1095 HOH A O 1 HETATM 9472 O O . HOH WA 10 . ? -52.742 15.209 40.119 1.00 27.91 ? 1096 HOH A O 1 HETATM 9473 O O . HOH WA 10 . ? -14.388 22.067 12.034 1.00 25.39 ? 1097 HOH A O 1 HETATM 9474 O O . HOH WA 10 . ? -42.753 14.117 45.568 1.00 27.71 ? 1098 HOH A O 1 HETATM 9475 O O . HOH WA 10 . ? -14.701 18.399 34.392 1.00 25.99 ? 1099 HOH A O 1 HETATM 9476 O O . HOH WA 10 . ? -45.898 21.550 30.533 1.00 20.13 ? 1100 HOH A O 1 HETATM 9477 O O . HOH WA 10 . ? -53.008 29.656 24.498 1.00 25.71 ? 1101 HOH A O 1 HETATM 9478 O O . HOH WA 10 . ? -58.036 28.379 40.286 1.00 25.71 ? 1102 HOH A O 1 HETATM 9479 O O . HOH WA 10 . ? -54.162 41.272 33.694 1.00 25.18 ? 1103 HOH A O 1 HETATM 9480 O O . HOH WA 10 . ? -36.692 39.418 43.175 1.00 21.46 ? 1104 HOH A O 1 HETATM 9481 O O . HOH WA 10 . ? -43.503 21.574 -2.164 1.00 25.18 ? 1105 HOH A O 1 HETATM 9482 O O . HOH WA 10 . ? -39.747 38.592 41.464 1.00 20.34 ? 1106 HOH A O 1 HETATM 9483 O O . HOH WA 10 . ? -23.889 9.437 12.612 1.00 23.47 ? 1107 HOH A O 1 HETATM 9484 O O . HOH WA 10 . ? -19.583 51.973 21.763 1.00 31.42 ? 1108 HOH A O 1 HETATM 9485 O O . HOH WA 10 . ? -25.310 13.360 10.661 1.00 22.07 ? 1109 HOH A O 1 HETATM 9486 O O . HOH WA 10 . ? -40.288 52.463 6.788 1.00 32.74 ? 1110 HOH A O 1 HETATM 9487 O O . HOH WA 10 . ? -44.611 17.760 -0.743 1.00 20.86 ? 1111 HOH A O 1 HETATM 9488 O O . HOH WA 10 . ? -36.480 36.611 61.946 1.00 27.40 ? 1112 HOH A O 1 HETATM 9489 O O . HOH WA 10 . ? -39.059 18.277 2.466 1.00 26.94 ? 1113 HOH A O 1 HETATM 9490 O O . HOH WA 10 . ? -59.819 30.458 39.115 1.00 28.79 ? 1114 HOH A O 1 HETATM 9491 O O . HOH WA 10 . ? -36.648 52.252 8.733 1.00 35.59 ? 1115 HOH A O 1 HETATM 9492 O O . HOH WA 10 . ? -29.434 4.538 35.595 1.00 32.13 ? 1116 HOH A O 1 HETATM 9493 O O . HOH WA 10 . ? -22.470 -1.746 27.436 1.00 28.91 ? 1117 HOH A O 1 HETATM 9494 O O . HOH WA 10 . ? -27.416 11.769 32.461 1.00 27.30 ? 1118 HOH A O 1 HETATM 9495 O O . HOH WA 10 . ? -12.670 43.589 22.718 1.00 34.41 ? 1119 HOH A O 1 HETATM 9496 O O . HOH WA 10 . ? -15.786 31.527 55.019 1.00 45.96 ? 1120 HOH A O 1 HETATM 9497 O O . HOH WA 10 . ? -35.748 56.924 22.493 1.00 26.53 ? 1121 HOH A O 1 HETATM 9498 O O . HOH WA 10 . ? -12.694 33.108 54.127 1.00 30.16 ? 1122 HOH A O 1 HETATM 9499 O O . HOH WA 10 . ? -39.976 12.653 44.332 1.00 37.42 ? 1123 HOH A O 1 HETATM 9500 O O . HOH WA 10 . ? -17.651 2.341 30.324 1.00 31.50 ? 1124 HOH A O 1 HETATM 9501 O O . HOH WA 10 . ? -40.140 17.645 50.357 1.00 23.72 ? 1125 HOH A O 1 HETATM 9502 O O . HOH WA 10 . ? -56.982 35.412 27.389 1.00 35.16 ? 1126 HOH A O 1 HETATM 9503 O O . HOH WA 10 . ? -39.895 42.126 1.821 1.00 20.28 ? 1127 HOH A O 1 HETATM 9504 O O . HOH WA 10 . ? -18.278 40.481 9.803 1.00 28.70 ? 1128 HOH A O 1 HETATM 9505 O O . HOH WA 10 . ? -26.352 27.125 5.174 1.00 27.93 ? 1129 HOH A O 1 HETATM 9506 O O . HOH WA 10 . ? -45.043 11.619 39.638 1.00 23.60 ? 1130 HOH A O 1 HETATM 9507 O O . HOH WA 10 . ? -35.761 41.803 38.704 1.00 24.70 ? 1131 HOH A O 1 HETATM 9508 O O . HOH WA 10 . ? -37.506 26.712 -4.643 1.00 36.90 ? 1132 HOH A O 1 HETATM 9509 O O . HOH WA 10 . ? -21.193 46.644 13.161 1.00 38.48 ? 1133 HOH A O 1 HETATM 9510 O O . HOH WA 10 . ? -59.606 19.389 39.819 1.00 28.51 ? 1134 HOH A O 1 HETATM 9511 O O . HOH WA 10 . ? -39.470 10.334 13.039 1.00 29.83 ? 1135 HOH A O 1 HETATM 9512 O O . HOH WA 10 . ? -47.673 48.568 30.783 1.00 40.97 ? 1136 HOH A O 1 HETATM 9513 O O . HOH WA 10 . ? -15.491 47.168 33.175 1.00 38.10 ? 1137 HOH A O 1 HETATM 9514 O O . HOH WA 10 . ? -25.902 56.480 20.124 1.00 26.90 ? 1138 HOH A O 1 HETATM 9515 O O . HOH WA 10 . ? -29.439 24.847 51.570 1.00 26.71 ? 1139 HOH A O 1 HETATM 9516 O O . HOH WA 10 . ? -30.397 39.910 62.832 1.00 34.25 ? 1140 HOH A O 1 HETATM 9517 O O . HOH WA 10 . ? -29.279 35.504 20.442 1.00 26.17 ? 1141 HOH A O 1 HETATM 9518 O O . HOH WA 10 . ? -13.910 43.967 44.640 1.00 38.85 ? 1142 HOH A O 1 HETATM 9519 O O . HOH WA 10 . ? -4.773 15.181 25.815 1.00 21.10 ? 1143 HOH A O 1 HETATM 9520 O O . HOH WA 10 . ? -17.668 11.588 33.782 1.00 19.64 ? 1144 HOH A O 1 HETATM 9521 O O . HOH WA 10 . ? -16.009 30.614 52.646 1.00 32.61 ? 1145 HOH A O 1 HETATM 9522 O O . HOH WA 10 . ? -22.138 32.389 7.030 1.00 23.40 ? 1146 HOH A O 1 HETATM 9523 O O . HOH WA 10 . ? -45.202 35.861 43.031 1.00 24.55 ? 1147 HOH A O 1 HETATM 9524 O O . HOH WA 10 . ? -33.152 47.641 38.177 1.00 24.44 ? 1148 HOH A O 1 HETATM 9525 O O . HOH WA 10 . ? -24.928 -0.790 28.900 1.00 23.81 ? 1149 HOH A O 1 HETATM 9526 O O . HOH WA 10 . ? -18.603 37.556 57.794 1.00 20.68 ? 1150 HOH A O 1 HETATM 9527 O O . HOH WA 10 . ? -12.837 24.005 15.347 1.00 30.80 ? 1151 HOH A O 1 HETATM 9528 O O . HOH WA 10 . ? -28.778 53.452 37.329 1.00 28.84 ? 1152 HOH A O 1 HETATM 9529 O O . HOH WA 10 . ? -58.105 22.536 41.422 1.00 30.25 ? 1153 HOH A O 1 HETATM 9530 O O . HOH WA 10 . ? -26.097 54.786 17.708 1.00 30.20 ? 1154 HOH A O 1 HETATM 9531 O O . HOH WA 10 . ? -8.410 23.048 34.701 1.00 19.64 ? 1155 HOH A O 1 HETATM 9532 O O . HOH WA 10 . ? -50.192 32.294 44.076 1.00 33.94 ? 1156 HOH A O 1 HETATM 9533 O O . HOH WA 10 . ? -11.933 23.113 41.563 1.00 26.05 ? 1157 HOH A O 1 HETATM 9534 O O . HOH WA 10 . ? -49.501 21.848 16.974 1.00 16.26 ? 1158 HOH A O 1 HETATM 9535 O O . HOH WA 10 . ? -49.695 38.498 38.833 1.00 33.02 ? 1159 HOH A O 1 HETATM 9536 O O . HOH WA 10 . ? -15.478 31.647 23.804 1.00 33.06 ? 1160 HOH A O 1 HETATM 9537 O O . HOH WA 10 . ? -10.890 34.322 52.155 1.00 25.54 ? 1161 HOH A O 1 HETATM 9538 O O . HOH WA 10 . ? -43.466 30.821 57.520 1.00 29.82 ? 1162 HOH A O 1 HETATM 9539 O O . HOH WA 10 . ? -44.076 15.980 1.232 1.00 28.79 ? 1163 HOH A O 1 HETATM 9540 O O . HOH WA 10 . ? -14.447 6.608 19.789 1.00 38.13 ? 1164 HOH A O 1 HETATM 9541 O O . HOH WA 10 . ? -54.586 38.312 18.766 1.00 39.79 ? 1165 HOH A O 1 HETATM 9542 O O . HOH WA 10 . ? -52.960 28.200 48.829 1.00 25.23 ? 1166 HOH A O 1 HETATM 9543 O O . HOH WA 10 . ? -33.835 9.858 42.661 1.00 33.20 ? 1167 HOH A O 1 HETATM 9544 O O . HOH WA 10 . ? -48.541 51.921 17.093 1.00 29.57 ? 1168 HOH A O 1 HETATM 9545 O O . HOH WA 10 . ? -18.648 48.743 54.309 1.00 24.45 ? 1169 HOH A O 1 HETATM 9546 O O . HOH WA 10 . ? -13.733 28.136 39.594 1.00 27.78 ? 1170 HOH A O 1 HETATM 9547 O O . HOH WA 10 . ? -10.983 26.985 25.428 1.00 31.17 ? 1171 HOH A O 1 HETATM 9548 O O . HOH WA 10 . ? -58.904 32.695 40.402 1.00 38.08 ? 1172 HOH A O 1 HETATM 9549 O O . HOH WA 10 . ? -42.733 18.923 53.086 1.00 44.46 ? 1173 HOH A O 1 HETATM 9550 O O . HOH WA 10 . ? -12.153 45.403 41.229 1.00 37.45 ? 1174 HOH A O 1 HETATM 9551 O O . HOH WA 10 . ? -58.262 27.687 30.191 1.00 30.87 ? 1175 HOH A O 1 HETATM 9552 O O . HOH WA 10 . ? -55.030 29.413 26.926 1.00 32.09 ? 1176 HOH A O 1 HETATM 9553 O O . HOH WA 10 . ? -30.756 3.738 32.220 1.00 28.45 ? 1177 HOH A O 1 HETATM 9554 O O . HOH WA 10 . ? -36.863 30.044 4.411 1.00 37.88 ? 1178 HOH A O 1 HETATM 9555 O O . HOH WA 10 . ? -52.707 42.877 6.909 1.00 34.01 ? 1179 HOH A O 1 HETATM 9556 O O . HOH WA 10 . ? -45.774 27.986 31.922 1.00 25.29 ? 1180 HOH A O 1 HETATM 9557 O O . HOH WA 10 . ? -42.329 35.850 44.700 1.00 34.24 ? 1181 HOH A O 1 HETATM 9558 O O . HOH WA 10 . ? -33.885 52.944 31.959 1.00 32.98 ? 1182 HOH A O 1 HETATM 9559 O O . HOH WA 10 . ? -49.133 11.898 37.777 1.00 31.82 ? 1183 HOH A O 1 HETATM 9560 O O . HOH WA 10 . ? -15.629 41.422 11.837 1.00 23.97 ? 1184 HOH A O 1 HETATM 9561 O O . HOH WA 10 . ? -47.010 43.678 13.146 1.00 23.00 ? 1185 HOH A O 1 HETATM 9562 O O . HOH WA 10 . ? -58.733 22.775 37.033 1.00 28.78 ? 1186 HOH A O 1 HETATM 9563 O O . HOH WA 10 . ? -31.514 4.274 17.865 1.00 34.66 ? 1187 HOH A O 1 HETATM 9564 O O . HOH WA 10 . ? -57.457 25.411 25.666 1.00 35.79 ? 1188 HOH A O 1 HETATM 9565 O O . HOH WA 10 . ? -51.806 22.725 53.046 1.00 31.91 ? 1189 HOH A O 1 HETATM 9566 O O . HOH WA 10 . ? -53.489 16.577 14.292 1.00 28.34 ? 1190 HOH A O 1 HETATM 9567 O O . HOH WA 10 . ? -19.767 15.318 44.209 1.00 41.39 ? 1191 HOH A O 1 HETATM 9568 O O . HOH WA 10 . ? -57.396 38.779 7.562 1.00 42.17 ? 1192 HOH A O 1 HETATM 9569 O O . HOH WA 10 . ? -9.237 24.548 37.451 1.00 32.94 ? 1193 HOH A O 1 HETATM 9570 O O . HOH WA 10 . ? -5.200 28.176 33.894 1.00 26.06 ? 1194 HOH A O 1 HETATM 9571 O O . HOH WA 10 . ? -19.956 53.106 26.534 1.00 26.21 ? 1195 HOH A O 1 HETATM 9572 O O . HOH WA 10 . ? -27.740 -0.365 20.767 1.00 36.95 ? 1196 HOH A O 1 HETATM 9573 O O . HOH WA 10 . ? -50.601 23.258 55.385 1.00 39.25 ? 1197 HOH A O 1 HETATM 9574 O O . HOH WA 10 . ? -26.797 40.871 13.871 1.00 36.03 ? 1198 HOH A O 1 HETATM 9575 O O . HOH WA 10 . ? -44.743 8.650 39.776 1.00 29.61 ? 1199 HOH A O 1 HETATM 9576 O O . HOH WA 10 . ? -41.591 38.065 43.753 1.00 29.65 ? 1200 HOH A O 1 HETATM 9577 O O . HOH WA 10 . ? -49.374 31.828 4.931 1.00 26.42 ? 1201 HOH A O 1 HETATM 9578 O O . HOH WA 10 . ? -21.987 26.174 54.397 1.00 44.19 ? 1202 HOH A O 1 HETATM 9579 O O . HOH WA 10 . ? -10.998 34.277 48.264 1.00 37.83 ? 1203 HOH A O 1 HETATM 9580 O O . HOH WA 10 . ? -44.874 28.600 -0.381 1.00 40.28 ? 1204 HOH A O 1 HETATM 9581 O O . HOH WA 10 . ? -15.788 53.276 33.395 1.00 35.19 ? 1205 HOH A O 1 HETATM 9582 O O . HOH WA 10 . ? -34.818 3.195 31.973 1.00 50.54 ? 1206 HOH A O 1 HETATM 9583 O O . HOH WA 10 . ? -30.562 55.677 32.923 1.00 29.43 ? 1207 HOH A O 1 HETATM 9584 O O . HOH WA 10 . ? -11.990 20.863 10.671 1.00 28.23 ? 1208 HOH A O 1 HETATM 9585 O O . HOH WA 10 . ? -37.989 55.079 26.188 1.00 31.30 ? 1209 HOH A O 1 HETATM 9586 O O . HOH WA 10 . ? -14.691 47.517 30.294 1.00 21.29 ? 1210 HOH A O 1 HETATM 9587 O O . HOH WA 10 . ? -30.848 7.603 38.634 1.00 44.26 ? 1211 HOH A O 1 HETATM 9588 O O . HOH WA 10 . ? -47.251 31.830 49.387 1.00 29.66 ? 1212 HOH A O 1 HETATM 9589 O O . HOH WA 10 . ? -55.479 17.386 29.877 1.00 34.72 ? 1213 HOH A O 1 HETATM 9590 O O . HOH WA 10 . ? -18.351 19.691 36.570 1.00 29.11 ? 1214 HOH A O 1 HETATM 9591 O O . HOH WA 10 . ? -11.634 20.493 37.654 1.00 35.75 ? 1215 HOH A O 1 HETATM 9592 O O . HOH WA 10 . ? -19.873 22.683 4.887 1.00 37.33 ? 1216 HOH A O 1 HETATM 9593 O O . HOH WA 10 . ? -38.824 39.779 3.498 1.00 30.45 ? 1217 HOH A O 1 HETATM 9594 O O . HOH WA 10 . ? -19.122 41.536 57.889 1.00 38.61 ? 1218 HOH A O 1 HETATM 9595 O O . HOH WA 10 . ? -23.925 3.661 18.272 1.00 31.20 ? 1219 HOH A O 1 HETATM 9596 O O . HOH WA 10 . ? -58.204 38.340 11.627 1.00 42.22 ? 1220 HOH A O 1 HETATM 9597 O O . HOH WA 10 . ? -52.915 22.507 23.985 1.00 38.60 ? 1221 HOH A O 1 HETATM 9598 O O . HOH WA 10 . ? -36.380 25.622 -1.793 1.00 45.32 ? 1222 HOH A O 1 HETATM 9599 O O . HOH WA 10 . ? -11.615 35.570 45.879 1.00 36.49 ? 1223 HOH A O 1 HETATM 9600 O O . HOH WA 10 . ? -50.156 17.754 48.567 1.00 33.77 ? 1224 HOH A O 1 HETATM 9601 O O . HOH WA 10 . ? -16.792 45.909 41.182 1.00 34.27 ? 1225 HOH A O 1 HETATM 9602 O O . HOH WA 10 . ? -50.880 41.174 34.671 1.00 29.24 ? 1226 HOH A O 1 HETATM 9603 O O . HOH WA 10 . ? -34.267 30.870 0.298 1.00 34.71 ? 1227 HOH A O 1 HETATM 9604 O O . HOH WA 10 . ? -16.946 0.204 19.471 1.00 37.41 ? 1228 HOH A O 1 HETATM 9605 O O . HOH WA 10 . ? -46.163 41.446 37.350 1.00 41.26 ? 1229 HOH A O 1 HETATM 9606 O O . HOH WA 10 . ? -42.936 20.889 56.291 1.00 35.75 ? 1230 HOH A O 1 HETATM 9607 O O . HOH WA 10 . ? -37.455 39.851 47.005 1.00 36.20 ? 1231 HOH A O 1 HETATM 9608 O O . HOH WA 10 . ? -37.033 40.396 60.247 1.00 33.23 ? 1232 HOH A O 1 HETATM 9609 O O . HOH WA 10 . ? -27.205 36.578 6.689 1.00 26.75 ? 1233 HOH A O 1 HETATM 9610 O O . HOH WA 10 . ? -62.911 32.947 32.324 1.00 31.87 ? 1234 HOH A O 1 HETATM 9611 O O . HOH WA 10 . ? -18.451 14.967 14.066 1.00 30.43 ? 1235 HOH A O 1 HETATM 9612 O O . HOH WA 10 . ? -18.742 54.195 36.152 1.00 38.54 ? 1236 HOH A O 1 HETATM 9613 O O . HOH WA 10 . ? -50.507 20.435 55.429 1.00 43.95 ? 1237 HOH A O 1 HETATM 9614 O O . HOH WA 10 . ? -8.842 41.189 42.827 1.00 40.34 ? 1238 HOH A O 1 HETATM 9615 O O . HOH WA 10 . ? -49.685 22.708 -1.896 1.00 42.04 ? 1239 HOH A O 1 HETATM 9616 O O . HOH WA 10 . ? -32.574 44.434 50.360 1.00 35.69 ? 1240 HOH A O 1 HETATM 9617 O O . HOH WA 10 . ? -25.863 11.586 38.779 1.00 27.38 ? 1241 HOH A O 1 HETATM 9618 O O . HOH WA 10 . ? -38.588 55.927 14.256 1.00 31.35 ? 1242 HOH A O 1 HETATM 9619 O O . HOH WA 10 . ? -14.728 47.541 26.897 1.00 26.98 ? 1243 HOH A O 1 HETATM 9620 O O . HOH WA 10 . ? -38.288 28.614 59.174 1.00 44.87 ? 1244 HOH A O 1 HETATM 9621 O O . HOH WA 10 . ? -23.178 6.749 11.633 1.00 32.73 ? 1245 HOH A O 1 HETATM 9622 O O . HOH WA 10 . ? -36.371 2.341 21.679 1.00 31.46 ? 1246 HOH A O 1 HETATM 9623 O O . HOH WA 10 . ? -19.403 28.153 3.765 1.00 41.36 ? 1247 HOH A O 1 HETATM 9624 O O . HOH WA 10 . ? -37.332 22.388 56.338 1.00 34.64 ? 1248 HOH A O 1 HETATM 9625 O O . HOH WA 10 . ? -40.464 5.125 27.751 1.00 26.55 ? 1249 HOH A O 1 HETATM 9626 O O . HOH WA 10 . ? -39.795 56.103 21.095 1.00 34.05 ? 1250 HOH A O 1 HETATM 9627 O O . HOH WA 10 . ? -17.011 48.158 46.390 1.00 34.91 ? 1251 HOH A O 1 HETATM 9628 O O . HOH WA 10 . ? -55.812 30.556 18.734 1.00 37.99 ? 1252 HOH A O 1 HETATM 9629 O O . HOH WA 10 . ? -47.775 47.854 5.881 1.00 33.07 ? 1253 HOH A O 1 HETATM 9630 O O . HOH WA 10 . ? -12.058 17.574 35.245 1.00 47.63 ? 1254 HOH A O 1 HETATM 9631 O O . HOH WA 10 . ? -41.371 40.297 45.131 1.00 39.99 ? 1255 HOH A O 1 HETATM 9632 O O . HOH WA 10 . ? -34.797 9.162 8.603 1.00 41.10 ? 1256 HOH A O 1 HETATM 9633 O O . HOH WA 10 . ? -15.720 22.210 9.561 1.00 34.87 ? 1257 HOH A O 1 HETATM 9634 O O . HOH WA 10 . ? -27.876 50.656 40.437 1.00 35.19 ? 1258 HOH A O 1 HETATM 9635 O O . HOH WA 10 . ? -37.099 12.805 8.302 1.00 49.85 ? 1259 HOH A O 1 HETATM 9636 O O . HOH WA 10 . ? -38.059 11.373 41.781 1.00 35.23 ? 1260 HOH A O 1 HETATM 9637 O O . HOH WA 10 . ? -58.503 35.288 6.290 1.00 36.42 ? 1261 HOH A O 1 HETATM 9638 O O . HOH WA 10 . ? -28.007 38.196 4.591 1.00 43.35 ? 1262 HOH A O 1 HETATM 9639 O O . HOH WA 10 . ? -52.332 19.677 29.791 1.00 39.64 ? 1263 HOH A O 1 HETATM 9640 O O . HOH WA 10 . ? -18.187 51.689 45.736 1.00 51.27 ? 1264 HOH A O 1 HETATM 9641 O O . HOH WA 10 . ? -29.053 0.204 29.372 1.00 37.92 ? 1265 HOH A O 1 HETATM 9642 O O . HOH WA 10 . ? -5.896 12.791 26.444 1.00 29.26 ? 1266 HOH A O 1 HETATM 9643 O O . HOH WA 10 . ? -27.628 43.860 28.243 1.00 24.14 ? 1267 HOH A O 1 HETATM 9644 O O . HOH WA 10 . ? -29.944 50.868 38.816 1.00 29.51 ? 1268 HOH A O 1 HETATM 9645 O O . HOH WA 10 . ? -18.633 20.423 39.327 1.00 32.59 ? 1269 HOH A O 1 HETATM 9646 O O . HOH WA 10 . ? -31.417 40.372 32.942 1.00 34.42 ? 1270 HOH A O 1 HETATM 9647 O O . HOH WA 10 . ? -10.714 45.684 39.044 1.00 34.99 ? 1271 HOH A O 1 HETATM 9648 O O . HOH WA 10 . ? -28.828 33.457 22.213 1.00 28.04 ? 1272 HOH A O 1 HETATM 9649 O O . HOH WA 10 . ? -30.938 14.631 43.283 1.00 28.33 ? 1273 HOH A O 1 HETATM 9650 O O . HOH WA 10 . ? -34.699 24.242 56.953 1.00 37.88 ? 1274 HOH A O 1 HETATM 9651 O O . HOH WA 10 . ? -24.794 1.647 19.919 1.00 34.63 ? 1275 HOH A O 1 HETATM 9652 O O . HOH WA 10 . ? -18.258 -0.836 29.031 1.00 33.01 ? 1276 HOH A O 1 HETATM 9653 O O . HOH WA 10 . ? -54.856 31.765 21.865 1.00 33.75 ? 1277 HOH A O 1 HETATM 9654 O O . HOH WA 10 . ? -22.582 58.439 25.169 1.00 32.21 ? 1278 HOH A O 1 HETATM 9655 O O . HOH WA 10 . ? -47.536 26.658 57.071 1.00 29.29 ? 1279 HOH A O 1 HETATM 9656 O O . HOH WA 10 . ? -34.954 20.415 4.118 1.00 35.83 ? 1280 HOH A O 1 HETATM 9657 O O . HOH WA 10 . ? -14.501 50.289 30.863 1.00 34.08 ? 1281 HOH A O 1 HETATM 9658 O O . HOH WA 10 . ? -54.475 25.584 22.525 1.00 36.10 ? 