data_1WPX # _entry.id 1WPX # _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 1WPX RCSB RCSB023865 WWPDB D_1000023865 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 1BD9 . unspecified PDB 1BEH . unspecified PDB 1A44 . unspecified PDB 1QOU . unspecified PDB 1FJJ . unspecified PDB 1FUX . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 1WPX _pdbx_database_status.recvd_initial_deposition_date 2004-09-14 _pdbx_database_status.deposit_site PDBJ _pdbx_database_status.process_site PDBJ _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_cs ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Mima, J.' 1 'Hayashida, M.' 2 'Fujii, T.' 3 'Narita, Y.' 4 'Hayashi, R.' 5 'Ueda, M.' 6 'Hata, Y.' 7 # _citation.id primary _citation.title ;Structure of the carboxypeptidase y inhibitor i(c) in complex with the cognate proteinase reveals a novel mode of the proteinase-protein inhibitor interaction ; _citation.journal_abbrev J.Mol.Biol. _citation.journal_volume 346 _citation.page_first 1323 _citation.page_last 1334 _citation.year 2005 _citation.journal_id_ASTM JMOBAK _citation.country UK _citation.journal_id_ISSN 0022-2836 _citation.journal_id_CSD 0070 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 15713484 _citation.pdbx_database_id_DOI 10.1016/j.jmb.2004.12.051 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Mima, J.' 1 primary 'Hayashida, M.' 2 primary 'Fujii, T.' 3 primary 'Narita, Y.' 4 primary 'Hayashi, R.' 5 primary 'Ueda, M.' 6 primary 'Hata, Y.' 7 # _cell.entry_id 1WPX _cell.length_a 81.129 _cell.length_b 186.590 _cell.length_c 65.140 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 4 _cell.pdbx_unique_axis ? # _symmetry.entry_id 1WPX _symmetry.space_group_name_H-M 'P 21 21 21' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 19 _symmetry.space_group_name_Hall ? # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer nat 'Carboxypeptidase Y' 47355.363 1 3.4.16.5 ? ? ? 2 polymer nat 'Carboxypeptidase Y inhibitor' 24411.309 1 ? ? ? ? 3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 1 ? ? ? ? 4 non-polymer man '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' 221.208 2 ? ? ? ? 5 non-polymer syn 'SULFATE ION' 96.063 2 ? ? ? ? 6 water nat water 18.015 51 ? ? ? ? # loop_ _entity_name_com.entity_id _entity_name_com.name 1 'Carboxypeptidase YSCY' 2 'CPY inhibitor, Ic, IC, DKA1 protein, NSP1 protein, TFS1 protein' # loop_ _entity_poly.entity_id _entity_poly.type _entity_poly.nstd_linkage _entity_poly.nstd_monomer _entity_poly.pdbx_seq_one_letter_code _entity_poly.pdbx_seq_one_letter_code_can _entity_poly.pdbx_strand_id _entity_poly.pdbx_target_identifier 1 'polypeptide(L)' no no ;KIKDPKILGIDPNVTQYTGYLDVEDEDKHFFFWTFESRNDPAKDPVILWLNGGPGCSSLTGLFFELGPSSIGPDLKPIGN PYSWNSNATVIFLDQPVNVGFSYSGSSGVSNTVAAGKDVYNFLELFFDQFPEYVNKGQDFHIAGESYAGHYIPVFASEIL SHKDRNFNLTSVLIGNGLTDPLTQYNYYEPMACGEGGEPSVLPSEECSAMEDSLERCLGLIESCYDSQSVWSCVPATIYC NNAQLAPYQRTGRNVYDIRKDCEGGNLCYPTLQDIDDYLNQDYVKEAVGAEVDHYESCNFDINRNFLFAGDWMKPYHTAV TDLLNQDLPILVYAGDKDFICNWLGNKAWTDVLPWKYDEEFASQKVRNWTASITDEVAGEVKSYKHFTYLRVFNGGHMVP FDVPENALSMVNEWIHGGFSL ; ;KIKDPKILGIDPNVTQYTGYLDVEDEDKHFFFWTFESRNDPAKDPVILWLNGGPGCSSLTGLFFELGPSSIGPDLKPIGN PYSWNSNATVIFLDQPVNVGFSYSGSSGVSNTVAAGKDVYNFLELFFDQFPEYVNKGQDFHIAGESYAGHYIPVFASEIL SHKDRNFNLTSVLIGNGLTDPLTQYNYYEPMACGEGGEPSVLPSEECSAMEDSLERCLGLIESCYDSQSVWSCVPATIYC NNAQLAPYQRTGRNVYDIRKDCEGGNLCYPTLQDIDDYLNQDYVKEAVGAEVDHYESCNFDINRNFLFAGDWMKPYHTAV TDLLNQDLPILVYAGDKDFICNWLGNKAWTDVLPWKYDEEFASQKVRNWTASITDEVAGEVKSYKHFTYLRVFNGGHMVP FDVPENALSMVNEWIHGGFSL ; A ? 2 'polypeptide(L)' no yes ;(ACE)MNQAIDFAQASIDSYKKHGILEDVIHDTSFQPSGILAVEYSSSAPVAMGNTLPTEKARSKPQFQFTFNKQMQKSV PQANAYVPQDDDLFTLVMTDPDAPSKTDHKWSEFCHLVECDLKLLNEATHETSGATEFFASEFNTKGSNTLIEYMGPAPP KGSGPHRYVFLLYKQPKGVDSSKFSKIKDRPNWGYGTPATGVGKWAKENNLQLVASNFFYAETK ; ;XMNQAIDFAQASIDSYKKHGILEDVIHDTSFQPSGILAVEYSSSAPVAMGNTLPTEKARSKPQFQFTFNKQMQKSVPQAN AYVPQDDDLFTLVMTDPDAPSKTDHKWSEFCHLVECDLKLLNEATHETSGATEFFASEFNTKGSNTLIEYMGPAPPKGSG PHRYVFLLYKQPKGVDSSKFSKIKDRPNWGYGTPATGVGKWAKENNLQLVASNFFYAETK ; B ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 LYS n 1 2 ILE n 1 3 LYS n 1 4 ASP n 1 5 PRO n 1 6 LYS n 1 7 ILE n 1 8 LEU n 1 9 GLY n 1 10 ILE n 1 11 ASP n 1 12 PRO n 1 13 ASN n 1 14 VAL n 1 15 THR n 1 16 GLN n 1 17 TYR n 1 18 THR n 1 19 GLY n 1 20 TYR n 1 21 LEU n 1 22 ASP n 1 23 VAL n 1 24 GLU n 1 25 ASP n 1 26 GLU n 1 27 ASP n 1 28 LYS n 1 29 HIS n 1 30 PHE n 1 31 PHE n 1 32 PHE n 1 33 TRP n 1 34 THR n 1 35 PHE n 1 36 GLU n 1 37 SER n 1 38 ARG n 1 39 ASN n 1 40 ASP n 1 41 PRO n 1 42 ALA n 1 43 LYS n 1 44 ASP n 1 45 PRO n 1 46 VAL n 1 47 ILE n 1 48 LEU n 1 49 TRP n 1 50 LEU n 1 51 ASN n 1 52 GLY n 1 53 GLY n 1 54 PRO n 1 55 GLY n 1 56 CYS n 1 57 SER n 1 58 SER n 1 59 LEU n 1 60 THR n 1 61 GLY n 1 62 LEU n 1 63 PHE n 1 64 PHE n 1 65 GLU n 1 66 LEU n 1 67 GLY n 1 68 PRO n 1 69 SER n 1 70 SER n 1 71 ILE n 1 72 GLY n 1 73 PRO n 1 74 ASP n 1 75 LEU n 1 76 LYS n 1 77 PRO n 1 78 ILE n 1 79 GLY n 1 80 ASN n 1 81 PRO n 1 82 TYR n 1 83 SER n 1 84 TRP n 1 85 ASN n 1 86 SER n 1 87 ASN n 1 88 ALA n 1 89 THR n 1 90 VAL n 1 91 ILE n 1 92 PHE n 1 93 LEU n 1 94 ASP n 1 95 GLN n 1 96 PRO n 1 97 VAL n 1 98 ASN n 1 99 VAL n 1 100 GLY n 1 101 PHE n 1 102 SER n 1 103 TYR n 1 104 SER n 1 105 GLY n 1 106 SER n 1 107 SER n 1 108 GLY n 1 109 VAL n 1 110 SER n 1 111 ASN n 1 112 THR n 1 113 VAL n 1 114 ALA n 1 115 ALA n 1 116 GLY n 1 117 LYS n 1 118 ASP n 1 119 VAL n 1 120 TYR n 1 121 ASN n 1 122 PHE n 1 123 LEU n 1 124 GLU n 1 125 LEU n 1 126 PHE n 1 127 PHE n 1 128 ASP n 1 129 GLN n 1 130 PHE n 1 131 PRO n 1 132 GLU n 1 133 TYR n 1 134 VAL n 1 135 ASN n 1 136 LYS n 1 137 GLY n 1 138 GLN n 1 139 ASP n 1 140 PHE n 1 141 HIS n 1 142 ILE n 1 143 ALA n 1 144 GLY n 1 145 GLU n 1 146 SER n 1 147 TYR n 1 148 ALA n 1 149 GLY n 1 150 HIS n 1 151 TYR n 1 152 ILE n 1 153 PRO n 1 154 VAL n 1 155 PHE n 1 156 ALA n 1 157 SER n 1 158 GLU n 1 159 ILE n 1 160 LEU n 1 161 SER n 1 162 HIS n 1 163 LYS n 1 164 ASP n 1 165 ARG n 1 166 ASN n 1 167 PHE n 1 168 ASN n 1 169 LEU n 1 170 THR n 1 171 SER n 1 172 VAL n 1 173 LEU n 1 174 ILE n 1 175 GLY n 1 176 ASN n 1 177 GLY n 1 178 LEU n 1 179 THR n 1 180 ASP n 1 181 PRO n 1 182 LEU n 1 183 THR n 1 184 GLN n 1 185 TYR n 1 186 ASN n 1 187 TYR n 1 188 TYR n 1 189 GLU n 1 190 PRO n 1 191 MET n 1 192 ALA n 1 193 CYS n 1 194 GLY n 1 195 GLU n 1 196 GLY n 1 197 GLY n 1 198 GLU n 1 199 PRO n 1 200 SER n 1 201 VAL n 1 202 LEU n 1 203 PRO n 1 204 SER n 1 205 GLU n 1 206 GLU n 1 207 CYS n 1 208 SER n 1 209 ALA n 1 210 MET n 1 211 GLU n 1 212 ASP n 1 213 SER n 1 214 LEU n 1 215 GLU n 1 216 ARG n 1 217 CYS n 1 218 LEU n 1 219 GLY n 1 220 LEU n 1 221 ILE n 1 222 GLU n 1 223 SER n 1 224 CYS n 1 225 TYR n 1 226 ASP n 1 227 SER n 1 228 GLN n 1 229 SER n 1 230 VAL n 1 231 TRP n 1 232 SER n 1 233 CYS n 1 234 VAL n 1 235 PRO n 1 236 ALA n 1 237 THR n 1 238 ILE n 1 239 TYR n 1 240 CYS n 1 241 ASN n 1 242 ASN n 1 243 ALA n 1 244 GLN n 1 245 LEU n 1 246 ALA n 1 247 PRO n 1 248 TYR n 1 249 GLN n 1 250 ARG n 1 251 THR n 1 252 GLY n 1 253 ARG n 1 254 ASN n 1 255 VAL n 1 256 TYR n 1 257 ASP n 1 258 ILE n 1 259 ARG n 1 260 LYS n 1 261 ASP n 1 262 CYS n 1 263 GLU n 1 264 GLY n 1 265 GLY n 1 266 ASN n 1 267 LEU n 1 268 CYS n 1 269 TYR n 1 270 PRO n 1 271 THR n 1 272 LEU n 1 273 GLN n 1 274 ASP n 1 275 ILE n 1 276 ASP n 1 277 ASP n 1 278 TYR n 1 279 LEU n 1 280 ASN n 1 281 GLN n 1 282 ASP n 1 283 TYR n 1 284 VAL n 1 285 LYS n 1 286 GLU n 1 287 ALA n 1 288 VAL n 1 289 GLY n 1 290 ALA n 1 291 GLU n 1 292 VAL n 1 293 ASP n 1 294 HIS n 1 295 TYR n 1 296 GLU n 1 297 SER n 1 298 CYS n 1 299 ASN n 1 300 PHE n 1 301 ASP n 1 302 ILE n 1 303 ASN n 1 304 ARG n 1 305 ASN n 1 306 PHE n 1 307 LEU n 1 308 PHE n 1 309 ALA n 1 310 GLY n 1 311 ASP n 1 312 TRP n 1 313 MET n 1 314 LYS n 1 315 PRO n 1 316 TYR n 1 317 HIS n 1 318 THR n 1 319 ALA n 1 320 VAL n 1 321 THR n 1 322 ASP n 1 323 LEU n 1 324 LEU n 1 325 ASN n 1 326 GLN n 1 327 ASP n 1 328 LEU n 1 329 PRO n 1 330 ILE n 1 331 LEU n 1 332 VAL n 1 333 TYR n 1 334 ALA n 1 335 GLY n 1 336 ASP n 1 337 LYS n 1 338 ASP n 1 339 PHE n 1 340 ILE n 1 341 CYS n 1 342 ASN n 1 343 TRP n 1 344 LEU n 1 345 GLY n 1 346 ASN n 1 347 LYS n 1 348 ALA n 1 349 TRP n 1 350 THR n 1 351 ASP n 1 352 VAL n 1 353 LEU n 1 354 PRO n 1 355 TRP n 1 356 LYS n 1 357 TYR n 1 358 ASP n 1 359 GLU n 1 360 GLU n 1 361 PHE n 1 362 ALA n 1 363 SER n 1 364 GLN n 1 365 LYS n 1 366 VAL n 1 367 ARG n 1 368 ASN n 1 369 TRP n 1 370 THR n 1 371 ALA n 1 372 SER n 1 373 ILE n 1 374 THR n 1 375 ASP n 1 376 GLU n 1 377 VAL n 1 378 ALA n 1 379 GLY n 1 380 GLU n 1 381 VAL n 1 382 LYS n 1 383 SER n 1 384 TYR n 1 385 LYS n 1 386 HIS n 1 387 PHE n 1 388 THR n 1 389 TYR n 1 390 LEU n 1 391 ARG n 1 392 VAL n 1 393 PHE n 1 394 ASN n 1 395 GLY n 1 396 GLY n 1 397 HIS n 1 398 MET n 1 399 VAL n 1 400 PRO n 1 401 PHE n 1 402 ASP n 1 403 VAL n 1 404 PRO n 1 405 GLU n 1 406 ASN n 1 407 ALA n 1 408 LEU n 1 409 SER n 1 410 MET n 1 411 VAL n 1 412 ASN n 1 413 GLU n 1 414 TRP n 1 415 ILE n 1 416 HIS n 1 417 GLY n 1 418 GLY n 1 419 PHE n 1 420 SER n 1 421 LEU n 2 1 ACE n 2 2 MET n 2 3 ASN n 2 4 GLN n 2 5 ALA n 2 6 ILE n 2 7 ASP n 2 8 PHE n 2 9 ALA n 2 10 GLN n 2 11 ALA n 2 12 SER n 2 13 ILE n 2 14 ASP n 2 15 SER n 2 16 TYR n 2 17 LYS n 2 18 LYS n 2 19 HIS n 2 20 GLY n 2 21 ILE n 2 22 LEU n 2 23 GLU n 2 24 ASP n 2 25 VAL n 2 26 ILE n 2 27 HIS n 2 28 ASP n 2 29 THR n 2 30 SER n 2 31 PHE n 2 32 GLN n 2 33 PRO n 2 34 SER n 2 35 GLY n 2 36 ILE n 2 37 LEU n 2 38 ALA n 2 39 VAL n 2 40 GLU n 2 41 TYR n 2 42 SER n 2 43 SER n 2 44 SER n 2 45 ALA n 2 46 PRO n 2 47 VAL n 2 48 ALA n 2 49 MET n 2 50 GLY n 2 51 ASN n 2 52 THR n 2 53 LEU n 2 54 PRO n 2 55 THR n 2 56 GLU n 2 57 LYS n 2 58 ALA n 2 59 ARG n 2 60 SER n 2 61 LYS n 2 62 PRO n 2 63 GLN n 2 64 PHE n 2 65 GLN n 2 66 PHE n 2 67 THR n 2 68 PHE n 2 69 ASN n 2 70 LYS n 2 71 GLN n 2 72 MET n 2 73 GLN n 2 74 LYS n 2 75 SER n 2 76 VAL n 2 77 PRO n 2 78 GLN n 2 79 ALA n 2 80 ASN n 2 81 ALA n 2 82 TYR n 2 83 VAL n 2 84 PRO n 2 85 GLN n 2 86 ASP n 2 87 ASP n 2 88 ASP n 2 89 LEU n 2 90 PHE n 2 91 THR n 2 92 LEU n 2 93 VAL n 2 94 MET n 2 95 THR n 2 96 ASP n 2 97 PRO n 2 98 ASP n 2 99 ALA n 2 100 PRO n 2 101 SER n 2 102 LYS n 2 103 THR n 2 104 ASP n 2 105 HIS n 2 106 LYS n 2 107 TRP n 2 108 SER n 2 109 GLU n 2 110 PHE n 2 111 CYS n 2 112 HIS n 2 113 LEU n 2 114 VAL n 2 115 GLU n 2 116 CYS n 2 117 ASP n 2 118 LEU n 2 119 LYS n 2 120 LEU n 2 121 LEU n 2 122 ASN n 2 123 GLU n 2 124 ALA n 2 125 THR n 2 126 HIS n 2 127 GLU n 2 128 THR n 2 129 SER n 2 130 GLY n 2 131 ALA n 2 132 THR n 2 133 GLU n 2 134 PHE n 2 135 PHE n 2 136 ALA n 2 137 SER n 2 138 GLU n 2 139 PHE n 2 140 ASN n 2 141 THR n 2 142 LYS n 2 143 GLY n 2 144 SER n 2 145 ASN n 2 146 THR n 2 147 LEU n 2 148 ILE n 2 149 GLU n 2 150 TYR n 2 151 MET n 2 152 GLY n 2 153 PRO n 2 154 ALA n 2 155 PRO n 2 156 PRO n 2 157 LYS n 2 158 GLY n 2 159 SER n 2 160 GLY n 2 161 PRO n 2 162 HIS n 2 163 ARG n 2 164 TYR n 2 165 VAL n 2 166 PHE n 2 167 LEU n 2 168 LEU n 2 169 TYR n 2 170 LYS n 2 171 GLN n 2 172 PRO n 2 173 LYS n 2 174 GLY n 2 175 VAL n 2 176 ASP n 2 177 SER n 2 178 SER n 2 179 LYS n 2 180 PHE n 2 181 SER n 2 182 LYS n 2 183 ILE n 2 184 LYS n 2 185 ASP n 2 186 ARG n 2 187 PRO n 2 188 ASN n 2 189 TRP n 2 190 GLY n 2 191 TYR n 2 192 GLY n 2 193 THR n 2 194 PRO n 2 195 ALA n 2 196 THR n 2 197 GLY n 2 198 VAL n 2 199 GLY n 2 200 LYS n 2 201 TRP n 2 202 ALA n 2 203 LYS n 2 204 GLU n 2 205 ASN n 2 206 ASN n 2 207 LEU n 2 208 GLN n 2 209 LEU n 2 210 VAL n 2 211 ALA n 2 212 SER n 2 213 ASN n 2 214 PHE n 2 215 PHE n 2 216 TYR n 2 217 ALA n 2 218 GLU n 2 219 THR n 2 220 LYS n # loop_ _entity_src_nat.entity_id _entity_src_nat.pdbx_src_id _entity_src_nat.pdbx_alt_source_flag _entity_src_nat.pdbx_beg_seq_num _entity_src_nat.pdbx_end_seq_num _entity_src_nat.common_name _entity_src_nat.pdbx_organism_scientific _entity_src_nat.pdbx_ncbi_taxonomy_id _entity_src_nat.genus _entity_src_nat.species _entity_src_nat.strain _entity_src_nat.tissue _entity_src_nat.tissue_fraction _entity_src_nat.pdbx_secretion _entity_src_nat.pdbx_fragment _entity_src_nat.pdbx_variant _entity_src_nat.pdbx_cell_line _entity_src_nat.pdbx_atcc _entity_src_nat.pdbx_cellular_location _entity_src_nat.pdbx_organ _entity_src_nat.pdbx_organelle _entity_src_nat.pdbx_cell _entity_src_nat.pdbx_plasmid_name _entity_src_nat.pdbx_plasmid_details _entity_src_nat.details 1 1 sample ? ? ;baker's yeast ; 'Saccharomyces cerevisiae' 4932 Saccharomyces ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 2 1 sample ? ? ;baker's yeast ; 'Saccharomyces cerevisiae' 4932 Saccharomyces ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? # loop_ _struct_ref.id _struct_ref.db_name _struct_ref.db_code _struct_ref.pdbx_db_accession _struct_ref.entity_id _struct_ref.pdbx_seq_one_letter_code _struct_ref.pdbx_align_begin _struct_ref.pdbx_db_isoform 1 UNP CBPY_YEAST P00729 1 ;KIKDPKILGIDPNVTQYTGYLDVEDEDKHFFFWTFESRNDPAKDPVILWLNGGPGCSSLTGLFFELGPSSIGPDLKPIGN PYSWNSNATVIFLDQPVNVGFSYSGSSGVSNTVAAGKDVYNFLELFFDQFPEYVNKGQDFHIAGESYAGHYIPVFASEIL SHKDRNFNLTSVLIGNGLTDPLTQYNYYEPMACGEGGEPSVLPSEECSAMEDSLERCLGLIESCYDSQSVWSCVPATIYC NNAQLAPYQRTGRNVYDIRKDCEGGNLCYPTLQDIDDYLNQDYVKEAVGAEVDHYESCNFDINRNFLFAGDWMKPYHTAV TDLLNQDLPILVYAGDKDFICNWLGNKAWTDVLPWKYDEEFASQKVRNWTASITDEVAGEVKSYKHFTYLRVFNGGHMVP FDVPENALSMVNEWIHGGFSL ; 112 ? 2 UNP CPYI_YEAST P14306 2 ;MNQAIDFAQASIDSYKKHGILEDVIHDTSFQPSGILAVEYSSSAPVAMGNTLPTEKARSKPQFQFTFNKQMQKSVPQANA YVPQDDDLFTLVMTDPDAPSKTDHKWSEFCHLVECDLKLLNEATHETSGATEFFASEFNTKGSNTLIEYMGPAPPKGSGP HRYVFLLYKQPKGVDSSKFSKIKDRPNWGYGTPATGVGKWAKENNLQLVASNFFYAETK ; 1 ? # loop_ _struct_ref_seq.align_id _struct_ref_seq.ref_id _struct_ref_seq.pdbx_PDB_id_code _struct_ref_seq.pdbx_strand_id _struct_ref_seq.seq_align_beg _struct_ref_seq.pdbx_seq_align_beg_ins_code _struct_ref_seq.seq_align_end _struct_ref_seq.pdbx_seq_align_end_ins_code _struct_ref_seq.pdbx_db_accession _struct_ref_seq.db_align_beg _struct_ref_seq.pdbx_db_align_beg_ins_code _struct_ref_seq.db_align_end _struct_ref_seq.pdbx_db_align_end_ins_code _struct_ref_seq.pdbx_auth_seq_align_beg _struct_ref_seq.pdbx_auth_seq_align_end 1 1 1WPX A 1 ? 421 ? P00729 112 ? 532 ? 1 421 2 2 1WPX B 2 ? 220 ? P14306 1 ? 219 ? 501 719 # 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 ACE non-polymer . 'ACETYL GROUP' ? 'C2 H4 O' 44.053 ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 NDG D-saccharide . '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 SO4 non-polymer . 'SULFATE ION' ? 'O4 S -2' 96.063 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 1WPX _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.16 _exptl_crystal.density_percent_sol 61 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.temp 298 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 4.7 _exptl_crystal_grow.pdbx_details '0.1M Sodium acetate, 1.95M ammonium sulfate, pH 4.7, VAPOR DIFFUSION, HANGING DROP, temperature 298K' _exptl_crystal_grow.pdbx_pH_range . # _diffrn.id 1 _diffrn.ambient_temp 298.0 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector 'IMAGE PLATE' _diffrn_detector.type 'RIGAKU RAXIS IV' _diffrn_detector.pdbx_collection_date 2004-01-07 _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 1.5418 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source 'ROTATING ANODE' _diffrn_source.type 'RIGAKU RU300' _diffrn_source.pdbx_synchrotron_site ? _diffrn_source.pdbx_synchrotron_beamline ? _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 1.5418 # _reflns.entry_id 1WPX _reflns.observed_criterion_sigma_I ? _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 44.99 _reflns.d_resolution_high 2.70 _reflns.number_obs 28017 _reflns.number_all ? _reflns.percent_possible_obs ? _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI ? _reflns.B_iso_Wilson_estimate 56.6 _reflns.pdbx_redundancy ? _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _reflns_shell.d_res_high 2.7 _reflns_shell.d_res_low 2.8 _reflns_shell.percent_possible_all ? _reflns_shell.Rmerge_I_obs ? _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs ? _reflns_shell.pdbx_redundancy ? _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all ? _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 # _refine.entry_id 1WPX _refine.ls_number_reflns_obs 27780 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 0.0 _refine.pdbx_data_cutoff_high_absF 1566324.26 _refine.pdbx_data_cutoff_low_absF 0.000000 _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 44.99 _refine.ls_d_res_high 2.70 _refine.ls_percent_reflns_obs 99.3 _refine.ls_R_factor_obs 0.183 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.183 _refine.ls_R_factor_R_free 0.225 _refine.ls_R_factor_R_free_error 0.005 _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 8.8 _refine.ls_number_reflns_R_free 2456 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.B_iso_mean 38.4 _refine.aniso_B[1][1] 7.93 _refine.aniso_B[2][2] -7.25 _refine.aniso_B[3][3] -0.68 _refine.aniso_B[1][2] 0.00 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details 'FLAT MODEL' _refine.solvent_model_param_ksol 0.346374 _refine.solvent_model_param_bsol 40.4796 _refine.pdbx_solvent_vdw_probe_radii ? _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii ? _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details ? _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model RESTRAINED _refine.pdbx_stereochemistry_target_values ? _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML ? _refine.overall_SU_B ? _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_overall_phase_error ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_analyze.entry_id 1WPX _refine_analyze.Luzzati_coordinate_error_obs 0.27 _refine_analyze.Luzzati_sigma_a_obs 0.32 _refine_analyze.Luzzati_d_res_low_obs 5.00 _refine_analyze.Luzzati_coordinate_error_free 0.36 _refine_analyze.Luzzati_sigma_a_free 0.42 _refine_analyze.Luzzati_d_res_low_free ? _refine_analyze.number_disordered_residues ? _refine_analyze.occupancy_sum_hydrogen ? _refine_analyze.occupancy_sum_non_hydrogen ? _refine_analyze.pdbx_Luzzati_d_res_high_obs ? _refine_analyze.pdbx_refine_id 'X-RAY DIFFRACTION' # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 4960 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 52 _refine_hist.number_atoms_solvent 51 _refine_hist.number_atoms_total 5063 _refine_hist.d_res_high 2.70 _refine_hist.d_res_low 44.99 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function c_bond_d 0.006 ? ? ? 'X-RAY DIFFRACTION' ? c_angle_deg 1.4 ? ? ? 'X-RAY DIFFRACTION' ? c_dihedral_angle_d 24.0 ? ? ? 'X-RAY DIFFRACTION' ? c_improper_angle_d 0.82 ? ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_total_number_of_bins_used 6 _refine_ls_shell.d_res_high 2.70 _refine_ls_shell.d_res_low 2.87 _refine_ls_shell.number_reflns_R_work 4386 _refine_ls_shell.R_factor_R_work 0.261 _refine_ls_shell.percent_reflns_obs 100.0 _refine_ls_shell.R_factor_R_free 0.33 _refine_ls_shell.R_factor_R_free_error 0.025 _refine_ls_shell.percent_reflns_R_free 3.9 _refine_ls_shell.number_reflns_R_free 179 _refine_ls_shell.number_reflns_obs 4386 _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.number_reflns_all ? _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.R_factor_all ? # loop_ _pdbx_xplor_file.serial_no _pdbx_xplor_file.param_file _pdbx_xplor_file.topol_file _pdbx_xplor_file.pdbx_refine_id 1 PROTEIN_REP.PARAM PROTEIN.TOP 'X-RAY DIFFRACTION' 2 CAPPING.PARAM WATER.TOP 'X-RAY DIFFRACTION' 3 CARBOHYDRATE.PARAM CARBOHYDRATE.TOP 'X-RAY DIFFRACTION' 4 WATER_REP.PARAM CAPPING.TOP 'X-RAY DIFFRACTION' 5 ION.PARAM ION.TOP 'X-RAY DIFFRACTION' # _struct.entry_id 1WPX _struct.title 'Crystal structure of carboxypeptidase Y inhibitor complexed with the cognate proteinase' _struct.pdbx_descriptor 'Carboxypeptidase Y (E.C.3.4.16.5)/Carboxypeptidase Y inhibitor' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 1WPX _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text ;Carboxypeptidase inhibitor, serine proteinase inhibitor, proteinase-inhibitor complex, phosphatidylethanolamine-binding protein, phospholipid, Hydrolase ; # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 4 ? E N N 4 ? F N N 5 ? G N N 5 ? H N N 6 ? I N N 6 ? # _struct_biol.id 1 _struct_biol.pdbx_parent_biol_id ? _struct_biol.details ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 ASP A 4 ? LEU A 8 ? ASP A 4 LEU A 8 5 ? 5 HELX_P HELX_P2 2 SER A 58 ? PHE A 64 ? SER A 58 PHE A 64 1 ? 7 HELX_P HELX_P3 3 SER A 83 ? ASN A 87 ? SER A 83 ASN A 87 5 ? 5 HELX_P HELX_P4 4 ASN A 111 ? PHE A 130 ? ASN A 111 PHE A 130 1 ? 20 HELX_P HELX_P5 5 PRO A 131 ? LYS A 136 ? PRO A 131 LYS A 136 1 ? 6 HELX_P HELX_P6 6 TYR A 147 ? HIS A 162 ? TYR A 147 HIS A 162 1 ? 16 HELX_P HELX_P7 7 ASP A 180 ? TYR A 185 ? ASP A 180 TYR A 185 1 ? 6 HELX_P HELX_P8 8 TYR A 187 ? CYS A 193 ? TYR A 187 CYS A 193 1 ? 7 HELX_P HELX_P9 9 PRO A 203 ? GLN A 228 ? PRO A 203 GLN A 228 1 ? 26 HELX_P HELX_P10 10 SER A 229 ? LEU A 245 ? SER A 229 LEU A 245 1 ? 17 HELX_P HELX_P11 11 LEU A 245 ? THR A 251 ? LEU A 245 THR A 251 1 ? 7 HELX_P HELX_P12 12 THR A 271 ? ASN A 280 ? THR A 271 ASN A 280 1 ? 10 HELX_P HELX_P13 13 GLN A 281 ? GLY A 289 ? GLN A 281 GLY A 289 1 ? 9 HELX_P HELX_P14 14 ASN A 299 ? PHE A 308 ? ASN A 299 PHE A 308 1 ? 10 HELX_P HELX_P15 15 HIS A 317 ? GLN A 326 ? HIS A 317 GLN A 326 1 ? 10 HELX_P HELX_P16 16 ASN A 342 ? LEU A 353 ? ASN A 342 LEU A 353 1 ? 12 HELX_P HELX_P17 17 TYR A 357 ? GLN A 364 ? TYR A 357 GLN A 364 1 ? 8 HELX_P HELX_P18 18 MET A 398 ? VAL A 403 ? MET A 398 VAL A 403 1 ? 6 HELX_P HELX_P19 19 VAL A 403 ? HIS A 416 ? VAL A 403 HIS A 416 1 ? 14 HELX_P HELX_P20 20 MET B 2 ? ILE B 6 ? MET B 501 ILE B 505 5 ? 5 HELX_P HELX_P21 21 ASP B 7 ? HIS B 19 ? ASP B 506 HIS B 518 1 ? 13 HELX_P HELX_P22 22 GLY B 20 ? VAL B 25 ? GLY B 519 VAL B 524 1 ? 6 HELX_P HELX_P23 23 PRO B 54 ? ARG B 59 ? PRO B 553 ARG B 558 5 ? 6 HELX_P HELX_P24 24 ASP B 176 ? PHE B 180 ? ASP B 675 PHE B 679 5 ? 5 HELX_P HELX_P25 25 ARG B 186 ? TYR B 191 ? ARG B 685 TYR B 690 5 ? 6 HELX_P HELX_P26 26 GLY B 197 ? GLU B 204 ? GLY B 696 GLU B 703 1 ? 8 # _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 56 SG ? ? ? 1_555 A CYS 298 SG ? ? A CYS 56 A CYS 298 1_555 ? ? ? ? ? ? ? 2.033 ? disulf2 disulf ? ? A CYS 193 SG ? ? ? 1_555 A CYS 207 SG ? ? A CYS 193 A CYS 207 1_555 ? ? ? ? ? ? ? 2.026 ? disulf3 disulf ? ? A CYS 217 SG ? ? ? 1_555 A CYS 240 SG ? ? A CYS 217 A CYS 240 1_555 ? ? ? ? ? ? ? 2.032 ? disulf4 disulf ? ? A CYS 224 SG ? ? ? 1_555 A CYS 233 SG ? ? A CYS 224 A CYS 233 1_555 ? ? ? ? ? ? ? 2.024 ? disulf5 disulf ? ? A CYS 262 SG ? ? ? 1_555 A CYS 268 SG ? ? A CYS 262 A CYS 268 1_555 ? ? ? ? ? ? ? 2.021 ? covale1 covale ? ? A ASN 87 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 87 A NAG 810 1_555 ? ? ? ? ? ? ? 1.448 ? covale2 covale ? ? A ASN 168 ND2 ? ? ? 1_555 D NDG . C1 ? ? A ASN 168 A NDG 820 1_555 ? ? ? ? ? ? ? 1.448 ? covale3 covale ? ? A ASN 368 ND2 ? ? ? 1_555 E NDG . C1 ? ? A ASN 368 A NDG 830 1_555 ? ? ? ? ? ? ? 1.447 ? covale4 covale ? ? B ACE 1 C ? ? ? 1_555 B MET 2 N ? ? B ACE 500 B MET 501 1_555 ? ? ? ? ? ? ? 1.329 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 GLY 53 A . ? GLY 53 A PRO 54 A ? PRO 54 A 1 -0.10 2 GLN 95 A . ? GLN 95 A PRO 96 A ? PRO 96 A 1 -0.23 3 ALA 99 B . ? ALA 598 B PRO 100 B ? PRO 599 B 1 -0.08 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 11 ? B ? 2 ? C ? 6 ? D ? 8 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? anti-parallel A 2 3 ? anti-parallel A 3 4 ? anti-parallel A 4 5 ? parallel A 5 6 ? parallel A 6 7 ? parallel A 7 8 ? parallel A 8 9 ? parallel A 9 10 ? anti-parallel A 10 11 ? anti-parallel B 1 2 ? anti-parallel C 1 2 ? anti-parallel C 2 3 ? anti-parallel C 3 4 ? anti-parallel C 4 5 ? anti-parallel C 5 6 ? anti-parallel D 1 2 ? anti-parallel D 2 3 ? anti-parallel D 3 4 ? anti-parallel D 4 5 ? anti-parallel D 5 6 ? anti-parallel D 6 7 ? anti-parallel D 7 8 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 ILE A 2 ? LYS A 3 ? ILE A 2 LYS A 3 A 2 GLN A 16 ? ASP A 22 ? GLN A 16 ASP A 22 A 3 HIS A 29 ? PHE A 35 ? HIS A 29 PHE A 35 A 4 THR A 89 ? LEU A 93 ? THR A 89 LEU A 93 A 5 VAL A 46 ? LEU A 50 ? VAL A 46 LEU A 50 A 6 PHE A 140 ? GLU A 145 ? PHE A 140 GLU A 145 A 7 SER A 171 ? GLY A 175 ? SER A 171 GLY A 175 A 8 ILE A 330 ? GLY A 335 ? ILE A 330 GLY A 335 A 9 PHE A 387 ? VAL A 392 ? PHE A 387 VAL A 392 A 10 VAL A 377 ? TYR A 384 ? VAL A 377 TYR A 384 A 11 ARG A 367 ? THR A 370 ? ARG A 367 THR A 370 B 1 SER A 69 ? ILE A 71 ? SER A 69 ILE A 71 B 2 PRO A 77 ? GLY A 79 ? PRO A 77 GLY A 79 C 1 ALA B 45 ? VAL B 47 ? ALA B 544 VAL B 546 C 2 GLY B 35 ? SER B 42 ? GLY B 534 SER B 541 C 3 GLN B 63 ? ASN B 69 ? GLN B 562 ASN B 568 C 4 PHE B 134 ? ASN B 140 ? PHE B 633 ASN B 639 C 5 PHE B 110 ? LEU B 120 ? PHE B 609 LEU B 619 C 6 ASN B 145 ? ILE B 148 ? ASN B 644 ILE B 647 D 1 ALA B 45 ? VAL B 47 ? ALA B 544 VAL B 546 D 2 GLY B 35 ? SER B 42 ? GLY B 534 SER B 541 D 3 GLN B 63 ? ASN B 69 ? GLN B 562 ASN B 568 D 4 PHE B 134 ? ASN B 140 ? PHE B 633 ASN B 639 D 5 PHE B 110 ? LEU B 120 ? PHE B 609 LEU B 619 D 6 PHE B 90 ? ASP B 96 ? PHE B 589 ASP B 595 D 7 HIS B 162 ? LYS B 170 ? HIS B 661 LYS B 669 D 8 GLN B 208 ? ALA B 217 ? GLN B 707 ALA B 716 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 N LYS A 3 ? N LYS A 3 O THR A 18 ? O THR A 18 A 2 3 N TYR A 17 ? N TYR A 17 O THR A 34 ? O THR A 34 A 3 4 N TRP A 33 ? N TRP A 33 O PHE A 92 ? O PHE A 92 A 4 5 O ILE A 91 ? O ILE A 91 N TRP A 49 ? N TRP A 49 A 5 6 N LEU A 48 ? N LEU A 48 O ALA A 143 ? O ALA A 143 A 6 7 N ILE A 142 ? N ILE A 142 O LEU A 173 ? O LEU A 173 A 7 8 N ILE A 174 ? N ILE A 174 O LEU A 331 ? O LEU A 331 A 8 9 N VAL A 332 ? N VAL A 332 O THR A 388 ? O THR A 388 A 9 10 O TYR A 389 ? O TYR A 389 N LYS A 382 ? N LYS A 382 A 10 11 O GLY A 379 ? O GLY A 379 N TRP A 369 ? N TRP A 369 B 1 2 N SER A 70 ? N SER A 70 O ILE A 78 ? O ILE A 78 C 1 2 O ALA B 45 ? O ALA B 544 N SER B 42 ? N SER B 541 C 2 3 N GLU B 40 ? N GLU B 539 O GLN B 63 ? O GLN B 562 C 3 4 N PHE B 66 ? N PHE B 565 O SER B 137 ? O SER B 636 C 4 5 O ASN B 140 ? O ASN B 639 N LYS B 119 ? N LYS B 618 C 5 6 N CYS B 116 ? N CYS B 615 O ASN B 145 ? O ASN B 644 D 1 2 O ALA B 45 ? O ALA B 544 N SER B 42 ? N SER B 541 D 2 3 N GLU B 40 ? N GLU B 539 O GLN B 63 ? O GLN B 562 D 3 4 N PHE B 66 ? N PHE B 565 O SER B 137 ? O SER B 636 D 4 5 O ASN B 140 ? O ASN B 639 N LYS B 119 ? N LYS B 618 D 5 6 O LEU B 118 ? O LEU B 617 N PHE B 90 ? N PHE B 589 D 6 7 N THR B 91 ? N THR B 590 O TYR B 169 ? O TYR B 668 D 7 8 N LEU B 168 ? N LEU B 667 O VAL B 210 ? O VAL B 709 # 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 ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG A 810' AC2 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NDG A 820' AC3 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NDG A 830' AC4 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE SO4 A 901' AC5 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE SO4 B 902' # 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 4 ASN A 39 ? ASN A 39 . ? 1_555 ? 2 AC1 4 ASN A 87 ? ASN A 87 . ? 1_555 ? 3 AC1 4 HIS A 416 ? HIS A 416 . ? 1_555 ? 4 AC1 4 HOH H . ? HOH A 1034 . ? 1_555 ? 5 AC2 2 ASN A 166 ? ASN A 166 . ? 1_555 ? 6 AC2 2 ASN A 168 ? ASN A 168 . ? 1_555 ? 7 AC3 1 ASN A 368 ? ASN A 368 . ? 1_555 ? 8 AC4 8 GLY A 52 ? GLY A 52 . ? 1_555 ? 9 AC4 8 GLY A 53 ? GLY A 53 . ? 1_555 ? 10 AC4 8 SER A 146 ? SER A 146 . ? 1_555 ? 11 AC4 8 TYR A 256 ? TYR A 256 . ? 1_555 ? 12 AC4 8 HIS A 397 ? HIS A 397 . ? 1_555 ? 13 AC4 8 HOH H . ? HOH A 1000 . ? 1_555 ? 14 AC4 8 ACE B 1 ? ACE B 500 . ? 1_555 ? 15 AC4 8 MET B 2 ? MET B 501 . ? 1_555 ? 16 AC5 7 ASP B 96 ? ASP B 595 . ? 1_555 ? 17 AC5 7 PHE B 110 ? PHE B 609 . ? 1_555 ? 18 AC5 7 HIS B 112 ? HIS B 611 . ? 1_555 ? 19 AC5 7 ALA B 154 ? ALA B 653 . ? 1_555 ? 20 AC5 7 PRO B 155 ? PRO B 654 . ? 1_555 ? 21 AC5 7 HIS B 162 ? HIS B 661 . ? 1_555 ? 22 AC5 7 TYR B 164 ? TYR B 663 . ? 1_555 ? # _database_PDB_matrix.entry_id 1WPX _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 1WPX _atom_sites.fract_transf_matrix[1][1] 0.012326 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.005359 _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] 0.015352 _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 . LYS A 1 1 ? 27.570 6.573 54.074 1.00 51.95 ? 1 LYS A N 1 ATOM 2 C CA . LYS A 1 1 ? 28.025 5.153 54.060 1.00 50.81 ? 1 LYS A CA 1 ATOM 3 C C . LYS A 1 1 ? 28.301 4.655 52.650 1.00 49.00 ? 1 LYS A C 1 ATOM 4 O O . LYS A 1 1 ? 27.735 5.157 51.677 1.00 50.10 ? 1 LYS A O 1 ATOM 5 C CB . LYS A 1 1 ? 26.983 4.251 54.739 1.00 52.51 ? 1 LYS A CB 1 ATOM 6 C CG . LYS A 1 1 ? 25.539 4.660 54.506 1.00 55.16 ? 1 LYS A CG 1 ATOM 7 C CD . LYS A 1 1 ? 25.112 4.475 53.058 1.00 56.14 ? 1 LYS A CD 1 ATOM 8 C CE . LYS A 1 1 ? 23.692 4.993 52.829 1.00 55.96 ? 1 LYS A CE 1 ATOM 9 N NZ . LYS A 1 1 ? 22.662 4.304 53.666 1.00 55.86 ? 1 LYS A NZ 1 ATOM 10 N N . ILE A 1 2 ? 29.185 3.669 52.551 1.00 45.71 ? 2 ILE A N 1 ATOM 11 C CA . ILE A 1 2 ? 29.553 3.093 51.270 1.00 42.29 ? 2 ILE A CA 1 ATOM 12 C C . ILE A 1 2 ? 29.069 1.657 51.194 1.00 39.81 ? 2 ILE A C 1 ATOM 13 O O . ILE A 1 2 ? 29.066 0.942 52.192 1.00 38.32 ? 2 ILE A O 1 ATOM 14 C CB . ILE A 1 2 ? 31.062 3.143 51.079 1.00 42.45 ? 2 ILE A CB 1 ATOM 15 C CG1 . ILE A 1 2 ? 31.515 4.604 51.095 1.00 43.25 ? 2 ILE A CG1 1 ATOM 16 C CG2 . ILE A 1 2 ? 31.442 2.455 49.783 1.00 42.78 ? 2 ILE A CG2 1 ATOM 17 C CD1 . ILE A 1 2 ? 33.009 4.784 51.021 1.00 45.19 ? 2 ILE A CD1 1 ATOM 18 N N . LYS A 1 3 ? 28.658 1.240 50.004 1.00 37.90 ? 3 LYS A N 1 ATOM 19 C CA . LYS A 1 3 ? 28.136 -0.104 49.808 1.00 35.49 ? 3 LYS A CA 1 ATOM 20 C C . LYS A 1 3 ? 28.716 -0.778 48.583 1.00 33.50 ? 3 LYS A C 1 ATOM 21 O O . LYS A 1 3 ? 29.268 -0.125 47.700 1.00 32.76 ? 3 LYS A O 1 ATOM 22 C CB . LYS A 1 3 ? 26.614 -0.053 49.642 1.00 37.08 ? 3 LYS A CB 1 ATOM 23 C CG . LYS A 1 3 ? 25.858 0.504 50.835 1.00 37.84 ? 3 LYS A CG 1 ATOM 24 C CD . LYS A 1 3 ? 25.660 -0.562 51.891 1.00 39.18 ? 3 LYS A CD 1 ATOM 25 C CE . LYS A 1 3 ? 24.615 -1.565 51.452 1.00 41.12 ? 3 LYS A CE 1 ATOM 26 N NZ . LYS A 1 3 ? 23.270 -0.932 51.417 1.00 43.65 ? 3 LYS A NZ 1 ATOM 27 N N . ASP A 1 4 ? 28.574 -2.097 48.543 1.00 31.85 ? 4 ASP A N 1 ATOM 28 C CA . ASP A 1 4 ? 29.023 -2.900 47.419 1.00 31.00 ? 4 ASP A CA 1 ATOM 29 C C . ASP A 1 4 ? 27.738 -3.343 46.720 1.00 31.12 ? 4 ASP A C 1 ATOM 30 O O . ASP A 1 4 ? 27.052 -4.250 47.188 1.00 32.22 ? 4 ASP A O 1 ATOM 31 C CB . ASP A 1 4 ? 29.799 -4.111 47.910 1.00 29.24 ? 4 ASP A CB 1 ATOM 32 C CG . ASP A 1 4 ? 30.155 -5.058 46.791 1.00 32.63 ? 4 ASP A CG 1 ATOM 33 O OD1 . ASP A 1 4 ? 30.781 -6.099 47.084 1.00 36.50 ? 4 ASP A OD1 1 ATOM 34 O OD2 . ASP A 1 4 ? 29.808 -4.767 45.621 1.00 30.41 ? 4 ASP A OD2 1 ATOM 35 N N . PRO A 1 5 ? 27.392 -2.698 45.592 1.00 30.72 ? 5 PRO A N 1 ATOM 36 C CA . PRO A 1 5 ? 26.184 -3.002 44.821 1.00 30.86 ? 5 PRO A CA 1 ATOM 37 C C . PRO A 1 5 ? 26.338 -4.122 43.809 1.00 32.25 ? 5 PRO A C 1 ATOM 38 O O . PRO A 1 5 ? 25.526 -4.248 42.887 1.00 31.62 ? 5 PRO A O 1 ATOM 39 C CB . PRO A 1 5 ? 25.895 -1.678 44.140 1.00 31.33 ? 5 PRO A CB 1 ATOM 40 C CG . PRO A 1 5 ? 27.279 -1.230 43.761 1.00 30.52 ? 5 PRO A CG 1 ATOM 41 C CD . PRO A 1 5 ? 28.101 -1.540 45.009 1.00 30.52 ? 5 PRO A CD 1 ATOM 42 N N . LYS A 1 6 ? 27.371 -4.937 43.973 1.00 33.65 ? 6 LYS A N 1 ATOM 43 C CA . LYS A 1 6 ? 27.599 -6.004 43.018 1.00 35.09 ? 6 LYS A CA 1 ATOM 44 C C . LYS A 1 6 ? 26.412 -6.933 42.820 1.00 34.01 ? 6 LYS A C 1 ATOM 45 O O . LYS A 1 6 ? 26.216 -7.431 41.719 1.00 32.85 ? 6 LYS A O 1 ATOM 46 C CB . LYS A 1 6 ? 28.817 -6.837 43.406 1.00 38.56 ? 6 LYS A CB 1 ATOM 47 C CG . LYS A 1 6 ? 28.598 -7.748 44.599 1.00 42.89 ? 6 LYS A CG 1 ATOM 48 C CD . LYS A 1 6 ? 29.695 -8.800 44.667 1.00 48.31 ? 6 LYS A CD 1 ATOM 49 C CE . LYS A 1 6 ? 29.508 -9.727 45.861 1.00 52.76 ? 6 LYS A CE 1 ATOM 50 N NZ . LYS A 1 6 ? 29.559 -8.987 47.168 1.00 55.51 ? 6 LYS A NZ 1 ATOM 51 N N . ILE A 1 7 ? 25.612 -7.166 43.857 1.00 33.11 ? 7 ILE A N 1 ATOM 52 C CA . ILE A 1 7 ? 24.497 -8.089 43.688 1.00 34.00 ? 7 ILE A CA 1 ATOM 53 C C . ILE A 1 7 ? 23.550 -7.700 42.569 1.00 34.17 ? 7 ILE A C 1 ATOM 54 O O . ILE A 1 7 ? 22.817 -8.542 42.061 1.00 36.26 ? 7 ILE A O 1 ATOM 55 C CB . ILE A 1 7 ? 23.688 -8.317 44.996 1.00 34.50 ? 7 ILE A CB 1 ATOM 56 C CG1 . ILE A 1 7 ? 22.906 -7.064 45.394 1.00 34.13 ? 7 ILE A CG1 1 ATOM 57 C CG2 . ILE A 1 7 ? 24.633 -8.772 46.092 1.00 35.09 ? 7 ILE A CG2 1 ATOM 58 C CD1 . ILE A 1 7 ? 23.770 -5.910 45.818 1.00 40.64 ? 7 ILE A CD1 1 ATOM 59 N N . LEU A 1 8 ? 23.552 -6.432 42.182 1.00 34.00 ? 8 LEU A N 1 ATOM 60 C CA . LEU A 1 8 ? 22.707 -5.998 41.076 1.00 34.62 ? 8 LEU A CA 1 ATOM 61 C C . LEU A 1 8 ? 23.419 -6.491 39.819 1.00 36.25 ? 8 LEU A C 1 ATOM 62 O O . LEU A 1 8 ? 24.545 -6.979 39.890 1.00 37.35 ? 8 LEU A O 1 ATOM 63 C CB . LEU A 1 8 ? 22.607 -4.476 41.051 1.00 33.92 ? 8 LEU A CB 1 ATOM 64 C CG . LEU A 1 8 ? 22.045 -3.826 42.313 1.00 33.80 ? 8 LEU A CG 1 ATOM 65 C CD1 . LEU A 1 8 ? 22.084 -2.310 42.173 1.00 32.66 ? 8 LEU A CD1 1 ATOM 66 C CD2 . LEU A 1 8 ? 20.623 -4.321 42.548 1.00 31.85 ? 8 LEU A CD2 1 ATOM 67 N N . GLY A 1 9 ? 22.794 -6.382 38.661 1.00 38.21 ? 9 GLY A N 1 ATOM 68 C CA . GLY A 1 9 ? 23.495 -6.854 37.476 1.00 42.28 ? 9 GLY A CA 1 ATOM 69 C C . GLY A 1 9 ? 24.683 -5.967 37.151 1.00 42.00 ? 9 GLY A C 1 ATOM 70 O O . GLY A 1 9 ? 25.817 -6.279 37.467 1.00 42.13 ? 9 GLY A O 1 ATOM 71 N N . ILE A 1 10 ? 24.372 -4.843 36.517 1.00 44.24 ? 10 ILE A N 1 ATOM 72 C CA . ILE A 1 10 ? 25.300 -3.805 36.086 1.00 42.69 ? 10 ILE A CA 1 ATOM 73 C C . ILE A 1 10 ? 26.655 -4.219 35.521 1.00 41.39 ? 10 ILE A C 1 ATOM 74 O O . ILE A 1 10 ? 26.869 -4.069 34.320 1.00 41.33 ? 10 ILE A O 1 ATOM 75 C CB . ILE A 1 10 ? 25.483 -2.752 37.181 1.00 42.97 ? 10 ILE A CB 1 ATOM 76 C CG1 . ILE A 1 10 ? 24.146 -2.068 37.488 1.00 42.67 ? 10 ILE A CG1 1 ATOM 77 C CG2 . ILE A 1 10 ? 26.359 -1.645 36.656 1.00 44.49 ? 10 ILE A CG2 1 ATOM 78 C CD1 . ILE A 1 10 ? 23.022 -2.986 37.884 1.00 41.25 ? 10 ILE A CD1 1 ATOM 79 N N . ASP A 1 11 ? 27.586 -4.696 36.341 1.00 39.97 ? 11 ASP A N 1 ATOM 80 C CA . ASP A 1 11 ? 28.870 -5.131 35.776 1.00 40.70 ? 11 ASP A CA 1 ATOM 81 C C . ASP A 1 11 ? 29.571 -6.201 36.609 1.00 41.68 ? 11 ASP A C 1 ATOM 82 O O . ASP A 1 11 ? 30.442 -5.907 37.434 1.00 42.48 ? 11 ASP A O 1 ATOM 83 C CB . ASP A 1 11 ? 29.816 -3.939 35.550 1.00 39.15 ? 11 ASP A CB 1 ATOM 84 C CG . ASP A 1 11 ? 30.893 -4.236 34.499 1.00 37.65 ? 11 ASP A CG 1 ATOM 85 O OD1 . ASP A 1 11 ? 31.685 -3.338 34.160 1.00 37.42 ? 11 ASP A OD1 1 ATOM 86 O OD2 . ASP A 1 11 ? 30.953 -5.373 34.000 1.00 38.97 ? 11 ASP A OD2 1 ATOM 87 N N . PRO A 1 12 ? 29.203 -7.471 36.389 1.00 42.49 ? 12 PRO A N 1 ATOM 88 C CA . PRO A 1 12 ? 29.787 -8.604 37.112 1.00 44.21 ? 12 PRO A CA 1 ATOM 89 C C . PRO A 1 12 ? 31.308 -8.709 36.986 1.00 45.39 ? 12 PRO A C 1 ATOM 90 O O . PRO A 1 12 ? 31.892 -8.404 35.944 1.00 46.24 ? 12 PRO A O 1 ATOM 91 C CB . PRO A 1 12 ? 29.067 -9.807 36.506 1.00 42.58 ? 12 PRO A CB 1 ATOM 92 C CG . PRO A 1 12 ? 28.786 -9.360 35.112 1.00 42.78 ? 12 PRO A CG 1 ATOM 93 C CD . PRO A 1 12 ? 28.308 -7.943 35.320 1.00 42.31 ? 12 PRO A CD 1 ATOM 94 N N . ASN A 1 13 ? 31.945 -9.126 38.070 1.00 47.05 ? 13 ASN A N 1 ATOM 95 C CA . ASN A 1 13 ? 33.394 -9.289 38.096 1.00 49.09 ? 13 ASN A CA 1 ATOM 96 C C . ASN A 1 13 ? 34.187 -8.012 37.765 1.00 46.56 ? 13 ASN A C 1 ATOM 97 O O . ASN A 1 13 ? 35.113 -8.024 36.960 1.00 47.44 ? 13 ASN A O 1 ATOM 98 C CB . ASN A 1 13 ? 33.786 -10.443 37.163 1.00 53.44 ? 13 ASN A CB 1 ATOM 99 C CG . ASN A 1 13 ? 33.121 -11.771 37.560 1.00 57.27 ? 13 ASN A CG 1 ATOM 100 O OD1 . ASN A 1 13 ? 33.236 -12.776 36.853 1.00 60.58 ? 13 ASN A OD1 1 ATOM 101 N ND2 . ASN A 1 13 ? 32.428 -11.773 38.697 1.00 56.42 ? 13 ASN A ND2 1 ATOM 102 N N . VAL A 1 14 ? 33.796 -6.920 38.415 1.00 43.18 ? 14 VAL A N 1 ATOM 103 C CA . VAL A 1 14 ? 34.418 -5.600 38.307 1.00 38.50 ? 14 VAL A CA 1 ATOM 104 C C . VAL A 1 14 ? 33.995 -4.954 39.618 1.00 35.56 ? 14 VAL A C 1 ATOM 105 O O . VAL A 1 14 ? 32.806 -4.769 39.857 1.00 35.14 ? 14 VAL A O 1 ATOM 106 C CB . VAL A 1 14 ? 33.841 -4.763 37.144 1.00 39.70 ? 14 VAL A CB 1 ATOM 107 C CG1 . VAL A 1 14 ? 34.427 -3.361 37.178 1.00 38.45 ? 14 VAL A CG1 1 ATOM 108 C CG2 . VAL A 1 14 ? 34.158 -5.417 35.814 1.00 40.03 ? 14 VAL A CG2 1 ATOM 109 N N . THR A 1 15 ? 34.947 -4.626 40.482 1.00 33.32 ? 15 THR A N 1 ATOM 110 C CA . THR A 1 15 ? 34.572 -4.044 41.763 1.00 32.15 ? 15 THR A CA 1 ATOM 111 C C . THR A 1 15 ? 34.008 -2.631 41.615 1.00 31.17 ? 15 THR A C 1 ATOM 112 O O . THR A 1 15 ? 34.407 -1.866 40.739 1.00 30.63 ? 15 THR A O 1 ATOM 113 C CB . THR A 1 15 ? 35.756 -4.092 42.771 1.00 30.66 ? 15 THR A CB 1 ATOM 114 O OG1 . THR A 1 15 ? 36.064 -2.773 43.228 1.00 33.83 ? 15 THR A OG1 1 ATOM 115 C CG2 . THR A 1 15 ? 36.971 -4.721 42.134 1.00 29.83 ? 15 THR A CG2 1 ATOM 116 N N . GLN A 1 16 ? 33.062 -2.291 42.475 1.00 30.72 ? 16 GLN A N 1 ATOM 117 C CA . GLN A 1 16 ? 32.421 -0.996 42.380 1.00 31.67 ? 16 GLN A CA 1 ATOM 118 C C . GLN A 1 16 ? 31.864 -0.529 43.722 1.00 31.57 ? 16 GLN A C 1 ATOM 119 O O . GLN A 1 16 ? 31.602 -1.335 44.608 1.00 32.92 ? 16 GLN A O 1 ATOM 120 C CB . GLN A 1 16 ? 31.306 -1.095 41.332 1.00 31.98 ? 16 GLN A CB 1 ATOM 121 C CG . GLN A 1 16 ? 30.265 -2.164 41.637 1.00 32.99 ? 16 GLN A CG 1 ATOM 122 C CD . GLN A 1 16 ? 29.510 -2.644 40.399 1.00 34.19 ? 16 GLN A CD 1 ATOM 123 O OE1 . GLN A 1 16 ? 30.056 -3.362 39.563 1.00 34.17 ? 16 GLN A OE1 1 ATOM 124 N NE2 . GLN A 1 16 ? 28.249 -2.250 40.285 1.00 33.96 ? 16 GLN A NE2 1 ATOM 125 N N . TYR A 1 17 ? 31.700 0.777 43.880 1.00 31.12 ? 17 TYR A N 1 ATOM 126 C CA . TYR A 1 17 ? 31.157 1.305 45.123 1.00 31.58 ? 17 TYR A CA 1 ATOM 127 C C . TYR A 1 17 ? 30.036 2.301 44.861 1.00 31.36 ? 17 TYR A C 1 ATOM 128 O O . TYR A 1 17 ? 30.045 3.016 43.863 1.00 32.58 ? 17 TYR A O 1 ATOM 129 C CB . TYR A 1 17 ? 32.235 2.023 45.943 1.00 32.74 ? 17 TYR A CB 1 ATOM 130 C CG . TYR A 1 17 ? 33.513 1.254 46.143 1.00 34.53 ? 17 TYR A CG 1 ATOM 131 C CD1 . TYR A 1 17 ? 34.472 1.189 45.135 1.00 33.68 ? 17 TYR A CD1 1 ATOM 132 C CD2 . TYR A 1 17 ? 33.769 0.587 47.345 1.00 35.50 ? 17 TYR A CD2 1 ATOM 133 C CE1 . TYR A 1 17 ? 35.649 0.480 45.313 1.00 35.27 ? 17 TYR A CE1 1 ATOM 134 C CE2 . TYR A 1 17 ? 34.949 -0.127 47.535 1.00 34.46 ? 17 TYR A CE2 1 ATOM 135 C CZ . TYR A 1 17 ? 35.880 -0.176 46.514 1.00 35.98 ? 17 TYR A CZ 1 ATOM 136 O OH . TYR A 1 17 ? 37.044 -0.880 46.686 1.00 39.61 ? 17 TYR A OH 1 ATOM 137 N N . THR A 1 18 ? 29.064 2.332 45.760 1.00 30.35 ? 18 THR A N 1 ATOM 138 C CA . THR A 1 18 ? 27.970 3.284 45.672 1.00 31.10 ? 18 THR A CA 1 ATOM 139 C C . THR A 1 18 ? 27.843 3.787 47.093 1.00 31.50 ? 18 THR A C 1 ATOM 140 O O . THR A 1 18 ? 28.349 3.160 48.028 1.00 32.24 ? 18 THR A O 1 ATOM 141 C CB . THR A 1 18 ? 26.633 2.634 45.254 1.00 32.88 ? 18 THR A CB 1 ATOM 142 O OG1 . THR A 1 18 ? 26.297 1.586 46.172 1.00 33.91 ? 18 THR A OG1 1 ATOM 143 C CG2 . THR A 1 18 ? 26.729 2.068 43.852 1.00 32.83 ? 18 THR A CG2 1 ATOM 144 N N . GLY A 1 19 ? 27.181 4.917 47.270 1.00 31.75 ? 19 GLY A N 1 ATOM 145 C CA . GLY A 1 19 ? 27.024 5.436 48.611 1.00 32.51 ? 19 GLY A CA 1 ATOM 146 C C . GLY A 1 19 ? 27.125 6.940 48.644 1.00 33.41 ? 19 GLY A C 1 ATOM 147 O O . GLY A 1 19 ? 26.942 7.612 47.626 1.00 32.98 ? 19 GLY A O 1 ATOM 148 N N . TYR A 1 20 ? 27.436 7.472 49.817 1.00 33.36 ? 20 TYR A N 1 ATOM 149 C CA . TYR A 1 20 ? 27.532 8.907 49.969 1.00 33.85 ? 20 TYR A CA 1 ATOM 150 C C . TYR A 1 20 ? 28.839 9.370 50.557 1.00 34.74 ? 20 TYR A C 1 ATOM 151 O O . TYR A 1 20 ? 29.467 8.678 51.351 1.00 36.69 ? 20 TYR A O 1 ATOM 152 C CB . TYR A 1 20 ? 26.400 9.411 50.856 1.00 30.79 ? 20 TYR A CB 1 ATOM 153 C CG . TYR A 1 20 ? 25.030 9.281 50.249 1.00 29.89 ? 20 TYR A CG 1 ATOM 154 C CD1 . TYR A 1 20 ? 24.515 10.281 49.430 1.00 29.47 ? 20 TYR A CD1 1 ATOM 155 C CD2 . TYR A 1 20 ? 24.234 8.170 50.514 1.00 28.57 ? 20 TYR A CD2 1 ATOM 156 C CE1 . TYR A 1 20 ? 23.239 10.182 48.895 1.00 29.13 ? 20 TYR A CE1 1 ATOM 157 C CE2 . TYR A 1 20 ? 22.957 8.060 49.983 1.00 29.33 ? 20 TYR A CE2 1 ATOM 158 C CZ . TYR A 1 20 ? 22.466 9.072 49.175 1.00 29.19 ? 20 TYR A CZ 1 ATOM 159 O OH . TYR A 1 20 ? 21.201 8.973 48.647 1.00 30.27 ? 20 TYR A OH 1 ATOM 160 N N . LEU A 1 21 ? 29.235 10.559 50.142 1.00 35.72 ? 21 LEU A N 1 ATOM 161 C CA . LEU A 1 21 ? 30.430 11.201 50.633 1.00 37.99 ? 21 LEU A CA 1 ATOM 162 C C . LEU A 1 21 ? 29.815 12.476 51.184 1.00 40.44 ? 21 LEU A C 1 ATOM 163 O O . LEU A 1 21 ? 29.091 13.165 50.476 1.00 41.36 ? 21 LEU A O 1 ATOM 164 C CB . LEU A 1 21 ? 31.389 11.469 49.474 1.00 36.28 ? 21 LEU A CB 1 ATOM 165 C CG . LEU A 1 21 ? 32.769 10.813 49.615 1.00 34.03 ? 21 LEU A CG 1 ATOM 166 C CD1 . LEU A 1 21 ? 32.633 9.446 50.263 1.00 31.78 ? 21 LEU A CD1 1 ATOM 167 C CD2 . LEU A 1 21 ? 33.431 10.711 48.247 1.00 33.43 ? 21 LEU A CD2 1 ATOM 168 N N . ASP A 1 22 ? 30.072 12.779 52.451 1.00 45.20 ? 22 ASP A N 1 ATOM 169 C CA . ASP A 1 22 ? 29.456 13.950 53.057 1.00 48.09 ? 22 ASP A CA 1 ATOM 170 C C . ASP A 1 22 ? 30.332 15.134 53.396 1.00 50.59 ? 22 ASP A C 1 ATOM 171 O O . ASP A 1 22 ? 31.524 15.008 53.651 1.00 51.06 ? 22 ASP A O 1 ATOM 172 C CB . ASP A 1 22 ? 28.705 13.541 54.322 1.00 47.94 ? 22 ASP A CB 1 ATOM 173 C CG . ASP A 1 22 ? 27.950 12.241 54.151 1.00 50.57 ? 22 ASP A CG 1 ATOM 174 O OD1 . ASP A 1 22 ? 28.497 11.178 54.530 1.00 50.95 ? 22 ASP A OD1 1 ATOM 175 O OD2 . ASP A 1 22 ? 26.817 12.280 53.624 1.00 51.34 ? 22 ASP A OD2 1 ATOM 176 N N . VAL A 1 23 ? 29.689 16.294 53.389 1.00 54.25 ? 23 VAL A N 1 ATOM 177 C CA . VAL A 1 23 ? 30.287 17.570 53.733 1.00 57.24 ? 23 VAL A CA 1 ATOM 178 C C . VAL A 1 23 ? 29.273 18.056 54.775 1.00 60.77 ? 23 VAL A C 1 ATOM 179 O O . VAL A 1 23 ? 28.669 19.118 54.635 1.00 62.17 ? 23 VAL A O 1 ATOM 180 C CB . VAL A 1 23 ? 30.309 18.528 52.510 1.00 56.21 ? 23 VAL A CB 1 ATOM 181 C CG1 . VAL A 1 23 ? 31.089 19.784 52.839 1.00 56.44 ? 23 VAL A CG1 1 ATOM 182 C CG2 . VAL A 1 23 ? 30.930 17.838 51.314 1.00 54.75 ? 23 VAL A CG2 1 ATOM 183 N N . GLU A 1 24 ? 29.076 17.228 55.804 1.00 65.08 ? 24 GLU A N 1 ATOM 184 C CA . GLU A 1 24 ? 28.124 17.475 56.899 1.00 68.50 ? 24 GLU A CA 1 ATOM 185 C C . GLU A 1 24 ? 28.172 18.876 57.500 1.00 68.67 ? 24 GLU A C 1 ATOM 186 O O . GLU A 1 24 ? 27.163 19.382 57.997 1.00 68.63 ? 24 GLU A O 1 ATOM 187 C CB . GLU A 1 24 ? 28.326 16.441 58.016 1.00 70.24 ? 24 GLU A CB 1 ATOM 188 C CG . GLU A 1 24 ? 29.669 16.551 58.716 1.00 73.22 ? 24 GLU A CG 1 ATOM 189 C CD . GLU A 1 24 ? 30.838 16.400 57.758 1.00 75.56 ? 24 GLU A CD 1 ATOM 190 O OE1 . GLU A 1 24 ? 31.029 15.285 57.223 1.00 76.15 ? 24 GLU A OE1 1 ATOM 191 O OE2 . GLU A 1 24 ? 31.559 17.398 57.533 1.00 77.10 ? 24 GLU A OE2 1 ATOM 192 N N . ASP A 1 25 ? 29.346 19.495 57.465 1.00 69.19 ? 25 ASP A N 1 ATOM 193 C CA . ASP A 1 25 ? 29.507 20.843 57.990 1.00 69.88 ? 25 ASP A CA 1 ATOM 194 C C . ASP A 1 25 ? 28.782 21.831 57.075 1.00 68.14 ? 25 ASP A C 1 ATOM 195 O O . ASP A 1 25 ? 28.921 23.045 57.215 1.00 69.38 ? 25 ASP A O 1 ATOM 196 C CB . ASP A 1 25 ? 30.996 21.181 58.083 1.00 73.13 ? 25 ASP A CB 1 ATOM 197 C CG . ASP A 1 25 ? 31.743 20.881 56.794 1.00 76.17 ? 25 ASP A CG 1 ATOM 198 O OD1 . ASP A 1 25 ? 31.646 21.691 55.846 1.00 77.94 ? 25 ASP A OD1 1 ATOM 199 O OD2 . ASP A 1 25 ? 32.417 19.827 56.726 1.00 77.63 ? 25 ASP A OD2 1 ATOM 200 N N . GLU A 1 26 ? 28.012 21.292 56.135 1.00 65.33 ? 26 GLU A N 1 ATOM 201 C CA . GLU A 1 26 ? 27.237 22.088 55.186 1.00 62.54 ? 26 GLU A CA 1 ATOM 202 C C . GLU A 1 26 ? 25.987 21.293 54.823 1.00 59.62 ? 26 GLU A C 1 ATOM 203 O O . GLU A 1 26 ? 25.146 21.745 54.044 1.00 59.35 ? 26 GLU A O 1 ATOM 204 C CB . GLU A 1 26 ? 28.048 22.364 53.918 1.00 63.10 ? 26 GLU A CB 1 ATOM 205 C CG . GLU A 1 26 ? 29.419 22.950 54.170 1.00 64.75 ? 26 GLU A CG 1 ATOM 206 C CD . GLU A 1 26 ? 30.180 23.224 52.886 1.00 67.13 ? 26 GLU A CD 1 ATOM 207 O OE1 . GLU A 1 26 ? 31.417 23.413 52.961 1.00 66.99 ? 26 GLU A OE1 1 ATOM 208 O OE2 . GLU A 1 26 ? 29.541 23.259 51.806 1.00 67.91 ? 26 GLU A OE2 1 ATOM 209 N N . ASP A 1 27 ? 25.886 20.098 55.393 1.00 56.09 ? 27 ASP A N 1 ATOM 210 C CA . ASP A 1 27 ? 24.755 19.215 55.156 1.00 52.38 ? 27 ASP A CA 1 ATOM 211 C C . ASP A 1 27 ? 24.579 18.912 53.668 1.00 50.05 ? 27 ASP A C 1 ATOM 212 O O . ASP A 1 27 ? 23.543 19.208 53.073 1.00 48.68 ? 27 ASP A O 1 ATOM 213 C CB . ASP A 1 27 ? 23.481 19.838 55.726 1.00 51.71 ? 27 ASP A CB 1 ATOM 214 C CG . ASP A 1 27 ? 22.297 18.900 55.656 1.00 52.34 ? 27 ASP A CG 1 ATOM 215 O OD1 . ASP A 1 27 ? 22.448 17.726 56.053 1.00 51.06 ? 27 ASP A OD1 1 ATOM 216 O OD2 . ASP A 1 27 ? 21.213 19.337 55.213 1.00 54.90 ? 27 ASP A OD2 1 ATOM 217 N N . LYS A 1 28 ? 25.608 18.320 53.073 1.00 46.75 ? 28 LYS A N 1 ATOM 218 C CA . LYS A 1 28 ? 25.573 17.962 51.662 1.00 42.99 ? 28 LYS A CA 1 ATOM 219 C C . LYS A 1 28 ? 25.973 16.506 51.493 1.00 41.69 ? 28 LYS A C 1 ATOM 220 O O . LYS A 1 28 ? 27.062 16.086 51.890 1.00 41.96 ? 28 LYS A O 1 ATOM 221 C CB . LYS A 1 28 ? 26.493 18.879 50.859 1.00 40.13 ? 28 LYS A CB 1 ATOM 222 C CG . LYS A 1 28 ? 25.945 20.284 50.758 1.00 38.50 ? 28 LYS A CG 1 ATOM 223 C CD . LYS A 1 28 ? 26.860 21.201 49.981 1.00 37.71 ? 28 LYS A CD 1 ATOM 224 C CE . LYS A 1 28 ? 26.196 22.548 49.764 1.00 35.80 ? 28 LYS A CE 1 ATOM 225 N NZ . LYS A 1 28 ? 27.142 23.531 49.198 1.00 35.94 ? 28 LYS A NZ 1 ATOM 226 N N . HIS A 1 29 ? 25.073 15.738 50.896 1.00 39.00 ? 29 HIS A N 1 ATOM 227 C CA . HIS A 1 29 ? 25.297 14.322 50.701 1.00 36.41 ? 29 HIS A CA 1 ATOM 228 C C . HIS A 1 29 ? 25.341 13.975 49.225 1.00 35.16 ? 29 HIS A C 1 ATOM 229 O O . HIS A 1 29 ? 24.317 13.939 48.546 1.00 34.36 ? 29 HIS A O 1 ATOM 230 C CB . HIS A 1 29 ? 24.187 13.577 51.428 1.00 36.95 ? 29 HIS A CB 1 ATOM 231 C CG . HIS A 1 29 ? 23.940 14.114 52.802 1.00 38.35 ? 29 HIS A CG 1 ATOM 232 N ND1 . HIS A 1 29 ? 24.812 13.902 53.848 1.00 37.79 ? 29 HIS A ND1 1 ATOM 233 C CD2 . HIS A 1 29 ? 22.998 14.967 53.268 1.00 39.35 ? 29 HIS A CD2 1 ATOM 234 C CE1 . HIS A 1 29 ? 24.422 14.604 54.895 1.00 36.90 ? 29 HIS A CE1 1 ATOM 235 N NE2 . HIS A 1 29 ? 23.324 15.260 54.570 1.00 37.78 ? 29 HIS A NE2 1 ATOM 236 N N . PHE A 1 30 ? 26.549 13.721 48.736 1.00 33.57 ? 30 PHE A N 1 ATOM 237 C CA . PHE A 1 30 ? 26.753 13.389 47.341 1.00 32.59 ? 30 PHE A CA 1 ATOM 238 C C . PHE A 1 30 ? 26.720 11.905 47.056 1.00 31.28 ? 30 PHE A C 1 ATOM 239 O O . PHE A 1 30 ? 27.529 11.152 47.586 1.00 31.40 ? 30 PHE A O 1 ATOM 240 C CB . PHE A 1 30 ? 28.081 13.955 46.872 1.00 34.83 ? 30 PHE A CB 1 ATOM 241 C CG . PHE A 1 30 ? 28.097 15.446 46.796 1.00 38.01 ? 30 PHE A CG 1 ATOM 242 C CD1 . PHE A 1 30 ? 27.355 16.107 45.826 1.00 37.12 ? 30 PHE A CD1 1 ATOM 243 C CD2 . PHE A 1 30 ? 28.831 16.194 47.708 1.00 38.83 ? 30 PHE A CD2 1 ATOM 244 C CE1 . PHE A 1 30 ? 27.342 17.492 45.763 1.00 39.29 ? 30 PHE A CE1 1 ATOM 245 C CE2 . PHE A 1 30 ? 28.824 17.585 47.653 1.00 40.73 ? 30 PHE A CE2 1 ATOM 246 C CZ . PHE A 1 30 ? 28.077 18.235 46.678 1.00 39.66 ? 30 PHE A CZ 1 ATOM 247 N N . PHE A 1 31 ? 25.775 11.483 46.220 1.00 29.57 ? 31 PHE A N 1 ATOM 248 C CA . PHE A 1 31 ? 25.693 10.083 45.850 1.00 26.80 ? 31 PHE A CA 1 ATOM 249 C C . PHE A 1 31 ? 26.551 9.840 44.625 1.00 26.49 ? 31 PHE A C 1 ATOM 250 O O . PHE A 1 31 ? 26.600 10.666 43.709 1.00 26.31 ? 31 PHE A O 1 ATOM 251 C CB . PHE A 1 31 ? 24.264 9.664 45.534 1.00 25.42 ? 31 PHE A CB 1 ATOM 252 C CG . PHE A 1 31 ? 24.164 8.252 45.023 1.00 26.94 ? 31 PHE A CG 1 ATOM 253 C CD1 . PHE A 1 31 ? 24.293 7.974 43.666 1.00 26.30 ? 31 PHE A CD1 1 ATOM 254 C CD2 . PHE A 1 31 ? 23.975 7.192 45.903 1.00 25.29 ? 31 PHE A CD2 1 ATOM 255 C CE1 . PHE A 1 31 ? 24.235 6.664 43.193 1.00 26.44 ? 31 PHE A CE1 1 ATOM 256 C CE2 . PHE A 1 31 ? 23.916 5.879 45.437 1.00 26.20 ? 31 PHE A CE2 1 ATOM 257 C CZ . PHE A 1 31 ? 24.045 5.615 44.083 1.00 26.09 ? 31 PHE A CZ 1 ATOM 258 N N . PHE A 1 32 ? 27.225 8.700 44.600 1.00 26.01 ? 32 PHE A N 1 ATOM 259 C CA . PHE A 1 32 ? 28.067 8.371 43.467 1.00 26.19 ? 32 PHE A CA 1 ATOM 260 C C . PHE A 1 32 ? 28.084 6.868 43.259 1.00 26.51 ? 32 PHE A C 1 ATOM 261 O O . PHE A 1 32 ? 27.675 6.101 44.124 1.00 26.46 ? 32 PHE A O 1 ATOM 262 C CB . PHE A 1 32 ? 29.495 8.856 43.700 1.00 25.69 ? 32 PHE A CB 1 ATOM 263 C CG . PHE A 1 32 ? 30.217 8.081 44.749 1.00 28.78 ? 32 PHE A CG 1 ATOM 264 C CD1 . PHE A 1 32 ? 30.022 8.360 46.097 1.00 31.41 ? 32 PHE A CD1 1 ATOM 265 C CD2 . PHE A 1 32 ? 31.033 7.016 44.400 1.00 29.57 ? 32 PHE A CD2 1 ATOM 266 C CE1 . PHE A 1 32 ? 30.628 7.583 47.081 1.00 29.56 ? 32 PHE A CE1 1 ATOM 267 C CE2 . PHE A 1 32 ? 31.639 6.240 45.374 1.00 30.75 ? 32 PHE A CE2 1 ATOM 268 C CZ . PHE A 1 32 ? 31.433 6.526 46.719 1.00 30.15 ? 32 PHE A CZ 1 ATOM 269 N N . TRP A 1 33 ? 28.555 6.464 42.088 1.00 27.15 ? 33 TRP A N 1 ATOM 270 C CA . TRP A 1 33 ? 28.665 5.064 41.733 1.00 26.51 ? 33 TRP A CA 1 ATOM 271 C C . TRP A 1 33 ? 29.985 4.999 40.971 1.00 28.40 ? 33 TRP A C 1 ATOM 272 O O . TRP A 1 33 ? 30.207 5.772 40.034 1.00 28.61 ? 33 TRP A O 1 ATOM 273 C CB . TRP A 1 33 ? 27.508 4.637 40.831 1.00 23.65 ? 33 TRP A CB 1 ATOM 274 C CG . TRP A 1 33 ? 27.279 3.147 40.793 1.00 24.97 ? 33 TRP A CG 1 ATOM 275 C CD1 . TRP A 1 33 ? 28.236 2.165 40.795 1.00 23.62 ? 33 TRP A CD1 1 ATOM 276 C CD2 . TRP A 1 33 ? 26.010 2.467 40.712 1.00 23.44 ? 33 TRP A CD2 1 ATOM 277 N NE1 . TRP A 1 33 ? 27.644 0.927 40.718 1.00 23.06 ? 33 TRP A NE1 1 ATOM 278 C CE2 . TRP A 1 33 ? 26.282 1.080 40.664 1.00 23.69 ? 33 TRP A CE2 1 ATOM 279 C CE3 . TRP A 1 33 ? 24.675 2.897 40.675 1.00 21.70 ? 33 TRP A CE3 1 ATOM 280 C CZ2 . TRP A 1 33 ? 25.259 0.110 40.579 1.00 23.22 ? 33 TRP A CZ2 1 ATOM 281 C CZ3 . TRP A 1 33 ? 23.659 1.935 40.592 1.00 22.58 ? 33 TRP A CZ3 1 ATOM 282 C CH2 . TRP A 1 33 ? 23.962 0.556 40.545 1.00 22.74 ? 33 TRP A CH2 1 ATOM 283 N N . THR A 1 34 ? 30.858 4.089 41.395 1.00 29.04 ? 34 THR A N 1 ATOM 284 C CA . THR A 1 34 ? 32.168 3.907 40.787 1.00 30.70 ? 34 THR A CA 1 ATOM 285 C C . THR A 1 34 ? 32.315 2.536 40.138 1.00 30.69 ? 34 THR A C 1 ATOM 286 O O . THR A 1 34 ? 31.824 1.541 40.655 1.00 31.80 ? 34 THR A O 1 ATOM 287 C CB . THR A 1 34 ? 33.275 4.049 41.842 1.00 31.80 ? 34 THR A CB 1 ATOM 288 O OG1 . THR A 1 34 ? 33.306 5.396 42.323 1.00 35.56 ? 34 THR A OG1 1 ATOM 289 C CG2 . THR A 1 34 ? 34.629 3.701 41.245 1.00 33.86 ? 34 THR A CG2 1 ATOM 290 N N . PHE A 1 35 ? 33.001 2.494 39.004 1.00 29.07 ? 35 PHE A N 1 ATOM 291 C CA . PHE A 1 35 ? 33.239 1.246 38.294 1.00 29.10 ? 35 PHE A CA 1 ATOM 292 C C . PHE A 1 35 ? 34.701 1.214 37.894 1.00 29.66 ? 35 PHE A C 1 ATOM 293 O O . PHE A 1 35 ? 35.212 2.187 37.341 1.00 28.37 ? 35 PHE A O 1 ATOM 294 C CB . PHE A 1 35 ? 32.385 1.172 37.033 1.00 28.25 ? 35 PHE A CB 1 ATOM 295 C CG . PHE A 1 35 ? 30.937 0.951 37.298 1.00 27.92 ? 35 PHE A CG 1 ATOM 296 C CD1 . PHE A 1 35 ? 30.451 -0.327 37.530 1.00 27.13 ? 35 PHE A CD1 1 ATOM 297 C CD2 . PHE A 1 35 ? 30.045 2.025 37.293 1.00 28.24 ? 35 PHE A CD2 1 ATOM 298 C CE1 . PHE A 1 35 ? 29.094 -0.540 37.751 1.00 27.75 ? 35 PHE A CE1 1 ATOM 299 C CE2 . PHE A 1 35 ? 28.686 1.824 37.513 1.00 28.43 ? 35 PHE A CE2 1 ATOM 300 C CZ . PHE A 1 35 ? 28.208 0.539 37.741 1.00 26.98 ? 35 PHE A CZ 1 ATOM 301 N N . GLU A 1 36 ? 35.380 0.108 38.172 1.00 30.59 ? 36 GLU A N 1 ATOM 302 C CA . GLU A 1 36 ? 36.787 0.015 37.805 1.00 33.34 ? 36 GLU A CA 1 ATOM 303 C C . GLU A 1 36 ? 36.946 -0.411 36.360 1.00 33.09 ? 36 GLU A C 1 ATOM 304 O O . GLU A 1 36 ? 36.023 -0.965 35.762 1.00 33.90 ? 36 GLU A O 1 ATOM 305 C CB . GLU A 1 36 ? 37.515 -0.971 38.704 1.00 32.27 ? 36 GLU A CB 1 ATOM 306 C CG . GLU A 1 36 ? 37.412 -0.630 40.159 1.00 35.78 ? 36 GLU A CG 1 ATOM 307 C CD . GLU A 1 36 ? 38.393 -1.417 40.984 1.00 38.15 ? 36 GLU A CD 1 ATOM 308 O OE1 . GLU A 1 36 ? 38.577 -2.619 40.685 1.00 37.54 ? 36 GLU A OE1 1 ATOM 309 O OE2 . GLU A 1 36 ? 38.974 -0.835 41.927 1.00 39.52 ? 36 GLU A OE2 1 ATOM 310 N N . SER A 1 37 ? 38.115 -0.133 35.798 1.00 32.82 ? 37 SER A N 1 ATOM 311 C CA . SER A 1 37 ? 38.397 -0.506 34.421 1.00 33.81 ? 37 SER A CA 1 ATOM 312 C C . SER A 1 37 ? 38.266 -2.020 34.268 1.00 34.68 ? 37 SER A C 1 ATOM 313 O O . SER A 1 37 ? 38.684 -2.782 35.142 1.00 35.69 ? 37 SER A O 1 ATOM 314 C CB . SER A 1 37 ? 39.814 -0.073 34.037 1.00 33.18 ? 37 SER A CB 1 ATOM 315 O OG . SER A 1 37 ? 40.154 -0.540 32.743 1.00 33.02 ? 37 SER A OG 1 ATOM 316 N N . ARG A 1 38 ? 37.684 -2.460 33.159 1.00 34.40 ? 38 ARG A N 1 ATOM 317 C CA . ARG A 1 38 ? 37.526 -3.885 32.926 1.00 34.26 ? 38 ARG A CA 1 ATOM 318 C C . ARG A 1 38 ? 38.871 -4.450 32.516 1.00 34.55 ? 38 ARG A C 1 ATOM 319 O O . ARG A 1 38 ? 39.018 -5.641 32.276 1.00 35.20 ? 38 ARG A O 1 ATOM 320 C CB . ARG A 1 38 ? 36.463 -4.124 31.852 1.00 32.25 ? 38 ARG A CB 1 ATOM 321 C CG . ARG A 1 38 ? 35.124 -3.549 32.283 1.00 32.50 ? 38 ARG A CG 1 ATOM 322 C CD . ARG A 1 38 ? 33.941 -4.356 31.815 1.00 30.43 ? 38 ARG A CD 1 ATOM 323 N NE . ARG A 1 38 ? 33.512 -3.977 30.481 1.00 29.12 ? 38 ARG A NE 1 ATOM 324 C CZ . ARG A 1 38 ? 32.252 -3.696 30.157 1.00 29.27 ? 38 ARG A CZ 1 ATOM 325 N NH1 . ARG A 1 38 ? 31.293 -3.750 31.078 1.00 25.46 ? 38 ARG A NH1 1 ATOM 326 N NH2 . ARG A 1 38 ? 31.955 -3.353 28.910 1.00 29.07 ? 38 ARG A NH2 1 ATOM 327 N N . ASN A 1 39 ? 39.859 -3.569 32.469 1.00 36.55 ? 39 ASN A N 1 ATOM 328 C CA . ASN A 1 39 ? 41.216 -3.936 32.098 1.00 37.25 ? 39 ASN A CA 1 ATOM 329 C C . ASN A 1 39 ? 42.102 -3.904 33.338 1.00 36.65 ? 39 ASN A C 1 ATOM 330 O O . ASN A 1 39 ? 42.089 -4.840 34.130 1.00 36.67 ? 39 ASN A O 1 ATOM 331 C CB . ASN A 1 39 ? 41.738 -2.959 31.051 1.00 39.58 ? 39 ASN A CB 1 ATOM 332 C CG . ASN A 1 39 ? 43.070 -3.372 30.494 1.00 41.60 ? 39 ASN A CG 1 ATOM 333 O OD1 . ASN A 1 39 ? 43.711 -2.613 29.766 1.00 43.12 ? 39 ASN A OD1 1 ATOM 334 N ND2 . ASN A 1 39 ? 43.500 -4.584 30.827 1.00 41.87 ? 39 ASN A ND2 1 ATOM 335 N N . ASP A 1 40 ? 42.864 -2.828 33.513 1.00 36.96 ? 40 ASP A N 1 ATOM 336 C CA . ASP A 1 40 ? 43.742 -2.700 34.678 1.00 38.36 ? 40 ASP A CA 1 ATOM 337 C C . ASP A 1 40 ? 43.461 -1.414 35.452 1.00 36.99 ? 40 ASP A C 1 ATOM 338 O O . ASP A 1 40 ? 43.964 -0.349 35.103 1.00 36.28 ? 40 ASP A O 1 ATOM 339 C CB . ASP A 1 40 ? 45.208 -2.704 34.246 1.00 41.45 ? 40 ASP A CB 1 ATOM 340 C CG . ASP A 1 40 ? 46.155 -2.903 35.414 1.00 45.20 ? 40 ASP A CG 1 ATOM 341 O OD1 . ASP A 1 40 ? 45.759 -2.609 36.566 1.00 46.43 ? 40 ASP A OD1 1 ATOM 342 O OD2 . ASP A 1 40 ? 47.300 -3.346 35.180 1.00 48.05 ? 40 ASP A OD2 1 ATOM 343 N N . PRO A 1 41 ? 42.664 -1.499 36.526 1.00 37.33 ? 41 PRO A N 1 ATOM 344 C CA . PRO A 1 41 ? 42.336 -0.315 37.327 1.00 38.32 ? 41 PRO A CA 1 ATOM 345 C C . PRO A 1 41 ? 43.523 0.383 37.973 1.00 39.18 ? 41 PRO A C 1 ATOM 346 O O . PRO A 1 41 ? 43.400 1.509 38.452 1.00 40.43 ? 41 PRO A O 1 ATOM 347 C CB . PRO A 1 41 ? 41.339 -0.852 38.354 1.00 36.77 ? 41 PRO A CB 1 ATOM 348 C CG . PRO A 1 41 ? 41.724 -2.283 38.485 1.00 37.63 ? 41 PRO A CG 1 ATOM 349 C CD . PRO A 1 41 ? 41.989 -2.692 37.059 1.00 36.95 ? 41 PRO A CD 1 ATOM 350 N N . ALA A 1 42 ? 44.675 -0.271 37.978 1.00 40.35 ? 42 ALA A N 1 ATOM 351 C CA . ALA A 1 42 ? 45.859 0.328 38.579 1.00 41.75 ? 42 ALA A CA 1 ATOM 352 C C . ALA A 1 42 ? 46.661 1.128 37.557 1.00 42.21 ? 42 ALA A C 1 ATOM 353 O O . ALA A 1 42 ? 47.481 1.971 37.920 1.00 42.44 ? 42 ALA A O 1 ATOM 354 C CB . ALA A 1 42 ? 46.729 -0.754 39.205 1.00 40.75 ? 42 ALA A CB 1 ATOM 355 N N . LYS A 1 43 ? 46.406 0.870 36.279 1.00 42.58 ? 43 LYS A N 1 ATOM 356 C CA . LYS A 1 43 ? 47.111 1.557 35.202 1.00 42.73 ? 43 LYS A CA 1 ATOM 357 C C . LYS A 1 43 ? 46.199 2.525 34.456 1.00 41.06 ? 43 LYS A C 1 ATOM 358 O O . LYS A 1 43 ? 46.575 3.666 34.181 1.00 39.89 ? 43 LYS A O 1 ATOM 359 C CB . LYS A 1 43 ? 47.649 0.536 34.197 1.00 46.57 ? 43 LYS A CB 1 ATOM 360 C CG . LYS A 1 43 ? 48.555 -0.538 34.778 1.00 52.98 ? 43 LYS A CG 1 ATOM 361 C CD . LYS A 1 43 ? 50.023 -0.165 34.620 1.00 57.37 ? 43 LYS A CD 1 ATOM 362 C CE . LYS A 1 43 ? 50.931 -1.353 34.916 1.00 59.90 ? 43 LYS A CE 1 ATOM 363 N NZ . LYS A 1 43 ? 52.363 -1.047 34.617 1.00 61.39 ? 43 LYS A NZ 1 ATOM 364 N N . ASP A 1 44 ? 45.001 2.056 34.117 1.00 39.08 ? 44 ASP A N 1 ATOM 365 C CA . ASP A 1 44 ? 44.050 2.868 33.370 1.00 36.88 ? 44 ASP A CA 1 ATOM 366 C C . ASP A 1 44 ? 43.612 4.141 34.099 1.00 35.25 ? 44 ASP A C 1 ATOM 367 O O . ASP A 1 44 ? 43.564 4.194 35.331 1.00 36.14 ? 44 ASP A O 1 ATOM 368 C CB . ASP A 1 44 ? 42.831 2.023 32.977 1.00 36.74 ? 44 ASP A CB 1 ATOM 369 C CG . ASP A 1 44 ? 43.182 0.916 31.986 1.00 38.00 ? 44 ASP A CG 1 ATOM 370 O OD1 . ASP A 1 44 ? 44.035 1.151 31.104 1.00 38.81 ? 44 ASP A OD1 1 ATOM 371 O OD2 . ASP A 1 44 ? 42.598 -0.184 32.069 1.00 38.18 ? 44 ASP A OD2 1 ATOM 372 N N . PRO A 1 45 ? 43.286 5.191 33.335 1.00 32.17 ? 45 PRO A N 1 ATOM 373 C CA . PRO A 1 45 ? 42.860 6.457 33.923 1.00 30.59 ? 45 PRO A CA 1 ATOM 374 C C . PRO A 1 45 ? 41.475 6.434 34.562 1.00 30.12 ? 45 PRO A C 1 ATOM 375 O O . PRO A 1 45 ? 40.660 5.555 34.295 1.00 30.45 ? 45 PRO A O 1 ATOM 376 C CB . PRO A 1 45 ? 42.947 7.419 32.743 1.00 31.24 ? 45 PRO A CB 1 ATOM 377 C CG . PRO A 1 45 ? 42.570 6.555 31.595 1.00 31.53 ? 45 PRO A CG 1 ATOM 378 C CD . PRO A 1 45 ? 43.324 5.279 31.864 1.00 31.36 ? 45 PRO A CD 1 ATOM 379 N N . VAL A 1 46 ? 