data_2YP7 # _entry.id 2YP7 # _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 2YP7 PDBE EBI-54637 WWPDB D_1290054637 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.content_type _pdbx_database_related.details PDB 2YP2 unspecified 'HAEMAGGLUTININ OF 2004 HUMAN H3N2 VIRUS' PDB 2YP3 unspecified 'HAEMAGGLUTININ OF 2004 HUMAN H3N2 VIRUS IN COMPLEX WITH HUMAN RECEPTOR ANALOGUE 6SLN' PDB 2YP4 unspecified 'HAEMAGGLUTININ OF 2004 HUMAN H3N2 VIRUS IN COMPLEX WITH HUMAN RECEPTOR ANALOGUE LSTC' PDB 2YP5 unspecified 'HAEMAGGLUTININ OF 2004 HUMAN H3N2 VIRUS IN COMPLEX' PDB 2YP7 unspecified 'HAEMAGGLUTININ OF 2005 HUMAN H3N2 VIRUS' PDB 2YP8 unspecified 'HAEMAGGLUTININ OF 2005 HUMAN H3N2 VIRUS IN COMPLEX WITH HUMAN RECEPTOR ANALOGUE 6SLN' PDB 2YP9 unspecified 'HAEMAGGLUTININ OF 2005 HUMAN H3N2 VIRUS IN COMPLEX WITH AVIAN RECEPTOR ANALOGUE 3SLN' PDB 2YPG unspecified 'HAEMAGGLUTININ OF 1968 HUMAN H3N2 VIRUS IN COMPLEX WITH HUMAN RECEPTOR ANALOGUE LSTC' # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 2YP7 _pdbx_database_status.deposit_site PDBE _pdbx_database_status.process_site PDBE _pdbx_database_status.SG_entry . _pdbx_database_status.recvd_initial_deposition_date 2012-10-29 _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_sf ? _pdbx_database_status.status_code_mr ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Xiong, X.' 1 'Lin, Y.P.' 2 'Wharton, S.A.' 3 'Martin, S.R.' 4 'Coombs, P.J.' 5 'Vachieri, S.G.' 6 'Christodoulou, E.' 7 'Walker, P.A.' 8 'Liu, J.' 9 'Skehel, J.J.' 10 'Gamblin, S.J.' 11 'Hay, A.J.' 12 'Daniels, R.S.' 13 'McCauley, J.W.' 14 # _citation.id primary _citation.title 'Evolution of the Receptor Binding Properties of the Influenza A(H3N2) Hemagglutinin.' _citation.journal_abbrev Proc.Natl.Acad.Sci.USA _citation.journal_volume 109 _citation.page_first 21474 _citation.page_last ? _citation.year 2012 _citation.journal_id_ASTM PNASA6 _citation.country US _citation.journal_id_ISSN 0027-8424 _citation.journal_id_CSD 0040 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 23236176 _citation.pdbx_database_id_DOI 10.1073/PNAS.1218841110 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Lin, Y.P.' 1 primary 'Xiong, X.' 2 primary 'Wharton, S.A.' 3 primary 'Martin, S.R.' 4 primary 'Coombs, P.J.' 5 primary 'Vachieri, S.G.' 6 primary 'Christodoulou, E.' 7 primary 'Walker, P.A.' 8 primary 'Liu, J.' 9 primary 'Skehel, J.J.' 10 primary 'Gamblin, S.J.' 11 primary 'Hay, A.J.' 12 primary 'Daniels, R.S.' 13 primary 'Mccauley, J.W.' 14 # _cell.entry_id 2YP7 _cell.length_a 100.890 _cell.length_b 100.890 _cell.length_c 386.260 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 120.00 _cell.Z_PDB 18 _cell.pdbx_unique_axis ? # _symmetry.entry_id 2YP7 _symmetry.space_group_name_H-M 'H 3 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 155 # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer man HEMAGGLUTININ 56488.215 1 ? YES 'TRYPSIN RELEASED ECTODOMAIN, RESIDUES 17-519' ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 10 ? ? ? ? 3 non-polymer man ALPHA-D-MANNOSE 180.156 1 ? ? ? ? 4 non-polymer syn '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' 238.305 2 ? ? ? ? 5 non-polymer syn 'TRIS(HYDROXYETHYL)AMINOMETHANE' 163.215 1 ? ? ? ? 6 water nat water 18.015 424 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name HAEMAGGLUTININ # _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 ;QKLPGNDNSTATLCLGHHAVPNGTIVKTITNDQIEVTNATELVQSSSTGGICDSPHQILDGENCTLIDALLGDPQCDGFQ NKKWDLFVERSKAYSNCYPYDVPDYASLRSLVASSGTLEFNNESFNWTGVTQNGTSSACKRKSNNSFFSRLNWLTHLKFK YPALNVTMPNNEKFDKLYIWGVHHPGTDNDQIFLYAQASGRITVSTKRSQQTVIPNIGSRPRVRNIPSRISIYWTIVKPG DILLINSTGNLIAPRGYFKIRSGKSSIMRSDAPIGKCNSECITPNGSIPNDKPFQNVNRITYGACPRYVKQNTLKLATGM RNVPEKQTQGIFGAIAGFIENGWEGMVDGWYGFRHQNSEGIGQAADLKSTQAAINQINGKLNRLIGKTNEKFHQIEKEFS EVEGRIQDLEKYVEDTKIDLWSYNAELLVALENQHTIDLTDSEMNKLFERTKKQLRENAEDMGNGCFKIYHKCDNACIGS IRNGTYDHDVYRDEALNNRFQIK ; _entity_poly.pdbx_seq_one_letter_code_can ;QKLPGNDNSTATLCLGHHAVPNGTIVKTITNDQIEVTNATELVQSSSTGGICDSPHQILDGENCTLIDALLGDPQCDGFQ NKKWDLFVERSKAYSNCYPYDVPDYASLRSLVASSGTLEFNNESFNWTGVTQNGTSSACKRKSNNSFFSRLNWLTHLKFK YPALNVTMPNNEKFDKLYIWGVHHPGTDNDQIFLYAQASGRITVSTKRSQQTVIPNIGSRPRVRNIPSRISIYWTIVKPG DILLINSTGNLIAPRGYFKIRSGKSSIMRSDAPIGKCNSECITPNGSIPNDKPFQNVNRITYGACPRYVKQNTLKLATGM RNVPEKQTQGIFGAIAGFIENGWEGMVDGWYGFRHQNSEGIGQAADLKSTQAAINQINGKLNRLIGKTNEKFHQIEKEFS EVEGRIQDLEKYVEDTKIDLWSYNAELLVALENQHTIDLTDSEMNKLFERTKKQLRENAEDMGNGCFKIYHKCDNACIGS IRNGTYDHDVYRDEALNNRFQIK ; _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 LYS n 1 3 LEU n 1 4 PRO n 1 5 GLY n 1 6 ASN n 1 7 ASP n 1 8 ASN n 1 9 SER n 1 10 THR n 1 11 ALA n 1 12 THR n 1 13 LEU n 1 14 CYS n 1 15 LEU n 1 16 GLY n 1 17 HIS n 1 18 HIS n 1 19 ALA n 1 20 VAL n 1 21 PRO n 1 22 ASN n 1 23 GLY n 1 24 THR n 1 25 ILE n 1 26 VAL n 1 27 LYS n 1 28 THR n 1 29 ILE n 1 30 THR n 1 31 ASN n 1 32 ASP n 1 33 GLN n 1 34 ILE n 1 35 GLU n 1 36 VAL n 1 37 THR n 1 38 ASN n 1 39 ALA n 1 40 THR n 1 41 GLU n 1 42 LEU n 1 43 VAL n 1 44 GLN n 1 45 SER n 1 46 SER n 1 47 SER n 1 48 THR n 1 49 GLY n 1 50 GLY n 1 51 ILE n 1 52 CYS n 1 53 ASP n 1 54 SER n 1 55 PRO n 1 56 HIS n 1 57 GLN n 1 58 ILE n 1 59 LEU n 1 60 ASP n 1 61 GLY n 1 62 GLU n 1 63 ASN n 1 64 CYS n 1 65 THR n 1 66 LEU n 1 67 ILE n 1 68 ASP n 1 69 ALA n 1 70 LEU n 1 71 LEU n 1 72 GLY n 1 73 ASP n 1 74 PRO n 1 75 GLN n 1 76 CYS n 1 77 ASP n 1 78 GLY n 1 79 PHE n 1 80 GLN n 1 81 ASN n 1 82 LYS n 1 83 LYS n 1 84 TRP n 1 85 ASP n 1 86 LEU n 1 87 PHE n 1 88 VAL n 1 89 GLU n 1 90 ARG n 1 91 SER n 1 92 LYS n 1 93 ALA n 1 94 TYR n 1 95 SER n 1 96 ASN n 1 97 CYS n 1 98 TYR n 1 99 PRO n 1 100 TYR n 1 101 ASP n 1 102 VAL n 1 103 PRO n 1 104 ASP n 1 105 TYR n 1 106 ALA n 1 107 SER n 1 108 LEU n 1 109 ARG n 1 110 SER n 1 111 LEU n 1 112 VAL n 1 113 ALA n 1 114 SER n 1 115 SER n 1 116 GLY n 1 117 THR n 1 118 LEU n 1 119 GLU n 1 120 PHE n 1 121 ASN n 1 122 ASN n 1 123 GLU n 1 124 SER n 1 125 PHE n 1 126 ASN n 1 127 TRP n 1 128 THR n 1 129 GLY n 1 130 VAL n 1 131 THR n 1 132 GLN n 1 133 ASN n 1 134 GLY n 1 135 THR n 1 136 SER n 1 137 SER n 1 138 ALA n 1 139 CYS n 1 140 LYS n 1 141 ARG n 1 142 LYS n 1 143 SER n 1 144 ASN n 1 145 ASN n 1 146 SER n 1 147 PHE n 1 148 PHE n 1 149 SER n 1 150 ARG n 1 151 LEU n 1 152 ASN n 1 153 TRP n 1 154 LEU n 1 155 THR n 1 156 HIS n 1 157 LEU n 1 158 LYS n 1 159 PHE n 1 160 LYS n 1 161 TYR n 1 162 PRO n 1 163 ALA n 1 164 LEU n 1 165 ASN n 1 166 VAL n 1 167 THR n 1 168 MET n 1 169 PRO n 1 170 ASN n 1 171 ASN n 1 172 GLU n 1 173 LYS n 1 174 PHE n 1 175 ASP n 1 176 LYS n 1 177 LEU n 1 178 TYR n 1 179 ILE n 1 180 TRP n 1 181 GLY n 1 182 VAL n 1 183 HIS n 1 184 HIS n 1 185 PRO n 1 186 GLY n 1 187 THR n 1 188 ASP n 1 189 ASN n 1 190 ASP n 1 191 GLN n 1 192 ILE n 1 193 PHE n 1 194 LEU n 1 195 TYR n 1 196 ALA n 1 197 GLN n 1 198 ALA n 1 199 SER n 1 200 GLY n 1 201 ARG n 1 202 ILE n 1 203 THR n 1 204 VAL n 1 205 SER n 1 206 THR n 1 207 LYS n 1 208 ARG n 1 209 SER n 1 210 GLN n 1 211 GLN n 1 212 THR n 1 213 VAL n 1 214 ILE n 1 215 PRO n 1 216 ASN n 1 217 ILE n 1 218 GLY n 1 219 SER n 1 220 ARG n 1 221 PRO n 1 222 ARG n 1 223 VAL n 1 224 ARG n 1 225 ASN n 1 226 ILE n 1 227 PRO n 1 228 SER n 1 229 ARG n 1 230 ILE n 1 231 SER n 1 232 ILE n 1 233 TYR n 1 234 TRP n 1 235 THR n 1 236 ILE n 1 237 VAL n 1 238 LYS n 1 239 PRO n 1 240 GLY n 1 241 ASP n 1 242 ILE n 1 243 LEU n 1 244 LEU n 1 245 ILE n 1 246 ASN n 1 247 SER n 1 248 THR n 1 249 GLY n 1 250 ASN n 1 251 LEU n 1 252 ILE n 1 253 ALA n 1 254 PRO n 1 255 ARG n 1 256 GLY n 1 257 TYR n 1 258 PHE n 1 259 LYS n 1 260 ILE n 1 261 ARG n 1 262 SER n 1 263 GLY n 1 264 LYS n 1 265 SER n 1 266 SER n 1 267 ILE n 1 268 MET n 1 269 ARG n 1 270 SER n 1 271 ASP n 1 272 ALA n 1 273 PRO n 1 274 ILE n 1 275 GLY n 1 276 LYS n 1 277 CYS n 1 278 ASN n 1 279 SER n 1 280 GLU n 1 281 CYS n 1 282 ILE n 1 283 THR n 1 284 PRO n 1 285 ASN n 1 286 GLY n 1 287 SER n 1 288 ILE n 1 289 PRO n 1 290 ASN n 1 291 ASP n 1 292 LYS n 1 293 PRO n 1 294 PHE n 1 295 GLN n 1 296 ASN n 1 297 VAL n 1 298 ASN n 1 299 ARG n 1 300 ILE n 1 301 THR n 1 302 TYR n 1 303 GLY n 1 304 ALA n 1 305 CYS n 1 306 PRO n 1 307 ARG n 1 308 TYR n 1 309 VAL n 1 310 LYS n 1 311 GLN n 1 312 ASN n 1 313 THR n 1 314 LEU n 1 315 LYS n 1 316 LEU n 1 317 ALA n 1 318 THR n 1 319 GLY n 1 320 MET n 1 321 ARG n 1 322 ASN n 1 323 VAL n 1 324 PRO n 1 325 GLU n 1 326 LYS n 1 327 GLN n 1 328 THR n 1 329 GLN n 1 330 GLY n 1 331 ILE n 1 332 PHE n 1 333 GLY n 1 334 ALA n 1 335 ILE n 1 336 ALA n 1 337 GLY n 1 338 PHE n 1 339 ILE n 1 340 GLU n 1 341 ASN n 1 342 GLY n 1 343 TRP n 1 344 GLU n 1 345 GLY n 1 346 MET n 1 347 VAL n 1 348 ASP n 1 349 GLY n 1 350 TRP n 1 351 TYR n 1 352 GLY n 1 353 PHE n 1 354 ARG n 1 355 HIS n 1 356 GLN n 1 357 ASN n 1 358 SER n 1 359 GLU n 1 360 GLY n 1 361 ILE n 1 362 GLY n 1 363 GLN n 1 364 ALA n 1 365 ALA n 1 366 ASP n 1 367 LEU n 1 368 LYS n 1 369 SER n 1 370 THR n 1 371 GLN n 1 372 ALA n 1 373 ALA n 1 374 ILE n 1 375 ASN n 1 376 GLN n 1 377 ILE n 1 378 ASN n 1 379 GLY n 1 380 LYS n 1 381 LEU n 1 382 ASN n 1 383 ARG n 1 384 LEU n 1 385 ILE n 1 386 GLY n 1 387 LYS n 1 388 THR n 1 389 ASN n 1 390 GLU n 1 391 LYS n 1 392 PHE n 1 393 HIS n 1 394 GLN n 1 395 ILE n 1 396 GLU n 1 397 LYS n 1 398 GLU n 1 399 PHE n 1 400 SER n 1 401 GLU n 1 402 VAL n 1 403 GLU n 1 404 GLY n 1 405 ARG n 1 406 ILE n 1 407 GLN n 1 408 ASP n 1 409 LEU n 1 410 GLU n 1 411 LYS n 1 412 TYR n 1 413 VAL n 1 414 GLU n 1 415 ASP n 1 416 THR n 1 417 LYS n 1 418 ILE n 1 419 ASP n 1 420 LEU n 1 421 TRP n 1 422 SER n 1 423 TYR n 1 424 ASN n 1 425 ALA n 1 426 GLU n 1 427 LEU n 1 428 LEU n 1 429 VAL n 1 430 ALA n 1 431 LEU n 1 432 GLU n 1 433 ASN n 1 434 GLN n 1 435 HIS n 1 436 THR n 1 437 ILE n 1 438 ASP n 1 439 LEU n 1 440 THR n 1 441 ASP n 1 442 SER n 1 443 GLU n 1 444 MET n 1 445 ASN n 1 446 LYS n 1 447 LEU n 1 448 PHE n 1 449 GLU n 1 450 ARG n 1 451 THR n 1 452 LYS n 1 453 LYS n 1 454 GLN n 1 455 LEU n 1 456 ARG n 1 457 GLU n 1 458 ASN n 1 459 ALA n 1 460 GLU n 1 461 ASP n 1 462 MET n 1 463 GLY n 1 464 ASN n 1 465 GLY n 1 466 CYS n 1 467 PHE n 1 468 LYS n 1 469 ILE n 1 470 TYR n 1 471 HIS n 1 472 LYS n 1 473 CYS n 1 474 ASP n 1 475 ASN n 1 476 ALA n 1 477 CYS n 1 478 ILE n 1 479 GLY n 1 480 SER n 1 481 ILE n 1 482 ARG n 1 483 ASN n 1 484 GLY n 1 485 THR n 1 486 TYR n 1 487 ASP n 1 488 HIS n 1 489 ASP n 1 490 VAL n 1 491 TYR n 1 492 ARG n 1 493 ASP n 1 494 GLU n 1 495 ALA n 1 496 LEU n 1 497 ASN n 1 498 ASN n 1 499 ARG n 1 500 PHE n 1 501 GLN n 1 502 ILE n 1 503 LYS n # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _entity_src_gen.pdbx_seq_type ? _entity_src_gen.pdbx_beg_seq_num ? _entity_src_gen.pdbx_end_seq_num ? _entity_src_gen.gene_src_common_name ? _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene ? _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain H3N2 _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 'INFLUENZA A VIRUS' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 11320 _entity_src_gen.pdbx_gene_src_variant 'A/HONG KONG/4443/2005' _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 'FALL ARMYWORM' _entity_src_gen.pdbx_host_org_scientific_name 'SPODOPTERA FRUGIPERDA' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 7108 _entity_src_gen.host_org_genus ? _entity_src_gen.pdbx_host_org_gene ? _entity_src_gen.pdbx_host_org_organ ? _entity_src_gen.host_org_species ? _entity_src_gen.pdbx_host_org_tissue ? _entity_src_gen.pdbx_host_org_tissue_fraction ? _entity_src_gen.pdbx_host_org_strain ? _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line SF9 _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 BACULOVIRUS _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name PACGP67A _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code I2D7A8_9INFA _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ? _struct_ref.pdbx_align_begin ? _struct_ref.pdbx_db_accession I2D7A8 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 2YP7 _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 503 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession I2D7A8 _struct_ref_seq.db_align_beg 17 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 519 _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 503 # _struct_ref_seq_dif.align_id 1 _struct_ref_seq_dif.pdbx_pdb_id_code 2YP7 _struct_ref_seq_dif.mon_id GLN _struct_ref_seq_dif.pdbx_pdb_strand_id A _struct_ref_seq_dif.seq_num 329 _struct_ref_seq_dif.pdbx_pdb_ins_code ? _struct_ref_seq_dif.pdbx_seq_db_name UNP _struct_ref_seq_dif.pdbx_seq_db_accession_code I2D7A8 _struct_ref_seq_dif.db_mon_id ARG _struct_ref_seq_dif.pdbx_seq_db_seq_num 345 _struct_ref_seq_dif.details 'engineered mutation' _struct_ref_seq_dif.pdbx_auth_seq_num 329 _struct_ref_seq_dif.pdbx_ordinal 1 # 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 EPE non-polymer . '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' HEPES 'C8 H18 N2 O4 S' 238.305 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MAN D-saccharide . ALPHA-D-MANNOSE ? 'C6 H12 O6' 180.156 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 TAM non-polymer . 'TRIS(HYDROXYETHYL)AMINOMETHANE' ? 'C7 H17 N O3' 163.215 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 2YP7 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.35 _exptl_crystal.density_percent_sol 63.27 _exptl_crystal.description NONE # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method ? _exptl_crystal_grow.temp ? _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH ? _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details 'SITTING DROP, DEGLYCOSYLATED PROTEIN, 0.1 M HEPES PH 7.5, 0.2 M KCL, 30% PENTAERYTHRITOL PROPOXYLATE (5/4 PO/OH)' # _diffrn.id 1 _diffrn.ambient_temp 77 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'ADSC CCD' _diffrn_detector.pdbx_collection_date 2012-12-18 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.976253 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'DIAMOND BEAMLINE I03' _diffrn_source.pdbx_synchrotron_site Diamond _diffrn_source.pdbx_synchrotron_beamline I03 _diffrn_source.pdbx_wavelength 0.976253 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 2YP7 _reflns.observed_criterion_sigma_I 2.2 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 64.79 _reflns.d_resolution_high 1.85 _reflns.number_obs 65292 _reflns.number_all ? _reflns.percent_possible_obs 100.0 _reflns.pdbx_Rmerge_I_obs 0.12 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 8.30 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 8.5 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 2YP7 _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 61939 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F . _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 128.75 _refine.ls_d_res_high 1.85 _refine.ls_percent_reflns_obs 99.91 _refine.ls_R_factor_obs 0.18455 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.18290 _refine.ls_R_factor_R_free 0.21551 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.1 _refine.ls_number_reflns_R_free 3300 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.960 _refine.correlation_coeff_Fo_to_Fc_free 0.946 _refine.B_iso_mean 32.770 _refine.aniso_B[1][1] 1.12 _refine.aniso_B[2][2] 1.12 _refine.aniso_B[3][3] -1.68 _refine.aniso_B[1][2] 0.56 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details MASK _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.20 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.' _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.111 _refine.pdbx_overall_ESU_R_Free 0.110 _refine.overall_SU_ML 0.076 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 4.718 _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 3873 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 192 _refine_hist.number_atoms_solvent 424 _refine_hist.number_atoms_total 4489 _refine_hist.d_res_high 1.85 _refine_hist.d_res_low 128.75 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function r_bond_refined_d 0.011 0.020 ? 4209 'X-RAY DIFFRACTION' ? r_bond_other_d 0.001 0.020 ? 2873 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.451 1.989 ? 5719 'X-RAY DIFFRACTION' ? r_angle_other_deg 0.839 3.003 ? 6964 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 5.875 5.000 ? 502 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 35.931 24.851 ? 202 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 12.362 15.000 ? 698 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 15.264 15.000 ? 25 'X-RAY DIFFRACTION' ? r_chiral_restr 0.084 0.200 ? 642 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.006 0.020 ? 4606 'X-RAY DIFFRACTION' ? r_gen_planes_other 0.001 0.020 ? 815 'X-RAY DIFFRACTION' ? r_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_rigid_bond_restr ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_free ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_bonded ? ? ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 1.849 _refine_ls_shell.d_res_low 1.897 _refine_ls_shell.number_reflns_R_work 4260 _refine_ls_shell.R_factor_R_work 0.280 _refine_ls_shell.percent_reflns_obs 99.56 _refine_ls_shell.R_factor_R_free 0.323 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 225 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? # _struct.entry_id 2YP7 _struct.title 'Haemagglutinin of 2005 Human H3N2 Virus' _struct.pdbx_descriptor HEMAGGLUTININ _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 2YP7 _struct_keywords.pdbx_keywords 'VIRAL PROTEIN' _struct_keywords.text 'VIRAL PROTEIN, RECEPTOR BINDING, MEMBRANE FUSION, INFLUENZA VIRUS EVOLUTION, GLYCOPROTEIN' # 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 2 ? D N N 2 ? E N N 2 ? F N N 2 ? G N N 3 ? H N N 2 ? I N N 2 ? J N N 2 ? K N N 2 ? L N N 2 ? M N N 4 ? N N N 4 ? O N N 5 ? P 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 THR A 65 ? GLY A 72 ? THR A 65 GLY A 72 1 ? 8 HELX_P HELX_P2 2 ASP A 73 ? GLN A 80 ? ASP A 73 GLN A 80 5 ? 8 HELX_P HELX_P3 3 ASP A 104 ? GLY A 116 ? ASP A 104 GLY A 116 1 ? 13 HELX_P HELX_P4 4 THR A 187 ? ALA A 196 ? THR A 187 ALA A 196 1 ? 10 HELX_P HELX_P5 5 ASP A 366 ? ILE A 385 ? ASP A 366 ILE A 385 1 ? 20 HELX_P HELX_P6 6 GLY A 404 ? ARG A 456 ? GLY A 404 ARG A 456 1 ? 53 HELX_P HELX_P7 7 ASP A 474 ? ASN A 483 ? ASP A 474 ASN A 483 1 ? 10 HELX_P HELX_P8 8 ASP A 487 ? PHE A 500 ? ASP A 487 PHE A 500 1 ? 14 # _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 14 SG ? ? ? 1_555 A CYS 466 SG ? ? A CYS 14 A CYS 466 1_555 ? ? ? ? ? ? ? 2.064 ? disulf2 disulf ? ? A CYS 52 SG ? ? ? 1_555 A CYS 277 SG ? ? A CYS 52 A CYS 277 1_555 ? ? ? ? ? ? ? 2.119 ? disulf3 disulf ? ? A CYS 64 SG ? ? ? 1_555 A CYS 76 SG ? ? A CYS 64 A CYS 76 1_555 ? ? ? ? ? ? ? 2.125 ? disulf4 disulf ? ? A CYS 97 SG ? ? ? 1_555 A CYS 139 SG ? ? A CYS 97 A CYS 139 1_555 ? ? ? ? ? ? ? 2.057 ? disulf5 disulf ? ? A CYS 281 SG ? ? ? 1_555 A CYS 305 SG ? ? A CYS 281 A CYS 305 1_555 ? ? ? ? ? ? ? 2.057 ? disulf6 disulf ? ? A CYS 473 SG ? ? ? 1_555 A CYS 477 SG ? ? A CYS 473 A CYS 477 1_555 ? ? ? ? ? ? ? 2.132 ? covale1 covale ? ? A ASN 38 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 38 A NAG 801 1_555 ? ? ? ? ? ? ? 1.444 ? covale2 covale ? ? A ASN 63 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 63 A NAG 802 1_555 ? ? ? ? ? ? ? 1.441 ? covale3 covale ? ? A ASN 126 ND2 ? ? ? 1_555 K NAG . C1 ? ? A ASN 126 A NAG 812 1_555 ? ? ? ? ? ? ? 1.447 ? covale4 covale ? ? A ASN 133 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 133 A NAG 804 1_555 ? ? ? ? ? ? ? 1.437 ? covale5 covale ? ? A ASN 165 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 165 A NAG 805 1_555 ? ? ? ? ? ? ? 1.432 ? covale6 covale ? ? A ASN 246 ND2 ? ? ? 1_555 H NAG . C1 ? ? A ASN 246 A NAG 808 1_555 ? ? ? ? ? ? ? 1.457 ? covale7 covale ? ? A ASN 285 ND2 ? ? ? 1_555 J NAG . C1 ? ? A ASN 285 A NAG 811 1_555 ? ? ? ? ? ? ? 1.480 ? covale8 covale ? ? A ASN 483 ND2 ? ? ? 1_555 L NAG . C1 ? ? A ASN 483 A NAG 813 1_555 ? ? ? ? ? ? ? 1.457 ? covale9 covale ? ? E NAG . O4 ? ? ? 1_555 F NAG . C1 ? ? A NAG 805 A NAG 806 1_555 ? ? ? ? ? ? ? 1.436 ? covale10 covale ? ? G MAN . C1 ? ? ? 1_555 F NAG . O4 ? ? A MAN 807 A NAG 806 1_555 ? ? ? ? ? ? ? 1.454 ? covale11 covale ? ? H NAG . O4 ? ? ? 1_555 I NAG . C1 ? ? A NAG 808 A NAG 809 1_555 ? ? ? ? ? ? ? 1.445 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # _struct_mon_prot_cis.pdbx_id 1 _struct_mon_prot_cis.label_comp_id SER _struct_mon_prot_cis.label_seq_id 54 _struct_mon_prot_cis.label_asym_id A _struct_mon_prot_cis.label_alt_id . _struct_mon_prot_cis.pdbx_PDB_ins_code ? _struct_mon_prot_cis.auth_comp_id SER _struct_mon_prot_cis.auth_seq_id 54 _struct_mon_prot_cis.auth_asym_id A _struct_mon_prot_cis.pdbx_label_comp_id_2 PRO _struct_mon_prot_cis.pdbx_label_seq_id_2 55 _struct_mon_prot_cis.pdbx_label_asym_id_2 A _struct_mon_prot_cis.pdbx_PDB_ins_code_2 ? _struct_mon_prot_cis.pdbx_auth_comp_id_2 PRO _struct_mon_prot_cis.pdbx_auth_seq_id_2 55 _struct_mon_prot_cis.pdbx_auth_asym_id_2 A _struct_mon_prot_cis.pdbx_PDB_model_num 1 _struct_mon_prot_cis.pdbx_omega_angle -0.93 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA ? 5 ? AB ? 2 ? AC ? 2 ? AD ? 3 ? AE ? 2 ? AF ? 3 ? AG ? 5 ? AH ? 5 ? AI ? 2 ? AJ ? 2 ? AK ? 4 ? AL ? 4 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense AA 1 2 ? anti-parallel AA 2 3 ? anti-parallel AA 3 4 ? anti-parallel AA 4 5 ? anti-parallel AB 1 2 ? anti-parallel AC 1 2 ? anti-parallel AD 1 2 ? parallel AD 2 3 ? parallel AE 1 2 ? parallel AF 1 2 ? parallel AF 2 3 ? parallel AG 1 2 ? parallel AG 2 3 ? anti-parallel AG 3 4 ? anti-parallel AG 4 5 ? anti-parallel AH 1 2 ? parallel AH 2 3 ? anti-parallel AH 3 4 ? anti-parallel AH 4 5 ? anti-parallel AI 1 2 ? anti-parallel AJ 1 2 ? anti-parallel AK 1 2 ? anti-parallel AK 2 3 ? anti-parallel AK 3 4 ? anti-parallel AL 1 2 ? anti-parallel AL 2 3 ? anti-parallel AL 3 4 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id AA 1 GLY A 360 ? ALA A 365 ? GLY A 360 ALA A 365 AA 2 TYR A 351 ? ASN A 357 ? TYR A 351 ASN A 357 AA 3 ALA A 11 ? HIS A 17 ? ALA A 11 HIS A 17 AA 4 CYS A 466 ? ILE A 469 ? CYS A 466 ILE A 469 AA 5 ALA A 459 ? ASP A 461 ? ALA A 459 ASP A 461 AB 1 THR A 24 ? VAL A 26 ? THR A 24 VAL A 26 AB 2 ILE A 34 ? VAL A 36 ? ILE A 34 VAL A 36 AC 1 ALA A 39 ? GLU A 41 ? ALA A 39 GLU A 41 AC 2 LYS A 315 ? ALA A 317 ? LYS A 315 ALA A 317 AD 1 VAL A 43 ? GLN A 44 ? VAL A 43 GLN A 44 AD 2 PHE A 294 ? GLN A 295 ? PHE A 294 GLN A 295 AD 3 ARG A 307 ? TYR A 308 ? ARG A 307 TYR A 308 AE 1 ILE A 51 ? SER A 54 ? ILE A 51 SER A 54 AE 2 ILE A 274 ? ASN A 278 ? ILE A 274 ASN A 278 AF 1 ILE A 58 ? ASP A 60 ? ILE A 58 ASP A 60 AF 2 LEU A 86 ? GLU A 89 ? LEU A 86 GLU A 89 AF 3 SER A 266 ? ARG A 269 ? SER A 266 ARG A 269 AG 1 TYR A 100 ? ASP A 101 ? TYR A 100 ASP A 101 AG 2 ARG A 229 ? VAL A 237 ? ARG A 229 VAL A 237 AG 3 LYS A 176 ? HIS A 184 ? LYS A 176 HIS A 184 AG 4 LEU A 251 ? PRO A 254 ? LEU A 251 PRO A 254 AG 5 LEU A 151 ? TRP A 153 ? LEU A 151 TRP A 153 AH 1 TYR A 100 ? ASP A 101 ? TYR A 100 ASP A 101 AH 2 ARG A 229 ? VAL A 237 ? ARG A 229 VAL A 237 AH 3 LYS A 176 ? HIS A 184 ? LYS A 176 HIS A 184 AH 4 GLY A 256 ? LYS A 259 ? GLY A 256 LYS A 259 AH 5 PHE A 120 ? ASN A 122 ? PHE A 120 ASN A 122 AI 1 VAL A 130 ? THR A 131 ? VAL A 130 THR A 131 AI 2 THR A 155 ? HIS A 156 ? THR A 155 HIS A 156 AJ 1 SER A 136 ? ARG A 141 ? SER A 136 ARG A 141 AJ 2 ASN A 144 ? SER A 146 ? ASN A 144 SER A 146 AK 1 LEU A 164 ? PRO A 169 ? LEU A 164 PRO A 169 AK 2 ILE A 242 ? SER A 247 ? ILE A 242 SER A 247 AK 3 ILE A 202 ? SER A 205 ? ILE A 202 SER A 205 AK 4 GLN A 210 ? VAL A 213 ? GLN A 210 VAL A 213 AL 1 GLY A 286 ? ILE A 288 ? GLY A 286 ILE A 288 AL 2 CYS A 281 ? THR A 283 ? CYS A 281 THR A 283 AL 3 TYR A 302 ? CYS A 305 ? TYR A 302 CYS A 305 AL 4 ASN A 389 ? LYS A 391 ? ASN A 389 LYS A 391 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id AA 1 2 N ALA A 364 ? N ALA A 364 O PHE A 353 ? O PHE A 353 AA 2 3 N GLN A 356 ? N GLN A 356 O THR A 12 ? O THR A 12 AA 3 4 N LEU A 13 ? N LEU A 13 O PHE A 467 ? O PHE A 467 AA 4 5 N LYS A 468 ? N LYS A 468 O GLU A 460 ? O GLU A 460 AB 1 2 N VAL A 26 ? N VAL A 26 O ILE A 34 ? O ILE A 34 AC 1 2 N THR A 40 ? N THR A 40 O LEU A 316 ? O LEU A 316 AD 1 2 N GLN A 44 ? N GLN A 44 O PHE A 294 ? O PHE A 294 AD 2 3 N GLN A 295 ? N GLN A 295 O ARG A 307 ? O ARG A 307 AE 1 2 N ASP A 53 ? N ASP A 53 O GLY A 275 ? O GLY A 275 AF 1 2 N LEU A 59 ? N LEU A 59 O LEU A 86 ? O LEU A 86 AF 2 3 N PHE A 87 ? N PHE A 87 O SER A 266 ? O SER A 266 AG 1 2 N ASP A 101 ? N ASP A 101 O ILE A 230 ? O ILE A 230 AG 2 3 N VAL A 237 ? N VAL A 237 O LYS A 176 ? O LYS A 176 AG 3 4 N GLY A 181 ? N GLY A 181 O ILE A 252 ? O ILE A 252 AG 4 5 N ALA A 253 ? N ALA A 253 O ASN A 152 ? O ASN A 152 AH 1 2 N ASP A 101 ? N ASP A 101 O ILE A 230 ? O ILE A 230 AH 2 3 N VAL A 237 ? N VAL A 237 O LYS A 176 ? O LYS A 176 AH 3 4 N LEU A 177 ? N LEU A 177 O PHE A 258 ? O PHE A 258 AH 4 5 N TYR A 257 ? N TYR A 257 O ASN A 121 ? O ASN A 121 AI 1 2 N THR A 131 ? N THR A 131 O THR A 155 ? O THR A 155 AJ 1 2 N ARG A 141 ? N ARG A 141 O ASN A 144 ? O ASN A 144 AK 1 2 N MET A 168 ? N MET A 168 O LEU A 243 ? O LEU A 243 AK 2 3 N ASN A 246 ? N ASN A 246 O THR A 203 ? O THR A 203 AK 3 4 N VAL A 204 ? N VAL A 204 O GLN A 211 ? O GLN A 211 AL 1 2 N ILE A 288 ? N ILE A 288 O CYS A 281 ? O CYS A 281 AL 2 3 N ILE A 282 ? N ILE A 282 O TYR A 302 ? O TYR A 302 AL 3 4 N CYS A 305 ? N CYS A 305 O ASN A 389 ? O ASN A 389 # 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 ? ? ? ? 10 'BINDING SITE FOR RESIDUE EPE A 1504' AC2 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE EPE A 1505' AC3 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE TAM A 1506' AC4 Software ? ? ? ? 3 'BINDING SITE FOR MONO-SACCHARIDE NAG A 801 BOUND TO ASN A 38' AC5 Software ? ? ? ? 3 'BINDING SITE FOR MONO-SACCHARIDE NAG A 802 BOUND TO ASN A 63' AC6 Software ? ? ? ? 2 'BINDING SITE FOR MONO-SACCHARIDE NAG A 812 BOUND TO ASN A 126' AC7 Software ? ? ? ? 2 'BINDING SITE FOR MONO-SACCHARIDE NAG A 804 BOUND TO ASN A 133' AC8 Software ? ? ? ? 9 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 165 RESIDUES 805 TO 807' AC9 Software ? ? ? ? 9 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 246 RESIDUES 808 TO 809' BC1 Software ? ? ? ? 6 'BINDING SITE FOR MONO-SACCHARIDE NAG A 811 BOUND TO ASN A 285' BC2 Software ? ? ? ? 1 'BINDING SITE FOR MONO-SACCHARIDE NAG A 813 BOUND TO ASN A 483' # 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 10 ASP A 77 ? ASP A 77 . ? 1_555 ? 2 AC1 10 GLN A 80 ? GLN A 80 . ? 1_555 ? 3 AC1 10 ARG A 141 ? ARG A 141 . ? 1_555 ? 4 AC1 10 SER A 146 ? SER A 146 . ? 1_555 ? 5 AC1 10 PHE A 147 ? PHE A 147 . ? 1_555 ? 6 AC1 10 PHE A 148 ? PHE A 148 . ? 1_555 ? 7 AC1 10 LEU A 151 ? LEU A 151 . ? 1_555 ? 8 AC1 10 ARG A 255 ? ARG A 255 . ? 1_555 ? 9 AC1 10 NAG D . ? NAG A 804 . ? 1_555 ? 10 AC1 10 HOH P . ? HOH A 2142 . ? 1_555 ? 11 AC2 6 SER A 95 ? SER A 95 . ? 1_555 ? 12 AC2 6 PRO A 99 ? PRO A 99 . ? 1_555 ? 13 AC2 6 TYR A 100 ? TYR A 100 . ? 1_555 ? 14 AC2 6 ARG A 208 ? ARG A 208 . ? 3_455 ? 15 AC2 6 ARG A 224 ? ARG A 224 . ? 1_555 ? 16 AC2 6 GLU A 401 ? GLU A 401 . ? 1_555 ? 17 AC3 2 ARG A 383 ? ARG A 383 . ? 1_555 ? 18 AC3 2 HOH P . ? HOH A 2423 . ? 1_555 ? 19 AC4 3 ASN A 38 ? ASN A 38 . ? 1_555 ? 20 AC4 3 THR A 318 ? THR A 318 . ? 1_555 ? 21 AC4 3 LEU A 381 ? LEU A 381 . ? 1_555 ? 22 AC5 3 ASN A 63 ? ASN A 63 . ? 1_555 ? 23 AC5 3 TYR A 94 ? TYR A 94 . ? 1_555 ? 24 AC5 3 HOH P . ? HOH A 2421 . ? 1_555 ? 25 AC6 2 ASN A 126 ? ASN A 126 . ? 1_555 ? 26 AC6 2 THR A 128 ? THR A 128 . ? 1_555 ? 27 AC7 2 ASN A 133 ? ASN A 133 . ? 1_555 ? 28 AC7 2 EPE M . ? EPE A 1504 . ? 1_555 ? 29 AC8 9 ASN A 165 ? ASN A 165 . ? 1_555 ? 30 AC8 9 SER A 219 ? SER A 219 . ? 2_565 ? 31 AC8 9 PRO A 221 ? PRO A 221 . ? 2_565 ? 32 AC8 9 ARG A 222 ? ARG A 222 . ? 2_565 ? 33 AC8 9 NAG H . ? NAG A 808 . ? 1_555 ? 34 AC8 9 HOH P . ? HOH A 2169 . ? 1_555 ? 35 AC8 9 HOH P . ? HOH A 2187 . ? 2_565 ? 36 AC8 9 HOH P . ? HOH A 2211 . ? 2_565 ? 37 AC8 9 HOH P . ? HOH A 2213 . ? 2_565 ? 38 AC9 9 ALA A 163 ? ALA A 163 . ? 1_555 ? 39 AC9 9 LEU A 164 ? LEU A 164 . ? 1_555 ? 40 AC9 9 ASN A 165 ? ASN A 165 . ? 1_555 ? 41 AC9 9 ARG A 201 ? ARG A 201 . ? 1_555 ? 42 AC9 9 ASN A 246 ? ASN A 246 . ? 1_555 ? 43 AC9 9 SER A 247 ? SER A 247 . ? 1_555 ? 44 AC9 9 THR A 248 ? THR A 248 . ? 1_555 ? 45 AC9 9 NAG E . ? NAG A 805 . ? 1_555 ? 46 AC9 9 HOH P . ? HOH A 2197 . ? 1_555 ? 47 BC1 6 ASN A 285 ? ASN A 285 . ? 1_555 ? 48 BC1 6 VAL A 297 ? VAL A 297 . ? 1_555 ? 49 BC1 6 ASN A 298 ? ASN A 298 . ? 1_555 ? 50 BC1 6 GLU A 398 ? GLU A 398 . ? 1_555 ? 51 BC1 6 HOH P . ? HOH A 2253 . ? 1_555 ? 52 BC1 6 HOH P . ? HOH A 2267 . ? 1_555 ? 53 BC2 1 ASN A 483 ? ASN A 483 . ? 1_555 ? # _database_PDB_matrix.entry_id 2YP7 _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 2YP7 _atom_sites.fract_transf_matrix[1][1] 0.009912 _atom_sites.fract_transf_matrix[1][2] 0.005723 _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] 0.011445 _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] 0.002589 _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 . ASN A 1 8 ? -55.240 8.447 -12.797 1.00 74.40 ? 8 ASN A N 1 ATOM 2 C CA . ASN A 1 8 ? -53.816 8.395 -12.353 1.00 74.91 ? 8 ASN A CA 1 ATOM 3 C C . ASN A 1 8 ? -53.074 9.694 -12.714 1.00 70.63 ? 8 ASN A C 1 ATOM 4 O O . ASN A 1 8 ? -53.714 10.715 -12.993 1.00 72.08 ? 8 ASN A O 1 ATOM 5 C CB . ASN A 1 8 ? -53.126 7.149 -12.938 1.00 78.60 ? 8 ASN A CB 1 ATOM 6 C CG . ASN A 1 8 ? -52.861 7.260 -14.434 1.00 83.55 ? 8 ASN A CG 1 ATOM 7 O OD1 . ASN A 1 8 ? -53.533 8.005 -15.155 1.00 85.97 ? 8 ASN A OD1 1 ATOM 8 N ND2 . ASN A 1 8 ? -51.874 6.507 -14.907 1.00 85.76 ? 8 ASN A ND2 1 ATOM 9 N N . SER A 1 9 ? -51.737 9.658 -12.695 1.00 63.78 ? 9 SER A N 1 ATOM 10 C CA . SER A 1 9 ? -50.893 10.843 -12.930 1.00 57.48 ? 9 SER A CA 1 ATOM 11 C C . SER A 1 9 ? -50.865 11.784 -11.717 1.00 49.98 ? 9 SER A C 1 ATOM 12 O O . SER A 1 9 ? -50.234 12.838 -11.760 1.00 46.11 ? 9 SER A O 1 ATOM 13 C CB . SER A 1 9 ? -51.315 11.587 -14.213 1.00 59.39 ? 9 SER A CB 1 ATOM 14 O OG . SER A 1 9 ? -52.304 12.582 -13.978 1.00 59.32 ? 9 SER A OG 1 ATOM 15 N N . THR A 1 10 ? -51.543 11.397 -10.636 1.00 46.39 ? 10 THR A N 1 ATOM 16 C CA . THR A 1 10 ? -51.481 12.123 -9.362 1.00 42.62 ? 10 THR A CA 1 ATOM 17 C C . THR A 1 10 ? -51.308 11.128 -8.225 1.00 39.60 ? 10 THR A C 1 ATOM 18 O O . THR A 1 10 ? -51.465 9.940 -8.399 1.00 40.49 ? 10 THR A O 1 ATOM 19 C CB . THR A 1 10 ? -52.757 12.942 -9.091 1.00 42.88 ? 10 THR A CB 1 ATOM 20 O OG1 . THR A 1 10 ? -53.896 12.083 -9.166 1.00 45.66 ? 10 THR A OG1 1 ATOM 21 C CG2 . THR A 1 10 ? -52.907 14.059 -10.098 1.00 44.64 ? 10 THR A CG2 1 ATOM 22 N N . ALA A 1 11 ? -50.991 11.636 -7.047 1.00 35.03 ? 11 ALA A N 1 ATOM 23 C CA . ALA A 1 11 ? -50.912 10.812 -5.877 1.00 33.86 ? 11 ALA A CA 1 ATOM 24 C C . ALA A 1 11 ? -51.548 11.603 -4.743 1.00 32.84 ? 11 ALA A C 1 ATOM 25 O O . ALA A 1 11 ? -51.729 12.813 -4.857 1.00 31.14 ? 11 ALA A O 1 ATOM 26 C CB . ALA A 1 11 ? -49.454 10.512 -5.549 1.00 33.01 ? 11 ALA A CB 1 ATOM 27 N N . THR A 1 12 ? -51.854 10.914 -3.648 1.00 32.09 ? 12 THR A N 1 ATOM 28 C CA . THR A 1 12 ? -52.337 11.561 -2.422 1.00 31.61 ? 12 THR A CA 1 ATOM 29 C C . THR A 1 12 ? -51.394 11.273 -1.273 1.00 30.26 ? 12 THR A C 1 ATOM 30 O O . THR A 1 12 ? -50.942 10.147 -1.105 1.00 31.21 ? 12 THR A O 1 ATOM 31 C CB . THR A 1 12 ? -53.735 11.043 -2.058 1.00 32.39 ? 12 THR A CB 1 ATOM 32 O OG1 . THR A 1 12 ? -54.602 11.276 -3.158 1.00 35.15 ? 12 THR A OG1 1 ATOM 33 C CG2 . THR A 1 12 ? -54.296 11.744 -0.809 1.00 33.07 ? 12 THR A CG2 1 ATOM 34 N N . LEU A 1 13 ? -51.104 12.284 -0.464 1.00 29.16 ? 13 LEU A N 1 ATOM 35 C CA . LEU A 1 13 ? -50.290 12.099 0.732 1.00 28.59 ? 13 LEU A CA 1 ATOM 36 C C . LEU A 1 13 ? -50.981 12.735 1.935 1.00 29.68 ? 13 LEU A C 1 ATOM 37 O O . LEU A 1 13 ? -51.155 13.946 1.972 1.00 30.19 ? 13 LEU A O 1 ATOM 38 C CB . LEU A 1 13 ? -48.895 12.696 0.553 1.00 27.90 ? 13 LEU A CB 1 ATOM 39 C CG . LEU A 1 13 ? -47.892 12.555 1.717 1.00 28.16 ? 13 LEU A CG 1 ATOM 40 C CD1 . LEU A 1 13 ? -47.588 11.086 1.980 1.00 30.21 ? 13 LEU A CD1 1 ATOM 41 C CD2 . LEU A 1 13 ? -46.621 13.368 1.468 1.00 28.20 ? 13 LEU A CD2 1 ATOM 42 N N . CYS A 1 14 ? -51.366 11.913 2.905 1.00 30.91 ? 14 CYS A N 1 ATOM 43 C CA . CYS A 1 14 ? -52.068 12.393 4.101 1.00 30.96 ? 14 CYS A CA 1 ATOM 44 C C . CYS A 1 14 ? -51.150 12.370 5.297 1.00 30.12 ? 14 CYS A C 1 ATOM 45 O O . CYS A 1 14 ? -50.314 11.477 5.443 1.00 29.22 ? 14 CYS A O 1 ATOM 46 C CB . CYS A 1 14 ? -53.315 11.532 4.368 1.00 33.37 ? 14 CYS A CB 1 ATOM 47 S SG . CYS A 1 14 ? -54.538 11.533 3.039 1.00 36.85 ? 14 CYS A SG 1 ATOM 48 N N . LEU A 1 15 ? -51.273 13.403 6.140 1.00 27.99 ? 15 LEU A N 1 ATOM 49 C CA . LEU A 1 15 ? -50.605 13.451 7.408 1.00 27.97 ? 15 LEU A CA 1 ATOM 50 C C . LEU A 1 15 ? -51.597 13.098 8.494 1.00 27.60 ? 15 LEU A C 1 ATOM 51 O O . LEU A 1 15 ? -52.756 13.515 8.428 1.00 28.95 ? 15 LEU A O 1 ATOM 52 C CB . LEU A 1 15 ? -50.089 14.855 7.658 1.00 27.56 ? 15 LEU A CB 1 ATOM 53 C CG . LEU A 1 15 ? -48.815 15.257 6.920 1.00 28.68 ? 15 LEU A CG 1 ATOM 54 C CD1 . LEU A 1 15 ? -47.694 14.391 7.449 1.00 31.10 ? 15 LEU A CD1 1 ATOM 55 C CD2 . LEU A 1 15 ? -48.945 15.133 5.409 1.00 31.27 ? 15 LEU A CD2 1 ATOM 56 N N . GLY A 1 16 ? -51.153 12.360 9.503 1.00 26.95 ? 16 GLY A N 1 ATOM 57 C CA . GLY A 1 16 ? -52.083 11.892 10.520 1.00 27.13 ? 16 GLY A CA 1 ATOM 58 C C . GLY A 1 16 ? -51.436 11.597 11.833 1.00 26.56 ? 16 GLY A C 1 ATOM 59 O O . GLY A 1 16 ? -50.222 11.699 11.970 1.00 25.50 ? 16 GLY A O 1 ATOM 60 N N . HIS A 1 17 ? -52.257 11.217 12.807 1.00 26.27 ? 17 HIS A N 1 ATOM 61 C CA . HIS A 1 17 ? -51.743 10.847 14.114 1.00 26.88 ? 17 HIS A CA 1 ATOM 62 C C . HIS A 1 17 ? -52.527 9.701 14.647 1.00 27.23 ? 17 HIS A C 1 ATOM 63 O O . HIS A 1 17 ? -53.642 9.464 14.202 1.00 28.69 ? 17 HIS A O 1 ATOM 64 C CB . HIS A 1 17 ? -51.808 12.053 15.078 1.00 26.57 ? 17 HIS A CB 1 ATOM 65 C CG . HIS A 1 17 ? -53.212 12.547 15.330 1.00 27.71 ? 17 HIS A CG 1 ATOM 66 N ND1 . HIS A 1 17 ? -54.127 11.822 16.006 1.00 28.52 ? 17 HIS A ND1 1 ATOM 67 C CD2 . HIS A 1 17 ? -53.852 13.703 14.932 1.00 29.58 ? 17 HIS A CD2 1 ATOM 68 C CE1 . HIS A 1 17 ? -55.294 12.490 16.030 1.00 30.02 ? 17 HIS A CE1 1 ATOM 69 N NE2 . HIS A 1 17 ? -55.134 13.628 15.364 1.00 30.10 ? 17 HIS A NE2 1 ATOM 70 N N . HIS A 1 18 ? -51.954 8.960 15.584 1.00 27.76 ? 18 HIS A N 1 ATOM 71 C CA . HIS A 1 18 ? -52.606 7.770 16.108 1.00 29.06 ? 18 HIS A CA 1 ATOM 72 C C . HIS A 1 18 ? -53.838 8.060 16.958 1.00 30.26 ? 18 HIS A C 1 ATOM 73 O O . HIS A 1 18 ? -54.123 9.198 17.311 1.00 28.90 ? 18 HIS A O 1 ATOM 74 C CB . HIS A 1 18 ? -51.604 6.886 16.857 1.00 29.32 ? 18 HIS A CB 1 ATOM 75 C CG . HIS A 1 18 ? -51.214 7.391 18.235 1.00 29.12 ? 18 HIS A CG 1 ATOM 76 N ND1 . HIS A 1 18 ? -50.747 6.571 19.192 1.00 30.21 ? 18 HIS A ND1 1 ATOM 77 C CD2 . HIS A 1 18 ? -51.255 8.673 18.803 1.00 29.32 ? 18 HIS A CD2 1 ATOM 78 C CE1 . HIS A 1 18 ? -50.478 7.291 20.310 1.00 30.13 ? 18 HIS A CE1 1 ATOM 79 N NE2 . HIS A 1 18 ? -50.786 8.572 20.071 1.00 28.31 ? 18 HIS A NE2 1 ATOM 80 N N . ALA A 1 19 ? -54.583 7.005 17.252 1.00 30.20 ? 19 ALA A N 1 ATOM 81 C CA . ALA A 1 19 ? -55.729 7.035 18.147 1.00 32.26 ? 19 ALA A CA 1 ATOM 82 C C . ALA A 1 19 ? -55.818 5.619 18.732 1.00 34.33 ? 19 ALA A C 1 ATOM 83 O O . ALA A 1 19 ? -55.338 4.665 18.112 1.00 36.70 ? 19 ALA A O 1 ATOM 84 C CB . ALA A 1 19 ? -57.018 7.414 17.413 1.00 32.21 ? 19 ALA A CB 1 ATOM 85 N N . VAL A 1 20 ? -56.406 5.495 19.919 1.00 34.84 ? 20 VAL A N 1 ATOM 86 C CA . VAL A 1 20 ? -56.447 4.230 20.640 1.00 36.24 ? 20 VAL A CA 1 ATOM 87 C C . VAL A 1 20 ? -57.899 3.933 20.938 1.00 39.17 ? 20 VAL A C 1 ATOM 88 O O . VAL A 1 20 ? -58.733 4.844 20.945 1.00 37.21 ? 20 VAL A O 1 ATOM 89 C CB . VAL A 1 20 ? -55.596 4.244 21.932 1.00 36.35 ? 20 VAL A CB 1 ATOM 90 C CG1 . VAL A 1 20 ? -54.127 4.481 21.600 1.00 35.63 ? 20 VAL A CG1 1 ATOM 91 C CG2 . VAL A 1 20 ? -56.112 5.262 22.943 1.00 34.16 ? 20 VAL A CG2 1 ATOM 92 N N . PRO A 1 21 ? -58.232 2.640 21.100 1.00 42.46 ? 21 PRO A N 1 ATOM 93 C CA . PRO A 1 21 ? -59.621 2.290 21.402 1.00 44.83 ? 21 PRO A CA 1 ATOM 94 C C . PRO A 1 21 ? -60.025 2.607 22.847 1.00 46.44 ? 21 PRO A C 1 ATOM 95 O O . PRO A 1 21 ? -61.199 2.868 23.093 1.00 51.77 ? 21 PRO A O 1 ATOM 96 C CB . PRO A 1 21 ? -59.682 0.780 21.124 1.00 44.73 ? 21 PRO A CB 1 ATOM 97 C CG . PRO A 1 21 ? -58.281 0.288 21.284 1.00 44.44 ? 21 PRO A CG 1 ATOM 98 C CD . PRO A 1 21 ? -57.359 1.457 20.978 1.00 43.22 ? 21 PRO A CD 1 ATOM 99 N N . ASN A 1 22 ? -59.063 2.625 23.769 1.00 47.04 ? 22 ASN A N 1 ATOM 100 C CA . ASN A 1 22 ? -59.332 2.788 25.211 1.00 47.08 ? 22 ASN A CA 1 ATOM 101 C C . ASN A 1 22 ? -58.724 4.097 25.805 1.00 43.08 ? 22 ASN A C 1 ATOM 102 O O . ASN A 1 22 ? -57.789 4.040 26.603 1.00 41.30 ? 22 ASN A O 1 ATOM 103 C CB . ASN A 1 22 ? -58.776 1.572 25.975 1.00 48.65 ? 22 ASN A CB 1 ATOM 104 C CG . ASN A 1 22 ? -57.266 1.406 25.788 1.00 52.54 ? 22 ASN A CG 1 ATOM 105 O OD1 . ASN A 1 22 ? -56.710 1.790 24.738 1.00 56.06 ? 22 ASN A OD1 1 ATOM 106 N ND2 . ASN A 1 22 ? -56.591 0.849 26.801 1.00 53.64 ? 22 ASN A ND2 1 ATOM 107 N N . GLY A 1 23 ? -59.262 5.251 25.422 1.00 41.34 ? 23 GLY A N 1 ATOM 108 C CA . GLY A 1 23 ? -58.695 6.542 25.848 1.00 41.44 ? 23 GLY A CA 1 ATOM 109 C C . GLY A 1 23 ? -59.102 6.868 27.274 1.00 40.69 ? 23 GLY A C 1 ATOM 110 O O . GLY A 1 23 ? -59.958 6.182 27.832 1.00 38.72 ? 23 GLY A O 1 ATOM 111 N N . THR A 1 24 ? -58.500 7.907 27.863 1.00 37.28 ? 24 THR A N 1 ATOM 112 C CA . THR A 1 24 ? -58.825 8.312 29.242 1.00 36.62 ? 24 THR A CA 1 ATOM 113 C C . THR A 1 24 ? -59.195 9.786 29.302 1.00 33.25 ? 24 THR A C 1 ATOM 114 O O . THR A 1 24 ? -58.595 10.608 28.607 1.00 31.16 ? 24 THR A O 1 ATOM 115 C CB . THR A 1 24 ? -57.659 8.128 30.224 1.00 39.27 ? 24 THR A CB 1 ATOM 116 O OG1 . THR A 1 24 ? -56.904 6.964 29.904 1.00 44.44 ? 24 THR A OG1 1 ATOM 117 C CG2 . THR A 1 24 ? -58.173 7.988 31.637 1.00 41.34 ? 24 THR A CG2 1 ATOM 118 N N . ILE A 1 25 ? -60.118 10.121 30.189 1.00 29.78 ? 25 ILE A N 1 ATOM 119 C CA . ILE A 1 25 ? -60.607 11.486 30.306 1.00 30.38 ? 25 ILE A CA 1 ATOM 120 C C . ILE A 1 25 ? -59.712 12.288 31.257 1.00 27.57 ? 25 ILE A C 1 ATOM 121 O O . ILE A 1 25 ? -59.365 11.817 32.349 1.00 26.24 ? 25 ILE A O 1 ATOM 122 C CB . ILE A 1 25 ? -62.064 11.527 30.796 1.00 32.13 ? 25 ILE A CB 1 ATOM 123 C CG1 . ILE A 1 25 ? -62.988 10.845 29.779 1.00 34.99 ? 25 ILE A CG1 1 ATOM 124 C CG2 . ILE A 1 25 ? -62.498 12.979 31.048 1.00 31.43 ? 25 ILE A CG2 1 ATOM 125 C CD1 . ILE A 1 25 ? -63.340 11.695 28.580 1.00 36.35 ? 25 ILE A CD1 1 ATOM 126 N N . VAL A 1 26 ? -59.297 13.474 30.812 1.00 25.59 ? 26 VAL A N 1 ATOM 127 C CA . VAL A 1 26 ? -58.542 14.411 31.645 1.00 24.28 ? 26 VAL A CA 1 ATOM 128 C C . VAL A 1 26 ? -59.175 15.798 31.595 1.00 24.63 ? 26 VAL A C 1 ATOM 129 O O . VAL A 1 26 ? -60.062 16.071 30.774 1.00 24.76 ? 26 VAL A O 1 ATOM 130 C CB . VAL A 1 26 ? -57.053 14.540 31.235 1.00 23.27 ? 26 VAL A CB 1 ATOM 131 C CG1 . VAL A 1 26 ? -56.319 13.208 31.348 1.00 23.00 ? 26 VAL A CG1 1 ATOM 132 C CG2 . VAL A 1 26 ? -56.919 15.147 29.834 1.00 21.64 ? 26 VAL A CG2 1 ATOM 133 N N . LYS A 1 27 ? -58.689 16.681 32.468 1.00 25.84 ? 27 LYS A N 1 ATOM 134 C CA . LYS A 1 27 ? -59.179 18.036 32.560 1.00 27.62 ? 27 LYS A CA 1 ATOM 135 C C . LYS A 1 27 ? -58.087 18.999 32.076 1.00 26.99 ? 27 LYS A C 1 ATOM 136 O O . LYS A 1 27 ? -56.929 18.836 32.388 1.00 23.86 ? 27 LYS A O 1 ATOM 137 C CB . LYS A 1 27 ? -59.544 18.367 34.003 1.00 31.11 ? 27 LYS A CB 1 ATOM 138 C CG . LYS A 1 27 ? -60.029 19.782 34.255 1.00 34.90 ? 27 LYS A CG 1 ATOM 139 C CD . LYS A 1 27 ? -60.439 19.991 35.717 1.00 39.18 ? 27 LYS A CD 1 ATOM 140 C CE . LYS A 1 27 ? -60.588 21.486 36.061 1.00 41.62 ? 27 LYS A CE 1 ATOM 141 N NZ . LYS A 1 27 ? -60.969 21.741 37.493 1.00 42.35 ? 27 LYS A NZ 1 ATOM 142 N N . THR A 1 28 ? -58.487 19.991 31.298 1.00 27.91 ? 28 THR A N 1 ATOM 143 C CA . THR A 1 28 ? -57.540 21.008 30.848 1.00 29.65 ? 28 THR A CA 1 ATOM 144 C C . THR A 1 28 ? -58.118 22.338 31.240 1.00 32.00 ? 28 THR A C 1 ATOM 145 O O . THR A 1 28 ? -59.126 22.417 31.949 1.00 32.16 ? 28 THR A O 1 ATOM 146 C CB . THR A 1 28 ? -57.263 20.936 29.332 1.00 28.99 ? 28 THR A CB 1 ATOM 147 O OG1 . THR A 1 28 ? -58.454 21.265 28.601 1.00 30.68 ? 28 THR A OG1 1 ATOM 148 C CG2 . THR A 1 28 ? -56.794 19.550 28.920 1.00 29.62 ? 28 THR A CG2 1 ATOM 149 N N . ILE A 1 29 ? -57.456 23.403 30.819 1.00 34.07 ? 29 ILE A N 1 ATOM 150 C CA . ILE A 1 29 ? -58.013 24.724 31.026 1.00 34.98 ? 29 ILE A CA 1 ATOM 151 C C . ILE A 1 29 ? -59.196 24.916 30.076 1.00 36.49 ? 29 ILE A C 1 ATOM 152 O O . ILE A 1 29 ? -60.218 25.425 30.494 1.00 39.21 ? 29 ILE A O 1 ATOM 153 C CB . ILE A 1 29 ? -56.965 25.824 30.807 1.00 35.95 ? 29 ILE A CB 1 ATOM 154 C CG1 . ILE A 1 29 ? -55.791 25.599 31.773 1.00 36.00 ? 29 ILE A CG1 1 ATOM 155 C CG2 . ILE A 1 29 ? -57.620 27.189 31.054 1.00 36.49 ? 29 ILE A CG2 1 ATOM 156 C CD1 . ILE A 1 29 ? -56.217 25.754 33.228 1.00 37.28 ? 29 ILE A CD1 1 ATOM 157 N N . THR A 1 30 ? -59.049 24.463 28.826 1.00 37.62 ? 30 THR A N 1 ATOM 158 C CA . THR A 1 30 ? -60.091 24.563 27.788 1.00 39.56 ? 30 THR A CA 1 ATOM 159 C C . THR A 1 30 ? -61.324 23.661 28.013 1.00 41.89 ? 30 THR A C 1 ATOM 160 O O . THR A 1 30 ? -62.438 24.043 27.674 1.00 42.58 ? 30 THR A O 1 ATOM 161 C CB . THR A 1 30 ? -59.495 24.217 26.395 1.00 39.90 ? 30 THR A CB 1 ATOM 162 O OG1 . THR A 1 30 ? -58.372 25.066 26.112 1.00 38.43 ? 30 THR A OG1 1 ATOM 163 C CG2 . THR A 1 30 ? -60.533 24.366 25.273 1.00 41.84 ? 30 THR A CG2 1 ATOM 164 N N . ASN A 1 31 ? -61.112 22.465 28.562 1.00 41.15 ? 31 ASN A N 1 ATOM 165 C CA . ASN A 1 31 ? -62.160 21.432 28.666 1.00 41.36 ? 31 ASN A CA 1 ATOM 166 C C . ASN A 1 31 ? -62.185 20.782 30.058 1.00 37.98 ? 31 ASN A C 1 ATOM 167 O O . ASN A 1 31 ? -61.157 20.343 30.535 1.00 32.89 ? 31 ASN A O 1 ATOM 168 C CB . ASN A 1 31 ? -61.839 20.317 27.664 1.00 43.88 ? 31 ASN A CB 1 ATOM 169 C CG . ASN A 1 31 ? -62.118 20.701 26.222 1.00 47.32 ? 31 ASN A CG 1 ATOM 170 O OD1 . ASN A 1 31 ? -63.278 20.793 25.819 1.00 51.37 ? 31 ASN A OD1 1 ATOM 171 N ND2 . ASN A 1 31 ? -61.054 20.887 25.421 1.00 44.56 ? 31 ASN A ND2 1 ATOM 172 N N . ASP A 1 32 ? -63.359 20.695 30.672 1.00 36.74 ? 32 ASP A N 1 ATOM 173 C CA A ASP A 1 32 ? -63.579 19.895 31.879 0.50 37.95 ? 32 ASP A CA 1 ATOM 174 C CA B ASP A 1 32 ? -63.548 19.910 31.879 0.50 37.44 ? 32 ASP A CA 1 ATOM 175 C C . ASP A 1 32 ? -63.234 18.421 31.639 1.00 37.45 ? 32 ASP A C 1 ATOM 176 O O . ASP A 1 32 ? -62.674 17.760 32.500 1.00 36.66 ? 32 ASP A O 1 ATOM 177 C CB A ASP A 1 32 ? -65.052 19.949 32.310 0.50 41.12 ? 32 ASP A CB 1 ATOM 178 C CB B ASP A 1 32 ? -64.988 20.068 32.355 0.50 39.89 ? 32 ASP A CB 1 ATOM 179 C CG A ASP A 1 32 ? -65.495 21.333 32.748 0.50 43.21 ? 32 ASP A CG 1 ATOM 180 C CG B ASP A 1 32 ? -65.266 19.325 33.633 0.50 40.75 ? 32 ASP A CG 1 ATOM 181 O OD1 A ASP A 1 32 ? -65.187 21.722 33.894 0.50 45.01 ? 32 ASP A OD1 1 ATOM 182 O OD1 B ASP A 1 32 ? -64.382 19.288 34.518 0.50 41.02 ? 32 ASP A OD1 1 ATOM 183 O OD2 A ASP A 1 32 ? -66.174 22.014 31.948 0.50 44.41 ? 32 ASP A OD2 1 ATOM 184 O OD2 B ASP A 1 32 ? -66.384 18.784 33.747 0.50 43.51 ? 32 ASP A OD2 1 ATOM 185 N N . GLN A 1 33 ? -63.589 17.924 30.461 1.00 35.37 ? 33 GLN A N 1 ATOM 186 C CA . GLN A 1 33 ? -63.407 16.525 30.091 1.00 37.10 ? 33 GLN A CA 1 ATOM 187 C C . GLN A 1 33 ? -62.917 16.461 28.668 1.00 34.75 ? 33 GLN A C 1 ATOM 188 O O . GLN A 1 33 ? -63.613 16.911 27.768 1.00 36.84 ? 33 GLN A O 1 ATOM 189 C CB . GLN A 1 33 ? -64.742 15.775 30.204 1.00 40.33 ? 33 GLN A CB 1 ATOM 190 C CG . GLN A 1 33 ? -65.243 15.669 31.637 1.00 43.68 ? 33 GLN A CG 1 ATOM 191 C CD . GLN A 1 33 ? -66.340 14.631 31.802 1.00 48.12 ? 33 GLN A CD 1 ATOM 192 O OE1 . GLN A 1 33 ? -67.226 14.512 30.957 1.00 51.72 ? 33 GLN A OE1 1 ATOM 193 N NE2 . GLN A 1 33 ? -66.268 13.855 32.879 1.00 49.74 ? 33 GLN A NE2 1 ATOM 194 N N . ILE A 1 34 ? -61.716 15.944 28.463 1.00 30.79 ? 34 ILE A N 1 ATOM 195 C CA . ILE A 1 34 ? -61.213 15.685 27.127 1.00 29.89 ? 34 ILE A CA 1 ATOM 196 C C . ILE A 1 34 ? -60.533 14.339 27.132 1.00 28.48 ? 34 ILE A C 1 ATOM 197 O O . ILE A 1 34 ? -59.793 14.022 28.068 1.00 26.16 ? 34 ILE A O 1 ATOM 198 C CB . ILE A 1 34 ? -60.267 16.803 26.612 1.00 30.66 ? 34 ILE A CB 1 ATOM 199 C CG1 . ILE A 1 34 ? -59.740 16.459 25.208 1.00 31.96 ? 34 ILE A CG1 1 ATOM 200 C CG2 . ILE A 1 34 ? -59.117 17.030 27.559 1.00 29.11 ? 34 ILE A CG2 1 ATOM 201 C CD1 . ILE A 1 34 ? -59.122 17.631 24.458 1.00 32.44 ? 34 ILE A CD1 1 ATOM 202 N N . GLU A 1 35 ? -60.826 13.522 26.111 1.00 27.81 ? 35 GLU A N 1 ATOM 203 C CA . GLU A 1 35 ? -60.211 12.222 26.040 1.00 28.60 ? 35 GLU A CA 1 ATOM 204 C C . GLU A 1 35 ? -58.840 12.337 25.365 1.00 26.24 ? 35 GLU A C 1 ATOM 205 O O . GLU A 1 35 ? -58.709 12.893 24.293 1.00 26.15 ? 35 GLU A O 1 ATOM 206 C CB . GLU A 1 35 ? -61.105 11.233 25.290 1.00 31.49 ? 35 GLU A CB 1 ATOM 207 C CG . GLU A 1 35 ? -60.701 9.791 25.473 1.00 34.84 ? 35 GLU A CG 1 ATOM 208 C CD . GLU A 1 35 ? -61.586 8.848 24.680 1.00 39.70 ? 35 GLU A CD 1 ATOM 209 O OE1 . GLU A 1 35 ? -62.757 8.656 25.072 1.00 47.60 ? 35 GLU A OE1 1 ATOM 210 O OE2 . GLU A 1 35 ? -61.117 8.312 23.656 1.00 42.02 ? 35 GLU A OE2 1 ATOM 211 N N . VAL A 1 36 ? -57.856 11.767 26.013 1.00 24.79 ? 36 VAL A N 1 ATOM 212 C CA . VAL A 1 36 ? -56.503 11.634 25.503 1.00 24.87 ? 36 VAL A CA 1 ATOM 213 C C . VAL A 1 36 ? -56.148 10.161 25.375 1.00 25.63 ? 36 VAL A C 1 ATOM 214 O O . VAL A 1 36 ? -56.876 9.302 25.870 1.00 26.52 ? 36 VAL A O 1 ATOM 215 C CB . VAL A 1 36 ? -55.507 12.380 26.404 1.00 24.40 ? 36 VAL A CB 1 ATOM 216 C CG1 . VAL A 1 36 ? -55.790 13.869 26.329 1.00 23.42 ? 36 VAL A CG1 1 ATOM 217 C CG2 . VAL A 1 36 ? -55.534 11.889 27.880 1.00 23.91 ? 36 VAL A CG2 1 ATOM 218 N N . THR A 1 37 ? -55.033 9.864 24.724 1.00 26.05 ? 37 THR A N 1 ATOM 219 C CA . THR A 1 37 ? -54.654 8.481 24.462 1.00 26.83 ? 37 THR A CA 1 ATOM 220 C C . THR A 1 37 ? -54.157 7.765 25.713 1.00 27.39 ? 37 THR A C 1 ATOM 221 O O . THR A 1 37 ? -54.243 6.561 25.817 1.00 28.06 ? 37 THR A O 1 ATOM 222 C CB . THR A 1 37 ? -53.600 8.390 23.354 1.00 26.94 ? 37 THR A CB 1 ATOM 223 O OG1 . THR A 1 37 ? -52.392 9.012 23.787 1.00 28.22 ? 37 THR A OG1 1 ATOM 224 C CG2 . THR A 1 37 ? -54.124 9.013 22.043 1.00 25.79 ? 37 THR A CG2 1 ATOM 225 N N . ASN A 1 38 ? -53.657 8.515 26.685 1.00 26.49 ? 38 ASN A N 1 ATOM 226 C CA . ASN A 1 38 ? -53.096 7.920 27.873 1.00 27.98 ? 38 ASN A CA 1 ATOM 227 C C . ASN A 1 38 ? -52.950 8.995 28.931 1.00 26.33 ? 38 ASN A C 1 ATOM 228 O O . ASN A 1 38 ? -52.821 10.175 28.586 1.00 24.24 ? 38 ASN A O 1 ATOM 229 C CB . ASN A 1 38 ? -51.739 7.313 27.566 1.00 30.55 ? 38 ASN A CB 1 ATOM 230 C CG . ASN A 1 38 ? -51.246 6.383 28.663 1.00 34.71 ? 38 ASN A CG 1 ATOM 231 O OD1 . ASN A 1 38 ? -52.028 5.786 29.415 1.00 34.61 ? 38 ASN A OD1 1 ATOM 232 N ND2 . ASN A 1 38 ? -49.935 6.263 28.752 1.00 43.32 ? 38 ASN A ND2 1 ATOM 233 N N . ALA A 1 39 ? -52.976 8.574 30.191 1.00 25.70 ? 39 ALA A N 1 ATOM 234 C CA . ALA A 1 39 ? -52.753 9.484 31.309 1.00 25.55 ? 39 ALA A CA 1 ATOM 235 C C . ALA A 1 39 ? -52.165 8.711 32.473 1.00 26.57 ? 39 ALA A C 1 ATOM 236 O O . ALA A 1 39 ? -52.119 7.471 32.471 1.00 27.23 ? 39 ALA A O 1 ATOM 237 C CB . ALA A 1 39 ? -54.064 10.176 31.694 1.00 24.90 ? 39 ALA A CB 1 ATOM 238 N N . THR A 1 40 ? -51.669 9.430 33.465 1.00 26.62 ? 40 THR A N 1 ATOM 239 C CA . THR A 1 40 ? -51.105 8.788 34.643 1.00 27.31 ? 40 THR A CA 1 ATOM 240 C C . THR A 1 40 ? -51.633 9.494 35.912 1.00 26.53 ? 40 THR A C 1 ATOM 241 O O . THR A 1 40 ? -51.914 10.691 35.900 1.00 26.41 ? 40 THR A O 1 ATOM 242 C CB . THR A 1 40 ? -49.565 8.757 34.550 1.00 28.37 ? 40 THR A CB 1 ATOM 243 O OG1 . THR A 1 40 ? -49.039 7.813 35.493 1.00 32.82 ? 40 THR A OG1 1 ATOM 244 C CG2 . THR A 1 40 ? -48.976 10.105 34.848 1.00 29.89 ? 40 THR A CG2 1 ATOM 245 N N . GLU A 1 41 ? -51.811 8.731 36.983 1.00 25.99 ? 41 GLU A N 1 ATOM 246 C CA . GLU A 1 41 ? -52.416 9.240 38.225 1.00 26.05 ? 41 GLU A CA 1 ATOM 247 C C . GLU A 1 41 ? -51.383 9.978 39.061 1.00 24.52 ? 41 GLU A C 1 ATOM 248 O O . GLU A 1 41 ? -50.280 9.456 39.300 1.00 24.62 ? 41 GLU A O 1 ATOM 249 C CB . GLU A 1 41 ? -53.004 8.054 38.992 1.00 26.87 ? 41 GLU A CB 1 ATOM 250 C CG . GLU A 1 41 ? -53.641 8.347 40.335 1.00 27.12 ? 41 GLU A CG 1 ATOM 251 C CD . GLU A 1 41 ? -54.736 9.374 40.262 1.00 27.89 ? 41 GLU A CD 1 ATOM 252 O OE1 . GLU A 1 41 ? -55.818 9.008 39.750 1.00 28.06 ? 41 GLU A OE1 1 ATOM 253 O OE2 . GLU A 1 41 ? -54.512 10.557 40.692 1.00 25.56 ? 41 GLU A OE2 1 ATOM 254 N N . LEU A 1 42 ? -51.718 11.181 39.529 1.00 22.38 ? 42 LEU A N 1 ATOM 255 C CA . LEU A 1 42 ? -50.772 11.978 40.340 1.00 21.59 ? 42 LEU A CA 1 ATOM 256 C C . LEU A 1 42 ? -51.112 11.999 41.833 1.00 20.71 ? 42 LEU A C 1 ATOM 257 O O . LEU A 1 42 ? -50.387 12.560 42.612 1.00 20.02 ? 42 LEU A O 1 ATOM 258 C CB . LEU A 1 42 ? -50.704 13.409 39.827 1.00 21.14 ? 42 LEU A CB 1 ATOM 259 C CG . LEU A 1 42 ? -50.071 13.563 38.430 1.00 21.67 ? 42 LEU A CG 1 ATOM 260 C CD1 . LEU A 1 42 ? -49.824 15.039 38.201 1.00 21.92 ? 42 LEU A CD1 1 ATOM 261 C CD2 . LEU A 1 42 ? -48.753 12.759 38.306 1.00 21.57 ? 42 LEU A CD2 1 ATOM 262 N N . VAL A 1 43 ? -52.224 11.403 42.221 1.00 20.58 ? 43 VAL A N 1 ATOM 263 C CA . VAL A 1 43 ? -52.610 11.300 43.619 1.00 20.80 ? 43 VAL A CA 1 ATOM 264 C C . VAL A 1 43 ? -52.487 9.855 44.075 1.00 21.78 ? 43 VAL A C 1 ATOM 265 O O . VAL A 1 43 ? -53.193 8.945 43.586 1.00 21.49 ? 43 VAL A O 1 ATOM 266 C CB . VAL A 1 43 ? -54.044 11.808 43.860 1.00 20.78 ? 43 VAL A CB 1 ATOM 267 C CG1 . VAL A 1 43 ? -54.435 11.682 45.342 1.00 21.09 ? 43 VAL A CG1 1 ATOM 268 C CG2 . VAL A 1 43 ? -54.166 13.263 43.383 1.00 20.55 ? 43 VAL A CG2 1 ATOM 269 N N . GLN A 1 44 ? -51.617 9.647 45.044 1.00 21.70 ? 44 GLN A N 1 ATOM 270 C CA . GLN A 1 44 ? -51.531 8.358 45.718 1.00 22.90 ? 44 GLN A CA 1 ATOM 271 C C . GLN A 1 44 ? -52.701 8.165 46.691 1.00 24.61 ? 44 GLN A C 1 ATOM 272 O O . GLN A 1 44 ? -52.868 8.945 47.636 1.00 23.25 ? 44 GLN A O 1 ATOM 273 C CB . GLN A 1 44 ? -50.198 8.260 46.461 1.00 22.34 ? 44 GLN A CB 1 ATOM 274 C CG . GLN A 1 44 ? -49.927 6.921 47.095 1.00 23.02 ? 44 GLN A CG 1 ATOM 275 C CD . GLN A 1 44 ? -49.735 5.814 46.076 1.00 24.39 ? 44 GLN A CD 1 ATOM 276 O OE1 . GLN A 1 44 ? -49.108 6.015 45.058 1.00 25.32 ? 44 GLN A OE1 1 ATOM 277 N NE2 . GLN A 1 44 ? -50.311 4.665 46.343 1.00 25.12 ? 44 GLN A NE2 1 ATOM 278 N N . SER A 1 45 ? -53.501 7.127 46.484 1.00 25.52 ? 45 SER A N 1 ATOM 279 C CA . SER A 1 45 ? -54.702 6.942 47.301 1.00 29.11 ? 45 SER A CA 1 ATOM 280 C C . SER A 1 45 ? -54.739 5.640 48.123 1.00 30.90 ? 45 SER A C 1 ATOM 281 O O . SER A 1 45 ? -55.647 5.427 48.915 1.00 33.01 ? 45 SER A O 1 ATOM 282 C CB . SER A 1 45 ? -55.963 7.152 46.459 1.00 31.36 ? 45 SER A CB 1 ATOM 283 O OG . SER A 1 45 ? -56.066 6.159 45.468 1.00 34.48 ? 45 SER A OG 1 ATOM 284 N N . SER A 1 46 ? -53.733 4.795 47.996 1.00 31.72 ? 46 SER A N 1 ATOM 285 C CA . SER A 1 46 ? -53.712 3.563 48.800 1.00 35.08 ? 46 SER A CA 1 ATOM 286 C C . SER A 1 46 ? -52.425 3.450 49.571 1.00 34.68 ? 46 SER A C 1 ATOM 287 O O . SER A 1 46 ? -51.395 4.025 49.182 1.00 31.23 ? 46 SER A O 1 ATOM 288 C CB . SER A 1 46 ? -53.838 2.338 47.889 1.00 35.39 ? 46 SER A CB 1 ATOM 289 O OG . SER A 1 46 ? -52.773 2.353 46.947 1.00 35.72 ? 46 SER A OG 1 ATOM 290 N N . SER A 1 47 ? -52.494 2.717 50.680 1.00 37.97 ? 47 SER A N 1 ATOM 291 C CA . SER A 1 47 ? -51.306 2.253 51.397 1.00 38.68 ? 47 SER A CA 1 ATOM 292 C C . SER A 1 47 ? -51.399 0.740 51.515 1.00 42.15 ? 47 SER A C 1 ATOM 293 O O . SER A 1 47 ? -52.487 0.202 51.546 1.00 43.59 ? 47 SER A O 1 ATOM 294 C CB . SER A 1 47 ? -51.243 2.805 52.819 1.00 40.05 ? 47 SER A CB 1 ATOM 295 O OG . SER A 1 47 ? -50.167 2.178 53.523 1.00 40.58 ? 47 SER A OG 1 ATOM 296 N N . THR A 1 48 ? -50.239 0.098 51.621 1.00 46.11 ? 48 THR A N 1 ATOM 297 C CA . THR A 1 48 ? -50.097 -1.316 51.997 1.00 50.14 ? 48 THR A CA 1 ATOM 298 C C . THR A 1 48 ? -50.754 -1.643 53.330 1.00 49.66 ? 48 THR A C 1 ATOM 299 O O . THR A 1 48 ? -51.183 -2.774 53.566 1.00 52.44 ? 48 THR A O 1 ATOM 300 C CB . THR A 1 48 ? -48.608 -1.662 52.199 1.00 52.01 ? 48 THR A CB 1 ATOM 301 O OG1 . THR A 1 48 ? -47.842 -1.189 51.079 1.00 54.29 ? 48 THR A OG1 1 ATOM 302 C CG2 . THR A 1 48 ? -48.427 -3.158 52.374 1.00 52.57 ? 48 THR A CG2 1 ATOM 303 N N . GLY A 1 49 ? -50.772 -0.660 54.225 1.00 46.92 ? 49 GLY A N 1 ATOM 304 C CA . GLY A 1 49 ? -51.366 -0.846 55.528 1.00 46.58 ? 49 GLY A CA 1 ATOM 305 C C . GLY A 1 49 ? -50.346 -1.190 56.594 1.00 45.15 ? 49 GLY A C 1 ATOM 306 O O . GLY A 1 49 ? -50.719 -1.227 57.769 1.00 48.33 ? 49 GLY A O 1 ATOM 307 N N . GLY A 1 50 ? -49.086 -1.459 56.197 1.00 37.88 ? 50 GLY A N 1 ATOM 308 C CA . GLY A 1 50 ? -47.992 -1.634 57.154 1.00 34.64 ? 50 GLY A CA 1 ATOM 309 C C . GLY A 1 50 ? -46.993 -0.489 57.111 1.00 30.40 ? 50 GLY A C 1 ATOM 310 O O . GLY A 1 50 ? -46.756 0.080 56.036 1.00 28.18 ? 50 GLY A O 1 ATOM 311 N N . ILE A 1 51 ? -46.413 -0.152 58.272 1.00 27.69 ? 51 ILE A N 1 ATOM 312 C CA . ILE A 1 51 ? -45.310 0.786 58.343 1.00 26.81 ? 51 ILE A CA 1 ATOM 313 C C . ILE A 1 51 ? -44.011 -0.011 58.118 1.00 28.67 ? 51 ILE A C 1 ATOM 314 O O . ILE A 1 51 ? -43.683 -0.870 58.934 1.00 28.20 ? 51 ILE A O 1 ATOM 315 C CB . ILE A 1 51 ? -45.254 1.477 59.717 1.00 26.94 ? 51 ILE A CB 1 ATOM 316 C CG1 . ILE A 1 51 ? -46.457 2.411 59.907 1.00 27.24 ? 51 ILE A CG1 1 ATOM 317 C CG2 . ILE A 1 51 ? -43.958 2.303 59.840 1.00 27.82 ? 51 ILE A CG2 1 ATOM 318 C CD1 . ILE A 1 51 ? -46.658 2.902 61.328 1.00 27.60 ? 51 ILE A CD1 1 ATOM 319 N N . CYS A 1 52 ? -43.286 0.282 57.041 1.00 27.56 ? 52 CYS A N 1 ATOM 320 C CA . CYS A 1 52 ? -42.011 -0.391 56.757 1.00 29.18 ? 52 CYS A CA 1 ATOM 321 C C . CYS A 1 52 ? -40.933 0.026 57.753 1.00 28.72 ? 52 CYS A C 1 ATOM 322 O O . CYS A 1 52 ? -40.780 1.228 58.032 1.00 26.27 ? 52 CYS A O 1 ATOM 323 C CB . CYS A 1 52 ? -41.572 -0.040 55.340 1.00 31.84 ? 52 CYS A CB 1 ATOM 324 S SG . CYS A 1 52 ? -42.648 -0.745 54.059 1.00 34.95 ? 52 CYS A SG 1 ATOM 325 N N . ASP A 1 53 ? -40.180 -0.959 58.261 1.00 27.59 ? 53 ASP A N 1 ATOM 326 C CA . ASP A 1 53 ? -39.147 -0.717 59.268 1.00 27.96 ? 53 ASP A CA 1 ATOM 327 C C . ASP A 1 53 ? -37.847 -0.142 58.707 1.00 27.04 ? 53 ASP A C 1 ATOM 328 O O . ASP A 1 53 ? -36.916 0.134 59.467 1.00 28.14 ? 53 ASP A O 1 ATOM 329 C CB . ASP A 1 53 ? -38.856 -1.987 60.061 1.00 29.17 ? 53 ASP A CB 1 ATOM 330 C CG . ASP A 1 53 ? -38.145 -3.070 59.240 1.00 30.88 ? 53 ASP A CG 1 ATOM 331 O OD1 . ASP A 1 53 ? -37.787 -2.841 58.051 1.00 30.97 ? 53 ASP A OD1 1 ATOM 332 O OD2 . ASP A 1 53 ? -37.936 -4.181 59.806 1.00 31.97 ? 53 ASP A OD2 1 ATOM 333 N N . SER A 1 54 ? -37.782 0.023 57.395 1.00 26.12 ? 54 SER A N 1 ATOM 334 C CA . SER A 1 54 ? -36.664 0.648 56.702 1.00 25.74 ? 54 SER A CA 1 ATOM 335 C C . SER A 1 54 ? -37.168 1.737 55.753 1.00 25.40 ? 54 SER A C 1 ATOM 336 O O . SER A 1 54 ? -38.328 1.642 55.269 1.00 24.82 ? 54 SER A O 1 ATOM 337 C CB . SER A 1 54 ? -35.922 -0.428 55.907 1.00 26.87 ? 54 SER A CB 1 ATOM 338 O OG . SER A 1 54 ? -35.582 -1.512 56.757 1.00 27.17 ? 54 SER A OG 1 ATOM 339 N N . PRO A 1 55 ? -36.351 2.778 55.487 1.00 24.89 ? 55 PRO A N 1 ATOM 340 C CA . PRO A 1 55 ? -35.018 3.086 55.970 1.00 26.10 ? 55 PRO A CA 1 ATOM 341 C C . PRO A 1 55 ? -34.936 3.955 57.260 1.00 25.86 ? 55 PRO A C 1 ATOM 342 O O . PRO A 1 55 ? -33.813 4.280 57.714 1.00 24.93 ? 55 PRO A O 1 ATOM 343 C CB . PRO A 1 55 ? -34.437 3.874 54.820 1.00 25.36 ? 55 PRO A CB 1 ATOM 344 C CG . PRO A 1 55 ? -35.612 4.755 54.375 1.00 25.25 ? 55 PRO A CG 1 ATOM 345 C CD . PRO A 1 55 ? -36.827 3.854 54.573 1.00 25.67 ? 55 PRO A CD 1 ATOM 346 N N . HIS A 1 56 ? -36.089 4.330 57.822 1.00 24.36 ? 56 HIS A N 1 ATOM 347 C CA . HIS A 1 56 ? -36.140 5.095 59.053 1.00 24.48 ? 56 HIS A CA 1 ATOM 348 C C . HIS A 1 56 ? -36.101 4.176 60.234 1.00 25.00 ? 56 HIS A C 1 ATOM 349 O O . HIS A 1 56 ? -36.630 3.044 60.184 1.00 25.22 ? 56 HIS A O 1 ATOM 350 C CB . HIS A 1 56 ? -37.395 5.963 59.110 1.00 24.92 ? 56 HIS A CB 1 ATOM 351 C CG . HIS A 1 56 ? -37.608 6.807 57.892 1.00 24.52 ? 56 HIS A CG 1 ATOM 352 N ND1 . HIS A 1 56 ? -36.783 7.836 57.555 1.00 24.63 ? 56 HIS A ND1 1 ATOM 353 C CD2 . HIS A 1 56 ? -38.597 6.759 56.916 1.00 25.12 ? 56 HIS A CD2 1 ATOM 354 C CE1 . HIS A 1 56 ? -37.233 8.412 56.425 1.00 24.72 ? 56 HIS A CE1 1 ATOM 355 N NE2 . HIS A 1 56 ? -38.353 7.763 56.042 1.00 24.66 ? 56 HIS A NE2 1 ATOM 356 N N . GLN A 1 57 ? -35.475 4.644 61.313 1.00 24.66 ? 57 GLN A N 1 ATOM 357 C CA . GLN A 1 57 ? -35.428 3.889 62.542 1.00 23.59 ? 57 GLN A CA 1 ATOM 358 C C . GLN A 1 57 ? -36.730 4.035 63.281 1.00 23.12 ? 57 GLN A C 1 ATOM 359 O O . GLN A 1 57 ? -37.077 5.112 63.800 1.00 22.84 ? 57 GLN A O 1 ATOM 360 C CB . GLN A 1 57 ? -34.297 4.345 63.462 1.00 24.00 ? 57 GLN A CB 1 ATOM 361 C CG . GLN A 1 57 ? -34.189 3.485 64.719 1.00 23.65 ? 57 GLN A CG 1 ATOM 362 C CD . GLN A 1 57 ? -33.018 3.852 65.615 1.00 24.61 ? 57 GLN A CD 1 ATOM 363 O OE1 . GLN A 1 57 ? -32.574 5.007 65.655 1.00 25.97 ? 57 GLN A OE1 1 ATOM 364 N NE2 . GLN A 1 57 ? -32.540 2.875 66.367 1.00 23.60 ? 57 GLN A NE2 1 ATOM 365 N N . ILE A 1 58 ? -37.461 2.941 63.325 1.00 23.41 ? 58 ILE A N 1 ATOM 366 C CA . ILE A 1 58 ? -38.768 2.917 63.926 1.00 24.30 ? 58 ILE A CA 1 ATOM 367 C C . ILE A 1 58 ? -38.672 2.382 65.344 1.00 25.80 ? 58 ILE A C 1 ATOM 368 O O . ILE A 1 58 ? -37.943 1.408 65.596 1.00 28.43 ? 58 ILE A O 1 ATOM 369 C CB . ILE A 1 58 ? -39.709 2.007 63.115 1.00 25.86 ? 58 ILE A CB 1 ATOM 370 C CG1 . ILE A 1 58 ? -39.756 2.448 61.644 1.00 26.40 ? 58 ILE A CG1 1 ATOM 371 C CG2 . ILE A 1 58 ? -41.104 2.007 63.730 1.00 26.42 ? 58 ILE A CG2 1 ATOM 372 C CD1 . ILE A 1 58 ? -40.225 3.856 61.362 1.00 27.02 ? 58 ILE A CD1 1 ATOM 373 N N . LEU A 1 59 ? -39.380 3.004 66.281 1.00 24.90 ? 59 LEU A N 1 ATOM 374 C CA . LEU A 1 59 ? -39.519 2.454 67.625 1.00 25.89 ? 59 LEU A CA 1 ATOM 375 C C . LEU A 1 59 ? -41.002 2.268 67.907 1.00 26.04 ? 59 LEU A C 1 ATOM 376 O O . LEU A 1 59 ? -41.744 3.248 68.021 1.00 26.02 ? 59 LEU A O 1 ATOM 377 C CB . LEU A 1 59 ? -38.881 3.352 68.672 1.00 25.47 ? 59 LEU A CB 1 ATOM 378 C CG . LEU A 1 59 ? -38.892 2.858 70.117 1.00 27.15 ? 59 LEU A CG 1 ATOM 379 C CD1 . LEU A 1 59 ? -38.458 1.393 70.161 1.00 28.16 ? 59 LEU A CD1 1 ATOM 380 C CD2 . LEU A 1 59 ? -37.971 3.738 70.961 1.00 26.14 ? 59 LEU A CD2 1 ATOM 381 N N . ASP A 1 60 ? -41.422 1.012 67.958 1.00 25.79 ? 60 ASP A N 1 ATOM 382 C CA . ASP A 1 60 ? -42.819 0.672 68.271 1.00 25.91 ? 60 ASP A CA 1 ATOM 383 C C . ASP A 1 60 ? -43.045 0.724 69.769 1.00 26.50 ? 60 ASP A C 1 ATOM 384 O O . ASP A 1 60 ? -42.469 -0.064 70.509 1.00 26.99 ? 60 ASP A O 1 ATOM 385 C CB . ASP A 1 60 ? -43.134 -0.721 67.763 1.00 27.17 ? 60 ASP A CB 1 ATOM 386 C CG . ASP A 1 60 ? -44.611 -1.089 67.907 1.00 27.97 ? 60 ASP A CG 1 ATOM 387 O OD1 . ASP A 1 60 ? -45.355 -0.376 68.636 1.00 27.16 ? 60 ASP A OD1 1 ATOM 388 O OD2 . ASP A 1 60 ? -45.009 -2.104 67.280 1.00 29.81 ? 60 ASP A OD2 1 ATOM 389 N N . GLY A 1 61 ? -43.864 1.670 70.224 1.00 26.48 ? 61 GLY A N 1 ATOM 390 C CA . GLY A 1 61 ? -44.142 1.840 71.638 1.00 27.08 ? 61 GLY A CA 1 ATOM 391 C C . GLY A 1 61 ? -44.886 0.673 72.281 1.00 28.91 ? 61 GLY A C 1 ATOM 392 O O . GLY A 1 61 ? -44.837 0.495 73.498 1.00 29.46 ? 61 GLY A O 1 ATOM 393 N N . GLU A 1 62 ? -45.551 -0.132 71.467 1.00 30.25 ? 62 GLU A N 1 ATOM 394 C CA . GLU A 1 62 ? -46.348 -1.272 71.958 1.00 32.15 ? 62 GLU A CA 1 ATOM 395 C C . GLU A 1 62 ? -47.326 -0.787 73.035 1.00 32.03 ? 62 GLU A C 1 ATOM 396 O O . GLU A 1 62 ? -48.177 0.053 72.737 1.00 30.54 ? 62 GLU A O 1 ATOM 397 C CB . GLU A 1 62 ? -45.409 -2.405 72.405 1.00 35.31 ? 62 GLU A CB 1 ATOM 398 C CG . GLU A 1 62 ? -44.463 -2.780 71.267 1.00 37.72 ? 62 GLU A CG 1 ATOM 399 C CD . GLU A 1 62 ? -43.704 -4.079 71.460 1.00 42.46 ? 62 GLU A CD 1 ATOM 400 O OE1 . GLU A 1 62 ? -42.623 -4.066 72.102 1.00 44.35 ? 62 GLU A OE1 1 ATOM 401 O OE2 . GLU A 1 62 ? -44.167 -5.106 70.904 1.00 46.93 ? 62 GLU A OE2 1 ATOM 402 N N . ASN A 1 63 ? -47.206 -1.264 74.278 1.00 32.37 ? 63 ASN A N 1 ATOM 403 C CA . ASN A 1 63 ? -48.106 -0.816 75.355 1.00 34.06 ? 63 ASN A CA 1 ATOM 404 C C . ASN A 1 63 ? -47.729 0.502 76.050 1.00 32.57 ? 63 ASN A C 1 ATOM 405 O O . ASN A 1 63 ? -48.431 0.938 76.954 1.00 32.31 ? 63 ASN A O 1 ATOM 406 C CB . ASN A 1 63 ? -48.212 -1.908 76.426 1.00 37.53 ? 63 ASN A CB 1 ATOM 407 C CG . ASN A 1 63 ? -49.031 -3.087 75.962 1.00 41.23 ? 63 ASN A CG 1 ATOM 408 O OD1 . ASN A 1 63 ? -49.933 -2.945 75.120 1.00 42.31 ? 63 ASN A OD1 1 ATOM 409 N ND2 . ASN A 1 63 ? -48.733 -4.254 76.507 1.00 46.61 ? 63 ASN A ND2 1 ATOM 410 N N . CYS A 1 64 ? -46.646 1.141 75.608 1.00 31.55 ? 64 CYS A N 1 ATOM 411 C CA . CYS A 1 64 ? -46.109 2.318 76.258 1.00 31.62 ? 64 CYS A CA 1 ATOM 412 C C . CYS A 1 64 ? -46.248 3.566 75.400 1.00 30.71 ? 64 CYS A C 1 ATOM 413 O O . CYS A 1 64 ? -45.934 3.535 74.204 1.00 29.79 ? 64 CYS A O 1 ATOM 414 C CB . CYS A 1 64 ? -44.619 2.112 76.522 1.00 34.28 ? 64 CYS A CB 1 ATOM 415 S SG . CYS A 1 64 ? -44.214 0.756 77.671 1.00 38.08 ? 64 CYS A SG 1 ATOM 416 N N . THR A 1 65 ? -46.658 4.672 76.021 1.00 28.76 ? 65 THR A N 1 ATOM 417 C CA . THR A 1 65 ? -46.471 5.972 75.428 1.00 27.42 ? 65 THR A CA 1 ATOM 418 C C . THR A 1 65 ? -45.018 6.365 75.580 1.00 26.30 ? 65 THR A C 1 ATOM 419 O O . THR A 1 65 ? -44.270 5.776 76.410 1.00 26.29 ? 65 THR A O 1 ATOM 420 C CB . THR A 1 65 ? -47.332 7.024 76.114 1.00 27.51 ? 65 THR A CB 1 ATOM 421 O OG1 . THR A 1 65 ? -46.906 7.128 77.475 1.00 28.42 ? 65 THR A OG1 1 ATOM 422 C CG2 . THR A 1 65 ? -48.848 6.612 76.067 1.00 29.32 ? 65 THR A CG2 1 ATOM 423 N N . LEU A 1 66 ? -44.616 7.380 74.821 1.00 25.70 ? 66 LEU A N 1 ATOM 424 C CA . LEU A 1 66 ? -43.265 7.929 74.943 1.00 25.51 ? 66 LEU A CA 1 ATOM 425 C C . LEU A 1 66 ? -43.032 8.409 76.377 1.00 25.47 ? 66 LEU A C 1 ATOM 426 O O . LEU A 1 66 ? -41.961 8.167 76.955 1.00 24.51 ? 66 LEU A O 1 ATOM 427 C CB . LEU A 1 66 ? -43.052 9.083 73.956 1.00 25.38 ? 66 LEU A CB 1 ATOM 428 C CG . LEU A 1 66 ? -41.702 9.827 74.036 1.00 25.60 ? 66 LEU A CG 1 ATOM 429 C CD1 . LEU A 1 66 ? -40.564 8.826 74.006 1.00 25.61 ? 66 LEU A CD1 1 ATOM 430 C CD2 . LEU A 1 66 ? -41.569 10.868 72.904 1.00 23.52 ? 66 LEU A CD2 1 ATOM 431 N N . ILE A 1 67 ? -44.028 9.097 76.939 1.00 27.42 ? 67 ILE A N 1 ATOM 432 C CA . ILE A 1 67 ? -43.879 9.675 78.288 1.00 28.49 ? 67 ILE A CA 1 ATOM 433 C C . ILE A 1 67 ? -43.738 8.540 79.312 1.00 28.50 ? 67 ILE A C 1 ATOM 434 O O . ILE A 1 67 ? -42.903 8.636 80.219 1.00 30.12 ? 67 ILE A O 1 ATOM 435 C CB . ILE A 1 67 ? -45.014 10.680 78.652 1.00 28.96 ? 67 ILE A CB 1 ATOM 436 C CG1 . ILE A 1 67 ? -44.935 11.983 77.838 1.00 30.48 ? 67 ILE A CG1 1 ATOM 437 C CG2 . ILE A 1 67 ? -44.990 11.045 80.142 1.00 30.04 ? 67 ILE A CG2 1 ATOM 438 C CD1 . ILE A 1 67 ? -43.553 12.579 77.651 1.00 31.28 ? 67 ILE A CD1 1 ATOM 439 N N . ASP A 1 68 ? -44.478 7.432 79.149 1.00 29.25 ? 68 ASP A N 1 ATOM 440 C CA . ASP A 1 68 ? -44.300 6.282 80.062 1.00 29.76 ? 68 ASP A CA 1 ATOM 441 C C . ASP A 1 68 ? -42.889 5.694 79.942 1.00 29.50 ? 68 ASP A C 1 ATOM 442 O O . ASP A 1 68 ? -42.246 5.341 80.954 1.00 29.52 ? 68 ASP A O 1 ATOM 443 C CB . ASP A 1 68 ? -45.356 5.190 79.840 1.00 31.33 ? 68 ASP A CB 1 ATOM 444 C CG . ASP A 1 68 ? -46.706 5.544 80.457 1.00 34.21 ? 68 ASP A CG 1 ATOM 445 O OD1 . ASP A 1 68 ? -46.788 6.482 81.259 1.00 36.48 ? 68 ASP A OD1 1 ATOM 446 O OD2 . ASP A 1 68 ? -47.720 4.909 80.125 1.00 39.58 ? 68 ASP A OD2 1 ATOM 447 N N . ALA A 1 69 ? -42.398 5.603 78.710 1.00 28.19 ? 69 ALA A N 1 ATOM 448 C CA . ALA A 1 69 ? -41.045 5.130 78.454 1.00 28.28 ? 69 ALA A CA 1 ATOM 449 C C . ALA A 1 69 ? -39.994 6.062 79.052 1.00 28.97 ? 69 ALA A C 1 ATOM 450 O O . ALA A 1 69 ? -38.943 5.596 79.537 1.00 29.46 ? 69 ALA A O 1 ATOM 451 C CB . ALA A 1 69 ? -40.815 4.969 76.949 1.00 28.83 ? 69 ALA A CB 1 ATOM 452 N N . LEU A 1 70 ? -40.265 7.371 79.000 1.00 27.42 ? 70 LEU A N 1 ATOM 453 C CA . LEU A 1 70 ? -39.384 8.394 79.586 1.00 27.40 ? 70 LEU A CA 1 ATOM 454 C C . LEU A 1 70 ? -39.265 8.220 81.118 1.00 28.44 ? 70 LEU A C 1 ATOM 455 O O . LEU A 1 70 ? -38.168 8.115 81.666 1.00 28.27 ? 70 LEU A O 1 ATOM 456 C CB . LEU A 1 70 ? -39.950 9.785 79.274 1.00 26.66 ? 70 LEU A CB 1 ATOM 457 C CG . LEU A 1 70 ? -39.196 11.029 79.766 1.00 26.58 ? 70 LEU A CG 1 ATOM 458 C CD1 . LEU A 1 70 ? -37.955 11.292 78.919 1.00 26.79 ? 70 LEU A CD1 1 ATOM 459 C CD2 . LEU A 1 70 ? -40.079 12.280 79.751 1.00 26.67 ? 70 LEU A CD2 1 ATOM 460 N N . LEU A 1 71 ? -40.407 8.220 81.792 1.00 28.48 ? 71 LEU A N 1 ATOM 461 C CA . LEU A 1 71 ? -40.447 8.133 83.254 1.00 30.35 ? 71 LEU A CA 1 ATOM 462 C C . LEU A 1 71 ? -39.893 6.788 83.736 1.00 30.46 ? 71 LEU A C 1 ATOM 463 O O . LEU A 1 71 ? -39.269 6.719 84.785 1.00 31.79 ? 71 LEU A O 1 ATOM 464 C CB . LEU A 1 71 ? -41.886 8.324 83.762 1.00 30.62 ? 71 LEU A CB 1 ATOM 465 C CG . LEU A 1 71 ? -42.645 9.609 83.411 1.00 31.32 ? 71 LEU A CG 1 ATOM 466 C CD1 . LEU A 1 71 ? -44.026 9.603 84.058 1.00 32.09 ? 71 LEU A CD1 1 ATOM 467 C CD2 . LEU A 1 71 ? -41.899 10.861 83.840 1.00 32.58 ? 71 LEU A CD2 1 ATOM 468 N N . GLY A 1 72 ? -40.098 5.735 82.958 1.00 31.04 ? 72 GLY A N 1 ATOM 469 C CA . GLY A 1 72 ? -39.579 4.412 83.309 1.00 30.99 ? 72 GLY A CA 1 ATOM 470 C C . GLY A 1 72 ? -40.612 3.510 83.984 1.00 33.24 ? 72 GLY A C 1 ATOM 471 O O . GLY A 1 72 ? -40.304 2.826 84.960 1.00 31.73 ? 72 GLY A O 1 ATOM 472 N N . ASP A 1 73 ? -41.843 3.534 83.473 1.00 33.39 ? 73 ASP A N 1 ATOM 473 C CA . ASP A 1 73 ? -42.876 2.543 83.825 1.00 35.04 ? 73 ASP A CA 1 ATOM 474 C C . ASP A 1 73 ? -42.266 1.130 83.612 1.00 35.96 ? 73 ASP A C 1 ATOM 475 O O . ASP A 1 73 ? -41.589 0.900 82.617 1.00 33.76 ? 73 ASP A O 1 ATOM 476 C CB . ASP A 1 73 ? -44.107 2.821 82.940 1.00 36.12 ? 73 ASP A CB 1 ATOM 477 C CG . ASP A 1 73 ? -45.325 1.964 83.285 1.00 38.10 ? 73 ASP A CG 1 ATOM 478 O OD1 . ASP A 1 73 ? -45.161 0.829 83.755 1.00 41.30 ? 73 ASP A OD1 1 ATOM 479 O OD2 . ASP A 1 73 ? -46.450 2.433 83.067 1.00 38.95 ? 73 ASP A OD2 1 ATOM 480 N N . PRO A 1 74 ? -42.428 0.199 84.582 1.00 38.45 ? 74 PRO A N 1 ATOM 481 C CA . PRO A 1 74 ? -41.776 -1.124 84.456 1.00 40.05 ? 74 PRO A CA 1 ATOM 482 C C . PRO A 1 74 ? -42.002 -1.866 83.132 1.00 40.28 ? 74 PRO A C 1 ATOM 483 O O . PRO A 1 74 ? -41.047 -2.441 82.581 1.00 40.17 ? 74 PRO A O 1 ATOM 484 C CB . PRO A 1 74 ? -42.356 -1.906 85.639 1.00 42.27 ? 74 PRO A CB 1 ATOM 485 C CG . PRO A 1 74 ? -42.522 -0.842 86.686 1.00 42.05 ? 74 PRO A CG 1 ATOM 486 C CD . PRO A 1 74 ? -42.981 0.395 85.933 1.00 39.93 ? 74 PRO A CD 1 ATOM 487 N N . GLN A 1 75 ? -43.214 -1.804 82.586 1.00 39.84 ? 75 GLN A N 1 ATOM 488 C CA . GLN A 1 75 ? -43.466 -2.451 81.299 1.00 40.26 ? 75 GLN A CA 1 ATOM 489 C C . GLN A 1 75 ? -42.669 -1.824 80.153 1.00 37.18 ? 75 GLN A C 1 ATOM 490 O O . GLN A 1 75 ? -42.575 -2.425 79.093 1.00 35.58 ? 75 GLN A O 1 ATOM 491 C CB . GLN A 1 75 ? -44.959 -2.535 80.975 1.00 41.61 ? 75 GLN A CB 1 ATOM 492 C CG . GLN A 1 75 ? -45.615 -1.249 80.532 1.00 43.23 ? 75 GLN A CG 1 ATOM 493 C CD . GLN A 1 75 ? -47.124 -1.380 80.430 1.00 45.33 ? 75 GLN A CD 1 ATOM 494 O OE1 . GLN A 1 75 ? -47.661 -2.482 80.502 1.00 50.05 ? 75 GLN A OE1 1 ATOM 495 N NE2 . GLN A 1 75 ? -47.815 -0.257 80.262 1.00 44.40 ? 75 GLN A NE2 1 ATOM 496 N N . CYS A 1 76 ? -42.078 -0.645 80.382 1.00 35.07 ? 76 CYS A N 1 ATOM 497 C CA . CYS A 1 76 ? -41.277 0.035 79.365 1.00 34.86 ? 76 CYS A CA 1 ATOM 498 C C . CYS A 1 76 ? -39.781 -0.067 79.587 1.00 34.39 ? 76 CYS A C 1 ATOM 499 O O . CYS A 1 76 ? -39.036 0.660 78.945 1.00 32.64 ? 76 CYS A O 1 ATOM 500 C CB . CYS A 1 76 ? -41.636 1.516 79.291 1.00 36.92 ? 76 CYS A CB 1 ATOM 501 S SG . CYS A 1 76 ? -43.394 1.830 79.311 1.00 37.58 ? 76 CYS A SG 1 ATOM 502 N N . ASP A 1 77 ? -39.333 -0.969 80.466 1.00 33.30 ? 77 ASP A N 1 ATOM 503 C CA . ASP A 1 77 ? -37.898 -1.078 80.779 1.00 34.82 ? 77 ASP A CA 1 ATOM 504 C C . ASP A 1 77 ? -37.029 -1.419 79.558 1.00 33.62 ? 77 ASP A C 1 ATOM 505 O O . ASP A 1 77 ? -35.855 -1.016 79.468 1.00 32.54 ? 77 ASP A O 1 ATOM 506 C CB . ASP A 1 77 ? -37.664 -2.118 81.893 1.00 36.75 ? 77 ASP A CB 1 ATOM 507 C CG . ASP A 1 77 ? -38.037 -1.601 83.277 1.00 38.42 ? 77 ASP A CG 1 ATOM 508 O OD1 . ASP A 1 77 ? -38.258 -0.377 83.449 1.00 37.90 ? 77 ASP A OD1 1 ATOM 509 O OD2 . ASP A 1 77 ? -38.080 -2.422 84.221 1.00 37.84 ? 77 ASP A OD2 1 ATOM 510 N N . GLY A 1 78 ? -37.624 -2.133 78.609 1.00 34.43 ? 78 GLY A N 1 ATOM 511 C CA . GLY A 1 78 ? -36.962 -2.479 77.363 1.00 34.74 ? 78 GLY A CA 1 ATOM 512 C C . GLY A 1 78 ? -36.578 -1.280 76.492 1.00 32.42 ? 78 GLY A C 1 ATOM 513 O O . GLY A 1 78 ? -35.703 -1.406 75.623 1.00 30.94 ? 78 GLY A O 1 ATOM 514 N N . PHE A 1 79 ? -37.192 -0.122 76.749 1.00 31.68 ? 79 PHE A N 1 ATOM 515 C CA . PHE A 1 79 ? -36.943 1.074 75.941 1.00 31.18 ? 79 PHE A CA 1 ATOM 516 C C . PHE A 1 79 ? -35.766 1.918 76.408 1.00 29.44 ? 79 PHE A C 1 ATOM 517 O O . PHE A 1 79 ? -35.426 2.913 75.755 1.00 27.08 ? 79 PHE A O 1 ATOM 518 C CB . PHE A 1 79 ? -38.180 1.991 75.920 1.00 33.45 ? 79 PHE A CB 1 ATOM 519 C CG . PHE A 1 79 ? -39.358 1.418 75.195 1.00 35.33 ? 79 PHE A CG 1 ATOM 520 C CD1 . PHE A 1 79 ? -40.278 0.621 75.854 1.00 37.94 ? 79 PHE A CD1 1 ATOM 521 C CD2 . PHE A 1 79 ? -39.592 1.732 73.875 1.00 39.25 ? 79 PHE A CD2 1 ATOM 522 C CE1 . PHE A 1 79 ? -41.387 0.109 75.199 1.00 37.12 ? 79 PHE A CE1 1 ATOM 523 C CE2 . PHE A 1 79 ? -40.688 1.210 73.214 1.00 40.03 ? 79 PHE A CE2 1 ATOM 524 C CZ . PHE A 1 79 ? -41.587 0.390 73.882 1.00 37.26 ? 79 PHE A CZ 1 ATOM 525 N N . GLN A 1 80 ? -35.139 1.556 77.535 1.00 28.29 ? 80 GLN A N 1 ATOM 526 C CA . GLN A 1 80 ? -34.110 2.410 78.103 1.00 27.50 ? 80 GLN A CA 1 ATOM 527 C C . GLN A 1 80 ? -33.043 2.735 77.078 1.00 27.41 ? 80 GLN A C 1 ATOM 528 O O . GLN A 1 80 ? -32.513 1.828 76.425 1.00 27.58 ? 80 GLN A O 1 ATOM 529 C CB . GLN A 1 80 ? -33.449 1.768 79.341 1.00 29.14 ? 80 GLN A CB 1 ATOM 530 C CG . GLN A 1 80 ? -34.316 1.832 80.588 1.00 29.99 ? 80 GLN A CG 1 ATOM 531 C CD . GLN A 1 80 ? -33.545 1.508 81.859 1.00 32.44 ? 80 GLN A CD 1 ATOM 532 O OE1 . GLN A 1 80 ? -32.401 1.021 81.811 1.00 31.37 ? 80 GLN A OE1 1 ATOM 533 N NE2 . GLN A 1 80 ? -34.174 1.777 83.014 1.00 33.42 ? 80 GLN A NE2 1 ATOM 534 N N . ASN A 1 81 ? -32.719 4.023 76.983 1.00 25.50 ? 81 ASN A N 1 ATOM 535 C CA . ASN A 1 81 ? -31.633 4.546 76.165 1.00 26.45 ? 81 ASN A CA 1 ATOM 536 C C . ASN A 1 81 ? -31.788 4.409 74.657 1.00 26.54 ? 81 ASN A C 1 ATOM 537 O O . ASN A 1 81 ? -30.866 4.724 73.910 1.00 27.24 ? 81 ASN A O 1 ATOM 538 C CB . ASN A 1 81 ? -30.266 4.018 76.629 1.00 27.77 ? 81 ASN A CB 1 ATOM 539 C CG . ASN A 1 81 ? -29.971 4.392 78.078 1.00 28.90 ? 81 ASN A CG 1 ATOM 540 O OD1 . ASN A 1 81 ? -29.909 5.588 78.450 1.00 29.11 ? 81 ASN A OD1 1 ATOM 541 N ND2 . ASN A 1 81 ? -29.827 3.375 78.916 1.00 30.00 ? 81 ASN A ND2 1 ATOM 542 N N . LYS A 1 82 ? -32.953 3.988 74.197 1.00 26.48 ? 82 LYS A N 1 ATOM 543 C CA . LYS A 1 82 ? -33.151 3.805 72.743 1.00 27.90 ? 82 LYS A CA 1 ATOM 544 C C . LYS A 1 82 ? -33.351 5.122 72.034 1.00 26.68 ? 82 LYS A C 1 ATOM 545 O O . LYS A 1 82 ? -33.773 6.096 72.664 1.00 25.29 ? 82 LYS A O 1 ATOM 546 C CB . LYS A 1 82 ? -34.358 2.908 72.481 1.00 29.12 ? 82 LYS A CB 1 ATOM 547 C CG . LYS A 1 82 ? -34.107 1.469 72.861 1.00 31.78 ? 82 LYS A CG 1 ATOM 548 C CD . LYS A 1 82 ? -35.312 0.567 72.598 1.00 34.30 ? 82 LYS A CD 1 ATOM 549 C CE . LYS A 1 82 ? -35.406 0.076 71.158 1.00 35.61 ? 82 LYS A CE 1 ATOM 550 N NZ . LYS A 1 82 ? -36.069 -1.270 71.195 1.00 38.55 ? 82 LYS A NZ 1 ATOM 551 N N . LYS A 1 83 ? -33.046 5.115 70.731 1.00 26.39 ? 83 LYS A N 1 ATOM 552 C CA . LYS A 1 83 ? -33.211 6.226 69.838 1.00 25.97 ? 83 LYS A CA 1 ATOM 553 C C . LYS A 1 83 ? -34.201 5.843 68.721 1.00 25.15 ? 83 LYS A C 1 ATOM 554 O O . LYS A 1 83 ? -34.537 4.654 68.513 1.00 24.41 ? 83 LYS A O 1 ATOM 555 C CB . LYS A 1 83 ? -31.865 6.665 69.231 1.00 27.02 ? 83 LYS A CB 1 ATOM 556 C CG . LYS A 1 83 ? -30.779 6.997 70.235 1.00 28.42 ? 83 LYS A CG 1 ATOM 557 C CD . LYS A 1 83 ? -29.597 7.669 69.543 1.00 29.43 ? 83 LYS A CD 1 ATOM 558 C CE . LYS A 1 83 ? -28.334 7.580 70.381 1.00 31.91 ? 83 LYS A CE 1 ATOM 559 N NZ . LYS A 1 83 ? -27.684 6.241 70.315 1.00 31.52 ? 83 LYS A NZ 1 ATOM 560 N N . TRP A 1 84 ? -34.717 6.860 68.047 1.00 23.80 ? 84 TRP A N 1 ATOM 561 C CA . TRP A 1 84 ? -35.616 6.647 66.931 1.00 22.93 ? 84 TRP A CA 1 ATOM 562 C C . TRP A 1 84 ? -35.563 7.801 65.991 1.00 22.66 ? 84 TRP A C 1 ATOM 563 O O . TRP A 1 84 ? -35.260 8.939 66.381 1.00 22.30 ? 84 TRP A O 1 ATOM 564 C CB . TRP A 1 84 ? -37.069 6.507 67.385 1.00 22.19 ? 84 TRP A CB 1 ATOM 565 C CG . TRP A 1 84 ? -37.561 7.731 68.155 1.00 21.93 ? 84 TRP A CG 1 ATOM 566 C CD1 . TRP A 1 84 ? -38.238 8.840 67.679 1.00 21.28 ? 84 TRP A CD1 1 ATOM 567 C CD2 . TRP A 1 84 ? -37.376 7.976 69.580 1.00 21.94 ? 84 TRP A CD2 1 ATOM 568 N NE1 . TRP A 1 84 ? -38.454 9.745 68.683 1.00 21.04 ? 84 TRP A NE1 1 ATOM 569 C CE2 . TRP A 1 84 ? -37.974 9.275 69.856 1.00 21.95 ? 84 TRP A CE2 1 ATOM 570 C CE3 . TRP A 1 84 ? -36.788 7.268 70.610 1.00 22.73 ? 84 TRP A CE3 1 ATOM 571 C CZ2 . TRP A 1 84 ? -38.006 9.804 71.135 1.00 21.97 ? 84 TRP A CZ2 1 ATOM 572 C CZ3 . TRP A 1 84 ? -36.787 7.814 71.889 1.00 23.03 ? 84 TRP A CZ3 1 ATOM 573 C CH2 . TRP A 1 84 ? -37.343 9.067 72.146 1.00 22.87 ? 84 TRP A CH2 1 ATOM 574 N N . ASP A 1 85 ? -35.958 7.514 64.764 1.00 22.37 ? 85 ASP A N 1 ATOM 575 C CA . ASP A 1 85 ? -36.414 8.545 63.844 1.00 21.74 ? 85 ASP A CA 1 ATOM 576 C C . ASP A 1 85 ? -37.904 8.755 64.071 1.00 21.26 ? 85 ASP A C 1 ATOM 577 O O . ASP A 1 85 ? -38.379 9.922 64.138 1.00 20.73 ? 85 ASP A O 1 ATOM 578 C CB . ASP A 1 85 ? -36.144 8.135 62.400 1.00 22.03 ? 85 ASP A CB 1 ATOM 579 C CG . ASP A 1 85 ? -34.646 8.065 62.056 1.00 23.68 ? 85 ASP A CG 1 ATOM 580 O OD1 . ASP A 1 85 ? -33.848 8.874 62.603 1.00 23.66 ? 85 ASP A OD1 1 ATOM 581 O OD2 . ASP A 1 85 ? -34.292 7.239 61.163 1.00 23.30 ? 85 ASP A OD2 1 ATOM 582 N N . LEU A 1 86 ? -38.659 7.654 64.163 1.00 21.09 ? 86 LEU A N 1 ATOM 583 C CA . LEU A 1 86 ? -40.102 7.723 64.384 1.00 21.53 ? 86 LEU A CA 1 ATOM 584 C C . LEU A 1 86 ? -40.538 6.799 65.495 1.00 21.21 ? 86 LEU A C 1 ATOM 585 O O . LEU A 1 86 ? -40.323 5.587 65.450 1.00 21.87 ? 86 LEU A O 1 ATOM 586 C CB . LEU A 1 86 ? -40.913 7.433 63.083 1.00 20.61 ? 86 LEU A CB 1 ATOM 587 C CG . LEU A 1 86 ? -42.424 7.710 63.224 1.00 21.10 ? 86 LEU A CG 1 ATOM 588 C CD1 . LEU A 1 86 ? -42.717 9.206 63.453 1.00 20.40 ? 86 LEU A CD1 1 ATOM 589 C CD2 . LEU A 1 86 ? -43.118 7.208 61.971 1.00 20.39 ? 86 LEU A CD2 1 ATOM 590 N N . PHE A 1 87 ? -41.085 7.415 66.543 1.00 21.86 ? 87 PHE A N 1 ATOM 591 C CA . PHE A 1 87 ? -41.680 6.700 67.665 1.00 22.03 ? 87 PHE A CA 1 ATOM 592 C C . PHE A 1 87 ? -43.140 6.498 67.323 1.00 22.15 ? 87 PHE A C 1 ATOM 593 O O . PHE A 1 87 ? -43.832 7.450 67.006 1.00 21.84 ? 87 PHE A O 1 ATOM 594 C CB . PHE A 1 87 ? -41.547 7.488 68.953 1.00 22.17 ? 87 PHE A CB 1 ATOM 595 C CG . PHE A 1 87 ? -41.894 6.697 70.172 1.00 23.25 ? 87 PHE A CG 1 ATOM 596 C CD1 . PHE A 1 87 ? -43.213 6.380 70.458 1.00 23.46 ? 87 PHE A CD1 1 ATOM 597 C CD2 . PHE A 1 87 ? -40.891 6.209 71.015 1.00 24.50 ? 87 PHE A CD2 1 ATOM 598 C CE1 . PHE A 1 87 ? -43.530 5.630 71.597 1.00 24.98 ? 87 PHE A CE1 1 ATOM 599 C CE2 . PHE A 1 87 ? -41.207 5.451 72.136 1.00 25.39 ? 87 PHE A CE2 1 ATOM 600 C CZ . PHE A 1 87 ? -42.525 5.169 72.430 1.00 24.86 ? 87 PHE A CZ 1 ATOM 601 N N . VAL A 1 88 ? -43.594 5.253 67.351 1.00 22.83 ? 88 VAL A N 1 ATOM 602 C CA . VAL A 1 88 ? -44.965 4.948 67.008 1.00 23.83 ? 88 VAL A CA 1 ATOM 603 C C . VAL A 1 88 ? -45.755 4.587 68.270 1.00 24.59 ? 88 VAL A C 1 ATOM 604 O O . VAL A 1 88 ? -45.466 3.588 68.928 1.00 25.22 ? 88 VAL A O 1 ATOM 605 C CB . VAL A 1 88 ? -45.059 3.835 65.932 1.00 24.14 ? 88 VAL A CB 1 ATOM 606 C CG1 . VAL A 1 88 ? -46.511 3.425 65.676 1.00 24.71 ? 88 VAL A CG1 1 ATOM 607 C CG2 . VAL A 1 88 ? -44.388 4.277 64.633 1.00 23.09 ? 88 VAL A CG2 1 ATOM 608 N N . GLU A 1 89 ? -46.763 5.403 68.585 1.00 25.13 ? 89 GLU A N 1 ATOM 609 C CA . GLU A 1 89 ? -47.610 5.190 69.762 1.00 26.87 ? 89 GLU A CA 1 ATOM 610 C C . GLU A 1 89 ? -48.906 4.541 69.344 1.00 26.55 ? 89 GLU A C 1 ATOM 611 O O . GLU A 1 89 ? -49.599 5.037 68.431 1.00 25.56 ? 89 GLU A O 1 ATOM 612 C CB . GLU A 1 89 ? -47.991 6.512 70.468 1.00 28.02 ? 89 GLU A CB 1 ATOM 613 C CG . GLU A 1 89 ? -46.902 7.136 71.280 1.00 29.08 ? 89 GLU A CG 1 ATOM 614 C CD . GLU A 1 89 ? -47.341 8.349 72.110 1.00 28.54 ? 89 GLU A CD 1 ATOM 615 O OE1 . GLU A 1 89 ? -48.228 9.136 71.663 1.00 27.18 ? 89 GLU A OE1 1 ATOM 616 O OE2 . GLU A 1 89 ? -46.739 8.525 73.199 1.00 27.70 ? 89 GLU A OE2 1 ATOM 617 N N . ARG A 1 90 ? -49.264 3.494 70.087 1.00 27.56 ? 90 ARG A N 1 ATOM 618 C CA . ARG A 1 90 ? -50.422 2.650 69.808 1.00 28.50 ? 90 ARG A CA 1 ATOM 619 C C . ARG A 1 90 ? -51.633 3.060 70.625 1.00 29.23 ? 90 ARG A C 1 ATOM 620 O O . ARG A 1 90 ? -51.498 3.490 71.746 1.00 29.39 ? 90 ARG A O 1 ATOM 621 C CB . ARG A 1 90 ? -50.083 1.174 70.109 1.00 28.56 ? 90 ARG A CB 1 ATOM 622 C CG . ARG A 1 90 ? -48.776 0.698 69.508 1.00 28.65 ? 90 ARG A CG 1 ATOM 623 C CD . ARG A 1 90 ? -48.747 0.906 68.016 1.00 28.46 ? 90 ARG A CD 1 ATOM 624 N NE . ARG A 1 90 ? -47.804 0.047 67.304 1.00 28.30 ? 90 ARG A NE 1 ATOM 625 C CZ . ARG A 1 90 ? -47.805 -0.086 65.986 1.00 27.69 ? 90 ARG A CZ 1 ATOM 626 N NH1 . ARG A 1 90 ? -48.700 0.557 65.248 1.00 27.28 ? 90 ARG A NH1 1 ATOM 627 N NH2 . ARG A 1 90 ? -46.937 -0.878 65.398 1.00 28.87 ? 90 ARG A NH2 1 ATOM 628 N N . SER A 1 91 ? -52.823 2.920 70.061 1.00 31.35 ? 91 SER A N 1 ATOM 629 C CA . SER A 1 91 ? -54.035 3.282 70.789 1.00 33.44 ? 91 SER A CA 1 ATOM 630 C C . SER A 1 91 ? -54.266 2.381 72.007 1.00 34.87 ? 91 SER A C 1 ATOM 631 O O . SER A 1 91 ? -54.911 2.802 72.951 1.00 36.47 ? 91 SER A O 1 ATOM 632 C CB . SER A 1 91 ? -55.255 3.253 69.876 1.00 34.20 ? 91 SER A CB 1 ATOM 633 O OG . SER A 1 91 ? -55.570 1.919 69.528 1.00 35.66 ? 91 SER A OG 1 ATOM 634 N N . LYS A 1 92 ? -53.723 1.165 71.998 1.00 35.76 ? 92 LYS A N 1 ATOM 635 C CA . LYS A 1 92 ? -53.864 0.237 73.143 1.00 39.12 ? 92 LYS A CA 1 ATOM 636 C C . LYS A 1 92 ? -52.955 0.600 74.332 1.00 36.23 ? 92 LYS A C 1 ATOM 637 O O . LYS A 1 92 ? -53.060 -0.013 75.386 1.00 36.04 ? 92 LYS A O 1 ATOM 638 C CB . LYS A 1 92 ? -53.547 -1.212 72.717 1.00 41.80 ? 92 LYS A CB 1 ATOM 639 C CG . LYS A 1 92 ? -52.043 -1.518 72.595 1.00 44.03 ? 92 LYS A CG 1 ATOM 640 C CD . LYS A 1 92 ? -51.741 -2.866 71.931 1.00 47.72 ? 92 LYS A CD 1 ATOM 641 C CE . LYS A 1 92 ? -50.232 -3.048 71.731 1.00 50.35 ? 92 LYS A CE 1 ATOM 642 N NZ . LYS A 1 92 ? -49.830 -4.435 71.375 1.00 50.55 ? 92 LYS A NZ 1 ATOM 643 N N . ALA A 1 93 ? -52.044 1.559 74.157 1.00 35.14 ? 93 ALA A N 1 ATOM 644 C CA . ALA A 1 93 ? -51.038 1.850 75.180 1.00 33.44 ? 93 ALA A CA 1 ATOM 645 C C . ALA A 1 93 ? -51.741 2.245 76.489 1.00 34.40 ? 93 ALA A C 1 ATOM 646 O O . ALA A 1 93 ? -52.789 2.885 76.461 1.00 33.43 ? 93 ALA A O 1 ATOM 647 C CB . ALA A 1 93 ? -50.087 2.956 74.717 1.00 32.56 ? 93 ALA A CB 1 ATOM 648 N N . TYR A 1 94 ? -51.187 1.838 77.624 1.00 34.45 ? 94 TYR A N 1 ATOM 649 C CA . TYR A 1 94 ? -51.789 2.181 78.929 1.00 36.82 ? 94 TYR A CA 1 ATOM 650 C C . TYR A 1 94 ? -50.694 2.293 79.965 1.00 35.86 ? 94 TYR A C 1 ATOM 651 O O . TYR A 1 94 ? -49.665 1.655 79.838 1.00 34.13 ? 94 TYR A O 1 ATOM 652 C CB . TYR A 1 94 ? -52.808 1.120 79.367 1.00 38.91 ? 94 TYR A CB 1 ATOM 653 C CG . TYR A 1 94 ? -52.205 -0.254 79.526 1.00 40.79 ? 94 TYR A CG 1 ATOM 654 C CD1 . TYR A 1 94 ? -52.041 -1.089 78.430 1.00 42.09 ? 94 TYR A CD1 1 ATOM 655 C CD2 . TYR A 1 94 ? -51.791 -0.723 80.776 1.00 43.32 ? 94 TYR A CD2 1 ATOM 656 C CE1 . TYR A 1 94 ? -51.500 -2.354 78.566 1.00 43.33 ? 94 TYR A CE1 1 ATOM 657 C CE2 . TYR A 1 94 ? -51.239 -1.985 80.920 1.00 44.32 ? 94 TYR A CE2 1 ATOM 658 C CZ . TYR A 1 94 ? -51.101 -2.801 79.808 1.00 45.09 ? 94 TYR A CZ 1 ATOM 659 O OH . TYR A 1 94 ? -50.539 -4.061 79.929 1.00 45.09 ? 94 TYR A OH 1 ATOM 660 N N . SER A 1 95 ? -50.905 3.120 80.985 1.00 36.27 ? 95 SER A N 1 ATOM 661 C CA . SER A 1 95 ? -49.910 3.261 82.060 1.00 36.63 ? 95 SER A CA 1 ATOM 662 C C . SER A 1 95 ? -50.152 2.221 83.142 1.00 37.67 ? 95 SER A C 1 ATOM 663 O O . SER A 1 95 ? -51.295 1.851 83.403 1.00 37.02 ? 95 SER A O 1 ATOM 664 C CB . SER A 1 95 ? -49.996 4.641 82.678 1.00 37.53 ? 95 SER A CB 1 ATOM 665 O OG . SER A 1 95 ? -49.846 5.619 81.687 1.00 36.87 ? 95 SER A OG 1 ATOM 666 N N . ASN A 1 96 ? -49.080 1.747 83.768 1.00 37.44 ? 96 ASN A N 1 ATOM 667 C CA . ASN A 1 96 ? -49.227 0.713 84.794 1.00 40.26 ? 96 ASN A CA 1 ATOM 668 C C . ASN A 1 96 ? -48.315 0.942 86.003 1.00 38.33 ? 96 ASN A C 1 ATOM 669 O O . ASN A 1 96 ? -47.713 0.017 86.542 1.00 37.08 ? 96 ASN A O 1 ATOM 670 C CB . ASN A 1 96 ? -49.008 -0.668 84.160 1.00 43.58 ? 96 ASN A CB 1 ATOM 671 C CG . ASN A 1 96 ? -49.678 -1.776 84.942 1.00 46.13 ? 96 ASN A CG 1 ATOM 672 O OD1 . ASN A 1 96 ? -50.674 -1.541 85.632 1.00 47.70 ? 96 ASN A OD1 1 ATOM 673 N ND2 . ASN A 1 96 ? -49.124 -2.983 84.860 1.00 45.71 ? 96 ASN A ND2 1 ATOM 674 N N . CYS A 1 97 ? -48.245 2.197 86.438 1.00 38.35 ? 97 CYS A N 1 ATOM 675 C CA . CYS A 1 97 ? -47.398 2.590 87.559 1.00 39.12 ? 97 CYS A CA 1 ATOM 676 C C . CYS A 1 97 ? -48.209 3.589 88.367 1.00 38.21 ? 97 CYS A C 1 ATOM 677 O O . CYS A 1 97 ? -49.443 3.558 88.325 1.00 38.25 ? 97 CYS A O 1 ATOM 678 C CB . CYS A 1 97 ? -46.068 3.138 87.016 1.00 40.76 ? 97 CYS A CB 1 ATOM 679 S SG . CYS A 1 97 ? -44.662 3.431 88.157 1.00 42.79 ? 97 CYS A SG 1 ATOM 680 N N . TYR A 1 98 ? -47.550 4.474 89.098 1.00 38.51 ? 98 TYR A N 1 ATOM 681 C CA . TYR A 1 98 ? -48.276 5.432 89.926 1.00 39.08 ? 98 TYR A CA 1 ATOM 682 C C . TYR A 1 98 ? -49.019 6.427 89.040 1.00 40.03 ? 98 TYR A C 1 ATOM 683 O O . TYR A 1 98 ? -48.446 6.917 88.054 1.00 39.04 ? 98 TYR A O 1 ATOM 684 C CB . TYR A 1 98 ? -47.307 6.173 90.831 1.00 39.35 ? 98 TYR A CB 1 ATOM 685 C CG . TYR A 1 98 ? -47.878 6.622 92.158 1.00 38.79 ? 98 TYR A CG 1 ATOM 686 C CD1 . TYR A 1 98 ? -47.851 5.775 93.265 1.00 39.88 ? 98 TYR A CD1 1 ATOM 687 C CD2 . TYR A 1 98 ? -48.387 7.912 92.325 1.00 38.65 ? 98 TYR A CD2 1 ATOM 688 C CE1 . TYR A 1 98 ? -48.357 6.179 94.492 1.00 38.84 ? 98 TYR A CE1 1 ATOM 689 C CE2 . TYR A 1 98 ? -48.879 8.330 93.555 1.00 39.90 ? 98 TYR A CE2 1 ATOM 690 C CZ . TYR A 1 98 ? -48.854 7.450 94.640 1.00 39.31 ? 98 TYR A CZ 1 ATOM 691 O OH . TYR A 1 98 ? -49.329 7.840 95.874 1.00 38.82 ? 98 TYR A OH 1 ATOM 692 N N . PRO A 1 99 ? -50.290 6.723 89.368 1.00 39.46 ? 99 PRO A N 1 ATOM 693 C CA . PRO A 1 99 ? -50.997 7.676 88.529 1.00 38.41 ? 99 PRO A CA 1 ATOM 694 C C . PRO A 1 99 ? -50.343 9.070 88.511 1.00 37.36 ? 99 PRO A C 1 ATOM 695 O O . PRO A 1 99 ? -49.940 9.594 89.552 1.00 34.85 ? 99 PRO A O 1 ATOM 696 C CB . PRO A 1 99 ? -52.419 7.718 89.122 1.00 40.37 ? 99 PRO A CB 1 ATOM 697 C CG . PRO A 1 99 ? -52.333 7.013 90.430 1.00 40.75 ? 99 PRO A CG 1 ATOM 698 C CD . PRO A 1 99 ? -51.169 6.099 90.374 1.00 40.06 ? 99 PRO A CD 1 ATOM 699 N N . TYR A 1 100 ? -50.210 9.645 87.319 1.00 34.07 ? 100 TYR A N 1 ATOM 700 C CA . TYR A 1 100 ? -49.568 10.952 87.169 1.00 34.58 ? 100 TYR A CA 1 ATOM 701 C C . TYR A 1 100 ? -50.281 11.811 86.137 1.00 34.29 ? 100 TYR A C 1 ATOM 702 O O . TYR A 1 100 ? -51.063 11.315 85.333 1.00 34.63 ? 100 TYR A O 1 ATOM 703 C CB . TYR A 1 100 ? -48.084 10.781 86.763 1.00 34.95 ? 100 TYR A CB 1 ATOM 704 C CG . TYR A 1 100 ? -47.901 10.244 85.357 1.00 35.03 ? 100 TYR A CG 1 ATOM 705 C CD1 . TYR A 1 100 ? -47.941 8.880 85.106 1.00 35.66 ? 100 TYR A CD1 1 ATOM 706 C CD2 . TYR A 1 100 ? -47.716 11.115 84.266 1.00 34.42 ? 100 TYR A CD2 1 ATOM 707 C CE1 . TYR A 1 100 ? -47.779 8.380 83.819 1.00 36.61 ? 100 TYR A CE1 1 ATOM 708 C CE2 . TYR A 1 100 ? -47.570 10.626 82.971 1.00 34.08 ? 100 TYR A CE2 1 ATOM 709 C CZ . TYR A 1 100 ? -47.606 9.254 82.750 1.00 35.56 ? 100 TYR A CZ 1 ATOM 710 O OH . TYR A 1 100 ? -47.457 8.756 81.475 1.00 34.09 ? 100 TYR A OH 1 ATOM 711 N N . ASP A 1 101 ? -50.027 13.113 86.195 1.00 35.64 ? 101 ASP A N 1 ATOM 712 C CA . ASP A 1 101 ? -50.332 14.012 85.092 1.00 35.63 ? 101 ASP A CA 1 ATOM 713 C C . ASP A 1 101 ? -49.095 14.851 84.764 1.00 34.61 ? 101 ASP A C 1 ATOM 714 O O . ASP A 1 101 ? -48.147 14.930 85.559 1.00 32.83 ? 101 ASP A O 1 ATOM 715 C CB . ASP A 1 101 ? -51.523 14.914 85.426 1.00 41.56 ? 101 ASP A CB 1 ATOM 716 C CG . ASP A 1 101 ? -51.358 15.637 86.745 1.00 46.48 ? 101 ASP A CG 1 ATOM 717 O OD1 . ASP A 1 101 ? -50.350 16.358 86.926 1.00 47.71 ? 101 ASP A OD1 1 ATOM 718 O OD2 . ASP A 1 101 ? -52.238 15.470 87.622 1.00 56.83 ? 101 ASP A OD2 1 ATOM 719 N N . VAL A 1 102 ? -49.113 15.459 83.588 1.00 31.49 ? 102 VAL A N 1 ATOM 720 C CA . VAL A 1 102 ? -48.055 16.354 83.160 1.00 30.81 ? 102 VAL A CA 1 ATOM 721 C C . VAL A 1 102 ? -48.698 17.648 82.731 1.00 31.33 ? 102 VAL A C 1 ATOM 722 O O . VAL A 1 102 ? -49.335 17.703 81.662 1.00 30.33 ? 102 VAL A O 1 ATOM 723 C CB . VAL A 1 102 ? -47.270 15.789 81.960 1.00 30.51 ? 102 VAL A CB 1 ATOM 724 C CG1 . VAL A 1 102 ? -46.072 16.681 81.654 1.00 29.56 ? 102 VAL A CG1 1 ATOM 725 C CG2 . VAL A 1 102 ? -46.822 14.351 82.230 1.00 30.59 ? 102 VAL A CG2 1 ATOM 726 N N . PRO A 1 103 ? -48.564 18.706 83.546 1.00 32.01 ? 103 PRO A N 1 ATOM 727 C CA . PRO A 1 103 ? -49.025 19.969 82.990 1.00 32.81 ? 103 PRO A CA 1 ATOM 728 C C . PRO A 1 103 ? -48.273 20.212 81.658 1.00 33.15 ? 103 PRO A C 1 ATOM 729 O O . PRO A 1 103 ? -47.068 19.992 81.594 1.00 34.30 ? 103 PRO A O 1 ATOM 730 C CB . PRO A 1 103 ? -48.646 20.987 84.069 1.00 33.09 ? 103 PRO A CB 1 ATOM 731 C CG . PRO A 1 103 ? -48.677 20.192 85.350 1.00 33.24 ? 103 PRO A CG 1 ATOM 732 C CD . PRO A 1 103 ? -48.148 18.832 84.965 1.00 32.64 ? 103 PRO A CD 1 ATOM 733 N N . ASP A 1 104 ? -48.971 20.581 80.602 1.00 33.44 ? 104 ASP A N 1 ATOM 734 C CA . ASP A 1 104 ? -48.332 20.681 79.242 1.00 33.39 ? 104 ASP A CA 1 ATOM 735 C C . ASP A 1 104 ? -47.658 19.372 78.793 1.00 29.79 ? 104 ASP A C 1 ATOM 736 O O . ASP A 1 104 ? -46.551 19.343 78.234 1.00 28.56 ? 104 ASP A O 1 ATOM 737 C CB . ASP A 1 104 ? -47.345 21.857 79.147 1.00 35.92 ? 104 ASP A CB 1 ATOM 738 C CG . ASP A 1 104 ? -47.188 22.422 77.705 1.00 39.69 ? 104 ASP A CG 1 ATOM 739 O OD1 . ASP A 1 104 ? -47.911 22.054 76.692 1.00 39.46 ? 104 ASP A OD1 1 ATOM 740 O OD2 . ASP A 1 104 ? -46.297 23.302 77.592 1.00 45.47 ? 104 ASP A OD2 1 ATOM 741 N N . TYR A 1 105 ? -48.382 18.291 79.004 1.00 27.95 ? 105 TYR A N 1 ATOM 742 C CA . TYR A 1 105 ? -48.050 16.988 78.453 1.00 26.78 ? 105 TYR A CA 1 ATOM 743 C C . TYR A 1 105 ? -47.657 17.051 76.962 1.00 25.32 ? 105 TYR A C 1 ATOM 744 O O . TYR A 1 105 ? -46.631 16.491 76.570 1.00 24.57 ? 105 TYR A O 1 ATOM 745 C CB . TYR A 1 105 ? -49.257 16.073 78.649 1.00 27.64 ? 105 TYR A CB 1 ATOM 746 C CG . TYR A 1 105 ? -49.053 14.650 78.200 1.00 28.26 ? 105 TYR A CG 1 ATOM 747 C CD1 . TYR A 1 105 ? -49.238 14.293 76.872 1.00 29.56 ? 105 TYR A CD1 1 ATOM 748 C CD2 . TYR A 1 105 ? -48.747 13.647 79.111 1.00 28.86 ? 105 TYR A CD2 1 ATOM 749 C CE1 . TYR A 1 105 ? -49.067 12.973 76.456 1.00 29.19 ? 105 TYR A CE1 1 ATOM 750 C CE2 . TYR A 1 105 ? -48.592 12.326 78.706 1.00 29.65 ? 105 TYR A CE2 1 ATOM 751 C CZ . TYR A 1 105 ? -48.733 12.004 77.368 1.00 29.92 ? 105 TYR A CZ 1 ATOM 752 O OH . TYR A 1 105 ? -48.595 10.703 76.930 1.00 31.94 ? 105 TYR A OH 1 ATOM 753 N N . ALA A 1 106 ? -48.461 17.746 76.150 1.00 24.48 ? 106 ALA A N 1 ATOM 754 C CA . ALA A 1 106 ? -48.222 17.815 74.706 1.00 23.84 ? 106 ALA A CA 1 ATOM 755 C C . ALA A 1 106 ? -46.850 18.386 74.413 1.00 24.11 ? 106 ALA A C 1 ATOM 756 O O . ALA A 1 106 ? -46.162 17.890 73.533 1.00 24.44 ? 106 ALA A O 1 ATOM 757 C CB . ALA A 1 106 ? -49.297 18.638 73.977 1.00 23.91 ? 106 ALA A CB 1 ATOM 758 N N . SER A 1 107 ? -46.430 19.401 75.165 1.00 24.67 ? 107 SER A N 1 ATOM 759 C CA . SER A 1 107 ? -45.086 19.955 74.920 1.00 24.58 ? 107 SER A CA 1 ATOM 760 C C . SER A 1 107 ? -43.955 19.024 75.311 1.00 24.09 ? 107 SER A C 1 ATOM 761 O O . SER A 1 107 ? -42.954 18.962 74.611 1.00 24.36 ? 107 SER A O 1 ATOM 762 C CB . SER A 1 107 ? -44.912 21.328 75.553 1.00 24.59 ? 107 SER A CB 1 ATOM 763 O OG . SER A 1 107 ? -45.686 22.286 74.804 1.00 25.34 ? 107 SER A OG 1 ATOM 764 N N . LEU A 1 108 ? -44.080 18.329 76.423 1.00 24.69 ? 108 LEU A N 1 ATOM 765 C CA . LEU A 1 108 ? -43.011 17.446 76.867 1.00 24.54 ? 108 LEU A CA 1 ATOM 766 C C . LEU A 1 108 ? -42.913 16.273 75.875 1.00 23.99 ? 108 LEU A C 1 ATOM 767 O O . LEU A 1 108 ? -41.820 15.907 75.430 1.00 24.12 ? 108 LEU A O 1 ATOM 768 C CB . LEU A 1 108 ? -43.242 16.939 78.285 1.00 25.35 ? 108 LEU A CB 1 ATOM 769 C CG . LEU A 1 108 ? -42.167 15.976 78.826 1.00 25.64 ? 108 LEU A CG 1 ATOM 770 C CD1 . LEU A 1 108 ? -40.776 16.615 78.792 1.00 27.04 ? 108 LEU A CD1 1 ATOM 771 C CD2 . LEU A 1 108 ? -42.527 15.518 80.225 1.00 25.52 ? 108 LEU A CD2 1 ATOM 772 N N . ARG A 1 109 ? -44.068 15.727 75.505 1.00 22.85 ? 109 ARG A N 1 ATOM 773 C CA . ARG A 1 109 ? -44.133 14.698 74.458 1.00 22.34 ? 109 ARG A CA 1 ATOM 774 C C . ARG A 1 109 ? -43.448 15.138 73.166 1.00 22.52 ? 109 ARG A C 1 ATOM 775 O O . ARG A 1 109 ? -42.623 14.416 72.610 1.00 21.70 ? 109 ARG A O 1 ATOM 776 C CB . ARG A 1 109 ? -45.574 14.277 74.241 1.00 22.32 ? 109 ARG A CB 1 ATOM 777 C CG . ARG A 1 109 ? -45.776 13.238 73.152 1.00 23.29 ? 109 ARG A CG 1 ATOM 778 C CD . ARG A 1 109 ? -47.250 12.833 73.081 1.00 23.21 ? 109 ARG A CD 1 ATOM 779 N NE . ARG A 1 109 ? -47.529 11.908 71.981 1.00 22.69 ? 109 ARG A NE 1 ATOM 780 C CZ . ARG A 1 109 ? -47.751 12.271 70.708 1.00 22.61 ? 109 ARG A CZ 1 ATOM 781 N NH1 . ARG A 1 109 ? -47.729 13.538 70.329 1.00 21.42 ? 109 ARG A NH1 1 ATOM 782 N NH2 . ARG A 1 109 ? -48.000 11.339 69.794 1.00 21.62 ? 109 ARG A NH2 1 ATOM 783 N N . SER A 1 110 ? -43.758 16.351 72.715 1.00 22.53 ? 110 SER A N 1 ATOM 784 C CA . SER A 1 110 ? -43.183 16.890 71.491 1.00 22.59 ? 110 SER A CA 1 ATOM 785 C C . SER A 1 110 ? -41.666 17.086 71.560 1.00 23.12 ? 110 SER A C 1 ATOM 786 O O . SER A 1 110 ? -40.946 16.727 70.635 1.00 22.79 ? 110 SER A O 1 ATOM 787 C CB . SER A 1 110 ? -43.841 18.234 71.136 1.00 21.65 ? 110 SER A CB 1 ATOM 788 O OG . SER A 1 110 ? -43.197 18.784 69.988 1.00 22.33 ? 110 SER A OG 1 ATOM 789 N N . LEU A 1 111 ? -41.173 17.671 72.645 1.00 23.87 ? 111 LEU A N 1 ATOM 790 C CA . LEU A 1 111 ? -39.735 17.966 72.720 1.00 24.88 ? 111 LEU A CA 1 ATOM 791 C C . LEU A 1 111 ? -38.897 16.702 72.850 1.00 23.26 ? 111 LEU A C 1 ATOM 792 O O . LEU A 1 111 ? -37.846 16.647 72.240 1.00 23.65 ? 111 LEU A O 1 ATOM 793 C CB . LEU A 1 111 ? -39.413 19.008 73.786 1.00 25.85 ? 111 LEU A CB 1 ATOM 794 C CG . LEU A 1 111 ? -39.453 18.599 75.219 1.00 26.69 ? 111 LEU A CG 1 ATOM 795 C CD1 . LEU A 1 111 ? -38.120 17.973 75.582 1.00 27.51 ? 111 LEU A CD1 1 ATOM 796 C CD2 . LEU A 1 111 ? -39.803 19.796 76.117 1.00 28.73 ? 111 LEU A CD2 1 ATOM 797 N N . VAL A 1 112 ? -39.390 15.692 73.564 1.00 22.76 ? 112 VAL A N 1 ATOM 798 C CA . VAL A 1 112 ? -38.714 14.367 73.639 1.00 23.06 ? 112 VAL A CA 1 ATOM 799 C C . VAL A 1 112 ? -38.772 13.649 72.285 1.00 22.01 ? 112 VAL A C 1 ATOM 800 O O . VAL A 1 112 ? -37.772 13.136 71.802 1.00 21.23 ? 112 VAL A O 1 ATOM 801 C CB . VAL A 1 112 ? -39.259 13.462 74.767 1.00 23.18 ? 112 VAL A CB 1 ATOM 802 C CG1 . VAL A 1 112 ? -38.502 12.103 74.751 1.00 23.29 ? 112 VAL A CG1 1 ATOM 803 C CG2 . VAL A 1 112 ? -39.049 14.136 76.151 1.00 23.50 ? 112 VAL A CG2 1 ATOM 804 N N . ALA A 1 113 ? -39.934 13.706 71.626 1.00 21.90 ? 113 ALA A N 1 ATOM 805 C CA . ALA A 1 113 ? -40.110 13.085 70.321 1.00 21.38 ? 113 ALA A CA 1 ATOM 806 C C . ALA A 1 113 ? -39.164 13.649 69.309 1.00 21.88 ? 113 ALA A C 1 ATOM 807 O O . ALA A 1 113 ? -38.611 12.892 68.520 1.00 21.80 ? 113 ALA A O 1 ATOM 808 C CB . ALA A 1 113 ? -41.556 13.256 69.806 1.00 20.65 ? 113 ALA A CB 1 ATOM 809 N N . SER A 1 114 ? -39.028 14.983 69.304 1.00 21.76 ? 114 SER A N 1 ATOM 810 C CA . SER A 1 114 ? -38.198 15.682 68.355 1.00 23.23 ? 114 SER A CA 1 ATOM 811 C C . SER A 1 114 ? -36.704 15.425 68.623 1.00 23.81 ? 114 SER A C 1 ATOM 812 O O . SER A 1 114 ? -35.896 15.346 67.662 1.00 24.76 ? 114 SER A O 1 ATOM 813 C CB . SER A 1 114 ? -38.499 17.188 68.376 1.00 23.73 ? 114 SER A CB 1 ATOM 814 O OG . SER A 1 114 ? -37.687 17.848 67.434 1.00 26.43 ? 114 SER A OG 1 ATOM 815 N N . SER A 1 115 ? -36.352 15.300 69.898 1.00 23.00 ? 115 SER A N 1 ATOM 816 C CA . SER A 1 115 ? -34.977 14.987 70.300 1.00 24.36 ? 115 SER A CA 1 ATOM 817 C C . SER A 1 115 ? -34.561 13.589 69.840 1.00 23.44 ? 115 SER A C 1 ATOM 818 O O . SER A 1 115 ? -33.424 13.383 69.396 1.00 25.33 ? 115 SER A O 1 ATOM 819 C CB . SER A 1 115 ? -34.809 15.192 71.805 1.00 25.19 ? 115 SER A CB 1 ATOM 820 O OG . SER A 1 115 ? -33.610 14.651 72.304 1.00 27.64 ? 115 SER A OG 1 ATOM 821 N N . GLY A 1 116 ? -35.467 12.633 69.911 1.00 22.36 ? 116 GLY A N 1 ATOM 822 C CA . GLY A 1 116 ? -35.241 11.326 69.270 1.00 22.47 ? 116 GLY A CA 1 ATOM 823 C C . GLY A 1 116 ? -34.392 10.350 70.059 1.00 23.07 ? 116 GLY A C 1 ATOM 824 O O . GLY A 1 116 ? -33.843 9.397 69.490 1.00 23.59 ? 116 GLY A O 1 ATOM 825 N N . THR A 1 117 ? -34.318 10.551 71.370 1.00 23.47 ? 117 THR A N 1 ATOM 826 C CA . THR A 1 117 ? -33.467 9.713 72.218 1.00 24.02 ? 117 THR A CA 1 ATOM 827 C C . THR A 1 117 ? -33.956 9.654 73.643 1.00 24.31 ? 117 THR A C 1 ATOM 828 O O . THR A 1 117 ? -34.424 10.654 74.199 1.00 25.08 ? 117 THR A O 1 ATOM 829 C CB . THR A 1 117 ? -31.993 10.207 72.250 1.00 24.88 ? 117 THR A CB 1 ATOM 830 O OG1 . THR A 1 117 ? -31.210 9.342 73.083 1.00 24.90 ? 