data_1ST8 # _entry.id 1ST8 # _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 1ST8 RCSB RCSB021983 WWPDB D_1000021983 # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 1ST8 _pdbx_database_status.recvd_initial_deposition_date 2004-03-25 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _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 'Verhaest, M.' 1 'Van den Ende, W.' 2 'De Ranter, C.J.' 3 'Van Laere, A.' 4 'Rabijns, A.' 5 # _citation.id primary _citation.title 'X-ray diffraction structure of a plant glycosyl hydrolase family 32 protein: fructan 1-exohydrolase IIa of Cichorium intybus.' _citation.journal_abbrev 'Plant J.' _citation.journal_volume 41 _citation.page_first 400 _citation.page_last 411 _citation.year 2005 _citation.journal_id_ASTM PLJUED _citation.country UK _citation.journal_id_ISSN 0960-7412 _citation.journal_id_CSD 2117 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 15659099 _citation.pdbx_database_id_DOI 10.1111/j.1365-313X.2004.02304.x # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Verhaest, M.' 1 primary 'van den Ende, W.' 2 primary 'Roy, K.L.' 3 primary 'De Ranter, C.J.' 4 primary 'van Laere, A.' 5 primary 'Rabijns, A.' 6 # _cell.entry_id 1ST8 _cell.length_a 139.830 _cell.length_b 139.830 _cell.length_c 181.940 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 8 _cell.pdbx_unique_axis ? # _symmetry.entry_id 1ST8 _symmetry.space_group_name_H-M 'P 41 21 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 92 _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 'fructan 1-exohydrolase IIa' 61115.965 1 3.2.1.80 ? ? ? 2 non-polymer man '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' 221.208 1 ? ? ? ? 3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 3 ? ? ? ? 4 non-polymer man ALPHA-D-MANNOSE 180.156 1 ? ? ? ? 5 non-polymer syn GLYCEROL 92.094 4 ? ? ? ? 6 water nat water 18.015 331 ? ? ? ? # _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 ;QQIEQPYRTGYHFQPPSNWMNDPNGPMLYQGVYHFFYQYNPYAATFGDVIIWGHAVSYDLVNWIHLDPAIYPTQEADSKS CWSGSATILPGNIPAMLYTGSDSKSRQVQDLAWPKNLSDPFLREWVKHPKNPLITPPEGVKDDCFRDPSTAWLGPDGVWR IVVGGDRDNNGMAFLYQSTDFVNWKRYDQPLSSADATGTWECPDFYPVPLNSTNGLDTSVYGGSVRHVMKAGFEGHDWYT IGTYSPDRENFLPQNGLSLTGSTLDLRYDYGQFYASKSFFDDAKNRRVLWAWVPETDSQADDIEKGWAGLQSFPRALWID RNGKQLIQWPVEEIEELRQNQVNLQNKNLKPGSVLEIHGIAASQADVTISFKLEGLKEAEVLDTTLVDPQALCNERGASS RGALGPFGLLAMASKDLKEQSAIFFRVFQNQLGRYSVLMCSDLSRSTVRSNIDTTSYGAFVDIDPRSEEISLRNLIDHSI IESFGAGGKTCITSRIYPKFVNNEEAHLFVFNNGTQNVKISEMSAWSMKNAKFVVDQSVKSAA ; _entity_poly.pdbx_seq_one_letter_code_can ;QQIEQPYRTGYHFQPPSNWMNDPNGPMLYQGVYHFFYQYNPYAATFGDVIIWGHAVSYDLVNWIHLDPAIYPTQEADSKS CWSGSATILPGNIPAMLYTGSDSKSRQVQDLAWPKNLSDPFLREWVKHPKNPLITPPEGVKDDCFRDPSTAWLGPDGVWR IVVGGDRDNNGMAFLYQSTDFVNWKRYDQPLSSADATGTWECPDFYPVPLNSTNGLDTSVYGGSVRHVMKAGFEGHDWYT IGTYSPDRENFLPQNGLSLTGSTLDLRYDYGQFYASKSFFDDAKNRRVLWAWVPETDSQADDIEKGWAGLQSFPRALWID RNGKQLIQWPVEEIEELRQNQVNLQNKNLKPGSVLEIHGIAASQADVTISFKLEGLKEAEVLDTTLVDPQALCNERGASS RGALGPFGLLAMASKDLKEQSAIFFRVFQNQLGRYSVLMCSDLSRSTVRSNIDTTSYGAFVDIDPRSEEISLRNLIDHSI IESFGAGGKTCITSRIYPKFVNNEEAHLFVFNNGTQNVKISEMSAWSMKNAKFVVDQSVKSAA ; _entity_poly.pdbx_strand_id A _entity_poly.pdbx_target_identifier ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 GLN n 1 2 GLN n 1 3 ILE n 1 4 GLU n 1 5 GLN n 1 6 PRO n 1 7 TYR n 1 8 ARG n 1 9 THR n 1 10 GLY n 1 11 TYR n 1 12 HIS n 1 13 PHE n 1 14 GLN n 1 15 PRO n 1 16 PRO n 1 17 SER n 1 18 ASN n 1 19 TRP n 1 20 MET n 1 21 ASN n 1 22 ASP n 1 23 PRO n 1 24 ASN n 1 25 GLY n 1 26 PRO n 1 27 MET n 1 28 LEU n 1 29 TYR n 1 30 GLN n 1 31 GLY n 1 32 VAL n 1 33 TYR n 1 34 HIS n 1 35 PHE n 1 36 PHE n 1 37 TYR n 1 38 GLN n 1 39 TYR n 1 40 ASN n 1 41 PRO n 1 42 TYR n 1 43 ALA n 1 44 ALA n 1 45 THR n 1 46 PHE n 1 47 GLY n 1 48 ASP n 1 49 VAL n 1 50 ILE n 1 51 ILE n 1 52 TRP n 1 53 GLY n 1 54 HIS n 1 55 ALA n 1 56 VAL n 1 57 SER n 1 58 TYR n 1 59 ASP n 1 60 LEU n 1 61 VAL n 1 62 ASN n 1 63 TRP n 1 64 ILE n 1 65 HIS n 1 66 LEU n 1 67 ASP n 1 68 PRO n 1 69 ALA n 1 70 ILE n 1 71 TYR n 1 72 PRO n 1 73 THR n 1 74 GLN n 1 75 GLU n 1 76 ALA n 1 77 ASP n 1 78 SER n 1 79 LYS n 1 80 SER n 1 81 CYS n 1 82 TRP n 1 83 SER n 1 84 GLY n 1 85 SER n 1 86 ALA n 1 87 THR n 1 88 ILE n 1 89 LEU n 1 90 PRO n 1 91 GLY n 1 92 ASN n 1 93 ILE n 1 94 PRO n 1 95 ALA n 1 96 MET n 1 97 LEU n 1 98 TYR n 1 99 THR n 1 100 GLY n 1 101 SER n 1 102 ASP n 1 103 SER n 1 104 LYS n 1 105 SER n 1 106 ARG n 1 107 GLN n 1 108 VAL n 1 109 GLN n 1 110 ASP n 1 111 LEU n 1 112 ALA n 1 113 TRP n 1 114 PRO n 1 115 LYS n 1 116 ASN n 1 117 LEU n 1 118 SER n 1 119 ASP n 1 120 PRO n 1 121 PHE n 1 122 LEU n 1 123 ARG n 1 124 GLU n 1 125 TRP n 1 126 VAL n 1 127 LYS n 1 128 HIS n 1 129 PRO n 1 130 LYS n 1 131 ASN n 1 132 PRO n 1 133 LEU n 1 134 ILE n 1 135 THR n 1 136 PRO n 1 137 PRO n 1 138 GLU n 1 139 GLY n 1 140 VAL n 1 141 LYS n 1 142 ASP n 1 143 ASP n 1 144 CYS n 1 145 PHE n 1 146 ARG n 1 147 ASP n 1 148 PRO n 1 149 SER n 1 150 THR n 1 151 ALA n 1 152 TRP n 1 153 LEU n 1 154 GLY n 1 155 PRO n 1 156 ASP n 1 157 GLY n 1 158 VAL n 1 159 TRP n 1 160 ARG n 1 161 ILE n 1 162 VAL n 1 163 VAL n 1 164 GLY n 1 165 GLY n 1 166 ASP n 1 167 ARG n 1 168 ASP n 1 169 ASN n 1 170 ASN n 1 171 GLY n 1 172 MET n 1 173 ALA n 1 174 PHE n 1 175 LEU n 1 176 TYR n 1 177 GLN n 1 178 SER n 1 179 THR n 1 180 ASP n 1 181 PHE n 1 182 VAL n 1 183 ASN n 1 184 TRP n 1 185 LYS n 1 186 ARG n 1 187 TYR n 1 188 ASP n 1 189 GLN n 1 190 PRO n 1 191 LEU n 1 192 SER n 1 193 SER n 1 194 ALA n 1 195 ASP n 1 196 ALA n 1 197 THR n 1 198 GLY n 1 199 THR n 1 200 TRP n 1 201 GLU n 1 202 CYS n 1 203 PRO n 1 204 ASP n 1 205 PHE n 1 206 TYR n 1 207 PRO n 1 208 VAL n 1 209 PRO n 1 210 LEU n 1 211 ASN n 1 212 SER n 1 213 THR n 1 214 ASN n 1 215 GLY n 1 216 LEU n 1 217 ASP n 1 218 THR n 1 219 SER n 1 220 VAL n 1 221 TYR n 1 222 GLY n 1 223 GLY n 1 224 SER n 1 225 VAL n 1 226 ARG n 1 227 HIS n 1 228 VAL n 1 229 MET n 1 230 LYS n 1 231 ALA n 1 232 GLY n 1 233 PHE n 1 234 GLU n 1 235 GLY n 1 236 HIS n 1 237 ASP n 1 238 TRP n 1 239 TYR n 1 240 THR n 1 241 ILE n 1 242 GLY n 1 243 THR n 1 244 TYR n 1 245 SER n 1 246 PRO n 1 247 ASP n 1 248 ARG n 1 249 GLU n 1 250 ASN n 1 251 PHE n 1 252 LEU n 1 253 PRO n 1 254 GLN n 1 255 ASN n 1 256 GLY n 1 257 LEU n 1 258 SER n 1 259 LEU n 1 260 THR n 1 261 GLY n 1 262 SER n 1 263 THR n 1 264 LEU n 1 265 ASP n 1 266 LEU n 1 267 ARG n 1 268 TYR n 1 269 ASP n 1 270 TYR n 1 271 GLY n 1 272 GLN n 1 273 PHE n 1 274 TYR n 1 275 ALA n 1 276 SER n 1 277 LYS n 1 278 SER n 1 279 PHE n 1 280 PHE n 1 281 ASP n 1 282 ASP n 1 283 ALA n 1 284 LYS n 1 285 ASN n 1 286 ARG n 1 287 ARG n 1 288 VAL n 1 289 LEU n 1 290 TRP n 1 291 ALA n 1 292 TRP n 1 293 VAL n 1 294 PRO n 1 295 GLU n 1 296 THR n 1 297 ASP n 1 298 SER n 1 299 GLN n 1 300 ALA n 1 301 ASP n 1 302 ASP n 1 303 ILE n 1 304 GLU n 1 305 LYS n 1 306 GLY n 1 307 TRP n 1 308 ALA n 1 309 GLY n 1 310 LEU n 1 311 GLN n 1 312 SER n 1 313 PHE n 1 314 PRO n 1 315 ARG n 1 316 ALA n 1 317 LEU n 1 318 TRP n 1 319 ILE n 1 320 ASP n 1 321 ARG n 1 322 ASN n 1 323 GLY n 1 324 LYS n 1 325 GLN n 1 326 LEU n 1 327 ILE n 1 328 GLN n 1 329 TRP n 1 330 PRO n 1 331 VAL n 1 332 GLU n 1 333 GLU n 1 334 ILE n 1 335 GLU n 1 336 GLU n 1 337 LEU n 1 338 ARG n 1 339 GLN n 1 340 ASN n 1 341 GLN n 1 342 VAL n 1 343 ASN n 1 344 LEU n 1 345 GLN n 1 346 ASN n 1 347 LYS n 1 348 ASN n 1 349 LEU n 1 350 LYS n 1 351 PRO n 1 352 GLY n 1 353 SER n 1 354 VAL n 1 355 LEU n 1 356 GLU n 1 357 ILE n 1 358 HIS n 1 359 GLY n 1 360 ILE n 1 361 ALA n 1 362 ALA n 1 363 SER n 1 364 GLN n 1 365 ALA n 1 366 ASP n 1 367 VAL n 1 368 THR n 1 369 ILE n 1 370 SER n 1 371 PHE n 1 372 LYS n 1 373 LEU n 1 374 GLU n 1 375 GLY n 1 376 LEU n 1 377 LYS n 1 378 GLU n 1 379 ALA n 1 380 GLU n 1 381 VAL n 1 382 LEU n 1 383 ASP n 1 384 THR n 1 385 THR n 1 386 LEU n 1 387 VAL n 1 388 ASP n 1 389 PRO n 1 390 GLN n 1 391 ALA n 1 392 LEU n 1 393 CYS n 1 394 ASN n 1 395 GLU n 1 396 ARG n 1 397 GLY n 1 398 ALA n 1 399 SER n 1 400 SER n 1 401 ARG n 1 402 GLY n 1 403 ALA n 1 404 LEU n 1 405 GLY n 1 406 PRO n 1 407 PHE n 1 408 GLY n 1 409 LEU n 1 410 LEU n 1 411 ALA n 1 412 MET n 1 413 ALA n 1 414 SER n 1 415 LYS n 1 416 ASP n 1 417 LEU n 1 418 LYS n 1 419 GLU n 1 420 GLN n 1 421 SER n 1 422 ALA n 1 423 ILE n 1 424 PHE n 1 425 PHE n 1 426 ARG n 1 427 VAL n 1 428 PHE n 1 429 GLN n 1 430 ASN n 1 431 GLN n 1 432 LEU n 1 433 GLY n 1 434 ARG n 1 435 TYR n 1 436 SER n 1 437 VAL n 1 438 LEU n 1 439 MET n 1 440 CYS n 1 441 SER n 1 442 ASP n 1 443 LEU n 1 444 SER n 1 445 ARG n 1 446 SER n 1 447 THR n 1 448 VAL n 1 449 ARG n 1 450 SER n 1 451 ASN n 1 452 ILE n 1 453 ASP n 1 454 THR n 1 455 THR n 1 456 SER n 1 457 TYR n 1 458 GLY n 1 459 ALA n 1 460 PHE n 1 461 VAL n 1 462 ASP n 1 463 ILE n 1 464 ASP n 1 465 PRO n 1 466 ARG n 1 467 SER n 1 468 GLU n 1 469 GLU n 1 470 ILE n 1 471 SER n 1 472 LEU n 1 473 ARG n 1 474 ASN n 1 475 LEU n 1 476 ILE n 1 477 ASP n 1 478 HIS n 1 479 SER n 1 480 ILE n 1 481 ILE n 1 482 GLU n 1 483 SER n 1 484 PHE n 1 485 GLY n 1 486 ALA n 1 487 GLY n 1 488 GLY n 1 489 LYS n 1 490 THR n 1 491 CYS n 1 492 ILE n 1 493 THR n 1 494 SER n 1 495 ARG n 1 496 ILE n 1 497 TYR n 1 498 PRO n 1 499 LYS n 1 500 PHE n 1 501 VAL n 1 502 ASN n 1 503 ASN n 1 504 GLU n 1 505 GLU n 1 506 ALA n 1 507 HIS n 1 508 LEU n 1 509 PHE n 1 510 VAL n 1 511 PHE n 1 512 ASN n 1 513 ASN n 1 514 GLY n 1 515 THR n 1 516 GLN n 1 517 ASN n 1 518 VAL n 1 519 LYS n 1 520 ILE n 1 521 SER n 1 522 GLU n 1 523 MET n 1 524 SER n 1 525 ALA n 1 526 TRP n 1 527 SER n 1 528 MET n 1 529 LYS n 1 530 ASN n 1 531 ALA n 1 532 LYS n 1 533 PHE n 1 534 VAL n 1 535 VAL n 1 536 ASP n 1 537 GLN n 1 538 SER n 1 539 VAL n 1 540 LYS n 1 541 SER n 1 542 ALA n 1 543 ALA n # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _entity_src_gen.pdbx_seq_type ? _entity_src_gen.pdbx_beg_seq_num ? _entity_src_gen.pdbx_end_seq_num ? _entity_src_gen.gene_src_common_name chicory _entity_src_gen.gene_src_genus Cichorium _entity_src_gen.pdbx_gene_src_gene '1-feh IIa' _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain ? _entity_src_gen.gene_src_tissue ? _entity_src_gen.gene_src_tissue_fraction ? _entity_src_gen.gene_src_details ? _entity_src_gen.pdbx_gene_src_fragment ? _entity_src_gen.pdbx_gene_src_scientific_name 'Cichorium intybus' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 13427 _entity_src_gen.pdbx_gene_src_variant ? _entity_src_gen.pdbx_gene_src_cell_line ? _entity_src_gen.pdbx_gene_src_atcc ? _entity_src_gen.pdbx_gene_src_organ ? _entity_src_gen.pdbx_gene_src_organelle ? _entity_src_gen.pdbx_gene_src_cell ? _entity_src_gen.pdbx_gene_src_cellular_location ? _entity_src_gen.host_org_common_name ? _entity_src_gen.pdbx_host_org_scientific_name 'Pichia pastoris' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 4922 _entity_src_gen.host_org_genus Pichia _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 GB _struct_ref.db_code CAC37922 _struct_ref.pdbx_db_accession 13940209 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;QQIEQPYRTGYHFQPPSNWMNDPNGPMLYQGVYHFFYQYNPYAATFGDVIIWGHAVSYDLVNWIHLDPAIYPTQEADSKS CWSGSATILPGNIPAMLYTGSDSKSRQVQDLAWPKNLSDPFLREWVKHPKNPLITPPEGVKDDCFRDPSTAWLGPDGVWR IVVGGDRDNNGMAFLYQSTDFVNWKRYDQPLSSADATGTWECPDFYPVPLNSTNGLDTSVYGGSVRHVMKAGFEGHDWYT IGTYSPDRENFLPQNGLSLTGSTLDLRYDYGQFYASKSFFDDAKNRRVLWAWVPETDSQADDIEKGWAGLQSFPRALWID RNGKQLIQWPVEEIEELRQNQVNLQNKNLKPGSVLEIHGIAASQADVTISFKLEGLKEAEVLDTTLVDPQALCNERGASS RGALGPFGLLAMASKDLKEQSAIFFRVFQNQLGRYSVLMCSDLSRSTVRSNIDTTSYGAFVDIDPRSEEISLRNLIDHSI IESFGAGGKTCITSRIYPKFVNNEEAHLFVFNNGTQNVKISEMSAWSMKNAKFVVDQSVKSAA ; _struct_ref.pdbx_align_begin 39 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 1ST8 _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 1 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 543 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession 13940209 _struct_ref_seq.db_align_beg 39 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 581 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 1 _struct_ref_seq.pdbx_auth_seq_align_end 543 # 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 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 GOL non-polymer . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3' 92.094 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MAN D-saccharide . ALPHA-D-MANNOSE ? 'C6 H12 O6' 180.156 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 NDG D-saccharide . '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 1ST8 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_percent_sol 83 _exptl_crystal.description ? _exptl_crystal.density_Matthews 7.25 _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.temp 277 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 7.0 _exptl_crystal_grow.pdbx_details 'sodium potassium phosphate, potassium phosphate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K' _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 MARRESEARCH _diffrn_detector.pdbx_collection_date 2002-05-23 _diffrn_detector.details 'bent mirror' # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator 'triangular monochromator' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.81100 _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_synchrotron_site 'EMBL/DESY, Hamburg' _diffrn_source.pdbx_synchrotron_beamline X11 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 0.81100 # _reflns.entry_id 1ST8 _reflns.observed_criterion_sigma_I 0 _reflns.observed_criterion_sigma_F 1.41 _reflns.d_resolution_low 30.0 _reflns.d_resolution_high 2.35 _reflns.number_obs 69991 _reflns.number_all 74996 _reflns.percent_possible_obs 84 _reflns.pdbx_Rmerge_I_obs 0.075 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI ? _reflns.B_iso_Wilson_estimate 30.6 _reflns.pdbx_redundancy 4.8 _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 2.35 _reflns_shell.d_res_low 2.39 _reflns_shell.percent_possible_all 98.7 _reflns_shell.Rmerge_I_obs ? _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs ? _reflns_shell.pdbx_redundancy ? _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all 3698 _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 1ST8 _refine.ls_number_reflns_obs 69991 _refine.ls_number_reflns_all 69991 _refine.pdbx_ls_sigma_I 0.0 _refine.pdbx_ls_sigma_F 0.0 _refine.pdbx_data_cutoff_high_absF 381717.76 _refine.pdbx_data_cutoff_low_absF 0.000000 _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 29.60 _refine.ls_d_res_high 2.35 _refine.ls_percent_reflns_obs 92.7 _refine.ls_R_factor_obs 0.183 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.183 _refine.ls_R_factor_R_free 0.2 _refine.ls_R_factor_R_free_error 0.003 _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.1 _refine.ls_number_reflns_R_free 3576 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.B_iso_mean 32.1 _refine.aniso_B[1][1] 2.48 _refine.aniso_B[2][2] 2.48 _refine.aniso_B[3][3] -4.97 _refine.aniso_B[1][2] 0.00 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details 'FLAT MODEL' _refine.solvent_model_param_ksol 0.359725 _refine.solvent_model_param_bsol 34.8612 _refine.pdbx_solvent_vdw_probe_radii ? _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii ? _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details ? _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct SAD _refine.pdbx_isotropic_thermal_model RESTRAINED _refine.pdbx_stereochemistry_target_values 'Engh & Huber' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML ? _refine.overall_SU_B ? _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_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_analyze.entry_id 1ST8 _refine_analyze.Luzzati_coordinate_error_obs 0.25 _refine_analyze.Luzzati_sigma_a_obs 0.25 _refine_analyze.Luzzati_d_res_low_obs 5.00 _refine_analyze.Luzzati_coordinate_error_free 0.28 _refine_analyze.Luzzati_sigma_a_free 0.26 _refine_analyze.Luzzati_d_res_low_free ? _refine_analyze.number_disordered_residues ? _refine_analyze.occupancy_sum_hydrogen ? _refine_analyze.occupancy_sum_non_hydrogen ? _refine_analyze.pdbx_Luzzati_d_res_high_obs ? _refine_analyze.pdbx_refine_id 'X-RAY DIFFRACTION' # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 4274 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 91 _refine_hist.number_atoms_solvent 331 _refine_hist.number_atoms_total 4696 _refine_hist.d_res_high 2.35 _refine_hist.d_res_low 29.60 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function c_bond_d 0.006 ? ? ? 'X-RAY DIFFRACTION' ? c_angle_deg 1.4 ? ? ? 'X-RAY DIFFRACTION' ? c_dihedral_angle_d 26.0 ? ? ? 'X-RAY DIFFRACTION' ? c_improper_angle_d 0.83 ? ? ? 'X-RAY DIFFRACTION' ? c_mcbond_it 1.15 1.50 ? ? 'X-RAY DIFFRACTION' ? c_mcangle_it 1.91 2.00 ? ? 'X-RAY DIFFRACTION' ? c_scbond_it 2.16 2.00 ? ? 'X-RAY DIFFRACTION' ? c_scangle_it 3.20 2.50 ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_total_number_of_bins_used 6 _refine_ls_shell.d_res_high 2.35 _refine_ls_shell.d_res_low 2.50 _refine_ls_shell.number_reflns_R_work 9980 _refine_ls_shell.R_factor_R_work 0.245 _refine_ls_shell.percent_reflns_obs 85.2 _refine_ls_shell.R_factor_R_free 0.262 _refine_ls_shell.R_factor_R_free_error 0.011 _refine_ls_shell.percent_reflns_R_free 5.5 _refine_ls_shell.number_reflns_R_free 580 _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.number_reflns_all ? _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.R_factor_all ? # loop_ _pdbx_xplor_file.serial_no _pdbx_xplor_file.param_file _pdbx_xplor_file.topol_file _pdbx_xplor_file.pdbx_refine_id 1 PROTEIN_REP.PARAM PROTEIN.TOP 'X-RAY DIFFRACTION' 2 WATER_REP.PARAM WATER.TOP 'X-RAY DIFFRACTION' 3 CARBOHYDRATE.PARAM CARBOHYDRATE.TOP 'X-RAY DIFFRACTION' 4 GOL.PARAM GOL.TOP 'X-RAY DIFFRACTION' # _struct.entry_id 1ST8 _struct.title 'Crystal structure of fructan 1-exohydrolase IIa from Cichorium intybus' _struct.pdbx_descriptor 'fructan 1-exohydrolase IIa (E.C.3.2.1.80)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 1ST8 _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'five fold beta propeller, HYDROLASE' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 4 ? E N N 3 ? F N N 3 ? G N N 5 ? H N N 5 ? I N N 5 ? J N N 5 ? K N N 6 ? # _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 GLN A 74 ? SER A 78 ? GLN A 74 SER A 78 5 ? 5 HELX_P HELX_P2 2 SER A 298 ? GLY A 306 ? SER A 298 GLY A 306 1 ? 9 HELX_P HELX_P3 3 GLU A 332 ? GLU A 336 ? GLU A 332 GLU A 336 5 ? 5 HELX_P HELX_P4 4 GLY A 375 ? ALA A 379 ? GLY A 375 ALA A 379 5 ? 5 HELX_P HELX_P5 5 ASP A 388 ? ARG A 396 ? ASP A 388 ARG A 396 1 ? 9 HELX_P HELX_P6 6 LYS A 499 ? ASN A 503 ? LYS A 499 ASN A 503 5 ? 5 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 393 SG ? ? ? 1_555 A CYS 440 SG ? ? A CYS 393 A CYS 440 1_555 ? ? ? ? ? ? ? 2.044 ? covale1 covale ? ? A ASN 116 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 116 A NAG 680 1_555 ? ? ? ? ? ? ? 1.448 ? covale2 covale ? ? A ASN 513 ND2 ? ? ? 1_555 B NDG . C1 ? ? A ASN 513 A NDG 650 1_555 ? ? ? ? ? ? ? 1.458 ? covale3 covale ? ? B NDG . O4 ? ? ? 1_555 C NAG . C1 ? ? A NDG 650 A NAG 660 1_555 ? ? ? ? ? ? ? 1.398 ? covale4 covale ? ? C NAG . O4 ? ? ? 1_555 D MAN . C1 ? ? A NAG 660 A MAN 670 1_555 ? ? ? ? ? ? ? 1.394 ? covale5 covale ? ? E NAG . O4 ? ? ? 1_555 F NAG . C1 ? ? A NAG 680 A NAG 690 1_555 ? ? ? ? ? ? ? 1.389 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 ASN 131 A . ? ASN 131 A PRO 132 A ? PRO 132 A 1 0.08 2 GLY 405 A . ? GLY 405 A PRO 406 A ? PRO 406 A 1 0.17 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 6 ? B ? 4 ? C ? 4 ? D ? 4 ? E ? 4 ? F ? 4 ? G ? 3 ? H ? 4 ? I ? 6 ? J ? 5 ? K ? 6 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? parallel A 2 3 ? anti-parallel A 3 4 ? anti-parallel A 4 5 ? anti-parallel A 5 6 ? parallel B 1 2 ? anti-parallel B 2 3 ? anti-parallel B 3 4 ? anti-parallel C 1 2 ? anti-parallel C 2 3 ? anti-parallel C 3 4 ? anti-parallel D 1 2 ? anti-parallel D 2 3 ? anti-parallel D 3 4 ? anti-parallel E 1 2 ? anti-parallel E 2 3 ? anti-parallel E 3 4 ? anti-parallel F 1 2 ? anti-parallel F 2 3 ? anti-parallel F 3 4 ? anti-parallel G 1 2 ? anti-parallel G 2 3 ? anti-parallel H 1 2 ? anti-parallel H 2 3 ? anti-parallel H 3 4 ? anti-parallel I 1 2 ? anti-parallel I 2 3 ? anti-parallel I 3 4 ? anti-parallel I 4 5 ? anti-parallel I 5 6 ? anti-parallel J 1 2 ? anti-parallel J 2 3 ? anti-parallel J 3 4 ? anti-parallel J 4 5 ? parallel K 1 2 ? anti-parallel K 2 3 ? anti-parallel K 3 4 ? anti-parallel K 4 5 ? anti-parallel K 5 6 ? 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 TRP A 307 ? ALA A 308 ? TRP A 307 ALA A 308 A 2 ASN A 18 ? TYR A 29 ? ASN A 18 TYR A 29 A 3 VAL A 32 ? ASN A 40 ? VAL A 32 ASN A 40 A 4 ILE A 51 ? SER A 57 ? ILE A 51 SER A 57 A 5 TRP A 63 ? HIS A 65 ? TRP A 63 HIS A 65 A 6 PHE A 533 ? VAL A 535 ? PHE A 533 VAL A 535 B 1 SER A 80 ? LEU A 89 ? SER A 80 LEU A 89 B 2 ILE A 93 ? SER A 101 ? ILE A 93 SER A 101 B 3 GLN A 107 ? PRO A 114 ? GLN A 107 PRO A 114 B 4 TRP A 125 ? LYS A 127 ? TRP A 125 LYS A 127 C 1 PHE A 145 ? ARG A 146 ? PHE A 145 ARG A 146 C 2 TRP A 159 ? ARG A 167 ? TRP A 159 ARG A 167 C 3 ASN A 170 ? SER A 178 ? ASN A 170 SER A 178 C 4 LYS A 185 ? ARG A 186 ? LYS A 185 ARG A 186 D 1 TRP A 152 ? LEU A 153 ? TRP A 152 LEU A 153 D 2 TRP A 159 ? ARG A 167 ? TRP A 159 ARG A 167 D 3 ASN A 170 ? SER A 178 ? ASN A 170 SER A 178 D 4 SER A 192 ? ALA A 194 ? SER A 192 ALA A 194 E 1 GLU A 201 ? PRO A 209 ? GLU A 201 PRO A 209 E 2 VAL A 225 ? PHE A 233 ? VAL A 225 PHE A 233 E 3 HIS A 236 ? SER A 245 ? HIS A 236 SER A 245 E 4 ASN A 250 ? PRO A 253 ? ASN A 250 PRO A 253 F 1 GLU A 201 ? PRO A 209 ? GLU A 201 PRO A 209 F 2 VAL A 225 ? PHE A 233 ? VAL A 225 PHE A 233 F 3 HIS A 236 ? SER A 245 ? HIS A 236 SER A 245 F 4 LEU A 266 ? ARG A 267 ? LEU A 266 ARG A 267 G 1 TYR A 274 ? ASP A 281 ? TYR A 274 ASP A 281 G 2 ARG A 286 ? VAL A 293 ? ARG A 286 VAL A 293 G 3 LEU A 310 ? GLN A 311 ? LEU A 310 GLN A 311 H 1 TYR A 274 ? ASP A 281 ? TYR A 274 ASP A 281 H 2 ARG A 286 ? VAL A 293 ? ARG A 286 VAL A 293 H 3 ARG A 315 ? ILE A 319 ? ARG A 315 ILE A 319 H 4 LEU A 326 ? PRO A 330 ? LEU A 326 PRO A 330 I 1 ARG A 338 ? LEU A 349 ? ARG A 338 LEU A 349 I 2 VAL A 518 ? MET A 528 ? VAL A 518 MET A 528 I 3 GLN A 364 ? LEU A 373 ? GLN A 364 LEU A 373 I 4 ILE A 470 ? ASP A 477 ? ILE A 470 ASP A 477 I 5 ILE A 480 ? GLY A 485 ? ILE A 480 GLY A 485 I 6 THR A 490 ? ARG A 495 ? THR A 490 ARG A 495 J 1 SER A 353 ? GLU A 356 ? SER A 353 GLU A 356 J 2 HIS A 507 ? ASN A 512 ? HIS A 507 ASN A 512 J 3 PHE A 407 ? ALA A 413 ? PHE A 407 ALA A 413 J 4 SER A 421 ? GLN A 429 ? SER A 421 GLN A 429 J 5 GLU A 380 ? VAL A 381 ? GLU A 380 VAL A 381 K 1 SER A 353 ? GLU A 356 ? SER A 353 GLU A 356 K 2 HIS A 507 ? ASN A 512 ? HIS A 507 ASN A 512 K 3 PHE A 407 ? ALA A 413 ? PHE A 407 ALA A 413 K 4 SER A 421 ? GLN A 429 ? SER A 421 GLN A 429 K 5 TYR A 435 ? ASP A 442 ? TYR A 435 ASP A 442 K 6 TYR A 457 ? VAL A 461 ? TYR A 457 VAL A 461 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 O ALA A 308 ? O ALA A 308 N ASN A 18 ? N ASN A 18 A 2 3 N ASN A 24 ? N ASN A 24 O PHE A 36 ? O PHE A 36 A 3 4 N TYR A 33 ? N TYR A 33 O SER A 57 ? O SER A 57 A 4 5 N VAL A 56 ? N VAL A 56 O ILE A 64 ? O ILE A 64 A 5 6 N HIS A 65 ? N HIS A 65 O VAL A 534 ? O VAL A 534 B 1 2 N THR A 87 ? N THR A 87 O ALA A 95 ? O ALA A 95 B 2 3 N MET A 96 ? N MET A 96 O ALA A 112 ? O ALA A 112 B 3 4 N TRP A 113 ? N TRP A 113 O VAL A 126 ? O VAL A 126 C 1 2 N ARG A 146 ? N ARG A 146 O GLY A 164 ? O GLY A 164 C 2 3 N TRP A 159 ? N TRP A 159 O SER A 178 ? O SER A 178 C 3 4 N GLN A 177 ? N GLN A 177 O LYS A 185 ? O LYS A 185 D 1 2 N TRP A 152 ? N TRP A 152 O ARG A 160 ? O ARG A 160 D 2 3 N TRP A 159 ? N TRP A 159 O SER A 178 ? O SER A 178 D 3 4 N ALA A 173 ? N ALA A 173 O SER A 192 ? O SER A 192 E 1 2 N TYR A 206 ? N TYR A 206 O VAL A 228 ? O VAL A 228 E 2 3 N HIS A 227 ? N HIS A 227 O GLY A 242 ? O GLY A 242 E 3 4 N THR A 243 ? N THR A 243 O LEU A 252 ? O LEU A 252 F 1 2 N TYR A 206 ? N TYR A 206 O VAL A 228 ? O VAL A 228 F 2 3 N HIS A 227 ? N HIS A 227 O GLY A 242 ? O GLY A 242 F 3 4 N TYR A 239 ? N TYR A 239 O LEU A 266 ? O LEU A 266 G 1 2 N ASP A 281 ? N ASP A 281 O ARG A 286 ? O ARG A 286 G 2 3 N VAL A 293 ? N VAL A 293 O LEU A 310 ? O LEU A 310 H 1 2 N ASP A 281 ? N ASP A 281 O ARG A 286 ? O ARG A 286 H 2 3 N LEU A 289 ? N LEU A 289 O ARG A 315 ? O ARG A 315 H 3 4 N TRP A 318 ? N TRP A 318 O ILE A 327 ? O ILE A 327 I 1 2 N LYS A 347 ? N LYS A 347 O ILE A 520 ? O ILE A 520 I 2 3 O SER A 524 ? O SER A 524 N THR A 368 ? N THR A 368 I 3 4 N VAL A 367 ? N VAL A 367 O ASN A 474 ? O ASN A 474 I 4 5 N ARG A 473 ? N ARG A 473 O PHE A 484 ? O PHE A 484 I 5 6 N GLY A 485 ? N GLY A 485 O THR A 490 ? O THR A 490 J 1 2 N LEU A 355 ? N LEU A 355 O VAL A 510 ? O VAL A 510 J 2 3 O PHE A 509 ? O PHE A 509 N LEU A 410 ? N LEU A 410 J 3 4 N LEU A 409 ? N LEU A 409 O ILE A 423 ? O ILE A 423 J 4 5 O GLN A 429 ? O GLN A 429 N GLU A 380 ? N GLU A 380 K 1 2 N LEU A 355 ? N LEU A 355 O VAL A 510 ? O VAL A 510 K 2 3 O PHE A 509 ? O PHE A 509 N LEU A 410 ? N LEU A 410 K 3 4 N LEU A 409 ? N LEU A 409 O ILE A 423 ? O ILE A 423 K 4 5 N PHE A 424 ? N PHE A 424 O CYS A 440 ? O CYS A 440 K 5 6 N SER A 441 ? N SER A 441 O TYR A 457 ? O TYR A 457 # 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 ? ? ? ? 8 'BINDING SITE FOR RESIDUE NDG A 650' AC2 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 660' AC3 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE MAN A 670' AC4 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 680' AC5 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG A 690' AC6 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE GOL A 1758' AC7 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE GOL A 1759' AC8 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE GOL A 1760' AC9 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE GOL A 1772' # 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 8 ALA A 398 ? ALA A 398 . ? 1_555 ? 2 AC1 8 SER A 399 ? SER A 399 . ? 1_555 ? 3 AC1 8 ARG A 401 ? ARG A 401 . ? 1_555 ? 4 AC1 8 GLN A 420 ? GLN A 420 . ? 1_555 ? 5 AC1 8 ARG A 445 ? ARG A 445 . ? 1_555 ? 6 AC1 8 ASN A 513 ? ASN A 513 . ? 1_555 ? 7 AC1 8 NAG C . ? NAG A 660 . ? 1_555 ? 8 AC1 8 HOH K . ? HOH A 1187 . ? 1_555 ? 9 AC2 3 ARG A 445 ? ARG A 445 . ? 1_555 ? 10 AC2 3 NDG B . ? NDG A 650 . ? 1_555 ? 11 AC2 3 MAN D . ? MAN A 670 . ? 1_555 ? 12 AC3 1 NAG C . ? NAG A 660 . ? 1_555 ? 13 AC4 6 ASN A 116 ? ASN A 116 . ? 1_555 ? 14 AC4 6 SER A 118 ? SER A 118 . ? 1_555 ? 15 AC4 6 ASP A 119 ? ASP A 119 . ? 1_555 ? 16 AC4 6 GLU A 234 ? GLU A 234 . ? 4_454 ? 17 AC4 6 NAG F . ? NAG A 690 . ? 1_555 ? 18 AC4 6 HOH K . ? HOH A 1331 . ? 1_555 ? 19 AC5 1 NAG E . ? NAG A 680 . ? 1_555 ? 20 AC6 6 ASP A 22 ? ASP A 22 . ? 1_555 ? 21 AC6 6 SER A 83 ? SER A 83 . ? 1_555 ? 22 AC6 6 ARG A 146 ? ARG A 146 . ? 1_555 ? 23 AC6 6 ASP A 147 ? ASP A 147 . ? 1_555 ? 24 AC6 6 GLU A 201 ? GLU A 201 . ? 1_555 ? 25 AC6 6 HOH K . ? HOH A 1218 . ? 1_555 ? 26 AC7 5 GLY A 235 ? GLY A 235 . ? 1_555 ? 27 AC7 5 TYR A 274 ? TYR A 274 . ? 1_555 ? 28 AC7 5 PRO A 294 ? PRO A 294 . ? 1_555 ? 29 AC7 5 HOH K . ? HOH A 1189 . ? 1_555 ? 30 AC7 5 HOH K . ? HOH A 1252 . ? 1_555 ? 31 AC8 2 PHE A 46 ? PHE A 46 . ? 1_555 ? 32 AC8 2 TRP A 292 ? TRP A 292 . ? 1_555 ? 33 AC9 10 LEU A 266 ? LEU A 266 . ? 1_555 ? 34 AC9 10 ARG A 267 ? ARG A 267 . ? 1_555 ? 35 AC9 10 TYR A 270 ? TYR A 270 . ? 1_555 ? 36 AC9 10 GLN A 325 ? GLN A 325 . ? 1_555 ? 37 AC9 10 PHE A 460 ? PHE A 460 . ? 1_555 ? 38 AC9 10 ASP A 462 ? ASP A 462 . ? 1_555 ? 39 AC9 10 LYS A 489 ? LYS A 489 . ? 1_555 ? 40 AC9 10 THR A 490 ? THR A 490 . ? 1_555 ? 41 AC9 10 HOH K . ? HOH A 1009 . ? 1_555 ? 42 AC9 10 HOH K . ? HOH A 1245 . ? 1_555 ? # _database_PDB_matrix.entry_id 1ST8 _database_PDB_matrix.origx[1][1] 1.000000 _database_PDB_matrix.origx[1][2] 0.000000 _database_PDB_matrix.origx[1][3] 0.000000 _database_PDB_matrix.origx[2][1] 0.000000 _database_PDB_matrix.origx[2][2] 1.000000 _database_PDB_matrix.origx[2][3] 0.000000 _database_PDB_matrix.origx[3][1] 0.000000 _database_PDB_matrix.origx[3][2] 0.000000 _database_PDB_matrix.origx[3][3] 1.000000 _database_PDB_matrix.origx_vector[1] 0.00000 _database_PDB_matrix.origx_vector[2] 0.00000 _database_PDB_matrix.origx_vector[3] 0.00000 # _atom_sites.entry_id 1ST8 _atom_sites.fract_transf_matrix[1][1] 0.007152 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.007152 _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] 0.005496 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . GLN A 1 2 ? 42.668 66.029 -12.897 1.00 60.55 ? 2 GLN A N 1 ATOM 2 C CA . GLN A 1 2 ? 41.298 66.568 -12.662 1.00 60.40 ? 2 GLN A CA 1 ATOM 3 C C . GLN A 1 2 ? 40.208 65.689 -13.264 1.00 58.41 ? 2 GLN A C 1 ATOM 4 O O . GLN A 1 2 ? 40.092 65.560 -14.483 1.00 58.55 ? 2 GLN A O 1 ATOM 5 C CB . GLN A 1 2 ? 41.186 67.984 -13.227 1.00 62.76 ? 2 GLN A CB 1 ATOM 6 C CG . GLN A 1 2 ? 41.231 69.063 -12.163 1.00 67.72 ? 2 GLN A CG 1 ATOM 7 C CD . GLN A 1 2 ? 39.975 69.097 -11.302 1.00 70.75 ? 2 GLN A CD 1 ATOM 8 O OE1 . GLN A 1 2 ? 39.922 69.802 -10.291 1.00 72.67 ? 2 GLN A OE1 1 ATOM 9 N NE2 . GLN A 1 2 ? 38.954 68.342 -11.703 1.00 71.62 ? 2 GLN A NE2 1 ATOM 10 N N . ILE A 1 3 ? 39.407 65.090 -12.388 1.00 55.52 ? 3 ILE A N 1 ATOM 11 C CA . ILE A 1 3 ? 38.315 64.215 -12.790 1.00 52.06 ? 3 ILE A CA 1 ATOM 12 C C . ILE A 1 3 ? 37.062 65.045 -13.057 1.00 50.13 ? 3 ILE A C 1 ATOM 13 O O . ILE A 1 3 ? 36.710 65.918 -12.266 1.00 50.35 ? 3 ILE A O 1 ATOM 14 C CB . ILE A 1 3 ? 38.040 63.180 -11.683 1.00 51.84 ? 3 ILE A CB 1 ATOM 15 C CG1 . ILE A 1 3 ? 39.317 62.374 -11.426 1.00 51.67 ? 3 ILE A CG1 1 ATOM 16 C CG2 . ILE A 1 3 ? 36.898 62.260 -12.083 1.00 50.04 ? 3 ILE A CG2 1 ATOM 17 C CD1 . ILE A 1 3 ? 39.228 61.410 -10.265 1.00 53.36 ? 3 ILE A CD1 1 ATOM 18 N N . GLU A 1 4 ? 36.400 64.779 -14.178 1.00 48.60 ? 4 GLU A N 1 ATOM 19 C CA . GLU A 1 4 ? 35.188 65.514 -14.540 1.00 48.65 ? 4 GLU A CA 1 ATOM 20 C C . GLU A 1 4 ? 33.954 64.999 -13.804 1.00 44.72 ? 4 GLU A C 1 ATOM 21 O O . GLU A 1 4 ? 33.755 63.787 -13.693 1.00 43.84 ? 4 GLU A O 1 ATOM 22 C CB . GLU A 1 4 ? 34.935 65.419 -16.050 1.00 53.66 ? 4 GLU A CB 1 ATOM 23 C CG . GLU A 1 4 ? 36.018 66.054 -16.914 1.00 62.64 ? 4 GLU A CG 1 ATOM 24 C CD . GLU A 1 4 ? 36.194 67.544 -16.640 1.00 66.93 ? 4 GLU A CD 1 ATOM 25 O OE1 . GLU A 1 4 ? 35.194 68.291 -16.758 1.00 69.03 ? 4 GLU A OE1 1 ATOM 26 O OE2 . GLU A 1 4 ? 37.330 67.964 -16.310 1.00 68.27 ? 4 GLU A OE2 1 ATOM 27 N N . GLN A 1 5 ? 33.133 65.926 -13.310 1.00 39.35 ? 5 GLN A N 1 ATOM 28 C CA . GLN A 1 5 ? 31.899 65.585 -12.603 1.00 35.19 ? 5 GLN A CA 1 ATOM 29 C C . GLN A 1 5 ? 32.084 64.432 -11.625 1.00 33.81 ? 5 GLN A C 1 ATOM 30 O O . GLN A 1 5 ? 31.403 63.409 -11.720 1.00 33.89 ? 5 GLN A O 1 ATOM 31 C CB . GLN A 1 5 ? 30.819 65.218 -13.616 1.00 33.39 ? 5 GLN A CB 1 ATOM 32 C CG . GLN A 1 5 ? 30.364 66.385 -14.464 1.00 32.40 ? 5 GLN A CG 1 ATOM 33 C CD . GLN A 1 5 ? 29.529 67.374 -13.678 1.00 32.64 ? 5 GLN A CD 1 ATOM 34 O OE1 . GLN A 1 5 ? 29.186 68.443 -14.176 1.00 34.34 ? 5 GLN A OE1 1 ATOM 35 N NE2 . GLN A 1 5 ? 29.190 67.018 -12.444 1.00 30.78 ? 5 GLN A NE2 1 ATOM 36 N N . PRO A 1 6 ? 32.999 64.590 -10.661 1.00 31.51 ? 6 PRO A N 1 ATOM 37 C CA . PRO A 1 6 ? 33.253 63.536 -9.679 1.00 30.34 ? 6 PRO A CA 1 ATOM 38 C C . PRO A 1 6 ? 32.064 63.200 -8.779 1.00 30.43 ? 6 PRO A C 1 ATOM 39 O O . PRO A 1 6 ? 32.053 62.149 -8.138 1.00 31.06 ? 6 PRO A O 1 ATOM 40 C CB . PRO A 1 6 ? 34.440 64.086 -8.894 1.00 28.91 ? 6 PRO A CB 1 ATOM 41 C CG . PRO A 1 6 ? 34.175 65.561 -8.910 1.00 29.69 ? 6 PRO A CG 1 ATOM 42 C CD . PRO A 1 6 ? 33.774 65.804 -10.344 1.00 29.68 ? 6 PRO A CD 1 ATOM 43 N N . TYR A 1 7 ? 31.064 64.076 -8.731 1.00 29.64 ? 7 TYR A N 1 ATOM 44 C CA . TYR A 1 7 ? 29.904 63.828 -7.880 1.00 29.08 ? 7 TYR A CA 1 ATOM 45 C C . TYR A 1 7 ? 28.738 63.139 -8.580 1.00 29.55 ? 7 TYR A C 1 ATOM 46 O O . TYR A 1 7 ? 27.784 62.717 -7.922 1.00 30.16 ? 7 TYR A O 1 ATOM 47 C CB . TYR A 1 7 ? 29.439 65.133 -7.233 1.00 28.18 ? 7 TYR A CB 1 ATOM 48 C CG . TYR A 1 7 ? 30.531 65.786 -6.420 1.00 30.04 ? 7 TYR A CG 1 ATOM 49 C CD1 . TYR A 1 7 ? 31.181 65.082 -5.404 1.00 29.08 ? 7 TYR A CD1 1 ATOM 50 C CD2 . TYR A 1 7 ? 30.944 67.091 -6.686 1.00 29.54 ? 7 TYR A CD2 1 ATOM 51 C CE1 . TYR A 1 7 ? 32.219 65.661 -4.676 1.00 30.17 ? 7 TYR A CE1 1 ATOM 52 C CE2 . TYR A 1 7 ? 31.982 67.680 -5.964 1.00 30.27 ? 7 TYR A CE2 1 ATOM 53 C CZ . TYR A 1 7 ? 32.613 66.959 -4.962 1.00 30.74 ? 7 TYR A CZ 1 ATOM 54 O OH . TYR A 1 7 ? 33.632 67.535 -4.243 1.00 32.15 ? 7 TYR A OH 1 ATOM 55 N N . ARG A 1 8 ? 28.798 63.019 -9.902 1.00 27.98 ? 8 ARG A N 1 ATOM 56 C CA . ARG A 1 8 ? 27.723 62.332 -10.602 1.00 28.60 ? 8 ARG A CA 1 ATOM 57 C C . ARG A 1 8 ? 27.837 60.862 -10.225 1.00 28.36 ? 8 ARG A C 1 ATOM 58 O O . ARG A 1 8 ? 28.942 60.350 -10.021 1.00 29.30 ? 8 ARG A O 1 ATOM 59 C CB . ARG A 1 8 ? 27.833 62.519 -12.120 1.00 25.90 ? 8 ARG A CB 1 ATOM 60 C CG . ARG A 1 8 ? 27.455 63.933 -12.572 1.00 27.32 ? 8 ARG A CG 1 ATOM 61 C CD . ARG A 1 8 ? 27.344 64.041 -14.081 1.00 25.67 ? 8 ARG A CD 1 ATOM 62 N NE . ARG A 1 8 ? 26.195 63.305 -14.602 1.00 26.38 ? 8 ARG A NE 1 ATOM 63 C CZ . ARG A 1 8 ? 24.934 63.719 -14.518 1.00 26.85 ? 8 ARG A CZ 1 ATOM 64 N NH1 . ARG A 1 8 ? 24.646 64.876 -13.934 1.00 26.66 ? 8 ARG A NH1 1 ATOM 65 N NH2 . ARG A 1 8 ? 23.957 62.971 -15.015 1.00 25.83 ? 8 ARG A NH2 1 ATOM 66 N N . THR A 1 9 ? 26.695 60.192 -10.110 1.00 27.35 ? 9 THR A N 1 ATOM 67 C CA . THR A 1 9 ? 26.674 58.788 -9.727 1.00 25.56 ? 9 THR A CA 1 ATOM 68 C C . THR A 1 9 ? 26.849 57.875 -10.933 1.00 25.92 ? 9 THR A C 1 ATOM 69 O O . THR A 1 9 ? 26.623 58.283 -12.075 1.00 26.18 ? 9 THR A O 1 ATOM 70 C CB . THR A 1 9 ? 25.354 58.434 -9.059 1.00 25.14 ? 9 THR A CB 1 ATOM 71 O OG1 . THR A 1 9 ? 24.315 58.479 -10.042 1.00 25.26 ? 9 THR A OG1 1 ATOM 72 C CG2 . THR A 1 9 ? 25.034 59.425 -7.938 1.00 23.01 ? 9 THR A CG2 1 ATOM 73 N N . GLY A 1 10 ? 27.237 56.631 -10.669 1.00 25.04 ? 10 GLY A N 1 ATOM 74 C CA . GLY A 1 10 ? 27.435 55.678 -11.742 1.00 23.19 ? 10 GLY A CA 1 ATOM 75 C C . GLY A 1 10 ? 26.250 54.760 -11.965 1.00 23.79 ? 10 GLY A C 1 ATOM 76 O O . GLY A 1 10 ? 26.065 54.258 -13.073 1.00 24.62 ? 10 GLY A O 1 ATOM 77 N N . TYR A 1 11 ? 25.448 54.519 -10.929 1.00 23.56 ? 11 TYR A N 1 ATOM 78 C CA . TYR A 1 11 ? 24.291 53.643 -11.087 1.00 22.73 ? 11 TYR A CA 1 ATOM 79 C C . TYR A 1 11 ? 22.994 54.109 -10.414 1.00 22.23 ? 11 TYR A C 1 ATOM 80 O O . TYR A 1 11 ? 22.063 53.321 -10.232 1.00 23.39 ? 11 TYR A O 1 ATOM 81 C CB . TYR A 1 11 ? 24.642 52.210 -10.652 1.00 21.83 ? 11 TYR A CB 1 ATOM 82 C CG . TYR A 1 11 ? 25.116 52.065 -9.225 1.00 21.94 ? 11 TYR A CG 1 ATOM 83 C CD1 . TYR A 1 11 ? 24.209 51.881 -8.180 1.00 21.59 ? 11 TYR A CD1 1 ATOM 84 C CD2 . TYR A 1 11 ? 26.476 52.126 -8.917 1.00 20.75 ? 11 TYR A CD2 1 ATOM 85 C CE1 . TYR A 1 11 ? 24.649 51.761 -6.856 1.00 21.99 ? 11 TYR A CE1 1 ATOM 86 C CE2 . TYR A 1 11 ? 26.925 52.010 -7.605 1.00 19.30 ? 11 TYR A CE2 1 ATOM 87 C CZ . TYR A 1 11 ? 26.007 51.829 -6.580 1.00 21.99 ? 11 TYR A CZ 1 ATOM 88 O OH . TYR A 1 11 ? 26.452 51.733 -5.280 1.00 23.18 ? 11 TYR A OH 1 ATOM 89 N N . HIS A 1 12 ? 22.932 55.381 -10.040 1.00 20.88 ? 12 HIS A N 1 ATOM 90 C CA . HIS A 1 12 ? 21.710 55.926 -9.454 1.00 21.64 ? 12 HIS A CA 1 ATOM 91 C C . HIS A 1 12 ? 21.013 56.722 -10.544 1.00 22.42 ? 12 HIS A C 1 ATOM 92 O O . HIS A 1 12 ? 21.672 57.283 -11.419 1.00 22.02 ? 12 HIS A O 1 ATOM 93 C CB . HIS A 1 12 ? 22.013 56.851 -8.279 1.00 19.89 ? 12 HIS A CB 1 ATOM 94 C CG . HIS A 1 12 ? 22.252 56.126 -6.996 1.00 20.89 ? 12 HIS A CG 1 ATOM 95 N ND1 . HIS A 1 12 ? 23.406 55.417 -6.747 1.00 20.53 ? 12 HIS A ND1 1 ATOM 96 C CD2 . HIS A 1 12 ? 21.465 55.960 -5.906 1.00 19.59 ? 12 HIS A CD2 1 ATOM 97 C CE1 . HIS A 1 12 ? 23.320 54.844 -5.560 1.00 21.14 ? 12 HIS A CE1 1 ATOM 98 N NE2 . HIS A 1 12 ? 22.152 55.158 -5.029 1.00 20.34 ? 12 HIS A NE2 1 ATOM 99 N N . PHE A 1 13 ? 19.688 56.777 -10.508 1.00 22.60 ? 13 PHE A N 1 ATOM 100 C CA . PHE A 1 13 ? 18.993 57.528 -11.535 1.00 22.19 ? 13 PHE A CA 1 ATOM 101 C C . PHE A 1 13 ? 19.116 59.021 -11.332 1.00 23.39 ? 13 PHE A C 1 ATOM 102 O O . PHE A 1 13 ? 18.991 59.522 -10.217 1.00 24.52 ? 13 PHE A O 1 ATOM 103 C CB . PHE A 1 13 ? 17.501 57.195 -11.589 1.00 22.49 ? 13 PHE A CB 1 ATOM 104 C CG . PHE A 1 13 ? 16.777 57.914 -12.704 1.00 22.02 ? 13 PHE A CG 1 ATOM 105 C CD1 . PHE A 1 13 ? 16.677 57.338 -13.968 1.00 22.91 ? 13 PHE A CD1 1 ATOM 106 C CD2 . PHE A 1 13 ? 16.269 59.199 -12.510 1.00 19.95 ? 13 PHE A CD2 1 ATOM 107 C CE1 . PHE A 1 13 ? 16.084 58.033 -15.031 1.00 22.75 ? 13 PHE A CE1 1 ATOM 108 C CE2 . PHE A 1 13 ? 15.677 59.904 -13.560 1.00 21.81 ? 13 PHE A CE2 1 ATOM 109 C CZ . PHE A 1 13 ? 15.584 59.321 -14.826 1.00 22.27 ? 13 PHE A CZ 1 ATOM 110 N N . GLN A 1 14 ? 19.348 59.726 -12.430 1.00 23.95 ? 14 GLN A N 1 ATOM 111 C CA . GLN A 1 14 ? 19.432 61.177 -12.420 1.00 24.10 ? 14 GLN A CA 1 ATOM 112 C C . GLN A 1 14 ? 19.413 61.607 -13.883 1.00 24.73 ? 14 GLN A C 1 ATOM 113 O O . GLN A 1 14 ? 19.901 60.886 -14.757 1.00 25.49 ? 14 GLN A O 1 ATOM 114 C CB . GLN A 1 14 ? 20.703 61.665 -11.693 1.00 23.27 ? 14 GLN A CB 1 ATOM 115 C CG . GLN A 1 14 ? 22.044 61.343 -12.351 1.00 23.81 ? 14 GLN A CG 1 ATOM 116 C CD . GLN A 1 14 ? 23.241 61.765 -11.481 1.00 27.32 ? 14 GLN A CD 1 ATOM 117 O OE1 . GLN A 1 14 ? 23.928 60.921 -10.886 1.00 26.50 ? 14 GLN A OE1 1 ATOM 118 N NE2 . GLN A 1 14 ? 23.483 63.075 -11.397 1.00 23.22 ? 14 GLN A NE2 1 ATOM 119 N N . PRO A 1 15 ? 18.821 62.772 -14.178 1.00 24.84 ? 15 PRO A N 1 ATOM 120 C CA . PRO A 1 15 ? 18.768 63.242 -15.568 1.00 25.49 ? 15 PRO A CA 1 ATOM 121 C C . PRO A 1 15 ? 20.142 63.668 -16.074 1.00 26.90 ? 15 PRO A C 1 ATOM 122 O O . PRO A 1 15 ? 21.080 63.822 -15.290 1.00 26.54 ? 15 PRO A O 1 ATOM 123 C CB . PRO A 1 15 ? 17.803 64.416 -15.491 1.00 24.80 ? 15 PRO A CB 1 ATOM 124 C CG . PRO A 1 15 ? 18.128 65.000 -14.139 1.00 26.24 ? 15 PRO A CG 1 ATOM 125 C CD . PRO A 1 15 ? 18.227 63.762 -13.261 1.00 24.39 ? 15 PRO A CD 1 ATOM 126 N N . PRO A 1 16 ? 20.280 63.858 -17.396 1.00 27.93 ? 16 PRO A N 1 ATOM 127 C CA . PRO A 1 16 ? 21.566 64.274 -17.958 1.00 27.42 ? 16 PRO A CA 1 ATOM 128 C C . PRO A 1 16 ? 22.090 65.509 -17.232 1.00 27.64 ? 16 PRO A C 1 ATOM 129 O O . PRO A 1 16 ? 23.290 65.640 -16.991 1.00 29.53 ? 16 PRO A O 1 ATOM 130 C CB . PRO A 1 16 ? 21.223 64.538 -19.418 1.00 26.95 ? 16 PRO A CB 1 ATOM 131 C CG . PRO A 1 16 ? 20.203 63.467 -19.692 1.00 26.85 ? 16 PRO A CG 1 ATOM 132 C CD . PRO A 1 16 ? 19.309 63.572 -18.469 1.00 27.59 ? 16 PRO A CD 1 ATOM 133 N N . SER A 1 17 ? 21.184 66.411 -16.875 1.00 27.15 ? 17 SER A N 1 ATOM 134 C CA . SER A 1 17 ? 21.572 67.610 -16.147 1.00 28.38 ? 17 SER A CA 1 ATOM 135 C C . SER A 1 17 ? 20.358 68.314 -15.570 1.00 27.70 ? 17 SER A C 1 ATOM 136 O O . SER A 1 17 ? 19.230 67.835 -15.687 1.00 27.13 ? 17 SER A O 1 ATOM 137 C CB . SER A 1 17 ? 22.328 68.580 -17.058 1.00 30.25 ? 17 SER A CB 1 ATOM 138 O OG . SER A 1 17 ? 21.447 69.175 -17.992 1.00 33.85 ? 17 SER A OG 1 ATOM 139 N N . ASN A 1 18 ? 20.611 69.458 -14.947 1.00 27.06 ? 18 ASN A N 1 ATOM 140 C CA . ASN A 1 18 ? 19.579 70.281 -14.336 1.00 27.36 ? 18 ASN A CA 1 ATOM 141 C C . ASN A 1 18 ? 19.008 69.730 -13.047 1.00 27.22 ? 18 ASN A C 1 ATOM 142 O O . ASN A 1 18 ? 19.517 68.760 -12.486 1.00 27.36 ? 18 ASN A O 1 ATOM 143 C CB . ASN A 1 18 ? 18.447 70.556 -15.323 1.00 29.32 ? 18 ASN A CB 1 ATOM 144 C CG . ASN A 1 18 ? 18.917 71.341 -16.520 1.00 31.31 ? 18 ASN A CG 1 ATOM 145 O OD1 . ASN A 1 18 ? 19.709 72.272 -16.388 1.00 34.41 ? 18 ASN A OD1 1 ATOM 146 N ND2 . ASN A 1 18 ? 18.432 70.978 -17.694 1.00 34.64 ? 18 ASN A ND2 1 ATOM 147 N N . TRP A 1 19 ? 17.934 70.364 -12.593 1.00 25.23 ? 19 TRP A N 1 ATOM 148 C CA . TRP A 1 19 ? 17.288 70.005 -11.345 1.00 25.64 ? 19 TRP A CA 1 ATOM 149 C C . TRP A 1 19 ? 16.197 68.948 -11.418 1.00 26.34 ? 19 TRP A C 1 ATOM 150 O O . TRP A 1 19 ? 15.369 68.941 -12.329 1.00 27.27 ? 19 TRP A O 1 ATOM 151 C CB . TRP A 1 19 ? 16.721 71.272 -10.700 1.00 22.97 ? 19 TRP A CB 1 ATOM 152 C CG . TRP A 1 19 ? 15.751 71.036 -9.575 1.00 21.95 ? 19 TRP A CG 1 ATOM 153 C CD1 . TRP A 1 19 ? 14.473 70.561 -9.674 1.00 21.54 ? 19 TRP A CD1 1 ATOM 154 C CD2 . TRP A 1 19 ? 15.970 71.311 -8.187 1.00 20.97 ? 19 TRP A CD2 1 ATOM 155 N NE1 . TRP A 1 19 ? 13.881 70.529 -8.431 1.00 22.37 ? 19 TRP A NE1 1 ATOM 156 C CE2 . TRP A 1 19 ? 14.779 70.985 -7.502 1.00 21.22 ? 19 TRP A CE2 1 ATOM 157 C CE3 . TRP A 1 19 ? 17.059 71.803 -7.455 1.00 21.40 ? 19 TRP A CE3 1 ATOM 158 C CZ2 . TRP A 1 19 ? 14.644 71.137 -6.118 1.00 23.28 ? 19 TRP A CZ2 1 ATOM 159 C CZ3 . TRP A 1 19 ? 16.925 71.954 -6.075 1.00 21.04 ? 19 TRP A CZ3 1 ATOM 160 C CH2 . TRP A 1 19 ? 15.725 71.623 -5.423 1.00 23.02 ? 19 TRP A CH2 1 ATOM 161 N N . MET A 1 20 ? 16.202 68.066 -10.425 1.00 25.05 ? 20 MET A N 1 ATOM 162 C CA . MET A 1 20 ? 15.206 67.014 -10.313 1.00 24.75 ? 20 MET A CA 1 ATOM 163 C C . MET A 1 20 ? 14.826 66.822 -8.857 1.00 23.92 ? 20 MET A C 1 ATOM 164 O O . MET A 1 20 ? 15.699 66.791 -7.995 1.00 25.43 ? 20 MET A O 1 ATOM 165 C CB . MET A 1 20 ? 15.745 65.675 -10.834 1.00 21.56 ? 20 MET A CB 1 ATOM 166 C CG . MET A 1 20 ? 14.920 64.466 -10.345 1.00 22.38 ? 20 MET A CG 1 ATOM 167 S SD . MET A 1 20 ? 15.499 62.809 -10.857 1.00 24.37 ? 20 MET A SD 1 ATOM 168 C CE . MET A 1 20 ? 16.976 62.631 -9.846 1.00 20.15 ? 20 MET A CE 1 ATOM 169 N N . ASN A 1 21 ? 13.533 66.742 -8.562 1.00 24.15 ? 21 ASN A N 1 ATOM 170 C CA . ASN A 1 21 ? 13.150 66.431 -7.195 1.00 24.49 ? 21 ASN A CA 1 ATOM 171 C C . ASN A 1 21 ? 12.208 65.218 -7.170 1.00 25.60 ? 21 ASN A C 1 ATOM 172 O O . ASN A 1 21 ? 12.584 64.155 -7.673 1.00 26.29 ? 21 ASN A O 1 ATOM 173 C CB . ASN A 1 21 ? 12.624 67.657 -6.381 1.00 23.98 ? 21 ASN A CB 1 ATOM 174 C CG . ASN A 1 21 ? 11.448 68.399 -7.021 1.00 25.26 ? 21 ASN A CG 1 ATOM 175 O OD1 . ASN A 1 21 ? 11.565 68.992 -8.093 1.00 23.57 ? 21 ASN A OD1 1 ATOM 176 N ND2 . ASN A 1 21 ? 10.313 68.403 -6.324 1.00 22.45 ? 21 ASN A ND2 1 ATOM 177 N N . ASP A 1 22 ? 11.008 65.354 -6.619 1.00 25.15 ? 22 ASP A N 1 ATOM 178 C CA . ASP A 1 22 ? 10.058 64.236 -6.494 1.00 24.52 ? 22 ASP A CA 1 ATOM 179 C C . ASP A 1 22 ? 9.914 63.182 -7.590 1.00 24.96 ? 22 ASP A C 1 ATOM 180 O O . ASP A 1 22 ? 9.817 63.504 -8.775 1.00 26.02 ? 22 ASP A O 1 ATOM 181 C CB . ASP A 1 22 ? 8.640 64.763 -6.279 1.00 25.27 ? 22 ASP A CB 1 ATOM 182 C CG . ASP A 1 22 ? 8.530 65.728 -5.136 1.00 25.88 ? 22 ASP A CG 1 ATOM 183 O OD1 . ASP A 1 22 ? 9.550 66.339 -4.738 1.00 24.80 ? 22 ASP A OD1 1 ATOM 184 O OD2 . ASP A 1 22 ? 7.392 65.887 -4.652 1.00 27.24 ? 22 ASP A OD2 1 ATOM 185 N N . PRO A 1 23 ? 9.888 61.896 -7.203 1.00 24.60 ? 23 PRO A N 1 ATOM 186 C CA . PRO A 1 23 ? 9.711 60.847 -8.211 1.00 23.21 ? 23 PRO A CA 1 ATOM 187 C C . PRO A 1 23 ? 8.202 60.916 -8.519 1.00 23.38 ? 23 PRO A C 1 ATOM 188 O O . PRO A 1 23 ? 7.404 61.159 -7.609 1.00 21.61 ? 23 PRO A O 1 ATOM 189 C CB . PRO A 1 23 ? 10.084 59.576 -7.455 1.00 22.15 ? 23 PRO A CB 1 ATOM 190 C CG . PRO A 1 23 ? 9.739 59.911 -6.022 1.00 20.61 ? 23 PRO A CG 1 ATOM 191 C CD . PRO A 1 23 ? 10.270 61.314 -5.903 1.00 23.44 ? 23 PRO A CD 1 ATOM 192 N N . ASN A 1 24 ? 7.806 60.726 -9.774 1.00 22.69 ? 24 ASN A N 1 ATOM 193 C CA . ASN A 1 24 ? 6.386 60.799 -10.126 1.00 23.29 ? 24 ASN A CA 1 ATOM 194 C C . ASN A 1 24 ? 5.895 59.603 -10.933 1.00 25.24 ? 24 ASN A C 1 ATOM 195 O O . ASN A 1 24 ? 6.636 59.024 -11.734 1.00 24.63 ? 24 ASN A O 1 ATOM 196 C CB . ASN A 1 24 ? 6.090 62.056 -10.956 1.00 23.51 ? 24 ASN A CB 1 ATOM 197 C CG . ASN A 1 24 ? 6.345 63.356 -10.202 1.00 24.62 ? 24 ASN A CG 1 ATOM 198 O OD1 . ASN A 1 24 ? 6.666 64.373 -10.821 1.00 25.16 ? 24 ASN A OD1 1 ATOM 199 N ND2 . ASN A 1 24 ? 6.184 63.340 -8.880 1.00 23.48 ? 24 ASN A ND2 1 ATOM 200 N N . GLY A 1 25 ? 4.626 59.262 -10.720 1.00 24.92 ? 25 GLY A N 1 ATOM 201 C CA . GLY A 1 25 ? 3.979 58.174 -11.431 1.00 25.19 ? 25 GLY A CA 1 ATOM 202 C C . GLY A 1 25 ? 4.748 56.901 -11.745 1.00 25.94 ? 25 GLY A C 1 ATOM 203 O O . GLY A 1 25 ? 4.622 56.385 -12.851 1.00 26.57 ? 25 GLY A O 1 ATOM 204 N N . PRO A 1 26 ? 5.543 56.361 -10.810 1.00 24.85 ? 26 PRO A N 1 ATOM 205 C CA . PRO A 1 26 ? 6.278 55.126 -11.112 1.00 24.35 ? 26 PRO A CA 1 ATOM 206 C C . PRO A 1 26 ? 5.266 54.017 -11.419 1.00 24.68 ? 26 PRO A C 1 ATOM 207 O O . PRO A 1 26 ? 4.191 53.976 -10.816 1.00 24.46 ? 26 PRO A O 1 ATOM 208 C CB . PRO A 1 26 ? 7.017 54.816 -9.809 1.00 23.88 ? 26 PRO A CB 1 ATOM 209 C CG . PRO A 1 26 ? 6.997 56.100 -9.039 1.00 26.10 ? 26 PRO A CG 1 ATOM 210 C CD . PRO A 1 26 ? 5.703 56.750 -9.400 1.00 24.35 ? 26 PRO A CD 1 ATOM 211 N N . MET A 1 27 ? 5.607 53.117 -12.337 1.00 24.29 ? 27 MET A N 1 ATOM 212 C CA . MET A 1 27 ? 4.717 52.008 -12.669 1.00 24.67 ? 27 MET A CA 1 ATOM 213 C C . MET A 1 27 ? 5.394 51.032 -13.617 1.00 25.37 ? 27 MET A C 1 ATOM 214 O O . MET A 1 27 ? 6.452 51.317 -14.179 1.00 24.97 ? 27 MET A O 1 ATOM 215 C CB . MET A 1 27 ? 3.430 52.520 -13.337 1.00 24.71 ? 27 MET A CB 1 ATOM 216 C CG . MET A 1 27 ? 3.659 53.111 -14.731 1.00 24.25 ? 27 MET A CG 1 ATOM 217 S SD . MET A 1 27 ? 2.158 53.497 -15.684 1.00 28.05 ? 27 MET A SD 1 ATOM 218 C CE . MET A 1 27 ? 2.821 54.643 -16.900 1.00 22.15 ? 27 MET A CE 1 ATOM 219 N N . LEU A 1 28 ? 4.769 49.872 -13.772 1.00 26.74 ? 28 LEU A N 1 ATOM 220 C CA . LEU A 1 28 ? 5.233 48.840 -14.687 1.00 27.30 ? 28 LEU A CA 1 ATOM 221 C C . LEU A 1 28 ? 4.070 48.694 -15.656 1.00 28.26 ? 28 LEU A C 1 ATOM 222 O O . LEU A 1 28 ? 2.935 48.463 -15.231 1.00 29.34 ? 28 LEU A O 1 ATOM 223 C CB . LEU A 1 28 ? 5.452 47.509 -13.963 1.00 26.19 ? 28 LEU A CB 1 ATOM 224 C CG . LEU A 1 28 ? 5.604 46.286 -14.887 1.00 26.13 ? 28 LEU A CG 1 ATOM 225 C CD1 . LEU A 1 28 ? 6.862 46.414 -15.735 1.00 23.93 ? 28 LEU A CD1 1 ATOM 226 C CD2 . LEU A 1 28 ? 5.665 45.018 -14.058 1.00 22.94 ? 28 LEU A CD2 1 ATOM 227 N N . TYR A 1 29 ? 4.335 48.849 -16.946 1.00 27.75 ? 29 TYR A N 1 ATOM 228 C CA . TYR A 1 29 ? 3.274 48.723 -17.935 1.00 27.55 ? 29 TYR A CA 1 ATOM 229 C C . TYR A 1 29 ? 3.765 47.987 -19.166 1.00 28.39 ? 29 TYR A C 1 ATOM 230 O O . TYR A 1 29 ? 4.761 48.379 -19.776 1.00 28.34 ? 29 TYR A O 1 ATOM 231 C CB . TYR A 1 29 ? 2.754 50.102 -18.345 1.00 26.90 ? 29 TYR A CB 1 ATOM 232 C CG . TYR A 1 29 ? 1.534 50.047 -19.239 1.00 26.30 ? 29 TYR A CG 1 ATOM 233 C CD1 . TYR A 1 29 ? 0.305 49.610 -18.746 1.00 24.19 ? 29 TYR A CD1 1 ATOM 234 C CD2 . TYR A 1 29 ? 1.611 50.416 -20.582 1.00 25.91 ? 29 TYR A CD2 1 ATOM 235 C CE1 . TYR A 1 29 ? -0.817 49.540 -19.565 1.00 25.31 ? 29 TYR A CE1 1 ATOM 236 C CE2 . TYR A 1 29 ? 0.495 50.349 -21.413 1.00 26.25 ? 29 TYR A CE2 1 ATOM 237 C CZ . TYR A 1 29 ? -0.714 49.910 -20.898 1.00 26.85 ? 29 TYR A CZ 1 ATOM 238 O OH . TYR A 1 29 ? -1.814 49.832 -21.716 1.00 27.92 ? 29 TYR A OH 1 ATOM 239 N N . GLN A 1 30 ? 3.068 46.912 -19.523 1.00 29.62 ? 30 GLN A N 1 ATOM 240 C CA . GLN A 1 30 ? 3.434 46.134 -20.697 1.00 29.40 ? 30 GLN A CA 1 ATOM 241 C C . GLN A 1 30 ? 4.919 45.786 -20.704 1.00 28.49 ? 30 GLN A C 1 ATOM 242 O O . GLN A 1 30 ? 5.601 45.969 -21.715 1.00 27.36 ? 30 GLN A O 1 ATOM 243 C CB . GLN A 1 30 ? 3.099 46.919 -21.966 1.00 31.92 ? 30 GLN A CB 1 ATOM 244 C CG . GLN A 1 30 ? 1.620 47.205 -22.167 1.00 36.84 ? 30 GLN A CG 1 ATOM 245 C CD . GLN A 1 30 ? 0.808 45.948 -22.424 1.00 38.70 ? 30 GLN A CD 1 ATOM 246 O OE1 . GLN A 1 30 ? 0.526 45.177 -21.511 1.00 39.39 ? 30 GLN A OE1 1 ATOM 247 N NE2 . GLN A 1 30 ? 0.438 45.733 -23.680 1.00 40.68 ? 30 GLN A NE2 1 ATOM 248 N N . GLY A 1 31 ? 5.420 45.311 -19.567 1.00 28.07 ? 31 GLY A N 1 ATOM 249 C CA . GLY A 1 31 ? 6.815 44.917 -19.472 1.00 25.39 ? 31 GLY A CA 1 ATOM 250 C C . GLY A 1 31 ? 7.847 46.025 -19.399 1.00 26.07 ? 31 GLY A C 1 ATOM 251 O O . GLY A 1 31 ? 9.044 45.748 -19.383 1.00 27.51 ? 31 GLY A O 1 ATOM 252 N N . VAL A 1 32 ? 7.405 47.277 -19.357 1.00 24.80 ? 32 VAL A N 1 ATOM 253 C CA . VAL A 1 32 ? 8.344 48.392 -19.278 1.00 23.50 ? 32 VAL A CA 1 ATOM 254 C C . VAL A 1 32 ? 8.161 49.166 -17.974 1.00 24.17 ? 32 VAL A C 1 ATOM 255 O O . VAL A 1 32 ? 7.037 49.498 -17.594 1.00 24.30 ? 32 VAL A O 1 ATOM 256 C CB . VAL A 1 32 ? 8.152 49.378 -20.460 1.00 23.29 ? 32 VAL A CB 1 ATOM 257 C CG1 . VAL A 1 32 ? 9.058 50.589 -20.283 1.00 21.48 ? 32 VAL A CG1 1 ATOM 258 C CG2 . VAL A 1 32 ? 8.457 48.681 -21.781 1.00 21.85 ? 32 VAL A CG2 1 ATOM 259 N N . TYR A 1 33 ? 9.262 49.437 -17.281 1.00 22.63 ? 33 TYR A N 1 ATOM 260 C CA . TYR A 1 33 ? 9.195 50.206 -16.042 1.00 22.70 ? 33 TYR A CA 1 ATOM 261 C C . TYR A 1 33 ? 9.243 51.677 -16.425 1.00 22.72 ? 33 TYR A C 1 ATOM 262 O O . TYR A 1 33 ? 10.143 52.107 -17.153 1.00 23.51 ? 33 TYR A O 1 ATOM 263 C CB . TYR A 1 33 ? 10.381 49.888 -15.129 1.00 22.74 ? 33 TYR A CB 1 ATOM 264 C CG . TYR A 1 33 ? 10.317 48.523 -14.487 1.00 22.84 ? 33 TYR A CG 1 ATOM 265 C CD1 . TYR A 1 33 ? 9.478 48.281 -13.399 1.00 21.30 ? 33 TYR A CD1 1 ATOM 266 C CD2 . TYR A 1 33 ? 11.084 47.466 -14.981 1.00 21.66 ? 33 TYR A CD2 1 ATOM 267 C CE1 . TYR A 1 33 ? 9.402 47.018 -12.818 1.00 21.28 ? 33 TYR A CE1 1 ATOM 268 C CE2 . TYR A 1 33 ? 11.014 46.199 -14.409 1.00 21.72 ? 33 TYR A CE2 1 ATOM 269 C CZ . TYR A 1 33 ? 10.170 45.982 -13.331 1.00 22.33 ? 33 TYR A CZ 1 ATOM 270 O OH . TYR A 1 33 ? 10.073 44.722 -12.790 1.00 25.16 ? 33 TYR A OH 1 ATOM 271 N N . HIS A 1 34 ? 8.271 52.445 -15.949 1.00 20.83 ? 34 HIS A N 1 ATOM 272 C CA . HIS A 1 34 ? 8.228 53.868 -16.243 1.00 21.00 ? 34 HIS A CA 1 ATOM 273 C C . HIS A 1 34 ? 8.606 54.677 -15.020 1.00 21.40 ? 34 HIS A C 1 ATOM 274 O O . HIS A 1 34 ? 8.184 54.367 -13.906 1.00 20.46 ? 34 HIS A O 1 ATOM 275 C CB . HIS A 1 34 ? 6.827 54.279 -16.689 1.00 20.39 ? 34 HIS A CB 1 ATOM 276 C CG . HIS A 1 34 ? 6.481 53.834 -18.072 1.00 21.52 ? 34 HIS A CG 1 ATOM 277 N ND1 . HIS A 1 34 ? 6.720 54.613 -19.184 1.00 20.58 ? 34 HIS A ND1 1 ATOM 278 C CD2 . HIS A 1 34 ? 5.963 52.670 -18.529 1.00 20.38 ? 34 HIS A CD2 1 ATOM 279 C CE1 . HIS A 1 34 ? 6.366 53.946 -20.267 1.00 21.58 ? 34 HIS A CE1 1 ATOM 280 N NE2 . HIS A 1 34 ? 5.904 52.764 -19.898 1.00 23.11 ? 34 HIS A NE2 1 ATOM 281 N N . PHE A 1 35 ? 9.417 55.707 -15.230 1.00 21.70 ? 35 PHE A N 1 ATOM 282 C CA . PHE A 1 35 ? 9.799 56.586 -14.141 1.00 21.94 ? 35 PHE A CA 1 ATOM 283 C C . PHE A 1 35 ? 9.664 58.029 -14.599 1.00 22.69 ? 35 PHE A C 1 ATOM 284 O O . PHE A 1 35 ? 10.156 58.394 -15.667 1.00 23.85 ? 35 PHE A O 1 ATOM 285 C CB . PHE A 1 35 ? 11.239 56.339 -13.682 1.00 21.43 ? 35 PHE A CB 1 ATOM 286 C CG . PHE A 1 35 ? 11.631 57.182 -12.499 1.00 20.67 ? 35 PHE A CG 1 ATOM 287 C CD1 . PHE A 1 35 ? 11.044 56.963 -11.258 1.00 19.36 ? 35 PHE A CD1 1 ATOM 288 C CD2 . PHE A 1 35 ? 12.525 58.237 -12.642 1.00 20.38 ? 35 PHE A CD2 1 ATOM 289 C CE1 . PHE A 1 35 ? 11.335 57.782 -10.174 1.00 19.54 ? 35 PHE A CE1 1 ATOM 290 C CE2 . PHE A 1 35 ? 12.824 59.066 -11.567 1.00 21.03 ? 35 PHE A CE2 1 ATOM 291 C CZ . PHE A 1 35 ? 12.225 58.838 -10.326 1.00 21.06 ? 35 PHE A CZ 1 ATOM 292 N N . PHE A 1 36 ? 8.975 58.836 -13.797 1.00 22.19 ? 36 PHE A N 1 ATOM 293 C CA . PHE A 1 36 ? 8.783 60.248 -14.092 1.00 21.94 ? 36 PHE A CA 1 ATOM 294 C C . PHE A 1 36 ? 9.321 60.981 -12.872 1.00 23.36 ? 36 PHE A C 1 ATOM 295 O O . PHE A 1 36 ? 9.508 60.373 -11.816 1.00 22.53 ? 36 PHE A O 1 ATOM 296 C CB . PHE A 1 36 ? 7.298 60.570 -14.269 1.00 22.81 ? 36 PHE A CB 1 ATOM 297 C CG . PHE A 1 36 ? 6.614 59.749 -15.325 1.00 21.90 ? 36 PHE A CG 1 ATOM 298 C CD1 . PHE A 1 36 ? 6.506 60.216 -16.632 1.00 22.51 ? 36 PHE A CD1 1 ATOM 299 C CD2 . PHE A 1 36 ? 6.074 58.503 -15.012 1.00 20.76 ? 36 PHE A CD2 1 ATOM 300 C CE1 . PHE A 1 36 ? 5.867 59.453 -17.614 1.00 23.02 ? 36 PHE A CE1 1 ATOM 301 C CE2 . PHE A 1 36 ? 5.436 57.732 -15.984 1.00 21.56 ? 36 PHE A CE2 1 ATOM 302 C CZ . PHE A 1 36 ? 5.331 58.207 -17.288 1.00 21.80 ? 36 PHE A CZ 1 ATOM 303 N N . TYR A 1 37 ? 9.556 62.283 -13.005 1.00 22.82 ? 37 TYR A N 1 ATOM 304 C CA . TYR A 1 37 ? 10.092 63.057 -11.896 1.00 23.03 ? 37 TYR A CA 1 ATOM 305 C C . TYR A 1 37 ? 9.969 64.566 -12.100 1.00 24.85 ? 37 TYR A C 1 ATOM 306 O O . TYR A 1 37 ? 9.998 65.055 -13.232 1.00 24.13 ? 37 TYR A O 1 ATOM 307 C CB . TYR A 1 37 ? 11.566 62.715 -11.704 1.00 18.79 ? 37 TYR A CB 1 ATOM 308 C CG . TYR A 1 37 ? 12.369 62.857 -12.977 1.00 21.31 ? 37 TYR A CG 1 ATOM 309 C CD1 . TYR A 1 37 ? 12.425 61.817 -13.909 1.00 21.84 ? 37 TYR A CD1 1 ATOM 310 C CD2 . TYR A 1 37 ? 13.055 64.038 -13.265 1.00 20.87 ? 37 TYR A CD2 1 ATOM 311 C CE1 . TYR A 1 37 ? 13.148 61.947 -15.096 1.00 21.91 ? 37 TYR A CE1 1 ATOM 312 C CE2 . TYR A 1 37 ? 13.781 64.182 -14.447 1.00 21.65 ? 37 TYR A CE2 1 ATOM 313 C CZ . TYR A 1 37 ? 13.826 63.130 -15.357 1.00 23.55 ? 37 TYR A CZ 1 ATOM 314 O OH . TYR A 1 37 ? 14.570 63.249 -16.508 1.00 19.87 ? 37 TYR A OH 1 ATOM 315 N N . GLN A 1 38 ? 9.838 65.296 -10.994 1.00 24.84 ? 38 GLN A N 1 ATOM 316 C CA . GLN A 1 38 ? 9.752 66.751 -11.045 1.00 25.44 ? 38 GLN A CA 1 ATOM 317 C C . GLN A 1 38 ? 11.067 67.221 -11.655 1.00 25.95 ? 38 GLN A C 1 ATOM 318 O O . GLN A 1 38 ? 12.149 66.896 -11.157 1.00 27.49 ? 38 GLN A O 1 ATOM 319 C CB . GLN A 1 38 ? 9.582 67.318 -9.634 1.00 24.51 ? 38 GLN A CB 1 ATOM 320 C CG . GLN A 1 38 ? 8.236 66.993 -9.019 1.00 23.38 ? 38 GLN A CG 1 ATOM 321 C CD . GLN A 1 38 ? 7.103 67.721 -9.717 1.00 25.20 ? 38 GLN A CD 1 ATOM 322 O OE1 . GLN A 1 38 ? 6.739 68.840 -9.342 1.00 26.05 ? 38 GLN A OE1 1 ATOM 323 N NE2 . GLN A 1 38 ? 6.553 67.098 -10.751 1.00 21.30 ? 38 GLN A NE2 1 ATOM 324 N N . TYR A 1 39 ? 10.974 67.988 -12.730 1.00 24.44 ? 39 TYR A N 1 ATOM 325 C CA . TYR A 1 39 ? 12.167 68.447 -13.417 1.00 25.79 ? 39 TYR A CA 1 ATOM 326 C C . TYR A 1 39 ? 12.081 69.908 -13.853 1.00 27.31 ? 39 TYR A C 1 ATOM 327 O O . TYR A 1 39 ? 11.016 70.392 -14.242 1.00 28.12 ? 39 TYR A O 1 ATOM 328 C CB . TYR A 1 39 ? 12.395 67.536 -14.628 1.00 24.10 ? 39 TYR A CB 1 ATOM 329 C CG . TYR A 1 39 ? 13.543 67.898 -15.543 1.00 24.46 ? 39 TYR A CG 1 ATOM 330 C CD1 . TYR A 1 39 ? 13.304 68.393 -16.827 1.00 24.99 ? 39 TYR A CD1 1 ATOM 331 C CD2 . TYR A 1 39 ? 14.867 67.693 -15.153 1.00 24.78 ? 39 TYR A CD2 1 ATOM 332 C CE1 . TYR A 1 39 ? 14.356 68.670 -17.705 1.00 23.77 ? 39 TYR A CE1 1 ATOM 333 C CE2 . TYR A 1 39 ? 15.929 67.968 -16.023 1.00 24.18 ? 39 TYR A CE2 1 ATOM 334 C CZ . TYR A 1 39 ? 15.663 68.456 -17.297 1.00 25.91 ? 39 TYR A CZ 1 ATOM 335 O OH . TYR A 1 39 ? 16.704 68.729 -18.162 1.00 27.27 ? 39 TYR A OH 1 ATOM 336 N N . ASN A 1 40 ? 13.206 70.611 -13.756 1.00 27.44 ? 40 ASN A N 1 ATOM 337 C CA . ASN A 1 40 ? 