41.231 7.416 35.423 1.00 29.13 ? 46 VAL A N 1 ATOM 380 C CA . VAL A 1 46 ? 39.962 7.560 36.107 1.00 26.84 ? 46 VAL A CA 1 ATOM 381 C C . VAL A 1 46 ? 39.177 8.659 35.387 1.00 27.40 ? 46 VAL A C 1 ATOM 382 O O . VAL A 1 46 ? 39.745 9.687 35.005 1.00 25.78 ? 46 VAL A O 1 ATOM 383 C CB . VAL A 1 46 ? 40.191 7.962 37.572 1.00 27.47 ? 46 VAL A CB 1 ATOM 384 C CG1 . VAL A 1 46 ? 38.870 8.196 38.274 1.00 28.14 ? 46 VAL A CG1 1 ATOM 385 C CG2 . VAL A 1 46 ? 40.968 6.872 38.277 1.00 27.78 ? 46 VAL A CG2 1 ATOM 386 N N . ILE A 1 47 ? 37.881 8.432 35.185 1.00 26.50 ? 47 ILE A N 1 ATOM 387 C CA . ILE A 1 47 ? 37.031 9.414 34.518 1.00 25.63 ? 47 ILE A CA 1 ATOM 388 C C . ILE A 1 47 ? 35.789 9.760 35.345 1.00 25.95 ? 47 ILE A C 1 ATOM 389 O O . ILE A 1 47 ? 35.066 8.867 35.798 1.00 26.24 ? 47 ILE A O 1 ATOM 390 C CB . ILE A 1 47 ? 36.544 8.899 33.149 1.00 25.42 ? 47 ILE A CB 1 ATOM 391 C CG1 . ILE A 1 47 ? 37.732 8.695 32.210 1.00 24.88 ? 47 ILE A CG1 1 ATOM 392 C CG2 . ILE A 1 47 ? 35.539 9.880 32.546 1.00 22.23 ? 47 ILE A CG2 1 ATOM 393 C CD1 . ILE A 1 47 ? 37.339 8.047 30.883 1.00 24.15 ? 47 ILE A CD1 1 ATOM 394 N N . LEU A 1 48 ? 35.557 11.054 35.543 1.00 23.31 ? 48 LEU A N 1 ATOM 395 C CA . LEU A 1 48 ? 34.379 11.525 36.266 1.00 24.05 ? 48 LEU A CA 1 ATOM 396 C C . LEU A 1 48 ? 33.357 11.943 35.206 1.00 24.35 ? 48 LEU A C 1 ATOM 397 O O . LEU A 1 48 ? 33.645 12.801 34.361 1.00 25.43 ? 48 LEU A O 1 ATOM 398 C CB . LEU A 1 48 ? 34.722 12.734 37.151 1.00 22.20 ? 48 LEU A CB 1 ATOM 399 C CG . LEU A 1 48 ? 33.524 13.459 37.787 1.00 21.44 ? 48 LEU A CG 1 ATOM 400 C CD1 . LEU A 1 48 ? 32.781 12.497 38.712 1.00 21.43 ? 48 LEU A CD1 1 ATOM 401 C CD2 . LEU A 1 48 ? 33.991 14.696 38.561 1.00 19.70 ? 48 LEU A CD2 1 ATOM 402 N N . TRP A 1 49 ? 32.177 11.332 35.229 1.00 24.07 ? 49 TRP A N 1 ATOM 403 C CA . TRP A 1 49 ? 31.142 11.674 34.252 1.00 24.25 ? 49 TRP A CA 1 ATOM 404 C C . TRP A 1 49 ? 30.039 12.559 34.838 1.00 23.48 ? 49 TRP A C 1 ATOM 405 O O . TRP A 1 49 ? 29.523 12.285 35.921 1.00 22.51 ? 49 TRP A O 1 ATOM 406 C CB . TRP A 1 49 ? 30.518 10.409 33.655 1.00 24.73 ? 49 TRP A CB 1 ATOM 407 C CG . TRP A 1 49 ? 29.367 10.732 32.763 1.00 25.30 ? 49 TRP A CG 1 ATOM 408 C CD1 . TRP A 1 49 ? 28.039 10.699 33.088 1.00 22.94 ? 49 TRP A CD1 1 ATOM 409 C CD2 . TRP A 1 49 ? 29.442 11.259 31.433 1.00 25.74 ? 49 TRP A CD2 1 ATOM 410 N NE1 . TRP A 1 49 ? 27.285 11.179 32.047 1.00 22.72 ? 49 TRP A NE1 1 ATOM 411 C CE2 . TRP A 1 49 ? 28.117 11.532 31.017 1.00 25.00 ? 49 TRP A CE2 1 ATOM 412 C CE3 . TRP A 1 49 ? 30.502 11.533 30.553 1.00 23.35 ? 49 TRP A CE3 1 ATOM 413 C CZ2 . TRP A 1 49 ? 27.821 12.068 29.755 1.00 23.77 ? 49 TRP A CZ2 1 ATOM 414 C CZ3 . TRP A 1 49 ? 30.208 12.067 29.299 1.00 23.98 ? 49 TRP A CZ3 1 ATOM 415 C CH2 . TRP A 1 49 ? 28.875 12.330 28.914 1.00 23.68 ? 49 TRP A CH2 1 ATOM 416 N N . LEU A 1 50 ? 29.679 13.614 34.110 1.00 23.43 ? 50 LEU A N 1 ATOM 417 C CA . LEU A 1 50 ? 28.647 14.544 34.559 1.00 24.85 ? 50 LEU A CA 1 ATOM 418 C C . LEU A 1 50 ? 27.590 14.821 33.497 1.00 25.43 ? 50 LEU A C 1 ATOM 419 O O . LEU A 1 50 ? 27.928 15.176 32.372 1.00 27.03 ? 50 LEU A O 1 ATOM 420 C CB . LEU A 1 50 ? 29.270 15.889 34.947 1.00 24.82 ? 50 LEU A CB 1 ATOM 421 C CG . LEU A 1 50 ? 30.322 15.944 36.056 1.00 27.76 ? 50 LEU A CG 1 ATOM 422 C CD1 . LEU A 1 50 ? 30.739 17.389 36.280 1.00 23.91 ? 50 LEU A CD1 1 ATOM 423 C CD2 . LEU A 1 50 ? 29.756 15.352 37.334 1.00 27.08 ? 50 LEU A CD2 1 ATOM 424 N N . ASN A 1 51 ? 26.314 14.658 33.838 1.00 24.89 ? 51 ASN A N 1 ATOM 425 C CA . ASN A 1 51 ? 25.268 14.986 32.876 1.00 24.34 ? 51 ASN A CA 1 ATOM 426 C C . ASN A 1 51 ? 24.922 16.453 33.110 1.00 25.31 ? 51 ASN A C 1 ATOM 427 O O . ASN A 1 51 ? 25.444 17.070 34.042 1.00 23.83 ? 51 ASN A O 1 ATOM 428 C CB . ASN A 1 51 ? 24.032 14.104 33.053 1.00 24.03 ? 51 ASN A CB 1 ATOM 429 C CG . ASN A 1 51 ? 24.189 12.738 32.388 1.00 24.24 ? 51 ASN A CG 1 ATOM 430 O OD1 . ASN A 1 51 ? 24.652 11.781 33.005 1.00 25.17 ? 51 ASN A OD1 1 ATOM 431 N ND2 . ASN A 1 51 ? 23.819 12.653 31.119 1.00 21.70 ? 51 ASN A ND2 1 ATOM 432 N N . GLY A 1 52 ? 24.059 17.017 32.269 1.00 25.74 ? 52 GLY A N 1 ATOM 433 C CA . GLY A 1 52 ? 23.709 18.419 32.419 1.00 25.60 ? 52 GLY A CA 1 ATOM 434 C C . GLY A 1 52 ? 22.352 18.711 33.031 1.00 26.50 ? 52 GLY A C 1 ATOM 435 O O . GLY A 1 52 ? 22.067 18.325 34.164 1.00 27.43 ? 52 GLY A O 1 ATOM 436 N N . GLY A 1 53 ? 21.514 19.401 32.264 1.00 27.62 ? 53 GLY A N 1 ATOM 437 C CA . GLY A 1 53 ? 20.183 19.765 32.716 1.00 27.35 ? 53 GLY A CA 1 ATOM 438 C C . GLY A 1 53 ? 19.971 21.263 32.560 1.00 27.43 ? 53 GLY A C 1 ATOM 439 O O . GLY A 1 53 ? 19.458 21.713 31.536 1.00 27.89 ? 53 GLY A O 1 ATOM 440 N N . PRO A 1 54 ? 20.371 22.067 33.556 1.00 25.08 ? 54 PRO A N 1 ATOM 441 C CA . PRO A 1 54 ? 20.999 21.578 34.786 1.00 24.30 ? 54 PRO A CA 1 ATOM 442 C C . PRO A 1 54 ? 19.983 20.951 35.741 1.00 25.98 ? 54 PRO A C 1 ATOM 443 O O . PRO A 1 54 ? 18.822 21.374 35.790 1.00 26.96 ? 54 PRO A O 1 ATOM 444 C CB . PRO A 1 54 ? 21.651 22.834 35.363 1.00 24.31 ? 54 PRO A CB 1 ATOM 445 C CG . PRO A 1 54 ? 20.732 23.931 34.906 1.00 25.16 ? 54 PRO A CG 1 ATOM 446 C CD . PRO A 1 54 ? 20.411 23.537 33.483 1.00 23.74 ? 54 PRO A CD 1 ATOM 447 N N . GLY A 1 55 ? 20.426 19.944 36.494 1.00 25.31 ? 55 GLY A N 1 ATOM 448 C CA . GLY A 1 55 ? 19.553 19.278 37.437 1.00 22.50 ? 55 GLY A CA 1 ATOM 449 C C . GLY A 1 55 ? 19.280 17.822 37.098 1.00 23.13 ? 55 GLY A C 1 ATOM 450 O O . GLY A 1 55 ? 18.416 17.192 37.710 1.00 23.04 ? 55 GLY A O 1 ATOM 451 N N . CYS A 1 56 ? 19.997 17.278 36.122 1.00 21.90 ? 56 CYS A N 1 ATOM 452 C CA . CYS A 1 56 ? 19.798 15.881 35.759 1.00 22.52 ? 56 CYS A CA 1 ATOM 453 C C . CYS A 1 56 ? 20.865 14.938 36.335 1.00 23.17 ? 56 CYS A C 1 ATOM 454 O O . CYS A 1 56 ? 22.038 15.296 36.475 1.00 24.57 ? 56 CYS A O 1 ATOM 455 C CB . CYS A 1 56 ? 19.743 15.740 34.247 1.00 22.32 ? 56 CYS A CB 1 ATOM 456 S SG . CYS A 1 56 ? 18.386 16.664 33.454 1.00 24.71 ? 56 CYS A SG 1 ATOM 457 N N . SER A 1 57 ? 20.436 13.725 36.668 1.00 23.78 ? 57 SER A N 1 ATOM 458 C CA . SER A 1 57 ? 21.299 12.700 37.248 1.00 21.97 ? 57 SER A CA 1 ATOM 459 C C . SER A 1 57 ? 22.324 12.121 36.282 1.00 21.73 ? 57 SER A C 1 ATOM 460 O O . SER A 1 57 ? 22.054 11.948 35.092 1.00 20.40 ? 57 SER A O 1 ATOM 461 C CB . SER A 1 57 ? 20.438 11.562 37.794 1.00 20.98 ? 57 SER A CB 1 ATOM 462 O OG . SER A 1 57 ? 21.232 10.458 38.187 1.00 22.29 ? 57 SER A OG 1 ATOM 463 N N . SER A 1 58 ? 23.503 11.810 36.808 1.00 20.85 ? 58 SER A N 1 ATOM 464 C CA . SER A 1 58 ? 24.549 11.228 35.989 1.00 20.85 ? 58 SER A CA 1 ATOM 465 C C . SER A 1 58 ? 24.287 9.746 35.784 1.00 21.52 ? 58 SER A C 1 ATOM 466 O O . SER A 1 58 ? 24.998 9.084 35.033 1.00 21.54 ? 58 SER A O 1 ATOM 467 C CB . SER A 1 58 ? 25.912 11.432 36.637 1.00 20.15 ? 58 SER A CB 1 ATOM 468 O OG . SER A 1 58 ? 26.351 12.765 36.444 1.00 20.59 ? 58 SER A OG 1 ATOM 469 N N . LEU A 1 59 ? 23.263 9.222 36.452 1.00 21.90 ? 59 LEU A N 1 ATOM 470 C CA . LEU A 1 59 ? 22.932 7.814 36.297 1.00 22.31 ? 59 LEU A CA 1 ATOM 471 C C . LEU A 1 59 ? 22.291 7.617 34.929 1.00 23.28 ? 59 LEU A C 1 ATOM 472 O O . LEU A 1 59 ? 22.136 6.494 34.446 1.00 24.23 ? 59 LEU A O 1 ATOM 473 C CB . LEU A 1 59 ? 22.005 7.352 37.424 1.00 20.47 ? 59 LEU A CB 1 ATOM 474 C CG . LEU A 1 59 ? 22.646 7.484 38.813 1.00 21.18 ? 59 LEU A CG 1 ATOM 475 C CD1 . LEU A 1 59 ? 21.783 6.789 39.867 1.00 21.84 ? 59 LEU A CD1 1 ATOM 476 C CD2 . LEU A 1 59 ? 24.032 6.868 38.790 1.00 20.69 ? 59 LEU A CD2 1 ATOM 477 N N . THR A 1 60 ? 21.931 8.725 34.297 1.00 24.73 ? 60 THR A N 1 ATOM 478 C CA . THR A 1 60 ? 21.342 8.674 32.970 1.00 26.58 ? 60 THR A CA 1 ATOM 479 C C . THR A 1 60 ? 22.454 8.226 32.039 1.00 25.81 ? 60 THR A C 1 ATOM 480 O O . THR A 1 60 ? 22.271 7.332 31.225 1.00 26.45 ? 60 THR A O 1 ATOM 481 C CB . THR A 1 60 ? 20.845 10.068 32.519 1.00 27.78 ? 60 THR A CB 1 ATOM 482 O OG1 . THR A 1 60 ? 19.833 10.526 33.421 1.00 33.20 ? 60 THR A OG1 1 ATOM 483 C CG2 . THR A 1 60 ? 20.273 10.008 31.115 1.00 26.73 ? 60 THR A CG2 1 ATOM 484 N N . GLY A 1 61 ? 23.616 8.856 32.172 1.00 25.67 ? 61 GLY A N 1 ATOM 485 C CA . GLY A 1 61 ? 24.740 8.503 31.328 1.00 26.56 ? 61 GLY A CA 1 ATOM 486 C C . GLY A 1 61 ? 25.180 7.071 31.557 1.00 26.30 ? 61 GLY A C 1 ATOM 487 O O . GLY A 1 61 ? 25.641 6.389 30.643 1.00 28.54 ? 61 GLY A O 1 ATOM 488 N N . LEU A 1 62 ? 25.024 6.612 32.789 1.00 25.21 ? 62 LEU A N 1 ATOM 489 C CA . LEU A 1 62 ? 25.407 5.263 33.164 1.00 24.77 ? 62 LEU A CA 1 ATOM 490 C C . LEU A 1 62 ? 24.549 4.198 32.474 1.00 25.03 ? 62 LEU A C 1 ATOM 491 O O . LEU A 1 62 ? 25.063 3.351 31.741 1.00 23.36 ? 62 LEU A O 1 ATOM 492 C CB . LEU A 1 62 ? 25.301 5.118 34.689 1.00 24.75 ? 62 LEU A CB 1 ATOM 493 C CG . LEU A 1 62 ? 25.873 3.890 35.406 1.00 26.16 ? 62 LEU A CG 1 ATOM 494 C CD1 . LEU A 1 62 ? 25.679 4.062 36.915 1.00 25.66 ? 62 LEU A CD1 1 ATOM 495 C CD2 . LEU A 1 62 ? 25.179 2.622 34.934 1.00 26.94 ? 62 LEU A CD2 1 ATOM 496 N N . PHE A 1 63 ? 23.239 4.253 32.705 1.00 25.06 ? 63 PHE A N 1 ATOM 497 C CA . PHE A 1 63 ? 22.316 3.265 32.158 1.00 24.06 ? 63 PHE A CA 1 ATOM 498 C C . PHE A 1 63 ? 21.843 3.483 30.735 1.00 24.85 ? 63 PHE A C 1 ATOM 499 O O . PHE A 1 63 ? 21.551 2.525 30.021 1.00 26.32 ? 63 PHE A O 1 ATOM 500 C CB . PHE A 1 63 ? 21.093 3.149 33.068 1.00 23.11 ? 63 PHE A CB 1 ATOM 501 C CG . PHE A 1 63 ? 21.391 2.547 34.421 1.00 24.04 ? 63 PHE A CG 1 ATOM 502 C CD1 . PHE A 1 63 ? 21.759 1.206 34.537 1.00 22.67 ? 63 PHE A CD1 1 ATOM 503 C CD2 . PHE A 1 63 ? 21.305 3.317 35.576 1.00 21.24 ? 63 PHE A CD2 1 ATOM 504 C CE1 . PHE A 1 63 ? 22.035 0.638 35.779 1.00 21.00 ? 63 PHE A CE1 1 ATOM 505 C CE2 . PHE A 1 63 ? 21.579 2.758 36.822 1.00 23.90 ? 63 PHE A CE2 1 ATOM 506 C CZ . PHE A 1 63 ? 21.947 1.406 36.921 1.00 21.68 ? 63 PHE A CZ 1 ATOM 507 N N . PHE A 1 64 ? 21.784 4.739 30.319 1.00 25.12 ? 64 PHE A N 1 ATOM 508 C CA . PHE A 1 64 ? 21.287 5.097 28.998 1.00 24.30 ? 64 PHE A CA 1 ATOM 509 C C . PHE A 1 64 ? 22.345 5.396 27.941 1.00 25.43 ? 64 PHE A C 1 ATOM 510 O O . PHE A 1 64 ? 22.104 5.181 26.760 1.00 25.96 ? 64 PHE A O 1 ATOM 511 C CB . PHE A 1 64 ? 20.383 6.317 29.146 1.00 25.84 ? 64 PHE A CB 1 ATOM 512 C CG . PHE A 1 64 ? 19.458 6.550 27.996 1.00 27.76 ? 64 PHE A CG 1 ATOM 513 C CD1 . PHE A 1 64 ? 18.376 5.706 27.776 1.00 29.70 ? 64 PHE A CD1 1 ATOM 514 C CD2 . PHE A 1 64 ? 19.625 7.654 27.171 1.00 29.35 ? 64 PHE A CD2 1 ATOM 515 C CE1 . PHE A 1 64 ? 17.470 5.962 26.755 1.00 30.55 ? 64 PHE A CE1 1 ATOM 516 C CE2 . PHE A 1 64 ? 18.726 7.925 26.145 1.00 31.57 ? 64 PHE A CE2 1 ATOM 517 C CZ . PHE A 1 64 ? 17.643 7.076 25.938 1.00 32.43 ? 64 PHE A CZ 1 ATOM 518 N N . GLU A 1 65 ? 23.516 5.872 28.349 1.00 26.11 ? 65 GLU A N 1 ATOM 519 C CA . GLU A 1 65 ? 24.527 6.248 27.365 1.00 27.09 ? 65 GLU A CA 1 ATOM 520 C C . GLU A 1 65 ? 25.832 5.471 27.244 1.00 28.36 ? 65 GLU A C 1 ATOM 521 O O . GLU A 1 65 ? 26.101 4.858 26.203 1.00 28.05 ? 65 GLU A O 1 ATOM 522 C CB . GLU A 1 65 ? 24.906 7.726 27.548 1.00 25.41 ? 65 GLU A CB 1 ATOM 523 C CG . GLU A 1 65 ? 23.745 8.689 27.623 1.00 25.03 ? 65 GLU A CG 1 ATOM 524 C CD . GLU A 1 65 ? 24.195 10.139 27.717 1.00 25.00 ? 65 GLU A CD 1 ATOM 525 O OE1 . GLU A 1 65 ? 24.780 10.646 26.736 1.00 25.98 ? 65 GLU A OE1 1 ATOM 526 O OE2 . GLU A 1 65 ? 23.967 10.770 28.769 1.00 23.16 ? 65 GLU A OE2 1 ATOM 527 N N . LEU A 1 66 ? 26.646 5.512 28.298 1.00 27.57 ? 66 LEU A N 1 ATOM 528 C CA . LEU A 1 66 ? 27.966 4.900 28.245 1.00 28.75 ? 66 LEU A CA 1 ATOM 529 C C . LEU A 1 66 ? 28.426 3.995 29.380 1.00 28.59 ? 66 LEU A C 1 ATOM 530 O O . LEU A 1 66 ? 29.596 3.609 29.412 1.00 29.00 ? 66 LEU A O 1 ATOM 531 C CB . LEU A 1 66 ? 28.993 6.021 28.052 1.00 27.86 ? 66 LEU A CB 1 ATOM 532 C CG . LEU A 1 66 ? 28.865 7.154 29.080 1.00 28.72 ? 66 LEU A CG 1 ATOM 533 C CD1 . LEU A 1 66 ? 29.776 6.872 30.257 1.00 26.79 ? 66 LEU A CD1 1 ATOM 534 C CD2 . LEU A 1 66 ? 29.226 8.495 28.446 1.00 30.35 ? 66 LEU A CD2 1 ATOM 535 N N . GLY A 1 67 ? 27.531 3.657 30.302 1.00 28.60 ? 67 GLY A N 1 ATOM 536 C CA . GLY A 1 67 ? 27.902 2.792 31.413 1.00 26.92 ? 67 GLY A CA 1 ATOM 537 C C . GLY A 1 67 ? 27.900 1.309 31.065 1.00 26.44 ? 67 GLY A C 1 ATOM 538 O O . GLY A 1 67 ? 27.453 0.933 29.981 1.00 25.49 ? 67 GLY A O 1 ATOM 539 N N . PRO A 1 68 ? 28.383 0.441 31.975 1.00 27.29 ? 68 PRO A N 1 ATOM 540 C CA . PRO A 1 68 ? 28.469 -1.022 31.820 1.00 27.75 ? 68 PRO A CA 1 ATOM 541 C C . PRO A 1 68 ? 27.179 -1.785 31.507 1.00 28.49 ? 68 PRO A C 1 ATOM 542 O O . PRO A 1 68 ? 27.225 -2.890 30.967 1.00 28.86 ? 68 PRO A O 1 ATOM 543 C CB . PRO A 1 68 ? 29.108 -1.476 33.135 1.00 27.16 ? 68 PRO A CB 1 ATOM 544 C CG . PRO A 1 68 ? 28.714 -0.410 34.106 1.00 26.93 ? 68 PRO A CG 1 ATOM 545 C CD . PRO A 1 68 ? 28.898 0.846 33.296 1.00 26.96 ? 68 PRO A CD 1 ATOM 546 N N . SER A 1 69 ? 26.032 -1.214 31.853 1.00 28.24 ? 69 SER A N 1 ATOM 547 C CA . SER A 1 69 ? 24.764 -1.873 31.564 1.00 29.37 ? 69 SER A CA 1 ATOM 548 C C . SER A 1 69 ? 23.658 -0.882 31.265 1.00 29.94 ? 69 SER A C 1 ATOM 549 O O . SER A 1 69 ? 23.662 0.247 31.759 1.00 30.34 ? 69 SER A O 1 ATOM 550 C CB . SER A 1 69 ? 24.315 -2.749 32.737 1.00 30.61 ? 69 SER A CB 1 ATOM 551 O OG . SER A 1 69 ? 24.983 -3.995 32.757 1.00 32.87 ? 69 SER A OG 1 ATOM 552 N N . SER A 1 70 ? 22.715 -1.305 30.434 1.00 29.85 ? 70 SER A N 1 ATOM 553 C CA . SER A 1 70 ? 21.564 -0.476 30.120 1.00 31.07 ? 70 SER A CA 1 ATOM 554 C C . SER A 1 70 ? 20.425 -1.264 30.740 1.00 30.01 ? 70 SER A C 1 ATOM 555 O O . SER A 1 70 ? 20.649 -2.359 31.255 1.00 29.68 ? 70 SER A O 1 ATOM 556 C CB . SER A 1 70 ? 21.359 -0.354 28.617 1.00 29.61 ? 70 SER A CB 1 ATOM 557 O OG . SER A 1 70 ? 21.017 -1.610 28.076 1.00 35.14 ? 70 SER A OG 1 ATOM 558 N N . ILE A 1 71 ? 19.212 -0.734 30.689 1.00 29.56 ? 71 ILE A N 1 ATOM 559 C CA . ILE A 1 71 ? 18.093 -1.436 31.292 1.00 30.83 ? 71 ILE A CA 1 ATOM 560 C C . ILE A 1 71 ? 16.974 -1.783 30.327 1.00 30.42 ? 71 ILE A C 1 ATOM 561 O O . ILE A 1 71 ? 16.451 -0.926 29.633 1.00 29.35 ? 71 ILE A O 1 ATOM 562 C CB . ILE A 1 71 ? 17.549 -0.621 32.485 1.00 31.88 ? 71 ILE A CB 1 ATOM 563 C CG1 . ILE A 1 71 ? 18.609 -0.611 33.592 1.00 32.77 ? 71 ILE A CG1 1 ATOM 564 C CG2 . ILE A 1 71 ? 16.243 -1.215 32.998 1.00 29.01 ? 71 ILE A CG2 1 ATOM 565 C CD1 . ILE A 1 71 ? 18.414 0.475 34.609 1.00 38.14 ? 71 ILE A CD1 1 ATOM 566 N N . GLY A 1 72 ? 16.610 -3.060 30.302 1.00 31.80 ? 72 GLY A N 1 ATOM 567 C CA . GLY A 1 72 ? 15.553 -3.515 29.419 1.00 34.63 ? 72 GLY A CA 1 ATOM 568 C C . GLY A 1 72 ? 14.145 -3.214 29.901 1.00 35.99 ? 72 GLY A C 1 ATOM 569 O O . GLY A 1 72 ? 13.941 -2.808 31.041 1.00 36.06 ? 72 GLY A O 1 ATOM 570 N N . PRO A 1 73 ? 13.141 -3.408 29.039 1.00 38.18 ? 73 PRO A N 1 ATOM 571 C CA . PRO A 1 73 ? 11.733 -3.161 29.364 1.00 38.33 ? 73 PRO A CA 1 ATOM 572 C C . PRO A 1 73 ? 11.246 -3.955 30.568 1.00 37.68 ? 73 PRO A C 1 ATOM 573 O O . PRO A 1 73 ? 10.243 -3.601 31.184 1.00 38.76 ? 73 PRO A O 1 ATOM 574 C CB . PRO A 1 73 ? 11.010 -3.568 28.083 1.00 38.10 ? 73 PRO A CB 1 ATOM 575 C CG . PRO A 1 73 ? 12.004 -3.224 27.021 1.00 38.93 ? 73 PRO A CG 1 ATOM 576 C CD . PRO A 1 73 ? 13.288 -3.766 27.616 1.00 39.65 ? 73 PRO A CD 1 ATOM 577 N N . ASP A 1 74 ? 11.961 -5.026 30.894 1.00 37.15 ? 74 ASP A N 1 ATOM 578 C CA . ASP A 1 74 ? 11.609 -5.895 32.013 1.00 36.51 ? 74 ASP A CA 1 ATOM 579 C C . ASP A 1 74 ? 12.395 -5.564 33.275 1.00 37.04 ? 74 ASP A C 1 ATOM 580 O O . ASP A 1 74 ? 12.407 -6.346 34.232 1.00 38.19 ? 74 ASP A O 1 ATOM 581 C CB . ASP A 1 74 ? 11.871 -7.340 31.621 1.00 38.29 ? 74 ASP A CB 1 ATOM 582 C CG . ASP A 1 74 ? 13.323 -7.588 31.282 1.00 41.36 ? 74 ASP A CG 1 ATOM 583 O OD1 . ASP A 1 74 ? 14.015 -6.634 30.863 1.00 42.33 ? 74 ASP A OD1 1 ATOM 584 O OD2 . ASP A 1 74 ? 13.774 -8.742 31.426 1.00 45.80 ? 74 ASP A OD2 1 ATOM 585 N N . LEU A 1 75 ? 13.064 -4.414 33.258 1.00 35.88 ? 75 LEU A N 1 ATOM 586 C CA . LEU A 1 75 ? 13.858 -3.935 34.384 1.00 34.17 ? 75 LEU A CA 1 ATOM 587 C C . LEU A 1 75 ? 15.072 -4.790 34.714 1.00 34.22 ? 75 LEU A C 1 ATOM 588 O O . LEU A 1 75 ? 15.557 -4.780 35.840 1.00 34.63 ? 75 LEU A O 1 ATOM 589 C CB . LEU A 1 75 ? 12.967 -3.775 35.621 1.00 32.66 ? 75 LEU A CB 1 ATOM 590 C CG . LEU A 1 75 ? 12.170 -2.462 35.714 1.00 33.45 ? 75 LEU A CG 1 ATOM 591 C CD1 . LEU A 1 75 ? 11.517 -2.154 34.387 1.00 32.30 ? 75 LEU A CD1 1 ATOM 592 C CD2 . LEU A 1 75 ? 11.130 -2.552 36.820 1.00 29.96 ? 75 LEU A CD2 1 ATOM 593 N N . LYS A 1 76 ? 15.572 -5.527 33.731 1.00 34.91 ? 76 LYS A N 1 ATOM 594 C CA . LYS A 1 76 ? 16.749 -6.360 33.949 1.00 35.27 ? 76 LYS A CA 1 ATOM 595 C C . LYS A 1 76 ? 17.936 -5.737 33.229 1.00 33.73 ? 76 LYS A C 1 ATOM 596 O O . LYS A 1 76 ? 17.836 -5.347 32.067 1.00 34.82 ? 76 LYS A O 1 ATOM 597 C CB . LYS A 1 76 ? 16.516 -7.776 33.417 1.00 39.08 ? 76 LYS A CB 1 ATOM 598 C CG . LYS A 1 76 ? 15.265 -8.437 33.947 1.00 45.37 ? 76 LYS A CG 1 ATOM 599 C CD . LYS A 1 76 ? 15.241 -8.447 35.469 1.00 51.68 ? 76 LYS A CD 1 ATOM 600 C CE . LYS A 1 76 ? 13.906 -8.968 35.990 1.00 55.43 ? 76 LYS A CE 1 ATOM 601 N NZ . LYS A 1 76 ? 13.615 -10.348 35.494 1.00 58.08 ? 76 LYS A NZ 1 ATOM 602 N N . PRO A 1 77 ? 19.080 -5.623 33.912 1.00 32.73 ? 77 PRO A N 1 ATOM 603 C CA . PRO A 1 77 ? 20.250 -5.030 33.260 1.00 31.39 ? 77 PRO A CA 1 ATOM 604 C C . PRO A 1 77 ? 20.769 -5.855 32.087 1.00 30.19 ? 77 PRO A C 1 ATOM 605 O O . PRO A 1 77 ? 20.718 -7.082 32.104 1.00 30.40 ? 77 PRO A O 1 ATOM 606 C CB . PRO A 1 77 ? 21.266 -4.939 34.398 1.00 30.42 ? 77 PRO A CB 1 ATOM 607 C CG . PRO A 1 77 ? 20.911 -6.098 35.259 1.00 31.35 ? 77 PRO A CG 1 ATOM 608 C CD . PRO A 1 77 ? 19.395 -6.020 35.294 1.00 32.16 ? 77 PRO A CD 1 ATOM 609 N N . ILE A 1 78 ? 21.261 -5.160 31.069 1.00 29.11 ? 78 ILE A N 1 ATOM 610 C CA . ILE A 1 78 ? 21.828 -5.787 29.880 1.00 28.20 ? 78 ILE A CA 1 ATOM 611 C C . ILE A 1 78 ? 23.245 -5.229 29.742 1.00 27.49 ? 78 ILE A C 1 ATOM 612 O O . ILE A 1 78 ? 23.437 -4.014 29.687 1.00 28.78 ? 78 ILE A O 1 ATOM 613 C CB . ILE A 1 78 ? 21.023 -5.423 28.617 1.00 28.03 ? 78 ILE A CB 1 ATOM 614 C CG1 . ILE A 1 78 ? 19.560 -5.815 28.801 1.00 28.93 ? 78 ILE A CG1 1 ATOM 615 C CG2 . ILE A 1 78 ? 21.592 -6.140 27.418 1.00 26.68 ? 78 ILE A CG2 1 ATOM 616 C CD1 . ILE A 1 78 ? 18.638 -5.265 27.730 1.00 27.69 ? 78 ILE A CD1 1 ATOM 617 N N . GLY A 1 79 ? 24.235 -6.110 29.694 1.00 25.92 ? 79 GLY A N 1 ATOM 618 C CA . GLY A 1 79 ? 25.608 -5.656 29.586 1.00 25.93 ? 79 GLY A CA 1 ATOM 619 C C . GLY A 1 79 ? 25.903 -4.828 28.353 1.00 26.58 ? 79 GLY A C 1 ATOM 620 O O . GLY A 1 79 ? 25.415 -5.118 27.266 1.00 28.71 ? 79 GLY A O 1 ATOM 621 N N . ASN A 1 80 ? 26.701 -3.782 28.524 1.00 26.86 ? 80 ASN A N 1 ATOM 622 C CA . ASN A 1 80 ? 27.090 -2.918 27.416 1.00 26.05 ? 80 ASN A CA 1 ATOM 623 C C . ASN A 1 80 ? 28.550 -3.249 27.113 1.00 27.42 ? 80 ASN A C 1 ATOM 624 O O . ASN A 1 80 ? 29.427 -3.002 27.929 1.00 26.91 ? 80 ASN A O 1 ATOM 625 C CB . ASN A 1 80 ? 26.933 -1.451 27.824 1.00 22.20 ? 80 ASN A CB 1 ATOM 626 C CG . ASN A 1 80 ? 27.410 -0.491 26.756 1.00 20.96 ? 80 ASN A CG 1 ATOM 627 O OD1 . ASN A 1 80 ? 27.520 -0.847 25.583 1.00 20.26 ? 80 ASN A OD1 1 ATOM 628 N ND2 . ASN A 1 80 ? 27.684 0.742 27.157 1.00 20.94 ? 80 ASN A ND2 1 ATOM 629 N N . PRO A 1 81 ? 28.825 -3.832 25.937 1.00 30.59 ? 81 PRO A N 1 ATOM 630 C CA . PRO A 1 81 ? 30.207 -4.187 25.582 1.00 31.94 ? 81 PRO A CA 1 ATOM 631 C C . PRO A 1 81 ? 31.068 -2.977 25.266 1.00 32.99 ? 81 PRO A C 1 ATOM 632 O O . PRO A 1 81 ? 32.294 -3.073 25.238 1.00 34.13 ? 81 PRO A O 1 ATOM 633 C CB . PRO A 1 81 ? 30.047 -5.089 24.352 1.00 32.85 ? 81 PRO A CB 1 ATOM 634 C CG . PRO A 1 81 ? 28.593 -5.533 24.390 1.00 34.66 ? 81 PRO A CG 1 ATOM 635 C CD . PRO A 1 81 ? 27.881 -4.306 24.909 1.00 33.35 ? 81 PRO A CD 1 ATOM 636 N N . TYR A 1 82 ? 30.424 -1.838 25.031 1.00 32.33 ? 82 TYR A N 1 ATOM 637 C CA . TYR A 1 82 ? 31.153 -0.633 24.684 1.00 31.00 ? 82 TYR A CA 1 ATOM 638 C C . TYR A 1 82 ? 31.142 0.401 25.794 1.00 30.25 ? 82 TYR A C 1 ATOM 639 O O . TYR A 1 82 ? 31.309 1.599 25.554 1.00 30.79 ? 82 TYR A O 1 ATOM 640 C CB . TYR A 1 82 ? 30.586 -0.062 23.381 1.00 31.96 ? 82 TYR A CB 1 ATOM 641 C CG . TYR A 1 82 ? 30.561 -1.097 22.276 1.00 33.46 ? 82 TYR A CG 1 ATOM 642 C CD1 . TYR A 1 82 ? 29.358 -1.653 21.833 1.00 35.59 ? 82 TYR A CD1 1 ATOM 643 C CD2 . TYR A 1 82 ? 31.747 -1.579 21.727 1.00 33.71 ? 82 TYR A CD2 1 ATOM 644 C CE1 . TYR A 1 82 ? 29.343 -2.675 20.868 1.00 35.89 ? 82 TYR A CE1 1 ATOM 645 C CE2 . TYR A 1 82 ? 31.746 -2.591 20.771 1.00 35.34 ? 82 TYR A CE2 1 ATOM 646 C CZ . TYR A 1 82 ? 30.544 -3.136 20.346 1.00 37.23 ? 82 TYR A CZ 1 ATOM 647 O OH . TYR A 1 82 ? 30.559 -4.144 19.406 1.00 39.51 ? 82 TYR A OH 1 ATOM 648 N N . SER A 1 83 ? 30.956 -0.075 27.019 1.00 29.11 ? 83 SER A N 1 ATOM 649 C CA . SER A 1 83 ? 30.947 0.801 28.182 1.00 28.49 ? 83 SER A CA 1 ATOM 650 C C . SER A 1 83 ? 32.277 1.548 28.259 1.00 28.56 ? 83 SER A C 1 ATOM 651 O O . SER A 1 83 ? 33.304 1.035 27.825 1.00 28.87 ? 83 SER A O 1 ATOM 652 C CB . SER A 1 83 ? 30.748 -0.022 29.448 1.00 27.00 ? 83 SER A CB 1 ATOM 653 O OG . SER A 1 83 ? 31.033 0.757 30.586 1.00 28.56 ? 83 SER A OG 1 ATOM 654 N N . TRP A 1 84 ? 32.257 2.760 28.804 1.00 29.13 ? 84 TRP A N 1 ATOM 655 C CA . TRP A 1 84 ? 33.476 3.559 28.926 1.00 28.61 ? 84 TRP A CA 1 ATOM 656 C C . TRP A 1 84 ? 34.425 3.061 30.012 1.00 28.81 ? 84 TRP A C 1 ATOM 657 O O . TRP A 1 84 ? 35.533 3.578 30.146 1.00 27.17 ? 84 TRP A O 1 ATOM 658 C CB . TRP A 1 84 ? 33.126 5.027 29.181 1.00 26.60 ? 84 TRP A CB 1 ATOM 659 C CG . TRP A 1 84 ? 32.727 5.770 27.937 1.00 26.22 ? 84 TRP A CG 1 ATOM 660 C CD1 . TRP A 1 84 ? 32.255 5.230 26.769 1.00 24.79 ? 84 TRP A CD1 1 ATOM 661 C CD2 . TRP A 1 84 ? 32.716 7.193 27.753 1.00 25.51 ? 84 TRP A CD2 1 ATOM 662 N NE1 . TRP A 1 84 ? 31.949 6.229 25.873 1.00 23.81 ? 84 TRP A NE1 1 ATOM 663 C CE2 . TRP A 1 84 ? 32.219 7.443 26.449 1.00 25.25 ? 84 TRP A CE2 1 ATOM 664 C CE3 . TRP A 1 84 ? 33.075 8.280 28.563 1.00 23.36 ? 84 TRP A CE3 1 ATOM 665 C CZ2 . TRP A 1 84 ? 32.072 8.738 25.936 1.00 25.70 ? 84 TRP A CZ2 1 ATOM 666 C CZ3 . TRP A 1 84 ? 32.931 9.566 28.054 1.00 26.28 ? 84 TRP A CZ3 1 ATOM 667 C CH2 . TRP A 1 84 ? 32.432 9.783 26.748 1.00 25.86 ? 84 TRP A CH2 1 ATOM 668 N N . ASN A 1 85 ? 33.996 2.067 30.790 1.00 29.23 ? 85 ASN A N 1 ATOM 669 C CA . ASN A 1 85 ? 34.867 1.526 31.828 1.00 31.37 ? 85 ASN A CA 1 ATOM 670 C C . ASN A 1 85 ? 35.626 0.325 31.266 1.00 32.61 ? 85 ASN A C 1 ATOM 671 O O . ASN A 1 85 ? 36.117 -0.526 32.004 1.00 32.59 ? 85 ASN A O 1 ATOM 672 C CB . ASN A 1 85 ? 34.075 1.149 33.099 1.00 31.11 ? 85 ASN A CB 1 ATOM 673 C CG . ASN A 1 85 ? 33.430 -0.234 33.033 1.00 31.41 ? 85 ASN A CG 1 ATOM 674 O OD1 . ASN A 1 85 ? 32.608 -0.519 32.161 1.00 31.10 ? 85 ASN A OD1 1 ATOM 675 N ND2 . ASN A 1 85 ? 33.792 -1.093 33.980 1.00 31.40 ? 85 ASN A ND2 1 ATOM 676 N N . SER A 1 86 ? 35.724 0.278 29.942 1.00 33.72 ? 86 SER A N 1 ATOM 677 C CA . SER A 1 86 ? 36.437 -0.794 29.264 1.00 35.85 ? 86 SER A CA 1 ATOM 678 C C . SER A 1 86 ? 37.930 -0.635 29.494 1.00 36.34 ? 86 SER A C 1 ATOM 679 O O . SER A 1 86 ? 38.643 -1.618 29.710 1.00 37.39 ? 86 SER A O 1 ATOM 680 C CB . SER A 1 86 ? 36.163 -0.753 27.764 1.00 34.85 ? 86 SER A CB 1 ATOM 681 O OG . SER A 1 86 ? 34.797 -0.994 27.498 1.00 38.94 ? 86 SER A OG 1 ATOM 682 N N . ASN A 1 87 ? 38.392 0.613 29.441 1.00 35.64 ? 87 ASN A N 1 ATOM 683 C CA . ASN A 1 87 ? 39.800 0.931 29.631 1.00 35.28 ? 87 ASN A CA 1 ATOM 684 C C . ASN A 1 87 ? 39.971 2.172 30.495 1.00 34.25 ? 87 ASN A C 1 ATOM 685 O O . ASN A 1 87 ? 40.820 3.024 30.227 1.00 31.79 ? 87 ASN A O 1 ATOM 686 C CB . ASN A 1 87 ? 40.466 1.149 28.278 1.00 38.45 ? 87 ASN A CB 1 ATOM 687 C CG . ASN A 1 87 ? 40.353 -0.060 27.380 1.00 42.99 ? 87 ASN A CG 1 ATOM 688 O OD1 . ASN A 1 87 ? 39.278 -0.364 26.866 1.00 43.87 ? 87 ASN A OD1 1 ATOM 689 N ND2 . ASN A 1 87 ? 41.468 -0.759 27.202 1.00 48.09 ? 87 ASN A ND2 1 ATOM 690 N N . ALA A 1 88 ? 39.151 2.262 31.535 1.00 33.84 ? 88 ALA A N 1 ATOM 691 C CA . ALA A 1 88 ? 39.181 3.388 32.462 1.00 32.06 ? 88 ALA A CA 1 ATOM 692 C C . ALA A 1 88 ? 38.212 3.084 33.591 1.00 31.03 ? 88 ALA A C 1 ATOM 693 O O . ALA A 1 88 ? 37.214 2.393 33.384 1.00 30.90 ? 88 ALA A O 1 ATOM 694 C CB . ALA A 1 88 ? 38.752 4.667 31.749 1.00 30.11 ? 88 ALA A CB 1 ATOM 695 N N . THR A 1 89 ? 38.506 3.561 34.794 1.00 28.94 ? 89 THR A N 1 ATOM 696 C CA . THR A 1 89 ? 37.572 3.326 35.874 1.00 29.75 ? 89 THR A CA 1 ATOM 697 C C . THR A 1 89 ? 36.750 4.615 35.847 1.00 29.84 ? 89 THR A C 1 ATOM 698 O O . THR A 1 89 ? 37.297 5.718 35.791 1.00 29.43 ? 89 THR A O 1 ATOM 699 C CB . THR A 1 89 ? 38.281 3.074 37.251 1.00 28.46 ? 89 THR A CB 1 ATOM 700 O OG1 . THR A 1 89 ? 38.279 4.268 38.038 1.00 28.34 ? 89 THR A OG1 1 ATOM 701 C CG2 . THR A 1 89 ? 39.711 2.605 37.041 1.00 30.37 ? 89 THR A CG2 1 ATOM 702 N N . VAL A 1 90 ? 35.432 4.469 35.843 1.00 29.42 ? 90 VAL A N 1 ATOM 703 C CA . VAL A 1 90 ? 34.547 5.615 35.752 1.00 28.63 ? 90 VAL A CA 1 ATOM 704 C C . VAL A 1 90 ? 33.798 5.950 37.031 1.00 28.16 ? 90 VAL A C 1 ATOM 705 O O . VAL A 1 90 ? 33.448 5.068 37.811 1.00 30.05 ? 90 VAL A O 1 ATOM 706 C CB . VAL A 1 90 ? 33.519 5.385 34.618 1.00 28.28 ? 90 VAL A CB 1 ATOM 707 C CG1 . VAL A 1 90 ? 32.660 6.617 34.430 1.00 28.28 ? 90 VAL A CG1 1 ATOM 708 C CG2 . VAL A 1 90 ? 34.244 5.028 33.328 1.00 25.70 ? 90 VAL A CG2 1 ATOM 709 N N . ILE A 1 91 ? 33.551 7.239 37.235 1.00 27.42 ? 91 ILE A N 1 ATOM 710 C CA . ILE A 1 91 ? 32.809 7.711 38.397 1.00 26.31 ? 91 ILE A CA 1 ATOM 711 C C . ILE A 1 91 ? 31.585 8.481 37.925 1.00 25.87 ? 91 ILE A C 1 ATOM 712 O O . ILE A 1 91 ? 31.704 9.440 37.155 1.00 25.52 ? 91 ILE A O 1 ATOM 713 C CB . ILE A 1 91 ? 33.613 8.690 39.249 1.00 28.38 ? 91 ILE A CB 1 ATOM 714 C CG1 . ILE A 1 91 ? 34.994 8.120 39.566 1.00 27.36 ? 91 ILE A CG1 1 ATOM 715 C CG2 . ILE A 1 91 ? 32.821 9.001 40.520 1.00 28.13 ? 91 ILE A CG2 1 ATOM 716 C CD1 . ILE A 1 91 ? 35.864 9.082 40.326 1.00 27.35 ? 91 ILE A CD1 1 ATOM 717 N N . PHE A 1 92 ? 30.413 8.069 38.393 1.00 24.77 ? 92 PHE A N 1 ATOM 718 C CA . PHE A 1 92 ? 29.170 8.738 38.025 1.00 22.75 ? 92 PHE A CA 1 ATOM 719 C C . PHE A 1 92 ? 28.705 9.493 39.257 1.00 22.04 ? 92 PHE A C 1 ATOM 720 O O . PHE A 1 92 ? 28.399 8.895 40.285 1.00 22.80 ? 92 PHE A O 1 ATOM 721 C CB . PHE A 1 92 ? 28.126 7.705 37.580 1.00 21.10 ? 92 PHE A CB 1 ATOM 722 C CG . PHE A 1 92 ? 28.489 6.991 36.296 1.00 17.72 ? 92 PHE A CG 1 ATOM 723 C CD1 . PHE A 1 92 ? 28.243 7.586 35.059 1.00 15.01 ? 92 PHE A CD1 1 ATOM 724 C CD2 . PHE A 1 92 ? 29.106 5.745 36.327 1.00 16.25 ? 92 PHE A CD2 1 ATOM 725 C CE1 . PHE A 1 92 ? 28.604 6.954 33.872 1.00 14.55 ? 92 PHE A CE1 1 ATOM 726 C CE2 . PHE A 1 92 ? 29.474 5.100 35.142 1.00 17.89 ? 92 PHE A CE2 1 ATOM 727 C CZ . PHE A 1 92 ? 29.222 5.709 33.907 1.00 14.96 ? 92 PHE A CZ 1 ATOM 728 N N . LEU A 1 93 ? 28.671 10.813 39.156 1.00 22.00 ? 93 LEU A N 1 ATOM 729 C CA . LEU A 1 93 ? 28.277 11.647 40.283 1.00 23.46 ? 93 LEU A CA 1 ATOM 730 C C . LEU A 1 93 ? 26.974 12.412 40.093 1.00 24.04 ? 93 LEU A C 1 ATOM 731 O O . LEU A 1 93 ? 26.772 13.060 39.075 1.00 24.89 ? 93 LEU A O 1 ATOM 732 C CB . LEU A 1 93 ? 29.395 12.648 40.590 1.00 22.66 ? 93 LEU A CB 1 ATOM 733 C CG . LEU A 1 93 ? 29.086 13.749 41.604 1.00 23.52 ? 93 LEU A CG 1 ATOM 734 C CD1 . LEU A 1 93 ? 28.885 13.133 42.980 1.00 24.24 ? 93 LEU A CD1 1 ATOM 735 C CD2 . LEU A 1 93 ? 30.221 14.763 41.623 1.00 20.98 ? 93 LEU A CD2 1 ATOM 736 N N . ASP A 1 94 ? 26.080 12.321 41.070 1.00 24.96 ? 94 ASP A N 1 ATOM 737 C CA . ASP A 1 94 ? 24.843 13.080 41.001 1.00 25.08 ? 94 ASP A CA 1 ATOM 738 C C . ASP A 1 94 ? 25.175 14.427 41.629 1.00 25.78 ? 94 ASP A C 1 ATOM 739 O O . ASP A 1 94 ? 25.551 14.506 42.798 1.00 25.96 ? 94 ASP A O 1 ATOM 740 C CB . ASP A 1 94 ? 23.725 12.393 41.773 1.00 24.31 ? 94 ASP A CB 1 ATOM 741 C CG . ASP A 1 94 ? 22.920 11.472 40.902 1.00 25.84 ? 94 ASP A CG 1 ATOM 742 O OD1 . ASP A 1 94 ? 23.061 11.571 39.665 1.00 26.72 ? 94 ASP A OD1 1 ATOM 743 O OD2 . ASP A 1 94 ? 22.140 10.664 41.442 1.00 26.04 ? 94 ASP A OD2 1 ATOM 744 N N . GLN A 1 95 ? 25.036 15.484 40.843 1.00 25.91 ? 95 GLN A N 1 ATOM 745 C CA . GLN A 1 95 ? 25.376 16.819 41.298 1.00 25.25 ? 95 GLN A CA 1 ATOM 746 C C . GLN A 1 95 ? 24.587 17.867 40.499 1.00 23.95 ? 95 GLN A C 1 ATOM 747 O O . GLN A 1 95 ? 24.311 17.676 39.323 1.00 25.03 ? 95 GLN A O 1 ATOM 748 C CB . GLN A 1 95 ? 26.891 16.985 41.116 1.00 24.33 ? 95 GLN A CB 1 ATOM 749 C CG . GLN A 1 95 ? 27.394 18.399 41.132 1.00 28.22 ? 95 GLN A CG 1 ATOM 750 C CD . GLN A 1 95 ? 27.292 19.092 39.790 1.00 28.90 ? 95 GLN A CD 1 ATOM 751 O OE1 . GLN A 1 95 ? 27.322 20.313 39.734 1.00 33.20 ? 95 GLN A OE1 1 ATOM 752 N NE2 . GLN A 1 95 ? 27.185 18.324 38.706 1.00 27.36 ? 95 GLN A NE2 1 ATOM 753 N N . PRO A 1 96 ? 24.201 18.987 41.126 1.00 24.07 ? 96 PRO A N 1 ATOM 754 C CA . PRO A 1 96 ? 24.382 19.452 42.508 1.00 22.86 ? 96 PRO A CA 1 ATOM 755 C C . PRO A 1 96 ? 23.544 18.638 43.495 1.00 22.13 ? 96 PRO A C 1 ATOM 756 O O . PRO A 1 96 ? 22.823 17.721 43.103 1.00 21.55 ? 96 PRO A O 1 ATOM 757 C CB . PRO A 1 96 ? 23.909 20.905 42.446 1.00 22.44 ? 96 PRO A CB 1 ATOM 758 C CG . PRO A 1 96 ? 24.059 21.279 41.011 1.00 22.74 ? 96 PRO A CG 1 ATOM 759 C CD . PRO A 1 96 ? 23.604 20.050 40.301 1.00 23.01 ? 96 PRO A CD 1 ATOM 760 N N . VAL A 1 97 ? 23.629 18.981 44.776 1.00 23.16 ? 97 VAL A N 1 ATOM 761 C CA . VAL A 1 97 ? 22.856 18.268 45.785 1.00 24.92 ? 97 VAL A CA 1 ATOM 762 C C . VAL A 1 97 ? 21.380 18.349 45.421 1.00 25.98 ? 97 VAL A C 1 ATOM 763 O O . VAL A 1 97 ? 20.930 19.350 44.863 1.00 26.42 ? 97 VAL A O 1 ATOM 764 C CB . VAL A 1 97 ? 23.066 18.861 47.196 1.00 26.08 ? 97 VAL A CB 1 ATOM 765 C CG1 . VAL A 1 97 ? 24.482 18.571 47.671 1.00 27.77 ? 97 VAL A CG1 1 ATOM 766 C CG2 . VAL A 1 97 ? 22.822 20.367 47.176 1.00 25.95 ? 97 VAL A CG2 1 ATOM 767 N N . ASN A 1 98 ? 20.648 17.278 45.728 1.00 25.77 ? 98 ASN A N 1 ATOM 768 C CA . ASN A 1 98 ? 19.222 17.149 45.454 1.00 25.30 ? 98 ASN A CA 1 ATOM 769 C C . ASN A 1 98 ? 18.921 16.666 44.045 1.00 26.18 ? 98 ASN A C 1 ATOM 770 O O . ASN A 1 98 ? 17.772 16.637 43.614 1.00 27.36 ? 98 ASN A O 1 ATOM 771 C CB . ASN A 1 98 ? 18.497 18.454 45.760 1.00 25.04 ? 98 ASN A CB 1 ATOM 772 C CG . ASN A 1 98 ? 18.509 18.772 47.238 1.00 25.77 ? 98 ASN A CG 1 ATOM 773 O OD1 . ASN A 1 98 ? 18.627 19.925 47.633 1.00 29.16 ? 98 ASN A OD1 1 ATOM 774 N ND2 . ASN A 1 98 ? 18.387 17.743 48.066 1.00 25.10 ? 98 ASN A ND2 1 ATOM 775 N N . VAL A 1 99 ? 19.964 16.286 43.324 1.00 26.22 ? 99 VAL A N 1 ATOM 776 C CA . VAL A 1 99 ? 19.792 15.740 41.987 1.00 26.09 ? 99 VAL A CA 1 ATOM 777 C C . VAL A 1 99 ? 19.988 14.232 42.147 1.00 26.20 ? 99 VAL A C 1 ATOM 778 O O . VAL A 1 99 ? 20.934 13.788 42.802 1.00 24.17 ? 99 VAL A O 1 ATOM 779 C CB . VAL A 1 99 ? 20.842 16.295 41.004 1.00 26.13 ? 99 VAL A CB 1 ATOM 780 C CG1 . VAL A 1 99 ? 20.835 15.477 39.723 1.00 22.83 ? 99 VAL A CG1 1 ATOM 781 C CG2 . VAL A 1 99 ? 20.551 17.766 40.715 1.00 22.99 ? 99 VAL A CG2 1 ATOM 782 N N . GLY A 1 100 ? 19.084 13.453 41.567 1.00 27.41 ? 100 GLY A N 1 ATOM 783 C CA . GLY A 1 100 ? 19.178 12.006 41.671 1.00 28.92 ? 100 GLY A CA 1 ATOM 784 C C . GLY A 1 100 ? 19.079 11.563 43.118 1.00 31.16 ? 100 GLY A C 1 ATOM 785 O O . GLY A 1 100 ? 18.087 11.855 43.795 1.00 31.19 ? 100 GLY A O 1 ATOM 786 N N . PHE A 1 101 ? 20.105 10.860 43.596 1.00 30.76 ? 101 PHE A N 1 ATOM 787 C CA . PHE A 1 101 ? 20.134 10.396 44.976 1.00 30.53 ? 101 PHE A CA 1 ATOM 788 C C . PHE A 1 101 ? 20.901 11.359 45.887 1.00 31.40 ? 101 PHE A C 1 ATOM 789 O O . PHE A 1 101 ? 20.947 11.167 47.102 1.00 33.15 ? 101 PHE A O 1 ATOM 790 C CB . PHE A 1 101 ? 20.747 8.994 45.061 1.00 28.03 ? 101 PHE A CB 1 ATOM 791 C CG . PHE A 1 101 ? 19.844 7.902 44.553 1.00 27.69 ? 101 PHE A CG 1 ATOM 792 C CD1 . PHE A 1 101 ? 18.519 7.818 44.983 1.00 26.70 ? 101 PHE A CD1 1 ATOM 793 C CD2 . PHE A 1 101 ? 20.319 6.939 43.668 1.00 27.10 ? 101 PHE A CD2 1 ATOM 794 C CE1 . PHE A 1 101 ? 17.687 6.795 44.542 1.00 23.44 ? 101 PHE A CE1 1 ATOM 795 C CE2 . PHE A 1 101 ? 19.484 5.904 43.221 1.00 23.50 ? 101 PHE A CE2 1 ATOM 796 C CZ . PHE A 1 101 ? 18.174 5.836 43.660 1.00 23.94 ? 101 PHE A CZ 1 ATOM 797 N N . SER A 1 102 ? 21.506 12.390 45.309 1.00 30.77 ? 102 SER A N 1 ATOM 798 C CA . SER A 1 102 ? 22.241 13.362 46.110 1.00 31.08 ? 102 SER A CA 1 ATOM 799 C C . SER A 1 102 ? 21.216 14.265 46.765 1.00 31.68 ? 102 SER A C 1 ATOM 800 O O . SER A 1 102 ? 20.231 14.628 46.137 1.00 32.54 ? 102 SER A O 1 ATOM 801 C CB . SER A 1 102 ? 23.174 14.200 45.233 1.00 30.07 ? 102 SER A CB 1 ATOM 802 O OG . SER A 1 102 ? 24.286 13.439 44.799 1.00 28.52 ? 102 SER A OG 1 ATOM 803 N N . TYR A 1 103 ? 21.430 14.621 48.024 1.00 32.08 ? 103 TYR A N 1 ATOM 804 C CA . TYR A 1 103 ? 20.483 15.491 48.699 1.00 34.82 ? 103 TYR A CA 1 ATOM 805 C C . TYR A 1 103 ? 21.135 16.392 49.734 1.00 36.73 ? 103 TYR A C 1 ATOM 806 O O . TYR A 1 103 ? 22.304 16.232 50.083 1.00 37.17 ? 103 TYR A O 1 ATOM 807 C CB . TYR A 1 103 ? 19.397 14.671 49.379 1.00 34.57 ? 103 TYR A CB 1 ATOM 808 C CG . TYR A 1 103 ? 19.899 13.897 50.573 1.00 36.83 ? 103 TYR A CG 1 ATOM 809 C CD1 . TYR A 1 103 ? 20.643 12.723 50.407 1.00 36.23 ? 103 TYR A CD1 1 ATOM 810 C CD2 . TYR A 1 103 ? 19.642 14.344 51.874 1.00 34.57 ? 103 TYR A CD2 1 ATOM 811 C CE1 . TYR A 1 103 ? 21.113 12.012 51.502 1.00 36.05 ? 103 TYR A CE1 1 ATOM 812 C CE2 . TYR A 1 103 ? 20.108 13.641 52.977 1.00 34.86 ? 103 TYR A CE2 1 ATOM 813 C CZ . TYR A 1 103 ? 20.841 12.476 52.784 1.00 36.25 ? 103 TYR A CZ 1 ATOM 814 O OH . TYR A 1 103 ? 21.294 11.771 53.868 1.00 34.28 ? 103 TYR A OH 1 ATOM 815 N N . SER A 1 104 ? 20.349 17.338 50.227 1.00 38.80 ? 104 SER A N 1 ATOM 816 C CA . SER A 1 104 ? 20.802 18.289 51.224 1.00 41.54 ? 104 SER A CA 1 ATOM 817 C C . SER A 1 104 ? 19.582 18.948 51.821 1.00 43.81 ? 104 SER A C 1 ATOM 818 O O . SER A 1 104 ? 18.757 19.506 51.100 1.00 44.87 ? 104 SER A O 1 ATOM 819 C CB . SER A 1 104 ? 21.687 19.350 50.582 1.00 41.89 ? 104 SER A CB 1 ATOM 820 O OG . SER A 1 104 ? 21.833 20.461 51.446 1.00 43.86 ? 104 SER A OG 1 ATOM 821 N N . GLY A 1 105 ? 19.470 18.889 53.140 1.00 46.53 ? 105 GLY A N 1 ATOM 822 C CA . GLY A 1 105 ? 18.328 19.483 53.803 1.00 50.80 ? 105 GLY A CA 1 ATOM 823 C C . GLY A 1 105 ? 18.319 20.997 53.786 1.00 53.77 ? 105 GLY A C 1 ATOM 824 O O . GLY A 1 105 ? 17.334 21.612 53.382 1.00 54.52 ? 105 GLY A O 1 ATOM 825 N N . SER A 1 106 ? 19.421 21.604 54.212 1.00 56.08 ? 106 SER A N 1 ATOM 826 C CA . SER A 1 106 ? 19.512 23.060 54.274 1.00 58.38 ? 106 SER A CA 1 ATOM 827 C C . SER A 1 106 ? 19.878 23.773 52.969 1.00 57.77 ? 106 SER A C 1 ATOM 828 O O . SER A 1 106 ? 19.021 24.348 52.308 1.00 57.77 ? 106 SER A O 1 ATOM 829 C CB . SER A 1 106 ? 20.506 23.465 55.371 1.00 59.47 ? 106 SER A CB 1 ATOM 830 O OG . SER A 1 106 ? 21.789 22.906 55.131 1.00 60.39 ? 106 SER A OG 1 ATOM 831 N N . SER A 1 107 ? 21.158 23.732 52.618 1.00 58.40 ? 107 SER A N 1 ATOM 832 C CA . SER A 1 107 ? 21.688 24.391 51.426 1.00 57.59 ? 107 SER A CA 1 ATOM 833 C C . SER A 1 107 ? 21.087 24.024 50.071 1.00 55.92 ? 107 SER A C 1 ATOM 834 O O . SER A 1 107 ? 20.243 23.129 49.952 1.00 57.27 ? 107 SER A O 1 ATOM 835 C CB . SER A 1 107 ? 23.199 24.173 51.360 1.00 59.63 ? 107 SER A CB 1 ATOM 836 O OG . SER A 1 107 ? 23.826 24.638 52.545 1.00 63.70 ? 107 SER A OG 1 ATOM 837 N N . GLY A 1 108 ? 21.558 24.738 49.053 1.00 52.86 ? 108 GLY A N 1 ATOM 838 C CA . GLY A 1 108 ? 21.113 24.540 47.687 1.00 47.66 ? 108 GLY A CA 1 ATOM 839 C C . GLY A 1 108 ? 21.905 25.473 46.789 1.00 44.97 ? 108 GLY A C 1 ATOM 840 O O . GLY A 1 108 ? 22.130 26.632 47.133 1.00 45.00 ? 108 GLY A O 1 ATOM 841 N N . VAL A 1 109 ? 22.318 24.971 45.633 1.00 42.42 ? 109 VAL A N 1 ATOM 842 C CA . VAL A 1 109 ? 23.111 25.733 44.673 1.00 38.74 ? 109 VAL A CA 1 ATOM 843 C C . VAL A 1 109 ? 22.275 26.352 43.543 1.00 36.99 ? 109 VAL A C 1 ATOM 844 O O . VAL A 1 109 ? 21.378 25.709 43.012 1.00 37.18 ? 109 VAL A O 1 ATOM 845 C CB . VAL A 1 109 ? 24.185 24.809 44.073 1.00 37.67 ? 109 VAL A CB 1 ATOM 846 C CG1 . VAL A 1 109 ? 24.984 25.527 42.997 1.00 38.26 ? 109 VAL A CG1 1 ATOM 847 C CG2 . VAL A 1 109 ? 25.088 24.321 45.182 1.00 36.83 ? 109 VAL A CG2 1 ATOM 848 N N . SER A 1 110 ? 22.584 27.593 43.171 1.00 35.61 ? 110 SER A N 1 ATOM 849 C CA . SER A 1 110 ? 21.854 28.288 42.105 1.00 34.35 ? 110 SER A CA 1 ATOM 850 C C . SER A 1 110 ? 22.675 28.659 40.879 1.00 33.56 ? 110 SER A C 1 ATOM 851 O O . SER A 1 110 ? 22.126 29.145 39.900 1.00 34.28 ? 110 SER A O 1 ATOM 852 C CB . SER A 1 110 ? 21.216 29.568 42.637 1.00 34.28 ? 110 SER A CB 1 ATOM 853 O OG . SER A 1 110 ? 20.093 29.271 43.433 1.00 39.35 ? 110 SER A OG 1 ATOM 854 N N . ASN A 1 111 ? 23.985 28.462 40.933 1.00 32.61 ? 111 ASN A N 1 ATOM 855 C CA . ASN A 1 111 ? 24.827 28.794 39.798 1.00 30.38 ? 111 ASN A CA 1 ATOM 856 C C . ASN A 1 111 ? 25.945 27.776 39.673 1.00 30.38 ? 111 ASN A C 1 ATOM 857 O O . ASN A 1 111 ? 26.156 26.964 40.575 1.00 30.54 ? 111 ASN A O 1 ATOM 858 C CB . ASN A 1 111 ? 25.402 30.203 39.960 1.00 30.83 ? 111 ASN A CB 1 ATOM 859 C CG . ASN A 1 111 ? 26.377 30.307 41.112 1.00 32.25 ? 111 ASN A CG 1 ATOM 860 O OD1 . ASN A 1 111 ? 27.503 29.792 41.048 1.00 34.26 ? 111 ASN A OD1 1 ATOM 861 N ND2 . ASN A 1 111 ? 25.952 30.970 42.178 1.00 30.06 ? 111 ASN A ND2 1 ATOM 862 N N . THR A 1 112 ? 26.660 27.831 38.554 1.00 29.30 ? 112 THR A N 1 ATOM 863 C CA . THR A 1 112 ? 27.751 26.907 38.271 1.00 27.89 ? 112 THR A CA 1 ATOM 864 C C . THR A 1 112 ? 28.955 27.046 39.201 1.00 27.56 ? 112 THR A C 1 ATOM 865 O O . THR A 1 112 ? 29.523 26.043 39.639 1.00 26.28 ? 112 THR A O 1 ATOM 866 C CB . THR A 1 112 ? 28.226 27.075 36.814 1.00 28.24 ? 112 THR A CB 1 ATOM 867 O OG1 . THR A 1 112 ? 27.143 26.768 35.926 1.00 28.82 ? 112 THR A OG1 1 ATOM 868 C CG2 . THR A 1 112 ? 29.398 26.147 36.516 1.00 28.15 ? 112 THR A CG2 1 ATOM 869 N N . VAL A 1 113 ? 29.346 28.283 39.496 1.00 27.17 ? 113 VAL A N 1 ATOM 870 C CA . VAL A 1 113 ? 30.493 28.528 40.369 1.00 25.84 ? 113 VAL A CA 1 ATOM 871 C C . VAL A 1 113 ? 30.300 27.834 41.712 1.00 26.62 ? 113 VAL A C 1 ATOM 872 O O . VAL A 1 113 ? 31.179 27.095 42.176 1.00 27.10 ? 113 VAL A O 1 ATOM 873 C CB . VAL A 1 113 ? 30.722 30.052 40.597 1.00 24.62 ? 113 VAL A CB 1 ATOM 874 C CG1 . VAL A 1 113 ? 31.825 30.277 41.619 1.00 18.03 ? 113 VAL A CG1 1 ATOM 875 C CG2 . VAL A 1 113 ? 31.096 30.719 39.275 1.00 20.09 ? 113 VAL A CG2 1 ATOM 876 N N . ALA A 1 114 ? 29.147 28.056 42.330 1.00 24.24 ? 114 ALA A N 1 ATOM 877 C CA . ALA A 1 114 ? 28.880 27.423 43.609 1.00 24.96 ? 114 ALA A CA 1 ATOM 878 C C . ALA A 1 114 ? 28.922 25.897 43.464 1.00 25.64 ? 114 ALA A C 1 ATOM 879 O O . ALA A 1 114 ? 29.460 25.200 44.329 1.00 26.34 ? 114 ALA A O 1 ATOM 880 C CB . ALA A 1 114 ? 27.535 27.876 44.144 1.00 21.47 ? 114 ALA A CB 1 ATOM 881 N N . ALA A 1 115 ? 28.362 25.370 42.376 1.00 25.94 ? 115 ALA A N 1 ATOM 882 C CA . ALA A 1 115 ? 28.381 23.920 42.160 1.00 26.24 ? 115 ALA A CA 1 ATOM 883 C C . ALA A 1 115 ? 29.833 23.466 42.043 1.00 26.06 ? 115 ALA A C 1 ATOM 884 O O . ALA A 1 115 ? 30.183 22.359 42.442 1.00 26.51 ? 115 ALA A O 1 ATOM 885 C CB . ALA A 1 115 ? 27.609 23.545 40.893 1.00 23.58 ? 115 ALA A CB 1 ATOM 886 N N . GLY A 1 116 ? 30.675 24.335 41.497 1.00 27.35 ? 116 GLY A N 1 ATOM 887 C CA . GLY A 1 116 ? 32.085 24.008 41.355 1.00 28.78 ? 116 GLY A CA 1 ATOM 888 C C . GLY A 1 116 ? 32.776 23.838 42.697 1.00 28.93 ? 116 GLY A C 1 ATOM 889 O O . GLY A 1 116 ? 33.636 22.979 42.847 1.00 28.41 ? 116 GLY A O 1 ATOM 890 N N . LYS A 1 117 ? 32.407 24.660 43.675 1.00 30.12 ? 117 LYS A N 1 ATOM 891 C CA . LYS A 1 117 ? 33.002 24.564 45.002 1.00 30.55 ? 117 LYS A CA 1 ATOM 892 C C . LYS A 1 117 ? 32.655 23.201 45.587 1.00 30.98 ? 117 LYS A C 1 ATOM 893 O O . LYS A 1 117 ? 33.510 22.515 46.156 1.00 31.63 ? 117 LYS A O 1 ATOM 894 C CB . LYS A 1 117 ? 32.443 25.646 45.930 1.00 32.84 ? 117 LYS A CB 1 ATOM 895 C CG . LYS A 1 117 ? 32.525 27.068 45.403 1.00 37.79 ? 117 LYS A CG 1 ATOM 896 C CD . LYS A 1 117 ? 33.959 27.546 45.267 1.00 41.25 ? 117 LYS A CD 1 ATOM 897 C CE . LYS A 1 117 ? 34.001 28.948 44.683 1.00 44.25 ? 117 LYS A CE 1 ATOM 898 N NZ . LYS A 1 117 ? 33.181 29.908 45.483 1.00 48.52 ? 117 LYS A NZ 1 ATOM 899 N N . ASP A 1 118 ? 31.393 22.811 45.442 1.00 29.47 ? 118 ASP A N 1 ATOM 900 C CA . ASP A 1 118 ? 30.937 21.539 45.977 1.00 29.19 ? 118 ASP A CA 1 ATOM 901 C C . ASP A 1 118 ? 31.617 20.330 45.344 1.00 29.45 ? 118 ASP A C 1 ATOM 902 O O . ASP A 1 118 ? 32.011 19.396 46.041 1.00 28.67 ? 118 ASP A O 1 ATOM 903 C CB . ASP A 1 118 ? 29.415 21.411 45.834 1.00 28.81 ? 118 ASP A CB 1 ATOM 904 C CG . ASP A 1 118 ? 28.654 22.278 46.828 1.00 27.94 ? 118 ASP A CG 1 ATOM 905 O OD1 . ASP A 1 118 ? 29.286 22.867 47.729 1.00 28.30 ? 118 ASP A OD1 1 ATOM 906 O OD2 . ASP A 1 118 ? 27.415 22.364 46.717 1.00 28.28 ? 118 ASP A OD2 1 ATOM 907 N N . VAL A 1 119 ? 31.760 20.339 44.025 1.00 29.86 ? 119 VAL A N 1 ATOM 908 C CA . VAL A 1 119 ? 32.387 19.209 43.362 1.00 31.71 ? 119 VAL A CA 1 ATOM 909 C C . VAL A 1 119 ? 33.844 19.085 43.785 1.00 32.68 ? 119 VAL A C 1 ATOM 910 O O . VAL A 1 119 ? 34.353 17.973 43.970 1.00 32.35 ? 119 VAL A O 1 ATOM 911 C CB . VAL A 1 119 ? 32.270 19.328 41.826 1.00 31.60 ? 119 VAL A CB 1 ATOM 912 C CG1 . VAL A 1 119 ? 33.093 18.251 41.140 1.00 30.96 ? 119 VAL A CG1 1 ATOM 913 C CG2 . VAL A 1 119 ? 30.818 19.181 41.427 1.00 31.86 ? 119 VAL A CG2 1 ATOM 914 N N . TYR A 1 120 ? 34.520 20.216 43.951 1.00 33.22 ? 120 TYR A N 1 ATOM 915 C CA . TYR A 1 120 ? 35.906 20.159 44.374 1.00 34.33 ? 120 TYR A CA 1 ATOM 916 C C . TYR A 1 120 ? 35.992 19.441 45.723 1.00 34.84 ? 120 TYR A C 1 ATOM 917 O O . TYR A 1 120 ? 36.838 18.566 45.913 1.00 34.70 ? 120 TYR A O 1 ATOM 918 C CB . TYR A 1 120 ? 36.515 21.557 44.485 1.00 35.03 ? 120 TYR A CB 1 ATOM 919 C CG . TYR A 1 120 ? 37.915 21.495 45.042 1.00 36.56 ? 120 TYR A CG 1 ATOM 920 C CD1 . TYR A 1 120 ? 38.166 21.770 46.388 1.00 36.27 ? 120 TYR A CD1 1 ATOM 921 C CD2 . TYR A 1 120 ? 38.974 21.062 44.250 1.00 36.34 ? 120 TYR A CD2 1 ATOM 922 C CE1 . TYR A 1 120 ? 39.430 21.612 46.927 1.00 37.04 ? 120 TYR A CE1 1 ATOM 923 C CE2 . TYR A 1 120 ? 40.241 20.895 44.782 1.00 38.55 ? 120 TYR A CE2 1 ATOM 924 C CZ . TYR A 1 120 ? 40.463 21.171 46.121 1.00 39.70 ? 120 TYR A CZ 1 ATOM 925 O OH . TYR A 1 120 ? 41.723 20.994 46.652 1.00 44.58 ? 120 TYR A OH 1 ATOM 926 N N . ASN A 1 121 ? 35.117 19.808 46.656 1.00 34.23 ? 121 ASN A N 1 ATOM 927 C CA . ASN A 1 121 ? 35.099 19.159 47.962 1.00 35.61 ? 121 ASN A CA 1 ATOM 928 C C . ASN A 1 121 ? 34.839 17.661 47.827 1.00 35.99 ? 121 ASN A C 1 ATOM 929 O O . ASN A 1 121 ? 35.508 16.852 48.473 1.00 37.42 ? 121 ASN A O 1 ATOM 930 C CB . ASN A 1 121 ? 34.029 19.776 48.863 1.00 36.06 ? 121 ASN A CB 1 ATOM 931 C CG . ASN A 1 121 ? 34.456 21.110 49.449 1.00 37.34 ? 121 ASN A CG 1 ATOM 932 O OD1 . ASN A 1 121 ? 33.685 21.754 50.147 1.00 41.45 ? 121 ASN A OD1 1 ATOM 933 N ND2 . ASN A 1 121 ? 35.687 21.527 49.170 1.00 37.72 ? 121 ASN A ND2 1 ATOM 934 N N . PHE A 1 122 ? 33.870 17.287 46.994 1.00 34.95 ? 122 PHE A N 1 ATOM 935 C CA . PHE A 1 122 ? 33.568 15.874 46.797 1.00 33.19 ? 122 PHE A CA 1 ATOM 936 C C . PHE A 1 122 ? 34.798 15.106 46.321 1.00 32.50 ? 122 PHE A C 1 ATOM 937 O O . PHE A 1 122 ? 35.094 14.027 46.827 1.00 32.76 ? 122 PHE A O 1 ATOM 938 C CB . PHE A 1 122 ? 32.424 15.680 45.790 1.00 31.04 ? 122 PHE A CB 1 ATOM 939 C CG . PHE A 1 122 ? 32.311 14.266 45.279 1.00 30.13 ? 122 PHE A CG 1 ATOM 940 C CD1 . PHE A 1 122 ? 32.981 13.874 44.123 1.00 30.54 ? 122 PHE A CD1 1 ATOM 941 C CD2 . PHE A 1 122 ? 31.603 13.307 45.997 1.00 30.24 ? 122 PHE A CD2 1 ATOM 942 C CE1 . PHE A 1 122 ? 32.954 12.545 43.690 1.00 30.32 ? 122 PHE A CE1 1 ATOM 943 C CE2 . PHE A 1 122 ? 31.570 11.977 45.574 1.00 29.39 ? 122 PHE A CE2 1 ATOM 944 C CZ . PHE A 1 122 ? 32.249 11.596 44.417 1.00 29.91 ? 122 PHE A CZ 1 ATOM 945 N N . LEU A 1 123 ? 35.508 15.658 45.344 1.00 32.52 ? 123 LEU A N 1 ATOM 946 C CA . LEU A 1 123 ? 36.698 15.001 44.821 1.00 34.51 ? 123 LEU A CA 1 ATOM 947 C C . LEU A 1 123 ? 37.794 14.841 45.881 1.00 35.78 ? 123 LEU A C 1 ATOM 948 O O . LEU A 1 123 ? 38.493 13.828 45.904 1.00 34.68 ? 123 LEU A O 1 ATOM 949 C CB . LEU A 1 123 ? 37.227 15.761 43.600 1.00 34.16 ? 123 LEU A CB 1 ATOM 950 C CG . LEU A 1 123 ? 36.274 15.718 42.396 1.00 35.42 ? 123 LEU A CG 1 ATOM 951 C CD1 . LEU A 1 123 ? 36.812 16.586 41.278 1.00 34.43 ? 123 LEU A CD1 1 ATOM 952 C CD2 . LEU A 1 123 ? 36.103 14.274 41.918 1.00 34.97 ? 123 LEU A CD2 1 ATOM 953 N N . GLU A 1 124 ? 37.943 15.833 46.756 1.00 37.08 ? 124 GLU A N 1 ATOM 954 C CA . GLU A 1 124 ? 38.939 15.755 47.820 1.00 38.66 ? 124 GLU A CA 1 ATOM 955 C C . GLU A 1 124 ? 38.579 14.587 48.731 1.00 38.51 ? 124 GLU A C 1 ATOM 956 O O . GLU A 1 124 ? 39.428 13.766 49.077 1.00 39.27 ? 124 GLU A O 1 ATOM 957 C CB . GLU A 1 124 ? 38.961 17.049 48.633 1.00 40.77 ? 124 GLU A CB 1 ATOM 958 C CG . GLU A 1 124 ? 39.771 18.168 48.008 1.00 47.51 ? 124 GLU A CG 1 ATOM 959 C CD . GLU A 1 124 ? 41.266 17.997 48.223 1.00 52.02 ? 124 GLU A CD 1 ATOM 960 O OE1 . GLU A 1 124 ? 41.737 18.239 49.358 1.00 53.38 ? 124 GLU A OE1 1 ATOM 961 O OE2 . GLU A 1 124 ? 41.970 17.615 47.260 1.00 53.85 ? 124 GLU A OE2 1 ATOM 962 N N . LEU A 1 125 ? 37.312 14.512 49.118 1.00 36.94 ? 125 LEU A N 1 ATOM 963 C CA . LEU A 1 125 ? 36.869 13.436 49.982 1.00 36.84 ? 125 LEU A CA 1 ATOM 964 C C . LEU A 1 125 ? 37.005 12.109 49.250 1.00 36.77 ? 125 LEU A C 1 ATOM 965 O O . LEU A 1 125 ? 37.404 11.106 49.837 1.00 37.56 ? 125 LEU A O 1 ATOM 966 C CB . LEU A 1 125 ? 35.415 13.658 50.409 1.00 36.34 ? 125 LEU A CB 1 ATOM 967 C CG . LEU A 1 125 ? 35.158 14.863 51.321 1.00 37.30 ? 125 LEU A CG 1 ATOM 968 C CD1 . LEU A 1 125 ? 33.662 15.170 51.408 1.00 36.77 ? 125 LEU A CD1 1 ATOM 969 C CD2 . LEU A 1 125 ? 35.732 14.582 52.691 1.00 34.73 ? 125 LEU A CD2 1 ATOM 970 N N . PHE A 1 126 ? 36.692 12.106 47.960 1.00 36.84 ? 126 PHE A N 1 ATOM 971 C CA . PHE A 1 126 ? 36.772 10.875 47.179 1.00 37.19 ? 126 PHE A CA 1 ATOM 972 C C . PHE A 1 126 ? 38.173 10.264 47.124 1.00 36.95 ? 126 PHE A C 1 ATOM 973 O O . PHE A 1 126 ? 38.381 9.131 47.554 1.00 36.56 ? 126 PHE A O 1 ATOM 974 C CB . PHE A 1 126 ? 36.255 11.103 45.755 1.00 34.21 ? 126 PHE A CB 1 ATOM 975 C CG . PHE A 1 126 ? 36.284 9.868 44.902 1.00 32.47 ? 126 PHE A CG 1 ATOM 976 C CD1 . PHE A 1 126 ? 37.419 9.537 44.168 1.00 33.18 ? 126 PHE A CD1 1 ATOM 977 C CD2 . PHE A 1 126 ? 35.189 9.012 44.863 1.00 32.24 ? 126 PHE A CD2 1 ATOM 978 C CE1 . PHE A 1 126 ? 37.467 8.366 43.406 1.00 33.68 ? 126 PHE A CE1 1 ATOM 979 C CE2 . PHE A 1 126 ? 35.221 7.840 44.107 1.00 33.38 ? 126 PHE A CE2 1 ATOM 980 C CZ . PHE A 1 126 ? 36.364 7.515 43.376 1.00 33.23 ? 126 PHE A CZ 1 ATOM 981 N N . PHE A 1 127 ? 39.130 11.010 46.591 1.00 37.01 ? 127 PHE A N 1 ATOM 982 C CA . PHE A 1 127 ? 40.486 10.508 46.484 1.00 39.19 ? 127 PHE A CA 1 ATOM 983 C C . PHE A 1 127 ? 41.117 10.257 47.849 1.00 41.58 ? 127 PHE A C 1 ATOM 984 O O . PHE A 1 127 ? 42.180 9.637 47.958 1.00 41.65 ? 127 PHE A O 1 ATOM 985 C CB . PHE A 1 127 ? 41.320 11.472 45.642 1.00 37.95 ? 127 PHE A CB 1 ATOM 986 C CG . PHE A 1 127 ? 40.963 11.442 44.183 1.00 37.36 ? 127 PHE A CG 1 ATOM 987 C CD1 . PHE A 1 127 ? 41.106 10.271 43.446 1.00 37.19 ? 127 PHE A CD1 1 ATOM 988 C CD2 . PHE A 1 127 ? 40.479 12.573 43.544 1.00 36.93 ? 127 PHE A CD2 1 ATOM 989 C CE1 . PHE A 1 127 ? 40.774 10.233 42.095 1.00 36.18 ? 127 PHE A CE1 1 ATOM 990 C CE2 . PHE A 1 127 ? 40.146 12.540 42.192 1.00 36.01 ? 127 PHE A CE2 1 ATOM 991 C CZ . PHE A 1 127 ? 40.295 11.371 41.470 1.00 34.29 ? 127 PHE A CZ 1 ATOM 992 N N . ASP A 1 128 ? 40.439 10.726 48.890 1.00 43.46 ? 128 ASP A N 1 ATOM 993 C CA . ASP A 1 128 ? 40.896 10.532 50.255 1.00 44.06 ? 128 ASP A CA 1 ATOM 994 C C . ASP A 1 128 ? 40.436 9.136 50.678 1.00 44.15 ? 128 ASP A C 1 ATOM 995 O O . ASP A 1 128 ? 41.177 8.387 51.311 1.00 45.06 ? 128 ASP A O 1 ATOM 996 C CB . ASP A 1 128 ? 40.265 11.582 51.159 1.00 47.54 ? 128 ASP A CB 1 ATOM 997 C CG . ASP A 1 128 ? 41.238 12.135 52.167 1.00 52.11 ? 128 ASP A CG 1 ATOM 998 O OD1 . ASP A 1 128 ? 42.188 12.842 51.747 1.00 52.86 ? 128 ASP A OD1 1 ATOM 999 O OD2 . ASP A 1 128 ? 41.055 11.859 53.375 1.00 53.17 ? 128 ASP A OD2 1 ATOM 1000 N N . GLN A 1 129 ? 39.202 8.802 50.310 1.00 42.74 ? 129 GLN A N 1 ATOM 1001 C CA . GLN A 1 129 ? 38.603 7.506 50.607 1.00 41.67 ? 129 GLN A CA 1 ATOM 1002 C C . GLN A 1 129 ? 39.161 6.397 49.718 1.00 40.36 ? 129 GLN A C 1 ATOM 1003 O O . GLN A 1 129 ? 39.228 5.242 50.126 1.00 39.26 ? 129 GLN A O 1 ATOM 1004 C CB . GLN A 1 129 ? 37.092 7.576 50.399 1.00 44.71 ? 129 GLN A CB 1 ATOM 1005 C CG . GLN A 1 129 ? 36.289 7.816 51.654 1.00 49.37 ? 129 GLN A CG 1 ATOM 1006 C CD . GLN A 1 129 ? 36.273 6.602 52.551 1.00 50.89 ? 129 GLN A CD 1 ATOM 1007 O OE1 . GLN A 1 129 ? 35.883 5.514 52.131 1.00 49.83 ? 129 GLN A OE1 1 ATOM 1008 N NE2 . GLN A 1 129 ? 36.700 6.779 53.795 1.00 54.09 ? 129 GLN A NE2 1 ATOM 1009 N N . PHE A 1 130 ? 39.547 6.747 48.496 1.00 39.58 ? 130 PHE A N 1 ATOM 1010 C CA . PHE A 1 130 ? 40.076 5.759 47.564 1.00 39.54 ? 130 PHE A CA 1 ATOM 1011 C C . PHE A 1 130 ? 41.417 6.187 46.989 1.00 39.48 ? 130 PHE A C 1 ATOM 1012 O O . PHE A 1 130 ? 41.522 6.529 45.813 1.00 38.61 ? 130 PHE A O 1 ATOM 1013 C CB . PHE A 1 130 ? 39.081 5.516 46.421 1.00 39.02 ? 130 PHE A CB 1 ATOM 1014 C CG . PHE A 1 130 ? 37.694 5.174 46.885 1.00 37.76 ? 130 PHE A CG 1 ATOM 1015 C CD1 . PHE A 1 130 ? 36.728 6.168 47.023 1.00 37.55 ? 130 PHE A CD1 1 ATOM 1016 C CD2 . PHE A 1 130 ? 37.358 3.866 47.206 1.00 36.46 ? 130 PHE A CD2 1 ATOM 1017 C CE1 . PHE A 1 130 ? 35.447 5.864 47.478 1.00 37.72 ? 130 PHE A CE1 1 ATOM 1018 C CE2 . PHE A 1 130 ? 36.081 3.550 47.662 1.00 38.07 ? 130 PHE A CE2 1 ATOM 1019 C CZ . PHE A 1 130 ? 35.122 4.552 47.799 1.00 38.40 ? 130 PHE A CZ 1 ATOM 1020 N N . PRO A 1 131 ? 42.472 6.161 47.816 1.00 41.06 ? 131 PRO A N 1 ATOM 1021 C CA . PRO A 1 131 ? 43.802 6.562 47.344 1.00 39.94 ? 131 PRO A CA 1 ATOM 1022 C C . PRO A 1 131 ? 44.256 5.695 46.176 1.00 39.78 ? 131 PRO A C 1 ATOM 1023 O O . PRO A 1 131 ? 45.100 6.102 45.380 1.00 39.74 ? 131 PRO A O 1 ATOM 1024 C CB . PRO A 1 131 ? 44.673 6.375 48.581 1.00 39.62 ? 131 PRO A CB 1 ATOM 1025 C CG . PRO A 1 131 ? 43.693 6.576 49.723 1.00 39.73 ? 131 PRO A CG 1 ATOM 1026 C CD . PRO A 1 131 ? 42.506 5.796 49.244 1.00 39.55 ? 131 PRO A CD 1 ATOM 1027 N N . GLU A 1 132 ? 43.672 4.505 46.075 1.00 39.45 ? 132 GLU A N 1 ATOM 1028 C CA . GLU A 1 132 ? 44.005 3.561 45.018 1.00 40.54 ? 132 GLU A CA 1 ATOM 1029 C C . GLU A 1 132 ? 43.882 4.142 43.618 1.00 41.44 ? 132 GLU A C 1 ATOM 1030 O O . GLU A 1 132 ? 44.577 3.705 42.702 1.00 41.39 ? 132 GLU A O 1 ATOM 1031 C CB . GLU A 1 132 ? 43.095 2.340 45.093 1.00 42.27 ? 132 GLU A CB 1 ATOM 1032 C CG . GLU A 1 132 ? 42.806 1.875 46.491 1.00 46.23 ? 132 GLU A CG 1 ATOM 1033 C CD . GLU A 1 132 ? 41.501 2.415 47.019 1.00 45.81 ? 132 GLU A CD 1 ATOM 1034 O OE1 . GLU A 1 132 ? 40.441 1.933 46.565 1.00 45.08 ? 132 GLU A OE1 1 ATOM 1035 O OE2 . GLU A 1 132 ? 41.542 3.318 47.883 1.00 47.12 ? 132 GLU A OE2 1 ATOM 1036 N N . TYR A 1 133 ? 42.997 5.118 43.446 1.00 41.45 ? 133 TYR A N 1 ATOM 1037 C CA . TYR A 1 133 ? 42.790 5.693 42.127 1.00 42.50 ? 133 TYR A CA 1 ATOM 1038 C C . TYR A 1 133 ? 43.651 6.916 41.821 1.00 44.45 ? 133 TYR A C 1 ATOM 1039 O O . TYR A 1 133 ? 43.409 7.634 40.849 1.00 43.77 ? 133 TYR A O 1 ATOM 1040 C CB . TYR A 1 133 ? 41.297 5.982 41.936 1.00 40.78 ? 133 TYR A CB 1 ATOM 1041 C CG . TYR A 1 133 ? 40.442 4.749 42.192 1.00 37.51 ? 133 TYR A CG 1 ATOM 1042 C CD1 . TYR A 1 133 ? 40.695 3.551 41.516 1.00 35.62 ? 133 TYR A CD1 1 ATOM 1043 C CD2 . TYR A 1 133 ? 39.425 4.763 43.148 1.00 35.12 ? 133 TYR A CD2 1 ATOM 1044 C CE1 . TYR A 1 133 ? 39.965 2.396 41.790 1.00 33.97 ? 133 TYR A CE1 1 ATOM 1045 C CE2 . TYR A 1 133 ? 38.688 3.614 43.430 1.00 34.51 ? 133 TYR A CE2 1 ATOM 1046 C CZ . TYR A 1 133 ? 38.964 2.433 42.749 1.00 34.94 ? 133 TYR A CZ 1 ATOM 1047 O OH . TYR A 1 133 ? 38.245 1.289 43.029 1.00 33.53 ? 133 TYR A OH 1 ATOM 1048 N N . VAL A 1 134 ? 44.665 7.137 42.654 1.00 46.70 ? 134 VAL A N 1 ATOM 1049 C CA . VAL A 1 134 ? 45.607 8.238 42.461 1.00 49.06 ? 134 VAL A CA 1 ATOM 1050 C C . VAL A 1 134 ? 47.036 7.763 42.719 1.00 50.19 ? 134 VAL A C 1 ATOM 1051 O O . VAL A 1 134 ? 47.943 8.070 41.945 1.00 51.00 ? 134 VAL A O 1 ATOM 1052 C CB . VAL A 1 134 ? 45.307 9.449 43.378 1.00 48.89 ? 134 VAL A CB 1 ATOM 1053 C CG1 . VAL A 1 134 ? 44.323 10.372 42.700 1.00 49.44 ? 134 VAL A CG1 1 ATOM 1054 C CG2 . VAL A 1 134 ? 44.766 8.980 44.717 1.00 49.77 ? 134 VAL A CG2 1 ATOM 1055 N N . ASN A 1 135 ? 47.223 7.014 43.804 1.00 50.45 ? 135 ASN A N 1 ATOM 1056 C CA . ASN A 1 135 ? 48.530 6.473 44.177 1.00 51.82 ? 135 ASN A CA 1 ATOM 1057 C C . ASN A 1 135 ? 49.368 6.025 42.989 1.00 51.20 ? 135 ASN A C 1 ATOM 1058 O O . ASN A 1 135 ? 50.464 6.528 42.770 1.00 52.43 ? 135 ASN A O 1 ATOM 1059 C CB . ASN A 1 135 ? 48.363 5.267 45.099 1.00 55.38 ? 135 ASN A CB 1 ATOM 1060 C CG . ASN A 1 135 ? 47.863 5.644 46.466 1.00 58.84 ? 135 ASN A CG 1 ATOM 1061 O OD1 . ASN A 1 135 ? 47.578 4.773 47.293 1.00 59.91 ? 135 ASN A OD1 1 ATOM 1062 N ND2 . ASN A 1 135 ? 47.756 6.948 46.724 1.00 60.87 ? 135 ASN A ND2 1 ATOM 1063 N N . LYS A 1 136 ? 48.846 5.061 42.237 1.00 49.31 ? 136 LYS A N 1 ATOM 1064 C CA . LYS A 1 136 ? 49.543 4.509 41.082 1.00 46.98 ? 136 LYS A CA 1 ATOM 1065 C C . LYS A 1 136 ? 49.762 5.492 39.932 1.00 45.22 ? 136 LYS A C 1 ATOM 1066 O O . LYS A 1 136 ? 50.092 5.083 38.818 1.00 45.13 ? 136 LYS A O 1 ATOM 1067 C CB . LYS A 1 136 ? 48.796 3.281 40.567 1.00 48.35 ? 136 LYS A CB 1 ATOM 1068 C CG . LYS A 1 136 ? 48.710 2.139 41.570 1.00 52.47 ? 136 LYS A CG 1 ATOM 1069 C CD . LYS A 1 136 ? 47.849 2.496 42.777 1.00 56.51 ? 136 LYS A CD 1 ATOM 1070 C CE . LYS A 1 136 ? 47.652 1.293 43.694 1.00 57.99 ? 136 LYS A CE 1 ATOM 1071 N NZ . LYS A 1 136 ? 48.953 0.796 44.235 1.00 60.14 ? 136 LYS A NZ 1 ATOM 1072 N N . GLY A 1 137 ? 49.567 6.779 40.203 1.00 41.88 ? 137 GLY A N 1 ATOM 1073 C CA . GLY A 1 137 ? 49.769 7.796 39.188 1.00 40.69 ? 137 GLY A CA 1 ATOM 1074 C C . GLY A 1 137 ? 48.848 7.798 37.975 1.00 41.28 ? 137 GLY A C 1 ATOM 1075 O O . GLY A 1 137 ? 49.247 8.281 36.916 1.00 42.38 ? 137 GLY A O 1 ATOM 1076 N N . GLN A 1 138 ? 47.627 7.281 38.111 1.00 39.54 ? 138 GLN A N 1 ATOM 1077 C CA . GLN A 1 138 ? 46.678 7.252 36.994 1.00 37.56 ? 138 GLN A CA 1 ATOM 1078 C C . GLN A 1 138 ? 46.195 8.647 36.603 1.00 35.87 ? 138 GLN A C 1 ATOM 1079 O O . GLN A 1 138 ? 46.052 9.520 37.456 1.00 34.44 ? 138 GLN A O 1 ATOM 1080 C CB . GLN A 1 138 ? 45.446 6.409 37.349 1.00 39.13 ? 138 GLN A CB 1 ATOM 1081 C CG . GLN A 1 138 ? 45.749 4.991 37.802 1.00 39.94 ? 138 GLN A CG 1 ATOM 1082 C CD . GLN A 1 138 ? 45.739 4.845 39.306 1.00 40.37 ? 138 GLN A CD 1 ATOM 1083 O OE1 . GLN A 1 138 ? 46.431 5.575 40.022 1.00 40.65 ? 138 GLN A OE1 1 ATOM 1084 N NE2 . GLN A 1 138 ? 44.952 3.895 39.797 1.00 39.80 ? 138 GLN A NE2 1 ATOM 1085 N N . ASP A 1 139 ? 45.941 8.859 35.314 1.00 34.80 ? 139 ASP A N 1 ATOM 1086 C CA . ASP A 1 139 ? 45.437 10.153 34.865 1.00 35.26 ? 139 ASP A CA 1 ATOM 1087 C C . ASP A 1 139 ? 43.972 10.299 35.285 1.00 34.46 ? 139 ASP A C 1 ATOM 1088 O O . ASP A 1 139 ? 43.237 9.313 35.381 1.00 33.56 ? 139 ASP A O 1 ATOM 1089 C CB . ASP A 1 139 ? 45.532 10.291 33.344 1.00 37.71 ? 139 ASP A CB 1 ATOM 1090 C CG . ASP A 1 139 ? 46.961 10.360 32.849 1.00 40.91 ? 139 ASP A CG 1 ATOM 1091 O OD1 . ASP A 1 139 ? 47.803 10.970 33.538 1.00 43.26 ? 139 ASP A OD1 1 ATOM 1092 O OD2 . ASP A 1 139 ? 47.243 9.822 31.757 1.00 43.28 ? 139 ASP A OD2 1 ATOM 1093 N N . PHE A 1 140 ? 43.549 11.530 35.545 1.00 32.65 ? 140 PHE A N 1 ATOM 1094 C CA . PHE A 1 140 ? 42.168 11.784 35.934 1.00 30.19 ? 140 PHE A CA 1 ATOM 1095 C C . PHE A 1 140 ? 41.545 12.775 34.968 1.00 29.59 ? 140 PHE A C 1 ATOM 1096 O O . PHE A 1 140 ? 42.104 13.838 34.717 1.00 31.00 ? 140 PHE A O 1 ATOM 1097 C CB . PHE A 1 140 ? 42.102 12.346 37.348 1.00 28.13 ? 140 PHE A CB 1 ATOM 1098 C CG . PHE A 1 140 ? 40.737 12.816 37.744 1.00 29.25 ? 140 PHE A CG 1 ATOM 1099 C CD1 . PHE A 1 140 ? 39.699 11.905 37.931 1.00 28.64 ? 140 PHE A CD1 1 ATOM 1100 C CD2 . PHE A 1 140 ? 40.478 14.179 37.913 1.00 30.19 ? 140 PHE A CD2 1 ATOM 1101 C CE1 . PHE A 1 140 ? 38.420 12.342 38.281 1.00 28.78 ? 140 PHE A CE1 1 ATOM 1102 C CE2 . PHE A 1 140 ? 39.200 14.632 38.263 1.00 29.33 ? 140 PHE A CE2 1 ATOM 1103 C CZ . PHE A 1 140 ? 38.170 13.711 38.447 1.00 30.56 ? 140 PHE A CZ 1 ATOM 1104 N N . HIS A 1 141 ? 40.386 12.422 34.428 1.00 29.72 ? 141 HIS A N 1 ATOM 1105 C CA . HIS A 1 141 ? 39.683 13.289 33.488 1.00 29.32 ? 141 HIS A CA 1 ATOM 1106 C C . HIS A 1 141 ? 38.289 13.641 33.994 1.00 30.09 ? 141 HIS A C 1 ATOM 1107 O O . HIS A 1 141 ? 37.741 12.977 34.869 1.00 31.94 ? 141 HIS A O 1 ATOM 1108 C CB . HIS A 1 141 ? 39.534 12.588 32.139 1.00 29.28 ? 141 HIS A CB 1 ATOM 1109 C CG . HIS A 1 141 ? 40.808 12.013 31.610 1.00 30.24 ? 141 HIS A CG 1 ATOM 1110 N ND1 . HIS A 1 141 ? 41.594 12.669 30.688 1.00 29.83 ? 141 HIS A ND1 1 ATOM 1111 C CD2 . HIS A 1 141 ? 41.443 10.851 31.890 1.00 29.43 ? 141 HIS A CD2 1 ATOM 1112 C CE1 . HIS A 1 141 ? 42.660 11.936 30.423 1.00 29.80 ? 141 HIS A CE1 1 ATOM 1113 N NE2 . HIS A 1 141 ? 