data_1SDD # _entry.id 1SDD # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.281 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 1SDD RCSB RCSB021614 WWPDB D_1000021614 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 1CZV . unspecified PDB 1CZT . unspecified PDB 1CZS . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 1SDD _pdbx_database_status.recvd_initial_deposition_date 2004-02-13 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_cs ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Adams, T.E.' 1 'Hockin, M.F.' 2 'Mann, K.G.' 3 'Everse, S.J.' 4 # _citation.id primary _citation.title 'The crystal structure of activated protein C-inactivated bovine factor Va: Implications for cofactor function.' _citation.journal_abbrev Proc.Natl.Acad.Sci.USA _citation.journal_volume 101 _citation.page_first 8918 _citation.page_last 8923 _citation.year 2004 _citation.journal_id_ASTM PNASA6 _citation.country US _citation.journal_id_ISSN 0027-8424 _citation.journal_id_CSD 0040 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 15184653 _citation.pdbx_database_id_DOI 10.1073/pnas.0403072101 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Adams, T.E.' 1 primary 'Hockin, M.F.' 2 primary 'Mann, K.G.' 3 primary 'Everse, S.J.' 4 # _cell.entry_id 1SDD _cell.length_a 63.370 _cell.length_b 86.560 _cell.length_c 229.200 _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 1SDD _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 'Coagulation factor V' 34730.359 1 ? ? 'A1 Domain (residues 29-305)' ? 2 polymer nat 'Coagulation factor V' 74711.453 1 ? ? 'Light Chain (A3, C1, C2 domains, residues 1565-2211)' ? 3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 3 ? ? ? ? 4 non-polymer syn 'CALCIUM ION' 40.078 1 ? ? ? ? 5 non-polymer man '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' 221.208 2 ? ? ? ? 6 non-polymer syn 'COPPER (II) ION' 63.546 1 ? ? ? ? 7 water nat water 18.015 189 ? ? ? ? # loop_ _entity_name_com.entity_id _entity_name_com.name 1 'Activated protein C cofactor' 2 'Activated protein C cofactor' # 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 ;AKLRQFYVAAQSIRWNYRPESTHLSSKPFETSFKKIVYREYEAYFQKEKPQSRTSGLLGPTLYAEVGDIMKVHFKNKAHK PLSIHAQGIKYSKFSEGASYSDHTLPMEKMDDAVAPGQEYTYEWIISEHSGPTHDDPPCLTHIYYSYVNLVEDFNSGLIG PLLICKKGTLTEDGTQKMFEKQHVLMFAVFDESKSWNQTSSLMYTVNGYVNGTMPDITVCAHDHISWHLIGMSSGPELFS IHFNGQVLEQNHHKISAITLVSATSTTANMTVSPEGRWTIASLIPRHFQAGMQAYIDIKNCAKKTR ; ;AKLRQFYVAAQSIRWNYRPESTHLSSKPFETSFKKIVYREYEAYFQKEKPQSRTSGLLGPTLYAEVGDIMKVHFKNKAHK PLSIHAQGIKYSKFSEGASYSDHTLPMEKMDDAVAPGQEYTYEWIISEHSGPTHDDPPCLTHIYYSYVNLVEDFNSGLIG PLLICKKGTLTEDGTQKMFEKQHVLMFAVFDESKSWNQTSSLMYTVNGYVNGTMPDITVCAHDHISWHLIGMSSGPELFS IHFNGQVLEQNHHKISAITLVSATSTTANMTVSPEGRWTIASLIPRHFQAGMQAYIDIKNCAKKTR ; A ? 2 'polypeptide(L)' no no ;SNTGNRKYYYIAAEEISWDYSKFVQSDDVDYVPEDTVYKKVVFRKYLDSTFTKLDPQGEYEEHLGILGPVIRAEVDDVIQ VRFKNLASRPYSLHAHGLSYEKSSEGKTYEDDSPEWFKEDNAIQPNKTYTYVWHATTRSGPENPGSACRAWAYYSAVNPE KDIHSGLIGPLLICRKGTLDKETNMPVDMREFVLLFMVFDEKKSWYYDKKPTRSWRRASSEVKNSHEFHAINGMIYNLPG LRMYEQEWVRLHLLNLGGSRDIHVVHFHGQTLLENGTQQHQLGVWPLLPGSFKTLEMKASKPGWWLLDTEVGEIQRAGMQ TPFLIVDRECKMPMGLSTGLIADSQIQASEFWGYWEPKLARLNNGGSYNAWIAEKLSTEFNPEPWIQVDMQKEVLLTGIQ TQGAKHYLKPYYTTEFCVAYSLDRKNWRIFKGNSTRNVMYFGGNSDASTIKENQIDPPVVARYIRISPTGSYNKPALRLE LQGCEVNGCSTPLGMESGKIENKQITASSFKKSWWGNYWEPFLARLNAQGRVNAWQAKANNNNQWLQIDLLKIKKITAIV TQGCKSLSSEMYVKSYTIHYSDQGTDWKPYREKSSMVDKIFEGNNNVRGHVKNFFNPPIISRFIRIIPKTWNQSIALRLE LFGCDMY ; ;SNTGNRKYYYIAAEEISWDYSKFVQSDDVDYVPEDTVYKKVVFRKYLDSTFTKLDPQGEYEEHLGILGPVIRAEVDDVIQ VRFKNLASRPYSLHAHGLSYEKSSEGKTYEDDSPEWFKEDNAIQPNKTYTYVWHATTRSGPENPGSACRAWAYYSAVNPE KDIHSGLIGPLLICRKGTLDKETNMPVDMREFVLLFMVFDEKKSWYYDKKPTRSWRRASSEVKNSHEFHAINGMIYNLPG LRMYEQEWVRLHLLNLGGSRDIHVVHFHGQTLLENGTQQHQLGVWPLLPGSFKTLEMKASKPGWWLLDTEVGEIQRAGMQ TPFLIVDRECKMPMGLSTGLIADSQIQASEFWGYWEPKLARLNNGGSYNAWIAEKLSTEFNPEPWIQVDMQKEVLLTGIQ TQGAKHYLKPYYTTEFCVAYSLDRKNWRIFKGNSTRNVMYFGGNSDASTIKENQIDPPVVARYIRISPTGSYNKPALRLE LQGCEVNGCSTPLGMESGKIENKQITASSFKKSWWGNYWEPFLARLNAQGRVNAWQAKANNNNQWLQIDLLKIKKITAIV TQGCKSLSSEMYVKSYTIHYSDQGTDWKPYREKSSMVDKIFEGNNNVRGHVKNFFNPPIISRFIRIIPKTWNQSIALRLE LFGCDMY ; B ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 ALA n 1 2 LYS n 1 3 LEU n 1 4 ARG n 1 5 GLN n 1 6 PHE n 1 7 TYR n 1 8 VAL n 1 9 ALA n 1 10 ALA n 1 11 GLN n 1 12 SER n 1 13 ILE n 1 14 ARG n 1 15 TRP n 1 16 ASN n 1 17 TYR n 1 18 ARG n 1 19 PRO n 1 20 GLU n 1 21 SER n 1 22 THR n 1 23 HIS n 1 24 LEU n 1 25 SER n 1 26 SER n 1 27 LYS n 1 28 PRO n 1 29 PHE n 1 30 GLU n 1 31 THR n 1 32 SER n 1 33 PHE n 1 34 LYS n 1 35 LYS n 1 36 ILE n 1 37 VAL n 1 38 TYR n 1 39 ARG n 1 40 GLU n 1 41 TYR n 1 42 GLU n 1 43 ALA n 1 44 TYR n 1 45 PHE n 1 46 GLN n 1 47 LYS n 1 48 GLU n 1 49 LYS n 1 50 PRO n 1 51 GLN n 1 52 SER n 1 53 ARG n 1 54 THR n 1 55 SER n 1 56 GLY n 1 57 LEU n 1 58 LEU n 1 59 GLY n 1 60 PRO n 1 61 THR n 1 62 LEU n 1 63 TYR n 1 64 ALA n 1 65 GLU n 1 66 VAL n 1 67 GLY n 1 68 ASP n 1 69 ILE n 1 70 MET n 1 71 LYS n 1 72 VAL n 1 73 HIS n 1 74 PHE n 1 75 LYS n 1 76 ASN n 1 77 LYS n 1 78 ALA n 1 79 HIS n 1 80 LYS n 1 81 PRO n 1 82 LEU n 1 83 SER n 1 84 ILE n 1 85 HIS n 1 86 ALA n 1 87 GLN n 1 88 GLY n 1 89 ILE n 1 90 LYS n 1 91 TYR n 1 92 SER n 1 93 LYS n 1 94 PHE n 1 95 SER n 1 96 GLU n 1 97 GLY n 1 98 ALA n 1 99 SER n 1 100 TYR n 1 101 SER n 1 102 ASP n 1 103 HIS n 1 104 THR n 1 105 LEU n 1 106 PRO n 1 107 MET n 1 108 GLU n 1 109 LYS n 1 110 MET n 1 111 ASP n 1 112 ASP n 1 113 ALA n 1 114 VAL n 1 115 ALA n 1 116 PRO n 1 117 GLY n 1 118 GLN n 1 119 GLU n 1 120 TYR n 1 121 THR n 1 122 TYR n 1 123 GLU n 1 124 TRP n 1 125 ILE n 1 126 ILE n 1 127 SER n 1 128 GLU n 1 129 HIS n 1 130 SER n 1 131 GLY n 1 132 PRO n 1 133 THR n 1 134 HIS n 1 135 ASP n 1 136 ASP n 1 137 PRO n 1 138 PRO n 1 139 CYS n 1 140 LEU n 1 141 THR n 1 142 HIS n 1 143 ILE n 1 144 TYR n 1 145 TYR n 1 146 SER n 1 147 TYR n 1 148 VAL n 1 149 ASN n 1 150 LEU n 1 151 VAL n 1 152 GLU n 1 153 ASP n 1 154 PHE n 1 155 ASN n 1 156 SER n 1 157 GLY n 1 158 LEU n 1 159 ILE n 1 160 GLY n 1 161 PRO n 1 162 LEU n 1 163 LEU n 1 164 ILE n 1 165 CYS n 1 166 LYS n 1 167 LYS n 1 168 GLY n 1 169 THR n 1 170 LEU n 1 171 THR n 1 172 GLU n 1 173 ASP n 1 174 GLY n 1 175 THR n 1 176 GLN n 1 177 LYS n 1 178 MET n 1 179 PHE n 1 180 GLU n 1 181 LYS n 1 182 GLN n 1 183 HIS n 1 184 VAL n 1 185 LEU n 1 186 MET n 1 187 PHE n 1 188 ALA n 1 189 VAL n 1 190 PHE n 1 191 ASP n 1 192 GLU n 1 193 SER n 1 194 LYS n 1 195 SER n 1 196 TRP n 1 197 ASN n 1 198 GLN n 1 199 THR n 1 200 SER n 1 201 SER n 1 202 LEU n 1 203 MET n 1 204 TYR n 1 205 THR n 1 206 VAL n 1 207 ASN n 1 208 GLY n 1 209 TYR n 1 210 VAL n 1 211 ASN n 1 212 GLY n 1 213 THR n 1 214 MET n 1 215 PRO n 1 216 ASP n 1 217 ILE n 1 218 THR n 1 219 VAL n 1 220 CYS n 1 221 ALA n 1 222 HIS n 1 223 ASP n 1 224 HIS n 1 225 ILE n 1 226 SER n 1 227 TRP n 1 228 HIS n 1 229 LEU n 1 230 ILE n 1 231 GLY n 1 232 MET n 1 233 SER n 1 234 SER n 1 235 GLY n 1 236 PRO n 1 237 GLU n 1 238 LEU n 1 239 PHE n 1 240 SER n 1 241 ILE n 1 242 HIS n 1 243 PHE n 1 244 ASN n 1 245 GLY n 1 246 GLN n 1 247 VAL n 1 248 LEU n 1 249 GLU n 1 250 GLN n 1 251 ASN n 1 252 HIS n 1 253 HIS n 1 254 LYS n 1 255 ILE n 1 256 SER n 1 257 ALA n 1 258 ILE n 1 259 THR n 1 260 LEU n 1 261 VAL n 1 262 SER n 1 263 ALA n 1 264 THR n 1 265 SER n 1 266 THR n 1 267 THR n 1 268 ALA n 1 269 ASN n 1 270 MET n 1 271 THR n 1 272 VAL n 1 273 SER n 1 274 PRO n 1 275 GLU n 1 276 GLY n 1 277 ARG n 1 278 TRP n 1 279 THR n 1 280 ILE n 1 281 ALA n 1 282 SER n 1 283 LEU n 1 284 ILE n 1 285 PRO n 1 286 ARG n 1 287 HIS n 1 288 PHE n 1 289 GLN n 1 290 ALA n 1 291 GLY n 1 292 MET n 1 293 GLN n 1 294 ALA n 1 295 TYR n 1 296 ILE n 1 297 ASP n 1 298 ILE n 1 299 LYS n 1 300 ASN n 1 301 CYS n 1 302 ALA n 1 303 LYS n 1 304 LYS n 1 305 THR n 1 306 ARG n 2 1 SER n 2 2 ASN n 2 3 THR n 2 4 GLY n 2 5 ASN n 2 6 ARG n 2 7 LYS n 2 8 TYR n 2 9 TYR n 2 10 TYR n 2 11 ILE n 2 12 ALA n 2 13 ALA n 2 14 GLU n 2 15 GLU n 2 16 ILE n 2 17 SER n 2 18 TRP n 2 19 ASP n 2 20 TYR n 2 21 SER n 2 22 LYS n 2 23 PHE n 2 24 VAL n 2 25 GLN n 2 26 SER n 2 27 ASP n 2 28 ASP n 2 29 VAL n 2 30 ASP n 2 31 TYR n 2 32 VAL n 2 33 PRO n 2 34 GLU n 2 35 ASP n 2 36 THR n 2 37 VAL n 2 38 TYR n 2 39 LYS n 2 40 LYS n 2 41 VAL n 2 42 VAL n 2 43 PHE n 2 44 ARG n 2 45 LYS n 2 46 TYR n 2 47 LEU n 2 48 ASP n 2 49 SER n 2 50 THR n 2 51 PHE n 2 52 THR n 2 53 LYS n 2 54 LEU n 2 55 ASP n 2 56 PRO n 2 57 GLN n 2 58 GLY n 2 59 GLU n 2 60 TYR n 2 61 GLU n 2 62 GLU n 2 63 HIS n 2 64 LEU n 2 65 GLY n 2 66 ILE n 2 67 LEU n 2 68 GLY n 2 69 PRO n 2 70 VAL n 2 71 ILE n 2 72 ARG n 2 73 ALA n 2 74 GLU n 2 75 VAL n 2 76 ASP n 2 77 ASP n 2 78 VAL n 2 79 ILE n 2 80 GLN n 2 81 VAL n 2 82 ARG n 2 83 PHE n 2 84 LYS n 2 85 ASN n 2 86 LEU n 2 87 ALA n 2 88 SER n 2 89 ARG n 2 90 PRO n 2 91 TYR n 2 92 SER n 2 93 LEU n 2 94 HIS n 2 95 ALA n 2 96 HIS n 2 97 GLY n 2 98 LEU n 2 99 SER n 2 100 TYR n 2 101 GLU n 2 102 LYS n 2 103 SER n 2 104 SER n 2 105 GLU n 2 106 GLY n 2 107 LYS n 2 108 THR n 2 109 TYR n 2 110 GLU n 2 111 ASP n 2 112 ASP n 2 113 SER n 2 114 PRO n 2 115 GLU n 2 116 TRP n 2 117 PHE n 2 118 LYS n 2 119 GLU n 2 120 ASP n 2 121 ASN n 2 122 ALA n 2 123 ILE n 2 124 GLN n 2 125 PRO n 2 126 ASN n 2 127 LYS n 2 128 THR n 2 129 TYR n 2 130 THR n 2 131 TYR n 2 132 VAL n 2 133 TRP n 2 134 HIS n 2 135 ALA n 2 136 THR n 2 137 THR n 2 138 ARG n 2 139 SER n 2 140 GLY n 2 141 PRO n 2 142 GLU n 2 143 ASN n 2 144 PRO n 2 145 GLY n 2 146 SER n 2 147 ALA n 2 148 CYS n 2 149 ARG n 2 150 ALA n 2 151 TRP n 2 152 ALA n 2 153 TYR n 2 154 TYR n 2 155 SER n 2 156 ALA n 2 157 VAL n 2 158 ASN n 2 159 PRO n 2 160 GLU n 2 161 LYS n 2 162 ASP n 2 163 ILE