1282 HOH A O 1 HETATM 9659 O O . HOH WA 10 . ? -53.037 34.294 43.096 1.00 40.86 ? 1283 HOH A O 1 HETATM 9660 O O . HOH WA 10 . ? -29.135 30.444 2.129 1.00 40.89 ? 1284 HOH A O 1 HETATM 9661 O O . HOH WA 10 . ? -17.225 55.751 33.746 1.00 38.54 ? 1285 HOH A O 1 HETATM 9662 O O . HOH WA 10 . ? -43.963 32.883 55.644 1.00 32.07 ? 1286 HOH A O 1 HETATM 9663 O O . HOH WA 10 . ? -18.558 27.403 47.401 1.00 43.72 ? 1287 HOH A O 1 HETATM 9664 O O . HOH WA 10 . ? -39.640 54.492 16.307 1.00 36.44 ? 1288 HOH A O 1 HETATM 9665 O O . HOH WA 10 . ? -27.059 43.123 30.580 1.00 25.73 ? 1289 HOH A O 1 HETATM 9666 O O . HOH WA 10 . ? -17.534 10.865 14.460 1.00 36.84 ? 1290 HOH A O 1 HETATM 9667 O O . HOH WA 10 . ? -34.701 -3.133 24.286 1.00 30.13 ? 1291 HOH A O 1 HETATM 9668 O O . HOH WA 10 . ? -26.080 47.665 47.903 1.00 30.79 ? 1292 HOH A O 1 HETATM 9669 O O . HOH WA 10 . ? -49.393 45.063 5.143 1.00 40.13 ? 1293 HOH A O 1 HETATM 9670 O O . HOH WA 10 . ? -8.582 25.625 25.112 1.00 25.97 ? 1294 HOH A O 1 HETATM 9671 O O . HOH WA 10 . ? -50.545 36.991 3.231 1.00 39.67 ? 1295 HOH A O 1 HETATM 9672 O O . HOH WA 10 . ? -16.084 37.654 58.843 1.00 29.55 ? 1296 HOH A O 1 HETATM 9673 O O . HOH WA 10 . ? -34.434 49.523 56.365 1.00 42.65 ? 1297 HOH A O 1 HETATM 9674 O O . HOH WA 10 . ? -38.144 36.247 0.939 1.00 39.04 ? 1298 HOH A O 1 HETATM 9675 O O . HOH WA 10 . ? -45.261 44.193 0.158 1.00 30.06 ? 1299 HOH A O 1 HETATM 9676 O O . HOH WA 10 . ? -23.652 38.230 64.183 1.00 37.78 ? 1300 HOH A O 1 HETATM 9677 O O . HOH WA 10 . ? -16.153 5.013 18.306 1.00 39.12 ? 1301 HOH A O 1 HETATM 9678 O O . HOH WA 10 . ? -18.181 -3.276 26.179 1.00 32.64 ? 1302 HOH A O 1 HETATM 9679 O O . HOH WA 10 . ? -19.149 18.150 10.771 1.00 42.39 ? 1303 HOH A O 1 HETATM 9680 O O . HOH WA 10 . ? -34.584 7.067 6.908 1.00 50.77 ? 1304 HOH A O 1 HETATM 9681 O O . HOH WA 10 . ? -25.275 53.041 11.824 1.00 42.25 ? 1305 HOH A O 1 HETATM 9682 O O . HOH WA 10 . ? -44.980 7.396 14.711 1.00 29.15 ? 1306 HOH A O 1 HETATM 9683 O O . HOH WA 10 . ? -13.746 43.490 13.484 1.00 41.97 ? 1307 HOH A O 1 HETATM 9684 O O . HOH WA 10 . ? -13.618 31.050 62.778 1.00 47.56 ? 1308 HOH A O 1 HETATM 9685 O O . HOH WA 10 . ? -33.430 23.733 53.004 1.00 54.54 ? 1309 HOH A O 1 HETATM 9686 O O . HOH WA 10 . ? -13.154 12.013 33.184 1.00 33.40 ? 1310 HOH A O 1 HETATM 9687 O O . HOH WA 10 . ? -38.460 31.354 -5.963 1.00 50.19 ? 1311 HOH A O 1 HETATM 9688 O O . HOH WA 10 . ? -14.440 44.936 10.608 1.00 41.10 ? 1312 HOH A O 1 HETATM 9689 O O . HOH WA 10 . ? -29.109 47.446 45.250 1.00 28.46 ? 1313 HOH A O 1 HETATM 9690 O O . HOH WA 10 . ? -55.485 19.747 47.402 1.00 34.15 ? 1314 HOH A O 1 HETATM 9691 O O . HOH WA 10 . ? -36.357 10.792 14.405 1.00 48.49 ? 1315 HOH A O 1 HETATM 9692 O O . HOH WA 10 . ? -11.044 38.996 20.355 1.00 26.71 ? 1316 HOH A O 1 HETATM 9693 O O . HOH WA 10 . ? -52.036 25.504 -0.726 1.00 47.88 ? 1317 HOH A O 1 HETATM 9694 O O . HOH WA 10 . ? -59.724 27.939 14.052 1.00 23.75 ? 1318 HOH A O 1 HETATM 9695 O O . HOH WA 10 . ? -46.245 40.205 1.119 1.00 31.00 ? 1319 HOH A O 1 HETATM 9696 O O . HOH WA 10 . ? -11.600 14.691 34.560 1.00 36.98 ? 1320 HOH A O 1 HETATM 9697 O O . HOH WA 10 . ? -11.053 9.796 23.306 1.00 38.81 ? 1321 HOH A O 1 HETATM 9698 O O . HOH WA 10 . ? -11.459 11.363 17.110 1.00 49.76 ? 1322 HOH A O 1 HETATM 9699 O O . HOH WA 10 . ? -37.774 31.791 -1.423 1.00 40.32 ? 1323 HOH A O 1 HETATM 9700 O O . HOH WA 10 . ? -9.211 49.738 37.668 1.00 43.61 ? 1324 HOH A O 1 HETATM 9701 O O . HOH WA 10 . ? -23.911 34.549 4.979 1.00 49.20 ? 1325 HOH A O 1 HETATM 9702 O O . HOH WA 10 . ? -24.603 17.320 43.483 1.00 35.37 ? 1326 HOH A O 1 HETATM 9703 O O . HOH WA 10 . ? -25.089 49.719 60.205 1.00 42.32 ? 1327 HOH A O 1 HETATM 9704 O O . HOH WA 10 . ? -33.927 -1.245 28.802 1.00 52.34 ? 1328 HOH A O 1 HETATM 9705 O O . HOH WA 10 . ? -11.838 32.456 6.030 1.00 34.07 ? 1329 HOH A O 1 HETATM 9706 O O . HOH WA 10 . ? -18.188 34.141 19.567 1.00 49.61 ? 1330 HOH A O 1 HETATM 9707 O O . HOH WA 10 . ? -21.089 26.177 51.335 1.00 37.85 ? 1331 HOH A O 1 HETATM 9708 O O . HOH WA 10 . ? -33.162 50.952 2.142 1.00 42.03 ? 1332 HOH A O 1 HETATM 9709 O O . HOH WA 10 . ? -47.584 48.161 10.579 1.00 40.59 ? 1333 HOH A O 1 HETATM 9710 O O . HOH WA 10 . ? -36.738 31.491 1.746 1.00 44.11 ? 1334 HOH A O 1 HETATM 9711 O O . HOH WA 10 . ? -42.015 51.219 33.341 1.00 39.65 ? 1335 HOH A O 1 HETATM 9712 O O . HOH WA 10 . ? -32.749 54.838 11.016 1.00 26.87 ? 1336 HOH A O 1 HETATM 9713 O O . HOH WA 10 . ? -29.001 43.424 12.684 1.00 36.10 ? 1337 HOH A O 1 HETATM 9714 O O . HOH WA 10 . ? -17.350 52.649 27.194 1.00 33.69 ? 1338 HOH A O 1 HETATM 9715 O O . HOH WA 10 . ? -44.764 19.270 27.297 1.00 37.49 ? 1339 HOH A O 1 HETATM 9716 O O . HOH WA 10 . ? -47.016 6.365 16.814 1.00 28.28 ? 1340 HOH A O 1 HETATM 9717 O O . HOH WA 10 . ? -46.098 47.061 0.017 1.00 38.76 ? 1341 HOH A O 1 HETATM 9718 O O . HOH WA 10 . ? -55.778 19.403 32.190 1.00 31.52 ? 1342 HOH A O 1 HETATM 9719 O O . HOH WA 10 . ? -22.075 18.942 44.232 1.00 37.44 ? 1343 HOH A O 1 HETATM 9720 O O . HOH WA 10 . ? -10.402 37.766 11.355 1.00 38.56 ? 1344 HOH A O 1 HETATM 9721 O O . HOH WA 10 . ? -48.953 8.295 26.200 1.00 53.06 ? 1345 HOH A O 1 HETATM 9722 O O . HOH WA 10 . ? -27.031 26.562 1.716 1.00 27.65 ? 1346 HOH A O 1 HETATM 9723 O O . HOH WA 10 . ? -11.644 26.042 43.070 1.00 43.34 ? 1347 HOH A O 1 HETATM 9724 O O . HOH WA 10 . ? -22.165 42.400 60.265 1.00 37.82 ? 1348 HOH A O 1 HETATM 9725 O O . HOH WA 10 . ? -46.776 32.871 54.992 1.00 44.09 ? 1349 HOH A O 1 HETATM 9726 O O . HOH WA 10 . ? -45.605 14.729 6.247 1.00 47.51 ? 1350 HOH A O 1 HETATM 9727 O O . HOH WA 10 . ? -39.349 13.420 47.778 1.00 32.73 ? 1351 HOH A O 1 HETATM 9728 O O . HOH WA 10 . ? -37.581 2.713 29.934 1.00 38.17 ? 1352 HOH A O 1 HETATM 9729 O O . HOH WA 10 . ? -42.114 6.232 33.636 1.00 43.39 ? 1353 HOH A O 1 HETATM 9730 O O . HOH WA 10 . ? -41.471 9.589 8.010 1.00 39.18 ? 1354 HOH A O 1 HETATM 9731 O O . HOH WA 10 . ? -26.677 53.591 41.117 1.00 43.67 ? 1355 HOH A O 1 HETATM 9732 O O . HOH WA 10 . ? -41.529 34.237 57.073 1.00 36.18 ? 1356 HOH A O 1 HETATM 9733 O O . HOH WA 10 . ? -24.937 41.339 24.581 1.00 39.07 ? 1357 HOH A O 1 HETATM 9734 O O . HOH WA 10 . ? -48.248 21.419 4.980 1.00 47.02 ? 1358 HOH A O 1 HETATM 9735 O O . HOH WA 10 . ? -61.986 19.136 41.729 1.00 36.07 ? 1359 HOH A O 1 HETATM 9736 O O . HOH WA 10 . ? -47.281 26.268 -2.085 1.00 45.47 ? 1360 HOH A O 1 HETATM 9737 O O . HOH WA 10 . ? -31.141 50.298 35.141 1.00 27.41 ? 1361 HOH A O 1 HETATM 9738 O O . HOH WA 10 . ? -45.368 10.169 30.306 1.00 35.23 ? 1362 HOH A O 1 HETATM 9739 O O . HOH WA 10 . ? -21.025 18.761 37.294 1.00 45.81 ? 1363 HOH A O 1 HETATM 9740 O O . HOH WA 10 . ? -51.626 31.105 3.901 1.00 47.85 ? 1364 HOH A O 1 HETATM 9741 O O . HOH WA 10 . ? -57.331 28.239 50.864 1.00 41.68 ? 1365 HOH A O 1 HETATM 9742 O O . HOH WA 10 . ? -50.575 24.973 16.625 1.00 51.03 ? 1366 HOH A O 1 HETATM 9743 O O . HOH WA 10 . ? -10.184 28.907 27.311 1.00 37.64 ? 1367 HOH A O 1 HETATM 9744 O O . HOH WA 10 . ? -35.977 20.653 1.549 1.00 33.67 ? 1368 HOH A O 1 HETATM 9745 O O . HOH WA 10 . ? -48.754 31.364 56.094 1.00 34.98 ? 1369 HOH A O 1 HETATM 9746 O O . HOH WA 10 . ? -31.947 39.567 3.607 1.00 44.73 ? 1370 HOH A O 1 HETATM 9747 O O . HOH WA 10 . ? -47.673 14.614 11.439 1.00 62.31 ? 1371 HOH A O 1 HETATM 9748 O O . HOH WA 10 . ? -26.869 45.208 64.415 1.00 39.29 ? 1372 HOH A O 1 HETATM 9749 O O . HOH WA 10 . ? -25.731 48.335 63.225 1.00 45.44 ? 1373 HOH A O 1 HETATM 9750 O O . HOH WA 10 . ? -51.113 17.913 27.002 1.00 40.66 ? 1374 HOH A O 1 HETATM 9751 O O . HOH WA 10 . ? -54.896 33.985 19.841 1.00 45.35 ? 1375 HOH A O 1 HETATM 9752 O O . HOH WA 10 . ? -23.121 55.215 41.702 1.00 35.87 ? 1376 HOH A O 1 HETATM 9753 O O . HOH WA 10 . ? -37.654 41.652 54.086 1.00 39.27 ? 1377 HOH A O 1 HETATM 9754 O O . HOH WA 10 . ? -32.134 37.961 64.190 1.00 47.29 ? 1378 HOH A O 1 HETATM 9755 O O . HOH WA 10 . ? -56.015 29.354 22.679 1.00 33.23 ? 1379 HOH A O 1 HETATM 9756 O O . HOH WA 10 . ? -48.604 38.928 41.364 1.00 43.13 ? 1380 HOH A O 1 HETATM 9757 O O . HOH WA 10 . ? -25.263 17.276 5.322 1.00 42.57 ? 1381 HOH A O 1 HETATM 9758 O O . HOH WA 10 . ? -48.526 21.305 57.148 1.00 50.82 ? 1382 HOH A O 1 HETATM 9759 O O . HOH WA 10 . ? -28.860 55.293 15.680 1.00 41.94 ? 1383 HOH A O 1 HETATM 9760 O O . HOH WA 10 . ? -16.246 47.937 24.915 1.00 29.15 ? 1384 HOH A O 1 HETATM 9761 O O . HOH WA 10 . ? -58.202 37.970 36.916 1.00 43.38 ? 1385 HOH A O 1 HETATM 9762 O O . HOH WA 10 . ? -42.082 23.147 57.488 1.00 38.00 ? 1386 HOH A O 1 HETATM 9763 O O . HOH WA 10 . ? -16.821 35.507 61.664 1.00 46.81 ? 1387 HOH A O 1 HETATM 9764 O O . HOH WA 10 . ? -10.259 23.803 31.664 1.00 20.37 ? 1388 HOH A O 1 HETATM 9765 O O . HOH WA 10 . ? -36.361 28.863 8.770 1.00 43.63 ? 1389 HOH A O 1 HETATM 9766 O O . HOH WA 10 . ? -35.304 17.083 51.832 1.00 35.40 ? 1390 HOH A O 1 HETATM 9767 O O . HOH WA 10 . ? -47.486 19.124 2.145 1.00 24.35 ? 1391 HOH A O 1 HETATM 9768 O O . HOH WA 10 . ? -22.410 17.594 40.098 1.00 36.25 ? 1392 HOH A O 1 HETATM 9769 O O . HOH WA 10 . ? -31.054 44.083 29.845 1.00 29.47 ? 1393 HOH A O 1 HETATM 9770 O O . HOH WA 10 . ? -31.330 20.805 5.359 1.00 30.21 ? 1394 HOH A O 1 HETATM 9771 O O . HOH WA 10 . ? -9.257 26.383 44.830 1.00 34.68 ? 1395 HOH A O 1 HETATM 9772 O O . HOH WA 10 . ? -33.071 46.947 50.831 1.00 41.84 ? 1396 HOH A O 1 HETATM 9773 O O . HOH WA 10 . ? -34.975 38.553 63.726 1.00 41.49 ? 1397 HOH A O 1 HETATM 9774 O O . HOH WA 10 . ? -40.518 19.450 -1.928 1.00 45.01 ? 1398 HOH A O 1 HETATM 9775 O O . HOH WA 10 . ? -51.769 46.901 6.567 1.00 34.27 ? 1399 HOH A O 1 HETATM 9776 O O . HOH WA 10 . ? -19.914 18.133 42.807 1.00 40.54 ? 1400 HOH A O 1 HETATM 9777 O O . HOH WA 10 . ? -45.465 34.553 5.404 1.00 30.46 ? 1401 HOH A O 1 HETATM 9778 O O . HOH XA 10 . ? 20.639 32.466 38.107 1.00 8.38 ? 801 HOH B O 1 HETATM 9779 O O . HOH XA 10 . ? 22.698 34.326 38.917 1.00 7.06 ? 802 HOH B O 1 HETATM 9780 O O . HOH XA 10 . ? 23.031 40.270 31.858 1.00 11.55 ? 803 HOH B O 1 HETATM 9781 O O . HOH XA 10 . ? 32.100 37.076 33.501 1.00 13.91 ? 804 HOH B O 1 HETATM 9782 O O . HOH XA 10 . ? -0.385 32.313 34.780 1.00 12.49 ? 805 HOH B O 1 HETATM 9783 O O . HOH XA 10 . ? 20.319 17.819 33.978 1.00 10.74 ? 806 HOH B O 1 HETATM 9784 O O . HOH XA 10 . ? 7.013 40.733 29.766 1.00 10.01 ? 807 HOH B O 1 HETATM 9785 O O . HOH XA 10 . ? 10.406 23.161 18.065 1.00 11.97 ? 808 HOH B O 1 HETATM 9786 O O . HOH XA 10 . ? 25.598 32.025 42.474 1.00 16.00 ? 809 HOH B O 1 HETATM 9787 O O . HOH XA 10 . ? 29.211 39.956 39.132 1.00 10.46 ? 810 HOH B O 1 HETATM 9788 O O . HOH XA 10 . ? -2.149 28.720 31.432 1.00 12.18 ? 811 HOH B O 1 HETATM 9789 O O . HOH XA 10 . ? 0.403 12.772 25.098 1.00 14.32 ? 812 HOH B O 1 HETATM 9790 O O . HOH XA 10 . ? 2.168 25.590 14.590 1.00 10.05 ? 813 HOH B O 1 HETATM 9791 O O . HOH XA 10 . ? 24.970 30.235 40.635 1.00 11.03 ? 814 HOH B O 1 HETATM 9792 O O . HOH XA 10 . ? 14.344 20.604 20.259 1.00 8.29 ? 815 HOH B O 1 HETATM 9793 O O . HOH XA 10 . ? 23.318 34.423 41.498 1.00 9.48 ? 816 HOH B O 1 HETATM 9794 O O . HOH XA 10 . ? 5.948 36.117 39.109 1.00 10.39 ? 817 HOH B O 1 HETATM 9795 O O . HOH XA 10 . ? 0.962 21.496 24.760 1.00 13.40 ? 818 HOH B O 1 HETATM 9796 O O . HOH XA 10 . ? -0.729 21.806 42.532 1.00 13.46 ? 819 HOH B O 1 HETATM 9797 O O . HOH XA 10 . ? 15.777 9.712 15.510 1.00 9.37 ? 820 HOH B O 1 HETATM 9798 O O . HOH XA 10 . ? 1.562 27.421 42.509 1.00 16.36 ? 821 HOH B O 1 HETATM 9799 O O . HOH XA 10 . ? 23.150 21.656 36.828 1.00 14.42 ? 822 HOH B O 1 HETATM 9800 O O . HOH XA 10 . ? 1.300 26.243 47.377 1.00 21.48 ? 823 HOH B O 1 HETATM 9801 O O . HOH XA 10 . ? 21.974 36.172 43.251 1.00 13.14 ? 824 HOH B O 1 HETATM 9802 O O . HOH XA 10 . ? 36.276 42.367 21.849 1.00 47.94 ? 825 HOH B O 1 HETATM 9803 O O . HOH XA 10 . ? -2.240 34.958 17.230 1.00 13.01 ? 826 HOH B O 1 HETATM 9804 O O . HOH XA 10 . ? -1.058 22.828 27.605 1.00 11.94 ? 827 HOH B O 1 HETATM 9805 O O . HOH XA 10 . ? 4.217 37.306 37.537 1.00 12.01 ? 828 HOH B O 1 HETATM 9806 O O . HOH XA 10 . ? -1.510 43.470 27.392 1.00 11.21 ? 829 HOH B O 1 HETATM 9807 O O . HOH XA 10 . ? 18.894 46.183 33.790 1.00 13.29 ? 830 HOH B O 1 HETATM 9808 O O . HOH XA 10 . ? 20.437 34.344 26.013 1.00 10.10 ? 831 HOH B O 1 HETATM 9809 O O . HOH XA 10 . ? 30.205 13.069 30.997 1.00 17.26 ? 832 HOH B O 1 HETATM 9810 O O . HOH XA 10 . ? 10.468 12.228 28.026 1.00 24.02 ? 833 HOH B O 1 HETATM 9811 O O . HOH XA 10 . ? 0.321 34.286 45.362 1.00 19.94 ? 834 HOH B O 1 HETATM 9812 O O . HOH XA 10 . ? 25.153 40.617 5.493 1.00 18.41 ? 835 HOH B O 1 HETATM 9813 O O . HOH XA 10 . ? 37.240 27.014 38.973 1.00 18.13 ? 836 HOH B O 1 HETATM 9814 O O . HOH XA 10 . ? 3.334 23.274 15.311 1.00 14.79 ? 837 HOH B O 1 HETATM 9815 O O . HOH XA 10 . ? 17.813 32.197 10.232 1.00 11.95 ? 838 HOH B O 1 HETATM 9816 O O . HOH XA 10 . ? 26.001 39.369 24.822 1.00 14.94 ? 839 HOH B O 1 HETATM 9817 O O . HOH XA 10 . ? 0.771 42.685 30.048 1.00 11.71 ? 840 HOH B O 1 HETATM 9818 O O . HOH XA 10 . ? -9.363 35.960 34.640 1.00 21.86 ? 841 HOH B O 1 HETATM 9819 O O . HOH XA 10 . ? 7.598 35.766 37.007 1.00 8.78 ? 842 HOH B O 1 HETATM 9820 O O . HOH XA 10 . ? 5.799 30.207 48.287 1.00 13.66 ? 843 HOH B O 1 HETATM 9821 O O . HOH XA 10 . ? 8.887 11.486 23.727 1.00 12.20 ? 844 HOH B O 1 HETATM 9822 O O . HOH XA 10 . ? -8.882 44.185 32.286 1.00 22.76 ? 845 HOH B O 1 HETATM 9823 O O . HOH XA 10 . ? 19.643 41.440 47.614 1.00 17.49 ? 846 HOH B O 1 HETATM 9824 O O . HOH XA 10 . ? 19.212 19.104 5.677 1.00 19.78 ? 847 HOH B O 1 HETATM 9825 O O . HOH XA 10 . ? 28.123 22.562 11.469 1.00 11.97 ? 848 HOH B O 1 HETATM 9826 O O . HOH XA 10 . ? 26.140 27.961 46.549 1.00 23.67 ? 849 HOH B O 1 HETATM 9827 O O . HOH XA 10 . ? 7.988 18.139 27.327 1.00 12.75 ? 850 HOH B O 1 HETATM 9828 O O . HOH XA 10 . ? 23.426 44.371 29.262 1.00 22.38 ? 851 HOH B O 1 HETATM 9829 O O . HOH XA 10 . ? 17.380 32.207 38.011 1.00 21.13 ? 852 HOH B O 1 HETATM 9830 O O . HOH XA 10 . ? 9.530 12.250 18.065 1.00 15.38 ? 853 HOH B O 1 HETATM 9831 O O . HOH XA 10 . ? 6.698 8.669 23.071 1.00 13.50 ? 854 HOH B O 1 HETATM 9832 O O . HOH XA 10 . ? 28.216 29.385 45.850 1.00 20.35 ? 855 HOH B O 1 HETATM 9833 O O . HOH XA 10 . ? 35.864 33.321 6.591 1.00 42.54 ? 856 HOH B O 1 HETATM 9834 O O . HOH XA 10 . ? 3.192 24.846 11.323 1.00 13.33 ? 857 HOH B O 1 HETATM 9835 O O . HOH XA 10 . ? 0.473 45.374 19.574 1.00 19.54 ? 858 HOH B O 1 HETATM 9836 O O . HOH XA 10 . ? 6.959 14.444 24.450 1.00 20.92 ? 859 HOH B O 1 HETATM 9837 O O . HOH XA 10 . ? 32.194 24.995 14.860 1.00 16.10 ? 860 HOH B O 1 HETATM 9838 O O . HOH XA 10 . ? 3.743 9.407 20.062 1.00 18.27 ? 861 HOH B O 1 HETATM 9839 O O . HOH XA 10 . ? 0.957 26.406 16.869 1.00 15.58 ? 862 HOH B O 1 HETATM 9840 O O . HOH XA 10 . ? 10.795 39.522 34.049 1.00 10.41 ? 863 HOH B O 1 HETATM 9841 O O . HOH XA 10 . ? -5.226 34.036 8.804 1.00 22.28 ? 864 HOH B O 1 HETATM 9842 O O . HOH XA 10 . ? 6.208 36.857 41.603 1.00 14.20 ? 865 HOH B O 1 HETATM 9843 O O . HOH XA 10 . ? 25.363 40.554 39.685 1.00 15.06 ? 866 HOH B O 1 HETATM 9844 O O . HOH XA 10 . ? -3.859 24.946 38.474 1.00 20.08 ? 867 HOH B O 1 HETATM 9845 O O . HOH XA 10 . ? 18.162 12.917 28.669 1.00 16.85 ? 868 HOH B O 1 HETATM 9846 O O . HOH XA 10 . ? 17.060 13.707 10.652 1.00 19.05 ? 869 HOH B O 1 HETATM 9847 O O . HOH XA 10 . ? 