42.593 10.828 31.140 1.00 31.79 ? 141 HIS A NE2 1 ATOM 1114 N N . ILE A 1 142 ? 37.724 14.704 33.444 1.00 30.52 ? 142 ILE A N 1 ATOM 1115 C CA . ILE A 1 142 ? 36.371 15.108 33.785 1.00 30.24 ? 142 ILE A CA 1 ATOM 1116 C C . ILE A 1 142 ? 35.661 15.178 32.446 1.00 30.61 ? 142 ILE A C 1 ATOM 1117 O O . ILE A 1 142 ? 36.106 15.893 31.548 1.00 32.26 ? 142 ILE A O 1 ATOM 1118 C CB . ILE A 1 142 ? 36.314 16.500 34.436 1.00 29.74 ? 142 ILE A CB 1 ATOM 1119 C CG1 . ILE A 1 142 ? 36.952 16.456 35.826 1.00 29.42 ? 142 ILE A CG1 1 ATOM 1120 C CG2 . ILE A 1 142 ? 34.872 16.954 34.538 1.00 27.46 ? 142 ILE A CG2 1 ATOM 1121 C CD1 . ILE A 1 142 ? 36.858 17.764 36.584 1.00 25.60 ? 142 ILE A CD1 1 ATOM 1122 N N . ALA A 1 143 ? 34.585 14.415 32.293 1.00 29.60 ? 143 ALA A N 1 ATOM 1123 C CA . ALA A 1 143 ? 33.842 14.431 31.041 1.00 28.10 ? 143 ALA A CA 1 ATOM 1124 C C . ALA A 1 143 ? 32.364 14.613 31.327 1.00 27.43 ? 143 ALA A C 1 ATOM 1125 O O . ALA A 1 143 ? 31.862 14.160 32.352 1.00 28.13 ? 143 ALA A O 1 ATOM 1126 C CB . ALA A 1 143 ? 34.071 13.147 30.273 1.00 27.15 ? 143 ALA A CB 1 ATOM 1127 N N . GLY A 1 144 ? 31.675 15.284 30.414 1.00 25.68 ? 144 GLY A N 1 ATOM 1128 C CA . GLY A 1 144 ? 30.258 15.526 30.579 1.00 25.06 ? 144 GLY A CA 1 ATOM 1129 C C . GLY A 1 144 ? 29.658 16.050 29.290 1.00 27.08 ? 144 GLY A C 1 ATOM 1130 O O . GLY A 1 144 ? 30.382 16.347 28.325 1.00 26.75 ? 144 GLY A O 1 ATOM 1131 N N . GLU A 1 145 ? 28.334 16.176 29.266 1.00 26.31 ? 145 GLU A N 1 ATOM 1132 C CA . GLU A 1 145 ? 27.652 16.654 28.074 1.00 26.44 ? 145 GLU A CA 1 ATOM 1133 C C . GLU A 1 145 ? 26.630 17.725 28.374 1.00 25.63 ? 145 GLU A C 1 ATOM 1134 O O . GLU A 1 145 ? 26.271 17.966 29.529 1.00 23.63 ? 145 GLU A O 1 ATOM 1135 C CB . GLU A 1 145 ? 26.929 15.498 27.384 1.00 27.33 ? 145 GLU A CB 1 ATOM 1136 C CG . GLU A 1 145 ? 25.927 14.808 28.294 1.00 30.48 ? 145 GLU A CG 1 ATOM 1137 C CD . GLU A 1 145 ? 25.073 13.785 27.570 1.00 33.51 ? 145 GLU A CD 1 ATOM 1138 O OE1 . GLU A 1 145 ? 25.640 12.943 26.840 1.00 34.40 ? 145 GLU A OE1 1 ATOM 1139 O OE2 . GLU A 1 145 ? 23.834 13.817 27.745 1.00 34.15 ? 145 GLU A OE2 1 ATOM 1140 N N . SER A 1 146 ? 26.172 18.367 27.305 1.00 25.38 ? 146 SER A N 1 ATOM 1141 C CA . SER A 1 146 ? 25.132 19.376 27.402 1.00 24.75 ? 146 SER A CA 1 ATOM 1142 C C . SER A 1 146 ? 25.481 20.586 28.268 1.00 24.60 ? 146 SER A C 1 ATOM 1143 O O . SER A 1 146 ? 26.432 21.307 27.990 1.00 24.29 ? 146 SER A O 1 ATOM 1144 C CB . SER A 1 146 ? 23.864 18.706 27.930 1.00 21.76 ? 146 SER A CB 1 ATOM 1145 O OG . SER A 1 146 ? 22.761 19.564 27.792 1.00 24.62 ? 146 SER A OG 1 ATOM 1146 N N . TYR A 1 147 ? 24.699 20.805 29.320 1.00 24.69 ? 147 TYR A N 1 ATOM 1147 C CA . TYR A 1 147 ? 24.927 21.937 30.203 1.00 23.37 ? 147 TYR A CA 1 ATOM 1148 C C . TYR A 1 147 ? 26.250 21.795 30.944 1.00 23.39 ? 147 TYR A C 1 ATOM 1149 O O . TYR A 1 147 ? 26.713 22.743 31.588 1.00 22.91 ? 147 TYR A O 1 ATOM 1150 C CB . TYR A 1 147 ? 23.778 22.086 31.209 1.00 22.36 ? 147 TYR A CB 1 ATOM 1151 C CG . TYR A 1 147 ? 23.688 23.475 31.802 1.00 23.53 ? 147 TYR A CG 1 ATOM 1152 C CD1 . TYR A 1 147 ? 23.165 24.539 31.063 1.00 23.01 ? 147 TYR A CD1 1 ATOM 1153 C CD2 . TYR A 1 147 ? 24.155 23.736 33.088 1.00 23.35 ? 147 TYR A CD2 1 ATOM 1154 C CE1 . TYR A 1 147 ? 23.109 25.822 31.589 1.00 21.41 ? 147 TYR A CE1 1 ATOM 1155 C CE2 . TYR A 1 147 ? 24.103 25.018 33.622 1.00 21.88 ? 147 TYR A CE2 1 ATOM 1156 C CZ . TYR A 1 147 ? 23.581 26.054 32.870 1.00 21.63 ? 147 TYR A CZ 1 ATOM 1157 O OH . TYR A 1 147 ? 23.540 27.323 33.402 1.00 21.68 ? 147 TYR A OH 1 ATOM 1158 N N . ALA A 1 148 ? 26.858 20.613 30.866 1.00 22.27 ? 148 ALA A N 1 ATOM 1159 C CA . ALA A 1 148 ? 28.147 20.416 31.522 1.00 23.76 ? 148 ALA A CA 1 ATOM 1160 C C . ALA A 1 148 ? 29.135 21.326 30.788 1.00 23.06 ? 148 ALA A C 1 ATOM 1161 O O . ALA A 1 148 ? 30.266 21.527 31.223 1.00 22.71 ? 148 ALA A O 1 ATOM 1162 C CB . ALA A 1 148 ? 28.587 18.953 31.441 1.00 24.05 ? 148 ALA A CB 1 ATOM 1163 N N . GLY A 1 149 ? 28.681 21.869 29.661 1.00 23.13 ? 149 GLY A N 1 ATOM 1164 C CA . GLY A 1 149 ? 29.493 22.793 28.892 1.00 24.04 ? 149 GLY A CA 1 ATOM 1165 C C . GLY A 1 149 ? 29.714 24.024 29.755 1.00 25.97 ? 149 GLY A C 1 ATOM 1166 O O . GLY A 1 149 ? 30.638 24.813 29.516 1.00 25.14 ? 149 GLY A O 1 ATOM 1167 N N . HIS A 1 150 ? 28.838 24.200 30.746 1.00 24.80 ? 150 HIS A N 1 ATOM 1168 C CA . HIS A 1 150 ? 28.971 25.297 31.694 1.00 25.17 ? 150 HIS A CA 1 ATOM 1169 C C . HIS A 1 150 ? 29.859 24.761 32.820 1.00 26.60 ? 150 HIS A C 1 ATOM 1170 O O . HIS A 1 150 ? 30.893 25.351 33.139 1.00 27.91 ? 150 HIS A O 1 ATOM 1171 C CB . HIS A 1 150 ? 27.620 25.695 32.288 1.00 25.03 ? 150 HIS A CB 1 ATOM 1172 C CG . HIS A 1 150 ? 26.881 26.738 31.506 1.00 26.10 ? 150 HIS A CG 1 ATOM 1173 N ND1 . HIS A 1 150 ? 26.742 26.690 30.135 1.00 26.99 ? 150 HIS A ND1 1 ATOM 1174 C CD2 . HIS A 1 150 ? 26.189 27.830 31.916 1.00 24.74 ? 150 HIS A CD2 1 ATOM 1175 C CE1 . HIS A 1 150 ? 25.998 27.706 29.735 1.00 24.85 ? 150 HIS A CE1 1 ATOM 1176 N NE2 . HIS A 1 150 ? 25.649 28.412 30.796 1.00 24.10 ? 150 HIS A NE2 1 ATOM 1177 N N . TYR A 1 151 ? 29.467 23.620 33.393 1.00 25.45 ? 151 TYR A N 1 ATOM 1178 C CA . TYR A 1 151 ? 30.204 23.017 34.503 1.00 26.24 ? 151 TYR A CA 1 ATOM 1179 C C . TYR A 1 151 ? 31.700 22.811 34.298 1.00 27.63 ? 151 TYR A C 1 ATOM 1180 O O . TYR A 1 151 ? 32.512 23.425 34.984 1.00 30.09 ? 151 TYR A O 1 ATOM 1181 C CB . TYR A 1 151 ? 29.635 21.650 34.889 1.00 26.06 ? 151 TYR A CB 1 ATOM 1182 C CG . TYR A 1 151 ? 28.160 21.574 35.232 1.00 27.38 ? 151 TYR A CG 1 ATOM 1183 C CD1 . TYR A 1 151 ? 27.507 22.602 35.921 1.00 25.00 ? 151 TYR A CD1 1 ATOM 1184 C CD2 . TYR A 1 151 ? 27.433 20.416 34.930 1.00 26.03 ? 151 TYR A CD2 1 ATOM 1185 C CE1 . TYR A 1 151 ? 26.166 22.467 36.299 1.00 26.37 ? 151 TYR A CE1 1 ATOM 1186 C CE2 . TYR A 1 151 ? 26.113 20.273 35.302 1.00 26.71 ? 151 TYR A CE2 1 ATOM 1187 C CZ . TYR A 1 151 ? 25.483 21.294 35.982 1.00 27.61 ? 151 TYR A CZ 1 ATOM 1188 O OH . TYR A 1 151 ? 24.167 21.120 36.319 1.00 29.78 ? 151 TYR A OH 1 ATOM 1189 N N . ILE A 1 152 ? 32.053 21.932 33.364 1.00 27.92 ? 152 ILE A N 1 ATOM 1190 C CA . ILE A 1 152 ? 33.444 21.582 33.108 1.00 27.61 ? 152 ILE A CA 1 ATOM 1191 C C . ILE A 1 152 ? 34.476 22.704 33.138 1.00 27.46 ? 152 ILE A C 1 ATOM 1192 O O . ILE A 1 152 ? 35.400 22.672 33.946 1.00 26.52 ? 152 ILE A O 1 ATOM 1193 C CB . ILE A 1 152 ? 33.606 20.843 31.775 1.00 28.52 ? 152 ILE A CB 1 ATOM 1194 C CG1 . ILE A 1 152 ? 32.604 19.689 31.678 1.00 29.58 ? 152 ILE A CG1 1 ATOM 1195 C CG2 . ILE A 1 152 ? 35.024 20.317 31.665 1.00 26.26 ? 152 ILE A CG2 1 ATOM 1196 C CD1 . ILE A 1 152 ? 32.753 18.650 32.734 1.00 29.92 ? 152 ILE A CD1 1 ATOM 1197 N N . PRO A 1 153 ? 34.350 23.704 32.256 1.00 27.91 ? 153 PRO A N 1 ATOM 1198 C CA . PRO A 1 153 ? 35.369 24.754 32.321 1.00 27.12 ? 153 PRO A CA 1 ATOM 1199 C C . PRO A 1 153 ? 35.474 25.411 33.698 1.00 27.60 ? 153 PRO A C 1 ATOM 1200 O O . PRO A 1 153 ? 36.570 25.566 34.225 1.00 29.08 ? 153 PRO A O 1 ATOM 1201 C CB . PRO A 1 153 ? 34.958 25.716 31.200 1.00 26.04 ? 153 PRO A CB 1 ATOM 1202 C CG . PRO A 1 153 ? 33.498 25.503 31.067 1.00 28.58 ? 153 PRO A CG 1 ATOM 1203 C CD . PRO A 1 153 ? 33.325 24.014 31.245 1.00 29.43 ? 153 PRO A CD 1 ATOM 1204 N N . VAL A 1 154 ? 34.349 25.781 34.299 1.00 27.10 ? 154 VAL A N 1 ATOM 1205 C CA . VAL A 1 154 ? 34.409 26.396 35.619 1.00 26.85 ? 154 VAL A CA 1 ATOM 1206 C C . VAL A 1 154 ? 34.972 25.410 36.644 1.00 28.25 ? 154 VAL A C 1 ATOM 1207 O O . VAL A 1 154 ? 35.844 25.761 37.443 1.00 28.72 ? 154 VAL A O 1 ATOM 1208 C CB . VAL A 1 154 ? 33.026 26.860 36.098 1.00 25.28 ? 154 VAL A CB 1 ATOM 1209 C CG1 . VAL A 1 154 ? 33.134 27.385 37.514 1.00 19.82 ? 154 VAL A CG1 1 ATOM 1210 C CG2 . VAL A 1 154 ? 32.486 27.946 35.171 1.00 23.57 ? 154 VAL A CG2 1 ATOM 1211 N N . PHE A 1 155 ? 34.468 24.179 36.614 1.00 28.40 ? 155 PHE A N 1 ATOM 1212 C CA . PHE A 1 155 ? 34.919 23.133 37.525 1.00 28.48 ? 155 PHE A CA 1 ATOM 1213 C C . PHE A 1 155 ? 36.432 22.946 37.460 1.00 30.63 ? 155 PHE A C 1 ATOM 1214 O O . PHE A 1 155 ? 37.110 22.920 38.491 1.00 30.68 ? 155 PHE A O 1 ATOM 1215 C CB . PHE A 1 155 ? 34.231 21.808 37.191 1.00 26.02 ? 155 PHE A CB 1 ATOM 1216 C CG . PHE A 1 155 ? 32.809 21.713 37.677 1.00 25.91 ? 155 PHE A CG 1 ATOM 1217 C CD1 . PHE A 1 155 ? 32.121 22.845 38.109 1.00 23.71 ? 155 PHE A CD1 1 ATOM 1218 C CD2 . PHE A 1 155 ? 32.142 20.483 37.667 1.00 24.98 ? 155 PHE A CD2 1 ATOM 1219 C CE1 . PHE A 1 155 ? 30.789 22.751 38.520 1.00 26.88 ? 155 PHE A CE1 1 ATOM 1220 C CE2 . PHE A 1 155 ? 30.808 20.377 38.074 1.00 22.07 ? 155 PHE A CE2 1 ATOM 1221 C CZ . PHE A 1 155 ? 30.129 21.506 38.499 1.00 23.07 ? 155 PHE A CZ 1 ATOM 1222 N N . ALA A 1 156 ? 36.958 22.818 36.245 1.00 31.89 ? 156 ALA A N 1 ATOM 1223 C CA . ALA A 1 156 ? 38.388 22.628 36.053 1.00 32.43 ? 156 ALA A CA 1 ATOM 1224 C C . ALA A 1 156 ? 39.177 23.784 36.668 1.00 34.02 ? 156 ALA A C 1 ATOM 1225 O O . ALA A 1 156 ? 40.215 23.562 37.299 1.00 34.56 ? 156 ALA A O 1 ATOM 1226 C CB . ALA A 1 156 ? 38.703 22.495 34.569 1.00 31.20 ? 156 ALA A CB 1 ATOM 1227 N N . SER A 1 157 ? 38.689 25.012 36.488 1.00 34.21 ? 157 SER A N 1 ATOM 1228 C CA . SER A 1 157 ? 39.356 26.184 37.055 1.00 35.44 ? 157 SER A CA 1 ATOM 1229 C C . SER A 1 157 ? 39.373 26.098 38.571 1.00 36.38 ? 157 SER A C 1 ATOM 1230 O O . SER A 1 157 ? 40.398 26.331 39.208 1.00 36.34 ? 157 SER A O 1 ATOM 1231 C CB . SER A 1 157 ? 38.646 27.471 36.649 1.00 33.80 ? 157 SER A CB 1 ATOM 1232 O OG . SER A 1 157 ? 38.849 27.735 35.279 1.00 37.30 ? 157 SER A OG 1 ATOM 1233 N N . GLU A 1 158 ? 38.228 25.767 39.150 1.00 36.57 ? 158 GLU A N 1 ATOM 1234 C CA . GLU A 1 158 ? 38.147 25.649 40.590 1.00 38.91 ? 158 GLU A CA 1 ATOM 1235 C C . GLU A 1 158 ? 39.236 24.719 41.118 1.00 39.39 ? 158 GLU A C 1 ATOM 1236 O O . GLU A 1 158 ? 40.020 25.112 41.979 1.00 39.46 ? 158 GLU A O 1 ATOM 1237 C CB . GLU A 1 158 ? 36.770 25.124 40.995 1.00 41.48 ? 158 GLU A CB 1 ATOM 1238 C CG . GLU A 1 158 ? 36.535 25.002 42.499 1.00 44.39 ? 158 GLU A CG 1 ATOM 1239 C CD . GLU A 1 158 ? 36.609 26.334 43.224 1.00 46.97 ? 158 GLU A CD 1 ATOM 1240 O OE1 . GLU A 1 158 ? 36.268 27.370 42.613 1.00 49.39 ? 158 GLU A OE1 1 ATOM 1241 O OE2 . GLU A 1 158 ? 36.992 26.343 44.412 1.00 48.06 ? 158 GLU A OE2 1 ATOM 1242 N N . ILE A 1 159 ? 39.315 23.500 40.590 1.00 39.88 ? 159 ILE A N 1 ATOM 1243 C CA . ILE A 1 159 ? 40.310 22.555 41.091 1.00 41.09 ? 159 ILE A CA 1 ATOM 1244 C C . ILE A 1 159 ? 41.772 22.969 40.837 1.00 41.34 ? 159 ILE A C 1 ATOM 1245 O O . ILE A 1 159 ? 42.645 22.696 41.663 1.00 40.26 ? 159 ILE A O 1 ATOM 1246 C CB . ILE A 1 159 ? 40.067 21.104 40.545 1.00 40.49 ? 159 ILE A CB 1 ATOM 1247 C CG1 . ILE A 1 159 ? 40.700 20.938 39.175 1.00 41.45 ? 159 ILE A CG1 1 ATOM 1248 C CG2 . ILE A 1 159 ? 38.586 20.793 40.473 1.00 38.93 ? 159 ILE A CG2 1 ATOM 1249 C CD1 . ILE A 1 159 ? 42.099 20.384 39.251 1.00 43.32 ? 159 ILE A CD1 1 ATOM 1250 N N . LEU A 1 160 ? 42.043 23.633 39.716 1.00 41.12 ? 160 LEU A N 1 ATOM 1251 C CA . LEU A 1 160 ? 43.412 24.052 39.416 1.00 41.36 ? 160 LEU A CA 1 ATOM 1252 C C . LEU A 1 160 ? 43.892 25.266 40.210 1.00 42.58 ? 160 LEU A C 1 ATOM 1253 O O . LEU A 1 160 ? 45.077 25.592 40.185 1.00 43.79 ? 160 LEU A O 1 ATOM 1254 C CB . LEU A 1 160 ? 43.582 24.337 37.920 1.00 39.22 ? 160 LEU A CB 1 ATOM 1255 C CG . LEU A 1 160 ? 43.636 23.127 36.981 1.00 39.02 ? 160 LEU A CG 1 ATOM 1256 C CD1 . LEU A 1 160 ? 43.976 23.588 35.580 1.00 39.32 ? 160 LEU A CD1 1 ATOM 1257 C CD2 . LEU A 1 160 ? 44.675 22.141 37.459 1.00 37.61 ? 160 LEU A CD2 1 ATOM 1258 N N . SER A 1 161 ? 42.985 25.941 40.909 1.00 43.45 ? 161 SER A N 1 ATOM 1259 C CA . SER A 1 161 ? 43.376 27.104 41.696 1.00 43.71 ? 161 SER A CA 1 ATOM 1260 C C . SER A 1 161 ? 43.808 26.664 43.092 1.00 45.45 ? 161 SER A C 1 ATOM 1261 O O . SER A 1 161 ? 44.419 27.427 43.834 1.00 45.97 ? 161 SER A O 1 ATOM 1262 C CB . SER A 1 161 ? 42.230 28.117 41.780 1.00 42.00 ? 161 SER A CB 1 ATOM 1263 O OG . SER A 1 161 ? 41.140 27.614 42.521 1.00 40.96 ? 161 SER A OG 1 ATOM 1264 N N . HIS A 1 162 ? 43.495 25.424 43.445 1.00 47.28 ? 162 HIS A N 1 ATOM 1265 C CA . HIS A 1 162 ? 43.888 24.887 44.739 1.00 49.97 ? 162 HIS A CA 1 ATOM 1266 C C . HIS A 1 162 ? 45.281 24.293 44.588 1.00 52.86 ? 162 HIS A C 1 ATOM 1267 O O . HIS A 1 162 ? 45.510 23.422 43.747 1.00 53.02 ? 162 HIS A O 1 ATOM 1268 C CB . HIS A 1 162 ? 42.904 23.812 45.190 1.00 49.24 ? 162 HIS A CB 1 ATOM 1269 C CG . HIS A 1 162 ? 41.562 24.352 45.565 1.00 49.57 ? 162 HIS A CG 1 ATOM 1270 N ND1 . HIS A 1 162 ? 41.281 24.832 46.824 1.00 50.06 ? 162 HIS A ND1 1 ATOM 1271 C CD2 . HIS A 1 162 ? 40.438 24.533 44.834 1.00 49.99 ? 162 HIS A CD2 1 ATOM 1272 C CE1 . HIS A 1 162 ? 40.040 25.284 46.854 1.00 50.34 ? 162 HIS A CE1 1 ATOM 1273 N NE2 . HIS A 1 162 ? 39.506 25.115 45.658 1.00 49.60 ? 162 HIS A NE2 1 ATOM 1274 N N . LYS A 1 163 ? 46.215 24.777 45.399 1.00 55.74 ? 163 LYS A N 1 ATOM 1275 C CA . LYS A 1 163 ? 47.591 24.300 45.344 1.00 58.21 ? 163 LYS A CA 1 ATOM 1276 C C . LYS A 1 163 ? 47.761 23.058 46.208 1.00 57.98 ? 163 LYS A C 1 ATOM 1277 O O . LYS A 1 163 ? 48.648 22.243 45.983 1.00 57.81 ? 163 LYS A O 1 ATOM 1278 C CB . LYS A 1 163 ? 48.530 25.404 45.834 1.00 60.83 ? 163 LYS A CB 1 ATOM 1279 C CG . LYS A 1 163 ? 48.397 26.728 45.078 1.00 65.36 ? 163 LYS A CG 1 ATOM 1280 C CD . LYS A 1 163 ? 49.237 26.765 43.796 1.00 68.44 ? 163 LYS A CD 1 ATOM 1281 C CE . LYS A 1 163 ? 48.832 25.693 42.785 1.00 71.34 ? 163 LYS A CE 1 ATOM 1282 N NZ . LYS A 1 163 ? 47.427 25.849 42.306 1.00 73.32 ? 163 LYS A NZ 1 ATOM 1283 N N . ASP A 1 164 ? 46.877 22.921 47.184 1.00 58.13 ? 164 ASP A N 1 ATOM 1284 C CA . ASP A 1 164 ? 46.900 21.819 48.131 1.00 58.79 ? 164 ASP A CA 1 ATOM 1285 C C . ASP A 1 164 ? 46.040 20.615 47.744 1.00 57.67 ? 164 ASP A C 1 ATOM 1286 O O . ASP A 1 164 ? 45.844 19.712 48.557 1.00 58.50 ? 164 ASP A O 1 ATOM 1287 C CB . ASP A 1 164 ? 46.432 22.346 49.485 1.00 62.50 ? 164 ASP A CB 1 ATOM 1288 C CG . ASP A 1 164 ? 45.103 23.104 49.386 1.00 66.60 ? 164 ASP A CG 1 ATOM 1289 O OD1 . ASP A 1 164 ? 45.022 24.095 48.620 1.00 67.15 ? 164 ASP A OD1 1 ATOM 1290 O OD2 . ASP A 1 164 ? 44.136 22.706 50.072 1.00 68.81 ? 164 ASP A OD2 1 ATOM 1291 N N . ARG A 1 165 ? 45.524 20.589 46.520 1.00 55.63 ? 165 ARG A N 1 ATOM 1292 C CA . ARG A 1 165 ? 44.663 19.481 46.105 1.00 52.91 ? 165 ARG A CA 1 ATOM 1293 C C . ARG A 1 165 ? 45.392 18.139 46.196 1.00 51.17 ? 165 ARG A C 1 ATOM 1294 O O . ARG A 1 165 ? 46.610 18.078 46.024 1.00 51.23 ? 165 ARG A O 1 ATOM 1295 C CB . ARG A 1 165 ? 44.153 19.716 44.679 1.00 50.95 ? 165 ARG A CB 1 ATOM 1296 C CG . ARG A 1 165 ? 45.135 19.341 43.592 1.00 49.77 ? 165 ARG A CG 1 ATOM 1297 C CD . ARG A 1 165 ? 44.579 19.684 42.229 1.00 47.16 ? 165 ARG A CD 1 ATOM 1298 N NE . ARG A 1 165 ? 45.161 20.915 41.720 1.00 46.19 ? 165 ARG A NE 1 ATOM 1299 C CZ . ARG A 1 165 ? 46.260 20.964 40.980 1.00 44.93 ? 165 ARG A CZ 1 ATOM 1300 N NH1 . ARG A 1 165 ? 46.890 19.845 40.657 1.00 46.23 ? 165 ARG A NH1 1 ATOM 1301 N NH2 . ARG A 1 165 ? 46.732 22.129 40.569 1.00 46.17 ? 165 ARG A NH2 1 ATOM 1302 N N . ASN A 1 166 ? 44.648 17.069 46.472 1.00 48.33 ? 166 ASN A N 1 ATOM 1303 C CA . ASN A 1 166 ? 45.246 15.744 46.589 1.00 46.64 ? 166 ASN A CA 1 ATOM 1304 C C . ASN A 1 166 ? 45.130 14.880 45.340 1.00 45.56 ? 166 ASN A C 1 ATOM 1305 O O . ASN A 1 166 ? 45.210 13.655 45.425 1.00 45.30 ? 166 ASN A O 1 ATOM 1306 C CB . ASN A 1 166 ? 44.650 14.980 47.776 1.00 48.11 ? 166 ASN A CB 1 ATOM 1307 C CG . ASN A 1 166 ? 43.146 14.810 47.674 1.00 49.89 ? 166 ASN A CG 1 ATOM 1308 O OD1 . ASN A 1 166 ? 42.562 14.911 46.592 1.00 51.59 ? 166 ASN A OD1 1 ATOM 1309 N ND2 . ASN A 1 166 ? 42.510 14.535 48.807 1.00 49.55 ? 166 ASN A ND2 1 ATOM 1310 N N . PHE A 1 167 ? 44.940 15.512 44.185 1.00 43.84 ? 167 PHE A N 1 ATOM 1311 C CA . PHE A 1 167 ? 44.836 14.788 42.920 1.00 42.43 ? 167 PHE A CA 1 ATOM 1312 C C . PHE A 1 167 ? 45.140 15.744 41.771 1.00 41.62 ? 167 PHE A C 1 ATOM 1313 O O . PHE A 1 167 ? 45.238 16.947 41.977 1.00 40.22 ? 167 PHE A O 1 ATOM 1314 C CB . PHE A 1 167 ? 43.425 14.205 42.739 1.00 41.50 ? 167 PHE A CB 1 ATOM 1315 C CG . PHE A 1 167 ? 42.351 15.251 42.599 1.00 40.67 ? 167 PHE A CG 1 ATOM 1316 C CD1 . PHE A 1 167 ? 41.823 15.885 43.723 1.00 40.53 ? 167 PHE A CD1 1 ATOM 1317 C CD2 . PHE A 1 167 ? 41.897 15.634 41.339 1.00 39.04 ? 167 PHE A CD2 1 ATOM 1318 C CE1 . PHE A 1 167 ? 40.860 16.890 43.592 1.00 40.65 ? 167 PHE A CE1 1 ATOM 1319 C CE2 . PHE A 1 167 ? 40.937 16.637 41.197 1.00 39.81 ? 167 PHE A CE2 1 ATOM 1320 C CZ . PHE A 1 167 ? 40.417 17.268 42.325 1.00 40.09 ? 167 PHE A CZ 1 ATOM 1321 N N . ASN A 1 168 ? 45.293 15.211 40.564 1.00 42.98 ? 168 ASN A N 1 ATOM 1322 C CA . ASN A 1 168 ? 45.562 16.058 39.407 1.00 45.51 ? 168 ASN A CA 1 ATOM 1323 C C . ASN A 1 168 ? 44.494 15.949 38.328 1.00 43.36 ? 168 ASN A C 1 ATOM 1324 O O . ASN A 1 168 ? 43.715 15.002 38.312 1.00 44.72 ? 168 ASN A O 1 ATOM 1325 C CB . ASN A 1 168 ? 46.925 15.734 38.796 1.00 50.67 ? 168 ASN A CB 1 ATOM 1326 C CG . ASN A 1 168 ? 48.058 16.410 39.522 1.00 56.40 ? 168 ASN A CG 1 ATOM 1327 O OD1 . ASN A 1 168 ? 47.975 17.594 39.850 1.00 56.17 ? 168 ASN A OD1 1 ATOM 1328 N ND2 . ASN A 1 168 ? 49.129 15.665 39.763 1.00 63.38 ? 168 ASN A ND2 1 ATOM 1329 N N . LEU A 1 169 ? 44.475 16.928 37.429 1.00 39.97 ? 169 LEU A N 1 ATOM 1330 C CA . LEU A 1 169 ? 43.512 16.970 36.339 1.00 37.33 ? 169 LEU A CA 1 ATOM 1331 C C . LEU A 1 169 ? 44.255 16.874 35.015 1.00 36.20 ? 169 LEU A C 1 ATOM 1332 O O . LEU A 1 169 ? 44.948 17.804 34.623 1.00 37.19 ? 169 LEU A O 1 ATOM 1333 C CB . LEU A 1 169 ? 42.722 18.277 36.412 1.00 36.60 ? 169 LEU A CB 1 ATOM 1334 C CG . LEU A 1 169 ? 41.650 18.518 35.351 1.00 36.35 ? 169 LEU A CG 1 ATOM 1335 C CD1 . LEU A 1 169 ? 40.687 17.346 35.324 1.00 35.34 ? 169 LEU A CD1 1 ATOM 1336 C CD2 . LEU A 1 169 ? 40.918 19.819 35.659 1.00 35.66 ? 169 LEU A CD2 1 ATOM 1337 N N . THR A 1 170 ? 44.099 15.752 34.321 1.00 35.54 ? 170 THR A N 1 ATOM 1338 C CA . THR A 1 170 ? 44.792 15.534 33.053 1.00 33.54 ? 170 THR A CA 1 ATOM 1339 C C . THR A 1 170 ? 44.150 16.205 31.837 1.00 34.30 ? 170 THR A C 1 ATOM 1340 O O . THR A 1 170 ? 44.856 16.727 30.972 1.00 34.14 ? 170 THR A O 1 ATOM 1341 C CB . THR A 1 170 ? 44.928 14.029 32.761 1.00 34.42 ? 170 THR A CB 1 ATOM 1342 O OG1 . THR A 1 170 ? 45.486 13.366 33.902 1.00 33.88 ? 170 THR A OG1 1 ATOM 1343 C CG2 . THR A 1 170 ? 45.834 13.802 31.570 1.00 33.11 ? 170 THR A CG2 1 ATOM 1344 N N . SER A 1 171 ? 42.820 16.172 31.755 1.00 33.17 ? 171 SER A N 1 ATOM 1345 C CA . SER A 1 171 ? 42.105 16.793 30.639 1.00 31.24 ? 171 SER A CA 1 ATOM 1346 C C . SER A 1 171 ? 40.605 16.756 30.862 1.00 30.60 ? 171 SER A C 1 ATOM 1347 O O . SER A 1 171 ? 40.120 16.104 31.786 1.00 30.98 ? 171 SER A O 1 ATOM 1348 C CB . SER A 1 171 ? 42.402 16.068 29.327 1.00 32.66 ? 171 SER A CB 1 ATOM 1349 O OG . SER A 1 171 ? 41.514 14.975 29.145 1.00 31.77 ? 171 SER A OG 1 ATOM 1350 N N . VAL A 1 172 ? 39.869 17.448 30.000 1.00 28.92 ? 172 VAL A N 1 ATOM 1351 C CA . VAL A 1 172 ? 38.421 17.470 30.101 1.00 28.59 ? 172 VAL A CA 1 ATOM 1352 C C . VAL A 1 172 ? 37.797 17.245 28.731 1.00 30.06 ? 172 VAL A C 1 ATOM 1353 O O . VAL A 1 172 ? 38.345 17.671 27.714 1.00 30.75 ? 172 VAL A O 1 ATOM 1354 C CB . VAL A 1 172 ? 37.917 18.807 30.673 1.00 26.11 ? 172 VAL A CB 1 ATOM 1355 C CG1 . VAL A 1 172 ? 38.537 19.048 32.033 1.00 23.75 ? 172 VAL A CG1 1 ATOM 1356 C CG2 . VAL A 1 172 ? 38.251 19.946 29.720 1.00 25.47 ? 172 VAL A CG2 1 ATOM 1357 N N . LEU A 1 173 ? 36.658 16.557 28.715 1.00 29.95 ? 173 LEU A N 1 ATOM 1358 C CA . LEU A 1 173 ? 35.936 16.271 27.482 1.00 28.66 ? 173 LEU A CA 1 ATOM 1359 C C . LEU A 1 173 ? 34.559 16.897 27.584 1.00 28.70 ? 173 LEU A C 1 ATOM 1360 O O . LEU A 1 173 ? 33.923 16.834 28.636 1.00 30.76 ? 173 LEU A O 1 ATOM 1361 C CB . LEU A 1 173 ? 35.777 14.765 27.279 1.00 28.23 ? 173 LEU A CB 1 ATOM 1362 C CG . LEU A 1 173 ? 37.042 13.916 27.150 1.00 29.41 ? 173 LEU A CG 1 ATOM 1363 C CD1 . LEU A 1 173 ? 37.691 13.716 28.517 1.00 28.27 ? 173 LEU A CD1 1 ATOM 1364 C CD2 . LEU A 1 173 ? 36.670 12.576 26.552 1.00 28.91 ? 173 LEU A CD2 1 ATOM 1365 N N . ILE A 1 174 ? 34.095 17.503 26.497 1.00 26.75 ? 174 ILE A N 1 ATOM 1366 C CA . ILE A 1 174 ? 32.782 18.128 26.505 1.00 25.17 ? 174 ILE A CA 1 ATOM 1367 C C . ILE A 1 174 ? 32.016 17.843 25.229 1.00 25.23 ? 174 ILE A C 1 ATOM 1368 O O . ILE A 1 174 ? 32.380 18.335 24.162 1.00 26.50 ? 174 ILE A O 1 ATOM 1369 C CB . ILE A 1 174 ? 32.889 19.655 26.673 1.00 24.65 ? 174 ILE A CB 1 ATOM 1370 C CG1 . ILE A 1 174 ? 33.634 19.979 27.972 1.00 23.49 ? 174 ILE A CG1 1 ATOM 1371 C CG2 . ILE A 1 174 ? 31.494 20.274 26.684 1.00 20.59 ? 174 ILE A CG2 1 ATOM 1372 C CD1 . ILE A 1 174 ? 33.770 21.464 28.248 1.00 25.88 ? 174 ILE A CD1 1 ATOM 1373 N N . GLY A 1 175 ? 30.954 17.048 25.348 1.00 23.96 ? 175 GLY A N 1 ATOM 1374 C CA . GLY A 1 175 ? 30.135 16.717 24.194 1.00 21.85 ? 175 GLY A CA 1 ATOM 1375 C C . GLY A 1 175 ? 28.824 17.486 24.134 1.00 20.28 ? 175 GLY A C 1 ATOM 1376 O O . GLY A 1 175 ? 28.144 17.657 25.149 1.00 20.13 ? 175 GLY A O 1 ATOM 1377 N N . ASN A 1 176 ? 28.471 17.942 22.936 1.00 19.85 ? 176 ASN A N 1 ATOM 1378 C CA . ASN A 1 176 ? 27.242 18.699 22.688 1.00 20.38 ? 176 ASN A CA 1 ATOM 1379 C C . ASN A 1 176 ? 26.847 19.619 23.840 1.00 22.03 ? 176 ASN A C 1 ATOM 1380 O O . ASN A 1 176 ? 25.739 19.533 24.374 1.00 22.18 ? 176 ASN A O 1 ATOM 1381 C CB . ASN A 1 176 ? 26.095 17.742 22.372 1.00 19.04 ? 176 ASN A CB 1 ATOM 1382 C CG . ASN A 1 176 ? 26.346 16.938 21.114 1.00 20.27 ? 176 ASN A CG 1 ATOM 1383 O OD1 . ASN A 1 176 ? 27.075 15.942 21.129 1.00 18.36 ? 176 ASN A OD1 1 ATOM 1384 N ND2 . ASN A 1 176 ? 25.753 17.374 20.008 1.00 18.89 ? 176 ASN A ND2 1 ATOM 1385 N N . GLY A 1 177 ? 27.759 20.513 24.209 1.00 22.94 ? 177 GLY A N 1 ATOM 1386 C CA . GLY A 1 177 ? 27.495 21.413 25.307 1.00 23.23 ? 177 GLY A CA 1 ATOM 1387 C C . GLY A 1 177 ? 27.235 22.848 24.911 1.00 24.43 ? 177 GLY A C 1 ATOM 1388 O O . GLY A 1 177 ? 27.418 23.235 23.755 1.00 23.93 ? 177 GLY A O 1 ATOM 1389 N N . LEU A 1 178 ? 26.775 23.624 25.889 1.00 24.36 ? 178 LEU A N 1 ATOM 1390 C CA . LEU A 1 178 ? 26.500 25.043 25.725 1.00 24.42 ? 178 LEU A CA 1 ATOM 1391 C C . LEU A 1 178 ? 27.614 25.686 26.557 1.00 26.56 ? 178 LEU A C 1 ATOM 1392 O O . LEU A 1 178 ? 27.633 25.563 27.789 1.00 26.55 ? 178 LEU A O 1 ATOM 1393 C CB . LEU A 1 178 ? 25.132 25.388 26.303 1.00 22.75 ? 178 LEU A CB 1 ATOM 1394 C CG . LEU A 1 178 ? 24.633 26.809 26.055 1.00 25.22 ? 178 LEU A CG 1 ATOM 1395 C CD1 . LEU A 1 178 ? 24.488 27.042 24.547 1.00 24.68 ? 178 LEU A CD1 1 ATOM 1396 C CD2 . LEU A 1 178 ? 23.303 27.022 26.770 1.00 23.34 ? 178 LEU A CD2 1 ATOM 1397 N N . THR A 1 179 ? 28.543 26.354 25.880 1.00 25.48 ? 179 THR A N 1 ATOM 1398 C CA . THR A 1 179 ? 29.682 26.952 26.552 1.00 27.60 ? 179 THR A CA 1 ATOM 1399 C C . THR A 1 179 ? 29.849 28.445 26.291 1.00 28.94 ? 179 THR A C 1 ATOM 1400 O O . THR A 1 179 ? 30.182 29.207 27.199 1.00 28.65 ? 179 THR A O 1 ATOM 1401 C CB . THR A 1 179 ? 30.969 26.215 26.127 1.00 28.96 ? 179 THR A CB 1 ATOM 1402 O OG1 . THR A 1 179 ? 30.886 24.842 26.537 1.00 26.95 ? 179 THR A OG1 1 ATOM 1403 C CG2 . THR A 1 179 ? 32.195 26.861 26.738 1.00 27.63 ? 179 THR A CG2 1 ATOM 1404 N N . ASP A 1 180 ? 29.614 28.857 25.049 1.00 28.64 ? 180 ASP A N 1 ATOM 1405 C CA . ASP A 1 180 ? 29.753 30.253 24.653 1.00 26.48 ? 180 ASP A CA 1 ATOM 1406 C C . ASP A 1 180 ? 28.475 30.691 23.937 1.00 26.26 ? 180 ASP A C 1 ATOM 1407 O O . ASP A 1 180 ? 28.420 30.762 22.708 1.00 26.18 ? 180 ASP A O 1 ATOM 1408 C CB . ASP A 1 180 ? 31.000 30.377 23.765 1.00 27.22 ? 180 ASP A CB 1 ATOM 1409 C CG . ASP A 1 180 ? 31.152 31.745 23.118 1.00 30.75 ? 180 ASP A CG 1 ATOM 1410 O OD1 . ASP A 1 180 ? 30.732 32.769 23.715 1.00 28.29 ? 180 ASP A OD1 1 ATOM 1411 O OD2 . ASP A 1 180 ? 31.721 31.781 22.000 1.00 30.27 ? 180 ASP A OD2 1 ATOM 1412 N N . PRO A 1 181 ? 27.422 30.994 24.719 1.00 26.52 ? 181 PRO A N 1 ATOM 1413 C CA . PRO A 1 181 ? 26.094 31.428 24.269 1.00 27.05 ? 181 PRO A CA 1 ATOM 1414 C C . PRO A 1 181 ? 26.094 32.500 23.191 1.00 28.61 ? 181 PRO A C 1 ATOM 1415 O O . PRO A 1 181 ? 25.365 32.384 22.195 1.00 29.27 ? 181 PRO A O 1 ATOM 1416 C CB . PRO A 1 181 ? 25.435 31.924 25.554 1.00 25.82 ? 181 PRO A CB 1 ATOM 1417 C CG . PRO A 1 181 ? 26.039 31.077 26.582 1.00 25.73 ? 181 PRO A CG 1 ATOM 1418 C CD . PRO A 1 181 ? 27.499 31.054 26.188 1.00 26.23 ? 181 PRO A CD 1 ATOM 1419 N N . LEU A 1 182 ? 26.894 33.546 23.395 1.00 27.19 ? 182 LEU A N 1 ATOM 1420 C CA . LEU A 1 182 ? 26.962 34.633 22.429 1.00 26.77 ? 182 LEU A CA 1 ATOM 1421 C C . LEU A 1 182 ? 27.259 34.105 21.020 1.00 27.55 ? 182 LEU A C 1 ATOM 1422 O O . LEU A 1 182 ? 26.648 34.552 20.044 1.00 27.68 ? 182 LEU A O 1 ATOM 1423 C CB . LEU A 1 182 ? 28.027 35.651 22.844 1.00 25.26 ? 182 LEU A CB 1 ATOM 1424 C CG . LEU A 1 182 ? 28.171 36.870 21.924 1.00 24.86 ? 182 LEU A CG 1 ATOM 1425 C CD1 . LEU A 1 182 ? 26.888 37.697 21.925 1.00 22.42 ? 182 LEU A CD1 1 ATOM 1426 C CD2 . LEU A 1 182 ? 29.347 37.705 22.387 1.00 24.34 ? 182 LEU A CD2 1 ATOM 1427 N N . THR A 1 183 ? 28.183 33.152 20.918 1.00 26.45 ? 183 THR A N 1 ATOM 1428 C CA . THR A 1 183 ? 28.536 32.579 19.625 1.00 26.82 ? 183 THR A CA 1 ATOM 1429 C C . THR A 1 183 ? 27.521 31.518 19.194 1.00 28.23 ? 183 THR A C 1 ATOM 1430 O O . THR A 1 183 ? 26.934 31.600 18.111 1.00 28.67 ? 183 THR A O 1 ATOM 1431 C CB . THR A 1 183 ? 29.942 31.916 19.659 1.00 26.63 ? 183 THR A CB 1 ATOM 1432 O OG1 . THR A 1 183 ? 30.934 32.899 19.975 1.00 27.70 ? 183 THR A OG1 1 ATOM 1433 C CG2 . THR A 1 183 ? 30.276 31.294 18.311 1.00 22.67 ? 183 THR A CG2 1 ATOM 1434 N N . GLN A 1 184 ? 27.308 30.526 20.050 1.00 27.86 ? 184 GLN A N 1 ATOM 1435 C CA . GLN A 1 184 ? 26.394 29.437 19.731 1.00 28.65 ? 184 GLN A CA 1 ATOM 1436 C C . GLN A 1 184 ? 24.956 29.815 19.354 1.00 29.38 ? 184 GLN A C 1 ATOM 1437 O O . GLN A 1 184 ? 24.338 29.153 18.519 1.00 28.09 ? 184 GLN A O 1 ATOM 1438 C CB . GLN A 1 184 ? 26.390 28.430 20.877 1.00 26.43 ? 184 GLN A CB 1 ATOM 1439 C CG . GLN A 1 184 ? 27.696 27.686 21.007 1.00 26.59 ? 184 GLN A CG 1 ATOM 1440 C CD . GLN A 1 184 ? 27.709 26.724 22.175 1.00 29.54 ? 184 GLN A CD 1 ATOM 1441 O OE1 . GLN A 1 184 ? 28.065 27.094 23.298 1.00 32.49 ? 184 GLN A OE1 1 ATOM 1442 N NE2 . GLN A 1 184 ? 27.308 25.481 21.923 1.00 28.14 ? 184 GLN A NE2 1 ATOM 1443 N N . TYR A 1 185 ? 24.418 30.873 19.947 1.00 29.93 ? 185 TYR A N 1 ATOM 1444 C CA . TYR A 1 185 ? 23.052 31.253 19.618 1.00 30.89 ? 185 TYR A CA 1 ATOM 1445 C C . TYR A 1 185 ? 22.897 31.752 18.185 1.00 31.68 ? 185 TYR A C 1 ATOM 1446 O O . TYR A 1 185 ? 21.781 31.992 17.711 1.00 31.68 ? 185 TYR A O 1 ATOM 1447 C CB . TYR A 1 185 ? 22.521 32.280 20.625 1.00 29.43 ? 185 TYR A CB 1 ATOM 1448 C CG . TYR A 1 185 ? 21.769 31.619 21.751 1.00 27.54 ? 185 TYR A CG 1 ATOM 1449 C CD1 . TYR A 1 185 ? 22.439 30.868 22.716 1.00 26.91 ? 185 TYR A CD1 1 ATOM 1450 C CD2 . TYR A 1 185 ? 20.376 31.670 21.805 1.00 27.80 ? 185 TYR A CD2 1 ATOM 1451 C CE1 . TYR A 1 185 ? 21.744 30.176 23.703 1.00 26.80 ? 185 TYR A CE1 1 ATOM 1452 C CE2 . TYR A 1 185 ? 19.665 30.979 22.789 1.00 28.33 ? 185 TYR A CE2 1 ATOM 1453 C CZ . TYR A 1 185 ? 20.357 30.234 23.732 1.00 27.88 ? 185 TYR A CZ 1 ATOM 1454 O OH . TYR A 1 185 ? 19.666 29.538 24.693 1.00 27.74 ? 185 TYR A OH 1 ATOM 1455 N N . ASN A 1 186 ? 24.022 31.879 17.493 1.00 31.89 ? 186 ASN A N 1 ATOM 1456 C CA . ASN A 1 186 ? 24.027 32.313 16.099 1.00 32.97 ? 186 ASN A CA 1 ATOM 1457 C C . ASN A 1 186 ? 23.728 31.168 15.144 1.00 31.72 ? 186 ASN A C 1 ATOM 1458 O O . ASN A 1 186 ? 23.420 31.401 13.981 1.00 33.18 ? 186 ASN A O 1 ATOM 1459 C CB . ASN A 1 186 ? 25.398 32.871 15.725 1.00 36.71 ? 186 ASN A CB 1 ATOM 1460 C CG . ASN A 1 186 ? 25.450 34.368 15.793 1.00 41.13 ? 186 ASN A CG 1 ATOM 1461 O OD1 . ASN A 1 186 ? 24.827 35.055 14.978 1.00 42.01 ? 186 ASN A OD1 1 ATOM 1462 N ND2 . ASN A 1 186 ? 26.189 34.895 16.772 1.00 42.43 ? 186 ASN A ND2 1 ATOM 1463 N N . TYR A 1 187 ? 23.808 29.935 15.632 1.00 30.20 ? 187 TYR A N 1 ATOM 1464 C CA . TYR A 1 187 ? 23.617 28.779 14.767 1.00 28.61 ? 187 TYR A CA 1 ATOM 1465 C C . TYR A 1 187 ? 22.363 27.928 14.919 1.00 28.20 ? 187 TYR A C 1 ATOM 1466 O O . TYR A 1 187 ? 22.325 26.791 14.452 1.00 27.92 ? 187 TYR A O 1 ATOM 1467 C CB . TYR A 1 187 ? 24.865 27.902 14.862 1.00 26.19 ? 187 TYR A CB 1 ATOM 1468 C CG . TYR A 1 187 ? 26.089 28.664 14.442 1.00 27.08 ? 187 TYR A CG 1 ATOM 1469 C CD1 . TYR A 1 187 ? 26.496 28.683 13.106 1.00 26.28 ? 187 TYR A CD1 1 ATOM 1470 C CD2 . TYR A 1 187 ? 26.781 29.465 15.357 1.00 27.43 ? 187 TYR A CD2 1 ATOM 1471 C CE1 . TYR A 1 187 ? 27.557 29.487 12.683 1.00 25.48 ? 187 TYR A CE1 1 ATOM 1472 C CE2 . TYR A 1 187 ? 27.840 30.275 14.948 1.00 27.75 ? 187 TYR A CE2 1 ATOM 1473 C CZ . TYR A 1 187 ? 28.222 30.283 13.606 1.00 27.48 ? 187 TYR A CZ 1 ATOM 1474 O OH . TYR A 1 187 ? 29.247 31.096 13.189 1.00 22.46 ? 187 TYR A OH 1 ATOM 1475 N N . TYR A 1 188 ? 21.331 28.463 15.550 1.00 27.03 ? 188 TYR A N 1 ATOM 1476 C CA . TYR A 1 188 ? 20.119 27.685 15.688 1.00 27.53 ? 188 TYR A CA 1 ATOM 1477 C C . TYR A 1 188 ? 19.307 27.786 14.409 1.00 28.99 ? 188 TYR A C 1 ATOM 1478 O O . TYR A 1 188 ? 18.692 26.810 13.973 1.00 30.94 ? 188 TYR A O 1 ATOM 1479 C CB . TYR A 1 188 ? 19.315 28.162 16.898 1.00 27.04 ? 188 TYR A CB 1 ATOM 1480 C CG . TYR A 1 188 ? 19.922 27.704 18.208 1.00 26.83 ? 188 TYR A CG 1 ATOM 1481 C CD1 . TYR A 1 188 ? 20.015 26.350 18.510 1.00 26.32 ? 188 TYR A CD1 1 ATOM 1482 C CD2 . TYR A 1 188 ? 20.426 28.620 19.133 1.00 28.08 ? 188 TYR A CD2 1 ATOM 1483 C CE1 . TYR A 1 188 ? 20.590 25.916 19.688 1.00 27.28 ? 188 TYR A CE1 1 ATOM 1484 C CE2 . TYR A 1 188 ? 21.008 28.193 20.324 1.00 26.46 ? 188 TYR A CE2 1 ATOM 1485 C CZ . TYR A 1 188 ? 21.086 26.838 20.590 1.00 27.87 ? 188 TYR A CZ 1 ATOM 1486 O OH . TYR A 1 188 ? 21.666 26.391 21.752 1.00 28.57 ? 188 TYR A OH 1 ATOM 1487 N N . GLU A 1 189 ? 19.333 28.962 13.791 1.00 30.76 ? 189 GLU A N 1 ATOM 1488 C CA . GLU A 1 189 ? 18.598 29.198 12.554 1.00 31.57 ? 189 GLU A CA 1 ATOM 1489 C C . GLU A 1 189 ? 19.180 28.324 11.445 1.00 30.82 ? 189 GLU A C 1 ATOM 1490 O O . GLU A 1 189 ? 18.472 27.518 10.842 1.00 29.68 ? 189 GLU A O 1 ATOM 1491 C CB . GLU A 1 189 ? 18.676 30.682 12.192 1.00 34.75 ? 189 GLU A CB 1 ATOM 1492 C CG . GLU A 1 189 ? 17.737 31.144 11.088 1.00 38.93 ? 189 GLU A CG 1 ATOM 1493 C CD . GLU A 1 189 ? 18.277 30.875 9.702 1.00 39.44 ? 189 GLU A CD 1 ATOM 1494 O OE1 . GLU A 1 189 ? 19.495 31.046 9.496 1.00 42.39 ? 189 GLU A OE1 1 ATOM 1495 O OE2 . GLU A 1 189 ? 17.482 30.511 8.815 1.00 41.14 ? 189 GLU A OE2 1 ATOM 1496 N N . PRO A 1 190 ? 20.486 28.461 11.164 1.00 30.47 ? 190 PRO A N 1 ATOM 1497 C CA . PRO A 1 190 ? 21.021 27.606 10.102 1.00 30.12 ? 190 PRO A CA 1 ATOM 1498 C C . PRO A 1 190 ? 20.830 26.108 10.350 1.00 30.22 ? 190 PRO A C 1 ATOM 1499 O O . PRO A 1 190 ? 20.590 25.355 9.416 1.00 31.23 ? 190 PRO A O 1 ATOM 1500 C CB . PRO A 1 190 ? 22.495 28.019 10.020 1.00 29.87 ? 190 PRO A CB 1 ATOM 1501 C CG . PRO A 1 190 ? 22.775 28.664 11.346 1.00 30.50 ? 190 PRO A CG 1 ATOM 1502 C CD . PRO A 1 190 ? 21.506 29.407 11.646 1.00 28.85 ? 190 PRO A CD 1 ATOM 1503 N N . MET A 1 191 ? 20.911 25.671 11.601 1.00 31.29 ? 191 MET A N 1 ATOM 1504 C CA . MET A 1 191 ? 20.746 24.249 11.897 1.00 31.12 ? 191 MET A CA 1 ATOM 1505 C C . MET A 1 191 ? 19.316 23.795 11.642 1.00 32.11 ? 191 MET A C 1 ATOM 1506 O O . MET A 1 191 ? 19.077 22.691 11.152 1.00 32.26 ? 191 MET A O 1 ATOM 1507 C CB . MET A 1 191 ? 21.115 23.949 13.356 1.00 29.89 ? 191 MET A CB 1 ATOM 1508 C CG . MET A 1 191 ? 21.119 22.461 13.726 1.00 25.67 ? 191 MET A CG 1 ATOM 1509 S SD . MET A 1 191 ? 22.497 21.537 12.982 1.00 27.58 ? 191 MET A SD 1 ATOM 1510 C CE . MET A 1 191 ? 21.840 19.847 12.947 1.00 24.60 ? 191 MET A CE 1 ATOM 1511 N N . ALA A 1 192 ? 18.360 24.652 11.971 1.00 33.77 ? 192 ALA A N 1 ATOM 1512 C CA . ALA A 1 192 ? 16.954 24.307 11.785 1.00 35.10 ? 192 ALA A CA 1 ATOM 1513 C C . ALA A 1 192 ? 16.428 24.613 10.381 1.00 34.68 ? 192 ALA A C 1 ATOM 1514 O O . ALA A 1 192 ? 15.330 24.183 10.026 1.00 34.45 ? 192 ALA A O 1 ATOM 1515 C CB . ALA A 1 192 ? 16.102 25.035 12.830 1.00 34.36 ? 192 ALA A CB 1 ATOM 1516 N N . CYS A 1 193 ? 17.210 25.336 9.583 1.00 34.09 ? 193 CYS A N 1 ATOM 1517 C CA . CYS A 1 193 ? 16.767 25.706 8.246 1.00 35.58 ? 193 CYS A CA 1 ATOM 1518 C C . CYS A 1 193 ? 17.563 25.126 7.072 1.00 37.65 ? 193 CYS A C 1 ATOM 1519 O O . CYS A 1 193 ? 17.791 25.799 6.064 1.00 38.20 ? 193 CYS A O 1 ATOM 1520 C CB . CYS A 1 193 ? 16.683 27.233 8.168 1.00 34.99 ? 193 CYS A CB 1 ATOM 1521 S SG . CYS A 1 193 ? 15.628 27.842 9.525 1.00 34.97 ? 193 CYS A SG 1 ATOM 1522 N N . GLY A 1 194 ? 17.978 23.869 7.215 1.00 38.26 ? 194 GLY A N 1 ATOM 1523 C CA . GLY A 1 194 ? 18.696 23.178 6.157 1.00 38.38 ? 194 GLY A CA 1 ATOM 1524 C C . GLY A 1 194 ? 20.170 23.436 5.910 1.00 40.17 ? 194 GLY A C 1 ATOM 1525 O O . GLY A 1 194 ? 20.672 23.078 4.844 1.00 41.83 ? 194 GLY A O 1 ATOM 1526 N N . GLU A 1 195 ? 20.881 24.023 6.865 1.00 39.80 ? 195 GLU A N 1 ATOM 1527 C CA . GLU A 1 195 ? 22.300 24.298 6.661 1.00 40.30 ? 195 GLU A CA 1 ATOM 1528 C C . GLU A 1 195 ? 23.232 23.593 7.638 1.00 39.86 ? 195 GLU A C 1 ATOM 1529 O O . GLU A 1 195 ? 24.387 23.994 7.798 1.00 40.02 ? 195 GLU A O 1 ATOM 1530 C CB . GLU A 1 195 ? 22.539 25.802 6.714 1.00 42.90 ? 195 GLU A CB 1 ATOM 1531 C CG . GLU A 1 195 ? 22.018 26.518 5.484 1.00 51.13 ? 195 GLU A CG 1 ATOM 1532 C CD . GLU A 1 195 ? 21.631 27.957 5.755 1.00 55.66 ? 195 GLU A CD 1 ATOM 1533 O OE1 . GLU A 1 195 ? 22.425 28.692 6.388 1.00 57.95 ? 195 GLU A OE1 1 ATOM 1534 O OE2 . GLU A 1 195 ? 20.524 28.351 5.324 1.00 59.57 ? 195 GLU A OE2 1 ATOM 1535 N N . GLY A 1 196 ? 22.737 22.535 8.275 1.00 37.91 ? 196 GLY A N 1 ATOM 1536 C CA . GLY A 1 196 ? 23.545 21.806 9.234 1.00 36.07 ? 196 GLY A CA 1 ATOM 1537 C C . GLY A 1 196 ? 23.734 20.352 8.863 1.00 35.82 ? 196 GLY A C 1 ATOM 1538 O O . GLY A 1 196 ? 24.201 19.554 9.679 1.00 34.62 ? 196 GLY A O 1 ATOM 1539 N N . GLY A 1 197 ? 23.362 20.005 7.631 1.00 34.97 ? 197 GLY A N 1 ATOM 1540 C CA . GLY A 1 197 ? 23.512 18.639 7.167 1.00 33.09 ? 197 GLY A CA 1 ATOM 1541 C C . GLY A 1 197 ? 22.210 17.871 7.175 1.00 34.05 ? 197 GLY A C 1 ATOM 1542 O O . GLY A 1 197 ? 22.189 16.656 6.978 1.00 35.92 ? 197 GLY A O 1 ATOM 1543 N N . GLU A 1 198 ? 21.116 18.576 7.416 1.00 32.90 ? 198 GLU A N 1 ATOM 1544 C CA . GLU A 1 198 ? 19.807 17.951 7.444 1.00 33.73 ? 198 GLU A CA 1 ATOM 1545 C C . GLU A 1 198 ? 18.794 18.891 6.822 1.00 34.98 ? 198 GLU A C 1 ATOM 1546 O O . GLU A 1 198 ? 18.910 20.108 6.939 1.00 35.42 ? 198 GLU A O 1 ATOM 1547 C CB . GLU A 1 198 ? 19.413 17.618 8.881 1.00 35.37 ? 198 GLU A CB 1 ATOM 1548 C CG . GLU A 1 198 ? 20.167 16.432 9.439 1.00 36.18 ? 198 GLU A CG 1 ATOM 1549 C CD . GLU A 1 198 ? 19.635 15.114 8.906 1.00 39.12 ? 198 GLU A CD 1 ATOM 1550 O OE1 . GLU A 1 198 ? 20.406 14.131 8.866 1.00 40.17 ? 198 GLU A OE1 1 ATOM 1551 O OE2 . GLU A 1 198 ? 18.439 15.055 8.541 1.00 37.87 ? 198 GLU A OE2 1 ATOM 1552 N N . PRO A 1 199 ? 17.786 18.335 6.142 1.00 36.01 ? 199 PRO A N 1 ATOM 1553 C CA . PRO A 1 199 ? 16.741 19.133 5.489 1.00 36.12 ? 199 PRO A CA 1 ATOM 1554 C C . PRO A 1 199 ? 16.114 20.105 6.473 1.00 35.41 ? 199 PRO A C 1 ATOM 1555 O O . PRO A 1 199 ? 15.974 19.792 7.655 1.00 35.92 ? 199 PRO A O 1 ATOM 1556 C CB . PRO A 1 199 ? 15.737 18.079 5.027 1.00 36.58 ? 199 PRO A CB 1 ATOM 1557 C CG . PRO A 1 199 ? 16.579 16.840 4.873 1.00 36.06 ? 199 PRO A CG 1 ATOM 1558 C CD . PRO A 1 199 ? 17.473 16.900 6.071 1.00 34.75 ? 199 PRO A CD 1 ATOM 1559 N N . SER A 1 200 ? 15.737 21.281 5.994 1.00 35.32 ? 200 SER A N 1 ATOM 1560 C CA . SER A 1 200 ? 15.117 22.258 6.876 1.00 35.80 ? 200 SER A CA 1 ATOM 1561 C C . SER A 1 200 ? 13.909 21.620 7.563 1.00 35.54 ? 200 SER A C 1 ATOM 1562 O O . SER A 1 200 ? 13.242 20.769 6.976 1.00 35.80 ? 200 SER A O 1 ATOM 1563 C CB . SER A 1 200 ? 14.673 23.478 6.081 1.00 34.29 ? 200 SER A CB 1 ATOM 1564 O OG . SER A 1 200 ? 14.015 24.394 6.935 1.00 38.42 ? 200 SER A OG 1 ATOM 1565 N N . VAL A 1 201 ? 13.639 22.021 8.803 1.00 35.10 ? 201 VAL A N 1 ATOM 1566 C CA . VAL A 1 201 ? 12.508 21.482 9.559 1.00 35.42 ? 201 VAL A CA 1 ATOM 1567 C C . VAL A 1 201 ? 11.525 22.593 9.889 1.00 36.85 ? 201 VAL A C 1 ATOM 1568 O O . VAL A 1 201 ? 10.467 22.356 10.462 1.00 37.29 ? 201 VAL A O 1 ATOM 1569 C CB . VAL A 1 201 ? 12.962 20.834 10.898 1.00 36.62 ? 201 VAL A CB 1 ATOM 1570 C CG1 . VAL A 1 201 ? 13.886 19.648 10.628 1.00 35.69 ? 201 VAL A CG1 1 ATOM 1571 C CG2 . VAL A 1 201 ? 13.657 21.871 11.775 1.00 33.96 ? 201 VAL A CG2 1 ATOM 1572 N N . LEU A 1 202 ? 11.884 23.813 9.517 1.00 38.46 ? 202 LEU A N 1 ATOM 1573 C CA . LEU A 1 202 ? 11.052 24.974 9.788 1.00 39.31 ? 202 LEU A CA 1 ATOM 1574 C C . LEU A 1 202 ? 10.647 25.679 8.498 1.00 40.02 ? 202 LEU A C 1 ATOM 1575 O O . LEU A 1 202 ? 11.468 25.861 7.595 1.00 39.24 ? 202 LEU A O 1 ATOM 1576 C CB . LEU A 1 202 ? 11.833 25.949 10.672 1.00 40.69 ? 202 LEU A CB 1 ATOM 1577 C CG . LEU A 1 202 ? 11.351 26.298 12.079 1.00 42.53 ? 202 LEU A CG 1 ATOM 1578 C CD1 . LEU A 1 202 ? 10.808 25.077 12.799 1.00 43.47 ? 202 LEU A CD1 1 ATOM 1579 C CD2 . LEU A 1 202 ? 12.523 26.900 12.837 1.00 43.13 ? 202 LEU A CD2 1 ATOM 1580 N N . PRO A 1 203 ? 9.369 26.079 8.389 1.00 40.54 ? 203 PRO A N 1 ATOM 1581 C CA . PRO A 1 203 ? 8.917 26.771 7.179 1.00 41.31 ? 203 PRO A CA 1 ATOM 1582 C C . PRO A 1 203 ? 9.684 28.079 7.027 1.00 42.85 ? 203 PRO A C 1 ATOM 1583 O O . PRO A 1 203 ? 10.112 28.669 8.015 1.00 43.68 ? 203 PRO A O 1 ATOM 1584 C CB . PRO A 1 203 ? 7.427 26.978 7.438 1.00 39.93 ? 203 PRO A CB 1 ATOM 1585 C CG . PRO A 1 203 ? 7.335 27.020 8.930 1.00 38.82 ? 203 PRO A CG 1 ATOM 1586 C CD . PRO A 1 203 ? 8.262 25.917 9.347 1.00 39.79 ? 203 PRO A CD 1 ATOM 1587 N N . SER A 1 204 ? 9.861 28.532 5.795 1.00 45.48 ? 204 SER A N 1 ATOM 1588 C CA . SER A 1 204 ? 10.611 29.761 5.546 1.00 49.63 ? 204 SER A CA 1 ATOM 1589 C C . SER A 1 204 ? 10.223 30.953 6.425 1.00 50.76 ? 204 SER A C 1 ATOM 1590 O O . SER A 1 204 ? 11.100 31.624 6.973 1.00 50.85 ? 204 SER A O 1 ATOM 1591 C CB . SER A 1 204 ? 10.511 30.152 4.065 1.00 50.17 ? 204 SER A CB 1 ATOM 1592 O OG . SER A 1 204 ? 9.160 30.234 3.652 1.00 53.97 ? 204 SER A OG 1 ATOM 1593 N N . GLU A 1 205 ? 8.925 31.221 6.562 1.00 51.76 ? 205 GLU A N 1 ATOM 1594 C CA . GLU A 1 205 ? 8.480 32.350 7.379 1.00 53.66 ? 205 GLU A CA 1 ATOM 1595 C C . GLU A 1 205 ? 9.091 32.346 8.778 1.00 52.19 ? 205 GLU A C 1 ATOM 1596 O O . GLU A 1 205 ? 9.422 33.405 9.317 1.00 52.45 ? 205 GLU A O 1 ATOM 1597 C CB . GLU A 1 205 ? 6.947 32.390 7.481 1.00 57.37 ? 205 GLU A CB 1 ATOM 1598 C CG . GLU A 1 205 ? 6.236 31.054 7.273 1.00 64.93 ? 205 GLU A CG 1 ATOM 1599 C CD . GLU A 1 205 ? 6.087 30.688 5.800 1.00 68.68 ? 205 GLU A CD 1 ATOM 1600 O OE1 . GLU A 1 205 ? 5.445 31.462 5.054 1.00 70.40 ? 205 GLU A OE1 1 ATOM 1601 O OE2 . GLU A 1 205 ? 6.609 29.628 5.387 1.00 71.41 ? 205 GLU A OE2 1 ATOM 1602 N N . GLU A 1 206 ? 9.249 31.160 9.358 1.00 50.37 ? 206 GLU A N 1 ATOM 1603 C CA . GLU A 1 206 ? 9.828 31.023 10.693 1.00 49.01 ? 206 GLU A CA 1 ATOM 1604 C C . GLU A 1 206 ? 11.328 31.320 10.678 1.00 46.89 ? 206 GLU A C 1 ATOM 1605 O O . GLU A 1 206 ? 11.830 32.067 11.517 1.00 46.40 ? 206 GLU A O 1 ATOM 1606 C CB . GLU A 1 206 ? 9.600 29.607 11.228 1.00 52.12 ? 206 GLU A CB 1 ATOM 1607 C CG . GLU A 1 206 ? 8.144 29.193 11.315 1.00 57.03 ? 206 GLU A CG 1 ATOM 1608 C CD . GLU A 1 206 ? 7.398 29.884 12.440 1.00 62.11 ? 206 GLU A CD 1 ATOM 1609 O OE1 . GLU A 1 206 ? 6.152 29.765 12.482 1.00 64.53 ? 206 GLU A OE1 1 ATOM 1610 O OE2 . GLU A 1 206 ? 8.054 30.540 13.284 1.00 64.29 ? 206 GLU A OE2 1 ATOM 1611 N N . CYS A 1 207 ? 12.045 30.732 9.725 1.00 43.96 ? 207 CYS A N 1 ATOM 1612 C CA . CYS A 1 207 ? 13.484 30.949 9.629 1.00 42.61 ? 207 CYS A CA 1 ATOM 1613 C C . CYS A 1 207 ? 13.825 32.429 9.528 1.00 43.05 ? 207 CYS A C 1 ATOM 1614 O O . CYS A 1 207 ? 14.827 32.883 10.087 1.00 42.69 ? 207 CYS A O 1 ATOM 1615 C CB . CYS A 1 207 ? 14.051 30.184 8.432 1.00 39.43 ? 207 CYS A CB 1 ATOM 1616 S SG . CYS A 1 207 ? 13.879 28.386 8.660 1.00 39.77 ? 207 CYS A SG 1 ATOM 1617 N N . SER A 1 208 ? 12.975 33.176 8.827 1.00 43.04 ? 208 SER A N 1 ATOM 1618 C CA . SER A 1 208 ? 13.167 34.611 8.649 1.00 42.47 ? 208 SER A CA 1 ATOM 1619 C C . SER A 1 208 ? 12.909 35.305 9.971 1.00 40.96 ? 208 SER A C 1 ATOM 1620 O O . SER A 1 208 ? 13.653 36.197 10.374 1.00 39.83 ? 208 SER A O 1 ATOM 1621 C CB . SER A 1 208 ? 12.191 35.153 7.604 1.00 43.72 ? 208 SER A CB 1 ATOM 1622 O OG . SER A 1 208 ? 12.245 34.384 6.420 1.00 47.24 ? 208 SER A OG 1 ATOM 1623 N N . ALA A 1 209 ? 11.835 34.896 10.638 1.00 39.73 ? 209 ALA A N 1 ATOM 1624 C CA . ALA A 1 209 ? 11.480 35.476 11.922 1.00 39.25 ? 209 ALA A CA 1 ATOM 1625 C C . ALA A 1 209 ? 12.682 35.358 12.848 1.00 39.96 ? 209 ALA A C 1 ATOM 1626 O O . ALA A 1 209 ? 13.060 36.320 13.520 1.00 40.72 ? 209 ALA A O 1 ATOM 1627 C CB . ALA A 1 209 ? 10.287 34.750 12.512 1.00 37.03 ? 209 ALA A CB 1 ATOM 1628 N N . MET A 1 210 ? 13.286 34.173 12.865 1.00 39.62 ? 210 MET A N 1 ATOM 1629 C CA . MET A 1 210 ? 14.454 33.919 13.696 1.00 39.35 ? 210 MET A CA 1 ATOM 1630 C C . MET A 1 210 ? 15.613 34.848 13.351 1.00 38.90 ? 210 MET A C 1 ATOM 1631 O O . MET A 1 210 ? 16.346 35.285 14.237 1.00 39.03 ? 210 MET A O 1 ATOM 1632 C CB . MET A 1 210 ? 14.897 32.455 13.555 1.00 39.16 ? 210 MET A CB 1 ATOM 1633 C CG . MET A 1 210 ? 14.093 31.476 14.397 1.00 35.71 ? 210 MET A CG 1 ATOM 1634 S SD . MET A 1 210 ? 14.459 29.753 14.015 1.00 38.92 ? 210 MET A SD 1 ATOM 1635 C CE . MET A 1 210 ? 16.032 29.514 14.825 1.00 36.14 ? 210 MET A CE 1 ATOM 1636 N N . GLU A 1 211 ? 15.783 35.153 12.069 1.00 39.05 ? 211 GLU A N 1 ATOM 1637 C CA . GLU A 1 211 ? 16.868 36.035 11.659 1.00 40.49 ? 211 GLU A CA 1 ATOM 1638 C C . GLU A 1 211 ? 16.660 37.445 12.169 1.00 39.83 ? 211 GLU A C 1 ATOM 1639 O O . GLU A 1 211 ? 17.607 38.090 12.624 1.00 40.93 ? 211 GLU A O 1 ATOM 1640 C CB . GLU A 1 211 ? 17.002 36.078 10.138 1.00 43.11 ? 211 GLU A CB 1 ATOM 1641 C CG . GLU A 1 211 ? 17.616 34.843 9.529 1.00 50.99 ? 211 GLU A CG 1 ATOM 1642 C CD . GLU A 1 211 ? 18.973 34.520 10.127 1.00 57.39 ? 211 GLU A CD 1 ATOM 1643 O OE1 . GLU A 1 211 ? 19.025 34.100 11.307 1.00 60.86 ? 211 GLU A OE1 1 ATOM 1644 O OE2 . GLU A 1 211 ? 19.991 34.691 9.421 1.00 61.04 ? 211 GLU A OE2 1 ATOM 1645 N N . ASP A 1 212 ? 15.421 37.922 12.101 1.00 38.97 ? 212 ASP A N 1 ATOM 1646 C CA . ASP A 1 212 ? 15.116 39.278 12.537 1.00 38.50 ? 212 ASP A CA 1 ATOM 1647 C C . ASP A 1 212 ? 15.364 39.510 14.013 1.00 37.00 ? 212 ASP A C 1 ATOM 1648 O O . ASP A 1 212 ? 15.943 40.527 14.395 1.00 37.88 ? 212 ASP A O 1 ATOM 1649 C CB . ASP A 1 212 ? 13.674 39.635 12.199 1.00 40.87 ? 212 ASP A CB 1 ATOM 1650 C CG . ASP A 1 212 ? 13.389 39.537 10.717 1.00 43.91 ? 212 ASP A CG 1 ATOM 1651 O OD1 . ASP A 1 212 ? 14.257 39.955 9.913 1.00 43.91 ? 212 ASP A OD1 1 ATOM 1652 O OD2 . ASP A 1 212 ? 12.294 39.049 10.357 1.00 46.55 ? 212 ASP A OD2 1 ATOM 1653 N N . SER A 1 213 ? 14.941 38.562 14.839 1.00 34.76 ? 213 SER A N 1 ATOM 1654 C CA . SER A 1 213 ? 15.119 38.670 16.280 1.00 33.66 ? 213 SER A CA 1 ATOM 1655 C C . SER A 1 213 ? 16.529 38.315 16.754 1.00 34.19 ? 213 SER A C 1 ATOM 1656 O O . SER A 1 213 ? 16.872 38.530 17.914 1.00 34.59 ? 213 SER A O 1 ATOM 1657 C CB . SER A 1 213 ? 14.111 37.772 16.981 1.00 32.17 ? 213 SER A CB 1 ATOM 1658 O OG . SER A 1 213 ? 14.186 36.461 16.459 1.00 32.72 ? 213 SER A OG 1 ATOM 1659 N N . LEU A 1 214 ? 17.354 37.791 15.859 1.00 34.16 ? 214 LEU A N 1 ATOM 1660 C CA . LEU A 1 214 ? 18.697 37.399 16.240 1.00 37.01 ? 214 LEU A CA 1 ATOM 1661 C C . LEU A 1 214 ? 19.524 38.518 16.875 1.00 39.44 ? 214 LEU A C 1 ATOM 1662 O O . LEU A 1 214 ? 20.117 38.333 17.941 1.00 40.51 ? 214 LEU A O 1 ATOM 1663 C CB . LEU A 1 214 ? 19.418 36.817 15.028 1.00 37.39 ? 214 LEU A CB 1 ATOM 1664 C CG . LEU A 1 214 ? 20.728 36.083 15.308 1.00 37.68 ? 214 LEU A CG 1 ATOM 1665 C CD1 . LEU A 1 214 ? 20.580 35.162 16.518 1.00 38.22 ? 214 LEU A CD1 1 ATOM 1666 C CD2 . LEU A 1 214 ? 21.108 35.294 14.071 1.00 37.07 ? 214 LEU A CD2 1 ATOM 1667 N N . GLU A 1 215 ? 19.560 39.675 16.221 1.00 42.47 ? 215 GLU A N 1 ATOM 1668 C CA . GLU A 1 215 ? 20.304 40.838 16.712 1.00 42.09 ? 215 GLU A CA 1 ATOM 1669 C C . GLU A 1 215 ? 19.944 41.202 18.147 1.00 39.34 ? 215 GLU A C 1 ATOM 1670 O O . GLU A 1 215 ? 20.817 41.328 19.004 1.00 38.13 ? 215 GLU A O 1 ATOM 1671 C CB . GLU A 1 215 ? 20.027 42.041 15.816 1.00 47.50 ? 215 GLU A CB 1 ATOM 1672 C CG . GLU A 1 215 ? 20.623 41.927 14.431 1.00 56.13 ? 215 GLU A CG 1 ATOM 1673 C CD . GLU A 1 215 ? 22.052 42.433 14.381 1.00 60.54 ? 215 GLU A CD 1 ATOM 1674 O OE1 . GLU A 1 215 ? 22.719 42.237 13.336 1.00 62.18 ? 215 GLU A OE1 1 ATOM 1675 O OE2 . GLU A 1 215 ? 22.498 43.036 15.387 1.00 62.06 ? 215 GLU A OE2 1 ATOM 1676 N N . ARG A 1 216 ? 18.654 41.378 18.403 1.00 36.71 ? 216 ARG A N 1 ATOM 1677 C CA . ARG A 1 216 ? 18.192 41.736 19.734 1.00 35.64 ? 216 ARG A CA 1 ATOM 1678 C C . ARG A 1 216 ? 18.688 40.720 20.750 1.00 34.19 ? 216 ARG A C 1 ATOM 1679 O O . ARG A 1 216 ? 19.250 41.084 21.787 1.00 33.83 ? 216 ARG A O 1 ATOM 1680 C CB . ARG A 1 216 ? 16.666 41.807 19.759 1.00 38.24 ? 216 ARG A CB 1 ATOM 1681 C CG . ARG A 1 216 ? 16.078 42.452 21.002 1.00 43.97 ? 216 ARG A CG 1 ATOM 1682 C CD . ARG A 1 216 ? 15.037 43.500 20.619 1.00 49.47 ? 216 ARG A CD 1 ATOM 1683 N NE . ARG A 1 216 ? 14.112 43.835 21.706 1.00 54.48 ? 216 ARG A NE 1 ATOM 1684 C CZ . ARG A 1 216 ? 14.471 44.328 22.892 1.00 57.70 ? 216 ARG A CZ 1 ATOM 1685 N NH1 . ARG A 1 216 ? 15.754 44.553 23.174 1.00 57.67 ? 216 ARG A NH1 1 ATOM 1686 N NH2 . ARG A 1 216 ? 13.540 44.602 23.802 1.00 58.55 ? 216 ARG A NH2 1 ATOM 1687 N N . CYS A 1 217 ? 18.494 39.441 20.449 1.00 32.15 ? 217 CYS A N 1 ATOM 1688 C CA . CYS A 1 217 ? 18.936 38.404 21.362 1.00 30.50 ? 217 CYS A CA 1 ATOM 1689 C C . CYS A 1 217 ? 20.425 38.542 21.662 1.00 30.20 ? 217 CYS A C 1 ATOM 1690 O O . CYS A 1 217 ? 20.826 38.653 22.823 1.00 29.73 ? 217 CYS A O 1 ATOM 1691 C CB . CYS A 1 217 ? 18.634 37.009 20.794 1.00 31.08 ? 217 CYS A CB 1 ATOM 1692 S SG . CYS A 1 217 ? 19.710 35.729 21.515 1.00 30.01 ? 217 CYS A SG 1 ATOM 1693 N N . LEU A 1 218 ? 21.247 38.546 20.618 1.00 30.25 ? 218 LEU A N 1 ATOM 1694 C CA . LEU A 1 218 ? 22.688 38.662 20.805 1.00 30.71 ? 218 LEU A CA 1 ATOM 1695 C C . LEU A 1 218 ? 23.071 39.876 21.646 1.00 31.22 ? 218 LEU A C 1 ATOM 1696 O O . LEU A 1 218 ? 23.953 39.788 22.501 1.00 31.75 ? 218 LEU A O 1 ATOM 1697 C CB . LEU A 1 218 ? 23.394 38.724 19.455 1.00 30.05 ? 218 LEU A CB 1 ATOM 1698 C CG . LEU A 1 218 ? 23.276 37.460 18.611 1.00 31.80 ? 218 LEU A CG 1 ATOM 1699 C CD1 . LEU A 1 218 ? 23.977 37.661 17.286 1.00 29.75 ? 218 LEU A CD1 1 ATOM 1700 C CD2 . LEU A 1 218 ? 23.891 36.292 19.365 1.00 33.00 ? 218 LEU A CD2 1 ATOM 1701 N N . GLY A 1 219 ? 22.411 41.008 21.404 1.00 30.77 ? 219 GLY A N 1 ATOM 1702 C CA . GLY A 1 219 ? 22.711 42.206 22.168 1.00 28.00 ? 219 GLY A CA 1 ATOM 1703 C C . GLY A 1 219 ? 22.488 41.951 23.643 1.00 28.61 ? 219 GLY A C 1 ATOM 1704 O O . GLY A 1 219 ? 23.310 42.317 24.484 1.00 29.17 ? 219 GLY A O 1 ATOM 1705 N N . LEU A 1 220 ? 21.370 41.308 23.963 1.00 27.98 ? 220 LEU A N 1 ATOM 1706 C CA . LEU A 1 220 ? 21.047 40.997 25.346 1.00 27.11 ? 220 LEU A CA 1 ATOM 1707 C C . LEU A 1 220 ? 22.089 40.056 25.946 1.00 27.48 ? 220 LEU A C 1 ATOM 1708 O O . LEU A 1 220 ? 22.499 40.215 27.096 1.00 27.60 ? 220 LEU A O 1 ATOM 1709 C CB . LEU A 1 220 ? 19.649 40.384 25.426 1.00 26.74 ? 220 LEU A CB 1 ATOM 1710 C CG . LEU A 1 220 ? 18.558 41.418 25.143 1.00 26.48 ? 220 LEU A CG 1 ATOM 1711 C CD1 . LEU A 1 220 ? 17.214 40.760 24.891 1.00 24.63 ? 220 LEU A CD1 1 ATOM 1712 C CD2 . LEU A 1 220 ? 18.494 42.361 26.327 1.00 25.72 ? 220 LEU A CD2 1 ATOM 1713 N N . ILE A 1 221 ? 22.529 39.079 25.171 1.00 26.95 ? 221 ILE A N 1 ATOM 1714 C CA . ILE A 1 221 ? 23.531 38.161 25.680 1.00 29.29 ? 221 ILE A CA 1 ATOM 1715 C C . ILE A 1 221 ? 24.823 38.925 25.982 1.00 30.14 ? 221 ILE A C 1 ATOM 1716 O O . ILE A 1 221 ? 25.475 38.690 27.003 1.00 29.06 ? 221 ILE A O 1 ATOM 1717 C CB . ILE A 1 221 ? 23.819 37.026 24.666 1.00 28.50 ? 221 ILE A CB 1 ATOM 1718 C CG1 . ILE A 1 221 ? 22.542 36.203 24.450 1.00 26.60 ? 221 ILE A CG1 1 ATOM 1719 C CG2 . ILE A 1 221 ? 24.966 36.151 25.169 1.00 25.50 ? 221 ILE A CG2 1 ATOM 1720 C CD1 . ILE A 1 221 ? 22.658 35.149 23.386 1.00 27.25 ? 221 ILE A CD1 1 ATOM 1721 N N . GLU A 1 222 ? 25.181 39.850 25.099 1.00 31.84 ? 222 GLU A N 1 ATOM 1722 C CA . GLU A 1 222 ? 26.398 40.632 25.284 1.00 33.75 ? 222 GLU A CA 1 ATOM 1723 C C . GLU A 1 222 ? 26.305 41.438 26.568 1.00 32.36 ? 222 GLU A C 1 ATOM 1724 O O . GLU A 1 222 ? 27.274 41.578 27.314 1.00 30.47 ? 222 GLU A O 1 ATOM 1725 C CB . GLU A 1 222 ? 26.613 41.560 24.090 1.00 36.50 ? 222 GLU A CB 1 ATOM 1726 C CG . GLU A 1 222 ? 27.778 42.509 24.270 1.00 42.50 ? 222 GLU A CG 1 ATOM 1727 C CD . GLU A 1 222 ? 28.386 42.921 22.954 1.00 46.62 ? 222 GLU A CD 1 ATOM 1728 O OE1 . GLU A 1 222 ? 29.287 43.789 22.966 1.00 48.52 ? 222 GLU A OE1 1 ATOM 1729 O OE2 . GLU A 1 222 ? 27.967 42.369 21.908 1.00 48.24 ? 222 GLU A OE2 1 ATOM 1730 N N . SER A 1 223 ? 25.114 41.958 26.819 1.00 32.22 ? 223 SER A N 1 ATOM 1731 C CA . SER A 1 223 ? 24.860 42.742 28.010 1.00 31.10 ? 223 SER A CA 1 ATOM 1732 C C . SER A 1 223 ? 25.072 41.889 29.261 1.00 30.26 ? 223 SER A C 1 ATOM 1733 O O . SER A 1 223 ? 25.630 42.357 30.255 1.00 30.42 ? 223 SER A O 1 ATOM 1734 C CB . SER A 1 223 ? 23.436 43.269 27.965 1.00 30.97 ? 223 SER A CB 1 ATOM 1735 O OG . SER A 1 223 ? 23.252 44.228 28.974 1.00 37.86 ? 223 SER A OG 1 ATOM 1736 N N . CYS A 1 224 ? 24.627 40.636 29.209 1.00 29.21 ? 224 CYS A N 1 ATOM 1737 C CA . CYS A 1 224 ? 24.797 39.724 30.332 1.00 29.46 ? 224 CYS A CA 1 ATOM 1738 C C . CYS A 1 224 ? 26.280 39.447 30.487 1.00 30.91 ? 224 CYS A C 1 ATOM 1739 O O . CYS A 1 224 ? 26.808 39.406 31.603 1.00 30.81 ? 224 CYS A O 1 ATOM 1740 C CB . CYS A 1 224 ? 24.040 38.410 30.085 1.00 31.45 ? 224 CYS A CB 1 ATOM 1741 S SG . CYS A 1 224 ? 24.477 37.021 31.194 1.00 26.60 ? 224 CYS A SG 1 ATOM 1742 N N . TYR A 1 225 ? 26.952 39.259 29.358 1.00 31.90 ? 225 TYR A N 1 ATOM 1743 C CA . TYR A 1 225 ? 28.388 38.999 29.360 1.00 33.50 ? 225 TYR A CA 1 ATOM 1744 C C . TYR A 1 225 ? 29.135 40.113 30.077 1.00 35.13 ? 225 TYR A C 1 ATOM 1745 O O . TYR A 1 225 ? 30.070 39.861 30.842 1.00 34.34 ? 225 TYR A O 1 ATOM 1746 C CB . TYR A 1 225 ? 28.908 38.907 27.926 1.00 32.71 ? 225 TYR A CB 1 ATOM 1747 C CG . TYR A 1 225 ? 28.887 37.522 27.332 1.00 34.35 ? 225 TYR A CG 1 ATOM 1748 C CD1 . TYR A 1 225 ? 27.950 36.566 27.747 1.00 32.41 ? 225 TYR A CD1 1 ATOM 1749 C CD2 . TYR A 1 225 ? 29.788 37.171 26.324 1.00 34.80 ? 225 TYR A CD2 1 ATOM 1750 C CE1 . TYR A 1 225 ? 27.914 35.296 27.166 1.00 32.81 ? 225 TYR A CE1 1 ATOM 1751 C CE2 . TYR A 1 225 ? 29.761 35.905 25.737 1.00 34.86 ? 225 TYR A CE2 1 ATOM 1752 C CZ . TYR A 1 225 ? 28.823 34.974 26.161 1.00 33.68 ? 225 TYR A CZ 1 ATOM 1753 O OH . TYR A 1 225 ? 28.798 33.734 25.567 1.00 33.44 ? 225 TYR A OH 1 ATOM 1754 N N . ASP A 1 226 ? 28.703 41.347 29.837 1.00 37.57 ? 226 ASP A N 1 ATOM 1755 C CA . ASP A 1 226 ? 29.364 42.501 30.423 1.00 40.29 ? 226 ASP A CA 1 ATOM 1756 C C . ASP A 1 226 ? 29.073 42.799 31.883 1.00 39.59 ? 226 ASP A C 1 ATOM 1757 O O . ASP A 1 226 ? 29.965 43.231 32.606 1.00 40.14 ? 226 ASP A O 1 ATOM 1758 C CB . ASP A 1 226 ? 29.072 43.750 29.590 1.00 44.57 ? 226 ASP A CB 1 ATOM 1759 C CG . ASP A 1 226 ? 30.040 44.881 29.889 1.00 48.44 ? 226 ASP A CG 1 ATOM 1760 O OD1 . ASP A 1 226 ? 31.265 44.683 29.695 1.00 48.08 ? 226 ASP A OD1 1 ATOM 1761 O OD2 . ASP A 1 226 ? 29.577 45.960 30.323 1.00 50.42 ? 226 ASP A OD2 1 ATOM 1762 N N . SER A 1 227 ? 27.842 42.576 32.326 1.00 39.31 ? 227 SER A N 1 ATOM 1763 C CA . SER A 1 227 ? 27.494 42.863 33.715 1.00 39.41 ? 227 SER A CA 1 ATOM 1764 C C . SER A 1 227 ? 27.325 41.626 34.581 1.00 39.44 ? 227 SER A C 1 ATOM 1765 O O . SER A 1 227 ? 27.365 41.719 35.801 1.00 40.57 ? 227 SER A O 1 ATOM 1766 C CB . SER A 1 227 ? 26.205 43.685 33.774 1.00 39.86 ? 227 SER A CB 1 ATOM 1767 O OG . SER A 1 227 ? 25.104 42.937 33.281 1.00 43.62 ? 227 SER A OG 1 ATOM 1768 N N . GLN A 1 228 ? 27.128 40.472 33.952 1.00 39.82 ? 228 GLN A N 1 ATOM 1769 C CA . GLN A 1 228 ? 26.939 39.223 34.683 1.00 39.69 ? 228 GLN A CA 1 ATOM 1770 C C . GLN A 1 228 ? 25.962 39.373 35.850 1.00 38.81 ? 228 GLN A C 1 ATOM 1771 O O . GLN A 1 228 ? 26.205 38.870 36.945 1.00 38.18 ? 228 GLN A O 1 ATOM 1772 C CB . GLN A 1 228 ? 28.276 38.718 35.196 1.00 39.53 ? 228 GLN A CB 1 ATOM 1773 C CG . GLN A 1 228 ? 29.214 38.338 34.091 1.00 44.11 ? 228 GLN A CG 1 ATOM 1774 C CD . GLN A 1 228 ? 30.580 37.974 34.608 1.00 46.38 ? 228 GLN A CD 1 ATOM 1775 O OE1 . GLN A 1 228 ? 30.725 37.061 35.418 1.00 47.80 ? 228 GLN A OE1 1 ATOM 1776 N NE2 . GLN A 1 228 ? 31.595 38.691 34.146 1.00 48.18 ? 228 GLN A NE2 1 ATOM 1777 N N . SER A 1 229 ? 24.853 40.060 35.606 1.00 36.96 ? 229 SER A N 1 ATOM 1778 C CA . SER A 1 229 ? 23.860 40.270 36.643 1.00 36.25 ? 229 SER A CA 1 ATOM 1779 C C . SER A 1 229 ? 22.525 39.634 36.292 1.00 35.03 ? 229 SER A C 1 ATOM 1780 O O . SER A 1 229 ? 22.267 39.293 35.141 1.00 35.19 ? 229 SER A O 1 ATOM 1781 C CB . SER A 1 229 ? 23.664 41.763 36.878 1.00 36.99 ? 229 SER A CB 1 ATOM 1782 O OG . SER A 1 229 ? 23.241 42.398 35.687 1.00 40.52 ? 229 SER A OG 1 ATOM 1783 N N . VAL A 1 230 ? 21.678 39.475 37.300 1.00 34.32 ? 230 VAL A N 1 ATOM 1784 C CA . VAL A 1 230 ? 20.368 38.885 37.105 1.00 34.09 ? 230 VAL A CA 1 ATOM 1785 C C . VAL A 1 230 ? 19.585 39.767 36.141 1.00 33.29 ? 230 VAL A C 1 ATOM 1786 O O . VAL A 1 230 ? 19.081 39.301 35.120 1.00 31.65 ? 230 VAL A O 1 ATOM 1787 C CB . VAL A 1 230 ? 19.614 38.791 38.450 1.00 36.17 ? 230 VAL A CB 1 ATOM 1788 C CG1 . VAL A 1 230 ? 18.230 38.184 38.240 1.00 36.76 ? 230 VAL A CG1 1 ATOM 1789 C CG2 . VAL A 1 230 ? 20.421 37.957 39.431 1.00 34.59 ? 230 VAL A CG2 1 ATOM 1790 N N . TRP A 1 231 ? 19.511 41.051 36.477 1.00 33.21 ? 231 TRP A N 1 ATOM 1791 C CA . TRP A 1 231 ? 18.805 42.057 35.686 1.00 33.69 ? 231 TRP A CA 1 ATOM 1792 C C . TRP A 1 231 ? 19.072 41.954 34.182 1.00 33.69 ? 231 TRP A C 1 ATOM 1793 O O . TRP A 1 231 ? 18.190 42.204 33.358 1.00 33.82 ? 231 TRP A O 1 ATOM 1794 C CB . TRP A 1 231 ? 19.218 43.448 36.168 1.00 33.44 ? 231 TRP A CB 1 ATOM 1795 C CG . TRP A 1 231 ? 19.287 43.549 37.662 1.00 36.47 ? 231 TRP A CG 1 ATOM 1796 C CD1 . TRP A 1 231 ? 20.326 44.031 38.404 1.00 35.01 ? 231 TRP A CD1 1 ATOM 1797 C CD2 . TRP A 1 231 ? 18.285 43.127 38.600 1.00 36.94 ? 231 TRP A CD2 1 ATOM 1798 N NE1 . TRP A 1 231 ? 20.035 43.935 39.747 1.00 36.58 ? 231 TRP A NE1 1 ATOM 1799 C CE2 . TRP A 1 231 ? 18.789 43.385 39.895 1.00 36.96 ? 231 TRP A CE2 1 ATOM 1800 C CE3 . TRP A 1 231 ? 17.011 42.555 38.472 1.00 34.76 ? 231 TRP A CE3 1 ATOM 1801 C CZ2 . TRP A 1 231 ? 18.063 43.092 41.054 1.00 38.34 ? 231 TRP A CZ2 1 ATOM 1802 C CZ3 . TRP A 1 231 ? 16.290 42.261 39.625 1.00 34.76 ? 231 TRP A CZ3 1 ATOM 1803 C CH2 . TRP A 1 231 ? 16.817 42.531 40.898 1.00 36.67 ? 231 TRP A CH2 1 ATOM 1804 N N . SER A 1 232 ? 20.291 41.569 33.831 1.00 32.30 ? 232 SER A N 1 ATOM 1805 C CA . SER A 1 232 ? 20.679 41.477 32.440 1.00 32.04 ? 232 SER A CA 1 ATOM 1806 C C . SER A 1 232 ? 20.646 40.068 31.852 1.00 32.18 ? 232 SER A C 1 ATOM 1807 O O . SER A 1 232 ? 20.242 39.874 30.705 1.00 31.85 ? 232 SER A O 1 ATOM 1808 C CB . SER A 1 232 ? 22.078 42.068 32.287 1.00 34.31 ? 232 SER A CB 1 ATOM 1809 O OG . SER A 1 232 ? 22.428 42.215 30.929 1.00 40.87 ? 232 SER A OG 1 ATOM 1810 N N . CYS A 1 233 ? 21.064 39.086 32.643 1.00 31.66 ? 233 CYS A N 1 ATOM 1811 C CA . CYS A 1 233 ? 21.115 37.706 32.187 1.00 28.94 ? 233 CYS A CA 1 ATOM 1812 C C . CYS A 1 233 ? 19.782 36.962 32.117 1.00 29.47 ? 233 CYS A C 1 ATOM 1813 O O . CYS A 1 233 ? 19.554 36.184 31.185 1.00 30.15 ? 233 CYS A O 1 ATOM 1814 C CB . CYS A 1 233 ? 22.099 36.932 33.057 1.00 28.65 ? 233 CYS A CB 1 ATOM 1815 S SG . CYS A 1 233 ? 23.794 37.609 33.006 1.00 29.74 ? 233 CYS A SG 1 ATOM 1816 N N . VAL A 1 234 ? 18.899 37.181 33.087 1.00 27.71 ? 234 VAL A N 1 ATOM 1817 C CA . VAL A 1 234 ? 17.616 36.494 33.067 1.00 26.38 ? 234 VAL A CA 1 ATOM 1818 C C . VAL A 1 234 ? 16.794 36.910 31.846 1.00 27.57 ? 234 VAL A C 1 ATOM 1819 O O . VAL A 1 234 ? 16.306 36.054 31.103 1.00 26.67 ? 234 VAL A O 1 ATOM 1820 C CB . VAL A 1 234 ? 16.827 36.739 34.370 1.00 26.25 ? 234 VAL A CB 1 ATOM 1821 C CG1 . VAL A 1 234 ? 15.363 36.343 34.192 1.00 24.45 ? 234 VAL A CG1 1 ATOM 1822 C CG2 . VAL A 1 234 ? 17.453 35.917 35.498 1.00 24.44 ? 234 VAL A CG2 1 ATOM 1823 N N . PRO A 1 235 ? 16.632 38.227 31.616 1.00 28.51 ? 235 PRO A N 1 ATOM 1824 C CA . PRO A 1 235 ? 15.858 38.675 30.449 1.00 28.89 ? 235 PRO A CA 1 ATOM 1825 C C . PRO A 1 235 ? 16.464 38.112 29.153 1.00 29.35 ? 235 PRO A C 1 ATOM 1826 O O . PRO A 1 235 ? 15.745 37.670 28.248 1.00 31.46 ? 235 PRO A O 1 ATOM 1827 C CB . PRO A 1 235 ? 15.970 40.194 30.526 1.00 28.14 ? 235 PRO A CB 1 ATOM 1828 C CG . PRO A 1 235 ? 