117 THR A OG1 1 ATOM 831 C CG2 . THR A 1 117 ? -31.850 11.660 72.754 1.00 24.98 ? 117 THR A CG2 1 ATOM 832 N N . LEU A 1 118 ? -33.824 8.471 74.227 1.00 24.46 ? 118 LEU A N 1 ATOM 833 C CA . LEU A 1 118 ? -34.100 8.265 75.636 1.00 25.41 ? 118 LEU A CA 1 ATOM 834 C C . LEU A 1 118 ? -32.801 8.067 76.426 1.00 26.50 ? 118 LEU A C 1 ATOM 835 O O . LEU A 1 118 ? -32.840 7.560 77.535 1.00 28.30 ? 118 LEU A O 1 ATOM 836 C CB . LEU A 1 118 ? -35.007 7.049 75.789 1.00 25.69 ? 118 LEU A CB 1 ATOM 837 C CG . LEU A 1 118 ? -36.480 7.297 75.514 1.00 25.72 ? 118 LEU A CG 1 ATOM 838 C CD1 . LEU A 1 118 ? -37.226 5.974 75.451 1.00 26.62 ? 118 LEU A CD1 1 ATOM 839 C CD2 . LEU A 1 118 ? -37.066 8.200 76.582 1.00 26.34 ? 118 LEU A CD2 1 ATOM 840 N N . GLU A 1 119 ? -31.657 8.464 75.856 1.00 27.89 ? 119 GLU A N 1 ATOM 841 C CA . GLU A 1 119 ? -30.375 8.313 76.558 1.00 28.66 ? 119 GLU A CA 1 ATOM 842 C C . GLU A 1 119 ? -30.404 9.060 77.887 1.00 29.03 ? 119 GLU A C 1 ATOM 843 O O . GLU A 1 119 ? -30.701 10.259 77.927 1.00 27.21 ? 119 GLU A O 1 ATOM 844 C CB . GLU A 1 119 ? -29.212 8.867 75.753 1.00 31.17 ? 119 GLU A CB 1 ATOM 845 C CG . GLU A 1 119 ? -28.855 8.086 74.517 1.00 33.90 ? 119 GLU A CG 1 ATOM 846 C CD . GLU A 1 119 ? -28.020 8.919 73.570 1.00 37.00 ? 119 GLU A CD 1 ATOM 847 O OE1 . GLU A 1 119 ? -28.599 9.772 72.811 1.00 35.03 ? 119 GLU A OE1 1 ATOM 848 O OE2 . GLU A 1 119 ? -26.773 8.761 73.655 1.00 37.14 ? 119 GLU A OE2 1 ATOM 849 N N . PHE A 1 120 ? -30.041 8.352 78.959 1.00 28.36 ? 120 PHE A N 1 ATOM 850 C CA . PHE A 1 120 ? -30.166 8.851 80.308 1.00 29.02 ? 120 PHE A CA 1 ATOM 851 C C . PHE A 1 120 ? -28.834 8.600 81.027 1.00 31.31 ? 120 PHE A C 1 ATOM 852 O O . PHE A 1 120 ? -28.291 7.513 80.923 1.00 30.49 ? 120 PHE A O 1 ATOM 853 C CB . PHE A 1 120 ? -31.299 8.128 81.036 1.00 29.31 ? 120 PHE A CB 1 ATOM 854 C CG . PHE A 1 120 ? -31.551 8.646 82.418 1.00 29.97 ? 120 PHE A CG 1 ATOM 855 C CD1 . PHE A 1 120 ? -32.426 9.695 82.624 1.00 30.27 ? 120 PHE A CD1 1 ATOM 856 C CD2 . PHE A 1 120 ? -30.906 8.087 83.521 1.00 30.26 ? 120 PHE A CD2 1 ATOM 857 C CE1 . PHE A 1 120 ? -32.661 10.200 83.892 1.00 30.71 ? 120 PHE A CE1 1 ATOM 858 C CE2 . PHE A 1 120 ? -31.141 8.580 84.796 1.00 31.03 ? 120 PHE A CE2 1 ATOM 859 C CZ . PHE A 1 120 ? -32.014 9.640 84.983 1.00 31.38 ? 120 PHE A CZ 1 ATOM 860 N N . ASN A 1 121 ? -28.326 9.624 81.711 1.00 32.39 ? 121 ASN A N 1 ATOM 861 C CA . ASN A 1 121 ? -27.080 9.535 82.461 1.00 35.51 ? 121 ASN A CA 1 ATOM 862 C C . ASN A 1 121 ? -27.390 9.711 83.929 1.00 36.39 ? 121 ASN A C 1 ATOM 863 O O . ASN A 1 121 ? -27.927 10.748 84.342 1.00 35.77 ? 121 ASN A O 1 ATOM 864 C CB . ASN A 1 121 ? -26.111 10.607 82.000 1.00 38.17 ? 121 ASN A CB 1 ATOM 865 C CG . ASN A 1 121 ? -25.321 10.192 80.778 1.00 41.53 ? 121 ASN A CG 1 ATOM 866 O OD1 . ASN A 1 121 ? -25.365 9.038 80.353 1.00 44.26 ? 121 ASN A OD1 1 ATOM 867 N ND2 . ASN A 1 121 ? -24.577 11.132 80.213 1.00 46.10 ? 121 ASN A ND2 1 ATOM 868 N N . ASN A 1 122 ? -27.081 8.683 84.708 1.00 37.34 ? 122 ASN A N 1 ATOM 869 C CA . ASN A 1 122 ? -27.308 8.720 86.149 1.00 39.50 ? 122 ASN A CA 1 ATOM 870 C C . ASN A 1 122 ? -26.382 9.740 86.796 1.00 38.45 ? 122 ASN A C 1 ATOM 871 O O . ASN A 1 122 ? -25.248 9.913 86.354 1.00 38.79 ? 122 ASN A O 1 ATOM 872 C CB . ASN A 1 122 ? -27.118 7.319 86.750 1.00 41.76 ? 122 ASN A CB 1 ATOM 873 C CG . ASN A 1 122 ? -28.332 6.430 86.523 1.00 44.07 ? 122 ASN A CG 1 ATOM 874 O OD1 . ASN A 1 122 ? -29.349 6.565 87.199 1.00 46.95 ? 122 ASN A OD1 1 ATOM 875 N ND2 . ASN A 1 122 ? -28.241 5.538 85.549 1.00 47.11 ? 122 ASN A ND2 1 ATOM 876 N N . GLU A 1 123 ? -26.884 10.440 87.811 1.00 38.74 ? 123 GLU A N 1 ATOM 877 C CA . GLU A 1 123 ? -26.052 11.317 88.628 1.00 38.93 ? 123 GLU A CA 1 ATOM 878 C C . GLU A 1 123 ? -26.258 11.059 90.122 1.00 40.26 ? 123 GLU A C 1 ATOM 879 O O . GLU A 1 123 ? -27.342 10.648 90.567 1.00 39.34 ? 123 GLU A O 1 ATOM 880 C CB . GLU A 1 123 ? -26.351 12.794 88.336 1.00 37.72 ? 123 GLU A CB 1 ATOM 881 C CG . GLU A 1 123 ? -25.974 13.252 86.944 1.00 37.36 ? 123 GLU A CG 1 ATOM 882 C CD . GLU A 1 123 ? -26.402 14.680 86.650 1.00 36.25 ? 123 GLU A CD 1 ATOM 883 O OE1 . GLU A 1 123 ? -27.583 15.035 86.901 1.00 36.44 ? 123 GLU A OE1 1 ATOM 884 O OE2 . GLU A 1 123 ? -25.568 15.440 86.136 1.00 34.22 ? 123 GLU A OE2 1 ATOM 885 N N . SER A 1 124 ? -25.211 11.346 90.891 1.00 42.65 ? 124 SER A N 1 ATOM 886 C CA . SER A 1 124 ? -25.210 11.120 92.335 1.00 44.19 ? 124 SER A CA 1 ATOM 887 C C . SER A 1 124 ? -25.629 12.397 93.044 1.00 44.47 ? 124 SER A C 1 ATOM 888 O O . SER A 1 124 ? -24.797 13.263 93.347 1.00 43.58 ? 124 SER A O 1 ATOM 889 C CB . SER A 1 124 ? -23.818 10.688 92.817 1.00 46.74 ? 124 SER A CB 1 ATOM 890 O OG . SER A 1 124 ? -23.433 9.458 92.224 1.00 48.66 ? 124 SER A OG 1 ATOM 891 N N . PHE A 1 125 ? -26.928 12.517 93.276 1.00 43.53 ? 125 PHE A N 1 ATOM 892 C CA . PHE A 1 125 ? -27.464 13.642 94.010 1.00 44.78 ? 125 PHE A CA 1 ATOM 893 C C . PHE A 1 125 ? -27.184 13.388 95.470 1.00 46.58 ? 125 PHE A C 1 ATOM 894 O O . PHE A 1 125 ? -27.201 12.250 95.907 1.00 48.50 ? 125 PHE A O 1 ATOM 895 C CB . PHE A 1 125 ? -28.971 13.778 93.792 1.00 43.23 ? 125 PHE A CB 1 ATOM 896 C CG . PHE A 1 125 ? -29.318 14.411 92.488 1.00 41.24 ? 125 PHE A CG 1 ATOM 897 C CD1 . PHE A 1 125 ? -29.405 13.648 91.343 1.00 40.53 ? 125 PHE A CD1 1 ATOM 898 C CD2 . PHE A 1 125 ? -29.482 15.791 92.396 1.00 41.76 ? 125 PHE A CD2 1 ATOM 899 C CE1 . PHE A 1 125 ? -29.688 14.238 90.128 1.00 39.97 ? 125 PHE A CE1 1 ATOM 900 C CE2 . PHE A 1 125 ? -29.771 16.390 91.181 1.00 42.21 ? 125 PHE A CE2 1 ATOM 901 C CZ . PHE A 1 125 ? -29.877 15.607 90.042 1.00 40.26 ? 125 PHE A CZ 1 ATOM 902 N N . ASN A 1 126 ? -26.931 14.447 96.218 1.00 49.46 ? 126 ASN A N 1 ATOM 903 C CA . ASN A 1 126 ? -26.690 14.304 97.655 1.00 53.07 ? 126 ASN A CA 1 ATOM 904 C C . ASN A 1 126 ? -28.003 14.373 98.425 1.00 49.44 ? 126 ASN A C 1 ATOM 905 O O . ASN A 1 126 ? -28.431 15.463 98.819 1.00 48.97 ? 126 ASN A O 1 ATOM 906 C CB . ASN A 1 126 ? -25.723 15.395 98.115 1.00 59.92 ? 126 ASN A CB 1 ATOM 907 C CG . ASN A 1 126 ? -25.542 15.426 99.620 1.00 67.28 ? 126 ASN A CG 1 ATOM 908 O OD1 . ASN A 1 126 ? -25.953 14.505 100.330 1.00 66.03 ? 126 ASN A OD1 1 ATOM 909 N ND2 . ASN A 1 126 ? -24.926 16.509 100.115 1.00 78.57 ? 126 ASN A ND2 1 ATOM 910 N N . TRP A 1 127 ? -28.642 13.219 98.640 1.00 46.40 ? 127 TRP A N 1 ATOM 911 C CA . TRP A 1 127 ? -29.874 13.159 99.435 1.00 46.32 ? 127 TRP A CA 1 ATOM 912 C C . TRP A 1 127 ? -29.606 12.783 100.876 1.00 48.48 ? 127 TRP A C 1 ATOM 913 O O . TRP A 1 127 ? -30.308 11.945 101.452 1.00 49.20 ? 127 TRP A O 1 ATOM 914 C CB . TRP A 1 127 ? -30.873 12.176 98.844 1.00 45.24 ? 127 TRP A CB 1 ATOM 915 C CG . TRP A 1 127 ? -31.199 12.454 97.392 1.00 44.37 ? 127 TRP A CG 1 ATOM 916 C CD1 . TRP A 1 127 ? -31.100 11.574 96.328 1.00 43.85 ? 127 TRP A CD1 1 ATOM 917 C CD2 . TRP A 1 127 ? -31.685 13.714 96.806 1.00 44.99 ? 127 TRP A CD2 1 ATOM 918 N NE1 . TRP A 1 127 ? -31.474 12.172 95.155 1.00 43.77 ? 127 TRP A NE1 1 ATOM 919 C CE2 . TRP A 1 127 ? -31.836 13.457 95.364 1.00 44.17 ? 127 TRP A CE2 1 ATOM 920 C CE3 . TRP A 1 127 ? -31.987 14.980 97.302 1.00 44.28 ? 127 TRP A CE3 1 ATOM 921 C CZ2 . TRP A 1 127 ? -32.270 14.438 94.483 1.00 45.23 ? 127 TRP A CZ2 1 ATOM 922 C CZ3 . TRP A 1 127 ? -32.433 15.966 96.402 1.00 45.45 ? 127 TRP A CZ3 1 ATOM 923 C CH2 . TRP A 1 127 ? -32.570 15.700 95.025 1.00 45.51 ? 127 TRP A CH2 1 ATOM 924 N N . THR A 1 128 ? -28.595 13.397 101.475 1.00 50.44 ? 128 THR A N 1 ATOM 925 C CA . THR A 1 128 ? -28.329 13.185 102.905 1.00 52.65 ? 128 THR A CA 1 ATOM 926 C C . THR A 1 128 ? -29.551 13.601 103.727 1.00 51.19 ? 128 THR A C 1 ATOM 927 O O . THR A 1 128 ? -30.029 14.730 103.597 1.00 50.86 ? 128 THR A O 1 ATOM 928 C CB . THR A 1 128 ? -27.102 13.998 103.372 1.00 55.42 ? 128 THR A CB 1 ATOM 929 O OG1 . THR A 1 128 ? -25.946 13.610 102.612 1.00 56.97 ? 128 THR A OG1 1 ATOM 930 C CG2 . THR A 1 128 ? -26.824 13.769 104.876 1.00 55.29 ? 128 THR A CG2 1 ATOM 931 N N . GLY A 1 129 ? -30.071 12.674 104.534 1.00 52.87 ? 129 GLY A N 1 ATOM 932 C CA . GLY A 1 129 ? -31.077 12.990 105.559 1.00 52.21 ? 129 GLY A CA 1 ATOM 933 C C . GLY A 1 129 ? -32.481 12.484 105.290 1.00 52.48 ? 129 GLY A C 1 ATOM 934 O O . GLY A 1 129 ? -33.383 12.680 106.118 1.00 50.60 ? 129 GLY A O 1 ATOM 935 N N . VAL A 1 130 ? -32.671 11.847 104.129 1.00 49.83 ? 130 VAL A N 1 ATOM 936 C CA . VAL A 1 130 ? -33.949 11.252 103.756 1.00 46.92 ? 130 VAL A CA 1 ATOM 937 C C . VAL A 1 130 ? -33.747 9.804 103.320 1.00 44.60 ? 130 VAL A C 1 ATOM 938 O O . VAL A 1 130 ? -32.617 9.379 103.068 1.00 44.30 ? 130 VAL A O 1 ATOM 939 C CB . VAL A 1 130 ? -34.625 12.043 102.604 1.00 46.76 ? 130 VAL A CB 1 ATOM 940 C CG1 . VAL A 1 130 ? -34.949 13.468 103.052 1.00 46.58 ? 130 VAL A CG1 1 ATOM 941 C CG2 . VAL A 1 130 ? -33.733 12.036 101.365 1.00 45.96 ? 130 VAL A CG2 1 ATOM 942 N N . THR A 1 131 ? -34.846 9.055 103.264 1.00 43.87 ? 131 THR A N 1 ATOM 943 C CA . THR A 1 131 ? -34.868 7.708 102.700 1.00 44.14 ? 131 THR A CA 1 ATOM 944 C C . THR A 1 131 ? -35.124 7.819 101.182 1.00 44.09 ? 131 THR A C 1 ATOM 945 O O . THR A 1 131 ? -36.060 8.524 100.743 1.00 40.89 ? 131 THR A O 1 ATOM 946 C CB . THR A 1 131 ? -35.986 6.851 103.330 1.00 45.37 ? 131 THR A CB 1 ATOM 947 O OG1 . THR A 1 131 ? -35.926 6.941 104.765 1.00 46.58 ? 131 THR A OG1 1 ATOM 948 C CG2 . THR A 1 131 ? -35.868 5.380 102.909 1.00 45.86 ? 131 THR A CG2 1 ATOM 949 N N . GLN A 1 132 ? -34.296 7.128 100.398 1.00 43.87 ? 132 GLN A N 1 ATOM 950 C CA . GLN A 1 132 ? -34.435 7.089 98.934 1.00 43.25 ? 132 GLN A CA 1 ATOM 951 C C . GLN A 1 132 ? -35.221 5.859 98.492 1.00 43.62 ? 132 GLN A C 1 ATOM 952 O O . GLN A 1 132 ? -35.530 4.976 99.300 1.00 41.87 ? 132 GLN A O 1 ATOM 953 C CB . GLN A 1 132 ? -33.053 7.068 98.270 1.00 44.22 ? 132 GLN A CB 1 ATOM 954 C CG . GLN A 1 132 ? -32.184 8.262 98.619 1.00 44.51 ? 132 GLN A CG 1 ATOM 955 C CD . GLN A 1 132 ? -30.936 8.344 97.761 1.00 45.77 ? 132 GLN A CD 1 ATOM 956 O OE1 . GLN A 1 132 ? -30.995 8.176 96.538 1.00 44.92 ? 132 GLN A OE1 1 ATOM 957 N NE2 . GLN A 1 132 ? -29.797 8.611 98.394 1.00 45.80 ? 132 GLN A NE2 1 ATOM 958 N N . ASN A 1 133 ? -35.561 5.824 97.200 1.00 41.85 ? 133 ASN A N 1 ATOM 959 C CA . ASN A 1 133 ? -36.106 4.633 96.555 1.00 41.40 ? 133 ASN A CA 1 ATOM 960 C C . ASN A 1 133 ? -37.452 4.150 97.081 1.00 40.68 ? 133 ASN A C 1 ATOM 961 O O . ASN A 1 133 ? -37.688 2.938 97.180 1.00 39.31 ? 133 ASN A O 1 ATOM 962 C CB . ASN A 1 133 ? -35.101 3.479 96.632 1.00 44.73 ? 133 ASN A CB 1 ATOM 963 C CG . ASN A 1 133 ? -33.812 3.759 95.893 1.00 48.99 ? 133 ASN A CG 1 ATOM 964 O OD1 . ASN A 1 133 ? -33.682 4.747 95.155 1.00 46.57 ? 133 ASN A OD1 1 ATOM 965 N ND2 . ASN A 1 133 ? -32.841 2.877 96.089 1.00 54.92 ? 133 ASN A ND2 1 ATOM 966 N N . GLY A 1 134 ? -38.362 5.071 97.375 1.00 39.98 ? 134 GLY A N 1 ATOM 967 C CA . GLY A 1 134 ? -39.711 4.676 97.769 1.00 41.08 ? 134 GLY A CA 1 ATOM 968 C C . GLY A 1 134 ? -40.381 3.856 96.677 1.00 42.22 ? 134 GLY A C 1 ATOM 969 O O . GLY A 1 134 ? -40.096 4.052 95.475 1.00 40.91 ? 134 GLY A O 1 ATOM 970 N N . THR A 1 135 ? -41.257 2.939 97.092 1.00 41.41 ? 135 THR A N 1 ATOM 971 C CA . THR A 1 135 ? -41.972 2.063 96.170 1.00 43.49 ? 135 THR A CA 1 ATOM 972 C C . THR A 1 135 ? -43.475 2.040 96.436 1.00 44.64 ? 135 THR A C 1 ATOM 973 O O . THR A 1 135 ? -43.949 2.563 97.447 1.00 44.09 ? 135 THR A O 1 ATOM 974 C CB . THR A 1 135 ? -41.398 0.638 96.178 1.00 44.86 ? 135 THR A CB 1 ATOM 975 O OG1 . THR A 1 135 ? -41.639 0.022 97.452 1.00 44.50 ? 135 THR A OG1 1 ATOM 976 C CG2 . THR A 1 135 ? -39.879 0.657 95.882 1.00 45.15 ? 135 THR A CG2 1 ATOM 977 N N . SER A 1 136 ? -44.213 1.473 95.481 1.00 44.44 ? 136 SER A N 1 ATOM 978 C CA . SER A 1 136 ? -45.667 1.386 95.543 1.00 44.18 ? 136 SER A CA 1 ATOM 979 C C . SER A 1 136 ? -46.138 0.058 94.962 1.00 45.33 ? 136 SER A C 1 ATOM 980 O O . SER A 1 136 ? -45.547 -0.451 93.996 1.00 45.49 ? 136 SER A O 1 ATOM 981 C CB . SER A 1 136 ? -46.287 2.539 94.753 1.00 43.43 ? 136 SER A CB 1 ATOM 982 O OG . SER A 1 136 ? -47.702 2.505 94.779 1.00 43.48 ? 136 SER A OG 1 ATOM 983 N N . SER A 1 137 ? -47.215 -0.494 95.531 1.00 44.32 ? 137 SER A N 1 ATOM 984 C CA . SER A 1 137 ? -47.828 -1.719 95.006 1.00 45.00 ? 137 SER A CA 1 ATOM 985 C C . SER A 1 137 ? -48.562 -1.440 93.695 1.00 46.76 ? 137 SER A C 1 ATOM 986 O O . SER A 1 137 ? -48.916 -2.378 92.970 1.00 46.38 ? 137 SER A O 1 ATOM 987 C CB . SER A 1 137 ? -48.811 -2.325 96.017 1.00 46.04 ? 137 SER A CB 1 ATOM 988 O OG . SER A 1 137 ? -49.925 -1.472 96.160 1.00 46.22 ? 137 SER A OG 1 ATOM 989 N N . ALA A 1 138 ? -48.791 -0.156 93.403 1.00 45.69 ? 138 ALA A N 1 ATOM 990 C CA . ALA A 1 138 ? -49.375 0.275 92.118 1.00 46.05 ? 138 ALA A CA 1 ATOM 991 C C . ALA A 1 138 ? -48.362 0.272 90.963 1.00 45.64 ? 138 ALA A C 1 ATOM 992 O O . ALA A 1 138 ? -48.737 0.492 89.809 1.00 47.30 ? 138 ALA A O 1 ATOM 993 C CB . ALA A 1 138 ? -49.989 1.666 92.262 1.00 43.50 ? 138 ALA A CB 1 ATOM 994 N N . CYS A 1 139 ? -47.090 0.039 91.267 1.00 46.16 ? 139 CYS A N 1 ATOM 995 C CA . CYS A 1 139 ? -46.057 0.045 90.249 1.00 46.50 ? 139 CYS A CA 1 ATOM 996 C C . CYS A 1 139 ? -45.145 -1.140 90.469 1.00 47.59 ? 139 CYS A C 1 ATOM 997 O O . CYS A 1 139 ? -44.036 -0.985 90.948 1.00 50.45 ? 139 CYS A O 1 ATOM 998 C CB . CYS A 1 139 ? -45.279 1.361 90.310 1.00 46.55 ? 139 CYS A CB 1 ATOM 999 S SG . CYS A 1 139 ? -44.102 1.619 88.953 1.00 46.62 ? 139 CYS A SG 1 ATOM 1000 N N . LYS A 1 140 ? -45.625 -2.329 90.123 1.00 47.40 ? 140 LYS A N 1 ATOM 1001 C CA . LYS A 1 140 ? -44.856 -3.551 90.328 1.00 49.78 ? 140 LYS A CA 1 ATOM 1002 C C . LYS A 1 140 ? -43.842 -3.803 89.211 1.00 48.51 ? 140 LYS A C 1 ATOM 1003 O O . LYS A 1 140 ? -44.144 -3.616 88.021 1.00 44.97 ? 140 LYS A O 1 ATOM 1004 C CB . LYS A 1 140 ? -45.792 -4.757 90.503 1.00 52.53 ? 140 LYS A CB 1 ATOM 1005 C CG . LYS A 1 140 ? -46.671 -4.634 91.739 1.00 56.15 ? 140 LYS A CG 1 ATOM 1006 C CD . LYS A 1 140 ? -47.169 -5.977 92.234 1.00 59.40 ? 140 LYS A CD 1 ATOM 1007 C CE . LYS A 1 140 ? -48.030 -5.822 93.481 1.00 61.62 ? 140 LYS A CE 1 ATOM 1008 N NZ . LYS A 1 140 ? -47.212 -5.506 94.687 1.00 62.81 ? 140 LYS A NZ 1 ATOM 1009 N N . ARG A 1 141 ? -42.628 -4.178 89.610 1.00 46.48 ? 141 ARG A N 1 ATOM 1010 C CA . ARG A 1 141 ? -41.567 -4.573 88.682 1.00 48.90 ? 141 ARG A CA 1 ATOM 1011 C C . ARG A 1 141 ? -41.081 -5.956 89.115 1.00 53.79 ? 141 ARG A C 1 ATOM 1012 O O . ARG A 1 141 ? -40.652 -6.130 90.265 1.00 53.62 ? 141 ARG A O 1 ATOM 1013 C CB . ARG A 1 141 ? -40.412 -3.558 88.709 1.00 47.51 ? 141 ARG A CB 1 ATOM 1014 C CG . ARG A 1 141 ? -39.199 -3.936 87.860 1.00 47.23 ? 141 ARG A CG 1 ATOM 1015 C CD . ARG A 1 141 ? -38.137 -2.846 87.859 1.00 47.47 ? 141 ARG A CD 1 ATOM 1016 N NE . ARG A 1 141 ? -38.396 -1.797 86.858 1.00 47.46 ? 141 ARG A NE 1 ATOM 1017 C CZ . ARG A 1 141 ? -38.921 -0.589 87.097 1.00 46.33 ? 141 ARG A CZ 1 ATOM 1018 N NH1 . ARG A 1 141 ? -39.295 -0.215 88.322 1.00 46.27 ? 141 ARG A NH1 1 ATOM 1019 N NH2 . ARG A 1 141 ? -39.086 0.268 86.087 1.00 46.29 ? 141 ARG A NH2 1 ATOM 1020 N N . LYS A 1 142 ? -41.174 -6.933 88.212 1.00 58.04 ? 142 LYS A N 1 ATOM 1021 C CA . LYS A 1 142 ? -40.819 -8.327 88.514 1.00 62.33 ? 142 LYS A CA 1 ATOM 1022 C C . LYS A 1 142 ? -41.510 -8.807 89.796 1.00 63.87 ? 142 LYS A C 1 ATOM 1023 O O . LYS A 1 142 ? -40.872 -9.407 90.665 1.00 65.98 ? 142 LYS A O 1 ATOM 1024 C CB . LYS A 1 142 ? -39.291 -8.493 88.640 1.00 65.50 ? 142 LYS A CB 1 ATOM 1025 C CG . LYS A 1 142 ? -38.499 -8.153 87.382 1.00 67.56 ? 142 LYS A CG 1 ATOM 1026 C CD . LYS A 1 142 ? -38.836 -9.094 86.229 1.00 70.79 ? 142 LYS A CD 1 ATOM 1027 C CE . LYS A 1 142 ? -37.993 -8.808 84.992 1.00 72.10 ? 142 LYS A CE 1 ATOM 1028 N NZ . LYS A 1 142 ? -38.532 -9.500 83.785 1.00 72.95 ? 142 LYS A NZ 1 ATOM 1029 N N . SER A 1 143 ? -42.805 -8.508 89.910 1.00 64.31 ? 143 SER A N 1 ATOM 1030 C CA . SER A 1 143 ? -43.649 -8.939 91.043 1.00 64.60 ? 143 SER A CA 1 ATOM 1031 C C . SER A 1 143 ? -43.446 -8.166 92.359 1.00 62.57 ? 143 SER A C 1 ATOM 1032 O O . SER A 1 143 ? -44.255 -8.302 93.284 1.00 64.38 ? 143 SER A O 1 ATOM 1033 C CB . SER A 1 143 ? -43.497 -10.444 91.298 1.00 67.63 ? 143 SER A CB 1 ATOM 1034 O OG . SER A 1 143 ? -43.593 -11.164 90.081 1.00 70.25 ? 143 SER A OG 1 ATOM 1035 N N . ASN A 1 144 ? -42.394 -7.354 92.444 1.00 57.04 ? 144 ASN A N 1 ATOM 1036 C CA . ASN A 1 144 ? -42.132 -6.556 93.635 1.00 54.04 ? 144 ASN A CA 1 ATOM 1037 C C . ASN A 1 144 ? -42.663 -5.140 93.503 1.00 51.56 ? 144 ASN A C 1 ATOM 1038 O O . ASN A 1 144 ? -42.740 -4.605 92.392 1.00 46.95 ? 144 ASN A O 1 ATOM 1039 C CB . ASN A 1 144 ? -40.632 -6.475 93.901 1.00 55.15 ? 144 ASN A CB 1 ATOM 1040 C CG . ASN A 1 144 ? -40.019 -7.823 94.204 1.00 59.41 ? 144 ASN A CG 1 ATOM 1041 O OD1 . ASN A 1 144 ? -38.862 -8.070 93.867 1.00 64.77 ? 144 ASN A OD1 1 ATOM 1042 N ND2 . ASN A 1 144 ? -40.788 -8.705 94.837 1.00 58.15 ? 144 ASN A ND2 1 ATOM 1043 N N . ASN A 1 145 ? -42.998 -4.533 94.641 1.00 48.29 ? 145 ASN A N 1 ATOM 1044 C CA . ASN A 1 145 ? -43.316 -3.106 94.689 1.00 46.88 ? 145 ASN A CA 1 ATOM 1045 C C . ASN A 1 145 ? -42.132 -2.312 94.167 1.00 44.88 ? 145 ASN A C 1 ATOM 1046 O O . ASN A 1 145 ? -40.989 -2.611 94.500 1.00 43.95 ? 145 ASN A O 1 ATOM 1047 C CB . ASN A 1 145 ? -43.629 -2.671 96.116 1.00 47.60 ? 145 ASN A CB 1 ATOM 1048 C CG . ASN A 1 145 ? -44.948 -3.224 96.615 1.00 48.82 ? 145 ASN A CG 1 ATOM 1049 O OD1 . ASN A 1 145 ? -45.580 -4.047 95.944 1.00 48.76 ? 145 ASN A OD1 1 ATOM 1050 N ND2 . ASN A 1 145 ? -45.382 -2.762 97.796 1.00 48.35 ? 145 ASN A ND2 1 ATOM 1051 N N . SER A 1 146 ? -42.410 -1.310 93.333 1.00 44.09 ? 146 SER A N 1 ATOM 1052 C CA . SER A 1 146 ? -41.349 -0.554 92.684 1.00 41.45 ? 146 SER A CA 1 ATOM 1053 C C . SER A 1 146 ? -41.841 0.852 92.344 1.00 40.43 ? 146 SER A C 1 ATOM 1054 O O . SER A 1 146 ? -42.820 1.328 92.927 1.00 38.92 ? 146 SER A O 1 ATOM 1055 C CB . SER A 1 146 ? -40.871 -1.304 91.430 1.00 42.84 ? 146 SER A CB 1 ATOM 1056 O OG . SER A 1 146 ? -39.566 -0.894 91.047 1.00 41.74 ? 146 SER A OG 1 ATOM 1057 N N . PHE A 1 147 ? -41.161 1.501 91.398 1.00 38.46 ? 147 PHE A N 1 ATOM 1058 C CA . PHE A 1 147 ? -41.472 2.871 91.013 1.00 37.65 ? 147 PHE A CA 1 ATOM 1059 C C . PHE A 1 147 ? -40.863 3.148 89.635 1.00 34.84 ? 147 PHE A C 1 ATOM 1060 O O . PHE A 1 147 ? -40.054 2.363 89.104 1.00 33.32 ? 147 PHE A O 1 ATOM 1061 C CB . PHE A 1 147 ? -40.865 3.819 92.050 1.00 36.79 ? 147 PHE A CB 1 ATOM 1062 C CG . PHE A 1 147 ? -41.481 5.194 92.086 1.00 36.53 ? 147 PHE A CG 1 ATOM 1063 C CD1 . PHE A 1 147 ? -42.831 5.370 92.382 1.00 36.48 ? 147 PHE A CD1 1 ATOM 1064 C CD2 . PHE A 1 147 ? -40.683 6.323 91.894 1.00 36.61 ? 147 PHE A CD2 1 ATOM 1065 C CE1 . PHE A 1 147 ? -43.382 6.635 92.449 1.00 37.06 ? 147 PHE A CE1 1 ATOM 1066 C CE2 . PHE A 1 147 ? -41.228 7.588 91.959 1.00 36.76 ? 147 PHE A CE2 1 ATOM 1067 C CZ . PHE A 1 147 ? -42.581 7.750 92.231 1.00 37.61 ? 147 PHE A CZ 1 ATOM 1068 N N . PHE A 1 148 ? -41.242 4.274 89.070 1.00 33.96 ? 148 PHE A N 1 ATOM 1069 C CA . PHE A 1 148 ? -40.608 4.751 87.850 1.00 33.61 ? 148 PHE A CA 1 ATOM 1070 C C . PHE A 1 148 ? -39.091 4.650 87.960 1.00 34.79 ? 148 PHE A C 1 ATOM 1071 O O . PHE A 1 148 ? -38.482 5.150 88.921 1.00 34.74 ? 148 PHE A O 1 ATOM 1072 C CB . PHE A 1 148 ? -40.974 6.207 87.628 1.00 34.13 ? 148 PHE A CB 1 ATOM 1073 C CG . PHE A 1 148 ? -42.449 6.447 87.417 1.00 34.21 ? 148 PHE A CG 1 ATOM 1074 C CD1 . PHE A 1 148 ? -43.070 6.066 86.242 1.00 35.07 ? 148 PHE A CD1 1 ATOM 1075 C CD2 . PHE A 1 148 ? -43.208 7.067 88.398 1.00 35.91 ? 148 PHE A CD2 1 ATOM 1076 C CE1 . PHE A 1 148 ? -44.428 6.314 86.034 1.00 36.33 ? 148 PHE A CE1 1 ATOM 1077 C CE2 . PHE A 1 148 ? -44.565 7.315 88.209 1.00 36.16 ? 148 PHE A CE2 1 ATOM 1078 C CZ . PHE A 1 148 ? -45.178 6.935 87.022 1.00 37.14 ? 148 PHE A CZ 1 ATOM 1079 N N . SER A 1 149 ? -38.474 4.013 86.972 1.00 33.80 ? 149 SER A N 1 ATOM 1080 C CA . SER A 1 149 ? -37.031 3.771 87.000 1.00 33.85 ? 149 SER A CA 1 ATOM 1081 C C . SER A 1 149 ? -36.207 5.047 87.089 1.00 33.01 ? 149 SER A C 1 ATOM 1082 O O . SER A 1 149 ? -35.123 5.050 87.694 1.00 31.63 ? 149 SER A O 1 ATOM 1083 C CB . SER A 1 149 ? -36.579 2.980 85.760 1.00 35.27 ? 149 SER A CB 1 ATOM 1084 O OG . SER A 1 149 ? -36.729 3.746 84.555 1.00 33.02 ? 149 SER A OG 1 ATOM 1085 N N . ARG A 1 150 ? -36.693 6.133 86.479 1.00 30.41 ? 150 ARG A N 1 ATOM 1086 C CA . ARG A 1 150 ? -35.870 7.339 86.366 1.00 30.94 ? 150 ARG A CA 1 ATOM 1087 C C . ARG A 1 150 ? -36.142 8.357 87.482 1.00 30.44 ? 150 ARG A C 1 ATOM 1088 O O . ARG A 1 150 ? -35.499 9.406 87.520 1.00 29.82 ? 150 ARG A O 1 ATOM 1089 C CB . ARG A 1 150 ? -36.034 7.995 84.991 1.00 29.89 ? 150 ARG A CB 1 ATOM 1090 C CG . ARG A 1 150 ? -35.773 7.041 83.819 1.00 30.07 ? 150 ARG A CG 1 ATOM 1091 C CD . ARG A 1 150 ? -34.396 6.409 83.894 1.00 30.46 ? 150 ARG A CD 1 ATOM 1092 N NE . ARG A 1 150 ? -33.946 5.831 82.628 1.00 29.69 ? 150 ARG A NE 1 ATOM 1093 C CZ . ARG A 1 150 ? -32.826 5.127 82.480 1.00 29.46 ? 150 ARG A CZ 1 ATOM 1094 N NH1 . ARG A 1 150 ? -32.032 4.872 83.537 1.00 29.06 ? 150 ARG A NH1 1 ATOM 1095 N NH2 . ARG A 1 150 ? -32.487 4.671 81.276 1.00 28.52 ? 150 ARG A NH2 1 ATOM 1096 N N . LEU A 1 151 ? -37.047 8.010 88.396 1.00 30.47 ? 151 LEU A N 1 ATOM 1097 C CA . LEU A 1 151 ? -37.440 8.882 89.477 1.00 30.83 ? 151 LEU A CA 1 ATOM 1098 C C . LEU A 1 151 ? -37.171 8.215 90.837 1.00 32.17 ? 151 LEU A C 1 ATOM 1099 O O . LEU A 1 151 ? -37.137 6.989 90.966 1.00 32.54 ? 151 LEU A O 1 ATOM 1100 C CB . LEU A 1 151 ? -38.904 9.254 89.348 1.00 30.60 ? 151 LEU A CB 1 ATOM 1101 C CG . LEU A 1 151 ? -39.233 10.079 88.090 1.00 30.13 ? 151 LEU A CG 1 ATOM 1102 C CD1 . LEU A 1 151 ? -40.736 10.137 87.903 1.00 28.65 ? 151 LEU A CD1 1 ATOM 1103 C CD2 . LEU A 1 151 ? -38.631 11.500 88.114 1.00 28.96 ? 151 LEU A CD2 1 ATOM 1104 N N . ASN A 1 152 ? -36.996 9.066 91.831 1.00 33.54 ? 152 ASN A N 1 ATOM 1105 C CA . ASN A 1 152 ? -36.524 8.663 93.181 1.00 33.20 ? 152 ASN A CA 1 ATOM 1106 C C . ASN A 1 152 ? -37.479 9.272 94.207 1.00 34.46 ? 152 ASN A C 1 ATOM 1107 O O . ASN A 1 152 ? -37.447 10.472 94.466 1.00 34.95 ? 152 ASN A O 1 ATOM 1108 C CB . ASN A 1 152 ? -35.087 9.157 93.371 1.00 33.24 ? 152 ASN A CB 1 ATOM 1109 C CG . ASN A 1 152 ? -34.437 8.617 94.645 1.00 34.23 ? 152 ASN A CG 1 ATOM 1110 O OD1 . ASN A 1 152 ? -35.099 7.973 95.459 1.00 34.11 ? 152 ASN A OD1 1 ATOM 1111 N ND2 . ASN A 1 152 ? -33.135 8.875 94.810 1.00 33.68 ? 152 ASN A ND2 1 ATOM 1112 N N . TRP A 1 153 ? -38.376 8.440 94.724 1.00 35.73 ? 153 TRP A N 1 ATOM 1113 C CA . TRP A 1 153 ? -39.319 8.842 95.751 1.00 37.50 ? 153 TRP A CA 1 ATOM 1114 C C . TRP A 1 153 ? -38.624 8.940 97.092 1.00 39.17 ? 153 TRP A C 1 ATOM 1115 O O . TRP A 1 153 ? -38.370 7.922 97.729 1.00 39.83 ? 153 TRP A O 1 ATOM 1116 C CB . TRP A 1 153 ? -40.445 7.822 95.834 1.00 37.91 ? 153 TRP A CB 1 ATOM 1117 C CG . TRP A 1 153 ? -41.680 8.301 96.541 1.00 38.17 ? 153 TRP A CG 1 ATOM 1118 C CD1 . TRP A 1 153 ? -41.856 9.481 97.263 1.00 38.74 ? 153 TRP A CD1 1 ATOM 1119 C CD2 . TRP A 1 153 ? -42.980 7.619 96.605 1.00 39.57 ? 153 TRP A CD2 1 ATOM 1120 N NE1 . TRP A 1 153 ? -43.134 9.577 97.734 1.00 38.68 ? 153 TRP A NE1 1 ATOM 1121 C CE2 . TRP A 1 153 ? -43.862 8.493 97.378 1.00 39.69 ? 153 TRP A CE2 1 ATOM 1122 C CE3 . TRP A 1 153 ? -43.482 6.428 96.104 1.00 41.48 ? 153 TRP A CE3 1 ATOM 1123 C CZ2 . TRP A 1 153 ? -45.191 8.165 97.632 1.00 41.24 ? 153 TRP A CZ2 1 ATOM 1124 C CZ3 . TRP A 1 153 ? -44.818 6.090 96.385 1.00 42.04 ? 153 TRP A CZ3 1 ATOM 1125 C CH2 . TRP A 1 153 ? -45.658 6.952 97.114 1.00 42.58 ? 153 TRP A CH2 1 ATOM 1126 N N . LEU A 1 154 ? -38.328 10.170 97.521 1.00 39.52 ? 154 LEU A N 1 ATOM 1127 C CA . LEU A 1 154 ? -37.696 10.426 98.817 1.00 39.77 ? 154 LEU A CA 1 ATOM 1128 C C . LEU A 1 154 ? -38.764 10.511 99.922 1.00 40.89 ? 154 LEU A C 1 ATOM 1129 O O . LEU A 1 154 ? -39.830 11.112 99.738 1.00 39.12 ? 154 LEU A O 1 ATOM 1130 C CB . LEU A 1 154 ? -36.892 11.724 98.777 1.00 40.30 ? 154 LEU A CB 1 ATOM 1131 C CG . LEU A 1 154 ? -35.889 11.882 97.631 1.00 40.93 ? 154 LEU A CG 1 ATOM 1132 C CD1 . LEU A 1 154 ? -35.197 13.241 97.683 1.00 42.95 ? 154 LEU A CD1 1 ATOM 1133 C CD2 . LEU A 1 154 ? -34.876 10.755 97.596 1.00 39.27 ? 154 LEU A CD2 1 ATOM 1134 N N . THR A 1 155 ? -38.473 9.911 101.073 1.00 41.56 ? 155 THR A N 1 ATOM 1135 C CA . THR A 1 155 ? -39.392 9.967 102.222 1.00 42.75 ? 155 THR A CA 1 ATOM 1136 C C . THR A 1 155 ? -38.562 10.273 103.470 1.00 43.59 ? 155 THR A C 1 ATOM 1137 O O . THR A 1 155 ? -37.336 10.382 103.391 1.00 42.75 ? 155 THR A O 1 ATOM 1138 C CB . THR A 1 155 ? -40.177 8.641 102.407 1.00 42.76 ? 155 THR A CB 1 ATOM 1139 O OG1 . THR A 1 155 ? -39.259 7.549 102.493 1.00 42.73 ? 155 THR A OG1 1 ATOM 1140 C CG2 . THR A 1 155 ? -41.156 8.410 101.250 1.00 42.25 ? 155 THR A CG2 1 ATOM 1141 N N . HIS A 1 156 ? -39.223 10.419 104.616 1.00 45.86 ? 156 HIS A N 1 ATOM 1142 C CA . HIS A 1 156 ? -38.518 10.798 105.850 1.00 47.69 ? 156 HIS A CA 1 ATOM 1143 C C . HIS A 1 156 ? -37.517 9.752 106.265 1.00 48.49 ? 156 HIS A C 1 ATOM 1144 O O . HIS A 1 156 ? -37.638 8.582 105.878 1.00 48.12 ? 156 HIS A O 1 ATOM 1145 C CB . HIS A 1 156 ? -39.512 11.060 106.986 1.00 48.64 ? 156 HIS A CB 1 ATOM 1146 C CG . HIS A 1 156 ? -40.129 9.810 107.574 1.00 49.23 ? 156 HIS A CG 1 ATOM 1147 N ND1 . HIS A 1 156 ? -39.397 8.861 108.191 1.00 50.18 ? 156 HIS A ND1 1 ATOM 1148 C CD2 . HIS A 1 156 ? -41.458 9.394 107.653 1.00 50.55 ? 156 HIS A CD2 1 ATOM 1149 C CE1 . HIS A 1 156 ? -40.207 7.877 108.624 1.00 50.99 ? 156 HIS A CE1 1 ATOM 1150 N NE2 . HIS A 1 156 ? -41.472 8.205 108.301 1.00 51.48 ? 156 HIS A NE2 1 ATOM 1151 N N . LEU A 1 157 ? -36.522 10.172 107.054 1.00 50.30 ? 157 LEU A N 1 ATOM 1152 C CA . LEU A 1 157 ? -35.540 9.265 107.667 1.00 50.26 ? 157 LEU A CA 1 ATOM 1153 C C . LEU A 1 157 ? -35.661 9.424 109.188 1.00 51.83 ? 157 LEU A C 1 ATOM 1154 O O . LEU A 1 157 ? -35.433 10.514 109.712 1.00 49.48 ? 157 LEU A O 1 ATOM 1155 C CB . LEU A 1 157 ? -34.122 9.622 107.205 1.00 49.61 ? 157 LEU A CB 1 ATOM 1156 C CG . LEU A 1 157 ? -32.960 8.779 107.754 1.00 49.01 ? 157 LEU A CG 1 ATOM 1157 C CD1 . LEU A 1 157 ? -33.009 7.362 107.198 1.00 50.07 ? 157 LEU A CD1 1 ATOM 1158 C CD2 . LEU A 1 157 ? -31.606 9.413 107.479 1.00 48.04 ? 157 LEU A CD2 1 ATOM 1159 N N . LYS A 1 158 ? -36.052 8.349 109.876 1.00 54.60 ? 158 LYS A N 1 ATOM 1160 C CA . LYS A 1 158 ? -36.251 8.362 111.343 1.00 57.61 ? 158 LYS A CA 1 ATOM 1161 C C . LYS A 1 158 ? -37.281 9.419 111.756 1.00 57.85 ? 158 LYS A C 1 ATOM 1162 O O . LYS A 1 158 ? -37.125 10.066 112.788 1.00 57.93 ? 158 LYS A O 1 ATOM 1163 C CB . LYS A 1 158 ? -34.931 8.642 112.093 1.00 59.94 ? 158 LYS A CB 1 ATOM 1164 C CG . LYS A 1 158 ? -33.686 7.930 111.578 1.00 63.14 ? 158 LYS A CG 1 ATOM 1165 C CD . LYS A 1 158 ? -33.468 6.561 112.202 1.00 66.16 ? 158 LYS A CD 1 ATOM 1166 C CE . LYS A 1 158 ? -32.046 6.073 111.959 1.00 68.13 ? 158 LYS A CE 1 ATOM 1167 N NZ . LYS A 1 158 ? -31.613 6.228 110.538 1.00 69.38 ? 158 LYS A NZ 1 ATOM 1168 N N . PHE A 1 159 ? -38.312 9.603 110.933 1.00 54.57 ? 159 PHE A N 1 ATOM 1169 C CA . PHE A 1 159 ? -39.371 10.605 111.158 1.00 54.32 ? 159 PHE A CA 1 ATOM 1170 C C . PHE A 1 159 ? -38.901 12.067 111.099 1.00 52.59 ? 159 PHE A C 1 ATOM 1171 O O . PHE A 1 159 ? -39.573 12.961 111.613 1.00 50.37 ? 159 PHE A O 1 ATOM 1172 C CB . PHE A 1 159 ? -40.129 10.312 112.456 1.00 58.44 ? 159 PHE A CB 1 ATOM 1173 C CG . PHE A 1 159 ? -40.625 8.899 112.547 1.00 60.91 ? 159 PHE A CG 1 ATOM 1174 C CD1 . PHE A 1 159 ? -41.821 8.533 111.942 1.00 61.32 ? 159 PHE A CD1 1 ATOM 1175 C CD2 . PHE A 1 159 ? -39.889 7.926 113.222 1.00 62.90 ? 159 PHE A CD2 1 ATOM 1176 C CE1 . PHE A 1 159 ? -42.278 7.224 112.012 1.00 63.41 ? 159 PHE A CE1 1 ATOM 1177 C CE2 . PHE A 1 159 ? -40.341 6.617 113.297 1.00 63.19 ? 159 PHE A CE2 1 ATOM 1178 C CZ . PHE A 1 159 ? -41.538 6.265 112.692 1.00 63.74 ? 159 PHE A CZ 1 ATOM 1179 N N . LYS A 1 160 ? -37.761 12.293 110.443 1.00 52.53 ? 160 LYS A N 1 ATOM 1180 C CA . LYS A 1 160 ? -37.295 13.626 110.065 1.00 52.95 ? 160 LYS A CA 1 ATOM 1181 C C . LYS A 1 160 ? -37.198 13.730 108.528 1.00 51.54 ? 160 LYS A C 1 ATOM 1182 O O . LYS A 1 160 ? -36.827 12.773 107.843 1.00 48.51 ? 160 LYS A O 1 ATOM 1183 C CB . LYS A 1 160 ? -35.918 13.904 110.674 1.00 57.69 ? 160 LYS A CB 1 ATOM 1184 C CG . LYS A 1 160 ? -35.941 14.318 112.150 1.00 61.80 ? 160 LYS A CG 1 ATOM 1185 C CD . LYS A 1 160 ? -35.902 15.836 112.319 1.00 64.29 ? 160 LYS A CD 1 ATOM 1186 C CE . LYS A 1 160 ? -36.304 16.280 113.723 1.00 66.79 ? 160 LYS A CE 1 ATOM 1187 N NZ . LYS A 1 160 ? -35.371 15.806 114.788 1.00 67.49 ? 160 LYS A NZ 1 ATOM 1188 N N . TYR A 1 161 ? -37.524 14.901 108.006 1.00 51.50 ? 161 TYR A N 1 ATOM 1189 C CA . TYR A 1 161 ? -37.259 15.232 106.611 1.00 50.98 ? 161 TYR A CA 1 ATOM 1190 C C . TYR A 1 161 ? -36.633 16.625 106.616 1.00 52.06 ? 161 TYR A C 1 ATOM 1191 O O . TYR A 1 161 ? -37.350 17.627 106.610 1.00 51.71 ? 161 TYR A O 1 ATOM 1192 C CB . TYR A 1 161 ? -38.556 15.186 105.807 1.00 50.64 ? 161 TYR A CB 1 ATOM 1193 C CG . TYR A 1 161 ? -38.405 15.226 104.288 1.00 49.63 ? 161 TYR A CG 1 ATOM 1194 C CD1 . TYR A 1 161 ? -37.912 16.355 103.636 1.00 49.96 ? 161 TYR A CD1 1 ATOM 1195 C CD2 . TYR A 1 161 ? -38.787 14.135 103.505 1.00 50.65 ? 161 TYR A CD2 1 ATOM 1196 C CE1 . TYR A 1 161 ? -37.795 16.395 102.248 1.00 49.62 ? 161 TYR A CE1 1 ATOM 1197 C CE2 . TYR A 1 161 ? -38.683 14.170 102.113 1.00 49.62 ? 161 TYR A CE2 1 ATOM 1198 C CZ . TYR A 1 161 ? -38.181 15.301 101.490 1.00 50.07 ? 161 TYR A CZ 1 ATOM 1199 O OH . TYR A 1 161 ? -38.083 15.337 100.108 1.00 47.81 ? 161 TYR A OH 1 ATOM 1200 N N . PRO A 1 162 ? -35.286 16.690 106.674 1.00 54.53 ? 162 PRO A N 1 ATOM 1201 C CA . PRO A 1 162 ? -34.577 17.970 106.673 1.00 55.83 ? 162 PRO A CA 1 ATOM 1202 C C . PRO A 1 162 ? -34.848 18.733 105.392 1.00 56.83 ? 162 PRO A C 1 ATOM 1203 O O . PRO A 1 162 ? -35.077 18.111 104.352 1.00 59.02 ? 162 PRO A O 1 ATOM 1204 C CB . PRO A 1 162 ? -33.090 17.573 106.740 1.00 56.86 ? 162 PRO A CB 1 ATOM 1205 C CG . PRO A 1 162 ? -33.057 16.142 107.146 1.00 57.40 ? 162 PRO A CG 1 ATOM 1206 C CD . PRO A 1 162 ? -34.359 15.543 106.698 1.00 56.35 ? 162 PRO A CD 1 ATOM 1207 N N . ALA A 1 163 ? -34.829 20.059 105.471 1.00 56.08 ? 163 ALA A N 1 ATOM 1208 C CA . ALA A 1 163 ? -35.018 20.906 104.304 1.00 56.12 ? 163 ALA A CA 1 ATOM 1209 C C . ALA A 1 163 ? -33.901 20.623 103.305 1.00 55.76 ? 163 ALA A C 1 ATOM 1210 O O . ALA A 1 163 ? -32.721 20.735 103.645 1.00 57.35 ? 163 ALA A O 1 ATOM 1211 C CB . ALA A 1 163 ? -35.014 22.374 104.701 1.00 57.43 ? 163 ALA A CB 1 ATOM 1212 N N . LEU A 1 164 ? -34.277 20.221 102.090 1.00 51.66 ? 164 LEU A N 1 ATOM 1213 C CA . LEU A 1 164 ? -33.300 19.882 101.063 1.00 50.64 ? 164 LEU A CA 1 ATOM 1214 C C . LEU A 1 164 ? -32.928 21.127 100.293 1.00 49.11 ? 164 LEU A C 1 ATOM 1215 O O . LEU A 1 164 ? -33.773 21.973 100.021 1.00 48.10 ? 164 LEU A O 1 ATOM 1216 C CB . LEU A 1 164 ? -33.852 18.830 100.105 1.00 49.45 ? 164 LEU A CB 1 ATOM 1217 C CG . LEU A 1 164 ? -34.105 17.453 100.722 1.00 49.81 ? 164 LEU A CG 1 ATOM 1218 C CD1 . LEU A 1 164 ? -34.906 16.597 99.749 1.00 50.34 ? 164 LEU A CD1 1 ATOM 1219 C CD2 . LEU A 1 164 ? -32.790 16.771 101.088 1.00 48.89 ? 164 LEU A CD2 1 ATOM 1220 N N . ASN A 1 165 ? -31.649 21.231 99.964 1.00 48.87 ? 165 ASN A N 1 ATOM 1221 C CA . ASN A 1 165 ? -31.139 22.330 99.181 1.00 49.66 ? 165 ASN A CA 1 ATOM 1222 C C . ASN A 1 165 ? -29.978 21.782 98.365 1.00 49.52 ? 165 ASN A C 1 ATOM 1223 O O . ASN A 1 165 ? -28.808 21.949 98.734 1.00 48.38 ? 165 ASN A O 1 ATOM 1224 C CB . ASN A 1 165 ? -30.719 23.481 100.091 1.00 52.22 ? 165 ASN A CB 1 ATOM 1225 C CG . ASN A 1 165 ? -30.220 24.685 99.316 1.00 54.23 ? 165 ASN A CG 1 ATOM 1226 O OD1 . ASN A 1 165 ? -30.909 25.228 98.443 1.00 54.67 ? 165 ASN A OD1 1 ATOM 1227 N ND2 . ASN A 1 165 ? -29.009 25.105 99.635 1.00 54.41 ? 165 ASN A ND2 1 ATOM 1228 N N . VAL A 1 166 ? -30.325 21.110 97.260 1.00 46.41 ? 166 VAL A N 1 ATOM 1229 C CA . VAL A 1 166 ? -29.386 20.251 96.546 1.00 45.67 ? 166 VAL A CA 1 ATOM 1230 C C . VAL A 1 166 ? -29.045 20.808 95.173 1.00 45.35 ? 166 VAL A C 1 ATOM 1231 O O . VAL A 1 166 ? -29.927 21.244 94.420 1.00 42.91 ? 166 VAL A O 1 ATOM 1232 C CB . VAL A 1 166 ? -29.936 18.811 96.434 1.00 46.07 ? 166 VAL A CB 1 ATOM 1233 C CG1 . VAL A 1 166 ? -29.031 17.955 95.569 1.00 46.10 ? 166 VAL A CG1 1 ATOM 1234 C CG2 . VAL A 1 166 ? -30.074 18.191 97.829 1.00 47.54 ? 166 VAL A CG2 1 ATOM 1235 N N . THR A 1 167 ? -27.759 20.755 94.856 1.00 45.64 ? 167 THR A N 1 ATOM 1236 C CA . THR A 1 167 ? -27.219 21.324 93.636 1.00 47.87 ? 167 THR A CA 1 ATOM 1237 C C . THR A 1 167 ? -26.695 20.244 92.645 1.00 46.37 ? 167 THR A C 1 ATOM 1238 O O . THR A 1 167 ? -26.171 19.186 93.048 1.00 45.40 ? 167 THR A O 1 ATOM 1239 C CB . THR A 1 167 ? -26.078 22.302 93.994 1.00 51.65 ? 167 THR A CB 1 ATOM 1240 O OG1 . THR A 1 167 ? -25.710 23.050 92.834 1.00 59.09 ? 167 THR A OG1 1 ATOM 1241 C CG2 . THR A 1 167 ? -24.862 21.559 94.502 1.00 52.49 ? 167 THR A CG2 1 ATOM 1242 N N . MET A 1 168 ? -26.824 20.512 91.348 1.00 42.83 ? 168 MET A N 1 ATOM 1243 C CA . MET A 1 168 ? -26.152 19.696 90.345 1.00 42.69 ? 168 MET A CA 1 ATOM 1244 C C . MET A 1 168 ? -25.675 20.578 89.189 1.00 43.21 ? 168 MET A C 1 ATOM 1245 O O . MET A 1 168 ? -26.486 20.999 88.352 1.00 41.09 ? 168 MET A O 1 ATOM 1246 C CB . MET A 1 168 ? -27.076 18.586 89.831 1.00 42.66 ? 168 MET A CB 1 ATOM 1247 C CG . MET A 1 168 ? -26.392 17.557 88.954 1.00 42.32 ? 168 MET A CG 1 ATOM 1248 S SD . MET A 1 168 ? -25.065 16.610 89.769 1.00 44.60 ? 168 MET A SD 1 ATOM 1249 C CE . MET A 1 168 ? -26.024 15.712 90.990 1.00 46.03 ? 168 MET A CE 1 ATOM 1250 N N . PRO A 1 169 ? -24.362 20.875 89.145 1.00 42.98 ? 169 PRO A N 1 ATOM 1251 C CA . PRO A 1 169 ? -23.851 21.697 88.040 1.00 43.45 ? 169 PRO A CA 1 ATOM 1252 C C . PRO A 1 169 ? -23.823 20.952 86.704 1.00 41.79 ? 169 PRO A C 1 ATOM 1253 O O . PRO A 1 169 ? -23.668 19.736 86.680 1.00 41.15 ? 169 PRO A O 1 ATOM 1254 C CB . PRO A 1 169 ? -22.432 22.058 88.488 1.00 45.27 ? 169 PRO A CB 1 ATOM 1255 C CG . PRO A 1 169 ? -22.044 21.003 89.465 1.00 45.89 ? 169 PRO A CG 1 ATOM 1256 C CD . PRO A 1 169 ? -23.306 20.525 90.120 1.00 44.85 ? 169 PRO A CD 1 ATOM 1257 N N . ASN A 1 170 ? -24.023 21.681 85.610 1.00 42.38 ? 170 ASN A N 1 ATOM 1258 C CA . ASN A 1 170 ? -23.776 21.163 84.268 1.00 42.42 ? 170 ASN A CA 1 ATOM 1259 C C . ASN A 1 170 ? -22.389 21.644 83.834 1.00 45.06 ? 170 ASN A C 1 ATOM 1260 O O . ASN A 1 170 ? -22.219 22.796 83.423 1.00 43.82 ? 170 ASN A O 1 ATOM 1261 C CB . ASN A 1 170 ? -24.858 21.626 83.251 1.00 41.69 ? 170 ASN A CB 1 ATOM 1262 C CG . ASN A 1 170 ? -24.628 21.071 81.846 1.00 41.53 ? 170 ASN A CG 1 ATOM 1263 O OD1 . ASN A 1 170 ? -23.607 20.422 81.573 1.00 42.23 ? 170 ASN A OD1 1 ATOM 1264 N ND2 . ASN A 1 170 ? -25.591 21.311 80.938 1.00 42.76 ? 170 ASN A ND2 1 ATOM 1265 N N . ASN A 1 171 ? -21.414 20.747 83.943 1.00 47.56 ? 171 ASN A N 1 ATOM 1266 C CA . ASN A 1 171 ? -20.049 21.010 83.487 1.00 51.29 ? 171 ASN A CA 1 ATOM 1267 C C . ASN A 1 171 ? -19.767 20.315 82.169 1.00 52.33 ? 171 ASN A C 1 ATOM 1268 O O . ASN A 1 171 ? -18.605 20.117 81.816 1.00 55.20 ? 171 ASN A O 1 ATOM 1269 C CB . ASN A 1 171 ? -19.037 20.559 84.546 1.00 53.75 ? 171 ASN A CB 1 ATOM 1270 C CG . ASN A 1 171 ? -19.237 21.257 85.872 1.00 54.62 ? 171 ASN A CG 1 ATOM 1271 O OD1 . ASN A 1 171 ? -19.166 20.633 86.931 1.00 59.82 ? 171 ASN A OD1 1 ATOM 1272 N ND2 . ASN A 1 171 ? -19.499 22.558 85.826 1.00 53.94 ? 171 ASN A ND2 1 ATOM 1273 N N . GLU A 1 172 ? -20.832 19.943 81.452 1.00 48.89 ? 172 GLU A N 1 ATOM 1274 C CA . GLU A 1 172 ? -20.730 19.275 80.157 1.00 50.52 ? 172 GLU A CA 1 ATOM 1275 C C . GLU A 1 172 ? -20.840 20.315 79.061 1.00 50.58 ? 172 GLU A C 1 ATOM 1276 O O . GLU A 1 172 ? -21.149 21.470 79.322 1.00 48.74 ? 172 GLU A O 1 ATOM 1277 C CB . GLU A 1 172 ? -21.863 18.250 79.964 1.00 50.30 ? 172 GLU A CB 1 ATOM 1278 C CG . GLU A 1 172 ? -21.994 17.231 81.080 1.00 51.02 ? 172 GLU A CG 1 ATOM 1279 C CD . GLU A 1 172 ? -20.764 16.357 81.213 1.00 52.99 ? 172 GLU A CD 1 ATOM 1280 O OE1 . GLU A 1 172 ? -20.138 16.027 80.186 1.00 54.83 ? 172 GLU A OE1 1 ATOM 1281 O OE2 . GLU A 1 172 ? -20.416 16.014 82.355 1.00 58.66 ? 172 GLU A OE2 1 ATOM 1282 N N . LYS A 1 173 ? -20.605 19.877 77.832 1.00 52.03 ? 173 LYS A N 1 ATOM 1283 C CA . LYS A 1 173 ? -20.672 20.734 76.659 1.00 55.55 ? 173 LYS A CA 1 ATOM 1284 C C . LYS A 1 173 ? -22.074 20.740 76.043 1.00 54.04 ? 173 LYS A C 1 ATOM 1285 O O . LYS A 1 173 ? -22.338 21.530 75.136 1.00 55.12 ? 173 LYS A O 1 ATOM 1286 C CB . LYS A 1 173 ? -19.669 20.238 75.609 1.00 60.74 ? 173 LYS A CB 1 ATOM 1287 C CG . LYS A 1 173 ? -18.893 21.340 74.905 1.00 65.10 ? 173 LYS A CG 1 ATOM 1288 C CD . LYS A 1 173 ? -17.712 21.827 75.736 1.00 68.36 ? 173 LYS A CD 1 ATOM 1289 C CE . LYS A 1 173 ? -16.625 22.439 74.858 1.00 71.06 ? 173 LYS A CE 1 ATOM 1290 N NZ . LYS A 1 173 ? -15.392 22.748 75.635 1.00 72.08 ? 173 LYS A NZ 1 ATOM 1291 N N . PHE A 1 174 ? -22.963 19.872 76.543 1.00 51.83 ? 174 PHE A N 1 ATOM 1292 C CA . PHE A 1 174 ? -24.330 19.692 76.005 1.00 48.14 ? 174 PHE A CA 1 ATOM 1293 C C . PHE A 1 174 ? -25.398 20.009 77.067 1.00 46.11 ? 174 PHE A C 1 ATOM 1294 O O . PHE A 1 174 ? -25.103 20.068 78.260 1.00 44.35 ? 174 PHE A O 1 ATOM 1295 C CB . PHE A 1 174 ? -24.527 18.249 75.500 1.00 48.39 ? 174 PHE A CB 1 ATOM 1296 C CG . PHE A 1 174 ? -24.067 17.205 76.477 1.00 49.73 ? 174 PHE A CG 1 ATOM 1297 C CD1 . PHE A 1 174 ? -24.839 16.888 77.596 1.00 48.48 ? 174 PHE A CD1 1 ATOM 1298 C CD2 . PHE A 1 174 ? -22.842 16.572 76.310 1.00 50.30 ? 174 PHE A CD2 1 ATOM 1299 C CE1 . PHE A 1 174 ? -24.401 15.950 78.513 1.00 49.42 ? 174 PHE A CE1 1 ATOM 1300 C CE2 . PHE A 1 174 ? -22.396 15.626 77.225 1.00 51.38 ? 174 PHE A CE2 1 ATOM 1301 C CZ . PHE A 1 174 ? -23.175 15.318 78.332 1.00 51.81 ? 174 PHE A CZ 1 ATOM 1302 N N . ASP A 1 175 ? -26.635 20.204 76.626 1.00 42.52 ? 175 ASP A N 1 ATOM 1303 C CA . ASP A 1 175 ? -27.755 20.503 77.533 1.00 42.04 ? 175 ASP A CA 1 ATOM 1304 C C . ASP A 1 175 ? -28.230 19.254 78.263 1.00 39.56 ? 175 ASP A C 1 ATOM 1305 O O . ASP A 1 175 ? -28.070 18.144 77.766 1.00 39.25 ? 175 ASP A O 1 ATOM 1306 C CB . ASP A 1 175 ? -28.946 21.088 76.778 1.00 43.17 ? 175 ASP A CB 1 ATOM 1307 C CG . ASP A 1 175 ? -28.700 22.506 76.266 1.00 47.05 ? 175 ASP A CG 1 ATOM 1308 O OD1 . ASP A 1 175 ? -27.632 23.085 76.568 1.00 47.65 ? 175 ASP A OD1 1 ATOM 1309 O OD2 . ASP A 1 175 ? -29.597 23.036 75.553 1.00 44.64 ? 175 ASP A OD2 1 ATOM 1310 N N . LYS A 1 176 ? -28.794 19.454 79.454 1.00 36.97 ? 176 LYS A N 1 ATOM 1311 C CA . LYS A 1 176 ? -29.364 18.367 80.236 1.00 35.84 ? 176 LYS A CA 1 ATOM 1312 C C . LYS A 1 176 ? -30.861 18.584 80.421 1.00 33.76 ? 176 LYS A C 1 ATOM 1313 O O . LYS A 1 176 ? -31.294 19.686 80.804 1.00 34.70 ? 176 LYS A O 1 ATOM 1314 C CB . LYS A 1 176 ? -28.715 18.299 81.625 1.00 36.56 ? 176 LYS A CB 1 ATOM 1315 C CG . LYS A 1 176 ? -27.220 18.054 81.633 1.00 37.38 ? 176 LYS A CG 1 ATOM 1316 C CD . LYS A 1 176 ? -26.698 18.178 83.056 1.00 38.60 ? 176 LYS A CD 1 ATOM 1317 C CE . LYS A 1 176 ? -25.265 17.712 83.214 1.00 38.80 ? 176 LYS A CE 1 ATOM 1318 N NZ . LYS A 1 176 ? -24.901 17.666 84.664 1.00 38.89 ? 176 LYS A NZ 1 ATOM 1319 N N . LEU A 1 177 ? -31.633 17.533 80.191 1.00 32.28 ? 177 LEU A N 1 ATOM 1320 C CA . LEU A 1 177 ? -33.085 17.550 80.438 1.00 31.56 ? 177 LEU A CA 1 ATOM 1321 C C . LEU A 1 177 ? -33.364 16.768 81.716 1.00 30.52 ? 177 LEU A C 1 ATOM 1322 O O . LEU A 1 177 ? -33.143 15.568 81.756 1.00 29.35 ? 177 LEU A O 1 ATOM 1323 C CB . LEU A 1 177 ? -33.858 16.919 79.280 1.00 30.54 ? 177 LEU A CB 1 ATOM 1324 C CG . LEU A 1 177 ? -35.369 16.674 79.462 1.00 30.82 ? 177 LEU A CG 1 ATOM 1325 C CD1 . LEU A 1 177 ? -36.137 17.966 79.737 1.00 31.02 ? 177 LEU A CD1 1 ATOM 1326 C CD2 . LEU A 1 177 ? -35.912 15.988 78.215 1.00 30.83 ? 177 LEU A CD2 1 ATOM 1327 N N . TYR A 1 178 ? -33.903 17.455 82.709 1.00 30.94 ? 178 TYR A N 1 ATOM 1328 C CA . TYR A 1 178 ? -34.255 16.862 84.003 1.00 32.09 ? 178 TYR A CA 1 ATOM 1329 C C . TYR A 1 178 ? -35.769 16.721 84.096 1.00 32.40 ? 178 TYR A C 1 ATOM 1330 O O . TYR A 1 178 ? -36.512 17.664 83.760 1.00 31.89 ? 178 TYR A O 1 ATOM 1331 C CB . TYR A 1 178 ? -33.773 17.742 85.142 1.00 32.90 ? 178 TYR A CB 1 ATOM 1332 C CG . TYR A 1 178 ? -32.294 17.640 85.401 1.00 34.34 ? 178 TYR A CG 1 ATOM 1333 C CD1 . TYR A 1 178 ? -31.761 16.544 86.079 1.00 35.23 ? 178 TYR A CD1 1 ATOM 1334 C CD2 . TYR A 1 178 ? -31.422 18.626 84.952 1.00 34.72 ? 178 TYR A CD2 1 ATOM 1335 C CE1 . TYR A 1 178 ? -30.394 16.434 86.324 1.00 35.37 ? 178 TYR A CE1 1 ATOM 1336 C CE2 . TYR A 1 178 ? -30.060 18.540 85.190 1.00 35.65 ? 178 TYR A CE2 1 ATOM 1337 C CZ . TYR A 1 178 ? -29.545 17.435 85.883 1.00 36.21 ? 178 TYR A CZ 1 ATOM 1338 O OH . TYR A 1 178 ? -28.188 17.361 86.114 1.00 37.63 ? 178 TYR A OH 1 ATOM 1339 N N . ILE A 1 179 ? -36.212 15.530 84.497 1.00 30.85 ? 179 ILE A N 1 ATOM 1340 C CA . ILE A 1 179 ? -37.632 15.230 84.713 1.00 30.46 ? 179 ILE A CA 1 ATOM 1341 C C . ILE A 1 179 ? -37.796 14.943 86.201 1.00 31.18 ? 179 ILE A C 1 ATOM 1342 O O . ILE A 1 179 ? -37.024 14.159 86.769 1.00 31.06 ? 179 ILE A O 1 ATOM 1343 C CB . ILE A 1 179 ? -38.064 13.968 83.936 1.00 30.73 ? 179 ILE A CB 1 ATOM 1344 C CG1 . ILE A 1 179 ? -37.707 14.065 82.438 1.00 30.59 ? 179 ILE A CG1 1 ATOM 1345 C CG2 . ILE A 1 179 ? -39.556 13.722 84.110 1.00 30.41 ? 179 ILE A CG2 1 ATOM 1346 C CD1 . ILE A 1 179 ? -38.392 15.212 81.702 1.00 30.10 ? 179 ILE A CD1 1 ATOM 1347 N N . TRP A 1 180 ? -38.758 15.606 86.829 1.00 30.68 ? 180 TRP A N 1 ATOM 1348 C CA . TRP A 1 180 ? -38.973 15.480 88.266 1.00 32.60 ? 180 TRP A CA 1 ATOM 1349 C C . TRP A 1 180 ? -40.424 15.625 88.542 1.00 33.18 ? 180 TRP A C 1 ATOM 1350 O O . TRP A 1 180 ? -41.200 15.872 87.618 1.00 32.78 ? 180 TRP A O 1 ATOM 1351 C CB . TRP A 1 180 ? -38.147 16.496 89.019 1.00 33.35 ? 180 TRP A CB 1 ATOM 1352 C CG . TRP A 1 180 ? -38.306 17.915 88.536 1.00 34.86 ? 180 TRP A CG 1 ATOM 1353 C CD1 . TRP A 1 180 ? -37.614 18.542 87.496 1.00 35.41 ? 180 TRP A CD1 1 ATOM 1354 C CD2 . TRP A 1 180 ? -39.209 18.943 89.073 1.00 35.90 ? 180 TRP A CD2 1 ATOM 1355 N NE1 . TRP A 1 180 ? -38.021 19.851 87.362 1.00 35.76 ? 180 TRP A NE1 1 ATOM 1356 C CE2 . TRP A 1 180 ? -38.983 20.149 88.271 1.00 35.63 ? 180 TRP A CE2 1 ATOM 1357 C CE3 . TRP A 1 180 ? -40.145 18.984 90.102 1.00 36.02 ? 180 TRP A CE3 1 ATOM 1358 C CZ2 . TRP A 1 180 ? -39.673 21.331 88.511 1.00 35.78 ? 180 TRP A CZ2 1 ATOM 1359 C CZ3 . TRP A 1 180 ? -40.827 20.186 90.344 1.00 36.84 ? 180 TRP A CZ3 1 ATOM 1360 C CH2 . TRP A 1 180 ? -40.607 21.327 89.552 1.00 35.91 ? 180 TRP A CH2 1 ATOM 1361 N N . GLY A 1 181 ? -40.821 15.457 89.799 1.00 33.38 ? 181 GLY A N 1 ATOM 1362 C CA . GLY A 1 181 ? -42.236 15.406 90.100 1.00 32.92 ? 181 GLY A CA 1 ATOM 1363 C C . GLY A 1 181 ? -42.585 15.897 91.475 1.00 34.64 ? 181 GLY A C 1 ATOM 1364 O O . GLY A 1 181 ? -41.710 16.047 92.339 1.00 33.97 ? 181 GLY A O 1 ATOM 1365 N N . VAL A 1 182 ? -43.881 16.137 91.669 1.00 34.35 ? 182 VAL A N 1 ATOM 1366 C CA . VAL A 1 182 ? -44.412 16.484 92.961 1.00 36.07 ? 182 VAL A CA 1 ATOM 1367 C C . VAL A 1 182 ? -45.513 15.495 93.310 1.00 35.96 ? 182 VAL A C 1 ATOM 1368 O O . VAL A 1 182 ? -46.410 15.251 92.521 1.00 33.92 ? 182 VAL A O 1 ATOM 1369 C CB . VAL A 1 182 ? -44.978 17.924 92.995 1.00 37.59 ? 182 VAL A CB 1 ATOM 1370 C CG1 . VAL A 1 182 ? -45.465 18.263 94.400 1.00 39.40 ? 182 VAL A CG1 1 ATOM 1371 C CG2 . VAL A 1 182 ? -43.896 18.911 92.575 1.00 38.08 ? 182 VAL A CG2 1 ATOM 1372 N N . HIS A 1 183 ? -45.423 14.935 94.507 1.00 37.25 ? 183 HIS A N 1 ATOM 1373 C CA . HIS A 1 183 ? -46.420 13.989 94.994 1.00 38.30 ? 183 HIS A CA 1 ATOM 1374 C C . HIS A 1 183 ? -47.521 14.708 95.721 1.00 38.25 ? 183 HIS A C 1 ATOM 1375 O O . HIS A 1 183 ? -47.256 15.512 96.620 1.00 38.97 ? 183 HIS A O 1 ATOM 1376 C CB . HIS A 1 183 ? -45.758 12.980 95.925 1.00 39.20 ? 183 HIS A CB 1 ATOM 1377 C CG . HIS A 1 183 ? -46.688 11.905 96.390 1.00 40.14 ? 183 HIS A CG 1 ATOM 1378 N ND1 . HIS A 1 183 ? -46.881 11.630 97.693 1.00 41.00 ? 183 HIS A ND1 1 ATOM 1379 C CD2 . HIS A 1 183 ? -47.522 11.048 95.678 1.00 40.50 ? 183 HIS A CD2 1 ATOM 1380 C CE1 . HIS A 1 183 ? -47.775 10.632 97.810 1.00 40.23 ? 183 HIS A CE1 1 ATOM 1381 N NE2 . HIS A 1 183 ? -48.165 10.273 96.579 1.00 40.78 ? 183 HIS A NE2 1 ATOM 1382 N N . HIS A 1 184 ? -48.758 14.438 95.315 1.00 39.51 ? 184 HIS A N 1 ATOM 1383 C CA . HIS A 1 184 ? -49.961 14.970 95.957 1.00 40.42 ? 184 HIS A CA 1 ATOM 1384 C C . HIS A 1 184 ? -50.631 13.844 96.728 1.00 40.57 ? 184 HIS A C 1 ATOM 1385 O O . HIS A 1 184 ? -51.373 13.054 96.136 1.00 39.78 ? 184 HIS A O 1 ATOM 1386 C CB . HIS A 1 184 ? -50.925 15.481 94.896 1.00 40.38 ? 184 HIS A CB 1 ATOM 1387 C CG . HIS A 1 184 ? -50.353 16.560 93.988 1.00 41.74 ? 184 HIS A CG 1 ATOM 1388 N ND1 . HIS A 1 184 ? -50.207 17.839 94.381 1.00 41.28 ? 184 HIS A ND1 1 ATOM 1389 C CD2 . HIS A 1 184 ? -49.929 16.507 92.650 1.00 41.19 ? 184 HIS A CD2 1 ATOM 1390 C CE1 . HIS A 1 184 ? -49.710 18.575 93.351 1.00 41.89 ? 184 HIS A CE1 1 ATOM 1391 N NE2 . HIS A 1 184 ? -49.540 17.758 92.295 1.00 40.93 ? 184 HIS A NE2 1 ATOM 1392 N N . PRO A 1 185 ? -50.370 13.730 98.049 1.00 41.83 ? 185 PRO A N 1 ATOM 1393 C CA . PRO A 1 185 ? -50.976 12.617 98.804 1.00 42.91 ? 185 PRO A CA 1 ATOM 1394 C C . PRO A 1 185 ? -52.502 12.724 98.921 1.00 43.10 ? 185 PRO A C 1 ATOM 1395 O O . PRO A 1 185 ? -53.041 13.818 98.959 1.00 41.15 ? 185 PRO A O 1 ATOM 1396 C CB . PRO A 1 185 ? -50.330 12.726 100.190 1.00 44.10 ? 185 PRO A CB 1 ATOM 1397 C CG . PRO A 1 185 ? -49.210 13.693 100.043 1.00 43.58 ? 185 PRO A CG 1 ATOM 1398 C CD . PRO A 1 185 ? -49.590 14.608 98.930 1.00 42.60 ? 185 PRO A CD 1 ATOM 1399 N N . GLY A 1 186 ? -53.180 11.580 98.967 1.00 44.69 ? 186 GLY A N 1 ATOM 1400 C CA . GLY A 1 186 ? -54.643 11.544 99.068 1.00 45.79 ? 186 GLY A CA 1 ATOM 1401 C C . GLY A 1 186 ? -55.189 12.124 100.375 1.00 48.08 ? 186 GLY A C 1 ATOM 1402 O O . GLY A 1 186 ? -56.287 12.698 100.380 1.00 50.10 ? 186 GLY A O 1 ATOM 1403 N N . THR A 1 187 ? -54.426 11.980 101.464 1.00 49.05 ? 187 THR A N 1 ATOM 1404 C CA . THR A 1 187 ? -54.830 12.437 102.815 1.00 52.19 ? 187 THR A CA 1 ATOM 1405 C C . THR A 1 187 ? -53.681 13.024 103.668 1.00 53.09 ? 187 THR A C 1 ATOM 1406 O O . THR A 1 187 ? -52.500 12.817 103.383 1.00 50.83 ? 187 THR A O 1 ATOM 1407 C CB . THR A 1 187 ? -55.450 11.271 103.613 1.00 53.18 ? 187 THR A CB 1 ATOM 1408 O OG1 . THR A 1 187 ? -54.414 10.364 104.024 1.00 53.60 ? 187 THR A OG1 1 ATOM 1409 C CG2 . THR A 1 187 ? -56.503 10.526 102.766 1.00 52.68 ? 187 THR A CG2 1 ATOM 1410 N N . ASP A 1 188 ? -54.043 13.731 104.737 1.00 56.34 ? 188 ASP A N 1 ATOM 1411 C CA . ASP A 1 188 ? -53.059 14.284 105.679 1.00 59.05 ? 188 ASP A CA 1 ATOM 1412 C C . ASP A 1 188 ? -52.291 13.172 106.413 1.00 57.49 ? 188 ASP A C 1 ATOM 1413 O O . ASP A 1 188 ? -51.114 13.336 106.735 1.00 54.29 ? 188 ASP A O 1 ATOM 1414 C CB . ASP A 1 188 ? -53.731 15.225 106.693 1.00 62.84 ? 188 ASP A CB 1 ATOM 1415 C CG . ASP A 1 188 ? -54.435 16.400 106.026 1.00 66.78 ? 188 ASP A CG 1 ATOM 1416 O OD1 . ASP A 1 188 ? -53.798 17.107 105.209 1.00 69.56 ? 188 ASP A OD1 1 ATOM 1417 O OD2 . ASP A 1 188 ? -55.636 16.613 106.304 1.00 70.18 ? 188 ASP A OD2 1 ATOM 1418 N N . ASN A 1 189 ? -52.959 12.045 106.663 1.00 57.87 ? 189 ASN A N 1 ATOM 1419 C CA . ASN A 1 189 ? -52.300 10.849 107.205 1.00 58.13 ? 189 ASN A CA 1 ATOM 1420 C C . ASN A 1 189 ? -51.143 10.356 106.345 1.00 55.01 ? 189 ASN A C 1 ATOM 1421 O O . ASN A 1 189 ? -50.093 9.980 106.864 1.00 52.52 ? 189 ASN A O 1 ATOM 1422 C CB . ASN A 1 189 ? -53.308 9.702 107.370 1.00 61.31 ? 189 ASN A CB 1 ATOM 1423 C CG . ASN A 1 189 ? -54.036 9.736 108.705 1.00 65.80 ? 189 ASN A CG 1 ATOM 1424 O OD1 . ASN A 1 189 ? -55.011 9.009 108.904 1.00 69.18 ? 189 ASN A OD1 1 ATOM 1425 N ND2 . ASN A 1 189 ? -53.565 10.573 109.627 1.00 66.94 ? 189 ASN A ND2 1 ATOM 1426 N N . ASP A 1 190 ? -51.353 10.336 105.029 1.00 53.81 ? 190 ASP A N 1 ATOM 1427 C CA . ASP A 1 190 ? -50.316 9.898 104.095 1.00 52.52 ? 190 ASP A CA 1 ATOM 1428 C C . ASP A 1 190 ? -49.168 10.893 104.064 1.00 48.76 ? 190 ASP A C 1 ATOM 1429 O O . ASP A 1 190 ? -48.021 10.497 104.000 1.00 46.91 ? 190 ASP A O 1 ATOM 1430 C CB . ASP A 1 190 ? -50.888 9.728 102.680 1.00 54.32 ? 190 ASP A CB 1 ATOM 1431 C CG . ASP A 1 190 ? -51.692 8.445 102.514 1.00 57.37 ? 190 ASP A CG 1 ATOM 1432 O OD1 . ASP A 1 190 ? -51.645 7.563 103.394 1.00 62.01 ? 190 ASP A OD1 1 ATOM 1433 O OD2 . ASP A 1 190 ? -52.365 8.310 101.476 1.00 62.88 ? 190 ASP A OD2 1 ATOM 1434 N N . GLN A 1 191 ? -49.495 12.184 104.111 1.00 47.87 ? 191 GLN A N 1 ATOM 1435 C CA . GLN A 1 191 ? -48.494 13.249 104.124 1.00 46.81 ? 191 GLN A CA 1 ATOM 1436 C C . GLN A 1 191 ? -47.520 13.063 105.281 1.00 47.59 ? 191 GLN A C 1 ATOM 1437 O O . GLN A 1 191 ? -46.299 13.107 105.103 1.00 47.61 ? 191 GLN A O 1 ATOM 1438 C CB . GLN A 1 191 ? -49.179 14.625 104.201 1.00 46.11 ? 191 GLN A CB 1 ATOM 1439 C CG . GLN A 1 191 ? -48.253 15.829 104.354 1.00 45.16 ? 191 GLN A CG 1 ATOM 1440 C CD . GLN A 1 191 ? -47.393 16.104 103.123 1.00 45.11 ? 191 GLN A CD 1 ATOM 1441 O OE1 . GLN A 1 191 ? -47.829 15.917 101.992 1.00 44.08 ? 191 GLN A OE1 1 ATOM 1442 N NE2 . GLN A 1 191 ? -46.173 16.578 103.349 1.00 44.75 ? 191 GLN A NE2 1 ATOM 1443 N N . ILE A 1 192 ? -48.068 12.841 106.473 1.00 48.57 ? 192 ILE A N 1 ATOM 1444 C CA . ILE A 1 192 ? -47.254 12.662 107.675 1.00 48.27 ? 192 ILE A CA 1 ATOM 1445 C C . ILE A 1 192 ? -46.500 11.333 107.662 1.00 48.25 ? 192 ILE A C 1 ATOM 1446 O O . ILE A 1 192 ? -45.316 11.280 107.990 1.00 46.27 ? 192 ILE A O 1 ATOM 1447 C CB . ILE A 1 192 ? -48.127 12.765 108.931 1.00 49.86 ? 192 ILE A CB 1 ATOM 1448 C CG1 . ILE A 1 192 ? -48.740 14.171 109.019 1.00 50.18 ? 192 ILE A CG1 1 ATOM 1449 C CG2 . ILE A 1 192 ? -47.308 12.453 110.184 1.00 50.50 ? 192 ILE A CG2 1 ATOM 1450 C CD1 . ILE A 1 192 ? -47.719 15.287 109.141 1.00 49.94 ? 192 ILE A CD1 1 ATOM 1451 N N . PHE A 1 193 ? -47.176 10.267 107.249 1.00 49.85 ? 193 PHE A N 1 ATOM 1452 C CA . PHE A 1 193 ? -46.545 8.957 107.150 1.00 50.30 ? 193 PHE A CA 1 ATOM 1453 C C . PHE A 1 193 ? -45.332 8.999 106.217 1.00 49.64 ? 193 PHE A C 1 ATOM 1454 O O . PHE A 1 193 ? -44.323 8.349 106.490 1.00 48.46 ? 193 PHE A O 1 ATOM 1455 C CB . PHE A 1 193 ? -47.555 7.908 106.663 1.00 52.29 ? 193 PHE A CB 1 ATOM 1456 C CG . PHE A 1 193 ? -46.985 6.513 106.557 1.00 55.06 ? 193 PHE A CG 1 ATOM 1457 C CD1 . PHE A 1 193 ? -46.877 5.704 107.682 1.00 58.66 ? 193 PHE A CD1 1 ATOM 1458 C CD2 . PHE A 1 193 ? -46.560 6.004 105.334 1.00 56.63 ? 193 PHE A CD2 1 ATOM 1459 C CE1 . PHE A 1 193 ? -46.346 4.419 107.590 1.00 59.77 ? 193 PHE A CE1 1 ATOM 1460 C CE2 . PHE A 1 193 ? -46.036 4.720 105.235 1.00 57.14 ? 193 PHE A CE2 1 ATOM 1461 C CZ . PHE A 1 193 ? -45.927 3.929 106.364 1.00 58.79 ? 193 PHE A CZ 1 ATOM 1462 N N . LEU A 1 194 ? -45.429 9.764 105.118 1.00 47.24 ? 194 LEU A N 1 ATOM 1463 C CA . LEU A 1 194 ? -44.342 9.805 104.137 1.00 46.11 ? 194 LEU A CA 1 ATOM 1464 C C . LEU A 1 194 ? -43.259 10.850 104.428 1.00 44.16 ? 194 LEU A C 1 ATOM 1465 O O . LEU A 1 194 ? -42.078 10.564 104.269 1.00 45.98 ? 194 LEU A O 1 ATOM 1466 C CB . LEU A 1 194 ? -44.903 10.026 102.721 1.00 44.74 ? 194 LEU A CB 1 ATOM 1467 C CG . LEU A 1 194 ? -45.711 8.884 102.104 1.00 45.57 ? 194 LEU A CG 1 ATOM 1468 C CD1 . LEU A 1 194 ? -46.486 9.389 100.884 1.00 44.36 ? 194 LEU A CD1 1 ATOM 1469 C CD2 . LEU A 1 194 ? -44.808 7.714 101.729 1.00 45.88 ? 194 LEU A CD2 1 ATOM 1470 N N . TYR A 1 195 ? -43.653 12.060 104.829 1.00 44.44 ? 195 TYR A N 1 ATOM 1471 C CA . TYR A 1 195 ? -42.708 13.183 104.944 1.00 44.87 ? 195 TYR A CA 1 ATOM 1472 C C . TYR A 1 195 ? -42.520 13.729 106.369 1.00 47.65 ? 195 TYR A C 1 ATOM 1473 O O . TYR A 1 195 ? -41.659 14.586 106.603 1.00 47.66 ? 195 TYR A O 1 ATOM 1474 C CB . TYR A 1 195 ? -43.135 14.291 103.978 1.00 44.94 ? 195 TYR A CB 1 ATOM 1475 C CG . TYR A 1 195 ? -43.455 13.723 102.599 1.00 42.38 ? 195 TYR A CG 1 ATOM 1476 C CD1 . TYR A 1 195 ? -42.479 13.070 101.860 1.00 42.44 ? 195 TYR A CD1 1 ATOM 1477 C CD2 . TYR A 1 195 ? -44.741 13.782 102.075 1.00 43.42 ? 195 TYR A CD2 1 ATOM 1478 C CE1 . TYR A 1 195 ? -42.759 12.518 100.630 1.00 42.00 ? 195 TYR A CE1 1 ATOM 1479 C CE2 . TYR A 1 195 ? -45.040 13.232 100.839 1.00 41.86 ? 195 TYR A CE2 1 ATOM 1480 C CZ . TYR A 1 195 ? -44.039 12.602 100.123 1.00 41.77 ? 195 TYR A CZ 1 ATOM 1481 O OH . TYR A 1 195 ? -44.326 12.056 98.908 1.00 43.24 ? 195 TYR A OH 1 ATOM 1482 N N . ALA A 1 196 ? -43.323 13.230 107.310 1.00 49.72 ? 196 ALA A N 1 ATOM 1483 C CA . ALA A 1 196 ? -43.163 13.539 108.741 1.00 52.75 ? 196 ALA A CA 1 ATOM 1484 C C . ALA A 1 196 ? -43.543 14.977 109.090 1.00 55.10 ? 196 ALA A C 1 ATOM 1485 O O . ALA A 1 196 ? -43.233 15.444 110.183 1.00 59.12 ? 196 ALA A O 1 ATOM 1486 C CB . ALA A 1 196 ? -41.743 13.236 109.199 1.00 52.27 ? 196 ALA A CB 1 ATOM 1487 N N . GLN A 1 197 ? -44.240 15.664 108.189 1.00 55.28 ? 197 GLN A N 1 ATOM 1488 C CA . GLN A 1 197 ? -44.582 17.075 108.396 1.00 56.97 ? 197 GLN A CA 1 ATOM 1489 C C . GLN A 1 197 ? -45.554 17.590 107.335 1.00 55.68 ? 197 GLN A C 1 ATOM 1490 O O . GLN A 1 197 ? -45.768 16.931 106.315 1.00 54.36 ? 197 GLN A O 1 ATOM 1491 C CB . GLN A 1 197 ? -43.315 17.944 108.413 1.00 58.41 ? 197 GLN A CB 1 ATOM 1492 C CG . GLN A 1 197 ? -42.456 17.846 107.151 1.00 58.45 ? 197 GLN A CG 1 ATOM 1493 C CD . GLN A 1 197 ? -40.989 18.178 107.399 1.00 59.58 ? 197 GLN A CD 1 ATOM 1494 O OE1 . GLN A 1 197 ? -40.555 18.376 108.538 1.00 61.56 ? 197 GLN A OE1 1 ATOM 1495 N NE2 . GLN A 1 197 ? -40.219 18.239 106.328 1.00 59.78 ? 197 GLN A NE2 1 ATOM 1496 N N . ALA A 1 198 ? -46.126 18.767 107.594 1.00 54.34 ? 198 ALA A N 1 ATOM 1497 C CA . ALA A 1 198 ? -47.078 19.413 106.689 1.00 55.88 ? 198 ALA A CA 1 ATOM 1498 C C . ALA A 1 198 ? -46.416 19.777 105.351 1.00 54.58 ? 198 ALA A C 1 ATOM 1499 O O . ALA A 1 198 ? -45.217 20.073 105.300 1.00 54.68 ? 198 ALA A O 1 ATOM 1500 C CB . ALA A 1 198 ? -47.663 20.663 107.346 1.00 56.53 ? 198 ALA A CB 1 ATOM 1501 N N . SER A 1 199 ? -47.198 19.745 104.276 1.00 54.37 ? 199 SER A N 1 ATOM 1502 C CA . SER A 1 199 ? -46.658 19.947 102.928 1.00 53.14 ? 199 SER A CA 1 ATOM 1503 C C . SER A 1 199 ? -46.223 21.395 102.709 1.00 54.27 ? 199 SER A C 1 ATOM 1504 O O . SER A 1 199 ? -46.837 22.325 103.223 1.00 55.16 ? 199 SER A O 1 ATOM 1505 C CB . SER A 1 199 ? -47.671 19.523 101.857 1.00 50.66 ? 199 SER A CB 1 ATOM 1506 O OG . SER A 1 199 ? -48.795 20.369 101.836 1.00 49.55 ? 199 SER A OG 1 ATOM 1507 N N . GLY A 1 200 ? -45.141 21.565 101.960 1.00 55.26 ? 200 GLY A N 1 ATOM 1508 C CA . GLY A 1 200 ? -44.635 22.884 101.601 1.00 54.64 ? 200 GLY A CA 1 ATOM 1509 C C . GLY A 1 200 ? -44.164 22.888 100.157 1.00 52.86 ? 200 GLY A C 1 ATOM 1510 O O . GLY A 1 200 ? -43.893 21.836 99.576 1.00 53.07 ? 200 GLY A O 1 ATOM 1511 N N . ARG A 1 201 ? -44.027 24.079 99.595 1.00 50.46 ? 201 ARG A N 1 ATOM 1512 C CA . ARG A 1 201 ? -43.700 24.219 98.183 1.00 49.59 ? 201 ARG A CA 1 ATOM 1513 C C . ARG A 1 201 ? -42.359 23.575 97.821 1.00 46.38 ? 201 ARG A C 1 ATOM 1514 O O . ARG A 1 201 ? -41.488 23.362 98.680 1.00 45.24 ? 201 ARG A O 1 ATOM 1515 C CB . ARG A 1 201 ? -43.710 25.695 97.787 1.00 50.94 ? 201 ARG A CB 1 ATOM 1516 C CG . ARG A 1 201 ? -42.569 26.495 98.379 1.00 52.06 ? 201 ARG A CG 1 ATOM 1517 C CD . ARG A 1 201 ? -42.912 27.970 98.516 1.00 53.86 ? 201 ARG A CD 1 ATOM 1518 N NE . ARG A 1 201 ? -41.782 28.686 99.114 1.00 54.17 ? 201 ARG A NE 1 ATOM 1519 C CZ . ARG A 1 201 ? -41.620 28.919 100.419 1.00 56.60 ? 201 ARG A CZ 1 ATOM 1520 N NH1 . ARG A 1 201 ? -42.529 28.519 101.314 1.00 56.30 ? 201 ARG A NH1 1 ATOM 1521 N NH2 . ARG A 1 201 ? -40.538 29.574 100.833 1.00 56.34 ? 201 ARG A NH2 1 ATOM 1522 N N . ILE A 1 202 ? -42.227 23.239 96.538 1.00 43.30 ? 202 ILE A N 1 ATOM 1523 C CA . ILE A 1 202 ? -40.973 22.748 95.975 1.00 42.35 ? 202 ILE A CA 1 ATOM 1524 C C . ILE A 1 202 ? -40.504 23.778 94.957 1.00 40.90 ? 202 ILE A C 1 ATOM 1525 O O . ILE A 1 202 ? -41.302 24.220 94.123 1.00 41.14 ? 202 ILE A O 1 ATOM 1526 C CB . ILE A 1 202 ? -41.172 21.387 95.280 1.00 41.19 ? 202 ILE A CB 1 ATOM 1527 C CG1 . ILE A 1 202 ? -41.469 20.302 96.319 1.00 42.52 ? 202 ILE A CG1 1 ATOM 1528 C CG2 . ILE A 1 202 ? -39.951 21.008 94.448 1.00 41.92 ? 202 ILE A CG2 1 ATOM 1529 C CD1 . ILE A 1 202 ? -41.950 19.003 95.706 1.00 41.00 ? 202 ILE A CD1 1 ATOM 1530 N N . THR A 1 203 ? -39.233 24.169 95.024 1.00 39.76 ? 203 THR A N 1 ATOM 1531 C CA . THR A 1 203 ? -38.687 25.123 94.055 1.00 40.29 ? 203 THR A CA 1 ATOM 1532 C C . THR A 1 203 ? -37.471 24.515 93.386 1.00 40.29 ? 203 THR A C 1 ATOM 1533 O O . THR A 1 203 ? -36.554 24.013 94.057 1.00 40.11 ? 203 THR A O 1 ATOM 1534 C CB . THR A 1 203 ? -38.355 26.494 94.694 1.00 42.74 ? 203 THR A CB 1 ATOM 1535 O OG1 . THR A 1 203 ? -39.542 27.042 95.290 1.00 42.53 ? 203 THR A OG1 1 ATOM 1536 C CG2 . THR A 1 203 ? -37.815 27.493 93.621 1.00 42.89 ? 203 THR A CG2 1 ATOM 1537 N N . VAL A 1 204 ? -37.508 24.503 92.053 1.00 38.06 ? 204 VAL A N 1 ATOM 1538 C CA . VAL A 1 204 ? -36.422 23.978 91.244 1.00 37.53 ? 204 VAL A CA 1 ATOM 1539 C C . VAL A 1 204 ? -35.952 25.116 90.359 1.00 37.32 ? 204 VAL A C 1 ATOM 1540 O O . VAL A 1 204 ? -36.749 25.684 89.621 1.00 34.72 ? 204 VAL A O 1 ATOM 1541 C CB . VAL A 1 204 ? -36.878 22.792 90.374 1.00 36.88 ? 204 VAL A CB 1 ATOM 1542 C CG1 . VAL A 1 204 ? -35.784 22.378 89.404 1.00 35.58 ? 204 VAL A CG1 1 ATOM 1543 C CG2 . VAL A 1 204 ? -37.283 21.620 91.260 1.00 36.57 ? 204 VAL A CG2 1 ATOM 1544 N N . SER A 1 205 ? -34.667 25.460 90.453 1.00 38.76 ? 205 SER A N 1 ATOM 1545 C CA . SER A 1 205 ? -34.184 26.663 89.791 1.00 39.00 ? 205 SER A CA 1 ATOM 1546 C C . SER A 1 205 ? -32.830 26.483 89.125 1.00 39.63 ? 205 SER A C 1 ATOM 1547 O O . SER A 1 205 ? -32.085 25.533 89.392 1.00 39.34 ? 205 SER A O 1 ATOM 1548 C CB . SER A 1 205 ? -34.125 27.827 90.793 1.00 39.62 ? 205 SER A CB 1 ATOM 1549 O OG . SER A 1 205 ? -33.235 27.535 91.860 1.00 41.53 ? 205 SER A OG 1 ATOM 1550 N N . THR A 1 206 ? -32.565 27.408 88.212 1.00 39.03 ? 206 THR A N 1 ATOM 1551 C CA . THR A 1 206 ? -31.275 27.566 87.563 1.00 38.73 ? 206 THR A CA 1 ATOM 1552 C C . THR A 1 206 ? -30.958 29.065 87.604 1.00 38.43 ? 206 THR A C 1 ATOM 1553 O O . THR A 1 206 ? -31.731 29.856 88.140 1.00 36.97 ? 206 THR A O 1 ATOM 1554 C CB . THR A 1 206 ? -31.330 27.084 86.104 1.00 38.34 ? 206 THR A CB 1 ATOM 1555 O OG1 . THR A 1 206 ? -32.243 27.905 85.351 1.00 38.69 ? 206 THR A OG1 1 ATOM 1556 C CG2 . THR A 1 206 ? -31.805 25.627 86.020 1.00 37.88 ? 206 THR A CG2 1 ATOM 1557 N N . LYS A 1 207 ? -29.835 29.454 87.028 1.00 40.37 ? 207 LYS A N 1 ATOM 1558 C CA . LYS A 1 207 ? -29.527 30.870 86.845 1.00 42.55 ? 207 LYS A CA 1 ATOM 1559 C C . LYS A 1 207 ? -30.551 31.595 85.954 1.00 43.69 ? 207 LYS A C 1 ATOM 1560 O O . LYS A 1 207 ? -30.763 32.791 86.133 1.00 45.84 ? 207 LYS A O 1 ATOM 1561 C CB . LYS A 1 207 ? -28.142 31.041 86.239 1.00 43.91 ? 207 LYS A CB 1 ATOM 1562 C CG . LYS A 1 207 ? -27.002 30.621 87.143 1.00 45.16 ? 207 LYS A CG 1 ATOM 1563 C CD . LYS A 1 207 ? -25.681 31.021 86.507 1.00 47.28 ? 207 LYS A CD 1 ATOM 1564 C CE . LYS A 1 207 ? -24.578 30.017 86.778 1.00 48.60 ? 207 LYS A CE 1 ATOM 1565 N NZ . LYS A 1 207 ? -23.389 30.334 85.937 1.00 49.70 ? 207 LYS A NZ 1 ATOM 1566 N N . ARG A 1 208 ? -31.212 30.873 85.044 1.00 44.12 ? 208 ARG A N 1 ATOM 1567 C CA A ARG A 1 208 ? -32.123 31.481 84.066 0.50 44.45 ? 208 ARG A CA 1 ATOM 1568 C CA B ARG A 1 208 ? -32.125 31.518 84.104 0.50 44.71 ? 208 ARG A CA 1 ATOM 1569 C C . ARG A 1 208 ? -33.603 31.172 84.301 1.00 44.25 ? 208 ARG A C 1 ATOM 1570 O O . ARG A 1 208 ? -34.462 31.696 83.579 1.00 45.00 ? 208 ARG A O 1 ATOM 1571 C CB A ARG A 1 208 ? -31.753 31.042 82.640 0.50 45.55 ? 208 ARG A CB 1 ATOM 1572 C CB B ARG A 1 208 ? -31.692 31.223 82.668 0.50 46.09 ? 208 ARG A CB 1 ATOM 1573 C CG A ARG A 1 208 ? -32.224 29.639 82.263 0.50 45.97 ? 208 ARG A CG 1 ATOM 1574 C CG B ARG A 1 208 ? -31.606 29.750 82.305 0.50 47.08 ? 208 ARG A CG 1 ATOM 1575 C CD A ARG A 1 208 ? -32.225 29.397 80.758 0.50 47.17 ? 208 ARG A CD 1 ATOM 1576 C CD B ARG A 1 208 ? -31.291 29.618 80.829 0.50 48.42 ? 208 ARG A CD 1 ATOM 1577 N NE A ARG A 1 208 ? -33.136 30.284 80.030 0.50 47.23 ? 208 ARG A NE 1 ATOM 1578 N NE B ARG A 1 208 ? -32.175 30.482 80.060 0.50 50.15 ? 208 ARG A NE 1 ATOM 1579 C CZ A ARG A 1 208 ? -34.451 30.120 79.960 0.50 46.11 ? 208 ARG A CZ 1 ATOM 1580 C CZ B ARG A 1 208 ? -31.980 30.821 78.793 0.50 49.66 ? 208 ARG A CZ 1 ATOM 1581 N NH1 A ARG A 1 208 ? -35.028 29.099 80.572 0.50 45.32 ? 208 ARG A NH1 1 ATOM 1582 N NH1 B ARG A 1 208 ? -30.920 30.373 78.140 0.50 49.11 ? 208 ARG A NH1 1 ATOM 1583 N NH2 A ARG A 1 208 ? -35.186 30.981 79.274 0.50 46.44 ? 208 ARG A NH2 1 ATOM 1584 N NH2 B ARG A 1 208 ? -32.850 31.616 78.195 0.50 50.18 ? 208 ARG A NH2 1 ATOM 1585 N N . SER A 1 209 ? -33.920 30.315 85.271 1.00 41.55 ? 209 SER A N 1 ATOM 1586 C CA . SER A 1 209 ? -35.309 29.864 85.421 1.00 41.22 ? 209 SER A CA 1 ATOM 1587 C C . SER A 1 209 ? -35.658 29.433 86.829 1.00 40.40 ? 209 SER A C 1 ATOM 1588 O O . SER A 1 209 ? -34.787 29.095 87.611 1.00 40.05 ? 209 SER A O 1 ATOM 1589 C CB . SER A 1 209 ? -35.581 28.679 84.471 1.00 41.39 ? 209 SER A CB 1 ATOM 1590 O OG . SER A 1 209 ? -34.880 27.525 84.929 1.00 42.08 ? 209 SER A OG 1 ATOM 1591 N N . GLN A 1 210 ? -36.948 29.441 87.141 1.00 39.09 ? 210 GLN A N 1 ATOM 1592 C CA . GLN A 1 210 ? -37.426 28.971 88.438 1.00 40.21 ? 210 GLN A CA 1 ATOM 1593 C C . GLN A 1 210 ? -38.840 28.448 88.283 1.00 40.28 ? 210 GLN A C 1 ATOM 1594 O O . GLN A 1 210 ? -39.656 29.034 87.555 1.00 39.71 ? 210 GLN A O 1 ATOM 1595 C CB . GLN A 1 210 ? -37.393 30.073 89.493 1.00 41.94 ? 210 GLN A CB 1 ATOM 1596 C CG . GLN A 1 210 ? -38.008 31.389 89.061 1.00 42.95 ? 210 GLN A CG 1 ATOM 1597 C CD . GLN A 1 210 ? -38.085 32.411 90.177 1.00 46.10 ? 210 GLN A CD 1 ATOM 1598 O OE1 . GLN A 1 210 ? -37.768 32.114 91.324 1.00 48.20 ? 210 GLN A OE1 1 ATOM 1599 N NE2 . GLN A 1 210 ? -38.551 33.615 89.850 1.00 45.68 ? 210 GLN A NE2 1 ATOM 1600 N N . GLN A 1 211 ? -39.105 27.322 88.931 1.00 39.06 ? 211 GLN A N 1 ATOM 1601 C CA . GLN A 1 211 ? -40.416 26.712 88.928 1.00 38.07 ? 211 GLN A CA 1 ATOM 1602 C C . GLN A 1 211 ? -40.746 26.334 90.353 1.00 37.95 ? 211 GLN A C 1 ATOM 1603 O O . GLN A 1 211 ? -40.057 25.508 90.962 1.00 37.12 ? 211 GLN A O 1 ATOM 1604 C CB . GLN A 1 211 ? -40.418 25.441 88.072 1.00 38.92 ? 211 GLN A CB 1 ATOM 1605 C CG . GLN A 1 211 ? -40.028 25.614 86.605 1.00 39.45 ? 211 GLN A CG 1 ATOM 1606 C CD . GLN A 1 211 ? -39.602 24.297 85.967 1.00 39.82 ? 211 GLN A CD 1 ATOM 1607 O OE1 . GLN A 1 211 ? -40.430 23.556 85.441 1.00 42.28 ? 211 GLN A OE1 1 ATOM 1608 N NE2 . GLN A 1 211 ? -38.304 24.009 86.001 1.00 39.33 ? 211 GLN A NE2 1 ATOM 1609 N N . THR A 1 212 ? -41.795 26.933 90.890 1.00 38.67 ? 212 THR A N 1 ATOM 1610 C CA . THR A 1 212 ? -42.251 26.605 92.228 1.00 39.36 ? 212 THR A CA 1 ATOM 1611 C C . THR A 1 212 ? -43.605 25.893 92.112 1.00 40.73 ? 212 THR A C 1 ATOM 1612 O O . THR A 1 212 ? -44.494 26.330 91.381 1.00 39.38 ? 212 THR A O 1 ATOM 1613 C CB . THR A 1 212 ? -42.366 27.859 93.099 1.00 39.57 ? 212 THR A CB 1 ATOM 1614 O OG1 . THR A 1 212 ? -41.065 28.446 93.259 1.00 39.62 ? 212 THR A OG1 1 ATOM 1615 C CG2 . THR A 1 212 ? -42.919 27.483 94.456 1.00 40.11 ? 212 THR A CG2 1 ATOM 1616 N N . VAL A 1 213 ? -43.734 24.776 92.811 1.00 41.15 ? 213 VAL A N 1 ATOM 1617 C CA . VAL A 1 213 ? -44.919 23.950 92.726 1.00 40.77 ? 213 VAL A CA 1 ATOM 1618 C C . VAL A 1 213 ? -45.413 23.615 94.132 1.00 40.83 ? 213 VAL A C 1 ATOM 1619 O O . VAL A 1 213 ? -44.626 23.240 94.983 1.00 40.19 ? 213 VAL A O 1 ATOM 1620 C CB . VAL A 1 213 ? -44.623 22.633 91.998 1.00 40.93 ? 213 VAL A CB 1 ATOM 1621 C CG1 . VAL A 1 213 ? -45.865 21.759 91.991 1.00 40.95 ? 213 VAL A CG1 1 ATOM 1622 C CG2 . VAL A 1 213 ? -44.131 22.898 90.579 1.00 40.88 ? 213 VAL A CG2 1 ATOM 1623 N N . ILE A 1 214 ? -46.723 23.730 94.346 1.00 42.80 ? 214 ILE A N 1 ATOM 1624 C CA . ILE A 1 214 ? -47.344 23.503 95.662 1.00 44.49 ? 214 ILE A CA 1 ATOM 1625 C C . ILE A 1 214 ? -48.003 22.133 95.686 1.00 44.29 ? 214 ILE A C 1 ATOM 1626 O O . ILE A 1 214 ? -48.951 21.894 94.935 1.00 43.02 ? 214 ILE A O 1 ATOM 1627 C CB . ILE A 1 214 ? -48.448 24.541 95.983 1.00 47.00 ? 214 ILE A CB 1 ATOM 1628 C CG1 . ILE A 1 214 ? -47.905 25.969 95.876 1.00 48.19 ? 214 ILE A CG1 1 ATOM 1629 C CG2 . ILE A 1 214 ? -49.019 24.308 97.387 1.00 46.61 ? 214 ILE A CG2 1 ATOM 1630 C CD1 . ILE A 1 214 ? -46.916 26.302 96.973 1.00 51.63 ? 214 ILE A CD1 1 ATOM 1631 N N . PRO A 1 215 ? -47.517 21.229 96.553 1.00 44.30 ? 215 PRO A N 1 ATOM 1632 C CA . PRO A 1 215 ? -48.235 19.960 96.700 1.00 44.68 ? 215 PRO A CA 1 ATOM 1633 C C . PRO A 1 215 ? -49.606 20.214 97.315 1.00 44.45 ? 215 PRO A C 1 ATOM 1634 O O . PRO A 1 215 ? -49.720 21.044 98.212 1.00 45.05 ? 215 PRO A O 1 ATOM 1635 C CB . PRO A 1 215 ? -47.347 19.143 97.642 1.00 46.10 ? 215 PRO A CB 1 ATOM 1636 C CG . PRO A 1 215 ? -46.041 19.867 97.688 1.00 46.06 ? 215 PRO A CG 1 ATOM 1637 C CD . PRO A 1 215 ? -46.350 21.309 97.432 1.00 44.86 ? 215 PRO A CD 1 ATOM 1638 N N . ASN A 1 216 ? -50.628 19.535 96.794 1.00 43.91 ? 216 ASN A N 1 ATOM 1639 C CA . ASN A 1 216 ? -52.005 19.713 97.229 1.00 43.99 ? 216 ASN A CA 1 ATOM 1640 C C . ASN A 1 216 ? -52.603 18.386 97.678 1.00 43.76 ? 216 ASN A C 1 ATOM 1641 O O . ASN A 1 216 ? -52.907 17.520 96.859 1.00 42.54 ? 216 ASN A O 1 ATOM 1642 C CB . ASN A 1 216 ? -52.854 20.307 96.108 1.00 44.20 ? 216 ASN A CB 1 ATOM 1643 C CG . ASN A 1 216 ? -52.381 21.683 95.682 1.00 45.32 ? 216 ASN A CG 1 ATOM 1644 O OD1 . ASN A 1 216 ? -52.229 22.583 96.513 1.00 47.12 ? 216 ASN A OD1 1 ATOM 1645 N ND2 . ASN A 1 216 ? -52.169 21.862 94.377 1.00 45.75 ? 216 ASN A ND2 1 ATOM 1646 N N . ILE A 1 217 ? -52.780 18.253 98.993 1.00 44.73 ? 217 ILE A N 1 ATOM 1647 C CA . ILE A 1 217 ? -53.349 17.053 99.608 1.00 44.56 ? 217 ILE A CA 1 ATOM 1648 C C . ILE A 1 217 ? -54.834 16.937 99.285 1.00 45.26 ? 217 ILE A C 1 ATOM 1649 O O . ILE A 1 217 ? -55.570 17.929 99.309 1.00 44.99 ? 217 ILE A O 1 ATOM 1650 C CB . ILE A 1 217 ? -53.133 17.071 101.149 1.00 45.80 ? 217 ILE A CB 1 ATOM 1651 C CG1 . ILE A 1 217 ? -51.623 17.021 101.458 1.00 45.47 ? 217 ILE A CG1 1 ATOM 1652 C CG2 . ILE A 1 217 ? -53.850 15.895 101.819 1.00 45.23 ? 217 ILE A CG2 1 ATOM 1653 C CD1 . ILE A 1 217 ? -51.236 17.596 102.808 1.00 47.92 ? 217 ILE A CD1 1 ATOM 1654 N N . GLY A 1 218 ? -55.277 15.724 98.969 1.00 45.79 ? 218 GLY A N 1 ATOM 1655 C CA . GLY A 1 218 ? -56.700 15.479 98.750 1.00 45.70 ? 218 GLY A CA 1 ATOM 1656 C C . GLY A 1 218 ? -56.935 14.228 97.943 1.00 46.10 ? 218 GLY A C 1 ATOM 1657 O O . GLY A 1 218 ? -56.063 13.797 97.186 1.00 44.92 ? 218 GLY A O 1 ATOM 1658 N N . SER A 1 219 ? -58.111 13.633 98.107 1.00 45.28 ? 219 SER A N 1 ATOM 1659 C CA . SER A 1 219 ? -58.470 12.467 97.314 1.00 46.52 ? 219 SER A CA 1 ATOM 1660 C C . SER A 1 219 ? -58.847 12.891 95.896 1.00 45.76 ? 219 SER A C 1 ATOM 1661 O O . SER A 1 219 ? -59.628 13.827 95.703 1.00 47.74 ? 219 SER A O 1 ATOM 1662 C CB . SER A 1 219 ? -59.643 11.710 97.940 1.00 48.25 ? 219 SER A CB 1 ATOM 1663 O OG . SER A 1 219 ? -59.347 11.319 99.262 1.00 49.25 ? 219 SER A OG 1 ATOM 1664 N N . ARG A 1 220 ? -58.272 12.207 94.913 1.00 43.27 ? 220 ARG A N 1 ATOM 1665 C CA . ARG A 1 220 ? -58.797 12.222 93.545 1.00 44.58 ? 220 ARG A CA 1 ATOM 1666 C C . ARG A 1 220 ? -59.441 10.856 93.302 1.00 44.24 ? 220 ARG A C 1 ATOM 1667 O O . ARG A 1 220 ? -59.187 9.907 94.067 1.00 44.48 ? 220 ARG A O 1 ATOM 1668 C CB . ARG A 1 220 ? -57.689 12.467 92.525 1.00 43.80 ? 220 ARG A CB 1 ATOM 1669 C CG . ARG A 1 220 ? -57.144 13.885 92.510 1.00 43.51 ? 220 ARG A CG 1 ATOM 1670 C CD . ARG A 1 220 ? -56.093 14.089 93.577 1.00 44.49 ? 220 ARG A CD 1 ATOM 1671 N NE . ARG A 1 220 ? -55.318 15.315 93.372 1.00 45.25 ? 220 ARG A NE 1 ATOM 1672 C CZ . ARG A 1 220 ? -54.655 15.963 94.329 1.00 45.86 ? 220 ARG A CZ 1 ATOM 1673 N NH1 . ARG A 1 220 ? -54.670 15.529 95.584 1.00 45.33 ? 220 ARG A NH1 1 ATOM 1674 N NH2 . ARG A 1 220 ? -53.988 17.076 94.031 1.00 46.52 ? 220 ARG A NH2 1 ATOM 1675 N N . PRO A 1 221 ? -60.281 10.747 92.267 1.00 43.94 ? 221 PRO A N 1 ATOM 1676 C CA . PRO A 1 221 ? -60.851 9.434 91.968 1.00 44.38 ? 221 PRO A CA 1 ATOM 1677 C C . PRO A 1 221 ? -59.754 8.379 91.813 1.00 44.86 ? 221 PRO A C 1 ATOM 1678 O O . PRO A 1 221 ? -58.723 8.618 91.175 1.00 44.82 ? 221 PRO A O 1 ATOM 1679 C CB . PRO A 1 221 ? -61.619 9.687 90.667 1.00 43.70 ? 221 PRO A CB 1 ATOM 1680 C CG . PRO A 1 221 ? -62.067 11.101 90.814 1.00 42.81 ? 221 PRO A CG 1 ATOM 1681 C CD . PRO A 1 221 ? -60.852 11.783 91.385 1.00 42.99 ? 221 PRO A CD 1 ATOM 1682 N N . ARG A 1 222 ? -59.936 7.231 92.446 1.00 44.25 ? 222 ARG A N 1 ATOM 1683 C CA . ARG A 1 222 ? -58.892 6.233 92.421 1.00 44.38 ? 222 ARG A CA 1 ATOM 1684 C C . ARG A 1 222 ? -58.586 5.767 91.015 1.00 42.27 ? 222 ARG A C 1 ATOM 1685 O O . ARG A 1 222 ? -59.474 5.547 90.212 1.00 42.95 ? 222 ARG A O 1 ATOM 1686 C CB . ARG A 1 222 ? -59.237 5.049 93.312 1.00 46.01 ? 222 ARG A CB 1 ATOM 1687 C CG . ARG A 1 222 ? -59.231 5.433 94.761 1.00 47.12 ? 222 ARG A CG 1 ATOM 1688 C CD . ARG A 1 222 ? -59.510 4.220 95.617 1.00 49.51 ? 222 ARG A CD 1 ATOM 1689 N NE . ARG A 1 222 ? -59.395 4.542 97.026 1.00 50.22 ? 222 ARG A NE 1 ATOM 1690 C CZ . ARG A 1 222 ? -59.160 3.647 97.979 1.00 52.40 ? 222 ARG A CZ 1 ATOM 1691 N NH1 . ARG A 1 222 ? -58.996 2.359 97.681 1.00 53.00 ? 222 ARG A NH1 1 ATOM 1692 N NH2 . ARG A 1 222 ? -59.071 4.048 99.232 1.00 51.66 ? 222 ARG A NH2 1 ATOM 1693 N N . VAL A 1 223 ? -57.291 5.679 90.725 1.00 42.68 ? 223 VAL A N 1 ATOM 1694 C CA . VAL A 1 223 ? -56.798 5.138 89.471 1.00 42.06 ? 223 VAL A CA 1 ATOM 1695 C C . VAL A 1 223 ? -55.881 3.996 89.889 1.00 42.30 ? 223 VAL A C 1 ATOM 1696 O O . VAL A 1 223 ? -54.912 4.214 90.618 1.00 40.84 ? 223 VAL A O 1 ATOM 1697 C CB . VAL A 1 223 ? -55.992 6.182 88.669 1.00 41.78 ? 223 VAL A CB 1 ATOM 1698 C CG1 . VAL A 1 223 ? -55.318 5.530 87.458 1.00 41.37 ? 223 VAL A CG1 1 ATOM 1699 C CG2 . VAL A 1 223 ? -56.891 7.334 88.222 1.00 40.68 ? 223 VAL A CG2 1 ATOM 1700 N N . ARG A 1 224 ? -56.197 2.792 89.425 1.00 44.70 ? 224 ARG A N 1 ATOM 1701 C CA . ARG A 1 224 ? -55.497 1.588 89.845 1.00 47.18 ? 224 ARG A CA 1 ATOM 1702 C C . ARG A 1 224 ? -55.412 1.588 91.368 1.00 46.24 ? 224 ARG A C 1 ATOM 1703 O O . ARG A 1 224 ? -54.361 1.362 91.958 1.00 47.77 ? 224 ARG A O 1 ATOM 1704 C CB . ARG A 1 224 ? -54.131 1.495 89.144 1.00 48.10 ? 224 ARG A CB 1 ATOM 1705 C CG . ARG A 1 224 ? -54.277 1.482 87.616 1.00 48.05 ? 224 ARG A CG 1 ATOM 1706 C CD . ARG A 1 224 ? -52.947 1.317 86.881 1.00 48.73 ? 224 ARG A CD 1 ATOM 1707 N NE . ARG A 1 224 ? -52.113 2.519 86.943 1.00 47.41 ? 224 ARG A NE 1 ATOM 1708 C CZ . ARG A 1 224 ? -52.330 3.643 86.252 1.00 45.97 ? 224 ARG A CZ 1 ATOM 1709 N NH1 . ARG A 1 224 ? -53.368 3.762 85.439 1.00 46.15 ? 224 ARG A NH1 1 ATOM 1710 N NH2 . ARG A 1 224 ? -51.505 4.673 86.393 1.00 46.05 ? 224 ARG A NH2 1 ATOM 1711 N N . ASN A 1 225 ? -56.560 1.894 91.976 1.00 47.12 ? 225 ASN A N 1 ATOM 1712 C CA . ASN A 1 225 ? -56.756 1.950 93.428 1.00 47.25 ? 225 ASN A CA 1 ATOM 1713 C C . ASN A 1 225 ? -55.931 3.009 94.177 1.00 46.19 ? 225 ASN A C 1 ATOM 1714 O O . ASN A 1 225 ? -55.774 2.928 95.396 1.00 46.30 ? 225 ASN A O 1 ATOM 1715 C CB . ASN A 1 225 ? -56.547 0.554 94.048 1.00 50.03 ? 225 ASN A CB 1 ATOM 1716 C CG . ASN A 1 225 ? -57.315 0.370 95.358 1.00 53.25 ? 225 ASN A CG 1 ATOM 1717 O OD1 . ASN A 1 225 ? -58.437 0.855 95.504 1.00 55.37 ? 225 ASN A OD1 1 ATOM 1718 N ND2 . ASN A 1 225 ? -56.710 -0.329 96.317 1.00 54.98 ? 225 ASN A ND2 1 ATOM 1719 N N . ILE A 1 226 ? -55.436 4.026 93.465 1.00 42.84 ? 226 ILE A N 1 ATOM 1720 C CA . ILE A 1 226 ? -54.672 5.093 94.090 1.00 41.22 ? 226 ILE A CA 1 ATOM 1721 C C . ILE A 1 226 ? -55.390 6.436 93.963 1.00 40.68 ? 226 ILE A C 1 ATOM 1722 O O . ILE A 1 226 ? -55.637 6.917 92.846 1.00 38.97 ? 226 ILE A O 1 ATOM 1723 C CB . ILE A 1 226 ? -53.261 5.226 93.479 1.00 41.38 ? 226 ILE A CB 1 ATOM 1724 C CG1 . ILE A 1 226 ? -52.455 3.936 93.670 1.00 41.85 ? 226 ILE A CG1 1 ATOM 1725 C CG2 . ILE A 1 226 ? -52.533 6.419 94.076 1.00 39.95 ? 226 ILE A CG2 1 ATOM 1726 C CD1 . ILE A 1 226 ? -51.996 3.673 95.098 1.00 42.92 ? 226 ILE A CD1 1 ATOM 1727 N N . PRO A 1 227 ? -55.706 7.063 95.100 1.00 40.75 ? 227 PRO A N 1 ATOM 1728 C CA . PRO A 1 227 ? -56.323 8.385 95.089 1.00 41.20 ? 227 PRO A CA 1 ATOM 1729 C C . PRO A 1 227 ? -55.327 9.553 95.123 1.00 40.49 ? 227 PRO A C 1 ATOM 1730 O O . PRO A 1 227 ? -55.741 10.714 95.024 1.00 40.42 ? 227 PRO A O 1 ATOM 1731 C CB . PRO A 1 227 ? -57.154 8.378 96.385 1.00 42.05 ? 227 PRO A CB 1 ATOM 1732 C CG . PRO A 1 227 ? -56.385 7.528 97.306 1.00 42.36 ? 227 PRO A CG 1 ATOM 1733 C CD . PRO A 1 227 ? -55.771 6.446 96.447 1.00 42.82 ? 227 PRO A CD 1 ATOM 1734 N N . SER A 1 228 ? -54.045 9.256 95.297 1.00 39.98 ? 228 SER A N 1 ATOM 1735 C CA . SER A 1 228 ? -52.991 10.276 95.231 1.00 40.84 ? 228 SER A CA 1 ATOM 1736 C C . SER A 1 228 ? -52.645 10.569 93.764 1.00 39.01 ? 228 SER A C 1 ATOM 1737 O O . SER A 1 228 ? -53.096 9.858 92.865 1.00 38.29 ? 228 SER A O 1 ATOM 1738 C CB . SER A 1 228 ? -51.717 9.791 95.923 1.00 42.04 ? 228 SER A CB 1 ATOM 1739 O OG . SER A 1 228 ? -51.893 9.572 97.305 1.00 44.98 ? 228 SER A OG 1 ATOM 1740 N N . ARG A 1 229 ? -51.818 11.594 93.537 1.00 38.69 ? 229 ARG A N 1 ATOM 1741 C CA . ARG A 1 229 ? -51.281 11.885 92.188 1.00 36.77 ? 229 ARG A CA 1 ATOM 1742 C C . ARG A 1 229 ? -49.804 12.301 92.266 1.00 36.46 ? 229 ARG A C 1 ATOM 1743 O O . ARG A 1 229 ? -49.321 12.731 93.310 1.00 37.17 ? 229 ARG A O 1 ATOM 1744 C CB . ARG A 1 229 ? -52.093 12.986 91.496 1.00 36.14 ? 229 ARG A CB 1 ATOM 1745 C CG . ARG A 1 229 ? -53.532 12.617 91.115 1.00 37.14 ? 229 ARG A CG 1 ATOM 1746 C CD . ARG A 1 229 ? -53.650 11.476 90.101 1.00 36.73 ? 229 ARG A CD 1 ATOM 1747 N NE . ARG A 1 229 ? -55.061 11.294 89.711 1.00 38.07 ? 229 ARG A NE 1 ATOM 1748 C CZ . ARG A 1 229 ? -55.907 10.379 90.206 1.00 38.87 ? 229 ARG A CZ 1 ATOM 1749 N NH1 . ARG A 1 229 ? -55.522 9.496 91.132 1.00 40.09 ? 229 ARG A NH1 1 ATOM 1750 N NH2 . ARG A 1 229 ? -57.160 10.347 89.774 1.00 37.82 ? 229 ARG A NH2 1 ATOM 1751 N N . ILE A 1 230 ? -49.093 12.141 91.156 1.00 35.51 ? 230 ILE A N 1 ATOM 1752 C CA . ILE A 1 230 ? -47.786 12.768 90.952 1.00 35.13 ? 230 ILE A CA 1 ATOM 1753 C C . ILE A 1 230 ? -47.939 13.717 89.736 1.00 33.87 ? 230 ILE A C 1 ATOM 1754 O O . ILE A 1 230 ? -48.463 13.312 88.722 1.00 32.40 ? 230 ILE A O 1 ATOM 1755 C CB . ILE A 1 230 ? -46.692 11.719 90.669 1.00 36.15 ? 230 ILE A CB 1 ATOM 1756 C CG1 . ILE A 1 230 ? -46.365 10.936 91.957 1.00 37.13 ? 230 ILE A CG1 1 ATOM 1757 C CG2 . ILE A 1 230 ? -45.422 12.381 90.122 1.00 36.18 ? 230 ILE A CG2 1 ATOM 1758 C CD1 . ILE A 1 230 ? -45.468 9.739 91.754 1.00 37.68 ? 230 ILE A CD1 1 ATOM 1759 N N . SER A 1 231 ? -47.521 14.973 89.885 1.00 34.02 ? 231 SER A N 1 ATOM 1760 C CA . SER A 1 231 ? -47.468 15.917 88.776 1.00 33.71 ? 231 SER A CA 1 ATOM 1761 C C . SER A 1 231 ? -45.998 16.038 88.304 1.00 33.34 ? 231 SER A C 1 ATOM 1762 O O . SER A 1 231 ? -45.076 16.214 89.101 1.00 33.20 ? 231 SER A O 1 ATOM 1763 C CB . SER A 1 231 ? -48.074 17.265 89.189 1.00 34.35 ? 231 SER A CB 1 ATOM 1764 O OG . SER A 1 231 ? -49.484 17.143 89.371 1.00 35.51 ? 231 SER A OG 1 ATOM 1765 N N . ILE A 1 232 ? -45.807 15.911 86.998 1.00 32.60 ? 232 ILE A N 1 ATOM 1766 C CA . ILE A 1 232 ? -44.480 15.840 86.401 1.00 32.78 ? 232 ILE A CA 1 ATOM 1767 C C . ILE A 1 232 ? -44.094 17.180 85.784 1.00 33.18 ? 232 ILE A C 1 ATOM 1768 O O . ILE A 1 232 ? -44.911 17.813 85.087 1.00 32.29 ? 232 ILE A O 1 ATOM 1769 C CB . ILE A 1 232 ? -44.437 14.774 85.305 1.00 32.71 ? 232 ILE A CB 1 ATOM 1770 C CG1 . ILE A 1 232 ? -44.665 13.366 85.906 1.00 33.42 ? 232 ILE A CG1 1 ATOM 1771 C CG2 . ILE A 1 232 ? -43.119 14.844 84.528 1.00 32.54 ? 232 ILE A CG2 1 ATOM 1772 C CD1 . ILE A 1 232 ? -43.584 12.878 86.876 1.00 33.69 ? 232 ILE A CD1 1 ATOM 1773 N N . TYR A 1 233 ? -42.842 17.574 86.015 1.00 32.77 ? 233 TYR A N 1 ATOM 1774 C CA . TYR A 1 233 ? -42.295 18.840 85.524 1.00 33.49 ? 233 TYR A CA 1 ATOM 1775 C C . TYR A 1 233 ? -40.941 18.557 84.889 1.00 34.21 ? 233 TYR A C 1 ATOM 1776 O O . TYR A 1 233 ? -40.362 17.484 85.114 1.00 32.56 ? 233 TYR A O 1 ATOM 1777 C CB . TYR A 1 233 ? -42.158 19.834 86.671 1.00 33.63 ? 233 TYR A CB 1 ATOM 1778 C CG . TYR A 1 233 ? -43.510 20.196 87.237 1.00 34.65 ? 233 TYR A CG 1 ATOM 1779 C CD1 . TYR A 1 233 ? -44.107 19.423 88.239 1.00 34.95 ? 233 TYR A CD1 1 ATOM 1780 C CD2 . TYR A 1 233 ? -44.226 21.268 86.729 1.00 34.60 ? 233 TYR A CD2 1 ATOM 1781 C CE1 . TYR A 1 233 ? -45.369 19.718 88.711 1.00 34.74 ? 233 TYR A CE1 1 ATOM 1782 C CE2 . TYR A 1 233 ? -45.482 21.577 87.203 1.00 35.73 ? 233 TYR A CE2 1 ATOM 1783 C CZ . TYR A 1 233 ? -46.048 20.805 88.197 1.00 36.71 ? 233 TYR A CZ 1 ATOM 1784 O OH . TYR A 1 233 ? -47.305 21.132 88.652 1.00 37.16 ? 233 TYR A OH 1 ATOM 1785 N N . TRP A 1 234 ? -40.440 19.502 84.092 1.00 33.18 ? 234 TRP A N 1 ATOM 1786 C CA . TRP A 1 234 ? -39.116 19.339 83.478 1.00 31.97 ? 234 TRP A CA 1 ATOM 1787 C C . TRP A 1 234 ? -38.348 20.628 83.477 1.00 31.43 ? 234 TRP A C 1 ATOM 1788 O O . TRP A 1 234 ? -38.923 21.718 83.528 1.00 30.90 ? 234 TRP A O 1 ATOM 1789 C CB . TRP A 1 234 ? -39.228 18.744 82.071 1.00 32.85 ? 234 TRP A CB 1 ATOM 1790 C CG . TRP A 1 234 ? -39.708 19.710 81.018 1.00 33.55 ? 234 TRP A CG 1 ATOM 1791 C CD1 . TRP A 1 234 ? -38.934 20.537 80.196 1.00 34.59 ? 234 TRP A CD1 1 ATOM 1792 C CD2 . TRP A 1 234 ? -41.078 19.970 80.628 1.00 34.86 ? 234 TRP A CD2 1 ATOM 1793 N NE1 . TRP A 1 234 ? -39.718 21.274 79.372 1.00 35.55 ? 234 TRP A NE1 1 ATOM 1794 C CE2 . TRP A 1 234 ? -41.014 20.980 79.568 1.00 34.89 ? 234 TRP A CE2 1 ATOM 1795 C CE3 . TRP A 1 234 ? -42.312 19.473 81.017 1.00 36.10 ? 234 TRP A CE3 1 ATOM 1796 C CZ2 . TRP A 1 234 ? -42.134 21.461 78.958 1.00 37.41 ? 234 TRP A CZ2 1 ATOM 1797 C CZ3 . TRP A 1 234 ? -43.453 19.960 80.377 1.00 37.15 ? 234 TRP A CZ3 1 ATOM 1798 C CH2 . TRP A 1 234 ? -43.368 20.934 79.374 1.00 38.59 ? 234 TRP A CH2 1 ATOM 1799 N N . THR A 1 235 ? -37.040 20.509 83.429 1.00 31.98 ? 235 THR A N 1 ATOM 1800 C CA . THR A 1 235 ? -36.131 21.655 83.496 1.00 32.77 ? 235 THR A CA 1 ATOM 1801 C C . THR A 1 235 ? -34.943 21.314 82.611 1.00 34.31 ? 235 THR A C 1 ATOM 1802 O O . THR A 1 235 ? -34.331 20.241 82.763 1.00 34.52 ? 235 THR A O 1 ATOM 1803 C CB . THR A 1 235 ? -35.618 21.915 84.934 1.00 34.39 ? 235 THR A CB 1 ATOM 1804 O OG1 . THR A 1 235 ? -36.712 21.992 85.853 1.00 33.00 ? 235 THR A OG1 1 ATOM 1805 C CG2 . THR A 1 235 ? -34.790 23.231 85.017 1.00 34.71 ? 235 THR A CG2 1 ATOM 1806 N N . ILE A 1 236 ? -34.614 22.211 81.682 1.00 34.57 ? 236 ILE A N 1 ATOM 1807 C CA . ILE A 1 236 ? -33.420 22.039 80.846 1.00 35.05 ? 236 ILE A CA 1 ATOM 1808 C C . ILE A 1 236 ? -32.308 22.907 81.415 1.00 35.56 ? 236 ILE A C 1 ATOM 1809 O O . ILE A 1 236 ? -32.525 24.090 81.698 1.00 36.03 ? 236 ILE A O 1 ATOM 1810 C CB . ILE A 1 236 ? -33.716 22.386 79.367 1.00 35.84 ? 236 ILE A CB 1 ATOM 1811 C CG1 . ILE A 1 236 ? -34.697 21.362 78.787 1.00 36.15 ? 236 ILE A CG1 1 ATOM 1812 C CG2 . ILE A 1 236 ? -32.428 22.360 78.547 1.00 36.19 ? 236 ILE A CG2 1 ATOM 1813 C CD1 . ILE A 1 236 ? -35.308 21.765 77.463 1.00 36.18 ? 236 ILE A CD1 1 ATOM 1814 N N . VAL A 1 237 ? -31.129 22.320 81.619 1.00 35.78 ? 237 VAL A N 1 ATOM 1815 C CA . VAL A 1 237 ? -30.008 23.025 82.207 1.00 37.32 ? 237 VAL A CA 1 ATOM 1816 C C . VAL A 1 237 ? -28.855 23.110 81.198 1.00 39.06 ? 237 VAL A C 1 ATOM 1817 O O . VAL A 1 237 ? -28.357 22.090 80.706 1.00 37.81 ? 237 VAL A O 1 ATOM 1818 C CB . VAL A 1 237 ? -29.529 22.329 83.493 1.00 37.25 ? 237 VAL A CB 1 ATOM 1819 C CG1 . VAL A 1 237 ? -28.314 23.040 84.081 1.00 36.97 ? 237 VAL A CG1 1 ATOM 1820 C CG2 . VAL A 1 237 ? -30.672 22.261 84.504 1.00 37.13 ? 237 VAL A CG2 1 ATOM 1821 N N . LYS A 1 238 ? -28.445 24.343 80.914 1.00 40.68 ? 238 LYS A N 1 ATOM 1822 C CA . LYS A 1 238 ? -27.388 24.650 79.952 1.00 43.44 ? 238 LYS A CA 1 ATOM 1823 C C . LYS A 1 238 ? -26.000 24.452 80.559 1.00 43.40 ? 238 LYS A C 1 ATOM 1824 O O . LYS A 1 238 ? -25.827 24.635 81.768 1.00 45.20 ? 238 LYS A O 1 ATOM 1825 C CB . LYS A 1 238 ? -27.472 26.130 79.544 1.00 45.93 ? 238 LYS A CB 1 ATOM 1826 C CG . LYS A 1 238 ? -28.827 26.621 79.053 1.00 46.66 ? 238 LYS A CG 1 ATOM 1827 C CD . LYS A 1 238 ? -29.274 25.960 77.774 1.00 47.74 ? 238 LYS A CD 1 ATOM 1828 C CE . LYS A 1 238 ? -28.511 26.483 76.565 1.00 49.26 ? 238 LYS A CE 1 ATOM 1829 N NZ . LYS A 1 238 ? -29.068 25.910 75.311 1.00 48.09 ? 238 LYS A NZ 1 ATOM 1830 N N . PRO A 1 239 ? -24.994 24.131 79.712 1.00 44.28 ? 239 PRO A N 1 ATOM 1831 C CA . PRO A 1 239 ? -23.586 24.166 80.110 1.00 44.93 ? 239 PRO A CA 1 ATOM 1832 C C . PRO A 1 239 ? -23.265 25.430 80.889 1.00 45.31 ? 239 PRO A C 1 ATOM 1833 O O . PRO A 1 239 ? -23.684 26.516 80.494 1.00 45.29 ? 239 PRO A O 1 ATOM 1834 C CB . PRO A 1 239 ? -22.849 24.175 78.762 1.00 46.35 ? 239 PRO A CB 1 ATOM 1835 C CG . PRO A 1 239 ? -23.752 23.406 77.858 1.00 45.46 ? 239 PRO A CG 1 ATOM 1836 C CD . PRO A 1 239 ? -25.145 23.756 78.293 1.00 44.24 ? 239 PRO A CD 1 ATOM 1837 N N . GLY A 1 240 ? -22.580 25.274 82.015 1.00 46.48 ? 240 GLY A N 1 ATOM 1838 C CA . GLY A 1 240 ? -22.221 26.401 82.877 1.00 47.83 ? 240 GLY A CA 1 ATOM 1839 C C . GLY A 1 240 ? -23.326 26.859 83.809 1.00 46.65 ? 240 GLY A C 1 ATOM 1840 O O . GLY A 1 240 ? -23.104 27.729 84.657 1.00 49.43 ? 240 GLY A O 1 ATOM 1841 N N . ASP A 1 241 ? -24.526 26.302 83.651 1.00 46.83 ? 241 ASP A N 1 ATOM 1842 C CA . ASP A 1 241 ? -25.615 26.546 84.597 1.00 44.56 ? 241 ASP A CA 1 ATOM 1843 C C . ASP A 1 241 ? -25.649 25.412 85.624 1.00 44.65 ? 241 ASP A C 1 ATOM 1844 O O . ASP A 1 241 ? -24.819 24.495 85.580 1.00 44.52 ? 241 ASP A O 1 ATOM 1845 C CB . ASP A 1 241 ? -26.957 26.698 83.868 1.00 44.22 ? 241 ASP A CB 1 ATOM 1846 C CG . ASP A 1 241 ? -27.932 27.625 84.596 1.00 44.81 ? 241 ASP A CG 1 ATOM 1847 O OD1 . ASP A 1 241 ? -27.822 27.792 85.845 1.00 45.57 ? 241 ASP A OD1 1 ATOM 1848 O OD2 . ASP A 1 241 ? -28.815 28.197 83.912 1.00 45.24 ? 241 ASP A OD2 1 ATOM 1849 N N . ILE A 1 242 ? -26.570 25.532 86.581 1.00 43.93 ? 242 ILE A N 1 ATOM 1850 C CA . ILE A 1 242 ? -26.647 24.680 87.766 1.00 44.16 ? 242 ILE A CA 1 ATOM 1851 C C . ILE A 1 242 ? -28.120 24.412 88.111 1.00 42.65 ? 242 ILE A C 1 ATOM 1852 O O . ILE A 1 242 ? -28.925 25.332 88.117 1.00 43.22 ? 242 ILE A O 1 ATOM 1853 C CB . ILE A 1 242 ? -26.018 25.387 88.989 1.00 45.50 ? 242 ILE A CB 1 ATOM 1854 C CG1 . ILE A 1 242 ? -24.525 25.677 88.759 1.00 47.23 ? 242 ILE A CG1 1 ATOM 1855 C CG2 . ILE A 1 242 ? -26.209 24.560 90.243 1.00 47.53 ? 242 ILE A CG2 1 ATOM 1856 C CD1 . ILE A 1 242 ? -23.845 26.404 89.918 1.00 49.50 ? 242 ILE A CD1 1 ATOM 1857 N N . LEU A 1 243 ? -28.468 23.159 88.379 1.00 40.28 ? 243 LEU A N 1 ATOM 1858 C CA . LEU A 1 243 ? -29.795 22.822 88.887 1.00 38.66 ? 243 LEU A CA 1 ATOM 1859 C C . LEU A 1 243 ? -29.743 22.939 90.404 1.00 39.97 ? 243 LEU A C 1 ATOM 1860 O O . LEU A 1 243 ? -28.813 22.430 91.032 1.00 40.56 ? 243 LEU A O 1 ATOM 1861 C CB . LEU A 1 243 ? -30.163 21.388 88.510 1.00 37.52 ? 243 LEU A CB 1 ATOM 1862 C CG . LEU A 1 243 ? -31.599 20.958 88.800 1.00 37.37 ? 243 LEU A CG 1 ATOM 1863 C CD1 . LEU A 1 243 ? -32.549 21.626 87.806 1.00 37.00 ? 243 LEU A CD1 1 ATOM 1864 C CD2 . LEU A 1 243 ? -31.717 19.441 88.711 1.00 37.26 ? 243 LEU A CD2 1 ATOM 1865 N N . LEU A 1 244 ? -30.732 23.613 90.977 1.00 40.36 ? 244 LEU A N 1 ATOM 1866 C CA . LEU A 1 244 ? -30.883 23.710 92.415 1.00 41.44 ? 244 LEU A CA 1 ATOM 1867 C C . LEU A 1 244 ? -32.293 23.267 92.785 1.00 41.54 ? 244 LEU A C 1 ATOM 1868 O O . LEU A 1 244 ? -33.275 23.797 92.255 1.00 39.99 ? 244 LEU A O 1 ATOM 1869 C CB . LEU A 1 244 ? -30.625 25.144 92.882 1.00 42.86 ? 244 LEU A CB 1 ATOM 1870 C CG . LEU A 1 244 ? -30.587 25.408 94.389 1.00 44.03 ? 244 LEU A CG 1 ATOM 1871 C CD1 . LEU A 1 244 ? -29.601 24.477 95.077 1.00 46.61 ? 244 LEU A CD1 1 ATOM 1872 C CD2 . LEU A 1 244 ? -30.230 26.860 94.663 1.00 44.56 ? 244 LEU A CD2 1 ATOM 1873 N N . ILE A 1 245 ? -32.370 22.271 93.665 1.00 41.04 ? 245 ILE A N 1 ATOM 1874 C CA . ILE A 1 245 ? -33.622 21.725 94.158 1.00 41.26 ? 245 ILE A CA 1 ATOM 1875 C C . ILE A 1 245 ? -33.764 22.020 95.654 1.00 43.01 ? 245 ILE A C 1 ATOM 1876 O O . ILE A 1 245 ? -32.876 21.690 96.449 1.00 42.98 ? 245 ILE A O 1 ATOM 1877 C CB . ILE A 1 245 ? -33.693 20.207 93.928 1.00 41.77 ? 245 ILE A CB 1 ATOM 1878 C CG1 . ILE A 1 245 ? -33.546 19.898 92.431 1.00 42.43 ? 245 ILE A CG1 1 ATOM 1879 C CG2 . ILE A 1 245 ? -34.994 19.654 94.495 1.00 41.63 ? 245 ILE A CG2 1 ATOM 1880 C CD1 . ILE A 1 245 ? -33.432 18.430 92.092 1.00 42.51 ? 245 ILE A CD1 1 ATOM 1881 N N . ASN A 1 246 ? -34.901 22.613 96.004 1.00 43.69 ? 246 ASN A N 1 ATOM 1882 C CA . ASN A 1 246 ? -35.201 23.147 97.333 1.00 46.76 ? 246 ASN A CA 1 ATOM 1883 C C . ASN A 1 246 ? -36.581 22.594 97.733 1.00 46.41 ? 246 ASN A C 1 ATOM 1884 O O . ASN A 1 246 ? -37.588 22.939 97.105 1.00 46.07 ? 246 ASN A O 1 ATOM 1885 C CB . ASN A 1 246 ? -35.208 24.682 97.229 1.00 49.38 ? 246 ASN A CB 1 ATOM 1886 C CG . ASN A 1 246 ? -35.192 25.409 98.582 1.00 53.86 ? 246 ASN A CG 1 ATOM 1887 O OD1 . ASN A 1 246 ? -35.629 26.558 98.658 1.00 54.00 ? 246 ASN A OD1 1 ATOM 1888 N ND2 . ASN A 1 246 ? -34.691 24.770 99.630 1.00 59.59 ? 246 ASN A ND2 1 ATOM 1889 N N . SER A 1 247 ? -36.631 21.739 98.756 1.00 46.37 ? 247 SER A N 1 ATOM 1890 C CA . SER A 1 247 ? -37.878 21.070 99.168 1.00 45.16 ? 247 SER A CA 1 ATOM 1891 C C . SER A 1 247 ? -37.857 20.610 100.633 1.00 45.79 ? 247 SER A C 1 ATOM 1892 O O . SER A 1 247 ? -36.789 20.344 101.178 1.00 43.96 ? 247 SER A O 1 ATOM 1893 C CB . SER A 1 247 ? -38.105 19.834 98.306 1.00 45.68 ? 247 SER A CB 1 ATOM 1894 O OG . SER A 1 247 ? -39.261 19.120 98.723 1.00 47.15 ? 247 SER A OG 1 ATOM 1895 N N . THR A 1 248 ? -39.049 20.483 101.225 1.00 45.79 ? 248 THR A N 1 ATOM 1896 C CA . THR A 1 248 ? -39.234 19.942 102.577 1.00 48.31 ? 248 THR A CA 1 ATOM 1897 C C . THR A 1 248 ? -40.132 18.693 102.586 1.00 48.28 ? 248 THR A C 1 ATOM 1898 O O . THR A 1 248 ? -40.603 18.263 103.652 1.00 48.56 ? 248 THR A O 1 ATOM 1899 C CB . THR A 1 248 ? -39.901 20.980 103.488 1.00 50.07 ? 248 THR A CB 1 ATOM 1900 O OG1 . THR A 1 248 ? -41.123 21.404 102.873 1.00 51.94 ? 248 THR A OG1 1 ATOM 1901 C CG2 . THR A 1 248 ? -38.972 22.193 103.714 1.00 51.14 ? 248 THR A CG2 1 ATOM 1902 N N . GLY A 1 249 ? -40.363 18.123 101.407 1.00 45.48 ? 249 GLY A N 1 ATOM 1903 C CA . GLY A 1 249 ? -41.217 16.951 101.251 1.00 44.40 ? 249 GLY A CA 1 ATOM 1904 C C . GLY A 1 249 ? -41.903 16.932 99.902 1.00 43.35 ? 249 GLY A C 1 ATOM 1905 O O . GLY A 1 249 ? -41.877 17.919 99.165 1.00 41.90 ? 249 GLY A O 1 ATOM 1906 N N . ASN A 1 250 ? -42.531 15.795 99.599 1.00 41.76 ? 250 ASN A N 1 ATOM 1907 C CA . ASN A 1 250 ? -43.367 15.617 98.409 1.00 41.00 ? 250 ASN A CA 1 ATOM 1908 C C . ASN A 1 250 ? -42.593 15.624 97.082 1.00 38.87 ? 250 ASN A C 1 ATOM 1909 O O . ASN A 1 250 ? -43.199 15.643 96.026 1.00 38.07 ? 250 ASN A O 1 ATOM 1910 C CB . ASN A 1 250 ? -44.490 16.671 98.358 1.00 40.47 ? 250 ASN A CB 1 ATOM 1911 C CG . ASN A 1 250 ? -45.366 16.678 99.618 1.00 41.47 ? 250 ASN A CG 1 ATOM 1912 O OD1 . ASN A 1 250 ? -44.965 17.195 100.658 1.00 41.41 ? 250 ASN A OD1 1 ATOM 1913 N ND2 . ASN A 1 250 ? -46.588 16.150 99.501 1.00 39.42 ? 250 ASN A ND2 1 ATOM 1914 N N . LEU A 1 251 ? -41.272 15.621 97.162 1.00 37.99 ? 251 LEU A N 1 ATOM 1915 C CA . LEU A 1 251 ? -40.397 15.645 95.997 1.00 37.77 ? 251 LEU A CA 1 ATOM 1916 C C . LEU A 1 251 ? -40.208 14.246 95.395 1.00 37.53 ? 251 LEU A C 1 ATOM 1917 O O . LEU A 1 251 ? -39.727 13.326 96.064 1.00 36.84 ? 251 LEU A O 1 ATOM 1918 C CB . LEU A 1 251 ? -39.027 16.236 96.373 1.00 36.68 ? 251 LEU A CB 1 ATOM 1919 C CG . LEU A 1 251 ? -38.006 16.296 95.224 1.00 37.32 ? 251 LEU A CG 1 ATOM 1920 C CD1 . LEU A 1 251 ? -38.493 17.186 94.086 1.00 35.06 ? 251 LEU A CD1 1 ATOM 1921 C CD2 . LEU A 1 251 ? -36.624 16.711 95.735 1.00 36.15 ? 251 LEU A CD2 1 ATOM 1922 N N . ILE A 1 252 ? -40.592 14.100 94.131 1.00 35.60 ? 252 ILE A N 1 ATOM 1923 C CA . ILE A 1 252 ? -40.229 12.941 93.327 1.00 35.68 ? 252 ILE A CA 1 ATOM 1924 C C . ILE A 1 252 ? -38.994 13.364 92.528 1.00 35.39 ? 252 ILE A C 1 ATOM 1925 O O . ILE A 1 252 ? -39.091 14.106 91.543 1.00 33.82 ? 252 ILE A O 1 ATOM 1926 C CB . ILE A 1 252 ? -41.388 12.515 92.413 1.00 36.25 ? 252 ILE A CB 1 ATOM 1927 C CG1 . ILE A 1 252 ? -42.631 12.185 93.254 1.00 37.50 ? 252 ILE A CG1 1 ATOM 1928 C CG2 . ILE A 1 252 ? -41.011 11.307 91.552 1.00 35.80 ? 252 ILE A CG2 1 ATOM 1929 C CD1 . ILE A 1 252 ? -42.406 11.097 94.296 1.00 37.28 ? 252 ILE A CD1 1 ATOM 1930 N N . ALA A 1 253 ? -37.830 12.909 92.972 1.00 34.89 ? 253 ALA A N 1 ATOM 1931 C CA . ALA A 1 253 ? -36.549 13.460 92.518 1.00 35.69 ? 253 ALA A CA 1 ATOM 1932 C C . ALA A 1 253 ? -36.006 12.798 91.250 1.00 35.17 ? 253 ALA A C 1 ATOM 1933 O O . ALA A 1 253 ? -36.242 11.603 91.013 1.00 34.22 ? 253 ALA A O 1 ATOM 1934 C CB . ALA A 1 253 ? -35.514 13.358 93.631 1.00 35.50 ? 253 ALA A CB 1 ATOM 1935 N N . PRO A 1 254 ? -35.236 13.562 90.446 1.00 36.15 ? 254 PRO A N 1 ATOM 1936 C CA . PRO A 1 254 ? -34.576 12.957 89.274 1.00 36.18 ? 254 PRO A CA 1 ATOM 1937 C C . PRO A 1 254 ? -33.402 12.100 89.727 1.00 36.81 ? 254 PRO A C 1 ATOM 1938 O O . PRO A 1 254 ? -32.816 12.391 90.771 1.00 37.07 ? 254 PRO A O 1 ATOM 1939 C CB . PRO A 1 254 ? -34.041 14.173 88.522 1.00 36.11 ? 254 PRO A CB 1 ATOM 1940 C CG . PRO A 1 254 ? -33.668 15.118 89.615 1.00 36.24 ? 254 PRO A CG 1 ATOM 1941 C CD . PRO A 1 254 ? -34.737 14.935 90.693 1.00 35.80 ? 254 PRO A CD 1 ATOM 1942 N N . ARG A 1 255 ? -33.068 11.067 88.956 1.00 37.50 ? 255 ARG A N 1 ATOM 1943 C CA . ARG A 1 255 ? -31.879 10.221 89.232 1.00 38.00 ? 255 ARG A CA 1 ATOM 1944 C C . ARG A 1 255 ? -30.716 10.597 88.308 1.00 38.23 ? 255 ARG A C 1 ATOM 1945 O O . ARG A 1 255 ? -29.658 9.962 88.320 1.00 37.01 ? 255 ARG A O 1 ATOM 1946 C CB . ARG A 1 255 ? -32.199 8.750 89.005 1.00 38.62 ? 255 ARG A CB 1 ATOM 1947 C CG . ARG A 1 255 ? -33.253 8.177 89.936 1.00 39.54 ? 255 ARG A CG 1 ATOM 1948 C CD . ARG A 1 255 ? -33.316 6.661 89.811 1.00 40.78 ? 255 ARG A CD 1 ATOM 1949 N NE . ARG A 1 255 ? -34.304 6.130 90.743 1.00 42.28 ? 255 ARG A NE 1 ATOM 1950 C CZ . ARG A 1 255 ? -34.059 5.852 92.029 1.00 42.94 ? 255 ARG A CZ 1 ATOM 1951 N NH1 . ARG A 1 255 ? -32.844 6.011 92.556 1.00 42.75 ? 255 ARG A NH1 1 ATOM 1952 N NH2 . ARG A 1 255 ? -35.050 5.399 92.792 1.00 43.48 ? 255 ARG A NH2 1 ATOM 1953 N N . GLY A 1 256 ? -30.934 11.612 87.476 1.00 36.72 ? 256 GLY A N 1 ATOM 1954 C CA . GLY A 1 256 ? -29.976 11.976 86.436 1.00 36.88 ? 256 GLY A CA 1 ATOM 1955 C C . GLY A 1 256 ? -30.676 12.789 85.363 1.00 35.25 ? 256 GLY A C 1 ATOM 1956 O O . GLY A 1 256 ? -31.732 13.376 85.632 1.00 34.72 ? 256 GLY A O 1 ATOM 1957 N N . TYR A 1 257 ? -30.087 12.829 84.167 1.00 34.88 ? 257 TYR A N 1 ATOM 1958 C CA . TYR A 1 257 ? -30.615 13.651 83.077 1.00 34.85 ? 257 TYR A CA 1 ATOM 1959 C C . TYR A 1 257 ? -30.730 12.890 81.794 1.00 34.26 ? 257 TYR A C 1 ATOM 1960 O O . TYR A 1 257 ? -30.001 11.931 81.545 1.00 34.84 ? 257 TYR A O 1 ATOM 1961 C CB . TYR A 1 257 ? -29.754 14.887 82.811 1.00 35.63 ? 257 TYR A CB 1 ATOM 1962 C CG . TYR A 1 257 ? -28.346 14.571 82.404 1.00 37.48 ? 257 TYR A CG 1 ATOM 1963 C CD1 . TYR A 1 257 ? -28.009 14.401 81.073 1.00 37.69 ? 257 TYR A CD1 1 ATOM 1964 C CD2 . TYR A 1 257 ? -27.340 14.437 83.369 1.00 38.48 ? 257 TYR A CD2 1 ATOM 1965 C CE1 . TYR A 1 257 ? -26.715 14.102 80.697 1.00 38.75 ? 257 TYR A CE1 1 ATOM 1966 C CE2 . TYR A 1 257 ? -26.036 14.134 83.008 1.00 40.44 ? 257 TYR A CE2 1 ATOM 1967 C CZ . TYR A 1 257 ? -25.732 13.965 81.674 1.00 40.50 ? 257 TYR A CZ 1 ATOM 1968 O OH . TYR A 1 257 ? -24.462 13.680 81.285 1.00 41.56 ? 257 TYR A OH 1 ATOM 1969 N N . PHE A 1 258 ? -31.643 13.362 80.955 1.00 33.03 ? 258 PHE A N 1 ATOM 1970 C CA . PHE A 1 258 ? -31.743 12.859 79.607 1.00 33.28 ? 258 PHE A CA 1 ATOM 1971 C C . PHE A 1 258 ? -30.894 13.748 78.734 1.00 35.61 ? 258 PHE A C 1 ATOM 1972 O O . PHE A 1 258 ? -30.794 14.962 78.982 1.00 35.56 ? 258 PHE A O 1 ATOM 1973 C CB . PHE A 1 258 ? -33.185 12.875 79.124 1.00 31.56 ? 258 PHE A CB 1 ATOM 1974 C CG . PHE A 1 258 ? -34.043 11.872 79.814 1.00 30.27 ? 258 PHE A CG 1 ATOM 1975 C CD1 . PHE A 1 258 ? -34.131 10.579 79.324 1.00 30.92 ? 258 PHE A CD1 1 ATOM 1976 C CD2 . PHE A 1 258 ? -34.723 12.200 80.966 1.00 30.97 ? 258 PHE A CD2 1 ATOM 1977 C CE1 . PHE A 1 258 ? -34.914 9.641 79.962 1.00 30.91 ? 258 PHE A CE1 1 ATOM 1978 C CE2 . PHE A 1 258 ? -35.530 11.274 81.598 1.00 30.73 ? 258 PHE A CE2 1 ATOM 1979 C CZ . PHE A 1 258 ? -35.615 9.986 81.086 1.00 30.73 ? 258 PHE A CZ 1 ATOM 1980 N N . LYS A 1 259 ? -30.253 13.123 77.758 1.00 37.77 ? 259 LYS A N 1 ATOM 1981 C CA . LYS A 1 259 ? -29.606 13.845 76.697 1.00 41.96 ? 259 LYS A CA 1 ATOM 1982 C C . LYS A 1 259 ? -30.740 14.442 75.898 1.00 41.88 ? 259 LYS A C 1 ATOM 1983 O O . LYS A 1 259 ? -31.813 13.829 75.765 1.00 42.26 ? 259 LYS A O 1 ATOM 1984 C CB . LYS A 1 259 ? -28.787 12.906 75.828 1.00 45.36 ? 