n 2 164 HIS n 2 165 SER n 2 166 GLY n 2 167 LEU n 2 168 ILE n 2 169 GLY n 2 170 PRO n 2 171 LEU n 2 172 LEU n 2 173 ILE n 2 174 CYS n 2 175 ARG n 2 176 LYS n 2 177 GLY n 2 178 THR n 2 179 LEU n 2 180 ASP n 2 181 LYS n 2 182 GLU n 2 183 THR n 2 184 ASN n 2 185 MET n 2 186 PRO n 2 187 VAL n 2 188 ASP n 2 189 MET n 2 190 ARG n 2 191 GLU n 2 192 PHE n 2 193 VAL n 2 194 LEU n 2 195 LEU n 2 196 PHE n 2 197 MET n 2 198 VAL n 2 199 PHE n 2 200 ASP n 2 201 GLU n 2 202 LYS n 2 203 LYS n 2 204 SER n 2 205 TRP n 2 206 TYR n 2 207 TYR n 2 208 ASP n 2 209 LYS n 2 210 LYS n 2 211 PRO n 2 212 THR n 2 213 ARG n 2 214 SER n 2 215 TRP n 2 216 ARG n 2 217 ARG n 2 218 ALA n 2 219 SER n 2 220 SER n 2 221 GLU n 2 222 VAL n 2 223 LYS n 2 224 ASN n 2 225 SER n 2 226 HIS n 2 227 GLU n 2 228 PHE n 2 229 HIS n 2 230 ALA n 2 231 ILE n 2 232 ASN n 2 233 GLY n 2 234 MET n 2 235 ILE n 2 236 TYR n 2 237 ASN n 2 238 LEU n 2 239 PRO n 2 240 GLY n 2 241 LEU n 2 242 ARG n 2 243 MET n 2 244 TYR n 2 245 GLU n 2 246 GLN n 2 247 GLU n 2 248 TRP n 2 249 VAL n 2 250 ARG n 2 251 LEU n 2 252 HIS n 2 253 LEU n 2 254 LEU n 2 255 ASN n 2 256 LEU n 2 257 GLY n 2 258 GLY n 2 259 SER n 2 260 ARG n 2 261 ASP n 2 262 ILE n 2 263 HIS n 2 264 VAL n 2 265 VAL n 2 266 HIS n 2 267 PHE n 2 268 HIS n 2 269 GLY n 2 270 GLN n 2 271 THR n 2 272 LEU n 2 273 LEU n 2 274 GLU n 2 275 ASN n 2 276 GLY n 2 277 THR n 2 278 GLN n 2 279 GLN n 2 280 HIS n 2 281 GLN n 2 282 LEU n 2 283 GLY n 2 284 VAL n 2 285 TRP n 2 286 PRO n 2 287 LEU n 2 288 LEU n 2 289 PRO n 2 290 GLY n 2 291 SER n 2 292 PHE n 2 293 LYS n 2 294 THR n 2 295 LEU n 2 296 GLU n 2 297 MET n 2 298 LYS n 2 299 ALA n 2 300 SER n 2 301 LYS n 2 302 PRO n 2 303 GLY n 2 304 TRP n 2 305 TRP n 2 306 LEU n 2 307 LEU n 2 308 ASP n 2 309 THR n 2 310 GLU n 2 311 VAL n 2 312 GLY n 2 313 GLU n 2 314 ILE n 2 315 GLN n 2 316 ARG n 2 317 ALA n 2 318 GLY n 2 319 MET n 2 320 GLN n 2 321 THR n 2 322 PRO n 2 323 PHE n 2 324 LEU n 2 325 ILE n 2 326 VAL n 2 327 ASP n 2 328 ARG n 2 329 GLU n 2 330 CYS n 2 331 LYS n 2 332 MET n 2 333 PRO n 2 334 MET n 2 335 GLY n 2 336 LEU n 2 337 SER n 2 338 THR n 2 339 GLY n 2 340 LEU n 2 341 ILE n 2 342 ALA n 2 343 ASP n 2 344 SER n 2 345 GLN n 2 346 ILE n 2 347 GLN n 2 348 ALA n 2 349 SER n 2 350 GLU n 2 351 PHE n 2 352 TRP n 2 353 GLY n 2 354 TYR n 2 355 TRP n 2 356 GLU n 2 357 PRO n 2 358 LYS n 2 359 LEU n 2 360 ALA n 2 361 ARG n 2 362 LEU n 2 363 ASN n 2 364 ASN n 2 365 GLY n 2 366 GLY n 2 367 SER n 2 368 TYR n 2 369 ASN n 2 370 ALA n 2 371 TRP n 2 372 ILE n 2 373 ALA n 2 374 GLU n 2 375 LYS n 2 376 LEU n 2 377 SER n 2 378 THR n 2 379 GLU n 2 380 PHE n 2 381 ASN n 2 382 PRO n 2 383 GLU n 2 384 PRO n 2 385 TRP n 2 386 ILE n 2 387 GLN n 2 388 VAL n 2 389 ASP n 2 390 MET n 2 391 GLN n 2 392 LYS n 2 393 GLU n 2 394 VAL n 2 395 LEU n 2 396 LEU n 2 397 THR n 2 398 GLY n 2 399 ILE n 2 400 GLN n 2 401 THR n 2 402 GLN n 2 403 GLY n 2 404 ALA n 2 405 LYS n 2 406 HIS n 2 407 TYR n 2 408 LEU n 2 409 LYS n 2 410 PRO n 2 411 TYR n 2 412 TYR n 2 413 THR n 2 414 THR n 2 415 GLU n 2 416 PHE n 2 417 CYS n 2 418 VAL n 2 419 ALA n 2 420 TYR n 2 421 SER n 2 422 LEU n 2 423 ASP n 2 424 ARG n 2 425 LYS n 2 426 ASN n 2 427 TRP n 2 428 ARG n 2 429 ILE n 2 430 PHE n 2 431 LYS n 2 432 GLY n 2 433 ASN n 2 434 SER n 2 435 THR n 2 436 ARG n 2 437 ASN n 2 438 VAL n 2 439 MET n 2 440 TYR n 2 441 PHE n 2 442 GLY n 2 443 GLY n 2 444 ASN n 2 445 SER n 2 446 ASP n 2 447 ALA n 2 448 SER n 2 449 THR n 2 450 ILE n 2 451 LYS n 2 452 GLU n 2 453 ASN n 2 454 GLN n 2 455 ILE n 2 456 ASP n 2 457 PRO n 2 458 PRO n 2 459 VAL n 2 460 VAL n 2 461 ALA n 2 462 ARG n 2 463 TYR n 2 464 ILE n 2 465 ARG n 2 466 ILE n 2 467 SER n 2 468 PRO n 2 469 THR n 2 470 GLY n 2 471 SER n 2 472 TYR n 2 473 ASN n 2 474 LYS n 2 475 PRO n 2 476 ALA n 2 477 LEU n 2 478 ARG n 2 479 LEU n 2 480 GLU n 2 481 LEU n 2 482 GLN n 2 483 GLY n 2 484 CYS n 2 485 GLU n 2 486 VAL n 2 487 ASN n 2 488 GLY n 2 489 CYS n 2 490 SER n 2 491 THR n 2 492 PRO n 2 493 LEU n 2 494 GLY n 2 495 MET n 2 496 GLU n 2 497 SER n 2 498 GLY n 2 499 LYS n 2 500 ILE n 2 501 GLU n 2 502 ASN n 2 503 LYS n 2 504 GLN n 2 505 ILE n 2 506 THR n 2 507 ALA n 2 508 SER n 2 509 SER n 2 510 PHE n 2 511 LYS n 2 512 LYS n 2 513 SER n 2 514 TRP n 2 515 TRP n 2 516 GLY n 2 517 ASN n 2 518 TYR n 2 519 TRP n 2 520 GLU n 2 521 PRO n 2 522 PHE n 2 523 LEU n 2 524 ALA n 2 525 ARG n 2 526 LEU n 2 527 ASN n 2 528 ALA n 2 529 GLN n 2 530 GLY n 2 531 ARG n 2 532 VAL n 2 533 ASN n 2 534 ALA n 2 535 TRP n 2 536 GLN n 2 537 ALA n 2 538 LYS n 2 539 ALA n 2 540 ASN n 2 541 ASN n 2 542 ASN n 2 543 ASN n 2 544 GLN n 2 545 TRP n 2 546 LEU n 2 547 GLN n 2 548 ILE n 2 549 ASP n 2 550 LEU n 2 551 LEU n 2 552 LYS n 2 553 ILE n 2 554 LYS n 2 555 LYS n 2 556 ILE n 2 557 THR n 2 558 ALA n 2 559 ILE n 2 560 VAL n 2 561 THR n 2 562 GLN n 2 563 GLY n 2 564 CYS n 2 565 LYS n 2 566 SER n 2 567 LEU n 2 568 SER n 2 569 SER n 2 570 GLU n 2 571 MET n 2 572 TYR n 2 573 VAL n 2 574 LYS n 2 575 SER n 2 576 TYR n 2 577 THR n 2 578 ILE n 2 579 HIS n 2 580 TYR n 2 581 SER n 2 582 ASP n 2 583 GLN n 2 584 GLY n 2 585 THR n 2 586 ASP n 2 587 TRP n 2 588 LYS n 2 589 PRO n 2 590 TYR n 2 591 ARG n 2 592 GLU n 2 593 LYS n 2 594 SER n 2 595 SER n 2 596 MET n 2 597 VAL n 2 598 ASP n 2 599 LYS n 2 600 ILE n 2 601 PHE n 2 602 GLU n 2 603 GLY n 2 604 ASN n 2 605 ASN n 2 606 ASN n 2 607 VAL n 2 608 ARG n 2 609 GLY n 2 610 HIS n 2 611 VAL n 2 612 LYS n 2 613 ASN n 2 614 PHE n 2 615 PHE n 2 616 ASN n 2 617 PRO n 2 618 PRO n 2 619 ILE n 2 620 ILE n 2 621 SER n 2 622 ARG n 2 623 PHE n 2 624 ILE n 2 625 ARG n 2 626 ILE n 2 627 ILE n 2 628 PRO n 2 629 LYS n 2 630 THR n 2 631 TRP n 2 632 ASN n 2 633 GLN n 2 634 SER n 2 635 ILE n 2 636 ALA n 2 637 LEU n 2 638 ARG n 2 639 LEU n 2 640 GLU n 2 641 LEU n 2 642 PHE n 2 643 GLY n 2 644 CYS n 2 645 ASP n 2 646 MET n 2 647 TYR 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 ? ? cattle 'Bos taurus' 9913 Bos ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 'purified from plasma' 2 1 sample ? ? cattle 'Bos taurus' 9913 Bos ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 'purified from plasma' # 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 FA5_BOVIN Q28107 1 ;AKLRQFYVAAQSIRWNYRPESTHLSSKPFETSFKKIVYREYEAYFQKEKPQSRTSGLLGPTLYAEVGDIMKVHFKNKAHK PLSIHAQGIKYSKFSEGASYSDHTLPMEKMDDAVAPGQEYTYEWIISEHSGPTHDDPPCLTHIYYSYVNLVEDFNSGLIG PLLICKKGTLTEDGTQKMFEKQHVLMFAVFDESKSWNQTSSLMYTVNGYVNGTMPDITVCAHDHISWHLIGMSSGPELFS IHFNGQVLEQNHHKISAITLVSATSTTANMTVSPEGRWTIASLIPRHFQAGMQAYIDIKNCAKKTR ; 29 ? 2 UNP FA5_BOVIN Q28107 2 ;SNTGNRKYYYIAAEEISWDYSKFVQSDDVDYVPEDTVYKKVVFRKYLDSTFTKLDPQGEYEEHLGILGPVIRAEVDDVIQ VRFKNLASRPYSLHAHGLSYEKSSEGKTYEDDSPEWFKEDNAIQPNKTYTYVWHATTRSGPENPGSACRAWAYYSAVNPE KDIHSGLIGPLLICRKGTLDKETNMPVDMREFVLLFMVFDEKKSWYYDKKPTRSWRRASSEVKNSHEFHAINGMIYNLPG LRMYEQEWVRLHLLNLGGSRDIHVVHFHGQTLLENGTQQHQLGVWPLLPGSFKTLEMKASKPGWWLLDTEVGEIQRAGMQ TPFLIVDRECKMPMGLSTGLIADSQIQASEFWGYWEPKLARLNNGGSYNAWIAEKLSTEFNPEPWIQVDMQKEVLLTGIQ TQGAKHYLKPYYTTEFCVAYSLDRKNWRIFKGNSTRNVMYFGGNSDASTIKENQIDPPVVARYIRISPTGSYNKPALRLE LQGCEVNGCSTPLGMESGKIENKQITASSFKKSWWGNYWEPFLARLNAQGRVNAWQAKANNNNQWLQIDLLKIKKITAIV TQGCKSLSSEMYVKSYTIHYSDQGTDWKPYREKSSMVDKIFEGNNNVRGHVKNFFNPPIISRFIRIIPKTWNQSIALRLE LFGCDMY ; 1565 ? # 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 1SDD A 1 ? 306 ? Q28107 29 ? 334 ? 1 306 2 2 1SDD B 1 ? 647 ? Q28107 1565 ? 2211 ? 1537 2183 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 CA non-polymer . 'CALCIUM ION' ? 'Ca 2' 40.078 CU non-polymer . 'COPPER (II) ION' ? 'Cu 2' 63.546 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 NDG D-saccharide . '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 1SDD _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 4 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_percent_sol 60.90 _exptl_crystal.description ? _exptl_crystal.density_Matthews 3.17 _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, SITTING DROP' _exptl_crystal_grow.temp 285 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 7.0 _exptl_crystal_grow.pdbx_details 'PEG3350, MAGNESIUM CHLORIDE, CALCIUM CHLORIDE, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 285K' _exptl_crystal_grow.pdbx_pH_range . # loop_ _diffrn.id _diffrn.ambient_temp _diffrn.ambient_temp_details _diffrn.crystal_id 1 100 ? 1 2 100 ? 1 3 100 ? 1 4 100 ? 1 1,2,3,4 ? ? 1 # loop_ _diffrn_detector.diffrn_id _diffrn_detector.detector _diffrn_detector.type _diffrn_detector.pdbx_collection_date _diffrn_detector.details 1 CCD 'ADSC QUANTUM 4' 2002-03-20 ? 2 CCD 'BRANDEIS - B1.3' 2001-04-12 ? 3 CCD 'BRANDEIS - B4' 2000-03-10 ? 4 CCD 'BRANDEIS - B4' 2000-03-09 ? # loop_ _diffrn_radiation.diffrn_id _diffrn_radiation.wavelength_id _diffrn_radiation.pdbx_monochromatic_or_laue_m_l _diffrn_radiation.monochromator _diffrn_radiation.pdbx_diffrn_protocol _diffrn_radiation.pdbx_scattering_type 1 1 M 'Rh-COATED Si' 'SINGLE WAVELENGTH' x-ray 2 1 M 'CHANNEL-CUT Si(111)' MAD x-ray 3 1 M 'CHANNEL-CUT Si(111)' 'SINGLE WAVELENGTH' x-ray 4 1 M 'CHANNEL-CUT Si(111)' 'SINGLE WAVELENGTH' x-ray # loop_ _diffrn_radiation_wavelength.id _diffrn_radiation_wavelength.wavelength _diffrn_radiation_wavelength.wt 1 0.935 1.0 2 0.9803 1.0 3 1.0097 1.0 4 1.0106 1.0 5 1.100 1.0 # loop_ _diffrn_source.diffrn_id _diffrn_source.source _diffrn_source.type _diffrn_source.pdbx_synchrotron_site _diffrn_source.pdbx_synchrotron_beamline _diffrn_source.pdbx_wavelength _diffrn_source.pdbx_wavelength_list 1 SYNCHROTRON 'CHESS BEAMLINE A1' CHESS A1 ? 0.935 2 SYNCHROTRON 'NSLS BEAMLINE X12C' NSLS X12C ? '0.9803, 1.0097, 1.0106' 3 SYNCHROTRON 'NSLS BEAMLINE X25' NSLS X25 ? 