13.288 72.002 -14.188 1.00 28.80 ? 40 ASN A CA 1 ATOM 338 C C . ASN A 1 40 ? 14.137 71.973 -15.461 1.00 30.13 ? 40 ASN A C 1 ATOM 339 O O . ASN A 1 40 ? 15.341 71.726 -15.413 1.00 29.16 ? 40 ASN A O 1 ATOM 340 C CB . ASN A 1 40 ? 13.983 72.872 -13.145 1.00 28.58 ? 40 ASN A CB 1 ATOM 341 C CG . ASN A 1 40 ? 13.988 74.340 -13.533 1.00 30.85 ? 40 ASN A CG 1 ATOM 342 O OD1 . ASN A 1 40 ? 13.837 74.681 -14.714 1.00 29.01 ? 40 ASN A OD1 1 ATOM 343 N ND2 . ASN A 1 40 ? 14.170 75.220 -12.544 1.00 27.89 ? 40 ASN A ND2 1 ATOM 344 N N . PRO A 1 41 ? 13.516 72.230 -16.619 1.00 31.14 ? 41 PRO A N 1 ATOM 345 C CA . PRO A 1 41 ? 14.244 72.216 -17.890 1.00 32.38 ? 41 PRO A CA 1 ATOM 346 C C . PRO A 1 41 ? 15.179 73.399 -18.077 1.00 33.37 ? 41 PRO A C 1 ATOM 347 O O . PRO A 1 41 ? 15.996 73.404 -18.995 1.00 34.94 ? 41 PRO A O 1 ATOM 348 C CB . PRO A 1 41 ? 13.130 72.247 -18.941 1.00 32.69 ? 41 PRO A CB 1 ATOM 349 C CG . PRO A 1 41 ? 11.844 72.018 -18.166 1.00 33.15 ? 41 PRO A CG 1 ATOM 350 C CD . PRO A 1 41 ? 12.112 72.609 -16.825 1.00 30.74 ? 41 PRO A CD 1 ATOM 351 N N . TYR A 1 42 ? 15.073 74.389 -17.199 1.00 33.43 ? 42 TYR A N 1 ATOM 352 C CA . TYR A 1 42 ? 15.866 75.598 -17.355 1.00 35.29 ? 42 TYR A CA 1 ATOM 353 C C . TYR A 1 42 ? 16.988 75.893 -16.374 1.00 36.06 ? 42 TYR A C 1 ATOM 354 O O . TYR A 1 42 ? 17.764 76.818 -16.605 1.00 36.56 ? 42 TYR A O 1 ATOM 355 C CB . TYR A 1 42 ? 14.919 76.795 -17.393 1.00 35.57 ? 42 TYR A CB 1 ATOM 356 C CG . TYR A 1 42 ? 13.775 76.601 -18.353 1.00 36.92 ? 42 TYR A CG 1 ATOM 357 C CD1 . TYR A 1 42 ? 12.458 76.540 -17.897 1.00 37.23 ? 42 TYR A CD1 1 ATOM 358 C CD2 . TYR A 1 42 ? 14.011 76.443 -19.719 1.00 36.99 ? 42 TYR A CD2 1 ATOM 359 C CE1 . TYR A 1 42 ? 11.401 76.325 -18.781 1.00 38.43 ? 42 TYR A CE1 1 ATOM 360 C CE2 . TYR A 1 42 ? 12.966 76.226 -20.610 1.00 38.38 ? 42 TYR A CE2 1 ATOM 361 C CZ . TYR A 1 42 ? 11.664 76.168 -20.137 1.00 39.27 ? 42 TYR A CZ 1 ATOM 362 O OH . TYR A 1 42 ? 10.631 75.959 -21.023 1.00 41.28 ? 42 TYR A OH 1 ATOM 363 N N . ALA A 1 43 ? 17.086 75.135 -15.288 1.00 35.39 ? 43 ALA A N 1 ATOM 364 C CA . ALA A 1 43 ? 18.141 75.399 -14.319 1.00 34.06 ? 43 ALA A CA 1 ATOM 365 C C . ALA A 1 43 ? 18.408 74.231 -13.385 1.00 33.65 ? 43 ALA A C 1 ATOM 366 O O . ALA A 1 43 ? 17.666 73.249 -13.366 1.00 33.79 ? 43 ALA A O 1 ATOM 367 C CB . ALA A 1 43 ? 17.789 76.638 -13.503 1.00 33.73 ? 43 ALA A CB 1 ATOM 368 N N . ALA A 1 44 ? 19.479 74.364 -12.609 1.00 32.26 ? 44 ALA A N 1 ATOM 369 C CA . ALA A 1 44 ? 19.885 73.356 -11.642 1.00 31.89 ? 44 ALA A CA 1 ATOM 370 C C . ALA A 1 44 ? 19.359 73.737 -10.259 1.00 31.27 ? 44 ALA A C 1 ATOM 371 O O . ALA A 1 44 ? 19.969 73.413 -9.240 1.00 31.54 ? 44 ALA A O 1 ATOM 372 C CB . ALA A 1 44 ? 21.410 73.244 -11.612 1.00 31.87 ? 44 ALA A CB 1 ATOM 373 N N . THR A 1 45 ? 18.232 74.443 -10.237 1.00 29.56 ? 45 THR A N 1 ATOM 374 C CA . THR A 1 45 ? 17.591 74.861 -8.992 1.00 30.19 ? 45 THR A CA 1 ATOM 375 C C . THR A 1 45 ? 16.090 74.718 -9.205 1.00 29.85 ? 45 THR A C 1 ATOM 376 O O . THR A 1 45 ? 15.645 74.494 -10.326 1.00 29.04 ? 45 THR A O 1 ATOM 377 C CB . THR A 1 45 ? 17.873 76.345 -8.668 1.00 31.37 ? 45 THR A CB 1 ATOM 378 O OG1 . THR A 1 45 ? 17.177 77.178 -9.607 1.00 31.90 ? 45 THR A OG1 1 ATOM 379 C CG2 . THR A 1 45 ? 19.365 76.643 -8.752 1.00 32.06 ? 45 THR A CG2 1 ATOM 380 N N . PHE A 1 46 ? 15.302 74.836 -8.144 1.00 29.98 ? 46 PHE A N 1 ATOM 381 C CA . PHE A 1 46 ? 13.859 74.749 -8.315 1.00 31.82 ? 46 PHE A CA 1 ATOM 382 C C . PHE A 1 46 ? 13.480 75.989 -9.128 1.00 33.83 ? 46 PHE A C 1 ATOM 383 O O . PHE A 1 46 ? 14.192 76.996 -9.082 1.00 34.41 ? 46 PHE A O 1 ATOM 384 C CB . PHE A 1 46 ? 13.149 74.779 -6.967 1.00 31.06 ? 46 PHE A CB 1 ATOM 385 C CG . PHE A 1 46 ? 11.707 74.389 -7.042 1.00 31.34 ? 46 PHE A CG 1 ATOM 386 C CD1 . PHE A 1 46 ? 11.345 73.078 -7.338 1.00 31.78 ? 46 PHE A CD1 1 ATOM 387 C CD2 . PHE A 1 46 ? 10.706 75.328 -6.820 1.00 31.30 ? 46 PHE A CD2 1 ATOM 388 C CE1 . PHE A 1 46 ? 10.002 72.705 -7.409 1.00 32.66 ? 46 PHE A CE1 1 ATOM 389 C CE2 . PHE A 1 46 ? 9.362 74.968 -6.889 1.00 32.05 ? 46 PHE A CE2 1 ATOM 390 C CZ . PHE A 1 46 ? 9.008 73.652 -7.184 1.00 32.20 ? 46 PHE A CZ 1 ATOM 391 N N . GLY A 1 47 ? 12.377 75.925 -9.871 1.00 34.95 ? 47 GLY A N 1 ATOM 392 C CA . GLY A 1 47 ? 11.978 77.067 -10.678 1.00 34.08 ? 47 GLY A CA 1 ATOM 393 C C . GLY A 1 47 ? 10.482 77.236 -10.830 1.00 34.74 ? 47 GLY A C 1 ATOM 394 O O . GLY A 1 47 ? 9.704 76.409 -10.350 1.00 34.04 ? 47 GLY A O 1 ATOM 395 N N . ASP A 1 48 ? 10.079 78.312 -11.504 1.00 35.79 ? 48 ASP A N 1 ATOM 396 C CA . ASP A 1 48 ? 8.665 78.600 -11.717 1.00 37.14 ? 48 ASP A CA 1 ATOM 397 C C . ASP A 1 48 ? 8.013 77.593 -12.655 1.00 35.68 ? 48 ASP A C 1 ATOM 398 O O . ASP A 1 48 ? 6.802 77.386 -12.603 1.00 34.67 ? 48 ASP A O 1 ATOM 399 C CB . ASP A 1 48 ? 8.470 80.013 -12.281 1.00 41.30 ? 48 ASP A CB 1 ATOM 400 C CG . ASP A 1 48 ? 8.944 81.098 -11.325 1.00 45.45 ? 48 ASP A CG 1 ATOM 401 O OD1 . ASP A 1 48 ? 8.745 80.942 -10.100 1.00 45.70 ? 48 ASP A OD1 1 ATOM 402 O OD2 . ASP A 1 48 ? 9.505 82.111 -11.805 1.00 47.96 ? 48 ASP A OD2 1 ATOM 403 N N . VAL A 1 49 ? 8.814 76.979 -13.521 1.00 34.06 ? 49 VAL A N 1 ATOM 404 C CA . VAL A 1 49 ? 8.286 75.985 -14.445 1.00 33.87 ? 49 VAL A CA 1 ATOM 405 C C . VAL A 1 49 ? 8.865 74.600 -14.168 1.00 33.08 ? 49 VAL A C 1 ATOM 406 O O . VAL A 1 49 ? 10.024 74.321 -14.478 1.00 32.53 ? 49 VAL A O 1 ATOM 407 C CB . VAL A 1 49 ? 8.577 76.353 -15.922 1.00 35.59 ? 49 VAL A CB 1 ATOM 408 C CG1 . VAL A 1 49 ? 8.064 75.248 -16.840 1.00 33.32 ? 49 VAL A CG1 1 ATOM 409 C CG2 . VAL A 1 49 ? 7.898 77.672 -16.279 1.00 35.02 ? 49 VAL A CG2 1 ATOM 410 N N . ILE A 1 50 ? 8.046 73.744 -13.564 1.00 32.04 ? 50 ILE A N 1 ATOM 411 C CA . ILE A 1 50 ? 8.439 72.376 -13.258 1.00 29.96 ? 50 ILE A CA 1 ATOM 412 C C . ILE A 1 50 ? 7.581 71.439 -14.104 1.00 30.15 ? 50 ILE A C 1 ATOM 413 O O . ILE A 1 50 ? 6.361 71.622 -14.213 1.00 29.12 ? 50 ILE A O 1 ATOM 414 C CB . ILE A 1 50 ? 8.218 72.040 -11.767 1.00 29.66 ? 50 ILE A CB 1 ATOM 415 C CG1 . ILE A 1 50 ? 9.202 72.830 -10.901 1.00 28.89 ? 50 ILE A CG1 1 ATOM 416 C CG2 . ILE A 1 50 ? 8.378 70.538 -11.540 1.00 27.71 ? 50 ILE A CG2 1 ATOM 417 C CD1 . ILE A 1 50 ? 10.663 72.511 -11.182 1.00 28.82 ? 50 ILE A CD1 1 ATOM 418 N N . ILE A 1 51 ? 8.219 70.439 -14.703 1.00 28.34 ? 51 ILE A N 1 ATOM 419 C CA . ILE A 1 51 ? 7.509 69.481 -15.534 1.00 26.02 ? 51 ILE A CA 1 ATOM 420 C C . ILE A 1 51 ? 7.915 68.053 -15.176 1.00 26.92 ? 51 ILE A C 1 ATOM 421 O O . ILE A 1 51 ? 8.825 67.837 -14.375 1.00 27.34 ? 51 ILE A O 1 ATOM 422 C CB . ILE A 1 51 ? 7.792 69.730 -17.029 1.00 24.94 ? 51 ILE A CB 1 ATOM 423 C CG1 . ILE A 1 51 ? 9.264 69.468 -17.341 1.00 25.04 ? 51 ILE A CG1 1 ATOM 424 C CG2 . ILE A 1 51 ? 7.454 71.169 -17.386 1.00 25.76 ? 51 ILE A CG2 1 ATOM 425 C CD1 . ILE A 1 51 ? 9.629 69.719 -18.796 1.00 25.02 ? 51 ILE A CD1 1 ATOM 426 N N . TRP A 1 52 ? 7.226 67.085 -15.769 1.00 24.86 ? 52 TRP A N 1 ATOM 427 C CA . TRP A 1 52 ? 7.511 65.684 -15.529 1.00 22.46 ? 52 TRP A CA 1 ATOM 428 C C . TRP A 1 52 ? 8.546 65.135 -16.496 1.00 23.23 ? 52 TRP A C 1 ATOM 429 O O . TRP A 1 52 ? 8.273 64.993 -17.686 1.00 23.88 ? 52 TRP A O 1 ATOM 430 C CB . TRP A 1 52 ? 6.236 64.856 -15.674 1.00 21.43 ? 52 TRP A CB 1 ATOM 431 C CG . TRP A 1 52 ? 5.315 64.915 -14.500 1.00 19.41 ? 52 TRP A CG 1 ATOM 432 C CD1 . TRP A 1 52 ? 5.021 66.007 -13.737 1.00 18.47 ? 52 TRP A CD1 1 ATOM 433 C CD2 . TRP A 1 52 ? 4.544 63.830 -13.969 1.00 18.37 ? 52 TRP A CD2 1 ATOM 434 N NE1 . TRP A 1 52 ? 4.113 65.669 -12.756 1.00 19.74 ? 52 TRP A NE1 1 ATOM 435 C CE2 . TRP A 1 52 ? 3.805 64.337 -12.877 1.00 18.12 ? 52 TRP A CE2 1 ATOM 436 C CE3 . TRP A 1 52 ? 4.407 62.475 -14.310 1.00 19.71 ? 52 TRP A CE3 1 ATOM 437 C CZ2 . TRP A 1 52 ? 2.941 63.537 -12.119 1.00 18.49 ? 52 TRP A CZ2 1 ATOM 438 C CZ3 . TRP A 1 52 ? 3.545 61.675 -13.556 1.00 20.98 ? 52 TRP A CZ3 1 ATOM 439 C CH2 . TRP A 1 52 ? 2.824 62.212 -12.472 1.00 21.06 ? 52 TRP A CH2 1 ATOM 440 N N . GLY A 1 53 ? 9.738 64.840 -15.990 1.00 23.01 ? 53 GLY A N 1 ATOM 441 C CA . GLY A 1 53 ? 10.755 64.239 -16.832 1.00 21.35 ? 53 GLY A CA 1 ATOM 442 C C . GLY A 1 53 ? 10.261 62.810 -17.006 1.00 22.30 ? 53 GLY A C 1 ATOM 443 O O . GLY A 1 53 ? 9.386 62.372 -16.252 1.00 20.84 ? 53 GLY A O 1 ATOM 444 N N . HIS A 1 54 ? 10.814 62.070 -17.961 1.00 22.22 ? 54 HIS A N 1 ATOM 445 C CA . HIS A 1 54 ? 10.350 60.711 -18.212 1.00 20.71 ? 54 HIS A CA 1 ATOM 446 C C . HIS A 1 54 ? 11.483 59.811 -18.683 1.00 21.41 ? 54 HIS A C 1 ATOM 447 O O . HIS A 1 54 ? 12.300 60.215 -19.507 1.00 21.59 ? 54 HIS A O 1 ATOM 448 C CB . HIS A 1 54 ? 9.236 60.778 -19.268 1.00 20.46 ? 54 HIS A CB 1 ATOM 449 C CG . HIS A 1 54 ? 8.611 59.457 -19.614 1.00 22.34 ? 54 HIS A CG 1 ATOM 450 N ND1 . HIS A 1 54 ? 8.581 58.385 -18.746 1.00 24.90 ? 54 HIS A ND1 1 ATOM 451 C CD2 . HIS A 1 54 ? 7.907 59.072 -20.707 1.00 19.71 ? 54 HIS A CD2 1 ATOM 452 C CE1 . HIS A 1 54 ? 7.884 57.399 -19.288 1.00 22.14 ? 54 HIS A CE1 1 ATOM 453 N NE2 . HIS A 1 54 ? 7.463 57.792 -20.476 1.00 22.98 ? 54 HIS A NE2 1 ATOM 454 N N . ALA A 1 55 ? 11.540 58.596 -18.140 1.00 20.86 ? 55 ALA A N 1 ATOM 455 C CA . ALA A 1 55 ? 12.552 57.622 -18.531 1.00 20.50 ? 55 ALA A CA 1 ATOM 456 C C . ALA A 1 55 ? 11.935 56.232 -18.432 1.00 22.00 ? 55 ALA A C 1 ATOM 457 O O . ALA A 1 55 ? 11.005 56.012 -17.654 1.00 20.91 ? 55 ALA A O 1 ATOM 458 C CB . ALA A 1 55 ? 13.768 57.720 -17.628 1.00 19.82 ? 55 ALA A CB 1 ATOM 459 N N . VAL A 1 56 ? 12.439 55.297 -19.231 1.00 20.90 ? 56 VAL A N 1 ATOM 460 C CA . VAL A 1 56 ? 11.920 53.943 -19.201 1.00 21.91 ? 56 VAL A CA 1 ATOM 461 C C . VAL A 1 56 ? 13.044 52.944 -19.005 1.00 23.72 ? 56 VAL A C 1 ATOM 462 O O . VAL A 1 56 ? 14.208 53.228 -19.314 1.00 24.36 ? 56 VAL A O 1 ATOM 463 C CB . VAL A 1 56 ? 11.158 53.592 -20.497 1.00 21.94 ? 56 VAL A CB 1 ATOM 464 C CG1 . VAL A 1 56 ? 9.860 54.391 -20.564 1.00 21.49 ? 56 VAL A CG1 1 ATOM 465 C CG2 . VAL A 1 56 ? 12.032 53.878 -21.716 1.00 18.51 ? 56 VAL A CG2 1 ATOM 466 N N . SER A 1 57 ? 12.685 51.772 -18.497 1.00 22.59 ? 57 SER A N 1 ATOM 467 C CA . SER A 1 57 ? 13.655 50.720 -18.245 1.00 23.37 ? 57 SER A CA 1 ATOM 468 C C . SER A 1 57 ? 13.009 49.335 -18.225 1.00 24.17 ? 57 SER A C 1 ATOM 469 O O . SER A 1 57 ? 11.817 49.198 -17.953 1.00 24.53 ? 57 SER A O 1 ATOM 470 C CB . SER A 1 57 ? 14.339 50.966 -16.904 1.00 22.09 ? 57 SER A CB 1 ATOM 471 O OG . SER A 1 57 ? 15.137 49.856 -16.547 1.00 23.94 ? 57 SER A OG 1 ATOM 472 N N . TYR A 1 58 ? 13.803 48.310 -18.513 1.00 24.73 ? 58 TYR A N 1 ATOM 473 C CA . TYR A 1 58 ? 13.311 46.941 -18.494 1.00 26.25 ? 58 TYR A CA 1 ATOM 474 C C . TYR A 1 58 ? 13.755 46.258 -17.205 1.00 26.26 ? 58 TYR A C 1 ATOM 475 O O . TYR A 1 58 ? 13.258 45.188 -16.866 1.00 28.32 ? 58 TYR A O 1 ATOM 476 C CB . TYR A 1 58 ? 13.866 46.157 -19.685 1.00 26.80 ? 58 TYR A CB 1 ATOM 477 C CG . TYR A 1 58 ? 13.429 46.691 -21.025 1.00 29.20 ? 58 TYR A CG 1 ATOM 478 C CD1 . TYR A 1 58 ? 12.110 46.548 -21.462 1.00 30.27 ? 58 TYR A CD1 1 ATOM 479 C CD2 . TYR A 1 58 ? 14.329 47.359 -21.853 1.00 30.11 ? 58 TYR A CD2 1 ATOM 480 C CE1 . TYR A 1 58 ? 11.697 47.063 -22.696 1.00 31.75 ? 58 TYR A CE1 1 ATOM 481 C CE2 . TYR A 1 58 ? 13.928 47.876 -23.084 1.00 32.78 ? 58 TYR A CE2 1 ATOM 482 C CZ . TYR A 1 58 ? 12.614 47.725 -23.498 1.00 33.12 ? 58 TYR A CZ 1 ATOM 483 O OH . TYR A 1 58 ? 12.228 48.244 -24.711 1.00 38.77 ? 58 TYR A OH 1 ATOM 484 N N . ASP A 1 59 ? 14.676 46.884 -16.477 1.00 25.71 ? 59 ASP A N 1 ATOM 485 C CA . ASP A 1 59 ? 15.203 46.280 -15.257 1.00 26.18 ? 59 ASP A CA 1 ATOM 486 C C . ASP A 1 59 ? 15.373 47.202 -14.043 1.00 25.73 ? 59 ASP A C 1 ATOM 487 O O . ASP A 1 59 ? 15.932 46.778 -13.028 1.00 26.16 ? 59 ASP A O 1 ATOM 488 C CB . ASP A 1 59 ? 16.557 45.641 -15.569 1.00 25.42 ? 59 ASP A CB 1 ATOM 489 C CG . ASP A 1 59 ? 17.519 46.620 -16.225 1.00 28.65 ? 59 ASP A CG 1 ATOM 490 O OD1 . ASP A 1 59 ? 17.393 47.838 -15.964 1.00 28.62 ? 59 ASP A OD1 1 ATOM 491 O OD2 . ASP A 1 59 ? 18.405 46.181 -16.989 1.00 29.14 ? 59 ASP A OD2 1 ATOM 492 N N . LEU A 1 60 ? 14.905 48.445 -14.140 1.00 24.67 ? 60 LEU A N 1 ATOM 493 C CA . LEU A 1 60 ? 15.025 49.426 -13.048 1.00 24.48 ? 60 LEU A CA 1 ATOM 494 C C . LEU A 1 60 ? 16.467 49.895 -12.803 1.00 24.83 ? 60 LEU A C 1 ATOM 495 O O . LEU A 1 60 ? 16.721 50.725 -11.925 1.00 25.67 ? 60 LEU A O 1 ATOM 496 C CB . LEU A 1 60 ? 14.446 48.864 -11.738 1.00 21.90 ? 60 LEU A CB 1 ATOM 497 C CG . LEU A 1 60 ? 12.921 48.702 -11.673 1.00 22.20 ? 60 LEU A CG 1 ATOM 498 C CD1 . LEU A 1 60 ? 12.526 48.021 -10.369 1.00 17.64 ? 60 LEU A CD1 1 ATOM 499 C CD2 . LEU A 1 60 ? 12.252 50.074 -11.790 1.00 20.93 ? 60 LEU A CD2 1 ATOM 500 N N . VAL A 1 61 ? 17.406 49.373 -13.585 1.00 24.06 ? 61 VAL A N 1 ATOM 501 C CA . VAL A 1 61 ? 18.808 49.748 -13.438 1.00 23.51 ? 61 VAL A CA 1 ATOM 502 C C . VAL A 1 61 ? 19.298 50.577 -14.626 1.00 24.54 ? 61 VAL A C 1 ATOM 503 O O . VAL A 1 61 ? 19.868 51.653 -14.453 1.00 25.13 ? 61 VAL A O 1 ATOM 504 C CB . VAL A 1 61 ? 19.706 48.492 -13.304 1.00 22.92 ? 61 VAL A CB 1 ATOM 505 C CG1 . VAL A 1 61 ? 21.170 48.907 -13.217 1.00 22.80 ? 61 VAL A CG1 1 ATOM 506 C CG2 . VAL A 1 61 ? 19.305 47.694 -12.069 1.00 20.10 ? 61 VAL A CG2 1 ATOM 507 N N . ASN A 1 62 ? 19.079 50.067 -15.832 1.00 24.37 ? 62 ASN A N 1 ATOM 508 C CA . ASN A 1 62 ? 19.507 50.758 -17.044 1.00 25.14 ? 62 ASN A CA 1 ATOM 509 C C . ASN A 1 62 ? 18.334 51.533 -17.608 1.00 25.16 ? 62 ASN A C 1 ATOM 510 O O . ASN A 1 62 ? 17.243 50.986 -17.774 1.00 26.22 ? 62 ASN A O 1 ATOM 511 C CB . ASN A 1 62 ? 20.031 49.735 -18.035 1.00 23.43 ? 62 ASN A CB 1 ATOM 512 C CG . ASN A 1 62 ? 21.117 48.883 -17.430 1.00 25.73 ? 62 ASN A CG 1 ATOM 513 O OD1 . ASN A 1 62 ? 22.218 49.369 -17.164 1.00 24.22 ? 62 ASN A OD1 1 ATOM 514 N ND2 . ASN A 1 62 ? 20.806 47.613 -17.174 1.00 24.77 ? 62 ASN A ND2 1 ATOM 515 N N . TRP A 1 63 ? 18.561 52.807 -17.905 1.00 24.25 ? 63 TRP A N 1 ATOM 516 C CA . TRP A 1 63 ? 17.488 53.659 -18.384 1.00 23.99 ? 63 TRP A CA 1 ATOM 517 C C . TRP A 1 63 ? 17.665 54.347 -19.721 1.00 25.61 ? 63 TRP A C 1 ATOM 518 O O . TRP A 1 63 ? 18.782 54.546 -20.208 1.00 26.00 ? 63 TRP A O 1 ATOM 519 C CB . TRP A 1 63 ? 17.195 54.740 -17.340 1.00 22.84 ? 63 TRP A CB 1 ATOM 520 C CG . TRP A 1 63 ? 16.794 54.196 -16.011 1.00 23.42 ? 63 TRP A CG 1 ATOM 521 C CD1 . TRP A 1 63 ? 17.620 53.746 -15.014 1.00 21.98 ? 63 TRP A CD1 1 ATOM 522 C CD2 . TRP A 1 63 ? 15.454 53.971 -15.556 1.00 22.54 ? 63 TRP A CD2 1 ATOM 523 N NE1 . TRP A 1 63 ? 16.870 53.249 -13.967 1.00 23.25 ? 63 TRP A NE1 1 ATOM 524 C CE2 . TRP A 1 63 ? 15.540 53.375 -14.276 1.00 22.21 ? 63 TRP A CE2 1 ATOM 525 C CE3 . TRP A 1 63 ? 14.188 54.211 -16.110 1.00 20.60 ? 63 TRP A CE3 1 ATOM 526 C CZ2 . TRP A 1 63 ? 14.406 53.016 -13.542 1.00 22.99 ? 63 TRP A CZ2 1 ATOM 527 C CZ3 . TRP A 1 63 ? 13.062 53.853 -15.379 1.00 21.16 ? 63 TRP A CZ3 1 ATOM 528 C CH2 . TRP A 1 63 ? 13.179 53.262 -14.109 1.00 21.06 ? 63 TRP A CH2 1 ATOM 529 N N . ILE A 1 64 ? 16.524 54.723 -20.292 1.00 25.50 ? 64 ILE A N 1 ATOM 530 C CA . ILE A 1 64 ? 16.473 55.449 -21.545 1.00 23.86 ? 64 ILE A CA 1 ATOM 531 C C . ILE A 1 64 ? 15.740 56.750 -21.226 1.00 24.35 ? 64 ILE A C 1 ATOM 532 O O . ILE A 1 64 ? 14.579 56.725 -20.808 1.00 24.95 ? 64 ILE A O 1 ATOM 533 C CB . ILE A 1 64 ? 15.683 54.677 -22.611 1.00 24.57 ? 64 ILE A CB 1 ATOM 534 C CG1 . ILE A 1 64 ? 16.409 53.374 -22.957 1.00 24.61 ? 64 ILE A CG1 1 ATOM 535 C CG2 . ILE A 1 64 ? 15.512 55.535 -23.853 1.00 21.55 ? 64 ILE A CG2 1 ATOM 536 C CD1 . ILE A 1 64 ? 15.672 52.516 -23.973 1.00 22.66 ? 64 ILE A CD1 1 ATOM 537 N N . HIS A 1 65 ? 16.423 57.879 -21.391 1.00 24.02 ? 65 HIS A N 1 ATOM 538 C CA . HIS A 1 65 ? 15.817 59.183 -21.128 1.00 24.91 ? 65 HIS A CA 1 ATOM 539 C C . HIS A 1 65 ? 14.940 59.578 -22.313 1.00 26.17 ? 65 HIS A C 1 ATOM 540 O O . HIS A 1 65 ? 15.384 59.534 -23.458 1.00 26.81 ? 65 HIS A O 1 ATOM 541 C CB . HIS A 1 65 ? 16.897 60.243 -20.922 1.00 24.05 ? 65 HIS A CB 1 ATOM 542 C CG . HIS A 1 65 ? 17.726 60.035 -19.692 1.00 25.17 ? 65 HIS A CG 1 ATOM 543 N ND1 . HIS A 1 65 ? 17.190 60.046 -18.422 1.00 23.63 ? 65 HIS A ND1 1 ATOM 544 C CD2 . HIS A 1 65 ? 19.054 59.814 -19.538 1.00 24.41 ? 65 HIS A CD2 1 ATOM 545 C CE1 . HIS A 1 65 ? 18.152 59.840 -17.539 1.00 25.19 ? 65 HIS A CE1 1 ATOM 546 N NE2 . HIS A 1 65 ? 19.293 59.696 -18.190 1.00 24.96 ? 65 HIS A NE2 1 ATOM 547 N N . LEU A 1 66 ? 13.698 59.958 -22.036 1.00 25.12 ? 66 LEU A N 1 ATOM 548 C CA . LEU A 1 66 ? 12.766 60.357 -23.086 1.00 25.47 ? 66 LEU A CA 1 ATOM 549 C C . LEU A 1 66 ? 12.459 61.840 -22.934 1.00 26.95 ? 66 LEU A C 1 ATOM 550 O O . LEU A 1 66 ? 13.019 62.504 -22.066 1.00 27.53 ? 66 LEU A O 1 ATOM 551 C CB . LEU A 1 66 ? 11.464 59.559 -22.959 1.00 22.67 ? 66 LEU A CB 1 ATOM 552 C CG . LEU A 1 66 ? 11.596 58.030 -22.929 1.00 23.53 ? 66 LEU A CG 1 ATOM 553 C CD1 . LEU A 1 66 ? 10.244 57.386 -22.649 1.00 21.72 ? 66 LEU A CD1 1 ATOM 554 C CD2 . LEU A 1 66 ? 12.143 57.549 -24.256 1.00 22.91 ? 66 LEU A CD2 1 ATOM 555 N N . ASP A 1 67 ? 11.584 62.364 -23.785 1.00 27.91 ? 67 ASP A N 1 ATOM 556 C CA . ASP A 1 67 ? 11.193 63.762 -23.675 1.00 29.63 ? 67 ASP A CA 1 ATOM 557 C C . ASP A 1 67 ? 10.193 63.844 -22.534 1.00 29.02 ? 67 ASP A C 1 ATOM 558 O O . ASP A 1 67 ? 9.516 62.863 -22.229 1.00 27.75 ? 67 ASP A O 1 ATOM 559 C CB . ASP A 1 67 ? 10.533 64.251 -24.963 1.00 31.48 ? 67 ASP A CB 1 ATOM 560 C CG . ASP A 1 67 ? 11.526 64.437 -26.089 1.00 34.77 ? 67 ASP A CG 1 ATOM 561 O OD1 . ASP A 1 67 ? 12.564 65.105 -25.862 1.00 34.97 ? 67 ASP A OD1 1 ATOM 562 O OD2 . ASP A 1 67 ? 11.265 63.921 -27.197 1.00 38.15 ? 67 ASP A OD2 1 ATOM 563 N N . PRO A 1 68 ? 10.099 65.006 -21.870 1.00 29.49 ? 68 PRO A N 1 ATOM 564 C CA . PRO A 1 68 ? 9.135 65.096 -20.770 1.00 29.02 ? 68 PRO A CA 1 ATOM 565 C C . PRO A 1 68 ? 7.736 64.664 -21.200 1.00 29.00 ? 68 PRO A C 1 ATOM 566 O O . PRO A 1 68 ? 7.312 64.919 -22.326 1.00 28.81 ? 68 PRO A O 1 ATOM 567 C CB . PRO A 1 68 ? 9.227 66.562 -20.322 1.00 28.88 ? 68 PRO A CB 1 ATOM 568 C CG . PRO A 1 68 ? 10.032 67.252 -21.394 1.00 32.46 ? 68 PRO A CG 1 ATOM 569 C CD . PRO A 1 68 ? 10.952 66.202 -21.930 1.00 30.43 ? 68 PRO A CD 1 ATOM 570 N N . ALA A 1 69 ? 7.038 63.991 -20.292 1.00 28.13 ? 69 ALA A N 1 ATOM 571 C CA . ALA A 1 69 ? 5.711 63.463 -20.558 1.00 28.09 ? 69 ALA A CA 1 ATOM 572 C C . ALA A 1 69 ? 4.574 64.424 -20.248 1.00 28.71 ? 69 ALA A C 1 ATOM 573 O O . ALA A 1 69 ? 3.609 64.524 -21.005 1.00 27.17 ? 69 ALA A O 1 ATOM 574 C CB . ALA A 1 69 ? 5.517 62.171 -19.770 1.00 26.53 ? 69 ALA A CB 1 ATOM 575 N N . ILE A 1 70 ? 4.690 65.125 -19.129 1.00 29.60 ? 70 ILE A N 1 ATOM 576 C CA . ILE A 1 70 ? 3.653 66.050 -18.712 1.00 29.94 ? 70 ILE A CA 1 ATOM 577 C C . ILE A 1 70 ? 4.210 67.444 -18.454 1.00 30.63 ? 70 ILE A C 1 ATOM 578 O O . ILE A 1 70 ? 5.095 67.627 -17.621 1.00 30.98 ? 70 ILE A O 1 ATOM 579 C CB . ILE A 1 70 ? 2.953 65.503 -17.454 1.00 29.98 ? 70 ILE A CB 1 ATOM 580 C CG1 . ILE A 1 70 ? 2.353 64.130 -17.780 1.00 29.00 ? 70 ILE A CG1 1 ATOM 581 C CG2 . ILE A 1 70 ? 1.882 66.475 -16.976 1.00 29.97 ? 70 ILE A CG2 1 ATOM 582 C CD1 . ILE A 1 70 ? 1.592 63.491 -16.648 1.00 31.65 ? 70 ILE A CD1 1 ATOM 583 N N . TYR A 1 71 ? 3.690 68.418 -19.194 1.00 30.36 ? 71 TYR A N 1 ATOM 584 C CA . TYR A 1 71 ? 4.111 69.813 -19.081 1.00 32.21 ? 71 TYR A CA 1 ATOM 585 C C . TYR A 1 71 ? 2.885 70.698 -19.315 1.00 33.28 ? 71 TYR A C 1 ATOM 586 O O . TYR A 1 71 ? 1.960 70.301 -20.023 1.00 32.99 ? 71 TYR A O 1 ATOM 587 C CB . TYR A 1 71 ? 5.196 70.107 -20.117 1.00 31.61 ? 71 TYR A CB 1 ATOM 588 C CG . TYR A 1 71 ? 4.884 69.538 -21.482 1.00 32.79 ? 71 TYR A CG 1 ATOM 589 C CD1 . TYR A 1 71 ? 4.119 70.254 -22.403 1.00 32.02 ? 71 TYR A CD1 1 ATOM 590 C CD2 . TYR A 1 71 ? 5.312 68.255 -21.834 1.00 32.29 ? 71 TYR A CD2 1 ATOM 591 C CE1 . TYR A 1 71 ? 3.784 69.702 -23.645 1.00 33.03 ? 71 TYR A CE1 1 ATOM 592 C CE2 . TYR A 1 71 ? 4.984 67.695 -23.062 1.00 32.85 ? 71 TYR A CE2 1 ATOM 593 C CZ . TYR A 1 71 ? 4.219 68.422 -23.965 1.00 34.18 ? 71 TYR A CZ 1 ATOM 594 O OH . TYR A 1 71 ? 3.884 67.858 -25.175 1.00 33.94 ? 71 TYR A OH 1 ATOM 595 N N . PRO A 1 72 ? 2.862 71.906 -18.722 1.00 33.64 ? 72 PRO A N 1 ATOM 596 C CA . PRO A 1 72 ? 1.730 72.828 -18.874 1.00 34.12 ? 72 PRO A CA 1 ATOM 597 C C . PRO A 1 72 ? 1.206 73.026 -20.296 1.00 33.64 ? 72 PRO A C 1 ATOM 598 O O . PRO A 1 72 ? 1.945 73.449 -21.189 1.00 33.44 ? 72 PRO A O 1 ATOM 599 C CB . PRO A 1 72 ? 2.246 74.130 -18.244 1.00 34.87 ? 72 PRO A CB 1 ATOM 600 C CG . PRO A 1 72 ? 3.736 73.987 -18.275 1.00 35.57 ? 72 PRO A CG 1 ATOM 601 C CD . PRO A 1 72 ? 3.948 72.540 -17.958 1.00 33.70 ? 72 PRO A CD 1 ATOM 602 N N . THR A 1 73 ? -0.071 72.700 -20.496 1.00 31.96 ? 73 THR A N 1 ATOM 603 C CA . THR A 1 73 ? -0.720 72.849 -21.797 1.00 32.45 ? 73 THR A CA 1 ATOM 604 C C . THR A 1 73 ? -2.156 73.340 -21.637 1.00 33.29 ? 73 THR A C 1 ATOM 605 O O . THR A 1 73 ? -2.826 73.647 -22.620 1.00 33.97 ? 73 THR A O 1 ATOM 606 C CB . THR A 1 73 ? -0.761 71.523 -22.593 1.00 31.38 ? 73 THR A CB 1 ATOM 607 O OG1 . THR A 1 73 ? -1.546 70.559 -21.881 1.00 31.71 ? 73 THR A OG1 1 ATOM 608 C CG2 . THR A 1 73 ? 0.644 70.980 -22.809 1.00 32.37 ? 73 THR A CG2 1 ATOM 609 N N . GLN A 1 74 ? -2.645 73.389 -20.404 1.00 32.64 ? 74 GLN A N 1 ATOM 610 C CA . GLN A 1 74 ? -3.990 73.880 -20.185 1.00 33.68 ? 74 GLN A CA 1 ATOM 611 C C . GLN A 1 74 ? -4.064 74.793 -18.972 1.00 34.72 ? 74 GLN A C 1 ATOM 612 O O . GLN A 1 74 ? -3.113 74.896 -18.198 1.00 34.74 ? 74 GLN A O 1 ATOM 613 C CB . GLN A 1 74 ? -4.994 72.719 -20.082 1.00 33.75 ? 74 GLN A CB 1 ATOM 614 C CG . GLN A 1 74 ? -4.679 71.645 -19.079 1.00 37.59 ? 74 GLN A CG 1 ATOM 615 C CD . GLN A 1 74 ? -5.640 70.458 -19.163 1.00 37.55 ? 74 GLN A CD 1 ATOM 616 O OE1 . GLN A 1 74 ? -5.622 69.575 -18.306 1.00 39.79 ? 74 GLN A OE1 1 ATOM 617 N NE2 . GLN A 1 74 ? -6.476 70.433 -20.194 1.00 35.61 ? 74 GLN A NE2 1 ATOM 618 N N . GLU A 1 75 ? -5.183 75.491 -18.831 1.00 34.53 ? 75 GLU A N 1 ATOM 619 C CA . GLU A 1 75 ? -5.358 76.406 -17.718 1.00 34.02 ? 75 GLU A CA 1 ATOM 620 C C . GLU A 1 75 ? -5.154 75.684 -16.396 1.00 32.57 ? 75 GLU A C 1 ATOM 621 O O . GLU A 1 75 ? -4.557 76.236 -15.480 1.00 32.50 ? 75 GLU A O 1 ATOM 622 C CB . GLU A 1 75 ? -6.757 77.033 -17.763 1.00 34.47 ? 75 GLU A CB 1 ATOM 623 C CG . GLU A 1 75 ? -7.015 78.128 -16.720 1.00 37.24 ? 75 GLU A CG 1 ATOM 624 C CD . GLU A 1 75 ? -7.245 77.586 -15.312 1.00 39.44 ? 75 GLU A CD 1 ATOM 625 O OE1 . GLU A 1 75 ? -8.001 76.597 -15.163 1.00 40.80 ? 75 GLU A OE1 1 ATOM 626 O OE2 . GLU A 1 75 ? -6.681 78.157 -14.354 1.00 38.76 ? 75 GLU A OE2 1 ATOM 627 N N . ALA A 1 76 ? -5.640 74.449 -16.307 1.00 32.35 ? 76 ALA A N 1 ATOM 628 C CA . ALA A 1 76 ? -5.529 73.662 -15.080 1.00 31.09 ? 76 ALA A CA 1 ATOM 629 C C . ALA A 1 76 ? -4.097 73.322 -14.648 1.00 30.92 ? 76 ALA A C 1 ATOM 630 O O . ALA A 1 76 ? -3.895 72.787 -13.558 1.00 30.51 ? 76 ALA A O 1 ATOM 631 C CB . ALA A 1 76 ? -6.356 72.388 -15.200 1.00 30.44 ? 76 ALA A CB 1 ATOM 632 N N . ASP A 1 77 ? -3.106 73.616 -15.486 1.00 30.03 ? 77 ASP A N 1 ATOM 633 C CA . ASP A 1 77 ? -1.721 73.349 -15.105 1.00 30.52 ? 77 ASP A CA 1 ATOM 634 C C . ASP A 1 77 ? -0.752 74.306 -15.784 1.00 30.69 ? 77 ASP A C 1 ATOM 635 O O . ASP A 1 77 ? 0.430 74.011 -15.920 1.00 30.32 ? 77 ASP A O 1 ATOM 636 C CB . ASP A 1 77 ? -1.331 71.891 -15.416 1.00 30.80 ? 77 ASP A CB 1 ATOM 637 C CG . ASP A 1 77 ? -1.284 71.583 -16.912 1.00 32.06 ? 77 ASP A CG 1 ATOM 638 O OD1 . ASP A 1 77 ? -1.406 72.509 -17.741 1.00 31.11 ? 77 ASP A OD1 1 ATOM 639 O OD2 . ASP A 1 77 ? -1.113 70.393 -17.258 1.00 31.85 ? 77 ASP A OD2 1 ATOM 640 N N . SER A 1 78 ? -1.257 75.471 -16.175 1.00 31.77 ? 78 SER A N 1 ATOM 641 C CA . SER A 1 78 ? -0.461 76.476 -16.880 1.00 33.36 ? 78 SER A CA 1 ATOM 642 C C . SER A 1 78 ? 0.825 76.952 -16.218 1.00 33.12 ? 78 SER A C 1 ATOM 643 O O . SER A 1 78 ? 1.784 77.301 -16.910 1.00 33.73 ? 78 SER A O 1 ATOM 644 C CB . SER A 1 78 ? -1.335 77.692 -17.212 1.00 33.38 ? 78 SER A CB 1 ATOM 645 O OG . SER A 1 78 ? -1.998 78.172 -16.058 1.00 35.69 ? 78 SER A OG 1 ATOM 646 N N . LYS A 1 79 ? 0.860 76.974 -14.891 1.00 33.51 ? 79 LYS A N 1 ATOM 647 C CA . LYS A 1 79 ? 2.055 77.434 -14.194 1.00 34.47 ? 79 LYS A CA 1 ATOM 648 C C . LYS A 1 79 ? 3.078 76.354 -13.839 1.00 34.31 ? 79 LYS A C 1 ATOM 649 O O . LYS A 1 79 ? 4.234 76.670 -13.561 1.00 34.37 ? 79 LYS A O 1 ATOM 650 C CB . LYS A 1 79 ? 1.652 78.207 -12.938 1.00 36.59 ? 79 LYS A CB 1 ATOM 651 C CG . LYS A 1 79 ? 1.127 79.599 -13.248 1.00 38.55 ? 79 LYS A CG 1 ATOM 652 C CD . LYS A 1 79 ? 0.655 80.316 -12.000 1.00 42.22 ? 79 LYS A CD 1 ATOM 653 C CE . LYS A 1 79 ? 0.381 81.784 -12.294 1.00 44.74 ? 79 LYS A CE 1 ATOM 654 N NZ . LYS A 1 79 ? 1.628 82.499 -12.713 1.00 47.19 ? 79 LYS A NZ 1 ATOM 655 N N . SER A 1 80 ? 2.659 75.090 -13.856 1.00 32.95 ? 80 SER A N 1 ATOM 656 C CA . SER A 1 80 ? 3.546 73.969 -13.537 1.00 31.12 ? 80 SER A CA 1 ATOM 657 C C . SER A 1 80 ? 2.788 72.661 -13.379 1.00 29.64 ? 80 SER A C 1 ATOM 658 O O . SER A 1 80 ? 1.588 72.648 -13.101 1.00 29.07 ? 80 SER A O 1 ATOM 659 C CB . SER A 1 80 ? 4.324 74.226 -12.234 1.00 31.96 ? 80 SER A CB 1 ATOM 660 O OG . SER A 1 80 ? 5.604 74.791 -12.480 1.00 31.11 ? 80 SER A OG 1 ATOM 661 N N . CYS A 1 81 ? 3.505 71.559 -13.560 1.00 28.20 ? 81 CYS A N 1 ATOM 662 C CA . CYS A 1 81 ? 2.929 70.232 -13.395 1.00 26.26 ? 81 CYS A CA 1 ATOM 663 C C . CYS A 1 81 ? 3.673 69.602 -12.225 1.00 26.12 ? 81 CYS A C 1 ATOM 664 O O . CYS A 1 81 ? 4.792 69.102 -12.372 1.00 24.64 ? 81 CYS A O 1 ATOM 665 C CB . CYS A 1 81 ? 3.118 69.400 -14.660 1.00 26.31 ? 81 CYS A CB 1 ATOM 666 S SG . CYS A 1 81 ? 2.211 70.041 -16.082 1.00 28.61 ? 81 CYS A SG 1 ATOM 667 N N . TRP A 1 82 ? 3.056 69.645 -11.053 1.00 24.84 ? 82 TRP A N 1 ATOM 668 C CA . TRP A 1 82 ? 3.697 69.094 -9.879 1.00 25.38 ? 82 TRP A CA 1 ATOM 669 C C . TRP A 1 82 ? 3.418 67.611 -9.672 1.00 25.16 ? 82 TRP A C 1 ATOM 670 O O . TRP A 1 82 ? 2.798 66.966 -10.512 1.00 26.82 ? 82 TRP A O 1 ATOM 671 C CB . TRP A 1 82 ? 3.346 69.946 -8.652 1.00 24.04 ? 82 TRP A CB 1 ATOM 672 C CG . TRP A 1 82 ? 3.989 71.326 -8.739 1.00 25.45 ? 82 TRP A CG 1 ATOM 673 C CD1 . TRP A 1 82 ? 5.215 71.627 -9.278 1.00 25.20 ? 82 TRP A CD1 1 ATOM 674 C CD2 . TRP A 1 82 ? 3.456 72.567 -8.250 1.00 26.19 ? 82 TRP A CD2 1 ATOM 675 N NE1 . TRP A 1 82 ? 5.474 72.973 -9.154 1.00 24.97 ? 82 TRP A NE1 1 ATOM 676 C CE2 . TRP A 1 82 ? 4.413 73.573 -8.526 1.00 26.78 ? 82 TRP A CE2 1 ATOM 677 C CE3 . TRP A 1 82 ? 2.263 72.928 -7.603 1.00 26.78 ? 82 TRP A CE3 1 ATOM 678 C CZ2 . TRP A 1 82 ? 4.214 74.917 -8.176 1.00 28.38 ? 82 TRP A CZ2 1 ATOM 679 C CZ3 . TRP A 1 82 ? 2.065 74.265 -7.254 1.00 26.48 ? 82 TRP A CZ3 1 ATOM 680 C CH2 . TRP A 1 82 ? 3.037 75.242 -7.541 1.00 27.02 ? 82 TRP A CH2 1 ATOM 681 N N . SER A 1 83 ? 3.897 67.074 -8.560 1.00 25.64 ? 83 SER A N 1 ATOM 682 C CA . SER A 1 83 ? 3.787 65.651 -8.266 1.00 24.75 ? 83 SER A CA 1 ATOM 683 C C . SER A 1 83 ? 2.453 64.934 -8.398 1.00 25.05 ? 83 SER A C 1 ATOM 684 O O . SER A 1 83 ? 1.384 65.520 -8.227 1.00 25.76 ? 83 SER A O 1 ATOM 685 C CB . SER A 1 83 ? 4.390 65.387 -6.892 1.00 22.25 ? 83 SER A CB 1 ATOM 686 O OG . SER A 1 83 ? 5.756 65.765 -6.912 1.00 20.77 ? 83 SER A OG 1 ATOM 687 N N . GLY A 1 84 ? 2.547 63.639 -8.702 1.00 24.64 ? 84 GLY A N 1 ATOM 688 C CA . GLY A 1 84 ? 1.374 62.804 -8.874 1.00 24.56 ? 84 GLY A CA 1 ATOM 689 C C . GLY A 1 84 ? 1.723 61.328 -8.962 1.00 25.00 ? 84 GLY A C 1 ATOM 690 O O . GLY A 1 84 ? 2.892 60.950 -8.882 1.00 24.69 ? 84 GLY A O 1 ATOM 691 N N . SER A 1 85 ? 0.707 60.492 -9.159 1.00 25.07 ? 85 SER A N 1 ATOM 692 C CA . SER A 1 85 ? 0.898 59.053 -9.212 1.00 25.59 ? 85 SER A CA 1 ATOM 693 C C . SER A 1 85 ? 0.148 58.375 -10.353 1.00 26.30 ? 85 SER A C 1 ATOM 694 O O . SER A 1 85 ? -0.804 58.926 -10.907 1.00 26.29 ? 85 SER A O 1 ATOM 695 C CB . SER A 1 85 ? 0.440 58.442 -7.889 1.00 26.10 ? 85 SER A CB 1 ATOM 696 O OG . SER A 1 85 ? 0.920 59.202 -6.794 1.00 26.00 ? 85 SER A OG 1 ATOM 697 N N . ALA A 1 86 ? 0.578 57.160 -10.680 1.00 26.10 ? 86 ALA A N 1 ATOM 698 C CA . ALA A 1 86 ? -0.033 56.384 -11.747 1.00 24.33 ? 86 ALA A CA 1 ATOM 699 C C . ALA A 1 86 ? -0.900 55.261 -11.205 1.00 25.24 ? 86 ALA A C 1 ATOM 700 O O . ALA A 1 86 ? -0.545 54.604 -10.224 1.00 25.98 ? 86 ALA A O 1 ATOM 701 C CB . ALA A 1 86 ? 1.044 55.797 -12.641 1.00 23.27 ? 86 ALA A CB 1 ATOM 702 N N . THR A 1 87 ? -2.041 55.053 -11.852 1.00 25.14 ? 87 THR A N 1 ATOM 703 C CA . THR A 1 87 ? -2.960 53.979 -11.490 1.00 26.47 ? 87 THR A CA 1 ATOM 704 C C . THR A 1 87 ? -3.353 53.307 -12.798 1.00 27.17 ? 87 THR A C 1 ATOM 705 O O . THR A 1 87 ? -3.834 53.974 -13.718 1.00 27.75 ? 87 THR A O 1 ATOM 706 C CB . THR A 1 87 ? -4.253 54.496 -10.830 1.00 26.34 ? 87 THR A CB 1 ATOM 707 O OG1 . THR A 1 87 ? -3.940 55.180 -9.612 1.00 28.82 ? 87 THR A OG1 1 ATOM 708 C CG2 . THR A 1 87 ? -5.192 53.330 -10.528 1.00 26.26 ? 87 THR A CG2 1 ATOM 709 N N . ILE A 1 88 ? -3.138 52.000 -12.892 1.00 26.84 ? 88 ILE A N 1 ATOM 710 C CA . ILE A 1 88 ? -3.492 51.276 -14.105 1.00 26.71 ? 88 ILE A CA 1 ATOM 711 C C . ILE A 1 88 ? -4.906 50.732 -13.946 1.00 27.64 ? 88 ILE A C 1 ATOM 712 O O . ILE A 1 88 ? -5.154 49.803 -13.172 1.00 27.22 ? 88 ILE A O 1 ATOM 713 C CB . ILE A 1 88 ? -2.497 50.136 -14.374 1.00 27.57 ? 88 ILE A CB 1 ATOM 714 C CG1 . ILE A 1 88 ? -1.104 50.732 -14.601 1.00 26.57 ? 88 ILE A CG1 1 ATOM 715 C CG2 . ILE A 1 88 ? -2.938 49.328 -15.596 1.00 25.04 ? 88 ILE A CG2 1 ATOM 716 C CD1 . ILE A 1 88 ? -0.012 49.704 -14.726 1.00 29.72 ? 88 ILE A CD1 1 ATOM 717 N N . LEU A 1 89 ? -5.831 51.334 -14.685 1.00 27.09 ? 89 LEU A N 1 ATOM 718 C CA . LEU A 1 89 ? -7.233 50.963 -14.623 1.00 28.06 ? 89 LEU A CA 1 ATOM 719 C C . LEU A 1 89 ? -7.586 49.724 -15.429 1.00 28.62 ? 89 LEU A C 1 ATOM 720 O O . LEU A 1 89 ? -6.929 49.410 -16.420 1.00 28.40 ? 89 LEU A O 1 ATOM 721 C CB . LEU A 1 89 ? -8.092 52.118 -15.130 1.00 27.34 ? 89 LEU A CB 1 ATOM 722 C CG . LEU A 1 89 ? -7.783 53.520 -14.617 1.00 27.59 ? 89 LEU A CG 1 ATOM 723 C CD1 . LEU A 1 89 ? -8.803 54.482 -15.197 1.00 25.83 ? 89 LEU A CD1 1 ATOM 724 C CD2 . LEU A 1 89 ? -7.823 53.545 -13.103 1.00 26.17 ? 89 LEU A CD2 1 ATOM 725 N N . PRO A 1 90 ? -8.629 48.991 -14.998 1.00 29.44 ? 90 PRO A N 1 ATOM 726 C CA . PRO A 1 90 ? -9.047 47.791 -15.731 1.00 29.36 ? 90 PRO A CA 1 ATOM 727 C C . PRO A 1 90 ? -9.220 48.231 -17.185 1.00 29.09 ? 90 PRO A C 1 ATOM 728 O O . PRO A 1 90 ? -9.665 49.352 -17.451 1.00 27.03 ? 90 PRO A O 1 ATOM 729 C CB . PRO A 1 90 ? -10.373 47.433 -15.069 1.00 28.93 ? 90 PRO A CB 1 ATOM 730 C CG . PRO A 1 90 ? -10.128 47.813 -13.631 1.00 29.67 ? 90 PRO A CG 1 ATOM 731 C CD . PRO A 1 90 ? -9.406 49.153 -13.752 1.00 29.57 ? 90 PRO A CD 1 ATOM 732 N N . GLY A 1 91 ? -8.867 47.361 -18.119 1.00 29.66 ? 91 GLY A N 1 ATOM 733 C CA . GLY A 1 91 ? -8.956 47.733 -19.517 1.00 31.42 ? 91 GLY A CA 1 ATOM 734 C C . GLY A 1 91 ? -7.538 48.047 -19.949 1.00 32.19 ? 91 GLY A C 1 ATOM 735 O O . GLY A 1 91 ? -7.270 48.361 -21.113 1.00 31.27 ? 91 GLY A O 1 ATOM 736 N N . ASN A 1 92 ? -6.634 47.973 -18.970 1.00 32.29 ? 92 ASN A N 1 ATOM 737 C CA . ASN A 1 92 ? -5.204 48.193 -19.162 1.00 30.79 ? 92 ASN A CA 1 ATOM 738 C C . ASN A 1 92 ? -4.832 49.598 -19.632 1.00 31.26 ? 92 ASN A C 1 ATOM 739 O O . ASN A 1 92 ? -4.061 49.774 -20.580 1.00 32.31 ? 92 ASN A O 1 ATOM 740 C CB . ASN A 1 92 ? -4.672 47.140 -20.134 1.00 32.06 ? 92 ASN A CB 1 ATOM 741 C CG . ASN A 1 92 ? -3.210 46.850 -19.927 1.00 34.52 ? 92 ASN A CG 1 ATOM 742 O OD1 . ASN A 1 92 ? -2.726 46.825 -18.795 1.00 36.52 ? 92 ASN A OD1 1 ATOM 743 N ND2 . ASN A 1 92 ? -2.495 46.611 -21.018 1.00 38.06 ? 92 ASN A ND2 1 ATOM 744 N N . ILE A 1 93 ? -5.372 50.601 -18.954 1.00 29.85 ? 93 ILE A N 1 ATOM 745 C CA . ILE A 1 93 ? -5.091 51.981 -19.306 1.00 30.22 ? 93 ILE A CA 1 ATOM 746 C C . ILE A 1 93 ? -4.469 52.696 -18.105 1.00 30.48 ? 93 ILE A C 1 ATOM 747 O O . ILE A 1 93 ? -5.081 52.787 -17.037 1.00 31.41 ? 93 ILE A O 1 ATOM 748 C CB . ILE A 1 93 ? -6.400 52.708 -19.752 1.00 31.41 ? 93 ILE A CB 1 ATOM 749 C CG1 . ILE A 1 93 ? -6.140 54.194 -19.992 1.00 32.30 ? 93 ILE A CG1 1 ATOM 750 C CG2 . ILE A 1 93 ? -7.479 52.541 -18.710 1.00 32.92 ? 93 ILE A CG2 1 ATOM 751 C CD1 . ILE A 1 93 ? -5.446 54.484 -21.298 1.00 35.05 ? 93 ILE A CD1 1 ATOM 752 N N . PRO A 1 94 ? -3.223 53.181 -18.251 1.00 29.22 ? 94 PRO A N 1 ATOM 753 C CA . PRO A 1 94 ? -2.594 53.880 -17.126 1.00 28.76 ? 94 PRO A CA 1 ATOM 754 C C . PRO A 1 94 ? -3.121 55.300 -17.023 1.00 28.22 ? 94 PRO A C 1 ATOM 755 O O . PRO A 1 94 ? -3.091 56.047 -17.994 1.00 30.55 ? 94 PRO A O 1 ATOM 756 C CB . PRO A 1 94 ? -1.105 53.823 -17.464 1.00 28.09 ? 94 PRO A CB 1 ATOM 757 C CG . PRO A 1 94 ? -1.095 53.793 -18.948 1.00 30.47 ? 94 PRO A CG 1 ATOM 758 C CD . PRO A 1 94 ? -2.239 52.879 -19.303 1.00 28.36 ? 94 PRO A CD 1 ATOM 759 N N . ALA A 1 95 ? -3.629 55.657 -15.849 1.00 27.95 ? 95 ALA A N 1 ATOM 760 C CA . ALA A 1 95 ? -4.172 56.988 -15.610 1.00 27.41 ? 95 ALA A CA 1 ATOM 761 C C . ALA A 1 95 ? -3.257 57.726 -14.646 1.00 27.64 ? 95 ALA A C 1 ATOM 762 O O . ALA A 1 95 ? -2.857 57.181 -13.612 1.00 28.97 ? 95 ALA A O 1 ATOM 763 C CB . ALA A 1 95 ? -5.575 56.886 -15.028 1.00 27.05 ? 95 ALA A CB 1 ATOM 764 N N . MET A 1 96 ? -2.936 58.967 -14.985 1.00 26.37 ? 96 MET A N 1 ATOM 765 C CA . MET A 1 96 ? -2.044 59.779 -14.170 1.00 26.84 ? 96 MET A CA 1 ATOM 766 C C . MET A 1 96 ? -2.781 60.942 -13.507 1.00 28.02 ? 96 MET A C 1 ATOM 767 O O . MET A 1 96 ? -3.418 61.757 -14.182 1.00 29.19 ? 96 MET A O 1 ATOM 768 C CB . MET A 1 96 ? -0.917 60.322 -15.053 1.00 26.12 ? 96 MET A CB 1 ATOM 769 C CG . MET A 1 96 ? 0.387 60.584 -14.337 1.00 29.47 ? 96 MET A CG 1 ATOM 770 S SD . MET A 1 96 ? 1.152 59.074 -13.688 1.00 32.59 ? 96 MET A SD 1 ATOM 771 C CE . MET A 1 96 ? 1.905 58.392 -15.148 1.00 29.92 ? 96 MET A CE 1 ATOM 772 N N . LEU A 1 97 ? -2.707 61.003 -12.181 1.00 27.65 ? 97 LEU A N 1 ATOM 773 C CA . LEU A 1 97 ? -3.324 62.085 -11.418 1.00 26.97 ? 97 LEU A CA 1 ATOM 774 C C . LEU A 1 97 ? -2.171 62.908 -10.857 1.00 27.24 ? 97 LEU A C 1 ATOM 775 O O . LEU A 1 97 ? -1.282 62.365 -10.204 1.00 27.57 ? 97 LEU A O 1 ATOM 776 C CB . LEU A 1 97 ? -4.154 61.534 -10.262 1.00 26.49 ? 97 LEU A CB 1 ATOM 777 C CG . LEU A 1 97 ? -5.408 60.753 -10.634 1.00 28.46 ? 97 LEU A CG 1 ATOM 778 C CD1 . LEU A 1 97 ? -6.097 60.252 -9.368 1.00 24.32 ? 97 LEU A CD1 1 ATOM 779 C CD2 . LEU A 1 97 ? -6.330 61.657 -11.441 1.00 28.49 ? 97 LEU A CD2 1 ATOM 780 N N . TYR A 1 98 ? -2.173 64.210 -11.100 1.00 26.32 ? 98 TYR A N 1 ATOM 781 C CA . TYR A 1 98 ? -1.084 65.036 -10.605 1.00 26.65 ? 98 TYR A CA 1 ATOM 782 C C . TYR A 1 98 ? -1.578 66.417 -10.217 1.00 26.99 ? 98 TYR A C 1 ATOM 783 O O . TYR A 1 98 ? -2.650 66.845 -10.641 1.00 27.29 ? 98 TYR A O 1 ATOM 784 C CB . TYR A 1 98 ? -0.004 65.150 -11.679 1.00 25.72 ? 98 TYR A CB 1 ATOM 785 C CG . TYR A 1 98 ? -0.462 65.906 -12.900 1.00 25.69 ? 98 TYR A CG 1 ATOM 786 C CD1 . TYR A 1 98 ? -0.279 67.283 -12.996 1.00 26.91 ? 98 TYR A CD1 1 ATOM 787 C CD2 . TYR A 1 98 ? -1.118 65.253 -13.944 1.00 26.74 ? 98 TYR A CD2 1 ATOM 788 C CE1 . TYR A 1 98 ? -0.737 67.998 -14.101 1.00 26.73 ? 98 TYR A CE1 1 ATOM 789 C CE2 . TYR A 1 98 ? -1.584 65.959 -15.058 1.00 26.54 ? 98 TYR A CE2 1 ATOM 790 C CZ . TYR A 1 98 ? -1.388 67.332 -15.127 1.00 27.36 ? 98 TYR A CZ 1 ATOM 791 O OH . TYR A 1 98 ? -1.838 68.047 -16.216 1.00 29.90 ? 98 TYR A OH 1 ATOM 792 N N . THR A 1 99 ? -0.791 67.117 -9.409 1.00 26.49 ? 99 THR A N 1 ATOM 793 C CA . THR A 1 99 ? -1.172 68.452 -8.982 1.00 25.74 ? 99 THR A CA 1 ATOM 794 C C . THR A 1 99 ? -0.674 69.488 -9.967 1.00 25.89 ? 99 THR A C 1 ATOM 795 O O . THR A 1 99 ? 0.517 69.572 -10.244 1.00 26.26 ? 99 THR A O 1 ATOM 796 C CB . THR A 1 99 ? -0.598 68.791 -7.604 1.00 24.73 ? 99 THR A CB 1 ATOM 797 O OG1 . THR A 1 99 ? -1.138 67.892 -6.627 1.00 25.85 ? 99 THR A OG1 1 ATOM 798 C CG2 . THR A 1 99 ? -0.950 70.221 -7.226 1.00 22.99 ? 99 THR A CG2 1 ATOM 799 N N . GLY A 1 100 ? -1.594 70.270 -10.513 1.00 26.78 ? 100 GLY A N 1 ATOM 800 C CA . GLY A 1 100 ? -1.189 71.305 -11.441 1.00 26.73 ? 100 GLY A CA 1 ATOM 801 C C . GLY A 1 100 ? -1.300 72.649 -10.744 1.00 28.76 ? 100 GLY A C 1 ATOM 802 O O . GLY A 1 100 ? -2.076 72.799 -9.792 1.00 27.82 ? 100 GLY A O 1 ATOM 803 N N . SER A 1 101 ? -0.498 73.613 -11.182 1.00 28.42 ? 101 SER A N 1 ATOM 804 C CA . SER A 1 101 ? -0.559 74.961 -10.632 1.00 30.64 ? 101 SER A CA 1 ATOM 805 C C . SER A 1 101 ? -1.297 75.715 -11.740 1.00 32.09 ? 101 SER A C 1 ATOM 806 O O . SER A 1 101 ? -0.736 75.928 -12.818 1.00 32.06 ? 101 SER A O 1 ATOM 807 C CB . SER A 1 101 ? 0.852 75.521 -10.442 1.00 29.29 ? 101 SER A CB 1 ATOM 808 O OG . SER A 1 101 ? 0.821 76.779 -9.795 1.00 31.19 ? 101 SER A OG 1 ATOM 809 N N . ASP A 1 102 ? -2.553 76.091 -11.501 1.00 33.50 ? 102 ASP A N 1 ATOM 810 C CA . ASP A 1 102 ? -3.315 76.768 -12.548 1.00 35.77 ? 102 ASP A CA 1 ATOM 811 C C . ASP A 1 102 ? -2.991 78.243 -12.723 1.00 37.63 ? 102 ASP A C 1 ATOM 812 O O . ASP A 1 102 ? -2.113 78.778 -12.046 1.00 38.88 ? 102 ASP A O 1 ATOM 813 C CB . ASP A 1 102 ? -4.831 76.574 -12.352 1.00 35.78 ? 102 ASP A CB 1 ATOM 814 C CG . ASP A 1 102 ? -5.365 77.238 -11.100 1.00 36.92 ? 102 ASP A CG 1 ATOM 815 O OD1 . ASP A 1 102 ? -4.809 78.274 -10.676 1.00 37.73 ? 102 ASP A OD1 1 ATOM 816 O OD2 . ASP A 1 102 ? -6.367 76.729 -10.552 1.00 36.89 ? 102 ASP A OD2 1 ATOM 817 N N . SER A 1 103 ? -3.698 78.894 -13.644 1.00 38.75 ? 103 SER A N 1 ATOM 818 C CA . SER A 1 103 ? -3.470 80.305 -13.935 1.00 40.35 ? 103 SER A CA 1 ATOM 819 C C . SER A 1 103 ? -3.642 81.216 -12.725 1.00 41.22 ? 103 SER A C 1 ATOM 820 O O . SER A 1 103 ? -3.053 82.291 -12.677 1.00 42.42 ? 103 SER A O 1 ATOM 821 C CB . SER A 1 103 ? -4.384 80.759 -15.073 1.00 39.29 ? 103 SER A CB 1 ATOM 822 O OG . SER A 1 103 ? -5.733 80.426 -14.801 1.00 41.57 ? 103 SER A OG 1 ATOM 823 N N . LYS A 1 104 ? -4.442 80.789 -11.750 1.00 43.40 ? 104 LYS A N 1 ATOM 824 C CA . LYS A 1 104 ? -4.658 81.578 -10.532 1.00 45.59 ? 104 LYS A CA 1 ATOM 825 C C . LYS A 1 104 ? -3.668 81.146 -9.448 1.00 45.57 ? 104 LYS A C 1 ATOM 826 O O . LYS A 1 104 ? -3.812 81.495 -8.272 1.00 45.11 ? 104 LYS A O 1 ATOM 827 C CB . LYS A 1 104 ? -6.086 81.394 -10.006 1.00 49.01 ? 104 LYS A CB 1 ATOM 828 C CG . LYS A 1 104 ? -7.178 82.001 -10.877 1.00 54.64 ? 104 LYS A CG 1 ATOM 829 C CD . LYS A 1 104 ? -8.558 81.772 -10.250 1.00 60.30 ? 104 LYS A CD 1 ATOM 830 C CE . LYS A 1 104 ? -9.687 82.344 -11.114 1.00 62.39 ? 104 LYS A CE 1 ATOM 831 N NZ . LYS A 1 104 ? -11.038 82.069 -10.530 1.00 63.78 ? 104 LYS A NZ 1 ATOM 832 N N . SER A 1 105 ? -2.674 80.364 -9.856 1.00 44.41 ? 105 SER A N 1 ATOM 833 C CA . SER A 1 105 ? -1.645 79.877 -8.952 1.00 43.51 ? 105 SER A CA 1 ATOM 834 C C . SER A 1 105 ? -2.142 78.955 -7.850 1.00 42.14 ? 105 SER A C 1 ATOM 835 O O . SER A 1 105 ? -1.474 78.806 -6.829 1.00 43.39 ? 105 SER A O 1 ATOM 836 C CB . SER A 1 105 ? -0.898 81.053 -8.319 1.00 44.11 ? 105 SER A CB 1 ATOM 837 O OG . SER A 1 105 ? -0.150 81.759 -9.293 1.00 48.41 ? 105 SER A OG 1 ATOM 838 N N . ARG A 1 106 ? -3.302 78.333 -8.028 1.00 39.92 ? 106 ARG A N 1 ATOM 839 C CA . ARG A 1 106 ? -3.775 77.427 -6.992 1.00 38.56 ? 106 ARG A CA 1 ATOM 840 C C . ARG A 1 106 ? -3.527 75.967 -7.367 1.00 36.76 ? 106 ARG A C 1 ATOM 841 O O . ARG A 1 106 ? -3.463 75.608 -8.543 1.00 36.81 ? 106 ARG A O 1 ATOM 842 C CB . ARG A 1 106 ? -5.254 77.662 -6.679 1.00 39.69 ? 106 ARG A CB 1 ATOM 843 C CG . ARG A 1 106 ? -6.157 77.594 -7.857 1.00 44.91 ? 106 ARG A CG 1 ATOM 844 C CD . ARG A 1 106 ? -7.604 77.533 -7.419 1.00 46.86 ? 106 ARG A CD 1 ATOM 845 N NE . ARG A 1 106 ? -8.459 77.169 -8.544 1.00 49.18 ? 106 ARG A NE 1 ATOM 846 C CZ . ARG A 1 106 ? -9.717 76.766 -8.422 1.00 49.99 ? 106 ARG A CZ 1 ATOM 847 N NH1 . ARG A 1 106 ? -10.268 76.676 -7.218 1.00 49.66 ? 106 ARG A NH1 1 ATOM 848 N NH2 . ARG A 1 106 ? -10.417 76.442 -9.503 1.00 50.24 ? 106 ARG A NH2 1 ATOM 849 N N . GLN A 1 107 ? -3.362 75.134 -6.348 1.00 33.58 ? 107 GLN A N 1 ATOM 850 C CA . GLN A 1 107 ? -3.093 73.721 -6.538 1.00 30.98 ? 107 GLN A CA 1 ATOM 851 C C . GLN A 1 107 ? -4.364 72.929 -6.773 1.00 29.10 ? 107 GLN A C 1 ATOM 852 O O . GLN A 1 107 ? -5.230 72.863 -5.906 1.00 28.85 ? 107 GLN A O 1 ATOM 853 C CB . GLN A 1 107 ? -2.332 73.187 -5.321 1.00 29.96 ? 107 GLN A CB 1 ATOM 854 C CG . GLN A 1 107 ? -0.870 73.644 -5.307 1.00 31.32 ? 107 GLN A CG 1 ATOM 855 C CD . GLN A 1 107 ? -0.199 73.558 -3.940 1.00 30.36 ? 107 GLN A CD 1 ATOM 856 O OE1 . GLN A 1 107 ? -0.544 72.720 -3.101 1.00 30.19 ? 107 GLN A OE1 1 ATOM 857 N NE2 . GLN A 1 107 ? 0.783 74.419 -3.724 1.00 28.87 ? 107 GLN A NE2 1 ATOM 858 N N . VAL A 1 108 ? -4.462 72.333 -7.959 1.00 27.25 ? 108 VAL A N 1 ATOM 859 C CA . VAL A 1 108 ? -5.624 71.536 -8.347 1.00 26.98 ? 108 VAL A CA 1 ATOM 860 C C . VAL A 1 108 ? -5.172 70.175 -8.894 1.00 27.60 ? 108 VAL A C 1 ATOM 861 O O . VAL A 1 108 ? -4.044 70.038 -9.383 1.00 27.71 ? 108 VAL A O 1 ATOM 862 C CB . VAL A 1 108 ? -6.446 72.267 -9.429 1.00 26.99 ? 108 VAL A CB 1 ATOM 863 C CG1 . VAL A 1 108 ? -6.931 73.605 -8.899 1.00 27.02 ? 108 VAL A CG1 1 ATOM 864 C CG2 . VAL A 1 108 ? -5.594 72.481 -10.672 1.00 26.89 ? 108 VAL A CG2 1 ATOM 865 N N . GLN A 1 109 ? -6.046 69.173 -8.820 1.00 26.83 ? 109 GLN A N 1 ATOM 866 C CA . GLN A 1 109 ? -5.699 67.835 -9.297 1.00 28.13 ? 109 GLN A CA 1 ATOM 867 C C . GLN A 1 109 ? -6.191 67.572 -10.720 1.00 28.88 ? 109 GLN A C 1 ATOM 868 O O . GLN A 1 109 ? -7.389 67.688 -11.014 1.00 28.73 ? 109 GLN A O 1 ATOM 869 C CB . GLN A 1 109 ? -6.253 66.779 -8.339 1.00 27.22 ? 109 GLN A CB 1 ATOM 870 C CG . GLN A 1 109 ? -6.138 67.183 -6.871 1.00 29.47 ? 109 GLN A CG 1 ATOM 871 C CD . GLN A 1 109 ? -4.776 67.761 -6.519 1.00 29.76 ? 109 GLN A CD 1 ATOM 872 O OE1 . GLN A 1 109 ? -4.679 68.731 -5.755 1.00 31.44 ? 109 GLN A OE1 1 ATOM 873 N NE2 . GLN A 1 109 ? -3.718 67.170 -7.066 1.00 25.52 ? 109 GLN A NE2 1 ATOM 874 N N . ASP A 1 110 ? -5.250 67.205 -11.588 1.00 27.50 ? 110 ASP A N 1 ATOM 875 C CA . ASP A 1 110 ? -5.522 66.947 -12.999 1.00 27.46 ? 110 ASP A CA 1 ATOM 876 C C . ASP A 1 110 ? -5.325 65.492 -13.405 1.00 27.68 ? 110 ASP A C 1 ATOM 877 O O . ASP A 1 110 ? -4.614 64.736 -12.739 1.00 26.97 ? 110 ASP A O 1 ATOM 878 C CB . ASP A 1 110 ? -4.619 67.832 -13.849 1.00 28.65 ? 110 ASP A CB 1 ATOM 879 C CG . ASP A 1 110 ? -4.792 69.298 -13.531 1.00 29.38 ? 110 ASP A CG 1 ATOM 880 O OD1 . ASP A 1 110 ? -3.802 70.054 -13.629 1.00 30.79 ? 110 ASP A OD1 1 ATOM 881 O OD2 . ASP A 1 110 ? -5.925 69.693 -13.190 1.00 29.15 ? 110 ASP A OD2 1 ATOM 882 N N . LEU A 1 111 ? -5.943 65.122 -14.522 1.00 25.81 ? 111 LEU A N 1 ATOM 883 C CA . LEU A 1 111 ? -5.875 63.761 -15.038 1.00 25.50 ? 111 LEU A CA 1 ATOM 884 C C . LEU A 1 111 ? -5.281 63.735 -16.444 1.00 26.43 ? 111 LEU A C 1 ATOM 885 O O . LEU A 1 111 ? -5.547 64.614 -17.267 1.00 26.92 ? 111 LEU A O 1 ATOM 886 C CB . LEU A 1 111 ? -7.287 63.167 -15.069 1.00 25.94 ? 111 LEU A CB 1 ATOM 887 C CG . LEU A 1 111 ? -7.623 61.680 -15.247 1.00 27.95 ? 111 LEU A CG 1 ATOM 888 C CD1 . LEU A 1 111 ? -8.633 61.566 -16.370 1.00 25.61 ? 111 LEU A CD1 1 ATOM 889 C CD2 . LEU A 1 111 ? -6.394 60.837 -15.529 1.00 27.03 ? 111 LEU A CD2 1 ATOM 890 N N . ALA A 1 112 ? -4.468 62.724 -16.714 1.00 25.96 ? 112 ALA A N 1 ATOM 891 C CA . ALA A 1 112 ? -3.864 62.561 -18.028 1.00 25.68 ? 112 ALA A CA 1 ATOM 892 C C . ALA A 1 112 ? -3.679 61.068 -18.242 1.00 25.48 ? 112 ALA A C 1 ATOM 893 O O . ALA A 1 112 ? -3.628 60.305 -17.280 1.00 24.95 ? 112 ALA A O 1 ATOM 894 C CB . ALA A 1 112 ? -2.516 63.275 -18.092 1.00 22.34 ? 112 ALA A CB 1 ATOM 895 N N . TRP A 1 113 ? -3.607 60.646 -19.498 1.00 25.21 ? 113 TRP A N 1 ATOM 896 C CA . TRP A 1 113 ? -3.395 59.237 -19.806 1.00 26.40 ? 113 TRP A CA 1 ATOM 897 C C . TRP A 1 113 ? -2.684 59.175 -21.143 1.00 25.34 ? 113 TRP A C 1 ATOM 898 O O . TRP A 1 113 ? -2.720 60.132 -21.912 1.00 25.69 ? 113 TRP A O 1 ATOM 899 C CB . TRP A 1 113 ? -4.726 58.463 -19.811 1.00 27.62 ? 113 TRP A CB 1 ATOM 900 C CG . TRP A 1 113 ? -5.711 58.841 -20.876 1.00 30.62 ? 113 TRP A CG 1 ATOM 901 C CD1 . TRP A 1 113 ? -5.841 58.272 -22.113 1.00 32.53 ? 113 TRP A CD1 1 ATOM 902 C CD2 . TRP A 1 113 ? -6.725 59.854 -20.792 1.00 30.84 ? 113 TRP A CD2 1 ATOM 903 N NE1 . TRP A 1 113 ? -6.875 58.866 -22.803 1.00 33.78 ? 113 TRP A NE1 1 ATOM 904 C CE2 . TRP A 1 113 ? -7.433 59.841 -22.016 1.00 32.85 ? 113 TRP A CE2 1 ATOM 905 C CE3 . TRP A 1 113 ? -7.105 60.771 -19.803 1.00 31.06 ? 113 TRP A CE3 1 ATOM 906 C CZ2 . TRP A 1 113 ? -8.499 60.712 -22.277 1.00 31.64 ? 113 TRP A CZ2 1 ATOM 907 C CZ3 . TRP A 1 113 ? -8.165 61.636 -20.062 1.00 29.92 ? 113 TRP A CZ3 1 ATOM 908 C CH2 . TRP A 1 113 ? -8.847 61.599 -21.291 1.00 31.21 ? 113 TRP A CH2 1 ATOM 909 N N . PRO A 1 114 ? -1.990 58.067 -21.427 1.00 27.00 ? 114 PRO A N 1 ATOM 910 C CA . PRO A 1 114 ? -1.286 57.990 -22.711 1.00 27.86 ? 114 PRO A CA 1 ATOM 911 C C . PRO A 1 114 ? -2.188 58.091 -23.930 1.00 28.01 ? 114 PRO A C 1 ATOM 912 O O . PRO A 1 114 ? -3.290 57.543 -23.960 1.00 26.99 ? 114 PRO A O 1 ATOM 913 C CB . PRO A 1 114 ? -0.531 56.661 -22.623 1.00 27.39 ? 114 PRO A CB 1 ATOM 914 C CG . PRO A 1 114 ? -1.299 55.875 -21.614 1.00 29.96 ? 114 PRO A CG 1 ATOM 915 C CD . PRO A 1 114 ? -1.733 56.877 -20.599 1.00 27.62 ? 114 PRO A CD 1 ATOM 916 N N . LYS A 1 115 ? -1.708 58.803 -24.939 1.00 28.91 ? 115 LYS A N 1 ATOM 917 C CA . LYS A 1 115 ? -2.479 58.984 -26.156 1.00 31.71 ? 115 LYS A CA 1 ATOM 918 C C . LYS A 1 115 ? -2.211 57.903 -27.200 1.00 31.53 ? 115 LYS A C 1 ATOM 919 O O . LYS A 1 115 ? -2.959 57.768 -28.169 1.00 33.58 ? 115 LYS A O 1 ATOM 920 C CB . LYS A 1 115 ? -2.172 60.354 -26.756 1.00 33.72 ? 115 LYS A CB 1 ATOM 921 C CG . LYS A 1 115 ? -3.142 60.746 -27.842 1.00 38.37 ? 115 LYS A CG 1 ATOM 922 C CD . LYS A 1 115 ? -2.939 62.174 -28.292 1.00 39.03 ? 115 LYS A CD 1 ATOM 923 C CE . LYS A 1 115 ? -1.658 62.334 -29.061 1.00 39.64 ? 115 LYS A CE 1 ATOM 924 N NZ . LYS A 1 115 ? -1.737 63.578 -29.876 1.00 43.14 ? 115 LYS A NZ 1 ATOM 925 N N . ASN A 1 116 ? -1.158 57.121 -26.992 1.00 30.48 ? 116 ASN A N 1 ATOM 926 C CA . ASN A 1 116 ? -0.774 56.085 -27.942 1.00 29.82 ? 116 ASN A CA 1 ATOM 927 C C . ASN A 1 116 ? -0.318 54.815 -27.222 1.00 29.89 ? 116 ASN A C 1 ATOM 928 O O . ASN A 1 116 ? 0.882 54.595 -27.037 1.00 28.64 ? 116 ASN A O 1 ATOM 929 C CB . ASN A 1 116 ? 0.353 56.636 -28.810 1.00 29.46 ? 116 ASN A CB 1 ATOM 930 C CG . ASN A 1 116 ? 0.780 55.688 -29.905 1.00 32.81 ? 116 ASN A CG 1 ATOM 931 O OD1 . ASN A 1 116 ? 0.252 54.583 -30.043 1.00 31.98 ? 116 ASN A OD1 1 ATOM 932 N ND2 . ASN A 1 116 ? 1.755 56.143 -30.690 1.00 34.07 ? 116 ASN A ND2 1 ATOM 933 N N . LEU A 1 117 ? -1.273 53.977 -26.829 1.00 28.83 ? 117 LEU A N 1 ATOM 934 C CA . LEU A 1 117 ? -0.944 52.747 -26.117 1.00 30.05 ? 117 LEU A CA 1 ATOM 935 C C . LEU A 1 117 ? -0.102 51.766 -26.935 1.00 31.61 ? 117 LEU A C 1 ATOM 936 O O . LEU A 1 117 ? 0.412 50.788 -26.392 1.00 33.59 ? 117 LEU A O 1 ATOM 937 C CB . LEU A 1 117 ? -2.225 52.067 -25.602 1.00 28.07 ? 117 LEU A CB 1 ATOM 938 C CG . LEU A 1 117 ? -2.990 52.829 -24.502 1.00 28.55 ? 117 LEU A CG 1 ATOM 939 C CD1 . LEU A 1 117 ? -4.194 52.020 -24.055 1.00 27.44 ? 117 LEU A CD1 1 ATOM 940 C CD2 . LEU A 1 117 ? -2.081 53.098 -23.306 1.00 24.18 ? 117 LEU A CD2 1 ATOM 941 N N . SER A 1 118 ? 0.050 52.025 -28.230 1.00 32.51 ? 118 SER A N 1 ATOM 942 C CA . SER A 1 118 ? 0.871 51.165 -29.086 1.00 33.79 ? 118 SER A CA 1 ATOM 943 C C . SER A 1 118 ? 2.350 51.447 -28.833 1.00 32.74 ? 118 SER A C 1 ATOM 944 O O . SER A 1 118 ? 3.214 50.638 -29.163 1.00 32.67 ? 118 SER A O 1 ATOM 945 C CB . SER A 1 118 ? 0.581 51.424 -30.566 1.00 35.04 ? 118 SER A CB 1 ATOM 946 O OG . SER A 1 118 ? -0.736 51.036 -30.901 1.00 43.45 ? 118 SER A OG 1 ATOM 947 N N . ASP A 1 119 ? 2.629 52.613 -28.260 1.00 31.17 ? 119 ASP A N 1 ATOM 948 C CA . ASP A 1 119 ? 3.994 53.026 -27.958 1.00 30.75 ? 119 ASP A CA 1 ATOM 949 C C . ASP A 1 119 ? 4.468 52.395 -26.645 1.00 29.82 ? 119 ASP A C 1 ATOM 950 O O . ASP A 1 119 ? 3.980 52.739 -25.573 1.00 31.87 ? 119 ASP A O 1 ATOM 951 C CB . ASP A 1 119 ? 4.047 54.557 -27.865 1.00 30.32 ? 119 ASP A CB 1 ATOM 952 C CG . ASP A 1 119 ? 5.424 55.074 -27.518 1.00 29.79 ? 119 ASP A CG 1 ATOM 953 O OD1 . ASP A 1 119 ? 6.345 54.253 -27.357 1.00 30.61 ? 119 ASP A OD1 1 ATOM 954 O OD2 . ASP A 1 119 ? 5.589 56.306 -27.405 1.00 31.41 ? 119 ASP A OD2 1 ATOM 955 N N . PRO A 1 120 ? 5.433 51.464 -26.713 1.00 29.57 ? 120 PRO A N 1 ATOM 956 C CA . PRO A 1 120 ? 5.960 50.795 -25.518 1.00 29.29 ? 120 PRO A CA 1 ATOM 957 C C . PRO A 1 120 ? 6.494 51.781 -24.486 1.00 28.28 ? 120 PRO A C 1 ATOM 958 O O . PRO A 1 120 ? 6.514 51.488 -23.290 1.00 27.84 ? 120 PRO A O 1 ATOM 959 C CB . PRO A 1 120 ? 7.090 49.919 -26.069 1.00 29.30 ? 120 PRO A CB 1 ATOM 960 C CG . PRO A 1 120 ? 6.693 49.679 -27.474 1.00 32.52 ? 120 PRO A CG 1 ATOM 961 C CD . PRO A 1 120 ? 6.164 51.026 -27.913 1.00 31.43 ? 120 PRO A CD 1 ATOM 962 N N . PHE A 1 121 ? 6.929 52.946 -24.957 1.00 26.48 ? 121 PHE A N 1 ATOM 963 C CA . PHE A 1 121 ? 7.491 53.957 -24.077 1.00 26.76 ? 121 PHE A CA 1 ATOM 964 C C . PHE A 1 121 ? 6.526 55.046 -23.626 1.00 26.96 ? 121 PHE A C 1 ATOM 965 O O . PHE A 1 121 ? 6.924 55.961 -22.906 1.00 27.72 ? 121 PHE A O 1 ATOM 966 C CB . PHE A 1 121 ? 8.714 54.595 -24.743 1.00 26.36 ? 121 PHE A CB 1 ATOM 967 C CG . PHE A 1 121 ? 9.859 53.639 -24.951 1.00 27.30 ? 121 PHE A CG 1 ATOM 968 C CD1 . PHE A 1 121 ? 9.859 52.382 -24.341 1.00 26.64 ? 121 PHE A CD1 1 ATOM 969 C CD2 . PHE A 1 121 ? 10.955 54.005 -25.728 1.00 26.69 ? 121 PHE A CD2 1 ATOM 970 C CE1 . PHE A 1 121 ? 10.939 51.504 -24.500 1.00 25.46 ? 121 PHE A CE1 1 ATOM 971 C CE2 . PHE A 1 121 ? 12.039 53.135 -25.893 1.00 25.31 ? 121 PHE A CE2 1 ATOM 972 C CZ . PHE A 1 121 ? 12.030 51.884 -25.277 1.00 23.53 ? 121 PHE A CZ 1 ATOM 973 N N . LEU A 1 122 ? 5.265 54.952 -24.043 1.00 25.92 ? 122 LEU A N 1 ATOM 974 C CA . LEU A 1 122 ? 4.255 55.938 -23.662 1.00 25.42 ? 122 LEU A CA 1 ATOM 975 C C . LEU A 1 122 ? 4.810 57.368 -23.620 1.00 26.40 ? 122 LEU A C 1 ATOM 976 O O . LEU A 1 122 ? 4.790 58.025 -22.573 1.00 25.61 ? 122 LEU A O 1 ATOM 977 C CB . LEU A 1 122 ? 3.680 55.576 -22.292 1.00 23.74 ? 122 LEU A CB 1 ATOM 978 C CG . LEU A 1 122 ? 3.103 54.165 -22.154 1.00 24.50 ? 122 LEU A CG 1 ATOM 979 C CD1 . LEU A 1 122 ? 2.607 53.964 -20.727 1.00 22.50 ? 122 LEU A CD1 1 ATOM 980 C CD2 . LEU A 1 122 ? 1.972 53.952 -23.165 1.00 21.10 ? 122 LEU A CD2 1 ATOM 981 N N . ARG A 1 123 ? 5.290 57.859 -24.756 1.00 26.97 ? 123 ARG A N 1 ATOM 982 C CA . ARG A 1 123 ? 5.860 59.203 -24.794 1.00 29.80 ? 123 ARG A CA 1 ATOM 983 C C . ARG A 1 123 ? 4.843 60.335 -24.772 1.00 30.07 ? 123 ARG A C 1 ATOM 984 O O . ARG A 1 123 ? 5.056 61.342 -24.098 1.00 30.16 ? 123 ARG A O 1 ATOM 985 C CB . ARG A 1 123 ? 6.742 59.369 -26.027 1.00 30.01 ? 123 ARG A CB 1 ATOM 986 C CG . ARG A 1 123 ? 7.722 58.245 -26.232 1.00 33.52 ? 123 ARG A CG 1 ATOM 987 C CD . ARG A 1 123 ? 8.654 58.560 -27.373 1.00 36.58 ? 123 ARG A CD 1 ATOM 988 N NE . ARG A 1 123 ? 9.342 57.367 -27.844 1.00 40.59 ? 123 ARG A NE 1 ATOM 989 C CZ . ARG A 1 123 ? 10.618 57.337 -28.219 1.00 45.81 ? 123 ARG A CZ 1 ATOM 990 N NH1 . ARG A 1 123 ? 11.359 58.447 -28.176 1.00 47.07 ? 123 ARG A NH1 1 ATOM 991 N NH2 . ARG A 1 123 ? 11.157 56.196 -28.640 1.00 45.81 ? 123 ARG A NH2 1 ATOM 992 N N . GLU A 1 124 ? 3.746 60.169 -25.509 1.00 30.43 ? 124 GLU A N 1 ATOM 993 C CA . GLU A 1 124 ? 2.709 61.197 -25.606 1.00 31.64 ? 124 GLU A CA 1 ATOM 994 C C . GLU A 1 124 ? 1.541 60.975 -24.660 1.00 31.12 ? 124 GLU A C 1 ATOM 995 O O . GLU A 1 124 ? 0.989 59.873 -24.576 1.00 30.76 ? 124 GLU A O 1 ATOM 996 C CB . GLU A 1 124 ? 2.166 61.275 -27.036 1.00 35.35 ? 124 GLU A CB 1 ATOM 997 C CG . GLU A 1 124 ? 3.192 61.599 -28.113 1.00 39.90 ? 124 GLU A CG 1 ATOM 998 C CD . GLU A 1 124 ? 3.897 62.923 -27.873 1.00 45.16 ? 124 GLU A CD 1 ATOM 999 O OE1 . GLU A 1 124 ? 3.229 63.885 -27.430 1.00 46.42 ? 124 GLU A OE1 1 ATOM 1000 O OE2 . GLU A 1 124 ? 5.117 63.004 -28.140 1.00 46.87 ? 124 GLU A OE2 1 ATOM 1001 N N . TRP A 1 125 ? 1.150 62.041 -23.969 1.00 29.56 ? 125 TRP A N 1 ATOM 1002 C CA . TRP A 1 125 ? 0.044 61.976 -23.024 1.00 29.31 ? 125 TRP A CA 1 ATOM 1003 C C . TRP A 1 125 ? -1.041 62.997 -23.346 1.00 30.33 ? 125 TRP A C 1 ATOM 1004 O O . TRP A 1 125 ? -0.755 64.104 -23.806 1.00 31.46 ? 125 TRP A O 1 ATOM 1005 C CB . TRP A 1 125 ? 0.563 62.200 -21.601 1.00 26.61 ? 125 TRP A CB 1 ATOM 1006 C CG . TRP A 1 125 ? 1.439 61.082 -21.123 1.00 26.25 ? 125 TRP A CG 1 ATOM 1007 C CD1 . TRP A 1 125 ? 2.682 60.751 -21.591 1.00 26.51 ? 125 TRP A CD1 1 ATOM 1008 C CD2 . TRP A 1 125 ? 1.101 60.090 -20.147 1.00 23.92 ? 125 TRP A CD2 1 ATOM 1009 N NE1 . TRP A 1 125 ? 3.135 59.610 -20.969 1.00 25.58 ? 125 TRP A NE1 1 ATOM 1010 C CE2 . TRP A 1 125 ? 2.183 59.184 -20.079 1.00 24.00 ? 125 TRP A CE2 1 ATOM 1011 C CE3 . TRP A 1 125 ? -0.016 59.877 -19.327 1.00 24.00 ? 125 TRP A CE3 1 ATOM 1012 C CZ2 . TRP A 1 125 ? 2.182 58.077 -19.223 1.00 23.40 ? 125 TRP A CZ2 1 ATOM 1013 C CZ3 . TRP A 1 125 ? -0.019 58.775 -18.475 1.00 24.08 ? 125 TRP A CZ3 1 ATOM 1014 C CH2 . TRP A 1 125 ? 1.076 57.889 -18.432 1.00 25.02 ? 125 TRP A CH2 1 ATOM 1015 N N . VAL A 1 126 ? -2.290 62.620 -23.107 1.00 28.57 ? 126 VAL A N 1 ATOM 1016 C CA . VAL A 1 126 ? -3.404 63.516 -23.364 1.00 28.46 ? 126 VAL A CA 1 ATOM 1017 C C . VAL A 1 126 ? -4.042 63.874 -22.023 1.00 27.78 ? 126 VAL A C 1 ATOM 1018 O O . VAL A 1 126 ? -4.108 63.042 -21.117 1.00 26.48 ? 126 VAL A O 1 ATOM 1019 C CB . VAL A 1 126 ? -4.451 62.854 -24.310 1.00 29.29 ? 126 VAL A CB 1 ATOM 1020 C CG1 . VAL A 1 126 ? -4.993 61.576 -23.692 1.00 31.19 ? 126 VAL A CG1 1 ATOM 1021 C CG2 . VAL A 1 126 ? -5.587 63.819 -24.592 1.00 30.94 ? 126 VAL A CG2 1 ATOM 1022 N N . LYS A 1 127 ? -4.499 65.115 -21.897 1.00 27.08 ? 127 LYS A N 1 ATOM 1023 C CA . LYS A 1 127 ? -5.113 65.573 -20.660 1.00 29.04 ? 127 LYS A CA 1 ATOM 1024 C C . LYS A 1 127 ? -6.627 65.627 -20.744 1.00 29.03 ? 127 LYS A C 1 ATOM 1025 O O . LYS A 1 127 ? -7.188 65.917 -21.796 1.00 29.34 ? 127 LYS A O 1 ATOM 1026 C CB . LYS A 1 127 ? -4.545 66.942 -20.283 1.00 28.31 ? 127 LYS A CB 1 ATOM 1027 C CG . LYS A 1 127 ? -3.064 66.851 -19.954 1.00 29.59 ? 127 LYS A CG 1 ATOM 1028 C CD . LYS A 1 127 ? -2.430 68.197 -19.750 1.00 30.60 ? 127 LYS A CD 1 ATOM 1029 C CE . LYS A 1 127 ? -0.923 68.063 -19.635 1.00 27.31 ? 