259 LYS A CB 1 ATOM 1985 C CG . LYS A 1 259 ? -27.600 12.324 76.554 1.00 47.18 ? 259 LYS A CG 1 ATOM 1986 C CD . LYS A 1 259 ? -26.444 13.306 76.560 1.00 51.13 ? 259 LYS A CD 1 ATOM 1987 C CE . LYS A 1 259 ? -25.440 13.032 75.447 1.00 52.31 ? 259 LYS A CE 1 ATOM 1988 N NZ . LYS A 1 259 ? -24.297 12.203 75.923 1.00 53.24 ? 259 LYS A NZ 1 ATOM 1989 N N . ILE A 1 260 ? -30.542 15.662 75.437 1.00 40.29 ? 260 ILE A N 1 ATOM 1990 C CA . ILE A 1 260 ? -31.494 16.271 74.553 1.00 40.50 ? 260 ILE A CA 1 ATOM 1991 C C . ILE A 1 260 ? -30.722 16.582 73.275 1.00 41.83 ? 260 ILE A C 1 ATOM 1992 O O . ILE A 1 260 ? -29.679 17.215 73.322 1.00 43.42 ? 260 ILE A O 1 ATOM 1993 C CB . ILE A 1 260 ? -32.200 17.462 75.212 1.00 40.80 ? 260 ILE A CB 1 ATOM 1994 C CG1 . ILE A 1 260 ? -33.222 18.055 74.259 1.00 40.31 ? 260 ILE A CG1 1 ATOM 1995 C CG2 . ILE A 1 260 ? -31.209 18.507 75.699 1.00 41.49 ? 260 ILE A CG2 1 ATOM 1996 C CD1 . ILE A 1 260 ? -34.253 18.908 74.964 1.00 38.80 ? 260 ILE A CD1 1 ATOM 1997 N N . ARG A 1 261 ? -31.199 16.050 72.152 1.00 40.81 ? 261 ARG A N 1 ATOM 1998 C CA . ARG A 1 261 ? -30.522 16.207 70.870 1.00 42.94 ? 261 ARG A CA 1 ATOM 1999 C C . ARG A 1 261 ? -31.409 17.028 69.977 1.00 41.30 ? 261 ARG A C 1 ATOM 2000 O O . ARG A 1 261 ? -32.571 17.248 70.289 1.00 39.43 ? 261 ARG A O 1 ATOM 2001 C CB . ARG A 1 261 ? -30.238 14.839 70.233 1.00 45.66 ? 261 ARG A CB 1 ATOM 2002 C CG . ARG A 1 261 ? -29.361 13.959 71.127 1.00 48.78 ? 261 ARG A CG 1 ATOM 2003 C CD . ARG A 1 261 ? -28.826 12.729 70.403 1.00 53.80 ? 261 ARG A CD 1 ATOM 2004 N NE . ARG A 1 261 ? -27.902 11.942 71.241 1.00 58.36 ? 261 ARG A NE 1 ATOM 2005 C CZ . ARG A 1 261 ? -26.638 12.283 71.524 1.00 63.63 ? 261 ARG A CZ 1 ATOM 2006 N NH1 . ARG A 1 261 ? -26.106 13.416 71.062 1.00 64.84 ? 261 ARG A NH1 1 ATOM 2007 N NH2 . ARG A 1 261 ? -25.887 11.489 72.290 1.00 65.37 ? 261 ARG A NH2 1 ATOM 2008 N N . SER A 1 262 ? -30.858 17.499 68.873 1.00 42.93 ? 262 SER A N 1 ATOM 2009 C CA . SER A 1 262 ? -31.684 18.087 67.833 1.00 43.74 ? 262 SER A CA 1 ATOM 2010 C C . SER A 1 262 ? -31.485 17.298 66.561 1.00 43.04 ? 262 SER A C 1 ATOM 2011 O O . SER A 1 262 ? -30.372 16.863 66.245 1.00 42.95 ? 262 SER A O 1 ATOM 2012 C CB . SER A 1 262 ? -31.349 19.563 67.623 1.00 46.38 ? 262 SER A CB 1 ATOM 2013 O OG . SER A 1 262 ? -30.172 19.711 66.867 1.00 49.10 ? 262 SER A OG 1 ATOM 2014 N N . GLY A 1 263 ? -32.568 17.092 65.835 1.00 36.88 ? 263 GLY A N 1 ATOM 2015 C CA . GLY A 1 263 ? -32.486 16.368 64.585 1.00 36.75 ? 263 GLY A CA 1 ATOM 2016 C C . GLY A 1 263 ? -33.884 16.177 64.040 1.00 35.69 ? 263 GLY A C 1 ATOM 2017 O O . GLY A 1 263 ? -34.794 16.950 64.365 1.00 36.80 ? 263 GLY A O 1 ATOM 2018 N N . LYS A 1 264 ? -34.032 15.124 63.248 1.00 32.66 ? 264 LYS A N 1 ATOM 2019 C CA . LYS A 1 264 ? -35.186 14.939 62.403 1.00 32.08 ? 264 LYS A CA 1 ATOM 2020 C C . LYS A 1 264 ? -36.215 13.962 63.003 1.00 27.56 ? 264 LYS A C 1 ATOM 2021 O O . LYS A 1 264 ? -37.030 13.447 62.283 1.00 25.22 ? 264 LYS A O 1 ATOM 2022 C CB . LYS A 1 264 ? -34.713 14.444 61.033 1.00 35.80 ? 264 LYS A CB 1 ATOM 2023 C CG . LYS A 1 264 ? -33.571 15.262 60.400 1.00 42.13 ? 264 LYS A CG 1 ATOM 2024 C CD . LYS A 1 264 ? -33.804 16.773 60.400 1.00 45.07 ? 264 LYS A CD 1 ATOM 2025 C CE . LYS A 1 264 ? -32.718 17.544 59.630 1.00 49.62 ? 264 LYS A CE 1 ATOM 2026 N NZ . LYS A 1 264 ? -31.551 17.986 60.473 1.00 52.99 ? 264 LYS A NZ 1 ATOM 2027 N N . SER A 1 265 ? -36.163 13.700 64.308 1.00 24.56 ? 265 SER A N 1 ATOM 2028 C CA . SER A 1 265 ? -37.036 12.682 64.880 1.00 23.20 ? 265 SER A CA 1 ATOM 2029 C C . SER A 1 265 ? -38.458 13.186 65.127 1.00 22.50 ? 265 SER A C 1 ATOM 2030 O O . SER A 1 265 ? -38.693 14.379 65.253 1.00 21.58 ? 265 SER A O 1 ATOM 2031 C CB . SER A 1 265 ? -36.422 12.136 66.176 1.00 24.18 ? 265 SER A CB 1 ATOM 2032 O OG . SER A 1 265 ? -35.189 11.497 65.874 1.00 23.80 ? 265 SER A OG 1 ATOM 2033 N N . SER A 1 266 ? -39.404 12.268 65.206 1.00 21.79 ? 266 SER A N 1 ATOM 2034 C CA . SER A 1 266 ? -40.797 12.639 65.490 1.00 21.94 ? 266 SER A CA 1 ATOM 2035 C C . SER A 1 266 ? -41.544 11.466 66.153 1.00 21.55 ? 266 SER A C 1 ATOM 2036 O O . SER A 1 266 ? -40.939 10.431 66.491 1.00 21.55 ? 266 SER A O 1 ATOM 2037 C CB . SER A 1 266 ? -41.519 13.090 64.207 1.00 22.62 ? 266 SER A CB 1 ATOM 2038 O OG . SER A 1 266 ? -42.779 13.715 64.511 1.00 23.57 ? 266 SER A OG 1 ATOM 2039 N N . ILE A 1 267 ? -42.842 11.639 66.303 1.00 21.26 ? 267 ILE A N 1 ATOM 2040 C CA . ILE A 1 267 ? -43.759 10.667 66.897 1.00 21.69 ? 267 ILE A CA 1 ATOM 2041 C C . ILE A 1 267 ? -45.038 10.644 66.094 1.00 22.82 ? 267 ILE A C 1 ATOM 2042 O O . ILE A 1 267 ? -45.458 11.695 65.560 1.00 21.80 ? 267 ILE A O 1 ATOM 2043 C CB . ILE A 1 267 ? -43.975 11.034 68.382 1.00 22.25 ? 267 ILE A CB 1 ATOM 2044 C CG1 . ILE A 1 267 ? -44.738 9.941 69.142 1.00 22.33 ? 267 ILE A CG1 1 ATOM 2045 C CG2 . ILE A 1 267 ? -44.640 12.392 68.554 1.00 21.62 ? 267 ILE A CG2 1 ATOM 2046 C CD1 . ILE A 1 267 ? -44.554 10.059 70.649 1.00 22.38 ? 267 ILE A CD1 1 ATOM 2047 N N . MET A 1 268 ? -45.654 9.461 65.979 1.00 22.93 ? 268 MET A N 1 ATOM 2048 C CA . MET A 1 268 ? -46.863 9.298 65.226 1.00 23.84 ? 268 MET A CA 1 ATOM 2049 C C . MET A 1 268 ? -47.789 8.311 65.962 1.00 24.03 ? 268 MET A C 1 ATOM 2050 O O . MET A 1 268 ? -47.316 7.312 66.541 1.00 24.37 ? 268 MET A O 1 ATOM 2051 C CB . MET A 1 268 ? -46.544 8.754 63.832 1.00 24.25 ? 268 MET A CB 1 ATOM 2052 C CG . MET A 1 268 ? -47.712 8.798 62.855 1.00 25.15 ? 268 MET A CG 1 ATOM 2053 S SD . MET A 1 268 ? -47.279 8.085 61.258 1.00 25.46 ? 268 MET A SD 1 ATOM 2054 C CE . MET A 1 268 ? -46.262 9.390 60.550 1.00 24.01 ? 268 MET A CE 1 ATOM 2055 N N . ARG A 1 269 ? -49.080 8.624 65.990 1.00 23.10 ? 269 ARG A N 1 ATOM 2056 C CA . ARG A 1 269 ? -50.103 7.695 66.502 1.00 24.17 ? 269 ARG A CA 1 ATOM 2057 C C . ARG A 1 269 ? -50.565 6.825 65.355 1.00 24.24 ? 269 ARG A C 1 ATOM 2058 O O . ARG A 1 269 ? -51.053 7.351 64.324 1.00 23.24 ? 269 ARG A O 1 ATOM 2059 C CB . ARG A 1 269 ? -51.297 8.457 67.060 1.00 25.66 ? 269 ARG A CB 1 ATOM 2060 C CG . ARG A 1 269 ? -50.905 9.392 68.207 1.00 26.47 ? 269 ARG A CG 1 ATOM 2061 C CD . ARG A 1 269 ? -52.108 9.990 68.927 1.00 27.32 ? 269 ARG A CD 1 ATOM 2062 N NE . ARG A 1 269 ? -51.711 10.883 70.020 1.00 28.02 ? 269 ARG A NE 1 ATOM 2063 C CZ . ARG A 1 269 ? -51.449 12.188 69.875 1.00 29.06 ? 269 ARG A CZ 1 ATOM 2064 N NH1 . ARG A 1 269 ? -51.534 12.787 68.682 1.00 29.18 ? 269 ARG A NH1 1 ATOM 2065 N NH2 . ARG A 1 269 ? -51.106 12.901 70.931 1.00 29.09 ? 269 ARG A NH2 1 ATOM 2066 N N . SER A 1 270 ? -50.409 5.513 65.501 1.00 23.98 ? 270 SER A N 1 ATOM 2067 C CA . SER A 1 270 ? -50.850 4.584 64.493 1.00 25.12 ? 270 SER A CA 1 ATOM 2068 C C . SER A 1 270 ? -51.062 3.214 65.092 1.00 26.83 ? 270 SER A C 1 ATOM 2069 O O . SER A 1 270 ? -50.312 2.798 65.985 1.00 26.24 ? 270 SER A O 1 ATOM 2070 C CB . SER A 1 270 ? -49.813 4.481 63.367 1.00 24.89 ? 270 SER A CB 1 ATOM 2071 O OG . SER A 1 270 ? -50.164 3.488 62.404 1.00 25.68 ? 270 SER A OG 1 ATOM 2072 N N . ASP A 1 271 ? -52.040 2.500 64.561 1.00 27.51 ? 271 ASP A N 1 ATOM 2073 C CA . ASP A 1 271 ? -52.143 1.056 64.836 1.00 30.32 ? 271 ASP A CA 1 ATOM 2074 C C . ASP A 1 271 ? -51.659 0.139 63.698 1.00 30.85 ? 271 ASP A C 1 ATOM 2075 O O . ASP A 1 271 ? -51.877 -1.092 63.736 1.00 31.38 ? 271 ASP A O 1 ATOM 2076 C CB . ASP A 1 271 ? -53.581 0.734 65.270 1.00 33.08 ? 271 ASP A CB 1 ATOM 2077 C CG . ASP A 1 271 ? -53.917 1.374 66.592 1.00 34.88 ? 271 ASP A CG 1 ATOM 2078 O OD1 . ASP A 1 271 ? -52.985 1.537 67.414 1.00 34.86 ? 271 ASP A OD1 1 ATOM 2079 O OD2 . ASP A 1 271 ? -55.097 1.745 66.818 1.00 37.23 ? 271 ASP A OD2 1 ATOM 2080 N N . ALA A 1 272 ? -50.971 0.699 62.701 1.00 28.83 ? 272 ALA A N 1 ATOM 2081 C CA . ALA A 1 272 ? -50.508 -0.100 61.566 1.00 29.34 ? 272 ALA A CA 1 ATOM 2082 C C . ALA A 1 272 ? -49.402 -1.058 62.034 1.00 29.52 ? 272 ALA A C 1 ATOM 2083 O O . ALA A 1 272 ? -48.528 -0.644 62.773 1.00 28.74 ? 272 ALA A O 1 ATOM 2084 C CB . ALA A 1 272 ? -50.007 0.792 60.439 1.00 28.85 ? 272 ALA A CB 1 ATOM 2085 N N . PRO A 1 273 ? -49.439 -2.336 61.607 1.00 31.05 ? 273 PRO A N 1 ATOM 2086 C CA . PRO A 1 273 ? -48.336 -3.222 62.000 1.00 32.22 ? 273 PRO A CA 1 ATOM 2087 C C . PRO A 1 273 ? -47.027 -2.785 61.351 1.00 32.14 ? 273 PRO A C 1 ATOM 2088 O O . PRO A 1 273 ? -47.046 -2.140 60.299 1.00 29.90 ? 273 PRO A O 1 ATOM 2089 C CB . PRO A 1 273 ? -48.769 -4.604 61.458 1.00 33.67 ? 273 PRO A CB 1 ATOM 2090 C CG . PRO A 1 273 ? -49.741 -4.317 60.392 1.00 35.20 ? 273 PRO A CG 1 ATOM 2091 C CD . PRO A 1 273 ? -50.405 -3.003 60.718 1.00 33.27 ? 273 PRO A CD 1 ATOM 2092 N N . ILE A 1 274 ? -45.906 -3.138 61.961 1.00 32.99 ? 274 ILE A N 1 ATOM 2093 C CA . ILE A 1 274 ? -44.610 -2.774 61.402 1.00 34.16 ? 274 ILE A CA 1 ATOM 2094 C C . ILE A 1 274 ? -44.108 -3.931 60.560 1.00 36.46 ? 274 ILE A C 1 ATOM 2095 O O . ILE A 1 274 ? -44.092 -5.062 61.027 1.00 36.34 ? 274 ILE A O 1 ATOM 2096 C CB . ILE A 1 274 ? -43.630 -2.362 62.506 1.00 35.65 ? 274 ILE A CB 1 ATOM 2097 C CG1 . ILE A 1 274 ? -44.069 -0.989 63.064 1.00 36.20 ? 274 ILE A CG1 1 ATOM 2098 C CG2 . ILE A 1 274 ? -42.204 -2.227 61.961 1.00 35.56 ? 274 ILE A CG2 1 ATOM 2099 C CD1 . ILE A 1 274 ? -43.631 -0.781 64.475 1.00 37.09 ? 274 ILE A CD1 1 ATOM 2100 N N . GLY A 1 275 ? -43.772 -3.653 59.304 1.00 35.61 ? 275 GLY A N 1 ATOM 2101 C CA . GLY A 1 275 ? -43.322 -4.688 58.376 1.00 36.52 ? 275 GLY A CA 1 ATOM 2102 C C . GLY A 1 275 ? -41.828 -4.635 58.077 1.00 36.91 ? 275 GLY A C 1 ATOM 2103 O O . GLY A 1 275 ? -41.177 -3.582 58.220 1.00 32.86 ? 275 GLY A O 1 ATOM 2104 N N . LYS A 1 276 ? -41.289 -5.765 57.622 1.00 37.17 ? 276 LYS A N 1 ATOM 2105 C CA . LYS A 1 276 ? -39.905 -5.823 57.149 1.00 38.94 ? 276 LYS A CA 1 ATOM 2106 C C . LYS A 1 276 ? -39.871 -5.491 55.663 1.00 38.10 ? 276 LYS A C 1 ATOM 2107 O O . LYS A 1 276 ? -40.031 -6.349 54.809 1.00 39.12 ? 276 LYS A O 1 ATOM 2108 C CB . LYS A 1 276 ? -39.267 -7.174 57.476 1.00 41.89 ? 276 LYS A CB 1 ATOM 2109 C CG . LYS A 1 276 ? -39.205 -7.404 58.995 1.00 44.88 ? 276 LYS A CG 1 ATOM 2110 C CD . LYS A 1 276 ? -38.384 -8.619 59.420 1.00 47.79 ? 276 LYS A CD 1 ATOM 2111 C CE . LYS A 1 276 ? -38.622 -8.970 60.887 1.00 49.53 ? 276 LYS A CE 1 ATOM 2112 N NZ . LYS A 1 276 ? -38.194 -7.901 61.857 1.00 52.62 ? 276 LYS A NZ 1 ATOM 2113 N N . CYS A 1 277 ? -39.705 -4.212 55.362 1.00 35.93 ? 277 CYS A N 1 ATOM 2114 C CA . CYS A 1 277 ? -39.831 -3.695 53.993 1.00 35.60 ? 277 CYS A CA 1 ATOM 2115 C C . CYS A 1 277 ? -39.227 -2.305 54.022 1.00 32.48 ? 277 CYS A C 1 ATOM 2116 O O . CYS A 1 277 ? -38.871 -1.839 55.102 1.00 31.47 ? 277 CYS A O 1 ATOM 2117 C CB . CYS A 1 277 ? -41.294 -3.640 53.484 1.00 38.33 ? 277 CYS A CB 1 ATOM 2118 S SG . CYS A 1 277 ? -42.554 -2.813 54.512 1.00 44.52 ? 277 CYS A SG 1 ATOM 2119 N N . ASN A 1 278 ? -39.127 -1.663 52.862 1.00 29.37 ? 278 ASN A N 1 ATOM 2120 C CA . ASN A 1 278 ? -38.408 -0.411 52.748 1.00 29.30 ? 278 ASN A CA 1 ATOM 2121 C C . ASN A 1 278 ? -39.304 0.612 52.054 1.00 28.77 ? 278 ASN A C 1 ATOM 2122 O O . ASN A 1 278 ? -39.700 0.395 50.930 1.00 26.70 ? 278 ASN A O 1 ATOM 2123 C CB . ASN A 1 278 ? -37.124 -0.673 51.946 1.00 29.80 ? 278 ASN A CB 1 ATOM 2124 C CG . ASN A 1 278 ? -36.131 0.472 52.030 1.00 31.19 ? 278 ASN A CG 1 ATOM 2125 O OD1 . ASN A 1 278 ? -36.480 1.617 51.750 1.00 32.43 ? 278 ASN A OD1 1 ATOM 2126 N ND2 . ASN A 1 278 ? -34.875 0.164 52.404 1.00 31.03 ? 278 ASN A ND2 1 ATOM 2127 N N . SER A 1 279 ? -39.633 1.701 52.733 1.00 28.86 ? 279 SER A N 1 ATOM 2128 C CA . SER A 1 279 ? -40.446 2.774 52.131 1.00 29.94 ? 279 SER A CA 1 ATOM 2129 C C . SER A 1 279 ? -40.098 4.113 52.799 1.00 28.79 ? 279 SER A C 1 ATOM 2130 O O . SER A 1 279 ? -40.005 4.206 54.023 1.00 27.37 ? 279 SER A O 1 ATOM 2131 C CB . SER A 1 279 ? -41.948 2.419 52.248 1.00 31.27 ? 279 SER A CB 1 ATOM 2132 O OG . SER A 1 279 ? -42.767 3.465 51.756 1.00 33.95 ? 279 SER A OG 1 ATOM 2133 N N . GLU A 1 280 ? -39.882 5.148 51.990 1.00 28.48 ? 280 GLU A N 1 ATOM 2134 C CA . GLU A 1 280 ? -39.483 6.459 52.515 1.00 29.08 ? 280 GLU A CA 1 ATOM 2135 C C . GLU A 1 280 ? -40.583 7.237 53.262 1.00 27.74 ? 280 GLU A C 1 ATOM 2136 O O . GLU A 1 280 ? -40.272 8.029 54.167 1.00 27.33 ? 280 GLU A O 1 ATOM 2137 C CB . GLU A 1 280 ? -38.953 7.336 51.377 1.00 31.90 ? 280 GLU A CB 1 ATOM 2138 C CG . GLU A 1 280 ? -37.671 6.834 50.721 1.00 34.65 ? 280 GLU A CG 1 ATOM 2139 C CD . GLU A 1 280 ? -36.421 7.111 51.531 1.00 38.60 ? 280 GLU A CD 1 ATOM 2140 O OE1 . GLU A 1 280 ? -36.469 7.904 52.506 1.00 39.72 ? 280 GLU A OE1 1 ATOM 2141 O OE2 . GLU A 1 280 ? -35.387 6.496 51.204 1.00 40.43 ? 280 GLU A OE2 1 ATOM 2142 N N . CYS A 1 281 ? -41.839 7.055 52.841 1.00 26.34 ? 281 CYS A N 1 ATOM 2143 C CA . CYS A 1 281 ? -42.967 7.835 53.358 1.00 24.64 ? 281 CYS A CA 1 ATOM 2144 C C . CYS A 1 281 ? -43.849 7.042 54.300 1.00 23.47 ? 281 CYS A C 1 ATOM 2145 O O . CYS A 1 281 ? -44.378 5.985 53.929 1.00 24.41 ? 281 CYS A O 1 ATOM 2146 C CB . CYS A 1 281 ? -43.816 8.327 52.204 1.00 25.92 ? 281 CYS A CB 1 ATOM 2147 S SG . CYS A 1 281 ? -45.170 9.333 52.816 1.00 25.52 ? 281 CYS A SG 1 ATOM 2148 N N . ILE A 1 282 ? -43.963 7.520 55.529 1.00 22.28 ? 282 ILE A N 1 ATOM 2149 C CA . ILE A 1 282 ? -44.791 6.878 56.531 1.00 22.70 ? 282 ILE A CA 1 ATOM 2150 C C . ILE A 1 282 ? -46.038 7.735 56.827 1.00 22.02 ? 282 ILE A C 1 ATOM 2151 O O . ILE A 1 282 ? -45.940 8.944 57.018 1.00 20.19 ? 282 ILE A O 1 ATOM 2152 C CB . ILE A 1 282 ? -44.002 6.660 57.824 1.00 22.60 ? 282 ILE A CB 1 ATOM 2153 C CG1 . ILE A 1 282 ? -42.765 5.806 57.509 1.00 23.74 ? 282 ILE A CG1 1 ATOM 2154 C CG2 . ILE A 1 282 ? -44.908 6.026 58.881 1.00 22.73 ? 282 ILE A CG2 1 ATOM 2155 C CD1 . ILE A 1 282 ? -41.809 5.646 58.696 1.00 24.69 ? 282 ILE A CD1 1 ATOM 2156 N N . THR A 1 283 ? -47.193 7.090 56.877 1.00 21.95 ? 283 THR A N 1 ATOM 2157 C CA . THR A 1 283 ? -48.426 7.715 57.365 1.00 22.22 ? 283 THR A CA 1 ATOM 2158 C C . THR A 1 283 ? -49.030 6.793 58.425 1.00 23.15 ? 283 THR A C 1 ATOM 2159 O O . THR A 1 283 ? -48.635 5.618 58.508 1.00 23.31 ? 283 THR A O 1 ATOM 2160 C CB . THR A 1 283 ? -49.496 7.926 56.266 1.00 23.05 ? 283 THR A CB 1 ATOM 2161 O OG1 . THR A 1 283 ? -50.206 6.710 56.037 1.00 22.32 ? 283 THR A OG1 1 ATOM 2162 C CG2 . THR A 1 283 ? -48.878 8.477 54.963 1.00 22.84 ? 283 THR A CG2 1 ATOM 2163 N N . PRO A 1 284 ? -49.995 7.294 59.209 1.00 22.39 ? 284 PRO A N 1 ATOM 2164 C CA . PRO A 1 284 ? -50.672 6.423 60.191 1.00 23.23 ? 284 PRO A CA 1 ATOM 2165 C C . PRO A 1 284 ? -51.347 5.201 59.610 1.00 25.26 ? 284 PRO A C 1 ATOM 2166 O O . PRO A 1 284 ? -51.547 4.225 60.330 1.00 25.02 ? 284 PRO A O 1 ATOM 2167 C CB . PRO A 1 284 ? -51.703 7.337 60.827 1.00 23.73 ? 284 PRO A CB 1 ATOM 2168 C CG . PRO A 1 284 ? -51.127 8.715 60.699 1.00 23.20 ? 284 PRO A CG 1 ATOM 2169 C CD . PRO A 1 284 ? -50.358 8.710 59.403 1.00 22.86 ? 284 PRO A CD 1 ATOM 2170 N N . ASN A 1 285 ? -51.761 5.281 58.345 1.00 25.48 ? 285 ASN A N 1 ATOM 2171 C CA . ASN A 1 285 ? -52.389 4.173 57.650 1.00 28.31 ? 285 ASN A CA 1 ATOM 2172 C C . ASN A 1 285 ? -51.397 3.121 57.185 1.00 27.28 ? 285 ASN A C 1 ATOM 2173 O O . ASN A 1 285 ? -51.808 2.072 56.724 1.00 29.33 ? 285 ASN A O 1 ATOM 2174 C CB . ASN A 1 285 ? -53.070 4.687 56.391 1.00 32.52 ? 285 ASN A CB 1 ATOM 2175 C CG . ASN A 1 285 ? -54.440 5.269 56.641 1.00 39.49 ? 285 ASN A CG 1 ATOM 2176 O OD1 . ASN A 1 285 ? -55.385 4.536 56.869 1.00 55.02 ? 285 ASN A OD1 1 ATOM 2177 N ND2 . ASN A 1 285 ? -54.576 6.540 56.563 1.00 47.31 ? 285 ASN A ND2 1 ATOM 2178 N N . GLY A 1 286 ? -50.108 3.414 57.273 1.00 25.87 ? 286 GLY A N 1 ATOM 2179 C CA . GLY A 1 286 ? -49.038 2.590 56.718 1.00 25.64 ? 286 GLY A CA 1 ATOM 2180 C C . GLY A 1 286 ? -48.155 3.400 55.783 1.00 25.82 ? 286 GLY A C 1 ATOM 2181 O O . GLY A 1 286 ? -48.434 4.586 55.469 1.00 25.17 ? 286 GLY A O 1 ATOM 2182 N N . SER A 1 287 ? -47.085 2.780 55.318 1.00 25.47 ? 287 SER A N 1 ATOM 2183 C CA . SER A 1 287 ? -46.180 3.464 54.404 1.00 25.55 ? 287 SER A CA 1 ATOM 2184 C C . SER A 1 287 ? -46.846 3.558 53.047 1.00 24.93 ? 287 SER A C 1 ATOM 2185 O O . SER A 1 287 ? -47.666 2.739 52.693 1.00 25.16 ? 287 SER A O 1 ATOM 2186 C CB . SER A 1 287 ? -44.871 2.707 54.265 1.00 25.98 ? 287 SER A CB 1 ATOM 2187 O OG . SER A 1 287 ? -44.200 2.698 55.518 1.00 27.38 ? 287 SER A OG 1 ATOM 2188 N N . ILE A 1 288 ? -46.486 4.570 52.286 1.00 24.51 ? 288 ILE A N 1 ATOM 2189 C CA . ILE A 1 288 ? -47.023 4.723 50.957 1.00 25.51 ? 288 ILE A CA 1 ATOM 2190 C C . ILE A 1 288 ? -45.898 4.981 49.997 1.00 26.08 ? 288 ILE A C 1 ATOM 2191 O O . ILE A 1 288 ? -44.900 5.598 50.361 1.00 27.92 ? 288 ILE A O 1 ATOM 2192 C CB . ILE A 1 288 ? -48.078 5.853 50.844 1.00 25.20 ? 288 ILE A CB 1 ATOM 2193 C CG1 . ILE A 1 288 ? -47.460 7.207 51.209 1.00 25.02 ? 288 ILE A CG1 1 ATOM 2194 C CG2 . ILE A 1 288 ? -49.275 5.586 51.728 1.00 25.88 ? 288 ILE A CG2 1 ATOM 2195 C CD1 . ILE A 1 288 ? -48.387 8.393 50.928 1.00 24.94 ? 288 ILE A CD1 1 ATOM 2196 N N . PRO A 1 289 ? -46.061 4.524 48.756 1.00 28.16 ? 289 PRO A N 1 ATOM 2197 C CA . PRO A 1 289 ? -45.156 4.901 47.705 1.00 29.18 ? 289 PRO A CA 1 ATOM 2198 C C . PRO A 1 289 ? -45.079 6.417 47.553 1.00 29.28 ? 289 PRO A C 1 ATOM 2199 O O . PRO A 1 289 ? -46.098 7.099 47.747 1.00 28.60 ? 289 PRO A O 1 ATOM 2200 C CB . PRO A 1 289 ? -45.787 4.298 46.444 1.00 30.16 ? 289 PRO A CB 1 ATOM 2201 C CG . PRO A 1 289 ? -46.782 3.316 46.892 1.00 31.08 ? 289 PRO A CG 1 ATOM 2202 C CD . PRO A 1 289 ? -47.158 3.671 48.292 1.00 29.83 ? 289 PRO A CD 1 ATOM 2203 N N . ASN A 1 290 ? -43.907 6.916 47.190 1.00 28.70 ? 290 ASN A N 1 ATOM 2204 C CA . ASN A 1 290 ? -43.703 8.334 47.019 1.00 29.48 ? 290 ASN A CA 1 ATOM 2205 C C . ASN A 1 290 ? -43.300 8.747 45.592 1.00 29.44 ? 290 ASN A C 1 ATOM 2206 O O . ASN A 1 290 ? -42.655 9.772 45.401 1.00 30.86 ? 290 ASN A O 1 ATOM 2207 C CB . ASN A 1 290 ? -42.717 8.849 48.045 1.00 29.76 ? 290 ASN A CB 1 ATOM 2208 C CG . ASN A 1 290 ? -41.315 8.359 47.810 1.00 31.53 ? 290 ASN A CG 1 ATOM 2209 O OD1 . ASN A 1 290 ? -41.083 7.465 46.979 1.00 30.82 ? 290 ASN A OD1 1 ATOM 2210 N ND2 . ASN A 1 290 ? -40.368 8.921 48.567 1.00 30.16 ? 290 ASN A ND2 1 ATOM 2211 N N . ASP A 1 291 ? -43.719 7.964 44.608 1.00 28.91 ? 291 ASP A N 1 ATOM 2212 C CA . ASP A 1 291 ? -43.495 8.315 43.227 1.00 30.22 ? 291 ASP A CA 1 ATOM 2213 C C . ASP A 1 291 ? -44.375 9.529 42.817 1.00 29.00 ? 291 ASP A C 1 ATOM 2214 O O . ASP A 1 291 ? -43.897 10.442 42.139 1.00 30.04 ? 291 ASP A O 1 ATOM 2215 C CB . ASP A 1 291 ? -43.680 7.112 42.265 1.00 31.93 ? 291 ASP A CB 1 ATOM 2216 C CG . ASP A 1 291 ? -44.978 6.364 42.455 1.00 35.05 ? 291 ASP A CG 1 ATOM 2217 O OD1 . ASP A 1 291 ? -45.153 5.681 43.479 1.00 38.45 ? 291 ASP A OD1 1 ATOM 2218 O OD2 . ASP A 1 291 ? -45.844 6.431 41.559 1.00 38.75 ? 291 ASP A OD2 1 ATOM 2219 N N . LYS A 1 292 ? -45.610 9.568 43.297 1.00 25.13 ? 292 LYS A N 1 ATOM 2220 C CA . LYS A 1 292 ? -46.570 10.599 42.853 1.00 23.57 ? 292 LYS A CA 1 ATOM 2221 C C . LYS A 1 292 ? -46.336 11.890 43.636 1.00 22.09 ? 292 LYS A C 1 ATOM 2222 O O . LYS A 1 292 ? -45.845 11.857 44.766 1.00 22.33 ? 292 LYS A O 1 ATOM 2223 C CB . LYS A 1 292 ? -48.000 10.068 43.028 1.00 23.20 ? 292 LYS A CB 1 ATOM 2224 C CG . LYS A 1 292 ? -48.321 8.850 42.169 1.00 23.92 ? 292 LYS A CG 1 ATOM 2225 C CD . LYS A 1 292 ? -49.693 8.271 42.500 1.00 24.62 ? 292 LYS A CD 1 ATOM 2226 C CE . LYS A 1 292 ? -49.966 6.944 41.762 1.00 26.20 ? 292 LYS A CE 1 ATOM 2227 N NZ . LYS A 1 292 ? -48.960 5.891 42.136 1.00 28.52 ? 292 LYS A NZ 1 ATOM 2228 N N . PRO A 1 293 ? -46.696 13.037 43.063 1.00 21.14 ? 293 PRO A N 1 ATOM 2229 C CA . PRO A 1 293 ? -46.428 14.298 43.767 1.00 20.75 ? 293 PRO A CA 1 ATOM 2230 C C . PRO A 1 293 ? -47.439 14.603 44.902 1.00 20.10 ? 293 PRO A C 1 ATOM 2231 O O . PRO A 1 293 ? -47.150 15.421 45.801 1.00 19.69 ? 293 PRO A O 1 ATOM 2232 C CB . PRO A 1 293 ? -46.493 15.324 42.640 1.00 21.52 ? 293 PRO A CB 1 ATOM 2233 C CG . PRO A 1 293 ? -47.398 14.738 41.615 1.00 21.16 ? 293 PRO A CG 1 ATOM 2234 C CD . PRO A 1 293 ? -47.147 13.253 41.678 1.00 21.39 ? 293 PRO A CD 1 ATOM 2235 N N . PHE A 1 294 ? -48.604 13.974 44.836 1.00 19.78 ? 294 PHE A N 1 ATOM 2236 C CA . PHE A 1 294 ? -49.711 14.232 45.760 1.00 19.55 ? 294 PHE A CA 1 ATOM 2237 C C . PHE A 1 294 ? -50.245 12.917 46.329 1.00 19.68 ? 294 PHE A C 1 ATOM 2238 O O . PHE A 1 294 ? -49.986 11.811 45.784 1.00 19.53 ? 294 PHE A O 1 ATOM 2239 C CB . PHE A 1 294 ? -50.844 15.011 45.043 1.00 19.91 ? 294 PHE A CB 1 ATOM 2240 C CG . PHE A 1 294 ? -50.367 16.260 44.340 1.00 19.91 ? 294 PHE A CG 1 ATOM 2241 C CD1 . PHE A 1 294 ? -49.898 17.318 45.062 1.00 20.30 ? 294 PHE A CD1 1 ATOM 2242 C CD2 . PHE A 1 294 ? -50.405 16.370 42.958 1.00 21.15 ? 294 PHE A CD2 1 ATOM 2243 C CE1 . PHE A 1 294 ? -49.420 18.470 44.454 1.00 20.27 ? 294 PHE A CE1 1 ATOM 2244 C CE2 . PHE A 1 294 ? -49.930 17.525 42.338 1.00 20.49 ? 294 PHE A CE2 1 ATOM 2245 C CZ . PHE A 1 294 ? -49.427 18.557 43.079 1.00 20.40 ? 294 PHE A CZ 1 ATOM 2246 N N . GLN A 1 295 ? -50.974 13.036 47.427 1.00 19.28 ? 295 GLN A N 1 ATOM 2247 C CA . GLN A 1 295 ? -51.582 11.881 48.078 1.00 19.73 ? 295 GLN A CA 1 ATOM 2248 C C . GLN A 1 295 ? -52.801 12.311 48.853 1.00 19.40 ? 295 GLN A C 1 ATOM 2249 O O . GLN A 1 295 ? -52.877 13.449 49.293 1.00 18.97 ? 295 GLN A O 1 ATOM 2250 C CB . GLN A 1 295 ? -50.543 11.163 48.981 1.00 19.92 ? 295 GLN A CB 1 ATOM 2251 C CG . GLN A 1 295 ? -49.906 12.007 50.068 1.00 19.19 ? 295 GLN A CG 1 ATOM 2252 C CD . GLN A 1 295 ? -50.601 11.958 51.408 1.00 19.73 ? 295 GLN A CD 1 ATOM 2253 O OE1 . GLN A 1 295 ? -51.537 11.184 51.607 1.00 20.67 ? 295 GLN A OE1 1 ATOM 2254 N NE2 . GLN A 1 295 ? -50.102 12.759 52.368 1.00 18.40 ? 295 GLN A NE2 1 ATOM 2255 N N . ASN A 1 296 ? -53.765 11.397 49.000 1.00 19.63 ? 296 ASN A N 1 ATOM 2256 C CA A ASN A 1 296 ? -54.992 11.624 49.715 0.50 19.69 ? 296 ASN A CA 1 ATOM 2257 C CA B ASN A 1 296 ? -54.962 11.672 49.795 0.50 20.69 ? 296 ASN A CA 1 ATOM 2258 C C . ASN A 1 296 ? -55.165 10.575 50.831 1.00 21.15 ? 296 ASN A C 1 ATOM 2259 O O . ASN A 1 296 ? -56.278 10.317 51.314 1.00 22.10 ? 296 ASN A O 1 ATOM 2260 C CB A ASN A 1 296 ? -56.115 11.532 48.695 0.50 19.33 ? 296 ASN A CB 1 ATOM 2261 C CB B ASN A 1 296 ? -56.208 11.838 48.924 0.50 21.67 ? 296 ASN A CB 1 ATOM 2262 C CG A ASN A 1 296 ? -57.450 11.931 49.246 0.50 19.05 ? 296 ASN A CG 1 ATOM 2263 C CG B ASN A 1 296 ? -56.787 10.524 48.489 0.50 23.27 ? 296 ASN A CG 1 ATOM 2264 O OD1 A ASN A 1 296 ? -58.421 11.176 49.101 0.50 19.00 ? 296 ASN A OD1 1 ATOM 2265 O OD1 B ASN A 1 296 ? -56.057 9.539 48.311 0.50 25.14 ? 296 ASN A OD1 1 ATOM 2266 N ND2 A ASN A 1 296 ? -57.527 13.108 49.873 0.50 18.44 ? 296 ASN A ND2 1 ATOM 2267 N ND2 B ASN A 1 296 ? -58.108 10.477 48.366 0.50 23.80 ? 296 ASN A ND2 1 ATOM 2268 N N . VAL A 1 297 ? -54.062 9.937 51.221 1.00 20.92 ? 297 VAL A N 1 ATOM 2269 C CA . VAL A 1 297 ? -54.128 8.915 52.234 1.00 20.82 ? 297 VAL A CA 1 ATOM 2270 C C . VAL A 1 297 ? -54.231 9.543 53.625 1.00 20.54 ? 297 VAL A C 1 ATOM 2271 O O . VAL A 1 297 ? -55.116 9.188 54.387 1.00 20.88 ? 297 VAL A O 1 ATOM 2272 C CB . VAL A 1 297 ? -52.902 7.993 52.177 1.00 21.77 ? 297 VAL A CB 1 ATOM 2273 C CG1 . VAL A 1 297 ? -52.886 7.020 53.370 1.00 22.67 ? 297 VAL A CG1 1 ATOM 2274 C CG2 . VAL A 1 297 ? -52.896 7.227 50.839 1.00 22.27 ? 297 VAL A CG2 1 ATOM 2275 N N . ASN A 1 298 ? -53.341 10.475 53.978 1.00 19.62 ? 298 ASN A N 1 ATOM 2276 C CA . ASN A 1 298 ? -53.375 11.041 55.351 1.00 19.64 ? 298 ASN A CA 1 ATOM 2277 C C . ASN A 1 298 ? -52.642 12.358 55.373 1.00 19.55 ? 298 ASN A C 1 ATOM 2278 O O . ASN A 1 298 ? -51.513 12.490 54.816 1.00 19.17 ? 298 ASN A O 1 ATOM 2279 C CB . ASN A 1 298 ? -52.798 10.034 56.389 1.00 20.06 ? 298 ASN A CB 1 ATOM 2280 C CG . ASN A 1 298 ? -53.346 10.248 57.800 1.00 20.20 ? 298 ASN A CG 1 ATOM 2281 O OD1 . ASN A 1 298 ? -53.245 11.340 58.366 1.00 20.78 ? 298 ASN A OD1 1 ATOM 2282 N ND2 . ASN A 1 298 ? -53.943 9.203 58.369 1.00 21.20 ? 298 ASN A ND2 1 ATOM 2283 N N . ARG A 1 299 ? -53.234 13.321 56.070 1.00 19.84 ? 299 ARG A N 1 ATOM 2284 C CA . ARG A 1 299 ? -52.522 14.583 56.313 1.00 21.04 ? 299 ARG A CA 1 ATOM 2285 C C . ARG A 1 299 ? -51.298 14.447 57.234 1.00 20.22 ? 299 ARG A C 1 ATOM 2286 O O . ARG A 1 299 ? -50.400 15.280 57.198 1.00 18.88 ? 299 ARG A O 1 ATOM 2287 C CB . ARG A 1 299 ? -53.483 15.660 56.833 1.00 23.34 ? 299 ARG A CB 1 ATOM 2288 C CG . ARG A 1 299 ? -54.039 15.406 58.216 1.00 25.59 ? 299 ARG A CG 1 ATOM 2289 C CD . ARG A 1 299 ? -55.001 16.526 58.638 1.00 30.37 ? 299 ARG A CD 1 ATOM 2290 N NE . ARG A 1 299 ? -56.135 16.626 57.728 1.00 30.44 ? 299 ARG A NE 1 ATOM 2291 C CZ . ARG A 1 299 ? -56.997 17.660 57.659 1.00 34.15 ? 299 ARG A CZ 1 ATOM 2292 N NH1 . ARG A 1 299 ? -56.896 18.765 58.431 1.00 33.94 ? 299 ARG A NH1 1 ATOM 2293 N NH2 . ARG A 1 299 ? -57.990 17.592 56.802 1.00 34.47 ? 299 ARG A NH2 1 ATOM 2294 N N . ILE A 1 300 ? -51.258 13.386 58.018 1.00 19.35 ? 300 ILE A N 1 ATOM 2295 C CA . ILE A 1 300 ? -50.120 13.111 58.903 1.00 19.41 ? 300 ILE A CA 1 ATOM 2296 C C . ILE A 1 300 ? -49.130 12.277 58.131 1.00 19.36 ? 300 ILE A C 1 ATOM 2297 O O . ILE A 1 300 ? -49.448 11.191 57.666 1.00 18.78 ? 300 ILE A O 1 ATOM 2298 C CB . ILE A 1 300 ? -50.568 12.369 60.161 1.00 20.03 ? 300 ILE A CB 1 ATOM 2299 C CG1 . ILE A 1 300 ? -51.533 13.240 60.961 1.00 19.92 ? 300 ILE A CG1 1 ATOM 2300 C CG2 . ILE A 1 300 ? -49.355 11.942 61.025 1.00 19.26 ? 300 ILE A CG2 1 ATOM 2301 C CD1 . ILE A 1 300 ? -52.332 12.432 62.009 1.00 20.97 ? 300 ILE A CD1 1 ATOM 2302 N N . THR A 1 301 ? -47.933 12.818 57.934 1.00 20.00 ? 301 THR A N 1 ATOM 2303 C CA . THR A 1 301 ? -46.860 12.108 57.233 1.00 21.17 ? 301 THR A CA 1 ATOM 2304 C C . THR A 1 301 ? -45.500 12.288 57.912 1.00 21.49 ? 301 THR A C 1 ATOM 2305 O O . THR A 1 301 ? -45.285 13.252 58.673 1.00 22.36 ? 301 THR A O 1 ATOM 2306 C CB . THR A 1 301 ? -46.708 12.559 55.763 1.00 21.92 ? 301 THR A CB 1 ATOM 2307 O OG1 . THR A 1 301 ? -46.041 13.825 55.700 1.00 24.55 ? 301 THR A OG1 1 ATOM 2308 C CG2 . THR A 1 301 ? -48.052 12.689 55.079 1.00 23.40 ? 301 THR A CG2 1 ATOM 2309 N N . TYR A 1 302 ? -44.597 11.362 57.614 1.00 20.83 ? 302 TYR A N 1 ATOM 2310 C CA . TYR A 1 302 ? -43.198 11.444 58.039 1.00 20.52 ? 302 TYR A CA 1 ATOM 2311 C C . TYR A 1 302 ? -42.306 10.943 56.924 1.00 20.76 ? 302 TYR A C 1 ATOM 2312 O O . TYR A 1 302 ? -42.540 9.865 56.376 1.00 21.58 ? 302 TYR A O 1 ATOM 2313 C CB . TYR A 1 302 ? -42.944 10.666 59.346 1.00 21.44 ? 302 TYR A CB 1 ATOM 2314 C CG . TYR A 1 302 ? -41.511 10.761 59.804 1.00 20.90 ? 302 TYR A CG 1 ATOM 2315 C CD1 . TYR A 1 302 ? -40.570 9.858 59.354 1.00 22.72 ? 302 TYR A CD1 1 ATOM 2316 C CD2 . TYR A 1 302 ? -41.081 11.773 60.660 1.00 21.42 ? 302 TYR A CD2 1 ATOM 2317 C CE1 . TYR A 1 302 ? -39.255 9.956 59.739 1.00 22.02 ? 302 TYR A CE1 1 ATOM 2318 C CE2 . TYR A 1 302 ? -39.752 11.853 61.062 1.00 22.34 ? 302 TYR A CE2 1 ATOM 2319 C CZ . TYR A 1 302 ? -38.857 10.933 60.584 1.00 22.61 ? 302 TYR A CZ 1 ATOM 2320 O OH . TYR A 1 302 ? -37.520 11.025 60.956 1.00 24.27 ? 302 TYR A OH 1 ATOM 2321 N N . GLY A 1 303 ? -41.277 11.722 56.574 1.00 21.26 ? 303 GLY A N 1 ATOM 2322 C CA . GLY A 1 303 ? -40.270 11.301 55.587 1.00 21.80 ? 303 GLY A CA 1 ATOM 2323 C C . GLY A 1 303 ? -40.509 11.971 54.237 1.00 22.71 ? 303 GLY A C 1 ATOM 2324 O O . GLY A 1 303 ? -41.199 12.987 54.194 1.00 22.58 ? 303 GLY A O 1 ATOM 2325 N N . ALA A 1 304 ? -39.947 11.418 53.156 1.00 22.93 ? 304 ALA A N 1 ATOM 2326 C CA . ALA A 1 304 ? -40.130 11.984 51.808 1.00 23.63 ? 304 ALA A CA 1 ATOM 2327 C C . ALA A 1 304 ? -41.466 11.563 51.260 1.00 23.68 ? 304 ALA A C 1 ATOM 2328 O O . ALA A 1 304 ? -41.631 10.445 50.754 1.00 23.80 ? 304 ALA A O 1 ATOM 2329 C CB . ALA A 1 304 ? -38.994 11.589 50.867 1.00 25.37 ? 304 ALA A CB 1 ATOM 2330 N N . CYS A 1 305 ? -42.439 12.471 51.358 1.00 23.49 ? 305 CYS A N 1 ATOM 2331 C CA . CYS A 1 305 ? -43.832 12.110 51.103 1.00 23.77 ? 305 CYS A CA 1 ATOM 2332 C C . CYS A 1 305 ? -44.480 12.991 50.040 1.00 22.25 ? 305 CYS A C 1 ATOM 2333 O O . CYS A 1 305 ? -44.178 14.188 49.967 1.00 21.50 ? 305 CYS A O 1 ATOM 2334 C CB . CYS A 1 305 ? -44.657 12.281 52.369 1.00 24.33 ? 305 CYS A CB 1 ATOM 2335 S SG . CYS A 1 305 ? -44.268 11.011 53.591 1.00 27.32 ? 305 CYS A SG 1 ATOM 2336 N N . PRO A 1 306 ? -45.366 12.410 49.245 1.00 21.02 ? 306 PRO A N 1 ATOM 2337 C CA . PRO A 1 306 ? -46.229 13.290 48.428 1.00 21.13 ? 306 PRO A CA 1 ATOM 2338 C C . PRO A 1 306 ? -46.979 14.293 49.326 1.00 21.01 ? 306 PRO A C 1 ATOM 2339 O O . PRO A 1 306 ? -47.206 14.011 50.512 1.00 21.20 ? 306 PRO A O 1 ATOM 2340 C CB . PRO A 1 306 ? -47.176 12.316 47.749 1.00 21.20 ? 306 PRO A CB 1 ATOM 2341 C CG . PRO A 1 306 ? -46.507 10.958 47.881 1.00 21.80 ? 306 PRO A CG 1 ATOM 2342 C CD . PRO A 1 306 ? -45.793 11.010 49.163 1.00 21.25 ? 306 PRO A CD 1 ATOM 2343 N N . ARG A 1 307 ? -47.408 15.423 48.751 1.00 20.61 ? 307 ARG A N 1 ATOM 2344 C CA . ARG A 1 307 ? -48.156 16.405 49.493 1.00 19.65 ? 307 ARG A CA 1 ATOM 2345 C C . ARG A 1 307 ? -49.627 15.989 49.578 1.00 18.41 ? 307 ARG A C 1 ATOM 2346 O O . ARG A 1 307 ? -50.230 15.575 48.563 1.00 18.33 ? 307 ARG A O 1 ATOM 2347 C CB . ARG A 1 307 ? -48.041 17.770 48.829 1.00 20.02 ? 307 ARG A CB 1 ATOM 2348 C CG . ARG A 1 307 ? -46.639 18.342 48.998 1.00 21.49 ? 307 ARG A CG 1 ATOM 2349 C CD . ARG A 1 307 ? -46.621 19.823 48.638 1.00 21.50 ? 307 ARG A CD 1 ATOM 2350 N NE . ARG A 1 307 ? -45.302 20.424 48.928 1.00 21.08 ? 307 ARG A NE 1 ATOM 2351 C CZ . ARG A 1 307 ? -44.916 20.899 50.112 1.00 21.44 ? 307 ARG A CZ 1 ATOM 2352 N NH1 . ARG A 1 307 ? -45.667 20.824 51.192 1.00 21.03 ? 307 ARG A NH1 1 ATOM 2353 N NH2 . ARG A 1 307 ? -43.703 21.419 50.228 1.00 22.74 ? 307 ARG A NH2 1 ATOM 2354 N N . TYR A 1 308 ? -50.194 16.134 50.762 1.00 17.95 ? 308 TYR A N 1 ATOM 2355 C CA . TYR A 1 308 ? -51.623 15.873 50.973 1.00 17.93 ? 308 TYR A CA 1 ATOM 2356 C C . TYR A 1 308 ? -52.536 16.858 50.252 1.00 17.88 ? 308 TYR A C 1 ATOM 2357 O O . TYR A 1 308 ? -52.411 18.082 50.396 1.00 17.64 ? 308 TYR A O 1 ATOM 2358 C CB . TYR A 1 308 ? -51.953 15.830 52.444 1.00 18.78 ? 308 TYR A CB 1 ATOM 2359 C CG . TYR A 1 308 ? -53.372 15.393 52.711 1.00 19.45 ? 308 TYR A CG 1 ATOM 2360 C CD1 . TYR A 1 308 ? -53.728 14.044 52.677 1.00 20.12 ? 308 TYR A CD1 1 ATOM 2361 C CD2 . TYR A 1 308 ? -54.358 16.324 52.899 1.00 20.17 ? 308 TYR A CD2 1 ATOM 2362 C CE1 . TYR A 1 308 ? -55.044 13.642 52.919 1.00 21.38 ? 308 TYR A CE1 1 ATOM 2363 C CE2 . TYR A 1 308 ? -55.677 15.947 53.106 1.00 21.82 ? 308 TYR A CE2 1 ATOM 2364 C CZ . TYR A 1 308 ? -56.012 14.603 53.102 1.00 22.88 ? 308 TYR A CZ 1 ATOM 2365 O OH . TYR A 1 308 ? -57.316 14.258 53.302 1.00 24.58 ? 308 TYR A OH 1 ATOM 2366 N N . VAL A 1 309 ? -53.485 16.323 49.492 1.00 17.84 ? 309 VAL A N 1 ATOM 2367 C CA . VAL A 1 309 ? -54.488 17.122 48.826 1.00 17.63 ? 309 VAL A CA 1 ATOM 2368 C C . VAL A 1 309 ? -55.870 16.504 49.094 1.00 18.94 ? 309 VAL A C 1 ATOM 2369 O O . VAL A 1 309 ? -55.978 15.321 49.461 1.00 19.51 ? 309 VAL A O 1 ATOM 2370 C CB . VAL A 1 309 ? -54.235 17.222 47.307 1.00 17.06 ? 309 VAL A CB 1 ATOM 2371 C CG1 . VAL A 1 309 ? -52.896 17.959 47.030 1.00 16.82 ? 309 VAL A CG1 1 ATOM 2372 C CG2 . VAL A 1 309 ? -54.237 15.829 46.649 1.00 16.98 ? 309 VAL A CG2 1 ATOM 2373 N N . LYS A 1 310 ? -56.907 17.258 48.804 1.00 19.89 ? 310 LYS A N 1 ATOM 2374 C CA . LYS A 1 310 ? -58.286 16.762 49.027 1.00 21.46 ? 310 LYS A CA 1 ATOM 2375 C C . LYS A 1 310 ? -58.794 15.865 47.914 1.00 22.38 ? 310 LYS A C 1 ATOM 2376 O O . LYS A 1 310 ? -59.665 15.023 48.154 1.00 21.51 ? 310 LYS A O 1 ATOM 2377 C CB . LYS A 1 310 ? -59.238 17.928 49.231 1.00 24.69 ? 310 LYS A CB 1 ATOM 2378 C CG . LYS A 1 310 ? -59.026 18.635 50.570 1.00 27.70 ? 310 LYS A CG 1 ATOM 2379 C CD . LYS A 1 310 ? -59.895 19.893 50.718 1.00 31.71 ? 310 LYS A CD 1 ATOM 2380 C CE . LYS A 1 310 ? -59.957 20.725 49.442 1.00 33.99 ? 310 LYS A CE 1 ATOM 2381 N NZ . LYS A 1 310 ? -60.251 22.194 49.587 1.00 41.71 ? 310 LYS A NZ 1 ATOM 2382 N N . GLN A 1 311 ? -58.263 16.036 46.709 1.00 21.37 ? 311 GLN A N 1 ATOM 2383 C CA . GLN A 1 311 ? -58.707 15.285 45.537 1.00 21.82 ? 311 GLN A CA 1 ATOM 2384 C C . GLN A 1 311 ? -58.332 13.827 45.711 1.00 23.06 ? 311 GLN A C 1 ATOM 2385 O O . GLN A 1 311 ? -57.245 13.520 46.213 1.00 22.02 ? 311 GLN A O 1 ATOM 2386 C CB . GLN A 1 311 ? -58.036 15.819 44.265 1.00 21.38 ? 311 GLN A CB 1 ATOM 2387 C CG . GLN A 1 311 ? -58.421 17.268 43.902 1.00 21.49 ? 311 GLN A CG 1 ATOM 2388 C CD . GLN A 1 311 ? -57.429 18.290 44.398 1.00 21.53 ? 311 GLN A CD 1 ATOM 2389 O OE1 . GLN A 1 311 ? -56.851 18.140 45.481 1.00 20.35 ? 311 GLN A OE1 1 ATOM 2390 N NE2 . GLN A 1 311 ? -57.246 19.364 43.615 1.00 20.66 ? 311 GLN A NE2 1 ATOM 2391 N N . ASN A 1 312 ? -59.195 12.925 45.258 1.00 23.88 ? 312 ASN A N 1 ATOM 2392 C CA . ASN A 1 312 ? -58.827 11.501 45.287 1.00 26.39 ? 312 ASN A CA 1 ATOM 2393 C C . ASN A 1 312 ? -58.191 11.003 43.990 1.00 25.13 ? 312 ASN A C 1 ATOM 2394 O O . ASN A 1 312 ? -57.705 9.885 43.962 1.00 25.97 ? 312 ASN A O 1 ATOM 2395 C CB . ASN A 1 312 ? -59.996 10.589 45.729 1.00 30.11 ? 312 ASN A CB 1 ATOM 2396 C CG . ASN A 1 312 ? -61.240 10.816 44.941 1.00 34.01 ? 312 ASN A CG 1 ATOM 2397 O OD1 . ASN A 1 312 ? -61.187 11.189 43.781 1.00 39.14 ? 312 ASN A OD1 1 ATOM 2398 N ND2 . ASN A 1 312 ? -62.393 10.607 45.580 1.00 41.73 ? 312 ASN A ND2 1 ATOM 2399 N N . THR A 1 313 ? -58.212 11.836 42.937 1.00 23.83 ? 313 THR A N 1 ATOM 2400 C CA . THR A 1 313 ? -57.589 11.547 41.657 1.00 23.36 ? 313 THR A CA 1 ATOM 2401 C C . THR A 1 313 ? -57.281 12.838 40.917 1.00 22.90 ? 313 THR A C 1 ATOM 2402 O O . THR A 1 313 ? -58.060 13.787 40.954 1.00 22.30 ? 313 THR A O 1 ATOM 2403 C CB . THR A 1 313 ? -58.488 10.631 40.770 1.00 24.39 ? 313 THR A CB 1 ATOM 2404 O OG1 . THR A 1 313 ? -57.857 10.391 39.500 1.00 25.11 ? 313 THR A OG1 1 ATOM 2405 C CG2 . THR A 1 313 ? -59.869 11.260 40.540 1.00 23.95 ? 313 THR A CG2 1 ATOM 2406 N N . LEU A 1 314 ? -56.101 12.891 40.315 1.00 22.27 ? 314 LEU A N 1 ATOM 2407 C CA . LEU A 1 314 ? -55.765 13.913 39.349 1.00 22.58 ? 314 LEU A CA 1 ATOM 2408 C C . LEU A 1 314 ? -54.989 13.246 38.226 1.00 22.90 ? 314 LEU A C 1 ATOM 2409 O O . LEU A 1 314 ? -53.875 12.776 38.439 1.00 22.33 ? 314 LEU A O 1 ATOM 2410 C CB . LEU A 1 314 ? -54.896 14.977 40.013 1.00 22.42 ? 314 LEU A CB 1 ATOM 2411 C CG . LEU A 1 314 ? -55.577 15.925 40.971 1.00 22.93 ? 314 LEU A CG 1 ATOM 2412 C CD1 . LEU A 1 314 ? -54.530 16.667 41.812 1.00 23.94 ? 314 LEU A CD1 1 ATOM 2413 C CD2 . LEU A 1 314 ? -56.455 16.916 40.187 1.00 24.21 ? 314 LEU A CD2 1 ATOM 2414 N N . LYS A 1 315 ? -55.566 13.232 37.034 1.00 22.63 ? 315 LYS A N 1 ATOM 2415 C CA A LYS A 1 315 ? -54.951 12.554 35.907 0.50 23.26 ? 315 LYS A CA 1 ATOM 2416 C CA B LYS A 1 315 ? -54.943 12.546 35.925 0.50 23.18 ? 315 LYS A CA 1 ATOM 2417 C C . LYS A 1 315 ? -54.147 13.513 35.042 1.00 22.56 ? 315 LYS A C 1 ATOM 2418 O O . LYS A 1 315 ? -54.682 14.498 34.519 1.00 22.23 ? 315 LYS A O 1 ATOM 2419 C CB A LYS A 1 315 ? -56.024 11.874 35.061 0.50 24.31 ? 315 LYS A CB 1 ATOM 2420 C CB B LYS A 1 315 ? -56.011 11.788 35.133 0.50 24.13 ? 315 LYS A CB 1 ATOM 2421 C CG A LYS A 1 315 ? -56.759 10.769 35.806 0.50 25.99 ? 315 LYS A CG 1 ATOM 2422 C CG B LYS A 1 315 ? -56.643 10.645 35.940 0.50 25.58 ? 315 LYS A CG 1 ATOM 2423 C CD A LYS A 1 315 ? -55.827 9.606 36.104 0.50 26.76 ? 315 LYS A CD 1 ATOM 2424 C CD B LYS A 1 315 ? -58.062 10.314 35.485 0.50 26.22 ? 315 LYS A CD 1 ATOM 2425 C CE A LYS A 1 315 ? -55.907 8.569 34.991 0.50 28.29 ? 315 LYS A CE 1 ATOM 2426 C CE B LYS A 1 315 ? -58.655 9.129 36.243 0.50 28.03 ? 315 LYS A CE 1 ATOM 2427 N NZ A LYS A 1 315 ? -54.745 7.636 35.007 0.50 30.21 ? 315 LYS A NZ 1 ATOM 2428 N NZ B LYS A 1 315 ? -59.403 9.460 37.493 0.50 27.38 ? 315 LYS A NZ 1 ATOM 2429 N N . LEU A 1 316 ? -52.887 13.196 34.858 1.00 22.34 ? 316 LEU A N 1 ATOM 2430 C CA . LEU A 1 316 ? -52.013 13.949 33.988 1.00 22.27 ? 316 LEU A CA 1 ATOM 2431 C C . LEU A 1 316 ? -51.970 13.276 32.627 1.00 22.28 ? 316 LEU A C 1 ATOM 2432 O O . LEU A 1 316 ? -51.586 12.119 32.545 1.00 22.95 ? 316 LEU A O 1 ATOM 2433 C CB . LEU A 1 316 ? -50.613 13.929 34.574 1.00 22.37 ? 316 LEU A CB 1 ATOM 2434 C CG . LEU A 1 316 ? -49.546 14.720 33.840 1.00 22.25 ? 316 LEU A CG 1 ATOM 2435 C CD1 . LEU A 1 316 ? -49.650 16.221 34.135 1.00 22.28 ? 316 LEU A CD1 1 ATOM 2436 C CD2 . LEU A 1 316 ? -48.163 14.175 34.251 1.00 23.60 ? 316 LEU A CD2 1 ATOM 2437 N N . ALA A 1 317 ? -52.351 13.994 31.578 1.00 22.74 ? 317 ALA A N 1 ATOM 2438 C CA . ALA A 1 317 ? -52.190 13.512 30.196 1.00 23.08 ? 317 ALA A CA 1 ATOM 2439 C C . ALA A 1 317 ? -50.745 13.131 29.853 1.00 23.38 ? 317 ALA A C 1 ATOM 2440 O O . ALA A 1 317 ? -49.820 13.897 30.101 1.00 23.02 ? 317 ALA A O 1 ATOM 2441 C CB . ALA A 1 317 ? -52.709 14.544 29.204 1.00 22.66 ? 317 ALA A CB 1 ATOM 2442 N N . THR A 1 318 ? -50.574 11.927 29.294 1.00 24.26 ? 318 THR A N 1 ATOM 2443 C CA . THR A 1 318 ? -49.301 11.488 28.771 1.00 24.72 ? 318 THR A CA 1 ATOM 2444 C C . THR A 1 318 ? -49.405 11.099 27.278 1.00 26.13 ? 318 THR A C 1 ATOM 2445 O O . THR A 1 318 ? -48.573 10.351 26.760 1.00 28.11 ? 318 THR A O 1 ATOM 2446 C CB . THR A 1 318 ? -48.763 10.317 29.602 1.00 24.76 ? 318 THR A CB 1 ATOM 2447 O OG1 . THR A 1 318 ? -49.700 9.237 29.561 1.00 26.55 ? 318 THR A OG1 1 ATOM 2448 C CG2 . THR A 1 318 ? -48.549 10.757 31.097 1.00 24.77 ? 318 THR A CG2 1 ATOM 2449 N N . GLY A 1 319 ? -50.419 11.609 26.607 1.00 25.76 ? 319 GLY A N 1 ATOM 2450 C CA . GLY A 1 319 ? -50.562 11.456 25.176 1.00 26.54 ? 319 GLY A CA 1 ATOM 2451 C C . GLY A 1 319 ? -51.514 12.504 24.640 1.00 26.68 ? 319 GLY A C 1 ATOM 2452 O O . GLY A 1 319 ? -52.051 13.346 25.399 1.00 26.91 ? 319 GLY A O 1 ATOM 2453 N N . MET A 1 320 ? -51.703 12.482 23.322 1.00 26.03 ? 320 MET A N 1 ATOM 2454 C CA . MET A 1 320 ? -52.484 13.486 22.642 1.00 25.91 ? 320 MET A CA 1 ATOM 2455 C C . MET A 1 320 ? -53.981 13.282 22.768 1.00 25.61 ? 320 MET A C 1 ATOM 2456 O O . MET A 1 320 ? -54.443 12.258 23.266 1.00 26.09 ? 320 MET A O 1 ATOM 2457 C CB . MET A 1 320 ? -52.081 13.549 21.160 1.00 25.74 ? 320 MET A CB 1 ATOM 2458 C CG . MET A 1 320 ? -52.377 12.279 20.391 1.00 25.68 ? 320 MET A CG 1 ATOM 2459 S SD . MET A 1 320 ? -51.901 12.407 18.671 1.00 26.43 ? 320 MET A SD 1 ATOM 2460 C CE . MET A 1 320 ? -50.169 12.100 18.869 1.00 25.06 ? 320 MET A CE 1 ATOM 2461 N N . ARG A 1 321 ? -54.739 14.254 22.294 1.00 26.28 ? 321 ARG A N 1 ATOM 2462 C CA . ARG A 1 321 ? -56.181 14.090 22.156 1.00 27.36 ? 321 ARG A CA 1 ATOM 2463 C C . ARG A 1 321 ? -56.489 12.806 21.368 1.00 27.96 ? 321 ARG A C 1 ATOM 2464 O O . ARG A 1 321 ? -55.807 12.496 20.371 1.00 25.02 ? 321 ARG A O 1 ATOM 2465 C CB . ARG A 1 321 ? -56.850 15.276 21.476 1.00 30.13 ? 321 ARG A CB 1 ATOM 2466 C CG . ARG A 1 321 ? -56.522 15.428 19.986 1.00 34.27 ? 321 ARG A CG 1 ATOM 2467 C CD . ARG A 1 321 ? -57.275 16.569 19.289 1.00 37.84 ? 321 ARG A CD 1 ATOM 2468 N NE . ARG A 1 321 ? -56.806 17.893 19.682 1.00 39.68 ? 321 ARG A NE 1 ATOM 2469 C CZ . ARG A 1 321 ? -57.404 18.691 20.557 1.00 39.37 ? 321 ARG A CZ 1 ATOM 2470 N NH1 . ARG A 1 321 ? -58.521 18.319 21.176 1.00 41.17 ? 321 ARG A NH1 1 ATOM 2471 N NH2 . ARG A 1 321 ? -56.882 19.884 20.807 1.00 41.31 ? 321 ARG A NH2 1 ATOM 2472 N N . ASN A 1 322 ? -57.467 12.057 21.864 1.00 27.50 ? 322 ASN A N 1 ATOM 2473 C CA . ASN A 1 322 ? -57.855 10.792 21.237 1.00 29.67 ? 322 ASN A CA 1 ATOM 2474 C C . ASN A 1 322 ? -59.084 11.054 20.362 1.00 31.59 ? 322 ASN A C 1 ATOM 2475 O O . ASN A 1 322 ? -60.123 11.442 20.869 1.00 30.29 ? 322 ASN A O 1 ATOM 2476 C CB . ASN A 1 322 ? -58.159 9.724 22.280 1.00 29.96 ? 322 ASN A CB 1 ATOM 2477 C CG . ASN A 1 322 ? -58.185 8.319 21.683 1.00 30.97 ? 322 ASN A CG 1 ATOM 2478 O OD1 . ASN A 1 322 ? -57.305 7.941 20.903 1.00 30.78 ? 322 ASN A OD1 1 ATOM 2479 N ND2 . ASN A 1 322 ? -59.179 7.531 22.073 1.00 32.25 ? 322 ASN A ND2 1 ATOM 2480 N N . VAL A 1 323 ? -58.949 10.863 19.049 1.00 33.52 ? 323 VAL A N 1 ATOM 2481 C CA . VAL A 1 323 ? -59.988 11.273 18.102 1.00 34.25 ? 323 VAL A CA 1 ATOM 2482 C C . VAL A 1 323 ? -60.404 10.020 17.314 1.00 36.94 ? 323 VAL A C 1 ATOM 2483 O O . VAL A 1 323 ? -59.552 9.318 16.774 1.00 34.85 ? 323 VAL A O 1 ATOM 2484 C CB . VAL A 1 323 ? -59.504 12.396 17.156 1.00 35.38 ? 323 VAL A CB 1 ATOM 2485 C CG1 . VAL A 1 323 ? -60.661 12.970 16.345 1.00 37.08 ? 323 VAL A CG1 1 ATOM 2486 C CG2 . VAL A 1 323 ? -58.845 13.524 17.945 1.00 33.69 ? 323 VAL A CG2 1 ATOM 2487 N N . PRO A 1 324 ? -61.706 9.704 17.298 1.00 39.79 ? 324 PRO A N 1 ATOM 2488 C CA . PRO A 1 324 ? -62.176 8.537 16.505 1.00 40.50 ? 324 PRO A CA 1 ATOM 2489 C C . PRO A 1 324 ? -61.777 8.626 15.024 1.00 39.22 ? 324 PRO A C 1 ATOM 2490 O O . PRO A 1 324 ? -61.675 9.731 14.462 1.00 38.68 ? 324 PRO A O 1 ATOM 2491 C CB . PRO A 1 324 ? -63.703 8.607 16.649 1.00 41.56 ? 324 PRO A CB 1 ATOM 2492 C CG . PRO A 1 324 ? -63.948 9.386 17.902 1.00 42.80 ? 324 PRO A CG 1 ATOM 2493 C CD . PRO A 1 324 ? -62.806 10.358 18.035 1.00 41.00 ? 324 PRO A CD 1 ATOM 2494 N N . GLU A 1 325 ? -61.525 7.479 14.406 1.00 41.61 ? 325 GLU A N 1 ATOM 2495 C CA . GLU A 1 325 ? -61.342 7.426 12.955 1.00 43.80 ? 325 GLU A CA 1 ATOM 2496 C C . GLU A 1 325 ? -62.697 7.496 12.248 1.00 47.90 ? 325 GLU A C 1 ATOM 2497 O O . GLU A 1 325 ? -63.611 6.755 12.582 1.00 48.17 ? 325 GLU A O 1 ATOM 2498 C CB . GLU A 1 325 ? -60.588 6.164 12.525 1.00 42.47 ? 325 GLU A CB 1 ATOM 2499 C CG . GLU A 1 325 ? -60.121 6.250 11.072 1.00 41.63 ? 325 GLU A CG 1 ATOM 2500 C CD . GLU A 1 325 ? -58.860 5.455 10.784 1.00 41.71 ? 325 GLU A CD 1 ATOM 2501 O OE1 . GLU A 1 325 ? -58.437 4.641 11.640 1.00 40.35 ? 325 GLU A OE1 1 ATOM 2502 O OE2 . GLU A 1 325 ? -58.292 5.649 9.682 1.00 41.02 ? 325 GLU A OE2 1 ATOM 2503 N N . LYS A 1 326 ? -62.827 8.408 11.293 1.00 51.84 ? 326 LYS A N 1 ATOM 2504 C CA . LYS A 1 326 ? -64.041 8.518 10.486 1.00 56.66 ? 326 LYS A CA 1 ATOM 2505 C C . LYS A 1 326 ? -64.282 7.240 9.671 1.00 60.62 ? 326 LYS A C 1 ATOM 2506 O O . LYS A 1 326 ? -63.345 6.667 9.108 1.00 56.47 ? 326 LYS A O 1 ATOM 2507 C CB . LYS A 1 326 ? -63.947 9.728 9.552 1.00 57.36 ? 326 LYS A CB 1 ATOM 2508 C CG . LYS A 1 326 ? -64.216 11.049 10.243 1.00 59.64 ? 326 LYS A CG 1 ATOM 2509 C CD . LYS A 1 326 ? -63.831 12.224 9.353 1.00 63.11 ? 326 LYS A CD 1 ATOM 2510 C CE . LYS A 1 326 ? -64.182 13.563 9.995 1.00 63.53 ? 326 LYS A CE 1 ATOM 2511 N NZ . LYS A 1 326 ? -65.589 13.974 9.743 1.00 64.12 ? 326 LYS A NZ 1 ATOM 2512 N N . GLN A 1 327 ? -65.544 6.811 9.623 1.00 66.76 ? 327 GLN A N 1 ATOM 2513 C CA . GLN A 1 327 ? -65.954 5.568 8.951 1.00 71.51 ? 327 GLN A CA 1 ATOM 2514 C C . GLN A 1 327 ? -66.524 5.854 7.556 1.00 72.21 ? 327 GLN A C 1 ATOM 2515 O O . GLN A 1 327 ? -65.877 6.492 6.721 1.00 68.98 ? 327 GLN A O 1 ATOM 2516 C CB . GLN A 1 327 ? -66.996 4.836 9.814 1.00 76.33 ? 327 GLN A CB 1 ATOM 2517 C CG . GLN A 1 327 ? -67.694 3.651 9.147 1.00 80.75 ? 327 GLN A CG 1 ATOM 2518 C CD . GLN A 1 327 ? -68.718 2.977 10.054 1.00 82.39 ? 327 GLN A CD 1 ATOM 2519 O OE1 . GLN A 1 327 ? -68.509 2.848 11.264 1.00 82.58 ? 327 GLN A OE1 1 ATOM 2520 N NE2 . GLN A 1 327 ? -69.830 2.538 9.468 1.00 82.74 ? 327 GLN A NE2 1 ATOM 2521 N N . ALA A 1 334 ? -61.310 6.283 0.367 1.00 53.37 ? 334 ALA A N 1 ATOM 2522 C CA . ALA A 1 334 ? -60.171 7.141 0.098 1.00 52.69 ? 334 ALA A CA 1 ATOM 2523 C C . ALA A 1 334 ? -59.541 7.527 1.436 1.00 51.17 ? 334 ALA A C 1 ATOM 2524 O O . ALA A 1 334 ? -60.242 7.747 2.429 1.00 54.36 ? 334 ALA A O 1 ATOM 2525 C CB . ALA A 1 334 ? -60.591 8.385 -0.679 1.00 54.08 ? 334 ALA A CB 1 ATOM 2526 N N . ILE A 1 335 ? -58.216 7.594 1.457 1.00 45.60 ? 335 ILE A N 1 ATOM 2527 C CA . ILE A 1 335 ? -57.494 7.898 2.684 1.00 40.80 ? 335 ILE A CA 1 ATOM 2528 C C . ILE A 1 335 ? -57.794 9.324 3.128 1.00 38.78 ? 335 ILE A C 1 ATOM 2529 O O . ILE A 1 335 ? -58.235 10.150 2.337 1.00 38.05 ? 335 ILE A O 1 ATOM 2530 C CB . ILE A 1 335 ? -55.985 7.625 2.536 1.00 39.31 ? 335 ILE A CB 1 ATOM 2531 C CG1 . ILE A 1 335 ? -55.385 8.378 1.344 1.00 38.93 ? 335 ILE A CG1 1 ATOM 2532 C CG2 . ILE A 1 335 ? -55.745 6.128 2.361 1.00 39.09 ? 335 ILE A CG2 1 ATOM 2533 C CD1 . ILE A 1 335 ? -53.876 8.345 1.335 1.00 38.97 ? 335 ILE A CD1 1 ATOM 2534 N N . ALA A 1 336 ? -57.584 9.598 4.407 1.00 36.12 ? 336 ALA A N 1 ATOM 2535 C CA . ALA A 1 336 ? -57.919 10.900 4.989 1.00 35.40 ? 336 ALA A CA 1 ATOM 2536 C C . ALA A 1 336 ? -56.914 11.245 6.081 1.00 33.81 ? 336 ALA A C 1 ATOM 2537 O O . ALA A 1 336 ? -56.367 10.368 6.720 1.00 33.84 ? 336 ALA A O 1 ATOM 2538 C CB . ALA A 1 336 ? -59.347 10.877 5.527 1.00 35.64 ? 336 ALA A CB 1 ATOM 2539 N N . GLY A 1 337 ? -56.671 12.536 6.268 1.00 33.92 ? 337 GLY A N 1 ATOM 2540 C CA . GLY A 1 337 ? -55.622 13.045 7.131 1.00 32.51 ? 337 GLY A CA 1 ATOM 2541 C C . GLY A 1 337 ? -56.184 13.418 8.481 1.00 31.46 ? 337 GLY A C 1 ATOM 2542 O O . GLY A 1 337 ? -57.319 13.087 8.773 1.00 31.04 ? 337 GLY A O 1 ATOM 2543 N N . PHE A 1 338 ? -55.402 14.173 9.254 1.00 31.48 ? 338 PHE A N 1 ATOM 2544 C CA . PHE A 1 338 ? -55.717 14.453 10.657 1.00 32.41 ? 338 PHE A CA 1 ATOM 2545 C C . PHE A 1 338 ? -56.917 15.351 10.942 1.00 34.03 ? 338 PHE A C 1 ATOM 2546 O O . PHE A 1 338 ? -57.282 15.494 12.108 1.00 34.95 ? 338 PHE A O 1 ATOM 2547 C CB . PHE A 1 338 ? -54.496 15.003 11.403 1.00 32.00 ? 338 PHE A CB 1 ATOM 2548 C CG . PHE A 1 338 ? -54.089 16.400 10.993 1.00 33.41 ? 338 PHE A CG 1 ATOM 2549 C CD1 . PHE A 1 338 ? -53.217 16.604 9.940 1.00 33.30 ? 338 PHE A CD1 1 ATOM 2550 C CD2 . PHE A 1 338 ? -54.574 17.514 11.674 1.00 34.90 ? 338 PHE A CD2 1 ATOM 2551 C CE1 . PHE A 1 338 ? -52.833 17.882 9.561 1.00 34.73 ? 338 PHE A CE1 1 ATOM 2552 C CE2 . PHE A 1 338 ? -54.192 18.796 11.305 1.00 35.23 ? 338 PHE A CE2 1 ATOM 2553 C CZ . PHE A 1 338 ? -53.326 18.986 10.234 1.00 35.19 ? 338 PHE A CZ 1 ATOM 2554 N N . ILE A 1 339 ? -57.504 15.996 9.934 1.00 34.41 ? 339 ILE A N 1 ATOM 2555 C CA . ILE A 1 339 ? -58.568 16.960 10.222 1.00 37.85 ? 339 ILE A CA 1 ATOM 2556 C C . ILE A 1 339 ? -59.814 16.219 10.749 1.00 38.37 ? 339 ILE A C 1 ATOM 2557 O O . ILE A 1 339 ? -60.449 15.470 10.021 1.00 38.13 ? 339 ILE A O 1 ATOM 2558 C CB . ILE A 1 339 ? -58.893 17.845 9.005 1.00 38.21 ? 339 ILE A CB 1 ATOM 2559 C CG1 . ILE A 1 339 ? -57.689 18.719 8.665 1.00 38.84 ? 339 ILE A CG1 1 ATOM 2560 C CG2 . ILE A 1 339 ? -60.142 18.692 9.255 1.00 40.51 ? 339 ILE A CG2 1 ATOM 2561 C CD1 . ILE A 1 339 ? -57.276 19.677 9.763 1.00 39.75 ? 339 ILE A CD1 1 ATOM 2562 N N . GLU A 1 340 ? -60.110 16.419 12.038 1.00 41.29 ? 340 GLU A N 1 ATOM 2563 C CA . GLU A 1 340 ? -61.168 15.679 12.764 1.00 44.29 ? 340 GLU A CA 1 ATOM 2564 C C . GLU A 1 340 ? -61.122 14.151 12.577 1.00 41.88 ? 340 GLU A C 1 ATOM 2565 O O . GLU A 1 340 ? -62.134 13.504 12.413 1.00 42.44 ? 340 GLU A O 1 ATOM 2566 C CB . GLU A 1 340 ? -62.552 16.221 12.391 1.00 48.09 ? 340 GLU A CB 1 ATOM 2567 C CG . GLU A 1 340 ? -62.741 17.698 12.734 1.00 53.12 ? 340 GLU A CG 1 ATOM 2568 C CD . GLU A 1 340 ? -63.814 18.352 11.874 1.00 59.45 ? 340 GLU A CD 1 ATOM 2569 O OE1 . GLU A 1 340 ? -63.730 18.252 10.624 1.00 65.25 ? 340 GLU A OE1 1 ATOM 2570 O OE2 . GLU A 1 340 ? -64.751 18.956 12.440 1.00 61.59 ? 340 GLU A OE2 1 ATOM 2571 N N . ASN A 1 341 ? -59.932 13.577 12.661 1.00 41.77 ? 341 ASN A N 1 ATOM 2572 C CA . ASN A 1 341 ? -59.730 12.189 12.276 1.00 38.69 ? 341 ASN A CA 1 ATOM 2573 C C . ASN A 1 341 ? -58.433 11.637 12.845 1.00 37.89 ? 341 ASN A C 1 ATOM 2574 O O . ASN A 1 341 ? -57.362 12.184 12.576 1.00 40.21 ? 341 ASN A O 1 ATOM 2575 C CB . ASN A 1 341 ? -59.688 12.115 10.750 1.00 39.30 ? 341 ASN A CB 1 ATOM 2576 C CG . ASN A 1 341 ? -59.581 10.684 10.234 1.00 40.06 ? 341 ASN A CG 1 ATOM 2577 O OD1 . ASN A 1 341 ? -58.701 10.358 9.413 1.00 38.53 ? 341 ASN A OD1 1 ATOM 2578 N ND2 . ASN A 1 341 ? -60.456 9.816 10.733 1.00 37.48 ? 341 ASN A ND2 1 ATOM 2579 N N . GLY A 1 342 ? -58.526 10.593 13.663 1.00 35.00 ? 342 GLY A N 1 ATOM 2580 C CA . GLY A 1 342 ? -57.359 9.881 14.149 1.00 34.63 ? 342 GLY A CA 1 ATOM 2581 C C . GLY A 1 342 ? -57.203 8.537 13.453 1.00 34.13 ? 342 GLY A C 1 ATOM 2582 O O . GLY A 1 342 ? -58.135 8.042 12.857 1.00 35.04 ? 342 GLY A O 1 ATOM 2583 N N . TRP A 1 343 ? -56.026 7.940 13.559 1.00 34.21 ? 343 TRP A N 1 ATOM 2584 C CA . TRP A 1 343 ? -55.709 6.694 12.867 1.00 33.43 ? 343 TRP A CA 1 ATOM 2585 C C . TRP A 1 343 ? -55.503 5.577 13.838 1.00 35.35 ? 343 TRP A C 1 ATOM 2586 O O . TRP A 1 343 ? -54.434 5.430 14.419 1.00 34.12 ? 343 TRP A O 1 ATOM 2587 C CB . TRP A 1 343 ? -54.442 6.871 12.051 1.00 31.44 ? 343 TRP A CB 1 ATOM 2588 C CG . TRP A 1 343 ? -54.555 7.767 10.834 1.00 29.58 ? 343 TRP A CG 1 ATOM 2589 C CD1 . TRP A 1 343 ? -55.695 8.263 10.213 1.00 28.66 ? 343 TRP A CD1 1 ATOM 2590 C CD2 . TRP A 1 343 ? -53.442 8.233 10.022 1.00 28.74 ? 343 TRP A CD2 1 ATOM 2591 N NE1 . TRP A 1 343 ? -55.365 9.010 9.110 1.00 28.13 ? 343 TRP A NE1 1 ATOM 2592 C CE2 . TRP A 1 343 ? -54.017 9.046 8.960 1.00 27.72 ? 343 TRP A CE2 1 ATOM 2593 C CE3 . TRP A 1 343 ? -52.068 8.100 10.102 1.00 28.37 ? 343 TRP A CE3 1 ATOM 2594 C CZ2 . TRP A 1 343 ? -53.238 9.639 8.002 1.00 27.73 ? 343 TRP A CZ2 1 ATOM 2595 C CZ3 . TRP A 1 343 ? -51.290 8.710 9.129 1.00 28.36 ? 343 TRP A CZ3 1 ATOM 2596 C CH2 . TRP A 1 343 ? -51.863 9.463 8.107 1.00 28.12 ? 343 TRP A CH2 1 ATOM 2597 N N . GLU A 1 344 ? -56.520 4.751 14.028 1.00 39.04 ? 344 GLU A N 1 ATOM 2598 C CA . GLU A 1 344 ? -56.369 3.660 14.992 1.00 42.04 ? 344 GLU A CA 1 ATOM 2599 C C . GLU A 1 344 ? -55.353 2.615 14.532 1.00 41.31 ? 344 GLU A C 1 ATOM 2600 O O . GLU A 1 344 ? -54.647 2.036 15.351 1.00 39.61 ? 344 GLU A O 1 ATOM 2601 C CB . GLU A 1 344 ? -57.730 3.072 15.355 1.00 46.14 ? 344 GLU A CB 1 ATOM 2602 C CG . GLU A 1 344 ? -58.528 4.077 16.172 1.00 48.97 ? 344 GLU A CG 1 ATOM 2603 C CD . GLU A 1 344 ? -59.897 3.599 16.609 1.00 55.44 ? 344 GLU A CD 1 ATOM 2604 O OE1 . GLU A 1 344 ? -59.979 2.544 17.293 1.00 57.31 ? 344 GLU A OE1 1 ATOM 2605 O OE2 . GLU A 1 344 ? -60.884 4.310 16.279 1.00 57.83 ? 344 GLU A OE2 1 ATOM 2606 N N . GLY A 1 345 ? -55.216 2.443 13.221 1.00 41.64 ? 345 GLY A N 1 ATOM 2607 C CA . GLY A 1 345 ? -54.196 1.540 12.664 1.00 42.02 ? 345 GLY A CA 1 ATOM 2608 C C . GLY A 1 345 ? -52.743 1.975 12.732 1.00 42.37 ? 345 GLY A C 1 ATOM 2609 O O . GLY A 1 345 ? -51.856 1.226 12.323 1.00 41.98 ? 345 GLY A O 1 ATOM 2610 N N . MET A 1 346 ? -52.477 3.180 13.242 1.00 41.93 ? 346 MET A N 1 ATOM 2611 C CA . MET A 1 346 ? -51.110 3.691 13.394 1.00 43.34 ? 346 MET A CA 1 ATOM 2612 C C . MET A 1 346 ? -50.571 3.252 14.762 1.00 43.54 ? 346 MET A C 1 ATOM 2613 O O . MET A 1 346 ? -50.878 3.890 15.769 1.00 40.45 ? 346 MET A O 1 ATOM 2614 C CB . MET A 1 346 ? -51.158 5.233 13.264 1.00 45.21 ? 346 MET A CB 1 ATOM 2615 C CG . MET A 1 346 ? -49.899 6.039 13.534 1.00 47.23 ? 346 MET A CG 1 ATOM 2616 S SD . MET A 1 346 ? -48.860 6.297 12.093 1.00 51.78 ? 346 MET A SD 1 ATOM 2617 C CE . MET A 1 346 ? -47.526 5.191 12.510 1.00 52.54 ? 346 MET A CE 1 ATOM 2618 N N . VAL A 1 347 ? -49.767 2.186 14.801 1.00 43.07 ? 347 VAL A N 1 ATOM 2619 C CA . VAL A 1 347 ? -49.324 1.567 16.063 1.00 44.82 ? 347 VAL A CA 1 ATOM 2620 C C . VAL A 1 347 ? -47.808 1.621 16.336 1.00 44.95 ? 347 VAL A C 1 ATOM 2621 O O . VAL A 1 347 ? -47.372 1.305 17.444 1.00 48.62 ? 347 VAL A O 1 ATOM 2622 C CB . VAL A 1 347 ? -49.800 0.091 16.169 1.00 48.16 ? 347 VAL A CB 1 ATOM 2623 C CG1 . VAL A 1 347 ? -51.321 0.023 16.212 1.00 48.18 ? 347 VAL A CG1 1 ATOM 2624 C CG2 . VAL A 1 347 ? -49.258 -0.751 15.010 1.00 47.83 ? 347 VAL A CG2 1 ATOM 2625 N N . ASP A 1 348 ? -47.005 2.013 15.352 1.00 43.64 ? 348 ASP A N 1 ATOM 2626 C CA . ASP A 1 348 ? -45.558 2.106 15.531 1.00 43.68 ? 348 ASP A CA 1 ATOM 2627 C C . ASP A 1 348 ? -45.078 3.550 15.604 1.00 41.63 ? 348 ASP A C 1 ATOM 2628 O O . ASP A 1 348 ? -43.878 3.811 15.596 1.00 41.66 ? 348 ASP A O 1 ATOM 2629 C CB . ASP A 1 348 ? -44.823 1.368 14.413 1.00 47.80 ? 348 ASP A CB 1 ATOM 2630 C CG . ASP A 1 348 ? -45.099 1.948 13.044 1.00 50.97 ? 348 ASP A CG 1 ATOM 2631 O OD1 . ASP A 1 348 ? -46.177 2.564 12.835 1.00 51.28 ? 348 ASP A OD1 1 ATOM 2632 O OD2 . ASP A 1 348 ? -44.224 1.768 12.170 1.00 56.22 ? 348 ASP A OD2 1 ATOM 2633 N N . GLY A 1 349 ? -46.016 4.483 15.706 1.00 38.36 ? 349 GLY A N 1 ATOM 2634 C CA . GLY A 1 349 ? -45.666 5.897 15.837 1.00 35.26 ? 349 GLY A CA 1 ATOM 2635 C C . GLY A 1 349 ? -46.860 6.726 16.272 1.00 32.70 ? 349 GLY A C 1 ATOM 2636 O O . GLY A 1 349 ? -47.998 6.269 16.220 1.00 32.24 ? 349 GLY A O 1 ATOM 2637 N N . TRP A 1 350 ? -46.604 7.963 16.696 1.00 30.51 ? 350 TRP A N 1 ATOM 2638 C CA . TRP A 1 350 ? -47.682 8.872 17.077 1.00 29.10 ? 350 TRP A CA 1 ATOM 2639 C C . TRP A 1 350 ? -48.195 9.698 15.955 1.00 27.75 ? 350 TRP A C 1 ATOM 2640 O O . TRP A 1 350 ? -49.350 10.082 15.975 1.00 27.02 ? 350 TRP A O 1 ATOM 2641 C CB . TRP A 1 350 ? -47.215 9.799 18.167 1.00 29.00 ? 350 TRP A CB 1 ATOM 2642 C CG . TRP A 1 350 ? -47.167 9.136 19.506 1.00 29.68 ? 350 TRP A CG 1 ATOM 2643 C CD1 . TRP A 1 350 ? -47.097 7.775 19.797 1.00 30.77 ? 350 TRP A CD1 1 ATOM 2644 C CD2 . TRP A 1 350 ? -47.154 9.809 20.792 1.00 29.08 ? 350 TRP A CD2 1 ATOM 2645 N NE1 . TRP A 1 350 ? -47.075 7.572 21.146 1.00 31.53 ? 350 TRP A NE1 1 ATOM 2646 C CE2 . TRP A 1 350 ? -47.093 8.759 21.801 1.00 29.99 ? 350 TRP A CE2 1 ATOM 2647 C CE3 . TRP A 1 350 ? -47.202 11.136 21.192 1.00 29.10 ? 350 TRP A CE3 1 ATOM 2648 C CZ2 . TRP A 1 350 ? -47.088 9.047 23.153 1.00 30.14 ? 350 TRP A CZ2 1 ATOM 2649 C CZ3 . TRP A 1 350 ? -47.180 11.417 22.567 1.00 28.66 ? 350 TRP A CZ3 1 ATOM 2650 C CH2 . TRP A 1 350 ? -47.128 10.402 23.514 1.00 28.73 ? 350 TRP A CH2 1 ATOM 2651 N N . TYR A 1 351 ? -47.316 10.011 15.004 1.00 27.39 ? 351 TYR A N 1 ATOM 2652 C CA . TYR A 1 351 ? -47.633 10.797 13.836 1.00 27.05 ? 351 TYR A CA 1 ATOM 2653 C C . TYR A 1 351 ? -47.097 10.051 12.620 1.00 28.18 ? 351 TYR A C 1 ATOM 2654 O O . TYR A 1 351 ? -46.128 9.311 12.741 1.00 28.34 ? 351 TYR A O 1 ATOM 2655 C CB . TYR A 1 351 ? -46.935 12.130 13.887 1.00 27.46 ? 351 TYR A CB 1 ATOM 2656 C CG . TYR A 1 351 ? -47.221 12.900 15.162 1.00 26.76 ? 351 TYR A CG 1 ATOM 2657 C CD1 . TYR A 1 351 ? -48.340 13.705 15.249 1.00 26.46 ? 351 TYR A CD1 1 ATOM 2658 C CD2 . TYR A 1 351 ? -46.402 12.773 16.284 1.00 26.42 ? 351 TYR A CD2 1 ATOM 2659 C CE1 . TYR A 1 351 ? -48.623 14.417 16.417 1.00 26.23 ? 351 TYR A CE1 1 ATOM 2660 C CE2 . TYR A 1 351 ? -46.668 13.502 17.456 1.00 26.76 ? 351 TYR A CE2 1 ATOM 2661 C CZ . TYR A 1 351 ? -47.787 14.296 17.509 1.00 26.18 ? 351 TYR A CZ 1 ATOM 2662 O OH . TYR A 1 351 ? -48.091 15.003 18.656 1.00 28.04 ? 351 TYR A OH 1 ATOM 2663 N N . GLY A 1 352 ? -47.707 10.258 11.462 1.00 28.25 ? 352 GLY A N 1 ATOM 2664 C CA . GLY A 1 352 ? -47.199 9.623 10.243 1.00 29.18 ? 352 GLY A CA 1 ATOM 2665 C C . GLY A 1 352 ? -47.860 10.071 8.968 1.00 29.56 ? 352 GLY A C 1 ATOM 2666 O O . GLY A 1 352 ? -48.604 11.052 8.930 1.00 27.90 ? 352 GLY A O 1 ATOM 2667 N N . PHE A 1 353 ? -47.620 9.274 7.929 1.00 29.51 ? 353 PHE A N 1 ATOM 2668 C CA . PHE A 1 353 ? -48.012 9.574 6.579 1.00 30.26 ? 353 PHE A CA 1 ATOM 2669 C C . PHE A 1 353 ? -48.799 8.394 6.066 1.00 29.84 ? 353 PHE A C 1 ATOM 2670 O O . PHE A 1 353 ? -48.438 7.246 6.356 1.00 30.52 ? 353 PHE A O 1 ATOM 2671 C CB . PHE A 1 353 ? -46.767 9.673 5.691 1.00 31.04 ? 353 PHE A CB 1 ATOM 2672 C CG . PHE A 1 353 ? -45.818 10.785 6.041 1.00 32.04 ? 353 PHE A CG 1 ATOM 2673 C CD1 . PHE A 1 353 ? -45.942 12.026 5.438 1.00 32.09 ? 353 PHE A CD1 1 ATOM 2674 C CD2 . PHE A 1 353 ? -44.748 10.575 6.903 1.00 32.12 ? 353 PHE A CD2 1 ATOM 2675 C CE1 . PHE A 1 353 ? -45.034 13.037 5.707 1.00 32.86 ? 353 PHE A CE1 1 ATOM 2676 C CE2 . PHE A 1 353 ? -43.844 11.591 7.190 1.00 33.35 ? 353 PHE A CE2 1 ATOM 2677 C CZ . PHE A 1 353 ? -43.984 12.824 6.585 1.00 33.69 ? 353 PHE A CZ 1 ATOM 2678 N N . ARG A 1 354 ? -49.862 8.657 5.316 1.00 29.62 ? 354 ARG A N 1 ATOM 2679 C CA . ARG A 1 354 ? -50.508 7.645 4.480 1.00 29.59 ? 354 ARG A CA 1 ATOM 2680 C C . ARG A 1 354 ? -50.511 8.152 3.050 1.00 29.68 ? 354 ARG A C 1 ATOM 2681 O O . ARG A 1 354 ? -50.621 9.356 2.798 1.00 29.92 ? 354 ARG A O 1 ATOM 2682 C CB . ARG A 1 354 ? -51.929 7.367 4.928 1.00 30.11 ? 354 ARG A CB 1 ATOM 2683 C CG . ARG A 1 354 ? -52.010 6.429 6.115 1.00 31.23 ? 354 ARG A CG 1 ATOM 2684 C CD . ARG A 1 354 ? -53.431 6.142 6.531 1.00 31.84 ? 354 ARG A CD 1 ATOM 2685 N NE . ARG A 1 354 ? -53.462 5.332 7.740 1.00 32.04 ? 354 ARG A NE 1 ATOM 2686 C CZ . ARG A 1 354 ? -54.552 5.041 8.445 1.00 31.83 ? 354 ARG A CZ 1 ATOM 2687 N NH1 . ARG A 1 354 ? -55.730 5.495 8.106 1.00 32.27 ? 354 ARG A NH1 1 ATOM 2688 N NH2 . ARG A 1 354 ? -54.442 4.288 9.520 1.00 33.54 ? 354 ARG A NH2 1 ATOM 2689 N N . HIS A 1 355 ? -50.374 7.250 2.087 1.00 29.85 ? 355 HIS A N 1 ATOM 2690 C CA . HIS A 1 355 ? -50.303 7.687 0.705 1.00 30.24 ? 355 HIS A CA 1 ATOM 2691 C C . HIS A 1 355 ? -51.084 6.784 -0.159 1.00 31.37 ? 355 HIS A C 1 ATOM 2692 O O . HIS A 1 355 ? -51.346 5.634 0.215 1.00 30.68 ? 355 HIS A O 1 ATOM 2693 C CB . HIS A 1 355 ? -48.836 7.766 0.257 1.00 30.85 ? 355 HIS A CB 1 ATOM 2694 C CG . HIS A 1 355 ? -48.156 6.403 0.140 1.00 31.93 ? 355 HIS A CG 1 ATOM 2695 N ND1 . HIS A 1 355 ? -47.379 5.898 1.120 1.00 31.88 ? 355 HIS A ND1 1 ATOM 2696 C CD2 . HIS A 1 355 ? -48.194 5.434 -0.878 1.00 32.95 ? 355 HIS A CD2 1 ATOM 2697 C CE1 . HIS A 1 355 ? -46.936 4.670 0.755 1.00 33.82 ? 355 HIS A CE1 1 ATOM 2698 N NE2 . HIS A 1 355 ? -47.435 4.390 -0.469 1.00 32.86 ? 355 HIS A NE2 1 ATOM 2699 N N . GLN A 1 356 ? -51.514 7.319 -1.299 1.00 32.41 ? 356 GLN A N 1 ATOM 2700 C CA . GLN A 1 356 ? -52.058 6.561 -2.406 1.00 33.82 ? 356 GLN A CA 1 ATOM 2701 C C . GLN A 1 356 ? -51.298 6.959 -3.671 1.00 33.44 ? 356 GLN A C 1 ATOM 2702 O O . GLN A 1 356 ? -51.180 8.155 -3.991 1.00 31.59 ? 356 GLN A O 1 ATOM 2703 C CB . GLN A 1 356 ? -53.550 6.862 -2.572 1.00 36.56 ? 356 GLN A CB 1 ATOM 2704 C CG . GLN A 1 356 ? -54.254 5.989 -3.601 1.00 40.38 ? 356 GLN A CG 1 ATOM 2705 C CD . GLN A 1 356 ? -55.754 6.188 -3.608 1.00 44.15 ? 356 GLN A CD 1 ATOM 2706 O OE1 . GLN A 1 356 ? -56.498 5.322 -4.061 1.00 52.71 ? 356 GLN A OE1 1 ATOM 2707 N NE2 . GLN A 1 356 ? -56.208 7.335 -3.118 1.00 49.18 ? 356 GLN A NE2 1 ATOM 2708 N N . ASN A 1 357 ? -50.762 5.965 -4.379 1.00 33.08 ? 357 ASN A N 1 ATOM 2709 C CA . ASN A 1 357 ? -50.037 6.203 -5.615 1.00 33.03 ? 357 ASN A CA 1 ATOM 2710 C C . ASN A 1 357 ? -50.263 5.008 -6.544 1.00 35.41 ? 357 ASN A C 1 ATOM 2711 O O . ASN A 1 357 ? -51.161 4.187 -6.292 1.00 32.90 ? 357 ASN A O 1 ATOM 2712 C CB . ASN A 1 357 ? -48.548 6.483 -5.339 1.00 33.63 ? 357 ASN A CB 1 ATOM 2713 C CG . ASN A 1 357 ? -47.791 5.290 -4.746 1.00 33.10 ? 357 ASN A CG 1 ATOM 2714 O OD1 . ASN A 1 357 ? -48.285 4.143 -4.711 1.00 33.10 ? 357 ASN A OD1 1 ATOM 2715 N ND2 . ASN A 1 357 ? -46.560 5.543 -4.348 1.00 32.13 ? 357 ASN A ND2 1 ATOM 2716 N N . SER A 1 358 ? -49.490 4.975 -7.633 1.00 38.23 ? 358 SER A N 1 ATOM 2717 C CA . SER A 1 358 ? -49.501 3.905 -8.635 1.00 41.46 ? 358 SER A CA 1 ATOM 2718 C C . SER A 1 358 ? -49.332 2.514 -8.043 1.00 41.48 ? 358 SER A C 1 ATOM 2719 O O . SER A 1 358 ? -49.875 1.554 -8.591 1.00 44.84 ? 358 SER A O 1 ATOM 2720 C CB . SER A 1 358 ? -48.364 4.153 -9.661 1.00 43.09 ? 358 SER A CB 1 ATOM 2721 O OG . SER A 1 358 ? -47.247 4.821 -9.036 1.00 46.46 ? 358 SER A OG 1 ATOM 2722 N N . GLU A 1 359 ? -48.569 2.423 -6.955 1.00 40.56 ? 359 GLU A N 1 ATOM 2723 C CA . GLU A 1 359 ? -48.141 1.164 -6.347 1.00 41.19 ? 359 GLU A CA 1 ATOM 2724 C C . GLU A 1 359 ? -49.002 0.691 -5.146 1.00 40.29 ? 359 GLU A C 1 ATOM 2725 O O . GLU A 1 359 ? -48.721 -0.371 -4.583 1.00 40.52 ? 359 GLU A O 1 ATOM 2726 C CB . GLU A 1 359 ? -46.675 1.284 -5.915 1.00 42.02 ? 359 GLU A CB 1 ATOM 2727 C CG . GLU A 1 359 ? -45.731 1.700 -7.047 1.00 44.68 ? 359 GLU A CG 1 ATOM 2728 C CD . GLU A 1 359 ? -44.255 1.552 -6.699 1.00 46.55 ? 359 GLU A CD 1 ATOM 2729 O OE1 . GLU A 1 359 ? -43.721 0.420 -6.742 1.00 50.43 ? 359 GLU A OE1 1 ATOM 2730 O OE2 . GLU A 1 359 ? -43.596 2.561 -6.381 1.00 47.82 ? 359 GLU A OE2 1 ATOM 2731 N N . GLY A 1 360 ? -50.024 1.467 -4.762 1.00 36.84 ? 360 GLY A N 1 ATOM 2732 C CA . GLY A 1 360 ? -50.970 1.077 -3.713 1.00 35.34 ? 360 GLY A CA 1 ATOM 2733 C C . GLY A 1 360 ? -51.192 2.176 -2.667 1.00 34.49 ? 360 GLY A C 1 ATOM 2734 O O . GLY A 1 360 ? -51.019 3.356 -2.964 1.00 32.62 ? 360 GLY A O 1 ATOM 2735 N N . ILE A 1 361 ? -51.578 1.753 -1.468 1.00 34.18 ? 361 ILE A N 1 ATOM 2736 C CA . ILE A 1 361 ? -51.877 2.635 -0.332 1.00 35.31 ? 361 ILE A CA 1 ATOM 2737 C C . ILE A 1 361 ? -51.029 2.171 0.817 1.00 35.08 ? 361 ILE A C 1 ATOM 2738 O O . ILE A 1 361 ? -51.011 0.980 1.125 1.00 35.08 ? 361 ILE A O 1 ATOM 2739 C CB . ILE A 1 361 ? -53.350 2.523 0.106 1.00 36.49 ? 361 ILE A CB 1 ATOM 2740 C CG1 . ILE A 1 361 ? -54.250 3.204 -0.901 1.00 37.54 ? 361 ILE A CG1 1 ATOM 2741 C CG2 . ILE A 1 361 ? -53.563 3.146 1.496 1.00 38.34 ? 361 ILE A CG2 1 ATOM 2742 C CD1 . ILE A 1 361 ? -55.056 2.268 -1.747 1.00 40.22 ? 361 ILE A CD1 1 ATOM 2743 N N . GLY A 1 362 ? -50.315 3.091 1.445 1.00 33.52 ? 362 GLY A N 1 ATOM 2744 C CA . GLY A 1 362 ? -49.361 2.719 2.472 1.00 33.81 ? 362 GLY A CA 1 ATOM 2745 C C . GLY A 1 362 ? -49.409 3.668 3.655 1.00 34.16 ? 362 GLY A C 1 ATOM 2746 O O . GLY A 1 362 ? -50.063 4.716 3.597 1.00 32.68 ? 362 GLY A O 1 ATOM 2747 N N . GLN A 1 363 ? -48.686 3.277 4.698 1.00 34.67 ? 363 GLN A N 1 ATOM 2748 C CA . GLN A 1 363 ? -48.564 4.022 5.937 1.00 34.57 ? 363 GLN A CA 1 ATOM 2749 C C . GLN A 1 363 ? -47.136 3.905 6.429 1.00 35.17 ? 363 GLN A C 1 ATOM 2750 O O . GLN A 1 363 ? -46.524 2.842 6.317 1.00 34.17 ? 363 GLN A O 1 ATOM 2751 C CB . GLN A 1 363 ? -49.536 3.434 6.952 1.00 35.79 ? 363 GLN A CB 1 ATOM 2752 C CG . GLN A 1 363 ? -49.535 4.082 8.325 1.00 37.16 ? 363 GLN A CG 1 ATOM 2753 C CD . GLN A 1 363 ? -50.627 3.481 9.187 1.00 37.78 ? 363 GLN A CD 1 ATOM 2754 O OE1 . GLN A 1 363 ? -51.788 3.843 9.056 1.00 39.49 ? 363 GLN A OE1 1 ATOM 2755 N NE2 . GLN A 1 363 ? -50.267 2.521 10.036 1.00 40.67 ? 363 GLN A NE2 1 ATOM 2756 N N . ALA A 1 364 ? -46.596 4.999 6.973 1.00 33.36 ? 364 ALA A N 1 ATOM 2757 C CA . ALA A 1 364 ? -45.308 5.013 7.655 1.00 33.03 ? 364 ALA A CA 1 ATOM 2758 C C . ALA A 1 364 ? -45.356 6.042 8.796 1.00 33.14 ? 364 ALA A C 1 ATOM 2759 O O . ALA A 1 364 ? -45.858 7.152 8.619 1.00 30.29 ? 364 ALA A O 1 ATOM 2760 C CB . ALA A 1 364 ? -44.186 5.389 6.702 1.00 32.89 ? 364 ALA A CB 1 ATOM 2761 N N . ALA A 1 365 ? -44.793 5.661 9.936 1.00 34.78 ? 365 ALA A N 1 ATOM 2762 C CA . ALA A 1 365 ? -44.661 6.532 11.089 1.00 34.89 ? 365 ALA A CA 1 ATOM 2763 C C . ALA A 1 365 ? -43.570 7.567 10.846 1.00 36.43 ? 365 ALA A C 1 ATOM 2764 O O . ALA A 1 365 ? -42.605 7.291 10.133 1.00 36.49 ? 365 ALA A O 1 ATOM 2765 C CB . ALA A 1 365 ? -44.330 5.700 12.316 1.00 35.53 ? 365 ALA A CB 1 ATOM 2766 N N . ASP A 1 366 ? -43.727 8.768 11.421 1.00 34.90 ? 366 ASP A N 1 ATOM 2767 C CA . ASP A 1 366 ? -42.685 9.786 11.392 1.00 37.08 ? 366 ASP A CA 1 ATOM 2768 C C . ASP A 1 366 ? -42.010 9.818 12.758 1.00 38.80 ? 366 ASP A C 1 ATOM 2769 O O . ASP A 1 366 ? -42.638 10.190 13.768 1.00 36.62 ? 366 ASP A O 1 ATOM 2770 C CB . ASP A 1 366 ? -43.256 11.165 11.074 1.00 37.40 ? 366 ASP A CB 1 ATOM 2771 C CG . ASP A 1 366 ? -42.178 12.237 10.993 1.00 39.23 ? 366 ASP A CG 1 ATOM 2772 O OD1 . ASP A 1 366 ? -41.413 12.241 10.013 1.00 40.01 ? 366 ASP A OD1 1 ATOM 2773 O OD2 . ASP A 1 366 ? -42.096 13.093 11.905 1.00 38.56 ? 366 ASP A OD2 1 ATOM 2774 N N . LEU A 1 367 ? -40.735 9.452 12.780 1.00 40.55 ? 367 LEU A N 1 ATOM 2775 C CA . LEU A 1 367 ? -40.031 9.187 14.026 1.00 42.36 ? 367 LEU A CA 1 ATOM 2776 C C . LEU A 1 367 ? -39.733 10.489 14.748 1.00 41.60 ? 367 LEU A C 1 ATOM 2777 O O . LEU A 1 367 ? -39.902 10.566 15.959 1.00 39.80 ? 367 LEU A O 1 ATOM 2778 C CB . LEU A 1 367 ? -38.728 8.419 13.758 1.00 46.46 ? 367 LEU A CB 1 ATOM 2779 C CG . LEU A 1 367 ? -37.754 8.233 14.938 1.00 49.79 ? 367 LEU A CG 1 ATOM 2780 C CD1 . LEU A 1 367 ? -38.422 7.501 16.097 1.00 50.71 ? 367 LEU A CD1 1 ATOM 2781 C CD2 . LEU A 1 367 ? -36.497 7.494 14.486 1.00 52.10 ? 367 LEU A CD2 1 ATOM 2782 N N . LYS A 1 368 ? -39.286 11.498 14.004 1.00 41.82 ? 368 LYS A N 1 ATOM 2783 C CA . LYS A 1 368 ? -38.879 12.771 14.591 1.00 43.33 ? 368 LYS A CA 1 ATOM 2784 C C . LYS A 1 368 ? -40.005 13.395 15.394 1.00 40.70 ? 368 LYS A C 1 ATOM 2785 O O . LYS A 1 368 ? -39.810 13.775 16.549 1.00 38.96 ? 368 LYS A O 1 ATOM 2786 C CB . LYS A 1 368 ? -38.428 13.748 13.502 1.00 46.90 ? 368 LYS A CB 1 ATOM 2787 C CG . LYS A 1 368 ? -37.946 15.096 14.026 1.00 51.09 ? 368 LYS A CG 1 ATOM 2788 C CD . LYS A 1 368 ? -36.723 15.602 13.257 1.00 56.06 ? 368 LYS A CD 1 ATOM 2789 C CE . LYS A 1 368 ? -36.391 17.051 13.608 1.00 58.76 ? 368 LYS A CE 1 ATOM 2790 N NZ . LYS A 1 368 ? -37.464 17.979 13.142 1.00 60.68 ? 368 LYS A NZ 1 ATOM 2791 N N . SER A 1 369 ? -41.176 13.518 14.775 1.00 37.84 ? 369 SER A N 1 ATOM 2792 C CA . SER A 1 369 ? -42.325 14.135 15.439 1.00 35.91 ? 369 SER A CA 1 ATOM 2793 C C . SER A 1 369 ? -42.804 13.309 16.638 1.00 34.36 ? 369 SER A C 1 ATOM 2794 O O . SER A 1 369 ? -43.133 13.850 17.706 1.00 31.91 ? 369 SER A O 1 ATOM 2795 C CB . SER A 1 369 ? -43.455 14.366 14.446 1.00 35.30 ? 369 SER A CB 1 ATOM 2796 O OG . SER A 1 369 ? -43.945 13.128 13.972 1.00 36.83 ? 369 SER A OG 1 ATOM 2797 N N . THR A 1 370 ? -42.833 11.992 16.476 1.00 34.04 ? 370 THR A N 1 ATOM 2798 C CA . THR A 1 370 ? -43.197 11.100 17.561 1.00 33.55 ? 370 THR A CA 1 ATOM 2799 C C . THR A 1 370 ? -42.266 11.268 18.770 1.00 34.93 ? 370 THR A C 1 ATOM 2800 O O . THR A 1 370 ? -42.713 11.373 19.925 1.00 33.74 ? 370 THR A O 1 ATOM 2801 C CB . THR A 1 370 ? -43.173 9.639 17.091 1.00 33.63 ? 370 THR A CB 1 ATOM 2802 O OG1 . THR A 1 370 ? -44.128 9.476 16.042 1.00 32.12 ? 370 THR A OG1 1 ATOM 2803 C CG2 . THR A 1 370 ? -43.474 8.673 18.259 1.00 32.95 ? 370 THR A CG2 1 ATOM 2804 N N . GLN A 1 371 ? -40.971 11.327 18.496 1.00 36.65 ? 371 GLN A N 1 ATOM 2805 C CA . GLN A 1 371 ? -39.981 11.392 19.551 1.00 38.88 ? 371 GLN A CA 1 ATOM 2806 C C . GLN A 1 371 ? -39.970 12.757 20.237 1.00 37.74 ? 371 GLN A C 1 ATOM 2807 O O . GLN A 1 371 ? -39.710 12.844 21.436 1.00 38.07 ? 371 GLN A O 1 ATOM 2808 C CB . GLN A 1 371 ? -38.590 11.059 19.006 1.00 42.40 ? 371 GLN A CB 1 ATOM 2809 C CG . GLN A 1 371 ? -37.592 10.697 20.098 1.00 45.84 ? 371 GLN A CG 1 ATOM 2810 C CD . GLN A 1 371 ? -38.012 9.476 20.901 1.00 47.28 ? 371 GLN A CD 1 ATOM 2811 O OE1 . GLN A 1 371 ? -38.417 8.460 20.334 1.00 52.11 ? 371 GLN A OE1 1 ATOM 2812 N NE2 . GLN A 1 371 ? -37.920 9.572 22.230 1.00 49.46 ? 371 GLN A NE2 1 ATOM 2813 N N . ALA A 1 372 ? -40.227 13.813 19.477 1.00 35.85 ? 372 ALA A N 1 ATOM 2814 C CA . ALA A 1 372 ? -40.324 15.164 20.040 1.00 36.43 ? 372 ALA A CA 1 ATOM 2815 C C . ALA A 1 372 ? -41.458 15.264 21.076 1.00 34.92 ? 372 ALA A C 1 ATOM 2816 O O . ALA A 1 372 ? -41.290 15.912 22.131 1.00 34.31 ? 372 ALA A O 1 ATOM 2817 C CB . ALA A 1 372 ? -40.523 16.179 18.928 1.00 35.84 ? 372 ALA A CB 1 ATOM 2818 N N . ALA A 1 373 ? -42.600 14.641 20.782 1.00 33.25 ? 373 ALA A N 1 ATOM 2819 C CA . ALA A 1 373 ? -43.744 14.663 21.695 1.00 32.59 ? 373 ALA A CA 1 ATOM 2820 C C . ALA A 1 373 ? -43.468 13.801 22.921 1.00 32.88 ? 373 ALA A C 1 ATOM 2821 O O . ALA A 1 373 ? -43.668 14.245 24.070 1.00 32.91 ? 373 ALA A O 1 ATOM 2822 C CB . ALA A 1 373 ? -45.023 14.220 20.995 1.00 32.74 ? 373 ALA A CB 1 ATOM 2823 N N . ILE A 1 374 ? -42.968 12.594 22.692 1.00 33.24 ? 374 ILE A N 1 ATOM 2824 C CA . ILE A 1 374 ? -42.628 11.694 23.775 1.00 34.67 ? 374 ILE A CA 1 ATOM 2825 C C . ILE A 1 374 ? -41.587 12.293 24.735 1.00 35.50 ? 374 ILE A C 1 ATOM 2826 O O . ILE A 1 374 ? -41.738 12.181 25.957 1.00 33.70 ? 374 ILE A O 1 ATOM 2827 C CB . ILE A 1 374 ? -42.157 10.332 23.237 1.00 35.32 ? 374 ILE A CB 1 ATOM 2828 C CG1 . ILE A 1 374 ? -43.360 9.565 22.675 1.00 35.73 ? 374 ILE A CG1 1 ATOM 2829 C CG2 . ILE A 1 374 ? -41.441 9.548 24.323 1.00 35.70 ? 374 ILE A CG2 1 ATOM 2830 C CD1 . ILE A 1 374 ? -43.011 8.292 21.913 1.00 35.65 ? 374 ILE A CD1 1 ATOM 2831 N N . ASN A 1 375 ? -40.560 12.937 24.185 1.00 35.74 ? 375 ASN A N 1 ATOM 2832 C CA . ASN A 1 375 ? -39.514 13.536 25.011 1.00 38.34 ? 375 ASN A CA 1 ATOM 2833 C C . ASN A 1 375 ? -40.042 14.625 25.927 1.00 37.06 ? 375 ASN A C 1 ATOM 2834 O O . ASN A 1 375 ? -39.644 14.696 27.093 1.00 37.82 ? 375 ASN A O 1 ATOM 2835 C CB . ASN A 1 375 ? -38.382 14.100 24.151 1.00 39.58 ? 375 ASN A CB 1 ATOM 2836 C CG . ASN A 1 375 ? -37.491 13.012 23.578 1.00 42.21 ? 375 ASN A CG 1 ATOM 2837 O OD1 . ASN A 1 375 ? -37.569 11.841 23.973 1.00 43.10 ? 375 ASN A OD1 1 ATOM 2838 N ND2 . ASN A 1 375 ? -36.629 13.399 22.640 1.00 44.73 ? 375 ASN A ND2 1 ATOM 2839 N N . GLN A 1 376 ? -40.929 15.457 25.401 1.00 34.71 ? 376 GLN A N 1 ATOM 2840 C CA . GLN A 1 376 ? -41.472 16.558 26.160 1.00 35.48 ? 376 GLN A CA 1 ATOM 2841 C C . GLN A 1 376 ? -42.365 16.050 27.258 1.00 33.46 ? 376 GLN A C 1 ATOM 2842 O O . GLN A 1 376 ? -42.387 16.632 28.346 1.00 31.81 ? 376 GLN A O 1 ATOM 2843 C CB . GLN A 1 376 ? -42.246 17.501 25.259 1.00 35.75 ? 376 GLN A CB 1 ATOM 2844 C CG . GLN A 1 376 ? -41.342 18.259 24.308 1.00 38.29 ? 376 GLN A CG 1 ATOM 2845 C CD . GLN A 1 376 ? -42.141 19.127 23.392 1.00 37.88 ? 376 GLN A CD 1 ATOM 2846 O OE1 . GLN A 1 376 ? -42.749 20.079 23.831 1.00 41.72 ? 376 GLN A OE1 1 ATOM 2847 N NE2 . GLN A 1 376 ? -42.160 18.794 22.111 1.00 43.96 ? 376 GLN A NE2 1 ATOM 2848 N N . ILE A 1 377 ? -43.118 14.985 26.963 1.00 31.50 ? 377 ILE A N 1 ATOM 2849 C CA . ILE A 1 377 ? -43.997 14.400 27.944 1.00 31.84 ? 377 ILE A CA 1 ATOM 2850 C C . ILE A 1 377 ? -43.150 13.755 29.043 1.00 32.77 ? 377 ILE A C 1 ATOM 2851 O O . ILE A 1 377 ? -43.393 13.974 30.226 1.00 33.92 ? 377 ILE A O 1 ATOM 2852 C CB . ILE A 1 377 ? -45.020 13.454 27.325 1.00 30.64 ? 377 ILE A CB 1 ATOM 2853 C CG1 . ILE A 1 377 ? -46.079 14.292 26.570 1.00 30.95 ? 377 ILE A CG1 1 ATOM 2854 C CG2 . ILE A 1 377 ? -45.722 12.611 28.390 1.00 29.96 ? 377 ILE A CG2 1 ATOM 2855 C CD1 . ILE A 1 377 ? -46.987 13.459 25.673 1.00 31.04 ? 377 ILE A CD1 1 ATOM 2856 N N . ASN A 1 378 ? -42.116 13.036 28.658 1.00 33.93 ? 378 ASN A N 1 ATOM 2857 C CA . ASN A 1 378 ? -41.201 12.459 29.645 1.00 36.42 ? 378 ASN A CA 1 ATOM 2858 C C . ASN A 1 378 ? -40.492 13.523 30.486 1.00 37.43 ? 378 ASN A C 1 ATOM 2859 O O . ASN A 1 378 ? -40.201 13.292 31.664 1.00 37.96 ? 378 ASN A O 1 ATOM 2860 C CB . ASN A 1 378 ? -40.191 11.542 28.955 1.00 38.11 ? 378 ASN A CB 1 ATOM 2861 C CG . ASN A 1 378 ? -40.793 10.202 28.576 1.00 39.87 ? 378 ASN A CG 1 ATOM 2862 O OD1 . ASN A 1 378 ? -41.856 9.821 29.070 1.00 39.95 ? 378 ASN A OD1 1 ATOM 2863 N ND2 . ASN A 1 378 ? -40.110 9.471 27.706 1.00 41.84 ? 378 ASN A ND2 1 ATOM 2864 N N . GLY A 1 379 ? -40.211 14.673 29.876 1.00 37.02 ? 379 GLY A N 1 ATOM 2865 C CA . GLY A 1 379 ? -39.661 15.817 30.580 1.00 40.12 ? 379 GLY A CA 1 ATOM 2866 C C . GLY A 1 379 ? -40.542 16.220 31.744 1.00 40.91 ? 379 GLY A C 1 ATOM 2867 O O . GLY A 1 379 ? -40.065 16.388 32.879 1.00 37.10 ? 379 GLY A O 1 ATOM 2868 N N . LYS A 1 380 ? -41.837 16.379 31.486 1.00 38.45 ? 380 LYS A N 1 ATOM 2869 C CA . LYS A 1 380 ? -42.713 16.812 32.565 1.00 38.72 ? 380 LYS A CA 1 ATOM 2870 C C . LYS A 1 380 ? -42.987 15.710 33.570 1.00 36.91 ? 380 LYS A C 1 ATOM 2871 O O . LYS A 1 380 ? -43.133 15.994 34.754 1.00 40.33 ? 380 LYS A O 1 ATOM 2872 C CB . LYS A 1 380 ? -43.981 17.510 32.049 1.00 38.64 ? 380 LYS A CB 1 ATOM 2873 C CG . LYS A 1 380 ? -44.930 16.676 31.275 1.00 39.35 ? 380 LYS A CG 1 ATOM 2874 C CD . LYS A 1 380 ? -46.179 17.478 30.893 1.00 38.00 ? 380 LYS A CD 1 ATOM 2875 C CE . LYS A 1 380 ? -45.907 18.539 29.840 1.00 37.50 ? 380 LYS A CE 1 ATOM 2876 N NZ . LYS A 1 380 ? -47.093 19.412 29.674 1.00 35.33 ? 380 LYS A NZ 1 ATOM 2877 N N . LEU A 1 381 ? -42.997 14.458 33.140 1.00 36.26 ? 381 LEU A N 1 ATOM 2878 C CA . LEU A 1 381 ? -43.054 13.350 34.082 1.00 36.40 ? 381 LEU A CA 1 ATOM 2879 C C . LEU A 1 381 ? -41.860 13.353 35.046 1.00 39.86 ? 381 LEU A C 1 ATOM 2880 O O . LEU A 1 381 ? -42.017 13.131 36.239 1.00 39.77 ? 381 LEU A O 1 ATOM 2881 C CB . LEU A 1 381 ? -43.097 12.011 33.354 1.00 38.39 ? 381 LEU A CB 1 ATOM 2882 C CG . LEU A 1 381 ? -44.445 11.671 32.731 1.00 36.94 ? 381 LEU A CG 1 ATOM 2883 C CD1 . LEU A 1 381 ? -44.393 10.343 31.982 1.00 36.88 ? 381 LEU A CD1 1 ATOM 2884 C CD2 . LEU A 1 381 ? -45.480 11.645 33.842 1.00 36.68 ? 381 LEU A CD2 1 ATOM 2885 N N . ASN A 1 382 ? -40.675 13.634 34.525 1.00 41.31 ? 382 ASN A N 1 ATOM 2886 C CA . ASN A 1 382 ? -39.474 13.661 35.355 1.00 43.80 ? 382 ASN A CA 1 ATOM 2887 C C . ASN A 1 382 ? -39.489 14.779 36.428 1.00 42.82 ? 382 ASN A C 1 ATOM 2888 O O . ASN A 1 382 ? -38.912 14.611 37.501 1.00 42.03 ? 382 ASN A O 1 ATOM 2889 C CB . ASN A 1 382 ? -38.247 13.775 34.462 1.00 46.40 ? 382 ASN A CB 1 ATOM 2890 C CG . ASN A 1 382 ? -36.948 13.684 35.244 1.00 51.07 ? 382 ASN A CG 1 ATOM 2891 O OD1 . ASN A 1 382 ? -36.249 14.683 35.404 1.00 53.35 ? 382 ASN A OD1 1 ATOM 2892 N ND2 . ASN A 1 382 ? -36.637 12.494 35.762 1.00 51.05 ? 382 ASN A ND2 1 ATOM 2893 N N . ARG A 1 383 ? -40.139 15.905 36.139 1.00 40.14 ? 383 ARG A N 1 ATOM 2894 C CA . ARG A 1 383 ? -40.279 16.983 37.116 1.00 41.79 ? 383 ARG A CA 1 ATOM 2895 C C . ARG A 1 383 ? -41.273 16.651 38.225 1.00 38.98 ? 383 ARG A C 1 ATOM 2896 O O . ARG A 1 383 ? -41.172 17.166 39.324 1.00 37.07 ? 383 ARG A O 1 ATOM 2897 C CB . ARG A 1 383 ? -40.758 18.268 36.452 1.00 46.47 ? 383 ARG A CB 1 ATOM 2898 C CG . ARG A 1 383 ? -39.788 18.926 35.485 1.00 52.09 ? 383 ARG A CG 1 ATOM 2899 C CD . ARG A 1 383 ? -40.258 20.354 35.223 1.00 58.11 ? 383 ARG A CD 1 ATOM 2900 N NE . ARG A 1 383 ? -39.616 21.008 34.079 1.00 63.85 ? 383 ARG A NE 1 ATOM 2901 C CZ . ARG A 1 383 ? -39.988 22.192 33.574 1.00 67.13 ? 383 ARG A CZ 1 ATOM 2902 N NH1 . ARG A 1 383 ? -41.007 22.886 34.095 1.00 70.86 ? 383 ARG A NH1 1 ATOM 2903 N NH2 . ARG A 1 383 ? -39.338 22.691 32.538 1.00 64.91 ? 383 ARG A NH2 1 ATOM 2904 N N . LEU A 1 384 ? -42.246 15.805 37.923 1.00 36.86 ? 384 LEU A N 1 ATOM 2905 C CA . LEU A 1 384 ? -43.347 15.518 38.841 1.00 36.64 ? 384 LEU A CA 1 ATOM 2906 C C . LEU A 1 384 ? -43.276 14.172 39.545 1.00 38.73 ? 384 LEU A C 1 ATOM 2907 O O . LEU A 1 384 ? -43.937 14.000 40.578 1.00 37.63 ? 384 LEU A O 1 ATOM 2908 C CB . LEU A 1 384 ? -44.671 15.563 38.076 1.00 35.81 ? 384 LEU A CB 1 ATOM 2909 C CG . LEU A 1 384 ? -45.044 16.930 37.499 1.00 34.70 ? 384 LEU A CG 1 ATOM 2910 C CD1 . LEU A 1 384 ? -46.175 16.796 36.482 1.00 35.81 ? 384 LEU A CD1 1 ATOM 2911 C CD2 . LEU A 1 384 ? -45.399 17.892 38.619 1.00 35.52 ? 384 LEU A CD2 1 ATOM 2912 N N . ILE A 1 385 ? -42.559 13.203 38.957 1.00 36.05 ? 385 ILE A N 1 ATOM 2913 C CA . ILE A 1 385 ? -42.519 11.835 39.468 1.00 38.10 ? 385 ILE A CA 1 ATOM 2914 C C . ILE A 1 385 ? -41.194 11.591 40.200 1.00 38.30 ? 385 ILE A C 1 ATOM 2915 O O . ILE A 1 385 ? -40.118 11.955 39.715 1.00 39.28 ? 385 ILE A O 1 ATOM 2916 C CB . ILE A 1 385 ? -42.750 10.793 38.343 1.00 38.54 ? 385 ILE A CB 1 ATOM 2917 C CG1 . ILE A 1 385 ? -44.115 11.022 37.667 1.00 40.24 ? 385 ILE A CG1 1 ATOM 2918 C CG2 . ILE A 1 385 ? -42.669 9.354 38.872 1.00 38.33 ? 385 ILE A CG2 1 ATOM 2919 C CD1 . ILE A 1 385 ? -45.308 10.975 38.608 1.00 40.65 ? 385 ILE A CD1 1 ATOM 2920 N N . GLY A 1 386 ? -41.292 11.031 41.397 1.00 39.92 ? 386 GLY A N 1 ATOM 2921 C CA . GLY A 1 386 ? -40.121 10.754 42.234 1.00 41.02 ? 386 GLY A CA 1 ATOM 2922 C C . GLY A 1 386 ? -39.374 11.976 42.732 1.00 41.44 ? 386 GLY A C 1 ATOM 2923 O O . GLY A 1 386 ? -38.154 11.920 42.893 1.00 41.40 ? 386 GLY A O 1 ATOM 2924 N N . LYS A 1 387 ? -40.086 13.073 43.017 1.00 40.83 ? 387 LYS A N 1 ATOM 2925 C CA . LYS A 1 387 ? -39.426 14.322 43.404 1.00 40.69 ? 387 LYS A CA 1 ATOM 2926 C C . LYS A 1 387 ? -39.911 14.884 44.750 1.00 41.12 ? 387 LYS A C 1 ATOM 2927 O O . LYS A 1 387 ? -39.802 16.089 45.015 1.00 41.20 ? 387 LYS A O 1 ATOM 2928 C CB . LYS A 1 387 ? -39.575 15.349 42.283 1.00 44.06 ? 387 LYS A CB 1 ATOM 2929 C CG . LYS A 1 387 ? -38.969 14.880 40.961 1.00 44.42 ? 387 LYS A CG 1 ATOM 2930 C CD . LYS A 1 387 ? -37.445 14.893 41.020 1.00 46.85 ? 387 LYS A CD 1 ATOM 2931 C CE . LYS A 1 387 ? -36.799 14.552 39.684 1.00 47.59 ? 387 LYS A CE 1 ATOM 2932 N NZ . LYS A 1 387 ? -37.307 13.266 39.129 1.00 49.33 ? 387 LYS A NZ 1 ATOM 2933 N N . THR A 1 388 ? -40.422 14.001 45.609 1.00 37.89 ? 388 THR A N 1 ATOM 2934 C CA . THR A 1 388 ? -41.055 14.424 46.850 1.00 38.10 ? 388 THR A CA 1 ATOM 2935 C C . THR A 1 388 ? -39.996 14.939 47.807 1.00 41.15 ? 388 THR A C 1 ATOM 2936 O O . THR A 1 388 ? -38.799 14.591 47.714 1.00 40.59 ? 388 THR A O 1 ATOM 2937 C CB . THR A 1 388 ? -41.882 13.298 47.524 1.00 36.37 ? 388 THR A CB 1 ATOM 2938 O OG1 . THR A 1 388 ? -41.006 12.225 47.922 1.00 36.93 ? 388 THR A OG1 1 ATOM 2939 C CG2 . THR A 1 388 ? -42.996 12.776 46.564 1.00 34.81 ? 388 THR A CG2 1 ATOM 2940 N N . ASN A 1 389 ? -40.445 15.787 48.715 1.00 39.48 ? 389 ASN A N 1 ATOM 2941 C CA A ASN A 1 389 ? -39.523 16.343 49.686 0.50 40.68 ? 389 ASN A CA 1 ATOM 2942 C CA B ASN A 1 389 ? -39.583 16.428 49.692 0.50 40.57 ? 389 ASN A CA 1 ATOM 2943 C C . ASN A 1 389 ? -39.862 15.900 51.105 1.00 40.03 ? 389 ASN A C 1 ATOM 2944 O O . ASN A 1 389 ? -41.031 15.599 51.430 1.00 37.40 ? 389 ASN A O 1 ATOM 2945 C CB A ASN A 1 389 ? -39.438 17.865 49.560 0.50 42.03 ? 389 ASN A CB 1 ATOM 2946 C CB B ASN A 1 389 ? -39.828 17.934 49.638 0.50 41.09 ? 389 ASN A CB 1 ATOM 2947 C CG A ASN A 1 389 ? -40.721 18.571 49.933 0.50 41.16 ? 389 ASN A CG 1 ATOM 2948 C CG B ASN A 1 389 ? -39.198 18.581 48.416 0.50 41.67 ? 389 ASN A CG 1 ATOM 2949 O OD1 A ASN A 1 389 ? -41.702 17.954 50.359 0.50 39.86 ? 389 ASN A OD1 1 ATOM 2950 O OD1 B ASN A 1 389 ? -38.731 17.900 47.501 0.50 40.74 ? 389 ASN A OD1 1 ATOM 2951 N ND2 A ASN A 1 389 ? -40.707 19.900 49.797 0.50 41.41 ? 389 ASN A ND2 1 ATOM 2952 N ND2 B ASN A 1 389 ? -39.175 19.901 48.404 0.50 40.76 ? 389 ASN A ND2 1 ATOM 2953 N N . GLU A 1 390 ? -38.811 15.829 51.929 1.00 37.75 ? 390 GLU A N 1 ATOM 2954 C CA . GLU A 1 390 ? -38.915 15.338 53.285 1.00 34.29 ? 390 GLU A CA 1 ATOM 2955 C C . GLU A 1 390 ? -39.419 16.364 54.303 1.00 30.51 ? 390 GLU A C 1 ATOM 2956 O O . GLU A 1 390 ? -38.883 17.487 54.376 1.00 29.96 ? 390 GLU A O 1 ATOM 2957 C CB . GLU A 1 390 ? -37.535 14.862 53.751 1.00 36.33 ? 390 GLU A CB 1 ATOM 2958 C CG . GLU A 1 390 ? -37.034 13.620 53.051 1.00 40.12 ? 390 GLU A CG 1 ATOM 2959 C CD . GLU A 1 390 ? -35.839 13.020 53.737 1.00 42.41 ? 390 GLU A CD 1 ATOM 2960 O OE1 . GLU A 1 390 ? -34.813 13.709 53.731 1.00 41.72 ? 390 GLU A OE1 1 ATOM 2961 O OE2 . GLU A 1 390 ? -35.945 11.881 54.299 1.00 46.35 ? 390 GLU A OE2 1 ATOM 2962 N N . LYS A 1 391 ? -40.393 15.959 55.125 1.00 27.60 ? 391 LYS A N 1 ATOM 2963 C CA . LYS A 1 391 ? -40.742 16.676 56.365 1.00 26.96 ? 391 LYS A CA 1 ATOM 2964 C C . LYS A 1 391 ? -40.656 15.709 57.548 1.00 26.22 ? 391 LYS A C 1 ATOM 2965 O O . LYS A 1 391 ? -40.876 14.494 57.391 1.00 25.64 ? 391 LYS A O 1 ATOM 2966 C CB . LYS A 1 391 ? -42.154 17.272 56.319 1.00 27.48 ? 391 LYS A CB 1 ATOM 2967 C CG . LYS A 1 391 ? -42.410 18.276 55.193 1.00 28.02 ? 391 LYS A CG 1 ATOM 2968 C CD . LYS A 1 391 ? -41.547 19.523 55.303 1.00 27.77 ? 391 LYS A CD 1 ATOM 2969 C CE . LYS A 1 391 ? -41.812 20.519 54.173 1.00 27.71 ? 391 LYS A CE 1 ATOM 2970 N NZ . LYS A 1 391 ? -40.850 21.637 54.126 1.00 25.91 ? 391 LYS A NZ 1 ATOM 2971 N N . PHE A 1 392 ? -40.384 16.255 58.720 1.00 23.78 ? 392 PHE A N 1 ATOM 2972 C CA . PHE A 1 392 ? -40.105 15.440 59.890 1.00 24.84 ? 392 PHE A CA 1 ATOM 2973 C C . PHE A 1 392 ? -41.074 15.807 60.997 1.00 24.00 ? 392 PHE A C 1 ATOM 2974 O O . PHE A 1 392 ? -42.263 15.576 60.808 1.00 24.47 ? 392 PHE A O 1 ATOM 2975 C CB . PHE A 1 392 ? -38.626 15.547 60.244 1.00 25.96 ? 392 PHE A CB 1 ATOM 2976 C CG . PHE A 1 392 ? -37.724 15.135 59.109 1.00 26.67 ? 392 PHE A CG 1 ATOM 2977 C CD1 . PHE A 1 392 ? -37.714 13.832 58.671 1.00 28.72 ? 392 PHE A CD1 1 ATOM 2978 C CD2 . PHE A 1 392 ? -36.939 16.067 58.456 1.00 29.22 ? 392 PHE A CD2 1 ATOM 2979 C CE1 . PHE A 1 392 ? -36.912 13.437 57.608 1.00 30.13 ? 392 PHE A CE1 1 ATOM 2980 C CE2 . PHE A 1 392 ? -36.121 15.686 57.400 1.00 29.94 ? 392 PHE A CE2 1 ATOM 2981 C CZ . PHE A 1 392 ? -36.088 14.374 56.995 1.00 30.73 ? 392 PHE A CZ 1 ATOM 2982 N N . HIS A 1 393 ? -40.617 16.391 62.097 1.00 22.93 ? 393 HIS A N 1 ATOM 2983 C CA . HIS A 1 393 ? -41.546 16.782 63.157 1.00 23.35 ? 393 HIS A CA 1 ATOM 2984 C C . HIS A 1 393 ? -42.331 18.024 62.778 1.00 23.31 ? 393 HIS A C 1 ATOM 2985 O O . HIS A 1 393 ? -41.753 19.034 62.397 1.00 24.14 ? 393 HIS A O 1 ATOM 2986 C CB . HIS A 1 393 ? -40.806 17.036 64.440 1.00 24.19 ? 393 HIS A CB 1 ATOM 2987 C CG . HIS A 1 393 ? -41.677 17.034 65.655 1.00 24.55 ? 393 HIS A CG 1 ATOM 2988 N ND1 . HIS A 1 393 ? -42.523 16.022 65.940 1.00 26.00 ? 393 HIS A ND1 1 ATOM 2989 C CD2 . HIS A 1 393 ? -41.861 17.991 66.645 1.00 26.55 ? 393 HIS A CD2 1 ATOM 2990 C CE1 . HIS A 1 393 ? -43.193 16.304 67.081 1.00 26.47 ? 393 HIS A CE1 1 ATOM 2991 N NE2 . HIS A 1 393 ? -42.774 17.495 67.525 1.00 27.55 ? 393 HIS A NE2 1 ATOM 2992 N N . GLN A 1 394 ? -43.635 17.968 62.930 1.00 22.30 ? 394 GLN A N 1 ATOM 2993 C CA . GLN A 1 394 ? -44.521 19.045 62.438 1.00 23.46 ? 394 GLN A CA 1 ATOM 2994 C C . GLN A 1 394 ? -45.432 19.488 63.585 1.00 23.59 ? 394 GLN A C 1 ATOM 2995 O O . GLN A 1 394 ? -44.916 19.847 64.638 1.00 28.14 ? 394 GLN A O 1 ATOM 2996 C CB . GLN A 1 394 ? -45.266 18.537 61.201 1.00 23.71 ? 394 GLN A CB 1 ATOM 2997 C CG . GLN A 1 394 ? -44.336 18.175 60.043 1.00 25.25 ? 394 GLN A CG 1 ATOM 2998 C CD . GLN A 1 394 ? -45.004 17.254 59.034 1.00 27.74 ? 394 GLN A CD 1 ATOM 2999 O OE1 . GLN A 1 394 ? -46.031 17.613 58.478 1.00 27.00 ? 394 GLN A OE1 1 ATOM 3000 N NE2 . GLN A 1 394 ? -44.428 16.025 58.817 1.00 28.82 ? 394 GLN A NE2 1 ATOM 3001 N N . ILE A 1 395 ? -46.746 19.529 63.383 1.00 21.70 ? 395 ILE A N 1 ATOM 3002 C CA . ILE A 1 395 ? -47.698 19.837 64.441 1.00 21.01 ? 395 ILE A CA 1 ATOM 3003 C C . ILE A 1 395 ? -48.630 18.628 64.476 1.00 20.92 ? 395 ILE A C 1 ATOM 3004 O O . ILE A 1 395 ? -48.680 17.822 63.516 1.00 20.86 ? 395 ILE A O 1 ATOM 3005 C CB . ILE A 1 395 ? -48.507 21.128 64.198 1.00 20.58 ? 395 ILE A CB 1 ATOM 3006 C CG1 . ILE A 1 395 ? -49.270 21.072 62.846 1.00 20.35 ? 395 ILE A CG1 1 ATOM 3007 C CG2 . ILE A 1 395 ? -47.590 22.358 64.292 1.00 20.34 ? 395 ILE A CG2 1 ATOM 3008 C CD1 . ILE A 1 395 ? -50.367 22.148 62.741 1.00 21.05 ? 395 ILE A CD1 1 ATOM 3009 N N . GLU A 1 396 ? -49.357 18.493 65.579 1.00 21.36 ? 396 GLU A N 1 ATOM 3010 C CA . GLU A 1 396 ? -50.398 17.489 65.667 1.00 21.78 ? 396 GLU A CA 1 ATOM 3011 C C . GLU A 1 396 ? -51.607 17.929 64.837 1.00 21.84 ? 396 GLU A C 1 ATOM 3012 O O . GLU A 1 396 ? -51.878 19.132 64.689 1.00 21.22 ? 396 GLU A O 1 ATOM 3013 C CB . GLU A 1 396 ? -50.809 17.272 67.120 1.00 23.20 ? 396 GLU A CB 1 ATOM 3014 C CG . GLU A 1 396 ? -49.668 16.740 68.013 1.00 24.54 ? 396 GLU A CG 1 ATOM 3015 C CD . GLU A 1 396 ? -49.116 15.392 67.583 1.00 25.62 ? 396 GLU A CD 1 ATOM 3016 O OE1 . GLU A 1 396 ? -49.879 14.577 66.998 1.00 27.40 ? 396 GLU A OE1 1 ATOM 3017 O OE2 . GLU A 1 396 ? -47.905 15.117 67.854 1.00 27.73 ? 396 GLU A OE2 1 ATOM 3018 N N . LYS A 1 397 ? -52.308 16.933 64.295 1.00 21.53 ? 397 LYS A N 1 ATOM 3019 C CA . LYS A 1 397 ? -53.384 17.164 63.330 1.00 21.21 ? 397 LYS A CA 1 ATOM 3020 C C . LYS A 1 397 ? -54.677 16.419 63.695 1.00 22.16 ? 397 LYS A C 1 ATOM 3021 O O . LYS A 1 397 ? -55.687 16.583 63.025 1.00 23.11 ? 397 LYS A O 1 ATOM 3022 C CB . LYS A 1 397 ? -52.875 16.788 61.939 1.00 20.64 ? 397 LYS A CB 1 ATOM 3023 C CG . LYS A 1 397 ? -51.658 17.669 61.542 1.00 20.46 ? 397 LYS A CG 1 ATOM 3024 C CD . LYS A 1 397 ? -51.077 17.305 60.211 1.00 20.39 ? 397 LYS A CD 1 ATOM 3025 C CE . LYS A 1 397 ? -49.791 18.070 59.910 1.00 19.99 ? 397 LYS A CE 1 ATOM 3026 N NZ . LYS A 1 397 ? -49.353 17.818 58.516 1.00 19.78 ? 397 LYS A NZ 1 ATOM 3027 N N . GLU A 1 398 ? -54.638 15.649 64.771 1.00 23.00 ? 398 GLU A N 1 ATOM 3028 C CA . GLU A 1 398 ? -55.811 14.963 65.337 1.00 24.94 ? 398 GLU A CA 1 ATOM 3029 C C . GLU A 1 398 ? -55.748 15.139 66.842 1.00 25.18 ? 398 GLU A C 1 ATOM 3030 O O . GLU A 1 398 ? -54.649 15.109 67.424 1.00 24.02 ? 398 GLU A O 1 ATOM 3031 C CB . GLU A 1 398 ? -55.761 13.464 64.991 1.00 28.72 ? 398 GLU A CB 1 ATOM 3032 C CG . GLU A 1 398 ? -56.136 13.157 63.545 1.00 30.31 ? 398 GLU A CG 1 ATOM 3033 C CD . GLU A 1 398 ? -56.119 11.659 63.213 1.00 34.49 ? 398 GLU A CD 1 ATOM 3034 O OE1 . GLU A 1 398 ? -55.982 10.833 64.134 1.00 37.39 ? 398 GLU A OE1 1 ATOM 3035 O OE2 . GLU A 1 398 ? -56.216 11.300 62.019 1.00 37.46 ? 398 GLU A OE2 1 ATOM 3036 N N . PHE A 1 399 ? -56.904 15.311 67.491 1.00 24.62 ? 399 PHE A N 1 ATOM 3037 C CA . PHE A 1 399 ? -56.929 15.635 68.920 1.00 25.18 ? 399 PHE A CA 1 ATOM 3038 C C . PHE A 1 399 ? -57.990 14.794 69.649 1.00 27.56 ? 399 PHE A C 1 ATOM 3039 O O . PHE A 1 399 ? -59.139 14.763 69.205 1.00 29.20 ? 399 PHE A O 1 ATOM 3040 C CB . PHE A 1 399 ? -57.235 17.127 69.098 1.00 24.71 ? 399 PHE A CB 1 ATOM 3041 C CG . PHE A 1 399 ? -56.277 17.993 68.357 1.00 23.83 ? 399 PHE A CG 1 ATOM 3042 C CD1 . PHE A 1 399 ? -56.476 18.264 67.014 1.00 23.75 ? 399 PHE A CD1 1 ATOM 3043 C CD2 . PHE A 1 399 ? -55.109 18.415 68.963 1.00 24.26 ? 399 PHE A CD2 1 ATOM 3044 C CE1 . PHE A 1 399 ? -55.543 19.029 66.308 1.00 23.94 ? 399 PHE A CE1 1 ATOM 3045 C CE2 . PHE A 1 399 ? -54.175 19.168 68.260 1.00 24.48 ? 399 PHE A CE2 1 ATOM 3046 C CZ . PHE A 1 399 ? -54.393 19.458 66.921 1.00 23.12 ? 399 PHE A CZ 1 ATOM 3047 N N . SER A 1 400 ? -57.604 14.198 70.764 1.00 29.10 ? 400 SER A N 1 ATOM 3048 C CA . SER A 1 400 ? -58.530 13.382 71.592 1.00 31.88 ? 400 SER A CA 1 ATOM 3049 C C . SER A 1 400 ? -59.328 14.188 72.647 1.00 34.14 ? 400 SER A C 1 ATOM 3050 O O . SER A 1 400 ? -60.326 13.687 73.202 1.00 34.27 ? 400 SER A O 1 ATOM 3051 C CB . SER A 1 400 ? -57.739 12.263 72.254 1.00 32.51 ? 400 SER A CB 1 ATOM 3052 O OG . SER A 1 400 ? -56.769 12.794 73.152 1.00 34.66 ? 400 SER A OG 1 ATOM 3053 N N . GLU A 1 401 ? -58.897 15.417 72.932 1.00 32.97 ? 401 GLU A N 1 ATOM 3054 C CA . GLU A 1 401 ? -59.598 16.301 73.889 1.00 35.05 ? 401 GLU A CA 1 ATOM 3055 C C . GLU A 1 401 ? -59.924 17.653 73.281 1.00 33.22 ? 401 GLU A C 1 ATOM 3056 O O . GLU A 1 401 ? -59.205 18.142 72.409 1.00 30.29 ? 401 GLU A O 1 ATOM 3057 C CB . GLU A 1 401 ? -58.759 16.588 75.136 1.00 37.93 ? 401 GLU A CB 1 ATOM 3058 C CG . GLU A 1 401 ? -58.605 15.420 76.089 1.00 43.65 ? 401 GLU A CG 1 ATOM 3059 C CD . GLU A 1 401 ? -57.597 14.421 75.580 1.00 46.62 ? 401 GLU A CD 1 ATOM 3060 O OE1 . GLU A 1 401 ? -56.534 14.878 75.082 1.00 50.77 ? 401 GLU A OE1 1 ATOM 3061 O OE2 . GLU A 1 401 ? -57.875 13.193 75.667 1.00 50.40 ? 401 GLU A OE2 1 ATOM 3062 N N . VAL A 1 402 ? -60.979 18.265 73.812 1.00 31.88 ? 402 VAL A N 1 ATOM 3063 C CA . VAL A 1 402 ? -61.387 19.635 73.476 1.00 31.52 ? 402 VAL A CA 1 ATOM 3064 C C . VAL A 1 402 ? -60.500 20.634 74.233 1.00 30.03 ? 402 VAL A C 1 ATOM 3065 O O . VAL A 1 402 ? -60.282 20.490 75.438 1.00 29.12 ? 402 VAL A O 1 ATOM 3066 C CB . VAL A 1 402 ? -62.889 19.821 73.861 1.00 33.70 ? 402 VAL A CB 1 ATOM 3067 C CG1 . VAL A 1 402 ? -63.269 21.285 73.949 1.00 32.65 ? 402 VAL A CG1 1 ATOM 3068 C CG2 . VAL A 1 402 ? -63.788 19.082 72.873 1.00 34.14 ? 402 VAL A CG2 1 ATOM 3069 N N . GLU A 1 403 ? -59.952 21.637 73.549 1.00 28.70 ? 403 GLU A N 1 ATOM 3070 C CA . GLU A 1 403 ? -59.033 22.592 74.221 1.00 29.28 ? 403 GLU A CA 1 ATOM 3071 C C . GLU A 1 403 ? -59.284 24.065 73.924 1.00 28.67 ? 403 GLU A C 1 ATOM 3072 O O . GLU A 1 403 ? -58.823 24.927 74.671 1.00 31.17 ? 403 GLU A O 1 ATOM 3073 C CB . GLU A 1 403 ? -57.566 22.290 73.856 1.00 29.59 ? 403 GLU A CB 1 ATOM 3074 C CG . GLU A 1 403 ? -57.096 20.871 74.130 1.00 29.98 ? 403 GLU A CG 1 ATOM 3075 C CD . GLU A 1 403 ? -55.707 20.600 73.545 1.00 30.46 ? 403 GLU A CD 1 ATOM 3076 O OE1 . GLU A 1 403 ? -55.543 20.480 72.311 1.00 28.31 ? 403 GLU A OE1 1 ATOM 3077 O OE2 . GLU A 1 403 ? -54.761 20.519 74.333 1.00 32.26 ? 403 GLU A OE2 1 ATOM 3078 N N . GLY A 1 404 ? -59.947 24.365 72.817 1.00 26.89 ? 404 GLY A N 1 ATOM 3079 C CA . GLY A 1 404 ? -60.236 25.737 72.439 1.00 26.55 ? 404 GLY A CA 1 ATOM 3080 C C . GLY A 1 404 ? -59.106 26.369 71.608 1.00 26.04 ? 404 GLY A C 1 ATOM 3081 O O . GLY A 1 404 ? -58.646 25.781 70.647 1.00 24.40 ? 404 GLY A O 1 ATOM 3082 N N . ARG A 1 405 ? -58.670 27.562 72.020 1.00 24.73 ? 405 ARG A N 1 ATOM 3083 C CA . ARG A 1 405 ? -57.913 28.473 71.191 1.00 24.55 ? 405 ARG A CA 1 ATOM 3084 C C . ARG A 1 405 ? -56.694 27.893 70.460 1.00 23.32 ? 405 ARG A C 1 ATOM 3085 O O . ARG A 1 405 ? -56.568 28.056 69.259 1.00 22.77 ? 405 ARG A O 1 ATOM 3086 C CB . ARG A 1 405 ? -57.473 29.641 72.039 1.00 25.25 ? 405 ARG A CB 1 ATOM 3087 C CG . ARG A 1 405 ? -56.891 30.794 71.265 1.00 25.60 ? 405 ARG A CG 1 ATOM 3088 C CD . ARG A 1 405 ? -56.661 31.982 72.223 1.00 25.91 ? 405 ARG A CD 1 ATOM 3089 N NE . ARG A 1 405 ? -56.126 33.117 71.486 1.00 25.74 ? 405 ARG A NE 1 ATOM 3090 C CZ . ARG A 1 405 ? -55.932 34.324 72.004 1.00 26.62 ? 405 ARG A CZ 1 ATOM 3091 N NH1 . ARG A 1 405 ? -56.183 34.549 73.278 1.00 27.65 ? 405 ARG A NH1 1 ATOM 3092 N NH2 . ARG A 1 405 ? -55.480 35.303 71.241 1.00 26.73 ? 405 ARG A NH2 1 ATOM 3093 N N A ILE A 1 406 ? -55.796 27.237 71.176 0.50 23.37 ? 406 ILE A N 1 ATOM 3094 N N B ILE A 1 406 ? -55.804 27.230 71.183 0.50 23.42 ? 406 ILE A N 1 ATOM 3095 C CA A ILE A 1 406 ? -54.583 26.753 70.532 0.50 23.51 ? 406 ILE A CA 1 ATOM 3096 C CA B ILE A 1 406 ? -54.592 26.721 70.559 0.50 23.59 ? 406 ILE A CA 1 ATOM 3097 C C A ILE A 1 406 ? -54.922 25.642 69.519 0.50 22.68 ? 406 ILE A C 1 ATOM 3098 C C B ILE A 1 406 ? -54.939 25.654 69.515 0.50 22.73 ? 406 ILE A C 1 ATOM 3099 O O A ILE A 1 406 ? -54.348 25.591 68.421 0.50 21.41 ? 406 ILE A O 1 ATOM 3100 O O B ILE A 1 406 ? -54.383 25.635 68.406 0.50 21.44 ? 406 ILE A O 1 ATOM 3101 C CB A ILE A 1 406 ? -53.542 26.284 71.555 0.50 24.46 ? 406 ILE A CB 1 ATOM 3102 C CB B ILE A 1 406 ? -53.629 26.122 71.585 0.50 24.68 ? 406 ILE A CB 1 ATOM 3103 C CG1 A ILE A 1 406 ? -52.330 25.681 70.845 0.50 24.29 ? 406 ILE A CG1 1 ATOM 3104 C CG1 B ILE A 1 406 ? -52.235 25.995 70.969 0.50 24.73 ? 406 ILE A CG1 1 ATOM 3105 C CG2 A ILE A 1 406 ? -54.124 25.218 72.467 0.50 25.31 ? 406 ILE A CG2 1 ATOM 3106 C CG2 B ILE A 1 406 ? -54.111 24.748 72.038 0.50 24.94 ? 406 ILE A CG2 1 ATOM 3107 C CD1 A ILE A 1 406 ? -51.633 26.641 69.915 0.50 24.64 ? 406 ILE A CD1 1 ATOM 3108 C CD1 B ILE A 1 406 ? -51.607 27.331 70.648 0.50 25.43 ? 406 ILE A CD1 1 ATOM 3109 N N . GLN A 1 407 ? -55.887 24.789 69.858 1.00 22.35 ? 407 GLN A N 1 ATOM 3110 C CA . GLN A 1 407 ? -56.288 23.733 68.962 1.00 22.84 ? 407 GLN A CA 1 ATOM 3111 C C . GLN A 1 407 ? -56.991 24.283 67.732 1.00 22.08 ? 407 GLN A C 1 ATOM 3112 O O . GLN A 1 407 ? -56.808 23.765 66.610 1.00 21.87 ? 407 GLN A O 1 ATOM 3113 C CB . GLN A 1 407 ? -57.172 22.710 69.688 1.00 22.56 ? 407 GLN A CB 1 ATOM 3114 C CG . GLN A 1 407 ? -57.432 21.478 68.866 1.00 23.02 ? 407 GLN A CG 1 ATOM 3115 C CD . GLN A 1 407 ? -58.332 20.469 69.556 1.00 23.53 ? 407 GLN A CD 1 ATOM 3116 O OE1 . GLN A 1 407 ? -59.345 20.082 69.003 1.00 25.19 ? 407 GLN A OE1 1 ATOM 3117 N NE2 . GLN A 1 407 ? -57.991 20.089 70.780 1.00 23.09 ? 407 GLN A NE2 1 ATOM 3118 N N . ASP A 1 408 ? -57.821 25.313 67.929 1.00 22.30 ? 408 ASP A N 1 ATOM 3119 C CA . ASP A 1 408 ? -58.473 25.992 66.825 1.00 21.21 ? 408 ASP A CA 1 ATOM 3120 C C . ASP A 1 408 ? -57.406 26.501 65.828 1.00 21.16 ? 408 ASP A C 1 ATOM 3121 O O . ASP A 1 408 ? -57.590 26.385 64.625 1.00 19.41 ? 408 ASP A O 1 ATOM 3122 C CB . ASP A 1 408 ? -59.245 27.205 67.276 1.00 22.78 ? 408 ASP A CB 1 ATOM 3123 C CG . ASP A 1 408 ? -60.444 26.877 68.164 1.00 24.52 ? 408 ASP A CG 1 ATOM 3124 O OD1 . ASP A 1 408 ? -60.955 25.726 68.096 1.00 25.22 ? 408 ASP A OD1 1 ATOM 3125 O OD2 . ASP A 1 408 ? -60.838 27.811 68.926 1.00 25.04 ? 408 ASP A OD2 1 ATOM 3126 N N . LEU A 1 409 ? -56.316 27.052 66.359 1.00 20.27 ? 409 LEU A N 1 ATOM 3127 C CA . LEU A 1 409 ? -55.249 27.598 65.493 1.00 20.08 ? 409 LEU A CA 1 ATOM 3128 C C . LEU A 1 409 ? -54.526 26.464 64.758 1.00 19.65 ? 409 LEU A C 1 ATOM 3129 O O . LEU A 1 409 ? -54.310 26.554 63.556 1.00 19.35 ? 409 LEU A O 1 ATOM 3130 C CB . LEU A 1 409 ? -54.269 28.417 66.318 1.00 19.98 ? 409 LEU A CB 1 ATOM 3131 C CG . LEU A 1 409 ? -53.190 29.199 65.563 1.00 20.28 ? 409 LEU A CG 1 ATOM 3132 C CD1 . LEU A 1 409 ? -53.748 30.095 64.465 1.00 20.09 ? 409 LEU A CD1 1 ATOM 3133 C CD2 . LEU A 1 409 ? -52.471 29.988 66.654 1.00 21.19 ? 409 LEU A CD2 1 ATOM 3134 N N . GLU A 1 410 ? -54.154 25.411 65.489 1.00 20.00 ? 410 GLU A N 1 ATOM 3135 C CA . GLU A 1 410 ? -53.519 24.228 64.868 1.00 20.85 ? 410 GLU A CA 1 ATOM 3136 C C . GLU A 1 410 ? -54.355 23.663 63.730 1.00 20.31 ? 410 GLU A C 1 ATOM 3137 O O . GLU A 1 410 ? -53.851 23.408 62.625 1.00 19.04 ? 410 GLU A O 1 ATOM 3138 C CB . GLU A 1 410 ? -53.214 23.147 65.906 1.00 21.82 ? 410 GLU A CB 1 ATOM 3139 C CG . GLU A 1 410 ? -52.139 23.570 66.868 1.00 23.17 ? 410 GLU A CG 1 ATOM 3140 C CD . GLU A 1 410 ? -52.062 22.747 68.159 1.00 25.21 ? 410 GLU A CD 1 ATOM 3141 O OE1 . GLU A 1 410 ? -53.099 22.172 68.602 1.00 25.20 ? 410 GLU A OE1 1 ATOM 3142 O OE2 . GLU A 1 410 ? -50.951 22.693 68.760 1.00 25.83 ? 410 GLU A OE2 1 ATOM 3143 N N . LYS A 1 411 ? -55.655 23.506 63.956 1.00 19.79 ? 