4.000 38.585 10.705 1.00 16.24 ? 870 HOH B O 1 HETATM 9848 O O . HOH XA 10 . ? -1.588 41.212 29.805 1.00 10.03 ? 871 HOH B O 1 HETATM 9849 O O . HOH XA 10 . ? 11.401 17.566 35.939 1.00 20.80 ? 872 HOH B O 1 HETATM 9850 O O . HOH XA 10 . ? 13.876 3.176 17.527 1.00 23.07 ? 873 HOH B O 1 HETATM 9851 O O . HOH XA 10 . ? 27.070 20.756 14.932 1.00 14.68 ? 874 HOH B O 1 HETATM 9852 O O . HOH XA 10 . ? -4.899 34.165 25.169 1.00 15.20 ? 875 HOH B O 1 HETATM 9853 O O . HOH XA 10 . ? 22.953 32.022 23.364 1.00 20.12 ? 876 HOH B O 1 HETATM 9854 O O . HOH XA 10 . ? 29.343 25.016 14.450 1.00 15.37 ? 877 HOH B O 1 HETATM 9855 O O . HOH XA 10 . ? 31.613 22.297 14.908 1.00 18.46 ? 878 HOH B O 1 HETATM 9856 O O . HOH XA 10 . ? 24.830 38.840 49.048 1.00 16.86 ? 879 HOH B O 1 HETATM 9857 O O . HOH XA 10 . ? 28.814 46.480 30.450 1.00 22.58 ? 880 HOH B O 1 HETATM 9858 O O . HOH XA 10 . ? 23.319 41.423 38.206 1.00 14.62 ? 881 HOH B O 1 HETATM 9859 O O . HOH XA 10 . ? 5.029 23.259 13.067 1.00 14.57 ? 882 HOH B O 1 HETATM 9860 O O . HOH XA 10 . ? 24.102 42.038 25.589 1.00 14.67 ? 883 HOH B O 1 HETATM 9861 O O . HOH XA 10 . ? -0.592 35.161 19.367 1.00 14.35 ? 884 HOH B O 1 HETATM 9862 O O . HOH XA 10 . ? 21.326 31.457 17.388 1.00 12.73 ? 885 HOH B O 1 HETATM 9863 O O . HOH XA 10 . ? 31.502 24.562 41.204 1.00 20.42 ? 886 HOH B O 1 HETATM 9864 O O . HOH XA 10 . ? 26.822 29.643 43.473 1.00 13.74 ? 887 HOH B O 1 HETATM 9865 O O . HOH XA 10 . ? 13.936 7.475 14.335 1.00 13.21 ? 888 HOH B O 1 HETATM 9866 O O . HOH XA 10 . ? 7.027 25.437 10.018 1.00 14.48 ? 889 HOH B O 1 HETATM 9867 O O . HOH XA 10 . ? -1.475 24.751 17.527 1.00 17.52 ? 890 HOH B O 1 HETATM 9868 O O . HOH XA 10 . ? -6.485 18.766 35.207 1.00 16.75 ? 891 HOH B O 1 HETATM 9869 O O . HOH XA 10 . ? 13.854 23.702 20.129 1.00 15.51 ? 892 HOH B O 1 HETATM 9870 O O . HOH XA 10 . ? 7.961 27.530 8.813 1.00 17.90 ? 893 HOH B O 1 HETATM 9871 O O . HOH XA 10 . ? 21.666 7.655 26.225 1.00 22.38 ? 894 HOH B O 1 HETATM 9872 O O . HOH XA 10 . ? 23.814 40.302 27.542 1.00 15.81 ? 895 HOH B O 1 HETATM 9873 O O . HOH XA 10 . ? 24.209 28.538 23.652 1.00 14.77 ? 896 HOH B O 1 HETATM 9874 O O . HOH XA 10 . ? -1.971 38.576 30.413 1.00 14.47 ? 897 HOH B O 1 HETATM 9875 O O . HOH XA 10 . ? 39.373 30.066 32.594 1.00 13.27 ? 898 HOH B O 1 HETATM 9876 O O . HOH XA 10 . ? 15.860 36.711 5.494 1.00 10.92 ? 899 HOH B O 1 HETATM 9877 O O . HOH XA 10 . ? 41.398 34.051 43.014 1.00 27.25 ? 900 HOH B O 1 HETATM 9878 O O . HOH XA 10 . ? -2.438 22.846 39.417 1.00 21.96 ? 901 HOH B O 1 HETATM 9879 O O . HOH XA 10 . ? 14.410 33.794 -0.847 1.00 29.36 ? 902 HOH B O 1 HETATM 9880 O O . HOH XA 10 . ? 31.364 12.947 13.553 1.00 14.53 ? 903 HOH B O 1 HETATM 9881 O O . HOH XA 10 . ? 3.202 14.675 41.467 1.00 19.47 ? 904 HOH B O 1 HETATM 9882 O O . HOH XA 10 . ? 35.279 42.816 28.205 1.00 21.83 ? 905 HOH B O 1 HETATM 9883 O O . HOH XA 10 . ? -1.801 28.516 7.438 1.00 13.55 ? 906 HOH B O 1 HETATM 9884 O O . HOH XA 10 . ? 34.953 28.144 22.323 1.00 23.13 ? 907 HOH B O 1 HETATM 9885 O O . HOH XA 10 . ? 1.362 21.752 52.690 1.00 22.33 ? 908 HOH B O 1 HETATM 9886 O O . HOH XA 10 . ? 23.738 52.815 22.564 1.00 22.89 ? 909 HOH B O 1 HETATM 9887 O O . HOH XA 10 . ? -12.614 41.467 26.494 1.00 21.80 ? 910 HOH B O 1 HETATM 9888 O O . HOH XA 10 . ? 16.013 8.398 34.217 1.00 21.78 ? 911 HOH B O 1 HETATM 9889 O O . HOH XA 10 . ? 4.854 22.517 7.584 1.00 22.89 ? 912 HOH B O 1 HETATM 9890 O O . HOH XA 10 . ? -3.478 22.979 42.204 1.00 21.88 ? 913 HOH B O 1 HETATM 9891 O O . HOH XA 10 . ? -3.268 15.163 41.418 1.00 20.00 ? 914 HOH B O 1 HETATM 9892 O O . HOH XA 10 . ? 19.882 34.931 31.472 1.00 17.89 ? 915 HOH B O 1 HETATM 9893 O O . HOH XA 10 . ? 19.388 28.329 7.226 1.00 17.82 ? 916 HOH B O 1 HETATM 9894 O O . HOH XA 10 . ? 19.934 4.756 20.033 1.00 16.54 ? 917 HOH B O 1 HETATM 9895 O O . HOH XA 10 . ? 16.410 40.706 35.814 1.00 11.93 ? 918 HOH B O 1 HETATM 9896 O O . HOH XA 10 . ? 3.690 6.961 24.055 1.00 20.94 ? 919 HOH B O 1 HETATM 9897 O O . HOH XA 10 . ? 32.928 45.511 36.884 1.00 18.95 ? 920 HOH B O 1 HETATM 9898 O O . HOH XA 10 . ? 17.399 49.434 40.374 1.00 17.55 ? 921 HOH B O 1 HETATM 9899 O O . HOH XA 10 . ? 10.925 38.038 9.154 1.00 19.17 ? 922 HOH B O 1 HETATM 9900 O O . HOH XA 10 . ? 28.931 15.918 2.092 1.00 17.40 ? 923 HOH B O 1 HETATM 9901 O O . HOH XA 10 . ? 29.200 34.448 27.116 1.00 15.62 ? 924 HOH B O 1 HETATM 9902 O O . HOH XA 10 . ? 31.765 31.424 25.284 1.00 20.59 ? 925 HOH B O 1 HETATM 9903 O O . HOH XA 10 . ? 6.445 55.728 18.239 1.00 36.29 ? 926 HOH B O 1 HETATM 9904 O O . HOH XA 10 . ? 2.546 15.602 57.023 1.00 21.18 ? 927 HOH B O 1 HETATM 9905 O O . HOH XA 10 . ? 7.581 13.394 54.187 1.00 24.80 ? 928 HOH B O 1 HETATM 9906 O O . HOH XA 10 . ? 21.689 40.870 2.641 1.00 25.82 ? 929 HOH B O 1 HETATM 9907 O O . HOH XA 10 . ? 1.907 47.561 19.109 1.00 19.70 ? 930 HOH B O 1 HETATM 9908 O O . HOH XA 10 . ? 11.412 41.958 49.134 1.00 21.94 ? 931 HOH B O 1 HETATM 9909 O O . HOH XA 10 . ? 27.624 22.999 42.856 1.00 24.61 ? 932 HOH B O 1 HETATM 9910 O O . HOH XA 10 . ? -2.137 15.314 26.720 1.00 14.24 ? 933 HOH B O 1 HETATM 9911 O O . HOH XA 10 . ? 8.572 31.722 61.683 1.00 27.38 ? 934 HOH B O 1 HETATM 9912 O O . HOH XA 10 . ? 12.920 55.433 32.321 1.00 32.85 ? 935 HOH B O 1 HETATM 9913 O O . HOH XA 10 . ? 29.924 44.290 11.374 1.00 39.61 ? 936 HOH B O 1 HETATM 9914 O O . HOH XA 10 . ? 29.464 35.326 19.108 1.00 24.07 ? 937 HOH B O 1 HETATM 9915 O O . HOH XA 10 . ? -6.678 31.015 35.654 1.00 20.23 ? 938 HOH B O 1 HETATM 9916 O O . HOH XA 10 . ? 16.815 21.918 6.252 1.00 21.53 ? 939 HOH B O 1 HETATM 9917 O O . HOH XA 10 . ? 0.724 30.381 25.167 1.00 15.14 ? 940 HOH B O 1 HETATM 9918 O O . HOH XA 10 . ? -3.387 42.749 25.447 1.00 17.38 ? 941 HOH B O 1 HETATM 9919 O O . HOH XA 10 . ? 5.082 43.063 36.901 1.00 18.40 ? 942 HOH B O 1 HETATM 9920 O O . HOH XA 10 . ? 16.251 9.557 56.826 1.00 42.25 ? 943 HOH B O 1 HETATM 9921 O O . HOH XA 10 . ? 27.149 36.686 4.681 1.00 15.89 ? 944 HOH B O 1 HETATM 9922 O O . HOH XA 10 . ? 27.933 8.480 28.630 1.00 32.31 ? 945 HOH B O 1 HETATM 9923 O O . HOH XA 10 . ? 25.182 44.633 45.621 1.00 18.22 ? 946 HOH B O 1 HETATM 9924 O O . HOH XA 10 . ? -2.785 21.256 37.062 1.00 16.40 ? 947 HOH B O 1 HETATM 9925 O O . HOH XA 10 . ? 14.727 0.850 22.315 1.00 27.83 ? 948 HOH B O 1 HETATM 9926 O O . HOH XA 10 . ? 31.764 44.951 45.974 1.00 20.69 ? 949 HOH B O 1 HETATM 9927 O O . HOH XA 10 . ? 27.398 30.306 0.052 1.00 20.57 ? 950 HOH B O 1 HETATM 9928 O O . HOH XA 10 . ? 22.142 43.931 26.181 1.00 27.42 ? 951 HOH B O 1 HETATM 9929 O O . HOH XA 10 . ? 21.309 43.489 46.276 1.00 20.52 ? 952 HOH B O 1 HETATM 9930 O O . HOH XA 10 . ? 12.660 3.138 32.760 1.00 24.29 ? 953 HOH B O 1 HETATM 9931 O O . HOH XA 10 . ? 29.146 22.276 13.999 1.00 15.20 ? 954 HOH B O 1 HETATM 9932 O O . HOH XA 10 . ? 25.598 33.940 29.728 1.00 20.32 ? 955 HOH B O 1 HETATM 9933 O O . HOH XA 10 . ? 5.727 7.857 32.210 1.00 18.74 ? 956 HOH B O 1 HETATM 9934 O O . HOH XA 10 . ? 0.040 47.508 33.956 1.00 29.96 ? 957 HOH B O 1 HETATM 9935 O O . HOH XA 10 . ? -13.160 43.938 25.994 1.00 18.85 ? 958 HOH B O 1 HETATM 9936 O O . HOH XA 10 . ? 41.092 35.329 45.292 1.00 29.38 ? 959 HOH B O 1 HETATM 9937 O O . HOH XA 10 . ? 30.409 27.293 45.188 1.00 16.03 ? 960 HOH B O 1 HETATM 9938 O O . HOH XA 10 . ? 33.406 33.528 25.516 1.00 18.49 ? 961 HOH B O 1 HETATM 9939 O O . HOH XA 10 . ? 38.155 39.520 32.232 1.00 22.77 ? 962 HOH B O 1 HETATM 9940 O O . HOH XA 10 . ? 0.542 27.673 24.237 1.00 18.14 ? 963 HOH B O 1 HETATM 9941 O O . HOH XA 10 . ? 23.903 42.255 46.104 1.00 23.00 ? 964 HOH B O 1 HETATM 9942 O O . HOH XA 10 . ? 4.431 7.652 16.384 1.00 29.19 ? 965 HOH B O 1 HETATM 9943 O O . HOH XA 10 . ? 11.291 31.670 52.921 1.00 15.58 ? 966 HOH B O 1 HETATM 9944 O O . HOH XA 10 . ? -1.062 37.536 28.156 1.00 19.76 ? 967 HOH B O 1 HETATM 9945 O O . HOH XA 10 . ? -4.266 22.081 35.023 1.00 16.47 ? 968 HOH B O 1 HETATM 9946 O O . HOH XA 10 . ? 40.756 21.793 33.893 1.00 22.79 ? 969 HOH B O 1 HETATM 9947 O O . HOH XA 10 . ? 13.507 25.944 21.387 1.00 27.54 ? 970 HOH B O 1 HETATM 9948 O O . HOH XA 10 . ? 14.252 58.175 29.090 1.00 31.70 ? 971 HOH B O 1 HETATM 9949 O O . HOH XA 10 . ? 38.334 41.525 33.781 1.00 16.78 ? 972 HOH B O 1 HETATM 9950 O O . HOH XA 10 . ? -0.994 14.902 24.311 1.00 23.90 ? 973 HOH B O 1 HETATM 9951 O O . HOH XA 10 . ? 13.610 5.159 13.036 1.00 18.33 ? 974 HOH B O 1 HETATM 9952 O O . HOH XA 10 . ? -5.457 12.433 33.871 1.00 29.06 ? 975 HOH B O 1 HETATM 9953 O O . HOH XA 10 . ? 26.822 32.332 46.272 1.00 16.82 ? 976 HOH B O 1 HETATM 9954 O O . HOH XA 10 . ? 18.522 42.825 49.650 1.00 22.04 ? 977 HOH B O 1 HETATM 9955 O O . HOH XA 10 . ? 0.611 15.395 41.834 1.00 19.16 ? 978 HOH B O 1 HETATM 9956 O O . HOH XA 10 . ? 11.635 19.027 29.635 1.00 18.96 ? 979 HOH B O 1 HETATM 9957 O O . HOH XA 10 . ? 28.948 5.938 18.503 1.00 24.41 ? 980 HOH B O 1 HETATM 9958 O O . HOH XA 10 . ? 37.620 44.843 22.413 1.00 60.27 ? 981 HOH B O 1 HETATM 9959 O O . HOH XA 10 . ? 23.989 51.267 31.455 1.00 25.13 ? 982 HOH B O 1 HETATM 9960 O O . HOH XA 10 . ? 25.901 46.827 41.840 1.00 19.26 ? 983 HOH B O 1 HETATM 9961 O O . HOH XA 10 . ? 9.607 14.389 10.373 1.00 27.88 ? 984 HOH B O 1 HETATM 9962 O O . HOH XA 10 . ? 13.657 16.407 44.523 1.00 17.46 ? 985 HOH B O 1 HETATM 9963 O O . HOH XA 10 . ? 31.557 27.303 4.907 1.00 17.72 ? 986 HOH B O 1 HETATM 9964 O O . HOH XA 10 . ? 22.361 12.930 42.743 1.00 29.46 ? 987 HOH B O 1 HETATM 9965 O O . HOH XA 10 . ? 4.288 16.776 40.038 1.00 20.81 ? 988 HOH B O 1 HETATM 9966 O O . HOH XA 10 . ? -2.679 27.168 18.459 1.00 34.85 ? 989 HOH B O 1 HETATM 9967 O O . HOH XA 10 . ? 34.024 27.976 4.767 1.00 23.12 ? 990 HOH B O 1 HETATM 9968 O O . HOH XA 10 . ? 26.116 37.891 51.303 1.00 20.73 ? 991 HOH B O 1 HETATM 9969 O O . HOH XA 10 . ? 29.687 31.802 26.888 1.00 20.51 ? 992 HOH B O 1 HETATM 9970 O O . HOH XA 10 . ? -2.812 17.737 51.631 1.00 24.63 ? 993 HOH B O 1 HETATM 9971 O O . HOH XA 10 . ? 5.073 47.717 31.217 1.00 25.71 ? 994 HOH B O 1 HETATM 9972 O O . HOH XA 10 . ? 16.934 50.468 17.727 1.00 22.96 ? 995 HOH B O 1 HETATM 9973 O O . HOH XA 10 . ? 9.493 8.319 40.052 1.00 51.40 ? 996 HOH B O 1 HETATM 9974 O O . HOH XA 10 . ? 0.246 29.725 6.067 1.00 26.99 ? 997 HOH B O 1 HETATM 9975 O O . HOH XA 10 . ? 3.420 36.992 45.304 1.00 20.37 ? 998 HOH B O 1 HETATM 9976 O O . HOH XA 10 . ? 35.429 31.069 16.746 1.00 25.26 ? 999 HOH B O 1 HETATM 9977 O O . HOH XA 10 . ? 35.325 29.353 19.925 1.00 27.45 ? 1000 HOH B O 1 HETATM 9978 O O . HOH XA 10 . ? 12.548 14.643 17.335 1.00 20.78 ? 1001 HOH B O 1 HETATM 9979 O O . HOH XA 10 . ? 33.987 19.190 17.620 1.00 21.53 ? 1002 HOH B O 1 HETATM 9980 O O . HOH XA 10 . ? 25.750 36.200 36.198 1.00 26.51 ? 1003 HOH B O 1 HETATM 9981 O O . HOH XA 10 . ? -3.309 40.069 27.699 1.00 30.68 ? 1004 HOH B O 1 HETATM 9982 O O . HOH XA 10 . ? 41.782 28.302 39.262 1.00 25.08 ? 1005 HOH B O 1 HETATM 9983 O O . HOH XA 10 . ? 33.080 23.016 39.765 1.00 17.92 ? 1006 HOH B O 1 HETATM 9984 O O . HOH XA 10 . ? 6.178 49.771 12.713 1.00 33.46 ? 1007 HOH B O 1 HETATM 9985 O O . HOH XA 10 . ? -2.272 14.565 21.523 1.00 44.32 ? 1008 HOH B O 1 HETATM 9986 O O . HOH XA 10 . ? 29.763 32.120 57.239 1.00 31.13 ? 1009 HOH B O 1 HETATM 9987 O O . HOH XA 10 . ? -0.925 50.154 24.040 1.00 22.84 ? 1010 HOH B O 1 HETATM 9988 O O . HOH XA 10 . ? -2.405 41.609 13.664 1.00 23.07 ? 1011 HOH B O 1 HETATM 9989 O O . HOH XA 10 . ? 0.787 39.061 36.674 1.00 22.41 ? 1012 HOH B O 1 HETATM 9990 O O . HOH XA 10 . ? 41.815 24.288 12.569 1.00 25.69 ? 1013 HOH B O 1 HETATM 9991 O O . HOH XA 10 . ? -9.478 45.334 22.781 1.00 24.95 ? 1014 HOH B O 1 HETATM 9992 O O . HOH XA 10 . ? 19.106 6.848 9.193 1.00 29.16 ? 1015 HOH B O 1 HETATM 9993 O O . HOH XA 10 . ? 3.074 46.680 12.561 1.00 26.43 ? 1016 HOH B O 1 HETATM 9994 O O . HOH XA 10 . ? 2.600 36.681 4.740 1.00 31.42 ? 1017 HOH B O 1 HETATM 9995 O O . HOH XA 10 . ? 37.268 29.323 26.642 1.00 30.08 ? 1018 HOH B O 1 HETATM 9996 O O . HOH XA 10 . ? 11.471 6.454 34.901 1.00 40.08 ? 1019 HOH B O 1 HETATM 9997 O O . HOH XA 10 . ? -8.198 19.104 13.256 1.00 25.43 ? 1020 HOH B O 1 HETATM 9998 O O . HOH XA 10 . ? -0.924 27.346 20.323 1.00 28.76 ? 1021 HOH B O 1 HETATM 9999 O O . HOH XA 10 . ? 18.665 21.044 53.548 1.00 23.74 ? 1022 HOH B O 1 HETATM 10000 O O . HOH XA 10 . ? 10.658 17.398 16.702 1.00 21.97 ? 1023 HOH B O 1 HETATM 10001 O O . HOH XA 10 . ? 15.082 46.270 44.059 1.00 20.22 ? 1024 HOH B O 1 HETATM 10002 O O . HOH XA 10 . ? 18.614 38.552 1.817 1.00 32.21 ? 1025 HOH B O 1 HETATM 10003 O O . HOH XA 10 . ? 1.217 20.360 55.295 1.00 23.82 ? 1026 HOH B O 1 HETATM 10004 O O . HOH XA 10 . ? 9.951 59.416 20.820 1.00 27.32 ? 1027 HOH B O 1 HETATM 10005 O O . HOH XA 10 . ? 20.510 14.007 35.251 1.00 36.48 ? 1028 HOH B O 1 HETATM 10006 O O . HOH XA 10 . ? 36.639 20.598 7.772 1.00 28.20 ? 1029 HOH B O 1 HETATM 10007 O O . HOH XA 10 . ? 0.667 21.836 57.805 1.00 25.85 ? 1030 HOH B O 1 HETATM 10008 O O . HOH XA 10 . ? 12.901 10.315 37.099 1.00 19.17 ? 1031 HOH B O 1 HETATM 10009 O O . HOH XA 10 . ? -5.781 24.281 36.688 1.00 35.28 ? 1032 HOH B O 1 HETATM 10010 O O . HOH XA 10 . ? 17.856 2.104 22.649 1.00 18.09 ? 1033 HOH B O 1 HETATM 10011 O O . HOH XA 10 . ? 32.230 40.968 21.321 1.00 22.83 ? 1034 HOH B O 1 HETATM 10012 O O . HOH XA 10 . ? 24.882 10.771 0.554 1.00 26.48 ? 1035 HOH B O 1 HETATM 10013 O O . HOH XA 10 . ? 19.942 54.614 22.968 1.00 26.78 ? 1036 HOH B O 1 HETATM 10014 O O . HOH XA 10 . ? 13.162 8.631 34.892 1.00 26.04 ? 1037 HOH B O 1 HETATM 10015 O O . HOH XA 10 . ? 16.749 17.307 49.545 1.00 30.21 ? 1038 HOH B O 1 HETATM 10016 O O . HOH XA 10 . ? -7.405 21.311 11.371 1.00 32.40 ? 1039 HOH B O 1 HETATM 10017 O O . HOH XA 10 . ? -5.728 40.301 26.615 1.00 16.84 ? 1040 HOH B O 1 HETATM 10018 O O . HOH XA 10 . ? 29.000 25.463 1.600 1.00 20.35 ? 1041 HOH B O 1 HETATM 10019 O O . HOH XA 10 . ? 43.926 26.247 36.153 1.00 26.08 ? 1042 HOH B O 1 HETATM 10020 O O . HOH XA 10 . ? 3.010 32.663 50.913 1.00 37.23 ? 1043 HOH B O 1 HETATM 10021 O O . HOH XA 10 . ? -5.259 16.721 51.630 1.00 36.47 ? 1044 HOH B O 1 HETATM 10022 O O . HOH XA 10 . ? 37.938 42.012 45.370 1.00 34.96 ? 1045 HOH B O 1 HETATM 10023 O O . HOH XA 10 . ? 32.894 44.918 42.155 1.00 27.50 ? 1046 HOH B O 1 HETATM 10024 O O . HOH XA 10 . ? -7.675 16.185 34.354 1.00 25.86 ? 1047 HOH B O 1 HETATM 10025 O O . HOH XA 10 . ? 7.892 32.206 64.186 1.00 20.20 ? 1048 HOH B O 1 HETATM 10026 O O . HOH XA 10 . ? -4.830 35.280 15.272 1.00 26.50 ? 1049 HOH B O 1 HETATM 10027 O O . HOH XA 10 . ? 19.798 3.323 25.403 1.00 37.49 ? 1050 HOH B O 1 HETATM 10028 O O . HOH XA 10 . ? 6.833 15.739 41.918 1.00 25.47 ? 1051 HOH B O 1 HETATM 10029 O O . HOH XA 10 . ? 23.465 21.218 39.629 1.00 27.61 ? 1052 HOH B O 1 HETATM 10030 O O . HOH XA 10 . ? 35.210 23.738 38.374 1.00 20.64 ? 1053 HOH B O 1 HETATM 10031 O O . HOH XA 10 . ? 35.165 30.547 48.914 1.00 29.22 ? 1054 HOH B O 1 HETATM 10032 O O . HOH XA 10 . ? 26.094 37.495 -1.904 1.00 28.90 ? 1055 HOH B O 1 HETATM 10033 O O . HOH XA 10 . ? 11.669 37.514 6.598 1.00 25.63 ? 1056 HOH B O 1 HETATM 10034 O O . HOH XA 10 . ? 31.308 28.644 47.831 1.00 37.12 ? 1057 HOH B O 1 HETATM 10035 O O . HOH XA 10 . ? 20.773 53.422 20.538 1.00 27.89 ? 1058 HOH B O 1 HETATM 10036 O O . HOH XA 10 . ? 41.435 24.309 31.051 1.00 22.01 ? 1059 HOH B O 1 HETATM 10037 O O . HOH XA 10 . ? -1.677 51.487 26.932 1.00 41.02 ? 