127 LYS A CE 1 ATOM 1030 N NZ . LYS A 1 127 ? -0.298 69.406 -19.516 1.00 29.13 ? 127 LYS A NZ 1 ATOM 1031 N N . HIS A 1 128 ? -7.289 65.325 -19.633 1.00 29.49 ? 128 HIS A N 1 ATOM 1032 C CA . HIS A 1 128 ? -8.738 65.351 -19.613 1.00 30.40 ? 128 HIS A CA 1 ATOM 1033 C C . HIS A 1 128 ? -9.236 66.778 -19.819 1.00 31.94 ? 128 HIS A C 1 ATOM 1034 O O . HIS A 1 128 ? -8.739 67.712 -19.181 1.00 32.23 ? 128 HIS A O 1 ATOM 1035 C CB . HIS A 1 128 ? -9.277 64.824 -18.294 1.00 30.65 ? 128 HIS A CB 1 ATOM 1036 C CG . HIS A 1 128 ? -10.741 64.532 -18.341 1.00 33.47 ? 128 HIS A CG 1 ATOM 1037 N ND1 . HIS A 1 128 ? -11.240 63.295 -18.692 1.00 34.56 ? 128 HIS A ND1 1 ATOM 1038 C CD2 . HIS A 1 128 ? -11.814 65.340 -18.181 1.00 32.79 ? 128 HIS A CD2 1 ATOM 1039 C CE1 . HIS A 1 128 ? -12.558 63.355 -18.748 1.00 34.00 ? 128 HIS A CE1 1 ATOM 1040 N NE2 . HIS A 1 128 ? -12.931 64.585 -18.443 1.00 35.46 ? 128 HIS A NE2 1 ATOM 1041 N N . PRO A 1 129 ? -10.237 66.960 -20.704 1.00 32.51 ? 129 PRO A N 1 ATOM 1042 C CA . PRO A 1 129 ? -10.839 68.258 -21.036 1.00 32.63 ? 129 PRO A CA 1 ATOM 1043 C C . PRO A 1 129 ? -11.460 68.973 -19.843 1.00 33.35 ? 129 PRO A C 1 ATOM 1044 O O . PRO A 1 129 ? -11.548 70.198 -19.829 1.00 33.85 ? 129 PRO A O 1 ATOM 1045 C CB . PRO A 1 129 ? -11.901 67.898 -22.081 1.00 31.29 ? 129 PRO A CB 1 ATOM 1046 C CG . PRO A 1 129 ? -11.412 66.641 -22.667 1.00 32.20 ? 129 PRO A CG 1 ATOM 1047 C CD . PRO A 1 129 ? -10.894 65.888 -21.469 1.00 32.86 ? 129 PRO A CD 1 ATOM 1048 N N . LYS A 1 130 ? -11.898 68.206 -18.849 1.00 34.83 ? 130 LYS A N 1 ATOM 1049 C CA . LYS A 1 130 ? -12.525 68.790 -17.673 1.00 36.08 ? 130 LYS A CA 1 ATOM 1050 C C . LYS A 1 130 ? -11.584 69.106 -16.506 1.00 35.72 ? 130 LYS A C 1 ATOM 1051 O O . LYS A 1 130 ? -12.045 69.385 -15.399 1.00 35.75 ? 130 LYS A O 1 ATOM 1052 C CB . LYS A 1 130 ? -13.685 67.901 -17.200 1.00 38.90 ? 130 LYS A CB 1 ATOM 1053 C CG . LYS A 1 130 ? -14.868 67.908 -18.173 1.00 45.27 ? 130 LYS A CG 1 ATOM 1054 C CD . LYS A 1 130 ? -16.143 67.281 -17.591 1.00 50.79 ? 130 LYS A CD 1 ATOM 1055 C CE . LYS A 1 130 ? -16.068 65.756 -17.527 1.00 54.59 ? 130 LYS A CE 1 ATOM 1056 N NZ . LYS A 1 130 ? -17.328 65.133 -16.999 1.00 56.82 ? 130 LYS A NZ 1 ATOM 1057 N N . ASN A 1 131 ? -10.273 69.071 -16.741 1.00 33.92 ? 131 ASN A N 1 ATOM 1058 C CA . ASN A 1 131 ? -9.338 69.403 -15.668 1.00 33.75 ? 131 ASN A CA 1 ATOM 1059 C C . ASN A 1 131 ? -9.581 70.868 -15.303 1.00 34.54 ? 131 ASN A C 1 ATOM 1060 O O . ASN A 1 131 ? -9.866 71.691 -16.178 1.00 36.14 ? 131 ASN A O 1 ATOM 1061 C CB . ASN A 1 131 ? -7.877 69.240 -16.113 1.00 29.43 ? 131 ASN A CB 1 ATOM 1062 C CG . ASN A 1 131 ? -7.425 67.791 -16.144 1.00 27.92 ? 131 ASN A CG 1 ATOM 1063 O OD1 . ASN A 1 131 ? -7.949 66.947 -15.419 1.00 24.93 ? 131 ASN A OD1 1 ATOM 1064 N ND2 . ASN A 1 131 ? -6.427 67.503 -16.972 1.00 22.89 ? 131 ASN A ND2 1 ATOM 1065 N N . PRO A 1 132 ? -9.459 71.216 -14.012 1.00 34.91 ? 132 PRO A N 1 ATOM 1066 C CA . PRO A 1 132 ? -9.110 70.324 -12.898 1.00 34.21 ? 132 PRO A CA 1 ATOM 1067 C C . PRO A 1 132 ? -10.269 69.457 -12.422 1.00 34.02 ? 132 PRO A C 1 ATOM 1068 O O . PRO A 1 132 ? -11.416 69.900 -12.380 1.00 34.57 ? 132 PRO A O 1 ATOM 1069 C CB . PRO A 1 132 ? -8.649 71.295 -11.820 1.00 35.11 ? 132 PRO A CB 1 ATOM 1070 C CG . PRO A 1 132 ? -9.552 72.477 -12.056 1.00 34.39 ? 132 PRO A CG 1 ATOM 1071 C CD . PRO A 1 132 ? -9.513 72.620 -13.562 1.00 33.92 ? 132 PRO A CD 1 ATOM 1072 N N . LEU A 1 133 ? -9.954 68.221 -12.054 1.00 32.56 ? 133 LEU A N 1 ATOM 1073 C CA . LEU A 1 133 ? -10.949 67.276 -11.573 1.00 30.46 ? 133 LEU A CA 1 ATOM 1074 C C . LEU A 1 133 ? -11.277 67.510 -10.100 1.00 31.23 ? 133 LEU A C 1 ATOM 1075 O O . LEU A 1 133 ? -12.389 67.228 -9.648 1.00 31.20 ? 133 LEU A O 1 ATOM 1076 C CB . LEU A 1 133 ? -10.430 65.849 -11.762 1.00 29.16 ? 133 LEU A CB 1 ATOM 1077 C CG . LEU A 1 133 ? -10.899 65.034 -12.971 1.00 28.22 ? 133 LEU A CG 1 ATOM 1078 C CD1 . LEU A 1 133 ? -10.960 65.887 -14.217 1.00 25.55 ? 133 LEU A CD1 1 ATOM 1079 C CD2 . LEU A 1 133 ? -9.961 63.856 -13.152 1.00 25.76 ? 133 LEU A CD2 1 ATOM 1080 N N . ILE A 1 134 ? -10.303 68.016 -9.352 1.00 31.01 ? 134 ILE A N 1 ATOM 1081 C CA . ILE A 1 134 ? -10.491 68.275 -7.930 1.00 30.66 ? 134 ILE A CA 1 ATOM 1082 C C . ILE A 1 134 ? -9.808 69.574 -7.534 1.00 32.09 ? 134 ILE A C 1 ATOM 1083 O O . ILE A 1 134 ? -8.659 69.823 -7.912 1.00 32.50 ? 134 ILE A O 1 ATOM 1084 C CB . ILE A 1 134 ? -9.888 67.150 -7.064 1.00 30.01 ? 134 ILE A CB 1 ATOM 1085 C CG1 . ILE A 1 134 ? -10.456 65.797 -7.490 1.00 26.64 ? 134 ILE A CG1 1 ATOM 1086 C CG2 . ILE A 1 134 ? -10.187 67.415 -5.596 1.00 28.83 ? 134 ILE A CG2 1 ATOM 1087 C CD1 . ILE A 1 134 ? -9.786 64.620 -6.818 1.00 28.37 ? 134 ILE A CD1 1 ATOM 1088 N N . THR A 1 135 ? -10.522 70.398 -6.775 1.00 32.13 ? 135 THR A N 1 ATOM 1089 C CA . THR A 1 135 ? -9.987 71.669 -6.305 1.00 32.14 ? 135 THR A CA 1 ATOM 1090 C C . THR A 1 135 ? -10.003 71.661 -4.778 1.00 31.71 ? 135 THR A C 1 ATOM 1091 O O . THR A 1 135 ? -10.720 70.871 -4.163 1.00 30.76 ? 135 THR A O 1 ATOM 1092 C CB . THR A 1 135 ? -10.819 72.847 -6.835 1.00 33.31 ? 135 THR A CB 1 ATOM 1093 O OG1 . THR A 1 135 ? -12.197 72.649 -6.495 1.00 36.19 ? 135 THR A OG1 1 ATOM 1094 C CG2 . THR A 1 135 ? -10.674 72.955 -8.347 1.00 32.09 ? 135 THR A CG2 1 ATOM 1095 N N . PRO A 1 136 ? -9.214 72.542 -4.145 1.00 32.64 ? 136 PRO A N 1 ATOM 1096 C CA . PRO A 1 136 ? -9.144 72.613 -2.680 1.00 34.42 ? 136 PRO A CA 1 ATOM 1097 C C . PRO A 1 136 ? -10.489 72.612 -1.952 1.00 36.86 ? 136 PRO A C 1 ATOM 1098 O O . PRO A 1 136 ? -11.422 73.312 -2.350 1.00 36.49 ? 136 PRO A O 1 ATOM 1099 C CB . PRO A 1 136 ? -8.360 73.900 -2.435 1.00 34.38 ? 136 PRO A CB 1 ATOM 1100 C CG . PRO A 1 136 ? -7.450 73.967 -3.632 1.00 33.87 ? 136 PRO A CG 1 ATOM 1101 C CD . PRO A 1 136 ? -8.379 73.588 -4.762 1.00 32.00 ? 136 PRO A CD 1 ATOM 1102 N N . PRO A 1 137 ? -10.603 71.812 -0.875 1.00 38.96 ? 137 PRO A N 1 ATOM 1103 C CA . PRO A 1 137 ? -11.827 71.713 -0.071 1.00 41.26 ? 137 PRO A CA 1 ATOM 1104 C C . PRO A 1 137 ? -12.150 73.077 0.539 1.00 44.69 ? 137 PRO A C 1 ATOM 1105 O O . PRO A 1 137 ? -11.315 73.988 0.522 1.00 43.99 ? 137 PRO A O 1 ATOM 1106 C CB . PRO A 1 137 ? -11.460 70.685 0.997 1.00 41.15 ? 137 PRO A CB 1 ATOM 1107 C CG . PRO A 1 137 ? -10.449 69.823 0.302 1.00 39.85 ? 137 PRO A CG 1 ATOM 1108 C CD . PRO A 1 137 ? -9.599 70.835 -0.420 1.00 38.78 ? 137 PRO A CD 1 ATOM 1109 N N . GLU A 1 138 ? -13.346 73.208 1.101 1.00 48.34 ? 138 GLU A N 1 ATOM 1110 C CA . GLU A 1 138 ? -13.783 74.473 1.681 1.00 51.38 ? 138 GLU A CA 1 ATOM 1111 C C . GLU A 1 138 ? -12.769 75.272 2.507 1.00 50.41 ? 138 GLU A C 1 ATOM 1112 O O . GLU A 1 138 ? -12.413 76.395 2.130 1.00 51.51 ? 138 GLU A O 1 ATOM 1113 C CB . GLU A 1 138 ? -15.060 74.265 2.504 1.00 56.92 ? 138 GLU A CB 1 ATOM 1114 C CG . GLU A 1 138 ? -15.574 75.541 3.180 1.00 63.85 ? 138 GLU A CG 1 ATOM 1115 C CD . GLU A 1 138 ? -15.658 76.735 2.227 1.00 67.99 ? 138 GLU A CD 1 ATOM 1116 O OE1 . GLU A 1 138 ? -15.883 77.867 2.712 1.00 70.77 ? 138 GLU A OE1 1 ATOM 1117 O OE2 . GLU A 1 138 ? -15.502 76.548 0.998 1.00 69.70 ? 138 GLU A OE2 1 ATOM 1118 N N . GLY A 1 139 ? -12.299 74.721 3.620 1.00 46.60 ? 139 GLY A N 1 ATOM 1119 C CA . GLY A 1 139 ? -11.362 75.484 4.432 1.00 45.74 ? 139 GLY A CA 1 ATOM 1120 C C . GLY A 1 139 ? -9.875 75.244 4.221 1.00 44.51 ? 139 GLY A C 1 ATOM 1121 O O . GLY A 1 139 ? -9.091 75.372 5.164 1.00 45.08 ? 139 GLY A O 1 ATOM 1122 N N . VAL A 1 140 ? -9.477 74.912 2.996 1.00 41.52 ? 140 VAL A N 1 ATOM 1123 C CA . VAL A 1 140 ? -8.075 74.644 2.699 1.00 37.94 ? 140 VAL A CA 1 ATOM 1124 C C . VAL A 1 140 ? -7.515 75.697 1.753 1.00 37.90 ? 140 VAL A C 1 ATOM 1125 O O . VAL A 1 140 ? -8.167 76.069 0.777 1.00 38.36 ? 140 VAL A O 1 ATOM 1126 C CB . VAL A 1 140 ? -7.924 73.245 2.071 1.00 37.75 ? 140 VAL A CB 1 ATOM 1127 C CG1 . VAL A 1 140 ? -6.467 72.955 1.764 1.00 35.02 ? 140 VAL A CG1 1 ATOM 1128 C CG2 . VAL A 1 140 ? -8.493 72.202 3.015 1.00 35.31 ? 140 VAL A CG2 1 ATOM 1129 N N . LYS A 1 141 ? -6.307 76.177 2.041 1.00 37.39 ? 141 LYS A N 1 ATOM 1130 C CA . LYS A 1 141 ? -5.686 77.203 1.209 1.00 38.75 ? 141 LYS A CA 1 ATOM 1131 C C . LYS A 1 141 ? -5.324 76.685 -0.177 1.00 38.92 ? 141 LYS A C 1 ATOM 1132 O O . LYS A 1 141 ? -5.128 75.487 -0.370 1.00 38.89 ? 141 LYS A O 1 ATOM 1133 C CB . LYS A 1 141 ? -4.438 77.756 1.893 1.00 40.98 ? 141 LYS A CB 1 ATOM 1134 C CG . LYS A 1 141 ? -4.707 78.490 3.197 1.00 44.35 ? 141 LYS A CG 1 ATOM 1135 C CD . LYS A 1 141 ? -3.394 78.987 3.794 1.00 50.55 ? 141 LYS A CD 1 ATOM 1136 C CE . LYS A 1 141 ? -3.588 79.616 5.169 1.00 53.26 ? 141 LYS A CE 1 ATOM 1137 N NZ . LYS A 1 141 ? -4.392 80.867 5.098 1.00 57.69 ? 141 LYS A NZ 1 ATOM 1138 N N . ASP A 1 142 ? -5.226 77.599 -1.138 1.00 38.44 ? 142 ASP A N 1 ATOM 1139 C CA . ASP A 1 142 ? -4.904 77.236 -2.512 1.00 37.87 ? 142 ASP A CA 1 ATOM 1140 C C . ASP A 1 142 ? -3.529 76.613 -2.701 1.00 37.30 ? 142 ASP A C 1 ATOM 1141 O O . ASP A 1 142 ? -3.269 75.992 -3.730 1.00 37.66 ? 142 ASP A O 1 ATOM 1142 C CB . ASP A 1 142 ? -5.019 78.454 -3.432 1.00 40.12 ? 142 ASP A CB 1 ATOM 1143 C CG . ASP A 1 142 ? -6.454 78.924 -3.612 1.00 42.48 ? 142 ASP A CG 1 ATOM 1144 O OD1 . ASP A 1 142 ? -7.393 78.122 -3.389 1.00 42.84 ? 142 ASP A OD1 1 ATOM 1145 O OD2 . ASP A 1 142 ? -6.636 80.099 -3.997 1.00 43.55 ? 142 ASP A OD2 1 ATOM 1146 N N . ASP A 1 143 ? -2.640 76.777 -1.729 1.00 34.67 ? 143 ASP A N 1 ATOM 1147 C CA . ASP A 1 143 ? -1.310 76.200 -1.865 1.00 34.29 ? 143 ASP A CA 1 ATOM 1148 C C . ASP A 1 143 ? -1.024 75.135 -0.807 1.00 32.42 ? 143 ASP A C 1 ATOM 1149 O O . ASP A 1 143 ? 0.124 74.909 -0.435 1.00 31.16 ? 143 ASP A O 1 ATOM 1150 C CB . ASP A 1 143 ? -0.246 77.301 -1.819 1.00 35.50 ? 143 ASP A CB 1 ATOM 1151 C CG . ASP A 1 143 ? -0.290 78.110 -0.535 1.00 37.58 ? 143 ASP A CG 1 ATOM 1152 O OD1 . ASP A 1 143 ? 0.635 78.920 -0.323 1.00 39.91 ? 143 ASP A OD1 1 ATOM 1153 O OD2 . ASP A 1 143 ? -1.240 77.942 0.261 1.00 38.37 ? 143 ASP A OD2 1 ATOM 1154 N N . CYS A 1 144 ? -2.082 74.478 -0.340 1.00 30.43 ? 144 CYS A N 1 ATOM 1155 C CA . CYS A 1 144 ? -1.964 73.429 0.666 1.00 29.60 ? 144 CYS A CA 1 ATOM 1156 C C . CYS A 1 144 ? -2.847 72.238 0.301 1.00 28.02 ? 144 CYS A C 1 ATOM 1157 O O . CYS A 1 144 ? -3.497 71.650 1.159 1.00 26.88 ? 144 CYS A O 1 ATOM 1158 C CB . CYS A 1 144 ? -2.373 73.969 2.040 1.00 32.06 ? 144 CYS A CB 1 ATOM 1159 S SG . CYS A 1 144 ? -1.324 75.320 2.646 1.00 37.27 ? 144 CYS A SG 1 ATOM 1160 N N . PHE A 1 145 ? -2.852 71.874 -0.974 1.00 27.93 ? 145 PHE A N 1 ATOM 1161 C CA . PHE A 1 145 ? -3.678 70.764 -1.449 1.00 28.63 ? 145 PHE A CA 1 ATOM 1162 C C . PHE A 1 145 ? -2.949 70.107 -2.629 1.00 28.60 ? 145 PHE A C 1 ATOM 1163 O O . PHE A 1 145 ? -3.067 70.563 -3.769 1.00 27.90 ? 145 PHE A O 1 ATOM 1164 C CB . PHE A 1 145 ? -5.028 71.331 -1.891 1.00 27.09 ? 145 PHE A CB 1 ATOM 1165 C CG . PHE A 1 145 ? -6.032 70.293 -2.275 1.00 28.82 ? 145 PHE A CG 1 ATOM 1166 C CD1 . PHE A 1 145 ? -6.451 69.336 -1.356 1.00 28.51 ? 145 PHE A CD1 1 ATOM 1167 C CD2 . PHE A 1 145 ? -6.594 70.294 -3.548 1.00 27.28 ? 145 PHE A CD2 1 ATOM 1168 C CE1 . PHE A 1 145 ? -7.418 68.394 -1.697 1.00 28.72 ? 145 PHE A CE1 1 ATOM 1169 C CE2 . PHE A 1 145 ? -7.560 69.357 -3.896 1.00 27.14 ? 145 PHE A CE2 1 ATOM 1170 C CZ . PHE A 1 145 ? -7.974 68.406 -2.970 1.00 26.48 ? 145 PHE A CZ 1 ATOM 1171 N N . ARG A 1 146 ? -2.208 69.032 -2.373 1.00 27.21 ? 146 ARG A N 1 ATOM 1172 C CA . ARG A 1 146 ? -1.449 68.431 -3.458 1.00 25.61 ? 146 ARG A CA 1 ATOM 1173 C C . ARG A 1 146 ? -0.991 66.988 -3.322 1.00 25.91 ? 146 ARG A C 1 ATOM 1174 O O . ARG A 1 146 ? -1.175 66.337 -2.287 1.00 25.25 ? 146 ARG A O 1 ATOM 1175 C CB . ARG A 1 146 ? -0.208 69.283 -3.711 1.00 26.83 ? 146 ARG A CB 1 ATOM 1176 C CG . ARG A 1 146 ? 0.688 69.425 -2.472 1.00 25.52 ? 146 ARG A CG 1 ATOM 1177 C CD . ARG A 1 146 ? 1.914 70.269 -2.774 1.00 28.39 ? 146 ARG A CD 1 ATOM 1178 N NE . ARG A 1 146 ? 2.710 70.572 -1.587 1.00 30.36 ? 146 ARG A NE 1 ATOM 1179 C CZ . ARG A 1 146 ? 2.368 71.457 -0.656 1.00 33.19 ? 146 ARG A CZ 1 ATOM 1180 N NH1 . ARG A 1 146 ? 1.234 72.139 -0.765 1.00 33.18 ? 146 ARG A NH1 1 ATOM 1181 N NH2 . ARG A 1 146 ? 3.167 71.671 0.383 1.00 32.22 ? 146 ARG A NH2 1 ATOM 1182 N N . ASP A 1 147 ? -0.379 66.525 -4.414 1.00 25.75 ? 147 ASP A N 1 ATOM 1183 C CA . ASP A 1 147 ? 0.213 65.199 -4.553 1.00 25.77 ? 147 ASP A CA 1 ATOM 1184 C C . ASP A 1 147 ? -0.713 63.999 -4.433 1.00 25.40 ? 147 ASP A C 1 ATOM 1185 O O . ASP A 1 147 ? -0.608 63.218 -3.484 1.00 24.37 ? 147 ASP A O 1 ATOM 1186 C CB . ASP A 1 147 ? 1.370 65.065 -3.563 1.00 25.92 ? 147 ASP A CB 1 ATOM 1187 C CG . ASP A 1 147 ? 2.313 66.255 -3.615 1.00 27.32 ? 147 ASP A CG 1 ATOM 1188 O OD1 . ASP A 1 147 ? 2.454 66.847 -4.705 1.00 28.10 ? 147 ASP A OD1 1 ATOM 1189 O OD2 . ASP A 1 147 ? 2.918 66.597 -2.574 1.00 29.14 ? 147 ASP A OD2 1 ATOM 1190 N N . PRO A 1 148 ? -1.623 63.820 -5.409 1.00 24.92 ? 148 PRO A N 1 ATOM 1191 C CA . PRO A 1 148 ? -2.548 62.682 -5.362 1.00 24.29 ? 148 PRO A CA 1 ATOM 1192 C C . PRO A 1 148 ? -1.791 61.363 -5.438 1.00 23.76 ? 148 PRO A C 1 ATOM 1193 O O . PRO A 1 148 ? -0.783 61.248 -6.133 1.00 23.80 ? 148 PRO A O 1 ATOM 1194 C CB . PRO A 1 148 ? -3.458 62.921 -6.568 1.00 24.88 ? 148 PRO A CB 1 ATOM 1195 C CG . PRO A 1 148 ? -2.578 63.666 -7.519 1.00 24.94 ? 148 PRO A CG 1 ATOM 1196 C CD . PRO A 1 148 ? -1.834 64.624 -6.626 1.00 24.17 ? 148 PRO A CD 1 ATOM 1197 N N . SER A 1 149 ? -2.280 60.375 -4.708 1.00 23.85 ? 149 SER A N 1 ATOM 1198 C CA . SER A 1 149 ? -1.657 59.061 -4.656 1.00 23.46 ? 149 SER A CA 1 ATOM 1199 C C . SER A 1 149 ? -2.206 58.114 -5.716 1.00 25.52 ? 149 SER A C 1 ATOM 1200 O O . SER A 1 149 ? -3.107 58.460 -6.487 1.00 25.98 ? 149 SER A O 1 ATOM 1201 C CB . SER A 1 149 ? -1.938 58.427 -3.303 1.00 25.15 ? 149 SER A CB 1 ATOM 1202 O OG . SER A 1 149 ? -3.309 58.045 -3.237 1.00 23.34 ? 149 SER A OG 1 ATOM 1203 N N . THR A 1 150 ? -1.646 56.910 -5.744 1.00 24.36 ? 150 THR A N 1 ATOM 1204 C CA . THR A 1 150 ? -2.119 55.875 -6.645 1.00 23.39 ? 150 THR A CA 1 ATOM 1205 C C . THR A 1 150 ? -3.477 55.504 -6.046 1.00 23.44 ? 150 THR A C 1 ATOM 1206 O O . THR A 1 150 ? -3.636 55.504 -4.825 1.00 23.43 ? 150 THR A O 1 ATOM 1207 C CB . THR A 1 150 ? -1.179 54.652 -6.619 1.00 22.89 ? 150 THR A CB 1 ATOM 1208 O OG1 . THR A 1 150 ? 0.000 54.946 -7.380 1.00 23.82 ? 150 THR A OG1 1 ATOM 1209 C CG2 . THR A 1 150 ? -1.871 53.421 -7.195 1.00 21.31 ? 150 THR A CG2 1 ATOM 1210 N N . ALA A 1 151 ? -4.454 55.203 -6.890 1.00 23.35 ? 151 ALA A N 1 ATOM 1211 C CA . ALA A 1 151 ? -5.789 54.864 -6.407 1.00 23.34 ? 151 ALA A CA 1 ATOM 1212 C C . ALA A 1 151 ? -5.963 53.383 -6.128 1.00 24.56 ? 151 ALA A C 1 ATOM 1213 O O . ALA A 1 151 ? -5.222 52.548 -6.650 1.00 25.72 ? 151 ALA A O 1 ATOM 1214 C CB . ALA A 1 151 ? -6.824 55.300 -7.424 1.00 21.16 ? 151 ALA A CB 1 ATOM 1215 N N . TRP A 1 152 ? -6.936 53.057 -5.285 1.00 24.92 ? 152 TRP A N 1 ATOM 1216 C CA . TRP A 1 152 ? -7.240 51.662 -5.012 1.00 26.65 ? 152 TRP A CA 1 ATOM 1217 C C . TRP A 1 152 ? -8.744 51.469 -5.204 1.00 28.01 ? 152 TRP A C 1 ATOM 1218 O O . TRP A 1 152 ? -9.548 52.353 -4.884 1.00 27.06 ? 152 TRP A O 1 ATOM 1219 C CB . TRP A 1 152 ? -6.757 51.228 -3.612 1.00 25.58 ? 152 TRP A CB 1 ATOM 1220 C CG . TRP A 1 152 ? -7.284 51.999 -2.442 1.00 26.38 ? 152 TRP A CG 1 ATOM 1221 C CD1 . TRP A 1 152 ? -8.325 51.645 -1.625 1.00 25.29 ? 152 TRP A CD1 1 ATOM 1222 C CD2 . TRP A 1 152 ? -6.767 53.233 -1.921 1.00 25.26 ? 152 TRP A CD2 1 ATOM 1223 N NE1 . TRP A 1 152 ? -8.482 52.579 -0.627 1.00 26.41 ? 152 TRP A NE1 1 ATOM 1224 C CE2 . TRP A 1 152 ? -7.541 53.564 -0.785 1.00 26.16 ? 152 TRP A CE2 1 ATOM 1225 C CE3 . TRP A 1 152 ? -5.725 54.089 -2.305 1.00 24.34 ? 152 TRP A CE3 1 ATOM 1226 C CZ2 . TRP A 1 152 ? -7.306 54.717 -0.027 1.00 25.64 ? 152 TRP A CZ2 1 ATOM 1227 C CZ3 . TRP A 1 152 ? -5.491 55.238 -1.554 1.00 25.15 ? 152 TRP A CZ3 1 ATOM 1228 C CH2 . TRP A 1 152 ? -6.281 55.540 -0.426 1.00 27.24 ? 152 TRP A CH2 1 ATOM 1229 N N . LEU A 1 153 ? -9.108 50.325 -5.777 1.00 30.73 ? 153 LEU A N 1 ATOM 1230 C CA . LEU A 1 153 ? -10.504 50.003 -6.060 1.00 31.78 ? 153 LEU A CA 1 ATOM 1231 C C . LEU A 1 153 ? -11.095 49.136 -4.963 1.00 33.07 ? 153 LEU A C 1 ATOM 1232 O O . LEU A 1 153 ? -10.666 47.999 -4.765 1.00 33.86 ? 153 LEU A O 1 ATOM 1233 C CB . LEU A 1 153 ? -10.600 49.274 -7.405 1.00 31.10 ? 153 LEU A CB 1 ATOM 1234 C CG . LEU A 1 153 ? -11.986 48.928 -7.957 1.00 30.85 ? 153 LEU A CG 1 ATOM 1235 C CD1 . LEU A 1 153 ? -12.770 50.206 -8.231 1.00 29.02 ? 153 LEU A CD1 1 ATOM 1236 C CD2 . LEU A 1 153 ? -11.825 48.123 -9.237 1.00 27.98 ? 153 LEU A CD2 1 ATOM 1237 N N . GLY A 1 154 ? -12.080 49.677 -4.252 1.00 35.00 ? 154 GLY A N 1 ATOM 1238 C CA . GLY A 1 154 ? -12.711 48.929 -3.179 1.00 36.72 ? 154 GLY A CA 1 ATOM 1239 C C . GLY A 1 154 ? -13.566 47.783 -3.687 1.00 39.01 ? 154 GLY A C 1 ATOM 1240 O O . GLY A 1 154 ? -13.890 47.726 -4.874 1.00 38.86 ? 154 GLY A O 1 ATOM 1241 N N . PRO A 1 155 ? -13.957 46.850 -2.806 1.00 41.07 ? 155 PRO A N 1 ATOM 1242 C CA . PRO A 1 155 ? -14.785 45.714 -3.228 1.00 41.71 ? 155 PRO A CA 1 ATOM 1243 C C . PRO A 1 155 ? -16.145 46.158 -3.786 1.00 42.05 ? 155 PRO A C 1 ATOM 1244 O O . PRO A 1 155 ? -16.828 45.393 -4.474 1.00 41.89 ? 155 PRO A O 1 ATOM 1245 C CB . PRO A 1 155 ? -14.907 44.890 -1.947 1.00 42.36 ? 155 PRO A CB 1 ATOM 1246 C CG . PRO A 1 155 ? -14.888 45.953 -0.870 1.00 43.14 ? 155 PRO A CG 1 ATOM 1247 C CD . PRO A 1 155 ? -13.773 46.860 -1.342 1.00 41.74 ? 155 PRO A CD 1 ATOM 1248 N N . ASP A 1 156 ? -16.521 47.400 -3.493 1.00 40.58 ? 156 ASP A N 1 ATOM 1249 C CA . ASP A 1 156 ? -17.785 47.962 -3.962 1.00 39.62 ? 156 ASP A CA 1 ATOM 1250 C C . ASP A 1 156 ? -17.615 48.639 -5.323 1.00 38.73 ? 156 ASP A C 1 ATOM 1251 O O . ASP A 1 156 ? -18.509 49.345 -5.794 1.00 38.87 ? 156 ASP A O 1 ATOM 1252 C CB . ASP A 1 156 ? -18.313 48.975 -2.940 1.00 39.61 ? 156 ASP A CB 1 ATOM 1253 C CG . ASP A 1 156 ? -17.334 50.115 -2.683 1.00 42.43 ? 156 ASP A CG 1 ATOM 1254 O OD1 . ASP A 1 156 ? -16.178 50.033 -3.152 1.00 41.23 ? 156 ASP A OD1 1 ATOM 1255 O OD2 . ASP A 1 156 ? -17.718 51.095 -2.005 1.00 43.47 ? 156 ASP A OD2 1 ATOM 1256 N N . GLY A 1 157 ? -16.458 48.432 -5.945 1.00 37.59 ? 157 GLY A N 1 ATOM 1257 C CA . GLY A 1 157 ? -16.199 49.030 -7.243 1.00 34.73 ? 157 GLY A CA 1 ATOM 1258 C C . GLY A 1 157 ? -15.981 50.533 -7.222 1.00 34.77 ? 157 GLY A C 1 ATOM 1259 O O . GLY A 1 157 ? -16.114 51.198 -8.254 1.00 34.13 ? 157 GLY A O 1 ATOM 1260 N N . VAL A 1 158 ? -15.651 51.080 -6.056 1.00 32.81 ? 158 VAL A N 1 ATOM 1261 C CA . VAL A 1 158 ? -15.409 52.517 -5.940 1.00 32.42 ? 158 VAL A CA 1 ATOM 1262 C C . VAL A 1 158 ? -13.919 52.796 -5.731 1.00 31.93 ? 158 VAL A C 1 ATOM 1263 O O . VAL A 1 158 ? -13.270 52.161 -4.895 1.00 31.53 ? 158 VAL A O 1 ATOM 1264 C CB . VAL A 1 158 ? -16.202 53.123 -4.766 1.00 33.37 ? 158 VAL A CB 1 ATOM 1265 C CG1 . VAL A 1 158 ? -15.920 54.613 -4.662 1.00 31.43 ? 158 VAL A CG1 1 ATOM 1266 C CG2 . VAL A 1 158 ? -17.691 52.886 -4.975 1.00 33.13 ? 158 VAL A CG2 1 ATOM 1267 N N . TRP A 1 159 ? -13.383 53.736 -6.502 1.00 30.30 ? 159 TRP A N 1 ATOM 1268 C CA . TRP A 1 159 ? -11.972 54.098 -6.408 1.00 30.65 ? 159 TRP A CA 1 ATOM 1269 C C . TRP A 1 159 ? -11.720 55.074 -5.270 1.00 30.55 ? 159 TRP A C 1 ATOM 1270 O O . TRP A 1 159 ? -12.541 55.949 -4.997 1.00 30.62 ? 159 TRP A O 1 ATOM 1271 C CB . TRP A 1 159 ? -11.482 54.771 -7.698 1.00 29.52 ? 159 TRP A CB 1 ATOM 1272 C CG . TRP A 1 159 ? -11.350 53.882 -8.892 1.00 30.41 ? 159 TRP A CG 1 ATOM 1273 C CD1 . TRP A 1 159 ? -12.211 53.795 -9.947 1.00 29.24 ? 159 TRP A CD1 1 ATOM 1274 C CD2 . TRP A 1 159 ? -10.271 52.980 -9.177 1.00 30.24 ? 159 TRP A CD2 1 ATOM 1275 N NE1 . TRP A 1 159 ? -11.734 52.899 -10.874 1.00 30.32 ? 159 TRP A NE1 1 ATOM 1276 C CE2 . TRP A 1 159 ? -10.546 52.383 -10.428 1.00 29.42 ? 159 TRP A CE2 1 ATOM 1277 C CE3 . TRP A 1 159 ? -9.099 52.620 -8.496 1.00 29.47 ? 159 TRP A CE3 1 ATOM 1278 C CZ2 . TRP A 1 159 ? -9.692 51.444 -11.016 1.00 30.06 ? 159 TRP A CZ2 1 ATOM 1279 C CZ3 . TRP A 1 159 ? -8.246 51.685 -9.081 1.00 29.79 ? 159 TRP A CZ3 1 ATOM 1280 C CH2 . TRP A 1 159 ? -8.550 51.108 -10.331 1.00 30.28 ? 159 TRP A CH2 1 ATOM 1281 N N . ARG A 1 160 ? -10.571 54.928 -4.622 1.00 30.52 ? 160 ARG A N 1 ATOM 1282 C CA . ARG A 1 160 ? -10.173 55.832 -3.551 1.00 29.93 ? 160 ARG A CA 1 ATOM 1283 C C . ARG A 1 160 ? -8.775 56.364 -3.836 1.00 30.11 ? 160 ARG A C 1 ATOM 1284 O O . ARG A 1 160 ? -7.937 55.659 -4.404 1.00 30.90 ? 160 ARG A O 1 ATOM 1285 C CB . ARG A 1 160 ? -10.123 55.119 -2.196 1.00 30.12 ? 160 ARG A CB 1 ATOM 1286 C CG . ARG A 1 160 ? -11.432 55.002 -1.445 1.00 30.68 ? 160 ARG A CG 1 ATOM 1287 C CD . ARG A 1 160 ? -12.227 53.806 -1.896 1.00 33.00 ? 160 ARG A CD 1 ATOM 1288 N NE . ARG A 1 160 ? -13.157 53.365 -0.861 1.00 34.54 ? 160 ARG A NE 1 ATOM 1289 C CZ . ARG A 1 160 ? -14.042 52.387 -1.022 1.00 36.36 ? 160 ARG A CZ 1 ATOM 1290 N NH1 . ARG A 1 160 ? -14.120 51.749 -2.183 1.00 36.99 ? 160 ARG A NH1 1 ATOM 1291 N NH2 . ARG A 1 160 ? -14.842 52.035 -0.023 1.00 36.47 ? 160 ARG A NH2 1 ATOM 1292 N N . ILE A 1 161 ? -8.539 57.615 -3.459 1.00 29.52 ? 161 ILE A N 1 ATOM 1293 C CA . ILE A 1 161 ? -7.222 58.231 -3.584 1.00 28.09 ? 161 ILE A CA 1 ATOM 1294 C C . ILE A 1 161 ? -7.116 59.208 -2.432 1.00 28.61 ? 161 ILE A C 1 ATOM 1295 O O . ILE A 1 161 ? -8.133 59.624 -1.866 1.00 28.19 ? 161 ILE A O 1 ATOM 1296 C CB . ILE A 1 161 ? -7.017 59.081 -4.873 1.00 27.71 ? 161 ILE A CB 1 ATOM 1297 C CG1 . ILE A 1 161 ? -8.005 60.248 -4.896 1.00 26.35 ? 161 ILE A CG1 1 ATOM 1298 C CG2 . ILE A 1 161 ? -7.115 58.219 -6.101 1.00 27.84 ? 161 ILE A CG2 1 ATOM 1299 C CD1 . ILE A 1 161 ? -7.714 61.258 -5.989 1.00 25.42 ? 161 ILE A CD1 1 ATOM 1300 N N . VAL A 1 162 ? -5.891 59.560 -2.065 1.00 27.04 ? 162 VAL A N 1 ATOM 1301 C CA . VAL A 1 162 ? -5.712 60.558 -1.030 1.00 27.39 ? 162 VAL A CA 1 ATOM 1302 C C . VAL A 1 162 ? -4.913 61.677 -1.660 1.00 27.00 ? 162 VAL A C 1 ATOM 1303 O O . VAL A 1 162 ? -4.108 61.452 -2.571 1.00 26.85 ? 162 VAL A O 1 ATOM 1304 C CB . VAL A 1 162 ? -4.963 60.027 0.230 1.00 27.87 ? 162 VAL A CB 1 ATOM 1305 C CG1 . VAL A 1 162 ? -5.861 59.073 0.996 1.00 27.67 ? 162 VAL A CG1 1 ATOM 1306 C CG2 . VAL A 1 162 ? -3.654 59.353 -0.163 1.00 27.10 ? 162 VAL A CG2 1 ATOM 1307 N N . VAL A 1 163 ? -5.177 62.891 -1.202 1.00 27.14 ? 163 VAL A N 1 ATOM 1308 C CA . VAL A 1 163 ? -4.467 64.061 -1.674 1.00 27.46 ? 163 VAL A CA 1 ATOM 1309 C C . VAL A 1 163 ? -3.964 64.719 -0.396 1.00 29.09 ? 163 VAL A C 1 ATOM 1310 O O . VAL A 1 163 ? -4.699 64.818 0.590 1.00 28.72 ? 163 VAL A O 1 ATOM 1311 C CB . VAL A 1 163 ? -5.398 65.029 -2.434 1.00 27.54 ? 163 VAL A CB 1 ATOM 1312 C CG1 . VAL A 1 163 ? -4.606 66.232 -2.932 1.00 25.80 ? 163 VAL A CG1 1 ATOM 1313 C CG2 . VAL A 1 163 ? -6.051 64.307 -3.601 1.00 26.49 ? 163 VAL A CG2 1 ATOM 1314 N N . GLY A 1 164 ? -2.709 65.147 -0.403 1.00 29.08 ? 164 GLY A N 1 ATOM 1315 C CA . GLY A 1 164 ? -2.160 65.765 0.783 1.00 29.89 ? 164 GLY A CA 1 ATOM 1316 C C . GLY A 1 164 ? -2.502 67.230 0.918 1.00 30.67 ? 164 GLY A C 1 ATOM 1317 O O . GLY A 1 164 ? -2.858 67.902 -0.048 1.00 30.86 ? 164 GLY A O 1 ATOM 1318 N N . GLY A 1 165 ? -2.380 67.727 2.138 1.00 32.52 ? 165 GLY A N 1 ATOM 1319 C CA . GLY A 1 165 ? -2.658 69.123 2.406 1.00 34.81 ? 165 GLY A CA 1 ATOM 1320 C C . GLY A 1 165 ? -2.732 69.318 3.900 1.00 35.01 ? 165 GLY A C 1 ATOM 1321 O O . GLY A 1 165 ? -2.184 68.519 4.663 1.00 35.41 ? 165 GLY A O 1 ATOM 1322 N N . ASP A 1 166 ? -3.394 70.385 4.323 1.00 35.44 ? 166 ASP A N 1 ATOM 1323 C CA . ASP A 1 166 ? -3.557 70.643 5.741 1.00 36.95 ? 166 ASP A CA 1 ATOM 1324 C C . ASP A 1 166 ? -4.685 71.629 5.960 1.00 37.17 ? 166 ASP A C 1 ATOM 1325 O O . ASP A 1 166 ? -4.968 72.477 5.112 1.00 36.21 ? 166 ASP A O 1 ATOM 1326 C CB . ASP A 1 166 ? -2.261 71.188 6.356 1.00 36.66 ? 166 ASP A CB 1 ATOM 1327 C CG . ASP A 1 166 ? -2.051 72.660 6.074 1.00 37.36 ? 166 ASP A CG 1 ATOM 1328 O OD1 . ASP A 1 166 ? -2.706 73.496 6.735 1.00 37.65 ? 166 ASP A OD1 1 ATOM 1329 O OD2 . ASP A 1 166 ? -1.233 72.984 5.188 1.00 37.81 ? 166 ASP A OD2 1 ATOM 1330 N N . ARG A 1 167 ? -5.340 71.489 7.102 1.00 38.74 ? 167 ARG A N 1 ATOM 1331 C CA . ARG A 1 167 ? -6.423 72.373 7.476 1.00 40.10 ? 167 ARG A CA 1 ATOM 1332 C C . ARG A 1 167 ? -5.955 73.051 8.758 1.00 40.76 ? 167 ARG A C 1 ATOM 1333 O O . ARG A 1 167 ? -5.907 72.423 9.817 1.00 40.63 ? 167 ARG A O 1 ATOM 1334 C CB . ARG A 1 167 ? -7.693 71.564 7.724 1.00 40.61 ? 167 ARG A CB 1 ATOM 1335 C CG . ARG A 1 167 ? -8.941 72.413 7.867 1.00 41.59 ? 167 ARG A CG 1 ATOM 1336 C CD . ARG A 1 167 ? -10.133 71.558 8.260 1.00 41.90 ? 167 ARG A CD 1 ATOM 1337 N NE . ARG A 1 167 ? -10.575 70.656 7.197 1.00 41.95 ? 167 ARG A NE 1 ATOM 1338 C CZ . ARG A 1 167 ? -11.129 71.058 6.056 1.00 41.68 ? 167 ARG A CZ 1 ATOM 1339 N NH1 . ARG A 1 167 ? -11.308 72.356 5.820 1.00 40.53 ? 167 ARG A NH1 1 ATOM 1340 N NH2 . ARG A 1 167 ? -11.527 70.162 5.160 1.00 39.04 ? 167 ARG A NH2 1 ATOM 1341 N N . ASP A 1 168 ? -5.582 74.324 8.650 1.00 41.27 ? 168 ASP A N 1 ATOM 1342 C CA . ASP A 1 168 ? -5.101 75.087 9.802 1.00 42.97 ? 168 ASP A CA 1 ATOM 1343 C C . ASP A 1 168 ? -3.831 74.467 10.371 1.00 43.03 ? 168 ASP A C 1 ATOM 1344 O O . ASP A 1 168 ? -3.728 74.225 11.575 1.00 42.97 ? 168 ASP A O 1 ATOM 1345 C CB . ASP A 1 168 ? -6.168 75.144 10.899 1.00 43.72 ? 168 ASP A CB 1 ATOM 1346 C CG . ASP A 1 168 ? -7.473 75.731 10.408 1.00 45.28 ? 168 ASP A CG 1 ATOM 1347 O OD1 . ASP A 1 168 ? -7.448 76.850 9.847 1.00 44.70 ? 168 ASP A OD1 1 ATOM 1348 O OD2 . ASP A 1 168 ? -8.521 75.070 10.585 1.00 46.89 ? 168 ASP A OD2 1 ATOM 1349 N N . ASN A 1 169 ? -2.874 74.209 9.486 1.00 42.43 ? 169 ASN A N 1 ATOM 1350 C CA . ASN A 1 169 ? -1.588 73.625 9.849 1.00 41.71 ? 169 ASN A CA 1 ATOM 1351 C C . ASN A 1 169 ? -1.662 72.184 10.357 1.00 40.24 ? 169 ASN A C 1 ATOM 1352 O O . ASN A 1 169 ? -0.682 71.659 10.880 1.00 39.56 ? 169 ASN A O 1 ATOM 1353 C CB . ASN A 1 169 ? -0.879 74.503 10.884 1.00 42.91 ? 169 ASN A CB 1 ATOM 1354 C CG . ASN A 1 169 ? 0.598 74.175 11.008 1.00 44.60 ? 169 ASN A CG 1 ATOM 1355 O OD1 . ASN A 1 169 ? 1.335 74.206 10.020 1.00 45.42 ? 169 ASN A OD1 1 ATOM 1356 N ND2 . ASN A 1 169 ? 1.039 73.857 12.224 1.00 45.14 ? 169 ASN A ND2 1 ATOM 1357 N N . ASN A 1 170 ? -2.819 71.543 10.208 1.00 39.20 ? 170 ASN A N 1 ATOM 1358 C CA . ASN A 1 170 ? -2.955 70.152 10.628 1.00 38.38 ? 170 ASN A CA 1 ATOM 1359 C C . ASN A 1 170 ? -2.900 69.250 9.395 1.00 38.05 ? 170 ASN A C 1 ATOM 1360 O O . ASN A 1 170 ? -3.798 69.277 8.551 1.00 37.57 ? 170 ASN A O 1 ATOM 1361 C CB . ASN A 1 170 ? -4.266 69.930 11.381 1.00 39.41 ? 170 ASN A CB 1 ATOM 1362 C CG . ASN A 1 170 ? -4.338 70.729 12.672 1.00 42.42 ? 170 ASN A CG 1 ATOM 1363 O OD1 . ASN A 1 170 ? -3.427 70.679 13.499 1.00 41.90 ? 170 ASN A OD1 1 ATOM 1364 N ND2 . ASN A 1 170 ? -5.429 71.468 12.851 1.00 42.30 ? 170 ASN A ND2 1 ATOM 1365 N N . GLY A 1 171 ? -1.828 68.468 9.299 1.00 37.37 ? 171 GLY A N 1 ATOM 1366 C CA . GLY A 1 171 ? -1.637 67.562 8.180 1.00 35.38 ? 171 GLY A CA 1 ATOM 1367 C C . GLY A 1 171 ? -2.866 66.733 7.869 1.00 35.09 ? 171 GLY A C 1 ATOM 1368 O O . GLY A 1 171 ? -3.528 66.221 8.773 1.00 34.79 ? 171 GLY A O 1 ATOM 1369 N N . MET A 1 172 ? -3.151 66.584 6.580 1.00 34.09 ? 172 MET A N 1 ATOM 1370 C CA . MET A 1 172 ? -4.323 65.848 6.127 1.00 34.36 ? 172 MET A CA 1 ATOM 1371 C C . MET A 1 172 ? -4.058 64.932 4.934 1.00 32.92 ? 172 MET A C 1 ATOM 1372 O O . MET A 1 172 ? -3.270 65.252 4.046 1.00 32.33 ? 172 MET A O 1 ATOM 1373 C CB . MET A 1 172 ? -5.418 66.832 5.687 1.00 36.04 ? 172 MET A CB 1 ATOM 1374 C CG . MET A 1 172 ? -5.961 67.769 6.741 1.00 36.44 ? 172 MET A CG 1 ATOM 1375 S SD . MET A 1 172 ? -7.232 66.971 7.706 1.00 39.78 ? 172 MET A SD 1 ATOM 1376 C CE . MET A 1 172 ? -6.764 67.447 9.374 1.00 39.49 ? 172 MET A CE 1 ATOM 1377 N N . ALA A 1 173 ? -4.740 63.795 4.919 1.00 31.23 ? 173 ALA A N 1 ATOM 1378 C CA . ALA A 1 173 ? -4.675 62.877 3.791 1.00 29.41 ? 173 ALA A CA 1 ATOM 1379 C C . ALA A 1 173 ? -6.131 62.910 3.345 1.00 28.72 ? 173 ALA A C 1 ATOM 1380 O O . ALA A 1 173 ? -6.926 62.075 3.766 1.00 29.90 ? 173 ALA A O 1 ATOM 1381 C CB . ALA A 1 173 ? -4.292 61.474 4.235 1.00 27.43 ? 173 ALA A CB 1 ATOM 1382 N N . PHE A 1 174 ? -6.490 63.904 2.538 1.00 28.21 ? 174 PHE A N 1 ATOM 1383 C CA . PHE A 1 174 ? -7.865 64.033 2.063 1.00 29.03 ? 174 PHE A CA 1 ATOM 1384 C C . PHE A 1 174 ? -8.250 62.858 1.178 1.00 29.47 ? 174 PHE A C 1 ATOM 1385 O O . PHE A 1 174 ? -7.562 62.543 0.208 1.00 30.10 ? 174 PHE A O 1 ATOM 1386 C CB . PHE A 1 174 ? -8.043 65.344 1.300 1.00 29.70 ? 174 PHE A CB 1 ATOM 1387 C CG . PHE A 1 174 ? -7.914 66.567 2.165 1.00 31.78 ? 174 PHE A CG 1 ATOM 1388 C CD1 . PHE A 1 174 ? -8.798 66.785 3.218 1.00 33.05 ? 174 PHE A CD1 1 ATOM 1389 C CD2 . PHE A 1 174 ? -6.914 67.503 1.924 1.00 32.48 ? 174 PHE A CD2 1 ATOM 1390 C CE1 . PHE A 1 174 ? -8.688 67.918 4.019 1.00 33.57 ? 174 PHE A CE1 1 ATOM 1391 C CE2 . PHE A 1 174 ? -6.794 68.642 2.719 1.00 33.29 ? 174 PHE A CE2 1 ATOM 1392 C CZ . PHE A 1 174 ? -7.683 68.850 3.768 1.00 32.83 ? 174 PHE A CZ 1 ATOM 1393 N N . LEU A 1 175 ? -9.360 62.219 1.524 1.00 28.66 ? 175 LEU A N 1 ATOM 1394 C CA . LEU A 1 175 ? -9.852 61.061 0.801 1.00 29.35 ? 175 LEU A CA 1 ATOM 1395 C C . LEU A 1 175 ? -10.933 61.417 -0.212 1.00 31.16 ? 175 LEU A C 1 ATOM 1396 O O . LEU A 1 175 ? -11.904 62.096 0.117 1.00 33.12 ? 175 LEU A O 1 ATOM 1397 C CB . LEU A 1 175 ? -10.412 60.053 1.800 1.00 29.48 ? 175 LEU A CB 1 ATOM 1398 C CG . LEU A 1 175 ? -10.979 58.741 1.258 1.00 32.25 ? 175 LEU A CG 1 ATOM 1399 C CD1 . LEU A 1 175 ? -9.859 57.893 0.677 1.00 30.93 ? 175 LEU A CD1 1 ATOM 1400 C CD2 . LEU A 1 175 ? -11.674 57.993 2.387 1.00 32.99 ? 175 LEU A CD2 1 ATOM 1401 N N . TYR A 1 176 ? -10.756 60.959 -1.448 1.00 31.38 ? 176 TYR A N 1 ATOM 1402 C CA . TYR A 1 176 ? -11.733 61.193 -2.506 1.00 30.42 ? 176 TYR A CA 1 ATOM 1403 C C . TYR A 1 176 ? -12.198 59.864 -3.085 1.00 31.36 ? 176 TYR A C 1 ATOM 1404 O O . TYR A 1 176 ? -11.455 58.878 -3.085 1.00 30.05 ? 176 TYR A O 1 ATOM 1405 C CB . TYR A 1 176 ? -11.142 62.065 -3.610 1.00 29.80 ? 176 TYR A CB 1 ATOM 1406 C CG . TYR A 1 176 ? -10.973 63.498 -3.185 1.00 31.12 ? 176 TYR A CG 1 ATOM 1407 C CD1 . TYR A 1 176 ? -9.905 63.885 -2.374 1.00 30.62 ? 176 TYR A CD1 1 ATOM 1408 C CD2 . TYR A 1 176 ? -11.918 64.460 -3.535 1.00 30.56 ? 176 TYR A CD2 1 ATOM 1409 C CE1 . TYR A 1 176 ? -9.786 65.195 -1.917 1.00 30.42 ? 176 TYR A CE1 1 ATOM 1410 C CE2 . TYR A 1 176 ? -11.809 65.772 -3.082 1.00 31.21 ? 176 TYR A CE2 1 ATOM 1411 C CZ . TYR A 1 176 ? -10.742 66.133 -2.271 1.00 31.66 ? 176 TYR A CZ 1 ATOM 1412 O OH . TYR A 1 176 ? -10.644 67.429 -1.809 1.00 33.28 ? 176 TYR A OH 1 ATOM 1413 N N . GLN A 1 177 ? -13.434 59.835 -3.569 1.00 32.07 ? 177 GLN A N 1 ATOM 1414 C CA . GLN A 1 177 ? -13.993 58.620 -4.140 1.00 33.02 ? 177 GLN A CA 1 ATOM 1415 C C . GLN A 1 177 ? -14.512 58.849 -5.551 1.00 32.79 ? 177 GLN A C 1 ATOM 1416 O O . GLN A 1 177 ? -14.910 59.963 -5.906 1.00 32.62 ? 177 GLN A O 1 ATOM 1417 C CB . GLN A 1 177 ? -15.115 58.100 -3.246 1.00 36.06 ? 177 GLN A CB 1 ATOM 1418 C CG . GLN A 1 177 ? -14.627 57.512 -1.928 1.00 41.95 ? 177 GLN A CG 1 ATOM 1419 C CD . GLN A 1 177 ? -15.751 57.325 -0.920 1.00 46.74 ? 177 GLN A CD 1 ATOM 1420 O OE1 . GLN A 1 177 ? -15.626 56.549 0.030 1.00 48.33 ? 177 GLN A OE1 1 ATOM 1421 N NE2 . GLN A 1 177 ? -16.853 58.049 -1.118 1.00 48.48 ? 177 GLN A NE2 1 ATOM 1422 N N . SER A 1 178 ? -14.505 57.787 -6.352 1.00 31.72 ? 178 SER A N 1 ATOM 1423 C CA . SER A 1 178 ? -14.969 57.860 -7.732 1.00 31.42 ? 178 SER A CA 1 ATOM 1424 C C . SER A 1 178 ? -15.191 56.478 -8.336 1.00 31.93 ? 178 SER A C 1 ATOM 1425 O O . SER A 1 178 ? -14.537 55.507 -7.948 1.00 32.54 ? 178 SER A O 1 ATOM 1426 C CB . SER A 1 178 ? -13.950 58.614 -8.581 1.00 31.63 ? 178 SER A CB 1 ATOM 1427 O OG . SER A 1 178 ? -14.348 58.657 -9.937 1.00 32.23 ? 178 SER A OG 1 ATOM 1428 N N . THR A 1 179 ? -16.121 56.392 -9.284 1.00 31.21 ? 179 THR A N 1 ATOM 1429 C CA . THR A 1 179 ? -16.406 55.129 -9.959 1.00 30.87 ? 179 THR A CA 1 ATOM 1430 C C . THR A 1 179 ? -15.870 55.173 -11.390 1.00 29.58 ? 179 THR A C 1 ATOM 1431 O O . THR A 1 179 ? -15.467 54.149 -11.934 1.00 29.96 ? 179 THR A O 1 ATOM 1432 C CB . THR A 1 179 ? -17.933 54.822 -10.015 1.00 31.18 ? 179 THR A CB 1 ATOM 1433 O OG1 . THR A 1 179 ? -18.642 56.003 -10.404 1.00 32.69 ? 179 THR A OG1 1 ATOM 1434 C CG2 . THR A 1 179 ? -18.448 54.344 -8.665 1.00 29.41 ? 179 THR A CG2 1 ATOM 1435 N N . ASP A 1 180 ? -15.845 56.359 -11.992 1.00 28.19 ? 180 ASP A N 1 ATOM 1436 C CA . ASP A 1 180 ? -15.373 56.487 -13.370 1.00 29.23 ? 180 ASP A CA 1 ATOM 1437 C C . ASP A 1 180 ? -13.981 57.101 -13.488 1.00 29.42 ? 180 ASP A C 1 ATOM 1438 O O . ASP A 1 180 ? -13.473 57.298 -14.595 1.00 28.15 ? 180 ASP A O 1 ATOM 1439 C CB . ASP A 1 180 ? -16.365 57.319 -14.188 1.00 29.57 ? 180 ASP A CB 1 ATOM 1440 C CG . ASP A 1 180 ? -16.505 58.742 -13.671 1.00 31.88 ? 180 ASP A CG 1 ATOM 1441 O OD1 . ASP A 1 180 ? -15.785 59.117 -12.718 1.00 33.04 ? 180 ASP A OD1 1 ATOM 1442 O OD2 . ASP A 1 180 ? -17.338 59.491 -14.223 1.00 33.52 ? 180 ASP A OD2 1 ATOM 1443 N N . PHE A 1 181 ? -13.380 57.405 -12.340 1.00 29.14 ? 181 PHE A N 1 ATOM 1444 C CA . PHE A 1 181 ? -12.044 57.994 -12.266 1.00 28.59 ? 181 PHE A CA 1 ATOM 1445 C C . PHE A 1 181 ? -11.990 59.423 -12.810 1.00 29.72 ? 181 PHE A C 1 ATOM 1446 O O . PHE A 1 181 ? -10.909 60.005 -12.933 1.00 29.21 ? 181 PHE A O 1 ATOM 1447 C CB . PHE A 1 181 ? -11.026 57.126 -13.021 1.00 26.40 ? 181 PHE A CB 1 ATOM 1448 C CG . PHE A 1 181 ? -9.690 57.026 -12.333 1.00 25.41 ? 181 PHE A CG 1 ATOM 1449 C CD1 . PHE A 1 181 ? -9.521 56.188 -11.231 1.00 25.47 ? 181 PHE A CD1 1 ATOM 1450 C CD2 . PHE A 1 181 ? -8.607 57.790 -12.765 1.00 24.00 ? 181 PHE A CD2 1 ATOM 1451 C CE1 . PHE A 1 181 ? -8.288 56.112 -10.568 1.00 26.50 ? 181 PHE A CE1 1 ATOM 1452 C CE2 . PHE A 1 181 ? -7.377 57.724 -12.114 1.00 22.95 ? 181 PHE A CE2 1 ATOM 1453 C CZ . PHE A 1 181 ? -7.216 56.884 -11.012 1.00 24.57 ? 181 PHE A CZ 1 ATOM 1454 N N . VAL A 1 182 ? -13.154 59.990 -13.127 1.00 30.33 ? 182 VAL A N 1 ATOM 1455 C CA . VAL A 1 182 ? -13.222 61.352 -13.659 1.00 30.18 ? 182 VAL A CA 1 ATOM 1456 C C . VAL A 1 182 ? -13.972 62.289 -12.711 1.00 31.34 ? 182 VAL A C 1 ATOM 1457 O O . VAL A 1 182 ? -13.552 63.428 -12.496 1.00 29.69 ? 182 VAL A O 1 ATOM 1458 C CB . VAL A 1 182 ? -13.890 61.365 -15.057 1.00 29.84 ? 182 VAL A CB 1 ATOM 1459 C CG1 . VAL A 1 182 ? -14.200 62.792 -15.490 1.00 29.60 ? 182 VAL A CG1 1 ATOM 1460 C CG2 . VAL A 1 182 ? -12.963 60.707 -16.071 1.00 27.89 ? 182 VAL A CG2 1 ATOM 1461 N N . ASN A 1 183 ? -15.081 61.809 -12.152 1.00 33.07 ? 183 ASN A N 1 ATOM 1462 C CA . ASN A 1 183 ? -15.865 62.599 -11.205 1.00 34.90 ? 183 ASN A CA 1 ATOM 1463 C C . ASN A 1 183 ? -15.514 62.110 -9.809 1.00 34.22 ? 183 ASN A C 1 ATOM 1464 O O . ASN A 1 183 ? -15.820 60.970 -9.447 1.00 32.96 ? 183 ASN A O 1 ATOM 1465 C CB . ASN A 1 183 ? -17.363 62.414 -11.449 1.00 39.33 ? 183 ASN A CB 1 ATOM 1466 C CG . ASN A 1 183 ? -17.783 62.867 -12.830 1.00 44.16 ? 183 ASN A CG 1 ATOM 1467 O OD1 . ASN A 1 183 ? -17.735 64.060 -13.152 1.00 46.87 ? 183 ASN A OD1 1 ATOM 1468 N ND2 . ASN A 1 183 ? -18.189 61.913 -13.664 1.00 46.48 ? 183 ASN A ND2 1 ATOM 1469 N N . TRP A 1 184 ? -14.861 62.971 -9.034 1.00 33.23 ? 184 TRP A N 1 ATOM 1470 C CA . TRP A 1 184 ? -14.454 62.621 -7.680 1.00 33.78 ? 184 TRP A CA 1 ATOM 1471 C C . TRP A 1 184 ? -15.231 63.411 -6.634 1.00 35.65 ? 184 TRP A C 1 ATOM 1472 O O . TRP A 1 184 ? -15.549 64.585 -6.839 1.00 36.53 ? 184 TRP A O 1 ATOM 1473 C CB . TRP A 1 184 ? -12.957 62.880 -7.499 1.00 32.35 ? 184 TRP A CB 1 ATOM 1474 C CG . TRP A 1 184 ? -12.091 62.070 -8.405 1.00 29.95 ? 184 TRP A CG 1 ATOM 1475 C CD1 . TRP A 1 184 ? -11.755 62.357 -9.696 1.00 29.08 ? 184 TRP A CD1 1 ATOM 1476 C CD2 . TRP A 1 184 ? -11.462 60.820 -8.095 1.00 28.66 ? 184 TRP A CD2 1 ATOM 1477 N NE1 . TRP A 1 184 ? -10.955 61.363 -10.211 1.00 28.11 ? 184 TRP A NE1 1 ATOM 1478 C CE2 . TRP A 1 184 ? -10.758 60.408 -9.249 1.00 27.29 ? 184 TRP A CE2 1 ATOM 1479 C CE3 . TRP A 1 184 ? -11.425 60.008 -6.952 1.00 27.20 ? 184 TRP A CE3 1 ATOM 1480 C CZ2 . TRP A 1 184 ? -10.024 59.221 -9.296 1.00 27.33 ? 184 TRP A CZ2 1 ATOM 1481 C CZ3 . TRP A 1 184 ? -10.696 58.827 -6.997 1.00 28.06 ? 184 TRP A CZ3 1 ATOM 1482 C CH2 . TRP A 1 184 ? -10.003 58.445 -8.165 1.00 28.80 ? 184 TRP A CH2 1 ATOM 1483 N N . LYS A 1 185 ? -15.537 62.759 -5.518 1.00 37.28 ? 185 LYS A N 1 ATOM 1484 C CA . LYS A 1 185 ? -16.272 63.394 -4.430 1.00 40.47 ? 185 LYS A CA 1 ATOM 1485 C C . LYS A 1 185 ? -15.479 63.205 -3.142 1.00 39.90 ? 185 LYS A C 1 ATOM 1486 O O . LYS A 1 185 ? -15.103 62.085 -2.795 1.00 38.88 ? 185 LYS A O 1 ATOM 1487 C CB . LYS A 1 185 ? -17.665 62.767 -4.284 1.00 43.78 ? 185 LYS A CB 1 ATOM 1488 C CG . LYS A 1 185 ? -18.449 62.703 -5.595 1.00 52.36 ? 185 LYS A CG 1 ATOM 1489 C CD . LYS A 1 185 ? -19.860 62.133 -5.420 1.00 56.80 ? 185 LYS A CD 1 ATOM 1490 C CE . LYS A 1 185 ? -20.816 63.148 -4.794 1.00 60.53 ? 185 LYS A CE 1 ATOM 1491 N NZ . LYS A 1 185 ? -21.031 64.344 -5.668 1.00 60.68 ? 185 LYS A NZ 1 ATOM 1492 N N . ARG A 1 186 ? -15.222 64.301 -2.438 1.00 40.31 ? 186 ARG A N 1 ATOM 1493 C CA . ARG A 1 186 ? -14.462 64.228 -1.198 1.00 41.64 ? 186 ARG A CA 1 ATOM 1494 C C . ARG A 1 186 ? -15.234 63.502 -0.115 1.00 41.97 ? 186 ARG A C 1 ATOM 1495 O O . ARG A 1 186 ? -16.421 63.754 0.084 1.00 43.03 ? 186 ARG A O 1 ATOM 1496 C CB . ARG A 1 186 ? -14.112 65.628 -0.695 1.00 42.97 ? 186 ARG A CB 1 ATOM 1497 C CG . ARG A 1 186 ? -13.188 65.609 0.515 1.00 47.40 ? 186 ARG A CG 1 ATOM 1498 C CD . ARG A 1 186 ? -12.807 67.007 0.988 1.00 49.94 ? 186 ARG A CD 1 ATOM 1499 N NE . ARG A 1 186 ? -13.462 67.345 2.249 1.00 54.34 ? 186 ARG A NE 1 ATOM 1500 C CZ . ARG A 1 186 ? -14.519 68.146 2.361 1.00 57.06 ? 186 ARG A CZ 1 ATOM 1501 N NH1 . ARG A 1 186 ? -15.057 68.713 1.283 1.00 58.26 ? 186 ARG A NH1 1 ATOM 1502 N NH2 . ARG A 1 186 ? -15.045 68.375 3.557 1.00 56.89 ? 186 ARG A NH2 1 ATOM 1503 N N . TYR A 1 187 ? -14.564 62.594 0.583 1.00 42.09 ? 187 TYR A N 1 ATOM 1504 C CA . TYR A 1 187 ? -15.209 61.872 1.668 1.00 42.92 ? 187 TYR A CA 1 ATOM 1505 C C . TYR A 1 187 ? -15.314 62.869 2.821 1.00 44.34 ? 187 TYR A C 1 ATOM 1506 O O . TYR A 1 187 ? -14.498 63.787 2.932 1.00 43.82 ? 187 TYR A O 1 ATOM 1507 C CB . TYR A 1 187 ? -14.372 60.667 2.094 1.00 40.82 ? 187 TYR A CB 1 ATOM 1508 C CG . TYR A 1 187 ? -15.103 59.731 3.022 1.00 39.83 ? 187 TYR A CG 1 ATOM 1509 C CD1 . TYR A 1 187 ? -16.204 59.001 2.579 1.00 39.47 ? 187 TYR A CD1 1 ATOM 1510 C CD2 . TYR A 1 187 ? -14.700 59.577 4.350 1.00 40.77 ? 187 TYR A CD2 1 ATOM 1511 C CE1 . TYR A 1 187 ? -16.891 58.136 3.436 1.00 39.87 ? 187 TYR A CE1 1 ATOM 1512 C CE2 . TYR A 1 187 ? -15.378 58.717 5.218 1.00 40.00 ? 187 TYR A CE2 1 ATOM 1513 C CZ . TYR A 1 187 ? -16.471 58.000 4.755 1.00 41.61 ? 187 TYR A CZ 1 ATOM 1514 O OH . TYR A 1 187 ? -17.140 57.149 5.609 1.00 41.37 ? 187 TYR A OH 1 ATOM 1515 N N . ASP A 1 188 ? -16.316 62.693 3.672 1.00 46.69 ? 188 ASP A N 1 ATOM 1516 C CA . ASP A 1 188 ? -16.524 63.598 4.795 1.00 49.16 ? 188 ASP A CA 1 ATOM 1517 C C . ASP A 1 188 ? -15.295 63.774 5.696 1.00 47.99 ? 188 ASP A C 1 ATOM 1518 O O . ASP A 1 188 ? -14.917 64.899 6.031 1.00 46.86 ? 188 ASP A O 1 ATOM 1519 C CB . ASP A 1 188 ? -17.717 63.123 5.624 1.00 54.20 ? 188 ASP A CB 1 ATOM 1520 C CG . ASP A 1 188 ? -18.000 64.032 6.802 1.00 60.71 ? 188 ASP A CG 1 ATOM 1521 O OD1 . ASP A 1 188 ? -18.147 65.259 6.581 1.00 62.98 ? 188 ASP A OD1 1 ATOM 1522 O OD2 . ASP A 1 188 ? -18.075 63.522 7.945 1.00 63.68 ? 188 ASP A OD2 1 ATOM 1523 N N . GLN A 1 189 ? -14.676 62.663 6.084 1.00 46.72 ? 189 GLN A N 1 ATOM 1524 C CA . GLN A 1 189 ? -13.495 62.697 6.945 1.00 46.14 ? 189 GLN A CA 1 ATOM 1525 C C . GLN A 1 189 ? -12.218 62.318 6.194 1.00 44.78 ? 189 GLN A C 1 ATOM 1526 O O . GLN A 1 189 ? -12.265 61.599 5.195 1.00 45.32 ? 189 GLN A O 1 ATOM 1527 C CB . GLN A 1 189 ? -13.682 61.739 8.127 1.00 47.17 ? 189 GLN A CB 1 ATOM 1528 C CG . GLN A 1 189 ? -14.753 62.165 9.117 1.00 51.90 ? 189 GLN A CG 1 ATOM 1529 C CD . GLN A 1 189 ? -14.435 63.500 9.774 1.00 55.30 ? 189 GLN A CD 1 ATOM 1530 O OE1 . GLN A 1 189 ? -13.382 63.666 10.393 1.00 57.42 ? 189 GLN A OE1 1 ATOM 1531 N NE2 . GLN A 1 189 ? -15.347 64.458 9.644 1.00 57.40 ? 189 GLN A NE2 1 ATOM 1532 N N . PRO A 1 190 ? -11.057 62.810 6.662 1.00 42.77 ? 190 PRO A N 1 ATOM 1533 C CA . PRO A 1 190 ? -9.766 62.509 6.032 1.00 40.25 ? 190 PRO A CA 1 ATOM 1534 C C . PRO A 1 190 ? -9.457 61.042 6.302 1.00 38.08 ? 190 PRO A C 1 ATOM 1535 O O . PRO A 1 190 ? -9.991 60.468 7.248 1.00 38.61 ? 190 PRO A O 1 ATOM 1536 C CB . PRO A 1 190 ? -8.788 63.414 6.779 1.00 39.82 ? 190 PRO A CB 1 ATOM 1537 C CG . PRO A 1 190 ? -9.641 64.509 7.306 1.00 42.54 ? 190 PRO A CG 1 ATOM 1538 C CD . PRO A 1 190 ? -10.884 63.792 7.744 1.00 41.56 ? 190 PRO A CD 1 ATOM 1539 N N . LEU A 1 191 ? -8.606 60.431 5.488 1.00 35.73 ? 191 LEU A N 1 ATOM 1540 C CA . LEU A 1 191 ? -8.260 59.036 5.723 1.00 34.41 ? 191 LEU A CA 1 ATOM 1541 C C . LEU A 1 191 ? -7.446 58.989 7.011 1.00 34.07 ? 191 LEU A C 1 ATOM 1542 O O . LEU A 1 191 ? -7.587 58.078 7.824 1.00 34.43 ? 191 LEU A O 1 ATOM 1543 C CB . LEU A 1 191 ? -7.436 58.475 4.563 1.00 33.27 ? 191 LEU A CB 1 ATOM 1544 C CG . LEU A 1 191 ? -7.009 57.016 4.742 1.00 32.31 ? 191 LEU A CG 1 ATOM 1545 C CD1 . LEU A 1 191 ? -8.237 56.145 4.949 1.00 32.77 ? 191 LEU A CD1 1 ATOM 1546 C CD2 . LEU A 1 191 ? -6.215 56.556 3.529 1.00 32.60 ? 191 LEU A CD2 1 ATOM 1547 N N . SER A 1 192 ? -6.595 59.992 7.186 1.00 34.03 ? 192 SER A N 1 ATOM 1548 C CA . SER A 1 192 ? -5.756 60.108 8.371 1.00 33.16 ? 192 SER A CA 1 ATOM 1549 C C . SER A 1 192 ? -5.314 61.565 8.469 1.00 32.72 ? 192 SER A C 1 ATOM 1550 O O . SER A 1 192 ? -5.467 62.328 7.512 1.00 31.99 ? 192 SER A O 1 ATOM 1551 C CB . SER A 1 192 ? -4.542 59.190 8.256 1.00 34.23 ? 192 SER A CB 1 ATOM 1552 O OG . SER A 1 192 ? -3.807 59.174 9.465 1.00 37.12 ? 192 SER A OG 1 ATOM 1553 N N . SER A 1 193 ? -4.779 61.953 9.622 1.00 31.91 ? 193 SER A N 1 ATOM 1554 C CA . SER A 1 193 ? -4.339 63.329 9.830 1.00 32.20 ? 193 SER A CA 1 ATOM 1555 C C . SER A 1 193 ? -3.500 63.444 11.092 1.00 32.13 ? 193 SER A C 1 ATOM 1556 O O . SER A 1 193 ? -3.371 62.488 11.850 1.00 32.33 ? 193 SER A O 1 ATOM 1557 C CB . SER A 1 193 ? -5.550 64.247 9.959 1.00 33.02 ? 193 SER A CB 1 ATOM 1558 O OG . SER A 1 193 ? -6.374 63.809 11.029 1.00 34.56 ? 193 SER A OG 1 ATOM 1559 N N . ALA A 1 194 ? -2.937 64.624 11.318 1.00 32.30 ? 194 ALA A N 1 ATOM 1560 C CA . ALA A 1 194 ? -2.114 64.857 12.496 1.00 33.46 ? 194 ALA A CA 1 ATOM 1561 C C . ALA A 1 194 ? -2.053 66.348 12.778 1.00 34.74 ? 194 ALA A C 1 ATOM 1562 O O . ALA A 1 194 ? -1.935 67.161 11.858 1.00 34.68 ? 194 ALA A O 1 ATOM 1563 C CB . ALA A 1 194 ? -0.708 64.307 12.277 1.00 31.63 ? 194 ALA A CB 1 ATOM 1564 N N . ASP A 1 195 ? -2.128 66.707 14.054 1.00 36.13 ? 195 ASP A N 1 ATOM 1565 C CA . ASP A 1 195 ? -2.087 68.108 14.447 1.00 37.43 ? 195 ASP A CA 1 ATOM 1566 C C . ASP A 1 195 ? -0.730 68.773 14.270 1.00 36.22 ? 195 ASP A C 1 ATOM 1567 O O . ASP A 1 195 ? 0.313 68.150 14.457 1.00 36.48 ? 195 ASP A O 1 ATOM 1568 C CB . ASP A 1 195 ? -2.508 68.259 15.912 1.00 41.93 ? 195 ASP A CB 1 ATOM 1569 C CG . ASP A 1 195 ? -3.999 68.072 16.118 1.00 46.44 ? 195 ASP A CG 1 ATOM 1570 O OD1 . ASP A 1 195 ? -4.427 68.031 17.292 1.00 48.87 ? 195 ASP A OD1 1 ATOM 1571 O OD2 . ASP A 1 195 ? -4.743 67.973 15.115 1.00 48.66 ? 195 ASP A OD2 1 ATOM 1572 N N . ALA A 1 196 ? -0.769 70.046 13.896 1.00 35.24 ? 196 ALA A N 1 ATOM 1573 C CA . ALA A 1 196 ? 0.419 70.880 13.745 1.00 35.57 ? 196 ALA A CA 1 ATOM 1574 C C . ALA A 1 196 ? 1.625 70.317 12.999 1.00 35.63 ? 196 ALA A C 1 ATOM 1575 O O . ALA A 1 196 ? 2.762 70.657 13.328 1.00 37.38 ? 196 ALA A O 1 ATOM 1576 C CB . ALA A 1 196 ? 0.859 71.356 15.129 1.00 33.69 ? 196 ALA A CB 1 ATOM 1577 N N . THR A 1 197 ? 1.394 69.483 11.992 1.00 35.55 ? 197 THR A N 1 ATOM 1578 C CA . THR A 1 197 ? 2.498 68.911 11.224 1.00 34.08 ? 197 THR A CA 1 ATOM 1579 C C . THR A 1 197 ? 2.786 69.719 9.964 1.00 33.35 ? 197 THR A C 1 ATOM 1580 O O . THR A 1 197 ? 3.866 69.619 9.382 1.00 32.01 ? 197 THR A O 1 ATOM 1581 C CB . THR A 1 197 ? 2.190 67.471 10.778 1.00 35.11 ? 197 THR A CB 1 ATOM 1582 O OG1 . THR A 1 197 ? 1.027 67.474 9.938 1.00 34.74 ? 197 THR A OG1 1 ATOM 1583 C CG2 . THR A 1 197 ? 1.945 66.579 11.981 1.00 34.33 ? 197 THR A CG2 1 ATOM 1584 N N . GLY A 1 198 ? 1.821 70.528 9.546 1.00 33.47 ? 198 GLY A N 1 ATOM 1585 C CA . GLY A 1 198 ? 2.001 71.290 8.325 1.00 32.82 ? 198 GLY A CA 1 ATOM 1586 C C . GLY A 1 198 ? 1.449 70.432 7.198 1.00 34.27 ? 198 GLY A C 1 ATOM 1587 O O . GLY A 1 198 ? 0.938 69.333 7.443 1.00 33.43 ? 198 GLY A O 1 ATOM 1588 N N . THR A 1 199 ? 1.553 70.911 5.963 1.00 34.85 ? 199 THR A N 1 ATOM 1589 C CA . THR A 1 199 ? 1.032 70.171 4.819 1.00 34.24 ? 199 THR A CA 1 ATOM 1590 C C . THR A 1 199 ? 1.644 68.781 4.663 1.00 32.84 ? 199 THR A C 1 ATOM 1591 O O . THR A 1 199 ? 2.858 68.606 4.759 1.00 32.52 ? 199 THR A O 1 ATOM 1592 C CB . THR A 1 199 ? 1.265 70.943 3.501 1.00 36.11 ? 199 THR A CB 1 ATOM 1593 O OG1 . THR A 1 199 ? 0.635 72.228 3.577 1.00 40.11 ? 199 THR A OG1 1 ATOM 1594 C CG2 . THR A 1 199 ? 0.679 70.179 2.326 1.00 35.95 ? 199 THR A CG2 1 ATOM 1595 N N . TRP A 1 200 ? 0.790 67.793 4.435 1.00 30.72 ? 200 TRP A N 1 ATOM 1596 C CA . TRP A 1 200 ? 1.252 66.432 4.214 1.00 29.54 ? 200 TRP A CA 1 ATOM 1597 C C . TRP A 1 200 ? 1.591 66.352 2.734 1.00 29.55 ? 200 TRP A C 1 ATOM 1598 O O . TRP A 1 200 ? 0.727 66.562 1.881 1.00 30.36 ? 200 TRP A O 1 ATOM 1599 C CB . TRP A 1 200 ? 0.151 65.430 4.560 1.00 28.18 ? 200 TRP A CB 1 ATOM 1600 C CG . TRP A 1 200 ? 0.157 65.021 5.997 1.00 26.57 ? 200 TRP A CG 1 ATOM 1601 C CD1 . TRP A 1 200 ? 0.772 65.669 7.032 1.00 25.42 ? 200 TRP A CD1 1 ATOM 1602 C CD2 . TRP A 1 200 ? -0.476 63.869 6.562 1.00 25.99 ? 200 TRP A CD2 1 ATOM 1603 N NE1 . TRP A 1 200 ? 0.562 64.987 8.208 1.00 26.36 ? 200 TRP A NE1 1 ATOM 1604 C CE2 . TRP A 1 200 ? -0.201 63.879 7.950 1.00 26.20 ? 200 TRP A CE2 1 ATOM 1605 C CE3 . TRP A 1 200 ? -1.250 62.829 6.032 1.00 25.41 ? 200 TRP A CE3 1 ATOM 1606 C CZ2 . TRP A 1 200 ? -0.672 62.887 8.816 1.00 25.59 ? 200 TRP A CZ2 1 ATOM 1607 C CZ3 . TRP A 1 200 ? -1.719 61.843 6.892 1.00 26.44 ? 200 TRP A CZ3 1 ATOM 1608 C CH2 . TRP A 1 200 ? -1.427 61.880 8.270 1.00 26.84 ? 200 TRP A CH2 1 ATOM 1609 N N . GLU A 1 201 ? 2.852 66.072 2.429 1.00 27.84 ? 201 GLU A N 1 ATOM 1610 C CA . GLU A 1 201 ? 3.282 65.990 1.045 1.00 27.86 ? 201 GLU A CA 1 ATOM 1611 C C . GLU A 1 201 ? 3.451 64.553 0.572 1.00 27.83 ? 201 GLU A C 1 ATOM 1612 O O . GLU A 1 201 ? 3.840 63.677 1.344 1.00 26.26 ? 201 GLU A O 1 ATOM 1613 C CB . GLU A 1 201 ? 4.585 66.770 0.865 1.00 27.99 ? 201 GLU A CB 1 ATOM 1614 C CG . GLU A 1 201 ? 4.406 68.265 1.093 1.00 30.45 ? 201 GLU A CG 1 ATOM 1615 C CD . GLU A 1 201 ? 5.680 69.063 0.896 1.00 30.98 ? 201 GLU A CD 1 ATOM 1616 O OE1 . GLU A 1 201 ? 5.575 70.235 0.480 1.00 33.44 ? 201 GLU A OE1 1 ATOM 1617 O OE2 . GLU A 1 201 ? 6.779 68.532 1.159 1.00 29.99 ? 201 GLU A OE2 1 ATOM 1618 N N . CYS A 1 202 ? 3.135 64.330 -0.702 1.00 27.70 ? 202 CYS A N 1 ATOM 1619 C CA . CYS A 1 202 ? 3.241 63.017 -1.340 1.00 28.24 ? 202 CYS A CA 1 ATOM 1620 C C . CYS A 1 202 ? 2.753 61.853 -0.481 1.00 26.89 ? 202 CYS A C 1 ATOM 1621 O O . CYS A 1 202 ? 3.510 60.925 -0.189 1.00 25.58 ? 202 CYS A O 1 ATOM 1622 C CB . CYS A 1 202 ? 4.687 62.769 -1.770 1.00 28.62 ? 202 CYS A CB 1 ATOM 1623 S SG . CYS A 1 202 ? 5.310 64.011 -2.937 1.00 34.87 ? 202 CYS A SG 1 ATOM 1624 N N . PRO A 1 203 ? 1.474 61.882 -0.074 1.00 26.20 ? 203 PRO A N 1 ATOM 1625 C CA . PRO A 1 203 ? 0.942 60.796 0.750 1.00 25.43 ? 203 PRO A CA 1 ATOM 1626 C C . PRO A 1 203 ? 0.942 59.516 -0.071 1.00 26.42 ? 203 PRO A C 1 ATOM 1627 O O . PRO A 1 203 ? 0.751 59.554 -1.289 1.00 26.29 ? 203 PRO A O 1 ATOM 1628 C CB . PRO A 1 203 ? -0.490 61.233 1.052 1.00 25.97 ? 203 PRO A CB 1 ATOM 1629 C CG . PRO A 1 203 ? -0.590 62.641 0.551 1.00 27.22 ? 203 PRO A CG 1 ATOM 1630 C CD . PRO A 1 203 ? 0.396 62.763 -0.543 1.00 25.36 ? 203 PRO A CD 1 ATOM 1631 N N . ASP A 1 204 ? 1.157 58.387 0.588 1.00 25.33 ? 204 ASP A N 1 ATOM 1632 C CA . ASP A 1 204 ? 1.142 57.103 -0.095 1.00 25.47 ? 204 ASP A CA 1 ATOM 1633 C C . ASP A 1 204 ? 0.364 56.211 0.854 1.00 24.75 ? 204 ASP A C 1 ATOM 1634 O O . ASP A 1 204 ? 0.540 56.295 2.071 1.00 24.53 ? 204 ASP A O 1 ATOM 1635 C CB . ASP A 1 204 ? 2.572 56.579 -0.306 1.00 25.95 ? 204 ASP A CB 1 ATOM 1636 C CG . ASP A 1 204 ? 2.667 55.564 -1.452 1.00 29.25 ? 204 ASP A CG 1 ATOM 1637 O OD1 . ASP A 1 204 ? 1.652 55.372 -2.165 1.00 28.36 ? 204 ASP A OD1 1 ATOM 1638 O OD2 . ASP A 1 204 ? 3.756 54.965 -1.647 1.00 26.45 ? 204 ASP A OD2 1 ATOM 1639 N N . PHE A 1 205 ? -0.519 55.386 0.305 1.00 24.12 ? 205 PHE A N 1 ATOM 1640 C CA . PHE A 1 205 ? -1.342 54.491 1.112 1.00 23.04 ? 205 PHE A CA 1 ATOM 1641 C C . PHE A 1 205 ? -1.439 53.163 0.377 1.00 23.85 ? 205 PHE A C 1 ATOM 1642 O O . PHE A 1 205 ? -1.962 53.093 -0.740 1.00 23.73 ? 205 PHE A O 1 ATOM 1643 C CB . PHE A 1 205 ? -2.733 55.091 1.294 1.00 23.27 ? 205 PHE A CB 1 ATOM 1644 C CG . PHE A 1 205 ? -3.576 54.369 2.297 1.00 25.75 ? 205 PHE A CG 1 ATOM 1645 C CD1 . PHE A 1 205 ? -3.274 54.436 3.652 1.00 25.45 ? 205 PHE A CD1 1 ATOM 1646 C CD2 . PHE A 1 205 ? -4.671 53.613 1.888 1.00 25.43 ? 205 PHE A CD2 1 ATOM 1647 C CE1 . PHE A 1 205 ? -4.052 53.760 4.588 1.00 26.83 ? 205 PHE A CE1 1 ATOM 1648 C CE2 . PHE A 1 205 ? -5.455 52.933 2.817 1.00 26.57 ? 205 PHE A CE2 1 ATOM 1649 C CZ . PHE A 1 205 ? -5.146 53.006 4.168 1.00 26.64 ? 205 PHE A CZ 1 ATOM 1650 N N . TYR A 1 206 ? -0.942 52.104 1.005 1.00 23.18 ? 206 TYR A N 1 ATOM 1651 C CA . TYR A 1 206 ? -0.935 50.802 0.361 1.00 22.42 ? 206 TYR A CA 1 ATOM 1652 C C . TYR A 1 206 ? -0.884 49.660 1.363 1.00 23.53 ? 206 TYR A C 1 ATOM 1653 O O . TYR A 1 206 ? -0.523 49.848 2.527 1.00 23.14 ? 206 TYR A O 1 ATOM 1654 C CB . TYR A 1 206 ? 0.281 50.716 -0.562 1.00 21.42 ? 206 TYR A CB 1 ATOM 1655 C CG . TYR A 1 206 ? 1.579 50.983 0.168 1.00 20.86 ? 206 TYR A CG 1 ATOM 1656 C CD1 . TYR A 1 206 ? 2.240 49.963 0.850 1.00 20.70 ? 206 TYR A CD1 1 ATOM 1657 C CD2 . TYR A 1 206 ? 2.127 52.268 0.210 1.00 21.38 ? 206 TYR A CD2 1 ATOM 1658 C CE1 . TYR A 1 206 ? 3.412 50.210 1.553 1.00 21.89 ? 206 TYR A CE1 1 ATOM 1659 C CE2 . TYR A 1 206 ? 3.300 52.527 0.911 1.00 21.45 ? 206 TYR A CE2 1 ATOM 1660 C CZ . TYR A 1 206 ? 3.938 51.492 1.580 1.00 22.33 ? 206 TYR A CZ 1 ATOM 1661 O OH . TYR A 1 206 ? 5.100 51.734 2.272 1.00 20.65 ? 206 TYR A OH 1 ATOM 1662 N N . PRO A 1 207 ? -1.244 48.452 0.914 1.00 23.41 ? 207 PRO A N 1 ATOM 1663 C CA . PRO A 1 207 ? -1.236 47.272 1.775 1.00 22.88 ? 207 PRO A CA 1 ATOM 1664 C C . PRO A 1 207 ? 0.069 46.493 1.658 1.00 23.41 ? 207 PRO A C 1 ATOM 1665 O O . PRO A 1 207 ? 0.766 46.575 0.646 1.00 23.64 ? 207 PRO A O 1 ATOM 1666 C CB . PRO A 1 207 ? -2.413 46.473 1.241 1.00 22.39 ? 207 PRO A CB 1 ATOM 1667 C CG . PRO A 1 207 ? -2.271 46.686 -0.240 1.00 22.53 ? 207 PRO A CG 1 ATOM 1668 C CD . PRO A 1 207 ? -1.972 48.176 -0.343 1.00 22.83 ? 207 PRO A CD 1 ATOM 1669 N N . VAL A 1 208 ? 0.393 45.748 2.707 1.00 23.67 ? 208 VAL A N 1 ATOM 1670 C CA . VAL A 1 208 ? 1.577 44.899 2.727 1.00 25.54 ? 208 VAL A CA 1 ATOM 1671 C C . VAL A 1 208 ? 1.107 43.565 3.315 1.00 26.13 ? 208 VAL A C 1 ATOM 1672 O O . VAL A 1 208 ? 0.290 43.540 4.233 1.00 25.94 ? 208 VAL A O 1 ATOM 1673 C CB . VAL A 1 208 ? 2.716 45.490 3.600 1.00 24.71 ? 208 VAL A CB 1 ATOM 1674 C CG1 . VAL A 1 208 ? 3.234 46.772 2.970 1.00 24.82 ? 208 VAL A CG1 1 ATOM 1675 C CG2 . VAL A 1 208 ? 2.219 45.753 5.016 1.00 23.02 ? 208 VAL A CG2 1 ATOM 1676 N N . PRO A 1 209 ? 1.600 42.443 2.777 1.00 27.10 ? 209 PRO A N 1 ATOM 1677 C CA . PRO A 1 209 ? 1.192 41.131 3.285 1.00 28.61 ? 209 PRO A CA 1 ATOM 1678 C C . PRO A 1 209 ? 1.936 40.711 4.549 1.00 31.45 ? 209 PRO A C 1 ATOM 1679 O O . PRO A 1 209 ? 3.164 40.817 4.622 1.00 30.30 ? 209 PRO A O 1 ATOM 1680 C CB . PRO A 1 209 ? 1.494 40.211 2.111 1.00 28.19 ? 209 PRO A CB 1 ATOM 1681 C CG . PRO A 1 209 ? 2.753 40.817 1.547 1.00 28.15 ? 209 PRO A CG 1 ATOM 1682 C CD . PRO A 1 209 ? 2.465 42.309 1.589 1.00 26.82 ? 209 PRO A CD 1 ATOM 1683 N N . LEU A 1 210 ? 1.190 40.235 5.544 1.00 34.07 ? 210 LEU A N 1 ATOM 1684 C CA . LEU A 1 210 ? 1.796 39.783 6.791 1.00 37.80 ? 210 LEU A CA 1 ATOM 1685 C C . LEU A 1 210 ? 2.570 38.490 6.555 1.00 40.39 ? 210 LEU A C 1 ATOM 1686 O O . LEU A 1 210 ? 2.171 37.650 5.742 1.00 40.39 ? 210 LEU A O 1 ATOM 1687 C CB . LEU A 1 210 ? 0.724 39.555 7.859 1.00 37.10 ? 210 LEU A CB 1 ATOM 1688 C CG . LEU A 1 210 ? -0.007 40.809 8.340 1.00 38.75 ? 210 LEU A CG 1 ATOM 1689 C CD1 . LEU A 1 210 ? -1.011 40.431 9.414 1.00 37.66 ? 210 LEU A CD1 1 ATOM 1690 C CD2 . LEU A 1 210 ? 1.001 41.818 8.881 1.00 37.07 ? 210 LEU A CD2 1 ATOM 1691 N N . ASN A 1 211 ? 3.681 38.337 7.267 1.00 43.53 ? 211 ASN A N 1 ATOM 1692 C CA . ASN A 1 211 ? 4.524 37.152 7.139 1.00 46.86 ? 211 ASN A CA 1 ATOM 1693 C C . ASN A 1 211 ? 4.813 36.823 5.676 1.00 45.40 ? 211 ASN A C 1 ATOM 1694 O O . ASN A 1 211 ? 4.513 35.726 5.202 1.00 46.25 ? 211 ASN A O 1 ATOM 1695 C CB . ASN A 1 211 ? 3.865 35.938 7.806 1.00 52.04 ? 211 ASN A CB 1 ATOM 1696 C CG . ASN A 1 211 ? 4.870 34.843 8.144 1.00 57.48 ? 211 ASN A CG 1 ATOM 1697 O OD1 . ASN A 1 211 ? 4.538 33.650 8.149 1.00 60.58 ? 211 ASN A OD1 1 ATOM 1698 N ND2 . ASN A 1 211 ? 6.107 35.247 8.443 1.00 57.62 ? 211 ASN A ND2 1 ATOM 1699 N N . SER A 1 212 ? 5.392 37.784 4.966 1.00 43.49 ? 212 SER A N 1 ATOM 1700 C CA . SER A 1 212 ? 5.742 37.612 3.562 1.00 40.02 ? 212 SER A CA 1 ATOM 1701 C C . SER A 1 212 ? 6.693 38.732 3.176 1.00 38.80 ? 212 SER A C 1 ATOM 1702 O O . SER A 1 212 ? 6.658 39.809 3.767 1.00 38.63 ? 212 SER A O 1 ATOM 1703 C CB . SER A 1 212 ? 4.487 37.674 2.684 1.00 40.11 ? 212 SER A CB 1 ATOM 1704 O OG . SER A 1 212 ? 4.816 37.621 1.302 1.00 38.45 ? 212 SER A OG 1 ATOM 1705 N N . THR A 1 213 ? 7.550 38.475 2.196 1.00 36.84 ? 213 THR A N 1 ATOM 1706 C CA . THR A 1 213 ? 8.490 39.488 1.736 1.00 35.66 ? 213 THR A CA 1 ATOM 1707 C C . THR A 1 213 ? 8.030 40.002 0.379 1.00 35.09 ? 213 THR A C 1 ATOM 1708 O O . THR A 1 213 ? 8.757 40.713 -0.310 1.00 36.42 ? 