411 LYS A N 1 ATOM 3144 C CA . LYS A 1 411 ? -56.537 23.044 62.902 1.00 20.61 ? 411 LYS A CA 1 ATOM 3145 C C . LYS A 1 411 ? -56.661 23.969 61.710 1.00 19.15 ? 411 LYS A C 1 ATOM 3146 O O . LYS A 1 411 ? -56.703 23.505 60.548 1.00 18.36 ? 411 LYS A O 1 ATOM 3147 C CB . LYS A 1 411 ? -57.935 22.723 63.466 1.00 22.19 ? 411 LYS A CB 1 ATOM 3148 C CG . LYS A 1 411 ? -57.956 21.495 64.372 1.00 23.23 ? 411 LYS A CG 1 ATOM 3149 C CD . LYS A 1 411 ? -59.350 21.294 64.996 1.00 25.63 ? 411 LYS A CD 1 ATOM 3150 C CE . LYS A 1 411 ? -59.527 19.905 65.547 1.00 27.85 ? 411 LYS A CE 1 ATOM 3151 N NZ . LYS A 1 411 ? -60.871 19.650 66.147 1.00 30.21 ? 411 LYS A NZ 1 ATOM 3152 N N . TYR A 1 412 ? -56.741 25.271 61.960 1.00 18.68 ? 412 TYR A N 1 ATOM 3153 C CA . TYR A 1 412 ? -56.949 26.246 60.907 1.00 18.47 ? 412 TYR A CA 1 ATOM 3154 C C . TYR A 1 412 ? -55.667 26.332 60.057 1.00 18.13 ? 412 TYR A C 1 ATOM 3155 O O . TYR A 1 412 ? -55.748 26.489 58.861 1.00 18.23 ? 412 TYR A O 1 ATOM 3156 C CB . TYR A 1 412 ? -57.190 27.634 61.508 1.00 18.65 ? 412 TYR A CB 1 ATOM 3157 C CG . TYR A 1 412 ? -57.572 28.725 60.539 1.00 18.92 ? 412 TYR A CG 1 ATOM 3158 C CD1 . TYR A 1 412 ? -58.818 28.752 59.947 1.00 18.75 ? 412 TYR A CD1 1 ATOM 3159 C CD2 . TYR A 1 412 ? -56.694 29.788 60.246 1.00 19.09 ? 412 TYR A CD2 1 ATOM 3160 C CE1 . TYR A 1 412 ? -59.211 29.804 59.120 1.00 19.01 ? 412 TYR A CE1 1 ATOM 3161 C CE2 . TYR A 1 412 ? -57.057 30.800 59.396 1.00 19.08 ? 412 TYR A CE2 1 ATOM 3162 C CZ . TYR A 1 412 ? -58.308 30.818 58.833 1.00 19.03 ? 412 TYR A CZ 1 ATOM 3163 O OH . TYR A 1 412 ? -58.681 31.845 58.002 1.00 18.54 ? 412 TYR A OH 1 ATOM 3164 N N . VAL A 1 413 ? -54.520 26.212 60.702 1.00 17.87 ? 413 VAL A N 1 ATOM 3165 C CA . VAL A 1 413 ? -53.240 26.255 59.982 1.00 17.92 ? 413 VAL A CA 1 ATOM 3166 C C . VAL A 1 413 ? -53.210 25.100 58.975 1.00 17.95 ? 413 VAL A C 1 ATOM 3167 O O . VAL A 1 413 ? -52.893 25.303 57.816 1.00 17.86 ? 413 VAL A O 1 ATOM 3168 C CB . VAL A 1 413 ? -52.061 26.191 60.957 1.00 18.30 ? 413 VAL A CB 1 ATOM 3169 C CG1 . VAL A 1 413 ? -50.794 25.776 60.209 1.00 18.88 ? 413 VAL A CG1 1 ATOM 3170 C CG2 . VAL A 1 413 ? -51.864 27.568 61.616 1.00 18.18 ? 413 VAL A CG2 1 ATOM 3171 N N . GLU A 1 414 ? -53.635 23.922 59.413 1.00 17.89 ? 414 GLU A N 1 ATOM 3172 C CA . GLU A 1 414 ? -53.526 22.727 58.563 1.00 18.93 ? 414 GLU A CA 1 ATOM 3173 C C . GLU A 1 414 ? -54.583 22.765 57.473 1.00 18.84 ? 414 GLU A C 1 ATOM 3174 O O . GLU A 1 414 ? -54.275 22.427 56.324 1.00 18.55 ? 414 GLU A O 1 ATOM 3175 C CB . GLU A 1 414 ? -53.618 21.467 59.411 1.00 19.45 ? 414 GLU A CB 1 ATOM 3176 C CG . GLU A 1 414 ? -53.405 20.152 58.646 1.00 20.07 ? 414 GLU A CG 1 ATOM 3177 C CD . GLU A 1 414 ? -52.007 19.976 58.056 1.00 20.94 ? 414 GLU A CD 1 ATOM 3178 O OE1 . GLU A 1 414 ? -51.113 20.811 58.350 1.00 21.48 ? 414 GLU A OE1 1 ATOM 3179 O OE2 . GLU A 1 414 ? -51.765 18.959 57.330 1.00 21.58 ? 414 GLU A OE2 1 ATOM 3180 N N . ASP A 1 415 ? -55.832 23.133 57.819 1.00 19.60 ? 415 ASP A N 1 ATOM 3181 C CA . ASP A 1 415 ? -56.875 23.363 56.799 1.00 20.63 ? 415 ASP A CA 1 ATOM 3182 C C . ASP A 1 415 ? -56.445 24.310 55.698 1.00 19.99 ? 415 ASP A C 1 ATOM 3183 O O . ASP A 1 415 ? -56.678 24.040 54.507 1.00 18.97 ? 415 ASP A O 1 ATOM 3184 C CB . ASP A 1 415 ? -58.181 23.859 57.425 1.00 22.86 ? 415 ASP A CB 1 ATOM 3185 C CG . ASP A 1 415 ? -59.374 23.619 56.543 1.00 25.68 ? 415 ASP A CG 1 ATOM 3186 O OD1 . ASP A 1 415 ? -59.556 22.515 56.005 1.00 29.27 ? 415 ASP A OD1 1 ATOM 3187 O OD2 . ASP A 1 415 ? -60.105 24.563 56.320 1.00 29.43 ? 415 ASP A OD2 1 ATOM 3188 N N . THR A 1 416 ? -55.873 25.450 56.110 1.00 19.00 ? 416 THR A N 1 ATOM 3189 C CA . THR A 1 416 ? -55.405 26.473 55.215 1.00 18.29 ? 416 THR A CA 1 ATOM 3190 C C . THR A 1 416 ? -54.384 25.911 54.230 1.00 16.92 ? 416 THR A C 1 ATOM 3191 O O . THR A 1 416 ? -54.496 26.119 53.028 1.00 16.18 ? 416 THR A O 1 ATOM 3192 C CB . THR A 1 416 ? -54.830 27.652 56.048 1.00 18.67 ? 416 THR A CB 1 ATOM 3193 O OG1 . THR A 1 416 ? -55.930 28.258 56.757 1.00 19.12 ? 416 THR A OG1 1 ATOM 3194 C CG2 . THR A 1 416 ? -54.166 28.737 55.140 1.00 18.22 ? 416 THR A CG2 1 ATOM 3195 N N . LYS A 1 417 ? -53.403 25.204 54.777 1.00 16.21 ? 417 LYS A N 1 ATOM 3196 C CA . LYS A 1 417 ? -52.324 24.588 54.007 1.00 16.29 ? 417 LYS A CA 1 ATOM 3197 C C . LYS A 1 417 ? -52.881 23.623 52.987 1.00 15.94 ? 417 LYS A C 1 ATOM 3198 O O . LYS A 1 417 ? -52.522 23.675 51.831 1.00 15.48 ? 417 LYS A O 1 ATOM 3199 C CB . LYS A 1 417 ? -51.353 23.859 54.919 1.00 16.10 ? 417 LYS A CB 1 ATOM 3200 C CG . LYS A 1 417 ? -50.219 23.150 54.192 1.00 16.45 ? 417 LYS A CG 1 ATOM 3201 C CD . LYS A 1 417 ? -49.215 22.513 55.136 1.00 16.77 ? 417 LYS A CD 1 ATOM 3202 C CE . LYS A 1 417 ? -48.346 21.490 54.400 1.00 17.32 ? 417 LYS A CE 1 ATOM 3203 N NZ . LYS A 1 417 ? -47.375 20.778 55.323 1.00 18.61 ? 417 LYS A NZ 1 ATOM 3204 N N . ILE A 1 418 ? -53.815 22.771 53.423 1.00 15.89 ? 418 ILE A N 1 ATOM 3205 C CA . ILE A 1 418 ? -54.345 21.733 52.547 1.00 16.08 ? 418 ILE A CA 1 ATOM 3206 C C . ILE A 1 418 ? -55.129 22.350 51.407 1.00 15.87 ? 418 ILE A C 1 ATOM 3207 O O . ILE A 1 418 ? -55.027 21.894 50.271 1.00 15.37 ? 418 ILE A O 1 ATOM 3208 C CB . ILE A 1 418 ? -55.201 20.741 53.368 1.00 16.25 ? 418 ILE A CB 1 ATOM 3209 C CG1 . ILE A 1 418 ? -54.250 19.954 54.274 1.00 16.36 ? 418 ILE A CG1 1 ATOM 3210 C CG2 . ILE A 1 418 ? -56.016 19.823 52.448 1.00 16.54 ? 418 ILE A CG2 1 ATOM 3211 C CD1 . ILE A 1 418 ? -54.930 19.061 55.317 1.00 17.76 ? 418 ILE A CD1 1 ATOM 3212 N N . ASP A 1 419 ? -55.897 23.396 51.695 1.00 15.61 ? 419 ASP A N 1 ATOM 3213 C CA . ASP A 1 419 ? -56.689 23.981 50.650 1.00 16.10 ? 419 ASP A CA 1 ATOM 3214 C C . ASP A 1 419 ? -55.771 24.653 49.637 1.00 15.48 ? 419 ASP A C 1 ATOM 3215 O O . ASP A 1 419 ? -56.078 24.644 48.445 1.00 15.75 ? 419 ASP A O 1 ATOM 3216 C CB . ASP A 1 419 ? -57.685 25.001 51.184 1.00 16.96 ? 419 ASP A CB 1 ATOM 3217 C CG . ASP A 1 419 ? -58.940 24.357 51.795 1.00 18.79 ? 419 ASP A CG 1 ATOM 3218 O OD1 . ASP A 1 419 ? -59.130 23.103 51.703 1.00 20.30 ? 419 ASP A OD1 1 ATOM 3219 O OD2 . ASP A 1 419 ? -59.708 25.147 52.384 1.00 20.53 ? 419 ASP A OD2 1 ATOM 3220 N N . LEU A 1 420 ? -54.689 25.280 50.104 1.00 15.49 ? 420 LEU A N 1 ATOM 3221 C CA . LEU A 1 420 ? -53.791 25.943 49.169 1.00 15.37 ? 420 LEU A CA 1 ATOM 3222 C C . LEU A 1 420 ? -53.065 24.921 48.246 1.00 15.35 ? 420 LEU A C 1 ATOM 3223 O O . LEU A 1 420 ? -52.954 25.141 47.043 1.00 15.14 ? 420 LEU A O 1 ATOM 3224 C CB . LEU A 1 420 ? -52.851 26.854 49.900 1.00 15.39 ? 420 LEU A CB 1 ATOM 3225 C CG . LEU A 1 420 ? -53.494 28.169 50.336 1.00 15.38 ? 420 LEU A CG 1 ATOM 3226 C CD1 . LEU A 1 420 ? -52.733 28.793 51.516 1.00 15.71 ? 420 LEU A CD1 1 ATOM 3227 C CD2 . LEU A 1 420 ? -53.650 29.111 49.145 1.00 15.89 ? 420 LEU A CD2 1 ATOM 3228 N N . TRP A 1 421 ? -52.573 23.839 48.830 1.00 15.86 ? 421 TRP A N 1 ATOM 3229 C CA . TRP A 1 421 ? -52.004 22.748 48.022 1.00 15.92 ? 421 TRP A CA 1 ATOM 3230 C C . TRP A 1 421 ? -52.964 22.070 47.092 1.00 15.91 ? 421 TRP A C 1 ATOM 3231 O O . TRP A 1 421 ? -52.594 21.717 45.973 1.00 15.49 ? 421 TRP A O 1 ATOM 3232 C CB . TRP A 1 421 ? -51.296 21.763 48.908 1.00 16.13 ? 421 TRP A CB 1 ATOM 3233 C CG . TRP A 1 421 ? -49.964 22.279 49.243 1.00 16.04 ? 421 TRP A CG 1 ATOM 3234 C CD1 . TRP A 1 421 ? -49.498 22.711 50.482 1.00 16.43 ? 421 TRP A CD1 1 ATOM 3235 C CD2 . TRP A 1 421 ? -48.859 22.559 48.301 1.00 16.31 ? 421 TRP A CD2 1 ATOM 3236 N NE1 . TRP A 1 421 ? -48.224 23.179 50.369 1.00 16.41 ? 421 TRP A NE1 1 ATOM 3237 C CE2 . TRP A 1 421 ? -47.789 23.116 49.095 1.00 16.78 ? 421 TRP A CE2 1 ATOM 3238 C CE3 . TRP A 1 421 ? -48.675 22.382 46.929 1.00 16.49 ? 421 TRP A CE3 1 ATOM 3239 C CZ2 . TRP A 1 421 ? -46.570 23.513 48.528 1.00 16.95 ? 421 TRP A CZ2 1 ATOM 3240 C CZ3 . TRP A 1 421 ? -47.445 22.773 46.378 1.00 17.42 ? 421 TRP A CZ3 1 ATOM 3241 C CH2 . TRP A 1 421 ? -46.445 23.338 47.158 1.00 17.41 ? 421 TRP A CH2 1 ATOM 3242 N N . SER A 1 422 ? -54.213 21.862 47.529 1.00 15.67 ? 422 SER A N 1 ATOM 3243 C CA . SER A 1 422 ? -55.204 21.273 46.665 1.00 16.02 ? 422 SER A CA 1 ATOM 3244 C C . SER A 1 422 ? -55.492 22.139 45.458 1.00 15.77 ? 422 SER A C 1 ATOM 3245 O O . SER A 1 422 ? -55.615 21.636 44.347 1.00 15.38 ? 422 SER A O 1 ATOM 3246 C CB . SER A 1 422 ? -56.491 20.956 47.446 1.00 16.18 ? 422 SER A CB 1 ATOM 3247 O OG . SER A 1 422 ? -56.234 20.101 48.557 1.00 16.66 ? 422 SER A OG 1 ATOM 3248 N N . TYR A 1 423 ? -55.550 23.466 45.668 1.00 15.98 ? 423 TYR A N 1 ATOM 3249 C CA . TYR A 1 423 ? -55.702 24.436 44.587 1.00 16.02 ? 423 TYR A CA 1 ATOM 3250 C C . TYR A 1 423 ? -54.469 24.354 43.650 1.00 15.69 ? 423 TYR A C 1 ATOM 3251 O O . TYR A 1 423 ? -54.602 24.257 42.427 1.00 15.55 ? 423 TYR A O 1 ATOM 3252 C CB . TYR A 1 423 ? -55.860 25.857 45.145 1.00 16.11 ? 423 TYR A CB 1 ATOM 3253 C CG . TYR A 1 423 ? -55.889 26.879 44.039 1.00 16.72 ? 423 TYR A CG 1 ATOM 3254 C CD1 . TYR A 1 423 ? -57.056 27.120 43.366 1.00 17.02 ? 423 TYR A CD1 1 ATOM 3255 C CD2 . TYR A 1 423 ? -54.733 27.546 43.615 1.00 16.70 ? 423 TYR A CD2 1 ATOM 3256 C CE1 . TYR A 1 423 ? -57.116 27.990 42.299 1.00 17.94 ? 423 TYR A CE1 1 ATOM 3257 C CE2 . TYR A 1 423 ? -54.769 28.411 42.540 1.00 17.37 ? 423 TYR A CE2 1 ATOM 3258 C CZ . TYR A 1 423 ? -55.983 28.642 41.893 1.00 18.11 ? 423 TYR A CZ 1 ATOM 3259 O OH . TYR A 1 423 ? -56.075 29.486 40.838 1.00 19.64 ? 423 TYR A OH 1 ATOM 3260 N N . ASN A 1 424 ? -53.271 24.331 44.234 1.00 15.60 ? 424 ASN A N 1 ATOM 3261 C CA . ASN A 1 424 ? -52.061 24.263 43.397 1.00 15.65 ? 424 ASN A CA 1 ATOM 3262 C C . ASN A 1 424 ? -52.066 23.010 42.524 1.00 15.71 ? 424 ASN A C 1 ATOM 3263 O O . ASN A 1 424 ? -51.754 23.099 41.346 1.00 15.83 ? 424 ASN A O 1 ATOM 3264 C CB . ASN A 1 424 ? -50.783 24.250 44.229 1.00 16.01 ? 424 ASN A CB 1 ATOM 3265 C CG . ASN A 1 424 ? -50.485 25.606 44.867 1.00 16.03 ? 424 ASN A CG 1 ATOM 3266 O OD1 . ASN A 1 424 ? -51.016 26.651 44.450 1.00 16.86 ? 424 ASN A OD1 1 ATOM 3267 N ND2 . ASN A 1 424 ? -49.623 25.601 45.843 1.00 15.94 ? 424 ASN A ND2 1 ATOM 3268 N N . ALA A 1 425 ? -52.477 21.895 43.093 1.00 15.64 ? 425 ALA A N 1 ATOM 3269 C CA . ALA A 1 425 ? -52.514 20.618 42.367 1.00 16.57 ? 425 ALA A CA 1 ATOM 3270 C C . ALA A 1 425 ? -53.508 20.701 41.228 1.00 17.39 ? 425 ALA A C 1 ATOM 3271 O O . ALA A 1 425 ? -53.224 20.266 40.092 1.00 18.15 ? 425 ALA A O 1 ATOM 3272 C CB . ALA A 1 425 ? -52.866 19.460 43.320 1.00 16.13 ? 425 ALA A CB 1 ATOM 3273 N N . GLU A 1 426 ? -54.706 21.210 41.532 1.00 18.24 ? 426 GLU A N 1 ATOM 3274 C CA . GLU A 1 426 ? -55.743 21.350 40.538 1.00 19.51 ? 426 GLU A CA 1 ATOM 3275 C C . GLU A 1 426 ? -55.297 22.221 39.337 1.00 19.32 ? 426 GLU A C 1 ATOM 3276 O O . GLU A 1 426 ? -55.422 21.824 38.171 1.00 19.39 ? 426 GLU A O 1 ATOM 3277 C CB . GLU A 1 426 ? -57.007 21.916 41.170 1.00 20.95 ? 426 GLU A CB 1 ATOM 3278 C CG . GLU A 1 426 ? -58.249 21.835 40.289 1.00 23.26 ? 426 GLU A CG 1 ATOM 3279 C CD . GLU A 1 426 ? -58.845 20.417 40.184 1.00 24.84 ? 426 GLU A CD 1 ATOM 3280 O OE1 . GLU A 1 426 ? -58.810 19.651 41.167 1.00 25.16 ? 426 GLU A OE1 1 ATOM 3281 O OE2 . GLU A 1 426 ? -59.381 20.067 39.100 1.00 28.15 ? 426 GLU A OE2 1 ATOM 3282 N N . LEU A 1 427 ? -54.779 23.399 39.618 1.00 19.08 ? 427 LEU A N 1 ATOM 3283 C CA . LEU A 1 427 ? -54.244 24.285 38.594 1.00 19.18 ? 427 LEU A CA 1 ATOM 3284 C C . LEU A 1 427 ? -53.080 23.667 37.805 1.00 18.69 ? 427 LEU A C 1 ATOM 3285 O O . LEU A 1 427 ? -53.075 23.769 36.572 1.00 18.87 ? 427 LEU A O 1 ATOM 3286 C CB . LEU A 1 427 ? -53.830 25.645 39.207 1.00 19.59 ? 427 LEU A CB 1 ATOM 3287 C CG . LEU A 1 427 ? -53.345 26.687 38.207 1.00 20.01 ? 427 LEU A CG 1 ATOM 3288 C CD1 . LEU A 1 427 ? -54.455 27.013 37.183 1.00 21.06 ? 427 LEU A CD1 1 ATOM 3289 C CD2 . LEU A 1 427 ? -52.888 27.930 38.973 1.00 21.04 ? 427 LEU A CD2 1 ATOM 3290 N N . LEU A 1 428 ? -52.134 23.037 38.483 1.00 18.10 ? 428 LEU A N 1 ATOM 3291 C CA . LEU A 1 428 ? -50.949 22.474 37.839 1.00 19.66 ? 428 LEU A CA 1 ATOM 3292 C C . LEU A 1 428 ? -51.320 21.418 36.801 1.00 18.82 ? 428 LEU A C 1 ATOM 3293 O O . LEU A 1 428 ? -50.800 21.383 35.669 1.00 18.79 ? 428 LEU A O 1 ATOM 3294 C CB . LEU A 1 428 ? -49.999 21.855 38.858 1.00 19.61 ? 428 LEU A CB 1 ATOM 3295 C CG . LEU A 1 428 ? -48.683 21.286 38.304 1.00 20.92 ? 428 LEU A CG 1 ATOM 3296 C CD1 . LEU A 1 428 ? -47.861 22.345 37.590 1.00 21.19 ? 428 LEU A CD1 1 ATOM 3297 C CD2 . LEU A 1 428 ? -47.875 20.638 39.428 1.00 20.94 ? 428 LEU A CD2 1 ATOM 3298 N N . VAL A 1 429 ? -52.238 20.563 37.187 1.00 19.59 ? 429 VAL A N 1 ATOM 3299 C CA . VAL A 1 429 ? -52.625 19.488 36.309 1.00 20.19 ? 429 VAL A CA 1 ATOM 3300 C C . VAL A 1 429 ? -53.421 20.020 35.102 1.00 20.04 ? 429 VAL A C 1 ATOM 3301 O O . VAL A 1 429 ? -53.176 19.586 33.950 1.00 20.97 ? 429 VAL A O 1 ATOM 3302 C CB . VAL A 1 429 ? -53.339 18.388 37.084 1.00 21.11 ? 429 VAL A CB 1 ATOM 3303 C CG1 . VAL A 1 429 ? -53.888 17.346 36.111 1.00 23.15 ? 429 VAL A CG1 1 ATOM 3304 C CG2 . VAL A 1 429 ? -52.356 17.757 38.071 1.00 21.35 ? 429 VAL A CG2 1 ATOM 3305 N N . ALA A 1 430 ? -54.296 21.001 35.324 1.00 19.42 ? 430 ALA A N 1 ATOM 3306 C CA . ALA A 1 430 ? -55.036 21.613 34.242 1.00 20.44 ? 430 ALA A CA 1 ATOM 3307 C C . ALA A 1 430 ? -54.061 22.319 33.239 1.00 20.41 ? 430 ALA A C 1 ATOM 3308 O O . ALA A 1 430 ? -54.180 22.144 31.998 1.00 21.27 ? 430 ALA A O 1 ATOM 3309 C CB . ALA A 1 430 ? -56.058 22.608 34.783 1.00 19.55 ? 430 ALA A CB 1 ATOM 3310 N N . LEU A 1 431 ? -53.134 23.086 33.786 1.00 20.18 ? 431 LEU A N 1 ATOM 3311 C CA . LEU A 1 431 ? -52.096 23.760 32.994 1.00 21.56 ? 431 LEU A CA 1 ATOM 3312 C C . LEU A 1 431 ? -51.189 22.805 32.203 1.00 21.25 ? 431 LEU A C 1 ATOM 3313 O O . LEU A 1 431 ? -50.950 23.055 31.014 1.00 22.17 ? 431 LEU A O 1 ATOM 3314 C CB . LEU A 1 431 ? -51.250 24.678 33.846 1.00 21.50 ? 431 LEU A CB 1 ATOM 3315 C CG . LEU A 1 431 ? -51.893 25.981 34.334 1.00 22.35 ? 431 LEU A CG 1 ATOM 3316 C CD1 . LEU A 1 431 ? -50.957 26.695 35.294 1.00 21.93 ? 431 LEU A CD1 1 ATOM 3317 C CD2 . LEU A 1 431 ? -52.325 26.925 33.213 1.00 23.03 ? 431 LEU A CD2 1 ATOM 3318 N N . GLU A 1 432 ? -50.649 21.792 32.876 1.00 21.43 ? 432 GLU A N 1 ATOM 3319 C CA . GLU A 1 432 ? -49.836 20.771 32.241 1.00 22.19 ? 432 GLU A CA 1 ATOM 3320 C C . GLU A 1 432 ? -50.612 20.057 31.132 1.00 21.68 ? 432 GLU A C 1 ATOM 3321 O O . GLU A 1 432 ? -50.061 19.834 30.048 1.00 21.18 ? 432 GLU A O 1 ATOM 3322 C CB . GLU A 1 432 ? -49.314 19.791 33.253 1.00 23.49 ? 432 GLU A CB 1 ATOM 3323 C CG . GLU A 1 432 ? -48.302 20.403 34.177 1.00 25.41 ? 432 GLU A CG 1 ATOM 3324 C CD . GLU A 1 432 ? -46.911 20.477 33.628 1.00 29.19 ? 432 GLU A CD 1 ATOM 3325 O OE1 . GLU A 1 432 ? -46.677 20.317 32.402 1.00 31.08 ? 432 GLU A OE1 1 ATOM 3326 O OE2 . GLU A 1 432 ? -46.045 20.707 34.480 1.00 32.57 ? 432 GLU A OE2 1 ATOM 3327 N N . ASN A 1 433 ? -51.872 19.702 31.404 1.00 20.72 ? 433 ASN A N 1 ATOM 3328 C CA . ASN A 1 433 ? -52.684 18.997 30.419 1.00 20.80 ? 433 ASN A CA 1 ATOM 3329 C C . ASN A 1 433 ? -52.994 19.849 29.189 1.00 21.55 ? 433 ASN A C 1 ATOM 3330 O O . ASN A 1 433 ? -52.924 19.364 28.046 1.00 21.14 ? 433 ASN A O 1 ATOM 3331 C CB . ASN A 1 433 ? -53.975 18.466 31.052 1.00 20.61 ? 433 ASN A CB 1 ATOM 3332 C CG . ASN A 1 433 ? -53.734 17.308 31.986 1.00 20.24 ? 433 ASN A CG 1 ATOM 3333 O OD1 . ASN A 1 433 ? -52.642 16.763 32.056 1.00 20.86 ? 433 ASN A OD1 1 ATOM 3334 N ND2 . ASN A 1 433 ? -54.764 16.922 32.731 1.00 20.32 ? 433 ASN A ND2 1 ATOM 3335 N N . GLN A 1 434 ? -53.268 21.139 29.404 1.00 21.70 ? 434 GLN A N 1 ATOM 3336 C CA . GLN A 1 434 ? -53.439 22.066 28.328 1.00 23.52 ? 434 GLN A CA 1 ATOM 3337 C C . GLN A 1 434 ? -52.150 22.156 27.495 1.00 22.90 ? 434 GLN A C 1 ATOM 3338 O O . GLN A 1 434 ? -52.202 22.153 26.266 1.00 22.88 ? 434 GLN A O 1 ATOM 3339 C CB . GLN A 1 434 ? -53.818 23.470 28.830 1.00 25.66 ? 434 GLN A CB 1 ATOM 3340 C CG . GLN A 1 434 ? -54.184 24.410 27.692 1.00 27.86 ? 434 GLN A CG 1 ATOM 3341 C CD . GLN A 1 434 ? -55.439 23.961 26.977 1.00 31.07 ? 434 GLN A CD 1 ATOM 3342 O OE1 . GLN A 1 434 ? -56.504 23.792 27.609 1.00 33.19 ? 434 GLN A OE1 1 ATOM 3343 N NE2 . GLN A 1 434 ? -55.311 23.649 25.664 1.00 35.76 ? 434 GLN A NE2 1 ATOM 3344 N N . HIS A 1 435 ? -51.025 22.163 28.166 1.00 23.48 ? 435 HIS A N 1 ATOM 3345 C CA . HIS A 1 435 ? -49.725 22.267 27.484 1.00 24.65 ? 435 HIS A CA 1 ATOM 3346 C C . HIS A 1 435 ? -49.412 21.017 26.650 1.00 24.35 ? 435 HIS A C 1 ATOM 3347 O O . HIS A 1 435 ? -48.919 21.123 25.518 1.00 24.73 ? 435 HIS A O 1 ATOM 3348 C CB . HIS A 1 435 ? -48.642 22.518 28.503 1.00 25.75 ? 435 HIS A CB 1 ATOM 3349 C CG . HIS A 1 435 ? -47.260 22.594 27.916 1.00 27.93 ? 435 HIS A CG 1 ATOM 3350 N ND1 . HIS A 1 435 ? -46.397 21.526 27.941 1.00 30.37 ? 435 HIS A ND1 1 ATOM 3351 C CD2 . HIS A 1 435 ? -46.593 23.633 27.288 1.00 29.83 ? 435 HIS A CD2 1 ATOM 3352 C CE1 . HIS A 1 435 ? -45.240 21.890 27.342 1.00 31.14 ? 435 HIS A CE1 1 ATOM 3353 N NE2 . HIS A 1 435 ? -45.353 23.189 26.968 1.00 31.60 ? 435 HIS A NE2 1 ATOM 3354 N N . THR A 1 436 ? -49.733 19.862 27.197 1.00 23.14 ? 436 THR A N 1 ATOM 3355 C CA . THR A 1 436 ? -49.616 18.572 26.490 1.00 23.43 ? 436 THR A CA 1 ATOM 3356 C C . THR A 1 436 ? -50.519 18.504 25.245 1.00 24.02 ? 436 THR A C 1 ATOM 3357 O O . THR A 1 436 ? -50.044 18.102 24.153 1.00 24.83 ? 436 THR A O 1 ATOM 3358 C CB . THR A 1 436 ? -49.860 17.412 27.456 1.00 23.31 ? 436 THR A CB 1 ATOM 3359 O OG1 . THR A 1 436 ? -48.849 17.413 28.482 1.00 24.05 ? 436 THR A OG1 1 ATOM 3360 C CG2 . THR A 1 436 ? -49.845 16.020 26.701 1.00 23.57 ? 436 THR A CG2 1 ATOM 3361 N N . ILE A 1 437 ? -51.795 18.888 25.366 1.00 23.23 ? 437 ILE A N 1 ATOM 3362 C CA . ILE A 1 437 ? -52.672 18.953 24.203 1.00 25.08 ? 437 ILE A CA 1 ATOM 3363 C C . ILE A 1 437 ? -52.053 19.910 23.154 1.00 25.63 ? 437 ILE A C 1 ATOM 3364 O O . ILE A 1 437 ? -51.976 19.579 21.956 1.00 24.91 ? 437 ILE A O 1 ATOM 3365 C CB . ILE A 1 437 ? -54.102 19.386 24.593 1.00 25.16 ? 437 ILE A CB 1 ATOM 3366 C CG1 . ILE A 1 437 ? -54.744 18.356 25.500 1.00 25.41 ? 437 ILE A CG1 1 ATOM 3367 C CG2 . ILE A 1 437 ? -54.976 19.627 23.366 1.00 25.54 ? 437 ILE A CG2 1 ATOM 3368 C CD1 . ILE A 1 437 ? -54.675 16.950 24.971 1.00 26.42 ? 437 ILE A CD1 1 ATOM 3369 N N . ASP A 1 438 ? -51.601 21.083 23.600 1.00 24.89 ? 438 ASP A N 1 ATOM 3370 C CA . ASP A 1 438 ? -50.918 22.056 22.711 1.00 26.84 ? 438 ASP A CA 1 ATOM 3371 C C . ASP A 1 438 ? -49.622 21.569 22.041 1.00 25.36 ? 438 ASP A C 1 ATOM 3372 O O . ASP A 1 438 ? -49.470 21.741 20.851 1.00 27.98 ? 438 ASP A O 1 ATOM 3373 C CB . ASP A 1 438 ? -50.623 23.354 23.447 1.00 28.05 ? 438 ASP A CB 1 ATOM 3374 C CG . ASP A 1 438 ? -51.878 24.132 23.823 1.00 30.10 ? 438 ASP A CG 1 ATOM 3375 O OD1 . ASP A 1 438 ? -52.982 23.763 23.401 1.00 33.43 ? 438 ASP A OD1 1 ATOM 3376 O OD2 . ASP A 1 438 ? -51.733 25.109 24.608 1.00 32.89 ? 438 ASP A OD2 1 ATOM 3377 N N . LEU A 1 439 ? -48.731 20.940 22.772 1.00 24.88 ? 439 LEU A N 1 ATOM 3378 C CA . LEU A 1 439 ? -47.482 20.456 22.223 1.00 25.84 ? 439 LEU A CA 1 ATOM 3379 C C . LEU A 1 439 ? -47.725 19.264 21.237 1.00 26.63 ? 439 LEU A C 1 ATOM 3380 O O . LEU A 1 439 ? -47.046 19.162 20.225 1.00 26.72 ? 439 LEU A O 1 ATOM 3381 C CB . LEU A 1 439 ? -46.495 20.058 23.319 1.00 26.74 ? 439 LEU A CB 1 ATOM 3382 C CG . LEU A 1 439 ? -46.506 18.716 24.102 1.00 27.02 ? 439 LEU A CG 1 ATOM 3383 C CD1 . LEU A 1 439 ? -45.869 17.513 23.364 1.00 27.49 ? 439 LEU A CD1 1 ATOM 3384 C CD2 . LEU A 1 439 ? -45.773 18.921 25.443 1.00 27.42 ? 439 LEU A CD2 1 ATOM 3385 N N . THR A 1 440 ? -48.723 18.431 21.508 1.00 25.65 ? 440 THR A N 1 ATOM 3386 C CA . THR A 1 440 ? -48.987 17.287 20.623 1.00 26.88 ? 440 THR A CA 1 ATOM 3387 C C . THR A 1 440 ? -49.727 17.727 19.368 1.00 28.33 ? 440 THR A C 1 ATOM 3388 O O . THR A 1 440 ? -49.479 17.202 18.244 1.00 31.34 ? 440 THR A O 1 ATOM 3389 C CB . THR A 1 440 ? -49.750 16.170 21.342 1.00 26.19 ? 440 THR A CB 1 ATOM 3390 O OG1 . THR A 1 440 ? -50.915 16.691 21.987 1.00 25.90 ? 440 THR A OG1 1 ATOM 3391 C CG2 . THR A 1 440 ? -48.865 15.448 22.331 1.00 26.03 ? 440 THR A CG2 1 ATOM 3392 N N . ASP A 1 441 ? -50.652 18.671 19.528 1.00 27.39 ? 441 ASP A N 1 ATOM 3393 C CA . ASP A 1 441 ? -51.288 19.294 18.387 1.00 28.58 ? 441 ASP A CA 1 ATOM 3394 C C . ASP A 1 441 ? -50.213 20.011 17.522 1.00 30.06 ? 441 ASP A C 1 ATOM 3395 O O . ASP A 1 441 ? -50.270 19.984 16.265 1.00 29.74 ? 441 ASP A O 1 ATOM 3396 C CB . ASP A 1 441 ? -52.339 20.309 18.806 1.00 28.96 ? 441 ASP A CB 1 ATOM 3397 C CG . ASP A 1 441 ? -53.675 19.688 19.260 1.00 30.53 ? 441 ASP A CG 1 ATOM 3398 O OD1 . ASP A 1 441 ? -53.898 18.454 19.214 1.00 31.78 ? 441 ASP A OD1 1 ATOM 3399 O OD2 . ASP A 1 441 ? -54.549 20.479 19.696 1.00 31.23 ? 441 ASP A OD2 1 ATOM 3400 N N . SER A 1 442 ? -49.291 20.695 18.197 1.00 30.83 ? 442 SER A N 1 ATOM 3401 C CA . SER A 1 442 ? -48.234 21.430 17.497 1.00 31.82 ? 442 SER A CA 1 ATOM 3402 C C . SER A 1 442 ? -47.340 20.508 16.651 1.00 31.21 ? 442 SER A C 1 ATOM 3403 O O . SER A 1 442 ? -47.026 20.872 15.523 1.00 32.39 ? 442 SER A O 1 ATOM 3404 C CB . SER A 1 442 ? -47.390 22.267 18.456 1.00 32.15 ? 442 SER A CB 1 ATOM 3405 O OG . SER A 1 442 ? -46.403 22.963 17.709 1.00 33.30 ? 442 SER A OG 1 ATOM 3406 N N . GLU A 1 443 ? -46.929 19.352 17.172 1.00 30.94 ? 443 GLU A N 1 ATOM 3407 C CA . GLU A 1 443 ? -46.110 18.417 16.376 1.00 32.24 ? 443 GLU A CA 1 ATOM 3408 C C . GLU A 1 443 ? -46.839 17.999 15.108 1.00 31.33 ? 443 GLU A C 1 ATOM 3409 O O . GLU A 1 443 ? -46.211 17.948 14.073 1.00 31.56 ? 443 GLU A O 1 ATOM 3410 C CB . GLU A 1 443 ? -45.627 17.183 17.152 1.00 33.42 ? 443 GLU A CB 1 ATOM 3411 C CG . GLU A 1 443 ? -44.597 17.448 18.241 1.00 35.28 ? 443 GLU A CG 1 ATOM 3412 C CD . GLU A 1 443 ? -43.351 18.190 17.757 1.00 37.25 ? 443 GLU A CD 1 ATOM 3413 O OE1 . GLU A 1 443 ? -42.824 17.897 16.659 1.00 39.91 ? 443 GLU A OE1 1 ATOM 3414 O OE2 . GLU A 1 443 ? -42.890 19.076 18.489 1.00 38.50 ? 443 GLU A OE2 1 ATOM 3415 N N . MET A 1 444 ? -48.158 17.777 15.165 1.00 30.76 ? 444 MET A N 1 ATOM 3416 C CA . MET A 1 444 ? -48.950 17.421 13.973 1.00 30.80 ? 444 MET A CA 1 ATOM 3417 C C . MET A 1 444 ? -48.937 18.576 12.966 1.00 32.74 ? 444 MET A C 1 ATOM 3418 O O . MET A 1 444 ? -48.710 18.373 11.761 1.00 30.14 ? 444 MET A O 1 ATOM 3419 C CB . MET A 1 444 ? -50.404 17.099 14.346 1.00 30.44 ? 444 MET A CB 1 ATOM 3420 C CG . MET A 1 444 ? -51.308 16.681 13.201 1.00 30.52 ? 444 MET A CG 1 ATOM 3421 S SD . MET A 1 444 ? -50.952 14.976 12.678 1.00 29.75 ? 444 MET A SD 1 ATOM 3422 C CE . MET A 1 444 ? -49.616 15.201 11.506 1.00 32.83 ? 444 MET A CE 1 ATOM 3423 N N . ASN A 1 445 ? -49.190 19.783 13.462 1.00 31.67 ? 445 ASN A N 1 ATOM 3424 C CA . ASN A 1 445 ? -49.227 20.967 12.599 1.00 34.05 ? 445 ASN A CA 1 ATOM 3425 C C . ASN A 1 445 ? -47.863 21.245 11.966 1.00 31.72 ? 445 ASN A C 1 ATOM 3426 O O . ASN A 1 445 ? -47.795 21.570 10.795 1.00 33.07 ? 445 ASN A O 1 ATOM 3427 C CB . ASN A 1 445 ? -49.724 22.209 13.380 1.00 36.44 ? 445 ASN A CB 1 ATOM 3428 C CG . ASN A 1 445 ? -51.177 22.070 13.846 1.00 40.56 ? 445 ASN A CG 1 ATOM 3429 O OD1 . ASN A 1 445 ? -51.513 22.434 14.983 1.00 48.17 ? 445 ASN A OD1 1 ATOM 3430 N ND2 . ASN A 1 445 ? -52.036 21.565 12.980 1.00 37.02 ? 445 ASN A ND2 1 ATOM 3431 N N . LYS A 1 446 ? -46.792 21.055 12.719 1.00 32.47 ? 446 LYS A N 1 ATOM 3432 C CA . LYS A 1 446 ? -45.433 21.275 12.199 1.00 35.03 ? 446 LYS A CA 1 ATOM 3433 C C . LYS A 1 446 ? -45.089 20.260 11.076 1.00 35.21 ? 446 LYS A C 1 ATOM 3434 O O . LYS A 1 446 ? -44.454 20.617 10.074 1.00 34.25 ? 446 LYS A O 1 ATOM 3435 C CB . LYS A 1 446 ? -44.390 21.194 13.307 1.00 37.40 ? 446 LYS A CB 1 ATOM 3436 C CG . LYS A 1 446 ? -44.256 22.482 14.131 1.00 39.55 ? 446 LYS A CG 1 ATOM 3437 C CD . LYS A 1 446 ? -43.805 22.213 15.561 1.00 41.83 ? 446 LYS A CD 1 ATOM 3438 C CE . LYS A 1 446 ? -42.389 21.688 15.674 1.00 43.32 ? 446 LYS A CE 1 ATOM 3439 N NZ . LYS A 1 446 ? -42.033 21.425 17.104 1.00 46.33 ? 446 LYS A NZ 1 ATOM 3440 N N . LEU A 1 447 ? -45.540 19.023 11.235 1.00 33.37 ? 447 LEU A N 1 ATOM 3441 C CA . LEU A 1 447 ? -45.261 18.000 10.249 1.00 32.90 ? 447 LEU A CA 1 ATOM 3442 C C . LEU A 1 447 ? -45.998 18.324 8.961 1.00 32.62 ? 447 LEU A C 1 ATOM 3443 O O . LEU A 1 447 ? -45.448 18.180 7.867 1.00 33.08 ? 447 LEU A O 1 ATOM 3444 C CB . LEU A 1 447 ? -45.665 16.636 10.795 1.00 33.93 ? 447 LEU A CB 1 ATOM 3445 C CG . LEU A 1 447 ? -45.401 15.437 9.877 1.00 35.27 ? 447 LEU A CG 1 ATOM 3446 C CD1 . LEU A 1 447 ? -43.908 15.349 9.526 1.00 36.32 ? 447 LEU A CD1 1 ATOM 3447 C CD2 . LEU A 1 447 ? -45.906 14.179 10.553 1.00 35.02 ? 447 LEU A CD2 1 ATOM 3448 N N . PHE A 1 448 ? -47.254 18.742 9.074 1.00 31.13 ? 448 PHE A N 1 ATOM 3449 C CA . PHE A 1 448 ? -48.001 19.151 7.916 1.00 30.92 ? 448 PHE A CA 1 ATOM 3450 C C . PHE A 1 448 ? -47.302 20.305 7.219 1.00 32.36 ? 448 PHE A C 1 ATOM 3451 O O . PHE A 1 448 ? -47.210 20.326 5.994 1.00 31.76 ? 448 PHE A O 1 ATOM 3452 C CB . PHE A 1 448 ? -49.417 19.556 8.305 1.00 30.22 ? 448 PHE A CB 1 ATOM 3453 C CG . PHE A 1 448 ? -50.322 19.835 7.149 1.00 30.95 ? 448 PHE A CG 1 ATOM 3454 C CD1 . PHE A 1 448 ? -50.944 18.813 6.470 1.00 30.82 ? 448 PHE A CD1 1 ATOM 3455 C CD2 . PHE A 1 448 ? -50.563 21.136 6.733 1.00 32.22 ? 448 PHE A CD2 1 ATOM 3456 C CE1 . PHE A 1 448 ? -51.786 19.065 5.411 1.00 31.35 ? 448 PHE A CE1 1 ATOM 3457 C CE2 . PHE A 1 448 ? -51.411 21.393 5.668 1.00 31.28 ? 448 PHE A CE2 1 ATOM 3458 C CZ . PHE A 1 448 ? -52.031 20.358 5.010 1.00 32.12 ? 448 PHE A CZ 1 ATOM 3459 N N . GLU A 1 449 ? -46.872 21.302 7.986 1.00 34.38 ? 449 GLU A N 1 ATOM 3460 C CA . GLU A 1 449 ? -46.288 22.494 7.373 1.00 37.65 ? 449 GLU A CA 1 ATOM 3461 C C . GLU A 1 449 ? -44.987 22.203 6.677 1.00 34.67 ? 449 GLU A C 1 ATOM 3462 O O . GLU A 1 449 ? -44.761 22.724 5.602 1.00 34.88 ? 449 GLU A O 1 ATOM 3463 C CB . GLU A 1 449 ? -46.090 23.621 8.405 1.00 43.16 ? 449 GLU A CB 1 ATOM 3464 C CG . GLU A 1 449 ? -47.380 24.337 8.767 1.00 48.46 ? 449 GLU A CG 1 ATOM 3465 C CD . GLU A 1 449 ? -48.078 24.950 7.552 1.00 53.27 ? 449 GLU A CD 1 ATOM 3466 O OE1 . GLU A 1 449 ? -47.409 25.725 6.812 1.00 55.24 ? 449 GLU A OE1 1 ATOM 3467 O OE2 . GLU A 1 449 ? -49.288 24.643 7.335 1.00 53.02 ? 449 GLU A OE2 1 ATOM 3468 N N . ARG A 1 450 ? -44.136 21.380 7.271 1.00 35.71 ? 450 ARG A N 1 ATOM 3469 C CA . ARG A 1 450 ? -42.867 21.021 6.645 1.00 37.85 ? 450 ARG A CA 1 ATOM 3470 C C . ARG A 1 450 ? -43.097 20.283 5.311 1.00 35.29 ? 450 ARG A C 1 ATOM 3471 O O . ARG A 1 450 ? -42.419 20.548 4.321 1.00 35.63 ? 450 ARG A O 1 ATOM 3472 C CB . ARG A 1 450 ? -41.946 20.258 7.623 1.00 42.30 ? 450 ARG A CB 1 ATOM 3473 C CG . ARG A 1 450 ? -41.902 18.729 7.570 1.00 45.69 ? 450 ARG A CG 1 ATOM 3474 C CD . ARG A 1 450 ? -40.865 18.129 8.551 1.00 50.05 ? 450 ARG A CD 1 ATOM 3475 N NE . ARG A 1 450 ? -41.068 18.614 9.920 1.00 53.84 ? 450 ARG A NE 1 ATOM 3476 C CZ . ARG A 1 450 ? -41.336 17.861 11.000 1.00 56.37 ? 450 ARG A CZ 1 ATOM 3477 N NH1 . ARG A 1 450 ? -41.376 16.522 10.957 1.00 57.10 ? 450 ARG A NH1 1 ATOM 3478 N NH2 . ARG A 1 450 ? -41.534 18.461 12.163 1.00 55.75 ? 450 ARG A NH2 1 ATOM 3479 N N . THR A 1 451 ? -44.085 19.405 5.283 1.00 32.26 ? 451 THR A N 1 ATOM 3480 C CA . THR A 1 451 ? -44.434 18.659 4.066 1.00 30.62 ? 451 THR A CA 1 ATOM 3481 C C . THR A 1 451 ? -44.934 19.625 3.009 1.00 30.63 ? 451 THR A C 1 ATOM 3482 O O . THR A 1 451 ? -44.503 19.576 1.867 1.00 31.28 ? 451 THR A O 1 ATOM 3483 C CB . THR A 1 451 ? -45.494 17.578 4.399 1.00 29.04 ? 451 THR A CB 1 ATOM 3484 O OG1 . THR A 1 451 ? -45.026 16.763 5.482 1.00 29.38 ? 451 THR A OG1 1 ATOM 3485 C CG2 . THR A 1 451 ? -45.781 16.701 3.222 1.00 26.68 ? 451 THR A CG2 1 ATOM 3486 N N . LYS A 1 452 ? -45.825 20.526 3.403 1.00 32.60 ? 452 LYS A N 1 ATOM 3487 C CA . LYS A 1 452 ? -46.341 21.551 2.521 1.00 34.09 ? 452 LYS A CA 1 ATOM 3488 C C . LYS A 1 452 ? -45.195 22.338 1.876 1.00 35.60 ? 452 LYS A C 1 ATOM 3489 O O . LYS A 1 452 ? -45.214 22.593 0.640 1.00 32.58 ? 452 LYS A O 1 ATOM 3490 C CB . LYS A 1 452 ? -47.262 22.504 3.279 1.00 37.40 ? 452 LYS A CB 1 ATOM 3491 C CG . LYS A 1 452 ? -47.767 23.650 2.420 1.00 40.41 ? 452 LYS A CG 1 ATOM 3492 C CD . LYS A 1 452 ? -48.742 24.533 3.167 1.00 45.05 ? 452 LYS A CD 1 ATOM 3493 C CE . LYS A 1 452 ? -49.455 25.441 2.177 1.00 48.87 ? 452 LYS A CE 1 ATOM 3494 N NZ . LYS A 1 452 ? -50.189 24.617 1.157 1.00 50.71 ? 452 LYS A NZ 1 ATOM 3495 N N . LYS A 1 453 ? -44.191 22.670 2.688 1.00 35.99 ? 453 LYS A N 1 ATOM 3496 C CA . LYS A 1 453 ? -43.059 23.463 2.198 1.00 38.28 ? 453 LYS A CA 1 ATOM 3497 C C . LYS A 1 453 ? -42.220 22.687 1.180 1.00 36.42 ? 453 LYS A C 1 ATOM 3498 O O . LYS A 1 453 ? -41.804 23.271 0.188 1.00 35.81 ? 453 LYS A O 1 ATOM 3499 C CB . LYS A 1 453 ? -42.172 23.996 3.338 1.00 41.12 ? 453 LYS A CB 1 ATOM 3500 C CG . LYS A 1 453 ? -42.859 24.829 4.419 1.00 43.71 ? 453 LYS A CG 1 ATOM 3501 C CD . LYS A 1 453 ? -43.398 26.178 3.942 1.00 45.10 ? 453 LYS A CD 1 ATOM 3502 C CE . LYS A 1 453 ? -44.271 26.872 4.989 1.00 46.57 ? 453 LYS A CE 1 ATOM 3503 N NZ . LYS A 1 453 ? -43.667 28.052 5.657 1.00 47.34 ? 453 LYS A NZ 1 ATOM 3504 N N . GLN A 1 454 ? -42.000 21.383 1.405 1.00 34.71 ? 454 GLN A N 1 ATOM 3505 C CA . GLN A 1 454 ? -41.232 20.565 0.491 1.00 35.34 ? 454 GLN A CA 1 ATOM 3506 C C . GLN A 1 454 ? -41.891 20.516 -0.884 1.00 33.07 ? 454 GLN A C 1 ATOM 3507 O O . GLN A 1 454 ? -41.211 20.558 -1.904 1.00 31.71 ? 454 GLN A O 1 ATOM 3508 C CB . GLN A 1 454 ? -41.129 19.120 0.972 1.00 36.46 ? 454 GLN A CB 1 ATOM 3509 C CG . GLN A 1 454 ? -40.010 18.838 1.934 1.00 40.42 ? 454 GLN A CG 1 ATOM 3510 C CD . GLN A 1 454 ? -39.974 17.380 2.335 1.00 40.21 ? 454 GLN A CD 1 ATOM 3511 O OE1 . GLN A 1 454 ? -40.675 16.959 3.255 1.00 40.96 ? 454 GLN A OE1 1 ATOM 3512 N NE2 . GLN A 1 454 ? -39.133 16.618 1.676 1.00 39.63 ? 454 GLN A NE2 1 ATOM 3513 N N . LEU A 1 455 ? -43.215 20.368 -0.886 1.00 30.59 ? 455 LEU A N 1 ATOM 3514 C CA . LEU A 1 455 ? -43.970 20.148 -2.120 1.00 29.03 ? 455 LEU A CA 1 ATOM 3515 C C . LEU A 1 455 ? -44.041 21.363 -3.021 1.00 28.74 ? 455 LEU A C 1 ATOM 3516 O O . LEU A 1 455 ? -44.198 21.216 -4.215 1.00 27.72 ? 455 LEU A O 1 ATOM 3517 C CB . LEU A 1 455 ? -45.380 19.627 -1.787 1.00 28.64 ? 455 LEU A CB 1 ATOM 3518 C CG . LEU A 1 455 ? -45.340 18.262 -1.126 1.00 28.37 ? 455 LEU A CG 1 ATOM 3519 C CD1 . LEU A 1 455 ? -46.701 17.863 -0.567 1.00 28.17 ? 455 LEU A CD1 1 ATOM 3520 C CD2 . LEU A 1 455 ? -44.849 17.183 -2.102 1.00 28.81 ? 455 LEU A CD2 1 ATOM 3521 N N . ARG A 1 456 ? -43.902 22.559 -2.457 1.00 30.68 ? 456 ARG A N 1 ATOM 3522 C CA . ARG A 1 456 ? -43.868 23.797 -3.237 1.00 33.11 ? 456 ARG A CA 1 ATOM 3523 C C . ARG A 1 456 ? -45.109 23.899 -4.128 1.00 32.44 ? 456 ARG A C 1 ATOM 3524 O O . ARG A 1 456 ? -46.219 23.781 -3.637 1.00 31.85 ? 456 ARG A O 1 ATOM 3525 C CB . ARG A 1 456 ? -42.571 23.908 -4.055 1.00 35.12 ? 456 ARG A CB 1 ATOM 3526 C CG . ARG A 1 456 ? -41.336 24.257 -3.253 1.00 37.71 ? 456 ARG A CG 1 ATOM 3527 C CD . ARG A 1 456 ? -41.289 25.740 -2.910 1.00 39.71 ? 456 ARG A CD 1 ATOM 3528 N NE . ARG A 1 456 ? -40.980 26.611 -4.057 1.00 41.34 ? 456 ARG A NE 1 ATOM 3529 C CZ . ARG A 1 456 ? -39.761 27.020 -4.415 1.00 43.02 ? 456 ARG A CZ 1 ATOM 3530 N NH1 . ARG A 1 456 ? -38.666 26.616 -3.765 1.00 44.76 ? 456 ARG A NH1 1 ATOM 3531 N NH2 . ARG A 1 456 ? -39.623 27.832 -5.454 1.00 43.54 ? 456 ARG A NH2 1 ATOM 3532 N N . GLU A 1 457 ? -44.922 24.037 -5.430 1.00 32.77 ? 457 GLU A N 1 ATOM 3533 C CA . GLU A 1 457 ? -46.026 24.214 -6.356 1.00 34.20 ? 457 GLU A CA 1 ATOM 3534 C C . GLU A 1 457 ? -46.492 22.874 -6.948 1.00 32.14 ? 457 GLU A C 1 ATOM 3535 O O . GLU A 1 457 ? -47.282 22.857 -7.895 1.00 32.75 ? 457 GLU A O 1 ATOM 3536 C CB . GLU A 1 457 ? -45.594 25.157 -7.478 1.00 36.99 ? 457 GLU A CB 1 ATOM 3537 C CG . GLU A 1 457 ? -45.273 26.550 -6.973 1.00 40.24 ? 457 GLU A CG 1 ATOM 3538 C CD . GLU A 1 457 ? -46.424 27.154 -6.214 1.00 41.68 ? 457 GLU A CD 1 ATOM 3539 O OE1 . GLU A 1 457 ? -47.547 27.074 -6.730 1.00 47.06 ? 457 GLU A OE1 1 ATOM 3540 O OE2 . GLU A 1 457 ? -46.231 27.704 -5.114 1.00 42.63 ? 457 GLU A OE2 1 ATOM 3541 N N . ASN A 1 458 ? -46.013 21.759 -6.402 1.00 30.17 ? 458 ASN A N 1 ATOM 3542 C CA . ASN A 1 458 ? -46.306 20.433 -6.991 1.00 28.87 ? 458 ASN A CA 1 ATOM 3543 C C . ASN A 1 458 ? -47.525 19.752 -6.382 1.00 27.81 ? 458 ASN A C 1 ATOM 3544 O O . ASN A 1 458 ? -47.918 18.672 -6.818 1.00 27.99 ? 458 ASN A O 1 ATOM 3545 C CB . ASN A 1 458 ? -45.097 19.513 -6.842 1.00 28.09 ? 458 ASN A CB 1 ATOM 3546 C CG . ASN A 1 458 ? -43.882 20.046 -7.568 1.00 29.49 ? 458 ASN A CG 1 ATOM 3547 O OD1 . ASN A 1 458 ? -43.975 21.040 -8.294 1.00 29.82 ? 458 ASN A OD1 1 ATOM 3548 N ND2 . ASN A 1 458 ? -42.747 19.364 -7.418 1.00 30.64 ? 458 ASN A ND2 1 ATOM 3549 N N . ALA A 1 459 ? -48.101 20.380 -5.370 1.00 27.38 ? 459 ALA A N 1 ATOM 3550 C CA . ALA A 1 459 ? -49.241 19.817 -4.653 1.00 26.91 ? 459 ALA A CA 1 ATOM 3551 C C . ALA A 1 459 ? -50.200 20.889 -4.206 1.00 28.63 ? 459 ALA A C 1 ATOM 3552 O O . ALA A 1 459 ? -49.819 22.071 -4.054 1.00 29.97 ? 459 ALA A O 1 ATOM 3553 C CB . ALA A 1 459 ? -48.754 19.015 -3.457 1.00 26.11 ? 459 ALA A CB 1 ATOM 3554 N N . GLU A 1 460 ? -51.445 20.490 -3.977 1.00 28.10 ? 460 GLU A N 1 ATOM 3555 C CA . GLU A 1 460 ? -52.443 21.347 -3.360 1.00 30.09 ? 460 GLU A CA 1 ATOM 3556 C C . GLU A 1 460 ? -53.001 20.711 -2.089 1.00 30.69 ? 460 GLU A C 1 ATOM 3557 O O . GLU A 1 460 ? -53.136 19.483 -1.980 1.00 29.97 ? 460 GLU A O 1 ATOM 3558 C CB . GLU A 1 460 ? -53.562 21.658 -4.345 1.00 31.10 ? 460 GLU A CB 1 ATOM 3559 C CG . GLU A 1 460 ? -53.124 22.598 -5.443 1.00 30.93 ? 460 GLU A CG 1 ATOM 3560 C CD . GLU A 1 460 ? -54.162 22.814 -6.527 1.00 32.35 ? 460 GLU A CD 1 ATOM 3561 O OE1 . GLU A 1 460 ? -55.380 22.597 -6.281 1.00 33.46 ? 460 GLU A OE1 1 ATOM 3562 O OE2 . GLU A 1 460 ? -53.746 23.198 -7.635 1.00 31.57 ? 460 GLU A OE2 1 ATOM 3563 N N . ASP A 1 461 ? -53.289 21.560 -1.116 1.00 32.23 ? 461 ASP A N 1 ATOM 3564 C CA . ASP A 1 461 ? -53.904 21.156 0.132 1.00 33.75 ? 461 ASP A CA 1 ATOM 3565 C C . ASP A 1 461 ? -55.407 20.833 -0.061 1.00 35.32 ? 461 ASP A C 1 ATOM 3566 O O . ASP A 1 461 ? -56.183 21.721 -0.411 1.00 36.02 ? 461 ASP A O 1 ATOM 3567 C CB . ASP A 1 461 ? -53.752 22.320 1.117 1.00 35.22 ? 461 ASP A CB 1 ATOM 3568 C CG . ASP A 1 461 ? -54.205 21.992 2.505 1.00 36.47 ? 461 ASP A CG 1 ATOM 3569 O OD1 . ASP A 1 461 ? -54.922 20.990 2.729 1.00 37.09 ? 461 ASP A OD1 1 ATOM 3570 O OD2 . ASP A 1 461 ? -53.855 22.790 3.407 1.00 40.28 ? 461 ASP A OD2 1 ATOM 3571 N N . MET A 1 462 ? -55.805 19.584 0.178 1.00 34.60 ? 462 MET A N 1 ATOM 3572 C CA . MET A 1 462 ? -57.209 19.151 -0.021 1.00 37.77 ? 462 MET A CA 1 ATOM 3573 C C . MET A 1 462 ? -58.129 19.459 1.171 1.00 40.29 ? 462 MET A C 1 ATOM 3574 O O . MET A 1 462 ? -59.327 19.123 1.144 1.00 43.03 ? 462 MET A O 1 ATOM 3575 C CB . MET A 1 462 ? -57.266 17.646 -0.295 1.00 37.64 ? 462 MET A CB 1 ATOM 3576 C CG . MET A 1 462 ? -56.450 17.170 -1.488 1.00 38.20 ? 462 MET A CG 1 ATOM 3577 S SD . MET A 1 462 ? -56.172 15.376 -1.520 1.00 40.80 ? 462 MET A SD 1 ATOM 3578 C CE . MET A 1 462 ? -57.824 14.790 -1.142 1.00 42.63 ? 462 MET A CE 1 ATOM 3579 N N . GLY A 1 463 ? -57.583 20.049 2.230 1.00 37.95 ? 463 GLY A N 1 ATOM 3580 C CA . GLY A 1 463 ? -58.402 20.514 3.348 1.00 40.43 ? 463 GLY A CA 1 ATOM 3581 C C . GLY A 1 463 ? -58.690 19.510 4.435 1.00 39.86 ? 463 GLY A C 1 ATOM 3582 O O . GLY A 1 463 ? -59.328 19.848 5.425 1.00 41.62 ? 463 GLY A O 1 ATOM 3583 N N . ASN A 1 464 ? -58.190 18.286 4.285 1.00 37.68 ? 464 ASN A N 1 ATOM 3584 C CA . ASN A 1 464 ? -58.497 17.203 5.216 1.00 39.32 ? 464 ASN A CA 1 ATOM 3585 C C . ASN A 1 464 ? -57.231 16.606 5.832 1.00 37.17 ? 464 ASN A C 1 ATOM 3586 O O . ASN A 1 464 ? -57.250 15.478 6.321 1.00 37.43 ? 464 ASN A O 1 ATOM 3587 C CB . ASN A 1 464 ? -59.275 16.106 4.482 1.00 40.28 ? 464 ASN A CB 1 ATOM 3588 C CG . ASN A 1 464 ? -58.477 15.491 3.344 1.00 40.14 ? 464 ASN A CG 1 ATOM 3589 O OD1 . ASN A 1 464 ? -57.503 16.077 2.860 1.00 39.56 ? 464 ASN A OD1 1 ATOM 3590 N ND2 . ASN A 1 464 ? -58.888 14.307 2.901 1.00 42.21 ? 464 ASN A ND2 1 ATOM 3591 N N . GLY A 1 465 ? -56.141 17.372 5.805 1.00 34.28 ? 465 GLY A N 1 ATOM 3592 C CA . GLY A 1 465 ? -54.844 16.871 6.226 1.00 33.02 ? 465 GLY A CA 1 ATOM 3593 C C . GLY A 1 465 ? -54.072 16.135 5.152 1.00 30.70 ? 465 GLY A C 1 ATOM 3594 O O . GLY A 1 465 ? -53.051 15.525 5.457 1.00 31.63 ? 465 GLY A O 1 ATOM 3595 N N . CYS A 1 466 ? -54.532 16.215 3.907 1.00 30.08 ? 466 CYS A N 1 ATOM 3596 C CA . CYS A 1 466 ? -53.875 15.568 2.780 1.00 30.54 ? 466 CYS A CA 1 ATOM 3597 C C . CYS A 1 466 ? -53.500 16.548 1.679 1.00 29.67 ? 466 CYS A C 1 ATOM 3598 O O . CYS A 1 466 ? -54.151 17.593 1.491 1.00 29.32 ? 466 CYS A O 1 ATOM 3599 C CB . CYS A 1 466 ? -54.764 14.482 2.153 1.00 33.30 ? 466 CYS A CB 1 ATOM 3600 S SG . CYS A 1 466 ? -55.520 13.327 3.318 1.00 36.57 ? 466 CYS A SG 1 ATOM 3601 N N . PHE A 1 467 ? -52.450 16.176 0.955 1.00 28.20 ? 467 PHE A N 1 ATOM 3602 C CA . PHE A 1 467 ? -52.044 16.835 -0.278 1.00 27.32 ? 467 PHE A CA 1 ATOM 3603 C C . PHE A 1 467 ? -52.402 15.992 -1.509 1.00 28.13 ? 467 PHE A C 1 ATOM 3604 O O . PHE A 1 467 ? -52.262 14.761 -1.493 1.00 27.71 ? 467 PHE A O 1 ATOM 3605 C CB . PHE A 1 467 ? -50.534 17.081 -0.269 1.00 26.45 ? 467 PHE A CB 1 ATOM 3606 C CG . PHE A 1 467 ? -50.074 17.952 0.861 1.00 26.96 ? 467 PHE A CG 1 ATOM 3607 C CD1 . PHE A 1 467 ? -50.184 19.329 0.767 1.00 28.74 ? 467 PHE A CD1 1 ATOM 3608 C CD2 . PHE A 1 467 ? -49.567 17.391 2.010 1.00 27.05 ? 467 PHE A CD2 1 ATOM 3609 C CE1 . PHE A 1 467 ? -49.771 20.144 1.823 1.00 29.58 ? 467 PHE A CE1 1 ATOM 3610 C CE2 . PHE A 1 467 ? -49.178 18.185 3.067 1.00 28.42 ? 467 PHE A CE2 1 ATOM 3611 C CZ . PHE A 1 467 ? -49.276 19.558 2.977 1.00 29.18 ? 467 PHE A CZ 1 ATOM 3612 N N . LYS A 1 468 ? -52.906 16.663 -2.533 1.00 28.25 ? 468 LYS A N 1 ATOM 3613 C CA . LYS A 1 468 ? -52.989 16.124 -3.870 1.00 29.10 ? 468 LYS A CA 1 ATOM 3614 C C . LYS A 1 468 ? -51.705 16.519 -4.582 1.00 27.97 ? 468 LYS A C 1 ATOM 3615 O O . LYS A 1 468 ? -51.444 17.698 -4.796 1.00 27.57 ? 468 LYS A O 1 ATOM 3616 C CB . LYS A 1 468 ? -54.202 16.671 -4.610 1.00 32.70 ? 468 LYS A CB 1 ATOM 3617 C CG . LYS A 1 468 ? -54.289 16.149 -6.037 1.00 35.45 ? 468 LYS A CG 1 ATOM 3618 C CD . LYS A 1 468 ? -55.624 16.484 -6.669 1.00 39.05 ? 468 LYS A CD 1 ATOM 3619 C CE . LYS A 1 468 ? -55.687 15.978 -8.105 1.00 42.24 ? 468 LYS A CE 1 ATOM 3620 N NZ . LYS A 1 468 ? -56.993 16.327 -8.741 1.00 45.71 ? 468 LYS A NZ 1 ATOM 3621 N N . ILE A 1 469 ? -50.882 15.520 -4.885 1.00 27.31 ? 469 ILE A N 1 ATOM 3622 C CA . ILE A 1 469 ? -49.611 15.716 -5.568 1.00 27.48 ? 469 ILE A CA 1 ATOM 3623 C C . ILE A 1 469 ? -49.884 15.512 -7.061 1.00 29.20 ? 469 ILE A C 1 ATOM 3624 O O . ILE A 1 469 ? -50.377 14.460 -7.488 1.00 31.38 ? 469 ILE A O 1 ATOM 3625 C CB . ILE A 1 469 ? -48.560 14.716 -5.049 1.00 28.12 ? 469 ILE A CB 1 ATOM 3626 C CG1 . ILE A 1 469 ? -48.302 14.926 -3.547 1.00 27.39 ? 469 ILE A CG1 1 ATOM 3627 C CG2 . ILE A 1 469 ? -47.261 14.790 -5.853 1.00 27.05 ? 469 ILE A CG2 1 ATOM 3628 C CD1 . ILE A 1 469 ? -47.532 13.780 -2.929 1.00 28.82 ? 469 ILE A CD1 1 ATOM 3629 N N . TYR A 1 470 ? -49.570 16.516 -7.867 1.00 29.80 ? 470 TYR A N 1 ATOM 3630 C CA . TYR A 1 470 ? -50.011 16.539 -9.262 1.00 31.43 ? 470 TYR A CA 1 ATOM 3631 C C . TYR A 1 470 ? -49.003 15.928 -10.223 1.00 32.29 ? 470 TYR A C 1 ATOM 3632 O O . TYR A 1 470 ? -48.837 16.405 -11.345 1.00 32.62 ? 470 TYR A O 1 ATOM 3633 C CB . TYR A 1 470 ? -50.342 17.974 -9.660 1.00 31.36 ? 470 TYR A CB 1 ATOM 3634 C CG . TYR A 1 470 ? -51.684 18.435 -9.181 1.00 31.14 ? 470 TYR A CG 1 ATOM 3635 C CD1 . TYR A 1 470 ? -51.850 18.932 -7.898 1.00 30.13 ? 470 TYR A CD1 1 ATOM 3636 C CD2 . TYR A 1 470 ? -52.785 18.412 -10.021 1.00 33.35 ? 470 TYR A CD2 1 ATOM 3637 C CE1 . TYR A 1 470 ? -53.078 19.375 -7.461 1.00 31.55 ? 470 TYR A CE1 1 ATOM 3638 C CE2 . TYR A 1 470 ? -54.030 18.856 -9.589 1.00 34.19 ? 470 TYR A CE2 1 ATOM 3639 C CZ . TYR A 1 470 ? -54.166 19.332 -8.299 1.00 33.60 ? 470 TYR A CZ 1 ATOM 3640 O OH . TYR A 1 470 ? -55.381 19.779 -7.846 1.00 36.43 ? 470 TYR A OH 1 ATOM 3641 N N . HIS A 1 471 ? -48.321 14.878 -9.775 1.00 32.96 ? 471 HIS A N 1 ATOM 3642 C CA . HIS A 1 471 ? -47.403 14.136 -10.624 1.00 34.11 ? 471 HIS A CA 1 ATOM 3643 C C . HIS A 1 471 ? -47.332 12.724 -10.164 1.00 34.75 ? 471 HIS A C 1 ATOM 3644 O O . HIS A 1 471 ? -47.736 12.417 -9.058 1.00 33.56 ? 471 HIS A O 1 ATOM 3645 C CB . HIS A 1 471 ? -46.004 14.778 -10.636 1.00 33.63 ? 471 HIS A CB 1 ATOM 3646 C CG . HIS A 1 471 ? -45.295 14.781 -9.293 1.00 31.22 ? 471 HIS A CG 1 ATOM 3647 N ND1 . HIS A 1 471 ? -44.598 13.721 -8.836 1.00 32.20 ? 471 HIS A ND1 1 ATOM 3648 C CD2 . HIS A 1 471 ? -45.128 15.795 -8.355 1.00 29.73 ? 471 HIS A CD2 1 ATOM 3649 C CE1 . HIS A 1 471 ? -44.059 14.030 -7.633 1.00 30.27 ? 471 HIS A CE1 1 ATOM 3650 N NE2 . HIS A 1 471 ? -44.373 15.301 -7.351 1.00 29.93 ? 471 HIS A NE2 1 ATOM 3651 N N . LYS A 1 472 ? -46.837 11.840 -11.022 1.00 35.56 ? 472 LYS A N 1 ATOM 3652 C CA . LYS A 1 472 ? -46.667 10.452 -10.645 1.00 38.72 ? 472 LYS A CA 1 ATOM 3653 C C . LYS A 1 472 ? -45.652 10.432 -9.508 1.00 36.48 ? 472 LYS A C 1 ATOM 3654 O O . LYS A 1 472 ? -44.581 11.017 -9.637 1.00 35.68 ? 472 LYS A O 1 ATOM 3655 C CB . LYS A 1 472 ? -46.156 9.639 -11.839 1.00 41.98 ? 472 LYS A CB 1 ATOM 3656 C CG . LYS A 1 472 ? -46.111 8.143 -11.599 1.00 47.26 ? 472 LYS A CG 1 ATOM 3657 C CD . LYS A 1 472 ? -45.463 7.416 -12.776 1.00 51.16 ? 472 LYS A CD 1 ATOM 3658 C CE . LYS A 1 472 ? -45.726 5.911 -12.752 1.00 55.59 ? 472 LYS A CE 1 ATOM 3659 N NZ . LYS A 1 472 ? -45.382 5.288 -11.442 1.00 58.53 ? 472 LYS A NZ 1 ATOM 3660 N N . CYS A 1 473 ? -45.990 9.795 -8.396 1.00 35.95 ? 473 CYS A N 1 ATOM 3661 C CA . CYS A 1 473 ? -45.092 9.804 -7.224 1.00 36.68 ? 473 CYS A CA 1 ATOM 3662 C C . CYS A 1 473 ? -45.097 8.399 -6.650 1.00 37.31 ? 473 CYS A C 1 ATOM 3663 O O . CYS A 1 473 ? -45.922 8.059 -5.822 1.00 37.10 ? 473 CYS A O 1 ATOM 3664 C CB . CYS A 1 473 ? -45.481 10.927 -6.206 1.00 38.66 ? 473 CYS A CB 1 ATOM 3665 S SG . CYS A 1 473 ? -44.272 11.299 -4.878 1.00 40.89 ? 473 CYS A SG 1 ATOM 3666 N N . ASP A 1 474 ? -44.150 7.588 -7.116 1.00 37.38 ? 474 ASP A N 1 ATOM 3667 C CA . ASP A 1 474 ? -44.050 6.186 -6.743 1.00 38.34 ? 474 ASP A CA 1 ATOM 3668 C C . ASP A 1 474 ? -43.505 6.000 -5.317 1.00 38.39 ? 474 ASP A C 1 ATOM 3669 O O . ASP A 1 474 ? -43.305 6.966 -4.582 1.00 36.20 ? 474 ASP A O 1 ATOM 3670 C CB . ASP A 1 474 ? -43.215 5.422 -7.788 1.00 41.15 ? 474 ASP A CB 1 ATOM 3671 C CG . ASP A 1 474 ? -41.745 5.846 -7.838 1.00 41.71 ? 474 ASP A CG 1 ATOM 3672 O OD1 . ASP A 1 474 ? -41.238 6.568 -6.948 1.00 41.65 ? 474 ASP A OD1 1 ATOM 3673 O OD2 . ASP A 1 474 ? -41.069 5.432 -8.798 1.00 43.05 ? 474 ASP A OD2 1 ATOM 3674 N N . ASN A 1 475 ? -43.304 4.762 -4.896 1.00 38.58 ? 475 ASN A N 1 ATOM 3675 C CA . ASN A 1 475 ? -42.951 4.539 -3.503 1.00 39.08 ? 475 ASN A CA 1 ATOM 3676 C C . ASN A 1 475 ? -41.677 5.274 -3.097 1.00 37.74 ? 475 ASN A C 1 ATOM 3677 O O . ASN A 1 475 ? -41.615 5.811 -1.998 1.00 36.05 ? 475 ASN A O 1 ATOM 3678 C CB . ASN A 1 475 ? -42.856 3.054 -3.184 1.00 42.30 ? 475 ASN A CB 1 ATOM 3679 C CG . ASN A 1 475 ? -44.223 2.389 -3.075 1.00 44.06 ? 475 ASN A CG 1 ATOM 3680 O OD1 . ASN A 1 475 ? -45.277 3.055 -3.049 1.00 42.77 ? 475 ASN A OD1 1 ATOM 3681 N ND2 . ASN A 1 475 ? -44.214 1.065 -3.005 1.00 46.64 ? 475 ASN A ND2 1 ATOM 3682 N N . ALA A 1 476 ? -40.687 5.302 -3.984 1.00 38.07 ? 476 ALA A N 1 ATOM 3683 C CA . ALA A 1 476 ? -39.422 5.990 -3.707 1.00 39.08 ? 476 ALA A CA 1 ATOM 3684 C C . ALA A 1 476 ? -39.634 7.508 -3.600 1.00 36.70 ? 476 ALA A C 1 ATOM 3685 O O . ALA A 1 476 ? -39.105 8.146 -2.713 1.00 37.54 ? 476 ALA A O 1 ATOM 3686 C CB . ALA A 1 476 ? -38.375 5.651 -4.762 1.00 40.17 ? 476 ALA A CB 1 ATOM 3687 N N . CYS A 1 477 ? -40.461 8.060 -4.469 1.00 37.11 ? 477 CYS A N 1 ATOM 3688 C CA . CYS A 1 477 ? -40.812 9.475 -4.416 1.00 36.27 ? 477 CYS A CA 1 ATOM 3689 C C . CYS A 1 477 ? -41.485 9.833 -3.081 1.00 33.99 ? 477 CYS A C 1 ATOM 3690 O O . CYS A 1 477 ? -41.079 10.783 -2.405 1.00 34.31 ? 477 CYS A O 1 ATOM 3691 C CB . CYS A 1 477 ? -41.709 9.794 -5.615 1.00 38.27 ? 477 CYS A CB 1 ATOM 3692 S SG . CYS A 1 477 ? -42.337 11.478 -5.756 1.00 39.08 ? 477 CYS A SG 1 ATOM 3693 N N . ILE A 1 478 ? -42.482 9.061 -2.676 1.00 32.91 ? 478 ILE A N 1 ATOM 3694 C CA . ILE A 1 478 ? -43.119 9.270 -1.398 1.00 32.63 ? 478 ILE A CA 1 ATOM 3695 C C . ILE A 1 478 ? -42.111 9.179 -0.254 1.00 34.17 ? 478 ILE A C 1 ATOM 3696 O O . ILE A 1 478 ? -42.141 10.013 0.656 1.00 33.55 ? 478 ILE A O 1 ATOM 3697 C CB . ILE A 1 478 ? -44.278 8.295 -1.131 1.00 32.73 ? 478 ILE A CB 1 ATOM 3698 C CG1 . ILE A 1 478 ? -45.408 8.484 -2.162 1.00 31.90 ? 478 ILE A CG1 1 ATOM 3699 C CG2 . ILE A 1 478 ? -44.796 8.464 0.299 1.00 32.46 ? 478 ILE A CG2 1 ATOM 3700 C CD1 . ILE A 1 478 ? -46.092 9.834 -2.136 1.00 31.12 ? 478 ILE A CD1 1 ATOM 3701 N N . GLY A 1 479 ? -41.241 8.166 -0.288 1.00 36.05 ? 479 GLY A N 1 ATOM 3702 C CA . GLY A 1 479 ? -40.154 8.043 0.687 1.00 36.77 ? 479 GLY A CA 1 ATOM 3703 C C . GLY A 1 479 ? -39.283 9.292 0.742 1.00 37.04 ? 479 GLY A C 1 ATOM 3704 O O . GLY A 1 479 ? -38.890 9.724 1.824 1.00 37.47 ? 479 GLY A O 1 ATOM 3705 N N . SER A 1 480 ? -38.991 9.879 -0.416 1.00 36.00 ? 480 SER A N 1 ATOM 3706 C CA . SER A 1 480 ? -38.163 11.093 -0.486 1.00 37.15 ? 480 SER A CA 1 ATOM 3707 C C . SER A 1 480 ? -38.812 12.266 0.276 1.00 36.85 ? 480 SER A C 1 ATOM 3708 O O . SER A 1 480 ? -38.130 13.036 0.966 1.00 36.00 ? 480 SER A O 1 ATOM 3709 C CB . SER A 1 480 ? -37.834 11.459 -1.949 1.00 37.79 ? 480 SER A CB 1 ATOM 3710 O OG . SER A 1 480 ? -38.892 12.137 -2.646 1.00 36.41 ? 480 SER A OG 1 ATOM 3711 N N . ILE A 1 481 ? -40.135 12.357 0.182 1.00 34.27 ? 481 ILE A N 1 ATOM 3712 C CA . ILE A 1 481 ? -40.887 13.391 0.887 1.00 33.04 ? 481 ILE A CA 1 ATOM 3713 C C . ILE A 1 481 ? -40.802 13.122 2.375 1.00 34.24 ? 481 ILE A C 1 ATOM 3714 O O . ILE A 1 481 ? -40.503 14.014 3.169 1.00 36.60 ? 481 ILE A O 1 ATOM 3715 C CB . ILE A 1 481 ? -42.357 13.414 0.452 1.00 31.30 ? 481 ILE A CB 1 ATOM 3716 C CG1 . ILE A 1 481 ? -42.433 13.667 -1.052 1.00 30.77 ? 481 ILE A CG1 1 ATOM 3717 C CG2 . ILE A 1 481 ? -43.131 14.470 1.248 1.00 30.19 ? 481 ILE A CG2 1 ATOM 3718 C CD1 . ILE A 1 481 ? -43.827 13.685 -1.617 1.00 30.57 ? 481 ILE A CD1 1 ATOM 3719 N N . ARG A 1 482 ? -41.052 11.880 2.758 1.00 35.49 ? 482 ARG A N 1 ATOM 3720 C CA . ARG A 1 482 ? -40.975 11.484 4.151 1.00 37.28 ? 482 ARG A CA 1 ATOM 3721 C C . ARG A 1 482 ? -39.581 11.647 4.777 1.00 41.24 ? 482 ARG A C 1 ATOM 3722 O O . ARG A 1 482 ? -39.499 12.009 5.948 1.00 43.17 ? 482 ARG A O 1 ATOM 3723 C CB . ARG A 1 482 ? -41.426 10.037 4.309 1.00 38.46 ? 482 ARG A CB 1 ATOM 3724 C CG . ARG A 1 482 ? -42.875 9.778 3.988 1.00 37.37 ? 482 ARG A CG 1 ATOM 3725 C CD . ARG A 1 482 ? -43.309 8.398 4.445 1.00 38.46 ? 482 ARG A CD 1 ATOM 3726 N NE . ARG A 1 482 ? -42.352 7.388 4.028 1.00 41.58 ? 482 ARG A NE 1 ATOM 3727 C CZ . ARG A 1 482 ? -42.623 6.305 3.300 1.00 43.70 ? 482 ARG A CZ 1 ATOM 3728 N NH1 . ARG A 1 482 ? -43.857 6.004 2.903 1.00 43.73 ? 482 ARG A NH1 1 ATOM 3729 N NH2 . ARG A 1 482 ? -41.623 5.501 2.965 1.00 45.10 ? 482 ARG A NH2 1 ATOM 3730 N N . ASN A 1 483 ? -38.500 11.359 4.045 1.00 44.97 ? 483 ASN A N 1 ATOM 3731 C CA . ASN A 1 483 ? -37.141 11.580 4.593 1.00 51.77 ? 483 ASN A CA 1 ATOM 3732 C C . ASN A 1 483 ? -36.626 12.994 4.360 1.00 49.83 ? 483 ASN A C 1 ATOM 3733 O O . ASN A 1 483 ? -35.487 13.284 4.701 1.00 51.81 ? 483 ASN A O 1 ATOM 3734 C CB . ASN A 1 483 ? -36.042 10.668 4.023 1.00 59.58 ? 483 ASN A CB 1 ATOM 3735 C CG . ASN A 1 483 ? -36.476 9.245 3.755 1.00 66.42 ? 483 ASN A CG 1 ATOM 3736 O OD1 . ASN A 1 483 ? -37.481 8.743 4.272 1.00 66.54 ? 483 ASN A OD1 1 ATOM 3737 N ND2 . ASN A 1 483 ? -35.650 8.569 2.920 1.00 79.64 ? 483 ASN A ND2 1 ATOM 3738 N N . GLY A 1 484 ? -37.418 13.852 3.737 1.00 45.98 ? 484 GLY A N 1 ATOM 3739 C CA . GLY A 1 484 ? -37.034 15.240 3.568 1.00 46.05 ? 484 GLY A CA 1 ATOM 3740 C C . GLY A 1 484 ? -36.010 15.476 2.477 1.00 47.10 ? 484 GLY A C 1 ATOM 3741 O O . GLY A 1 484 ? -35.292 16.476 2.523 1.00 48.15 ? 484 GLY A O 1 ATOM 3742 N N . THR A 1 485 ? -35.939 14.582 1.487 1.00 45.28 ? 485 THR A N 1 ATOM 3743 C CA . THR A 1 485 ? -34.995 14.742 0.377 1.00 46.26 ? 485 THR A CA 1 ATOM 3744 C C . THR A 1 485 ? -35.680 14.950 -0.988 1.00 43.93 ? 485 THR A C 1 ATOM 3745 O O . THR A 1 485 ? -35.023 14.958 -2.008 1.00 44.85 ? 485 THR A O 1 ATOM 3746 C CB . THR A 1 485 ? -34.032 13.549 0.297 1.00 48.55 ? 485 THR A CB 1 ATOM 3747 O OG1 . THR A 1 485 ? -34.764 12.345 0.026 1.00 46.95 ? 485 THR A OG1 1 ATOM 3748 C CG2 . THR A 1 485 ? -33.278 13.412 1.620 1.00 50.42 ? 485 THR A CG2 1 ATOM 3749 N N . TYR A 1 486 ? -36.992 15.145 -0.990 1.00 41.19 ? 486 TYR A N 1 ATOM 3750 C CA . TYR A 1 486 ? -37.753 15.393 -2.229 1.00 38.77 ? 486 TYR A CA 1 ATOM 3751 C C . TYR A 1 486 ? -37.292 16.676 -2.899 1.00 39.47 ? 486 TYR A C 1 ATOM 3752 O O . TYR A 1 486 ? -37.247 17.730 -2.270 1.00 39.02 ? 486 TYR A O 1 ATOM 3753 C CB . TYR A 1 486 ? -39.234 15.473 -1.875 1.00 36.58 ? 486 TYR A CB 1 ATOM 3754 C CG . TYR A 1 486 ? -40.202 15.884 -2.959 1.00 34.66 ? 486 TYR A CG 1 ATOM 3755 C CD1 . TYR A 1 486 ? -40.777 14.939 -3.806 1.00 34.13 ? 486 TYR A CD1 1 ATOM 3756 C CD2 . TYR A 1 486 ? -40.611 17.206 -3.086 1.00 32.66 ? 486 TYR A CD2 1 ATOM 3757 C CE1 . TYR A 1 486 ? -41.700 15.319 -4.778 1.00 32.43 ? 486 TYR A CE1 1 ATOM 3758 C CE2 . TYR A 1 486 ? -41.518 17.589 -4.050 1.00 30.64 ? 486 TYR A CE2 1 ATOM 3759 C CZ . TYR A 1 486 ? -42.067 16.640 -4.889 1.00 31.53 ? 486 TYR A CZ 1 ATOM 3760 O OH . TYR A 1 486 ? -42.987 17.031 -5.830 1.00 30.15 ? 486 TYR A OH 1 ATOM 3761 N N . ASP A 1 487 ? -36.944 16.588 -4.174 1.00 39.35 ? 487 ASP A N 1 ATOM 3762 C CA . ASP A 1 487 ? -36.506 17.746 -4.938 1.00 41.19 ? 487 ASP A CA 1 ATOM 3763 C C . ASP A 1 487 ? -37.655 18.193 -5.845 1.00 38.72 ? 487 ASP A C 1 ATOM 3764 O O . ASP A 1 487 ? -37.907 17.582 -6.881 1.00 39.19 ? 487 ASP A O 1 ATOM 3765 C CB . ASP A 1 487 ? -35.273 17.378 -5.768 1.00 44.86 ? 487 ASP A CB 1 ATOM 3766 C CG . ASP A 1 487 ? -34.694 18.556 -6.542 1.00 47.22 ? 487 ASP A CG 1 ATOM 3767 O OD1 . ASP A 1 487 ? -35.363 19.610 -6.676 1.00 47.07 ? 487 ASP A OD1 1 ATOM 3768 O OD2 . ASP A 1 487 ? -33.540 18.414 -7.009 1.00 49.87 ? 487 ASP A OD2 1 ATOM 3769 N N . HIS A 1 488 ? -38.317 19.281 -5.472 1.00 36.23 ? 488 HIS A N 1 ATOM 3770 C CA . HIS A 1 488 ? -39.527 19.729 -6.183 1.00 34.43 ? 488 HIS A CA 1 ATOM 3771 C C . HIS A 1 488 ? -39.241 20.118 -7.616 1.00 35.25 ? 488 HIS A C 1 ATOM 3772 O O . HIS A 1 488 ? -40.134 20.050 -8.466 1.00 34.15 ? 488 HIS A O 1 ATOM 3773 C CB . HIS A 1 488 ? -40.163 20.891 -5.437 1.00 34.50 ? 488 HIS A CB 1 ATOM 3774 C CG . HIS A 1 488 ? -39.469 22.196 -5.685 1.00 35.91 ? 488 HIS A CG 1 ATOM 3775 N ND1 . HIS A 1 488 ? -39.942 23.107 -6.554 1.00 36.93 ? 488 HIS A ND1 1 ATOM 3776 C CD2 . HIS A 1 488 ? -38.259 22.695 -5.205 1.00 37.45 ? 488 HIS A CD2 1 ATOM 3777 C CE1 . HIS A 1 488 ? -39.083 24.156 -6.623 1.00 36.78 ? 488 HIS A CE1 1 ATOM 3778 N NE2 . HIS A 1 488 ? -38.054 23.907 -5.794 1.00 37.55 ? 488 HIS A NE2 1 ATOM 3779 N N . ASP A 1 489 ? -38.004 20.524 -7.915 1.00 37.04 ? 489 ASP A N 1 ATOM 3780 C CA . ASP A 1 489 ? -37.669 20.972 -9.274 1.00 41.27 ? 489 ASP A CA 1 ATOM 3781 C C . ASP A 1 489 ? -37.755 19.842 -10.287 1.00 40.07 ? 489 ASP A C 1 ATOM 3782 O O . ASP A 1 489 ? -38.100 20.076 -11.431 1.00 41.67 ? 489 ASP A O 1 ATOM 3783 C CB . ASP A 1 489 ? -36.265 21.603 -9.357 1.00 45.10 ? 489 ASP A CB 1 ATOM 3784 C CG . ASP A 1 489 ? -36.253 23.039 -8.910 1.00 48.96 ? 489 ASP A CG 1 ATOM 3785 O OD1 . ASP A 1 489 ? -37.139 23.797 -9.358 1.00 53.99 ? 489 ASP A OD1 1 ATOM 3786 O OD2 . ASP A 1 489 ? -35.375 23.409 -8.101 1.00 52.29 ? 489 ASP A OD2 1 ATOM 3787 N N . VAL A 1 490 ? -37.464 18.625 -9.858 1.00 41.26 ? 490 VAL A N 1 ATOM 3788 C CA . VAL A 1 490 ? -37.522 17.463 -10.754 1.00 43.05 ? 490 VAL A CA 1 ATOM 3789 C C . VAL A 1 490 ? -38.917 17.270 -11.353 1.00 40.91 ? 490 VAL A C 1 ATOM 3790 O O . VAL A 1 490 ? -39.064 16.830 -12.500 1.00 40.48 ? 490 VAL A O 1 ATOM 3791 C CB . VAL A 1 490 ? -37.116 16.171 -10.007 1.00 44.26 ? 490 VAL A CB 1 ATOM 3792 C CG1 . VAL A 1 490 ? -37.133 14.970 -10.938 1.00 50.34 ? 490 VAL A CG1 1 ATOM 3793 C CG2 . VAL A 1 490 ? -35.736 16.331 -9.388 1.00 47.21 ? 490 VAL A CG2 1 ATOM 3794 N N . TYR A 1 491 ? -39.941 17.588 -10.568 1.00 38.41 ? 491 TYR A N 1 ATOM 3795 C CA . TYR A 1 491 ? -41.336 17.276 -10.917 1.00 36.60 ? 491 TYR A CA 1 ATOM 3796 C C . TYR A 1 491 ? -42.174 18.480 -11.297 1.00 35.95 ? 491 TYR A C 1 ATOM 3797 O O . TYR A 1 491 ? -43.290 18.307 -11.752 1.00 37.65 ? 491 TYR A O 1 ATOM 3798 C CB . TYR A 1 491 ? -42.022 16.573 -9.744 1.00 34.92 ? 491 TYR A CB 1 ATOM 3799 C CG . TYR A 1 491 ? -41.323 15.340 -9.269 1.00 36.88 ? 491 TYR A CG 1 ATOM 3800 C CD1 . TYR A 1 491 ? -41.498 14.114 -9.914 1.00 38.69 ? 491 TYR A CD1 1 ATOM 3801 C CD2 . TYR A 1 491 ? -40.492 15.380 -8.157 1.00 37.54 ? 491 TYR A CD2 1 ATOM 3802 C CE1 . TYR A 1 491 ? -40.863 12.965 -9.456 1.00 39.44 ? 491 TYR A CE1 1 ATOM 3803 C CE2 . TYR A 1 491 ? -39.844 14.247 -7.708 1.00 38.91 ? 491 TYR A CE2 1 ATOM 3804 C CZ . TYR A 1 491 ? -40.037 13.041 -8.345 1.00 39.44 ? 491 TYR A CZ 1 ATOM 3805 O OH . TYR A 1 491 ? -39.381 11.928 -7.864 1.00 41.25 ? 491 TYR A OH 1 ATOM 3806 N N . ARG A 1 492 ? -41.636 19.692 -11.129 1.00 35.99 ? 492 ARG A N 1 ATOM 3807 C CA . ARG A 1 492 ? -42.409 20.921 -11.286 1.00 36.04 ? 492 ARG A CA 1 ATOM 3808 C C . ARG A 1 492 ? -43.094 21.062 -12.651 1.00 36.85 ? 492 ARG A C 1 ATOM 3809 O O . ARG A 1 492 ? -44.272 21.424 -12.730 1.00 37.06 ? 492 ARG A O 1 ATOM 3810 C CB . ARG A 1 492 ? -41.514 22.140 -11.006 1.00 35.95 ? 492 ARG A CB 1 ATOM 3811 C CG . ARG A 1 492 ? -42.218 23.473 -11.050 1.00 36.38 ? 492 ARG A CG 1 ATOM 3812 C CD . ARG A 1 492 ? -41.275 24.562 -10.582 1.00 37.55 ? 492 ARG A CD 1 ATOM 3813 N NE . ARG A 1 492 ? -41.816 25.913 -10.681 1.00 37.11 ? 492 ARG A NE 1 ATOM 3814 C CZ . ARG A 1 492 ? -42.095 26.715 -9.664 1.00 37.67 ? 492 ARG A CZ 1 ATOM 3815 N NH1 . ARG A 1 492 ? -41.965 26.308 -8.407 1.00 38.17 ? 492 ARG A NH1 1 ATOM 3816 N NH2 . ARG A 1 492 ? -42.552 27.939 -9.900 1.00 38.81 ? 492 ARG A NH2 1 ATOM 3817 N N . ASP A 1 493 ? -42.356 20.817 -13.720 1.00 38.74 ? 493 ASP A N 1 ATOM 3818 C CA . ASP A 1 493 ? -42.920 20.903 -15.071 1.00 42.75 ? 493 ASP A CA 1 ATOM 3819 C C . ASP A 1 493 ? -44.159 20.011 -15.204 1.00 40.05 ? 493 ASP A C 1 ATOM 3820 O O . ASP A 1 493 ? -45.217 20.479 -15.626 1.00 40.05 ? 493 ASP A O 1 ATOM 3821 C CB . ASP A 1 493 ? -41.878 20.519 -16.142 1.00 45.96 ? 493 ASP A CB 1 ATOM 3822 C CG . ASP A 1 493 ? -40.867 21.633 -16.419 1.00 49.26 ? 493 ASP A CG 1 ATOM 3823 O OD1 . ASP A 1 493 ? -41.019 22.731 -15.858 1.00 49.67 ? 493 ASP A OD1 1 ATOM 3824 O OD2 . ASP A 1 493 ? -39.912 21.405 -17.204 1.00 51.65 ? 493 ASP A OD2 1 ATOM 3825 N N . GLU A 1 494 ? -44.010 18.739 -14.857 1.00 38.91 ? 494 GLU A N 1 ATOM 3826 C CA . GLU A 1 494 ? -45.130 17.787 -14.895 1.00 39.53 ? 494 GLU A CA 1 ATOM 3827 C C . GLU A 1 494 ? -46.267 18.309 -14.029 1.00 38.35 ? 494 GLU A C 1 ATOM 3828 O O . GLU A 1 494 ? -47.421 18.375 -14.466 1.00 37.24 ? 494 GLU A O 1 ATOM 3829 C CB . GLU A 1 494 ? -44.692 16.418 -14.401 1.00 39.76 ? 494 GLU A CB 1 ATOM 3830 C CG . GLU A 1 494 ? -45.775 15.334 -14.436 1.00 41.77 ? 494 GLU A CG 1 ATOM 3831 C CD . GLU A 1 494 ? -45.311 14.000 -13.868 1.00 42.06 ? 494 GLU A CD 1 ATOM 3832 O OE1 . GLU A 1 494 ? -44.111 13.863 -13.543 1.00 44.23 ? 494 GLU A OE1 1 ATOM 3833 O OE2 . GLU A 1 494 ? -46.140 13.065 -13.719 1.00 41.45 ? 494 GLU A OE2 1 ATOM 3834 N N . ALA A 1 495 ? -45.928 18.715 -12.808 1.00 35.67 ? 495 ALA A N 1 ATOM 3835 C CA . ALA A 1 495 ? -46.953 19.112 -11.856 1.00 35.66 ? 495 ALA A CA 1 ATOM 3836 C C . ALA A 1 495 ? -47.727 20.344 -12.295 1.00 36.74 ? 495 ALA A C 1 ATOM 3837 O O . ALA A 1 495 ? -48.952 20.372 -12.230 1.00 37.24 ? 495 ALA A O 1 ATOM 3838 C CB . ALA A 1 495 ? -46.347 19.282 -10.458 1.00 34.16 ? 495 ALA A CB 1 ATOM 3839 N N . LEU A 1 496 ? -47.019 21.366 -12.764 1.00 38.70 ? 496 LEU A N 1 ATOM 3840 C CA . LEU A 1 496 ? -47.664 22.602 -13.218 1.00 40.44 ? 496 LEU A CA 1 ATOM 3841 C C . LEU A 1 496 ? -48.584 22.387 -14.405 1.00 42.17 ? 496 LEU A C 1 ATOM 3842 O O . LEU A 1 496 ? -49.634 23.021 -14.502 1.00 44.01 ? 496 LEU A O 1 ATOM 3843 C CB . LEU A 1 496 ? -46.620 23.662 -13.575 1.00 41.87 ? 496 LEU A CB 1 ATOM 3844 C CG . LEU A 1 496 ? -45.908 24.268 -12.364 1.00 42.94 ? 496 LEU A CG 1 ATOM 3845 C CD1 . LEU A 1 496 ? -44.837 25.228 -12.857 1.00 43.35 ? 496 LEU A CD1 1 ATOM 3846 C CD2 . LEU A 1 496 ? -46.879 24.960 -11.416 1.00 43.18 ? 496 LEU A CD2 1 ATOM 3847 N N . ASN A 1 497 ? -48.170 21.531 -15.329 1.00 42.02 ? 497 ASN A N 1 ATOM 3848 C CA A ASN A 1 497 ? -49.011 21.149 -16.460 0.50 43.48 ? 497 ASN A CA 1 ATOM 3849 C CA B ASN A 1 497 ? -49.026 21.198 -16.453 0.50 43.95 ? 497 ASN A CA 1 ATOM 3850 C C . ASN A 1 497 ? -50.311 20.489 -16.000 1.00 43.67 ? 497 ASN A C 1 ATOM 3851 O O . ASN A 1 497 ? -51.398 20.800 -16.509 1.00 44.57 ? 497 ASN A O 1 ATOM 3852 C CB A ASN A 1 497 ? -48.274 20.184 -17.388 0.50 44.40 ? 497 ASN A CB 1 ATOM 3853 C CB B ASN A 1 497 ? -48.260 20.399 -17.507 0.50 45.68 ? 497 ASN A CB 1 ATOM 3854 C CG A ASN A 1 497 ? -49.165 19.655 -18.495 0.50 46.81 ? 497 ASN A CG 1 ATOM 3855 C CG B ASN A 1 497 ? -47.508 21.297 -18.474 0.50 47.23 ? 497 ASN A CG 1 ATOM 3856 O OD1 A ASN A 1 497 ? -49.539 18.481 -18.501 0.50 47.77 ? 497 ASN A OD1 1 ATOM 3857 O OD1 B ASN A 1 497 ? -47.764 21.273 -19.673 0.50 50.80 ? 497 ASN A OD1 1 ATOM 3858 N ND2 A ASN A 1 497 ? -49.544 20.535 -19.419 0.50 49.16 ? 497 ASN A ND2 1 ATOM 3859 N ND2 B ASN A 1 497 ? -46.594 22.114 -17.952 0.50 46.23 ? 497 ASN A ND2 1 ATOM 3860 N N . ASN A 1 498 ? -50.197 19.575 -15.036 1.00 41.18 ? 498 ASN A N 1 ATOM 3861 C CA . ASN A 1 498 ? -51.380 18.901 -14.497 1.00 42.13 ? 498 ASN A CA 1 ATOM 3862 C C . ASN A 1 498 ? -52.280 19.846 -13.685 1.00 42.40 ? 498 ASN A C 1 ATOM 3863 O O . ASN A 1 498 ? -53.504 19.807 -13.806 1.00 43.32 ? 498 ASN A O 1 ATOM 3864 C CB . ASN A 1 498 ? -50.985 17.690 -13.659 1.00 40.70 ? 498 ASN A CB 1 ATOM 3865 C CG . ASN A 1 498 ? -50.506 16.536 -14.503 1.00 42.22 ? 498 ASN A CG 1 ATOM 3866 O OD1 . ASN A 1 498 ? -50.803 16.459 -15.708 1.00 45.55 ? 498 ASN A OD1 1 ATOM 3867 N ND2 . ASN A 1 498 ? -49.763 15.634 -13.896 1.00 39.86 ? 498 ASN A ND2 1 ATOM 3868 N N . ARG A 1 499 ? -51.672 20.705 -12.876 1.00 42.21 ? 499 ARG A N 1 ATOM 3869 C CA . ARG A 1 499 ? -52.441 21.660 -12.062 1.00 44.08 ? 499 ARG A CA 1 ATOM 3870 C C . ARG A 1 499 ? -53.203 22.686 -12.857 1.00 49.43 ? 499 ARG A C 1 ATOM 3871 O O . ARG A 1 499 ? -54.385 22.902 -12.608 1.00 52.16 ? 499 ARG A O 1 ATOM 3872 C CB . ARG A 1 499 ? -51.528 22.424 -11.120 1.00 42.05 ? 499 ARG A CB 1 ATOM 3873 C CG . ARG A 1 499 ? -51.196 21.666 -9.868 1.00 39.15 ? 499 ARG A CG 1 ATOM 3874 C CD . ARG A 1 499 ? -50.302 22.511 -8.992 1.00 38.61 ? 499 ARG A CD 1 ATOM 3875 N NE . ARG A 1 499 ? -51.045 23.519 -8.250 1.00 38.27 ? 499 ARG A NE 1 ATOM 3876 C CZ . ARG A 1 499 ? -50.498 24.597 -7.693 1.00 39.89 ? 499 ARG A CZ 1 ATOM 3877 N NH1 . ARG A 1 499 ? -49.194 24.841 -7.806 1.00 39.88 ? 499 ARG A NH1 1 ATOM 3878 N NH2 . ARG A 1 499 ? -51.263 25.455 -7.040 1.00 40.71 ? 499 ARG A NH2 1 ATOM 3879 N N . PHE A 1 500 ? -52.518 23.336 -13.793 1.00 52.45 ? 500 PHE A N 1 ATOM 3880 C CA . PHE A 1 500 ? -53.079 24.486 -14.494 1.00 57.40 ? 500 PHE A CA 1 ATOM 3881 C C . PHE A 1 500 ? -53.494 24.163 -15.926 1.00 62.75 ? 500 PHE A C 1 ATOM 3882 O O . PHE A 1 500 ? -53.505 25.040 -16.789 1.00 67.07 ? 500 PHE A O 1 ATOM 3883 C CB . PHE A 1 500 ? -52.120 25.687 -14.407 1.00 56.01 ? 500 PHE A CB 1 ATOM 3884 C CG . PHE A 1 500 ? -51.786 26.082 -12.989 1.00 55.84 ? 500 PHE A CG 1 ATOM 3885 C CD1 . PHE A 1 500 ? -52.796 26.270 -12.049 1.00 56.19 ? 500 PHE A CD1 1 ATOM 3886 C CD2 . PHE A 1 500 ? -50.471 26.245 -12.585 1.00 55.70 ? 500 PHE A CD2 1 ATOM 3887 C CE1 . PHE A 1 500 ? -52.505 26.610 -10.738 1.00 56.58 ? 500 PHE A CE1 1 ATOM 3888 C CE2 . PHE A 1 500 ? -50.169 26.584 -11.272 1.00 54.71 ? 500 PHE A CE2 1 ATOM 3889 C CZ . PHE A 1 500 ? -51.187 26.774 -10.347 1.00 55.83 ? 500 PHE A CZ 1 ATOM 3890 N N . GLN A 1 501 ? -53.886 22.907 -16.152 1.00 66.67 ? 501 GLN A N 1 ATOM 3891 C CA . GLN A 1 501 ? -54.543 22.504 -17.395 1.00 72.45 ? 501 GLN A CA 1 ATOM 3892 C C . GLN A 1 501 ? -55.969 23.041 -17.413 1.00 78.31 ? 501 GLN A C 1 ATOM 3893 O O . GLN A 1 501 ? -56.565 23.261 -16.350 1.00 79.41 ? 501 GLN A O 1 ATOM 3894 C CB . GLN A 1 501 ? -54.586 20.971 -17.523 1.00 73.29 ? 501 GLN A CB 1 ATOM 3895 C CG . GLN A 1 501 ? -55.523 20.269 -16.541 1.00 73.17 ? 501 GLN A CG 1 ATOM 3896 C CD . GLN A 1 501 ? -55.495 18.754 -16.663 1.00 73.58 ? 501 GLN A CD 1 ATOM 3897 O OE1 . GLN A 1 501 ? -54.935 18.060 -15.813 1.00 70.37 ? 501 GLN A OE1 1 ATOM 3898 N NE2 . GLN A 1 501 ? -56.107 18.233 -17.724 1.00 76.95 ? 501 GLN A NE2 1 ATOM 3899 N N . ILE A 1 502 ? -56.515 23.230 -18.615 1.00 83.16 ? 502 ILE A N 1 ATOM 3900 C CA . ILE A 1 502 ? -57.937 23.547 -18.788 1.00 86.94 ? 502 ILE A CA 1 ATOM 3901 C C . ILE A 1 502 ? -58.671 22.211 -18.944 1.00 88.85 ? 502 ILE A C 1 ATOM 3902 O O . ILE A 1 502 ? -58.397 21.458 -19.882 1.00 90.66 ? 502 ILE A O 1 ATOM 3903 C CB . ILE A 1 502 ? -58.229 24.442 -20.029 1.00 90.83 ? 502 ILE A CB 1 ATOM 3904 C CG1 . ILE A 1 502 ? -57.102 25.453 -20.298 1.00 90.05 ? 502 ILE A CG1 1 ATOM 3905 C CG2 . ILE A 1 502 ? -59.558 25.170 -19.860 1.00 93.06 ? 502 ILE A CG2 1 ATOM 3906 C CD1 . ILE A 1 502 ? -56.052 24.968 -21.284 1.00 88.88 ? 502 ILE A CD1 1 ATOM 3907 N N . LYS A 1 503 ? -59.579 21.907 -18.018 1.00 88.66 ? 503 LYS A N 1 ATOM 3908 C CA . LYS A 1 503 ? -60.357 20.669 -18.070 1.00 89.84 ? 503 LYS A CA 1 ATOM 3909 C C . LYS A 1 503 ? -61.668 20.892 -18.816 1.00 94.63 ? 503 LYS A C 1 ATOM 3910 O O . LYS A 1 503 ? -62.288 19.944 -19.298 1.00 96.65 ? 503 LYS A O 1 ATOM 3911 C CB . LYS A 1 503 ? -60.642 20.154 -16.659 1.00 87.99 ? 503 LYS A CB 1 ATOM 3912 C CG . LYS A 1 503 ? -59.393 19.795 -15.869 1.00 83.58 ? 503 LYS A CG 1 ATOM 3913 C CD . LYS A 1 503 ? -59.722 19.391 -14.440 1.00 82.24 ? 503 LYS A CD 1 ATOM 3914 C CE . LYS A 1 503 ? -60.451 18.057 -14.379 1.00 84.01 ? 503 LYS A CE 1 ATOM 3915 N NZ . LYS A 1 503 ? -60.526 17.517 -12.992 1.00 80.68 ? 503 LYS A NZ 1 HETATM 3916 C C1 . NAG B 2 . ? -49.198 5.529 29.754 1.00 47.81 ? 801 NAG A C1 1 HETATM 3917 C C2 . NAG B 2 . ? -48.412 4.317 29.244 1.00 56.39 ? 801 NAG A C2 1 HETATM 3918 C C3 . NAG B 2 . ? -47.468 3.745 30.296 1.00 58.24 ? 801 NAG A C3 1 HETATM 3919 C C4 . NAG B 2 . ? -46.569 4.866 30.815 1.00 58.41 ? 801 NAG A C4 1 HETATM 3920 C C5 . NAG B 2 . ? -47.417 6.035 31.356 1.00 57.64 ? 801 NAG A C5 1 HETATM 3921 C C6 . NAG B 2 . ? -46.539 7.197 31.831 1.00 56.05 ? 801 NAG A C6 1 HETATM 3922 C C7 . NAG B 2 . ? -49.578 3.033 27.542 1.00 61.98 ? 801 NAG A C7 1 HETATM 3923 C C8 . NAG B 2 . ? -50.631 1.999 27.267 1.00 60.31 ? 801 NAG A C8 1 HETATM 3924 N N2 . NAG B 2 . ? -49.379 3.321 28.823 1.00 58.55 ? 801 NAG A N2 1 HETATM 3925 O O3 . NAG B 2 . ? -46.680 2.727 29.713 1.00 58.53 ? 801 NAG A O3 1 HETATM 3926 O O4 . NAG B 2 . ? -45.666 4.354 31.785 1.00 59.12 ? 801 NAG A O4 1 HETATM 3927 O O5 . NAG B 2 . ? -48.358 6.511 30.390 1.00 50.73 ? 801 NAG A O5 1 HETATM 3928 O O6 . NAG B 2 . ? -45.796 7.723 30.746 1.00 58.19 ? 801 NAG A O6 1 HETATM 3929 O O7 . NAG B 2 . ? -48.947 3.565 26.622 1.00 62.05 ? 801 NAG A O7 1 HETATM 3930 C C1 . NAG C 2 . ? -49.456 -5.454 76.171 1.00 47.03 ? 802 NAG A C1 1 HETATM 3931 C C2 . NAG C 2 . ? -48.577 -6.697 76.155 1.00 53.12 ? 802 NAG A C2 1 HETATM 3932 C C3 . NAG C 2 . ? -49.410 -7.954 75.903 1.00 56.68 ? 802 NAG A C3 1 HETATM 3933 C C4 . NAG C 2 . ? -50.570 -8.008 76.894 1.00 57.94 ? 802 NAG A C4 1 HETATM 3934 C C5 . NAG C 2 . ? -51.366 -6.702 76.767 1.00 57.47 ? 802 NAG A C5 1 HETATM 3935 C C6 . NAG C 2 . ? -52.636 -6.640 77.617 1.00 56.52 ? 802 NAG A C6 1 HETATM 3936 C C7 . NAG C 2 . ? -46.243 -6.434 75.518 1.00 56.77 ? 802 NAG A C7 1 HETATM 3937 C C8 . NAG C 2 . ? -45.210 -6.353 74.424 1.00 57.51 ? 802 NAG A C8 1 HETATM 3938 N N2 . NAG C 2 . ? -47.517 -6.600 75.159 1.00 56.06 ? 802 NAG A N2 1 HETATM 3939 O O3 . NAG C 2 . ? -48.575 -9.083 76.022 1.00 56.96 ? 802 NAG A O3 1 HETATM 3940 O O4 . NAG C 2 . ? -51.373 -9.143 76.632 1.00 65.42 ? 802 NAG A O4 1 HETATM 3941 O O5 . NAG C 2 . ? -50.504 -5.624 77.112 1.00 50.82 ? 802 NAG A O5 1 HETATM 3942 O O6 . NAG C 2 . ? -52.321 -6.335 78.960 1.00 57.73 ? 802 NAG A O6 1 HETATM 3943 O O7 . NAG C 2 . ? -45.912 -6.337 76.697 1.00 59.57 ? 802 NAG A O7 1 HETATM 3944 C C1 . NAG D 2 . ? -31.565 2.929 95.431 1.00 56.41 ? 804 NAG A C1 1 HETATM 3945 C C2 . NAG D 2 . ? -30.313 2.593 96.256 1.00 66.74 ? 804 NAG A C2 1 HETATM 3946 C C3 . NAG D 2 . ? -29.095 2.409 95.354 1.00 70.30 ? 804 NAG A C3 1 HETATM 3947 C C4 . NAG D 2 . ? -29.384 1.341 94.305 1.00 73.12 ? 804 NAG A C4 1 HETATM 3948 C C5 . NAG D 2 . ? -30.681 1.637 93.548 1.00 72.75 ? 804 NAG A C5 1 HETATM 3949 C C6 . NAG D 2 . ? -31.073 0.422 92.700 1.00 73.51 ? 804 NAG A C6 1 HETATM 3950 C C7 . NAG D 2 . ? -30.407 3.518 98.520 1.00 67.83 ? 804 NAG A C7 1 HETATM 3951 C C8 . NAG D 2 . ? -30.000 4.657 99.412 1.00 63.48 ? 804 NAG A C8 1 HETATM 3952 N N2 . NAG D 2 . ? -30.009 3.609 97.249 1.00 66.51 ? 804 NAG A N2 1 HETATM 3953 O O3 . NAG D 2 . ? -27.983 2.013 96.131 1.00 75.25 ? 804 NAG A O3 1 HETATM 3954 O O4 . NAG D 2 . ? -28.317 1.269 93.385 1.00 79.52 ? 804 NAG A O4 1 HETATM 3955 O O5 . NAG D 2 . ? -31.748 1.928 94.438 1.00 62.15 ? 804 NAG A O5 1 HETATM 3956 O O6 . NAG D 2 . ? -32.242 0.694 91.957 1.00 72.66 ? 804 NAG A O6 1 HETATM 3957 O O7 . NAG D 2 . ? -31.072 2.577 98.958 1.00 66.66 ? 804 NAG A O7 1 HETATM 3958 C C1 . NAG E 2 . ? -28.353 26.217 99.015 1.00 43.95 ? 805 NAG A C1 1 HETATM 3959 C C2 . NAG E 2 . ? -27.926 27.448 99.831 1.00 47.07 ? 805 NAG A C2 1 HETATM 3960 C C3 . NAG E 2 . ? -27.108 28.448 99.023 1.00 46.56 ? 805 NAG A C3 1 HETATM 3961 C C4 . NAG E 2 . ? -26.012 27.773 98.236 1.00 47.31 ? 805 NAG A C4 1 HETATM 3962 C C5 . NAG E 2 . ? -26.652 26.678 97.387 1.00 46.74 ? 805 NAG A C5 1 HETATM 3963 C C6 . NAG E 2 . ? -25.642 25.987 96.475 1.00 46.68 ? 805 NAG A C6 1 HETATM 3964 C C7 . NAG E 2 . ? -29.322 28.048 101.782 1.00 56.55 ? 805 NAG A C7 1 HETATM 3965 C C8 . NAG E 2 . ? -30.518 28.807 102.277 1.00 52.80 ? 805 NAG A C8 1 HETATM 3966 N N2 . NAG E 2 . ? -29.059 28.117 100.455 1.00 50.59 ? 805 NAG A N2 1 HETATM 3967 O O3 . NAG E 2 . ? -26.518 29.418 99.859 1.00 47.62 ? 805 NAG A O3 1 HETATM 3968 O O4 . NAG E 2 . ? -25.475 28.771 97.408 1.00 48.97 ? 805 NAG A O4 1 HETATM 3969 O O5 . NAG E 2 . ? -27.303 25.718 98.211 1.00 43.99 ? 805 NAG A O5 1 HETATM 3970 O O6 . NAG E 2 . ? -24.835 25.106 97.217 1.00 52.26 ? 805 NAG A O6 1 HETATM 3971 O O7 . NAG E 2 . ? -28.657 27.409 102.607 1.00 53.63 ? 805 NAG A O7 1 HETATM 3972 C C1 . NAG F 2 . ? -24.078 29.039 97.607 1.00 54.00 ? 806 NAG A C1 1 HETATM 3973 C C2 . NAG F 2 . ? -23.603 29.772 96.361 1.00 52.83 ? 806 NAG A C2 1 HETATM 3974 C C3 . NAG F 2 . ? -22.137 30.206 96.463 1.00 57.13 ? 806 NAG A C3 1 HETATM 3975 C C4 . NAG F 2 . ? -21.767 30.802 97.828 1.00 63.73 ? 806 NAG A C4 1 HETATM 3976 C C5 . NAG F 2 . ? -22.403 29.970 98.952 1.00 62.21 ? 806 NAG A C5 1 HETATM 3977 C C6 . NAG F 2 . ? -22.177 30.554 100.347 1.00 62.68 ? 806 NAG A C6 1 HETATM 3978 C C7 . NAG F 2 . ? -24.651 29.103 94.234 1.00 52.53 ? 806 NAG A C7 1 HETATM 3979 C C8 . NAG F 2 . ? -24.685 28.052 93.159 1.00 49.94 ? 806 NAG A C8 1 HETATM 3980 N N2 . NAG F 2 . ? -23.787 28.886 95.227 1.00 53.25 ? 806 NAG A N2 1 HETATM 3981 O O3 . NAG F 2 . ? -21.855 31.154 95.453 1.00 52.13 ? 806 NAG A O3 1 HETATM 3982 O O4 . NAG F 2 . ? -20.340 30.814 97.937 1.00 72.43 ? 806 NAG A O4 1 HETATM 3983 O O5 . NAG F 2 . ? -23.800 29.848 98.737 1.00 55.30 ? 806 NAG A O5 1 HETATM 3984 O O6 . NAG F 2 . ? -22.433 31.944 100.350 1.00 67.03 ? 806 NAG A O6 1 HETATM 3985 O O7 . NAG F 2 . ? -25.373 30.098 94.163 1.00 50.44 ? 806 NAG A O7 1 HETATM 3986 C C1 . MAN G 3 . ? -19.713 32.101 98.189 1.00 79.24 ? 807 MAN A C1 1 HETATM 3987 C C2 . MAN G 3 . ? -18.713 32.480 97.095 1.00 82.02 ? 807 MAN A C2 1 HETATM 3988 C C3 . MAN G 3 . ? -18.065 33.846 97.364 1.00 84.42 ? 807 MAN A C3 1 HETATM 3989 C C4 . MAN G 3 . ? -18.420 34.393 98.745 1.00 85.36 ? 807 MAN A C4 1 HETATM 3990 C C5 . MAN G 3 . ? -18.396 33.315 99.834 1.00 86.65 ? 807 MAN A C5 1 HETATM 3991 C C6 . MAN G 3 . ? -19.139 33.786 101.083 1.00 88.72 ? 807 MAN A C6 1 HETATM 3992 O O2 . MAN G 3 . ? -19.338 32.487 95.807 1.00 80.48 ? 807 MAN A O2 1 HETATM 3993 O O3 . MAN G 3 . ? -18.455 34.818 96.380 1.00 81.17 ? 807 MAN A O3 1 HETATM 3994 O O4 . MAN G 3 . ? -17.485 35.418 99.092 1.00 84.60 ? 807 MAN A O4 1 HETATM 3995 O O5 . MAN G 3 . ? -18.971 32.073 99.409 1.00 83.32 ? 807 MAN A O5 1 HETATM 3996 O O6 . MAN G 3 . ? -18.363 34.781 101.763 1.00 88.50 ? 807 MAN A O6 1 HETATM 3997 C C1 . NAG H 2 . ? -34.658 25.441 100.923 1.00 56.38 ? 808 NAG A C1 1 HETATM 3998 C C2 . NAG H 2 . ? -35.969 25.351 101.712 1.00 59.77 ? 808 NAG A C2 1 HETATM 3999 C C3 . NAG H 2 . ? -35.859 26.207 102.965 1.00 66.28 ? 808 NAG A C3 1 HETATM 4000 C C4 . NAG H 2 . ? -34.628 25.809 103.775 1.00 69.67 ? 808 NAG A C4 1 HETATM 4001 C C5 . NAG H 2 . ? -33.365 25.758 102.906 1.00 68.07 ? 808 NAG A C5 1 HETATM 4002 C C6 . NAG H 2 . ? -32.206 25.134 103.681 1.00 67.59 ? 808 NAG A C6 1 HETATM 4003 C C7 . NAG H 2 . ? -38.181 25.094 100.659 1.00 58.81 ? 808 NAG A C7 1 HETATM 4004 C C8 . NAG H 2 . ? -39.262 25.762 99.862 1.00 62.99 ? 808 NAG A C8 1 HETATM 4005 N N2 . NAG H 2 . ? -37.110 25.833 100.949 1.00 56.49 ? 808 NAG A N2 1 HETATM 4006 O O3 . NAG H 2 . ? -37.050 26.079 103.719 1.00 65.57 ? 808 NAG A O3 1 HETATM 4007 O O4 . NAG H 2 . ? -34.452 26.737 104.831 1.00 79.18 ? 808 NAG A O4 1 HETATM 4008 O O5 . NAG H 2 . ? -33.565 25.003 101.717 1.00 60.74 ? 808 NAG A O5 1 HETATM 4009 O O6 . NAG H 2 . ? -31.011 25.346 102.965 1.00 71.42 ? 808 NAG A O6 1 HETATM 4010 O O7 . NAG H 2 . ? -38.326 23.928 101.004 1.00 60.53 ? 808 NAG A O7 1 HETATM 4011 C C1 . NAG I 2 . ? -34.533 26.124 106.137 1.00 83.73 ? 809 NAG A C1 1 HETATM 4012 C C2 . NAG I 2 . ? -34.068 27.176 107.148 1.00 85.26 ? 809 NAG A C2 1 HETATM 4013 C C3 . NAG I 2 . ? -34.345 26.763 108.595 1.00 88.12 ? 809 NAG A C3 1 HETATM 4014 C C4 . NAG I 2 . ? -35.737 26.158 108.765 1.00 92.33 ? 809 NAG A C4 1 HETATM 4015 C C5 . NAG I 2 . ? -35.953 25.063 107.720 1.00 90.65 ? 809 NAG A C5 1 HETATM 4016 C C6 . NAG I 2 . ? -37.303 24.347 107.857 1.00 90.10 ? 809 NAG A C6 1 HETATM 4017 C C7 . NAG I 2 . ? -32.148 28.567 106.450 1.00 77.23 ? 809 NAG A C7 1 HETATM 4018 C C8 . NAG I 2 . ? -30.656 28.641 106.283 1.00 74.74 ? 809 NAG A C8 1 HETATM 4019 N N2 . NAG I 2 . ? -32.644 27.422 106.932 1.00 82.90 ? 809 NAG A N2 1 HETATM 4020 O O3 . NAG I 2 . ? -34.238 27.885 109.437 1.00 89.11 ? 809 NAG A O3 1 HETATM 4021 O O4 . NAG I 2 . ? -35.863 25.656 110.080 1.00 94.13 ? 809 NAG A O4 1 HETATM 4022 O O5 . NAG I 2 . ? -35.835 25.654 106.437 1.00 87.56 ? 809 NAG A O5 1 HETATM 4023 O O6 . NAG I 2 . ? -38.320 24.979 107.107 1.00 86.00 ? 809 NAG A O6 1 HETATM 4024 O O7 . NAG I 2 . ? -32.843 29.537 106.154 1.00 75.35 ? 809 NAG A O7 1 HETATM 4025 C C1 . NAG J 2 . ? -56.025 6.809 56.697 1.00 44.73 ? 811 NAG A C1 1 HETATM 4026 C C2 . NAG J 2 . ? -57.202 6.388 55.747 1.00 50.63 ? 811 NAG A C2 1 HETATM 4027 C C3 . NAG J 2 . ? -58.440 7.297 55.897 1.00 54.73 ? 811 NAG A C3 1 HETATM 4028 C C4 . NAG J 2 . ? -58.816 7.473 57.356 1.00 56.63 ? 811 NAG A C4 1 HETATM 4029 C C5 . NAG J 2 . ? -57.568 7.725 58.221 1.00 57.47 ? 811 NAG A C5 1 HETATM 4030 C C6 . NAG J 2 . ? -57.917 7.790 59.707 1.00 55.03 ? 811 NAG A C6 1 HETATM 4031 C C7 . NAG J 2 . ? -56.756 5.015 53.690 1.00 49.74 ? 811 NAG A C7 1 HETATM 4032 C C8 . NAG J 2 . ? -56.763 3.763 54.510 1.00 45.89 ? 811 NAG A C8 1 HETATM 4033 N N2 . NAG J 2 . ? -56.935 6.221 54.305 1.00 46.15 ? 811 NAG A N2 1 HETATM 4034 O O3 . NAG J 2 . ? -59.567 6.822 55.174 1.00 58.73 ? 811 NAG A O3 1 HETATM 4035 O O4 . NAG J 2 . ? -59.679 8.590 57.416 1.00 59.85 ? 811 NAG A O4 1 HETATM 4036 O O5 . NAG J 2 . ? -56.546 6.741 58.001 1.00 48.62 ? 811 NAG A O5 1 HETATM 4037 O O6 . NAG J 2 . ? -56.699 8.056 60.364 1.00 61.78 ? 811 NAG A O6 1 HETATM 4038 O O7 . NAG J 2 . ? -56.557 4.874 52.471 1.00 51.56 ? 811 NAG A O7 1 HETATM 4039 C C1 . NAG K 2 . ? -24.655 16.747 101.516 1.00 78.08 ? 812 NAG A C1 1 HETATM 4040 C C2 . NAG K 2 . ? -23.159 17.018 101.683 1.00 86.87 ? 812 NAG A C2 1 HETATM 4041 C C3 . NAG K 2 . ? -22.814 17.469 103.096 1.00 89.19 ? 812 NAG A C3 1 HETATM 4042 C C4 . NAG K 2 . ? -23.662 18.692 103.419 1.00 91.19 ? 812 NAG A C4 1 HETATM 4043 C C5 . NAG K 2 . ? -25.146 18.330 103.324 1.00 93.68 ? 812 NAG A C5 1 HETATM 4044 C C6 . NAG K 2 . ? -26.025 19.568 103.537 1.00 94.01 ? 812 NAG A C6 1 HETATM 4045 C C7 . NAG K 2 . ? -21.509 15.809 100.278 1.00 85.82 ? 812 NAG A C7 1 HETATM 4046 C C8 . NAG K 2 . ? -21.242 17.061 99.482 1.00 80.90 ? 812 NAG A C8 1 HETATM 4047 N N2 . NAG K 2 . ? -22.394 15.840 101.284 1.00 86.38 ? 812 NAG A N2 1 HETATM 4048 O O3 . NAG K 2 . ? -21.443 17.795 103.173 1.00 87.72 ? 812 NAG A O3 1 HETATM 4049 O O4 . NAG K 2 . ? -23.349 19.177 104.707 1.00 90.26 ? 812 NAG A O4 1 HETATM 4050 O O5 . NAG K 2 . ? -25.476 17.771 102.059 1.00 86.63 ? 812 NAG A O5 1 HETATM 4051 O O6 . NAG K 2 . ? -27.092 19.272 104.412 1.00 91.92 ? 812 NAG A O6 1 HETATM 4052 O O7 . NAG K 2 . ? -20.904 14.776 99.995 1.00 83.20 ? 812 NAG A O7 1 HETATM 4053 C C1 . NAG L 2 . ? -35.623 7.242 2.318 1.00 79.27 ? 813 NAG A C1 1 HETATM 4054 C C2 . NAG L 2 . ? -36.714 6.197 2.618 1.00 87.40 ? 813 NAG A C2 1 HETATM 4055 C C3 . NAG L 2 . ? -36.955 5.167 1.489 1.00 92.13 ? 813 NAG A C3 1 HETATM 4056 C C4 . NAG L 2 . ? -36.690 5.697 0.078 1.00 91.65 ? 813 NAG A C4 1 HETATM 4057 C C5 . NAG L 2 . ? -35.398 6.497 0.056 1.00 92.78 ? 813 NAG A C5 1 HETATM 4058 C C6 . NAG L 2 . ? -35.092 7.053 -1.330 1.00 94.39 ? 813 NAG A C6 1 HETATM 4059 C C7 . NAG L 2 . ? -35.567 4.634 4.213 1.00 91.43 ? 813 NAG A C7 1 HETATM 4060 C C8 . NAG L 2 . ? -35.552 4.118 5.627 1.00 89.06 ? 813 NAG A C8 1 HETATM 4061 N N2 . NAG L 2 . ? -36.504 5.554 3.924 1.00 90.21 ? 813 NAG A N2 1 HETATM 4062 O O3 . NAG L 2 . ? -38.273 4.658 1.558 1.00 93.39 ? 813 NAG A O3 1 HETATM 4063 O O4 . NAG L 2 . ? -36.591 4.624 -0.833 1.00 92.46 ? 813 NAG A O4 1 HETATM 4064 O O5 . NAG L 2 . ? -35.557 7.573 0.941 1.00 82.71 ? 813 NAG A O5 1 HETATM 4065 O O6 . NAG L 2 . ? -34.566 8.356 -1.201 1.00 98.50 ? 813 NAG A O6 1 HETATM 4066 O O7 . NAG L 2 . ? -34.737 4.199 3.414 1.00 91.65 ? 813 NAG A O7 1 HETATM 4067 N N1 . EPE M 4 . ? -35.070 0.100 88.964 1.00 78.66 ? 1504 EPE A N1 1 HETATM 4068 C C2 . EPE M 4 . ? -35.278 -0.723 90.166 1.00 77.30 ? 1504 EPE A C2 1 HETATM 4069 C C3 . EPE M 4 . ? -36.460 -0.093 90.888 1.00 74.25 ? 1504 EPE A C3 1 HETATM 4070 N N4 . EPE M 4 . ? -36.239 1.339 91.216 1.00 71.08 ? 1504 EPE A N4 1 HETATM 4071 C C5 . EPE M 4 . ? -35.589 2.152 90.158 1.00 66.77 ? 1504 EPE A C5 1 HETATM 4072 C C6 . EPE M 4 . ? -34.520 1.402 89.369 1.00 71.12 ? 1504 EPE A C6 1 HETATM 4073 C C7 . EPE M 4 . ? -37.546 1.939 91.554 1.00 62.11 ? 1504 EPE A C7 1 HETATM 4074 C C8 . EPE M 4 . ? -37.348 3.239 92.311 1.00 59.24 ? 1504 EPE A C8 1 HETATM 4075 O O8 . EPE M 4 . ? -37.449 4.397 91.454 1.00 44.50 ? 1504 EPE A O8 1 HETATM 4076 C C9 . EPE M 4 . ? -34.229 -0.576 87.970 1.00 84.49 ? 1504 EPE A C9 1 HETATM 4077 C C10 . EPE M 4 . ? -35.041 -0.673 86.688 1.00 88.71 ? 1504 EPE A C10 1 HETATM 4078 S S . EPE M 4 . ? -34.137 -1.396 85.499 1.00 103.60 ? 1504 EPE A S 1 HETATM 4079 O O1S . EPE M 4 . ? -35.008 -1.810 84.435 1.00 103.50 ? 1504 EPE A O1S 1 HETATM 4080 O O2S . EPE M 4 . ? -33.464 -2.560 86.017 1.00 105.39 ? 1504 EPE A O2S 1 HETATM 4081 O O3S . EPE M 4 . ? -33.028 -0.330 84.931 1.00 100.39 ? 1504 EPE A O3S 1 HETATM 4082 N N1 . EPE N 4 . ? -52.379 9.357 81.112 1.00 77.91 ? 1505 EPE A N1 1 HETATM 4083 C C2 . EPE N 4 . ? -51.856 10.737 81.257 1.00 79.77 ? 1505 EPE A C2 1 HETATM 4084 C C3 . EPE N 4 . ? -52.524 11.632 80.217 1.00 81.31 ? 1505 EPE A C3 1 HETATM 4085 N N4 . EPE N 4 . ? -52.129 11.149 78.881 1.00 82.14 ? 1505 EPE A N4 1 HETATM 4086 C C5 . EPE N 4 . ? -52.674 9.794 78.675 1.00 82.99 ? 1505 EPE A C5 1 HETATM 4087 C C6 . EPE N 4 . ? -52.101 8.861 79.744 1.00 80.38 ? 1505 EPE A C6 1 HETATM 4088 C C7 . EPE N 4 . ? -52.491 12.078 77.789 1.00 82.88 ? 1505 EPE A C7 1 HETATM 4089 C C8 . EPE N 4 . ? -53.909 12.620 77.914 1.00 83.53 ? 1505 EPE A C8 1 HETATM 4090 O O8 . EPE N 4 . ? -54.412 12.936 76.612 1.00 82.81 ? 1505 EPE A O8 1 HETATM 4091 C C9 . EPE N 4 . ? -51.785 8.390 82.077 1.00 71.58 ? 1505 EPE A C9 1 HETATM 4092 C C10 . EPE N 4 . ? -51.911 8.849 83.532 1.00 65.12 ? 1505 EPE A C10 1 HETATM 4093 S S . EPE N 4 . ? -52.312 7.660 84.659 1.00 62.83 ? 1505 EPE A S 1 HETATM 4094 O O1S . EPE N 4 . ? -51.105 7.203 85.278 1.00 51.76 ? 1505 EPE A O1S 1 HETATM 4095 O O2S . EPE N 4 . ? -53.017 6.544 84.055 1.00 57.05 ? 1505 EPE A O2S 1 HETATM 4096 O O3S . EPE N 4 . ? -53.270 8.443 85.728 1.00 56.62 ? 1505 EPE A O3S 1 HETATM 4097 C C . TAM O 5 . ? -42.610 21.399 40.697 1.00 66.00 ? 1506 TAM A C 1 HETATM 4098 C C1 . TAM O 5 . ? -42.961 22.683 39.924 1.00 63.53 ? 1506 TAM A C1 1 HETATM 4099 C C2 . TAM O 5 . ? -43.858 20.718 41.312 1.00 65.38 ? 1506 TAM A C2 1 HETATM 4100 C C3 . TAM O 5 . ? -41.458 21.667 41.681 1.00 66.15 ? 1506 TAM A C3 1 HETATM 4101 C C4 . TAM O 5 . ? -43.678 22.441 38.590 1.00 63.50 ? 1506 TAM A C4 1 HETATM 4102 C C5 . TAM O 5 . ? -43.875 20.465 42.829 1.00 64.57 ? 1506 TAM A C5 1 HETATM 4103 C C6 . TAM O 5 . ? -41.607 22.906 42.558 1.00 62.43 ? 1506 TAM A C6 1 HETATM 4104 N N . TAM O 5 . ? -42.052 20.464 39.727 1.00 72.26 ? 1506 TAM A N 1 HETATM 4105 O O4 . TAM O 5 . ? -43.514 23.574 37.729 1.00 61.79 ? 1506 TAM A O4 1 HETATM 4106 O O5 . TAM O 5 . ? -45.092 19.805 43.212 1.00 64.69 ? 1506 TAM A O5 1 HETATM 4107 O O6 . TAM O 5 . ? -40.374 23.110 43.248 1.00 66.85 ? 1506 TAM A O6 1 HETATM 4108 O O . HOH P 6 . ? -48.644 13.258 -14.209 1.00 47.95 ? 2001 HOH A O 1 HETATM 4109 O O . HOH P 6 . ? -51.993 12.897 -16.668 1.00 61.75 ? 2002 HOH A O 1 HETATM 4110 O O . HOH P 6 . ? -48.539 7.994 -8.671 1.00 33.34 ? 2003 HOH A O 1 HETATM 4111 O O . HOH P 6 . ? -57.329 10.624 -2.226 1.00 58.78 ? 2004 HOH A O 1 HETATM 4112 O O . HOH P 6 . ? -58.975 16.807 15.948 1.00 43.24 ? 2005 HOH A O 1 HETATM 4113 O O . HOH P 6 . ? -54.959 11.146 11.648 1.00 28.71 ? 2006 HOH A O 1 HETATM 4114 O O . HOH P 6 . ? -56.195 10.706 18.372 1.00 28.36 ? 2007 HOH A O 1 HETATM 4115 O O . HOH P 6 . ? -56.955 15.236 14.677 1.00 39.74 ? 2008 HOH A O 1 HETATM 4116 O O . HOH P 6 . ? -54.091 17.039 15.457 1.00 41.42 ? 2009 HOH A O 1 HETATM 4117 O O . HOH P 6 . ? -50.488 10.091 22.248 1.00 26.29 ? 2010 HOH A O 1 HETATM 4118 O O . HOH P 6 . ? -53.421 2.659 18.078 1.00 51.64 ? 2011 HOH A O 1 HETATM 4119 O O . HOH P 6 . ? -61.447 5.324 23.693 1.00 50.05 ? 2012 HOH A O 1 HETATM 4120 O O . HOH P 6 . ? -61.431 8.014 31.535 1.00 37.14 ? 2013 HOH A O 1 HETATM 4121 O O . HOH P 6 . ? -57.115 15.698 34.674 1.00 21.42 ? 2014 HOH A O 1 HETATM 4122 O O . HOH P 6 . ? -58.113 20.738 25.704 1.00 35.65 ? 2015 HOH A O 1 HETATM 4123 O O . HOH P 6 . ? -30.163 8.619 65.848 1.00 30.45 ? 2016 HOH A O 1 HETATM 4124 O O . HOH P 6 . ? -60.721 26.650 32.928 1.00 57.48 ? 2017 HOH A O 1 HETATM 4125 O O . HOH P 6 . ? -65.687 24.343 28.029 1.00 50.85 ? 2018 HOH A O 1 HETATM 4126 O O . HOH P 6 . ? -64.993 19.463 28.548 1.00 46.51 ? 2019 HOH A O 1 HETATM 4127 O O . HOH P 6 . ? -60.069 20.846 22.939 1.00 55.59 ? 2020 HOH A O 1 HETATM 4128 O O . HOH P 6 . ? -62.599 14.237 24.043 1.00 36.33 ? 2021 HOH A O 1 HETATM 4129 O O . HOH P 6 . ? -60.519 13.790 22.264 1.00 41.32 ? 2022 HOH A O 1 HETATM 4130 O O . HOH P 6 . ? -62.218 7.110 19.856 1.00 53.53 ? 2023 HOH A O 1 HETATM 4131 O O . HOH P 6 . ? -50.240 7.228 24.153 1.00 50.46 ? 2024 HOH A O 1 HETATM 4132 O O . HOH P 6 . ? -52.054 4.714 32.042 1.00 50.52 ? 2025 HOH A O 1 HETATM 4133 O O . HOH P 6 . ? -48.437 7.657 26.435 1.00 41.11 ? 2026 HOH A O 1 HETATM 4134 O O . HOH P 6 . ? -50.269 5.048 33.649 1.00 54.36 ? 2027 HOH A O 1 HETATM 4135 O O . HOH P 6 . ? -51.811 5.752 36.670 1.00 33.38 ? 2028 HOH A O 1 HETATM 4136 O O . HOH P 6 . ? -48.361 7.885 38.106 1.00 35.01 ? 2029 HOH A O 1 HETATM 4137 O O . HOH P 6 . ? -54.675 6.446 79.190 1.00 64.15 ? 2030 HOH A O 1 HETATM 4138 O O . HOH P 6 . ? -56.349 6.604 38.910 1.00 40.84 ? 2031 HOH A O 1 HETATM 4139 O O . HOH P 6 . ? -55.765 8.215 43.172 1.00 24.87 ? 2032 HOH A O 1 HETATM 4140 O O . HOH P 6 . ? -45.395 23.073 84.172 1.00 40.40 ? 2033 HOH A O 1 HETATM 4141 O O . HOH P 6 . ? -49.429 2.635 44.255 1.00 36.84 ? 2034 HOH A O 1 HETATM 4142 O O . HOH P 6 . ? -46.741 8.011 45.278 1.00 29.90 ? 2035 HOH A O 1 HETATM 4143 O O . HOH P 6 . ? -47.269 3.846 43.487 1.00 44.83 ? 2036 HOH A O 1 HETATM 4144 O O . HOH P 6 . ? -52.977 5.290 44.175 1.00 35.43 ? 2037 HOH A O 1 HETATM 4145 O O . HOH P 6 . ? -52.410 17.254 75.042 1.00 41.28 ? 2038 HOH A O 1 HETATM 4146 O O . HOH P 6 . ? -56.602 3.579 45.645 1.00 48.49 ? 2039 HOH A O 1 HETATM 4147 O O . HOH P 6 . ? -51.733 17.799 70.800 1.00 22.54 ? 2040 HOH A O 1 HETATM 4148 O O . HOH P 6 . ? -50.834 15.045 74.060 1.00 30.74 ? 2041 HOH A O 1 HETATM 4149 O O . HOH P 6 . ? -48.342 13.270 63.917 1.00 33.67 ? 2042 HOH A O 1 HETATM 4150 O O . HOH P 6 . ? -38.318 20.866 70.584 1.00 31.20 ? 2043 HOH A O 1 HETATM 4151 O O . HOH P 6 . ? -34.288 20.725 68.681 1.00 47.02 ? 2044 HOH A O 1 HETATM 4152 O O . HOH P 6 . ? -55.051 1.384 50.796 1.00 43.32 ? 2045 HOH A O 1 HETATM 4153 O O . HOH P 6 . ? -51.714 -2.494 49.453 1.00 78.28 ? 2046 HOH A O 1 HETATM 4154 O O . HOH P 6 . ? -54.430 -1.512 49.596 1.00 66.75 ? 2047 HOH A O 1 HETATM 4155 O O . HOH P 6 . ? -48.203 1.160 50.406 1.00 45.57 ? 2048 HOH A O 1 HETATM 4156 O O . HOH P 6 . ? -53.064 -0.559 59.138 1.00 50.25 ? 2049 HOH A O 1 HETATM 4157 O O . HOH P 6 . ? -26.347 5.082 90.095 1.00 62.90 ? 2050 HOH A O 1 HETATM 4158 O O . HOH P 6 . ? -41.614 3.231 56.040 1.00 28.17 ? 2051 HOH A O 1 HETATM 4159 O O . HOH P 6 . ? -38.624 3.007 58.255 1.00 26.11 ? 2052 HOH A O 1 HETATM 4160 O O . HOH P 6 . ? -34.169 1.393 59.247 1.00 31.74 ? 2053 HOH A O 1 HETATM 4161 O O . HOH P 6 . ? -36.405 0.429 62.156 1.00 23.04 ? 2054 HOH A O 1 HETATM 4162 O O . HOH P 6 . ? -36.272 -4.567 56.630 1.00 44.30 ? 2055 HOH A O 1 HETATM 4163 O O . HOH P 6 . ? -39.404 -5.033 61.919 1.00 39.31 ? 2056 HOH A O 1 HETATM 4164 O O . HOH P 6 . ? -35.674 -5.196 60.159 1.00 44.31 ? 2057 HOH A O 1 HETATM 4165 O O . HOH P 6 . ? -35.513 -3.211 61.758 1.00 68.12 ? 2058 HOH A O 1 HETATM 4166 O O . HOH P 6 . ? -32.037 3.471 59.700 1.00 26.44 ? 2059 HOH A O 1 HETATM 4167 O O . HOH P 6 . ? -34.136 8.531 58.659 1.00 38.44 ? 2060 HOH A O 1 HETATM 4168 O O . HOH P 6 . ? -37.650 9.939 53.606 1.00 32.70 ? 2061 HOH A O 1 HETATM 4169 O O . HOH P 6 . ? -32.322 7.463 64.391 1.00 30.84 ? 2062 HOH A O 1 HETATM 4170 O O . HOH P 6 . ? -29.863 5.749 66.302 1.00 32.97 ? 2063 HOH A O 1 HETATM 4171 O O . HOH P 6 . ? -33.453 0.025 65.898 1.00 23.44 ? 2064 HOH A O 1 HETATM 4172 O O . HOH P 6 . ? -34.551 1.961 68.818 1.00 40.52 ? 2065 HOH A O 1 HETATM 4173 O O . HOH P 6 . ? -37.263 -1.521 63.786 1.00 36.99 ? 2066 HOH A O 1 HETATM 4174 O O . HOH P 6 . ? -35.889 0.447 67.060 1.00 34.14 ? 2067 HOH A O 1 HETATM 4175 O O . HOH P 6 . ? -39.702 -1.222 67.977 1.00 30.99 ? 2068 HOH A O 1 HETATM 4176 O O . HOH P 6 . ? -40.913 -2.218 70.642 1.00 36.97 ? 2069 HOH A O 1 HETATM 4177 O O . HOH P 6 . ? -47.110 -3.345 68.002 1.00 38.42 ? 2070 HOH A O 1 HETATM 4178 O O . HOH P 6 . ? -43.248 -3.892 66.390 1.00 34.28 ? 2071 HOH A O 1 HETATM 4179 O O . HOH P 6 . ? -47.519 2.678 72.086 1.00 26.19 ? 2072 HOH A O 1 HETATM 4180 O O . HOH P 6 . ? -44.920 -2.520 75.784 1.00 44.65 ? 2073 HOH A O 1 HETATM 4181 O O . HOH P 6 . ? -48.321 3.817 78.373 1.00 39.82 ? 2074 HOH A O 1 HETATM 4182 O O . HOH P 6 . ? -52.532 -3.729 75.284 1.00 54.26 ? 2075 HOH A O 1 HETATM 4183 O O . HOH P 6 . ? -48.458 8.725 78.907 1.00 28.78 ? 2076 HOH A O 1 HETATM 4184 O O . HOH P 6 . ? -46.275 10.317 75.226 1.00 24.95 ? 2077 HOH A O 1 HETATM 4185 O O . HOH P 6 . ? -46.739 5.068 83.678 1.00 35.08 ? 2078 HOH A O 1 HETATM 4186 O O . HOH P 6 . ? -50.180 5.768 79.034 1.00 50.95 ? 2079 HOH A O 1 HETATM 4187 O O . HOH P 6 . ? -31.895 20.937 72.428 1.00 38.49 ? 2080 HOH A O 1 HETATM 4188 O O . HOH P 6 . ? -38.015 3.033 80.185 1.00 30.84 ? 2081 HOH A O 1 HETATM 4189 O O . HOH P 6 . ? -36.258 6.216 80.581 1.00 31.98 ? 2082 HOH A O 1 HETATM 4190 O O . HOH P 6 . ? -45.783 -1.584 84.441 1.00 45.61 ? 2083 HOH A O 1 HETATM 4191 O O . HOH P 6 . ? -40.105 -2.855 77.924 1.00 49.26 ? 2084 HOH A O 1 HETATM 4192 O O . HOH P 6 . ? -33.498 -2.253 79.811 1.00 39.82 ? 2085 HOH A O 1 HETATM 4193 O O . HOH P 6 . ? -37.255 2.138 82.732 1.00 34.11 ? 2086 HOH A O 1 HETATM 4194 O O . HOH P 6 . ? -35.563 -4.211 74.571 1.00 35.01 ? 2087 HOH A O 1 HETATM 4195 O O . HOH P 6 . ? -33.969 5.807 79.184 1.00 27.46 ? 2088 HOH A O 1 HETATM 4196 O O . HOH P 6 . ? -28.851 4.536 71.992 1.00 36.50 ? 2089 HOH A O 1 HETATM 4197 O O . HOH P 6 . ? -29.713 4.217 81.675 1.00 42.81 ? 2090 HOH A O 1 HETATM 4198 O O . HOH P 6 . ? -37.133 -1.559 68.598 1.00 40.86 ? 2091 HOH A O 1 HETATM 4199 O O . HOH P 6 . ? -38.673 -1.188 73.074 1.00 47.83 ? 2092 HOH A O 1 HETATM 4200 O O . HOH P 6 . ? -51.931 26.611 98.549 1.00 54.87 ? 2093 HOH A O 1 HETATM 4201 O O . HOH P 6 . ? -25.401 7.343 72.050 1.00 43.06 ? 2094 HOH A O 1 HETATM 4202 O O . HOH P 6 . ? -32.298 9.888 67.195 1.00 34.96 ? 2095 HOH A O 1 HETATM 4203 O O . HOH P 6 . ? -31.694 9.353 61.164 1.00 33.32 ? 2096 HOH A O 1 HETATM 4204 O O . HOH P 6 . ? -33.410 11.484 63.618 1.00 43.43 ? 2097 HOH A O 1 HETATM 4205 O O . HOH P 6 . ? -32.025 6.197 60.452 1.00 35.22 ? 2098 HOH A O 1 HETATM 4206 O O . HOH P 6 . ? -47.556 24.277 85.436 1.00 42.89 ? 2099 HOH A O 1 HETATM 4207 O O . HOH P 6 . ? -52.202 6.050 69.255 1.00 40.85 ? 2100 HOH A O 1 HETATM 4208 O O . HOH P 6 . ? -50.685 8.975 72.021 1.00 36.66 ? 2101 HOH A O 1 HETATM 4209 O O . HOH P 6 . ? -51.209 5.785 72.877 1.00 41.60 ? 2102 HOH A O 1 HETATM 4210 O O . HOH P 6 . ? -53.152 -0.460 69.434 1.00 33.60 ? 2103 HOH A O 1 HETATM 4211 O O . HOH P 6 . ? -54.262 4.584 75.043 1.00 46.63 ? 2104 HOH A O 1 HETATM 4212 O O . HOH P 6 . ? -55.751 -0.101 76.467 1.00 53.97 ? 2105 HOH A O 1 HETATM 4213 O O . HOH P 6 . ? -52.361 5.874 75.106 1.00 47.83 ? 2106 HOH A O 1 HETATM 4214 O O . HOH P 6 . ? -53.281 4.666 81.155 1.00 52.42 ? 2107 HOH A O 1 HETATM 4215 O O . HOH P 6 . ? -48.566 5.342 85.822 1.00 40.69 ? 2108 HOH A O 1 HETATM 4216 O O . HOH P 6 . ? -49.583 5.953 97.756 1.00 42.82 ? 2109 HOH A O 1 HETATM 4217 O O . HOH P 6 . ? -54.546 14.282 86.986 1.00 46.62 ? 2110 HOH A O 1 HETATM 4218 O O . HOH P 6 . ? -51.383 14.581 81.778 1.00 35.90 ? 2111 HOH A O 1 HETATM 4219 O O . HOH P 6 . ? -51.634 19.070 79.558 1.00 44.46 ? 2112 HOH A O 1 HETATM 4220 O O . HOH P 6 . ? -52.279 17.815 82.298 1.00 49.09 ? 2113 HOH A O 1 HETATM 4221 O O . HOH P 6 . ? -45.065 20.178 83.590 1.00 39.29 ? 2114 HOH A O 1 HETATM 4222 O O . HOH P 6 . ? -42.672 2.083 47.879 1.00 45.60 ? 2115 HOH A O 1 HETATM 4223 O O . HOH P 6 . ? -50.478 21.736 75.715 1.00 31.77 ? 2116 HOH A O 1 HETATM 4224 O O . HOH P 6 . ? -50.993 19.081 76.873 1.00 30.09 ? 2117 HOH A O 1 HETATM 4225 O O . HOH P 6 . ? -50.467 10.204 74.858 1.00 43.71 ? 2118 HOH A O 1 HETATM 4226 O O . HOH P 6 . ? -47.288 16.154 71.543 1.00 22.84 ? 2119 HOH A O 1 HETATM 4227 O O . HOH P 6 . ? -50.027 15.821 71.546 1.00 22.47 ? 2120 HOH A O 1 HETATM 4228 O O . HOH P 6 . ? -48.409 12.257 67.207 1.00 24.15 ? 2121 HOH A O 1 HETATM 4229 O O . HOH P 6 . ? -60.442 22.511 60.451 1.00 39.75 ? 2122 HOH A O 1 HETATM 4230 O O . HOH P 6 . ? -45.967 16.678 69.011 1.00 23.67 ? 2123 HOH A O 1 HETATM 4231 O O . HOH P 6 . ? -36.639 19.018 71.436 1.00 26.32 ? 2124 HOH A O 1 HETATM 4232 O O . HOH P 6 . ? -37.323 16.844 64.985 1.00 32.82 ? 2125 HOH A O 1 HETATM 4233 O O . HOH P 6 . ? -33.886 14.263 66.220 1.00 34.27 ? 2126 HOH A O 1 HETATM 4234 O O . HOH P 6 . ? -34.800 18.262 67.053 1.00 41.85 ? 2127 HOH A O 1 HETATM 4235 O O . HOH P 6 . ? -62.049 18.110 46.307 1.00 50.02 ? 2128 HOH A O 1 HETATM 4236 O O . HOH P 6 . ? -31.760 12.635 67.527 1.00 51.30 ? 2129 HOH A O 1 HETATM 4237 O O . HOH P 6 . ? -34.369 13.427 74.726 1.00 38.42 ? 2130 HOH A O 1 HETATM 4238 O O . HOH P 6 . ? -61.651 16.522 42.841 1.00 45.32 ? 2131 HOH A O 1 HETATM 4239 O O . HOH P 6 . ? -62.002 13.837 39.098 1.00 42.12 ? 2132 HOH A O 1 HETATM 4240 O O . HOH P 6 . ? -25.365 6.331 83.671 1.00 42.15 ? 2133 HOH A O 1 HETATM 4241 O O . HOH P 6 . ? -24.174 8.544 89.351 1.00 51.63 ? 2134 HOH A O 1 HETATM 4242 O O . HOH P 6 . ? -32.292 5.477 86.455 1.00 40.68 ? 2135 HOH A O 1 HETATM 4243 O O . HOH P 6 . ? -28.668 8.165 89.679 1.00 39.95 ? 2136 HOH A O 1 HETATM 4244 O O . HOH P 6 . ? -29.528 3.671 84.355 1.00 59.14 ? 2137 HOH A O 1 HETATM 4245 O O . HOH P 6 . ? -22.923 12.944 89.571 1.00 50.79 ? 2138 HOH A O 1 HETATM 4246 O O . HOH P 6 . ? -26.101 16.973 94.992 1.00 47.58 ? 2139 HOH A O 1 HETATM 4247 O O . HOH P 6 . ? -31.885 10.701 92.726 1.00 38.42 ? 2140 HOH A O 1 HETATM 4248 O O . HOH P 6 . ? -38.484 6.218 100.191 1.00 42.91 ? 2141 HOH A O 1 HETATM 4249 O O . HOH P 6 . ? -38.045 5.586 94.083 1.00 33.83 ? 2142 HOH A O 1 HETATM 4250 O O . HOH P 6 . ? -43.791 -0.607 98.733 1.00 50.81 ? 2143 HOH A O 1 HETATM 4251 O O . HOH P 6 . ? -45.542 4.416 100.163 1.00 59.53 ? 2144 HOH A O 1 HETATM 4252 O O . HOH P 6 . ? -48.700 3.370 96.971 1.00 40.82 ? 2145 HOH A O 1 HETATM 4253 O O . HOH P 6 . ? -52.102 -0.953 94.796 1.00 53.30 ? 2146 HOH A O 1 HETATM 4254 O O . HOH P 6 . ? -44.356 6.930 25.875 1.00 55.57 ? 2147 HOH A O 1 HETATM 4255 O O . HOH P 6 . ? -38.228 -5.731 91.146 1.00 63.00 ? 2148 HOH A O 1 HETATM 4256 O O . HOH P 6 . ? -38.456 22.327 62.172 1.00 42.74 ? 2149 HOH A O 1 HETATM 4257 O O . HOH P 6 . ? -41.657 -5.883 85.400 1.00 62.45 ? 2150 HOH A O 1 HETATM 4258 O O . HOH P 6 . ? -57.922 11.439 68.257 1.00 50.49 ? 2151 HOH A O 1 HETATM 4259 O O . HOH P 6 . ? -63.267 20.098 69.166 1.00 45.21 ? 2152 HOH A O 1 HETATM 4260 O O . HOH P 6 . ? -36.387 -4.900 94.649 1.00 64.07 ? 2153 HOH A O 1 HETATM 4261 O O . HOH P 6 . ? -42.441 -6.012 97.187 1.00 52.74 ? 2154 HOH A O 1 HETATM 4262 O O . HOH P 6 . ? -39.535 -3.901 96.767 1.00 62.99 ? 2155 HOH A O 1 HETATM 4263 O O . HOH P 6 . ? -35.711 11.943 86.082 1.00 36.84 ? 2156 HOH A O 1 HETATM 4264 O O . HOH P 6 . ? -53.109 27.169 29.407 1.00 50.37 ? 2157 HOH A O 1 HETATM 4265 O O . HOH P 6 . ? -39.850 13.533 98.758 1.00 41.08 ? 2158 HOH A O 1 HETATM 4266 O O . HOH P 6 . ? -39.723 6.939 105.166 1.00 46.20 ? 2159 HOH A O 1 HETATM 4267 O O . HOH P 6 . ? -53.433 28.067 27.098 1.00 43.48 ? 2160 HOH A O 1 HETATM 4268 O O . HOH P 6 . ? -50.443 29.120 27.143 0.33 43.33 ? 2161 HOH A O 1 HETATM 4269 O O . HOH P 6 . ? -43.984 6.674 108.588 1.00 48.14 ? 2162 HOH A O 1 HETATM 4270 O O . HOH P 6 . ? -50.445 29.125 24.850 0.33 55.41 ? 2163 HOH A O 1 HETATM 4271 O O . HOH P 6 . ? -36.308 5.933 109.034 1.00 51.47 ? 2164 HOH A O 1 HETATM 4272 O O . HOH P 6 . ? -37.813 17.413 16.776 1.00 53.54 ? 2165 HOH A O 1 HETATM 4273 O O . HOH P 6 . ? -38.804 19.958 5.377 1.00 49.15 ? 2166 HOH A O 1 HETATM 4274 O O . HOH P 6 . ? -37.406 21.523 0.732 1.00 39.24 ? 2167 HOH A O 1 HETATM 4275 O O . HOH P 6 . ? -29.500 19.485 101.172 1.00 44.58 ? 2168 HOH A O 1 HETATM 4276 O O . HOH P 6 . ? -26.295 23.017 97.878 1.00 55.08 ? 2169 HOH A O 1 HETATM 4277 O O . HOH P 6 . ? -55.376 25.674 0.161 1.00 54.09 ? 2170 HOH A O 1 HETATM 4278 O O . HOH P 6 . ? -25.768 19.696 96.987 1.00 47.24 ? 2171 HOH A O 1 HETATM 4279 O O . HOH P 6 . ? -26.553 19.710 85.837 1.00 34.15 ? 2172 HOH A O 1 HETATM 4280 O O . HOH P 6 . ? -22.048 17.958 84.623 1.00 41.66 ? 2173 HOH A O 1 HETATM 4281 O O . HOH P 6 . ? -22.085 17.701 87.654 1.00 43.20 ? 2174 HOH A O 1 HETATM 4282 O O . HOH P 6 . ? -19.865 23.454 80.851 1.00 57.86 ? 2175 HOH A O 1 HETATM 4283 O O . HOH P 6 . ? -15.785 18.985 83.101 1.00 68.70 ? 2176 HOH A O 1 HETATM 4284 O O . HOH P 6 . ? -18.658 22.517 88.879 1.00 54.08 ? 2177 HOH A O 1 HETATM 4285 O O . HOH P 6 . ? -16.028 23.590 86.292 1.00 61.11 ? 2178 HOH A O 1 HETATM 4286 O O . HOH P 6 . ? -19.376 17.244 77.725 1.00 49.01 ? 2179 HOH A O 1 HETATM 4287 O O . HOH P 6 . ? -30.214 12.228 3.370 1.00 69.74 ? 2180 HOH A O 1 HETATM 4288 O O . HOH P 6 . ? -41.249 17.158 -17.218 1.00 50.70 ? 2181 HOH A O 1 HETATM 4289 O O . HOH P 6 . ? -27.025 20.188 73.913 1.00 42.19 ? 2182 HOH A O 1 HETATM 4290 O O . HOH P 6 . ? -27.788 16.544 75.433 1.00 36.29 ? 2183 HOH A O 1 HETATM 4291 O O . HOH P 6 . ? -32.086 22.246 74.801 1.00 42.63 ? 2184 HOH A O 1 HETATM 4292 O O . HOH P 6 . ? -34.352 13.402 84.571 1.00 29.91 ? 2185 HOH A O 1 HETATM 4293 O O . HOH P 6 . ? -48.839 20.101 90.627 1.00 40.16 ? 2186 HOH A O 1 HETATM 4294 O O . HOH P 6 . ? -57.947 13.188 102.137 1.00 61.94 ? 2187 HOH A O 1 HETATM 4295 O O . HOH P 6 . ? -55.905 11.898 106.997 1.00 53.54 ? 2188 HOH A O 1 HETATM 4296 O O . HOH P 6 . ? -50.153 9.249 99.549 1.00 48.52 ? 2189 HOH A O 1 HETATM 4297 O O . HOH P 6 . ? -49.331 3.097 103.487 1.00 65.79 ? 