1060 HOH B O 1 HETATM 10038 O O . HOH XA 10 . ? 20.545 47.484 41.629 1.00 27.88 ? 1061 HOH B O 1 HETATM 10039 O O . HOH XA 10 . ? 13.103 13.710 44.992 1.00 30.20 ? 1062 HOH B O 1 HETATM 10040 O O . HOH XA 10 . ? -3.343 36.858 12.095 1.00 25.28 ? 1063 HOH B O 1 HETATM 10041 O O . HOH XA 10 . ? 11.352 17.512 27.539 1.00 28.03 ? 1064 HOH B O 1 HETATM 10042 O O . HOH XA 10 . ? 28.780 26.563 51.571 1.00 40.47 ? 1065 HOH B O 1 HETATM 10043 O O . HOH XA 10 . ? 21.783 45.200 48.292 1.00 30.03 ? 1066 HOH B O 1 HETATM 10044 O O . HOH XA 10 . ? 34.546 41.666 46.933 1.00 23.61 ? 1067 HOH B O 1 HETATM 10045 O O . HOH XA 10 . ? -0.395 27.861 49.052 1.00 29.05 ? 1068 HOH B O 1 HETATM 10046 O O . HOH XA 10 . ? 11.471 6.935 62.510 1.00 50.24 ? 1069 HOH B O 1 HETATM 10047 O O . HOH XA 10 . ? 12.657 30.675 26.956 1.00 20.89 ? 1070 HOH B O 1 HETATM 10048 O O . HOH XA 10 . ? 11.946 51.633 9.155 1.00 28.18 ? 1071 HOH B O 1 HETATM 10049 O O . HOH XA 10 . ? 18.227 12.433 35.142 1.00 19.63 ? 1072 HOH B O 1 HETATM 10050 O O . HOH XA 10 . ? 24.071 15.017 36.894 1.00 26.85 ? 1073 HOH B O 1 HETATM 10051 O O . HOH XA 10 . ? 3.253 58.377 27.051 1.00 27.80 ? 1074 HOH B O 1 HETATM 10052 O O . HOH XA 10 . ? -6.775 32.044 25.775 1.00 24.02 ? 1075 HOH B O 1 HETATM 10053 O O . HOH XA 10 . ? 2.376 46.300 31.779 1.00 29.20 ? 1076 HOH B O 1 HETATM 10054 O O . HOH XA 10 . ? 11.933 26.695 61.970 1.00 35.43 ? 1077 HOH B O 1 HETATM 10055 O O . HOH XA 10 . ? 12.779 32.020 1.462 1.00 25.46 ? 1078 HOH B O 1 HETATM 10056 O O . HOH XA 10 . ? 21.898 20.334 41.590 1.00 30.38 ? 1079 HOH B O 1 HETATM 10057 O O . HOH XA 10 . ? 26.354 49.302 35.496 1.00 24.67 ? 1080 HOH B O 1 HETATM 10058 O O . HOH XA 10 . ? -3.978 30.996 39.851 1.00 30.80 ? 1081 HOH B O 1 HETATM 10059 O O . HOH XA 10 . ? 7.734 5.947 15.101 1.00 35.11 ? 1082 HOH B O 1 HETATM 10060 O O . HOH XA 10 . ? 11.414 23.335 20.389 1.00 21.16 ? 1083 HOH B O 1 HETATM 10061 O O . HOH XA 10 . ? -6.293 28.615 36.430 1.00 32.78 ? 1084 HOH B O 1 HETATM 10062 O O . HOH XA 10 . ? 27.330 47.162 39.639 1.00 22.81 ? 1085 HOH B O 1 HETATM 10063 O O . HOH XA 10 . ? -6.267 37.805 25.662 1.00 21.86 ? 1086 HOH B O 1 HETATM 10064 O O . HOH XA 10 . ? 39.213 27.843 31.318 1.00 26.05 ? 1087 HOH B O 1 HETATM 10065 O O . HOH XA 10 . ? 7.753 48.982 32.329 1.00 24.79 ? 1088 HOH B O 1 HETATM 10066 O O . HOH XA 10 . ? 13.799 13.364 3.632 1.00 31.45 ? 1089 HOH B O 1 HETATM 10067 O O . HOH XA 10 . ? 32.098 41.227 48.392 1.00 27.89 ? 1090 HOH B O 1 HETATM 10068 O O . HOH XA 10 . ? 13.279 15.062 30.056 1.00 38.40 ? 1091 HOH B O 1 HETATM 10069 O O . HOH XA 10 . ? 14.633 4.263 10.695 1.00 28.29 ? 1092 HOH B O 1 HETATM 10070 O O . HOH XA 10 . ? 13.858 40.465 7.461 1.00 35.95 ? 1093 HOH B O 1 HETATM 10071 O O . HOH XA 10 . ? 40.367 36.393 41.405 1.00 32.68 ? 1094 HOH B O 1 HETATM 10072 O O . HOH XA 10 . ? -0.651 12.937 55.322 1.00 23.36 ? 1095 HOH B O 1 HETATM 10073 O O . HOH XA 10 . ? 37.551 32.024 26.685 1.00 24.98 ? 1096 HOH B O 1 HETATM 10074 O O . HOH XA 10 . ? -0.123 29.532 33.817 1.00 16.46 ? 1097 HOH B O 1 HETATM 10075 O O . HOH XA 10 . ? 27.670 44.653 28.216 1.00 41.17 ? 1098 HOH B O 1 HETATM 10076 O O . HOH XA 10 . ? 17.452 43.150 7.891 1.00 24.88 ? 1099 HOH B O 1 HETATM 10077 O O . HOH XA 10 . ? -8.543 28.712 7.692 1.00 34.23 ? 1100 HOH B O 1 HETATM 10078 O O . HOH XA 10 . ? 25.762 48.259 28.524 1.00 34.90 ? 1101 HOH B O 1 HETATM 10079 O O . HOH XA 10 . ? 40.628 31.160 30.391 1.00 32.30 ? 1102 HOH B O 1 HETATM 10080 O O . HOH XA 10 . ? 7.370 9.224 54.170 1.00 30.74 ? 1103 HOH B O 1 HETATM 10081 O O . HOH XA 10 . ? 14.822 42.459 42.350 1.00 21.09 ? 1104 HOH B O 1 HETATM 10082 O O . HOH XA 10 . ? 32.345 31.055 17.156 1.00 24.15 ? 1105 HOH B O 1 HETATM 10083 O O . HOH XA 10 . ? 20.493 41.294 5.130 1.00 33.80 ? 1106 HOH B O 1 HETATM 10084 O O . HOH XA 10 . ? 35.126 43.821 39.866 1.00 37.14 ? 1107 HOH B O 1 HETATM 10085 O O . HOH XA 10 . ? 44.729 30.843 34.690 1.00 30.34 ? 1108 HOH B O 1 HETATM 10086 O O . HOH XA 10 . ? 15.950 28.849 4.633 1.00 26.87 ? 1109 HOH B O 1 HETATM 10087 O O . HOH XA 10 . ? 4.687 0.271 25.244 1.00 41.50 ? 1110 HOH B O 1 HETATM 10088 O O . HOH XA 10 . ? 22.535 41.258 50.377 1.00 38.00 ? 1111 HOH B O 1 HETATM 10089 O O . HOH XA 10 . ? 29.732 37.850 4.716 1.00 31.18 ? 1112 HOH B O 1 HETATM 10090 O O . HOH XA 10 . ? 25.430 39.900 53.260 1.00 32.74 ? 1113 HOH B O 1 HETATM 10091 O O . HOH XA 10 . ? 22.066 54.926 25.092 1.00 31.99 ? 1114 HOH B O 1 HETATM 10092 O O . HOH XA 10 . ? -5.172 34.050 12.731 1.00 44.30 ? 1115 HOH B O 1 HETATM 10093 O O . HOH XA 10 . ? 33.384 33.310 16.903 1.00 28.67 ? 1116 HOH B O 1 HETATM 10094 O O . HOH XA 10 . ? 14.782 23.876 4.624 1.00 43.69 ? 1117 HOH B O 1 HETATM 10095 O O . HOH XA 10 . ? -0.797 29.024 51.991 1.00 44.95 ? 1118 HOH B O 1 HETATM 10096 O O . HOH XA 10 . ? 11.907 40.706 9.141 1.00 30.46 ? 1119 HOH B O 1 HETATM 10097 O O . HOH XA 10 . ? 39.506 23.544 27.497 1.00 43.93 ? 1120 HOH B O 1 HETATM 10098 O O . HOH XA 10 . ? -6.359 22.168 38.719 1.00 27.76 ? 1121 HOH B O 1 HETATM 10099 O O . HOH XA 10 . ? -14.594 34.549 26.417 1.00 26.88 ? 1122 HOH B O 1 HETATM 10100 O O . HOH XA 10 . ? 7.780 45.696 10.848 1.00 21.53 ? 1123 HOH B O 1 HETATM 10101 O O . HOH XA 10 . ? -0.498 13.482 19.325 1.00 37.61 ? 1124 HOH B O 1 HETATM 10102 O O . HOH XA 10 . ? 2.222 30.454 49.710 1.00 30.45 ? 1125 HOH B O 1 HETATM 10103 O O . HOH XA 10 . ? 22.176 17.068 1.868 1.00 24.55 ? 1126 HOH B O 1 HETATM 10104 O O . HOH XA 10 . ? -4.739 50.067 21.303 1.00 38.75 ? 1127 HOH B O 1 HETATM 10105 O O . HOH XA 10 . ? 16.609 34.719 53.600 1.00 27.24 ? 1128 HOH B O 1 HETATM 10106 O O . HOH XA 10 . ? 11.098 25.549 22.098 1.00 26.02 ? 1129 HOH B O 1 HETATM 10107 O O . HOH XA 10 . ? 0.519 37.477 46.482 1.00 41.02 ? 1130 HOH B O 1 HETATM 10108 O O . HOH XA 10 . ? 16.942 0.286 24.699 1.00 36.91 ? 1131 HOH B O 1 HETATM 10109 O O . HOH XA 10 . ? 29.802 10.391 30.728 1.00 39.15 ? 1132 HOH B O 1 HETATM 10110 O O . HOH XA 10 . ? 9.351 15.822 30.111 1.00 31.76 ? 1133 HOH B O 1 HETATM 10111 O O . HOH XA 10 . ? -2.361 27.321 24.033 1.00 35.79 ? 1134 HOH B O 1 HETATM 10112 O O . HOH XA 10 . ? -2.291 17.474 11.950 1.00 27.91 ? 1135 HOH B O 1 HETATM 10113 O O . HOH XA 10 . ? 24.464 23.110 44.447 1.00 30.98 ? 1136 HOH B O 1 HETATM 10114 O O . HOH XA 10 . ? 21.971 11.703 32.066 1.00 28.71 ? 1137 HOH B O 1 HETATM 10115 O O . HOH XA 10 . ? -5.774 37.958 10.476 1.00 34.16 ? 1138 HOH B O 1 HETATM 10116 O O . HOH XA 10 . ? 14.865 52.057 17.069 1.00 34.48 ? 1139 HOH B O 1 HETATM 10117 O O . HOH XA 10 . ? -3.240 11.688 30.414 1.00 25.97 ? 1140 HOH B O 1 HETATM 10118 O O . HOH XA 10 . ? 19.265 28.955 4.334 1.00 42.57 ? 1141 HOH B O 1 HETATM 10119 O O . HOH XA 10 . ? 8.195 47.470 38.085 1.00 37.66 ? 1142 HOH B O 1 HETATM 10120 O O . HOH XA 10 . ? -2.073 11.798 33.046 1.00 41.71 ? 1143 HOH B O 1 HETATM 10121 O O . HOH XA 10 . ? 36.227 17.585 33.605 1.00 31.48 ? 1144 HOH B O 1 HETATM 10122 O O . HOH XA 10 . ? -3.253 24.400 26.349 1.00 30.01 ? 1145 HOH B O 1 HETATM 10123 O O . HOH XA 10 . ? 27.694 11.415 6.925 1.00 25.58 ? 1146 HOH B O 1 HETATM 10124 O O . HOH XA 10 . ? 18.436 17.197 36.302 1.00 35.88 ? 1147 HOH B O 1 HETATM 10125 O O . HOH XA 10 . ? -9.167 18.118 42.629 1.00 34.05 ? 1148 HOH B O 1 HETATM 10126 O O . HOH XA 10 . ? 0.872 27.494 2.792 1.00 32.12 ? 1149 HOH B O 1 HETATM 10127 O O . HOH XA 10 . ? 14.436 8.503 62.636 1.00 48.34 ? 1150 HOH B O 1 HETATM 10128 O O . HOH XA 10 . ? 23.644 20.648 43.835 1.00 24.28 ? 1151 HOH B O 1 HETATM 10129 O O . HOH XA 10 . ? 28.039 41.374 5.577 1.00 34.57 ? 1152 HOH B O 1 HETATM 10130 O O . HOH XA 10 . ? 28.263 32.862 29.674 1.00 30.16 ? 1153 HOH B O 1 HETATM 10131 O O . HOH XA 10 . ? 38.446 21.963 14.182 1.00 30.86 ? 1154 HOH B O 1 HETATM 10132 O O . HOH XA 10 . ? 25.550 24.345 49.743 1.00 20.79 ? 1155 HOH B O 1 HETATM 10133 O O . HOH XA 10 . ? 20.277 19.396 52.156 1.00 29.03 ? 1156 HOH B O 1 HETATM 10134 O O . HOH XA 10 . ? 13.081 44.511 43.432 1.00 34.23 ? 1157 HOH B O 1 HETATM 10135 O O . HOH XA 10 . ? 0.736 41.290 13.759 1.00 23.84 ? 1158 HOH B O 1 HETATM 10136 O O . HOH XA 10 . ? 34.216 27.798 1.756 1.00 42.97 ? 1159 HOH B O 1 HETATM 10137 O O . HOH XA 10 . ? -3.072 25.447 58.080 1.00 46.38 ? 1160 HOH B O 1 HETATM 10138 O O . HOH XA 10 . ? 19.188 35.382 53.341 1.00 27.01 ? 1161 HOH B O 1 HETATM 10139 O O . HOH XA 10 . ? 12.591 43.821 46.086 1.00 38.40 ? 1162 HOH B O 1 HETATM 10140 O O . HOH XA 10 . ? 11.408 34.166 51.647 1.00 31.72 ? 1163 HOH B O 1 HETATM 10141 O O . HOH XA 10 . ? 30.162 24.035 5.012 1.00 27.87 ? 1164 HOH B O 1 HETATM 10142 O O . HOH XA 10 . ? 37.324 24.406 6.555 1.00 28.99 ? 1165 HOH B O 1 HETATM 10143 O O . HOH XA 10 . ? 21.902 20.368 56.220 1.00 30.06 ? 1166 HOH B O 1 HETATM 10144 O O . HOH XA 10 . ? 11.663 16.054 12.951 1.00 39.54 ? 1167 HOH B O 1 HETATM 10145 O O . HOH XA 10 . ? 5.032 32.500 55.299 1.00 40.79 ? 1168 HOH B O 1 HETATM 10146 O O . HOH XA 10 . ? 3.637 0.714 35.548 1.00 40.38 ? 1169 HOH B O 1 HETATM 10147 O O . HOH XA 10 . ? 18.740 18.474 57.028 1.00 42.50 ? 1170 HOH B O 1 HETATM 10148 O O . HOH XA 10 . ? 15.201 3.925 33.119 1.00 33.67 ? 1171 HOH B O 1 HETATM 10149 O O . HOH XA 10 . ? 11.445 33.709 57.430 1.00 32.78 ? 1172 HOH B O 1 HETATM 10150 O O . HOH XA 10 . ? 0.512 10.492 54.503 1.00 27.41 ? 1173 HOH B O 1 HETATM 10151 O O . HOH XA 10 . ? -1.798 14.812 44.038 1.00 31.28 ? 1174 HOH B O 1 HETATM 10152 O O . HOH XA 10 . ? 12.120 17.489 3.999 1.00 37.30 ? 1175 HOH B O 1 HETATM 10153 O O . HOH XA 10 . ? 11.190 11.191 45.348 1.00 31.85 ? 1176 HOH B O 1 HETATM 10154 O O . HOH XA 10 . ? 16.112 44.034 47.875 1.00 36.96 ? 1177 HOH B O 1 HETATM 10155 O O . HOH XA 10 . ? -4.830 26.399 54.083 1.00 34.85 ? 1178 HOH B O 1 HETATM 10156 O O . HOH XA 10 . ? 16.345 46.605 46.661 1.00 34.18 ? 1179 HOH B O 1 HETATM 10157 O O . HOH XA 10 . ? 42.948 24.155 8.590 1.00 23.42 ? 1180 HOH B O 1 HETATM 10158 O O . HOH XA 10 . ? -5.680 36.088 41.617 1.00 32.14 ? 1181 HOH B O 1 HETATM 10159 O O . HOH XA 10 . ? 6.775 9.292 60.163 1.00 31.71 ? 1182 HOH B O 1 HETATM 10160 O O . HOH XA 10 . ? 9.049 30.087 5.268 1.00 28.17 ? 1183 HOH B O 1 HETATM 10161 O O . HOH XA 10 . ? 19.446 18.909 47.086 1.00 51.72 ? 1184 HOH B O 1 HETATM 10162 O O . HOH XA 10 . ? 0.937 4.911 35.934 1.00 40.31 ? 1185 HOH B O 1 HETATM 10163 O O . HOH XA 10 . ? 10.377 47.776 35.134 1.00 38.42 ? 1186 HOH B O 1 HETATM 10164 O O . HOH XA 10 . ? -6.741 20.363 20.175 1.00 42.02 ? 1187 HOH B O 1 HETATM 10165 O O . HOH XA 10 . ? 24.772 51.916 28.989 1.00 42.22 ? 1188 HOH B O 1 HETATM 10166 O O . HOH XA 10 . ? 41.055 36.017 37.367 1.00 38.46 ? 1189 HOH B O 1 HETATM 10167 O O . HOH XA 10 . ? 15.430 0.025 19.865 1.00 37.04 ? 1190 HOH B O 1 HETATM 10168 O O . HOH XA 10 . ? 13.875 54.913 18.016 1.00 44.20 ? 1191 HOH B O 1 HETATM 10169 O O . HOH XA 10 . ? -6.169 38.786 37.412 1.00 35.84 ? 1192 HOH B O 1 HETATM 10170 O O . HOH XA 10 . ? 1.177 31.399 52.442 1.00 43.50 ? 1193 HOH B O 1 HETATM 10171 O O . HOH XA 10 . ? 34.537 14.161 30.718 1.00 42.99 ? 1194 HOH B O 1 HETATM 10172 O O . HOH XA 10 . ? 29.261 19.346 1.365 1.00 46.96 ? 1195 HOH B O 1 HETATM 10173 O O . HOH XA 10 . ? 24.554 4.609 16.641 1.00 32.74 ? 1196 HOH B O 1 HETATM 10174 O O . HOH XA 10 . ? 8.083 2.513 20.082 1.00 37.52 ? 1197 HOH B O 1 HETATM 10175 O O . HOH XA 10 . ? 12.001 54.783 35.551 1.00 42.19 ? 1198 HOH B O 1 HETATM 10176 O O . HOH XA 10 . ? 16.283 55.863 31.653 1.00 36.78 ? 1199 HOH B O 1 HETATM 10177 O O . HOH XA 10 . ? 10.039 32.564 1.795 1.00 34.50 ? 1200 HOH B O 1 HETATM 10178 O O . HOH XA 10 . ? 41.187 34.210 29.649 1.00 41.79 ? 1201 HOH B O 1 HETATM 10179 O O . HOH XA 10 . ? 26.098 25.762 55.584 1.00 35.03 ? 1202 HOH B O 1 HETATM 10180 O O . HOH XA 10 . ? 37.997 28.627 19.182 1.00 33.20 ? 1203 HOH B O 1 HETATM 10181 O O . HOH XA 10 . ? 3.732 45.278 35.078 1.00 48.46 ? 1204 HOH B O 1 HETATM 10182 O O . HOH XA 10 . ? 24.052 53.157 34.297 1.00 39.53 ? 1205 HOH B O 1 HETATM 10183 O O . HOH XA 10 . ? 15.722 45.896 10.631 1.00 44.72 ? 1206 HOH B O 1 HETATM 10184 O O . HOH XA 10 . ? 4.148 27.185 60.833 1.00 36.43 ? 1207 HOH B O 1 HETATM 10185 O O . HOH XA 10 . ? 40.383 28.810 47.208 1.00 42.09 ? 1208 HOH B O 1 HETATM 10186 O O . HOH XA 10 . ? 8.799 32.779 4.390 1.00 35.59 ? 1209 HOH B O 1 HETATM 10187 O O . HOH XA 10 . ? 4.622 41.665 39.819 1.00 39.93 ? 1210 HOH B O 1 HETATM 10188 O O . HOH XA 10 . ? 29.466 46.705 25.949 1.00 42.92 ? 1211 HOH B O 1 HETATM 10189 O O . HOH XA 10 . ? 5.191 39.312 42.317 1.00 35.12 ? 1212 HOH B O 1 HETATM 10190 O O . HOH XA 10 . ? 34.980 24.143 42.949 1.00 44.28 ? 1213 HOH B O 1 HETATM 10191 O O . HOH XA 10 . ? -3.124 11.663 26.819 1.00 29.19 ? 1214 HOH B O 1 HETATM 10192 O O . HOH XA 10 . ? -4.828 25.556 32.920 1.00 24.16 ? 1215 HOH B O 1 HETATM 10193 O O . HOH XA 10 . ? 0.778 44.265 14.489 1.00 28.18 ? 1216 HOH B O 1 HETATM 10194 O O . HOH XA 10 . ? 20.237 31.143 -0.729 1.00 39.46 ? 1217 HOH B O 1 HETATM 10195 O O . HOH XA 10 . ? 11.325 58.544 29.920 1.00 31.30 ? 1218 HOH B O 1 HETATM 10196 O O . HOH XA 10 . ? 14.525 13.964 50.613 1.00 45.36 ? 1219 HOH B O 1 HETATM 10197 O O . HOH XA 10 . ? 30.496 17.989 37.067 1.00 44.74 ? 1220 HOH B O 1 HETATM 10198 O O . HOH XA 10 . ? 21.839 48.689 13.072 1.00 28.62 ? 1221 HOH B O 1 HETATM 10199 O O . HOH XA 10 . ? 2.278 6.027 26.252 1.00 24.43 ? 1222 HOH B O 1 HETATM 10200 O O . HOH XA 10 . ? 8.168 11.483 47.905 1.00 38.20 ? 1223 HOH B O 1 HETATM 10201 O O . HOH XA 10 . ? 29.201 15.079 13.473 1.00 32.82 ? 1224 HOH B O 1 HETATM 10202 O O . HOH XA 10 . ? 2.020 2.319 29.887 1.00 25.97 ? 1225 HOH B O 1 HETATM 10203 O O . HOH XA 10 . ? 4.691 25.053 9.014 1.00 20.85 ? 1226 HOH B O 1 HETATM 10204 O O . HOH XA 10 . ? 35.684 32.332 24.656 1.00 20.92 ? 1227 HOH B O 1 HETATM 10205 O O . HOH XA 10 . ? 0.856 41.830 11.242 1.00 30.71 ? 1228 HOH B O 1 HETATM 10206 O O . HOH XA 10 . ? 16.206 2.590 19.100 1.00 26.38 ? 1229 HOH B O 1 HETATM 10207 O O . HOH XA 10 . ? 15.145 11.113 37.879 1.00 32.77 ? 1230 HOH B O 1 HETATM 10208 O O . HOH XA 10 . ? -0.264 3.213 33.641 1.00 38.04 ? 1231 HOH B O 1 HETATM 10209 O O . HOH XA 10 . ? 19.152 19.404 43.125 1.00 30.54 ? 1232 HOH B O 1 HETATM 10210 O O . HOH XA 10 . ? 24.572 11.617 32.963 1.00 37.22 ? 1233 HOH B O 1 HETATM 10211 O O . HOH XA 10 . ? 16.429 13.794 36.700 1.00 35.46 ? 1234 HOH B O 1 HETATM 10212 O O . HOH XA 10 . ? 33.836 28.130 48.799 1.00 35.17 ? 1235 HOH B O 1 HETATM 10213 O O . HOH XA 10 . ? 42.250 30.773 13.932 1.00 31.93 ? 1236 HOH B O 1 HETATM 10214 O O . HOH XA 10 . ? 7.933 32.451 55.283 1.00 26.88 ? 1237 HOH B O 1 HETATM 10215 O O . HOH XA 10 . ? 3.877 -0.873 27.549 1.00 38.56 ? 1238 HOH B O 1 HETATM 10216 O O . HOH XA 10 . ? 4.731 49.973 33.041 1.00 31.91 ? 1239 HOH B O 1 HETATM 10217 O O . HOH XA 10 . ? 36.164 39.655 19.939 1.00 43.37 ? 1240 HOH B O 1 HETATM 10218 O O . HOH XA 10 . ? 8.699 38.471 4.852 1.00 40.55 ? 1241 HOH B O 1 HETATM 10219 O O . HOH XA 10 . ? -3.613 35.543 7.400 1.00 32.11 ? 1242 HOH B O 1 HETATM 10220 O O . HOH XA 10 . ? -0.425 6.447 27.175 1.00 33.84 ? 1243 HOH B O 1 HETATM 10221 O O . HOH XA 10 . ? 14.991 55.035 22.264 1.00 45.74 ? 1244 HOH B O 1 HETATM 10222 O O . HOH XA 10 . ? 36.101 44.519 42.356 1.00 42.11 ? 1245 HOH B O 1 HETATM 10223 O O . HOH XA 10 . ? 28.366 37.599 30.512 1.00 35.12 ? 1246 HOH B O 1 HETATM 10224 O O . HOH XA 10 . ? 4.345 30.868 4.327 1.00 46.70 ? 1247 HOH B O 1 HETATM 10225 O O . HOH XA 10 . ? 