213 THR A O 1 ATOM 1709 C CB . THR A 1 213 ? 9.905 38.913 1.589 1.00 36.22 ? 213 THR A CB 1 ATOM 1710 O OG1 . THR A 1 213 ? 9.901 37.881 0.593 1.00 38.08 ? 213 THR A OG1 1 ATOM 1711 C CG2 . THR A 1 213 ? 10.379 38.339 2.917 1.00 35.78 ? 213 THR A CG2 1 ATOM 1712 N N . ASN A 1 214 ? 6.813 39.639 0.000 1.00 33.85 ? 214 ASN A N 1 ATOM 1713 C CA . ASN A 1 214 ? 6.262 40.058 -1.278 1.00 34.31 ? 214 ASN A CA 1 ATOM 1714 C C . ASN A 1 214 ? 5.530 41.389 -1.210 1.00 32.83 ? 214 ASN A C 1 ATOM 1715 O O . ASN A 1 214 ? 5.367 41.976 -0.141 1.00 31.19 ? 214 ASN A O 1 ATOM 1716 C CB . ASN A 1 214 ? 5.307 38.988 -1.807 1.00 36.90 ? 214 ASN A CB 1 ATOM 1717 C CG . ASN A 1 214 ? 6.030 37.737 -2.269 1.00 40.83 ? 214 ASN A CG 1 ATOM 1718 O OD1 . ASN A 1 214 ? 5.406 36.699 -2.477 1.00 43.55 ? 214 ASN A OD1 1 ATOM 1719 N ND2 . ASN A 1 214 ? 7.350 37.831 -2.442 1.00 40.46 ? 214 ASN A ND2 1 ATOM 1720 N N . GLY A 1 215 ? 5.102 41.858 -2.377 1.00 31.65 ? 215 GLY A N 1 ATOM 1721 C CA . GLY A 1 215 ? 4.366 43.100 -2.462 1.00 30.89 ? 215 GLY A CA 1 ATOM 1722 C C . GLY A 1 215 ? 2.943 42.772 -2.862 1.00 31.20 ? 215 GLY A C 1 ATOM 1723 O O . GLY A 1 215 ? 2.657 41.655 -3.297 1.00 31.04 ? 215 GLY A O 1 ATOM 1724 N N . LEU A 1 216 ? 2.041 43.734 -2.714 1.00 30.75 ? 216 LEU A N 1 ATOM 1725 C CA . LEU A 1 216 ? 0.650 43.510 -3.076 1.00 29.42 ? 216 LEU A CA 1 ATOM 1726 C C . LEU A 1 216 ? 0.127 44.620 -3.953 1.00 29.84 ? 216 LEU A C 1 ATOM 1727 O O . LEU A 1 216 ? 0.587 45.758 -3.872 1.00 30.03 ? 216 LEU A O 1 ATOM 1728 C CB . LEU A 1 216 ? -0.227 43.433 -1.827 1.00 27.97 ? 216 LEU A CB 1 ATOM 1729 C CG . LEU A 1 216 ? -0.062 42.207 -0.935 1.00 29.67 ? 216 LEU A CG 1 ATOM 1730 C CD1 . LEU A 1 216 ? -0.860 42.422 0.337 1.00 28.48 ? 216 LEU A CD1 1 ATOM 1731 C CD2 . LEU A 1 216 ? -0.524 40.951 -1.676 1.00 27.42 ? 216 LEU A CD2 1 ATOM 1732 N N . ASP A 1 217 ? -0.829 44.281 -4.807 1.00 30.54 ? 217 ASP A N 1 ATOM 1733 C CA . ASP A 1 217 ? -1.452 45.283 -5.649 1.00 31.09 ? 217 ASP A CA 1 ATOM 1734 C C . ASP A 1 217 ? -2.091 46.225 -4.630 1.00 29.76 ? 217 ASP A C 1 ATOM 1735 O O . ASP A 1 217 ? -2.501 45.790 -3.556 1.00 29.19 ? 217 ASP A O 1 ATOM 1736 C CB . ASP A 1 217 ? -2.540 44.650 -6.516 1.00 33.05 ? 217 ASP A CB 1 ATOM 1737 C CG . ASP A 1 217 ? -3.280 45.676 -7.351 1.00 35.91 ? 217 ASP A CG 1 ATOM 1738 O OD1 . ASP A 1 217 ? -2.677 46.201 -8.316 1.00 37.65 ? 217 ASP A OD1 1 ATOM 1739 O OD2 . ASP A 1 217 ? -4.455 45.969 -7.031 1.00 35.73 ? 217 ASP A OD2 1 ATOM 1740 N N . THR A 1 218 ? -2.193 47.503 -4.961 1.00 30.33 ? 218 THR A N 1 ATOM 1741 C CA . THR A 1 218 ? -2.764 48.476 -4.035 1.00 32.07 ? 218 THR A CA 1 ATOM 1742 C C . THR A 1 218 ? -4.197 48.188 -3.580 1.00 32.02 ? 218 THR A C 1 ATOM 1743 O O . THR A 1 218 ? -4.598 48.617 -2.501 1.00 31.82 ? 218 THR A O 1 ATOM 1744 C CB . THR A 1 218 ? -2.733 49.886 -4.643 1.00 32.51 ? 218 THR A CB 1 ATOM 1745 O OG1 . THR A 1 218 ? -1.459 50.107 -5.257 1.00 35.71 ? 218 THR A OG1 1 ATOM 1746 C CG2 . THR A 1 218 ? -2.936 50.935 -3.564 1.00 31.10 ? 218 THR A CG2 1 ATOM 1747 N N . SER A 1 219 ? -4.958 47.452 -4.387 1.00 32.32 ? 219 SER A N 1 ATOM 1748 C CA . SER A 1 219 ? -6.352 47.161 -4.064 1.00 33.43 ? 219 SER A CA 1 ATOM 1749 C C . SER A 1 219 ? -6.638 45.937 -3.189 1.00 35.96 ? 219 SER A C 1 ATOM 1750 O O . SER A 1 219 ? -7.801 45.607 -2.947 1.00 38.47 ? 219 SER A O 1 ATOM 1751 C CB . SER A 1 219 ? -7.166 47.053 -5.357 1.00 32.06 ? 219 SER A CB 1 ATOM 1752 O OG . SER A 1 219 ? -7.118 48.265 -6.095 1.00 29.10 ? 219 SER A OG 1 ATOM 1753 N N . VAL A 1 220 ? -5.599 45.267 -2.706 1.00 36.74 ? 220 VAL A N 1 ATOM 1754 C CA . VAL A 1 220 ? -5.801 44.098 -1.859 1.00 37.73 ? 220 VAL A CA 1 ATOM 1755 C C . VAL A 1 220 ? -6.167 44.508 -0.436 1.00 41.00 ? 220 VAL A C 1 ATOM 1756 O O . VAL A 1 220 ? -5.676 45.510 0.079 1.00 42.23 ? 220 VAL A O 1 ATOM 1757 C CB . VAL A 1 220 ? -4.539 43.224 -1.810 1.00 36.90 ? 220 VAL A CB 1 ATOM 1758 C CG1 . VAL A 1 220 ? -4.776 42.010 -0.923 1.00 34.21 ? 220 VAL A CG1 1 ATOM 1759 C CG2 . VAL A 1 220 ? -4.159 42.796 -3.214 1.00 36.06 ? 220 VAL A CG2 1 ATOM 1760 N N . TYR A 1 221 ? -7.043 43.736 0.192 1.00 43.89 ? 221 TYR A N 1 ATOM 1761 C CA . TYR A 1 221 ? -7.464 44.010 1.561 1.00 47.83 ? 221 TYR A CA 1 ATOM 1762 C C . TYR A 1 221 ? -7.717 42.668 2.244 1.00 47.29 ? 221 TYR A C 1 ATOM 1763 O O . TYR A 1 221 ? -7.766 41.630 1.583 1.00 48.01 ? 221 TYR A O 1 ATOM 1764 C CB . TYR A 1 221 ? -8.739 44.868 1.573 1.00 53.43 ? 221 TYR A CB 1 ATOM 1765 C CG . TYR A 1 221 ? -9.946 44.180 0.976 1.00 61.57 ? 221 TYR A CG 1 ATOM 1766 C CD1 . TYR A 1 221 ? -11.164 44.135 1.666 1.00 64.46 ? 221 TYR A CD1 1 ATOM 1767 C CD2 . TYR A 1 221 ? -9.867 43.539 -0.266 1.00 64.83 ? 221 TYR A CD2 1 ATOM 1768 C CE1 . TYR A 1 221 ? -12.273 43.460 1.132 1.00 66.62 ? 221 TYR A CE1 1 ATOM 1769 C CE2 . TYR A 1 221 ? -10.965 42.865 -0.807 1.00 67.10 ? 221 TYR A CE2 1 ATOM 1770 C CZ . TYR A 1 221 ? -12.161 42.827 -0.104 1.00 67.96 ? 221 TYR A CZ 1 ATOM 1771 O OH . TYR A 1 221 ? -13.231 42.142 -0.638 1.00 69.48 ? 221 TYR A OH 1 ATOM 1772 N N . GLY A 1 222 ? -7.868 42.674 3.561 1.00 47.00 ? 222 GLY A N 1 ATOM 1773 C CA . GLY A 1 222 ? -8.105 41.419 4.249 1.00 46.51 ? 222 GLY A CA 1 ATOM 1774 C C . GLY A 1 222 ? -7.442 41.351 5.605 1.00 46.16 ? 222 GLY A C 1 ATOM 1775 O O . GLY A 1 222 ? -6.721 42.266 5.999 1.00 46.73 ? 222 GLY A O 1 ATOM 1776 N N . GLY A 1 223 ? -7.680 40.255 6.315 1.00 45.67 ? 223 GLY A N 1 ATOM 1777 C CA . GLY A 1 223 ? -7.112 40.093 7.641 1.00 44.99 ? 223 GLY A CA 1 ATOM 1778 C C . GLY A 1 223 ? -5.629 39.792 7.657 1.00 44.46 ? 223 GLY A C 1 ATOM 1779 O O . GLY A 1 223 ? -4.944 40.092 8.631 1.00 45.39 ? 223 GLY A O 1 ATOM 1780 N N . SER A 1 224 ? -5.133 39.195 6.582 1.00 43.94 ? 224 SER A N 1 ATOM 1781 C CA . SER A 1 224 ? -3.717 38.857 6.481 1.00 45.18 ? 224 SER A CA 1 ATOM 1782 C C . SER A 1 224 ? -2.961 40.009 5.822 1.00 43.54 ? 224 SER A C 1 ATOM 1783 O O . SER A 1 224 ? -1.873 39.827 5.268 1.00 43.20 ? 224 SER A O 1 ATOM 1784 C CB . SER A 1 224 ? -3.550 37.592 5.643 1.00 46.92 ? 224 SER A CB 1 ATOM 1785 O OG . SER A 1 224 ? -4.171 37.763 4.378 1.00 50.69 ? 224 SER A OG 1 ATOM 1786 N N . VAL A 1 225 ? -3.550 41.196 5.896 1.00 41.42 ? 225 VAL A N 1 ATOM 1787 C CA . VAL A 1 225 ? -2.968 42.384 5.297 1.00 39.36 ? 225 VAL A CA 1 ATOM 1788 C C . VAL A 1 225 ? -3.051 43.600 6.213 1.00 38.70 ? 225 VAL A C 1 ATOM 1789 O O . VAL A 1 225 ? -4.043 43.803 6.917 1.00 39.26 ? 225 VAL A O 1 ATOM 1790 C CB . VAL A 1 225 ? -3.691 42.727 3.970 1.00 39.30 ? 225 VAL A CB 1 ATOM 1791 C CG1 . VAL A 1 225 ? -3.225 44.064 3.445 1.00 37.60 ? 225 VAL A CG1 1 ATOM 1792 C CG2 . VAL A 1 225 ? -3.437 41.639 2.945 1.00 39.36 ? 225 VAL A CG2 1 ATOM 1793 N N . ARG A 1 226 ? -1.996 44.405 6.199 1.00 36.22 ? 226 ARG A N 1 ATOM 1794 C CA . ARG A 1 226 ? -1.960 45.629 6.981 1.00 34.07 ? 226 ARG A CA 1 ATOM 1795 C C . ARG A 1 226 ? -1.684 46.753 5.996 1.00 32.46 ? 226 ARG A C 1 ATOM 1796 O O . ARG A 1 226 ? -1.104 46.518 4.933 1.00 31.75 ? 226 ARG A O 1 ATOM 1797 C CB . ARG A 1 226 ? -0.862 45.563 8.043 1.00 35.00 ? 226 ARG A CB 1 ATOM 1798 C CG . ARG A 1 226 ? -1.207 44.651 9.204 1.00 37.21 ? 226 ARG A CG 1 ATOM 1799 C CD . ARG A 1 226 ? -2.457 45.138 9.926 1.00 40.44 ? 226 ARG A CD 1 ATOM 1800 N NE . ARG A 1 226 ? -2.835 44.247 11.020 1.00 43.21 ? 226 ARG A NE 1 ATOM 1801 C CZ . ARG A 1 226 ? -3.415 43.060 10.859 1.00 44.19 ? 226 ARG A CZ 1 ATOM 1802 N NH1 . ARG A 1 226 ? -3.702 42.607 9.645 1.00 42.80 ? 226 ARG A NH1 1 ATOM 1803 N NH2 . ARG A 1 226 ? -3.693 42.315 11.920 1.00 44.95 ? 226 ARG A NH2 1 ATOM 1804 N N . HIS A 1 227 ? -2.112 47.965 6.333 1.00 29.51 ? 227 HIS A N 1 ATOM 1805 C CA . HIS A 1 227 ? -1.896 49.097 5.448 1.00 28.07 ? 227 HIS A CA 1 ATOM 1806 C C . HIS A 1 227 ? -0.888 50.089 5.994 1.00 27.91 ? 227 HIS A C 1 ATOM 1807 O O . HIS A 1 227 ? -0.727 50.242 7.213 1.00 26.96 ? 227 HIS A O 1 ATOM 1808 C CB . HIS A 1 227 ? -3.218 49.815 5.152 1.00 27.84 ? 227 HIS A CB 1 ATOM 1809 C CG . HIS A 1 227 ? -4.018 49.178 4.058 1.00 29.14 ? 227 HIS A CG 1 ATOM 1810 N ND1 . HIS A 1 227 ? -4.577 47.922 4.176 1.00 28.21 ? 227 HIS A ND1 1 ATOM 1811 C CD2 . HIS A 1 227 ? -4.324 49.610 2.811 1.00 28.74 ? 227 HIS A CD2 1 ATOM 1812 C CE1 . HIS A 1 227 ? -5.191 47.609 3.049 1.00 28.59 ? 227 HIS A CE1 1 ATOM 1813 N NE2 . HIS A 1 227 ? -5.053 48.616 2.204 1.00 29.60 ? 227 HIS A NE2 1 ATOM 1814 N N . VAL A 1 228 ? -0.200 50.755 5.073 1.00 25.71 ? 228 VAL A N 1 ATOM 1815 C CA . VAL A 1 228 ? 0.795 51.746 5.426 1.00 24.89 ? 228 VAL A CA 1 ATOM 1816 C C . VAL A 1 228 ? 0.318 53.123 4.992 1.00 25.91 ? 228 VAL A C 1 ATOM 1817 O O . VAL A 1 228 ? -0.067 53.319 3.837 1.00 27.87 ? 228 VAL A O 1 ATOM 1818 C CB . VAL A 1 228 ? 2.139 51.456 4.729 1.00 24.93 ? 228 VAL A CB 1 ATOM 1819 C CG1 . VAL A 1 228 ? 3.154 52.540 5.075 1.00 22.85 ? 228 VAL A CG1 1 ATOM 1820 C CG2 . VAL A 1 228 ? 2.649 50.083 5.139 1.00 24.43 ? 228 VAL A CG2 1 ATOM 1821 N N . MET A 1 229 ? 0.320 54.067 5.925 1.00 25.74 ? 229 MET A N 1 ATOM 1822 C CA . MET A 1 229 ? -0.063 55.443 5.629 1.00 25.54 ? 229 MET A CA 1 ATOM 1823 C C . MET A 1 229 ? 1.252 56.205 5.712 1.00 26.36 ? 229 MET A C 1 ATOM 1824 O O . MET A 1 229 ? 1.870 56.275 6.780 1.00 26.74 ? 229 MET A O 1 ATOM 1825 C CB . MET A 1 229 ? -1.041 55.981 6.677 1.00 26.43 ? 229 MET A CB 1 ATOM 1826 C CG . MET A 1 229 ? -1.344 57.479 6.557 1.00 28.37 ? 229 MET A CG 1 ATOM 1827 S SD . MET A 1 229 ? -2.399 57.938 5.147 1.00 34.82 ? 229 MET A SD 1 ATOM 1828 C CE . MET A 1 229 ? -1.184 58.566 3.982 1.00 30.25 ? 229 MET A CE 1 ATOM 1829 N N . LYS A 1 230 ? 1.690 56.753 4.586 1.00 24.92 ? 230 LYS A N 1 ATOM 1830 C CA . LYS A 1 230 ? 2.941 57.493 4.538 1.00 23.61 ? 230 LYS A CA 1 ATOM 1831 C C . LYS A 1 230 ? 2.706 58.931 4.100 1.00 24.31 ? 230 LYS A C 1 ATOM 1832 O O . LYS A 1 230 ? 1.871 59.197 3.236 1.00 25.15 ? 230 LYS A O 1 ATOM 1833 C CB . LYS A 1 230 ? 3.914 56.802 3.575 1.00 22.32 ? 230 LYS A CB 1 ATOM 1834 C CG . LYS A 1 230 ? 5.178 57.586 3.271 1.00 21.55 ? 230 LYS A CG 1 ATOM 1835 C CD . LYS A 1 230 ? 4.965 58.579 2.144 1.00 22.38 ? 230 LYS A CD 1 ATOM 1836 C CE . LYS A 1 230 ? 6.213 59.414 1.907 1.00 23.87 ? 230 LYS A CE 1 ATOM 1837 N NZ . LYS A 1 230 ? 6.020 60.364 0.775 1.00 23.74 ? 230 LYS A NZ 1 ATOM 1838 N N . ALA A 1 231 ? 3.436 59.858 4.706 1.00 23.35 ? 231 ALA A N 1 ATOM 1839 C CA . ALA A 1 231 ? 3.312 61.267 4.350 1.00 24.59 ? 231 ALA A CA 1 ATOM 1840 C C . ALA A 1 231 ? 4.601 61.990 4.686 1.00 24.75 ? 231 ALA A C 1 ATOM 1841 O O . ALA A 1 231 ? 5.319 61.609 5.617 1.00 24.71 ? 231 ALA A O 1 ATOM 1842 C CB . ALA A 1 231 ? 2.145 61.912 5.097 1.00 22.91 ? 231 ALA A CB 1 ATOM 1843 N N . GLY A 1 232 ? 4.898 63.025 3.912 1.00 24.30 ? 232 GLY A N 1 ATOM 1844 C CA . GLY A 1 232 ? 6.089 63.804 4.159 1.00 24.33 ? 232 GLY A CA 1 ATOM 1845 C C . GLY A 1 232 ? 5.710 65.120 4.816 1.00 26.54 ? 232 GLY A C 1 ATOM 1846 O O . GLY A 1 232 ? 4.741 65.769 4.417 1.00 24.88 ? 232 GLY A O 1 ATOM 1847 N N . PHE A 1 233 ? 6.446 65.495 5.854 1.00 27.10 ? 233 PHE A N 1 ATOM 1848 C CA . PHE A 1 233 ? 6.220 66.761 6.540 1.00 28.80 ? 233 PHE A CA 1 ATOM 1849 C C . PHE A 1 233 ? 7.373 67.037 7.496 1.00 29.67 ? 233 PHE A C 1 ATOM 1850 O O . PHE A 1 233 ? 8.059 66.115 7.950 1.00 28.27 ? 233 PHE A O 1 ATOM 1851 C CB . PHE A 1 233 ? 4.860 66.781 7.265 1.00 29.23 ? 233 PHE A CB 1 ATOM 1852 C CG . PHE A 1 233 ? 4.713 65.754 8.352 1.00 29.52 ? 233 PHE A CG 1 ATOM 1853 C CD1 . PHE A 1 233 ? 5.277 65.960 9.606 1.00 29.67 ? 233 PHE A CD1 1 ATOM 1854 C CD2 . PHE A 1 233 ? 3.994 64.586 8.124 1.00 30.50 ? 233 PHE A CD2 1 ATOM 1855 C CE1 . PHE A 1 233 ? 5.125 65.017 10.620 1.00 29.53 ? 233 PHE A CE1 1 ATOM 1856 C CE2 . PHE A 1 233 ? 3.836 63.637 9.129 1.00 30.75 ? 233 PHE A CE2 1 ATOM 1857 C CZ . PHE A 1 233 ? 4.405 63.855 10.382 1.00 29.92 ? 233 PHE A CZ 1 ATOM 1858 N N . GLU A 1 234 ? 7.593 68.318 7.772 1.00 29.34 ? 234 GLU A N 1 ATOM 1859 C CA . GLU A 1 234 ? 8.674 68.753 8.641 1.00 29.77 ? 234 GLU A CA 1 ATOM 1860 C C . GLU A 1 234 ? 10.017 68.242 8.130 1.00 28.75 ? 234 GLU A C 1 ATOM 1861 O O . GLU A 1 234 ? 10.920 67.931 8.904 1.00 29.59 ? 234 GLU A O 1 ATOM 1862 C CB . GLU A 1 234 ? 8.412 68.311 10.084 1.00 30.65 ? 234 GLU A CB 1 ATOM 1863 C CG . GLU A 1 234 ? 7.080 68.849 10.586 1.00 34.77 ? 234 GLU A CG 1 ATOM 1864 C CD . GLU A 1 234 ? 6.862 68.667 12.069 1.00 36.30 ? 234 GLU A CD 1 ATOM 1865 O OE1 . GLU A 1 234 ? 7.180 67.584 12.601 1.00 38.73 ? 234 GLU A OE1 1 ATOM 1866 O OE2 . GLU A 1 234 ? 6.349 69.609 12.703 1.00 39.16 ? 234 GLU A OE2 1 ATOM 1867 N N . GLY A 1 235 ? 10.125 68.155 6.807 1.00 28.37 ? 235 GLY A N 1 ATOM 1868 C CA . GLY A 1 235 ? 11.363 67.736 6.173 1.00 27.49 ? 235 GLY A CA 1 ATOM 1869 C C . GLY A 1 235 ? 11.670 66.263 5.991 1.00 27.32 ? 235 GLY A C 1 ATOM 1870 O O . GLY A 1 235 ? 12.705 65.929 5.412 1.00 28.28 ? 235 GLY A O 1 ATOM 1871 N N . HIS A 1 236 ? 10.795 65.378 6.458 1.00 26.64 ? 236 HIS A N 1 ATOM 1872 C CA . HIS A 1 236 ? 11.053 63.947 6.323 1.00 25.29 ? 236 HIS A CA 1 ATOM 1873 C C . HIS A 1 236 ? 9.839 63.134 5.923 1.00 25.35 ? 236 HIS A C 1 ATOM 1874 O O . HIS A 1 236 ? 8.711 63.619 5.960 1.00 26.98 ? 236 HIS A O 1 ATOM 1875 C CB . HIS A 1 236 ? 11.599 63.396 7.637 1.00 22.74 ? 236 HIS A CB 1 ATOM 1876 C CG . HIS A 1 236 ? 12.854 64.066 8.087 1.00 25.89 ? 236 HIS A CG 1 ATOM 1877 N ND1 . HIS A 1 236 ? 12.954 64.731 9.292 1.00 27.31 ? 236 HIS A ND1 1 ATOM 1878 C CD2 . HIS A 1 236 ? 14.055 64.206 7.478 1.00 24.86 ? 236 HIS A CD2 1 ATOM 1879 C CE1 . HIS A 1 236 ? 14.162 65.253 9.404 1.00 24.61 ? 236 HIS A CE1 1 ATOM 1880 N NE2 . HIS A 1 236 ? 14.849 64.949 8.317 1.00 25.92 ? 236 HIS A NE2 1 ATOM 1881 N N . ASP A 1 237 ? 10.086 61.888 5.537 1.00 24.81 ? 237 ASP A N 1 ATOM 1882 C CA . ASP A 1 237 ? 9.015 60.980 5.160 1.00 24.51 ? 237 ASP A CA 1 ATOM 1883 C C . ASP A 1 237 ? 8.720 60.061 6.343 1.00 24.67 ? 237 ASP A C 1 ATOM 1884 O O . ASP A 1 237 ? 9.597 59.329 6.811 1.00 24.77 ? 237 ASP A O 1 ATOM 1885 C CB . ASP A 1 237 ? 9.419 60.153 3.940 1.00 24.48 ? 237 ASP A CB 1 ATOM 1886 C CG . ASP A 1 237 ? 9.298 60.932 2.637 1.00 28.84 ? 237 ASP A CG 1 ATOM 1887 O OD1 . ASP A 1 237 ? 8.827 62.094 2.669 1.00 28.57 ? 237 ASP A OD1 1 ATOM 1888 O OD2 . ASP A 1 237 ? 9.667 60.376 1.576 1.00 29.15 ? 237 ASP A OD2 1 ATOM 1889 N N . TRP A 1 238 ? 7.487 60.111 6.833 1.00 24.18 ? 238 TRP A N 1 ATOM 1890 C CA . TRP A 1 238 ? 7.088 59.283 7.965 1.00 24.75 ? 238 TRP A CA 1 ATOM 1891 C C . TRP A 1 238 ? 6.035 58.299 7.508 1.00 24.74 ? 238 TRP A C 1 ATOM 1892 O O . TRP A 1 238 ? 5.393 58.505 6.481 1.00 26.18 ? 238 TRP A O 1 ATOM 1893 C CB . TRP A 1 238 ? 6.485 60.143 9.087 1.00 24.36 ? 238 TRP A CB 1 ATOM 1894 C CG . TRP A 1 238 ? 7.227 61.409 9.342 1.00 23.77 ? 238 TRP A CG 1 ATOM 1895 C CD1 . TRP A 1 238 ? 7.132 62.575 8.634 1.00 23.08 ? 238 TRP A CD1 1 ATOM 1896 C CD2 . TRP A 1 238 ? 8.237 61.621 10.335 1.00 22.53 ? 238 TRP A CD2 1 ATOM 1897 N NE1 . TRP A 1 238 ? 8.027 63.498 9.122 1.00 24.38 ? 238 TRP A NE1 1 ATOM 1898 C CE2 . TRP A 1 238 ? 8.718 62.937 10.166 1.00 22.98 ? 238 TRP A CE2 1 ATOM 1899 C CE3 . TRP A 1 238 ? 8.784 60.823 11.350 1.00 22.81 ? 238 TRP A CE3 1 ATOM 1900 C CZ2 . TRP A 1 238 ? 9.726 63.477 10.975 1.00 21.56 ? 238 TRP A CZ2 1 ATOM 1901 C CZ3 . TRP A 1 238 ? 9.789 61.363 12.156 1.00 22.64 ? 238 TRP A CZ3 1 ATOM 1902 C CH2 . TRP A 1 238 ? 10.246 62.679 11.958 1.00 19.75 ? 238 TRP A CH2 1 ATOM 1903 N N . TYR A 1 239 ? 5.861 57.224 8.264 1.00 23.79 ? 239 TYR A N 1 ATOM 1904 C CA . TYR A 1 239 ? 4.831 56.256 7.929 1.00 24.44 ? 239 TYR A CA 1 ATOM 1905 C C . TYR A 1 239 ? 4.398 55.551 9.199 1.00 24.98 ? 239 TYR A C 1 ATOM 1906 O O . TYR A 1 239 ? 5.108 55.556 10.201 1.00 25.44 ? 239 TYR A O 1 ATOM 1907 C CB . TYR A 1 239 ? 5.325 55.238 6.880 1.00 21.11 ? 239 TYR A CB 1 ATOM 1908 C CG . TYR A 1 239 ? 6.259 54.168 7.399 1.00 20.41 ? 239 TYR A CG 1 ATOM 1909 C CD1 . TYR A 1 239 ? 5.772 53.069 8.107 1.00 20.64 ? 239 TYR A CD1 1 ATOM 1910 C CD2 . TYR A 1 239 ? 7.636 54.258 7.190 1.00 22.28 ? 239 TYR A CD2 1 ATOM 1911 C CE1 . TYR A 1 239 ? 6.634 52.082 8.596 1.00 20.98 ? 239 TYR A CE1 1 ATOM 1912 C CE2 . TYR A 1 239 ? 8.511 53.276 7.673 1.00 22.05 ? 239 TYR A CE2 1 ATOM 1913 C CZ . TYR A 1 239 ? 8.000 52.192 8.373 1.00 22.58 ? 239 TYR A CZ 1 ATOM 1914 O OH . TYR A 1 239 ? 8.852 51.218 8.840 1.00 23.63 ? 239 TYR A OH 1 ATOM 1915 N N . THR A 1 240 ? 3.213 54.963 9.151 1.00 26.09 ? 240 THR A N 1 ATOM 1916 C CA . THR A 1 240 ? 2.674 54.236 10.278 1.00 27.12 ? 240 THR A CA 1 ATOM 1917 C C . THR A 1 240 ? 1.883 53.066 9.720 1.00 27.46 ? 240 THR A C 1 ATOM 1918 O O . THR A 1 240 ? 1.181 53.195 8.713 1.00 25.68 ? 240 THR A O 1 ATOM 1919 C CB . THR A 1 240 ? 1.758 55.134 11.147 1.00 29.20 ? 240 THR A CB 1 ATOM 1920 O OG1 . THR A 1 240 ? 1.110 54.332 12.142 1.00 31.79 ? 240 THR A OG1 1 ATOM 1921 C CG2 . THR A 1 240 ? 0.712 55.834 10.293 1.00 29.52 ? 240 THR A CG2 1 ATOM 1922 N N . ILE A 1 241 ? 2.021 51.919 10.373 1.00 27.76 ? 241 ILE A N 1 ATOM 1923 C CA . ILE A 1 241 ? 1.343 50.702 9.964 1.00 27.91 ? 241 ILE A CA 1 ATOM 1924 C C . ILE A 1 241 ? 0.016 50.595 10.697 1.00 30.13 ? 241 ILE A C 1 ATOM 1925 O O . ILE A 1 241 ? -0.073 50.917 11.881 1.00 30.87 ? 241 ILE A O 1 ATOM 1926 C CB . ILE A 1 241 ? 2.216 49.473 10.290 1.00 28.21 ? 241 ILE A CB 1 ATOM 1927 C CG1 . ILE A 1 241 ? 3.506 49.539 9.466 1.00 26.46 ? 241 ILE A CG1 1 ATOM 1928 C CG2 . ILE A 1 241 ? 1.443 48.181 10.028 1.00 26.81 ? 241 ILE A CG2 1 ATOM 1929 C CD1 . ILE A 1 241 ? 4.536 48.499 9.847 1.00 27.93 ? 241 ILE A CD1 1 ATOM 1930 N N . GLY A 1 242 ? -1.016 50.142 9.994 1.00 31.23 ? 242 GLY A N 1 ATOM 1931 C CA . GLY A 1 242 ? -2.312 50.013 10.627 1.00 31.76 ? 242 GLY A CA 1 ATOM 1932 C C . GLY A 1 242 ? -3.289 49.144 9.861 1.00 33.29 ? 242 GLY A C 1 ATOM 1933 O O . GLY A 1 242 ? -2.922 48.456 8.904 1.00 32.14 ? 242 GLY A O 1 ATOM 1934 N N . THR A 1 243 ? -4.545 49.190 10.297 1.00 33.87 ? 243 THR A N 1 ATOM 1935 C CA . THR A 1 243 ? -5.625 48.424 9.697 1.00 34.14 ? 243 THR A CA 1 ATOM 1936 C C . THR A 1 243 ? -6.577 49.360 8.964 1.00 34.48 ? 243 THR A C 1 ATOM 1937 O O . THR A 1 243 ? -6.942 50.421 9.476 1.00 33.57 ? 243 THR A O 1 ATOM 1938 C CB . THR A 1 243 ? -6.411 47.656 10.778 1.00 35.03 ? 243 THR A CB 1 ATOM 1939 O OG1 . THR A 1 243 ? -5.542 46.705 11.406 1.00 36.65 ? 243 THR A OG1 1 ATOM 1940 C CG2 . THR A 1 243 ? -7.604 46.926 10.166 1.00 34.83 ? 243 THR A CG2 1 ATOM 1941 N N . TYR A 1 244 ? -6.983 48.954 7.766 1.00 35.57 ? 244 TYR A N 1 ATOM 1942 C CA . TYR A 1 244 ? -7.880 49.750 6.941 1.00 37.71 ? 244 TYR A CA 1 ATOM 1943 C C . TYR A 1 244 ? -9.236 49.083 6.722 1.00 40.05 ? 244 TYR A C 1 ATOM 1944 O O . TYR A 1 244 ? -9.313 47.901 6.396 1.00 40.11 ? 244 TYR A O 1 ATOM 1945 C CB . TYR A 1 244 ? -7.217 50.025 5.590 1.00 35.14 ? 244 TYR A CB 1 ATOM 1946 C CG . TYR A 1 244 ? -8.111 50.686 4.562 1.00 34.56 ? 244 TYR A CG 1 ATOM 1947 C CD1 . TYR A 1 244 ? -8.730 51.908 4.822 1.00 33.38 ? 244 TYR A CD1 1 ATOM 1948 C CD2 . TYR A 1 244 ? -8.287 50.115 3.301 1.00 34.45 ? 244 TYR A CD2 1 ATOM 1949 C CE1 . TYR A 1 244 ? -9.493 52.549 3.846 1.00 33.33 ? 244 TYR A CE1 1 ATOM 1950 C CE2 . TYR A 1 244 ? -9.046 50.746 2.320 1.00 32.89 ? 244 TYR A CE2 1 ATOM 1951 C CZ . TYR A 1 244 ? -9.642 51.962 2.596 1.00 33.11 ? 244 TYR A CZ 1 ATOM 1952 O OH . TYR A 1 244 ? -10.357 52.599 1.610 1.00 33.83 ? 244 TYR A OH 1 ATOM 1953 N N . SER A 1 245 ? -10.299 49.861 6.907 1.00 43.66 ? 245 SER A N 1 ATOM 1954 C CA . SER A 1 245 ? -11.666 49.381 6.715 1.00 46.97 ? 245 SER A CA 1 ATOM 1955 C C . SER A 1 245 ? -12.325 50.212 5.618 1.00 47.98 ? 245 SER A C 1 ATOM 1956 O O . SER A 1 245 ? -12.754 51.341 5.858 1.00 48.73 ? 245 SER A O 1 ATOM 1957 C CB . SER A 1 245 ? -12.468 49.525 8.009 1.00 47.61 ? 245 SER A CB 1 ATOM 1958 O OG . SER A 1 245 ? -11.871 48.785 9.059 1.00 51.05 ? 245 SER A OG 1 ATOM 1959 N N . PRO A 1 246 ? -12.410 49.662 4.398 1.00 49.39 ? 246 PRO A N 1 ATOM 1960 C CA . PRO A 1 246 ? -13.018 50.356 3.258 1.00 51.89 ? 246 PRO A CA 1 ATOM 1961 C C . PRO A 1 246 ? -14.417 50.874 3.588 1.00 55.27 ? 246 PRO A C 1 ATOM 1962 O O . PRO A 1 246 ? -14.764 52.023 3.292 1.00 54.57 ? 246 PRO A O 1 ATOM 1963 C CB . PRO A 1 246 ? -13.056 49.277 2.179 1.00 50.53 ? 246 PRO A CB 1 ATOM 1964 C CG . PRO A 1 246 ? -11.891 48.408 2.519 1.00 50.07 ? 246 PRO A CG 1 ATOM 1965 C CD . PRO A 1 246 ? -11.990 48.302 4.020 1.00 49.66 ? 246 PRO A CD 1 ATOM 1966 N N . ASP A 1 247 ? -15.205 49.998 4.205 1.00 58.99 ? 247 ASP A N 1 ATOM 1967 C CA . ASP A 1 247 ? -16.584 50.279 4.595 1.00 62.04 ? 247 ASP A CA 1 ATOM 1968 C C . ASP A 1 247 ? -16.762 51.655 5.213 1.00 62.12 ? 247 ASP A C 1 ATOM 1969 O O . ASP A 1 247 ? -17.524 52.484 4.711 1.00 62.86 ? 247 ASP A O 1 ATOM 1970 C CB . ASP A 1 247 ? -17.049 49.222 5.592 1.00 66.13 ? 247 ASP A CB 1 ATOM 1971 C CG . ASP A 1 247 ? -16.499 47.847 5.271 1.00 70.67 ? 247 ASP A CG 1 ATOM 1972 O OD1 . ASP A 1 247 ? -16.852 47.299 4.202 1.00 71.97 ? 247 ASP A OD1 1 ATOM 1973 O OD2 . ASP A 1 247 ? -15.702 47.321 6.083 1.00 72.74 ? 247 ASP A OD2 1 ATOM 1974 N N . ARG A 1 248 ? -16.052 51.893 6.308 1.00 61.19 ? 248 ARG A N 1 ATOM 1975 C CA . ARG A 1 248 ? -16.150 53.160 7.011 1.00 60.26 ? 248 ARG A CA 1 ATOM 1976 C C . ARG A 1 248 ? -14.995 54.113 6.718 1.00 57.55 ? 248 ARG A C 1 ATOM 1977 O O . ARG A 1 248 ? -14.876 55.160 7.359 1.00 57.47 ? 248 ARG A O 1 ATOM 1978 C CB . ARG A 1 248 ? -16.243 52.883 8.510 1.00 64.18 ? 248 ARG A CB 1 ATOM 1979 C CG . ARG A 1 248 ? -15.249 51.837 8.981 1.00 68.67 ? 248 ARG A CG 1 ATOM 1980 C CD . ARG A 1 248 ? -15.527 51.395 10.409 1.00 73.39 ? 248 ARG A CD 1 ATOM 1981 N NE . ARG A 1 248 ? -14.576 50.374 10.846 1.00 77.21 ? 248 ARG A NE 1 ATOM 1982 C CZ . ARG A 1 248 ? -14.657 49.712 11.996 1.00 78.84 ? 248 ARG A CZ 1 ATOM 1983 N NH1 . ARG A 1 248 ? -15.653 49.957 12.842 1.00 79.81 ? 248 ARG A NH1 1 ATOM 1984 N NH2 . ARG A 1 248 ? -13.742 48.800 12.300 1.00 78.94 ? 248 ARG A NH2 1 ATOM 1985 N N . GLU A 1 249 ? -14.162 53.762 5.738 1.00 54.04 ? 249 GLU A N 1 ATOM 1986 C CA . GLU A 1 249 ? -13.006 54.581 5.369 1.00 49.73 ? 249 GLU A CA 1 ATOM 1987 C C . GLU A 1 249 ? -12.218 54.913 6.622 1.00 47.51 ? 249 GLU A C 1 ATOM 1988 O O . GLU A 1 249 ? -11.876 56.068 6.875 1.00 46.71 ? 249 GLU A O 1 ATOM 1989 C CB . GLU A 1 249 ? -13.445 55.879 4.691 1.00 49.20 ? 249 GLU A CB 1 ATOM 1990 C CG . GLU A 1 249 ? -14.040 55.699 3.309 1.00 51.16 ? 249 GLU A CG 1 ATOM 1991 C CD . GLU A 1 249 ? -13.187 54.818 2.412 1.00 50.95 ? 249 GLU A CD 1 ATOM 1992 O OE1 . GLU A 1 249 ? -11.953 54.782 2.601 1.00 49.39 ? 249 GLU A OE1 1 ATOM 1993 O OE2 . GLU A 1 249 ? -13.753 54.168 1.508 1.00 52.27 ? 249 GLU A OE2 1 ATOM 1994 N N . ASN A 1 250 ? -11.926 53.881 7.402 1.00 45.60 ? 250 ASN A N 1 ATOM 1995 C CA . ASN A 1 250 ? -11.207 54.056 8.648 1.00 44.70 ? 250 ASN A CA 1 ATOM 1996 C C . ASN A 1 250 ? -9.818 53.424 8.671 1.00 42.44 ? 250 ASN A C 1 ATOM 1997 O O . ASN A 1 250 ? -9.651 52.241 8.365 1.00 41.06 ? 250 ASN A O 1 ATOM 1998 C CB . ASN A 1 250 ? -12.039 53.480 9.794 1.00 47.84 ? 250 ASN A CB 1 ATOM 1999 C CG . ASN A 1 250 ? -11.373 53.656 11.136 1.00 52.20 ? 250 ASN A CG 1 ATOM 2000 O OD1 . ASN A 1 250 ? -11.217 54.780 11.621 1.00 55.57 ? 250 ASN A OD1 1 ATOM 2001 N ND2 . ASN A 1 250 ? -10.964 52.546 11.747 1.00 53.79 ? 250 ASN A ND2 1 ATOM 2002 N N . PHE A 1 251 ? -8.822 54.229 9.028 1.00 39.93 ? 251 PHE A N 1 ATOM 2003 C CA . PHE A 1 251 ? -7.456 53.739 9.144 1.00 38.13 ? 251 PHE A CA 1 ATOM 2004 C C . PHE A 1 251 ? -7.087 53.816 10.616 1.00 37.09 ? 251 PHE A C 1 ATOM 2005 O O . PHE A 1 251 ? -7.062 54.896 11.202 1.00 37.43 ? 251 PHE A O 1 ATOM 2006 C CB . PHE A 1 251 ? -6.471 54.588 8.341 1.00 34.98 ? 251 PHE A CB 1 ATOM 2007 C CG . PHE A 1 251 ? -5.041 54.169 8.529 1.00 33.97 ? 251 PHE A CG 1 ATOM 2008 C CD1 . PHE A 1 251 ? -4.614 52.905 8.121 1.00 32.96 ? 251 PHE A CD1 1 ATOM 2009 C CD2 . PHE A 1 251 ? -4.126 55.018 9.146 1.00 32.67 ? 251 PHE A CD2 1 ATOM 2010 C CE1 . PHE A 1 251 ? -3.294 52.492 8.326 1.00 32.04 ? 251 PHE A CE1 1 ATOM 2011 C CE2 . PHE A 1 251 ? -2.806 54.616 9.356 1.00 31.84 ? 251 PHE A CE2 1 ATOM 2012 C CZ . PHE A 1 251 ? -2.390 53.350 8.945 1.00 31.60 ? 251 PHE A CZ 1 ATOM 2013 N N . LEU A 1 252 ? -6.803 52.666 11.210 1.00 37.43 ? 252 LEU A N 1 ATOM 2014 C CA . LEU A 1 252 ? -6.456 52.610 12.620 1.00 38.28 ? 252 LEU A CA 1 ATOM 2015 C C . LEU A 1 252 ? -4.976 52.276 12.808 1.00 37.11 ? 252 LEU A C 1 ATOM 2016 O O . LEU A 1 252 ? -4.541 51.169 12.493 1.00 36.44 ? 252 LEU A O 1 ATOM 2017 C CB . LEU A 1 252 ? -7.310 51.547 13.311 1.00 41.21 ? 252 LEU A CB 1 ATOM 2018 C CG . LEU A 1 252 ? -7.825 51.817 14.727 1.00 45.88 ? 252 LEU A CG 1 ATOM 2019 C CD1 . LEU A 1 252 ? -8.360 50.505 15.302 1.00 45.82 ? 252 LEU A CD1 1 ATOM 2020 C CD2 . LEU A 1 252 ? -6.713 52.373 15.617 1.00 46.81 ? 252 LEU A CD2 1 ATOM 2021 N N . PRO A 1 253 ? -4.185 53.233 13.321 1.00 36.65 ? 253 PRO A N 1 ATOM 2022 C CA . PRO A 1 253 ? -2.751 53.014 13.545 1.00 37.13 ? 253 PRO A CA 1 ATOM 2023 C C . PRO A 1 253 ? -2.535 51.875 14.537 1.00 37.33 ? 253 PRO A C 1 ATOM 2024 O O . PRO A 1 253 ? -3.157 51.839 15.599 1.00 38.32 ? 253 PRO A O 1 ATOM 2025 C CB . PRO A 1 253 ? -2.276 54.347 14.120 1.00 37.25 ? 253 PRO A CB 1 ATOM 2026 C CG . PRO A 1 253 ? -3.261 55.337 13.574 1.00 39.51 ? 253 PRO A CG 1 ATOM 2027 C CD . PRO A 1 253 ? -4.569 54.604 13.696 1.00 37.06 ? 253 PRO A CD 1 ATOM 2028 N N . GLN A 1 254 ? -1.650 50.954 14.190 1.00 36.94 ? 254 GLN A N 1 ATOM 2029 C CA . GLN A 1 254 ? -1.342 49.814 15.041 1.00 37.39 ? 254 GLN A CA 1 ATOM 2030 C C . GLN A 1 254 ? -0.907 50.245 16.448 1.00 36.72 ? 254 GLN A C 1 ATOM 2031 O O . GLN A 1 254 ? -1.296 49.630 17.440 1.00 36.02 ? 254 GLN A O 1 ATOM 2032 C CB . GLN A 1 254 ? -0.221 49.003 14.400 1.00 40.91 ? 254 GLN A CB 1 ATOM 2033 C CG . GLN A 1 254 ? -0.329 47.514 14.598 1.00 45.48 ? 254 GLN A CG 1 ATOM 2034 C CD . GLN A 1 254 ? 0.807 46.775 13.927 1.00 48.30 ? 254 GLN A CD 1 ATOM 2035 O OE1 . GLN A 1 254 ? 0.652 45.626 13.502 1.00 51.64 ? 254 GLN A OE1 1 ATOM 2036 N NE2 . GLN A 1 254 ? 1.964 47.428 13.835 1.00 48.01 ? 254 GLN A NE2 1 ATOM 2037 N N . ASN A 1 255 ? -0.090 51.292 16.530 1.00 35.43 ? 255 ASN A N 1 ATOM 2038 C CA . ASN A 1 255 ? 0.396 51.771 17.819 1.00 35.77 ? 255 ASN A CA 1 ATOM 2039 C C . ASN A 1 255 ? -0.522 52.830 18.432 1.00 36.76 ? 255 ASN A C 1 ATOM 2040 O O . ASN A 1 255 ? -0.186 53.440 19.446 1.00 37.65 ? 255 ASN A O 1 ATOM 2041 C CB . ASN A 1 255 ? 1.817 52.335 17.684 1.00 32.50 ? 255 ASN A CB 1 ATOM 2042 C CG . ASN A 1 255 ? 1.886 53.555 16.780 1.00 33.50 ? 255 ASN A CG 1 ATOM 2043 O OD1 . ASN A 1 255 ? 0.872 54.195 16.489 1.00 31.74 ? 255 ASN A OD1 1 ATOM 2044 N ND2 . ASN A 1 255 ? 3.092 53.894 16.343 1.00 33.46 ? 255 ASN A ND2 1 ATOM 2045 N N . GLY A 1 256 ? -1.674 53.045 17.802 1.00 37.35 ? 256 GLY A N 1 ATOM 2046 C CA . GLY A 1 256 ? -2.640 54.016 18.294 1.00 36.80 ? 256 GLY A CA 1 ATOM 2047 C C . GLY A 1 256 ? -2.185 55.464 18.342 1.00 36.96 ? 256 GLY A C 1 ATOM 2048 O O . GLY A 1 256 ? -2.832 56.299 18.973 1.00 37.61 ? 256 GLY A O 1 ATOM 2049 N N . LEU A 1 257 ? -1.088 55.787 17.674 1.00 36.24 ? 257 LEU A N 1 ATOM 2050 C CA . LEU A 1 257 ? -0.602 57.156 17.703 1.00 36.78 ? 257 LEU A CA 1 ATOM 2051 C C . LEU A 1 257 ? -0.924 57.933 16.441 1.00 38.17 ? 257 LEU A C 1 ATOM 2052 O O . LEU A 1 257 ? -1.198 57.357 15.389 1.00 39.18 ? 257 LEU A O 1 ATOM 2053 C CB . LEU A 1 257 ? 0.916 57.175 17.906 1.00 35.33 ? 257 LEU A CB 1 ATOM 2054 C CG . LEU A 1 257 ? 1.492 56.430 19.111 1.00 36.82 ? 257 LEU A CG 1 ATOM 2055 C CD1 . LEU A 1 257 ? 3.000 56.677 19.187 1.00 36.83 ? 257 LEU A CD1 1 ATOM 2056 C CD2 . LEU A 1 257 ? 0.810 56.906 20.380 1.00 34.92 ? 257 LEU A CD2 1 ATOM 2057 N N . SER A 1 258 ? -0.908 59.254 16.567 1.00 38.55 ? 258 SER A N 1 ATOM 2058 C CA . SER A 1 258 ? -1.113 60.138 15.431 1.00 38.79 ? 258 SER A CA 1 ATOM 2059 C C . SER A 1 258 ? 0.324 60.549 15.149 1.00 38.34 ? 258 SER A C 1 ATOM 2060 O O . SER A 1 258 ? 1.121 60.669 16.081 1.00 38.50 ? 258 SER A O 1 ATOM 2061 C CB . SER A 1 258 ? -1.925 61.370 15.829 1.00 39.34 ? 258 SER A CB 1 ATOM 2062 O OG . SER A 1 258 ? -3.187 61.001 16.355 1.00 46.13 ? 258 SER A OG 1 ATOM 2063 N N . LEU A 1 259 ? 0.674 60.754 13.888 1.00 36.93 ? 259 LEU A N 1 ATOM 2064 C CA . LEU A 1 259 ? 2.040 61.143 13.584 1.00 36.47 ? 259 LEU A CA 1 ATOM 2065 C C . LEU A 1 259 ? 2.364 62.479 14.249 1.00 37.17 ? 259 LEU A C 1 ATOM 2066 O O . LEU A 1 259 ? 1.522 63.380 14.303 1.00 38.64 ? 259 LEU A O 1 ATOM 2067 C CB . LEU A 1 259 ? 2.238 61.215 12.066 1.00 35.84 ? 259 LEU A CB 1 ATOM 2068 C CG . LEU A 1 259 ? 2.111 59.851 11.372 1.00 36.09 ? 259 LEU A CG 1 ATOM 2069 C CD1 . LEU A 1 259 ? 2.080 60.026 9.864 1.00 36.40 ? 259 LEU A CD1 1 ATOM 2070 C CD2 . LEU A 1 259 ? 3.276 58.954 11.789 1.00 34.45 ? 259 LEU A CD2 1 ATOM 2071 N N . THR A 1 260 ? 3.572 62.587 14.795 1.00 35.87 ? 260 THR A N 1 ATOM 2072 C CA . THR A 1 260 ? 4.013 63.818 15.443 1.00 35.45 ? 260 THR A CA 1 ATOM 2073 C C . THR A 1 260 ? 5.336 64.290 14.851 1.00 35.25 ? 260 THR A C 1 ATOM 2074 O O . THR A 1 260 ? 5.765 65.420 15.091 1.00 36.07 ? 260 THR A O 1 ATOM 2075 C CB . THR A 1 260 ? 4.214 63.635 16.970 1.00 35.27 ? 260 THR A CB 1 ATOM 2076 O OG1 . THR A 1 260 ? 5.077 62.517 17.215 1.00 34.34 ? 260 THR A OG1 1 ATOM 2077 C CG2 . THR A 1 260 ? 2.882 63.420 17.666 1.00 35.02 ? 260 THR A CG2 1 ATOM 2078 N N . GLY A 1 261 ? 5.979 63.425 14.074 1.00 33.71 ? 261 GLY A N 1 ATOM 2079 C CA . GLY A 1 261 ? 7.254 63.782 13.489 1.00 31.87 ? 261 GLY A CA 1 ATOM 2080 C C . GLY A 1 261 ? 8.315 63.783 14.572 1.00 31.36 ? 261 GLY A C 1 ATOM 2081 O O . GLY A 1 261 ? 9.225 64.613 14.568 1.00 31.76 ? 261 GLY A O 1 ATOM 2082 N N . SER A 1 262 ? 8.191 62.852 15.513 1.00 28.97 ? 262 SER A N 1 ATOM 2083 C CA . SER A 1 262 ? 9.148 62.743 16.608 1.00 29.44 ? 262 SER A CA 1 ATOM 2084 C C . SER A 1 262 ? 9.827 61.372 16.612 1.00 30.07 ? 262 SER A C 1 ATOM 2085 O O . SER A 1 262 ? 9.505 60.498 15.805 1.00 29.94 ? 262 SER A O 1 ATOM 2086 C CB . SER A 1 262 ? 8.442 62.955 17.947 1.00 28.66 ? 262 SER A CB 1 ATOM 2087 O OG . SER A 1 262 ? 7.556 61.885 18.217 1.00 27.43 ? 262 SER A OG 1 ATOM 2088 N N . THR A 1 263 ? 10.760 61.182 17.535 1.00 30.42 ? 263 THR A N 1 ATOM 2089 C CA . THR A 1 263 ? 11.472 59.914 17.641 1.00 31.36 ? 263 THR A CA 1 ATOM 2090 C C . THR A 1 263 ? 10.489 58.800 17.975 1.00 31.57 ? 263 THR A C 1 ATOM 2091 O O . THR A 1 263 ? 10.862 57.641 18.118 1.00 32.64 ? 263 THR A O 1 ATOM 2092 C CB . THR A 1 263 ? 12.569 59.993 18.720 1.00 30.62 ? 263 THR A CB 1 ATOM 2093 O OG1 . THR A 1 263 ? 11.988 60.381 19.973 1.00 30.44 ? 263 THR A OG1 1 ATOM 2094 C CG2 . THR A 1 263 ? 13.623 61.016 18.319 1.00 28.82 ? 263 THR A CG2 1 ATOM 2095 N N . LEU A 1 264 ? 9.222 59.173 18.085 1.00 33.32 ? 264 LEU A N 1 ATOM 2096 C CA . LEU A 1 264 ? 8.142 58.241 18.385 1.00 34.95 ? 264 LEU A CA 1 ATOM 2097 C C . LEU A 1 264 ? 7.661 57.555 17.093 1.00 35.38 ? 264 LEU A C 1 ATOM 2098 O O . LEU A 1 264 ? 7.091 56.461 17.134 1.00 36.40 ? 264 LEU A O 1 ATOM 2099 C CB . LEU A 1 264 ? 6.978 59.019 19.005 1.00 34.88 ? 264 LEU A CB 1 ATOM 2100 C CG . LEU A 1 264 ? 6.469 58.812 20.434 1.00 36.81 ? 264 LEU A CG 1 ATOM 2101 C CD1 . LEU A 1 264 ? 7.592 58.519 21.407 1.00 35.75 ? 264 LEU A CD1 1 ATOM 2102 C CD2 . LEU A 1 264 ? 5.716 60.076 20.836 1.00 35.85 ? 264 LEU A CD2 1 ATOM 2103 N N . ASP A 1 265 ? 7.895 58.204 15.952 1.00 32.71 ? 265 ASP A N 1 ATOM 2104 C CA . ASP A 1 265 ? 7.444 57.679 14.667 1.00 30.89 ? 265 ASP A CA 1 ATOM 2105 C C . ASP A 1 265 ? 8.519 57.035 13.801 1.00 29.58 ? 265 ASP A C 1 ATOM 2106 O O . ASP A 1 265 ? 9.715 57.285 13.969 1.00 29.96 ? 265 ASP A O 1 ATOM 2107 C CB . ASP A 1 265 ? 6.764 58.788 13.859 1.00 32.28 ? 265 ASP A CB 1 ATOM 2108 C CG . ASP A 1 265 ? 5.681 59.506 14.646 1.00 34.34 ? 265 ASP A CG 1 ATOM 2109 O OD1 . ASP A 1 265 ? 4.901 58.824 15.350 1.00 35.36 ? 265 ASP A OD1 1 ATOM 2110 O OD2 . ASP A 1 265 ? 5.606 60.751 14.554 1.00 33.01 ? 265 ASP A OD2 1 ATOM 2111 N N . LEU A 1 266 ? 8.070 56.212 12.860 1.00 26.03 ? 266 LEU A N 1 ATOM 2112 C CA . LEU A 1 266 ? 8.965 55.523 11.945 1.00 24.46 ? 266 LEU A CA 1 ATOM 2113 C C . LEU A 1 266 ? 9.186 56.321 10.664 1.00 23.68 ? 266 LEU A C 1 ATOM 2114 O O . LEU A 1 266 ? 8.355 57.136 10.265 1.00 22.57 ? 266 LEU A O 1 ATOM 2115 C CB . LEU A 1 266 ? 8.393 54.148 11.578 1.00 23.49 ? 266 LEU A CB 1 ATOM 2116 C CG . LEU A 1 266 ? 8.316 53.090 12.686 1.00 23.29 ? 266 LEU A CG 1 ATOM 2117 C CD1 . LEU A 1 266 ? 7.512 51.890 12.203 1.00 19.50 ? 266 LEU A CD1 1 ATOM 2118 C CD2 . LEU A 1 266 ? 9.729 52.671 13.088 1.00 20.91 ? 266 LEU A CD2 1 ATOM 2119 N N . ARG A 1 267 ? 10.331 56.085 10.036 1.00 23.05 ? 267 ARG A N 1 ATOM 2120 C CA . ARG A 1 267 ? 10.672 56.720 8.774 1.00 22.57 ? 267 ARG A CA 1 ATOM 2121 C C . ARG A 1 267 ? 11.183 55.590 7.899 1.00 22.87 ? 267 ARG A C 1 ATOM 2122 O O . ARG A 1 267 ? 11.603 54.549 8.411 1.00 23.33 ? 267 ARG A O 1 ATOM 2123 C CB . ARG A 1 267 ? 11.813 57.726 8.926 1.00 22.49 ? 267 ARG A CB 1 ATOM 2124 C CG . ARG A 1 267 ? 11.584 58.890 9.858 1.00 24.45 ? 267 ARG A CG 1 ATOM 2125 C CD . ARG A 1 267 ? 12.692 59.905 9.621 1.00 24.50 ? 267 ARG A CD 1 ATOM 2126 N NE . ARG A 1 267 ? 12.948 60.744 10.783 1.00 26.88 ? 267 ARG A NE 1 ATOM 2127 C CZ . ARG A 1 267 ? 13.916 61.653 10.839 1.00 28.19 ? 267 ARG A CZ 1 ATOM 2128 N NH1 . ARG A 1 267 ? 14.713 61.842 9.792 1.00 25.62 ? 267 ARG A NH1 1 ATOM 2129 N NH2 . ARG A 1 267 ? 14.101 62.359 11.947 1.00 29.45 ? 267 ARG A NH2 1 ATOM 2130 N N . TYR A 1 268 ? 11.146 55.782 6.587 1.00 21.72 ? 268 TYR A N 1 ATOM 2131 C CA . TYR A 1 268 ? 11.677 54.771 5.687 1.00 22.03 ? 268 TYR A CA 1 ATOM 2132 C C . TYR A 1 268 ? 13.194 54.831 5.813 1.00 22.22 ? 268 TYR A C 1 ATOM 2133 O O . TYR A 1 268 ? 13.874 53.814 5.890 1.00 23.02 ? 268 TYR A O 1 ATOM 2134 C CB . TYR A 1 268 ? 11.369 55.095 4.225 1.00 20.73 ? 268 TYR A CB 1 ATOM 2135 C CG . TYR A 1 268 ? 9.966 54.860 3.751 1.00 22.10 ? 268 TYR A CG 1 ATOM 2136 C CD1 . TYR A 1 268 ? 9.331 53.635 3.954 1.00 22.40 ? 268 TYR A CD1 1 ATOM 2137 C CD2 . TYR A 1 268 ? 9.310 55.827 2.991 1.00 21.38 ? 268 TYR A CD2 1 ATOM 2138 C CE1 . TYR A 1 268 ? 8.077 53.376 3.395 1.00 23.31 ? 268 TYR A CE1 1 ATOM 2139 C CE2 . TYR A 1 268 ? 8.066 55.581 2.431 1.00 21.91 ? 268 TYR A CE2 1 ATOM 2140 C CZ . TYR A 1 268 ? 7.455 54.356 2.630 1.00 22.60 ? 268 TYR A CZ 1 ATOM 2141 O OH . TYR A 1 268 ? 6.241 54.107 2.033 1.00 23.32 ? 268 TYR A OH 1 ATOM 2142 N N . ASP A 1 269 ? 13.706 56.058 5.817 1.00 22.85 ? 269 ASP A N 1 ATOM 2143 C CA . ASP A 1 269 ? 15.138 56.314 5.835 1.00 22.97 ? 269 ASP A CA 1 ATOM 2144 C C . ASP A 1 269 ? 15.408 57.498 6.757 1.00 24.07 ? 269 ASP A C 1 ATOM 2145 O O . ASP A 1 269 ? 14.668 58.481 6.740 1.00 25.34 ? 269 ASP A O 1 ATOM 2146 C CB . ASP A 1 269 ? 15.558 56.636 4.395 1.00 21.22 ? 269 ASP A CB 1 ATOM 2147 C CG . ASP A 1 269 ? 17.051 56.699 4.208 1.00 21.44 ? 269 ASP A CG 1 ATOM 2148 O OD1 . ASP A 1 269 ? 17.577 55.843 3.471 1.00 20.39 ? 269 ASP A OD1 1 ATOM 2149 O OD2 . ASP A 1 269 ? 17.697 57.605 4.781 1.00 22.42 ? 269 ASP A OD2 1 ATOM 2150 N N . TYR A 1 270 ? 16.476 57.412 7.544 1.00 23.07 ? 270 TYR A N 1 ATOM 2151 C CA . TYR A 1 270 ? 16.814 58.465 8.492 1.00 22.67 ? 270 TYR A CA 1 ATOM 2152 C C . TYR A 1 270 ? 17.842 59.487 8.022 1.00 22.67 ? 270 TYR A C 1 ATOM 2153 O O . TYR A 1 270 ? 18.363 60.254 8.830 1.00 24.34 ? 270 TYR A O 1 ATOM 2154 C CB . TYR A 1 270 ? 17.253 57.823 9.812 1.00 23.36 ? 270 TYR A CB 1 ATOM 2155 C CG . TYR A 1 270 ? 16.122 57.056 10.451 1.00 24.29 ? 270 TYR A CG 1 ATOM 2156 C CD1 . TYR A 1 270 ? 15.241 57.682 11.337 1.00 25.78 ? 270 TYR A CD1 1 ATOM 2157 C CD2 . TYR A 1 270 ? 15.850 55.737 10.076 1.00 25.05 ? 270 TYR A CD2 1 ATOM 2158 C CE1 . TYR A 1 270 ? 14.103 57.008 11.829 1.00 26.38 ? 270 TYR A CE1 1 ATOM 2159 C CE2 . TYR A 1 270 ? 14.721 55.060 10.556 1.00 24.89 ? 270 TYR A CE2 1 ATOM 2160 C CZ . TYR A 1 270 ? 13.854 55.700 11.426 1.00 26.12 ? 270 TYR A CZ 1 ATOM 2161 O OH . TYR A 1 270 ? 12.728 55.037 11.866 1.00 26.86 ? 270 TYR A OH 1 ATOM 2162 N N . GLY A 1 271 ? 18.125 59.501 6.723 1.00 20.91 ? 271 GLY A N 1 ATOM 2163 C CA . GLY A 1 271 ? 19.071 60.458 6.174 1.00 19.97 ? 271 GLY A CA 1 ATOM 2164 C C . GLY A 1 271 ? 18.351 61.360 5.185 1.00 21.16 ? 271 GLY A C 1 ATOM 2165 O O . GLY A 1 271 ? 17.208 61.761 5.430 1.00 20.51 ? 271 GLY A O 1 ATOM 2166 N N . GLN A 1 272 ? 19.015 61.685 4.076 1.00 21.46 ? 272 GLN A N 1 ATOM 2167 C CA . GLN A 1 272 ? 18.439 62.528 3.024 1.00 21.69 ? 272 GLN A CA 1 ATOM 2168 C C . GLN A 1 272 ? 17.536 61.635 2.181 1.00 22.71 ? 272 GLN A C 1 ATOM 2169 O O . GLN A 1 272 ? 18.016 60.869 1.347 1.00 22.16 ? 272 GLN A O 1 ATOM 2170 C CB . GLN A 1 272 ? 19.553 63.105 2.153 1.00 23.89 ? 272 GLN A CB 1 ATOM 2171 C CG . GLN A 1 272 ? 20.376 64.178 2.831 1.00 24.49 ? 272 GLN A CG 1 ATOM 2172 C CD . GLN A 1 272 ? 19.538 65.392 3.186 1.00 27.53 ? 272 GLN A CD 1 ATOM 2173 O OE1 . GLN A 1 272 ? 18.729 65.858 2.381 1.00 27.70 ? 272 GLN A OE1 1 ATOM 2174 N NE2 . GLN A 1 272 ? 19.734 65.917 4.392 1.00 26.49 ? 272 GLN A NE2 1 ATOM 2175 N N . PHE A 1 273 ? 16.229 61.759 2.378 1.00 22.93 ? 273 PHE A N 1 ATOM 2176 C CA . PHE A 1 273 ? 15.266 60.896 1.693 1.00 23.45 ? 273 PHE A CA 1 ATOM 2177 C C . PHE A 1 273 ? 13.923 61.625 1.735 1.00 23.28 ? 273 PHE A C 1 ATOM 2178 O O . PHE A 1 273 ? 13.389 61.850 2.815 1.00 22.65 ? 273 PHE A O 1 ATOM 2179 C CB . PHE A 1 273 ? 15.168 59.599 2.500 1.00 22.04 ? 273 PHE A CB 1 ATOM 2180 C CG . PHE A 1 273 ? 14.643 58.416 1.739 1.00 23.40 ? 273 PHE A CG 1 ATOM 2181 C CD1 . PHE A 1 273 ? 15.503 57.636 0.963 1.00 22.43 ? 273 PHE A CD1 1 ATOM 2182 C CD2 . PHE A 1 273 ? 13.315 58.016 1.881 1.00 20.61 ? 273 PHE A CD2 1 ATOM 2183 C CE1 . PHE A 1 273 ? 15.048 56.466 0.351 1.00 21.74 ? 273 PHE A CE1 1 ATOM 2184 C CE2 . PHE A 1 273 ? 12.849 56.851 1.273 1.00 21.38 ? 273 PHE A CE2 1 ATOM 2185 C CZ . PHE A 1 273 ? 13.718 56.072 0.509 1.00 22.85 ? 273 PHE A CZ 1 ATOM 2186 N N . TYR A 1 274 ? 13.362 61.982 0.584 1.00 22.92 ? 274 TYR A N 1 ATOM 2187 C CA . TYR A 1 274 ? 12.091 62.698 0.607 1.00 22.79 ? 274 TYR A CA 1 ATOM 2188 C C . TYR A 1 274 ? 11.179 62.446 -0.595 1.00 21.54 ? 274 TYR A C 1 ATOM 2189 O O . TYR A 1 274 ? 11.627 62.018 -1.658 1.00 21.30 ? 274 TYR A O 1 ATOM 2190 C CB . TYR A 1 274 ? 12.352 64.210 0.736 1.00 20.94 ? 274 TYR A CB 1 ATOM 2191 C CG . TYR A 1 274 ? 11.162 64.974 1.276 1.00 20.94 ? 274 TYR A CG 1 ATOM 2192 C CD1 . TYR A 1 274 ? 10.736 64.788 2.595 1.00 21.06 ? 274 TYR A CD1 1 ATOM 2193 C CD2 . TYR A 1 274 ? 10.424 65.836 0.460 1.00 20.22 ? 274 TYR A CD2 1 ATOM 2194 C CE1 . TYR A 1 274 ? 9.602 65.432 3.091 1.00 21.29 ? 274 TYR A CE1 1 ATOM 2195 C CE2 . TYR A 1 274 ? 9.283 66.490 0.946 1.00 20.52 ? 274 TYR A CE2 1 ATOM 2196 C CZ . TYR A 1 274 ? 8.879 66.278 2.262 1.00 22.77 ? 274 TYR A CZ 1 ATOM 2197 O OH . TYR A 1 274 ? 7.737 66.875 2.744 1.00 23.78 ? 274 TYR A OH 1 ATOM 2198 N N . ALA A 1 275 ? 9.891 62.721 -0.405 1.00 21.20 ? 275 ALA A N 1 ATOM 2199 C CA . ALA A 1 275 ? 8.898 62.563 -1.461 1.00 22.49 ? 275 ALA A CA 1 ATOM 2200 C C . ALA A 1 275 ? 8.878 61.142 -2.014 1.00 22.17 ? 275 ALA A C 1 ATOM 2201 O O . ALA A 1 275 ? 8.623 60.923 -3.203 1.00 23.07 ? 275 ALA A O 1 ATOM 2202 C CB . ALA A 1 275 ? 9.182 63.564 -2.585 1.00 20.27 ? 275 ALA A CB 1 ATOM 2203 N N . SER A 1 276 ? 9.137 60.177 -1.143 1.00 21.52 ? 276 SER A N 1 ATOM 2204 C CA . SER A 1 276 ? 9.166 58.785 -1.551 1.00 22.48 ? 276 SER A CA 1 ATOM 2205 C C . SER A 1 276 ? 7.798 58.321 -2.046 1.00 23.50 ? 276 SER A C 1 ATOM 2206 O O . SER A 1 276 ? 6.757 58.715 -1.508 1.00 23.53 ? 276 SER A O 1 ATOM 2207 C CB . SER A 1 276 ? 9.639 57.908 -0.389 1.00 22.12 ? 276 SER A CB 1 ATOM 2208 O OG . SER A 1 276 ? 8.754 58.001 0.714 1.00 24.54 ? 276 SER A OG 1 ATOM 2209 N N . LYS A 1 277 ? 7.817 57.482 -3.079 1.00 23.53 ? 277 LYS A N 1 ATOM 2210 C CA . LYS A 1 277 ? 6.599 56.951 -3.677 1.00 22.88 ? 277 LYS A CA 1 ATOM 2211 C C . LYS A 1 277 ? 6.837 55.508 -4.123 1.00 23.16 ? 277 LYS A C 1 ATOM 2212 O O . LYS A 1 277 ? 7.871 55.190 -4.714 1.00 24.20 ? 277 LYS A O 1 ATOM 2213 C CB . LYS A 1 277 ? 6.192 57.821 -4.871 1.00 21.35 ? 277 LYS A CB 1 ATOM 2214 C CG . LYS A 1 277 ? 4.869 57.432 -5.512 1.00 22.24 ? 277 LYS A CG 1 ATOM 2215 C CD . LYS A 1 277 ? 4.362 58.519 -6.461 1.00 21.26 ? 277 LYS A CD 1 ATOM 2216 C CE . LYS A 1 277 ? 3.873 59.742 -5.692 1.00 20.09 ? 277 LYS A CE 1 ATOM 2217 N NZ . LYS A 1 277 ? 2.815 59.369 -4.697 1.00 20.24 ? 277 LYS A NZ 1 ATOM 2218 N N . SER A 1 278 ? 5.879 54.635 -3.837 1.00 22.83 ? 278 SER A N 1 ATOM 2219 C CA . SER A 1 278 ? 6.006 53.231 -4.197 1.00 22.13 ? 278 SER A CA 1 ATOM 2220 C C . SER A 1 278 ? 4.978 52.812 -5.240 1.00 22.98 ? 278 SER A C 1 ATOM 2221 O O . SER A 1 278 ? 3.970 53.491 -5.448 1.00 22.39 ? 278 SER A O 1 ATOM 2222 C CB . SER A 1 278 ? 5.815 52.359 -2.958 1.00 22.25 ? 278 SER A CB 1 ATOM 2223 O OG . SER A 1 278 ? 4.461 52.399 -2.527 1.00 20.09 ? 278 SER A OG 1 ATOM 2224 N N . PHE A 1 279 ? 5.242 51.681 -5.888 1.00 22.90 ? 279 PHE A N 1 ATOM 2225 C CA . PHE A 1 279 ? 4.334 51.139 -6.885 1.00 22.67 ? 279 PHE A CA 1 ATOM 2226 C C . PHE A 1 279 ? 4.422 49.619 -6.836 1.00 23.76 ? 279 PHE A C 1 ATOM 2227 O O . PHE A 1 279 ? 5.424 49.063 -6.379 1.00 24.12 ? 279 PHE A O 1 ATOM 2228 C CB . PHE A 1 279 ? 4.687 51.668 -8.283 1.00 22.34 ? 279 PHE A CB 1 ATOM 2229 C CG . PHE A 1 279 ? 5.938 51.073 -8.879 1.00 22.98 ? 279 PHE A CG 1 ATOM 2230 C CD1 . PHE A 1 279 ? 5.862 49.975 -9.741 1.00 22.03 ? 279 PHE A CD1 1 ATOM 2231 C CD2 . PHE A 1 279 ? 7.187 51.623 -8.602 1.00 21.84 ? 279 PHE A CD2 1 ATOM 2232 C CE1 . PHE A 1 279 ? 7.012 49.436 -10.322 1.00 22.00 ? 279 PHE A CE1 1 ATOM 2233 C CE2 . PHE A 1 279 ? 8.347 51.091 -9.177 1.00 22.61 ? 279 PHE A CE2 1 ATOM 2234 C CZ . PHE A 1 279 ? 8.261 49.997 -10.039 1.00 22.27 ? 279 PHE A CZ 1 ATOM 2235 N N . PHE A 1 280 ? 3.367 48.945 -7.275 1.00 23.95 ? 280 PHE A N 1 ATOM 2236 C CA . PHE A 1 280 ? 3.376 47.492 -7.275 1.00 24.73 ? 280 PHE A CA 1 ATOM 2237 C C . PHE A 1 280 ? 3.906 46.971 -8.601 1.00 25.67 ? 280 PHE A C 1 ATOM 2238 O O . PHE A 1 280 ? 3.514 47.441 -9.670 1.00 26.98 ? 280 PHE A O 1 ATOM 2239 C CB . PHE A 1 280 ? 1.973 46.939 -7.029 1.00 23.91 ? 280 PHE A CB 1 ATOM 2240 C CG . PHE A 1 280 ? 1.893 45.436 -7.109 1.00 25.18 ? 280 PHE A CG 1 ATOM 2241 C CD1 . PHE A 1 280 ? 2.640 44.638 -6.244 1.00 25.68 ? 280 PHE A CD1 1 ATOM 2242 C CD2 . PHE A 1 280 ? 1.074 44.818 -8.052 1.00 24.88 ? 280 PHE A CD2 1 ATOM 2243 C CE1 . PHE A 1 280 ? 2.576 43.242 -6.316 1.00 24.52 ? 280 PHE A CE1 1 ATOM 2244 C CE2 . PHE A 1 280 ? 1.000 43.426 -8.132 1.00 25.00 ? 280 PHE A CE2 1 ATOM 2245 C CZ . PHE A 1 280 ? 1.753 42.636 -7.263 1.00 24.15 ? 280 PHE A CZ 1 ATOM 2246 N N . ASP A 1 281 ? 4.803 45.999 -8.514 1.00 26.52 ? 281 ASP A N 1 ATOM 2247 C CA . ASP A 1 281 ? 5.421 45.365 -9.675 1.00 27.74 ? 281 ASP A CA 1 ATOM 2248 C C . ASP A 1 281 ? 4.859 43.941 -9.724 1.00 29.71 ? 281 ASP A C 1 ATOM 2249 O O . ASP A 1 281 ? 5.334 43.063 -9.002 1.00 28.49 ? 281 ASP A O 1 ATOM 2250 C CB . ASP A 1 281 ? 6.936 45.335 -9.461 1.00 28.00 ? 281 ASP A CB 1 ATOM 2251 C CG . ASP A 1 281 ? 7.671 44.509 -10.498 1.00 30.15 ? 281 ASP A CG 1 ATOM 2252 O OD1 . ASP A 1 281 ? 7.035 43.688 -11.199 1.00 29.47 ? 281 ASP A OD1 1 ATOM 2253 O OD2 . ASP A 1 281 ? 8.908 44.675 -10.591 1.00 29.77 ? 281 ASP A OD2 1 ATOM 2254 N N . ASP A 1 282 ? 3.855 43.705 -10.565 1.00 31.80 ? 282 ASP A N 1 ATOM 2255 C CA . ASP A 1 282 ? 3.249 42.377 -10.640 1.00 35.92 ? 282 ASP A CA 1 ATOM 2256 C C . ASP A 1 282 ? 4.094 41.336 -11.355 1.00 36.02 ? 282 ASP A C 1 ATOM 2257 O O . ASP A 1 282 ? 3.797 40.145 -11.285 1.00 37.78 ? 282 ASP A O 1 ATOM 2258 C CB . ASP A 1 282 ? 1.856 42.447 -11.279 1.00 40.49 ? 282 ASP A CB 1 ATOM 2259 C CG . ASP A 1 282 ? 1.885 42.996 -12.685 1.00 46.39 ? 282 ASP A CG 1 ATOM 2260 O OD1 . ASP A 1 282 ? 2.514 44.058 -12.895 1.00 52.30 ? 282 ASP A OD1 1 ATOM 2261 O OD2 . ASP A 1 282 ? 1.272 42.373 -13.578 1.00 49.77 ? 282 ASP A OD2 1 ATOM 2262 N N . ALA A 1 283 ? 5.149 41.772 -12.034 1.00 35.43 ? 283 ALA A N 1 ATOM 2263 C CA . ALA A 1 283 ? 6.023 40.833 -12.728 1.00 35.50 ? 283 ALA A CA 1 ATOM 2264 C C . ALA A 1 283 ? 6.864 40.082 -11.698 1.00 36.77 ? 283 ALA A C 1 ATOM 2265 O O . ALA A 1 283 ? 7.100 38.881 -11.837 1.00 36.94 ? 283 ALA A O 1 ATOM 2266 C CB . ALA A 1 283 ? 6.932 41.571 -13.706 1.00 34.17 ? 283 ALA A CB 1 ATOM 2267 N N . LYS A 1 284 ? 7.313 40.791 -10.664 1.00 36.12 ? 284 LYS A N 1 ATOM 2268 C CA . LYS A 1 284 ? 8.128 40.178 -9.615 1.00 35.18 ? 284 LYS A CA 1 ATOM 2269 C C . LYS A 1 284 ? 7.355 40.066 -8.304 1.00 34.42 ? 284 LYS A C 1 ATOM 2270 O O . LYS A 1 284 ? 7.879 39.561 -7.314 1.00 34.72 ? 284 LYS A O 1 ATOM 2271 C CB . LYS A 1 284 ? 9.394 41.002 -9.360 1.00 36.13 ? 284 LYS A CB 1 ATOM 2272 C CG . LYS A 1 284 ? 10.367 41.119 -10.526 1.00 37.87 ? 284 LYS A CG 1 ATOM 2273 C CD . LYS A 1 284 ? 11.033 39.794 -10.841 1.00 40.23 ? 284 LYS A CD 1 ATOM 2274 C CE . LYS A 1 284 ? 12.225 39.967 -11.786 1.00 42.27 ? 284 LYS A CE 1 ATOM 2275 N NZ . LYS A 1 284 ? 13.433 40.557 -11.112 1.00 41.71 ? 284 LYS A NZ 1 ATOM 2276 N N . ASN A 1 285 ? 6.115 40.544 -8.291 1.00 33.87 ? 285 ASN A N 1 ATOM 2277 C CA . ASN A 1 285 ? 5.304 40.498 -7.078 1.00 33.70 ? 285 ASN A CA 1 ATOM 2278 C C . ASN A 1 285 ? 6.001 41.156 -5.893 1.00 31.51 ? 285 ASN A C 1 ATOM 2279 O O . ASN A 1 285 ? 6.154 40.554 -4.827 1.00 29.95 ? 285 ASN A O 1 ATOM 2280 C CB . ASN A 1 285 ? 4.949 39.052 -6.737 1.00 37.41 ? 285 ASN A CB 1 ATOM 2281 C CG . ASN A 1 285 ? 3.656 38.620 -7.382 1.00 43.02 ? 285 ASN A CG 1 ATOM 2282 O OD1 . ASN A 1 285 ? 2.574 38.987 -6.919 1.00 45.74 ? 285 ASN A OD1 1 ATOM 2283 N ND2 . ASN A 1 285 ? 3.754 37.863 -8.474 1.00 43.78 ? 285 ASN A ND2 1 ATOM 2284 N N . ARG A 1 286 ? 6.415 42.403 -6.091 1.00 28.75 ? 286 ARG A N 1 ATOM 2285 C CA . ARG A 1 286 ? 7.096 43.166 -5.052 1.00 27.05 ? 286 ARG A CA 1 ATOM 2286 C C . ARG A 1 286 ? 6.635 44.610 -5.131 1.00 24.87 ? 286 ARG A C 1 ATOM 2287 O O . ARG A 1 286 ? 6.105 45.047 -6.156 1.00 25.06 ? 286 ARG A O 1 ATOM 2288 C CB . ARG A 1 286 ? 8.609 43.119 -5.279 1.00 25.08 ? 286 ARG A CB 1 ATOM 2289 C CG . ARG A 1 286 ? 8.999 43.734 -6.609 1.00 24.24 ? 286 ARG A CG 1 ATOM 2290 C CD . ARG A 1 286 ? 10.478 43.599 -6.924 1.00 25.35 ? 286 ARG A CD 1 ATOM 2291 N NE . ARG A 1 286 ? 10.723 44.001 -8.305 1.00 23.45 ? 286 ARG A NE 1 ATOM 2292 C CZ . ARG A 1 286 ? 11.905 43.962 -8.909 1.00 24.46 ? 286 ARG A CZ 1 ATOM 2293 N NH1 . ARG A 1 286 ? 12.980 43.537 -8.257 1.00 20.58 ? 286 ARG A NH1 1 ATOM 2294 N NH2 . ARG A 1 286 ? 12.004 44.352 -10.175 1.00 23.55 ? 286 ARG A NH2 1 ATOM 2295 N N . ARG A 1 287 ? 6.818 45.345 -4.043 1.00 22.96 ? 287 ARG A N 1 ATOM 2296 C CA . ARG A 1 287 ? 6.468 46.759 -4.033 1.00 21.86 ? 287 ARG A CA 1 ATOM 2297 C C . ARG A 1 287 ? 7.815 47.467 -4.078 1.00 21.77 ? 287 ARG A C 1 ATOM 2298 O O . ARG A 1 287 ? 8.710 47.171 -3.282 1.00 20.57 ? 287 ARG A O 1 ATOM 2299 C CB . ARG A 1 287 ? 5.704 47.136 -2.764 1.00 21.38 ? 287 ARG A CB 1 ATOM 2300 C CG . ARG A 1 287 ? 5.394 48.626 -2.652 1.00 21.11 ? 287 ARG A CG 1 ATOM 2301 C CD . ARG A 1 287 ? 4.258 48.863 -1.673 1.00 21.56 ? 287 ARG A CD 1 ATOM 2302 N NE . ARG A 1 287 ? 2.984 48.421 -2.234 1.00 22.05 ? 287 ARG A NE 1 ATOM 2303 C CZ . ARG A 1 287 ? 2.234 49.146 -3.060 1.00 21.73 ? 287 ARG A CZ 1 ATOM 2304 N NH1 . ARG A 1 287 ? 2.616 50.366 -3.421 1.00 18.98 ? 287 ARG A NH1 1 ATOM 2305 N NH2 . ARG A 1 287 ? 1.108 48.638 -3.549 1.00 22.74 ? 287 ARG A NH2 1 ATOM 2306 N N . VAL A 1 288 ? 7.965 48.377 -5.031 1.00 20.20 ? 288 VAL A N 1 ATOM 2307 C CA . VAL A 1 288 ? 9.210 49.098 -5.198 1.00 20.82 ? 288 VAL A CA 1 ATOM 2308 C C . VAL A 1 288 ? 9.066 50.538 -4.739 1.00 22.94 ? 288 VAL A C 1 ATOM 2309 O O . VAL A 1 288 ? 8.076 51.216 -5.052 1.00 22.79 ? 288 VAL A O 1 ATOM 2310 C CB . VAL A 1 288 ? 9.658 49.054 -6.671 1.00 21.43 ? 288 VAL A CB 1 ATOM 2311 C CG1 . VAL A 1 288 ? 10.982 49.793 -6.853 1.00 19.85 ? 288 VAL A CG1 1 ATOM 2312 C CG2 . VAL A 1 288 ? 9.788 47.608 -7.107 1.00 19.66 ? 288 VAL A CG2 1 ATOM 2313 N N . LEU A 1 289 ? 10.065 50.999 -3.994 1.00 22.58 ? 289 LEU A N 1 ATOM 2314 C CA . LEU A 1 289 ? 10.064 52.348 -3.454 1.00 23.23 ? 289 LEU A CA 1 ATOM 2315 C C . LEU A 1 289 ? 11.119 53.242 -4.092 1.00 23.96 ? 289 LEU A C 1 ATOM 2316 O O . LEU A 1 289 ? 12.290 52.858 -4.193 1.00 25.67 ? 289 LEU A O 1 ATOM 2317 C CB . LEU A 1 289 ? 10.303 52.294 -1.940 1.00 23.04 ? 289 LEU A CB 1 ATOM 2318 C CG . LEU A 1 289 ? 10.224 53.613 -1.164 1.00 23.98 ? 289 LEU A CG 1 ATOM 2319 C CD1 . LEU A 1 289 ? 8.775 54.091 -1.131 1.00 21.44 ? 289 LEU A CD1 1 ATOM 2320 C CD2 . LEU A 1 289 ? 10.750 53.412 0.256 1.00 22.22 ? 289 LEU A CD2 1 ATOM 2321 N N . TRP A 1 290 ? 10.685 54.427 -4.524 1.00 22.50 ? 290 TRP A N 1 ATOM 2322 C CA . TRP A 1 290 ? 11.556 55.443 -5.114 1.00 21.29 ? 290 TRP A CA 1 ATOM 2323 C C . TRP A 1 290 ? 11.573 56.642 -4.159 1.00 22.54 ? 290 TRP A C 1 ATOM 2324 O O . TRP A 1 290 ? 10.571 56.926 -3.494 1.00 21.59 ? 290 TRP A O 1 ATOM 2325 C CB . TRP A 1 290 ? 11.008 55.955 -6.447 1.00 22.40 ? 290 TRP A CB 1 ATOM 2326 C CG . TRP A 1 290 ? 11.215 55.088 -7.649 1.00 21.56 ? 290 TRP A CG 1 ATOM 2327 C CD1 . TRP A 1 290 ? 10.286 54.289 -8.253 1.00 21.21 ? 290 TRP A CD1 1 ATOM 2328 C CD2 . TRP A 1 290 ? 12.389 55.024 -8.462 1.00 21.49 ? 290 TRP A CD2 1 ATOM 2329 N NE1 . TRP A 1 290 ? 10.807 53.741 -9.403 1.00 23.54 ? 290 TRP A NE1 1 ATOM 2330 C CE2 . TRP A 1 290 ? 12.097 54.176 -9.555 1.00 22.25 ? 290 TRP A CE2 1 ATOM 2331 C CE3 . TRP A 1 290 ? 13.661 55.609 -8.380 1.00 21.02 ? 290 TRP A CE3 1 ATOM 2332 C CZ2 . TRP A 1 290 ? 13.030 53.898 -10.560 1.00 21.71 ? 290 TRP A CZ2 1 ATOM 2333 C CZ3 . TRP A 1 290 ? 14.591 55.333 -9.383 1.00 21.91 ? 290 TRP A CZ3 1 ATOM 2334 C CH2 . TRP A 1 290 ? 14.267 54.485 -10.459 1.00 21.92 ? 290 TRP A CH2 1 ATOM 2335 N N . ALA A 1 291 ? 12.695 57.351 -4.097 1.00 20.75 ? 291 ALA A N 1 ATOM 2336 C CA . ALA A 1 291 ? 12.779 58.531 -3.246 1.00 22.40 ? 291 ALA A CA 1 ATOM 2337 C C . ALA A 1 291 ? 13.764 59.558 -3.782 1.00 22.24 ? 291 ALA A C 1 ATOM 2338 O O . ALA A 1 291 ? 14.816 59.214 -4.324 1.00 22.85 ? 291 ALA A O 1 ATOM 2339 C CB . ALA A 1 291 ? 13.165 58.142 -1.823 1.00 20.89 ? 291 ALA A CB 1 ATOM 2340 N N . TRP A 1 292 ? 13.406 60.828 -3.637 1.00 22.04 ? 292 TRP A N 1 ATOM 2341 C CA . TRP A 1 292 ? 14.268 61.913 -4.071 1.00 21.28 ? 292 TRP A CA 1 ATOM 2342 C C . TRP A 1 292 ? 15.336 62.109 -2.997 1.00 20.79 ? 292 TRP A C 1 ATOM 2343 O O . TRP A 1 292 ? 15.035 62.103 -1.805 1.00 20.63 ? 292 TRP A O 1 ATOM 2344 C CB . TRP A 1 292 ? 13.439 63.192 -4.246 1.00 21.62 ? 292 TRP A CB 1 ATOM 2345 C CG . TRP A 1 292 ? 14.236 64.473 -4.357 1.00 22.94 ? 292 TRP A CG 1 ATOM 2346 C CD1 . TRP A 1 292 ? 15.399 64.670 -5.060 1.00 21.58 ? 292 TRP A CD1 1 ATOM 2347 C CD2 . TRP A 1 292 ? 13.904 65.739 -3.772 1.00 21.83 ? 292 TRP A CD2 1 ATOM 2348 N NE1 . TRP A 1 292 ? 15.808 65.979 -4.944 1.00 21.94 ? 292 TRP A NE1 1 ATOM 2349 C CE2 . TRP A 1 292 ? 14.911 66.657 -4.159 1.00 22.49 ? 292 TRP A CE2 1 ATOM 2350 C CE3 . TRP A 1 292 ? 12.854 66.188 -2.958 1.00 22.08 ? 292 TRP A CE3 1 ATOM 2351 C CZ2 . TRP A 1 292 ? 14.899 68.002 -3.757 1.00 22.74 ? 292 TRP A CZ2 1 ATOM 2352 C CZ3 . TRP A 1 292 ? 12.840 67.527 -2.557 1.00 24.05 ? 292 TRP A CZ3 1 ATOM 2353 C CH2 . TRP A 1 292 ? 13.860 68.417 -2.960 1.00 23.09 ? 292 TRP A CH2 1 ATOM 2354 N N . VAL A 1 293 ? 16.588 62.236 -3.417 1.00 20.56 ? 293 VAL A N 1 ATOM 2355 C CA . VAL A 1 293 ? 17.670 62.472 -2.471 1.00 21.42 ? 293 VAL A CA 1 ATOM 2356 C C . VAL A 1 293 ? 18.246 63.844 -2.819 1.00 22.21 ? 293 VAL A C 1 ATOM 2357 O O . VAL A 1 293 ? 19.006 63.991 -3.778 1.00 19.95 ? 293 VAL A O 1 ATOM 2358 C CB . VAL A 1 293 ? 18.770 61.398 -2.571 1.00 21.35 ? 293 VAL A CB 1 ATOM 2359 C CG1 . VAL A 1 293 ? 19.835 61.661 -1.523 1.00 19.58 ? 293 VAL A CG1 1 ATOM 2360 C CG2 . VAL A 1 293 ? 18.167 60.014 -2.366 1.00 19.28 ? 293 VAL A CG2 1 ATOM 2361 N N . PRO A 1 294 ? 17.866 64.873 -2.046 1.00 22.39 ? 294 PRO A N 1 ATOM 2362 C CA . PRO A 1 294 ? 18.327 66.249 -2.260 1.00 23.30 ? 294 PRO A CA 1 ATOM 2363 C C . PRO A 1 294 ? 19.839 66.400 -2.184 1.00 24.98 ? 294 PRO A C 1 ATOM 2364 O O . PRO A 1 294 ? 20.542 65.523 -1.679 1.00 24.29 ? 294 PRO A O 1 ATOM 2365 C CB . PRO A 1 294 ? 17.639 67.031 -1.134 1.00 22.50 ? 294 PRO A CB 1 ATOM 2366 C CG . PRO A 1 294 ? 16.433 66.202 -0.795 1.00 21.74 ? 294 PRO A CG 1 ATOM 2367 C CD . PRO A 1 294 ? 16.980 64.796 -0.870 1.00 23.01 ? 294 PRO A CD 1 ATOM 2368 N N . GLU A 1 295 ? 20.330 67.525 -2.690 1.00 25.87 ? 295 GLU A N 1 ATOM 2369 C CA . GLU A 1 295 ? 21.752 67.840 -2.640 1.00 27.65 ? 295 GLU A CA 1 ATOM 2370 C C . GLU A 1 295 ? 21.997 68.416 -1.246 1.00 28.11 ? 295 GLU A C 1 ATOM 2371 O O . GLU A 1 295 ? 21.071 68.940 -0.622 1.00 28.21 ? 295 GLU A O 1 ATOM 2372 C CB . GLU A 1 295 ? 22.096 68.921 -3.665 1.00 27.87 ? 295 GLU A CB 1 ATOM 2373 C CG . GLU A 1 295 ? 21.882 68.528 -5.105 1.00 28.92 ? 295 GLU A CG 1 ATOM 2374 C CD . GLU A 1 295 ? 22.838 67.451 -5.534 1.00 30.32 ? 295 GLU A CD 1 ATOM 2375 O OE1 . GLU A 1 295 ? 24.061 67.677 -5.417 1.00 30.16 ? 295 GLU A OE1 1 ATOM 2376 O OE2 . GLU A 1 295 ? 22.372 66.382 -5.981 1.00 31.66 ? 295 GLU A OE2 1 ATOM 2377 N N . THR A 1 296 ? 23.222 68.302 -0.744 1.00 27.95 ? 296 THR A N 1 ATOM 2378 C CA . THR A 1 296 ? 23.544 68.893 0.550 1.00 27.46 ? 296 THR A CA 1 ATOM 2379 C C . THR A 1 296 ? 24.708 69.859 0.360 1.00 27.82 ? 296 THR A C 1 ATOM 2380 O O . THR A 1 296 ? 25.328 70.307 1.323 1.00 29.03 ? 296 THR A O 1 ATOM 2381 C CB . THR A 1 296 ? 23.893 67.849 1.637 1.00 26.37 ? 296 THR A CB 1 ATOM 2382 O OG1 . THR A 1 296 ? 24.888 66.944 1.146 1.00 28.64 ? 296 THR A OG1 1 ATOM 2383 C CG2 . THR A 1 296 ? 22.647 67.086 2.053 1.00 24.88 ? 296 THR A CG2 1 ATOM 2384 N N . ASP A 1 297 ? 25.015 70.163 -0.899 1.00 27.67 ? 297 ASP A N 1 ATOM 2385 C CA . ASP A 1 297 ? 26.054 71.136 -1.195 1.00 28.35 ? 297 ASP A CA 1 ATOM 2386 C C . ASP A 1 297 ? 25.277 72.452 -1.362 1.00 28.70 ? 297 ASP A C 1 ATOM 2387 O O . ASP A 1 297 ? 24.063 72.475 -1.144 1.00 27.52 ? 297 ASP A O 1 ATOM 2388 C CB . ASP A 1 297 ? 26.838 70.748 -2.461 1.00 27.57 ? 297 ASP A CB 1 ATOM 2389 C CG . ASP A 1 297 ? 25.974 70.690 -3.704 1.00 29.35 ? 297 ASP A CG 1 ATOM 2390 O OD1 . ASP A 1 297 ? 24.745 70.880 -3.596 1.00 30.00 ? 297 ASP A OD1 1 ATOM 2391 O OD2 . ASP A 1 297 ? 26.535 70.451 -4.797 1.00 27.96 ? 297 ASP A OD2 1 ATOM 2392 N N . SER A 1 298 ? 25.941 73.542 -1.728 1.00 29.65 ? 