16.044 40.442 32.003 1.00 28.66 ? 235 PRO A CG 1 ATOM 1829 C CD . PRO A 1 235 ? 17.013 39.373 32.462 1.00 28.07 ? 235 PRO A CD 1 ATOM 1830 N N . ALA A 1 236 ? 17.792 38.124 29.074 1.00 27.70 ? 236 ALA A N 1 ATOM 1831 C CA . ALA A 1 236 ? 18.493 37.608 27.908 1.00 26.23 ? 236 ALA A CA 1 ATOM 1832 C C . ALA A 1 236 ? 18.085 36.157 27.651 1.00 26.88 ? 236 ALA A C 1 ATOM 1833 O O . ALA A 1 236 ? 17.864 35.756 26.505 1.00 25.77 ? 236 ALA A O 1 ATOM 1834 C CB . ALA A 1 236 ? 19.993 37.697 28.124 1.00 23.43 ? 236 ALA A CB 1 ATOM 1835 N N . THR A 1 237 ? 17.978 35.371 28.720 1.00 26.56 ? 237 THR A N 1 ATOM 1836 C CA . THR A 1 237 ? 17.595 33.974 28.573 1.00 26.90 ? 237 THR A CA 1 ATOM 1837 C C . THR A 1 237 ? 16.173 33.859 28.038 1.00 26.56 ? 237 THR A C 1 ATOM 1838 O O . THR A 1 237 ? 15.907 33.092 27.107 1.00 25.15 ? 237 THR A O 1 ATOM 1839 C CB . THR A 1 237 ? 17.672 33.200 29.914 1.00 27.06 ? 237 THR A CB 1 ATOM 1840 O OG1 . THR A 1 237 ? 18.973 33.362 30.496 1.00 26.19 ? 237 THR A OG1 1 ATOM 1841 C CG2 . THR A 1 237 ? 17.411 31.710 29.674 1.00 25.13 ? 237 THR A CG2 1 ATOM 1842 N N . ILE A 1 238 ? 15.263 34.629 28.623 1.00 26.72 ? 238 ILE A N 1 ATOM 1843 C CA . ILE A 1 238 ? 13.869 34.586 28.202 1.00 28.69 ? 238 ILE A CA 1 ATOM 1844 C C . ILE A 1 238 ? 13.675 35.004 26.743 1.00 28.70 ? 238 ILE A C 1 ATOM 1845 O O . ILE A 1 238 ? 13.008 34.310 25.974 1.00 27.90 ? 238 ILE A O 1 ATOM 1846 C CB . ILE A 1 238 ? 12.994 35.471 29.113 1.00 29.16 ? 238 ILE A CB 1 ATOM 1847 C CG1 . ILE A 1 238 ? 13.173 35.022 30.565 1.00 31.74 ? 238 ILE A CG1 1 ATOM 1848 C CG2 . ILE A 1 238 ? 11.521 35.352 28.714 1.00 26.28 ? 238 ILE A CG2 1 ATOM 1849 C CD1 . ILE A 1 238 ? 12.410 35.851 31.572 1.00 33.67 ? 238 ILE A CD1 1 ATOM 1850 N N . TYR A 1 239 ? 14.272 36.122 26.353 1.00 28.26 ? 239 TYR A N 1 ATOM 1851 C CA . TYR A 1 239 ? 14.119 36.585 24.985 1.00 28.67 ? 239 TYR A CA 1 ATOM 1852 C C . TYR A 1 239 ? 14.707 35.651 23.936 1.00 26.99 ? 239 TYR A C 1 ATOM 1853 O O . TYR A 1 239 ? 14.037 35.306 22.960 1.00 24.47 ? 239 TYR A O 1 ATOM 1854 C CB . TYR A 1 239 ? 14.726 37.978 24.816 1.00 30.10 ? 239 TYR A CB 1 ATOM 1855 C CG . TYR A 1 239 ? 14.462 38.550 23.449 1.00 30.34 ? 239 TYR A CG 1 ATOM 1856 C CD1 . TYR A 1 239 ? 15.302 38.262 22.377 1.00 31.06 ? 239 TYR A CD1 1 ATOM 1857 C CD2 . TYR A 1 239 ? 13.329 39.325 23.213 1.00 31.87 ? 239 TYR A CD2 1 ATOM 1858 C CE1 . TYR A 1 239 ? 15.017 38.730 21.093 1.00 33.19 ? 239 TYR A CE1 1 ATOM 1859 C CE2 . TYR A 1 239 ? 13.034 39.799 21.940 1.00 33.66 ? 239 TYR A CE2 1 ATOM 1860 C CZ . TYR A 1 239 ? 13.880 39.498 20.885 1.00 34.49 ? 239 TYR A CZ 1 ATOM 1861 O OH . TYR A 1 239 ? 13.583 39.968 19.625 1.00 37.28 ? 239 TYR A OH 1 ATOM 1862 N N . CYS A 1 240 ? 15.957 35.250 24.133 1.00 27.34 ? 240 CYS A N 1 ATOM 1863 C CA . CYS A 1 240 ? 16.626 34.363 23.182 1.00 29.41 ? 240 CYS A CA 1 ATOM 1864 C C . CYS A 1 240 ? 15.993 32.983 23.062 1.00 30.11 ? 240 CYS A C 1 ATOM 1865 O O . CYS A 1 240 ? 15.809 32.474 21.955 1.00 32.12 ? 240 CYS A O 1 ATOM 1866 C CB . CYS A 1 240 ? 18.083 34.173 23.555 1.00 27.30 ? 240 CYS A CB 1 ATOM 1867 S SG . CYS A 1 240 ? 19.140 35.643 23.464 1.00 30.06 ? 240 CYS A SG 1 ATOM 1868 N N . ASN A 1 241 ? 15.673 32.365 24.192 1.00 29.09 ? 241 ASN A N 1 ATOM 1869 C CA . ASN A 1 241 ? 15.081 31.043 24.138 1.00 28.52 ? 241 ASN A CA 1 ATOM 1870 C C . ASN A 1 241 ? 13.719 31.029 23.461 1.00 28.50 ? 241 ASN A C 1 ATOM 1871 O O . ASN A 1 241 ? 13.347 30.036 22.832 1.00 27.47 ? 241 ASN A O 1 ATOM 1872 C CB . ASN A 1 241 ? 14.984 30.443 25.538 1.00 27.87 ? 241 ASN A CB 1 ATOM 1873 C CG . ASN A 1 241 ? 16.305 29.914 26.024 1.00 28.21 ? 241 ASN A CG 1 ATOM 1874 O OD1 . ASN A 1 241 ? 17.348 30.132 25.240 1.00 26.65 ? 241 ASN A OD1 1 ATOM 1875 N ND2 . ASN A 1 241 ? 16.394 29.317 27.092 1.00 32.11 ? 241 ASN A ND2 1 ATOM 1876 N N . ASN A 1 242 ? 12.978 32.127 23.578 1.00 28.62 ? 242 ASN A N 1 ATOM 1877 C CA . ASN A 1 242 ? 11.664 32.188 22.958 1.00 29.43 ? 242 ASN A CA 1 ATOM 1878 C C . ASN A 1 242 ? 11.803 32.466 21.473 1.00 30.33 ? 242 ASN A C 1 ATOM 1879 O O . ASN A 1 242 ? 11.072 31.909 20.648 1.00 30.75 ? 242 ASN A O 1 ATOM 1880 C CB . ASN A 1 242 ? 10.815 33.262 23.617 1.00 29.87 ? 242 ASN A CB 1 ATOM 1881 C CG . ASN A 1 242 ? 9.468 33.415 22.955 1.00 33.88 ? 242 ASN A CG 1 ATOM 1882 O OD1 . ASN A 1 242 ? 9.287 34.262 22.077 1.00 37.09 ? 242 ASN A OD1 1 ATOM 1883 N ND2 . ASN A 1 242 ? 8.513 32.586 23.358 1.00 34.61 ? 242 ASN A ND2 1 ATOM 1884 N N . ALA A 1 243 ? 12.770 33.309 21.137 1.00 29.50 ? 243 ALA A N 1 ATOM 1885 C CA . ALA A 1 243 ? 13.025 33.669 19.757 1.00 28.64 ? 243 ALA A CA 1 ATOM 1886 C C . ALA A 1 243 ? 13.753 32.585 18.963 1.00 29.83 ? 243 ALA A C 1 ATOM 1887 O O . ALA A 1 243 ? 13.358 32.269 17.840 1.00 31.60 ? 243 ALA A O 1 ATOM 1888 C CB . ALA A 1 243 ? 13.821 34.957 19.710 1.00 28.45 ? 243 ALA A CB 1 ATOM 1889 N N . GLN A 1 244 ? 14.803 32.005 19.538 1.00 28.60 ? 244 GLN A N 1 ATOM 1890 C CA . GLN A 1 244 ? 15.581 31.002 18.820 1.00 27.65 ? 244 GLN A CA 1 ATOM 1891 C C . GLN A 1 244 ? 15.268 29.532 19.063 1.00 27.70 ? 244 GLN A C 1 ATOM 1892 O O . GLN A 1 244 ? 15.519 28.714 18.181 1.00 29.19 ? 244 GLN A O 1 ATOM 1893 C CB . GLN A 1 244 ? 17.072 31.230 19.066 1.00 27.63 ? 244 GLN A CB 1 ATOM 1894 C CG . GLN A 1 244 ? 17.530 32.639 18.761 1.00 30.45 ? 244 GLN A CG 1 ATOM 1895 C CD . GLN A 1 244 ? 17.217 33.055 17.338 1.00 32.33 ? 244 GLN A CD 1 ATOM 1896 O OE1 . GLN A 1 244 ? 17.630 32.391 16.388 1.00 33.04 ? 244 GLN A OE1 1 ATOM 1897 N NE2 . GLN A 1 244 ? 16.483 34.156 17.184 1.00 31.11 ? 244 GLN A NE2 1 ATOM 1898 N N . LEU A 1 245 ? 14.734 29.180 20.231 1.00 26.61 ? 245 LEU A N 1 ATOM 1899 C CA . LEU A 1 245 ? 14.431 27.776 20.517 1.00 25.75 ? 245 LEU A CA 1 ATOM 1900 C C . LEU A 1 245 ? 12.947 27.378 20.411 1.00 26.80 ? 245 LEU A C 1 ATOM 1901 O O . LEU A 1 245 ? 12.621 26.279 19.957 1.00 26.08 ? 245 LEU A O 1 ATOM 1902 C CB . LEU A 1 245 ? 14.945 27.396 21.915 1.00 26.54 ? 245 LEU A CB 1 ATOM 1903 C CG . LEU A 1 245 ? 16.440 27.405 22.268 1.00 26.16 ? 245 LEU A CG 1 ATOM 1904 C CD1 . LEU A 1 245 ? 17.242 26.693 21.190 1.00 27.68 ? 245 LEU A CD1 1 ATOM 1905 C CD2 . LEU A 1 245 ? 16.921 28.832 22.391 1.00 31.27 ? 245 LEU A CD2 1 ATOM 1906 N N . ALA A 1 246 ? 12.054 28.271 20.829 1.00 27.98 ? 246 ALA A N 1 ATOM 1907 C CA . ALA A 1 246 ? 10.613 28.001 20.819 1.00 26.89 ? 246 ALA A CA 1 ATOM 1908 C C . ALA A 1 246 ? 10.014 27.560 19.479 1.00 26.83 ? 246 ALA A C 1 ATOM 1909 O O . ALA A 1 246 ? 9.235 26.610 19.435 1.00 27.53 ? 246 ALA A O 1 ATOM 1910 C CB . ALA A 1 246 ? 9.865 29.208 21.345 1.00 24.31 ? 246 ALA A CB 1 ATOM 1911 N N . PRO A 1 247 ? 10.354 28.246 18.374 1.00 26.36 ? 247 PRO A N 1 ATOM 1912 C CA . PRO A 1 247 ? 9.801 27.855 17.072 1.00 26.39 ? 247 PRO A CA 1 ATOM 1913 C C . PRO A 1 247 ? 10.053 26.382 16.768 1.00 27.59 ? 247 PRO A C 1 ATOM 1914 O O . PRO A 1 247 ? 9.124 25.628 16.458 1.00 28.64 ? 247 PRO A O 1 ATOM 1915 C CB . PRO A 1 247 ? 10.523 28.780 16.098 1.00 26.90 ? 247 PRO A CB 1 ATOM 1916 C CG . PRO A 1 247 ? 10.739 30.010 16.920 1.00 27.32 ? 247 PRO A CG 1 ATOM 1917 C CD . PRO A 1 247 ? 11.202 29.443 18.244 1.00 26.76 ? 247 PRO A CD 1 ATOM 1918 N N . TYR A 1 248 ? 11.314 25.977 16.864 1.00 28.05 ? 248 TYR A N 1 ATOM 1919 C CA . TYR A 1 248 ? 11.697 24.595 16.620 1.00 28.41 ? 248 TYR A CA 1 ATOM 1920 C C . TYR A 1 248 ? 10.895 23.664 17.527 1.00 29.53 ? 248 TYR A C 1 ATOM 1921 O O . TYR A 1 248 ? 10.335 22.666 17.069 1.00 29.77 ? 248 TYR A O 1 ATOM 1922 C CB . TYR A 1 248 ? 13.202 24.424 16.874 1.00 28.72 ? 248 TYR A CB 1 ATOM 1923 C CG . TYR A 1 248 ? 13.724 23.010 16.725 1.00 26.93 ? 248 TYR A CG 1 ATOM 1924 C CD1 . TYR A 1 248 ? 13.456 22.040 17.691 1.00 26.44 ? 248 TYR A CD1 1 ATOM 1925 C CD2 . TYR A 1 248 ? 14.497 22.646 15.626 1.00 26.19 ? 248 TYR A CD2 1 ATOM 1926 C CE1 . TYR A 1 248 ? 13.944 20.748 17.570 1.00 25.77 ? 248 TYR A CE1 1 ATOM 1927 C CE2 . TYR A 1 248 ? 14.992 21.353 15.492 1.00 26.59 ? 248 TYR A CE2 1 ATOM 1928 C CZ . TYR A 1 248 ? 14.712 20.408 16.472 1.00 28.71 ? 248 TYR A CZ 1 ATOM 1929 O OH . TYR A 1 248 ? 15.207 19.123 16.357 1.00 29.61 ? 248 TYR A OH 1 ATOM 1930 N N . GLN A 1 249 ? 10.822 23.996 18.811 1.00 30.14 ? 249 GLN A N 1 ATOM 1931 C CA . GLN A 1 249 ? 10.095 23.146 19.750 1.00 32.81 ? 249 GLN A CA 1 ATOM 1932 C C . GLN A 1 249 ? 8.610 22.990 19.455 1.00 33.45 ? 249 GLN A C 1 ATOM 1933 O O . GLN A 1 249 ? 8.038 21.918 19.658 1.00 32.71 ? 249 GLN A O 1 ATOM 1934 C CB . GLN A 1 249 ? 10.252 23.658 21.179 1.00 32.42 ? 249 GLN A CB 1 ATOM 1935 C CG . GLN A 1 249 ? 9.580 22.755 22.185 1.00 33.66 ? 249 GLN A CG 1 ATOM 1936 C CD . GLN A 1 249 ? 9.767 23.224 23.600 1.00 37.38 ? 249 GLN A CD 1 ATOM 1937 O OE1 . GLN A 1 249 ? 9.326 24.317 23.970 1.00 40.60 ? 249 GLN A OE1 1 ATOM 1938 N NE2 . GLN A 1 249 ? 10.426 22.401 24.412 1.00 37.28 ? 249 GLN A NE2 1 ATOM 1939 N N . ARG A 1 250 ? 7.981 24.058 18.986 1.00 35.48 ? 250 ARG A N 1 ATOM 1940 C CA . ARG A 1 250 ? 6.559 24.009 18.691 1.00 37.55 ? 250 ARG A CA 1 ATOM 1941 C C . ARG A 1 250 ? 6.199 23.045 17.561 1.00 35.91 ? 250 ARG A C 1 ATOM 1942 O O . ARG A 1 250 ? 5.052 22.641 17.442 1.00 36.95 ? 250 ARG A O 1 ATOM 1943 C CB . ARG A 1 250 ? 6.041 25.421 18.395 1.00 40.58 ? 250 ARG A CB 1 ATOM 1944 C CG . ARG A 1 250 ? 5.915 26.285 19.651 1.00 48.69 ? 250 ARG A CG 1 ATOM 1945 C CD . ARG A 1 250 ? 5.430 27.706 19.356 1.00 56.36 ? 250 ARG A CD 1 ATOM 1946 N NE . ARG A 1 250 ? 4.219 27.716 18.534 1.00 64.89 ? 250 ARG A NE 1 ATOM 1947 C CZ . ARG A 1 250 ? 3.477 28.796 18.287 1.00 68.94 ? 250 ARG A CZ 1 ATOM 1948 N NH1 . ARG A 1 250 ? 3.812 29.975 18.806 1.00 70.36 ? 250 ARG A NH1 1 ATOM 1949 N NH2 . ARG A 1 250 ? 2.401 28.701 17.509 1.00 70.10 ? 250 ARG A NH2 1 ATOM 1950 N N . THR A 1 251 ? 7.175 22.655 16.747 1.00 34.95 ? 251 THR A N 1 ATOM 1951 C CA . THR A 1 251 ? 6.909 21.732 15.642 1.00 33.23 ? 251 THR A CA 1 ATOM 1952 C C . THR A 1 251 ? 6.806 20.300 16.149 1.00 33.11 ? 251 THR A C 1 ATOM 1953 O O . THR A 1 251 ? 6.484 19.393 15.391 1.00 34.80 ? 251 THR A O 1 ATOM 1954 C CB . THR A 1 251 ? 8.034 21.752 14.577 1.00 32.92 ? 251 THR A CB 1 ATOM 1955 O OG1 . THR A 1 251 ? 9.188 21.080 15.096 1.00 31.50 ? 251 THR A OG1 1 ATOM 1956 C CG2 . THR A 1 251 ? 8.414 23.177 14.208 1.00 30.88 ? 251 THR A CG2 1 ATOM 1957 N N . GLY A 1 252 ? 7.103 20.090 17.423 1.00 32.49 ? 252 GLY A N 1 ATOM 1958 C CA . GLY A 1 252 ? 7.029 18.748 17.970 1.00 32.04 ? 252 GLY A CA 1 ATOM 1959 C C . GLY A 1 252 ? 8.282 17.943 17.698 1.00 32.47 ? 252 GLY A C 1 ATOM 1960 O O . GLY A 1 252 ? 8.379 16.768 18.068 1.00 32.25 ? 252 GLY A O 1 ATOM 1961 N N . ARG A 1 253 ? 9.249 18.584 17.051 1.00 31.84 ? 253 ARG A N 1 ATOM 1962 C CA . ARG A 1 253 ? 10.518 17.945 16.724 1.00 31.81 ? 253 ARG A CA 1 ATOM 1963 C C . ARG A 1 253 ? 11.394 17.777 17.975 1.00 29.90 ? 253 ARG A C 1 ATOM 1964 O O . ARG A 1 253 ? 11.308 18.575 18.907 1.00 29.28 ? 253 ARG A O 1 ATOM 1965 C CB . ARG A 1 253 ? 11.253 18.788 15.692 1.00 33.76 ? 253 ARG A CB 1 ATOM 1966 C CG . ARG A 1 253 ? 12.464 18.119 15.149 1.00 39.19 ? 253 ARG A CG 1 ATOM 1967 C CD . ARG A 1 253 ? 12.075 17.006 14.215 1.00 42.63 ? 253 ARG A CD 1 ATOM 1968 N NE . ARG A 1 253 ? 11.734 17.524 12.899 1.00 46.79 ? 253 ARG A NE 1 ATOM 1969 C CZ . ARG A 1 253 ? 11.672 16.779 11.801 1.00 49.90 ? 253 ARG A CZ 1 ATOM 1970 N NH1 . ARG A 1 253 ? 11.927 15.478 11.861 1.00 51.51 ? 253 ARG A NH1 1 ATOM 1971 N NH2 . ARG A 1 253 ? 11.363 17.337 10.639 1.00 51.56 ? 253 ARG A NH2 1 ATOM 1972 N N . ASN A 1 254 ? 12.238 16.744 17.988 1.00 28.30 ? 254 ASN A N 1 ATOM 1973 C CA . ASN A 1 254 ? 13.120 16.461 19.128 1.00 25.84 ? 254 ASN A CA 1 ATOM 1974 C C . ASN A 1 254 ? 14.294 17.443 19.184 1.00 25.69 ? 254 ASN A C 1 ATOM 1975 O O . ASN A 1 254 ? 15.065 17.538 18.235 1.00 27.09 ? 254 ASN A O 1 ATOM 1976 C CB . ASN A 1 254 ? 13.668 15.039 19.012 1.00 25.46 ? 254 ASN A CB 1 ATOM 1977 C CG . ASN A 1 254 ? 14.290 14.534 20.308 1.00 27.20 ? 254 ASN A CG 1 ATOM 1978 O OD1 . ASN A 1 254 ? 14.863 15.302 21.089 1.00 27.78 ? 254 ASN A OD1 1 ATOM 1979 N ND2 . ASN A 1 254 ? 14.193 13.228 20.534 1.00 25.41 ? 254 ASN A ND2 1 ATOM 1980 N N . VAL A 1 255 ? 14.447 18.167 20.289 1.00 24.71 ? 255 VAL A N 1 ATOM 1981 C CA . VAL A 1 255 ? 15.550 19.119 20.386 1.00 25.36 ? 255 VAL A CA 1 ATOM 1982 C C . VAL A 1 255 ? 16.897 18.416 20.549 1.00 26.19 ? 255 VAL A C 1 ATOM 1983 O O . VAL A 1 255 ? 17.951 19.044 20.417 1.00 26.33 ? 255 VAL A O 1 ATOM 1984 C CB . VAL A 1 255 ? 15.357 20.120 21.557 1.00 24.99 ? 255 VAL A CB 1 ATOM 1985 C CG1 . VAL A 1 255 ? 14.120 20.966 21.313 1.00 24.41 ? 255 VAL A CG1 1 ATOM 1986 C CG2 . VAL A 1 255 ? 15.248 19.371 22.881 1.00 26.20 ? 255 VAL A CG2 1 ATOM 1987 N N . TYR A 1 256 ? 16.859 17.112 20.816 1.00 25.08 ? 256 TYR A N 1 ATOM 1988 C CA . TYR A 1 256 ? 18.075 16.330 20.990 1.00 25.54 ? 256 TYR A CA 1 ATOM 1989 C C . TYR A 1 256 ? 18.493 15.559 19.731 1.00 26.50 ? 256 TYR A C 1 ATOM 1990 O O . TYR A 1 256 ? 19.647 15.141 19.603 1.00 25.67 ? 256 TYR A O 1 ATOM 1991 C CB . TYR A 1 256 ? 17.901 15.352 22.146 1.00 25.52 ? 256 TYR A CB 1 ATOM 1992 C CG . TYR A 1 256 ? 17.598 16.024 23.458 1.00 25.25 ? 256 TYR A CG 1 ATOM 1993 C CD1 . TYR A 1 256 ? 18.402 17.058 23.931 1.00 25.01 ? 256 TYR A CD1 1 ATOM 1994 C CD2 . TYR A 1 256 ? 16.507 15.625 24.234 1.00 25.64 ? 256 TYR A CD2 1 ATOM 1995 C CE1 . TYR A 1 256 ? 18.134 17.684 25.149 1.00 26.12 ? 256 TYR A CE1 1 ATOM 1996 C CE2 . TYR A 1 256 ? 16.227 16.245 25.452 1.00 27.99 ? 256 TYR A CE2 1 ATOM 1997 C CZ . TYR A 1 256 ? 17.047 17.274 25.902 1.00 26.49 ? 256 TYR A CZ 1 ATOM 1998 O OH . TYR A 1 256 ? 16.776 17.888 27.100 1.00 27.27 ? 256 TYR A OH 1 ATOM 1999 N N . ASP A 1 257 ? 17.554 15.367 18.811 1.00 25.26 ? 257 ASP A N 1 ATOM 2000 C CA . ASP A 1 257 ? 17.841 14.652 17.574 1.00 25.85 ? 257 ASP A CA 1 ATOM 2001 C C . ASP A 1 257 ? 16.911 15.178 16.487 1.00 26.34 ? 257 ASP A C 1 ATOM 2002 O O . ASP A 1 257 ? 15.731 14.826 16.448 1.00 27.45 ? 257 ASP A O 1 ATOM 2003 C CB . ASP A 1 257 ? 17.641 13.146 17.778 1.00 26.47 ? 257 ASP A CB 1 ATOM 2004 C CG . ASP A 1 257 ? 18.122 12.327 16.592 1.00 27.59 ? 257 ASP A CG 1 ATOM 2005 O OD1 . ASP A 1 257 ? 18.494 11.143 16.786 1.00 26.13 ? 257 ASP A OD1 1 ATOM 2006 O OD2 . ASP A 1 257 ? 18.116 12.870 15.466 1.00 26.02 ? 257 ASP A OD2 1 ATOM 2007 N N . ILE A 1 258 ? 17.455 16.017 15.607 1.00 23.76 ? 258 ILE A N 1 ATOM 2008 C CA . ILE A 1 258 ? 16.684 16.642 14.534 1.00 24.03 ? 258 ILE A CA 1 ATOM 2009 C C . ILE A 1 258 ? 15.954 15.680 13.583 1.00 24.55 ? 258 ILE A C 1 ATOM 2010 O O . ILE A 1 258 ? 15.042 16.080 12.851 1.00 23.56 ? 258 ILE A O 1 ATOM 2011 C CB . ILE A 1 258 ? 17.591 17.582 13.717 1.00 21.78 ? 258 ILE A CB 1 ATOM 2012 C CG1 . ILE A 1 258 ? 16.741 18.496 12.835 1.00 19.76 ? 258 ILE A CG1 1 ATOM 2013 C CG2 . ILE A 1 258 ? 18.562 16.771 12.888 1.00 21.04 ? 258 ILE A CG2 1 ATOM 2014 C CD1 . ILE A 1 258 ? 17.516 19.691 12.298 1.00 18.11 ? 258 ILE A CD1 1 ATOM 2015 N N . ARG A 1 259 ? 16.347 14.414 13.608 1.00 23.61 ? 259 ARG A N 1 ATOM 2016 C CA . ARG A 1 259 ? 15.731 13.412 12.760 1.00 23.67 ? 259 ARG A CA 1 ATOM 2017 C C . ARG A 1 259 ? 14.488 12.802 13.404 1.00 25.96 ? 259 ARG A C 1 ATOM 2018 O O . ARG A 1 259 ? 13.729 12.102 12.741 1.00 27.84 ? 259 ARG A O 1 ATOM 2019 C CB . ARG A 1 259 ? 16.733 12.293 12.474 1.00 23.78 ? 259 ARG A CB 1 ATOM 2020 C CG . ARG A 1 259 ? 18.070 12.744 11.896 1.00 23.37 ? 259 ARG A CG 1 ATOM 2021 C CD . ARG A 1 259 ? 19.086 11.606 11.995 1.00 22.37 ? 259 ARG A CD 1 ATOM 2022 N NE . ARG A 1 259 ? 19.301 11.202 13.384 1.00 19.70 ? 259 ARG A NE 1 ATOM 2023 C CZ . ARG A 1 259 ? 20.128 10.238 13.775 1.00 19.77 ? 259 ARG A CZ 1 ATOM 2024 N NH1 . ARG A 1 259 ? 20.838 9.549 12.886 1.00 21.21 ? 259 ARG A NH1 1 ATOM 2025 N NH2 . ARG A 1 259 ? 20.254 9.968 15.064 1.00 16.75 ? 259 ARG A NH2 1 ATOM 2026 N N . LYS A 1 260 ? 14.280 13.059 14.693 1.00 27.19 ? 260 LYS A N 1 ATOM 2027 C CA . LYS A 1 260 ? 13.147 12.486 15.411 1.00 27.50 ? 260 LYS A CA 1 ATOM 2028 C C . LYS A 1 260 ? 12.141 13.480 15.957 1.00 30.94 ? 260 LYS A C 1 ATOM 2029 O O . LYS A 1 260 ? 12.364 14.694 15.974 1.00 32.05 ? 260 LYS A O 1 ATOM 2030 C CB . LYS A 1 260 ? 13.644 11.657 16.594 1.00 26.15 ? 260 LYS A CB 1 ATOM 2031 C CG . LYS A 1 260 ? 14.645 10.593 16.242 1.00 28.07 ? 260 LYS A CG 1 ATOM 2032 C CD . LYS A 1 260 ? 15.048 9.787 17.461 1.00 26.65 ? 260 LYS A CD 1 ATOM 2033 C CE . LYS A 1 260 ? 16.076 8.739 17.076 1.00 27.78 ? 260 LYS A CE 1 ATOM 2034 N NZ . LYS A 1 260 ? 16.435 7.848 18.207 1.00 28.52 ? 260 LYS A NZ 1 ATOM 2035 N N . ASP A 1 261 ? 11.024 12.941 16.425 1.00 34.10 ? 261 ASP A N 1 ATOM 2036 C CA . ASP A 1 261 ? 9.999 13.762 17.034 1.00 37.60 ? 261 ASP A CA 1 ATOM 2037 C C . ASP A 1 261 ? 10.108 13.534 18.523 1.00 38.28 ? 261 ASP A C 1 ATOM 2038 O O . ASP A 1 261 ? 10.425 12.434 18.969 1.00 38.07 ? 261 ASP A O 1 ATOM 2039 C CB . ASP A 1 261 ? 8.610 13.371 16.542 1.00 40.67 ? 261 ASP A CB 1 ATOM 2040 C CG . ASP A 1 261 ? 8.272 14.010 15.214 1.00 45.12 ? 261 ASP A CG 1 ATOM 2041 O OD1 . ASP A 1 261 ? 8.857 13.610 14.186 1.00 49.42 ? 261 ASP A OD1 1 ATOM 2042 O OD2 . ASP A 1 261 ? 7.432 14.932 15.202 1.00 48.96 ? 261 ASP A OD2 1 ATOM 2043 N N . CYS A 1 262 ? 9.877 14.583 19.296 1.00 40.28 ? 262 CYS A N 1 ATOM 2044 C CA . CYS A 1 262 ? 9.953 14.453 20.733 1.00 41.72 ? 262 CYS A CA 1 ATOM 2045 C C . CYS A 1 262 ? 8.769 13.627 21.188 1.00 46.30 ? 262 CYS A C 1 ATOM 2046 O O . CYS A 1 262 ? 7.623 14.049 21.043 1.00 48.26 ? 262 CYS A O 1 ATOM 2047 C CB . CYS A 1 262 ? 9.889 15.813 21.398 1.00 39.30 ? 262 CYS A CB 1 ATOM 2048 S SG . CYS A 1 262 ? 9.855 15.625 23.196 1.00 32.45 ? 262 CYS A SG 1 ATOM 2049 N N . GLU A 1 263 ? 9.037 12.450 21.737 1.00 50.86 ? 263 GLU A N 1 ATOM 2050 C CA . GLU A 1 263 ? 7.963 11.580 22.197 1.00 55.60 ? 263 GLU A CA 1 ATOM 2051 C C . GLU A 1 263 ? 8.247 10.986 23.566 1.00 57.45 ? 263 GLU A C 1 ATOM 2052 O O . GLU A 1 263 ? 9.348 10.506 23.826 1.00 59.22 ? 263 GLU A O 1 ATOM 2053 C CB . GLU A 1 263 ? 7.746 10.457 21.190 1.00 57.21 ? 263 GLU A CB 1 ATOM 2054 C CG . GLU A 1 263 ? 9.004 9.693 20.867 1.00 61.61 ? 263 GLU A CG 1 ATOM 2055 C CD . GLU A 1 263 ? 8.765 8.618 19.835 1.00 65.02 ? 263 GLU A CD 1 ATOM 2056 O OE1 . GLU A 1 263 ? 8.272 8.957 18.735 1.00 66.38 ? 263 GLU A OE1 1 ATOM 2057 O OE2 . GLU A 1 263 ? 9.066 7.438 20.126 1.00 66.26 ? 263 GLU A OE2 1 ATOM 2058 N N . GLY A 1 264 ? 7.248 11.025 24.441 1.00 58.68 ? 264 GLY A N 1 ATOM 2059 C CA . GLY A 1 264 ? 7.425 10.472 25.769 1.00 60.05 ? 264 GLY A CA 1 ATOM 2060 C C . GLY A 1 264 ? 7.351 11.498 26.881 1.00 61.85 ? 264 GLY A C 1 ATOM 2061 O O . GLY A 1 264 ? 6.415 12.300 26.946 1.00 62.67 ? 264 GLY A O 1 ATOM 2062 N N . GLY A 1 265 ? 8.352 11.474 27.757 1.00 62.26 ? 265 GLY A N 1 ATOM 2063 C CA . GLY A 1 265 ? 8.383 12.400 28.875 1.00 61.52 ? 265 GLY A CA 1 ATOM 2064 C C . GLY A 1 265 ? 8.930 13.784 28.575 1.00 60.83 ? 265 GLY A C 1 ATOM 2065 O O . GLY A 1 265 ? 8.896 14.271 27.439 1.00 58.85 ? 265 GLY A O 1 ATOM 2066 N N . ASN A 1 266 ? 9.438 14.421 29.622 1.00 60.62 ? 266 ASN A N 1 ATOM 2067 C CA . ASN A 1 266 ? 9.986 15.761 29.510 1.00 60.50 ? 266 ASN A CA 1 ATOM 2068 C C . ASN A 1 266 ? 11.311 15.723 28.765 1.00 59.05 ? 266 ASN A C 1 ATOM 2069 O O . ASN A 1 266 ? 11.872 16.773 28.446 1.00 60.84 ? 266 ASN A O 1 ATOM 2070 C CB . ASN A 1 266 ? 10.222 16.367 30.903 1.00 62.58 ? 266 ASN A CB 1 ATOM 2071 C CG . ASN A 1 266 ? 9.144 15.984 31.912 1.00 64.43 ? 266 ASN A CG 1 ATOM 2072 O OD1 . ASN A 1 266 ? 9.011 14.815 32.284 1.00 65.65 ? 266 ASN A OD1 1 ATOM 2073 N ND2 . ASN A 1 266 ? 8.375 16.973 32.364 1.00 64.48 ? 266 ASN A ND2 1 ATOM 2074 N N . LEU A 1 267 ? 11.814 14.522 28.487 1.00 55.75 ? 267 LEU A N 1 ATOM 2075 C CA . LEU A 1 267 ? 13.098 14.399 27.808 1.00 51.36 ? 267 LEU A CA 1 ATOM 2076 C C . LEU A 1 267 ? 13.071 13.797 26.408 1.00 47.94 ? 267 LEU A C 1 ATOM 2077 O O . LEU A 1 267 ? 14.121 13.583 25.805 1.00 48.47 ? 267 LEU A O 1 ATOM 2078 C CB . LEU A 1 267 ? 14.077 13.636 28.702 1.00 53.21 ? 267 LEU A CB 1 ATOM 2079 C CG . LEU A 1 267 ? 14.507 14.407 29.961 1.00 54.98 ? 267 LEU A CG 1 ATOM 2080 C CD1 . LEU A 1 267 ? 15.345 13.516 30.863 1.00 55.38 ? 267 LEU A CD1 1 ATOM 2081 C CD2 . LEU A 1 267 ? 15.297 15.647 29.562 1.00 54.35 ? 267 LEU A CD2 1 ATOM 2082 N N . CYS A 1 268 ? 11.874 13.519 25.900 1.00 43.38 ? 268 CYS A N 1 ATOM 2083 C CA . CYS A 1 268 ? 11.698 12.993 24.547 1.00 38.81 ? 268 CYS A CA 1 ATOM 2084 C C . CYS A 1 268 ? 12.176 11.574 24.249 1.00 36.70 ? 268 CYS A C 1 ATOM 2085 O O . CYS A 1 268 ? 12.080 11.119 23.113 1.00 35.76 ? 268 CYS A O 1 ATOM 2086 C CB . CYS A 1 268 ? 12.345 13.948 23.540 1.00 37.63 ? 268 CYS A CB 1 ATOM 2087 S SG . CYS A 1 268 ? 11.815 15.689 23.686 1.00 35.42 ? 268 CYS A SG 1 ATOM 2088 N N . TYR A 1 269 ? 12.700 10.877 25.247 1.00 35.15 ? 269 TYR A N 1 ATOM 2089 C CA . TYR A 1 269 ? 13.149 9.502 25.049 1.00 33.99 ? 269 TYR A CA 1 ATOM 2090 C C . TYR A 1 269 ? 12.388 8.615 26.034 1.00 35.09 ? 269 TYR A C 1 ATOM 2091 O O . TYR A 1 269 ? 12.778 8.478 27.196 1.00 35.01 ? 269 TYR A O 1 ATOM 2092 C CB . TYR A 1 269 ? 14.657 9.392 25.277 1.00 32.82 ? 269 TYR A CB 1 ATOM 2093 C CG . TYR A 1 269 ? 15.497 9.895 24.122 1.00 31.42 ? 269 TYR A CG 1 ATOM 2094 C CD1 . TYR A 1 269 ? 15.870 9.046 23.081 1.00 31.05 ? 269 TYR A CD1 1 ATOM 2095 C CD2 . TYR A 1 269 ? 15.930 11.219 24.073 1.00 30.04 ? 269 TYR A CD2 1 ATOM 2096 C CE1 . TYR A 1 269 ? 16.658 9.503 22.022 1.00 29.43 ? 269 TYR A CE1 1 ATOM 2097 C CE2 . TYR A 1 269 ? 16.714 11.681 23.021 1.00 27.73 ? 269 TYR A CE2 1 ATOM 2098 C CZ . TYR A 1 269 ? 17.076 10.821 22.005 1.00 28.17 ? 269 TYR A CZ 1 ATOM 2099 O OH . TYR A 1 269 ? 17.880 11.276 20.986 1.00 28.22 ? 269 TYR A OH 1 ATOM 2100 N N . PRO A 1 270 ? 11.282 8.004 25.574 1.00 35.99 ? 270 PRO A N 1 ATOM 2101 C CA . PRO A 1 270 ? 10.411 7.122 26.358 1.00 36.31 ? 270 PRO A CA 1 ATOM 2102 C C . PRO A 1 270 ? 11.150 6.150 27.259 1.00 35.83 ? 270 PRO A C 1 ATOM 2103 O O . PRO A 1 270 ? 10.778 5.950 28.413 1.00 37.57 ? 270 PRO A O 1 ATOM 2104 C CB . PRO A 1 270 ? 9.598 6.403 25.285 1.00 35.61 ? 270 PRO A CB 1 ATOM 2105 C CG . PRO A 1 270 ? 9.450 7.458 24.245 1.00 36.21 ? 270 PRO A CG 1 ATOM 2106 C CD . PRO A 1 270 ? 10.849 8.031 24.164 1.00 36.26 ? 270 PRO A CD 1 ATOM 2107 N N . THR A 1 271 ? 12.201 5.552 26.723 1.00 35.39 ? 271 THR A N 1 ATOM 2108 C CA . THR A 1 271 ? 12.996 4.587 27.462 1.00 35.66 ? 271 THR A CA 1 ATOM 2109 C C . THR A 1 271 ? 13.632 5.076 28.768 1.00 35.09 ? 271 THR A C 1 ATOM 2110 O O . THR A 1 271 ? 13.898 4.268 29.656 1.00 35.63 ? 271 THR A O 1 ATOM 2111 C CB . THR A 1 271 ? 14.080 4.009 26.548 1.00 36.12 ? 271 THR A CB 1 ATOM 2112 O OG1 . THR A 1 271 ? 13.446 3.209 25.548 1.00 38.08 ? 271 THR A OG1 1 ATOM 2113 C CG2 . THR A 1 271 ? 15.062 3.146 27.334 1.00 41.32 ? 271 THR A CG2 1 ATOM 2114 N N . LEU A 1 272 ? 13.883 6.376 28.902 1.00 33.82 ? 272 LEU A N 1 ATOM 2115 C CA . LEU A 1 272 ? 14.484 6.862 30.136 1.00 34.40 ? 272 LEU A CA 1 ATOM 2116 C C . LEU A 1 272 ? 13.626 6.447 31.326 1.00 34.15 ? 272 LEU A C 1 ATOM 2117 O O . LEU A 1 272 ? 14.135 6.193 32.418 1.00 32.61 ? 272 LEU A O 1 ATOM 2118 C CB . LEU A 1 272 ? 14.624 8.384 30.121 1.00 34.98 ? 272 LEU A CB 1 ATOM 2119 C CG . LEU A 1 272 ? 15.717 8.991 29.245 1.00 37.04 ? 272 LEU A CG 1 ATOM 2120 C CD1 . LEU A 1 272 ? 15.724 10.498 29.432 1.00 35.77 ? 272 LEU A CD1 1 ATOM 2121 C CD2 . LEU A 1 272 ? 17.073 8.408 29.619 1.00 37.63 ? 272 LEU A CD2 1 ATOM 2122 N N . GLN A 1 273 ? 12.319 6.378 31.099 1.00 34.09 ? 273 GLN A N 1 ATOM 2123 C CA . GLN A 1 273 ? 11.366 5.998 32.135 1.00 34.26 ? 273 GLN A CA 1 ATOM 2124 C C . GLN A 1 273 ? 11.767 4.649 32.737 1.00 33.23 ? 273 GLN A C 1 ATOM 2125 O O . GLN A 1 273 ? 11.695 4.443 33.957 1.00 31.19 ? 273 GLN A O 1 ATOM 2126 C CB . GLN A 1 273 ? 9.956 5.924 31.531 1.00 35.98 ? 273 GLN A CB 1 ATOM 2127 C CG . GLN A 1 273 ? 8.852 5.650 32.535 1.00 40.37 ? 273 GLN A CG 1 ATOM 2128 C CD . GLN A 1 273 ? 8.873 6.624 33.704 1.00 44.94 ? 273 GLN A CD 1 ATOM 2129 O OE1 . GLN A 1 273 ? 8.794 7.843 33.519 1.00 47.34 ? 273 GLN A OE1 1 ATOM 2130 N NE2 . GLN A 1 273 ? 8.981 6.088 34.920 1.00 46.36 ? 273 GLN A NE2 1 ATOM 2131 N N . ASP A 1 274 ? 12.203 3.734 31.877 1.00 31.37 ? 274 ASP A N 1 ATOM 2132 C CA . ASP A 1 274 ? 12.622 2.426 32.341 1.00 31.89 ? 274 ASP A CA 1 ATOM 2133 C C . ASP A 1 274 ? 13.698 2.489 33.411 1.00 32.31 ? 274 ASP A C 1 ATOM 2134 O O . ASP A 1 274 ? 13.603 1.778 34.410 1.00 34.34 ? 274 ASP A O 1 ATOM 2135 C CB . ASP A 1 274 ? 13.105 1.563 31.184 1.00 31.67 ? 274 ASP A CB 1 ATOM 2136 C CG . ASP A 1 274 ? 11.973 1.067 30.332 1.00 33.07 ? 274 ASP A CG 1 ATOM 2137 O OD1 . ASP A 1 274 ? 10.871 0.862 30.876 1.00 35.97 ? 274 ASP A OD1 1 ATOM 2138 O OD2 . ASP A 1 274 ? 12.179 0.868 29.125 1.00 36.57 ? 274 ASP A OD2 1 ATOM 2139 N N . ILE A 1 275 ? 14.722 3.321 33.230 1.00 31.23 ? 275 ILE A N 1 ATOM 2140 C CA . ILE A 1 275 ? 15.745 3.380 34.263 1.00 31.57 ? 275 ILE A CA 1 ATOM 2141 C C . ILE A 1 275 ? 15.183 4.028 35.529 1.00 31.62 ? 275 ILE A C 1 ATOM 2142 O O . ILE A 1 275 ? 15.579 3.668 36.639 1.00 31.75 ? 275 ILE A O 1 ATOM 2143 C CB . ILE A 1 275 ? 17.060 4.109 33.809 1.00 31.99 ? 275 ILE A CB 1 ATOM 2144 C CG1 . ILE A 1 275 ? 17.245 5.393 34.603 1.00 32.13 ? 275 ILE A CG1 1 ATOM 2145 C CG2 . ILE A 1 275 ? 17.062 4.362 32.308 1.00 30.70 ? 275 ILE A CG2 1 ATOM 2146 C CD1 . ILE A 1 275 ? 18.647 5.919 34.562 1.00 36.51 ? 275 ILE A CD1 1 ATOM 2147 N N . ASP A 1 276 ? 14.256 4.971 35.373 1.00 32.32 ? 276 ASP A N 1 ATOM 2148 C CA . ASP A 1 276 ? 13.637 5.606 36.539 1.00 33.55 ? 276 ASP A CA 1 ATOM 2149 C C . ASP A 1 276 ? 12.915 4.529 37.361 1.00 33.40 ? 276 ASP A C 1 ATOM 2150 O O . ASP A 1 276 ? 13.013 4.491 38.592 1.00 32.41 ? 276 ASP A O 1 ATOM 2151 C CB . ASP A 1 276 ? 12.629 6.677 36.104 1.00 36.01 ? 276 ASP A CB 1 ATOM 2152 C CG . ASP A 1 276 ? 13.283 8.015 35.811 1.00 39.16 ? 276 ASP A CG 1 ATOM 2153 O OD1 . ASP A 1 276 ? 13.354 8.870 36.716 1.00 41.84 ? 276 ASP A OD1 1 ATOM 2154 O OD2 . ASP A 1 276 ? 13.736 8.214 34.671 1.00 41.52 ? 276 ASP A OD2 1 ATOM 2155 N N . ASP A 1 277 ? 12.192 3.645 36.680 1.00 31.52 ? 277 ASP A N 1 ATOM 2156 C CA . ASP A 1 277 ? 11.485 2.598 37.392 1.00 32.28 ? 277 ASP A CA 1 ATOM 2157 C C . ASP A 1 277 ? 12.455 1.600 38.012 1.00 31.15 ? 277 ASP A C 1 ATOM 2158 O O . ASP A 1 277 ? 12.203 1.066 39.091 1.00 31.32 ? 277 ASP A O 1 ATOM 2159 C CB . ASP A 1 277 ? 10.505 1.873 36.463 1.00 32.85 ? 277 ASP A CB 1 ATOM 2160 C CG . ASP A 1 277 ? 9.377 2.773 35.992 1.00 35.23 ? 277 ASP A CG 1 ATOM 2161 O OD1 . ASP A 1 277 ? 9.006 3.721 36.724 1.00 34.69 ? 277 ASP A OD1 1 ATOM 2162 O OD2 . ASP A 1 277 ? 8.850 2.523 34.891 1.00 36.83 ? 277 ASP A OD2 1 ATOM 2163 N N . TYR A 1 278 ? 13.566 1.350 37.334 1.00 29.17 ? 278 TYR A N 1 ATOM 2164 C CA . TYR A 1 278 ? 14.549 0.415 37.849 1.00 27.68 ? 278 TYR A CA 1 ATOM 2165 C C . TYR A 1 278 ? 15.180 0.956 39.129 1.00 26.99 ? 278 TYR A C 1 ATOM 2166 O O . TYR A 1 278 ? 15.300 0.233 40.114 1.00 28.13 ? 278 TYR A O 1 ATOM 2167 C CB . TYR A 1 278 ? 15.628 0.133 36.790 1.00 26.35 ? 278 TYR A CB 1 ATOM 2168 C CG . TYR A 1 278 ? 16.795 -0.667 37.319 1.00 26.16 ? 278 TYR A CG 1 ATOM 2169 C CD1 . TYR A 1 278 ? 17.838 -0.037 37.999 1.00 26.71 ? 278 TYR A CD1 1 ATOM 2170 C CD2 . TYR A 1 278 ? 16.824 -2.059 37.206 1.00 26.58 ? 278 TYR A CD2 1 ATOM 2171 C CE1 . TYR A 1 278 ? 18.880 -0.766 38.561 1.00 28.25 ? 278 TYR A CE1 1 ATOM 2172 C CE2 . TYR A 1 278 ? 17.865 -2.807 37.767 1.00 26.14 ? 278 TYR A CE2 1 ATOM 2173 C CZ . TYR A 1 278 ? 18.888 -2.150 38.447 1.00 28.81 ? 278 TYR A CZ 1 ATOM 2174 O OH . TYR A 1 278 ? 19.907 -2.861 39.043 1.00 28.67 ? 278 TYR A OH 1 ATOM 2175 N N . LEU A 1 279 ? 15.567 2.229 39.116 1.00 26.02 ? 279 LEU A N 1 ATOM 2176 C CA . LEU A 1 279 ? 16.190 2.857 40.277 1.00 25.91 ? 279 LEU A CA 1 ATOM 2177 C C . LEU A 1 279 ? 15.252 3.066 41.457 1.00 26.02 ? 279 LEU A C 1 ATOM 2178 O O . LEU A 1 279 ? 15.712 3.293 42.577 1.00 26.94 ? 279 LEU A O 1 ATOM 2179 C CB . LEU A 1 279 ? 16.801 4.200 39.888 1.00 24.32 ? 279 LEU A CB 1 ATOM 2180 C CG . LEU A 1 279 ? 18.299 4.279 39.574 1.00 25.98 ? 279 LEU A CG 1 ATOM 2181 C CD1 . LEU A 1 279 ? 18.904 2.890 39.369 1.00 21.21 ? 279 LEU A CD1 1 ATOM 2182 C CD2 . LEU A 1 279 ? 18.482 5.172 38.344 1.00 22.60 ? 279 LEU A CD2 1 ATOM 2183 N N . ASN A 1 280 ? 13.946 2.992 41.214 1.00 25.79 ? 280 ASN A N 1 ATOM 2184 C CA . ASN A 1 280 ? 12.967 3.178 42.282 1.00 26.49 ? 280 ASN A CA 1 ATOM 2185 C C . ASN A 1 280 ? 12.505 1.882 42.932 1.00 27.27 ? 280 ASN A C 1 ATOM 2186 O O . ASN A 1 280 ? 11.666 1.903 43.833 1.00 28.09 ? 280 ASN A O 1 ATOM 2187 C CB . ASN A 1 280 ? 11.748 3.952 41.769 1.00 24.68 ? 280 ASN A CB 1 ATOM 2188 C CG . ASN A 1 280 ? 11.972 5.455 41.773 1.00 25.63 ? 280 ASN A CG 1 ATOM 2189 O OD1 . ASN A 1 280 ? 12.187 6.053 42.825 1.00 25.33 ? 280 ASN A OD1 1 ATOM 2190 N ND2 . ASN A 1 280 ? 11.932 6.069 40.595 1.00 25.02 ? 280 ASN A ND2 1 ATOM 2191 N N . GLN A 1 281 ? 13.043 0.751 42.485 1.00 26.75 ? 281 GLN A N 1 ATOM 2192 C CA . GLN A 1 281 ? 12.658 -0.520 43.077 1.00 27.56 ? 281 GLN A CA 1 ATOM 2193 C C . GLN A 1 281 ? 13.196 -0.640 44.506 1.00 27.72 ? 281 GLN A C 1 ATOM 2194 O O . GLN A 1 281 ? 14.266 -0.119 44.831 1.00 29.34 ? 281 GLN A O 1 ATOM 2195 C CB . GLN A 1 281 ? 13.164 -1.675 42.222 1.00 28.64 ? 281 GLN A CB 1 ATOM 2196 C CG . GLN A 1 281 ? 12.398 -1.846 40.931 1.00 29.48 ? 281 GLN A CG 1 ATOM 2197 C CD . GLN A 1 281 ? 12.955 -2.965 40.070 1.00 30.54 ? 281 GLN A CD 1 ATOM 2198 O OE1 . GLN A 1 281 ? 14.102 -2.905 39.613 1.00 30.94 ? 281 GLN A OE1 1 ATOM 2199 N NE2 . GLN A 1 281 ? 12.146 -3.997 39.848 1.00 29.71 ? 281 GLN A NE2 1 ATOM 2200 N N . ASP A 1 282 ? 12.442 -1.328 45.353 1.00 26.98 ? 282 ASP A N 1 ATOM 2201 C CA . ASP A 1 282 ? 12.807 -1.523 46.749 1.00 26.82 ? 282 ASP A CA 1 ATOM 2202 C C . ASP A 1 282 ? 14.195 -2.151 46.929 1.00 27.86 ? 282 ASP A C 1 ATOM 2203 O O . ASP A 1 282 ? 15.009 -1.653 47.710 1.00 27.64 ? 282 ASP A O 1 ATOM 2204 C CB . ASP A 1 282 ? 11.761 -2.410 47.426 1.00 27.35 ? 282 ASP A CB 1 ATOM 2205 C CG . ASP A 1 282 ? 11.884 -2.418 48.936 1.00 29.22 ? 282 ASP A CG 1 ATOM 2206 O OD1 . ASP A 1 282 ? 11.434 -3.404 49.560 1.00 30.28 ? 282 ASP A OD1 1 ATOM 2207 O OD2 . ASP A 1 282 ? 12.412 -1.438 49.504 1.00 30.65 ? 282 ASP A OD2 1 ATOM 2208 N N . TYR A 1 283 ? 14.477 -3.234 46.208 1.00 27.59 ? 283 TYR A N 1 ATOM 2209 C CA . TYR A 1 283 ? 15.768 -3.889 46.369 1.00 28.41 ? 283 TYR A CA 1 ATOM 2210 C C . TYR A 1 283 ? 16.940 -3.128 45.765 1.00 29.04 ? 283 TYR A C 1 ATOM 2211 O O . TYR A 1 283 ? 18.068 -3.234 46.256 1.00 29.47 ? 283 TYR A O 1 ATOM 2212 C CB . TYR A 1 283 ? 15.732 -5.331 45.830 1.00 27.22 ? 283 TYR A CB 1 ATOM 2213 C CG . TYR A 1 283 ? 16.019 -5.501 44.358 1.00 24.89 ? 283 TYR A CG 1 ATOM 2214 C CD1 . TYR A 1 283 ? 15.019 -5.321 43.398 1.00 25.27 ? 283 TYR A CD1 1 ATOM 2215 C CD2 . TYR A 1 283 ? 17.289 -5.879 43.925 1.00 24.24 ? 283 TYR A CD2 1 ATOM 2216 C CE1 . TYR A 1 283 ? 15.279 -5.519 42.044 1.00 23.05 ? 283 TYR A CE1 1 ATOM 2217 C CE2 . TYR A 1 283 ? 17.565 -6.078 42.580 1.00 22.10 ? 283 TYR A CE2 1 ATOM 2218 C CZ . TYR A 1 283 ? 16.560 -5.898 41.644 1.00 25.06 ? 283 TYR A CZ 1 ATOM 2219 O OH . TYR A 1 283 ? 16.845 -6.094 40.308 1.00 28.05 ? 283 TYR A OH 1 ATOM 2220 N N . VAL A 1 284 ? 16.688 -2.358 44.710 1.00 29.20 ? 284 VAL A N 1 ATOM 2221 C CA . VAL A 1 284 ? 17.768 -1.589 44.098 1.00 28.89 ? 284 VAL A CA 1 ATOM 2222 C C . VAL A 1 284 ? 18.151 -0.419 45.007 1.00 29.19 ? 284 VAL A C 1 ATOM 2223 O O . VAL A 1 284 ? 19.335 -0.198 45.267 1.00 28.28 ? 284 VAL A O 1 ATOM 2224 C CB . VAL A 1 284 ? 17.375 -1.057 42.694 1.00 29.24 ? 284 VAL A CB 1 ATOM 2225 C CG1 . VAL A 1 284 ? 18.421 -0.063 42.201 1.00 26.38 ? 284 VAL A CG1 1 ATOM 2226 C CG2 . VAL A 1 284 ? 17.254 -2.231 41.702 1.00 27.00 ? 284 VAL A CG2 1 ATOM 2227 N N . LYS A 1 285 ? 17.158 0.319 45.502 1.00 29.56 ? 285 LYS A N 1 ATOM 2228 C CA . LYS A 1 285 ? 17.445 1.444 46.388 1.00 31.50 ? 285 LYS A CA 1 ATOM 2229 C C . LYS A 1 285 ? 18.245 0.976 47.595 1.00 32.33 ? 285 LYS A C 1 ATOM 2230 O O . LYS A 1 285 ? 19.233 1.599 47.980 1.00 33.00 ? 285 LYS A O 1 ATOM 2231 C CB . LYS A 1 285 ? 16.157 2.121 46.860 1.00 31.31 ? 285 LYS A CB 1 ATOM 2232 C CG . LYS A 1 285 ? 15.500 3.001 45.809 1.00 33.05 ? 285 LYS A CG 1 ATOM 2233 C CD . LYS A 1 285 ? 14.392 3.855 46.404 1.00 33.34 ? 285 LYS A CD 1 ATOM 2234 C CE . LYS A 1 285 ? 13.248 3.015 46.945 1.00 35.10 ? 285 LYS A CE 1 ATOM 2235 N NZ . LYS A 1 285 ? 12.254 3.848 47.684 1.00 38.17 ? 285 LYS A NZ 1 ATOM 2236 N N . GLU A 1 286 ? 17.821 -0.135 48.184 1.00 33.48 ? 286 GLU A N 1 ATOM 2237 C CA . GLU A 1 286 ? 18.509 -0.688 49.343 1.00 34.65 ? 286 GLU A CA 1 ATOM 2238 C C . GLU A 1 286 ? 19.943 -1.117 49.012 1.00 34.07 ? 286 GLU A C 1 ATOM 2239 O O . GLU A 1 286 ? 20.893 -0.705 49.674 1.00 33.70 ? 286 GLU A O 1 ATOM 2240 C CB . GLU A 1 286 ? 17.738 -1.893 49.889 1.00 35.20 ? 286 GLU A CB 1 ATOM 2241 C CG . GLU A 1 286 ? 18.325 -2.455 51.162 1.00 36.84 ? 286 GLU A CG 1 ATOM 2242 C CD . GLU A 1 286 ? 18.162 -1.505 52.331 1.00 41.66 ? 286 GLU A CD 1 ATOM 2243 O OE1 . GLU A 1 286 ? 18.845 -1.711 53.361 1.00 43.46 ? 286 GLU A OE1 1 ATOM 2244 O OE2 . GLU A 1 286 ? 17.341 -0.559 52.221 1.00 41.89 ? 286 GLU A OE2 1 ATOM 2245 N N . ALA A 1 287 ? 20.091 -1.950 47.990 1.00 32.63 ? 287 ALA A N 1 ATOM 2246 C CA . ALA A 1 287 ? 21.400 -2.440 47.594 1.00 32.52 ? 287 ALA A CA 1 ATOM 2247 C C . ALA A 1 287 ? 22.366 -1.300 47.322 1.00 33.49 ? 287 ALA A C 1 ATOM 2248 O O . ALA A 1 287 ? 23.573 -1.432 47.503 1.00 34.51 ? 287 ALA A O 1 ATOM 2249 C CB . ALA A 1 287 ? 21.273 -3.311 46.349 1.00 32.53 ? 287 ALA A CB 1 ATOM 2250 N N . VAL A 1 288 ? 21.828 -0.171 46.893 1.00 33.45 ? 288 VAL A N 1 ATOM 2251 C CA . VAL A 1 288 ? 22.663 0.965 46.560 1.00 32.66 ? 288 VAL A CA 1 ATOM 2252 C C . VAL A 1 288 ? 22.905 1.909 47.736 1.00 33.13 ? 288 VAL A C 1 ATOM 2253 O O . VAL A 1 288 ? 23.794 2.760 47.680 1.00 33.40 ? 288 VAL A O 1 ATOM 2254 C CB . VAL A 1 288 ? 22.049 1.721 45.350 1.00 31.76 ? 288 VAL A CB 1 ATOM 2255 C CG1 . VAL A 1 288 ? 21.523 3.089 45.761 1.00 28.05 ? 288 VAL A CG1 1 ATOM 2256 C CG2 . VAL A 1 288 ? 23.079 1.823 44.252 1.00 32.81 ? 288 VAL A CG2 1 ATOM 2257 N N . GLY A 1 289 ? 22.115 1.755 48.795 1.00 31.90 ? 289 GLY A N 1 ATOM 2258 C CA . GLY A 1 289 ? 22.270 2.599 49.967 1.00 32.22 ? 289 GLY A CA 1 ATOM 2259 C C . GLY A 1 289 ? 21.665 3.981 49.820 1.00 33.53 ? 289 GLY A C 1 ATOM 2260 O O . GLY A 1 289 ? 22.097 4.937 50.463 1.00 33.71 ? 289 GLY A O 1 ATOM 2261 N N . ALA A 1 290 ? 20.649 4.094 48.979 1.00 34.66 ? 290 ALA A N 1 ATOM 2262 C CA . ALA A 1 290 ? 20.016 5.383 48.751 1.00 36.31 ? 290 ALA A CA 1 ATOM 2263 C C . ALA A 1 290 ? 19.397 5.903 50.037 1.00 37.26 ? 290 ALA A C 1 ATOM 2264 O O . ALA A 1 290 ? 18.780 5.151 50.782 1.00 38.02 ? 290 ALA A O 1 ATOM 2265 C CB . ALA A 1 290 ? 18.951 5.261 47.657 1.00 33.77 ? 290 ALA A CB 1 ATOM 2266 N N . GLU A 1 291 ? 19.579 7.192 50.302 1.00 39.06 ? 291 GLU A N 1 ATOM 2267 C CA . GLU A 1 291 ? 19.012 7.804 51.494 1.00 40.41 ? 291 GLU A CA 1 ATOM 2268 C C . GLU A 1 291 ? 17.895 8.750 51.088 1.00 41.28 ? 291 GLU A C 1 ATOM 2269 O O . GLU A 1 291 ? 17.423 9.552 51.886 1.00 42.08 ? 291 GLU A O 1 ATOM 2270 C CB . GLU A 1 291 ? 20.090 8.546 52.288 1.00 40.11 ? 291 GLU A CB 1 ATOM 2271 C CG . GLU A 1 291 ? 20.990 7.615 53.085 1.00 41.36 ? 291 GLU A CG 1 ATOM 2272 C CD . GLU A 1 291 ? 22.230 8.297 53.636 1.00 43.33 ? 291 GLU A CD 1 ATOM 2273 O OE1 . GLU A 1 291 ? 23.042 7.606 54.287 1.00 44.57 ? 291 GLU A OE1 1 ATOM 2274 O OE2 . GLU A 1 291 ? 22.404 9.516 53.422 1.00 45.51 ? 291 GLU A OE2 1 ATOM 2275 N N . VAL A 1 292 ? 17.479 8.642 49.833 1.00 41.85 ? 292 VAL A N 1 ATOM 2276 C CA . VAL A 1 292 ? 16.398 9.461 49.306 1.00 42.70 ? 292 VAL A CA 1 ATOM 2277 C C . VAL A 1 292 ? 15.273 8.508 48.927 1.00 43.84 ? 292 VAL A C 1 ATOM 2278 O O . VAL A 1 292 ? 15.515 7.448 48.366 1.00 45.51 ? 292 VAL A O 1 ATOM 2279 C CB . VAL A 1 292 ? 16.860 10.275 48.075 1.00 41.29 ? 292 VAL A CB 1 ATOM 2280 C CG1 . VAL A 1 292 ? 15.669 10.832 47.341 1.00 40.76 ? 292 VAL A CG1 1 ATOM 2281 C CG2 . VAL A 1 292 ? 17.756 11.416 48.525 1.00 38.80 ? 292 VAL A CG2 1 ATOM 2282 N N . ASP A 1 293 ? 14.045 8.890 49.239 1.00 44.88 ? 293 ASP A N 1 ATOM 2283 C CA . ASP A 1 293 ? 12.880 8.058 48.975 1.00 46.95 ? 293 ASP A CA 1 ATOM 2284 C C . ASP A 1 293 ? 12.510 7.801 47.504 1.00 45.35 ? 293 ASP A C 1 ATOM 2285 O O . ASP A 1 293 ? 12.292 6.657 47.109 1.00 45.16 ? 293 ASP A O 1 ATOM 2286 C CB . ASP A 1 293 ? 11.674 8.658 49.703 1.00 53.07 ? 293 ASP A CB 1 ATOM 2287 C CG . ASP A 1 293 ? 10.424 7.813 49.558 1.00 59.54 ? 293 ASP A CG 1 ATOM 2288 O OD1 . ASP A 1 293 ? 9.315 8.348 49.803 1.00 62.02 ? 293 ASP A OD1 1 ATOM 2289 O OD2 . ASP A 1 293 ? 10.552 6.614 49.208 1.00 63.13 ? 293 ASP A OD2 1 ATOM 2290 N N . HIS A 1 294 ? 12.426 8.858 46.702 1.00 43.37 ? 294 HIS A N 1 ATOM 2291 C CA . HIS A 1 294 ? 12.045 8.730 45.297 1.00 41.05 ? 294 HIS A CA 1 ATOM 2292 C C . HIS A 1 294 ? 13.132 9.243 44.359 1.00 39.73 ? 294 HIS A C 1 ATOM 2293 O O . HIS A 1 294 ? 13.678 10.328 44.558 1.00 41.46 ? 294 HIS A O 1 ATOM 2294 C CB . HIS A 1 294 ? 10.734 9.501 45.050 1.00 41.62 ? 294 HIS A CB 1 ATOM 2295 C CG . HIS A 1 294 ? 10.178 9.346 43.665 1.00 44.74 ? 294 HIS A CG 1 ATOM 2296 N ND1 . HIS A 1 294 ? 10.178 10.372 42.741 1.00 46.23 ? 294 HIS A ND1 1 ATOM 2297 C CD2 . HIS A 1 294 ? 9.593 8.290 43.050 1.00 45.15 ? 294 HIS A CD2 1 ATOM 2298 C CE1 . HIS A 1 294 ? 9.616 9.954 41.619 1.00 45.17 ? 294 HIS A CE1 1 ATOM 2299 N NE2 . HIS A 1 294 ? 9.253 8.694 41.780 1.00 45.82 ? 294 HIS A NE2 1 ATOM 2300 N N . TYR A 1 295 ? 13.441 8.468 43.328 1.00 36.16 ? 295 TYR A N 1 ATOM 2301 C CA . TYR A 1 295 ? 14.458 8.879 42.379 1.00 34.12 ? 295 TYR A CA 1 ATOM 2302 C C . TYR A 1 295 ? 13.847 9.463 41.107 1.00 34.56 ? 295 TYR A C 1 ATOM 2303 O O . TYR A 1 295 ? 12.796 9.013 40.652 1.00 34.76 ? 295 TYR A O 1 ATOM 2304 C CB . TYR A 1 295 ? 15.363 7.695 42.029 1.00 31.75 ? 295 TYR A CB 1 ATOM 2305 C CG . TYR A 1 295 ? 16.320 7.998 40.902 1.00 30.10 ? 295 TYR A CG 1 ATOM 2306 C CD1 . TYR A 1 295 ? 15.933 7.844 39.571 1.00 28.03 ? 295 TYR A CD1 1 ATOM 2307 C CD2 . TYR A 1 295 ? 17.593 8.505 41.164 1.00 28.54 ? 295 TYR A CD2 1 ATOM 2308 C CE1 . TYR A 1 295 ? 16.784 8.193 38.531 1.00 27.96 ? 295 TYR A CE1 1 ATOM 2309 C CE2 . TYR A 1 295 ? 18.448 8.854 40.134 1.00 28.71 ? 295 TYR A CE2 1 ATOM 2310 C CZ . TYR A 1 295 ? 18.038 8.700 38.822 1.00 28.24 ? 295 TYR A CZ 1 ATOM 2311 O OH . TYR A 1 295 ? 18.879 9.070 37.806 1.00 28.36 ? 295 TYR A OH 1 ATOM 2312 N N . GLU A 1 296 ? 14.514 10.469 40.545 1.00 34.39 ? 296 GLU A N 1 ATOM 2313 C CA . GLU A 1 296 ? 14.072 11.132 39.316 1.00 34.89 ? 296 GLU A CA 1 ATOM 2314 C C . GLU A 1 296 ? 15.270 11.462 38.446 1.00 33.76 ? 296 GLU A C 1 ATOM 2315 O O . GLU A 1 296 ? 16.308 11.877 38.959 1.00 34.72 ? 296 GLU A O 1 ATOM 2316 C CB . GLU A 1 296 ? 13.349 12.440 39.624 1.00 36.14 ? 296 GLU A CB 1 ATOM 2317 C CG . GLU A 1 296 ? 11.926 12.283 40.066 1.00 43.07 ? 296 GLU A CG 1 ATOM 2318 C CD . GLU A 1 296 ? 11.288 13.610 40.415 1.00 47.65 ? 296 GLU A CD 1 ATOM 2319 O OE1 . GLU A 1 296 ? 10.075 13.612 40.733 1.00 50.40 ? 296 GLU A OE1 1 ATOM 2320 O OE2 . GLU A 1 296 ? 11.997 14.647 40.376 1.00 48.23 ? 296 GLU A OE2 1 ATOM 2321 N N . SER A 1 297 ? 15.119 11.296 37.136 1.00 30.86 ? 297 SER A N 1 ATOM 2322 C CA . SER A 1 297 ? 16.189 11.599 36.197 1.00 28.66 ? 297 SER A CA 1 ATOM 2323 C C . SER A 1 297 ? 16.674 13.032 36.352 1.00 27.73 ? 297 SER A C 1 ATOM 2324 O O . SER A 1 297 ? 17.871 13.274 36.476 1.00 28.35 ? 297 SER A O 1 ATOM 2325 C CB . SER A 1 297 ? 15.717 11.371 34.771 1.00 27.80 ? 297 SER A CB 1 ATOM 2326 O OG . SER A 1 297 ? 15.548 9.989 34.551 1.00 30.09 ? 297 SER A OG 1 ATOM 2327 N N . CYS A 1 298 ? 15.754 13.986 36.332 1.00 25.43 ? 298 CYS A N 1 ATOM 2328 C CA . CYS A 1 298 ? 16.151 15.375 36.511 1.00 25.39 ? 298 CYS A CA 1 ATOM 2329 C C . CYS A 1 298 ? 15.328 16.026 37.609 1.00 25.73 ? 298 CYS A C 1 ATOM 2330 O O . CYS A 1 298 ? 14.214 15.608 37.907 1.00 25.70 ? 298 CYS A O 1 ATOM 2331 C CB . CYS A 1 298 ? 15.951 16.185 35.234 1.00 24.02 ? 298 CYS A CB 1 ATOM 2332 S SG . CYS A 1 298 ? 16.726 15.524 33.735 1.00 24.33 ? 298 CYS A SG 1 ATOM 2333 N N . ASN A 1 299 ? 15.902 17.049 38.221 1.00 25.73 ? 299 ASN A N 1 ATOM 2334 C CA . ASN A 1 299 ? 15.215 17.799 39.248 1.00 25.97 ? 299 ASN A CA 1 ATOM 2335 C C . ASN A 1 299 ? 14.959 19.147 38.574 1.00 25.61 ? 299 ASN A C 1 ATOM 2336 O O . ASN A 1 299 ? 15.890 19.925 38.351 1.00 24.65 ? 299 ASN A O 1 ATOM 2337 C CB . ASN A 1 299 ? 16.115 17.976 40.457 1.00 27.24 ? 299 ASN A CB 1 ATOM 2338 C CG . ASN A 1 299 ? 15.430 18.711 41.569 1.00 29.13 ? 299 ASN A CG 1 ATOM 2339 O OD1 . ASN A 1 299 ? 14.652 19.631 41.323 1.00 29.17 ? 299 ASN A OD1 1 ATOM 2340 N ND2 . ASN A 1 299 ? 15.717 18.323 42.804 1.00 29.51 ? 299 ASN A ND2 1 ATOM 2341 N N . PHE A 1 300 ? 13.704 19.418 38.234 1.00 25.10 ? 300 PHE A N 1 ATOM 2342 C CA . PHE A 1 300 ? 13.376 20.654 37.545 1.00 24.97 ? 300 PHE A CA 1 ATOM 2343 C C . PHE A 1 300 ? 13.318 21.899 38.400 1.00 25.42 ? 300 PHE A C 1 ATOM 2344 O O . PHE A 1 300 ? 13.214 23.009 37.882 1.00 26.44 ? 300 PHE A O 1 ATOM 2345 C CB . PHE A 1 300 ? 12.105 20.460 36.726 1.00 23.99 ? 300 PHE A CB 1 ATOM 2346 C CG . PHE A 1 300 ? 12.294 19.502 35.590 1.00 25.92 ? 300 PHE A CG 1 ATOM 2347 C CD1 . PHE A 1 300 ? 13.227 19.776 34.593 1.00 24.77 ? 300 PHE A CD1 1 ATOM 2348 C CD2 . PHE A 1 300 ? 11.625 18.283 35.564 1.00 28.36 ? 300 PHE A CD2 1 ATOM 2349 C CE1 . PHE A 1 300 ? 13.499 18.845 33.589 1.00 26.64 ? 300 PHE A CE1 1 ATOM 2350 C CE2 . PHE A 1 300 ? 11.889 17.342 34.561 1.00 28.74 ? 300 PHE A CE2 1 ATOM 2351 C CZ . PHE A 1 300 ? 12.829 17.624 33.574 1.00 27.11 ? 300 PHE A CZ 1 ATOM 2352 N N . ASP A 1 301 ? 13.402 21.723 39.711 1.00 25.88 ? 301 ASP A N 1 ATOM 2353 C CA . ASP A 1 301 ? 13.434 22.871 40.587 1.00 25.54 ? 301 ASP A CA 1 ATOM 2354 C C . ASP A 1 301 ? 14.832 23.481 40.470 1.00 27.33 ? 301 ASP A C 1 ATOM 2355 O O . ASP A 1 301 ? 14.958 24.685 40.225 1.00 27.20 ? 301 ASP A O 1 ATOM 2356 C CB . ASP A 1 301 ? 13.172 22.479 42.037 1.00 25.06 ? 301 ASP A CB 1 ATOM 2357 C CG . ASP A 1 301 ? 11.707 22.438 42.375 1.00 26.35 ? 301 ASP A CG 1 ATOM 2358 O OD1 . ASP A 1 301 ? 10.980 23.376 41.987 1.00 26.91 ? 301 ASP A OD1 1 ATOM 2359 O OD2 . ASP A 1 301 ? 11.277 21.476 43.046 1.00 30.09 ? 301 ASP A OD2 1 ATOM 2360 N N . ILE A 1 302 ? 15.884 22.664 40.618 1.00 27.09 ? 302 ILE A N 1 ATOM 2361 C CA . ILE A 1 302 ? 17.232 23.224 40.527 1.00 28.77 ? 302 ILE A CA 1 ATOM 2362 C C . ILE A 1 302 ? 17.483 23.697 39.099 1.00 28.93 ? 302 ILE A C 1 ATOM 2363 O O . ILE A 1 302 ? 18.316 24.577 38.864 1.00 29.37 ? 302 ILE A O 1 ATOM 2364 C CB . ILE A 1 302 ? 18.367 22.233 41.005 1.00 28.69 ? 302 ILE A CB 1 ATOM 2365 C CG1 . ILE A 1 302 ? 19.040 21.578 39.813 1.00 30.87 ? 302 ILE A CG1 1 ATOM 2366 C CG2 . ILE A 1 302 ? 17.829 21.199 41.978 1.00 27.59 ? 302 ILE A CG2 1 ATOM 2367 C CD1 . ILE A 1 302 ? 20.288 22.308 39.370 1.00 31.29 ? 302 ILE A CD1 1 ATOM 2368 N N . ASN A 1 303 ? 16.746 23.126 38.149 1.00 28.81 ? 303 ASN A N 1 ATOM 2369 C CA . ASN A 1 303 ? 16.861 23.534 36.753 1.00 29.45 ? 303 ASN A CA 1 ATOM 2370 C C . ASN A 1 303 ? 16.344 24.983 36.669 1.00 29.97 ? 303 ASN A C 1 ATOM 2371 O O . ASN A 1 303 ? 16.978 25.859 36.063 1.00 28.58 ? 303 ASN A O 1 ATOM 2372 C CB . ASN A 1 303 ? 16.026 22.602 35.857 1.00 30.05 ? 303 ASN A CB 1 ATOM 2373 C CG . ASN A 1 303 ? 16.041 23.018 34.387 1.00 31.93 ? 303 ASN A CG 1 ATOM 2374 O OD1 . ASN A 1 303 ? 15.231 23.837 33.955 1.00 32.72 ? 303 ASN A OD1 1 ATOM 2375 N ND2 . ASN A 1 303 ? 16.974 22.462 33.618 1.00 30.74 ? 303 ASN A ND2 1 ATOM 2376 N N . ARG A 1 304 ? 15.197 25.232 37.298 1.00 29.26 ? 304 ARG A N 1 ATOM 2377 C CA . ARG A 1 304 ? 14.616 26.570 37.310 1.00 28.76 ? 304 ARG A CA 1 ATOM 2378 C C . ARG A 1 304 ? 15.456 27.496 38.181 1.00 28.98 ? 304 ARG A C 1 ATOM 2379 O O . ARG A 1 304 ? 15.536 28.700 37.924 1.00 28.98 ? 304 ARG A O 1 ATOM 2380 C CB . ARG A 1 304 ? 13.189 26.546 37.857 1.00 28.62 ? 304 ARG A CB 1 ATOM 2381 C CG . ARG A 1 304 ? 12.238 25.682 37.084 1.00 28.34 ? 304 ARG A CG 1 ATOM 2382 C CD . ARG A 1 304 ? 10.849 25.777 37.666 1.00 28.53 ? 304 ARG A CD 1 ATOM 2383 N NE . ARG A 1 304 ? 10.092 24.551 37.441 1.00 29.53 ? 304 ARG A NE 1 ATOM 2384 C CZ . ARG A 1 304 ? 10.039 23.548 38.304 1.00 28.38 ? 304 ARG A CZ 1 ATOM 2385 N NH1 . ARG A 1 304 ? 10.697 23.632 39.445 1.00 29.80 ? 304 ARG A NH1 1 ATOM 2386 N NH2 . ARG A 1 304 ? 9.327 22.467 38.030 1.00 32.22 ? 304 ARG A NH2 1 ATOM 2387 N N . ASN A 1 305 ? 16.070 26.944 39.223 1.00 27.68 ? 305 ASN A N 1 ATOM 2388 C CA . ASN A 1 305 ? 16.898 27.765 40.086 1.00 27.00 ? 305 ASN A CA 1 ATOM 2389 C C . ASN A 1 305 ? 18.000 28.390 39.245 1.00 26.51 ? 305 ASN A C 1 ATOM 2390 O O . ASN A 1 305 ? 18.216 29.595 39.299 1.00 27.34 ? 305 ASN A O 1 ATOM 2391 C CB . ASN A 1 305 ? 17.504 26.936 41.220 1.00 27.98 ? 305 ASN A CB 1 ATOM 2392 C CG . ASN A 1 305 ? 16.454 26.392 42.161 1.00 29.46 ? 305 ASN A CG 1 ATOM 2393 O OD1 . ASN A 1 305 ? 16.734 25.240 42.764 1.00 29.60 ? 305 ASN A OD1 1 ATOM 2394 N ND2 . ASN A 1 305 ? 15.405 27.008 42.355 1.00 30.65 ? 305 ASN A ND2 1 ATOM 2395 N N . PHE A 1 306 ? 18.689 27.574 38.455 1.00 24.78 ? 306 PHE A N 1 ATOM 2396 C CA . PHE A 1 306 ? 19.754 28.098 37.619 1.00 23.57 ? 306 PHE A CA 1 ATOM 2397 C C . PHE A 1 306 ? 19.213 29.115 36.622 1.00 25.28 ? 306 PHE A C 1 ATOM 2398 O O . PHE A 1 306 ? 19.807 30.174 36.428 1.00 25.36 ? 306 PHE A O 1 ATOM 2399 C CB . PHE A 1 306 ? 20.455 26.966 36.865 1.00 23.31 ? 306 PHE A CB 1 ATOM 2400 C CG . PHE A 1 306 ? 21.576 26.318 37.633 1.00 19.25 ? 306 PHE A CG 1 ATOM 2401 C CD1 . PHE A 1 306 ? 21.321 25.601 38.797 1.00 17.82 ? 306 PHE A CD1 1 ATOM 2402 C CD2 . PHE A 1 306 ? 22.886 26.407 37.172 1.00 16.26 ? 306 PHE A CD2 1 ATOM 2403 C CE1 . PHE A 1 306 ? 22.353 24.976 39.493 1.00 18.12 ? 306 PHE A CE1 1 ATOM 2404 C CE2 . PHE A 1 306 ? 23.922 25.794 37.851 1.00 17.77 ? 306 PHE A CE2 1 ATOM 2405 C CZ . PHE A 1 306 ? 23.657 25.070 39.023 1.00 18.48 ? 306 PHE A CZ 1 ATOM 2406 N N . LEU A 1 307 ? 18.087 28.792 35.990 1.00 26.08 ? 307 LEU A N 1 ATOM 2407 C CA . LEU A 1 307 ? 17.483 29.681 35.003 1.00 26.77 ? 307 LEU A CA 1 ATOM 2408 C C . LEU A 1 307 ? 17.144 31.057 35.540 1.00 27.20 ? 307 LEU A C 1 ATOM 2409 O O . LEU A 1 307 ? 17.550 32.072 34.975 1.00 26.95 ? 307 LEU A O 1 ATOM 2410 C CB . LEU A 1 307 ? 16.214 29.062 34.433 1.00 28.81 ? 307 LEU A CB 1 ATOM 2411 C CG . LEU A 1 307 ? 16.365 28.155 33.218 1.00 31.46 ? 307 LEU A CG 1 ATOM 2412 C CD1 . LEU A 1 307 ? 15.023 27.514 32.897 1.00 32.88 ? 307 LEU A CD1 1 ATOM 2413 C CD2 . LEU A 1 307 ? 16.861 28.978 32.041 1.00 33.26 ? 307 LEU A CD2 1 ATOM 2414 N N . PHE A 1 308 ? 16.387 31.092 36.628 1.00 28.83 ? 308 PHE A N 1 ATOM 2415 C CA . PHE A 1 308 ? 15.972 32.359 37.220 1.00 29.31 ? 308 PHE A CA 1 ATOM 2416 C C . PHE A 1 308 ? 17.081 33.061 37.988 1.00 28.22 ? 308 PHE A C 1 ATOM 2417 O O . PHE A 1 308 ? 16.853 34.098 38.594 1.00 31.69 ? 308 PHE A O 1 ATOM 2418 C CB . PHE A 1 308 ? 14.752 32.141 38.117 1.00 27.69 ? 308 PHE A CB 1 ATOM 2419 C CG . PHE A 1 308 ? 13.484 31.855 37.352 1.00 27.32 ? 308 PHE A CG 1 ATOM 2420 C CD1 . PHE A 1 308 ? 12.509 32.839 37.197 1.00 26.83 ? 308 PHE A CD1 1 ATOM 2421 C CD2 . PHE A 1 308 ? 13.264 30.605 36.785 1.00 25.96 ? 308 PHE A CD2 1 ATOM 2422 C CE1 . PHE A 1 308 ? 11.332 32.580 36.491 1.00 24.55 ? 308 PHE A CE1 1 ATOM 2423 C CE2 . PHE A 1 308 ? 12.085 30.337 36.076 1.00 26.06 ? 308 PHE A CE2 1 ATOM 2424 C CZ . PHE A 1 308 ? 11.118 31.331 35.932 1.00 24.45 ? 308 PHE A CZ 1 ATOM 2425 N N . ALA A 1 309 ? 18.281 32.497 37.953 1.00 26.00 ? 309 ALA A N 1 ATOM 2426 C CA . ALA A 1 309 ? 19.424 33.100 38.621 1.00 25.59 ? 309 ALA A CA 1 ATOM 2427 C C . ALA A 1 309 ? 20.346 33.686 37.548 1.00 27.52 ? 309 ALA A C 1 ATOM 2428 O O . ALA A 1 309 ? 21.361 34.309 37.866 1.00 28.64 ? 309 ALA A O 1 ATOM 2429 C CB . ALA A 1 309 ? 20.167 32.061 39.447 1.00 24.08 ? 309 ALA A CB 1 ATOM 2430 N N . GLY A 1 310 ? 19.985 33.471 36.282 1.00 26.56 ? 310 GLY A N 1 ATOM 2431 C CA . GLY A 1 310 ? 20.757 33.994 35.166 1.00 27.94 ? 310 GLY A CA 1 ATOM 2432 C C . GLY A 1 310 ? 22.028 33.250 34.775 1.00 29.00 ? 310 GLY A C 1 ATOM 2433 O O . GLY A 1 310 ? 22.870 33.788 34.058 1.00 30.11 ? 310 GLY A O 1 ATOM 2434 N N . ASP A 1 311 ? 22.165 32.007 35.216 1.00 28.28 ? 311 ASP A N 1 ATOM 2435 C CA . ASP A 1 311 ? 23.360 31.223 34.921 1.00 27.74 ? 311 ASP A CA 1 ATOM 2436 C C . ASP A 1 311 ? 23.487 30.780 33.467 1.00 26.69 ? 311 ASP A C 1 ATOM 2437 O O . ASP A 1 311 ? 24.590 30.581 32.957 1.00 26.77 ? 311 ASP A O 1 ATOM 2438 C CB . ASP A 1 311 ? 23.393 29.978 35.814 1.00 26.66 ? 311 ASP A CB 1 ATOM 2439 C CG . ASP A 1 311 ? 24.745 29.306 35.816 1.00 26.19 ? 311 ASP A CG 1 ATOM 2440 O OD1 . ASP A 1 311 ? 25.671 29.865 36.437 1.00 28.54 ? 311 ASP A OD1 1 ATOM 2441 O OD2 . ASP A 1 311 ? 24.888 28.234 35.194 1.00 24.62 ? 311 ASP A OD2 1 ATOM 2442 N N . TRP A 1 312 ? 22.351 30.618 32.807 1.00 25.98 ? 312 TRP A N 1 ATOM 2443 C CA . TRP A 1 312 ? 22.323 30.151 31.429 1.00 25.49 ? 312 TRP A CA 1 ATOM 2444 C C . TRP A 1 312 ? 23.175 30.964 30.445 1.00 26.58 ? 312 TRP A C 1 ATOM 2445 O O . TRP A 1 312 ? 23.918 30.387 29.652 1.00 26.45 ? 312 TRP A O 1 ATOM 2446 C CB . TRP A 1 312 ? 20.861 30.083 30.971 1.00 23.21 ? 312 TRP A CB 1 ATOM 2447 C CG . TRP A 1 312 ? 20.622 29.452 29.639 1.00 22.50 ? 312 TRP A CG 1 ATOM 2448 C CD1 . TRP A 1 312 ? 20.800 30.029 28.414 1.00 22.99 ? 312 TRP A CD1 1 ATOM 2449 C CD2 . TRP A 1 312 ? 20.107 28.136 29.393 1.00 21.30 ? 312 TRP A CD2 1 ATOM 2450 N NE1 . TRP A 1 312 ? 20.418 29.156 27.420 1.00 23.75 ? 312 TRP A NE1 1 ATOM 2451 C CE2 . TRP A 1 312 ? 19.991 27.987 27.993 1.00 21.09 ? 312 TRP A CE2 1 ATOM 2452 C CE3 . TRP A 1 312 ? 19.731 27.068 30.222 1.00 22.15 ? 312 TRP A CE3 1 ATOM 2453 C CZ2 . TRP A 1 312 ? 19.516 26.815 27.398 1.00 21.67 ? 312 TRP A CZ2 1 ATOM 2454 C CZ3 . TRP A 1 312 ? 19.257 25.897 29.631 1.00 23.50 ? 312 TRP A CZ3 1 ATOM 2455 C CH2 . TRP A 1 312 ? 19.155 25.782 28.229 1.00 23.86 ? 312 TRP A CH2 1 ATOM 2456 N N . MET A 1 313 ? 23.103 32.291 30.511 1.00 26.36 ? 313 MET A N 1 ATOM 2457 C CA . MET A 1 313 ? 23.857 33.129 29.576 1.00 27.75 ? 313 MET A CA 1 ATOM 2458 C C . MET A 1 313 ? 25.210 33.686 30.029 1.00 28.87 ? 313 MET A C 1 ATOM 2459 O O . MET A 1 313 ? 25.755 34.567 29.359 1.00 27.83 ? 313 MET A O 1 ATOM 2460 C CB . MET A 1 313 ? 22.984 34.300 29.110 1.00 28.12 ? 313 MET A CB 1 ATOM 2461 C CG . MET A 1 313 ? 21.727 33.890 28.361 1.00 28.62 ? 313 MET A CG 1 ATOM 2462 S SD . MET A 1 313 ? 22.112 33.043 26.826 1.00 33.39 ? 313 MET A SD 1 ATOM 2463 C CE . MET A 1 313 ? 20.487 32.924 26.067 1.00 30.91 ? 313 MET A CE 1 ATOM 2464 N N . LYS A 1 314 ? 25.761 33.194 31.139 1.00 29.44 ? 314 LYS A N 1 ATOM 2465 C CA . LYS A 1 314 ? 27.052 33.705 31.612 1.00 29.91 ? 314 LYS A CA 1 ATOM 2466 C C . LYS A 1 314 ? 28.187 33.332 30.659 1.00 29.84 ? 314 LYS A C 1 ATOM 2467 O O . LYS A 1 314 ? 28.120 32.319 29.965 1.00 29.69 ? 314 LYS A O 1 ATOM 2468 C CB . LYS A 1 314 ? 27.380 33.172 33.011 1.00 32.66 ? 314 LYS A CB 1 ATOM 2469 C CG . LYS A 1 314 ? 26.376 33.523 34.105 1.00 32.56 ? 314 LYS A CG 1 ATOM 2470 C CD . LYS A 1 314 ? 26.240 35.013 34.305 1.00 34.27 ? 314 LYS A CD 1 ATOM 2471 C CE . LYS A 1 314 ? 25.367 35.323 35.518 1.00 36.29 ? 314 LYS A CE 1 ATOM 2472 N NZ . LYS A 1 314 ? 25.977 34.827 36.785 1.00 37.64 ? 314 LYS A NZ 1 ATOM 2473 N N . PRO A 1 315 ? 29.250 34.155 30.618 1.00 30.15 ? 315 PRO A N 1 ATOM 2474 C CA . PRO A 1 315 ? 30.430 33.957 29.764 1.00 30.07 ? 315 PRO A CA 1 ATOM 2475 C C . PRO A 1 315 ? 31.474 33.007 30.358 1.00 30.36 ? 315 PRO A C 1 ATOM 2476 O O . PRO A 1 315 ? 32.640 33.380 30.521 1.00 31.56 ? 315 PRO A O 1 ATOM 2477 C CB . PRO A 1 315 ? 30.977 35.368 29.623 1.00 29.54 ? 315 PRO A CB 1 ATOM 2478 C CG . PRO A 1 315 ? 30.752 35.908 31.001 1.00 29.51 ? 315 PRO A CG 1 ATOM 2479 C CD . PRO A 1 315 ? 29.323 35.463 31.297 1.00 30.18 ? 315 PRO A CD 1 ATOM 2480 N N . TYR A 1 316 ? 31.059 31.785 30.668 1.00 28.39 ? 316 TYR A N 1 ATOM 2481 C CA . TYR A 1 316 ? 31.957 30.806 31.246 1.00 27.62 ? 316 TYR A CA 1 ATOM 2482 C C . TYR A 1 316 ? 33.010 30.313 30.273 1.00 28.96 ? 316 TYR A C 1 ATOM 2483 O O . TYR A 1 316 ? 33.997 29.701 30.685 1.00 30.15 ? 316 TYR A O 1 ATOM 2484 C CB . TYR A 1 316 ? 31.167 29.617 31.788 1.00 28.96 ? 316 TYR A CB 1 ATOM 2485 C CG . TYR A 1 316 ? 30.318 29.946 32.997 1.00 28.59 ? 316 TYR A CG 1 ATOM 2486 C CD1 . TYR A 1 316 ? 30.863 30.615 34.098 1.00 26.40 ? 316 TYR A CD1 1 ATOM 2487 C CD2 . TYR A 1 316 ? 28.974 29.571 33.049 1.00 25.64 ? 316 TYR A CD2 1 ATOM 2488 C CE1 . TYR A 1 316 ? 30.089 30.898 35.221 1.00 27.13 ? 316 TYR A CE1 1 ATOM 2489 C CE2 . TYR A 1 316 ? 28.192 29.849 34.161 1.00 25.52 ? 316 TYR A CE2 1 ATOM 2490 C CZ . TYR A 1 316 ? 28.751 30.510 35.244 1.00 27.42 ? 316 TYR A CZ 1 ATOM 2491 O OH . TYR A 1 316 ? 27.977 30.771 36.350 1.00 27.11 ? 316 TYR A OH 1 ATOM 2492 N N . HIS A 1 317 ? 32.815 30.577 28.985 1.00 28.79 ? 317 HIS A N 1 ATOM 2493 C CA . HIS A 1 317 ? 33.791 30.141 27.987 1.00 28.94 ? 317 HIS A CA 1 ATOM 2494 C C . HIS A 1 317 ? 35.164 30.770 28.242 1.00 28.34 ? 317 HIS A C 1 ATOM 2495 O O . HIS A 1 317 ? 36.196 30.184 27.905 1.00 29.27 ? 317 HIS A O 1 ATOM 2496 C CB . HIS A 1 317 ? 33.307 30.486 26.574 1.00 27.73 ? 317 HIS A CB 1 ATOM 2497 C CG . HIS A 1 317 ? 33.063 31.944 26.358 1.00 28.52 ? 317 HIS A CG 1 ATOM 2498 N ND1 . HIS A 1 317 ? 33.847 32.712 25.523 1.00 28.85 ? 317 HIS A ND1 1 ATOM 2499 C CD2 . HIS A 1 317 ? 32.128 32.779 26.871 1.00 27.38 ? 317 HIS A CD2 1 ATOM 2500 C CE1 . HIS A 1 317 ? 33.405 33.957 25.530 1.00 26.15 ? 317 HIS A CE1 1 ATOM 2501 N NE2 . HIS A 1 317 ? 32.363 34.025 26.339 1.00 27.95 ? 317 HIS A NE2 1 ATOM 2502 N N . THR A 1 318 ? 35.185 31.956 28.846 1.00 26.62 ? 318 THR A N 1 ATOM 2503 C CA . THR A 1 318 ? 36.459 32.603 29.123 1.00 26.26 ? 318 THR A CA 1 ATOM 2504 C C . THR A 1 318 ? 37.345 31.695 29.969 1.00 26.49 ? 318 THR A C 1 ATOM 2505 O O . THR A 1 318 ? 38.568 31.812 29.932 1.00 28.22 ? 318 THR A O 1 ATOM 2506 C CB . THR A 1 318 ? 36.283 33.943 29.861 1.00 25.08 ? 318 THR A CB 1 ATOM 2507 O OG1 . THR A 1 318 ? 35.673 33.709 31.134 1.00 26.47 ? 318 THR A OG1 1 ATOM 2508 C CG2 . THR A 1 318 ? 35.422 34.898 29.040 1.00 22.83 ? 318 THR A CG2 1 ATOM 2509 N N . ALA A 1 319 ? 36.738 30.784 30.727 1.00 25.50 ? 319 ALA A N 1 ATOM 2510 C CA . ALA A 1 319 ? 37.527 29.874 31.549 1.00 25.83 ? 319 ALA A CA 1 ATOM 2511 C C . ALA A 1 319 ? 38.302 28.915 30.658 1.00 27.20 ? 319 ALA A C 1 ATOM 2512 O O . ALA A 1 319 ? 39.377 28.447 31.027 1.00 26.59 ? 319 ALA A O 1 ATOM 2513 C CB . ALA A 1 319 ? 36.630 29.091 32.498 1.00 23.76 ? 319 ALA A CB 1 ATOM 2514 N N . VAL A 1 320 ? 37.750 28.614 29.487 1.00 27.53 ? 320 VAL A N 1 ATOM 2515 C CA . VAL A 1 320 ? 38.427 27.712 28.572 1.00 30.03 ? 320 VAL A CA 1 ATOM 2516 C C . VAL A 1 320 ? 39.751 28.326 28.132 1.00 31.82 ? 320 VAL A C 1 ATOM 2517 O O . VAL A 1 320 ? 40.759 27.624 28.027 1.00 33.69 ? 320 VAL A O 1 ATOM 2518 C CB . VAL A 1 320 ? 37.575 27.403 27.324 1.00 28.75 ? 320 VAL A CB 1 ATOM 2519 C CG1 . VAL A 1 320 ? 38.316 26.440 26.432 1.00 27.96 ? 320 VAL A CG1 1 ATOM 2520 C CG2 . VAL A 1 320 ? 36.248 26.792 27.732 1.00 29.95 ? 320 VAL A CG2 1 ATOM 2521 N N . THR A 1 321 ? 39.756 29.634 27.880 1.00 32.44 ? 321 THR A N 1 ATOM 2522 C CA . THR A 1 321 ? 40.981 30.310 27.468 1.00 34.32 ? 321 THR A CA 1 ATOM 2523 C C . THR A 1 321 ? 42.071 30.129 28.528 1.00 35.80 ? 321 THR A C 1 ATOM 2524 O O . THR A 1 321 ? 43.213 29.796 28.207 1.00 35.38 ? 321 THR A O 1 ATOM 2525 C CB . THR A 1 321 ? 40.764 31.821 27.245 1.00 34.53 ? 321 THR A CB 1 ATOM 2526 O OG1 . THR A 1 321 ? 39.810 32.027 26.194 1.00 34.54 ? 321 THR A OG1 1 ATOM 2527 C CG2 . THR A 1 321 ? 42.078 32.484 26.850 1.00 33.39 ? 321 THR A CG2 1 ATOM 2528 N N . ASP A 1 322 ? 41.719 30.353 29.791 1.00 36.46 ? 322 ASP A N 1 ATOM 2529 C CA . ASP A 1 322 ? 42.681 30.188 30.870 1.00 37.63 ? 322 ASP A CA 1 ATOM 2530 C C . ASP A 1 322 ? 43.225 28.769 30.822 1.00 37.56 ? 322 ASP A C 1 ATOM 2531 O O . ASP A 1 322 ? 44.436 28.562 30.736 1.00 39.88 ? 322 ASP A O 1 ATOM 2532 C CB . ASP A 1 322 ? 42.022 30.433 32.230 1.00 42.54 ? 322 ASP A CB 1 ATOM 2533 C CG . ASP A 1 322 ? 41.629 31.889 32.447 1.00 46.21 ? 322 ASP A CG 1 ATOM 2534 O OD1 . ASP A 1 322 ? 40.790 32.153 33.336 1.00 48.30 ? 322 ASP A OD1 1 ATOM 2535 O OD2 . ASP A 1 322 ? 42.161 32.771 31.740 1.00 49.74 ? 322 ASP A OD2 1 ATOM 2536 N N . LEU A 1 323 ? 42.329 27.790 30.863 1.00 36.34 ? 323 LEU A N 1 ATOM 2537 C CA . LEU A 1 323 ? 42.738 26.389 30.837 1.00 36.48 ? 323 LEU A CA 1 ATOM 2538 C C . LEU A 1 323 ? 43.679 26.078 29.667 1.00 36.31 ? 323 LEU A C 1 ATOM 2539 O O . LEU A 1 323 ? 44.783 25.576 29.876 1.00 36.04 ? 323 LEU A O 1 ATOM 2540 C CB . LEU A 1 323 ? 41.499 25.486 30.798 1.00 36.07 ? 323 LEU A CB 1 ATOM 2541 C CG . LEU A 1 323 ? 40.587 25.611 32.028 1.00 36.64 ? 323 LEU A CG 1 ATOM 2542 C CD1 . LEU A 1 323 ? 39.235 24.972 31.749 1.00 35.41 ? 323 LEU A CD1 1 ATOM 2543 C CD2 . LEU A 1 323 ? 41.256 24.972 33.239 1.00 34.28 ? 