1.100 4 SYNCHROTRON 'NSLS BEAMLINE X25' NSLS X25 ? 1.100 # _reflns.entry_id 1SDD _reflns.observed_criterion_sigma_F 1.0 _reflns.observed_criterion_sigma_I 1.0 _reflns.d_resolution_high 2.8 _reflns.d_resolution_low 30 _reflns.number_all 32016 _reflns.number_obs 28745 _reflns.percent_possible_obs 88.8 _reflns.pdbx_Rmerge_I_obs 0.049 _reflns.pdbx_Rsym_value 0.054 _reflns.pdbx_netI_over_sigmaI 7.2 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 4.2 _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 1,2,3,4 # _reflns_shell.d_res_high 2.80 _reflns_shell.d_res_low 2.90 _reflns_shell.percent_possible_all 80.8 _reflns_shell.Rmerge_I_obs 0.206 _reflns_shell.pdbx_Rsym_value 0.307 _reflns_shell.meanI_over_sigI_obs 2.3 _reflns_shell.pdbx_redundancy 2.0 _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all 3154 _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 1,2,3,4 # _refine.entry_id 1SDD _refine.ls_d_res_high 2.8 _refine.ls_d_res_low 30 _refine.pdbx_ls_sigma_F 0.0 _refine.pdbx_ls_sigma_I ? _refine.ls_number_reflns_all 31911 _refine.ls_number_reflns_obs 28745 _refine.ls_number_reflns_R_free 1098 _refine.ls_percent_reflns_obs 90.1 _refine.ls_R_factor_all 0.258 _refine.ls_R_factor_obs 0.262 _refine.ls_R_factor_R_work 0.252 _refine.ls_R_factor_R_free 0.296 _refine.ls_redundancy_reflns_obs ? _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.ls_percent_reflns_R_free ? _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.pdbx_method_to_determine_struct 'MIR + MAD' _refine.pdbx_starting_model ? _refine.pdbx_ls_cross_valid_method ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_stereochemistry_target_values 'Engh & Huber' _refine.solvent_model_details ? _refine.solvent_model_param_bsol ? _refine.solvent_model_param_ksol ? _refine.occupancy_max ? _refine.occupancy_min ? _refine.pdbx_isotropic_thermal_model ? _refine.B_iso_mean ? _refine.aniso_B[1][1] ? _refine.aniso_B[1][2] ? _refine.aniso_B[1][3] ? _refine.aniso_B[2][2] ? _refine.aniso_B[2][3] ? _refine.aniso_B[3][3] ? _refine.details ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.pdbx_solvent_vdw_probe_radii ? _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.overall_SU_B ? _refine.overall_SU_ML ? _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.pdbx_data_cutoff_high_rms_absF ? _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 1SDD _refine_analyze.Luzzati_coordinate_error_obs 0.45 _refine_analyze.Luzzati_sigma_a_obs 0.55 _refine_analyze.Luzzati_d_res_low_obs 5.0 _refine_analyze.Luzzati_coordinate_error_free 0.56 _refine_analyze.Luzzati_sigma_a_free 0.63 _refine_analyze.Luzzati_d_res_low_free ? _refine_analyze.number_disordered_residues ? _refine_analyze.occupancy_sum_non_hydrogen ? _refine_analyze.occupancy_sum_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 7010 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 72 _refine_hist.number_atoms_solvent 189 _refine_hist.number_atoms_total 7271 _refine_hist.d_res_high 2.8 _refine_hist.d_res_low 30 # 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 x_angle_deg 1.94 ? ? ? 'X-RAY DIFFRACTION' ? x_bond_d 0.019 ? ? ? 'X-RAY DIFFRACTION' ? x_dihedral_angle_d 25.56 ? ? ? 'X-RAY DIFFRACTION' ? x_improper_angle_d 1.19 ? ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_total_number_of_bins_used ? _refine_ls_shell.d_res_high 2.80 _refine_ls_shell.d_res_low 2.90 _refine_ls_shell.number_reflns_R_work ? _refine_ls_shell.R_factor_R_work 0.388 _refine_ls_shell.percent_reflns_obs 76.4 _refine_ls_shell.R_factor_R_free 0.446 _refine_ls_shell.R_factor_R_free_error 0.035 _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 72 _refine_ls_shell.number_reflns_obs 2409 _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 ? # _struct.entry_id 1SDD _struct.title 'Crystal Structure of Bovine Factor Vai' _struct.pdbx_descriptor 'Coagulation factor V' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 1SDD _struct_keywords.pdbx_keywords 'BLOOD CLOTTING' _struct_keywords.text 'COAGULATION, COPPER-BINDING PROTEIN, COFACTOR, BLOOD CLOTTING' # 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 3 ? E N N 4 ? F N N 5 ? G N N 3 ? H N N 5 ? I N N 6 ? J N N 7 ? K N N 7 ? # _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 LEU A 105 ? MET A 110 ? LEU A 105 MET A 110 1 ? 6 HELX_P HELX_P2 2 SER A 127 ? GLY A 131 ? SER A 127 GLY A 131 5 ? 5 HELX_P HELX_P3 3 LEU A 150 ? SER A 156 ? LEU A 150 SER A 156 1 ? 7 HELX_P HELX_P4 4 HIS A 287 ? GLY A 291 ? HIS A 287 GLY A 291 5 ? 5 HELX_P HELX_P5 5 GLU B 61 ? GLY B 65 ? GLU B 1597 GLY B 1601 5 ? 5 HELX_P HELX_P6 6 ASN B 158 ? HIS B 164 ? ASN B 1694 HIS B 1700 1 ? 7 HELX_P HELX_P7 7 LYS B 202 ? SER B 204 ? LYS B 1738 SER B 1740 5 ? 3 HELX_P HELX_P8 8 VAL B 311 ? ARG B 316 ? VAL B 1847 ARG B 1852 1 ? 6 HELX_P HELX_P9 9 ALA B 342 ? SER B 344 ? ALA B 1878 SER B 1880 5 ? 3 HELX_P HELX_P10 10 GLU B 356 ? ALA B 360 ? GLU B 1892 ALA B 1896 5 ? 5 HELX_P HELX_P11 11 GLU B 520 ? ALA B 524 ? GLU B 2056 ALA B 2060 5 ? 5 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 139 SG ? ? ? 1_555 A CYS 165 SG ? ? A CYS 139 A CYS 165 1_555 ? ? ? ? ? ? ? 2.030 ? disulf2 disulf ? ? B CYS 148 SG ? ? ? 1_555 B CYS 174 SG ? ? B CYS 1684 B CYS 1710 1_555 ? ? ? ? ? ? ? 2.031 ? disulf3 disulf ? ? B CYS 330 SG ? ? ? 1_555 B CYS 484 SG ? ? B CYS 1866 B CYS 2020 1_555 ? ? ? ? ? ? ? 2.036 ? disulf4 disulf ? ? B CYS 489 SG ? ? ? 1_555 B CYS 644 SG ? ? B CYS 2025 B CYS 2180 1_555 ? ? ? ? ? ? ? 2.047 ? metalc1 metalc ? ? A LYS 93 O ? ? ? 1_555 E CA . CA ? ? A LYS 93 A CA 2184 1_555 ? ? ? ? ? ? ? 2.251 ? metalc2 metalc ? ? A GLU 108 O ? ? ? 1_555 E CA . CA ? ? A GLU 108 A CA 2184 1_555 ? ? ? ? ? ? ? 2.972 ? metalc3 metalc ? ? A ASP 111 OD1 ? ? ? 1_555 E CA . CA ? ? A ASP 111 A CA 2184 1_555 ? ? ? ? ? ? ? 2.262 ? metalc4 metalc ? ? A ASP 111 OD2 ? ? ? 1_555 E CA . CA ? ? A ASP 111 A CA 2184 1_555 ? ? ? ? ? ? ? 2.691 ? covale1 covale ? ? A ASN 197 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 197 A NAG 2185 1_555 ? ? ? ? ? ? ? 1.452 ? covale2 covale ? ? A ASN 211 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 211 A NAG 2186 1_555 ? ? ? ? ? ? ? 1.448 ? metalc5 metalc ? ? B HIS 266 ND1 ? ? ? 1_555 I CU . CU ? ? B HIS 1802 B CU 2190 1_555 ? ? ? ? ? ? ? 2.275 ? covale3 covale ? ? B ASN 275 ND2 ? ? ? 1_555 G NAG . C1 ? ? B ASN 1811 B NAG 2188 1_555 ? ? ? ? ? ? ? 1.454 ? metalc6 metalc ? ? B ASP 308 OD1 ? ? ? 1_555 I CU . CU ? ? B ASP 1844 B CU 2190 1_555 ? ? ? ? ? ? ? 2.208 ? metalc7 metalc ? ? B ASP 308 OD2 ? ? ? 1_555 I CU . CU ? ? B ASP 1844 B CU 2190 1_555 ? ? ? ? ? ? ? 2.397 ? covale4 covale ? ? B ASN 126 ND2 ? ? ? 1_555 F NDG . C1 ? ? B ASN 1662 B NDG 2187 1_555 ? ? ? ? ? ? ? 1.457 ? covale5 covale ? ? B ASN 433 ND2 ? ? ? 1_555 H NDG . C1 ? ? B ASN 1969 B NDG 2189 1_555 ? ? ? ? ? ? ? 1.448 ? metalc8 metalc ? ? E CA . CA ? ? ? 1_555 A ASP 112 OD2 ? ? A CA 2184 A ASP 112 1_555 ? ? ? ? ? ? ? 1.968 ? metalc9 metalc ? ? I CU . CU ? ? ? 1_555 B ASP 308 CG ? ? B CU 2190 B ASP 1844 1_555 ? ? ? ? ? ? ? 2.632 ? metalc10 metalc ? ? E CA . CA ? ? ? 1_555 A ASP 112 OD1 ? ? A CA 2184 A ASP 112 1_555 ? ? ? ? ? ? ? 3.387 ? metalc11 metalc ? ? I CU . CU ? ? ? 1_555 B HIS 268 NE2 ? ? B CU 2190 B HIS 1804 1_555 ? ? ? ? ? ? ? 2.626 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? metalc ? ? covale ? ? # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 4 ? B ? 3 ? C ? 4 ? D ? 2 ? E ? 2 ? F ? 2 ? G ? 4 ? H ? 4 ? I ? 4 ? J ? 4 ? K ? 5 ? L ? 2 ? M ? 14 ? N ? 4 ? O ? 5 ? P ? 2 ? Q ? 3 ? R ? 3 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? parallel A 2 3 ? parallel A 3 4 ? anti-parallel B 1 2 ? parallel B 2 3 ? anti-parallel C 1 2 ? parallel C 2 3 ? anti-parallel C 3 4 ? anti-parallel D 1 2 ? anti-parallel E 1 2 ? anti-parallel F 1 2 ? anti-parallel G 1 2 ? anti-parallel G 2 3 ? parallel G 3 4 ? anti-parallel H 1 2 ? anti-parallel H 2 3 ? parallel H 3 4 ? anti-parallel I 1 2 ? parallel I 2 3 ? anti-parallel I 3 4 ? anti-parallel J 1 2 ? anti-parallel J 2 3 ? parallel J 3 4 ? anti-parallel K 1 2 ? parallel K 2 3 ? anti-parallel K 3 4 ? anti-parallel K 4 5 ? anti-parallel L 1 2 ? anti-parallel M 1 2 ? anti-parallel M 2 3 ? anti-parallel M 3 4 ? anti-parallel M 4 5 ? anti-parallel M 5 6 ? anti-parallel M 6 7 ? anti-parallel M 7 8 ? anti-parallel M 8 9 ? anti-parallel M 9 10 ? anti-parallel M 10 11 ? anti-parallel M 11 12 ? anti-parallel M 12 13 ? anti-parallel M 13 14 ? anti-parallel N 1 2 ? anti-parallel N 2 3 ? anti-parallel N 3 4 ? anti-parallel O 1 2 ? anti-parallel O 2 3 ? anti-parallel O 3 4 ? anti-parallel O 4 5 ? anti-parallel P 1 2 ? anti-parallel Q 1 2 ? anti-parallel Q 2 3 ? anti-parallel R 1 2 ? anti-parallel R 2 3 ? 