298 SER A N 1 ATOM 2393 C CA . SER A 1 298 ? 25.234 74.820 -1.856 1.00 30.04 ? 298 SER A CA 1 ATOM 2394 C C . SER A 1 298 ? 24.560 75.009 -3.210 1.00 30.90 ? 298 SER A C 1 ATOM 2395 O O . SER A 1 298 ? 24.911 74.348 -4.195 1.00 29.63 ? 298 SER A O 1 ATOM 2396 C CB . SER A 1 298 ? 26.197 75.986 -1.631 1.00 29.65 ? 298 SER A CB 1 ATOM 2397 O OG . SER A 1 298 ? 27.021 76.179 -2.772 1.00 29.68 ? 298 SER A OG 1 ATOM 2398 N N . GLN A 1 299 ? 23.600 75.929 -3.260 1.00 31.00 ? 299 GLN A N 1 ATOM 2399 C CA . GLN A 1 299 ? 22.908 76.207 -4.509 1.00 32.83 ? 299 GLN A CA 1 ATOM 2400 C C . GLN A 1 299 ? 23.915 76.670 -5.554 1.00 32.37 ? 299 GLN A C 1 ATOM 2401 O O . GLN A 1 299 ? 23.819 76.316 -6.728 1.00 33.23 ? 299 GLN A O 1 ATOM 2402 C CB . GLN A 1 299 ? 21.848 77.285 -4.315 1.00 34.08 ? 299 GLN A CB 1 ATOM 2403 C CG . GLN A 1 299 ? 21.264 77.761 -5.630 1.00 37.51 ? 299 GLN A CG 1 ATOM 2404 C CD . GLN A 1 299 ? 20.093 78.688 -5.441 1.00 40.34 ? 299 GLN A CD 1 ATOM 2405 O OE1 . GLN A 1 299 ? 19.029 78.275 -4.976 1.00 41.62 ? 299 GLN A OE1 1 ATOM 2406 N NE2 . GLN A 1 299 ? 20.279 79.955 -5.795 1.00 41.28 ? 299 GLN A NE2 1 ATOM 2407 N N . ALA A 1 300 ? 24.879 77.474 -5.120 1.00 32.40 ? 300 ALA A N 1 ATOM 2408 C CA . ALA A 1 300 ? 25.907 77.963 -6.024 1.00 31.87 ? 300 ALA A CA 1 ATOM 2409 C C . ALA A 1 300 ? 26.659 76.761 -6.573 1.00 31.69 ? 300 ALA A C 1 ATOM 2410 O O . ALA A 1 300 ? 27.027 76.744 -7.744 1.00 32.54 ? 300 ALA A O 1 ATOM 2411 C CB . ALA A 1 300 ? 26.864 78.895 -5.286 1.00 30.13 ? 300 ALA A CB 1 ATOM 2412 N N . ASP A 1 301 ? 26.891 75.756 -5.727 1.00 32.79 ? 301 ASP A N 1 ATOM 2413 C CA . ASP A 1 301 ? 27.596 74.552 -6.169 1.00 33.30 ? 301 ASP A CA 1 ATOM 2414 C C . ASP A 1 301 ? 26.783 73.838 -7.244 1.00 32.60 ? 301 ASP A C 1 ATOM 2415 O O . ASP A 1 301 ? 27.339 73.344 -8.229 1.00 32.18 ? 301 ASP A O 1 ATOM 2416 C CB . ASP A 1 301 ? 27.834 73.576 -5.007 1.00 35.18 ? 301 ASP A CB 1 ATOM 2417 C CG . ASP A 1 301 ? 28.818 74.106 -3.982 1.00 38.38 ? 301 ASP A CG 1 ATOM 2418 O OD1 . ASP A 1 301 ? 29.845 74.691 -4.387 1.00 41.19 ? 301 ASP A OD1 1 ATOM 2419 O OD2 . ASP A 1 301 ? 28.572 73.923 -2.769 1.00 40.29 ? 301 ASP A OD2 1 ATOM 2420 N N . ASP A 1 302 ? 25.465 73.789 -7.045 1.00 31.19 ? 302 ASP A N 1 ATOM 2421 C CA . ASP A 1 302 ? 24.568 73.130 -7.987 1.00 30.41 ? 302 ASP A CA 1 ATOM 2422 C C . ASP A 1 302 ? 24.583 73.820 -9.336 1.00 29.99 ? 302 ASP A C 1 ATOM 2423 O O . ASP A 1 302 ? 24.700 73.171 -10.376 1.00 30.06 ? 302 ASP A O 1 ATOM 2424 C CB . ASP A 1 302 ? 23.137 73.102 -7.442 1.00 28.53 ? 302 ASP A CB 1 ATOM 2425 C CG . ASP A 1 302 ? 23.021 72.306 -6.156 1.00 29.27 ? 302 ASP A CG 1 ATOM 2426 O OD1 . ASP A 1 302 ? 23.865 71.410 -5.935 1.00 27.59 ? 302 ASP A OD1 1 ATOM 2427 O OD2 . ASP A 1 302 ? 22.083 72.566 -5.373 1.00 28.86 ? 302 ASP A OD2 1 ATOM 2428 N N . ILE A 1 303 ? 24.457 75.140 -9.313 1.00 31.12 ? 303 ILE A N 1 ATOM 2429 C CA . ILE A 1 303 ? 24.466 75.925 -10.537 1.00 32.11 ? 303 ILE A CA 1 ATOM 2430 C C . ILE A 1 303 ? 25.811 75.746 -11.223 1.00 33.53 ? 303 ILE A C 1 ATOM 2431 O O . ILE A 1 303 ? 25.893 75.688 -12.449 1.00 34.67 ? 303 ILE A O 1 ATOM 2432 C CB . ILE A 1 303 ? 24.237 77.418 -10.228 1.00 32.52 ? 303 ILE A CB 1 ATOM 2433 C CG1 . ILE A 1 303 ? 22.810 77.619 -9.716 1.00 31.39 ? 303 ILE A CG1 1 ATOM 2434 C CG2 . ILE A 1 303 ? 24.486 78.259 -11.470 1.00 30.70 ? 303 ILE A CG2 1 ATOM 2435 C CD1 . ILE A 1 303 ? 22.570 78.981 -9.124 1.00 33.17 ? 303 ILE A CD1 1 ATOM 2436 N N . GLU A 1 304 ? 26.865 75.638 -10.426 1.00 33.91 ? 304 GLU A N 1 ATOM 2437 C CA . GLU A 1 304 ? 28.199 75.465 -10.972 1.00 36.57 ? 304 GLU A CA 1 ATOM 2438 C C . GLU A 1 304 ? 28.369 74.092 -11.634 1.00 35.97 ? 304 GLU A C 1 ATOM 2439 O O . GLU A 1 304 ? 28.843 74.010 -12.771 1.00 35.97 ? 304 GLU A O 1 ATOM 2440 C CB . GLU A 1 304 ? 29.247 75.668 -9.869 1.00 41.59 ? 304 GLU A CB 1 ATOM 2441 C CG . GLU A 1 304 ? 30.639 76.021 -10.381 1.00 48.72 ? 304 GLU A CG 1 ATOM 2442 C CD . GLU A 1 304 ? 31.353 74.846 -11.036 1.00 55.81 ? 304 GLU A CD 1 ATOM 2443 O OE1 . GLU A 1 304 ? 32.267 75.094 -11.856 1.00 59.18 ? 304 GLU A OE1 1 ATOM 2444 O OE2 . GLU A 1 304 ? 31.014 73.677 -10.725 1.00 58.43 ? 304 GLU A OE2 1 ATOM 2445 N N . LYS A 1 305 ? 27.985 73.013 -10.949 1.00 33.47 ? 305 LYS A N 1 ATOM 2446 C CA . LYS A 1 305 ? 28.140 71.690 -11.553 1.00 31.08 ? 305 LYS A CA 1 ATOM 2447 C C . LYS A 1 305 ? 27.062 71.394 -12.599 1.00 30.28 ? 305 LYS A C 1 ATOM 2448 O O . LYS A 1 305 ? 27.182 70.441 -13.371 1.00 29.64 ? 305 LYS A O 1 ATOM 2449 C CB . LYS A 1 305 ? 28.206 70.586 -10.481 1.00 30.12 ? 305 LYS A CB 1 ATOM 2450 C CG . LYS A 1 305 ? 26.949 70.297 -9.671 1.00 29.12 ? 305 LYS A CG 1 ATOM 2451 C CD . LYS A 1 305 ? 27.272 69.215 -8.627 1.00 28.58 ? 305 LYS A CD 1 ATOM 2452 C CE . LYS A 1 305 ? 26.028 68.593 -7.984 1.00 26.22 ? 305 LYS A CE 1 ATOM 2453 N NZ . LYS A 1 305 ? 25.281 69.524 -7.106 1.00 27.47 ? 305 LYS A NZ 1 ATOM 2454 N N . GLY A 1 306 ? 26.020 72.223 -12.629 1.00 29.72 ? 306 GLY A N 1 ATOM 2455 C CA . GLY A 1 306 ? 24.969 72.068 -13.623 1.00 28.29 ? 306 GLY A CA 1 ATOM 2456 C C . GLY A 1 306 ? 23.809 71.130 -13.351 1.00 29.31 ? 306 GLY A C 1 ATOM 2457 O O . GLY A 1 306 ? 22.975 70.918 -14.231 1.00 29.87 ? 306 GLY A O 1 ATOM 2458 N N . TRP A 1 307 ? 23.738 70.557 -12.155 1.00 27.84 ? 307 TRP A N 1 ATOM 2459 C CA . TRP A 1 307 ? 22.643 69.654 -11.841 1.00 26.82 ? 307 TRP A CA 1 ATOM 2460 C C . TRP A 1 307 ? 22.412 69.546 -10.346 1.00 26.87 ? 307 TRP A C 1 ATOM 2461 O O . TRP A 1 307 ? 23.256 69.937 -9.540 1.00 26.01 ? 307 TRP A O 1 ATOM 2462 C CB . TRP A 1 307 ? 22.908 68.255 -12.418 1.00 27.11 ? 307 TRP A CB 1 ATOM 2463 C CG . TRP A 1 307 ? 24.146 67.602 -11.886 1.00 27.09 ? 307 TRP A CG 1 ATOM 2464 C CD1 . TRP A 1 307 ? 25.415 67.734 -12.371 1.00 28.01 ? 307 TRP A CD1 1 ATOM 2465 C CD2 . TRP A 1 307 ? 24.244 66.761 -10.725 1.00 26.63 ? 307 TRP A CD2 1 ATOM 2466 N NE1 . TRP A 1 307 ? 26.300 67.028 -11.584 1.00 28.68 ? 307 TRP A NE1 1 ATOM 2467 C CE2 . TRP A 1 307 ? 25.608 66.422 -10.568 1.00 26.98 ? 307 TRP A CE2 1 ATOM 2468 C CE3 . TRP A 1 307 ? 23.312 66.265 -9.801 1.00 26.66 ? 307 TRP A CE3 1 ATOM 2469 C CZ2 . TRP A 1 307 ? 26.063 65.608 -9.522 1.00 25.86 ? 307 TRP A CZ2 1 ATOM 2470 C CZ3 . TRP A 1 307 ? 23.767 65.453 -8.756 1.00 24.76 ? 307 TRP A CZ3 1 ATOM 2471 C CH2 . TRP A 1 307 ? 25.130 65.136 -8.630 1.00 25.51 ? 307 TRP A CH2 1 ATOM 2472 N N . ALA A 1 308 ? 21.253 69.015 -9.979 1.00 26.55 ? 308 ALA A N 1 ATOM 2473 C CA . ALA A 1 308 ? 20.920 68.847 -8.578 1.00 26.27 ? 308 ALA A CA 1 ATOM 2474 C C . ALA A 1 308 ? 19.834 67.802 -8.425 1.00 25.42 ? 308 ALA A C 1 ATOM 2475 O O . ALA A 1 308 ? 18.876 67.769 -9.198 1.00 26.08 ? 308 ALA A O 1 ATOM 2476 C CB . ALA A 1 308 ? 20.460 70.177 -7.977 1.00 25.61 ? 308 ALA A CB 1 ATOM 2477 N N . GLY A 1 309 ? 19.999 66.943 -7.427 1.00 25.34 ? 309 GLY A N 1 ATOM 2478 C CA . GLY A 1 309 ? 19.013 65.915 -7.168 1.00 24.27 ? 309 GLY A CA 1 ATOM 2479 C C . GLY A 1 309 ? 19.330 64.545 -7.729 1.00 23.87 ? 309 GLY A C 1 ATOM 2480 O O . GLY A 1 309 ? 19.773 64.398 -8.870 1.00 23.10 ? 309 GLY A O 1 ATOM 2481 N N . LEU A 1 310 ? 19.098 63.535 -6.903 1.00 22.17 ? 310 LEU A N 1 ATOM 2482 C CA . LEU A 1 310 ? 19.311 62.152 -7.286 1.00 21.67 ? 310 LEU A CA 1 ATOM 2483 C C . LEU A 1 310 ? 18.078 61.400 -6.826 1.00 22.09 ? 310 LEU A C 1 ATOM 2484 O O . LEU A 1 310 ? 17.249 61.941 -6.092 1.00 21.62 ? 310 LEU A O 1 ATOM 2485 C CB . LEU A 1 310 ? 20.507 61.552 -6.544 1.00 21.63 ? 310 LEU A CB 1 ATOM 2486 C CG . LEU A 1 310 ? 21.932 62.048 -6.758 1.00 22.00 ? 310 LEU A CG 1 ATOM 2487 C CD1 . LEU A 1 310 ? 22.850 61.274 -5.823 1.00 20.33 ? 310 LEU A CD1 1 ATOM 2488 C CD2 . LEU A 1 310 ? 22.349 61.852 -8.208 1.00 21.00 ? 310 LEU A CD2 1 ATOM 2489 N N . GLN A 1 311 ? 17.954 60.158 -7.271 1.00 21.13 ? 311 GLN A N 1 ATOM 2490 C CA . GLN A 1 311 ? 16.872 59.300 -6.816 1.00 21.93 ? 311 GLN A CA 1 ATOM 2491 C C . GLN A 1 311 ? 17.631 58.226 -6.048 1.00 22.76 ? 311 GLN A C 1 ATOM 2492 O O . GLN A 1 311 ? 18.780 57.917 -6.378 1.00 22.29 ? 311 GLN A O 1 ATOM 2493 C CB . GLN A 1 311 ? 16.126 58.635 -7.979 1.00 21.68 ? 311 GLN A CB 1 ATOM 2494 C CG . GLN A 1 311 ? 15.202 59.537 -8.777 1.00 21.42 ? 311 GLN A CG 1 ATOM 2495 C CD . GLN A 1 311 ? 14.100 60.159 -7.932 1.00 23.94 ? 311 GLN A CD 1 ATOM 2496 O OE1 . GLN A 1 311 ? 13.450 59.480 -7.125 1.00 21.27 ? 311 GLN A OE1 1 ATOM 2497 N NE2 . GLN A 1 311 ? 13.874 61.456 -8.124 1.00 21.81 ? 311 GLN A NE2 1 ATOM 2498 N N . SER A 1 312 ? 17.021 57.678 -5.007 1.00 22.46 ? 312 SER A N 1 ATOM 2499 C CA . SER A 1 312 ? 17.661 56.602 -4.263 1.00 22.76 ? 312 SER A CA 1 ATOM 2500 C C . SER A 1 312 ? 17.609 55.385 -5.195 1.00 23.31 ? 312 SER A C 1 ATOM 2501 O O . SER A 1 312 ? 16.840 55.373 -6.162 1.00 22.10 ? 312 SER A O 1 ATOM 2502 C CB . SER A 1 312 ? 16.857 56.310 -3.002 1.00 22.29 ? 312 SER A CB 1 ATOM 2503 O OG . SER A 1 312 ? 15.488 56.160 -3.341 1.00 22.86 ? 312 SER A OG 1 ATOM 2504 N N . PHE A 1 313 ? 18.423 54.366 -4.941 1.00 23.48 ? 313 PHE A N 1 ATOM 2505 C CA . PHE A 1 313 ? 18.341 53.194 -5.796 1.00 22.80 ? 313 PHE A CA 1 ATOM 2506 C C . PHE A 1 313 ? 17.027 52.510 -5.404 1.00 23.46 ? 313 PHE A C 1 ATOM 2507 O O . PHE A 1 313 ? 16.762 52.293 -4.219 1.00 23.33 ? 313 PHE A O 1 ATOM 2508 C CB . PHE A 1 313 ? 19.510 52.244 -5.564 1.00 22.23 ? 313 PHE A CB 1 ATOM 2509 C CG . PHE A 1 313 ? 19.551 51.119 -6.550 1.00 23.43 ? 313 PHE A CG 1 ATOM 2510 C CD1 . PHE A 1 313 ? 20.056 51.320 -7.829 1.00 23.31 ? 313 PHE A CD1 1 ATOM 2511 C CD2 . PHE A 1 313 ? 18.996 49.888 -6.235 1.00 24.47 ? 313 PHE A CD2 1 ATOM 2512 C CE1 . PHE A 1 313 ? 20.003 50.316 -8.784 1.00 24.06 ? 313 PHE A CE1 1 ATOM 2513 C CE2 . PHE A 1 313 ? 18.938 48.874 -7.186 1.00 26.24 ? 313 PHE A CE2 1 ATOM 2514 C CZ . PHE A 1 313 ? 19.442 49.091 -8.464 1.00 25.83 ? 313 PHE A CZ 1 ATOM 2515 N N . PRO A 1 314 ? 16.185 52.164 -6.387 1.00 23.69 ? 314 PRO A N 1 ATOM 2516 C CA . PRO A 1 314 ? 14.905 51.514 -6.064 1.00 23.19 ? 314 PRO A CA 1 ATOM 2517 C C . PRO A 1 314 ? 14.999 50.331 -5.108 1.00 24.50 ? 314 PRO A C 1 ATOM 2518 O O . PRO A 1 314 ? 15.823 49.436 -5.291 1.00 24.30 ? 314 PRO A O 1 ATOM 2519 C CB . PRO A 1 314 ? 14.343 51.124 -7.437 1.00 22.59 ? 314 PRO A CB 1 ATOM 2520 C CG . PRO A 1 314 ? 15.534 51.122 -8.344 1.00 24.66 ? 314 PRO A CG 1 ATOM 2521 C CD . PRO A 1 314 ? 16.389 52.249 -7.843 1.00 24.61 ? 314 PRO A CD 1 ATOM 2522 N N . ARG A 1 315 ? 14.166 50.324 -4.071 1.00 24.56 ? 315 ARG A N 1 ATOM 2523 C CA . ARG A 1 315 ? 14.208 49.208 -3.144 1.00 25.04 ? 315 ARG A CA 1 ATOM 2524 C C . ARG A 1 315 ? 12.903 48.451 -2.962 1.00 25.33 ? 315 ARG A C 1 ATOM 2525 O O . ARG A 1 315 ? 11.815 49.025 -2.990 1.00 26.75 ? 315 ARG A O 1 ATOM 2526 C CB . ARG A 1 315 ? 14.776 49.638 -1.775 1.00 24.81 ? 315 ARG A CB 1 ATOM 2527 C CG . ARG A 1 315 ? 14.549 51.071 -1.341 1.00 25.63 ? 315 ARG A CG 1 ATOM 2528 C CD . ARG A 1 315 ? 15.861 51.737 -0.864 1.00 23.88 ? 315 ARG A CD 1 ATOM 2529 N NE . ARG A 1 315 ? 15.682 52.429 0.407 1.00 26.40 ? 315 ARG A NE 1 ATOM 2530 C CZ . ARG A 1 315 ? 16.535 53.296 0.955 1.00 25.20 ? 315 ARG A CZ 1 ATOM 2531 N NH1 . ARG A 1 315 ? 17.672 53.622 0.366 1.00 23.42 ? 315 ARG A NH1 1 ATOM 2532 N NH2 . ARG A 1 315 ? 16.236 53.846 2.118 1.00 24.19 ? 315 ARG A NH2 1 ATOM 2533 N N . ALA A 1 316 ? 13.028 47.134 -2.825 1.00 23.95 ? 316 ALA A N 1 ATOM 2534 C CA . ALA A 1 316 ? 11.876 46.278 -2.603 1.00 22.68 ? 316 ALA A CA 1 ATOM 2535 C C . ALA A 1 316 ? 11.444 46.637 -1.191 1.00 23.18 ? 316 ALA A C 1 ATOM 2536 O O . ALA A 1 316 ? 12.273 46.996 -0.346 1.00 21.48 ? 316 ALA A O 1 ATOM 2537 C CB . ALA A 1 316 ? 12.275 44.814 -2.687 1.00 21.05 ? 316 ALA A CB 1 ATOM 2538 N N . LEU A 1 317 ? 10.153 46.519 -0.927 1.00 23.67 ? 317 LEU A N 1 ATOM 2539 C CA . LEU A 1 317 ? 9.609 46.903 0.360 1.00 24.49 ? 317 LEU A CA 1 ATOM 2540 C C . LEU A 1 317 ? 8.616 45.881 0.897 1.00 24.59 ? 317 LEU A C 1 ATOM 2541 O O . LEU A 1 317 ? 7.754 45.414 0.160 1.00 25.38 ? 317 LEU A O 1 ATOM 2542 C CB . LEU A 1 317 ? 8.922 48.256 0.169 1.00 27.62 ? 317 LEU A CB 1 ATOM 2543 C CG . LEU A 1 317 ? 8.060 48.940 1.215 1.00 29.06 ? 317 LEU A CG 1 ATOM 2544 C CD1 . LEU A 1 317 ? 8.905 49.345 2.404 1.00 33.27 ? 317 LEU A CD1 1 ATOM 2545 C CD2 . LEU A 1 317 ? 7.442 50.168 0.582 1.00 30.06 ? 317 LEU A CD2 1 ATOM 2546 N N . TRP A 1 318 ? 8.734 45.536 2.176 1.00 23.00 ? 318 TRP A N 1 ATOM 2547 C CA . TRP A 1 318 ? 7.805 44.589 2.785 1.00 23.83 ? 318 TRP A CA 1 ATOM 2548 C C . TRP A 1 318 ? 7.760 44.766 4.303 1.00 25.19 ? 318 TRP A C 1 ATOM 2549 O O . TRP A 1 318 ? 8.553 45.518 4.871 1.00 24.56 ? 318 TRP A O 1 ATOM 2550 C CB . TRP A 1 318 ? 8.182 43.149 2.407 1.00 22.93 ? 318 TRP A CB 1 ATOM 2551 C CG . TRP A 1 318 ? 9.500 42.672 2.937 1.00 22.75 ? 318 TRP A CG 1 ATOM 2552 C CD1 . TRP A 1 318 ? 9.735 42.106 4.155 1.00 22.70 ? 318 TRP A CD1 1 ATOM 2553 C CD2 . TRP A 1 318 ? 10.767 42.713 2.262 1.00 21.25 ? 318 TRP A CD2 1 ATOM 2554 N NE1 . TRP A 1 318 ? 11.067 41.787 4.281 1.00 21.93 ? 318 TRP A NE1 1 ATOM 2555 C CE2 . TRP A 1 318 ? 11.724 42.148 3.136 1.00 21.34 ? 318 TRP A CE2 1 ATOM 2556 C CE3 . TRP A 1 318 ? 11.186 43.172 1.002 1.00 22.04 ? 318 TRP A CE3 1 ATOM 2557 C CZ2 . TRP A 1 318 ? 13.079 42.028 2.794 1.00 21.29 ? 318 TRP A CZ2 1 ATOM 2558 C CZ3 . TRP A 1 318 ? 12.536 43.054 0.658 1.00 21.65 ? 318 TRP A CZ3 1 ATOM 2559 C CH2 . TRP A 1 318 ? 13.465 42.485 1.554 1.00 22.78 ? 318 TRP A CH2 1 ATOM 2560 N N . ILE A 1 319 ? 6.823 44.093 4.962 1.00 26.32 ? 319 ILE A N 1 ATOM 2561 C CA . ILE A 1 319 ? 6.708 44.224 6.407 1.00 28.46 ? 319 ILE A CA 1 ATOM 2562 C C . ILE A 1 319 ? 7.541 43.176 7.122 1.00 29.62 ? 319 ILE A C 1 ATOM 2563 O O . ILE A 1 319 ? 7.647 42.036 6.677 1.00 29.75 ? 319 ILE A O 1 ATOM 2564 C CB . ILE A 1 319 ? 5.236 44.119 6.874 1.00 29.28 ? 319 ILE A CB 1 ATOM 2565 C CG1 . ILE A 1 319 ? 5.113 44.618 8.316 1.00 28.98 ? 319 ILE A CG1 1 ATOM 2566 C CG2 . ILE A 1 319 ? 4.748 42.679 6.773 1.00 27.90 ? 319 ILE A CG2 1 ATOM 2567 C CD1 . ILE A 1 319 ? 3.675 44.800 8.775 1.00 27.56 ? 319 ILE A CD1 1 ATOM 2568 N N . ASP A 1 320 ? 8.145 43.580 8.230 1.00 31.54 ? 320 ASP A N 1 ATOM 2569 C CA . ASP A 1 320 ? 8.982 42.692 9.019 1.00 32.86 ? 320 ASP A CA 1 ATOM 2570 C C . ASP A 1 320 ? 8.179 41.565 9.672 1.00 34.74 ? 320 ASP A C 1 ATOM 2571 O O . ASP A 1 320 ? 6.969 41.677 9.869 1.00 33.11 ? 320 ASP A O 1 ATOM 2572 C CB . ASP A 1 320 ? 9.699 43.498 10.105 1.00 32.45 ? 320 ASP A CB 1 ATOM 2573 C CG . ASP A 1 320 ? 10.619 42.643 10.954 1.00 32.97 ? 320 ASP A CG 1 ATOM 2574 O OD1 . ASP A 1 320 ? 11.711 42.264 10.481 1.00 36.19 ? 320 ASP A OD1 1 ATOM 2575 O OD2 . ASP A 1 320 ? 10.243 42.335 12.097 1.00 33.84 ? 320 ASP A OD2 1 ATOM 2576 N N . ARG A 1 321 ? 8.875 40.481 9.998 1.00 38.21 ? 321 ARG A N 1 ATOM 2577 C CA . ARG A 1 321 ? 8.291 39.314 10.658 1.00 41.53 ? 321 ARG A CA 1 ATOM 2578 C C . ARG A 1 321 ? 7.482 39.752 11.891 1.00 39.98 ? 321 ARG A C 1 ATOM 2579 O O . ARG A 1 321 ? 6.374 39.267 12.112 1.00 39.12 ? 321 ARG A O 1 ATOM 2580 C CB . ARG A 1 321 ? 9.422 38.372 11.091 1.00 47.33 ? 321 ARG A CB 1 ATOM 2581 C CG . ARG A 1 321 ? 10.484 39.126 11.910 1.00 58.49 ? 321 ARG A CG 1 ATOM 2582 C CD . ARG A 1 321 ? 11.841 38.426 12.046 1.00 65.46 ? 321 ARG A CD 1 ATOM 2583 N NE . ARG A 1 321 ? 12.897 39.405 12.341 1.00 70.94 ? 321 ARG A NE 1 ATOM 2584 C CZ . ARG A 1 321 ? 14.161 39.098 12.634 1.00 74.12 ? 321 ARG A CZ 1 ATOM 2585 N NH1 . ARG A 1 321 ? 14.547 37.829 12.682 1.00 75.48 ? 321 ARG A NH1 1 ATOM 2586 N NH2 . ARG A 1 321 ? 15.047 40.063 12.867 1.00 75.83 ? 321 ARG A NH2 1 ATOM 2587 N N . ASN A 1 322 ? 8.041 40.672 12.682 1.00 38.11 ? 322 ASN A N 1 ATOM 2588 C CA . ASN A 1 322 ? 7.380 41.163 13.893 1.00 37.45 ? 322 ASN A CA 1 ATOM 2589 C C . ASN A 1 322 ? 6.174 42.053 13.621 1.00 35.66 ? 322 ASN A C 1 ATOM 2590 O O . ASN A 1 322 ? 5.460 42.425 14.548 1.00 36.97 ? 322 ASN A O 1 ATOM 2591 C CB . ASN A 1 322 ? 8.367 41.930 14.792 1.00 41.02 ? 322 ASN A CB 1 ATOM 2592 C CG . ASN A 1 322 ? 8.854 43.259 14.168 1.00 46.63 ? 322 ASN A CG 1 ATOM 2593 O OD1 . ASN A 1 322 ? 8.094 43.988 13.518 1.00 45.29 ? 322 ASN A OD1 1 ATOM 2594 N ND2 . ASN A 1 322 ? 10.130 43.580 14.393 1.00 49.76 ? 322 ASN A ND2 1 ATOM 2595 N N . GLY A 1 323 ? 5.968 42.414 12.358 1.00 33.94 ? 323 GLY A N 1 ATOM 2596 C CA . GLY A 1 323 ? 4.838 43.249 11.981 1.00 31.21 ? 323 GLY A CA 1 ATOM 2597 C C . GLY A 1 323 ? 4.808 44.678 12.501 1.00 31.16 ? 323 GLY A C 1 ATOM 2598 O O . GLY A 1 323 ? 3.807 45.365 12.335 1.00 30.52 ? 323 GLY A O 1 ATOM 2599 N N . LYS A 1 324 ? 5.898 45.143 13.103 1.00 32.49 ? 324 LYS A N 1 ATOM 2600 C CA . LYS A 1 324 ? 5.943 46.491 13.663 1.00 33.41 ? 324 LYS A CA 1 ATOM 2601 C C . LYS A 1 324 ? 6.654 47.545 12.821 1.00 32.12 ? 324 LYS A C 1 ATOM 2602 O O . LYS A 1 324 ? 6.616 48.734 13.150 1.00 32.21 ? 324 LYS A O 1 ATOM 2603 C CB . LYS A 1 324 ? 6.573 46.448 15.059 1.00 37.84 ? 324 LYS A CB 1 ATOM 2604 C CG . LYS A 1 324 ? 5.731 45.701 16.088 1.00 44.50 ? 324 LYS A CG 1 ATOM 2605 C CD . LYS A 1 324 ? 6.393 45.671 17.467 1.00 50.53 ? 324 LYS A CD 1 ATOM 2606 C CE . LYS A 1 324 ? 7.686 44.850 17.460 1.00 55.57 ? 324 LYS A CE 1 ATOM 2607 N NZ . LYS A 1 324 ? 8.301 44.724 18.823 1.00 57.65 ? 324 LYS A NZ 1 ATOM 2608 N N . GLN A 1 325 ? 7.309 47.120 11.746 1.00 29.13 ? 325 GLN A N 1 ATOM 2609 C CA . GLN A 1 325 ? 8.002 48.060 10.874 1.00 26.48 ? 325 GLN A CA 1 ATOM 2610 C C . GLN A 1 325 ? 8.203 47.479 9.489 1.00 25.95 ? 325 GLN A C 1 ATOM 2611 O O . GLN A 1 325 ? 8.036 46.281 9.266 1.00 25.79 ? 325 GLN A O 1 ATOM 2612 C CB . GLN A 1 325 ? 9.371 48.440 11.444 1.00 24.51 ? 325 GLN A CB 1 ATOM 2613 C CG . GLN A 1 325 ? 10.356 47.287 11.483 1.00 26.34 ? 325 GLN A CG 1 ATOM 2614 C CD . GLN A 1 325 ? 11.785 47.746 11.697 1.00 28.80 ? 325 GLN A CD 1 ATOM 2615 O OE1 . GLN A 1 325 ? 12.398 48.348 10.814 1.00 29.97 ? 325 GLN A OE1 1 ATOM 2616 N NE2 . GLN A 1 325 ? 12.321 47.469 12.877 1.00 29.37 ? 325 GLN A NE2 1 ATOM 2617 N N . LEU A 1 326 ? 8.578 48.353 8.566 1.00 25.57 ? 326 LEU A N 1 ATOM 2618 C CA . LEU A 1 326 ? 8.832 47.980 7.186 1.00 24.97 ? 326 LEU A CA 1 ATOM 2619 C C . LEU A 1 326 ? 10.309 47.640 7.001 1.00 24.30 ? 326 LEU A C 1 ATOM 2620 O O . LEU A 1 326 ? 11.163 48.095 7.764 1.00 24.39 ? 326 LEU A O 1 ATOM 2621 C CB . LEU A 1 326 ? 8.445 49.141 6.266 1.00 25.21 ? 326 LEU A CB 1 ATOM 2622 C CG . LEU A 1 326 ? 7.060 49.168 5.605 1.00 26.52 ? 326 LEU A CG 1 ATOM 2623 C CD1 . LEU A 1 326 ? 6.067 48.319 6.362 1.00 25.89 ? 326 LEU A CD1 1 ATOM 2624 C CD2 . LEU A 1 326 ? 6.595 50.607 5.509 1.00 24.53 ? 326 LEU A CD2 1 ATOM 2625 N N . ILE A 1 327 ? 10.590 46.825 5.990 1.00 23.62 ? 327 ILE A N 1 ATOM 2626 C CA . ILE A 1 327 ? 11.947 46.416 5.653 1.00 22.22 ? 327 ILE A CA 1 ATOM 2627 C C . ILE A 1 327 ? 12.181 46.861 4.212 1.00 23.66 ? 327 ILE A C 1 ATOM 2628 O O . ILE A 1 327 ? 11.270 46.757 3.384 1.00 23.38 ? 327 ILE A O 1 ATOM 2629 C CB . ILE A 1 327 ? 12.103 44.881 5.696 1.00 22.71 ? 327 ILE A CB 1 ATOM 2630 C CG1 . ILE A 1 327 ? 11.803 44.350 7.102 1.00 22.56 ? 327 ILE A CG1 1 ATOM 2631 C CG2 . ILE A 1 327 ? 13.508 44.489 5.243 1.00 21.33 ? 327 ILE A CG2 1 ATOM 2632 C CD1 . ILE A 1 327 ? 12.774 44.803 8.160 1.00 21.38 ? 327 ILE A CD1 1 ATOM 2633 N N . GLN A 1 328 ? 13.387 47.353 3.918 1.00 22.86 ? 328 GLN A N 1 ATOM 2634 C CA . GLN A 1 328 ? 13.748 47.797 2.566 1.00 21.72 ? 328 GLN A CA 1 ATOM 2635 C C . GLN A 1 328 ? 15.052 47.145 2.114 1.00 21.37 ? 328 GLN A C 1 ATOM 2636 O O . GLN A 1 328 ? 15.937 46.880 2.929 1.00 21.37 ? 328 GLN A O 1 ATOM 2637 C CB . GLN A 1 328 ? 13.933 49.309 2.521 1.00 21.79 ? 328 GLN A CB 1 ATOM 2638 C CG . GLN A 1 328 ? 12.668 50.122 2.610 1.00 22.90 ? 328 GLN A CG 1 ATOM 2639 C CD . GLN A 1 328 ? 12.945 51.480 3.218 1.00 23.80 ? 328 GLN A CD 1 ATOM 2640 O OE1 . GLN A 1 328 ? 12.944 51.634 4.445 1.00 23.86 ? 328 GLN A OE1 1 ATOM 2641 N NE2 . GLN A 1 328 ? 13.223 52.463 2.371 1.00 20.44 ? 328 GLN A NE2 1 ATOM 2642 N N . TRP A 1 329 ? 15.185 46.921 0.811 1.00 19.51 ? 329 TRP A N 1 ATOM 2643 C CA . TRP A 1 329 ? 16.382 46.285 0.281 1.00 21.24 ? 329 TRP A CA 1 ATOM 2644 C C . TRP A 1 329 ? 16.476 46.605 -1.206 1.00 22.05 ? 329 TRP A C 1 ATOM 2645 O O . TRP A 1 329 ? 15.480 46.514 -1.927 1.00 22.82 ? 329 TRP A O 1 ATOM 2646 C CB . TRP A 1 329 ? 16.275 44.770 0.486 1.00 19.88 ? 329 TRP A CB 1 ATOM 2647 C CG . TRP A 1 329 ? 17.577 44.039 0.438 1.00 21.19 ? 329 TRP A CG 1 ATOM 2648 C CD1 . TRP A 1 329 ? 17.965 43.115 -0.493 1.00 20.27 ? 329 TRP A CD1 1 ATOM 2649 C CD2 . TRP A 1 329 ? 18.643 44.115 1.398 1.00 21.16 ? 329 TRP A CD2 1 ATOM 2650 N NE1 . TRP A 1 329 ? 19.200 42.606 -0.168 1.00 21.67 ? 329 TRP A NE1 1 ATOM 2651 C CE2 . TRP A 1 329 ? 19.640 43.202 0.987 1.00 20.59 ? 329 TRP A CE2 1 ATOM 2652 C CE3 . TRP A 1 329 ? 18.851 44.864 2.568 1.00 20.64 ? 329 TRP A CE3 1 ATOM 2653 C CZ2 . TRP A 1 329 ? 20.831 43.016 1.704 1.00 20.76 ? 329 TRP A CZ2 1 ATOM 2654 C CZ3 . TRP A 1 329 ? 20.038 44.680 3.284 1.00 21.84 ? 329 TRP A CZ3 1 ATOM 2655 C CH2 . TRP A 1 329 ? 21.011 43.761 2.846 1.00 21.77 ? 329 TRP A CH2 1 ATOM 2656 N N . PRO A 1 330 ? 17.668 46.991 -1.689 1.00 22.05 ? 330 PRO A N 1 ATOM 2657 C CA . PRO A 1 330 ? 17.763 47.301 -3.119 1.00 21.01 ? 330 PRO A CA 1 ATOM 2658 C C . PRO A 1 330 ? 17.282 46.149 -3.997 1.00 22.21 ? 330 PRO A C 1 ATOM 2659 O O . PRO A 1 330 ? 17.580 44.987 -3.716 1.00 22.72 ? 330 PRO A O 1 ATOM 2660 C CB . PRO A 1 330 ? 19.243 47.646 -3.315 1.00 21.61 ? 330 PRO A CB 1 ATOM 2661 C CG . PRO A 1 330 ? 19.929 47.215 -2.047 1.00 21.89 ? 330 PRO A CG 1 ATOM 2662 C CD . PRO A 1 330 ? 18.905 47.342 -0.975 1.00 21.96 ? 330 PRO A CD 1 ATOM 2663 N N . VAL A 1 331 ? 16.520 46.469 -5.044 1.00 21.10 ? 331 VAL A N 1 ATOM 2664 C CA . VAL A 1 331 ? 15.994 45.438 -5.931 1.00 22.30 ? 331 VAL A CA 1 ATOM 2665 C C . VAL A 1 331 ? 17.128 44.557 -6.442 1.00 23.96 ? 331 VAL A C 1 ATOM 2666 O O . VAL A 1 331 ? 18.214 45.047 -6.762 1.00 22.79 ? 331 VAL A O 1 ATOM 2667 C CB . VAL A 1 331 ? 15.197 46.053 -7.114 1.00 21.43 ? 331 VAL A CB 1 ATOM 2668 C CG1 . VAL A 1 331 ? 13.976 46.768 -6.572 1.00 20.13 ? 331 VAL A CG1 1 ATOM 2669 C CG2 . VAL A 1 331 ? 16.055 47.021 -7.902 1.00 17.50 ? 331 VAL A CG2 1 ATOM 2670 N N . GLU A 1 332 ? 16.870 43.253 -6.497 1.00 24.74 ? 332 GLU A N 1 ATOM 2671 C CA . GLU A 1 332 ? 17.872 42.278 -6.922 1.00 26.02 ? 332 GLU A CA 1 ATOM 2672 C C . GLU A 1 332 ? 18.577 42.588 -8.228 1.00 25.25 ? 332 GLU A C 1 ATOM 2673 O O . GLU A 1 332 ? 19.728 42.194 -8.410 1.00 25.45 ? 332 GLU A O 1 ATOM 2674 C CB . GLU A 1 332 ? 17.253 40.885 -7.010 1.00 27.27 ? 332 GLU A CB 1 ATOM 2675 C CG . GLU A 1 332 ? 15.999 40.840 -7.850 1.00 33.80 ? 332 GLU A CG 1 ATOM 2676 C CD . GLU A 1 332 ? 15.451 39.437 -7.998 1.00 37.53 ? 332 GLU A CD 1 ATOM 2677 O OE1 . GLU A 1 332 ? 15.756 38.587 -7.132 1.00 39.67 ? 332 GLU A OE1 1 ATOM 2678 O OE2 . GLU A 1 332 ? 14.707 39.188 -8.972 1.00 39.42 ? 332 GLU A OE2 1 ATOM 2679 N N . GLU A 1 333 ? 17.901 43.281 -9.141 1.00 24.77 ? 333 GLU A N 1 ATOM 2680 C CA . GLU A 1 333 ? 18.521 43.618 -10.420 1.00 25.76 ? 333 GLU A CA 1 ATOM 2681 C C . GLU A 1 333 ? 19.860 44.334 -10.272 1.00 26.19 ? 333 GLU A C 1 ATOM 2682 O O . GLU A 1 333 ? 20.680 44.302 -11.190 1.00 27.07 ? 333 GLU A O 1 ATOM 2683 C CB . GLU A 1 333 ? 17.589 44.483 -11.281 1.00 26.91 ? 333 GLU A CB 1 ATOM 2684 C CG . GLU A 1 333 ? 16.448 43.718 -11.930 1.00 27.88 ? 333 GLU A CG 1 ATOM 2685 C CD . GLU A 1 333 ? 15.246 43.570 -11.014 1.00 30.72 ? 333 GLU A CD 1 ATOM 2686 O OE1 . GLU A 1 333 ? 15.396 43.782 -9.791 1.00 29.40 ? 333 GLU A OE1 1 ATOM 2687 O OE2 . GLU A 1 333 ? 14.153 43.234 -11.521 1.00 30.49 ? 333 GLU A OE2 1 ATOM 2688 N N . ILE A 1 334 ? 20.090 44.977 -9.131 1.00 25.44 ? 334 ILE A N 1 ATOM 2689 C CA . ILE A 1 334 ? 21.348 45.690 -8.926 1.00 26.58 ? 334 ILE A CA 1 ATOM 2690 C C . ILE A 1 334 ? 22.535 44.735 -8.914 1.00 27.36 ? 334 ILE A C 1 ATOM 2691 O O . ILE A 1 334 ? 23.656 45.113 -9.262 1.00 25.70 ? 334 ILE A O 1 ATOM 2692 C CB . ILE A 1 334 ? 21.354 46.472 -7.594 1.00 26.90 ? 334 ILE A CB 1 ATOM 2693 C CG1 . ILE A 1 334 ? 22.516 47.467 -7.583 1.00 27.54 ? 334 ILE A CG1 1 ATOM 2694 C CG2 . ILE A 1 334 ? 21.514 45.512 -6.421 1.00 24.78 ? 334 ILE A CG2 1 ATOM 2695 C CD1 . ILE A 1 334 ? 22.501 48.419 -6.405 1.00 26.93 ? 334 ILE A CD1 1 ATOM 2696 N N . GLU A 1 335 ? 22.285 43.494 -8.518 1.00 28.48 ? 335 GLU A N 1 ATOM 2697 C CA . GLU A 1 335 ? 23.348 42.502 -8.444 1.00 32.25 ? 335 GLU A CA 1 ATOM 2698 C C . GLU A 1 335 ? 24.051 42.249 -9.776 1.00 32.49 ? 335 GLU A C 1 ATOM 2699 O O . GLU A 1 335 ? 25.191 41.785 -9.798 1.00 32.67 ? 335 GLU A O 1 ATOM 2700 C CB . GLU A 1 335 ? 22.794 41.205 -7.848 1.00 33.32 ? 335 GLU A CB 1 ATOM 2701 C CG . GLU A 1 335 ? 22.563 41.325 -6.337 1.00 38.25 ? 335 GLU A CG 1 ATOM 2702 C CD . GLU A 1 335 ? 21.610 40.280 -5.772 1.00 41.18 ? 335 GLU A CD 1 ATOM 2703 O OE1 . GLU A 1 335 ? 21.738 39.092 -6.149 1.00 39.79 ? 335 GLU A OE1 1 ATOM 2704 O OE2 . GLU A 1 335 ? 20.741 40.654 -4.939 1.00 42.47 ? 335 GLU A OE2 1 ATOM 2705 N N . GLU A 1 336 ? 23.386 42.578 -10.881 1.00 32.03 ? 336 GLU A N 1 ATOM 2706 C CA . GLU A 1 336 ? 23.968 42.392 -12.208 1.00 33.16 ? 336 GLU A CA 1 ATOM 2707 C C . GLU A 1 336 ? 25.114 43.366 -12.474 1.00 31.99 ? 336 GLU A C 1 ATOM 2708 O O . GLU A 1 336 ? 25.894 43.166 -13.405 1.00 33.37 ? 336 GLU A O 1 ATOM 2709 C CB . GLU A 1 336 ? 22.903 42.572 -13.292 1.00 37.29 ? 336 GLU A CB 1 ATOM 2710 C CG . GLU A 1 336 ? 21.772 41.565 -13.217 1.00 46.83 ? 336 GLU A CG 1 ATOM 2711 C CD . GLU A 1 336 ? 22.275 40.135 -13.299 1.00 53.15 ? 336 GLU A CD 1 ATOM 2712 O OE1 . GLU A 1 336 ? 22.955 39.805 -14.300 1.00 55.56 ? 336 GLU A OE1 1 ATOM 2713 O OE2 . GLU A 1 336 ? 21.993 39.346 -12.365 1.00 55.54 ? 336 GLU A OE2 1 ATOM 2714 N N . LEU A 1 337 ? 25.209 44.423 -11.671 1.00 29.44 ? 337 LEU A N 1 ATOM 2715 C CA . LEU A 1 337 ? 26.270 45.414 -11.844 1.00 28.22 ? 337 LEU A CA 1 ATOM 2716 C C . LEU A 1 337 ? 27.573 44.987 -11.174 1.00 27.82 ? 337 LEU A C 1 ATOM 2717 O O . LEU A 1 337 ? 28.631 45.559 -11.439 1.00 28.49 ? 337 LEU A O 1 ATOM 2718 C CB . LEU A 1 337 ? 25.837 46.771 -11.275 1.00 27.04 ? 337 LEU A CB 1 ATOM 2719 C CG . LEU A 1 337 ? 24.624 47.458 -11.914 1.00 27.57 ? 337 LEU A CG 1 ATOM 2720 C CD1 . LEU A 1 337 ? 24.311 48.728 -11.136 1.00 25.60 ? 337 LEU A CD1 1 ATOM 2721 C CD2 . LEU A 1 337 ? 24.900 47.774 -13.384 1.00 23.38 ? 337 LEU A CD2 1 ATOM 2722 N N . ARG A 1 338 ? 27.491 43.982 -10.309 1.00 27.55 ? 338 ARG A N 1 ATOM 2723 C CA . ARG A 1 338 ? 28.656 43.480 -9.586 1.00 28.49 ? 338 ARG A CA 1 ATOM 2724 C C . ARG A 1 338 ? 29.729 42.896 -10.501 1.00 29.39 ? 338 ARG A C 1 ATOM 2725 O O . ARG A 1 338 ? 29.439 42.058 -11.351 1.00 30.16 ? 338 ARG A O 1 ATOM 2726 C CB . ARG A 1 338 ? 28.215 42.427 -8.567 1.00 26.27 ? 338 ARG A CB 1 ATOM 2727 C CG . ARG A 1 338 ? 27.398 43.014 -7.430 1.00 28.03 ? 338 ARG A CG 1 ATOM 2728 C CD . ARG A 1 338 ? 26.817 41.953 -6.512 1.00 27.74 ? 338 ARG A CD 1 ATOM 2729 N NE . ARG A 1 338 ? 26.151 42.563 -5.362 1.00 27.67 ? 338 ARG A NE 1 ATOM 2730 C CZ . ARG A 1 338 ? 25.567 41.879 -4.384 1.00 28.36 ? 338 ARG A CZ 1 ATOM 2731 N NH1 . ARG A 1 338 ? 25.560 40.553 -4.414 1.00 28.61 ? 338 ARG A NH1 1 ATOM 2732 N NH2 . ARG A 1 338 ? 25.003 42.519 -3.367 1.00 28.14 ? 338 ARG A NH2 1 ATOM 2733 N N . GLN A 1 339 ? 30.966 43.353 -10.316 1.00 29.68 ? 339 GLN A N 1 ATOM 2734 C CA . GLN A 1 339 ? 32.101 42.886 -11.102 1.00 31.40 ? 339 GLN A CA 1 ATOM 2735 C C . GLN A 1 339 ? 32.963 41.961 -10.238 1.00 31.14 ? 339 GLN A C 1 ATOM 2736 O O . GLN A 1 339 ? 32.522 40.875 -9.868 1.00 31.14 ? 339 GLN A O 1 ATOM 2737 C CB . GLN A 1 339 ? 32.924 44.080 -11.600 1.00 35.42 ? 339 GLN A CB 1 ATOM 2738 C CG . GLN A 1 339 ? 32.127 45.063 -12.447 1.00 42.38 ? 339 GLN A CG 1 ATOM 2739 C CD . GLN A 1 339 ? 31.514 44.407 -13.682 1.00 50.17 ? 339 GLN A CD 1 ATOM 2740 O OE1 . GLN A 1 339 ? 32.205 44.146 -14.674 1.00 54.35 ? 339 GLN A OE1 1 ATOM 2741 N NE2 . GLN A 1 339 ? 30.213 44.124 -13.620 1.00 51.98 ? 339 GLN A NE2 1 ATOM 2742 N N . ASN A 1 340 ? 34.182 42.382 -9.908 1.00 30.79 ? 340 ASN A N 1 ATOM 2743 C CA . ASN A 1 340 ? 35.057 41.548 -9.084 1.00 31.12 ? 340 ASN A CA 1 ATOM 2744 C C . ASN A 1 340 ? 34.673 41.651 -7.614 1.00 30.96 ? 340 ASN A C 1 ATOM 2745 O O . ASN A 1 340 ? 34.156 42.676 -7.162 1.00 29.00 ? 340 ASN A O 1 ATOM 2746 C CB . ASN A 1 340 ? 36.526 41.953 -9.247 1.00 30.20 ? 340 ASN A CB 1 ATOM 2747 C CG . ASN A 1 340 ? 36.825 43.317 -8.658 1.00 31.53 ? 340 ASN A CG 1 ATOM 2748 O OD1 . ASN A 1 340 ? 36.352 44.337 -9.155 1.00 31.79 ? 340 ASN A OD1 1 ATOM 2749 N ND2 . ASN A 1 340 ? 37.614 43.342 -7.591 1.00 30.35 ? 340 ASN A ND2 1 ATOM 2750 N N . GLN A 1 341 ? 34.935 40.584 -6.869 1.00 31.23 ? 341 GLN A N 1 ATOM 2751 C CA . GLN A 1 341 ? 34.603 40.558 -5.456 1.00 30.81 ? 341 GLN A CA 1 ATOM 2752 C C . GLN A 1 341 ? 35.822 40.400 -4.556 1.00 30.67 ? 341 GLN A C 1 ATOM 2753 O O . GLN A 1 341 ? 36.777 39.705 -4.898 1.00 31.29 ? 341 GLN A O 1 ATOM 2754 C CB . GLN A 1 341 ? 33.630 39.412 -5.175 1.00 31.06 ? 341 GLN A CB 1 ATOM 2755 C CG . GLN A 1 341 ? 33.013 39.464 -3.790 1.00 34.13 ? 341 GLN A CG 1 ATOM 2756 C CD . GLN A 1 341 ? 32.246 38.203 -3.428 1.00 37.36 ? 341 GLN A CD 1 ATOM 2757 O OE1 . GLN A 1 341 ? 31.652 37.551 -4.289 1.00 40.49 ? 341 GLN A OE1 1 ATOM 2758 N NE2 . GLN A 1 341 ? 32.241 37.865 -2.143 1.00 37.20 ? 341 GLN A NE2 1 ATOM 2759 N N . VAL A 1 342 ? 35.783 41.065 -3.408 1.00 30.75 ? 342 VAL A N 1 ATOM 2760 C CA . VAL A 1 342 ? 36.839 40.966 -2.409 1.00 30.55 ? 342 VAL A CA 1 ATOM 2761 C C . VAL A 1 342 ? 36.099 40.558 -1.139 1.00 32.60 ? 342 VAL A C 1 ATOM 2762 O O . VAL A 1 342 ? 35.135 41.210 -0.739 1.00 33.25 ? 342 VAL A O 1 ATOM 2763 C CB . VAL A 1 342 ? 37.563 42.294 -2.198 1.00 30.17 ? 342 VAL A CB 1 ATOM 2764 C CG1 . VAL A 1 342 ? 38.460 42.199 -0.969 1.00 27.72 ? 342 VAL A CG1 1 ATOM 2765 C CG2 . VAL A 1 342 ? 38.399 42.619 -3.433 1.00 27.48 ? 342 VAL A CG2 1 ATOM 2766 N N . ASN A 1 343 ? 36.553 39.477 -0.515 1.00 33.27 ? 343 ASN A N 1 ATOM 2767 C CA . ASN A 1 343 ? 35.890 38.930 0.659 1.00 33.16 ? 343 ASN A CA 1 ATOM 2768 C C . ASN A 1 343 ? 36.817 38.764 1.862 1.00 32.72 ? 343 ASN A C 1 ATOM 2769 O O . ASN A 1 343 ? 38.010 38.524 1.706 1.00 31.86 ? 343 ASN A O 1 ATOM 2770 C CB . ASN A 1 343 ? 35.316 37.565 0.273 1.00 37.87 ? 343 ASN A CB 1 ATOM 2771 C CG . ASN A 1 343 ? 34.144 37.155 1.125 1.00 44.30 ? 343 ASN A CG 1 ATOM 2772 O OD1 . ASN A 1 343 ? 33.009 37.565 0.873 1.00 48.64 ? 343 ASN A OD1 1 ATOM 2773 N ND2 . ASN A 1 343 ? 34.405 36.339 2.145 1.00 47.22 ? 343 ASN A ND2 1 ATOM 2774 N N . LEU A 1 344 ? 36.263 38.894 3.062 1.00 30.81 ? 344 LEU A N 1 ATOM 2775 C CA . LEU A 1 344 ? 37.032 38.707 4.288 1.00 31.10 ? 344 LEU A CA 1 ATOM 2776 C C . LEU A 1 344 ? 36.199 37.847 5.229 1.00 31.21 ? 344 LEU A C 1 ATOM 2777 O O . LEU A 1 344 ? 34.973 37.944 5.234 1.00 32.14 ? 344 LEU A O 1 ATOM 2778 C CB . LEU A 1 344 ? 37.329 40.041 4.975 1.00 31.65 ? 344 LEU A CB 1 ATOM 2779 C CG . LEU A 1 344 ? 38.149 41.110 4.251 1.00 34.37 ? 344 LEU A CG 1 ATOM 2780 C CD1 . LEU A 1 344 ? 38.421 42.246 5.230 1.00 34.05 ? 344 LEU A CD1 1 ATOM 2781 C CD2 . LEU A 1 344 ? 39.463 40.536 3.735 1.00 33.52 ? 344 LEU A CD2 1 ATOM 2782 N N . GLN A 1 345 ? 36.851 36.992 6.009 1.00 29.97 ? 345 GLN A N 1 ATOM 2783 C CA . GLN A 1 345 ? 36.129 36.159 6.966 1.00 31.68 ? 345 GLN A CA 1 ATOM 2784 C C . GLN A 1 345 ? 36.948 35.906 8.212 1.00 30.29 ? 345 GLN A C 1 ATOM 2785 O O . GLN A 1 345 ? 38.175 35.848 8.157 1.00 28.83 ? 345 GLN A O 1 ATOM 2786 C CB . GLN A 1 345 ? 35.741 34.811 6.362 1.00 32.17 ? 345 GLN A CB 1 ATOM 2787 C CG . GLN A 1 345 ? 34.803 34.920 5.197 1.00 39.24 ? 345 GLN A CG 1 ATOM 2788 C CD . GLN A 1 345 ? 34.255 33.579 4.760 1.00 41.83 ? 345 GLN A CD 1 ATOM 2789 O OE1 . GLN A 1 345 ? 33.728 33.451 3.655 1.00 45.42 ? 345 GLN A OE1 1 ATOM 2790 N NE2 . GLN A 1 345 ? 34.363 32.576 5.627 1.00 42.00 ? 345 GLN A NE2 1 ATOM 2791 N N . ASN A 1 346 ? 36.253 35.769 9.333 1.00 30.15 ? 346 ASN A N 1 ATOM 2792 C CA . ASN A 1 346 ? 36.890 35.489 10.609 1.00 31.63 ? 346 ASN A CA 1 ATOM 2793 C C . ASN A 1 346 ? 38.075 36.419 10.875 1.00 31.34 ? 346 ASN A C 1 ATOM 2794 O O . ASN A 1 346 ? 39.170 35.971 11.212 1.00 32.05 ? 346 ASN A O 1 ATOM 2795 C CB . ASN A 1 346 ? 37.341 34.030 10.618 1.00 33.58 ? 346 ASN A CB 1 ATOM 2796 C CG . ASN A 1 346 ? 37.619 33.517 12.007 1.00 39.09 ? 346 ASN A CG 1 ATOM 2797 O OD1 . ASN A 1 346 ? 36.801 33.685 12.918 1.00 41.26 ? 346 ASN A OD1 1 ATOM 2798 N ND2 . ASN A 1 346 ? 38.772 32.877 12.184 1.00 38.74 ? 346 ASN A ND2 1 ATOM 2799 N N . LYS A 1 347 ? 37.844 37.718 10.723 1.00 30.84 ? 347 LYS A N 1 ATOM 2800 C CA . LYS A 1 347 ? 38.886 38.714 10.930 1.00 31.15 ? 347 LYS A CA 1 ATOM 2801 C C . LYS A 1 347 ? 38.619 39.608 12.137 1.00 33.49 ? 347 LYS A C 1 ATOM 2802 O O . LYS A 1 347 ? 37.612 40.318 12.198 1.00 33.41 ? 347 LYS A O 1 ATOM 2803 C CB . LYS A 1 347 ? 39.033 39.577 9.676 1.00 29.73 ? 347 LYS A CB 1 ATOM 2804 C CG . LYS A 1 347 ? 39.945 40.780 9.838 1.00 27.56 ? 347 LYS A CG 1 ATOM 2805 C CD . LYS A 1 347 ? 41.356 40.368 10.195 1.00 27.90 ? 347 LYS A CD 1 ATOM 2806 C CE . LYS A 1 347 ? 42.244 41.590 10.349 1.00 27.89 ? 347 LYS A CE 1 ATOM 2807 N NZ . LYS A 1 347 ? 43.624 41.213 10.760 1.00 27.57 ? 347 LYS A NZ 1 ATOM 2808 N N . ASN A 1 348 ? 39.536 39.570 13.095 1.00 35.02 ? 348 ASN A N 1 ATOM 2809 C CA . ASN A 1 348 ? 39.417 40.375 14.296 1.00 36.75 ? 348 ASN A CA 1 ATOM 2810 C C . ASN A 1 348 ? 39.829 41.814 14.065 1.00 35.46 ? 348 ASN A C 1 ATOM 2811 O O . ASN A 1 348 ? 40.829 42.080 13.405 1.00 35.10 ? 348 ASN A O 1 ATOM 2812 C CB . ASN A 1 348 ? 40.289 39.796 15.405 1.00 40.78 ? 348 ASN A CB 1 ATOM 2813 C CG . ASN A 1 348 ? 39.501 38.972 16.379 1.00 46.44 ? 348 ASN A CG 1 ATOM 2814 O OD1 . ASN A 1 348 ? 38.626 39.493 17.077 1.00 51.74 ? 348 ASN A OD1 1 ATOM 2815 N ND2 . ASN A 1 348 ? 39.796 37.673 16.437 1.00 48.79 ? 348 ASN A ND2 1 ATOM 2816 N N . LEU A 1 349 ? 39.041 42.739 14.602 1.00 34.45 ? 349 LEU A N 1 ATOM 2817 C CA . LEU A 1 349 ? 39.351 44.157 14.505 1.00 35.53 ? 349 LEU A CA 1 ATOM 2818 C C . LEU A 1 349 ? 39.665 44.593 15.926 1.00 36.10 ? 349 LEU A C 1 ATOM 2819 O O . LEU A 1 349 ? 38.763 44.762 16.749 1.00 35.09 ? 349 LEU A O 1 ATOM 2820 C CB . LEU A 1 349 ? 38.160 44.961 13.975 1.00 36.79 ? 349 LEU A CB 1 ATOM 2821 C CG . LEU A 1 349 ? 37.752 44.783 12.510 1.00 37.94 ? 349 LEU A CG 1 ATOM 2822 C CD1 . LEU A 1 349 ? 36.634 45.766 12.182 1.00 36.54 ? 349 LEU A CD1 1 ATOM 2823 C CD2 . LEU A 1 349 ? 38.950 45.023 11.600 1.00 37.31 ? 349 LEU A CD2 1 ATOM 2824 N N . LYS A 1 350 ? 40.950 44.746 16.220 1.00 37.31 ? 350 LYS A N 1 ATOM 2825 C CA . LYS A 1 350 ? 41.367 45.147 17.552 1.00 39.67 ? 350 LYS A CA 1 ATOM 2826 C C . LYS A 1 350 ? 40.982 46.605 17.785 1.00 37.52 ? 350 LYS A C 1 ATOM 2827 O O . LYS A 1 350 ? 40.739 47.353 16.836 1.00 37.62 ? 350 LYS A O 1 ATOM 2828 C CB . LYS A 1 350 ? 42.881 44.972 17.714 1.00 43.42 ? 350 LYS A CB 1 ATOM 2829 C CG . LYS A 1 350 ? 43.704 45.948 16.887 1.00 51.21 ? 350 LYS A CG 1 ATOM 2830 C CD . LYS A 1 350 ? 45.174 45.969 17.315 1.00 55.57 ? 350 LYS A CD 1 ATOM 2831 C CE . LYS A 1 350 ? 45.922 47.150 16.680 1.00 58.43 ? 350 LYS A CE 1 ATOM 2832 N NZ . LYS A 1 350 ? 45.356 48.490 17.063 1.00 58.62 ? 350 LYS A NZ 1 ATOM 2833 N N . PRO A 1 351 ? 40.913 47.024 19.054 1.00 35.22 ? 351 PRO A N 1 ATOM 2834 C CA . PRO A 1 351 ? 40.557 48.396 19.425 1.00 34.15 ? 351 PRO A CA 1 ATOM 2835 C C . PRO A 1 351 ? 41.395 49.471 18.725 1.00 33.14 ? 351 PRO A C 1 ATOM 2836 O O . PRO A 1 351 ? 42.618 49.394 18.689 1.00 33.00 ? 351 PRO A O 1 ATOM 2837 C CB . PRO A 1 351 ? 40.761 48.398 20.937 1.00 33.16 ? 351 PRO A CB 1 ATOM 2838 C CG . PRO A 1 351 ? 40.359 47.008 21.311 1.00 34.02 ? 351 PRO A CG 1 ATOM 2839 C CD . PRO A 1 351 ? 41.049 46.179 20.253 1.00 34.57 ? 351 PRO A CD 1 ATOM 2840 N N . GLY A 1 352 ? 40.720 50.473 18.171 1.00 32.21 ? 352 GLY A N 1 ATOM 2841 C CA . GLY A 1 352 ? 41.413 51.555 17.498 1.00 31.21 ? 352 GLY A CA 1 ATOM 2842 C C . GLY A 1 352 ? 42.074 51.192 16.183 1.00 32.30 ? 352 GLY A C 1 ATOM 2843 O O . GLY A 1 352 ? 42.958 51.913 15.725 1.00 33.82 ? 352 GLY A O 1 ATOM 2844 N N . SER A 1 353 ? 41.655 50.095 15.560 1.00 31.81 ? 353 SER A N 1 ATOM 2845 C CA . SER A 1 353 ? 42.261 49.683 14.296 1.00 32.21 ? 353 SER A CA 1 ATOM 2846 C C . SER A 1 353 ? 41.489 50.125 13.057 1.00 32.90 ? 353 SER A C 1 ATOM 2847 O O . SER A 1 353 ? 40.288 50.407 13.114 1.00 33.09 ? 353 SER A O 1 ATOM 2848 C CB . SER A 1 353 ? 42.416 48.164 14.250 1.00 32.07 ? 353 SER A CB 1 ATOM 2849 O OG . SER A 1 353 ? 41.150 47.525 14.217 1.00 33.25 ? 353 SER A OG 1 ATOM 2850 N N . VAL A 1 354 ? 42.203 50.175 11.937 1.00 32.72 ? 354 VAL A N 1 ATOM 2851 C CA . VAL A 1 354 ? 41.636 50.546 10.647 1.00 31.48 ? 354 VAL A CA 1 ATOM 2852 C C . VAL A 1 354 ? 42.192 49.564 9.615 1.00 31.85 ? 354 VAL A C 1 ATOM 2853 O O . VAL A 1 354 ? 43.405 49.449 9.440 1.00 32.18 ? 354 VAL A O 1 ATOM 2854 C CB . VAL A 1 354 ? 42.023 51.988 10.251 1.00 29.98 ? 354 VAL A CB 1 ATOM 2855 C CG1 . VAL A 1 354 ? 41.486 52.307 8.866 1.00 29.77 ? 354 VAL A CG1 1 ATOM 2856 C CG2 . VAL A 1 354 ? 41.459 52.975 11.267 1.00 30.26 ? 354 VAL A CG2 1 ATOM 2857 N N . LEU A 1 355 ? 41.298 48.851 8.943 1.00 31.02 ? 355 LEU A N 1 ATOM 2858 C CA . LEU A 1 355 ? 41.688 47.862 7.945 1.00 30.33 ? 355 LEU A CA 1 ATOM 2859 C C . LEU A 1 355 ? 41.225 48.278 6.554 1.00 30.73 ? 355 LEU A C 1 ATOM 2860 O O . LEU A 1 355 ? 40.025 48.379 6.297 1.00 31.66 ? 355 LEU A O 1 ATOM 2861 C CB . LEU A 1 355 ? 41.073 46.513 8.308 1.00 27.96 ? 355 LEU A CB 1 ATOM 2862 C CG . LEU A 1 355 ? 41.316 45.365 7.338 1.00 28.65 ? 355 LEU A CG 1 ATOM 2863 C CD1 . LEU A 1 355 ? 42.788 44.965 7.392 1.00 26.42 ? 355 LEU A CD1 1 ATOM 2864 C CD2 . LEU A 1 355 ? 40.417 44.194 7.711 1.00 25.75 ? 355 LEU A CD2 1 ATOM 2865 N N . GLU A 1 356 ? 42.170 48.514 5.651 1.00 30.62 ? 356 GLU A N 1 ATOM 2866 C CA . GLU A 1 356 ? 41.814 48.926 4.303 1.00 31.78 ? 356 GLU A CA 1 ATOM 2867 C C . GLU A 1 356 ? 41.435 47.757 3.404 1.00 32.44 ? 356 GLU A C 1 ATOM 2868 O O . GLU A 1 356 ? 42.059 46.697 3.449 1.00 34.46 ? 356 GLU A O 1 ATOM 2869 C CB . GLU A 1 356 ? 42.958 49.725 3.665 1.00 31.01 ? 356 GLU A CB 1 ATOM 2870 C CG . GLU A 1 356 ? 42.800 49.901 2.160 1.00 33.90 ? 356 GLU A CG 1 ATOM 2871 C CD . GLU A 1 356 ? 43.625 51.042 1.585 1.00 35.95 ? 356 GLU A CD 1 ATOM 2872 O OE1 . GLU A 1 356 ? 44.692 51.369 2.146 1.00 37.35 ? 356 GLU A OE1 1 ATOM 2873 O OE2 . GLU A 1 356 ? 43.208 51.606 0.550 1.00 36.81 ? 356 GLU A OE2 1 ATOM 2874 N N . ILE A 1 357 ? 40.398 47.964 2.596 1.00 32.81 ? 357 ILE A N 1 ATOM 2875 C CA . ILE A 1 357 ? 39.921 46.956 1.660 1.00 32.26 ? 357 ILE A CA 1 ATOM 2876 C C . ILE A 1 357 ? 40.491 47.316 0.293 1.00 33.72 ? 357 ILE A C 1 ATOM 2877 O O . ILE A 1 357 ? 40.067 48.295 -0.323 1.00 35.83 ? 357 ILE A O 1 ATOM 2878 C CB . ILE A 1 357 ? 38.379 46.956 1.553 1.00 32.12 ? 357 ILE A CB 1 ATOM 2879 C CG1 . ILE A 1 357 ? 37.749 46.879 2.943 1.00 30.95 ? 357 ILE A CG1 1 ATOM 2880 C CG2 . ILE A 1 357 ? 37.918 45.774 0.713 1.00 30.16 ? 357 ILE A CG2 1 ATOM 2881 C CD1 . ILE A 1 357 ? 38.149 45.659 3.733 1.00 33.30 ? 357 ILE A CD1 1 ATOM 2882 N N . HIS A 1 358 ? 41.448 46.520 -0.175 1.00 33.55 ? 358 HIS A N 1 ATOM 2883 C CA . HIS A 1 358 ? 42.097 46.754 -1.464 1.00 33.06 ? 358 HIS A CA 1 ATOM 2884 C C . HIS A 1 358 ? 41.401 46.025 -2.608 1.00 32.09 ? 358 HIS A C 1 ATOM 2885 O O . HIS A 1 358 ? 40.683 45.053 -2.387 1.00 31.52 ? 358 HIS A O 1 ATOM 2886 C CB . HIS A 1 358 ? 43.554 46.275 -1.410 1.00 32.34 ? 358 HIS A CB 1 ATOM 2887 C CG . HIS A 1 358 ? 44.390 46.976 -0.388 1.00 33.28 ? 358 HIS A CG 1 ATOM 2888 N ND1 . HIS A 1 358 ? 45.124 48.107 -0.674 1.00 34.38 ? 358 HIS A ND1 1 ATOM 2889 C CD2 . HIS A 1 358 ? 44.605 46.709 0.922 1.00 33.42 ? 358 HIS A CD2 1 ATOM 2890 C CE1 . HIS A 1 358 ? 45.758 48.505 0.415 1.00 33.60 ? 358 HIS A CE1 1 ATOM 2891 N NE2 . HIS A 1 358 ? 45.460 47.674 1.398 1.00 33.50 ? 358 HIS A NE2 1 ATOM 2892 N N . GLY A 1 359 ? 41.627 46.505 -3.828 1.00 32.02 ? 359 GLY A N 1 ATOM 2893 C CA . GLY A 1 359 ? 41.064 45.859 -5.001 1.00 32.01 ? 359 GLY A CA 1 ATOM 2894 C C . GLY A 1 359 ? 39.644 46.186 -5.411 1.00 31.78 ? 359 GLY A C 1 ATOM 2895 O O . GLY A 1 359 ? 39.128 45.588 -6.353 1.00 31.39 ? 359 GLY A O 1 ATOM 2896 N N . ILE A 1 360 ? 39.013 47.133 -4.726 1.00 31.32 ? 360 ILE A N 1 ATOM 2897 C CA . ILE A 1 360 ? 37.640 47.517 -5.040 1.00 30.27 ? 360 ILE A CA 1 ATOM 2898 C C . ILE A 1 360 ? 37.558 48.938 -5.588 1.00 29.48 ? 360 ILE A C 1 ATOM 2899 O O . ILE A 1 360 ? 38.344 49.798 -5.200 1.00 31.45 ? 360 ILE A O 1 ATOM 2900 C CB . ILE A 1 360 ? 36.759 47.440 -3.768 1.00 30.81 ? 360 ILE A CB 1 ATOM 2901 C CG1 . ILE A 1 360 ? 36.618 45.986 -3.328 1.00 31.17 ? 360 ILE A CG1 1 ATOM 2902 C CG2 . ILE A 1 360 ? 35.389 48.066 -4.022 1.00 30.84 ? 360 ILE A CG2 1 ATOM 2903 C CD1 . ILE A 1 360 ? 35.917 45.110 -4.349 1.00 31.84 ? 360 ILE A CD1 1 ATOM 2904 N N . ALA A 1 361 ? 36.623 49.181 -6.501 1.00 28.79 ? 361 ALA A N 1 ATOM 2905 C CA . ALA A 1 361 ? 36.421 50.533 -7.029 1.00 28.22 ? 361 ALA A CA 1 ATOM 2906 C C . ALA A 1 361 ? 35.698 51.223 -5.864 1.00 27.99 ? 361 ALA A C 1 ATOM 2907 O O . ALA A 1 361 ? 34.472 51.164 -5.765 1.00 28.75 ? 361 ALA A O 1 ATOM 2908 C CB . ALA A 1 361 ? 35.526 50.484 -8.262 1.00 27.26 ? 361 ALA A CB 1 ATOM 2909 N N . ALA A 1 362 ? 36.463 51.857 -4.981 1.00 27.18 ? 362 ALA A N 1 ATOM 2910 C CA . ALA A 1 362 ? 35.918 52.485 -3.774 1.00 26.94 ? 362 ALA A CA 1 ATOM 2911 C C . ALA A 1 362 ? 34.854 53.575 -3.902 1.00 26.89 ? 362 ALA A C 1 ATOM 2912 O O . ALA A 1 362 ? 34.187 53.892 -2.917 1.00 26.45 ? 362 ALA A O 1 ATOM 2913 C CB . ALA A 1 362 ? 37.071 52.990 -2.897 1.00 26.14 ? 362 ALA A CB 1 ATOM 2914 N N . SER A 1 363 ? 34.692 54.150 -5.089 1.00 26.52 ? 363 SER A N 1 ATOM 2915 C CA . SER A 1 363 ? 33.685 55.196 -5.296 1.00 28.40 ? 363 SER A CA 1 ATOM 2916 C C . SER A 1 363 ? 32.387 54.634 -5.872 1.00 28.13 ? 363 SER A C 1 ATOM 2917 O O . SER A 1 363 ? 31.380 55.337 -5.951 1.00 29.00 ? 363 SER A O 1 ATOM 2918 C CB . SER A 1 363 ? 34.202 56.270 -6.263 1.00 27.82 ? 363 SER A CB 1 ATOM 2919 O OG . SER A 1 363 ? 35.230 57.052 -5.686 1.00 33.56 ? 363 SER A OG 1 ATOM 2920 N N . GLN A 1 364 ? 32.413 53.370 -6.276 1.00 27.02 ? 364 GLN A N 1 ATOM 2921 C CA . GLN A 1 364 ? 31.246 52.742 -6.888 1.00 26.50 ? 364 GLN A CA 1 ATOM 2922 C C . GLN A 1 364 ? 31.267 51.269 -6.495 1.00 25.38 ? 364 GLN A C 1 ATOM 2923 O O . GLN A 1 364 ? 31.754 50.411 -7.240 1.00 24.69 ? 364 GLN A O 1 ATOM 2924 C CB . GLN A 1 364 ? 31.353 52.909 -8.406 1.00 25.35 ? 364 GLN A CB 1 ATOM 2925 C CG . GLN A 1 364 ? 30.059 52.825 -9.163 1.00 26.97 ? 364 GLN A CG 1 ATOM 2926 C CD . GLN A 1 364 ? 30.222 53.300 -10.595 1.00 26.73 ? 364 GLN A CD 1 ATOM 2927 O OE1 . GLN A 1 364 ? 30.657 54.426 -10.836 1.00 26.98 ? 364 GLN A OE1 1 ATOM 2928 N NE2 . GLN A 1 364 ? 29.873 52.445 -11.552 1.00 25.59 ? 364 GLN A NE2 1 ATOM 2929 N N . ALA A 1 365 ? 30.722 50.982 -5.318 1.00 24.84 ? 365 ALA A N 1 ATOM 2930 C CA . ALA A 1 365 ? 30.744 49.630 -4.796 1.00 23.55 ? 365 ALA A CA 1 ATOM 2931 C C . ALA A 1 365 ? 29.526 49.256 -3.976 1.00 24.55 ? 365 ALA A C 1 ATOM 2932 O O . ALA A 1 365 ? 28.740 50.109 -3.568 1.00 25.91 ? 365 ALA A O 1 ATOM 2933 C CB . ALA A 1 365 ? 31.995 49.449 -3.959 1.00 20.87 ? 365 ALA A CB 1 ATOM 2934 N N . ASP A 1 366 ? 29.399 47.956 -3.738 1.00 24.55 ? 366 ASP A N 1 ATOM 2935 C CA . ASP A 1 366 ? 28.315 47.370 -2.965 1.00 24.99 ? 366 ASP A CA 1 ATOM 2936 C C . ASP A 1 366 ? 29.054 46.573 -1.883 1.00 26.08 ? 366 ASP A C 1 ATOM 2937 O O . ASP A 1 366 ? 29.677 45.548 -2.165 1.00 25.93 ? 366 ASP A O 1 ATOM 2938 C CB . ASP A 1 366 ? 27.491 46.451 -3.873 1.00 24.40 ? 366 ASP A CB 1 ATOM 2939 C CG . ASP A 1 366 ? 26.260 45.892 -3.190 1.00 26.81 ? 366 ASP A CG 1 ATOM 2940 O OD1 . ASP A 1 366 ? 26.062 46.151 -1.984 1.00 26.62 ? 366 ASP A OD1 1 ATOM 2941 O OD2 . ASP A 1 366 ? 25.484 45.185 -3.872 1.00 27.70 ? 366 ASP A OD2 1 ATOM 2942 N N . VAL A 1 367 ? 28.999 47.058 -0.647 1.00 26.63 ? 367 VAL A N 1 ATOM 2943 C CA . VAL A 1 367 ? 29.712 46.419 0.451 1.00 26.68 ? 367 VAL A CA 1 ATOM 2944 C C . VAL A 1 367 ? 28.812 45.925 1.571 1.00 27.02 ? 367 VAL A C 1 ATOM 2945 O O . VAL A 1 367 ? 27.968 46.658 2.073 1.00 29.93 ? 367 VAL A O 1 ATOM 2946 C CB . VAL A 1 367 ? 30.753 47.395 1.053 1.00 25.53 ? 367 VAL A CB 1 ATOM 2947 C CG1 . VAL A 1 367 ? 31.601 46.685 2.089 1.00 24.73 ? 367 VAL A CG1 1 ATOM 2948 C CG2 . VAL A 1 367 ? 31.626 47.961 -0.053 1.00 24.50 ? 367 VAL A CG2 1 ATOM 2949 N N . THR A 1 368 ? 29.006 44.672 1.961 1.00 27.16 ? 368 THR A N 1 ATOM 2950 C CA . THR A 1 368 ? 28.231 44.070 3.034 1.00 27.99 ? 368 THR A CA 1 ATOM 2951 C C . THR A 1 368 ? 29.199 43.550 4.081 1.00 28.64 ? 368 THR A C 1 ATOM 2952 O O . THR A 1 368 ? 30.245 42.989 3.751 1.00 27.25 ? 368 THR A O 1 ATOM 2953 C CB . THR A 1 368 ? 27.390 42.893 2.527 1.00 29.88 ? 368 THR A CB 1 ATOM 2954 O OG1 . THR A 1 368 ? 26.487 43.356 1.515 1.00 33.51 ? 368 THR A OG1 1 ATOM 2955 C CG2 . THR A 1 368 ? 26.592 42.279 3.673 1.00 31.10 ? 368 THR A CG2 1 ATOM 2956 N N . ILE A 1 369 ? 28.857 43.740 5.347 1.00 28.62 ? 369 ILE A N 1 ATOM 2957 C CA . ILE A 1 369 ? 29.717 43.273 6.416 1.00 28.73 ? 369 ILE A CA 1 ATOM 2958 C C . ILE A 1 369 ? 28.875 42.817 7.598 1.00 28.57 ? 369 ILE A C 1 ATOM 2959 O O . ILE A 1 369 ? 27.787 43.336 7.841 1.00 27.98 ? 369 ILE A O 1 ATOM 2960 C CB . ILE A 1 369 ? 30.714 44.376 6.828 1.00 30.02 ? 369 ILE A CB 1 ATOM 2961 C CG1 . ILE A 1 369 ? 31.679 43.850 7.885 1.00 31.41 ? 369 ILE A CG1 1 ATOM 2962 C CG2 . ILE A 1 369 ? 29.977 45.579 7.347 1.00 30.79 ? 369 ILE A CG2 1 ATOM 2963 C CD1 . ILE A 1 369 ? 32.872 44.769 8.100 1.00 33.76 ? 369 ILE A CD1 1 ATOM 2964 N N . SER A 1 370 ? 29.368 41.817 8.317 1.00 28.25 ? 370 SER A N 1 ATOM 2965 C CA . SER A 1 370 ? 28.643 41.291 9.458 1.00 28.43 ? 370 SER A CA 1 ATOM 2966 C C . SER A 1 370 ? 29.602 41.206 10.639 1.00 28.97 ? 370 SER A C 1 ATOM 2967 O O . SER A 1 370 ? 30.683 40.623 10.534 1.00 29.76 ? 370 SER A O 1 ATOM 2968 C CB . SER A 1 370 ? 28.072 39.914 9.109 1.00 28.62 ? 370 SER A CB 1 ATOM 2969 O OG . SER A 1 370 ? 27.089 39.512 10.044 1.00 32.92 ? 370 SER A OG 1 ATOM 2970 N N . PHE A 1 371 ? 29.202 41.802 11.758 1.00 29.04 ? 371 PHE A N 1 ATOM 2971 C CA . PHE A 1 371 ? 30.019 41.832 12.967 1.00 29.43 ? 371 PHE A CA 1 ATOM 2972 C C . PHE A 1 371 ? 29.551 40.861 14.049 1.00 31.33 ? 371 PHE A C 1 ATOM 2973 O O . PHE A 1 371 ? 28.360 40.801 14.363 1.00 32.01 ? 371 PHE A O 1 ATOM 2974 C CB . PHE A 1 371 ? 30.005 43.242 13.562 1.00 27.06 ? 371 PHE A CB 1 ATOM 2975 C CG . PHE A 1 371 ? 30.625 44.285 12.684 1.00 26.39 ? 371 PHE A CG 1 ATOM 2976 C CD1 . PHE A 1 371 ? 32.008 44.432 12.624 1.00 25.16 ? 371 PHE A CD1 1 ATOM 2977 C CD2 . PHE A 1 371 ? 29.827 45.135 11.924 1.00 25.38 ? 371 PHE A CD2 1 ATOM 2978 C CE1 . PHE A 1 371 ? 32.587 45.413 11.823 1.00 26.18 ? 371 PHE A CE1 1 ATOM 2979 C CE2 . PHE A 1 371 ? 30.394 46.120 11.118 1.00 25.67 ? 371 PHE A CE2 1 ATOM 2980 C CZ . PHE A 1 371 ? 31.777 46.260 11.067 1.00 25.92 ? 371 PHE A CZ 1 ATOM 2981 N N . LYS A 1 372 ? 30.494 40.110 14.616 1.00 33.33 ? 372 LYS A N 1 ATOM 2982 C CA . LYS A 1 372 ? 30.202 39.180 15.707 1.00 35.33 ? 372 LYS A CA 1 ATOM 2983 C C . LYS A 1 372 ? 30.796 39.848 16.941 1.00 35.63 ? 372 LYS A C 1 ATOM 2984 O O . LYS A 1 372 ? 31.989 40.160 16.970 1.00 33.49 ? 372 LYS A O 1 ATOM 2985 C CB . LYS A 1 372 ? 30.871 37.820 15.488 1.00 38.62 ? 372 LYS A CB 1 ATOM 2986 C CG . LYS A 1 372 ? 30.507 36.800 16.565 1.00 44.27 ? 372 LYS A CG 1 ATOM 2987 C CD . LYS A 1 372 ? 30.998 35.393 16.242 1.00 49.64 ? 372 LYS A CD 1 ATOM 2988 C CE . LYS A 1 372 ? 32.518 35.274 16.325 1.00 54.71 ? 372 LYS A CE 1 ATOM 2989 N NZ . LYS A 1 372 ? 33.055 35.472 17.714 1.00 58.15 ? 372 LYS A NZ 1 ATOM 2990 N N . LEU A 1 373 ? 29.967 40.069 17.957 1.00 36.28 ? 373 LEU A N 1 ATOM 2991 C CA . LEU A 1 373 ? 30.426 40.746 19.163 1.00 38.01 ? 373 LEU A CA 1 ATOM 2992 C C . LEU A 1 373 ? 30.814 39.844 20.319 1.00 40.58 ? 373 LEU A C 1 ATOM 2993 O O . LEU A 1 373 ? 30.274 38.750 20.496 1.00 40.36 ? 373 LEU A O 1 ATOM 2994 C CB . LEU A 1 373 ? 29.358 41.724 19.649 1.00 35.56 ? 373 LEU A CB 1 ATOM 2995 C CG . LEU A 1 373 ? 28.810 42.688 18.603 1.00 35.99 ? 373 LEU A CG 1 ATOM 2996 C CD1 . LEU A 1 373 ? 27.811 43.616 19.260 1.00 37.03 ? 373 LEU A CD1 1 ATOM 2997 C CD2 . LEU A 1 373 ? 29.946 43.476 17.982 1.00 35.97 ? 373 LEU A CD2 1 ATOM 2998 N N . GLU A 1 374 ? 31.755 40.337 21.115 1.00 44.72 ? 374 GLU A N 1 ATOM 2999 C CA . GLU A 1 374 ? 32.233 39.623 22.290 1.00 48.25 ? 374 GLU A CA 1 ATOM 3000 C C . GLU A 1 374 ? 32.187 40.583 23.479 1.00 47.46 ? 374 GLU A C 1 ATOM 3001 O O . GLU A 1 374 ? 32.453 41.784 23.337 1.00 48.08 ? 374 GLU A O 1 ATOM 3002 C CB . GLU A 1 374 ? 33.676 39.147 22.084 1.00 52.01 ? 374 GLU A CB 1 ATOM 3003 C CG . GLU A 1 374 ? 34.680 40.286 21.891 1.00 57.15 ? 374 GLU A CG 1 ATOM 3004 C CD . GLU A 1 374 ? 36.128 39.852 22.090 1.00 61.02 ? 374 GLU A CD 1 ATOM 3005 O OE1 . GLU A 1 374 ? 36.608 38.976 21.334 1.00 61.50 ? 374 GLU A OE1 1 ATOM 3006 O OE2 . GLU A 1 374 ? 36.785 40.393 23.009 1.00 63.16 ? 374 GLU A OE2 1 ATOM 3007 N N . GLY A 1 375 ? 31.848 40.052 24.646 1.00 46.03 ? 375 GLY A N 1 ATOM 3008 C CA . GLY A 1 375 ? 31.794 40.875 25.839 1.00 43.84 ? 375 GLY A CA 1 ATOM 3009 C C . GLY A 1 375 ? 30.714 41.936 25.812 1.00 41.92 ? 375 GLY A C 1 ATOM 3010 O O . GLY A 1 375 ? 30.994 43.110 26.042 1.00 41.79 ? 375 GLY A O 1 ATOM 3011 N N . LEU A 1 376 ? 29.481 41.522 25.530 1.00 40.17 ? 376 LEU A N 1 ATOM 3012 C CA . LEU A 1 376 ? 28.354 42.442 25.491 1.00 39.67 ? 376 LEU A CA 1 ATOM 3013 C C . LEU A 1 376 ? 28.146 43.103 26.844 1.00 40.40 ? 376 LEU A C 1 ATOM 3014 O O . LEU A 1 376 ? 27.765 44.272 26.916 1.00 41.59 ? 376 LEU A O 1 ATOM 3015 C CB . LEU A 1 376 ? 27.073 41.709 25.093 1.00 39.13 ? 376 LEU A CB 1 ATOM 3016 C CG . LEU A 1 376 ? 26.885 41.371 23.618 1.00 39.39 ? 376 LEU A CG 1 ATOM 3017 C CD1 . LEU A 1 376 ? 25.598 40.583 23.437 1.00 40.97 ? 376 LEU A CD1 1 ATOM 3018 C CD2 . LEU A 1 376 ? 26.842 42.654 22.807 1.00 40.19 ? 376 LEU A CD2 1 ATOM 3019 N N . LYS A 1 377 ? 28.390 42.346 27.910 1.00 39.51 ? 377 LYS A N 1 ATOM 3020 C CA . LYS A 1 377 ? 28.228 42.846 29.271 1.00 40.29 ? 377 LYS A CA 1 ATOM 3021 C C . LYS A 1 377 ? 29.033 44.121 29.481 1.00 38.50 ? 377 LYS A C 1 ATOM 3022 O O . LYS A 1 377 ? 28.767 44.878 30.413 1.00 38.25 ? 377 LYS A O 1 ATOM 3023 C CB . LYS A 1 377 ? 28.672 41.782 30.282 1.00 43.52 ? 377 LYS A CB 1 ATOM 3024 C CG . LYS A 1 377 ? 30.088 41.269 30.026 1.00 51.48 ? 377 LYS A CG 1 ATOM 3025 C CD . LYS A 1 377 ? 30.493 40.126 30.957 1.00 54.84 ? 377 LYS A CD 1 ATOM 3026 C CE . LYS A 1 377 ? 30.852 40.619 32.351 1.00 57.40 ? 377 LYS A CE 1 ATOM 3027 N NZ . LYS A 1 377 ? 31.291 39.501 33.240 1.00 58.16 ? 377 LYS A NZ 1 ATOM 3028 N N . GLU A 1 378 ? 30.011 44.363 28.612 1.00 36.81 ? 378 GLU A N 1 ATOM 3029 C CA . GLU A 1 378 ? 30.848 45.557 28.721 1.00 36.48 ? 378 GLU A CA 1 ATOM 3030 C C . GLU A 1 378 ? 30.221 46.792 28.078 1.00 35.19 ? 378 GLU A C 1 ATOM 3031 O O . GLU A 1 378 ? 30.772 47.886 28.161 1.00 34.17 ? 378 GLU A O 1 ATOM 3032 C CB . GLU A 1 378 ? 32.217 45.308 28.087 1.00 39.47 ? 378 GLU A CB 1 ATOM 3033 C CG . GLU A 1 378 ? 32.990 44.158 28.707 1.00 44.12 ? 378 GLU A CG 1 ATOM 3034 C CD . GLU A 1 378 ? 33.052 44.256 30.220 1.00 47.16 ? 378 GLU A CD 1 ATOM 3035 O OE1 . GLU A 1 378 ? 33.491 45.311 30.734 1.00 48.18 ? 378 GLU A OE1 1 ATOM 3036 O OE2 . GLU A 1 378 ? 32.659 43.276 30.892 1.00 49.58 ? 378 GLU A OE2 1 ATOM 3037 N N . ALA A 1 379 ? 29.072 46.616 27.437 1.00 33.35 ? 379 ALA A N 1 ATOM 3038 C CA . ALA A 1 379 ? 28.397 47.728 26.783 1.00 32.92 ? 379 ALA A CA 1 ATOM 3039 C C . ALA A 1 379 ? 28.155 48.893 27.738 1.00 32.96 ? 379 ALA A C 1 ATOM 3040 O O . ALA A 1 379 ? 27.733 48.701 28.881 1.00 33.03 ? 379 ALA A O 1 ATOM 3041 C CB . ALA A 1 379 ? 27.073 47.257 26.194 1.00 31.79 ? 379 ALA A CB 1 ATOM 3042 N N . GLU A 1 380 ? 28.436 50.101 27.259 1.00 32.40 ? 380 GLU A N 1 ATOM 3043 C CA . GLU A 1 380 ? 28.231 51.317 28.037 1.00 31.18 ? 380 GLU A CA 1 ATOM 3044 C C . GLU A 1 380 ? 26.794 51.357 28.524 1.00 31.16 ? 380 GLU A C 1 ATOM 3045 O O . GLU A 1 380 ? 25.870 51.040 27.771 1.00 31.27 ? 380 GLU A O 1 ATOM 3046 C CB . GLU A 1 380 ? 28.477 52.543 27.167 1.00 31.84 ? 380 GLU A CB 1 ATOM 3047 C CG . GLU A 1 380 ? 29.925 52.830 26.853 1.00 33.04 ? 380 GLU A CG 1 ATOM 3048 C CD . GLU A 1 380 ? 30.076 53.581 25.545 1.00 35.55 ? 380 GLU A CD 1 ATOM 3049 O OE1 . GLU A 1 380 ? 30.145 52.918 24.486 1.00 34.98 ? 380 GLU A OE1 1 ATOM 3050 O OE2 . GLU A 1 380 ? 30.109 54.830 25.572 1.00 37.38 ? 380 GLU A OE2 1 ATOM 3051 N N . VAL A 1 381 ? 26.598 51.746 29.779 1.00 31.08 ? 381 VAL A N 1 ATOM 3052 C CA . VAL A 1 381 ? 25.249 51.829 30.320 1.00 31.15 ? 381 VAL A CA 1 ATOM 3053 C C . VAL A 1 381 ? 24.602 53.132 29.873 1.00 30.74 ? 381 VAL A C 1 ATOM 3054 O O . VAL A 1 381 ? 25.078 54.215 30.197 1.00 31.50 ? 381 VAL A O 1 ATOM 3055 C CB . VAL A 1 381 ? 25.251 51.782 31.851 1.00 31.88 ? 381 VAL A CB 1 ATOM 3056 C CG1 . VAL A 1 381 ? 23.821 51.835 32.374 1.00 30.84 ? 381 VAL A CG1 1 ATOM 3057 C CG2 . VAL A 1 381 ? 25.951 50.519 32.321 1.00 31.22 ? 381 VAL A CG2 1 ATOM 3058 N N . LEU A 1 382 ? 23.525 53.020 29.109 1.00 30.61 ? 382 LEU A N 1 ATOM 3059 C CA . LEU A 1 382 ? 22.812 54.188 28.624 1.00 30.61 ? 382 LEU A CA 1 ATOM 3060 C C . LEU A 1 382 ? 21.389 53.812 28.268 1.00 31.55 ? 382 LEU A C 1 ATOM 3061 O O . LEU A 1 382 ? 21.157 53.066 27.318 1.00 32.79 ? 382 LEU A O 1 ATOM 3062 C CB . LEU A 1 382 ? 23.502 54.772 27.387 1.00 31.68 ? 382 LEU A CB 1 ATOM 3063 C CG . LEU A 1 382 ? 22.762 55.918 26.681 1.00 33.91 ? 382 LEU A CG 1 ATOM 3064 C CD1 . LEU A 1 382 ? 22.611 57.091 27.637 1.00 32.91 ? 382 LEU A CD1 1 ATOM 3065 C CD2 . LEU A 1 382 ? 23.518 56.348 25.431 1.00 33.25 ? 382 LEU A CD2 1 ATOM 3066 N N . ASP A 1 383 ? 20.433 54.309 29.041 1.00 32.15 ? 383 ASP A N 1 ATOM 3067 C CA . ASP A 1 383 ? 19.034 54.035 28.758 1.00 32.36 ? 383 ASP A CA 1 ATOM 3068 C C . ASP A 1 383 ? 18.745 54.903 27.536 1.00 32.75 ? 383 ASP A C 1 ATOM 3069 O O . ASP A 1 383 ? 19.086 56.085 27.522 1.00 32.57 ? 383 ASP A O 1 ATOM 3070 C CB . ASP A 1 383 ? 18.162 54.462 29.935 1.00 31.96 ? 383 ASP A CB 1 ATOM 3071 C CG . ASP A 1 383 ? 16.732 54.011 29.782 1.00 34.11 ? 383 ASP A CG 1 ATOM 3072 O OD1 . ASP A 1 383 ? 