323 LEU A CD2 1 ATOM 2544 N N . LEU A 1 324 ? 43.253 26.379 28.443 1.00 35.65 ? 324 LEU A N 1 ATOM 2545 C CA . LEU A 1 324 ? 44.093 26.129 27.274 1.00 35.79 ? 324 LEU A CA 1 ATOM 2546 C C . LEU A 1 324 ? 45.457 26.806 27.396 1.00 36.08 ? 324 LEU A C 1 ATOM 2547 O O . LEU A 1 324 ? 46.483 26.207 27.062 1.00 36.43 ? 324 LEU A O 1 ATOM 2548 C CB . LEU A 1 324 ? 43.401 26.608 25.991 1.00 34.79 ? 324 LEU A CB 1 ATOM 2549 C CG . LEU A 1 324 ? 42.295 25.706 25.439 1.00 33.97 ? 324 LEU A CG 1 ATOM 2550 C CD1 . LEU A 1 324 ? 41.653 26.342 24.213 1.00 33.29 ? 324 LEU A CD1 1 ATOM 2551 C CD2 . LEU A 1 324 ? 42.889 24.353 25.085 1.00 33.52 ? 324 LEU A CD2 1 ATOM 2552 N N . ASN A 1 325 ? 45.477 28.050 27.867 1.00 35.58 ? 325 ASN A N 1 ATOM 2553 C CA . ASN A 1 325 ? 46.744 28.760 28.015 1.00 35.89 ? 325 ASN A CA 1 ATOM 2554 C C . ASN A 1 325 ? 47.659 28.062 29.011 1.00 37.14 ? 325 ASN A C 1 ATOM 2555 O O . ASN A 1 325 ? 48.879 28.231 28.959 1.00 37.01 ? 325 ASN A O 1 ATOM 2556 C CB . ASN A 1 325 ? 46.523 30.211 28.448 1.00 32.65 ? 325 ASN A CB 1 ATOM 2557 C CG . ASN A 1 325 ? 46.102 31.099 27.300 1.00 30.64 ? 325 ASN A CG 1 ATOM 2558 O OD1 . ASN A 1 325 ? 46.466 30.859 26.147 1.00 28.08 ? 325 ASN A OD1 1 ATOM 2559 N ND2 . ASN A 1 325 ? 45.347 32.145 27.610 1.00 29.99 ? 325 ASN A ND2 1 ATOM 2560 N N . GLN A 1 326 ? 47.069 27.277 29.910 1.00 37.66 ? 326 GLN A N 1 ATOM 2561 C CA . GLN A 1 326 ? 47.843 26.537 30.896 1.00 38.56 ? 326 GLN A CA 1 ATOM 2562 C C . GLN A 1 326 ? 48.183 25.141 30.396 1.00 38.77 ? 326 GLN A C 1 ATOM 2563 O O . GLN A 1 326 ? 48.658 24.303 31.154 1.00 39.72 ? 326 GLN A O 1 ATOM 2564 C CB . GLN A 1 326 ? 47.078 26.425 32.205 1.00 39.88 ? 326 GLN A CB 1 ATOM 2565 C CG . GLN A 1 326 ? 46.902 27.732 32.931 1.00 45.04 ? 326 GLN A CG 1 ATOM 2566 C CD . GLN A 1 326 ? 46.001 27.583 34.136 1.00 48.14 ? 326 GLN A CD 1 ATOM 2567 O OE1 . GLN A 1 326 ? 46.251 26.754 35.013 1.00 50.29 ? 326 GLN A OE1 1 ATOM 2568 N NE2 . GLN A 1 326 ? 44.941 28.382 34.186 1.00 49.13 ? 326 GLN A NE2 1 ATOM 2569 N N . ASP A 1 327 ? 47.919 24.884 29.121 1.00 39.94 ? 327 ASP A N 1 ATOM 2570 C CA . ASP A 1 327 ? 48.228 23.589 28.518 1.00 41.04 ? 327 ASP A CA 1 ATOM 2571 C C . ASP A 1 327 ? 47.372 22.401 28.969 1.00 39.27 ? 327 ASP A C 1 ATOM 2572 O O . ASP A 1 327 ? 47.824 21.252 28.918 1.00 39.24 ? 327 ASP A O 1 ATOM 2573 C CB . ASP A 1 327 ? 49.703 23.260 28.750 1.00 43.61 ? 327 ASP A CB 1 ATOM 2574 C CG . ASP A 1 327 ? 50.620 24.350 28.254 1.00 46.57 ? 327 ASP A CG 1 ATOM 2575 O OD1 . ASP A 1 327 ? 51.554 24.718 28.999 1.00 49.42 ? 327 ASP A OD1 1 ATOM 2576 O OD2 . ASP A 1 327 ? 50.407 24.835 27.121 1.00 46.91 ? 327 ASP A OD2 1 ATOM 2577 N N . LEU A 1 328 ? 46.146 22.665 29.408 1.00 36.47 ? 328 LEU A N 1 ATOM 2578 C CA . LEU A 1 328 ? 45.254 21.587 29.821 1.00 34.74 ? 328 LEU A CA 1 ATOM 2579 C C . LEU A 1 328 ? 44.557 21.074 28.560 1.00 33.41 ? 328 LEU A C 1 ATOM 2580 O O . LEU A 1 328 ? 43.844 21.820 27.895 1.00 34.16 ? 328 LEU A O 1 ATOM 2581 C CB . LEU A 1 328 ? 44.220 22.117 30.818 1.00 33.75 ? 328 LEU A CB 1 ATOM 2582 C CG . LEU A 1 328 ? 43.335 21.131 31.592 1.00 33.81 ? 328 LEU A CG 1 ATOM 2583 C CD1 . LEU A 1 328 ? 41.921 21.158 31.054 1.00 32.44 ? 328 LEU A CD1 1 ATOM 2584 C CD2 . LEU A 1 328 ? 43.934 19.735 31.531 1.00 31.93 ? 328 LEU A CD2 1 ATOM 2585 N N . PRO A 1 329 ? 44.771 19.800 28.197 1.00 31.80 ? 329 PRO A N 1 ATOM 2586 C CA . PRO A 1 329 ? 44.109 19.292 26.988 1.00 31.37 ? 329 PRO A CA 1 ATOM 2587 C C . PRO A 1 329 ? 42.577 19.336 27.114 1.00 31.05 ? 329 PRO A C 1 ATOM 2588 O O . PRO A 1 329 ? 42.012 18.986 28.155 1.00 29.83 ? 329 PRO A O 1 ATOM 2589 C CB . PRO A 1 329 ? 44.632 17.856 26.874 1.00 30.42 ? 329 PRO A CB 1 ATOM 2590 C CG . PRO A 1 329 ? 45.934 17.891 27.623 1.00 28.60 ? 329 PRO A CG 1 ATOM 2591 C CD . PRO A 1 329 ? 45.620 18.765 28.806 1.00 29.55 ? 329 PRO A CD 1 ATOM 2592 N N . ILE A 1 330 ? 41.913 19.767 26.049 1.00 29.81 ? 330 ILE A N 1 ATOM 2593 C CA . ILE A 1 330 ? 40.464 19.850 26.040 1.00 27.95 ? 330 ILE A CA 1 ATOM 2594 C C . ILE A 1 330 ? 39.897 19.283 24.747 1.00 28.65 ? 330 ILE A C 1 ATOM 2595 O O . ILE A 1 330 ? 40.360 19.616 23.648 1.00 27.82 ? 330 ILE A O 1 ATOM 2596 C CB . ILE A 1 330 ? 39.991 21.312 26.187 1.00 28.38 ? 330 ILE A CB 1 ATOM 2597 C CG1 . ILE A 1 330 ? 40.442 21.863 27.544 1.00 27.32 ? 330 ILE A CG1 1 ATOM 2598 C CG2 . ILE A 1 330 ? 38.475 21.386 26.041 1.00 26.22 ? 330 ILE A CG2 1 ATOM 2599 C CD1 . ILE A 1 330 ? 40.051 23.298 27.785 1.00 28.31 ? 330 ILE A CD1 1 ATOM 2600 N N . LEU A 1 331 ? 38.902 18.411 24.884 1.00 28.79 ? 331 LEU A N 1 ATOM 2601 C CA . LEU A 1 331 ? 38.246 17.818 23.725 1.00 27.70 ? 331 LEU A CA 1 ATOM 2602 C C . LEU A 1 331 ? 36.792 18.276 23.688 1.00 27.15 ? 331 LEU A C 1 ATOM 2603 O O . LEU A 1 331 ? 36.023 18.013 24.616 1.00 26.84 ? 331 LEU A O 1 ATOM 2604 C CB . LEU A 1 331 ? 38.297 16.289 23.780 1.00 28.26 ? 331 LEU A CB 1 ATOM 2605 C CG . LEU A 1 331 ? 37.378 15.567 22.775 1.00 30.85 ? 331 LEU A CG 1 ATOM 2606 C CD1 . LEU A 1 331 ? 37.819 15.856 21.352 1.00 30.59 ? 331 LEU A CD1 1 ATOM 2607 C CD2 . LEU A 1 331 ? 37.395 14.071 23.039 1.00 31.90 ? 331 LEU A CD2 1 ATOM 2608 N N . VAL A 1 332 ? 36.430 18.979 22.620 1.00 25.62 ? 332 VAL A N 1 ATOM 2609 C CA . VAL A 1 332 ? 35.068 19.456 22.445 1.00 23.94 ? 332 VAL A CA 1 ATOM 2610 C C . VAL A 1 332 ? 34.467 18.676 21.292 1.00 24.63 ? 332 VAL A C 1 ATOM 2611 O O . VAL A 1 332 ? 34.835 18.900 20.136 1.00 24.81 ? 332 VAL A O 1 ATOM 2612 C CB . VAL A 1 332 ? 35.045 20.954 22.109 1.00 24.46 ? 332 VAL A CB 1 ATOM 2613 C CG1 . VAL A 1 332 ? 33.599 21.411 21.828 1.00 20.77 ? 332 VAL A CG1 1 ATOM 2614 C CG2 . VAL A 1 332 ? 35.666 21.747 23.269 1.00 22.50 ? 332 VAL A CG2 1 ATOM 2615 N N . TYR A 1 333 ? 33.561 17.749 21.600 1.00 24.97 ? 333 TYR A N 1 ATOM 2616 C CA . TYR A 1 333 ? 32.924 16.934 20.562 1.00 25.81 ? 333 TYR A CA 1 ATOM 2617 C C . TYR A 1 333 ? 31.409 17.133 20.521 1.00 25.77 ? 333 TYR A C 1 ATOM 2618 O O . TYR A 1 333 ? 30.786 17.433 21.539 1.00 25.80 ? 333 TYR A O 1 ATOM 2619 C CB . TYR A 1 333 ? 33.251 15.441 20.764 1.00 25.67 ? 333 TYR A CB 1 ATOM 2620 C CG . TYR A 1 333 ? 32.663 14.810 22.018 1.00 27.31 ? 333 TYR A CG 1 ATOM 2621 C CD1 . TYR A 1 333 ? 33.284 14.957 23.257 1.00 27.95 ? 333 TYR A CD1 1 ATOM 2622 C CD2 . TYR A 1 333 ? 31.478 14.070 21.962 1.00 27.61 ? 333 TYR A CD2 1 ATOM 2623 C CE1 . TYR A 1 333 ? 32.746 14.381 24.408 1.00 27.00 ? 333 TYR A CE1 1 ATOM 2624 C CE2 . TYR A 1 333 ? 30.932 13.496 23.102 1.00 27.15 ? 333 TYR A CE2 1 ATOM 2625 C CZ . TYR A 1 333 ? 31.571 13.655 24.324 1.00 29.24 ? 333 TYR A CZ 1 ATOM 2626 O OH . TYR A 1 333 ? 31.032 13.090 25.462 1.00 30.75 ? 333 TYR A OH 1 ATOM 2627 N N . ALA A 1 334 ? 30.813 16.956 19.347 1.00 26.06 ? 334 ALA A N 1 ATOM 2628 C CA . ALA A 1 334 ? 29.371 17.131 19.206 1.00 24.78 ? 334 ALA A CA 1 ATOM 2629 C C . ALA A 1 334 ? 28.777 16.303 18.073 1.00 26.85 ? 334 ALA A C 1 ATOM 2630 O O . ALA A 1 334 ? 29.314 16.289 16.966 1.00 29.73 ? 334 ALA A O 1 ATOM 2631 C CB . ALA A 1 334 ? 29.063 18.589 18.972 1.00 22.09 ? 334 ALA A CB 1 ATOM 2632 N N . GLY A 1 335 ? 27.672 15.613 18.347 1.00 26.92 ? 335 GLY A N 1 ATOM 2633 C CA . GLY A 1 335 ? 27.017 14.838 17.308 1.00 26.23 ? 335 GLY A CA 1 ATOM 2634 C C . GLY A 1 335 ? 26.358 15.821 16.350 1.00 27.06 ? 335 GLY A C 1 ATOM 2635 O O . GLY A 1 335 ? 25.761 16.802 16.794 1.00 27.00 ? 335 GLY A O 1 ATOM 2636 N N . ASP A 1 336 ? 26.454 15.575 15.044 1.00 26.97 ? 336 ASP A N 1 ATOM 2637 C CA . ASP A 1 336 ? 25.871 16.492 14.065 1.00 27.84 ? 336 ASP A CA 1 ATOM 2638 C C . ASP A 1 336 ? 24.357 16.429 13.877 1.00 26.98 ? 336 ASP A C 1 ATOM 2639 O O . ASP A 1 336 ? 23.822 17.121 13.014 1.00 28.02 ? 336 ASP A O 1 ATOM 2640 C CB . ASP A 1 336 ? 26.544 16.330 12.691 1.00 29.87 ? 336 ASP A CB 1 ATOM 2641 C CG . ASP A 1 336 ? 26.465 14.902 12.146 1.00 32.94 ? 336 ASP A CG 1 ATOM 2642 O OD1 . ASP A 1 336 ? 25.568 14.131 12.550 1.00 34.57 ? 336 ASP A OD1 1 ATOM 2643 O OD2 . ASP A 1 336 ? 27.304 14.552 11.291 1.00 34.41 ? 336 ASP A OD2 1 ATOM 2644 N N . LYS A 1 337 ? 23.661 15.618 14.668 1.00 25.85 ? 337 LYS A N 1 ATOM 2645 C CA . LYS A 1 337 ? 22.209 15.520 14.527 1.00 25.16 ? 337 LYS A CA 1 ATOM 2646 C C . LYS A 1 337 ? 21.460 16.196 15.673 1.00 24.52 ? 337 LYS A C 1 ATOM 2647 O O . LYS A 1 337 ? 20.239 16.293 15.656 1.00 24.45 ? 337 LYS A O 1 ATOM 2648 C CB . LYS A 1 337 ? 21.782 14.053 14.412 1.00 25.64 ? 337 LYS A CB 1 ATOM 2649 C CG . LYS A 1 337 ? 22.416 13.319 13.227 1.00 25.48 ? 337 LYS A CG 1 ATOM 2650 C CD . LYS A 1 337 ? 22.173 14.048 11.905 1.00 23.71 ? 337 LYS A CD 1 ATOM 2651 C CE . LYS A 1 337 ? 23.130 13.551 10.834 1.00 21.91 ? 337 LYS A CE 1 ATOM 2652 N NZ . LYS A 1 337 ? 22.961 14.228 9.521 1.00 22.90 ? 337 LYS A NZ 1 ATOM 2653 N N . ASP A 1 338 ? 22.203 16.665 16.666 1.00 25.14 ? 338 ASP A N 1 ATOM 2654 C CA . ASP A 1 338 ? 21.615 17.350 17.807 1.00 25.42 ? 338 ASP A CA 1 ATOM 2655 C C . ASP A 1 338 ? 21.206 18.750 17.358 1.00 26.34 ? 338 ASP A C 1 ATOM 2656 O O . ASP A 1 338 ? 21.761 19.293 16.400 1.00 27.13 ? 338 ASP A O 1 ATOM 2657 C CB . ASP A 1 338 ? 22.645 17.436 18.941 1.00 25.18 ? 338 ASP A CB 1 ATOM 2658 C CG . ASP A 1 338 ? 22.108 18.133 20.179 1.00 27.38 ? 338 ASP A CG 1 ATOM 2659 O OD1 . ASP A 1 338 ? 20.909 17.967 20.499 1.00 27.48 ? 338 ASP A OD1 1 ATOM 2660 O OD2 . ASP A 1 338 ? 22.896 18.829 20.850 1.00 27.92 ? 338 ASP A OD2 1 ATOM 2661 N N . PHE A 1 339 ? 20.232 19.338 18.036 1.00 26.18 ? 339 PHE A N 1 ATOM 2662 C CA . PHE A 1 339 ? 19.807 20.677 17.674 1.00 25.12 ? 339 PHE A CA 1 ATOM 2663 C C . PHE A 1 339 ? 20.105 21.725 18.734 1.00 25.15 ? 339 PHE A C 1 ATOM 2664 O O . PHE A 1 339 ? 20.670 22.772 18.426 1.00 25.03 ? 339 PHE A O 1 ATOM 2665 C CB . PHE A 1 339 ? 18.306 20.725 17.386 1.00 25.04 ? 339 PHE A CB 1 ATOM 2666 C CG . PHE A 1 339 ? 17.750 22.129 17.361 1.00 23.75 ? 339 PHE A CG 1 ATOM 2667 C CD1 . PHE A 1 339 ? 18.065 23.000 16.318 1.00 23.95 ? 339 PHE A CD1 1 ATOM 2668 C CD2 . PHE A 1 339 ? 16.959 22.595 18.408 1.00 21.59 ? 339 PHE A CD2 1 ATOM 2669 C CE1 . PHE A 1 339 ? 17.603 24.316 16.319 1.00 26.13 ? 339 PHE A CE1 1 ATOM 2670 C CE2 . PHE A 1 339 ? 16.490 23.908 18.422 1.00 22.54 ? 339 PHE A CE2 1 ATOM 2671 C CZ . PHE A 1 339 ? 16.809 24.774 17.378 1.00 24.81 ? 339 PHE A CZ 1 ATOM 2672 N N . ILE A 1 340 ? 19.716 21.440 19.975 1.00 24.82 ? 340 ILE A N 1 ATOM 2673 C CA . ILE A 1 340 ? 19.881 22.392 21.067 1.00 24.50 ? 340 ILE A CA 1 ATOM 2674 C C . ILE A 1 340 ? 21.320 22.736 21.442 1.00 23.92 ? 340 ILE A C 1 ATOM 2675 O O . ILE A 1 340 ? 21.571 23.751 22.096 1.00 23.25 ? 340 ILE A O 1 ATOM 2676 C CB . ILE A 1 340 ? 19.106 21.927 22.315 1.00 24.27 ? 340 ILE A CB 1 ATOM 2677 C CG1 . ILE A 1 340 ? 18.866 23.127 23.237 1.00 24.81 ? 340 ILE A CG1 1 ATOM 2678 C CG2 . ILE A 1 340 ? 19.862 20.818 23.021 1.00 23.23 ? 340 ILE A CG2 1 ATOM 2679 C CD1 . ILE A 1 340 ? 17.766 22.903 24.257 1.00 24.40 ? 340 ILE A CD1 1 ATOM 2680 N N . CYS A 1 341 ? 22.256 21.895 21.023 1.00 22.21 ? 341 CYS A N 1 ATOM 2681 C CA . CYS A 1 341 ? 23.676 22.127 21.269 1.00 23.35 ? 341 CYS A CA 1 ATOM 2682 C C . CYS A 1 341 ? 24.371 21.613 20.029 1.00 24.47 ? 341 CYS A C 1 ATOM 2683 O O . CYS A 1 341 ? 25.371 20.904 20.120 1.00 26.95 ? 341 CYS A O 1 ATOM 2684 C CB . CYS A 1 341 ? 24.173 21.336 22.484 1.00 23.05 ? 341 CYS A CB 1 ATOM 2685 S SG . CYS A 1 341 ? 23.661 21.976 24.100 1.00 24.04 ? 341 CYS A SG 1 ATOM 2686 N N . ASN A 1 342 ? 23.828 21.971 18.869 1.00 24.09 ? 342 ASN A N 1 ATOM 2687 C CA . ASN A 1 342 ? 24.352 21.513 17.584 1.00 24.66 ? 342 ASN A CA 1 ATOM 2688 C C . ASN A 1 342 ? 25.857 21.687 17.364 1.00 24.47 ? 342 ASN A C 1 ATOM 2689 O O . ASN A 1 342 ? 26.531 22.423 18.085 1.00 23.78 ? 342 ASN A O 1 ATOM 2690 C CB . ASN A 1 342 ? 23.570 22.172 16.444 1.00 23.49 ? 342 ASN A CB 1 ATOM 2691 C CG . ASN A 1 342 ? 23.818 23.653 16.351 1.00 24.64 ? 342 ASN A CG 1 ATOM 2692 O OD1 . ASN A 1 342 ? 24.897 24.084 15.935 1.00 25.63 ? 342 ASN A OD1 1 ATOM 2693 N ND2 . ASN A 1 342 ? 22.825 24.450 16.744 1.00 21.45 ? 342 ASN A ND2 1 ATOM 2694 N N . TRP A 1 343 ? 26.369 20.994 16.352 1.00 25.04 ? 343 TRP A N 1 ATOM 2695 C CA . TRP A 1 343 ? 27.783 21.027 16.033 1.00 24.81 ? 343 TRP A CA 1 ATOM 2696 C C . TRP A 1 343 ? 28.240 22.325 15.385 1.00 25.58 ? 343 TRP A C 1 ATOM 2697 O O . TRP A 1 343 ? 29.413 22.687 15.492 1.00 25.02 ? 343 TRP A O 1 ATOM 2698 C CB . TRP A 1 343 ? 28.150 19.849 15.128 1.00 24.89 ? 343 TRP A CB 1 ATOM 2699 C CG . TRP A 1 343 ? 27.586 19.942 13.753 1.00 25.77 ? 343 TRP A CG 1 ATOM 2700 C CD1 . TRP A 1 343 ? 26.295 19.723 13.380 1.00 26.08 ? 343 TRP A CD1 1 ATOM 2701 C CD2 . TRP A 1 343 ? 28.292 20.315 12.564 1.00 27.22 ? 343 TRP A CD2 1 ATOM 2702 N NE1 . TRP A 1 343 ? 26.148 19.937 12.031 1.00 26.74 ? 343 TRP A NE1 1 ATOM 2703 C CE2 . TRP A 1 343 ? 27.360 20.302 11.504 1.00 26.60 ? 343 TRP A CE2 1 ATOM 2704 C CE3 . TRP A 1 343 ? 29.626 20.663 12.291 1.00 27.94 ? 343 TRP A CE3 1 ATOM 2705 C CZ2 . TRP A 1 343 ? 27.714 20.621 10.188 1.00 26.12 ? 343 TRP A CZ2 1 ATOM 2706 C CZ3 . TRP A 1 343 ? 29.980 20.981 10.981 1.00 27.32 ? 343 TRP A CZ3 1 ATOM 2707 C CH2 . TRP A 1 343 ? 29.024 20.957 9.947 1.00 26.56 ? 343 TRP A CH2 1 ATOM 2708 N N . LEU A 1 344 ? 27.332 23.021 14.707 1.00 26.36 ? 344 LEU A N 1 ATOM 2709 C CA . LEU A 1 344 ? 27.708 24.276 14.068 1.00 28.01 ? 344 LEU A CA 1 ATOM 2710 C C . LEU A 1 344 ? 28.106 25.270 15.144 1.00 28.87 ? 344 LEU A C 1 ATOM 2711 O O . LEU A 1 344 ? 29.188 25.855 15.094 1.00 30.86 ? 344 LEU A O 1 ATOM 2712 C CB . LEU A 1 344 ? 26.557 24.836 13.227 1.00 26.89 ? 344 LEU A CB 1 ATOM 2713 C CG . LEU A 1 344 ? 26.243 24.029 11.958 1.00 28.70 ? 344 LEU A CG 1 ATOM 2714 C CD1 . LEU A 1 344 ? 25.108 24.686 11.185 1.00 26.95 ? 344 LEU A CD1 1 ATOM 2715 C CD2 . LEU A 1 344 ? 27.485 23.931 11.093 1.00 25.96 ? 344 LEU A CD2 1 ATOM 2716 N N . GLY A 1 345 ? 27.238 25.441 16.130 1.00 29.75 ? 345 GLY A N 1 ATOM 2717 C CA . GLY A 1 345 ? 27.534 26.358 17.211 1.00 30.52 ? 345 GLY A CA 1 ATOM 2718 C C . GLY A 1 345 ? 28.804 25.967 17.937 1.00 31.85 ? 345 GLY A C 1 ATOM 2719 O O . GLY A 1 345 ? 29.611 26.832 18.274 1.00 32.46 ? 345 GLY A O 1 ATOM 2720 N N . ASN A 1 346 ? 28.996 24.671 18.172 1.00 32.34 ? 346 ASN A N 1 ATOM 2721 C CA . ASN A 1 346 ? 30.189 24.200 18.872 1.00 34.08 ? 346 ASN A CA 1 ATOM 2722 C C . ASN A 1 346 ? 31.491 24.351 18.093 1.00 34.72 ? 346 ASN A C 1 ATOM 2723 O O . ASN A 1 346 ? 32.562 24.508 18.682 1.00 35.04 ? 346 ASN A O 1 ATOM 2724 C CB . ASN A 1 346 ? 30.000 22.752 19.318 1.00 34.03 ? 346 ASN A CB 1 ATOM 2725 C CG . ASN A 1 346 ? 29.364 22.658 20.693 1.00 36.57 ? 346 ASN A CG 1 ATOM 2726 O OD1 . ASN A 1 346 ? 29.965 23.063 21.692 1.00 36.43 ? 346 ASN A OD1 1 ATOM 2727 N ND2 . ASN A 1 346 ? 28.141 22.143 20.752 1.00 35.88 ? 346 ASN A ND2 1 ATOM 2728 N N . LYS A 1 347 ? 31.404 24.298 16.771 1.00 35.10 ? 347 LYS A N 1 ATOM 2729 C CA . LYS A 1 347 ? 32.583 24.472 15.936 1.00 33.91 ? 347 LYS A CA 1 ATOM 2730 C C . LYS A 1 347 ? 32.885 25.966 15.880 1.00 32.72 ? 347 LYS A C 1 ATOM 2731 O O . LYS A 1 347 ? 34.044 26.381 15.810 1.00 31.33 ? 347 LYS A O 1 ATOM 2732 C CB . LYS A 1 347 ? 32.320 23.944 14.522 1.00 35.18 ? 347 LYS A CB 1 ATOM 2733 C CG . LYS A 1 347 ? 33.327 24.404 13.485 1.00 34.37 ? 347 LYS A CG 1 ATOM 2734 C CD . LYS A 1 347 ? 33.020 23.819 12.116 1.00 36.88 ? 347 LYS A CD 1 ATOM 2735 C CE . LYS A 1 347 ? 33.864 24.478 11.025 1.00 39.50 ? 347 LYS A CE 1 ATOM 2736 N NZ . LYS A 1 347 ? 35.341 24.423 11.326 1.00 41.55 ? 347 LYS A NZ 1 ATOM 2737 N N . ALA A 1 348 ? 31.830 26.774 15.932 1.00 29.58 ? 348 ALA A N 1 ATOM 2738 C CA . ALA A 1 348 ? 31.989 28.221 15.868 1.00 28.99 ? 348 ALA A CA 1 ATOM 2739 C C . ALA A 1 348 ? 32.716 28.843 17.070 1.00 29.19 ? 348 ALA A C 1 ATOM 2740 O O . ALA A 1 348 ? 33.686 29.581 16.891 1.00 29.29 ? 348 ALA A O 1 ATOM 2741 C CB . ALA A 1 348 ? 30.635 28.881 15.670 1.00 25.69 ? 348 ALA A CB 1 ATOM 2742 N N . TRP A 1 349 ? 32.276 28.561 18.292 1.00 27.25 ? 349 TRP A N 1 ATOM 2743 C CA . TRP A 1 349 ? 32.962 29.166 19.421 1.00 28.47 ? 349 TRP A CA 1 ATOM 2744 C C . TRP A 1 349 ? 34.361 28.582 19.564 1.00 29.61 ? 349 TRP A C 1 ATOM 2745 O O . TRP A 1 349 ? 35.264 29.191 20.143 1.00 30.63 ? 349 TRP A O 1 ATOM 2746 C CB . TRP A 1 349 ? 32.168 28.996 20.725 1.00 24.80 ? 349 TRP A CB 1 ATOM 2747 C CG . TRP A 1 349 ? 32.279 27.658 21.395 1.00 23.75 ? 349 TRP A CG 1 ATOM 2748 C CD1 . TRP A 1 349 ? 31.384 26.627 21.319 1.00 23.83 ? 349 TRP A CD1 1 ATOM 2749 C CD2 . TRP A 1 349 ? 33.312 27.227 22.296 1.00 22.92 ? 349 TRP A CD2 1 ATOM 2750 N NE1 . TRP A 1 349 ? 31.791 25.587 22.118 1.00 24.53 ? 349 TRP A NE1 1 ATOM 2751 C CE2 . TRP A 1 349 ? 32.971 25.926 22.729 1.00 23.44 ? 349 TRP A CE2 1 ATOM 2752 C CE3 . TRP A 1 349 ? 34.494 27.815 22.779 1.00 22.64 ? 349 TRP A CE3 1 ATOM 2753 C CZ2 . TRP A 1 349 ? 33.769 25.197 23.624 1.00 22.63 ? 349 TRP A CZ2 1 ATOM 2754 C CZ3 . TRP A 1 349 ? 35.291 27.091 23.669 1.00 21.37 ? 349 TRP A CZ3 1 ATOM 2755 C CH2 . TRP A 1 349 ? 34.921 25.793 24.081 1.00 23.17 ? 349 TRP A CH2 1 ATOM 2756 N N . THR A 1 350 ? 34.544 27.402 19.002 1.00 30.69 ? 350 THR A N 1 ATOM 2757 C CA . THR A 1 350 ? 35.828 26.739 19.074 1.00 31.66 ? 350 THR A CA 1 ATOM 2758 C C . THR A 1 350 ? 36.824 27.360 18.072 1.00 32.35 ? 350 THR A C 1 ATOM 2759 O O . THR A 1 350 ? 38.023 27.406 18.325 1.00 33.11 ? 350 THR A O 1 ATOM 2760 C CB . THR A 1 350 ? 35.639 25.230 18.815 1.00 31.99 ? 350 THR A CB 1 ATOM 2761 O OG1 . THR A 1 350 ? 36.598 24.498 19.572 1.00 34.43 ? 350 THR A OG1 1 ATOM 2762 C CG2 . THR A 1 350 ? 35.806 24.897 17.343 1.00 33.14 ? 350 THR A CG2 1 ATOM 2763 N N . ASP A 1 351 ? 36.318 27.853 16.946 1.00 31.88 ? 351 ASP A N 1 ATOM 2764 C CA . ASP A 1 351 ? 37.158 28.463 15.923 1.00 30.63 ? 351 ASP A CA 1 ATOM 2765 C C . ASP A 1 351 ? 37.574 29.894 16.260 1.00 31.51 ? 351 ASP A C 1 ATOM 2766 O O . ASP A 1 351 ? 38.589 30.380 15.770 1.00 35.10 ? 351 ASP A O 1 ATOM 2767 C CB . ASP A 1 351 ? 36.428 28.501 14.572 1.00 31.25 ? 351 ASP A CB 1 ATOM 2768 C CG . ASP A 1 351 ? 36.542 27.200 13.786 1.00 33.22 ? 351 ASP A CG 1 ATOM 2769 O OD1 . ASP A 1 351 ? 37.399 26.348 14.112 1.00 35.11 ? 351 ASP A OD1 1 ATOM 2770 O OD2 . ASP A 1 351 ? 35.772 27.040 12.815 1.00 33.03 ? 351 ASP A OD2 1 ATOM 2771 N N . VAL A 1 352 ? 36.795 30.582 17.083 1.00 29.95 ? 352 VAL A N 1 ATOM 2772 C CA . VAL A 1 352 ? 37.112 31.967 17.398 1.00 26.74 ? 352 VAL A CA 1 ATOM 2773 C C . VAL A 1 352 ? 37.568 32.232 18.819 1.00 27.22 ? 352 VAL A C 1 ATOM 2774 O O . VAL A 1 352 ? 37.880 33.367 19.163 1.00 28.35 ? 352 VAL A O 1 ATOM 2775 C CB . VAL A 1 352 ? 35.906 32.867 17.118 1.00 26.05 ? 352 VAL A CB 1 ATOM 2776 C CG1 . VAL A 1 352 ? 35.429 32.638 15.702 1.00 22.15 ? 352 VAL A CG1 1 ATOM 2777 C CG2 . VAL A 1 352 ? 34.785 32.582 18.130 1.00 24.05 ? 352 VAL A CG2 1 ATOM 2778 N N . LEU A 1 353 ? 37.602 31.198 19.647 1.00 27.54 ? 353 LEU A N 1 ATOM 2779 C CA . LEU A 1 353 ? 38.019 31.371 21.028 1.00 28.30 ? 353 LEU A CA 1 ATOM 2780 C C . LEU A 1 353 ? 39.437 31.923 21.067 1.00 29.58 ? 353 LEU A C 1 ATOM 2781 O O . LEU A 1 353 ? 40.309 31.439 20.360 1.00 32.78 ? 353 LEU A O 1 ATOM 2782 C CB . LEU A 1 353 ? 37.983 30.032 21.767 1.00 25.92 ? 353 LEU A CB 1 ATOM 2783 C CG . LEU A 1 353 ? 38.429 30.125 23.230 1.00 24.88 ? 353 LEU A CG 1 ATOM 2784 C CD1 . LEU A 1 353 ? 37.350 30.844 24.028 1.00 21.66 ? 353 LEU A CD1 1 ATOM 2785 C CD2 . LEU A 1 353 ? 38.687 28.740 23.800 1.00 22.64 ? 353 LEU A CD2 1 ATOM 2786 N N . PRO A 1 354 ? 39.687 32.951 21.888 1.00 29.87 ? 354 PRO A N 1 ATOM 2787 C CA . PRO A 1 354 ? 41.048 33.489 21.943 1.00 29.64 ? 354 PRO A CA 1 ATOM 2788 C C . PRO A 1 354 ? 41.904 32.680 22.917 1.00 30.56 ? 354 PRO A C 1 ATOM 2789 O O . PRO A 1 354 ? 41.434 32.282 23.988 1.00 31.86 ? 354 PRO A O 1 ATOM 2790 C CB . PRO A 1 354 ? 40.846 34.921 22.444 1.00 29.63 ? 354 PRO A CB 1 ATOM 2791 C CG . PRO A 1 354 ? 39.358 35.190 22.258 1.00 29.57 ? 354 PRO A CG 1 ATOM 2792 C CD . PRO A 1 354 ? 38.744 33.859 22.556 1.00 30.32 ? 354 PRO A CD 1 ATOM 2793 N N . TRP A 1 355 ? 43.147 32.424 22.528 1.00 29.74 ? 355 TRP A N 1 ATOM 2794 C CA . TRP A 1 355 ? 44.112 31.707 23.360 1.00 30.85 ? 355 TRP A CA 1 ATOM 2795 C C . TRP A 1 355 ? 45.461 31.762 22.649 1.00 32.21 ? 355 TRP A C 1 ATOM 2796 O O . TRP A 1 355 ? 45.527 32.124 21.469 1.00 31.51 ? 355 TRP A O 1 ATOM 2797 C CB . TRP A 1 355 ? 43.673 30.257 23.635 1.00 29.96 ? 355 TRP A CB 1 ATOM 2798 C CG . TRP A 1 355 ? 43.516 29.392 22.431 1.00 28.74 ? 355 TRP A CG 1 ATOM 2799 C CD1 . TRP A 1 355 ? 42.679 29.599 21.371 1.00 30.55 ? 355 TRP A CD1 1 ATOM 2800 C CD2 . TRP A 1 355 ? 44.201 28.165 22.169 1.00 26.87 ? 355 TRP A CD2 1 ATOM 2801 N NE1 . TRP A 1 355 ? 42.804 28.572 20.459 1.00 29.55 ? 355 TRP A NE1 1 ATOM 2802 C CE2 . TRP A 1 355 ? 43.732 27.680 20.926 1.00 26.74 ? 355 TRP A CE2 1 ATOM 2803 C CE3 . TRP A 1 355 ? 45.166 27.426 22.865 1.00 27.60 ? 355 TRP A CE3 1 ATOM 2804 C CZ2 . TRP A 1 355 ? 44.196 26.493 20.365 1.00 26.12 ? 355 TRP A CZ2 1 ATOM 2805 C CZ3 . TRP A 1 355 ? 45.630 26.243 22.307 1.00 27.09 ? 355 TRP A CZ3 1 ATOM 2806 C CH2 . TRP A 1 355 ? 45.143 25.789 21.067 1.00 28.88 ? 355 TRP A CH2 1 ATOM 2807 N N . LYS A 1 356 ? 46.536 31.412 23.350 1.00 33.71 ? 356 LYS A N 1 ATOM 2808 C CA . LYS A 1 356 ? 47.855 31.512 22.749 1.00 34.97 ? 356 LYS A CA 1 ATOM 2809 C C . LYS A 1 356 ? 48.028 30.903 21.365 1.00 37.26 ? 356 LYS A C 1 ATOM 2810 O O . LYS A 1 356 ? 48.796 31.436 20.563 1.00 37.95 ? 356 LYS A O 1 ATOM 2811 C CB . LYS A 1 356 ? 48.930 30.992 23.706 1.00 35.60 ? 356 LYS A CB 1 ATOM 2812 C CG . LYS A 1 356 ? 48.856 29.531 24.083 1.00 38.02 ? 356 LYS A CG 1 ATOM 2813 C CD . LYS A 1 356 ? 49.820 29.262 25.236 1.00 37.28 ? 356 LYS A CD 1 ATOM 2814 C CE . LYS A 1 356 ? 49.982 27.779 25.518 1.00 38.93 ? 356 LYS A CE 1 ATOM 2815 N NZ . LYS A 1 356 ? 50.783 27.546 26.759 1.00 40.09 ? 356 LYS A NZ 1 ATOM 2816 N N . TYR A 1 357 ? 47.322 29.816 21.058 1.00 38.37 ? 357 TYR A N 1 ATOM 2817 C CA . TYR A 1 357 ? 47.458 29.219 19.729 1.00 40.41 ? 357 TYR A CA 1 ATOM 2818 C C . TYR A 1 357 ? 46.212 29.355 18.862 1.00 41.25 ? 357 TYR A C 1 ATOM 2819 O O . TYR A 1 357 ? 46.022 28.578 17.930 1.00 41.20 ? 357 TYR A O 1 ATOM 2820 C CB . TYR A 1 357 ? 47.829 27.738 19.824 1.00 41.91 ? 357 TYR A CB 1 ATOM 2821 C CG . TYR A 1 357 ? 49.142 27.469 20.518 1.00 45.76 ? 357 TYR A CG 1 ATOM 2822 C CD1 . TYR A 1 357 ? 50.284 28.207 20.209 1.00 47.49 ? 357 TYR A CD1 1 ATOM 2823 C CD2 . TYR A 1 357 ? 49.245 26.475 21.486 1.00 47.26 ? 357 TYR A CD2 1 ATOM 2824 C CE1 . TYR A 1 357 ? 51.494 27.962 20.852 1.00 48.50 ? 357 TYR A CE1 1 ATOM 2825 C CE2 . TYR A 1 357 ? 50.447 26.221 22.135 1.00 48.53 ? 357 TYR A CE2 1 ATOM 2826 C CZ . TYR A 1 357 ? 51.567 26.968 21.815 1.00 49.55 ? 357 TYR A CZ 1 ATOM 2827 O OH . TYR A 1 357 ? 52.755 26.720 22.465 1.00 51.00 ? 357 TYR A OH 1 ATOM 2828 N N . ASP A 1 358 ? 45.371 30.343 19.143 1.00 41.96 ? 358 ASP A N 1 ATOM 2829 C CA . ASP A 1 358 ? 44.154 30.506 18.356 1.00 44.91 ? 358 ASP A CA 1 ATOM 2830 C C . ASP A 1 358 ? 44.397 30.688 16.863 1.00 47.01 ? 358 ASP A C 1 ATOM 2831 O O . ASP A 1 358 ? 43.526 30.392 16.045 1.00 47.92 ? 358 ASP A O 1 ATOM 2832 C CB . ASP A 1 358 ? 43.301 31.671 18.886 1.00 43.10 ? 358 ASP A CB 1 ATOM 2833 C CG . ASP A 1 358 ? 44.056 32.984 18.944 1.00 43.90 ? 358 ASP A CG 1 ATOM 2834 O OD1 . ASP A 1 358 ? 45.122 33.104 18.305 1.00 45.57 ? 358 ASP A OD1 1 ATOM 2835 O OD2 . ASP A 1 358 ? 43.567 33.908 19.624 1.00 42.93 ? 358 ASP A OD2 1 ATOM 2836 N N . GLU A 1 359 ? 45.580 31.168 16.505 1.00 50.22 ? 359 GLU A N 1 ATOM 2837 C CA . GLU A 1 359 ? 45.906 31.394 15.102 1.00 53.45 ? 359 GLU A CA 1 ATOM 2838 C C . GLU A 1 359 ? 46.230 30.098 14.378 1.00 52.59 ? 359 GLU A C 1 ATOM 2839 O O . GLU A 1 359 ? 45.739 29.848 13.278 1.00 52.12 ? 359 GLU A O 1 ATOM 2840 C CB . GLU A 1 359 ? 47.089 32.357 14.990 1.00 57.66 ? 359 GLU A CB 1 ATOM 2841 C CG . GLU A 1 359 ? 46.811 33.721 15.593 1.00 65.52 ? 359 GLU A CG 1 ATOM 2842 C CD . GLU A 1 359 ? 45.655 34.432 14.906 1.00 69.86 ? 359 GLU A CD 1 ATOM 2843 O OE1 . GLU A 1 359 ? 45.197 35.471 15.432 1.00 72.17 ? 359 GLU A OE1 1 ATOM 2844 O OE2 . GLU A 1 359 ? 45.208 33.955 13.837 1.00 72.20 ? 359 GLU A OE2 1 ATOM 2845 N N . GLU A 1 360 ? 47.064 29.279 15.003 1.00 51.48 ? 360 GLU A N 1 ATOM 2846 C CA . GLU A 1 360 ? 47.461 28.012 14.423 1.00 51.07 ? 360 GLU A CA 1 ATOM 2847 C C . GLU A 1 360 ? 46.273 27.062 14.362 1.00 51.58 ? 360 GLU A C 1 ATOM 2848 O O . GLU A 1 360 ? 46.182 26.226 13.456 1.00 52.93 ? 360 GLU A O 1 ATOM 2849 C CB . GLU A 1 360 ? 48.596 27.389 15.240 1.00 51.02 ? 360 GLU A CB 1 ATOM 2850 C CG . GLU A 1 360 ? 49.897 28.180 15.207 1.00 51.12 ? 360 GLU A CG 1 ATOM 2851 C CD . GLU A 1 360 ? 49.945 29.304 16.227 1.00 52.48 ? 360 GLU A CD 1 ATOM 2852 O OE1 . GLU A 1 360 ? 48.988 30.105 16.300 1.00 52.03 ? 360 GLU A OE1 1 ATOM 2853 O OE2 . GLU A 1 360 ? 50.954 29.391 16.958 1.00 53.83 ? 360 GLU A OE2 1 ATOM 2854 N N . PHE A 1 361 ? 45.361 27.196 15.326 1.00 50.22 ? 361 PHE A N 1 ATOM 2855 C CA . PHE A 1 361 ? 44.173 26.346 15.383 1.00 47.97 ? 361 PHE A CA 1 ATOM 2856 C C . PHE A 1 361 ? 43.227 26.700 14.240 1.00 47.81 ? 361 PHE A C 1 ATOM 2857 O O . PHE A 1 361 ? 42.811 25.836 13.466 1.00 46.98 ? 361 PHE A O 1 ATOM 2858 C CB . PHE A 1 361 ? 43.455 26.515 16.729 1.00 43.35 ? 361 PHE A CB 1 ATOM 2859 C CG . PHE A 1 361 ? 42.252 25.615 16.898 1.00 40.34 ? 361 PHE A CG 1 ATOM 2860 C CD1 . PHE A 1 361 ? 40.960 26.124 16.783 1.00 36.99 ? 361 PHE A CD1 1 ATOM 2861 C CD2 . PHE A 1 361 ? 42.413 24.254 17.158 1.00 39.75 ? 361 PHE A CD2 1 ATOM 2862 C CE1 . PHE A 1 361 ? 39.849 25.299 16.923 1.00 34.63 ? 361 PHE A CE1 1 ATOM 2863 C CE2 . PHE A 1 361 ? 41.304 23.417 17.300 1.00 38.15 ? 361 PHE A CE2 1 ATOM 2864 C CZ . PHE A 1 361 ? 40.019 23.944 17.182 1.00 37.03 ? 361 PHE A CZ 1 ATOM 2865 N N . ALA A 1 362 ? 42.897 27.981 14.139 1.00 47.65 ? 362 ALA A N 1 ATOM 2866 C CA . ALA A 1 362 ? 42.006 28.447 13.096 1.00 48.38 ? 362 ALA A CA 1 ATOM 2867 C C . ALA A 1 362 ? 42.548 28.063 11.722 1.00 49.32 ? 362 ALA A C 1 ATOM 2868 O O . ALA A 1 362 ? 41.780 27.777 10.802 1.00 49.40 ? 362 ALA A O 1 ATOM 2869 C CB . ALA A 1 362 ? 41.838 29.949 13.200 1.00 47.54 ? 362 ALA A CB 1 ATOM 2870 N N . SER A 1 363 ? 43.872 28.050 11.591 1.00 50.26 ? 363 SER A N 1 ATOM 2871 C CA . SER A 1 363 ? 44.522 27.701 10.332 1.00 51.74 ? 363 SER A CA 1 ATOM 2872 C C . SER A 1 363 ? 44.375 26.225 9.988 1.00 52.64 ? 363 SER A C 1 ATOM 2873 O O . SER A 1 363 ? 44.151 25.878 8.834 1.00 53.03 ? 363 SER A O 1 ATOM 2874 C CB . SER A 1 363 ? 46.013 28.043 10.383 1.00 52.66 ? 363 SER A CB 1 ATOM 2875 O OG . SER A 1 363 ? 46.221 29.440 10.353 1.00 55.89 ? 363 SER A OG 1 ATOM 2876 N N . GLN A 1 364 ? 44.516 25.359 10.989 1.00 53.45 ? 364 GLN A N 1 ATOM 2877 C CA . GLN A 1 364 ? 44.404 23.921 10.778 1.00 53.41 ? 364 GLN A CA 1 ATOM 2878 C C . GLN A 1 364 ? 43.223 23.573 9.890 1.00 52.93 ? 364 GLN A C 1 ATOM 2879 O O . GLN A 1 364 ? 42.164 24.194 9.978 1.00 52.48 ? 364 GLN A O 1 ATOM 2880 C CB . GLN A 1 364 ? 44.260 23.202 12.115 1.00 55.01 ? 364 GLN A CB 1 ATOM 2881 C CG . GLN A 1 364 ? 45.513 23.248 12.962 1.00 58.85 ? 364 GLN A CG 1 ATOM 2882 C CD . GLN A 1 364 ? 46.700 22.600 12.271 1.00 59.95 ? 364 GLN A CD 1 ATOM 2883 O OE1 . GLN A 1 364 ? 46.702 21.395 12.003 1.00 59.69 ? 364 GLN A OE1 1 ATOM 2884 N NE2 . GLN A 1 364 ? 47.715 23.402 11.972 1.00 60.64 ? 364 GLN A NE2 1 ATOM 2885 N N . LYS A 1 365 ? 43.414 22.580 9.030 1.00 52.32 ? 365 LYS A N 1 ATOM 2886 C CA . LYS A 1 365 ? 42.358 22.148 8.123 1.00 53.21 ? 365 LYS A CA 1 ATOM 2887 C C . LYS A 1 365 ? 41.633 20.949 8.728 1.00 51.11 ? 365 LYS A C 1 ATOM 2888 O O . LYS A 1 365 ? 42.270 20.056 9.285 1.00 50.04 ? 365 LYS A O 1 ATOM 2889 C CB . LYS A 1 365 ? 42.949 21.758 6.760 1.00 55.87 ? 365 LYS A CB 1 ATOM 2890 C CG . LYS A 1 365 ? 41.931 21.811 5.626 1.00 58.97 ? 365 LYS A CG 1 ATOM 2891 C CD . LYS A 1 365 ? 41.505 23.258 5.338 1.00 60.93 ? 365 LYS A CD 1 ATOM 2892 C CE . LYS A 1 365 ? 40.013 23.364 5.031 1.00 61.51 ? 365 LYS A CE 1 ATOM 2893 N NZ . LYS A 1 365 ? 39.178 23.010 6.221 1.00 61.59 ? 365 LYS A NZ 1 ATOM 2894 N N . VAL A 1 366 ? 40.308 20.923 8.625 1.00 49.08 ? 366 VAL A N 1 ATOM 2895 C CA . VAL A 1 366 ? 39.565 19.802 9.186 1.00 48.08 ? 366 VAL A CA 1 ATOM 2896 C C . VAL A 1 366 ? 39.875 18.558 8.369 1.00 46.69 ? 366 VAL A C 1 ATOM 2897 O O . VAL A 1 366 ? 39.949 18.613 7.143 1.00 47.73 ? 366 VAL A O 1 ATOM 2898 C CB . VAL A 1 366 ? 38.031 20.054 9.186 1.00 46.66 ? 366 VAL A CB 1 ATOM 2899 C CG1 . VAL A 1 366 ? 37.754 21.488 9.565 1.00 47.65 ? 366 VAL A CG1 1 ATOM 2900 C CG2 . VAL A 1 366 ? 37.425 19.724 7.838 1.00 47.33 ? 366 VAL A CG2 1 ATOM 2901 N N . ARG A 1 367 ? 40.071 17.440 9.050 1.00 44.74 ? 367 ARG A N 1 ATOM 2902 C CA . ARG A 1 367 ? 40.369 16.198 8.363 1.00 45.92 ? 367 ARG A CA 1 ATOM 2903 C C . ARG A 1 367 ? 39.394 15.109 8.793 1.00 44.84 ? 367 ARG A C 1 ATOM 2904 O O . ARG A 1 367 ? 38.600 15.308 9.704 1.00 45.04 ? 367 ARG A O 1 ATOM 2905 C CB . ARG A 1 367 ? 41.817 15.784 8.651 1.00 47.35 ? 367 ARG A CB 1 ATOM 2906 C CG . ARG A 1 367 ? 42.170 15.739 10.117 1.00 49.68 ? 367 ARG A CG 1 ATOM 2907 C CD . ARG A 1 367 ? 43.636 15.395 10.326 1.00 50.88 ? 367 ARG A CD 1 ATOM 2908 N NE . ARG A 1 367 ? 43.905 15.037 11.720 1.00 53.03 ? 367 ARG A NE 1 ATOM 2909 C CZ . ARG A 1 367 ? 43.890 15.893 12.737 1.00 52.67 ? 367 ARG A CZ 1 ATOM 2910 N NH1 . ARG A 1 367 ? 44.141 15.463 13.965 1.00 52.58 ? 367 ARG A NH1 1 ATOM 2911 N NH2 . ARG A 1 367 ? 43.642 17.182 12.528 1.00 53.64 ? 367 ARG A NH2 1 ATOM 2912 N N . ASN A 1 368 ? 39.431 13.964 8.125 1.00 45.12 ? 368 ASN A N 1 ATOM 2913 C CA . ASN A 1 368 ? 38.533 12.880 8.489 1.00 43.75 ? 368 ASN A CA 1 ATOM 2914 C C . ASN A 1 368 ? 39.067 12.129 9.683 1.00 41.38 ? 368 ASN A C 1 ATOM 2915 O O . ASN A 1 368 ? 40.279 11.958 9.831 1.00 40.14 ? 368 ASN A O 1 ATOM 2916 C CB . ASN A 1 368 ? 38.346 11.900 7.334 1.00 47.53 ? 368 ASN A CB 1 ATOM 2917 C CG . ASN A 1 368 ? 37.292 12.350 6.358 1.00 53.37 ? 368 ASN A CG 1 ATOM 2918 O OD1 . ASN A 1 368 ? 36.527 13.263 6.647 1.00 55.56 ? 368 ASN A OD1 1 ATOM 2919 N ND2 . ASN A 1 368 ? 37.237 11.703 5.200 1.00 61.36 ? 368 ASN A ND2 1 ATOM 2920 N N . TRP A 1 369 ? 38.153 11.696 10.544 1.00 39.26 ? 369 TRP A N 1 ATOM 2921 C CA . TRP A 1 369 ? 38.523 10.928 11.720 1.00 37.25 ? 369 TRP A CA 1 ATOM 2922 C C . TRP A 1 369 ? 37.997 9.508 11.572 1.00 37.97 ? 369 TRP A C 1 ATOM 2923 O O . TRP A 1 369 ? 36.796 9.297 11.381 1.00 38.33 ? 369 TRP A O 1 ATOM 2924 C CB . TRP A 1 369 ? 37.946 11.549 12.992 1.00 35.34 ? 369 TRP A CB 1 ATOM 2925 C CG . TRP A 1 369 ? 38.240 10.730 14.211 1.00 32.02 ? 369 TRP A CG 1 ATOM 2926 C CD1 . TRP A 1 369 ? 39.470 10.419 14.706 1.00 30.17 ? 369 TRP A CD1 1 ATOM 2927 C CD2 . TRP A 1 369 ? 37.287 10.059 15.048 1.00 31.75 ? 369 TRP A CD2 1 ATOM 2928 N NE1 . TRP A 1 369 ? 39.348 9.590 15.796 1.00 32.25 ? 369 TRP A NE1 1 ATOM 2929 C CE2 . TRP A 1 369 ? 38.019 9.352 16.030 1.00 30.75 ? 369 TRP A CE2 1 ATOM 2930 C CE3 . TRP A 1 369 ? 35.886 9.982 15.062 1.00 30.75 ? 369 TRP A CE3 1 ATOM 2931 C CZ2 . TRP A 1 369 ? 37.399 8.575 17.019 1.00 29.04 ? 369 TRP A CZ2 1 ATOM 2932 C CZ3 . TRP A 1 369 ? 35.265 9.204 16.051 1.00 30.09 ? 369 TRP A CZ3 1 ATOM 2933 C CH2 . TRP A 1 369 ? 36.026 8.512 17.013 1.00 29.63 ? 369 TRP A CH2 1 ATOM 2934 N N . THR A 1 370 ? 38.908 8.542 11.642 1.00 37.72 ? 370 THR A N 1 ATOM 2935 C CA . THR A 1 370 ? 38.556 7.136 11.540 1.00 37.63 ? 370 THR A CA 1 ATOM 2936 C C . THR A 1 370 ? 38.527 6.536 12.932 1.00 37.91 ? 370 THR A C 1 ATOM 2937 O O . THR A 1 370 ? 39.522 6.581 13.655 1.00 38.37 ? 370 THR A O 1 ATOM 2938 C CB . THR A 1 370 ? 39.578 6.354 10.686 1.00 36.47 ? 370 THR A CB 1 ATOM 2939 O OG1 . THR A 1 370 ? 39.468 6.771 9.323 1.00 38.70 ? 370 THR A OG1 1 ATOM 2940 C CG2 . THR A 1 370 ? 39.318 4.860 10.758 1.00 35.98 ? 370 THR A CG2 1 ATOM 2941 N N . ALA A 1 371 ? 37.376 5.990 13.312 1.00 38.36 ? 371 ALA A N 1 ATOM 2942 C CA . ALA A 1 371 ? 37.236 5.362 14.619 1.00 38.28 ? 371 ALA A CA 1 ATOM 2943 C C . ALA A 1 371 ? 38.093 4.100 14.604 1.00 38.30 ? 371 ALA A C 1 ATOM 2944 O O . ALA A 1 371 ? 38.039 3.314 13.657 1.00 38.41 ? 371 ALA A O 1 ATOM 2945 C CB . ALA A 1 371 ? 35.773 5.010 14.884 1.00 36.33 ? 371 ALA A CB 1 ATOM 2946 N N . SER A 1 372 ? 38.890 3.910 15.646 1.00 38.79 ? 372 SER A N 1 ATOM 2947 C CA . SER A 1 372 ? 39.754 2.737 15.717 1.00 39.01 ? 372 SER A CA 1 ATOM 2948 C C . SER A 1 372 ? 38.967 1.434 15.808 1.00 37.90 ? 372 SER A C 1 ATOM 2949 O O . SER A 1 372 ? 39.244 0.499 15.073 1.00 39.17 ? 372 SER A O 1 ATOM 2950 C CB . SER A 1 372 ? 40.696 2.846 16.916 1.00 38.89 ? 372 SER A CB 1 ATOM 2951 O OG . SER A 1 372 ? 39.964 2.908 18.128 1.00 43.68 ? 372 SER A OG 1 ATOM 2952 N N . ILE A 1 373 ? 37.984 1.378 16.701 1.00 36.49 ? 373 ILE A N 1 ATOM 2953 C CA . ILE A 1 373 ? 37.190 0.169 16.880 1.00 34.39 ? 373 ILE A CA 1 ATOM 2954 C C . ILE A 1 373 ? 36.504 -0.291 15.602 1.00 34.48 ? 373 ILE A C 1 ATOM 2955 O O . ILE A 1 373 ? 36.664 -1.431 15.185 1.00 35.89 ? 373 ILE A O 1 ATOM 2956 C CB . ILE A 1 373 ? 36.057 0.348 17.938 1.00 35.10 ? 373 ILE A CB 1 ATOM 2957 C CG1 . ILE A 1 373 ? 36.604 0.890 19.263 1.00 33.89 ? 373 ILE A CG1 1 ATOM 2958 C CG2 . ILE A 1 373 ? 35.352 -0.984 18.160 1.00 32.22 ? 373 ILE A CG2 1 ATOM 2959 C CD1 . ILE A 1 373 ? 37.455 -0.062 20.025 1.00 37.68 ? 373 ILE A CD1 1 ATOM 2960 N N . THR A 1 374 ? 35.734 0.604 14.992 1.00 34.31 ? 374 THR A N 1 ATOM 2961 C CA . THR A 1 374 ? 34.955 0.289 13.796 1.00 34.31 ? 374 THR A CA 1 ATOM 2962 C C . THR A 1 374 ? 35.665 0.490 12.475 1.00 35.63 ? 374 THR A C 1 ATOM 2963 O O . THR A 1 374 ? 35.265 -0.075 11.461 1.00 34.40 ? 374 THR A O 1 ATOM 2964 C CB . THR A 1 374 ? 33.688 1.142 13.736 1.00 34.37 ? 374 THR A CB 1 ATOM 2965 O OG1 . THR A 1 374 ? 34.057 2.527 13.668 1.00 32.52 ? 374 THR A OG1 1 ATOM 2966 C CG2 . THR A 1 374 ? 32.824 0.900 14.960 1.00 34.96 ? 374 THR A CG2 1 ATOM 2967 N N . ASP A 1 375 ? 36.694 1.326 12.482 1.00 37.38 ? 375 ASP A N 1 ATOM 2968 C CA . ASP A 1 375 ? 37.455 1.607 11.278 1.00 37.92 ? 375 ASP A CA 1 ATOM 2969 C C . ASP A 1 375 ? 36.621 2.404 10.279 1.00 36.78 ? 375 ASP A C 1 ATOM 2970 O O . ASP A 1 375 ? 36.940 2.462 9.092 1.00 36.18 ? 375 ASP A O 1 ATOM 2971 C CB . ASP A 1 375 ? 37.942 0.302 10.644 1.00 40.61 ? 375 ASP A CB 1 ATOM 2972 C CG . ASP A 1 375 ? 38.948 0.537 9.543 1.00 45.48 ? 375 ASP A CG 1 ATOM 2973 O OD1 . ASP A 1 375 ? 39.994 1.164 9.829 1.00 48.06 ? 375 ASP A OD1 1 ATOM 2974 O OD2 . ASP A 1 375 ? 38.696 0.102 8.396 1.00 48.04 ? 375 ASP A OD2 1 ATOM 2975 N N . GLU A 1 376 ? 35.551 3.023 10.765 1.00 35.36 ? 376 GLU A N 1 ATOM 2976 C CA . GLU A 1 376 ? 34.691 3.836 9.906 1.00 33.10 ? 376 GLU A CA 1 ATOM 2977 C C . GLU A 1 376 ? 35.152 5.291 9.957 1.00 31.50 ? 376 GLU A C 1 ATOM 2978 O O . GLU A 1 376 ? 35.772 5.715 10.935 1.00 32.08 ? 376 GLU A O 1 ATOM 2979 C CB . GLU A 1 376 ? 33.240 3.790 10.395 1.00 32.64 ? 376 GLU A CB 1 ATOM 2980 C CG . GLU A 1 376 ? 32.695 2.409 10.677 1.00 34.32 ? 376 GLU A CG 1 ATOM 2981 C CD . GLU A 1 376 ? 31.291 2.440 11.281 1.00 35.82 ? 376 GLU A CD 1 ATOM 2982 O OE1 . GLU A 1 376 ? 30.816 1.374 11.722 1.00 37.42 ? 376 GLU A OE1 1 ATOM 2983 O OE2 . GLU A 1 376 ? 30.660 3.519 11.318 1.00 34.57 ? 376 GLU A OE2 1 ATOM 2984 N N . VAL A 1 377 ? 34.879 6.050 8.903 1.00 29.32 ? 377 VAL A N 1 ATOM 2985 C CA . VAL A 1 377 ? 35.205 7.471 8.921 1.00 29.66 ? 377 VAL A CA 1 ATOM 2986 C C . VAL A 1 377 ? 34.009 7.982 9.721 1.00 30.68 ? 377 VAL A C 1 ATOM 2987 O O . VAL A 1 377 ? 32.924 8.186 9.175 1.00 30.38 ? 377 VAL A O 1 ATOM 2988 C CB . VAL A 1 377 ? 35.213 8.081 7.507 1.00 28.58 ? 377 VAL A CB 1 ATOM 2989 C CG1 . VAL A 1 377 ? 35.282 9.587 7.590 1.00 28.47 ? 377 VAL A CG1 1 ATOM 2990 C CG2 . VAL A 1 377 ? 36.414 7.572 6.741 1.00 28.28 ? 377 VAL A CG2 1 ATOM 2991 N N . ALA A 1 378 ? 34.215 8.150 11.025 1.00 31.07 ? 378 ALA A N 1 ATOM 2992 C CA . ALA A 1 378 ? 33.157 8.552 11.941 1.00 32.01 ? 378 ALA A CA 1 ATOM 2993 C C . ALA A 1 378 ? 32.959 10.041 12.174 1.00 33.10 ? 378 ALA A C 1 ATOM 2994 O O . ALA A 1 378 ? 32.020 10.431 12.873 1.00 33.92 ? 378 ALA A O 1 ATOM 2995 C CB . ALA A 1 378 ? 33.357 7.843 13.287 1.00 30.55 ? 378 ALA A CB 1 ATOM 2996 N N . GLY A 1 379 ? 33.822 10.876 11.605 1.00 32.72 ? 379 GLY A N 1 ATOM 2997 C CA . GLY A 1 379 ? 33.658 12.305 11.814 1.00 32.34 ? 379 GLY A CA 1 ATOM 2998 C C . GLY A 1 379 ? 34.749 13.177 11.236 1.00 32.12 ? 379 GLY A C 1 ATOM 2999 O O . GLY A 1 379 ? 35.629 12.707 10.518 1.00 33.30 ? 379 GLY A O 1 ATOM 3000 N N . GLU A 1 380 ? 34.687 14.464 11.550 1.00 32.83 ? 380 GLU A N 1 ATOM 3001 C CA . GLU A 1 380 ? 35.672 15.420 11.062 1.00 32.42 ? 380 GLU A CA 1 ATOM 3002 C C . GLU A 1 380 ? 36.355 16.049 12.259 1.00 32.17 ? 380 GLU A C 1 ATOM 3003 O O . GLU A 1 380 ? 35.692 16.534 13.176 1.00 32.17 ? 380 GLU A O 1 ATOM 3004 C CB . GLU A 1 380 ? 34.988 16.497 10.216 1.00 31.70 ? 380 GLU A CB 1 ATOM 3005 C CG . GLU A 1 380 ? 34.173 15.929 9.067 1.00 35.48 ? 380 GLU A CG 1 ATOM 3006 C CD . GLU A 1 380 ? 33.337 16.976 8.358 1.00 38.79 ? 380 GLU A CD 1 ATOM 3007 O OE1 . GLU A 1 380 ? 32.684 17.789 9.049 1.00 42.43 ? 380 GLU A OE1 1 ATOM 3008 O OE2 . GLU A 1 380 ? 33.320 16.981 7.108 1.00 38.05 ? 380 GLU A OE2 1 ATOM 3009 N N . VAL A 1 381 ? 37.682 16.014 12.256 1.00 32.34 ? 381 VAL A N 1 ATOM 3010 C CA . VAL A 1 381 ? 38.467 16.583 13.340 1.00 33.54 ? 381 VAL A CA 1 ATOM 3011 C C . VAL A 1 381 ? 39.171 17.854 12.928 1.00 34.45 ? 381 VAL A C 1 ATOM 3012 O O . VAL A 1 381 ? 39.291 18.178 11.749 1.00 35.82 ? 381 VAL A O 1 ATOM 3013 C CB . VAL A 1 381 ? 39.588 15.646 13.817 1.00 34.01 ? 381 VAL A CB 1 ATOM 3014 C CG1 . VAL A 1 381 ? 39.372 15.283 15.264 1.00 34.74 ? 381 VAL A CG1 1 ATOM 3015 C CG2 . VAL A 1 381 ? 39.670 14.425 12.923 1.00 34.02 ? 381 VAL A CG2 1 ATOM 3016 N N . LYS A 1 382 ? 39.647 18.558 13.939 1.00 34.95 ? 382 LYS A N 1 ATOM 3017 C CA . LYS A 1 382 ? 40.396 19.779 13.771 1.00 35.63 ? 382 LYS A CA 1 ATOM 3018 C C . LYS A 1 382 ? 41.058 19.973 15.107 1.00 36.79 ? 382 LYS A C 1 ATOM 3019 O O . LYS A 1 382 ? 40.384 20.171 16.121 1.00 37.07 ? 382 LYS A O 1 ATOM 3020 C CB . LYS A 1 382 ? 39.493 20.965 13.470 1.00 34.94 ? 382 LYS A CB 1 ATOM 3021 C CG . LYS A 1 382 ? 40.273 22.265 13.329 1.00 35.95 ? 382 LYS A CG 1 ATOM 3022 C CD . LYS A 1 382 ? 39.391 23.379 12.810 1.00 36.88 ? 382 LYS A CD 1 ATOM 3023 C CE . LYS A 1 382 ? 40.129 24.690 12.738 1.00 34.26 ? 382 LYS A CE 1 ATOM 3024 N NZ . LYS A 1 382 ? 39.254 25.721 12.127 1.00 35.07 ? 382 LYS A NZ 1 ATOM 3025 N N . SER A 1 383 ? 42.379 19.880 15.118 1.00 38.33 ? 383 SER A N 1 ATOM 3026 C CA . SER A 1 383 ? 43.114 20.052 16.356 1.00 41.35 ? 383 SER A CA 1 ATOM 3027 C C . SER A 1 383 ? 44.502 20.597 16.121 1.00 42.44 ? 383 SER A C 1 ATOM 3028 O O . SER A 1 383 ? 45.084 20.429 15.052 1.00 44.77 ? 383 SER A O 1 ATOM 3029 C CB . SER A 1 383 ? 43.213 18.726 17.108 1.00 40.22 ? 383 SER A CB 1 ATOM 3030 O OG . SER A 1 383 ? 43.817 17.737 16.300 1.00 41.36 ? 383 SER A OG 1 ATOM 3031 N N . TYR A 1 384 ? 45.012 21.273 17.138 1.00 42.95 ? 384 TYR A N 1 ATOM 3032 C CA . TYR A 1 384 ? 46.340 21.833 17.113 1.00 43.78 ? 384 TYR A CA 1 ATOM 3033 C C . TYR A 1 384 ? 46.801 21.757 18.545 1.00 44.76 ? 384 TYR A C 1 ATOM 3034 O O . TYR A 1 384 ? 46.124 22.244 19.443 1.00 45.52 ? 384 TYR A O 1 ATOM 3035 C CB . TYR A 1 384 ? 46.327 23.283 16.646 1.00 46.24 ? 384 TYR A CB 1 ATOM 3036 C CG . TYR A 1 384 ? 47.708 23.886 16.644 1.00 48.92 ? 384 TYR A CG 1 ATOM 3037 C CD1 . TYR A 1 384 ? 48.245 24.452 17.796 1.00 50.42 ? 384 TYR A CD1 1 ATOM 3038 C CD2 . TYR A 1 384 ? 48.512 23.821 15.506 1.00 51.13 ? 384 TYR A CD2 1 ATOM 3039 C CE1 . TYR A 1 384 ? 49.549 24.937 17.819 1.00 53.62 ? 384 TYR A CE1 1 ATOM 3040 C CE2 . TYR A 1 384 ? 49.820 24.299 15.518 1.00 52.81 ? 384 TYR A CE2 1 ATOM 3041 C CZ . TYR A 1 384 ? 50.332 24.854 16.677 1.00 53.77 ? 384 TYR A CZ 1 ATOM 3042 O OH . TYR A 1 384 ? 51.628 25.316 16.696 1.00 55.10 ? 384 TYR A OH 1 ATOM 3043 N N . LYS A 1 385 ? 47.949 21.136 18.763 1.00 45.96 ? 385 LYS A N 1 ATOM 3044 C CA . LYS A 1 385 ? 48.463 20.996 20.108 1.00 47.10 ? 385 LYS A CA 1 ATOM 3045 C C . LYS A 1 385 ? 47.430 20.266 20.962 1.00 47.10 ? 385 LYS A C 1 ATOM 3046 O O . LYS A 1 385 ? 46.968 19.189 20.594 1.00 47.93 ? 385 LYS A O 1 ATOM 3047 C CB . LYS A 1 385 ? 48.782 22.371 20.701 1.00 49.70 ? 385 LYS A CB 1 ATOM 3048 C CG . LYS A 1 385 ? 50.268 22.702 20.737 1.00 53.81 ? 385 LYS A CG 1 ATOM 3049 C CD . LYS A 1 385 ? 50.910 22.591 19.358 1.00 57.25 ? 385 LYS A CD 1 ATOM 3050 C CE . LYS A 1 385 ? 52.437 22.634 19.439 1.00 59.08 ? 385 LYS A CE 1 ATOM 3051 N NZ . LYS A 1 385 ? 52.949 23.872 20.093 1.00 59.97 ? 385 LYS A NZ 1 ATOM 3052 N N . HIS A 1 386 ? 47.045 20.868 22.080 1.00 45.90 ? 386 HIS A N 1 ATOM 3053 C CA . HIS A 1 386 ? 46.105 20.250 23.002 1.00 44.59 ? 386 HIS A CA 1 ATOM 3054 C C . HIS A 1 386 ? 44.649 20.719 22.915 1.00 42.67 ? 386 HIS A C 1 ATOM 3055 O O . HIS A 1 386 ? 43.908 20.637 23.898 1.00 42.66 ? 386 HIS A O 1 ATOM 3056 C CB . HIS A 1 386 ? 46.642 20.441 24.417 1.00 47.37 ? 386 HIS A CB 1 ATOM 3057 C CG . HIS A 1 386 ? 47.217 21.803 24.644 1.00 52.05 ? 386 HIS A CG 1 ATOM 3058 N ND1 . HIS A 1 386 ? 46.431 22.915 24.860 1.00 53.50 ? 386 HIS A ND1 1 ATOM 3059 C CD2 . HIS A 1 386 ? 48.493 22.249 24.586 1.00 53.66 ? 386 HIS A CD2 1 ATOM 3060 C CE1 . HIS A 1 386 ? 47.198 23.988 24.921 1.00 54.50 ? 386 HIS A CE1 1 ATOM 3061 N NE2 . HIS A 1 386 ? 48.453 23.612 24.757 1.00 55.45 ? 386 HIS A NE2 1 ATOM 3062 N N . PHE A 1 387 ? 44.234 21.204 21.750 1.00 39.21 ? 387 PHE A N 1 ATOM 3063 C CA . PHE A 1 387 ? 42.850 21.642 21.571 1.00 37.02 ? 387 PHE A CA 1 ATOM 3064 C C . PHE A 1 387 ? 42.287 20.872 20.377 1.00 35.86 ? 387 PHE A C 1 ATOM 3065 O O . PHE A 1 387 ? 42.839 20.927 19.279 1.00 35.99 ? 387 PHE A O 1 ATOM 3066 C CB . PHE A 1 387 ? 42.790 23.153 21.327 1.00 35.27 ? 387 PHE A CB 1 ATOM 3067 C CG . PHE A 1 387 ? 41.418 23.748 21.489 1.00 32.93 ? 387 PHE A CG 1 ATOM 3068 C CD1 . PHE A 1 387 ? 40.561 23.300 22.493 1.00 31.47 ? 387 PHE A CD1 1 ATOM 3069 C CD2 . PHE A 1 387 ? 41.004 24.808 20.676 1.00 33.43 ? 387 PHE A CD2 1 ATOM 3070 C CE1 . PHE A 1 387 ? 39.309 23.903 22.689 1.00 30.56 ? 387 PHE A CE1 1 ATOM 3071 C CE2 . PHE A 1 387 ? 39.754 25.421 20.862 1.00 29.77 ? 387 PHE A CE2 1 ATOM 3072 C CZ . PHE A 1 387 ? 38.909 24.966 21.872 1.00 29.75 ? 387 PHE A CZ 1 ATOM 3073 N N . THR A 1 388 ? 41.194 20.147 20.598 1.00 33.58 ? 388 THR A N 1 ATOM 3074 C CA . THR A 1 388 ? 40.596 19.336 19.546 1.00 31.14 ? 388 THR A CA 1 ATOM 3075 C C . THR A 1 388 ? 39.085 19.489 19.479 1.00 31.69 ? 388 THR A C 1 ATOM 3076 O O . THR A 1 388 ? 38.409 19.499 20.507 1.00 32.26 ? 388 THR A O 1 ATOM 3077 C CB . THR A 1 388 ? 40.913 17.828 19.767 1.00 29.25 ? 388 THR A CB 1 ATOM 3078 O OG1 . THR A 1 388 ? 42.330 17.633 19.797 1.00 28.44 ? 388 THR A OG1 1 ATOM 3079 C CG2 . THR A 1 388 ? 40.311 16.978 18.662 1.00 26.44 ? 388 THR A CG2 1 ATOM 3080 N N . TYR A 1 389 ? 38.563 19.608 18.262 1.00 31.12 ? 389 TYR A N 1 ATOM 3081 C CA . TYR A 1 389 ? 37.126 19.712 18.061 1.00 30.54 ? 389 TYR A CA 1 ATOM 3082 C C . TYR A 1 389 ? 36.679 18.570 17.163 1.00 31.20 ? 389 TYR A C 1 ATOM 3083 O O . TYR A 1 389 ? 37.147 18.448 16.033 1.00 31.34 ? 389 TYR A O 1 ATOM 3084 C CB . TYR A 1 389 ? 36.737 21.025 17.395 1.00 28.95 ? 389 TYR A CB 1 ATOM 3085 C CG . TYR A 1 389 ? 35.292 21.006 16.963 1.00 28.01 ? 389 TYR A CG 1 ATOM 3086 C CD1 . TYR A 1 389 ? 34.264 21.087 17.896 1.00 27.25 ? 389 TYR A CD1 1 ATOM 3087 C CD2 . TYR A 1 389 ? 34.951 20.830 15.629 1.00 27.52 ? 389 TYR A CD2 1 ATOM 3088 C CE1 . TYR A 1 389 ? 32.941 20.988 17.511 1.00 27.56 ? 389 TYR A CE1 1 ATOM 3089 C CE2 . TYR A 1 389 ? 33.629 20.732 15.233 1.00 27.22 ? 389 TYR A CE2 1 ATOM 3090 C CZ . TYR A 1 389 ? 32.627 20.809 16.176 1.00 28.18 ? 389 TYR A CZ 1 ATOM 3091 O OH . TYR A 1 389 ? 31.312 20.690 15.779 1.00 29.02 ? 389 TYR A OH 1 ATOM 3092 N N . LEU A 1 390 ? 35.759 17.746 17.655 1.00 31.16 ? 390 LEU A N 1 ATOM 3093 C CA . LEU A 1 390 ? 35.285 16.616 16.875 1.00 30.15 ? 390 LEU A CA 1 ATOM 3094 C C . LEU A 1 390 ? 33.804 16.643 16.533 1.00 31.02 ? 390 LEU A C 1 ATOM 3095 O O . LEU A 1 390 ? 32.939 16.746 17.413 1.00 30.81 ? 390 LEU A O 1 ATOM 3096 C CB . LEU A 1 390 ? 35.592 15.304 17.605 1.00 29.47 ? 390 LEU A CB 1 ATOM 3097 C CG . LEU A 1 390 ? 35.237 14.011 16.855 1.00 28.66 ? 390 LEU A CG 1 ATOM 3098 C CD1 . LEU A 1 390 ? 36.150 13.853 15.638 1.00 26.98 ? 390 LEU A CD1 1 ATOM 3099 C CD2 . LEU A 1 390 ? 35.394 12.815 17.785 1.00 27.42 ? 390 LEU A CD2 1 ATOM 3100 N N . ARG A 1 391 ? 33.519 16.557 15.240 1.00 30.71 ? 391 ARG A N 1 ATOM 3101 C CA . ARG A 1 391 ? 32.145 16.497 14.769 1.00 30.31 ? 391 ARG A CA 1 ATOM 3102 C C . ARG A 1 391 ? 31.852 15.000 14.625 1.00 29.39 ? 391 ARG A C 1 ATOM 3103 O O . ARG A 1 391 ? 32.519 14.313 13.855 1.00 29.78 ? 391 ARG A O 1 ATOM 3104 C CB . ARG A 1 391 ? 32.009 17.162 13.406 1.00 29.75 ? 391 ARG A CB 1 ATOM 3105 C CG . ARG A 1 391 ? 30.676 16.873 12.752 1.00 30.66 ? 391 ARG A CG 1 ATOM 3106 C CD . ARG A 1 391 ? 30.654 17.307 11.314 1.00 30.48 ? 391 ARG A CD 1 ATOM 3107 N NE . ARG A 1 391 ? 29.380 16.973 10.693 1.00 32.06 ? 391 ARG A NE 1 ATOM 3108 C CZ . ARG A 1 391 ? 29.067 17.265 9.438 1.00 32.19 ? 391 ARG A CZ 1 ATOM 3109 N NH1 . ARG A 1 391 ? 29.944 17.896 8.668 1.00 31.97 ? 391 ARG A NH1 1 ATOM 3110 N NH2 . ARG A 1 391 ? 27.871 16.947 8.963 1.00 29.74 ? 391 ARG A NH2 1 ATOM 3111 N N . VAL A 1 392 ? 30.874 14.489 15.363 1.00 27.71 ? 392 VAL A N 1 ATOM 3112 C CA . VAL A 1 392 ? 30.559 13.068 15.282 1.00 27.26 ? 392 VAL A CA 1 ATOM 3113 C C . VAL A 1 392 ? 29.377 12.798 14.346 1.00 28.11 ? 392 VAL A C 1 ATOM 3114 O O . VAL A 1 392 ? 28.259 13.262 14.596 1.00 29.85 ? 392 VAL A O 1 ATOM 3115 C CB . VAL A 1 392 ? 30.251 12.494 16.684 1.00 25.52 ? 392 VAL A CB 1 ATOM 3116 C CG1 . VAL A 1 392 ? 30.160 10.982 16.625 1.00 24.93 ? 392 VAL A CG1 1 ATOM 3117 C CG2 . VAL A 1 392 ? 31.335 12.911 17.662 1.00 25.46 ? 392 VAL A CG2 1 ATOM 3118 N N . PHE A 1 393 ? 29.628 12.047 13.271 1.00 26.09 ? 393 PHE A N 1 ATOM 3119 C CA . PHE A 1 393 ? 28.581 11.719 12.304 1.00 25.75 ? 393 PHE A CA 1 ATOM 3120 C C . PHE A 1 393 ? 27.481 10.856 12.899 1.00 25.35 ? 393 PHE A C 1 ATOM 3121 O O . PHE A 1 393 ? 27.753 9.906 13.634 1.00 23.98 ? 393 PHE A O 1 ATOM 3122 C CB . PHE A 1 393 ? 29.141 10.961 11.093 1.00 25.51 ? 393 PHE A CB 1 ATOM 3123 C CG . PHE A 1 393 ? 30.115 11.743 10.263 1.00 26.88 ? 393 PHE A CG 1 ATOM 3124 C CD1 . PHE A 1 393 ? 29.948 13.111 10.060 1.00 28.21 ? 393 PHE A CD1 1 ATOM 3125 C CD2 . PHE A 1 393 ? 31.177 11.098 9.637 1.00 25.99 ? 393 PHE A CD2 1 ATOM 3126 C CE1 . PHE A 1 393 ? 30.827 13.827 9.241 1.00 28.09 ? 393 PHE A CE1 1 ATOM 3127 C CE2 . PHE A 1 393 ? 32.057 11.799 8.820 1.00 27.47 ? 393 PHE A CE2 1 ATOM 3128 C CZ . PHE A 1 393 ? 31.881 13.168 8.621 1.00 27.66 ? 393 PHE A CZ 1 ATOM 3129 N N . ASN A 1 394 ? 26.238 11.194 12.558 1.00 25.75 ? 394 ASN A N 1 ATOM 3130 C CA . ASN A 1 394 ? 25.055 10.450 12.992 1.00 26.75 ? 394 ASN A CA 1 ATOM 3131 C C . ASN A 1 394 ? 24.875 10.315 14.491 1.00 26.02 ? 394 ASN A C 1 ATOM 3132 O O . ASN A 1 394 ? 24.438 9.273 14.983 1.00 26.03 ? 394 ASN A O 1 ATOM 3133 C CB . ASN A 1 394 ? 25.055 9.062 12.349 1.00 26.98 ? 394 ASN A CB 1 ATOM 3134 C CG . ASN A 1 394 ? 25.308 9.131 10.862 1.00 28.92 ? 394 ASN A CG 1 ATOM 3135 O OD1 . ASN A 1 394 ? 24.595 9.827 10.142 1.00 27.93 ? 394 ASN A OD1 1 ATOM 3136 N ND2 . ASN A 1 394 ? 26.338 8.423 10.394 1.00 27.41 ? 394 ASN A ND2 1 ATOM 3137 N N . GLY A 1 395 ? 25.215 11.377 15.208 1.00 25.86 ? 395 GLY A N 1 ATOM 3138 C CA . GLY A 1 395 ? 25.057 11.382 16.645 1.00 25.20 ? 395 GLY A CA 1 ATOM 3139 C C . GLY A 1 395 ? 24.135 12.521 17.035 1.00 25.11 ? 395 GLY A C 1 ATOM 3140 O O . GLY A 1 395 ? 24.181 13.612 16.451 1.00 24.02 ? 395 GLY A O 1 ATOM 3141 N N . GLY A 1 396 ? 23.270 12.265 18.006 1.00 24.46 ? 396 GLY A N 1 ATOM 3142 C CA . GLY A 1 396 ? 22.373 13.303 18.468 1.00 23.56 ? 396 GLY A CA 1 ATOM 3143 C C . GLY A 1 396 ? 22.994 13.951 19.688 1.00 22.89 ? 396 GLY A C 1 ATOM 3144 O O . GLY A 1 396 ? 24.211 13.953 19.850 1.00 22.39 ? 396 GLY A O 1 ATOM 3145 N N . HIS A 1 397 ? 22.152 14.490 20.558 1.00 23.71 ? 397 HIS A N 1 ATOM 3146 C CA . HIS A 1 397 ? 22.605 15.140 21.777 1.00 23.90 ? 397 HIS A CA 1 ATOM 3147 C C . HIS A 1 397 ? 23.441 14.188 22.634 1.00 24.65 ? 397 HIS A C 1 ATOM 3148 O O . HIS A 1 397 ? 24.419 14.595 23.251 1.00 24.75 ? 397 HIS A O 1 ATOM 3149 C CB . HIS A 1 397 ? 21.389 15.612 22.573 1.00 23.85 ? 397 HIS A CB 1 ATOM 3150 C CG . HIS A 1 397 ? 21.704 16.629 23.623 1.00 25.06 ? 397 HIS A CG 1 ATOM 3151 N ND1 . HIS A 1 397 ? 22.153 17.897 23.318 1.00 25.20 ? 397 HIS A ND1 1 ATOM 3152 C CD2 . HIS A 1 397 ? 21.601 16.579 24.971 1.00 23.90 ? 397 HIS A CD2 1 ATOM 3153 C CE1 . HIS A 1 397 ? 22.308 18.586 24.435 1.00 25.52 ? 397 HIS A CE1 1 ATOM 3154 N NE2 . HIS A 1 397 ? 21.980 17.810 25.452 1.00 25.69 ? 397 HIS A NE2 1 ATOM 3155 N N . MET A 1 398 ? 23.051 12.919 22.669 1.00 26.57 ? 398 MET A N 1 ATOM 3156 C CA . MET A 1 398 ? 23.761 11.925 23.465 1.00 29.18 ? 398 MET A CA 1 ATOM 3157 C C . MET A 1 398 ? 24.500 10.958 22.556 1.00 28.99 ? 398 MET A C 1 ATOM 3158 O O . MET A 1 398 ? 24.043 9.851 22.292 1.00 28.96 ? 398 MET A O 1 ATOM 3159 C CB . MET A 1 398 ? 22.769 11.169 24.348 1.00 32.68 ? 398 MET A CB 1 ATOM 3160 C CG . MET A 1 398 ? 21.855 12.089 25.132 1.00 38.39 ? 398 MET A CG 1 ATOM 3161 S SD . MET A 1 398 ? 20.396 11.256 25.763 1.00 46.84 ? 398 MET A SD 1 ATOM 3162 C CE . MET A 1 398 ? 20.957 10.787 27.386 1.00 46.78 ? 398 MET A CE 1 ATOM 3163 N N . VAL A 1 399 ? 25.655 11.401 22.083 1.00 29.98 ? 399 VAL A N 1 ATOM 3164 C CA . VAL A 1 399 ? 26.505 10.625 21.197 1.00 29.75 ? 399 VAL A CA 1 ATOM 3165 C C . VAL A 1 399 ? 26.620 9.113 21.468 1.00 29.51 ? 399 VAL A C 1 ATOM 3166 O O . VAL A 1 399 ? 26.277 8.307 20.605 1.00 28.78 ? 399 VAL A O 1 ATOM 3167 C CB . VAL A 1 399 ? 27.912 11.259 21.165 1.00 30.28 ? 399 VAL A CB 1 ATOM 3168 C CG1 . VAL A 1 399 ? 28.896 10.365 20.419 1.00 30.70 ? 399 VAL A CG1 1 ATOM 3169 C CG2 . VAL A 1 399 ? 27.825 12.619 20.501 1.00 29.77 ? 399 VAL A CG2 1 ATOM 3170 N N . PRO A 1 400 ? 27.074 8.709 22.671 1.00 29.45 ? 400 PRO A N 1 ATOM 3171 C CA . PRO A 1 400 ? 27.223 7.276 22.988 1.00 28.36 ? 400 PRO A CA 1 ATOM 3172 C C . PRO A 1 400 ? 25.980 6.421 22.734 1.00 28.89 ? 400 PRO A C 1 ATOM 3173 O O . PRO A 1 400 ? 26.077 5.244 22.383 1.00 29.65 ? 400 PRO A O 1 ATOM 3174 C CB . PRO A 1 400 ? 27.620 7.278 24.467 1.00 28.30 ? 400 PRO A CB 1 ATOM 3175 C CG . PRO A 1 400 ? 28.238 8.647 24.669 1.00 29.67 ? 400 PRO A CG 1 ATOM 3176 C CD . PRO A 1 400 ? 27.327 9.538 23.863 1.00 28.47 ? 400 PRO A CD 1 ATOM 3177 N N . PHE A 1 401 ? 24.811 7.015 22.930 1.00 27.33 ? 401 PHE A N 1 ATOM 3178 C CA . PHE A 1 401 ? 23.550 6.323 22.727 1.00 24.83 ? 401 PHE A CA 1 ATOM 3179 C C . PHE A 1 401 ? 23.295 6.050 21.236 1.00 25.28 ? 401 PHE A C 1 ATOM 3180 O O . PHE A 1 401 ? 22.705 5.035 20.880 1.00 25.01 ? 401 PHE A O 1 ATOM 3181 C CB . PHE A 1 401 ? 22.424 7.172 23.325 1.00 23.56 ? 401 PHE A CB 1 ATOM 3182 C CG . PHE A 1 401 ? 21.047 6.700 22.977 1.00 24.67 ? 401 PHE A CG 1 ATOM 3183 C CD1 . PHE A 1 401 ? 20.438 5.684 23.705 1.00 25.30 ? 401 PHE A CD1 1 ATOM 3184 C CD2 . PHE A 1 401 ? 20.352 7.275 21.913 1.00 24.93 ? 401 PHE A CD2 1 ATOM 3185 C CE1 . PHE A 1 401 ? 19.150 5.244 23.375 1.00 25.73 ? 401 PHE A CE1 1 ATOM 3186 C CE2 . PHE A 1 401 ? 19.072 6.844 21.576 1.00 23.92 ? 401 PHE A CE2 1 ATOM 3187 C CZ . PHE A 1 401 ? 18.469 5.827 22.308 1.00 23.47 ? 401 PHE A CZ 1 ATOM 3188 N N . ASP A 1 402 ? 23.750 6.943 20.362 1.00 25.64 ? 402 ASP A N 1 ATOM 3189 C CA . ASP A 1 402 ? 23.527 6.762 18.926 1.00 24.98 ? 402 ASP A CA 1 ATOM 3190 C C . ASP A 1 402 ? 24.614 5.978 18.211 1.00 23.71 ? 402 ASP A C 1 ATOM 3191 O O . ASP A 1 402 ? 24.327 5.229 17.283 1.00 23.51 ? 402 ASP A O 1 ATOM 3192 C CB . ASP A 1 402 ? 23.353 8.118 18.236 1.00 25.96 ? 402 ASP A CB 1 ATOM 3193 C CG . ASP A 1 402 ? 22.139 8.876 18.740 1.00 28.62 ? 402 ASP A CG 1 ATOM 3194 O OD1 . ASP A 1 402 ? 21.036 8.286 18.761 1.00 30.73 ? 402 ASP A OD1 1 ATOM 3195 O OD2 . ASP A 1 402 ? 22.282 10.060 19.109 1.00 28.21 ? 402 ASP A OD2 1 ATOM 3196 N N . VAL A 1 403 ? 25.860 6.174 18.635 1.00 22.34 ? 403 VAL A N 1 ATOM 3197 C CA . VAL A 1 403 ? 27.013 5.503 18.051 1.00 20.17 ? 403 VAL A CA 1 ATOM 3198 C C . VAL A 1 403 ? 27.929 5.070 19.188 1.00 22.53 ? 403 VAL A C 1 ATOM 3199 O O . VAL A 1 403 ? 28.989 5.650 19.423 1.00 21.37 ? 403 VAL A O 1 ATOM 3200 C CB . VAL A 1 403 ? 27.784 6.441 17.088 1.00 20.81 ? 403 VAL A CB 1 ATOM 3201 C CG1 . VAL A 1 403 ? 26.982 6.647 15.802 1.00 15.96 ? 403 VAL A CG1 1 ATOM 3202 C CG2 . VAL A 1 403 ? 28.066 7.790 17.776 1.00 18.77 ? 403 VAL A CG2 1 ATOM 3203 N N . PRO A 1 404 ? 27.527 4.024 19.912 1.00 23.95 ? 404 PRO A N 1 ATOM 3204 C CA . PRO A 1 404 ? 28.314 3.519 21.034 1.00 25.73 ? 404 PRO A CA 1 ATOM 3205 C C . PRO A 1 404 ? 29.744 3.097 20.718 1.00 27.53 ? 404 PRO A C 1 ATOM 3206 O O . PRO A 1 404 ? 30.650 3.388 21.498 1.00 29.09 ? 404 PRO A O 1 ATOM 3207 C CB . PRO A 1 404 ? 27.457 2.371 21.560 1.00 24.98 ? 404 PRO A CB 1 ATOM 3208 C CG . PRO A 1 404 ? 26.774 1.885 20.332 1.00 24.38 ? 404 PRO A CG 1 ATOM 3209 C CD . PRO A 1 404 ? 26.361 3.162 19.661 1.00 24.01 ? 404 PRO A CD 1 ATOM 3210 N N . GLU A 1 405 ? 29.951 2.416 19.592 1.00 27.57 ? 405 GLU A N 1 ATOM 3211 C CA . GLU A 1 405 ? 31.290 1.955 19.223 1.00 28.92 ? 405 GLU A CA 1 ATOM 3212 C C . GLU A 1 405 ? 32.222 3.093 18.821 1.00 29.26 ? 405 GLU A C 1 ATOM 3213 O O . GLU A 1 405 ? 33.382 3.141 19.234 1.00 28.55 ? 405 GLU A O 1 ATOM 3214 C CB . GLU A 1 405 ? 31.199 0.929 18.095 1.00 30.46 ? 405 GLU A CB 1 ATOM 3215 C CG . GLU A 1 405 ? 30.593 -0.382 18.546 1.00 37.26 ? 405 GLU A CG 1 ATOM 3216 C CD . GLU A 1 405 ? 30.356 -1.362 17.409 1.00 40.77 ? 405 GLU A CD 1 ATOM 3217 O OE1 . GLU A 1 405 ? 29.375 -1.179 16.656 1.00 42.67 ? 405 GLU A OE1 1 ATOM 3218 O OE2 . GLU A 1 405 ? 31.155 -2.316 17.267 1.00 43.31 ? 405 GLU A OE2 1 ATOM 3219 N N . ASN A 1 406 ? 31.716 4.016 18.014 1.00 28.61 ? 406 ASN A N 1 ATOM 3220 C CA . ASN A 1 406 ? 32.534 5.132 17.594 1.00 26.82 ? 406 ASN A CA 1 ATOM 3221 C C . ASN A 1 406 ? 32.837 6.009 18.799 1.00 27.14 ? 406 ASN A C 1 ATOM 3222 O O . ASN A 1 406 ? 33.940 6.541 18.926 1.00 29.83 ? 406 ASN A O 1 ATOM 3223 C CB . ASN A 1 406 ? 31.825 5.915 16.488 1.00 26.03 ? 406 ASN A CB 1 ATOM 3224 C CG . ASN A 1 406 ? 31.713 5.110 15.199 1.00 26.14 ? 406 ASN A CG 1 ATOM 3225 O OD1 . ASN A 1 406 ? 32.377 4.091 15.047 1.00 26.89 ? 406 ASN A OD1 1 ATOM 3226 N ND2 . ASN A 1 406 ? 30.887 5.567 14.269 1.00 25.20 ? 406 ASN A ND2 1 ATOM 3227 N N . ALA A 1 407 ? 31.866 6.134 19.696 1.00 25.77 ? 407 ALA A N 1 ATOM 3228 C CA . ALA A 1 407 ? 32.036 6.934 20.901 1.00 24.36 ? 407 ALA A CA 1 ATOM 3229 C C . ALA A 1 407 ? 33.136 6.354 21.783 1.00 25.23 ? 407 ALA A C 1 ATOM 3230 O O . ALA A 1 407 ? 33.943 7.102 22.348 1.00 26.06 ? 407 ALA A O 1 ATOM 3231 C CB . ALA A 1 407 ? 30.729 6.996 21.679 1.00 25.34 ? 407 ALA A CB 1 ATOM 3232 N N . LEU A 1 408 ? 33.173 5.028 21.911 1.00 23.58 ? 408 LEU A N 1 ATOM 3233 C CA . LEU A 1 408 ? 34.202 4.392 22.726 1.00 23.60 ? 408 LEU A CA 1 ATOM 3234 C C . LEU A 1 408 ? 35.566 4.583 22.064 1.00 25.68 ? 408 LEU A C 1 ATOM 3235 O O . LEU A 1 408 ? 36.585 4.726 22.741 1.00 25.01 ? 408 LEU A O 1 ATOM 3236 C CB . LEU A 1 408 ? 33.919 2.904 22.908 1.00 23.55 ? 408 LEU A CB 1 ATOM 3237 C CG . LEU A 1 408 ? 34.957 2.157 23.761 1.00 24.35 ? 408 LEU A CG 1 ATOM 3238 C CD1 . LEU A 1 408 ? 35.039 2.785 25.145 1.00 23.24 ? 408 LEU A CD1 1 ATOM 3239 C CD2 . LEU A 1 408 ? 34.583 0.683 23.867 1.00 22.13 ? 408 LEU A CD2 1 ATOM 3240 N N . SER A 1 409 ? 35.582 4.586 20.735 1.00 26.34 ? 409 SER A N 1 ATOM 3241 C CA . SER A 1 409 ? 36.824 4.791 20.008 1.00 28.28 ? 409 SER A CA 1 ATOM 3242 C C . SER A 1 409 ? 37.366 6.171 20.335 1.00 29.30 ? 409 SER A C 1 ATOM 3243 O O . SER A 1 409 ? 38.554 6.329 20.598 1.00 29.82 ? 409 SER A O 1 ATOM 3244 C CB . SER A 1 409 ? 36.591 4.711 18.504 1.00 29.61 ? 409 SER A CB 1 ATOM 3245 O OG . SER A 1 409 ? 36.285 3.396 18.105 1.00 32.02 ? 409 SER A OG 1 ATOM 3246 N N . MET A 1 410 ? 36.477 7.163 20.307 1.00 29.48 ? 410 MET A N 1 ATOM 3247 C CA . MET A 1 410 ? 36.826 8.550 20.582 1.00 28.98 ? 410 MET A CA 1 ATOM 3248 C C . MET A 1 410 ? 37.458 8.728 21.958 1.00 30.11 ? 410 MET A C 1 ATOM 3249 O O . MET A 1 410 ? 38.582 9.217 22.067 1.00 30.44 ? 410 MET A O 1 ATOM 3250 C CB . MET A 1 410 ? 35.582 9.437 20.474 1.00 28.35 ? 410 MET A CB 1 ATOM 3251 C CG . MET A 1 410 ? 35.852 10.919 20.707 1.00 27.98 ? 410 MET A CG 1 ATOM 3252 S SD . MET A 1 410 ? 34.358 11.859 21.087 1.00 30.76 ? 410 MET A SD 1 ATOM 3253 C CE . MET A 1 410 ? 33.917 11.141 22.679 1.00 28.60 ? 410 MET A CE 1 ATOM 3254 N N . VAL A 1 411 ? 36.749 8.330 23.011 1.00 31.33 ? 411 VAL A N 1 ATOM 3255 C CA . VAL A 1 411 ? 37.285 8.487 24.362 1.00 33.29 ? 411 VAL A CA 1 ATOM 3256 C C . VAL A 1 411 ? 38.605 7.724 24.573 1.00 33.44 ? 411 VAL A C 1 ATOM 3257 O O . VAL A 1 411 ? 39.527 8.247 25.198 1.00 33.64 ? 411 VAL A O 1 ATOM 3258 C CB . VAL A 1 411 ? 