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 GLN A 5 ? PHE A 6 ? GLN A 5 PHE A 6 A 2 ILE A 69 ? ASN A 76 ? ILE A 69 ASN A 76 A 3 ALA A 9 ? TRP A 15 ? ALA A 9 TRP A 15 A 4 PHE A 33 ? ARG A 39 ? PHE A 33 ARG A 39 B 1 GLN A 5 ? PHE A 6 ? GLN A 5 PHE A 6 B 2 ILE A 69 ? ASN A 76 ? ILE A 69 ASN A 76 B 3 GLU A 119 ? ILE A 125 ? GLU A 119 ILE A 125 C 1 LEU A 62 ? GLU A 65 ? LEU A 62 GLU A 65 C 2 GLY A 160 ? CYS A 165 ? GLY A 160 CYS A 165 C 3 CYS A 139 ? TYR A 145 ? CYS A 139 TYR A 145 C 4 HIS A 85 ? GLN A 87 ? HIS A 85 GLN A 87 D 1 VAL A 189 ? ASP A 191 ? VAL A 189 ASP A 191 D 2 LEU A 202 ? TYR A 204 ? LEU A 202 TYR A 204 E 1 LEU A 238 ? PHE A 239 ? LEU A 238 PHE A 239 E 2 LEU A 260 ? VAL A 261 ? LEU A 260 VAL A 261 F 1 GLU A 249 ? GLN A 250 ? GLU A 249 GLN A 250 F 2 HIS A 253 ? LYS A 254 ? HIS A 253 LYS A 254 G 1 VAL B 37 ? TYR B 46 ? VAL B 1573 TYR B 1582 G 2 ARG B 6 ? ASP B 19 ? ARG B 1542 ASP B 1555 G 3 VAL B 78 ? PHE B 83 ? VAL B 1614 PHE B 1619 G 4 TYR B 129 ? THR B 130 ? TYR B 1665 THR B 1666 H 1 VAL B 37 ? TYR B 46 ? VAL B 1573 TYR B 1582 H 2 ARG B 6 ? ASP B 19 ? ARG B 1542 ASP B 1555 H 3 VAL B 78 ? PHE B 83 ? VAL B 1614 PHE B 1619 H 4 TRP B 133 ? HIS B 134 ? TRP B 1669 HIS B 1670 I 1 ILE B 71 ? GLU B 74 ? ILE B 1607 GLU B 1610 I 2 ILE B 168 ? CYS B 174 ? ILE B 1704 CYS B 1710 I 3 CYS B 148 ? TYR B 154 ? CYS B 1684 TYR B 1690 I 4 HIS B 94 ? HIS B 96 ? HIS B 1630 HIS B 1632 J 1 GLU B 227 ? ILE B 231 ? GLU B 1763 ILE B 1767 J 2 GLU B 191 ? ASP B 200 ? GLU B 1727 ASP B 1736 J 3 TRP B 248 ? ASN B 255 ? TRP B 1784 ASN B 1791 J 4 SER B 291 ? LYS B 298 ? SER B 1827 LYS B 1834 K 1 ARG B 242 ? TYR B 244 ? ARG B 1778 TYR B 1780 K 2 GLN B 320 ? VAL B 326 ? GLN B 1856 VAL B 1862 K 3 GLY B 303 ? ASP B 308 ? GLY B 1839 ASP B 1844 K 4 HIS B 263 ? PHE B 267 ? HIS B 1799 PHE B 1803 K 5 TRP B 285 ? LEU B 287 ? TRP B 1821 LEU B 1823 L 1 LEU B 272 ? GLU B 274 ? LEU B 1808 GLU B 1810 L 2 HIS B 280 ? LEU B 282 ? HIS B 1816 LEU B 1818 M 1 MET B 332 ? PRO B 333 ? MET B 1868 PRO B 1869 M 2 ALA B 476 ? CYS B 484 ? ALA B 2012 CYS B 2020 M 3 TRP B 371 ? ILE B 372 ? TRP B 1907 ILE B 1908 M 4 ALA B 476 ? CYS B 484 ? ALA B 2012 CYS B 2020 M 5 ILE B 386 ? GLN B 402 ? ILE B 1922 GLN B 1938 M 6 ILE B 346 ? ALA B 348 ? ILE B 1882 ALA B 1884 M 7 ILE B 386 ? GLN B 402 ? ILE B 1922 GLN B 1938 M 8 LYS B 451 ? TYR B 472 ? LYS B 1987 TYR B 2008 M 9 PRO B 410 ? SER B 421 ? PRO B 1946 SER B 1957 M 10 ALA B 404 ? LYS B 405 ? ALA B 1940 LYS B 1941 M 11 PRO B 410 ? SER B 421 ? PRO B 1946 SER B 1957 M 12 ARG B 428 ? ILE B 429 ? ARG B 1964 ILE B 1965 M 13 PRO B 410 ? SER B 421 ? PRO B 1946 SER B 1957 M 14 PHE B 441 ? GLY B 442 ? PHE B 1977 GLY B 1978 N 1 ILE B 505 ? ALA B 507 ? ILE B 2041 ALA B 2043 N 2 LEU B 546 ? GLN B 562 ? LEU B 2082 GLN B 2098 N 3 ALA B 636 ? CYS B 644 ? ALA B 2172 CYS B 2180 N 4 TRP B 535 ? GLN B 536 ? TRP B 2071 GLN B 2072 O 1 ILE B 505 ? ALA B 507 ? ILE B 2041 ALA B 2043 O 2 LEU B 546 ? GLN B 562 ? LEU B 2082 GLN B 2098 O 3 VAL B 611 ? ILE B 626 ? VAL B 2147 ILE B 2162 O 4 ILE B 578 ? SER B 581 ? ILE B 2114 SER B 2117 O 5 LYS B 588 ? PRO B 589 ? LYS B 2124 PRO B 2125 P 1 LYS B 512 ? SER B 513 ? LYS B 2048 SER B 2049 P 2 ASN B 517 ? TYR B 518 ? ASN B 2053 TYR B 2054 Q 1 CYS B 564 ? SER B 566 ? CYS B 2100 SER B 2102 Q 2 SER B 569 ? TYR B 576 ? SER B 2105 TYR B 2112 Q 3 PHE B 601 ? GLU B 602 ? PHE B 2137 GLU B 2138 R 1 CYS B 564 ? SER B 566 ? CYS B 2100 SER B 2102 R 2 SER B 569 ? TYR B 576 ? SER B 2105 TYR B 2112 R 3 THR B 630 ? ASN B 632 ? THR B 2166 ASN B 2168 # 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 PHE A 6 ? N PHE A 6 O HIS A 73 ? O HIS A 73 A 2 3 O LYS A 75 ? O LYS A 75 N ALA A 10 ? N ALA A 10 A 3 4 N ILE A 13 ? N ILE A 13 O LYS A 35 ? O LYS A 35 B 1 2 N PHE A 6 ? N PHE A 6 O HIS A 73 ? O HIS A 73 B 2 3 N PHE A 74 ? N PHE A 74 O TYR A 120 ? O TYR A 120 C 1 2 N ALA A 64 ? N ALA A 64 O CYS A 165 ? O CYS A 165 C 2 3 O LEU A 162 ? O LEU A 162 N HIS A 142 ? N HIS A 142 C 3 4 O TYR A 145 ? O TYR A 145 N HIS A 85 ? N HIS A 85 D 1 2 N PHE A 190 ? N PHE A 190 O MET A 203 ? O MET A 203 E 1 2 N PHE A 239 ? N PHE A 239 O LEU A 260 ? O LEU A 260 F 1 2 N GLN A 250 ? N GLN A 250 O HIS A 253 ? O HIS A 253 G 1 2 O ARG B 44 ? O ARG B 1580 N ALA B 12 ? N ALA B 1548 G 2 3 N TYR B 9 ? N TYR B 1545 O ARG B 82 ? O ARG B 1618 G 3 4 N PHE B 83 ? N PHE B 1619 O TYR B 129 ? O TYR B 1665 H 1 2 O ARG B 44 ? O ARG B 1580 N ALA B 12 ? N ALA B 1548 H 2 3 N TYR B 9 ? N TYR B 1545 O ARG B 82 ? O ARG B 1618 H 3 4 N ILE B 79 ? N ILE B 1615 O TRP B 133 ? O TRP B 1669 I 1 2 N ILE B 71 ? N ILE B 1607 O LEU B 172 ? O LEU B 1708 I 2 3 O ILE B 173 ? O ILE B 1709 N ARG B 149 ? N ARG B 1685 I 3 4 O TYR B 154 ? O TYR B 1690 N HIS B 94 ? N HIS B 1630 J 1 2 O PHE B 228 ? O PHE B 1764 N PHE B 199 ? N PHE B 1735 J 2 3 N PHE B 192 ? N PHE B 1728 O HIS B 252 ? O HIS B 1788 J 3 4 N LEU B 253 ? N LEU B 1789 O LYS B 293 ? O LYS B 1829 K 1 2 N MET B 243 ? N MET B 1779 O VAL B 326 ? O VAL B 1862 K 2 3 O PHE B 323 ? O PHE B 1859 N TRP B 305 ? N TRP B 1841 K 3 4 O ASP B 308 ? O ASP B 1844 N HIS B 266 ? N HIS B 1802 K 4 5 N HIS B 263 ? N HIS B 1799 O LEU B 287 ? O LEU B 1823 L 1 2 N GLU B 274 ? N GLU B 1810 O HIS B 280 ? O HIS B 1816 M 1 2 N MET B 332 ? N MET B 1868 O GLY B 483 ? O GLY B 2019 M 2 3 O LEU B 477 ? O LEU B 2013 N TRP B 371 ? N TRP B 1907 M 3 4 N TRP B 371 ? N TRP B 1907 O LEU B 477 ? O LEU B 2013 M 4 5 O GLU B 480 ? O GLU B 2016 N GLN B 400 ? N GLN B 1936 M 5 6 O GLN B 387 ? O GLN B 1923 N GLN B 347 ? N GLN B 1883 M 6 7 N GLN B 347 ? N GLN B 1883 O GLN B 387 ? O GLN B 1923 M 7 8 N ILE B 386 ? N ILE B 1922 O ILE B 466 ? O ILE B 2002 M 8 9 O ARG B 465 ? O ARG B 2001 N ALA B 419 ? N ALA B 1955 M 9 10 O TYR B 411 ? O TYR B 1947 N ALA B 404 ? N ALA B 1940 M 10 11 N ALA B 404 ? N ALA B 1940 O TYR B 411 ? O TYR B 1947 M 11 12 N TYR B 420 ? N TYR B 1956 O ARG B 428 ? O ARG B 1964 M 12 13 O ARG B 428 ? O ARG B 1964 N TYR B 420 ? N TYR B 1956 M 13 14 N PHE B 416 ? N PHE B 1952 O PHE B 441 ? O PHE B 1977 N 1 2 N THR B 506 ? N THR B 2042 O GLN B 547 ? O GLN B 2083 N 2 3 N THR B 557 ? N THR B 2093 O PHE B 642 ? O PHE B 2178 N 3 4 O LEU B 637 ? O LEU B 2173 N TRP B 535 ? N TRP B 2071 O 1 2 N THR B 506 ? N THR B 2042 O GLN B 547 ? O GLN B 2083 O 2 3 N ILE B 556 ? N ILE B 2092 O ILE B 619 ? O ILE B 2155 O 3 4 O PHE B 623 ? O PHE B 2159 N SER B 581 ? N SER B 2117 O 4 5 N TYR B 580 ? N TYR B 2116 O LYS B 588 ? O LYS B 2124 P 1 2 N SER B 513 ? N SER B 2049 O ASN B 517 ? O ASN B 2053 Q 1 2 N SER B 566 ? N SER B 2102 O SER B 569 ? O SER B 2105 Q 2 3 N TYR B 576 ? N TYR B 2112 O PHE B 601 ? O PHE B 2137 R 1 2 N SER B 566 ? N SER B 2102 O SER B 569 ? O SER B 2105 R 2 3 N SER B 575 ? N SER B 2111 O THR B 630 ? O THR B 2166 # 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 ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 2185' AC2 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE NAG A 2186' AC3 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NDG B 2187' AC4 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE NAG B 2188' AC5 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NDG B 2189' AC6 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE CU B 2190' AC7 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CA A 2184' # 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 3 ASN A 197 ? ASN A 197 . ? 1_555 ? 2 AC1 3 GLN A 198 ? GLN A 198 . ? 1_555 ? 3 AC1 3 HOH J . ? HOH A 2305 . ? 1_555 ? 4 AC2 7 TYR A 44 ? TYR A 44 . ? 3_555 ? 5 AC2 7 GLN A 46 ? GLN A 46 . ? 3_555 ? 6 AC2 7 VAL A 210 ? VAL A 210 . ? 1_555 ? 7 AC2 7 ASN A 211 ? ASN A 211 . ? 1_555 ? 8 AC2 7 GLN A 289 ? GLN A 289 . ? 1_555 ? 9 AC2 7 ALA A 290 ? ALA A 290 . ? 1_555 ? 10 AC2 7 HOH J . ? HOH A 2269 . ? 1_555 ? 11 AC3 2 PRO B 125 ? PRO B 1661 . ? 1_555 ? 12 AC3 2 ASN B 126 ? ASN B 1662 . ? 1_555 ? 13 AC4 7 PRO B 144 ? PRO B 1680 . ? 1_555 ? 14 AC4 7 GLY B 145 ? GLY B 1681 . ? 1_555 ? 15 AC4 7 SER B 146 ? SER B 1682 . ? 1_555 ? 16 AC4 7 ARG B 175 ? ARG B 1711 . ? 1_555 ? 17 AC4 7 TRP B 248 ? TRP B 1784 . ? 1_555 ? 18 AC4 7 ASN B 275 ? ASN B 1811 . ? 1_555 ? 19 AC4 7 GLU B 296 ? GLU B 1832 . ? 1_555 ? 20 AC5 2 MET B 185 ? MET B 1721 . ? 1_555 ? 21 AC5 2 ASN B 433 ? ASN B 1969 . ? 1_555 ? 22 AC6 3 HIS B 266 ? HIS B 1802 . ? 1_555 ? 23 AC6 3 HIS B 268 ? HIS B 1804 . ? 1_555 ? 24 AC6 3 ASP B 308 ? ASP B 1844 . ? 1_555 ? 25 AC7 4 LYS A 93 ? LYS A 93 . ? 1_555 ? 26 AC7 4 GLU A 108 ? GLU A 108 . ? 1_555 ? 27 AC7 4 ASP A 111 ? ASP A 111 . ? 1_555 ? 28 AC7 4 ASP A 112 ? ASP A 112 . ? 1_555 ? # _database_PDB_matrix.entry_id 1SDD _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 1SDD _atom_sites.fract_transf_matrix[1][1] 0.015780 _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] 0.011553 _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] 0.004363 _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 CA CU N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . ALA A 1 1 ? 24.117 17.336 55.626 1.00 102.41 ? 1 ALA A N 1 ATOM 2 C CA . ALA A 1 1 ? 23.148 17.448 54.497 1.00 102.53 ? 1 ALA A CA 1 ATOM 3 C C . ALA A 1 1 ? 21.721 17.214 54.989 1.00 102.47 ? 1 ALA A C 1 ATOM 4 O O . ALA A 1 1 ? 20.996 16.379 54.444 1.00 102.83 ? 1 ALA A O 1 ATOM 5 C CB . ALA A 1 1 ? 23.501 16.437 53.407 1.00 101.75 ? 1 ALA A CB 1 ATOM 6 N N . LYS A 1 2 ? 21.322 17.957 56.018 1.00 101.83 ? 2 LYS A N 1 ATOM 7 C CA . LYS A 1 2 ? 19.983 17.817 56.582 1.00 101.15 ? 2 LYS A CA 1 ATOM 8 C C . LYS A 1 2 ? 18.855 18.139 55.608 1.00 99.52 ? 2 LYS A C 1 ATOM 9 O O . LYS A 1 2 ? 19.076 18.355 54.416 1.00 99.56 ? 2 LYS A O 1 ATOM 10 C CB . LYS A 1 2 ? 19.828 18.698 57.827 1.00 102.44 ? 2 LYS A CB 1 ATOM 11 C CG . LYS A 1 2 ? 20.220 18.019 59.130 1.00 103.95 ? 2 LYS A CG 1 ATOM 12 C CD . LYS A 1 2 ? 19.832 18.872 60.329 1.00 104.81 ? 2 LYS A CD 1 ATOM 13 C CE . LYS A 1 2 ? 20.213 18.199 61.640 1.00 104.47 ? 2 LYS A CE 1 ATOM 14 N NZ . LYS A 1 2 ? 19.847 19.049 62.806 1.00 104.19 ? 2 LYS A NZ 1 ATOM 15 N N . LEU A 1 3 ? 17.639 18.161 56.146 1.00 96.86 ? 3 LEU A N 1 ATOM 16 C CA . LEU A 1 3 ? 16.440 18.464 55.381 1.00 93.64 ? 3 LEU A CA 1 ATOM 17 C C . LEU A 1 3 ? 15.702 19.571 56.121 1.00 92.33 ? 3 LEU A C 1 ATOM 18 O O . LEU A 1 3 ? 15.554 19.516 57.336 1.00 92.06 ? 3 LEU A O 1 ATOM 19 C CB . LEU A 1 3 ? 15.563 17.214 55.272 1.00 91.71 ? 3 LEU A CB 1 ATOM 20 C CG . LEU A 1 3 ? 14.204 17.309 54.569 1.00 90.75 ? 3 LEU A CG 1 ATOM 21 C CD1 . LEU A 1 3 ? 13.707 15.911 54.246 1.00 89.74 ? 3 LEU A CD1 1 ATOM 22 C CD2 . LEU A 1 3 ? 13.203 18.042 55.445 1.00 89.38 ? 3 LEU A CD2 1 ATOM 23 N N . ARG A 1 4 ? 