2190 HOH A O 1 HETATM 4298 O O . HOH P 6 . ? -42.480 6.790 105.073 1.00 51.14 ? 2191 HOH A O 1 HETATM 4299 O O . HOH P 6 . ? -49.838 20.096 105.010 1.00 52.33 ? 2192 HOH A O 1 HETATM 4300 O O . HOH P 6 . ? -48.563 22.518 100.150 1.00 51.97 ? 2193 HOH A O 1 HETATM 4301 O O . HOH P 6 . ? -51.922 20.420 100.718 1.00 49.95 ? 2194 HOH A O 1 HETATM 4302 O O . HOH P 6 . ? -43.692 19.606 101.271 1.00 43.58 ? 2195 HOH A O 1 HETATM 4303 O O . HOH P 6 . ? -41.264 20.638 99.563 1.00 47.48 ? 2196 HOH A O 1 HETATM 4304 O O . HOH P 6 . ? -41.149 23.433 101.418 1.00 47.76 ? 2197 HOH A O 1 HETATM 4305 O O . HOH P 6 . ? -34.705 26.393 93.887 1.00 44.65 ? 2198 HOH A O 1 HETATM 4306 O O . HOH P 6 . ? -32.693 26.432 83.074 1.00 46.57 ? 2199 HOH A O 1 HETATM 4307 O O . HOH P 6 . ? -38.405 31.290 85.131 1.00 44.68 ? 2200 HOH A O 1 HETATM 4308 O O . HOH P 6 . ? -40.663 31.147 92.070 1.00 47.40 ? 2201 HOH A O 1 HETATM 4309 O O . HOH P 6 . ? -43.039 24.374 85.335 1.00 49.67 ? 2202 HOH A O 1 HETATM 4310 O O . HOH P 6 . ? -42.377 21.758 83.639 1.00 30.85 ? 2203 HOH A O 1 HETATM 4311 O O . HOH P 6 . ? -48.287 24.958 92.048 1.00 35.32 ? 2204 HOH A O 1 HETATM 4312 O O . HOH P 6 . ? -49.580 22.169 92.385 1.00 38.39 ? 2205 HOH A O 1 HETATM 4313 O O . HOH P 6 . ? -52.035 22.829 99.355 1.00 51.93 ? 2206 HOH A O 1 HETATM 4314 O O . HOH P 6 . ? -52.566 25.416 96.137 1.00 48.55 ? 2207 HOH A O 1 HETATM 4315 O O . HOH P 6 . ? -56.080 19.716 97.269 1.00 54.77 ? 2208 HOH A O 1 HETATM 4316 O O . HOH P 6 . ? -60.605 14.367 99.492 1.00 66.76 ? 2209 HOH A O 1 HETATM 4317 O O . HOH P 6 . ? -59.136 16.459 96.132 1.00 46.22 ? 2210 HOH A O 1 HETATM 4318 O O . HOH P 6 . ? -60.714 8.785 95.908 1.00 35.03 ? 2211 HOH A O 1 HETATM 4319 O O . HOH P 6 . ? -62.035 5.601 90.618 1.00 46.51 ? 2212 HOH A O 1 HETATM 4320 O O . HOH P 6 . ? -59.874 7.264 98.112 1.00 48.18 ? 2213 HOH A O 1 HETATM 4321 O O . HOH P 6 . ? -58.898 2.219 90.924 1.00 52.53 ? 2214 HOH A O 1 HETATM 4322 O O . HOH P 6 . ? -52.618 -0.995 92.123 1.00 54.13 ? 2215 HOH A O 1 HETATM 4323 O O . HOH P 6 . ? -52.789 7.193 97.724 1.00 52.40 ? 2216 HOH A O 1 HETATM 4324 O O . HOH P 6 . ? -56.415 13.514 88.609 1.00 41.06 ? 2217 HOH A O 1 HETATM 4325 O O . HOH P 6 . ? -48.300 23.234 87.717 1.00 46.35 ? 2218 HOH A O 1 HETATM 4326 O O . HOH P 6 . ? -40.072 23.451 81.722 1.00 47.61 ? 2219 HOH A O 1 HETATM 4327 O O . HOH P 6 . ? -39.184 23.304 77.822 1.00 44.75 ? 2220 HOH A O 1 HETATM 4328 O O . HOH P 6 . ? -36.397 24.640 81.348 1.00 46.17 ? 2221 HOH A O 1 HETATM 4329 O O . HOH P 6 . ? -32.542 26.469 79.484 1.00 52.10 ? 2222 HOH A O 1 HETATM 4330 O O . HOH P 6 . ? -30.080 26.554 82.363 1.00 45.16 ? 2223 HOH A O 1 HETATM 4331 O O . HOH P 6 . ? -27.622 29.936 82.138 1.00 48.96 ? 2224 HOH A O 1 HETATM 4332 O O . HOH P 6 . ? -30.404 6.940 91.649 1.00 40.24 ? 2225 HOH A O 1 HETATM 4333 O O . HOH P 6 . ? -34.082 19.389 70.883 1.00 33.96 ? 2226 HOH A O 1 HETATM 4334 O O . HOH P 6 . ? -27.702 17.702 69.063 1.00 45.69 ? 2227 HOH A O 1 HETATM 4335 O O . HOH P 6 . ? -35.001 20.289 64.886 1.00 62.51 ? 2228 HOH A O 1 HETATM 4336 O O . HOH P 6 . ? -31.760 13.367 62.822 1.00 38.58 ? 2229 HOH A O 1 HETATM 4337 O O . HOH P 6 . ? -44.265 13.686 61.425 1.00 40.94 ? 2230 HOH A O 1 HETATM 4338 O O . HOH P 6 . ? -45.218 15.653 63.465 1.00 29.07 ? 2231 HOH A O 1 HETATM 4339 O O . HOH P 6 . ? -46.260 14.323 65.756 1.00 30.00 ? 2232 HOH A O 1 HETATM 4340 O O . HOH P 6 . ? -45.882 12.053 62.854 1.00 33.41 ? 2233 HOH A O 1 HETATM 4341 O O . HOH P 6 . ? -49.849 11.118 64.806 1.00 23.65 ? 2234 HOH A O 1 HETATM 4342 O O . HOH P 6 . ? -53.214 8.792 63.531 1.00 38.03 ? 2235 HOH A O 1 HETATM 4343 O O . HOH P 6 . ? -52.379 11.717 65.779 1.00 26.40 ? 2236 HOH A O 1 HETATM 4344 O O . HOH P 6 . ? -52.868 15.546 69.469 1.00 21.98 ? 2237 HOH A O 1 HETATM 4345 O O . HOH P 6 . ? -54.475 14.147 71.065 1.00 32.09 ? 2238 HOH A O 1 HETATM 4346 O O . HOH P 6 . ? -51.364 12.298 73.606 1.00 37.73 ? 2239 HOH A O 1 HETATM 4347 O O . HOH P 6 . ? -53.601 3.321 62.237 1.00 36.44 ? 2240 HOH A O 1 HETATM 4348 O O . HOH P 6 . ? -50.646 -2.790 65.735 1.00 47.17 ? 2241 HOH A O 1 HETATM 4349 O O . HOH P 6 . ? -46.124 -4.680 64.189 1.00 36.31 ? 2242 HOH A O 1 HETATM 4350 O O . HOH P 6 . ? -42.522 -8.287 57.484 1.00 47.96 ? 2243 HOH A O 1 HETATM 4351 O O . HOH P 6 . ? -35.504 -7.390 61.853 1.00 49.47 ? 2244 HOH A O 1 HETATM 4352 O O . HOH P 6 . ? -39.486 -3.267 50.609 1.00 40.80 ? 2245 HOH A O 1 HETATM 4353 O O . HOH P 6 . ? -42.168 -0.729 50.205 1.00 52.33 ? 2246 HOH A O 1 HETATM 4354 O O . HOH P 6 . ? -35.230 3.822 50.644 1.00 34.31 ? 2247 HOH A O 1 HETATM 4355 O O . HOH P 6 . ? -44.713 2.222 50.427 1.00 39.76 ? 2248 HOH A O 1 HETATM 4356 O O . HOH P 6 . ? -42.303 5.954 50.045 1.00 35.04 ? 2249 HOH A O 1 HETATM 4357 O O . HOH P 6 . ? -39.774 4.568 49.140 1.00 31.38 ? 2250 HOH A O 1 HETATM 4358 O O . HOH P 6 . ? -33.676 7.947 54.705 1.00 47.21 ? 2251 HOH A O 1 HETATM 4359 O O . HOH P 6 . ? -53.959 1.346 54.887 1.00 61.88 ? 2252 HOH A O 1 HETATM 4360 O O . HOH P 6 . ? -58.611 3.382 56.868 1.00 58.48 ? 2253 HOH A O 1 HETATM 4361 O O . HOH P 6 . ? -41.996 4.675 46.837 1.00 39.74 ? 2254 HOH A O 1 HETATM 4362 O O . HOH P 6 . ? -40.383 11.014 45.674 1.00 40.82 ? 2255 HOH A O 1 HETATM 4363 O O . HOH P 6 . ? -37.491 9.077 48.220 1.00 43.30 ? 2256 HOH A O 1 HETATM 4364 O O . HOH P 6 . ? -43.034 13.259 42.989 1.00 35.86 ? 2257 HOH A O 1 HETATM 4365 O O . HOH P 6 . ? -43.056 4.007 43.773 1.00 49.84 ? 2258 HOH A O 1 HETATM 4366 O O . HOH P 6 . ? -45.951 7.292 39.128 1.00 38.06 ? 2259 HOH A O 1 HETATM 4367 O O . HOH P 6 . ? -44.669 16.601 46.140 1.00 25.46 ? 2260 HOH A O 1 HETATM 4368 O O . HOH P 6 . ? -58.003 11.718 52.848 1.00 38.08 ? 2261 HOH A O 1 HETATM 4369 O O . HOH P 6 . ? -58.544 8.148 48.239 1.00 54.00 ? 2262 HOH A O 1 HETATM 4370 O O . HOH P 6 . ? -60.491 14.401 50.570 1.00 41.42 ? 2263 HOH A O 1 HETATM 4371 O O . HOH P 6 . ? -56.988 10.337 55.760 1.00 45.85 ? 2264 HOH A O 1 HETATM 4372 O O . HOH P 6 . ? -55.336 12.473 59.878 1.00 28.58 ? 2265 HOH A O 1 HETATM 4373 O O . HOH P 6 . ? -56.012 12.901 57.067 1.00 27.66 ? 2266 HOH A O 1 HETATM 4374 O O . HOH P 6 . ? -54.548 9.199 61.219 1.00 32.75 ? 2267 HOH A O 1 HETATM 4375 O O . HOH P 6 . ? -49.176 17.005 55.402 1.00 26.80 ? 2268 HOH A O 1 HETATM 4376 O O . HOH P 6 . ? -47.686 15.488 59.626 1.00 26.87 ? 2269 HOH A O 1 HETATM 4377 O O . HOH P 6 . ? -56.685 14.938 60.580 1.00 47.58 ? 2270 HOH A O 1 HETATM 4378 O O . HOH P 6 . ? -57.773 21.031 60.317 1.00 26.39 ? 2271 HOH A O 1 HETATM 4379 O O . HOH P 6 . ? -55.731 19.159 61.580 1.00 25.30 ? 2272 HOH A O 1 HETATM 4380 O O . HOH P 6 . ? -58.934 17.283 54.307 1.00 53.69 ? 2273 HOH A O 1 HETATM 4381 O O . HOH P 6 . ? -46.690 14.990 52.936 1.00 36.48 ? 2274 HOH A O 1 HETATM 4382 O O . HOH P 6 . ? -43.424 14.091 55.422 1.00 27.01 ? 2275 HOH A O 1 HETATM 4383 O O . HOH P 6 . ? -46.661 16.404 56.121 1.00 34.81 ? 2276 HOH A O 1 HETATM 4384 O O . HOH P 6 . ? -34.922 10.858 59.428 1.00 42.90 ? 2277 HOH A O 1 HETATM 4385 O O . HOH P 6 . ? -43.087 15.506 52.783 1.00 35.56 ? 2278 HOH A O 1 HETATM 4386 O O . HOH P 6 . ? -43.100 21.538 47.088 1.00 45.38 ? 2279 HOH A O 1 HETATM 4387 O O . HOH P 6 . ? -48.238 19.534 51.713 1.00 22.40 ? 2280 HOH A O 1 HETATM 4388 O O . HOH P 6 . ? -44.173 18.099 52.239 1.00 41.37 ? 2281 HOH A O 1 HETATM 4389 O O . HOH P 6 . ? -48.516 16.971 53.003 1.00 26.25 ? 2282 HOH A O 1 HETATM 4390 O O . HOH P 6 . ? -50.944 19.828 52.052 1.00 19.72 ? 2283 HOH A O 1 HETATM 4391 O O . HOH P 6 . ? -62.170 14.217 46.870 1.00 56.20 ? 2284 HOH A O 1 HETATM 4392 O O . HOH P 6 . ? -58.653 24.359 47.512 1.00 28.93 ? 2285 HOH A O 1 HETATM 4393 O O . HOH P 6 . ? -61.625 14.158 43.916 1.00 47.48 ? 2286 HOH A O 1 HETATM 4394 O O . HOH P 6 . ? -59.440 7.252 44.252 1.00 65.73 ? 2287 HOH A O 1 HETATM 4395 O O . HOH P 6 . ? -63.214 12.135 42.471 1.00 50.10 ? 2288 HOH A O 1 HETATM 4396 O O . HOH P 6 . ? -59.645 15.061 39.147 1.00 37.95 ? 2289 HOH A O 1 HETATM 4397 O O . HOH P 6 . ? -58.356 14.148 36.778 1.00 27.58 ? 2290 HOH A O 1 HETATM 4398 O O . HOH P 6 . ? -49.985 16.468 30.718 1.00 21.68 ? 2291 HOH A O 1 HETATM 4399 O O . HOH P 6 . ? -53.610 16.732 21.199 1.00 27.78 ? 2292 HOH A O 1 HETATM 4400 O O . HOH P 6 . ? -60.517 15.968 20.697 1.00 40.79 ? 2293 HOH A O 1 HETATM 4401 O O . HOH P 6 . ? -63.311 11.635 14.088 1.00 44.26 ? 2294 HOH A O 1 HETATM 4402 O O . HOH P 6 . ? -56.536 3.107 10.838 1.00 38.08 ? 2295 HOH A O 1 HETATM 4403 O O . HOH P 6 . ? -60.594 2.574 12.000 1.00 58.58 ? 2296 HOH A O 1 HETATM 4404 O O . HOH P 6 . ? -58.731 7.874 8.121 1.00 32.43 ? 2297 HOH A O 1 HETATM 4405 O O . HOH P 6 . ? -65.571 2.834 6.119 1.00 67.38 ? 2298 HOH A O 1 HETATM 4406 O O . HOH P 6 . ? -56.948 7.272 5.934 1.00 36.46 ? 2299 HOH A O 1 HETATM 4407 O O . HOH P 6 . ? -59.844 14.156 7.680 1.00 38.09 ? 2300 HOH A O 1 HETATM 4408 O O . HOH P 6 . ? -43.842 2.955 9.898 1.00 41.81 ? 2301 HOH A O 1 HETATM 4409 O O . HOH P 6 . ? -43.559 4.555 21.629 1.00 62.56 ? 2302 HOH A O 1 HETATM 4410 O O . HOH P 6 . ? -46.788 6.852 3.609 1.00 34.12 ? 2303 HOH A O 1 HETATM 4411 O O . HOH P 6 . ? -47.825 2.518 -2.513 1.00 33.30 ? 2304 HOH A O 1 HETATM 4412 O O . HOH P 6 . ? -46.349 -0.746 -3.024 1.00 42.53 ? 2305 HOH A O 1 HETATM 4413 O O . HOH P 6 . ? -40.427 3.371 -6.062 1.00 47.02 ? 2306 HOH A O 1 HETATM 4414 O O . HOH P 6 . ? -53.339 1.073 6.549 1.00 53.48 ? 2307 HOH A O 1 HETATM 4415 O O . HOH P 6 . ? -41.762 8.227 7.600 1.00 42.59 ? 2308 HOH A O 1 HETATM 4416 O O . HOH P 6 . ? -40.600 10.535 8.269 1.00 42.46 ? 2309 HOH A O 1 HETATM 4417 O O . HOH P 6 . ? -38.486 11.837 11.116 1.00 45.19 ? 2310 HOH A O 1 HETATM 4418 O O . HOH P 6 . ? -36.995 13.763 27.927 1.00 50.70 ? 2311 HOH A O 1 HETATM 4419 O O . HOH P 6 . ? -34.671 11.627 20.840 1.00 61.53 ? 2312 HOH A O 1 HETATM 4420 O O . HOH P 6 . ? -44.586 20.328 20.151 1.00 36.06 ? 2313 HOH A O 1 HETATM 4421 O O . HOH P 6 . ? -44.619 9.411 26.965 1.00 56.08 ? 2314 HOH A O 1 HETATM 4422 O O . HOH P 6 . ? -40.752 7.134 26.642 1.00 55.24 ? 2315 HOH A O 1 HETATM 4423 O O . HOH P 6 . ? -37.478 17.091 33.445 1.00 51.91 ? 2316 HOH A O 1 HETATM 4424 O O . HOH P 6 . ? -40.308 19.571 31.898 1.00 63.39 ? 2317 HOH A O 1 HETATM 4425 O O . HOH P 6 . ? -42.508 17.542 42.075 1.00 46.58 ? 2318 HOH A O 1 HETATM 4426 O O . HOH P 6 . ? -38.980 18.587 39.954 1.00 55.13 ? 2319 HOH A O 1 HETATM 4427 O O . HOH P 6 . ? -43.084 15.662 44.071 1.00 38.18 ? 2320 HOH A O 1 HETATM 4428 O O . HOH P 6 . ? -37.131 17.269 44.830 1.00 62.08 ? 2321 HOH A O 1 HETATM 4429 O O . HOH P 6 . ? -39.286 19.742 52.636 1.00 46.26 ? 2322 HOH A O 1 HETATM 4430 O O . HOH P 6 . ? -39.729 20.067 46.059 1.00 52.47 ? 2323 HOH A O 1 HETATM 4431 O O . HOH P 6 . ? -36.023 17.042 50.799 1.00 42.70 ? 2324 HOH A O 1 HETATM 4432 O O . HOH P 6 . ? -33.965 11.280 52.029 1.00 54.71 ? 2325 HOH A O 1 HETATM 4433 O O . HOH P 6 . ? -34.283 10.844 56.282 1.00 40.76 ? 2326 HOH A O 1 HETATM 4434 O O . HOH P 6 . ? -39.889 19.119 58.949 1.00 32.61 ? 2327 HOH A O 1 HETATM 4435 O O . HOH P 6 . ? -38.022 17.973 62.627 1.00 32.37 ? 2328 HOH A O 1 HETATM 4436 O O . HOH P 6 . ? -39.338 19.777 61.738 1.00 38.38 ? 2329 HOH A O 1 HETATM 4437 O O . HOH P 6 . ? -42.047 20.793 65.233 1.00 44.11 ? 2330 HOH A O 1 HETATM 4438 O O . HOH P 6 . ? -48.415 15.506 62.348 1.00 33.01 ? 2331 HOH A O 1 HETATM 4439 O O . HOH P 6 . ? -48.467 20.255 67.731 1.00 21.78 ? 2332 HOH A O 1 HETATM 4440 O O . HOH P 6 . ? -53.589 20.524 62.894 1.00 20.73 ? 2333 HOH A O 1 HETATM 4441 O O . HOH P 6 . ? -51.540 14.245 64.995 1.00 29.23 ? 2334 HOH A O 1 HETATM 4442 O O . HOH P 6 . ? -58.144 17.516 63.614 1.00 39.08 ? 2335 HOH A O 1 HETATM 4443 O O . HOH P 6 . ? -55.390 11.918 68.793 1.00 45.20 ? 2336 HOH A O 1 HETATM 4444 O O . HOH P 6 . ? -54.272 10.475 65.356 1.00 43.39 ? 2337 HOH A O 1 HETATM 4445 O O . HOH P 6 . ? -59.132 15.621 65.784 1.00 31.90 ? 2338 HOH A O 1 HETATM 4446 O O . HOH P 6 . ? -61.502 16.132 70.655 1.00 52.68 ? 2339 HOH A O 1 HETATM 4447 O O . HOH P 6 . ? -55.900 16.337 72.573 1.00 36.04 ? 2340 HOH A O 1 HETATM 4448 O O . HOH P 6 . ? -61.540 11.506 71.877 1.00 52.34 ? 2341 HOH A O 1 HETATM 4449 O O . HOH P 6 . ? -62.955 14.724 73.272 1.00 52.17 ? 2342 HOH A O 1 HETATM 4450 O O . HOH P 6 . ? -61.145 13.027 75.877 1.00 57.00 ? 2343 HOH A O 1 HETATM 4451 O O . HOH P 6 . ? -61.211 18.371 69.826 1.00 33.59 ? 2344 HOH A O 1 HETATM 4452 O O . HOH P 6 . ? -62.703 16.561 75.710 1.00 39.08 ? 2345 HOH A O 1 HETATM 4453 O O . HOH P 6 . ? -60.994 22.368 70.906 1.00 27.64 ? 2346 HOH A O 1 HETATM 4454 O O . HOH P 6 . ? -56.251 26.696 74.056 1.00 28.31 ? 2347 HOH A O 1 HETATM 4455 O O . HOH P 6 . ? -53.805 18.171 72.571 1.00 31.09 ? 2348 HOH A O 1 HETATM 4456 O O . HOH P 6 . ? -60.361 23.138 68.266 1.00 29.66 ? 2349 HOH A O 1 HETATM 4457 O O . HOH P 6 . ? -60.137 26.088 63.476 1.00 23.71 ? 2350 HOH A O 1 HETATM 4458 O O . HOH P 6 . ? -63.359 25.192 69.474 1.00 29.03 ? 2351 HOH A O 1 HETATM 4459 O O . HOH P 6 . ? -61.392 30.322 67.730 1.00 32.03 ? 2352 HOH A O 1 HETATM 4460 O O . HOH P 6 . ? -50.558 19.871 69.539 1.00 29.64 ? 2353 HOH A O 1 HETATM 4461 O O . HOH P 6 . ? -48.557 22.844 67.728 1.00 22.09 ? 2354 HOH A O 1 HETATM 4462 O O . HOH P 6 . ? -61.038 17.150 67.099 1.00 36.38 ? 2355 HOH A O 1 HETATM 4463 O O . HOH P 6 . ? -60.109 25.213 60.766 1.00 28.90 ? 2356 HOH A O 1 HETATM 4464 O O . HOH P 6 . ? -51.433 27.723 56.943 1.00 34.39 ? 2357 HOH A O 1 HETATM 4465 O O . HOH P 6 . ? -50.811 19.126 54.821 1.00 25.40 ? 2358 HOH A O 1 HETATM 4466 O O . HOH P 6 . ? -59.042 21.707 53.965 1.00 37.56 ? 2359 HOH A O 1 HETATM 4467 O O . HOH P 6 . ? -61.848 26.149 58.918 1.00 40.11 ? 2360 HOH A O 1 HETATM 4468 O O . HOH P 6 . ? -60.127 26.531 57.537 1.00 36.73 ? 2361 HOH A O 1 HETATM 4469 O O . HOH P 6 . ? -58.526 27.894 56.146 1.00 20.44 ? 2362 HOH A O 1 HETATM 4470 O O . HOH P 6 . ? -45.907 18.705 54.354 1.00 32.79 ? 2363 HOH A O 1 HETATM 4471 O O . HOH P 6 . ? -58.895 27.490 53.398 1.00 18.45 ? 2364 HOH A O 1 HETATM 4472 O O . HOH P 6 . ? -52.111 27.996 46.483 1.00 19.67 ? 2365 HOH A O 1 HETATM 4473 O O . HOH P 6 . ? -46.656 24.424 52.410 1.00 15.03 ? 2366 HOH A O 1 HETATM 4474 O O . HOH P 6 . ? -53.894 30.894 40.356 1.00 17.96 ? 2367 HOH A O 1 HETATM 4475 O O . HOH P 6 . ? -50.874 27.547 41.786 1.00 18.07 ? 2368 HOH A O 1 HETATM 4476 O O . HOH P 6 . ? -57.321 20.120 37.167 1.00 29.86 ? 2369 HOH A O 1 HETATM 4477 O O . HOH P 6 . ? -60.666 17.714 41.058 1.00 41.10 ? 2370 HOH A O 1 HETATM 4478 O O . HOH P 6 . ? -59.869 17.358 38.320 1.00 43.06 ? 2371 HOH A O 1 HETATM 4479 O O . HOH P 6 . ? -50.991 25.436 29.631 1.00 29.52 ? 2372 HOH A O 1 HETATM 4480 O O . HOH P 6 . ? -43.742 19.903 34.914 1.00 45.48 ? 2373 HOH A O 1 HETATM 4481 O O . HOH P 6 . ? -53.578 26.694 24.893 1.00 51.90 ? 2374 HOH A O 1 HETATM 4482 O O . HOH P 6 . ? -50.364 25.530 27.105 1.00 35.60 ? 2375 HOH A O 1 HETATM 4483 O O . HOH P 6 . ? -50.752 23.690 19.409 1.00 47.18 ? 2376 HOH A O 1 HETATM 4484 O O . HOH P 6 . ? -49.227 26.810 23.144 1.00 54.30 ? 2377 HOH A O 1 HETATM 4485 O O . HOH P 6 . ? -43.416 17.795 13.999 1.00 36.34 ? 2378 HOH A O 1 HETATM 4486 O O . HOH P 6 . ? -40.336 18.118 15.755 1.00 44.81 ? 2379 HOH A O 1 HETATM 4487 O O . HOH P 6 . ? -49.958 23.169 9.648 1.00 47.81 ? 2380 HOH A O 1 HETATM 4488 O O . HOH P 6 . ? -50.202 24.389 16.539 1.00 55.67 ? 2381 HOH A O 1 HETATM 4489 O O . HOH P 6 . ? -42.924 22.912 10.416 1.00 49.14 ? 2382 HOH A O 1 HETATM 4490 O O . HOH P 6 . ? -51.529 25.400 5.847 1.00 47.45 ? 2383 HOH A O 1 HETATM 4491 O O . HOH P 6 . ? -40.085 21.818 4.671 1.00 41.94 ? 2384 HOH A O 1 HETATM 4492 O O . HOH P 6 . ? -42.396 16.126 5.377 1.00 45.14 ? 2385 HOH A O 1 HETATM 4493 O O . HOH P 6 . ? -46.955 23.143 -1.200 1.00 37.03 ? 2386 HOH A O 1 HETATM 4494 O O . HOH P 6 . ? -49.612 22.562 -0.922 1.00 44.94 ? 2387 HOH A O 1 HETATM 4495 O O . HOH P 6 . ? -52.102 24.649 3.074 1.00 51.10 ? 2388 HOH A O 1 HETATM 4496 O O . HOH P 6 . ? -38.847 21.946 -1.721 1.00 45.71 ? 2389 HOH A O 1 HETATM 4497 O O . HOH P 6 . ? -37.200 17.875 0.352 1.00 49.50 ? 2390 HOH A O 1 HETATM 4498 O O . HOH P 6 . ? -44.148 27.007 -3.813 1.00 45.13 ? 2391 HOH A O 1 HETATM 4499 O O . HOH P 6 . ? -38.199 24.658 -1.742 1.00 34.34 ? 2392 HOH A O 1 HETATM 4500 O O . HOH P 6 . ? -36.005 28.143 -4.912 1.00 42.12 ? 2393 HOH A O 1 HETATM 4501 O O . HOH P 6 . ? -42.682 23.305 -7.377 1.00 32.52 ? 2394 HOH A O 1 HETATM 4502 O O . HOH P 6 . ? -52.883 24.392 -1.517 1.00 41.29 ? 2395 HOH A O 1 HETATM 4503 O O . HOH P 6 . ? -55.734 20.234 5.267 1.00 31.51 ? 2396 HOH A O 1 HETATM 4504 O O . HOH P 6 . ? -60.284 22.408 6.369 1.00 42.03 ? 2397 HOH A O 1 HETATM 4505 O O . HOH P 6 . ? -55.518 16.213 -11.810 1.00 54.36 ? 2398 HOH A O 1 HETATM 4506 O O . HOH P 6 . ? -43.168 11.635 -12.027 1.00 37.38 ? 2399 HOH A O 1 HETATM 4507 O O . HOH P 6 . ? -42.469 8.947 -9.272 1.00 32.04 ? 2400 HOH A O 1 HETATM 4508 O O . HOH P 6 . ? -38.820 7.756 -7.647 1.00 41.61 ? 2401 HOH A O 1 HETATM 4509 O O . HOH P 6 . ? -43.260 4.803 0.228 1.00 48.95 ? 2402 HOH A O 1 HETATM 4510 O O . HOH P 6 . ? -43.410 2.163 0.259 1.00 50.34 ? 2403 HOH A O 1 HETATM 4511 O O . HOH P 6 . ? -37.953 12.035 -5.370 1.00 43.96 ? 2404 HOH A O 1 HETATM 4512 O O . HOH P 6 . ? -40.467 14.707 6.379 1.00 51.92 ? 2405 HOH A O 1 HETATM 4513 O O . HOH P 6 . ? -40.350 6.572 6.065 1.00 51.83 ? 2406 HOH A O 1 HETATM 4514 O O . HOH P 6 . ? -32.619 11.569 4.704 1.00 76.28 ? 2407 HOH A O 1 HETATM 4515 O O . HOH P 6 . ? -32.898 8.788 3.655 1.00 59.73 ? 2408 HOH A O 1 HETATM 4516 O O . HOH P 6 . ? -37.466 20.271 -2.916 1.00 41.54 ? 2409 HOH A O 1 HETATM 4517 O O . HOH P 6 . ? -36.550 14.347 -5.552 1.00 45.61 ? 2410 HOH A O 1 HETATM 4518 O O . HOH P 6 . ? -39.553 19.850 -13.775 1.00 45.06 ? 2411 HOH A O 1 HETATM 4519 O O . HOH P 6 . ? -41.565 14.877 -13.734 1.00 39.72 ? 2412 HOH A O 1 HETATM 4520 O O . HOH P 6 . ? -41.252 17.553 -14.415 1.00 37.43 ? 2413 HOH A O 1 HETATM 4521 O O . HOH P 6 . ? -37.062 16.950 -14.579 1.00 50.30 ? 2414 HOH A O 1 HETATM 4522 O O . HOH P 6 . ? -39.861 9.571 -9.308 1.00 47.48 ? 2415 HOH A O 1 HETATM 4523 O O . HOH P 6 . ? -47.964 16.679 -16.858 1.00 42.95 ? 2416 HOH A O 1 HETATM 4524 O O . HOH P 6 . ? -49.331 25.275 -18.323 1.00 62.40 ? 2417 HOH A O 1 HETATM 4525 O O . HOH P 6 . ? -56.195 20.120 -12.541 1.00 45.83 ? 2418 HOH A O 1 HETATM 4526 O O . HOH P 6 . ? -57.173 22.831 -13.481 1.00 46.73 ? 2419 HOH A O 1 HETATM 4527 O O . HOH P 6 . ? -45.681 5.452 34.936 1.00 51.15 ? 2420 HOH A O 1 HETATM 4528 O O . HOH P 6 . ? -52.238 -11.904 77.555 1.00 64.55 ? 2421 HOH A O 1 HETATM 4529 O O . HOH P 6 . ? -31.745 -1.664 89.499 1.00 85.79 ? 2422 HOH A O 1 HETATM 4530 O O . HOH P 6 . ? -40.143 24.533 45.348 1.00 56.42 ? 2423 HOH A O 1 HETATM 4531 O O . HOH P 6 . ? -30.509 -4.113 94.247 1.00 67.69 ? 2424 HOH A O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . ASN A 8 ? 1.0983 0.8701 0.8581 -0.1163 -0.1264 -0.0724 8 ASN A N 2 C CA . ASN A 8 ? 1.1094 0.8670 0.8696 -0.1042 -0.1206 -0.0776 8 ASN A CA 3 C C . ASN A 8 ? 1.0471 0.8172 0.8192 -0.0919 -0.1134 -0.0793 8 ASN A C 4 O O . ASN A 8 ? 1.0550 0.8461 0.8377 -0.0920 -0.1124 -0.0756 8 ASN A O 5 C CB . ASN A 8 ? 1.1742 0.9003 0.9120 -0.1046 -0.1226 -0.0837 8 ASN A CB 6 C CG . ASN A 8 ? 1.2431 0.9614 0.9698 -0.1024 -0.1224 -0.0878 8 ASN A CG 7 O OD1 . ASN A 8 ? 1.2666 1.0013 0.9986 -0.1053 -0.1231 -0.0854 8 ASN A OD1 8 N ND2 . ASN A 8 ? 1.2850 0.9779 0.9953 -0.0968 -0.1212 -0.0939 8 ASN A ND2 9 N N . SER A 9 ? 0.9653 0.7228 0.7350 -0.0813 -0.1084 -0.0845 9 SER A N 10 C CA . SER A 9 ? 0.8785 0.6465 0.6589 -0.0700 -0.1013 -0.0862 9 SER A CA 11 C C . SER A 9 ? 0.7710 0.5576 0.5702 -0.0658 -0.0973 -0.0824 9 SER A C 12 O O . SER A 9 ? 0.7158 0.5119 0.5241 -0.0576 -0.0916 -0.0831 9 SER A O 13 C CB . SER A 9 ? 0.9000 0.6771 0.6794 -0.0706 -0.1013 -0.0860 9 SER A CB 14 O OG . SER A 9 ? 0.8867 0.6874 0.6795 -0.0733 -0.1013 -0.0801 9 SER A OG 15 N N . THR A 10 ? 0.7226 0.5135 0.5265 -0.0718 -0.1003 -0.0783 10 THR A N 16 C CA . THR A 10 ? 0.6646 0.4702 0.4845 -0.0679 -0.0967 -0.0749 10 THR A CA 17 C C . THR A 10 ? 0.6304 0.4256 0.4484 -0.0703 -0.0987 -0.0748 10 THR A C 18 O O . THR A 10 ? 0.6517 0.4303 0.4563 -0.0763 -0.1033 -0.0762 10 THR A O 19 C CB . THR A 10 ? 0.6566 0.4850 0.4876 -0.0725 -0.0981 -0.0682 10 THR A CB 20 O OG1 . THR A 10 ? 0.6940 0.5220 0.5185 -0.0841 -0.1050 -0.0649 10 THR A OG1 21 C CG2 . THR A 10 ? 0.6741 0.5138 0.5079 -0.0687 -0.0954 -0.0679 10 THR A CG2 22 N N . ALA A 11 ? 0.5653 0.3696 0.3958 -0.0657 -0.0951 -0.0729 11 ALA A N 23 C CA . ALA A 11 ? 0.5528 0.3501 0.3833 -0.0678 -0.0967 -0.0719 11 ALA A CA 24 C C . ALA A 11 ? 0.5280 0.3455 0.3743 -0.0684 -0.0955 -0.0662 11 ALA A C 25 O O . ALA A 11 ? 0.4977 0.3313 0.3538 -0.0646 -0.0921 -0.0642 11 ALA A O 26 C CB . ALA A 11 ? 0.5473 0.3316 0.3752 -0.0586 -0.0925 -0.0768 11 ALA A CB 27 N N . THR A 12 ? 0.5187 0.3340 0.3663 -0.0727 -0.0980 -0.0637 12 THR A N 28 C CA . THR A 12 ? 0.5020 0.3347 0.3640 -0.0723 -0.0965 -0.0585 12 THR A CA 29 C C . THR A 12 ? 0.4861 0.3118 0.3516 -0.0669 -0.0937 -0.0603 12 THR A C 30 O O . THR A 12 ? 0.5072 0.3154 0.3630 -0.0683 -0.0958 -0.0630 12 THR A O 31 C CB . THR A 12 ? 0.5093 0.3499 0.3713 -0.0834 -0.1024 -0.0527 12 THR A CB 32 O OG1 . THR A 12 ? 0.5430 0.3911 0.4014 -0.0886 -0.1053 -0.0509 12 THR A OG1 33 C CG2 . THR A 12 ? 0.5066 0.3664 0.3833 -0.0823 -0.1007 -0.0469 12 THR A CG2 34 N N . LEU A 13 ? 0.4637 0.3024 0.3419 -0.0608 -0.0889 -0.0586 13 LEU A N 35 C CA . LEU A 13 ? 0.4561 0.2911 0.3390 -0.0562 -0.0863 -0.0595 13 LEU A CA 36 C C . LEU A 13 ? 0.4603 0.3118 0.3556 -0.0571 -0.0855 -0.0539 13 LEU A C 37 O O . LEU A 13 ? 0.4593 0.3247 0.3628 -0.0533 -0.0820 -0.0519 13 LEU A O 38 C CB . LEU A 13 ? 0.4478 0.2799 0.3323 -0.0465 -0.0805 -0.0641 13 LEU A CB 39 C CG . LEU A 13 ? 0.4504 0.2798 0.3396 -0.0410 -0.0774 -0.0653 13 LEU A CG 40 C CD1 . LEU A 13 ? 0.4855 0.2975 0.3647 -0.0428 -0.0806 -0.0673 13 LEU A CD1 41 C CD2 . LEU A 13 ? 0.4492 0.2807 0.3413 -0.0325 -0.0715 -0.0689 13 LEU A CD2 42 N N . CYS A 14 ? 0.4766 0.3256 0.3722 -0.0618 -0.0886 -0.0513 14 CYS A N 43 C CA . CYS A 14 ? 0.4684 0.3326 0.3750 -0.0629 -0.0882 -0.0457 14 CYS A CA 44 C C . CYS A 14 ? 0.4572 0.3181 0.3689 -0.0573 -0.0849 -0.0470 14 CYS A C 45 O O . CYS A 14 ? 0.4530 0.2988 0.3584 -0.0560 -0.0853 -0.0507 14 CYS A O 46 C CB . CYS A 14 ? 0.4990 0.3659 0.4030 -0.0733 -0.0944 -0.0409 14 CYS A CB 47 S SG . CYS A 14 ? 0.5425 0.4167 0.4409 -0.0815 -0.0989 -0.0383 14 CYS A SG 48 N N . LEU A 15 ? 0.4219 0.2970 0.3445 -0.0534 -0.0813 -0.0439 15 LEU A N 49 C CA . LEU A 15 ? 0.4198 0.2945 0.3482 -0.0493 -0.0787 -0.0440 15 LEU A CA 50 C C . LEU A 15 ? 0.4110 0.2935 0.3442 -0.0545 -0.0815 -0.0384 15 LEU A C 51 O O . LEU A 15 ? 0.4224 0.3183 0.3592 -0.0580 -0.0831 -0.0334 15 LEU A O 52 C CB . LEU A 15 ? 0.4092 0.2931 0.3449 -0.0421 -0.0728 -0.0443 15 LEU A CB 53 C CG . LEU A 15 ? 0.4267 0.3037 0.3591 -0.0363 -0.0690 -0.0499 15 LEU A CG 54 C CD1 . LEU A 15 ? 0.4619 0.3278 0.3920 -0.0338 -0.0686 -0.0534 15 LEU A CD1 55 C CD2 . LEU A 15 ? 0.4637 0.3358 0.3885 -0.0378 -0.0705 -0.0523 15 LEU A CD2 56 N N . GLY A 16 ? 0.4049 0.2805 0.3385 -0.0545 -0.0821 -0.0387 16 GLY A N 57 C CA . GLY A 16 ? 0.4037 0.2857 0.3410 -0.0601 -0.0852 -0.0334 16 GLY A CA 58 C C . GLY A 16 ? 0.3964 0.2750 0.3376 -0.0570 -0.0836 -0.0336 16 GLY A C 59 O O . GLY A 16 ? 0.3856 0.2569 0.3264 -0.0506 -0.0803 -0.0379 16 GLY A O 60 N N . HIS A 17 ? 0.3894 0.2743 0.3343 -0.0618 -0.0862 -0.0285 17 HIS A N 61 C CA . HIS A 17 ? 0.3970 0.2787 0.3453 -0.0595 -0.0852 -0.0282 17 HIS A CA 62 C C . HIS A 17 ? 0.4039 0.2821 0.3487 -0.0679 -0.0903 -0.0246 17 HIS A C 63 O O . HIS A 17 ? 0.4211 0.3050 0.3638 -0.0756 -0.0943 -0.0209 17 HIS A O 64 C CB . HIS A 17 ? 0.3844 0.2814 0.3438 -0.0542 -0.0808 -0.0253 17 HIS A CB 65 C CG . HIS A 17 ? 0.3912 0.3053 0.3562 -0.0579 -0.0822 -0.0187 17 HIS A CG 66 N ND1 . HIS A 17 ? 0.3996 0.3183 0.3656 -0.0646 -0.0861 -0.0137 17 HIS A ND1 67 C CD2 . HIS A 17 ? 0.4089 0.3370 0.3779 -0.0554 -0.0800 -0.0160 17 HIS A CD2 68 C CE1 . HIS A 17 ? 0.4108 0.3476 0.3821 -0.0661 -0.0863 -0.0079 17 HIS A CE1 69 N NE2 . HIS A 17 ? 0.4097 0.3516 0.3823 -0.0601 -0.0826 -0.0093 17 HIS A NE2 70 N N . HIS A 18 ? 0.4141 0.2829 0.3576 -0.0669 -0.0905 -0.0254 18 HIS A N 71 C CA . HIS A 18 ? 0.4345 0.2968 0.3727 -0.0752 -0.0955 -0.0223 18 HIS A CA 72 C C . HIS A 18 ? 0.4407 0.3213 0.3875 -0.0803 -0.0971 -0.0150 18 HIS A C 73 O O . HIS A 18 ? 0.4144 0.3120 0.3715 -0.0760 -0.0937 -0.0124 18 HIS A O 74 C CB . HIS A 18 ? 0.4448 0.2910 0.3782 -0.0718 -0.0950 -0.0252 18 HIS A CB 75 C CG . HIS A 18 ? 0.4355 0.2910 0.3796 -0.0661 -0.0915 -0.0235 18 HIS A CG 76 N ND1 . HIS A 18 ? 0.4534 0.2994 0.3950 -0.0653 -0.0920 -0.0236 18 HIS A ND1 77 C CD2 . HIS A 18 ? 0.4283 0.3012 0.3846 -0.0610 -0.0873 -0.0216 18 HIS A CD2 78 C CE1 . HIS A 18 ? 0.4448 0.3025 0.3974 -0.0601 -0.0885 -0.0220 18 HIS A CE1 79 N NE2 . HIS A 18 ? 0.4137 0.2871 0.3746 -0.0577 -0.0856 -0.0208 18 HIS A NE2 80 N N . ALA A 19 ? 0.4433 0.3196 0.3846 -0.0898 -0.1022 -0.0115 19 ALA A N 81 C CA . ALA A 19 ? 0.4615 0.3542 0.4098 -0.0956 -0.1042 -0.0042 19 ALA A CA 82 C C . ALA A 19 ? 0.4956 0.3734 0.4351 -0.1033 -0.1087 -0.0032 19 ALA A C 83 O O . ALA A 19 ? 0.5373 0.3936 0.4635 -0.1061 -0.1112 -0.0073 19 ALA A O 84 C CB . ALA A 19 ? 0.4548 0.3642 0.4049 -0.1024 -0.1070 0.0006 19 ALA A CB 85 N N . VAL A 20 ? 0.4965 0.3846 0.4424 -0.1063 -0.1095 0.0022 20 VAL A N 86 C CA . VAL A 20 ? 0.5215 0.3958 0.4596 -0.1129 -0.1132 0.0036 20 VAL A CA 87 C C . VAL A 20 ? 0.5530 0.4423 0.4928 -0.1247 -0.1179 0.0115 20 VAL A C 88 O O . VAL A 20 ? 0.5167 0.4300 0.4671 -0.1246 -0.1169 0.0162 20 VAL A O 89 C CB . VAL A 20 ? 0.5223 0.3931 0.4657 -0.1049 -0.1096 0.0024 20 VAL A CB 90 C CG1 . VAL A 20 ? 0.5184 0.3757 0.4596 -0.0938 -0.1053 -0.0049 20 VAL A CG1 91 C CG2 . VAL A 20 ? 0.4814 0.3763 0.4402 -0.1012 -0.1066 0.0076 20 VAL A CG2 92 N N . PRO A 21 ? 0.6033 0.4783 0.5315 -0.1354 -0.1232 0.0131 21 PRO A N 93 C CA . PRO A 21 ? 0.6279 0.5180 0.5572 -0.1481 -0.1281 0.0211 21 PRO A CA 94 C C . PRO A 21 ? 0.6383 0.5461 0.5800 -0.1463 -0.1263 0.0269 21 PRO A C 95 O O . PRO A 21 ? 0.6958 0.6265 0.6445 -0.1527 -0.1283 0.0343 21 PRO A O 96 C CB . PRO A 21 ? 0.6415 0.5062 0.5519 -0.1600 -0.1341 0.0201 21 PRO A CB 97 C CG . PRO A 21 ? 0.6496 0.4873 0.5516 -0.1510 -0.1314 0.0128 21 PRO A CG 98 C CD . PRO A 21 ? 0.6285 0.4727 0.5408 -0.1362 -0.1249 0.0078 21 PRO A CD 99 N N . ASN A 22 ? 0.6478 0.5467 0.5925 -0.1371 -0.1225 0.0239 22 ASN A N 100 C CA . ASN A 22 ? 0.6408 0.5527 0.5954 -0.1353 -0.1210 0.0289 22 ASN A CA 101 C C . ASN A 22 ? 0.5811 0.5058 0.5496 -0.1209 -0.1141 0.0273 22 ASN A C 102 O O . ASN A 22 ? 0.5614 0.4766 0.5312 -0.1136 -0.1111 0.0242 22 ASN A O 103 C CB . ASN A 22 ? 0.6712 0.5608 0.6162 -0.1381 -0.1230 0.0274 22 ASN A CB 104 C CG . ASN A 22 ? 0.7303 0.5968 0.6691 -0.1277 -0.1196 0.0190 22 ASN A CG 105 O OD1 . ASN A 22 ? 0.7778 0.6383 0.7138 -0.1228 -0.1180 0.0138 22 ASN A OD1 106 N ND2 . ASN A 22 ? 0.7488 0.6035 0.6855 -0.1240 -0.1186 0.0180 22 ASN A ND2 107 N N . GLY A 23 ? 0.5493 0.4947 0.5268 -0.1172 -0.1117 0.0296 23 GLY A N 108 C CA . GLY A 23 ? 0.5439 0.4988 0.5317 -0.1042 -0.1052 0.0278 23 GLY A CA 109 C C . GLY A 23 ? 0.5263 0.4961 0.5234 -0.1016 -0.1034 0.0333 23 GLY A C 110 O O . GLY A 23 ? 0.4992 0.4757 0.4962 -0.1102 -0.1071 0.0392 23 GLY A O 111 N N . THR A 24 ? 0.4790 0.4537 0.4835 -0.0904 -0.0977 0.0315 24 THR A N 112 C CA . THR A 24 ? 0.4635 0.4515 0.4762 -0.0867 -0.0954 0.0363 24 THR A CA 113 C C . THR A 24 ? 0.4122 0.4184 0.4325 -0.0781 -0.0907 0.0386 24 THR A C 114 O O . THR A 24 ? 0.3874 0.3896 0.4068 -0.0715 -0.0874 0.0340 24 THR A O 115 C CB . THR A 24 ? 0.5014 0.4762 0.5145 -0.0807 -0.0928 0.0322 24 THR A CB 116 O OG1 . THR A 24 ? 0.5771 0.5300 0.5811 -0.0847 -0.0957 0.0275 24 THR A OG1 117 C CG2 . THR A 24 ? 0.5223 0.5074 0.5410 -0.0814 -0.0928 0.0380 24 THR A CG2 118 N N . ILE A 25 ? 0.3600 0.3849 0.3866 -0.0777 -0.0900 0.0458 25 ILE A N 119 C CA . ILE A 25 ? 0.3601 0.4022 0.3921 -0.0691 -0.0855 0.0490 25 ILE A CA 120 C C . ILE A 25 ? 0.3254 0.3621 0.3598 -0.0587 -0.0801 0.0458 25 ILE A C 121 O O . ILE A 25 ? 0.3096 0.3418 0.3456 -0.0589 -0.0801 0.0461 25 ILE A O 122 C CB . ILE A 25 ? 0.3723 0.4388 0.4093 -0.0725 -0.0871 0.0587 25 ILE A CB 123 C CG1 . ILE A 25 ? 0.4069 0.4811 0.4413 -0.0835 -0.0925 0.0622 25 ILE A CG1 124 C CG2 . ILE A 25 ? 0.3568 0.4395 0.3980 -0.0613 -0.0816 0.0620 25 ILE A CG2 125 C CD1 . ILE A 25 ? 0.4216 0.5041 0.4552 -0.0801 -0.0912 0.0620 25 ILE A CD1 126 N N . VAL A 26 ? 0.3009 0.3367 0.3345 -0.0501 -0.0755 0.0426 26 VAL A N 127 C CA . VAL A 26 ? 0.2853 0.3170 0.3199 -0.0406 -0.0702 0.0401 26 VAL A CA 128 C C . VAL A 26 ? 0.2854 0.3300 0.3203 -0.0323 -0.0658 0.0435 26 VAL A C 129 O O . VAL A 26 ? 0.2833 0.3395 0.3179 -0.0332 -0.0666 0.0470 26 VAL A O 130 C CB . VAL A 26 ? 0.2803 0.2927 0.3109 -0.0376 -0.0683 0.0313 26 VAL A CB 131 C CG1 . VAL A 26 ? 0.2822 0.2805 0.3111 -0.0437 -0.0719 0.0277 26 VAL A CG1 132 C CG2 . VAL A 26 ? 0.2619 0.2715 0.2887 -0.0361 -0.0673 0.0279 26 VAL A CG2 133 N N . LYS A 27 ? 0.3018 0.3437 0.3362 -0.0242 -0.0611 0.0425 27 LYS A N 134 C CA . LYS A 27 ? 0.3222 0.3726 0.3544 -0.0152 -0.0564 0.0453 27 LYS A CA 135 C C . LYS A 27 ? 0.3213 0.3566 0.3474 -0.0095 -0.0523 0.0384 27 LYS A C 136 O O . LYS A 27 ? 0.2867 0.3082 0.3116 -0.0100 -0.0517 0.0327 27 LYS A O 137 C CB . LYS A 27 ? 0.3632 0.4212 0.3973 -0.0102 -0.0539 0.0500 27 LYS A CB 138 C CG . LYS A 27 ? 0.4105 0.4751 0.4402 0.0004 -0.0485 0.0532 27 LYS A CG 139 C CD . LYS A 27 ? 0.4617 0.5339 0.4928 0.0051 -0.0464 0.0582 27 LYS A CD 140 C CE . LYS A 27 ? 0.4955 0.5670 0.5188 0.0170 -0.0402 0.0595 27 LYS A CE 141 N NZ . LYS A 27 ? 0.5026 0.5804 0.5259 0.0224 -0.0378 0.0642 27 LYS A NZ 142 N N . THR A 28 ? 0.3333 0.3722 0.3550 -0.0043 -0.0497 0.0392 28 THR A N 143 C CA . THR A 28 ? 0.3622 0.3873 0.3770 0.0008 -0.0456 0.0333 28 THR A CA 144 C C . THR A 28 ? 0.3922 0.4222 0.4011 0.0105 -0.0406 0.0371 28 THR A C 145 O O . THR A 28 ? 0.3889 0.4329 0.4000 0.0137 -0.0401 0.0439 28 THR A O 146 C CB . THR A 28 ? 0.3563 0.3762 0.3688 -0.0021 -0.0470 0.0292 28 THR A CB 147 O OG1 . THR A 28 ? 0.3733 0.4070 0.3854 -0.0005 -0.0473 0.0345 28 THR A OG1 148 C CG2 . THR A 28 ? 0.3648 0.3791 0.3812 -0.0112 -0.0521 0.0259 28 THR A CG2 149 N N . ILE A 29 ? 0.4252 0.4433 0.4259 0.0155 -0.0366 0.0329 29 ILE A N 150 C CA . ILE A 29 ? 0.4389 0.4588 0.4312 0.0253 -0.0316 0.0362 29 ILE A CA 151 C C . ILE A 29 ? 0.4533 0.4875 0.4456 0.0277 -0.0321 0.0414 29 ILE A C 152 O O . ILE A 29 ? 0.4842 0.5307 0.4747 0.0345 -0.0300 0.0480 29 ILE A O 153 C CB . ILE A 29 ? 0.4610 0.4623 0.4424 0.0291 -0.0273 0.0303 29 ILE A CB 154 C CG1 . ILE A 29 ? 0.4655 0.4550 0.4473 0.0261 -0.0272 0.0256 29 ILE A CG1 155 C CG2 . ILE A 29 ? 0.4716 0.4727 0.4418 0.0398 -0.0220 0.0342 29 ILE A CG2 156 C CD1 . ILE A 29 ? 0.4803 0.4742 0.4619 0.0303 -0.0255 0.0300 29 ILE A CD1 157 N N . THR A 30 ? 0.4671 0.5006 0.4616 0.0221 -0.0350 0.0386 30 THR A N 158 C CA . THR A 30 ? 0.4870 0.5342 0.4819 0.0230 -0.0361 0.0429 30 THR A CA 159 C C . THR A 30 ? 0.5062 0.5753 0.5099 0.0188 -0.0402 0.0505 30 THR A C 160 O O . THR A 30 ? 0.5097 0.5952 0.5129 0.0230 -0.0396 0.0569 30 THR A O 161 C CB . THR A 30 ? 0.4941 0.5330 0.4886 0.0170 -0.0385 0.0372 30 THR A CB 162 O OG1 . THR A 30 ? 0.4844 0.5047 0.4708 0.0203 -0.0348 0.0306 30 THR A OG1 163 C CG2 . THR A 30 ? 0.5141 0.5669 0.5084 0.0179 -0.0397 0.0415 30 THR A CG2 164 N N . ASN A 31 ? 0.4942 0.5637 0.5053 0.0103 -0.0444 0.0499 31 ASN A N 165 C CA . ASN A 31 ? 0.4881 0.5763 0.5071 0.0033 -0.0493 0.0563 31 ASN A CA 166 C C . ASN A 31 ? 0.4425 0.5336 0.4667 0.0008 -0.0505 0.0588 31 ASN A C 167 O O . ASN A 31 ? 0.3830 0.4589 0.4076 -0.0021 -0.0510 0.0533 31 ASN A O 168 C CB . ASN A 31 ? 0.5209 0.6037 0.5425 -0.0078 -0.0548 0.0524 31 ASN A CB 169 C CG . ASN A 31 ? 0.5648 0.6500 0.5829 -0.0075 -0.0551 0.0517 31 ASN A CG 170 O OD1 . ASN A 31 ? 0.6093 0.7134 0.6290 -0.0073 -0.0562 0.0583 31 ASN A OD1 171 N ND2 . ASN A 31 ? 0.5375 0.6046 0.5510 -0.0078 -0.0542 0.0439 31 ASN A ND2 172 N N . ASP A 32 ? 0.4187 0.5303 0.4468 0.0021 -0.0510 0.0673 32 ASP A N 173 C CA A ASP A 32 ? 0.4300 0.5478 0.4641 -0.0020 -0.0531 0.0709 32 ASP A CA 174 C CA B ASP A 32 ? 0.4237 0.5409 0.4576 -0.0018 -0.0530 0.0707 32 ASP A CA 175 C C . ASP A 32 ? 0.4243 0.5359 0.4626 -0.0152 -0.0593 0.0681 32 ASP A C 176 O O . ASP A 32 ? 0.4164 0.5196 0.4569 -0.0187 -0.0605 0.0661 32 ASP A O 177 C CB A ASP A 32 ? 0.4598 0.6046 0.4978 0.0000 -0.0533 0.0814 32 ASP A CB 178 C CB B ASP A 32 ? 0.4448 0.5884 0.4822 0.0012 -0.0527 0.0811 32 ASP A CB 179 C CG A ASP A 32 ? 0.4857 0.6373 0.5184 0.0144 -0.0469 0.0853 32 ASP A CG 180 C CG B ASP A 32 ? 0.4513 0.6024 0.4945 -0.0024 -0.0545 0.0853 32 ASP A CG 181 O OD1 A ASP A 32 ? 0.5111 0.6570 0.5418 0.0205 -0.0436 0.0852 32 ASP A OD1 182 O OD1 B ASP A 32 ? 0.4601 0.5961 0.5023 -0.0010 -0.0529 0.0809 32 ASP A OD1 183 O OD2 A ASP A 32 ? 0.4985 0.6608 0.5281 0.0198 -0.0452 0.0886 32 ASP A OD2 184 O OD2 B ASP A 32 ? 0.4772 0.6501 0.5257 -0.0071 -0.0575 0.0932 32 ASP A OD2 185 N N . GLN A 33 ? 0.3966 0.5120 0.4352 -0.0223 -0.0632 0.0682 33 GLN A N 186 C CA . GLN A 33 ? 0.4200 0.5292 0.4602 -0.0351 -0.0693 0.0662 33 GLN A CA 187 C C . GLN A 33 ? 0.3956 0.4933 0.4314 -0.0382 -0.0708 0.0603 33 GLN A C 188 O O . GLN A 33 ? 0.4186 0.5276 0.4534 -0.0371 -0.0708 0.0631 33 GLN A O 189 C CB . GLN A 33 ? 0.4521 0.5833 0.4969 -0.0433 -0.0739 0.0750 33 GLN A CB 190 C CG . GLN A 33 ? 0.4890 0.6322 0.5385 -0.0416 -0.0730 0.0812 33 GLN A CG 191 C CD . GLN A 33 ? 0.5377 0.6990 0.5914 -0.0530 -0.0786 0.0889 33 GLN A CD 192 O OE1 . GLN A 33 ? 0.5780 0.7547 0.6321 -0.0580 -0.0814 0.0934 33 GLN A OE1 193 N NE2 . GLN A 33 ? 0.5580 0.7174 0.6143 -0.0577 -0.0804 0.0906 33 GLN A NE2 194 N N . ILE A 34 ? 0.3536 0.4296 0.3865 -0.0411 -0.0717 0.0524 34 ILE A N 195 C CA . ILE A 34 ? 0.3476 0.4119 0.3761 -0.0449 -0.0736 0.0467 34 ILE A CA 196 C C . ILE A 34 ? 0.3357 0.3840 0.3623 -0.0538 -0.0780 0.0425 34 ILE A C 197 O O . ILE A 34 ? 0.3093 0.3477 0.3368 -0.0526 -0.0771 0.0400 34 ILE A O 198 C CB . ILE A 34 ? 0.3627 0.4151 0.3871 -0.0359 -0.0685 0.0404 34 ILE A CB 199 C CG1 . ILE A 34 ? 0.3845 0.4252 0.4044 -0.0402 -0.0707 0.0347 34 ILE A CG1 200 C CG2 . ILE A 34 ? 0.3478 0.3863 0.3718 -0.0311 -0.0652 0.0357 34 ILE A CG2 201 C CD1 . ILE A 34 ? 0.3943 0.4281 0.4099 -0.0323 -0.0661 0.0301 34 ILE A CD1 202 N N . GLU A 35 ? 0.3291 0.3749 0.3523 -0.0627 -0.0828 0.0420 35 GLU A N 203 C CA . GLU A 35 ? 0.3464 0.3748 0.3653 -0.0707 -0.0869 0.0379 35 GLU A CA 204 C C . GLU A 35 ? 0.3251 0.3329 0.3390 -0.0665 -0.0848 0.0289 35 GLU A C 205 O O . GLU A 35 ? 0.3251 0.3317 0.3365 -0.0641 -0.0836 0.0262 35 GLU A O 206 C CB . GLU A 35 ? 0.3828 0.4154 0.3981 -0.0828 -0.0932 0.0413 35 GLU A CB 207 C CG . GLU A 35 ? 0.4330 0.4482 0.4424 -0.0918 -0.0978 0.0390 35 GLU A CG 208 C CD . GLU A 35 ? 0.4958 0.5131 0.4994 -0.1048 -0.1042 0.0422 35 GLU A CD 209 O OE1 . GLU A 35 ? 0.5884 0.6245 0.5956 -0.1113 -0.1069 0.0501 35 GLU A OE1 210 O OE2 . GLU A 35 ? 0.5335 0.5343 0.5285 -0.1087 -0.1065 0.0370 35 GLU A OE2 211 N N . VAL A 36 ? 0.3121 0.3050 0.3247 -0.0657 -0.0845 0.0248 36 VAL A N 212 C CA . VAL A 36 ? 0.3211 0.2948 0.3288 -0.0625 -0.0831 0.0167 36 VAL A CA 213 C C . VAL A 36 ? 0.3383 0.2959 0.3393 -0.0698 -0.0877 0.0144 36 VAL A C 214 O O . VAL A 36 ? 0.3489 0.3092 0.3493 -0.0772 -0.0916 0.0189 36 VAL A O 215 C CB . VAL A 36 ? 0.3152 0.2856 0.3263 -0.0535 -0.0780 0.0138 36 VAL A CB 216 C CG1 . VAL A 36 ? 0.2977 0.2798 0.3120 -0.0463 -0.0734 0.0153 36 VAL A CG1 217 C CG2 . VAL A 36 ? 0.3072 0.2792 0.3220 -0.0541 -0.0784 0.0168 36 VAL A CG2 218 N N . THR A 37 ? 0.3513 0.2919 0.3463 -0.0675 -0.0871 0.0075 37 THR A N 219 C CA . THR A 37 ? 0.3702 0.2928 0.3563 -0.0732 -0.0911 0.0049 37 THR A CA 220 C C . THR A 37 ? 0.3797 0.2949 0.3660 -0.0725 -0.0913 0.0051 37 THR A C 221 O O . THR A 37 ? 0.3946 0.2978 0.3736 -0.0787 -0.0952 0.0055 37 THR A O 222 C CB . THR A 37 ? 0.3791 0.2863 0.3581 -0.0697 -0.0901 -0.0022 37 THR A CB 223 O OG1 . THR A 37 ? 0.3950 0.2995 0.3775 -0.0604 -0.0852 -0.0064 37 THR A OG1 224 C CG2 . THR A 37 ? 0.3628 0.2764 0.3406 -0.0711 -0.0903 -0.0025 37 THR A CG2 225 N N . ASN A 38 ? 0.3636 0.2853 0.3574 -0.0651 -0.0870 0.0051 38 ASN A N 226 C CA . ASN A 38 ? 0.3844 0.2996 0.3788 -0.0635 -0.0868 0.0051 38 ASN A CA 227 C C . ASN A 38 ? 0.3562 0.2842 0.3600 -0.0567 -0.0823 0.0068 38 ASN A C 228 O O . ASN A 38 ? 0.3261 0.2616 0.3333 -0.0516 -0.0787 0.0056 38 ASN A O 229 C CB . ASN A 38 ? 0.4255 0.3221 0.4129 -0.0595 -0.0861 -0.0013 38 ASN A CB 230 C CG . ASN A 38 ? 0.4820 0.3695 0.4673 -0.0590 -0.0869 -0.0010 38 ASN A CG 231 O OD1 . ASN A 38 ? 0.4797 0.3696 0.4654 -0.0647 -0.0898 0.0037 38 ASN A OD1 232 N ND2 . ASN A 38 ? 0.5950 0.4727 0.5781 -0.0520 -0.0844 -0.0060 38 ASN A ND2 233 N N . ALA A 39 ? 0.3469 0.2760 0.3534 -0.0570 -0.0827 0.0095 39 ALA A N 234 C CA . ALA A 39 ? 0.3393 0.2781 0.3533 -0.0507 -0.0786 0.0109 39 ALA A CA 235 C C . ALA A 39 ? 0.3545 0.2864 0.3685 -0.0499 -0.0790 0.0109 39 ALA A C 236 O O . ALA A 39 ? 0.3687 0.2891 0.3768 -0.0546 -0.0826 0.0108 39 ALA A O 237 C CB . ALA A 39 ? 0.3229 0.2802 0.3427 -0.0521 -0.0783 0.0176 39 ALA A CB 238 N N . THR A 40 ? 0.3516 0.2889 0.3709 -0.0439 -0.0754 0.0108 40 THR A N 239 C CA . THR A 40 ? 0.3617 0.2941 0.3817 -0.0426 -0.0755 0.0110 40 THR A CA 240 C C . THR A 40 ? 0.3450 0.2908 0.3719 -0.0404 -0.0733 0.0157 40 THR A C 241 O O . THR A 40 ? 0.3391 0.2950 0.3694 -0.0368 -0.0703 0.0166 40 THR A O 242 C CB . THR A 40 ? 0.3794 0.3014 0.3969 -0.0366 -0.0731 0.0047 40 THR A CB 243 O OG1 . THR A 40 ? 0.4387 0.3534 0.4548 -0.0360 -0.0742 0.0049 40 THR A OG1 244 C CG2 . THR A 40 ? 0.3945 0.3243 0.4166 -0.0305 -0.0684 0.0028 40 THR A CG2 245 N N . GLU A 41 ? 0.3380 0.2833 0.3660 -0.0425 -0.0750 0.0188 41 GLU A N 246 C CA . GLU A 41 ? 0.3325 0.2905 0.3665 -0.0410 -0.0735 0.0239 41 GLU A CA 247 C C . GLU A 41 ? 0.3125 0.2702 0.3490 -0.0336 -0.0694 0.0210 41 GLU A C 248 O O . GLU A 41 ? 0.3177 0.2655 0.3521 -0.0316 -0.0692 0.0172 41 GLU A O 249 C CB . GLU A 41 ? 0.3435 0.3003 0.3770 -0.0469 -0.0772 0.0285 41 GLU A CB 250 C CG . GLU A 41 ? 0.3405 0.3098 0.3798 -0.0459 -0.0762 0.0342 41 GLU A CG 251 C CD . GLU A 41 ? 0.3431 0.3296 0.3867 -0.0449 -0.0745 0.0388 41 GLU A CD 252 O OE1 . GLU A 41 ? 0.3431 0.3366 0.3864 -0.0513 -0.0775 0.0432 41 GLU A OE1 253 O OE2 . GLU A 41 ? 0.3107 0.3032 0.3570 -0.0377 -0.0701 0.0382 41 GLU A OE2 254 N N . LEU A 42 ? 0.2806 0.2490 0.3206 -0.0296 -0.0660 0.0229 42 LEU A N 255 C CA . LEU A 42 ? 0.2705 0.2382 0.3114 -0.0235 -0.0621 0.0203 42 LEU A CA 256 C C . LEU A 42 ? 0.2561 0.2304 0.3004 -0.0221 -0.0614 0.0246 42 LEU A C 257 O O . LEU A 42 ? 0.2473 0.2211 0.2920 -0.0180 -0.0586 0.0229 42 LEU A O 258 C CB . LEU A 42 ? 0.2641 0.2353 0.3037 -0.0193 -0.0583 0.0185 42 LEU A CB 259 C CG . LEU A 42 ? 0.2744 0.2384 0.3104 -0.0195 -0.0581 0.0132 42 LEU A CG 260 C CD1 . LEU A 42 ? 0.2776 0.2436 0.3114 -0.0150 -0.0539 0.0113 42 LEU A CD1 261 C CD2 . LEU A 42 ? 0.2772 0.2307 0.3116 -0.0195 -0.0591 0.0081 42 LEU A CD2 262 N N . VAL A 43 ? 0.2514 0.2326 0.2980 -0.0261 -0.0639 0.0305 43 VAL A N 263 C CA . VAL A 43 ? 0.2508 0.2386 0.3006 -0.0252 -0.0635 0.0350 43 VAL A CA 264 C C . VAL A 43 ? 0.2656 0.2469 0.3151 -0.0300 -0.0673 0.0362 43 VAL A C 265 O O . VAL A 43 ? 0.2627 0.2430 0.3108 -0.0366 -0.0711 0.0388 43 VAL A O 266 C CB . VAL A 43 ? 0.2447 0.2476 0.2971 -0.0255 -0.0631 0.0419 43 VAL A CB 267 C CG1 . VAL A 43 ? 0.2451 0.2553 0.3007 -0.0243 -0.0626 0.0468 43 VAL A CG1 268 C CG2 . VAL A 43 ? 0.2409 0.2483 0.2916 -0.0197 -0.0591 0.0408 43 VAL A CG2 269 N N . GLN A 44 ? 0.2659 0.2425 0.3159 -0.0271 -0.0663 0.0345 44 GLN A N 270 C CA . GLN A 44 ? 0.2833 0.2541 0.3326 -0.0304 -0.0693 0.0363 44 GLN A CA 271 C C . GLN A 44 ? 0.3001 0.2819 0.3529 -0.0333 -0.0704 0.0436 44 GLN A C 272 O O . GLN A 44 ? 0.2788 0.2696 0.3350 -0.0291 -0.0676 0.0459 44 GLN A O 273 C CB . GLN A 44 ? 0.2786 0.2426 0.3275 -0.0256 -0.0676 0.0324 44 GLN A CB 274 C CG . GLN A 44 ? 0.2907 0.2463 0.3374 -0.0277 -0.0704 0.0335 44 GLN A CG 275 C CD . GLN A 44 ? 0.3147 0.2568 0.3549 -0.0315 -0.0737 0.0312 44 GLN A CD 276 O OE1 . GLN A 44 ? 0.3294 0.2658 0.3667 -0.0298 -0.0730 0.0265 44 GLN A OE1 277 N NE2 . GLN A 44 ? 0.3270 0.2635 0.3637 -0.0371 -0.0772 0.0348 44 GLN A NE2 278 N N . SER A 45 ? 0.3125 0.2934 0.3637 -0.0407 -0.0745 0.0474 45 SER A N 279 C CA . SER A 45 ? 0.3526 0.3461 0.4072 -0.0444 -0.0757 0.0550 45 SER A CA 280 C C . SER A 45 ? 0.3780 0.3651 0.4307 -0.0494 -0.0789 0.0579 45 SER A C 281 O O . SER A 45 ? 0.4004 0.3979 0.4559 -0.0526 -0.0800 0.0643 45 SER A O 282 C CB . SER A 45 ? 0.3769 0.3820 0.4325 -0.0494 -0.0773 0.0593 45 SER A CB 283 O OG . SER A 45 ? 0.4216 0.4166 0.4718 -0.0571 -0.0815 0.0582 45 SER A OG 284 N N . SER A 46 ? 0.3959 0.3660 0.4431 -0.0493 -0.0803 0.0533 46 SER A N 285 C CA . SER A 46 ? 0.4424 0.4042 0.4861 -0.0533 -0.0831 0.0559 46 SER A CA 286 C C . SER A 46 ? 0.4404 0.3936 0.4834 -0.0462 -0.0810 0.0519 46 SER A C 287 O O . SER A 46 ? 0.3980 0.3474 0.4411 -0.0399 -0.0783 0.0462 46 SER A O 288 C CB . SER A 46 ? 0.4546 0.4010 0.4890 -0.0610 -0.0876 0.0552 46 SER A CB 289 O OG . SER A 46 ? 0.4647 0.3981 0.4944 -0.0568 -0.0867 0.0481 46 SER A OG 290 N N . SER A 47 ? 0.4829 0.4342 0.5254 -0.0475 -0.0821 0.0554 47 SER A N 291 C CA . SER A 47 ? 0.4961 0.4371 0.5361 -0.0420 -0.0811 0.0523 47 SER A CA 292 C C . SER A 47 ? 0.5481 0.4738 0.5793 -0.0475 -0.0851 0.0542 47 SER A C 293 O O . SER A 47 ? 0.5663 0.4939 0.5957 -0.0558 -0.0881 0.0594 47 SER A O 294 C CB . SER A 47 ? 0.5076 0.4597 0.5542 -0.0374 -0.0785 0.0549 47 SER A CB 295 O OG . SER A 47 ? 0.5186 0.4609 0.5621 -0.0330 -0.0782 0.0526 47 SER A OG 296 N N . THR A 48 ? 0.6052 0.5163 0.6305 -0.0426 -0.0848 0.0502 48 THR A N 297 C CA . THR A 48 ? 0.6650 0.5594 0.6804 -0.0452 -0.0877 0.0517 48 THR A CA 298 C C . THR A 48 ? 0.6559 0.5568 0.6742 -0.0484 -0.0886 0.0579 48 THR A C 299 O O . THR A 48 ? 0.6975 0.5871 0.7076 -0.0546 -0.0919 0.0613 48 THR A O 300 C CB . THR A 48 ? 0.6939 0.5770 0.7050 -0.0360 -0.0858 0.0468 48 THR A CB 301 O OG1 . THR A 48 ? 0.7240 0.6043 0.7342 -0.0315 -0.0842 0.0408 48 THR A OG1 302 C CG2 . THR A 48 ? 0.7123 0.5747 0.7104 -0.0379 -0.0887 0.0478 48 THR A CG2 303 N N . GLY A 49 ? 0.6120 0.5299 0.6408 -0.0439 -0.0855 0.0593 49 GLY A N 304 C CA . GLY A 49 ? 0.6039 0.5298 0.6361 -0.0458 -0.0858 0.0652 49 GLY A CA 305 C C . GLY A 49 ? 0.5879 0.5083 0.6191 -0.0389 -0.0843 0.0639 49 GLY A C 306 O O . GLY A 49 ? 0.6244 0.5524 0.6593 -0.0393 -0.0840 0.0684 49 GLY A O 307 N N . GLY A 50 ? 0.5015 0.4098 0.5278 -0.0326 -0.0834 0.0582 50 GLY A N 308 C CA . GLY A 50 ? 0.4612 0.3673 0.4875 -0.0247 -0.0815 0.0567 50 GLY A CA 309 C C . GLY A 50 ? 0.4019 0.3179 0.4350 -0.0167 -0.0777 0.0518 50 GLY A C 310 O O . GLY A 50 ? 0.3735 0.2901 0.4071 -0.0160 -0.0768 0.0479 50 GLY A O 311 N N . ILE A 51 ? 0.3636 0.2872 0.4012 -0.0114 -0.0756 0.0523 51 ILE A N 312 C CA . ILE A 51 ? 0.3483 0.2799 0.3904 -0.0045 -0.0723 0.0478 51 ILE A CA 313 C C . ILE A 51 ? 0.3776 0.2981 0.4133 0.0015 -0.0723 0.0442 51 ILE A C 314 O O . ILE A 51 ? 0.3749 0.2896 0.4069 0.0041 -0.0730 0.0462 51 ILE A O 315 C CB . ILE A 51 ? 0.3435 0.2879 0.3921 -0.0019 -0.0702 0.0500 51 ILE A CB 316 C CG1 . ILE A 51 ? 0.3414 0.2976 0.3957 -0.0060 -0.0695 0.0533 51 ILE A CG1 317 C CG2 . ILE A 51 ? 0.3516 0.3025 0.4029 0.0044 -0.0673 0.0454 51 ILE A CG2 318 C CD1 . ILE A 51 ? 0.3409 0.3077 0.3998 -0.0042 -0.0679 0.0567 51 ILE A CD1 319 N N . CYS A 52 ? 0.3649 0.2832 0.3990 0.0044 -0.0713 0.0393 52 CYS A N 320 C CA . CYS A 52 ? 0.3902 0.3001 0.4183 0.0113 -0.0708 0.0360 52 CYS A CA 321 C C . CYS A 52 ? 0.3791 0.3001 0.4118 0.0179 -0.0684 0.0352 52 CYS A C 322 O O . CYS A 52 ? 0.3408 0.2759 0.3811 0.0178 -0.0664 0.0341 52 CYS A O 323 C CB . CYS A 52 ? 0.4253 0.3327 0.4515 0.0124 -0.0701 0.0312 52 CYS A CB 324 S SG . CYS A 52 ? 0.4726 0.3644 0.4908 0.0052 -0.0733 0.0316 52 CYS A SG 325 N N . ASP A 53 ? 0.3690 0.2831 0.3962 0.0237 -0.0688 0.0359 53 ASP A N 326 C CA . ASP A 53 ? 0.3687 0.2937 0.3996 0.0300 -0.0668 0.0358 53 ASP A CA 327 C C . ASP A 53 ? 0.3536 0.2873 0.3864 0.0357 -0.0646 0.0313 53 ASP A C 328 O O . ASP A 53 ? 0.3626 0.3075 0.3987 0.0404 -0.0630 0.0311 53 ASP A O 329 C CB . ASP A 53 ? 0.3896 0.3048 0.4137 0.0345 -0.0679 0.0386 53 ASP A CB 330 C CG . ASP A 53 ? 0.4201 0.3200 0.4330 0.0406 -0.0684 0.0367 53 ASP A CG 331 O OD1 . ASP A 53 ? 0.4225 0.3205 0.4336 0.0417 -0.0678 0.0329 53 ASP A OD1 332 O OD2 . ASP A 53 ? 0.4403 0.3290 0.4451 0.0448 -0.0693 0.0390 53 ASP A OD2 333 N N . SER A 54 ? 0.3442 0.2734 0.3746 0.0350 -0.0645 0.0279 54 SER A N 334 C CA . SER A 54 ? 0.3358 0.2739 0.3681 0.0391 -0.0623 0.0238 54 SER A CA 335 C C . SER A 54 ? 0.3288 0.2710 0.3651 0.0333 -0.0618 0.0212 54 SER A C 336 O O . SER A 54 ? 0.3247 0.2585 0.3596 0.0276 -0.0634 0.0223 54 SER A O 337 C CB . SER A 54 ? 0.3570 0.2835 0.3801 0.0460 -0.0626 0.0221 54 SER A CB 338 O OG . SER A 54 ? 0.3650 0.2849 0.3824 0.0517 -0.0632 0.0249 54 SER A OG 339 N N . PRO A 55 ? 0.3165 0.2716 0.3573 0.0344 -0.0596 0.0182 55 PRO A N 340 C CA . PRO A 55 ? 0.3267 0.2950 0.3699 0.0395 -0.0577 0.0171 55 PRO A CA 341 C C . PRO A 55 ? 0.3172 0.2988 0.3665 0.0371 -0.0568 0.0187 55 PRO A C 342 O O . PRO A 55 ? 0.3004 0.2947 0.3519 0.0403 -0.0555 0.0180 55 PRO A O 343 C CB . PRO A 55 ? 0.3151 0.2891 0.3593 0.0390 -0.0563 0.0130 55 PRO A CB 344 C CG . PRO A 55 ? 0.3139 0.2851 0.3603 0.0313 -0.0565 0.0126 55 PRO A CG 345 C CD . PRO A 55 ? 0.3246 0.2825 0.3681 0.0290 -0.0589 0.0158 55 PRO A CD 346 N N . HIS A 56 ? 0.2982 0.2777 0.3497 0.0317 -0.0575 0.0211 56 HIS A N 347 C CA . HIS A 56 ? 0.2949 0.2844 0.3505 0.0297 -0.0566 0.0228 56 HIS A CA 348 C C . HIS A 56 ? 0.3021 0.2904 0.3572 0.0330 -0.0576 0.0264 56 HIS A C 349 O O . HIS A 56 ? 0.3100 0.2866 0.3614 0.0342 -0.0593 0.0286 56 HIS A O 350 C CB . HIS A 56 ? 0.3003 0.2886 0.3578 0.0236 -0.0564 0.0239 56 HIS A CB 351 C CG . HIS A 56 ? 0.2957 0.2831 0.3528 0.0204 -0.0555 0.0207 56 HIS A CG 352 N ND1 . HIS A 56 ? 0.2943 0.2896 0.3518 0.0197 -0.0537 0.0174 56 HIS A ND1 353 C CD2 . HIS A 56 ? 0.3064 0.2857 0.3622 0.0174 -0.0563 0.0207 56 HIS A CD2 354 C CE1 . HIS A 56 ? 0.2970 0.2886 0.3534 0.0169 -0.0532 0.0153 56 HIS A CE1 355 N NE2 . HIS A 56 ? 0.2995 0.2819 0.3553 0.0156 -0.0548 0.0173 56 HIS A NE2 356 N N . GLN A 57 ? 0.2931 0.2928 0.3509 0.0340 -0.0566 0.0271 57 GLN A N 357 C CA . GLN A 57 ? 0.2794 0.2795 0.3371 0.0371 -0.0574 0.0307 57 GLN A CA 358 C C . GLN A 57 ? 0.2744 0.2706 0.3335 0.0326 -0.0581 0.0341 57 GLN A C 359 O O . GLN A 57 ? 0.2676 0.2706 0.3293 0.0290 -0.0570 0.0343 57 GLN A O 360 C CB . GLN A 57 ? 0.2789 0.2937 0.3390 0.0395 -0.0563 0.0305 57 GLN A CB 361 C CG . GLN A 57 ? 0.2745 0.2897 0.3341 0.0435 -0.0571 0.0343 57 GLN A CG 362 C CD . GLN A 57 ? 0.2808 0.3116 0.3426 0.0460 -0.0562 0.0344 57 GLN A CD 363 O OE1 . GLN A 57 ? 0.2936 0.3352 0.3575 0.0422 -0.0551 0.0323 57 GLN A OE1 364 N NE2 . GLN A 57 ? 0.2682 0.2999 0.3286 0.0521 -0.0568 0.0371 57 GLN A NE2 365 N N . ILE A 58 ? 0.2827 0.2677 0.3390 0.0329 -0.0599 0.0370 58 ILE A N 366 C CA . ILE A 58 ? 0.2946 0.2763 0.3521 0.0285 -0.0608 0.0408 58 ILE A CA 367 C C . ILE A 58 ? 0.3127 0.2968 0.3705 0.0309 -0.0612 0.0445 58 ILE A C 368 O O . ILE A 58 ? 0.3483 0.3289 0.4029 0.0361 -0.0619 0.0451 58 ILE A O 369 C CB . ILE A 58 ? 0.3204 0.2882 0.3738 0.0258 -0.0629 0.0422 58 ILE A CB 370 C CG1 . ILE A 58 ? 0.3285 0.2934 0.3811 0.0238 -0.0627 0.0385 58 ILE A CG1 371 C CG2 . ILE A 58 ? 0.3271 0.2943 0.3823 0.0205 -0.0639 0.0468 58 ILE A CG2 372 C CD1 . ILE A 58 ? 0.3321 0.3053 0.3890 0.0198 -0.0611 0.0371 58 ILE A CD1 373 N N . LEU A 59 ? 0.2983 0.2883 0.3593 0.0280 -0.0607 0.0471 59 LEU A N 374 C CA . LEU A 59 ? 0.3104 0.3017 0.3716 0.0295 -0.0613 0.0512 59 LEU A CA 375 C C . LEU A 59 ? 0.3134 0.3007 0.3751 0.0247 -0.0623 0.0556 59 LEU A C 376 O O . LEU A 59 ? 0.3102 0.3033 0.3747 0.0215 -0.0612 0.0563 59 LEU A O 377 C CB . LEU A 59 ? 0.3000 0.3038 0.3640 0.0309 -0.0596 0.0508 59 LEU A CB 378 C CG . LEU A 59 ? 0.3201 0.3267 0.3845 0.0330 -0.0600 0.0548 59 LEU A CG 379 C CD1 . LEU A 59 ? 0.3369 0.3354 0.3976 0.0375 -0.0616 0.0564 59 LEU A CD1 380 C CD2 . LEU A 59 ? 0.3026 0.3216 0.3686 0.0345 -0.0585 0.0533 59 LEU A CD2 381 N N . ASP A 60 ? 0.3149 0.2919 0.3729 0.0243 -0.0644 0.0587 60 ASP A N 382 C CA . ASP A 60 ? 0.3173 0.2914 0.3755 0.0191 -0.0658 0.0637 60 ASP A CA 383 C C . ASP A 60 ? 0.3217 0.3027 0.3822 0.0200 -0.0653 0.0677 60 ASP A C 384 O O . ASP A 60 ? 0.3297 0.3079 0.3879 0.0235 -0.0659 0.0691 60 ASP A O 385 C CB . ASP A 60 ? 0.3405 0.2995 0.3921 0.0173 -0.0685 0.0655 60 ASP A CB 386 C CG . ASP A 60 ? 0.3516 0.3082 0.4029 0.0102 -0.0703 0.0708 60 ASP A CG 387 O OD1 . ASP A 60 ? 0.3357 0.3035 0.3924 0.0081 -0.0693 0.0738 60 ASP A OD1 388 O OD2 . ASP A 60 ? 0.3814 0.3248 0.4262 0.0066 -0.0728 0.0720 60 ASP A OD2 389 N N . GLY A 61 ? 0.3170 0.3073 0.3816 0.0174 -0.0640 0.0697 61 GLY A N 390 C CA . GLY A 61 ? 0.3216 0.3191 0.3882 0.0183 -0.0633 0.0735 61 GLY A CA 391 C C . GLY A 61 ? 0.3471 0.3394 0.4119 0.0161 -0.0654 0.0793 61 GLY A C 392 O O . GLY A 61 ? 0.3525 0.3487 0.4179 0.0180 -0.0651 0.0823 61 GLY A O 393 N N . GLU A 62 ? 0.3680 0.3512 0.4299 0.0116 -0.0676 0.0808 62 GLU A N 394 C CA . GLU A 62 ? 0.3954 0.3722 0.4540 0.0077 -0.0699 0.0866 62 GLU A CA 395 C C . GLU A 62 ? 0.3882 0.3771 0.4515 0.0057 -0.0690 0.0919 62 GLU A C 396 O O . GLU A 62 ? 0.3652 0.3628 0.4323 0.0030 -0.0680 0.0930 62 GLU A O 397 C CB . GLU A 62 ? 0.4409 0.4069 0.4936 0.0119 -0.0710 0.0864 62 GLU A CB 398 C CG . GLU A 62 ? 0.4766 0.4320 0.5244 0.0149 -0.0715 0.0812 62 GLU A CG 399 C CD . GLU A 62 ? 0.5441 0.4855 0.5834 0.0192 -0.0727 0.0815 62 GLU A CD 400 O OE1 . GLU A 62 ? 0.5666 0.5119 0.6063 0.0264 -0.0714 0.0800 62 GLU A OE1 401 O OE2 . GLU A 62 ? 0.6086 0.5345 0.6397 0.0154 -0.0751 0.0831 62 GLU A OE2 402 N N . ASN A 63 ? 0.3923 0.3822 0.4550 0.0076 -0.0691 0.0953 63 ASN A N 403 C CA . ASN A 63 ? 0.4085 0.4102 0.4752 0.0064 -0.0681 0.1005 63 ASN A CA 404 C C . ASN A 63 ? 0.3843 0.3979 0.4550 0.0115 -0.0648 0.0984 63 ASN A C 405 O O . ASN A 63 ? 0.3772 0.4001 0.4502 0.0116 -0.0636 0.1025 63 ASN A O 406 C CB . ASN A 63 ? 0.4548 0.4523 0.5186 0.0059 -0.0696 0.1054 63 ASN A CB 407 C CG . ASN A 63 ? 0.5067 0.4941 0.5657 -0.0012 -0.0728 0.1096 63 ASN A CG 408 O OD1 . ASN A 63 ? 0.5195 0.5086 0.5794 -0.0072 -0.0737 0.1109 63 ASN A OD1 409 N ND2 . ASN A 63 ? 0.5804 0.5569 0.6334 -0.0011 -0.0745 0.1119 63 ASN A ND2 410 N N . CYS A 64 ? 0.3717 0.3846 0.4422 0.0154 -0.0635 0.0923 64 CYS A N 411 C CA . CYS A 64 ? 0.3692 0.3908 0.4413 0.0195 -0.0608 0.0898 64 CYS A CA 412 C C . CYS A 64 ? 0.3563 0.3814 0.4290 0.0190 -0.0589 0.0861 64 CYS A C 413 O O . CYS A 64 ? 0.3465 0.3664 0.4186 0.0179 -0.0596 0.0824 64 CYS A O 414 C CB . CYS A 64 ? 0.4041 0.4235 0.4746 0.0240 -0.0608 0.0857 64 CYS A CB 415 S SG . CYS A 64 ? 0.4543 0.4697 0.5227 0.0265 -0.0625 0.0896 64 CYS A SG 416 N N . THR A 65 ? 0.3290 0.3618 0.4018 0.0205 -0.0565 0.0870 65 THR A N 417 C CA . THR A 65 ? 0.3120 0.3466 0.3833 0.0214 -0.0542 0.0827 65 THR A CA 418 C C . THR A 65 ? 0.2988 0.3323 0.3680 0.0238 -0.0536 0.0773 65 THR A C 419 O O . THR A 65 ? 0.2984 0.3325 0.3677 0.0257 -0.0545 0.0777 65 THR A O 420 C CB . THR A 65 ? 0.3113 0.3528 0.3811 0.0230 -0.0516 0.0855 65 THR A CB 421 O OG1 . THR A 65 ? 0.3224 0.3668 0.3905 0.0258 -0.0508 0.0866 65 THR A OG1 422 C CG2 . THR A 65 ? 0.3317 0.3778 0.4042 0.0208 -0.0521 0.0920 65 THR A CG2 423 N N . LEU A 66 ? 0.2922 0.3250 0.3592 0.0236 -0.0522 0.0726 66 LEU A N 424 C CA . LEU A 66 ? 0.2904 0.3240 0.3548 0.0248 -0.0515 0.0676 66 LEU A CA 425 C C . LEU A 66 ? 0.2892 0.3274 0.3509 0.0267 -0.0503 0.0690 66 LEU A C 426 O O . LEU A 66 ? 0.2764 0.3171 0.3378 0.0278 -0.0510 0.0675 66 LEU A O 427 C CB . LEU A 66 ? 0.2905 0.3222 0.3516 0.0235 -0.0499 0.0630 66 LEU A CB 428 C CG . LEU A 66 ? 0.2939 0.3273 0.3513 0.0232 -0.0491 0.0580 66 LEU A CG 429 C CD1 . LEU A 66 ? 0.2922 0.3277 0.3530 0.0243 -0.0511 0.0567 66 LEU A CD1 430 C CD2 . LEU A 66 ? 0.2699 0.3000 0.3236 0.0211 -0.0478 0.0536 66 LEU A CD2 431 N N . ILE A 67 ? 0.3143 0.3541 0.3734 0.0273 -0.0485 0.0719 67 ILE A N 432 C CA . ILE A 67 ? 0.3282 0.3712 0.3831 0.0292 -0.0470 0.0731 67 ILE A CA 433 C C . ILE A 67 ? 0.3260 0.3722 0.3847 0.0306 -0.0488 0.0769 67 ILE A C 434 O O . ILE A 67 ? 0.3462 0.3952 0.4029 0.0317 -0.0488 0.0760 67 ILE A O 435 C CB . ILE A 67 ? 0.3357 0.3789 0.3856 0.0308 -0.0443 0.0757 67 ILE A CB 436 C CG1 . ILE A 67 ? 0.3588 0.3972 0.4019 0.0302 -0.0422 0.0714 67 ILE A CG1 437 C CG2 . ILE A 67 ? 0.3500 0.3959 0.3954 0.0333 -0.0430 0.0778 67 ILE A CG2 438 C CD1 . ILE A 67 ? 0.3714 0.4070 0.4099 0.0281 -0.0423 0.0654 67 ILE A CD1 439 N N . ASP A 68 ? 0.3339 0.3796 0.3976 0.0301 -0.0504 0.0811 68 ASP A N 440 C CA . ASP A 68 ? 0.3391 0.3861 0.4053 0.0312 -0.0521 0.0846 68 ASP A CA 441 C C . ASP A 68 ? 0.3361 0.3818 0.4028 0.0324 -0.0537 0.0811 68 ASP A C 442 O O . ASP A 68 ? 0.3355 0.3843 0.4018 0.0346 -0.0541 0.0821 68 ASP A O 443 C CB . ASP A 68 ? 0.3586 0.4035 0.4283 0.0293 -0.0538 0.0898 68 ASP A CB 444 C CG . ASP A 68 ? 0.3931 0.4435 0.4631 0.0291 -0.0524 0.0953 68 ASP A CG 445 O OD1 . ASP A 68 ? 0.4214 0.4760 0.4883 0.0316 -0.0502 0.0955 68 ASP A OD1 446 O OD2 . ASP A 68 ? 0.4602 0.5108 0.5327 0.0263 -0.0536 0.0996 68 ASP A OD2 447 N N . ALA A 69 ? 0.3206 0.3624 0.3879 0.0313 -0.0544 0.0773 69 ALA A N 448 C CA . ALA A 69 ? 0.3216 0.3636 0.3891 0.0332 -0.0554 0.0739 69 ALA A CA 449 C C . ALA A 69 ? 0.3289 0.3779 0.3939 0.0339 -0.0543 0.0707 69 ALA A C 450 O O . ALA A 69 ? 0.3335 0.3868 0.3988 0.0363 -0.0552 0.0702 69 ALA A O 451 C CB . ALA A 69 ? 0.3302 0.3669 0.3982 0.0319 -0.0561 0.0704 69 ALA A CB 452 N N . LEU A 70 ? 0.3100 0.3599 0.3716 0.0317 -0.0524 0.0687 70 LEU A N 453 C CA . LEU A 70 ? 0.3097 0.3646 0.3667 0.0308 -0.0514 0.0658 70 LEU A CA 454 C C . LEU A 70 ? 0.3216 0.3813 0.3775 0.0327 -0.0515 0.0689 70 LEU A C 455 O O . LEU A 70 ? 0.3176 0.3834 0.3730 0.0334 -0.0522 0.0678 70 LEU A O 456 C CB . LEU A 70 ? 0.3034 0.3547 0.3546 0.0283 -0.0492 0.0637 70 LEU A CB 457 C CG . LEU A 70 ? 0.3046 0.3574 0.3479 0.0261 -0.0479 0.0604 70 LEU A CG 458 C CD1 . LEU A 70 ? 0.3065 0.3620 0.3494 0.0233 -0.0487 0.0555 70 LEU A CD1 459 C CD2 . LEU A 70 ? 0.3105 0.3568 0.3458 0.0252 -0.0454 0.0601 70 LEU A CD2 460 N N . LEU A 71 ? 0.3229 0.3808 0.3783 0.0336 -0.0506 0.0730 71 LEU A N 461 C CA . LEU A 71 ? 0.3458 0.4076 0.3995 0.0355 -0.0505 0.0763 71 LEU A CA 462 C C . LEU A 71 ? 0.3447 0.4096 0.4031 0.0381 -0.0525 0.0787 71 LEU A C 463 O O . LEU A 71 ? 0.3601 0.4304 0.4172 0.0395 -0.0529 0.0795 71 LEU A O 464 C CB . LEU A 71 ? 0.3502 0.4101 0.4029 0.0364 -0.0490 0.0808 71 LEU A CB 465 C CG . LEU A 71 ? 0.3621 0.4185 0.4090 0.0356 -0.0465 0.0796 71 LEU A CG 466 C CD1 . LEU A 71 ? 0.3716 0.4291 0.4183 0.0378 -0.0451 0.0852 71 LEU A CD1 467 C CD2 . LEU A 71 ? 0.3815 0.4369 0.4194 0.0345 -0.0451 0.0756 71 LEU A CD2 468 N N . GLY A 72 ? 0.3520 0.4128 0.4147 0.0387 -0.0540 0.0798 72 GLY A N 469 C CA . GLY A 72 ? 0.3504 0.4114 0.4155 0.0418 -0.0558 0.0821 72 GLY A CA 470 C C . GLY A 72 ? 0.3796 0.4372 0.4460 0.0426 -0.0564 0.0881 72 GLY A C 471 O O . GLY A 72 ? 0.3597 0.4195 0.4261 0.0453 -0.0572 0.0909 72 GLY A O 472 N N . ASP A 73 ? 0.3826 0.4358 0.4500 0.0399 -0.0561 0.0902 73 ASP A N 473 C CA . ASP A 73 ? 0.4043 0.4540 0.4730 0.0391 -0.0572 0.0961 73 ASP A CA 474 C C . ASP A 73 ? 0.4183 0.4613 0.4866 0.0409 -0.0594 0.0968 73 ASP A C 475 O O . ASP A 73 ? 0.3919 0.4307 0.4597 0.0416 -0.0601 0.0931 73 ASP A O 476 C CB . ASP A 73 ? 0.4183 0.4655 0.4883 0.0353 -0.0568 0.0973 73 ASP A CB 477 C CG . ASP A 73 ? 0.4435 0.4892 0.5147 0.0329 -0.0579 0.1039 73 ASP A CG 478 O OD1 . ASP A 73 ? 0.4856 0.5273 0.5561 0.0335 -0.0596 0.1068 73 ASP A OD1 479 O OD2 . ASP A 73 ? 0.4528 0.5017 0.5251 0.0305 -0.0570 0.1064 73 ASP A OD2 480 N N . PRO A 74 ? 0.4506 0.4923 0.5181 0.0425 -0.0604 0.1015 74 PRO A N 481 C CA . PRO A 74 ? 0.4744 0.5080 0.5392 0.0453 -0.0622 0.1022 74 PRO A CA 482 C C . PRO A 74 ? 0.4819 0.5038 0.5447 0.0432 -0.0637 0.1012 74 PRO A C 483 O O . PRO A 74 ? 0.4832 0.4996 0.5432 0.0468 -0.0644 0.0985 74 PRO A O 484 C CB . PRO A 74 ? 0.5033 0.5358 0.5670 0.0456 -0.0629 0.1083 74 PRO A CB 485 C CG . PRO A 74 ? 0.4958 0.5401 0.5618 0.0460 -0.0610 0.1090 74 PRO A CG 486 C CD . PRO A 74 ? 0.4671 0.5150 0.5350 0.0429 -0.0596 0.1058 74 PRO A CD 487 N N . GLN A 75 ? 0.4771 0.4957 0.5407 0.0376 -0.0641 0.1032 75 GLN A N 488 C CA . GLN A 75 ? 0.4872 0.4944 0.5481 0.0347 -0.0657 0.1022 75 GLN A CA 489 C C . GLN A 75 ? 0.4478 0.4554 0.5095 0.0362 -0.0650 0.0958 75 GLN A C 490 O O . GLN A 75 ? 0.4319 0.4293 0.4904 0.0354 -0.0662 0.0941 75 GLN A O 491 C CB . GLN A 75 ? 0.5045 0.5100 0.5662 0.0277 -0.0665 0.1062 75 GLN A CB 492 C CG . GLN A 75 ? 0.5203 0.5352 0.5868 0.0251 -0.0648 0.1048 75 GLN A CG 493 C CD . GLN A 75 ? 0.5459 0.5626 0.6136 0.0189 -0.0656 0.1102 75 GLN A CD 494 O OE1 . GLN A 75 ? 0.6092 0.6186 0.6739 0.0151 -0.0677 0.1145 75 GLN A OE1 495 N NE2 . GLN A 75 ? 0.5297 0.5561 0.6011 0.0177 -0.0637 0.1102 75 GLN A NE2 496 N N . CYS A 76 ? 0.4163 0.4347 0.4812 0.0382 -0.0630 0.0923 76 CYS A N 497 C CA . CYS A 76 ? 0.4129 0.4330 0.4784 0.0391 -0.0623 0.0865 76 CYS A CA 498 C C . CYS A 76 ? 0.4059 0.4302 0.4705 0.0447 -0.0620 0.0835 76 CYS A C 499 O O . CYS A 76 ? 0.3818 0.4109 0.4474 0.0452 -0.0611 0.0789 76 CYS A O 500 C CB . CYS A 76 ? 0.4353 0.4638 0.5035 0.0365 -0.0603 0.0843 76 CYS A CB 501 S SG . CYS A 76 ? 0.4431 0.4717 0.5129 0.0315 -0.0600 0.0888 76 CYS A SG 502 N N . ASP A 77 ? 0.3931 0.4164 0.4556 0.0489 -0.0627 0.0863 77 ASP A N 503 C CA . ASP A 77 ? 0.4103 0.4404 0.4721 0.0548 -0.0624 0.0842 77 ASP A CA 504 C C . ASP A 77 ? 0.3971 0.4233 0.4569 0.0580 -0.0626 0.0804 77 ASP A C 505 O O . ASP A 77 ? 0.3797 0.4158 0.4406 0.0613 -0.0619 0.0774 77 ASP A O 506 C CB . ASP A 77 ? 0.4363 0.4645 0.4953 0.0594 -0.0632 0.0885 77 ASP A CB 507 C CG . ASP A 77 ? 0.4537 0.4907 0.5151 0.0581 -0.0626 0.0915 77 ASP A CG 508 O OD1 . ASP A 77 ? 0.4434 0.4887 0.5079 0.0547 -0.0613 0.0897 77 ASP A OD1 509 O OD2 . ASP A 77 ? 0.4477 0.4826 0.5071 0.0610 -0.0632 0.0956 77 ASP A OD2 510 N N . GLY A 78 ? 0.4130 0.4255 0.4695 0.0565 -0.0637 0.0807 78 GLY A N 511 C CA . GLY A 78 ? 0.4198 0.4265 0.4733 0.0593 -0.0638 0.0772 78 GLY A CA 512 C C . GLY A 78 ? 0.3863 0.4017 0.4439 0.0568 -0.0626 0.0721 78 GLY A C 513 O O . GLY A 78 ? 0.3679 0.3835 0.4240 0.0604 -0.0623 0.0689 78 GLY A O 514 N N . PHE A 79 ? 0.3730 0.3955 0.4349 0.0513 -0.0618 0.0716 79 PHE A N 515 C CA . PHE A 79 ? 0.3638 0.3925 0.4281 0.0483 -0.0606 0.0671 79 PHE A CA 516 C C . PHE A 79 ? 0.3364 0.3795 0.4024 0.0498 -0.0595 0.0645 79 PHE A C 517 O O . PHE A 79 ? 0.3045 0.3527 0.3714 0.0470 -0.0585 0.0607 79 PHE A O 518 C CB . PHE A 79 ? 0.3921 0.4203 0.4584 0.0421 -0.0599 0.0677 79 PHE A CB 519 C CG . PHE A 79 ? 0.4200 0.4368 0.4853 0.0389 -0.0610 0.0696 79 PHE A CG 520 C CD1 . PHE A 79 ? 0.4552 0.4665 0.5196 0.0377 -0.0622 0.0747 79 PHE A CD1 521 C CD2 . PHE A 79 ? 0.4712 0.4837 0.5364 0.0363 -0.0610 0.0666 79 PHE A CD2 522 C CE1 . PHE A 79 ? 0.4484 0.4505 0.5115 0.0335 -0.0635 0.0769 79 PHE A CE1 523 C CE2 . PHE A 79 ? 0.4845 0.4876 0.5486 0.0326 -0.0622 0.0686 79 PHE A CE2 524 C CZ . PHE A 79 ? 0.4515 0.4496 0.5144 0.0309 -0.0636 0.0738 79 PHE A CZ 525 N N . GLN A 80 ? 0.3197 0.3697 0.3855 0.0536 -0.0597 0.0668 80 GLN A N 526 C CA . GLN A 80 ? 0.3042 0.3691 0.3713 0.0536 -0.0589 0.0649 80 GLN A CA 527 C C . GLN A 80 ? 0.3008 0.3721 0.3682 0.0545 -0.0585 0.0608 80 GLN A C 528 O O . GLN A 80 ? 0.3044 0.3727 0.3706 0.0598 -0.0589 0.0606 80 GLN A O 529 C CB . GLN A 80 ? 0.3228 0.3948 0.3896 0.0587 -0.0594 0.0681 80 GLN A CB 530 C CG . GLN A 80 ? 0.3340 0.4045 0.4008 0.0569 -0.0595 0.0718 80 GLN A CG 531 C CD . GLN A 80 ? 0.3618 0.4422 0.4284 0.0610 -0.0598 0.0743 80 GLN A CD 532 O OE1 . GLN A 80 ? 0.3458 0.4336 0.4122 0.0662 -0.0601 0.0740 80 GLN A OE1 533 N NE2 . GLN A 80 ? 0.3740 0.4553 0.4404 0.0590 -0.0597 0.0771 80 GLN A NE2 534 N N . ASN A 81 ? 0.2737 0.3534 0.3416 0.0495 -0.0576 0.0577 81 ASN A N 535 C CA . ASN A 81 ? 0.2826 0.3715 0.3508 0.0488 -0.0572 0.0540 81 ASN A CA 536 C C . ASN A 81 ? 0.2863 0.3674 0.3545 0.0488 -0.0570 0.0513 81 ASN A C 537 O O . ASN A 81 ? 0.2925 0.3814 0.3609 0.0489 -0.0566 0.0484 81 ASN A O 538 C CB . ASN A 81 ? 0.2944 0.3974 0.3633 0.0544 -0.0576 0.0550 81 ASN A CB 539 C CG . ASN A 81 ? 0.3052 0.4186 0.3740 0.0531 -0.0579 0.0571 81 ASN A CG 540 O OD1 . ASN A 81 ? 0.3065 0.4255 0.3739 0.0464 -0.0575 0.0554 81 ASN A OD1 541 N ND2 . ASN A 81 ? 0.3188 0.4331 0.3878 0.0593 -0.0585 0.0608 81 ASN A ND2 542 N N . LYS A 82 ? 0.2906 0.3573 0.3582 0.0481 -0.0573 0.0522 82 LYS A N 543 C CA . LYS A 82 ? 0.3116 0.3699 0.3786 0.0479 -0.0572 0.0497 82 LYS A CA 544 C C . LYS A 82 ? 0.2956 0.3554 0.3627 0.0415 -0.0562 0.0461 82 LYS A C 545 O O . LYS A 82 ? 0.2774 0.3395 0.3440 0.0370 -0.0555 0.0461 82 LYS A O 546 C CB . LYS A 82 ? 0.3327 0.3753 0.3984 0.0481 -0.0582 0.0521 82 LYS A CB 547 C CG . LYS A 82 ? 0.3691 0.4061 0.4322 0.0547 -0.0593 0.0552 82 LYS A CG 548 C CD . LYS A 82 ? 0.4075 0.4279 0.4677 0.0534 -0.0606 0.0578 82 LYS A CD 549 C CE . LYS A 82 ? 0.4290 0.4382 0.4858 0.0539 -0.0611 0.0556 82 LYS A CE 550 N NZ . LYS A 82 ? 0.4735 0.4665 0.5245 0.0553 -0.0627 0.0589 82 LYS A NZ 551 N N . LYS A 83 ? 0.2927 0.3502 0.3596 0.0418 -0.0560 0.0431 83 LYS A N 552 C CA . LYS A 83 ? 0.2877 0.3449 0.3541 0.0364 -0.0550 0.0395 83 LYS A CA 553 C C . LYS A 83 ? 0.2820 0.3256 0.3479 0.0357 -0.0553 0.0390 83 LYS A C 554 O O . LYS A 83 ? 0.2757 0.3106 0.3409 0.0394 -0.0565 0.0410 83 LYS A O 555 C CB . LYS A 83 ? 0.2972 0.3658 0.3636 0.0366 -0.0544 0.0363 83 LYS A CB 556 C CG . LYS A 83 ? 0.3095 0.3937 0.3763 0.0367 -0.0544 0.0369 83 LYS A CG 557 C CD . LYS A 83 ? 0.3183 0.4149 0.3850 0.0345 -0.0538 0.0338 83 LYS A CD 558 C CE . LYS A 83 ? 0.3433 0.4578 0.4111 0.0364 -0.0541 0.0351 83 LYS A CE 559 N NZ . LYS A 83 ? 0.3363 0.4551 0.4060 0.0460 -0.0545 0.0373 83 LYS A NZ 560 N N . TRP A 84 ? 0.2660 0.3071 0.3312 0.0307 -0.0544 0.0367 84 TRP A N 561 C CA . TRP A 84 ? 0.2587 0.2890 0.3235 0.0294 -0.0547 0.0361 84 TRP A CA 562 C C . TRP A 84 ? 0.2553 0.2865 0.3189 0.0254 -0.0534 0.0323 84 TRP A C 563 O O . TRP A 84 ? 0.2493 0.2865 0.3113 0.0221 -0.0522 0.0309 84 TRP A O 564 C CB . TRP A 84 ? 0.2518 0.2746 0.3168 0.0273 -0.0552 0.0396 84 TRP A CB 565 C CG . TRP A 84 ? 0.2473 0.2741 0.3115 0.0239 -0.0537 0.0402 84 TRP A CG 566 C CD1 . TRP A 84 ? 0.2404 0.2651 0.3027 0.0203 -0.0523 0.0388 84 TRP A CD1 567 C CD2 . TRP A 84 ? 0.2456 0.2785 0.3095 0.0244 -0.0534 0.0423 84 TRP A CD2 568 N NE1 . TRP A 84 ? 0.2373 0.2651 0.2970 0.0190 -0.0510 0.0398 84 TRP A NE1 569 C CE2 . TRP A 84 ? 0.2467 0.2796 0.3074 0.0210 -0.0517 0.0419 84 TRP A CE2 570 C CE3 . TRP A 84 ? 0.2536 0.2913 0.3185 0.0277 -0.0542 0.0444 84 TRP A CE3 571 C CZ2 . TRP A 84 ? 0.2465 0.2833 0.3049 0.0207 -0.0509 0.0435 84 TRP A CZ2 572 C CZ3 . TRP A 84 ? 0.2560 0.2991 0.3198 0.0269 -0.0536 0.0461 84 TRP A CZ3 573 C CH2 . TRP A 84 ? 0.2554 0.2979 0.3157 0.0234 -0.0520 0.0455 84 TRP A CH2 574 N N . ASP A 85 ? 0.2543 0.2780 0.3177 0.0251 -0.0538 0.0309 85 ASP A N 575 C CA . ASP A 85 ? 0.2476 0.2686 0.3096 0.0210 -0.0527 0.0284 85 ASP A CA 576 C C . ASP A 85 ? 0.2437 0.2584 0.3055 0.0186 -0.0527 0.0312 85 ASP A C 577 O O . ASP A 85 ? 0.2375 0.2527 0.2973 0.0156 -0.0511 0.0306 85 ASP A O 578 C CB . ASP A 85 ? 0.2529 0.2696 0.3146 0.0220 -0.0531 0.0256 85 ASP A CB 579 C CG . ASP A 85 ? 0.2709 0.2960 0.3326 0.0246 -0.0527 0.0229 85 ASP A CG 580 O OD1 . ASP A 85 ? 0.2673 0.3027 0.3288 0.0229 -0.0517 0.0219 85 ASP A OD1 581 O OD2 . ASP A 85 ? 0.2675 0.2889 0.3286 0.0281 -0.0533 0.0218 85 ASP A OD2 582 N N . LEU A 86 ? 0.2431 0.2517 0.3063 0.0198 -0.0543 0.0344 86 LEU A N 583 C CA . LEU A 86 ? 0.2498 0.2546 0.3134 0.0175 -0.0546 0.0379 86 LEU A CA 584 C C . LEU A 86 ? 0.2456 0.2497 0.3105 0.0188 -0.0559 0.0425 86 LEU A C 585 O O . LEU A 86 ? 0.2557 0.2549 0.3202 0.0207 -0.0577 0.0437 86 LEU A O 586 C CB . LEU A 86 ? 0.2407 0.2382 0.3040 0.0153 -0.0555 0.0376 86 LEU A CB 587 C CG . LEU A 86 ? 0.2469 0.2438 0.3110 0.0125 -0.0555 0.0415 86 LEU A CG 588 C CD1 . LEU A 86 ? 0.2369 0.2386 0.2995 0.0118 -0.0528 0.0407 86 LEU A CD1 589 C CD2 . LEU A 86 ? 0.2401 0.2305 0.3038 0.0100 -0.0570 0.0415 86 LEU A CD2 590 N N . PHE A 87 ? 0.2522 0.2608 0.3174 0.0181 -0.0548 0.0452 87 PHE A N 591 C CA . PHE A 87 ? 0.2538 0.2627 0.3202 0.0188 -0.0558 0.0501 87 PHE A CA 592 C C . PHE A 87 ? 0.2561 0.2619 0.3234 0.0159 -0.0565 0.0537 87 PHE A C 593 O O . PHE A 87 ? 0.2516 0.2597 0.3186 0.0143 -0.0550 0.0537 87 PHE A O 594 C CB . PHE A 87 ? 0.2535 0.2693 0.3193 0.0197 -0.0542 0.0512 87 PHE A CB 595 C CG . PHE A 87 ? 0.2664 0.2834 0.3335 0.0211 -0.0551 0.0559 87 PHE A CG 596 C CD1 . PHE A 87 ? 0.2690 0.2850 0.3373 0.0195 -0.0557 0.0607 87 PHE A CD1 597 C CD2 . PHE A 87 ? 0.2812 0.3013 0.3484 0.0240 -0.0556 0.0558 87 PHE A CD2 598 C CE1 . PHE A 87 ? 0.2875 0.3046 0.3568 0.0204 -0.0566 0.0653 87 PHE A CE1 599 C CE2 . PHE A 87 ? 0.2920 0.3126 0.3600 0.0254 -0.0565 0.0603 87 PHE A CE2 600 C CZ . PHE A 87 ? 0.2855 0.3043 0.3545 0.0234 -0.0570 0.0649 87 PHE A CZ 601 N N . VAL A 88 ? 0.2663 0.2669 0.3339 0.0150 -0.0588 0.0570 88 VAL A N 602 C CA . VAL A 88 ? 0.2794 0.2781 0.3476 0.0110 -0.0600 0.0609 88 VAL A CA 603 C C . VAL A 88 ? 0.2872 0.2900 0.3569 0.0104 -0.0604 0.0668 88 VAL A C 604 O O . VAL A 88 ? 0.2967 0.2959 0.3654 0.0113 -0.0619 0.0688 88 VAL A O 605 C CB . VAL A 88 ? 0.2876 0.2761 0.3536 0.0086 -0.0626 0.0605 88 VAL A CB 606 C CG1 . VAL A 88 ? 0.2950 0.2827 0.3613 0.0031 -0.0644 0.0653 88 VAL A CG1 607 C CG2 . VAL A 88 ? 0.2756 0.2611 0.3404 0.0092 -0.0620 0.0548 88 VAL A CG2 608 N N . GLU A 89 ? 0.2911 0.3013 0.3623 0.0094 -0.0589 0.0698 89 GLU A N 609 C CA . GLU A 89 ? 0.3108 0.3268 0.3834 0.0091 -0.0589 0.0758 89 GLU A CA 610 C C . GLU A 89 ? 0.3061 0.3227 0.3799 0.0040 -0.0609 0.0809 89 GLU A C 611 O O . GLU A 89 ? 0.2925 0.3116 0.3669 0.0019 -0.0606 0.0809 89 GLU A O 612 C CB . GLU A 89 ? 0.3223 0.3471 0.3949 0.0119 -0.0557 0.0768 89 GLU A CB 613 C CG . GLU A 89 ? 0.3363 0.3618 0.4068 0.0157 -0.0539 0.0734 89 GLU A CG 614 C CD . GLU A 89 ? 0.3282 0.3599 0.3962 0.0184 -0.0509 0.0748 89 GLU A CD 615 O OE1 . GLU A 89 ? 0.3105 0.3449 0.3772 0.0186 -0.0492 0.0761 89 GLU A OE1 616 O OE2 . GLU A 89 ? 0.3176 0.3508 0.3840 0.0208 -0.0501 0.0746 89 GLU A OE2 617 N N . ARG A 90 ? 0.3192 0.3345 0.3931 0.0019 -0.0629 0.0856 90 ARG A N 618 C CA . ARG A 90 ? 0.3312 0.3463 0.4051 -0.0043 -0.0655 0.0910 90 ARG A CA 619 C C . ARG A 90 ? 0.3350 0.3635 0.4121 -0.0052 -0.0644 0.0976 90 ARG A C 620 O O . ARG A 90 ? 0.3348 0.3690 0.4129 -0.0011 -0.0624 0.0989 90 ARG A O 621 C CB . ARG A 90 ? 0.3369 0.3409 0.4072 -0.0066 -0.0685 0.0925 90 ARG A CB 622 C CG . ARG A 90 ? 0.3437 0.3350 0.4099 -0.0037 -0.0692 0.0866 90 ARG A CG 623 C CD . ARG A 90 ? 0.3433 0.3297 0.4081 -0.0058 -0.0697 0.0826 90 ARG A CD 624 N NE . ARG A 90 ? 0.3480 0.3200 0.4072 -0.0046 -0.0712 0.0786 90 ARG A NE 625 C CZ . ARG A 90 ? 0.3436 0.3084 0.3999 -0.0070 -0.0723 0.0756 90 ARG A CZ 626 N NH1 . ARG A 90 ? 0.3354 0.3065 0.3945 -0.0111 -0.0722 0.0763 90 ARG A NH1 627 N NH2 . ARG A 90 ? 0.3651 0.3165 0.4153 -0.0049 -0.0735 0.0721 90 ARG A NH2 628 N N . SER A 91 ? 0.3595 0.3936 0.4379 -0.0105 -0.0657 0.1019 91 SER A N 629 C CA . SER A 91 ? 0.3799 0.4289 0.4615 -0.0111 -0.0645 0.1089 91 SER A CA 630 C C . SER A 91 ? 0.3976 0.4477 0.4792 -0.0129 -0.0659 0.1143 91 SER A C 631 O O . SER A 91 ? 0.4131 0.4752 0.4971 -0.0107 -0.0641 0.1191 91 SER A O 632 C CB . SER A 91 ? 0.3864 0.4431 0.4696 -0.0169 -0.0659 0.1130 91 SER A CB 633 O OG . SER A 91 ? 0.4081 0.4578 0.4891 -0.0254 -0.0701 0.1157 91 SER A OG 634 N N . LYS A 92 ? 0.4144 0.4515 0.4925 -0.0164 -0.0689 0.1135 92 LYS A N 635 C CA . LYS A 92 ? 0.4578 0.4938 0.5348 -0.0182 -0.0703 0.1185 92 LYS A CA 636 C C . LYS A 92 ? 0.4209 0.4572 0.4984 -0.0106 -0.0679 0.1164 92 LYS A C 637 O O . LYS A 92 ? 0.4185 0.4554 0.4953 -0.0109 -0.0685 0.1205 92 LYS A O 638 C CB . LYS A 92 ? 0.4994 0.5184 0.5701 -0.0240 -0.0742 0.1182 92 LYS A CB 639 C CG . LYS A 92 ? 0.5340 0.5381 0.6005 -0.0184 -0.0740 0.1113 92 LYS A CG 640 C CD . LYS A 92 ? 0.5898 0.5751 0.6480 -0.0230 -0.0775 0.1104 92 LYS A CD 641 C CE . LYS A 92 ? 0.6286 0.6016 0.6829 -0.0158 -0.0768 0.1037 92 LYS A CE 642 N NZ . LYS A 92 ? 0.6410 0.5942 0.6852 -0.0179 -0.0796 0.1033 92 LYS A NZ 643 N N . ALA A 93 ? 0.4072 0.4428 0.4851 -0.0042 -0.0653 0.1101 93 ALA A N 644 C CA . ALA A 93 ? 0.3861 0.4209 0.4635 0.0020 -0.0635 0.1076 93 ALA A CA 645 C C . ALA A 93 ? 0.3935 0.4403 0.4730 0.0040 -0.0617 0.1131 93 ALA A C 646 O O . ALA A 93 ? 0.3770 0.4346 0.4586 0.0034 -0.0603 0.1168 93 ALA A O 647 C CB . ALA A 93 ? 0.3753 0.4093 0.4523 0.0070 -0.0611 0.1005 93 ALA A CB 648 N N . TYR A 94 ? 0.3951 0.4403 0.4736 0.0067 -0.0617 0.1140 94 TYR A N 649 C CA . TYR A 94 ? 0.4209 0.4769 0.5009 0.0090 -0.0599 0.1192 94 TYR A CA 650 C C . TYR A 94 ? 0.4101 0.4637 0.4885 0.0144 -0.0589 0.1165 94 TYR A C 651 O O . TYR A 94 ? 0.3920 0.4363 0.4685 0.0151 -0.0603 0.1130 94 TYR A O 652 C CB . TYR A 94 ? 0.4461 0.5051 0.5270 0.0034 -0.0622 0.1269 94 TYR A CB 653 C CG . TYR A 94 ? 0.4753 0.5215 0.5529 0.0007 -0.0652 0.1270 94 TYR A CG 654 C CD1 . TYR A 94 ? 0.4969 0.5309 0.5713 -0.0040 -0.0681 0.1251 94 TYR A CD1 655 C CD2 . TYR A 94 ? 0.5080 0.5533 0.5844 0.0034 -0.0652 0.1291 94 TYR A CD2 656 C CE1 . TYR A 94 ? 0.5190 0.5392 0.5881 -0.0056 -0.0706 0.1253 94 TYR A CE1 657 C CE2 . TYR A 94 ? 0.5264 0.5590 0.5984 0.0019 -0.0677 0.1294 94 TYR A CE2 658 C CZ . TYR A 94 ? 0.5419 0.5614 0.6098 -0.0024 -0.0704 0.1275 94 TYR A CZ 659 O OH . TYR A 94 ? 0.5491 0.5537 0.6104 -0.0032 -0.0727 0.1277 94 TYR A OH 660 N N . SER A 95 ? 0.4124 0.4747 0.4908 0.0185 -0.0562 0.1182 95 SER A N 661 C CA . SER A 95 ? 0.4180 0.4791 0.4945 0.0231 -0.0553 0.1161 95 SER A CA 662 C C . SER A 95 ? 0.4306 0.4927 0.5076 0.0223 -0.0567 0.1217 95 SER A C 663 O O . SER A 95 ? 0.4200 0.4879 0.4987 0.0192 -0.0572 0.1281 95 SER A O 664 C CB . SER A 95 ? 0.4278 0.4958 0.5021 0.0278 -0.0518 0.1151 95 SER A CB 665 O OG . SER A 95 ? 0.4207 0.4868 0.4932 0.0284 -0.0504 0.1103 95 SER A OG 666 N N . ASN A 96 ? 0.4300 0.4871 0.5054 0.0249 -0.0575 0.1196 96 ASN A N 667 C CA . ASN A 96 ? 0.4660 0.5226 0.5410 0.0244 -0.0589 0.1248 96 ASN A CA 668 C C . ASN A 96 ? 0.4413 0.5001 0.5149 0.0297 -0.0577 0.1234 96 ASN A C 669 O O . ASN A 96 ? 0.4275 0.4816 0.4997 0.0308 -0.0593 0.1243 96 ASN A O 670 C CB . ASN A 96 ? 0.5125 0.5573 0.5857 0.0206 -0.0621 0.1252 96 ASN A CB 671 C CG . ASN A 96 ? 0.5457 0.5892 0.6177 0.0174 -0.0638 0.1322 96 ASN A CG 672 O OD1 . ASN A 96 ? 0.5615 0.6150 0.6357 0.0160 -0.0629 0.1377 96 ASN A OD1 673 N ND2 . ASN A 96 ? 0.5459 0.5770 0.6136 0.0167 -0.0662 0.1322 96 ASN A ND2 674 N N . CYS A 97 ? 0.4394 0.5051 0.5123 0.0330 -0.0550 0.1215 97 CYS A N 675 C CA . CYS A 97 ? 0.4491 0.5175 0.5197 0.0374 -0.0539 0.1199 97 CYS A CA 676 C C . CYS A 97 ? 0.4354 0.5120 0.5044 0.0395 -0.0511 0.1227 97 CYS A C 677 O O . CYS A 97 ? 0.4337 0.5151 0.5044 0.0379 -0.0505 0.1278 97 CYS A O 678 C CB . CYS A 97 ? 0.4716 0.5366 0.5404 0.0390 -0.0538 0.1125 97 CYS A CB 679 S SG . CYS A 97 ? 0.4972 0.5653 0.5630 0.0431 -0.0534 0.1095 97 CYS A SG 680 N N . TYR A 98 ? 0.4399 0.5183 0.5048 0.0430 -0.0494 0.1198 98 TYR A N 681 C CA . TYR A 98 ? 0.4463 0.5306 0.5076 0.0459 -0.0465 0.1223 98 TYR A CA 682 C C . TYR A 98 ? 0.4588 0.5436 0.5183 0.0460 -0.0444 0.1212 98 TYR A C 683 O O . TYR A 98 ? 0.4485 0.5281 0.5066 0.0448 -0.0444 0.1156 98 TYR A O 684 C CB . TYR A 98 ? 0.4519 0.5358 0.5074 0.0490 -0.0453 0.1187 98 TYR A CB 685 C CG . TYR A 98 ? 0.4445 0.5335 0.4958 0.0525 -0.0432 0.1228 98 TYR A CG 686 C CD1 . TYR A 98 ? 0.4564 0.5490 0.5097 0.0535 -0.0442 0.1271 98 TYR A CD1 687 C CD2 . TYR A 98 ? 0.4450 0.5343 0.4891 0.0555 -0.0400 0.1221 98 TYR A CD2 688 C CE1 . TYR A 98 ? 0.4429 0.5404 0.4922 0.0570 -0.0422 0.1308 98 TYR A CE1 689 C CE2 . TYR A 98 ? 0.4612 0.5544 0.5003 0.0595 -0.0378 0.1258 98 TYR A CE2 690 C CZ . TYR A 98 ? 0.4512 0.5489 0.4933 0.0600 -0.0390 0.1301 98 TYR A CZ 691 O OH . TYR A 98 ? 0.4453 0.5471 0.4823 0.0642 -0.0368 0.1338 98 TYR A OH 692 N N . PRO A 99 ? 0.4495 0.5410 0.5086 0.0476 -0.0424 0.1267 99 PRO A N 693 C CA . PRO A 99 ? 0.4367 0.5292 0.4934 0.0487 -0.0402 0.1260 99 PRO A CA 694 C C . PRO A 99 ? 0.4284 0.5148 0.4761 0.0520 -0.0377 0.1199 99 PRO A C 695 O O . PRO A 99 ? 0.3991 0.4845 0.4404 0.0551 -0.0363 0.1191 99 PRO A O 696 C CB . PRO A 99 ? 0.4577 0.5608 0.5152 0.0510 -0.0383 0.1339 99 PRO A CB 697 C CG . PRO A 99 ? 0.4609 0.5676 0.5197 0.0517 -0.0391 0.1379 99 PRO A CG 698 C CD . PRO A 99 ? 0.4536 0.5531 0.5152 0.0483 -0.0423 0.1343 99 PRO A CD 699 N N . TYR A 100 ? 0.3888 0.4704 0.4350 0.0507 -0.0373 0.1156 100 TYR A N 700 C CA . TYR A 100 ? 0.4010 0.4752 0.4375 0.0527 -0.0352 0.1096 100 TYR A CA 701 C C . TYR A 100 ? 0.3992 0.4715 0.4322 0.0540 -0.0330 0.1089 100 TYR A C 702 O O . TYR A 100 ? 0.3996 0.4768 0.4394 0.0524 -0.0338 0.1119 100 TYR A O 703 C CB . TYR A 100 ? 0.4076 0.4754 0.4446 0.0489 -0.0375 0.1030 100 TYR A CB 704 C CG . TYR A 100 ? 0.4071 0.4729 0.4507 0.0450 -0.0396 0.1006 100 TYR A CG 705 C CD1 . TYR A 100 ? 0.4114 0.4796 0.4639 0.0423 -0.0425 0.1031 100 TYR A CD1 706 C CD2 . TYR A 100 ? 0.4026 0.4629 0.4422 0.0441 -0.0385 0.0958 100 TYR A CD2 707 C CE1 . TYR A 100 ? 0.4229 0.4879 0.4800 0.0389 -0.0444 0.1008 100 TYR A CE1 708 C CE2 . TYR A 100 ? 0.3969 0.4554 0.4423 0.0407 -0.0403 0.0937 100 TYR A CE2 709 C CZ . TYR A 100 ? 0.4120 0.4728 0.4660 0.0382 -0.0433 0.0962 100 TYR A CZ 710 O OH . TYR A 100 ? 0.3930 0.4507 0.4513 0.0350 -0.0451 0.0940 100 TYR A OH 711 N N . ASP A 101 ? 0.4225 0.4876 0.4439 0.0569 -0.0302 0.1051 101 ASP A N 712 C CA . ASP A 101 ? 0.4257 0.4858 0.4421 0.0578 -0.0284 0.1024 101 ASP A CA 713 C C . ASP A 101 ? 0.4196 0.4681 0.4273 0.0554 -0.0283 0.0947 101 ASP A C 714 O O . ASP A 101 ? 0.3995 0.4448 0.4030 0.0540 -0.0291 0.0920 101 ASP A O 715 C CB . ASP A 101 ? 0.5030 0.5649 0.5110 0.0648 -0.0242 0.1067 101 ASP A CB 716 C CG . ASP A 101 ? 0.5708 0.6282 0.5669 0.0694 -0.0218 0.1068 101 ASP A CG 717 O OD1 . ASP A 101 ? 0.5935 0.6397 0.5795 0.0680 -0.0216 0.1009 101 ASP A OD1 718 O OD2 . ASP A 101 ? 0.6991 0.7645 0.6954 0.0741 -0.0202 0.1130 101 ASP A OD2 719 N N . VAL A 102 ? 0.3828 0.4258 0.3875 0.0545 -0.0275 0.0913 102 VAL A N 720 C CA . VAL A 102 ? 0.3809 0.4130 0.3763 0.0518 -0.0272 0.0843 102 VAL A CA 721 C C . VAL A 102 ? 0.3946 0.4186 0.3772 0.0560 -0.0234 0.0836 102 VAL A C 722 O O . VAL A 102 ? 0.3804 0.4057 0.3663 0.0567 -0.0229 0.0843 102 VAL A O 723 C CB . VAL A 102 ? 0.3743 0.4064 0.3784 0.0460 -0.0301 0.0802 102 VAL A CB 724 C CG1 . VAL A 102 ? 0.3686 0.3912 0.3631 0.0424 -0.0300 0.0733 102 VAL A CG1 725 C CG2 . VAL A 102 ? 0.3684 0.4084 0.3854 0.0432 -0.0337 0.0818 102 VAL A CG2 726 N N . PRO A 103 ? 0.4116 0.4263 0.3784 0.0590 -0.0208 0.0823 103 PRO A N 727 C CA . PRO A 103 ? 0.4299 0.4338 0.3825 0.0629 -0.0172 0.0808 103 PRO A CA 728 C C . PRO A 103 ? 0.4361 0.4339 0.3894 0.0571 -0.0186 0.0749 103 PRO A C 729 O O . PRO A 103 ? 0.4505 0.4466 0.4059 0.0505 -0.0213 0.0704 103 PRO A O 730 C CB . PRO A 103 ? 0.4438 0.4355 0.3777 0.0649 -0.0150 0.0788 103 PRO A CB 731 C CG . PRO A 103 ? 0.4405 0.4415 0.3808 0.0659 -0.0162 0.0827 103 PRO A CG 732 C CD . PRO A 103 ? 0.4225 0.4353 0.3823 0.0599 -0.0206 0.0827 103 PRO A CD 733 N N . ASP A 104 ? 0.4404 0.4368 0.3931 0.0595 -0.0170 0.0754 104 ASP A N 734 C CA . ASP A 104 ? 0.4403 0.4325 0.3957 0.0541 -0.0185 0.0703 104 ASP A CA 735 C C . ASP A 104 ? 0.3855 0.3877 0.3587 0.0477 -0.0229 0.0693 104 ASP A C 736 O O . ASP A 104 ? 0.3705 0.3695 0.3448 0.0418 -0.0249 0.0641 104 ASP A O 737 C CB . ASP A 104 ? 0.4833 0.4596 0.4219 0.0506 -0.0175 0.0639 104 ASP A CB 738 C CG . ASP A 104 ? 0.5345 0.5036 0.4699 0.0483 -0.0170 0.0600 104 ASP A CG 739 O OD1 . ASP A 104 ? 0.5264 0.5018 0.4711 0.0501 -0.0170 0.0620 104 ASP A OD1 740 O OD2 . ASP A 104 ? 0.6162 0.5728 0.5385 0.0440 -0.0166 0.0548 104 ASP A OD2 741 N N . TYR A 105 ? 0.3539 0.3681 0.3400 0.0493 -0.0242 0.0746 105 TYR A N 742 C CA . TYR A 105 ? 0.3311 0.3534 0.3328 0.0446 -0.0280 0.0747 105 TYR A CA 743 C C . TYR A 105 ? 0.3129 0.3317 0.3173 0.0409 -0.0291 0.0704 105 TYR A C 744 O O . TYR A 105 ? 0.3014 0.3204 0.3115 0.0361 -0.0317 0.0668 105 TYR A O 745 C CB . TYR A 105 ? 0.3349 0.3685 0.3467 0.0471 -0.0285 0.0818 105 TYR A CB 746 C CG . TYR A 105 ? 0.3359 0.3760 0.3617 0.0425 -0.0324 0.0827 105 TYR A CG 747 C CD1 . TYR A 105 ? 0.3502 0.3907 0.3820 0.0397 -0.0338 0.0817 105 TYR A CD1 748 C CD2 . TYR A 105 ? 0.3398 0.3847 0.3718 0.0412 -0.0346 0.0850 105 TYR A CD2 749 C CE1 . TYR A 105 ? 0.3408 0.3849 0.3833 0.0356 -0.0373 0.0825 105 TYR A CE1 750 C CE2 . TYR A 105 ? 0.3451 0.3935 0.3877 0.0375 -0.0379 0.0861 105 TYR A CE2 751 C CZ . TYR A 105 ? 0.3474 0.3947 0.3946 0.0346 -0.0393 0.0846 105 TYR A CZ 752 O OH . TYR A 105 ? 0.3698 0.4183 0.4254 0.0310 -0.0426 0.0855 105 TYR A OH 753 N N . ALA A 106 ? 0.3047 0.3208 0.3047 0.0436 -0.0268 0.0710 106 ALA A N 754 C CA . ALA A 106 ? 0.2967 0.3099 0.2993 0.0404 -0.0276 0.0674 106 ALA A CA 755 C C . ALA A 106 ? 0.3052 0.3095 0.3012 0.0360 -0.0281 0.0606 106 ALA A C 756 O O . ALA A 106 ? 0.3068 0.3121 0.3097 0.0316 -0.0304 0.0574 106 ALA A O 757 C CB . ALA A 106 ? 0.3002 0.3113 0.2968 0.0449 -0.0247 0.0692 106 ALA A CB 758 N N . SER A 107 ? 0.3197 0.3156 0.3020 0.0367 -0.0261 0.0585 107 SER A N 759 C CA . SER A 107 ? 0.3233 0.3118 0.2988 0.0311 -0.0268 0.0523 107 SER A CA 760 C C . SER A 107 ? 0.3115 0.3074 0.2962 0.0265 -0.0302 0.0508 107 SER A C 761 O O . SER A 107 ? 0.3142 0.3101 0.3011 0.0216 -0.0318 0.0466 107 SER A O 762 C CB . SER A 107 ? 0.3340 0.3098 0.2903 0.0319 -0.0240 0.0503 107 SER A CB 763 O OG . SER A 107 ? 0.3500 0.3166 0.2961 0.0356 -0.0209 0.0502 107 SER A OG 764 N N . LEU A 108 ? 0.3152 0.3177 0.3049 0.0283 -0.0311 0.0543 108 LEU A N 765 C CA . LEU A 108 ? 0.3085 0.3180 0.3059 0.0249 -0.0341 0.0532 108 LEU A CA 766 C C . LEU A 108 ? 0.2946 0.3106 0.3061 0.0237 -0.0366 0.0534 108 LEU A C 767 O O . LEU A 108 ? 0.2942 0.3127 0.3095 0.0203 -0.0385 0.0500 108 LEU A O 768 C CB . LEU A 108 ? 0.3163 0.3310 0.3155 0.0276 -0.0344 0.0573 108 LEU A CB 769 C CG . LEU A 108 ? 0.3148 0.3374 0.3219 0.0251 -0.0374 0.0568 108 LEU A CG 770 C CD1 . LEU A 108 ? 0.3353 0.3563 0.3357 0.0200 -0.0381 0.0516 108 LEU A CD1 771 C CD2 . LEU A 108 ? 0.3114 0.3384 0.3196 0.0282 -0.0374 0.0613 108 LEU A CD2 772 N N . ARG A 109 ? 0.2773 0.2957 0.2951 0.0266 -0.0365 0.0573 109 ARG A N 773 C CA . ARG A 109 ? 0.2660 0.2878 0.2947 0.0252 -0.0387 0.0575 109 ARG A CA 774 C C . ARG A 109 ? 0.2703 0.2879 0.2973 0.0221 -0.0389 0.0522 109 ARG A C 775 O O . ARG A 109 ? 0.2571 0.2770 0.2901 0.0199 -0.0410 0.0500 109 ARG A O 776 C CB . ARG A 109 ? 0.2633 0.2880 0.2966 0.0276 -0.0384 0.0627 109 ARG A CB 777 C CG . ARG A 109 ? 0.2719 0.2985 0.3144 0.0255 -0.0408 0.0631 109 ARG A CG 778 C CD . ARG A 109 ? 0.2681 0.2992 0.3146 0.0269 -0.0407 0.0691 109 ARG A CD 779 N NE . ARG A 109 ? 0.2589 0.2905 0.3125 0.0240 -0.0431 0.0695 109 ARG A NE 780 C CZ . ARG A 109 ? 0.2590 0.2879 0.3121 0.0228 -0.0429 0.0673 109 ARG A CZ 781 N NH1 . ARG A 109 ? 0.2474 0.2728 0.2933 0.0244 -0.0402 0.0645 109 ARG A NH1 782 N NH2 . ARG A 109 ? 0.2446 0.2735 0.3034 0.0198 -0.0453 0.0680 109 ARG A NH2 783 N N . SER A 110 ? 0.2758 0.2866 0.2935 0.0223 -0.0364 0.0504 110 SER A N 784 C CA . SER A 110 ? 0.2790 0.2852 0.2940 0.0193 -0.0362 0.0456 110 SER A CA 785 C C . SER A 110 ? 0.2864 0.2930 0.2988 0.0149 -0.0373 0.0409 110 SER A C 786 O O . SER A 110 ? 0.2800 0.2886 0.2971 0.0124 -0.0387 0.0380 110 SER A O 787 C CB . SER A 110 ? 0.2740 0.2715 0.2771 0.0209 -0.0330 0.0448 110 SER A CB 788 O OG . SER A 110 ? 0.2854 0.2779 0.2851 0.0174 -0.0328 0.0400 110 SER A OG 789 N N . LEU A 111 ? 0.2990 0.3043 0.3035 0.0140 -0.0366 0.0404 111 LEU A N 790 C CA . LEU A 111 ? 0.3124 0.3195 0.3135 0.0089 -0.0377 0.0363 111 LEU A CA 791 C C . LEU A 111 ? 0.2843 0.3024 0.2971 0.0086 -0.0405 0.0368 111 LEU A C 792 O O . LEU A 111 ? 0.2873 0.3093 0.3018 0.0053 -0.0416 0.0336 111 LEU A O 793 C CB . LEU A 111 ? 0.3309 0.3327 0.3185 0.0069 -0.0363 0.0355 111 LEU A CB 794 C CG . LEU A 111 ? 0.3397 0.3460 0.3281 0.0089 -0.0369 0.0386 111 LEU A CG 795 C CD1 . LEU A 111 ? 0.3447 0.3615 0.3389 0.0054 -0.0395 0.0373 111 LEU A CD1 796 C CD2 . LEU A 111 ? 0.3744 0.3704 0.3466 0.0091 -0.0345 0.0387 111 LEU A CD2 797 N N . VAL A 112 ? 0.2739 0.2967 0.2942 0.0124 -0.0415 0.0409 112 VAL A N 798 C CA . VAL A 112 ? 0.2713 0.3027 0.3020 0.0134 -0.0441 0.0418 112 VAL A CA 799 C C . VAL A 112 ? 0.2558 0.2868 0.2936 0.0139 -0.0452 0.0408 112 VAL A C 800 O O . VAL A 112 ? 0.2430 0.2788 0.2846 0.0132 -0.0466 0.0387 112 VAL A O 801 C CB . VAL A 112 ? 0.2702 0.3050 0.3056 0.0171 -0.0449 0.0467 112 VAL A CB 802 C CG1 . VAL A 112 ? 0.2663 0.3079 0.3105 0.0186 -0.0474 0.0474 112 VAL A CG1 803 C CG2 . VAL A 112 ? 0.2763 0.3120 0.3044 0.0166 -0.0440 0.0474 112 VAL A CG2 804 N N . ALA A 113 ? 0.2560 0.2815 0.2945 0.0150 -0.0443 0.0422 113 ALA A N 805 C CA . ALA A 113 ? 0.2481 0.2719 0.2921 0.0150 -0.0454 0.0413 113 ALA A CA 806 C C . ALA A 113 ? 0.2554 0.2787 0.2969 0.0122 -0.0451 0.0363 113 ALA A C 807 O O . ALA A 113 ? 0.2521 0.2775 0.2987 0.0124 -0.0465 0.0349 113 ALA A O 808 C CB . ALA A 113 ? 0.2404 0.2595 0.2844 0.0160 -0.0444 0.0438 113 ALA A CB 809 N N . SER A 114 ? 0.2580 0.2777 0.2907 0.0095 -0.0432 0.0338 114 SER A N 810 C CA . SER A 114 ? 0.2783 0.2970 0.3072 0.0059 -0.0427 0.0293 114 SER A CA 811 C C . SER A 114 ? 0.2822 0.3098 0.3126 0.0037 -0.0441 0.0272 114 SER A C 812 O O . SER A 114 ? 0.2925 0.3234 0.3249 0.0020 -0.0446 0.0243 114 SER A O 813 C CB . SER A 114 ? 0.2914 0.3018 0.3081 0.0034 -0.0402 0.0276 114 SER A CB 814 O OG . SER A 114 ? 0.3274 0.3365 0.3400 -0.0007 -0.0399 0.0233 114 SER A OG 815 N N . SER A 115 ? 0.2706 0.3031 0.3002 0.0040 -0.0446 0.0290 115 SER A N 816 C CA . SER A 115 ? 0.2835 0.3269 0.3151 0.0025 -0.0460 0.0280 115 SER A CA 817 C C . SER A 115 ? 0.2663 0.3162 0.3080 0.0068 -0.0478 0.0289 115 SER A C 818 O O . SER A 115 ? 0.2867 0.3451 0.3306 0.0061 -0.0485 0.0270 115 SER A O 819 C CB . SER A 115 ? 0.2941 0.3407 0.3220 0.0020 -0.0462 0.0299 115 SER A CB 820 O OG . SER A 115 ? 0.3198 0.3789 0.3514 0.0018 -0.0478 0.0301 115 SER A OG 821 N N . GLY A 116 ? 0.2522 0.2980 0.2991 0.0111 -0.0484 0.0320 116 GLY A N 822 C CA . GLY A 116 ? 0.2509 0.2982 0.3047 0.0151 -0.0499 0.0326 116 GLY A CA 823 C C . GLY A 116 ? 0.2544 0.3102 0.3118 0.0188 -0.0512 0.0345 116 GLY A C 824 O O . GLY A 116 ? 0.2591 0.3170 0.3200 0.0225 -0.0522 0.0343 116 GLY A O 825 N N . THR A 117 ? 0.2586 0.3186 0.3144 0.0185 -0.0512 0.0365 117 THR A N 826 C CA . THR A 117 ? 0.2615 0.3307 0.3202 0.0222 -0.0524 0.0385 117 THR A CA 827 C C . THR A 117 ? 0.2655 0.3348 0.3232 0.0229 -0.0525 0.0419 117 THR A C 828 O O . THR A 117 ? 0.2778 0.3445 0.3307 0.0193 -0.0515 0.0417 117 THR A O 829 C CB . THR A 117 ? 0.2684 0.3509 0.3258 0.0199 -0.0525 0.0361 117 THR A CB 830 O OG1 . THR A 117 ? 0.2643 0.3569 0.3247 0.0244 -0.0536 0.0386 117 THR A OG1 831 C CG2 . THR A 117 ? 0.2715 0.3555 0.3219 0.0130 -0.0516 0.0343 117 THR A CG2 832 N N . LEU A 118 ? 0.2654 0.3370 0.3268 0.0279 -0.0537 0.0450 118 LEU A N 833 C CA . LEU A 118 ? 0.2769 0.3504 0.3379 0.0292 -0.0540 0.0485 118 LEU A CA 834 C C . LEU A 118 ? 0.2861 0.3729 0.3476 0.0309 -0.0547 0.0488 118 LEU A C 835 O O . LEU A 118 ? 0.3079 0.3973 0.3700 0.0335 -0.0553 0.0520 118 LEU A O 836 C CB . LEU A 118 ? 0.2821 0.3477 0.3461 0.0333 -0.0548 0.0524 118 LEU A CB 837 C CG . LEU A 118 ? 0.2860 0.3415 0.3495 0.0311 -0.0542 0.0537 118 LEU A CG 838 C CD1 . LEU A 118 ? 0.2990 0.3473 0.3651 0.0340 -0.0555 0.0574 118 LEU A CD1 839 C CD2 . LEU A 118 ? 0.2946 0.3511 0.3548 0.0289 -0.0530 0.0552 118 LEU A CD2 840 N N . GLU A 119 ? 0.3008 0.3969 0.3619 0.0292 -0.0548 0.0458 119 GLU A N 841 C CA . GLU A 119 ? 0.3051 0.4167 0.3669 0.0305 -0.0556 0.0465 119 GLU A CA 842 C C . GLU A 119 ? 0.3099 0.4253 0.3677 0.0266 -0.0556 0.0476 119 GLU A C 843 O O . GLU A 119 ? 0.2901 0.4014 0.3422 0.0202 -0.0547 0.0455 119 GLU A O 844 C CB . GLU A 119 ? 0.3333 0.4561 0.3947 0.0275 -0.0555 0.0433 119 GLU A CB 845 C CG . GLU A 119 ? 0.3667 0.4894 0.4316 0.0324 -0.0555 0.0423 119 GLU A CG 846 C CD . GLU A 119 ? 0.4037 0.5346 0.4674 0.0276 -0.0550 0.0387 119 GLU A CD 847 O OE1 . GLU A 119 ? 0.3828 0.5043 0.4437 0.0222 -0.0542 0.0359 119 GLU A OE1 848 O OE2 . GLU A 119 ? 0.3993 0.5471 0.4646 0.0291 -0.0555 0.0391 119 GLU A OE2 849 N N . PHE A 120 ? 0.2983 0.4211 0.3579 0.0306 -0.0565 0.0508 120 PHE A N 850 C CA . PHE A 120 ? 0.3071 0.4324 0.3631 0.0281 -0.0566 0.0524 120 PHE A CA 851 C C . PHE A 120 ? 0.3298 0.4730 0.3868 0.0293 -0.0578 0.0536 120 PHE A C 852 O O . PHE A 120 ? 0.3156 0.4654 0.3774 0.0361 -0.0584 0.0556 120 PHE A O 853 C CB . PHE A 120 ? 0.3136 0.4290 0.3709 0.0323 -0.0565 0.0562 120 PHE A CB 854 C CG . PHE A 120 ? 0.3229 0.4396 0.3760 0.0302 -0.0563 0.0580 120 PHE A CG 855 C CD1 . PHE A 120 ? 0.3319 0.4392 0.3790 0.0257 -0.0551 0.0570 120 PHE A CD1 856 C CD2 . PHE A 120 ? 0.3227 0.4497 0.3771 0.0332 -0.0574 0.0608 120 PHE A CD2 857 C CE1 . PHE A 120 ? 0.3391 0.4466 0.3810 0.0241 -0.0548 0.0585 120 PHE A CE1 858 C CE2 . PHE A 120 ? 0.3336 0.4614 0.3836 0.0311 -0.0573 0.0623 120 PHE A CE2 859 C CZ . PHE A 120 ? 0.3437 0.4614 0.3871 0.0265 -0.0560 0.0611 120 PHE A CZ 860 N N . ASN A 121 ? 0.3427 0.4933 0.3943 0.0226 -0.0581 0.0525 121 ASN A N 861 C CA . ASN A 121 ? 0.3758 0.5453 0.4278 0.0222 -0.0595 0.0538 121 ASN A CA 862 C C . ASN A 121 ? 0.3884 0.5573 0.4366 0.0212 -0.0599 0.0562 121 ASN A C 863 O O . ASN A 121 ? 0.3860 0.5463 0.4267 0.0149 -0.0593 0.0547 121 ASN A O 864 C CB . ASN A 121 ? 0.4075 0.5875 0.4553 0.0137 -0.0599 0.0506 121 ASN A CB 865 C CG . ASN A 121 ? 0.4451 0.6344 0.4982 0.0163 -0.0599 0.0494 121 ASN A CG 866 O OD1 . ASN A 121 ? 0.4778 0.6667 0.5371 0.0252 -0.0597 0.0511 121 ASN A OD1 867 N ND2 . ASN A 121 ? 0.5015 0.6989 0.5510 0.0083 -0.0602 0.0466 121 ASN A ND2 868 N N . ASN A 122 ? 0.3962 0.5733 0.4489 0.0280 -0.0607 0.0599 122 ASN A N 869 C CA . ASN A 122 ? 0.4243 0.6023 0.4740 0.0279 -0.0611 0.0626 122 ASN A CA 870 C C . ASN A 122 ? 0.4088 0.5996 0.4523 0.0198 -0.0622 0.0612 122 ASN A C 871 O O . ASN A 122 ? 0.4076 0.6138 0.4522 0.0171 -0.0632 0.0601 122 ASN A O 872 C CB . ASN A 122 ? 0.4490 0.6329 0.5046 0.0375 -0.0617 0.0670 122 ASN A CB 873 C CG . ASN A 122 ? 0.4829 0.6499 0.5414 0.0435 -0.0609 0.0689 122 ASN A CG 874 O OD1 . ASN A 122 ? 0.5237 0.6802 0.5799 0.0427 -0.0603 0.0704 122 ASN A OD1 875 N ND2 . ASN A 122 ? 0.5210 0.6853 0.5837 0.0492 -0.0607 0.0690 122 ASN A ND2 876 N N . GLU A 123 ? 0.4171 0.6014 0.4533 0.0154 -0.0621 0.0614 123 GLU A N 877 C CA . GLU A 123 ? 0.4184 0.6134 0.4471 0.0075 -0.0635 0.0607 123 GLU A CA 878 C C . GLU A 123 ? 0.4355 0.6321 0.4620 0.0098 -0.0640 0.0640 123 GLU A C 879 O O . GLU A 123 ? 0.4277 0.6116 0.4552 0.0149 -0.0629 0.0660 123 GLU A O 880 C CB . GLU A 123 ? 0.4110 0.5939 0.4279 -0.0025 -0.0628 0.0566 123 GLU A CB 881 C CG . GLU A 123 ? 0.4063 0.5894 0.4235 -0.0068 -0.0625 0.0531 123 GLU A CG 882 C CD . GLU A 123 ? 0.4017 0.5694 0.4059 -0.0160 -0.0615 0.0492 123 GLU A CD 883 O OE1 . GLU A 123 ? 0.4122 0.5614 0.4108 -0.0145 -0.0598 0.0490 123 GLU A OE1 884 O OE2 . GLU A 123 ? 0.3756 0.5496 0.3747 -0.0244 -0.0624 0.0466 123 GLU A OE2 885 N N . SER A 124 ? 0.4614 0.6744 0.4847 0.0052 -0.0659 0.0647 124 SER A N 886 C CA . SER A 124 ? 0.4802 0.6976 0.5013 0.0068 -0.0667 0.0678 124 SER A CA 887 C C . SER A 124 ? 0.4922 0.6979 0.4994 -0.0018 -0.0666 0.0657 124 SER A C 888 O O . SER A 124 ? 0.4810 0.6949 0.4799 -0.0112 -0.0681 0.0640 124 SER A O 889 C CB . SER A 124 ? 0.5025 0.7456 0.5275 0.0071 -0.0690 0.0702 124 SER A CB 890 O OG . SER A 124 ? 0.5199 0.7728 0.5562 0.0169 -0.0688 0.0725 124 SER A OG 891 N N . PHE A 125 ? 0.4878 0.6742 0.4918 0.0011 -0.0646 0.0659 125 PHE A N 892 C CA . PHE A 125 ? 0.5129 0.6857 0.5026 -0.0049 -0.0639 0.0643 125 PHE A CA 893 C C . PHE A 125 ? 0.5337 0.7149 0.5212 -0.0039 -0.0652 0.0674 125 PHE A C 894 O O . PHE A 125 ? 0.5519 0.7414 0.5494 0.0041 -0.0655 0.0712 125 PHE A O 895 C CB . PHE A 125 ? 0.5010 0.6527 0.4886 -0.0004 -0.0611 0.0643 125 PHE A CB 896 C CG . PHE A 125 ? 0.4803 0.6209 0.4655 -0.0034 -0.0597 0.0606 125 PHE A CG 897 C CD1 . PHE A 125 ? 0.4666 0.6096 0.4636 0.0011 -0.0594 0.0607 125 PHE A CD1 898 C CD2 . PHE A 125 ? 0.4965 0.6239 0.4662 -0.0112 -0.0588 0.0571 125 PHE A CD2 899 C CE1 . PHE A 125 ? 0.4635 0.5970 0.4582 -0.0017 -0.0582 0.0574 125 PHE A CE1 900 C CE2 . PHE A 125 ? 0.5066 0.6237 0.4735 -0.0138 -0.0575 0.0538 125 PHE A CE2 901 C CZ . PHE A 125 ? 0.4761 0.5970 0.4562 -0.0091 -0.0572 0.0540 125 PHE A CZ 902 N N . ASN A 126 ? 0.5759 0.7538 0.5492 -0.0123 -0.0659 0.0657 126 ASN A N 903 C CA . ASN A 126 ? 0.6207 0.8055 0.5902 -0.0120 -0.0672 0.0684 126 ASN A CA 904 C C . ASN A 126 ? 0.5823 0.7495 0.5466 -0.0068 -0.0649 0.0699 126 ASN A C 905 O O . ASN A 126 ? 0.5865 0.7387 0.5353 -0.0120 -0.0639 0.0677 126 ASN A O 906 C CB . ASN A 126 ? 0.7102 0.9005 0.6658 -0.0244 -0.0694 0.0659 126 ASN A CB 907 C CG . ASN A 126 ? 0.8042 0.9990 0.7531 -0.0254 -0.0707 0.0683 126 ASN A CG 908 O OD1 . ASN A 126 ? 0.7845 0.9827 0.7414 -0.0164 -0.0702 0.0721 126 ASN A OD1 909 N ND2 . ASN A 126 ? 0.9526 1.1468 0.8857 -0.0370 -0.0724 0.0659 126 ASN A ND2 910 N N . TRP A 127 ? 0.5394 0.7078 0.5155 0.0033 -0.0640 0.0739 127 TRP A N 911 C CA . TRP A 127 ? 0.5441 0.6990 0.5167 0.0087 -0.0619 0.0763 127 TRP A CA 912 C C . TRP A 127 ? 0.5690 0.7326 0.5402 0.0106 -0.0631 0.0796 127 TRP A C 913 O O . TRP A 127 ? 0.5764 0.7388 0.5539 0.0185 -0.0622 0.0837 127 TRP A O 914 C CB . TRP A 127 ? 0.5281 0.6777 0.5128 0.0177 -0.0602 0.0789 127 TRP A CB 915 C CG . TRP A 127 ? 0.5190 0.6605 0.5060 0.0164 -0.0590 0.0759 127 TRP A CG 916 C CD1 . TRP A 127 ? 0.5069 0.6528 0.5063 0.0203 -0.0592 0.0763 127 TRP A CD1 917 C CD2 . TRP A 127 ? 0.5358 0.6621 0.5112 0.0112 -0.0573 0.0720 127 TRP A CD2 918 N NE1 . TRP A 127 ? 0.5098 0.6459 0.5072 0.0176 -0.0580 0.0730 127 TRP A NE1 919 C CE2 . TRP A 127 ? 0.5236 0.6478 0.5070 0.0122 -0.0567 0.0703 127 TRP A CE2 920 C CE3 . TRP A 127 ? 0.5368 0.6502 0.4953 0.0063 -0.0561 0.0697 127 TRP A CE3 921 C CZ2 . TRP A 127 ? 0.5439 0.6550 0.5195 0.0085 -0.0551 0.0667 127 TRP A CZ2 922 C CZ3 . TRP A 127 ? 0.5594 0.6583 0.5090 0.0029 -0.0543 0.0661 127 TRP A CZ3 923 C CH2 . TRP A 127 ? 0.5574 0.6557 0.5160 0.0040 -0.0538 0.0647 127 TRP A CH2 924 N N . THR A 128 ? 0.5938 0.7662 0.5564 0.0030 -0.0653 0.0782 128 THR A N 925 C CA . THR A 128 ? 0.6203 0.8003 0.5796 0.0038 -0.0665 0.0811 128 THR A CA 926 C C . THR A 128 ? 0.6110 0.7731 0.5606 0.0068 -0.0641 0.0821 128 THR A C 927 O O . THR A 128 ? 0.6171 0.7627 0.5526 0.0022 -0.0626 0.0789 128 THR A O 928 C CB . THR A 128 ? 0.6556 0.8460 0.6041 -0.0069 -0.0694 0.0789 128 THR A CB 929 O OG1 . THR A 128 ? 0.6656 0.8753 0.6235 -0.0093 -0.0715 0.0785 128 THR A OG1 930 C CG2 . THR A 128 ? 0.6524 0.8511 0.5972 -0.0061 -0.0708 0.0820 128 THR A CG2 931 N N . GLY A 129 ? 0.6290 0.7941 0.5858 0.0151 -0.0635 0.0867 129 GLY A N 932 C CA . GLY A 129 ? 0.6277 0.7803 0.5755 0.0182 -0.0615 0.0886 129 GLY A CA 933 C C . GLY A 129 ? 0.6326 0.7744 0.5869 0.0266 -0.0586 0.0913 129 GLY A C 934 O O . GLY A 129 ? 0.6138 0.7468 0.5616 0.0302 -0.0566 0.0935 129 GLY A O 935 N N . VAL A 130 ? 0.5946 0.7375 0.5610 0.0295 -0.0582 0.0914 130 VAL A N 936 C CA . VAL A 130 ? 0.5579 0.6928 0.5318 0.0364 -0.0559 0.0944 130 VAL A CA 937 C C . VAL A 130 ? 0.5198 0.6647 0.5100 0.0417 -0.0571 0.0975 130 VAL A C 938 O O . VAL A 130 ? 0.5102 0.6673 0.5056 0.0403 -0.0594 0.0967 130 VAL A O 939 C CB . VAL A 130 ? 0.5617 0.6833 0.5315 0.0345 -0.0538 0.0911 130 VAL A CB 940 C CG1 . VAL A 130 ? 0.5700 0.6783 0.5213 0.0306 -0.0521 0.0883 130 VAL A CG1 941 C CG2 . VAL A 130 ? 0.5480 0.6749 0.5231 0.0301 -0.0554 0.0874 130 VAL A CG2 942 N N . THR A 131 ? 0.5100 0.6497 0.5069 0.0476 -0.0556 0.1014 131 THR A N 943 C CA . THR A 131 ? 0.5076 0.6516 0.5176 0.0524 -0.0564 0.1043 131 THR A CA 944 C C . THR A 131 ? 0.5077 0.6455 0.5217 0.0508 -0.0558 0.1014 131 THR A C 945 O O . THR A 131 ? 0.4721 0.5994 0.4819 0.0496 -0.0538 0.1003 131 THR A O 946 C CB . THR A 131 ? 0.5230 0.6635 0.5374 0.0582 -0.0553 0.1101 131 THR A CB 947 O OG1 . THR A 131 ? 0.5388 0.6832 0.5478 0.0594 -0.0553 0.1126 131 THR A OG1 948 C CG2 . THR A 131 ? 0.5243 0.6682 0.5497 0.0626 -0.0565 0.1133 131 THR A CG2 949 N N . GLN A 132 ? 0.5002 0.6447 0.5217 0.0514 -0.0575 0.1004 132 GLN A N 950 C CA . GLN A 132 ? 0.4926 0.6321 0.5185 0.0504 -0.0571 0.0978 132 GLN A CA 951 C C . GLN A 132 ? 0.4960 0.6307 0.5305 0.0555 -0.0569 0.1016 132 GLN A C 952 O O . GLN A 132 ? 0.4726 0.6085 0.5097 0.0598 -0.0572 0.1062 132 GLN A O 953 C CB . GLN A 132 ? 0.5006 0.6503 0.5289 0.0481 -0.0590 0.0945 132 GLN A CB 954 C CG . GLN A 132 ? 0.5053 0.6608 0.5247 0.0414 -0.0597 0.0908 132 GLN A CG 955 C CD . GLN A 132 ? 0.5169 0.6829 0.5389 0.0383 -0.0613 0.0876 132 GLN A CD 956 O OE1 . GLN A 132 ? 0.5058 0.6684 0.5323 0.0386 -0.0609 0.0857 132 GLN A OE1 957 N NE2 . GLN A 132 ? 0.5138 0.6935 0.5326 0.0350 -0.0630 0.0871 132 GLN A NE2 958 N N . ASN A 133 ? 0.4746 0.6030 0.5124 0.0545 -0.0565 0.0996 133 ASN A N 959 C CA . ASN A 133 ? 