16.317 53.075 30.505 1.00 34.58 ? 383 ASP A OD1 1 ATOM 3073 O OD2 . ASP A 1 383 ? 16.025 54.587 28.927 1.00 34.68 ? 383 ASP A OD2 1 ATOM 3074 N N . THR A 1 384 ? 18.131 54.327 26.509 1.00 32.58 ? 384 THR A N 1 ATOM 3075 C CA . THR A 1 384 ? 17.865 55.085 25.291 1.00 32.85 ? 384 THR A CA 1 ATOM 3076 C C . THR A 1 384 ? 16.390 55.285 24.991 1.00 33.02 ? 384 THR A C 1 ATOM 3077 O O . THR A 1 384 ? 16.015 55.547 23.849 1.00 32.89 ? 384 THR A O 1 ATOM 3078 C CB . THR A 1 384 ? 18.540 54.409 24.071 1.00 33.31 ? 384 THR A CB 1 ATOM 3079 O OG1 . THR A 1 384 ? 18.260 53.004 24.089 1.00 32.50 ? 384 THR A OG1 1 ATOM 3080 C CG2 . THR A 1 384 ? 20.050 54.622 24.106 1.00 31.47 ? 384 THR A CG2 1 ATOM 3081 N N . THR A 1 385 ? 15.562 55.178 26.026 1.00 33.26 ? 385 THR A N 1 ATOM 3082 C CA . THR A 1 385 ? 14.115 55.336 25.895 1.00 31.78 ? 385 THR A CA 1 ATOM 3083 C C . THR A 1 385 ? 13.666 56.628 25.191 1.00 31.59 ? 385 THR A C 1 ATOM 3084 O O . THR A 1 385 ? 12.813 56.591 24.299 1.00 31.56 ? 385 THR A O 1 ATOM 3085 C CB . THR A 1 385 ? 13.437 55.281 27.286 1.00 32.02 ? 385 THR A CB 1 ATOM 3086 O OG1 . THR A 1 385 ? 13.798 54.063 27.947 1.00 31.03 ? 385 THR A OG1 1 ATOM 3087 C CG2 . THR A 1 385 ? 11.922 55.343 27.149 1.00 30.07 ? 385 THR A CG2 1 ATOM 3088 N N . LEU A 1 386 ? 14.230 57.765 25.587 1.00 29.68 ? 386 LEU A N 1 ATOM 3089 C CA . LEU A 1 386 ? 13.842 59.042 24.995 1.00 29.30 ? 386 LEU A CA 1 ATOM 3090 C C . LEU A 1 386 ? 14.966 59.690 24.197 1.00 29.68 ? 386 LEU A C 1 ATOM 3091 O O . LEU A 1 386 ? 14.812 60.800 23.683 1.00 29.75 ? 386 LEU A O 1 ATOM 3092 C CB . LEU A 1 386 ? 13.391 60.010 26.094 1.00 28.69 ? 386 LEU A CB 1 ATOM 3093 C CG . LEU A 1 386 ? 12.271 59.532 27.022 1.00 29.89 ? 386 LEU A CG 1 ATOM 3094 C CD1 . LEU A 1 386 ? 11.987 60.587 28.082 1.00 29.09 ? 386 LEU A CD1 1 ATOM 3095 C CD2 . LEU A 1 386 ? 11.019 59.252 26.209 1.00 27.56 ? 386 LEU A CD2 1 ATOM 3096 N N . VAL A 1 387 ? 16.094 58.997 24.090 1.00 28.99 ? 387 VAL A N 1 ATOM 3097 C CA . VAL A 1 387 ? 17.238 59.532 23.370 1.00 28.59 ? 387 VAL A CA 1 ATOM 3098 C C . VAL A 1 387 ? 16.988 59.739 21.880 1.00 28.73 ? 387 VAL A C 1 ATOM 3099 O O . VAL A 1 387 ? 16.364 58.907 21.227 1.00 29.67 ? 387 VAL A O 1 ATOM 3100 C CB . VAL A 1 387 ? 18.459 58.616 23.540 1.00 28.78 ? 387 VAL A CB 1 ATOM 3101 C CG1 . VAL A 1 387 ? 19.591 59.078 22.638 1.00 28.29 ? 387 VAL A CG1 1 ATOM 3102 C CG2 . VAL A 1 387 ? 18.906 58.626 24.995 1.00 28.21 ? 387 VAL A CG2 1 ATOM 3103 N N . ASP A 1 388 ? 17.465 60.863 21.356 1.00 27.91 ? 388 ASP A N 1 ATOM 3104 C CA . ASP A 1 388 ? 17.335 61.164 19.935 1.00 28.07 ? 388 ASP A CA 1 ATOM 3105 C C . ASP A 1 388 ? 18.585 60.580 19.290 1.00 27.82 ? 388 ASP A C 1 ATOM 3106 O O . ASP A 1 388 ? 19.686 61.111 19.453 1.00 27.94 ? 388 ASP A O 1 ATOM 3107 C CB . ASP A 1 388 ? 17.299 62.674 19.692 1.00 28.79 ? 388 ASP A CB 1 ATOM 3108 C CG . ASP A 1 388 ? 17.305 63.028 18.213 1.00 31.14 ? 388 ASP A CG 1 ATOM 3109 O OD1 . ASP A 1 388 ? 17.470 62.122 17.368 1.00 33.74 ? 388 ASP A OD1 1 ATOM 3110 O OD2 . ASP A 1 388 ? 17.151 64.220 17.889 1.00 33.72 ? 388 ASP A OD2 1 ATOM 3111 N N . PRO A 1 389 ? 18.431 59.477 18.545 1.00 26.92 ? 389 PRO A N 1 ATOM 3112 C CA . PRO A 1 389 ? 19.583 58.844 17.896 1.00 25.64 ? 389 PRO A CA 1 ATOM 3113 C C . PRO A 1 389 ? 20.409 59.769 17.005 1.00 24.97 ? 389 PRO A C 1 ATOM 3114 O O . PRO A 1 389 ? 21.633 59.658 16.965 1.00 25.53 ? 389 PRO A O 1 ATOM 3115 C CB . PRO A 1 389 ? 18.954 57.674 17.134 1.00 25.73 ? 389 PRO A CB 1 ATOM 3116 C CG . PRO A 1 389 ? 17.552 58.154 16.860 1.00 26.19 ? 389 PRO A CG 1 ATOM 3117 C CD . PRO A 1 389 ? 17.169 58.828 18.146 1.00 25.32 ? 389 PRO A CD 1 ATOM 3118 N N . GLN A 1 390 ? 19.765 60.688 16.296 1.00 24.22 ? 390 GLN A N 1 ATOM 3119 C CA . GLN A 1 390 ? 20.534 61.583 15.440 1.00 24.76 ? 390 GLN A CA 1 ATOM 3120 C C . GLN A 1 390 ? 21.383 62.516 16.293 1.00 24.38 ? 390 GLN A C 1 ATOM 3121 O O . GLN A 1 390 ? 22.546 62.767 15.982 1.00 25.43 ? 390 GLN A O 1 ATOM 3122 C CB . GLN A 1 390 ? 19.626 62.415 14.531 1.00 24.75 ? 390 GLN A CB 1 ATOM 3123 C CG . GLN A 1 390 ? 20.404 63.462 13.750 1.00 27.78 ? 390 GLN A CG 1 ATOM 3124 C CD . GLN A 1 390 ? 19.542 64.263 12.802 1.00 30.39 ? 390 GLN A CD 1 ATOM 3125 O OE1 . GLN A 1 390 ? 18.409 64.606 13.122 1.00 35.09 ? 390 GLN A OE1 1 ATOM 3126 N NE2 . GLN A 1 390 ? 20.084 64.584 11.636 1.00 30.57 ? 390 GLN A NE2 1 ATOM 3127 N N . ALA A 1 391 ? 20.795 63.037 17.365 1.00 25.16 ? 391 ALA A N 1 ATOM 3128 C CA . ALA A 1 391 ? 21.512 63.941 18.258 1.00 25.54 ? 391 ALA A CA 1 ATOM 3129 C C . ALA A 1 391 ? 22.734 63.211 18.814 1.00 25.78 ? 391 ALA A C 1 ATOM 3130 O O . ALA A 1 391 ? 23.840 63.755 18.853 1.00 25.27 ? 391 ALA A O 1 ATOM 3131 C CB . ALA A 1 391 ? 20.598 64.387 19.396 1.00 24.98 ? 391 ALA A CB 1 ATOM 3132 N N . LEU A 1 392 ? 22.527 61.964 19.220 1.00 24.55 ? 392 LEU A N 1 ATOM 3133 C CA . LEU A 1 392 ? 23.603 61.163 19.770 1.00 25.74 ? 392 LEU A CA 1 ATOM 3134 C C . LEU A 1 392 ? 24.730 60.918 18.762 1.00 27.53 ? 392 LEU A C 1 ATOM 3135 O O . LEU A 1 392 ? 25.901 60.948 19.140 1.00 27.02 ? 392 LEU A O 1 ATOM 3136 C CB . LEU A 1 392 ? 23.043 59.838 20.284 1.00 24.65 ? 392 LEU A CB 1 ATOM 3137 C CG . LEU A 1 392 ? 23.979 58.946 21.094 1.00 25.47 ? 392 LEU A CG 1 ATOM 3138 C CD1 . LEU A 1 392 ? 24.580 59.729 22.265 1.00 27.50 ? 392 LEU A CD1 1 ATOM 3139 C CD2 . LEU A 1 392 ? 23.190 57.754 21.599 1.00 23.61 ? 392 LEU A CD2 1 ATOM 3140 N N . CYS A 1 393 ? 24.403 60.692 17.487 1.00 28.14 ? 393 CYS A N 1 ATOM 3141 C CA . CYS A 1 393 ? 25.462 60.456 16.499 1.00 31.17 ? 393 CYS A CA 1 ATOM 3142 C C . CYS A 1 393 ? 26.221 61.734 16.202 1.00 29.89 ? 393 CYS A C 1 ATOM 3143 O O . CYS A 1 393 ? 27.414 61.699 15.917 1.00 29.40 ? 393 CYS A O 1 ATOM 3144 C CB . CYS A 1 393 ? 24.921 59.900 15.175 1.00 32.73 ? 393 CYS A CB 1 ATOM 3145 S SG . CYS A 1 393 ? 24.141 58.245 15.231 1.00 47.00 ? 393 CYS A SG 1 ATOM 3146 N N . ASN A 1 394 ? 25.528 62.865 16.247 1.00 29.43 ? 394 ASN A N 1 ATOM 3147 C CA . ASN A 1 394 ? 26.192 64.135 15.991 1.00 30.90 ? 394 ASN A CA 1 ATOM 3148 C C . ASN A 1 394 ? 27.074 64.514 17.176 1.00 30.80 ? 394 ASN A C 1 ATOM 3149 O O . ASN A 1 394 ? 28.073 65.212 17.020 1.00 30.47 ? 394 ASN A O 1 ATOM 3150 C CB . ASN A 1 394 ? 25.158 65.222 15.702 1.00 29.88 ? 394 ASN A CB 1 ATOM 3151 C CG . ASN A 1 394 ? 24.726 65.224 14.248 1.00 32.22 ? 394 ASN A CG 1 ATOM 3152 O OD1 . ASN A 1 394 ? 25.485 65.638 13.369 1.00 32.50 ? 394 ASN A OD1 1 ATOM 3153 N ND2 . ASN A 1 394 ? 23.516 64.741 13.983 1.00 30.05 ? 394 ASN A ND2 1 ATOM 3154 N N . GLU A 1 395 ? 26.706 64.038 18.360 1.00 31.10 ? 395 GLU A N 1 ATOM 3155 C CA . GLU A 1 395 ? 27.490 64.309 19.554 1.00 32.44 ? 395 GLU A CA 1 ATOM 3156 C C . GLU A 1 395 ? 28.691 63.358 19.626 1.00 32.90 ? 395 GLU A C 1 ATOM 3157 O O . GLU A 1 395 ? 29.781 63.762 20.024 1.00 33.55 ? 395 GLU A O 1 ATOM 3158 C CB . GLU A 1 395 ? 26.628 64.142 20.811 1.00 33.82 ? 395 GLU A CB 1 ATOM 3159 C CG . GLU A 1 395 ? 27.427 64.185 22.110 1.00 38.65 ? 395 GLU A CG 1 ATOM 3160 C CD . GLU A 1 395 ? 26.574 63.976 23.360 1.00 42.71 ? 395 GLU A CD 1 ATOM 3161 O OE1 . GLU A 1 395 ? 25.789 63.000 23.410 1.00 41.89 ? 395 GLU A OE1 1 ATOM 3162 O OE2 . GLU A 1 395 ? 26.702 64.790 24.304 1.00 47.00 ? 395 GLU A OE2 1 ATOM 3163 N N . ARG A 1 396 ? 28.494 62.102 19.228 1.00 31.71 ? 396 ARG A N 1 ATOM 3164 C CA . ARG A 1 396 ? 29.569 61.111 19.280 1.00 29.83 ? 396 ARG A CA 1 ATOM 3165 C C . ARG A 1 396 ? 29.868 60.469 17.930 1.00 28.68 ? 396 ARG A C 1 ATOM 3166 O O . ARG A 1 396 ? 29.300 59.433 17.585 1.00 26.85 ? 396 ARG A O 1 ATOM 3167 C CB . ARG A 1 396 ? 29.219 60.010 20.283 1.00 31.38 ? 396 ARG A CB 1 ATOM 3168 C CG . ARG A 1 396 ? 28.882 60.515 21.671 1.00 34.83 ? 396 ARG A CG 1 ATOM 3169 C CD . ARG A 1 396 ? 28.635 59.371 22.643 1.00 36.79 ? 396 ARG A CD 1 ATOM 3170 N NE . ARG A 1 396 ? 27.871 59.831 23.802 1.00 41.61 ? 396 ARG A NE 1 ATOM 3171 C CZ . ARG A 1 396 ? 27.433 59.049 24.787 1.00 42.85 ? 396 ARG A CZ 1 ATOM 3172 N NH1 . ARG A 1 396 ? 27.680 57.742 24.773 1.00 42.80 ? 396 ARG A NH1 1 ATOM 3173 N NH2 . ARG A 1 396 ? 26.735 59.579 25.786 1.00 42.46 ? 396 ARG A NH2 1 ATOM 3174 N N . GLY A 1 397 ? 30.771 61.083 17.176 1.00 26.99 ? 397 GLY A N 1 ATOM 3175 C CA . GLY A 1 397 ? 31.132 60.547 15.879 1.00 27.20 ? 397 GLY A CA 1 ATOM 3176 C C . GLY A 1 397 ? 32.151 59.432 15.997 1.00 28.32 ? 397 GLY A C 1 ATOM 3177 O O . GLY A 1 397 ? 32.380 58.897 17.084 1.00 28.64 ? 397 GLY A O 1 ATOM 3178 N N . ALA A 1 398 ? 32.772 59.089 14.874 1.00 29.09 ? 398 ALA A N 1 ATOM 3179 C CA . ALA A 1 398 ? 33.767 58.022 14.826 1.00 30.00 ? 398 ALA A CA 1 ATOM 3180 C C . ALA A 1 398 ? 34.954 58.272 15.757 1.00 31.40 ? 398 ALA A C 1 ATOM 3181 O O . ALA A 1 398 ? 35.648 57.330 16.156 1.00 30.85 ? 398 ALA A O 1 ATOM 3182 C CB . ALA A 1 398 ? 34.260 57.838 13.391 1.00 27.23 ? 398 ALA A CB 1 ATOM 3183 N N . SER A 1 399 ? 35.186 59.535 16.101 1.00 30.44 ? 399 SER A N 1 ATOM 3184 C CA . SER A 1 399 ? 36.296 59.889 16.977 1.00 30.62 ? 399 SER A CA 1 ATOM 3185 C C . SER A 1 399 ? 35.967 59.719 18.456 1.00 29.85 ? 399 SER A C 1 ATOM 3186 O O . SER A 1 399 ? 36.864 59.732 19.290 1.00 31.05 ? 399 SER A O 1 ATOM 3187 C CB . SER A 1 399 ? 36.728 61.329 16.725 1.00 30.54 ? 399 SER A CB 1 ATOM 3188 O OG . SER A 1 399 ? 35.668 62.218 17.024 1.00 32.45 ? 399 SER A OG 1 ATOM 3189 N N . SER A 1 400 ? 34.686 59.578 18.784 1.00 29.56 ? 400 SER A N 1 ATOM 3190 C CA . SER A 1 400 ? 34.270 59.393 20.176 1.00 30.35 ? 400 SER A CA 1 ATOM 3191 C C . SER A 1 400 ? 34.315 57.892 20.472 1.00 30.82 ? 400 SER A C 1 ATOM 3192 O O . SER A 1 400 ? 33.435 57.144 20.052 1.00 30.90 ? 400 SER A O 1 ATOM 3193 C CB . SER A 1 400 ? 32.849 59.935 20.379 1.00 30.35 ? 400 SER A CB 1 ATOM 3194 O OG . SER A 1 400 ? 32.371 59.669 21.689 1.00 32.61 ? 400 SER A OG 1 ATOM 3195 N N . ARG A 1 401 ? 35.338 57.457 21.200 1.00 30.45 ? 401 ARG A N 1 ATOM 3196 C CA . ARG A 1 401 ? 35.516 56.038 21.501 1.00 30.19 ? 401 ARG A CA 1 ATOM 3197 C C . ARG A 1 401 ? 34.659 55.462 22.628 1.00 30.91 ? 401 ARG A C 1 ATOM 3198 O O . ARG A 1 401 ? 34.637 55.990 23.738 1.00 32.70 ? 401 ARG A O 1 ATOM 3199 C CB . ARG A 1 401 ? 36.992 55.771 21.800 1.00 28.94 ? 401 ARG A CB 1 ATOM 3200 C CG . ARG A 1 401 ? 37.941 56.330 20.739 1.00 30.85 ? 401 ARG A CG 1 ATOM 3201 C CD . ARG A 1 401 ? 39.349 55.810 20.938 1.00 30.47 ? 401 ARG A CD 1 ATOM 3202 N NE . ARG A 1 401 ? 39.388 54.353 20.848 1.00 32.39 ? 401 ARG A NE 1 ATOM 3203 C CZ . ARG A 1 401 ? 40.421 53.603 21.225 1.00 33.50 ? 401 ARG A CZ 1 ATOM 3204 N NH1 . ARG A 1 401 ? 41.511 54.173 21.722 1.00 33.27 ? 401 ARG A NH1 1 ATOM 3205 N NH2 . ARG A 1 401 ? 40.363 52.282 21.110 1.00 31.59 ? 401 ARG A NH2 1 ATOM 3206 N N . GLY A 1 402 ? 33.960 54.368 22.341 1.00 29.31 ? 402 GLY A N 1 ATOM 3207 C CA . GLY A 1 402 ? 33.139 53.735 23.358 1.00 29.12 ? 402 GLY A CA 1 ATOM 3208 C C . GLY A 1 402 ? 33.681 52.350 23.676 1.00 30.07 ? 402 GLY A C 1 ATOM 3209 O O . GLY A 1 402 ? 34.824 52.035 23.339 1.00 29.88 ? 402 GLY A O 1 ATOM 3210 N N . ALA A 1 403 ? 32.877 51.524 24.338 1.00 29.31 ? 403 ALA A N 1 ATOM 3211 C CA . ALA A 1 403 ? 33.289 50.162 24.655 1.00 30.11 ? 403 ALA A CA 1 ATOM 3212 C C . ALA A 1 403 ? 32.971 49.359 23.397 1.00 30.00 ? 403 ALA A C 1 ATOM 3213 O O . ALA A 1 403 ? 33.870 48.889 22.699 1.00 29.66 ? 403 ALA A O 1 ATOM 3214 C CB . ALA A 1 403 ? 32.496 49.633 25.839 1.00 30.29 ? 403 ALA A CB 1 ATOM 3215 N N . LEU A 1 404 ? 31.679 49.216 23.116 1.00 29.57 ? 404 LEU A N 1 ATOM 3216 C CA . LEU A 1 404 ? 31.209 48.521 21.919 1.00 29.00 ? 404 LEU A CA 1 ATOM 3217 C C . LEU A 1 404 ? 30.859 49.605 20.900 1.00 28.57 ? 404 LEU A C 1 ATOM 3218 O O . LEU A 1 404 ? 29.750 50.147 20.901 1.00 27.91 ? 404 LEU A O 1 ATOM 3219 C CB . LEU A 1 404 ? 29.971 47.682 22.245 1.00 30.22 ? 404 LEU A CB 1 ATOM 3220 C CG . LEU A 1 404 ? 30.131 46.168 22.438 1.00 32.80 ? 404 LEU A CG 1 ATOM 3221 C CD1 . LEU A 1 404 ? 31.564 45.802 22.716 1.00 33.75 ? 404 LEU A CD1 1 ATOM 3222 C CD2 . LEU A 1 404 ? 29.231 45.717 23.572 1.00 32.93 ? 404 LEU A CD2 1 ATOM 3223 N N . GLY A 1 405 ? 31.819 49.933 20.043 1.00 27.12 ? 405 GLY A N 1 ATOM 3224 C CA . GLY A 1 405 ? 31.596 50.964 19.051 1.00 27.24 ? 405 GLY A CA 1 ATOM 3225 C C . GLY A 1 405 ? 32.500 52.155 19.316 1.00 28.18 ? 405 GLY A C 1 ATOM 3226 O O . GLY A 1 405 ? 32.977 52.340 20.441 1.00 27.77 ? 405 GLY A O 1 ATOM 3227 N N . PRO A 1 406 ? 32.755 52.990 18.301 1.00 27.71 ? 406 PRO A N 1 ATOM 3228 C CA . PRO A 1 406 ? 32.207 52.816 16.958 1.00 27.36 ? 406 PRO A CA 1 ATOM 3229 C C . PRO A 1 406 ? 32.955 51.803 16.100 1.00 27.93 ? 406 PRO A C 1 ATOM 3230 O O . PRO A 1 406 ? 34.181 51.805 16.040 1.00 29.11 ? 406 PRO A O 1 ATOM 3231 C CB . PRO A 1 406 ? 32.271 54.224 16.364 1.00 27.11 ? 406 PRO A CB 1 ATOM 3232 C CG . PRO A 1 406 ? 33.321 54.973 17.202 1.00 27.96 ? 406 PRO A CG 1 ATOM 3233 C CD . PRO A 1 406 ? 33.751 54.074 18.335 1.00 28.19 ? 406 PRO A CD 1 ATOM 3234 N N . PHE A 1 407 ? 32.209 50.923 15.448 1.00 27.70 ? 407 PHE A N 1 ATOM 3235 C CA . PHE A 1 407 ? 32.816 49.952 14.555 1.00 26.67 ? 407 PHE A CA 1 ATOM 3236 C C . PHE A 1 407 ? 31.941 49.899 13.322 1.00 26.34 ? 407 PHE A C 1 ATOM 3237 O O . PHE A 1 407 ? 30.715 49.880 13.411 1.00 26.24 ? 407 PHE A O 1 ATOM 3238 C CB . PHE A 1 407 ? 32.962 48.567 15.217 1.00 25.63 ? 407 PHE A CB 1 ATOM 3239 C CG . PHE A 1 407 ? 31.667 47.949 15.678 1.00 24.07 ? 407 PHE A CG 1 ATOM 3240 C CD1 . PHE A 1 407 ? 30.813 47.326 14.776 1.00 23.13 ? 407 PHE A CD1 1 ATOM 3241 C CD2 . PHE A 1 407 ? 31.317 47.967 17.025 1.00 24.42 ? 407 PHE A CD2 1 ATOM 3242 C CE1 . PHE A 1 407 ? 29.629 46.729 15.210 1.00 22.38 ? 407 PHE A CE1 1 ATOM 3243 C CE2 . PHE A 1 407 ? 30.136 47.373 17.470 1.00 23.11 ? 407 PHE A CE2 1 ATOM 3244 C CZ . PHE A 1 407 ? 29.290 46.752 16.558 1.00 23.23 ? 407 PHE A CZ 1 ATOM 3245 N N . GLY A 1 408 ? 32.578 49.927 12.164 1.00 26.25 ? 408 GLY A N 1 ATOM 3246 C CA . GLY A 1 408 ? 31.823 49.896 10.937 1.00 25.28 ? 408 GLY A CA 1 ATOM 3247 C C . GLY A 1 408 ? 32.686 50.120 9.721 1.00 26.16 ? 408 GLY A C 1 ATOM 3248 O O . GLY A 1 408 ? 33.770 49.550 9.590 1.00 26.72 ? 408 GLY A O 1 ATOM 3249 N N . LEU A 1 409 ? 32.218 50.995 8.846 1.00 27.17 ? 409 LEU A N 1 ATOM 3250 C CA . LEU A 1 409 ? 32.904 51.260 7.598 1.00 27.91 ? 409 LEU A CA 1 ATOM 3251 C C . LEU A 1 409 ? 33.300 52.719 7.394 1.00 27.83 ? 409 LEU A C 1 ATOM 3252 O O . LEU A 1 409 ? 32.641 53.630 7.895 1.00 28.01 ? 409 LEU A O 1 ATOM 3253 C CB . LEU A 1 409 ? 31.977 50.830 6.466 1.00 30.34 ? 409 LEU A CB 1 ATOM 3254 C CG . LEU A 1 409 ? 32.539 50.306 5.157 1.00 35.51 ? 409 LEU A CG 1 ATOM 3255 C CD1 . LEU A 1 409 ? 33.158 48.931 5.390 1.00 37.02 ? 409 LEU A CD1 1 ATOM 3256 C CD2 . LEU A 1 409 ? 31.409 50.209 4.142 1.00 37.75 ? 409 LEU A CD2 1 ATOM 3257 N N . LEU A 1 410 ? 34.387 52.929 6.657 1.00 26.40 ? 410 LEU A N 1 ATOM 3258 C CA . LEU A 1 410 ? 34.842 54.270 6.313 1.00 25.35 ? 410 LEU A CA 1 ATOM 3259 C C . LEU A 1 410 ? 34.732 54.286 4.789 1.00 26.41 ? 410 LEU A C 1 ATOM 3260 O O . LEU A 1 410 ? 35.527 53.640 4.099 1.00 27.10 ? 410 LEU A O 1 ATOM 3261 C CB . LEU A 1 410 ? 36.297 54.496 6.741 1.00 23.86 ? 410 LEU A CB 1 ATOM 3262 C CG . LEU A 1 410 ? 36.603 54.429 8.243 1.00 23.89 ? 410 LEU A CG 1 ATOM 3263 C CD1 . LEU A 1 410 ? 38.087 54.712 8.473 1.00 21.08 ? 410 LEU A CD1 1 ATOM 3264 C CD2 . LEU A 1 410 ? 35.747 55.434 9.002 1.00 20.90 ? 410 LEU A CD2 1 ATOM 3265 N N . ALA A 1 411 ? 33.730 54.992 4.268 1.00 25.39 ? 411 ALA A N 1 ATOM 3266 C CA . ALA A 1 411 ? 33.508 55.056 2.828 1.00 24.43 ? 411 ALA A CA 1 ATOM 3267 C C . ALA A 1 411 ? 33.886 56.424 2.261 1.00 25.26 ? 411 ALA A C 1 ATOM 3268 O O . ALA A 1 411 ? 34.010 57.390 3.008 1.00 26.44 ? 411 ALA A O 1 ATOM 3269 C CB . ALA A 1 411 ? 32.056 54.727 2.520 1.00 22.57 ? 411 ALA A CB 1 ATOM 3270 N N . MET A 1 412 ? 34.059 56.503 0.941 1.00 25.73 ? 412 MET A N 1 ATOM 3271 C CA . MET A 1 412 ? 34.461 57.746 0.279 1.00 26.85 ? 412 MET A CA 1 ATOM 3272 C C . MET A 1 412 ? 35.531 58.440 1.116 1.00 28.13 ? 412 MET A C 1 ATOM 3273 O O . MET A 1 412 ? 35.437 59.631 1.418 1.00 28.45 ? 412 MET A O 1 ATOM 3274 C CB . MET A 1 412 ? 33.265 58.681 0.083 1.00 26.29 ? 412 MET A CB 1 ATOM 3275 C CG . MET A 1 412 ? 32.233 58.177 -0.920 1.00 26.88 ? 412 MET A CG 1 ATOM 3276 S SD . MET A 1 412 ? 32.976 57.632 -2.478 1.00 29.04 ? 412 MET A SD 1 ATOM 3277 C CE . MET A 1 412 ? 33.685 59.163 -3.099 1.00 25.00 ? 412 MET A CE 1 ATOM 3278 N N . ALA A 1 413 ? 36.554 57.675 1.485 1.00 28.99 ? 413 ALA A N 1 ATOM 3279 C CA . ALA A 1 413 ? 37.644 58.185 2.304 1.00 28.96 ? 413 ALA A CA 1 ATOM 3280 C C . ALA A 1 413 ? 38.906 58.428 1.489 1.00 29.67 ? 413 ALA A C 1 ATOM 3281 O O . ALA A 1 413 ? 39.176 57.711 0.527 1.00 30.13 ? 413 ALA A O 1 ATOM 3282 C CB . ALA A 1 413 ? 37.939 57.197 3.423 1.00 26.18 ? 413 ALA A CB 1 ATOM 3283 N N . SER A 1 414 ? 39.671 59.449 1.866 1.00 30.56 ? 414 SER A N 1 ATOM 3284 C CA . SER A 1 414 ? 40.926 59.737 1.180 1.00 33.07 ? 414 SER A CA 1 ATOM 3285 C C . SER A 1 414 ? 41.965 58.789 1.780 1.00 34.47 ? 414 SER A C 1 ATOM 3286 O O . SER A 1 414 ? 41.767 58.252 2.872 1.00 33.59 ? 414 SER A O 1 ATOM 3287 C CB . SER A 1 414 ? 41.344 61.194 1.393 1.00 31.32 ? 414 SER A CB 1 ATOM 3288 O OG . SER A 1 414 ? 41.427 61.507 2.770 1.00 32.71 ? 414 SER A OG 1 ATOM 3289 N N . LYS A 1 415 ? 43.062 58.573 1.064 1.00 37.58 ? 415 LYS A N 1 ATOM 3290 C CA . LYS A 1 415 ? 44.108 57.668 1.533 1.00 40.64 ? 415 LYS A CA 1 ATOM 3291 C C . LYS A 1 415 ? 44.608 58.010 2.939 1.00 40.22 ? 415 LYS A C 1 ATOM 3292 O O . LYS A 1 415 ? 44.838 57.119 3.755 1.00 40.10 ? 415 LYS A O 1 ATOM 3293 C CB . LYS A 1 415 ? 45.284 57.673 0.549 1.00 43.62 ? 415 LYS A CB 1 ATOM 3294 C CG . LYS A 1 415 ? 46.286 56.546 0.776 1.00 48.62 ? 415 LYS A CG 1 ATOM 3295 C CD . LYS A 1 415 ? 47.414 56.582 -0.256 1.00 51.95 ? 415 LYS A CD 1 ATOM 3296 C CE . LYS A 1 415 ? 48.392 55.423 -0.060 1.00 53.77 ? 415 LYS A CE 1 ATOM 3297 N NZ . LYS A 1 415 ? 47.724 54.093 -0.223 1.00 56.39 ? 415 LYS A NZ 1 ATOM 3298 N N . ASP A 1 416 ? 44.766 59.300 3.218 1.00 39.72 ? 416 ASP A N 1 ATOM 3299 C CA . ASP A 1 416 ? 45.247 59.756 4.520 1.00 40.03 ? 416 ASP A CA 1 ATOM 3300 C C . ASP A 1 416 ? 44.134 59.916 5.559 1.00 39.05 ? 416 ASP A C 1 ATOM 3301 O O . ASP A 1 416 ? 44.384 60.367 6.681 1.00 38.32 ? 416 ASP A O 1 ATOM 3302 C CB . ASP A 1 416 ? 45.974 61.094 4.364 1.00 42.76 ? 416 ASP A CB 1 ATOM 3303 C CG . ASP A 1 416 ? 45.115 62.153 3.681 1.00 45.41 ? 416 ASP A CG 1 ATOM 3304 O OD1 . ASP A 1 416 ? 43.868 62.046 3.734 1.00 45.16 ? 416 ASP A OD1 1 ATOM 3305 O OD2 . ASP A 1 416 ? 45.688 63.103 3.103 1.00 47.24 ? 416 ASP A OD2 1 ATOM 3306 N N . LEU A 1 417 ? 42.913 59.555 5.181 1.00 36.66 ? 417 LEU A N 1 ATOM 3307 C CA . LEU A 1 417 ? 41.759 59.670 6.070 1.00 35.22 ? 417 LEU A CA 1 ATOM 3308 C C . LEU A 1 417 ? 41.482 61.107 6.505 1.00 34.68 ? 417 LEU A C 1 ATOM 3309 O O . LEU A 1 417 ? 40.860 61.343 7.538 1.00 33.92 ? 417 LEU A O 1 ATOM 3310 C CB . LEU A 1 417 ? 41.930 58.782 7.308 1.00 32.21 ? 417 LEU A CB 1 ATOM 3311 C CG . LEU A 1 417 ? 41.871 57.267 7.082 1.00 31.66 ? 417 LEU A CG 1 ATOM 3312 C CD1 . LEU A 1 417 ? 41.868 56.572 8.431 1.00 29.46 ? 417 LEU A CD1 1 ATOM 3313 C CD2 . LEU A 1 417 ? 40.618 56.889 6.293 1.00 28.95 ? 417 LEU A CD2 1 ATOM 3314 N N . LYS A 1 418 ? 41.944 62.065 5.708 1.00 36.20 ? 418 LYS A N 1 ATOM 3315 C CA . LYS A 1 418 ? 41.720 63.477 5.997 1.00 36.80 ? 418 LYS A CA 1 ATOM 3316 C C . LYS A 1 418 ? 40.228 63.735 5.780 1.00 35.08 ? 418 LYS A C 1 ATOM 3317 O O . LYS A 1 418 ? 39.644 64.637 6.375 1.00 36.31 ? 418 LYS A O 1 ATOM 3318 C CB . LYS A 1 418 ? 42.547 64.346 5.043 1.00 42.10 ? 418 LYS A CB 1 ATOM 3319 C CG . LYS A 1 418 ? 43.083 65.626 5.667 1.00 47.99 ? 418 LYS A CG 1 ATOM 3320 C CD . LYS A 1 418 ? 44.168 65.320 6.698 1.00 51.96 ? 418 LYS A CD 1 ATOM 3321 C CE . LYS A 1 418 ? 45.429 64.752 6.046 1.00 54.09 ? 418 LYS A CE 1 ATOM 3322 N NZ . LYS A 1 418 ? 46.109 65.745 5.157 1.00 55.53 ? 418 LYS A NZ 1 ATOM 3323 N N . GLU A 1 419 ? 39.627 62.938 4.903 1.00 31.75 ? 419 GLU A N 1 ATOM 3324 C CA . GLU A 1 419 ? 38.200 63.023 4.607 1.00 30.68 ? 419 GLU A CA 1 ATOM 3325 C C . GLU A 1 419 ? 37.648 61.599 4.650 1.00 29.08 ? 419 GLU A C 1 ATOM 3326 O O . GLU A 1 419 ? 38.255 60.673 4.113 1.00 28.39 ? 419 GLU A O 1 ATOM 3327 C CB . GLU A 1 419 ? 37.962 63.648 3.225 1.00 29.57 ? 419 GLU A CB 1 ATOM 3328 C CG . GLU A 1 419 ? 38.250 65.143 3.169 1.00 29.74 ? 419 GLU A CG 1 ATOM 3329 C CD . GLU A 1 419 ? 38.056 65.737 1.783 1.00 30.82 ? 419 GLU A CD 1 ATOM 3330 O OE1 . GLU A 1 419 ? 38.780 65.327 0.850 1.00 32.19 ? 419 GLU A OE1 1 ATOM 3331 O OE2 . GLU A 1 419 ? 37.178 66.616 1.624 1.00 31.19 ? 419 GLU A OE2 1 ATOM 3332 N N . GLN A 1 420 ? 36.502 61.426 5.300 1.00 27.07 ? 420 GLN A N 1 ATOM 3333 C CA . GLN A 1 420 ? 35.894 60.108 5.421 1.00 27.49 ? 420 GLN A CA 1 ATOM 3334 C C . GLN A 1 420 ? 34.433 60.209 5.839 1.00 27.54 ? 420 GLN A C 1 ATOM 3335 O O . GLN A 1 420 ? 34.019 61.183 6.475 1.00 27.89 ? 420 GLN A O 1 ATOM 3336 C CB . GLN A 1 420 ? 36.632 59.284 6.484 1.00 27.42 ? 420 GLN A CB 1 ATOM 3337 C CG . GLN A 1 420 ? 36.530 59.898 7.887 1.00 28.64 ? 420 GLN A CG 1 ATOM 3338 C CD . GLN A 1 420 ? 37.177 59.049 8.971 1.00 31.02 ? 420 GLN A CD 1 ATOM 3339 O OE1 . GLN A 1 420 ? 38.269 58.508 8.783 1.00 31.46 ? 420 GLN A OE1 1 ATOM 3340 N NE2 . GLN A 1 420 ? 36.512 58.943 10.120 1.00 26.57 ? 420 GLN A NE2 1 ATOM 3341 N N . SER A 1 421 ? 33.661 59.191 5.478 1.00 25.30 ? 421 SER A N 1 ATOM 3342 C CA . SER A 1 421 ? 32.259 59.110 5.857 1.00 24.97 ? 421 SER A CA 1 ATOM 3343 C C . SER A 1 421 ? 32.216 57.808 6.625 1.00 25.06 ? 421 SER A C 1 ATOM 3344 O O . SER A 1 421 ? 32.489 56.745 6.064 1.00 25.67 ? 421 SER A O 1 ATOM 3345 C CB . SER A 1 421 ? 31.366 59.033 4.625 1.00 24.34 ? 421 SER A CB 1 ATOM 3346 O OG . SER A 1 421 ? 31.456 60.230 3.881 1.00 25.13 ? 421 SER A OG 1 ATOM 3347 N N . ALA A 1 422 ? 31.897 57.890 7.910 1.00 23.58 ? 422 ALA A N 1 ATOM 3348 C CA . ALA A 1 422 ? 31.871 56.711 8.758 1.00 23.66 ? 422 ALA A CA 1 ATOM 3349 C C . ALA A 1 422 ? 30.478 56.178 9.067 1.00 24.17 ? 422 ALA A C 1 ATOM 3350 O O . ALA A 1 422 ? 29.667 56.868 9.690 1.00 25.22 ? 422 ALA A O 1 ATOM 3351 C CB . ALA A 1 422 ? 32.611 57.017 10.064 1.00 23.10 ? 422 ALA A CB 1 ATOM 3352 N N . ILE A 1 423 ? 30.198 54.953 8.626 1.00 24.13 ? 423 ILE A N 1 ATOM 3353 C CA . ILE A 1 423 ? 28.911 54.316 8.898 1.00 23.75 ? 423 ILE A CA 1 ATOM 3354 C C . ILE A 1 423 ? 29.247 53.246 9.927 1.00 23.83 ? 423 ILE A C 1 ATOM 3355 O O . ILE A 1 423 ? 29.997 52.309 9.644 1.00 22.44 ? 423 ILE A O 1 ATOM 3356 C CB . ILE A 1 423 ? 28.282 53.682 7.623 1.00 25.60 ? 423 ILE A CB 1 ATOM 3357 C CG1 . ILE A 1 423 ? 28.021 54.763 6.570 1.00 26.92 ? 423 ILE A CG1 1 ATOM 3358 C CG2 . ILE A 1 423 ? 26.928 53.056 7.962 1.00 21.96 ? 423 ILE A CG2 1 ATOM 3359 C CD1 . ILE A 1 423 ? 29.255 55.319 5.950 1.00 30.77 ? 423 ILE A CD1 1 ATOM 3360 N N . PHE A 1 424 ? 28.695 53.390 11.127 1.00 23.74 ? 424 PHE A N 1 ATOM 3361 C CA . PHE A 1 424 ? 29.024 52.471 12.201 1.00 22.60 ? 424 PHE A CA 1 ATOM 3362 C C . PHE A 1 424 ? 27.916 52.228 13.205 1.00 23.27 ? 424 PHE A C 1 ATOM 3363 O O . PHE A 1 424 ? 26.854 52.847 13.149 1.00 24.12 ? 424 PHE A O 1 ATOM 3364 C CB . PHE A 1 424 ? 30.240 53.014 12.941 1.00 22.30 ? 424 PHE A CB 1 ATOM 3365 C CG . PHE A 1 424 ? 29.991 54.335 13.637 1.00 22.91 ? 424 PHE A CG 1 ATOM 3366 C CD1 . PHE A 1 424 ? 29.301 54.382 14.852 1.00 22.29 ? 424 PHE A CD1 1 ATOM 3367 C CD2 . PHE A 1 424 ? 30.469 55.527 13.092 1.00 20.97 ? 424 PHE A CD2 1 ATOM 3368 C CE1 . PHE A 1 424 ? 29.097 55.595 15.521 1.00 22.38 ? 424 PHE A CE1 1 ATOM 3369 C CE2 . PHE A 1 424 ? 30.272 56.746 13.749 1.00 22.14 ? 424 PHE A CE2 1 ATOM 3370 C CZ . PHE A 1 424 ? 29.583 56.779 14.972 1.00 21.71 ? 424 PHE A CZ 1 ATOM 3371 N N . PHE A 1 425 ? 28.203 51.333 14.146 1.00 23.44 ? 425 PHE A N 1 ATOM 3372 C CA . PHE A 1 425 ? 27.269 50.966 15.202 1.00 24.23 ? 425 PHE A CA 1 ATOM 3373 C C . PHE A 1 425 ? 27.897 51.179 16.574 1.00 25.06 ? 425 PHE A C 1 ATOM 3374 O O . PHE A 1 425 ? 29.121 51.277 16.707 1.00 25.33 ? 425 PHE A O 1 ATOM 3375 C CB . PHE A 1 425 ? 26.900 49.487 15.096 1.00 22.61 ? 425 PHE A CB 1 ATOM 3376 C CG . PHE A 1 425 ? 26.296 49.098 13.784 1.00 24.34 ? 425 PHE A CG 1 ATOM 3377 C CD1 . PHE A 1 425 ? 24.960 49.360 13.516 1.00 22.91 ? 425 PHE A CD1 1 ATOM 3378 C CD2 . PHE A 1 425 ? 27.064 48.456 12.816 1.00 23.84 ? 425 PHE A CD2 1 ATOM 3379 C CE1 . PHE A 1 425 ? 24.395 48.987 12.304 1.00 22.71 ? 425 PHE A CE1 1 ATOM 3380 C CE2 . PHE A 1 425 ? 26.508 48.079 11.600 1.00 24.75 ? 425 PHE A CE2 1 ATOM 3381 C CZ . PHE A 1 425 ? 25.170 48.345 11.343 1.00 23.66 ? 425 PHE A CZ 1 ATOM 3382 N N . ARG A 1 426 ? 27.039 51.250 17.587 1.00 25.40 ? 426 ARG A N 1 ATOM 3383 C CA . ARG A 1 426 ? 27.462 51.370 18.978 1.00 26.04 ? 426 ARG A CA 1 ATOM 3384 C C . ARG A 1 426 ? 26.449 50.487 19.687 1.00 26.40 ? 426 ARG A C 1 ATOM 3385 O O . ARG A 1 426 ? 25.305 50.377 19.238 1.00 27.06 ? 426 ARG A O 1 ATOM 3386 C CB . ARG A 1 426 ? 27.345 52.809 19.506 1.00 25.61 ? 426 ARG A CB 1 ATOM 3387 C CG . ARG A 1 426 ? 27.946 53.875 18.600 1.00 30.86 ? 426 ARG A CG 1 ATOM 3388 C CD . ARG A 1 426 ? 28.052 55.233 19.299 1.00 28.19 ? 426 ARG A CD 1 ATOM 3389 N NE . ARG A 1 426 ? 29.270 55.247 20.075 1.00 32.27 ? 426 ARG A NE 1 ATOM 3390 C CZ . ARG A 1 426 ? 30.322 56.020 19.835 1.00 31.29 ? 426 ARG A CZ 1 ATOM 3391 N NH1 . ARG A 1 426 ? 30.331 56.892 18.835 1.00 26.83 ? 426 ARG A NH1 1 ATOM 3392 N NH2 . ARG A 1 426 ? 31.399 55.866 20.583 1.00 32.40 ? 426 ARG A NH2 1 ATOM 3393 N N . VAL A 1 427 ? 26.861 49.831 20.764 1.00 26.46 ? 427 VAL A N 1 ATOM 3394 C CA . VAL A 1 427 ? 25.936 48.991 21.510 1.00 26.26 ? 427 VAL A CA 1 ATOM 3395 C C . VAL A 1 427 ? 25.882 49.491 22.945 1.00 27.37 ? 427 VAL A C 1 ATOM 3396 O O . VAL A 1 427 ? 26.916 49.700 23.578 1.00 27.61 ? 427 VAL A O 1 ATOM 3397 C CB . VAL A 1 427 ? 26.368 47.507 21.503 1.00 27.13 ? 427 VAL A CB 1 ATOM 3398 C CG1 . VAL A 1 427 ? 25.359 46.668 22.283 1.00 25.67 ? 427 VAL A CG1 1 ATOM 3399 C CG2 . VAL A 1 427 ? 26.458 46.999 20.073 1.00 26.04 ? 427 VAL A CG2 1 ATOM 3400 N N . PHE A 1 428 ? 24.668 49.701 23.444 1.00 27.50 ? 428 PHE A N 1 ATOM 3401 C CA . PHE A 1 428 ? 24.463 50.175 24.806 1.00 26.62 ? 428 PHE A CA 1 ATOM 3402 C C . PHE A 1 428 ? 23.555 49.188 25.534 1.00 28.66 ? 428 PHE A C 1 ATOM 3403 O O . PHE A 1 428 ? 22.982 48.280 24.922 1.00 28.66 ? 428 PHE A O 1 ATOM 3404 C CB . PHE A 1 428 ? 23.761 51.538 24.799 1.00 25.01 ? 428 PHE A CB 1 ATOM 3405 C CG . PHE A 1 428 ? 24.520 52.623 24.087 1.00 23.58 ? 428 PHE A CG 1 ATOM 3406 C CD1 . PHE A 1 428 ? 25.621 53.226 24.680 1.00 23.61 ? 428 PHE A CD1 1 ATOM 3407 C CD2 . PHE A 1 428 ? 24.115 53.062 22.831 1.00 23.53 ? 428 PHE A CD2 1 ATOM 3408 C CE1 . PHE A 1 428 ? 26.308 54.257 24.034 1.00 21.96 ? 428 PHE A CE1 1 ATOM 3409 C CE2 . PHE A 1 428 ? 24.796 54.092 22.175 1.00 22.22 ? 428 PHE A CE2 1 ATOM 3410 C CZ . PHE A 1 428 ? 25.892 54.689 22.780 1.00 22.56 ? 428 PHE A CZ 1 ATOM 3411 N N . GLN A 1 429 ? 23.428 49.373 26.844 1.00 29.34 ? 429 GLN A N 1 ATOM 3412 C CA . GLN A 1 429 ? 22.538 48.552 27.654 1.00 29.84 ? 429 GLN A CA 1 ATOM 3413 C C . GLN A 1 429 ? 21.926 49.477 28.699 1.00 30.78 ? 429 GLN A C 1 ATOM 3414 O O . GLN A 1 429 ? 22.563 50.452 29.112 1.00 28.27 ? 429 GLN A O 1 ATOM 3415 C CB . GLN A 1 429 ? 23.297 47.416 28.349 1.00 30.15 ? 429 GLN A CB 1 ATOM 3416 C CG . GLN A 1 429 ? 24.317 47.858 29.386 1.00 28.81 ? 429 GLN A CG 1 ATOM 3417 C CD . GLN A 1 429 ? 24.984 46.677 30.085 1.00 30.89 ? 429 GLN A CD 1 ATOM 3418 O OE1 . GLN A 1 429 ? 26.214 46.559 30.095 1.00 29.86 ? 429 GLN A OE1 1 ATOM 3419 N NE2 . GLN A 1 429 ? 24.173 45.800 30.676 1.00 27.65 ? 429 GLN A NE2 1 ATOM 3420 N N . ASN A 1 430 ? 20.688 49.203 29.104 1.00 32.19 ? 430 ASN A N 1 ATOM 3421 C CA . ASN A 1 430 ? 20.063 50.026 30.132 1.00 34.32 ? 430 ASN A CA 1 ATOM 3422 C C . ASN A 1 430 ? 20.465 49.429 31.479 1.00 36.65 ? 430 ASN A C 1 ATOM 3423 O O . ASN A 1 430 ? 21.281 48.504 31.534 1.00 35.83 ? 430 ASN A O 1 ATOM 3424 C CB . ASN A 1 430 ? 18.532 50.067 29.989 1.00 32.28 ? 430 ASN A CB 1 ATOM 3425 C CG . ASN A 1 430 ? 17.887 48.701 30.108 1.00 32.91 ? 430 ASN A CG 1 ATOM 3426 O OD1 . ASN A 1 430 ? 18.518 47.733 30.529 1.00 34.22 ? 430 ASN A OD1 1 ATOM 3427 N ND2 . ASN A 1 430 ? 16.613 48.621 29.746 1.00 30.39 ? 430 ASN A ND2 1 ATOM 3428 N N . GLN A 1 431 ? 19.897 49.949 32.559 1.00 39.30 ? 431 GLN A N 1 ATOM 3429 C CA . GLN A 1 431 ? 20.241 49.466 33.884 1.00 42.51 ? 431 GLN A CA 1 ATOM 3430 C C . GLN A 1 431 ? 19.832 48.008 34.102 1.00 43.14 ? 431 GLN A C 1 ATOM 3431 O O . GLN A 1 431 ? 20.488 47.285 34.852 1.00 43.59 ? 431 GLN A O 1 ATOM 3432 C CB . GLN A 1 431 ? 19.601 50.363 34.949 1.00 45.58 ? 431 GLN A CB 1 ATOM 3433 C CG . GLN A 1 431 ? 20.355 50.372 36.272 1.00 50.09 ? 431 GLN A CG 1 ATOM 3434 C CD . GLN A 1 431 ? 21.806 50.809 36.107 1.00 53.53 ? 431 GLN A CD 1 ATOM 3435 O OE1 . GLN A 1 431 ? 22.088 51.907 35.613 1.00 54.79 ? 431 GLN A OE1 1 ATOM 3436 N NE2 . GLN A 1 431 ? 22.734 49.949 36.519 1.00 54.51 ? 431 GLN A NE2 1 ATOM 3437 N N . LEU A 1 432 ? 18.760 47.572 33.443 1.00 42.99 ? 432 LEU A N 1 ATOM 3438 C CA . LEU A 1 432 ? 18.287 46.198 33.592 1.00 43.37 ? 432 LEU A CA 1 ATOM 3439 C C . LEU A 1 432 ? 19.037 45.187 32.725 1.00 43.69 ? 432 LEU A C 1 ATOM 3440 O O . LEU A 1 432 ? 18.696 44.003 32.713 1.00 44.44 ? 432 LEU A O 1 ATOM 3441 C CB . LEU A 1 432 ? 16.789 46.104 33.280 1.00 44.55 ? 432 LEU A CB 1 ATOM 3442 C CG . LEU A 1 432 ? 15.815 46.886 34.167 1.00 47.17 ? 432 LEU A CG 1 ATOM 3443 C CD1 . LEU A 1 432 ? 16.140 46.614 35.631 1.00 47.29 ? 432 LEU A CD1 1 ATOM 3444 C CD2 . LEU A 1 432 ? 15.916 48.378 33.868 1.00 48.95 ? 432 LEU A CD2 1 ATOM 3445 N N . GLY A 1 433 ? 20.046 45.645 31.993 1.00 42.42 ? 433 GLY A N 1 ATOM 3446 C CA . GLY A 1 433 ? 20.803 44.729 31.158 1.00 41.74 ? 433 GLY A CA 1 ATOM 3447 C C . GLY A 1 433 ? 20.248 44.499 29.762 1.00 40.81 ? 433 GLY A C 1 ATOM 3448 O O . GLY A 1 433 ? 20.688 43.589 29.063 1.00 40.78 ? 433 GLY A O 1 ATOM 3449 N N . ARG A 1 434 ? 19.278 45.310 29.354 1.00 39.93 ? 434 ARG A N 1 ATOM 3450 C CA . ARG A 1 434 ? 18.693 45.193 28.022 1.00 39.70 ? 434 ARG A CA 1 ATOM 3451 C C . ARG A 1 434 ? 19.555 45.985 27.040 1.00 37.54 ? 434 ARG A C 1 ATOM 3452 O O . ARG A 1 434 ? 19.883 47.144 27.291 1.00 38.12 ? 434 ARG A O 1 ATOM 3453 C CB . ARG A 1 434 ? 17.265 45.736 28.030 1.00 44.16 ? 434 ARG A CB 1 ATOM 3454 C CG . ARG A 1 434 ? 16.247 44.751 28.573 1.00 51.42 ? 434 ARG A CG 1 ATOM 3455 C CD . ARG A 1 434 ? 15.818 43.794 27.474 1.00 57.74 ? 434 ARG A CD 1 ATOM 3456 N NE . ARG A 1 434 ? 15.639 42.426 27.949 1.00 61.48 ? 434 ARG A NE 1 ATOM 3457 C CZ . ARG A 1 434 ? 15.321 41.409 27.156 1.00 63.99 ? 434 ARG A CZ 1 ATOM 3458 N NH1 . ARG A 1 434 ? 15.144 41.620 25.856 1.00 65.02 ? 434 ARG A NH1 1 ATOM 3459 N NH2 . ARG A 1 434 ? 15.197 40.182 27.654 1.00 64.75 ? 434 ARG A NH2 1 ATOM 3460 N N . TYR A 1 435 ? 19.915 45.360 25.924 1.00 33.76 ? 435 TYR A N 1 ATOM 3461 C CA . TYR A 1 435 ? 20.764 46.006 24.926 1.00 31.94 ? 435 TYR A CA 1 ATOM 3462 C C . TYR A 1 435 ? 20.012 46.745 23.831 1.00 31.45 ? 435 TYR A C 1 ATOM 3463 O O . TYR A 1 435 ? 18.916 46.346 23.432 1.00 30.90 ? 435 TYR A O 1 ATOM 3464 C CB . TYR A 1 435 ? 21.667 44.971 24.258 1.00 30.27 ? 435 TYR A CB 1 ATOM 3465 C CG . TYR A 1 435 ? 22.564 44.234 25.217 1.00 30.50 ? 435 TYR A CG 1 ATOM 3466 C CD1 . TYR A 1 435 ? 23.684 44.852 25.771 1.00 29.42 ? 435 TYR A CD1 1 ATOM 3467 C CD2 . TYR A 1 435 ? 22.279 42.921 25.589 1.00 30.30 ? 435 TYR A CD2 1 ATOM 3468 C CE1 . TYR A 1 435 ? 24.500 44.180 26.672 1.00 31.53 ? 435 TYR A CE1 1 ATOM 3469 C CE2 . TYR A 1 435 ? 23.085 42.240 26.489 1.00 31.91 ? 435 TYR A CE2 1 ATOM 3470 C CZ . TYR A 1 435 ? 24.193 42.873 27.026 1.00 31.94 ? 435 TYR A CZ 1 ATOM 3471 O OH . TYR A 1 435 ? 24.990 42.195 27.912 1.00 34.33 ? 435 TYR A OH 1 ATOM 3472 N N . SER A 1 436 ? 20.614 47.828 23.351 1.00 29.14 ? 436 SER A N 1 ATOM 3473 C CA . SER A 1 436 ? 20.046 48.606 22.259 1.00 28.92 ? 436 SER A CA 1 ATOM 3474 C C . SER A 1 436 ? 21.197 48.823 21.274 1.00 27.86 ? 436 SER A C 1 ATOM 3475 O O . SER A 1 436 ? 22.365 48.830 21.671 1.00 28.95 ? 436 SER A O 1 ATOM 3476 C CB . SER A 1 436 ? 19.497 49.948 22.755 1.00 27.80 ? 436 SER A CB 1 ATOM 3477 O OG . SER A 1 436 ? 20.542 50.862 23.034 1.00 31.19 ? 436 SER A OG 1 ATOM 3478 N N . VAL A 1 437 ? 20.868 48.980 19.995 1.00 27.10 ? 437 VAL A N 1 ATOM 3479 C CA . VAL A 1 437 ? 21.872 49.172 18.954 1.00 24.69 ? 437 VAL A CA 1 ATOM 3480 C C . VAL A 1 437 ? 21.643 50.474 18.201 1.00 24.68 ? 437 VAL A C 1 ATOM 3481 O O . VAL A 1 437 ? 20.542 50.736 17.717 1.00 25.89 ? 437 VAL A O 1 ATOM 3482 C CB . VAL A 1 437 ? 21.838 48.006 17.930 1.00 24.42 ? 437 VAL A CB 1 ATOM 3483 C CG1 . VAL A 1 437 ? 22.894 48.227 16.842 1.00 21.62 ? 437 VAL A CG1 1 ATOM 3484 C CG2 . VAL A 1 437 ? 22.067 46.681 18.646 1.00 23.28 ? 437 VAL A CG2 1 ATOM 3485 N N . LEU A 1 438 ? 22.692 51.282 18.105 1.00 24.15 ? 438 LEU A N 1 ATOM 3486 C CA . LEU A 1 438 ? 22.626 52.557 17.405 1.00 24.10 ? 438 LEU A CA 1 ATOM 3487 C C . LEU A 1 438 ? 23.406 52.479 16.096 1.00 25.49 ? 438 LEU A C 1 ATOM 3488 O O . LEU A 1 438 ? 24.555 52.027 16.074 1.00 25.16 ? 438 LEU A O 1 ATOM 3489 C CB . LEU A 1 438 ? 23.223 53.672 18.266 1.00 23.24 ? 438 LEU A CB 1 ATOM 3490 C CG . LEU A 1 438 ? 23.341 55.036 17.572 1.00 25.49 ? 438 LEU A CG 1 ATOM 3491 C CD1 . LEU A 1 438 ? 21.951 55.675 17.451 1.00 24.10 ? 438 LEU A CD1 1 ATOM 3492 C CD2 . LEU A 1 438 ? 24.284 55.939 18.361 1.00 25.04 ? 438 LEU A CD2 1 ATOM 3493 N N . MET A 1 439 ? 22.775 52.913 15.009 1.00 25.96 ? 439 MET A N 1 ATOM 3494 C CA . MET A 1 439 ? 23.425 52.924 13.702 1.00 26.32 ? 439 MET A CA 1 ATOM 3495 C C . MET A 1 439 ? 23.662 54.383 13.330 1.00 25.48 ? 439 MET A C 1 ATOM 3496 O O . MET A 1 439 ? 22.743 55.199 13.391 1.00 25.18 ? 439 MET A O 1 ATOM 3497 C CB . MET A 1 439 ? 22.541 52.263 12.650 1.00 25.24 ? 439 MET A CB 1 ATOM 3498 C CG . MET A 1 439 ? 23.200 52.188 11.290 1.00 27.35 ? 439 MET A CG 1 ATOM 3499 S SD . MET A 1 439 ? 22.107 51.538 10.025 1.00 30.43 ? 439 MET A SD 1 ATOM 3500 C CE . MET A 1 439 ? 22.828 52.271 8.549 1.00 27.84 ? 439 MET A CE 1 ATOM 3501 N N . CYS A 1 440 ? 24.886 54.707 12.933 1.00 25.65 ? 440 CYS A N 1 ATOM 3502 C CA . CYS A 1 440 ? 25.225 56.081 12.599 1.00 26.38 ? 440 CYS A CA 1 ATOM 3503 C C . CYS A 1 440 ? 25.899 56.291 11.259 1.00 26.77 ? 440 CYS A C 1 ATOM 3504 O O . CYS A 1 440 ? 26.672 55.451 10.799 1.00 27.86 ? 440 CYS A O 1 ATOM 3505 C CB . CYS A 1 440 ? 26.193 56.662 13.627 1.00 28.71 ? 440 CYS A CB 1 ATOM 3506 S SG . CYS A 1 440 ? 25.653 56.874 15.343 1.00 34.03 ? 440 CYS A SG 1 ATOM 3507 N N . SER A 1 441 ? 25.615 57.444 10.661 1.00 24.75 ? 441 SER A N 1 ATOM 3508 C CA . SER A 1 441 ? 26.255 57.866 9.428 1.00 25.79 ? 441 SER A CA 1 ATOM 3509 C C . SER A 1 441 ? 26.890 59.185 9.847 1.00 26.82 ? 441 SER A C 1 ATOM 3510 O O . SER A 1 441 ? 26.248 60.240 9.820 1.00 26.13 ? 441 SER A O 1 ATOM 3511 C CB . SER A 1 441 ? 25.248 58.110 8.311 1.00 26.76 ? 441 SER A CB 1 ATOM 3512 O OG . SER A 1 441 ? 24.711 56.885 7.853 1.00 31.57 ? 441 SER A OG 1 ATOM 3513 N N . ASP A 1 442 ? 28.138 59.102 10.292 1.00 26.26 ? 442 ASP A N 1 ATOM 3514 C CA . ASP A 1 442 ? 28.884 60.265 10.737 1.00 25.74 ? 442 ASP A CA 1 ATOM 3515 C C . ASP A 1 442 ? 29.495 60.935 9.513 1.00 24.36 ? 442 ASP A C 1 ATOM 3516 O O . ASP A 1 442 ? 30.415 60.407 8.899 1.00 24.68 ? 442 ASP A O 1 ATOM 3517 C CB . ASP A 1 442 ? 29.965 59.824 11.736 1.00 26.10 ? 442 ASP A CB 1 ATOM 3518 C CG . ASP A 1 442 ? 30.962 60.927 12.060 1.00 27.63 ? 442 ASP A CG 1 ATOM 3519 O OD1 . ASP A 1 442 ? 30.695 62.104 11.727 1.00 27.30 ? 442 ASP A OD1 1 ATOM 3520 O OD2 . ASP A 1 442 ? 32.016 60.607 12.658 1.00 26.14 ? 442 ASP A OD2 1 ATOM 3521 N N . LEU A 1 443 ? 28.963 62.101 9.163 1.00 24.28 ? 443 LEU A N 1 ATOM 3522 C CA . LEU A 1 443 ? 29.426 62.851 8.001 1.00 24.47 ? 443 LEU A CA 1 ATOM 3523 C C . LEU A 1 443 ? 30.253 64.083 8.388 1.00 25.35 ? 443 LEU A C 1 ATOM 3524 O O . LEU A 1 443 ? 30.670 64.862 7.523 1.00 24.95 ? 443 LEU A O 1 ATOM 3525 C CB . LEU A 1 443 ? 28.206 63.274 7.167 1.00 23.46 ? 443 LEU A CB 1 ATOM 3526 C CG . LEU A 1 443 ? 27.572 62.282 6.169 1.00 25.29 ? 443 LEU A CG 1 ATOM 3527 C CD1 . LEU A 1 443 ? 27.767 60.857 6.612 1.00 24.01 ? 443 LEU A CD1 1 ATOM 3528 C CD2 . LEU A 1 443 ? 26.098 62.604 5.994 1.00 19.76 ? 443 LEU A CD2 1 ATOM 3529 N N . SER A 1 444 ? 30.497 64.244 9.686 1.00 25.35 ? 444 SER A N 1 ATOM 3530 C CA . SER A 1 444 ? 31.242 65.391 10.199 1.00 27.50 ? 444 SER A CA 1 ATOM 3531 C C . SER A 1 444 ? 32.561 65.652 9.484 1.00 27.70 ? 444 SER A C 1 ATOM 3532 O O . SER A 1 444 ? 32.971 66.802 9.338 1.00 28.38 ? 444 SER A O 1 ATOM 3533 C CB . SER A 1 444 ? 31.510 65.223 11.695 1.00 26.94 ? 444 SER A CB 1 ATOM 3534 O OG . SER A 1 444 ? 32.374 64.125 11.935 1.00 29.84 ? 444 SER A OG 1 ATOM 3535 N N . ARG A 1 445 ? 33.224 64.593 9.034 1.00 27.90 ? 445 ARG A N 1 ATOM 3536 C CA . ARG A 1 445 ? 34.499 64.750 8.344 1.00 28.20 ? 445 ARG A CA 1 ATOM 3537 C C . ARG A 1 445 ? 34.461 64.256 6.906 1.00 28.40 ? 445 ARG A C 1 ATOM 3538 O O . ARG A 1 445 ? 35.504 63.945 6.324 1.00 27.55 ? 445 ARG A O 1 ATOM 3539 C CB . ARG A 1 445 ? 35.594 64.004 9.097 1.00 29.25 ? 445 ARG A CB 1 ATOM 3540 C CG . ARG A 1 445 ? 35.955 64.626 10.431 1.00 33.34 ? 445 ARG A CG 1 ATOM 3541 C CD . ARG A 1 445 ? 37.072 63.844 11.085 1.00 35.29 ? 445 ARG A CD 1 ATOM 3542 N NE . ARG A 1 445 ? 36.585 62.766 11.939 1.00 36.14 ? 445 ARG A NE 1 ATOM 3543 C CZ . ARG A 1 445 ? 37.291 61.675 12.229 1.00 38.05 ? 445 ARG A CZ 1 ATOM 3544 N NH1 . ARG A 1 445 ? 38.507 61.516 11.716 1.00 36.23 ? 445 ARG A NH1 1 ATOM 3545 N NH2 . ARG A 1 445 ? 36.798 60.761 13.058 1.00 36.98 ? 445 ARG A NH2 1 ATOM 3546 N N . SER A 1 446 ? 33.265 64.192 6.331 1.00 27.57 ? 446 SER A N 1 ATOM 3547 C CA . SER A 1 446 ? 33.115 63.713 4.965 1.00 27.71 ? 446 SER A CA 1 ATOM 3548 C C . SER A 1 446 ? 33.767 64.646 3.955 1.00 28.03 ? 446 SER A C 1 ATOM 3549 O O . SER A 1 446 ? 34.085 64.231 2.840 1.00 27.97 ? 446 SER A O 1 ATOM 3550 C CB . SER A 1 446 ? 31.633 63.528 4.625 1.00 27.25 ? 446 SER A CB 1 ATOM 3551 O OG . SER A 1 446 ? 30.925 64.749 4.736 1.00 27.49 ? 446 SER A OG 1 ATOM 3552 N N . THR A 1 447 ? 33.980 65.902 4.337 1.00 28.27 ? 447 THR A N 1 ATOM 3553 C CA . THR A 1 447 ? 34.600 66.855 3.421 1.00 28.62 ? 447 THR A CA 1 ATOM 3554 C C . THR A 1 447 ? 35.294 67.999 4.145 1.00 29.06 ? 447 THR A C 1 ATOM 3555 O O . THR A 1 447 ? 34.921 68.347 5.265 1.00 29.46 ? 447 THR A O 1 ATOM 3556 C CB . THR A 1 447 ? 33.548 67.459 2.449 1.00 28.35 ? 447 THR A CB 1 ATOM 3557 O OG1 . THR A 1 447 ? 34.207 68.254 1.455 1.00 25.98 ? 447 THR A OG1 1 ATOM 3558 C CG2 . THR A 1 447 ? 32.553 68.332 3.208 1.00 26.55 ? 447 THR A CG2 1 ATOM 3559 N N . VAL A 1 448 ? 36.316 68.567 3.509 1.00 29.40 ? 448 VAL A N 1 ATOM 3560 C CA . VAL A 1 448 ? 37.029 69.707 4.080 1.00 31.30 ? 448 VAL A CA 1 ATOM 3561 C C . VAL A 1 448 ? 36.464 70.970 3.443 1.00 32.63 ? 448 VAL A C 1 ATOM 3562 O O . VAL A 1 448 ? 36.872 72.079 3.777 1.00 34.94 ? 448 VAL A O 1 ATOM 3563 C CB . VAL A 1 448 ? 38.554 69.659 3.804 1.00 30.73 ? 448 VAL A CB 1 ATOM 3564 C CG1 . VAL A 1 448 ? 39.164 68.445 4.479 1.00 30.35 ? 448 VAL A CG1 1 ATOM 3565 C CG2 . VAL A 1 448 ? 38.819 69.636 2.308 1.00 29.43 ? 448 VAL A CG2 1 ATOM 3566 N N . ARG A 1 449 ? 35.519 70.791 2.524 1.00 32.08 ? 449 ARG A N 1 ATOM 3567 C CA . ARG A 1 449 ? 34.889 71.912 1.840 1.00 32.86 ? 449 ARG A CA 1 ATOM 3568 C C . ARG A 1 449 ? 33.951 72.725 2.733 1.00 34.24 ? 449 ARG A C 1 ATOM 3569 O O . ARG A 1 449 ? 33.370 72.208 3.691 1.00 33.31 ? 449 ARG A O 1 ATOM 3570 C CB . ARG A 1 449 ? 34.099 71.419 0.630 1.00 32.30 ? 449 ARG A CB 1 ATOM 3571 C CG . ARG A 1 449 ? 34.946 70.959 -0.526 1.00 31.16 ? 449 ARG A CG 1 ATOM 3572 C CD . ARG A 1 449 ? 34.282 71.391 -1.806 1.00 33.21 ? 449 ARG A CD 1 ATOM 3573 N NE . ARG A 1 449 ? 33.320 70.421 -2.303 1.00 34.20 ? 449 ARG A NE 1 ATOM 3574 C CZ . ARG A 1 449 ? 32.249 70.734 -3.027 1.00 34.06 ? 449 ARG A CZ 1 ATOM 3575 N NH1 . ARG A 1 449 ? 31.986 71.997 -3.329 1.00 32.90 ? 449 ARG A NH1 1 ATOM 3576 N NH2 . ARG A 1 449 ? 31.462 69.773 -3.485 1.00 34.70 ? 449 ARG A NH2 1 ATOM 3577 N N . SER A 1 450 ? 33.804 74.003 2.400 1.00 35.02 ? 450 SER A N 1 ATOM 3578 C CA . SER A 1 450 ? 32.929 74.905 3.140 1.00 36.57 ? 450 SER A CA 1 ATOM 3579 C C . SER A 1 450 ? 31.561 74.907 2.470 1.00 36.44 ? 450 SER A C 1 ATOM 3580 O O . SER A 1 450 ? 31.432 74.529 1.304 1.00 36.75 ? 450 SER A O 1 ATOM 3581 C CB . SER A 1 450 ? 33.489 76.333 3.120 1.00 38.28 ? 450 SER A CB 1 ATOM 3582 O OG . SER A 1 450 ? 34.799 76.393 3.661 1.00 41.68 ? 450 SER A OG 1 ATOM 3583 N N . ASN A 1 451 ? 30.545 75.338 3.207 1.00 36.11 ? 451 ASN A N 1 ATOM 3584 C CA . ASN A 1 451 ? 29.185 75.416 2.676 1.00 38.02 ? 451 ASN A CA 1 ATOM 3585 C C . ASN A 1 451 ? 28.576 74.086 2.264 1.00 36.03 ? 451 ASN A C 1 ATOM 3586 O O . ASN A 1 451 ? 27.804 74.021 1.305 1.00 37.33 ? 451 ASN A O 1 ATOM 3587 C CB . ASN A 1 451 ? 29.139 76.370 1.485 1.00 40.39 ? 451 ASN A CB 1 ATOM 3588 C CG . ASN A 1 451 ? 29.698 77.724 1.822 1.00 43.93 ? 451 ASN A CG 1 ATOM 3589 O OD1 . ASN A 1 451 ? 29.289 78.342 2.806 1.00 45.55 ? 451 ASN A OD1 1 ATOM 3590 N ND2 . ASN A 1 451 ? 30.644 78.196 1.014 1.00 44.70 ? 451 ASN A ND2 1 ATOM 3591 N N . ILE A 1 452 ? 28.931 73.030 2.985 1.00 32.45 ? 452 ILE A N 1 ATOM 3592 C CA . ILE A 1 452 ? 28.387 71.711 2.720 1.00 29.61 ? 452 ILE A CA 1 ATOM 3593 C C . ILE A 1 452 ? 27.690 71.303 4.008 1.00 29.15 ? 452 ILE A C 1 ATOM 3594 O O . ILE A 1 452 ? 28.257 71.443 5.090 1.00 29.61 ? 452 ILE A O 1 ATOM 3595 C CB . ILE A 1 452 ? 29.497 70.682 2.400 1.00 28.15 ? 452 ILE A CB 1 ATOM 3596 C CG1 . ILE A 1 452 ? 30.315 71.140 1.190 1.00 26.55 ? 452 ILE A CG1 1 ATOM 3597 C CG2 . ILE A 1 452 ? 28.874 69.317 2.117 1.00 27.12 ? 452 ILE A CG2 1 ATOM 3598 C CD1 . ILE A 1 452 ? 29.538 71.196 -0.112 1.00 23.97 ? 452 ILE A CD1 1 ATOM 3599 N N . ASP A 1 453 ? 26.454 70.828 3.903 1.00 28.66 ? 453 ASP A N 1 ATOM 3600 C CA . ASP A 1 453 ? 25.725 70.395 5.086 1.00 27.36 ? 453 ASP A CA 1 ATOM 3601 C C . ASP A 1 453 ? 26.258 69.025 5.478 1.00 27.71 ? 453 ASP A C 1 ATOM 3602 O O . ASP A 1 453 ? 25.902 68.012 4.875 1.00 27.22 ? 453 ASP A O 1 ATOM 3603 C CB . ASP A 1 453 ? 24.232 70.296 4.793 1.00 28.35 ? 453 ASP A CB 1 ATOM 3604 C CG . ASP A 1 453 ? 23.430 69.852 6.006 1.00 31.64 ? 453 ASP A CG 1 ATOM 3605 O OD1 . ASP A 1 453 ? 24.036 69.415 7.009 1.00 31.95 ? 453 ASP A OD1 1 ATOM 3606 O OD2 . ASP A 1 453 ? 22.185 69.932 5.957 1.00 35.40 ? 453 ASP A OD2 1 ATOM 3607 N N . THR A 1 454 ? 27.113 69.001 6.493 1.00 27.09 ? 454 THR A N 1 ATOM 3608 C CA . THR A 1 454 ? 27.710 67.759 6.956 1.00 26.14 ? 454 THR A CA 1 ATOM 3609 C C . THR A 1 454 ? 27.047 67.177 8.203 1.00 26.25 ? 454 THR A C 1 ATOM 3610 O O . THR A 1 454 ? 27.688 66.459 8.974 1.00 26.34 ? 454 THR A O 1 ATOM 3611 C CB . THR A 1 454 ? 29.206 67.951 7.240 1.00 26.74 ? 454 THR A CB 1 ATOM 3612 O OG1 . THR A 1 454 ? 29.375 69.009 8.193 1.00 26.56 ? 454 THR A OG1 1 ATOM 3613 C CG2 . THR A 1 454 ? 29.949 68.298 5.952 1.00 25.14 ? 454 THR A CG2 1 ATOM 3614 N N . THR A 1 455 ? 25.770 67.494 8.404 1.00 25.85 ? 455 THR A N 1 ATOM 3615 C CA . THR A 1 455 ? 25.013 66.968 9.540 1.00 25.94 ? 455 THR A CA 1 ATOM 3616 C C . THR A 1 455 ? 25.056 65.436 9.476 1.00 27.01 ? 455 THR A C 1 ATOM 3617 O O . THR A 1 455 ? 25.005 64.851 8.386 1.00 26.51 ? 455 THR A O 1 ATOM 3618 C CB . THR A 1 455 ? 23.531 67.396 9.463 1.00 26.84 ? 455 THR A CB 1 ATOM 3619 O OG1 . THR A 1 455 ? 23.450 68.821 9.375 1.00 29.43 ? 455 THR A OG1 1 ATOM 3620 C CG2 . THR A 1 455 ? 22.763 66.925 10.693 1.00 26.41 ? 455 THR A CG2 1 ATOM 3621 N N . SER A 1 456 ? 25.149 64.791 10.635 1.00 24.86 ? 456 SER A N 1 ATOM 3622 C CA . SER A 1 456 ? 25.183 63.335 10.697 1.00 24.31 ? 456 SER A CA 1 ATOM 3623 C C . SER A 1 456 ? 23.790 62.780 10.956 1.00 23.81 ? 456 SER A C 1 ATOM 3624 O O . SER A 1 456 ? 22.911 63.495 11.434 1.00 24.16 ? 456 SER A O 1 ATOM 3625 C CB . SER A 1 456 ? 26.141 62.873 11.796 1.00 23.00 ? 456 SER A CB 1 ATOM 3626 O OG . SER A 1 456 ? 27.487 63.108 11.412 1.00 23.85 ? 456 SER A OG 1 ATOM 3627 N N . TYR A 1 457 ? 23.594 61.502 10.646 1.00 23.09 ? 457 TYR A N 1 ATOM 3628 C CA . TYR A 1 457 ? 22.297 60.856 10.834 1.00 21.94 ? 457 TYR A CA 1 ATOM 3629 C C . TYR A 1 457 ? 22.442 59.582 11.644 1.00 22.21 ? 457 TYR A C 1 ATOM 3630 O O . TYR A 1 457 ? 23.483 58.930 11.607 1.00 24.91 ? 457 TYR A O 1 ATOM 3631 C CB . TYR A 1 457 ? 21.681 60.528 9.471 1.00 21.76 ? 457 TYR A CB 1 ATOM 3632 C CG . TYR A 1 457 ? 21.633 61.724 8.559 1.00 21.08 ? 457 TYR A CG 1 ATOM 3633 C CD1 . TYR A 1 457 ? 20.778 62.790 8.826 1.00 21.25 ? 457 TYR A CD1 1 ATOM 3634 C CD2 . TYR A 1 457 ? 22.505 61.833 7.481 1.00 21.88 ? 457 TYR A CD2 1 ATOM 3635 C CE1 . TYR A 1 457 ? 20.803 63.945 8.041 1.00 23.00 ? 457 TYR A CE1 1 ATOM 3636 C CE2 . TYR A 1 457 ? 22.538 62.982 6.691 1.00 21.99 ? 457 TYR A CE2 1 ATOM 3637 C CZ . TYR A 1 457 ? 21.689 64.033 6.978 1.00 23.03 ? 457 TYR A CZ 1 ATOM 3638 O OH . TYR A 1 457 ? 21.741 65.182 6.221 1.00 25.25 ? 457 TYR A OH 1 ATOM 3639 N N . GLY A 1 458 ? 21.394 59.221 12.371 1.00 21.89 ? 458 GLY A N 1 ATOM 3640 C CA . GLY A 1 458 ? 21.452 58.012 13.164 1.00 22.31 ? 458 GLY A CA 1 ATOM 3641 C C . GLY A 1 458 ? 20.073 57.489 13.495 1.00 24.10 ? 458 GLY A C 1 ATOM 3642 O O . GLY A 1 458 ? 19.082 58.212 13.381 1.00 24.64 ? 458 GLY A O 1 ATOM 3643 N N . ALA A 1 459 ? 20.006 56.225 13.898 1.00 24.50 ? 459 ALA A N 1 ATOM 3644 C CA . ALA A 1 459 ? 18.739 55.602 14.267 1.00 24.76 ? 459 ALA A CA 1 ATOM 3645 C C . ALA A 1 459 ? 19.038 54.335 15.044 1.00 24.98 ? 459 ALA A C 1 ATOM 3646 O O . ALA A 1 459 ? 20.108 53.748 14.889 1.00 26.48 ? 459 ALA A O 1 ATOM 3647 C CB . ALA A 1 459 ? 17.927 55.266 13.017 1.00 24.20 ? 459 ALA A CB 1 ATOM 3648 N N . PHE A 1 460 ? 18.102 53.922 15.890 1.00 25.07 ? 460 PHE A N 1 ATOM 3649 C CA . PHE A 1 460 ? 18.277 52.706 16.663 1.00 26.77 ? 460 PHE A CA 1 ATOM 3650 C C . PHE A 1 460 ? 17.830 51.528 15.812 1.00 28.62 ? 460 PHE A C 1 ATOM 3651 O O . PHE A 1 460 ? 16.866 51.639 15.060 1.00 30.26 ? 460 PHE A O 1 ATOM 3652 C CB . PHE A 1 460 ? 17.466 52.779 17.958 1.00 25.96 ? 460 PHE A CB 1 ATOM 3653 C CG . PHE A 1 460 ? 18.052 53.720 18.970 1.00 27.34 ? 460 PHE A CG 1 ATOM 3654 C CD1 . PHE A 1 460 ? 17.413 54.911 19.290 1.00 26.80 ? 460 PHE A CD1 1 ATOM 3655 C CD2 . PHE A 1 460 ? 19.281 53.438 19.562 1.00 27.20 ? 460 PHE A CD2 1 ATOM 3656 C CE1 . PHE A 1 460 ? 17.991 55.813 20.184 1.00 27.89 ? 460 PHE A CE1 1 ATOM 3657 C CE2 . PHE A 1 460 ? 19.868 54.334 20.458 1.00 28.10 ? 460 PHE A CE2 1 ATOM 3658 C CZ . PHE A 1 460 ? 19.222 55.523 20.769 1.00 27.18 ? 460 PHE A CZ 1 ATOM 3659 N N . VAL A 1 461 ? 18.544 50.411 15.913 1.00 28.43 ? 461 VAL A N 1 ATOM 3660 C CA . VAL A 1 461 ? 18.213 49.219 15.135 1.00 28.04 ? 461 VAL A CA 1 ATOM 3661 C C . VAL A 1 461 ? 17.515 48.211 16.036 1.00 29.20 ? 461 VAL A C 1 ATOM 3662 O O . VAL A 1 461 ? 18.029 47.860 17.096 1.00 29.39 ? 461 VAL A O 1 ATOM 3663 C CB . VAL A 1 461 ? 19.482 48.567 14.550 1.00 26.75 ? 461 VAL A CB 1 ATOM 3664 C CG1 . VAL A 1 461 ? 19.096 47.481 13.568 1.00 26.98 ? 461 VAL A CG1 1 ATOM 3665 C CG2 . VAL A 1 461 ? 20.352 49.621 13.876 1.00 25.11 ? 461 VAL A CG2 1 ATOM 3666 N N . ASP A 1 462 ? 16.349 47.738 15.615 1.00 30.19 ? 462 ASP A N 1 ATOM 3667 C CA . ASP A 1 462 ? 15.603 46.790 16.427 1.00 32.22 ? 462 ASP A CA 1 ATOM 3668 C C . ASP A 1 462 ? 16.040 45.336 16.270 1.00 32.87 ? 462 ASP A C 1 ATOM 3669 O O . ASP A 1 462 ? 15.372 44.537 15.611 1.00 32.60 ? 462 ASP A O 1 ATOM 3670 C CB . ASP A 1 462 ? 14.106 46.921 16.140 1.00 35.09 ? 462 ASP A CB 1 ATOM 3671 C CG . ASP A 1 462 ? 13.268 45.961 16.968 1.00 39.11 ? 462 ASP A CG 1 ATOM 3672 O OD1 . ASP A 1 462 ? 13.683 45.638 18.104 1.00 39.83 ? 462 ASP A OD1 1 ATOM 3673 O OD2 . ASP A 1 462 ? 12.191 45.540 16.489 1.00 43.45 ? 462 ASP A OD2 1 ATOM 3674 N N . ILE A 1 463 ? 17.173 45.006 16.882 1.00 33.46 ? 463 ILE A N 1 ATOM 3675 C CA . ILE A 1 463 ? 17.708 43.652 16.860 1.00 33.35 ? 463 ILE A CA 1 ATOM 3676 C C . ILE A 1 463 ? 18.244 43.322 18.246 1.00 33.20 ? 463 ILE A C 1 ATOM 3677 O O . ILE A 1 463 ? 18.478 44.216 19.058 1.00 33.65 ? 463 ILE A O 1 ATOM 3678 C CB . ILE A 1 463 ? 18.864 43.492 15.851 1.00 33.77 ? 463 ILE A CB 1 ATOM 3679 C CG1 . ILE A 1 463 ? 19.990 44.470 16.179 1.00 33.28 ? 463 ILE A CG1 1 ATOM 3680 C CG2 . ILE A 1 463 ? 18.353 43.702 14.441 1.00 34.98 ? 463 ILE A CG2 1 ATOM 3681 C CD1 . ILE A 1 463 ? 21.188 44.323 15.268 1.00 33.44 ? 463 ILE A CD1 1 ATOM 3682 N N . ASP A 1 464 ? 18.430 42.033 18.508 1.00 33.49 ? 464 ASP A N 1 ATOM 3683 C CA . ASP A 1 464 ? 18.949 41.558 19.786 1.00 32.49 ? 464 ASP A CA 1 ATOM 3684 C C . ASP A 1 464 ? 20.401 41.143 19.547 1.00 31.89 ? 464 ASP A C 1 ATOM 3685 O O . ASP A 1 464 ? 20.663 40.085 18.970 1.00 31.35 ? 464 ASP A O 1 ATOM 3686 C CB . ASP A 1 464 ? 18.124 40.359 20.260 1.00 33.62 ? 464 ASP A CB 1 ATOM 3687 C CG . ASP A 1 464 ? 18.559 39.842 21.621 1.00 35.40 ? 464 ASP A CG 1 ATOM 3688 O OD1 . ASP A 1 464 ? 19.620 40.273 22.130 1.00 34.16 ? 464 ASP A OD1 1 ATOM 3689 O OD2 . ASP A 1 464 ? 17.833 38.988 22.176 1.00 37.71 ? 464 ASP A OD2 1 ATOM 3690 N N . PRO A 1 465 ? 21.363 41.969 19.998 1.00 31.15 ? 465 PRO A N 1 ATOM 3691 C CA . PRO A 1 465 ? 22.802 41.720 19.840 1.00 31.85 ? 465 PRO A CA 1 ATOM 3692 C C . PRO A 1 465 ? 23.265 40.390 20.429 1.00 33.30 ? 465 PRO A C 1 ATOM 3693 O O . PRO A 1 465 ? 24.315 39.871 20.052 1.00 33.69 ? 465 PRO A O 1 ATOM 3694 C CB . PRO A 1 465 ? 23.450 42.899 20.569 1.00 31.17 ? 465 PRO A CB 1 ATOM 3695 C CG . PRO A 1 465 ? 22.383 43.927 20.645 1.00 30.92 ? 465 PRO A CG 1 ATOM 3696 C CD . PRO A 1 465 ? 21.136 43.134 20.866 1.00 29.91 ? 465 PRO A CD 1 ATOM 3697 N N . ARG A 1 466 ? 22.488 39.848 21.360 1.00 34.06 ? 466 ARG A N 1 ATOM 3698 C CA . ARG A 1 466 ? 22.845 38.592 22.006 1.00 35.89 ? 466 ARG A CA 1 ATOM 3699 C C . ARG A 1 466 ? 22.738 37.401 21.068 1.00 37.15 ? 466 ARG A C 1 ATOM 3700 O O . ARG A 1 466 ? 23.574 36.499 21.109 1.00 38.67 ? 466 ARG A O 1 ATOM 3701 C CB . ARG A 1 466 ? 21.949 38.340 23.222 1.00 33.99 ? 466 ARG A CB 1 ATOM 3702 C CG . ARG A 1 466 ? 22.090 39.362 24.331 1.00 36.45 ? 466 ARG A CG 1 ATOM 3703 C CD . ARG A 1 466 ? 21.086 39.083 25.432 1.00 36.01 ? 466 ARG A CD 1 ATOM 3704 N NE . ARG A 1 466 ? 19.718 39.129 24.926 1.00 35.99 ? 466 ARG A NE 1 ATOM 3705 C CZ . ARG A 1 466 ? 18.655 38.735 25.618 1.00 38.11 ? 466 ARG A CZ 1 ATOM 3706 N NH1 . ARG A 1 466 ? 18.803 38.260 26.847 1.00 38.78 ? 466 ARG A NH1 1 ATOM 3707 N NH2 . ARG A 1 466 ? 17.442 38.814 25.084 1.00 38.25 ? 466 ARG A NH2 1 ATOM 3708 N N . SER A 1 467 ? 21.712 37.399 20.223 1.00 37.50 ? 467 SER A N 1 ATOM 3709 C CA . SER A 1 467 ? 21.495 36.284 19.319 1.00 38.39 ? 467 SER A CA 1 ATOM 3710 C C . SER A 1 467 ? 21.740 36.544 17.835 1.00 39.21 ? 467 SER A C 1 ATOM 3711 O O . SER A 1 467 ? 21.800 35.598 17.052 1.00 40.99 ? 467 SER A O 1 ATOM 3712 C CB . SER A 1 467 ? 20.082 35.743 19.514 1.00 38.33 ? 467 SER A CB 1 ATOM 3713 O OG . SER A 1 467 ? 19.121 36.748 19.254 1.00 43.03 ? 467 SER A OG 1 ATOM 3714 N N . GLU A 1 468 ? 21.870 37.801 17.426 1.00 38.45 ? 468 GLU A N 1 ATOM 3715 C CA . GLU A 1 468 ? 22.123 38.070 16.013 1.00 37.51 ? 468 GLU A CA 1 ATOM 3716 C C . GLU A 1 468 ? 23.259 39.046 15.769 1.00 35.84 ? 468 GLU A C 1 ATOM 3717 O O . GLU A 1 468 ? 23.369 40.070 16.441 1.00 35.82 ? 468 GLU A O 1 ATOM 3718 C CB . GLU A 1 468 ? 20.848 38.557 15.304 1.00 38.08 ? 468 GLU A CB 1 ATOM 3719 C CG . GLU A 1 468 ? 19.942 39.442 16.134 1.00 43.85 ? 468 GLU A CG 1 ATOM 3720 C CD . GLU A 1 468 ? 18.608 39.752 15.443 1.00 47.01 ? 468 GLU A CD 1 ATOM 3721 O OE1 . GLU A 1 468 ? 17.672 40.215 16.143 1.00 43.77 ? 468 GLU A OE1 1 ATOM 3722 O OE2 . GLU A 1 468 ? 18.500 39.541 14.207 1.00 47.75 ? 468 GLU A OE2 1 ATOM 3723 N N . GLU A 1 469 ? 24.116 38.707 14.809 1.00 33.15 ? 469 GLU A N 1 ATOM 3724 C CA . GLU A 1 469 ? 25.237 39.565 14.457 1.00 32.47 ? 469 GLU A CA 1 ATOM 3725 C C . GLU A 1 469 ? 24.675 40.846 13.857 1.00 30.69 ? 469 GLU A C 1 ATOM 3726 O O . GLU A 1 469 ? 23.558 40.865 13.339 1.00 29.44 ? 469 GLU A O 1 ATOM 3727 C CB . GLU A 1 469 ? 26.152 38.874 13.443 1.00 32.97 ? 469 GLU A CB 1 ATOM 3728 C CG . GLU A 1 469 ? 26.781 37.581 13.953 1.00 34.92 ? 469 GLU A CG 1 ATOM 3729 C CD . GLU A 1 469 ? 27.808 37.009 12.991 1.00 37.33 ? 469 GLU A CD 1 ATOM 3730 O OE1 . GLU A 1 469 ? 28.367 35.928 13.286 1.00 38.41 ? 469 GLU A OE1 1 ATOM 3731 O OE2 . GLU A 1 469 ? 28.060 37.643 11.941 1.00 36.73 ? 469 GLU A OE2 1 ATOM 3732 N N . ILE A 1 470 ? 25.450 41.916 13.934 1.00 29.95 ? 470 ILE A N 1 ATOM 3733 C CA . ILE A 1 470 ? 25.022 43.201 13.409 1.00 28.92 ? 470 ILE A CA 1 ATOM 3734 C C . ILE A 1 470 ? 25.524 43.332 11.983 1.00 27.97 ? 470 ILE A C 1 ATOM 3735 O O . ILE A 1 470 ? 26.731 43.412 11.756 1.00 27.75 ? 470 ILE A O 1 ATOM 3736 C CB . ILE A 1 470 ? 25.589 44.331 14.271 1.00 29.45 ? 470 ILE A CB 1 ATOM 3737 C CG1 . ILE A 1 470 ? 25.174 44.101 15.726 1.00 30.27 ? 470 ILE A CG1 1 ATOM 3738 C CG2 . ILE A 1 470 ? 25.096 45.675 13.764 1.00 28.80 ? 470 ILE A CG2 1 ATOM 3739 C CD1 . ILE A 1 470 ? 25.715 45.126 16.689 1.00 32.61 ? 470 ILE A CD1 1 ATOM 3740 N N . SER A 1 471 ? 24.607 43.352 11.021 1.00 25.53 ? 471 SER A N 1 ATOM 3741 C CA . SER A 1 471 ? 25.014 43.452 9.629 1.00 26.40 ? 471 SER A CA 1 ATOM 3742 C C . SER A 1 471 ? 24.749 44.811 9.003 1.00 25.54 ? 471 SER A C 1 ATOM 3743 O O . SER A 1 471 ? 23.806 45.521 9.368 1.00 24.79 ? 471 SER A O 1 ATOM 3744 C CB . SER A 1 471 ? 24.343 42.358 8.795 1.00 26.75 ? 471 SER A CB 1 ATOM 3745 O OG . SER A 1 471 ? 22.942 42.527 8.769 1.00 33.61 ? 471 SER A OG 1 ATOM 3746 N N . LEU A 1 472 ? 25.592 45.150 8.036 1.00 25.22 ? 472 LEU A N 1 ATOM 3747 C CA . LEU A 1 472 ? 25.507 46.423 7.349 1.00 25.12 ? 472 LEU A CA 1 ATOM 3748 C C . LEU A 1 472 ? 25.853 46.314 5.870 1.00 25.31 ? 472 LEU A C 1 ATOM 3749 O O . LEU A 1 472 ? 26.895 45.764 5.508 1.00 27.23 ? 472 LEU A O 1 ATOM 3750 C CB . LEU A 1 472 ? 26.465 47.416 8.011 1.00 24.45 ? 472 LEU A CB 1 ATOM 3751 C CG . LEU A 1 472 ? 26.644 48.787 7.355 1.00 23.96 ? 472 LEU A CG 1 ATOM 3752 C CD1 . LEU A 1 472 ? 25.355 49.584 7.477 1.00 23.02 ? 472 LEU A CD1 1 ATOM 3753 C CD2 . LEU A 1 472 ? 27.799 49.524 8.029 1.00 22.84 ? 