36.235 8.069 25.448 1.00 34.73 ? 411 VAL A CB 1 ATOM 3259 C CG1 . VAL A 1 411 ? 35.858 6.597 25.292 1.00 35.80 ? 411 VAL A CG1 1 ATOM 3260 C CG2 . VAL A 1 411 ? 36.787 8.340 26.846 1.00 32.40 ? 411 VAL A CG2 1 ATOM 3261 N N . ASN A 1 412 ? 38.710 6.508 24.040 1.00 33.40 ? 412 ASN A N 1 ATOM 3262 C CA . ASN A 1 412 ? 39.943 5.727 24.198 1.00 34.49 ? 412 ASN A CA 1 ATOM 3263 C C . ASN A 1 412 ? 41.136 6.306 23.436 1.00 34.58 ? 412 ASN A C 1 ATOM 3264 O O . ASN A 1 412 ? 42.252 6.324 23.956 1.00 33.29 ? 412 ASN A O 1 ATOM 3265 C CB . ASN A 1 412 ? 39.722 4.268 23.788 1.00 32.13 ? 412 ASN A CB 1 ATOM 3266 C CG . ASN A 1 412 ? 39.116 3.432 24.901 1.00 32.04 ? 412 ASN A CG 1 ATOM 3267 O OD1 . ASN A 1 412 ? 38.685 2.306 24.677 1.00 32.69 ? 412 ASN A OD1 1 ATOM 3268 N ND2 . ASN A 1 412 ? 39.090 3.977 26.110 1.00 31.76 ? 412 ASN A ND2 1 ATOM 3269 N N . GLU A 1 413 ? 40.913 6.779 22.213 1.00 35.19 ? 413 GLU A N 1 ATOM 3270 C CA . GLU A 1 413 ? 42.004 7.372 21.437 1.00 37.52 ? 413 GLU A CA 1 ATOM 3271 C C . GLU A 1 413 ? 42.469 8.643 22.142 1.00 37.54 ? 413 GLU A C 1 ATOM 3272 O O . GLU A 1 413 ? 43.608 9.074 21.996 1.00 37.72 ? 413 GLU A O 1 ATOM 3273 C CB . GLU A 1 413 ? 41.551 7.708 20.008 1.00 37.65 ? 413 GLU A CB 1 ATOM 3274 C CG . GLU A 1 413 ? 40.977 6.507 19.242 1.00 42.69 ? 413 GLU A CG 1 ATOM 3275 C CD . GLU A 1 413 ? 40.629 6.829 17.793 1.00 45.86 ? 413 GLU A CD 1 ATOM 3276 O OE1 . GLU A 1 413 ? 39.968 5.985 17.139 1.00 44.72 ? 413 GLU A OE1 1 ATOM 3277 O OE2 . GLU A 1 413 ? 41.024 7.922 17.313 1.00 47.67 ? 413 GLU A OE2 1 ATOM 3278 N N . TRP A 1 414 ? 41.578 9.237 22.924 1.00 37.83 ? 414 TRP A N 1 ATOM 3279 C CA . TRP A 1 414 ? 41.907 10.455 23.645 1.00 37.03 ? 414 TRP A CA 1 ATOM 3280 C C . TRP A 1 414 ? 42.610 10.131 24.950 1.00 37.66 ? 414 TRP A C 1 ATOM 3281 O O . TRP A 1 414 ? 43.699 10.622 25.225 1.00 38.11 ? 414 TRP A O 1 ATOM 3282 C CB . TRP A 1 414 ? 40.632 11.247 23.934 1.00 35.10 ? 414 TRP A CB 1 ATOM 3283 C CG . TRP A 1 414 ? 40.878 12.535 24.665 1.00 31.91 ? 414 TRP A CG 1 ATOM 3284 C CD1 . TRP A 1 414 ? 40.751 12.761 26.010 1.00 28.64 ? 414 TRP A CD1 1 ATOM 3285 C CD2 . TRP A 1 414 ? 41.267 13.782 24.084 1.00 27.66 ? 414 TRP A CD2 1 ATOM 3286 N NE1 . TRP A 1 414 ? 41.031 14.073 26.296 1.00 25.85 ? 414 TRP A NE1 1 ATOM 3287 C CE2 . TRP A 1 414 ? 41.351 14.723 25.133 1.00 25.78 ? 414 TRP A CE2 1 ATOM 3288 C CE3 . TRP A 1 414 ? 41.551 14.196 22.774 1.00 26.70 ? 414 TRP A CE3 1 ATOM 3289 C CZ2 . TRP A 1 414 ? 41.707 16.056 24.915 1.00 24.01 ? 414 TRP A CZ2 1 ATOM 3290 C CZ3 . TRP A 1 414 ? 41.906 15.524 22.557 1.00 25.08 ? 414 TRP A CZ3 1 ATOM 3291 C CH2 . TRP A 1 414 ? 41.980 16.436 23.625 1.00 24.34 ? 414 TRP A CH2 1 ATOM 3292 N N . ILE A 1 415 ? 41.966 9.295 25.748 1.00 38.13 ? 415 ILE A N 1 ATOM 3293 C CA . ILE A 1 415 ? 42.488 8.896 27.038 1.00 39.59 ? 415 ILE A CA 1 ATOM 3294 C C . ILE A 1 415 ? 43.772 8.067 26.937 1.00 40.04 ? 415 ILE A C 1 ATOM 3295 O O . ILE A 1 415 ? 44.652 8.183 27.780 1.00 39.81 ? 415 ILE A O 1 ATOM 3296 C CB . ILE A 1 415 ? 41.368 8.133 27.829 1.00 40.96 ? 415 ILE A CB 1 ATOM 3297 C CG1 . ILE A 1 415 ? 40.876 9.014 28.966 1.00 40.95 ? 415 ILE A CG1 1 ATOM 3298 C CG2 . ILE A 1 415 ? 41.850 6.788 28.352 1.00 41.39 ? 415 ILE A CG2 1 ATOM 3299 C CD1 . ILE A 1 415 ? 40.355 10.340 28.493 1.00 44.03 ? 415 ILE A CD1 1 ATOM 3300 N N . HIS A 1 416 ? 43.881 7.242 25.902 1.00 41.10 ? 416 HIS A N 1 ATOM 3301 C CA . HIS A 1 416 ? 45.054 6.393 25.724 1.00 41.64 ? 416 HIS A CA 1 ATOM 3302 C C . HIS A 1 416 ? 45.927 6.821 24.547 1.00 42.96 ? 416 HIS A C 1 ATOM 3303 O O . HIS A 1 416 ? 47.064 6.371 24.422 1.00 44.06 ? 416 HIS A O 1 ATOM 3304 C CB . HIS A 1 416 ? 44.629 4.934 25.510 1.00 41.16 ? 416 HIS A CB 1 ATOM 3305 C CG . HIS A 1 416 ? 43.997 4.296 26.709 1.00 41.92 ? 416 HIS A CG 1 ATOM 3306 N ND1 . HIS A 1 416 ? 44.652 4.161 27.915 1.00 41.19 ? 416 HIS A ND1 1 ATOM 3307 C CD2 . HIS A 1 416 ? 42.778 3.728 26.879 1.00 42.02 ? 416 HIS A CD2 1 ATOM 3308 C CE1 . HIS A 1 416 ? 43.866 3.536 28.775 1.00 40.26 ? 416 HIS A CE1 1 ATOM 3309 N NE2 . HIS A 1 416 ? 42.723 3.262 28.171 1.00 41.40 ? 416 HIS A NE2 1 ATOM 3310 N N . GLY A 1 417 ? 45.402 7.687 23.686 1.00 43.21 ? 417 GLY A N 1 ATOM 3311 C CA . GLY A 1 417 ? 46.169 8.115 22.530 1.00 43.91 ? 417 GLY A CA 1 ATOM 3312 C C . GLY A 1 417 ? 46.870 9.454 22.651 1.00 44.86 ? 417 GLY A C 1 ATOM 3313 O O . GLY A 1 417 ? 47.058 10.150 21.652 1.00 45.29 ? 417 GLY A O 1 ATOM 3314 N N . GLY A 1 418 ? 47.251 9.826 23.866 1.00 45.01 ? 418 GLY A N 1 ATOM 3315 C CA . GLY A 1 418 ? 47.945 11.083 24.058 1.00 46.49 ? 418 GLY A CA 1 ATOM 3316 C C . GLY A 1 418 ? 47.166 12.352 23.764 1.00 49.03 ? 418 GLY A C 1 ATOM 3317 O O . GLY A 1 418 ? 47.728 13.317 23.252 1.00 49.97 ? 418 GLY A O 1 ATOM 3318 N N . PHE A 1 419 ? 45.874 12.354 24.077 1.00 50.47 ? 419 PHE A N 1 ATOM 3319 C CA . PHE A 1 419 ? 45.025 13.532 23.882 1.00 50.91 ? 419 PHE A CA 1 ATOM 3320 C C . PHE A 1 419 ? 45.121 14.155 22.503 1.00 52.11 ? 419 PHE A C 1 ATOM 3321 O O . PHE A 1 419 ? 45.303 15.365 22.373 1.00 52.75 ? 419 PHE A O 1 ATOM 3322 C CB . PHE A 1 419 ? 45.374 14.577 24.936 1.00 48.49 ? 419 PHE A CB 1 ATOM 3323 C CG . PHE A 1 419 ? 45.730 13.975 26.249 1.00 48.24 ? 419 PHE A CG 1 ATOM 3324 C CD1 . PHE A 1 419 ? 44.805 13.205 26.941 1.00 46.54 ? 419 PHE A CD1 1 ATOM 3325 C CD2 . PHE A 1 419 ? 47.019 14.095 26.754 1.00 47.06 ? 419 PHE A CD2 1 ATOM 3326 C CE1 . PHE A 1 419 ? 45.161 12.558 28.112 1.00 47.12 ? 419 PHE A CE1 1 ATOM 3327 C CE2 . PHE A 1 419 ? 47.385 13.450 27.928 1.00 45.42 ? 419 PHE A CE2 1 ATOM 3328 C CZ . PHE A 1 419 ? 46.456 12.680 28.607 1.00 45.58 ? 419 PHE A CZ 1 ATOM 3329 N N . SER A 1 420 ? 44.992 13.325 21.475 1.00 53.51 ? 420 SER A N 1 ATOM 3330 C CA . SER A 1 420 ? 45.051 13.807 20.107 1.00 54.65 ? 420 SER A CA 1 ATOM 3331 C C . SER A 1 420 ? 44.328 12.852 19.171 1.00 55.29 ? 420 SER A C 1 ATOM 3332 O O . SER A 1 420 ? 44.704 11.686 19.049 1.00 54.84 ? 420 SER A O 1 ATOM 3333 C CB . SER A 1 420 ? 46.503 13.951 19.664 1.00 55.13 ? 420 SER A CB 1 ATOM 3334 O OG . SER A 1 420 ? 46.570 14.485 18.354 1.00 59.45 ? 420 SER A OG 1 ATOM 3335 N N . LEU A 1 421 ? 43.288 13.352 18.514 1.00 55.28 ? 421 LEU A N 1 ATOM 3336 C CA . LEU A 1 421 ? 42.528 12.539 17.577 1.00 56.66 ? 421 LEU A CA 1 ATOM 3337 C C . LEU A 1 421 ? 43.070 12.743 16.170 1.00 57.95 ? 421 LEU A C 1 ATOM 3338 O O . LEU A 1 421 ? 43.078 11.764 15.386 1.00 58.73 ? 421 LEU A O 1 ATOM 3339 C CB . LEU A 1 421 ? 41.043 12.906 17.614 1.00 54.91 ? 421 LEU A CB 1 ATOM 3340 C CG . LEU A 1 421 ? 40.311 12.685 18.936 1.00 53.94 ? 421 LEU A CG 1 ATOM 3341 C CD1 . LEU A 1 421 ? 38.825 12.890 18.714 1.00 55.19 ? 421 LEU A CD1 1 ATOM 3342 C CD2 . LEU A 1 421 ? 40.575 11.290 19.455 1.00 53.80 ? 421 LEU A CD2 1 ATOM 3343 O OXT . LEU A 1 421 ? 43.467 13.891 15.873 1.00 59.06 ? 421 LEU A OXT 1 HETATM 3344 C C . ACE B 2 1 ? 16.554 20.344 30.251 1.00 32.78 ? 500 ACE B C 1 HETATM 3345 O O . ACE B 2 1 ? 15.694 21.171 30.541 1.00 31.40 ? 500 ACE B O 1 HETATM 3346 C CH3 . ACE B 2 1 ? 16.621 19.021 30.969 1.00 33.55 ? 500 ACE B CH3 1 ATOM 3347 N N . MET B 2 2 ? 17.467 20.550 29.307 1.00 32.98 ? 501 MET B N 1 ATOM 3348 C CA . MET B 2 2 ? 17.505 21.791 28.546 1.00 35.04 ? 501 MET B CA 1 ATOM 3349 C C . MET B 2 2 ? 16.203 21.978 27.785 1.00 36.34 ? 501 MET B C 1 ATOM 3350 O O . MET B 2 2 ? 15.873 23.069 27.330 1.00 37.22 ? 501 MET B O 1 ATOM 3351 C CB . MET B 2 2 ? 18.698 21.784 27.587 1.00 34.41 ? 501 MET B CB 1 ATOM 3352 C CG . MET B 2 2 ? 20.028 22.037 28.291 1.00 36.16 ? 501 MET B CG 1 ATOM 3353 S SD . MET B 2 2 ? 21.420 22.187 27.156 1.00 36.88 ? 501 MET B SD 1 ATOM 3354 C CE . MET B 2 2 ? 20.957 23.667 26.262 1.00 37.38 ? 501 MET B CE 1 ATOM 3355 N N . ASN B 2 3 ? 15.462 20.891 27.662 1.00 37.68 ? 502 ASN B N 1 ATOM 3356 C CA . ASN B 2 3 ? 14.185 20.901 26.983 1.00 38.33 ? 502 ASN B CA 1 ATOM 3357 C C . ASN B 2 3 ? 13.205 21.799 27.753 1.00 37.81 ? 502 ASN B C 1 ATOM 3358 O O . ASN B 2 3 ? 12.386 22.487 27.158 1.00 37.38 ? 502 ASN B O 1 ATOM 3359 C CB . ASN B 2 3 ? 13.657 19.465 26.930 1.00 42.53 ? 502 ASN B CB 1 ATOM 3360 C CG . ASN B 2 3 ? 12.476 19.299 25.997 1.00 47.51 ? 502 ASN B CG 1 ATOM 3361 O OD1 . ASN B 2 3 ? 12.089 20.374 25.312 1.00 50.52 ? 502 ASN B OD1 1 ATOM 3362 N ND2 . ASN B 2 3 ? 11.918 18.208 25.890 1.00 50.60 ? 502 ASN B ND2 1 ATOM 3363 N N . GLN B 2 4 ? 13.311 21.799 29.079 1.00 37.05 ? 503 GLN B N 1 ATOM 3364 C CA . GLN B 2 4 ? 12.413 22.572 29.932 1.00 36.33 ? 503 GLN B CA 1 ATOM 3365 C C . GLN B 2 4 ? 12.737 24.047 30.076 1.00 36.86 ? 503 GLN B C 1 ATOM 3366 O O . GLN B 2 4 ? 11.966 24.788 30.687 1.00 37.84 ? 503 GLN B O 1 ATOM 3367 C CB . GLN B 2 4 ? 12.365 21.959 31.331 1.00 37.63 ? 503 GLN B CB 1 ATOM 3368 C CG . GLN B 2 4 ? 11.989 20.499 31.357 1.00 39.28 ? 503 GLN B CG 1 ATOM 3369 C CD . GLN B 2 4 ? 10.668 20.238 30.682 1.00 41.90 ? 503 GLN B CD 1 ATOM 3370 O OE1 . GLN B 2 4 ? 9.657 20.850 31.020 1.00 43.45 ? 503 GLN B OE1 1 ATOM 3371 N NE2 . GLN B 2 4 ? 10.664 19.323 29.716 1.00 44.45 ? 503 GLN B NE2 1 ATOM 3372 N N . ALA B 2 5 ? 13.866 24.481 29.525 1.00 35.83 ? 504 ALA B N 1 ATOM 3373 C CA . ALA B 2 5 ? 14.266 25.880 29.634 1.00 34.05 ? 504 ALA B CA 1 ATOM 3374 C C . ALA B 2 5 ? 13.804 26.769 28.480 1.00 34.33 ? 504 ALA B C 1 ATOM 3375 O O . ALA B 2 5 ? 14.255 27.909 28.366 1.00 35.11 ? 504 ALA B O 1 ATOM 3376 C CB . ALA B 2 5 ? 15.777 25.971 29.774 1.00 32.86 ? 504 ALA B CB 1 ATOM 3377 N N . ILE B 2 6 ? 12.910 26.269 27.632 1.00 33.46 ? 505 ILE B N 1 ATOM 3378 C CA . ILE B 2 6 ? 12.437 27.061 26.501 1.00 34.47 ? 505 ILE B CA 1 ATOM 3379 C C . ILE B 2 6 ? 11.299 28.018 26.860 1.00 34.56 ? 505 ILE B C 1 ATOM 3380 O O . ILE B 2 6 ? 11.389 29.224 26.626 1.00 36.20 ? 505 ILE B O 1 ATOM 3381 C CB . ILE B 2 6 ? 11.921 26.176 25.341 1.00 35.76 ? 505 ILE B CB 1 ATOM 3382 C CG1 . ILE B 2 6 ? 12.904 25.041 25.039 1.00 36.25 ? 505 ILE B CG1 1 ATOM 3383 C CG2 . ILE B 2 6 ? 11.723 27.034 24.101 1.00 36.14 ? 505 ILE B CG2 1 ATOM 3384 C CD1 . ILE B 2 6 ? 14.274 25.502 24.674 1.00 37.69 ? 505 ILE B CD1 1 ATOM 3385 N N . ASP B 2 7 ? 10.231 27.469 27.430 1.00 33.79 ? 506 ASP B N 1 ATOM 3386 C CA . ASP B 2 7 ? 9.046 28.235 27.792 1.00 32.20 ? 506 ASP B CA 1 ATOM 3387 C C . ASP B 2 7 ? 9.022 28.691 29.254 1.00 33.65 ? 506 ASP B C 1 ATOM 3388 O O . ASP B 2 7 ? 8.617 27.932 30.134 1.00 34.97 ? 506 ASP B O 1 ATOM 3389 C CB . ASP B 2 7 ? 7.820 27.376 27.516 1.00 31.44 ? 506 ASP B CB 1 ATOM 3390 C CG . ASP B 2 7 ? 6.538 28.164 27.535 1.00 35.25 ? 506 ASP B CG 1 ATOM 3391 O OD1 . ASP B 2 7 ? 6.522 29.296 28.069 1.00 35.66 ? 506 ASP B OD1 1 ATOM 3392 O OD2 . ASP B 2 7 ? 5.532 27.637 27.013 1.00 39.05 ? 506 ASP B OD2 1 ATOM 3393 N N . PHE B 2 8 ? 9.429 29.928 29.521 1.00 33.35 ? 507 PHE B N 1 ATOM 3394 C CA . PHE B 2 8 ? 9.427 30.421 30.893 1.00 33.07 ? 507 PHE B CA 1 ATOM 3395 C C . PHE B 2 8 ? 8.049 30.488 31.520 1.00 33.52 ? 507 PHE B C 1 ATOM 3396 O O . PHE B 2 8 ? 7.920 30.548 32.745 1.00 33.47 ? 507 PHE B O 1 ATOM 3397 C CB . PHE B 2 8 ? 10.077 31.794 30.983 1.00 33.83 ? 507 PHE B CB 1 ATOM 3398 C CG . PHE B 2 8 ? 11.538 31.736 31.265 1.00 36.25 ? 507 PHE B CG 1 ATOM 3399 C CD1 . PHE B 2 8 ? 12.428 31.289 30.293 1.00 37.54 ? 507 PHE B CD1 1 ATOM 3400 C CD2 . PHE B 2 8 ? 12.026 32.092 32.515 1.00 37.05 ? 507 PHE B CD2 1 ATOM 3401 C CE1 . PHE B 2 8 ? 13.789 31.193 30.561 1.00 37.88 ? 507 PHE B CE1 1 ATOM 3402 C CE2 . PHE B 2 8 ? 13.381 32.002 32.798 1.00 39.83 ? 507 PHE B CE2 1 ATOM 3403 C CZ . PHE B 2 8 ? 14.269 31.549 31.813 1.00 39.66 ? 507 PHE B CZ 1 ATOM 3404 N N . ALA B 2 9 ? 7.017 30.476 30.686 1.00 33.88 ? 508 ALA B N 1 ATOM 3405 C CA . ALA B 2 9 ? 5.659 30.531 31.195 1.00 34.82 ? 508 ALA B CA 1 ATOM 3406 C C . ALA B 2 9 ? 5.310 29.179 31.788 1.00 35.90 ? 508 ALA B C 1 ATOM 3407 O O . ALA B 2 9 ? 4.907 29.082 32.955 1.00 37.08 ? 508 ALA B O 1 ATOM 3408 C CB . ALA B 2 9 ? 4.689 30.876 30.083 1.00 34.98 ? 508 ALA B CB 1 ATOM 3409 N N . GLN B 2 10 ? 5.478 28.129 30.990 1.00 35.18 ? 509 GLN B N 1 ATOM 3410 C CA . GLN B 2 10 ? 5.161 26.796 31.470 1.00 34.96 ? 509 GLN B CA 1 ATOM 3411 C C . GLN B 2 10 ? 6.025 26.458 32.674 1.00 34.96 ? 509 GLN B C 1 ATOM 3412 O O . GLN B 2 10 ? 5.555 25.857 33.645 1.00 34.77 ? 509 GLN B O 1 ATOM 3413 C CB . GLN B 2 10 ? 5.366 25.757 30.370 1.00 35.66 ? 509 GLN B CB 1 ATOM 3414 C CG . GLN B 2 10 ? 5.037 24.354 30.834 1.00 43.13 ? 509 GLN B CG 1 ATOM 3415 C CD . GLN B 2 10 ? 3.655 24.265 31.489 1.00 49.26 ? 509 GLN B CD 1 ATOM 3416 O OE1 . GLN B 2 10 ? 3.421 23.423 32.367 1.00 49.14 ? 509 GLN B OE1 1 ATOM 3417 N NE2 . GLN B 2 10 ? 2.732 25.130 31.057 1.00 49.05 ? 509 GLN B NE2 1 ATOM 3418 N N . ALA B 2 11 ? 7.289 26.861 32.615 1.00 33.12 ? 510 ALA B N 1 ATOM 3419 C CA . ALA B 2 11 ? 8.209 26.596 33.704 1.00 32.80 ? 510 ALA B CA 1 ATOM 3420 C C . ALA B 2 11 ? 7.679 27.214 34.994 1.00 33.82 ? 510 ALA B C 1 ATOM 3421 O O . ALA B 2 11 ? 7.771 26.611 36.062 1.00 32.45 ? 510 ALA B O 1 ATOM 3422 C CB . ALA B 2 11 ? 9.578 27.158 33.374 1.00 32.23 ? 510 ALA B CB 1 ATOM 3423 N N . SER B 2 12 ? 7.121 28.418 34.892 1.00 34.01 ? 511 SER B N 1 ATOM 3424 C CA . SER B 2 12 ? 6.585 29.103 36.063 1.00 34.28 ? 511 SER B CA 1 ATOM 3425 C C . SER B 2 12 ? 5.381 28.368 36.631 1.00 34.56 ? 511 SER B C 1 ATOM 3426 O O . SER B 2 12 ? 5.295 28.157 37.841 1.00 33.07 ? 511 SER B O 1 ATOM 3427 C CB . SER B 2 12 ? 6.179 30.539 35.714 1.00 34.43 ? 511 SER B CB 1 ATOM 3428 O OG . SER B 2 12 ? 7.312 31.354 35.482 1.00 35.62 ? 511 SER B OG 1 ATOM 3429 N N . ILE B 2 13 ? 4.455 27.985 35.753 1.00 34.51 ? 512 ILE B N 1 ATOM 3430 C CA . ILE B 2 13 ? 3.250 27.288 36.179 1.00 35.66 ? 512 ILE B CA 1 ATOM 3431 C C . ILE B 2 13 ? 3.632 26.011 36.913 1.00 35.93 ? 512 ILE B C 1 ATOM 3432 O O . ILE B 2 13 ? 3.125 25.735 37.999 1.00 36.49 ? 512 ILE B O 1 ATOM 3433 C CB . ILE B 2 13 ? 2.344 26.897 34.977 1.00 39.00 ? 512 ILE B CB 1 ATOM 3434 C CG1 . ILE B 2 13 ? 2.034 28.120 34.110 1.00 39.40 ? 512 ILE B CG1 1 ATOM 3435 C CG2 . ILE B 2 13 ? 1.038 26.290 35.489 1.00 35.45 ? 512 ILE B CG2 1 ATOM 3436 C CD1 . ILE B 2 13 ? 1.155 29.139 34.790 1.00 43.16 ? 512 ILE B CD1 1 ATOM 3437 N N . ASP B 2 14 ? 4.529 25.233 36.312 1.00 35.13 ? 513 ASP B N 1 ATOM 3438 C CA . ASP B 2 14 ? 4.962 23.982 36.912 1.00 34.44 ? 513 ASP B CA 1 ATOM 3439 C C . ASP B 2 14 ? 5.480 24.172 38.326 1.00 33.80 ? 513 ASP B C 1 ATOM 3440 O O . ASP B 2 14 ? 5.149 23.394 39.222 1.00 33.93 ? 513 ASP B O 1 ATOM 3441 C CB . ASP B 2 14 ? 6.026 23.313 36.044 1.00 35.58 ? 513 ASP B CB 1 ATOM 3442 C CG . ASP B 2 14 ? 5.461 22.814 34.725 1.00 38.51 ? 513 ASP B CG 1 ATOM 3443 O OD1 . ASP B 2 14 ? 4.217 22.732 34.611 1.00 39.98 ? 513 ASP B OD1 1 ATOM 3444 O OD2 . ASP B 2 14 ? 6.249 22.495 33.807 1.00 40.22 ? 513 ASP B OD2 1 ATOM 3445 N N . SER B 2 15 ? 6.279 25.209 38.533 1.00 32.67 ? 514 SER B N 1 ATOM 3446 C CA . SER B 2 15 ? 6.810 25.483 39.856 1.00 33.13 ? 514 SER B CA 1 ATOM 3447 C C . SER B 2 15 ? 5.678 25.824 40.838 1.00 34.23 ? 514 SER B C 1 ATOM 3448 O O . SER B 2 15 ? 5.607 25.252 41.927 1.00 34.56 ? 514 SER B O 1 ATOM 3449 C CB . SER B 2 15 ? 7.819 26.632 39.789 1.00 32.23 ? 514 SER B CB 1 ATOM 3450 O OG . SER B 2 15 ? 8.457 26.836 41.041 1.00 33.41 ? 514 SER B OG 1 ATOM 3451 N N . TYR B 2 16 ? 4.795 26.744 40.448 1.00 35.00 ? 515 TYR B N 1 ATOM 3452 C CA . TYR B 2 16 ? 3.674 27.162 41.297 1.00 35.36 ? 515 TYR B CA 1 ATOM 3453 C C . TYR B 2 16 ? 2.828 25.972 41.715 1.00 35.43 ? 515 TYR B C 1 ATOM 3454 O O . TYR B 2 16 ? 2.341 25.913 42.844 1.00 34.42 ? 515 TYR B O 1 ATOM 3455 C CB . TYR B 2 16 ? 2.762 28.143 40.560 1.00 37.27 ? 515 TYR B CB 1 ATOM 3456 C CG . TYR B 2 16 ? 3.406 29.434 40.110 1.00 39.98 ? 515 TYR B CG 1 ATOM 3457 C CD1 . TYR B 2 16 ? 2.962 30.073 38.945 1.00 40.69 ? 515 TYR B CD1 1 ATOM 3458 C CD2 . TYR B 2 16 ? 4.443 30.027 40.837 1.00 40.34 ? 515 TYR B CD2 1 ATOM 3459 C CE1 . TYR B 2 16 ? 3.530 31.267 38.502 1.00 40.91 ? 515 TYR B CE1 1 ATOM 3460 C CE2 . TYR B 2 16 ? 5.023 31.230 40.406 1.00 43.03 ? 515 TYR B CE2 1 ATOM 3461 C CZ . TYR B 2 16 ? 4.558 31.842 39.231 1.00 42.88 ? 515 TYR B CZ 1 ATOM 3462 O OH . TYR B 2 16 ? 5.116 33.014 38.772 1.00 41.10 ? 515 TYR B OH 1 ATOM 3463 N N . LYS B 2 17 ? 2.637 25.038 40.790 1.00 35.99 ? 516 LYS B N 1 ATOM 3464 C CA . LYS B 2 17 ? 1.844 23.847 41.059 1.00 37.92 ? 516 LYS B CA 1 ATOM 3465 C C . LYS B 2 17 ? 2.519 22.928 42.054 1.00 37.39 ? 516 LYS B C 1 ATOM 3466 O O . LYS B 2 17 ? 1.969 22.621 43.109 1.00 36.95 ? 516 LYS B O 1 ATOM 3467 C CB . LYS B 2 17 ? 1.591 23.068 39.771 1.00 39.88 ? 516 LYS B CB 1 ATOM 3468 C CG . LYS B 2 17 ? 0.641 23.751 38.809 1.00 45.51 ? 516 LYS B CG 1 ATOM 3469 C CD . LYS B 2 17 ? 0.423 22.904 37.565 1.00 50.66 ? 516 LYS B CD 1 ATOM 3470 C CE . LYS B 2 17 ? -0.074 21.512 37.926 1.00 52.83 ? 516 LYS B CE 1 ATOM 3471 N NZ . LYS B 2 17 ? -0.260 20.667 36.711 1.00 57.20 ? 516 LYS B NZ 1 ATOM 3472 N N . LYS B 2 18 ? 3.724 22.495 41.710 1.00 38.25 ? 517 LYS B N 1 ATOM 3473 C CA . LYS B 2 18 ? 4.476 21.584 42.559 1.00 38.32 ? 517 LYS B CA 1 ATOM 3474 C C . LYS B 2 18 ? 4.620 22.065 44.000 1.00 37.27 ? 517 LYS B C 1 ATOM 3475 O O . LYS B 2 18 ? 4.660 21.253 44.924 1.00 36.36 ? 517 LYS B O 1 ATOM 3476 C CB . LYS B 2 18 ? 5.859 21.335 41.952 1.00 39.40 ? 517 LYS B CB 1 ATOM 3477 C CG . LYS B 2 18 ? 6.696 20.327 42.713 1.00 42.61 ? 517 LYS B CG 1 ATOM 3478 C CD . LYS B 2 18 ? 8.058 20.166 42.078 1.00 46.79 ? 517 LYS B CD 1 ATOM 3479 C CE . LYS B 2 18 ? 8.962 19.298 42.930 1.00 48.65 ? 517 LYS B CE 1 ATOM 3480 N NZ . LYS B 2 18 ? 10.319 19.169 42.322 1.00 51.18 ? 517 LYS B NZ 1 ATOM 3481 N N . HIS B 2 19 ? 4.683 23.379 44.193 1.00 36.31 ? 518 HIS B N 1 ATOM 3482 C CA . HIS B 2 19 ? 4.845 23.939 45.530 1.00 36.23 ? 518 HIS B CA 1 ATOM 3483 C C . HIS B 2 19 ? 3.576 24.564 46.105 1.00 36.71 ? 518 HIS B C 1 ATOM 3484 O O . HIS B 2 19 ? 3.643 25.387 47.019 1.00 37.20 ? 518 HIS B O 1 ATOM 3485 C CB . HIS B 2 19 ? 5.989 24.953 45.514 1.00 35.00 ? 518 HIS B CB 1 ATOM 3486 C CG . HIS B 2 19 ? 7.286 24.371 45.044 1.00 37.03 ? 518 HIS B CG 1 ATOM 3487 N ND1 . HIS B 2 19 ? 8.118 23.644 45.868 1.00 38.17 ? 518 HIS B ND1 1 ATOM 3488 C CD2 . HIS B 2 19 ? 7.856 24.341 43.816 1.00 37.96 ? 518 HIS B CD2 1 ATOM 3489 C CE1 . HIS B 2 19 ? 9.143 23.190 45.168 1.00 36.40 ? 518 HIS B CE1 1 ATOM 3490 N NE2 . HIS B 2 19 ? 9.007 23.598 43.920 1.00 36.80 ? 518 HIS B NE2 1 ATOM 3491 N N . GLY B 2 20 ? 2.427 24.157 45.568 1.00 36.68 ? 519 GLY B N 1 ATOM 3492 C CA . GLY B 2 20 ? 1.141 24.650 46.040 1.00 38.32 ? 519 GLY B CA 1 ATOM 3493 C C . GLY B 2 20 ? 0.925 26.154 46.137 1.00 40.97 ? 519 GLY B C 1 ATOM 3494 O O . GLY B 2 20 ? 0.120 26.613 46.950 1.00 40.28 ? 519 GLY B O 1 ATOM 3495 N N . ILE B 2 21 ? 1.623 26.927 45.311 1.00 41.97 ? 520 ILE B N 1 ATOM 3496 C CA . ILE B 2 21 ? 1.479 28.378 45.332 1.00 42.29 ? 520 ILE B CA 1 ATOM 3497 C C . ILE B 2 21 ? 0.143 28.808 44.717 1.00 43.83 ? 520 ILE B C 1 ATOM 3498 O O . ILE B 2 21 ? -0.412 29.840 45.089 1.00 43.47 ? 520 ILE B O 1 ATOM 3499 C CB . ILE B 2 21 ? 2.622 29.060 44.550 1.00 42.53 ? 520 ILE B CB 1 ATOM 3500 C CG1 . ILE B 2 21 ? 3.981 28.652 45.132 1.00 41.30 ? 520 ILE B CG1 1 ATOM 3501 C CG2 . ILE B 2 21 ? 2.445 30.568 44.584 1.00 41.57 ? 520 ILE B CG2 1 ATOM 3502 C CD1 . ILE B 2 21 ? 4.241 29.154 46.526 1.00 39.83 ? 520 ILE B CD1 1 ATOM 3503 N N . LEU B 2 22 ? -0.371 28.013 43.780 1.00 45.10 ? 521 LEU B N 1 ATOM 3504 C CA . LEU B 2 22 ? -1.637 28.328 43.119 1.00 47.76 ? 521 LEU B CA 1 ATOM 3505 C C . LEU B 2 22 ? -2.863 28.076 43.995 1.00 50.16 ? 521 LEU B C 1 ATOM 3506 O O . LEU B 2 22 ? -3.904 28.698 43.802 1.00 51.60 ? 521 LEU B O 1 ATOM 3507 C CB . LEU B 2 22 ? -1.790 27.517 41.826 1.00 45.79 ? 521 LEU B CB 1 ATOM 3508 C CG . LEU B 2 22 ? -0.801 27.753 40.683 1.00 45.77 ? 521 LEU B CG 1 ATOM 3509 C CD1 . LEU B 2 22 ? -1.156 26.859 39.506 1.00 43.65 ? 521 LEU B CD1 1 ATOM 3510 C CD2 . LEU B 2 22 ? -0.840 29.208 40.268 1.00 45.63 ? 521 LEU B CD2 1 ATOM 3511 N N . GLU B 2 23 ? -2.740 27.167 44.956 1.00 52.06 ? 522 GLU B N 1 ATOM 3512 C CA . GLU B 2 23 ? -3.858 26.828 45.823 1.00 53.80 ? 522 GLU B CA 1 ATOM 3513 C C . GLU B 2 23 ? -3.770 27.432 47.211 1.00 53.12 ? 522 GLU B C 1 ATOM 3514 O O . GLU B 2 23 ? -4.769 27.894 47.753 1.00 54.77 ? 522 GLU B O 1 ATOM 3515 C CB . GLU B 2 23 ? -3.991 25.306 45.937 1.00 58.00 ? 522 GLU B CB 1 ATOM 3516 C CG . GLU B 2 23 ? -2.719 24.551 45.586 1.00 65.03 ? 522 GLU B CG 1 ATOM 3517 C CD . GLU B 2 23 ? -2.447 24.544 44.084 1.00 69.17 ? 522 GLU B CD 1 ATOM 3518 O OE1 . GLU B 2 23 ? -1.257 24.497 43.679 1.00 68.25 ? 522 GLU B OE1 1 ATOM 3519 O OE2 . GLU B 2 23 ? -3.435 24.576 43.313 1.00 71.06 ? 522 GLU B OE2 1 ATOM 3520 N N . ASP B 2 24 ? -2.580 27.433 47.792 1.00 51.33 ? 523 ASP B N 1 ATOM 3521 C CA . ASP B 2 24 ? -2.416 27.982 49.129 1.00 50.03 ? 523 ASP B CA 1 ATOM 3522 C C . ASP B 2 24 ? -2.400 29.500 49.158 1.00 49.62 ? 523 ASP B C 1 ATOM 3523 O O . ASP B 2 24 ? -2.876 30.107 50.116 1.00 50.15 ? 523 ASP B O 1 ATOM 3524 C CB . ASP B 2 24 ? -1.114 27.489 49.749 1.00 49.91 ? 523 ASP B CB 1 ATOM 3525 C CG . ASP B 2 24 ? -1.012 25.996 49.756 1.00 51.11 ? 523 ASP B CG 1 ATOM 3526 O OD1 . ASP B 2 24 ? 0.044 25.475 50.176 1.00 51.25 ? 523 ASP B OD1 1 ATOM 3527 O OD2 . ASP B 2 24 ? -1.991 25.344 49.338 1.00 52.14 ? 523 ASP B OD2 1 ATOM 3528 N N . VAL B 2 25 ? -1.857 30.114 48.111 1.00 48.25 ? 524 VAL B N 1 ATOM 3529 C CA . VAL B 2 25 ? -1.733 31.561 48.083 1.00 46.84 ? 524 VAL B CA 1 ATOM 3530 C C . VAL B 2 25 ? -2.557 32.311 47.048 1.00 47.52 ? 524 VAL B C 1 ATOM 3531 O O . VAL B 2 25 ? -3.374 33.157 47.403 1.00 49.19 ? 524 VAL B O 1 ATOM 3532 C CB . VAL B 2 25 ? -0.259 31.953 47.911 1.00 45.74 ? 524 VAL B CB 1 ATOM 3533 C CG1 . VAL B 2 25 ? -0.082 33.434 48.150 1.00 46.05 ? 524 VAL B CG1 1 ATOM 3534 C CG2 . VAL B 2 25 ? 0.599 31.155 48.874 1.00 44.73 ? 524 VAL B CG2 1 ATOM 3535 N N . ILE B 2 26 ? -2.339 32.010 45.774 1.00 47.87 ? 525 ILE B N 1 ATOM 3536 C CA . ILE B 2 26 ? -3.047 32.684 44.689 1.00 47.11 ? 525 ILE B CA 1 ATOM 3537 C C . ILE B 2 26 ? -4.519 32.290 44.562 1.00 48.47 ? 525 ILE B C 1 ATOM 3538 O O . ILE B 2 26 ? -5.337 33.073 44.083 1.00 48.78 ? 525 ILE B O 1 ATOM 3539 C CB . ILE B 2 26 ? -2.328 32.429 43.347 1.00 44.99 ? 525 ILE B CB 1 ATOM 3540 C CG1 . ILE B 2 26 ? -0.915 33.017 43.409 1.00 44.61 ? 525 ILE B CG1 1 ATOM 3541 C CG2 . ILE B 2 26 ? -3.111 33.041 42.204 1.00 44.69 ? 525 ILE B CG2 1 ATOM 3542 C CD1 . ILE B 2 26 ? -0.055 32.712 42.203 1.00 43.80 ? 525 ILE B CD1 1 ATOM 3543 N N . HIS B 2 27 ? -4.851 31.080 44.996 1.00 49.58 ? 526 HIS B N 1 ATOM 3544 C CA . HIS B 2 27 ? -6.222 30.580 44.928 1.00 50.69 ? 526 HIS B CA 1 ATOM 3545 C C . HIS B 2 27 ? -6.812 30.576 43.517 1.00 51.99 ? 526 HIS B C 1 ATOM 3546 O O . HIS B 2 27 ? -8.018 30.747 43.341 1.00 53.28 ? 526 HIS B O 1 ATOM 3547 C CB . HIS B 2 27 ? -7.141 31.382 45.858 1.00 49.23 ? 526 HIS B CB 1 ATOM 3548 C CG . HIS B 2 27 ? -6.888 31.143 47.313 1.00 48.58 ? 526 HIS B CG 1 ATOM 3549 N ND1 . HIS B 2 27 ? -6.189 32.029 48.104 1.00 48.91 ? 526 HIS B ND1 1 ATOM 3550 C CD2 . HIS B 2 27 ? -7.227 30.108 48.117 1.00 48.51 ? 526 HIS B CD2 1 ATOM 3551 C CE1 . HIS B 2 27 ? -6.109 31.552 49.334 1.00 49.03 ? 526 HIS B CE1 1 ATOM 3552 N NE2 . HIS B 2 27 ? -6.731 30.387 49.369 1.00 50.41 ? 526 HIS B NE2 1 ATOM 3553 N N . ASP B 2 28 ? -5.966 30.384 42.513 1.00 52.46 ? 527 ASP B N 1 ATOM 3554 C CA . ASP B 2 28 ? -6.432 30.333 41.136 1.00 53.39 ? 527 ASP B CA 1 ATOM 3555 C C . ASP B 2 28 ? -5.521 29.418 40.336 1.00 54.30 ? 527 ASP B C 1 ATOM 3556 O O . ASP B 2 28 ? -4.400 29.792 39.993 1.00 55.87 ? 527 ASP B O 1 ATOM 3557 C CB . ASP B 2 28 ? -6.433 31.724 40.512 1.00 54.47 ? 527 ASP B CB 1 ATOM 3558 C CG . ASP B 2 28 ? -6.929 31.711 39.079 1.00 56.42 ? 527 ASP B CG 1 ATOM 3559 O OD1 . ASP B 2 28 ? -7.024 32.796 38.468 1.00 56.89 ? 527 ASP B OD1 1 ATOM 3560 O OD2 . ASP B 2 28 ? -7.225 30.609 38.565 1.00 55.80 ? 527 ASP B OD2 1 ATOM 3561 N N . THR B 2 29 ? -6.009 28.220 40.033 1.00 53.60 ? 528 THR B N 1 ATOM 3562 C CA . THR B 2 29 ? -5.224 27.242 39.294 1.00 53.23 ? 528 THR B CA 1 ATOM 3563 C C . THR B 2 29 ? -5.172 27.495 37.792 1.00 53.54 ? 528 THR B C 1 ATOM 3564 O O . THR B 2 29 ? -4.536 26.742 37.054 1.00 53.87 ? 528 THR B O 1 ATOM 3565 C CB . THR B 2 29 ? -5.764 25.830 39.522 1.00 53.84 ? 528 THR B CB 1 ATOM 3566 O OG1 . THR B 2 29 ? -7.104 25.750 39.024 1.00 56.11 ? 528 THR B OG1 1 ATOM 3567 C CG2 . THR B 2 29 ? -5.761 25.495 41.002 1.00 54.05 ? 528 THR B CG2 1 ATOM 3568 N N . SER B 2 30 ? -5.838 28.548 37.334 1.00 53.13 ? 529 SER B N 1 ATOM 3569 C CA . SER B 2 30 ? -5.835 28.869 35.911 1.00 52.21 ? 529 SER B CA 1 ATOM 3570 C C . SER B 2 30 ? -4.905 30.053 35.651 1.00 51.01 ? 529 SER B C 1 ATOM 3571 O O . SER B 2 30 ? -4.683 30.448 34.503 1.00 51.00 ? 529 SER B O 1 ATOM 3572 C CB . SER B 2 30 ? -7.250 29.215 35.437 1.00 53.62 ? 529 SER B CB 1 ATOM 3573 O OG . SER B 2 30 ? -7.666 30.472 35.953 1.00 56.69 ? 529 SER B OG 1 ATOM 3574 N N . PHE B 2 31 ? -4.364 30.614 36.726 1.00 48.75 ? 530 PHE B N 1 ATOM 3575 C CA . PHE B 2 31 ? -3.465 31.754 36.616 1.00 47.64 ? 530 PHE B CA 1 ATOM 3576 C C . PHE B 2 31 ? -2.378 31.582 35.549 1.00 47.77 ? 530 PHE B C 1 ATOM 3577 O O . PHE B 2 31 ? -1.714 30.543 35.469 1.00 46.67 ? 530 PHE B O 1 ATOM 3578 C CB . PHE B 2 31 ? -2.814 32.041 37.972 1.00 44.90 ? 530 PHE B CB 1 ATOM 3579 C CG . PHE B 2 31 ? -1.684 33.024 37.903 1.00 41.80 ? 530 PHE B CG 1 ATOM 3580 C CD1 . PHE B 2 31 ? -0.393 32.641 38.253 1.00 40.31 ? 530 PHE B CD1 1 ATOM 3581 C CD2 . PHE B 2 31 ? -1.905 34.333 37.478 1.00 40.61 ? 530 PHE B CD2 1 ATOM 3582 C CE1 . PHE B 2 31 ? 0.661 33.546 38.179 1.00 39.91 ? 530 PHE B CE1 1 ATOM 3583 C CE2 . PHE B 2 31 ? -0.859 35.250 37.400 1.00 38.37 ? 530 PHE B CE2 1 ATOM 3584 C CZ . PHE B 2 31 ? 0.426 34.857 37.751 1.00 39.58 ? 530 PHE B CZ 1 ATOM 3585 N N . GLN B 2 32 ? -2.217 32.619 34.732 1.00 47.49 ? 531 GLN B N 1 ATOM 3586 C CA . GLN B 2 32 ? -1.220 32.646 33.671 1.00 46.78 ? 531 GLN B CA 1 ATOM 3587 C C . GLN B 2 32 ? -0.360 33.877 33.888 1.00 44.48 ? 531 GLN B C 1 ATOM 3588 O O . GLN B 2 32 ? -0.870 34.991 33.923 1.00 43.94 ? 531 GLN B O 1 ATOM 3589 C CB . GLN B 2 32 ? -1.887 32.759 32.297 1.00 50.51 ? 531 GLN B CB 1 ATOM 3590 C CG . GLN B 2 32 ? -2.652 31.528 31.846 1.00 56.35 ? 531 GLN B CG 1 ATOM 3591 C CD . GLN B 2 32 ? -1.739 30.361 31.532 1.00 59.72 ? 531 GLN B CD 1 ATOM 3592 O OE1 . GLN B 2 32 ? -0.984 29.904 32.392 1.00 63.02 ? 531 GLN B OE1 1 ATOM 3593 N NE2 . GLN B 2 32 ? -1.801 29.872 30.296 1.00 60.59 ? 531 GLN B NE2 1 ATOM 3594 N N . PRO B 2 33 ? 0.955 33.695 34.052 1.00 42.92 ? 532 PRO B N 1 ATOM 3595 C CA . PRO B 2 33 ? 1.846 34.842 34.260 1.00 41.30 ? 532 PRO B CA 1 ATOM 3596 C C . PRO B 2 33 ? 1.964 35.658 32.971 1.00 39.08 ? 532 PRO B C 1 ATOM 3597 O O . PRO B 2 33 ? 2.000 35.091 31.880 1.00 37.97 ? 532 PRO B O 1 ATOM 3598 C CB . PRO B 2 33 ? 3.177 34.188 34.639 1.00 42.01 ? 532 PRO B CB 1 ATOM 3599 C CG . PRO B 2 33 ? 2.767 32.853 35.200 1.00 43.45 ? 532 PRO B CG 1 ATOM 3600 C CD . PRO B 2 33 ? 1.668 32.427 34.272 1.00 43.12 ? 532 PRO B CD 1 ATOM 3601 N N . SER B 2 34 ? 2.022 36.981 33.097 1.00 37.33 ? 533 SER B N 1 ATOM 3602 C CA . SER B 2 34 ? 2.145 37.847 31.930 1.00 37.14 ? 533 SER B CA 1 ATOM 3603 C C . SER B 2 34 ? 3.596 38.202 31.703 1.00 37.25 ? 533 SER B C 1 ATOM 3604 O O . SER B 2 34 ? 3.973 38.668 30.631 1.00 39.55 ? 533 SER B O 1 ATOM 3605 C CB . SER B 2 34 ? 1.332 39.122 32.116 1.00 36.57 ? 533 SER B CB 1 ATOM 3606 O OG . SER B 2 34 ? -0.049 38.828 32.113 1.00 38.05 ? 533 SER B OG 1 ATOM 3607 N N . GLY B 2 35 ? 4.406 37.979 32.728 1.00 36.78 ? 534 GLY B N 1 ATOM 3608 C CA . GLY B 2 35 ? 5.824 38.262 32.638 1.00 36.01 ? 534 GLY B CA 1 ATOM 3609 C C . GLY B 2 35 ? 6.502 37.507 33.757 1.00 35.07 ? 534 GLY B C 1 ATOM 3610 O O . GLY B 2 35 ? 5.896 36.613 34.347 1.00 36.09 ? 534 GLY B O 1 ATOM 3611 N N . ILE B 2 36 ? 7.753 37.834 34.050 1.00 32.96 ? 535 ILE B N 1 ATOM 3612 C CA . ILE B 2 36 ? 8.427 37.157 35.138 1.00 32.41 ? 535 ILE B CA 1 ATOM 3613 C C . ILE B 2 36 ? 9.041 38.196 36.060 1.00 30.98 ? 535 ILE B C 1 ATOM 3614 O O . ILE B 2 36 ? 9.554 39.221 35.612 1.00 30.23 ? 535 ILE B O 1 ATOM 3615 C CB . ILE B 2 36 ? 9.507 36.155 34.624 1.00 33.75 ? 535 ILE B CB 1 ATOM 3616 C CG1 . ILE B 2 36 ? 10.791 36.889 34.278 1.00 32.90 ? 535 ILE B CG1 1 ATOM 3617 C CG2 . ILE B 2 36 ? 8.976 35.360 33.433 1.00 32.14 ? 535 ILE B CG2 1 ATOM 3618 C CD1 . ILE B 2 36 ? 11.794 36.827 35.404 1.00 34.90 ? 535 ILE B CD1 1 ATOM 3619 N N . LEU B 2 37 ? 8.970 37.927 37.358 1.00 30.82 ? 536 LEU B N 1 ATOM 3620 C CA . LEU B 2 37 ? 9.492 38.842 38.362 1.00 30.00 ? 536 LEU B CA 1 ATOM 3621 C C . LEU B 2 37 ? 10.857 38.419 38.891 1.00 31.02 ? 536 LEU B C 1 ATOM 3622 O O . LEU B 2 37 ? 10.974 37.422 39.606 1.00 31.91 ? 536 LEU B O 1 ATOM 3623 C CB . LEU B 2 37 ? 8.505 38.937 39.528 1.00 27.42 ? 536 LEU B CB 1 ATOM 3624 C CG . LEU B 2 37 ? 8.789 39.973 40.619 1.00 26.89 ? 536 LEU B CG 1 ATOM 3625 C CD1 . LEU B 2 37 ? 8.684 41.390 40.064 1.00 22.91 ? 536 LEU B CD1 1 ATOM 3626 C CD2 . LEU B 2 37 ? 7.783 39.775 41.737 1.00 28.65 ? 536 LEU B CD2 1 ATOM 3627 N N . ALA B 2 38 ? 11.892 39.172 38.538 1.00 30.28 ? 537 ALA B N 1 ATOM 3628 C CA . ALA B 2 38 ? 13.227 38.862 39.022 1.00 30.50 ? 537 ALA B CA 1 ATOM 3629 C C . ALA B 2 38 ? 13.397 39.618 40.328 1.00 31.39 ? 537 ALA B C 1 ATOM 3630 O O . ALA B 2 38 ? 13.170 40.820 40.396 1.00 31.76 ? 537 ALA B O 1 ATOM 3631 C CB . ALA B 2 38 ? 14.274 39.301 38.022 1.00 29.66 ? 537 ALA B CB 1 ATOM 3632 N N . VAL B 2 39 ? 13.781 38.897 41.370 1.00 33.07 ? 538 VAL B N 1 ATOM 3633 C CA . VAL B 2 39 ? 13.973 39.486 42.683 1.00 33.70 ? 538 VAL B CA 1 ATOM 3634 C C . VAL B 2 39 ? 15.340 39.054 43.188 1.00 36.01 ? 538 VAL B C 1 ATOM 3635 O O . VAL B 2 39 ? 15.755 37.916 42.977 1.00 35.30 ? 538 VAL B O 1 ATOM 3636 C CB . VAL B 2 39 ? 12.883 38.996 43.662 1.00 33.81 ? 538 VAL B CB 1 ATOM 3637 C CG1 . VAL B 2 39 ? 13.003 39.720 45.001 1.00 32.22 ? 538 VAL B CG1 1 ATOM 3638 C CG2 . VAL B 2 39 ? 11.498 39.211 43.042 1.00 34.53 ? 538 VAL B CG2 1 ATOM 3639 N N . GLU B 2 40 ? 16.037 39.966 43.856 1.00 39.25 ? 539 GLU B N 1 ATOM 3640 C CA . GLU B 2 40 ? 17.362 39.675 44.384 1.00 40.93 ? 539 GLU B CA 1 ATOM 3641 C C . GLU B 2 40 ? 17.697 40.502 45.622 1.00 40.99 ? 539 GLU B C 1 ATOM 3642 O O . GLU B 2 40 ? 17.355 41.680 45.703 1.00 42.63 ? 539 GLU B O 1 ATOM 3643 C CB . GLU B 2 40 ? 18.406 39.942 43.307 1.00 42.28 ? 539 GLU B CB 1 ATOM 3644 C CG . GLU B 2 40 ? 19.818 39.703 43.762 1.00 47.77 ? 539 GLU B CG 1 ATOM 3645 C CD . GLU B 2 40 ? 20.826 40.194 42.755 1.00 51.33 ? 539 GLU B CD 1 ATOM 3646 O OE1 . GLU B 2 40 ? 20.845 41.417 42.489 1.00 52.80 ? 539 GLU B OE1 1 ATOM 3647 O OE2 . GLU B 2 40 ? 21.592 39.357 42.228 1.00 53.88 ? 539 GLU B OE2 1 ATOM 3648 N N . TYR B 2 41 ? 18.366 39.879 46.586 1.00 40.69 ? 540 TYR B N 1 ATOM 3649 C CA . TYR B 2 41 ? 18.768 40.564 47.808 1.00 39.19 ? 540 TYR B CA 1 ATOM 3650 C C . TYR B 2 41 ? 20.187 41.057 47.614 1.00 40.25 ? 540 TYR B C 1 ATOM 3651 O O . TYR B 2 41 ? 20.543 42.151 48.049 1.00 41.02 ? 540 TYR B O 1 ATOM 3652 C CB . TYR B 2 41 ? 18.700 39.611 48.993 1.00 36.36 ? 540 TYR B CB 1 ATOM 3653 C CG . TYR B 2 41 ? 17.292 39.352 49.461 1.00 35.94 ? 540 TYR B CG 1 ATOM 3654 C CD1 . TYR B 2 41 ? 16.629 40.271 50.274 1.00 35.46 ? 540 TYR B CD1 1 ATOM 3655 C CD2 . TYR B 2 41 ? 16.607 38.202 49.070 1.00 35.18 ? 540 TYR B CD2 1 ATOM 3656 C CE1 . TYR B 2 41 ? 15.316 40.049 50.690 1.00 34.13 ? 540 TYR B CE1 1 ATOM 3657 C CE2 . TYR B 2 41 ? 15.296 37.973 49.478 1.00 33.60 ? 540 TYR B CE2 1 ATOM 3658 C CZ . TYR B 2 41 ? 14.660 38.899 50.287 1.00 32.95 ? 540 TYR B CZ 1 ATOM 3659 O OH . TYR B 2 41 ? 13.375 38.670 50.697 1.00 30.93 ? 540 TYR B OH 1 ATOM 3660 N N . SER B 2 42 ? 20.989 40.232 46.953 1.00 41.74 ? 541 SER B N 1 ATOM 3661 C CA . SER B 2 42 ? 22.381 40.553 46.650 1.00 44.36 ? 541 SER B CA 1 ATOM 3662 C C . SER B 2 42 ? 22.847 39.588 45.565 1.00 44.75 ? 541 SER B C 1 ATOM 3663 O O . SER B 2 42 ? 22.228 38.545 45.349 1.00 44.87 ? 541 SER B O 1 ATOM 3664 C CB . SER B 2 42 ? 23.263 40.412 47.894 1.00 43.04 ? 541 SER B CB 1 ATOM 3665 O OG . SER B 2 42 ? 23.310 39.069 48.333 1.00 45.24 ? 541 SER B OG 1 ATOM 3666 N N . SER B 2 43 ? 23.934 39.935 44.886 1.00 45.34 ? 542 SER B N 1 ATOM 3667 C CA . SER B 2 43 ? 24.452 39.100 43.810 1.00 46.18 ? 542 SER B CA 1 ATOM 3668 C C . SER B 2 43 ? 24.533 37.624 44.193 1.00 46.10 ? 542 SER B C 1 ATOM 3669 O O . SER B 2 43 ? 24.511 36.746 43.325 1.00 46.38 ? 542 SER B O 1 ATOM 3670 C CB . SER B 2 43 ? 25.831 39.603 43.362 1.00 46.42 ? 542 SER B CB 1 ATOM 3671 O OG . SER B 2 43 ? 26.791 39.487 44.396 1.00 49.42 ? 542 SER B OG 1 ATOM 3672 N N . SER B 2 44 ? 24.610 37.348 45.490 1.00 44.54 ? 543 SER B N 1 ATOM 3673 C CA . SER B 2 44 ? 24.698 35.972 45.951 1.00 45.17 ? 543 SER B CA 1 ATOM 3674 C C . SER B 2 44 ? 23.382 35.490 46.547 1.00 45.83 ? 543 SER B C 1 ATOM 3675 O O . SER B 2 44 ? 23.277 34.341 46.992 1.00 47.08 ? 543 SER B O 1 ATOM 3676 C CB . SER B 2 44 ? 25.798 35.841 47.005 1.00 45.41 ? 543 SER B CB 1 ATOM 3677 O OG . SER B 2 44 ? 25.436 36.522 48.198 1.00 48.50 ? 543 SER B OG 1 ATOM 3678 N N . ALA B 2 45 ? 22.379 36.364 46.560 1.00 44.62 ? 544 ALA B N 1 ATOM 3679 C CA . ALA B 2 45 ? 21.088 36.009 47.129 1.00 42.19 ? 544 ALA B CA 1 ATOM 3680 C C . ALA B 2 45 ? 19.924 36.318 46.203 1.00 41.54 ? 544 ALA B C 1 ATOM 3681 O O . ALA B 2 45 ? 19.126 37.218 46.465 1.00 41.49 ? 544 ALA B O 1 ATOM 3682 C CB . ALA B 2 45 ? 20.896 36.723 48.457 1.00 42.43 ? 544 ALA B CB 1 ATOM 3683 N N . PRO B 2 46 ? 19.817 35.579 45.091 1.00 40.22 ? 545 PRO B N 1 ATOM 3684 C CA . PRO B 2 46 ? 18.710 35.825 44.166 1.00 37.38 ? 545 PRO B CA 1 ATOM 3685 C C . PRO B 2 46 ? 17.567 34.915 44.574 1.00 35.25 ? 545 PRO B C 1 ATOM 3686 O O . PRO B 2 46 ? 17.800 33.837 45.114 1.00 34.57 ? 545 PRO B O 1 ATOM 3687 C CB . PRO B 2 46 ? 19.294 35.406 42.827 1.00 37.64 ? 545 PRO B CB 1 ATOM 3688 C CG . PRO B 2 46 ? 20.092 34.190 43.217 1.00 37.47 ? 545 PRO B CG 1 ATOM 3689 C CD . PRO B 2 46 ? 20.783 34.624 44.513 1.00 37.86 ? 545 PRO B CD 1 ATOM 3690 N N . VAL B 2 47 ? 16.334 35.346 44.361 1.00 33.89 ? 546 VAL B N 1 ATOM 3691 C CA . VAL B 2 47 ? 15.222 34.470 44.676 1.00 33.36 ? 546 VAL B CA 1 ATOM 3692 C C . VAL B 2 47 ? 14.938 33.880 43.299 1.00 31.49 ? 546 VAL B C 1 ATOM 3693 O O . VAL B 2 47 ? 14.577 34.601 42.370 1.00 32.14 ? 546 VAL B O 1 ATOM 3694 C CB . VAL B 2 47 ? 14.013 35.256 45.289 1.00 33.82 ? 546 VAL B CB 1 ATOM 3695 C CG1 . VAL B 2 47 ? 14.384 36.711 45.444 1.00 34.67 ? 546 VAL B CG1 1 ATOM 3696 C CG2 . VAL B 2 47 ? 12.746 35.070 44.458 1.00 33.31 ? 546 VAL B CG2 1 ATOM 3697 N N . ALA B 2 48 ? 15.148 32.573 43.166 1.00 29.13 ? 547 ALA B N 1 ATOM 3698 C CA . ALA B 2 48 ? 14.983 31.903 41.889 1.00 29.84 ? 547 ALA B CA 1 ATOM 3699 C C . ALA B 2 48 ? 13.959 30.775 41.828 1.00 30.56 ? 547 ALA B C 1 ATOM 3700 O O . ALA B 2 48 ? 14.309 29.623 41.552 1.00 32.08 ? 547 ALA B O 1 ATOM 3701 C CB . ALA B 2 48 ? 16.339 31.388 41.421 1.00 29.75 ? 547 ALA B CB 1 ATOM 3702 N N . MET B 2 49 ? 12.695 31.104 42.058 1.00 29.54 ? 548 MET B N 1 ATOM 3703 C CA . MET B 2 49 ? 11.635 30.107 41.999 1.00 30.52 ? 548 MET B CA 1 ATOM 3704 C C . MET B 2 49 ? 11.905 28.863 42.840 1.00 31.19 ? 548 MET B C 1 ATOM 3705 O O . MET B 2 49 ? 12.134 27.780 42.297 1.00 32.11 ? 548 MET B O 1 ATOM 3706 C CB . MET B 2 49 ? 11.391 29.679 40.545 1.00 29.37 ? 548 MET B CB 1 ATOM 3707 C CG . MET B 2 49 ? 10.879 30.787 39.629 1.00 32.23 ? 548 MET B CG 1 ATOM 3708 S SD . MET B 2 49 ? 9.170 31.320 39.955 1.00 31.25 ? 548 MET B SD 1 ATOM 3709 C CE . MET B 2 49 ? 8.286 29.992 39.206 1.00 32.22 ? 548 MET B CE 1 ATOM 3710 N N . GLY B 2 50 ? 11.902 29.014 44.161 1.00 31.08 ? 549 GLY B N 1 ATOM 3711 C CA . GLY B 2 50 ? 12.093 27.855 45.017 1.00 30.90 ? 549 GLY B CA 1 ATOM 3712 C C . GLY B 2 50 ? 13.440 27.555 45.649 1.00 29.40 ? 549 GLY B C 1 ATOM 3713 O O . GLY B 2 50 ? 13.550 26.586 46.393 1.00 29.01 ? 549 GLY B O 1 ATOM 3714 N N . ASN B 2 51 ? 14.467 28.345 45.368 1.00 28.44 ? 550 ASN B N 1 ATOM 3715 C CA . ASN B 2 51 ? 15.755 28.078 45.982 1.00 28.74 ? 550 ASN B CA 1 ATOM 3716 C C . ASN B 2 51 ? 15.685 28.431 47.470 1.00 31.17 ? 550 ASN B C 1 ATOM 3717 O O . ASN B 2 51 ? 14.735 29.067 47.926 1.00 31.30 ? 550 ASN B O 1 ATOM 3718 C CB . ASN B 2 51 ? 16.852 28.879 45.285 1.00 27.79 ? 550 ASN B CB 1 ATOM 3719 C CG . ASN B 2 51 ? 16.639 30.369 45.385 1.00 29.54 ? 550 ASN B CG 1 ATOM 3720 O OD1 . ASN B 2 51 ? 15.529 30.868 45.182 1.00 29.21 ? 550 ASN B OD1 1 ATOM 3721 N ND2 . ASN B 2 51 ? 17.708 31.096 45.683 1.00 29.02 ? 550 ASN B ND2 1 ATOM 3722 N N . THR B 2 52 ? 16.677 27.991 48.233 1.00 33.09 ? 551 THR B N 1 ATOM 3723 C CA . THR B 2 52 ? 16.712 28.264 49.662 1.00 34.18 ? 551 THR B CA 1 ATOM 3724 C C . THR B 2 52 ? 17.712 29.380 49.921 1.00 35.19 ? 551 THR B C 1 ATOM 3725 O O . THR B 2 52 ? 18.773 29.425 49.313 1.00 35.21 ? 551 THR B O 1 ATOM 3726 C CB . THR B 2 52 ? 17.121 26.997 50.469 1.00 33.61 ? 551 THR B CB 1 ATOM 3727 O OG1 . THR B 2 52 ? 16.084 26.012 50.373 1.00 35.32 ? 551 THR B OG1 1 ATOM 3728 C CG2 . THR B 2 52 ? 17.330 27.332 51.925 1.00 33.76 ? 551 THR B CG2 1 ATOM 3729 N N . LEU B 2 53 ? 17.358 30.295 50.813 1.00 36.83 ? 552 LEU B N 1 ATOM 3730 C CA . LEU B 2 53 ? 18.239 31.399 51.141 1.00 38.64 ? 552 LEU B CA 1 ATOM 3731 C C . LEU B 2 53 ? 18.428 31.486 52.641 1.00 40.75 ? 552 LEU B C 1 ATOM 3732 O O . LEU B 2 53 ? 17.480 31.297 53.410 1.00 39.59 ? 552 LEU B O 1 ATOM 3733 C CB . LEU B 2 53 ? 17.663 32.726 50.641 1.00 38.65 ? 552 LEU B CB 1 ATOM 3734 C CG . LEU B 2 53 ? 17.765 33.049 49.156 1.00 39.73 ? 552 LEU B CG 1 ATOM 3735 C CD1 . LEU B 2 53 ? 17.060 34.364 48.871 1.00 41.33 ? 552 LEU B CD1 1 ATOM 3736 C CD2 . LEU B 2 53 ? 19.227 33.139 48.761 1.00 42.13 ? 552 LEU B CD2 1 ATOM 3737 N N . PRO B 2 54 ? 19.666 31.749 53.084 1.00 42.50 ? 553 PRO B N 1 ATOM 3738 C CA . PRO B 2 54 ? 19.890 31.856 54.522 1.00 43.78 ? 553 PRO B CA 1 ATOM 3739 C C . PRO B 2 54 ? 19.195 33.122 55.016 1.00 45.50 ? 553 PRO B C 1 ATOM 3740 O O . PRO B 2 54 ? 19.364 34.204 54.451 1.00 45.36 ? 553 PRO B O 1 ATOM 3741 C CB . PRO B 2 54 ? 21.410 31.924 54.629 1.00 42.92 ? 553 PRO B CB 1 ATOM 3742 C CG . PRO B 2 54 ? 21.808 32.575 53.350 1.00 43.81 ? 553 PRO B CG 1 ATOM 3743 C CD . PRO B 2 54 ? 20.932 31.883 52.342 1.00 42.35 ? 553 PRO B CD 1 ATOM 3744 N N . THR B 2 55 ? 18.394 32.962 56.060 1.00 47.23 ? 554 THR B N 1 ATOM 3745 C CA . THR B 2 55 ? 17.643 34.056 56.656 1.00 48.34 ? 554 THR B CA 1 ATOM 3746 C C . THR B 2 55 ? 18.343 35.412 56.715 1.00 48.53 ? 554 THR B C 1 ATOM 3747 O O . THR B 2 55 ? 17.761 36.423 56.333 1.00 48.56 ? 554 THR B O 1 ATOM 3748 C CB . THR B 2 55 ? 17.195 33.662 58.070 1.00 49.15 ? 554 THR B CB 1 ATOM 3749 O OG1 . THR B 2 55 ? 16.107 32.734 57.973 1.00 51.69 ? 554 THR B OG1 1 ATOM 3750 C CG2 . THR B 2 55 ? 16.767 34.883 58.866 1.00 51.05 ? 554 THR B CG2 1 ATOM 3751 N N . GLU B 2 56 ? 19.583 35.436 57.192 1.00 50.06 ? 555 GLU B N 1 ATOM 3752 C CA . GLU B 2 56 ? 20.326 36.690 57.320 1.00 51.10 ? 555 GLU B CA 1 ATOM 3753 C C . GLU B 2 56 ? 20.543 37.433 56.012 1.00 50.30 ? 555 GLU B C 1 ATOM 3754 O O . GLU B 2 56 ? 20.776 38.640 56.015 1.00 49.86 ? 555 GLU B O 1 ATOM 3755 C CB . GLU B 2 56 ? 21.682 36.455 57.999 1.00 53.47 ? 555 GLU B CB 1 ATOM 3756 C CG . GLU B 2 56 ? 22.564 35.429 57.312 1.00 57.41 ? 555 GLU B CG 1 ATOM 3757 C CD . GLU B 2 56 ? 22.171 33.991 57.636 1.00 60.69 ? 555 GLU B CD 1 ATOM 3758 O OE1 . GLU B 2 56 ? 22.809 33.076 57.067 1.00 61.41 ? 555 GLU B OE1 1 ATOM 3759 O OE2 . GLU B 2 56 ? 21.243 33.772 58.457 1.00 59.38 ? 555 GLU B OE2 1 ATOM 3760 N N . LYS B 2 57 ? 20.478 36.722 54.893 1.00 50.22 ? 556 LYS B N 1 ATOM 3761 C CA . LYS B 2 57 ? 20.660 37.369 53.603 1.00 50.37 ? 556 LYS B CA 1 ATOM 3762 C C . LYS B 2 57 ? 19.395 38.102 53.164 1.00 50.39 ? 556 LYS B C 1 ATOM 3763 O O . LYS B 2 57 ? 19.467 39.075 52.416 1.00 50.94 ? 556 LYS B O 1 ATOM 3764 C CB . LYS B 2 57 ? 21.087 36.346 52.549 1.00 50.82 ? 556 LYS B CB 1 ATOM 3765 C CG . LYS B 2 57 ? 22.580 36.044 52.579 1.00 52.61 ? 556 LYS B CG 1 ATOM 3766 C CD . LYS B 2 57 ? 22.960 34.989 51.553 1.00 56.96 ? 556 LYS B CD 1 ATOM 3767 C CE . LYS B 2 57 ? 24.471 34.787 51.472 1.00 57.58 ? 556 LYS B CE 1 ATOM 3768 N NZ . LYS B 2 57 ? 25.160 35.976 50.888 1.00 58.66 ? 556 LYS B NZ 1 ATOM 3769 N N . ALA B 2 58 ? 18.242 37.645 53.647 1.00 49.90 ? 557 ALA B N 1 ATOM 3770 C CA . ALA B 2 58 ? 16.962 38.260 53.311 1.00 50.16 ? 557 ALA B CA 1 ATOM 3771 C C . ALA B 2 58 ? 16.572 39.266 54.394 1.00 51.61 ? 557 ALA B C 1 ATOM 3772 O O . ALA B 2 58 ? 15.392 39.510 54.648 1.00 50.88 ? 557 ALA B O 1 ATOM 3773 C CB . ALA B 2 58 ? 15.894 37.188 53.184 1.00 48.48 ? 557 ALA B CB 1 ATOM 3774 N N . ARG B 2 59 ? 17.585 39.860 55.012 1.00 53.26 ? 558 ARG B N 1 ATOM 3775 C CA . ARG B 2 59 ? 17.398 40.821 56.092 1.00 55.34 ? 558 ARG B CA 1 ATOM 3776 C C . ARG B 2 59 ? 16.843 42.181 55.649 1.00 53.94 ? 558 ARG B C 1 ATOM 3777 O O . ARG B 2 59 ? 15.973 42.741 56.311 1.00 54.23 ? 558 ARG B O 1 ATOM 3778 C CB . ARG B 2 59 ? 18.734 41.006 56.818 1.00 59.24 ? 558 ARG B CB 1 ATOM 3779 C CG . ARG B 2 59 ? 18.632 41.620 58.192 1.00 65.16 ? 558 ARG B CG 1 ATOM 3780 C CD . ARG B 2 59 ? 20.014 41.826 58.792 1.00 70.81 ? 558 ARG B CD 1 ATOM 3781 N NE . ARG B 2 59 ? 20.905 42.527 57.867 1.00 75.51 ? 558 ARG B NE 1 ATOM 3782 C CZ . ARG B 2 59 ? 21.974 43.228 58.236 1.00 77.06 ? 558 ARG B CZ 1 ATOM 3783 N NH1 . ARG B 2 59 ? 22.294 43.332 59.521 1.00 77.29 ? 558 ARG B NH1 1 ATOM 3784 N NH2 . ARG B 2 59 ? 22.728 43.825 57.318 1.00 77.80 ? 558 ARG B NH2 1 ATOM 3785 N N . SER B 2 60 ? 17.342 42.714 54.537 1.00 52.52 ? 559 SER B N 1 ATOM 3786 C CA . SER B 2 60 ? 16.874 44.009 54.040 1.00 50.68 ? 559 SER B CA 1 ATOM 3787 C C . SER B 2 60 ? 15.938 43.843 52.849 1.00 48.78 ? 559 SER B C 1 ATOM 3788 O O . SER B 2 60 ? 15.729 42.731 52.370 1.00 48.31 ? 559 SER B O 1 ATOM 3789 C CB . SER B 2 60 ? 18.064 44.882 53.641 1.00 51.38 ? 559 SER B CB 1 ATOM 3790 O OG . SER B 2 60 ? 18.941 45.064 54.741 1.00 53.97 ? 559 SER B OG 1 ATOM 3791 N N . LYS B 2 61 ? 15.368 44.945 52.371 1.00 47.35 ? 560 LYS B N 1 ATOM 3792 C CA . LYS B 2 61 ? 14.453 44.869 51.240 1.00 46.45 ? 560 LYS B CA 1 ATOM 3793 C C . LYS B 2 61 ? 15.201 44.551 49.946 1.00 45.08 ? 560 LYS B C 1 ATOM 3794 O O . LYS B 2 61 ? 16.249 45.130 49.664 1.00 43.93 ? 560 LYS B O 1 ATOM 3795 C CB . LYS B 2 61 ? 13.663 46.174 51.085 1.00 46.68 ? 560 LYS B CB 1 ATOM 3796 C CG . LYS B 2 61 ? 12.518 46.043 50.089 1.00 48.88 ? 560 LYS B CG 1 ATOM 3797 C CD . LYS B 2 61 ? 11.513 47.183 50.164 1.00 48.87 ? 560 LYS B CD 1 ATOM 3798 C CE . LYS B 2 61 ? 12.038 48.464 49.543 1.00 49.68 ? 560 LYS B CE 1 ATOM 3799 N NZ . LYS B 2 61 ? 10.963 49.501 49.509 1.00 49.26 ? 560 LYS B NZ 1 ATOM 3800 N N . PRO B 2 62 ? 14.666 43.616 49.142 1.00 43.79 ? 561 PRO B N 1 ATOM 3801 C CA . PRO B 2 62 ? 15.277 43.210 47.875 1.00 42.83 ? 561 PRO B CA 1 ATOM 3802 C C . PRO B 2 62 ? 14.946 44.126 46.703 1.00 42.85 ? 561 PRO B C 1 ATOM 3803 O O . PRO B 2 62 ? 14.056 44.969 46.792 1.00 42.01 ? 561 PRO B O 1 ATOM 3804 C CB . PRO B 2 62 ? 14.712 41.815 47.672 1.00 41.90 ? 561 PRO B CB 1 ATOM 3805 C CG . PRO B 2 62 ? 13.317 41.981 48.162 1.00 41.73 ? 561 PRO B CG 1 ATOM 3806 C CD . PRO B 2 62 ? 13.501 42.765 49.449 1.00 42.48 ? 561 PRO B CD 1 ATOM 3807 N N . GLN B 2 63 ? 15.674 43.948 45.603 1.00 43.84 ? 562 GLN B N 1 ATOM 3808 C CA . GLN B 2 63 ? 15.448 44.719 44.384 1.00 44.60 ? 562 GLN B CA 1 ATOM 3809 C C . GLN B 2 63 ? 14.546 43.900 43.461 1.00 43.73 ? 562 GLN B C 1 ATOM 3810 O O . GLN B 2 63 ? 14.549 42.665 43.510 1.00 43.35 ? 562 GLN B O 1 ATOM 3811 C CB . GLN B 2 63 ? 16.765 45.001 43.680 1.00 46.27 ? 562 GLN B CB 1 ATOM 3812 C CG . GLN B 2 63 ? 17.758 45.755 44.521 1.00 53.61 ? 562 GLN B CG 1 ATOM 3813 C CD . GLN B 2 63 ? 19.080 45.937 43.808 1.00 58.79 ? 562 GLN B CD 1 ATOM 3814 O OE1 . GLN B 2 63 ? 19.153 46.598 42.764 1.00 60.50 ? 562 GLN B OE1 1 ATOM 3815 N NE2 . GLN B 2 63 ? 20.137 45.340 44.360 1.00 60.26 ? 562 GLN B NE2 1 ATOM 3816 N N . PHE B 2 64 ? 13.786 44.587 42.614 1.00 41.41 ? 563 PHE B N 1 ATOM 3817 C CA . PHE B 2 64 ? 12.870 43.916 41.699 1.00 38.85 ? 563 PHE B CA 1 ATOM 3818 C C . PHE B 2 64 ? 13.035 44.364 40.251 1.00 37.05 ? 563 PHE B C 1 ATOM 3819 O O . PHE B 2 64 ? 13.513 45.462 39.974 1.00 35.56 ? 563 PHE B O 1 ATOM 3820 C CB . PHE B 2 64 ? 11.428 44.185 42.123 1.00 40.13 ? 563 PHE B CB 1 ATOM 3821 C CG . PHE B 2 64 ? 11.121 43.780 43.532 1.00 42.13 ? 563 PHE B CG 1 ATOM 3822 C CD1 . PHE B 2 64 ? 10.640 42.503 43.814 1.00 41.74 ? 563 PHE B CD1 1 ATOM 3823 C CD2 . PHE B 2 64 ? 11.294 44.683 44.582 1.00 42.19 ? 563 PHE B CD2 1 ATOM 3824 C CE1 . PHE B 2 64 ? 10.329 42.127 45.125 1.00 41.95 ? 563 PHE B CE1 1 ATOM 3825 C CE2 . PHE B 2 64 ? 10.988 44.320 45.896 1.00 42.76 ? 563 PHE B CE2 1 ATOM 3826 C CZ . PHE B 2 64 ? 10.502 43.036 46.167 1.00 42.75 ? 563 PHE B CZ 1 ATOM 3827 N N . GLN B 2 65 ? 12.632 43.489 39.334 1.00 35.20 ? 564 GLN B N 1 ATOM 3828 C CA . GLN B 2 65 ? 12.671 43.763 37.905 1.00 33.18 ? 564 GLN B CA 1 ATOM 3829 C C . GLN B 2 65 ? 11.520 43.000 37.293 1.00 31.94 ? 564 GLN B C 1 ATOM 3830 O O . GLN B 2 65 ? 11.243 41.873 37.692 1.00 32.34 ? 564 GLN B O 1 ATOM 3831 C CB . GLN B 2 65 ? 13.973 43.291 37.253 1.00 32.88 ? 564 GLN B CB 1 ATOM 3832 C CG . GLN B 2 65 ? 13.968 43.495 35.731 1.00 32.91 ? 564 GLN B CG 1 ATOM 3833 C CD . GLN B 2 65 ? 15.149 42.852 35.028 1.00 33.98 ? 564 GLN B CD 1 ATOM 3834 O OE1 . GLN B 2 65 ? 15.363 41.646 35.130 1.00 34.16 ? 564 GLN B OE1 1 ATOM 3835 N NE2 . GLN B 2 65 ? 15.916 43.655 34.300 1.00 32.52 ? 564 GLN B NE2 1 ATOM 3836 N N . PHE B 2 66 ? 10.848 43.615 36.328 1.00 31.94 ? 565 PHE B N 1 ATOM 3837 C CA . PHE B 2 66 ? 9.724 42.974 35.660 1.00 31.29 ? 565 PHE B CA 1 ATOM 3838 C C . PHE B 2 66 ? 10.033 42.825 34.181 1.00 30.46 ? 565 PHE B C 1 ATOM 3839 O O . PHE B 2 66 ? 10.396 43.784 33.513 1.00 29.66 ? 565 PHE B O 1 ATOM 3840 C CB . PHE B 2 66 ? 8.452 43.799 35.844 1.00 31.76 ? 565 PHE B CB 1 ATOM 3841 C CG . PHE B 2 66 ? 7.252 43.236 35.133 1.00 34.92 ? 565 PHE B CG 1 ATOM 3842 C CD1 . PHE B 2 66 ? 6.814 41.942 35.389 1.00 35.42 ? 565 PHE B CD1 1 ATOM 3843 C CD2 . PHE B 2 66 ? 6.549 44.007 34.213 1.00 36.72 ? 565 PHE B CD2 1 ATOM 3844 C CE1 . PHE B 2 66 ? 5.695 41.421 34.740 1.00 35.92 ? 565 PHE B CE1 1 ATOM 3845 C CE2 . PHE B 2 66 ? 5.426 43.495 33.558 1.00 38.00 ? 565 PHE B CE2 1 ATOM 3846 C CZ . PHE B 2 66 ? 5.000 42.200 33.823 1.00 37.56 ? 565 PHE B CZ 1 ATOM 3847 N N . THR B 2 67 ? 9.924 41.605 33.681 1.00 30.23 ? 566 THR B N 1 ATOM 3848 C CA . THR B 2 67 ? 10.171 41.362 32.276 1.00 31.74 ? 566 THR B CA 1 ATOM 3849 C C . THR B 2 67 ? 8.846 40.980 31.655 1.00 34.17 ? 566 THR B C 1 ATOM 3850 O O . THR B 2 67 ? 8.238 39.974 32.020 1.00 32.21 ? 566 THR B O 1 ATOM 3851 C CB . THR B 2 67 ? 11.191 40.224 32.056 1.00 30.83 ? 566 THR B CB 1 ATOM 3852 O OG1 . THR B 2 67 ? 12.501 40.690 32.389 1.00 32.90 ? 566 THR B OG1 1 ATOM 3853 C CG2 . THR B 2 67 ? 11.188 39.771 30.611 1.00 29.07 ? 566 THR B CG2 1 ATOM 3854 N N . PHE B 2 68 ? 8.380 41.813 30.738 1.00 38.39 ? 567 PHE B N 1 ATOM 3855 C CA . PHE B 2 68 ? 7.131 41.528 30.064 1.00 43.85 ? 567 PHE B CA 1 ATOM 3856 C C . PHE B 2 68 ? 7.456 40.907 28.718 1.00 47.85 ? 567 PHE B C 1 ATOM 3857 O O . PHE B 2 68 ? 8.379 41.341 28.021 1.00 45.80 ? 567 PHE B O 1 ATOM 3858 C CB . PHE B 2 68 ? 6.303 42.804 29.880 1.00 41.76 ? 567 PHE B CB 1 ATOM 3859 C CG . PHE B 2 68 ? 5.136 42.635 28.952 1.00 41.75 ? 567 PHE B CG 1 ATOM 3860 C CD1 . PHE B 2 68 ? 5.246 42.972 27.604 1.00 40.76 ? 567 PHE B CD1 1 ATOM 3861 C CD2 . PHE B 2 68 ? 3.932 42.105 29.414 1.00 42.45 ? 567 PHE B CD2 1 ATOM 3862 C CE1 . PHE B 2 68 ? 4.175 42.783 26.729 1.00 40.90 ? 567 PHE B CE1 1 ATOM 3863 C CE2 . PHE B 2 68 ? 2.850 41.911 28.545 1.00 41.79 ? 567 PHE B CE2 1 ATOM 3864 C CZ . PHE B 2 68 ? 2.973 42.250 27.202 1.00 40.66 ? 567 PHE B CZ 1 ATOM 3865 N N . ASN B 2 69 ? 6.704 39.872 28.370 1.00 54.18 ? 568 ASN B N 1 ATOM 3866 C CA . ASN B 2 69 ? 6.894 39.185 27.103 1.00 60.52 ? 568 ASN B CA 1 ATOM 3867 C C . ASN B 2 69 ? 5.535 38.898 26.492 1.00 63.77 ? 568 ASN B C 1 ATOM 3868 O O . ASN B 2 69 ? 4.851 37.960 26.909 1.00 63.88 ? 568 ASN B O 1 ATOM 3869 C CB . ASN B 2 69 ? 7.648 37.874 27.316 1.00 62.67 ? 568 ASN B CB 1 ATOM 3870 C CG . ASN B 2 69 ? 7.861 37.115 26.026 1.00 66.72 ? 568 ASN B CG 1 ATOM 3871 O OD1 . ASN B 2 69 ? 8.416 37.652 25.066 1.00 69.68 ? 568 ASN B OD1 1 ATOM 3872 N ND2 . ASN B 2 69 ? 7.422 35.859 25.993 1.00 68.96 ? 568 ASN B ND2 1 ATOM 3873 N N . LYS B 2 70 ? 5.134 39.718 25.524 1.00 67.26 ? 569 LYS B N 1 ATOM 3874 C CA . LYS B 2 70 ? 3.849 39.522 24.863 1.00 71.14 ? 569 LYS B CA 1 ATOM 3875 C C . LYS B 2 70 ? 3.925 38.218 24.091 1.00 72.65 ? 569 LYS B C 1 ATOM 3876 O O . LYS B 2 70 ? 4.305 38.194 22.919 1.00 74.34 ? 569 LYS B O 1 ATOM 3877 C CB . LYS B 2 70 ? 3.549 40.676 23.906 1.00 72.74 ? 569 LYS B CB 1 ATOM 3878 C CG . LYS B 2 70 ? 2.337 40.440 23.016 1.00 74.85 ? 569 LYS B CG 1 ATOM 3879 C CD . LYS B 2 70 ? 2.060 41.650 22.141 1.00 77.85 ? 569 LYS B CD 1 ATOM 3880 C CE . LYS B 2 70 ? 1.135 41.298 20.991 1.00 79.74 ? 569 LYS B CE 1 ATOM 3881 N NZ . LYS B 2 70 ? 1.777 40.308 20.075 1.00 80.55 ? 569 LYS B NZ 1 ATOM 3882 N N . GLN B 2 71 ? 3.573 37.131 24.766 1.00 73.39 ? 570 GLN B N 1 ATOM 3883 C CA . GLN B 2 71 ? 3.612 35.810 24.166 1.00 74.61 ? 570 GLN B CA 1 ATOM 3884 C C . GLN B 2 71 ? 3.229 34.815 25.254 1.00 74.09 ? 570 GLN B C 1 ATOM 3885 O O . GLN B 2 71 ? 2.533 33.833 25.000 1.00 74.37 ? 570 GLN B O 1 ATOM 3886 C CB . GLN B 2 71 ? 5.023 35.513 23.641 1.00 76.40 ? 570 GLN B CB 1 ATOM 3887 C CG . GLN B 2 71 ? 5.072 34.425 22.586 1.00 80.11 ? 570 GLN B CG 1 ATOM 3888 C CD . GLN B 2 71 ? 4.707 33.058 23.135 1.00 82.79 ? 570 GLN B CD 1 ATOM 3889 O OE1 . GLN B 2 71 ? 4.243 32.184 22.400 1.00 83.96 ? 570 GLN B OE1 1 ATOM 3890 N NE2 . GLN B 2 71 ? 4.930 32.860 24.431 1.00 84.31 ? 570 GLN B NE2 1 ATOM 3891 N N . MET B 2 72 ? 3.687 35.084 26.472 1.00 73.27 ? 571 MET B N 1 ATOM 3892 C CA . MET B 2 72 ? 3.387 34.230 27.614 1.00 72.92 ? 571 MET B CA 1 ATOM 3893 C C . MET B 2 72 ? 1.885 34.237 27.888 1.00 73.79 ? 571 MET B C 1 ATOM 3894 O O . MET B 2 72 ? 1.416 33.670 28.880 1.00 73.63 ? 571 MET B O 1 ATOM 3895 C CB . MET B 2 72 ? 4.131 34.733 28.847 1.00 71.38 ? 571 MET B CB 1 ATOM 3896 C CG . MET B 2 72 ? 5.632 34.784 28.676 1.00 70.42 ? 571 MET B CG 1 ATOM 3897 S SD . MET B 2 72 ? 6.436 35.363 30.167 1.00 67.50 ? 571 MET B SD 1 ATOM 3898 C CE . MET B 2 72 ? 6.202 33.937 31.222 1.00 69.43 ? 571 MET B CE 1 ATOM 3899 N N . GLN B 2 73 ? 1.139 34.883 26.996 1.00 74.35 ? 572 GLN B N 1 ATOM 3900 C CA . GLN B 2 73 ? -0.307 34.984 27.122 1.00 74.57 ? 572 GLN B CA 1 ATOM 3901 C C . GLN B 2 73 ? -1.015 34.457 25.876 1.00 74.07 ? 572 GLN B C 1 ATOM 3902 O O . GLN B 2 73 ? -0.529 34.618 24.756 1.00 73.51 ? 572 GLN B O 1 ATOM 3903 C CB . GLN B 2 73 ? -0.695 36.442 27.369 1.00 74.76 ? 572 GLN B CB 1 ATOM 3904 C CG . GLN B 2 73 ? -0.088 37.028 28.631 1.00 75.39 ? 572 GLN B CG 1 ATOM 3905 C CD . GLN B 2 73 ? -0.526 38.457 28.884 1.00 76.19 ? 572 GLN B CD 1 ATOM 3906 O OE1 . GLN B 2 73 ? -0.140 39.378 28.164 1.00 76.19 ? 572 GLN B OE1 1 ATOM 3907 N NE2 . GLN B 2 73 ? -1.345 38.648 29.910 1.00 76.90 ? 572 GLN B NE2 1 ATOM 3908 N N . ASN B 2 80 ? -8.927 40.327 31.487 1.00 75.66 ? 579 ASN B N 1 ATOM 3909 C CA . ASN B 2 80 ? -8.176 39.075 31.494 1.00 76.02 ? 579 ASN B CA 1 ATOM 3910 C C . ASN B 2 80 ? -6.687 39.283 31.195 1.00 74.92 ? 579 ASN B C 1 ATOM 3911 O O . ASN B 2 80 ? -5.849 39.222 32.098 1.00 75.20 ? 579 ASN B O 1 ATOM 3912 C CB . ASN B 2 80 ? -8.788 38.083 30.488 1.00 76.56 ? 579 ASN B CB 1 ATOM 3913 C CG . ASN B 2 80 ? -8.853 38.640 29.071 1.00 77.15 ? 579 ASN B CG 1 ATOM 3914 O OD1 . ASN B 2 80 ? -9.319 39.760 28.851 1.00 77.49 ? 579 ASN B OD1 1 ATOM 3915 N ND2 . ASN B 2 80 ? -8.395 37.853 28.101 1.00 77.34 ? 579 ASN B ND2 1 ATOM 3916 N N . ALA B 2 81 ? -6.361 39.535 29.931 1.00 73.07 ? 580 ALA B N 1 ATOM 3917 C CA . ALA B 2 81 ? -4.974 39.740 29.528 1.00 71.45 ? 580 ALA B CA 1 ATOM 3918 C C . ALA B 2 81 ? -4.435 41.100 29.964 1.00 70.06 ? 580 ALA B C 1 ATOM 3919 O O . ALA B 2 81 ? -5.148 42.106 29.946 1.00 70.12 ? 580 ALA B O 1 ATOM 3920 C CB . ALA B 2 81 ? -4.842 39.594 28.013 1.00 71.25 ? 580 ALA B CB 1 ATOM 3921 N N . TYR B 2 82 ? -3.168 41.116 30.362 1.00 66.84 ? 581 TYR B N 1 ATOM 3922 C CA . TYR B 2 82 ? -2.518 42.343 30.782 1.00 63.09 ? 581 TYR B CA 1 ATOM 3923 C C . TYR B 2 82 ? -1.778 42.979 29.609 1.00 62.08 ? 581 TYR B C 1 ATOM 3924 O O . TYR B 2 82 ? -0.896 42.360 29.006 1.00 61.03 ? 581 TYR B O 1 ATOM 3925 C CB . TYR B 2 82 ? -1.528 42.068 31.917 1.00 60.89 ? 581 TYR B CB 1 ATOM 3926 C CG . TYR B 2 82 ? -0.523 43.183 32.101 1.00 58.87 ? 581 TYR B CG 1 ATOM 3927 C CD1 . TYR B 2 82 ? -0.937 44.470 32.442 1.00 58.18 ? 581 TYR B CD1 1 ATOM 3928 C CD2 . TYR B 2 82 ? 0.832 42.971 31.861 1.00 57.94 ? 581 TYR B CD2 1 ATOM 3929 C CE1 . TYR B 2 82 ? -0.030 45.518 32.532 1.00 57.43 ? 581 TYR B CE1 1 ATOM 3930 C CE2 . TYR B 2 82 ? 1.748 44.012 31.947 1.00 57.73 ? 581 TYR B CE2 1 ATOM 3931 C CZ . TYR B 2 82 ? 1.309 45.283 32.280 1.00 57.95 ? 581 TYR B CZ 1 ATOM 3932 O OH . TYR B 2 82 ? 2.205 46.326 32.337 1.00 59.00 ? 581 TYR B OH 1 ATOM 3933 N N . VAL B 2 83 ? -2.145 44.217 29.291 1.00 61.48 ? 582 VAL B N 1 ATOM 3934 C CA . VAL B 2 83 ? -1.509 44.962 28.210 1.00 60.29 ? 582 VAL B CA 1 ATOM 3935 C C . VAL B 2 83 ? -0.848 46.180 28.840 1.00 59.19 ? 582 VAL B C 1 ATOM 3936 O O . VAL B 2 83 ? -1.527 47.107 29.276 1.00 58.84 ? 582 VAL B O 1 ATOM 3937 C CB . VAL B 2 83 ? -2.537 45.440 27.169 1.00 60.66 ? 582 VAL B CB 1 ATOM 3938 C CG1 . VAL B 2 83 ? -1.815 45.915 25.918 1.00 60.99 ? 582 VAL B CG1 1 ATOM 3939 C CG2 . VAL B 2 83 ? -3.507 44.315 26.836 1.00 60.60 ? 582 VAL B CG2 1 ATOM 3940 N N . PRO B 2 84 ? 0.491 46.193 28.899 1.00 59.17 ? 583 PRO B N 1 ATOM 3941 C CA . PRO B 2 84 ? 1.231 47.313 29.491 1.00 59.52 ? 583 PRO B CA 1 ATOM 3942 C C . PRO B 2 84 ? 0.835 48.688 28.967 1.00 59.95 ? 583 PRO B C 1 ATOM 3943 O O . PRO B 2 84 ? 0.529 48.848 27.789 1.00 59.40 ? 583 PRO B O 1 ATOM 3944 C CB . PRO B 2 84 ? 2.689 46.963 29.192 1.00 59.29 ? 583 PRO B CB 1 ATOM 3945 C CG . PRO B 2 84 ? 2.593 46.123 27.949 1.00 59.30 ? 583 PRO B CG 1 ATOM 3946 C CD . PRO B 2 84 ? 1.410 45.246 28.246 1.00 58.34 ? 583 PRO B CD 1 ATOM 3947 N N . GLN B 2 85 ? 0.835 49.670 29.867 1.00 62.11 ? 584 GLN B N 1 ATOM 3948 C CA . GLN B 2 85 ? 0.489 51.055 29.547 1.00 62.91 ? 584 GLN B CA 1 ATOM 3949 C C . GLN B 2 85 ? 1.264 52.007 30.445 1.00 63.48 ? 584 GLN B C 1 ATOM 3950 O O . GLN B 2 85 ? 1.931 51.575 31.380 1.00 63.89 ? 584 GLN B O 1 ATOM 3951 C CB . GLN B 2 85 ? -1.009 51.288 29.722 1.00 63.52 ? 584 GLN B CB 1 ATOM 3952 C CG . GLN B 2 85 ? -1.859 50.587 28.677 1.00 66.27 ? 584 GLN B CG 1 ATOM 3953 C CD . GLN B 2 85 ? -3.337 50.886 28.835 1.00 67.77 ? 584 GLN B CD 1 ATOM 3954 O OE1 . GLN B 2 85 ? -3.746 52.048 28.868 1.00 68.80 ? 584 GLN B OE1 1 ATOM 3955 N NE2 . GLN B 2 85 ? -4.149 49.837 28.928 1.00 67.53 ? 584 GLN B NE2 1 ATOM 3956 N N . ASP B 2 86 ? 1.166 53.304 30.167 1.00 65.28 ? 585 ASP B N 1 ATOM 3957 C CA . ASP B 2 86 ? 1.890 54.317 30.936 1.00 66.69 ? 585 ASP B CA 1 ATOM 3958 C C . ASP B 2 86 ? 1.259 54.711 32.264 1.00 66.22 ? 585 ASP B C 1 ATOM 3959 O O . ASP B 2 86 ? 1.966 55.052 33.215 1.00 66.48 ? 585 ASP B O 1 ATOM 3960 C CB . ASP B 2 86 ? 2.077 55.571 30.088 1.00 70.50 ? 585 ASP B CB 1 ATOM 3961 C CG . ASP B 2 86 ? 2.944 55.325 28.875 1.00 73.79 ? 585 ASP B CG 1 ATOM 3962 O OD1 . ASP B 2 86 ? 3.078 56.252 28.047 1.00 76.59 ? 585 ASP B OD1 1 ATOM 3963 O OD2 . ASP B 2 86 ? 3.494 54.206 28.752 1.00 74.58 ? 585 ASP B OD2 1 ATOM 3964 N N . ASP B 2 87 ? -0.067 54.681 32.324 1.00 64.62 ? 586 ASP B N 1 ATOM 3965 C CA . ASP B 2 87 ? -0.780 55.038 33.547 1.00 62.24 ? 586 ASP B CA 1 ATOM 3966 C C . ASP B 2 87 ? -0.552 53.982 34.626 1.00 58.01 ? 586 ASP B C 1 ATOM 3967 O O . ASP B 2 87 ? -0.559 54.287 35.815 1.00 58.22 ? 586 ASP B O 1 ATOM 3968 C CB . ASP B 2 87 ? -2.281 55.138 33.267 1.00 66.29 ? 586 ASP B CB 1 ATOM 3969 C CG . ASP B 2 87 ? -2.590 55.973 32.047 1.00 69.71 ? 586 ASP B CG 1 ATOM 3970 O OD1 . ASP B 2 87 ? -2.427 57.213 32.111 1.00 71.23 ? 586 ASP B OD1 1 ATOM 3971 O OD2 . ASP B 2 87 ? -2.989 55.381 31.018 1.00 72.35 ? 586 ASP B OD2 1 ATOM 3972 N N . ASP B 2 88 ? -0.351 52.742 34.193 1.00 52.58 ? 587 ASP B N 1 ATOM 3973 C CA . ASP B 2 88 ? -0.154 51.614 35.089 1.00 47.45 ? 587 ASP B CA 1 ATOM 3974 C C . ASP B 2 88 ? 0.596 51.862 36.388 1.00 43.42 ? 587 ASP B C 1 ATOM 3975 O O . ASP B 2 88 ? 1.693 52.409 36.403 1.00 42.26 ? 587 ASP B O 1 ATOM 3976 C CB . ASP B 2 88 ? 0.529 50.464 34.349 1.00 48.98 ? 587 ASP B CB 1 ATOM 3977 C CG . ASP B 2 88 ? -0.397 49.756 33.380 1.00 50.62 ? 587 ASP B CG 1 ATOM 3978 O OD1 . ASP B 2 88 ? -1.627 49.987 33.445 1.00 50.48 ? 587 ASP B OD1 1 ATOM 3979 O OD2 . ASP B 2 88 ? 0.113 48.954 32.561 1.00 50.51 ? 587 ASP B OD2 1 ATOM 3980 N N . LEU B 2 89 ? -0.025 51.442 37.480 1.00 39.38 ? 588 LEU B N 1 ATOM 3981 C CA . LEU B 2 89 ? 0.555 51.542 38.804 1.00 37.17 ? 588 LEU B CA 1 ATOM 3982 C C . LEU B 2 89 ? 0.544 50.119 39.355 1.00 36.02 ? 588 LEU B C 1 ATOM 3983 O O . LEU B 2 89 ? -0.427 49.385 39.175 1.00 34.55 ? 