0.4682 0.5916 0.5132 0.0581 -0.0568 0.1025 133 ASN A CA 960 C C . ASN A 133 ? 0.4609 0.5777 0.5069 0.0602 -0.0558 0.1075 133 ASN A C 961 O O . ASN A 133 ? 0.4427 0.5578 0.4930 0.0635 -0.0566 0.1115 133 ASN A O 962 C CB . ASN A 133 ? 0.5065 0.6369 0.5559 0.0625 -0.0586 0.1039 133 ASN A CB 963 C CG . ASN A 133 ? 0.5577 0.6960 0.6076 0.0612 -0.0596 0.0996 133 ASN A CG 964 O OD1 . ASN A 133 ? 0.5281 0.6655 0.5757 0.0563 -0.0591 0.0953 133 ASN A OD1 965 N ND2 . ASN A 133 ? 0.6290 0.7758 0.6816 0.0658 -0.0609 0.1011 133 ASN A ND2 966 N N . GLY A 134 ? 0.4549 0.5678 0.4964 0.0583 -0.0539 0.1077 134 GLY A N 967 C CA . GLY A 134 ? 0.4697 0.5784 0.5126 0.0600 -0.0527 0.1129 134 GLY A CA 968 C C . GLY A 134 ? 0.4841 0.5869 0.5331 0.0597 -0.0532 0.1144 134 GLY A C 969 O O . GLY A 134 ? 0.4680 0.5679 0.5184 0.0577 -0.0535 0.1106 134 GLY A O 970 N N . THR A 135 ? 0.4735 0.5745 0.5253 0.0612 -0.0534 0.1201 135 THR A N 971 C CA . THR A 135 ? 0.5003 0.5952 0.5566 0.0601 -0.0541 0.1224 135 THR A CA 972 C C . THR A 135 ? 0.5149 0.6089 0.5720 0.0590 -0.0529 0.1277 135 THR A C 973 O O . THR A 135 ? 0.5075 0.6058 0.5618 0.0603 -0.0513 0.1301 135 THR A O 974 C CB . THR A 135 ? 0.5178 0.6100 0.5764 0.0623 -0.0563 0.1245 135 THR A CB 975 O OG1 . THR A 135 ? 0.5128 0.6073 0.5707 0.0646 -0.0565 0.1297 135 THR A OG1 976 C CG2 . THR A 135 ? 0.5205 0.6160 0.5787 0.0643 -0.0573 0.1197 135 THR A CG2 977 N N . SER A 136 ? 0.5130 0.6020 0.5733 0.0564 -0.0535 0.1293 136 SER A N 978 C CA . SER A 136 ? 0.5090 0.5990 0.5707 0.0545 -0.0526 0.1347 136 SER A CA 979 C C . SER A 136 ? 0.5245 0.6085 0.5892 0.0515 -0.0548 0.1384 136 SER A C 980 O O . SER A 136 ? 0.5286 0.6057 0.5939 0.0505 -0.0564 0.1352 136 SER A O 981 C CB . SER A 136 ? 0.4994 0.5903 0.5604 0.0531 -0.0507 0.1323 136 SER A CB 982 O OG . SER A 136 ? 0.4982 0.5926 0.5609 0.0517 -0.0496 0.1379 136 SER A OG 983 N N . SER A 137 ? 0.5106 0.5969 0.5763 0.0499 -0.0548 0.1452 137 SER A N 984 C CA . SER A 137 ? 0.5210 0.6008 0.5878 0.0455 -0.0570 0.1494 137 SER A CA 985 C C . SER A 137 ? 0.5431 0.6215 0.6121 0.0411 -0.0571 0.1484 137 SER A C 986 O O . SER A 137 ? 0.5407 0.6118 0.6096 0.0366 -0.0593 0.1504 137 SER A O 987 C CB . SER A 137 ? 0.5326 0.6168 0.5997 0.0440 -0.0571 0.1574 137 SER A CB 988 O OG . SER A 137 ? 0.5309 0.6252 0.5998 0.0432 -0.0549 0.1604 137 SER A OG 989 N N . ALA A 138 ? 0.5272 0.6117 0.5968 0.0423 -0.0548 0.1456 138 ALA A N 990 C CA . ALA A 138 ? 0.5315 0.6153 0.6028 0.0390 -0.0546 0.1439 138 ALA A CA 991 C C . ALA A 138 ? 0.5293 0.6046 0.6002 0.0387 -0.0558 0.1369 138 ALA A C 992 O O . ALA A 138 ? 0.5505 0.6237 0.6227 0.0358 -0.0560 0.1352 138 ALA A O 993 C CB . ALA A 138 ? 0.4965 0.5890 0.5672 0.0415 -0.0514 0.1436 138 ALA A CB 994 N N . CYS A 139 ? 0.5378 0.6092 0.6069 0.0420 -0.0565 0.1332 139 CYS A N 995 C CA . CYS A 139 ? 0.5443 0.6094 0.6129 0.0424 -0.0574 0.1269 139 CYS A CA 996 C C . CYS A 139 ? 0.5608 0.6193 0.6278 0.0445 -0.0595 0.1270 139 CYS A C 997 O O . CYS A 139 ? 0.5967 0.6575 0.6625 0.0485 -0.0593 0.1241 139 CYS A O 998 C CB . CYS A 139 ? 0.5437 0.6137 0.6110 0.0451 -0.0555 0.1213 139 CYS A CB 999 S SG . CYS A 139 ? 0.5463 0.6114 0.6134 0.0450 -0.0562 0.1136 139 CYS A SG 1000 N N . LYS A 140 ? 0.5617 0.6117 0.6275 0.0416 -0.0615 0.1306 140 LYS A N 1001 C CA . LYS A 140 ? 0.5960 0.6372 0.6581 0.0442 -0.0633 0.1313 140 LYS A CA 1002 C C . LYS A 140 ? 0.5831 0.6165 0.6432 0.0462 -0.0641 0.1258 140 LYS A C 1003 O O . LYS A 140 ? 0.5394 0.5688 0.6002 0.0429 -0.0645 0.1234 140 LYS A O 1004 C CB . LYS A 140 ? 0.6345 0.6675 0.6936 0.0399 -0.0651 0.1378 140 LYS A CB 1005 C CG . LYS A 140 ? 0.6769 0.7186 0.7377 0.0387 -0.0642 0.1438 140 LYS A CG 1006 C CD . LYS A 140 ? 0.7223 0.7556 0.7788 0.0359 -0.0662 0.1502 140 LYS A CD 1007 C CE . LYS A 140 ? 0.7464 0.7899 0.8049 0.0348 -0.0651 0.1564 140 LYS A CE 1008 N NZ . LYS A 140 ? 0.7593 0.8092 0.8179 0.0416 -0.0638 0.1556 140 LYS A NZ 1009 N N . ARG A 141 ? 0.5583 0.5913 0.6162 0.0521 -0.0643 0.1240 141 ARG A N 1010 C CA . ARG A 141 ? 0.5920 0.6185 0.6473 0.0556 -0.0650 0.1196 141 ARG A CA 1011 C C . ARG A 141 ? 0.6594 0.6760 0.7084 0.0600 -0.0663 0.1226 141 ARG A C 1012 O O . ARG A 141 ? 0.6556 0.6776 0.7041 0.0641 -0.0660 0.1249 141 ARG A O 1013 C CB . ARG A 141 ? 0.5695 0.6077 0.6277 0.0593 -0.0637 0.1143 141 ARG A CB 1014 C CG . ARG A 141 ? 0.5678 0.6029 0.6238 0.0639 -0.0641 0.1102 141 ARG A CG 1015 C CD . ARG A 141 ? 0.5652 0.6138 0.6244 0.0659 -0.0630 0.1054 141 ARG A CD 1016 N NE . ARG A 141 ? 0.5636 0.6140 0.6254 0.0613 -0.0622 0.1011 141 ARG A NE 1017 C CZ . ARG A 141 ? 0.5463 0.6034 0.6105 0.0572 -0.0609 0.1001 141 ARG A CZ 1018 N NH1 . ARG A 141 ? 0.5436 0.6065 0.6080 0.0569 -0.0602 0.1029 141 ARG A NH1 1019 N NH2 . ARG A 141 ? 0.5454 0.6024 0.6109 0.0538 -0.0602 0.0962 141 ARG A NH2 1020 N N . LYS A 142 ? 0.7203 0.7216 0.7634 0.0593 -0.0678 0.1228 142 LYS A N 1021 C CA . LYS A 142 ? 0.7820 0.7697 0.8163 0.0635 -0.0690 0.1259 142 LYS A CA 1022 C C . LYS A 142 ? 0.8020 0.7896 0.8349 0.0618 -0.0694 0.1322 142 LYS A C 1023 O O . LYS A 142 ? 0.8304 0.8170 0.8594 0.0678 -0.0693 0.1343 142 LYS A O 1024 C CB . LYS A 142 ? 0.8217 0.8130 0.8540 0.0733 -0.0683 0.1229 142 LYS A CB 1025 C CG . LYS A 142 ? 0.8475 0.8390 0.8803 0.0758 -0.0678 0.1171 142 LYS A CG 1026 C CD . LYS A 142 ? 0.8979 0.8692 0.9223 0.0742 -0.0692 0.1169 142 LYS A CD 1027 C CE . LYS A 142 ? 0.9144 0.8860 0.9388 0.0777 -0.0686 0.1113 142 LYS A CE 1028 N NZ . LYS A 142 ? 0.9341 0.8865 0.9510 0.0742 -0.0699 0.1107 142 LYS A NZ 1029 N N . SER A 143 ? 0.8058 0.7957 0.8419 0.0539 -0.0697 0.1354 143 SER A N 1030 C CA . SER A 143 ? 0.8096 0.8002 0.8448 0.0509 -0.0701 0.1420 143 SER A CA 1031 C C . SER A 143 ? 0.7764 0.7836 0.8174 0.0543 -0.0683 0.1430 143 SER A C 1032 O O . SER A 143 ? 0.7979 0.8086 0.8396 0.0515 -0.0683 0.1484 143 SER A O 1033 C CB . SER A 143 ? 0.8575 0.8304 0.8817 0.0526 -0.0717 0.1458 143 SER A CB 1034 O OG . SER A 143 ? 0.8989 0.8545 0.9157 0.0499 -0.0733 0.1444 143 SER A OG 1035 N N . ASN A 144 ? 0.7016 0.7191 0.7463 0.0599 -0.0670 0.1382 144 ASN A N 1036 C CA . ASN A 144 ? 0.6573 0.6896 0.7062 0.0626 -0.0655 0.1386 144 ASN A CA 1037 C C . ASN A 144 ? 0.6200 0.6639 0.6751 0.0590 -0.0639 0.1362 144 ASN A C 1038 O O . ASN A 144 ? 0.5613 0.6041 0.6182 0.0565 -0.0637 0.1323 144 ASN A O 1039 C CB . ASN A 144 ? 0.6697 0.7076 0.7179 0.0702 -0.0651 0.1350 144 ASN A CB 1040 C CG . ASN A 144 ? 0.7294 0.7571 0.7707 0.0759 -0.0662 0.1376 144 ASN A CG 1041 O OD1 . ASN A 144 ? 0.7980 0.8257 0.8371 0.0821 -0.0663 0.1347 144 ASN A OD1 1042 N ND2 . ASN A 144 ? 0.7177 0.7370 0.7548 0.0740 -0.0670 0.1435 144 ASN A ND2 1043 N N . ASN A 145 ? 0.5744 0.6286 0.6315 0.0593 -0.0626 0.1386 145 ASN A N 1044 C CA . ASN A 145 ? 0.5520 0.6165 0.6126 0.0577 -0.0607 0.1361 145 ASN A CA 1045 C C . ASN A 145 ? 0.5251 0.5937 0.5863 0.0601 -0.0602 0.1293 145 ASN A C 1046 O O . ASN A 145 ? 0.5131 0.5836 0.5729 0.0645 -0.0608 0.1277 145 ASN A O 1047 C CB . ASN A 145 ? 0.5581 0.6316 0.6188 0.0592 -0.0594 0.1395 145 ASN A CB 1048 C CG . ASN A 145 ? 0.5738 0.6463 0.6347 0.0560 -0.0595 0.1465 145 ASN A CG 1049 O OD1 . ASN A 145 ? 0.5758 0.6402 0.6363 0.0521 -0.0609 0.1492 145 ASN A OD1 1050 N ND2 . ASN A 145 ? 0.5650 0.6459 0.6260 0.0572 -0.0581 0.1498 145 ASN A ND2 1051 N N . SER A 146 ? 0.5140 0.5842 0.5768 0.0572 -0.0592 0.1256 146 SER A N 1052 C CA . SER A 146 ? 0.4796 0.5529 0.5424 0.0582 -0.0589 0.1192 146 SER A CA 1053 C C . SER A 146 ? 0.4652 0.5424 0.5283 0.0552 -0.0570 0.1163 146 SER A C 1054 O O . SER A 146 ? 0.4455 0.5252 0.5081 0.0541 -0.0556 0.1194 146 SER A O 1055 C CB . SER A 146 ? 0.4999 0.5650 0.5628 0.0585 -0.0603 0.1167 146 SER A CB 1056 O OG . SER A 146 ? 0.4844 0.5543 0.5471 0.0610 -0.0603 0.1116 146 SER A OG 1057 N N . PHE A 147 ? 0.4403 0.5176 0.5033 0.0543 -0.0568 0.1107 147 PHE A N 1058 C CA . PHE A 147 ? 0.4299 0.5091 0.4913 0.0518 -0.0550 0.1074 147 PHE A CA 1059 C C . PHE A 147 ? 0.3951 0.4714 0.4572 0.0502 -0.0554 0.1020 147 PHE A C 1060 O O . PHE A 147 ? 0.3759 0.4504 0.4395 0.0518 -0.0569 0.1006 147 PHE A O 1061 C CB . PHE A 147 ? 0.4182 0.5042 0.4755 0.0528 -0.0539 0.1057 147 PHE A CB 1062 C CG . PHE A 147 ? 0.4165 0.5023 0.4692 0.0509 -0.0516 0.1041 147 PHE A CG 1063 C CD1 . PHE A 147 ? 0.4164 0.5010 0.4686 0.0512 -0.0501 0.1083 147 PHE A CD1 1064 C CD2 . PHE A 147 ? 0.4188 0.5057 0.4665 0.0492 -0.0509 0.0988 147 PHE A CD2 1065 C CE1 . PHE A 147 ? 0.4258 0.5096 0.4724 0.0509 -0.0476 0.1071 147 PHE A CE1 1066 C CE2 . PHE A 147 ? 0.4237 0.5079 0.4648 0.0480 -0.0487 0.0973 147 PHE A CE2 1067 C CZ . PHE A 147 ? 0.4354 0.5177 0.4757 0.0495 -0.0469 0.1015 147 PHE A CZ 1068 N N . PHE A 148 ? 0.3848 0.4605 0.4451 0.0477 -0.0538 0.0992 148 PHE A N 1069 C CA . PHE A 148 ? 0.3809 0.4548 0.4411 0.0459 -0.0539 0.0937 148 PHE A CA 1070 C C . PHE A 148 ? 0.3942 0.4734 0.4540 0.0473 -0.0550 0.0904 148 PHE A C 1071 O O . PHE A 148 ? 0.3925 0.4781 0.4493 0.0477 -0.0547 0.0899 148 PHE A O 1072 C CB . PHE A 148 ? 0.3892 0.4626 0.4449 0.0436 -0.0518 0.0909 148 PHE A CB 1073 C CG . PHE A 148 ? 0.3912 0.4615 0.4471 0.0429 -0.0504 0.0941 148 PHE A CG 1074 C CD1 . PHE A 148 ? 0.4024 0.4683 0.4618 0.0412 -0.0509 0.0943 148 PHE A CD1 1075 C CD2 . PHE A 148 ? 0.4134 0.4856 0.4654 0.0442 -0.0485 0.0971 148 PHE A CD2 1076 C CE1 . PHE A 148 ? 0.4184 0.4837 0.4782 0.0405 -0.0496 0.0977 148 PHE A CE1 1077 C CE2 . PHE A 148 ? 0.4168 0.4882 0.4689 0.0444 -0.0470 0.1005 148 PHE A CE2 1078 C CZ . PHE A 148 ? 0.4287 0.4975 0.4851 0.0424 -0.0476 0.1010 148 PHE A CZ 1079 N N . SER A 149 ? 0.3815 0.4588 0.4438 0.0481 -0.0562 0.0884 149 SER A N 1080 C CA . SER A 149 ? 0.3798 0.4640 0.4423 0.0504 -0.0572 0.0860 149 SER A CA 1081 C C . SER A 149 ? 0.3676 0.4595 0.4269 0.0474 -0.0564 0.0817 149 SER A C 1082 O O . SER A 149 ? 0.3472 0.4486 0.4058 0.0486 -0.0571 0.0811 149 SER A O 1083 C CB . SER A 149 ? 0.3984 0.4785 0.4631 0.0522 -0.0581 0.0842 149 SER A CB 1084 O OG . SER A 149 ? 0.3709 0.4480 0.4355 0.0485 -0.0574 0.0802 149 SER A OG 1085 N N . ARG A 150 ? 0.3370 0.4248 0.3935 0.0432 -0.0551 0.0789 150 ARG A N 1086 C CA . ARG A 150 ? 0.3436 0.4364 0.3955 0.0394 -0.0546 0.0744 150 ARG A CA 1087 C C . ARG A 150 ? 0.3395 0.4327 0.3844 0.0371 -0.0534 0.0748 150 ARG A C 1088 O O . ARG A 150 ? 0.3329 0.4284 0.3716 0.0330 -0.0531 0.0713 150 ARG A O 1089 C CB . ARG A 150 ? 0.3323 0.4196 0.3834 0.0361 -0.0538 0.0705 150 ARG A CB 1090 C CG . ARG A 150 ? 0.3333 0.4190 0.3901 0.0383 -0.0549 0.0698 150 ARG A CG 1091 C CD . ARG A 150 ? 0.3342 0.4299 0.3933 0.0410 -0.0563 0.0691 150 ARG A CD 1092 N NE . ARG A 150 ? 0.3237 0.4182 0.3859 0.0428 -0.0568 0.0672 150 ARG A NE 1093 C CZ . ARG A 150 ? 0.3175 0.4198 0.3818 0.0467 -0.0578 0.0670 150 ARG A CZ 1094 N NH1 . ARG A 150 ? 0.3090 0.4220 0.3732 0.0493 -0.0584 0.0689 150 ARG A NH1 1095 N NH2 . ARG A 150 ? 0.3058 0.4059 0.3718 0.0487 -0.0580 0.0651 150 ARG A NH2 1096 N N . LEU A 151 ? 0.3407 0.4313 0.3857 0.0397 -0.0529 0.0791 151 LEU A N 1097 C CA . LEU A 151 ? 0.3480 0.4377 0.3857 0.0387 -0.0516 0.0800 151 LEU A CA 1098 C C . LEU A 151 ? 0.3624 0.4586 0.4012 0.0416 -0.0525 0.0837 151 LEU A C 1099 O O . LEU A 151 ? 0.3640 0.4627 0.4094 0.0452 -0.0538 0.0869 151 LEU A O 1100 C CB . LEU A 151 ? 0.3484 0.4299 0.3843 0.0394 -0.0495 0.0821 151 LEU A CB 1101 C CG . LEU A 151 ? 0.3455 0.4203 0.3787 0.0368 -0.0483 0.0785 151 LEU A CG 1102 C CD1 . LEU A 151 ? 0.3285 0.3978 0.3621 0.0388 -0.0465 0.0819 151 LEU A CD1 1103 C CD2 . LEU A 151 ? 0.3352 0.4074 0.3577 0.0328 -0.0472 0.0739 151 LEU A CD2 1104 N N . ASN A 152 ? 0.3818 0.4795 0.4129 0.0400 -0.0519 0.0832 152 ASN A N 1105 C CA . ASN A 152 ? 0.3752 0.4804 0.4057 0.0419 -0.0528 0.0859 152 ASN A CA 1106 C C . ASN A 152 ? 0.3951 0.4953 0.4186 0.0427 -0.0510 0.0884 152 ASN A C 1107 O O . ASN A 152 ? 0.4061 0.5022 0.4194 0.0397 -0.0498 0.0857 152 ASN A O 1108 C CB . ASN A 152 ? 0.3740 0.4879 0.4007 0.0382 -0.0542 0.0825 152 ASN A CB 1109 C CG . ASN A 152 ? 0.3831 0.5070 0.4104 0.0404 -0.0556 0.0852 152 ASN A CG 1110 O OD1 . ASN A 152 ? 0.3813 0.5040 0.4107 0.0445 -0.0553 0.0896 152 ASN A OD1 1111 N ND2 . ASN A 152 ? 0.3732 0.5078 0.3986 0.0373 -0.0572 0.0830 152 ASN A ND2 1112 N N . TRP A 153 ? 0.4100 0.5095 0.4381 0.0469 -0.0506 0.0935 153 TRP A N 1113 C CA . TRP A 153 ? 0.4351 0.5318 0.4579 0.0488 -0.0488 0.0968 153 TRP A CA 1114 C C . TRP A 153 ? 0.4559 0.5583 0.4739 0.0491 -0.0495 0.0975 153 TRP A C 1115 O O . TRP A 153 ? 0.4604 0.5690 0.4840 0.0519 -0.0509 0.1009 153 TRP A O 1116 C CB . TRP A 153 ? 0.4381 0.5341 0.4681 0.0524 -0.0485 0.1025 153 TRP A CB 1117 C CG . TRP A 153 ? 0.4438 0.5371 0.4692 0.0547 -0.0460 0.1062 153 TRP A CG 1118 C CD1 . TRP A 153 ? 0.4557 0.5460 0.4700 0.0550 -0.0440 0.1050 153 TRP A CD1 1119 C CD2 . TRP A 153 ? 0.4598 0.5532 0.4905 0.0571 -0.0452 0.1120 153 TRP A CD2 1120 N NE1 . TRP A 153 ? 0.4560 0.5450 0.4687 0.0584 -0.0417 0.1097 153 TRP A NE1 1121 C CE2 . TRP A 153 ? 0.4643 0.5564 0.4872 0.0595 -0.0424 0.1142 153 TRP A CE2 1122 C CE3 . TRP A 153 ? 0.4807 0.5749 0.5204 0.0572 -0.0466 0.1157 153 TRP A CE3 1123 C CZ2 . TRP A 153 ? 0.4823 0.5766 0.5079 0.0622 -0.0409 0.1202 153 TRP A CZ2 1124 C CZ3 . TRP A 153 ? 0.4866 0.5821 0.5285 0.0587 -0.0454 0.1216 153 TRP A CZ3 1125 C CH2 . TRP A 153 ? 0.4951 0.5918 0.5308 0.0612 -0.0426 0.1240 153 TRP A CH2 1126 N N . LEU A 154 ? 0.4651 0.5646 0.4716 0.0461 -0.0486 0.0943 154 LEU A N 1127 C CA . LEU A 154 ? 0.4690 0.5731 0.4689 0.0455 -0.0493 0.0947 154 LEU A CA 1128 C C . LEU A 154 ? 0.4859 0.5865 0.4813 0.0496 -0.0473 0.0991 154 LEU A C 1129 O O . LEU A 154 ? 0.4677 0.5602 0.4582 0.0512 -0.0447 0.0998 154 LEU A O 1130 C CB . LEU A 154 ? 0.4809 0.5819 0.4684 0.0394 -0.0494 0.0893 154 LEU A CB 1131 C CG . LEU A 154 ? 0.4869 0.5913 0.4770 0.0344 -0.0510 0.0848 154 LEU A CG 1132 C CD1 . LEU A 154 ? 0.5186 0.6187 0.4945 0.0273 -0.0511 0.0799 154 LEU A CD1 1133 C CD2 . LEU A 154 ? 0.4575 0.5758 0.4587 0.0355 -0.0537 0.0859 154 LEU A CD2 1134 N N . THR A 155 ? 0.4915 0.5991 0.4884 0.0517 -0.0484 0.1022 155 THR A N 1135 C CA . THR A 155 ? 0.5087 0.6143 0.5011 0.0557 -0.0466 0.1066 155 THR A CA 1136 C C . THR A 155 ? 0.5204 0.6304 0.5051 0.0544 -0.0477 0.1060 155 THR A C 1137 O O . THR A 155 ? 0.5083 0.6239 0.4921 0.0502 -0.0499 0.1027 155 THR A O 1138 C CB . THR A 155 ? 0.5037 0.6134 0.5076 0.0604 -0.0467 0.1128 155 THR A CB 1139 O OG1 . THR A 155 ? 0.4977 0.6156 0.5099 0.0607 -0.0494 0.1137 155 THR A OG1 1140 C CG2 . THR A 155 ? 0.4966 0.6018 0.5066 0.0610 -0.0456 0.1139 155 THR A CG2 1141 N N . HIS A 156 ? 0.5517 0.6600 0.5305 0.0577 -0.0461 0.1095 156 HIS A N 1142 C CA . HIS A 156 ? 0.5770 0.6883 0.5467 0.0563 -0.0470 0.1089 156 HIS A CA 1143 C C . HIS A 156 ? 0.5797 0.7039 0.5586 0.0563 -0.0501 0.1105 156 HIS A C 1144 O O . HIS A 156 ? 0.5691 0.6984 0.5606 0.0594 -0.0509 0.1135 156 HIS A O 1145 C CB . HIS A 156 ? 0.5929 0.6999 0.5552 0.0609 -0.0445 0.1129 156 HIS A CB 1146 C CG . HIS A 156 ? 0.5942 0.7086 0.5676 0.0664 -0.0446 0.1195 156 HIS A CG 1147 N ND1 . HIS A 156 ? 0.6006 0.7249 0.5808 0.0669 -0.0470 0.1216 156 HIS A ND1 1148 C CD2 . HIS A 156 ? 0.6098 0.7230 0.5877 0.0713 -0.0424 0.1247 156 HIS A CD2 1149 C CE1 . HIS A 156 ? 0.6072 0.7346 0.5952 0.0717 -0.0464 0.1277 156 HIS A CE1 1150 N NE2 . HIS A 156 ? 0.6160 0.7372 0.6027 0.0739 -0.0437 0.1297 156 HIS A NE2 1151 N N . LEU A 157 ? 0.6036 0.7327 0.5749 0.0529 -0.0517 0.1086 157 LEU A N 1152 C CA . LEU A 157 ? 0.5961 0.7391 0.5742 0.0537 -0.0545 0.1106 157 LEU A CA 1153 C C . LEU A 157 ? 0.6183 0.7625 0.5885 0.0553 -0.0542 0.1132 157 LEU A C 1154 O O . LEU A 157 ? 0.5948 0.7341 0.5510 0.0512 -0.0540 0.1104 157 LEU A O 1155 C CB . LEU A 157 ? 0.5857 0.7366 0.5624 0.0474 -0.0571 0.1061 157 LEU A CB 1156 C CG . LEU A 157 ? 0.5704 0.7380 0.5535 0.0483 -0.0599 0.1079 157 LEU A CG 1157 C CD1 . LEU A 157 ? 0.5772 0.7501 0.5750 0.0546 -0.0604 0.1113 157 LEU A CD1 1158 C CD2 . LEU A 157 ? 0.5565 0.7334 0.5352 0.0409 -0.0623 0.1037 157 LEU A CD2 1159 N N . LYS A 158 ? 0.6490 0.7984 0.6270 0.0612 -0.0542 0.1187 158 LYS A N 1160 C CA . LYS A 158 ? 0.6886 0.8398 0.6603 0.0637 -0.0538 0.1220 158 LYS A CA 1161 C C . LYS A 158 ? 0.7001 0.8388 0.6591 0.0642 -0.0507 0.1216 158 LYS A C 1162 O O . LYS A 158 ? 0.7057 0.8426 0.6528 0.0631 -0.0505 0.1212 158 LYS A O 1163 C CB . LYS A 158 ? 0.7169 0.8777 0.6827 0.0596 -0.0565 0.1200 158 LYS A CB 1164 C CG . LYS A 158 ? 0.7497 0.9241 0.7251 0.0582 -0.0595 0.1191 158 LYS A CG 1165 C CD . LYS A 158 ? 0.7812 0.9661 0.7665 0.0646 -0.0606 0.1245 158 LYS A CD 1166 C CE . LYS A 158 ? 0.7991 0.9994 0.7900 0.0636 -0.0636 0.1236 158 LYS A CE 1167 N NZ . LYS A 158 ? 0.8134 1.0138 0.8086 0.0605 -0.0640 0.1197 158 LYS A NZ 1168 N N . PHE A 159 ? 0.6608 0.7909 0.6216 0.0660 -0.0483 0.1219 159 PHE A N 1169 C CA . PHE A 159 ? 0.6656 0.7838 0.6143 0.0679 -0.0449 0.1219 159 PHE A CA 1170 C C . PHE A 159 ? 0.6529 0.7609 0.5841 0.0626 -0.0445 0.1159 159 PHE A C 1171 O O . PHE A 159 ? 0.6330 0.7304 0.5501 0.0646 -0.0418 0.1158 159 PHE A O 1172 C CB . PHE A 159 ? 0.7181 0.8378 0.6644 0.0735 -0.0433 0.1274 159 PHE A CB 1173 C CG . PHE A 159 ? 0.7413 0.8697 0.7030 0.0779 -0.0437 0.1335 159 PHE A CG 1174 C CD1 . PHE A 159 ? 0.7449 0.8712 0.7137 0.0811 -0.0416 0.1371 159 PHE A CD1 1175 C CD2 . PHE A 159 ? 0.7609 0.8994 0.7295 0.0785 -0.0463 0.1359 159 PHE A CD2 1176 C CE1 . PHE A 159 ? 0.7650 0.8979 0.7464 0.0839 -0.0423 0.1428 159 PHE A CE1 1177 C CE2 . PHE A 159 ? 0.7586 0.9027 0.7394 0.0822 -0.0467 0.1416 159 PHE A CE2 1178 C CZ . PHE A 159 ? 0.7647 0.9053 0.7516 0.0844 -0.0448 0.1450 159 PHE A CZ 1179 N N . LYS A 160 ? 0.6511 0.7619 0.5826 0.0559 -0.0470 0.1111 160 LYS A N 1180 C CA . LYS A 160 ? 0.6652 0.7655 0.5810 0.0493 -0.0469 0.1051 160 LYS A CA 1181 C C . LYS A 160 ? 0.6461 0.7440 0.5682 0.0465 -0.0471 0.1018 160 LYS A C 1182 O O . LYS A 160 ? 0.5989 0.7072 0.5368 0.0468 -0.0488 0.1027 160 LYS A O 1183 C CB . LYS A 160 ? 0.7252 0.8323 0.6342 0.0422 -0.0503 0.1023 160 LYS A CB 1184 C CG . LYS A 160 ? 0.7828 0.8869 0.6781 0.0427 -0.0500 0.1036 160 LYS A CG 1185 C CD . LYS A 160 ? 0.8281 0.9150 0.6995 0.0373 -0.0489 0.0989 160 LYS A CD 1186 C CE . LYS A 160 ? 0.8674 0.9469 0.7234 0.0401 -0.0475 0.1007 160 LYS A CE 1187 N NZ . LYS A 160 ? 0.8712 0.9642 0.7287 0.0371 -0.0508 0.1021 160 LYS A NZ 1188 N N . TYR A 161 ? 0.6549 0.7382 0.5634 0.0441 -0.0451 0.0981 161 TYR A N 1189 C CA . TYR A 161 ? 0.6486 0.7285 0.5596 0.0399 -0.0454 0.0940 161 TYR A CA 1190 C C . TYR A 161 ? 0.6732 0.7411 0.5636 0.0320 -0.0456 0.0884 161 TYR A C 1191 O O . TYR A 161 ? 0.6795 0.7307 0.5543 0.0334 -0.0427 0.0870 161 TYR A O 1192 C CB . TYR A 161 ? 0.6453 0.7179 0.5609 0.0458 -0.0422 0.0959 161 TYR A CB 1193 C CG . TYR A 161 ? 0.6305 0.7019 0.5530 0.0429 -0.0425 0.0927 161 TYR A CG 1194 C CD1 . TYR A 161 ? 0.6424 0.7036 0.5521 0.0365 -0.0425 0.0871 161 TYR A CD1 1195 C CD2 . TYR A 161 ? 0.6347 0.7141 0.5754 0.0463 -0.0429 0.0955 161 TYR A CD2 1196 C CE1 . TYR A 161 ? 0.6364 0.6965 0.5522 0.0340 -0.0427 0.0844 161 TYR A CE1 1197 C CE2 . TYR A 161 ? 0.6203 0.6981 0.5667 0.0438 -0.0432 0.0927 161 TYR A CE2 1198 C CZ . TYR A 161 ? 0.6330 0.7018 0.5675 0.0379 -0.0430 0.0871 161 TYR A CZ 1199 O OH . TYR A 161 ? 0.6029 0.6703 0.5432 0.0356 -0.0432 0.0844 161 TYR A OH 1200 N N . PRO A 162 ? 0.7019 0.7785 0.5914 0.0238 -0.0491 0.0856 162 PRO A N 1201 C CA . PRO A 162 ? 0.7285 0.7946 0.5981 0.0144 -0.0500 0.0803 162 PRO A CA 1202 C C . PRO A 162 ? 0.7472 0.8005 0.6113 0.0119 -0.0484 0.0765 162 PRO A C 1203 O O . PRO A 162 ? 0.7678 0.8269 0.6476 0.0147 -0.0481 0.0771 162 PRO A O 1204 C CB . PRO A 162 ? 0.7333 0.8175 0.6095 0.0066 -0.0544 0.0792 162 PRO A CB 1205 C CG . PRO A 162 ? 0.7275 0.8298 0.6236 0.0135 -0.0555 0.0842 162 PRO A CG 1206 C CD . PRO A 162 ? 0.7124 0.8095 0.6190 0.0231 -0.0525 0.0874 162 PRO A CD 1207 N N . ALA A 163 ? 0.7516 0.7865 0.5926 0.0066 -0.0473 0.0726 163 ALA A N 1208 C CA . ALA A 163 ? 0.7596 0.7804 0.5923 0.0035 -0.0457 0.0687 163 ALA A CA 1209 C C . ALA A 163 ? 0.7468 0.7807 0.5908 -0.0044 -0.0490 0.0660 163 ALA A C 1210 O O . ALA A 163 ? 0.7650 0.8081 0.6058 -0.0133 -0.0524 0.0643 163 ALA A O 1211 C CB . ALA A 163 ? 0.7938 0.7915 0.5968 -0.0017 -0.0444 0.0649 163 ALA A CB 1212 N N . LEU A 164 ? 0.6896 0.7259 0.5473 -0.0010 -0.0480 0.0660 164 LEU A N 1213 C CA . LEU A 164 ? 0.6684 0.7176 0.5378 -0.0072 -0.0507 0.0638 164 LEU A CA 1214 C C . LEU A 164 ? 0.6595 0.6944 0.5121 -0.0161 -0.0505 0.0586 164 LEU A C 1215 O O . LEU A 164 ? 0.6579 0.6727 0.4966 -0.0138 -0.0473 0.0571 164 LEU A O 1216 C CB . LEU A 164 ? 0.6434 0.7010 0.5344 0.0002 -0.0498 0.0662 164 LEU A CB 1217 C CG . LEU A 164 ? 0.6370 0.7095 0.5459 0.0081 -0.0505 0.0715 164 LEU A CG 1218 C CD1 . LEU A 164 ? 0.6375 0.7121 0.5629 0.0151 -0.0491 0.0737 164 LEU A CD1 1219 C CD2 . LEU A 164 ? 0.6159 0.7081 0.5335 0.0041 -0.0542 0.0720 164 LEU A CD2 1220 N N . ASN A 165 ? 0.6320 0.7307 0.4940 0.1059 -0.1323 -0.0932 165 ASN A N 1221 C CA . ASN A 165 ? 0.6408 0.7384 0.5076 0.1036 -0.1301 -0.0999 165 ASN A CA 1222 C C . ASN A 165 ? 0.6344 0.7344 0.5126 0.1022 -0.1332 -0.1028 165 ASN A C 1223 O O . ASN A 165 ? 0.6182 0.7213 0.4986 0.1021 -0.1374 -0.1076 165 ASN A O 1224 C CB . ASN A 165 ? 0.6753 0.7734 0.5355 0.1039 -0.1313 -0.1055 165 ASN A CB 1225 C CG . ASN A 165 ? 0.6999 0.7958 0.5645 0.1008 -0.1297 -0.1119 165 ASN A CG 1226 O OD1 . ASN A 165 ? 0.7061 0.7985 0.5725 0.0991 -0.1254 -0.1116 165 ASN A OD1 1227 N ND2 . ASN A 165 ? 0.7008 0.7990 0.5674 0.0997 -0.1338 -0.1174 165 ASN A ND2 1228 N N . VAL A 166 ? 0.5929 0.6922 0.4783 0.1013 -0.1312 -0.1002 166 VAL A N 1229 C CA . VAL A 166 ? 0.5786 0.6815 0.4749 0.1011 -0.1346 -0.1022 166 VAL A CA 1230 C C . VAL A 166 ? 0.5710 0.6761 0.4758 0.0975 -0.1313 -0.1067 166 VAL A C 1231 O O . VAL A 166 ? 0.5412 0.6434 0.4455 0.0954 -0.1260 -0.1048 166 VAL A O 1232 C CB . VAL A 166 ? 0.5835 0.6847 0.4821 0.1033 -0.1366 -0.0959 166 VAL A CB 1233 C CG1 . VAL A 166 ? 0.5786 0.6834 0.4893 0.1038 -0.1401 -0.0991 166 VAL A CG1 1234 C CG2 . VAL A 166 ? 0.6052 0.7052 0.4958 0.1061 -0.1412 -0.0910 166 VAL A CG2 1235 N N . THR A 167 ? 0.5700 0.6812 0.4827 0.0965 -0.1346 -0.1124 167 THR A N 1236 C CA . THR A 167 ? 0.5939 0.7100 0.5147 0.0922 -0.1322 -0.1172 167 THR A CA 1237 C C . THR A 167 ? 0.5688 0.6915 0.5013 0.0928 -0.1338 -0.1191 167 THR A C 1238 O O . THR A 167 ? 0.5546 0.6795 0.4908 0.0967 -0.1391 -0.1195 167 THR A O 1239 C CB . THR A 167 ? 0.6403 0.7606 0.5612 0.0897 -0.1344 -0.1234 167 THR A CB 1240 O OG1 . THR A 167 ? 0.7311 0.8557 0.6581 0.0842 -0.1316 -0.1269 167 THR A OG1 1241 C CG2 . THR A 167 ? 0.6471 0.7741 0.5731 0.0923 -0.1407 -0.1270 167 THR A CG2 1242 N N . MET A 168 ? 0.5209 0.6469 0.4593 0.0891 -0.1297 -0.1205 168 MET A N 1243 C CA . MET A 168 ? 0.5123 0.6472 0.4625 0.0891 -0.1311 -0.1244 168 MET A CA 1244 C C . MET A 168 ? 0.5144 0.6573 0.4701 0.0829 -0.1275 -0.1288 168 MET A C 1245 O O . MET A 168 ? 0.4887 0.6290 0.4434 0.0795 -0.1225 -0.1260 168 MET A O 1246 C CB . MET A 168 ? 0.5123 0.6435 0.4649 0.0919 -0.1302 -0.1199 168 MET A CB 1247 C CG . MET A 168 ? 0.5011 0.6410 0.4659 0.0936 -0.1330 -0.1245 168 MET A CG 1248 S SD . MET A 168 ? 0.5262 0.6713 0.4969 0.0991 -0.1420 -0.1295 168 MET A SD 1249 C CE . MET A 168 ? 0.5517 0.6834 0.5137 0.1041 -0.1458 -0.1207 168 MET A CE 1250 N N . PRO A 169 ? 0.5062 0.6592 0.4675 0.0809 -0.1303 -0.1352 169 PRO A N 1251 C CA . PRO A 169 ? 0.5073 0.6695 0.4739 0.0739 -0.1273 -0.1389 169 PRO A CA 1252 C C . PRO A 169 ? 0.4798 0.6515 0.4563 0.0731 -0.1254 -0.1411 169 PRO A C 1253 O O . PRO A 169 ? 0.4687 0.6434 0.4511 0.0785 -0.1284 -0.1427 169 PRO A O 1254 C CB . PRO A 169 ? 0.5261 0.6977 0.4962 0.0725 -0.1315 -0.1452 169 PRO A CB 1255 C CG . PRO A 169 ? 0.5338 0.7046 0.5049 0.0799 -0.1371 -0.1462 169 PRO A CG 1256 C CD . PRO A 169 ? 0.5281 0.6850 0.4908 0.0844 -0.1365 -0.1390 169 PRO A CD 1257 N N . ASN A 170 ? 0.4853 0.6612 0.4634 0.0664 -0.1209 -0.1408 170 ASN A N 1258 C CA . ASN A 170 ? 0.4783 0.6669 0.4662 0.0643 -0.1190 -0.1442 170 ASN A CA 1259 C C . ASN A 170 ? 0.5039 0.7093 0.4989 0.0591 -0.1203 -0.1511 170 ASN A C 1260 O O . ASN A 170 ? 0.4880 0.6961 0.4809 0.0512 -0.1180 -0.1505 170 ASN A O 1261 C CB . ASN A 170 ? 0.4713 0.6559 0.4567 0.0595 -0.1132 -0.1393 170 ASN A CB 1262 C CG . ASN A 170 ? 0.4613 0.6601 0.4565 0.0572 -0.1111 -0.1430 170 ASN A CG 1263 O OD1 . ASN A 170 ? 0.4623 0.6753 0.4667 0.0589 -0.1139 -0.1500 170 ASN A OD1 1264 N ND2 . ASN A 170 ? 0.4785 0.6741 0.4720 0.0536 -0.1064 -0.1386 170 ASN A ND2 1265 N N . ASN A 171 ? 0.5289 0.7456 0.5324 0.0636 -0.1246 -0.1577 171 ASN A N 1266 C CA . ASN A 171 ? 0.5669 0.8028 0.5788 0.0594 -0.1260 -0.1652 171 ASN A CA 1267 C C . ASN A 171 ? 0.5709 0.8235 0.5938 0.0588 -0.1244 -0.1705 171 ASN A C 1268 O O . ASN A 171 ? 0.5980 0.8692 0.6301 0.0580 -0.1265 -0.1783 171 ASN A O 1269 C CB . ASN A 171 ? 0.5961 0.8352 0.6107 0.0650 -0.1323 -0.1700 171 ASN A CB 1270 C CG . ASN A 171 ? 0.6157 0.8401 0.6195 0.0655 -0.1341 -0.1656 171 ASN A CG 1271 O OD1 . ASN A 171 ? 0.6845 0.9021 0.6862 0.0724 -0.1386 -0.1653 171 ASN A OD1 1272 N ND2 . ASN A 171 ? 0.6110 0.8305 0.6079 0.0582 -0.1311 -0.1622 171 ASN A ND2 1273 N N . GLU A 172 ? 0.5296 0.7765 0.5515 0.0593 -0.1208 -0.1666 172 GLU A N 1274 C CA . GLU A 172 ? 0.5420 0.8038 0.5736 0.0588 -0.1189 -0.1713 172 GLU A CA 1275 C C . GLU A 172 ? 0.5403 0.8106 0.5709 0.0481 -0.1134 -0.1695 172 GLU A C 1276 O O . GLU A 172 ? 0.5227 0.7841 0.5449 0.0420 -0.1115 -0.1638 172 GLU A O 1277 C CB . GLU A 172 ? 0.5431 0.7936 0.5742 0.0650 -0.1184 -0.1679 172 GLU A CB 1278 C CG . GLU A 172 ? 0.5566 0.7951 0.5868 0.0747 -0.1241 -0.1673 172 GLU A CG 1279 C CD . GLU A 172 ? 0.5734 0.8254 0.6146 0.0804 -0.1301 -0.1767 172 GLU A CD 1280 O OE1 . GLU A 172 ? 0.5871 0.8575 0.6385 0.0795 -0.1296 -0.1844 172 GLU A OE1 1281 O OE2 . GLU A 172 ? 0.6481 0.8931 0.6876 0.0859 -0.1355 -0.1767 172 GLU A OE2 1282 N N . LYS A 173 ? 0.5501 0.8375 0.5893 0.0461 -0.1114 -0.1744 173 LYS A N 1283 C CA . LYS A 173 ? 0.5910 0.8892 0.6302 0.0356 -0.1065 -0.1728 173 LYS A CA 1284 C C . LYS A 173 ? 0.5777 0.8637 0.6117 0.0344 -0.1021 -0.1656 173 LYS A C 1285 O O . LYS A 173 ? 0.5904 0.8814 0.6225 0.0255 -0.0981 -0.1623 173 LYS A O 1286 C CB . LYS A 173 ? 0.6435 0.9695 0.6948 0.0338 -0.1063 -0.1824 173 LYS A CB 1287 C CG . LYS A 173 ? 0.6923 1.0363 0.7447 0.0216 -0.1040 -0.1833 173 LYS A CG 1288 C CD . LYS A 173 ? 0.7312 1.0815 0.7847 0.0202 -0.1079 -0.1869 173 LYS A CD 1289 C CE . LYS A 173 ? 0.7543 1.1317 0.8139 0.0098 -0.1065 -0.1915 173 LYS A CE 1290 N NZ . LYS A 173 ? 0.7634 1.1496 0.8257 0.0092 -0.1107 -0.1963 173 LYS A NZ 1291 N N . PHE A 174 ? 0.5557 0.8261 0.5873 0.0430 -0.1032 -0.1628 174 PHE A N 1292 C CA . PHE A 174 ? 0.5142 0.7732 0.5416 0.0431 -0.0994 -0.1565 174 PHE A CA 1293 C C . PHE A 174 ? 0.5002 0.7350 0.5166 0.0462 -0.0994 -0.1478 174 PHE A C 1294 O O . PHE A 174 ? 0.4819 0.7085 0.4946 0.0501 -0.1029 -0.1475 174 PHE A O 1295 C CB . PHE A 174 ? 0.5131 0.7769 0.5485 0.0504 -0.1007 -0.1611 174 PHE A CB 1296 C CG . PHE A 174 ? 0.5301 0.7899 0.5693 0.0603 -0.1068 -0.1654 174 PHE A CG 1297 C CD1 . PHE A 174 ? 0.5236 0.7627 0.5555 0.0661 -0.1091 -0.1590 174 PHE A CD1 1298 C CD2 . PHE A 174 ? 0.5278 0.8054 0.5777 0.0635 -0.1107 -0.1756 174 PHE A CD2 1299 C CE1 . PHE A 174 ? 0.5359 0.7710 0.5708 0.0744 -0.1154 -0.1621 174 PHE A CE1 1300 C CE2 . PHE A 174 ? 0.5417 0.8149 0.5953 0.0727 -0.1172 -0.1793 174 PHE A CE2 1301 C CZ . PHE A 174 ? 0.5570 0.8084 0.6028 0.0779 -0.1197 -0.1721 174 PHE A CZ 1302 N N . ASP A 175 ? 0.4600 0.6844 0.4712 0.0444 -0.0956 -0.1411 175 ASP A N 1303 C CA . ASP A 175 ? 0.4642 0.6676 0.4652 0.0473 -0.0950 -0.1331 175 ASP A CA 1304 C C . ASP A 175 ? 0.4359 0.6300 0.4370 0.0567 -0.0979 -0.1324 175 ASP A C 1305 O O . ASP A 175 ? 0.4270 0.6282 0.4359 0.0606 -0.0994 -0.1365 175 ASP A O 1306 C CB . ASP A 175 ? 0.4825 0.6789 0.4786 0.0425 -0.0902 -0.1264 175 ASP A CB 1307 C CG . ASP A 175 ? 0.5314 0.7314 0.5246 0.0328 -0.0881 -0.1245 175 ASP A CG 1308 O OD1 . ASP A 175 ? 0.5363 0.7433 0.5307 0.0294 -0.0904 -0.1281 175 ASP A OD1 1309 O OD2 . ASP A 175 ? 0.5036 0.6988 0.4934 0.0283 -0.0846 -0.1192 175 ASP A OD2 1310 N N . LYS A 176 ? 0.4111 0.5898 0.4036 0.0601 -0.0991 -0.1272 176 LYS A N 1311 C CA . LYS A 176 ? 0.4006 0.5694 0.3916 0.0679 -0.1020 -0.1247 176 LYS A CA 1312 C C . LYS A 176 ? 0.3819 0.5363 0.3643 0.0681 -0.0985 -0.1162 176 LYS A C 1313 O O . LYS A 176 ? 0.3987 0.5461 0.3733 0.0651 -0.0962 -0.1123 176 LYS A O 1314 C CB . LYS A 176 ? 0.4122 0.5767 0.4001 0.0722 -0.1069 -0.1258 176 LYS A CB 1315 C CG . LYS A 176 ? 0.4152 0.5934 0.4114 0.0729 -0.1110 -0.1343 176 LYS A CG 1316 C CD . LYS A 176 ? 0.4342 0.6067 0.4257 0.0763 -0.1155 -0.1343 176 LYS A CD 1317 C CE . LYS A 176 ? 0.4297 0.6147 0.4297 0.0787 -0.1206 -0.1425 176 LYS A CE 1318 N NZ . LYS A 176 ? 0.4349 0.6128 0.4298 0.0829 -0.1255 -0.1415 176 LYS A NZ 1319 N N . LEU A 177 ? 0.3640 0.5143 0.3482 0.0719 -0.0987 -0.1136 177 LEU A N 1320 C CA . LEU A 177 ? 0.3615 0.4993 0.3381 0.0728 -0.0959 -0.1055 177 LEU A CA 1321 C C . LEU A 177 ? 0.3529 0.4814 0.3252 0.0789 -0.1001 -0.1021 177 LEU A C 1322 O O . LEU A 177 ? 0.3360 0.4654 0.3137 0.0831 -0.1043 -0.1037 177 LEU A O 1323 C CB . LEU A 177 ? 0.3466 0.4861 0.3276 0.0720 -0.0933 -0.1040 177 LEU A CB 1324 C CG . LEU A 177 ? 0.3561 0.4840 0.3308 0.0734 -0.0909 -0.0958 177 LEU A CG 1325 C CD1 . LEU A 177 ? 0.3638 0.4850 0.3296 0.0702 -0.0866 -0.0908 177 LEU A CD1 1326 C CD2 . LEU A 177 ? 0.3530 0.4847 0.3337 0.0724 -0.0890 -0.0958 177 LEU A CD2 1327 N N . TYR A 178 ? 0.3643 0.4842 0.3270 0.0792 -0.0991 -0.0974 178 TYR A N 1328 C CA . TYR A 178 ? 0.3834 0.4953 0.3403 0.0840 -0.1025 -0.0932 178 TYR A CA 1329 C C . TYR A 178 ? 0.3921 0.4958 0.3428 0.0844 -0.0993 -0.0854 178 TYR A C 1330 O O . TYR A 178 ? 0.3879 0.4894 0.3343 0.0814 -0.0943 -0.0829 178 TYR A O 1331 C CB . TYR A 178 ? 0.3966 0.5066 0.3468 0.0842 -0.1038 -0.0941 178 TYR A CB 1332 C CG . TYR A 178 ? 0.4106 0.5278 0.3661 0.0850 -0.1084 -0.1009 178 TYR A CG 1333 C CD1 . TYR A 178 ? 0.4210 0.5382 0.3792 0.0898 -0.1145 -0.1018 178 TYR A CD1 1334 C CD2 . TYR A 178 ? 0.4121 0.5366 0.3703 0.0808 -0.1071 -0.1063 178 TYR A CD2 1335 C CE1 . TYR A 178 ? 0.4186 0.5431 0.3823 0.0910 -0.1191 -0.1085 178 TYR A CE1 1336 C CE2 . TYR A 178 ? 0.4195 0.5519 0.3829 0.0814 -0.1113 -0.1127 178 TYR A CE2 1337 C CZ . TYR A 178 ? 0.4256 0.5583 0.3919 0.0869 -0.1172 -0.1141 178 TYR A CZ 1338 O OH . TYR A 178 ? 0.4388 0.5800 0.4108 0.0877 -0.1216 -0.1208 178 TYR A OH 1339 N N . ILE A 179 ? 0.3739 0.4735 0.3247 0.0878 -0.1026 -0.0814 179 ILE A N 1340 C CA . ILE A 179 ? 0.3732 0.4659 0.3181 0.0882 -0.1003 -0.0734 179 ILE A CA 1341 C C . ILE A 179 ? 0.3866 0.4744 0.3237 0.0912 -0.1038 -0.0691 179 ILE A C 1342 O O . ILE A 179 ? 0.3842 0.4721 0.3238 0.0938 -0.1099 -0.0705 179 ILE A O 1343 C CB . ILE A 179 ? 0.3747 0.4665 0.3260 0.0891 -0.1019 -0.0716 179 ILE A CB 1344 C CG1 . ILE A 179 ? 0.3676 0.4665 0.3279 0.0865 -0.0994 -0.0772 179 ILE A CG1 1345 C CG2 . ILE A 179 ? 0.3747 0.4604 0.3200 0.0887 -0.0992 -0.0631 179 ILE A CG2 1346 C CD1 . ILE A 179 ? 0.3622 0.4620 0.3194 0.0822 -0.0924 -0.0758 179 ILE A CD1 1347 N N . TRP A 180 ? 0.3844 0.4688 0.3123 0.0906 -0.1001 -0.0642 180 TRP A N 1348 C CA . TRP A 180 ? 0.4124 0.4942 0.3319 0.0928 -0.1027 -0.0601 180 TRP A CA 1349 C C . TRP A 180 ? 0.4230 0.5023 0.3351 0.0923 -0.0986 -0.0532 180 TRP A C 1350 O O . TRP A 180 ? 0.4175 0.4965 0.3314 0.0905 -0.0940 -0.0519 180 TRP A O 1351 C CB . TRP A 180 ? 0.4226 0.5063 0.3381 0.0933 -0.1032 -0.0649 180 TRP A CB 1352 C CG . TRP A 180 ? 0.4421 0.5265 0.3559 0.0908 -0.0979 -0.0682 180 TRP A CG 1353 C CD1 . TRP A 180 ? 0.4458 0.5333 0.3661 0.0880 -0.0964 -0.0739 180 TRP A CD1 1354 C CD2 . TRP A 180 ? 0.4590 0.5411 0.3640 0.0909 -0.0939 -0.0662 180 TRP A CD2 1355 N NE1 . TRP A 180 ? 0.4522 0.5380 0.3683 0.0860 -0.0923 -0.0748 180 TRP A NE1 1356 C CE2 . TRP A 180 ? 0.4547 0.5370 0.3620 0.0881 -0.0908 -0.0708 180 TRP A CE2 1357 C CE3 . TRP A 180 ? 0.4638 0.5446 0.3599 0.0929 -0.0930 -0.0615 180 TRP A CE3 1358 C CZ2 . TRP A 180 ? 0.4596 0.5391 0.3607 0.0879 -0.0875 -0.0708 180 TRP A CZ2 1359 C CZ3 . TRP A 180 ? 0.4766 0.5565 0.3666 0.0931 -0.0890 -0.0624 180 TRP A CZ3 1360 C CH2 . TRP A 180 ? 0.4644 0.5427 0.3571 0.0909 -0.0866 -0.0670 180 TRP A CH2 1361 N N . GLY A 181 ? 0.4286 0.5070 0.3324 0.0937 -0.1003 -0.0485 181 GLY A N 1362 C CA . GLY A 181 ? 0.4252 0.5032 0.3224 0.0932 -0.0968 -0.0415 181 GLY A CA 1363 C C . GLY A 181 ? 0.4497 0.5299 0.3365 0.0945 -0.0965 -0.0393 181 GLY A C 1364 O O . GLY A 181 ? 0.4418 0.5230 0.3259 0.0959 -0.1001 -0.0421 181 GLY A O 1365 N N . VAL A 182 ? 0.4474 0.5294 0.3283 0.0941 -0.0922 -0.0345 182 VAL A N 1366 C CA . VAL A 182 ? 0.4711 0.5573 0.3418 0.0953 -0.0915 -0.0319 182 VAL A CA 1367 C C . VAL A 182 ? 0.4702 0.5586 0.3372 0.0938 -0.0917 -0.0225 182 VAL A C 1368 O O . VAL A 182 ? 0.4438 0.5316 0.3134 0.0923 -0.0886 -0.0191 182 VAL A O 1369 C CB . VAL A 182 ? 0.4911 0.5796 0.3575 0.0966 -0.0858 -0.0362 182 VAL A CB 1370 C CG1 . VAL A 182 ? 0.5154 0.6100 0.3713 0.0984 -0.0854 -0.0347 182 VAL A CG1 1371 C CG2 . VAL A 182 ? 0.4970 0.5825 0.3673 0.0970 -0.0861 -0.0448 182 VAL A CG2 1372 N N . HIS A 183 ? 0.4878 0.5791 0.3485 0.0938 -0.0958 -0.0181 183 HIS A N 1373 C CA . HIS A 183 ? 0.5016 0.5959 0.3576 0.0914 -0.0968 -0.0083 183 HIS A CA 1374 C C . HIS A 183 ? 0.5010 0.6042 0.3478 0.0918 -0.0916 -0.0065 183 HIS A C 1375 O O . HIS A 183 ? 0.5107 0.6186 0.3511 0.0939 -0.0909 -0.0107 183 HIS A O 1376 C CB . HIS A 183 ? 0.5141 0.6074 0.3677 0.0906 -0.1047 -0.0037 183 HIS A CB 1377 C CG . HIS A 183 ? 0.5268 0.6223 0.3761 0.0871 -0.1071 0.0073 183 HIS A CG 1378 N ND1 . HIS A 183 ? 0.5386 0.6402 0.3786 0.0857 -0.1098 0.0131 183 HIS A ND1 1379 C CD2 . HIS A 183 ? 0.5309 0.6237 0.3839 0.0842 -0.1071 0.0141 183 HIS A CD2 1380 C CE1 . HIS A 183 ? 0.5292 0.6320 0.3671 0.0816 -0.1118 0.0235 183 HIS A CE1 1381 N NE2 . HIS A 183 ? 0.5355 0.6324 0.3815 0.0808 -0.1102 0.0240 183 HIS A NE2 1382 N N . HIS A 184 ? 0.5163 0.6223 0.3627 0.0899 -0.0879 -0.0009 184 HIS A N 1383 C CA . HIS A 184 ? 0.5269 0.6433 0.3653 0.0901 -0.0829 0.0014 184 HIS A CA 1384 C C . HIS A 184 ? 0.5288 0.6510 0.3615 0.0862 -0.0858 0.0122 184 HIS A C 1385 O O . HIS A 184 ? 0.5182 0.6391 0.3539 0.0830 -0.0856 0.0190 184 HIS A O 1386 C CB . HIS A 184 ? 0.5251 0.6415 0.3674 0.0903 -0.0767 0.0002 184 HIS A CB 1387 C CG . HIS A 184 ? 0.5424 0.6525 0.3907 0.0931 -0.0742 -0.0091 184 HIS A CG 1388 N ND1 . HIS A 184 ? 0.5370 0.6495 0.3818 0.0965 -0.0717 -0.0166 184 HIS A ND1 1389 C CD2 . HIS A 184 ? 0.5352 0.6370 0.3928 0.0923 -0.0740 -0.0118 184 HIS A CD2 1390 C CE1 . HIS A 184 ? 0.5449 0.6502 0.3963 0.0973 -0.0704 -0.0230 184 HIS A CE1 1391 N NE2 . HIS A 184 ? 0.5321 0.6316 0.3912 0.0946 -0.0716 -0.0200 184 HIS A NE2 1392 N N . PRO A 185 ? 0.5454 0.6741 0.3698 0.0859 -0.0888 0.0144 185 PRO A N 1393 C CA . PRO A 185 ? 0.5590 0.6935 0.3776 0.0811 -0.0923 0.0258 185 PRO A CA 1394 C C . PRO A 185 ? 0.5590 0.7055 0.3729 0.0790 -0.0866 0.0310 185 PRO A C 1395 O O . PRO A 185 ? 0.5326 0.6865 0.3440 0.0823 -0.0802 0.0249 185 PRO A O 1396 C CB . PRO A 185 ? 0.5749 0.7153 0.3852 0.0816 -0.0961 0.0255 185 PRO A CB 1397 C CG . PRO A 185 ? 0.5691 0.7040 0.3826 0.0865 -0.0958 0.0141 185 PRO A CG 1398 C CD . PRO A 185 ? 0.5557 0.6876 0.3751 0.0893 -0.0893 0.0071 185 PRO A CD 1399 N N . GLY A 186 ? 0.5790 0.7271 0.3919 0.0736 -0.0893 0.0421 186 GLY A N 1400 C CA . GLY A 186 ? 0.5902 0.7507 0.3988 0.0707 -0.0843 0.0481 186 GLY A CA 1401 C C . GLY A 186 ? 0.6169 0.7954 0.4143 0.0710 -0.0812 0.0482 186 GLY A C 1402 O O . GLY A 186 ? 0.6393 0.8300 0.4341 0.0718 -0.0746 0.0472 186 GLY A O 1403 N N . THR A 187 ? 0.6305 0.8115 0.4217 0.0706 -0.0859 0.0489 187 THR A N 1404 C CA . THR A 187 ? 0.6679 0.8672 0.4477 0.0705 -0.0838 0.0491 187 THR A CA 1405 C C . THR A 187 ? 0.6809 0.8796 0.4565 0.0742 -0.0865 0.0418 187 THR A C 1406 O O . THR A 187 ? 0.6554 0.8398 0.4361 0.0756 -0.0917 0.0391 187 THR A O 1407 C CB . THR A 187 ? 0.6796 0.8887 0.4523 0.0624 -0.0878 0.0633 187 THR A CB 1408 O OG1 . THR A 187 ? 0.6884 0.8873 0.4606 0.0594 -0.0970 0.0688 187 THR A OG1 1409 C CG2 . THR A 187 ? 0.6720 0.8801 0.4492 0.0576 -0.0865 0.0718 187 THR A CG2 1410 N N . ASP A 188 ? 0.7196 0.9349 0.4859 0.0759 -0.0833 0.0385 188 ASP A N 1411 C CA . ASP A 188 ? 0.7552 0.9722 0.5162 0.0791 -0.0859 0.0319 188 ASP A CA 1412 C C . ASP A 188 ? 0.7377 0.9514 0.4950 0.0740 -0.0946 0.0411 188 ASP A C 1413 O O . ASP A 188 ? 0.6996 0.9059 0.4572 0.0764 -0.0990 0.0363 188 ASP A O 1414 C CB . ASP A 188 ? 0.7995 1.0371 0.5510 0.0819 -0.0806 0.0265 188 ASP A CB 1415 C CG . ASP A 188 ? 0.8472 1.0874 0.6027 0.0879 -0.0730 0.0164 188 ASP A CG 1416 O OD1 . ASP A 188 ? 0.8846 1.1105 0.6476 0.0927 -0.0724 0.0074 188 ASP A OD1 1417 O OD2 . ASP A 188 ? 0.8860 1.1430 0.6372 0.0877 -0.0679 0.0175 188 ASP A OD2 1418 N N . ASN A 189 ? 0.7419 0.9608 0.4958 0.0667 -0.0975 0.0543 189 ASN A N 1419 C CA . ASN A 189 ? 0.7479 0.9609 0.4996 0.0612 -0.1071 0.0646 189 ASN A CA 1420 C C . ASN A 189 ? 0.7123 0.9030 0.4746 0.0630 -0.1133 0.0627 189 ASN A C 1421 O O . ASN A 189 ? 0.6833 0.8676 0.4446 0.0628 -0.1206 0.0634 189 ASN A O 1422 C CB . ASN A 189 ? 0.7872 1.0069 0.5353 0.0525 -0.1095 0.0796 189 ASN A CB 1423 C CG . ASN A 189 ? 0.8406 1.0836 0.5756 0.0481 -0.1079 0.0856 189 ASN A CG 1424 O OD1 . ASN A 189 ? 0.8815 1.1343 0.6124 0.0408 -0.1083 0.0971 189 ASN A OD1 1425 N ND2 . ASN A 189 ? 0.8541 1.1069 0.5822 0.0520 -0.1064 0.0777 189 ASN A ND2 1426 N N . ASP A 190 ? 0.6974 0.8772 0.4698 0.0646 -0.1107 0.0601 190 ASP A N 1427 C CA . ASP A 190 ? 0.6839 0.8442 0.4672 0.0666 -0.1159 0.0572 190 ASP A CA 1428 C C . ASP A 190 ? 0.6369 0.7924 0.4230 0.0732 -0.1150 0.0443 190 ASP A C 1429 O O . ASP A 190 ? 0.6156 0.7604 0.4062 0.0743 -0.1216 0.0427 190 ASP A O 1430 C CB . ASP A 190 ? 0.7062 0.8584 0.4991 0.0667 -0.1125 0.0569 190 ASP A CB 1431 C CG . ASP A 190 ? 0.7451 0.8961 0.5383 0.0598 -0.1165 0.0702 190 ASP A CG 1432 O OD1 . ASP A 190 ? 0.8051 0.9584 0.5924 0.0547 -0.1234 0.0801 190 ASP A OD1 1433 O OD2 . ASP A 190 ? 0.8141 0.9613 0.6136 0.0592 -0.1131 0.0709 190 ASP A OD2 1434 N N . GLN A 191 ? 0.6238 0.7874 0.4073 0.0775 -0.1072 0.0352 191 GLN A N 1435 C CA . GLN A 191 ? 0.6110 0.7708 0.3964 0.0832 -0.1061 0.0229 191 GLN A CA 1436 C C . GLN A 191 ? 0.6223 0.7840 0.4017 0.0830 -0.1125 0.0233 191 GLN A C 1437 O O . GLN A 191 ? 0.6242 0.7759 0.4087 0.0854 -0.1168 0.0181 191 GLN A O 1438 C CB . GLN A 191 ? 0.6001 0.7698 0.3819 0.0874 -0.0977 0.0143 191 GLN A CB 1439 C CG . GLN A 191 ? 0.5888 0.7557 0.3712 0.0929 -0.0967 0.0017 191 GLN A CG 1440 C CD . GLN A 191 ? 0.5896 0.7410 0.3833 0.0953 -0.0973 -0.0048 191 GLN A CD 1441 O OE1 . GLN A 191 ? 0.5762 0.7215 0.3771 0.0945 -0.0948 -0.0035 191 GLN A OE1 1442 N NE2 . GLN A 191 ? 0.5863 0.7326 0.3813 0.0978 -0.1005 -0.0120 191 GLN A NE2 1443 N N . ILE A 192 ? 0.6338 0.8093 0.4022 0.0799 -0.1132 0.0297 192 ILE A N 1444 C CA . ILE A 192 ? 0.6310 0.8105 0.3923 0.0791 -0.1192 0.0310 192 ILE A CA 1445 C C . ILE A 192 ? 0.6334 0.8013 0.3984 0.0754 -0.1292 0.0397 192 ILE A C 1446 O O . ILE A 192 ? 0.6100 0.7717 0.3763 0.0773 -0.1350 0.0364 192 ILE A O 1447 C CB . ILE A 192 ? 0.6490 0.8483 0.3971 0.0761 -0.1170 0.0360 192 ILE A CB 1448 C CG1 . ILE A 192 ? 0.6503 0.8610 0.3953 0.0812 -0.1079 0.0252 192 ILE A CG1 1449 C CG2 . ILE A 192 ? 0.6583 0.8619 0.3986 0.0743 -0.1239 0.0389 192 ILE A CG2 1450 C CD1 . ILE A 192 ? 0.6482 0.8544 0.3946 0.0876 -0.1075 0.0118 192 ILE A CD1 1451 N N . PHE A 193 ? 0.6541 0.8187 0.4213 0.0704 -0.1317 0.0504 193 PHE A N 1452 C CA . PHE A 193 ? 0.6623 0.8146 0.4340 0.0671 -0.1420 0.0587 193 PHE A CA 1453 C C . PHE A 193 ? 0.6553 0.7916 0.4392 0.0721 -0.1451 0.0499 193 PHE A C 1454 O O . PHE A 193 ? 0.6422 0.7704 0.4285 0.0722 -0.1539 0.0515 193 PHE A O 1455 C CB . PHE A 193 ? 0.6877 0.8378 0.4612 0.0612 -0.1435 0.0704 193 PHE A CB 1456 C CG . PHE A 193 ? 0.7258 0.8622 0.5041 0.0578 -0.1551 0.0792 193 PHE A CG 1457 C CD1 . PHE A 193 ? 0.7728 0.9126 0.5430 0.0523 -0.1635 0.0901 193 PHE A CD1 1458 C CD2 . PHE A 193 ? 0.7467 0.8670 0.5378 0.0600 -0.1582 0.0765 193 PHE A CD2 1459 C CE1 . PHE A 193 ? 0.7900 0.9158 0.5651 0.0495 -0.1754 0.0982 193 PHE A CE1 1460 C CE2 . PHE A 193 ? 0.7557 0.8631 0.5519 0.0576 -0.1696 0.0837 193 PHE A CE2 1461 C CZ . PHE A 193 ? 0.7787 0.8880 0.5670 0.0525 -0.1785 0.0946 193 PHE A CZ 1462 N N . LEU A 194 ? 0.6237 0.7561 0.4151 0.0762 -0.1380 0.0408 194 LEU A N 1463 C CA . LEU A 194 ? 0.6098 0.7289 0.4131 0.0803 -0.1404 0.0326 194 LEU A CA 1464 C C . LEU A 194 ? 0.5848 0.7047 0.3881 0.0852 -0.1393 0.0211 194 LEU A C 1465 O O . LEU A 194 ? 0.6085 0.7203 0.4181 0.0873 -0.1453 0.0174 194 LEU A O 1466 C CB . LEU A 194 ? 0.5912 0.7053 0.4033 0.0814 -0.1343 0.0291 194 LEU A CB 1467 C CG . LEU A 194 ? 0.6021 0.7112 0.4179 0.0772 -0.1367 0.0389 194 LEU A CG 1468 C CD1 . LEU A 194 ? 0.5852 0.6935 0.4067 0.0783 -0.1285 0.0349 194 LEU A CD1 1469 C CD2 . LEU A 194 ? 0.6076 0.7036 0.4318 0.0770 -0.1468 0.0413 194 LEU A CD2 1470 N N . TYR A 195 ? 0.5872 0.7169 0.3842 0.0872 -0.1320 0.0150 195 TYR A N 1471 C CA . TYR A 195 ? 0.5926 0.7219 0.3904 0.0918 -0.1303 0.0032 195 TYR A CA 1472 C C . TYR A 195 ? 0.6279 0.7680 0.4144 0.0924 -0.1310 0.0017 195 TYR A C 1473 O O . TYR A 195 ? 0.6281 0.7679 0.4148 0.0959 -0.1309 -0.0075 195 TYR A O 1474 C CB . TYR A 195 ? 0.5921 0.7207 0.3944 0.0947 -0.1219 -0.0051 195 TYR A CB 1475 C CG . TYR A 195 ? 0.5593 0.6791 0.3718 0.0936 -0.1208 -0.0028 195 TYR A CG 1476 C CD1 . TYR A 195 ? 0.5602 0.6696 0.3827 0.0940 -0.1261 -0.0042 195 TYR A CD1 1477 C CD2 . TYR A 195 ? 0.5715 0.6946 0.3835 0.0921 -0.1148 0.0006 195 TYR A CD2 1478 C CE1 . TYR A 195 ? 0.5540 0.6563 0.3855 0.0931 -0.1255 -0.0026 195 TYR A CE1 1479 C CE2 . TYR A 195 ? 0.5514 0.6668 0.3722 0.0909 -0.1141 0.0028 195 TYR A CE2 1480 C CZ . TYR A 195 ? 0.5504 0.6555 0.3809 0.0914 -0.1195 0.0010 195 TYR A CZ 1481 O OH . TYR A 195 ? 0.5683 0.6667 0.4076 0.0904 -0.1189 0.0025 195 TYR A OH 1482 N N . ALA A 196 ? 0.6540 0.8043 0.4307 0.0887 -0.1318 0.0108 196 ALA A N 1483 C CA . ALA A 196 ? 0.6924 0.8543 0.4576 0.0884 -0.1335 0.0110 196 ALA A CA 1484 C C . ALA A 196 ? 0.7206 0.8927 0.4803 0.0923 -0.1258 0.0009 196 ALA A C 1485 O O . ALA A 196 ? 0.7712 0.9522 0.5225 0.0933 -0.1269 -0.0021 196 ALA A O 1486 C CB . ALA A 196 ? 0.6879 0.8434 0.4547 0.0894 -0.1417 0.0092 196 ALA A CB 1487 N N . GLN A 197 ? 0.7217 0.8926 0.4859 0.0945 -0.1186 -0.0040 197 GLN A N 1488 C CA . GLN A 197 ? 0.7419 0.9201 0.5024 0.0989 -0.1121 -0.0145 197 GLN A CA 1489 C C . GLN A 197 ? 0.7243 0.9009 0.4901 0.1005 -0.1050 -0.0172 197 GLN A C 1490 O O . GLN A 197 ? 0.7080 0.8760 0.4814 0.0984 -0.1050 -0.0123 197 GLN A O 1491 C CB . GLN A 197 ? 0.7614 0.9326 0.5250 0.1030 -0.1142 -0.0256 197 GLN A CB 1492 C CG . GLN A 197 ? 0.7631 0.9184 0.5393 0.1037 -0.1159 -0.0288 197 GLN A CG 1493 C CD . GLN A 197 ? 0.7784 0.9280 0.5571 0.1056 -0.1209 -0.0357 197 GLN A CD 1494 O OE1 . GLN A 197 ? 0.8039 0.9601 0.5750 0.1062 -0.1238 -0.0373 197 GLN A OE1 1495 N NE2 . GLN A 197 ? 0.7812 0.9194 0.5707 0.1064 -0.1219 -0.0399 197 GLN A NE2 1496 N N . ALA A 198 ? 0.7060 0.8908 0.4677 0.1043 -0.0994 -0.0253 198 ALA A N 1497 C CA . ALA A 198 ? 0.7243 0.9084 0.4903 0.1065 -0.0928 -0.0289 198 ALA A CA 1498 C C . ALA A 198 ? 0.7095 0.8771 0.4870 0.1080 -0.0927 -0.0342 198 ALA A C 1499 O O . ALA A 198 ? 0.7124 0.8717 0.4932 0.1093 -0.0963 -0.0397 198 ALA A O 1500 C CB . ALA A 198 ? 0.7308 0.9266 0.4903 0.1112 -0.0883 -0.0380 198 ALA A CB 1501 N N . SER A 199 ? 0.7061 0.8699 0.4896 0.1076 -0.0886 -0.0324 199 SER A N 1502 C CA . SER A 199 ? 0.6916 0.8411 0.4861 0.1079 -0.0884 -0.0359 199 SER A CA 1503 C C . SER A 199 ? 0.7068 0.8519 0.5031 0.1122 -0.0867 -0.0477 199 SER A C 1504 O O . SER A 199 ? 0.7174 0.8697 0.5084 0.1156 -0.0836 -0.0532 199 SER A O 1505 C CB . SER A 199 ? 0.6592 0.8066 0.4590 0.1060 -0.0846 -0.0305 199 SER A CB 1506 O OG . SER A 199 ? 0.6435 0.7983 0.4406 0.1087 -0.0788 -0.0339 199 SER A OG 1507 N N . GLY A 200 ? 0.7207 0.8542 0.5247 0.1119 -0.0893 -0.0517 200 GLY A N 1508 C CA . GLY A 200 ? 0.7139 0.8414 0.5208 0.1147 -0.0885 -0.0619 200 GLY A CA 1509 C C . GLY A 200 ? 0.6916 0.8077 0.5091 0.1127 -0.0884 -0.0627 200 GLY A C 1510 O O . GLY A 200 ? 0.6935 0.8063 0.5164 0.1098 -0.0900 -0.0569 200 GLY A O 1511 N N . ARG A 201 ? 0.6621 0.7725 0.4827 0.1143 -0.0869 -0.0702 201 ARG A N 1512 C CA . ARG A 201 ? 0.6509 0.7522 0.4811 0.1119 -0.0862 -0.0711 201 ARG A CA 1513 C C . ARG A 201 ? 0.6097 0.7065 0.4460 0.1092 -0.0904 -0.0707 201 ARG A C 1514 O O . ARG A 201 ? 0.5955 0.6942 0.4290 0.1096 -0.0945 -0.0722 201 ARG A O 1515 C CB . ARG A 201 ? 0.6692 0.7652 0.5007 0.1136 -0.0850 -0.0790 201 ARG A CB 1516 C CG . ARG A 201 ? 0.6849 0.7781 0.5147 0.1145 -0.0890 -0.0865 201 ARG A CG 1517 C CD . ARG A 201 ? 0.7095 0.7998 0.5369 0.1175 -0.0885 -0.0943 201 ARG A CD 1518 N NE . ARG A 201 ? 0.7150 0.8025 0.5408 0.1179 -0.0929 -0.1013 201 ARG A NE 1519 C CZ . ARG A 201 ? 0.7464 0.8395 0.5644 0.1211 -0.0949 -0.1050 201 ARG A CZ 1520 N NH1 . ARG A 201 ? 0.7416 0.8449 0.5524 0.1241 -0.0928 -0.1026 201 ARG A NH1 1521 N NH2 . ARG A 201 ? 0.7444 0.8341 0.5620 0.1209 -0.0992 -0.1114 201 ARG A NH2 1522 N N . ILE A 202 ? 0.5694 0.6611 0.4144 0.1065 -0.0895 -0.0690 202 ILE A N 1523 C CA . ILE A 202 ? 0.5561 0.6443 0.4085 0.1041 -0.0931 -0.0702 202 ILE A CA 1524 C C . ILE A 202 ? 0.5376 0.6204 0.3960 0.1023 -0.0920 -0.0760 202 ILE A C 1525 O O . ILE A 202 ? 0.5408 0.6211 0.4012 0.1016 -0.0883 -0.0753 202 ILE A O 1526 C CB . ILE A 202 ? 0.5396 0.6275 0.3976 0.1021 -0.0934 -0.0634 202 ILE A CB 1527 C CG1 . ILE A 202 ? 0.5569 0.6492 0.4093 0.1029 -0.0960 -0.0570 202 ILE A CG1 1528 C CG2 . ILE A 202 ? 0.5467 0.6318 0.4141 0.1001 -0.0965 -0.0662 202 ILE A CG2 1529 C CD1 . ILE A 202 ? 0.5365 0.6278 0.3934 0.1011 -0.0965 -0.0495 202 ILE A CD1 1530 N N . THR A 203 ? 0.5227 0.6041 0.3837 0.1012 -0.0955 -0.0813 203 THR A N 1531 C CA . THR A 203 ? 0.5290 0.6061 0.3957 0.0984 -0.0952 -0.0863 203 THR A CA 1532 C C . THR A 203 ? 0.5257 0.6041 0.4008 0.0954 -0.0979 -0.0874 203 THR A C 1533 O O . THR A 203 ? 0.5225 0.6037 0.3975 0.0962 -0.1019 -0.0887 203 THR A O 1534 C CB . THR A 203 ? 0.5625 0.6370 0.4245 0.0994 -0.0967 -0.0928 203 THR A CB 1535 O OG1 . THR A 203 ? 0.5623 0.6366 0.4170 0.1029 -0.0942 -0.0927 203 THR A OG1 1536 C CG2 . THR A 203 ? 0.5641 0.6334 0.4320 0.0952 -0.0970 -0.0968 203 THR A CG2 1537 N N . VAL A 204 ? 0.4955 0.5727 0.3778 0.0921 -0.0958 -0.0868 204 VAL A N 1538 C CA . VAL A 204 ? 0.4848 0.5650 0.3760 0.0891 -0.0978 -0.0887 204 VAL A CA 1539 C C . VAL A 204 ? 0.4814 0.5601 0.3765 0.0847 -0.0970 -0.0928 204 VAL A C 1540 O O . VAL A 204 ? 0.4496 0.5248 0.3447 0.0829 -0.0937 -0.0912 204 VAL A O 1541 C CB . VAL A 204 ? 0.4741 0.5560 0.3710 0.0887 -0.0962 -0.0841 204 VAL A CB 1542 C CG1 . VAL A 204 ? 0.4529 0.5392 0.3597 0.0858 -0.0979 -0.0874 204 VAL A CG1 1543 C CG2 . VAL A 204 ? 0.4711 0.5539 0.3644 0.0923 -0.0980 -0.0792 204 VAL A CG2 1544 N N . SER A 205 ? 0.4978 0.5791 0.3958 0.0825 -0.1004 -0.0978 205 SER A N 1545 C CA . SER A 205 ? 0.5005 0.5802 0.4008 0.0776 -0.1005 -0.1014 205 SER A CA 1546 C C . SER A 205 ? 0.5034 0.5903 0.4120 0.0733 -0.1028 -0.1050 205 SER A C 1547 O O . SER A 205 ? 0.4965 0.5894 0.4087 0.0751 -0.1052 -0.1063 205 SER A O 1548 C CB . SER A 205 ? 0.5126 0.5870 0.4056 0.0788 -0.1027 -0.1048 205 SER A CB 1549 O OG . SER A 205 ? 0.5364 0.6141 0.4273 0.0811 -0.1065 -0.1078 205 SER A OG 1550 N N . THR A 206 ? 0.4948 0.5814 0.4065 0.0674 -0.1021 -0.1065 206 THR A N 1551 C CA . THR A 206 ? 0.4860 0.5804 0.4048 0.0620 -0.1041 -0.1103 206 THR A CA 1552 C C . THR A 206 ? 0.4849 0.5743 0.4008 0.0571 -0.1060 -0.1126 206 THR A C 1553 O O . THR A 206 ? 0.4719 0.5516 0.3809 0.0591 -0.1060 -0.1117 206 THR A O 1554 C CB . THR A 206 ? 0.4764 0.5773 0.4030 0.0579 -0.1012 -0.1088 206 THR A CB 1555 O OG1 . THR A 206 ? 0.4835 0.5781 0.4081 0.0544 -0.0984 -0.1054 206 THR A OG1 1556 C CG2 . THR A 206 ? 0.4686 0.5725 0.3979 0.0628 -0.0998 -0.1063 206 THR A CG2 1557 N N . LYS A 207 ? 0.5054 0.6016 0.4268 0.0508 -0.1080 -0.1156 207 LYS A N 1558 C CA . LYS A 207 ? 0.5352 0.6265 0.4548 0.0446 -0.1102 -0.1169 207 LYS A CA 1559 C C . LYS A 207 ? 0.5526 0.6363 0.4709 0.0411 -0.1078 -0.1127 207 LYS A C 1560 O O . LYS A 207 ? 0.5845 0.6586 0.4986 0.0388 -0.1102 -0.1128 207 LYS A O 1561 C CB . LYS A 207 ? 0.5464 0.6489 0.4730 0.0373 -0.1125 -0.1201 207 LYS A CB 1562 C CG . LYS A 207 ? 0.5594 0.6689 0.4873 0.0398 -0.1160 -0.1249 207 LYS A CG 1563 C CD . LYS A 207 ? 0.5803 0.7012 0.5148 0.0315 -0.1182 -0.1281 207 LYS A CD 1564 C CE . LYS A 207 ? 0.5905 0.7249 0.5311 0.0340 -0.1199 -0.1326 207 LYS A CE 1565 N NZ . LYS A 207 ? 0.5971 0.7456 0.5454 0.0255 -0.1211 -0.1355 207 LYS A NZ 1566 N N . ARG A 208 ? 0.5557 0.6428 0.4775 0.0412 -0.1037 -0.1091 208 ARG A N 1567 C CA A ARG A 208 ? 0.5620 0.6433 0.4835 0.0373 -0.1015 -0.1048 208 ARG A CA 1568 C CA B ARG A 208 ? 0.5655 0.6464 0.4867 0.0374 -0.1016 -0.1049 208 ARG A CA 1569 C C . ARG A 208 ? 0.5636 0.6370 0.4806 0.0439 -0.0983 -0.1011 208 ARG A C 1570 O O . ARG A 208 ? 0.5753 0.6429 0.4915 0.0416 -0.0966 -0.0976 208 ARG A O 1571 C CB A ARG A 208 ? 0.5696 0.6621 0.4989 0.0308 -0.0992 -0.1034 208 ARG A CB 1572 C CB B ARG A 208 ? 0.5768 0.6685 0.5057 0.0301 -0.0997 -0.1036 208 ARG A CB 1573 C CG A ARG A 208 ? 0.5715 0.6705 0.5045 0.0353 -0.0953 -0.1019 208 ARG A CG 1574 C CG B ARG A 208 ? 0.5839 0.6865 0.5184 0.0334 -0.0967 -0.1039 208 ARG A CG 1575 C CD A ARG A 208 ? 0.5817 0.6896 0.5211 0.0291 -0.0925 -0.1000 208 ARG A CD 1576 C CD B ARG A 208 ? 0.5948 0.7083 0.5363 0.0260 -0.0947 -0.1030 208 ARG A CD 1577 N NE A ARG A 208 ? 0.5858 0.6858 0.5226 0.0249 -0.0912 -0.0953 208 ARG A NE 1578 N NE B ARG A 208 ? 0.6201 0.7259 0.5591 0.0214 -0.0934 -0.0982 208 ARG A NE 1579 C CZ A ARG A 208 ? 0.5753 0.6673 0.5090 0.0290 -0.0885 -0.0913 208 ARG A CZ 1580 C CZ B ARG A 208 ? 0.6102 0.7230 0.5534 0.0130 -0.0924 -0.0963 208 ARG A CZ 1581 N NH1 A ARG A 208 ? 0.5662 0.6572 0.4985 0.0368 -0.0866 -0.0909 208 ARG A NH1 1582 N NH1 B ARG A 208 ? 0.5956 0.7244 0.5456 0.0082 -0.0923 -0.0994 208 ARG A NH1 1583 N NH2 A ARG A 208 ? 0.5824 0.6675 0.5143 0.0248 -0.0879 -0.0874 208 ARG A NH2 1584 N NH2 B ARG A 208 ? 0.6207 0.7248 0.5610 0.0094 -0.0918 -0.0915 208 ARG A NH2 1585 N N . SER A 209 ? 0.5303 0.6038 0.4443 0.0515 -0.0975 -0.1015 209 SER A N 1586 C CA . SER A 209 ? 0.5289 0.5977 0.4393 0.0570 -0.0940 -0.0976 209 SER A CA 1587 C C . SER A 209 ? 0.5214 0.5879 0.4255 0.0647 -0.0946 -0.0983 209 SER A C 1588 O O . SER A 209 ? 0.5158 0.5861 0.4195 0.0663 -0.0973 -0.1014 209 SER A O 1589 C CB . SER A 209 ? 0.5267 0.6027 0.4430 0.0565 -0.0905 -0.0944 209 SER A CB 1590 O OG . SER A 209 ? 0.5320 0.6154 0.4510 0.0596 -0.0916 -0.0963 209 SER A OG 1591 N N . GLN A 210 ? 0.5082 0.5696 0.4074 0.0691 -0.0921 -0.0954 210 GLN A N 1592 C CA . GLN A 210 ? 0.5245 0.5856 0.4173 0.0760 -0.0922 -0.0953 210 GLN A CA 1593 C C . GLN A 210 ? 0.5264 0.5866 0.4172 0.0793 -0.0881 -0.0902 210 GLN A C 1594 O O . GLN A 210 ? 0.5205 0.5764 0.4118 0.0779 -0.0860 -0.0884 210 GLN A O 1595 C CB . GLN A 210 ? 0.5507 0.6061 0.4368 0.0785 -0.0950 -0.0995 210 GLN A CB 1596 C CG . GLN A 210 ? 0.5667 0.6137 0.4514 0.0769 -0.0953 -0.1004 210 GLN A CG 1597 C CD . GLN A 210 ? 0.6107 0.6519 0.4887 0.0807 -0.0985 -0.1053 210 GLN A CD 1598 O OE1 . GLN A 210 ? 0.6378 0.6822 0.5114 0.0846 -0.0999 -0.1078 210 GLN A OE1 1599 N NE2 . GLN A 210 ? 0.6086 0.6411 0.4857 0.0797 -0.1000 -0.1068 210 GLN A NE2 1600 N N . GLN A 211 ? 0.5102 0.5746 0.3992 0.0832 -0.0873 -0.0877 211 GLN A N 1601 C CA . GLN A 211 ? 0.4982 0.5630 0.3849 0.0861 -0.0838 -0.0825 211 GLN A CA 1602 C C . GLN A 211 ? 0.4986 0.5656 0.3778 0.0912 -0.0846 -0.0820 211 GLN A C 1603 O O . GLN A 211 ? 0.4868 0.5576 0.3659 0.0921 -0.0871 -0.0818 211 GLN A O 1604 C CB . GLN A 211 ? 0.5056 0.5745 0.3986 0.0843 -0.0824 -0.0785 211 GLN A CB 1605 C CG . GLN A 211 ? 0.5096 0.5790 0.4103 0.0789 -0.0814 -0.0790 211 GLN A CG 1606 C CD . GLN A 211 ? 0.5100 0.5852 0.4176 0.0778 -0.0815 -0.0775 211 GLN A CD 1607 O OE1 . GLN A 211 ? 0.5404 0.6161 0.4497 0.0782 -0.0791 -0.0732 211 GLN A OE1 1608 N NE2 . GLN A 211 ? 0.5009 0.5805 0.4128 0.0765 -0.0848 -0.0814 211 GLN A NE2 1609 N N . THR A 212 ? 0.5102 0.5756 0.3834 0.0946 -0.0828 -0.0818 212 THR A N 1610 C CA . THR A 212 ? 0.5201 0.5897 0.3857 0.0992 -0.0830 -0.0810 212 THR A CA 1611 C C . THR A 212 ? 0.5369 0.6097 0.4008 0.1007 -0.0791 -0.0747 212 THR A C 1612 O O . THR A 212 ? 0.5201 0.5906 0.3855 0.1005 -0.0760 -0.0736 212 THR A O 1613 C CB . THR A 212 ? 0.5255 0.5929 0.3848 0.1024 -0.0843 -0.0869 212 THR A CB 1614 O OG1 . THR A 212 ? 0.5267 0.5911 0.3873 0.1005 -0.0884 -0.0923 212 THR A OG1 1615 C CG2 . THR A 212 ? 0.5329 0.6069 0.3840 0.1069 -0.0840 -0.0860 212 THR A CG2 1616 N N . VAL A 213 ? 0.5414 0.6196 0.4025 0.1019 -0.0796 -0.0703 213 VAL A N 1617 C CA . VAL A 213 ? 0.5357 0.6177 0.3955 0.1023 -0.0765 -0.0636 213 VAL A CA 1618 C C . VAL A 213 ? 0.5370 0.6261 0.3881 0.1054 -0.0768 -0.0614 213 VAL A C 1619 O O . VAL A 213 ? 0.5291 0.6202 0.3774 0.1057 -0.0804 -0.0620 213 VAL A O 1620 C CB . VAL A 213 ? 0.5356 0.6174 0.4018 0.0993 -0.0774 -0.0584 213 VAL A CB 1621 C CG1 . VAL A 213 ? 0.5353 0.6208 0.3998 0.0994 -0.0748 -0.0510 213 VAL A CG1 1622 C CG2 . VAL A 213 ? 0.5337 0.6109 0.4086 0.0960 -0.0768 -0.0606 213 VAL A CG2 1623 N N . ILE A 214 ? 0.5618 0.6555 0.4088 0.1072 -0.0732 -0.0588 214 ILE A N 1624 C CA . ILE A 214 ? 0.5830 0.6859 0.4212 0.1098 -0.0728 -0.0568 214 ILE A CA 1625 C C . ILE A 214 ? 0.5790 0.6869 0.4167 0.1074 -0.0722 -0.0474 214 ILE A C 1626 O O . ILE A 214 ? 0.5619 0.6702 0.4024 0.1064 -0.0688 -0.0434 214 ILE A O 1627 C CB . ILE A 214 ? 0.6148 0.7223 0.4485 0.1137 -0.0693 -0.0605 214 ILE A CB 1628 C CG1 . ILE A 214 ? 0.6318 0.7325 0.4664 0.1160 -0.0707 -0.0699 214 ILE A CG1 1629 C CG2 . ILE A 214 ? 0.6089 0.7285 0.4332 0.1161 -0.0689 -0.0591 214 ILE A CG2 1630 C CD1 . ILE A 214 ? 0.6766 0.7785 0.5063 0.1176 -0.0746 -0.0751 214 ILE A CD1 1631 N N . PRO A 215 ? 0.5792 0.6907 0.4133 0.1064 -0.0758 -0.0435 215 PRO A N 1632 C CA . PRO A 215 ? 0.5829 0.6991 0.4155 0.1038 -0.0758 -0.0339 215 PRO A CA 1633 C C . PRO A 215 ? 0.5787 0.7057 0.4043 0.1052 -0.0717 -0.0315 215 PRO A C 1634 O O . PRO A 215 ? 0.5863 0.7197 0.4055 0.1084 -0.0708 -0.0366 215 PRO A O 1635 C CB . PRO A 215 ? 0.6015 0.7189 0.4309 0.1026 -0.0815 -0.0311 215 PRO A CB 1636 C CG . PRO A 215 ? 0.6021 0.7140 0.4337 0.1043 -0.0842 -0.0394 215 PRO A CG 1637 C CD . PRO A 215 ? 0.5874 0.6986 0.4185 0.1071 -0.0803 -0.0471 215 PRO A CD 1638 N N . ASN A 216 ? 0.5705 0.7001 0.3978 0.1028 -0.0692 -0.0244 216 ASN A N 1639 C CA . ASN A 216 ? 0.5695 0.7106 0.3913 0.1038 -0.0648 -0.0218 216 ASN A CA 1640 C C . ASN A 216 ? 0.5654 0.7135 0.3837 0.0994 -0.0661 -0.0108 216 ASN A C 1641 O O . ASN A 216 ? 0.5497 0.6933 0.3733 0.0960 -0.0664 -0.0044 216 ASN A O 1642 C CB . ASN A 216 ? 0.5711 0.7097 0.3983 0.1049 -0.0601 -0.0237 216 ASN A CB 1643 C CG . ASN A 216 ? 0.5867 0.7182 0.4167 0.1087 -0.0593 -0.0339 216 ASN A CG 1644 O OD1 . ASN A 216 ? 0.6099 0.7453 0.4349 0.1125 -0.0595 -0.0405 216 ASN A OD1 1645 N ND2 . ASN A 216 ? 0.5928 0.7144 0.4310 0.1074 -0.0588 -0.0350 216 ASN A ND2 1646 N N . ILE A 217 ? 0.5768 0.7364 0.3862 0.0994 -0.0670 -0.0087 217 ILE A N 1647 C CA . ILE A 217 ? 0.5735 0.7413 0.3779 0.0945 -0.0689 0.0022 217 ILE A CA 1648 C C . ILE A 217 ? 0.5794 0.7566 0.3834 0.0931 -0.0638 0.0070 217 ILE A C 1649 O O . ILE A 217 ? 0.5740 0.7588 0.3764 0.0970 -0.0586 0.0012 217 ILE A O 1650 C CB . ILE A 217 ? 0.5888 0.7683 0.3829 0.0946 -0.0710 0.0027 217 ILE A CB 1651 C CG1 . ILE A 217 ? 0.5876 0.7575 0.3825 0.0954 -0.0769 -0.0008 217 ILE A CG1 1652 C CG2 . ILE A 217 ? 0.5801 0.7701 0.3683 0.0887 -0.0728 0.0150 217 ILE A CG2 1653 C CD1 . ILE A 217 ? 0.6184 0.7978 0.4042 0.0977 -0.0780 -0.0053 217 ILE A CD1 1654 N N . GLY A 218 ? 0.5858 0.7622 0.3915 0.0876 -0.0656 0.0175 218 GLY A N 1655 C CA . GLY A 218 ? 0.5816 0.7682 0.3865 0.0853 -0.0613 0.0234 218 GLY A CA 1656 C C . GLY A 218 ? 0.5874 0.7662 0.3977 0.0797 -0.0640 0.0330 218 GLY A C 1657 O O . GLY A 218 ? 0.5751 0.7389 0.3925 0.0792 -0.0679 0.0324 218 GLY A O 1658 N N . SER A 219 ? 0.5744 0.7640 0.3817 0.0753 -0.0622 0.0417 219 SER A N 1659 C CA . SER A 219 ? 0.5907 0.7732 0.4034 0.0698 -0.0649 0.0509 219 SER A CA 1660 C C . SER A 219 ? 0.5806 0.7556 0.4022 0.0721 -0.0607 0.0465 219 SER A C 1661 O O . SER A 219 ? 0.6031 0.7861 0.4244 0.0756 -0.0544 0.0416 219 SER A O 1662 C CB . SER A 219 ? 0.6098 0.8071 0.4163 0.0637 -0.0645 0.0621 219 SER A CB 1663 O OG . SER A 219 ? 0.6226 0.8282 0.4202 0.0608 -0.0684 0.0670 219 SER A OG 1664 N N . ARG A 220 ? 0.5514 0.7113 0.3810 0.0705 -0.0645 0.0479 220 ARG A N 1665 C CA . ARG A 220 ? 0.5673 0.7212 0.4050 0.0704 -0.0614 0.0472 220 ARG A CA 1666 C C . ARG A 220 ? 0.5628 0.7160 0.4020 0.0638 -0.0648 0.0587 220 ARG A C 1667 O O . ARG A 220 ? 0.5671 0.7203 0.4023 0.0596 -0.0707 0.0662 220 ARG A O 1668 C CB . ARG A 220 ? 0.5597 0.6983 0.4058 0.0733 -0.0631 0.0397 220 ARG A CB 1669 C CG . ARG A 220 ? 0.5563 0.6943 0.4024 0.0791 -0.0597 0.0285 220 ARG A CG 1670 C CD . ARG A 220 ? 0.5704 0.7084 0.4115 0.0810 -0.0633 0.0251 220 ARG A CD 1671 N NE . ARG A 220 ? 0.5810 0.7145 0.4239 0.0859 -0.0616 0.0143 220 ARG A NE 1672 C CZ . ARG A 220 ? 0.5895 0.7258 0.4271 0.0889 -0.0626 0.0090 220 ARG A CZ 1673 N NH1 . ARG A 220 ? 0.5827 0.7271 0.4125 0.0876 -0.0651 0.0133 220 ARG A NH1 1674 N NH2 . ARG A 220 ? 0.5988 0.7300 0.4387 0.0928 -0.0614 -0.0004 220 ARG A NH2 1675 N N . PRO A 221 ? 0.5576 0.7098 0.4021 0.0625 -0.0616 0.0604 221 PRO A N 1676 C CA . PRO A 221 ? 0.5631 0.7132 0.4096 0.0560 -0.0655 0.0710 221 PRO A CA 1677 C C . PRO A 221 ? 0.5728 0.7081 0.4234 0.0540 -0.0741 0.0734 221 PRO A C 1678 O O . PRO A 221 ? 0.5740 0.6981 0.4307 0.0577 -0.0756 0.0656 221 PRO A O 1679 C CB . PRO A 221 ? 0.5529 0.7012 0.4063 0.0565 -0.0607 0.0693 221 PRO A CB 1680 C CG . PRO A 221 ? 0.5392 0.6974 0.3899 0.0618 -0.0532 0.0617 221 PRO A CG 1681 C CD . PRO A 221 ? 0.5436 0.6976 0.3921 0.0664 -0.0548 0.0537 221 PRO A CD 1682 N N . ARG A 222 ? 0.5661 0.7018 0.4133 0.0482 -0.0803 0.0838 222 ARG A N 1683 C CA . ARG A 222 ? 0.5711 0.6929 0.4220 0.0468 -0.0896 0.0858 222 ARG A CA 1684 C C . ARG A 222 ? 0.5453 0.6534 0.4071 0.0477 -0.0917 0.0826 222 ARG A C 1685 O O . ARG A 222 ? 0.5525 0.6613 0.4178 0.0454 -0.0891 0.0854 222 ARG A O 1686 C CB . ARG A 222 ? 0.5929 0.7168 0.4383 0.0397 -0.0967 0.0987 222 ARG A CB 1687 C CG . ARG A 222 ? 0.6062 0.7430 0.4409 0.0390 -0.0960 0.1011 222 ARG A CG 1688 C CD . ARG A 222 ? 0.6378 0.7762 0.4669 0.0310 -0.1040 0.1147 222 ARG A CD 1689 N NE . ARG A 222 ? 0.6461 0.7971 0.4647 0.0301 -0.1040 0.1170 222 ARG A NE 1690 C CZ . ARG A 222 ? 0.6758 0.8266 0.4886 0.0244 -0.1123 0.1269 222 ARG A CZ 1691 N NH1 . ARG A 222 ? 0.6864 0.8238 0.5035 0.0194 -0.1219 0.1353 222 ARG A NH1 1692 N NH2 . ARG A 222 ? 0.6652 0.8292 0.4682 0.0238 -0.1114 0.1280 222 ARG A NH2 1693 N N . VAL A 223 ? 0.5525 0.6494 0.4197 0.0513 -0.0962 0.0758 223 VAL A N 1694 C CA . VAL A 223 ? 0.5453 0.6298 0.4230 0.0524 -0.0995 0.0719 223 VAL A CA 1695 C C . VAL A 223 ? 0.5511 0.6253 0.4308 0.0512 -0.1105 0.0751 223 VAL A C 1696 O O . VAL A 223 ? 0.5338 0.6069 0.4110 0.0539 -0.1134 0.0717 223 VAL A O 1697 C CB . VAL A 223 ? 0.5407 0.6227 0.4239 0.0583 -0.0947 0.0592 223 VAL A CB 1698 C CG1 . VAL A 223 ? 0.5357 0.6063 0.4297 0.0594 -0.0990 0.0547 223 VAL A CG1 1699 C CG2 . VAL A 223 ? 0.5244 0.6151 0.4060 0.0596 -0.0848 0.0561 223 VAL A CG2 1700 N N . ARG A 224 ? 0.5826 0.6487 0.4669 0.0473 -0.1169 0.0815 224 ARG A N 1701 C CA . ARG A 224 ? 0.6170 0.6725 0.5032 0.0457 -0.1287 0.0861 224 ARG A CA 1702 C C . ARG A 224 ? 0.6063 0.6680 0.4822 0.0433 -0.1315 0.0928 224 ARG A C 1703 O O . ARG A 224 ? 0.6276 0.6841 0.5033 0.0454 -0.1379 0.0909 224 ARG A O 1704 C CB . ARG A 224 ? 0.6288 0.6740 0.5246 0.0515 -0.1329 0.0752 224 ARG A CB 1705 C CG . ARG A 224 ? 0.6262 0.6673 0.5318 0.0533 -0.1299 0.0688 224 ARG A CG 1706 C CD . ARG A 224 ? 0.6343 0.6672 0.5498 0.0587 -0.1342 0.0578 224 ARG A CD 1707 N NE . ARG A 224 ? 0.6160 0.6545 0.5308 0.0635 -0.1283 0.0480 224 ARG A NE 1708 C CZ . ARG A 224 ? 0.5953 0.6404 0.5108 0.0653 -0.1186 0.0416 224 ARG A CZ 1709 N NH1 . ARG A 224 ? 0.5964 0.6440 0.5131 0.0630 -0.1132 0.0436 224 ARG A NH1 1710 N NH2 . ARG A 224 ? 0.5954 0.6443 0.5100 0.0691 -0.1147 0.0333 224 ARG A NH2 1711 N N . ASN A 225 ? 0.6162 0.6906 0.4835 0.0389 -0.1261 0.1003 225 ASN A N 1712 C CA . ASN A 225 ? 0.6182 0.7026 0.4743 0.0355 -0.1272 0.1077 225 ASN A CA 1713 C C . ASN A 225 ? 0.6044 0.6948 0.4557 0.0409 -0.1236 0.0995 225 ASN A C 1714 O O . ASN A 225 ? 0.6065 0.7029 0.4495 0.0387 -0.1266 0.1046 225 ASN A O 1715 C CB . ASN A 225 ? 0.6567 0.7326 0.5116 0.0298 -0.1397 0.1188 225 ASN A CB 1716 C CG . ASN A 225 ? 0.6971 0.7860 0.5400 0.0228 -0.1404 0.1309 225 ASN A CG 1717 O OD1 . ASN A 225 ? 0.7209 0.8243 0.5584 0.0200 -0.1325 0.1342 225 ASN A OD1 1718 N ND2 . ASN A 225 ? 0.7218 0.8064 0.5605 0.0199 -0.1501 0.1374 225 ASN A ND2 1719 N N . ILE A 226 ? 0.5606 0.6502 0.4168 0.0474 -0.1171 0.0872 226 ILE A N 1720 C CA . ILE A 226 ? 0.5397 0.6344 0.3919 0.0524 -0.1136 0.0790 226 ILE A CA 1721 C C . ILE A 226 ? 0.5300 0.6366 0.3789 0.0551 -0.1025 0.0733 226 ILE A C 1722 O O . ILE A 226 ? 0.5070 0.6112 0.3623 0.0574 -0.0972 0.0676 226 ILE A O 1723 C CB . ILE A 226 ? 0.5427 0.6260 0.4033 0.0579 -0.1168 0.0686 226 ILE A CB 1724 C CG1 . ILE A 226 ? 0.5514 0.6230 0.4158 0.0565 -0.1287 0.0729 226 ILE A CG1 1725 C CG2 . ILE A 226 ? 0.5241 0.6131 0.3807 0.0627 -0.1128 0.0599 226 ILE A CG2 1726 C CD1 . ILE A 226 ? 0.5667 0.6410 0.4228 0.0548 -0.1347 0.0781 226 ILE A CD1 1727 N N . PRO A 227 ? 0.5299 0.6493 0.3690 0.0550 -0.0991 0.0744 227 PRO A N 1728 C CA . PRO A 227 ? 0.5328 0.6635 0.3688 0.0586 -0.0895 0.0679 227 PRO A CA 1729 C C . PRO A 227 ? 0.5243 0.6528 0.3611 0.0651 -0.0868 0.0557 227 PRO A C 1730 O O . PRO A 227 ? 0.5216 0.6571 0.3569 0.0687 -0.0796 0.0492 227 PRO A O 1731 C CB . PRO A 227 ? 0.5420 0.6889 0.3668 0.0550 -0.0881 0.0753 227 PRO A CB 1732 C CG . PRO A 227 ? 0.5484 0.6917 0.3693 0.0520 -0.0968 0.0812 227 PRO A CG 1733 C CD . PRO A 227 ? 0.5569 0.6829 0.3870 0.0505 -0.1044 0.0836 227 PRO A CD 1734 N N . SER A 228 ? 0.5201 0.6394 0.3593 0.0667 -0.0930 0.0528 228 SER A N 1735 C CA . SER A 228 ? 0.5315 0.6476 0.3726 0.0722 -0.0914 0.0414 228 SER A CA 1736 C C . SER A 228 ? 0.5079 0.6147 0.3595 0.0746 -0.0892 0.0343 228 SER A C 1737 O O . SER A 228 ? 0.4984 0.6004 0.3559 0.0722 -0.0900 0.0381 228 SER A O 1738 C CB . SER A 228 ? 0.5487 0.6592 0.3893 0.0728 -0.0993 0.0409 228 SER A CB 1739 O OG . SER A 228 ? 0.5864 0.7056 0.4170 0.0705 -0.1018 0.0470 228 SER A OG 1740 N N . ARG A 229 ? 0.5039 0.6085 0.3577 0.0789 -0.0870 0.0242 229 ARG A N 1741 C CA . ARG A 229 ? 0.4790 0.5754 0.3426 0.0807 -0.0856 0.0172 229 ARG A CA 1742 C C . ARG A 229 ? 0.4756 0.5673 0.3421 0.0837 -0.0887 0.0089 229 ARG A C 1743 O O . ARG A 229 ? 0.4855 0.5806 0.3460 0.0853 -0.0899 0.0069 229 ARG A O 1744 C CB . ARG A 229 ? 0.4696 0.5697 0.3338 0.0821 -0.0777 0.0132 229 ARG A CB 1745 C CG . ARG A 229 ? 0.4809 0.5855 0.3445 0.0793 -0.0742 0.0202 229 ARG A CG 1746 C CD . ARG A 229 ? 0.4756 0.5730 0.3468 0.0762 -0.0772 0.0247 229 ARG A CD 1747 N NE . ARG A 229 ? 0.4910 0.5935 0.3616 0.0736 -0.0732 0.0307 229 ARG A NE 1748 C CZ . ARG A 229 ? 0.5010 0.6077 0.3679 0.0696 -0.0751 0.0405 229 ARG A CZ 1749 N NH1 . ARG A 229 ? 0.5181 0.6239 0.3812 0.0673 -0.0816 0.0463 229 ARG A NH1 1750 N NH2 . ARG A 229 ? 0.4860 0.5980 0.3528 0.0674 -0.0709 0.0450 229 ARG A NH2 1751 N N . ILE A 230 ? 0.4628 0.5474 0.3387 0.0842 -0.0900 0.0041 230 ILE A N 1752 C CA . ILE A 230 ? 0.4577 0.5395 0.3375 0.0868 -0.0912 -0.0050 230 ILE A CA 1753 C C . ILE A 230 ? 0.4402 0.5214 0.3252 0.0873 -0.0852 -0.0109 230 ILE A C 1754 O O . ILE A 230 ? 0.4205 0.4997 0.3108 0.0856 -0.0837 -0.0090 230 ILE A O 1755 C CB . ILE A 230 ? 0.4702 0.5459 0.3574 0.0870 -0.0986 -0.0060 230 ILE A CB 1756 C CG1 . ILE A 230 ? 0.4844 0.5600 0.3663 0.0868 -0.1054 -0.0008 230 ILE A CG1 1757 C CG2 . ILE A 230 ? 0.4690 0.5433 0.3624 0.0891 -0.0987 -0.0160 230 ILE A CG2 1758 C CD1 . ILE A 230 ? 0.4912 0.5601 0.3803 0.0871 -0.1139 -0.0005 230 ILE A CD1 1759 N N . SER A 231 ? 0.4423 0.5251 0.3252 0.0891 -0.0823 -0.0177 231 SER A N 1760 C CA . SER A 231 ? 0.4372 0.5186 0.3249 0.0890 -0.0780 -0.0234 231 SER A CA 1761 C C . SER A 231 ? 0.4313 0.5099 0.3256 0.0892 -0.0812 -0.0305 231 SER A C 1762 O O . SER A 231 ? 0.4300 0.5090 0.3222 0.0907 -0.0845 -0.0337 231 SER A O 1763 C CB . SER A 231 ? 0.4463 0.5308 0.3278 0.0907 -0.0733 -0.0259 231 SER A CB 1764 O OG . SER A 231 ? 0.4611 0.5496 0.3383 0.0904 -0.0698 -0.0200 231 SER A OG 1765 N N . ILE A 232 ? 0.4197 0.4967 0.3221 0.0876 -0.0802 -0.0328 232 ILE A N 1766 C CA . ILE A 232 ? 0.4196 0.4962 0.3294 0.0873 -0.0831 -0.0392 232 ILE A CA 1767 C C . ILE A 232 ? 0.4240 0.5015 0.3351 0.0860 -0.0796 -0.0453 232 ILE A C 1768 O O . ILE A 232 ? 0.4129 0.4901 0.3239 0.0846 -0.0750 -0.0442 232 ILE A O 1769 C CB . ILE A 232 ? 0.4161 0.4919 0.3346 0.0860 -0.0847 -0.0385 232 ILE A CB 1770 C CG1 . ILE A 232 ? 0.4261 0.4994 0.3442 0.0869 -0.0900 -0.0327 232 ILE A CG1 1771 C CG2 . ILE A 232 ? 0.4106 0.4885 0.3373 0.0856 -0.0867 -0.0463 232 ILE A CG2 1772 C CD1 . ILE A 232 ? 0.4299 0.5024 0.3475 0.0891 -0.0966 -0.0344 232 ILE A CD1 1773 N N . TYR A 233 ? 0.4178 0.4964 0.3307 0.0864 -0.0823 -0.0512 233 TYR A N 1774 C CA . TYR A 233 ? 0.4263 0.5057 0.3404 0.0845 -0.0802 -0.0568 233 TYR A CA 1775 C C . TYR A 233 ? 0.4315 0.5144 0.3538 0.0830 -0.0832 -0.0626 233 TYR A C 1776 O O . TYR A 233 ? 0.4089 0.4931 0.3349 0.0847 -0.0874 -0.0630 233 TYR A O 1777 C CB . TYR A 233 ? 0.4310 0.5092 0.3374 0.0862 -0.0805 -0.0587 233 TYR A CB 1778 C CG . TYR A 233 ? 0.4469 0.5237 0.3457 0.0879 -0.0772 -0.0543 233 TYR A CG 1779 C CD1 . TYR A 233 ? 0.4522 0.5301 0.3456 0.0902 -0.0783 -0.0492 233 TYR A CD1 1780 C CD2 . TYR A 233 ? 0.4474 0.5223 0.3448 0.0870 -0.0733 -0.0549 233 TYR A CD2 1781 C CE1 . TYR A 233 ? 0.4513 0.5303 0.3382 0.0916 -0.0750 -0.0453 233 TYR A CE1 1782 C CE2 . TYR A 233 ? 0.4637 0.5387 0.3551 0.0891 -0.0704 -0.0515 233 TYR A CE2 1783 C CZ . TYR A 233 ? 0.4769 0.5547 0.3630 0.0914 -0.0710 -0.0470 233 TYR A CZ 1784 O OH . TYR A 233 ? 0.4838 0.5638 0.3641 0.0933 -0.0678 -0.0440 233 TYR A OH 1785 N N . TRP A 234 ? 0.4168 0.5017 0.3422 0.0798 -0.0814 -0.0669 234 TRP A N 1786 C CA . TRP A 234 ? 0.3969 0.4876 0.3301 0.0779 -0.0838 -0.0729 234 TRP A CA 1787 C C . TRP A 234 ? 0.3899 0.4821 0.3222 0.0750 -0.0836 -0.0775 234 TRP A C 1788 O O . TRP A 234 ? 0.3863 0.4743 0.3135 0.0736 -0.0811 -0.0762 234 TRP A O 1789 C CB . TRP A 234 ? 0.4040 0.4989 0.3452 0.0755 -0.0823 -0.0733 234 TRP A CB 1790 C CG . TRP A 234 ? 0.4125 0.5080 0.3541 0.0709 -0.0777 -0.0728 234 TRP A CG 1791 C CD1 . TRP A 234 ? 0.4226 0.5234 0.3680 0.0660 -0.0770 -0.0771 234 TRP A CD1 1792 C CD2 . TRP A 234 ? 0.4316 0.5227 0.3699 0.0702 -0.0737 -0.0674 234 TRP A CD2 1793 N NE1 . TRP A 234 ? 0.4357 0.5347 0.3800 0.0624 -0.0732 -0.0743 234 TRP A NE1 1794 C CE2 . TRP A 234 ? 0.4307 0.5239 0.3710 0.0650 -0.0710 -0.0688 234 TRP A CE2 1795 C CE3 . TRP A 234 ? 0.4503 0.5368 0.3845 0.0729 -0.0722 -0.0615 234 TRP A CE3 1796 C CZ2 . TRP A 234 ? 0.4644 0.5543 0.4027 0.0632 -0.0674 -0.0646 234 TRP A CZ2 1797 C CZ3 . TRP A 234 ? 0.4649 0.5490 0.3973 0.0711 -0.0681 -0.0577 234 TRP A CZ3 1798 C CH2 . TRP A 234 ? 0.4821 0.5674 0.4166 0.0667 -0.0658 -0.0593 234 TRP A CH2 1799 N N . THR A 235 ? 0.3932 0.4911 0.3305 0.0742 -0.0868 -0.0829 235 THR A N 1800 C CA . THR A 235 ? 0.4026 0.5027 0.3395 0.0709 -0.0876 -0.0875 235 THR A CA 1801 C C . THR A 235 ? 0.4155 0.5260 0.3618 0.0680 -0.0891 -0.0929 235 THR A C 1802 O O . THR A 235 ? 0.4150 0.5301 0.3663 0.0711 -0.0923 -0.0954 235 THR A O 1803 C CB . THR A 235 ? 0.4260 0.5233 0.3571 0.0742 -0.0910 -0.0891 235 THR A CB 1804 O OG1 . THR A 235 ? 0.4136 0.5037 0.3363 0.0777 -0.0899 -0.0844 235 THR A OG1 1805 C CG2 . THR A 235 ? 0.4301 0.5283 0.3601 0.0703 -0.0919 -0.0934 235 THR A CG2 1806 N N . ILE A 236 ? 0.4166 0.5313 0.3654 0.0620 -0.0872 -0.0948 236 ILE A N 1807 C CA . ILE A 236 ? 0.4157 0.5429 0.3731 0.0584 -0.0884 -0.1005 236 ILE A CA 1808 C C . ILE A 236 ? 0.4216 0.5514 0.3779 0.0559 -0.0911 -0.1046 236 ILE A C 1809 O O . ILE A 236 ? 0.4316 0.5551 0.3821 0.0531 -0.0905 -0.1029 236 ILE A O 1810 C CB . ILE A 236 ? 0.4226 0.5552 0.3840 0.0522 -0.0847 -0.0996 236 ILE A CB 1811 C CG1 . ILE A 236 ? 0.4261 0.5575 0.3897 0.0549 -0.0825 -0.0964 236 ILE A CG1 1812 C CG2 . ILE A 236 ? 0.4191 0.5670 0.3888 0.0476 -0.0857 -0.1058 236 ILE A CG2 1813 C CD1 . ILE A 236 ? 0.4250 0.5591 0.3903 0.0494 -0.0785 -0.0940 236 ILE A CD1 1814 N N . VAL A 237 ? 0.4194 0.5583 0.3815 0.0574 -0.0946 -0.1101 237 VAL A N 1815 C CA . VAL A 237 ? 0.4379 0.5804 0.3996 0.0554 -0.0976 -0.1143 237 VAL A CA 1816 C C . VAL A 237 ? 0.4517 0.6101 0.4223 0.0497 -0.0979 -0.1198 237 VAL A C 1817 O O . VAL A 237 ? 0.4297 0.5985 0.4084 0.0519 -0.0989 -0.1239 237 VAL A O 1818 C CB . VAL A 237 ? 0.4381 0.5786 0.3985 0.0620 -0.1020 -0.1162 237 VAL A CB 1819 C CG1 . VAL A 237 ? 0.4330 0.5780 0.3933 0.0598 -0.1053 -0.1209 237 VAL A CG1 1820 C CG2 . VAL A 237 ? 0.4442 0.5711 0.3953 0.0669 -0.1016 -0.1104 237 VAL A CG2 1821 N N . LYS A 238 ? 0.4720 0.6323 0.4410 0.0425 -0.0975 -0.1202 238 LYS A N 1822 C CA . LYS A 238 ? 0.4993 0.6756 0.4755 0.0353 -0.0975 -0.1245 238 LYS A CA 1823 C C . LYS A 238 ? 0.4940 0.6802 0.4746 0.0365 -0.1017 -0.1310 238 LYS A C 1824 O O . LYS A 238 ? 0.5212 0.6993 0.4968 0.0403 -0.1047 -0.1312 238 LYS A O 1825 C CB . LYS A 238 ? 0.5334 0.7063 0.5053 0.0264 -0.0965 -0.1214 238 LYS A CB 1826 C CG . LYS A 238 ? 0.5483 0.7096 0.5149 0.0246 -0.0931 -0.1147 238 LYS A CG 1827 C CD . LYS A 238 ? 0.5575 0.7270 0.5294 0.0229 -0.0895 -0.1136 238 LYS A CD 1828 C CE . LYS A 238 ? 0.5698 0.7547 0.5471 0.0129 -0.0888 -0.1153 238 LYS A CE 1829 N NZ . LYS A 238 ? 0.5510 0.7433 0.5326 0.0111 -0.0850 -0.1140 238 LYS A NZ 1830 N N . PRO A 239 ? 0.4959 0.7008 0.4857 0.0330 -0.1020 -0.1367 239 PRO A N 1831 C CA . PRO A 239 ? 0.4984 0.7155 0.4930 0.0322 -0.1057 -0.1432 239 PRO A CA 1832 C C . PRO A 239 ? 0.5080 0.7175 0.4957 0.0278 -0.1077 -0.1415 239 PRO A C 1833 O O . PRO A 239 ? 0.5113 0.7151 0.4943 0.0207 -0.1060 -0.1371 239 PRO A O 1834 C CB . PRO A 239 ? 0.5063 0.7447 0.5098 0.0251 -0.1039 -0.1474 239 PRO A CB 1835 C CG . PRO A 239 ? 0.4942 0.7328 0.5002 0.0272 -0.1005 -0.1457 239 PRO A CG 1836 C CD . PRO A 239 ? 0.4892 0.7062 0.4854 0.0292 -0.0986 -0.1375 239 PRO A CD 1837 N N . GLY A 240 ? 0.5235 0.7318 0.5105 0.0323 -0.1118 -0.1448 240 GLY A N 1838 C CA . GLY A 240 ? 0.5452 0.7461 0.5257 0.0291 -0.1144 -0.1440 240 GLY A CA 1839 C C . GLY A 240 ? 0.5408 0.7209 0.5105 0.0330 -0.1143 -0.1386 240 GLY A C 1840 O O . GLY A 240 ? 0.5805 0.7531 0.5444 0.0318 -0.1169 -0.1386 240 GLY A O 1841 N N . ASP A 241 ? 0.5469 0.7183 0.5140 0.0375 -0.1113 -0.1343 241 ASP A N 1842 C CA . ASP A 241 ? 0.5273 0.6811 0.4846 0.0425 -0.1110 -0.1297 241 ASP A CA 1843 C C . ASP A 241 ? 0.5294 0.6809 0.4859 0.0517 -0.1133 -0.1305 241 ASP A C 1844 O O . ASP A 241 ? 0.5218 0.6839 0.4855 0.0543 -0.1156 -0.1347 241 ASP A O 1845 C CB . ASP A 241 ? 0.5266 0.6724 0.4810 0.0414 -0.1065 -0.1240 241 ASP A CB 1846 C CG . ASP A 241 ? 0.5428 0.6723 0.4872 0.0427 -0.1062 -0.1199 241 ASP A CG 1847 O OD1 . ASP A 241 ? 0.5564 0.6797 0.4952 0.0470 -0.1090 -0.1211 241 ASP A OD1 1848 O OD2 . ASP A 241 ? 0.5510 0.6745 0.4932 0.0395 -0.1034 -0.1159 241 ASP A OD2 1849 N N . ILE A 242 ? 0.5277 0.6659 0.4754 0.0563 -0.1132 -0.1267 242 ILE A N 1850 C CA . ILE A 242 ? 0.5331 0.6674 0.4774 0.0640 -0.1159 -0.1263 242 ILE A CA 1851 C C . ILE A 242 ? 0.5201 0.6430 0.4573 0.0682 -0.1132 -0.1201 242 ILE A C 1852 O O . ILE A 242 ? 0.5320 0.6469 0.4631 0.0664 -0.1107 -0.1174 242 ILE A O 1853 C CB . ILE A 242 ? 0.5529 0.6842 0.4917 0.0647 -0.1198 -0.1289 242 ILE A CB 1854 C CG1 . ILE A 242 ? 0.5686 0.7116 0.5141 0.0604 -0.1228 -0.1349 242 ILE A CG1 1855 C CG2 . ILE A 242 ? 0.5815 0.7086 0.5156 0.0721 -0.1226 -0.1275 242 ILE A CG2 1856 C CD1 . ILE A 242 ? 0.6000 0.7405 0.5403 0.0605 -0.1269 -0.1378 242 ILE A CD1 1857 N N . LEU A 243 ? 0.4898 0.6124 0.4282 0.0737 -0.1141 -0.1180 243 LEU A N 1858 C CA . LEU A 243 ? 0.4748 0.5880 0.4060 0.0777 -0.1121 -0.1119 243 LEU A CA 1859 C C . LEU A 243 ? 0.4957 0.6043 0.4187 0.0816 -0.1153 -0.1115 243 LEU A C 1860 O O . LEU A 243 ? 0.5011 0.6139 0.4261 0.0839 -0.1198 -0.1143 243 LEU A O 1861 C CB . LEU A 243 ? 0.4582 0.5731 0.3943 0.0811 -0.1125 -0.1093 243 LEU A CB 1862 C CG . LEU A 243 ? 0.4610 0.5677 0.3909 0.0840 -0.1100 -0.1024 243 LEU A CG 1863 C CD1 . LEU A 243 ? 0.4575 0.5614 0.3867 0.0803 -0.1044 -0.0999 243 LEU A CD1 1864 C CD2 . LEU A 243 ? 0.4578 0.5655 0.3923 0.0876 -0.1126 -0.1001 243 LEU A CD2 1865 N N . LEU A 244 ? 0.5061 0.6070 0.4201 0.0826 -0.1130 -0.1084 244 LEU A N 1866 C CA . LEU A 244 ? 0.5239 0.6212 0.4292 0.0864 -0.1153 -0.1076 244 LEU A CA 1867 C C . LEU A 244 ? 0.5289 0.6213 0.4278 0.0897 -0.1126 -0.1013 244 LEU A C 1868 O O . LEU A 244 ? 0.5112 0.5998 0.4081 0.0884 -0.1083 -0.0991 244 LEU A O 1869 C CB . LEU A 244 ? 0.5447 0.6390 0.4448 0.0844 -0.1157 -0.1115 244 LEU A CB 1870 C CG . LEU A 244 ? 0.5632 0.6553 0.4543 0.0881 -0.1185 -0.1125 244 LEU A CG 1871 C CD1 . LEU A 244 ? 0.5934 0.6910 0.4866 0.0905 -0.1234 -0.1136 244 LEU A CD1 1872 C CD2 . LEU A 244 ? 0.5721 0.6610 0.4598 0.0857 -0.1195 -0.1174 244 LEU A CD2 1873 N N . ILE A 245 ? 0.5233 0.6165 0.4193 0.0934 -0.1154 -0.0982 245 ILE A N 1874 C CA . ILE A 245 ? 0.5292 0.6195 0.4188 0.0961 -0.1136 -0.0917 245 ILE A CA 1875 C C . ILE A 245 ? 0.5548 0.6448 0.4342 0.0988 -0.1155 -0.0912 245 ILE A C 1876 O O . ILE A 245 ? 0.5539 0.6465 0.4326 0.1002 -0.1203 -0.0929 245 ILE A O 1877 C CB . ILE A 245 ? 0.5337 0.6250 0.4280 0.0975 -0.1160 -0.0872 245 ILE A CB 1878 C CG1 . ILE A 245 ? 0.5383 0.6310 0.4429 0.0951 -0.1141 -0.0885 245 ILE A CG1 1879 C CG2 . ILE A 245 ? 0.5351 0.6241 0.4223 0.0993 -0.1144 -0.0796 245 ILE A CG2 1880 C CD1 . ILE A 245 ? 0.5368 0.6305 0.4479 0.0967 -0.1174 -0.0859 245 ILE A CD1 1881 N N . ASN A 246 ? 0.5667 0.6546 0.4386 0.0998 -0.1117 -0.0891 246 ASN A N 1882 C CA . ASN A 246 ? 0.6087 0.6975 0.4703 0.1023 -0.1124 -0.0899 246 ASN A CA 1883 C C . ASN A 246 ? 0.6059 0.6960 0.4613 0.1041 -0.1096 -0.0830 246 ASN A C 1884 O O . ASN A 246 ? 0.6023 0.6905 0.4577 0.1037 -0.1049 -0.0814 246 ASN A O 1885 C CB . ASN A 246 ? 0.6435 0.7293 0.5031 0.1016 -0.1105 -0.0960 246 ASN A CB 1886 C CG . ASN A 246 ? 0.7031 0.7902 0.5532 0.1044 -0.1123 -0.0995 246 ASN A CG 1887 O OD1 . ASN A 246 ? 0.7069 0.7911 0.5535 0.1051 -0.1105 -0.1034 246 ASN A OD1 1888 N ND2 . ASN A 246 ? 0.7755 0.8669 0.6217 0.1060 -0.1161 -0.0985 246 ASN A ND2 1889 N N . SER A 247 ? 0.6060 0.6997 0.4562 0.1056 -0.1126 -0.0786 247 SER A N 1890 C CA . SER A 247 ? 0.5916 0.6880 0.4360 0.1064 -0.1105 -0.0711 247 SER A CA 1891 C C . SER A 247 ? 0.6008 0.7026 0.4362 0.1077 -0.1141 -0.0678 247 SER A C 1892 O O . SER A 247 ? 0.5773 0.6796 0.4131 0.1080 -0.1193 -0.0696 247 SER A O 1893 C CB . SER A 247 ? 0.5967 0.6909 0.4480 0.1047 -0.1111 -0.0649 247 SER A CB 1894 O OG . SER A 247 ? 0.6163 0.7132 0.4621 0.1046 -0.1098 -0.0569 247 SER A OG 1895 N N . THR A 248 ? 0.6018 0.7085 0.4294 0.1083 -0.1113 -0.0628 248 THR A N 1896 C CA . THR A 248 ? 0.6346 0.7481 0.4528 0.1087 -0.1142 -0.0581 248 THR A CA 1897 C C . THR A 248 ? 0.6339 0.7496 0.4508 0.1065 -0.1145 -0.0474 248 THR A C 1898 O O . THR A 248 ? 0.6379 0.7609 0.4461 0.1059 -0.1159 -0.0419 248 THR A O 1899 C CB . THR A 248 ? 0.6577 0.7784 0.4661 0.1109 -0.1109 -0.0619 248 THR A CB 1900 O OG1 . THR A 248 ? 0.6812 0.8026 0.4897 0.1114 -0.1047 -0.0613 248 THR A OG1 1901 C CG2 . THR A 248 ? 0.6720 0.7904 0.4804 0.1129 -0.1120 -0.0723 248 THR A CG2 1902 N N . GLY A 249 ? 0.5976 0.7075 0.4228 0.1050 -0.1134 -0.0445 249 GLY A N 1903 C CA . GLY A 249 ? 0.5837 0.6942 0.4090 0.1026 -0.1139 -0.0346 249 GLY A CA 1904 C C . GLY A 249 ? 0.5695 0.6756 0.4019 0.1017 -0.1093 -0.0339 249 GLY A C 1905 O O . GLY A 249 ? 0.5507 0.6545 0.3868 0.1028 -0.1051 -0.0406 249 GLY A O 1906 N N . ASN A 250 ? 0.5492 0.6541 0.3834 0.0993 -0.1106 -0.0254 250 ASN A N 1907 C CA . ASN A 250 ? 0.5385 0.6404 0.3785 0.0980 -0.1064 -0.0231 250 ASN A CA 1908 C C . ASN A 250 ? 0.5103 0.6046 0.3619 0.0983 -0.1068 -0.0285 250 ASN A C 1909 O O . ASN A 250 ? 0.4992 0.5912 0.3558 0.0973 -0.1029 -0.0280 250 ASN A O 1910 C CB . ASN A 250 ? 0.5316 0.6388 0.3669 0.0989 -0.0988 -0.0251 250 ASN A CB 1911 C CG . ASN A 250 ? 0.5446 0.6622 0.3686 0.0987 -0.0977 -0.0203 250 ASN A CG 1912 O OD1 . ASN A 250 ? 0.5445 0.6670 0.3618 0.1004 -0.0989 -0.0237 250 ASN A OD1 1913 N ND2 . ASN A 250 ? 0.5180 0.6398 0.3399 0.0965 -0.0950 -0.0128 250 ASN A ND2 1914 N N . LEU A 251 ? 0.4987 0.5903 0.3543 0.0994 -0.1114 -0.0337 251 LEU A N 1915 C CA . LEU A 251 ? 0.4938 0.5808 0.3602 0.0996 -0.1121 -0.0396 251 LEU A CA 1916 C C . LEU A 251 ? 0.4896 0.5723 0.3638 0.0987 -0.1170 -0.0354 251 LEU A C 1917 O O . LEU A 251 ? 0.4815 0.5630 0.3551 0.0991 -0.1238 -0.0320 251 LEU A O 1918 C CB . LEU A 251 ? 0.4794 0.5668 0.3471 0.1011 -0.1152 -0.0473 251 LEU A CB 1919 C CG . LEU A 251 ? 0.4846 0.5697 0.3635 0.1009 -0.1162 -0.0540 251 LEU A CG 1920 C CD1 . LEU A 251 ? 0.4551 0.5396 0.3374 0.0994 -0.1096 -0.0572 251 LEU A CD1 1921 C CD2 . LEU A 251 ? 0.4688 0.5556 0.3489 0.1021 -0.1202 -0.0606 251 LEU A CD2 1922 N N . ILE A 252 ? 0.4636 0.5439 0.3449 0.0977 -0.1140 -0.0359 252 ILE A N 1923 C CA . ILE A 252 ? 0.4629 0.5390 0.3535 0.0975 -0.1185 -0.0349 252 ILE A CA 1924 C C . ILE A 252 ? 0.4560 0.5328 0.3556 0.0986 -0.1190 -0.0444 252 ILE A C 1925 O O . ILE A 252 ? 0.4344 0.5124 0.3378 0.0974 -0.1137 -0.0488 252 ILE A O 1926 C CB . ILE A 252 ? 0.4700 0.5443 0.3631 0.0955 -0.1149 -0.0300 252 ILE A CB 1927 C CG1 . ILE A 252 ? 0.4883 0.5640 0.3722 0.0939 -0.1139 -0.0205 252 ILE A CG1 1928 C CG2 . ILE A 252 ? 0.4623 0.5323 0.3656 0.0957 -0.1200 -0.0299 252 ILE A CG2 1929 C CD1 . ILE A 252 ? 0.4872 0.5613 0.3676 0.0936 -0.1218 -0.0140 252 ILE A CD1 1930 N N . ALA A 253 ? 0.4487 0.5255 0.3515 0.1004 -0.1256 -0.0475 253 ALA A N 1931 C CA . ALA A 253 ? 0.4555 0.5354 0.3651 0.1013 -0.1263 -0.0569 253 ALA A CA 1932 C C . ALA A 253 ? 0.4447 0.5249 0.3666 0.1017 -0.1282 -0.0613 253 ALA A C 1933 O O . ALA A 253 ? 0.4325 0.5091 0.3586 0.1026 -0.1325 -0.0577 253 ALA A O 1934 C CB . ALA A 253 ? 0.4534 0.5345 0.3607 0.1034 -0.1325 -0.0589 253 ALA A CB 1935 N N . PRO A 254 ? 0.4535 0.5386 0.3813 0.1009 -0.1254 -0.0694 254 PRO A N 1936 C CA . PRO A 254 ? 0.4488 0.5371 0.3887 0.1014 -0.1274 -0.0749 254 PRO A CA 1937 C C . PRO A 254 ? 0.4544 0.5439 0.4001 0.1049 -0.1359 -0.0785 254 PRO A C 1938 O O . PRO A 254 ? 0.4591 0.5491 0.4002 0.1060 -0.1388 -0.0791 254 PRO A O 1939 C CB . PRO A 254 ? 0.4448 0.5395 0.3875 0.0987 -0.1221 -0.0818 254 PRO A CB 1940 C CG . PRO A 254 ? 0.4491 0.5439 0.3838 0.0986 -0.1221 -0.0826 254 PRO A CG 1941 C CD . PRO A 254 ? 0.4490 0.5378 0.3733 0.0995 -0.1220 -0.0744 254 PRO A CD 1942 N N . ARG A 255 ? 0.4596 0.5497 0.4154 0.1069 -0.1401 -0.0813 255 ARG A N 1943 C CA . ARG A 255 ? 0.4628 0.5547 0.4262 0.1110 -0.1489 -0.0862 255 ARG A CA 1944 C C . ARG A 255 ? 0.4587 0.5614 0.4323 0.1112 -0.1480 -0.0972 255 ARG A C 1945 O O . ARG A 255 ? 0.4392 0.5458 0.4210 0.1149 -0.1546 -0.1032 255 ARG A O 1946 C CB . ARG A 255 ? 0.4709 0.5564 0.4398 0.1138 -0.1556 -0.0831 255 ARG A CB 1947 C CG . ARG A 255 ? 0.4890 0.5646 0.4487 0.1131 -0.1581 -0.0717 255 ARG A CG 1948 C CD . ARG A 255 ? 0.5048 0.5733 0.4710 0.1159 -0.1672 -0.0692 255 ARG A CD 1949 N NE . ARG A 255 ? 0.5299 0.5896 0.4868 0.1142 -0.1700 -0.0574 255 ARG A NE 1950 C CZ . ARG A 255 ? 0.5414 0.5976 0.4921 0.1149 -0.1761 -0.0524 255 ARG A CZ 1951 N NH1 . ARG A 255 ? 0.5371 0.5969 0.4902 0.1178 -0.1806 -0.0582 255 ARG A NH1 1952 N NH2 . ARG A 255 ? 0.5533 0.6032 0.4952 0.1123 -0.1779 -0.0411 255 ARG A NH2 1953 N N . GLY A 256 ? 0.4378 0.5459 0.4111 0.1072 -0.1400 -0.0996 256 GLY A N 1954 C CA . GLY A 256 ? 0.4329 0.5527 0.4157 0.1060 -0.1383 -0.1091 256 GLY A CA 1955 C C . GLY A 256 ? 0.4115 0.5342 0.3934 0.1010 -0.1298 -0.1085 256 GLY A C 1956 O O . GLY A 256 ? 0.4102 0.5260 0.3830 0.0985 -0.1251 -0.1017 256 GLY A O 1957 N N . TYR A 257 ? 0.4002 0.5336 0.3914 0.0995 -0.1282 -0.1157 257 TYR A N 1958 C CA . TYR A 257 ? 0.3985 0.5361 0.3893 0.0940 -0.1206 -0.1155 257 TYR A CA 1959 C C . TYR A 257 ? 0.3859 0.5295 0.3860 0.0943 -0.1202 -0.1191 257 TYR A C 1960 O O . TYR A 257 ? 0.3884 0.5376 0.3977 0.0984 -0.1256 -0.1253 257 TYR A O 1961 C CB . TYR A 257 ? 0.4050 0.5524 0.3963 0.0893 -0.1175 -0.1206 257 TYR A CB 1962 C CG . TYR A 257 ? 0.4202 0.5816 0.4221 0.0904 -0.1212 -0.1302 257 TYR A CG 1963 C CD1 . TYR A 257 ? 0.4157 0.5897 0.4266 0.0883 -0.1192 -0.1362 257 TYR A CD1 1964 C CD2 . TYR A 257 ? 0.4319 0.5951 0.4347 0.0937 -0.1268 -0.1337 257 TYR A CD2 1965 C CE1 . TYR A 257 ? 0.4207 0.6098 0.4417 0.0895 -0.1225 -0.1457 257 TYR A CE1 1966 C CE2 . TYR A 257 ? 0.4487 0.6259 0.4617 0.0951 -0.1303 -0.1430 257 TYR A CE2 1967 C CZ . TYR A 257 ? 0.4420 0.6326 0.4643 0.0931 -0.1281 -0.1492 257 TYR A CZ 1968 O OH . TYR A 257 ? 0.4465 0.6532 0.4793 0.0945 -0.1313 -0.1590 257 TYR A OH 1969 N N . PHE A 258 ? 0.3715 0.5143 0.3692 0.0901 -0.1139 -0.1157 258 PHE A N 1970 C CA . PHE A 258 ? 0.3692 0.5198 0.3752 0.0892 -0.1124 -0.1195 258 PHE A CA 1971 C C . PHE A 258 ? 0.3923 0.5578 0.4026 0.0840 -0.1088 -0.1261 258 PHE A C 1972 O O . PHE A 258 ? 0.3937 0.5593 0.3981 0.0794 -0.1053 -0.1242 258 PHE A O 1973 C CB . PHE A 258 ? 0.3518 0.4944 0.3529 0.0869 -0.1077 -0.1121 258 PHE A CB 1974 C CG . PHE A 258 ? 0.3406 0.4706 0.3387 0.0912 -0.1114 -0.1057 258 PHE A CG 1975 C CD1 . PHE A 258 ? 0.3466 0.4761 0.3522 0.0948 -0.1158 -0.1078 258 PHE A CD1 1976 C CD2 . PHE A 258 ? 0.3566 0.4757 0.3443 0.0915 -0.1110 -0.0979 258 PHE A CD2 1977 C CE1 . PHE A 258 ? 0.3514 0.4689 0.3541 0.0979 -0.1200 -0.1012 258 PHE A CE1 1978 C CE2 . PHE A 258 ? 0.3581 0.4669 0.3426 0.0944 -0.1145 -0.0912 258 PHE A CE2 1979 C CZ . PHE A 258 ? 0.3560 0.4635 0.3480 0.0973 -0.1191 -0.0925 258 PHE A CZ 1980 N N . LYS A 259 ? 0.4118 0.5902 0.4328 0.0849 -0.1102 -0.1340 259 LYS A N 1981 C CA . LYS A 259 ? 0.4579 0.6526 0.4835 0.0791 -0.1062 -0.1397 259 LYS A CA 1982 C C . LYS A 259 ? 0.4598 0.6509 0.4804 0.0735 -0.0997 -0.1335 259 LYS A C 1983 O O . LYS A 259 ? 0.4685 0.6500 0.4872 0.0757 -0.0992 -0.1286 259 LYS A O 1984 C CB . LYS A 259 ? 0.4917 0.7019 0.5299 0.0821 -0.1093 -0.1499 259 LYS A CB 1985 C CG . LYS A 259 ? 0.5111 0.7261 0.5554 0.0880 -0.1163 -0.1569 259 LYS A CG 1986 C CD . LYS A 259 ? 0.5558 0.7851 0.6015 0.0834 -0.1149 -0.1619 259 LYS A CD 1987 C CE . LYS A 259 ? 0.5591 0.8117 0.6167 0.0825 -0.1150 -0.1731 259 LYS A CE 1988 N NZ . LYS A 259 ? 0.5653 0.8255 0.6319 0.0898 -0.1224 -0.1821 259 LYS A NZ 1989 N N . ILE A 260 ? 0.4384 0.6361 0.4563 0.0662 -0.0952 -0.1329 260 ILE A N 1990 C CA . ILE A 260 ? 0.4428 0.6389 0.4570 0.0604 -0.0894 -0.1277 260 ILE A CA 1991 C C . ILE A 260 ? 0.4507 0.6667 0.4720 0.0544 -0.0872 -0.1341 260 ILE A C 1992 O O . ILE A 260 ? 0.4667 0.6932 0.4898 0.0508 -0.0877 -0.1382 260 ILE A O 1993 C CB . ILE A 260 ? 0.4546 0.6377 0.4578 0.0570 -0.0866 -0.1195 260 ILE A CB 1994 C CG1 . ILE A 260 ? 0.4501 0.6312 0.4500 0.0514 -0.0813 -0.1142 260 ILE A CG1 1995 C CG2 . ILE A 260 ? 0.4626 0.6500 0.4638 0.0532 -0.0875 -0.1218 260 ILE A CG2 1996 C CD1 . ILE A 260 ? 0.4398 0.6050 0.4293 0.0507 -0.0793 -0.1058 260 ILE A CD1 1997 N N . ARG A 261 ? 0.4341 0.6564 0.4599 0.0535 -0.0850 -0.1353 261 ARG A N 1998 C CA . ARG A 261 ? 0.4518 0.6950 0.4846 0.0480 -0.0828 -0.1417 261 ARG A CA 1999 C C . ARG A 261 ? 0.4331 0.6752 0.4609 0.0402 -0.0773 -0.1352 261 ARG A C 2000 O O . ARG A 261 ? 0.4173 0.6429 0.4378 0.0407 -0.0756 -0.1269 261 ARG A O 2001 C CB . ARG A 261 ? 0.4792 0.7330 0.5224 0.0537 -0.0855 -0.1502 261 ARG A CB 2002 C CG . ARG A 261 ? 0.5169 0.7708 0.5658 0.0621 -0.0921 -0.1568 261 ARG A CG 2003 C CD . ARG A 261 ? 0.5717 0.8396 0.6325 0.0675 -0.0955 -0.1674 261 ARG A CD 2004 N NE . ARG A 261 ? 0.6272 0.8958 0.6942 0.0755 -0.1026 -0.1742 261 ARG A NE 2005 C CZ . ARG A 261 ? 0.6882 0.9700 0.7592 0.0750 -0.1045 -0.1808 261 ARG A CZ 2006 N NH1 . ARG A 261 ? 0.6995 0.9952 0.7689 0.0664 -0.0999 -0.1812 261 ARG A NH1 2007 N NH2 . ARG A 261 ? 0.7086 0.9898 0.7853 0.0830 -0.1115 -0.1867 261 ARG A NH2 2008 N N . SER A 262 ? 0.4463 0.7067 0.4779 0.0328 -0.0747 -0.1387 262 SER A N 2009 C CA . SER A 262 ? 0.4573 0.7189 0.4857 0.0256 -0.0700 -0.1332 262 SER A CA 2010 C C . SER A 262 ? 0.4394 0.7196 0.4763 0.0249 -0.0689 -0.1401 262 SER A C 2011 O O . SER A 262 ? 0.4293 0.7282 0.4744 0.0258 -0.0706 -0.1497 262 SER A O 2012 C CB . SER A 262 ? 0.4911 0.7565 0.5145 0.0154 -0.0679 -0.1291 262 SER A CB 2013 O OG . SER A 262 ? 0.5155 0.8045 0.5454 0.0097 -0.0678 -0.1361 262 SER A OG 2014 N N . GLY A 263 ? 0.4444 0.4728 0.4841 -0.0024 -0.0711 -0.0395 263 GLY A N 2015 C CA . GLY A 263 ? 0.4389 0.4732 0.4841 0.0002 -0.0721 -0.0424 263 GLY A CA 2016 C C . GLY A 263 ? 0.4292 0.4541 0.4728 0.0008 -0.0706 -0.0382 263 GLY A C 2017 O O . GLY A 263 ? 0.4477 0.4643 0.4861 -0.0020 -0.0674 -0.0337 263 GLY A O 2018 N N . LYS A 264 ? 0.3889 0.4152 0.4367 0.0046 -0.0732 -0.0399 264 LYS A N 2019 C CA . LYS A 264 ? 0.3836 0.4041 0.4309 0.0047 -0.0717 -0.0370 264 LYS A CA 2020 C C . LYS A 264 ? 0.3302 0.3403 0.3763 0.0078 -0.0747 -0.0329 264 LYS A C 2021 O O . LYS A 264 ? 0.3016 0.3081 0.3483 0.0088 -0.0750 -0.0313 264 LYS A O 2022 C CB . LYS A 264 ? 0.4264 0.4550 0.4786 0.0063 -0.0723 -0.0414 264 LYS A CB 2023 C CG . LYS A 264 ? 0.5019 0.5428 0.5559 0.0031 -0.0697 -0.0461 264 LYS A CG 2024 C CD . LYS A 264 ? 0.5415 0.5806 0.5903 -0.0032 -0.0645 -0.0437 264 LYS A CD 2025 C CE . LYS A 264 ? 0.5948 0.6458 0.6447 -0.0073 -0.0620 -0.0483 264 LYS A CE 2026 N NZ . LYS A 264 ? 0.6351 0.6934 0.6847 -0.0093 -0.0626 -0.0509 264 LYS A NZ 2027 N N . SER A 265 ? 0.2946 0.2999 0.3384 0.0090 -0.0771 -0.0312 265 SER A N 2028 C CA . SER A 265 ? 0.2812 0.2770 0.3233 0.0115 -0.0805 -0.0277 265 SER A CA 2029 C C . SER A 265 ? 0.2764 0.2641 0.3144 0.0088 -0.0772 -0.0216 265 SER A C 2030 O O . SER A 265 ? 0.2655 0.2533 0.3009 0.0054 -0.0727 -0.0199 265 SER A O 2031 C CB . SER A 265 ? 0.2947 0.2884 0.3356 0.0139 -0.0848 -0.0283 265 SER A CB 2032 O OG . SER A 265 ? 0.2859 0.2874 0.3309 0.0176 -0.0885 -0.0340 265 SER A OG 2033 N N . SER A 266 ? 0.2699 0.2507 0.3070 0.0102 -0.0796 -0.0184 266 SER A N 2034 C CA . SER A 266 ? 0.2752 0.2496 0.3088 0.0078 -0.0768 -0.0126 266 SER A CA 2035 C C . SER A 266 ? 0.2735 0.2401 0.3050 0.0091 -0.0809 -0.0093 266 SER A C 2036 O O . SER A 266 ? 0.2740 0.2387 0.3058 0.0119 -0.0861 -0.0114 266 SER A O 2037 C CB . SER A 266 ? 0.2826 0.2592 0.3176 0.0062 -0.0733 -0.0116 266 SER A CB 2038 O OG . SER A 266 ? 0.2971 0.2694 0.3289 0.0041 -0.0698 -0.0063 266 SER A OG 2039 N N . ILE A 267 ? 0.2721 0.2345 0.3012 0.0071 -0.0787 -0.0042 267 ILE A N 2040 C CA . ILE A 267 ? 0.2808 0.2362 0.3071 0.0069 -0.0818 -0.0001 267 ILE A CA 2041 C C . ILE A 267 ? 0.2950 0.2501 0.3217 0.0052 -0.0797 0.0034 267 ILE A C 2042 O O . ILE A 267 ? 0.2806 0.2395 0.3082 0.0038 -0.0748 0.0043 267 ILE A O 2043 C CB . ILE A 267 ? 0.2905 0.2420 0.3126 0.0058 -0.0810 0.0028 267 ILE A CB 2044 C CG1 . ILE A 267 ? 0.2953 0.2394 0.3137 0.0052 -0.0848 0.0066 267 ILE A CG1 2045 C CG2 . ILE A 267 ? 0.2826 0.2358 0.3030 0.0036 -0.0749 0.0056 267 ILE A CG2 2046 C CD1 . ILE A 267 ? 0.2986 0.2386 0.3128 0.0048 -0.0856 0.0081 267 ILE A CD1 2047 N N . MET A 268 ? 0.2984 0.2488 0.3240 0.0051 -0.0835 0.0053 268 MET A N 2048 C CA . MET A 268 ? 0.3098 0.2603 0.3358 0.0031 -0.0823 0.0088 268 MET A CA 2049 C C . MET A 268 ? 0.3157 0.2597 0.3376 0.0012 -0.0855 0.0133 268 MET A C 2050 O O . MET A 268 ? 0.3228 0.2608 0.3420 0.0023 -0.0907 0.0123 268 MET A O 2051 C CB . MET A 268 ? 0.3133 0.2656 0.3424 0.0044 -0.0841 0.0055 268 MET A CB 2052 C CG . MET A 268 ? 0.3238 0.2776 0.3539 0.0022 -0.0821 0.0086 268 MET A CG 2053 S SD . MET A 268 ? 0.3264 0.2814 0.3593 0.0037 -0.0846 0.0045 268 MET A SD 2054 C CE . MET A 268 ? 0.3039 0.2673 0.3408 0.0049 -0.0800 -0.0001 268 MET A CE 2055 N N . ARG A 269 ? 0.3037 0.2491 0.3249 -0.0014 -0.0826 0.0181 269 ARG A N 2056 C CA . ARG A 269 ? 0.3200 0.2607 0.3374 -0.0043 -0.0853 0.0227 269 ARG A CA 2057 C C . ARG A 269 ? 0.3210 0.2606 0.3392 -0.0053 -0.0880 0.0230 269 ARG A C 2058 O O . ARG A 269 ? 0.3054 0.2504 0.3270 -0.0058 -0.0848 0.0234 269 ARG A O 2059 C CB . ARG A 269 ? 0.3379 0.2823 0.3545 -0.0067 -0.0807 0.0278 269 ARG A CB 2060 C CG . ARG A 269 ? 0.3485 0.2934 0.3635 -0.0057 -0.0777 0.0277 269 ARG A CG 2061 C CD . ARG A 269 ? 0.3590 0.3068 0.3720 -0.0077 -0.0738 0.0327 269 ARG A CD 2062 N NE . ARG A 269 ? 0.3688 0.3161 0.3794 -0.0065 -0.0710 0.0324 269 ARG A NE 2063 C CZ . ARG A 269 ? 0.3806 0.3313 0.3922 -0.0047 -0.0663 0.0309 269 ARG A CZ 2064 N NH1 . ARG A 269 ? 0.3796 0.3345 0.3944 -0.0037 -0.0638 0.0296 269 ARG A NH1 2065 N NH2 . ARG A 269 ? 0.3826 0.3316 0.3909 -0.0040 -0.0643 0.0308 269 ARG A NH2 2066 N N . SER A 270 ? 0.3216 0.2534 0.3360 -0.0057 -0.0940 0.0228 270 SER A N 2067 C CA . SER A 270 ? 0.3372 0.2662 0.3508 -0.0070 -0.0972 0.0232 270 SER A CA 2068 C C . SER A 270 ? 0.3645 0.2833 0.3713 -0.0089 -0.1035 0.0251 270 SER A C 2069 O O . SER A 270 ? 0.3602 0.2729 0.3636 -0.0071 -0.1068 0.0234 270 SER A O 2070 C CB . SER A 270 ? 0.3328 0.2629 0.3498 -0.0032 -0.0984 0.0174 270 SER A CB 2071 O OG . SER A 270 ? 0.3448 0.2707 0.3600 -0.0041 -0.1021 0.0174 270 SER A OG 2072 N N . ASP A 271 ? 0.3748 0.2911 0.3791 -0.0127 -0.1054 0.0284 271 ASP A N 2073 C CA . ASP A 271 ? 0.4169 0.3215 0.4134 -0.0146 -0.1123 0.0295 271 ASP A CA 2074 C C . ASP A 271 ? 0.4261 0.3247 0.4210 -0.0125 -0.1170 0.0259 271 ASP A C 2075 O O . ASP A 271 ? 0.4390 0.3268 0.4264 -0.0145 -0.1229 0.0270 271 ASP A O 2076 C CB . ASP A 271 ? 0.4533 0.3577 0.4459 -0.0213 -0.1122 0.0361 271 ASP A CB 2077 C CG . ASP A 271 ? 0.4751 0.3829 0.4672 -0.0230 -0.1090 0.0392 271 ASP A CG 2078 O OD1 . ASP A 271 ? 0.4762 0.3809 0.4674 -0.0197 -0.1098 0.0366 271 ASP A OD1 2079 O OD2 . ASP A 271 ? 0.5025 0.4168 0.4952 -0.0272 -0.1055 0.0440 271 ASP A OD2 2080 N N . ALA A 272 ? 0.3965 0.3012 0.3975 -0.0085 -0.1145 0.0214 272 ALA A N 2081 C CA . ALA A 272 ? 0.4049 0.3049 0.4047 -0.0061 -0.1184 0.0177 272 ALA A CA 2082 C C . ALA A 272 ? 0.4124 0.3022 0.4069 -0.0016 -0.1248 0.0136 272 ALA A C 2083 O O . ALA A 272 ? 0.4013 0.2931 0.3976 0.0018 -0.1242 0.0110 272 ALA A O 2084 C CB . ALA A 272 ? 0.3930 0.3027 0.4005 -0.0030 -0.1139 0.0137 272 ALA A CB 2085 N N . PRO A 273 ? 0.4379 0.3165 0.4253 -0.0015 -0.1311 0.0130 273 PRO A N 2086 C CA . PRO A 273 ? 0.4577 0.3265 0.4398 0.0037 -0.1373 0.0087 273 PRO A CA 2087 C C . PRO A 273 ? 0.4521 0.3281 0.4407 0.0108 -0.1360 0.0017 273 PRO A C 2088 O O . PRO A 273 ? 0.4186 0.3037 0.4137 0.0111 -0.1317 0.0000 273 PRO A O 2089 C CB . PRO A 273 ? 0.4838 0.3389 0.4564 0.0021 -0.1439 0.0096 273 PRO A CB 2090 C CG . PRO A 273 ? 0.5003 0.3610 0.4760 -0.0022 -0.1405 0.0122 273 PRO A CG 2091 C CD . PRO A 273 ? 0.4687 0.3428 0.4523 -0.0058 -0.1329 0.0158 273 PRO A CD 2092 N N . ILE A 274 ? 0.4647 0.3371 0.4515 0.0164 -0.1397 -0.0024 274 ILE A N 2093 C CA . ILE A 274 ? 0.4748 0.3553 0.4678 0.0231 -0.1387 -0.0092 274 ILE A CA 2094 C C . ILE A 274 ? 0.5083 0.3805 0.4964 0.0279 -0.1447 -0.0135 274 ILE A C 2095 O O . ILE A 274 ? 0.5145 0.3728 0.4933 0.0292 -0.1515 -0.0131 274 ILE A O 2096 C CB . ILE A 274 ? 0.4918 0.3757 0.4869 0.0266 -0.1388 -0.0116 274 ILE A CB 2097 C CG1 . ILE A 274 ? 0.4934 0.3876 0.4945 0.0222 -0.1316 -0.0081 274 ILE A CG1 2098 C CG2 . ILE A 274 ? 0.4863 0.3781 0.4867 0.0339 -0.1392 -0.0191 274 ILE A CG2 2099 C CD1 . ILE A 274 ? 0.5055 0.3984 0.5051 0.0229 -0.1325 -0.0075 274 ILE A CD1 2100 N N . GLY A 275 ? 0.4931 0.3730 0.4866 0.0301 -0.1422 -0.0173 275 GLY A N 2101 C CA . GLY A 275 ? 0.5085 0.3814 0.4975 0.0349 -0.1473 -0.0217 275 GLY A CA 2102 C C . GLY A 275 ? 0.5095 0.3897 0.5029 0.0433 -0.1481 -0.0295 275 GLY A C 2103 O O . GLY A 275 ? 0.4508 0.3449 0.4528 0.0443 -0.1431 -0.0318 275 GLY A O 2104 N N . LYS A 276 ? 0.5180 0.3892 0.5052 0.0492 -0.1543 -0.0337 276 LYS A N 2105 C CA . LYS A 276 ? 0.5363 0.4154 0.5276 0.0578 -0.1553 -0.0416 276 LYS A CA 2106 C C . LYS A 276 ? 0.5210 0.4088 0.5175 0.0579 -0.1514 -0.0445 276 LYS A C 2107 O O . LYS A 276 ? 0.5387 0.4182 0.5295 0.0598 -0.1549 -0.0461 276 LYS A O 2108 C CB . LYS A 276 ? 0.5815 0.4468 0.5633 0.0652 -0.1640 -0.0451 276 LYS A CB 2109 C CG . LYS A 276 ? 0.6235 0.4811 0.6005 0.0651 -0.1677 -0.0424 276 LYS A CG 2110 C CD . LYS A 276 ? 0.6675 0.5126 0.6354 0.0736 -0.1764 -0.0466 276 LYS A CD 2111 C CE . LYS A 276 ? 0.6957 0.5294 0.6565 0.0716 -0.1805 -0.0425 276 LYS A CE 2112 N NZ . LYS A 276 ? 0.7277 0.5744 0.6970 0.0704 -0.1761 -0.0419 276 LYS A NZ 2113 N N . CYS A 277 ? 0.4849 0.3888 0.4914 0.0553 -0.1441 -0.0450 277 CYS A N 2114 C CA . CYS A 277 ? 0.4760 0.3888 0.4876 0.0536 -0.1394 -0.0467 277 CYS A CA 2115 C C . CYS A 277 ? 0.4273 0.3577 0.4490 0.0525 -0.1326 -0.0485 277 CYS A C 2116 O O . CYS A 277 ? 0.4126 0.3464 0.4364 0.0524 -0.1319 -0.0477 277 CYS A O 2117 C CB . CYS A 277 ? 0.5135 0.4203 0.5224 0.0460 -0.1375 -0.0403 277 CYS A CB 2118 S SG . CYS A 277 ? 