15.253 20.584 55.391 1.00 91.92 ? 4 ARG A N 1 ATOM 24 C CA . ARG A 1 4 ? 14.533 21.687 56.009 1.00 93.01 ? 4 ARG A CA 1 ATOM 25 C C . ARG A 1 4 ? 13.035 21.560 55.765 1.00 93.39 ? 4 ARG A C 1 ATOM 26 O O . ARG A 1 4 ? 12.605 21.009 54.750 1.00 93.84 ? 4 ARG A O 1 ATOM 27 C CB . ARG A 1 4 ? 15.030 23.026 55.462 1.00 93.18 ? 4 ARG A CB 1 ATOM 28 C CG . ARG A 1 4 ? 16.535 23.224 55.570 1.00 94.88 ? 4 ARG A CG 1 ATOM 29 C CD . ARG A 1 4 ? 17.071 22.792 56.927 1.00 95.56 ? 4 ARG A CD 1 ATOM 30 N NE . ARG A 1 4 ? 18.433 23.261 57.156 1.00 95.30 ? 4 ARG A NE 1 ATOM 31 C CZ . ARG A 1 4 ? 18.746 24.508 57.484 1.00 95.58 ? 4 ARG A CZ 1 ATOM 32 N NH1 . ARG A 1 4 ? 17.791 25.420 57.626 1.00 95.33 ? 4 ARG A NH1 1 ATOM 33 N NH2 . ARG A 1 4 ? 20.014 24.844 57.672 1.00 96.02 ? 4 ARG A NH2 1 ATOM 34 N N . GLN A 1 5 ? 12.241 22.070 56.701 1.00 92.65 ? 5 GLN A N 1 ATOM 35 C CA . GLN A 1 5 ? 10.793 21.998 56.571 1.00 91.45 ? 5 GLN A CA 1 ATOM 36 C C . GLN A 1 5 ? 10.161 23.351 56.845 1.00 91.28 ? 5 GLN A C 1 ATOM 37 O O . GLN A 1 5 ? 10.688 24.153 57.620 1.00 91.11 ? 5 GLN A O 1 ATOM 38 C CB . GLN A 1 5 ? 10.221 20.972 57.547 1.00 90.35 ? 5 GLN A CB 1 ATOM 39 C CG . GLN A 1 5 ? 9.011 20.231 57.015 1.00 89.21 ? 5 GLN A CG 1 ATOM 40 C CD . GLN A 1 5 ? 9.362 18.849 56.495 1.00 88.52 ? 5 GLN A CD 1 ATOM 41 O OE1 . GLN A 1 5 ? 8.536 18.175 55.881 1.00 89.16 ? 5 GLN A OE1 1 ATOM 42 N NE2 . GLN A 1 5 ? 10.591 18.416 56.750 1.00 86.95 ? 5 GLN A NE2 1 ATOM 43 N N . PHE A 1 6 ? 9.033 23.605 56.194 1.00 90.24 ? 6 PHE A N 1 ATOM 44 C CA . PHE A 1 6 ? 8.305 24.856 56.365 1.00 88.57 ? 6 PHE A CA 1 ATOM 45 C C . PHE A 1 6 ? 6.868 24.555 55.986 1.00 87.51 ? 6 PHE A C 1 ATOM 46 O O . PHE A 1 6 ? 6.613 23.680 55.155 1.00 86.62 ? 6 PHE A O 1 ATOM 47 C CB . PHE A 1 6 ? 8.879 25.942 55.450 1.00 88.10 ? 6 PHE A CB 1 ATOM 48 C CG . PHE A 1 6 ? 10.355 26.128 55.601 1.00 87.87 ? 6 PHE A CG 1 ATOM 49 C CD1 . PHE A 1 6 ? 10.865 26.988 56.560 1.00 88.21 ? 6 PHE A CD1 1 ATOM 50 C CD2 . PHE A 1 6 ? 11.242 25.375 54.835 1.00 87.73 ? 6 PHE A CD2 1 ATOM 51 C CE1 . PHE A 1 6 ? 12.239 27.095 56.759 1.00 88.74 ? 6 PHE A CE1 1 ATOM 52 C CE2 . PHE A 1 6 ? 12.614 25.473 55.026 1.00 87.18 ? 6 PHE A CE2 1 ATOM 53 C CZ . PHE A 1 6 ? 13.114 26.334 55.990 1.00 88.01 ? 6 PHE A CZ 1 ATOM 54 N N . TYR A 1 7 ? 5.933 25.262 56.611 1.00 85.87 ? 7 TYR A N 1 ATOM 55 C CA . TYR A 1 7 ? 4.525 25.057 56.319 1.00 84.20 ? 7 TYR A CA 1 ATOM 56 C C . TYR A 1 7 ? 3.806 26.381 56.105 1.00 84.69 ? 7 TYR A C 1 ATOM 57 O O . TYR A 1 7 ? 2.647 26.534 56.490 1.00 86.28 ? 7 TYR A O 1 ATOM 58 C CB . TYR A 1 7 ? 3.852 24.268 57.448 1.00 81.10 ? 7 TYR A CB 1 ATOM 59 C CG . TYR A 1 7 ? 4.345 22.838 57.583 1.00 78.11 ? 7 TYR A CG 1 ATOM 60 C CD1 . TYR A 1 7 ? 5.546 22.547 58.235 1.00 77.36 ? 7 TYR A CD1 1 ATOM 61 C CD2 . TYR A 1 7 ? 3.620 21.776 57.038 1.00 75.55 ? 7 TYR A CD2 1 ATOM 62 C CE1 . TYR A 1 7 ? 6.009 21.235 58.340 1.00 75.20 ? 7 TYR A CE1 1 ATOM 63 C CE2 . TYR A 1 7 ? 4.075 20.467 57.133 1.00 73.75 ? 7 TYR A CE2 1 ATOM 64 C CZ . TYR A 1 7 ? 5.268 20.202 57.785 1.00 74.34 ? 7 TYR A CZ 1 ATOM 65 O OH . TYR A 1 7 ? 5.723 18.906 57.878 1.00 74.47 ? 7 TYR A OH 1 ATOM 66 N N . VAL A 1 8 ? 4.498 27.331 55.478 1.00 83.31 ? 8 VAL A N 1 ATOM 67 C CA . VAL A 1 8 ? 3.936 28.648 55.200 1.00 81.43 ? 8 VAL A CA 1 ATOM 68 C C . VAL A 1 8 ? 2.660 28.555 54.369 1.00 80.64 ? 8 VAL A C 1 ATOM 69 O O . VAL A 1 8 ? 2.507 27.649 53.549 1.00 79.31 ? 8 VAL A O 1 ATOM 70 C CB . VAL A 1 8 ? 4.968 29.527 54.475 1.00 81.00 ? 8 VAL A CB 1 ATOM 71 C CG1 . VAL A 1 8 ? 5.636 28.724 53.400 1.00 83.46 ? 8 VAL A CG1 1 ATOM 72 C CG2 . VAL A 1 8 ? 4.301 30.763 53.880 1.00 81.67 ? 8 VAL A CG2 1 ATOM 73 N N . ALA A 1 9 ? 1.747 29.499 54.593 1.00 80.75 ? 9 ALA A N 1 ATOM 74 C CA . ALA A 1 9 ? 0.471 29.529 53.887 1.00 81.32 ? 9 ALA A CA 1 ATOM 75 C C . ALA A 1 9 ? 0.071 30.937 53.479 1.00 82.22 ? 9 ALA A C 1 ATOM 76 O O . ALA A 1 9 ? 0.641 31.918 53.950 1.00 82.82 ? 9 ALA A O 1 ATOM 77 C CB . ALA A 1 9 ? -0.607 28.931 54.760 1.00 82.60 ? 9 ALA A CB 1 ATOM 78 N N . ALA A 1 10 ? -0.921 31.027 52.601 1.00 83.80 ? 10 ALA A N 1 ATOM 79 C CA . ALA A 1 10 ? -1.413 32.312 52.119 1.00 85.64 ? 10 ALA A CA 1 ATOM 80 C C . ALA A 1 10 ? -2.763 32.601 52.759 1.00 87.45 ? 10 ALA A C 1 ATOM 81 O O . ALA A 1 10 ? -3.612 31.716 52.856 1.00 86.40 ? 10 ALA A O 1 ATOM 82 C CB . ALA A 1 10 ? -1.547 32.287 50.599 1.00 84.97 ? 10 ALA A CB 1 ATOM 83 N N . GLN A 1 11 ? -2.959 33.844 53.191 1.00 89.86 ? 11 GLN A N 1 ATOM 84 C CA . GLN A 1 11 ? -4.206 34.245 53.835 1.00 91.33 ? 11 GLN A CA 1 ATOM 85 C C . GLN A 1 11 ? -4.412 35.753 53.805 1.00 92.08 ? 11 GLN A C 1 ATOM 86 O O . GLN A 1 11 ? -3.454 36.522 53.881 1.00 92.15 ? 11 GLN A O 1 ATOM 87 C CB . GLN A 1 11 ? -4.217 33.782 55.290 1.00 91.43 ? 11 GLN A CB 1 ATOM 88 C CG . GLN A 1 11 ? -2.981 34.200 56.073 1.00 91.31 ? 11 GLN A CG 1 ATOM 89 C CD . GLN A 1 11 ? -3.219 34.215 57.567 1.00 91.98 ? 11 GLN A CD 1 ATOM 90 O OE1 . GLN A 1 11 ? -3.801 35.162 58.100 1.00 92.38 ? 11 GLN A OE1 1 ATOM 91 N NE2 . GLN A 1 11 ? -2.784 33.159 58.253 1.00 90.53 ? 11 GLN A NE2 1 ATOM 92 N N . SER A 1 12 ? -5.671 36.168 53.705 1.00 93.08 ? 12 SER A N 1 ATOM 93 C CA . SER A 1 12 ? -6.004 37.585 53.679 1.00 93.83 ? 12 SER A CA 1 ATOM 94 C C . SER A 1 12 ? -6.046 38.108 55.103 1.00 93.22 ? 12 SER A C 1 ATOM 95 O O . SER A 1 12 ? -6.459 37.400 56.019 1.00 93.58 ? 12 SER A O 1 ATOM 96 C CB . SER A 1 12 ? -7.363 37.808 53.011 1.00 94.97 ? 12 SER A CB 1 ATOM 97 O OG . SER A 1 12 ? -8.380 37.075 53.671 1.00 97.95 ? 12 SER A OG 1 ATOM 98 N N . ILE A 1 13 ? -5.600 39.344 55.285 1.00 92.80 ? 13 ILE A N 1 ATOM 99 C CA . ILE A 1 13 ? -5.593 39.967 56.596 1.00 92.69 ? 13 ILE A CA 1 ATOM 100 C C . ILE A 1 13 ? -5.684 41.477 56.453 1.00 93.17 ? 13 ILE A C 1 ATOM 101 O O . ILE A 1 13 ? -4.980 42.077 55.644 1.00 92.09 ? 13 ILE A O 1 ATOM 102 C CB . ILE A 1 13 ? -4.306 39.642 57.392 1.00 92.22 ? 13 ILE A CB 1 ATOM 103 C CG1 . ILE A 1 13 ? -3.087 40.219 56.671 1.00 92.70 ? 13 ILE A CG1 1 ATOM 104 C CG2 . ILE A 1 13 ? -4.170 38.142 57.587 1.00 91.51 ? 13 ILE A CG2 1 ATOM 105 C CD1 . ILE A 1 13 ? -1.845 40.292 57.533 1.00 94.36 ? 13 ILE A CD1 1 ATOM 106 N N . ARG A 1 14 ? -6.561 42.090 57.240 1.00 94.72 ? 14 ARG A N 1 ATOM 107 C CA . ARG A 1 14 ? -6.720 43.538 57.207 1.00 95.50 ? 14 ARG A CA 1 ATOM 108 C C . ARG A 1 14 ? -5.312 44.087 57.455 1.00 94.68 ? 14 ARG A C 1 ATOM 109 O O . ARG A 1 14 ? -4.441 43.345 57.916 1.00 94.71 ? 14 ARG A O 1 ATOM 110 C CB . ARG A 1 14 ? -7.675 43.980 58.326 1.00 96.81 ? 14 ARG A CB 1 ATOM 111 C CG . ARG A 1 14 ? -8.304 45.355 58.127 1.00 98.89 ? 14 ARG A CG 1 ATOM 112 C CD . ARG A 1 14 ? -9.387 45.335 57.043 1.00 101.06 ? 14 ARG A CD 1 ATOM 113 N NE . ARG A 1 14 ? -10.557 44.539 57.426 1.00 101.63 ? 14 ARG A NE 1 ATOM 114 C CZ . ARG A 1 14 ? -11.665 44.435 56.697 1.00 100.74 ? 14 ARG A CZ 1 ATOM 115 N NH1 . ARG A 1 14 ? -11.759 45.074 55.538 1.00 99.62 ? 14 ARG A NH1 1 ATOM 116 N NH2 . ARG A 1 14 ? -12.681 43.699 57.130 1.00 99.96 ? 14 ARG A NH2 1 ATOM 117 N N . TRP A 1 15 ? -5.066 45.358 57.144 1.00 92.36 ? 15 TRP A N 1 ATOM 118 C CA . TRP A 1 15 ? -3.732 45.898 57.384 1.00 89.98 ? 15 TRP A CA 1 ATOM 119 C C . TRP A 1 15 ? -3.611 47.423 57.347 1.00 89.65 ? 15 TRP A C 1 ATOM 120 O O . TRP A 1 15 ? -4.130 48.087 56.445 1.00 88.49 ? 15 TRP A O 1 ATOM 121 C CB . TRP A 1 15 ? -2.721 45.284 56.397 1.00 88.52 ? 15 TRP A CB 1 ATOM 122 C CG . TRP A 1 15 ? -1.315 45.226 56.955 1.00 86.06 ? 15 TRP A CG 1 ATOM 123 C CD1 . TRP A 1 15 ? -0.809 44.282 57.811 1.00 85.08 ? 15 TRP A CD1 1 ATOM 124 C CD2 . TRP A 1 15 ? -0.285 46.211 56.794 1.00 84.22 ? 15 TRP A CD2 1 ATOM 125 N NE1 . TRP A 1 15 ? 0.464 44.625 58.200 1.00 83.06 ? 15 TRP A NE1 1 ATOM 126 C CE2 . TRP A 1 15 ? 0.811 45.803 57.592 1.00 82.97 ? 15 TRP A CE2 1 ATOM 127 C CE3 . TRP A 1 15 ? -0.184 47.402 56.059 1.00 83.01 ? 15 TRP A CE3 1 ATOM 128 C CZ2 . TRP A 1 15 ? 1.992 46.542 57.677 1.00 81.84 ? 15 TRP A CZ2 1 ATOM 129 C CZ3 . TRP A 1 15 ? 0.991 48.139 56.145 1.00 82.25 ? 15 TRP A CZ3 1 ATOM 130 C CH2 . TRP A 1 15 ? 2.063 47.702 56.952 1.00 83.02 ? 15 TRP A CH2 1 ATOM 131 N N . ASN A 1 16 ? -2.908 47.955 58.346 1.00 89.34 ? 16 ASN A N 1 ATOM 132 C CA . ASN A 1 16 ? -2.655 49.386 58.478 1.00 89.70 ? 16 ASN A CA 1 ATOM 133 C C . ASN A 1 16 ? -2.276 50.006 57.137 1.00 89.80 ? 16 ASN A C 1 ATOM 134 O O . ASN A 1 16 ? -2.055 51.213 57.038 1.00 89.90 ? 16 ASN A O 1 ATOM 135 C CB . ASN A 1 16 ? -1.528 49.612 59.493 1.00 89.85 ? 16 ASN A CB 1 ATOM 136 C CG . ASN A 1 16 ? -0.922 51.000 59.398 1.00 89.38 ? 16 ASN A CG 1 ATOM 137 O OD1 . ASN A 1 16 ? -1.626 52.007 59.479 1.00 87.99 ? 16 ASN A OD1 1 ATOM 138 N ND2 . ASN A 1 16 ? 0.396 51.057 59.230 1.00 89.33 ? 16 ASN A ND2 1 ATOM 139 N N . THR A 1 31 ? -5.452 54.281 56.606 1.00 93.79 ? 31 THR A N 1 ATOM 140 C CA . THR A 1 31 ? -6.331 53.315 57.256 1.00 94.49 ? 31 THR A CA 1 ATOM 141 C C . THR A 1 31 ? -5.991 51.876 56.872 1.00 95.07 ? 31 THR A C 1 ATOM 142 O O . THR A 1 31 ? -4.845 51.565 56.534 1.00 95.72 ? 31 THR A O 1 ATOM 143 C CB . THR A 1 31 ? -7.820 53.576 56.912 1.00 94.31 ? 31 THR A CB 1 ATOM 144 O OG1 . THR A 1 31 ? -7.953 53.812 55.503 1.00 93.00 ? 31 THR A OG1 1 ATOM 145 C CG2 . THR A 1 31 ? -8.361 54.764 57.712 1.00 93.21 ? 31 THR A CG2 1 ATOM 146 N N . SER A 1 32 ? -6.995 51.003 56.922 1.00 94.81 ? 32 SER A N 1 ATOM 147 C CA . SER A 1 32 ? -6.805 49.593 56.602 1.00 93.66 ? 32 SER A CA 1 ATOM 148 C C . SER A 1 32 ? -7.400 49.168 55.259 1.00 92.05 ? 32 SER A C 1 ATOM 149 O O . SER A 1 32 ? -8.275 49.835 54.697 1.00 91.11 ? 32 SER A O 1 ATOM 150 C CB . SER A 1 32 ? -7.390 48.711 57.721 1.00 94.60 ? 