0.213 56.710 30.542 1.00 32.56 ? 1248 HOH B O 1 HETATM 10226 O O . HOH XA 10 . ? 13.217 42.931 5.834 1.00 30.87 ? 1249 HOH B O 1 HETATM 10227 O O . HOH XA 10 . ? -1.915 21.143 58.564 1.00 28.68 ? 1250 HOH B O 1 HETATM 10228 O O . HOH XA 10 . ? -11.927 46.230 27.047 1.00 28.13 ? 1251 HOH B O 1 HETATM 10229 O O . HOH XA 10 . ? -6.310 21.340 8.941 1.00 39.98 ? 1252 HOH B O 1 HETATM 10230 O O . HOH XA 10 . ? -5.829 21.759 53.724 1.00 33.67 ? 1253 HOH B O 1 HETATM 10231 O O . HOH XA 10 . ? 20.981 30.811 59.044 1.00 33.67 ? 1254 HOH B O 1 HETATM 10232 O O . HOH XA 10 . ? -3.055 8.385 31.123 1.00 37.06 ? 1255 HOH B O 1 HETATM 10233 O O . HOH XA 10 . ? 31.726 37.041 17.120 1.00 25.31 ? 1256 HOH B O 1 HETATM 10234 O O . HOH XA 10 . ? -0.703 27.443 58.336 1.00 47.04 ? 1257 HOH B O 1 HETATM 10235 O O . HOH XA 10 . ? 34.362 35.694 53.162 1.00 33.30 ? 1258 HOH B O 1 HETATM 10236 O O . HOH XA 10 . ? 21.985 5.272 33.580 1.00 41.05 ? 1259 HOH B O 1 HETATM 10237 O O . HOH XA 10 . ? 35.850 24.010 17.497 1.00 33.09 ? 1260 HOH B O 1 HETATM 10238 O O . HOH XA 10 . ? 12.320 8.218 38.718 1.00 34.46 ? 1261 HOH B O 1 HETATM 10239 O O . HOH XA 10 . ? 6.127 3.700 40.978 1.00 32.63 ? 1262 HOH B O 1 HETATM 10240 O O . HOH XA 10 . ? 8.246 4.341 17.656 1.00 45.46 ? 1263 HOH B O 1 HETATM 10241 O O . HOH XA 10 . ? -5.357 16.892 54.794 1.00 39.31 ? 1264 HOH B O 1 HETATM 10242 O O . HOH XA 10 . ? 18.128 22.406 62.455 1.00 42.72 ? 1265 HOH B O 1 HETATM 10243 O O . HOH XA 10 . ? 34.668 44.751 10.431 1.00 36.43 ? 1266 HOH B O 1 HETATM 10244 O O . HOH XA 10 . ? 22.509 6.645 6.610 1.00 30.77 ? 1267 HOH B O 1 HETATM 10245 O O . HOH XA 10 . ? 9.178 -0.146 18.988 1.00 37.92 ? 1268 HOH B O 1 HETATM 10246 O O . HOH XA 10 . ? 31.950 20.444 38.792 1.00 51.38 ? 1269 HOH B O 1 HETATM 10247 O O . HOH XA 10 . ? 36.356 32.095 19.853 1.00 47.81 ? 1270 HOH B O 1 HETATM 10248 O O . HOH XA 10 . ? -1.198 9.558 52.496 1.00 38.47 ? 1271 HOH B O 1 HETATM 10249 O O . HOH XA 10 . ? -3.253 15.245 13.401 1.00 34.89 ? 1272 HOH B O 1 HETATM 10250 O O . HOH XA 10 . ? 5.746 41.240 47.091 1.00 36.15 ? 1273 HOH B O 1 HETATM 10251 O O . HOH XA 10 . ? 1.278 19.185 61.688 1.00 44.76 ? 1274 HOH B O 1 HETATM 10252 O O . HOH XA 10 . ? 12.611 19.483 62.891 1.00 35.59 ? 1275 HOH B O 1 HETATM 10253 O O . HOH XA 10 . ? 22.232 16.172 43.350 1.00 38.81 ? 1276 HOH B O 1 HETATM 10254 O O . HOH XA 10 . ? -6.574 15.237 43.449 1.00 36.81 ? 1277 HOH B O 1 HETATM 10255 O O . HOH XA 10 . ? 16.818 36.530 -0.486 1.00 34.59 ? 1278 HOH B O 1 HETATM 10256 O O . HOH XA 10 . ? 21.366 19.595 49.273 1.00 39.58 ? 1279 HOH B O 1 HETATM 10257 O O . HOH XA 10 . ? -4.871 27.015 40.910 1.00 47.95 ? 1280 HOH B O 1 HETATM 10258 O O . HOH XA 10 . ? 6.974 17.771 24.321 1.00 34.61 ? 1281 HOH B O 1 HETATM 10259 O O . HOH XA 10 . ? 7.213 15.198 27.199 1.00 10.54 ? 1282 HOH B O 1 HETATM 10260 O O . HOH XA 10 . ? -7.415 35.271 31.678 1.00 13.51 ? 1283 HOH B O 1 HETATM 10261 O O . HOH XA 10 . ? 35.860 31.536 39.714 1.00 11.21 ? 1284 HOH B O 1 HETATM 10262 O O . HOH XA 10 . ? 40.121 30.246 40.223 1.00 30.62 ? 1285 HOH B O 1 HETATM 10263 O O . HOH XA 10 . ? 28.062 6.693 26.880 1.00 34.84 ? 1286 HOH B O 1 HETATM 10264 O O . HOH XA 10 . ? 37.534 33.243 40.557 1.00 20.17 ? 1287 HOH B O 1 HETATM 10265 O O . HOH XA 10 . ? 2.853 28.546 5.080 1.00 28.00 ? 1288 HOH B O 1 HETATM 10266 O O . HOH XA 10 . ? 8.886 17.991 13.759 1.00 30.19 ? 1289 HOH B O 1 HETATM 10267 O O . HOH XA 10 . ? 33.535 22.866 17.778 1.00 31.48 ? 1290 HOH B O 1 HETATM 10268 O O . HOH XA 10 . ? 18.852 2.606 18.378 1.00 37.93 ? 1291 HOH B O 1 HETATM 10269 O O . HOH XA 10 . ? 13.087 18.481 33.271 1.00 43.26 ? 1292 HOH B O 1 HETATM 10270 O O . HOH XA 10 . ? -0.057 32.278 47.510 1.00 37.95 ? 1293 HOH B O 1 HETATM 10271 O O . HOH XA 10 . ? -5.923 11.493 29.875 1.00 32.49 ? 1294 HOH B O 1 HETATM 10272 O O . HOH XA 10 . ? 12.249 8.749 64.753 1.00 30.95 ? 1295 HOH B O 1 HETATM 10273 O O . HOH XA 10 . ? -4.845 6.049 42.408 1.00 44.57 ? 1296 HOH B O 1 HETATM 10274 O O . HOH XA 10 . ? 24.948 7.491 8.277 1.00 37.19 ? 1297 HOH B O 1 HETATM 10275 O O . HOH XA 10 . ? 4.347 6.153 13.435 1.00 50.61 ? 1298 HOH B O 1 HETATM 10276 O O . HOH XA 10 . ? 12.652 1.546 30.571 1.00 37.59 ? 1299 HOH B O 1 HETATM 10277 O O . HOH XA 10 . ? 25.300 38.144 56.325 1.00 38.21 ? 1300 HOH B O 1 HETATM 10278 O O . HOH XA 10 . ? 4.832 39.243 48.656 1.00 39.06 ? 1301 HOH B O 1 HETATM 10279 O O . HOH XA 10 . ? -5.775 7.956 30.737 1.00 48.42 ? 1302 HOH B O 1 HETATM 10280 O O . HOH XA 10 . ? 21.936 40.501 53.521 1.00 43.76 ? 1303 HOH B O 1 HETATM 10281 O O . HOH XA 10 . ? 23.597 31.181 60.120 1.00 47.91 ? 1304 HOH B O 1 HETATM 10282 O O . HOH XA 10 . ? 19.733 16.261 55.706 1.00 33.93 ? 1305 HOH B O 1 HETATM 10283 O O . HOH XA 10 . ? 0.583 7.070 45.565 1.00 42.26 ? 1306 HOH B O 1 HETATM 10284 O O . HOH XA 10 . ? 33.975 21.670 3.624 1.00 39.73 ? 1307 HOH B O 1 HETATM 10285 O O . HOH XA 10 . ? -4.105 46.864 33.537 1.00 45.30 ? 1308 HOH B O 1 HETATM 10286 O O . HOH XA 10 . ? 13.507 54.771 9.830 1.00 40.22 ? 1309 HOH B O 1 HETATM 10287 O O . HOH XA 10 . ? 30.200 11.423 6.011 1.00 38.22 ? 1310 HOH B O 1 HETATM 10288 O O . HOH XA 10 . ? 4.014 16.162 60.288 1.00 49.64 ? 1311 HOH B O 1 HETATM 10289 O O . HOH XA 10 . ? 3.609 5.134 44.007 1.00 31.51 ? 1312 HOH B O 1 HETATM 10290 O O . HOH XA 10 . ? 3.170 40.018 37.526 1.00 44.89 ? 1313 HOH B O 1 HETATM 10291 O O . HOH XA 10 . ? -5.094 27.736 19.352 1.00 42.90 ? 1314 HOH B O 1 HETATM 10292 O O . HOH XA 10 . ? -8.238 34.600 37.234 1.00 34.15 ? 1315 HOH B O 1 HETATM 10293 O O . HOH XA 10 . ? -12.340 35.630 25.585 1.00 37.56 ? 1316 HOH B O 1 HETATM 10294 O O . HOH XA 10 . ? 1.287 17.757 57.741 1.00 39.36 ? 1317 HOH B O 1 HETATM 10295 O O . HOH XA 10 . ? 15.680 8.156 1.641 1.00 39.96 ? 1318 HOH B O 1 HETATM 10296 O O . HOH XA 10 . ? 13.653 2.767 14.610 1.00 40.72 ? 1319 HOH B O 1 HETATM 10297 O O . HOH XA 10 . ? -3.708 9.201 20.012 1.00 36.34 ? 1320 HOH B O 1 HETATM 10298 O O . HOH XA 10 . ? -5.727 26.725 5.885 1.00 39.16 ? 1321 HOH B O 1 HETATM 10299 O O . HOH XA 10 . ? 40.236 42.132 8.566 1.00 41.17 ? 1322 HOH B O 1 HETATM 10300 O O . HOH XA 10 . ? 9.831 28.207 3.577 1.00 36.72 ? 1323 HOH B O 1 HETATM 10301 O O . HOH XA 10 . ? -0.991 46.282 13.279 1.00 44.90 ? 1324 HOH B O 1 HETATM 10302 O O . HOH XA 10 . ? 14.283 29.162 1.817 1.00 47.64 ? 1325 HOH B O 1 HETATM 10303 O O . HOH XA 10 . ? -11.595 20.471 46.789 1.00 48.01 ? 1326 HOH B O 1 HETATM 10304 O O . HOH XA 10 . ? -2.865 40.684 34.383 1.00 41.37 ? 1327 HOH B O 1 HETATM 10305 O O . HOH XA 10 . ? 25.063 26.561 59.209 1.00 53.54 ? 1328 HOH B O 1 HETATM 10306 O O . HOH XA 10 . ? 5.337 52.274 11.910 1.00 44.77 ? 1329 HOH B O 1 HETATM 10307 O O . HOH XA 10 . ? -6.805 24.326 52.373 1.00 36.84 ? 1330 HOH B O 1 HETATM 10308 O O . HOH XA 10 . ? 21.281 47.531 10.425 1.00 42.41 ? 1331 HOH B O 1 HETATM 10309 O O . HOH XA 10 . ? 2.375 12.503 58.037 1.00 48.68 ? 1332 HOH B O 1 HETATM 10310 O O . HOH XA 10 . ? 44.827 25.917 32.180 1.00 45.86 ? 1333 HOH B O 1 HETATM 10311 O O . HOH XA 10 . ? 11.652 12.036 61.486 1.00 43.51 ? 1334 HOH B O 1 HETATM 10312 O O . HOH XA 10 . ? 16.797 60.275 28.592 1.00 48.37 ? 1335 HOH B O 1 HETATM 10313 O O . HOH XA 10 . ? 32.976 17.792 34.706 1.00 39.82 ? 1336 HOH B O 1 HETATM 10314 O O . HOH XA 10 . ? 31.444 28.161 51.762 1.00 51.76 ? 1337 HOH B O 1 HETATM 10315 O O . HOH XA 10 . ? 35.215 29.549 24.693 1.00 28.93 ? 1338 HOH B O 1 HETATM 10316 O O . HOH XA 10 . ? -5.486 38.501 23.172 1.00 36.26 ? 1339 HOH B O 1 HETATM 10317 O O . HOH XA 10 . ? -5.485 41.179 35.125 1.00 35.58 ? 1340 HOH B O 1 HETATM 10318 O O . HOH XA 10 . ? 24.911 41.497 48.669 1.00 30.23 ? 1341 HOH B O 1 HETATM 10319 O O . HOH XA 10 . ? 23.918 6.463 26.616 1.00 33.33 ? 1342 HOH B O 1 HETATM 10320 O O . HOH XA 10 . ? -1.656 10.931 24.758 1.00 34.07 ? 1343 HOH B O 1 HETATM 10321 O O . HOH XA 10 . ? 27.558 24.329 5.475 1.00 34.69 ? 1344 HOH B O 1 HETATM 10322 O O . HOH XA 10 . ? 13.561 40.875 50.556 1.00 41.93 ? 1345 HOH B O 1 HETATM 10323 O O . HOH XA 10 . ? 35.690 42.753 14.495 1.00 45.58 ? 1346 HOH B O 1 HETATM 10324 O O . HOH XA 10 . ? 37.662 41.260 29.831 1.00 40.90 ? 1347 HOH B O 1 HETATM 10325 O O . HOH XA 10 . ? 20.264 31.024 -5.182 1.00 34.90 ? 1348 HOH B O 1 HETATM 10326 O O . HOH XA 10 . ? 16.149 48.417 16.314 1.00 34.78 ? 1349 HOH B O 1 HETATM 10327 O O . HOH XA 10 . ? 23.451 20.288 53.971 1.00 45.23 ? 1350 HOH B O 1 HETATM 10328 O O . HOH XA 10 . ? 26.303 49.814 32.722 1.00 36.11 ? 1351 HOH B O 1 HETATM 10329 O O . HOH XA 10 . ? -2.388 52.493 29.410 1.00 38.91 ? 1352 HOH B O 1 HETATM 10330 O O . HOH XA 10 . ? 36.617 33.742 22.366 1.00 44.53 ? 1353 HOH B O 1 HETATM 10331 O O . HOH XA 10 . ? 17.041 4.845 9.278 1.00 37.76 ? 1354 HOH B O 1 HETATM 10332 O O . HOH XA 10 . ? 17.916 17.091 38.713 1.00 27.49 ? 1355 HOH B O 1 HETATM 10333 O O . HOH XA 10 . ? -0.312 30.103 58.113 1.00 33.74 ? 1356 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 1 GLU GLU 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 LEU 559 559 559 LEU LEU A . n B 1 1 GLU 1 1 1 GLU GLU 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 LEU 559 559 559 LEU LEU 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 4 713 713 MAN MAN A . H 4 MAN 5 714 714 MAN MAN A . I 2 NAG 1 720 720 NAG NAG A . J 2 NAG 2 721 721 NAG NAG A . K 3 BMA 3 722 722 BMA BMA A . L 2 NAG 1 730 730 NAG NAG A . M 2 NAG 2 731 731 NAG NAG A . N 3 BMA 3 732 732 BMA BMA A . O 2 NAG 1 740 740 NAG NAG A . P 2 NAG 2 741 741 NAG NAG A . Q 2 NAG 1 750 750 NAG NAG A . R 2 NAG 1 760 760 NAG NAG A . S 5 NDG 1 770 770 NDG NDG A . T 6 CU 1 601 601 CU CU A . U 6 CU 1 602 602 CU CU A . V 6 CU 1 603 603 CU CU A . W 6 CU 1 604 604 CU CU A . X 7 CL 1 610 610 CL CL A . Y 8 SO4 1 800 800 SO4 SO4 A . Z 8 SO4 1 801 801 SO4 SO4 A . AA 9 OXY 1 620 620 OXY OXY A . BA 2 NAG 1 700 700 NAG NAG B . CA 2 NAG 1 710 710 NAG NAG B . DA 2 NAG 2 711 711 NAG NAG B . EA 3 BMA 3 712 712 BMA BMA B . FA 4 MAN 4 714 714 MAN MAN B . GA 2 NAG 1 720 720 NAG NAG B . HA 2 NAG 2 721 721 NAG NAG B . IA 2 NAG 1 730 730 NAG NAG B . JA 2 NAG 2 731 731 NAG NAG B . KA 3 BMA 3 732 732 BMA BMA B . LA 2 NAG 1 740 740 NAG NAG B . MA 2 NAG 2 741 741 NAG NAG B . NA 2 NAG 1 750 750 NAG NAG B . OA 2 NAG 1 760 760 NAG NAG B . PA 6 CU 1 601 601 CU CU B . QA 6 CU 1 602 602 CU CU B . RA 6 CU 1 603 603 CU CU B . SA 6 CU 1 604 604 CU CU B . TA 7 CL 1 610 610 CL CL B . UA 8 SO4 1 800 800 SO4 SO4 B . VA 9 OXY 1 620 620 OXY OXY B . WA 10 HOH 1 802 2 HOH HOH A . WA 10 HOH 2 803 3 HOH HOH A . WA 10 HOH 3 804 4 HOH HOH A . WA 10 HOH 4 805 6 HOH HOH A . WA 10 HOH 5 806 8 HOH HOH A . WA 10 HOH 6 807 9 HOH HOH A . WA 10 HOH 7 808 10 HOH HOH A . WA 10 HOH 8 809 12 HOH HOH A . WA 10 HOH 9 810 15 HOH HOH A . WA 10 HOH 10 811 16 HOH HOH A . WA 10 HOH 11 812 19 HOH HOH A . WA 10 HOH 12 813 21 HOH HOH A . WA 10 HOH 13 814 22 HOH HOH A . WA 10 HOH 14 815 23 HOH HOH A . WA 10 HOH 15 816 24 HOH HOH A . WA 10 HOH 16 817 25 HOH HOH A . WA 10 HOH 17 818 27 HOH HOH A . WA 10 HOH 18 819 29 HOH HOH A . WA 10 HOH 19 820 33 HOH HOH A . WA 10 HOH 20 821 35 HOH HOH A . WA 10 HOH 21 822 39 HOH HOH A . WA 10 HOH 22 823 40 HOH HOH A . WA 10 HOH 23 824 41 HOH HOH A . WA 10 HOH 24 825 42 HOH HOH A . WA 10 HOH 25 826 44 HOH HOH A . WA 10 HOH 26 827 45 HOH HOH A . WA 10 HOH 27 828 46 HOH HOH A . WA 10 HOH 28 829 47 HOH HOH A . WA 10 HOH 29 830 48 HOH HOH A . WA 10 HOH 30 831 49 HOH HOH A . WA 10 HOH 31 832 50 HOH HOH A . WA 10 HOH 32 833 51 HOH HOH A . WA 10 HOH 33 834 52 HOH HOH A . WA 10 HOH 34 835 54 HOH HOH A . WA 10 HOH 35 836 55 HOH HOH A . WA 10 HOH 36 837 58 HOH HOH A . WA 10 HOH 37 838 59 HOH HOH A . WA 10 HOH 38 839 60 HOH HOH A . WA 10 HOH 39 840 61 HOH HOH A . WA 10 HOH 40 841 64 HOH HOH A . WA 10 HOH 41 842 66 HOH HOH A . WA 10 HOH 42 843 69 HOH HOH A . WA 10 HOH 43 844 70 HOH HOH A . WA 10 HOH 44 845 71 HOH HOH A . WA 10 HOH 45 846 72 HOH HOH A . WA 10 HOH 46 847 73 HOH HOH A . WA 10 HOH 47 848 75 HOH HOH A . WA 10 HOH 48 849 78 HOH HOH A . WA 10 HOH 49 850 82 HOH HOH A . WA 10 HOH 50 851 83 HOH HOH A . WA 10 HOH 51 852 85 HOH HOH A . WA 10 HOH 52 853 87 HOH HOH A . WA 10 HOH 53 854 88 HOH HOH A . WA 10 HOH 54 855 90 HOH HOH A . WA 10 HOH 55 856 91 HOH HOH A . WA 10 HOH 56 857 93 HOH HOH A . WA 10 HOH 57 858 94 HOH HOH A . WA 10 HOH 58 859 99 HOH HOH A . WA 10 HOH 59 860 102 HOH HOH A . WA 10 HOH 60 861 104 HOH HOH A . WA 10 HOH 61 862 105 HOH HOH A . WA 10 HOH 62 863 108 HOH HOH A . WA 10 HOH 63 864 111 HOH HOH A . WA 10 HOH 64 865 112 HOH HOH A . WA 10 HOH 65 866 114 HOH HOH A . WA 10 HOH 66 867 115 HOH HOH A . WA 10 HOH 67 868 116 HOH HOH A . WA 10 HOH 68 869 117 HOH HOH A . WA 10 HOH 69 870 118 HOH HOH A . WA 10 HOH 70 871 120 HOH HOH A . WA 10 HOH 71 872 121 HOH HOH A . WA 10 HOH 72 873 122 HOH HOH A . WA 10 HOH 73 874 123 HOH HOH A . WA 10 HOH 74 875 124 HOH HOH A . WA 10 HOH 75 876 126 HOH HOH A . WA 10 HOH 76 877 128 HOH HOH A . WA 10 HOH 77 878 132 HOH HOH A . WA 10 HOH 78 879 134 HOH HOH A . WA 10 HOH 79 880 135 HOH HOH A . WA 10 HOH 80 881 140 HOH HOH A . WA 10 HOH 81 882 141 HOH HOH A . WA 10 HOH 82 883 142 HOH HOH A . WA 10 HOH 83 884 143 HOH HOH A . WA 10 HOH 84 885 145 HOH HOH A . WA 10 HOH 85 886 146 HOH HOH A . WA 10 HOH 86 887 147 HOH HOH A . WA 10 HOH 87 888 151 HOH HOH A . WA 10 HOH 88 889 153 HOH HOH A . WA 10 HOH 89 890 156 HOH HOH A . WA 10 HOH 90 891 159 HOH HOH A . WA 10 HOH 91 892 161 HOH HOH A . WA 10 HOH 92 893 166 HOH HOH A . WA 10 HOH 93 894 169 HOH HOH A . WA 10 HOH 94 895 173 HOH HOH A . WA 10 HOH 95 896 174 HOH HOH A . WA 10 HOH 96 897 176 HOH HOH A . WA 10 HOH 97 898 177 HOH HOH A . WA 10 HOH 98 899 178 HOH HOH A . WA 10 HOH 99 900 179 HOH HOH A . WA 10 HOH 100 901 180 HOH HOH A . WA 10 HOH 101 902 181 HOH HOH A . WA 10 HOH 102 903 183 HOH HOH A . WA 10 HOH 103 904 184 HOH HOH A . WA 10 HOH 104 905 187 HOH HOH A . WA 10 HOH 105 906 188 HOH HOH A . WA 10 HOH 106 907 189 HOH HOH A . WA 10 HOH 107 908 190 HOH HOH A . WA 10 HOH 108 909 194 HOH HOH A . WA 10 HOH 109 910 195 HOH HOH A . WA 10 HOH 110 911 197 HOH HOH A . WA 10 HOH 111 912 198 HOH HOH A . WA 10 HOH 112 913 202 HOH HOH A . WA 10 HOH 113 914 203 HOH HOH A . WA 10 HOH 114 915 204 HOH HOH A . WA 10 HOH 115 916 206 HOH HOH A . WA 10 HOH 116 917 207 HOH HOH A . WA 10 HOH 117 918 208 HOH HOH A . WA 10 HOH 118 919 209 HOH HOH A . WA 10 HOH 119 920 210 HOH HOH A . WA 10 HOH 120 921 211 HOH HOH A . WA 10 HOH 121 922 212 HOH HOH A . WA 10 HOH 122 923 214 HOH HOH A . WA 10 HOH 123 924 215 HOH HOH A . WA 10 HOH 124 925 218 HOH HOH A . WA 10 HOH 125 926 220 HOH HOH A . WA 10 HOH 126 927 221 HOH HOH A . WA 10 HOH 127 928 222 HOH HOH A . WA 10 HOH 128 929 224 HOH HOH A . WA 10 HOH 129 930 225 HOH HOH A . WA 10 HOH 130 931 227 HOH HOH A . WA 10 HOH 131 932 229 HOH HOH A . WA 10 HOH 132 933 230 HOH HOH A . WA 10 HOH 133 934 236 HOH HOH A . WA 10 HOH 134 935 237 HOH HOH A . WA 10 HOH 135 936 240 HOH HOH A . WA 10 HOH 136 937 242 HOH HOH A . WA 10 HOH 137 938 244 HOH HOH A . WA 10 HOH 138 939 249 HOH HOH A . WA 10 HOH 139 940 250 HOH HOH A . WA 10 HOH 140 941 252 HOH HOH A . WA 10 HOH 141 942 258 HOH HOH A . WA 10 HOH 142 943 259 HOH HOH A . WA 10 HOH 143 944 260 HOH HOH A . WA 10 HOH 144 945 264 HOH HOH A . WA 10 HOH 145 946 266 HOH HOH A . WA 10 HOH 146 947 267 HOH HOH A . WA 10 HOH 147 948 269 HOH HOH A . WA 10 HOH 148 949 270 HOH HOH A . WA 