0.5917 0.4982 0.6016 0.0372 -0.1335 -0.0317 277 CYS A SG 2119 N N . ASN A 278 ? 0.3827 0.3233 0.4098 0.0511 -0.1278 -0.0506 278 ASN A N 2120 C CA . ASN A 278 ? 0.3735 0.3305 0.4092 0.0503 -0.1219 -0.0533 278 ASN A CA 2121 C C . ASN A 278 ? 0.3641 0.3259 0.4030 0.0431 -0.1155 -0.0493 278 ASN A C 2122 O O . ASN A 278 ? 0.3386 0.2992 0.3766 0.0422 -0.1150 -0.0497 278 ASN A O 2123 C CB . ASN A 278 ? 0.3757 0.3421 0.4145 0.0569 -0.1228 -0.0613 278 ASN A CB 2124 C CG . ASN A 278 ? 0.3849 0.3685 0.4316 0.0566 -0.1178 -0.0649 278 ASN A CG 2125 O OD1 . ASN A 278 ? 0.3968 0.3876 0.4475 0.0506 -0.1118 -0.0625 278 ASN A OD1 2126 N ND2 . ASN A 278 ? 0.3798 0.3703 0.4286 0.0631 -0.1205 -0.0706 278 ASN A ND2 2127 N N . SER A 279 ? 0.3628 0.3291 0.4047 0.0385 -0.1110 -0.0456 279 SER A N 2128 C CA . SER A 279 ? 0.3740 0.3449 0.4186 0.0323 -0.1050 -0.0419 279 SER A CA 2129 C C . SER A 279 ? 0.3549 0.3350 0.4038 0.0296 -0.0999 -0.0413 279 SER A C 2130 O O . SER A 279 ? 0.3380 0.3159 0.3860 0.0298 -0.1009 -0.0395 279 SER A O 2131 C CB . SER A 279 ? 0.3959 0.3560 0.4359 0.0279 -0.1060 -0.0351 279 SER A CB 2132 O OG . SER A 279 ? 0.4276 0.3921 0.4701 0.0225 -0.1004 -0.0314 279 SER A OG 2133 N N . GLU A 280 ? 0.3465 0.3362 0.3992 0.0270 -0.0947 -0.0428 280 GLU A N 2134 C CA . GLU A 280 ? 0.3504 0.3483 0.4061 0.0242 -0.0900 -0.0426 280 GLU A CA 2135 C C . GLU A 280 ? 0.3356 0.3287 0.3894 0.0194 -0.0870 -0.0358 280 GLU A C 2136 O O . GLU A 280 ? 0.3292 0.3253 0.3836 0.0182 -0.0849 -0.0351 280 GLU A O 2137 C CB . GLU A 280 ? 0.3815 0.3899 0.4405 0.0222 -0.0854 -0.0461 280 GLU A CB 2138 C CG . GLU A 280 ? 0.4126 0.4294 0.4743 0.0266 -0.0872 -0.0534 280 GLU A CG 2139 C CD . GLU A 280 ? 0.4588 0.4843 0.5233 0.0289 -0.0875 -0.0574 280 GLU A CD 2140 O OE1 . GLU A 280 ? 0.4730 0.4988 0.5373 0.0261 -0.0855 -0.0546 280 GLU A OE1 2141 O OE2 . GLU A 280 ? 0.4791 0.5112 0.5458 0.0337 -0.0900 -0.0633 280 GLU A OE2 2142 N N . CYS A 281 ? 0.3207 0.3074 0.3724 0.0169 -0.0867 -0.0312 281 CYS A N 2143 C CA . CYS A 281 ? 0.3007 0.2845 0.3509 0.0127 -0.0835 -0.0250 281 CYS A CA 2144 C C . CYS A 281 ? 0.2901 0.2646 0.3368 0.0125 -0.0870 -0.0202 281 CYS A C 2145 O O . CYS A 281 ? 0.3049 0.2731 0.3492 0.0130 -0.0907 -0.0191 281 CYS A O 2146 C CB . CYS A 281 ? 0.3164 0.3013 0.3669 0.0095 -0.0803 -0.0229 281 CYS A CB 2147 S SG . CYS A 281 ? 0.3127 0.2953 0.3616 0.0054 -0.0763 -0.0157 281 CYS A SG 2148 N N . ILE A 282 ? 0.2757 0.2492 0.3214 0.0116 -0.0859 -0.0176 282 ILE A N 2149 C CA . ILE A 282 ? 0.2850 0.2504 0.3271 0.0108 -0.0887 -0.0129 282 ILE A CA 2150 C C . ILE A 282 ? 0.2765 0.2420 0.3179 0.0068 -0.0845 -0.0069 282 ILE A C 2151 O O . ILE A 282 ? 0.2513 0.2217 0.2940 0.0057 -0.0799 -0.0066 282 ILE A O 2152 C CB . ILE A 282 ? 0.2846 0.2483 0.3255 0.0132 -0.0912 -0.0143 282 ILE A CB 2153 C CG1 . ILE A 282 ? 0.2986 0.2630 0.3403 0.0180 -0.0955 -0.0204 282 ILE A CG1 2154 C CG2 . ILE A 282 ? 0.2907 0.2457 0.3271 0.0117 -0.0939 -0.0091 282 ILE A CG2 2155 C CD1 . ILE A 282 ? 0.3109 0.2751 0.3520 0.0209 -0.0981 -0.0227 282 ILE A CD1 2156 N N . THR A 283 ? 0.2782 0.2384 0.3171 0.0048 -0.0863 -0.0023 283 THR A N 2157 C CA . THR A 283 ? 0.2818 0.2424 0.3198 0.0015 -0.0831 0.0035 283 THR A CA 2158 C C . THR A 283 ? 0.2973 0.2510 0.3313 0.0004 -0.0869 0.0072 283 THR A C 2159 O O . THR A 283 ? 0.3023 0.2498 0.3337 0.0018 -0.0922 0.0056 283 THR A O 2160 C CB . THR A 283 ? 0.2913 0.2540 0.3302 -0.0008 -0.0810 0.0063 283 THR A CB 2161 O OG1 . THR A 283 ? 0.2848 0.2421 0.3212 -0.0023 -0.0853 0.0086 283 THR A OG1 2162 C CG2 . THR A 283 ? 0.2860 0.2538 0.3279 0.0000 -0.0788 0.0021 283 THR A CG2 2163 N N . PRO A 284 ? 0.2877 0.2421 0.3206 -0.0020 -0.0843 0.0123 284 PRO A N 2164 C CA . PRO A 284 ? 0.3018 0.2503 0.3304 -0.0040 -0.0877 0.0163 284 PRO A CA 2165 C C . PRO A 284 ? 0.3301 0.2734 0.3560 -0.0062 -0.0920 0.0182 284 PRO A C 2166 O O . PRO A 284 ? 0.3310 0.2672 0.3522 -0.0075 -0.0964 0.0200 284 PRO A O 2167 C CB . PRO A 284 ? 0.3066 0.2594 0.3354 -0.0063 -0.0831 0.0212 284 PRO A CB 2168 C CG . PRO A 284 ? 0.2970 0.2554 0.3288 -0.0043 -0.0781 0.0187 284 PRO A CG 2169 C CD . PRO A 284 ? 0.2912 0.2515 0.3257 -0.0026 -0.0784 0.0140 284 PRO A CD 2170 N N . ASN A 285 ? 0.3312 0.2776 0.3593 -0.0070 -0.0909 0.0181 285 ASN A N 2171 C CA . ASN A 285 ? 0.3697 0.3111 0.3948 -0.0094 -0.0949 0.0197 285 ASN A CA 2172 C C . ASN A 285 ? 0.3598 0.2941 0.3825 -0.0065 -0.1002 0.0148 285 ASN A C 2173 O O . ASN A 285 ? 0.3893 0.3171 0.4079 -0.0082 -0.1044 0.0159 285 ASN A O 2174 C CB . ASN A 285 ? 0.4198 0.3673 0.4483 -0.0109 -0.0918 0.0207 285 ASN A CB 2175 C CG . ASN A 285 ? 0.5059 0.4590 0.5353 -0.0145 -0.0884 0.0266 285 ASN A CG 2176 O OD1 . ASN A 285 ? 0.7044 0.6551 0.7308 -0.0182 -0.0908 0.0308 285 ASN A OD1 2177 N ND2 . ASN A 285 ? 0.6014 0.5617 0.6344 -0.0134 -0.0831 0.0269 285 ASN A ND2 2178 N N . GLY A 286 ? 0.3407 0.2764 0.3655 -0.0020 -0.1000 0.0095 286 GLY A N 2179 C CA . GLY A 286 ? 0.3397 0.2711 0.3633 0.0019 -0.1042 0.0040 286 GLY A CA 2180 C C . GLY A 286 ? 0.3373 0.2771 0.3665 0.0047 -0.1007 -0.0010 286 GLY A C 2181 O O . GLY A 286 ? 0.3251 0.2727 0.3584 0.0032 -0.0951 0.0000 286 GLY A O 2182 N N . SER A 287 ? 0.3335 0.2716 0.3624 0.0090 -0.1039 -0.0066 287 SER A N 2183 C CA . SER A 287 ? 0.3300 0.2766 0.3639 0.0114 -0.1008 -0.0117 287 SER A CA 2184 C C . SER A 287 ? 0.3212 0.2697 0.3561 0.0091 -0.0991 -0.0109 287 SER A C 2185 O O . SER A 287 ? 0.3276 0.2695 0.3588 0.0071 -0.1020 -0.0082 287 SER A O 2186 C CB . SER A 287 ? 0.3360 0.2815 0.3694 0.0170 -0.1049 -0.0181 287 SER A CB 2187 O OG . SER A 287 ? 0.3543 0.2989 0.3871 0.0193 -0.1065 -0.0191 287 SER A OG 2188 N N . ILE A 288 ? 0.3115 0.2686 0.3508 0.0089 -0.0944 -0.0132 288 ILE A N 2189 C CA . ILE A 288 ? 0.3233 0.2824 0.3635 0.0069 -0.0926 -0.0129 288 ILE A CA 2190 C C . ILE A 288 ? 0.3274 0.2928 0.3705 0.0095 -0.0913 -0.0192 288 ILE A C 2191 O O . ILE A 288 ? 0.3478 0.3194 0.3937 0.0114 -0.0893 -0.0227 288 ILE A O 2192 C CB . ILE A 288 ? 0.3173 0.2808 0.3593 0.0027 -0.0875 -0.0079 288 ILE A CB 2193 C CG1 . ILE A 288 ? 0.3116 0.2823 0.3567 0.0030 -0.0825 -0.0095 288 ILE A CG1 2194 C CG2 . ILE A 288 ? 0.3283 0.2872 0.3677 0.0000 -0.0885 -0.0016 288 ILE A CG2 2195 C CD1 . ILE A 288 ? 0.3090 0.2835 0.3551 -0.0001 -0.0775 -0.0055 288 ILE A CD1 2196 N N . PRO A 289 ? 0.3543 0.3187 0.3967 0.0094 -0.0923 -0.0207 289 PRO A N 2197 C CA . PRO A 289 ? 0.3640 0.3355 0.4091 0.0110 -0.0901 -0.0262 289 PRO A CA 2198 C C . PRO A 289 ? 0.3611 0.3413 0.4098 0.0082 -0.0839 -0.0258 289 PRO A C 2199 O O . PRO A 289 ? 0.3529 0.3323 0.4013 0.0047 -0.0813 -0.0205 289 PRO A O 2200 C CB . PRO A 289 ? 0.3783 0.3461 0.4213 0.0097 -0.0916 -0.0257 289 PRO A CB 2201 C CG . PRO A 289 ? 0.3950 0.3526 0.4334 0.0083 -0.0959 -0.0211 289 PRO A CG 2202 C CD . PRO A 289 ? 0.3793 0.3360 0.4178 0.0071 -0.0952 -0.0169 289 PRO A CD 2203 N N . ASN A 290 ? 0.3503 0.3384 0.4017 0.0098 -0.0819 -0.0312 290 ASN A N 2204 C CA . ASN A 290 ? 0.3570 0.3524 0.4104 0.0069 -0.0764 -0.0313 290 ASN A CA 2205 C C . ASN A 290 ? 0.3543 0.3555 0.4087 0.0056 -0.0738 -0.0349 290 ASN A C 2206 O O . ASN A 290 ? 0.3693 0.3777 0.4251 0.0039 -0.0700 -0.0371 290 ASN A O 2207 C CB . ASN A 290 ? 0.3584 0.3586 0.4135 0.0082 -0.0754 -0.0336 290 ASN A CB 2208 C CG . ASN A 290 ? 0.3781 0.3845 0.4353 0.0120 -0.0773 -0.0405 290 ASN A CG 2209 O OD1 . ASN A 290 ? 0.3694 0.3752 0.4264 0.0146 -0.0799 -0.0437 290 ASN A OD1 2210 N ND2 . ASN A 290 ? 0.3581 0.3707 0.4171 0.0126 -0.0760 -0.0430 290 ASN A ND2 2211 N N . ASP A 291 ? 0.3491 0.3469 0.4023 0.0060 -0.0760 -0.0352 291 ASP A N 2212 C CA . ASP A 291 ? 0.3640 0.3664 0.4175 0.0044 -0.0736 -0.0380 291 ASP A CA 2213 C C . ASP A 291 ? 0.3487 0.3516 0.4014 -0.0004 -0.0691 -0.0337 291 ASP A C 2214 O O . ASP A 291 ? 0.3598 0.3686 0.4129 -0.0027 -0.0655 -0.0360 291 ASP A O 2215 C CB . ASP A 291 ? 0.3878 0.3857 0.4395 0.0063 -0.0773 -0.0397 291 ASP A CB 2216 C CG . ASP A 291 ? 0.4316 0.4196 0.4804 0.0052 -0.0805 -0.0341 291 ASP A CG 2217 O OD1 . ASP A 291 ? 0.4770 0.4594 0.5244 0.0070 -0.0839 -0.0323 291 ASP A OD1 2218 O OD2 . ASP A 291 ? 0.4797 0.4654 0.5270 0.0023 -0.0797 -0.0315 291 ASP A OD2 2219 N N . LYS A 292 ? 0.3022 0.2992 0.3535 -0.0020 -0.0695 -0.0275 292 LYS A N 2220 C CA . LYS A 292 ? 0.2829 0.2797 0.3330 -0.0058 -0.0660 -0.0232 292 LYS A CA 2221 C C . LYS A 292 ? 0.2632 0.2629 0.3132 -0.0070 -0.0621 -0.0222 292 LYS A C 2222 O O . LYS A 292 ? 0.2658 0.2659 0.3166 -0.0054 -0.0628 -0.0227 292 LYS A O 2223 C CB . LYS A 292 ? 0.2806 0.2712 0.3294 -0.0067 -0.0681 -0.0172 292 LYS A CB 2224 C CG . LYS A 292 ? 0.2914 0.2781 0.3391 -0.0063 -0.0719 -0.0178 292 LYS A CG 2225 C CD . LYS A 292 ? 0.3027 0.2837 0.3488 -0.0079 -0.0743 -0.0117 292 LYS A CD 2226 C CE . LYS A 292 ? 0.3253 0.3009 0.3691 -0.0078 -0.0788 -0.0122 292 LYS A CE 2227 N NZ . LYS A 292 ? 0.3561 0.3284 0.3989 -0.0040 -0.0827 -0.0168 292 LYS A NZ 2228 N N . PRO A 293 ? 0.2514 0.2522 0.2996 -0.0100 -0.0584 -0.0206 293 PRO A N 2229 C CA . PRO A 293 ? 0.2464 0.2487 0.2930 -0.0112 -0.0549 -0.0199 293 PRO A CA 2230 C C . PRO A 293 ? 0.2401 0.2381 0.2856 -0.0107 -0.0546 -0.0142 293 PRO A C 2231 O O . PRO A 293 ? 0.2353 0.2334 0.2794 -0.0109 -0.0525 -0.0137 293 PRO A O 2232 C CB . PRO A 293 ? 0.2567 0.2602 0.3005 -0.0145 -0.0515 -0.0204 293 PRO A CB 2233 C CG . PRO A 293 ? 0.2529 0.2541 0.2968 -0.0149 -0.0530 -0.0184 293 PRO A CG 2234 C CD . PRO A 293 ? 0.2550 0.2558 0.3018 -0.0122 -0.0572 -0.0204 293 PRO A CD 2235 N N . PHE A 294 ? 0.2369 0.2316 0.2829 -0.0104 -0.0565 -0.0100 294 PHE A N 2236 C CA . PHE A 294 ? 0.2352 0.2272 0.2803 -0.0101 -0.0561 -0.0043 294 PHE A CA 2237 C C . PHE A 294 ? 0.2372 0.2266 0.2839 -0.0089 -0.0602 -0.0021 294 PHE A C 2238 O O . PHE A 294 ? 0.2353 0.2236 0.2829 -0.0085 -0.0635 -0.0043 294 PHE A O 2239 C CB . PHE A 294 ? 0.2406 0.2320 0.2837 -0.0116 -0.0538 -0.0004 294 PHE A CB 2240 C CG . PHE A 294 ? 0.2414 0.2337 0.2814 -0.0132 -0.0503 -0.0025 294 PHE A CG 2241 C CD1 . PHE A 294 ? 0.2474 0.2392 0.2847 -0.0133 -0.0475 -0.0030 294 PHE A CD1 2242 C CD2 . PHE A 294 ? 0.2570 0.2500 0.2963 -0.0150 -0.0498 -0.0039 294 PHE A CD2 2243 C CE1 . PHE A 294 ? 0.2484 0.2400 0.2817 -0.0153 -0.0445 -0.0049 294 PHE A CE1 2244 C CE2 . PHE A 294 ? 0.2499 0.2430 0.2853 -0.0169 -0.0467 -0.0058 294 PHE A CE2 2245 C CZ . PHE A 294 ? 0.2501 0.2424 0.2824 -0.0173 -0.0441 -0.0063 294 PHE A CZ 2246 N N . GLN A 295 ? 0.2328 0.2207 0.2790 -0.0085 -0.0600 0.0021 295 GLN A N 2247 C CA . GLN A 295 ? 0.2392 0.2243 0.2859 -0.0083 -0.0637 0.0049 295 GLN A CA 2248 C C . GLN A 295 ? 0.2352 0.2206 0.2812 -0.0089 -0.0622 0.0107 295 GLN A C 2249 O O . GLN A 295 ? 0.2297 0.2165 0.2745 -0.0083 -0.0587 0.0117 295 GLN A O 2250 C CB . GLN A 295 ? 0.2421 0.2253 0.2891 -0.0063 -0.0664 0.0016 295 GLN A CB 2251 C CG . GLN A 295 ? 0.2326 0.2170 0.2792 -0.0053 -0.0640 0.0008 295 GLN A CG 2252 C CD . GLN A 295 ? 0.2406 0.2229 0.2861 -0.0051 -0.0643 0.0051 295 GLN A CD 2253 O OE1 . GLN A 295 ? 0.2533 0.2334 0.2985 -0.0060 -0.0667 0.0089 295 GLN A OE1 2254 N NE2 . GLN A 295 ? 0.2239 0.2067 0.2684 -0.0043 -0.0621 0.0046 295 GLN A NE2 2255 N N . ASN A 296 ? 0.2386 0.2227 0.2846 -0.0101 -0.0650 0.0145 296 ASN A N 2256 C CA A ASN A 296 ? 0.2388 0.2245 0.2845 -0.0109 -0.0640 0.0201 296 ASN A CA 2257 C CA B ASN A 296 ? 0.2515 0.2373 0.2972 -0.0108 -0.0639 0.0201 296 ASN A CA 2258 C C . ASN A 296 ? 0.2585 0.2413 0.3035 -0.0115 -0.0675 0.0220 296 ASN A C 2259 O O . ASN A 296 ? 0.2703 0.2545 0.3149 -0.0131 -0.0680 0.0268 296 ASN A O 2260 C CB A ASN A 296 ? 0.2332 0.2214 0.2795 -0.0128 -0.0642 0.0233 296 ASN A CB 2261 C CB B ASN A 296 ? 0.2626 0.2516 0.3088 -0.0124 -0.0632 0.0239 296 ASN A CB 2262 C CG A ASN A 296 ? 0.2283 0.2206 0.2748 -0.0134 -0.0626 0.0289 296 ASN A CG 2263 C CG B ASN A 296 ? 0.2835 0.2709 0.3297 -0.0150 -0.0674 0.0256 296 ASN A CG 2264 O OD1 A ASN A 296 ? 0.2271 0.2209 0.2740 -0.0158 -0.0649 0.0325 296 ASN A OD1 2265 O OD1 B ASN A 296 ? 0.3089 0.2917 0.3544 -0.0151 -0.0709 0.0225 296 ASN A OD1 2266 N ND2 A ASN A 296 ? 0.2200 0.2145 0.2658 -0.0113 -0.0587 0.0298 296 ASN A ND2 2267 N ND2 B ASN A 296 ? 0.2888 0.2799 0.3355 -0.0169 -0.0674 0.0306 296 ASN A ND2 2268 N N . VAL A 297 ? 0.2572 0.2360 0.3015 -0.0102 -0.0700 0.0181 297 VAL A N 2269 C CA . VAL A 297 ? 0.2579 0.2324 0.3005 -0.0107 -0.0737 0.0196 297 VAL A CA 2270 C C . VAL A 297 ? 0.2542 0.2298 0.2961 -0.0100 -0.0715 0.0217 297 VAL A C 2271 O O . VAL A 297 ? 0.2591 0.2345 0.2997 -0.0117 -0.0724 0.0260 297 VAL A O 2272 C CB . VAL A 297 ? 0.2720 0.2414 0.3136 -0.0088 -0.0777 0.0145 297 VAL A CB 2273 C CG1 . VAL A 297 ? 0.2863 0.2501 0.3250 -0.0090 -0.0817 0.0159 297 VAL A CG1 2274 C CG2 . VAL A 297 ? 0.2791 0.2465 0.3203 -0.0095 -0.0803 0.0127 297 VAL A CG2 2275 N N . ASN A 298 ? 0.2420 0.2189 0.2844 -0.0077 -0.0687 0.0187 298 ASN A N 2276 C CA . ASN A 298 ? 0.2427 0.2196 0.2838 -0.0070 -0.0668 0.0205 298 ASN A CA 2277 C C . ASN A 298 ? 0.2409 0.2199 0.2820 -0.0053 -0.0627 0.0178 298 ASN A C 2278 O O . ASN A 298 ? 0.2357 0.2148 0.2776 -0.0044 -0.0628 0.0129 298 ASN A O 2279 C CB . ASN A 298 ? 0.2502 0.2221 0.2896 -0.0066 -0.0708 0.0196 298 ASN A CB 2280 C CG . ASN A 298 ? 0.2528 0.2243 0.2903 -0.0072 -0.0698 0.0233 298 ASN A CG 2281 O OD1 . ASN A 298 ? 0.2595 0.2332 0.2966 -0.0060 -0.0660 0.0236 298 ASN A OD1 2282 N ND2 . ASN A 298 ? 0.2672 0.2355 0.3026 -0.0092 -0.0733 0.0264 298 ASN A ND2 2283 N N . ARG A 299 ? 0.2445 0.2250 0.2841 -0.0049 -0.0592 0.0208 299 ARG A N 2284 C CA . ARG A 299 ? 0.2602 0.2409 0.2981 -0.0036 -0.0556 0.0185 299 ARG A CA 2285 C C . ARG A 299 ? 0.2509 0.2292 0.2880 -0.0028 -0.0569 0.0151 299 ARG A C 2286 O O . ARG A 299 ? 0.2342 0.2128 0.2703 -0.0024 -0.0548 0.0120 299 ARG A O 2287 C CB . ARG A 299 ? 0.2898 0.2718 0.3253 -0.0028 -0.0517 0.0224 299 ARG A CB 2288 C CG . ARG A 299 ? 0.3188 0.3003 0.3530 -0.0026 -0.0520 0.0258 299 ARG A CG 2289 C CD . ARG A 299 ? 0.3796 0.3630 0.4113 -0.0011 -0.0478 0.0293 299 ARG A CD 2290 N NE . ARG A 299 ? 0.3786 0.3662 0.4118 -0.0012 -0.0470 0.0322 299 ARG A NE 2291 C CZ . ARG A 299 ? 0.4254 0.4155 0.4566 0.0007 -0.0435 0.0347 299 ARG A CZ 2292 N NH1 . ARG A 299 ? 0.4249 0.4128 0.4518 0.0030 -0.0403 0.0347 299 ARG A NH1 2293 N NH2 . ARG A 299 ? 0.4272 0.4218 0.4604 0.0005 -0.0433 0.0371 299 ARG A NH2 2294 N N . ILE A 300 ? 0.2406 0.2165 0.2779 -0.0028 -0.0604 0.0159 300 ILE A N 2295 C CA . ILE A 300 ? 0.2424 0.2159 0.2790 -0.0018 -0.0624 0.0128 300 ILE A CA 2296 C C . ILE A 300 ? 0.2411 0.2146 0.2799 -0.0010 -0.0658 0.0081 300 ILE A C 2297 O O . ILE A 300 ? 0.2341 0.2058 0.2737 -0.0012 -0.0693 0.0085 300 ILE A O 2298 C CB . ILE A 300 ? 0.2520 0.2221 0.2868 -0.0021 -0.0649 0.0159 300 ILE A CB 2299 C CG1 . ILE A 300 ? 0.2510 0.2221 0.2835 -0.0025 -0.0611 0.0203 300 ILE A CG1 2300 C CG2 . ILE A 300 ? 0.2434 0.2107 0.2774 -0.0007 -0.0677 0.0126 300 ILE A CG2 2301 C CD1 . ILE A 300 ? 0.2656 0.2345 0.2963 -0.0038 -0.0633 0.0245 300 ILE A CD1 2302 N N . THR A 301 ? 0.2481 0.2239 0.2877 -0.0001 -0.0648 0.0035 301 THR A N 2303 C CA . THR A 301 ? 0.2616 0.2390 0.3035 0.0011 -0.0677 -0.0016 301 THR A CA 2304 C C . THR A 301 ? 0.2649 0.2441 0.3072 0.0026 -0.0684 -0.0058 301 THR A C 2305 O O . THR A 301 ? 0.2764 0.2562 0.3168 0.0018 -0.0656 -0.0053 301 THR A O 2306 C CB . THR A 301 ? 0.2692 0.2507 0.3129 0.0003 -0.0656 -0.0040 301 THR A CB 2307 O OG1 . THR A 301 ? 0.3015 0.2865 0.3445 -0.0005 -0.0617 -0.0061 301 THR A OG1 2308 C CG2 . THR A 301 ? 0.2884 0.2690 0.3317 -0.0012 -0.0641 0.0002 301 THR A CG2 2309 N N . TYR A 302 ? 0.2556 0.2358 0.2998 0.0048 -0.0722 -0.0101 302 TYR A N 2310 C CA . TYR A 302 ? 0.2500 0.2340 0.2954 0.0065 -0.0732 -0.0149 302 TYR A CA 2311 C C . TYR A 302 ? 0.2504 0.2394 0.2989 0.0083 -0.0749 -0.0204 302 TYR A C 2312 O O . TYR A 302 ? 0.2616 0.2478 0.3105 0.0101 -0.0783 -0.0209 302 TYR A O 2313 C CB . TYR A 302 ? 0.2637 0.2431 0.3075 0.0085 -0.0772 -0.0144 302 TYR A CB 2314 C CG . TYR A 302 ? 0.2549 0.2390 0.3001 0.0105 -0.0785 -0.0193 302 TYR A CG 2315 C CD1 . TYR A 302 ? 0.2761 0.2631 0.3238 0.0140 -0.0824 -0.0243 302 TYR A CD1 2316 C CD2 . TYR A 302 ? 0.2612 0.2474 0.3053 0.0090 -0.0758 -0.0192 302 TYR A CD2 2317 C CE1 . TYR A 302 ? 0.2647 0.2577 0.3142 0.0160 -0.0835 -0.0289 302 TYR A CE1 2318 C CE2 . TYR A 302 ? 0.2705 0.2621 0.3161 0.0105 -0.0770 -0.0237 302 TYR A CE2 2319 C CZ . TYR A 302 ? 0.2716 0.2671 0.3202 0.0140 -0.0809 -0.0285 302 TYR A CZ 2320 O OH . TYR A 302 ? 0.2896 0.2922 0.3403 0.0157 -0.0822 -0.0332 302 TYR A OH 2321 N N . GLY A 303 ? 0.2537 0.2502 0.3039 0.0078 -0.0724 -0.0246 303 GLY A N 2322 C CA . GLY A 303 ? 0.2572 0.2604 0.3106 0.0096 -0.0738 -0.0304 303 GLY A CA 2323 C C . GLY A 303 ? 0.2672 0.2743 0.3213 0.0069 -0.0700 -0.0310 303 GLY A C 2324 O O . GLY A 303 ? 0.2669 0.2722 0.3186 0.0035 -0.0661 -0.0275 303 GLY A O 2325 N N . ALA A 304 ? 0.2676 0.2794 0.3241 0.0085 -0.0713 -0.0354 304 ALA A N 2326 C CA . ALA A 304 ? 0.2752 0.2904 0.3320 0.0058 -0.0681 -0.0362 304 ALA A CA 2327 C C . ALA A 304 ? 0.2788 0.2868 0.3341 0.0051 -0.0686 -0.0319 304 ALA A C 2328 O O . ALA A 304 ? 0.2809 0.2863 0.3367 0.0076 -0.0721 -0.0328 304 ALA A O 2329 C CB . ALA A 304 ? 0.2934 0.3173 0.3533 0.0076 -0.0689 -0.0428 304 ALA A CB 2330 N N . CYS A 305 ? 0.2783 0.2830 0.3311 0.0019 -0.0652 -0.0270 305 CYS A N 2331 C CA . CYS A 305 ? 0.2845 0.2828 0.3359 0.0012 -0.0659 -0.0220 305 CYS A CA 2332 C C . CYS A 305 ? 0.2652 0.2645 0.3155 -0.0017 -0.0621 -0.0203 305 CYS A C 2333 O O . CYS A 305 ? 0.2553 0.2572 0.3041 -0.0040 -0.0583 -0.0208 305 CYS A O 2334 C CB . CYS A 305 ? 0.2939 0.2870 0.3433 0.0009 -0.0658 -0.0168 305 CYS A CB 2335 S SG . CYS A 305 ? 0.3330 0.3222 0.3826 0.0043 -0.0711 -0.0173 305 CYS A SG 2336 N N . PRO A 306 ? 0.2506 0.2470 0.3009 -0.0020 -0.0634 -0.0182 306 PRO A N 2337 C CA . PRO A 306 ? 0.2526 0.2488 0.3013 -0.0048 -0.0600 -0.0153 306 PRO A CA 2338 C C . PRO A 306 ? 0.2527 0.2465 0.2989 -0.0058 -0.0572 -0.0106 306 PRO A C 2339 O O . PRO A 306 ? 0.2561 0.2473 0.3021 -0.0046 -0.0584 -0.0083 306 PRO A O 2340 C CB . PRO A 306 ? 0.2545 0.2473 0.3036 -0.0047 -0.0627 -0.0129 306 PRO A CB 2341 C CG . PRO A 306 ? 0.2620 0.2536 0.3124 -0.0019 -0.0673 -0.0163 306 PRO A CG 2342 C CD . PRO A 306 ? 0.2548 0.2469 0.3056 -0.0002 -0.0679 -0.0174 306 PRO A CD 2343 N N . ARG A 307 ? 0.2484 0.2423 0.2921 -0.0079 -0.0535 -0.0091 307 ARG A N 2344 C CA . ARG A 307 ? 0.2382 0.2294 0.2787 -0.0082 -0.0508 -0.0049 307 ARG A CA 2345 C C . ARG A 307 ? 0.2231 0.2121 0.2641 -0.0076 -0.0518 0.0005 307 ARG A C 2346 O O . ARG A 307 ? 0.2217 0.2110 0.2637 -0.0083 -0.0527 0.0014 307 ARG A O 2347 C CB . ARG A 307 ? 0.2442 0.2355 0.2808 -0.0103 -0.0470 -0.0054 307 ARG A CB 2348 C CG . ARG A 307 ? 0.2624 0.2563 0.2977 -0.0117 -0.0457 -0.0101 307 ARG A CG 2349 C CD . ARG A 307 ? 0.2653 0.2570 0.2946 -0.0143 -0.0419 -0.0098 307 ARG A CD 2350 N NE . ARG A 307 ? 0.2598 0.2540 0.2871 -0.0164 -0.0406 -0.0138 307 ARG A NE 2351 C CZ . ARG A 307 ? 0.2657 0.2582 0.2906 -0.0163 -0.0399 -0.0136 307 ARG A CZ 2352 N NH1 . ARG A 307 ? 0.2620 0.2505 0.2864 -0.0139 -0.0403 -0.0097 307 ARG A NH1 2353 N NH2 . ARG A 307 ? 0.2817 0.2773 0.3047 -0.0190 -0.0389 -0.0174 307 ARG A NH2 2354 N N . TYR A 308 ? 0.2182 0.2054 0.2582 -0.0066 -0.0514 0.0040 308 TYR A N 2355 C CA . TYR A 308 ? 0.2182 0.2046 0.2584 -0.0063 -0.0519 0.0094 308 TYR A CA 2356 C C . TYR A 308 ? 0.2180 0.2050 0.2561 -0.0067 -0.0489 0.0121 308 TYR A C 2357 O O . TYR A 308 ? 0.2167 0.2024 0.2510 -0.0063 -0.0457 0.0121 308 TYR A O 2358 C CB . TYR A 308 ? 0.2297 0.2148 0.2691 -0.0052 -0.0519 0.0122 308 TYR A CB 2359 C CG . TYR A 308 ? 0.2376 0.2236 0.2777 -0.0053 -0.0527 0.0176 308 TYR A CG 2360 C CD1 . TYR A 308 ? 0.2455 0.2311 0.2878 -0.0063 -0.0566 0.0188 308 TYR A CD1 2361 C CD2 . TYR A 308 ? 0.2470 0.2342 0.2852 -0.0045 -0.0496 0.0213 308 TYR A CD2 2362 C CE1 . TYR A 308 ? 0.2608 0.2480 0.3035 -0.0072 -0.0574 0.0238 308 TYR A CE1 2363 C CE2 . TYR A 308 ? 0.2665 0.2564 0.3058 -0.0047 -0.0502 0.0262 308 TYR A CE2 2364 C CZ . TYR A 308 ? 0.2790 0.2693 0.3207 -0.0065 -0.0540 0.0275 308 TYR A CZ 2365 O OH . TYR A 308 ? 0.2991 0.2929 0.3416 -0.0074 -0.0544 0.0323 308 TYR A OH 2366 N N . VAL A 309 ? 0.2165 0.2049 0.2564 -0.0073 -0.0502 0.0147 309 VAL A N 2367 C CA . VAL A 309 ? 0.2140 0.2034 0.2521 -0.0072 -0.0480 0.0177 309 VAL A CA 2368 C C . VAL A 309 ? 0.2291 0.2212 0.2693 -0.0071 -0.0495 0.0229 309 VAL A C 2369 O O . VAL A 309 ? 0.2355 0.2277 0.2781 -0.0080 -0.0526 0.0236 309 VAL A O 2370 C CB . VAL A 309 ? 0.2068 0.1964 0.2448 -0.0088 -0.0480 0.0153 309 VAL A CB 2371 C CG1 . VAL A 309 ? 0.2052 0.1933 0.2406 -0.0095 -0.0462 0.0103 309 VAL A CG1 2372 C CG2 . VAL A 309 ? 0.2043 0.1949 0.2458 -0.0101 -0.0518 0.0144 309 VAL A CG2 2373 N N . LYS A 310 ? 0.2408 0.2350 0.2798 -0.0061 -0.0474 0.0262 310 LYS A N 2374 C CA . LYS A 310 ? 0.2586 0.2571 0.2997 -0.0062 -0.0485 0.0313 310 LYS A CA 2375 C C . LYS A 310 ? 0.2686 0.2692 0.3123 -0.0086 -0.0512 0.0322 310 LYS A C 2376 O O . LYS A 310 ? 0.2559 0.2597 0.3016 -0.0101 -0.0534 0.0356 310 LYS A O 2377 C CB . LYS A 310 ? 0.2994 0.3004 0.3382 -0.0035 -0.0453 0.0346 310 LYS A CB 2378 C CG . LYS A 310 ? 0.3389 0.3383 0.3750 -0.0010 -0.0430 0.0349 310 LYS A CG 2379 C CD . LYS A 310 ? 0.3905 0.3911 0.4230 0.0025 -0.0397 0.0376 310 LYS A CD 2380 C CE . LYS A 310 ? 0.4210 0.4197 0.4507 0.0031 -0.0386 0.0366 310 LYS A CE 2381 N NZ . LYS A 310 ? 0.5219 0.5175 0.5454 0.0069 -0.0354 0.0373 310 LYS A NZ 2382 N N . GLN A 311 ? 0.2567 0.2554 0.2997 -0.0095 -0.0513 0.0292 311 GLN A N 2383 C CA . GLN A 311 ? 0.2615 0.2614 0.3061 -0.0118 -0.0537 0.0297 311 GLN A CA 2384 C C . GLN A 311 ? 0.2773 0.2752 0.3236 -0.0138 -0.0577 0.0286 311 GLN A C 2385 O O . GLN A 311 ? 0.2652 0.2599 0.3113 -0.0133 -0.0584 0.0250 311 GLN A O 2386 C CB . GLN A 311 ? 0.2573 0.2549 0.3001 -0.0123 -0.0527 0.0261 311 GLN A CB 2387 C CG . GLN A 311 ? 0.2597 0.2574 0.2992 -0.0106 -0.0492 0.0272 311 GLN A CG 2388 C CD . GLN A 311 ? 0.2626 0.2566 0.2985 -0.0093 -0.0464 0.0241 311 GLN A CD 2389 O OE1 . GLN A 311 ? 0.2479 0.2410 0.2842 -0.0086 -0.0463 0.0230 311 GLN A OE1 2390 N NE2 . GLN A 311 ? 0.2539 0.2454 0.2855 -0.0092 -0.0443 0.0229 311 GLN A NE2 2391 N N . ASN A 312 ? 0.2867 0.2863 0.3343 -0.0162 -0.0605 0.0314 312 ASN A N 2392 C CA . ASN A 312 ? 0.3196 0.3155 0.3673 -0.0182 -0.0648 0.0301 312 ASN A CA 2393 C C . ASN A 312 ? 0.3050 0.2976 0.3522 -0.0193 -0.0666 0.0262 312 ASN A C 2394 O O . ASN A 312 ? 0.3173 0.3056 0.3637 -0.0201 -0.0702 0.0242 312 ASN A O 2395 C CB . ASN A 312 ? 0.3660 0.3639 0.4141 -0.0209 -0.0676 0.0352 312 ASN A CB 2396 C CG . ASN A 312 ? 0.4131 0.4166 0.4623 -0.0226 -0.0672 0.0392 312 ASN A CG 2397 O OD1 . ASN A 312 ? 0.4782 0.4818 0.5272 -0.0226 -0.0665 0.0378 312 ASN A OD1 2398 N ND2 . ASN A 312 ? 0.5088 0.5177 0.5589 -0.0242 -0.0676 0.0443 312 ASN A ND2 2399 N N . THR A 313 ? 0.2881 0.2823 0.3349 -0.0191 -0.0643 0.0252 313 THR A N 2400 C CA . THR A 313 ? 0.2832 0.2750 0.3292 -0.0200 -0.0653 0.0214 313 THR A CA 2401 C C . THR A 313 ? 0.2774 0.2705 0.3222 -0.0192 -0.0616 0.0196 313 THR A C 2402 O O . THR A 313 ? 0.2689 0.2647 0.3133 -0.0186 -0.0592 0.0228 313 THR A O 2403 C CB . THR A 313 ? 0.2964 0.2879 0.3421 -0.0230 -0.0686 0.0240 313 THR A CB 2404 O OG1 . THR A 313 ? 0.3068 0.2957 0.3513 -0.0237 -0.0694 0.0200 313 THR A OG1 2405 C CG2 . THR A 313 ? 0.2889 0.2857 0.3354 -0.0239 -0.0672 0.0293 313 THR A CG2 2406 N N . LEU A 314 ? 0.2703 0.2614 0.3143 -0.0191 -0.0611 0.0143 314 LEU A N 2407 C CA . LEU A 314 ? 0.2748 0.2664 0.3168 -0.0195 -0.0583 0.0122 314 LEU A CA 2408 C C . LEU A 314 ? 0.2794 0.2695 0.3209 -0.0208 -0.0599 0.0076 314 LEU A C 2409 O O . LEU A 314 ? 0.2722 0.2616 0.3143 -0.0199 -0.0606 0.0031 314 LEU A O 2410 C CB . LEU A 314 ? 0.2732 0.2647 0.3137 -0.0181 -0.0550 0.0098 314 LEU A CB 2411 C CG . LEU A 314 ? 0.2799 0.2720 0.3193 -0.0164 -0.0526 0.0137 314 LEU A CG 2412 C CD1 . LEU A 314 ? 0.2935 0.2846 0.3314 -0.0153 -0.0503 0.0107 314 LEU A CD1 2413 C CD2 . LEU A 314 ? 0.2969 0.2893 0.3336 -0.0166 -0.0507 0.0165 314 LEU A CD2 2414 N N . LYS A 315 ? 0.2765 0.2664 0.3168 -0.0227 -0.0603 0.0087 315 LYS A N 2415 C CA A LYS A 315 ? 0.2852 0.2736 0.3247 -0.0240 -0.0619 0.0046 315 LYS A CA 2416 C CA B LYS A 315 ? 0.2842 0.2726 0.3237 -0.0239 -0.0620 0.0046 315 LYS A CA 2417 C C . LYS A 315 ? 0.2769 0.2661 0.3141 -0.0248 -0.0588 0.0008 315 LYS A C 2418 O O . LYS A 315 ? 0.2734 0.2628 0.3083 -0.0259 -0.0567 0.0029 315 LYS A O 2419 C CB A LYS A 315 ? 0.2990 0.2863 0.3380 -0.0261 -0.0646 0.0079 315 LYS A CB 2420 C CB B LYS A 315 ? 0.2968 0.2840 0.3359 -0.0260 -0.0649 0.0079 315 LYS A CB 2421 C CG A LYS A 315 ? 0.3203 0.3064 0.3607 -0.0263 -0.0682 0.0114 315 LYS A CG 2422 C CG B LYS A 315 ? 0.3152 0.3010 0.3557 -0.0260 -0.0685 0.0110 315 LYS A CG 2423 C CD A LYS A 315 ? 0.3313 0.3138 0.3715 -0.0252 -0.0712 0.0074 315 LYS A CD 2424 C CD B LYS A 315 ? 0.3231 0.3097 0.3634 -0.0286 -0.0705 0.0164 315 LYS A CD 2425 C CE A LYS A 315 ? 0.3527 0.3314 0.3907 -0.0269 -0.0746 0.0060 315 LYS A CE 2426 C CE B LYS A 315 ? 0.3464 0.3313 0.3871 -0.0297 -0.0743 0.0195 315 LYS A CE 2427 N NZ A LYS A 315 ? 0.3786 0.3536 0.4155 -0.0248 -0.0768 0.0004 315 LYS A NZ 2428 N NZ B LYS A 315 ? 0.3362 0.3249 0.3790 -0.0291 -0.0734 0.0241 315 LYS A NZ 2429 N N . LEU A 316 ? 0.2739 0.2637 0.3112 -0.0244 -0.0588 -0.0048 316 LEU A N 2430 C CA . LEU A 316 ? 0.2732 0.2646 0.3082 -0.0259 -0.0561 -0.0090 316 LEU A CA 2431 C C . LEU A 316 ? 0.2740 0.2646 0.3079 -0.0275 -0.0577 -0.0112 316 LEU A C 2432 O O . LEU A 316 ? 0.2822 0.2721 0.3173 -0.0263 -0.0605 -0.0138 316 LEU A O 2433 C CB . LEU A 316 ? 0.2731 0.2674 0.3094 -0.0246 -0.0551 -0.0142 316 LEU A CB 2434 C CG . LEU A 316 ? 0.2712 0.2687 0.3052 -0.0266 -0.0521 -0.0190 316 LEU A CG 2435 C CD1 . LEU A 316 ? 0.2730 0.2699 0.3036 -0.0283 -0.0485 -0.0170 316 LEU A CD1 2436 C CD2 . LEU A 316 ? 0.2860 0.2879 0.3225 -0.0248 -0.0525 -0.0249 316 LEU A CD2 2437 N N . ALA A 317 ? 0.2810 0.2711 0.3118 -0.0301 -0.0561 -0.0103 317 ALA A N 2438 C CA . ALA A 317 ? 0.2862 0.2756 0.3151 -0.0320 -0.0570 -0.0129 317 ALA A CA 2439 C C . ALA A 317 ? 0.2889 0.2813 0.3181 -0.0315 -0.0565 -0.0199 317 ALA A C 2440 O O . ALA A 317 ? 0.2833 0.2792 0.3121 -0.0319 -0.0536 -0.0230 317 ALA A O 2441 C CB . ALA A 317 ? 0.2826 0.2708 0.3074 -0.0349 -0.0550 -0.0110 317 ALA A CB 2442 N N . THR A 318 ? 0.3003 0.2915 0.3299 -0.0307 -0.0594 -0.0224 318 THR A N 2443 C CA . THR A 318 ? 0.3050 0.2995 0.3345 -0.0298 -0.0591 -0.0292 318 THR A CA 2444 C C . THR A 318 ? 0.3244 0.3174 0.3508 -0.0319 -0.0598 -0.0311 318 THR A C 2445 O O . THR A 318 ? 0.3490 0.3437 0.3752 -0.0304 -0.0608 -0.0364 318 THR A O 2446 C CB . THR A 318 ? 0.3047 0.2990 0.3370 -0.0256 -0.0622 -0.0317 318 THR A CB 2447 O OG1 . THR A 318 ? 0.3297 0.3177 0.3612 -0.0250 -0.0664 -0.0285 318 THR A OG1 2448 C CG2 . THR A 318 ? 0.3031 0.2994 0.3383 -0.0238 -0.0613 -0.0303 318 THR A CG2 2449 N N . GLY A 319 ? 0.3216 0.3116 0.3454 -0.0349 -0.0595 -0.0268 319 GLY A N 2450 C CA . GLY A 319 ? 0.3332 0.3216 0.3534 -0.0375 -0.0597 -0.0281 319 GLY A CA 2451 C C . GLY A 319 ? 0.3366 0.3230 0.3539 -0.0410 -0.0581 -0.0233 319 GLY A C 2452 O O . GLY A 319 ? 0.3394 0.3256 0.3573 -0.0408 -0.0568 -0.0192 319 GLY A O 2453 N N . MET A 320 ? 0.3302 0.3149 0.3439 -0.0437 -0.0583 -0.0241 320 MET A N 2454 C CA . MET A 320 ? 0.3306 0.3132 0.3406 -0.0470 -0.0569 -0.0204 320 MET A CA 2455 C C . MET A 320 ? 0.3278 0.3069 0.3384 -0.0469 -0.0596 -0.0136 320 MET A C 2456 O O . MET A 320 ? 0.3332 0.3112 0.3466 -0.0452 -0.0628 -0.0118 320 MET A O 2457 C CB . MET A 320 ? 0.3302 0.3123 0.3355 -0.0502 -0.0560 -0.0239 320 MET A CB 2458 C CG . MET A 320 ? 0.3306 0.3098 0.3353 -0.0501 -0.0594 -0.0247 320 MET A CG 2459 S SD . MET A 320 ? 0.3421 0.3209 0.3411 -0.0540 -0.0581 -0.0288 320 MET A SD 2460 C CE . MET A 320 ? 0.3219 0.3074 0.3227 -0.0520 -0.0559 -0.0371 320 MET A CE 2461 N N . ARG A 321 ? 0.3378 0.3154 0.3453 -0.0489 -0.0585 -0.0100 321 ARG A N 2462 C CA . ARG A 321 ? 0.3520 0.3276 0.3598 -0.0492 -0.0611 -0.0038 321 ARG A CA 2463 C C . ARG A 321 ? 0.3604 0.3338 0.3679 -0.0505 -0.0647 -0.0043 321 ARG A C 2464 O O . ARG A 321 ? 0.3246 0.2968 0.3291 -0.0522 -0.0645 -0.0087 321 ARG A O 2465 C CB . ARG A 321 ? 0.3891 0.3631 0.3926 -0.0511 -0.0598 -0.0007 321 ARG A CB 2466 C CG . ARG A 321 ? 0.4442 0.4156 0.4422 -0.0547 -0.0593 -0.0035 321 ARG A CG 2467 C CD . ARG A 321 ? 0.4920 0.4607 0.4849 -0.0565 -0.0586 0.0000 321 ARG A CD 2468 N NE . ARG A 321 ? 0.5168 0.4845 0.5063 -0.0563 -0.0552 -0.0006 321 ARG A NE 2469 C CZ . ARG A 321 ? 0.5129 0.4803 0.5027 -0.0537 -0.0546 0.0032 321 ARG A CZ 2470 N NH1 . ARG A 321 ? 0.5335 0.5029 0.5277 -0.0509 -0.0568 0.0081 321 ARG A NH1 2471 N NH2 . ARG A 321 ? 0.5398 0.5047 0.5248 -0.0540 -0.0517 0.0021 321 ARG A NH2 2472 N N . ASN A 322 ? 0.3538 0.3268 0.3639 -0.0499 -0.0679 0.0000 322 ASN A N 2473 C CA . ASN A 322 ? 0.3827 0.3526 0.3917 -0.0514 -0.0718 0.0003 322 ASN A CA 2474 C C . ASN A 322 ? 0.4081 0.3771 0.4149 -0.0543 -0.0733 0.0052 322 ASN A C 2475 O O . ASN A 322 ? 0.3901 0.3617 0.3990 -0.0540 -0.0738 0.0106 322 ASN A O 2476 C CB . ASN A 322 ? 0.3856 0.3549 0.3978 -0.0498 -0.0748 0.0021 322 ASN A CB 2477 C CG . ASN A 322 ? 0.4010 0.3652 0.4105 -0.0511 -0.0789 0.0007 322 ASN A CG 2478 O OD1 . ASN A 322 ? 0.4003 0.3621 0.4069 -0.0511 -0.0787 -0.0046 322 ASN A OD1 2479 N ND2 . ASN A 322 ? 0.4174 0.3801 0.4275 -0.0523 -0.0826 0.0053 322 ASN A ND2 2480 N N . VAL A 323 ? 0.4350 0.4010 0.4374 -0.0570 -0.0739 0.0030 323 VAL A N 2481 C CA . VAL A 323 ? 0.4454 0.4107 0.4451 -0.0598 -0.0749 0.0071 323 VAL A CA 2482 C C . VAL A 323 ? 0.4816 0.4431 0.4789 -0.0625 -0.0790 0.0074 323 VAL A C 2483 O O . VAL A 323 ? 0.4571 0.4151 0.4517 -0.0628 -0.0794 0.0024 323 VAL A O 2484 C CB . VAL A 323 ? 0.4615 0.4259 0.4567 -0.0613 -0.0718 0.0047 323 VAL A CB 2485 C CG1 . VAL A 323 ? 0.4841 0.4479 0.4766 -0.0635 -0.0730 0.0096 323 VAL A CG1 2486 C CG2 . VAL A 323 ? 0.4390 0.4057 0.4352 -0.0591 -0.0679 0.0033 323 VAL A CG2 2487 N N . PRO A 324 ? 0.5170 0.4794 0.5152 -0.0642 -0.0821 0.0133 324 PRO A N 2488 C CA . PRO A 324 ? 0.5286 0.4866 0.5235 -0.0675 -0.0863 0.0141 324 PRO A CA 2489 C C . PRO A 324 ? 0.5157 0.4696 0.5049 -0.0701 -0.0859 0.0107 324 PRO A C 2490 O O . PRO A 324 ? 0.5088 0.4641 0.4964 -0.0705 -0.0832 0.0103 324 PRO A O 2491 C CB . PRO A 324 ? 0.5401 0.5020 0.5370 -0.0695 -0.0888 0.0214 324 PRO A CB 2492 C CG . PRO A 324 ? 0.5518 0.5199 0.5541 -0.0662 -0.0866 0.0241 324 PRO A CG 2493 C CD . PRO A 324 ? 0.5292 0.4970 0.5312 -0.0633 -0.0821 0.0195 324 PRO A CD 2494 N N . GLU A 325 ? 0.5490 0.4973 0.5343 -0.0717 -0.0887 0.0081 325 GLU A N 2495 C CA . GLU A 325 ? 0.5802 0.5244 0.5596 -0.0746 -0.0890 0.0056 325 GLU A CA 2496 C C . GLU A 325 ? 0.6327 0.5768 0.6103 -0.0785 -0.0918 0.0115 325 GLU A C 2497 O O . GLU A 325 ? 0.6359 0.5799 0.6144 -0.0802 -0.0955 0.0159 325 GLU A O 2498 C CB . GLU A 325 ? 0.5669 0.5045 0.5420 -0.0745 -0.0910 0.0004 325 GLU A CB 2499 C CG . GLU A 325 ? 0.5595 0.4937 0.5286 -0.0768 -0.0902 -0.0034 325 GLU A CG 2500 C CD . GLU A 325 ? 0.5628 0.4932 0.5286 -0.0746 -0.0898 -0.0109 325 GLU A CD 2501 O OE1 . GLU A 325 ? 0.5455 0.4744 0.5130 -0.0714 -0.0912 -0.0128 325 GLU A OE1 2502 O OE2 . GLU A 325 ? 0.5560 0.4850 0.5173 -0.0760 -0.0881 -0.0150 325 GLU A OE2 2503 N N . LYS A 326 ? 0.6834 0.6279 0.6581 -0.0803 -0.0902 0.0118 326 LYS A N 2504 C CA . LYS A 326 ? 0.7452 0.6897 0.7177 -0.0839 -0.0929 0.0170 326 LYS A CA 2505 C C . LYS A 326 ? 0.7991 0.7375 0.7667 -0.0875 -0.0971 0.0165 326 LYS A C 2506 O O . LYS A 326 ? 0.7498 0.6826 0.7131 -0.0877 -0.0967 0.0109 326 LYS A O 2507 C CB . LYS A 326 ? 0.7552 0.6997 0.7243 -0.0849 -0.0903 0.0164 326 LYS A CB 2508 C CG . LYS A 326 ? 0.7812 0.7310 0.7537 -0.0820 -0.0876 0.0191 326 LYS A CG 2509 C CD . LYS A 326 ? 0.8276 0.7751 0.7949 -0.0830 -0.0848 0.0173 326 LYS A CD 2510 C CE . LYS A 326 ? 0.8311 0.7822 0.8003 -0.0800 -0.0826 0.0203 326 LYS A CE 2511 N NZ . LYS A 326 ? 0.8377 0.7914 0.8071 -0.0803 -0.0853 0.0268 326 LYS A NZ 2512 N N . GLN A 327 ? 0.8763 0.8160 0.8443 -0.0905 -0.1010 0.0225 327 GLN A N 2513 C CA . GLN A 327 ? 0.9402 0.8737 0.9031 -0.0946 -0.1056 0.0231 327 GLN A CA 2514 C C . GLN A 327 ? 0.9514 0.8830 0.9092 -0.0987 -0.1070 0.0248 327 GLN A C 2515 O O . GLN A 327 ? 0.9124 0.8417 0.8668 -0.0985 -0.1043 0.0211 327 GLN A O 2516 C CB . GLN A 327 ? 0.9992 0.9356 0.9652 -0.0963 -0.1095 0.0289 327 GLN A CB 2517 C CG . GLN A 327 ? 1.0591 0.9896 1.0193 -0.1018 -0.1148 0.0312 327 GLN A CG 2518 C CD . GLN A 327 ? 1.0777 1.0119 1.0407 -0.1042 -0.1185 0.0370 327 GLN A CD 2519 O OE1 . GLN A 327 ? 1.0778 1.0146 1.0452 -0.1014 -0.1176 0.0371 327 GLN A OE1 2520 N NE2 . GLN A 327 ? 1.0828 1.0177 1.0432 -0.1097 -0.1226 0.0419 327 GLN A NE2 2521 N N . ALA A 334 ? 0.7364 0.6378 0.6533 -0.1067 -0.0958 -0.0093 334 ALA A N 2522 C CA . ALA A 334 ? 0.7271 0.6317 0.6431 -0.1058 -0.0905 -0.0147 334 ALA A CA 2523 C C . ALA A 334 ? 0.7032 0.6143 0.6268 -0.1011 -0.0876 -0.0161 334 ALA A C 2524 O O . ALA A 334 ? 0.7406 0.6548 0.6701 -0.0995 -0.0887 -0.0111 334 ALA A O 2525 C CB . ALA A 334 ? 0.7455 0.6508 0.6584 -0.1095 -0.0891 -0.0120 334 ALA A CB 2526 N N . ILE A 335 ? 0.6319 0.5456 0.5552 -0.0990 -0.0838 -0.0230 335 ILE A N 2527 C CA . ILE A 335 ? 0.5667 0.4866 0.4967 -0.0947 -0.0809 -0.0250 335 ILE A CA 2528 C C . ILE A 335 ? 0.5387 0.4630 0.4717 -0.0954 -0.0784 -0.0212 335 ILE A C 2529 O O . ILE A 335 ? 0.5313 0.4541 0.4601 -0.0990 -0.0779 -0.0189 335 ILE A O 2530 C CB . ILE A 335 ? 0.5473 0.4701 0.4762 -0.0924 -0.0776 -0.0335 335 ILE A CB 2531 C CG1 . ILE A 335 ? 0.5442 0.4679 0.4670 -0.0963 -0.0741 -0.0372 335 ILE A CG1 2532 C CG2 . ILE A 335 ? 0.5470 0.4647 0.4734 -0.0901 -0.0807 -0.0370 335 ILE A CG2 2533 C CD1 . ILE A 335 ? 0.5426 0.4722 0.4656 -0.0942 -0.0700 -0.0453 335 ILE A CD1 2534 N N . ALA A 336 ? 0.5011 0.4302 0.4408 -0.0917 -0.0770 -0.0206 336 ALA A N 2535 C CA . ALA A 336 ? 0.4900 0.4225 0.4323 -0.0916 -0.0749 -0.0168 336 ALA A CA 2536 C C . ALA A 336 ? 0.4665 0.4045 0.4136 -0.0881 -0.0715 -0.0202 336 ALA A C 2537 O O . ALA A 336 ? 0.4651 0.4047 0.4158 -0.0848 -0.0719 -0.0233 336 ALA A O 2538 C CB . ALA A 336 ? 0.4920 0.4240 0.4377 -0.0911 -0.0785 -0.0091 336 ALA A CB 2539 N N . GLY A 337 ? 0.4673 0.4077 0.4138 -0.0889 -0.0682 -0.0197 337 GLY A N 2540 C CA . GLY A 337 ? 0.4467 0.3923 0.3963 -0.0868 -0.0645 -0.0233 337 GLY A CA 2541 C C . GLY A 337 ? 0.4306 0.3783 0.3863 -0.0834 -0.0649 -0.0187 337 GLY A C 2542 O O . GLY A 337 ? 0.4251 0.3711 0.3831 -0.0824 -0.0682 -0.0133 337 GLY A O 2543 N N . PHE A 338 ? 0.4290 0.3805 0.3865 -0.0821 -0.0615 -0.0208 338 PHE A N 2544 C CA . PHE A 338 ? 0.4380 0.3920 0.4014 -0.0784 -0.0615 -0.0175 338 PHE A CA 2545 C C . PHE A 338 ? 0.4594 0.4112 0.4223 -0.0782 -0.0625 -0.0107 338 PHE A C 2546 O O . PHE A 338 ? 0.4687 0.4227 0.4366 -0.0749 -0.0627 -0.0077 338 PHE A O 2547 C CB . PHE A 338 ? 0.4307 0.3893 0.3957 -0.0773 -0.0576 -0.0219 338 PHE A CB 2548 C CG . PHE A 338 ? 0.4508 0.4086 0.4097 -0.0808 -0.0543 -0.0226 338 PHE A CG 2549 C CD1 . PHE A 338 ? 0.4513 0.4095 0.4045 -0.0849 -0.0520 -0.0275 338 PHE A CD1 2550 C CD2 . PHE A 338 ? 0.4706 0.4266 0.4287 -0.0801 -0.0534 -0.0184 338 PHE A CD2 2551 C CE1 . PHE A 338 ? 0.4721 0.4287 0.4186 -0.0889 -0.0491 -0.0281 338 PHE A CE1 2552 C CE2 . PHE A 338 ? 0.4780 0.4315 0.4290 -0.0835 -0.0507 -0.0190 338 PHE A CE2 2553 C CZ . PHE A 338 ? 0.4795 0.4331 0.4244 -0.0883 -0.0486 -0.0237 338 PHE A CZ 2554 N N . ILE A 339 ? 0.4676 0.4154 0.4244 -0.0814 -0.0630 -0.0083 339 ILE A N 2555 C CA . ILE A 339 ? 0.5121 0.4581 0.4680 -0.0804 -0.0638 -0.0022 339 ILE A CA 2556 C C . ILE A 339 ? 0.5161 0.4639 0.4778 -0.0777 -0.0676 0.0031 339 ILE A C 2557 O O . ILE A 339 ? 0.5137 0.4601 0.4747 -0.0795 -0.0706 0.0047 339 ILE A O 2558 C CB . ILE A 339 ? 0.5213 0.4619 0.4685 -0.0841 -0.0638 -0.0010 339 ILE A CB 2559 C CG1 . ILE A 339 ? 0.5318 0.4708 0.4728 -0.0871 -0.0598 -0.0058 339 ILE A CG1 2560 C CG2 . ILE A 339 ? 0.5514 0.4901 0.4976 -0.0821 -0.0655 0.0054 339 ILE A CG2 2561 C CD1 . ILE A 339 ? 0.5429 0.4828 0.4844 -0.0850 -0.0571 -0.0057 339 ILE A CD1 2562 N N . GLU A 340 ? 0.5502 0.5013 0.5173 -0.0739 -0.0673 0.0057 340 GLU A N 2563 C CA . GLU A 340 ? 0.5849 0.5393 0.5583 -0.0715 -0.0705 0.0105 340 GLU A CA 2564 C C . GLU A 340 ? 0.5535 0.5081 0.5295 -0.0726 -0.0733 0.0090 340 GLU A C 2565 O O . GLU A 340 ? 0.5599 0.5150 0.5373 -0.0734 -0.0768 0.0130 340 GLU A O 2566 C CB . GLU A 340 ? 0.6336 0.5880 0.6056 -0.0715 -0.0728 0.0167 340 GLU A CB 2567 C CG . GLU A 340 ? 0.6985 0.6519 0.6676 -0.0692 -0.0706 0.0187 340 GLU A CG 2568 C CD . GLU A 340 ? 0.7809 0.7322 0.7455 -0.0699 -0.0727 0.0231 340 GLU A CD 2569 O OE1 . GLU A 340 ? 0.8576 0.8048 0.8167 -0.0738 -0.0736 0.0218 340 GLU A OE1 2570 O OE2 . GLU A 340 ? 0.8065 0.7605 0.7728 -0.0664 -0.0735 0.0278 340 GLU A OE2 2571 N N . ASN A 341 ? 0.5521 0.5064 0.5284 -0.0724 -0.0718 0.0032 341 ASN A N 2572 C CA . ASN A 341 ? 0.5137 0.4661 0.4900 -0.0734 -0.0744 0.0008 341 ASN A CA 2573 C C . ASN A 341 ? 0.5024 0.4561 0.4808 -0.0711 -0.0727 -0.0052 341 ASN A C 2574 O O . ASN A 341 ? 0.5322 0.4869 0.5085 -0.0715 -0.0693 -0.0101 341 ASN A O 2575 C CB . ASN A 341 ? 0.5250 0.4733 0.4948 -0.0773 -0.0750 -0.0009 341 ASN A CB 2576 C CG . ASN A 341 ? 0.5362 0.4811 0.5045 -0.0784 -0.0781 -0.0032 341 ASN A CG 2577 O OD1 . ASN A 341 ? 0.5189 0.4616 0.4832 -0.0797 -0.0770 -0.0087 341 ASN A OD1 2578 N ND2 . ASN A 341 ? 0.5027 0.4472 0.4739 -0.0780 -0.0818 0.0007 341 ASN A ND2 2579 N N . GLY A 342 ? 0.4644 0.4183 0.4468 -0.0689 -0.0751 -0.0048 342 GLY A N 2580 C CA . GLY A 342 ? 0.4590 0.4135 0.4430 -0.0662 -0.0744 -0.0105 342 GLY A CA 2581 C C . GLY A 342 ? 0.4554 0.4051 0.4362 -0.0669 -0.0776 -0.0133 342 GLY A C 2582 O O . GLY A 342 ? 0.4691 0.4149 0.4473 -0.0694 -0.0809 -0.0098 342 GLY A O 2583 N N . TRP A 343 ? 0.4564 0.4062 0.4370 -0.0643 -0.0768 -0.0196 343 TRP A N 2584 C CA . TRP A 343 ? 0.4496 0.3942 0.4261 -0.0641 -0.0796 -0.0233 343 TRP A CA 2585 C C . TRP A 343 ? 0.4741 0.4162 0.4525 -0.0603 -0.0825 -0.0243 343 TRP A C 2586 O O . TRP A 343 ? 0.4568 0.4019 0.4374 -0.0565 -0.0810 -0.0292 343 TRP A O 2587 C CB . TRP A 343 ? 0.4247 0.3716 0.3983 -0.0637 -0.0765 -0.0306 343 TRP A CB 2588 C CG . TRP A 343 ? 0.4023 0.3497 0.3716 -0.0682 -0.0741 -0.0306 343 TRP A CG 2589 C CD1 . TRP A 343 ? 0.3925 0.3371 0.3593 -0.0722 -0.0753 -0.0250 343 TRP A CD1 2590 C CD2 . TRP A 343 ? 0.3916 0.3424 0.3578 -0.0692 -0.0704 -0.0368 343 TRP A CD2 2591 N NE1 . TRP A 343 ? 0.3872 0.3322 0.3493 -0.0755 -0.0727 -0.0271 343 TRP A NE1 2592 C CE2 . TRP A 343 ? 0.3808 0.3298 0.3424 -0.0742 -0.0695 -0.0341 343 TRP A CE2 2593 C CE3 . TRP A 343 ? 0.3849 0.3410 0.3520 -0.0666 -0.0677 -0.0439 343 TRP A CE3 2594 C CZ2 . TRP A 343 ? 0.3816 0.3329 0.3389 -0.0769 -0.0661 -0.0385 343 TRP A CZ2 2595 C CZ3 . TRP A 343 ? 0.3847 0.3445 0.3480 -0.0694 -0.0641 -0.0484 343 TRP A CZ3 2596 C CH2 . TRP A 343 ? 0.3844 0.3414 0.3426 -0.0747 -0.0633 -0.0457 343 TRP A CH2 2597 N N . GLU A 344 ? 0.5231 0.4598 0.5003 -0.0616 -0.0870 -0.0196 344 GLU A N 2598 C CA . GLU A 344 ? 0.5621 0.4951 0.5401 -0.0584 -0.0902 -0.0201 344 GLU A CA 2599 C C . GLU A 344 ? 0.5561 0.4840 0.5293 -0.0554 -0.0917 -0.0271 344 GLU A C 2600 O O . GLU A 344 ? 0.5344 0.4616 0.5088 -0.0509 -0.0925 -0.0303 344 GLU A O 2601 C CB . GLU A 344 ? 0.6157 0.5444 0.5929 -0.0613 -0.0947 -0.0131 344 GLU A CB 2602 C CG . GLU A 344 ? 0.6472 0.5829 0.6306 -0.0622 -0.0928 -0.0072 344 GLU A CG 2603 C CD . GLU A 344 ? 0.7295 0.6636 0.7132 -0.0652 -0.0967 0.0000 344 GLU A CD 2604 O OE1 . GLU A 344 ? 0.7552 0.6845 0.7376 -0.0646 -0.1003 0.0004 344 GLU A OE1 2605 O OE2 . GLU A 344 ? 0.7579 0.6960 0.7430 -0.0683 -0.0963 0.0050 344 GLU A OE2 2606 N N . GLY A 345 ? 0.5632 0.4880 0.5308 -0.0574 -0.0918 -0.0298 345 GLY A N 2607 C CA . GLY A 345 ? 0.5711 0.4918 0.5337 -0.0540 -0.0927 -0.0371 345 GLY A CA 2608 C C . GLY A 345 ? 0.5719 0.5004 0.5373 -0.0498 -0.0884 -0.0444 345 GLY A C 2609 O O . GLY A 345 ? 0.5688 0.4953 0.5306 -0.0463 -0.0890 -0.0508 345 GLY A O 2610 N N . MET A 346 ? 0.5613 0.4990 0.5328 -0.0502 -0.0840 -0.0436 346 MET A N 2611 C CA . MET A 346 ? 0.5751 0.5216 0.5497 -0.0471 -0.0797 -0.0501 346 MET A CA 2612 C C . MET A 346 ? 0.5757 0.5239 0.5547 -0.0417 -0.0808 -0.0516 346 MET A C 2613 O O . MET A 346 ? 0.5337 0.4853 0.5179 -0.0420 -0.0797 -0.0477 346 MET A O 2614 C CB . MET A 346 ? 0.5953 0.5493 0.5728 -0.0510 -0.0749 -0.0481 346 MET A CB 2615 C CG . MET A 346 ? 0.6164 0.5805 0.5973 -0.0495 -0.0701 -0.0533 346 MET A CG 2616 S SD . MET A 346 ? 0.6740 0.6430 0.6504 -0.0513 -0.0666 -0.0605 346 MET A SD 2617 C CE . MET A 346 ? 0.6818 0.6547 0.6597 -0.0440 -0.0674 -0.0687 346 MET A CE 2618 N N . VAL A 347 ? 0.5714 0.5170 0.5481 -0.0366 -0.0829 -0.0572 347 VAL A N 2619 C CA . VAL A 347 ? 0.5927 0.5377 0.5723 -0.0311 -0.0850 -0.0585 347 VAL A CA 2620 C C . VAL A 347 ? 0.5903 0.5443 0.5730 -0.0257 -0.0823 -0.0663 347 VAL A C 2621 O O . VAL A 347 ? 0.6354 0.5906 0.6213 -0.0212 -0.0835 -0.0674 347 VAL A O 2622 C CB . VAL A 347 ? 0.6413 0.5735 0.6148 -0.0289 -0.0913 -0.0576 347 VAL A CB 2623 C CG1 . VAL A 347 ? 0.6445 0.5695 0.6163 -0.0344 -0.0942 -0.0493 347 VAL A CG1 2624 C CG2 . VAL A 347 ? 0.6411 0.5685 0.6075 -0.0268 -0.0928 -0.0636 347 VAL A CG2 2625 N N . ASP A 348 ? 0.5718 0.5327 0.5535 -0.0261 -0.0788 -0.0718 348 ASP A N 2626 C CA . ASP A 348 ? 0.5677 0.5392 0.5525 -0.0214 -0.0760 -0.0793 348 ASP A CA 2627 C C . ASP A 348 ? 0.5360 0.5198 0.5258 -0.0251 -0.0702 -0.0796 348 ASP A C 2628 O O . ASP A 348 ? 0.5320 0.5266 0.5244 -0.0228 -0.0671 -0.0858 348 ASP A O 2629 C CB . ASP A 348 ? 0.6217 0.5932 0.6012 -0.0185 -0.0764 -0.0865 348 ASP A CB 2630 C CG . ASP A 348 ? 0.6627 0.6352 0.6385 -0.0245 -0.0737 -0.0863 348 ASP A CG 2631 O OD1 . ASP A 348 ? 0.6684 0.6365 0.6434 -0.0306 -0.0735 -0.0796 348 ASP A OD1 2632 O OD2 . ASP A 348 ? 0.7283 0.7061 0.7016 -0.0228 -0.0718 -0.0930 348 ASP A OD2 2633 N N . GLY A 349 ? 0.4948 0.4769 0.4856 -0.0308 -0.0689 -0.0729 349 GLY A N 2634 C CA . GLY A 349 ? 0.4513 0.4428 0.4455 -0.0347 -0.0638 -0.0725 349 GLY A CA 2635 C C . GLY A 349 ? 0.4200 0.4071 0.4152 -0.0390 -0.0637 -0.0643 349 GLY A C 2636 O O . GLY A 349 ? 0.4178 0.3961 0.4110 -0.0401 -0.0671 -0.0591 349 GLY A O 2637 N N . TRP A 350 ? 0.3892 0.3828 0.3871 -0.0416 -0.0598 -0.0632 350 TRP A N 2638 C CA . TRP A 350 ? 0.3724 0.3625 0.3707 -0.0453 -0.0594 -0.0559 350 TRP A CA 2639 C C . TRP A 350 ? 0.3575 0.3457 0.3511 -0.0510 -0.0575 -0.0537 350 TRP A C 2640 O O . TRP A 350 ? 0.3503 0.3332 0.3430 -0.0533 -0.0587 -0.0474 350 TRP A O 2641 C CB . TRP A 350 ? 0.3677 0.3639 0.3702 -0.0450 -0.0565 -0.0554 350 TRP A CB 2642 C CG . TRP A 350 ? 0.3750 0.3705 0.3821 -0.0399 -0.0590 -0.0547 350 TRP A CG 2643 C CD1 . TRP A 350 ? 0.3898 0.3816 0.3976 -0.0352 -0.0630 -0.0564 350 TRP A CD1 2644 C CD2 . TRP A 350 ? 0.3651 0.3632 0.3762 -0.0391 -0.0577 -0.0520 350 TRP A CD2 2645 N NE1 . TRP A 350 ? 0.3980 0.3899 0.4099 -0.0318 -0.0643 -0.0548 350 TRP A NE1 2646 C CE2 . TRP A 350 ? 0.3763 0.3724 0.3907 -0.0340 -0.0611 -0.0523 350 TRP A CE2 2647 C CE3 . TRP A 350 ? 0.3644 0.3652 0.3759 -0.0421 -0.0544 -0.0495 350 TRP A CE3 2648 C CZ2 . TRP A 350 ? 0.3764 0.3739 0.3947 -0.0321 -0.0610 -0.0500 350 TRP A CZ2 2649 C CZ3 . TRP A 350 ? 0.3571 0.3593 0.3725 -0.0399 -0.0542 -0.0474 350 TRP A CZ3 2650 C CH2 . TRP A 350 ? 0.3573 0.3581 0.3762 -0.0351 -0.0574 -0.0476 350 TRP A CH2 2651 N N . TYR A 351 ? 0.3521 0.3455 0.3428 -0.0532 -0.0546 -0.0590 351 TYR A N 2652 C CA . TYR A 351 ? 0.3502 0.3419 0.3354 -0.0589 -0.0527 -0.0579 351 TYR A CA 2653 C C . TYR A 351 ? 0.3656 0.3581 0.3470 -0.0591 -0.0529 -0.0634 351 TYR A C 2654 O O . TYR A 351 ? 0.3653 0.3629 0.3486 -0.0551 -0.0529 -0.0694 351 TYR A O 2655 C CB . TYR A 351 ? 0.3536 0.3518 0.3379 -0.0626 -0.0481 -0.0593 351 TYR A CB 2656 C CG . TYR A 351 ? 0.3435 0.3418 0.3313 -0.0619 -0.0474 -0.0551 351 TYR A CG 2657 C CD1 . TYR A 351 ? 0.3426 0.3345 0.3282 -0.0644 -0.0478 -0.0484 351 TYR A CD1 2658 C CD2 . TYR A 351 ? 0.3354 0.3399 0.3284 -0.0583 -0.0466 -0.0578 351 TYR A CD2 2659 C CE1 . TYR A 351 ? 0.3388 0.3306 0.3271 -0.0633 -0.0472 -0.0446 351 TYR A CE1 2660 C CE2 . TYR A 351 ? 0.3389 0.3431 0.3346 -0.0578 -0.0460 -0.0539 351 TYR A CE2 2661 C CZ . TYR A 351 ? 0.3346 0.3321 0.3277 -0.0602 -0.0462 -0.0474 351 TYR A CZ 2662 O OH . TYR A 351 ? 0.3578 0.3545 0.3529 -0.0593 -0.0456 -0.0436 351 TYR A OH 2663 N N . GLY A 352 ? 0.3700 0.3574 0.3457 -0.0634 -0.0531 -0.0615 352 GLY A N 2664 C CA . GLY A 352 ? 0.3831 0.3711 0.3544 -0.0640 -0.0530 -0.0668 352 GLY A CA 2665 C C . GLY A 352 ? 0.3919 0.3746 0.3565 -0.0697 -0.0528 -0.0644 352 GLY A C 2666 O O . GLY A 352 ? 0.3725 0.3520 0.3354 -0.0737 -0.0522 -0.0591 352 GLY A O 2667 N N . PHE A 353 ? 0.3932 0.3743 0.3537 -0.0696 -0.0537 -0.0684 353 PHE A N 2668 C CA . PHE A 353 ? 0.4064 0.3834 0.3599 -0.0749 -0.0533 -0.0677 353 PHE A CA 2669 C C . PHE A 353 ? 0.4052 0.3730 0.3557 -0.0734 -0.0579 -0.0662 353 PHE A C 2670 O O . PHE A 353 ? 0.4135 0.3806 0.3653 -0.0682 -0.0602 -0.0696 353 PHE A O 2671 C CB . PHE A 353 ? 0.4147 0.3996 0.3649 -0.0765 -0.0495 -0.0754 353 PHE A CB 2672 C CG . PHE A 353 ? 0.4234 0.4185 0.3753 -0.0790 -0.0447 -0.0780 353 PHE A CG 2673 C CD1 . PHE A 353 ? 0.4259 0.4206 0.3727 -0.0860 -0.0420 -0.0760 353 PHE A CD1 2674 C CD2 . PHE A 353 ? 0.4192 0.4240 0.3769 -0.0747 -0.0431 -0.0829 353 PHE A CD2 2675 C CE1 . PHE A 353 ? 0.4327 0.4360 0.3798 -0.0891 -0.0377 -0.0785 353 PHE A CE1 2676 C CE2 . PHE A 353 ? 0.4312 0.4459 0.3900 -0.0776 -0.0387 -0.0853 353 PHE A CE2 2677 C CZ . PHE A 353 ? 0.4377 0.4514 0.3909 -0.0852 -0.0360 -0.0832 353 PHE A CZ 2678 N N . ARG A 354 ? 0.4063 0.3668 0.3523 -0.0778 -0.0596 -0.0611 354 ARG A N 2679 C CA . ARG A 354 ? 0.4104 0.3624 0.3514 -0.0781 -0.0635 -0.0604 354 ARG A CA 2680 C C . ARG A 354 ? 0.4145 0.3651 0.3482 -0.0838 -0.0618 -0.0615 354 ARG A C 2681 O O . ARG A 354 ? 0.4174 0.3699 0.3495 -0.0883 -0.0591 -0.0593 354 ARG A O 2682 C CB . ARG A 354 ? 0.4191 0.3634 0.3614 -0.0785 -0.0680 -0.0525 354 ARG A CB 2683 C CG . ARG A 354 ? 0.4321 0.3750 0.3793 -0.0731 -0.0710 -0.0518 354 ARG A CG 2684 C CD . ARG A 354 ? 0.4418 0.3781 0.3899 -0.0742 -0.0753 -0.0440 354 ARG A CD 2685 N NE . ARG A 354 ? 0.4432 0.3784 0.3957 -0.0695 -0.0779 -0.0433 354 ARG A NE 2686 C CZ . ARG A 354 ? 0.4410 0.3725 0.3958 -0.0698 -0.0814 -0.0369 354 ARG A CZ 2687 N NH1 . ARG A 354 ? 0.4476 0.3769 0.4014 -0.0740 -0.0828 -0.0305 354 ARG A NH1 2688 N NH2 . ARG A 354 ? 0.4620 0.3924 0.4200 -0.0658 -0.0836 -0.0370 354 ARG A NH2 2689 N N . HIS A 355 ? 0.4198 0.3663 0.3481 -0.0837 -0.0633 -0.0650 355 HIS A N 2690 C CA . HIS A 355 ? 0.4275 0.3730 0.3485 -0.0891 -0.0615 -0.0666 355 HIS A CA 2691 C C . HIS A 355 ? 0.4470 0.3826 0.3620 -0.0902 -0.0657 -0.0649 355 HIS A C 2692 O O . HIS A 355 ? 0.4399 0.3703 0.3556 -0.0861 -0.0695 -0.0648 355 HIS A O 2693 C CB . HIS A 355 ? 0.4325 0.3872 0.3522 -0.0885 -0.0570 -0.0752 355 HIS A CB 2694 C CG . HIS A 355 ? 0.4465 0.4013 0.3654 -0.0826 -0.0585 -0.0816 355 HIS A CG 2695 N ND1 . HIS A 355 ? 0.4419 0.4026 0.3667 -0.0762 -0.0582 -0.0854 355 HIS A ND1 2696 C CD2 . HIS A 355 ? 0.4638 0.4123 0.3758 -0.0821 -0.0606 -0.0846 355 HIS A CD2 2697 C CE1 . HIS A 355 ? 0.4684 0.4266 0.3900 -0.0714 -0.0602 -0.0908 355 HIS A CE1 2698 N NE2 . HIS A 355 ? 0.4613 0.4119 0.3750 -0.0750 -0.0616 -0.0903 355 HIS A NE2 2699 N N . GLN A 356 ? 0.4635 0.3955 0.3721 -0.0960 -0.0652 -0.0632 356 GLN A N 2700 C CA . GLN A 356 ? 0.4868 0.4102 0.3880 -0.0982 -0.0684 -0.0629 356 GLN A CA 2701 C C . GLN A 356 ? 0.4833 0.4093 0.3776 -0.1021 -0.0647 -0.0682 356 GLN A C 2702 O O . GLN A 356 ? 0.4592 0.3888 0.3521 -0.1068 -0.0615 -0.0673 356 GLN A O 2703 C CB . GLN A 356 ? 0.5245 0.4404 0.4242 -0.1022 -0.0721 -0.0543 356 GLN A CB 2704 C CG . GLN A 356 ? 0.5784 0.4847 0.4708 -0.1046 -0.0762 -0.0531 356 GLN A CG 2705 C CD . GLN A 356 ? 0.6282 0.5287 0.5205 -0.1079 -0.0802 -0.0444 356 GLN A CD 2706 O OE1 . GLN A 356 ? 0.7405 0.6333 0.6287 -0.1092 -0.0846 -0.0421 356 GLN A OE1 2707 N NE2 . GLN A 356 ? 0.6892 0.5935 0.5856 -0.1093 -0.0789 -0.0396 356 GLN A NE2 2708 N N . ASN A 357 ? 0.4811 0.4052 0.3706 -0.1002 -0.0653 -0.0740 357 ASN A N 2709 C CA . ASN A 357 ? 0.4818 0.4086 0.3643 -0.1037 -0.0619 -0.0795 357 ASN A CA 2710 C C . ASN A 357 ? 0.5174 0.4353 0.3924 -0.1028 -0.0653 -0.0818 357 ASN A C 2711 O O . ASN A 357 ? 0.4889 0.3975 0.3634 -0.1012 -0.0704 -0.0776 357 ASN A O 2712 C CB . ASN A 357 ? 0.4840 0.4239 0.3699 -0.1011 -0.0567 -0.0872 357 ASN A CB 2713 C CG . ASN A 357 ? 0.4752 0.4180 0.3645 -0.0928 -0.0576 -0.0930 357 ASN A CG 2714 O OD1 . ASN A 357 ? 0.4789 0.4125 0.3660 -0.0891 -0.0623 -0.0923 357 ASN A OD1 2715 N ND2 . ASN A 357 ? 0.4572 0.4126 0.3507 -0.0900 -0.0534 -0.0991 357 ASN A ND2 2716 N N . SER A 358 ? 0.5544 0.4750 0.4229 -0.1047 -0.0624 -0.0880 358 SER A N 2717 C CA . SER A 358 ? 0.6007 0.5136 0.4609 -0.1039 -0.0647 -0.0915 358 SER A CA 2718 C C . SER A 358 ? 0.6021 0.5106 0.4632 -0.0960 -0.0682 -0.0943 358 SER A C 2719 O O . SER A 358 ? 0.6507 0.5479 0.5049 -0.0956 -0.0725 -0.0938 358 SER A O 2720 C CB . SER A 358 ? 0.6205 0.5412 0.4755 -0.1056 -0.0596 -0.0993 358 SER A CB 2721 O OG . SER A 358 ? 0.6561 0.5914 0.5176 -0.1039 -0.0545 -0.1037 358 SER A OG 2722 N N . GLU A 359 ? 0.5851 0.5020 0.4540 -0.0900 -0.0666 -0.0975 359 GLU A N 2723 C CA . GLU A 359 ? 0.5937 0.5080 0.4634 -0.0816 -0.0694 -0.1016 359 GLU A CA 2724 C C . GLU A 359 ? 0.5830 0.4900 0.4575 -0.0788 -0.0743 -0.0953 359 GLU A C 2725 O O . GLU A 359 ? 0.5874 0.4904 0.4616 -0.0721 -0.0772 -0.0982 359 GLU A O 2726 C CB . GLU A 359 ? 0.5977 0.5264 0.4725 -0.0761 -0.0647 -0.1096 359 GLU A CB 2727 C CG . GLU A 359 ? 0.6297 0.5675 0.5001 -0.0786 -0.0596 -0.1164 359 GLU A CG 2728 C CD . GLU A 359 ? 0.6472 0.5996 0.5218 -0.0723 -0.0556 -0.1253 359 GLU A CD 2729 O OE1 . GLU A 359 ? 0.6977 0.6484 0.5697 -0.0647 -0.0574 -0.1312 359 GLU A OE1 2730 O OE2 . GLU A 359 ? 0.6568 0.6228 0.5373 -0.0746 -0.0508 -0.1266 359 GLU A OE2 2731 N N . GLY A 360 ? 0.5387 0.4441 0.4169 -0.0839 -0.0753 -0.0871 360 GLY A N 2732 C CA . GLY A 360 ? 0.5204 0.4194 0.4027 -0.0825 -0.0799 -0.0805 360 GLY A CA 2733 C C . GLY A 360 ? 0.5038 0.4108 0.3956 -0.0837 -0.0777 -0.0757 360 GLY A C 2734 O O . GLY A 360 ? 0.4773 0.3913 0.3706 -0.0878 -0.0736 -0.0751 360 GLY A O 2735 N N . ILE A 361 ? 0.4988 0.4038 0.3959 -0.0801 -0.0806 -0.0723 361 ILE A N 2736 C CA . ILE A 361 ? 0.5082 0.4193 0.4141 -0.0804 -0.0793 -0.0675 361 ILE A CA 2737 C C . ILE A 361 ? 0.5017 0.4177 0.4134 -0.0734 -0.0788 -0.0714 361 ILE A C 2738 O O . ILE A 361 ? 0.5047 0.4138 0.4140 -0.0689 -0.0827 -0.0730 361 ILE A O 2739 C CB . ILE A 361 ? 0.5252 0.4290 0.4322 -0.0832 -0.0839 -0.0585 361 ILE A CB 2740 C CG1 . ILE A 361 ? 0.5409 0.4418 0.4437 -0.0901 -0.0841 -0.0538 361 ILE A CG1 2741 C CG2 . ILE A 361 ? 0.5436 0.4534 0.4598 -0.0814 -0.0830 -0.0544 361 ILE A CG2 2742 C CD1 . ILE A 361 ? 0.5811 0.4709 0.4759 -0.0928 -0.0890 -0.0517 361 ILE A CD1 2743 N N . GLY A 362 ? 0.4761 0.4031 0.3943 -0.0724 -0.0744 -0.0731 362 GLY A N 2744 C CA . GLY A 362 ? 0.4758 0.4089 0.3995 -0.0657 -0.0735 -0.0776 362 GLY A CA 2745 C C . GLY A 362 ? 0.4751 0.4153 0.4072 -0.0658 -0.0714 -0.0740 362 GLY A C 2746 O O . GLY A 362 ? 0.4556 0.3969 0.3890 -0.0709 -0.0700 -0.0687 362 GLY A O 2747 N N . GLN A 363 ? 0.4783 0.4231 0.4156 -0.0598 -0.0714 -0.0772 363 GLN A N 2748 C CA . GLN A 363 ? 0.4722 0.4238 0.4174 -0.0588 -0.0695 -0.0747 363 GLN A CA 2749 C C . GLN A 363 ? 0.4751 0.4369 0.4242 -0.0534 -0.0667 -0.0822 363 GLN A C 2750 O O . GLN A 363 ? 0.4636 0.4240 0.4105 -0.0479 -0.0685 -0.0877 363 GLN A O 2751 C CB . GLN A 363 ? 0.4894 0.4332 0.4370 -0.0569 -0.0742 -0.0687 363 GLN A CB 2752 C CG . GLN A 363 ? 0.5022 0.4517 0.4578 -0.0555 -0.0729 -0.0656 363 GLN A CG 2753 C CD . GLN A 363 ? 0.5122 0.4538 0.4692 -0.0547 -0.0776 -0.0592 363 GLN A CD 2754 O OE1 . GLN A 363 ? 0.5355 0.4731 0.4918 -0.0590 -0.0790 -0.0525 363 GLN A OE1 2755 N NE2 . GLN A 363 ? 0.5492 0.4883 0.5075 -0.0491 -0.0803 -0.0613 363 GLN A NE2 2756 N N . ALA A 364 ? 0.4470 0.4190 0.4015 -0.0547 -0.0625 -0.0825 364 ALA A N 2757 C CA . ALA A 364 ? 0.4374 0.4206 0.3969 -0.0500 -0.0599 -0.0886 364 ALA A CA 2758 C C . ALA A 364 ? 0.4348 0.4234 0.4008 -0.0514 -0.0578 -0.0848 364 ALA A C 2759 O O . ALA A 364 ? 0.3988 0.3875 0.3643 -0.0572 -0.0556 -0.0804 364 ALA A O 2760 C CB . ALA A 364 ? 0.4329 0.4264 0.3901 -0.0515 -0.0554 -0.0958 364 ALA A CB 2761 N N . ALA A 365 ? 0.4524 0.4450 0.4238 -0.0457 -0.0585 -0.0868 365 ALA A N 2762 C CA . ALA A 365 ? 0.4498 0.4482 0.4274 -0.0461 -0.0565 -0.0842 365 ALA A CA 2763 C C . ALA A 365 ? 0.4646 0.4760 0.4434 -0.0491 -0.0510 -0.0887 365 ALA A C 2764 O O . ALA A 365 ? 0.4634 0.4821 0.4406 -0.0480 -0.0491 -0.0955 365 ALA A O 2765 C CB . ALA A 365 ? 0.4564 0.4550 0.4387 -0.0390 -0.0592 -0.0855 365 ALA A CB 2766 N N . ASP A 366 ? 0.4436 0.4577 0.4246 -0.0531 -0.0484 -0.0848 366 ASP A N 2767 C CA . ASP A 366 ? 0.4669 0.4929 0.4489 -0.0564 -0.0435 -0.0886 366 ASP A CA 2768 C C . ASP A 366 ? 0.4841 0.5172 0.4729 -0.0522 -0.0431 -0.0900 366 ASP A C 2769 O O . ASP A 366 ? 0.4570 0.4857 0.4486 -0.0520 -0.0442 -0.0845 366 ASP A O 2770 C CB . ASP A 366 ? 0.4732 0.4963 0.4514 -0.0641 -0.0410 -0.0836 366 ASP A CB 2771 C CG . ASP A 366 ? 0.4929 0.5272 0.4705 -0.0686 -0.0360 -0.0873 366 ASP A CG 2772 O OD1 . ASP A 366 ? 0.5015 0.5427 0.4759 -0.0711 -0.0336 -0.0927 366 ASP A OD1 2773 O OD2 . ASP A 366 ? 0.4829 0.5192 0.4627 -0.0701 -0.0346 -0.0848 366 ASP A OD2 2774 N N . LEU A 367 ? 0.5015 0.5462 0.4929 -0.0489 -0.0414 -0.0974 367 LEU A N 2775 C CA . LEU A 367 ? 0.5200 0.5716 0.5179 -0.0434 -0.0419 -0.0996 367 LEU A CA 2776 C C . LEU A 367 ? 0.5075 0.5652 0.5076 -0.0480 -0.0385 -0.0976 367 LEU A C 2777 O O . LEU A 367 ? 0.4838 0.5401 0.4881 -0.0454 -0.0397 -0.0947 367 LEU A O 2778 C CB . LEU A 367 ? 0.5674 0.6307 0.5672 -0.0381 -0.0412 -0.1085 367 LEU A CB 2779 C CG . LEU A 367 ? 0.6038 0.6775 0.6104 -0.0326 -0.0411 -0.1122 367 LEU A CG 2780 C CD1 . LEU A 367 ? 0.6180 0.6814 0.6274 -0.0268 -0.0459 -0.1081 367 LEU A CD1 2781 C CD2 . LEU A 367 ? 0.6285 0.7146 0.6364 -0.0273 -0.0404 -0.1213 367 LEU A CD2 2782 N N . LYS A 368 ? 0.5094 0.5735 0.5059 -0.0549 -0.0343 -0.0992 368 LYS A N 2783 C CA . LYS A 368 ? 0.5264 0.5962 0.5234 -0.0600 -0.0309 -0.0979 368 LYS A CA 2784 C C . LYS A 368 ? 0.4971 0.5556 0.4938 -0.0614 -0.0324 -0.0898 368 LYS A C 2785 O O . LYS A 368 ? 0.4731 0.5338 0.4735 -0.0602 -0.0321 -0.0883 368 LYS A O 2786 C CB . LYS A 368 ? 0.5719 0.6471 0.5628 -0.0683 -0.0267 -0.0999 368 LYS A CB 2787 C CG . LYS A 368 ? 0.6236 0.7041 0.6133 -0.0745 -0.0232 -0.0989 368 LYS A CG 2788 C CD . LYS A 368 ? 0.6827 0.7773 0.6697 -0.0802 -0.0189 -0.1052 368 LYS A CD 2789 C CE . LYS A 368 ? 0.7175 0.8144 0.7005 -0.0882 -0.0157 -0.1033 368 LYS A CE 2790 N NZ . LYS A 368 ? 0.7495 0.8317 0.7241 -0.0942 -0.0158 -0.0967 368 LYS A NZ 2791 N N . SER A 369 ? 0.4662 0.5130 0.4583 -0.0639 -0.0339 -0.0846 369 SER A N 2792 C CA . SER A 369 ? 0.4455 0.4819 0.4368 -0.0651 -0.0352 -0.0768 369 SER A CA 2793 C C . SER A 369 ? 0.4251 0.4577 0.4225 -0.0583 -0.0388 -0.0742 369 SER A C 2794 O O . SER A 369 ? 0.3941 0.4245 0.3936 -0.0579 -0.0389 -0.0702 369 SER A O 2795 C CB . SER A 369 ? 0.4433 0.4693 0.4286 -0.0688 -0.0363 -0.0722 369 SER A CB 2796 O OG . SER A 369 ? 0.4640 0.4853 0.4499 -0.0649 -0.0398 -0.0725 369 SER A OG 2797 N N . THR A 370 ? 0.4209 0.4520 0.4203 -0.0531 -0.0420 -0.0764 370 THR A N 2798 C CA . THR A 370 ? 0.4144 0.4416 0.4186 -0.0469 -0.0457 -0.0745 370 THR A CA 2799 C C . THR A 370 ? 0.4273 0.4629 0.4368 -0.0439 -0.0445 -0.0771 370 THR A C 2800 O O . THR A 370 ? 0.4123 0.4445 0.4249 -0.0420 -0.0458 -0.0730 370 THR A O 2801 C CB . THR A 370 ? 0.4165 0.4407 0.4203 -0.0420 -0.0492 -0.0777 370 THR A CB 2802 O OG1 . THR A 370 ? 0.4020 0.4176 0.4007 -0.0450 -0.0506 -0.0746 370 THR A OG1 2803 C CG2 . THR A 370 ? 0.4083 0.4277 0.4160 -0.0357 -0.0533 -0.0759 370 THR A CG2 2804 N N . GLN A 371 ? 0.4448 0.4921 0.4554 -0.0438 -0.0419 -0.0839 371 GLN A N 2805 C CA . GLN A 371 ? 0.4683 0.5250 0.4840 -0.0408 -0.0410 -0.0872 371 GLN A CA 2806 C C . GLN A 371 ? 0.4533 0.5117 0.4688 -0.0458 -0.0380 -0.0838 371 GLN A C 2807 O O . GLN A 371 ? 0.4554 0.5161 0.4750 -0.0432 -0.0384 -0.0832 371 GLN A O 2808 C CB . GLN A 371 ? 0.5078 0.5782 0.5248 -0.0393 -0.0390 -0.0957 371 GLN A CB 2809 C CG . GLN A 371 ? 0.5460 0.6261 0.5693 -0.0338 -0.0395 -0.0997 371 GLN A CG 2810 C CD . GLN A 371 ? 0.5660 0.6383 0.5921 -0.0259 -0.0445 -0.0985 371 GLN A CD 2811 O OE1 . GLN A 371 ? 0.6302 0.6955 0.6541 -0.0224 -0.0476 -0.0992 371 GLN A OE1 2812 N NE2 . GLN A 371 ? 0.5920 0.6647 0.6222 -0.0234 -0.0455 -0.0966 371 GLN A NE2 2813 N N . ALA A 372 ? 0.4318 0.4884 0.4418 -0.0528 -0.0352 -0.0819 372 ALA A N 2814 C CA . ALA A 372 ? 0.4402 0.4958 0.4480 -0.0579 -0.0327 -0.0783 372 ALA A CA 2815 C C . ALA A 372 ? 0.4242 0.4693 0.4333 -0.0555 -0.0351 -0.0712 372 ALA A C 2816 O O . ALA A 372 ? 0.4156 0.4618 0.4262 -0.0557 -0.0341 -0.0695 372 ALA A O 2817 C CB . ALA A 372 ? 0.4362 0.4891 0.4362 -0.0655 -0.0300 -0.0771 372 ALA A CB 2818 N N . ALA A 373 ? 0.4063 0.4419 0.4149 -0.0534 -0.0382 -0.0672 373 ALA A N 2819 C CA . ALA A 373 ? 0.4005 0.4272 0.4105 -0.0512 -0.0405 -0.0605 373 ALA A CA 2820 C C . ALA A 373 ? 0.4014 0.4302 0.4177 -0.0451 -0.0429 -0.0614 373 ALA A C 2821 O O . ALA A 373 ? 0.4015 0.4290 0.4198 -0.0441 -0.0428 -0.0582 373 ALA A O 2822 C CB . ALA A 373 ? 0.4063 0.4237 0.4139 -0.0513 -0.0432 -0.0560 373 ALA A CB 2823 N N . ILE A 374 ? 0.4040 0.4358 0.4228 -0.0408 -0.0450 -0.0659 374 ILE A N 2824 C CA . ILE A 374 ? 0.4200 0.4533 0.4439 -0.0347 -0.0477 -0.0673 374 ILE A CA 2825 C C . ILE A 374 ? 0.4265 0.4687 0.4537 -0.0343 -0.0453 -0.0700 374 ILE A C 2826 O O . ILE A 374 ? 0.4032 0.4436 0.4335 -0.0314 -0.0468 -0.0676 374 ILE A O 2827 C CB . ILE A 374 ? 0.4275 0.4621 0.4521 -0.0299 -0.0504 -0.0724 374 ILE A CB 2828 C CG1 . ILE A 374 ? 0.4376 0.4609 0.4592 -0.0296 -0.0539 -0.0684 374 ILE A CG1 2829 C CG2 . ILE A 374 ? 0.4295 0.4678 0.4588 -0.0236 -0.0526 -0.0755 374 ILE A CG2 2830 C CD1 . ILE A 374 ? 0.4374 0.4597 0.4574 -0.0257 -0.0566 -0.0732 374 ILE A CD1 2831 N N . ASN A 375 ? 0.4266 0.4785 0.4527 -0.0378 -0.0418 -0.0747 375 ASN A N 2832 C CA . ASN A 375 ? 0.4555 0.5170 0.4842 -0.0383 -0.0395 -0.0776 375 ASN A CA 2833 C C . ASN A 375 ? 0.4414 0.4979 0.4688 -0.0413 -0.0382 -0.0720 375 ASN A C 2834 O O . ASN A 375 ? 0.4489 0.5083 0.4797 -0.0391 -0.0385 -0.0720 375 ASN A O 2835 C CB . ASN A 375 ? 0.4678 0.5411 0.4948 -0.0427 -0.0358 -0.0834 375 ASN A CB 2836 C CG . ASN A 375 ? 0.4972 0.5795 0.5271 -0.0382 -0.0367 -0.0905 375 ASN A CG 2837 O OD1 . ASN A 375 ? 0.5082 0.5880 0.5414 -0.0312 -0.0404 -0.0915 375 ASN A OD1 2838 N ND2 . ASN A 375 ? 0.5263 0.6188 0.5543 -0.0422 -0.0335 -0.0955 375 ASN A ND2 2839 N N . GLN A 376 ? 0.4159 0.4647 0.4380 -0.0461 -0.0370 -0.0673 376 GLN A N 2840 C CA . GLN A 376 ? 0.4284 0.4716 0.4479 -0.0488 -0.0357 -0.0621 376 GLN A CA 2841 C C . GLN A 376 ? 0.4041 0.4403 0.4270 -0.0439 -0.0387 -0.0573 376 GLN A C 2842 O O . GLN A 376 ? 0.3833 0.4185 0.4068 -0.0437 -0.0381 -0.0550 376 GLN A O 2843 C CB . GLN A 376 ? 0.4366 0.4726 0.4489 -0.0542 -0.0342 -0.0585 376 GLN A CB 2844 C CG . GLN A 376 ? 0.4683 0.5105 0.4758 -0.0604 -0.0307 -0.0626 376 GLN A CG 2845 C CD . GLN A 376 ? 0.4686 0.5023 0.4682 -0.0654 -0.0297 -0.0589 376 GLN A CD 2846 O OE1 . GLN A 376 ? 0.5211 0.5474 0.5164 -0.0672 -0.0291 -0.0543 376 GLN A OE1 2847 N NE2 . GLN A 376 ? 0.5462 0.5805 0.5435 -0.0674 -0.0296 -0.0610 376 GLN A NE2 2848 N N . ILE A 377 ? 0.3803 0.4115 0.4049 -0.0404 -0.0420 -0.0558 377 ILE A N 2849 C CA . ILE A 377 ? 0.3858 0.4106 0.4133 -0.0364 -0.0451 -0.0512 377 ILE A CA 2850 C C . ILE A 377 ? 0.3941 0.4242 0.4267 -0.0318 -0.0464 -0.0544 377 ILE A C 2851 O O . ILE A 377 ? 0.4088 0.4368 0.4431 -0.0303 -0.0469 -0.0514 377 ILE A O 2852 C CB . ILE A 377 ? 0.3730 0.3910 0.4000 -0.0348 -0.0484 -0.0486 377 ILE A CB 2853 C CG1 . ILE A 377 ? 0.3804 0.3925 0.4027 -0.0391 -0.0472 -0.0437 377 ILE A CG1 2854 C CG2 . ILE A 377 ? 0.3650 0.3780 0.3953 -0.0306 -0.0519 -0.0449 377 ILE A CG2 2855 C CD1 . ILE A 377 ? 0.3839 0.3905 0.4049 -0.0388 -0.0500 -0.0417 377 ILE A CD1 2856 N N . ASN A 378 ? 0.4058 0.4429 0.4404 -0.0296 -0.0470 -0.0607 378 ASN A N 2857 C CA . ASN A 378 ? 0.4338 0.4768 0.4730 -0.0249 -0.0483 -0.0643 378 ASN A CA 2858 C C . ASN A 378 ? 0.4443 0.4934 0.4842 -0.0273 -0.0453 -0.0649 378 ASN A C 2859 O O . ASN A 378 ? 0.4495 0.4998 0.4927 -0.0240 -0.0467 -0.0648 378 ASN A O 2860 C CB . ASN A 378 ? 0.4522 0.5027 0.4930 -0.0217 -0.0493 -0.0714 378 ASN A CB 2861 C CG . ASN A 378 ? 0.4771 0.5200 0.5174 -0.0174 -0.0536 -0.0711 378 ASN A CG 2862 O OD1 . ASN A 378 ? 0.4817 0.5148 0.5214 -0.0163 -0.0563 -0.0657 378 ASN A OD1 2863 N ND2 . ASN A 378 ? 0.5007 0.5481 0.5407 -0.0150 -0.0543 -0.0769 378 ASN A ND2 2864 N N . GLY A 379 ? 0.4393 0.4917 0.4756 -0.0332 -0.0415 -0.0654 379 GLY A N 2865 C CA . GLY A 379 ? 0.4776 0.5339 0.5127 -0.0367 -0.0386 -0.0652 379 GLY A CA 2866 C C . GLY A 379 ? 0.4906 0.5383 0.5252 -0.0358 -0.0394 -0.0591 379 GLY A C 2867 O O . GLY A 379 ? 0.4407 0.4911 0.4775 -0.0344 -0.0394 -0.0594 379 GLY A O 2868 N N . LYS A 380 ? 0.4637 0.5016 0.4955 -0.0365 -0.0401 -0.0535 380 LYS A N 2869 C CA . LYS A 380 ? 0.4697 0.5002 0.5009 -0.0355 -0.0406 -0.0477 380 LYS A CA 2870 C C . LYS A 380 ? 0.4457 0.4745 0.4820 -0.0298 -0.0441 -0.0465 380 LYS A C 2871 O O . LYS A 380 ? 0.4895 0.5163 0.5266 -0.0286 -0.0442 -0.0440 380 LYS A O 2872 C CB . LYS A 380 ? 0.4733 0.4951 0.4995 -0.0380 -0.0399 -0.0421 380 LYS A CB 2873 C CG . LYS A 380 ? 0.4836 0.5010 0.5105 -0.0365 -0.0423 -0.0400 380 LYS A CG 2874 C CD . LYS A 380 ? 0.4705 0.4802 0.4927 -0.0388 -0.0416 -0.0342 380 LYS A CD 2875 C CE . LYS A 380 ? 0.4665 0.4759 0.4823 -0.0440 -0.0387 -0.0355 380 LYS A CE 2876 N NZ . LYS A 380 ? 0.4433 0.4447 0.4541 -0.0453 -0.0382 -0.0298 380 LYS A NZ 2877 N N . LEU A 381 ? 0.4365 0.4656 0.4756 -0.0265 -0.0471 -0.0485 381 LEU A N 2878 C CA . LEU A 381 ? 0.4376 0.4649 0.4805 -0.0213 -0.0507 -0.0483 381 LEU A CA 2879 C C . LEU A 381 ? 0.4780 0.5125 0.5240 -0.0192 -0.0505 -0.0522 381 LEU A C 2880 O O . LEU A 381 ? 0.4770 0.5090 0.5248 -0.0166 -0.0521 -0.0501 381 LEU A O 2881 C CB . LEU A 381 ? 0.4628 0.4888 0.5067 -0.0182 -0.0541 -0.0507 381 LEU A CB 2882 C CG . LEU A 381 ? 0.4482 0.4656 0.4896 -0.0193 -0.0558 -0.0458 381 LEU A CG 2883 C CD1 . LEU A 381 ? 0.4482 0.4636 0.4895 -0.0165 -0.0593 -0.0487 381 LEU A CD1 2884 C CD2 . LEU A 381 ? 0.4467 0.4578 0.4888 -0.0184 -0.0574 -0.0396 381 LEU A CD2 2885 N N . ASN A 382 ? 0.4931 0.5370 0.5396 -0.0206 -0.0485 -0.0580 382 ASN A N 2886 C CA . ASN A 382 ? 0.5207 0.5732 0.5703 -0.0188 -0.0482 -0.0621 382 ASN A CA 2887 C C . ASN A 382 ? 0.5091 0.5606 0.5573 -0.0216 -0.0460 -0.0590 382 ASN A C 2888 O O . ASN A 382 ? 0.4970 0.5517 0.5480 -0.0191 -0.0471 -0.0601 382 ASN A O 2889 C CB . ASN A 382 ? 0.5494 0.6137 0.5997 -0.0204 -0.0462 -0.0688 382 ASN A CB 2890 C CG . ASN A 382 ? 0.6037 0.6788 0.6579 -0.0182 -0.0463 -0.0737 382 ASN A CG 2891 O OD1 . ASN A 382 ? 0.6305 0.7126 0.6838 -0.0226 -0.0431 -0.0751 382 ASN A OD1 2892 N ND2 . ASN A 382 ? 0.6018 0.6778 0.6599 -0.0114 -0.0501 -0.0761 382 ASN A ND2 2893 N N . ARG A 383 ? 0.4784 0.5250 0.5218 -0.0265 -0.0432 -0.0551 383 ARG A N 2894 C CA . ARG A 383 ? 0.5011 0.5447 0.5418 -0.0289 -0.0413 -0.0518 383 ARG A CA 2895 C C . ARG A 383 ? 0.4680 0.5033 0.5098 -0.0254 -0.0435 -0.0464 383 ARG A C 2896 O O . ARG A 383 ? 0.4443 0.4785 0.4856 -0.0254 -0.0429 -0.0448 383 ARG A O 2897 C CB . ARG A 383 ? 0.5642 0.6032 0.5982 -0.0346 -0.0380 -0.0491 383 ARG A CB 2898 C CG . ARG A 383 ? 0.6338 0.6802 0.6648 -0.0398 -0.0352 -0.0536 383 ARG A CG 2899 C CD . ARG A 383 ? 0.7152 0.7547 0.7380 -0.0454 -0.0323 -0.0501 383 ARG A CD 2900 N NE . ARG A 383 ? 0.7880 0.8319 0.8060 -0.0514 -0.0297 -0.0533 383 ARG A NE 2901 C CZ . ARG A 383 ? 0.8347 0.8718 0.8442 -0.0567 -0.0274 -0.0509 383 ARG A CZ 2902 N NH1 . ARG A 383 ? 0.8872 0.9131 0.8919 -0.0563 -0.0274 -0.0452 383 ARG A NH1 2903 N NH2 . ARG A 383 ? 0.8065 0.8480 0.8117 -0.0625 -0.0253 -0.0541 383 ARG A NH2 2904 N N . LEU A 384 ? 0.4426 0.4722 0.4856 -0.0228 -0.0460 -0.0437 384 LEU A N 2905 C CA . LEU A 384 ? 0.4422 0.4642 0.4857 -0.0203 -0.0480 -0.0381 384 LEU A CA 2906 C C . LEU A 384 ? 0.4675 0.4888 0.5150 -0.0154 -0.0521 -0.0388 384 LEU A C 2907 O O . LEU A 384 ? 0.4550 0.4715 0.5030 -0.0138 -0.0534 -0.0347 384 LEU A O 2908 C CB . LEU A 384 ? 0.4346 0.4501 0.4757 -0.0215 -0.0481 -0.0335 384 LEU A CB 2909 C CG . LEU A 384 ? 0.4231 0.4364 0.4589 -0.0258 -0.0446 -0.0314 384 LEU A CG 2910 C CD1 . LEU A 384 ? 0.4393 0.4480 0.4733 -0.0267 -0.0452 -0.0281 384 LEU A CD1 2911 C CD2 . LEU A 384 ? 0.4355 0.4452 0.4688 -0.0261 -0.0429 -0.0277 384 LEU A CD2 2912 N N . ILE A 385 ? 0.4314 0.4569 0.4813 -0.0131 -0.0542 -0.0437 385 ILE A N 2913 C CA . ILE A 385 ? 0.4573 0.4804 0.5096 -0.0082 -0.0587 -0.0446 385 ILE A CA 2914 C C . ILE A 385 ? 0.4566 0.4867 0.5118 -0.0052 -0.0595 -0.0496 385 ILE A C 2915 O O . ILE A 385 ? 0.4656 0.5048 0.5219 -0.0061 -0.0575 -0.0548 385 ILE A O 2916 C CB . ILE A 385 ? 0.4639 0.4847 0.5157 -0.0067 -0.0612 -0.0463 385 ILE A CB 2917 C CG1 . ILE A 385 ? 0.4885 0.5027 0.5377 -0.0098 -0.0607 -0.0410 385 ILE A CG1 2918 C CG2 . ILE A 385 ? 0.4622 0.4790 0.5151 -0.0015 -0.0663 -0.0474 385 ILE A CG2 2919 C CD1 . ILE A 385 ? 0.4961 0.5033 0.5448 -0.0098 -0.0620 -0.0343 385 ILE A CD1 2920 N N . GLY A 386 ? 0.4780 0.5045 0.5343 -0.0020 -0.0623 -0.0480 386 GLY A N 2921 C CA . GLY A 386 ? 0.4890 0.5214 0.5480 0.0012 -0.0637 -0.0522 386 GLY A CA 2922 C C . GLY A 386 ? 0.4918 0.5314 0.5513 -0.0017 -0.0599 -0.0534 386 GLY A C 2923 O O . GLY A 386 ? 0.4874 0.5360 0.5494 -0.0002 -0.0600 -0.0586 386 GLY A O 2924 N N . LYS A 387 ? 0.4863 0.5219 0.5429 -0.0059 -0.0569 -0.0486 387 LYS A N 2925 C CA . LYS A 387 ? 0.4832 0.5240 0.5386 -0.0096 -0.0533 -0.0495 387 LYS A CA 2926 C C . LYS A 387 ? 0.4911 0.5263 0.5448 -0.0100 -0.0528 -0.0449 387 LYS A C 2927 O O . LYS A 387 ? 0.4932 0.5286 0.5436 -0.0139 -0.0495 -0.0437 387 LYS A O 2928 C CB . LYS A 387 ? 0.5267 0.5687 0.5786 -0.0149 -0.0494 -0.0494 387 LYS A CB 2929 C CG . LYS A 387 ? 0.5285 0.5773 0.5819 -0.0149 -0.0494 -0.0544 387 LYS A CG 2930 C CD . LYS A 387 ? 0.5542 0.6154 0.6104 -0.0147 -0.0489 -0.0609 387 LYS A CD 2931 C CE . LYS A 387 ? 0.5604 0.6298 0.6178 -0.0150 -0.0482 -0.0662 387 LYS A CE 2932 N NZ . LYS A 387 ? 0.5834 0.6483 0.6424 -0.0102 -0.0517 -0.0666 387 LYS A NZ 2933 N N . THR A 388 ? 0.4517 0.4813 0.5067 -0.0062 -0.0562 -0.0424 388 THR A N 2934 C CA . THR A 388 ? 0.4570 0.4805 0.5101 -0.0064 -0.0559 -0.0376 388 THR A CA 2935 C C . THR A 388 ? 0.4938 0.5224 0.5473 -0.0067 -0.0551 -0.0401 388 THR A C 2936 O O . THR A 388 ? 0.4830 0.5197 0.5394 -0.0054 -0.0562 -0.0455 388 THR A O 2937 C CB . THR A 388 ? 0.4371 0.4535 0.4911 -0.0029 -0.0599 -0.0342 388 THR A CB 2938 O OG1 . THR A 388 ? 0.4424 0.4615 0.4993 0.0012 -0.0637 -0.0382 388 THR A OG1 2939 C CG2 . THR A 388 ? 0.4192 0.4307 0.4725 -0.0032 -0.0608 -0.0314 388 THR A CG2 2940 N N . ASN A 389 ? 0.4752 0.4992 0.5256 -0.0085 -0.0533 -0.0362 389 ASN A N 2941 C CA A ASN A 389 ? 0.4893 0.5170 0.5391 -0.0093 -0.0525 -0.0379 389 ASN A CA 2942 C CA B ASN A 389 ? 0.4882 0.5155 0.5377 -0.0096 -0.0523 -0.0376 389 ASN A CA 2943 C C . ASN A 389 ? 0.4828 0.5053 0.5329 -0.0065 -0.0549 -0.0350 389 ASN A C 2944 O O . ASN A 389 ? 0.4524 0.4672 0.5013 -0.0053 -0.0557 -0.0302 389 ASN A O 2945 C CB A ASN A 389 ? 0.5083 0.5357 0.5529 -0.0145 -0.0481 -0.0370 389 ASN A CB 2946 C CB B ASN A 389 ? 0.4975 0.5222 0.5413 -0.0144 -0.0479 -0.0353 389 ASN A CB 2947 C CG A ASN A 389 ? 0.5020 0.5197 0.5419 -0.0155 -0.0463 -0.0309 389 ASN A CG 2948 C CG B ASN A 389 ? 0.5034 0.5339 0.5457 -0.0184 -0.0454 -0.0388 389 ASN A CG 2949 O OD1 A ASN A 389 ? 0.4871 0.4993 0.5280 -0.0126 -0.0481 -0.0272 389 ASN A OD1 2950 O OD1 B ASN A 389 ? 0.4884 0.5251 0.5344 -0.0175 -0.0465 -0.0426 389 ASN A OD1 2951 N ND2 A ASN A 389 ? 0.5079 0.5235 0.5418 -0.0195 -0.0428 -0.0300 389 ASN A ND2 2952 N ND2 B ASN A 389 ? 0.4947 0.5230 0.5310 -0.0230 -0.0420 -0.0376 389 ASN A ND2 2953 N N . GLU A 390 ? 0.4518 0.4790 0.5033 -0.0055 -0.0561 -0.0380 390 GLU A N 2954 C CA . GLU A 390 ? 0.4093 0.4324 0.4610 -0.0028 -0.0587 -0.0361 390 GLU A CA 2955 C C . GLU A 390 ? 0.3648 0.3822 0.4119 -0.0052 -0.0562 -0.0318 390 GLU A C 2956 O O . GLU A 390 ? 0.3580 0.3780 0.4022 -0.0087 -0.0532 -0.0328 390 GLU A O 2957 C CB . GLU A 390 ? 0.4314 0.4625 0.4865 -0.0005 -0.0613 -0.0413 390 GLU A CB 2958 C CG . GLU A 390 ? 0.4764 0.5120 0.5358 0.0037 -0.0649 -0.0455 390 GLU A CG 2959 C CD . GLU A 390 ? 0.5023 0.5443 0.5647 0.0073 -0.0682 -0.0500 390 GLU A CD 2960 O OE1 . GLU A 390 ? 0.4900 0.5415 0.5534 0.0051 -0.0663 -0.0535 390 GLU A OE1 2961 O OE2 . GLU A 390 ? 0.5535 0.5908 0.6167 0.0121 -0.0728 -0.0498 390 GLU A OE2 2962 N N . LYS A 391 ? 0.3309 0.3406 0.3768 -0.0033 -0.0576 -0.0272 391 LYS A N 2963 C CA . LYS A 391 ? 0.3259 0.3305 0.3678 -0.0043 -0.0561 -0.0236 391 LYS A CA 2964 C C . LYS A 391 ? 0.3170 0.3190 0.3603 -0.0011 -0.0601 -0.0229 391 LYS A C 2965 O O . LYS A 391 ? 0.3092 0.3099 0.3552 0.0017 -0.0638 -0.0231 391 LYS A O 2966 C CB . LYS A 391 ? 0.3360 0.3338 0.3743 -0.0054 -0.0535 -0.0181 391 LYS A CB 2967 C CG . LYS A 391 ? 0.3435 0.3417 0.3791 -0.0084 -0.0498 -0.0180 391 LYS A CG 2968 C CD . LYS A 391 ? 0.3412 0.3413 0.3726 -0.0118 -0.0469 -0.0202 391 LYS A CD 2969 C CE . LYS A 391 ? 0.3421 0.3412 0.3694 -0.0150 -0.0435 -0.0200 391 LYS A CE 2970 N NZ . LYS A 391 ? 0.3202 0.3213 0.3428 -0.0192 -0.0411 -0.0226 391 LYS A NZ 2971 N N . PHE A 392 ? 0.2875 0.2879 0.3281 -0.0018 -0.0594 -0.0220 392 PHE A N 2972 C CA . PHE A 392 ? 0.3014 0.2997 0.3427 0.0007 -0.0632 -0.0219 392 PHE A CA 2973 C C . PHE A 392 ? 0.2947 0.2853 0.3318 0.0001 -0.0620 -0.0165 392 PHE A C 2974 O O . PHE A 392 ? 0.3024 0.2885 0.3387 0.0004 -0.0615 -0.0126 392 PHE A O 2975 C CB . PHE A 392 ? 0.3126 0.3179 0.3556 0.0009 -0.0643 -0.0268 392 PHE A CB 2976 C CG . PHE A 392 ? 0.3172 0.3314 0.3647 0.0018 -0.0654 -0.0322 392 PHE A CG 2977 C CD1 . PHE A 392 ? 0.3419 0.3563 0.3928 0.0058 -0.0694 -0.0339 392 PHE A CD1 2978 C CD2 . PHE A 392 ? 0.3470 0.3687 0.3945 -0.0014 -0.0623 -0.0354 392 PHE A CD2 2979 C CE1 . PHE A 392 ? 0.3557 0.3784 0.4106 0.0072 -0.0703 -0.0391 392 PHE A CE1 2980 C CE2 . PHE A 392 ? 0.3517 0.3826 0.4033 -0.0007 -0.0630 -0.0405 392 PHE A CE2 2981 C CZ . PHE A 392 ? 0.3600 0.3917 0.4156 0.0039 -0.0670 -0.0425 392 PHE A CZ 2982 N N . HIS A 393 ? 0.2825 0.2720 0.3167 -0.0006 -0.0613 -0.0163 393 HIS A N 2983 C CA . HIS A 393 ? 0.2916 0.2741 0.3213 -0.0010 -0.0598 -0.0114 393 HIS A CA 2984 C C . HIS A 393 ? 0.2934 0.2733 0.3189 -0.0033 -0.0550 -0.0086 393 HIS A C 2985 O O . HIS A 393 ? 0.3040 0.2859 0.3271 -0.0057 -0.0523 -0.0106 393 HIS A O 2986 C CB . HIS A 393 ? 0.3033 0.2849 0.3306 -0.0013 -0.0607 -0.0121 393 HIS A CB 2987 C CG . HIS A 393 ? 0.3116 0.2860 0.3349 -0.0008 -0.0605 -0.0074 393 HIS A CG 2988 N ND1 . HIS A 393 ? 0.3308 0.3016 0.3552 0.0008 -0.0631 -0.0045 393 HIS A ND1 2989 C CD2 . HIS A 393 ? 0.3403 0.3105 0.3580 -0.0023 -0.0579 -0.0052 393 HIS A CD2 2990 C CE1 . HIS A 393 ? 0.3400 0.3054 0.3600 0.0004 -0.0620 -0.0006 393 HIS A CE1 2991 N NE2 . HIS A 393 ? 0.3552 0.3202 0.3713 -0.0011 -0.0588 -0.0011 393 HIS A NE2 2992 N N . GLN A 394 ? 0.2827 0.2580 0.3066 -0.0026 -0.0539 -0.0040 394 GLN A N 2993 C CA . GLN A 394 ? 0.2993 0.2723 0.3195 -0.0037 -0.0497 -0.0012 394 GLN A CA 2994 C C . GLN A 394 ? 0.3043 0.2719 0.3199 -0.0029 -0.0480 0.0032 394 GLN A C 2995 O O . GLN A 394 ? 0.3639 0.3292 0.3761 -0.0033 -0.0478 0.0028 394 GLN A O 2996 C CB . GLN A 394 ? 0.3007 0.2757 0.3245 -0.0032 -0.0500 -0.0004 394 GLN A CB 2997 C CG . GLN A 394 ? 0.3171 0.2974 0.3448 -0.0038 -0.0513 -0.0051 394 GLN A CG 2998 C CD . GLN A 394 ? 0.3469 0.3285 0.3786 -0.0029 -0.0531 -0.0044 394 GLN A CD 2999 O OE1 . GLN A 394 ? 0.3384 0.3186 0.3689 -0.0032 -0.0511 -0.0013 394 GLN A OE1 3000 N NE2 . GLN A 394 ? 0.3583 0.3423 0.3943 -0.0014 -0.0572 -0.0072 394 GLN A NE2 3001 N N . ILE A 395 ? 0.2811 0.2471 0.2960 -0.0020 -0.0465 0.0072 395 ILE A N 3002 C CA . ILE A 395 ? 0.2749 0.2373 0.2860 -0.0009 -0.0449 0.0115 395 ILE A CA 3003 C C . ILE A 395 ? 0.2718 0.2357 0.2871 0.0000 -0.0474 0.0144 395 ILE A C 3004 O O . ILE A 395 ? 0.2686 0.2353 0.2884 -0.0002 -0.0495 0.0135 395 ILE A O 3005 C CB . ILE A 395 ? 0.2720 0.2319 0.2779 -0.0003 -0.0405 0.0138 395 ILE A CB 3006 C CG1 . ILE A 395 ? 0.2672 0.2300 0.2758 0.0000 -0.0397 0.0147 395 ILE A CG1 3007 C CG2 . ILE A 395 ? 0.2721 0.2286 0.2719 -0.0017 -0.0382 0.0111 395 ILE A CG2 3008 C CD1 . ILE A 395 ? 0.2786 0.2389 0.2822 0.0017 -0.0360 0.0180 395 ILE A CD1 3009 N N . GLU A 396 ? 0.2789 0.2407 0.2919 0.0005 -0.0471 0.0180 396 GLU A N 3010 C CA . GLU A 396 ? 0.2829 0.2461 0.2985 0.0006 -0.0490 0.0215 396 GLU A CA 3011 C C . GLU A 396 ? 0.2824 0.2486 0.2985 0.0012 -0.0462 0.0244 396 GLU A C 3012 O O . GLU A 396 ? 0.2759 0.2416 0.2886 0.0023 -0.0424 0.0249 396 GLU A O 3013 C CB . GLU A 396 ? 0.3026 0.2635 0.3152 0.0006 -0.0493 0.0244 396 GLU A CB 3014 C CG . GLU A 396 ? 0.3209 0.2785 0.3328 0.0002 -0.0525 0.0219 396 GLU A CG 3015 C CD . GLU A 396 ? 0.3332 0.2910 0.3492 -0.0001 -0.0576 0.0197 396 GLU A CD 3016 O OE1 . GLU A 396 ? 0.3544 0.3135 0.3729 -0.0007 -0.0593 0.0217 396 GLU A OE1 3017 O OE2 . GLU A 396 ? 0.3601 0.3167 0.3765 0.0001 -0.0603 0.0161 396 GLU A OE2 3018 N N . LYS A 397 ? 0.2763 0.2453 0.2962 0.0004 -0.0485 0.0262 397 LYS A N 3019 C CA . LYS A 397 ? 0.2704 0.2432 0.2919 0.0007 -0.0467 0.0286 397 LYS A CA 3020 C C . LYS A 397 ? 0.2810 0.2570 0.3038 -0.0001 -0.0476 0.0334 397 LYS A C 3021 O O . LYS A 397 ? 0.2912 0.2715 0.3154 0.0000 -0.0462 0.0359 397 LYS A O 3022 C CB . LYS A 397 ? 0.2616 0.2357 0.2867 0.0000 -0.0485 0.0256 397 LYS A CB 3023 C CG . LYS A 397 ? 0.2605 0.2328 0.2840 0.0002 -0.0470 0.0211 397 LYS A CG 3024 C CD . LYS A 397 ? 0.2579 0.2319 0.2847 -0.0006 -0.0485 0.0178 397 LYS A CD 3025 C CE . LYS A 397 ? 0.2536 0.2270 0.2789 -0.0011 -0.0473 0.0132 397 LYS A CE 3026 N NZ . LYS A 397 ? 0.2490 0.2250 0.2772 -0.0019 -0.0481 0.0101 397 LYS A NZ 3027 N N . GLU A 398 ? 0.2925 0.2667 0.3144 -0.0012 -0.0500 0.0346 398 GLU A N 3028 C CA . GLU A 398 ? 0.3161 0.2932 0.3380 -0.0028 -0.0508 0.0392 398 GLU A CA 3029 C C . GLU A 398 ? 0.3214 0.2960 0.3394 -0.0026 -0.0500 0.0405 398 GLU A C 3030 O O . GLU A 398 ? 0.3090 0.2784 0.3252 -0.0024 -0.0514 0.0376 398 GLU A O 3031 C CB . GLU A 398 ? 0.3639 0.3394 0.3879 -0.0057 -0.0559 0.0393 398 GLU A CB 3032 C CG . GLU A 398 ? 0.3818 0.3604 0.4093 -0.0064 -0.0568 0.0391 398 GLU A CG 3033 C CD . GLU A 398 ? 0.4354 0.4113 0.4637 -0.0093 -0.0621 0.0393 398 GLU A CD 3034 O OE1 . GLU A 398 ? 0.4743 0.4460 0.5001 -0.0109 -0.0652 0.0402 398 GLU A OE1 3035 O OE2 . GLU A 398 ? 0.4719 0.4487 0.5025 -0.0099 -0.0635 0.0385 398 GLU A OE2 3036 N N . PHE A 399 ? 0.3133 0.2921 0.3300 -0.0028 -0.0478 0.0447 399 PHE A N 3037 C CA . PHE A 399 ? 0.3225 0.2994 0.3348 -0.0023 -0.0463 0.0459 399 PHE A CA 3038 C C . PHE A 399 ? 0.3515 0.3322 0.3634 -0.0051 -0.0474 0.0504 399 PHE A C 3039 O O . PHE A 399 ? 0.3690 0.3571 0.3830 -0.0056 -0.0460 0.0535 399 PHE A O 3040 C CB . PHE A 399 ? 0.3170 0.2954 0.3265 0.0013 -0.0410 0.0461 399 PHE A CB 3041 C CG . PHE A 399 ? 0.3074 0.2819 0.3162 0.0032 -0.0399 0.0421 399 PHE A CG 3042 C CD1 . PHE A 399 ? 0.3045 0.2816 0.3161 0.0039 -0.0392 0.0413 399 PHE A CD1 3043 C CD2 . PHE A 399 ? 0.3161 0.2842 0.3215 0.0036 -0.0400 0.0390 399 PHE A CD2 3044 C CE1 . PHE A 399 ? 0.3085 0.2820 0.3191 0.0050 -0.0383 0.0376 399 PHE A CE1 3045 C CE2 . PHE A 399 ? 0.3201 0.2852 0.3247 0.0044 -0.0392 0.0353 399 PHE A CE2 3046 C CZ . PHE A 399 ? 0.3012 0.2689 0.3083 0.0050 -0.0383 0.0346 399 PHE A CZ 3047 N N . SER A 400 ? 0.3735 0.3496 0.3824 -0.0070 -0.0497 0.0507 400 SER A N 3048 C CA . SER A 400 ? 0.4084 0.3871 0.4156 -0.0105 -0.0509 0.0550 400 SER A CA 3049 C C . SER A 400 ? 0.4366 0.4200 0.4406 -0.0091 -0.0464 0.0578 400 SER A C 3050 O O . SER A 400 ? 0.4367 0.4254 0.4399 -0.0120 -0.0463 0.0617 400 SER A O 3051 C CB . SER A 400 ? 0.4199 0.3905 0.4245 -0.0133 -0.0562 0.0540 400 SER A CB 3052 O OG . SER A 400 ? 0.4503 0.4150 0.4515 -0.0113 -0.0556 0.0516 400 SER A OG 3053 N N . GLU A 401 ? 0.4231 0.4045 0.4249 -0.0050 -0.0427 0.0558 401 GLU A N 3054 C CA . GLU A 401 ? 0.4496 0.4346 0.4476 -0.0027 -0.0382 0.0579 401 GLU A CA 3055 C C . GLU A 401 ? 0.4253 0.4135 0.4233 0.0022 -0.0336 0.0571 401 GLU A C 3056 O O . GLU A 401 ? 0.3892 0.3735 0.3882 0.0039 -0.0336 0.0540 401 GLU A O 3057 C CB . GLU A 401 ? 0.4904 0.4676 0.4830 -0.0023 -0.0382 0.0564 401 GLU A CB 3058 C CG . GLU A 401 ? 0.5647 0.5385 0.5553 -0.0067 -0.0420 0.0579 401 GLU A CG 3059 C CD . GLU A 401 ? 0.6037 0.5711 0.5963 -0.0090 -0.0476 0.0553 401 GLU A CD 3060 O OE1 . GLU A 401 ? 0.6574 0.6203 0.6510 -0.0067 -0.0480 0.0514 401 GLU A OE1 3061 O OE2 . GLU A 401 ? 0.6517 0.6186 0.6446 -0.0131 -0.0516 0.0572 401 GLU A OE2 3062 N N . VAL A 402 ? 0.4068 0.4015 0.4028 0.0045 -0.0296 0.0599 402 VAL A N 3063 C CA . VAL A 402 ? 0.4022 0.3990 0.3962 0.0101 -0.0251 0.0594 402 VAL A CA 3064 C C . VAL A 402 ? 0.3889 0.3761 0.3761 0.0129 -0.0232 0.0567 402 VAL A C 3065 O O . VAL A 402 ? 0.3796 0.3637 0.3629 0.0118 -0.0232 0.0572 402 VAL A O 3066 C CB . VAL A 402 ? 0.4258 0.4343 0.4202 0.0119 -0.0218 0.0633 402 VAL A CB 3067 C CG1 . VAL A 402 ? 0.4139 0.4227 0.4037 0.0187 -0.0170 0.0627 402 VAL A CG1 3068 C CG2 . VAL A 402 ? 0.4258 0.4443 0.4268 0.0096 -0.0233 0.0657 402 VAL A CG2 3069 N N . GLU A 403 ? 0.3744 0.3564 0.3594 0.0161 -0.0217 0.0539 403 GLU A N 3070 C CA . GLU A 403 ? 0.3876 0.3595 0.3652 0.0180 -0.0202 0.0513 403 GLU A CA 3071 C C . GLU A 403 ? 0.3828 0.3519 0.3546 0.0234 -0.0163 0.0504 403 GLU A C 3072 O O . GLU A 403 ? 0.4195 0.3809 0.3836 0.0253 -0.0145 0.0491 403 GLU A O 3073 C CB . GLU A 403 ? 0.3938 0.3581 0.3724 0.0149 -0.0236 0.0476 403 GLU A CB 3074 C CG . GLU A 403 ? 0.3970 0.3617 0.3801 0.0102 -0.0282 0.0476 403 GLU A CG 3075 C CD . GLU A 403 ? 0.4043 0.3634 0.3893 0.0082 -0.0314 0.0436 403 GLU A CD 3076 O OE1 . GLU A 403 ? 0.3752 0.3361 0.3644 0.0080 -0.0324 0.0422 403 GLU A OE1 3077 O OE2 . GLU A 403 ? 0.4300 0.3834 0.4122 0.0069 -0.0330 0.0418 403 GLU A OE2 3078 N N . GLY A 404 ? 0.3577 0.3317 0.3323 0.0258 -0.0153 0.0510 404 GLY A N 3079 C CA . GLY A 404 ? 0.3567 0.3271 0.3250 0.0312 -0.0120 0.0502 404 GLY A CA 3080 C C . GLY A 404 ? 0.3545 0.3152 0.3197 0.0304 -0.0128 0.0466 404 GLY A C 3081 O O . GLY A 404 ? 0.3313 0.2933 0.3023 0.0272 -0.0154 0.0453 404 GLY A O 3082 N N . ARG A 405 ? 0.3443 0.2952 0.2998 0.0331 -0.0107 0.0449 405 ARG A N 3083 C CA . ARG A 405 ? 0.3468 0.2888 0.2970 0.0333 -0.0106 0.0420 405 ARG A CA 3084 C C . ARG A 405 ? 0.3303 0.2704 0.2852 0.0277 -0.0138 0.0392 405 ARG A C 3085 O O . ARG A 405 ? 0.3227 0.2629 0.2793 0.0273 -0.0143 0.0380 405 ARG A O 3086 C CB . ARG A 405 ? 0.3634 0.2942 0.3016 0.0354 -0.0085 0.0407 405 ARG A CB 3087 C CG . ARG A 405 ? 0.3741 0.2945 0.3041 0.0361 -0.0078 0.0383 405 ARG A CG 3088 C CD . ARG A 405 ? 0.3864 0.2950 0.3029 0.0388 -0.0056 0.0375 405 ARG A CD 3089 N NE . ARG A 405 ? 0.3911 0.2886 0.2981 0.0389 -0.0052 0.0353 405 ARG A NE 3090 C CZ . ARG A 405 ? 0.4110 0.2959 0.3043 0.0412 -0.0035 0.0345 405 ARG A CZ 3091 N NH1 . ARG A 405 ? 0.4268 0.3089 0.3146 0.0438 -0.0019 0.0354 405 ARG A NH1 3092 N NH2 . ARG A 405 ? 0.4189 0.2934 0.3032 0.0408 -0.0034 0.0327 405 ARG A NH2 3093 N N A ILE A 406 ? 0.3309 0.2695 0.2876 0.0238 -0.0159 0.0380 406 ILE A N 3094 N N B ILE A 406 ? 0.3315 0.2700 0.2881 0.0238 -0.0159 0.0380 406 ILE A N 3095 C CA A ILE A 406 ? 0.3318 0.2689 0.2924 0.0193 -0.0189 0.0348 406 ILE A CA 3096 C CA B ILE A 406 ? 0.3327 0.2700 0.2935 0.0192 -0.0189 0.0349 406 ILE A CA 3097 C C A ILE A 406 ? 0.3150 0.2607 0.2858 0.0176 -0.0213 0.0355 406 ILE A C 3098 C C B ILE A 406 ? 0.3156 0.2614 0.2864 0.0177 -0.0212 0.0355 406 ILE A C 3099 O O A ILE A 406 ? 0.2981 0.2437 0.2716 0.0158 -0.0225 0.0332 406 ILE A O 3100 O O B ILE A 406 ? 0.2986 0.2442 0.2718 0.0159 -0.0224 0.0333 406 ILE A O 3101 C CB A ILE A 406 ? 0.3450 0.2790 0.3052 0.0160 -0.0209 0.0333 406 ILE A CB 3102 C CB B ILE A 406 ? 0.3472 0.2822 0.3084 0.0159 -0.0212 0.0336 406 ILE A CB 3103 C CG1 A ILE A 406 ? 0.3409 0.2755 0.3062 0.0119 -0.0242 0.0299 406 ILE A CG1 3104 C CG1 B ILE A 406 ? 0.3480 0.2805 0.3109 0.0121 -0.0236 0.0297 406 ILE A CG1 3105 C CG2 A ILE A 406 ? 0.3525 0.2919 0.3171 0.0156 -0.0222 0.0360 406 ILE A CG2 3106 C CG2 B ILE A 406 ? 0.3455 0.2878 0.3142 0.0147 -0.0235 0.0358 406 ILE A CG2 3107 C CD1 A ILE A 406 ? 0.3484 0.2783 0.3095 0.0110 -0.0233 0.0271 406 ILE A CD1 3108 C CD1 B ILE A 406 ? 0.3625 0.2871 0.3167 0.0120 -0.0217 0.0274 406 ILE A CD1 3109 N N . GLN A 407 ? 0.3066 0.2598 0.2826 0.0181 -0.0218 0.0386 407 GLN A N 3110 C CA . GLN A 407 ? 0.3075 0.2682 0.2921 0.0163 -0.0241 0.0396 407 GLN A CA 3111 C C . GLN A 407 ? 0.2967 0.2601 0.2819 0.0187 -0.0225 0.0402 407 GLN A C 3112 O O . GLN A 407 ? 0.2913 0.2574 0.2819 0.0167 -0.0245 0.0391 407 GLN A O 3113 C CB . GLN A 407 ? 0.3004 0.2678 0.2890 0.0155 -0.0251 0.0430 407 GLN A CB 3114 C CG . GLN A 407 ? 0.3015 0.2751 0.2981 0.0126 -0.0283 0.0438 407 GLN A CG 3115 C CD . GLN A 407 ? 0.3049 0.2847 0.3044 0.0109 -0.0295 0.0475 407 GLN A CD 3116 O OE1 . GLN A 407 ? 0.3221 0.3095 0.3255 0.0108 -0.0295 0.0501 407 GLN A OE1 3117 N NE2 . GLN A 407 ? 0.3011 0.2779 0.2981 0.0095 -0.0305 0.0478 407 GLN A NE2 3118 N N . ASP A 408 ? 0.3015 0.2644 0.2812 0.0232 -0.0191 0.0418 408 ASP A N 3119 C CA . ASP A 408 ? 0.2875 0.2519 0.2665 0.0262 -0.0176 0.0423 408 ASP A CA 3120 C C . ASP A 408 ? 0.2900 0.2472 0.2665 0.0242 -0.0184 0.0387 408 ASP A C 3121 O O . ASP A 408 ? 0.2659 0.2258 0.2458 0.0238 -0.0192 0.0384 408 ASP A O 3122 C CB . ASP A 408 ? 0.3109 0.2728 0.2819 0.0319 -0.0141 0.0437 408 ASP A CB 3123 C CG . ASP A 408 ? 0.3294 0.2999 0.3023 0.0346 -0.0126 0.0473 408 ASP A CG 3124 O OD1 . ASP A 408 ? 0.3323 0.3123 0.3135 0.0320 -0.0144 0.0493 408 ASP A OD1 3125 O OD2 . ASP A 408 ? 0.3396 0.3068 0.3049 0.0392 -0.0097 0.0479 408 ASP A OD2 3126 N N . LEU A 409 ? 0.2837 0.2323 0.2540 0.0228 -0.0182 0.0360 409 LEU A N 3127 C CA . LEU A 409 ? 0.2845 0.2268 0.2517 0.0203 -0.0187 0.0325 409 LEU A CA 3128 C C . LEU A 409 ? 0.2744 0.2216 0.2504 0.0158 -0.0220 0.0306 409 LEU A C 3129 O O . LEU A 409 ? 0.2700 0.2175 0.2475 0.0146 -0.0225 0.0291 409 LEU A O 3130 C CB . LEU A 409 ? 0.2892 0.2220 0.2476 0.0192 -0.0178 0.0304 409 LEU A CB 3131 C CG . LEU A 409 ? 0.2973 0.2230 0.2501 0.0162 -0.0179 0.0269 409 LEU A CG 3132 C CD1 . LEU A 409 ? 0.2977 0.2200 0.2456 0.0185 -0.0164 0.0273 409 LEU A CD1 3133 C CD2 . LEU A 409 ? 0.3150 0.2317 0.2583 0.0155 -0.0169 0.0257 409 LEU A CD2 3134 N N . GLU A 410 ? 0.2761 0.2264 0.2573 0.0137 -0.0242 0.0305 410 GLU A N 3135 C CA . GLU A 410 ? 0.2827 0.2374 0.2719 0.0103 -0.0277 0.0287 410 GLU A CA 3136 C C . GLU A 410 ? 0.2718 0.2328 0.2670 0.0106 -0.0285 0.0302 410 GLU A C 3137 O O . GLU A 410 ? 0.2543 0.2162 0.2526 0.0086 -0.0299 0.0279 410 GLU A O 3138 C CB . GLU A 410 ? 0.2932 0.2496 0.2860 0.0087 -0.0302 0.0290 410 GLU A CB 3139 C CG . GLU A 410 ? 0.3139 0.2646 0.3018 0.0076 -0.0302 0.0267 410 GLU A CG 3140 C CD . GLU A 410 ? 0.3392 0.2902 0.3283 0.0070 -0.0321 0.0279 410 GLU A CD 3141 O OE1 . GLU A 410 ? 0.3372 0.2918 0.3285 0.0080 -0.0322 0.0314 410 GLU A OE1 3142 O OE2 . GLU A 410 ? 0.3486 0.2964 0.3363 0.0053 -0.0336 0.0253 410 GLU A OE2 3143 N N . LYS A 411 ? 0.2632 0.2288 0.2597 0.0129 -0.0275 0.0341 411 LYS A N 3144 C CA . LYS A 411 ? 0.2697 0.2416 0.2714 0.0131 -0.0282 0.0359 411 LYS A CA 3145 C C . LYS A 411 ? 0.2529 0.2228 0.2518 0.0145 -0.0265 0.0350 411 LYS A C 3146 O O . LYS A 411 ? 0.2403 0.2133 0.2437 0.0130 -0.0281 0.0344 411 LYS A O 3147 C CB . LYS A 411 ? 0.2869 0.2655 0.2906 0.0151 -0.0273 0.0404 411 LYS A CB 3148 C CG . LYS A 411 ? 0.2979 0.2794 0.3053 0.0125 -0.0298 0.0417 411 LYS A CG 3149 C CD . LYS A 411 ? 0.3254 0.3143 0.3338 0.0139 -0.0285 0.0462 411 LYS A CD 3150 C CE . LYS A 411 ? 0.3509 0.3434 0.3636 0.0102 -0.0316 0.0480 411 LYS A CE 3151 N NZ . LYS A 411 ? 0.3777 0.3787 0.3914 0.0106 -0.0304 0.0525 411 LYS A NZ 3152 N N . TYR A 412 ? 0.2515 0.2158 0.2425 0.0175 -0.0236 0.0349 412 TYR A N 3153 C CA . TYR A 412 ? 0.2514 0.2124 0.2379 0.0192 -0.0221 0.0343 412 TYR A CA 3154 C C . TYR A 412 ? 0.2487 0.2054 0.2346 0.0152 -0.0233 0.0303 412 TYR A C 3155 O O . TYR A 412 ? 0.2497 0.2067 0.2361 0.0146 -0.0236 0.0296 412 TYR A O 3156 C CB . TYR A 412 ? 0.2595 0.2132 0.2357 0.0232 -0.0191 0.0348 412 TYR A CB 3157 C CG . TYR A 412 ? 0.2666 0.2157 0.2364 0.0259 -0.0176 0.0348 412 TYR A CG 3158 C CD1 . TYR A 412 ? 0.2617 0.2167 0.2339 0.0295 -0.0171 0.0376 412 TYR A CD1 3159 C CD2 . TYR A 412 ? 0.2754 0.2137 0.2359 0.0247 -0.0168 0.0320 412 TYR A CD2 3160 C CE1 . TYR A 412 ? 0.2690 0.2189 0.2344 0.0327 -0.0160 0.0376 412 TYR A CE1 3161 C CE2 . TYR A 412 ? 0.2796 0.2123 0.2329 0.0271 -0.0157 0.0321 412 TYR A CE2 3162 C CZ . TYR A 412 ? 0.2764 0.2144 0.2320 0.0314 -0.0154 0.0348 412 TYR A CZ 3163 O OH . TYR A 412 ? 0.2750 0.2066 0.2227 0.0342 -0.0146 0.0349 412 TYR A OH 3164 N N . VAL A 413 ? 0.2470 0.2002 0.2317 0.0125 -0.0241 0.0276 413 VAL A N 3165 C CA . VAL A 413 ? 0.2485 0.1993 0.2330 0.0085 -0.0252 0.0235 413 VAL A CA 3166 C C . VAL A 413 ? 0.2436 0.2013 0.2371 0.0065 -0.0278 0.0228 413 VAL A C 3167 O O . VAL A 413 ? 0.2425 0.1999 0.2359 0.0048 -0.0279 0.0209 413 VAL A O 3168 C CB . VAL A 413 ? 0.2547 0.2027 0.2376 0.0062 -0.0259 0.0210 413 VAL A CB 3169 C CG1 . VAL A 413 ? 0.2604 0.2102 0.2467 0.0020 -0.0278 0.0169 413 VAL A CG1 3170 C CG2 . VAL A 413 ? 0.2599 0.1989 0.2317 0.0072 -0.0233 0.0209 413 VAL A CG2 3171 N N . GLU A 414 ? 0.2386 0.2019 0.2390 0.0066 -0.0298 0.0245 414 GLU A N 3172 C CA . GLU A 414 ? 0.2475 0.2161 0.2556 0.0046 -0.0327 0.0236 414 GLU A CA 3173 C C . GLU A 414 ? 0.2447 0.2165 0.2545 0.0056 -0.0323 0.0259 414 GLU A C 3174 O O . GLU A 414 ? 0.2396 0.2129 0.2522 0.0038 -0.0336 0.0240 414 GLU A O 3175 C CB . GLU A 414 ? 0.2513 0.2231 0.2645 0.0040 -0.0354 0.0248 414 GLU A CB 3176 C CG . GLU A 414 ? 0.2557 0.2312 0.2755 0.0020 -0.0390 0.0236 414 GLU A CG 3177 C CD . GLU A 414 ? 0.2666 0.2412 0.2876 0.0000 -0.0405 0.0186 414 GLU A CD 3178 O OE1 . GLU A 414 ? 0.2759 0.2474 0.2928 -0.0003 -0.0389 0.0160 414 GLU A OE1 3179 O OE2 . GLU A 414 ? 0.2724 0.2495 0.2981 -0.0010 -0.0433 0.0170 414 GLU A OE2 3180 N N . ASP A 415 ? 0.2542 0.2278 0.2626 0.0087 -0.0307 0.0298 415 ASP A N 3181 C CA . ASP A 415 ? 0.2659 0.2427 0.2750 0.0102 -0.0300 0.0321 415 ASP A CA 3182 C C . ASP A 415 ? 0.2609 0.2329 0.2654 0.0099 -0.0288 0.0298 415 ASP A C 3183 O O . ASP A 415 ? 0.2463 0.2207 0.2535 0.0088 -0.0298 0.0296 415 ASP A O 3184 C CB . ASP A 415 ? 0.2940 0.2735 0.3011 0.0143 -0.0280 0.0362 415 ASP A CB 3185 C CG . ASP A 415 ? 0.3262 0.3125 0.3370 0.0155 -0.0283 0.0391 415 ASP A CG 3186 O OD1 . ASP A 415 ? 0.3678 0.3592 0.3850 0.0127 -0.0309 0.0396 415 ASP A OD1 3187 O OD2 . ASP A 415 ? 0.3751 0.3611 0.3819 0.0192 -0.0263 0.0406 415 ASP A OD2 3188 N N . THR A 416 ? 0.2535 0.2181 0.2500 0.0107 -0.0267 0.0282 416 THR A N 3189 C CA . THR A 416 ? 0.2487 0.2072 0.2387 0.0099 -0.0255 0.0261 416 THR A CA 3190 C C . THR A 416 ? 0.2297 0.1895 0.2234 0.0053 -0.0273 0.0224 416 THR A C 3191 O O . THR A 416 ? 0.2207 0.1802 0.2137 0.0044 -0.0274 0.0218 416 THR A O 3192 C CB . THR A 416 ? 0.2598 0.2094 0.2399 0.0106 -0.0234 0.0249 416 THR A CB 3193 O OG1 . THR A 416 ? 0.2674 0.2157 0.2432 0.0157 -0.0216 0.0283 416 THR A OG1 3194 C CG2 . THR A 416 ? 0.2595 0.2013 0.2312 0.0085 -0.0224 0.0223 416 THR A CG2 3195 N N . LYS A 417 ? 0.2191 0.1805 0.2164 0.0029 -0.0287 0.0200 417 LYS A N 3196 C CA . LYS A 417 ? 0.2179 0.1817 0.2191 -0.0008 -0.0305 0.0160 417 LYS A CA 3197 C C . LYS A 417 ? 0.2094 0.1787 0.2174 -0.0011 -0.0325 0.0168 417 LYS A C 3198 O O . LYS A 417 ? 0.2034 0.1731 0.2115 -0.0032 -0.0327 0.0147 417 LYS A O 3199 C CB . LYS A 417 ? 0.2138 0.1794 0.2185 -0.0022 -0.0322 0.0138 417 LYS A CB 3200 C CG . LYS A 417 ? 0.2154 0.1847 0.2246 -0.0052 -0.0341 0.0094 417 LYS A CG 3201 C CD . LYS A 417 ? 0.2180 0.1889 0.2300 -0.0059 -0.0359 0.0070 417 LYS A CD 3202 C CE . LYS A 417 ? 0.2213 0.1974 0.2394 -0.0075 -0.0386 0.0031 417 LYS A CE 3203 N NZ . LYS A 417 ? 0.2359 0.2141 0.2570 -0.0074 -0.0409 0.0006 417 LYS A NZ 3204 N N . ILE A 418 ? 0.2058 0.1792 0.2187 0.0005 -0.0338 0.0201 418 ILE A N 3205 C CA . ILE A 418 ? 0.2044 0.1828 0.2235 -0.0002 -0.0361 0.0210 418 ILE A CA 3206 C C . ILE A 418 ? 0.2025 0.1808 0.2195 0.0003 -0.0350 0.0225 418 ILE A C 3207 O O . ILE A 418 ? 0.1947 0.1748 0.2143 -0.0014 -0.0363 0.0212 418 ILE A O 3208 C CB . ILE A 418 ? 0.2037 0.1861 0.2273 0.0007 -0.0379 0.0245 418 ILE A CB 3209 C CG1 . ILE A 418 ? 0.2046 0.1863 0.2303 -0.0003 -0.0399 0.0222 418 ILE A CG1 3210 C CG2 . ILE A 418 ? 0.2043 0.1913 0.2328 -0.0001 -0.0401 0.0264 418 ILE A CG2 3211 C CD1 . ILE A 418 ? 0.2207 0.2047 0.2491 0.0001 -0.0416 0.0255 418 ILE A CD1 3212 N N . ASP A 419 ? 0.2018 0.1778 0.2136 0.0033 -0.0326 0.0251 419 ASP A N 3213 C CA . ASP A 419 ? 0.2088 0.1846 0.2184 0.0044 -0.0318 0.0268 419 ASP A CA 3214 C C . ASP A 419 ? 0.2042 0.1749 0.2091 0.0019 -0.0311 0.0231 419 ASP A C 3215 O O . ASP A 419 ? 0.2072 0.1787 0.2124 0.0010 -0.0317 0.0232 419 ASP A O 3216 C CB . ASP A 419 ? 0.2219 0.1960 0.2262 0.0089 -0.0295 0.0300 419 ASP A CB 3217 C CG . ASP A 419 ? 0.2409 0.2226 0.2504 0.0114 -0.0301 0.0343 419 ASP A CG 3218 O OD1 . ASP A 419 ? 0.2555 0.2433 0.2723 0.0092 -0.0325 0.0351 419 ASP A OD1 3219 O OD2 . ASP A 419 ? 0.2644 0.2456 0.2698 0.0156 -0.0281 0.0368 419 ASP A OD2 3220 N N . LEU A 420 ? 0.2077 0.1732 0.2076 0.0004 -0.0299 0.0202 420 LEU A N 3221 C CA . LEU A 420 ? 0.2093 0.1704 0.2041 -0.0027 -0.0292 0.0168 420 LEU A CA 3222 C C . LEU A 420 ? 0.2052 0.1714 0.2065 -0.0063 -0.0312 0.0136 420 LEU A C 3223 O O . LEU A 420 ? 0.2034 0.1688 0.2030 -0.0083 -0.0312 0.0123 420 LEU A O 3224 C CB . LEU A 420 ? 0.2141 0.1690 0.2016 -0.0040 -0.0275 0.0146 420 LEU A CB 3225 C CG . LEU A 420 ? 0.2199 0.1669 0.1976 -0.0008 -0.0254 0.0170 420 LEU A CG 3226 C CD1 . LEU A 420 ? 0.2278 0.1694 0.1996 -0.0013 -0.0241 0.0158 420 LEU A CD1 3227 C CD2 . LEU A 420 ? 0.2308 0.1719 0.2009 -0.0017 -0.0246 0.0168 420 LEU A CD2 3228 N N . TRP A 421 ? 0.2080 0.1787 0.2158 -0.0069 -0.0330 0.0123 421 TRP A N 3229 C CA . TRP A 421 ? 0.2051 0.1806 0.2191 -0.0092 -0.0353 0.0094 421 TRP A CA 3230 C C . TRP A 421 ? 0.2027 0.1812 0.2206 -0.0087 -0.0369 0.0116 421 TRP A C 3231 O O . TRP A 421 ? 0.1963 0.1763 0.2157 -0.0109 -0.0377 0.0093 421 TRP A O 3232 C CB . TRP A 421 ? 0.2050 0.1836 0.2241 -0.0092 -0.0372 0.0076 421 TRP A CB 3233 C CG . TRP A 421 ? 0.2052 0.1827 0.2214 -0.0112 -0.0362 0.0036 421 TRP A CG 3234 C CD1 . TRP A 421 ? 0.2117 0.1870 0.2252 -0.0107 -0.0353 0.0034 421 TRP A CD1 3235 C CD2 . TRP A 421 ? 0.2086 0.1875 0.2234 -0.0146 -0.0356 -0.0009 421 TRP A CD2 3236 N NE1 . TRP A 421 ? 0.2123 0.1878 0.2232 -0.0136 -0.0345 -0.0007 421 TRP A NE1 3237 C CE2 . TRP A 421 ? 0.2159 0.1939 0.2275 -0.0161 -0.0346 -0.0035 421 TRP A CE2 3238 C CE3 . TRP A 421 ? 0.2098 0.1909 0.2255 -0.0166 -0.0359 -0.0030 421 TRP A CE3 3239 C CZ2 . TRP A 421 ? 0.2180 0.1982 0.2276 -0.0198 -0.0338 -0.0080 421 TRP A CZ2 3240 C CZ3 . TRP A 421 ? 0.2217 0.2046 0.2353 -0.0202 -0.0350 -0.0076 421 TRP A CZ3 3241 C CH2 . TRP A 421 ? 0.2227 0.2055 0.2333 -0.0218 -0.0339 -0.0099 421 TRP A CH2 3242 N N . SER A 422 ? 0.1986 0.1785 0.2182 -0.0061 -0.0372 0.0162 422 SER A N 3243 C CA . SER A 422 ? 0.2008 0.1839 0.2238 -0.0060 -0.0388 0.0187 422 SER A CA 3244 C C . SER A 422 ? 0.1999 0.1807 0.2185 -0.0066 -0.0375 0.0187 422 SER A C 3245 O O . SER A 422 ? 0.1937 0.1762 0.2144 -0.0083 -0.0389 0.0181 422 SER A O 3246 C CB . SER A 422 ? 0.2009 0.1874 0.2264 -0.0035 -0.0392 0.0236 422 SER A CB 3247 O OG . SER A 422 ? 0.2054 0.1934 0.2343 -0.0035 -0.0407 0.0237 422 SER A OG 3248 N N . TYR A 423 ? 0.2066 0.1823 0.2180 -0.0051 -0.0349 0.0193 423 TYR A N 3249 C CA . TYR A 423 ? 0.2106 0.1821 0.2158 -0.0057 -0.0337 0.0191 423 TYR A CA 3250 C C . TYR A 423 ? 0.2071 0.1775 0.2113 -0.0102 -0.0339 0.0143 423 TYR A C 3251 O O . TYR A 423 ? 0.2053 0.1760 0.2094 -0.0119 -0.0345 0.0137 423 TYR A O 3252 C CB . TYR A 423 ? 0.2170 0.1816 0.2133 -0.0033 -0.0312 0.0202 423 TYR A CB 3253 C CG . TYR A 423 ? 0.2295 0.1879 0.2178 -0.0043 -0.0303 0.0197 423 TYR A CG 3254 C CD1 . TYR A 423 ? 0.2334 0.1922 0.2207 -0.0016 -0.0307 0.0229 423 TYR A CD1 3255 C CD2 . TYR A 423 ? 0.2332 0.1860 0.2151 -0.0082 -0.0292 0.0159 423 TYR A CD2 3256 C CE1 . TYR A 423 ? 0.2497 0.2024 0.2295 -0.0025 -0.0303 0.0225 423 TYR A CE1 3257 C CE2 . TYR A 423 ? 0.2464 0.1931 0.2205 -0.0098 -0.0287 0.0155 423 TYR A CE2 3258 C CZ . TYR A 423 ? 0.2563 0.2024 0.2291 -0.0067 -0.0293 0.0188 423 TYR A CZ 3259 O OH . TYR A 423 ? 0.2807 0.2201 0.2453 -0.0079 -0.0291 0.0187 423 TYR A OH 3260 N N . ASN A 424 ? 0.2063 0.1762 0.2103 -0.0121 -0.0334 0.0108 424 ASN A N 3261 C CA . ASN A 424 ? 0.2069 0.1775 0.2103 -0.0163 -0.0333 0.0060 424 ASN A CA 3262 C C . ASN A 424 ? 0.2034 0.1796 0.2138 -0.0173 -0.0357 0.0048 424 ASN A C 3263 O O . ASN A 424 ? 0.2054 0.1816 0.2143 -0.0200 -0.0356 0.0026 424 ASN A O 3264 C CB . ASN A 424 ? 0.2110 0.1826 0.2146 -0.0179 -0.0328 0.0024 424 ASN A CB 3265 C CG . ASN A 424 ? 0.2165 0.1814 0.2111 -0.0184 -0.0304 0.0026 424 ASN A CG 3266 O OD1 . ASN A 424 ? 