32 SER A CB 1 ATOM 151 O OG . SER A 1 32 ? -6.735 48.929 58.966 1.00 92.82 ? 32 SER A OG 1 ATOM 152 N N . PHE A 1 33 ? -6.902 48.037 54.766 1.00 90.45 ? 33 PHE A N 1 ATOM 153 C CA . PHE A 1 33 ? -7.331 47.449 53.503 1.00 87.55 ? 33 PHE A CA 1 ATOM 154 C C . PHE A 1 33 ? -7.327 45.934 53.652 1.00 87.80 ? 33 PHE A C 1 ATOM 155 O O . PHE A 1 33 ? -6.711 45.398 54.578 1.00 87.35 ? 33 PHE A O 1 ATOM 156 C CB . PHE A 1 33 ? -6.357 47.830 52.395 1.00 84.21 ? 33 PHE A CB 1 ATOM 157 C CG . PHE A 1 33 ? -6.511 49.235 51.900 1.00 81.29 ? 33 PHE A CG 1 ATOM 158 C CD1 . PHE A 1 33 ? -7.637 49.609 51.173 1.00 80.65 ? 33 PHE A CD1 1 ATOM 159 C CD2 . PHE A 1 33 ? -5.511 50.175 52.115 1.00 79.18 ? 33 PHE A CD2 1 ATOM 160 C CE1 . PHE A 1 33 ? -7.760 50.902 50.660 1.00 80.05 ? 33 PHE A CE1 1 ATOM 161 C CE2 . PHE A 1 33 ? -5.625 51.470 51.606 1.00 79.13 ? 33 PHE A CE2 1 ATOM 162 C CZ . PHE A 1 33 ? -6.750 51.833 50.877 1.00 78.39 ? 33 PHE A CZ 1 ATOM 163 N N . LYS A 1 34 ? -8.018 45.244 52.751 1.00 87.82 ? 34 LYS A N 1 ATOM 164 C CA . LYS A 1 34 ? -8.043 43.784 52.782 1.00 88.55 ? 34 LYS A CA 1 ATOM 165 C C . LYS A 1 34 ? -6.853 43.331 51.931 1.00 87.08 ? 34 LYS A C 1 ATOM 166 O O . LYS A 1 34 ? -6.846 43.518 50.709 1.00 88.68 ? 34 LYS A O 1 ATOM 167 C CB . LYS A 1 34 ? -9.358 43.255 52.195 1.00 91.75 ? 34 LYS A CB 1 ATOM 168 C CG . LYS A 1 34 ? -9.467 41.725 52.160 1.00 96.96 ? 34 LYS A CG 1 ATOM 169 C CD . LYS A 1 34 ? -10.660 41.197 52.967 1.00 100.62 ? 34 LYS A CD 1 ATOM 170 C CE . LYS A 1 34 ? -10.518 41.490 54.467 1.00 102.57 ? 34 LYS A CE 1 ATOM 171 N NZ . LYS A 1 34 ? -11.668 40.972 55.278 1.00 103.18 ? 34 LYS A NZ 1 ATOM 172 N N . LYS A 1 35 ? -5.844 42.746 52.575 1.00 83.95 ? 35 LYS A N 1 ATOM 173 C CA . LYS A 1 35 ? -4.645 42.313 51.864 1.00 80.35 ? 35 LYS A CA 1 ATOM 174 C C . LYS A 1 35 ? -4.265 40.851 52.118 1.00 78.25 ? 35 LYS A C 1 ATOM 175 O O . LYS A 1 35 ? -4.805 40.205 53.014 1.00 77.51 ? 35 LYS A O 1 ATOM 176 C CB . LYS A 1 35 ? -3.495 43.258 52.231 1.00 80.00 ? 35 LYS A CB 1 ATOM 177 C CG . LYS A 1 35 ? -3.916 44.731 52.134 1.00 79.84 ? 35 LYS A CG 1 ATOM 178 C CD . LYS A 1 35 ? -2.787 45.732 52.346 1.00 79.28 ? 35 LYS A CD 1 ATOM 179 C CE . LYS A 1 35 ? -1.814 45.781 51.171 1.00 77.91 ? 35 LYS A CE 1 ATOM 180 N NZ . LYS A 1 35 ? -0.916 46.977 51.284 1.00 75.95 ? 35 LYS A NZ 1 ATOM 181 N N . ILE A 1 36 ? -3.349 40.330 51.308 1.00 76.02 ? 36 ILE A N 1 ATOM 182 C CA . ILE A 1 36 ? -2.905 38.946 51.426 1.00 73.32 ? 36 ILE A CA 1 ATOM 183 C C . ILE A 1 36 ? -1.429 38.906 51.804 1.00 72.86 ? 36 ILE A C 1 ATOM 184 O O . ILE A 1 36 ? -0.645 39.725 51.344 1.00 72.71 ? 36 ILE A O 1 ATOM 185 C CB . ILE A 1 36 ? -3.050 38.197 50.091 1.00 72.79 ? 36 ILE A CB 1 ATOM 186 C CG1 . ILE A 1 36 ? -4.385 38.543 49.415 1.00 72.88 ? 36 ILE A CG1 1 ATOM 187 C CG2 . ILE A 1 36 ? -2.909 36.698 50.332 1.00 72.25 ? 36 ILE A CG2 1 ATOM 188 C CD1 . ILE A 1 36 ? -5.597 37.824 49.963 1.00 74.63 ? 36 ILE A CD1 1 ATOM 189 N N . VAL A 1 37 ? -1.045 37.945 52.630 1.00 72.48 ? 37 VAL A N 1 ATOM 190 C CA . VAL A 1 37 ? 0.343 37.825 53.037 1.00 73.98 ? 37 VAL A CA 1 ATOM 191 C C . VAL A 1 37 ? 0.671 36.363 53.291 1.00 76.65 ? 37 VAL A C 1 ATOM 192 O O . VAL A 1 37 ? -0.225 35.549 53.508 1.00 76.78 ? 37 VAL A O 1 ATOM 193 C CB . VAL A 1 37 ? 0.623 38.626 54.325 1.00 73.86 ? 37 VAL A CB 1 ATOM 194 C CG1 . VAL A 1 37 ? 2.048 38.402 54.768 1.00 74.78 ? 37 VAL A CG1 1 ATOM 195 C CG2 . VAL A 1 37 ? 0.383 40.104 54.089 1.00 72.49 ? 37 VAL A CG2 1 ATOM 196 N N . TYR A 1 38 ? 1.954 36.023 53.235 1.00 80.04 ? 38 TYR A N 1 ATOM 197 C CA . TYR A 1 38 ? 2.379 34.650 53.489 1.00 83.26 ? 38 TYR A CA 1 ATOM 198 C C . TYR A 1 38 ? 2.647 34.540 54.984 1.00 84.52 ? 38 TYR A C 1 ATOM 199 O O . TYR A 1 38 ? 3.269 35.432 55.570 1.00 85.46 ? 38 TYR A O 1 ATOM 200 C CB . TYR A 1 38 ? 3.675 34.312 52.735 1.00 85.12 ? 38 TYR A CB 1 ATOM 201 C CG . TYR A 1 38 ? 3.566 34.181 51.226 1.00 87.02 ? 38 TYR A CG 1 ATOM 202 C CD1 . TYR A 1 38 ? 3.736 35.287 50.389 1.00 87.18 ? 38 TYR A CD1 1 ATOM 203 C CD2 . TYR A 1 38 ? 3.340 32.939 50.634 1.00 88.38 ? 38 TYR A CD2 1 ATOM 204 C CE1 . TYR A 1 38 ? 3.692 35.154 49.004 1.00 87.99 ? 38 TYR A CE1 1 ATOM 205 C CE2 . TYR A 1 38 ? 3.291 32.796 49.253 1.00 88.76 ? 38 TYR A CE2 1 ATOM 206 C CZ . TYR A 1 38 ? 3.470 33.903 48.445 1.00 89.02 ? 38 TYR A CZ 1 ATOM 207 O OH . TYR A 1 38 ? 3.433 33.746 47.080 1.00 89.20 ? 38 TYR A OH 1 ATOM 208 N N . ARG A 1 39 ? 2.181 33.460 55.608 1.00 84.84 ? 39 ARG A N 1 ATOM 209 C CA . ARG A 1 39 ? 2.406 33.277 57.041 1.00 85.01 ? 39 ARG A CA 1 ATOM 210 C C . ARG A 1 39 ? 3.023 31.914 57.334 1.00 84.21 ? 39 ARG A C 1 ATOM 211 O O . ARG A 1 39 ? 2.616 30.896 56.772 1.00 82.37 ? 39 ARG A O 1 ATOM 212 C CB . ARG A 1 39 ? 1.101 33.437 57.831 1.00 84.86 ? 39 ARG A CB 1 ATOM 213 C CG . ARG A 1 39 ? 0.250 34.661 57.470 1.00 84.64 ? 39 ARG A CG 1 ATOM 214 C CD . ARG A 1 39 ? 1.038 35.968 57.259 1.00 85.94 ? 39 ARG A CD 1 ATOM 215 N NE . ARG A 1 39 ? 1.978 36.302 58.330 1.00 86.08 ? 39 ARG A NE 1 ATOM 216 C CZ . ARG A 1 39 ? 2.543 37.500 58.477 1.00 85.28 ? 39 ARG A CZ 1 ATOM 217 N NH1 . ARG A 1 39 ? 2.261 38.479 57.631 1.00 81.67 ? 39 ARG A NH1 1 ATOM 218 N NH2 . ARG A 1 39 ? 3.397 37.719 59.467 1.00 87.47 ? 39 ARG A NH2 1 ATOM 219 N N . GLU A 1 40 ? 4.001 31.919 58.232 1.00 84.69 ? 40 GLU A N 1 ATOM 220 C CA . GLU A 1 40 ? 4.740 30.728 58.629 1.00 86.61 ? 40 GLU A CA 1 ATOM 221 C C . GLU A 1 40 ? 3.983 29.431 58.921 1.00 89.12 ? 40 GLU A C 1 ATOM 222 O O . GLU A 1 40 ? 4.182 28.436 58.223 1.00 89.11 ? 40 GLU A O 1 ATOM 223 C CB . GLU A 1 40 ? 5.628 31.066 59.825 1.00 85.85 ? 40 GLU A CB 1 ATOM 224 C CG . GLU A 1 40 ? 6.981 31.632 59.440 1.00 84.08 ? 40 GLU A CG 1 ATOM 225 C CD . GLU A 1 40 ? 8.126 30.709 59.832 1.00 83.85 ? 40 GLU A CD 1 ATOM 226 O OE1 . GLU A 1 40 ? 8.005 29.479 59.605 1.00 81.37 ? 40 GLU A OE1 1 ATOM 227 O OE2 . GLU A 1 40 ? 9.144 31.218 60.358 1.00 82.21 ? 40 GLU A OE2 1 ATOM 228 N N . TYR A 1 41 ? 3.135 29.432 59.951 1.00 91.51 ? 41 TYR A N 1 ATOM 229 C CA . TYR A 1 41 ? 2.389 28.229 60.338 1.00 94.11 ? 41 TYR A CA 1 ATOM 230 C C . TYR A 1 41 ? 3.363 27.113 60.705 1.00 95.64 ? 41 TYR A C 1 ATOM 231 O O . TYR A 1 41 ? 4.514 27.127 60.274 1.00 96.85 ? 41 TYR A O 1 ATOM 232 C CB . TYR A 1 41 ? 1.467 27.769 59.208 1.00 94.56 ? 41 TYR A CB 1 ATOM 233 C CG . TYR A 1 41 ? 0.169 28.534 59.142 1.00 94.99 ? 41 TYR A CG 1 ATOM 234 C CD1 . TYR A 1 41 ? -1.028 27.962 59.586 1.00 94.88 ? 41 TYR A CD1 1 ATOM 235 C CD2 . TYR A 1 41 ? 0.140 29.846 58.664 1.00 96.40 ? 41 TYR A CD2 1 ATOM 236 C CE1 . TYR A 1 41 ? -2.227 28.685 59.554 1.00 95.89 ? 41 TYR A CE1 1 ATOM 237 C CE2 . TYR A 1 41 ? -1.048 30.579 58.629 1.00 96.93 ? 41 TYR A CE2 1 ATOM 238 C CZ . TYR A 1 41 ? -2.227 29.995 59.074 1.00 96.28 ? 41 TYR A CZ 1 ATOM 239 O OH . TYR A 1 41 ? -3.390 30.729 59.031 1.00 94.92 ? 41 TYR A OH 1 ATOM 240 N N . GLU A 1 42 ? 2.908 26.142 61.491 1.00 97.27 ? 42 GLU A N 1 ATOM 241 C CA . GLU A 1 42 ? 3.789 25.059 61.920 1.00 98.91 ? 42 GLU A CA 1 ATOM 242 C C . GLU A 1 42 ? 3.180 23.672 61.772 1.00 98.77 ? 42 GLU A C 1 ATOM 243 O O . GLU A 1 42 ? 2.107 23.509 61.196 1.00 97.93 ? 42 GLU A O 1 ATOM 244 C CB . GLU A 1 42 ? 4.185 25.270 63.383 1.00 101.58 ? 42 GLU A CB 1 ATOM 245 C CG . GLU A 1 42 ? 4.507 26.718 63.745 1.00 105.02 ? 42 GLU A CG 1 ATOM 246 C CD . GLU A 1 42 ? 4.791 26.900 65.230 1.00 106.62 ? 42 GLU A CD 1 ATOM 247 O OE1 . GLU A 1 42 ? 5.835 26.401 65.705 1.00 106.90 ? 42 GLU A OE1 1 ATOM 248 O OE2 . GLU A 1 42 ? 3.966 27.538 65.922 1.00 107.78 ? 42 GLU A OE2 1 ATOM 249 N N . ALA A 1 43 ? 3.890 22.680 62.309 1.00 99.76 ? 43 ALA A N 1 ATOM 250 C CA . ALA A 1 43 ? 3.471 21.278 62.285 1.00 101.31 ? 43 ALA A CA 1 ATOM 251 C C . ALA A 1 43 ? 2.675 20.908 61.040 1.00 101.97 ? 43 ALA A C 1 ATOM 252 O O . ALA A 1 43 ? 3.240 20.764 59.963 1.00 103.15 ? 43 ALA A O 1 ATOM 253 C CB . ALA A 1 43 ? 2.659 20.952 63.545 1.00 102.14 ? 43 ALA A CB 1 ATOM 254 N N . TYR A 1 44 ? 1.364 20.740 61.197 1.00 102.67 ? 44 TYR A N 1 ATOM 255 C CA . TYR A 1 44 ? 0.489 20.394 60.077 1.00 102.70 ? 44 TYR A CA 1 ATOM 256 C C . TYR A 1 44 ? -0.536 21.509 59.869 1.00 103.47 ? 44 TYR A C 1 ATOM 257 O O . TYR A 1 44 ? -1.688 21.250 59.513 1.00 102.79 ? 44 TYR A O 1 ATOM 258 C CB . TYR A 1 44 ? -0.232 19.066 60.344 1.00 101.18 ? 44 TYR A CB 1 ATOM 259 C CG . TYR A 1 44 ? 0.676 17.854 60.442 1.00 100.33 ? 44 TYR A CG 1 ATOM 260 C CD1 . TYR A 1 44 ? 1.658 17.764 61.432 1.00 99.31 ? 44 TYR A CD1 1 ATOM 261 C CD2 . TYR A 1 44 ? 0.540 16.787 59.551 1.00 100.03 ? 44 TYR A CD2 1 ATOM 262 C CE1 . TYR A 1 44 ? 2.482 16.638 61.527 1.00 99.07 ? 44 TYR A CE1 1 ATOM 263 C CE2 . TYR A 1 44 ? 1.355 15.660 59.638 1.00 98.91 ? 44 TYR A CE2 1 ATOM 264 C CZ . TYR A 1 44 ? 2.322 15.592 60.625 1.00 98.95 ? 44 TYR A CZ 1 ATOM 265 O OH . TYR A 1 44 ? 3.131 14.481 60.702 1.00 98.21 ? 44 TYR A OH 1 ATOM 266 N N . PHE A 1 45 ? -0.092 22.745 60.096 1.00 104.29 ? 45 PHE A N 1 ATOM 267 C CA . PHE A 1 45 ? -0.905 23.953 59.954 1.00 106.21 ? 45 PHE A CA 1 ATOM 268 C C . PHE A 1 45 ? -1.873 24.185 61.119 1.00 107.29 ? 45 PHE A C 1 ATOM 269 O O . PHE A 1 45 ? -3.059 24.434 60.905 1.00 107.10 ? 45 PHE A O 1 ATOM 270 C CB . PHE A 1 45 ? -1.690 23.937 58.632 1.00 107.52 ? 45 PHE A CB 1 ATOM 271 C CG . PHE A 1 45 ? -0.827 23.773 57.397 1.00 109.10 ? 45 PHE A CG 1 ATOM 272 C CD1 . PHE A 1 45 ? -0.467 22.504 56.937 1.00 109.17 ? 45 PHE A CD1 1 ATOM 273 C CD2 . PHE A 1 45 ? -0.378 24.889 56.690 1.00 108.95 ? 45 PHE A CD2 1 ATOM 274 C CE1 . PHE A 1 45 ? 0.325 22.348 55.795 1.00 108.22 ? 45 PHE A CE1 1 ATOM 275 C CE2 . PHE A 1 45 ? 