472 LEU A CD2 1 ATOM 3754 N N . ARG A 1 473 ? 24.977 46.843 5.021 1.00 23.91 ? 473 ARG A N 1 ATOM 3755 C CA . ARG A 1 473 ? 25.214 46.856 3.585 1.00 23.83 ? 473 ARG A CA 1 ATOM 3756 C C . ARG A 1 473 ? 25.279 48.313 3.143 1.00 25.42 ? 473 ARG A C 1 ATOM 3757 O O . ARG A 1 473 ? 24.444 49.128 3.539 1.00 25.96 ? 473 ARG A O 1 ATOM 3758 C CB . ARG A 1 473 ? 24.092 46.156 2.820 1.00 22.32 ? 473 ARG A CB 1 ATOM 3759 C CG . ARG A 1 473 ? 24.335 46.142 1.314 1.00 22.59 ? 473 ARG A CG 1 ATOM 3760 C CD . ARG A 1 473 ? 23.234 45.423 0.562 1.00 22.89 ? 473 ARG A CD 1 ATOM 3761 N NE . ARG A 1 473 ? 23.454 45.459 -0.880 1.00 23.68 ? 473 ARG A NE 1 ATOM 3762 C CZ . ARG A 1 473 ? 22.572 45.019 -1.777 1.00 26.60 ? 473 ARG A CZ 1 ATOM 3763 N NH1 . ARG A 1 473 ? 21.412 44.505 -1.375 1.00 24.29 ? 473 ARG A NH1 1 ATOM 3764 N NH2 . ARG A 1 473 ? 22.841 45.100 -3.074 1.00 23.97 ? 473 ARG A NH2 1 ATOM 3765 N N . ASN A 1 474 ? 26.274 48.639 2.327 1.00 24.99 ? 474 ASN A N 1 ATOM 3766 C CA . ASN A 1 474 ? 26.444 49.994 1.840 1.00 24.97 ? 474 ASN A CA 1 ATOM 3767 C C . ASN A 1 474 ? 26.532 50.059 0.332 1.00 25.11 ? 474 ASN A C 1 ATOM 3768 O O . ASN A 1 474 ? 27.296 49.321 -0.293 1.00 25.88 ? 474 ASN A O 1 ATOM 3769 C CB . ASN A 1 474 ? 27.716 50.618 2.412 1.00 26.43 ? 474 ASN A CB 1 ATOM 3770 C CG . ASN A 1 474 ? 27.539 51.099 3.823 1.00 29.68 ? 474 ASN A CG 1 ATOM 3771 O OD1 . ASN A 1 474 ? 26.920 52.133 4.063 1.00 31.70 ? 474 ASN A OD1 1 ATOM 3772 N ND2 . ASN A 1 474 ? 28.073 50.343 4.777 1.00 32.52 ? 474 ASN A ND2 1 ATOM 3773 N N . LEU A 1 475 ? 25.736 50.950 -0.243 1.00 23.95 ? 475 LEU A N 1 ATOM 3774 C CA . LEU A 1 475 ? 25.744 51.189 -1.676 1.00 22.64 ? 475 LEU A CA 1 ATOM 3775 C C . LEU A 1 475 ? 26.542 52.482 -1.785 1.00 23.51 ? 475 LEU A C 1 ATOM 3776 O O . LEU A 1 475 ? 26.066 53.547 -1.385 1.00 24.80 ? 475 LEU A O 1 ATOM 3777 C CB . LEU A 1 475 ? 24.319 51.395 -2.182 1.00 22.23 ? 475 LEU A CB 1 ATOM 3778 C CG . LEU A 1 475 ? 23.698 50.290 -3.040 1.00 24.04 ? 475 LEU A CG 1 ATOM 3779 C CD1 . LEU A 1 475 ? 24.046 48.918 -2.503 1.00 23.24 ? 475 LEU A CD1 1 ATOM 3780 C CD2 . LEU A 1 475 ? 22.200 50.497 -3.094 1.00 21.86 ? 475 LEU A CD2 1 ATOM 3781 N N . ILE A 1 476 ? 27.770 52.385 -2.281 1.00 22.75 ? 476 ILE A N 1 ATOM 3782 C CA . ILE A 1 476 ? 28.625 53.553 -2.424 1.00 22.03 ? 476 ILE A CA 1 ATOM 3783 C C . ILE A 1 476 ? 28.622 53.996 -3.877 1.00 24.00 ? 476 ILE A C 1 ATOM 3784 O O . ILE A 1 476 ? 28.984 53.222 -4.770 1.00 24.37 ? 476 ILE A O 1 ATOM 3785 C CB . ILE A 1 476 ? 30.071 53.232 -2.007 1.00 22.21 ? 476 ILE A CB 1 ATOM 3786 C CG1 . ILE A 1 476 ? 30.086 52.712 -0.565 1.00 21.18 ? 476 ILE A CG1 1 ATOM 3787 C CG2 . ILE A 1 476 ? 30.945 54.478 -2.158 1.00 19.32 ? 476 ILE A CG2 1 ATOM 3788 C CD1 . ILE A 1 476 ? 31.460 52.268 -0.075 1.00 21.78 ? 476 ILE A CD1 1 ATOM 3789 N N . ASP A 1 477 ? 28.222 55.240 -4.120 1.00 24.34 ? 477 ASP A N 1 ATOM 3790 C CA . ASP A 1 477 ? 28.171 55.741 -5.489 1.00 24.52 ? 477 ASP A CA 1 ATOM 3791 C C . ASP A 1 477 ? 28.505 57.231 -5.569 1.00 25.50 ? 477 ASP A C 1 ATOM 3792 O O . ASP A 1 477 ? 27.619 58.074 -5.721 1.00 25.24 ? 477 ASP A O 1 ATOM 3793 C CB . ASP A 1 477 ? 26.782 55.467 -6.084 1.00 22.25 ? 477 ASP A CB 1 ATOM 3794 C CG . ASP A 1 477 ? 26.768 55.534 -7.600 1.00 23.21 ? 477 ASP A CG 1 ATOM 3795 O OD1 . ASP A 1 477 ? 25.688 55.333 -8.198 1.00 23.25 ? 477 ASP A OD1 1 ATOM 3796 O OD2 . ASP A 1 477 ? 27.836 55.783 -8.198 1.00 23.77 ? 477 ASP A OD2 1 ATOM 3797 N N . HIS A 1 478 ? 29.794 57.538 -5.456 1.00 25.66 ? 478 HIS A N 1 ATOM 3798 C CA . HIS A 1 478 ? 30.299 58.905 -5.529 1.00 25.97 ? 478 HIS A CA 1 ATOM 3799 C C . HIS A 1 478 ? 29.760 59.883 -4.486 1.00 26.89 ? 478 HIS A C 1 ATOM 3800 O O . HIS A 1 478 ? 30.295 59.948 -3.383 1.00 29.55 ? 478 HIS A O 1 ATOM 3801 C CB . HIS A 1 478 ? 30.087 59.455 -6.939 1.00 25.82 ? 478 HIS A CB 1 ATOM 3802 C CG . HIS A 1 478 ? 30.809 58.673 -7.990 1.00 29.09 ? 478 HIS A CG 1 ATOM 3803 N ND1 . HIS A 1 478 ? 30.377 57.437 -8.425 1.00 29.82 ? 478 HIS A ND1 1 ATOM 3804 C CD2 . HIS A 1 478 ? 31.979 58.908 -8.632 1.00 28.67 ? 478 HIS A CD2 1 ATOM 3805 C CE1 . HIS A 1 478 ? 31.250 56.945 -9.286 1.00 28.42 ? 478 HIS A CE1 1 ATOM 3806 N NE2 . HIS A 1 478 ? 32.232 57.817 -9.429 1.00 27.76 ? 478 HIS A NE2 1 ATOM 3807 N N . SER A 1 479 ? 28.716 60.643 -4.809 1.00 26.20 ? 479 SER A N 1 ATOM 3808 C CA . SER A 1 479 ? 28.195 61.610 -3.842 1.00 24.60 ? 479 SER A CA 1 ATOM 3809 C C . SER A 1 479 ? 27.014 61.110 -3.026 1.00 25.22 ? 479 SER A C 1 ATOM 3810 O O . SER A 1 479 ? 26.374 61.885 -2.310 1.00 25.23 ? 479 SER A O 1 ATOM 3811 C CB . SER A 1 479 ? 27.822 62.930 -4.528 1.00 24.22 ? 479 SER A CB 1 ATOM 3812 O OG . SER A 1 479 ? 26.694 62.794 -5.374 1.00 24.37 ? 479 SER A OG 1 ATOM 3813 N N . ILE A 1 480 ? 26.711 59.821 -3.141 1.00 23.71 ? 480 ILE A N 1 ATOM 3814 C CA . ILE A 1 480 ? 25.628 59.243 -2.356 1.00 22.07 ? 480 ILE A CA 1 ATOM 3815 C C . ILE A 1 480 ? 26.063 57.912 -1.755 1.00 22.55 ? 480 ILE A C 1 ATOM 3816 O O . ILE A 1 480 ? 26.819 57.156 -2.370 1.00 22.90 ? 480 ILE A O 1 ATOM 3817 C CB . ILE A 1 480 ? 24.341 59.003 -3.196 1.00 21.18 ? 480 ILE A CB 1 ATOM 3818 C CG1 . ILE A 1 480 ? 23.182 58.624 -2.262 1.00 18.44 ? 480 ILE A CG1 1 ATOM 3819 C CG2 . ILE A 1 480 ? 24.571 57.896 -4.223 1.00 17.93 ? 480 ILE A CG2 1 ATOM 3820 C CD1 . ILE A 1 480 ? 21.832 58.496 -2.956 1.00 16.73 ? 480 ILE A CD1 1 ATOM 3821 N N . ILE A 1 481 ? 25.600 57.651 -0.538 1.00 21.63 ? 481 ILE A N 1 ATOM 3822 C CA . ILE A 1 481 ? 25.880 56.400 0.151 1.00 22.25 ? 481 ILE A CA 1 ATOM 3823 C C . ILE A 1 481 ? 24.570 55.954 0.796 1.00 23.33 ? 481 ILE A C 1 ATOM 3824 O O . ILE A 1 481 ? 23.972 56.702 1.572 1.00 25.12 ? 481 ILE A O 1 ATOM 3825 C CB . ILE A 1 481 ? 26.930 56.570 1.272 1.00 22.51 ? 481 ILE A CB 1 ATOM 3826 C CG1 . ILE A 1 481 ? 28.287 56.934 0.683 1.00 23.28 ? 481 ILE A CG1 1 ATOM 3827 C CG2 . ILE A 1 481 ? 27.051 55.278 2.070 1.00 22.23 ? 481 ILE A CG2 1 ATOM 3828 C CD1 . ILE A 1 481 ? 29.329 57.214 1.738 1.00 22.25 ? 481 ILE A CD1 1 ATOM 3829 N N . GLU A 1 482 ? 24.111 54.751 0.466 1.00 23.08 ? 482 GLU A N 1 ATOM 3830 C CA . GLU A 1 482 ? 22.884 54.233 1.062 1.00 23.53 ? 482 GLU A CA 1 ATOM 3831 C C . GLU A 1 482 ? 23.278 53.084 1.983 1.00 24.08 ? 482 GLU A C 1 ATOM 3832 O O . GLU A 1 482 ? 23.852 52.084 1.543 1.00 23.87 ? 482 GLU A O 1 ATOM 3833 C CB . GLU A 1 482 ? 21.907 53.762 -0.017 1.00 21.79 ? 482 GLU A CB 1 ATOM 3834 C CG . GLU A 1 482 ? 21.447 54.886 -0.927 1.00 23.68 ? 482 GLU A CG 1 ATOM 3835 C CD . GLU A 1 482 ? 20.413 54.440 -1.942 1.00 25.86 ? 482 GLU A CD 1 ATOM 3836 O OE1 . GLU A 1 482 ? 19.309 54.037 -1.524 1.00 26.84 ? 482 GLU A OE1 1 ATOM 3837 O OE2 . GLU A 1 482 ? 20.702 54.489 -3.157 1.00 24.82 ? 482 GLU A OE2 1 ATOM 3838 N N . SER A 1 483 ? 22.971 53.246 3.265 1.00 22.98 ? 483 SER A N 1 ATOM 3839 C CA . SER A 1 483 ? 23.313 52.261 4.274 1.00 22.65 ? 483 SER A CA 1 ATOM 3840 C C . SER A 1 483 ? 22.090 51.520 4.786 1.00 23.10 ? 483 SER A C 1 ATOM 3841 O O . SER A 1 483 ? 21.090 52.132 5.165 1.00 24.19 ? 483 SER A O 1 ATOM 3842 C CB . SER A 1 483 ? 24.019 52.960 5.431 1.00 21.83 ? 483 SER A CB 1 ATOM 3843 O OG . SER A 1 483 ? 25.027 53.820 4.928 1.00 22.83 ? 483 SER A OG 1 ATOM 3844 N N . PHE A 1 484 ? 22.191 50.195 4.797 1.00 22.84 ? 484 PHE A N 1 ATOM 3845 C CA . PHE A 1 484 ? 21.114 49.325 5.247 1.00 22.51 ? 484 PHE A CA 1 ATOM 3846 C C . PHE A 1 484 ? 21.606 48.496 6.423 1.00 22.68 ? 484 PHE A C 1 ATOM 3847 O O . PHE A 1 484 ? 22.457 47.624 6.265 1.00 23.36 ? 484 PHE A O 1 ATOM 3848 C CB . PHE A 1 484 ? 20.690 48.393 4.109 1.00 19.92 ? 484 PHE A CB 1 ATOM 3849 C CG . PHE A 1 484 ? 20.204 49.114 2.880 1.00 19.40 ? 484 PHE A CG 1 ATOM 3850 C CD1 . PHE A 1 484 ? 18.844 49.343 2.681 1.00 19.41 ? 484 PHE A CD1 1 ATOM 3851 C CD2 . PHE A 1 484 ? 21.106 49.570 1.924 1.00 17.54 ? 484 PHE A CD2 1 ATOM 3852 C CE1 . PHE A 1 484 ? 18.388 50.018 1.541 1.00 18.12 ? 484 PHE A CE1 1 ATOM 3853 C CE2 . PHE A 1 484 ? 20.660 50.245 0.784 1.00 18.85 ? 484 PHE A CE2 1 ATOM 3854 C CZ . PHE A 1 484 ? 19.299 50.469 0.593 1.00 18.25 ? 484 PHE A CZ 1 ATOM 3855 N N . GLY A 1 485 ? 21.077 48.772 7.606 1.00 22.33 ? 485 GLY A N 1 ATOM 3856 C CA . GLY A 1 485 ? 21.490 48.014 8.765 1.00 21.30 ? 485 GLY A CA 1 ATOM 3857 C C . GLY A 1 485 ? 20.538 46.867 9.035 1.00 22.17 ? 485 GLY A C 1 ATOM 3858 O O . GLY A 1 485 ? 19.337 46.970 8.771 1.00 23.15 ? 485 GLY A O 1 ATOM 3859 N N . ALA A 1 486 ? 21.081 45.767 9.549 1.00 22.10 ? 486 ALA A N 1 ATOM 3860 C CA . ALA A 1 486 ? 20.286 44.595 9.897 1.00 22.51 ? 486 ALA A CA 1 ATOM 3861 C C . ALA A 1 486 ? 19.302 44.143 8.817 1.00 22.87 ? 486 ALA A C 1 ATOM 3862 O O . ALA A 1 486 ? 18.110 43.976 9.083 1.00 23.55 ? 486 ALA A O 1 ATOM 3863 C CB . ALA A 1 486 ? 19.539 44.852 11.213 1.00 18.17 ? 486 ALA A CB 1 ATOM 3864 N N . GLY A 1 487 ? 19.805 43.945 7.602 1.00 23.55 ? 487 GLY A N 1 ATOM 3865 C CA . GLY A 1 487 ? 18.964 43.480 6.511 1.00 23.21 ? 487 GLY A CA 1 ATOM 3866 C C . GLY A 1 487 ? 17.883 44.422 6.013 1.00 23.92 ? 487 GLY A C 1 ATOM 3867 O O . GLY A 1 487 ? 16.913 43.982 5.399 1.00 24.31 ? 487 GLY A O 1 ATOM 3868 N N . GLY A 1 488 ? 18.039 45.714 6.264 1.00 22.91 ? 488 GLY A N 1 ATOM 3869 C CA . GLY A 1 488 ? 17.042 46.653 5.801 1.00 23.13 ? 488 GLY A CA 1 ATOM 3870 C C . GLY A 1 488 ? 16.133 47.156 6.902 1.00 24.98 ? 488 GLY A C 1 ATOM 3871 O O . GLY A 1 488 ? 15.181 47.890 6.624 1.00 25.70 ? 488 GLY A O 1 ATOM 3872 N N . LYS A 1 489 ? 16.405 46.769 8.147 1.00 23.05 ? 489 LYS A N 1 ATOM 3873 C CA . LYS A 1 489 ? 15.578 47.246 9.249 1.00 21.70 ? 489 LYS A CA 1 ATOM 3874 C C . LYS A 1 489 ? 15.798 48.735 9.477 1.00 21.88 ? 489 LYS A C 1 ATOM 3875 O O . LYS A 1 489 ? 14.878 49.436 9.882 1.00 20.83 ? 489 LYS A O 1 ATOM 3876 C CB . LYS A 1 489 ? 15.886 46.497 10.546 1.00 21.39 ? 489 LYS A CB 1 ATOM 3877 C CG . LYS A 1 489 ? 15.006 45.286 10.776 1.00 23.59 ? 489 LYS A CG 1 ATOM 3878 C CD . LYS A 1 489 ? 15.312 44.606 12.099 1.00 24.59 ? 489 LYS A CD 1 ATOM 3879 C CE . LYS A 1 489 ? 14.351 43.451 12.334 1.00 26.84 ? 489 LYS A CE 1 ATOM 3880 N NZ . LYS A 1 489 ? 14.570 42.776 13.642 1.00 28.54 ? 489 LYS A NZ 1 ATOM 3881 N N . THR A 1 490 ? 17.010 49.216 9.205 1.00 21.28 ? 490 THR A N 1 ATOM 3882 C CA . THR A 1 490 ? 17.341 50.625 9.408 1.00 21.81 ? 490 THR A CA 1 ATOM 3883 C C . THR A 1 490 ? 18.127 51.172 8.229 1.00 22.97 ? 490 THR A C 1 ATOM 3884 O O . THR A 1 490 ? 19.273 50.770 7.996 1.00 23.11 ? 490 THR A O 1 ATOM 3885 C CB . THR A 1 490 ? 18.198 50.801 10.662 1.00 23.19 ? 490 THR A CB 1 ATOM 3886 O OG1 . THR A 1 490 ? 17.565 50.140 11.759 1.00 22.78 ? 490 THR A OG1 1 ATOM 3887 C CG2 . THR A 1 490 ? 18.376 52.274 10.989 1.00 22.50 ? 490 THR A CG2 1 ATOM 3888 N N . CYS A 1 491 ? 17.528 52.107 7.502 1.00 22.01 ? 491 CYS A N 1 ATOM 3889 C CA . CYS A 1 491 ? 18.183 52.676 6.337 1.00 22.11 ? 491 CYS A CA 1 ATOM 3890 C C . CYS A 1 491 ? 18.533 54.141 6.521 1.00 22.85 ? 491 CYS A C 1 ATOM 3891 O O . CYS A 1 491 ? 17.747 54.911 7.070 1.00 23.64 ? 491 CYS A O 1 ATOM 3892 C CB . CYS A 1 491 ? 17.273 52.516 5.126 1.00 21.83 ? 491 CYS A CB 1 ATOM 3893 S SG . CYS A 1 491 ? 16.592 50.852 5.002 1.00 23.83 ? 491 CYS A SG 1 ATOM 3894 N N . ILE A 1 492 ? 19.719 54.520 6.054 1.00 22.94 ? 492 ILE A N 1 ATOM 3895 C CA . ILE A 1 492 ? 20.179 55.899 6.152 1.00 21.91 ? 492 ILE A CA 1 ATOM 3896 C C . ILE A 1 492 ? 20.883 56.288 4.862 1.00 22.63 ? 492 ILE A C 1 ATOM 3897 O O . ILE A 1 492 ? 21.892 55.684 4.497 1.00 23.62 ? 492 ILE A O 1 ATOM 3898 C CB . ILE A 1 492 ? 21.195 56.094 7.293 1.00 22.03 ? 492 ILE A CB 1 ATOM 3899 C CG1 . ILE A 1 492 ? 20.605 55.632 8.624 1.00 19.81 ? 492 ILE A CG1 1 ATOM 3900 C CG2 . ILE A 1 492 ? 21.596 57.570 7.367 1.00 20.49 ? 492 ILE A CG2 1 ATOM 3901 C CD1 . ILE A 1 492 ? 21.576 55.758 9.782 1.00 20.70 ? 492 ILE A CD1 1 ATOM 3902 N N . THR A 1 493 ? 20.355 57.296 4.178 1.00 21.19 ? 493 THR A N 1 ATOM 3903 C CA . THR A 1 493 ? 20.948 57.762 2.934 1.00 21.44 ? 493 THR A CA 1 ATOM 3904 C C . THR A 1 493 ? 21.761 59.023 3.194 1.00 21.62 ? 493 THR A C 1 ATOM 3905 O O . THR A 1 493 ? 21.261 59.977 3.796 1.00 22.64 ? 493 THR A O 1 ATOM 3906 C CB . THR A 1 493 ? 19.864 58.069 1.894 1.00 20.50 ? 493 THR A CB 1 ATOM 3907 O OG1 . THR A 1 493 ? 19.173 56.860 1.567 1.00 21.68 ? 493 THR A OG1 1 ATOM 3908 C CG2 . THR A 1 493 ? 20.478 58.665 0.636 1.00 18.57 ? 493 THR A CG2 1 ATOM 3909 N N . SER A 1 494 ? 23.011 59.028 2.733 1.00 21.86 ? 494 SER A N 1 ATOM 3910 C CA . SER A 1 494 ? 23.898 60.170 2.929 1.00 21.15 ? 494 SER A CA 1 ATOM 3911 C C . SER A 1 494 ? 24.398 60.764 1.619 1.00 22.66 ? 494 SER A C 1 ATOM 3912 O O . SER A 1 494 ? 24.633 60.040 0.646 1.00 21.40 ? 494 SER A O 1 ATOM 3913 C CB . SER A 1 494 ? 25.134 59.760 3.738 1.00 21.84 ? 494 SER A CB 1 ATOM 3914 O OG . SER A 1 494 ? 24.806 59.087 4.938 1.00 24.32 ? 494 SER A OG 1 ATOM 3915 N N . ARG A 1 495 ? 24.555 62.086 1.605 1.00 22.18 ? 495 ARG A N 1 ATOM 3916 C CA . ARG A 1 495 ? 25.107 62.792 0.451 1.00 21.59 ? 495 ARG A CA 1 ATOM 3917 C C . ARG A 1 495 ? 26.414 63.393 0.976 1.00 22.09 ? 495 ARG A C 1 ATOM 3918 O O . ARG A 1 495 ? 26.416 64.092 2.001 1.00 20.72 ? 495 ARG A O 1 ATOM 3919 C CB . ARG A 1 495 ? 24.178 63.912 -0.036 1.00 20.37 ? 495 ARG A CB 1 ATOM 3920 C CG . ARG A 1 495 ? 22.914 63.437 -0.746 1.00 20.75 ? 495 ARG A CG 1 ATOM 3921 C CD . ARG A 1 495 ? 23.219 62.511 -1.925 1.00 19.77 ? 495 ARG A CD 1 ATOM 3922 N NE . ARG A 1 495 ? 23.991 63.132 -3.008 1.00 20.40 ? 495 ARG A NE 1 ATOM 3923 C CZ . ARG A 1 495 ? 23.506 64.011 -3.886 1.00 20.22 ? 495 ARG A CZ 1 ATOM 3924 N NH1 . ARG A 1 495 ? 22.240 64.402 -3.824 1.00 17.29 ? 495 ARG A NH1 1 ATOM 3925 N NH2 . ARG A 1 495 ? 24.283 64.470 -4.861 1.00 18.32 ? 495 ARG A NH2 1 ATOM 3926 N N . ILE A 1 496 ? 27.520 63.094 0.298 1.00 21.10 ? 496 ILE A N 1 ATOM 3927 C CA . ILE A 1 496 ? 28.825 63.597 0.709 1.00 22.21 ? 496 ILE A CA 1 ATOM 3928 C C . ILE A 1 496 ? 29.575 64.177 -0.484 1.00 24.29 ? 496 ILE A C 1 ATOM 3929 O O . ILE A 1 496 ? 29.439 63.696 -1.611 1.00 24.89 ? 496 ILE A O 1 ATOM 3930 C CB . ILE A 1 496 ? 29.692 62.483 1.373 1.00 22.09 ? 496 ILE A CB 1 ATOM 3931 C CG1 . ILE A 1 496 ? 30.014 61.363 0.370 1.00 22.03 ? 496 ILE A CG1 1 ATOM 3932 C CG2 . ILE A 1 496 ? 28.972 61.932 2.596 1.00 19.98 ? 496 ILE A CG2 1 ATOM 3933 C CD1 . ILE A 1 496 ? 28.827 60.508 -0.050 1.00 22.85 ? 496 ILE A CD1 1 ATOM 3934 N N . TYR A 1 497 ? 30.364 65.216 -0.230 1.00 24.67 ? 497 TYR A N 1 ATOM 3935 C CA . TYR A 1 497 ? 31.114 65.874 -1.289 1.00 25.29 ? 497 TYR A CA 1 ATOM 3936 C C . TYR A 1 497 ? 32.573 66.104 -0.906 1.00 27.09 ? 497 TYR A C 1 ATOM 3937 O O . TYR A 1 497 ? 33.012 67.250 -0.763 1.00 26.83 ? 497 TYR A O 1 ATOM 3938 C CB . TYR A 1 497 ? 30.468 67.218 -1.611 1.00 25.63 ? 497 TYR A CB 1 ATOM 3939 C CG . TYR A 1 497 ? 29.003 67.132 -1.976 1.00 26.17 ? 497 TYR A CG 1 ATOM 3940 C CD1 . TYR A 1 497 ? 28.598 67.021 -3.304 1.00 24.44 ? 497 TYR A CD1 1 ATOM 3941 C CD2 . TYR A 1 497 ? 28.018 67.176 -0.987 1.00 24.73 ? 497 TYR A CD2 1 ATOM 3942 C CE1 . TYR A 1 497 ? 27.249 66.965 -3.639 1.00 26.25 ? 497 TYR A CE1 1 ATOM 3943 C CE2 . TYR A 1 497 ? 26.670 67.117 -1.310 1.00 24.90 ? 497 TYR A CE2 1 ATOM 3944 C CZ . TYR A 1 497 ? 26.292 67.014 -2.637 1.00 26.27 ? 497 TYR A CZ 1 ATOM 3945 O OH . TYR A 1 497 ? 24.956 66.979 -2.959 1.00 28.57 ? 497 TYR A OH 1 ATOM 3946 N N . PRO A 1 498 ? 33.342 65.022 -0.720 1.00 27.10 ? 498 PRO A N 1 ATOM 3947 C CA . PRO A 1 498 ? 34.746 65.218 -0.360 1.00 27.66 ? 498 PRO A CA 1 ATOM 3948 C C . PRO A 1 498 ? 35.468 65.962 -1.480 1.00 29.61 ? 498 PRO A C 1 ATOM 3949 O O . PRO A 1 498 ? 35.107 65.848 -2.654 1.00 29.11 ? 498 PRO A O 1 ATOM 3950 C CB . PRO A 1 498 ? 35.258 63.792 -0.171 1.00 26.56 ? 498 PRO A CB 1 ATOM 3951 C CG . PRO A 1 498 ? 34.391 62.989 -1.106 1.00 25.42 ? 498 PRO A CG 1 ATOM 3952 C CD . PRO A 1 498 ? 33.028 63.589 -0.868 1.00 27.50 ? 498 PRO A CD 1 ATOM 3953 N N . LYS A 1 499 ? 36.485 66.727 -1.106 1.00 31.39 ? 499 LYS A N 1 ATOM 3954 C CA . LYS A 1 499 ? 37.258 67.503 -2.061 1.00 32.94 ? 499 LYS A CA 1 ATOM 3955 C C . LYS A 1 499 ? 38.252 66.646 -2.842 1.00 32.38 ? 499 LYS A C 1 ATOM 3956 O O . LYS A 1 499 ? 38.481 66.879 -4.028 1.00 32.19 ? 499 LYS A O 1 ATOM 3957 C CB . LYS A 1 499 ? 38.005 68.613 -1.320 1.00 36.86 ? 499 LYS A CB 1 ATOM 3958 C CG . LYS A 1 499 ? 38.758 69.593 -2.204 1.00 40.71 ? 499 LYS A CG 1 ATOM 3959 C CD . LYS A 1 499 ? 39.406 70.677 -1.343 1.00 44.83 ? 499 LYS A CD 1 ATOM 3960 C CE . LYS A 1 499 ? 40.012 71.792 -2.185 1.00 46.78 ? 499 LYS A CE 1 ATOM 3961 N NZ . LYS A 1 499 ? 41.073 71.276 -3.096 1.00 50.87 ? 499 LYS A NZ 1 ATOM 3962 N N . PHE A 1 500 ? 38.820 65.640 -2.184 1.00 31.42 ? 500 PHE A N 1 ATOM 3963 C CA . PHE A 1 500 ? 39.819 64.784 -2.822 1.00 31.40 ? 500 PHE A CA 1 ATOM 3964 C C . PHE A 1 500 ? 39.391 64.092 -4.114 1.00 32.11 ? 500 PHE A C 1 ATOM 3965 O O . PHE A 1 500 ? 40.229 63.834 -4.980 1.00 32.53 ? 500 PHE A O 1 ATOM 3966 C CB . PHE A 1 500 ? 40.326 63.730 -1.825 1.00 30.53 ? 500 PHE A CB 1 ATOM 3967 C CG . PHE A 1 500 ? 39.443 62.512 -1.709 1.00 30.99 ? 500 PHE A CG 1 ATOM 3968 C CD1 . PHE A 1 500 ? 39.516 61.487 -2.651 1.00 29.62 ? 500 PHE A CD1 1 ATOM 3969 C CD2 . PHE A 1 500 ? 38.536 62.391 -0.657 1.00 30.50 ? 500 PHE A CD2 1 ATOM 3970 C CE1 . PHE A 1 500 ? 38.702 60.360 -2.551 1.00 30.96 ? 500 PHE A CE1 1 ATOM 3971 C CE2 . PHE A 1 500 ? 37.715 61.266 -0.546 1.00 30.90 ? 500 PHE A CE2 1 ATOM 3972 C CZ . PHE A 1 500 ? 37.799 60.249 -1.496 1.00 31.94 ? 500 PHE A CZ 1 ATOM 3973 N N . VAL A 1 501 ? 38.102 63.787 -4.252 1.00 31.96 ? 501 VAL A N 1 ATOM 3974 C CA . VAL A 1 501 ? 37.628 63.086 -5.446 1.00 32.87 ? 501 VAL A CA 1 ATOM 3975 C C . VAL A 1 501 ? 37.922 63.807 -6.753 1.00 34.48 ? 501 VAL A C 1 ATOM 3976 O O . VAL A 1 501 ? 37.812 63.218 -7.829 1.00 34.07 ? 501 VAL A O 1 ATOM 3977 C CB . VAL A 1 501 ? 36.113 62.780 -5.377 1.00 31.52 ? 501 VAL A CB 1 ATOM 3978 C CG1 . VAL A 1 501 ? 35.836 61.806 -4.238 1.00 31.29 ? 501 VAL A CG1 1 ATOM 3979 C CG2 . VAL A 1 501 ? 35.324 64.063 -5.199 1.00 31.70 ? 501 VAL A CG2 1 ATOM 3980 N N . ASN A 1 502 ? 38.300 65.076 -6.669 1.00 36.74 ? 502 ASN A N 1 ATOM 3981 C CA . ASN A 1 502 ? 38.617 65.816 -7.880 1.00 38.58 ? 502 ASN A CA 1 ATOM 3982 C C . ASN A 1 502 ? 39.940 65.370 -8.490 1.00 39.84 ? 502 ASN A C 1 ATOM 3983 O O . ASN A 1 502 ? 40.101 65.408 -9.706 1.00 39.69 ? 502 ASN A O 1 ATOM 3984 C CB . ASN A 1 502 ? 38.666 67.318 -7.604 1.00 38.14 ? 502 ASN A CB 1 ATOM 3985 C CG . ASN A 1 502 ? 37.294 67.945 -7.579 1.00 39.57 ? 502 ASN A CG 1 ATOM 3986 O OD1 . ASN A 1 502 ? 36.789 68.325 -6.520 1.00 40.29 ? 502 ASN A OD1 1 ATOM 3987 N ND2 . ASN A 1 502 ? 36.671 68.050 -8.751 1.00 39.73 ? 502 ASN A ND2 1 ATOM 3988 N N . ASN A 1 503 ? 40.881 64.932 -7.656 1.00 42.04 ? 503 ASN A N 1 ATOM 3989 C CA . ASN A 1 503 ? 42.183 64.519 -8.167 1.00 45.38 ? 503 ASN A CA 1 ATOM 3990 C C . ASN A 1 503 ? 42.673 63.122 -7.815 1.00 45.40 ? 503 ASN A C 1 ATOM 3991 O O . ASN A 1 503 ? 43.500 62.565 -8.534 1.00 46.83 ? 503 ASN A O 1 ATOM 3992 C CB . ASN A 1 503 ? 43.254 65.530 -7.752 1.00 49.09 ? 503 ASN A CB 1 ATOM 3993 C CG . ASN A 1 503 ? 43.072 66.875 -8.427 1.00 55.15 ? 503 ASN A CG 1 ATOM 3994 O OD1 . ASN A 1 503 ? 42.339 67.738 -7.936 1.00 58.08 ? 503 ASN A OD1 1 ATOM 3995 N ND2 . ASN A 1 503 ? 43.727 67.056 -9.574 1.00 57.30 ? 503 ASN A ND2 1 ATOM 3996 N N . GLU A 1 504 ? 42.189 62.549 -6.720 1.00 44.96 ? 504 GLU A N 1 ATOM 3997 C CA . GLU A 1 504 ? 42.645 61.216 -6.345 1.00 44.34 ? 504 GLU A CA 1 ATOM 3998 C C . GLU A 1 504 ? 41.504 60.234 -6.136 1.00 43.22 ? 504 GLU A C 1 ATOM 3999 O O . GLU A 1 504 ? 40.342 60.625 -6.034 1.00 44.84 ? 504 GLU A O 1 ATOM 4000 C CB . GLU A 1 504 ? 43.526 61.297 -5.096 1.00 44.95 ? 504 GLU A CB 1 ATOM 4001 C CG . GLU A 1 504 ? 42.877 61.975 -3.914 1.00 50.03 ? 504 GLU A CG 1 ATOM 4002 C CD . GLU A 1 504 ? 43.893 62.478 -2.897 1.00 52.46 ? 504 GLU A CD 1 ATOM 4003 O OE1 . GLU A 1 504 ? 44.661 63.405 -3.233 1.00 53.45 ? 504 GLU A OE1 1 ATOM 4004 O OE2 . GLU A 1 504 ? 43.924 61.948 -1.764 1.00 54.48 ? 504 GLU A OE2 1 ATOM 4005 N N . GLU A 1 505 ? 41.841 58.952 -6.087 1.00 41.57 ? 505 GLU A N 1 ATOM 4006 C CA . GLU A 1 505 ? 40.843 57.913 -5.904 1.00 40.82 ? 505 GLU A CA 1 ATOM 4007 C C . GLU A 1 505 ? 40.404 57.740 -4.461 1.00 38.77 ? 505 GLU A C 1 ATOM 4008 O O . GLU A 1 505 ? 41.143 58.040 -3.520 1.00 36.89 ? 505 GLU A O 1 ATOM 4009 C CB . GLU A 1 505 ? 41.362 56.579 -6.434 1.00 44.24 ? 505 GLU A CB 1 ATOM 4010 C CG . GLU A 1 505 ? 41.544 56.551 -7.938 1.00 50.42 ? 505 GLU A CG 1 ATOM 4011 C CD . GLU A 1 505 ? 42.012 55.200 -8.438 1.00 54.93 ? 505 GLU A CD 1 ATOM 4012 O OE1 . GLU A 1 505 ? 43.078 54.730 -7.975 1.00 57.09 ? 505 GLU A OE1 1 ATOM 4013 O OE2 . GLU A 1 505 ? 41.312 54.609 -9.292 1.00 57.53 ? 505 GLU A OE2 1 ATOM 4014 N N . ALA A 1 506 ? 39.184 57.243 -4.304 1.00 36.13 ? 506 ALA A N 1 ATOM 4015 C CA . ALA A 1 506 ? 38.610 57.008 -2.994 1.00 34.65 ? 506 ALA A CA 1 ATOM 4016 C C . ALA A 1 506 ? 39.144 55.701 -2.439 1.00 33.85 ? 506 ALA A C 1 ATOM 4017 O O . ALA A 1 506 ? 39.661 54.861 -3.177 1.00 33.85 ? 506 ALA A O 1 ATOM 4018 C CB . ALA A 1 506 ? 37.092 56.944 -3.098 1.00 32.34 ? 506 ALA A CB 1 ATOM 4019 N N . HIS A 1 507 ? 39.022 55.539 -1.130 1.00 33.70 ? 507 HIS A N 1 ATOM 4020 C CA . HIS A 1 507 ? 39.462 54.325 -0.471 1.00 32.32 ? 507 HIS A CA 1 ATOM 4021 C C . HIS A 1 507 ? 38.333 53.815 0.404 1.00 30.91 ? 507 HIS A C 1 ATOM 4022 O O . HIS A 1 507 ? 37.402 54.554 0.729 1.00 29.26 ? 507 HIS A O 1 ATOM 4023 C CB . HIS A 1 507 ? 40.713 54.584 0.363 1.00 34.90 ? 507 HIS A CB 1 ATOM 4024 C CG . HIS A 1 507 ? 41.938 54.830 -0.460 1.00 35.90 ? 507 HIS A CG 1 ATOM 4025 N ND1 . HIS A 1 507 ? 42.110 55.968 -1.217 1.00 38.52 ? 507 HIS A ND1 1 ATOM 4026 C CD2 . HIS A 1 507 ? 43.040 54.073 -0.663 1.00 36.57 ? 507 HIS A CD2 1 ATOM 4027 C CE1 . HIS A 1 507 ? 43.267 55.902 -1.851 1.00 38.72 ? 507 HIS A CE1 1 ATOM 4028 N NE2 . HIS A 1 507 ? 43.851 54.761 -1.531 1.00 39.17 ? 507 HIS A NE2 1 ATOM 4029 N N . LEU A 1 508 ? 38.424 52.546 0.775 1.00 29.57 ? 508 LEU A N 1 ATOM 4030 C CA . LEU A 1 508 ? 37.412 51.899 1.589 1.00 28.86 ? 508 LEU A CA 1 ATOM 4031 C C . LEU A 1 508 ? 38.099 51.209 2.756 1.00 28.52 ? 508 LEU A C 1 ATOM 4032 O O . LEU A 1 508 ? 39.094 50.511 2.569 1.00 28.85 ? 508 LEU A O 1 ATOM 4033 C CB . LEU A 1 508 ? 36.668 50.878 0.728 1.00 29.33 ? 508 LEU A CB 1 ATOM 4034 C CG . LEU A 1 508 ? 35.626 49.972 1.374 1.00 29.52 ? 508 LEU A CG 1 ATOM 4035 C CD1 . LEU A 1 508 ? 34.471 50.802 1.909 1.00 28.60 ? 508 LEU A CD1 1 ATOM 4036 C CD2 . LEU A 1 508 ? 35.136 48.976 0.336 1.00 30.12 ? 508 LEU A CD2 1 ATOM 4037 N N . PHE A 1 509 ? 37.570 51.401 3.959 1.00 27.41 ? 509 PHE A N 1 ATOM 4038 C CA . PHE A 1 509 ? 38.161 50.796 5.148 1.00 27.27 ? 509 PHE A CA 1 ATOM 4039 C C . PHE A 1 509 ? 37.098 50.227 6.075 1.00 26.53 ? 509 PHE A C 1 ATOM 4040 O O . PHE A 1 509 ? 35.922 50.570 5.983 1.00 26.16 ? 509 PHE A O 1 ATOM 4041 C CB . PHE A 1 509 ? 38.934 51.831 5.973 1.00 27.12 ? 509 PHE A CB 1 ATOM 4042 C CG . PHE A 1 509 ? 39.990 52.581 5.216 1.00 28.31 ? 509 PHE A CG 1 ATOM 4043 C CD1 . PHE A 1 509 ? 41.324 52.201 5.303 1.00 28.08 ? 509 PHE A CD1 1 ATOM 4044 C CD2 . PHE A 1 509 ? 39.664 53.718 4.484 1.00 27.66 ? 509 PHE A CD2 1 ATOM 4045 C CE1 . PHE A 1 509 ? 42.320 52.946 4.677 1.00 28.04 ? 509 PHE A CE1 1 ATOM 4046 C CE2 . PHE A 1 509 ? 40.650 54.471 3.853 1.00 28.05 ? 509 PHE A CE2 1 ATOM 4047 C CZ . PHE A 1 509 ? 41.984 54.085 3.952 1.00 28.73 ? 509 PHE A CZ 1 ATOM 4048 N N . VAL A 1 510 ? 37.544 49.361 6.975 1.00 26.53 ? 510 VAL A N 1 ATOM 4049 C CA . VAL A 1 510 ? 36.697 48.772 8.001 1.00 27.56 ? 510 VAL A CA 1 ATOM 4050 C C . VAL A 1 510 ? 37.410 49.265 9.257 1.00 28.84 ? 510 VAL A C 1 ATOM 4051 O O . VAL A 1 510 ? 38.641 49.324 9.282 1.00 29.80 ? 510 VAL A O 1 ATOM 4052 C CB . VAL A 1 510 ? 36.723 47.235 7.953 1.00 27.25 ? 510 VAL A CB 1 ATOM 4053 C CG1 . VAL A 1 510 ? 35.830 46.673 9.039 1.00 27.60 ? 510 VAL A CG1 1 ATOM 4054 C CG2 . VAL A 1 510 ? 36.248 46.753 6.590 1.00 26.69 ? 510 VAL A CG2 1 ATOM 4055 N N . PHE A 1 511 ? 36.674 49.648 10.291 1.00 29.19 ? 511 PHE A N 1 ATOM 4056 C CA . PHE A 1 511 ? 37.349 50.147 11.485 1.00 29.02 ? 511 PHE A CA 1 ATOM 4057 C C . PHE A 1 511 ? 36.613 49.831 12.775 1.00 29.67 ? 511 PHE A C 1 ATOM 4058 O O . PHE A 1 511 ? 35.419 49.513 12.773 1.00 27.91 ? 511 PHE A O 1 ATOM 4059 C CB . PHE A 1 511 ? 37.550 51.669 11.383 1.00 27.68 ? 511 PHE A CB 1 ATOM 4060 C CG . PHE A 1 511 ? 36.316 52.467 11.715 1.00 27.55 ? 511 PHE A CG 1 ATOM 4061 C CD1 . PHE A 1 511 ? 36.207 53.129 12.934 1.00 27.62 ? 511 PHE A CD1 1 ATOM 4062 C CD2 . PHE A 1 511 ? 35.239 52.507 10.835 1.00 27.35 ? 511 PHE A CD2 1 ATOM 4063 C CE1 . PHE A 1 511 ? 35.038 53.820 13.277 1.00 27.49 ? 511 PHE A CE1 1 ATOM 4064 C CE2 . PHE A 1 511 ? 34.068 53.192 11.167 1.00 27.54 ? 511 PHE A CE2 1 ATOM 4065 C CZ . PHE A 1 511 ? 33.968 53.849 12.394 1.00 27.08 ? 511 PHE A CZ 1 ATOM 4066 N N . ASN A 1 512 ? 37.353 49.915 13.875 1.00 29.91 ? 512 ASN A N 1 ATOM 4067 C CA . ASN A 1 512 ? 36.809 49.691 15.203 1.00 30.19 ? 512 ASN A CA 1 ATOM 4068 C C . ASN A 1 512 ? 37.510 50.657 16.145 1.00 31.23 ? 512 ASN A C 1 ATOM 4069 O O . ASN A 1 512 ? 38.675 50.454 16.494 1.00 31.34 ? 512 ASN A O 1 ATOM 4070 C CB . ASN A 1 512 ? 37.047 48.255 15.657 1.00 28.64 ? 512 ASN A CB 1 ATOM 4071 C CG . ASN A 1 512 ? 36.679 48.046 17.110 1.00 30.18 ? 512 ASN A CG 1 ATOM 4072 O OD1 . ASN A 1 512 ? 35.842 48.768 17.658 1.00 28.56 ? 512 ASN A OD1 1 ATOM 4073 N ND2 . ASN A 1 512 ? 37.294 47.051 17.744 1.00 30.32 ? 512 ASN A ND2 1 ATOM 4074 N N . ASN A 1 513 ? 36.812 51.722 16.535 1.00 32.01 ? 513 ASN A N 1 ATOM 4075 C CA . ASN A 1 513 ? 37.398 52.710 17.434 1.00 32.11 ? 513 ASN A CA 1 ATOM 4076 C C . ASN A 1 513 ? 36.918 52.515 18.860 1.00 31.24 ? 513 ASN A C 1 ATOM 4077 O O . ASN A 1 513 ? 37.098 53.389 19.706 1.00 31.13 ? 513 ASN A O 1 ATOM 4078 C CB . ASN A 1 513 ? 37.076 54.137 16.981 1.00 33.10 ? 513 ASN A CB 1 ATOM 4079 C CG . ASN A 1 513 ? 38.322 54.991 16.832 1.00 34.15 ? 513 ASN A CG 1 ATOM 4080 O OD1 . ASN A 1 513 ? 39.350 54.690 17.429 1.00 35.63 ? 513 ASN A OD1 1 ATOM 4081 N ND2 . ASN A 1 513 ? 38.227 56.041 16.018 1.00 38.61 ? 513 ASN A ND2 1 ATOM 4082 N N . GLY A 1 514 ? 36.300 51.370 19.124 1.00 30.58 ? 514 GLY A N 1 ATOM 4083 C CA . GLY A 1 514 ? 35.841 51.087 20.469 1.00 31.46 ? 514 GLY A CA 1 ATOM 4084 C C . GLY A 1 514 ? 37.008 50.549 21.282 1.00 32.14 ? 514 GLY A C 1 ATOM 4085 O O . GLY A 1 514 ? 38.108 50.383 20.754 1.00 32.15 ? 514 GLY A O 1 ATOM 4086 N N . THR A 1 515 ? 36.790 50.284 22.564 1.00 32.77 ? 515 THR A N 1 ATOM 4087 C CA . THR A 1 515 ? 37.857 49.745 23.401 1.00 33.86 ? 515 THR A CA 1 ATOM 4088 C C . THR A 1 515 ? 37.721 48.226 23.462 1.00 34.45 ? 515 THR A C 1 ATOM 4089 O O . THR A 1 515 ? 38.623 47.526 23.913 1.00 34.84 ? 515 THR A O 1 ATOM 4090 C CB . THR A 1 515 ? 37.816 50.335 24.828 1.00 32.79 ? 515 THR A CB 1 ATOM 4091 O OG1 . THR A 1 515 ? 36.534 50.084 25.421 1.00 33.48 ? 515 THR A OG1 1 ATOM 4092 C CG2 . THR A 1 515 ? 38.076 51.833 24.781 1.00 29.85 ? 515 THR A CG2 1 ATOM 4093 N N . GLN A 1 516 ? 36.576 47.727 23.009 1.00 35.09 ? 516 GLN A N 1 ATOM 4094 C CA . GLN A 1 516 ? 36.328 46.293 22.975 1.00 36.27 ? 516 GLN A CA 1 ATOM 4095 C C . GLN A 1 516 ? 36.612 45.785 21.572 1.00 37.11 ? 516 GLN A C 1 ATOM 4096 O O . GLN A 1 516 ? 36.473 46.506 20.584 1.00 36.04 ? 516 GLN A O 1 ATOM 4097 C CB . GLN A 1 516 ? 34.875 45.975 23.323 1.00 37.81 ? 516 GLN A CB 1 ATOM 4098 C CG . GLN A 1 516 ? 34.515 46.212 24.766 1.00 42.46 ? 516 GLN A CG 1 ATOM 4099 C CD . GLN A 1 516 ? 35.166 45.210 25.686 1.00 44.66 ? 516 GLN A CD 1 ATOM 4100 O OE1 . GLN A 1 516 ? 34.875 44.012 25.622 1.00 46.08 ? 516 GLN A OE1 1 ATOM 4101 N NE2 . GLN A 1 516 ? 36.058 45.690 26.548 1.00 44.37 ? 516 GLN A NE2 1 ATOM 4102 N N . ASN A 1 517 ? 36.998 44.523 21.503 1.00 38.10 ? 517 ASN A N 1 ATOM 4103 C CA . ASN A 1 517 ? 37.314 43.863 20.252 1.00 38.25 ? 517 ASN A CA 1 ATOM 4104 C C . ASN A 1 517 ? 36.022 43.449 19.545 1.00 36.65 ? 517 ASN A C 1 ATOM 4105 O O . ASN A 1 517 ? 35.034 43.115 20.201 1.00 36.55 ? 517 ASN A O 1 ATOM 4106 C CB . ASN A 1 517 ? 38.143 42.618 20.570 1.00 41.27 ? 517 ASN A CB 1 ATOM 4107 C CG . ASN A 1 517 ? 39.161 42.310 19.514 1.00 45.57 ? 517 ASN A CG 1 ATOM 4108 O OD1 . ASN A 1 517 ? 38.831 41.805 18.432 1.00 48.36 ? 517 ASN A OD1 1 ATOM 4109 N ND2 . ASN A 1 517 ? 40.422 42.615 19.815 1.00 46.42 ? 517 ASN A ND2 1 ATOM 4110 N N . VAL A 1 518 ? 36.024 43.498 18.215 1.00 35.30 ? 518 VAL A N 1 ATOM 4111 C CA . VAL A 1 518 ? 34.873 43.053 17.421 1.00 34.53 ? 518 VAL A CA 1 ATOM 4112 C C . VAL A 1 518 ? 35.429 42.228 16.270 1.00 33.56 ? 518 VAL A C 1 ATOM 4113 O O . VAL A 1 518 ? 36.555 42.449 15.824 1.00 33.82 ? 518 VAL A O 1 ATOM 4114 C CB . VAL A 1 518 ? 34.026 44.218 16.824 1.00 34.31 ? 518 VAL A CB 1 ATOM 4115 C CG1 . VAL A 1 518 ? 33.442 45.062 17.936 1.00 36.26 ? 518 VAL A CG1 1 ATOM 4116 C CG2 . VAL A 1 518 ? 34.867 45.058 15.882 1.00 33.83 ? 518 VAL A CG2 1 ATOM 4117 N N . LYS A 1 519 ? 34.646 41.273 15.790 1.00 32.25 ? 519 LYS A N 1 ATOM 4118 C CA . LYS A 1 519 ? 35.104 40.434 14.701 1.00 32.21 ? 519 LYS A CA 1 ATOM 4119 C C . LYS A 1 519 ? 34.237 40.530 13.455 1.00 31.17 ? 519 LYS A C 1 ATOM 4120 O O . LYS A 1 519 ? 33.010 40.612 13.535 1.00 31.17 ? 519 LYS A O 1 ATOM 4121 C CB . LYS A 1 519 ? 35.169 38.969 15.156 1.00 33.33 ? 519 LYS A CB 1 ATOM 4122 C CG . LYS A 1 519 ? 35.383 37.974 14.011 1.00 37.51 ? 519 LYS A CG 1 ATOM 4123 C CD . LYS A 1 519 ? 35.479 36.529 14.490 1.00 39.06 ? 519 LYS A CD 1 ATOM 4124 C CE . LYS A 1 519 ? 36.781 36.276 15.230 1.00 41.23 ? 519 LYS A CE 1 ATOM 4125 N NZ . LYS A 1 519 ? 36.907 34.842 15.621 1.00 44.83 ? 519 LYS A NZ 1 ATOM 4126 N N . ILE A 1 520 ? 34.891 40.532 12.301 1.00 29.98 ? 520 ILE A N 1 ATOM 4127 C CA . ILE A 1 520 ? 34.185 40.545 11.035 1.00 29.13 ? 520 ILE A CA 1 ATOM 4128 C C . ILE A 1 520 ? 33.998 39.067 10.745 1.00 29.43 ? 520 ILE A C 1 ATOM 4129 O O . ILE A 1 520 ? 34.959 38.388 10.403 1.00 30.58 ? 520 ILE A O 1 ATOM 4130 C CB . ILE A 1 520 ? 35.040 41.139 9.907 1.00 28.82 ? 520 ILE A CB 1 ATOM 4131 C CG1 . ILE A 1 520 ? 35.380 42.595 10.216 1.00 30.46 ? 520 ILE A CG1 1 ATOM 4132 C CG2 . ILE A 1 520 ? 34.288 41.050 8.589 1.00 27.50 ? 520 ILE A CG2 1 ATOM 4133 C CD1 . ILE A 1 520 ? 36.316 43.219 9.210 1.00 31.11 ? 520 ILE A CD1 1 ATOM 4134 N N . SER A 1 521 ? 32.787 38.547 10.912 1.00 29.50 ? 521 SER A N 1 ATOM 4135 C CA . SER A 1 521 ? 32.580 37.137 10.628 1.00 30.50 ? 521 SER A CA 1 ATOM 4136 C C . SER A 1 521 ? 32.680 36.997 9.114 1.00 32.36 ? 521 SER A C 1 ATOM 4137 O O . SER A 1 521 ? 33.258 36.040 8.600 1.00 33.45 ? 521 SER A O 1 ATOM 4138 C CB . SER A 1 521 ? 31.213 36.664 11.129 1.00 28.61 ? 521 SER A CB 1 ATOM 4139 O OG . SER A 1 521 ? 30.166 37.216 10.362 1.00 31.71 ? 521 SER A OG 1 ATOM 4140 N N . GLU A 1 522 ? 32.130 37.971 8.398 1.00 32.71 ? 522 GLU A N 1 ATOM 4141 C CA . GLU A 1 522 ? 32.191 37.947 6.948 1.00 34.17 ? 522 GLU A CA 1 ATOM 4142 C C . GLU A 1 522 ? 31.939 39.306 6.327 1.00 33.08 ? 522 GLU A C 1 ATOM 4143 O O . GLU A 1 522 ? 31.119 40.086 6.810 1.00 31.34 ? 522 GLU A O 1 ATOM 4144 C CB . GLU A 1 522 ? 31.196 36.938 6.372 1.00 37.81 ? 522 GLU A CB 1 ATOM 4145 C CG . GLU A 1 522 ? 31.104 37.001 4.848 1.00 45.30 ? 522 GLU A CG 1 ATOM 4146 C CD . GLU A 1 522 ? 30.525 35.740 4.226 1.00 49.69 ? 522 GLU A CD 1 ATOM 4147 O OE1 . GLU A 1 522 ? 29.491 35.241 4.728 1.00 51.31 ? 522 GLU A OE1 1 ATOM 4148 O OE2 . GLU A 1 522 ? 31.104 35.255 3.226 1.00 51.10 ? 522 GLU A OE2 1 ATOM 4149 N N . MET A 1 523 ? 32.662 39.578 5.248 1.00 32.22 ? 523 MET A N 1 ATOM 4150 C CA . MET A 1 523 ? 32.528 40.831 4.530 1.00 32.16 ? 523 MET A CA 1 ATOM 4151 C C . MET A 1 523 ? 32.621 40.582 3.024 1.00 31.95 ? 523 MET A C 1 ATOM 4152 O O . MET A 1 523 ? 33.509 39.864 2.567 1.00 32.15 ? 523 MET A O 1 ATOM 4153 C CB . MET A 1 523 ? 33.629 41.792 4.955 1.00 32.19 ? 523 MET A CB 1 ATOM 4154 C CG . MET A 1 523 ? 33.322 43.219 4.596 1.00 38.86 ? 523 MET A CG 1 ATOM 4155 S SD . MET A 1 523 ? 34.569 43.979 3.570 1.00 47.02 ? 523 MET A SD 1 ATOM 4156 C CE . MET A 1 523 ? 34.252 43.177 2.029 1.00 39.50 ? 523 MET A CE 1 ATOM 4157 N N . SER A 1 524 ? 31.696 41.154 2.259 1.00 30.78 ? 524 SER A N 1 ATOM 4158 C CA . SER A 1 524 ? 31.708 41.009 0.805 1.00 29.81 ? 524 SER A CA 1 ATOM 4159 C C . SER A 1 524 ? 31.639 42.379 0.161 1.00 29.52 ? 524 SER A C 1 ATOM 4160 O O . SER A 1 524 ? 30.753 43.181 0.471 1.00 28.45 ? 524 SER A O 1 ATOM 4161 C CB . SER A 1 524 ? 30.522 40.183 0.311 1.00 30.92 ? 524 SER A CB 1 ATOM 4162 O OG . SER A 1 524 ? 30.545 38.882 0.857 1.00 35.81 ? 524 SER A OG 1 ATOM 4163 N N . ALA A 1 525 ? 32.582 42.641 -0.736 1.00 27.70 ? 525 ALA A N 1 ATOM 4164 C CA . ALA A 1 525 ? 32.636 43.906 -1.445 1.00 26.55 ? 525 ALA A CA 1 ATOM 4165 C C . ALA A 1 525 ? 32.707 43.627 -2.940 1.00 27.13 ? 525 ALA A C 1 ATOM 4166 O O . ALA A 1 525 ? 33.437 42.743 -3.383 1.00 26.99 ? 525 ALA A O 1 ATOM 4167 C CB . ALA A 1 525 ? 33.853 44.705 -1.002 1.00 23.83 ? 525 ALA A CB 1 ATOM 4168 N N . TRP A 1 526 ? 31.939 44.382 -3.714 1.00 27.62 ? 526 TRP A N 1 ATOM 4169 C CA . TRP A 1 526 ? 31.927 44.226 -5.160 1.00 27.14 ? 526 TRP A CA 1 ATOM 4170 C C . TRP A 1 526 ? 32.107 45.580 -5.805 1.00 27.92 ? 526 TRP A C 1 ATOM 4171 O O . TRP A 1 526 ? 31.537 46.571 -5.343 1.00 28.92 ? 526 TRP A O 1 ATOM 4172 C CB . TRP A 1 526 ? 30.585 43.680 -5.644 1.00 27.19 ? 526 TRP A CB 1 ATOM 4173 C CG . TRP A 1 526 ? 30.340 42.232 -5.409 1.00 28.43 ? 526 TRP A CG 1 ATOM 4174 C CD1 . TRP A 1 526 ? 30.731 41.192 -6.204 1.00 28.79 ? 526 TRP A CD1 1 ATOM 4175 C CD2 . TRP A 1 526 ? 29.595 41.660 -4.331 1.00 28.99 ? 526 TRP A CD2 1 ATOM 4176 N NE1 . TRP A 1 526 ? 30.268 40.004 -5.686 1.00 30.37 ? 526 TRP A NE1 1 ATOM 4177 C CE2 . TRP A 1 526 ? 29.568 40.265 -4.536 1.00 28.65 ? 526 TRP A CE2 1 ATOM 4178 C CE3 . TRP A 1 526 ? 28.946 42.193 -3.210 1.00 31.05 ? 526 TRP A CE3 1 ATOM 4179 C CZ2 . TRP A 1 526 ? 28.915 39.393 -3.661 1.00 31.19 ? 526 TRP A CZ2 1 ATOM 4180 C CZ3 . TRP A 1 526 ? 28.295 41.322 -2.336 1.00 32.93 ? 526 TRP A CZ3 1 ATOM 4181 C CH2 . TRP A 1 526 ? 28.286 39.938 -2.570 1.00 32.36 ? 526 TRP A CH2 1 ATOM 4182 N N . SER A 1 527 ? 32.910 45.629 -6.860 1.00 27.08 ? 527 SER A N 1 ATOM 4183 C CA . SER A 1 527 ? 33.074 46.860 -7.609 1.00 27.06 ? 527 SER A CA 1 ATOM 4184 C C . SER A 1 527 ? 31.789 46.857 -8.438 1.00 26.83 ? 527 SER A C 1 ATOM 4185 O O . SER A 1 527 ? 31.339 45.799 -8.878 1.00 25.87 ? 527 SER A O 1 ATOM 4186 C CB . SER A 1 527 ? 34.285 46.778 -8.536 1.00 28.17 ? 527 SER A CB 1 ATOM 4187 O OG . SER A 1 527 ? 35.489 46.681 -7.800 1.00 32.56 ? 527 SER A OG 1 ATOM 4188 N N . MET A 1 528 ? 31.186 48.019 -8.635 1.00 26.76 ? 528 MET A N 1 ATOM 4189 C CA . MET A 1 528 ? 29.945 48.095 -9.398 1.00 27.09 ? 528 MET A CA 1 ATOM 4190 C C . MET A 1 528 ? 30.171 48.813 -10.717 1.00 27.55 ? 528 MET A C 1 ATOM 4191 O O . MET A 1 528 ? 30.705 49.923 -10.743 1.00 28.03 ? 528 MET A O 1 ATOM 4192 C CB . MET A 1 528 ? 28.887 48.843 -8.589 1.00 27.16 ? 528 MET A CB 1 ATOM 4193 C CG . MET A 1 528 ? 28.548 48.196 -7.259 1.00 28.22 ? 528 MET A CG 1 ATOM 4194 S SD . MET A 1 528 ? 27.650 46.667 -7.491 1.00 31.69 ? 528 MET A SD 1 ATOM 4195 C CE . MET A 1 528 ? 25.958 47.275 -7.495 1.00 32.05 ? 528 MET A CE 1 ATOM 4196 N N . LYS A 1 529 ? 29.772 48.192 -11.819 1.00 27.18 ? 529 LYS A N 1 ATOM 4197 C CA . LYS A 1 529 ? 29.956 48.847 -13.099 1.00 27.92 ? 529 LYS A CA 1 ATOM 4198 C C . LYS A 1 529 ? 28.837 49.867 -13.273 1.00 28.42 ? 529 LYS A C 1 ATOM 4199 O O . LYS A 1 529 ? 27.840 49.830 -12.556 1.00 27.63 ? 529 LYS A O 1 ATOM 4200 C CB . LYS A 1 529 ? 29.935 47.830 -14.241 1.00 29.18 ? 529 LYS A CB 1 ATOM 4201 C CG . LYS A 1 529 ? 28.588 47.210 -14.518 1.00 32.24 ? 529 LYS A CG 1 ATOM 4202 C CD . LYS A 1 529 ? 28.673 46.284 -15.723 1.00 35.04 ? 529 LYS A CD 1 ATOM 4203 C CE . LYS A 1 529 ? 27.356 45.558 -15.960 1.00 39.13 ? 529 LYS A CE 1 ATOM 4204 N NZ . LYS A 1 529 ? 27.418 44.655 -17.149 1.00 42.20 ? 529 LYS A NZ 1 ATOM 4205 N N . ASN A 1 530 ? 29.014 50.781 -14.219 1.00 27.55 ? 530 ASN A N 1 ATOM 4206 C CA . ASN A 1 530 ? 28.024 51.811 -14.481 1.00 28.25 ? 530 ASN A CA 1 ATOM 4207 C C . ASN A 1 530 ? 26.718 51.239 -15.016 1.00 29.10 ? 530 ASN A C 1 ATOM 4208 O O . ASN A 1 530 ? 26.702 50.211 -15.700 1.00 28.87 ? 530 ASN A O 1 ATOM 4209 C CB . ASN A 1 530 ? 28.553 52.804 -15.522 1.00 28.59 ? 530 ASN A CB 1 ATOM 4210 C CG . ASN A 1 530 ? 29.726 53.625 -15.021 1.00 29.86 ? 530 ASN A CG 1 ATOM 4211 O OD1 . ASN A 1 530 ? 30.463 54.198 -15.813 1.00 32.93 ? 530 ASN A OD1 1 ATOM 4212 N ND2 . ASN A 1 530 ? 29.894 53.700 -13.712 1.00 32.13 ? 530 ASN A ND2 1 ATOM 4213 N N . ALA A 1 531 ? 25.619 51.907 -14.689 1.00 28.23 ? 531 ALA A N 1 ATOM 4214 C CA . ALA A 1 531 ? 24.326 51.520 -15.221 1.00 28.05 ? 531 ALA A CA 1 ATOM 4215 C C . ALA A 1 531 ? 24.343 52.258 -16.568 1.00 28.55 ? 531 ALA A C 1 ATOM 4216 O O . ALA A 1 531 ? 25.075 53.236 -16.726 1.00 26.72 ? 531 ALA A O 1 ATOM 4217 C CB . ALA A 1 531 ? 23.205 52.051 -14.334 1.00 25.86 ? 531 ALA A CB 1 ATOM 4218 N N . LYS A 1 532 ? 23.576 51.796 -17.545 1.00 30.21 ? 532 LYS A N 1 ATOM 4219 C CA . LYS A 1 532 ? 23.562 52.479 -18.832 1.00 32.02 ? 532 LYS A CA 1 ATOM 4220 C C . LYS A 1 532 ? 22.428 53.490 -18.904 1.00 31.91 ? 532 LYS A C 1 ATOM 4221 O O . LYS A 1 532 ? 21.301 53.210 -18.493 1.00 32.80 ? 532 LYS A O 1 ATOM 4222 C CB . LYS A 1 532 ? 23.424 51.473 -19.976 1.00 34.12 ? 532 LYS A CB 1 ATOM 4223 C CG . LYS A 1 532 ? 24.608 50.531 -20.099 1.00 41.58 ? 532 LYS A CG 1 ATOM 4224 C CD . LYS A 1 532 ? 24.384 49.475 -21.177 1.00 47.97 ? 532 LYS A CD 1 ATOM 4225 C CE . LYS A 1 532 ? 25.536 48.474 -21.226 1.00 50.87 ? 532 LYS A CE 1 ATOM 4226 N NZ . LYS A 1 532 ? 25.719 47.752 -19.926 1.00 55.05 ? 532 LYS A NZ 1 ATOM 4227 N N . PHE A 1 533 ? 22.744 54.674 -19.410 1.00 31.61 ? 533 PHE A N 1 ATOM 4228 C CA . PHE A 1 533 ? 21.763 55.737 -19.576 1.00 32.51 ? 533 PHE A CA 1 ATOM 4229 C C . PHE A 1 533 ? 21.833 56.211 -21.016 1.00 33.96 ? 533 PHE A C 1 ATOM 4230 O O . PHE A 1 533 ? 22.788 56.877 -21.422 1.00 35.03 ? 533 PHE A O 1 ATOM 4231 C CB . PHE A 1 533 ? 22.055 56.897 -18.626 1.00 30.07 ? 533 PHE A CB 1 ATOM 4232 C CG . PHE A 1 533 ? 21.751 56.586 -17.195 1.00 30.81 ? 533 PHE A CG 1 ATOM 4233 C CD1 . PHE A 1 533 ? 20.461 56.728 -16.700 1.00 28.54 ? 533 PHE A CD1 1 ATOM 4234 C CD2 . PHE A 1 533 ? 22.747 56.103 -16.350 1.00 29.94 ? 533 PHE A CD2 1 ATOM 4235 C CE1 . PHE A 1 533 ? 20.164 56.392 -15.385 1.00 28.80 ? 533 PHE A CE1 1 ATOM 4236 C CE2 . PHE A 1 533 ? 22.459 55.760 -15.029 1.00 29.43 ? 533 PHE A CE2 1 ATOM 4237 C CZ . PHE A 1 533 ? 21.166 55.904 -14.547 1.00 28.93 ? 533 PHE A CZ 1 ATOM 4238 N N . VAL A 1 534 ? 20.819 55.838 -21.787 1.00 33.89 ? 534 VAL A N 1 ATOM 4239 C CA . VAL A 1 534 ? 20.732 56.203 -23.187 1.00 34.23 ? 534 VAL A CA 1 ATOM 4240 C C . VAL A 1 534 ? 19.724 57.329 -23.368 1.00 35.28 ? 534 VAL A C 1 ATOM 4241 O O . VAL A 1 534 ? 18.675 57.352 -22.723 1.00 34.91 ? 534 VAL A O 1 ATOM 4242 C CB . VAL A 1 534 ? 20.287 54.996 -24.031 1.00 34.89 ? 534 VAL A CB 1 ATOM 4243 C CG1 . VAL A 1 534 ? 20.071 55.414 -25.473 1.00 34.99 ? 534 VAL A CG1 1 ATOM 4244 C CG2 . VAL A 1 534 ? 21.335 53.899 -23.949 1.00 35.56 ? 534 VAL A CG2 1 ATOM 4245 N N . VAL A 1 535 ? 20.041 58.268 -24.245 1.00 36.68 ? 535 VAL A N 1 ATOM 4246 C CA . VAL A 1 535 ? 19.135 59.371 -24.504 1.00 38.97 ? 535 VAL A CA 1 ATOM 4247 C C . VAL A 1 535 ? 18.397 59.156 -25.820 1.00 41.44 ? 535 VAL A C 1 ATOM 4248 O O . VAL A 1 535 ? 19.011 58.920 -26.859 1.00 42.60 ? 535 VAL A O 1 ATOM 4249 C CB . VAL A 1 535 ? 19.885 60.704 -24.570 1.00 37.74 ? 535 VAL A CB 1 ATOM 4250 C CG1 . VAL A 1 535 ? 18.925 61.819 -24.948 1.00 36.96 ? 535 VAL A CG1 1 ATOM 4251 C CG2 . VAL A 1 535 ? 20.532 60.990 -23.228 1.00 37.53 ? 535 VAL A CG2 1 ATOM 4252 N N . ASP A 1 536 ? 17.074 59.224 -25.760 1.00 43.53 ? 536 ASP A N 1 ATOM 4253 C CA . ASP A 1 536 ? 16.231 59.062 -26.937 1.00 46.89 ? 536 ASP A CA 1 ATOM 4254 C C . ASP A 1 536 ? 15.218 60.206 -26.899 1.00 49.30 ? 536 ASP A C 1 ATOM 4255 O O . ASP A 1 536 ? 14.017 59.988 -26.726 1.00 48.95 ? 536 ASP A O 1 ATOM 4256 C CB . ASP A 1 536 ? 15.518 57.714 -26.878 1.00 47.73 ? 536 ASP A CB 1 ATOM 4257 C CG . ASP A 1 536 ? 14.664 57.451 -28.101 1.00 51.11 ? 536 ASP A CG 1 ATOM 4258 O OD1 . ASP A 1 536 ? 14.042 56.369 -28.164 1.00 51.02 ? 536 ASP A OD1 1 ATOM 4259 O OD2 . ASP A 1 536 ? 14.616 58.323 -28.997 1.00 54.44 ? 536 ASP A OD2 1 ATOM 4260 N N . GLN A 1 537 ? 15.720 61.429 -27.058 1.00 52.27 ? 537 GLN A N 1 ATOM 4261 C CA . GLN A 1 537 ? 14.887 62.627 -27.001 1.00 55.91 ? 537 GLN A CA 1 ATOM 4262 C C . GLN A 1 537 ? 14.769 63.419 -28.303 1.00 58.72 ? 537 GLN A C 1 ATOM 4263 O O . GLN A 1 537 ? 14.985 62.891 -29.395 1.00 59.07 ? 537 GLN A O 1 ATOM 4264 C CB . GLN A 1 537 ? 15.417 63.553 -25.905 1.00 54.70 ? 537 GLN A CB 1 ATOM 4265 C CG . GLN A 1 537 ? 15.227 63.028 -24.497 1.00 55.38 ? 537 GLN A CG 1 ATOM 4266 C CD . GLN A 1 537 ? 15.981 63.847 -23.472 1.00 55.97 ? 537 GLN A CD 1 ATOM 4267 O OE1 . GLN A 1 537 ? 15.678 63.805 -22.280 1.00 57.21 ? 537 GLN A OE1 1 ATOM 4268 N NE2 . GLN A 1 537 ? 16.980 64.593 -23.932 1.00 56.02 ? 537 GLN A NE2 1 ATOM 4269 N N . SER A 1 538 ? 14.416 64.697 -28.153 1.00 62.16 ? 538 SER A N 1 ATOM 4270 C CA . SER A 1 538 ? 14.251 65.639 -29.260 1.00 63.23 ? 538 SER A CA 1 ATOM 4271 C C . SER A 1 538 ? 13.302 65.110 -30.328 1.00 63.44 ? 538 SER A C 1 ATOM 4272 O O . SER A 1 538 ? 12.107 64.941 -30.079 1.00 62.94 ? 538 SER A O 1 ATOM 4273 C CB . SER A 1 538 ? 15.614 65.964 -29.881 1.00 64.38 ? 538 SER A CB 1 ATOM 4274 O OG . SER A 1 538 ? 15.500 66.964 -30.879 1.00 67.06 ? 538 SER A OG 1 HETATM 4275 C C1 . NDG B 2 . ? 38.738 57.363 16.361 1.00 39.04 ? 650 NDG A C1 1 HETATM 4276 C C2 . NDG B 2 . ? 39.108 58.084 15.058 1.00 40.16 ? 650 NDG A C2 1 HETATM 4277 C C3 . NDG B 2 . ? 40.353 58.960 15.197 1.00 41.43 ? 650 NDG A C3 1 HETATM 4278 C C4 . NDG B 2 . ? 40.341 59.652 16.565 1.00 44.77 ? 650 NDG A C4 1 HETATM 4279 C C5 . NDG B 2 . ? 40.365 58.590 17.681 1.00 42.44 ? 650 NDG A C5 1 HETATM 4280 C C6 . NDG B 2 . ? 39.564 58.978 18.897 1.00 43.80 ? 650 NDG A C6 1 HETATM 4281 C C7 . NDG B 2 . ? 38.516 57.130 12.941 1.00 36.83 ? 650 NDG A C7 1 HETATM 4282 C C8 . NDG B 2 . ? 38.712 56.033 11.908 1.00 32.71 ? 650 NDG A C8 1 HETATM 4283 O O . NDG B 2 . ? 39.874 57.292 17.229 1.00 40.90 ? 650 NDG A O 1 HETATM 4284 O O3 . NDG B 2 . ? 40.350 59.924 14.155 1.00 40.71 ? 650 NDG A O3 1 HETATM 4285 O O4 . NDG B 2 . ? 41.487 60.527 16.725 1.00 52.64 ? 650 NDG A O4 1 HETATM 4286 O O6 . NDG B 2 . ? 39.674 60.368 19.154 1.00 41.18 ? 650 NDG A O6 1 HETATM 4287 O O7 . NDG B 2 . ? 37.644 57.985 12.776 1.00 35.29 ? 650 NDG A O7 1 HETATM 4288 N N2 . NDG B 2 . ? 39.314 57.117 14.002 1.00 37.67 ? 650 NDG A N2 1 HETATM 4289 C C1 . NAG C 3 . ? 41.669 61.626 15.881 1.00 60.94 ? 660 NAG A C1 1 HETATM 4290 C C2 . NAG C 3 . ? 40.706 62.782 16.207 1.00 65.61 ? 660 NAG A C2 1 HETATM 4291 C C3 . NAG C 3 . ? 41.047 63.412 17.552 1.00 70.20 ? 660 NAG A C3 1 HETATM 4292 C C4 . NAG C 3 . ? 42.505 63.874 17.563 1.00 70.37 ? 660 NAG A C4 1 HETATM 4293 C C5 . NAG C 3 . ? 43.443 62.713 17.208 1.00 65.41 ? 660 NAG A C5 1 HETATM 4294 C C6 . NAG C 3 . ? 43.534 61.658 18.299 1.00 61.37 ? 660 NAG A C6 1 HETATM 4295 C C7 . NAG C 3 . ? 39.861 63.963 14.283 1.00 67.49 ? 660 NAG A C7 1 HETATM 4296 C C8 . NAG C 3 . ? 38.526 64.517 14.758 1.00 67.57 ? 660 NAG A C8 1 HETATM 4297 N N2 . NAG C 3 . ? 40.815 63.810 15.191 1.00 66.64 ? 660 NAG A N2 1 HETATM 4298 O O3 . NAG C 3 . ? 40.835 62.474 18.597 1.00 74.65 ? 660 NAG A O3 1 HETATM 4299 O O4 . NAG C 3 . ? 42.702 64.992 16.663 1.00 75.80 ? 660 NAG A O4 1 HETATM 4300 O O5 . NAG C 3 . ? 43.050 62.059 15.958 1.00 65.37 ? 660 NAG A O5 1 HETATM 4301 O O6 . NAG C 3 . ? 44.567 60.726 18.032 1.00 57.20 ? 660 NAG A O6 1 HETATM 4302 O O7 . NAG C 3 . ? 40.027 63.694 13.094 1.00 68.54 ? 660 NAG A O7 1 HETATM 4303 C C1 . MAN D 4 . ? 42.666 66.242 17.278 1.00 81.79 ? 670 MAN A C1 1 HETATM 4304 C C2 . MAN D 4 . ? 41.280 66.906 17.138 1.00 83.07 ? 670 MAN A C2 1 HETATM 4305 C C3 . MAN D 4 . ? 41.050 67.452 15.726 1.00 83.69 ? 670 MAN A C3 1 HETATM 4306 C C4 . MAN D 4 . ? 42.215 68.349 15.330 1.00 84.41 ? 670 MAN A C4 1 HETATM 4307 C C5 . MAN D 4 . ? 43.510 67.539 15.410 1.00 85.07 ? 670 MAN A C5 1 HETATM 4308 C C6 . MAN D 4 . ? 44.727 68.358 15.018 1.00 85.84 ? 670 MAN A C6 1 HETATM 4309 O O2 . MAN D 4 . ? 41.168 67.968 18.076 1.00 83.24 ? 670 MAN A O2 1 HETATM 4310 O O3 . MAN D 4 . ? 39.843 68.202 15.694 1.00 83.38 ? 670 MAN A O3 1 HETATM 4311 O O4 . MAN D 4 . ? 42.023 68.839 14.010 1.00 84.76 ? 670 MAN A O4 1 HETATM 4312 O O5 . MAN D 4 . ? 43.726 67.079 16.766 1.00 83.78 ? 670 MAN A O5 1 HETATM 4313 O O6 . MAN D 4 . ? 44.772 68.574 13.615 1.00 86.10 ? 670 MAN A O6 1 HETATM 4314 C C1 . NAG E 3 . ? 2.259 55.350 -31.792 1.00 36.71 ? 680 NAG A C1 1 HETATM 4315 C C2 . NAG E 3 . ? 2.802 56.282 -32.885 1.00 38.35 ? 680 NAG A C2 1 HETATM 4316 C C3 . NAG E 3 . ? 3.421 55.464 -34.025 1.00 39.67 ? 680 NAG A C3 1 HETATM 4317 C C4 . NAG E 3 . ? 4.440 54.450 -33.485 1.00 42.12 ? 680 NAG A C4 1 HETATM 4318 C C5 . NAG E 3 . ? 3.792 53.609 -32.380 1.00 40.52 ? 680 NAG A C5 1 HETATM 4319 C C6 . NAG E 3 . ? 4.772 52.654 -31.734 1.00 40.86 ? 680 NAG A C6 1 HETATM 4320 C C7 . NAG E 3 . ? 1.803 58.433 -33.362 1.00 36.99 ? 680 NAG A C7 1 HETATM 4321 C C8 . NAG E 3 . ? 0.512 59.203 -33.598 1.00 36.32 ? 680 NAG A C8 1 HETATM 4322 N N2 . NAG E 3 . ? 1.729 57.106 -33.410 1.00 37.11 ? 680 NAG A N2 1 HETATM 4323 O O3 . NAG E 3 . ? 4.056 56.341 -34.941 1.00 38.62 ? 680 NAG A O3 1 HETATM 4324 O O4 . NAG E 3 . ? 4.886 53.585 -34.554 1.00 47.52 ? 680 NAG A O4 1 HETATM 4325 O O5 . NAG E 3 . ? 3.291 54.468 -31.336 1.00 38.18 ? 680 NAG A O5 1 HETATM 4326 O O6 . NAG E 3 . ? 5.954 53.333 -31.337 1.00 39.92 ? 680 NAG A O6 1 HETATM 4327 O O7 . NAG E 3 . ? 2.848 59.044 -33.140 1.00 36.50 ? 680 NAG A O7 1 HETATM 4328 C C1 . NAG F 3 . ? 6.242 53.599 -34.854 1.00 53.34 ? 690 NAG A C1 1 HETATM 4329 C C2 . NAG F 3 . ? 6.572 52.449 -35.822 1.00 54.80 ? 690 NAG A C2 1 HETATM 4330 C C3 . NAG F 3 . ? 8.023 52.542 -36.296 1.00 57.45 ? 690 NAG A C3 1 HETATM 4331 C C4 . NAG F 3 . ? 8.317 53.929 -36.863 1.00 59.19 ? 690 NAG A C4 1 HETATM 4332 C C5 . NAG F 3 . ? 7.931 55.002 -35.836 1.00 60.00 ? 690 NAG A C5 1 HETATM 4333 C C6 . NAG F 3 . ? 8.095 56.402 -36.394 1.00 61.67 ? 690 NAG A C6 1 HETATM 4334 C C7 . NAG F 3 . ? 5.148 50.647 -35.105 1.00 54.54 ? 690 NAG A C7 1 HETATM 4335 C C8 . NAG F 3 . ? 4.867 49.704 -33.947 1.00 54.39 ? 690 NAG A C8 1 HETATM 4336 N N2 . NAG F 3 . ? 6.367 51.168 -35.177 1.00 53.64 ? 690 NAG A N2 1 HETATM 4337 O O3 . NAG F 3 . ? 8.259 51.561 -37.295 1.00 59.53 ? 690 NAG A O3 1 HETATM 4338 O O4 . NAG F 3 . ? 9.700 54.033 -37.180 1.00 61.16 ? 690 NAG A O4 1 HETATM 4339 O O5 . NAG F 3 . ? 6.540 54.863 -35.468 1.00 57.05 ? 690 NAG A O5 1 HETATM 4340 O O6 . NAG F 3 . ? 7.048 56.710 -37.306 1.00 64.48 ? 690 NAG A O6 1 HETATM 4341 O O7 . NAG F 3 . ? 4.263 50.904 -35.920 1.00 55.60 ? 690 NAG A O7 1 HETATM 4342 C C1 . GOL G 5 . ? 6.158 68.706 -4.300 1.00 43.46 ? 1758 GOL A C1 1 HETATM 4343 O O1 . GOL G 5 . ? 4.825 68.647 -5.246 1.00 44.38 ? 1758 GOL A O1 1 HETATM 4344 C C2 . GOL G 5 . ? 6.192 68.558 -2.893 1.00 45.48 ? 1758 GOL A C2 1 HETATM 4345 O O2 . GOL G 5 . ? 4.979 68.794 -2.337 1.00 45.76 ? 1758 GOL A O2 1 HETATM 4346 C C3 . GOL G 5 . ? 7.308 68.236 -2.526 1.00 43.47 ? 1758 GOL A C3 1 HETATM 4347 O O3 . GOL G 5 . ? 8.825 67.850 -2.550 1.00 33.75 ? 1758 GOL A O3 1 HETATM 4348 C C1 . GOL H 5 . ? 12.582 69.347 1.749 1.00 61.96 ? 1759 GOL A C1 1 HETATM 4349 O O1 . GOL H 5 . ? 11.296 69.549 2.702 1.00 60.96 ? 1759 GOL A O1 1 HETATM 4350 C C2 . GOL H 5 . ? 13.627 68.453 1.984 1.00 63.41 ? 1759 GOL A C2 1 HETATM 4351 O O2 . GOL H 5 . ? 13.251 67.481 2.829 1.00 64.73 ? 1759 GOL A O2 1 HETATM 4352 C C3 . GOL H 5 . ? 14.614 68.793 1.371 1.00 64.13 ? 1759 GOL A C3 1 HETATM 4353 O O3 . GOL H 5 . ? 15.568 69.611 0.435 1.00 64.40 ? 1759 GOL A O3 1 HETATM 4354 C C1 . GOL I 5 . ? 10.251 73.849 -3.055 1.00 73.52 ? 1760 GOL A C1 1 HETATM 4355 O O1 . GOL I 5 . ? 9.078 74.931 -3.314 1.00 74.33 ? 1760 GOL A O1 1 HETATM 4356 C C2 . GOL I 5 . ? 10.110 72.455 -3.113 1.00 72.86 ? 1760 GOL A C2 1 HETATM 4357 O O2 . GOL I 5 . ? 8.821 72.093 -3.277 1.00 73.51 ? 1760 GOL A O2 1 HETATM 4358 C C3 . GOL I 5 . ? 11.191 71.935 -2.993 1.00 71.00 ? 1760 GOL A C3 1 HETATM 4359 O O3 . GOL I 5 . ? 12.729 71.771 -2.806 1.00 70.40 ? 1760 GOL A O3 1 HETATM 4360 C C1 . GOL J 5 . ? 13.867 51.378 11.684 1.00 60.48 ? 1772 GOL A C1 1 HETATM 4361 O O1 . GOL J 5 . ? 12.905 52.585 11.231 1.00 57.24 ? 1772 GOL A O1 1 HETATM 4362 C C2 . GOL J 5 . ? 14.717 51.345 12.803 1.00 60.63 ? 1772 GOL A C2 1 HETATM 4363 O O2 . GOL J 5 . ? 15.136 52.586 13.144 1.00 63.02 ? 1772 GOL A O2 1 HETATM 4364 C C3 . GOL J 5 . ? 14.852 50.201 13.192 1.00 59.79 ? 1772 GOL A C3 1 HETATM 4365 O O3 . GOL J 5 . ? 14.712 48.648 13.297 1.00 53.30 ? 1772 GOL A O3 1 HETATM 4366 O O . HOH K 6 . ? 13.894 42.560 -5.561 1.00 7.52 ? 1000 HOH A O 1 HETATM 4367 O O . HOH K 6 . ? 24.397 56.456 5.040 1.00 17.65 ? 1001 HOH A O 1 HETATM 4368 O O . HOH K 6 . ? 7.556 61.090 -22.591 1.00 25.53 ? 1002 HOH A O 1 HETATM 4369 O O . HOH K 6 . ? -15.974 70.950 0.413 1.00 31.21 ? 1003 HOH A O 1 HETATM 4370 O O . HOH K 6 . ? 2.870 45.835 -0.957 1.00 22.72 ? 1004 HOH A O 1 HETATM 4371 O O . HOH K 6 . ? 8.516 39.038 -4.636 1.00 20.42 ? 1005 HOH A O 1 HETATM 4372 O O . HOH K 6 . ? 2.764 55.940 -9.309 1.00 18.02 ? 1006 HOH A O 1 HETATM 4373 O O . HOH K 6 . ? 4.049 58.927 -2.269 1.00 23.51 ? 1007 HOH A O 1 HETATM 4374 O O . HOH K 6 . ? 24.073 64.394 3.579 1.00 26.51 ? 1008 HOH A O 1 HETATM 4375 O O . HOH K 6 . ? 11.469 51.776 8.812 1.00 24.59 ? 1009 HOH A O 1 HETATM 4376 O O . HOH K 6 . ? 29.891 53.020 21.826 1.00 22.20 ? 1010 HOH A O 1 HETATM 4377 O O . HOH K 6 . ? 11.862 58.449 5.501 1.00 22.27 ? 1011 HOH A O 1 HETATM 4378 O O . HOH K 6 . ? 2.419 55.443 -6.688 1.00 20.36 ? 1012 HOH A O 1 HETATM 4379 O O . HOH K 6 . ? -1.831 54.661 -2.780 1.00 19.86 ? 1013 HOH A O 1 HETATM 4380 O O . HOH K 6 . ? 14.761 52.347 8.188 1.00 24.15 ? 1014 HOH A O 1 HETATM 4381 O O . HOH K 6 . ? 1.215 61.261 -3.326 1.00 21.74 ? 1015 HOH A O 1 HETATM 4382 O O . HOH K 6 . ? 24.308 65.889 5.884 1.00 19.30 ? 1016 HOH A O 1 HETATM 4383 O O . HOH K 6 . ? 32.721 61.848 8.764 1.00 24.40 ? 1017 HOH A O 1 HETATM 4384 O O . HOH K 6 . ? 5.117 42.114 3.506 1.00 26.98 ? 1018 HOH A O 1 HETATM 4385 O O . HOH K 6 . ? 9.517 66.714 13.131 1.00 29.65 ? 1019 HOH A O 1 HETATM 4386 O O . HOH K 6 . ? 12.943 61.103 5.269 1.00 17.50 ? 1020 HOH A O 1 HETATM 4387 O O . HOH K 6 . ? 17.725 53.201 -10.917 1.00 22.71 ? 1021 HOH A O 1 HETATM 4388 O O . HOH K 6 . ? 27.316 57.717 17.860 1.00 29.26 ? 1022 HOH A O 1 HETATM 4389 O O . HOH K 6 . ? 15.057 61.177 7.096 1.00 21.19 ? 1023 HOH A O 1 HETATM 4390 O O . HOH K 6 . ? 28.091 65.680 11.600 1.00 26.68 ? 1024 HOH A O 1 HETATM 4391 O O . HOH K 6 . ? 18.403 51.921 -2.315 1.00 30.77 ? 1025 HOH A O 1 HETATM 4392 O O . HOH K 6 . ? 1.060 56.765 -4.534 1.00 25.02 ? 1026 HOH A O 1 HETATM 4393 O O . HOH K 6 . ? 7.103 62.946 0.955 1.00 29.22 ? 1027 HOH A O 1 HETATM 4394 O O . HOH K 6 . ? 38.697 40.843 -6.735 1.00 22.90 ? 1028 HOH A O 1 HETATM 4395 O O . HOH K 6 . ? -5.445 48.210 -8.137 1.00 27.23 ? 1029 HOH A O 1 HETATM 4396 O O . HOH K 6 . ? 18.267 55.046 -8.814 1.00 20.03 ? 1030 HOH A O 1 HETATM 4397 O O . HOH K 6 . ? 19.968 65.888 -11.211 1.00 22.48 ? 1031 HOH A O 1 HETATM 4398 O O . HOH K 6 . ? 34.138 60.689 10.838 1.00 24.62 ? 1032 HOH A O 1 HETATM 4399 O O . HOH K 6 . ? 20.120 43.751 -3.574 1.00 27.75 ? 1033 HOH A O 1 HETATM 4400 O O . HOH K 6 . ? -3.756 50.538 -7.943 1.00 27.10 ? 1034 HOH A O 1 HETATM 4401 O O . HOH K 6 . ? 23.992 57.724 -13.065 1.00 28.75 ? 1035 HOH A O 1 HETATM 4402 O O . HOH K 6 . ? 5.070 44.659 0.353 1.00 21.60 ? 1036 HOH A O 1 HETATM 4403 O O . HOH K 6 . ? 27.312 66.436 2.956 1.00 20.21 ? 1037 HOH A O 1 HETATM 4404 O O . HOH K 6 . ? 13.139 49.896 7.076 1.00 21.06 ? 1038 HOH A O 1 HETATM 4405 O O . HOH K 6 . ? 7.160 75.285 -10.081 1.00 28.18 ? 1039 HOH A O 1 HETATM 4406 O O . HOH K 6 . ? 29.770 71.868 7.460 1.00 31.38 ? 1040 HOH A O 1 HETATM 4407 O O . HOH K 6 . ? 20.061 73.972 -6.616 1.00 25.79 ? 1041 HOH A O 1 HETATM 4408 O O . HOH K 6 . ? 34.765 54.158 -0.260 1.00 24.53 ? 1042 HOH A O 1 HETATM 4409 O O . HOH K 6 . ? 12.389 63.710 -19.664 1.00 23.99 ? 1043 HOH A O 1 HETATM 4410 O O . HOH K 6 . ? 29.385 50.300 24.519 1.00 23.20 ? 1044 HOH A O 1 HETATM 4411 O O . HOH K 6 . ? 2.689 49.370 -11.768 1.00 28.28 ? 1045 HOH A O 1 HETATM 4412 O O . HOH K 6 . ? 5.801 55.737 -0.062 1.00 24.43 ? 1047 HOH A O 1 HETATM 4413 O O . HOH K 6 . ? 25.819 62.684 26.886 1.00 21.76 ? 1048 HOH A O 1 HETATM 4414 O O . HOH K 6 . ? 30.009 66.111 2.488 1.00 21.61 ? 1049 HOH A O 1 HETATM 4415 O O . HOH K 6 . ? 21.705 65.001 -13.059 1.00 25.34 ? 1050 HOH A O 1 HETATM 4416 O O . HOH K 6 . ? 9.401 52.662 -11.981 1.00 17.66 ? 1051 HOH A O 1 HETATM 4417 O O . HOH K 6 . ? 17.738 52.005 32.548 1.00 32.44 ? 1052 HOH A O 1 HETATM 4418 O O . HOH K 6 . ? 1.388 52.022 14.116 1.00 30.25 ? 1053 HOH A O 1 HETATM 4419 O O . HOH K 6 . ? 1.955 74.002 2.008 1.00 28.65 ? 1054 HOH A O 1 HETATM 4420 O O . HOH K 6 . ? 30.186 66.573 -9.941 1.00 24.70 ? 1055 HOH A O 1 HETATM 4421 O O . HOH K 6 . ? 20.137 52.996 -12.005 1.00 22.20 ? 1056 HOH A O 1 HETATM 4422 O O . HOH K 6 . ? 14.563 61.115 -18.140 1.00 28.80 ? 1057 HOH A O 1 HETATM 4423 O O . HOH K 6 . ? 18.143 48.545 19.704 1.00 31.89 ? 1058 HOH A O 1 HETATM 4424 O O . HOH K 6 . ? 7.683 69.767 -6.827 1.00 23.48 ? 1059 HOH A O 1 HETATM 4425 O O . HOH K 6 . ? 1.911 67.594 -21.435 1.00 33.07 ? 1060 HOH A O 1 HETATM 4426 O O . HOH K 6 . ? 8.190 43.772 -1.908 1.00 21.29 ? 1061 HOH A O 1 HETATM 4427 O O . HOH K 6 . ? 39.553 52.898 14.525 1.00 33.65 ? 1062 HOH A O 1 HETATM 4428 O O . HOH K 6 . ? 4.150 43.886 -17.362 1.00 31.58 ? 1063 HOH A O 1 HETATM 4429 O O . HOH K 6 . ? 11.619 76.861 -14.354 1.00 34.94 ? 1064 HOH A O 1 HETATM 4430 O O . HOH K 6 . ? 13.803 62.112 21.245 1.00 31.15 ? 1065 HOH A O 1 HETATM 4431 O O . HOH K 6 . ? 5.161 55.137 12.958 1.00 28.97 ? 1066 HOH A O 1 HETATM 4432 O O . HOH K 6 . ? 23.466 63.433 22.458 1.00 30.98 ? 1067 HOH A O 1 HETATM 4433 O O . HOH K 6 . ? 