0.2317 0.1902 0.2186 -0.0182 -0.0290 0.0044 424 ASN A OD1 3267 N ND2 . ASN A 424 ? 0.2150 0.1807 0.2099 -0.0191 -0.0301 0.0006 424 ASN A ND2 3268 N N . ALA A 425 ? 0.1989 0.1790 0.2161 -0.0154 -0.0378 0.0063 425 ALA A N 3269 C CA . ALA A 425 ? 0.2074 0.1915 0.2305 -0.0162 -0.0405 0.0052 425 ALA A CA 3270 C C . ALA A 425 ? 0.2182 0.2019 0.2404 -0.0165 -0.0409 0.0077 425 ALA A C 3271 O O . ALA A 425 ? 0.2272 0.2120 0.2502 -0.0187 -0.0419 0.0055 425 ALA A O 3272 C CB . ALA A 425 ? 0.1991 0.1858 0.2279 -0.0142 -0.0430 0.0070 425 ALA A CB 3273 N N . GLU A 426 ? 0.2300 0.2125 0.2505 -0.0142 -0.0403 0.0125 426 GLU A N 3274 C CA . GLU A 426 ? 0.2463 0.2290 0.2660 -0.0141 -0.0408 0.0153 426 GLU A CA 3275 C C . GLU A 426 ? 0.2472 0.2260 0.2609 -0.0165 -0.0394 0.0130 426 GLU A C 3276 O O . GLU A 426 ? 0.2475 0.2272 0.2619 -0.0184 -0.0406 0.0123 426 GLU A O 3277 C CB . GLU A 426 ? 0.2649 0.2477 0.2832 -0.0105 -0.0400 0.0204 426 GLU A CB 3278 C CG . GLU A 426 ? 0.2930 0.2782 0.3122 -0.0099 -0.0412 0.0239 426 GLU A CG 3279 C CD . GLU A 426 ? 0.3088 0.2998 0.3351 -0.0109 -0.0442 0.0258 426 GLU A CD 3280 O OE1 . GLU A 426 ? 0.3107 0.3042 0.3410 -0.0105 -0.0452 0.0263 426 GLU A OE1 3281 O OE2 . GLU A 426 ? 0.3499 0.3424 0.3771 -0.0124 -0.0457 0.0268 426 GLU A OE2 3282 N N . LEU A 427 ? 0.2480 0.2218 0.2549 -0.0167 -0.0370 0.0118 427 LEU A N 3283 C CA . LEU A 427 ? 0.2531 0.2224 0.2530 -0.0197 -0.0356 0.0095 427 LEU A CA 3284 C C . LEU A 427 ? 0.2452 0.2174 0.2473 -0.0239 -0.0360 0.0045 427 LEU A C 3285 O O . LEU A 427 ? 0.2486 0.2199 0.2483 -0.0263 -0.0362 0.0034 427 LEU A O 3286 C CB . LEU A 427 ? 0.2635 0.2259 0.2546 -0.0196 -0.0331 0.0091 427 LEU A CB 3287 C CG . LEU A 427 ? 0.2741 0.2302 0.2559 -0.0232 -0.0318 0.0071 427 LEU A CG 3288 C CD1 . LEU A 427 ? 0.2893 0.2426 0.2680 -0.0220 -0.0326 0.0102 427 LEU A CD1 3289 C CD2 . LEU A 427 ? 0.2927 0.2413 0.2653 -0.0234 -0.0297 0.0068 427 LEU A CD2 3290 N N . LEU A 428 ? 0.2351 0.2111 0.2415 -0.0243 -0.0363 0.0014 428 LEU A N 3291 C CA . LEU A 428 ? 0.2529 0.2327 0.2614 -0.0275 -0.0366 -0.0037 428 LEU A CA 3292 C C . LEU A 428 ? 0.2397 0.2225 0.2527 -0.0279 -0.0389 -0.0040 428 LEU A C 3293 O O . LEU A 428 ? 0.2394 0.2232 0.2510 -0.0309 -0.0386 -0.0071 428 LEU A O 3294 C CB . LEU A 428 ? 0.2492 0.2332 0.2624 -0.0268 -0.0371 -0.0066 428 LEU A CB 3295 C CG . LEU A 428 ? 0.2631 0.2525 0.2789 -0.0293 -0.0374 -0.0124 428 LEU A CG 3296 C CD1 . LEU A 428 ? 0.2691 0.2576 0.2782 -0.0338 -0.0348 -0.0155 428 LEU A CD1 3297 C CD2 . LEU A 428 ? 0.2604 0.2539 0.2810 -0.0275 -0.0384 -0.0148 428 LEU A CD2 3298 N N . VAL A 429 ? 0.2473 0.2316 0.2654 -0.0251 -0.0411 -0.0007 429 VAL A N 3299 C CA . VAL A 429 ? 0.2529 0.2393 0.2748 -0.0256 -0.0436 -0.0007 429 VAL A CA 3300 C C . VAL A 429 ? 0.2531 0.2370 0.2710 -0.0270 -0.0433 0.0014 429 VAL A C 3301 O O . VAL A 429 ? 0.2647 0.2493 0.2826 -0.0293 -0.0441 -0.0008 429 VAL A O 3302 C CB . VAL A 429 ? 0.2621 0.2504 0.2896 -0.0231 -0.0463 0.0021 429 VAL A CB 3303 C CG1 . VAL A 429 ? 0.2869 0.2760 0.3167 -0.0240 -0.0491 0.0028 429 VAL A CG1 3304 C CG2 . VAL A 429 ? 0.2634 0.2536 0.2941 -0.0219 -0.0470 -0.0009 429 VAL A CG2 3305 N N . ALA A 430 ? 0.2477 0.2283 0.2616 -0.0256 -0.0421 0.0054 430 ALA A N 3306 C CA . ALA A 430 ? 0.2631 0.2409 0.2726 -0.0265 -0.0419 0.0075 430 ALA A CA 3307 C C . ALA A 430 ? 0.2657 0.2404 0.2690 -0.0305 -0.0402 0.0034 430 ALA A C 3308 O O . ALA A 430 ? 0.2773 0.2516 0.2792 -0.0329 -0.0409 0.0026 430 ALA A O 3309 C CB . ALA A 430 ? 0.2540 0.2288 0.2598 -0.0234 -0.0410 0.0121 430 ALA A CB 3310 N N . LEU A 431 ? 0.2648 0.2376 0.2642 -0.0316 -0.0380 0.0009 431 LEU A N 3311 C CA . LEU A 431 ? 0.2850 0.2557 0.2782 -0.0361 -0.0361 -0.0031 431 LEU A CA 3312 C C . LEU A 431 ? 0.2778 0.2542 0.2751 -0.0389 -0.0368 -0.0079 431 LEU A C 3313 O O . LEU A 431 ? 0.2912 0.2665 0.2845 -0.0424 -0.0363 -0.0097 431 LEU A O 3314 C CB . LEU A 431 ? 0.2867 0.2550 0.2751 -0.0372 -0.0339 -0.0048 431 LEU A CB 3315 C CG . LEU A 431 ? 0.3029 0.2630 0.2830 -0.0356 -0.0326 -0.0012 431 LEU A CG 3316 C CD1 . LEU A 431 ? 0.2997 0.2577 0.2757 -0.0369 -0.0307 -0.0032 431 LEU A CD1 3317 C CD2 . LEU A 431 ? 0.3170 0.2700 0.2880 -0.0376 -0.0322 0.0000 431 LEU A CD2 3318 N N . GLU A 432 ? 0.2759 0.2578 0.2804 -0.0373 -0.0379 -0.0101 432 GLU A N 3319 C CA . GLU A 432 ? 0.2822 0.2696 0.2909 -0.0386 -0.0389 -0.0147 432 GLU A CA 3320 C C . GLU A 432 ? 0.2756 0.2625 0.2856 -0.0388 -0.0410 -0.0133 432 GLU A C 3321 O O . GLU A 432 ? 0.2690 0.2576 0.2778 -0.0415 -0.0408 -0.0168 432 GLU A O 3322 C CB . GLU A 432 ? 0.2950 0.2870 0.3105 -0.0357 -0.0403 -0.0165 432 GLU A CB 3323 C CG . GLU A 432 ? 0.3190 0.3130 0.3334 -0.0363 -0.0384 -0.0190 432 GLU A CG 3324 C CD . GLU A 432 ? 0.3653 0.3647 0.3789 -0.0396 -0.0369 -0.0250 432 GLU A CD 3325 O OE1 . GLU A 432 ? 0.3892 0.3902 0.4014 -0.0421 -0.0367 -0.0275 432 GLU A OE1 3326 O OE2 . GLU A 432 ? 0.4068 0.4093 0.4211 -0.0396 -0.0359 -0.0273 432 GLU A OE2 3327 N N . ASN A 433 ? 0.2633 0.2482 0.2756 -0.0361 -0.0429 -0.0083 433 ASN A N 3328 C CA . ASN A 433 ? 0.2641 0.2486 0.2776 -0.0365 -0.0452 -0.0066 433 ASN A CA 3329 C C . ASN A 433 ? 0.2769 0.2578 0.2839 -0.0395 -0.0441 -0.0059 433 ASN A C 3330 O O . ASN A 433 ? 0.2718 0.2531 0.2783 -0.0416 -0.0450 -0.0077 433 ASN A O 3331 C CB . ASN A 433 ? 0.2605 0.2448 0.2778 -0.0335 -0.0475 -0.0012 433 ASN A CB 3332 C CG . ASN A 433 ? 0.2528 0.2399 0.2760 -0.0313 -0.0496 -0.0019 433 ASN A CG 3333 O OD1 . ASN A 433 ? 0.2595 0.2486 0.2843 -0.0315 -0.0497 -0.0066 433 ASN A OD1 3334 N ND2 . ASN A 433 ? 0.2528 0.2401 0.2788 -0.0293 -0.0512 0.0026 433 ASN A ND2 3335 N N . GLN A 434 ? 0.2821 0.2588 0.2834 -0.0396 -0.0421 -0.0037 434 GLN A N 3336 C CA . GLN A 434 ? 0.3092 0.2813 0.3030 -0.0425 -0.0411 -0.0034 434 GLN A CA 3337 C C . GLN A 434 ? 0.3019 0.2754 0.2925 -0.0471 -0.0395 -0.0091 434 GLN A C 3338 O O . GLN A 434 ? 0.3033 0.2754 0.2907 -0.0500 -0.0397 -0.0100 434 GLN A O 3339 C CB . GLN A 434 ? 0.3406 0.3067 0.3273 -0.0415 -0.0394 -0.0005 434 GLN A CB 3340 C CG . GLN A 434 ? 0.3735 0.3332 0.3515 -0.0440 -0.0390 0.0005 434 GLN A CG 3341 C CD . GLN A 434 ? 0.4135 0.3734 0.3934 -0.0424 -0.0415 0.0044 434 GLN A CD 3342 O OE1 . GLN A 434 ? 0.4387 0.3999 0.4223 -0.0382 -0.0428 0.0087 434 GLN A OE1 3343 N NE2 . GLN A 434 ? 0.4736 0.4332 0.4518 -0.0459 -0.0422 0.0026 434 GLN A NE2 3344 N N . HIS A 435 ? 0.3076 0.2845 0.2997 -0.0477 -0.0380 -0.0128 435 HIS A N 3345 C CA . HIS A 435 ? 0.3222 0.3024 0.3118 -0.0521 -0.0362 -0.0185 435 HIS A CA 3346 C C . HIS A 435 ? 0.3151 0.3005 0.3096 -0.0524 -0.0377 -0.0219 435 HIS A C 3347 O O . HIS A 435 ? 0.3207 0.3071 0.3116 -0.0562 -0.0368 -0.0249 435 HIS A O 3348 C CB . HIS A 435 ? 0.3345 0.3185 0.3252 -0.0523 -0.0345 -0.0216 435 HIS A CB 3349 C CG . HIS A 435 ? 0.3608 0.3505 0.3499 -0.0568 -0.0326 -0.0276 435 HIS A CG 3350 N ND1 . HIS A 435 ? 0.3865 0.3847 0.3824 -0.0557 -0.0332 -0.0322 435 HIS A ND1 3351 C CD2 . HIS A 435 ? 0.3881 0.3763 0.3690 -0.0625 -0.0301 -0.0297 435 HIS A CD2 3352 C CE1 . HIS A 435 ? 0.3957 0.3990 0.3885 -0.0603 -0.0309 -0.0372 435 HIS A CE1 3353 N NE2 . HIS A 435 ? 0.4066 0.4038 0.3901 -0.0650 -0.0290 -0.0355 435 HIS A NE2 3354 N N . THR A 436 ? 0.2963 0.2845 0.2982 -0.0484 -0.0402 -0.0211 436 THR A N 3355 C CA . THR A 436 ? 0.2977 0.2889 0.3036 -0.0478 -0.0423 -0.0236 436 THR A CA 3356 C C . THR A 436 ? 0.3075 0.2948 0.3102 -0.0496 -0.0436 -0.0212 436 THR A C 3357 O O . THR A 436 ? 0.3176 0.3065 0.3190 -0.0519 -0.0436 -0.0248 436 THR A O 3358 C CB . THR A 436 ? 0.2933 0.2862 0.3062 -0.0432 -0.0451 -0.0227 436 THR A CB 3359 O OG1 . THR A 436 ? 0.3002 0.2974 0.3159 -0.0418 -0.0440 -0.0258 436 THR A OG1 3360 C CG2 . THR A 436 ? 0.2952 0.2893 0.3109 -0.0424 -0.0479 -0.0250 436 THR A CG2 3361 N N . ILE A 437 ? 0.2995 0.2820 0.3008 -0.0485 -0.0446 -0.0154 437 ILE A N 3362 C CA . ILE A 437 ? 0.3253 0.3042 0.3232 -0.0503 -0.0459 -0.0128 437 ILE A CA 3363 C C . ILE A 437 ? 0.3355 0.3124 0.3258 -0.0550 -0.0434 -0.0156 437 ILE A C 3364 O O . ILE A 437 ? 0.3272 0.3037 0.3152 -0.0577 -0.0439 -0.0174 437 ILE A O 3365 C CB . ILE A 437 ? 0.3276 0.3030 0.3251 -0.0481 -0.0471 -0.0062 437 ILE A CB 3366 C CG1 . ILE A 437 ? 0.3276 0.3055 0.3322 -0.0445 -0.0497 -0.0035 437 ILE A CG1 3367 C CG2 . ILE A 437 ? 0.3351 0.3068 0.3283 -0.0501 -0.0483 -0.0036 437 ILE A CG2 3368 C CD1 . ILE A 437 ? 0.3387 0.3183 0.3468 -0.0449 -0.0524 -0.0053 437 ILE A CD1 3369 N N . ASP A 438 ? 0.3284 0.3034 0.3139 -0.0563 -0.0408 -0.0159 438 ASP A N 3370 C CA . ASP A 438 ? 0.3566 0.3292 0.3337 -0.0616 -0.0384 -0.0186 438 ASP A CA 3371 C C . ASP A 438 ? 0.3355 0.3144 0.3133 -0.0649 -0.0370 -0.0251 438 ASP A C 3372 O O . ASP A 438 ? 0.3709 0.3485 0.3437 -0.0689 -0.0365 -0.0267 438 ASP A O 3373 C CB . ASP A 438 ? 0.3751 0.3439 0.3464 -0.0625 -0.0361 -0.0177 438 ASP A CB 3374 C CG . ASP A 438 ? 0.4048 0.3661 0.3724 -0.0597 -0.0370 -0.0117 438 ASP A CG 3375 O OD1 . ASP A 438 ? 0.4471 0.4068 0.4163 -0.0576 -0.0393 -0.0080 438 ASP A OD1 3376 O OD2 . ASP A 438 ? 0.4431 0.4004 0.4061 -0.0594 -0.0356 -0.0106 438 ASP A OD2 3377 N N . LEU A 439 ? 0.3252 0.3110 0.3090 -0.0632 -0.0366 -0.0288 439 LEU A N 3378 C CA . LEU A 439 ? 0.3345 0.3278 0.3195 -0.0655 -0.0353 -0.0352 439 LEU A CA 3379 C C . LEU A 439 ? 0.3431 0.3378 0.3309 -0.0645 -0.0374 -0.0368 439 LEU A C 3380 O O . LEU A 439 ? 0.3440 0.3420 0.3292 -0.0678 -0.0362 -0.0410 439 LEU A O 3381 C CB . LEU A 439 ? 0.3413 0.3421 0.3324 -0.0630 -0.0346 -0.0387 439 LEU A CB 3382 C CG . LEU A 439 ? 0.3407 0.3453 0.3406 -0.0571 -0.0373 -0.0395 439 LEU A CG 3383 C CD1 . LEU A 439 ? 0.3436 0.3539 0.3469 -0.0560 -0.0384 -0.0447 439 LEU A CD1 3384 C CD2 . LEU A 439 ? 0.3431 0.3520 0.3464 -0.0553 -0.0363 -0.0408 439 LEU A CD2 3385 N N . THR A 440 ? 0.3301 0.3219 0.3223 -0.0605 -0.0406 -0.0331 440 THR A N 3386 C CA . THR A 440 ? 0.3452 0.3369 0.3390 -0.0597 -0.0430 -0.0343 440 THR A CA 3387 C C . THR A 440 ? 0.3674 0.3537 0.3550 -0.0634 -0.0433 -0.0319 440 THR A C 3388 O O . THR A 440 ? 0.4059 0.3930 0.3916 -0.0653 -0.0436 -0.0349 440 THR A O 3389 C CB . THR A 440 ? 0.3349 0.3252 0.3347 -0.0549 -0.0466 -0.0314 440 THR A CB 3390 O OG1 . THR A 440 ? 0.3328 0.3186 0.3327 -0.0538 -0.0475 -0.0249 440 THR A OG1 3391 C CG2 . THR A 440 ? 0.3292 0.3248 0.3347 -0.0513 -0.0469 -0.0350 440 THR A CG2 3392 N N . ASP A 441 ? 0.3587 0.3392 0.3427 -0.0641 -0.0432 -0.0266 441 ASP A N 3393 C CA . ASP A 441 ? 0.3778 0.3529 0.3549 -0.0676 -0.0433 -0.0243 441 ASP A CA 3394 C C . ASP A 441 ? 0.3985 0.3747 0.3688 -0.0730 -0.0402 -0.0290 441 ASP A C 3395 O O . ASP A 441 ? 0.3966 0.3710 0.3623 -0.0765 -0.0403 -0.0301 441 ASP A O 3396 C CB . ASP A 441 ? 0.3859 0.3548 0.3596 -0.0667 -0.0436 -0.0182 441 ASP A CB 3397 C CG . ASP A 441 ? 0.4044 0.3721 0.3832 -0.0625 -0.0469 -0.0127 441 ASP A CG 3398 O OD1 . ASP A 441 ? 0.4176 0.3878 0.4018 -0.0609 -0.0493 -0.0130 441 ASP A OD1 3399 O OD2 . ASP A 441 ? 0.4151 0.3792 0.3920 -0.0609 -0.0472 -0.0079 441 ASP A OD2 3400 N N . SER A 442 ? 0.4075 0.3868 0.3769 -0.0742 -0.0375 -0.0315 442 SER A N 3401 C CA . SER A 442 ? 0.4217 0.4030 0.3844 -0.0801 -0.0344 -0.0358 442 SER A CA 3402 C C . SER A 442 ? 0.4106 0.3995 0.3757 -0.0815 -0.0338 -0.0419 442 SER A C 3403 O O . SER A 442 ? 0.4278 0.4162 0.3865 -0.0866 -0.0325 -0.0440 442 SER A O 3404 C CB . SER A 442 ? 0.4253 0.4092 0.3868 -0.0814 -0.0318 -0.0373 442 SER A CB 3405 O OG . SER A 442 ? 0.4415 0.4277 0.3960 -0.0880 -0.0289 -0.0413 442 SER A OG 3406 N N . GLU A 443 ? 0.4022 0.3978 0.3756 -0.0770 -0.0349 -0.0447 443 GLU A N 3407 C CA . GLU A 443 ? 0.4157 0.4182 0.3910 -0.0772 -0.0347 -0.0507 443 GLU A CA 3408 C C . GLU A 443 ? 0.4071 0.4043 0.3787 -0.0787 -0.0364 -0.0495 443 GLU A C 3409 O O . GLU A 443 ? 0.4102 0.4106 0.3782 -0.0822 -0.0349 -0.0537 443 GLU A O 3410 C CB . GLU A 443 ? 0.4257 0.4344 0.4095 -0.0712 -0.0362 -0.0539 443 GLU A CB 3411 C CG . GLU A 443 ? 0.4453 0.4619 0.4330 -0.0700 -0.0343 -0.0569 443 GLU A CG 3412 C CD . GLU A 443 ? 0.4689 0.4935 0.4527 -0.0754 -0.0304 -0.0621 443 GLU A CD 3413 O OE1 . GLU A 443 ? 0.5019 0.5309 0.4835 -0.0779 -0.0294 -0.0664 443 GLU A OE1 3414 O OE2 . GLU A 443 ? 0.4845 0.5111 0.4672 -0.0775 -0.0284 -0.0618 443 GLU A OE2 3415 N N . MET A 444 ? 0.4023 0.3918 0.3744 -0.0765 -0.0395 -0.0437 444 MET A N 3416 C CA . MET A 444 ? 0.4059 0.3899 0.3743 -0.0782 -0.0415 -0.0419 444 MET A CA 3417 C C . MET A 444 ? 0.4349 0.4151 0.3940 -0.0845 -0.0394 -0.0415 444 MET A C 3418 O O . MET A 444 ? 0.4033 0.3835 0.3581 -0.0879 -0.0390 -0.0441 444 MET A O 3419 C CB . MET A 444 ? 0.4026 0.3802 0.3734 -0.0751 -0.0451 -0.0352 444 MET A CB 3420 C CG . MET A 444 ? 0.4066 0.3788 0.3741 -0.0767 -0.0476 -0.0328 444 MET A CG 3421 S SD . MET A 444 ? 0.3950 0.3695 0.3657 -0.0745 -0.0500 -0.0373 444 MET A SD 3422 C CE . MET A 444 ? 0.4342 0.4135 0.3996 -0.0788 -0.0465 -0.0447 444 MET A CE 3423 N N . ASN A 445 ? 0.4238 0.4001 0.3791 -0.0860 -0.0382 -0.0381 445 ASN A N 3424 C CA . ASN A 445 ? 0.4592 0.4299 0.4043 -0.0920 -0.0366 -0.0372 445 ASN A CA 3425 C C . ASN A 445 ? 0.4290 0.4059 0.3699 -0.0974 -0.0331 -0.0435 445 ASN A C 3426 O O . ASN A 445 ? 0.4495 0.4237 0.3831 -0.1024 -0.0324 -0.0446 445 ASN A O 3427 C CB . ASN A 445 ? 0.4930 0.4574 0.4340 -0.0918 -0.0362 -0.0325 445 ASN A CB 3428 C CG . ASN A 445 ? 0.5461 0.5048 0.4901 -0.0869 -0.0395 -0.0259 445 ASN A CG 3429 O OD1 . ASN A 445 ? 0.6420 0.5997 0.5886 -0.0834 -0.0397 -0.0229 445 ASN A OD1 3430 N ND2 . ASN A 445 ? 0.5024 0.4580 0.4458 -0.0868 -0.0420 -0.0236 445 ASN A ND2 3431 N N . LYS A 446 ? 0.4340 0.4197 0.3797 -0.0964 -0.0311 -0.0478 446 LYS A N 3432 C CA . LYS A 446 ? 0.4646 0.4588 0.4074 -0.1014 -0.0277 -0.0542 446 LYS A CA 3433 C C . LYS A 446 ? 0.4648 0.4640 0.4088 -0.1018 -0.0279 -0.0587 446 LYS A C 3434 O O . LYS A 446 ? 0.4539 0.4558 0.3916 -0.1076 -0.0256 -0.0623 446 LYS A O 3435 C CB . LYS A 446 ? 0.4894 0.4933 0.4383 -0.0995 -0.0259 -0.0578 446 LYS A CB 3436 C CG . LYS A 446 ? 0.5192 0.5197 0.4635 -0.1023 -0.0242 -0.0553 446 LYS A CG 3437 C CD . LYS A 446 ? 0.5434 0.5500 0.4958 -0.0977 -0.0241 -0.0562 446 LYS A CD 3438 C CE . LYS A 446 ? 0.5559 0.5768 0.5133 -0.0980 -0.0220 -0.0632 446 LYS A CE 3439 N NZ . LYS A 446 ? 0.5898 0.6157 0.5549 -0.0931 -0.0224 -0.0636 446 LYS A NZ 3440 N N . LEU A 447 ? 0.4390 0.4386 0.3900 -0.0957 -0.0307 -0.0585 447 LEU A N 3441 C CA . LEU A 447 ? 0.4318 0.4348 0.3834 -0.0952 -0.0313 -0.0627 447 LEU A CA 3442 C C . LEU A 447 ? 0.4337 0.4284 0.3771 -0.0998 -0.0321 -0.0602 447 LEU A C 3443 O O . LEU A 447 ? 0.4399 0.4378 0.3791 -0.1034 -0.0306 -0.0644 447 LEU A O 3444 C CB . LEU A 447 ? 0.4421 0.4451 0.4018 -0.0878 -0.0348 -0.0624 447 LEU A CB 3445 C CG . LEU A 447 ? 0.4582 0.4634 0.4182 -0.0860 -0.0359 -0.0669 447 LEU A CG 3446 C CD1 . LEU A 447 ? 0.4674 0.4848 0.4276 -0.0873 -0.0325 -0.0749 447 LEU A CD1 3447 C CD2 . LEU A 447 ? 0.4537 0.4565 0.4202 -0.0790 -0.0399 -0.0656 447 LEU A CD2 3448 N N . PHE A 448 ? 0.4189 0.4035 0.3602 -0.0994 -0.0345 -0.0534 448 PHE A N 3449 C CA . PHE A 448 ? 0.4217 0.3981 0.3549 -0.1036 -0.0355 -0.0506 448 PHE A CA 3450 C C . PHE A 448 ? 0.4430 0.4195 0.3669 -0.1111 -0.0321 -0.0527 448 PHE A C 3451 O O . PHE A 448 ? 0.4382 0.4130 0.3556 -0.1156 -0.0316 -0.0545 448 PHE A O 3452 C CB . PHE A 448 ? 0.4161 0.3830 0.3488 -0.1015 -0.0385 -0.0429 448 PHE A CB 3453 C CG . PHE A 448 ? 0.4306 0.3891 0.3559 -0.1048 -0.0404 -0.0395 448 PHE A CG 3454 C CD1 . PHE A 448 ? 0.4291 0.3857 0.3560 -0.1034 -0.0432 -0.0388 448 PHE A CD1 3455 C CD2 . PHE A 448 ? 0.4522 0.4037 0.3681 -0.1094 -0.0395 -0.0368 448 PHE A CD2 3456 C CE1 . PHE A 448 ? 0.4405 0.3896 0.3608 -0.1064 -0.0451 -0.0356 448 PHE A CE1 3457 C CE2 . PHE A 448 ? 0.4453 0.3888 0.3542 -0.1122 -0.0415 -0.0336 448 PHE A CE2 3458 C CZ . PHE A 448 ? 0.4554 0.3982 0.3668 -0.1107 -0.0443 -0.0329 448 PHE A CZ 3459 N N . GLU A 449 ? 0.6010 0.3582 0.3469 -0.0613 0.1125 -0.0945 449 GLU A N 3460 C CA . GLU A 449 ? 0.6459 0.3953 0.3890 -0.0728 0.1219 -0.1004 449 GLU A CA 3461 C C . GLU A 449 ? 0.5871 0.3788 0.3511 -0.0789 0.1011 -0.1023 449 GLU A C 3462 O O . GLU A 449 ? 0.5820 0.3798 0.3635 -0.0759 0.1067 -0.1009 449 GLU A O 3463 C CB . GLU A 449 ? 0.7470 0.4509 0.4420 -0.0965 0.1386 -0.1123 449 GLU A CB 3464 C CG . GLU A 449 ? 0.8384 0.4897 0.5131 -0.0871 0.1717 -0.1084 449 GLU A CG 3465 C CD . GLU A 449 ? 0.8908 0.5394 0.5939 -0.0675 0.1905 -0.0973 449 GLU A CD 3466 O OE1 . GLU A 449 ? 0.9155 0.5634 0.6198 -0.0755 0.1945 -0.1016 449 GLU A OE1 3467 O OE2 . GLU A 449 ? 0.8797 0.5299 0.6048 -0.0445 0.2007 -0.0830 449 GLU A OE2 3468 N N . ARG A 450 ? 0.5910 0.4122 0.3537 -0.0855 0.0790 -0.1034 450 ARG A N 3469 C CA . ARG A 450 ? 0.5943 0.4613 0.3822 -0.0880 0.0611 -0.1012 450 ARG A CA 3470 C C . ARG A 450 ? 0.5442 0.4300 0.3666 -0.0636 0.0592 -0.0914 450 ARG A C 3471 O O . ARG A 450 ? 0.5361 0.4396 0.3780 -0.0630 0.0591 -0.0901 450 ARG A O 3472 C CB . ARG A 450 ? 0.6423 0.5414 0.4234 -0.0964 0.0385 -0.0997 450 ARG A CB 3473 C CG . ARG A 450 ? 0.6701 0.5965 0.4692 -0.0732 0.0244 -0.0876 450 ARG A CG 3474 C CD . ARG A 450 ? 0.7157 0.6779 0.5080 -0.0802 0.0031 -0.0827 450 ARG A CD 3475 N NE . ARG A 450 ? 0.7862 0.7236 0.5359 -0.1009 0.0016 -0.0910 450 ARG A NE 3476 C CZ . ARG A 450 ? 0.8290 0.7587 0.5537 -0.0959 -0.0055 -0.0872 450 ARG A CZ 3477 N NH1 . ARG A 450 ? 0.8278 0.7750 0.5667 -0.0707 -0.0125 -0.0743 450 ARG A NH1 3478 N NH2 . ARG A 450 ? 0.8467 0.7456 0.5258 -0.1171 -0.0039 -0.0964 450 ARG A NH2 3479 N N . THR A 451 ? 0.5073 0.3849 0.3332 -0.0460 0.0594 -0.0851 451 THR A N 3480 C CA . THR A 451 ? 0.4755 0.3633 0.3243 -0.0273 0.0573 -0.0772 451 THR A CA 3481 C C . THR A 451 ? 0.4774 0.3518 0.3344 -0.0247 0.0711 -0.0766 451 THR A C 3482 O O . THR A 451 ? 0.4769 0.3635 0.3481 -0.0185 0.0693 -0.0737 451 THR A O 3483 C CB . THR A 451 ? 0.4595 0.3377 0.3058 -0.0154 0.0555 -0.0719 451 THR A CB 3484 O OG1 . THR A 451 ? 0.4659 0.3512 0.2992 -0.0166 0.0455 -0.0717 451 THR A OG1 3485 C CG2 . THR A 451 ? 0.4221 0.3077 0.2837 -0.0019 0.0513 -0.0656 451 THR A CG2 3486 N N . LYS A 452 ? 0.5155 0.3620 0.3609 -0.0279 0.0872 -0.0778 452 LYS A N 3487 C CA . LYS A 452 ? 0.5377 0.3692 0.3883 -0.0229 0.1035 -0.0742 452 LYS A CA 3488 C C . LYS A 452 ? 0.5552 0.3911 0.4064 -0.0324 0.1065 -0.0796 452 LYS A C 3489 O O . LYS A 452 ? 0.5118 0.3509 0.3752 -0.0228 0.1104 -0.0743 452 LYS A O 3490 C CB . LYS A 452 ? 0.5973 0.3935 0.4302 -0.0249 0.1256 -0.0738 452 LYS A CB 3491 C CG . LYS A 452 ? 0.6402 0.4185 0.4765 -0.0165 0.1464 -0.0671 452 LYS A CG 3492 C CD . LYS A 452 ? 0.7175 0.4576 0.5364 -0.0134 0.1736 -0.0630 452 LYS A CD 3493 C CE . LYS A 452 ? 0.7657 0.4957 0.5954 0.0037 0.1935 -0.0492 452 LYS A CE 3494 N NZ . LYS A 452 ? 0.7644 0.5333 0.6289 0.0216 0.1768 -0.0343 452 LYS A NZ 3495 N N . LYS A 453 ? 0.5638 0.4020 0.4015 -0.0524 0.1034 -0.0893 453 LYS A N 3496 C CA . LYS A 453 ? 0.5898 0.4347 0.4300 -0.0666 0.1073 -0.0949 453 LYS A CA 3497 C C . LYS A 453 ? 0.5447 0.4265 0.4124 -0.0566 0.0940 -0.0891 453 LYS A C 3498 O O . LYS A 453 ? 0.5347 0.4154 0.4105 -0.0558 0.1032 -0.0882 453 LYS A O 3499 C CB . LYS A 453 ? 0.6330 0.4769 0.4524 -0.0959 0.1044 -0.1063 453 LYS A CB 3500 C CG . LYS A 453 ? 0.6947 0.4911 0.4749 -0.1096 0.1211 -0.1142 453 LYS A CG 3501 C CD . LYS A 453 ? 0.7337 0.4827 0.4969 -0.1101 0.1521 -0.1160 453 LYS A CD 3502 C CE . LYS A 453 ? 0.7843 0.4784 0.5065 -0.1164 0.1746 -0.1205 453 LYS A CE 3503 N NZ . LYS A 453 ? 0.8225 0.4752 0.5008 -0.1494 0.1910 -0.1356 453 LYS A NZ 3504 N N . GLN A 454 ? 0.5106 0.4192 0.3891 -0.0473 0.0762 -0.0842 454 GLN A N 3505 C CA . GLN A 454 ? 0.5024 0.4385 0.4018 -0.0351 0.0683 -0.0772 454 GLN A CA 3506 C C . GLN A 454 ? 0.4781 0.3979 0.3805 -0.0183 0.0763 -0.0720 454 GLN A C 3507 O O . GLN A 454 ? 0.4550 0.3825 0.3672 -0.0131 0.0801 -0.0689 454 GLN A O 3508 C CB . GLN A 454 ? 0.5091 0.4640 0.4121 -0.0237 0.0534 -0.0711 454 GLN A CB 3509 C CG . GLN A 454 ? 0.5459 0.5348 0.4549 -0.0336 0.0410 -0.0697 454 GLN A CG 3510 C CD . GLN A 454 ? 0.5387 0.5407 0.4484 -0.0169 0.0303 -0.0607 454 GLN A CD 3511 O OE1 . GLN A 454 ? 0.5585 0.5465 0.4510 -0.0166 0.0260 -0.0622 454 GLN A OE1 3512 N NE2 . GLN A 454 ? 0.5176 0.5428 0.4452 -0.0021 0.0292 -0.0506 454 GLN A NE2 3513 N N . LEU A 455 ? 0.4561 0.3559 0.3499 -0.0101 0.0780 -0.0696 455 LEU A N 3514 C CA . LEU A 455 ? 0.4394 0.3294 0.3340 0.0040 0.0797 -0.0629 455 LEU A CA 3515 C C . LEU A 455 ? 0.4411 0.3167 0.3341 0.0051 0.0944 -0.0612 455 LEU A C 3516 O O . LEU A 455 ? 0.4296 0.3019 0.3216 0.0154 0.0946 -0.0556 455 LEU A O 3517 C CB . LEU A 455 ? 0.4382 0.3204 0.3297 0.0097 0.0754 -0.0585 455 LEU A CB 3518 C CG . LEU A 455 ? 0.4325 0.3232 0.3219 0.0110 0.0628 -0.0591 455 LEU A CG 3519 C CD1 . LEU A 455 ? 0.4330 0.3162 0.3212 0.0122 0.0612 -0.0557 455 LEU A CD1 3520 C CD2 . LEU A 455 ? 0.4377 0.3320 0.3247 0.0196 0.0559 -0.0562 455 LEU A CD2 3521 N N . ARG A 456 ? 0.4720 0.3343 0.3594 -0.0061 0.1082 -0.0663 456 ARG A N 3522 C CA . ARG A 456 ? 0.5111 0.3535 0.3931 -0.0053 0.1269 -0.0647 456 ARG A CA 3523 C C . ARG A 456 ? 0.5065 0.3387 0.3873 0.0130 0.1304 -0.0524 456 ARG A C 3524 O O . ARG A 456 ? 0.4994 0.3292 0.3814 0.0185 0.1295 -0.0468 456 ARG A O 3525 C CB . ARG A 456 ? 0.5309 0.3837 0.4197 -0.0091 0.1292 -0.0669 456 ARG A CB 3526 C CG . ARG A 456 ? 0.5575 0.4240 0.4511 -0.0311 0.1298 -0.0765 456 ARG A CG 3527 C CD . ARG A 456 ? 0.5982 0.4350 0.4755 -0.0481 0.1510 -0.0835 456 ARG A CD 3528 N NE . ARG A 456 ? 0.6256 0.4444 0.5005 -0.0446 0.1700 -0.0809 456 ARG A NE 3529 C CZ . ARG A 456 ? 0.6405 0.4694 0.5243 -0.0587 0.1767 -0.0851 456 ARG A CZ 3530 N NH1 . ARG A 456 ? 0.6447 0.5102 0.5457 -0.0772 0.1635 -0.0902 456 ARG A NH1 3531 N NH2 . ARG A 456 ? 0.6570 0.4626 0.5346 -0.0536 0.1971 -0.0820 456 ARG A NH2 3532 N N . GLU A 457 ? 0.5119 0.3419 0.3914 0.0225 0.1329 -0.0467 457 GLU A N 3533 C CA . GLU A 457 ? 0.5326 0.3575 0.4091 0.0388 0.1338 -0.0330 457 GLU A CA 3534 C C . GLU A 457 ? 0.5002 0.3428 0.3781 0.0446 0.1111 -0.0283 457 GLU A C 3535 O O . GLU A 457 ? 0.5088 0.3531 0.3822 0.0547 0.1061 -0.0169 457 GLU A O 3536 C CB . GLU A 457 ? 0.5773 0.3845 0.4435 0.0453 0.1498 -0.0287 457 GLU A CB 3537 C CG . GLU A 457 ? 0.6297 0.4106 0.4886 0.0382 0.1761 -0.0328 457 GLU A CG 3538 C CD . GLU A 457 ? 0.6528 0.4205 0.5100 0.0440 0.1880 -0.0255 457 GLU A CD 3539 O OE1 . GLU A 457 ? 0.7165 0.4924 0.5792 0.0620 0.1845 -0.0092 457 GLU A OE1 3540 O OE2 . GLU A 457 ? 0.6736 0.4231 0.5228 0.0306 0.2014 -0.0347 457 GLU A OE2 3541 N N . ASN A 458 ? 0.4704 0.3245 0.3512 0.0375 0.0980 -0.0364 458 ASN A N 3542 C CA . ASN A 458 ? 0.4543 0.3146 0.3279 0.0403 0.0806 -0.0343 458 ASN A CA 3543 C C . ASN A 458 ? 0.4354 0.3060 0.3153 0.0381 0.0686 -0.0303 458 ASN A C 3544 O O . ASN A 458 ? 0.4401 0.3124 0.3110 0.0364 0.0547 -0.0292 458 ASN A O 3545 C CB . ASN A 458 ? 0.4447 0.3072 0.3153 0.0373 0.0772 -0.0423 458 ASN A CB 3546 C CG . ASN A 458 ? 0.4649 0.3220 0.3336 0.0395 0.0894 -0.0438 458 ASN A CG 3547 O OD1 . ASN A 458 ? 0.4742 0.3203 0.3383 0.0429 0.1000 -0.0401 458 ASN A OD1 3548 N ND2 . ASN A 458 ? 0.4753 0.3405 0.3482 0.0394 0.0897 -0.0471 458 ASN A ND2 3549 N N . ALA A 459 ? 0.4248 0.2983 0.3173 0.0369 0.0762 -0.0286 459 ALA A N 3550 C CA . ALA A 459 ? 0.4118 0.2959 0.3145 0.0351 0.0691 -0.0239 459 ALA A CA 3551 C C . ALA A 459 ? 0.4292 0.3136 0.3448 0.0414 0.0834 -0.0134 459 ALA A C 3552 O O . ALA A 459 ? 0.4530 0.3212 0.3644 0.0443 0.1020 -0.0142 459 ALA A O 3553 C CB . ALA A 459 ? 0.4029 0.2856 0.3035 0.0273 0.0655 -0.0342 459 ALA A CB 3554 N N . GLU A 460 ? 0.4119 0.3127 0.3428 0.0432 0.0777 -0.0027 460 GLU A N 3555 C CA . GLU A 460 ? 0.4312 0.3338 0.3782 0.0518 0.0946 0.0099 460 GLU A CA 3556 C C . GLU A 460 ? 0.4354 0.3399 0.3906 0.0461 0.0955 0.0079 460 GLU A C 3557 O O . GLU A 460 ? 0.4222 0.3378 0.3786 0.0371 0.0785 0.0035 460 GLU A O 3558 C CB . GLU A 460 ? 0.4292 0.3575 0.3947 0.0632 0.0905 0.0318 460 GLU A CB 3559 C CG . GLU A 460 ? 0.4338 0.3531 0.3881 0.0734 0.0974 0.0371 460 GLU A CG 3560 C CD . GLU A 460 ? 0.4369 0.3863 0.4060 0.0850 0.0886 0.0607 460 GLU A CD 3561 O OE1 . GLU A 460 ? 0.4310 0.4122 0.4279 0.0884 0.0837 0.0777 460 GLU A OE1 3562 O OE2 . GLU A 460 ? 0.4341 0.3776 0.3875 0.0905 0.0861 0.0635 460 GLU A OE2 3563 N N . ASP A 461 ? 0.4609 0.3475 0.4161 0.0510 0.1184 0.0105 461 ASP A N 3564 C CA . ASP A 461 ? 0.4800 0.3622 0.4398 0.0481 0.1253 0.0107 461 ASP A CA 3565 C C . ASP A 461 ? 0.4777 0.3924 0.4716 0.0558 0.1233 0.0319 461 ASP A C 3566 O O . ASP A 461 ? 0.4771 0.4018 0.4894 0.0707 0.1379 0.0511 461 ASP A O 3567 C CB . ASP A 461 ? 0.5172 0.3620 0.4587 0.0511 0.1547 0.0078 461 ASP A CB 3568 C CG . ASP A 461 ? 0.5404 0.3695 0.4756 0.0475 0.1653 0.0054 461 ASP A CG 3569 O OD1 . ASP A 461 ? 0.5349 0.3856 0.4886 0.0466 0.1546 0.0111 461 ASP A OD1 3570 O OD2 . ASP A 461 ? 0.6110 0.4009 0.5182 0.0442 0.1867 -0.0023 461 ASP A OD2 3571 N N . MET A 462 ? 0.4599 0.3916 0.4628 0.0455 0.1069 0.0299 462 MET A N 3572 C CA . MET A 462 ? 0.4755 0.4450 0.5143 0.0469 0.1017 0.0497 462 MET A CA 3573 C C . MET A 462 ? 0.5031 0.4683 0.5593 0.0548 0.1263 0.0611 462 MET A C 3574 O O . MET A 462 ? 0.5139 0.5147 0.6064 0.0560 0.1252 0.0797 462 MET A O 3575 C CB . MET A 462 ? 0.4697 0.4537 0.5067 0.0287 0.0761 0.0417 462 MET A CB 3576 C CG . MET A 462 ? 0.4843 0.4673 0.4997 0.0205 0.0542 0.0313 462 MET A CG 3577 S SD . MET A 462 ? 0.5276 0.5010 0.5213 -0.0003 0.0343 0.0160 462 MET A SD 3578 C CE . MET A 462 ? 0.5274 0.5348 0.5573 -0.0106 0.0317 0.0321 462 MET A CE 3579 N N . GLY A 463 ? 0.4967 0.4188 0.5262 0.0582 0.1487 0.0504 463 GLY A N 3580 C CA . GLY A 463 ? 0.5310 0.4371 0.5678 0.0681 0.1784 0.0614 463 GLY A CA 3581 C C . GLY A 463 ? 0.5278 0.4256 0.5607 0.0583 0.1787 0.0551 463 GLY A C 3582 O O . GLY A 463 ? 0.5562 0.4349 0.5902 0.0662 0.2055 0.0632 463 GLY A O 3583 N N . ASN A 464 ? 0.5009 0.4063 0.5244 0.0424 0.1525 0.0409 464 ASN A N 3584 C CA . ASN A 464 ? 0.5256 0.4233 0.5449 0.0334 0.1521 0.0362 464 ASN A CA 3585 C C . ASN A 464 ? 0.5245 0.3887 0.4991 0.0240 0.1426 0.0131 464 ASN A C 3586 O O . ASN A 464 ? 0.5323 0.3912 0.4984 0.0159 0.1355 0.0074 464 ASN A O 3587 C CB . ASN A 464 ? 0.5132 0.4526 0.5643 0.0225 0.1316 0.0446 464 ASN A CB 3588 C CG . ASN A 464 ? 0.5130 0.4615 0.5503 0.0116 0.1028 0.0329 464 ASN A CG 3589 O OD1 . ASN A 464 ? 0.5163 0.4527 0.5339 0.0162 0.0987 0.0242 464 ASN A OD1 3590 N ND2 . ASN A 464 ? 0.5309 0.4971 0.5758 -0.0038 0.0853 0.0326 464 ASN A ND2 3591 N N . GLY A 465 ? 0.5038 0.3472 0.4512 0.0251 0.1432 0.0016 465 GLY A N 3592 C CA . GLY A 465 ? 0.5059 0.3306 0.4180 0.0167 0.1305 -0.0165 465 GLY A CA 3593 C C . GLY A 465 ? 0.4693 0.3137 0.3833 0.0121 0.1057 -0.0227 465 GLY A C 3594 O O . GLY A 465 ? 0.4917 0.3272 0.3827 0.0081 0.0952 -0.0337 465 GLY A O 3595 N N . CYS A 466 ? 0.4446 0.3148 0.3833 0.0139 0.0975 -0.0142 466 CYS A N 3596 C CA . CYS A 466 ? 0.4478 0.3298 0.3827 0.0096 0.0772 -0.0195 466 CYS A CA 3597 C C . CYS A 466 ? 0.4319 0.3231 0.3722 0.0147 0.0756 -0.0170 466 CYS A C 3598 O O . CYS A 466 ? 0.4198 0.3177 0.3764 0.0223 0.0878 -0.0059 466 CYS A O 3599 C CB . CYS A 466 ? 0.4719 0.3718 0.4213 0.0019 0.0649 -0.0131 466 CYS A CB 3600 S SG . CYS A 466 ? 0.5171 0.4068 0.4655 -0.0053 0.0706 -0.0126 466 CYS A SG 3601 N N . PHE A 467 ? 0.4187 0.3082 0.3443 0.0125 0.0633 -0.0258 467 PHE A N 3602 C CA . PHE A 467 ? 0.4047 0.3011 0.3319 0.0163 0.0598 -0.0239 467 PHE A CA 3603 C C . PHE A 467 ? 0.4109 0.3194 0.3383 0.0119 0.0433 -0.0202 467 PHE A C 3604 O O . PHE A 467 ? 0.4124 0.3136 0.3265 0.0047 0.0342 -0.0260 467 PHE A O 3605 C CB . PHE A 467 ? 0.4036 0.2882 0.3130 0.0162 0.0604 -0.0355 467 PHE A CB 3606 C CG . PHE A 467 ? 0.4168 0.2884 0.3190 0.0143 0.0737 -0.0410 467 PHE A CG 3607 C CD1 . PHE A 467 ? 0.4418 0.3045 0.3455 0.0169 0.0893 -0.0383 467 PHE A CD1 3608 C CD2 . PHE A 467 ? 0.4249 0.2892 0.3136 0.0093 0.0717 -0.0484 467 PHE A CD2 3609 C CE1 . PHE A 467 ? 0.4645 0.3066 0.3525 0.0106 0.1032 -0.0454 467 PHE A CE1 3610 C CE2 . PHE A 467 ? 0.4516 0.3014 0.3265 0.0034 0.0820 -0.0543 467 PHE A CE2 3611 C CZ . PHE A 467 ? 0.4665 0.3030 0.3390 0.0022 0.0979 -0.0540 467 PHE A CZ 3612 N N . LYS A 468 ? 0.4039 0.3273 0.3421 0.0158 0.0409 -0.0098 468 LYS A N 3613 C CA . LYS A 468 ? 0.4160 0.3456 0.3441 0.0105 0.0250 -0.0078 468 LYS A CA 3614 C C . LYS A 468 ? 0.4140 0.3265 0.3219 0.0164 0.0279 -0.0156 468 LYS A C 3615 O O . LYS A 468 ? 0.4072 0.3197 0.3206 0.0254 0.0384 -0.0119 468 LYS A O 3616 C CB . LYS A 468 ? 0.4445 0.4036 0.3941 0.0124 0.0192 0.0103 468 LYS A CB 3617 C CG . LYS A 468 ? 0.4839 0.4477 0.4152 0.0037 0.0000 0.0120 468 LYS A CG 3618 C CD . LYS A 468 ? 0.5081 0.5118 0.4638 0.0021 -0.0113 0.0328 468 LYS A CD 3619 C CE . LYS A 468 ? 0.5569 0.5623 0.4855 -0.0100 -0.0329 0.0336 468 LYS A CE 3620 N NZ . LYS A 468 ? 0.5762 0.6299 0.5306 -0.0128 -0.0482 0.0569 468 LYS A NZ 3621 N N . ILE A 469 ? 0.4195 0.3146 0.3036 0.0118 0.0220 -0.0258 469 ILE A N 3622 C CA . ILE A 469 ? 0.4323 0.3124 0.2992 0.0178 0.0266 -0.0319 469 ILE A CA 3623 C C . ILE A 469 ? 0.4626 0.3369 0.3099 0.0152 0.0172 -0.0278 469 ILE A C 3624 O O . ILE A 469 ? 0.4989 0.3653 0.3278 0.0045 0.0058 -0.0289 469 ILE A O 3625 C CB . ILE A 469 ? 0.4503 0.3151 0.3029 0.0182 0.0289 -0.0413 469 ILE A CB 3626 C CG1 . ILE A 469 ? 0.4336 0.3059 0.3011 0.0191 0.0351 -0.0444 469 ILE A CG1 3627 C CG2 . ILE A 469 ? 0.4453 0.2982 0.2840 0.0255 0.0352 -0.0444 469 ILE A CG2 3628 C CD1 . ILE A 469 ? 0.4590 0.3218 0.3140 0.0210 0.0349 -0.0491 469 ILE A CD1 3629 N N . TYR A 470 ? 0.4706 0.3449 0.3166 0.0233 0.0226 -0.0234 470 TYR A N 3630 C CA . TYR A 470 ? 0.4987 0.3702 0.3251 0.0216 0.0127 -0.0165 470 TYR A CA 3631 C C . TYR A 470 ? 0.5325 0.3724 0.3218 0.0218 0.0151 -0.0243 470 TYR A C 3632 O O . TYR A 470 ? 0.5462 0.3762 0.3169 0.0263 0.0159 -0.0201 470 TYR A O 3633 C CB . TYR A 470 ? 0.4881 0.3735 0.3298 0.0329 0.0196 -0.0044 470 TYR A CB 3634 C CG . TYR A 470 ? 0.4650 0.3813 0.3366 0.0340 0.0155 0.0098 470 TYR A CG 3635 C CD1 . TYR A 470 ? 0.4411 0.3644 0.3391 0.0383 0.0288 0.0100 470 TYR A CD1 3636 C CD2 . TYR A 470 ? 0.4848 0.4244 0.3579 0.0312 -0.0006 0.0250 470 TYR A CD2 3637 C CE1 . TYR A 470 ? 0.4410 0.3904 0.3673 0.0426 0.0301 0.0255 470 TYR A CE1 3638 C CE2 . TYR A 470 ? 0.4718 0.4475 0.3799 0.0350 -0.0026 0.0426 470 TYR A CE2 3639 C CZ . TYR A 470 ? 0.4543 0.4328 0.3896 0.0422 0.0150 0.0430 470 TYR A CZ 3640 O OH . TYR A 470 ? 0.4675 0.4786 0.4380 0.0490 0.0183 0.0623 470 TYR A OH 3641 N N . HIS A 471 ? 0.5512 0.3729 0.3280 0.0193 0.0188 -0.0340 471 HIS A N 3642 C CA . HIS A 471 ? 0.5900 0.3767 0.3294 0.0216 0.0254 -0.0395 471 HIS A CA 3643 C C . HIS A 471 ? 0.6111 0.3772 0.3317 0.0152 0.0252 -0.0461 471 HIS A C 3644 O O . HIS A 471 ? 0.5842 0.3655 0.3254 0.0115 0.0219 -0.0471 471 HIS A O 3645 C CB . HIS A 471 ? 0.5813 0.3656 0.3309 0.0362 0.0437 -0.0407 471 HIS A CB 3646 C CG . HIS A 471 ? 0.5343 0.3371 0.3145 0.0407 0.0509 -0.0436 471 HIS A CG 3647 N ND1 . HIS A 471 ? 0.5526 0.3452 0.3256 0.0447 0.0562 -0.0464 471 HIS A ND1 3648 C CD2 . HIS A 471 ? 0.4954 0.3246 0.3095 0.0416 0.0545 -0.0433 471 HIS A CD2 3649 C CE1 . HIS A 471 ? 0.5093 0.3277 0.3131 0.0475 0.0589 -0.0467 471 HIS A CE1 3650 N NE2 . HIS A 471 ? 0.4908 0.3291 0.3170 0.0435 0.0578 -0.0462 471 HIS A NE2 3651 N N . LYS A 472 ? 0.6497 0.3750 0.3261 0.0146 0.0315 -0.0501 472 LYS A N 3652 C CA . LYS A 472 ? 0.7084 0.4032 0.3593 0.0111 0.0373 -0.0556 472 LYS A CA 3653 C C . LYS A 472 ? 0.6644 0.3751 0.3464 0.0281 0.0506 -0.0541 472 LYS A C 3654 O O . LYS A 472 ? 0.6464 0.3660 0.3431 0.0428 0.0624 -0.0509 472 LYS A O 3655 C CB . LYS A 472 ? 0.7880 0.4271 0.3800 0.0108 0.0486 -0.0592 472 LYS A CB 3656 C CG . LYS A 472 ? 0.8827 0.4770 0.4360 0.0057 0.0582 -0.0647 472 LYS A CG 3657 C CD . LYS A 472 ? 0.9749 0.5046 0.4643 0.0087 0.0766 -0.0677 472 LYS A CD 3658 C CE . LYS A 472 ? 1.0687 0.5399 0.5036 -0.0033 0.0861 -0.0747 472 LYS A CE 3659 N NZ . LYS A 472 ? 1.0943 0.5743 0.5550 0.0097 0.0972 -0.0717 472 LYS A NZ 3660 N N . CYS A 473 ? 0.6521 0.3690 0.3447 0.0249 0.0481 -0.0554 473 CYS A N 3661 C CA . CYS A 473 ? 0.6449 0.3825 0.3662 0.0397 0.0568 -0.0523 473 CYS A CA 3662 C C . CYS A 473 ? 0.6700 0.3794 0.3679 0.0414 0.0638 -0.0530 473 CYS A C 3663 O O . CYS A 473 ? 0.6639 0.3782 0.3674 0.0318 0.0564 -0.0550 473 CYS A O 3664 C CB . CYS A 473 ? 0.6404 0.4226 0.4059 0.0365 0.0473 -0.0512 473 CYS A CB 3665 S SG . CYS A 473 ? 0.6470 0.4611 0.4454 0.0492 0.0534 -0.0478 473 CYS A SG 3666 N N . ASP A 474 ? 0.6913 0.3676 0.3612 0.0555 0.0816 -0.0500 474 ASP A N 3667 C CA . ASP A 474 ? 0.7271 0.3643 0.3652 0.0609 0.0948 -0.0490 474 ASP A CA 3668 C C . ASP A 474 ? 0.7080 0.3743 0.3763 0.0763 0.0977 -0.0412 474 ASP A C 3669 O O . ASP A 474 ? 0.6494 0.3653 0.3606 0.0779 0.0868 -0.0388 474 ASP A O 3670 C CB . ASP A 474 ? 0.7947 0.3803 0.3883 0.0739 0.1181 -0.0462 474 ASP A CB 3671 C CG . ASP A 474 ? 0.7843 0.3948 0.4056 0.1007 0.1330 -0.0341 474 ASP A CG 3672 O OD1 . ASP A 474 ? 0.7477 0.4146 0.4201 0.1088 0.1253 -0.0277 474 ASP A OD1 3673 O OD2 . ASP A 474 ? 0.8248 0.3963 0.4144 0.1127 0.1539 -0.0303 474 ASP A OD2 3674 N N . ASN A 475 ? 0.7307 0.3630 0.3720 0.0865 0.1126 -0.0370 475 ASN A N 3675 C CA . ASN A 475 ? 0.7202 0.3794 0.3852 0.0997 0.1125 -0.0287 475 ASN A CA 3676 C C . ASN A 475 ? 0.6715 0.3836 0.3788 0.1189 0.1119 -0.0169 475 ASN A C 3677 O O . ASN A 475 ? 0.6253 0.3801 0.3641 0.1179 0.0991 -0.0145 475 ASN A O 3678 C CB . ASN A 475 ? 0.7908 0.4003 0.4161 0.1117 0.1327 -0.0233 475 ASN A CB 3679 C CG . ASN A 475 ? 0.8369 0.4068 0.4304 0.0870 0.1293 -0.0352 475 ASN A CG 3680 O OD1 . ASN A 475 ? 0.8080 0.3989 0.4181 0.0628 0.1095 -0.0449 475 ASN A OD1 3681 N ND2 . ASN A 475 ? 0.9038 0.4161 0.4519 0.0933 0.1507 -0.0331 475 ASN A ND2 3682 N N . ALA A 476 ? 0.6774 0.3854 0.3834 0.1340 0.1261 -0.0095 476 ALA A N 3683 C CA . ALA A 476 ? 0.6571 0.4202 0.4073 0.1496 0.1262 0.0031 476 ALA A CA 3684 C C . ALA A 476 ? 0.5997 0.4083 0.3863 0.1305 0.1059 -0.0056 476 ALA A C 3685 O O . ALA A 476 ? 0.5818 0.4404 0.4041 0.1303 0.0955 -0.0007 476 ALA A O 3686 C CB . ALA A 476 ? 0.6801 0.4253 0.4209 0.1704 0.1503 0.0141 476 ALA A CB 3687 N N . CYS A 477 ? 0.6162 0.4044 0.3892 0.1134 0.1005 -0.0180 477 CYS A N 3688 C CA . CYS A 477 ? 0.5855 0.4062 0.3862 0.0970 0.0856 -0.0255 477 CYS A CA 3689 C C . CYS A 477 ? 0.5433 0.3876 0.3604 0.0853 0.0704 -0.0297 477 CYS A C 3690 O O . CYS A 477 ? 0.5251 0.4073 0.3710 0.0802 0.0631 -0.0295 477 CYS A O 3691 C CB . CYS A 477 ? 0.6289 0.4191 0.4059 0.0843 0.0836 -0.0346 477 CYS A CB 3692 S SG . CYS A 477 ? 0.6214 0.4395 0.4240 0.0681 0.0706 -0.0411 477 CYS A SG 3693 N N . ILE A 478 ? 0.5452 0.3640 0.3411 0.0797 0.0675 -0.0336 478 ILE A N 3694 C CA . ILE A 478 ? 0.5328 0.3672 0.3397 0.0711 0.0573 -0.0363 478 ILE A CA 3695 C C . ILE A 478 ? 0.5369 0.4017 0.3595 0.0821 0.0561 -0.0276 478 ILE A C 3696 O O . ILE A 478 ? 0.5144 0.4061 0.3541 0.0729 0.0465 -0.0301 478 ILE A O 3697 C CB . ILE A 478 ? 0.5534 0.3545 0.3354 0.0641 0.0576 -0.0400 478 ILE A CB 3698 C CG1 . ILE A 478 ? 0.5527 0.3354 0.3237 0.0479 0.0532 -0.0472 478 ILE A CG1 3699 C CG2 . ILE A 478 ? 0.5417 0.3573 0.3344 0.0589 0.0512 -0.0406 478 ILE A CG2 3700 C CD1 . ILE A 478 ? 0.5249 0.3348 0.3223 0.0364 0.0432 -0.0502 478 ILE A CD1 3701 N N . GLY A 479 ? 0.5656 0.4246 0.3795 0.1017 0.0666 -0.0163 479 GLY A N 3702 C CA . GLY A 479 ? 0.5558 0.4531 0.3882 0.1150 0.0640 -0.0032 479 GLY A CA 3703 C C . GLY A 479 ? 0.5305 0.4783 0.3983 0.1075 0.0549 -0.0020 479 GLY A C 3704 O O . GLY A 479 ? 0.5188 0.5029 0.4018 0.1016 0.0427 0.0009 479 GLY A O 3705 N N . SER A 480 ? 0.5146 0.4617 0.3915 0.1053 0.0612 -0.0048 480 SER A N 3706 C CA . SER A 480 ? 0.5040 0.4941 0.4133 0.0955 0.0559 -0.0046 480 SER A CA 3707 C C . SER A 480 ? 0.4957 0.4952 0.4090 0.0708 0.0424 -0.0178 480 SER A C 3708 O O . SER A 480 ? 0.4659 0.5034 0.3986 0.0590 0.0336 -0.0171 480 SER A O 3709 C CB . SER A 480 ? 0.5152 0.4929 0.4275 0.0989 0.0690 -0.0053 480 SER A CB 3710 O OG . SER A 480 ? 0.5132 0.4601 0.4098 0.0847 0.0680 -0.0194 480 SER A OG 3711 N N . ILE A 481 ? 0.4816 0.4456 0.3748 0.0625 0.0420 -0.0287 481 ILE A N 3712 C CA . ILE A 481 ? 0.4663 0.4298 0.3590 0.0434 0.0353 -0.0392 481 ILE A CA 3713 C C . ILE A 481 ? 0.4789 0.4556 0.3663 0.0401 0.0262 -0.0373 481 ILE A C 3714 O O . ILE A 481 ? 0.5013 0.4962 0.3928 0.0246 0.0196 -0.0415 481 ILE A O 3715 C CB . ILE A 481 ? 0.4609 0.3895 0.3385 0.0393 0.0382 -0.0462 481 ILE A CB 3716 C CG1 . ILE A 481 ? 0.4585 0.3744 0.3359 0.0422 0.0447 -0.0468 481 ILE A CG1 3717 C CG2 . ILE A 481 ? 0.4478 0.3737 0.3254 0.0241 0.0366 -0.0536 481 ILE A CG2 3718 C CD1 . ILE A 481 ? 0.4681 0.3594 0.3338 0.0375 0.0443 -0.0504 481 ILE A CD1 3719 N N . ARG A 482 ? 0.5042 0.4672 0.3771 0.0534 0.0269 -0.0311 482 ARG A N 3720 C CA . ARG A 482 ? 0.5272 0.4991 0.3901 0.0537 0.0192 -0.0271 482 ARG A CA 3721 C C . ARG A 482 ? 0.5558 0.5761 0.4348 0.0547 0.0089 -0.0169 482 ARG A C 3722 O O . ARG A 482 ? 0.5786 0.6123 0.4493 0.0428 -0.0019 -0.0184 482 ARG A O 3723 C CB . ARG A 482 ? 0.5582 0.5023 0.4008 0.0704 0.0257 -0.0206 482 ARG A CB 3724 C CG . ARG A 482 ? 0.5636 0.4661 0.3902 0.0642 0.0324 -0.0297 482 ARG A CG 3725 C CD . ARG A 482 ? 0.5950 0.4684 0.3977 0.0754 0.0392 -0.0245 482 ARG A CD 3726 N NE . ARG A 482 ? 0.6367 0.5089 0.4339 0.0965 0.0470 -0.0122 482 ARG A NE 3727 C CZ . ARG A 482 ? 0.6838 0.5172 0.4593 0.1056 0.0607 -0.0105 482 ARG A CZ 3728 N NH1 . ARG A 482 ? 0.7021 0.4987 0.4606 0.0923 0.0646 -0.0206 482 ARG A NH1 3729 N NH2 . ARG A 482 ? 0.7041 0.5353 0.4740 0.1278 0.0719 0.0028 482 ARG A NH2 3730 N N . ASN A 483 ? 0.5867 0.6342 0.4875 0.0682 0.0123 -0.0051 483 ASN A N 3731 C CA . ASN A 483 ? 0.6452 0.7513 0.5706 0.0674 0.0009 0.0078 483 ASN A CA 3732 C C . ASN A 483 ? 0.6044 0.7381 0.5505 0.0424 -0.0047 -0.0007 483 ASN A C 3733 O O . ASN A 483 ? 0.6034 0.7908 0.5741 0.0361 -0.0151 0.0091 483 ASN A O 3734 C CB . ASN A 483 ? 0.7276 0.8613 0.6748 0.0950 0.0091 0.0295 483 ASN A CB 3735 C CG . ASN A 483 ? 0.8361 0.9278 0.7596 0.1225 0.0247 0.0377 483 ASN A CG 3736 O OD1 . ASN A 483 ? 0.8611 0.9131 0.7540 0.1217 0.0254 0.0304 483 ASN A OD1 3737 N ND2 . ASN A 483 ? 0.9968 1.0953 0.9336 0.1473 0.0405 0.0541 483 ASN A ND2 3738 N N . GLY A 484 ? 0.5697 0.6695 0.5075 0.0286 0.0030 -0.0170 484 GLY A N 3739 C CA . GLY A 484 ? 0.5617 0.6763 0.5116 0.0040 0.0017 -0.0265 484 GLY A CA 3740 C C . GLY A 484 ? 0.5550 0.6977 0.5366 0.0088 0.0093 -0.0189 484 GLY A C 3741 O O . GLY A 484 ? 0.5533 0.7243 0.5517 -0.0124 0.0061 -0.0221 484 GLY A O 3742 N N . THR A 485 ? 0.5343 0.6650 0.5210 0.0349 0.0216 -0.0094 485 THR A N 3743 C CA . THR A 485 ? 0.5311 0.6816 0.5447 0.0429 0.0336 -0.0009 485 THR A CA 3744 C C . THR A 485 ? 0.5231 0.6247 0.5210 0.0487 0.0502 -0.0095 485 THR A C 3745 O O . THR A 485 ? 0.5290 0.6346 0.5406 0.0587 0.0636 -0.0027 485 THR A O 3746 C CB . THR A 485 ? 0.5435 0.7246 0.5763 0.0708 0.0383 0.0219 485 THR A CB 3747 O OG1 . THR A 485 ? 0.5489 0.6830 0.5518 0.0940 0.0478 0.0242 485 THR A OG1 3748 C CG2 . THR A 485 ? 0.5415 0.7810 0.5932 0.0653 0.0191 0.0341 485 THR A CG2 3749 N N . TYR A 486 ? 0.5125 0.5706 0.4819 0.0423 0.0491 -0.0229 486 TYR A N 3750 C CA . TYR A 486 ? 0.5011 0.5177 0.4539 0.0457 0.0605 -0.0296 486 TYR A CA 3751 C C . TYR A 486 ? 0.5032 0.5265 0.4697 0.0335 0.0687 -0.0339 486 TYR A C 3752 O O . TYR A 486 ? 0.4916 0.5265 0.4642 0.0129 0.0648 -0.0414 486 TYR A O 3753 C CB . TYR A 486 ? 0.4924 0.4760 0.4211 0.0386 0.0550 -0.0398 486 TYR A CB 3754 C CG . TYR A 486 ? 0.4847 0.4340 0.3979 0.0385 0.0616 -0.0453 486 TYR A CG 3755 C CD1 . TYR A 486 ? 0.4945 0.4152 0.3870 0.0499 0.0640 -0.0431 486 TYR A CD1 3756 C CD2 . TYR A 486 ? 0.4607 0.4042 0.3759 0.0259 0.0652 -0.0518 486 TYR A CD2 3757 C CE1 . TYR A 486 ? 0.4863 0.3819 0.3638 0.0477 0.0658 -0.0464 486 TYR A CE1 3758 C CE2 . TYR A 486 ? 0.4480 0.3656 0.3505 0.0284 0.0700 -0.0531 486 TYR A CE2 3759 C CZ . TYR A 486 ? 0.4716 0.3694 0.3568 0.0387 0.0680 -0.0499 486 TYR A CZ 3760 O OH . TYR A 486 ? 0.4648 0.3434 0.3372 0.0393 0.0690 -0.0493 486 TYR A OH 3761 N N . ASP A 487 ? 0.5063 0.5164 0.4724 0.0453 0.0825 -0.0295 487 ASP A N 3762 C CA . ASP A 487 ? 0.5261 0.5366 0.5022 0.0362 0.0940 -0.0324 487 ASP A CA 3763 C C . ASP A 487 ? 0.5196 0.4842 0.4672 0.0375 0.0996 -0.0397 487 ASP A C 3764 O O . ASP A 487 ? 0.5412 0.4785 0.4694 0.0520 0.1060 -0.0363 487 ASP A O 3765 C CB . ASP A 487 ? 0.5605 0.5881 0.5557 0.0503 0.1082 -0.0200 487 ASP A CB 3766 C CG . ASP A 487 ? 0.5854 0.6151 0.5934 0.0403 0.1227 -0.0220 487 ASP A CG 3767 O OD1 . ASP A 487 ? 0.5960 0.6023 0.5899 0.0264 0.1244 -0.0329 487 ASP A OD1 3768 O OD2 . ASP A 487 ? 0.6024 0.6570 0.6355 0.0480 0.1350 -0.0107 487 ASP A OD2 3769 N N . HIS A 488 ? 0.4926 0.4481 0.4357 0.0224 0.0983 -0.0482 488 HIS A N 3770 C CA . HIS A 488 ? 0.4894 0.4091 0.4095 0.0256 0.1018 -0.0511 488 HIS A CA 3771 C C . HIS A 488 ? 0.5090 0.4098 0.4205 0.0339 0.1161 -0.0476 488 HIS A C 3772 O O . HIS A 488 ? 0.5116 0.3854 0.4003 0.0420 0.1159 -0.0459 488 HIS A O 3773 C CB . HIS A 488 ? 0.4931 0.4061 0.4115 0.0109 0.1035 -0.0579 488 HIS A CB 3774 C CG . HIS A 488 ? 0.5097 0.4205 0.4342 -0.0010 0.1190 -0.0612 488 HIS A CG 3775 N ND1 . HIS A 488 ? 0.5363 0.4189 0.4476 0.0028 0.1333 -0.0602 488 HIS A ND1 3776 C CD2 . HIS A 488 ? 0.5149 0.4503 0.4576 -0.0181 0.1227 -0.0645 488 HIS A CD2 3777 C CE1 . HIS A 488 ? 0.5324 0.4145 0.4503 -0.0110 0.1486 -0.0640 488 HIS A CE1 3778 N NE2 . HIS A 488 ? 0.5241 0.4403 0.4623 -0.0261 0.1412 -0.0673 488 HIS A NE2 3779 N N . ASP A 489 ? 0.5207 0.4368 0.4499 0.0311 0.1282 -0.0455 489 ASP A N 3780 C CA . ASP A 489 ? 0.5848 0.4791 0.5039 0.0391 0.1454 -0.0419 489 ASP A CA 3781 C C . ASP A 489 ? 0.5848 0.4567 0.4807 0.0579 0.1469 -0.0358 489 ASP A C 3782 O O . ASP A 489 ? 0.6244 0.4646 0.4943 0.0653 0.1551 -0.0341 489 ASP A O 3783 C CB . ASP A 489 ? 0.6160 0.5343 0.5631 0.0307 0.1604 -0.0398 489 ASP A CB 3784 C CG . ASP A 489 ? 0.6631 0.5808 0.6163 0.0096 0.1675 -0.0475 489 ASP A CG 3785 O OD1 . ASP A 489 ? 0.7465 0.6291 0.6757 0.0114 0.1745 -0.0502 489 ASP A OD1 3786 O OD2 . ASP A 489 ? 0.6853 0.6366 0.6648 -0.0092 0.1665 -0.0500 489 ASP A OD2 3787 N N . VAL A 490 ? 0.5945 0.4785 0.4945 0.0653 0.1402 -0.0323 490 VAL A N 3788 C CA . VAL A 490 ? 0.6375 0.4906 0.5073 0.0816 0.1452 -0.0275 490 VAL A CA 3789 C C . VAL A 490 ? 0.6362 0.4522 0.4658 0.0804 0.1347 -0.0320 490 VAL A C 3790 O O . VAL A 490 ? 0.6551 0.4345 0.4484 0.0881 0.1413 -0.0302 490 VAL A O 3791 C CB . VAL A 490 ? 0.6454 0.5131 0.5229 0.0902 0.1411 -0.0224 490 VAL A CB 3792 C CG1 . VAL A 490 ? 0.7498 0.5745 0.5881 0.1061 0.1518 -0.0181 490 VAL A CG1 3793 C CG2 . VAL A 490 ? 0.6519 0.5677 0.5741 0.0917 0.1481 -0.0138 490 VAL A CG2 3794 N N . TYR A 491 ? 0.5990 0.4257 0.4345 0.0699 0.1187 -0.0368 491 TYR A N 3795 C CA . TYR A 491 ? 0.5925 0.3981 0.4000 0.0670 0.1049 -0.0383 491 TYR A CA 3796 C C . TYR A 491 ? 0.5855 0.3889 0.3915 0.0632 0.1031 -0.0370 491 TYR A C 3797 O O . TYR A 491 ? 0.6171 0.4100 0.4034 0.0616 0.0914 -0.0345 491 TYR A O 3798 C CB . TYR A 491 ? 0.5637 0.3831 0.3797 0.0608 0.0899 -0.0413 491 TYR A CB 3799 C CG . TYR A 491 ? 0.5888 0.4086 0.4038 0.0670 0.0921 -0.0404 491 TYR A CG 3800 C CD1 . TYR A 491 ? 0.6350 0.4210 0.4141 0.0720 0.0937 -0.0399 491 TYR A CD1 3801 C CD2 . TYR A 491 ? 0.5761 0.4279 0.4223 0.0675 0.0933 -0.0391 491 TYR A CD2 3802 C CE1 . TYR A 491 ? 0.6474 0.4282 0.4227 0.0812 0.1004 -0.0369 491 TYR A CE1 3803 C CE2 . TYR A 491 ? 0.5920 0.4474 0.4388 0.0773 0.0963 -0.0343 491 TYR A CE2 3804 C CZ . TYR A 491 ? 0.6227 0.4411 0.4346 0.0860 0.1016 -0.0326 491 TYR A CZ 3805 O OH . TYR A 491 ? 0.6462 0.4640 0.4568 0.0990 0.1090 -0.0257 491 TYR A OH 3806 N N . ARG A 492 ? 0.5759 0.3895 0.4020 0.0613 0.1156 -0.0371 492 ARG A N 3807 C CA . ARG A 492 ? 0.5779 0.3873 0.4040 0.0601 0.1187 -0.0342 492 ARG A CA 3808 C C . ARG A 492 ? 0.6062 0.3923 0.4014 0.0686 0.1174 -0.0265 492 ARG A C 3809 O O . ARG A 492 ? 0.6092 0.3982 0.4005 0.0699 0.1085 -0.0200 492 ARG A O 3810 C CB . ARG A 492 ? 0.5692 0.3828 0.4137 0.0548 0.1375 -0.0368 492 ARG A CB 3811 C CG . ARG A 492 ? 0.5797 0.3812 0.4212 0.0549 0.1475 -0.0334 492 ARG A CG 3812 C CD . ARG A 492 ? 0.5899 0.3910 0.4456 0.0434 0.1669 -0.0393 492 ARG A CD 3813 N NE . ARG A 492 ? 0.5950 0.3733 0.4414 0.0446 0.1840 -0.0359 492 ARG A NE 3814 C CZ . ARG A 492 ? 0.6022 0.3755 0.4533 0.0341 0.1925 -0.0402 492 ARG A CZ 3815 N NH1 . ARG A 492 ? 0.5979 0.3899 0.4622 0.0202 0.1817 -0.0487 492 ARG A NH1 3816 N NH2 . ARG A 492 ? 0.6310 0.3752 0.4683 0.0389 0.2138 -0.0351 492 ARG A NH2 3817 N N . ASP A 493 ? 0.6448 0.4093 0.4178 0.0751 0.1271 -0.0255 493 ASP A N 3818 C CA . ASP A 493 ? 0.7169 0.4553 0.4519 0.0820 0.1250 -0.0184 493 ASP A CA 3819 C C . ASP A 493 ? 0.6889 0.4289 0.4039 0.0768 0.1002 -0.0161 493 ASP A C 3820 O O . ASP A 493 ? 0.6900 0.4351 0.3966 0.0780 0.0894 -0.0070 493 ASP A O 3821 C CB . ASP A 493 ? 0.7771 0.4849 0.4841 0.0891 0.1408 -0.0188 493 ASP A CB 3822 C CG . ASP A 493 ? 0.8159 0.5189 0.5368 0.0940 0.1665 -0.0173 493 ASP A CG 3823 O OD1 . ASP A 493 ? 0.8082 0.5256 0.5534 0.0905 0.1721 -0.0168 493 ASP A OD1 3824 O OD2 . ASP A 493 ? 0.8586 0.5397 0.5639 0.1008 0.1840 -0.0164 493 ASP A OD2 3825 N N . GLU A 494 ? 0.6778 0.4145 0.3858 0.0710 0.0922 -0.0228 494 GLU A N 3826 C CA . GLU A 494 ? 0.6922 0.4286 0.3808 0.0608 0.0697 -0.0228 494 GLU A CA 3827 C C . GLU A 494 ? 0.6543 0.4266 0.3763 0.0562 0.0565 -0.0175 494 GLU A C 3828 O O . GLU A 494 ? 0.6395 0.4220 0.3531 0.0519 0.0401 -0.0090 494 GLU A O 3829 C CB . GLU A 494 ? 0.7020 0.4264 0.3820 0.0561 0.0695 -0.0312 494 GLU A CB 3830 C CG . GLU A 494 ? 0.7384 0.4553 0.3934 0.0414 0.0491 -0.0333 494 GLU A CG 3831 C CD . GLU A 494 ? 0.7519 0.4502 0.3959 0.0388 0.0541 -0.0411 494 GLU A CD 3832 O OE1 . GLU A 494 ? 0.7772 0.4708 0.4324 0.0512 0.0725 -0.0424 494 GLU A OE1 3833 O OE2 . GLU A 494 ? 0.7532 0.4430 0.3784 0.0245 0.0404 -0.0444 494 GLU A OE2 3834 N N . ALA A 495 ? 0.6011 0.3935 0.3607 0.0571 0.0644 -0.0211 495 ALA A N 3835 C CA . ALA A 495 ? 0.5822 0.4019 0.3707 0.0538 0.0566 -0.0166 495 ALA A CA 3836 C C . ALA A 495 ? 0.5906 0.4193 0.3858 0.0618 0.0596 -0.0034 495 ALA A C 3837 O O . ALA A 495 ? 0.5868 0.4362 0.3916 0.0608 0.0469 0.0071 495 ALA A O 3838 C CB . ALA A 495 ? 0.5497 0.3811 0.3670 0.0516 0.0659 -0.0244 495 ALA A CB 3839 N N . LEU A 496 ? 0.6216 0.4357 0.4129 0.0708 0.0781 -0.0018 496 LEU A N 3840 C CA . LEU A 496 ? 0.6423 0.4582 0.4359 0.0823 0.0863 0.0126 496 LEU A CA 3841 C C . LEU A 496 ? 0.6703 0.4909 0.4409 0.0863 0.0689 0.0267 496 LEU A C 3842 O O . LEU A 496 ? 0.6830 0.5236 0.4654 0.0949 0.0652 0.0438 496 LEU A O 3843 C CB . LEU A 496 ? 0.6705 0.4624 0.4580 0.0892 0.1121 0.0102 496 LEU A CB 3844 C CG . LEU A 496 ? 0.6762 0.4677 0.4875 0.0824 0.1298 -0.0001 496 LEU A CG 3845 C CD1 . LEU A 496 ? 0.6921 0.4597 0.4951 0.0845 0.1546 -0.0030 496 LEU A CD1 3846 C CD2 . LEU A 496 ? 0.6696 0.4711 0.4997 0.0847 0.1347 0.0065 496 LEU A CD2 3847 N N . ASN A 497 ? 0.6866 0.4878 0.4222 0.0807 0.0597 0.0210 497 ASN A N 3848 C CA A ASN A 497 ? 0.7149 0.5180 0.4192 0.0781 0.0386 0.0318 497 ASN A CA 3849 C CA B ASN A 497 ? 0.7203 0.5240 0.4256 0.0786 0.0390 0.0323 497 ASN A CA 3850 C C . ASN A 497 ? 0.6993 0.5388 0.4209 0.0660 0.0130 0.0383 497 ASN A C 3851 O O . ASN A 497 ? 0.7010 0.5676 0.4249 0.0680 -0.0027 0.0566 497 ASN A O 3852 C CB A ASN A 497 ? 0.7554 0.5206 0.4108 0.0703 0.0360 0.0208 497 ASN A CB 3853 C CB B ASN A 497 ? 0.7722 0.5365 0.4268 0.0731 0.0382 0.0229 497 ASN A CB 3854 C CG A ASN A 497 ? 0.8005 0.5636 0.4144 0.0606 0.0109 0.0291 497 ASN A CG 3855 C CG B ASN A 497 ? 0.8096 0.5446 0.4404 0.0878 0.0585 0.0273 497 ASN A CG 3856 O OD1 A ASN A 497 ? 0.8205 0.5799 0.4146 0.0419 -0.0070 0.0219 497 ASN A OD1 3857 O OD1 B ASN A 497 ? 0.8749 0.5921 0.4630 0.0893 0.0506 0.0349 497 ASN A OD1 3858 N ND2 A ASN A 497 ? 0.8347 0.6000 0.4330 0.0718 0.0093 0.0452 497 ASN A ND2 3859 N ND2 B ASN A 497 ? 0.7904 0.5194 0.4464 0.0967 0.0848 0.0228 497 ASN A ND2 3860 N N . ASN A 498 ? 0.6621 0.5049 0.3977 0.0536 0.0093 0.0252 498 ASN A N 3861 C CA . ASN A 498 ? 0.6568 0.5324 0.4114 0.0401 -0.0116 0.0300 498 ASN A CA 3862 C C . ASN A 498 ? 0.6311 0.5457 0.4341 0.0510 -0.0069 0.0460 498 ASN A C 3863 O O . ASN A 498 ? 0.6246 0.5765 0.4446 0.0474 -0.0241 0.0624 498 ASN A O 3864 C CB . ASN A 498 ? 0.6435 0.5060 0.3966 0.0263 -0.0127 0.0126 498 ASN A CB 3865 C CG . ASN A 498 ? 0.6926 0.5173 0.3940 0.0135 -0.0194 0.0011 498 ASN A CG 3866 O OD1 . ASN A 498 ? 0.7509 0.5645 0.4152 0.0078 -0.0313 0.0063 498 ASN A OD1 3867 N ND2 . ASN A 498 ? 0.6728 0.4744 0.3671 0.0096 -0.0106 -0.0131 498 ASN A ND2 3868 N N . ARG A 499 ? 0.6248 0.5302 0.4487 0.0636 0.0175 0.0422 499 ARG A N 3869 C CA . ARG A 499 ? 0.6278 0.5572 0.4896 0.0756 0.0293 0.0565 499 ARG A CA 3870 C C . ARG A 499 ? 0.6881 0.6348 0.5549 0.0931 0.0316 0.0813 499 ARG A C 3871 O O . ARG A 499 ? 0.7004 0.6844 0.5969 0.0990 0.0259 0.1012 499 ARG A O 3872 C CB . ARG A 499 ? 0.6072 0.5125 0.4777 0.0817 0.0569 0.0451 499 ARG A CB 3873 C CG . ARG A 499 ? 0.5675 0.4710 0.4489 0.0691 0.0563 0.0289 499 ARG A CG 3874 C CD . ARG A 499 ? 0.5664 0.4485 0.4520 0.0715 0.0807 0.0187 499 ARG A CD 3875 N NE . ARG A 499 ? 0.5551 0.4398 0.4592 0.0809 0.0984 0.0298 499 ARG A NE 3876 C CZ . ARG A 499 ? 0.5854 0.4446 0.4855 0.0836 0.1240 0.0250 499 ARG A CZ 3877 N NH1 . ARG A 499 ? 0.5977 0.4351 0.4822 0.0760 0.1323 0.0101 499 ARG A NH1 3878 N NH2 . ARG A 499 ? 0.5939 0.4480 0.5046 0.0933 0.1434 0.0362 499 ARG A NH2 3879 N N . PHE A 500 ? 0.7442 0.6646 0.5837 0.1032 0.0421 0.0823 500 PHE A N 3880 C CA . PHE A 500 ? 0.8037 0.7326 0.6445 0.1249 0.0511 0.1069 500 PHE A CA 3881 C C . PHE A 500 ? 0.8771 0.8180 0.6888 0.1238 0.0264 0.1199 500 PHE A C 3882 O O . PHE A 500 ? 0.9401 0.8726 0.7355 0.1417 0.0353 0.1357 500 PHE A O 3883 C CB . PHE A 500 ? 0.8031 0.6909 0.6341 0.1390 0.0864 0.1019 500 PHE A CB 3884 C CG . PHE A 500 ? 0.7977 0.6727 0.6511 0.1363 0.1092 0.0900 500 PHE A CG 3885 C CD1 . PHE A 500 ? 0.7834 0.6826 0.6689 0.1418 0.1131 0.1020 500 PHE A CD1 3886 C CD2 . PHE A 500 ? 0.8114 0.6517 0.6530 0.1269 0.1265 0.0675 500 PHE A CD2 3887 C CE1 . PHE A 500 ? 0.7906 0.6715 0.6877 0.1376 0.1343 0.0902 500 PHE A CE1 3888 C CE2 . PHE A 500 ? 0.7977 0.6268 0.6540 0.1202 0.1440 0.0561 500 PHE A CE2 3889 C CZ . PHE A 500 ? 0.7986 0.6438 0.6785 0.1254 0.1483 0.0665 500 PHE A CZ 3890 N N . GLN A 501 ? 0.9242 0.8827 0.7262 0.1017 -0.0040 0.1138 501 GLN A N 3891 C CA . GLN A 501 ? 1.0005 0.9778 0.7745 0.0941 -0.0334 0.1275 501 GLN A CA 3892 C C . GLN A 501 ? 1.0412 1.0801 0.8539 0.1055 -0.0460 0.1607 501 GLN A C 3893 O O . GLN A 501 ? 1.0292 1.0973 0.8906 0.1114 -0.0371 0.1687 501 GLN A O 3894 C CB . GLN A 501 ? 1.0208 0.9939 0.7698 0.0623 -0.0601 0.1098 501 GLN A CB 3895 C CG . GLN A 501 ? 0.9916 1.0067 0.7817 0.0464 -0.0748 0.1115 501 GLN A CG 3896 C CD . GLN A 501 ? 1.0123 1.0123 0.7708 0.0139 -0.0962 0.0922 501 GLN A CD 3897 O OE1 . GLN A 501 ? 0.9791 0.9547 0.7397 0.0055 -0.0859 0.0717 501 GLN A OE1 3898 N NE2 . GLN A 501 ? 1.0623 1.0740 0.7871 -0.0052 -0.1255 0.0993 501 GLN A NE2 3899 N N . ILE A 502 ? 1.1032 1.1627 0.8936 0.1089 -0.0664 0.1816 502 ILE A N 3900 C CA . ILE A 502 ? 1.1148 1.2456 0.9428 0.1168 -0.0862 0.2173 502 ILE A CA 3901 C C . ILE A 502 ? 1.1274 1.2953 0.9529 0.0799 -0.1271 0.2132 502 ILE A C 3902 O O . ILE A 502 ? 1.1765 1.3215 0.9466 0.0567 -0.1499 0.2007 502 ILE A O 3903 C CB . ILE A 502 ? 1.1676 1.3103 0.9732 0.1393 -0.0909 0.2466 502 ILE A CB 3904 C CG1 . ILE A 502 ? 1.1894 1.2675 0.9646 0.1646 -0.0528 0.2390 502 ILE A CG1 3905 C CG2 . ILE A 502 ? 1.1523 1.3690 1.0145 0.1621 -0.0949 0.2892 502 ILE A CG2 3906 C CD1 . ILE A 502 ? 1.2169 1.2369 0.9231 0.1504 -0.0574 0.2158 502 ILE A CD1 3907 N N . LYS A 503 ? 1.0896 1.3085 0.9706 0.0728 -0.1337 0.2226 503 LYS A N 3908 C CA . LYS A 503 ? 1.0906 1.3477 0.9750 0.0350 -0.1703 0.2197 503 LYS A CA 3909 C C . LYS A 503 ? 1.1160 1.4543 1.0249 0.0334 -0.2028 0.2581 503 LYS A C 3910 O O . LYS A 503 ? 1.1356 1.5056 1.0310 -0.0026 -0.2405 0.2582 503 LYS A O 3911 C CB . LYS A 503 ? 1.0470 1.3170 0.9790 0.0260 -0.1596 0.2096 503 LYS A CB 3912 C CG . LYS A 503 ? 1.0228 1.2212 0.9316 0.0242 -0.1330 0.1732 503 LYS A CG 3913 C CD . LYS A 503 ? 0.9863 1.1978 0.9404 0.0188 -0.1212 0.1666 503 LYS A CD 3914 C CE . LYS A 503 ? 0.9993 1.2375 0.9552 -0.0190 -0.1506 0.1610 503 LYS A CE 3915 N NZ . LYS A 503 ? 0.9487 1.1817 0.9350 -0.0254 -0.1357 0.1483 503 LYS A NZ # 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 LYS 2 2 ? ? ? A . n A 1 3 LEU 3 3 ? ? ? A . n A 1 4 PRO 4 4 ? ? ? A . n A 1 5 GLY 5 5 ? ? ? A . n A 1 6 ASN 6 6 ? ? ? A . n A 1 7 ASP 7 7 ? ? ? A . n A 1 8 ASN 8 8 8 ASN ASN A . n A 1 9 SER 9 9 9 SER SER A . n A 1 10 THR 10 10 10 THR THR A . n A 1 11 ALA 11 11 11 ALA ALA A . n A 1 12 THR 12 12 12 THR THR A . n A 1 13 LEU 13 13 13 LEU LEU A . n A 1 14 CYS 14 14 14 CYS CYS A . n A 1 15 LEU 15 15 15 LEU LEU A . n A 1 16 GLY 16 16 16 GLY GLY A . n A 1 17 HIS 17 17 17 HIS HIS A . n A 1 18 HIS 18 18 18 HIS HIS A . n A 1 19 ALA 19 19 19 ALA ALA A . n A 1 20 VAL 20 20 20 VAL VAL A . n A 1 21 PRO 21 21 21 PRO PRO A . n A 1 22 ASN 22 22 22 ASN ASN A . n A 1 23 GLY 23 23 23 GLY GLY A . n A 1 24 THR 24 24 24 THR THR A . n A 1 25 ILE 25 25 25 ILE ILE A . n A 1 26 VAL 26 26 26 VAL VAL A . n A 1 27 LYS 27 27 27 LYS LYS A . n A 1 28 THR 28 28 28 THR THR A . n A 1 29 ILE 29 29 29 ILE ILE A . n A 1 30 THR 30 30 30 THR THR A . n A 1 31 ASN 31 31 31 ASN ASN A . n A 1 32 ASP 32 32 32 ASP ASP A . n A 1 33 GLN 33 33 33 GLN GLN A . n A 1 34 ILE 34 34 34 ILE ILE A . n A 1 35 GLU 35 35 35 GLU GLU A . n A 1 36 VAL 36 36 36 VAL VAL A . n A 1 37 THR 37 37 37 THR THR A . n A 1 38 ASN 38 38 38 ASN ASN A . n A 1 39 ALA 39 39 39 ALA ALA A . n A 1 40 THR 40 40 40 THR THR A . n A 1 41 GLU 41 41 41 GLU GLU A . n A 1 42 LEU 42 42 42 LEU LEU A . n A 1 43 VAL 43 43 43 VAL VAL A . n A 1 44 GLN 44 44 44 GLN GLN A . n A 1 45 SER 45 45 45 SER SER A . n A 1 46 SER 46 46 46 SER SER A . n A 1 47 SER 47 47 47 SER SER A . n A 1 48 THR 48 48 48 THR THR A . n A 1 49 GLY 49 49 49 GLY GLY A . n A 1 50 GLY 50 50 50 GLY GLY A . n A 1 51 ILE 51 51 51 ILE ILE A . n A 1 52 CYS 52 52 52 CYS CYS A . n A 1 53 ASP 53 53 53 ASP ASP A . n A 1 54 SER 54 54 54 SER SER A . n A 1 55 PRO 55 55 55 PRO PRO A . n A 1 56 HIS 56 56 56 HIS HIS A . n A 1 57 GLN 57 57 57 GLN GLN A . n A 1 58 ILE 58 58 58 ILE ILE A . n A 1 59 LEU 59 59 59 LEU LEU A . n A 1 60 ASP 60 60 60 ASP ASP A . n A 1 61 GLY 61 61 61 GLY GLY A . n A 1 62 GLU 62 62 62 GLU GLU A . n A 1 63 ASN 63 63 63 ASN ASN A . n A 1 64 CYS 64 64 64 CYS CYS A . n A 1 65 THR 65 65 65 THR THR A . n A 1 66 LEU 66 66 66 LEU LEU A . n A 1 67 ILE 67 67 67 ILE ILE A . n A 1 68 ASP 68 68 68 ASP ASP A . n A 1 69 ALA 69 69 69 ALA ALA A . n A 1 70 LEU 70 70 70 LEU LEU A . n A 1 71 LEU 71 71 71 LEU LEU A . n A 1 72 GLY 72 72 72 GLY GLY A . n A 1 73 ASP 73 73 73 ASP ASP A . n A 1 74 PRO 74 74 74 PRO PRO A . n A 1 75 GLN 75 75 75 GLN GLN A . n A 1 76 CYS 76 76 76 CYS CYS A . n A 1 77 ASP 77 77 77 ASP ASP A . n A 1 78 GLY 78 78 78 GLY GLY A . n A 1 79 PHE 79 79 79 PHE PHE A . n A 1 80 GLN 80 80 80 GLN GLN A . n A 1 81 ASN 81 81 81 ASN ASN A . n A 1 82 LYS 82 82 82 LYS LYS A . n A 1 83 LYS 83 83 83 LYS LYS A . n A 1 84 TRP 84 84 84 TRP TRP A . n A 1 85 ASP 85 85 85 ASP ASP A . n A 1 86 LEU 86 86 86 LEU LEU A . n A 1 87 PHE 87 87 87 PHE PHE A . n A 1 88 VAL 88 88 88 VAL VAL A . n A 1 89 GLU 89 89 89 GLU GLU A . n A 1 90 ARG 90 90 90 ARG ARG A . n A 1 91 SER 91 91 91 SER SER A . n A 1 92 LYS 92 92 92 LYS LYS A . n A 1 93 ALA 93 93 93 ALA ALA A . n A 1 94 TYR 94 94 94 TYR TYR A . n A 1 95 SER 95 95 95 SER SER A . n A 1 96 ASN 96 96 96 ASN ASN A . n A 1 97 CYS 97 97 97 CYS CYS A . n A 1 98 TYR 98 98 98 TYR TYR A . n A 1 99 PRO 99 99 99 PRO PRO A . n A 1 100 TYR 100 100 100 TYR TYR A . n A 1 101 ASP 101 101 101 ASP ASP A . n A 1 102 VAL 102 102 102 VAL VAL A . n A 1 103 PRO 103 103 103 PRO PRO A . n A 1 104 ASP 104 104 104 ASP ASP A . n A 1 105 TYR 105 105 105 TYR TYR A . n A 1 106 ALA 106 106 106 ALA ALA A . n A 1 107 SER 107 107 107 SER SER A . n A 1 108 LEU 108 108 108 LEU LEU A . n A 1 109 ARG 109 109 109 ARG ARG A . n A 1 110 SER 110 110 110 SER SER A . n A 1 111 LEU 111 111 111 LEU LEU A . n A 1 112 VAL 112 112 112 VAL VAL A . n A 1 113 ALA 113 113 113 ALA ALA A . n A 1 114 SER 114 114 114 SER SER A . n A 1 115 SER 115 115 115 SER SER A . n A 1 116 GLY 116 116 116 GLY GLY A . n A 1 117 THR 117 117 117 THR THR A . n A 1 118 LEU 118 118 118 LEU LEU A . n A 1 119 GLU 119 119 119 GLU GLU A . n A 1 120 PHE 120 120 120 PHE PHE A . n A 1 121 ASN 121 121 121 ASN ASN A . n A 1 122 ASN 122 122 122 ASN ASN A . n A 1 123 GLU 123 123 123 GLU GLU A . n A 1 124 SER 124 124 124 SER SER A . n A 1 125 PHE 125 125 125 PHE PHE A . n A 1 126 ASN 126 126 126 ASN ASN A . n A 1 127 TRP 127 127 127 TRP TRP A . n A 1 128 THR 128 128 128 THR THR A . n A 1 129 GLY 129 129 129 GLY GLY A . n A 1 130 VAL 130 130 130 VAL VAL A . n A 1 131 THR 131 131 131 THR THR A . n A 1 132 GLN 132 132 132 GLN GLN A . n A 1 133 ASN 133 133 133 ASN ASN A . n A 1 134 GLY 134 134 134 GLY GLY A . n A 1 135 THR 135 135 135 THR THR A . n A 1 136 SER 136 136 136 SER SER A . n A 1 137 SER 137 137 137 SER SER A . n A 1 138 ALA 138 138 138 ALA ALA A . n A 1 139 CYS 139 139 139 CYS CYS A . n A 1 140 LYS 140 140 140 LYS LYS A . n A 1 141 ARG 141 141 141 ARG ARG A . n A 1 142 LYS 142 142 142 LYS LYS A . n A 1 143 SER 143 143 143 SER SER A . n A 1 144 ASN 144 144 144 ASN ASN A . n A 1 145 ASN 145 145 145 ASN ASN A . n A 1 146 SER 146 146 146 SER SER A . n A 1 147 PHE 147 147 147 PHE PHE A . n A 1 148 PHE 148 148 148 PHE PHE A . n A 1 149 SER 149 149 149 SER SER A . n A 1 150 ARG 150 150 150 ARG ARG A . n A 1 151 LEU 151 151 151 LEU LEU A . n A 1 152 ASN 152 152 152 ASN ASN A . n A 1 153 TRP 153 153 153 TRP TRP A . n A 1 154 LEU 154 154 154 LEU LEU A . n A 1 155 THR 155 155 155 THR THR A . n A 1 156 HIS 156 156 156 HIS HIS A . n A 1 157 LEU 157 157 157 LEU LEU A . n A 1 158 LYS 158 158 158 LYS LYS A . n A 1 159 PHE 159 159 159 PHE PHE A . n A 1 160 LYS 160 160 160 LYS LYS A . n A 1 161 TYR 161 161 161 TYR TYR A . n A 1 162 PRO 162 162 162 PRO PRO A . n A 1 163 ALA 163 163 163 ALA ALA A . n A 1 164 LEU 164 164 164 LEU LEU A . n A 1 165 ASN 165 165 165 ASN ASN A . n A 1 166 VAL 166 166 166 VAL VAL A . n A 1 167 THR 167 167 167 THR THR A . n A 1 168 MET 168 168 168 MET MET A . n A 1 169 PRO 169 169 169 PRO PRO A . n A 1 170 ASN 170 170 170 ASN ASN A . n A 1 171 ASN 171 171 171 ASN ASN A . n A 1 172 GLU 172 172 172 GLU GLU A . n A 1 173 LYS 173 173 173 LYS LYS A . n A 1 174 PHE 174 174 174 PHE PHE A . n A 1 175 ASP 175 175 175 ASP ASP A . n A 1 176 LYS 176 176 176 LYS LYS A . n A 1 177 LEU 177 177 177 LEU LEU A . n A 1 178 TYR 178 178 178 TYR TYR A . n A 1 179 ILE 179 179 179 ILE ILE A . n A 1 180 TRP 180 180 180 TRP TRP A . n A 1 181 GLY 181 181 181 GLY GLY A . n A 1 182 VAL 182 182 182 VAL VAL A . n A 1 183 HIS 183 183 183 HIS HIS A . n A 1 184 HIS 184 184 184 HIS HIS A . n A 1 185 PRO 185 185 185 PRO PRO A . n A 1 186 GLY 186 186 186 GLY GLY A . n A 1 187 THR 187 187 187 THR THR A . n A 1 188 ASP 188 188 188 ASP ASP A . n A 1 189 ASN 189 189 189 ASN ASN A . n A 1 190 ASP 190 190 190 ASP ASP A . n A 1 191 GLN 191 191 191 GLN GLN A . n A 1 192 ILE 192 192 192 ILE ILE A . n A 1 193 PHE 193 193 193 PHE PHE A . n A 1 194 LEU 194 194 194 LEU LEU A . n A 1 195 TYR 195 195 195 TYR TYR A . n A 1 196 ALA 196 196 196 ALA ALA A . n A 1 197 GLN 197 197 197 GLN GLN A . n A 1 198 ALA 198 198 198 ALA ALA A . n A 1 199 SER 199 199 199 SER SER A . n A 1 200 GLY 200 200 200 GLY GLY A . n A 1 201 ARG 201 201 201 ARG ARG A . n A 1 202 ILE 202 202 202 ILE ILE A . n A 1 203 THR 203 203 203 THR THR A . n A 1 204 VAL 204 204 204 VAL VAL A . n A 1 205 SER 205 205 205 SER SER A . n A 1 206 THR 206 206 206 THR THR A . n A 1 207 LYS 207 207 207 LYS LYS A . n A 1 208 ARG 208 208 208 ARG ARG A . n A 1 209 SER 209 209 209 SER SER A . n A 1 210 GLN 210 210 210 GLN GLN A . n A 1 211 GLN 211 211 211 GLN GLN A . n A 1 212 THR 212 212 212 THR THR A . n A 1 213 VAL 213 213 213 VAL VAL A . n A 1 214 ILE 214 214 214 ILE ILE A . n A 1 215 PRO 215 215 215 PRO PRO A . n A 1 216 ASN 216 216 216 ASN ASN A . n A 1 217 ILE 217 217 217 ILE ILE A . n A 1 218 GLY 218 218 218 GLY GLY A . n A 1 219 SER 219 219 219 SER SER A . n A 1 220 ARG 220 220 220 ARG ARG A . n A 1 221 PRO 221 221 221 PRO PRO A . n A 1 222 ARG 222 222 222 ARG ARG A . n A 1 223 VAL 223 223 223 VAL VAL A . n A 1 224 ARG 224 224 224 ARG ARG A . n A 1 225 ASN 225 225 225 ASN ASN A . n A 1 226 ILE 226 226 226 ILE ILE A . n A 1 227 PRO 227 227 227 PRO PRO A . n A 1 228 SER 228 228 228 SER SER A . n A 1 229 ARG 229 229 229 ARG ARG A . n A 1 230 ILE 230 230 230 ILE ILE A . n A 1 231 SER 231 231 231 SER SER A . n A 1 232 ILE 232 232 232 ILE ILE A . n A 1 233 TYR 233 233 233 TYR TYR A . n A 1 234 TRP 234 234 234 TRP TRP A . n A 1 235 THR 235 235 235 THR THR A . n A 1 236 ILE 236 236 236 ILE ILE A . n A 1 237 VAL 237 237 237 VAL VAL A . n A 1 238 LYS 238 238 238 LYS LYS A . n A 1 239 PRO 239 239 239 PRO PRO A . n A 1 240 GLY 240 240 240 GLY GLY A . n A 1 241 ASP 241 241 241 ASP ASP A . n A 1 242 ILE 242 242 242 ILE ILE A . n A 1 243 LEU 243 243 243 LEU LEU A . n A 1 244 LEU 244 244 244 LEU LEU A . n A 1 245 ILE 245 245 245 ILE ILE A . n A 1 246 ASN 246 246 246 ASN ASN A . n A 1 247 SER 247 247 247 SER SER A . n A 1 248 THR 248 248 248 THR THR A . n A 1 249 GLY 249 249 249 GLY GLY A . n A 1 250 ASN 250 250 250 ASN ASN A . n A 1 251 LEU 251 251 251 LEU LEU A . n A 1 252 ILE 252 252 252 ILE ILE A . n A 1 253 ALA 253 253 253 ALA ALA A . n A 1 254 PRO 254 254 254 PRO PRO A . n A 1 255 ARG 255 255 255 ARG ARG A . n A 1 256 GLY 256 256 256 GLY GLY A . n A 1 257 TYR 257 257 257 TYR TYR A . n A 1 258 PHE 258 258 258 PHE PHE A . n A 1 259 LYS 259 259 259 LYS LYS A . n A 1 260 ILE 260 260 260 ILE ILE A . n A 1 261 ARG 261 261 261 ARG ARG A . n A 1 262 SER 262 262 262 SER SER A . n A 1 263 GLY 263 263 263 GLY GLY A . n A 1 264 LYS 264 264 264 LYS LYS A . n A 1 265 SER 265 265 265 SER SER A . n A 1 266 SER 266 266 266 SER SER A . n A 1 267 ILE 267 267 267 ILE ILE A . n A 1 268 MET 268 268 268 MET MET A . n A 1 269 ARG 269 269 269 ARG ARG A . n A 1 270 SER 270 270 270 SER SER A . n A 1 271 ASP 271 271 271 ASP ASP A . n A 1 272 ALA 272 272 272 ALA ALA A . n A 1 273 PRO 273 273 273 PRO PRO A . n A 1 274 ILE 274 274 274 ILE ILE A . n A 1 275 GLY 275 275 275 GLY GLY A . n A 1 276 LYS 276 276 276 LYS LYS A . n A 1 277 CYS 277 277 277 CYS CYS A . n A 1 278 ASN 278 278 278 ASN ASN A . n A 1 279 SER 279 279 279 SER SER A . n A 1 280 GLU 280 280 280 GLU GLU A . n A 1 281 CYS 281 281 281 CYS CYS A . n A 1 282 ILE 282 282 282 ILE ILE A . n A 1 283 THR 283 283 283 THR THR A . n A 1 284 PRO 284 284 284 PRO PRO A . n A 1 285 ASN 285 285 285 ASN ASN A . n A 1 286 GLY 286 286 286 GLY GLY A . n A 1 287 SER 287 287 287 SER SER A . n A 1 288 ILE 288 288 288 ILE ILE A . n A 1 289 PRO 289 289 289 PRO PRO A . n A 1 290 ASN 290 290 290 ASN ASN A . n A 1 291 ASP 291 291 291 ASP ASP A . n A 1 292 LYS 292 292 292 LYS LYS A . n A 1 293 PRO 293 293 293 PRO PRO A . n A 1 294 PHE 294 294 294 PHE PHE A . n A 1 295 GLN 295 295 295 GLN GLN A . n A 1 296 ASN 296 296 296 ASN ASN A . n A 1 297 VAL 297 297 297 VAL VAL A . n A 1 298 ASN 298 298 298 ASN ASN A . n A 1 299 ARG 299 299 299 ARG ARG A . n A 1 300 ILE 300 300 300 ILE ILE A . n A 1 301 THR 301 301 301 THR THR A . n A 1 302 TYR 302 302 302 TYR TYR A . n A 1 303 GLY 303 303 303 GLY GLY A . n A 1 304 ALA 304 304 304 ALA ALA A . n A 1 305 CYS 305 305 305 CYS CYS A . n A 1 306 PRO 306 306 306 PRO PRO A . n A 1 307 ARG 307 307 307 ARG ARG A . n A 1 308 TYR 308 308 308 TYR TYR A . n A 1 309 VAL 309 309 309 VAL VAL A . n A 1 310 LYS 310 310 310 LYS LYS A . n A 1 311 GLN 311 311 311 GLN GLN A . n A 1 312 ASN 312 312 312 ASN ASN A . n A 1 313 THR 313 313 313 THR THR A . n A 1 314 LEU 314 314 314 LEU LEU A . n A 1 315 LYS 315 315 315 LYS LYS A . n A 1 316 LEU 316 316 316 LEU LEU A . n A 1 317 ALA 317 317 317 ALA ALA A . n A 1 318 THR 318 318 318 THR THR A . n A 1 319 GLY 319 319 319 GLY GLY A . n A 1 320 MET 320 320 320 MET MET 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 VAL 323 323 323 VAL VAL A . n A 1 324 PRO 324 324 324 PRO PRO A . n A 1 325 GLU 325 325 325 GLU GLU A . n A 1 326 LYS 326 326 326 LYS LYS A . n A 1 327 GLN 327 327 327 GLN GLN A . n A 1 328 THR 328 328 ? ? ? A . n A 1 329 GLN 329 329 ? ? ? A . n A 1 330 GLY 330 330 ? ? ? A . n A 1 331 ILE 331 331 ? ? ? A . n A 1 332 PHE 332 332 ? ? ? A . n A 1 333 GLY 333 333 ? ? ? A . n A 1 334 ALA 334 334 334 ALA ALA A . n A 1 335 ILE 335 335 335 ILE ILE A . n A 1 336 ALA 336 336 336 ALA ALA A . n A 1 337 GLY 337 337 337 GLY GLY A . n A 1 338 PHE 338 338 338 PHE PHE A . n A 1 339 ILE 339 339 339 ILE ILE A . n A 1 340 GLU 340 340 340 GLU GLU A . n A 1 341 ASN 341 341 341 ASN ASN A . n A 1 342 GLY 342 342 342 GLY GLY A . n A 1 343 TRP 343 343 343 TRP TRP A . n A 1 344 GLU 344 344 344 GLU GLU A . n A 1 345 GLY 345 345 345 GLY GLY A . n A 1 346 MET 346 346 346 MET MET A . n A 1 347 VAL 347 347 347 VAL VAL A . n A 1 348 ASP 348 348 348 ASP ASP A . n A 1 349 GLY 349 349 349 GLY GLY A . n A 1 350 TRP 350 350 350 TRP TRP A . n A 1 351 TYR 351 351 351 TYR TYR A . n A 1 352 GLY 352 352 352 GLY GLY A . n A 1 353 PHE 353 353 353 PHE PHE A . n A 1 354 ARG 354 354 354 ARG ARG A . n A 1 355 HIS 355 355 355 HIS HIS A . n A 1 356 GLN 356 356 356 GLN GLN A . n A 1 357 ASN 357 357 357 ASN ASN A . n A 1 358 SER 358 358 358 SER SER A . n A 1 359 GLU 359 359 359 GLU GLU A . n A 1 360 GLY 360 360 360 GLY GLY A . n A 1 361 ILE 361 361 361 ILE ILE A . n A 1 362 GLY 362 362 362 GLY GLY A . n A 1 363 GLN 363 363 363 GLN GLN A . n A 1 364 ALA 364 364 364 ALA ALA 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 LEU 367 367 367 LEU LEU A . n A 1 368 LYS 368 368 368 LYS LYS A . n A 1 369 SER 369 369 369 SER SER A . n A 1 370 THR 370 370 370 THR THR A . n A 1 371 GLN 371 371 371 GLN GLN A . n A 1 372 ALA 372 372 372 ALA ALA A . n A 1 373 ALA 373 373 373 ALA ALA A . n A 1 374 ILE 374 374 374 ILE ILE A . n A 1 375 ASN 375 375 375 ASN ASN A . n A 1 376 GLN 376 376 376 GLN GLN A . n A 1 377 ILE 377 377 377 ILE ILE A . n A 1 378 ASN 378 378 378 ASN ASN A . n A 1 379 GLY 379 379 379 GLY GLY A . n A 1 380 LYS 380 380 380 LYS LYS A . n A 1 381 LEU 381 381 381 LEU LEU A . n A 1 382 ASN 382 382 382 ASN ASN A . n A 1 383 ARG 383 383 383 ARG ARG A . n A 1 384 LEU 384 384 384 LEU LEU A . n A 1 385 ILE 385 385 385 ILE ILE A . n A 1 386 GLY 386 386 386 GLY GLY A . n A 1 387 LYS 387 387 387 LYS LYS A . n A 1 388 THR 388 388 388 THR THR A . n A 1 389 ASN 389 389 389 ASN ASN A . n A 1 390 GLU 390 390 390 GLU GLU A . n A 1 391 LYS 391 391 391 LYS LYS A . n A 1 392 PHE 392 392 392 PHE PHE A . n A 1 393 HIS 393 393 393 HIS HIS A . n A 1 394 GLN 394 394 394 GLN GLN A . n A 1 395 ILE 395 395 395 ILE ILE A . n A 1 396 GLU 396 396 396 GLU GLU A . n A 1 397 LYS 397 397 397 LYS LYS A . n A 1 398 GLU 398 398 398 GLU GLU A . n A 1 399 PHE 399 399 399 PHE PHE A . n A 1 400 SER 400 400 400 SER SER A . n A 1 401 GLU 401 401 401 GLU GLU A . n A 1 402 VAL 402 402 402 VAL VAL A . n A 1 403 GLU 403 403 403 GLU GLU A . n A 1 404 GLY 404 404 404 GLY GLY A . n A 1 405 ARG 405 405 405 ARG ARG A . n A 1 406 ILE 406 406 406 ILE ILE A . n A 1 407 GLN 407 407 407 GLN GLN A . n A 1 408 ASP 408 408 408 ASP ASP A . n A 1 409 LEU 409 409 409 LEU LEU A . n A 1 410 GLU 410 410 410 GLU GLU A . n A 1 411 LYS 411 411 411 LYS LYS A . n A 1 412 TYR 412 412 412 TYR TYR A . n A 1 413 VAL 413 413 413 VAL VAL A . n A 1 414 GLU 414 414 414 GLU GLU A . n A 1 415 ASP 415 415 415 ASP ASP A . n A 1 416 THR 416 416 416 THR THR A . n A 1 417 LYS 417 417 417 LYS LYS A . n A 1 418 ILE 418 418 418 ILE ILE A . n A 1 419 ASP 419 419 419 ASP ASP A . n A 1 420 LEU 420 420 420 LEU LEU A . n A 1 421 TRP 421 421 421 TRP TRP A . n A 1 422 SER 422 422 422 SER SER A . n A 1 423 TYR 423 423 423 TYR TYR A . n A 1 424 ASN 424 424 424 ASN ASN A . n A 1 425 ALA 425 425 425 ALA ALA A . n A 1 426 GLU 426 426 426 GLU GLU A . n A 1 427 LEU 427 427 427 LEU LEU A . n A 1 428 LEU 428 428 428 LEU LEU A . n A 1 429 VAL 429 429 429 VAL VAL A . n A 1 430 ALA 430 430 430 ALA ALA A . n A 1 431 LEU 431 431 431 LEU LEU A . n A 1 432 GLU 432 432 432 GLU GLU A . n A 1 433 ASN 433 433 433 ASN ASN A . n A 1 434 GLN 434 434 434 GLN GLN A . n A 1 435 HIS 435 435 435 HIS HIS A . n A 1 436 THR 436 436 436 THR THR A . n A 1 437 ILE 437 437 437 ILE ILE A . n A 1 438 ASP 438 438 438 ASP ASP A . n A 1 439 LEU 439 439 439 LEU LEU A . n A 1 440 THR 440 440 440 THR THR A . n A 1 441 ASP 441 441 441 ASP ASP A . n A 1 442 SER 442 442 442 SER SER A . n A 1 443 GLU 443 443 443 GLU GLU A . n A 1 444 MET 444 444 444 MET MET A . n A 1 445 ASN 445 445 445 ASN ASN A . n A 1 446 LYS 446 446 446 LYS LYS A . n A 1 447 LEU 447 447 447 LEU LEU A . n A 1 448 PHE 448 448 448 PHE PHE A . n A 1 449 GLU 449 449 449 GLU GLU A . n A 1 450 ARG 450 450 450 ARG ARG A . n A 1 451 THR 451 451 451 THR THR A . n A 1 452 LYS 452 452 452 LYS LYS A . n A 1 453 LYS 453 453 453 LYS LYS A . n A 1 454 GLN 454 454 454 GLN GLN A . n A 1 455 LEU 455 455 455 LEU LEU A . n A 1 456 ARG 456 456 456 ARG ARG A . n A 1 457 GLU 457 457 457 GLU GLU A . n A 1 458 ASN 458 458 458 ASN ASN A . n A 1 459 ALA 459 459 459 ALA ALA A . n A 1 460 GLU 460 460 460 GLU GLU A . n A 1 461 ASP 461 461 461 ASP ASP A . n A 1 462 MET 462 462 462 MET MET A . n A 1 463 GLY 463 463 463 GLY GLY A . n A 1 464 ASN 464 464 464 ASN ASN A . n A 1 465 GLY 465 465 465 GLY GLY A . n A 1 466 CYS 466 466 466 CYS CYS A . n A 1 467 PHE 467 467 467 PHE PHE A . n A 1 468 LYS 468 468 468 LYS LYS A . n A 1 469 ILE 469 469 469 ILE ILE A . n A 1 470 TYR 470 470 470 TYR TYR A . n A 1 471 HIS 471 471 471 HIS HIS A . n A 1 472 LYS 472 472 472 LYS LYS A . n A 1 473 CYS 473 473 473 CYS CYS A . n A 1 474 ASP 474 474 474 ASP ASP A . n A 1 475 ASN 475 475 475 ASN ASN A . n A 1 476 ALA 476 476 476 ALA ALA A . n A 1 477 CYS 477 477 477 CYS CYS A . n A 1 478 ILE 478 478 478 ILE ILE A . n A 1 479 GLY 479 479 479 GLY GLY A . n A 1 480 SER 480 480 480 SER SER A . n A 1 481 ILE 481 481 481 ILE ILE A . n A 1 482 ARG 482 482 482 ARG ARG A . n A 1 483 ASN 483 483 483 ASN ASN A . n A 1 484 GLY 484 484 484 GLY GLY A . n A 1 485 THR 485 485 485 THR THR A . n A 1 486 TYR 486 486 486 TYR TYR A . n A 1 487 ASP 487 487 487 ASP ASP A . n A 1 488 HIS 488 488 488 HIS HIS A . n A 1 489 ASP 489 489 489 ASP ASP A . n A 1 490 VAL 490 490 490 VAL VAL A . n A 1 491 TYR 491 491 491 TYR TYR A . n A 1 492 ARG 492 492 492 ARG ARG A . n A 1 493 ASP 493 493 493 ASP ASP A . n A 1 494 GLU 494 494 494 GLU GLU A . n A 1 495 ALA 495 495 495 ALA ALA A . n A 1 496 LEU 496 496 496 LEU LEU A . n A 1 497 ASN 497 497 497 ASN ASN A . n A 1 498 ASN 498 498 498 ASN ASN A . n A 1 499 ARG 499 499 499 ARG ARG A . n A 1 500 PHE 500 500 500 PHE PHE A . n A 1 501 GLN 501 501 501 GLN GLN A . n A 1 502 ILE 502 502 502 ILE ILE A . n A 1 503 LYS 503 503 503 LYS LYS 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 NAG 1 801 801 NAG NAG A . C 2 NAG 1 802 802 NAG NAG A . D 2 NAG 1 804 804 NAG NAG A . E 2 NAG 1 805 805 NAG NAG A . F 2 NAG 2 806 806 NAG NAG A . G 3 MAN 3 807 807 MAN MAN A . H 2 NAG 1 808 808 NAG NAG A . I 2 NAG 2 809 809 NAG NAG A . J 2 NAG 1 811 811 NAG NAG A . K 2 NAG 1 812 812 NAG NAG A . L 2 NAG 1 813 813 NAG NAG A . M 4 EPE 1 1504 1504 EPE EPE A . N 4 EPE 1 1505 1505 EPE EPE A . O 5 TAM 1 1506 1506 TAM TAM A . P 6 HOH 1 2001 2001 HOH HOH A . P 6 HOH 2 2002 2002 HOH HOH A . P 6 HOH 3 2003 2003 HOH HOH A . P 6 HOH 4 2004 2004 HOH HOH A . P 6 HOH 5 2005 2005 HOH HOH A . P 6 HOH 6 2006 2006 HOH HOH A . P 6 HOH 7 2007 2007 HOH HOH A . P 6 HOH 8 2008 2008 HOH HOH A . P 6 HOH 9 2009 2009 HOH HOH A . P 6 HOH 10 2010 2010 HOH HOH A . P 6 HOH 11 2011 2011 HOH HOH A . P 6 HOH 12 2012 2012 HOH HOH A . P 6 HOH 13 2013 2013 HOH HOH A . P 6 HOH 14 2014 2014 HOH HOH A . P 6 HOH 15 2015 2015 HOH HOH A . P 6 HOH 16 2016 2016 HOH HOH A . P 6 HOH 17 2017 2017 HOH HOH A . P 6 HOH 18 2018 2018 HOH HOH A . P 6 HOH 19 2019 2019 HOH HOH A . P 6 HOH 20 2020 2020 HOH HOH A . P 6 HOH 21 2021 2021 HOH HOH A . P 6 HOH 22 2022 2022 HOH HOH A . P 6 HOH 23 2023 2023 HOH HOH A . P 6 HOH 24 2024 2024 HOH HOH A . P 6 HOH 25 2025 2025 HOH HOH A . P 6 HOH 26 2026 2026 HOH HOH A . P 6 HOH 27 2027 2027 HOH HOH A . P 6 HOH 28 2028 2028 HOH HOH A . P 6 HOH 29 2029 2029 HOH HOH A . P 6 HOH 30 2030 2030 HOH HOH A . P 6 HOH 31 2031 2031 HOH HOH A . P 6 HOH 32 2032 2032 HOH HOH A . P 6 HOH 33 2033 2033 HOH HOH A . P 6 HOH 34 2034 2034 HOH HOH A . P 6 HOH 35 2035 2035 HOH HOH A . P 6 HOH 36 2036 2036 HOH HOH A . P 6 HOH 37 2037 2037 HOH HOH A . P 6 HOH 38 2038 2038 HOH HOH A . P 6 HOH 39 2039 2039 HOH HOH A . P 6 HOH 40 2040 2040 HOH HOH A . P 6 HOH 41 2041 2041 HOH HOH A . P 6 HOH 42 2042 2042 HOH HOH A . P 6 HOH 43 2043 2043 HOH HOH A . P 6 HOH 44 2044 2044 HOH HOH A . P 6 HOH 45 2045 2045 HOH HOH A . P 6 HOH 46 2046 2046 HOH HOH A . P 6 HOH 47 2047 2047 HOH HOH A . P 6 HOH 48 2048 2048 HOH HOH A . P 6 HOH 49 2049 2049 HOH HOH A . P 6 HOH 50 2050 2050 HOH HOH A . P 6 HOH 51 2051 2051 HOH HOH A . P 6 HOH 52 2052 2052 HOH HOH A . P 6 HOH 53 2053 2053 HOH HOH A . P 6 HOH 54 2054 2054 HOH HOH A . P 6 HOH 55 2055 2055 HOH HOH A . P 6 HOH 56 2056 2056 HOH HOH A . P 6 HOH 57 2057 2057 HOH HOH A . P 6 HOH 58 2058 2058 HOH HOH A . P 6 HOH 59 2059 2059 HOH HOH A . P 6 HOH 60 2060 2060 HOH HOH A . P 6 HOH 61 2061 2061 HOH HOH A . P 6 HOH 62 2062 2062 HOH HOH A . P 6 HOH 63 2063 2063 HOH HOH A . P 6 HOH 64 2064 2064 HOH HOH A . P 6 HOH 65 2065 2065 HOH HOH A . P 6 HOH 66 2066 2066 HOH HOH A . P 6 HOH 67 2067 2067 HOH HOH A . P 6 HOH 68 2068 2068 HOH HOH A . P 6 HOH 69 2069 2069 HOH HOH A . P 6 HOH 70 2070 2070 HOH HOH A . P 6 HOH 71 2071 2071 HOH HOH A . P 6 HOH 72 2072 2072 HOH HOH A . P 6 HOH 73 2073 2073 HOH HOH A . P 6 HOH 74 2074 2074 HOH HOH A . P 6 HOH 75 2075 2075 HOH HOH A . P 6 HOH 76 2076 2076 HOH HOH A . P 6 HOH 77 2077 2077 HOH HOH A . P 6 HOH 78 2078 2078 HOH HOH A . P 6 HOH 79 2079 2079 HOH HOH A . P 6 HOH 80 2080 2080 HOH HOH A . P 6 HOH 81 2081 2081 HOH HOH A . P 6 HOH 82 2082 2082 HOH HOH A . P 6 HOH 83 2083 2083 HOH HOH A . P 6 HOH 84 2084 2084 HOH HOH A . P 6 HOH 85 2085 2085 HOH HOH A . P 6 HOH 86 2086 2086 HOH HOH A . P 6 HOH 87 2087 2087 HOH HOH A . P 6 HOH 88 2088 2088 HOH HOH A . P 6 HOH 89 2089 2089 HOH HOH A . P 6 HOH 90 2090 2090 HOH HOH A . P 6 HOH 91 2091 2091 HOH HOH A . P 6 HOH 92 2092 2092 HOH HOH A . P 6 HOH 93 2093 2093 HOH HOH A . P 6 HOH 94 2094 2094 HOH HOH A . P 6 HOH 95 2095 2095 HOH HOH A . P 6 HOH 96 2096 2096 HOH HOH A . P 6 HOH 97 2097 2097 HOH HOH A . P 6 HOH 98 2098 2098 HOH HOH A . P 6 HOH 99 2099 2099 HOH HOH A . P 6 HOH 100 2100 2100 HOH HOH A . P 6 HOH 101 2101 2101 HOH HOH A . P 6 HOH 102 2102 2102 HOH HOH A . P 6 HOH 103 2103 2103 HOH HOH A . P 6 HOH 104 2104 2104 HOH HOH A . P 6 HOH 105 2105 2105 HOH HOH A . P 6 HOH 106 2106 2106 HOH HOH A . P 6 HOH 107 2107 2107 HOH HOH A . P 6 HOH 108 2108 2108 HOH HOH A . P 6 HOH 109 2109 2109 HOH HOH A . P 6 HOH 110 2110 2110 HOH HOH A . P 6 HOH 111 2111 2111 HOH HOH A . P 6 HOH 112 2112 2112 HOH HOH A . P 6 HOH 113 2113 2113 HOH HOH A . P 6 HOH 114 2114 2114 HOH HOH A . P 6 HOH 115 2115 2115 HOH HOH A . P 6 HOH 116 2116 2116 HOH HOH A . P 6 HOH 117 2117 2117 HOH HOH A . P 6 HOH 118 2118 2118 HOH HOH A . P 6 HOH 119 2119 2119 HOH HOH A . P 6 HOH 120 2120 2120 HOH HOH A . P 6 HOH 121 2121 2121 HOH HOH A . P 6 HOH 122 2122 2122 HOH HOH A . P 6 HOH 123 2123 2123 HOH HOH A . P 6 HOH 124 2124 2124 HOH HOH A . P 6 HOH 125 2125 2125 HOH HOH A . P 6 HOH 126 2126 2126 HOH HOH A . P 6 HOH 127 2127 2127 HOH HOH A . P 6 HOH 128 2128 2128 HOH HOH A . P 6 HOH 129 2129 2129 HOH HOH A . P 6 HOH 130 2130 2130 HOH HOH A . P 6 HOH 131 2131 2131 HOH HOH A . P 6 HOH 132 2132 2132 HOH HOH A . P 6 HOH 133 2133 2133 HOH HOH A . P 6 HOH 134 2134 2134 HOH HOH A . P 6 HOH 135 2135 2135 HOH HOH A . P 6 HOH 136 2136 2136 HOH HOH A . P 6 HOH 137 2137 2137 HOH HOH A . P 6 HOH 138 2138 2138 HOH HOH A . P 6 HOH 139 2139 2139 HOH HOH A . P 6 HOH 140 2140 2140 HOH HOH A . P 6 HOH 141 2141 2141 HOH HOH A . P 6 HOH 142 2142 2142 HOH HOH A . P 6 HOH 143 2143 2143 HOH HOH A . P 6 HOH 144 2144 2144 HOH HOH A . P 6 HOH 145 2145 2145 HOH HOH A . P 6 HOH 146 2146 2146 HOH HOH A . P 6 HOH 147 2147 2147 HOH HOH A . P 6 HOH 148 2148 2148 HOH HOH A . P 6 HOH 149 2149 2149 HOH HOH A . P 6 HOH 150 2150 2150 HOH HOH A . P 6 HOH 151 2151 2151 HOH HOH A . P 6 HOH 152 2152 2152 HOH HOH A . P 6 HOH 153 2153 2153 HOH HOH A . P 6 HOH 154 2154 2154 HOH HOH A . P 6 HOH 155 2155 2155 HOH HOH A . P 6 HOH 156 2156 2156 HOH HOH A . P 6 HOH 157 2157 2157 HOH HOH A . P 6 HOH 158 2158 2158 HOH HOH A . P 6 HOH 159 2159 2159 HOH HOH A . P 6 HOH 160 2160 2160 HOH HOH A . P 6 HOH 161 2161 2161 HOH HOH A . P 6 HOH 162 2162 2162 HOH HOH A . P 6 HOH 163 2163 2163 HOH HOH A . P 6 HOH 164 2164 2164 HOH HOH A . P 6 HOH 165 2165 2165 HOH HOH A . P 6 HOH 166 2166 2166 HOH HOH A . P 6 HOH 167 2167 2167 HOH HOH A . P 6 HOH 168 2168 2168 HOH HOH A . P 6 HOH 169 2169 2169 HOH HOH A . P 6 HOH 170 2170 2170 HOH HOH A . P 6 HOH 171 2171 2171 HOH HOH A . P 6 HOH 172 2172 2172 HOH HOH A . P 6 HOH 173 2173 2173 HOH HOH A . P 6 HOH 174 2174 2174 HOH HOH A . P 6 HOH 175 2175 2175 HOH HOH A . P 6 HOH 176 2176 2176 HOH HOH A . P 6 HOH 177 2177 2177 HOH HOH A . P 6 HOH 178 2178 2178 HOH HOH A . P 6 HOH 179 2179 2179 HOH HOH A . P 6 HOH 180 2180 2180 HOH HOH A . P 6 HOH 181 2181 2181 HOH HOH A . P 6 HOH 182 2182 2182 HOH HOH A . P 6 HOH 183 2183 2183 HOH HOH A . P 6 HOH 184 2184 2184 HOH HOH A . P 6 HOH 185 2185 2185 HOH HOH A . P 6 HOH 186 2186 2186 HOH HOH A . P 6 HOH 187 2187 2187 HOH HOH A . P 6 HOH 188 2188 2188 HOH HOH A . P 6 HOH 189 2189 2189 HOH HOH A . P 6 HOH 190 2190 2190 HOH HOH A . P 6 HOH 191 2191 2191 HOH HOH A . P 6 HOH 192 2192 2192 HOH HOH A . P 6 HOH 193 2193 2193 HOH HOH A . P 6 HOH 194 2194 2194 HOH HOH A . P 6 HOH 195 2195 2195 HOH HOH A . P 6 HOH 196 2196 2196 HOH HOH A . P 6 HOH 197 2197 2197 HOH HOH A . P 6 HOH 198 2198 2198 HOH HOH A . P 6 HOH 199 2199 2199 HOH HOH A . P 6 HOH 200 2200 2200 HOH HOH A . P 6 HOH 201 2201 2201 HOH HOH A . P 6 HOH 202 2202 2202 HOH HOH A . P 6 HOH 203 2203 2203 HOH HOH A . P 6 HOH 204 2204 2204 HOH HOH A . P 6 HOH 205 2205 2205 HOH HOH A . P 6 HOH 206 2206 2206 HOH HOH A . P 6 HOH 207 2207 2207 HOH HOH A . P 6 HOH 208 2208 2208 HOH HOH A . P 6 HOH 209 2209 2209 HOH HOH A . P 6 HOH 210 2210 2210 HOH HOH A . P 6 HOH 211 2211 2211 HOH HOH A . P 6 HOH 212 2212 2212 HOH HOH A . P 6 HOH 213 2213 2213 HOH HOH A . P 6 HOH 214 2214 2214 HOH HOH A . P 6 HOH 215 2215 2215 HOH HOH A . P 6 HOH 216 2216 2216 HOH HOH A . P 6 HOH 217 2217 2217 HOH HOH A . P 6 HOH 218 2218 2218 HOH HOH A . P 6 HOH 219 2219 2219 HOH HOH A . P 6 HOH 220 2220 2220 HOH HOH A . P 6 HOH 221 2221 2221 HOH HOH A . P 6 HOH 222 2222 2222 HOH HOH A . P 6 HOH 223 2223 2223 HOH HOH A . P 6 HOH 224 2224 2224 HOH HOH A . P 6 HOH 225 2225 2225 HOH HOH A . P 6 HOH 226 2226 2226 HOH HOH A . P 6 HOH 227 2227 2227 HOH HOH A . P 6 HOH 228 2228 2228 HOH HOH A . P 6 HOH 229 2229 2229 HOH HOH A . P 6 HOH 230 2230 2230 HOH HOH A . P 6 HOH 231 2231 2231 HOH HOH A . P 6 HOH 232 2232 2232 HOH HOH A . P 6 HOH 233 2233 2233 HOH HOH A . P 6 HOH 234 2234 2234 HOH HOH A . P 6 HOH 235 2235 2235 HOH HOH A . P 6 HOH 236 2236 2236 HOH HOH A . P 6 HOH 237 2237 2237 HOH HOH A . P 6 HOH 238 2238 2238 HOH HOH A . P 6 HOH 239 2239 2239 HOH HOH A . P 6 HOH 240 2240 2240 HOH HOH A . P 6 HOH 241 2241 2241 HOH HOH A . P 6 HOH 242 2242 2242 HOH HOH A . P 6 HOH 243 2243 2243 HOH HOH A . P 6 HOH 244 2244 2244 HOH HOH A . P 6 HOH 245 2245 2245 HOH HOH A . P 6 HOH 246 2246 2246 HOH HOH A . P 6 HOH 247 2247 2247 HOH HOH A . P 6 HOH 248 2248 2248 HOH HOH A . P 6 HOH 249 2249 2249 HOH HOH A . P 6 HOH 250 2250 2250 HOH HOH A . P 6 HOH 251 2251 2251 HOH HOH A . P 6 HOH 252 2252 2252 HOH HOH A . P 6 HOH 253 2253 2253 HOH HOH A . P 6 HOH 254 2254 2254 HOH HOH A . P 6 HOH 255 2255 2255 HOH HOH A . P 6 HOH 256 2256 2256 HOH HOH A . P 6 HOH 257 2257 2257 HOH HOH A . P 6 HOH 258 2258 2258 HOH HOH A . P 6 HOH 259 2259 2259 HOH HOH A . P 6 HOH 260 2260 2260 HOH HOH A . P 6 HOH 261 2261 2261 HOH HOH A . P 6 HOH 262 2262 2262 HOH HOH A . P 6 HOH 263 2263 2263 HOH HOH A . P 6 HOH 264 2264 2264 HOH HOH A . P 6 HOH 265 2265 2265 HOH HOH A . P 6 HOH 266 2266 2266 HOH HOH A . P 6 HOH 267 2267 2267 HOH HOH A . P 6 HOH 268 2268 2268 HOH HOH A . P 6 HOH 269 2269 2269 HOH HOH A . P 6 HOH 270 2270 2270 HOH HOH A . P 6 HOH 271 2271 2271 HOH HOH A . P 6 HOH 272 2272 2272 HOH HOH A . P 6 HOH 273 2273 2273 HOH HOH A . P 6 HOH 274 2274 2274 HOH HOH A . P 6 HOH 275 2275 2275 HOH HOH A . P 6 HOH 276 2276 2276 HOH HOH A . P 6 HOH 277 2277 2277 HOH HOH A . P 6 HOH 278 2278 2278 HOH HOH A . P 6 HOH 279 2279 2279 HOH HOH A . P 6 HOH 280 2280 2280 HOH HOH A . P 6 HOH 281 2281 2281 HOH HOH A . P 6 HOH 282 2282 2282 HOH HOH A . P 6 HOH 283 2283 2283 HOH HOH A . P 6 HOH 284 2284 2284 HOH HOH A . P 6 HOH 285 2285 2285 HOH HOH A . P 6 HOH 286 2286 2286 HOH HOH A . P 6 HOH 287 2287 2287 HOH HOH A . P 6 HOH 288 2288 2288 HOH HOH A . P 6 HOH 289 2289 2289 HOH HOH A . P 6 HOH 290 2290 2290 HOH HOH A . P 6 HOH 291 2291 2291 HOH HOH A . P 6 HOH 292 2292 2292 HOH HOH A . P 6 HOH 293 2293 2293 HOH HOH A . P 6 HOH 294 2294 2294 HOH HOH A . P 6 HOH 295 2295 2295 HOH HOH A . P 6 HOH 296 2296 2296 HOH HOH A . P 6 HOH 297 2297 2297 HOH HOH A . P 6 HOH 298 2298 2298 HOH HOH A . P 6 HOH 299 2299 2299 HOH HOH A . P 6 HOH 300 2300 2300 HOH HOH A . P 6 HOH 301 2301 2301 HOH HOH A . P 6 HOH 302 2302 2302 HOH HOH A . P 6 HOH 303 2303 2303 HOH HOH A . P 6 HOH 304 2304 2304 HOH HOH A . P 6 HOH 305 2305 2305 HOH HOH A . P 6 HOH 306 2306 2306 HOH HOH A . P 6 HOH 307 2307 2307 HOH HOH A . P 6 HOH 308 2308 2308 HOH HOH A . P 6 HOH 309 2309 2309 HOH HOH A . P 6 HOH 310 2310 2310 HOH HOH A . P 6 HOH 311 2311 2311 HOH HOH A . P 6 HOH 312 2312 2312 HOH HOH A . P 6 HOH 313 2313 2313 HOH HOH A . P 6 HOH 314 2314 2314 HOH HOH A . P 6 HOH 315 2315 2315 HOH HOH A . P 6 HOH 316 2316 2316 HOH HOH A . P 6 HOH 317 2317 2317 HOH HOH A . P 6 HOH 318 2318 2318 HOH HOH A . P 6 HOH 319 2319 2319 HOH HOH A . P 6 HOH 320 2320 2320 HOH HOH A . P 6 HOH 321 2321 2321 HOH HOH A . P 6 HOH 322 2322 2322 HOH HOH A . P 6 HOH 323 2323 2323 HOH HOH A . P 6 HOH 324 2324 2324 HOH HOH A . P 6 HOH 325 2325 2325 HOH HOH A . P 6 HOH 326 2326 2326 HOH HOH A . P 6 HOH 327 2327 2327 HOH HOH A . P 6 HOH 328 2328 2328 HOH HOH A . P 6 HOH 329 2329 2329 HOH HOH A . P 6 HOH 330 2330 2330 HOH HOH A . P 6 HOH 331 2331 2331 HOH HOH A . P 6 HOH 332 2332 2332 HOH HOH A . P 6 HOH 333 2333 2333 HOH HOH A . P 6 HOH 334 2334 2334 HOH HOH A . P 6 HOH 335 2335 2335 HOH HOH A . P 6 HOH 336 2336 2336 HOH HOH A . P 6 HOH 337 2337 2337 HOH HOH A . P 6 HOH 338 2338 2338 HOH HOH A . P 6 HOH 339 2339 2339 HOH HOH A . P 6 HOH 340 2340 2340 HOH HOH A . P 6 HOH 341 2341 2341 HOH HOH A . P 6 HOH 342 2342 2342 HOH HOH A . P 6 HOH 343 2343 2343 HOH HOH A . P 6 HOH 344 2344 2344 HOH HOH A . P 6 HOH 345 2345 2345 HOH HOH A . P 6 HOH 346 2346 2346 HOH HOH A . P 6 HOH 347 2347 2347 HOH HOH A . P 6 HOH 348 2348 2348 HOH HOH A . P 6 HOH 349 2349 2349 HOH HOH A . P 6 HOH 350 2350 2350 HOH HOH A . P 6 HOH 351 2351 2351 HOH HOH A . P 6 HOH 352 2352 2352 HOH HOH A . P 6 HOH 353 2353 2353 HOH HOH A . P 6 HOH 354 2354 2354 HOH HOH A . P 6 HOH 355 2355 2355 HOH HOH A . P 6 HOH 356 2356 2356 HOH HOH A . P 6 HOH 357 2357 2357 HOH HOH A . P 6 HOH 358 2358 2358 HOH HOH A . P 6 HOH 359 2359 2359 HOH HOH A . P 6 HOH 360 2360 2360 HOH HOH A . P 6 HOH 361 2361 2361 HOH HOH A . P 6 HOH 362 2362 2362 HOH HOH A . P 6 HOH 363 2363 2363 HOH HOH A . P 6 HOH 364 2364 2364 HOH HOH A . P 6 HOH 365 2365 2365 HOH HOH A . P 6 HOH 366 2366 2366 HOH HOH A . P 6 HOH 367 2367 2367 HOH HOH A . P 6 HOH 368 2368 2368 HOH HOH A . P 6 HOH 369 2369 2369 HOH HOH A . P 6 HOH 370 2370 2370 HOH HOH A . P 6 HOH 371 2371 2371 HOH HOH A . P 6 HOH 372 2372 2372 HOH HOH A . P 6 HOH 373 2373 2373 HOH HOH A . P 6 HOH 374 2374 2374 HOH HOH A . P 6 HOH 375 2375 2375 HOH HOH A . P 6 HOH 376 2376 2376 HOH HOH A . P 6 HOH 377 2377 2377 HOH HOH A . P 6 HOH 378 2378 2378 HOH HOH A . P 6 HOH 379 2379 2379 HOH HOH A . P 6 HOH 380 2380 2380 HOH HOH A . P 6 HOH 381 2381 2381 HOH HOH A . P 6 HOH 382 2382 2382 HOH HOH A . P 6 HOH 383 2383 2383 HOH HOH A . P 6 HOH 384 2384 2384 HOH HOH A . P 6 HOH 385 2385 2385 HOH HOH A . P 6 HOH 386 2386 2386 HOH HOH A . P 6 HOH 387 2387 2387 HOH HOH A . P 6 HOH 388 2388 2388 HOH HOH A . P 6 HOH 389 2389 2389 HOH HOH A . P 6 HOH 390 2390 2390 HOH HOH A . P 6 HOH 391 2391 2391 HOH HOH A . P 6 HOH 392 2392 2392 HOH HOH A . P 6 HOH 393 2393 2393 HOH HOH A . P 6 HOH 394 2394 2394 HOH HOH A . P 6 HOH 395 2395 2395 HOH HOH A . P 6 HOH 396 2396 2396 HOH HOH A . P 6 HOH 397 2397 2397 HOH HOH A . P 6 HOH 398 2398 2398 HOH HOH A . P 6 HOH 399 2399 2399 HOH HOH A . P 6 HOH 400 2400 2400 HOH HOH A . P 6 HOH 401 2401 2401 HOH HOH A . P 6 HOH 402 2402 2402 HOH HOH A . P 6 HOH 403 2403 2403 HOH HOH A . P 6 HOH 404 2404 2404 HOH HOH A . P 6 HOH 405 2405 2405 HOH HOH A . P 6 HOH 406 2406 2406 HOH HOH A . P 6 HOH 407 2407 2407 HOH HOH A . P 6 HOH 408 2408 2408 HOH HOH A . P 6 HOH 409 2409 2409 HOH HOH A . P 6 HOH 410 2410 2410 HOH HOH A . P 6 HOH 411 2411 2411 HOH HOH A . P 6 HOH 412 2412 2412 HOH HOH A . P 6 HOH 413 2413 2413 HOH HOH A . P 6 HOH 414 2414 2414 HOH HOH A . P 6 HOH 415 2415 2415 HOH HOH A . P 6 HOH 416 2416 2416 HOH HOH A . P 6 HOH 417 2417 2417 HOH HOH A . P 6 HOH 418 2418 2418 HOH HOH A . P 6 HOH 419 2419 2419 HOH HOH A . P 6 HOH 420 2420 2420 HOH HOH A . P 6 HOH 421 2421 2421 HOH HOH A . P 6 HOH 422 2422 2422 HOH HOH A . P 6 HOH 423 2423 2423 HOH HOH A . P 6 HOH 424 2424 2424 HOH HOH A . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 38 A ASN 38 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 63 A ASN 63 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 126 A ASN 126 ? ASN 'GLYCOSYLATION SITE' 4 A ASN 133 A ASN 133 ? ASN 'GLYCOSYLATION SITE' 5 A ASN 165 A ASN 165 ? ASN 'GLYCOSYLATION SITE' 6 A ASN 246 A ASN 246 ? ASN 'GLYCOSYLATION SITE' 7 A ASN 285 A ASN 285 ? ASN 'GLYCOSYLATION SITE' 8 A ASN 483 A ASN 483 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details trimeric _pdbx_struct_assembly.oligomeric_count 3 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1,2,3 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 1 'ABSA (A^2)' 26100 ? 1 MORE 142.2 ? 1 'SSA (A^2)' 61150 ? # loop_ _pdbx_struct_oper_list.id _pdbx_struct_oper_list.type _pdbx_struct_oper_list.name _pdbx_struct_oper_list.symmetry_operation _pdbx_struct_oper_list.matrix[1][1] _pdbx_struct_oper_list.matrix[1][2] _pdbx_struct_oper_list.matrix[1][3] _pdbx_struct_oper_list.vector[1] _pdbx_struct_oper_list.matrix[2][1] _pdbx_struct_oper_list.matrix[2][2] _pdbx_struct_oper_list.matrix[2][3] _pdbx_struct_oper_list.vector[2] _pdbx_struct_oper_list.matrix[3][1] _pdbx_struct_oper_list.matrix[3][2] _pdbx_struct_oper_list.matrix[3][3] _pdbx_struct_oper_list.vector[3] 1 'identity operation' 1_555 x,y,z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 2 'crystal symmetry operation' 2_565 -y,x-y+1,z -0.5000000000 -0.8660254038 0.0000000000 -50.4450000000 0.8660254038 -0.5000000000 0.0000000000 87.3733029878 0.0000000000 0.0000000000 1.0000000000 0.0000000000 3 'crystal symmetry operation' 3_455 -x+y-1,-x,z -0.5000000000 0.8660254038 0.0000000000 -100.8900000000 -0.8660254038 -0.5000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 # loop_ _pdbx_struct_special_symmetry.id _pdbx_struct_special_symmetry.PDB_model_num _pdbx_struct_special_symmetry.auth_asym_id _pdbx_struct_special_symmetry.auth_comp_id _pdbx_struct_special_symmetry.auth_seq_id _pdbx_struct_special_symmetry.PDB_ins_code _pdbx_struct_special_symmetry.label_asym_id _pdbx_struct_special_symmetry.label_comp_id _pdbx_struct_special_symmetry.label_seq_id 1 1 A HOH 2161 ? P HOH . 2 1 A HOH 2163 ? P HOH . # 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 2012-11-07 2 'Structure model' 1 1 2012-12-26 3 'Structure model' 1 2 2013-01-16 # _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' 'Database references' 2 2 'Structure model' 'Refinement description' 3 2 'Structure model' 'Structure summary' 4 3 'Structure model' 'Database references' # loop_ _pdbx_refine_tls.pdbx_refine_id _pdbx_refine_tls.id _pdbx_refine_tls.details _pdbx_refine_tls.method _pdbx_refine_tls.origin_x _pdbx_refine_tls.origin_y _pdbx_refine_tls.origin_z _pdbx_refine_tls.T[1][1] _pdbx_refine_tls.T[2][2] _pdbx_refine_tls.T[3][3] _pdbx_refine_tls.T[1][2] _pdbx_refine_tls.T[1][3] _pdbx_refine_tls.T[2][3] _pdbx_refine_tls.L[1][1] _pdbx_refine_tls.L[2][2] _pdbx_refine_tls.L[3][3] _pdbx_refine_tls.L[1][2] _pdbx_refine_tls.L[1][3] _pdbx_refine_tls.L[2][3] _pdbx_refine_tls.S[1][1] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[2][2] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] _pdbx_refine_tls.S[3][3] 'X-RAY DIFFRACTION' 1 ? refined -43.9861 7.8670 68.5532 0.0856 0.0997 0.1523 0.0161 -0.0538 0.0568 0.1236 0.1609 1.3618 -0.0315 -0.0322 -0.3046 0.0116 -0.0874 -0.1183 -0.0015 0.0827 0.0209 0.0692 -0.0125 -0.0943 'X-RAY DIFFRACTION' 2 ? refined -39.6074 17.5043 90.9465 0.1840 0.2654 0.0805 0.0950 -0.0997 -0.0583 0.8555 0.1969 0.7102 0.1677 0.5514 0.1205 0.0251 -0.1777 -0.0802 0.1673 0.1083 -0.1009 0.0126 0.0252 -0.1334 'X-RAY DIFFRACTION' 3 ? refined -49.7732 13.9485 38.2756 0.0994 0.0953 0.1407 -0.0189 -0.0553 -0.0133 0.0907 0.2057 0.8754 0.0882 0.1870 0.0403 0.0261 0.0383 -0.0694 -0.0296 0.1059 -0.0128 0.0195 0.0682 -0.1320 'X-RAY DIFFRACTION' 4 ? refined -45.9863 17.7073 -4.8471 0.1954 0.0712 0.0721 0.0294 0.0582 -0.0466 1.4738 3.7839 4.6444 0.3683 -2.3381 -1.7325 0.2084 0.0419 0.1538 -0.2098 -0.0037 0.0112 0.0399 0.0280 -0.2047 # loop_ _pdbx_refine_tls_group.pdbx_refine_id _pdbx_refine_tls_group.id _pdbx_refine_tls_group.refine_tls_id _pdbx_refine_tls_group.beg_auth_asym_id _pdbx_refine_tls_group.beg_auth_seq_id _pdbx_refine_tls_group.beg_label_asym_id _pdbx_refine_tls_group.beg_label_seq_id _pdbx_refine_tls_group.end_auth_asym_id _pdbx_refine_tls_group.end_auth_seq_id _pdbx_refine_tls_group.end_label_asym_id _pdbx_refine_tls_group.end_label_seq_id _pdbx_refine_tls_group.selection _pdbx_refine_tls_group.selection_details 'X-RAY DIFFRACTION' 1 1 A 8 ? ? A 164 ? ? ? ? 'X-RAY DIFFRACTION' 2 2 A 165 ? ? A 262 ? ? ? ? 'X-RAY DIFFRACTION' 3 3 A 263 ? ? A 448 ? ? ? ? 'X-RAY DIFFRACTION' 4 4 A 449 ? ? A 503 ? ? ? ? # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal REFMAC refinement 5.6.0117 ? 1 MOSFLM 'data reduction' . ? 2 SCALA 'data scaling' . ? 3 PHASER phasing . ? 4 # _pdbx_entry_details.entry_id 2YP7 _pdbx_entry_details.compound_details ? _pdbx_entry_details.source_details ? _pdbx_entry_details.nonpolymer_details ? _pdbx_entry_details.sequence_details ;THE GLOBAL INITIATIVE ON SHARING ALL INFLUENZA DATA ( GISAID) ACCESSION NUMBER PROVIDED EPI347408 ; # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 OE1 A GLU 398 ? ? O A HOH 2337 ? ? 2.13 2 1 OD2 A ASP 68 ? ? O A HOH 2074 ? ? 2.15 # loop_ _pdbx_validate_rmsd_angle.id _pdbx_validate_rmsd_angle.PDB_model_num _pdbx_validate_rmsd_angle.auth_atom_id_1 _pdbx_validate_rmsd_angle.auth_asym_id_1 _pdbx_validate_rmsd_angle.auth_comp_id_1 _pdbx_validate_rmsd_angle.auth_seq_id_1 _pdbx_validate_rmsd_angle.PDB_ins_code_1 _pdbx_validate_rmsd_angle.label_alt_id_1 _pdbx_validate_rmsd_angle.auth_atom_id_2 _pdbx_validate_rmsd_angle.auth_asym_id_2 _pdbx_validate_rmsd_angle.auth_comp_id_2 _pdbx_validate_rmsd_angle.auth_seq_id_2 _pdbx_validate_rmsd_angle.PDB_ins_code_2 _pdbx_validate_rmsd_angle.label_alt_id_2 _pdbx_validate_rmsd_angle.auth_atom_id_3 _pdbx_validate_rmsd_angle.auth_asym_id_3 _pdbx_validate_rmsd_angle.auth_comp_id_3 _pdbx_validate_rmsd_angle.auth_seq_id_3 _pdbx_validate_rmsd_angle.PDB_ins_code_3 _pdbx_validate_rmsd_angle.label_alt_id_3 _pdbx_validate_rmsd_angle.angle_value _pdbx_validate_rmsd_angle.angle_target_value _pdbx_validate_rmsd_angle.angle_deviation _pdbx_validate_rmsd_angle.angle_standard_deviation _pdbx_validate_rmsd_angle.linker_flag 1 1 CB A ASP 104 ? ? CG A ASP 104 ? ? OD1 A ASP 104 ? ? 124.33 118.30 6.03 0.90 N 2 1 NE A ARG 299 ? ? CZ A ARG 299 ? ? NH1 A ARG 299 ? ? 123.37 120.30 3.07 0.50 N # 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 22 ? ? -116.28 68.95 2 1 GLU A 62 ? ? 52.61 -117.06 3 1 CYS A 97 ? ? -139.64 -154.14 4 1 TRP A 127 ? ? -96.21 45.04 5 1 SER A 143 ? ? 75.86 -11.40 6 1 SER A 146 ? ? -153.72 -159.49 7 1 ASN A 341 ? ? -162.51 119.66 8 1 PHE A 392 ? ? -123.47 -113.28 9 1 GLN A 394 ? ? -128.12 -128.01 10 1 ARG A 456 ? ? 54.57 -123.20 11 1 TYR A 470 ? ? -92.25 36.14 # 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 LYS 2 ? A LYS 2 3 1 Y 1 A LEU 3 ? A LEU 3 4 1 Y 1 A PRO 4 ? A PRO 4 5 1 Y 1 A GLY 5 ? A GLY 5 6 1 Y 1 A ASN 6 ? A ASN 6 7 1 Y 1 A ASP 7 ? A ASP 7 8 1 Y 1 A THR 328 ? A THR 328 9 1 Y 1 A GLN 329 ? A GLN 329 10 1 Y 1 A GLY 330 ? A GLY 330 11 1 Y 1 A ILE 331 ? A ILE 331 12 1 Y 1 A PHE 332 ? A PHE 332 13 1 Y 1 A GLY 333 ? A GLY 333 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 ALPHA-D-MANNOSE MAN 4 '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' EPE 5 'TRIS(HYDROXYETHYL)AMINOMETHANE' TAM 6 water HOH #