0.415 24.741 55.547 1.00 109.01 ? 45 PHE A CE2 1 ATOM 276 C CZ . PHE A 1 45 ? 0.766 23.468 55.101 1.00 108.23 ? 45 PHE A CZ 1 ATOM 277 N N . GLN A 1 46 ? -1.360 24.108 62.347 1.00 109.36 ? 46 GLN A N 1 ATOM 278 C CA . GLN A 1 46 ? -2.169 24.323 63.555 1.00 110.98 ? 46 GLN A CA 1 ATOM 279 C C . GLN A 1 46 ? -2.322 25.810 63.873 1.00 112.12 ? 46 GLN A C 1 ATOM 280 O O . GLN A 1 46 ? -3.434 26.295 64.079 1.00 112.42 ? 46 GLN A O 1 ATOM 281 C CB . GLN A 1 46 ? -1.539 23.634 64.775 1.00 110.96 ? 46 GLN A CB 1 ATOM 282 C CG . GLN A 1 46 ? -2.001 22.206 65.064 1.00 110.36 ? 46 GLN A CG 1 ATOM 283 C CD . GLN A 1 46 ? -1.425 21.178 64.107 1.00 110.63 ? 46 GLN A CD 1 ATOM 284 O OE1 . GLN A 1 46 ? -1.882 21.039 62.972 1.00 110.64 ? 46 GLN A OE1 1 ATOM 285 N NE2 . GLN A 1 46 ? -0.409 20.452 64.564 1.00 110.26 ? 46 GLN A NE2 1 ATOM 286 N N . LYS A 1 47 ? -1.197 26.522 63.925 1.00 113.21 ? 47 LYS A N 1 ATOM 287 C CA . LYS A 1 47 ? -1.198 27.953 64.224 1.00 114.21 ? 47 LYS A CA 1 ATOM 288 C C . LYS A 1 47 ? 0.120 28.603 63.790 1.00 114.50 ? 47 LYS A C 1 ATOM 289 O O . LYS A 1 47 ? 1.116 27.915 63.564 1.00 113.68 ? 47 LYS A O 1 ATOM 290 C CB . LYS A 1 47 ? -1.402 28.176 65.726 1.00 114.97 ? 47 LYS A CB 1 ATOM 291 C CG . LYS A 1 47 ? -1.643 29.632 66.118 1.00 115.42 ? 47 LYS A CG 1 ATOM 292 C CD . LYS A 1 47 ? -1.193 29.918 67.551 1.00 116.23 ? 47 LYS A CD 1 ATOM 293 C CE . LYS A 1 47 ? -1.895 29.028 68.570 1.00 116.94 ? 47 LYS A CE 1 ATOM 294 N NZ . LYS A 1 47 ? -1.448 29.316 69.966 1.00 116.25 ? 47 LYS A NZ 1 ATOM 295 N N . GLU A 1 48 ? 0.117 29.930 63.684 1.00 115.34 ? 48 GLU A N 1 ATOM 296 C CA . GLU A 1 48 ? 1.303 30.679 63.281 1.00 116.85 ? 48 GLU A CA 1 ATOM 297 C C . GLU A 1 48 ? 1.903 31.425 64.465 1.00 117.50 ? 48 GLU A C 1 ATOM 298 O O . GLU A 1 48 ? 1.241 31.624 65.478 1.00 118.39 ? 48 GLU A O 1 ATOM 299 C CB . GLU A 1 48 ? 0.949 31.693 62.191 1.00 117.30 ? 48 GLU A CB 1 ATOM 300 C CG . GLU A 1 48 ? -0.033 32.770 62.647 1.00 118.41 ? 48 GLU A CG 1 ATOM 301 C CD . GLU A 1 48 ? 0.014 34.017 61.776 1.00 119.22 ? 48 GLU A CD 1 ATOM 302 O OE1 . GLU A 1 48 ? -0.761 34.965 62.032 1.00 118.76 ? 48 GLU A OE1 1 ATOM 303 O OE2 . GLU A 1 48 ? 0.835 34.053 60.836 1.00 120.79 ? 48 GLU A OE2 1 ATOM 304 N N . LYS A 1 49 ? 3.154 31.850 64.326 1.00 118.22 ? 49 LYS A N 1 ATOM 305 C CA . LYS A 1 49 ? 3.831 32.592 65.385 1.00 119.56 ? 49 LYS A CA 1 ATOM 306 C C . LYS A 1 49 ? 4.290 33.936 64.826 1.00 120.87 ? 49 LYS A C 1 ATOM 307 O O . LYS A 1 49 ? 5.490 34.180 64.703 1.00 121.04 ? 49 LYS A O 1 ATOM 308 C CB . LYS A 1 49 ? 5.056 31.822 65.876 1.00 119.25 ? 49 LYS A CB 1 ATOM 309 C CG . LYS A 1 49 ? 4.809 30.361 66.169 1.00 118.76 ? 49 LYS A CG 1 ATOM 310 C CD . LYS A 1 49 ? 6.123 29.640 66.430 1.00 119.09 ? 49 LYS A CD 1 ATOM 311 C CE . LYS A 1 49 ? 7.079 29.768 65.242 1.00 119.64 ? 49 LYS A CE 1 ATOM 312 N NZ . LYS A 1 49 ? 6.503 29.240 63.967 1.00 118.98 ? 49 LYS A NZ 1 ATOM 313 N N . PRO A 1 50 ? 3.339 34.827 64.488 1.00 121.98 ? 50 PRO A N 1 ATOM 314 C CA . PRO A 1 50 ? 3.614 36.160 63.933 1.00 122.63 ? 50 PRO A CA 1 ATOM 315 C C . PRO A 1 50 ? 4.867 36.868 64.458 1.00 123.06 ? 50 PRO A C 1 ATOM 316 O O . PRO A 1 50 ? 5.559 36.371 65.349 1.00 123.17 ? 50 PRO A O 1 ATOM 317 C CB . PRO A 1 50 ? 2.336 36.929 64.254 1.00 122.64 ? 50 PRO A CB 1 ATOM 318 C CG . PRO A 1 50 ? 1.288 35.881 64.071 1.00 122.41 ? 50 PRO A CG 1 ATOM 319 C CD . PRO A 1 50 ? 1.897 34.671 64.767 1.00 122.25 ? 50 PRO A CD 1 ATOM 320 N N . GLN A 1 51 ? 5.152 38.037 63.895 1.00 123.40 ? 51 GLN A N 1 ATOM 321 C CA . GLN A 1 51 ? 6.317 38.809 64.298 1.00 123.54 ? 51 GLN A CA 1 ATOM 322 C C . GLN A 1 51 ? 6.020 40.296 64.202 1.00 123.50 ? 51 GLN A C 1 ATOM 323 O O . GLN A 1 51 ? 6.262 40.920 63.174 1.00 122.71 ? 51 GLN A O 1 ATOM 324 C CB . GLN A 1 51 ? 7.503 38.468 63.403 1.00 124.20 ? 51 GLN A CB 1 ATOM 325 C CG . GLN A 1 51 ? 8.798 39.122 63.825 1.00 125.66 ? 51 GLN A CG 1 ATOM 326 C CD . GLN A 1 51 ? 9.835 39.094 62.722 1.00 127.17 ? 51 GLN A CD 1 ATOM 327 O OE1 . GLN A 1 51 ? 10.091 38.051 62.117 1.00 127.59 ? 51 GLN A OE1 1 ATOM 328 N NE2 . GLN A 1 51 ? 10.443 40.246 62.454 1.00 128.12 ? 51 GLN A NE2 1 ATOM 329 N N . SER A 1 52 ? 5.495 40.857 65.284 1.00 124.60 ? 52 SER A N 1 ATOM 330 C CA . SER A 1 52 ? 5.156 42.275 65.336 1.00 125.34 ? 52 SER A CA 1 ATOM 331 C C . SER A 1 52 ? 6.360 43.172 65.062 1.00 125.57 ? 52 SER A C 1 ATOM 332 O O . SER A 1 52 ? 6.244 44.174 64.354 1.00 125.79 ? 52 SER A O 1 ATOM 333 C CB . SER A 1 52 ? 4.563 42.624 66.706 1.00 125.42 ? 52 SER A CB 1 ATOM 334 O OG . SER A 1 52 ? 4.230 44.000 66.793 1.00 124.89 ? 52 SER A OG 1 ATOM 335 N N . ARG A 1 53 ? 7.513 42.815 65.622 1.00 125.26 ? 53 ARG A N 1 ATOM 336 C CA . ARG A 1 53 ? 8.718 43.614 65.432 1.00 124.77 ? 53 ARG A CA 1 ATOM 337 C C . ARG A 1 53 ? 9.104 43.749 63.956 1.00 123.97 ? 53 ARG A C 1 ATOM 338 O O . ARG A 1 53 ? 9.817 42.910 63.399 1.00 124.12 ? 53 ARG A O 1 ATOM 339 C CB . ARG A 1 53 ? 9.879 43.032 66.249 1.00 125.27 ? 53 ARG A CB 1 ATOM 340 C CG . ARG A 1 53 ? 10.267 41.599 65.932 1.00 125.92 ? 53 ARG A CG 1 ATOM 341 C CD . ARG A 1 53 ? 11.541 41.251 66.684 1.00 126.10 ? 53 ARG A CD 1 ATOM 342 N NE . ARG A 1 53 ? 12.564 42.272 66.464 1.00 126.26 ? 53 ARG A NE 1 ATOM 343 C CZ . ARG A 1 53 ? 13.713 42.345 67.127 1.00 126.45 ? 53 ARG A CZ 1 ATOM 344 N NH1 . ARG A 1 53 ? 14.002 41.453 68.062 1.00 127.15 ? 53 ARG A NH1 1 ATOM 345 N NH2 . ARG A 1 53 ? 14.568 43.323 66.862 1.00 126.22 ? 53 ARG A NH2 1 ATOM 346 N N . THR A 1 54 ? 8.622 44.830 63.344 1.00 122.59 ? 54 THR A N 1 ATOM 347 C CA . THR A 1 54 ? 8.853 45.140 61.932 1.00 120.66 ? 54 THR A CA 1 ATOM 348 C C . THR A 1 54 ? 8.216 44.056 61.074 1.00 118.64 ? 54 THR A C 1 ATOM 349 O O . THR A 1 54 ? 7.088 43.643 61.337 1.00 119.34 ? 54 THR A O 1 ATOM 350 C CB . THR A 1 54 ? 10.351 45.225 61.590 1.00 121.08 ? 54 THR A CB 1 ATOM 351 O OG1 . THR A 1 54 ? 11.104 45.489 62.780 1.00 121.69 ? 54 THR A OG1 1 ATOM 352 C CG2 . THR A 1 54 ? 10.592 46.354 60.585 1.00 120.69 ? 54 THR A CG2 1 ATOM 353 N N . SER A 1 55 ? 8.935 43.600 60.051 1.00 115.89 ? 55 SER A N 1 ATOM 354 C CA . SER A 1 55 ? 8.430 42.551 59.168 1.00 112.17 ? 55 SER A CA 1 ATOM 355 C C . SER A 1 55 ? 6.931 42.719 58.905 1.00 108.85 ? 55 SER A C 1 ATOM 356 O O . SER A 1 55 ? 6.174 41.747 58.960 1.00 107.66 ? 55 SER A O 1 ATOM 357 C CB . SER A 1 55 ? 8.699 41.183 59.802 1.00 112.78 ? 55 SER A CB 1 ATOM 358 O OG . SER A 1 55 ? 8.099 40.137 59.060 1.00 114.87 ? 55 SER A OG 1 ATOM 359 N N . GLY A 1 56 ? 6.520 43.957 58.625 1.00 105.10 ? 56 GLY A N 1 ATOM 360 C CA . GLY A 1 56 ? 5.120 44.258 58.370 1.00 100.68 ? 56 GLY A CA 1 ATOM 361 C C . GLY A 1 56 ? 4.416 43.258 57.475 1.00 98.23 ? 56 GLY A C 1 ATOM 362 O O . GLY A 1 56 ? 4.062 42.160 57.907 1.00 97.45 ? 56 GLY A O 1 ATOM 363 N N . LEU A 1 57 ? 4.201 43.640 56.221 1.00 95.72 ? 57 LEU A N 1 ATOM 364 C CA . LEU A 1 57 ? 3.549 42.761 55.262 1.00 91.96 ? 57 LEU A CA 1 ATOM 365 C C . LEU A 1 57 ? 4.487 41.635 54.834 1.00 89.22 ? 57 LEU A C 1 ATOM 366 O O . LEU A 1 57 ? 4.037 40.584 54.382 1.00 89.44 ? 57 LEU A O 1 ATOM 367 C CB . LEU A 1 57 ? 3.104 43.565 54.045 1.00 91.87 ? 57 LEU A CB 1 ATOM 368 C CG . LEU A 1 57 ? 1.836 44.391 54.264 1.00 92.63 ? 57 LEU A CG 1 ATOM 369 C CD1 . LEU A 1 57 ? 1.717 45.479 53.202 1.00 92.67 ? 57 LEU A CD1 1 ATOM 370 C CD2 . LEU A 1 57 ? 0.628 43.460 54.232 1.00 92.45 ? 57 LEU A CD2 1 ATOM 371 N N . LEU A 1 58 ? 5.789 41.861 54.990 1.00 85.59 ? 58 LEU A N 1 ATOM 372 C CA . LEU A 1 58 ? 6.805 40.877 54.624 1.00 82.61 ? 58 LEU A CA 1 ATOM 373 C C . LEU A 1 58 ? 6.394 39.464 55.044 1.00 79.39 ? 58 LEU A C 1 ATOM 374 O O . LEU A 1 58 ? 6.000 39.235 56.183 1.00 79.95 ? 58 LEU A O 1 ATOM 375 C CB . LEU A 1 58 ? 8.153 41.245 55.266 1.00 82.67 ? 58 LEU A CB 1 ATOM 376 C CG . LEU A 1 58 ? 9.375 40.447 54.794 1.00 82.89 ? 58 LEU A CG 1 ATOM 377 C CD1 . LEU A 1 58 ? 9.544 40.651 53.291 1.00 83.29 ? 58 LEU A CD1 1 ATOM 378 C CD2 . LEU A 1 58 ? 10.633 40.896 55.535 1.00 81.50 ? 58 LEU A CD2 1 ATOM 379 N N . GLY A 1 59 ? 6.479 38.516 54.118 1.00 75.61 ? 59 GLY A N 1 ATOM 380 C CA . GLY A 1 59 ? 6.100 37.152 54.440 1.00 71.06 ? 59 GLY A CA 1 ATOM 381 C C . GLY A 1 59 ? 7.106 36.528 55.382 1.00 67.67 ? 59 GLY A C 1 ATOM 382 O O . GLY A 1 59 ? 7.854 37.246 56.044 1.00 68.97 ? 59 GLY A O 1 ATOM 383 N N . PRO A 1 60 ? 7.146 35.194 55.474 1.00 64.00 ? 60 PRO A N 1 ATOM 384 C CA . PRO A 1 60 ? 8.090 34.516 56.356 1.00 63.60 ? 60 PRO A CA 1 ATOM 385 C C . PRO A 1 60 ? 9.543 34.918 56.111 1.00 64.99 ? 60 PRO A C 1 ATOM 386 O O . PRO A 1 60 ? 9.897 36.095 56.140 1.00 63.52 ? 60 PRO A O 1 ATOM 387 C CB . PRO A 1 60 ? 7.837 33.040 56.049 1.00 62.50 ? 60 PRO A CB 1 ATOM 388 C CG . PRO A 1 60 ? 6.385 33.008 55.801 1.00 62.20 ? 60 PRO A CG 1 ATOM 389 C CD . PRO A 1 60 ? 6.170 34.238 54.926 1.00 63.66 ? 60 PRO A CD 1 ATOM 390 N N . THR A 1 61 ? 10.374 33.904 55.891 1.00 67.62 ? 61 THR A N 1 ATOM 391 C CA . THR A 1 61 ? 11.800 34.044 55.629 1.00 69.46 ? 61 THR A CA 1 ATOM 392 C C . THR A 1 61 ? 12.314 32.626 55.483 1.00 73.01 ? 61 THR A C 1 ATOM 393 O O . THR A 1 61 ? 12.695 31.993 56.468 1.00 73.75 ? 61 THR A O 1 ATOM 394 C CB . THR A 1 61 ? 12.569 34.703 56.795 1.00 67.44 ? 61 THR A CB 1 ATOM 395 O OG1 . THR A 1 61 ? 12.272 36.103 56.853 1.00 66.47 ? 61 THR A OG1 1 ATOM 396 C CG2 . THR A 1 61 ? 14.063 34.520 56.604 1.00 65.34 ? 61 THR A CG2 1 ATOM 397 N N . LEU A 1 62 ? 12.309 32.122 54.253 1.00 76.10 ? 62 LEU A N 1 ATOM 398 C CA . LEU A 1 62 ? 12.772 30.764 53.995 1.00 79.50 ? 62 LEU A CA 1 ATOM 399 C C . LEU A 1 62 ? 14.298 30.723 53.866 1.00 81.03 ? 62 LEU A C 1 ATOM 400 O O . LEU A 1 62 ? 