3.636 56.466 14.763 1.00 27.57 ? 1068 HOH A O 1 HETATM 4434 O O . HOH K 6 . ? 14.621 53.626 -2.987 1.00 23.62 ? 1069 HOH A O 1 HETATM 4435 O O . HOH K 6 . ? 1.217 50.678 -7.935 1.00 23.67 ? 1070 HOH A O 1 HETATM 4436 O O . HOH K 6 . ? 24.797 48.345 -16.904 1.00 27.56 ? 1071 HOH A O 1 HETATM 4437 O O . HOH K 6 . ? 25.689 40.826 17.948 1.00 26.83 ? 1072 HOH A O 1 HETATM 4438 O O . HOH K 6 . ? 3.604 60.391 17.176 1.00 34.87 ? 1073 HOH A O 1 HETATM 4439 O O . HOH K 6 . ? 5.013 50.733 -21.402 1.00 31.38 ? 1074 HOH A O 1 HETATM 4440 O O . HOH K 6 . ? 28.966 62.438 13.888 1.00 28.66 ? 1075 HOH A O 1 HETATM 4441 O O . HOH K 6 . ? 8.189 68.819 4.638 1.00 32.75 ? 1076 HOH A O 1 HETATM 4442 O O . HOH K 6 . ? 6.581 61.636 -4.951 1.00 25.25 ? 1077 HOH A O 1 HETATM 4443 O O . HOH K 6 . ? 17.342 45.957 20.751 1.00 30.69 ? 1078 HOH A O 1 HETATM 4444 O O . HOH K 6 . ? 30.558 57.297 23.485 1.00 40.62 ? 1079 HOH A O 1 HETATM 4445 O O . HOH K 6 . ? 18.808 61.063 11.532 1.00 25.71 ? 1080 HOH A O 1 HETATM 4446 O O . HOH K 6 . ? 29.461 70.379 -4.935 1.00 26.30 ? 1082 HOH A O 1 HETATM 4447 O O . HOH K 6 . ? 31.613 68.971 -9.474 1.00 28.59 ? 1083 HOH A O 1 HETATM 4448 O O . HOH K 6 . ? 17.319 68.498 -6.288 1.00 30.13 ? 1084 HOH A O 1 HETATM 4449 O O . HOH K 6 . ? 20.107 51.085 25.802 1.00 33.42 ? 1085 HOH A O 1 HETATM 4450 O O . HOH K 6 . ? 23.830 59.455 -15.301 1.00 34.52 ? 1086 HOH A O 1 HETATM 4451 O O . HOH K 6 . ? 0.627 51.369 -5.343 1.00 30.86 ? 1087 HOH A O 1 HETATM 4452 O O . HOH K 6 . ? 33.663 61.329 2.688 1.00 28.92 ? 1088 HOH A O 1 HETATM 4453 O O . HOH K 6 . ? 0.493 53.446 -3.586 1.00 28.38 ? 1089 HOH A O 1 HETATM 4454 O O . HOH K 6 . ? 21.783 60.404 -16.772 1.00 30.50 ? 1090 HOH A O 1 HETATM 4455 O O . HOH K 6 . ? 34.136 48.326 19.649 1.00 26.60 ? 1091 HOH A O 1 HETATM 4456 O O . HOH K 6 . ? 30.822 70.588 -7.491 1.00 34.71 ? 1092 HOH A O 1 HETATM 4457 O O . HOH K 6 . ? -1.395 60.600 11.932 1.00 31.47 ? 1093 HOH A O 1 HETATM 4458 O O . HOH K 6 . ? 1.096 55.932 14.461 1.00 35.99 ? 1094 HOH A O 1 HETATM 4459 O O . HOH K 6 . ? 18.577 69.324 -4.051 1.00 29.38 ? 1095 HOH A O 1 HETATM 4460 O O . HOH K 6 . ? 27.421 38.623 17.818 1.00 38.00 ? 1096 HOH A O 1 HETATM 4461 O O . HOH K 6 . ? 14.758 37.556 27.024 1.00 41.28 ? 1097 HOH A O 1 HETATM 4462 O O . HOH K 6 . ? 1.048 39.986 -5.017 1.00 32.33 ? 1098 HOH A O 1 HETATM 4463 O O . HOH K 6 . ? 16.999 59.929 13.219 1.00 29.67 ? 1099 HOH A O 1 HETATM 4464 O O . HOH K 6 . ? 18.568 66.832 -18.643 1.00 34.39 ? 1100 HOH A O 1 HETATM 4465 O O . HOH K 6 . ? 22.048 42.613 11.840 1.00 32.15 ? 1101 HOH A O 1 HETATM 4466 O O . HOH K 6 . ? 18.210 49.387 26.081 1.00 35.97 ? 1102 HOH A O 1 HETATM 4467 O O . HOH K 6 . ? 3.693 52.430 12.988 1.00 35.75 ? 1103 HOH A O 1 HETATM 4468 O O . HOH K 6 . ? 15.138 65.948 18.021 1.00 33.04 ? 1104 HOH A O 1 HETATM 4469 O O . HOH K 6 . ? 15.379 55.170 15.728 1.00 28.82 ? 1105 HOH A O 1 HETATM 4470 O O . HOH K 6 . ? 1.345 57.365 -25.451 1.00 27.84 ? 1106 HOH A O 1 HETATM 4471 O O . HOH K 6 . ? 21.227 56.052 31.507 1.00 24.64 ? 1107 HOH A O 1 HETATM 4472 O O . HOH K 6 . ? 3.370 57.858 -27.285 1.00 25.64 ? 1108 HOH A O 1 HETATM 4473 O O . HOH K 6 . ? -1.188 41.480 -5.173 1.00 33.32 ? 1109 HOH A O 1 HETATM 4474 O O . HOH K 6 . ? 21.084 40.814 -1.575 1.00 29.75 ? 1110 HOH A O 1 HETATM 4475 O O . HOH K 6 . ? 26.194 36.445 18.456 1.00 40.91 ? 1111 HOH A O 1 HETATM 4476 O O . HOH K 6 . ? 1.719 52.715 -9.957 1.00 33.00 ? 1112 HOH A O 1 HETATM 4477 O O . HOH K 6 . ? 34.284 62.032 14.233 1.00 34.26 ? 1113 HOH A O 1 HETATM 4478 O O . HOH K 6 . ? 23.467 66.031 21.864 1.00 32.66 ? 1114 HOH A O 1 HETATM 4479 O O . HOH K 6 . ? -13.192 53.142 -13.317 1.00 28.17 ? 1115 HOH A O 1 HETATM 4480 O O . HOH K 6 . ? 16.890 51.760 26.907 1.00 31.43 ? 1116 HOH A O 1 HETATM 4481 O O . HOH K 6 . ? 13.693 64.649 20.238 1.00 32.57 ? 1117 HOH A O 1 HETATM 4482 O O . HOH K 6 . ? 2.877 78.541 -9.539 1.00 34.00 ? 1118 HOH A O 1 HETATM 4483 O O . HOH K 6 . ? -2.252 50.361 -10.350 1.00 29.81 ? 1119 HOH A O 1 HETATM 4484 O O . HOH K 6 . ? 5.581 70.420 7.520 1.00 33.69 ? 1120 HOH A O 1 HETATM 4485 O O . HOH K 6 . ? -4.830 74.970 4.267 1.00 35.08 ? 1121 HOH A O 1 HETATM 4486 O O . HOH K 6 . ? 15.646 42.915 -3.250 1.00 32.49 ? 1122 HOH A O 1 HETATM 4487 O O . HOH K 6 . ? 11.750 66.774 11.403 1.00 34.59 ? 1123 HOH A O 1 HETATM 4488 O O . HOH K 6 . ? 16.572 65.362 -20.045 1.00 32.10 ? 1124 HOH A O 1 HETATM 4489 O O . HOH K 6 . ? 23.645 41.243 -1.070 1.00 28.90 ? 1125 HOH A O 1 HETATM 4490 O O . HOH K 6 . ? 21.937 72.685 -2.778 1.00 32.43 ? 1126 HOH A O 1 HETATM 4491 O O . HOH K 6 . ? -12.187 50.812 -14.121 1.00 28.56 ? 1127 HOH A O 1 HETATM 4492 O O . HOH K 6 . ? -12.884 54.884 -15.432 1.00 32.71 ? 1128 HOH A O 1 HETATM 4493 O O . HOH K 6 . ? 2.983 58.591 -29.979 1.00 28.63 ? 1129 HOH A O 1 HETATM 4494 O O . HOH K 6 . ? 24.574 38.916 -2.210 1.00 30.88 ? 1130 HOH A O 1 HETATM 4495 O O . HOH K 6 . ? -11.463 51.138 -16.803 1.00 31.67 ? 1131 HOH A O 1 HETATM 4496 O O . HOH K 6 . ? 35.820 53.823 -7.699 1.00 37.92 ? 1132 HOH A O 1 HETATM 4497 O O . HOH K 6 . ? 16.530 48.845 -19.353 1.00 31.59 ? 1133 HOH A O 1 HETATM 4498 O O . HOH K 6 . ? 2.985 64.422 -23.712 1.00 32.40 ? 1134 HOH A O 1 HETATM 4499 O O . HOH K 6 . ? 12.132 41.525 14.101 1.00 48.37 ? 1135 HOH A O 1 HETATM 4500 O O . HOH K 6 . ? 2.371 60.527 19.877 1.00 38.50 ? 1136 HOH A O 1 HETATM 4501 O O . HOH K 6 . ? -15.912 67.230 -3.369 1.00 35.50 ? 1137 HOH A O 1 HETATM 4502 O O . HOH K 6 . ? -7.471 75.021 -20.791 1.00 35.88 ? 1138 HOH A O 1 HETATM 4503 O O . HOH K 6 . ? 42.894 59.361 -1.572 1.00 43.08 ? 1139 HOH A O 1 HETATM 4504 O O . HOH K 6 . ? -15.874 51.456 -10.980 1.00 33.43 ? 1140 HOH A O 1 HETATM 4505 O O . HOH K 6 . ? -5.491 46.941 6.629 1.00 30.51 ? 1141 HOH A O 1 HETATM 4506 O O . HOH K 6 . ? 16.231 58.249 27.673 1.00 34.27 ? 1142 HOH A O 1 HETATM 4507 O O . HOH K 6 . ? 30.945 56.577 -13.140 1.00 40.66 ? 1143 HOH A O 1 HETATM 4508 O O . HOH K 6 . ? -2.669 75.986 5.785 1.00 40.10 ? 1144 HOH A O 1 HETATM 4509 O O . HOH K 6 . ? 4.911 65.323 -25.633 1.00 37.45 ? 1145 HOH A O 1 HETATM 4510 O O . HOH K 6 . ? 27.659 40.664 -12.822 1.00 44.19 ? 1146 HOH A O 1 HETATM 4511 O O . HOH K 6 . ? -7.182 67.448 -23.933 1.00 36.05 ? 1147 HOH A O 1 HETATM 4512 O O . HOH K 6 . ? 12.065 59.064 14.034 1.00 36.25 ? 1148 HOH A O 1 HETATM 4513 O O . HOH K 6 . ? 5.026 78.711 -10.858 1.00 44.22 ? 1149 HOH A O 1 HETATM 4514 O O . HOH K 6 . ? -0.225 60.415 19.394 1.00 40.40 ? 1150 HOH A O 1 HETATM 4515 O O . HOH K 6 . ? 40.124 58.982 10.956 1.00 44.24 ? 1151 HOH A O 1 HETATM 4516 O O . HOH K 6 . ? 40.601 51.074 -0.410 1.00 30.38 ? 1152 HOH A O 1 HETATM 4517 O O . HOH K 6 . ? 5.547 58.779 -30.886 1.00 38.64 ? 1153 HOH A O 1 HETATM 4518 O O . HOH K 6 . ? 37.688 56.318 -6.801 1.00 40.22 ? 1154 HOH A O 1 HETATM 4519 O O . HOH K 6 . ? -2.329 53.082 -30.414 1.00 40.76 ? 1155 HOH A O 1 HETATM 4520 O O . HOH K 6 . ? -14.406 65.311 -10.056 1.00 39.04 ? 1156 HOH A O 1 HETATM 4521 O O . HOH K 6 . ? 1.273 77.646 -19.803 1.00 34.73 ? 1157 HOH A O 1 HETATM 4522 O O . HOH K 6 . ? 24.111 66.459 18.982 1.00 33.14 ? 1158 HOH A O 1 HETATM 4523 O O . HOH K 6 . ? 20.817 54.565 33.608 1.00 38.33 ? 1159 HOH A O 1 HETATM 4524 O O . HOH K 6 . ? 26.083 38.537 -6.428 1.00 34.96 ? 1160 HOH A O 1 HETATM 4525 O O . HOH K 6 . ? -3.276 57.831 -9.629 1.00 30.94 ? 1161 HOH A O 1 HETATM 4526 O O . HOH K 6 . ? 10.457 60.946 -26.241 1.00 40.50 ? 1162 HOH A O 1 HETATM 4527 O O . HOH K 6 . ? 0.788 66.427 -23.595 1.00 42.76 ? 1163 HOH A O 1 HETATM 4528 O O . HOH K 6 . ? 42.038 55.057 18.221 1.00 38.16 ? 1164 HOH A O 1 HETATM 4529 O O . HOH K 6 . ? 31.687 50.990 -15.748 1.00 34.70 ? 1165 HOH A O 1 HETATM 4530 O O . HOH K 6 . ? 18.396 42.563 25.164 1.00 35.21 ? 1166 HOH A O 1 HETATM 4531 O O . HOH K 6 . ? -4.449 67.086 -24.158 1.00 32.19 ? 1167 HOH A O 1 HETATM 4532 O O . HOH K 6 . ? 16.137 75.338 -5.498 1.00 31.56 ? 1168 HOH A O 1 HETATM 4533 O O . HOH K 6 . ? 22.266 44.741 6.533 1.00 32.65 ? 1169 HOH A O 1 HETATM 4534 O O . HOH K 6 . ? 14.354 57.214 21.251 1.00 37.71 ? 1170 HOH A O 1 HETATM 4535 O O . HOH K 6 . ? 41.224 35.409 13.163 1.00 38.04 ? 1171 HOH A O 1 HETATM 4536 O O . HOH K 6 . ? 26.318 55.663 -15.549 1.00 39.11 ? 1172 HOH A O 1 HETATM 4537 O O . HOH K 6 . ? 37.126 59.344 22.559 1.00 34.27 ? 1173 HOH A O 1 HETATM 4538 O O . HOH K 6 . ? 26.949 71.380 8.416 1.00 33.21 ? 1174 HOH A O 1 HETATM 4539 O O . HOH K 6 . ? 18.222 65.511 15.936 1.00 36.29 ? 1175 HOH A O 1 HETATM 4540 O O . HOH K 6 . ? 18.526 79.469 -10.851 1.00 37.51 ? 1176 HOH A O 1 HETATM 4541 O O . HOH K 6 . ? 12.871 61.675 14.453 1.00 34.60 ? 1177 HOH A O 1 HETATM 4542 O O . HOH K 6 . ? 31.362 75.948 6.204 1.00 41.57 ? 1178 HOH A O 1 HETATM 4543 O O . HOH K 6 . ? -7.985 73.678 -17.902 1.00 46.57 ? 1179 HOH A O 1 HETATM 4544 O O . HOH K 6 . ? 11.567 63.770 18.560 1.00 42.24 ? 1181 HOH A O 1 HETATM 4545 O O . HOH K 6 . ? 18.686 75.410 -4.878 1.00 40.79 ? 1182 HOH A O 1 HETATM 4546 O O . HOH K 6 . ? 24.763 79.177 -2.573 1.00 35.71 ? 1183 HOH A O 1 HETATM 4547 O O . HOH K 6 . ? 42.059 37.750 13.004 1.00 33.96 ? 1184 HOH A O 1 HETATM 4548 O O . HOH K 6 . ? -8.083 75.542 -12.512 1.00 34.68 ? 1185 HOH A O 1 HETATM 4549 O O . HOH K 6 . ? 14.998 63.698 4.828 1.00 36.50 ? 1186 HOH A O 1 HETATM 4550 O O . HOH K 6 . ? 41.299 55.049 14.012 1.00 39.35 ? 1187 HOH A O 1 HETATM 4551 O O . HOH K 6 . ? 14.932 51.294 29.111 1.00 38.02 ? 1188 HOH A O 1 HETATM 4552 O O . HOH K 6 . ? 9.019 70.331 1.125 1.00 35.60 ? 1189 HOH A O 1 HETATM 4553 O O . HOH K 6 . ? -9.587 50.141 10.690 1.00 37.57 ? 1190 HOH A O 1 HETATM 4554 O O . HOH K 6 . ? 34.204 69.531 -8.831 1.00 35.88 ? 1191 HOH A O 1 HETATM 4555 O O . HOH K 6 . ? 31.142 72.699 5.400 1.00 40.48 ? 1192 HOH A O 1 HETATM 4556 O O . HOH K 6 . ? -9.251 47.598 -1.709 1.00 46.89 ? 1193 HOH A O 1 HETATM 4557 O O . HOH K 6 . ? -17.589 58.677 -9.927 1.00 38.18 ? 1194 HOH A O 1 HETATM 4558 O O . HOH K 6 . ? -10.137 75.130 -16.371 1.00 43.97 ? 1195 HOH A O 1 HETATM 4559 O O . HOH K 6 . ? 37.851 43.044 23.841 1.00 38.76 ? 1196 HOH A O 1 HETATM 4560 O O . HOH K 6 . ? 35.659 52.408 26.566 1.00 39.17 ? 1197 HOH A O 1 HETATM 4561 O O . HOH K 6 . ? 4.598 74.102 -21.310 1.00 42.97 ? 1198 HOH A O 1 HETATM 4562 O O . HOH K 6 . ? -7.538 70.016 -23.108 1.00 43.35 ? 1199 HOH A O 1 HETATM 4563 O O . HOH K 6 . ? 19.654 51.970 -21.090 1.00 34.19 ? 1200 HOH A O 1 HETATM 4564 O O . HOH K 6 . ? 11.178 68.239 14.803 1.00 43.42 ? 1201 HOH A O 1 HETATM 4565 O O . HOH K 6 . ? 14.525 65.249 -18.588 1.00 45.08 ? 1202 HOH A O 1 HETATM 4566 O O . HOH K 6 . ? 17.400 43.666 22.935 1.00 44.33 ? 1203 HOH A O 1 HETATM 4567 O O . HOH K 6 . ? 15.941 65.472 3.184 1.00 40.25 ? 1204 HOH A O 1 HETATM 4568 O O . HOH K 6 . ? 39.135 53.145 -5.879 1.00 42.03 ? 1205 HOH A O 1 HETATM 4569 O O . HOH K 6 . ? 6.571 71.900 -5.648 1.00 47.59 ? 1206 HOH A O 1 HETATM 4570 O O . HOH K 6 . ? 2.605 50.449 -24.245 1.00 36.44 ? 1207 HOH A O 1 HETATM 4571 O O . HOH K 6 . ? 4.903 72.010 11.505 1.00 43.03 ? 1208 HOH A O 1 HETATM 4572 O O . HOH K 6 . ? -10.948 76.397 -0.740 1.00 42.95 ? 1209 HOH A O 1 HETATM 4573 O O . HOH K 6 . ? -11.424 63.512 3.051 1.00 39.85 ? 1210 HOH A O 1 HETATM 4574 O O . HOH K 6 . ? 34.686 59.610 -6.755 1.00 36.00 ? 1211 HOH A O 1 HETATM 4575 O O . HOH K 6 . ? 31.308 74.649 -1.421 1.00 43.78 ? 1212 HOH A O 1 HETATM 4576 O O . HOH K 6 . ? 31.794 70.638 -11.835 1.00 41.49 ? 1213 HOH A O 1 HETATM 4577 O O . HOH K 6 . ? 44.265 41.101 8.001 1.00 33.86 ? 1214 HOH A O 1 HETATM 4578 O O . HOH K 6 . ? 41.118 41.892 -6.229 1.00 35.93 ? 1215 HOH A O 1 HETATM 4579 O O . HOH K 6 . ? -7.318 50.563 -22.832 1.00 39.89 ? 1216 HOH A O 1 HETATM 4580 O O . HOH K 6 . ? 11.980 64.003 15.451 1.00 37.27 ? 1217 HOH A O 1 HETATM 4581 O O . HOH K 6 . ? 10.477 69.705 -0.874 1.00 41.91 ? 1218 HOH A O 1 HETATM 4582 O O . HOH K 6 . ? 15.930 52.305 22.481 1.00 46.22 ? 1219 HOH A O 1 HETATM 4583 O O . HOH K 6 . ? 22.641 72.566 -16.552 1.00 40.56 ? 1220 HOH A O 1 HETATM 4584 O O . HOH K 6 . ? 22.593 77.266 -0.774 1.00 38.37 ? 1221 HOH A O 1 HETATM 4585 O O . HOH K 6 . ? -16.838 54.094 1.777 1.00 45.33 ? 1222 HOH A O 1 HETATM 4586 O O . HOH K 6 . ? 3.264 48.216 -25.533 1.00 38.19 ? 1223 HOH A O 1 HETATM 4587 O O . HOH K 6 . ? 32.783 61.188 -5.975 1.00 38.74 ? 1224 HOH A O 1 HETATM 4588 O O . HOH K 6 . ? -13.253 71.679 -14.138 1.00 45.17 ? 1225 HOH A O 1 HETATM 4589 O O . HOH K 6 . ? 41.059 48.631 24.505 1.00 39.45 ? 1226 HOH A O 1 HETATM 4590 O O . HOH K 6 . ? 4.022 71.688 -5.034 1.00 48.50 ? 1227 HOH A O 1 HETATM 4591 O O . HOH K 6 . ? 9.649 41.342 -2.772 1.00 42.13 ? 1228 HOH A O 1 HETATM 4592 O O . HOH K 6 . ? 43.284 43.005 -3.878 1.00 42.75 ? 1229 HOH A O 1 HETATM 4593 O O . HOH K 6 . ? 14.017 78.190 -13.529 1.00 36.22 ? 1230 HOH A O 1 HETATM 4594 O O . HOH K 6 . ? 13.843 42.843 -14.163 1.00 41.74 ? 1231 HOH A O 1 HETATM 4595 O O . HOH K 6 . ? 16.012 41.692 9.042 1.00 39.14 ? 1232 HOH A O 1 HETATM 4596 O O . HOH K 6 . ? -1.303 48.499 -7.791 1.00 48.65 ? 1233 HOH A O 1 HETATM 4597 O O . HOH K 6 . ? 0.711 60.102 -30.238 1.00 40.30 ? 1234 HOH A O 1 HETATM 4598 O O . HOH K 6 . ? -5.812 80.551 -0.422 1.00 39.25 ? 1235 HOH A O 1 HETATM 4599 O O . HOH K 6 . ? 14.363 54.394 21.830 1.00 45.33 ? 1236 HOH A O 1 HETATM 4600 O O . HOH K 6 . ? 23.444 36.198 13.237 1.00 39.31 ? 1237 HOH A O 1 HETATM 4601 O O . HOH K 6 . ? 29.128 77.768 -2.138 1.00 40.09 ? 1238 HOH A O 1 HETATM 4602 O O . HOH K 6 . ? 4.576 40.268 9.458 1.00 45.90 ? 1239 HOH A O 1 HETATM 4603 O O . HOH K 6 . ? 7.437 39.274 6.718 1.00 44.42 ? 1240 HOH A O 1 HETATM 4604 O O . HOH K 6 . ? 43.580 41.981 -1.214 1.00 34.19 ? 1241 HOH A O 1 HETATM 4605 O O . HOH K 6 . ? 2.209 44.798 -15.842 1.00 44.66 ? 1242 HOH A O 1 HETATM 4606 O O . HOH K 6 . ? 5.710 47.100 -24.238 1.00 35.91 ? 1243 HOH A O 1 HETATM 4607 O O . HOH K 6 . ? 14.145 57.804 15.545 1.00 48.29 ? 1244 HOH A O 1 HETATM 4608 O O . HOH K 6 . ? 13.398 53.279 14.741 1.00 50.43 ? 1245 HOH A O 1 HETATM 4609 O O . HOH K 6 . ? 6.239 60.970 -29.736 1.00 43.60 ? 1246 HOH A O 1 HETATM 4610 O O . HOH K 6 . ? -1.006 63.104 19.098 1.00 39.77 ? 1247 HOH A O 1 HETATM 4611 O O . HOH K 6 . ? 30.713 59.454 -11.921 1.00 43.42 ? 1248 HOH A O 1 HETATM 4612 O O . HOH K 6 . ? 12.135 80.253 -12.526 1.00 39.59 ? 1249 HOH A O 1 HETATM 4613 O O . HOH K 6 . ? 22.917 45.739 -15.649 1.00 40.41 ? 1250 HOH A O 1 HETATM 4614 O O . HOH K 6 . ? 27.498 79.039 -9.491 1.00 44.45 ? 1251 HOH A O 1 HETATM 4615 O O . HOH K 6 . ? 18.159 68.901 1.962 1.00 40.51 ? 1252 HOH A O 1 HETATM 4616 O O . HOH K 6 . ? 12.797 40.283 6.089 1.00 37.34 ? 1253 HOH A O 1 HETATM 4617 O O . HOH K 6 . ? 14.244 65.557 15.463 1.00 41.23 ? 1254 HOH A O 1 HETATM 4618 O O . HOH K 6 . ? 6.902 77.487 -8.257 1.00 41.11 ? 1255 HOH A O 1 HETATM 4619 O O . HOH K 6 . ? 17.411 70.867 -2.015 1.00 45.01 ? 1256 HOH A O 1 HETATM 4620 O O . HOH K 6 . ? 20.962 66.524 16.293 1.00 41.69 ? 1257 HOH A O 1 HETATM 4621 O O . HOH K 6 . ? 40.704 50.317 -3.312 1.00 49.68 ? 1258 HOH A O 1 HETATM 4622 O O . HOH K 6 . ? 8.258 46.687 -24.892 1.00 34.28 ? 1259 HOH A O 1 HETATM 4623 O O . HOH K 6 . ? 34.067 74.344 -1.939 1.00 45.91 ? 1260 HOH A O 1 HETATM 4624 O O . HOH K 6 . ? 20.726 45.048 -14.078 1.00 47.18 ? 1261 HOH A O 1 HETATM 4625 O O . HOH K 6 . ? 31.060 61.351 -13.767 1.00 45.63 ? 1262 HOH A O 1 HETATM 4626 O O . HOH K 6 . ? 21.316 76.490 -13.037 1.00 40.31 ? 1263 HOH A O 1 HETATM 4627 O O . HOH K 6 . ? 20.455 79.243 -12.815 1.00 41.87 ? 1264 HOH A O 1 HETATM 4628 O O . HOH K 6 . ? 0.528 65.732 15.915 1.00 43.72 ? 1265 HOH A O 1 HETATM 4629 O O . HOH K 6 . ? 14.978 41.046 15.973 1.00 43.11 ? 1266 HOH A O 1 HETATM 4630 O O . HOH K 6 . ? -4.724 61.539 13.922 1.00 45.56 ? 1267 HOH A O 1 HETATM 4631 O O . HOH K 6 . ? 5.209 78.996 -14.708 1.00 42.17 ? 1268 HOH A O 1 HETATM 4632 O O . HOH K 6 . ? 45.091 50.164 12.453 1.00 44.37 ? 1269 HOH A O 1 HETATM 4633 O O . HOH K 6 . ? 33.491 71.378 -6.708 1.00 42.02 ? 1270 HOH A O 1 HETATM 4634 O O . HOH K 6 . ? 33.803 61.770 23.237 1.00 44.86 ? 1271 HOH A O 1 HETATM 4635 O O . HOH K 6 . ? 22.621 58.485 -25.348 1.00 46.71 ? 1272 HOH A O 1 HETATM 4636 O O . HOH K 6 . ? 11.456 39.902 8.710 1.00 43.22 ? 1273 HOH A O 1 HETATM 4637 O O . HOH K 6 . ? 17.423 40.527 -3.335 1.00 41.25 ? 1274 HOH A O 1 HETATM 4638 O O . HOH K 6 . ? -17.064 65.822 -9.322 1.00 46.64 ? 1275 HOH A O 1 HETATM 4639 O O . HOH K 6 . ? 8.672 55.233 -28.606 1.00 35.42 ? 1276 HOH A O 1 HETATM 4640 O O . HOH K 6 . ? 35.114 69.973 -5.055 1.00 43.18 ? 1277 HOH A O 1 HETATM 4641 O O . HOH K 6 . ? -10.229 77.054 -4.464 1.00 39.69 ? 1278 HOH A O 1 HETATM 4642 O O . HOH K 6 . ? 23.727 42.733 5.129 1.00 42.37 ? 1279 HOH A O 1 HETATM 4643 O O . HOH K 6 . ? 19.519 41.468 27.419 1.00 46.90 ? 1280 HOH A O 1 HETATM 4644 O O . HOH K 6 . ? 10.712 44.126 -17.980 1.00 41.10 ? 1281 HOH A O 1 HETATM 4645 O O . HOH K 6 . ? 21.736 68.226 21.499 1.00 41.25 ? 1282 HOH A O 1 HETATM 4646 O O . HOH K 6 . ? 23.615 75.907 -14.285 1.00 46.09 ? 1283 HOH A O 1 HETATM 4647 O O . HOH K 6 . ? 27.412 34.384 15.389 1.00 42.76 ? 1284 HOH A O 1 HETATM 4648 O O . HOH K 6 . ? 28.166 35.861 8.814 1.00 49.28 ? 1285 HOH A O 1 HETATM 4649 O O . HOH K 6 . ? -5.659 66.297 13.141 1.00 42.72 ? 1286 HOH A O 1 HETATM 4650 O O . HOH K 6 . ? 4.542 73.513 -3.134 1.00 43.14 ? 1287 HOH A O 1 HETATM 4651 O O . HOH K 6 . ? 33.849 34.314 12.409 1.00 43.79 ? 1288 HOH A O 1 HETATM 4652 O O . HOH K 6 . ? 15.412 61.205 15.350 1.00 50.45 ? 1289 HOH A O 1 HETATM 4653 O O . HOH K 6 . ? -2.226 71.094 -26.042 1.00 51.49 ? 1290 HOH A O 1 HETATM 4654 O O . HOH K 6 . ? 0.808 74.842 5.808 1.00 49.58 ? 1291 HOH A O 1 HETATM 4655 O O . HOH K 6 . ? -6.111 39.244 1.352 1.00 52.17 ? 1292 HOH A O 1 HETATM 4656 O O . HOH K 6 . ? 31.838 62.162 -3.645 1.00 47.38 ? 1293 HOH A O 1 HETATM 4657 O O . HOH K 6 . ? 39.513 63.237 9.709 1.00 42.25 ? 1294 HOH A O 1 HETATM 4658 O O . HOH K 6 . ? 25.756 67.276 -16.024 1.00 42.46 ? 1295 HOH A O 1 HETATM 4659 O O . HOH K 6 . ? -0.537 77.598 5.233 1.00 48.44 ? 1296 HOH A O 1 HETATM 4660 O O . HOH K 6 . ? 18.213 46.633 -19.619 1.00 42.30 ? 1297 HOH A O 1 HETATM 4661 O O . HOH K 6 . ? 33.874 70.958 6.198 1.00 46.00 ? 1298 HOH A O 1 HETATM 4662 O O . HOH K 6 . ? 45.101 43.588 10.887 1.00 43.98 ? 1299 HOH A O 1 HETATM 4663 O O . HOH K 6 . ? 19.938 41.164 11.009 1.00 46.94 ? 1300 HOH A O 1 HETATM 4664 O O . HOH K 6 . ? 11.142 79.513 -16.064 1.00 48.36 ? 1301 HOH A O 1 HETATM 4665 O O . HOH K 6 . ? 28.582 39.852 5.191 1.00 45.69 ? 1302 HOH A O 1 HETATM 4666 O O . HOH K 6 . ? 7.260 35.515 1.161 1.00 47.79 ? 1303 HOH A O 1 HETATM 4667 O O . HOH K 6 . ? 30.644 39.055 -9.210 1.00 43.54 ? 1304 HOH A O 1 HETATM 4668 O O . HOH K 6 . ? 25.521 55.158 -20.213 1.00 44.81 ? 1305 HOH A O 1 HETATM 4669 O O . HOH K 6 . ? 6.282 54.905 19.172 1.00 41.97 ? 1306 HOH A O 1 HETATM 4670 O O . HOH K 6 . ? 45.887 43.463 7.852 1.00 44.06 ? 1307 HOH A O 1 HETATM 4671 O O . HOH K 6 . ? 16.162 70.252 -20.204 1.00 44.32 ? 1308 HOH A O 1 HETATM 4672 O O . HOH K 6 . ? 23.293 47.060 33.299 1.00 50.78 ? 1309 HOH A O 1 HETATM 4673 O O . HOH K 6 . ? 43.758 64.365 1.076 1.00 50.26 ? 1310 HOH A O 1 HETATM 4674 O O . HOH K 6 . ? 22.466 38.913 11.365 1.00 47.19 ? 1311 HOH A O 1 HETATM 4675 O O . HOH K 6 . ? 31.557 74.620 -6.643 1.00 50.11 ? 1312 HOH A O 1 HETATM 4676 O O . HOH K 6 . ? 21.501 67.687 13.871 1.00 43.40 ? 1313 HOH A O 1 HETATM 4677 O O . HOH K 6 . ? 22.267 41.644 30.346 1.00 41.41 ? 1314 HOH A O 1 HETATM 4678 O O . HOH K 6 . ? 32.438 49.504 29.485 1.00 41.89 ? 1315 HOH A O 1 HETATM 4679 O O . HOH K 6 . ? 17.068 39.134 -0.948 1.00 41.93 ? 1316 HOH A O 1 HETATM 4680 O O . HOH K 6 . ? 34.267 53.853 -10.483 1.00 46.03 ? 1317 HOH A O 1 HETATM 4681 O O . HOH K 6 . ? 43.451 48.997 -4.036 1.00 36.56 ? 1318 HOH A O 1 HETATM 4682 O O . HOH K 6 . ? 22.843 61.052 -19.292 1.00 48.78 ? 1319 HOH A O 1 HETATM 4683 O O . HOH K 6 . ? 5.463 76.551 -19.249 1.00 44.20 ? 1320 HOH A O 1 HETATM 4684 O O . HOH K 6 . ? -2.828 72.875 15.240 1.00 49.53 ? 1321 HOH A O 1 HETATM 4685 O O . HOH K 6 . ? 46.273 44.768 5.041 1.00 53.19 ? 1322 HOH A O 1 HETATM 4686 O O . HOH K 6 . ? -10.832 75.770 -12.701 1.00 46.69 ? 1323 HOH A O 1 HETATM 4687 O O . HOH K 6 . ? -13.245 69.457 -6.284 1.00 42.10 ? 1324 HOH A O 1 HETATM 4688 O O . HOH K 6 . ? 14.340 47.074 30.504 1.00 46.64 ? 1325 HOH A O 1 HETATM 4689 O O . HOH K 6 . ? 47.284 47.672 3.913 1.00 32.14 ? 1326 HOH A O 1 HETATM 4690 O O . HOH K 6 . ? 48.736 45.899 3.669 1.00 42.71 ? 1327 HOH A O 1 HETATM 4691 O O . HOH K 6 . ? -3.221 77.763 -20.836 1.00 49.55 ? 1328 HOH A O 1 HETATM 4692 O O . HOH K 6 . ? -4.290 75.131 14.166 1.00 49.41 ? 1329 HOH A O 1 HETATM 4693 O O . HOH K 6 . ? 36.208 62.251 21.934 1.00 48.31 ? 1330 HOH A O 1 HETATM 4694 O O . HOH K 6 . ? 6.267 56.229 -30.725 1.00 46.04 ? 1331 HOH A O 1 HETATM 4695 O O . HOH K 6 . ? 18.509 61.966 -28.650 1.00 48.15 ? 1332 HOH A O 1 HETATM 4696 O O . HOH K 6 . ? -2.205 45.262 13.779 1.00 48.23 ? 1333 HOH A 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 GLN 1 1 ? ? ? A . n A 1 2 GLN 2 2 2 GLN GLN A . n A 1 3 ILE 3 3 3 ILE ILE A . n A 1 4 GLU 4 4 4 GLU GLU A . n A 1 5 GLN 5 5 5 GLN GLN A . n A 1 6 PRO 6 6 6 PRO PRO A . n A 1 7 TYR 7 7 7 TYR TYR A . n A 1 8 ARG 8 8 8 ARG ARG A . n A 1 9 THR 9 9 9 THR THR A . n A 1 10 GLY 10 10 10 GLY GLY A . n A 1 11 TYR 11 11 11 TYR TYR A . n A 1 12 HIS 12 12 12 HIS HIS A . n A 1 13 PHE 13 13 13 PHE PHE A . n A 1 14 GLN 14 14 14 GLN GLN A . n A 1 15 PRO 15 15 15 PRO PRO A . n A 1 16 PRO 16 16 16 PRO PRO A . n A 1 17 SER 17 17 17 SER SER A . n A 1 18 ASN 18 18 18 ASN ASN A . n A 1 19 TRP 19 19 19 TRP TRP A . n A 1 20 MET 20 20 20 MET MET A . n A 1 21 ASN 21 21 21 ASN ASN A . n A 1 22 ASP 22 22 22 ASP ASP A . n A 1 23 PRO 23 23 23 PRO PRO A . n A 1 24 ASN 24 24 24 ASN ASN A . n A 1 25 GLY 25 25 25 GLY GLY A . n A 1 26 PRO 26 26 26 PRO PRO A . n A 1 27 MET 27 27 27 MET MET A . n A 1 28 LEU 28 28 28 LEU LEU A . n A 1 29 TYR 29 29 29 TYR TYR A . n A 1 30 GLN 30 30 30 GLN GLN 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 TYR 33 33 33 TYR TYR A . n A 1 34 HIS 34 34 34 HIS HIS A . n A 1 35 PHE 35 35 35 PHE PHE A . n A 1 36 PHE 36 36 36 PHE PHE A . n A 1 37 TYR 37 37 37 TYR TYR A . n A 1 38 GLN 38 38 38 GLN GLN A . n A 1 39 TYR 39 39 39 TYR TYR A . n A 1 40 ASN 40 40 40 ASN ASN A . n A 1 41 PRO 41 41 41 PRO PRO A . n A 1 42 TYR 42 42 42 TYR TYR A . n A 1 43 ALA 43 43 43 ALA ALA A . n A 1 44 ALA 44 44 44 ALA ALA A . n A 1 45 THR 45 45 45 THR THR A . n A 1 46 PHE 46 46 46 PHE PHE A . n A 1 47 GLY 47 47 47 GLY GLY A . n A 1 48 ASP 48 48 48 ASP ASP A . n A 1 49 VAL 49 49 49 VAL VAL A . n A 1 50 ILE 50 50 50 ILE ILE A . n A 1 51 ILE 51 51 51 ILE ILE A . n A 1 52 TRP 52 52 52 TRP TRP A . n A 1 53 GLY 53 53 53 GLY GLY A . n A 1 54 HIS 54 54 54 HIS HIS A . n A 1 55 ALA 55 55 55 ALA ALA A . n A 1 56 VAL 56 56 56 VAL VAL A . n A 1 57 SER 57 57 57 SER SER A . n A 1 58 TYR 58 58 58 TYR TYR A . n A 1 59 ASP 59 59 59 ASP ASP A . n A 1 60 LEU 60 60 60 LEU LEU A . n A 1 61 VAL 61 61 61 VAL VAL A . n A 1 62 ASN 62 62 62 ASN ASN A . n A 1 63 TRP 63 63 63 TRP TRP A . n A 1 64 ILE 64 64 64 ILE ILE A . n A 1 65 HIS 65 65 65 HIS HIS A . n A 1 66 LEU 66 66 66 LEU LEU A . n A 1 67 ASP 67 67 67 ASP ASP A . n A 1 68 PRO 68 68 68 PRO PRO A . n A 1 69 ALA 69 69 69 ALA ALA A . n A 1 70 ILE 70 70 70 ILE ILE A . n A 1 71 TYR 71 71 71 TYR TYR A . n A 1 72 PRO 72 72 72 PRO PRO A . n A 1 73 THR 73 73 73 THR THR A . n A 1 74 GLN 74 74 74 GLN GLN A . n A 1 75 GLU 75 75 75 GLU GLU A . n A 1 76 ALA 76 76 76 ALA ALA A . n A 1 77 ASP 77 77 77 ASP ASP A . n A 1 78 SER 78 78 78 SER SER A . n A 1 79 LYS 79 79 79 LYS LYS A . n A 1 80 SER 80 80 80 SER SER A . n A 1 81 CYS 81 81 81 CYS CYS A . n A 1 82 TRP 82 82 82 TRP TRP A . n A 1 83 SER 83 83 83 SER SER A . n A 1 84 GLY 84 84 84 GLY GLY A . n A 1 85 SER 85 85 85 SER SER A . n A 1 86 ALA 86 86 86 ALA ALA A . n A 1 87 THR 87 87 87 THR THR A . n A 1 88 ILE 88 88 88 ILE ILE A . n A 1 89 LEU 89 89 89 LEU LEU A . n A 1 90 PRO 90 90 90 PRO PRO A . n A 1 91 GLY 91 91 91 GLY GLY A . n A 1 92 ASN 92 92 92 ASN ASN A . n A 1 93 ILE 93 93 93 ILE ILE A . n A 1 94 PRO 94 94 94 PRO PRO A . n A 1 95 ALA 95 95 95 ALA ALA A . n A 1 96 MET 96 96 96 MET MET A . n A 1 97 LEU 97 97 97 LEU LEU A . n A 1 98 TYR 98 98 98 TYR TYR A . n A 1 99 THR 99 99 99 THR THR A . n A 1 100 GLY 100 100 100 GLY GLY A . n A 1 101 SER 101 101 101 SER SER A . n A 1 102 ASP 102 102 102 ASP ASP A . n A 1 103 SER 103 103 103 SER SER A . n A 1 104 LYS 104 104 104 LYS LYS A . n A 1 105 SER 105 105 105 SER SER A . n A 1 106 ARG 106 106 106 ARG ARG A . n A 1 107 GLN 107 107 107 GLN GLN A . n A 1 108 VAL 108 108 108 VAL VAL A . n A 1 109 GLN 109 109 109 GLN GLN A . n A 1 110 ASP 110 110 110 ASP ASP A . n A 1 111 LEU 111 111 111 LEU LEU A . n A 1 112 ALA 112 112 112 ALA ALA A . n A 1 113 TRP 113 113 113 TRP TRP A . n A 1 114 PRO 114 114 114 PRO PRO A . n A 1 115 LYS 115 115 115 LYS LYS A . n A 1 116 ASN 116 116 116 ASN ASN A . n A 1 117 LEU 117 117 117 LEU LEU A . n A 1 118 SER 118 118 118 SER SER A . n A 1 119 ASP 119 119 119 ASP ASP A . n A 1 120 PRO 120 120 120 PRO PRO A . n A 1 121 PHE 121 121 121 PHE PHE A . n A 1 122 LEU 122 122 122 LEU LEU A . n A 1 123 ARG 123 123 123 ARG ARG A . n A 1 124 GLU 124 124 124 GLU GLU A . n A 1 125 TRP 125 125 125 TRP TRP A . n A 1 126 VAL 126 126 126 VAL VAL A . n A 1 127 LYS 127 127 127 LYS LYS A . n A 1 128 HIS 128 128 128 HIS HIS A . n A 1 129 PRO 129 129 129 PRO PRO A . n A 1 130 LYS 130 130 130 LYS LYS A . n A 1 131 ASN 131 131 131 ASN ASN A . n A 1 132 PRO 132 132 132 PRO PRO A . n A 1 133 LEU 133 133 133 LEU LEU A . n A 1 134 ILE 134 134 134 ILE ILE A . n A 1 135 THR 135 135 135 THR THR A . n A 1 136 PRO 136 136 136 PRO PRO A . n A 1 137 PRO 137 137 137 PRO PRO A . n A 1 138 GLU 138 138 138 GLU GLU A . n A 1 139 GLY 139 139 139 GLY GLY A . n A 1 140 VAL 140 140 140 VAL VAL A . n A 1 141 LYS 141 141 141 LYS LYS A . n A 1 142 ASP 142 142 142 ASP ASP A . n A 1 143 ASP 143 143 143 ASP ASP A . n A 1 144 CYS 144 144 144 CYS CYS A . n A 1 145 PHE 145 145 145 PHE PHE A . n A 1 146 ARG 146 146 146 ARG ARG A . n A 1 147 ASP 147 147 147 ASP ASP A . n A 1 148 PRO 148 148 148 PRO PRO A . n A 1 149 SER 149 149 149 SER SER A . n A 1 150 THR 150 150 150 THR THR A . n A 1 151 ALA 151 151 151 ALA ALA A . n A 1 152 TRP 152 152 152 TRP TRP A . n A 1 153 LEU 153 153 153 LEU LEU A . n A 1 154 GLY 154 154 154 GLY GLY A . n A 1 155 PRO 155 155 155 PRO PRO A . n A 1 156 ASP 156 156 156 ASP ASP A . n A 1 157 GLY 157 157 157 GLY GLY A . n A 1 158 VAL 158 158 158 VAL VAL A . n A 1 159 TRP 159 159 159 TRP TRP A . n A 1 160 ARG 160 160 160 ARG ARG A . n A 1 161 ILE 161 161 161 ILE ILE A . n A 1 162 VAL 162 162 162 VAL VAL A . n A 1 163 VAL 163 163 163 VAL VAL A . n A 1 164 GLY 164 164 164 GLY GLY A . n A 1 165 GLY 165 165 165 GLY GLY A . n A 1 166 ASP 166 166 166 ASP ASP A . n A 1 167 ARG 167 167 167 ARG ARG A . n A 1 168 ASP 168 168 168 ASP ASP A . n A 1 169 ASN 169 169 169 ASN ASN A . n A 1 170 ASN 170 170 170 ASN ASN A . n A 1 171 GLY 171 171 171 GLY GLY A . n A 1 172 MET 172 172 172 MET MET A . n A 1 173 ALA 173 173 173 ALA ALA A . n A 1 174 PHE 174 174 174 PHE PHE A . n A 1 175 LEU 175 175 175 LEU LEU A . n A 1 176 TYR 176 176 176 TYR TYR A . n A 1 177 GLN 177 177 177 GLN GLN A . n A 1 178 SER 178 178 178 SER SER A . n A 1 179 THR 179 179 179 THR THR A . n A 1 180 ASP 180 180 180 ASP ASP A . n A 1 181 PHE 181 181 181 PHE PHE A . n A 1 182 VAL 182 182 182 VAL VAL A . n A 1 183 ASN 183 183 183 ASN ASN A . n A 1 184 TRP 184 184 184 TRP TRP A . n A 1 185 LYS 185 185 185 LYS LYS A . n A 1 186 ARG 186 186 186 ARG ARG A . n A 1 187 TYR 187 187 187 TYR TYR A . n A 1 188 ASP 188 188 188 ASP ASP A . n A 1 189 GLN 189 189 189 GLN GLN A . n A 1 190 PRO 190 190 190 PRO PRO A . n A 1 191 LEU 191 191 191 LEU LEU A . n A 1 192 SER 192 192 192 SER SER A . n A 1 193 SER 193 193 193 SER SER A . n A 1 194 ALA 194 194 194 ALA ALA A . n A 1 195 ASP 195 195 195 ASP ASP A . n A 1 196 ALA 196 196 196 ALA ALA A . n A 1 197 THR 197 197 197 THR THR A . n A 1 198 GLY 198 198 198 GLY GLY A . n A 1 199 THR 199 199 199 THR THR A . n A 1 200 TRP 200 200 200 TRP TRP A . n A 1 201 GLU 201 201 201 GLU GLU A . n A 1 202 CYS 202 202 202 CYS CYS A . n A 1 203 PRO 203 203 203 PRO PRO A . n A 1 204 ASP 204 204 204 ASP ASP A . n A 1 205 PHE 205 205 205 PHE PHE A . n A 1 206 TYR 206 206 206 TYR TYR A . n A 1 207 PRO 207 207 207 PRO PRO A . n A 1 208 VAL 208 208 208 VAL VAL A . n A 1 209 PRO 209 209 209 PRO PRO A . n A 1 210 LEU 210 210 210 LEU LEU A . n A 1 211 ASN 211 211 211 ASN ASN A . n A 1 212 SER 212 212 212 SER SER A . n A 1 213 THR 213 213 213 THR THR A . n A 1 214 ASN 214 214 214 ASN ASN A . n A 1 215 GLY 215 215 215 GLY GLY A . n A 1 216 LEU 216 216 216 LEU LEU A . n A 1 217 ASP 217 217 217 ASP ASP A . n A 1 218 THR 218 218 218 THR THR A . n A 1 219 SER 219 219 219 SER SER A . n A 1 220 VAL 220 220 220 VAL VAL A . n A 1 221 TYR 221 221 221 TYR TYR A . n A 1 222 GLY 222 222 222 GLY GLY A . n A 1 223 GLY 223 223 223 GLY GLY A . n A 1 224 SER 224 224 224 SER SER A . n A 1 225 VAL 225 225 225 VAL VAL A . n A 1 226 ARG 226 226 226 ARG ARG A . n A 1 227 HIS 227 227 227 HIS HIS A . n A 1 228 VAL 228 228 228 VAL VAL A . n A 1 229 MET 229 229 229 MET MET A . n A 1 230 LYS 230 230 230 LYS LYS A . n A 1 231 ALA 231 231 231 ALA ALA A . n A 1 232 GLY 232 232 232 GLY GLY A . n A 1 233 PHE 233 233 233 PHE PHE A . n A 1 234 GLU 234 234 234 GLU GLU A . n A 1 235 GLY 235 235 235 GLY GLY A . n A 1 236 HIS 236 236 236 HIS HIS A . n A 1 237 ASP 237 237 237 ASP ASP A . n A 1 238 TRP 238 238 238 TRP TRP A . n A 1 239 TYR 239 239 239 TYR TYR A . n A 1 240 THR 240 240 240 THR THR A . n A 1 241 ILE 241 241 241 ILE ILE A . n A 1 242 GLY 242 242 242 GLY GLY A . n A 1 243 THR 243 243 243 THR THR A . n A 1 244 TYR 244 244 244 TYR TYR A . n A 1 245 SER 245 245 245 SER SER A . n A 1 246 PRO 246 246 246 PRO PRO A . n A 1 247 ASP 247 247 247 ASP ASP A . n A 1 248 ARG 248 248 248 ARG ARG A . n A 1 249 GLU 249 249 249 GLU GLU A . n A 1 250 ASN 250 250 250 ASN ASN A . n A 1 251 PHE 251 251 251 PHE PHE A . n A 1 252 LEU 252 252 252 LEU LEU A . n A 1 253 PRO 253 253 253 PRO PRO A . n A 1 254 GLN 254 254 254 GLN GLN A . n A 1 255 ASN 255 255 255 ASN ASN A . n A 1 256 GLY 256 256 256 GLY GLY A . n A 1 257 LEU 257 257 257 LEU LEU A . n A 1 258 SER 258 258 258 SER SER A . n A 1 259 LEU 259 259 259 LEU LEU A . n A 1 260 THR 260 260 260 THR THR A . n A 1 261 GLY 261 261 261 GLY GLY A . n A 1 262 SER 262 262 262 SER SER A . n A 1 263 THR 263 263 263 THR THR A . n A 1 264 LEU 264 264 264 LEU LEU A . n A 1 265 ASP 265 265 265 ASP ASP A . n A 1 266 LEU 266 266 266 LEU LEU A . n A 1 267 ARG 267 267 267 ARG ARG A . n A 1 268 TYR 268 268 268 TYR TYR A . n A 1 269 ASP 269 269 269 ASP ASP A . n A 1 270 TYR 270 270 270 TYR TYR A . n A 1 271 GLY 271 271 271 GLY GLY A . n A 1 272 GLN 272 272 272 GLN GLN A . n A 1 273 PHE 273 273 273 PHE PHE A . n A 1 274 TYR 274 274 274 TYR TYR A . n A 1 275 ALA 275 275 275 ALA ALA A . n A 1 276 SER 276 276 276 SER SER A . n A 1 277 LYS 277 277 277 LYS LYS A . n A 1 278 SER 278 278 278 SER SER A . n A 1 279 PHE 279 279 279 PHE PHE A . n A 1 280 PHE 280 280 280 PHE PHE A . n A 1 281 ASP 281 281 281 ASP ASP A . n A 1 282 ASP 282 282 282 ASP ASP A . n A 1 283 ALA 283 283 283 ALA ALA A . n A 1 284 LYS 284 284 284 LYS LYS A . n A 1 285 ASN 285 285 285 ASN ASN A . n A 1 286 ARG 286 286 286 ARG ARG A . n A 1 287 ARG 287 287 287 ARG ARG A . n A 1 288 VAL 288 288 288 VAL VAL A . n A 1 289 LEU 289 289 289 LEU LEU A . n A 1 290 TRP 290 290 290 TRP TRP A . n A 1 291 ALA 291 291 291 ALA ALA A . n A 1 292 TRP 292 292 292 TRP TRP A . n A 1 293 VAL 293 293 293 VAL VAL A . n A 1 294 PRO 294 294 294 PRO PRO A . n A 1 295 GLU 295 295 295 GLU GLU A . n A 1 296 THR 296 296 296 THR THR A . n A 1 297 ASP 297 297 297 ASP ASP A . n A 1 298 SER 298 298 298 SER SER A . n A 1 299 GLN 299 299 299 GLN GLN A . n A 1 300 ALA 300 300 300 ALA ALA A . n A 1 301 ASP 301 301 301 ASP ASP A . n A 1 302 ASP 302 302 302 ASP ASP A . n A 1 303 ILE 303 303 303 ILE ILE A . n A 1 304 GLU 304 304 304 GLU GLU A . n A 1 305 LYS 305 305 305 LYS LYS A . n A 1 306 GLY 306 306 306 GLY GLY A . n A 1 307 TRP 307 307 307 TRP TRP A . n A 1 308 ALA 308 308 308 ALA ALA A . n A 1 309 GLY 309 309 309 GLY GLY A . n A 1 310 LEU 310 310 310 LEU LEU A . n A 1 311 GLN 311 311 311 GLN GLN A . n A 1 312 SER 312 312 312 SER SER A . n A 1 313 PHE 313 313 313 PHE PHE A . n A 1 314 PRO 314 314 314 PRO PRO A . n A 1 315 ARG 315 315 315 ARG ARG A . n A 1 316 ALA 316 316 316 ALA ALA A . n A 1 317 LEU 317 317 317 LEU LEU A . n A 1 318 TRP 318 318 318 TRP TRP A . n A 1 319 ILE 319 319 319 ILE ILE A . n A 1 320 ASP 320 320 320 ASP ASP A . n A 1 321 ARG 321 321 321 ARG ARG A . n A 1 322 ASN 322 322 322 ASN ASN A . n A 1 323 GLY 323 323 323 GLY GLY A . n A 1 324 LYS 324 324 324 LYS LYS A . n A 1 325 GLN 325 325 325 GLN GLN A . n A 1 326 LEU 326 326 326 LEU LEU A . n A 1 327 ILE 327 327 327 ILE ILE A . n A 1 328 GLN 328 328 328 GLN GLN A . n A 1 329 TRP 329 329 329 TRP TRP A . n A 1 330 PRO 330 330 330 PRO PRO A . n A 1 331 VAL 331 331 331 VAL VAL A . n A 1 332 GLU 332 332 332 GLU GLU A . n A 1 333 GLU 333 333 333 GLU GLU A . n A 1 334 ILE 334 334 334 ILE ILE A . n A 1 335 GLU 335 335 335 GLU GLU A . n A 1 336 GLU 336 336 336 GLU GLU A . n A 1 337 LEU 337 337 337 LEU LEU A . n A 1 338 ARG 338 338 338 ARG ARG A . n A 1 339 GLN 339 339 339 GLN GLN A . n A 1 340 ASN 340 340 340 ASN ASN A . n A 1 341 GLN 341 341 341 GLN GLN A . n A 1 342 VAL 342 342 342 VAL VAL A . n A 1 343 ASN 343 343 343 ASN ASN A . n A 1 344 LEU 344 344 344 LEU LEU A . n A 1 345 GLN 345 345 345 GLN GLN A . n A 1 346 ASN 346 346 346 ASN ASN A . n A 1 347 LYS 347 347 347 LYS LYS A . n A 1 348 ASN 348 348 348 ASN ASN A . n A 1 349 LEU 349 349 349 LEU LEU A . n A 1 350 LYS 350 350 350 LYS LYS A . n A 1 351 PRO 351 351 351 PRO PRO A . n A 1 352 GLY 352 352 352 GLY GLY A . n A 1 353 SER 353 353 353 SER SER A . n A 1 354 VAL 354 354 354 VAL VAL A . n A 1 355 LEU 355 355 355 LEU LEU A . n A 1 356 GLU 356 356 356 GLU GLU A . n A 1 357 ILE 357 357 357 ILE ILE A . n A 1 358 HIS 358 358 358 HIS HIS A . n A 1 359 GLY 359 359 359 GLY GLY A . n A 1 360 ILE 360 360 360 ILE ILE A . n A 1 361 ALA 361 361 361 ALA ALA A . n A 1 362 ALA 362 362 362 ALA ALA A . n A 1 363 SER 363 363 363 SER SER A . n A 1 364 GLN 364 364 364 GLN GLN A . n A 1 365 ALA 365 365 365 ALA ALA A . n A 1 366 ASP 366 366 366 ASP ASP A . n A 1 367 VAL 367 367 367 VAL VAL A . n A 1 368 THR 368 368 368 THR THR A . n A 1 369 ILE 369 369 369 ILE ILE A . n A 1 370 SER 370 370 370 SER SER A . n A 1 371 PHE 371 371 371 PHE PHE A . n A 1 372 LYS 372 372 372 LYS LYS A . n A 1 373 LEU 373 373 373 LEU LEU A . n A 1 374 GLU 374 374 374 GLU GLU A . n A 1 375 GLY 375 375 375 GLY GLY A . n A 1 376 LEU 376 376 376 LEU LEU A . n A 1 377 LYS 377 377 377 LYS LYS A . n A 1 378 GLU 378 378 378 GLU GLU A . n A 1 379 ALA 379 379 379 ALA ALA A . n A 1 380 GLU 380 380 380 GLU GLU A . n A 1 381 VAL 381 381 381 VAL VAL A . n A 1 382 LEU 382 382 382 LEU LEU A . n A 1 383 ASP 383 383 383 ASP ASP A . n A 1 384 THR 384 384 384 THR THR A . n A 1 385 THR 385 385 385 THR THR A . n A 1 386 LEU 386 386 386 LEU LEU A . n A 1 387 VAL 387 387 387 VAL VAL A . n A 1 388 ASP 388 388 388 ASP ASP A . n A 1 389 PRO 389 389 389 PRO PRO A . n A 1 390 GLN 390 390 390 GLN GLN A . n A 1 391 ALA 391 391 391 ALA ALA A . n A 1 392 LEU 392 392 392 LEU LEU A . n A 1 393 CYS 393 393 393 CYS CYS A . n A 1 394 ASN 394 394 394 ASN ASN A . n A 1 395 GLU 395 395 395 GLU GLU A . n A 1 396 ARG 396 396 396 ARG ARG A . n A 1 397 GLY 397 397 397 GLY GLY A . n A 1 398 ALA 398 398 398 ALA ALA A . n A 1 399 SER 399 399 399 SER SER A . n A 1 400 SER 400 400 400 SER SER A . n A 1 401 ARG 401 401 401 ARG ARG A . n A 1 402 GLY 402 402 402 GLY GLY A . n A 1 403 ALA 403 403 403 ALA ALA A . n A 1 404 LEU 404 404 404 LEU LEU A . n A 1 405 GLY 405 405 405 GLY GLY A . n A 1 406 PRO 406 406 406 PRO PRO A . n A 1 407 PHE 407 407 407 PHE PHE A . n A 1 408 GLY 408 408 408 GLY GLY A . n A 1 409 LEU 409 409 409 LEU LEU A . n A 1 410 LEU 410 410 410 LEU LEU A . n A 1 411 ALA 411 411 411 ALA ALA A . n A 1 412 MET 412 412 412 MET MET A . n A 1 413 ALA 413 413 413 ALA ALA A . n A 1 414 SER 414 414 414 SER SER A . n A 1 415 LYS 415 415 415 LYS LYS A . n A 1 416 ASP 416 416 416 ASP ASP A . n A 1 417 LEU 417 417 417 LEU LEU A . n A 1 418 LYS 418 418 418 LYS LYS A . n A 1 419 GLU 419 419 419 GLU GLU A . n A 1 420 GLN 420 420 420 GLN GLN A . n A 1 421 SER 421 421 421 SER SER A . n A 1 422 ALA 422 422 422 ALA ALA A . n A 1 423 ILE 423 423 423 ILE ILE A . n A 1 424 PHE 424 424 424 PHE PHE A . n A 1 425 PHE 425 425 425 PHE PHE A . n A 1 426 ARG 426 426 426 ARG ARG A . n A 1 427 VAL 427 427 427 VAL VAL A . n A 1 428 PHE 428 428 428 PHE PHE A . n A 1 429 GLN 429 429 429 GLN GLN A . n A 1 430 ASN 430 430 430 ASN ASN A . n A 1 431 GLN 431 431 431 GLN GLN A . n A 1 432 LEU 432 432 432 LEU LEU A . n A 1 433 GLY 433 433 433 GLY GLY A . n A 1 434 ARG 434 434 434 ARG ARG A . n A 1 435 TYR 435 435 435 TYR TYR A . n A 1 436 SER 436 436 436 SER SER A . n A 1 437 VAL 437 437 437 VAL VAL A . n A 1 438 LEU 438 438 438 LEU LEU A . n A 1 439 MET 439 439 439 MET MET A . n A 1 440 CYS 440 440 440 CYS CYS A . n A 1 441 SER 441 441 441 SER SER A . n A 1 442 ASP 442 442 442 ASP ASP A . n A 1 443 LEU 443 443 443 LEU LEU A . n A 1 444 SER 444 444 444 SER SER 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 THR 447 447 447 THR THR A . n A 1 448 VAL 448 448 448 VAL VAL A . n A 1 449 ARG 449 449 449 ARG ARG A . n A 1 450 SER 450 450 450 SER SER A . n A 1 451 ASN 451 451 451 ASN ASN A . n A 1 452 ILE 452 452 452 ILE ILE A . n A 1 453 ASP 453 453 453 ASP ASP A . n A 1 454 THR 454 454 454 THR THR A . n A 1 455 THR 455 455 455 THR THR A . n A 1 456 SER 456 456 456 SER SER A . n A 1 457 TYR 457 457 457 TYR TYR A . n A 1 458 GLY 458 458 458 GLY GLY A . n A 1 459 ALA 459 459 459 ALA ALA A . n A 1 460 PHE 460 460 460 PHE PHE A . n A 1 461 VAL 461 461 461 VAL VAL A . n A 1 462 ASP 462 462 462 ASP ASP A . n A 1 463 ILE 463 463 463 ILE ILE A . n A 1 464 ASP 464 464 464 ASP ASP A . n A 1 465 PRO 465 465 465 PRO PRO A . n A 1 466 ARG 466 466 466 ARG ARG A . n A 1 467 SER 467 467 467 SER SER A . n A 1 468 GLU 468 468 468 GLU GLU A . n A 1 469 GLU 469 469 469 GLU GLU A . n A 1 470 ILE 470 470 470 ILE ILE A . n A 1 471 SER 471 471 471 SER SER A . n A 1 472 LEU 472 472 472 LEU LEU A . n A 1 473 ARG 473 473 473 ARG ARG A . n A 1 474 ASN 474 474 474 ASN ASN A . n A 1 475 LEU 475 475 475 LEU LEU A . n A 1 476 ILE 476 476 476 ILE ILE A . n A 1 477 ASP 477 477 477 ASP ASP A . n A 1 478 HIS 478 478 478 HIS HIS A . n A 1 479 SER 479 479 479 SER SER A . n A 1 480 ILE 480 480 480 ILE ILE A . n A 1 481 ILE 481 481 481 ILE ILE A . n A 1 482 GLU 482 482 482 GLU GLU A . n A 1 483 SER 483 483 483 SER SER A . n A 1 484 PHE 484 484 484 PHE PHE A . n A 1 485 GLY 485 485 485 GLY GLY A . n A 1 486 ALA 486 486 486 ALA ALA A . n A 1 487 GLY 487 487 487 GLY GLY A . n A 1 488 GLY 488 488 488 GLY GLY A . n A 1 489 LYS 489 489 489 LYS LYS A . n A 1 490 THR 490 490 490 THR THR A . n A 1 491 CYS 491 491 491 CYS CYS A . n A 1 492 ILE 492 492 492 ILE ILE A . n A 1 493 THR 493 493 493 THR THR A . n A 1 494 SER 494 494 494 SER SER A . n A 1 495 ARG 495 495 495 ARG ARG A . n A 1 496 ILE 496 496 496 ILE ILE A . n A 1 497 TYR 497 497 497 TYR TYR A . n A 1 498 PRO 498 498 498 PRO PRO A . n A 1 499 LYS 499 499 499 LYS LYS A . n A 1 500 PHE 500 500 500 PHE PHE A . n A 1 501 VAL 501 501 501 VAL VAL A . n A 1 502 ASN 502 502 502 ASN ASN A . n A 1 503 ASN 503 503 503 ASN ASN A . n A 1 504 GLU 504 504 504 GLU GLU A . n A 1 505 GLU 505 505 505 GLU GLU A . n A 1 506 ALA 506 506 506 ALA ALA A . n A 1 507 HIS 507 507 507 HIS HIS A . n A 1 508 LEU 508 508 508 LEU LEU A . n A 1 509 PHE 509 509 509 PHE PHE A . n A 1 510 VAL 510 510 510 VAL VAL A . n A 1 511 PHE 511 511 511 PHE PHE A . n A 1 512 ASN 512 512 512 ASN ASN A . n A 1 513 ASN 513 513 513 ASN ASN A . n A 1 514 GLY 514 514 514 GLY GLY A . n A 1 515 THR 515 515 515 THR THR A . n A 1 516 GLN 516 516 516 GLN GLN A . n A 1 517 ASN 517 517 517 ASN ASN A . n A 1 518 VAL 518 518 518 VAL VAL A . n A 1 519 LYS 519 519 519 LYS LYS A . n A 1 520 ILE 520 520 520 ILE ILE A . n A 1 521 SER 521 521 521 SER SER A . n A 1 522 GLU 522 522 522 GLU GLU A . n A 1 523 MET 523 523 523 MET MET A . n A 1 524 SER 524 524 524 SER SER A . n A 1 525 ALA 525 525 525 ALA ALA A . n A 1 526 TRP 526 526 526 TRP TRP A . n A 1 527 SER 527 527 527 SER SER A . n A 1 528 MET 528 528 528 MET MET A . n A 1 529 LYS 529 529 529 LYS LYS A . n A 1 530 ASN 530 530 530 ASN ASN A . n A 1 531 ALA 531 531 531 ALA ALA A . n A 1 532 LYS 532 532 532 LYS LYS A . n A 1 533 PHE 533 533 533 PHE PHE A . n A 1 534 VAL 534 534 534 VAL VAL A . n A 1 535 VAL 535 535 535 VAL VAL A . n A 1 536 ASP 536 536 536 ASP ASP A . n A 1 537 GLN 537 537 537 GLN GLN A . n A 1 538 SER 538 538 538 SER SER A . n A 1 539 VAL 539 539 ? ? ? A . n A 1 540 LYS 540 540 ? ? ? A . n A 1 541 SER 541 541 ? ? ? A . n A 1 542 ALA 542 542 ? ? ? A . n A 1 543 ALA 543 543 ? ? ? A . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code B 2 NDG 1 650 650 NDG NAG A . C 3 NAG 2 660 660 NAG NAG A . D 4 MAN 3 670 670 MAN MAN A . E 3 NAG 1 680 680 NAG NAG A . F 3 NAG 2 690 690 NAG NAG A . G 5 GOL 1 1758 1758 GOL GOL A . H 5 GOL 1 1759 1759 GOL GOL A . I 5 GOL 1 1760 1760 GOL GOL A . J 5 GOL 1 1772 1772 GOL GOL A . K 6 HOH 1 1000 1000 HOH TIP A . K 6 HOH 2 1001 1001 HOH TIP A . K 6 HOH 3 1002 1002 HOH TIP A . K 6 HOH 4 1003 1003 HOH TIP A . K 6 HOH 5 1004 1004 HOH TIP A . K 6 HOH 6 1005 1005 HOH TIP A . K 6 HOH 7 1006 1006 HOH TIP A . K 6 HOH 8 1007 1007 HOH TIP A . K 6 HOH 9 1008 1008 HOH TIP A . K 6 HOH 10 1009 1009 HOH TIP A . K 6 HOH 11 1010 1010 HOH TIP A . K 6 HOH 12 1011 1011 HOH TIP A . K 6 HOH 13 1012 1012 HOH TIP A . K 6 HOH 14 1013 1013 HOH TIP A . K 6 HOH 15 1014 1014 HOH TIP A . K 6 HOH 16 1015 1015 HOH TIP A . K 6 HOH 17 1016 1016 HOH TIP A . K 6 HOH 18 1017 1017 HOH TIP A . K 6 HOH 19 1018 1018 HOH TIP A . K 6 HOH 20 1019 1019 HOH TIP A . K 6 HOH 21 1020 1020 HOH TIP A . K 6 HOH 22 1021 1021 HOH TIP A . K 6 HOH 23 1022 1022 HOH TIP A . K 6 HOH 24 1023 1023 HOH TIP A . K 6 HOH 25 1024 1024 HOH TIP A . K 6 HOH 26 1025 1025 HOH TIP A . K 6 HOH 27 1026 1026 HOH TIP A . K 6 HOH 28 1027 1027 HOH TIP A . K 6 HOH 29 1028 1028 HOH TIP A . K 6 HOH 30 1029 1029 HOH TIP A . K 6 HOH 31 1030 1030 HOH TIP A . K 6 HOH 32 1031 1031 HOH TIP A . K 6 HOH 33 1032 1032 HOH TIP A . K 6 HOH 34 1033 1033 HOH TIP A . K 6 HOH 35 1034 1034 HOH TIP A . K 6 HOH 36 1035 1035 HOH TIP A . K 6 HOH 37 1036 1036 HOH TIP A . K 6 HOH 38 1037 1037 HOH TIP A . K 6 HOH 39 1038 1038 HOH TIP A . K 6 HOH 40 1039 1039 HOH TIP A . K 6 HOH 41 1040 1040 HOH TIP A . K 6 HOH 42 1041 1041 HOH TIP A . K 6 HOH 43 1042 1042 HOH TIP A . K 6 HOH 44 1043 1043 HOH TIP A . K 6 HOH 45 1044 1044 HOH TIP A . K 6 HOH 46 1045 1045 HOH TIP A . K 6 HOH 47 1047 1047 HOH TIP A . K 6 HOH 48 1048 1048 HOH TIP A . K 6 HOH 49 1049 1049 HOH TIP A . K 6 HOH 50 1050 1050 HOH TIP A . K 6 HOH 51 1051 1051 HOH TIP A . K 6 HOH 52 1052 1052 HOH TIP A . K 6 HOH 53 1053 1053 HOH TIP A . K 6 HOH 54 1054 1054 HOH TIP A . K 6 HOH 55 1055 1055 HOH TIP A . K 6 HOH 56 1056 1056 HOH TIP A . K 6 HOH 57 1057 1057 HOH TIP A . K 6 HOH 58 1058 1058 HOH TIP A . K 6 HOH 59 1059 1059 HOH TIP A . K 6 HOH 60 1060 1060 HOH TIP A . K 6 HOH 61 1061 1061 HOH TIP A . K 6 HOH 62 1062 1062 HOH TIP A . K 6 HOH 63 1063 1063 HOH TIP A . K 6 HOH 64 1064 1064 HOH TIP A . K 6 HOH 65 1065 1065 HOH TIP A . K 6 HOH 66 1066 1066 HOH TIP A . K 6 HOH 67 1067 1067 HOH TIP A . K 6 HOH 68 1068 1068 HOH TIP A . K 6 HOH 69 1069 1069 HOH TIP A . K 6 HOH 70 1070 1070 HOH TIP A . K 6 HOH 71 1071 1071 HOH TIP A . K 6 HOH 72 1072 1072 HOH TIP A . K 6 HOH 73 1073 1073 HOH TIP A . K 6 HOH 74 1074 1074 HOH TIP A . K 6 HOH 75 1075 1075 HOH TIP A . K 6 HOH 76 1076 1076 HOH TIP A . K 6 HOH 77 1077 1077 HOH TIP A . K 6 HOH 78 1078 1078 HOH TIP A . K 6 HOH 79 1079 1079 HOH TIP A . K 6 HOH 80 1080 1080 HOH TIP A . K 6 HOH 81 1082 1082 HOH TIP A . K 6 HOH 82 1083 1083 HOH TIP A . K 6 HOH 83 1084 1084 HOH TIP A . K 6 HOH 84 1085 1085 HOH TIP A . K 6 HOH 85 1086 1086 HOH TIP A . K 6 HOH 86 1087 1087 HOH TIP A . K 6 HOH 87 1088 1088 HOH TIP A . K 6 HOH 88 1089 1089 HOH TIP A . K 6 HOH 89 1090 1090 HOH TIP A . K 6 HOH 90 1091 1091 HOH TIP A . K 6 HOH 91 1092 1092 HOH TIP A . K 6 HOH 92 1093 1093 HOH TIP A . K 6 HOH 93 1094 1094 HOH TIP A . K 6 HOH 94 1095 1095 HOH TIP A . K 6 HOH 95 1096 1096 HOH TIP A . K 6 HOH 96 1097 1097 HOH TIP A . K 6 HOH 97 1098 1098 HOH TIP A . K 6 HOH 98 1099 1099 HOH TIP A . K 6 HOH 99 1100 1100 HOH TIP A . K 6 HOH 100 1101 1101 HOH TIP A . K 6 HOH 101 1102 1102 HOH TIP A . K 6 HOH 102 1103 1103 HOH TIP A . K 6 HOH 103 1104 1104 HOH TIP A . K 6 HOH 104 1105 1105 HOH TIP A . K 6 HOH 105 1106 1106 HOH TIP A . K 6 HOH 106 1107 1107 HOH TIP A . K 6 HOH 107 1108 1108 HOH TIP A . K 6 HOH 108 1109 1109 HOH TIP A . K 6 HOH 109 1110 1110 HOH TIP A . K 6 HOH 110 1111 1111 HOH TIP A . K 6 HOH 111 1112 1112 HOH TIP A . K 6 HOH 112 1113 1113 HOH TIP A . K 6 HOH 113 1114 1114 HOH TIP A . K 6 HOH 114 1115 1115 HOH TIP A . K 6 HOH 115 1116 1116 HOH TIP A . K 6 HOH 116 1117 1117 HOH TIP A . K 6 HOH 117 1118 1118 HOH TIP A . K 6 HOH 118 1119 1119 HOH TIP A . K 6 HOH 119 1120 1120 HOH TIP A . K 6 HOH 120 1121 1121 HOH TIP A . K 6 HOH 121 1122 1122 HOH TIP A . K 6 HOH 122 1123 1123 HOH TIP A . K 6 HOH 123 1124 1124 HOH TIP A . K 6 HOH 124 1125 1125 HOH TIP A . K 6 HOH 125 1126 1126 HOH TIP A . K 6 HOH 126 1127 1127 HOH TIP A . K 6 HOH 127 1128 1128 HOH TIP A . K 6 HOH 128 1129 1129 HOH TIP A . K 6 HOH 129 1130 1130 HOH TIP A . K 6 HOH 130 1131 1131 HOH TIP A . K 6 HOH 131 1132 1132 HOH TIP A . K 6 HOH 132 1133 1133 HOH TIP A . K 6 HOH 133 1134 1134 HOH TIP A . K 6 HOH 134 1135 1135 HOH TIP A . K 6 HOH 135 1136 1136 HOH TIP A . K 6 HOH 136 1137 1137 HOH TIP A . K 6 HOH 137 1138 1138 HOH TIP A . K 6 HOH 138 1139 1139 HOH TIP A . K 6 HOH 139 1140 1140 HOH TIP A . K 6 HOH 140 1141 1141 HOH TIP A . K 6 HOH 141 1142 1142 HOH TIP A . K 6 HOH 142 1143 1143 HOH TIP A . K 6 HOH 143 1144 1144 HOH TIP A . K 6 HOH 144 1145 1145 HOH TIP A . K 6 HOH 145 1146 1146 HOH TIP A . K 6 HOH 146 1147 1147 HOH TIP A . K 6 HOH 147 1148 1148 HOH TIP A . K 6 HOH 148 1149 1149 HOH TIP A . K 6 HOH 149 1150 1150 HOH TIP A . K 6 HOH 150 1151 1151 HOH TIP A . K 6 HOH 151 1152 1152 HOH TIP A . K 6 HOH 152 1153 1153 HOH TIP A . K 6 HOH 153 1154 1154 HOH TIP A . K 6 HOH 154 1155 1155 HOH TIP A . K 6 HOH 155 1156 1156 HOH TIP A . K 6 HOH 156 1157 1157 HOH TIP A . K 6 HOH 157 1158 1158 HOH TIP A . K 6 HOH 158 1159 1159 HOH TIP A . K 6 HOH 159 1160 1160 HOH TIP A . K 6 HOH 160 1161 1161 HOH TIP A . K 6 HOH 161 1162 1162 HOH TIP A . K 6 HOH 162 1163 1163 HOH TIP A . K 6 HOH 163 1164 1164 HOH TIP A . K 6 HOH 164 1165 1165 HOH TIP A . K 6 HOH 165 1166 1166 HOH TIP A . K 6 HOH 166 1167 1167 HOH TIP A . K 6 HOH 167 1168 1168 HOH TIP A . K 6 HOH 168 1169 1169 HOH TIP A . K 6 HOH 169 1170 1170 HOH TIP A . K 6 HOH 170 1171 1171 HOH TIP A . K 6 HOH 171 1172 1172 HOH TIP A . K 6 HOH 172 1173 1173 HOH TIP A . K 6 HOH 173 1174 1174 HOH TIP A . K 6 HOH 174 1175 1175 HOH TIP A . K 6 HOH 175 1176 1176 HOH TIP A . K 6 HOH 176 1177 1177 HOH TIP A . K 6 HOH 177 1178 1178 HOH TIP A . K 6 HOH 178 1179 1179 HOH TIP A . K 6 HOH 179 1181 1181 HOH TIP A . K 6 HOH 180 1182 1182 HOH TIP A . K 6 HOH 181 1183 1183 HOH TIP A . K 6 HOH 182 1184 1184 HOH TIP A . K 6 HOH 183 1185 1185 HOH TIP A . K 6 HOH 184 1186 1186 HOH TIP A . K 6 HOH 185 1187 1187 HOH TIP A . K 6 HOH 186 1188 1188 HOH TIP A . K 6 HOH 187 1189 1189 HOH TIP A . K 6 HOH 188 1190 1190 HOH TIP A . K 6 HOH 189 1191 1191 HOH TIP A . K 6 HOH 190 1192 1192 HOH TIP A . K 6 HOH 191 1193 1193 HOH TIP A . K 6 HOH 192 1194 1194 HOH TIP A . K 6 HOH 193 1195 1195 HOH TIP A . K 6 HOH 194 1196 1196 HOH TIP A . K 6 HOH 195 1197 1197 HOH TIP A . K 6 HOH 196 1198 1198 HOH TIP A . K 6 HOH 197 1199 1199 HOH TIP A . K 6 HOH 198 1200 1200 HOH TIP A . K 6 HOH 199 1201 1201 HOH TIP A . K 6 HOH 200 1202 1202 HOH TIP A . K 6 HOH 201 1203 1203 HOH TIP A . K 6 HOH 202 1204 1204 HOH TIP A . K 6 HOH 203 1205 1205 HOH TIP A . K 6 HOH 204 1206 1206 HOH TIP A . K 6 HOH 205 1207 1207 HOH TIP A . K 6 HOH 206 1208 1208 HOH TIP A . K 6 HOH 207 1209 1209 HOH TIP A . K 6 HOH 208 1210 1210 HOH TIP A . K 6 HOH 209 1211 1211 HOH TIP A . K 6 HOH 210 1212 1212 HOH TIP A . K 6 HOH 211 1213 1213 HOH TIP A . K 6 HOH 212 1214 1214 HOH TIP A . K 6 HOH 213 1215 1215 HOH TIP A . K 6 HOH 214 1216 1216 HOH TIP A . K 6 HOH 215 1217 1217 HOH TIP A . K 6 HOH 216 1218 1218 HOH TIP A . K 6 HOH 217 1219 1219 HOH TIP A . K 6 HOH 218 1220 1220 HOH TIP A . K 6 HOH 219 1221 1221 HOH TIP A . K 6 HOH 220 1222 1222 HOH TIP A . K 6 HOH 221 1223 1223 HOH TIP A . K 6 HOH 222 1224 1224 HOH TIP A . K 6 HOH 223 1225 1225 HOH TIP A . K 6 HOH 224 1226 1226 HOH TIP A . K 6 HOH 225 1227 1227 HOH TIP A . K 6 HOH 226 1228 1228 HOH TIP A . K 6 HOH 227 1229 1229 HOH TIP A . K 6 HOH 228 1230 1230 HOH TIP A . K 6 HOH 229 1231 1231 HOH TIP A . K 6 HOH 230 1232 1232 HOH TIP A . K 6 HOH 231 1233 1233 HOH TIP A . K 6 HOH 232 1234 1234 HOH TIP A . K 6 HOH 233 1235 1235 HOH TIP A . K 6 HOH 234 1236 1236 HOH TIP A . K 6 HOH 235 1237 1237 HOH TIP A . K 6 HOH 236 1238 1238 HOH TIP A . K 6 HOH 237 1239 1239 HOH TIP A . K 6 HOH 238 1240 1240 HOH TIP A . K 6 HOH 239 1241 1241 HOH TIP A . K 6 HOH 240 1242 1242 HOH TIP A . K 6 HOH 241 1243 1243 HOH TIP A . K 6 HOH 242 1244 1244 HOH TIP A . K 6 HOH 243 1245 1245 HOH TIP A . K 6 HOH 244 1246 1246 HOH TIP A . K 6 HOH 245 1247 1247 HOH TIP A . K 6 HOH 246 1248 1248 HOH TIP A . K 6 HOH 247 1249 1249 HOH TIP A . K 6 HOH 248 1250 1250 HOH TIP A . K 6 HOH 249 1251 1251 HOH TIP A . K 6 HOH 250 1252 1252 HOH TIP A . K 6 HOH 251 1253 1253 HOH TIP A . K 6 HOH 252 1254 1254 HOH TIP A . K 6 HOH 253 1255 1255 HOH TIP A . K 6 HOH 254 1256 1256 HOH TIP A . K 6 HOH 255 1257 1257 HOH TIP A . K 6 HOH 256 1258 1258 HOH TIP A . K 6 HOH 257 1259 1259 HOH TIP A . K 6 HOH 258 1260 1260 HOH TIP A . K 6 HOH 259 1261 1261 HOH TIP A . K 6 HOH 260 1262 1262 HOH TIP A . K 6 HOH 261 1263 1263 HOH TIP A . K 6 HOH 262 1264 1264 HOH TIP A . K 6 HOH 263 1265 1265 HOH TIP A . K 6 HOH 264 1266 1266 HOH TIP A . K 6 HOH 265 1267 1267 HOH TIP A . K 6 HOH 266 1268 1268 HOH TIP A . K 6 HOH 267 1269 1269 HOH TIP A . K 6 HOH 268 1270 1270 HOH TIP A . K 6 HOH 269 1271 1271 HOH TIP A . K 6 HOH 270 1272 1272 HOH TIP A . K 6 HOH 271 1273 1273 HOH TIP A . K 6 HOH 272 1274 1274 HOH TIP A . K 6 HOH 273 1275 1275 HOH TIP A . K 6 HOH 274 1276 1276 HOH TIP A . K 6 HOH 275 1277 1277 HOH TIP A . K 6 HOH 276 1278 1278 HOH TIP A . K 6 HOH 277 1279 1279 HOH TIP A . K 6 HOH 278 1280 1280 HOH TIP A . K 6 HOH 279 1281 1281 HOH TIP A . K 6 HOH 280 1282 1282 HOH TIP A . K 6 HOH 281 1283 1283 HOH TIP A . K 6 HOH 282 1284 1284 HOH TIP A . K 6 HOH 283 1285 1285 HOH TIP A . K 6 HOH 284 1286 1286 HOH TIP A . K 6 HOH 285 1287 1287 HOH TIP A . K 6 HOH 286 1288 1288 HOH TIP A . K 6 HOH 287 1289 1289 HOH TIP A . K 6 HOH 288 1290 1290 HOH TIP A . K 6 HOH 289 1291 1291 HOH TIP A . K 6 HOH 290 1292 1292 HOH TIP A . K 6 HOH 291 1293 1293 HOH TIP A . K 6 HOH 292 1294 1294 HOH TIP A . K 6 HOH 293 1295 1295 HOH TIP A . K 6 HOH 294 1296 1296 HOH TIP A . K 6 HOH 295 1297 1297 HOH TIP A . K 6 HOH 296 1298 1298 HOH TIP A . K 6 HOH 297 1299 1299 HOH TIP A . K 6 HOH 298 1300 1300 HOH TIP A . K 6 HOH 299 1301 1301 HOH TIP A . K 6 HOH 300 1302 1302 HOH TIP A . K 6 HOH 301 1303 1303 HOH TIP A . K 6 HOH 302 1304 1304 HOH TIP A . K 6 HOH 303 1305 1305 HOH TIP A . K 6 HOH 304 1306 1306 HOH TIP A . K 6 HOH 305 1307 1307 HOH TIP A . K 6 HOH 306 1308 1308 HOH TIP A . K 6 HOH 307 1309 1309 HOH TIP A . K 6 HOH 308 1310 1310 HOH TIP A . K 6 HOH 309 1311 1311 HOH TIP A . K 6 HOH 310 1312 1312 HOH TIP A . K 6 HOH 311 1313 1313 HOH TIP A . K 6 HOH 312 1314 1314 HOH TIP A . K 6 HOH 313 1315 1315 HOH TIP A . K 6 HOH 314 1316 1316 HOH TIP A . K 6 HOH 315 1317 1317 HOH TIP A . K 6 HOH 316 1318 1318 HOH TIP A . K 6 HOH 317 1319 1319 HOH TIP A . K 6 HOH 318 1320 1320 HOH TIP A . K 6 HOH 319 1321 1321 HOH TIP A . K 6 HOH 320 1322 1322 HOH TIP A . K 6 HOH 321 1323 1323 HOH TIP A . K 6 HOH 322 1324 1324 HOH TIP A . K 6 HOH 323 1325 1325 HOH TIP A . K 6 HOH 324 1326 1326 HOH TIP A . K 6 HOH 325 1327 1327 HOH TIP A . K 6 HOH 326 1328 1328 HOH TIP A . K 6 HOH 327 1329 1329 HOH TIP A . K 6 HOH 328 1330 1330 HOH TIP A . K 6 HOH 329 1331 1331 HOH TIP A . K 6 HOH 330 1332 1332 HOH TIP A . K 6 HOH 331 1333 1333 HOH TIP A . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 116 A ASN 116 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 513 A ASN 513 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_defined_assembly _pdbx_struct_assembly.method_details ? _pdbx_struct_assembly.oligomeric_details monomeric _pdbx_struct_assembly.oligomeric_count 1 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # 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 2005-03-01 2 'Structure model' 1 1 2008-04-29 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.classification _software.version _software.citation_id _software.pdbx_ordinal CNS refinement 1.1 ? 1 DENZO 'data reduction' . ? 2 SCALEPACK 'data scaling' . ? 3 SHARP phasing . ? 4 # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 ASN A 18 ? ? 73.41 -170.25 2 1 ASN A 21 ? ? -125.85 -122.37 3 1 ASP A 22 ? ? -37.75 133.84 4 1 THR A 73 ? ? -141.29 -8.33 5 1 ASP A 77 ? ? -151.76 23.95 6 1 SER A 80 ? ? 169.67 157.18 7 1 SER A 83 ? ? -49.30 151.10 8 1 LEU A 122 ? ? 37.92 61.10 9 1 ASP A 147 ? ? 62.10 67.85 10 1 THR A 263 ? ? -62.52 0.80 11 1 GLN A 339 ? ? -105.86 -112.93 12 1 HIS A 478 ? ? 59.66 -94.68 13 1 GLN A 537 ? ? -114.52 -158.13 # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A GLN 1 ? A GLN 1 2 1 Y 1 A VAL 539 ? A VAL 539 3 1 Y 1 A LYS 540 ? A LYS 540 4 1 Y 1 A SER 541 ? A SER 541 5 1 Y 1 A ALA 542 ? A ALA 542 6 1 Y 1 A ALA 543 ? A ALA 543 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' NDG 3 N-ACETYL-D-GLUCOSAMINE NAG 4 ALPHA-D-MANNOSE MAN 5 GLYCEROL GOL 6 water HOH #