588 LEU B O 1 ATOM 3984 C CB . LEU B 2 89 ? -0.278 52.467 39.687 1.00 37.60 ? 588 LEU B CB 1 ATOM 3985 C CG . LEU B 2 89 ? -0.218 53.959 39.352 1.00 37.45 ? 588 LEU B CG 1 ATOM 3986 C CD1 . LEU B 2 89 ? -1.104 54.729 40.321 1.00 38.48 ? 588 LEU B CD1 1 ATOM 3987 C CD2 . LEU B 2 89 ? 1.218 54.455 39.446 1.00 37.48 ? 588 LEU B CD2 1 ATOM 3988 N N . PHE B 2 90 ? 1.624 49.714 40.011 1.00 35.89 ? 589 PHE B N 1 ATOM 3989 C CA . PHE B 2 90 ? 1.687 48.358 40.539 1.00 35.75 ? 589 PHE B CA 1 ATOM 3990 C C . PHE B 2 90 ? 1.812 48.246 42.051 1.00 35.95 ? 589 PHE B C 1 ATOM 3991 O O . PHE B 2 90 ? 2.175 49.204 42.742 1.00 37.50 ? 589 PHE B O 1 ATOM 3992 C CB . PHE B 2 90 ? 2.847 47.595 39.893 1.00 33.88 ? 589 PHE B CB 1 ATOM 3993 C CG . PHE B 2 90 ? 2.781 47.546 38.398 1.00 33.82 ? 589 PHE B CG 1 ATOM 3994 C CD1 . PHE B 2 90 ? 3.254 48.609 37.634 1.00 34.34 ? 589 PHE B CD1 1 ATOM 3995 C CD2 . PHE B 2 90 ? 2.226 46.446 37.752 1.00 33.88 ? 589 PHE B CD2 1 ATOM 3996 C CE1 . PHE B 2 90 ? 3.175 48.581 36.248 1.00 33.42 ? 589 PHE B CE1 1 ATOM 3997 C CE2 . PHE B 2 90 ? 2.138 46.401 36.364 1.00 33.23 ? 589 PHE B CE2 1 ATOM 3998 C CZ . PHE B 2 90 ? 2.613 47.472 35.609 1.00 35.08 ? 589 PHE B CZ 1 ATOM 3999 N N . THR B 2 91 ? 1.491 47.057 42.550 1.00 35.03 ? 590 THR B N 1 ATOM 4000 C CA . THR B 2 91 ? 1.589 46.746 43.965 1.00 34.66 ? 590 THR B CA 1 ATOM 4001 C C . THR B 2 91 ? 2.441 45.492 44.116 1.00 35.18 ? 590 THR B C 1 ATOM 4002 O O . THR B 2 91 ? 2.202 44.471 43.467 1.00 32.93 ? 590 THR B O 1 ATOM 4003 C CB . THR B 2 91 ? 0.203 46.509 44.598 1.00 34.43 ? 590 THR B CB 1 ATOM 4004 O OG1 . THR B 2 91 ? -0.403 47.773 44.890 1.00 31.28 ? 590 THR B OG1 1 ATOM 4005 C CG2 . THR B 2 91 ? 0.330 45.693 45.886 1.00 32.29 ? 590 THR B CG2 1 ATOM 4006 N N . LEU B 2 92 ? 3.441 45.591 44.980 1.00 37.35 ? 591 LEU B N 1 ATOM 4007 C CA . LEU B 2 92 ? 4.363 44.497 45.241 1.00 37.88 ? 591 LEU B CA 1 ATOM 4008 C C . LEU B 2 92 ? 4.107 43.960 46.645 1.00 37.32 ? 591 LEU B C 1 ATOM 4009 O O . LEU B 2 92 ? 4.210 44.692 47.632 1.00 36.15 ? 591 LEU B O 1 ATOM 4010 C CB . LEU B 2 92 ? 5.796 45.016 45.115 1.00 39.83 ? 591 LEU B CB 1 ATOM 4011 C CG . LEU B 2 92 ? 6.909 44.062 44.694 1.00 41.33 ? 591 LEU B CG 1 ATOM 4012 C CD1 . LEU B 2 92 ? 6.423 43.068 43.645 1.00 42.90 ? 591 LEU B CD1 1 ATOM 4013 C CD2 . LEU B 2 92 ? 8.040 44.903 44.141 1.00 44.42 ? 591 LEU B CD2 1 ATOM 4014 N N . VAL B 2 93 ? 3.775 42.677 46.721 1.00 36.42 ? 592 VAL B N 1 ATOM 4015 C CA . VAL B 2 93 ? 3.480 42.024 47.991 1.00 35.63 ? 592 VAL B CA 1 ATOM 4016 C C . VAL B 2 93 ? 4.450 40.897 48.350 1.00 35.32 ? 592 VAL B C 1 ATOM 4017 O O . VAL B 2 93 ? 5.020 40.256 47.475 1.00 35.68 ? 592 VAL B O 1 ATOM 4018 C CB . VAL B 2 93 ? 2.050 41.422 47.963 1.00 35.17 ? 592 VAL B CB 1 ATOM 4019 C CG1 . VAL B 2 93 ? 1.813 40.546 49.187 1.00 33.68 ? 592 VAL B CG1 1 ATOM 4020 C CG2 . VAL B 2 93 ? 1.026 42.533 47.907 1.00 34.13 ? 592 VAL B CG2 1 ATOM 4021 N N . MET B 2 94 ? 4.642 40.674 49.648 1.00 35.92 ? 593 MET B N 1 ATOM 4022 C CA . MET B 2 94 ? 5.474 39.576 50.126 1.00 36.69 ? 593 MET B CA 1 ATOM 4023 C C . MET B 2 94 ? 4.730 38.922 51.283 1.00 36.03 ? 593 MET B C 1 ATOM 4024 O O . MET B 2 94 ? 4.446 39.566 52.290 1.00 36.78 ? 593 MET B O 1 ATOM 4025 C CB . MET B 2 94 ? 6.843 40.046 50.611 1.00 37.91 ? 593 MET B CB 1 ATOM 4026 C CG . MET B 2 94 ? 7.771 38.867 50.912 1.00 41.08 ? 593 MET B CG 1 ATOM 4027 S SD . MET B 2 94 ? 9.395 39.317 51.564 1.00 47.40 ? 593 MET B SD 1 ATOM 4028 C CE . MET B 2 94 ? 9.530 38.164 52.929 1.00 46.49 ? 593 MET B CE 1 ATOM 4029 N N . THR B 2 95 ? 4.402 37.646 51.139 1.00 35.03 ? 594 THR B N 1 ATOM 4030 C CA . THR B 2 95 ? 3.681 36.960 52.195 1.00 35.49 ? 594 THR B CA 1 ATOM 4031 C C . THR B 2 95 ? 4.195 35.543 52.456 1.00 37.17 ? 594 THR B C 1 ATOM 4032 O O . THR B 2 95 ? 4.804 34.916 51.587 1.00 36.22 ? 594 THR B O 1 ATOM 4033 C CB . THR B 2 95 ? 2.173 36.890 51.871 1.00 33.97 ? 594 THR B CB 1 ATOM 4034 O OG1 . THR B 2 95 ? 1.450 36.451 53.032 1.00 32.46 ? 594 THR B OG1 1 ATOM 4035 C CG2 . THR B 2 95 ? 1.924 35.925 50.715 1.00 30.97 ? 594 THR B CG2 1 ATOM 4036 N N . ASP B 2 96 ? 3.938 35.060 53.671 1.00 38.37 ? 595 ASP B N 1 ATOM 4037 C CA . ASP B 2 96 ? 4.327 33.723 54.100 1.00 38.69 ? 595 ASP B CA 1 ATOM 4038 C C . ASP B 2 96 ? 3.049 32.968 54.470 1.00 39.52 ? 595 ASP B C 1 ATOM 4039 O O . ASP B 2 96 ? 2.379 33.316 55.438 1.00 40.62 ? 595 ASP B O 1 ATOM 4040 C CB . ASP B 2 96 ? 5.258 33.814 55.318 1.00 37.67 ? 595 ASP B CB 1 ATOM 4041 C CG . ASP B 2 96 ? 5.594 32.447 55.910 1.00 37.87 ? 595 ASP B CG 1 ATOM 4042 O OD1 . ASP B 2 96 ? 5.120 31.419 55.381 1.00 35.59 ? 595 ASP B OD1 1 ATOM 4043 O OD2 . ASP B 2 96 ? 6.337 32.400 56.912 1.00 37.83 ? 595 ASP B OD2 1 ATOM 4044 N N . PRO B 2 97 ? 2.687 31.933 53.697 1.00 39.86 ? 596 PRO B N 1 ATOM 4045 C CA . PRO B 2 97 ? 1.470 31.174 54.005 1.00 40.12 ? 596 PRO B CA 1 ATOM 4046 C C . PRO B 2 97 ? 1.765 30.013 54.952 1.00 41.62 ? 596 PRO B C 1 ATOM 4047 O O . PRO B 2 97 ? 0.883 29.203 55.258 1.00 43.85 ? 596 PRO B O 1 ATOM 4048 C CB . PRO B 2 97 ? 1.026 30.690 52.637 1.00 38.06 ? 596 PRO B CB 1 ATOM 4049 C CG . PRO B 2 97 ? 2.345 30.343 52.003 1.00 38.32 ? 596 PRO B CG 1 ATOM 4050 C CD . PRO B 2 97 ? 3.262 31.500 52.410 1.00 38.62 ? 596 PRO B CD 1 ATOM 4051 N N . ASP B 2 98 ? 3.013 29.933 55.405 1.00 40.81 ? 597 ASP B N 1 ATOM 4052 C CA . ASP B 2 98 ? 3.433 28.869 56.310 1.00 41.31 ? 597 ASP B CA 1 ATOM 4053 C C . ASP B 2 98 ? 3.868 29.429 57.665 1.00 42.34 ? 597 ASP B C 1 ATOM 4054 O O . ASP B 2 98 ? 4.977 29.170 58.140 1.00 41.20 ? 597 ASP B O 1 ATOM 4055 C CB . ASP B 2 98 ? 4.573 28.065 55.675 1.00 38.78 ? 597 ASP B CB 1 ATOM 4056 C CG . ASP B 2 98 ? 4.201 27.511 54.315 1.00 38.24 ? 597 ASP B CG 1 ATOM 4057 O OD1 . ASP B 2 98 ? 3.089 26.956 54.181 1.00 37.73 ? 597 ASP B OD1 1 ATOM 4058 O OD2 . ASP B 2 98 ? 5.020 27.625 53.382 1.00 37.56 ? 597 ASP B OD2 1 ATOM 4059 N N . ALA B 2 99 ? 2.978 30.204 58.277 1.00 43.69 ? 598 ALA B N 1 ATOM 4060 C CA . ALA B 2 99 ? 3.246 30.809 59.571 1.00 45.17 ? 598 ALA B CA 1 ATOM 4061 C C . ALA B 2 99 ? 2.218 30.314 60.584 1.00 47.36 ? 598 ALA B C 1 ATOM 4062 O O . ALA B 2 99 ? 1.016 30.391 60.346 1.00 48.51 ? 598 ALA B O 1 ATOM 4063 C CB . ALA B 2 99 ? 3.186 32.317 59.455 1.00 43.50 ? 598 ALA B CB 1 ATOM 4064 N N . PRO B 2 100 ? 2.682 29.785 61.726 1.00 49.58 ? 599 PRO B N 1 ATOM 4065 C CA . PRO B 2 100 ? 4.090 29.630 62.105 1.00 50.80 ? 599 PRO B CA 1 ATOM 4066 C C . PRO B 2 100 ? 4.804 28.472 61.399 1.00 51.34 ? 599 PRO B C 1 ATOM 4067 O O . PRO B 2 100 ? 6.020 28.332 61.507 1.00 51.34 ? 599 PRO B O 1 ATOM 4068 C CB . PRO B 2 100 ? 4.008 29.419 63.609 1.00 50.67 ? 599 PRO B CB 1 ATOM 4069 C CG . PRO B 2 100 ? 2.754 28.607 63.734 1.00 50.49 ? 599 PRO B CG 1 ATOM 4070 C CD . PRO B 2 100 ? 1.797 29.329 62.813 1.00 50.18 ? 599 PRO B CD 1 ATOM 4071 N N . SER B 2 101 ? 4.048 27.644 60.684 1.00 51.99 ? 600 SER B N 1 ATOM 4072 C CA . SER B 2 101 ? 4.631 26.509 59.977 1.00 53.56 ? 600 SER B CA 1 ATOM 4073 C C . SER B 2 101 ? 3.742 26.072 58.819 1.00 55.11 ? 600 SER B C 1 ATOM 4074 O O . SER B 2 101 ? 2.628 26.568 58.653 1.00 54.38 ? 600 SER B O 1 ATOM 4075 C CB . SER B 2 101 ? 4.804 25.328 60.928 1.00 53.82 ? 600 SER B CB 1 ATOM 4076 O OG . SER B 2 101 ? 3.543 24.733 61.211 1.00 54.62 ? 600 SER B OG 1 ATOM 4077 N N . LYS B 2 102 ? 4.240 25.121 58.033 1.00 57.01 ? 601 LYS B N 1 ATOM 4078 C CA . LYS B 2 102 ? 3.503 24.604 56.890 1.00 58.92 ? 601 LYS B CA 1 ATOM 4079 C C . LYS B 2 102 ? 2.277 23.819 57.337 1.00 59.85 ? 601 LYS B C 1 ATOM 4080 O O . LYS B 2 102 ? 1.438 23.449 56.519 1.00 60.03 ? 601 LYS B O 1 ATOM 4081 C CB . LYS B 2 102 ? 4.406 23.699 56.047 1.00 60.29 ? 601 LYS B CB 1 ATOM 4082 C CG . LYS B 2 102 ? 3.750 23.188 54.773 1.00 63.54 ? 601 LYS B CG 1 ATOM 4083 C CD . LYS B 2 102 ? 4.569 22.082 54.117 1.00 66.61 ? 601 LYS B CD 1 ATOM 4084 C CE . LYS B 2 102 ? 3.847 21.503 52.898 1.00 67.69 ? 601 LYS B CE 1 ATOM 4085 N NZ . LYS B 2 102 ? 4.560 20.323 52.310 1.00 68.54 ? 601 LYS B NZ 1 ATOM 4086 N N . THR B 2 103 ? 2.172 23.565 58.637 1.00 61.72 ? 602 THR B N 1 ATOM 4087 C CA . THR B 2 103 ? 1.041 22.810 59.167 1.00 63.58 ? 602 THR B CA 1 ATOM 4088 C C . THR B 2 103 ? 0.156 23.628 60.097 1.00 64.57 ? 602 THR B C 1 ATOM 4089 O O . THR B 2 103 ? -1.068 23.602 59.970 1.00 64.03 ? 602 THR B O 1 ATOM 4090 C CB . THR B 2 103 ? 1.521 21.552 59.906 1.00 63.37 ? 602 THR B CB 1 ATOM 4091 O OG1 . THR B 2 103 ? 2.043 20.621 58.952 1.00 62.06 ? 602 THR B OG1 1 ATOM 4092 C CG2 . THR B 2 103 ? 0.372 20.904 60.667 1.00 64.69 ? 602 THR B CG2 1 ATOM 4093 N N . ASP B 2 104 ? 0.774 24.339 61.036 1.00 66.11 ? 603 ASP B N 1 ATOM 4094 C CA . ASP B 2 104 ? 0.027 25.179 61.969 1.00 67.78 ? 603 ASP B CA 1 ATOM 4095 C C . ASP B 2 104 ? -0.204 26.527 61.281 1.00 68.92 ? 603 ASP B C 1 ATOM 4096 O O . ASP B 2 104 ? 0.744 27.284 61.048 1.00 68.76 ? 603 ASP B O 1 ATOM 4097 C CB . ASP B 2 104 ? 0.826 25.384 63.259 1.00 68.57 ? 603 ASP B CB 1 ATOM 4098 C CG . ASP B 2 104 ? -0.039 25.869 64.416 1.00 69.60 ? 603 ASP B CG 1 ATOM 4099 O OD1 . ASP B 2 104 ? -0.790 26.853 64.249 1.00 70.58 ? 603 ASP B OD1 1 ATOM 4100 O OD2 . ASP B 2 104 ? 0.038 25.264 65.505 1.00 71.40 ? 603 ASP B OD2 1 ATOM 4101 N N . HIS B 2 105 ? -1.460 26.823 60.956 1.00 69.71 ? 604 HIS B N 1 ATOM 4102 C CA . HIS B 2 105 ? -1.793 28.071 60.279 1.00 70.70 ? 604 HIS B CA 1 ATOM 4103 C C . HIS B 2 105 ? -2.457 29.122 61.166 1.00 71.46 ? 604 HIS B C 1 ATOM 4104 O O . HIS B 2 105 ? -3.213 29.963 60.680 1.00 72.08 ? 604 HIS B O 1 ATOM 4105 C CB . HIS B 2 105 ? -2.685 27.775 59.073 1.00 70.15 ? 604 HIS B CB 1 ATOM 4106 C CG . HIS B 2 105 ? -2.037 26.892 58.053 1.00 70.53 ? 604 HIS B CG 1 ATOM 4107 N ND1 . HIS B 2 105 ? -0.821 27.193 57.474 1.00 70.62 ? 604 HIS B ND1 1 ATOM 4108 C CD2 . HIS B 2 105 ? -2.431 25.716 57.511 1.00 70.61 ? 604 HIS B CD2 1 ATOM 4109 C CE1 . HIS B 2 105 ? -0.495 26.240 56.620 1.00 70.50 ? 604 HIS B CE1 1 ATOM 4110 N NE2 . HIS B 2 105 ? -1.454 25.332 56.624 1.00 71.01 ? 604 HIS B NE2 1 ATOM 4111 N N . LYS B 2 106 ? -2.171 29.076 62.464 1.00 72.19 ? 605 LYS B N 1 ATOM 4112 C CA . LYS B 2 106 ? -2.737 30.038 63.401 1.00 72.85 ? 605 LYS B CA 1 ATOM 4113 C C . LYS B 2 106 ? -2.479 31.466 62.920 1.00 72.24 ? 605 LYS B C 1 ATOM 4114 O O . LYS B 2 106 ? -3.251 32.378 63.214 1.00 71.68 ? 605 LYS B O 1 ATOM 4115 C CB . LYS B 2 106 ? -2.134 29.831 64.800 1.00 74.39 ? 605 LYS B CB 1 ATOM 4116 C CG . LYS B 2 106 ? -2.334 30.999 65.773 1.00 76.79 ? 605 LYS B CG 1 ATOM 4117 C CD . LYS B 2 106 ? -3.807 31.317 66.036 1.00 78.49 ? 605 LYS B CD 1 ATOM 4118 C CE . LYS B 2 106 ? -4.472 30.257 66.907 1.00 79.95 ? 605 LYS B CE 1 ATOM 4119 N NZ . LYS B 2 106 ? -3.868 30.188 68.271 1.00 80.35 ? 605 LYS B NZ 1 ATOM 4120 N N . TRP B 2 107 ? -1.395 31.654 62.173 1.00 71.82 ? 606 TRP B N 1 ATOM 4121 C CA . TRP B 2 107 ? -1.047 32.974 61.657 1.00 72.41 ? 606 TRP B CA 1 ATOM 4122 C C . TRP B 2 107 ? -0.855 32.955 60.145 1.00 71.11 ? 606 TRP B C 1 ATOM 4123 O O . TRP B 2 107 ? -0.310 33.899 59.576 1.00 69.81 ? 606 TRP B O 1 ATOM 4124 C CB . TRP B 2 107 ? 0.242 33.476 62.312 1.00 74.47 ? 606 TRP B CB 1 ATOM 4125 C CG . TRP B 2 107 ? 0.258 33.327 63.796 1.00 77.48 ? 606 TRP B CG 1 ATOM 4126 C CD1 . TRP B 2 107 ? -0.767 33.596 64.657 1.00 78.40 ? 606 TRP B CD1 1 ATOM 4127 C CD2 . TRP B 2 107 ? 1.361 32.901 64.606 1.00 78.82 ? 606 TRP B CD2 1 ATOM 4128 N NE1 . TRP B 2 107 ? -0.371 33.364 65.953 1.00 79.82 ? 606 TRP B NE1 1 ATOM 4129 C CE2 . TRP B 2 107 ? 0.931 32.937 65.951 1.00 79.31 ? 606 TRP B CE2 1 ATOM 4130 C CE3 . TRP B 2 107 ? 2.673 32.493 64.326 1.00 79.13 ? 606 TRP B CE3 1 ATOM 4131 C CZ2 . TRP B 2 107 ? 1.766 32.581 67.015 1.00 79.02 ? 606 TRP B CZ2 1 ATOM 4132 C CZ3 . TRP B 2 107 ? 3.504 32.139 65.388 1.00 78.89 ? 606 TRP B CZ3 1 ATOM 4133 C CH2 . TRP B 2 107 ? 3.044 32.187 66.715 1.00 78.73 ? 606 TRP B CH2 1 ATOM 4134 N N . SER B 2 108 ? -1.310 31.881 59.505 1.00 70.66 ? 607 SER B N 1 ATOM 4135 C CA . SER B 2 108 ? -1.161 31.718 58.063 1.00 69.16 ? 607 SER B CA 1 ATOM 4136 C C . SER B 2 108 ? -1.344 33.020 57.300 1.00 67.11 ? 607 SER B C 1 ATOM 4137 O O . SER B 2 108 ? -2.332 33.743 57.482 1.00 65.31 ? 607 SER B O 1 ATOM 4138 C CB . SER B 2 108 ? -2.138 30.668 57.529 1.00 72.41 ? 607 SER B CB 1 ATOM 4139 O OG . SER B 2 108 ? -1.836 30.337 56.176 1.00 73.84 ? 607 SER B OG 1 ATOM 4140 N N . GLU B 2 109 ? -0.373 33.281 56.429 1.00 63.51 ? 608 GLU B N 1 ATOM 4141 C CA . GLU B 2 109 ? -0.317 34.482 55.619 1.00 57.52 ? 608 GLU B CA 1 ATOM 4142 C C . GLU B 2 109 ? 0.090 35.614 56.537 1.00 54.83 ? 608 GLU B C 1 ATOM 4143 O O . GLU B 2 109 ? -0.739 36.350 57.058 1.00 54.90 ? 608 GLU B O 1 ATOM 4144 C CB . GLU B 2 109 ? -1.663 34.754 54.949 1.00 56.75 ? 608 GLU B CB 1 ATOM 4145 C CG . GLU B 2 109 ? -1.920 33.849 53.745 1.00 55.26 ? 608 GLU B CG 1 ATOM 4146 C CD . GLU B 2 109 ? -1.574 34.500 52.412 1.00 53.18 ? 608 GLU B CD 1 ATOM 4147 O OE1 . GLU B 2 109 ? -0.727 35.417 52.389 1.00 52.10 ? 608 GLU B OE1 1 ATOM 4148 O OE2 . GLU B 2 109 ? -2.150 34.081 51.383 1.00 51.43 ? 608 GLU B OE2 1 ATOM 4149 N N . PHE B 2 110 ? 1.395 35.699 56.758 1.00 52.01 ? 609 PHE B N 1 ATOM 4150 C CA . PHE B 2 110 ? 1.998 36.728 57.585 1.00 49.31 ? 609 PHE B CA 1 ATOM 4151 C C . PHE B 2 110 ? 2.481 37.785 56.586 1.00 48.45 ? 609 PHE B C 1 ATOM 4152 O O . PHE B 2 110 ? 3.257 37.489 55.671 1.00 47.44 ? 609 PHE B O 1 ATOM 4153 C CB . PHE B 2 110 ? 3.163 36.124 58.370 1.00 48.73 ? 609 PHE B CB 1 ATOM 4154 C CG . PHE B 2 110 ? 3.753 37.044 59.396 1.00 49.14 ? 609 PHE B CG 1 ATOM 4155 C CD1 . PHE B 2 110 ? 4.702 37.994 59.037 1.00 49.47 ? 609 PHE B CD1 1 ATOM 4156 C CD2 . PHE B 2 110 ? 3.379 36.942 60.731 1.00 48.79 ? 609 PHE B CD2 1 ATOM 4157 C CE1 . PHE B 2 110 ? 5.275 38.827 59.995 1.00 49.49 ? 609 PHE B CE1 1 ATOM 4158 C CE2 . PHE B 2 110 ? 3.946 37.771 61.695 1.00 48.99 ? 609 PHE B CE2 1 ATOM 4159 C CZ . PHE B 2 110 ? 4.897 38.714 61.326 1.00 49.43 ? 609 PHE B CZ 1 ATOM 4160 N N . CYS B 2 111 ? 2.000 39.012 56.755 1.00 46.60 ? 610 CYS B N 1 ATOM 4161 C CA . CYS B 2 111 ? 2.337 40.105 55.853 1.00 44.61 ? 610 CYS B CA 1 ATOM 4162 C C . CYS B 2 111 ? 3.744 40.663 56.066 1.00 43.32 ? 610 CYS B C 1 ATOM 4163 O O . CYS B 2 111 ? 4.039 41.283 57.088 1.00 42.21 ? 610 CYS B O 1 ATOM 4164 C CB . CYS B 2 111 ? 1.294 41.218 55.992 1.00 44.45 ? 610 CYS B CB 1 ATOM 4165 S SG . CYS B 2 111 ? 1.255 42.364 54.611 1.00 44.46 ? 610 CYS B SG 1 ATOM 4166 N N . HIS B 2 112 ? 4.603 40.454 55.076 1.00 40.84 ? 611 HIS B N 1 ATOM 4167 C CA . HIS B 2 112 ? 5.979 40.912 55.153 1.00 40.52 ? 611 HIS B CA 1 ATOM 4168 C C . HIS B 2 112 ? 6.245 42.228 54.431 1.00 39.71 ? 611 HIS B C 1 ATOM 4169 O O . HIS B 2 112 ? 7.132 42.995 54.821 1.00 39.09 ? 611 HIS B O 1 ATOM 4170 C CB . HIS B 2 112 ? 6.908 39.828 54.597 1.00 41.24 ? 611 HIS B CB 1 ATOM 4171 C CG . HIS B 2 112 ? 7.199 38.729 55.569 1.00 42.40 ? 611 HIS B CG 1 ATOM 4172 N ND1 . HIS B 2 112 ? 8.154 38.844 56.555 1.00 43.06 ? 611 HIS B ND1 1 ATOM 4173 C CD2 . HIS B 2 112 ? 6.639 37.507 55.728 1.00 42.67 ? 611 HIS B CD2 1 ATOM 4174 C CE1 . HIS B 2 112 ? 8.172 37.739 57.280 1.00 42.63 ? 611 HIS B CE1 1 ATOM 4175 N NE2 . HIS B 2 112 ? 7.262 36.912 56.799 1.00 42.00 ? 611 HIS B NE2 1 ATOM 4176 N N . LEU B 2 113 ? 5.475 42.500 53.386 1.00 38.74 ? 612 LEU B N 1 ATOM 4177 C CA . LEU B 2 113 ? 5.693 43.714 52.620 1.00 38.02 ? 612 LEU B CA 1 ATOM 4178 C C . LEU B 2 113 ? 4.529 44.010 51.694 1.00 37.96 ? 612 LEU B C 1 ATOM 4179 O O . LEU B 2 113 ? 3.875 43.094 51.187 1.00 38.46 ? 612 LEU B O 1 ATOM 4180 C CB . LEU B 2 113 ? 6.995 43.565 51.823 1.00 37.65 ? 612 LEU B CB 1 ATOM 4181 C CG . LEU B 2 113 ? 7.529 44.616 50.845 1.00 37.55 ? 612 LEU B CG 1 ATOM 4182 C CD1 . LEU B 2 113 ? 6.790 44.509 49.536 1.00 37.93 ? 612 LEU B CD1 1 ATOM 4183 C CD2 . LEU B 2 113 ? 7.417 46.005 51.447 1.00 35.77 ? 612 LEU B CD2 1 ATOM 4184 N N . VAL B 2 114 ? 4.269 45.301 51.501 1.00 37.45 ? 613 VAL B N 1 ATOM 4185 C CA . VAL B 2 114 ? 3.201 45.777 50.630 1.00 36.51 ? 613 VAL B CA 1 ATOM 4186 C C . VAL B 2 114 ? 3.519 47.188 50.161 1.00 36.12 ? 613 VAL B C 1 ATOM 4187 O O . VAL B 2 114 ? 3.330 48.144 50.899 1.00 36.46 ? 613 VAL B O 1 ATOM 4188 C CB . VAL B 2 114 ? 1.833 45.816 51.342 1.00 34.80 ? 613 VAL B CB 1 ATOM 4189 C CG1 . VAL B 2 114 ? 0.806 46.480 50.438 1.00 35.84 ? 613 VAL B CG1 1 ATOM 4190 C CG2 . VAL B 2 114 ? 1.377 44.419 51.677 1.00 32.93 ? 613 VAL B CG2 1 ATOM 4191 N N . GLU B 2 115 ? 4.012 47.302 48.933 1.00 37.18 ? 614 GLU B N 1 ATOM 4192 C CA . GLU B 2 115 ? 4.354 48.589 48.337 1.00 36.73 ? 614 GLU B CA 1 ATOM 4193 C C . GLU B 2 115 ? 3.360 48.890 47.224 1.00 35.98 ? 614 GLU B C 1 ATOM 4194 O O . GLU B 2 115 ? 3.094 48.032 46.377 1.00 35.57 ? 614 GLU B O 1 ATOM 4195 C CB . GLU B 2 115 ? 5.750 48.534 47.741 1.00 39.62 ? 614 GLU B CB 1 ATOM 4196 C CG . GLU B 2 115 ? 6.772 49.350 48.467 1.00 43.03 ? 614 GLU B CG 1 ATOM 4197 C CD . GLU B 2 115 ? 8.038 49.467 47.662 1.00 44.96 ? 614 GLU B CD 1 ATOM 4198 O OE1 . GLU B 2 115 ? 8.681 48.422 47.423 1.00 45.95 ? 614 GLU B OE1 1 ATOM 4199 O OE2 . GLU B 2 115 ? 8.380 50.600 47.259 1.00 45.18 ? 614 GLU B OE2 1 ATOM 4200 N N . CYS B 2 116 ? 2.824 50.107 47.208 1.00 34.73 ? 615 CYS B N 1 ATOM 4201 C CA . CYS B 2 116 ? 1.848 50.467 46.189 1.00 34.57 ? 615 CYS B CA 1 ATOM 4202 C C . CYS B 2 116 ? 2.210 51.713 45.401 1.00 34.84 ? 615 CYS B C 1 ATOM 4203 O O . CYS B 2 116 ? 3.157 52.432 45.737 1.00 34.25 ? 615 CYS B O 1 ATOM 4204 C CB . CYS B 2 116 ? 0.474 50.661 46.825 1.00 32.58 ? 615 CYS B CB 1 ATOM 4205 S SG . CYS B 2 116 ? -0.042 49.304 47.889 1.00 34.80 ? 615 CYS B SG 1 ATOM 4206 N N . ASP B 2 117 ? 1.433 51.954 44.347 1.00 34.10 ? 616 ASP B N 1 ATOM 4207 C CA . ASP B 2 117 ? 1.621 53.103 43.477 1.00 34.49 ? 616 ASP B CA 1 ATOM 4208 C C . ASP B 2 117 ? 3.035 53.114 42.901 1.00 35.38 ? 616 ASP B C 1 ATOM 4209 O O . ASP B 2 117 ? 3.712 54.142 42.902 1.00 34.01 ? 616 ASP B O 1 ATOM 4210 C CB . ASP B 2 117 ? 1.358 54.396 44.247 1.00 33.68 ? 616 ASP B CB 1 ATOM 4211 C CG . ASP B 2 117 ? 0.122 54.311 45.124 1.00 35.49 ? 616 ASP B CG 1 ATOM 4212 O OD1 . ASP B 2 117 ? -0.954 53.917 44.618 1.00 33.76 ? 616 ASP B OD1 1 ATOM 4213 O OD2 . ASP B 2 117 ? 0.230 54.642 46.327 1.00 35.31 ? 616 ASP B OD2 1 ATOM 4214 N N . LEU B 2 118 ? 3.465 51.951 42.417 1.00 35.82 ? 617 LEU B N 1 ATOM 4215 C CA . LEU B 2 118 ? 4.780 51.777 41.814 1.00 36.57 ? 617 LEU B CA 1 ATOM 4216 C C . LEU B 2 118 ? 4.625 51.892 40.310 1.00 37.60 ? 617 LEU B C 1 ATOM 4217 O O . LEU B 2 118 ? 3.680 51.347 39.746 1.00 37.92 ? 617 LEU B O 1 ATOM 4218 C CB . LEU B 2 118 ? 5.330 50.385 42.127 1.00 37.39 ? 617 LEU B CB 1 ATOM 4219 C CG . LEU B 2 118 ? 5.939 50.074 43.490 1.00 39.00 ? 617 LEU B CG 1 ATOM 4220 C CD1 . LEU B 2 118 ? 5.927 48.571 43.725 1.00 39.24 ? 617 LEU B CD1 1 ATOM 4221 C CD2 . LEU B 2 118 ? 7.357 50.624 43.543 1.00 38.83 ? 617 LEU B CD2 1 ATOM 4222 N N . LYS B 2 119 ? 5.539 52.595 39.654 1.00 38.55 ? 618 LYS B N 1 ATOM 4223 C CA . LYS B 2 119 ? 5.461 52.706 38.207 1.00 40.40 ? 618 LYS B CA 1 ATOM 4224 C C . LYS B 2 119 ? 6.762 52.209 37.584 1.00 41.18 ? 618 LYS B C 1 ATOM 4225 O O . LYS B 2 119 ? 7.831 52.275 38.198 1.00 41.17 ? 618 LYS B O 1 ATOM 4226 C CB . LYS B 2 119 ? 5.161 54.149 37.777 1.00 41.20 ? 618 LYS B CB 1 ATOM 4227 C CG . LYS B 2 119 ? 6.208 55.163 38.165 1.00 48.19 ? 618 LYS B CG 1 ATOM 4228 C CD . LYS B 2 119 ? 5.921 56.518 37.526 1.00 53.04 ? 618 LYS B CD 1 ATOM 4229 C CE . LYS B 2 119 ? 6.843 57.622 38.075 1.00 56.45 ? 618 LYS B CE 1 ATOM 4230 N NZ . LYS B 2 119 ? 6.602 57.967 39.524 1.00 57.18 ? 618 LYS B NZ 1 ATOM 4231 N N . LEU B 2 120 ? 6.663 51.691 36.369 1.00 41.43 ? 619 LEU B N 1 ATOM 4232 C CA . LEU B 2 120 ? 7.821 51.170 35.666 1.00 43.95 ? 619 LEU B CA 1 ATOM 4233 C C . LEU B 2 120 ? 8.695 52.259 35.047 1.00 46.84 ? 619 LEU B C 1 ATOM 4234 O O . LEU B 2 120 ? 8.186 53.226 34.484 1.00 47.43 ? 619 LEU B O 1 ATOM 4235 C CB . LEU B 2 120 ? 7.355 50.210 34.569 1.00 41.77 ? 619 LEU B CB 1 ATOM 4236 C CG . LEU B 2 120 ? 6.814 48.857 35.034 1.00 41.64 ? 619 LEU B CG 1 ATOM 4237 C CD1 . LEU B 2 120 ? 5.933 48.219 33.963 1.00 37.77 ? 619 LEU B CD1 1 ATOM 4238 C CD2 . LEU B 2 120 ? 7.995 47.963 35.383 1.00 41.57 ? 619 LEU B CD2 1 ATOM 4239 N N . LEU B 2 121 ? 10.011 52.107 35.165 1.00 49.71 ? 620 LEU B N 1 ATOM 4240 C CA . LEU B 2 121 ? 10.939 53.053 34.557 1.00 52.81 ? 620 LEU B CA 1 ATOM 4241 C C . LEU B 2 121 ? 10.823 52.817 33.053 1.00 56.33 ? 620 LEU B C 1 ATOM 4242 O O . LEU B 2 121 ? 10.869 53.749 32.256 1.00 58.18 ? 620 LEU B O 1 ATOM 4243 C CB . LEU B 2 121 ? 12.375 52.768 34.996 1.00 50.89 ? 620 LEU B CB 1 ATOM 4244 C CG . LEU B 2 121 ? 12.757 53.027 36.454 1.00 51.29 ? 620 LEU B CG 1 ATOM 4245 C CD1 . LEU B 2 121 ? 14.083 52.351 36.759 1.00 50.74 ? 620 LEU B CD1 1 ATOM 4246 C CD2 . LEU B 2 121 ? 12.848 54.522 36.709 1.00 50.18 ? 620 LEU B CD2 1 ATOM 4247 N N . ASN B 2 122 ? 10.659 51.550 32.685 1.00 60.73 ? 621 ASN B N 1 ATOM 4248 C CA . ASN B 2 122 ? 10.534 51.136 31.290 1.00 64.74 ? 621 ASN B CA 1 ATOM 4249 C C . ASN B 2 122 ? 11.690 51.672 30.452 1.00 65.75 ? 621 ASN B C 1 ATOM 4250 O O . ASN B 2 122 ? 12.836 51.251 30.623 1.00 66.74 ? 621 ASN B O 1 ATOM 4251 C CB . ASN B 2 122 ? 9.198 51.612 30.705 1.00 68.30 ? 621 ASN B CB 1 ATOM 4252 C CG . ASN B 2 122 ? 8.953 51.082 29.292 1.00 71.88 ? 621 ASN B CG 1 ATOM 4253 O OD1 . ASN B 2 122 ? 9.694 51.401 28.356 1.00 73.75 ? 621 ASN B OD1 1 ATOM 4254 N ND2 . ASN B 2 122 ? 7.909 50.266 29.135 1.00 71.06 ? 621 ASN B ND2 1 ATOM 4255 N N . THR B 2 132 ? 5.420 40.051 20.120 1.00 70.96 ? 631 THR B N 1 ATOM 4256 C CA . THR B 2 132 ? 6.178 41.152 19.532 1.00 70.33 ? 631 THR B CA 1 ATOM 4257 C C . THR B 2 132 ? 6.646 42.150 20.596 1.00 69.39 ? 631 THR B C 1 ATOM 4258 O O . THR B 2 132 ? 7.708 42.766 20.465 1.00 69.95 ? 631 THR B O 1 ATOM 4259 C CB . THR B 2 132 ? 5.337 41.898 18.463 1.00 70.53 ? 631 THR B CB 1 ATOM 4260 O OG1 . THR B 2 132 ? 6.039 43.073 18.036 1.00 70.71 ? 631 THR B OG1 1 ATOM 4261 C CG2 . THR B 2 132 ? 3.972 42.286 19.023 1.00 70.37 ? 631 THR B CG2 1 ATOM 4262 N N . GLU B 2 133 ? 5.852 42.303 21.651 1.00 66.98 ? 632 GLU B N 1 ATOM 4263 C CA . GLU B 2 133 ? 6.193 43.217 22.731 1.00 63.41 ? 632 GLU B CA 1 ATOM 4264 C C . GLU B 2 133 ? 7.112 42.516 23.728 1.00 59.52 ? 632 GLU B C 1 ATOM 4265 O O . GLU B 2 133 ? 6.908 41.347 24.077 1.00 57.57 ? 632 GLU B O 1 ATOM 4266 C CB . GLU B 2 133 ? 4.922 43.687 23.446 1.00 66.54 ? 632 GLU B CB 1 ATOM 4267 C CG . GLU B 2 133 ? 3.923 44.392 22.553 1.00 70.18 ? 632 GLU B CG 1 ATOM 4268 C CD . GLU B 2 133 ? 4.356 45.794 22.195 1.00 72.67 ? 632 GLU B CD 1 ATOM 4269 O OE1 . GLU B 2 133 ? 5.533 45.971 21.819 1.00 74.63 ? 632 GLU B OE1 1 ATOM 4270 O OE2 . GLU B 2 133 ? 3.520 46.718 22.284 1.00 73.14 ? 632 GLU B OE2 1 ATOM 4271 N N . PHE B 2 134 ? 8.126 43.240 24.183 1.00 54.43 ? 633 PHE B N 1 ATOM 4272 C CA . PHE B 2 134 ? 9.074 42.702 25.142 1.00 49.85 ? 633 PHE B CA 1 ATOM 4273 C C . PHE B 2 134 ? 9.860 43.822 25.800 1.00 47.56 ? 633 PHE B C 1 ATOM 4274 O O . PHE B 2 134 ? 10.247 44.785 25.140 1.00 47.97 ? 633 PHE B O 1 ATOM 4275 C CB . PHE B 2 134 ? 10.061 41.754 24.451 1.00 47.80 ? 633 PHE B CB 1 ATOM 4276 C CG . PHE B 2 134 ? 11.211 41.336 25.331 1.00 44.78 ? 633 PHE B CG 1 ATOM 4277 C CD1 . PHE B 2 134 ? 11.098 40.230 26.171 1.00 44.11 ? 633 PHE B CD1 1 ATOM 4278 C CD2 . PHE B 2 134 ? 12.382 42.093 25.370 1.00 42.43 ? 633 PHE B CD2 1 ATOM 4279 C CE1 . PHE B 2 134 ? 12.133 39.886 27.041 1.00 42.80 ? 633 PHE B CE1 1 ATOM 4280 C CE2 . PHE B 2 134 ? 13.417 41.760 26.233 1.00 42.01 ? 633 PHE B CE2 1 ATOM 4281 C CZ . PHE B 2 134 ? 13.294 40.654 27.073 1.00 42.04 ? 633 PHE B CZ 1 ATOM 4282 N N . PHE B 2 135 ? 10.097 43.689 27.101 1.00 44.16 ? 634 PHE B N 1 ATOM 4283 C CA . PHE B 2 135 ? 10.881 44.671 27.836 1.00 40.97 ? 634 PHE B CA 1 ATOM 4284 C C . PHE B 2 135 ? 11.127 44.238 29.267 1.00 40.04 ? 634 PHE B C 1 ATOM 4285 O O . PHE B 2 135 ? 10.297 43.569 29.885 1.00 40.57 ? 634 PHE B O 1 ATOM 4286 C CB . PHE B 2 135 ? 10.207 46.052 27.819 1.00 39.20 ? 634 PHE B CB 1 ATOM 4287 C CG . PHE B 2 135 ? 8.933 46.133 28.620 1.00 36.36 ? 634 PHE B CG 1 ATOM 4288 C CD1 . PHE B 2 135 ? 8.965 46.167 30.008 1.00 35.60 ? 634 PHE B CD1 1 ATOM 4289 C CD2 . PHE B 2 135 ? 7.699 46.183 27.978 1.00 35.78 ? 634 PHE B CD2 1 ATOM 4290 C CE1 . PHE B 2 135 ? 7.789 46.249 30.747 1.00 36.40 ? 634 PHE B CE1 1 ATOM 4291 C CE2 . PHE B 2 135 ? 6.518 46.266 28.704 1.00 34.94 ? 634 PHE B CE2 1 ATOM 4292 C CZ . PHE B 2 135 ? 6.562 46.300 30.093 1.00 36.05 ? 634 PHE B CZ 1 ATOM 4293 N N . ALA B 2 136 ? 12.288 44.617 29.779 1.00 37.44 ? 635 ALA B N 1 ATOM 4294 C CA . ALA B 2 136 ? 12.667 44.312 31.140 1.00 37.15 ? 635 ALA B CA 1 ATOM 4295 C C . ALA B 2 136 ? 12.848 45.667 31.794 1.00 37.96 ? 635 ALA B C 1 ATOM 4296 O O . ALA B 2 136 ? 13.562 46.515 31.271 1.00 38.37 ? 635 ALA B O 1 ATOM 4297 C CB . ALA B 2 136 ? 13.969 43.537 31.166 1.00 36.86 ? 635 ALA B CB 1 ATOM 4298 N N . SER B 2 137 ? 12.197 45.877 32.931 1.00 38.69 ? 636 SER B N 1 ATOM 4299 C CA . SER B 2 137 ? 12.306 47.148 33.619 1.00 38.05 ? 636 SER B CA 1 ATOM 4300 C C . SER B 2 137 ? 12.235 47.039 35.128 1.00 38.59 ? 636 SER B C 1 ATOM 4301 O O . SER B 2 137 ? 11.591 46.151 35.678 1.00 36.95 ? 636 SER B O 1 ATOM 4302 C CB . SER B 2 137 ? 11.204 48.098 33.140 1.00 39.42 ? 636 SER B CB 1 ATOM 4303 O OG . SER B 2 137 ? 11.187 49.287 33.919 1.00 37.54 ? 636 SER B OG 1 ATOM 4304 N N . GLU B 2 138 ? 12.912 47.965 35.793 1.00 41.41 ? 637 GLU B N 1 ATOM 4305 C CA . GLU B 2 138 ? 12.903 48.024 37.241 1.00 43.86 ? 637 GLU B CA 1 ATOM 4306 C C . GLU B 2 138 ? 11.806 49.016 37.597 1.00 43.73 ? 637 GLU B C 1 ATOM 4307 O O . GLU B 2 138 ? 11.206 49.627 36.712 1.00 42.34 ? 637 GLU B O 1 ATOM 4308 C CB . GLU B 2 138 ? 14.248 48.511 37.759 1.00 45.95 ? 637 GLU B CB 1 ATOM 4309 C CG . GLU B 2 138 ? 15.391 47.611 37.351 1.00 53.04 ? 637 GLU B CG 1 ATOM 4310 C CD . GLU B 2 138 ? 16.686 47.985 38.028 1.00 57.38 ? 637 GLU B CD 1 ATOM 4311 O OE1 . GLU B 2 138 ? 17.128 49.144 37.855 1.00 57.88 ? 637 GLU B OE1 1 ATOM 4312 O OE2 . GLU B 2 138 ? 17.255 47.117 38.733 1.00 60.12 ? 637 GLU B OE2 1 ATOM 4313 N N . PHE B 2 139 ? 11.539 49.183 38.882 1.00 43.68 ? 638 PHE B N 1 ATOM 4314 C CA . PHE B 2 139 ? 10.492 50.099 39.286 1.00 44.60 ? 638 PHE B CA 1 ATOM 4315 C C . PHE B 2 139 ? 11.021 51.447 39.731 1.00 45.75 ? 638 PHE B C 1 ATOM 4316 O O . PHE B 2 139 ? 12.174 51.573 40.150 1.00 45.16 ? 638 PHE B O 1 ATOM 4317 C CB . PHE B 2 139 ? 9.671 49.474 40.408 1.00 43.90 ? 638 PHE B CB 1 ATOM 4318 C CG . PHE B 2 139 ? 8.967 48.228 39.999 1.00 45.26 ? 638 PHE B CG 1 ATOM 4319 C CD1 . PHE B 2 139 ? 7.809 48.292 39.236 1.00 45.32 ? 638 PHE B CD1 1 ATOM 4320 C CD2 . PHE B 2 139 ? 9.490 46.982 40.324 1.00 46.42 ? 638 PHE B CD2 1 ATOM 4321 C CE1 . PHE B 2 139 ? 7.180 47.132 38.797 1.00 47.43 ? 638 PHE B CE1 1 ATOM 4322 C CE2 . PHE B 2 139 ? 8.871 45.815 39.888 1.00 47.62 ? 638 PHE B CE2 1 ATOM 4323 C CZ . PHE B 2 139 ? 7.712 45.891 39.121 1.00 47.20 ? 638 PHE B CZ 1 ATOM 4324 N N . ASN B 2 140 ? 10.174 52.461 39.601 1.00 46.75 ? 639 ASN B N 1 ATOM 4325 C CA . ASN B 2 140 ? 10.529 53.793 40.043 1.00 47.82 ? 639 ASN B CA 1 ATOM 4326 C C . ASN B 2 140 ? 9.936 53.864 41.443 1.00 48.93 ? 639 ASN B C 1 ATOM 4327 O O . ASN B 2 140 ? 8.713 53.949 41.616 1.00 49.00 ? 639 ASN B O 1 ATOM 4328 C CB . ASN B 2 140 ? 9.905 54.852 39.145 1.00 49.68 ? 639 ASN B CB 1 ATOM 4329 C CG . ASN B 2 140 ? 10.358 56.248 39.504 1.00 50.13 ? 639 ASN B CG 1 ATOM 4330 O OD1 . ASN B 2 140 ? 10.051 57.211 38.807 1.00 50.11 ? 639 ASN B OD1 1 ATOM 4331 N ND2 . ASN B 2 140 ? 11.096 56.365 40.603 1.00 51.87 ? 639 ASN B ND2 1 ATOM 4332 N N . THR B 2 141 ? 10.819 53.799 42.433 1.00 49.39 ? 640 THR B N 1 ATOM 4333 C CA . THR B 2 141 ? 10.442 53.808 43.840 1.00 49.70 ? 640 THR B CA 1 ATOM 4334 C C . THR B 2 141 ? 9.937 55.156 44.368 1.00 49.10 ? 640 THR B C 1 ATOM 4335 O O . THR B 2 141 ? 9.242 55.202 45.381 1.00 47.42 ? 640 THR B O 1 ATOM 4336 C CB . THR B 2 141 ? 11.639 53.356 44.699 1.00 50.52 ? 640 THR B CB 1 ATOM 4337 O OG1 . THR B 2 141 ? 11.202 53.093 46.034 1.00 53.72 ? 640 THR B OG1 1 ATOM 4338 C CG2 . THR B 2 141 ? 12.720 54.443 44.726 1.00 50.57 ? 640 THR B CG2 1 ATOM 4339 N N . LYS B 2 142 ? 10.285 56.239 43.677 1.00 49.66 ? 641 LYS B N 1 ATOM 4340 C CA . LYS B 2 142 ? 9.894 57.593 44.071 1.00 51.10 ? 641 LYS B CA 1 ATOM 4341 C C . LYS B 2 142 ? 8.497 57.773 44.675 1.00 51.07 ? 641 LYS B C 1 ATOM 4342 O O . LYS B 2 142 ? 8.315 57.703 45.896 1.00 52.98 ? 641 LYS B O 1 ATOM 4343 C CB . LYS B 2 142 ? 10.029 58.549 42.882 1.00 53.35 ? 641 LYS B CB 1 ATOM 4344 C CG . LYS B 2 142 ? 11.448 58.772 42.408 1.00 55.61 ? 641 LYS B CG 1 ATOM 4345 C CD . LYS B 2 142 ? 12.332 59.265 43.534 1.00 58.82 ? 641 LYS B CD 1 ATOM 4346 C CE . LYS B 2 142 ? 13.787 59.322 43.091 1.00 60.88 ? 641 LYS B CE 1 ATOM 4347 N NZ . LYS B 2 142 ? 14.709 59.571 44.238 1.00 61.67 ? 641 LYS B NZ 1 ATOM 4348 N N . GLY B 2 143 ? 7.512 58.016 43.818 1.00 48.53 ? 642 GLY B N 1 ATOM 4349 C CA . GLY B 2 143 ? 6.163 58.248 44.303 1.00 46.49 ? 642 GLY B CA 1 ATOM 4350 C C . GLY B 2 143 ? 5.378 57.076 44.860 1.00 44.50 ? 642 GLY B C 1 ATOM 4351 O O . GLY B 2 143 ? 4.149 57.112 44.863 1.00 43.75 ? 642 GLY B O 1 ATOM 4352 N N . SER B 2 144 ? 6.055 56.044 45.346 1.00 42.57 ? 643 SER B N 1 ATOM 4353 C CA . SER B 2 144 ? 5.330 54.894 45.876 1.00 43.36 ? 643 SER B CA 1 ATOM 4354 C C . SER B 2 144 ? 4.883 55.110 47.317 1.00 42.24 ? 643 SER B C 1 ATOM 4355 O O . SER B 2 144 ? 5.315 56.055 47.973 1.00 42.39 ? 643 SER B O 1 ATOM 4356 C CB . SER B 2 144 ? 6.195 53.634 45.787 1.00 43.35 ? 643 SER B CB 1 ATOM 4357 O OG . SER B 2 144 ? 7.373 53.769 46.564 1.00 45.21 ? 643 SER B OG 1 ATOM 4358 N N . ASN B 2 145 ? 4.009 54.232 47.798 1.00 41.61 ? 644 ASN B N 1 ATOM 4359 C CA . ASN B 2 145 ? 3.510 54.305 49.166 1.00 41.98 ? 644 ASN B CA 1 ATOM 4360 C C . ASN B 2 145 ? 3.565 52.924 49.803 1.00 42.14 ? 644 ASN B C 1 ATOM 4361 O O . ASN B 2 145 ? 2.920 51.984 49.337 1.00 43.71 ? 644 ASN B O 1 ATOM 4362 C CB . ASN B 2 145 ? 2.062 54.825 49.205 1.00 43.70 ? 644 ASN B CB 1 ATOM 4363 C CG . ASN B 2 145 ? 1.939 56.268 48.726 1.00 45.78 ? 644 ASN B CG 1 ATOM 4364 O OD1 . ASN B 2 145 ? 1.827 56.536 47.527 1.00 46.48 ? 644 ASN B OD1 1 ATOM 4365 N ND2 . ASN B 2 145 ? 1.974 57.205 49.667 1.00 45.02 ? 644 ASN B ND2 1 ATOM 4366 N N . THR B 2 146 ? 4.341 52.806 50.871 1.00 41.11 ? 645 THR B N 1 ATOM 4367 C CA . THR B 2 146 ? 4.479 51.543 51.576 1.00 40.70 ? 645 THR B CA 1 ATOM 4368 C C . THR B 2 146 ? 3.402 51.410 52.648 1.00 40.71 ? 645 THR B C 1 ATOM 4369 O O . THR B 2 146 ? 3.421 52.132 53.639 1.00 43.12 ? 645 THR B O 1 ATOM 4370 C CB . THR B 2 146 ? 5.865 51.443 52.262 1.00 40.41 ? 645 THR B CB 1 ATOM 4371 O OG1 . THR B 2 146 ? 6.898 51.469 51.269 1.00 40.17 ? 645 THR B OG1 1 ATOM 4372 C CG2 . THR B 2 146 ? 5.975 50.156 53.066 1.00 41.45 ? 645 THR B CG2 1 ATOM 4373 N N . LEU B 2 147 ? 2.461 50.497 52.451 1.00 39.76 ? 646 LEU B N 1 ATOM 4374 C CA . LEU B 2 147 ? 1.411 50.285 53.436 1.00 40.11 ? 646 LEU B CA 1 ATOM 4375 C C . LEU B 2 147 ? 1.942 49.432 54.582 1.00 40.85 ? 646 LEU B C 1 ATOM 4376 O O . LEU B 2 147 ? 1.551 49.613 55.732 1.00 41.03 ? 646 LEU B O 1 ATOM 4377 C CB . LEU B 2 147 ? 0.204 49.580 52.811 1.00 40.63 ? 646 LEU B CB 1 ATOM 4378 C CG . LEU B 2 147 ? -0.534 50.278 51.667 1.00 41.74 ? 646 LEU B CG 1 ATOM 4379 C CD1 . LEU B 2 147 ? -1.793 49.487 51.336 1.00 39.68 ? 646 LEU B CD1 1 ATOM 4380 C CD2 . LEU B 2 147 ? -0.883 51.700 52.059 1.00 40.33 ? 646 LEU B CD2 1 ATOM 4381 N N . ILE B 2 148 ? 2.830 48.496 54.258 1.00 42.14 ? 647 ILE B N 1 ATOM 4382 C CA . ILE B 2 148 ? 3.423 47.607 55.255 1.00 43.82 ? 647 ILE B CA 1 ATOM 4383 C C . ILE B 2 148 ? 4.930 47.508 55.029 1.00 45.65 ? 647 ILE B C 1 ATOM 4384 O O . ILE B 2 148 ? 5.378 46.794 54.134 1.00 47.32 ? 647 ILE B O 1 ATOM 4385 C CB . ILE B 2 148 ? 2.811 46.191 55.162 1.00 42.99 ? 647 ILE B CB 1 ATOM 4386 C CG1 . ILE B 2 148 ? 1.313 46.245 55.482 1.00 43.93 ? 647 ILE B CG1 1 ATOM 4387 C CG2 . ILE B 2 148 ? 3.536 45.245 56.101 1.00 42.35 ? 647 ILE B CG2 1 ATOM 4388 C CD1 . ILE B 2 148 ? 0.989 46.692 56.893 1.00 41.35 ? 647 ILE B CD1 1 ATOM 4389 N N . GLU B 2 149 ? 5.711 48.220 55.837 1.00 46.58 ? 648 GLU B N 1 ATOM 4390 C CA . GLU B 2 149 ? 7.164 48.202 55.689 1.00 48.71 ? 648 GLU B CA 1 ATOM 4391 C C . GLU B 2 149 ? 7.729 46.781 55.631 1.00 47.83 ? 648 GLU B C 1 ATOM 4392 O O . GLU B 2 149 ? 7.151 45.843 56.181 1.00 47.41 ? 648 GLU B O 1 ATOM 4393 C CB . GLU B 2 149 ? 7.833 49.004 56.816 1.00 51.48 ? 648 GLU B CB 1 ATOM 4394 C CG . GLU B 2 149 ? 7.520 48.547 58.245 1.00 60.33 ? 648 GLU B CG 1 ATOM 4395 C CD . GLU B 2 149 ? 6.042 48.687 58.638 1.00 64.81 ? 648 GLU B CD 1 ATOM 4396 O OE1 . GLU B 2 149 ? 5.394 49.682 58.232 1.00 65.16 ? 648 GLU B OE1 1 ATOM 4397 O OE2 . GLU B 2 149 ? 5.534 47.805 59.375 1.00 67.13 ? 648 GLU B OE2 1 ATOM 4398 N N . TYR B 2 150 ? 8.859 46.630 54.946 1.00 46.23 ? 649 TYR B N 1 ATOM 4399 C CA . TYR B 2 150 ? 9.495 45.330 54.791 1.00 45.57 ? 649 TYR B CA 1 ATOM 4400 C C . TYR B 2 150 ? 10.023 44.718 56.079 1.00 45.71 ? 649 TYR B C 1 ATOM 4401 O O . TYR B 2 150 ? 10.592 45.403 56.927 1.00 45.02 ? 649 TYR B O 1 ATOM 4402 C CB . TYR B 2 150 ? 10.661 45.416 53.803 1.00 44.83 ? 649 TYR B CB 1 ATOM 4403 C CG . TYR B 2 150 ? 11.374 44.094 53.594 1.00 44.35 ? 649 TYR B CG 1 ATOM 4404 C CD1 . TYR B 2 150 ? 10.856 43.131 52.729 1.00 46.15 ? 649 TYR B CD1 1 ATOM 4405 C CD2 . TYR B 2 150 ? 12.553 43.795 54.276 1.00 43.00 ? 649 TYR B CD2 1 ATOM 4406 C CE1 . TYR B 2 150 ? 11.495 41.898 52.544 1.00 44.78 ? 649 TYR B CE1 1 ATOM 4407 C CE2 . TYR B 2 150 ? 13.199 42.569 54.103 1.00 42.86 ? 649 TYR B CE2 1 ATOM 4408 C CZ . TYR B 2 150 ? 12.664 41.626 53.233 1.00 44.59 ? 649 TYR B CZ 1 ATOM 4409 O OH . TYR B 2 150 ? 13.294 40.415 53.039 1.00 45.07 ? 649 TYR B OH 1 ATOM 4410 N N . MET B 2 151 ? 9.838 43.409 56.195 1.00 46.50 ? 650 MET B N 1 ATOM 4411 C CA . MET B 2 151 ? 10.324 42.641 57.329 1.00 46.33 ? 650 MET B CA 1 ATOM 4412 C C . MET B 2 151 ? 10.782 41.285 56.791 1.00 44.97 ? 650 MET B C 1 ATOM 4413 O O . MET B 2 151 ? 9.976 40.518 56.264 1.00 44.21 ? 650 MET B O 1 ATOM 4414 C CB . MET B 2 151 ? 9.226 42.439 58.363 1.00 48.92 ? 650 MET B CB 1 ATOM 4415 C CG . MET B 2 151 ? 9.758 41.860 59.653 1.00 53.20 ? 650 MET B CG 1 ATOM 4416 S SD . MET B 2 151 ? 8.495 41.621 60.896 1.00 59.07 ? 650 MET B SD 1 ATOM 4417 C CE . MET B 2 151 ? 8.227 39.843 60.721 1.00 58.46 ? 650 MET B CE 1 ATOM 4418 N N . GLY B 2 152 ? 12.078 41.004 56.915 1.00 43.04 ? 651 GLY B N 1 ATOM 4419 C CA . GLY B 2 152 ? 12.627 39.753 56.425 1.00 42.42 ? 651 GLY B CA 1 ATOM 4420 C C . GLY B 2 152 ? 12.113 38.491 57.095 1.00 43.06 ? 651 GLY B C 1 ATOM 4421 O O . GLY B 2 152 ? 11.401 38.558 58.097 1.00 42.54 ? 651 GLY B O 1 ATOM 4422 N N . PRO B 2 153 ? 12.469 37.310 56.560 1.00 43.93 ? 652 PRO B N 1 ATOM 4423 C CA . PRO B 2 153 ? 12.026 36.035 57.129 1.00 44.23 ? 652 PRO B CA 1 ATOM 4424 C C . PRO B 2 153 ? 12.503 35.877 58.565 1.00 45.00 ? 652 PRO B C 1 ATOM 4425 O O . PRO B 2 153 ? 13.619 36.288 58.919 1.00 45.17 ? 652 PRO B O 1 ATOM 4426 C CB . PRO B 2 153 ? 12.659 34.999 56.202 1.00 42.96 ? 652 PRO B CB 1 ATOM 4427 C CG . PRO B 2 153 ? 12.805 35.731 54.916 1.00 43.41 ? 652 PRO B CG 1 ATOM 4428 C CD . PRO B 2 153 ? 13.296 37.080 55.365 1.00 43.16 ? 652 PRO B CD 1 ATOM 4429 N N . ALA B 2 154 ? 11.650 35.280 59.387 1.00 44.71 ? 653 ALA B N 1 ATOM 4430 C CA . ALA B 2 154 ? 11.963 35.057 60.789 1.00 44.46 ? 653 ALA B CA 1 ATOM 4431 C C . ALA B 2 154 ? 11.182 33.845 61.275 1.00 44.23 ? 653 ALA B C 1 ATOM 4432 O O . ALA B 2 154 ? 10.517 33.892 62.316 1.00 43.43 ? 653 ALA B O 1 ATOM 4433 C CB . ALA B 2 154 ? 11.594 36.285 61.603 1.00 44.37 ? 653 ALA B CB 1 ATOM 4434 N N . PRO B 2 155 ? 11.258 32.735 60.524 1.00 43.81 ? 654 PRO B N 1 ATOM 4435 C CA . PRO B 2 155 ? 10.545 31.512 60.893 1.00 45.60 ? 654 PRO B CA 1 ATOM 4436 C C . PRO B 2 155 ? 11.000 30.948 62.239 1.00 47.40 ? 654 PRO B C 1 ATOM 4437 O O . PRO B 2 155 ? 12.181 31.021 62.595 1.00 46.40 ? 654 PRO B O 1 ATOM 4438 C CB . PRO B 2 155 ? 10.854 30.577 59.730 1.00 44.44 ? 654 PRO B CB 1 ATOM 4439 C CG . PRO B 2 155 ? 12.239 30.986 59.349 1.00 43.20 ? 654 PRO B CG 1 ATOM 4440 C CD . PRO B 2 155 ? 12.153 32.491 59.380 1.00 43.10 ? 654 PRO B CD 1 ATOM 4441 N N . PRO B 2 156 ? 10.056 30.389 63.011 1.00 49.31 ? 655 PRO B N 1 ATOM 4442 C CA . PRO B 2 156 ? 10.341 29.805 64.325 1.00 49.94 ? 655 PRO B CA 1 ATOM 4443 C C . PRO B 2 156 ? 11.271 28.598 64.212 1.00 50.37 ? 655 PRO B C 1 ATOM 4444 O O . PRO B 2 156 ? 11.032 27.684 63.421 1.00 50.10 ? 655 PRO B O 1 ATOM 4445 C CB . PRO B 2 156 ? 8.956 29.403 64.834 1.00 50.23 ? 655 PRO B CB 1 ATOM 4446 C CG . PRO B 2 156 ? 8.038 30.359 64.133 1.00 50.47 ? 655 PRO B CG 1 ATOM 4447 C CD . PRO B 2 156 ? 8.608 30.384 62.742 1.00 49.89 ? 655 PRO B CD 1 ATOM 4448 N N . LYS B 2 157 ? 12.332 28.602 65.005 1.00 50.46 ? 656 LYS B N 1 ATOM 4449 C CA . LYS B 2 157 ? 13.283 27.503 65.002 1.00 50.50 ? 656 LYS B CA 1 ATOM 4450 C C . LYS B 2 157 ? 12.536 26.176 65.100 1.00 50.00 ? 656 LYS B C 1 ATOM 4451 O O . LYS B 2 157 ? 11.698 25.994 65.978 1.00 49.96 ? 656 LYS B O 1 ATOM 4452 C CB . LYS B 2 157 ? 14.242 27.650 66.189 1.00 51.26 ? 656 LYS B CB 1 ATOM 4453 C CG . LYS B 2 157 ? 15.260 26.538 66.313 1.00 52.40 ? 656 LYS B CG 1 ATOM 4454 C CD . LYS B 2 157 ? 16.211 26.787 67.470 1.00 54.24 ? 656 LYS B CD 1 ATOM 4455 C CE . LYS B 2 157 ? 17.207 25.647 67.603 1.00 55.28 ? 656 LYS B CE 1 ATOM 4456 N NZ . LYS B 2 157 ? 16.504 24.340 67.767 1.00 56.81 ? 656 LYS B NZ 1 ATOM 4457 N N . GLY B 2 158 ? 12.830 25.259 64.185 1.00 50.32 ? 657 GLY B N 1 ATOM 4458 C CA . GLY B 2 158 ? 12.184 23.956 64.210 1.00 49.63 ? 657 GLY B CA 1 ATOM 4459 C C . GLY B 2 158 ? 10.872 23.830 63.457 1.00 49.45 ? 657 GLY B C 1 ATOM 4460 O O . GLY B 2 158 ? 10.401 22.716 63.228 1.00 48.92 ? 657 GLY B O 1 ATOM 4461 N N . SER B 2 159 ? 10.276 24.951 63.063 1.00 49.09 ? 658 SER B N 1 ATOM 4462 C CA . SER B 2 159 ? 9.004 24.914 62.343 1.00 48.90 ? 658 SER B CA 1 ATOM 4463 C C . SER B 2 159 ? 9.149 24.376 60.924 1.00 48.52 ? 658 SER B C 1 ATOM 4464 O O . SER B 2 159 ? 8.159 24.077 60.257 1.00 48.58 ? 658 SER B O 1 ATOM 4465 C CB . SER B 2 159 ? 8.379 26.308 62.304 1.00 48.39 ? 658 SER B CB 1 ATOM 4466 O OG . SER B 2 159 ? 9.292 27.254 61.785 1.00 49.91 ? 658 SER B OG 1 ATOM 4467 N N . GLY B 2 160 ? 10.388 24.237 60.471 1.00 48.20 ? 659 GLY B N 1 ATOM 4468 C CA . GLY B 2 160 ? 10.620 23.742 59.129 1.00 47.12 ? 659 GLY B CA 1 ATOM 4469 C C . GLY B 2 160 ? 10.756 24.914 58.178 1.00 46.65 ? 659 GLY B C 1 ATOM 4470 O O . GLY B 2 160 ? 10.771 26.066 58.617 1.00 46.35 ? 659 GLY B O 1 ATOM 4471 N N . PRO B 2 161 ? 10.877 24.660 56.869 1.00 45.84 ? 660 PRO B N 1 ATOM 4472 C CA . PRO B 2 161 ? 11.007 25.763 55.914 1.00 44.77 ? 660 PRO B CA 1 ATOM 4473 C C . PRO B 2 161 ? 9.670 26.455 55.654 1.00 42.90 ? 660 PRO B C 1 ATOM 4474 O O . PRO B 2 161 ? 8.604 25.857 55.822 1.00 41.85 ? 660 PRO B O 1 ATOM 4475 C CB . PRO B 2 161 ? 11.554 25.069 54.669 1.00 46.32 ? 660 PRO B CB 1 ATOM 4476 C CG . PRO B 2 161 ? 10.901 23.720 54.739 1.00 44.74 ? 660 PRO B CG 1 ATOM 4477 C CD . PRO B 2 161 ? 11.063 23.359 56.200 1.00 44.87 ? 660 PRO B CD 1 ATOM 4478 N N . HIS B 2 162 ? 9.735 27.722 55.260 1.00 41.94 ? 661 HIS B N 1 ATOM 4479 C CA . HIS B 2 162 ? 8.536 28.495 54.951 1.00 40.07 ? 661 HIS B CA 1 ATOM 4480 C C . HIS B 2 162 ? 8.634 29.027 53.533 1.00 38.46 ? 661 HIS B C 1 ATOM 4481 O O . HIS B 2 162 ? 9.730 29.276 53.022 1.00 36.58 ? 661 HIS B O 1 ATOM 4482 C CB . HIS B 2 162 ? 8.390 29.703 55.879 1.00 42.26 ? 661 HIS B CB 1 ATOM 4483 C CG . HIS B 2 162 ? 8.115 29.358 57.307 1.00 45.18 ? 661 HIS B CG 1 ATOM 4484 N ND1 . HIS B 2 162 ? 7.784 30.312 58.245 1.00 46.49 ? 661 HIS B ND1 1 ATOM 4485 C CD2 . HIS B 2 162 ? 8.121 28.173 57.961 1.00 46.27 ? 661 HIS B CD2 1 ATOM 4486 C CE1 . HIS B 2 162 ? 7.596 29.730 59.415 1.00 47.07 ? 661 HIS B CE1 1 ATOM 4487 N NE2 . HIS B 2 162 ? 7.795 28.432 59.270 1.00 47.75 ? 661 HIS B NE2 1 ATOM 4488 N N . ARG B 2 163 ? 7.481 29.213 52.905 1.00 37.19 ? 662 ARG B N 1 ATOM 4489 C CA . ARG B 2 163 ? 7.434 29.769 51.563 1.00 36.17 ? 662 ARG B CA 1 ATOM 4490 C C . ARG B 2 163 ? 7.313 31.287 51.682 1.00 37.47 ? 662 ARG B C 1 ATOM 4491 O O . ARG B 2 163 ? 6.425 31.798 52.370 1.00 37.68 ? 662 ARG B O 1 ATOM 4492 C CB . ARG B 2 163 ? 6.235 29.221 50.790 1.00 32.58 ? 662 ARG B CB 1 ATOM 4493 C CG . ARG B 2 163 ? 6.415 27.804 50.288 1.00 31.96 ? 662 ARG B CG 1 ATOM 4494 C CD . ARG B 2 163 ? 5.104 27.232 49.791 1.00 29.57 ? 662 ARG B CD 1 ATOM 4495 N NE . ARG B 2 163 ? 4.111 27.192 50.856 1.00 28.22 ? 662 ARG B NE 1 ATOM 4496 C CZ . ARG B 2 163 ? 2.853 26.800 50.689 1.00 30.29 ? 662 ARG B CZ 1 ATOM 4497 N NH1 . ARG B 2 163 ? 2.431 26.408 49.490 1.00 29.08 ? 662 ARG B NH1 1 ATOM 4498 N NH2 . ARG B 2 163 ? 2.013 26.810 51.719 1.00 27.95 ? 662 ARG B NH2 1 ATOM 4499 N N . TYR B 2 164 ? 8.225 32.002 51.033 1.00 37.72 ? 663 TYR B N 1 ATOM 4500 C CA . TYR B 2 164 ? 8.204 33.458 51.034 1.00 37.37 ? 663 TYR B CA 1 ATOM 4501 C C . TYR B 2 164 ? 7.860 33.861 49.608 1.00 37.21 ? 663 TYR B C 1 ATOM 4502 O O . TYR B 2 164 ? 8.711 33.824 48.714 1.00 38.02 ? 663 TYR B O 1 ATOM 4503 C CB . TYR B 2 164 ? 9.566 33.981 51.476 1.00 38.90 ? 663 TYR B CB 1 ATOM 4504 C CG . TYR B 2 164 ? 9.796 33.680 52.933 1.00 41.73 ? 663 TYR B CG 1 ATOM 4505 C CD1 . TYR B 2 164 ? 9.126 34.410 53.920 1.00 43.33 ? 663 TYR B CD1 1 ATOM 4506 C CD2 . TYR B 2 164 ? 10.587 32.599 53.330 1.00 41.78 ? 663 TYR B CD2 1 ATOM 4507 C CE1 . TYR B 2 164 ? 9.229 34.073 55.264 1.00 43.85 ? 663 TYR B CE1 1 ATOM 4508 C CE2 . TYR B 2 164 ? 10.697 32.247 54.678 1.00 43.66 ? 663 TYR B CE2 1 ATOM 4509 C CZ . TYR B 2 164 ? 10.010 32.989 55.639 1.00 44.51 ? 663 TYR B CZ 1 ATOM 4510 O OH . TYR B 2 164 ? 10.071 32.640 56.966 1.00 42.85 ? 663 TYR B OH 1 ATOM 4511 N N . VAL B 2 165 ? 6.597 34.239 49.412 1.00 35.47 ? 664 VAL B N 1 ATOM 4512 C CA . VAL B 2 165 ? 6.078 34.583 48.092 1.00 33.96 ? 664 VAL B CA 1 ATOM 4513 C C . VAL B 2 165 ? 5.933 36.056 47.700 1.00 33.73 ? 664 VAL B C 1 ATOM 4514 O O . VAL B 2 165 ? 5.248 36.830 48.364 1.00 32.98 ? 664 VAL B O 1 ATOM 4515 C CB . VAL B 2 165 ? 4.705 33.898 47.884 1.00 32.59 ? 664 VAL B CB 1 ATOM 4516 C CG1 . VAL B 2 165 ? 4.282 33.984 46.429 1.00 30.99 ? 664 VAL B CG1 1 ATOM 4517 C CG2 . VAL B 2 165 ? 4.783 32.446 48.334 1.00 31.83 ? 664 VAL B CG2 1 ATOM 4518 N N . PHE B 2 166 ? 6.581 36.428 46.597 1.00 33.58 ? 665 PHE B N 1 ATOM 4519 C CA . PHE B 2 166 ? 6.486 37.783 46.068 1.00 33.06 ? 665 PHE B CA 1 ATOM 4520 C C . PHE B 2 166 ? 5.417 37.780 44.978 1.00 32.98 ? 665 PHE B C 1 ATOM 4521 O O . PHE B 2 166 ? 5.389 36.879 44.134 1.00 31.10 ? 665 PHE B O 1 ATOM 4522 C CB . PHE B 2 166 ? 7.814 38.237 45.461 1.00 32.04 ? 665 PHE B CB 1 ATOM 4523 C CG . PHE B 2 166 ? 8.881 38.508 46.474 1.00 32.96 ? 665 PHE B CG 1 ATOM 4524 C CD1 . PHE B 2 166 ? 9.894 37.580 46.705 1.00 31.61 ? 665 PHE B CD1 1 ATOM 4525 C CD2 . PHE B 2 166 ? 8.881 39.699 47.197 1.00 31.06 ? 665 PHE B CD2 1 ATOM 4526 C CE1 . PHE B 2 166 ? 10.894 37.837 47.639 1.00 31.06 ? 665 PHE B CE1 1 ATOM 4527 C CE2 . PHE B 2 166 ? 9.875 39.963 48.132 1.00 31.31 ? 665 PHE B CE2 1 ATOM 4528 C CZ . PHE B 2 166 ? 10.887 39.029 48.354 1.00 30.96 ? 665 PHE B CZ 1 ATOM 4529 N N . LEU B 2 167 ? 4.534 38.777 45.005 1.00 32.65 ? 666 LEU B N 1 ATOM 4530 C CA . LEU B 2 167 ? 3.470 38.889 44.009 1.00 32.95 ? 666 LEU B CA 1 ATOM 4531 C C . LEU B 2 167 ? 3.351 40.314 43.475 1.00 33.79 ? 666 LEU B C 1 ATOM 4532 O O . LEU B 2 167 ? 3.328 41.279 44.248 1.00 34.27 ? 666 LEU B O 1 ATOM 4533 C CB . LEU B 2 167 ? 2.121 38.459 44.596 1.00 30.77 ? 666 LEU B CB 1 ATOM 4534 C CG . LEU B 2 167 ? 2.021 37.054 45.191 1.00 29.04 ? 666 LEU B CG 1 ATOM 4535 C CD1 . LEU B 2 167 ? 2.307 37.126 46.675 1.00 28.74 ? 666 LEU B CD1 1 ATOM 4536 C CD2 . LEU B 2 167 ? 0.637 36.491 44.972 1.00 28.14 ? 666 LEU B CD2 1 ATOM 4537 N N . LEU B 2 168 ? 3.282 40.440 42.151 1.00 32.95 ? 667 LEU B N 1 ATOM 4538 C CA . LEU B 2 168 ? 3.157 41.744 41.516 1.00 32.32 ? 667 LEU B CA 1 ATOM 4539 C C . LEU B 2 168 ? 1.735 41.928 40.985 1.00 32.76 ? 667 LEU B C 1 ATOM 4540 O O . LEU B 2 168 ? 1.255 41.128 40.178 1.00 32.08 ? 667 LEU B O 1 ATOM 4541 C CB . LEU B 2 168 ? 4.161 41.882 40.366 1.00 31.31 ? 667 LEU B CB 1 ATOM 4542 C CG . LEU B 2 168 ? 4.171 43.247 39.669 1.00 30.14 ? 667 LEU B CG 1 ATOM 4543 C CD1 . LEU B 2 168 ? 4.713 44.283 40.630 1.00 29.79 ? 667 LEU B CD1 1 ATOM 4544 C CD2 . LEU B 2 168 ? 5.026 43.206 38.413 1.00 29.26 ? 667 LEU B CD2 1 ATOM 4545 N N . TYR B 2 169 ? 1.061 42.978 41.447 1.00 32.03 ? 668 TYR B N 1 ATOM 4546 C CA . TYR B 2 169 ? -0.302 43.255 41.003 1.00 31.11 ? 668 TYR B CA 1 ATOM 4547 C C . TYR B 2 169 ? -0.414 44.568 40.243 1.00 32.65 ? 668 TYR B C 1 ATOM 4548 O O . TYR B 2 169 ? 0.309 45.524 40.522 1.00 33.70 ? 668 TYR B O 1 ATOM 4549 C CB . TYR B 2 169 ? -1.260 43.327 42.191 1.00 28.18 ? 668 TYR B CB 1 ATOM 4550 C CG . TYR B 2 169 ? -1.522 42.021 42.892 1.00 26.80 ? 668 TYR B CG 1 ATOM 4551 C CD1 . TYR B 2 169 ? -0.703 41.591 43.935 1.00 25.13 ? 668 TYR B CD1 1 ATOM 4552 C CD2 . TYR B 2 169 ? -2.607 41.221 42.526 1.00 26.26 ? 668 TYR B CD2 1 ATOM 4553 C CE1 . TYR B 2 169 ? -0.960 40.394 44.603 1.00 26.76 ? 668 TYR B CE1 1 ATOM 4554 C CE2 . TYR B 2 169 ? -2.873 40.022 43.179 1.00 26.28 ? 668 TYR B CE2 1 ATOM 4555 C CZ . TYR B 2 169 ? -2.047 39.613 44.222 1.00 27.66 ? 668 TYR B CZ 1 ATOM 4556 O OH . TYR B 2 169 ? -2.321 38.437 44.889 1.00 27.63 ? 668 TYR B OH 1 ATOM 4557 N N . LYS B 2 170 ? -1.323 44.608 39.276 1.00 33.97 ? 669 LYS B N 1 ATOM 4558 C CA . LYS B 2 170 ? -1.569 45.829 38.521 1.00 34.28 ? 669 LYS B CA 1 ATOM 4559 C C . LYS B 2 170 ? -2.789 46.455 39.184 1.00 32.89 ? 669 LYS B C 1 ATOM 4560 O O . LYS B 2 170 ? -3.794 45.777 39.384 1.00 33.44 ? 669 LYS B O 1 ATOM 4561 C CB . LYS B 2 170 ? -1.897 45.524 37.064 1.00 36.37 ? 669 LYS B CB 1 ATOM 4562 C CG . LYS B 2 170 ? -2.282 46.767 36.288 1.00 40.19 ? 669 LYS B CG 1 ATOM 4563 C CD . LYS B 2 170 ? -2.983 46.430 34.989 1.00 44.61 ? 669 LYS B CD 1 ATOM 4564 C CE . LYS B 2 170 ? -3.502 47.696 34.319 1.00 49.26 ? 669 LYS B CE 1 ATOM 4565 N NZ . LYS B 2 170 ? -4.158 47.422 33.004 1.00 54.43 ? 669 LYS B NZ 1 ATOM 4566 N N . GLN B 2 171 ? -2.701 47.732 39.541 1.00 31.57 ? 670 GLN B N 1 ATOM 4567 C CA . GLN B 2 171 ? -3.819 48.417 40.187 1.00 29.81 ? 670 GLN B CA 1 ATOM 4568 C C . GLN B 2 171 ? -4.804 48.909 39.134 1.00 28.53 ? 670 GLN B C 1 ATOM 4569 O O . GLN B 2 171 ? -4.417 49.154 37.995 1.00 26.91 ? 670 GLN B O 1 ATOM 4570 C CB . GLN B 2 171 ? -3.305 49.605 41.005 1.00 28.69 ? 670 GLN B CB 1 ATOM 4571 C CG . GLN B 2 171 ? -2.276 49.218 42.054 1.00 30.84 ? 670 GLN B CG 1 ATOM 4572 C CD . GLN B 2 171 ? -1.664 50.412 42.771 1.00 30.96 ? 670 GLN B CD 1 ATOM 4573 O OE1 . GLN B 2 171 ? -0.711 50.266 43.539 1.00 29.89 ? 670 GLN B OE1 1 ATOM 4574 N NE2 . GLN B 2 171 ? -2.212 51.597 42.528 1.00 32.91 ? 670 GLN B NE2 1 ATOM 4575 N N . PRO B 2 172 ? -6.093 49.049 39.498 1.00 29.42 ? 671 PRO B N 1 ATOM 4576 C CA . PRO B 2 172 ? -7.108 49.526 38.547 1.00 28.96 ? 671 PRO B CA 1 ATOM 4577 C C . PRO B 2 172 ? -6.720 50.951 38.157 1.00 30.19 ? 671 PRO B C 1 ATOM 4578 O O . PRO B 2 172 ? -6.240 51.716 39.002 1.00 30.66 ? 671 PRO B O 1 ATOM 4579 C CB . PRO B 2 172 ? -8.402 49.507 39.366 1.00 28.23 ? 671 PRO B CB 1 ATOM 4580 C CG . PRO B 2 172 ? -8.119 48.566 40.497 1.00 27.16 ? 671 PRO B CG 1 ATOM 4581 C CD . PRO B 2 172 ? -6.683 48.850 40.834 1.00 28.56 ? 671 PRO B CD 1 ATOM 4582 N N . LYS B 2 173 ? -6.932 51.324 36.899 1.00 30.59 ? 672 LYS B N 1 ATOM 4583 C CA . LYS B 2 173 ? -6.556 52.662 36.463 1.00 30.76 ? 672 LYS B CA 1 ATOM 4584 C C . LYS B 2 173 ? -7.161 53.806 37.288 1.00 31.13 ? 672 LYS B C 1 ATOM 4585 O O . LYS B 2 173 ? -8.356 53.816 37.609 1.00 30.80 ? 672 LYS B O 1 ATOM 4586 C CB . LYS B 2 173 ? -6.908 52.863 34.989 1.00 32.14 ? 672 LYS B CB 1 ATOM 4587 C CG . LYS B 2 173 ? -6.467 54.220 34.449 1.00 35.33 ? 672 LYS B CG 1 ATOM 4588 C CD . LYS B 2 173 ? -6.561 54.278 32.937 1.00 40.06 ? 672 LYS B CD 1 ATOM 4589 C CE . LYS B 2 173 ? -5.900 55.536 32.381 1.00 43.07 ? 672 LYS B CE 1 ATOM 4590 N NZ . LYS B 2 173 ? -5.868 55.522 30.885 1.00 44.30 ? 672 LYS B NZ 1 ATOM 4591 N N . GLY B 2 174 ? -6.311 54.769 37.627 1.00 30.27 ? 673 GLY B N 1 ATOM 4592 C CA . GLY B 2 174 ? -6.748 55.923 38.380 1.00 30.28 ? 673 GLY B CA 1 ATOM 4593 C C . GLY B 2 174 ? -6.917 55.763 39.879 1.00 31.09 ? 673 GLY B C 1 ATOM 4594 O O . GLY B 2 174 ? -7.061 56.761 40.583 1.00 33.23 ? 673 GLY B O 1 ATOM 4595 N N . VAL B 2 175 ? -6.911 54.541 40.394 1.00 29.16 ? 674 VAL B N 1 ATOM 4596 C CA . VAL B 2 175 ? -7.085 54.399 41.832 1.00 28.00 ? 674 VAL B CA 1 ATOM 4597 C C . VAL B 2 175 ? -5.779 54.112 42.565 1.00 27.84 ? 674 VAL B C 1 ATOM 4598 O O . VAL B 2 175 ? -5.126 53.101 42.332 1.00 29.11 ? 674 VAL B O 1 ATOM 4599 C CB . VAL B 2 175 ? -8.178 53.335 42.155 1.00 25.78 ? 674 VAL B CB 1 ATOM 4600 C CG1 . VAL B 2 175 ? -8.652 52.687 40.879 1.00 24.01 ? 674 VAL B CG1 1 ATOM 4601 C CG2 . VAL B 2 175 ? -7.669 52.314 43.143 1.00 22.04 ? 674 VAL B CG2 1 ATOM 4602 N N . ASP B 2 176 ? -5.404 55.041 43.439 1.00 27.02 ? 675 ASP B N 1 ATOM 4603 C CA . ASP B 2 176 ? -4.187 54.947 44.232 1.00 29.27 ? 675 ASP B CA 1 ATOM 4604 C C . ASP B 2 176 ? -4.408 54.077 45.477 1.00 30.59 ? 675 ASP B C 1 ATOM 4605 O O . ASP B 2 176 ? -5.539 53.703 45.794 1.00 28.80 ? 675 ASP B O 1 ATOM 4606 C CB . ASP B 2 176 ? -3.752 56.345 44.653 1.00 30.58 ? 675 ASP B CB 1 ATOM 4607 C CG . ASP B 2 176 ? -4.772 57.012 45.553 1.00 34.07 ? 675 ASP B CG 1 ATOM 4608 O OD1 . ASP B 2 176 ? -4.431 57.311 46.719 1.00 35.70 ? 675 ASP B OD1 1 ATOM 4609 O OD2 . ASP B 2 176 ? -5.918 57.225 45.094 1.00 34.01 ? 675 ASP B OD2 1 ATOM 4610 N N . SER B 2 177 ? -3.329 53.780 46.196 1.00 32.19 ? 676 SER B N 1 ATOM 4611 C CA . SER B 2 177 ? -3.420 52.922 47.377 1.00 34.74 ? 676 SER B CA 1 ATOM 4612 C C . SER B 2 177 ? -4.217 53.462 48.565 1.00 36.01 ? 676 SER B C 1 ATOM 4613 O O . SER B 2 177 ? -4.616 52.690 49.440 1.00 37.04 ? 676 SER B O 1 ATOM 4614 C CB . SER B 2 177 ? -2.015 52.513 47.845 1.00 34.93 ? 676 SER B CB 1 ATOM 4615 O OG . SER B 2 177 ? -1.226 53.626 48.225 1.00 35.17 ? 676 SER B OG 1 ATOM 4616 N N . SER B 2 178 ? -4.458 54.769 48.604 1.00 35.90 ? 677 SER B N 1 ATOM 4617 C CA . SER B 2 178 ? -5.216 55.346 49.710 1.00 36.16 ? 677 SER B CA 1 ATOM 4618 C C . SER B 2 178 ? -6.648 54.809 49.739 1.00 36.71 ? 677 SER B C 1 ATOM 4619 O O . SER B 2 178 ? -7.384 55.042 50.692 1.00 37.34 ? 677 SER B O 1 ATOM 4620 C CB . SER B 2 178 ? -5.255 56.874 49.602 1.00 37.23 ? 677 SER B CB 1 ATOM 4621 O OG . SER B 2 178 ? -6.136 57.303 48.573 1.00 37.32 ? 677 SER B OG 1 ATOM 4622 N N . LYS B 2 179 ? -7.036 54.083 48.696 1.00 37.51 ? 678 LYS B N 1 ATOM 4623 C CA . LYS B 2 179 ? -8.385 53.534 48.609 1.00 38.29 ? 678 LYS B CA 1 ATOM 4624 C C . LYS B 2 179 ? -8.479 52.028 48.837 1.00 38.99 ? 678 LYS B C 1 ATOM 4625 O O . LYS B 2 179 ? -9.565 51.449 48.776 1.00 38.25 ? 678 LYS B O 1 ATOM 4626 C CB . LYS B 2 179 ? -8.994 53.906 47.257 1.00 37.01 ? 678 LYS B CB 1 ATOM 4627 C CG . LYS B 2 179 ? -9.191 55.403 47.130 1.00 37.46 ? 678 LYS B CG 1 ATOM 4628 C CD . LYS B 2 179 ? -9.487 55.836 45.720 1.00 36.36 ? 678 LYS B CD 1 ATOM 4629 C CE . LYS B 2 179 ? -9.728 57.334 45.670 1.00 35.27 ? 678 LYS B CE 1 ATOM 4630 N NZ . LYS B 2 179 ? -8.544 58.098 46.131 1.00 34.22 ? 678 LYS B NZ 1 ATOM 4631 N N . PHE B 2 180 ? -7.346 51.391 49.108 1.00 39.67 ? 679 PHE B N 1 ATOM 4632 C CA . PHE B 2 180 ? -7.357 49.957 49.354 1.00 40.57 ? 679 PHE B CA 1 ATOM 4633 C C . PHE B 2 180 ? -7.718 49.684 50.805 1.00 40.67 ? 679 PHE B C 1 ATOM 4634 O O . PHE B 2 180 ? -7.404 50.481 51.685 1.00 40.98 ? 679 PHE B O 1 ATOM 4635 C CB . PHE B 2 180 ? -5.990 49.344 49.038 1.00 39.29 ? 679 PHE B CB 1 ATOM 4636 C CG . PHE B 2 180 ? -5.587 49.477 47.599 1.00 37.94 ? 679 PHE B CG 1 ATOM 4637 C CD1 . PHE B 2 180 ? -6.551 49.566 46.600 1.00 35.80 ? 679 PHE B CD1 1 ATOM 4638 C CD2 . PHE B 2 180 ? -4.243 49.490 47.237 1.00 38.31 ? 679 PHE B CD2 1 ATOM 4639 C CE1 . PHE B 2 180 ? -6.187 49.667 45.263 1.00 35.56 ? 679 PHE B CE1 1 ATOM 4640 C CE2 . PHE B 2 180 ? -3.867 49.589 45.897 1.00 37.71 ? 679 PHE B CE2 1 ATOM 4641 C CZ . PHE B 2 180 ? -4.844 49.678 44.907 1.00 35.55 ? 679 PHE B CZ 1 ATOM 4642 N N . SER B 2 181 ? -8.388 48.564 51.047 1.00 41.35 ? 680 SER B N 1 ATOM 4643 C CA . SER B 2 181 ? -8.780 48.182 52.398 1.00 43.20 ? 680 SER B CA 1 ATOM 4644 C C . SER B 2 181 ? -7.563 48.181 53.319 1.00 45.51 ? 680 SER B C 1 ATOM 4645 O O . SER B 2 181 ? -6.459 47.827 52.913 1.00 46.22 ? 680 SER B O 1 ATOM 4646 C CB . SER B 2 181 ? -9.426 46.798 52.380 1.00 42.17 ? 680 SER B CB 1 ATOM 4647 O OG . SER B 2 181 ? -8.626 45.877 51.658 1.00 42.89 ? 680 SER B OG 1 ATOM 4648 N N . LYS B 2 182 ? -7.767 48.581 54.564 1.00 48.26 ? 681 LYS B N 1 ATOM 4649 C CA . LYS B 2 182 ? -6.674 48.640 55.523 1.00 51.80 ? 681 LYS B CA 1 ATOM 4650 C C . LYS B 2 182 ? -6.157 47.251 55.907 1.00 51.58 ? 681 LYS B C 1 ATOM 4651 O O . LYS B 2 182 ? -6.832 46.241 55.697 1.00 50.51 ? 681 LYS B O 1 ATOM 4652 C CB . LYS B 2 182 ? -7.139 49.392 56.775 1.00 54.90 ? 681 LYS B CB 1 ATOM 4653 C CG . LYS B 2 182 ? -6.028 49.811 57.721 1.00 58.66 ? 681 LYS B CG 1 ATOM 4654 C CD . LYS B 2 182 ? -6.593 50.634 58.879 1.00 62.74 ? 681 LYS B CD 1 ATOM 4655 C CE . LYS B 2 182 ? -5.493 51.115 59.819 1.00 64.73 ? 681 LYS B CE 1 ATOM 4656 N NZ . LYS B 2 182 ? -4.710 49.979 60.393 1.00 65.58 ? 681 LYS B NZ 1 ATOM 4657 N N . ILE B 2 183 ? -4.947 47.212 56.454 1.00 51.84 ? 682 ILE B N 1 ATOM 4658 C CA . ILE B 2 183 ? -4.343 45.961 56.896 1.00 52.74 ? 682 ILE B CA 1 ATOM 4659 C C . ILE B 2 183 ? -4.040 46.089 58.387 1.00 53.25 ? 682 ILE B C 1 ATOM 4660 O O . ILE B 2 183 ? -2.986 46.598 58.771 1.00 51.35 ? 682 ILE B O 1 ATOM 4661 C CB . ILE B 2 183 ? -3.034 45.662 56.129 1.00 53.15 ? 682 ILE B CB 1 ATOM 4662 C CG1 . ILE B 2 183 ? -3.336 45.454 54.643 1.00 52.96 ? 682 ILE B CG1 1 ATOM 4663 C CG2 . ILE B 2 183 ? -2.365 44.418 56.694 1.00 51.84 ? 682 ILE B CG2 1 ATOM 4664 C CD1 . ILE B 2 183 ? -2.094 45.333 53.775 1.00 53.01 ? 682 ILE B CD1 1 ATOM 4665 N N . LYS B 2 184 ? -4.988 45.639 59.211 1.00 54.66 ? 683 LYS B N 1 ATOM 4666 C CA . LYS B 2 184 ? -4.880 45.683 60.670 1.00 56.61 ? 683 LYS B CA 1 ATOM 4667 C C . LYS B 2 184 ? -3.432 45.473 61.091 1.00 55.93 ? 683 LYS B C 1 ATOM 4668 O O . LYS B 2 184 ? -2.799 46.366 61.653 1.00 54.15 ? 683 LYS B O 1 ATOM 4669 C CB . LYS B 2 184 ? -5.771 44.598 61.280 1.00 60.92 ? 683 LYS B CB 1 ATOM 4670 C CG . LYS B 2 184 ? -5.793 44.544 62.808 1.00 66.43 ? 683 LYS B CG 1 ATOM 4671 C CD . LYS B 2 184 ? -6.769 43.466 63.296 1.00 69.80 ? 683 LYS B CD 1 ATOM 4672 C CE . LYS B 2 184 ? -6.995 43.521 64.805 1.00 71.95 ? 683 LYS B CE 1 ATOM 4673 N NZ . LYS B 2 184 ? -8.084 42.584 65.238 1.00 73.11 ? 683 LYS B NZ 1 ATOM 4674 N N . ASP B 2 185 ? -2.919 44.278 60.822 1.00 55.68 ? 684 ASP B N 1 ATOM 4675 C CA . ASP B 2 185 ? -1.535 43.953 61.125 1.00 55.35 ? 684 ASP B CA 1 ATOM 4676 C C . ASP B 2 185 ? -1.104 42.708 60.354 1.00 53.26 ? 684 ASP B C 1 ATOM 4677 O O . ASP B 2 185 ? -1.853 42.199 59.519 1.00 53.07 ? 684 ASP B O 1 ATOM 4678 C CB . ASP B 2 185 ? -1.317 43.799 62.639 1.00 57.46 ? 684 ASP B CB 1 ATOM 4679 C CG . ASP B 2 185 ? -2.116 42.672 63.240 1.00 59.89 ? 684 ASP B CG 1 ATOM 4680 O OD1 . ASP B 2 185 ? -3.286 42.485 62.840 1.00 61.03 ? 684 ASP B OD1 1 ATOM 4681 O OD2 . ASP B 2 185 ? -1.572 41.984 64.130 1.00 60.77 ? 684 ASP B OD2 1 ATOM 4682 N N . ARG B 2 186 ? 0.098 42.222 60.639 1.00 51.07 ? 685 ARG B N 1 ATOM 4683 C CA . ARG B 2 186 ? 0.676 41.086 59.928 1.00 48.67 ? 685 ARG B CA 1 ATOM 4684 C C . ARG B 2 186 ? 0.026 39.708 60.034 1.00 49.07 ? 685 ARG B C 1 ATOM 4685 O O . ARG B 2 186 ? -0.424 39.159 59.026 1.00 48.66 ? 685 ARG B O 1 ATOM 4686 C CB . ARG B 2 186 ? 2.163 41.033 60.262 1.00 45.07 ? 685 ARG B CB 1 ATOM 4687 C CG . ARG B 2 186 ? 2.783 42.376 59.930 1.00 43.12 ? 685 ARG B CG 1 ATOM 4688 C CD . ARG B 2 186 ? 4.278 42.439 60.043 1.00 42.80 ? 685 ARG B CD 1 ATOM 4689 N NE . ARG B 2 186 ? 4.780 43.480 59.153 1.00 42.73 ? 685 ARG B NE 1 ATOM 4690 C CZ . ARG B 2 186 ? 5.878 44.186 59.375 1.00 44.26 ? 685 ARG B CZ 1 ATOM 4691 N NH1 . ARG B 2 186 ? 6.257 45.110 58.507 1.00 43.78 ? 685 ARG B NH1 1 ATOM 4692 N NH2 . ARG B 2 186 ? 6.590 43.974 60.475 1.00 47.37 ? 685 ARG B NH2 1 ATOM 4693 N N . PRO B 2 187 ? -0.028 39.119 61.237 1.00 49.05 ? 686 PRO B N 1 ATOM 4694 C CA . PRO B 2 187 ? -0.665 37.799 61.287 1.00 48.28 ? 686 PRO B CA 1 ATOM 4695 C C . PRO B 2 187 ? -2.054 37.799 60.644 1.00 47.90 ? 686 PRO B C 1 ATOM 4696 O O . PRO B 2 187 ? -2.916 38.602 61.000 1.00 47.83 ? 686 PRO B O 1 ATOM 4697 C CB . PRO B 2 187 ? -0.690 37.482 62.783 1.00 48.04 ? 686 PRO B CB 1 ATOM 4698 C CG . PRO B 2 187 ? -0.590 38.838 63.442 1.00 47.66 ? 686 PRO B CG 1 ATOM 4699 C CD . PRO B 2 187 ? 0.392 39.557 62.577 1.00 47.73 ? 686 PRO B CD 1 ATOM 4700 N N . ASN B 2 188 ? -2.246 36.895 59.687 1.00 47.88 ? 687 ASN B N 1 ATOM 4701 C CA . ASN B 2 188 ? -3.501 36.750 58.947 1.00 48.34 ? 687 ASN B CA 1 ATOM 4702 C C . ASN B 2 188 ? -3.851 38.023 58.186 1.00 49.48 ? 