10 HOH 149 950 271 HOH HOH A . WA 10 HOH 150 951 272 HOH HOH A . WA 10 HOH 151 952 273 HOH HOH A . WA 10 HOH 152 953 275 HOH HOH A . WA 10 HOH 153 954 277 HOH HOH A . WA 10 HOH 154 955 280 HOH HOH A . WA 10 HOH 155 956 281 HOH HOH A . WA 10 HOH 156 957 283 HOH HOH A . WA 10 HOH 157 958 284 HOH HOH A . WA 10 HOH 158 959 285 HOH HOH A . WA 10 HOH 159 960 287 HOH HOH A . WA 10 HOH 160 961 289 HOH HOH A . WA 10 HOH 161 962 292 HOH HOH A . WA 10 HOH 162 963 293 HOH HOH A . WA 10 HOH 163 964 295 HOH HOH A . WA 10 HOH 164 965 297 HOH HOH A . WA 10 HOH 165 966 298 HOH HOH A . WA 10 HOH 166 967 299 HOH HOH A . WA 10 HOH 167 968 300 HOH HOH A . WA 10 HOH 168 969 301 HOH HOH A . WA 10 HOH 169 970 305 HOH HOH A . WA 10 HOH 170 971 306 HOH HOH A . WA 10 HOH 171 972 307 HOH HOH A . WA 10 HOH 172 973 311 HOH HOH A . WA 10 HOH 173 974 312 HOH HOH A . WA 10 HOH 174 975 315 HOH HOH A . WA 10 HOH 175 976 317 HOH HOH A . WA 10 HOH 176 977 318 HOH HOH A . WA 10 HOH 177 978 323 HOH HOH A . WA 10 HOH 178 979 324 HOH HOH A . WA 10 HOH 179 980 325 HOH HOH A . WA 10 HOH 180 981 326 HOH HOH A . WA 10 HOH 181 982 328 HOH HOH A . WA 10 HOH 182 983 331 HOH HOH A . WA 10 HOH 183 984 332 HOH HOH A . WA 10 HOH 184 985 336 HOH HOH A . WA 10 HOH 185 986 340 HOH HOH A . WA 10 HOH 186 987 341 HOH HOH A . WA 10 HOH 187 988 343 HOH HOH A . WA 10 HOH 188 989 348 HOH HOH A . WA 10 HOH 189 990 349 HOH HOH A . WA 10 HOH 190 991 351 HOH HOH A . WA 10 HOH 191 992 356 HOH HOH A . WA 10 HOH 192 993 358 HOH HOH A . WA 10 HOH 193 994 360 HOH HOH A . WA 10 HOH 194 995 362 HOH HOH A . WA 10 HOH 195 996 364 HOH HOH A . WA 10 HOH 196 997 366 HOH HOH A . WA 10 HOH 197 998 368 HOH HOH A . WA 10 HOH 198 999 369 HOH HOH A . WA 10 HOH 199 1000 370 HOH HOH A . WA 10 HOH 200 1001 371 HOH HOH A . WA 10 HOH 201 1002 372 HOH HOH A . WA 10 HOH 202 1003 373 HOH HOH A . WA 10 HOH 203 1004 374 HOH HOH A . WA 10 HOH 204 1005 376 HOH HOH A . WA 10 HOH 205 1006 377 HOH HOH A . WA 10 HOH 206 1007 378 HOH HOH A . WA 10 HOH 207 1008 380 HOH HOH A . WA 10 HOH 208 1009 382 HOH HOH A . WA 10 HOH 209 1010 383 HOH HOH A . WA 10 HOH 210 1011 384 HOH HOH A . WA 10 HOH 211 1012 385 HOH HOH A . WA 10 HOH 212 1013 387 HOH HOH A . WA 10 HOH 213 1014 388 HOH HOH A . WA 10 HOH 214 1015 389 HOH HOH A . WA 10 HOH 215 1016 392 HOH HOH A . WA 10 HOH 216 1017 395 HOH HOH A . WA 10 HOH 217 1018 397 HOH HOH A . WA 10 HOH 218 1019 398 HOH HOH A . WA 10 HOH 219 1020 399 HOH HOH A . WA 10 HOH 220 1021 402 HOH HOH A . WA 10 HOH 221 1022 404 HOH HOH A . WA 10 HOH 222 1023 405 HOH HOH A . WA 10 HOH 223 1024 406 HOH HOH A . WA 10 HOH 224 1025 410 HOH HOH A . WA 10 HOH 225 1026 411 HOH HOH A . WA 10 HOH 226 1027 412 HOH HOH A . WA 10 HOH 227 1028 413 HOH HOH A . WA 10 HOH 228 1029 418 HOH HOH A . WA 10 HOH 229 1030 420 HOH HOH A . WA 10 HOH 230 1031 421 HOH HOH A . WA 10 HOH 231 1032 422 HOH HOH A . WA 10 HOH 232 1033 424 HOH HOH A . WA 10 HOH 233 1034 426 HOH HOH A . WA 10 HOH 234 1035 427 HOH HOH A . WA 10 HOH 235 1036 429 HOH HOH A . WA 10 HOH 236 1037 432 HOH HOH A . WA 10 HOH 237 1038 435 HOH HOH A . WA 10 HOH 238 1039 436 HOH HOH A . WA 10 HOH 239 1040 437 HOH HOH A . WA 10 HOH 240 1041 439 HOH HOH A . WA 10 HOH 241 1042 441 HOH HOH A . WA 10 HOH 242 1043 442 HOH HOH A . WA 10 HOH 243 1044 443 HOH HOH A . WA 10 HOH 244 1045 444 HOH HOH A . WA 10 HOH 245 1046 445 HOH HOH A . WA 10 HOH 246 1047 446 HOH HOH A . WA 10 HOH 247 1048 449 HOH HOH A . WA 10 HOH 248 1049 450 HOH HOH A . WA 10 HOH 249 1050 451 HOH HOH A . WA 10 HOH 250 1051 453 HOH HOH A . WA 10 HOH 251 1052 454 HOH HOH A . WA 10 HOH 252 1053 455 HOH HOH A . WA 10 HOH 253 1054 456 HOH HOH A . WA 10 HOH 254 1055 460 HOH HOH A . WA 10 HOH 255 1056 462 HOH HOH A . WA 10 HOH 256 1057 463 HOH HOH A . WA 10 HOH 257 1058 466 HOH HOH A . WA 10 HOH 258 1059 468 HOH HOH A . WA 10 HOH 259 1060 470 HOH HOH A . WA 10 HOH 260 1061 471 HOH HOH A . WA 10 HOH 261 1062 475 HOH HOH A . WA 10 HOH 262 1063 476 HOH HOH A . WA 10 HOH 263 1064 477 HOH HOH A . WA 10 HOH 264 1065 479 HOH HOH A . WA 10 HOH 265 1066 480 HOH HOH A . WA 10 HOH 266 1067 482 HOH HOH A . WA 10 HOH 267 1068 483 HOH HOH A . WA 10 HOH 268 1069 485 HOH HOH A . WA 10 HOH 269 1070 486 HOH HOH A . WA 10 HOH 270 1071 489 HOH HOH A . WA 10 HOH 271 1072 490 HOH HOH A . WA 10 HOH 272 1073 492 HOH HOH A . WA 10 HOH 273 1074 493 HOH HOH A . WA 10 HOH 274 1075 494 HOH HOH A . WA 10 HOH 275 1076 495 HOH HOH A . WA 10 HOH 276 1077 499 HOH HOH A . WA 10 HOH 277 1078 503 HOH HOH A . WA 10 HOH 278 1079 504 HOH HOH A . WA 10 HOH 279 1080 505 HOH HOH A . WA 10 HOH 280 1081 506 HOH HOH A . WA 10 HOH 281 1082 512 HOH HOH A . WA 10 HOH 282 1083 513 HOH HOH A . WA 10 HOH 283 1084 515 HOH HOH A . WA 10 HOH 284 1085 516 HOH HOH A . WA 10 HOH 285 1086 518 HOH HOH A . WA 10 HOH 286 1087 520 HOH HOH A . WA 10 HOH 287 1088 522 HOH HOH A . WA 10 HOH 288 1089 525 HOH HOH A . WA 10 HOH 289 1090 527 HOH HOH A . WA 10 HOH 290 1091 528 HOH HOH A . WA 10 HOH 291 1092 532 HOH HOH A . WA 10 HOH 292 1093 533 HOH HOH A . WA 10 HOH 293 1094 534 HOH HOH A . WA 10 HOH 294 1095 536 HOH HOH A . WA 10 HOH 295 1096 538 HOH HOH A . WA 10 HOH 296 1097 540 HOH HOH A . WA 10 HOH 297 1098 541 HOH HOH A . WA 10 HOH 298 1099 542 HOH HOH A . WA 10 HOH 299 1100 544 HOH HOH A . WA 10 HOH 300 1101 545 HOH HOH A . WA 10 HOH 301 1102 548 HOH HOH A . WA 10 HOH 302 1103 550 HOH HOH A . WA 10 HOH 303 1104 552 HOH HOH A . WA 10 HOH 304 1105 554 HOH HOH A . WA 10 HOH 305 1106 557 HOH HOH A . WA 10 HOH 306 1107 561 HOH HOH A . WA 10 HOH 307 1108 562 HOH HOH A . WA 10 HOH 308 1109 563 HOH HOH A . WA 10 HOH 309 1110 565 HOH HOH A . WA 10 HOH 310 1111 566 HOH HOH A . WA 10 HOH 311 1112 567 HOH HOH A . WA 10 HOH 312 1113 569 HOH HOH A . WA 10 HOH 313 1114 570 HOH HOH A . WA 10 HOH 314 1115 573 HOH HOH A . WA 10 HOH 315 1116 575 HOH HOH A . WA 10 HOH 316 1117 577 HOH HOH A . WA 10 HOH 317 1118 579 HOH HOH A . WA 10 HOH 318 1119 580 HOH HOH A . WA 10 HOH 319 1120 584 HOH HOH A . WA 10 HOH 320 1121 587 HOH HOH A . WA 10 HOH 321 1122 588 HOH HOH A . WA 10 HOH 322 1123 591 HOH HOH A . WA 10 HOH 323 1124 593 HOH HOH A . WA 10 HOH 324 1125 594 HOH HOH A . WA 10 HOH 325 1126 595 HOH HOH A . WA 10 HOH 326 1127 596 HOH HOH A . WA 10 HOH 327 1128 597 HOH HOH A . WA 10 HOH 328 1129 601 HOH HOH A . WA 10 HOH 329 1130 602 HOH HOH A . WA 10 HOH 330 1131 603 HOH HOH A . WA 10 HOH 331 1132 604 HOH HOH A . WA 10 HOH 332 1133 606 HOH HOH A . WA 10 HOH 333 1134 607 HOH HOH A . WA 10 HOH 334 1135 608 HOH HOH A . WA 10 HOH 335 1136 611 HOH HOH A . WA 10 HOH 336 1137 617 HOH HOH A . WA 10 HOH 337 1138 618 HOH HOH A . WA 10 HOH 338 1139 620 HOH HOH A . WA 10 HOH 339 1140 621 HOH HOH A . WA 10 HOH 340 1141 624 HOH HOH A . WA 10 HOH 341 1142 628 HOH HOH A . WA 10 HOH 342 1143 629 HOH HOH A . WA 10 HOH 343 1144 631 HOH HOH A . WA 10 HOH 344 1145 633 HOH HOH A . WA 10 HOH 345 1146 636 HOH HOH A . WA 10 HOH 346 1147 637 HOH HOH A . WA 10 HOH 347 1148 638 HOH HOH A . WA 10 HOH 348 1149 639 HOH HOH A . WA 10 HOH 349 1150 640 HOH HOH A . WA 10 HOH 350 1151 643 HOH HOH A . WA 10 HOH 351 1152 646 HOH HOH A . WA 10 HOH 352 1153 647 HOH HOH A . WA 10 HOH 353 1154 648 HOH HOH A . WA 10 HOH 354 1155 651 HOH HOH A . WA 10 HOH 355 1156 653 HOH HOH A . WA 10 HOH 356 1157 655 HOH HOH A . WA 10 HOH 357 1158 657 HOH HOH A . WA 10 HOH 358 1159 662 HOH HOH A . WA 10 HOH 359 1160 663 HOH HOH A . WA 10 HOH 360 1161 664 HOH HOH A . WA 10 HOH 361 1162 667 HOH HOH A . WA 10 HOH 362 1163 669 HOH HOH A . WA 10 HOH 363 1164 670 HOH HOH A . WA 10 HOH 364 1165 671 HOH HOH A . WA 10 HOH 365 1166 672 HOH HOH A . WA 10 HOH 366 1167 673 HOH HOH A . WA 10 HOH 367 1168 676 HOH HOH A . WA 10 HOH 368 1169 678 HOH HOH A . WA 10 HOH 369 1170 679 HOH HOH A . WA 10 HOH 370 1171 681 HOH HOH A . WA 10 HOH 371 1172 683 HOH HOH A . WA 10 HOH 372 1173 684 HOH HOH A . WA 10 HOH 373 1174 686 HOH HOH A . WA 10 HOH 374 1175 687 HOH HOH A . WA 10 HOH 375 1176 688 HOH HOH A . WA 10 HOH 376 1177 689 HOH HOH A . WA 10 HOH 377 1178 696 HOH HOH A . WA 10 HOH 378 1179 698 HOH HOH A . WA 10 HOH 379 1180 699 HOH HOH A . WA 10 HOH 380 1181 700 HOH HOH A . WA 10 HOH 381 1182 702 HOH HOH A . WA 10 HOH 382 1183 704 HOH HOH A . WA 10 HOH 383 1184 705 HOH HOH A . WA 10 HOH 384 1185 709 HOH HOH A . WA 10 HOH 385 1186 717 HOH HOH A . WA 10 HOH 386 1187 718 HOH HOH A . WA 10 HOH 387 1188 719 HOH HOH A . WA 10 HOH 388 1189 722 HOH HOH A . WA 10 HOH 389 1190 723 HOH HOH A . WA 10 HOH 390 1191 725 HOH HOH A . WA 10 HOH 391 1192 726 HOH HOH A . WA 10 HOH 392 1193 728 HOH HOH A . WA 10 HOH 393 1194 731 HOH HOH A . WA 10 HOH 394 1195 733 HOH HOH A . WA 10 HOH 395 1196 734 HOH HOH A . WA 10 HOH 396 1197 737 HOH HOH A . WA 10 HOH 397 1198 741 HOH HOH A . WA 10 HOH 398 1199 745 HOH HOH A . WA 10 HOH 399 1200 746 HOH HOH A . WA 10 HOH 400 1201 747 HOH HOH A . WA 10 HOH 401 1202 748 HOH HOH A . WA 10 HOH 402 1203 750 HOH HOH A . WA 10 HOH 403 1204 753 HOH HOH A . WA 10 HOH 404 1205 756 HOH HOH A . WA 10 HOH 405 1206 757 HOH HOH A . WA 10 HOH 406 1207 758 HOH HOH A . WA 10 HOH 407 1208 763 HOH HOH A . WA 10 HOH 408 1209 767 HOH HOH A . WA 10 HOH 409 1210 768 HOH HOH A . WA 10 HOH 410 1211 771 HOH HOH A . WA 10 HOH 411 1212 773 HOH HOH A . WA 10 HOH 412 1213 777 HOH HOH A . WA 10 HOH 413 1214 779 HOH HOH A . WA 10 HOH 414 1215 781 HOH HOH A . WA 10 HOH 415 1216 784 HOH HOH A . WA 10 HOH 416 1217 787 HOH HOH A . WA 10 HOH 417 1218 789 HOH HOH A . WA 10 HOH 418 1219 791 HOH HOH A . WA 10 HOH 419 1220 792 HOH HOH A . WA 10 HOH 420 1221 795 HOH HOH A . WA 10 HOH 421 1222 802 HOH HOH A . WA 10 HOH 422 1223 803 HOH HOH A . WA 10 HOH 423 1224 804 HOH HOH A . WA 10 HOH 424 1225 806 HOH HOH A . WA 10 HOH 425 1226 811 HOH HOH A . WA 10 HOH 426 1227 813 HOH HOH A . WA 10 HOH 427 1228 814 HOH HOH A . WA 10 HOH 428 1229 815 HOH HOH A . WA 10 HOH 429 1230 817 HOH HOH A . WA 10 HOH 430 1231 819 HOH HOH A . WA 10 HOH 431 1232 822 HOH HOH A . WA 10 HOH 432 1233 825 HOH HOH A . WA 10 HOH 433 1234 829 HOH HOH A . WA 10 HOH 434 1235 830 HOH HOH A . WA 10 HOH 435 1236 832 HOH HOH A . WA 10 HOH 436 1237 835 HOH HOH A . WA 10 HOH 437 1238 836 HOH HOH A . WA 10 HOH 438 1239 842 HOH HOH A . WA 10 HOH 439 1240 844 HOH HOH A . WA 10 HOH 440 1241 847 HOH HOH A . WA 10 HOH 441 1242 849 HOH HOH A . WA 10 HOH 442 1243 851 HOH HOH A . WA 10 HOH 443 1244 852 HOH HOH A . WA 10 HOH 444 1245 853 HOH HOH A . WA 10 HOH 445 1246 855 HOH HOH A . WA 10 HOH 446 1247 861 HOH HOH A . WA 10 HOH 447 1248 864 HOH HOH A . WA 10 HOH 448 1249 866 HOH HOH A . WA 10 HOH 449 1250 868 HOH HOH A . WA 10 HOH 450 1251 869 HOH HOH A . WA 10 HOH 451 1252 871 HOH HOH A . WA 10 HOH 452 1253 872 HOH HOH A . WA 10 HOH 453 1254 873 HOH HOH A . WA 10 HOH 454 1255 874 HOH HOH A . WA 10 HOH 455 1256 875 HOH HOH A . WA 10 HOH 456 1257 876 HOH HOH A . WA 10 HOH 457 1258 877 HOH HOH A . WA 10 HOH 458 1259 880 HOH HOH A . WA 10 HOH 459 1260 882 HOH HOH A . WA 10 HOH 460 1261 886 HOH HOH A . WA 10 HOH 461 1262 888 HOH HOH A . WA 10 HOH 462 1263 890 HOH HOH A . WA 10 HOH 463 1264 891 HOH HOH A . WA 10 HOH 464 1265 892 HOH HOH A . WA 10 HOH 465 1266 896 HOH HOH A . WA 10 HOH 466 1267 897 HOH HOH A . WA 10 HOH 467 1268 898 HOH HOH A . WA 10 HOH 468 1269 899 HOH HOH A . WA 10 HOH 469 1270 900 HOH HOH A . WA 10 HOH 470 1271 901 HOH HOH A . WA 10 HOH 471 1272 903 HOH HOH A . WA 10 HOH 472 1273 904 HOH HOH A . WA 10 HOH 473 1274 907 HOH HOH A . WA 10 HOH 474 1275 909 HOH HOH A . WA 10 HOH 475 1276 910 HOH HOH A . WA 10 HOH 476 1277 912 HOH HOH A . WA 10 HOH 477 1278 913 HOH HOH A . WA 10 HOH 478 1279 915 HOH HOH A . WA 10 HOH 479 1280 916 HOH HOH A . WA 10 HOH 480 1281 918 HOH HOH A . WA 10 HOH 481 1282 920 HOH HOH A . WA 10 HOH 482 1283 921 HOH HOH A . WA 10 HOH 483 1284 923 HOH HOH A . WA 10 HOH 484 1285 928 HOH HOH A . WA 10 HOH 485 1286 929 HOH HOH A . WA 10 HOH 486 1287 931 HOH HOH A . WA 10 HOH 487 1288 932 HOH HOH A . WA 10 HOH 488 1289 933 HOH HOH A . WA 10 HOH 489 1290 937 HOH HOH A . WA 10 HOH 490 1291 938 HOH HOH A . WA 10 HOH 491 1292 941 HOH HOH A . WA 10 HOH 492 1293 942 HOH HOH A . WA 10 HOH 493 1294 943 HOH HOH A . WA 10 HOH 494 1295 944 HOH HOH A . WA 10 HOH 495 1296 948 HOH HOH A . WA 10 HOH 496 1297 953 HOH HOH A . WA 10 HOH 497 1298 956 HOH HOH A . WA 10 HOH 498 1299 957 HOH HOH A . WA 10 HOH 499 1300 958 HOH HOH A . WA 10 HOH 500 1301 959 HOH HOH A . WA 10 HOH 501 1302 961 HOH HOH A . WA 10 HOH 502 1303 963 HOH HOH A . WA 10 HOH 503 1304 964 HOH HOH A . WA 10 HOH 504 1305 967 HOH HOH A . WA 10 HOH 505 1306 970 HOH HOH A . WA 10 HOH 506 1307 971 HOH HOH A . WA 10 HOH 507 1308 973 HOH HOH A . WA 10 HOH 508 1309 974 HOH HOH A . WA 10 HOH 509 1310 975 HOH HOH A . WA 10 HOH 510 1311 978 HOH HOH A . WA 10 HOH 511 1312 979 HOH HOH A . WA 10 HOH 512 1313 982 HOH HOH A . WA 10 HOH 513 1314 986 HOH HOH A . WA 10 HOH 514 1315 987 HOH HOH A . WA 10 HOH 515 1316 989 HOH HOH A . WA 10 HOH 516 1317 990 HOH HOH A . WA 10 HOH 517 1318 991 HOH HOH A . WA 10 HOH 518 1319 994 HOH HOH A . WA 10 HOH 519 1320 995 HOH HOH A . WA 10 HOH 520 1321 996 HOH HOH A . WA 10 HOH 521 1322 998 HOH HOH A . WA 10 HOH 522 1323 999 HOH HOH A . WA 10 HOH 523 1324 1001 HOH HOH A . WA 10 HOH 524 1325 1003 HOH HOH A . WA 10 HOH 525 1326 1004 HOH HOH A . WA 10 HOH 526 1327 1005 HOH HOH A . WA 10 HOH 527 1328 1010 HOH HOH A . WA 10 HOH 528 1329 1013 HOH HOH A . WA 10 HOH 529 1330 1015 HOH HOH A . WA 10 HOH 530 1331 1016 HOH HOH A . WA 10 HOH 531 1332 1017 HOH HOH A . WA 10 HOH 532 1333 1018 HOH HOH A . WA 10 HOH 533 1334 1019 HOH HOH A . WA 10 HOH 534 1335 1020 HOH HOH A . WA 10 HOH 535 1336 1027 HOH HOH A . WA 10 HOH 536 1337 1029 HOH HOH A . WA 10 HOH 537 1338 1030 HOH HOH A . WA 10 HOH 538 1339 1031 HOH HOH A . WA 10 HOH 539 1340 1033 HOH HOH A . WA 10 HOH 540 1341 1034 HOH HOH A . WA 10 HOH 541 1342 1036 HOH HOH A . WA 10 HOH 542 1343 1043 HOH HOH A . WA 10 HOH 543 1344 1044 HOH HOH A . WA 10 HOH 544 1345 1046 HOH HOH A . WA 10 HOH 545 1346 1048 HOH HOH A . WA 10 HOH 546 1347 1049 HOH HOH A . WA 10 HOH 547 1348 1050 HOH HOH A . WA 10 HOH 548 1349 1053 HOH HOH A . WA 10 HOH 549 1350 1055 HOH HOH A . WA 10 HOH 550 1351 1056 HOH HOH A . WA 10 HOH 551 1352 1058 HOH HOH A . WA 10 HOH 552 1353 1059 HOH HOH A . WA 10 HOH 553 1354 1065 HOH HOH A . WA 10 HOH 554 1355 1066 HOH HOH A . WA 10 HOH 555 1356 1068 HOH HOH A . WA 10 HOH 556 1357 1069 HOH HOH A . WA 10 HOH 557 1358 1072 HOH HOH A . WA 10 HOH 558 1359 1074 HOH HOH A . WA 10 HOH 559 1360 1077 HOH HOH A . WA 10 HOH 560 1361 1079 HOH HOH A . WA 10 HOH 561 1362 1080 HOH HOH A . WA 10 HOH 562 1363 1082 HOH HOH A . WA 10 HOH 563 1364 1085 HOH HOH A . WA 10 HOH 564 1365 1086 HOH HOH A . WA 10 HOH 565 1366 1087 HOH HOH A . WA 10 HOH 566 1367 1088 HOH HOH A . WA 10 HOH 567 1368 1089 HOH HOH A . WA 10 HOH 568 1369 1090 HOH HOH A . WA 10 HOH 569 1370 1092 HOH HOH A . WA 10 HOH 570 1371 1094 HOH HOH A . WA 10 HOH 571 1372 1096 HOH HOH A . WA 10 HOH 572 1373 1100 HOH HOH A . WA 10 HOH 573 1374 1101 HOH HOH A . WA 10 HOH 574 1375 1104 HOH HOH A . WA 10 HOH 575 1376 1105 HOH HOH A . WA 10 HOH 576 1377 1109 HOH HOH A . WA 10 HOH 577 1378 1111 HOH HOH A . WA 10 HOH 578 1379 1113 HOH HOH A . WA 10 HOH 579 1380 1115 HOH HOH A . WA 10 HOH 580 1381 1117 HOH HOH A . WA 10 HOH 581 1382 1118 HOH HOH A . WA 10 HOH 582 1383 1120 HOH HOH A . WA 10 HOH 583 1384 1123 HOH HOH A . WA 10 HOH 584 1385 1129 HOH HOH A . WA 10 HOH 585 1386 1134 HOH HOH A . WA 10 HOH 586 1387 1135 HOH HOH A . WA 10 HOH 587 1388 1137 HOH HOH A . WA 10 HOH 588 1389 1139 HOH HOH A . WA 10 HOH 589 1390 1141 HOH HOH A . WA 10 HOH 590 1391 1142 HOH HOH A . WA 10 HOH 591 1392 1145 HOH HOH A . WA 10 HOH 592 1393 1149 HOH HOH A . WA 10 HOH 593 1394 1151 HOH HOH A . WA 10 HOH 594 1395 1153 HOH HOH A . WA 10 HOH 595 1396 1154 HOH HOH A . WA 10 HOH 596 1397 1157 HOH HOH A . WA 10 HOH 597 1398 1159 HOH HOH A . WA 10 HOH 598 1399 1164 HOH HOH A . WA 10 HOH 599 1400 1165 HOH HOH A . WA 10 HOH 600 1401 1166 HOH HOH A . XA 10 HOH 1 801 1 HOH HOH B . XA 10 HOH 2 802 5 HOH HOH B . XA 10 HOH 3 803 7 HOH HOH B . XA 10 HOH 4 804 11 HOH HOH B . XA 10 HOH 5 805 13 HOH HOH B . XA 10 HOH 6 806 14 HOH HOH B . XA 10 HOH 7 807 18 HOH HOH B . XA 10 HOH 8 808 20 HOH HOH B . XA 10 HOH 9 809 26 HOH HOH B . XA 10 HOH 10 810 28 HOH HOH B . XA 10 HOH 11 811 30 HOH HOH B . XA 10 HOH 12 812 31 HOH HOH B . XA 10 HOH 13 813 32 HOH HOH B . XA 10 HOH 14 814 34 HOH HOH B . XA 10 HOH 15 815 36 HOH HOH B . XA 10 HOH 16 816 37 HOH HOH B . XA 10 HOH 17 817 38 HOH HOH B . XA 10 HOH 18 818 43 HOH HOH B . XA 10 HOH 19 819 53 HOH HOH B . XA 10 HOH 20 820 56 HOH HOH B . XA 10 HOH 21 821 57 HOH HOH B . XA 10 HOH 22 822 62 HOH HOH B . XA 10 HOH 23 823 63 HOH HOH B . XA 10 HOH 24 824 65 HOH HOH B . XA 10 HOH 25 825 67 HOH HOH B . XA 10 HOH 26 826 68 HOH HOH B . XA 10 HOH 27 827 74 HOH HOH B . XA 10 HOH 28 828 76 HOH HOH B . XA 10 HOH 29 829 77 HOH HOH B . XA 10 HOH 30 830 79 HOH HOH B . XA 10 HOH 31 831 80 HOH HOH B . XA 10 HOH 32 832 81 HOH HOH B . XA 10 HOH 33 833 84 HOH HOH B . XA 10 HOH 34 834 86 HOH HOH B . XA 10 HOH 35 835 89 HOH HOH B . XA 10 HOH 36 836 92 HOH HOH B . XA 10 HOH 37 837 95 HOH HOH B . XA 10 HOH 38 838 96 HOH HOH B . XA 10 HOH 39 839 97 HOH HOH B . XA 10 HOH 40 840 98 HOH HOH B . XA 10 HOH 41 841 100 HOH HOH B . XA 10 HOH 42 842 101 HOH HOH B . XA 10 HOH 43 843 103 HOH HOH B . XA 10 HOH 44 844 106 HOH HOH B . XA 10 HOH 45 845 107 HOH HOH B . XA 10 HOH 46 846 109 HOH HOH B . XA 10 HOH 47 847 110 HOH HOH B . XA 10 HOH 48 848 113 HOH HOH B . XA 10 HOH 49 849 119 HOH HOH B . XA 10 HOH 50 850 125 HOH HOH B . XA 10 HOH 51 851 127 HOH HOH B . XA 10 HOH 52 852 129 HOH HOH B . XA 10 HOH 53 853 130 HOH HOH B . XA 10 HOH 54 854 131 HOH HOH B . XA 10 HOH 55 855 133 HOH HOH B . XA 10 HOH 56 856 136 HOH HOH B . XA 10 HOH 57 857 137 HOH HOH B . XA 10 HOH 58 858 138 HOH HOH B . XA 10 HOH 59 859 139 HOH HOH B . XA 10 HOH 60 860 144 HOH HOH B . XA 10 HOH 61 861 148 HOH HOH B . XA 10 HOH 62 862 149 HOH HOH B . XA 10 HOH 63 863 150 HOH HOH B . XA 10 HOH 64 864 152 HOH HOH B . XA 10 HOH 65 865 154 HOH HOH B . XA 10 HOH 66 866 155 HOH HOH B . XA 10 HOH 67 867 157 HOH HOH B . XA 10 HOH 68 868 158 HOH HOH B . XA 10 HOH 69 869 160 HOH HOH B . XA 10 HOH 70 870 162 HOH HOH B . XA 10 HOH 71 871 163 HOH HOH B . XA 10 HOH 72 872 164 HOH HOH B . XA 10 HOH 73 873 165 HOH HOH B . XA 10 HOH 74 874 167 HOH HOH B . XA 10 HOH 75 875 168 HOH HOH B . XA 10 HOH 76 876 170 HOH HOH B . XA 10 HOH 77 877 171 HOH HOH B . XA 10 HOH 78 878 172 HOH HOH B . XA 10 HOH 79 879 175 HOH HOH B . XA 10 HOH 80 880 182 HOH HOH B . XA 10 HOH 81 881 185 HOH HOH B . XA 10 HOH 82 882 186 HOH HOH B . XA 10 HOH 83 883 191 HOH HOH B . XA 10 HOH 84 884 192 HOH HOH B . XA 10 HOH 85 885 193 HOH HOH B . XA 10 HOH 86 886 196 HOH HOH B . XA 10 HOH 87 887 199 HOH HOH B . XA 10 HOH 88 888 200 HOH HOH B . XA 10 HOH 89 889 201 HOH HOH B . XA 10 HOH 90 890 205 HOH HOH B . XA 10 HOH 91 891 213 HOH HOH B . XA 10 HOH 92 892 216 HOH HOH B . XA 10 HOH 93 893 217 HOH HOH B . XA 10 HOH 94 894 219 HOH HOH B . XA 10 HOH 95 895 223 HOH HOH B . XA 10 HOH 96 896 226 HOH HOH B . XA 10 HOH 97 897 228 HOH HOH B . XA 10 HOH 98 898 231 HOH HOH B . XA 10 HOH 99 899 232 HOH HOH B . XA 10 HOH 100 900 233 HOH HOH B . XA 10 HOH 101 901 234 HOH HOH B . XA 10 HOH 102 902 235 HOH HOH B . XA 10 HOH 103 903 238 HOH HOH B . XA 10 HOH 104 904 239 HOH HOH B . XA 10 HOH 105 905 241 HOH HOH B . XA 10 HOH 106 906 243 HOH HOH B . XA 10 HOH 107 907 245 HOH HOH B . XA 10 HOH 108 908 246 HOH HOH B . XA 10 HOH 109 909 247 HOH HOH B . XA 10 HOH 110 910 248 HOH HOH B . XA 10 HOH 111 911 251 HOH HOH B . XA 10 HOH 112 912 253 HOH HOH B . XA 10 HOH 113 913 254 HOH HOH B . XA 10 HOH 114 914 255 HOH HOH B . XA 10 HOH 115 915 256 HOH HOH B . XA 10 HOH 116 916 257 HOH HOH B . XA 10 HOH 117 917 261 HOH HOH B . XA 10 HOH 118 918 262 HOH HOH B . XA 10 HOH 119 919 263 HOH HOH B . XA 10 HOH 120 920 265 HOH HOH B . XA 10 HOH 121 921 268 HOH HOH B . XA 10 HOH 122 922 274 HOH HOH B . XA 10 HOH 123 923 276 HOH HOH B . XA 10 HOH 124 924 278 HOH HOH B . XA 10 HOH 125 925 279 HOH HOH B . XA 10 HOH 126 926 282 HOH HOH B . XA 10 HOH 127 927 286 HOH HOH B . XA 10 HOH 128 928 288 HOH HOH B . XA 10 HOH 129 929 290 HOH HOH B . XA 10 HOH 130 930 291 HOH HOH B . XA 10 HOH 131 931 294 HOH HOH B . XA 10 HOH 132 932 296 HOH HOH B . XA 10 HOH 133 933 302 HOH HOH B . XA 10 HOH 134 934 303 HOH HOH B . XA 10 HOH 135 935 304 HOH HOH B . XA 10 HOH 136 936 308 HOH HOH B . XA 10 HOH 137 937 309 HOH HOH B . XA 10 HOH 138 938 310 HOH HOH B . XA 10 HOH 139 939 313 HOH HOH B . XA 10 HOH 140 940 314 HOH HOH B . XA 10 HOH 141 941 316 HOH HOH B . XA 10 HOH 142 942 319 HOH HOH B . XA 10 HOH 143 943 320 HOH HOH B . XA 10 HOH 144 944 321 HOH HOH B . XA 10 HOH 145 945 322 HOH HOH B . XA 10 HOH 146 946 327 HOH HOH B . XA 10 HOH 147 947 329 HOH HOH B . XA 10 HOH 148 948 330 HOH HOH B . XA 10 HOH 149 949 333 HOH HOH B . XA 10 HOH 150 950 334 HOH HOH B . XA 10 HOH 151 951 335 HOH HOH B . XA 10 HOH 152 952 337 HOH HOH B . XA 10 HOH 153 953 338 HOH HOH B . XA 10 HOH 154 954 339 HOH HOH B . XA 10 HOH 155 955 342 HOH HOH B . XA 10 HOH 156 956 344 HOH HOH B . XA 10 HOH 157 957 345 HOH HOH B . XA 10 HOH 158 958 346 HOH HOH B . XA 10 HOH 159 959 347 HOH HOH B . XA 10 HOH 160 960 350 HOH HOH B . XA 10 HOH 161 961 352 HOH HOH B . XA 10 HOH 162 962 353 HOH HOH B . XA 10 HOH 163 963 354 HOH HOH B . XA 10 HOH 164 964 355 HOH HOH B . XA 10 HOH 165 965 357 HOH HOH B . XA 10 HOH 166 966 359 HOH HOH B . XA 10 HOH 167 967 361 HOH HOH B . XA 10 HOH 168 968 363 HOH HOH B . XA 10 HOH 169 969 365 HOH HOH B . XA 10 HOH 170 970 367 HOH HOH B . XA 10 HOH 171 971 375 HOH HOH B . XA 10 HOH 172 972 379 HOH HOH B . XA 10 HOH 173 973 381 HOH HOH B . XA 10 HOH 174 974 386 HOH HOH B . XA 10 HOH 175 975 390 HOH HOH B . XA 10 HOH 176 976 391 HOH HOH B . XA 10 HOH 177 977 393 HOH HOH B . XA 10 HOH 178 978 394 HOH HOH B . XA 10 HOH 179 979 396 HOH HOH B . XA 10 HOH 180 980 400 HOH HOH B . XA 10 HOH 181 981 401 HOH HOH B . XA 10 HOH 182 982 403 HOH HOH B . XA 10 HOH 183 983 407 HOH HOH B . XA 10 HOH 184 984 408 HOH HOH B . XA 10 HOH 185 985 409 HOH HOH B . XA 10 HOH 186 986 414 HOH HOH B . XA 10 HOH 187 987 415 HOH HOH B . XA 10 HOH 188 988 416 HOH HOH B . XA 10 HOH 189 989 417 HOH HOH B . XA 10 HOH 190 990 419 HOH HOH B . XA 10 HOH 191 991 423 HOH HOH B . XA 10 HOH 192 992 425 HOH HOH B . XA 10 HOH 193 993 428 HOH HOH B . XA 10 HOH 194 994 430 HOH HOH B . XA 10 HOH 195 995 431 HOH HOH B . XA 10 HOH 196 996 433 HOH HOH B . XA 10 HOH 197 997 434 HOH HOH B . XA 10 HOH 198 998 438 HOH HOH B . XA 10 HOH 199 999 440 HOH HOH B . XA 10 HOH 200 1000 447 HOH HOH B . XA 10 HOH 201 1001 448 HOH HOH B . XA 10 HOH 202 1002 452 HOH HOH B . XA 10 HOH 203 1003 457 HOH HOH B . XA 10 HOH 204 1004 458 HOH HOH B . XA 10 HOH 205 1005 459 HOH HOH B . XA 10 HOH 206 1006 461 HOH HOH B . XA 10 HOH 207 1007 464 HOH HOH B . XA 10 HOH 208 1008 465 HOH HOH B . XA 10 HOH 209 1009 467 HOH HOH B . XA 10 HOH 210 1010 469 HOH HOH B . XA 10 HOH 211 1011 472 HOH HOH B . XA 10 HOH 212 1012 473 HOH HOH B . XA 10 HOH 213 1013 474 HOH HOH B . XA 10 HOH 214 1014 478 HOH HOH B . XA 10 HOH 215 1015 481 HOH HOH B . XA 10 HOH 216 1016 484 HOH HOH B . XA 10 HOH 217 1017 487 HOH HOH B . XA 10 HOH 218 1018 488 HOH HOH B . XA 10 HOH 219 1019 491 HOH HOH B . XA 10 HOH 220 1020 496 HOH HOH B . XA 10 HOH 221 1021 497 HOH HOH B . XA 10 HOH 222 1022 498 HOH HOH B . XA 10 HOH 223 1023 500 HOH HOH B . XA 10 HOH 224 1024 501 HOH HOH B . XA 10 HOH 225 1025 502 HOH HOH B . XA 10 HOH 226 1026 507 HOH HOH B . XA 10 HOH 227 1027 508 HOH HOH B . XA 10 HOH 228 1028 509 HOH HOH B . XA 10 HOH 229 1029 510 HOH HOH B . XA 10 HOH 230 1030 511 HOH HOH B . XA 10 HOH 231 1031 514 HOH HOH B . XA 10 HOH 232 1032 517 HOH HOH B . XA 10 HOH 233 1033 519 HOH HOH B . XA 10 HOH 234 1034 521 HOH HOH B . XA 10 HOH 235 1035 523 HOH HOH B . XA 10 HOH 236 1036 524 HOH HOH B . XA 10 HOH 237 1037 526 HOH HOH B . XA 10 HOH 238 1038 529 HOH HOH B . XA 10 HOH 239 1039 530 HOH HOH B . XA 10 HOH 240 1040 531 HOH HOH B . XA 10 HOH 241 1041 535 HOH HOH B . XA 10 HOH 242 1042 537 HOH HOH B . XA 10 HOH 243 1043 539 HOH HOH B . XA 10 HOH 244 1044 543 HOH HOH B . XA 10 HOH 245 1045 546 HOH HOH B . XA 10 HOH 246 1046 547 HOH HOH B . XA 10 HOH 247 1047 549 HOH HOH B . XA 10 HOH 248 1048 551 HOH HOH B . XA 10 HOH 249 1049 553 HOH HOH B . XA 10 HOH 250 1050 555 HOH HOH B . XA 10 HOH 251 1051 556 HOH HOH B . XA 10 HOH 252 1052 558 HOH HOH B . XA 10 HOH 253 1053 559 HOH HOH B . XA 10 HOH 254 1054 560 HOH HOH B . XA 10 HOH 255 1055 564 HOH HOH B . XA 10 HOH 256 1056 568 HOH HOH B . XA 10 HOH 257 1057 571 HOH HOH B . XA 10 HOH 258 1058 572 HOH HOH B . XA 10 HOH 259 1059 574 HOH HOH B . XA 10 HOH 260 1060 576 HOH HOH B . XA 10 HOH 261 1061 578 HOH HOH B . XA 10 HOH 262 1062 581 HOH HOH B . XA 10 HOH 263 1063 582 HOH HOH B . XA 10 HOH 264 1064 583 HOH HOH B . XA 10 HOH 265 1065 585 HOH HOH B . XA 10 HOH 266 1066 586 HOH HOH B . XA 10 HOH 267 1067 589 HOH HOH B . XA 10 HOH 268 1068 590 HOH HOH B . XA 10 HOH 269 1069 592 HOH HOH B . XA 10 HOH 270 1070 598 HOH HOH B . XA 10 HOH 271 1071 599 HOH HOH B . XA 10 HOH 272 1072 600 HOH HOH B . XA 10 HOH 273 1073 605 HOH HOH B . XA 10 HOH 274 1074 609 HOH HOH B . XA 10 HOH 275 1075 610 HOH HOH B . XA 10 HOH 276 1076 612 HOH HOH B . XA 10 HOH 277 1077 613 HOH HOH B . XA 10 HOH 278 1078 614 HOH HOH B . XA 10 HOH 279 1079 615 HOH HOH B . XA 10 HOH 280 1080 616 HOH HOH B . XA 10 HOH 281 1081 619 HOH HOH B . XA 10 HOH 282 1082 622 HOH HOH B . XA 10 HOH 283 1083 626 HOH HOH B . XA 10 HOH 284 1084 627 HOH HOH B . XA 10 HOH 285 1085 630 HOH HOH B . XA 10 HOH 286 1086 632 HOH HOH B . XA 10 HOH 287 1087 634 HOH HOH B . XA 10 HOH 288 1088 635 HOH HOH B . XA 10 HOH 289 1089 641 HOH HOH B . XA 10 HOH 290 1090 642 HOH HOH B . XA 10 HOH 291 1091 644 HOH HOH B . XA 10 HOH 292 1092 645 HOH HOH B . XA 10 HOH 293 1093 649 HOH HOH B . XA 10 HOH 294 1094 650 HOH HOH B . XA 10 HOH 295 1095 652 HOH HOH B . XA 10 HOH 296 1096 654 HOH HOH B . XA 10 HOH 297 1097 656 HOH HOH B . XA 10 HOH 298 1098 658 HOH HOH B . XA 10 HOH 299 1099 659 HOH HOH B . XA 10 HOH 300 1100 660 HOH HOH B . XA 10 HOH 301 1101 661 HOH HOH B . XA 10 HOH 302 1102 665 HOH HOH B . XA 10 HOH 303 1103 666 HOH HOH B . XA 10 HOH 304 1104 668 HOH HOH B . XA 10 HOH 305 1105 674 HOH HOH B . XA 10 HOH 306 1106 675 HOH HOH B . XA 10 HOH 307 1107 677 HOH HOH B . XA 10 HOH 308 1108 680 HOH HOH B . XA 10 HOH 309 1109 682 HOH HOH B . XA 10 HOH 310 1110 685 HOH HOH B . XA 10 HOH 311 1111 690 HOH HOH B . XA 10 HOH 312 1112 691 HOH HOH B . XA 10 HOH 313 1113 692 HOH HOH B . XA 10 HOH 314 1114 693 HOH HOH B . XA 10 HOH 315 1115 694 HOH HOH B . XA 10 HOH 316 1116 695 HOH HOH B . XA 10 HOH 317 1117 697 HOH HOH B . XA 10 HOH 318 1118 701 HOH HOH B . XA 10 HOH 319 1119 703 HOH HOH B . XA 10 HOH 320 1120 706 HOH HOH B . XA 10 HOH 321 1121 707 HOH HOH B . XA 10 HOH 322 1122 708 HOH HOH B . XA 10 HOH 323 1123 710 HOH HOH B . XA 10 HOH 324 1124 711 HOH HOH B . XA 10 HOH 325 1125 712 HOH HOH B . XA 10 HOH 326 1126 713 HOH HOH B . XA 10 HOH 327 1127 714 HOH HOH B . XA 10 HOH 328 1128 715 HOH HOH B . XA 10 HOH 329 1129 716 HOH HOH B . XA 10 HOH 330 1130 720 HOH HOH B . XA 10 HOH 331 1131 721 HOH HOH B . XA 10 HOH 332 1132 724 HOH HOH B . XA 10 HOH 333 1133 727 HOH HOH B . XA 10 HOH 334 1134 729 HOH HOH B . XA 10 HOH 335 1135 730 HOH HOH B . XA 10 HOH 336 1136 732 HOH HOH B . XA 10 HOH 337 1137 735 HOH HOH B . XA 10 HOH 338 1138 736 HOH HOH B . XA 10 HOH 339 1139 738 HOH HOH B . XA 10 HOH 340 1140 739 HOH HOH B . XA 10 HOH 341 1141 742 HOH HOH B . XA 10 HOH 342 1142 743 HOH HOH B . XA 10 HOH 343 1143 744 HOH HOH B . XA 10 HOH 344 1144 749 HOH HOH B . XA 10 HOH 345 1145 751 HOH HOH B . XA 10 HOH 346 1146 752 HOH HOH B . XA 10 HOH 347 1147 754 HOH HOH B . XA 10 HOH 348 1148 755 HOH HOH B . XA 10 HOH 349 1149 759 HOH HOH B . XA 10 HOH 350 1150 760 HOH HOH B . XA 10 HOH 351 1151 761 HOH HOH B . XA 10 HOH 352 1152 762 HOH HOH B . XA 10 HOH 353 1153 764 HOH HOH B . XA 10 HOH 354 1154 765 HOH HOH B . XA 10 HOH 355 1155 766 HOH HOH B . XA 10 HOH 356 1156 769 HOH HOH B . XA 10 HOH 357 1157 770 HOH HOH B . XA 10 HOH 358 1158 772 HOH HOH B . XA 10 HOH 359 1159 774 HOH HOH B . XA 10 HOH 360 1160 775 HOH HOH B . XA 10 HOH 361 1161 776 HOH HOH B . XA 10 HOH 362 1162 778 HOH HOH B . XA 10 HOH 363 1163 780 HOH HOH B . XA 10 HOH 364 1164 782 HOH HOH B . XA 10 HOH 365 1165 783 HOH HOH B . XA 10 HOH 366 1166 785 HOH HOH B . XA 10 HOH 367 1167 786 HOH HOH B . XA 10 HOH 368 1168 788 HOH HOH B . XA 10 HOH 369 1169 790 HOH HOH B . XA 10 HOH 370 1170 793 HOH HOH B . XA 10 HOH 371 1171 794 HOH HOH B . XA 10 HOH 372 1172 796 HOH HOH B . XA 10 HOH 373 1173 797 HOH HOH B . XA 10 HOH 374 1174 798 HOH HOH B . XA 10 HOH 375 1175 799 HOH HOH B . XA 10 HOH 376 1176 800 HOH HOH B . XA 10 HOH 377 1177 801 HOH HOH B . XA 10 HOH 378 1178 805 HOH HOH B . XA 10 HOH 379 1179 807 HOH HOH B . XA 10 HOH 380 1180 808 HOH HOH B . XA 10 HOH 381 1181 809 HOH HOH B . XA 10 HOH 382 1182 810 HOH HOH B . XA 10 HOH 383 1183 812 HOH HOH B . XA 10 HOH 384 1184 816 HOH HOH B . XA 10 HOH 385 1185 818 HOH HOH B . XA 10 HOH 386 1186 820 HOH HOH B . XA 10 HOH 387 1187 821 HOH HOH B . XA 10 HOH 388 1188 823 HOH HOH B . XA 10 HOH 389 1189 824 HOH HOH B . XA 10 HOH 390 1190 826 HOH HOH B . XA 10 HOH 391 1191 827 HOH HOH B . XA 10 HOH 392 1192 828 HOH HOH B . XA 10 HOH 393 1193 831 HOH HOH B . XA 10 HOH 394 1194 833 HOH HOH B . XA 10 HOH 395 1195 834 HOH HOH B . XA 10 HOH 396 1196 837 HOH HOH B . XA 10 HOH 397 1197 838 HOH HOH B . XA 10 HOH 398 1198 839 HOH HOH B . XA 10 HOH 399 1199 840 HOH HOH B . XA 10 HOH 400 1200 841 HOH HOH B . XA 10 HOH 401 1201 843 HOH HOH B . XA 10 HOH 402 1202 845 HOH HOH B . XA 10 HOH 403 1203 846 HOH HOH B . XA 10 HOH 404 1204 848 HOH HOH B . XA 10 HOH 405 1205 850 HOH HOH B . XA 10 HOH 406 1206 854 HOH HOH B . XA 10 HOH 407 1207 856 HOH HOH B . XA 10 HOH 408 1208 857 HOH HOH B . XA 10 HOH 409 1209 858 HOH HOH B . XA 10 HOH 410 1210 859 HOH HOH B . XA 10 HOH 411 1211 860 HOH HOH B . XA 10 HOH 412 1212 862 HOH HOH B . XA 10 HOH 413 1213 863 HOH HOH B . XA 10 HOH 414 1214 865 HOH HOH B . XA 10 HOH 415 1215 867 HOH HOH B . XA 10 HOH 416 1216 870 HOH HOH B . XA 10 HOH 417 1217 878 HOH HOH B . XA 10 HOH 418 1218 879 HOH HOH B . XA 10 HOH 419 1219 881 HOH HOH B . XA 10 HOH 420 1220 883 HOH HOH B . XA 10 HOH 421 1221 884 HOH HOH B . XA 10 HOH 422 1222 885 HOH HOH B . XA 10 HOH 423 1223 887 HOH HOH B . XA 10 HOH 424 1224 889 HOH HOH B . XA 10 HOH 425 1225 893 HOH HOH B . XA 10 HOH 426 1226 894 HOH HOH B . XA 10 HOH 427 1227 895 HOH HOH B . XA 10 HOH 428 1228 902 HOH HOH B . XA 10 HOH 429 1229 905 HOH HOH B . XA 10 HOH 430 1230 906 HOH HOH B . XA 10 HOH 431 1231 908 HOH HOH B . XA 10 HOH 432 1232 911 HOH HOH B . XA 10 HOH 433 1233 914 HOH HOH B . XA 10 HOH 434 1234 917 HOH HOH B . XA 10 HOH 435 1235 919 HOH HOH B . XA 10 HOH 436 1236 924 HOH HOH B . XA 10 HOH 437 1237 925 HOH HOH B . XA 10 HOH 438 1238 926 HOH HOH B . XA 10 HOH 439 1239 927 HOH HOH B . XA 10 HOH 440 1240 930 HOH HOH B . XA 10 HOH 441 1241 934 HOH HOH B . XA 10 HOH 442 1242 935 HOH HOH B . XA 10 HOH 443 1243 936 HOH HOH B . XA 10 HOH 444 1244 939 HOH HOH B . XA 10 HOH 445 1245 940 HOH HOH B . XA 10 HOH 446 1246 945 HOH HOH B . XA 10 HOH 447 1247 946 HOH HOH B . XA 10 HOH 448 1248 947 HOH HOH B . XA 10 HOH 449 1249 949 HOH HOH B . XA 10 HOH 450 1250 950 HOH HOH B . XA 10 HOH 451 1251 951 HOH HOH B . XA 10 HOH 452 1252 952 HOH HOH B . XA 10 HOH 453 1253 954 HOH HOH B . XA 10 HOH 454 1254 955 HOH HOH B . XA 10 HOH 455 1255 960 HOH HOH B . XA 10 HOH 456 1256 962 HOH HOH B . XA 10 HOH 457 1257 965 HOH HOH B . XA 10 HOH 458 1258 966 HOH HOH B . XA 10 HOH 459 1259 968 HOH HOH B . XA 10 HOH 460 1260 969 HOH HOH B . XA 10 HOH 461 1261 972 HOH HOH B . XA 10 HOH 462 1262 976 HOH HOH B . XA 10 HOH 463 1263 977 HOH HOH B . XA 10 HOH 464 1264 980 HOH HOH B . XA 10 HOH 465 1265 981 HOH HOH B . XA 10 HOH 466 1266 983 HOH HOH B . XA 10 HOH 467 1267 984 HOH HOH B . XA 10 HOH 468 1268 985 HOH HOH B . XA 10 HOH 469 1269 988 HOH HOH B . XA 10 HOH 470 1270 992 HOH HOH B . XA 10 HOH 471 1271 993 HOH HOH B . XA 10 HOH 472 1272 997 HOH HOH B . XA 10 HOH 473 1273 1000 HOH HOH B . XA 10 HOH 474 1274 1006 HOH HOH B . XA 10 HOH 475 1275 1007 HOH HOH B . XA 10 HOH 476 1276 1008 HOH HOH B . XA 10 HOH 477 1277 1009 HOH HOH B . XA 10 HOH 478 1278 1011 HOH HOH B . XA 10 HOH 479 1279 1012 HOH HOH B . XA 10 HOH 480 1280 1014 HOH HOH B . XA 10 HOH 481 1281 1022 HOH HOH B . XA 10 HOH 482 1282 1023 HOH HOH B . XA 10 HOH 483 1283 1024 HOH HOH B . XA 10 HOH 484 1284 1025 HOH HOH B . XA 10 HOH 485 1285 1026 HOH HOH B . XA 10 HOH 486 1286 1028 HOH HOH B . XA 10 HOH 487 1287 1032 HOH HOH B . XA 10 HOH 488 1288 1035 HOH HOH B . XA 10 HOH 489 1289 1037 HOH HOH B . XA 10 HOH 490 1290 1038 HOH HOH B . XA 10 HOH 491 1291 1039 HOH HOH B . XA 10 HOH 492 1292 1040 HOH HOH B . XA 10 HOH 493 1293 1041 HOH HOH B . XA 10 HOH 494 1294 1042 HOH HOH B . XA 10 HOH 495 1295 1045 HOH HOH B . XA 10 HOH 496 1296 1047 HOH HOH B . XA 10 HOH 497 1297 1051 HOH HOH B . XA 10 HOH 498 1298 1052 HOH HOH B . XA 10 HOH 499 1299 1054 HOH HOH B . XA 10 HOH 500 1300 1057 HOH HOH B . XA 10 HOH 501 1301 1060 HOH HOH B . XA 10 HOH 502 1302 1061 HOH HOH B . XA 10 HOH 503 1303 1062 HOH HOH B . XA 10 HOH 504 1304 1063 HOH HOH B . XA 10 HOH 505 1305 1064 HOH HOH B . XA 10 HOH 506 1306 1067 HOH HOH B . XA 10 HOH 507 1307 1070 HOH HOH B . XA 10 HOH 508 1308 1071 HOH HOH B . XA 10 HOH 509 1309 1073 HOH HOH B . XA 10 HOH 510 1310 1075 HOH HOH B . XA 10 HOH 511 1311 1076 HOH HOH B . XA 10 HOH 512 1312 1078 HOH HOH B . XA 10 HOH 513 1313 1081 HOH HOH B . XA 10 HOH 514 1314 1083 HOH HOH B . XA 10 HOH 515 1315 1084 HOH HOH B . XA 10 HOH 516 1316 1091 HOH HOH B . XA 10 HOH 517 1317 1095 HOH HOH B . XA 10 HOH 518 1318 1097 HOH HOH B . XA 10 HOH 519 1319 1098 HOH HOH B . XA 10 HOH 520 1320 1099 HOH HOH B . XA 10 HOH 521 1321 1102 HOH HOH B . XA 10 HOH 522 1322 1103 HOH HOH B . XA 10 HOH 523 1323 1106 HOH HOH B . XA 10 HOH 524 1324 1107 HOH HOH B . XA 10 HOH 525 1325 1108 HOH HOH B . XA 10 HOH 526 1326 1110 HOH HOH B . XA 10 HOH 527 1327 1112 HOH HOH B . XA 10 HOH 528 1328 1114 HOH HOH B . XA 10 HOH 529 1329 1116 HOH HOH B . XA 10 HOH 530 1330 1119 HOH HOH B . XA 10 HOH 531 1331 1122 HOH HOH B . XA 10 HOH 532 1332 1124 HOH HOH B . XA 10 HOH 533 1333 1125 HOH HOH B . XA 10 HOH 534 1334 1126 HOH HOH B . XA 10 HOH 535 1335 1127 HOH HOH B . XA 10 HOH 536 1336 1128 HOH HOH B . XA 10 HOH 537 1337 1130 HOH HOH B . XA 10 HOH 538 1338 1131 HOH HOH B . XA 10 HOH 539 1339 1133 HOH HOH B . XA 10 HOH 540 1340 1136 HOH HOH B . XA 10 HOH 541 1341 1140 HOH HOH B . XA 10 HOH 542 1342 1143 HOH HOH B . XA 10 HOH 543 1343 1144 HOH HOH B . XA 10 HOH 544 1344 1146 HOH HOH B . XA 10 HOH 545 1345 1147 HOH HOH B . XA 10 HOH 546 1346 1148 HOH HOH B . XA 10 HOH 547 1347 1150 HOH HOH B . XA 10 HOH 548 1348 1152 HOH HOH B . XA 10 HOH 549 1349 1155 HOH HOH B . XA 10 HOH 550 1350 1156 HOH HOH B . XA 10 HOH 551 1351 1158 HOH HOH B . XA 10 HOH 552 1352 1161 HOH HOH B . XA 10 HOH 553 1353 1162 HOH HOH B . XA 10 HOH 554 1354 1163 HOH HOH B . XA 10 HOH 555 1355 1167 HOH HOH B . XA 10 HOH 556 1356 1168 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 201 A ASN 201 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 396 A ASN 396 ? ASN 'GLYCOSYLATION SITE' 4 B ASN 39 B ASN 39 ? ASN 'GLYCOSYLATION SITE' 5 B ASN 201 B ASN 201 ? ASN 'GLYCOSYLATION SITE' 6 B ASN 396 B ASN 396 ? ASN 'GLYCOSYLATION SITE' 7 A ASN 88 A ASN 88 ? ASN 'GLYCOSYLATION SITE' 8 A ASN 216 A ASN 216 ? ASN 'GLYCOSYLATION SITE' 9 A ASN 244 A ASN 244 ? ASN 'GLYCOSYLATION SITE' 10 A ASN 289 A ASN 289 ? ASN 'GLYCOSYLATION SITE' 11 A ASN 376 A ASN 376 ? ASN 'GLYCOSYLATION SITE' 12 B ASN 88 B ASN 88 ? ASN 'GLYCOSYLATION SITE' 13 B ASN 216 B ASN 216 ? ASN 'GLYCOSYLATION SITE' 14 B ASN 289 B ASN 289 ? ASN 'GLYCOSYLATION SITE' 15 B ASN 376 B ASN 376 ? 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_defined_assembly ? monomeric 1 2 author_defined_assembly ? monomeric 1 # loop_ _pdbx_struct_assembly_gen.assembly_id _pdbx_struct_assembly_gen.oper_expression _pdbx_struct_assembly_gen.asym_id_list 1 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,Z,AA,WA 2 1 B,BA,CA,DA,EA,FA,GA,HA,IA,JA,KA,LA,MA,NA,OA,PA,QA,RA,SA,TA,UA,VA,XA # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_struct_conn_angle.id _pdbx_struct_conn_angle.ptnr1_label_atom_id _pdbx_struct_conn_angle.ptnr1_label_alt_id _pdbx_struct_conn_angle.ptnr1_label_asym_id _pdbx_struct_conn_angle.ptnr1_label_comp_id _pdbx_struct_conn_angle.ptnr1_label_seq_id _pdbx_struct_conn_angle.ptnr1_auth_atom_id _pdbx_struct_conn_angle.ptnr1_auth_asym_id _pdbx_struct_conn_angle.ptnr1_auth_comp_id _pdbx_struct_conn_angle.ptnr1_auth_seq_id _pdbx_struct_conn_angle.ptnr1_PDB_ins_code _pdbx_struct_conn_angle.ptnr1_symmetry _pdbx_struct_conn_angle.ptnr2_label_atom_id _pdbx_struct_conn_angle.ptnr2_label_alt_id _pdbx_struct_conn_angle.ptnr2_label_asym_id _pdbx_struct_conn_angle.ptnr2_label_comp_id _pdbx_struct_conn_angle.ptnr2_label_seq_id _pdbx_struct_conn_angle.ptnr2_auth_atom_id _pdbx_struct_conn_angle.ptnr2_auth_asym_id _pdbx_struct_conn_angle.ptnr2_auth_comp_id _pdbx_struct_conn_angle.ptnr2_auth_seq_id _pdbx_struct_conn_angle.ptnr2_PDB_ins_code _pdbx_struct_conn_angle.ptnr2_symmetry _pdbx_struct_conn_angle.ptnr3_label_atom_id _pdbx_struct_conn_angle.ptnr3_label_alt_id _pdbx_struct_conn_angle.ptnr3_label_asym_id _pdbx_struct_conn_angle.ptnr3_label_comp_id _pdbx_struct_conn_angle.ptnr3_label_seq_id _pdbx_struct_conn_angle.ptnr3_auth_atom_id _pdbx_struct_conn_angle.ptnr3_auth_asym_id _pdbx_struct_conn_angle.ptnr3_auth_comp_id _pdbx_struct_conn_angle.ptnr3_auth_seq_id _pdbx_struct_conn_angle.ptnr3_PDB_ins_code _pdbx_struct_conn_angle.ptnr3_symmetry _pdbx_struct_conn_angle.value _pdbx_struct_conn_angle.value_esd 1 SG ? A CYS 503 ? A CYS 503 ? 1_555 CU ? T CU . ? A CU 601 ? 1_555 ND1 ? A HIS 431 ? A HIS 431 ? 1_555 124.7 ? 2 SG ? A CYS 503 ? A CYS 503 ? 1_555 CU ? T CU . ? A CU 601 ? 1_555 ND1 ? A HIS 508 ? A HIS 508 ? 1_555 128.9 ? 3 ND1 ? A HIS 431 ? A HIS 431 ? 1_555 CU ? T CU . ? A CU 601 ? 1_555 ND1 ? A HIS 508 ? A HIS 508 ? 1_555 106.1 ? 4 NE2 ? A HIS 436 ? A HIS 436 ? 1_555 CU ? U CU . ? A CU 602 ? 1_555 NE2 ? A HIS 502 ? A HIS 502 ? 1_555 105.8 ? 5 NE2 ? A HIS 436 ? A HIS 436 ? 1_555 CU ? U CU . ? A CU 602 ? 1_555 NE2 ? A HIS 140 ? A HIS 140 ? 1_555 113.5 ? 6 NE2 ? A HIS 502 ? A HIS 502 ? 1_555 CU ? U CU . ? A CU 602 ? 1_555 NE2 ? A HIS 140 ? A HIS 140 ? 1_555 118.1 ? 7 NE2 ? A HIS 436 ? A HIS 436 ? 1_555 CU ? U CU . ? A CU 602 ? 1_555 O1 ? AA OXY . ? A OXY 620 ? 1_555 130.8 ? 8 NE2 ? A HIS 502 ? A HIS 502 ? 1_555 CU ? U CU . ? A CU 602 ? 1_555 O1 ? AA OXY . ? A OXY 620 ? 1_555 96.1 ? 9 NE2 ? A HIS 140 ? A HIS 140 ? 1_555 CU ? U CU . ? A CU 602 ? 1_555 O1 ? AA OXY . ? A OXY 620 ? 1_555 92.6 ? 10 NE2 ? A HIS 436 ? A HIS 436 ? 1_555 CU ? U CU . ? A CU 602 ? 1_555 O2 ? AA OXY . ? A OXY 620 ? 1_555 99.6 ? 11 NE2 ? A HIS 502 ? A HIS 502 ? 1_555 CU ? U CU . ? A CU 602 ? 1_555 O2 ? AA OXY . ? A OXY 620 ? 1_555 104.8 ? 12 NE2 ? A HIS 140 ? A HIS 140 ? 1_555 CU ? U CU . ? A CU 602 ? 1_555 O2 ? AA OXY . ? A OXY 620 ? 1_555 113.2 ? 13 O1 ? AA OXY . ? A OXY 620 ? 1_555 CU ? U CU . ? A CU 602 ? 1_555 O2 ? AA OXY . ? A OXY 620 ? 1_555 31.4 ? 14 ND1 ? A HIS 95 ? A HIS 95 ? 1_555 CU ? V CU . ? A CU 603 ? 1_555 NE2 ? A HIS 138 ? A HIS 138 ? 1_555 140.2 ? 15 ND1 ? A HIS 95 ? A HIS 95 ? 1_555 CU ? V CU . ? A CU 603 ? 1_555 NE2 ? A HIS 504 ? A HIS 504 ? 1_555 107.7 ? 16 NE2 ? A HIS 138 ? A HIS 138 ? 1_555 CU ? V CU . ? A CU 603 ? 1_555 NE2 ? A HIS 504 ? A HIS 504 ? 1_555 108.2 ? 17 ND1 ? A HIS 95 ? A HIS 95 ? 1_555 CU ? V CU . ? A CU 603 ? 1_555 O1 ? AA OXY . ? A OXY 620 ? 1_555 128.9 ? 18 NE2 ? A HIS 138 ? A HIS 138 ? 1_555 CU ? V CU . ? A CU 603 ? 1_555 O1 ? AA OXY . ? A OXY 620 ? 1_555 79.3 ? 19 NE2 ? A HIS 504 ? A HIS 504 ? 1_555 CU ? V CU . ? A CU 603 ? 1_555 O1 ? AA OXY . ? A OXY 620 ? 1_555 71.6 ? 20 ND1 ? A HIS 95 ? A HIS 95 ? 1_555 CU ? V CU . ? A CU 603 ? 1_555 O2 ? AA OXY . ? A OXY 620 ? 1_555 102.5 ? 21 NE2 ? A HIS 138 ? A HIS 138 ? 1_555 CU ? V CU . ? A CU 603 ? 1_555 O2 ? AA OXY . ? A OXY 620 ? 1_555 94.2 ? 22 NE2 ? A HIS 504 ? A HIS 504 ? 1_555 CU ? V CU . ? A CU 603 ? 1_555 O2 ? AA OXY . ? A OXY 620 ? 1_555 90.1 ? 23 O1 ? AA OXY . ? A OXY 620 ? 1_555 CU ? V CU . ? A CU 603 ? 1_555 O2 ? AA OXY . ? A OXY 620 ? 1_555 29.1 ? 24 NE2 ? A HIS 434 ? A HIS 434 ? 1_555 CU ? W CU . ? A CU 604 ? 1_555 NE2 ? A HIS 93 ? A HIS 93 ? 1_555 175.7 ? 25 NE2 ? A HIS 434 ? A HIS 434 ? 1_555 CU ? W CU . ? A CU 604 ? 1_555 CL ? X CL . ? A CL 610 ? 1_555 88.7 ? 26 NE2 ? A HIS 93 ? A HIS 93 ? 1_555 CU ? W CU . ? A CU 604 ? 1_555 CL ? X CL . ? A CL 610 ? 1_555 89.2 ? 27 NE2 ? A HIS 434 ? A HIS 434 ? 1_555 CU ? W CU . ? A CU 604 ? 1_555 O2 ? AA OXY . ? A OXY 620 ? 1_555 90.0 ? 28 NE2 ? A HIS 93 ? A HIS 93 ? 1_555 CU ? W CU . ? A CU 604 ? 1_555 O2 ? AA OXY . ? A OXY 620 ? 1_555 92.5 ? 29 CL ? X CL . ? A CL 610 ? 1_555 CU ? W CU . ? A CU 604 ? 1_555 O2 ? AA OXY . ? A OXY 620 ? 1_555 173.4 ? 30 ND1 ? B HIS 508 ? B HIS 508 ? 1_555 CU ? PA CU . ? B CU 601 ? 1_555 ND1 ? B HIS 431 ? B HIS 431 ? 1_555 107.0 ? 31 ND1 ? B HIS 508 ? B HIS 508 ? 1_555 CU ? PA CU . ? B CU 601 ? 1_555 SG ? B CYS 503 ? B CYS 503 ? 1_555 124.3 ? 32 ND1 ? B HIS 431 ? B HIS 431 ? 1_555 CU ? PA CU . ? B CU 601 ? 1_555 SG ? B CYS 503 ? B CYS 503 ? 1_555 128.1 ? 33 NE2 ? B HIS 502 ? B HIS 502 ? 1_555 CU ? QA CU . ? B CU 602 ? 1_555 O2 ? VA OXY . ? B OXY 620 ? 1_555 98.8 ? 34 NE2 ? B HIS 502 ? B HIS 502 ? 1_555 CU ? QA CU . ? B CU 602 ? 1_555 O1 ? VA OXY . ? B OXY 620 ? 1_555 89.4 ? 35 O2 ? VA OXY . ? B OXY 620 ? 1_555 CU ? QA CU . ? B CU 602 ? 1_555 O1 ? VA OXY . ? B OXY 620 ? 1_555 30.6 ? 36 NE2 ? B HIS 502 ? B HIS 502 ? 1_555 CU ? QA CU . ? B CU 602 ? 1_555 NE2 ? B HIS 436 ? B HIS 436 ? 1_555 111.2 ? 37 O2 ? VA OXY . ? B OXY 620 ? 1_555 CU ? QA CU . ? B CU 602 ? 1_555 NE2 ? B HIS 436 ? B HIS 436 ? 1_555 97.0 ? 38 O1 ? VA OXY . ? B OXY 620 ? 1_555 CU ? QA CU . ? B CU 602 ? 1_555 NE2 ? B HIS 436 ? B HIS 436 ? 1_555 127.4 ? 39 NE2 ? B HIS 502 ? B HIS 502 ? 1_555 CU ? QA CU . ? B CU 602 ? 1_555 NE2 ? B HIS 140 ? B HIS 140 ? 1_555 118.2 ? 40 O2 ? VA OXY . ? B OXY 620 ? 1_555 CU ? QA CU . ? B CU 602 ? 1_555 NE2 ? B HIS 140 ? B HIS 140 ? 1_555 111.5 ? 41 O1 ? VA OXY . ? B OXY 620 ? 1_555 CU ? QA CU . ? B CU 602 ? 1_555 NE2 ? B HIS 140 ? B HIS 140 ? 1_555 91.2 ? 42 NE2 ? B HIS 436 ? B HIS 436 ? 1_555 CU ? QA CU . ? B CU 602 ? 1_555 NE2 ? B HIS 140 ? B HIS 140 ? 1_555 116.4 ? 43 ND1 ? B HIS 95 ? B HIS 95 ? 1_555 CU ? RA CU . ? B CU 603 ? 1_555 O1 ? VA OXY . ? B OXY 620 ? 1_555 130.8 ? 44 ND1 ? B HIS 95 ? B HIS 95 ? 1_555 CU ? RA CU . ? B CU 603 ? 1_555 O2 ? VA OXY . ? B OXY 620 ? 1_555 105.0 ? 45 O1 ? VA OXY . ? B OXY 620 ? 1_555 CU ? RA CU . ? B CU 603 ? 1_555 O2 ? VA OXY . ? B OXY 620 ? 1_555 28.7 ? 46 ND1 ? B HIS 95 ? B HIS 95 ? 1_555 CU ? RA CU . ? B CU 603 ? 1_555 NE2 ? B HIS 138 ? B HIS 138 ? 1_555 137.9 ? 47 O1 ? VA OXY . ? B OXY 620 ? 1_555 CU ? RA CU . ? B CU 603 ? 1_555 NE2 ? B HIS 138 ? B HIS 138 ? 1_555 81.5 ? 48 O2 ? VA OXY . ? B OXY 620 ? 1_555 CU ? RA CU . ? B CU 603 ? 1_555 NE2 ? B HIS 138 ? B HIS 138 ? 1_555 95.7 ? 49 ND1 ? B HIS 95 ? B HIS 95 ? 1_555 CU ? RA CU . ? B CU 603 ? 1_555 NE2 ? B HIS 504 ? B HIS 504 ? 1_555 106.8 ? 50 O1 ? VA OXY . ? B OXY 620 ? 1_555 CU ? RA CU . ? B CU 603 ? 1_555 NE2 ? B HIS 504 ? B HIS 504 ? 1_555 71.9 ? 51 O2 ? VA OXY . ? B OXY 620 ? 1_555 CU ? RA CU . ? B CU 603 ? 1_555 NE2 ? B HIS 504 ? B HIS 504 ? 1_555 90.3 ? 52 NE2 ? B HIS 138 ? B HIS 138 ? 1_555 CU ? RA CU . ? B CU 603 ? 1_555 NE2 ? B HIS 504 ? B HIS 504 ? 1_555 109.3 ? 53 O2 ? VA OXY . ? B OXY 620 ? 1_555 CU ? SA CU . ? B CU 604 ? 1_555 NE2 ? B HIS 93 ? B HIS 93 ? 1_555 92.1 ? 54 O2 ? VA OXY . ? B OXY 620 ? 1_555 CU ? SA CU . ? B CU 604 ? 1_555 CL ? TA CL . ? B CL 610 ? 1_555 173.1 ? 55 NE2 ? B HIS 93 ? B HIS 93 ? 1_555 CU ? SA CU . ? B CU 604 ? 1_555 CL ? TA CL . ? B CL 610 ? 1_555 91.1 ? 56 O2 ? VA OXY . ? B OXY 620 ? 1_555 CU ? SA CU . ? B CU 604 ? 1_555 NE2 ? B HIS 434 ? B HIS 434 ? 1_555 87.8 ? 57 NE2 ? B HIS 93 ? B HIS 93 ? 1_555 CU ? SA CU . ? B CU 604 ? 1_555 NE2 ? B HIS 434 ? B HIS 434 ? 1_555 175.6 ? 58 CL ? TA CL . ? B CL 610 ? 1_555 CU ? SA CU . ? B CU 604 ? 1_555 NE2 ? B HIS 434 ? B HIS 434 ? 1_555 89.5 ? # 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 2006-11-14 2 'Structure model' 1 1 2008-05-01 3 'Structure model' 1 2 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' 'Version format compliance' 2 3 'Structure model' 'Non-polymer description' 3 3 '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 CNS 1.1 ? package 'Axel T. Brunger' axel.brunger@yale.edu refinement http://cns.csb.yale.edu/v1.1/ Fortran_77 ? 1 PDB_EXTRACT 2.000 'April. 3, 2006' package PDB sw-help@rcsb.rutgers.edu 'data extraction' http://pdb.rutgers.edu/software/ C++ ? 2 XDS . ? ? ? ? 'data reduction' ? ? ? 3 XSCALE . ? ? ? ? 'data scaling' ? ? ? 4 MOLREP . ? ? ? ? phasing ? ? ? 5 # 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 CYS A 4 ? ? -141.00 14.92 2 1 TRP A 13 ? ? -129.07 -67.35 3 1 SER A 91 ? ? -160.82 118.20 4 1 LYS A 100 ? ? -58.87 105.20 5 1 VAL A 111 ? ? -125.12 -67.92 6 1 SER A 142 ? ? 55.64 -131.78 7 1 GLU A 235 ? ? -144.87 -46.39 8 1 ASP A 253 ? ? 58.97 -123.20 9 1 ASP A 422 ? ? 36.77 58.32 10 1 ASP A 556 ? ? -134.69 -157.62 11 1 TRP B 13 ? ? -132.35 -65.61 12 1 LYS B 100 ? ? -58.10 106.70 13 1 VAL B 111 ? ? -124.73 -67.36 14 1 SER B 142 ? ? 56.49 -130.21 15 1 GLU B 235 ? ? -144.29 -48.90 16 1 ASP B 253 ? ? 62.69 -122.34 17 1 PRO B 283 ? ? -55.19 106.04 18 1 ASP B 422 ? ? 36.12 59.31 # 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 ? ? 0.075 'SIDE CHAIN' 2 1 TYR B 546 ? ? 0.068 'SIDE CHAIN' # 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 '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' NDG 6 'COPPER (II) ION' CU 7 'CHLORIDE ION' CL 8 'SULFATE ION' SO4 9 'OXYGEN MOLECULE' OXY 10 water HOH #