687 ASN B C 1 ATOM 4703 O O . ASN B 2 188 ? -4.983 38.189 57.728 1.00 49.03 ? 687 ASN B O 1 ATOM 4704 C CB . ASN B 2 188 ? -4.663 36.400 59.884 1.00 48.66 ? 687 ASN B CB 1 ATOM 4705 C CG . ASN B 2 188 ? -4.323 35.289 60.849 1.00 48.99 ? 687 ASN B CG 1 ATOM 4706 O OD1 . ASN B 2 188 ? -3.776 35.534 61.924 1.00 49.50 ? 687 ASN B OD1 1 ATOM 4707 N ND2 . ASN B 2 188 ? -4.634 34.056 60.469 1.00 50.61 ? 687 ASN B ND2 1 ATOM 4708 N N . TRP B 2 189 ? -2.876 38.915 58.037 1.00 50.77 ? 688 TRP B N 1 ATOM 4709 C CA . TRP B 2 189 ? -3.107 40.178 57.348 1.00 52.75 ? 688 TRP B CA 1 ATOM 4710 C C . TRP B 2 189 ? -4.208 40.923 58.094 1.00 54.07 ? 688 TRP B C 1 ATOM 4711 O O . TRP B 2 189 ? -4.966 41.701 57.508 1.00 55.05 ? 688 TRP B O 1 ATOM 4712 C CB . TRP B 2 189 ? -3.516 39.941 55.884 1.00 52.38 ? 688 TRP B CB 1 ATOM 4713 C CG . TRP B 2 189 ? -2.351 39.671 54.970 1.00 52.53 ? 688 TRP B CG 1 ATOM 4714 C CD1 . TRP B 2 189 ? -1.394 38.706 55.121 1.00 52.26 ? 688 TRP B CD1 1 ATOM 4715 C CD2 . TRP B 2 189 ? -1.998 40.400 53.785 1.00 52.88 ? 688 TRP B CD2 1 ATOM 4716 N NE1 . TRP B 2 189 ? -0.467 38.793 54.110 1.00 51.81 ? 688 TRP B NE1 1 ATOM 4717 C CE2 . TRP B 2 189 ? -0.812 39.823 53.277 1.00 52.31 ? 688 TRP B CE2 1 ATOM 4718 C CE3 . TRP B 2 189 ? -2.568 41.487 53.105 1.00 52.94 ? 688 TRP B CE3 1 ATOM 4719 C CZ2 . TRP B 2 189 ? -0.184 40.295 52.121 1.00 51.20 ? 688 TRP B CZ2 1 ATOM 4720 C CZ3 . TRP B 2 189 ? -1.942 41.957 51.953 1.00 51.56 ? 688 TRP B CZ3 1 ATOM 4721 C CH2 . TRP B 2 189 ? -0.762 41.359 51.476 1.00 51.71 ? 688 TRP B CH2 1 ATOM 4722 N N . GLY B 2 190 ? -4.285 40.661 59.397 1.00 54.26 ? 689 GLY B N 1 ATOM 4723 C CA . GLY B 2 190 ? -5.276 41.305 60.237 1.00 54.69 ? 689 GLY B CA 1 ATOM 4724 C C . GLY B 2 190 ? -6.711 40.898 59.970 1.00 55.32 ? 689 GLY B C 1 ATOM 4725 O O . GLY B 2 190 ? -7.632 41.641 60.298 1.00 55.67 ? 689 GLY B O 1 ATOM 4726 N N . TYR B 2 191 ? -6.914 39.724 59.384 1.00 55.85 ? 690 TYR B N 1 ATOM 4727 C CA . TYR B 2 191 ? -8.262 39.248 59.090 1.00 56.89 ? 690 TYR B CA 1 ATOM 4728 C C . TYR B 2 191 ? -8.808 38.342 60.185 1.00 58.18 ? 690 TYR B C 1 ATOM 4729 O O . TYR B 2 191 ? -9.974 37.954 60.146 1.00 59.11 ? 690 TYR B O 1 ATOM 4730 C CB . TYR B 2 191 ? -8.282 38.500 57.754 1.00 56.63 ? 690 TYR B CB 1 ATOM 4731 C CG . TYR B 2 191 ? -8.290 39.406 56.546 1.00 56.16 ? 690 TYR B CG 1 ATOM 4732 C CD1 . TYR B 2 191 ? -9.471 39.986 56.097 1.00 55.13 ? 690 TYR B CD1 1 ATOM 4733 C CD2 . TYR B 2 191 ? -7.111 39.706 55.868 1.00 57.01 ? 690 TYR B CD2 1 ATOM 4734 C CE1 . TYR B 2 191 ? -9.481 40.843 55.003 1.00 56.38 ? 690 TYR B CE1 1 ATOM 4735 C CE2 . TYR B 2 191 ? -7.110 40.565 54.772 1.00 56.81 ? 690 TYR B CE2 1 ATOM 4736 C CZ . TYR B 2 191 ? -8.297 41.131 54.346 1.00 56.63 ? 690 TYR B CZ 1 ATOM 4737 O OH . TYR B 2 191 ? -8.297 41.995 53.274 1.00 56.93 ? 690 TYR B OH 1 ATOM 4738 N N . GLY B 2 192 ? -7.969 38.000 61.157 1.00 59.13 ? 691 GLY B N 1 ATOM 4739 C CA . GLY B 2 192 ? -8.420 37.140 62.237 1.00 60.76 ? 691 GLY B CA 1 ATOM 4740 C C . GLY B 2 192 ? -8.473 35.662 61.884 1.00 62.27 ? 691 GLY B C 1 ATOM 4741 O O . GLY B 2 192 ? -7.867 34.839 62.570 1.00 63.55 ? 691 GLY B O 1 ATOM 4742 N N . THR B 2 193 ? -9.196 35.314 60.822 1.00 62.64 ? 692 THR B N 1 ATOM 4743 C CA . THR B 2 193 ? -9.309 33.917 60.404 1.00 63.26 ? 692 THR B CA 1 ATOM 4744 C C . THR B 2 193 ? -7.980 33.359 59.885 1.00 63.34 ? 692 THR B C 1 ATOM 4745 O O . THR B 2 193 ? -7.144 34.099 59.371 1.00 63.68 ? 692 THR B O 1 ATOM 4746 C CB . THR B 2 193 ? -10.381 33.751 59.310 1.00 62.94 ? 692 THR B CB 1 ATOM 4747 O OG1 . THR B 2 193 ? -10.058 34.580 58.189 1.00 63.75 ? 692 THR B OG1 1 ATOM 4748 C CG2 . THR B 2 193 ? -11.740 34.151 59.843 1.00 63.97 ? 692 THR B CG2 1 ATOM 4749 N N . PRO B 2 194 ? -7.767 32.039 60.027 1.00 63.52 ? 693 PRO B N 1 ATOM 4750 C CA . PRO B 2 194 ? -6.532 31.387 59.570 1.00 62.92 ? 693 PRO B CA 1 ATOM 4751 C C . PRO B 2 194 ? -6.503 31.142 58.061 1.00 61.62 ? 693 PRO B C 1 ATOM 4752 O O . PRO B 2 194 ? -7.552 30.986 57.424 1.00 61.53 ? 693 PRO B O 1 ATOM 4753 C CB . PRO B 2 194 ? -6.521 30.067 60.352 1.00 63.13 ? 693 PRO B CB 1 ATOM 4754 C CG . PRO B 2 194 ? -7.412 30.337 61.529 1.00 63.37 ? 693 PRO B CG 1 ATOM 4755 C CD . PRO B 2 194 ? -8.520 31.133 60.906 1.00 63.76 ? 693 PRO B CD 1 ATOM 4756 N N . ALA B 2 195 ? -5.292 31.102 57.507 1.00 58.99 ? 694 ALA B N 1 ATOM 4757 C CA . ALA B 2 195 ? -5.082 30.862 56.080 1.00 56.46 ? 694 ALA B CA 1 ATOM 4758 C C . ALA B 2 195 ? -5.723 31.910 55.176 1.00 54.91 ? 694 ALA B C 1 ATOM 4759 O O . ALA B 2 195 ? -6.346 31.574 54.165 1.00 54.01 ? 694 ALA B O 1 ATOM 4760 C CB . ALA B 2 195 ? -5.587 29.470 55.706 1.00 54.58 ? 694 ALA B CB 1 ATOM 4761 N N . THR B 2 196 ? -5.565 33.179 55.532 1.00 52.99 ? 695 THR B N 1 ATOM 4762 C CA . THR B 2 196 ? -6.134 34.251 54.727 1.00 52.46 ? 695 THR B CA 1 ATOM 4763 C C . THR B 2 196 ? -5.113 35.375 54.547 1.00 50.81 ? 695 THR B C 1 ATOM 4764 O O . THR B 2 196 ? -4.393 35.724 55.483 1.00 49.77 ? 695 THR B O 1 ATOM 4765 C CB . THR B 2 196 ? -7.419 34.815 55.381 1.00 52.74 ? 695 THR B CB 1 ATOM 4766 O OG1 . THR B 2 196 ? -7.089 35.414 56.637 1.00 55.86 ? 695 THR B OG1 1 ATOM 4767 C CG2 . THR B 2 196 ? -8.436 33.701 55.619 1.00 51.42 ? 695 THR B CG2 1 ATOM 4768 N N . GLY B 2 197 ? -5.048 35.934 53.342 1.00 49.29 ? 696 GLY B N 1 ATOM 4769 C CA . GLY B 2 197 ? -4.097 37.004 53.092 1.00 47.84 ? 696 GLY B CA 1 ATOM 4770 C C . GLY B 2 197 ? -4.216 37.680 51.736 1.00 47.12 ? 696 GLY B C 1 ATOM 4771 O O . GLY B 2 197 ? -5.272 38.212 51.390 1.00 47.70 ? 696 GLY B O 1 ATOM 4772 N N . VAL B 2 198 ? -3.130 37.655 50.966 1.00 45.49 ? 697 VAL B N 1 ATOM 4773 C CA . VAL B 2 198 ? -3.100 38.293 49.653 1.00 44.98 ? 697 VAL B CA 1 ATOM 4774 C C . VAL B 2 198 ? -4.310 37.975 48.791 1.00 44.19 ? 697 VAL B C 1 ATOM 4775 O O . VAL B 2 198 ? -4.805 38.839 48.074 1.00 44.32 ? 697 VAL B O 1 ATOM 4776 C CB . VAL B 2 198 ? -1.814 37.922 48.862 1.00 43.90 ? 697 VAL B CB 1 ATOM 4777 C CG1 . VAL B 2 198 ? -0.599 38.202 49.708 1.00 45.24 ? 697 VAL B CG1 1 ATOM 4778 C CG2 . VAL B 2 198 ? -1.840 36.468 48.444 1.00 42.31 ? 697 VAL B CG2 1 ATOM 4779 N N . GLY B 2 199 ? -4.784 36.736 48.860 1.00 44.37 ? 698 GLY B N 1 ATOM 4780 C CA . GLY B 2 199 ? -5.932 36.347 48.064 1.00 45.03 ? 698 GLY B CA 1 ATOM 4781 C C . GLY B 2 199 ? -7.151 37.175 48.408 1.00 46.38 ? 698 GLY B C 1 ATOM 4782 O O . GLY B 2 199 ? -7.770 37.765 47.529 1.00 48.06 ? 698 GLY B O 1 ATOM 4783 N N . LYS B 2 200 ? -7.487 37.211 49.693 1.00 48.00 ? 699 LYS B N 1 ATOM 4784 C CA . LYS B 2 200 ? -8.630 37.965 50.198 1.00 50.26 ? 699 LYS B CA 1 ATOM 4785 C C . LYS B 2 200 ? -8.491 39.457 49.884 1.00 50.45 ? 699 LYS B C 1 ATOM 4786 O O . LYS B 2 200 ? -9.367 40.061 49.255 1.00 50.50 ? 699 LYS B O 1 ATOM 4787 C CB . LYS B 2 200 ? -8.733 37.776 51.713 1.00 52.85 ? 699 LYS B CB 1 ATOM 4788 C CG . LYS B 2 200 ? -9.891 38.498 52.378 1.00 56.76 ? 699 LYS B CG 1 ATOM 4789 C CD . LYS B 2 200 ? -11.213 37.905 51.930 1.00 61.08 ? 699 LYS B CD 1 ATOM 4790 C CE . LYS B 2 200 ? -12.377 38.412 52.766 1.00 61.75 ? 699 LYS B CE 1 ATOM 4791 N NZ . LYS B 2 200 ? -13.643 37.739 52.350 1.00 62.98 ? 699 LYS B NZ 1 ATOM 4792 N N . TRP B 2 201 ? -7.377 40.033 50.327 1.00 48.85 ? 700 TRP B N 1 ATOM 4793 C CA . TRP B 2 201 ? -7.086 41.451 50.138 1.00 48.09 ? 700 TRP B CA 1 ATOM 4794 C C . TRP B 2 201 ? -7.016 41.894 48.677 1.00 47.44 ? 700 TRP B C 1 ATOM 4795 O O . TRP B 2 201 ? -7.501 42.971 48.332 1.00 48.01 ? 700 TRP B O 1 ATOM 4796 C CB . TRP B 2 201 ? -5.768 41.802 50.832 1.00 46.83 ? 700 TRP B CB 1 ATOM 4797 C CG . TRP B 2 201 ? -5.479 43.264 50.882 1.00 45.74 ? 700 TRP B CG 1 ATOM 4798 C CD1 . TRP B 2 201 ? -6.082 44.191 51.680 1.00 46.67 ? 700 TRP B CD1 1 ATOM 4799 C CD2 . TRP B 2 201 ? -4.498 43.973 50.112 1.00 45.13 ? 700 TRP B CD2 1 ATOM 4800 N NE1 . TRP B 2 201 ? -5.534 45.435 51.460 1.00 45.53 ? 700 TRP B NE1 1 ATOM 4801 C CE2 . TRP B 2 201 ? -4.561 45.329 50.502 1.00 44.91 ? 700 TRP B CE2 1 ATOM 4802 C CE3 . TRP B 2 201 ? -3.572 43.595 49.132 1.00 43.74 ? 700 TRP B CE3 1 ATOM 4803 C CZ2 . TRP B 2 201 ? -3.734 46.307 49.945 1.00 43.81 ? 700 TRP B CZ2 1 ATOM 4804 C CZ3 . TRP B 2 201 ? -2.750 44.568 48.579 1.00 42.99 ? 700 TRP B CZ3 1 ATOM 4805 C CH2 . TRP B 2 201 ? -2.837 45.908 48.989 1.00 44.12 ? 700 TRP B CH2 1 ATOM 4806 N N . ALA B 2 202 ? -6.409 41.075 47.823 1.00 46.26 ? 701 ALA B N 1 ATOM 4807 C CA . ALA B 2 202 ? -6.280 41.420 46.411 1.00 46.34 ? 701 ALA B CA 1 ATOM 4808 C C . ALA B 2 202 ? -7.630 41.465 45.708 1.00 46.89 ? 701 ALA B C 1 ATOM 4809 O O . ALA B 2 202 ? -7.851 42.293 44.823 1.00 46.23 ? 701 ALA B O 1 ATOM 4810 C CB . ALA B 2 202 ? -5.362 40.429 45.709 1.00 44.55 ? 701 ALA B CB 1 ATOM 4811 N N . LYS B 2 203 ? -8.531 40.572 46.103 1.00 48.19 ? 702 LYS B N 1 ATOM 4812 C CA . LYS B 2 203 ? -9.854 40.516 45.499 1.00 49.36 ? 702 LYS B CA 1 ATOM 4813 C C . LYS B 2 203 ? -10.743 41.684 45.892 1.00 48.67 ? 702 LYS B C 1 ATOM 4814 O O . LYS B 2 203 ? -11.367 42.304 45.032 1.00 47.86 ? 702 LYS B O 1 ATOM 4815 C CB . LYS B 2 203 ? -10.551 39.202 45.858 1.00 51.75 ? 702 LYS B CB 1 ATOM 4816 C CG . LYS B 2 203 ? -10.251 38.073 44.894 1.00 56.63 ? 702 LYS B CG 1 ATOM 4817 C CD . LYS B 2 203 ? -10.765 38.409 43.490 1.00 60.90 ? 702 LYS B CD 1 ATOM 4818 C CE . LYS B 2 203 ? -10.403 37.322 42.469 1.00 62.93 ? 702 LYS B CE 1 ATOM 4819 N NZ . LYS B 2 203 ? -10.911 37.625 41.094 1.00 63.62 ? 702 LYS B NZ 1 ATOM 4820 N N . GLU B 2 204 ? -10.806 41.990 47.183 1.00 48.18 ? 703 GLU B N 1 ATOM 4821 C CA . GLU B 2 204 ? -11.649 43.092 47.622 1.00 48.22 ? 703 GLU B CA 1 ATOM 4822 C C . GLU B 2 204 ? -11.137 44.443 47.140 1.00 47.52 ? 703 GLU B C 1 ATOM 4823 O O . GLU B 2 204 ? -11.782 45.463 47.344 1.00 49.42 ? 703 GLU B O 1 ATOM 4824 C CB . GLU B 2 204 ? -11.809 43.089 49.153 1.00 48.61 ? 703 GLU B CB 1 ATOM 4825 C CG . GLU B 2 204 ? -10.527 43.140 49.969 1.00 50.82 ? 703 GLU B CG 1 ATOM 4826 C CD . GLU B 2 204 ? -10.794 43.054 51.474 1.00 51.74 ? 703 GLU B CD 1 ATOM 4827 O OE1 . GLU B 2 204 ? -11.508 42.122 51.906 1.00 51.83 ? 703 GLU B OE1 1 ATOM 4828 O OE2 . GLU B 2 204 ? -10.289 43.913 52.226 1.00 51.89 ? 703 GLU B OE2 1 ATOM 4829 N N . ASN B 2 205 ? -9.983 44.450 46.483 1.00 45.88 ? 704 ASN B N 1 ATOM 4830 C CA . ASN B 2 205 ? -9.423 45.694 45.982 1.00 43.03 ? 704 ASN B CA 1 ATOM 4831 C C . ASN B 2 205 ? -9.245 45.682 44.470 1.00 42.53 ? 704 ASN B C 1 ATOM 4832 O O . ASN B 2 205 ? -8.587 46.548 43.904 1.00 43.76 ? 704 ASN B O 1 ATOM 4833 C CB . ASN B 2 205 ? -8.094 45.984 46.675 1.00 42.58 ? 704 ASN B CB 1 ATOM 4834 C CG . ASN B 2 205 ? -8.277 46.451 48.106 1.00 41.24 ? 704 ASN B CG 1 ATOM 4835 O OD1 . ASN B 2 205 ? -8.849 47.512 48.350 1.00 40.19 ? 704 ASN B OD1 1 ATOM 4836 N ND2 . ASN B 2 205 ? -7.792 45.660 49.062 1.00 39.29 ? 704 ASN B ND2 1 ATOM 4837 N N . ASN B 2 206 ? -9.830 44.687 43.820 1.00 41.47 ? 705 ASN B N 1 ATOM 4838 C CA . ASN B 2 206 ? -9.764 44.574 42.373 1.00 41.90 ? 705 ASN B CA 1 ATOM 4839 C C . ASN B 2 206 ? -8.369 44.641 41.776 1.00 40.72 ? 705 ASN B C 1 ATOM 4840 O O . ASN B 2 206 ? -8.175 45.276 40.743 1.00 40.40 ? 705 ASN B O 1 ATOM 4841 C CB . ASN B 2 206 ? -10.623 45.666 41.746 1.00 45.18 ? 705 ASN B CB 1 ATOM 4842 C CG . ASN B 2 206 ? -12.059 45.612 42.219 1.00 49.24 ? 705 ASN B CG 1 ATOM 4843 O OD1 . ASN B 2 206 ? -12.708 46.646 42.384 1.00 50.95 ? 705 ASN B OD1 1 ATOM 4844 N ND2 . ASN B 2 206 ? -12.571 44.400 42.432 1.00 50.95 ? 705 ASN B ND2 1 ATOM 4845 N N . LEU B 2 207 ? -7.397 43.990 42.409 1.00 40.34 ? 706 LEU B N 1 ATOM 4846 C CA . LEU B 2 207 ? -6.034 43.996 41.881 1.00 38.81 ? 706 LEU B CA 1 ATOM 4847 C C . LEU B 2 207 ? -5.857 42.842 40.901 1.00 38.32 ? 706 LEU B C 1 ATOM 4848 O O . LEU B 2 207 ? -6.442 41.780 41.073 1.00 38.16 ? 706 LEU B O 1 ATOM 4849 C CB . LEU B 2 207 ? -5.013 43.880 43.014 1.00 37.62 ? 706 LEU B CB 1 ATOM 4850 C CG . LEU B 2 207 ? -5.115 44.915 44.138 1.00 37.26 ? 706 LEU B CG 1 ATOM 4851 C CD1 . LEU B 2 207 ? -3.835 44.887 44.950 1.00 35.33 ? 706 LEU B CD1 1 ATOM 4852 C CD2 . LEU B 2 207 ? -5.340 46.303 43.565 1.00 36.32 ? 706 LEU B CD2 1 ATOM 4853 N N . GLN B 2 208 ? -5.056 43.058 39.867 1.00 38.55 ? 707 GLN B N 1 ATOM 4854 C CA . GLN B 2 208 ? -4.823 42.032 38.859 1.00 38.39 ? 707 GLN B CA 1 ATOM 4855 C C . GLN B 2 208 ? -3.422 41.439 39.006 1.00 36.43 ? 707 GLN B C 1 ATOM 4856 O O . GLN B 2 208 ? -2.431 42.131 38.786 1.00 35.89 ? 707 GLN B O 1 ATOM 4857 C CB . GLN B 2 208 ? -4.972 42.642 37.464 1.00 40.57 ? 707 GLN B CB 1 ATOM 4858 C CG . GLN B 2 208 ? -5.192 41.630 36.346 1.00 46.56 ? 707 GLN B CG 1 ATOM 4859 C CD . GLN B 2 208 ? -4.988 42.234 34.964 1.00 49.04 ? 707 GLN B CD 1 ATOM 4860 O OE1 . GLN B 2 208 ? -5.450 43.339 34.678 1.00 50.87 ? 707 GLN B OE1 1 ATOM 4861 N NE2 . GLN B 2 208 ? -4.296 41.504 34.098 1.00 51.25 ? 707 GLN B NE2 1 ATOM 4862 N N . LEU B 2 209 ? -3.346 40.163 39.378 1.00 35.21 ? 708 LEU B N 1 ATOM 4863 C CA . LEU B 2 209 ? -2.063 39.472 39.541 1.00 33.62 ? 708 LEU B CA 1 ATOM 4864 C C . LEU B 2 209 ? -1.345 39.409 38.196 1.00 32.32 ? 708 LEU B C 1 ATOM 4865 O O . LEU B 2 209 ? -1.928 38.985 37.203 1.00 33.32 ? 708 LEU B O 1 ATOM 4866 C CB . LEU B 2 209 ? -2.284 38.043 40.037 1.00 32.97 ? 708 LEU B CB 1 ATOM 4867 C CG . LEU B 2 209 ? -1.284 37.445 41.034 1.00 35.61 ? 708 LEU B CG 1 ATOM 4868 C CD1 . LEU B 2 209 ? -1.211 35.934 40.825 1.00 34.55 ? 708 LEU B CD1 1 ATOM 4869 C CD2 . LEU B 2 209 ? 0.085 38.066 40.861 1.00 36.72 ? 708 LEU B CD2 1 ATOM 4870 N N . VAL B 2 210 ? -0.082 39.817 38.161 1.00 31.53 ? 709 VAL B N 1 ATOM 4871 C CA . VAL B 2 210 ? 0.677 39.793 36.916 1.00 31.76 ? 709 VAL B CA 1 ATOM 4872 C C . VAL B 2 210 ? 1.882 38.857 36.953 1.00 30.64 ? 709 VAL B C 1 ATOM 4873 O O . VAL B 2 210 ? 2.228 38.256 35.938 1.00 29.89 ? 709 VAL B O 1 ATOM 4874 C CB . VAL B 2 210 ? 1.148 41.224 36.523 1.00 33.07 ? 709 VAL B CB 1 ATOM 4875 C CG1 . VAL B 2 210 ? 2.173 41.163 35.399 1.00 32.83 ? 709 VAL B CG1 1 ATOM 4876 C CG2 . VAL B 2 210 ? -0.043 42.042 36.061 1.00 34.83 ? 709 VAL B CG2 1 ATOM 4877 N N . ALA B 2 211 ? 2.519 38.728 38.115 1.00 29.85 ? 710 ALA B N 1 ATOM 4878 C CA . ALA B 2 211 ? 3.690 37.864 38.235 1.00 30.08 ? 710 ALA B CA 1 ATOM 4879 C C . ALA B 2 211 ? 3.965 37.428 39.667 1.00 29.99 ? 710 ALA B C 1 ATOM 4880 O O . ALA B 2 211 ? 3.399 37.976 40.616 1.00 28.82 ? 710 ALA B O 1 ATOM 4881 C CB . ALA B 2 211 ? 4.913 38.571 37.673 1.00 30.60 ? 710 ALA B CB 1 ATOM 4882 N N . SER B 2 212 ? 4.846 36.438 39.809 1.00 30.16 ? 711 SER B N 1 ATOM 4883 C CA . SER B 2 212 ? 5.216 35.909 41.119 1.00 28.83 ? 711 SER B CA 1 ATOM 4884 C C . SER B 2 212 ? 6.516 35.095 41.126 1.00 28.00 ? 711 SER B C 1 ATOM 4885 O O . SER B 2 212 ? 6.821 34.380 40.179 1.00 28.04 ? 711 SER B O 1 ATOM 4886 C CB . SER B 2 212 ? 4.086 35.038 41.662 1.00 28.82 ? 711 SER B CB 1 ATOM 4887 O OG . SER B 2 212 ? 4.445 34.479 42.913 1.00 31.86 ? 711 SER B OG 1 ATOM 4888 N N . ASN B 2 213 ? 7.275 35.223 42.205 1.00 28.19 ? 712 ASN B N 1 ATOM 4889 C CA . ASN B 2 213 ? 8.519 34.487 42.391 1.00 29.25 ? 712 ASN B CA 1 ATOM 4890 C C . ASN B 2 213 ? 8.528 34.118 43.873 1.00 31.42 ? 712 ASN B C 1 ATOM 4891 O O . ASN B 2 213 ? 7.748 34.666 44.647 1.00 33.34 ? 712 ASN B O 1 ATOM 4892 C CB . ASN B 2 213 ? 9.726 35.367 42.075 1.00 28.55 ? 712 ASN B CB 1 ATOM 4893 C CG . ASN B 2 213 ? 10.982 34.557 41.767 1.00 26.35 ? 712 ASN B CG 1 ATOM 4894 O OD1 . ASN B 2 213 ? 11.071 33.378 42.092 1.00 27.07 ? 712 ASN B OD1 1 ATOM 4895 N ND2 . ASN B 2 213 ? 11.959 35.198 41.147 1.00 25.09 ? 712 ASN B ND2 1 ATOM 4896 N N . PHE B 2 214 ? 9.392 33.199 44.284 1.00 32.64 ? 713 PHE B N 1 ATOM 4897 C CA . PHE B 2 214 ? 9.421 32.826 45.691 1.00 34.64 ? 713 PHE B CA 1 ATOM 4898 C C . PHE B 2 214 ? 10.680 32.057 46.071 1.00 35.93 ? 713 PHE B C 1 ATOM 4899 O O . PHE B 2 214 ? 11.417 31.571 45.214 1.00 37.47 ? 713 PHE B O 1 ATOM 4900 C CB . PHE B 2 214 ? 8.187 31.987 46.035 1.00 34.04 ? 713 PHE B CB 1 ATOM 4901 C CG . PHE B 2 214 ? 8.261 30.579 45.532 1.00 33.74 ? 713 PHE B CG 1 ATOM 4902 C CD1 . PHE B 2 214 ? 8.396 29.519 46.420 1.00 33.90 ? 713 PHE B CD1 1 ATOM 4903 C CD2 . PHE B 2 214 ? 8.246 30.312 44.170 1.00 33.74 ? 713 PHE B CD2 1 ATOM 4904 C CE1 . PHE B 2 214 ? 8.518 28.214 45.958 1.00 32.42 ? 713 PHE B CE1 1 ATOM 4905 C CE2 . PHE B 2 214 ? 8.367 29.013 43.697 1.00 33.61 ? 713 PHE B CE2 1 ATOM 4906 C CZ . PHE B 2 214 ? 8.505 27.961 44.594 1.00 33.20 ? 713 PHE B CZ 1 ATOM 4907 N N . PHE B 2 215 ? 10.919 31.953 47.371 1.00 36.21 ? 714 PHE B N 1 ATOM 4908 C CA . PHE B 2 215 ? 12.080 31.241 47.869 1.00 35.78 ? 714 PHE B CA 1 ATOM 4909 C C . PHE B 2 215 ? 11.734 30.596 49.205 1.00 36.50 ? 714 PHE B C 1 ATOM 4910 O O . PHE B 2 215 ? 10.653 30.834 49.758 1.00 36.28 ? 714 PHE B O 1 ATOM 4911 C CB . PHE B 2 215 ? 13.275 32.199 48.012 1.00 34.37 ? 714 PHE B CB 1 ATOM 4912 C CG . PHE B 2 215 ? 13.166 33.174 49.162 1.00 34.86 ? 714 PHE B CG 1 ATOM 4913 C CD1 . PHE B 2 215 ? 13.704 32.865 50.409 1.00 35.89 ? 714 PHE B CD1 1 ATOM 4914 C CD2 . PHE B 2 215 ? 12.579 34.425 48.983 1.00 36.00 ? 714 PHE B CD2 1 ATOM 4915 C CE1 . PHE B 2 215 ? 13.667 33.793 51.461 1.00 36.47 ? 714 PHE B CE1 1 ATOM 4916 C CE2 . PHE B 2 215 ? 12.534 35.364 50.029 1.00 36.78 ? 714 PHE B CE2 1 ATOM 4917 C CZ . PHE B 2 215 ? 13.081 35.047 51.268 1.00 36.58 ? 714 PHE B CZ 1 ATOM 4918 N N . TYR B 2 216 ? 12.638 29.755 49.697 1.00 36.12 ? 715 TYR B N 1 ATOM 4919 C CA . TYR B 2 216 ? 12.444 29.082 50.972 1.00 35.68 ? 715 TYR B CA 1 ATOM 4920 C C . TYR B 2 216 ? 13.504 29.552 51.953 1.00 36.37 ? 715 TYR B C 1 ATOM 4921 O O . TYR B 2 216 ? 14.625 29.895 51.571 1.00 35.69 ? 715 TYR B O 1 ATOM 4922 C CB . TYR B 2 216 ? 12.558 27.557 50.832 1.00 33.89 ? 715 TYR B CB 1 ATOM 4923 C CG . TYR B 2 216 ? 11.381 26.848 50.193 1.00 32.01 ? 715 TYR B CG 1 ATOM 4924 C CD1 . TYR B 2 216 ? 11.348 26.603 48.821 1.00 31.85 ? 715 TYR B CD1 1 ATOM 4925 C CD2 . TYR B 2 216 ? 10.324 26.374 50.971 1.00 31.65 ? 715 TYR B CD2 1 ATOM 4926 C CE1 . TYR B 2 216 ? 10.294 25.896 48.237 1.00 32.94 ? 715 TYR B CE1 1 ATOM 4927 C CE2 . TYR B 2 216 ? 9.262 25.667 50.401 1.00 31.74 ? 715 TYR B CE2 1 ATOM 4928 C CZ . TYR B 2 216 ? 9.253 25.430 49.033 1.00 33.96 ? 715 TYR B CZ 1 ATOM 4929 O OH . TYR B 2 216 ? 8.209 24.736 48.458 1.00 33.95 ? 715 TYR B OH 1 ATOM 4930 N N . ALA B 2 217 ? 13.132 29.566 53.224 1.00 37.43 ? 716 ALA B N 1 ATOM 4931 C CA . ALA B 2 217 ? 14.037 29.952 54.291 1.00 39.02 ? 716 ALA B CA 1 ATOM 4932 C C . ALA B 2 217 ? 13.654 29.085 55.481 1.00 41.05 ? 716 ALA B C 1 ATOM 4933 O O . ALA B 2 217 ? 12.486 28.711 55.643 1.00 38.98 ? 716 ALA B O 1 ATOM 4934 C CB . ALA B 2 217 ? 13.875 31.419 54.625 1.00 38.36 ? 716 ALA B CB 1 ATOM 4935 N N . GLU B 2 218 ? 14.639 28.762 56.307 1.00 44.59 ? 717 GLU B N 1 ATOM 4936 C CA . GLU B 2 218 ? 14.398 27.914 57.462 1.00 47.89 ? 717 GLU B CA 1 ATOM 4937 C C . GLU B 2 218 ? 15.336 28.257 58.610 1.00 49.30 ? 717 GLU B C 1 ATOM 4938 O O . GLU B 2 218 ? 16.444 28.747 58.398 1.00 48.21 ? 717 GLU B O 1 ATOM 4939 C CB . GLU B 2 218 ? 14.598 26.450 57.062 1.00 47.60 ? 717 GLU B CB 1 ATOM 4940 C CG . GLU B 2 218 ? 13.945 25.444 57.972 1.00 49.08 ? 717 GLU B CG 1 ATOM 4941 C CD . GLU B 2 218 ? 14.308 24.022 57.606 1.00 50.66 ? 717 GLU B CD 1 ATOM 4942 O OE1 . GLU B 2 218 ? 13.663 23.087 58.126 1.00 50.76 ? 717 GLU B OE1 1 ATOM 4943 O OE2 . GLU B 2 218 ? 15.248 23.838 56.803 1.00 52.51 ? 717 GLU B OE2 1 ATOM 4944 N N . THR B 2 219 ? 14.871 28.015 59.829 1.00 53.33 ? 718 THR B N 1 ATOM 4945 C CA . THR B 2 219 ? 15.674 28.253 61.023 1.00 56.42 ? 718 THR B CA 1 ATOM 4946 C C . THR B 2 219 ? 15.796 26.909 61.729 1.00 58.69 ? 718 THR B C 1 ATOM 4947 O O . THR B 2 219 ? 14.802 26.349 62.197 1.00 59.33 ? 718 THR B O 1 ATOM 4948 C CB . THR B 2 219 ? 15.009 29.272 61.970 1.00 56.16 ? 718 THR B CB 1 ATOM 4949 O OG1 . THR B 2 219 ? 15.062 30.579 61.382 1.00 56.25 ? 718 THR B OG1 1 ATOM 4950 C CG2 . THR B 2 219 ? 15.726 29.295 63.311 1.00 55.81 ? 718 THR B CG2 1 ATOM 4951 N N . LYS B 2 220 ? 17.013 26.379 61.779 1.00 61.05 ? 719 LYS B N 1 ATOM 4952 C CA . LYS B 2 220 ? 17.247 25.093 62.419 1.00 63.16 ? 719 LYS B CA 1 ATOM 4953 C C . LYS B 2 220 ? 17.790 25.262 63.830 1.00 64.26 ? 719 LYS B C 1 ATOM 4954 O O . LYS B 2 220 ? 17.213 24.637 64.744 1.00 65.40 ? 719 LYS B O 1 ATOM 4955 C CB . LYS B 2 220 ? 18.211 24.250 61.580 1.00 63.81 ? 719 LYS B CB 1 ATOM 4956 C CG . LYS B 2 220 ? 17.643 23.844 60.225 1.00 65.34 ? 719 LYS B CG 1 ATOM 4957 C CD . LYS B 2 220 ? 18.547 22.860 59.494 1.00 64.28 ? 719 LYS B CD 1 ATOM 4958 C CE . LYS B 2 220 ? 17.881 22.356 58.223 1.00 65.00 ? 719 LYS B CE 1 ATOM 4959 N NZ . LYS B 2 220 ? 16.553 21.724 58.501 1.00 65.17 ? 719 LYS B NZ 1 ATOM 4960 O OXT . LYS B 2 220 ? 18.778 26.010 64.005 1.00 64.65 ? 719 LYS B OXT 1 HETATM 4961 C C1 . NAG C 3 . ? 41.437 -2.015 26.483 1.00 52.86 ? 810 NAG A C1 1 HETATM 4962 C C2 . NAG C 3 . ? 42.718 -2.173 25.659 1.00 54.93 ? 810 NAG A C2 1 HETATM 4963 C C3 . NAG C 3 . ? 42.633 -3.468 24.870 1.00 56.95 ? 810 NAG A C3 1 HETATM 4964 C C4 . NAG C 3 . ? 42.487 -4.626 25.852 1.00 57.48 ? 810 NAG A C4 1 HETATM 4965 C C5 . NAG C 3 . ? 41.255 -4.405 26.749 1.00 56.64 ? 810 NAG A C5 1 HETATM 4966 C C6 . NAG C 3 . ? 41.176 -5.442 27.847 1.00 56.41 ? 810 NAG A C6 1 HETATM 4967 C C7 . NAG C 3 . ? 43.332 0.124 25.233 1.00 55.94 ? 810 NAG A C7 1 HETATM 4968 C C8 . NAG C 3 . ? 44.446 0.127 26.277 1.00 54.46 ? 810 NAG A C8 1 HETATM 4969 N N2 . NAG C 3 . ? 42.919 -1.051 24.762 1.00 54.65 ? 810 NAG A N2 1 HETATM 4970 O O3 . NAG C 3 . ? 43.809 -3.632 24.093 1.00 60.19 ? 810 NAG A O3 1 HETATM 4971 O O4 . NAG C 3 . ? 42.356 -5.846 25.135 1.00 59.08 ? 810 NAG A O4 1 HETATM 4972 O O5 . NAG C 3 . ? 41.316 -3.113 27.404 1.00 55.37 ? 810 NAG A O5 1 HETATM 4973 O O6 . NAG C 3 . ? 40.432 -6.572 27.423 1.00 58.20 ? 810 NAG A O6 1 HETATM 4974 O O7 . NAG C 3 . ? 42.859 1.196 24.844 1.00 55.77 ? 810 NAG A O7 1 HETATM 4975 C C1 . NDG D 4 . ? 49.637 15.555 41.114 1.00 70.11 ? 820 NDG A C1 1 HETATM 4976 C C2 . NDG D 4 . ? 50.979 16.291 41.221 1.00 72.83 ? 820 NDG A C2 1 HETATM 4977 C C3 . NDG D 4 . ? 51.904 15.610 42.240 1.00 74.58 ? 820 NDG A C3 1 HETATM 4978 C C4 . NDG D 4 . ? 51.086 15.032 43.400 1.00 74.99 ? 820 NDG A C4 1 HETATM 4979 C C5 . NDG D 4 . ? 50.071 13.989 42.892 1.00 73.70 ? 820 NDG A C5 1 HETATM 4980 C C6 . NDG D 4 . ? 48.751 14.045 43.631 1.00 72.32 ? 820 NDG A C6 1 HETATM 4981 C C7 . NDG D 4 . ? 52.881 16.738 39.813 1.00 76.52 ? 820 NDG A C7 1 HETATM 4982 C C8 . NDG D 4 . ? 53.966 15.670 39.790 1.00 76.24 ? 820 NDG A C8 1 HETATM 4983 O O . NDG D 4 . ? 49.786 14.175 41.482 1.00 72.02 ? 820 NDG A O 1 HETATM 4984 O O3 . NDG D 4 . ? 52.847 16.553 42.734 1.00 74.39 ? 820 NDG A O3 1 HETATM 4985 O O4 . NDG D 4 . ? 51.958 14.426 44.346 1.00 77.09 ? 820 NDG A O4 1 HETATM 4986 O O6 . NDG D 4 . ? 48.574 12.891 44.436 1.00 71.97 ? 820 NDG A O6 1 HETATM 4987 O O7 . NDG D 4 . ? 53.186 17.929 39.738 1.00 77.55 ? 820 NDG A O7 1 HETATM 4988 N N2 . NDG D 4 . ? 51.622 16.324 39.922 1.00 74.84 ? 820 NDG A N2 1 HETATM 4989 C C1 . NDG E 4 . ? 37.725 12.346 3.999 1.00 68.92 ? 830 NDG A C1 1 HETATM 4990 C C2 . NDG E 4 . ? 36.657 12.338 2.915 1.00 71.90 ? 830 NDG A C2 1 HETATM 4991 C C3 . NDG E 4 . ? 37.168 13.126 1.702 1.00 74.17 ? 830 NDG A C3 1 HETATM 4992 C C4 . NDG E 4 . ? 38.563 12.627 1.250 1.00 74.72 ? 830 NDG A C4 1 HETATM 4993 C C5 . NDG E 4 . ? 39.544 12.446 2.433 1.00 73.81 ? 830 NDG A C5 1 HETATM 4994 C C6 . NDG E 4 . ? 40.082 13.753 3.008 1.00 73.57 ? 830 NDG A C6 1 HETATM 4995 C C7 . NDG E 4 . ? 35.114 10.596 2.312 1.00 76.01 ? 830 NDG A C7 1 HETATM 4996 C C8 . NDG E 4 . ? 34.386 9.896 3.452 1.00 75.78 ? 830 NDG A C8 1 HETATM 4997 O O . NDG E 4 . ? 38.915 11.707 3.514 1.00 72.14 ? 830 NDG A O 1 HETATM 4998 O O3 . NDG E 4 . ? 37.226 14.512 2.017 1.00 74.02 ? 830 NDG A O3 1 HETATM 4999 O O4 . NDG E 4 . ? 38.434 11.395 0.550 1.00 75.88 ? 830 NDG A O4 1 HETATM 5000 O O6 . NDG E 4 . ? 40.299 13.654 4.411 1.00 72.45 ? 830 NDG A O6 1 HETATM 5001 O O7 . NDG E 4 . ? 34.540 10.797 1.240 1.00 76.88 ? 830 NDG A O7 1 HETATM 5002 N N2 . NDG E 4 . ? 36.368 10.970 2.536 1.00 74.02 ? 830 NDG A N2 1 HETATM 5003 S S . SO4 F 5 . ? 20.380 17.812 29.168 1.00 41.73 ? 901 SO4 A S 1 HETATM 5004 O O1 . SO4 F 5 . ? 20.321 16.818 30.259 1.00 43.23 ? 901 SO4 A O1 1 HETATM 5005 O O2 . SO4 F 5 . ? 21.075 19.023 29.638 1.00 44.03 ? 901 SO4 A O2 1 HETATM 5006 O O3 . SO4 F 5 . ? 21.116 17.231 28.033 1.00 44.70 ? 901 SO4 A O3 1 HETATM 5007 O O4 . SO4 F 5 . ? 19.021 18.174 28.735 1.00 42.57 ? 901 SO4 A O4 1 HETATM 5008 S S . SO4 G 5 . ? 7.530 34.652 59.317 1.00 73.88 ? 902 SO4 B S 1 HETATM 5009 O O1 . SO4 G 5 . ? 7.065 35.653 60.294 1.00 75.28 ? 902 SO4 B O1 1 HETATM 5010 O O2 . SO4 G 5 . ? 8.885 35.014 58.860 1.00 73.76 ? 902 SO4 B O2 1 HETATM 5011 O O3 . SO4 G 5 . ? 7.556 33.322 59.955 1.00 75.27 ? 902 SO4 B O3 1 HETATM 5012 O O4 . SO4 G 5 . ? 6.605 34.623 58.171 1.00 73.68 ? 902 SO4 B O4 1 HETATM 5013 O O . HOH H 6 . ? 22.734 15.441 29.941 1.00 29.36 ? 1000 HOH A O 1 HETATM 5014 O O . HOH H 6 . ? 19.925 31.385 15.379 1.00 21.28 ? 1001 HOH A O 1 HETATM 5015 O O . HOH H 6 . ? 20.579 21.427 9.115 1.00 22.51 ? 1002 HOH A O 1 HETATM 5016 O O . HOH H 6 . ? 14.420 -0.106 28.303 1.00 31.35 ? 1003 HOH A O 1 HETATM 5017 O O . HOH H 6 . ? 30.278 3.813 24.171 1.00 21.91 ? 1004 HOH A O 1 HETATM 5018 O O . HOH H 6 . ? 22.214 5.117 15.667 1.00 21.96 ? 1005 HOH A O 1 HETATM 5019 O O . HOH H 6 . ? 19.222 -5.502 39.043 1.00 20.95 ? 1006 HOH A O 1 HETATM 5020 O O . HOH H 6 . ? 25.822 24.867 19.393 1.00 17.81 ? 1007 HOH A O 1 HETATM 5021 O O . HOH H 6 . ? 27.787 2.758 25.194 1.00 22.38 ? 1008 HOH A O 1 HETATM 5022 O O . HOH H 6 . ? 15.553 12.071 42.806 1.00 31.76 ? 1009 HOH A O 1 HETATM 5023 O O . HOH H 6 . ? 17.813 13.799 45.679 1.00 35.04 ? 1010 HOH A O 1 HETATM 5024 O O . HOH H 6 . ? 46.166 6.621 33.681 1.00 28.80 ? 1011 HOH A O 1 HETATM 5025 O O . HOH H 6 . ? 20.448 29.510 46.180 1.00 30.04 ? 1012 HOH A O 1 HETATM 5026 O O . HOH H 6 . ? 30.445 20.211 23.048 1.00 18.96 ? 1013 HOH A O 1 HETATM 5027 O O . HOH H 6 . ? 8.478 19.637 38.180 1.00 31.21 ? 1014 HOH A O 1 HETATM 5028 O O . HOH H 6 . ? 19.425 32.003 33.152 1.00 29.95 ? 1015 HOH A O 1 HETATM 5029 O O . HOH H 6 . ? 12.359 -4.608 44.975 1.00 18.13 ? 1016 HOH A O 1 HETATM 5030 O O . HOH H 6 . ? 22.087 7.766 14.391 1.00 23.38 ? 1017 HOH A O 1 HETATM 5031 O O . HOH H 6 . ? 18.733 9.524 18.994 1.00 27.73 ? 1018 HOH A O 1 HETATM 5032 O O . HOH H 6 . ? 43.835 26.338 48.559 1.00 41.39 ? 1020 HOH A O 1 HETATM 5033 O O . HOH H 6 . ? 26.247 -4.206 40.089 1.00 32.62 ? 1021 HOH A O 1 HETATM 5034 O O . HOH H 6 . ? 11.193 17.876 39.096 1.00 43.26 ? 1022 HOH A O 1 HETATM 5035 O O . HOH H 6 . ? 34.604 31.635 21.728 1.00 24.77 ? 1023 HOH A O 1 HETATM 5036 O O . HOH H 6 . ? 24.575 14.765 37.913 1.00 19.53 ? 1024 HOH A O 1 HETATM 5037 O O . HOH H 6 . ? 23.471 26.778 18.436 1.00 30.81 ? 1025 HOH A O 1 HETATM 5038 O O . HOH H 6 . ? 27.139 14.171 23.160 1.00 32.29 ? 1027 HOH A O 1 HETATM 5039 O O . HOH H 6 . ? 28.213 12.710 25.146 1.00 20.29 ? 1028 HOH A O 1 HETATM 5040 O O . HOH H 6 . ? 21.158 11.552 21.222 1.00 26.49 ? 1029 HOH A O 1 HETATM 5041 O O . HOH H 6 . ? 37.560 -4.645 39.292 1.00 29.01 ? 1030 HOH A O 1 HETATM 5042 O O . HOH H 6 . ? 26.103 16.377 36.403 1.00 23.45 ? 1031 HOH A O 1 HETATM 5043 O O . HOH H 6 . ? 28.606 7.230 11.837 1.00 28.84 ? 1032 HOH A O 1 HETATM 5044 O O . HOH H 6 . ? 38.493 -4.248 28.557 1.00 36.00 ? 1034 HOH A O 1 HETATM 5045 O O . HOH H 6 . ? 37.573 3.167 28.108 1.00 24.29 ? 1035 HOH A O 1 HETATM 5046 O O . HOH H 6 . ? 24.448 -3.893 48.111 1.00 33.75 ? 1036 HOH A O 1 HETATM 5047 O O . HOH H 6 . ? 24.117 16.693 10.252 1.00 16.99 ? 1037 HOH A O 1 HETATM 5048 O O . HOH H 6 . ? 10.852 25.792 41.074 1.00 29.13 ? 1038 HOH A O 1 HETATM 5049 O O . HOH H 6 . ? 30.083 8.569 13.676 1.00 33.30 ? 1039 HOH A O 1 HETATM 5050 O O . HOH H 6 . ? 12.221 18.377 21.964 1.00 24.78 ? 1040 HOH A O 1 HETATM 5051 O O . HOH H 6 . ? 28.076 -6.073 39.073 1.00 25.24 ? 1041 HOH A O 1 HETATM 5052 O O . HOH H 6 . ? 27.965 20.805 42.670 1.00 40.07 ? 1042 HOH A O 1 HETATM 5053 O O . HOH H 6 . ? 19.011 2.066 29.621 1.00 36.43 ? 1043 HOH A O 1 HETATM 5054 O O . HOH H 6 . ? 24.480 1.958 29.036 1.00 31.86 ? 1044 HOH A O 1 HETATM 5055 O O . HOH H 6 . ? 12.763 10.385 20.666 1.00 39.89 ? 1045 HOH A O 1 HETATM 5056 O O . HOH H 6 . ? 12.580 24.921 33.864 1.00 33.21 ? 1046 HOH A O 1 HETATM 5057 O O . HOH H 6 . ? 14.260 0.611 49.657 1.00 40.29 ? 1047 HOH A O 1 HETATM 5058 O O . HOH H 6 . ? 9.576 19.265 20.448 1.00 33.23 ? 1050 HOH A O 1 HETATM 5059 O O . HOH I 6 . ? -8.848 58.019 42.674 1.00 32.72 ? 1019 HOH B O 1 HETATM 5060 O O . HOH I 6 . ? 5.730 46.544 62.152 1.00 40.65 ? 1026 HOH B O 1 HETATM 5061 O O . HOH I 6 . ? 13.172 47.857 41.114 1.00 36.38 ? 1033 HOH B O 1 HETATM 5062 O O . HOH I 6 . ? 4.145 52.169 34.805 1.00 31.20 ? 1048 HOH B O 1 HETATM 5063 O O . HOH I 6 . ? -10.529 49.492 55.305 1.00 43.38 ? 1049 HOH B O 1 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 LYS 1 1 1 LYS LYS A . n A 1 2 ILE 2 2 2 ILE ILE A . n A 1 3 LYS 3 3 3 LYS LYS A . n A 1 4 ASP 4 4 4 ASP ASP A . n A 1 5 PRO 5 5 5 PRO PRO A . n A 1 6 LYS 6 6 6 LYS LYS A . n A 1 7 ILE 7 7 7 ILE ILE A . n A 1 8 LEU 8 8 8 LEU LEU A . n A 1 9 GLY 9 9 9 GLY GLY A . n A 1 10 ILE 10 10 10 ILE ILE A . n A 1 11 ASP 11 11 11 ASP ASP A . n A 1 12 PRO 12 12 12 PRO PRO A . n A 1 13 ASN 13 13 13 ASN ASN A . n A 1 14 VAL 14 14 14 VAL VAL A . n A 1 15 THR 15 15 15 THR THR A . n A 1 16 GLN 16 16 16 GLN GLN A . n A 1 17 TYR 17 17 17 TYR TYR A . n A 1 18 THR 18 18 18 THR THR A . n A 1 19 GLY 19 19 19 GLY GLY A . n A 1 20 TYR 20 20 20 TYR TYR A . n A 1 21 LEU 21 21 21 LEU LEU A . n A 1 22 ASP 22 22 22 ASP ASP A . n A 1 23 VAL 23 23 23 VAL VAL A . n A 1 24 GLU 24 24 24 GLU GLU A . n A 1 25 ASP 25 25 25 ASP ASP A . n A 1 26 GLU 26 26 26 GLU GLU A . n A 1 27 ASP 27 27 27 ASP ASP A . n A 1 28 LYS 28 28 28 LYS LYS A . n A 1 29 HIS 29 29 29 HIS HIS A . n A 1 30 PHE 30 30 30 PHE PHE A . n A 1 31 PHE 31 31 31 PHE PHE A . n A 1 32 PHE 32 32 32 PHE PHE A . n A 1 33 TRP 33 33 33 TRP TRP A . n A 1 34 THR 34 34 34 THR THR A . n A 1 35 PHE 35 35 35 PHE PHE A . n A 1 36 GLU 36 36 36 GLU GLU A . n A 1 37 SER 37 37 37 SER SER A . n A 1 38 ARG 38 38 38 ARG ARG A . n A 1 39 ASN 39 39 39 ASN ASN A . n A 1 40 ASP 40 40 40 ASP ASP A . n A 1 41 PRO 41 41 41 PRO PRO A . n A 1 42 ALA 42 42 42 ALA ALA A . n A 1 43 LYS 43 43 43 LYS LYS A . n A 1 44 ASP 44 44 44 ASP ASP A . n A 1 45 PRO 45 45 45 PRO PRO A . n A 1 46 VAL 46 46 46 VAL VAL A . n A 1 47 ILE 47 47 47 ILE ILE A . n A 1 48 LEU 48 48 48 LEU LEU A . n A 1 49 TRP 49 49 49 TRP TRP A . n A 1 50 LEU 50 50 50 LEU LEU A . n A 1 51 ASN 51 51 51 ASN ASN A . n A 1 52 GLY 52 52 52 GLY GLY A . n A 1 53 GLY 53 53 53 GLY GLY A . n A 1 54 PRO 54 54 54 PRO PRO A . n A 1 55 GLY 55 55 55 GLY GLY A . n A 1 56 CYS 56 56 56 CYS CYS A . n A 1 57 SER 57 57 57 SER SER A . n A 1 58 SER 58 58 58 SER SER A . n A 1 59 LEU 59 59 59 LEU LEU A . n A 1 60 THR 60 60 60 THR THR A . n A 1 61 GLY 61 61 61 GLY GLY A . n A 1 62 LEU 62 62 62 LEU LEU A . n A 1 63 PHE 63 63 63 PHE PHE A . n A 1 64 PHE 64 64 64 PHE PHE A . n A 1 65 GLU 65 65 65 GLU GLU A . n A 1 66 LEU 66 66 66 LEU LEU A . n A 1 67 GLY 67 67 67 GLY GLY A . n A 1 68 PRO 68 68 68 PRO PRO A . n A 1 69 SER 69 69 69 SER SER A . n A 1 70 SER 70 70 70 SER SER A . n A 1 71 ILE 71 71 71 ILE ILE A . n A 1 72 GLY 72 72 72 GLY GLY A . n A 1 73 PRO 73 73 73 PRO PRO A . n A 1 74 ASP 74 74 74 ASP ASP A . n A 1 75 LEU 75 75 75 LEU LEU A . n A 1 76 LYS 76 76 76 LYS LYS A . n A 1 77 PRO 77 77 77 PRO PRO A . n A 1 78 ILE 78 78 78 ILE ILE A . n A 1 79 GLY 79 79 79 GLY GLY A . n A 1 80 ASN 80 80 80 ASN ASN A . n A 1 81 PRO 81 81 81 PRO PRO A . n A 1 82 TYR 82 82 82 TYR TYR A . n A 1 83 SER 83 83 83 SER SER A . n A 1 84 TRP 84 84 84 TRP TRP A . n A 1 85 ASN 85 85 85 ASN ASN A . n A 1 86 SER 86 86 86 SER SER A . n A 1 87 ASN 87 87 87 ASN ASN A . n A 1 88 ALA 88 88 88 ALA ALA A . n A 1 89 THR 89 89 89 THR THR A . n A 1 90 VAL 90 90 90 VAL VAL A . n A 1 91 ILE 91 91 91 ILE ILE A . n A 1 92 PHE 92 92 92 PHE PHE A . n A 1 93 LEU 93 93 93 LEU LEU A . n A 1 94 ASP 94 94 94 ASP ASP A . n A 1 95 GLN 95 95 95 GLN GLN A . n A 1 96 PRO 96 96 96 PRO PRO A . n A 1 97 VAL 97 97 97 VAL VAL A . n A 1 98 ASN 98 98 98 ASN ASN A . n A 1 99 VAL 99 99 99 VAL VAL A . n A 1 100 GLY 100 100 100 GLY GLY A . n A 1 101 PHE 101 101 101 PHE PHE A . n A 1 102 SER 102 102 102 SER SER A . n A 1 103 TYR 103 103 103 TYR TYR A . n A 1 104 SER 104 104 104 SER SER A . n A 1 105 GLY 105 105 105 GLY GLY A . n A 1 106 SER 106 106 106 SER SER A . n A 1 107 SER 107 107 107 SER SER A . n A 1 108 GLY 108 108 108 GLY GLY A . n A 1 109 VAL 109 109 109 VAL VAL A . n A 1 110 SER 110 110 110 SER SER A . n A 1 111 ASN 111 111 111 ASN ASN A . n A 1 112 THR 112 112 112 THR THR A . n A 1 113 VAL 113 113 113 VAL VAL A . n A 1 114 ALA 114 114 114 ALA ALA A . n A 1 115 ALA 115 115 115 ALA ALA A . n A 1 116 GLY 116 116 116 GLY GLY A . n A 1 117 LYS 117 117 117 LYS LYS A . n A 1 118 ASP 118 118 118 ASP ASP A . n A 1 119 VAL 119 119 119 VAL VAL A . n A 1 120 TYR 120 120 120 TYR TYR A . n A 1 121 ASN 121 121 121 ASN ASN A . n A 1 122 PHE 122 122 122 PHE PHE A . n A 1 123 LEU 123 123 123 LEU LEU A . n A 1 124 GLU 124 124 124 GLU GLU A . n A 1 125 LEU 125 125 125 LEU LEU A . n A 1 126 PHE 126 126 126 PHE PHE A . n A 1 127 PHE 127 127 127 PHE PHE A . n A 1 128 ASP 128 128 128 ASP ASP A . n A 1 129 GLN 129 129 129 GLN GLN A . n A 1 130 PHE 130 130 130 PHE PHE A . n A 1 131 PRO 131 131 131 PRO PRO A . n A 1 132 GLU 132 132 132 GLU GLU A . n A 1 133 TYR 133 133 133 TYR TYR A . n A 1 134 VAL 134 134 134 VAL VAL A . n A 1 135 ASN 135 135 135 ASN ASN A . n A 1 136 LYS 136 136 136 LYS LYS A . n A 1 137 GLY 137 137 137 GLY GLY A . n A 1 138 GLN 138 138 138 GLN GLN A . n A 1 139 ASP 139 139 139 ASP ASP A . n A 1 140 PHE 140 140 140 PHE PHE A . n A 1 141 HIS 141 141 141 HIS HIS A . n A 1 142 ILE 142 142 142 ILE ILE A . n A 1 143 ALA 143 143 143 ALA ALA A . n A 1 144 GLY 144 144 144 GLY GLY A . n A 1 145 GLU 145 145 145 GLU GLU A . n A 1 146 SER 146 146 146 SER SER A . n A 1 147 TYR 147 147 147 TYR TYR A . n A 1 148 ALA 148 148 148 ALA ALA A . n A 1 149 GLY 149 149 149 GLY GLY A . n A 1 150 HIS 150 150 150 HIS HIS A . n A 1 151 TYR 151 151 151 TYR TYR A . n A 1 152 ILE 152 152 152 ILE ILE A . n A 1 153 PRO 153 153 153 PRO PRO A . n A 1 154 VAL 154 154 154 VAL VAL A . n A 1 155 PHE 155 155 155 PHE PHE A . n A 1 156 ALA 156 156 156 ALA ALA A . n A 1 157 SER 157 157 157 SER SER A . n A 1 158 GLU 158 158 158 GLU GLU A . n A 1 159 ILE 159 159 159 ILE ILE A . n A 1 160 LEU 160 160 160 LEU LEU A . n A 1 161 SER 161 161 161 SER SER A . n A 1 162 HIS 162 162 162 HIS HIS A . n A 1 163 LYS 163 163 163 LYS LYS A . n A 1 164 ASP 164 164 164 ASP ASP A . n A 1 165 ARG 165 165 165 ARG ARG A . n A 1 166 ASN 166 166 166 ASN ASN A . n A 1 167 PHE 167 167 167 PHE PHE A . n A 1 168 ASN 168 168 168 ASN ASN A . n A 1 169 LEU 169 169 169 LEU LEU A . n A 1 170 THR 170 170 170 THR THR A . n A 1 171 SER 171 171 171 SER SER A . n A 1 172 VAL 172 172 172 VAL VAL A . n A 1 173 LEU 173 173 173 LEU LEU A . n A 1 174 ILE 174 174 174 ILE ILE A . n A 1 175 GLY 175 175 175 GLY GLY A . n A 1 176 ASN 176 176 176 ASN ASN A . n A 1 177 GLY 177 177 177 GLY GLY A . n A 1 178 LEU 178 178 178 LEU LEU A . n A 1 179 THR 179 179 179 THR THR A . n A 1 180 ASP 180 180 180 ASP ASP A . n A 1 181 PRO 181 181 181 PRO PRO A . n A 1 182 LEU 182 182 182 LEU LEU A . n A 1 183 THR 183 183 183 THR THR A . n A 1 184 GLN 184 184 184 GLN GLN A . n A 1 185 TYR 185 185 185 TYR TYR A . n A 1 186 ASN 186 186 186 ASN ASN A . n A 1 187 TYR 187 187 187 TYR TYR A . n A 1 188 TYR 188 188 188 TYR TYR A . n A 1 189 GLU 189 189 189 GLU GLU A . n A 1 190 PRO 190 190 190 PRO PRO A . n A 1 191 MET 191 191 191 MET MET A . n A 1 192 ALA 192 192 192 ALA ALA A . n A 1 193 CYS 193 193 193 CYS CYS A . n A 1 194 GLY 194 194 194 GLY GLY A . n A 1 195 GLU 195 195 195 GLU GLU A . n A 1 196 GLY 196 196 196 GLY GLY A . n A 1 197 GLY 197 197 197 GLY GLY A . n A 1 198 GLU 198 198 198 GLU GLU A . n A 1 199 PRO 199 199 199 PRO PRO A . n A 1 200 SER 200 200 200 SER SER A . n A 1 201 VAL 201 201 201 VAL VAL A . n A 1 202 LEU 202 202 202 LEU LEU A . n A 1 203 PRO 203 203 203 PRO PRO A . n A 1 204 SER 204 204 204 SER SER A . n A 1 205 GLU 205 205 205 GLU GLU A . n A 1 206 GLU 206 206 206 GLU GLU A . n A 1 207 CYS 207 207 207 CYS CYS A . n A 1 208 SER 208 208 208 SER SER A . n A 1 209 ALA 209 209 209 ALA ALA A . n A 1 210 MET 210 210 210 MET MET A . n A 1 211 GLU 211 211 211 GLU GLU A . n A 1 212 ASP 212 212 212 ASP ASP A . n A 1 213 SER 213 213 213 SER SER A . n A 1 214 LEU 214 214 214 LEU LEU A . n A 1 215 GLU 215 215 215 GLU GLU A . n A 1 216 ARG 216 216 216 ARG ARG A . n A 1 217 CYS 217 217 217 CYS CYS A . n A 1 218 LEU 218 218 218 LEU LEU A . n A 1 219 GLY 219 219 219 GLY GLY A . n A 1 220 LEU 220 220 220 LEU LEU A . n A 1 221 ILE 221 221 221 ILE ILE A . n A 1 222 GLU 222 222 222 GLU GLU A . n A 1 223 SER 223 223 223 SER SER A . n A 1 224 CYS 224 224 224 CYS CYS A . n A 1 225 TYR 225 225 225 TYR TYR A . n A 1 226 ASP 226 226 226 ASP ASP A . n A 1 227 SER 227 227 227 SER SER A . n A 1 228 GLN 228 228 228 GLN GLN A . n A 1 229 SER 229 229 229 SER SER A . n A 1 230 VAL 230 230 230 VAL VAL A . n A 1 231 TRP 231 231 231 TRP TRP A . n A 1 232 SER 232 232 232 SER SER A . n A 1 233 CYS 233 233 233 CYS CYS A . n A 1 234 VAL 234 234 234 VAL VAL A . n A 1 235 PRO 235 235 235 PRO PRO A . n A 1 236 ALA 236 236 236 ALA ALA A . n A 1 237 THR 237 237 237 THR THR A . n A 1 238 ILE 238 238 238 ILE ILE A . n A 1 239 TYR 239 239 239 TYR TYR A . n A 1 240 CYS 240 240 240 CYS CYS A . n A 1 241 ASN 241 241 241 ASN ASN A . n A 1 242 ASN 242 242 242 ASN ASN A . n A 1 243 ALA 243 243 243 ALA ALA A . n A 1 244 GLN 244 244 244 GLN GLN A . n A 1 245 LEU 245 245 245 LEU LEU A . n A 1 246 ALA 246 246 246 ALA ALA A . n A 1 247 PRO 247 247 247 PRO PRO A . n A 1 248 TYR 248 248 248 TYR TYR A . n A 1 249 GLN 249 249 249 GLN GLN A . n A 1 250 ARG 250 250 250 ARG ARG A . n A 1 251 THR 251 251 251 THR THR A . n A 1 252 GLY 252 252 252 GLY GLY A . n A 1 253 ARG 253 253 253 ARG ARG A . n A 1 254 ASN 254 254 254 ASN ASN A . n A 1 255 VAL 255 255 255 VAL VAL A . n A 1 256 TYR 256 256 256 TYR TYR A . n A 1 257 ASP 257 257 257 ASP ASP A . n A 1 258 ILE 258 258 258 ILE ILE A . n A 1 259 ARG 259 259 259 ARG ARG A . n A 1 260 LYS 260 260 260 LYS LYS A . n A 1 261 ASP 261 261 261 ASP ASP A . n A 1 262 CYS 262 262 262 CYS CYS A . n A 1 263 GLU 263 263 263 GLU GLU A . n A 1 264 GLY 264 264 264 GLY GLY A . n A 1 265 GLY 265 265 265 GLY GLY A . n A 1 266 ASN 266 266 266 ASN ASN A . n A 1 267 LEU 267 267 267 LEU LEU A . n A 1 268 CYS 268 268 268 CYS CYS A . n A 1 269 TYR 269 269 269 TYR TYR A . n A 1 270 PRO 270 270 270 PRO PRO A . n A 1 271 THR 271 271 271 THR THR A . n A 1 272 LEU 272 272 272 LEU LEU A . n A 1 273 GLN 273 273 273 GLN GLN A . n A 1 274 ASP 274 274 274 ASP ASP A . n A 1 275 ILE 275 275 275 ILE ILE A . n A 1 276 ASP 276 276 276 ASP ASP A . n A 1 277 ASP 277 277 277 ASP ASP A . n A 1 278 TYR 278 278 278 TYR TYR A . n A 1 279 LEU 279 279 279 LEU LEU A . n A 1 280 ASN 280 280 280 ASN ASN A . n A 1 281 GLN 281 281 281 GLN GLN A . n A 1 282 ASP 282 282 282 ASP ASP A . n A 1 283 TYR 283 283 283 TYR TYR A . n A 1 284 VAL 284 284 284 VAL VAL A . n A 1 285 LYS 285 285 285 LYS LYS A . n A 1 286 GLU 286 286 286 GLU GLU A . n A 1 287 ALA 287 287 287 ALA ALA A . n A 1 288 VAL 288 288 288 VAL VAL A . n A 1 289 GLY 289 289 289 GLY GLY A . n A 1 290 ALA 290 290 290 ALA ALA A . n A 1 291 GLU 291 291 291 GLU GLU A . n A 1 292 VAL 292 292 292 VAL VAL A . n A 1 293 ASP 293 293 293 ASP ASP A . n A 1 294 HIS 294 294 294 HIS HIS A . n A 1 295 TYR 295 295 295 TYR TYR A . n A 1 296 GLU 296 296 296 GLU GLU A . n A 1 297 SER 297 297 297 SER SER A . n A 1 298 CYS 298 298 298 CYS CYS A . n A 1 299 ASN 299 299 299 ASN ASN A . n A 1 300 PHE 300 300 300 PHE PHE A . n A 1 301 ASP 301 301 301 ASP ASP A . n A 1 302 ILE 302 302 302 ILE ILE A . n A 1 303 ASN 303 303 303 ASN ASN A . n A 1 304 ARG 304 304 304 ARG ARG A . n A 1 305 ASN 305 305 305 ASN ASN A . n A 1 306 PHE 306 306 306 PHE PHE A . n A 1 307 LEU 307 307 307 LEU LEU A . n A 1 308 PHE 308 308 308 PHE PHE A . n A 1 309 ALA 309 309 309 ALA ALA A . n A 1 310 GLY 310 310 310 GLY GLY A . n A 1 311 ASP 311 311 311 ASP ASP A . n A 1 312 TRP 312 312 312 TRP TRP A . n A 1 313 MET 313 313 313 MET MET A . n A 1 314 LYS 314 314 314 LYS LYS A . n A 1 315 PRO 315 315 315 PRO PRO A . n A 1 316 TYR 316 316 316 TYR TYR A . n A 1 317 HIS 317 317 317 HIS HIS A . n A 1 318 THR 318 318 318 THR THR A . n A 1 319 ALA 319 319 319 ALA ALA A . n A 1 320 VAL 320 320 320 VAL VAL A . n A 1 321 THR 321 321 321 THR THR A . n A 1 322 ASP 322 322 322 ASP ASP A . n A 1 323 LEU 323 323 323 LEU LEU A . n A 1 324 LEU 324 324 324 LEU LEU A . n A 1 325 ASN 325 325 325 ASN ASN A . n A 1 326 GLN 326 326 326 GLN GLN A . n A 1 327 ASP 327 327 327 ASP ASP A . n A 1 328 LEU 328 328 328 LEU LEU A . n A 1 329 PRO 329 329 329 PRO PRO A . n A 1 330 ILE 330 330 330 ILE ILE A . n A 1 331 LEU 331 331 331 LEU LEU A . n A 1 332 VAL 332 332 332 VAL VAL A . n A 1 333 TYR 333 333 333 TYR TYR A . n A 1 334 ALA 334 334 334 ALA ALA A . n A 1 335 GLY 335 335 335 GLY GLY A . n A 1 336 ASP 336 336 336 ASP ASP A . n A 1 337 LYS 337 337 337 LYS LYS A . n A 1 338 ASP 338 338 338 ASP ASP A . n A 1 339 PHE 339 339 339 PHE PHE A . n A 1 340 ILE 340 340 340 ILE ILE A . n A 1 341 CYS 341 341 341 CYS CYS A . n A 1 342 ASN 342 342 342 ASN ASN A . n A 1 343 TRP 343 343 343 TRP TRP A . n A 1 344 LEU 344 344 344 LEU LEU A . n A 1 345 GLY 345 345 345 GLY GLY A . n A 1 346 ASN 346 346 346 ASN ASN A . n A 1 347 LYS 347 347 347 LYS LYS A . n A 1 348 ALA 348 348 348 ALA ALA A . n A 1 349 TRP 349 349 349 TRP TRP A . n A 1 350 THR 350 350 350 THR THR A . n A 1 351 ASP 351 351 351 ASP ASP A . n A 1 352 VAL 352 352 352 VAL VAL A . n A 1 353 LEU 353 353 353 LEU LEU A . n A 1 354 PRO 354 354 354 PRO PRO A . n A 1 355 TRP 355 355 355 TRP TRP A . n A 1 356 LYS 356 356 356 LYS LYS A . n A 1 357 TYR 357 357 357 TYR TYR A . n A 1 358 ASP 358 358 358 ASP ASP A . n A 1 359 GLU 359 359 359 GLU GLU A . n A 1 360 GLU 360 360 360 GLU GLU A . n A 1 361 PHE 361 361 361 PHE PHE A . n A 1 362 ALA 362 362 362 ALA ALA A . n A 1 363 SER 363 363 363 SER SER A . n A 1 364 GLN 364 364 364 GLN GLN A . n A 1 365 LYS 365 365 365 LYS LYS A . n A 1 366 VAL 366 366 366 VAL VAL A . n A 1 367 ARG 367 367 367 ARG ARG A . n A 1 368 ASN 368 368 368 ASN ASN A . n A 1 369 TRP 369 369 369 TRP TRP A . n A 1 370 THR 370 370 370 THR THR A . n A 1 371 ALA 371 371 371 ALA ALA A . n A 1 372 SER 372 372 372 SER SER A . n A 1 373 ILE 373 373 373 ILE ILE A . n A 1 374 THR 374 374 374 THR THR A . n A 1 375 ASP 375 375 375 ASP ASP A . n A 1 376 GLU 376 376 376 GLU GLU A . n A 1 377 VAL 377 377 377 VAL VAL A . n A 1 378 ALA 378 378 378 ALA ALA A . n A 1 379 GLY 379 379 379 GLY GLY A . n A 1 380 GLU 380 380 380 GLU GLU A . n A 1 381 VAL 381 381 381 VAL VAL A . n A 1 382 LYS 382 382 382 LYS LYS A . n A 1 383 SER 383 383 383 SER SER A . n A 1 384 TYR 384 384 384 TYR TYR A . n A 1 385 LYS 385 385 385 LYS LYS A . n A 1 386 HIS 386 386 386 HIS HIS A . n A 1 387 PHE 387 387 387 PHE PHE A . n A 1 388 THR 388 388 388 THR THR A . n A 1 389 TYR 389 389 389 TYR TYR A . n A 1 390 LEU 390 390 390 LEU LEU A . n A 1 391 ARG 391 391 391 ARG ARG A . n A 1 392 VAL 392 392 392 VAL VAL A . n A 1 393 PHE 393 393 393 PHE PHE A . n A 1 394 ASN 394 394 394 ASN ASN A . n A 1 395 GLY 395 395 395 GLY GLY A . n A 1 396 GLY 396 396 396 GLY GLY A . n A 1 397 HIS 397 397 397 HIS HIS A . n A 1 398 MET 398 398 398 MET MET A . n A 1 399 VAL 399 399 399 VAL VAL A . n A 1 400 PRO 400 400 400 PRO PRO A . n A 1 401 PHE 401 401 401 PHE PHE A . n A 1 402 ASP 402 402 402 ASP ASP A . n A 1 403 VAL 403 403 403 VAL VAL A . n A 1 404 PRO 404 404 404 PRO PRO A . n A 1 405 GLU 405 405 405 GLU GLU A . n A 1 406 ASN 406 406 406 ASN ASN A . n A 1 407 ALA 407 407 407 ALA ALA A . n A 1 408 LEU 408 408 408 LEU LEU A . n A 1 409 SER 409 409 409 SER SER A . n A 1 410 MET 410 410 410 MET MET A . n A 1 411 VAL 411 411 411 VAL VAL A . n A 1 412 ASN 412 412 412 ASN ASN A . n A 1 413 GLU 413 413 413 GLU GLU A . n A 1 414 TRP 414 414 414 TRP TRP A . n A 1 415 ILE 415 415 415 ILE ILE A . n A 1 416 HIS 416 416 416 HIS HIS A . n A 1 417 GLY 417 417 417 GLY GLY A . n A 1 418 GLY 418 418 418 GLY GLY A . n A 1 419 PHE 419 419 419 PHE PHE A . n A 1 420 SER 420 420 420 SER SER A . n A 1 421 LEU 421 421 421 LEU LEU A . n B 2 1 ACE 1 500 500 ACE ACE B . n B 2 2 MET 2 501 501 MET MET B . n B 2 3 ASN 3 502 502 ASN ASN B . n B 2 4 GLN 4 503 503 GLN GLN B . n B 2 5 ALA 5 504 504 ALA ALA B . n B 2 6 ILE 6 505 505 ILE ILE B . n B 2 7 ASP 7 506 506 ASP ASP B . n B 2 8 PHE 8 507 507 PHE PHE B . n B 2 9 ALA 9 508 508 ALA ALA B . n B 2 10 GLN 10 509 509 GLN GLN B . n B 2 11 ALA 11 510 510 ALA ALA B . n B 2 12 SER 12 511 511 SER SER B . n B 2 13 ILE 13 512 512 ILE ILE B . n B 2 14 ASP 14 513 513 ASP ASP B . n B 2 15 SER 15 514 514 SER SER B . n B 2 16 TYR 16 515 515 TYR TYR B . n B 2 17 LYS 17 516 516 LYS LYS B . n B 2 18 LYS 18 517 517 LYS LYS B . n B 2 19 HIS 19 518 518 HIS HIS B . n B 2 20 GLY 20 519 519 GLY GLY B . n B 2 21 ILE 21 520 520 ILE ILE B . n B 2 22 LEU 22 521 521 LEU LEU B . n B 2 23 GLU 23 522 522 GLU GLU B . n B 2 24 ASP 24 523 523 ASP ASP B . n B 2 25 VAL 25 524 524 VAL VAL B . n B 2 26 ILE 26 525 525 ILE ILE B . n B 2 27 HIS 27 526 526 HIS HIS B . n B 2 28 ASP 28 527 527 ASP ASP B . n B 2 29 THR 29 528 528 THR THR B . n B 2 30 SER 30 529 529 SER SER B . n B 2 31 PHE 31 530 530 PHE PHE B . n B 2 32 GLN 32 531 531 GLN GLN B . n B 2 33 PRO 33 532 532 PRO PRO B . n B 2 34 SER 34 533 533 SER SER B . n B 2 35 GLY 35 534 534 GLY GLY B . n B 2 36 ILE 36 535 535 ILE ILE B . n B 2 37 LEU 37 536 536 LEU LEU B . n B 2 38 ALA 38 537 537 ALA ALA B . n B 2 39 VAL 39 538 538 VAL VAL B . n B 2 40 GLU 40 539 539 GLU GLU B . n B 2 41 TYR 41 540 540 TYR TYR B . n B 2 42 SER 42 541 541 SER SER B . n B 2 43 SER 43 542 542 SER SER B . n B 2 44 SER 44 543 543 SER SER B . n B 2 45 ALA 45 544 544 ALA ALA B . n B 2 46 PRO 46 545 545 PRO PRO B . n B 2 47 VAL 47 546 546 VAL VAL B . n B 2 48 ALA 48 547 547 ALA ALA B . n B 2 49 MET 49 548 548 MET MET B . n B 2 50 GLY 50 549 549 GLY GLY B . n B 2 51 ASN 51 550 550 ASN ASN B . n B 2 52 THR 52 551 551 THR THR B . n B 2 53 LEU 53 552 552 LEU LEU B . n B 2 54 PRO 54 553 553 PRO PRO B . n B 2 55 THR 55 554 554 THR THR B . n B 2 56 GLU 56 555 555 GLU GLU B . n B 2 57 LYS 57 556 556 LYS LYS B . n B 2 58 ALA 58 557 557 ALA ALA B . n B 2 59 ARG 59 558 558 ARG ARG B . n B 2 60 SER 60 559 559 SER SER B . n B 2 61 LYS 61 560 560 LYS LYS B . n B 2 62 PRO 62 561 561 PRO PRO B . n B 2 63 GLN 63 562 562 GLN GLN B . n B 2 64 PHE 64 563 563 PHE PHE B . n B 2 65 GLN 65 564 564 GLN GLN B . n B 2 66 PHE 66 565 565 PHE PHE B . n B 2 67 THR 67 566 566 THR THR B . n B 2 68 PHE 68 567 567 PHE PHE B . n B 2 69 ASN 69 568 568 ASN ASN B . n B 2 70 LYS 70 569 569 LYS LYS B . n B 2 71 GLN 71 570 570 GLN GLN B . n B 2 72 MET 72 571 571 MET MET B . n B 2 73 GLN 73 572 572 GLN GLN B . n B 2 74 LYS 74 573 ? ? ? B . n B 2 75 SER 75 574 ? ? ? B . n B 2 76 VAL 76 575 ? ? ? B . n B 2 77 PRO 77 576 ? ? ? B . n B 2 78 GLN 78 577 ? ? ? B . n B 2 79 ALA 79 578 ? ? ? B . n B 2 80 ASN 80 579 579 ASN ASN B . n B 2 81 ALA 81 580 580 ALA ALA B . n B 2 82 TYR 82 581 581 TYR TYR B . n B 2 83 VAL 83 582 582 VAL VAL B . n B 2 84 PRO 84 583 583 PRO PRO B . n B 2 85 GLN 85 584 584 GLN GLN B . n B 2 86 ASP 86 585 585 ASP ASP B . n B 2 87 ASP 87 586 586 ASP ASP B . n B 2 88 ASP 88 587 587 ASP ASP B . n B 2 89 LEU 89 588 588 LEU LEU B . n B 2 90 PHE 90 589 589 PHE PHE B . n B 2 91 THR 91 590 590 THR THR B . n B 2 92 LEU 92 591 591 LEU LEU B . n B 2 93 VAL 93 592 592 VAL VAL B . n B 2 94 MET 94 593 593 MET MET B . n B 2 95 THR 95 594 594 THR THR B . n B 2 96 ASP 96 595 595 ASP ASP B . n B 2 97 PRO 97 596 596 PRO PRO B . n B 2 98 ASP 98 597 597 ASP ASP B . n B 2 99 ALA 99 598 598 ALA ALA B . n B 2 100 PRO 100 599 599 PRO PRO B . n B 2 101 SER 101 600 600 SER SER B . n B 2 102 LYS 102 601 601 LYS LYS B . n B 2 103 THR 103 602 602 THR THR B . n B 2 104 ASP 104 603 603 ASP ASP B . n B 2 105 HIS 105 604 604 HIS HIS B . n B 2 106 LYS 106 605 605 LYS LYS B . n B 2 107 TRP 107 606 606 TRP TRP B . n B 2 108 SER 108 607 607 SER SER B . n B 2 109 GLU 109 608 608 GLU GLU B . n B 2 110 PHE 110 609 609 PHE PHE B . n B 2 111 CYS 111 610 610 CYS CYS B . n B 2 112 HIS 112 611 611 HIS HIS B . n B 2 113 LEU 113 612 612 LEU LEU B . n B 2 114 VAL 114 613 613 VAL VAL B . n B 2 115 GLU 115 614 614 GLU GLU B . n B 2 116 CYS 116 615 615 CYS CYS B . n B 2 117 ASP 117 616 616 ASP ASP B . n B 2 118 LEU 118 617 617 LEU LEU B . n B 2 119 LYS 119 618 618 LYS LYS B . n B 2 120 LEU 120 619 619 LEU LEU B . n B 2 121 LEU 121 620 620 LEU LEU B . n B 2 122 ASN 122 621 621 ASN ASN B . n B 2 123 GLU 123 622 ? ? ? B . n B 2 124 ALA 124 623 ? ? ? B . n B 2 125 THR 125 624 ? ? ? B . n B 2 126 HIS 126 625 ? ? ? B . n B 2 127 GLU 127 626 ? ? ? B . n B 2 128 THR 128 627 ? ? ? B . n B 2 129 SER 129 628 ? ? ? B . n B 2 130 GLY 130 629 ? ? ? B . n B 2 131 ALA 131 630 ? ? ? B . n B 2 132 THR 132 631 631 THR THR B . n B 2 133 GLU 133 632 632 GLU GLU B . n B 2 134 PHE 134 633 633 PHE PHE B . n B 2 135 PHE 135 634 634 PHE PHE B . n B 2 136 ALA 136 635 635 ALA ALA B . n B 2 137 SER 137 636 636 SER SER B . n B 2 138 GLU 138 637 637 GLU GLU B . n B 2 139 PHE 139 638 638 PHE PHE B . n B 2 140 ASN 140 639 639 ASN ASN B . n B 2 141 THR 141 640 640 THR THR B . n B 2 142 LYS 142 641 641 LYS LYS B . n B 2 143 GLY 143 642 642 GLY GLY B . n B 2 144 SER 144 643 643 SER SER B . n B 2 145 ASN 145 644 644 ASN ASN B . n B 2 146 THR 146 645 645 THR THR B . n B 2 147 LEU 147 646 646 LEU LEU B . n B 2 148 ILE 148 647 647 ILE ILE B . n B 2 149 GLU 149 648 648 GLU GLU B . n B 2 150 TYR 150 649 649 TYR TYR B . n B 2 151 MET 151 650 650 MET MET B . n B 2 152 GLY 152 651 651 GLY GLY B . n B 2 153 PRO 153 652 652 PRO PRO B . n B 2 154 ALA 154 653 653 ALA ALA B . n B 2 155 PRO 155 654 654 PRO PRO B . n B 2 156 PRO 156 655 655 PRO PRO B . n B 2 157 LYS 157 656 656 LYS LYS B . n B 2 158 GLY 158 657 657 GLY GLY B . n B 2 159 SER 159 658 658 SER SER B . n B 2 160 GLY 160 659 659 GLY GLY B . n B 2 161 PRO 161 660 660 PRO PRO B . n B 2 162 HIS 162 661 661 HIS HIS B . n B 2 163 ARG 163 662 662 ARG ARG B . n B 2 164 TYR 164 663 663 TYR TYR B . n B 2 165 VAL 165 664 664 VAL VAL B . n B 2 166 PHE 166 665 665 PHE PHE B . n B 2 167 LEU 167 666 666 LEU LEU B . n B 2 168 LEU 168 667 667 LEU LEU B . n B 2 169 TYR 169 668 668 TYR TYR B . n B 2 170 LYS 170 669 669 LYS LYS B . n B 2 171 GLN 171 670 670 GLN GLN B . n B 2 172 PRO 172 671 671 PRO PRO B . n B 2 173 LYS 173 672 672 LYS LYS B . n B 2 174 GLY 174 673 673 GLY GLY B . n B 2 175 VAL 175 674 674 VAL VAL B . n B 2 176 ASP 176 675 675 ASP ASP B . n B 2 177 SER 177 676 676 SER SER B . n B 2 178 SER 178 677 677 SER SER B . n B 2 179 LYS 179 678 678 LYS LYS B . n B 2 180 PHE 180 679 679 PHE PHE B . n B 2 181 SER 181 680 680 SER SER B . n B 2 182 LYS 182 681 681 LYS LYS B . n B 2 183 ILE 183 682 682 ILE ILE B . n B 2 184 LYS 184 683 683 LYS LYS B . n B 2 185 ASP 185 684 684 ASP ASP B . n B 2 186 ARG 186 685 685 ARG ARG B . n B 2 187 PRO 187 686 686 PRO PRO B . n B 2 188 ASN 188 687 687 ASN ASN B . n B 2 189 TRP 189 688 688 TRP TRP B . n B 2 190 GLY 190 689 689 GLY GLY B . n B 2 191 TYR 191 690 690 TYR TYR B . n B 2 192 GLY 192 691 691 GLY GLY B . n B 2 193 THR 193 692 692 THR THR B . n B 2 194 PRO 194 693 693 PRO PRO B . n B 2 195 ALA 195 694 694 ALA ALA B . n B 2 196 THR 196 695 695 THR THR B . n B 2 197 GLY 197 696 696 GLY GLY B . n B 2 198 VAL 198 697 697 VAL VAL B . n B 2 199 GLY 199 698 698 GLY GLY B . n B 2 200 LYS 200 699 699 LYS LYS B . n B 2 201 TRP 201 700 700 TRP TRP B . n B 2 202 ALA 202 701 701 ALA ALA B . n B 2 203 LYS 203 702 702 LYS LYS B . n B 2 204 GLU 204 703 703 GLU GLU B . n B 2 205 ASN 205 704 704 ASN ASN B . n B 2 206 ASN 206 705 705 ASN ASN B . n B 2 207 LEU 207 706 706 LEU LEU B . n B 2 208 GLN 208 707 707 GLN GLN B . n B 2 209 LEU 209 708 708 LEU LEU B . n B 2 210 VAL 210 709 709 VAL VAL B . n B 2 211 ALA 211 710 710 ALA ALA B . n B 2 212 SER 212 711 711 SER SER B . n B 2 213 ASN 213 712 712 ASN ASN B . n B 2 214 PHE 214 713 713 PHE PHE B . n B 2 215 PHE 215 714 714 PHE PHE B . n B 2 216 TYR 216 715 715 TYR TYR B . n B 2 217 ALA 217 716 716 ALA ALA B . n B 2 218 GLU 218 717 717 GLU GLU B . n B 2 219 THR 219 718 718 THR THR B . n B 2 220 LYS 220 719 719 LYS LYS B . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code C 3 NAG 1 810 810 NAG NAG A . D 4 NDG 1 820 820 NDG NAG A . E 4 NDG 1 830 830 NDG NAG A . F 5 SO4 1 901 901 SO4 SO4 A . G 5 SO4 1 902 902 SO4 SO4 B . H 6 HOH 1 1000 1000 HOH HOH A . H 6 HOH 2 1001 1001 HOH HOH A . H 6 HOH 3 1002 1002 HOH HOH A . H 6 HOH 4 1003 1003 HOH HOH A . H 6 HOH 5 1004 1004 HOH HOH A . H 6 HOH 6 1005 1005 HOH HOH A . H 6 HOH 7 1006 1006 HOH HOH A . H 6 HOH 8 1007 1007 HOH HOH A . H 6 HOH 9 1008 1008 HOH HOH A . H 6 HOH 10 1009 1009 HOH HOH A . H 6 HOH 11 1010 1010 HOH HOH A . H 6 HOH 12 1011 1011 HOH HOH A . H 6 HOH 13 1012 1012 HOH HOH A . H 6 HOH 14 1013 1013 HOH HOH A . H 6 HOH 15 1014 1014 HOH HOH A . H 6 HOH 16 1015 1015 HOH HOH A . H 6 HOH 17 1016 1016 HOH HOH A . H 6 HOH 18 1017 1017 HOH HOH A . H 6 HOH 19 1018 1018 HOH HOH A . H 6 HOH 20 1020 1020 HOH HOH A . H 6 HOH 21 1021 1021 HOH HOH A . H 6 HOH 22 1022 1022 HOH HOH A . H 6 HOH 23 1023 1023 HOH HOH A . H 6 HOH 24 1024 1024 HOH HOH A . H 6 HOH 25 1025 1025 HOH HOH A . H 6 HOH 26 1027 1027 HOH HOH A . H 6 HOH 27 1028 1028 HOH HOH A . H 6 HOH 28 1029 1029 HOH HOH A . H 6 HOH 29 1030 1030 HOH HOH A . H 6 HOH 30 1031 1031 HOH HOH A . H 6 HOH 31 1032 1032 HOH HOH A . H 6 HOH 32 1034 1034 HOH HOH A . H 6 HOH 33 1035 1035 HOH HOH A . H 6 HOH 34 1036 1036 HOH HOH A . H 6 HOH 35 1037 1037 HOH HOH A . H 6 HOH 36 1038 1038 HOH HOH A . H 6 HOH 37 1039 1039 HOH HOH A . H 6 HOH 38 1040 1040 HOH HOH A . H 6 HOH 39 1041 1041 HOH HOH A . H 6 HOH 40 1042 1042 HOH HOH A . H 6 HOH 41 1043 1043 HOH HOH A . H 6 HOH 42 1044 1044 HOH HOH A . H 6 HOH 43 1045 1045 HOH HOH A . H 6 HOH 44 1046 1046 HOH HOH A . H 6 HOH 45 1047 1047 HOH HOH A . H 6 HOH 46 1050 1050 HOH HOH A . I 6 HOH 1 1019 1019 HOH HOH B . I 6 HOH 2 1026 1026 HOH HOH B . I 6 HOH 3 1033 1033 HOH HOH B . I 6 HOH 4 1048 1048 HOH HOH B . I 6 HOH 5 1049 1049 HOH HOH B . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 87 A ASN 87 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 168 A ASN 168 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 368 A ASN 368 ? 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 dimeric _pdbx_struct_assembly.oligomeric_count 2 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I # 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)' 4460 ? 1 MORE -58 ? 1 'SSA (A^2)' 23270 ? # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2005-03-01 2 'Structure model' 1 1 2008-04-30 3 'Structure model' 1 2 2011-07-13 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Version format compliance' 2 3 'Structure model' 'Non-polymer description' 3 3 'Structure model' 'Version format compliance' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal CNS refinement 1.1 ? 1 HKL-2000 'data reduction' . ? 2 SCALEPACK 'data scaling' . ? 3 MOLREP phasing . ? 4 # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 ILE A 10 ? ? 38.94 -72.57 2 1 ASP A 11 ? ? -153.26 84.73 3 1 GLU A 26 ? ? -149.53 -1.30 4 1 ASN A 39 ? ? -107.66 -100.03 5 1 ALA A 88 ? ? -174.36 148.09 6 1 ASN A 98 ? ? 84.45 7.49 7 1 SER A 106 ? ? -83.02 -77.26 8 1 SER A 107 ? ? -57.24 175.37 9 1 VAL A 134 ? ? -137.18 -45.00 10 1 LYS A 136 ? ? -65.12 13.96 11 1 SER A 146 ? ? 60.66 -119.55 12 1 ASN A 176 ? ? 34.90 56.86 13 1 CYS A 341 ? ? -144.16 45.24 14 1 LYS A 382 ? ? -163.49 113.96 15 1 LYS A 385 ? ? 57.67 -125.45 16 1 ALA B 557 ? ? -95.22 30.34 17 1 LYS B 569 ? ? -66.27 88.86 18 1 GLN B 570 ? ? 176.52 -37.66 19 1 MET B 571 ? ? -63.69 6.22 20 1 ASP B 587 ? ? -34.75 128.00 21 1 ASP B 597 ? ? -116.63 54.37 22 1 SER B 607 ? ? -38.08 130.05 23 1 GLU B 608 ? ? 74.22 81.92 24 1 PHE B 634 ? ? -174.50 146.71 25 1 LYS B 641 ? ? -36.95 -89.32 26 1 ALA B 653 ? ? -153.12 49.90 # 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 B LYS 573 ? B LYS 74 2 1 Y 1 B SER 574 ? B SER 75 3 1 Y 1 B VAL 575 ? B VAL 76 4 1 Y 1 B PRO 576 ? B PRO 77 5 1 Y 1 B GLN 577 ? B GLN 78 6 1 Y 1 B ALA 578 ? B ALA 79 7 1 Y 1 B GLU 622 ? B GLU 123 8 1 Y 1 B ALA 623 ? B ALA 124 9 1 Y 1 B THR 624 ? B THR 125 10 1 Y 1 B HIS 625 ? B HIS 126 11 1 Y 1 B GLU 626 ? B GLU 127 12 1 Y 1 B THR 627 ? B THR 128 13 1 Y 1 B SER 628 ? B SER 129 14 1 Y 1 B GLY 629 ? B GLY 130 15 1 Y 1 B ALA 630 ? B ALA 131 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 3 N-ACETYL-D-GLUCOSAMINE NAG 4 '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' NDG 5 'SULFATE ION' SO4 6 water HOH #