14.909 31.625 53.278 1.00 80.96 ? 62 LEU A O 1 ATOM 401 C CB . LEU A 1 62 ? 12.101 30.222 52.726 1.00 80.01 ? 62 LEU A CB 1 ATOM 402 C CG . LEU A 1 62 ? 10.571 30.136 52.798 1.00 81.16 ? 62 LEU A CG 1 ATOM 403 C CD1 . LEU A 1 62 ? 9.997 29.849 51.428 1.00 81.00 ? 62 LEU A CD1 1 ATOM 404 C CD2 . LEU A 1 62 ? 10.167 29.046 53.789 1.00 82.01 ? 62 LEU A CD2 1 ATOM 405 N N . TYR A 1 63 ? 14.907 29.683 54.434 1.00 81.66 ? 63 TYR A N 1 ATOM 406 C CA . TYR A 1 63 ? 16.355 29.529 54.389 1.00 83.39 ? 63 TYR A CA 1 ATOM 407 C C . TYR A 1 63 ? 16.823 28.081 54.389 1.00 83.06 ? 63 TYR A C 1 ATOM 408 O O . TYR A 1 63 ? 16.127 27.189 54.866 1.00 82.87 ? 63 TYR A O 1 ATOM 409 C CB . TYR A 1 63 ? 17.003 30.271 55.558 1.00 86.85 ? 63 TYR A CB 1 ATOM 410 C CG . TYR A 1 63 ? 16.243 30.169 56.857 1.00 90.69 ? 63 TYR A CG 1 ATOM 411 C CD1 . TYR A 1 63 ? 15.905 28.927 57.401 1.00 92.47 ? 63 TYR A CD1 1 ATOM 412 C CD2 . TYR A 1 63 ? 15.882 31.320 57.558 1.00 92.54 ? 63 TYR A CD2 1 ATOM 413 C CE1 . TYR A 1 63 ? 15.224 28.837 58.618 1.00 94.67 ? 63 TYR A CE1 1 ATOM 414 C CE2 . TYR A 1 63 ? 15.206 31.245 58.772 1.00 94.93 ? 63 TYR A CE2 1 ATOM 415 C CZ . TYR A 1 63 ? 14.880 30.005 59.299 1.00 96.02 ? 63 TYR A CZ 1 ATOM 416 O OH . TYR A 1 63 ? 14.225 29.943 60.511 1.00 98.02 ? 63 TYR A OH 1 ATOM 417 N N . ALA A 1 64 ? 18.014 27.859 53.844 1.00 82.92 ? 64 ALA A N 1 ATOM 418 C CA . ALA A 1 64 ? 18.588 26.527 53.772 1.00 83.83 ? 64 ALA A CA 1 ATOM 419 C C . ALA A 1 64 ? 20.080 26.606 53.502 1.00 84.57 ? 64 ALA A C 1 ATOM 420 O O . ALA A 1 64 ? 20.644 27.690 53.360 1.00 85.23 ? 64 ALA A O 1 ATOM 421 C CB . ALA A 1 64 ? 17.904 25.717 52.678 1.00 83.43 ? 64 ALA A CB 1 ATOM 422 N N . GLU A 1 65 ? 20.715 25.445 53.437 1.00 85.94 ? 65 GLU A N 1 ATOM 423 C CA . GLU A 1 65 ? 22.143 25.367 53.185 1.00 86.98 ? 65 GLU A CA 1 ATOM 424 C C . GLU A 1 65 ? 22.409 24.391 52.048 1.00 87.17 ? 65 GLU A C 1 ATOM 425 O O . GLU A 1 65 ? 21.633 23.464 51.806 1.00 85.94 ? 65 GLU A O 1 ATOM 426 C CB . GLU A 1 65 ? 22.876 24.898 54.444 1.00 87.02 ? 65 GLU A CB 1 ATOM 427 C CG . GLU A 1 65 ? 22.679 25.803 55.648 1.00 88.18 ? 65 GLU A CG 1 ATOM 428 C CD . GLU A 1 65 ? 23.100 25.142 56.953 1.00 88.62 ? 65 GLU A CD 1 ATOM 429 O OE1 . GLU A 1 65 ? 22.544 24.067 57.284 1.00 87.59 ? 65 GLU A OE1 1 ATOM 430 O OE2 . GLU A 1 65 ? 23.983 25.698 57.646 1.00 87.86 ? 65 GLU A OE2 1 ATOM 431 N N . VAL A 1 66 ? 23.513 24.613 51.350 1.00 87.72 ? 66 VAL A N 1 ATOM 432 C CA . VAL A 1 66 ? 23.900 23.756 50.245 1.00 88.15 ? 66 VAL A CA 1 ATOM 433 C C . VAL A 1 66 ? 23.713 22.302 50.659 1.00 88.03 ? 66 VAL A C 1 ATOM 434 O O . VAL A 1 66 ? 24.180 21.894 51.719 1.00 89.31 ? 66 VAL A O 1 ATOM 435 C CB . VAL A 1 66 ? 25.367 24.007 49.872 1.00 87.65 ? 66 VAL A CB 1 ATOM 436 C CG1 . VAL A 1 66 ? 25.542 25.462 49.447 1.00 87.20 ? 66 VAL A CG1 1 ATOM 437 C CG2 . VAL A 1 66 ? 26.265 23.701 51.063 1.00 87.50 ? 66 VAL A CG2 1 ATOM 438 N N . GLY A 1 67 ? 23.007 21.534 49.834 1.00 87.70 ? 67 GLY A N 1 ATOM 439 C CA . GLY A 1 67 ? 22.770 20.134 50.134 1.00 87.57 ? 67 GLY A CA 1 ATOM 440 C C . GLY A 1 67 ? 21.437 19.861 50.808 1.00 87.98 ? 67 GLY A C 1 ATOM 441 O O . GLY A 1 67 ? 20.863 18.788 50.643 1.00 88.03 ? 67 GLY A O 1 ATOM 442 N N . ASP A 1 68 ? 20.937 20.832 51.565 1.00 88.28 ? 68 ASP A N 1 ATOM 443 C CA . ASP A 1 68 ? 19.671 20.674 52.279 1.00 88.69 ? 68 ASP A CA 1 ATOM 444 C C . ASP A 1 68 ? 18.462 20.518 51.362 1.00 87.56 ? 68 ASP A C 1 ATOM 445 O O . ASP A 1 68 ? 17.964 21.502 50.815 1.00 87.48 ? 68 ASP A O 1 ATOM 446 C CB . ASP A 1 68 ? 19.417 21.873 53.207 1.00 90.72 ? 68 ASP A CB 1 ATOM 447 C CG . ASP A 1 68 ? 20.360 21.916 54.396 1.00 91.47 ? 68 ASP A CG 1 ATOM 448 O OD1 . ASP A 1 68 ? 21.564 22.181 54.205 1.00 91.76 ? 68 ASP A OD1 1 ATOM 449 O OD2 . ASP A 1 68 ? 19.889 21.686 55.529 1.00 92.95 ? 68 ASP A OD2 1 ATOM 450 N N . ILE A 1 69 ? 17.979 19.290 51.204 1.00 85.78 ? 69 ILE A N 1 ATOM 451 C CA . ILE A 1 69 ? 16.809 19.052 50.368 1.00 85.42 ? 69 ILE A CA 1 ATOM 452 C C . ILE A 1 69 ? 15.574 19.592 51.088 1.00 84.87 ? 69 ILE A C 1 ATOM 453 O O . ILE A 1 69 ? 14.774 18.821 51.618 1.00 86.33 ? 69 ILE A O 1 ATOM 454 C CB . ILE A 1 69 ? 16.619 17.542 50.091 1.00 85.78 ? 69 ILE A CB 1 ATOM 455 C CG1 . ILE A 1 69 ? 17.779 17.031 49.238 1.00 86.56 ? 69 ILE A CG1 1 ATOM 456 C CG2 . ILE A 1 69 ? 15.291 17.289 49.382 1.00 84.48 ? 69 ILE A CG2 1 ATOM 457 C CD1 . ILE A 1 69 ? 17.677 15.567 48.874 1.00 88.24 ? 69 ILE A CD1 1 ATOM 458 N N . MET A 1 70 ? 15.414 20.916 51.105 1.00 82.43 ? 70 MET A N 1 ATOM 459 C CA . MET A 1 70 ? 14.278 21.519 51.794 1.00 79.37 ? 70 MET A CA 1 ATOM 460 C C . MET A 1 70 ? 12.952 21.191 51.125 1.00 78.15 ? 70 MET A C 1 ATOM 461 O O . MET A 1 70 ? 12.916 20.824 49.954 1.00 79.10 ? 70 MET A O 1 ATOM 462 C CB . MET A 1 70 ? 14.453 23.038 51.908 1.00 77.86 ? 70 MET A CB 1 ATOM 463 C CG . MET A 1 70 ? 14.012 23.850 50.712 1.00 77.34 ? 70 MET A CG 1 ATOM 464 S SD . MET A 1 70 ? 14.135 25.621 51.083 1.00 76.26 ? 70 MET A SD 1 ATOM 465 C CE . MET A 1 70 ? 15.686 26.031 50.292 1.00 76.55 ? 70 MET A CE 1 ATOM 466 N N . LYS A 1 71 ? 11.865 21.313 51.882 1.00 76.40 ? 71 LYS A N 1 ATOM 467 C CA . LYS A 1 71 ? 10.531 21.020 51.371 1.00 74.40 ? 71 LYS A CA 1 ATOM 468 C C . LYS A 1 71 ? 9.553 22.048 51.905 1.00 74.46 ? 71 LYS A C 1 ATOM 469 O O . LYS A 1 71 ? 9.249 22.051 53.092 1.00 75.32 ? 71 LYS A O 1 ATOM 470 C CB . LYS A 1 71 ? 10.096 19.623 51.811 1.00 71.39 ? 71 LYS A CB 1 ATOM 471 C CG . LYS A 1 71 ? 8.834 19.124 51.138 1.00 69.02 ? 71 LYS A CG 1 ATOM 472 C CD . LYS A 1 71 ? 8.410 17.743 51.645 1.00 66.99 ? 71 LYS A CD 1 ATOM 473 C CE . LYS A 1 71 ? 9.436 16.663 51.328 1.00 64.48 ? 71 LYS A CE 1 ATOM 474 N NZ . LYS A 1 71 ? 10.742 16.916 51.994 1.00 62.90 ? 71 LYS A NZ 1 ATOM 475 N N . VAL A 1 72 ? 9.064 22.922 51.030 1.00 75.80 ? 72 VAL A N 1 ATOM 476 C CA . VAL A 1 72 ? 8.120 23.964 51.437 1.00 76.45 ? 72 VAL A CA 1 ATOM 477 C C . VAL A 1 72 ? 6.660 23.587 51.210 1.00 78.41 ? 72 VAL A C 1 ATOM 478 O O . VAL A 1 72 ? 6.221 23.429 50.073 1.00 79.71 ? 72 VAL A O 1 ATOM 479 C CB . VAL A 1 72 ? 8.395 25.298 50.696 1.00 74.09 ? 72 VAL A CB 1 ATOM 480 C CG1 . VAL A 1 72 ? 7.221 26.253 50.872 1.00 71.64 ? 72 VAL A CG1 1 ATOM 481 C CG2 . VAL A 1 72 ? 9.661 25.928 51.233 1.00 72.92 ? 72 VAL A CG2 1 ATOM 482 N N . HIS A 1 73 ? 5.911 23.441 52.300 1.00 79.34 ? 73 HIS A N 1 ATOM 483 C CA . HIS A 1 73 ? 4.495 23.109 52.206 1.00 79.11 ? 73 HIS A CA 1 ATOM 484 C C . HIS A 1 73 ? 3.711 24.416 52.091 1.00 79.51 ? 73 HIS A C 1 ATOM 485 O O . HIS A 1 73 ? 3.917 25.343 52.873 1.00 79.40 ? 73 HIS A O 1 ATOM 486 C CB . HIS A 1 73 ? 4.030 22.333 53.446 1.00 77.74 ? 73 HIS A CB 1 ATOM 487 C CG . HIS A 1 73 ? 4.726 21.021 53.643 1.00 76.56 ? 73 HIS A CG 1 ATOM 488 N ND1 . HIS A 1 73 ? 5.993 20.921 54.177 1.00 75.85 ? 73 HIS A ND1 1 ATOM 489 C CD2 . HIS A 1 73 ? 4.337 19.754 53.363 1.00 76.20 ? 73 HIS A CD2 1 ATOM 490 C CE1 . HIS A 1 73 ? 6.353 19.650 54.218 1.00 74.91 ? 73 HIS A CE1 1 ATOM 491 N NE2 . HIS A 1 73 ? 5.366 18.921 53.728 1.00 74.79 ? 73 HIS A NE2 1 ATOM 492 N N . PHE A 1 74 ? 2.815 24.484 51.112 1.00 80.19 ? 74 PHE A N 1 ATOM 493 C CA . PHE A 1 74 ? 2.012 25.682 50.892 1.00 80.68 ? 74 PHE A CA 1 ATOM 494 C C . PHE A 1 74 ? 0.516 25.370 51.006 1.00 81.72 ? 74 PHE A C 1 ATOM 495 O O . PHE A 1 74 ? 0.037 24.381 50.454 1.00 81.20 ? 74 PHE A O 1 ATOM 496 C CB . PHE A 1 74 ? 2.331 26.263 49.503 1.00 77.95 ? 74 PHE A CB 1 ATOM 497 C CG . PHE A 1 74 ? 1.748 27.636 49.258 1.00 76.93 ? 74 PHE A CG 1 ATOM 498 C CD1 . PHE A 1 74 ? 2.043 28.698 50.110 1.00 75.31 ? 74 PHE A CD1 1 ATOM 499 C CD2 . PHE A 1 74 ? 0.917 27.871 48.159 1.00 75.96 ? 74 PHE A CD2 1 ATOM 500 C CE1 . PHE A 1 74 ? 1.520 29.976 49.872 1.00 74.03 ? 74 PHE A CE1 1 ATOM 501 C CE2 . PHE A 1 74 ? 0.390 29.143 47.912 1.00 73.52 ? 74 PHE A CE2 1 ATOM 502 C CZ . PHE A 1 74 ? 0.693 30.196 48.771 1.00 73.90 ? 74 PHE A CZ 1 ATOM 503 N N . LYS A 1 75 ? -0.208 26.215 51.737 1.00 83.91 ? 75 LYS A N 1 ATOM 504 C CA . LYS A 1 75 ? -1.653 26.060 51.919 1.00 85.95 ? 75 LYS A CA 1 ATOM 505 C C . LYS A 1 75 ? -2.313 27.413 51.662 1.00 86.63 ? 75 LYS A C 1 ATOM 506 O O . LYS A 1 75 ? -2.217 28.330 52.475 1.00 85.83 ? 75 LYS A O 1 ATOM 507 C CB . LYS A 1 75 ? -1.975 25.580 53.345 1.00 86.81 ? 75 LYS A CB 1 ATOM 508 C CG . LYS A 1 75 ? -3.469 25.392 53.629 1.00 88.65 ? 75 LYS A CG 1 ATOM 509 C CD . LYS A 1 75 ? -3.729 24.916 55.060 1.00 90.18 ? 75 LYS A CD 1 ATOM 510 C CE . LYS A 1 75 ? -5.225 24.939 55.424 1.00 90.15 ? 75 LYS A CE 1 ATOM 511 N NZ . LYS A 1 75 ? -6.063 23.988 54.632 1.00 89.11 ? 75 LYS A NZ 1 ATOM 512 N N . ASN A 1 76 ? -2.980 27.535 50.522 1.00 88.05 ? 76 ASN A N 1 ATOM 513 C CA . ASN A 1 76 ? -3.634 28.783 50.153 1.00 89.80 ? 76 ASN A CA 1 ATOM 514 C C . ASN A 1 76 ? -4.971 28.953 50.852 1.00 92.29 ? 76 ASN A C 1 ATOM 515 O O . ASN A 1 76 ? -5.747 28.002 50.990 1.00 93.12 ? 76 ASN A O 1 ATOM 516 C CB . ASN A 1 76 ? -3.822 28.839 48.630 1.00 88.87 ? 76 ASN A CB 1 ATOM 517 C CG . ASN A 1 76 ? -4.540 30.095 48.165 1.00 87.16 ? 76 ASN A CG 1 ATOM 518 O OD1 . ASN A 1 76 ? -4.269 31.197 48.639 1.00 87.22 ? 76 ASN A OD1 1 ATOM 519 N ND2 . ASN A 1 76 ? -5.449 29.933 47.214 1.00 86.20 ? 76 ASN A ND2 1 ATOM 520 N N . LYS A 1 77 ? -5.234 30.176 51.296 1.00 94.21 ? 77 LYS A N 1 ATOM 521 C CA . LYS A 1 77 ? -6.480 30.489 51.978 1.00 95.83 ? 77 LYS A CA 1 ATOM 522 C C . LYS A 1 77 ? -7.091 31.786 51.447 1.00 96.55 ? 77 LYS A C 1 ATOM 523 O O . LYS A 1 77 ? -8.198 32.158 51.840 1.00 97.95 ? 77 LYS A O 1 ATOM 524 C CB . LYS A 1 77 ? -6.248 30.602 53.492 1.00 96.86 ? 77 LYS A CB 1 ATOM 525 C CG . LYS A 1 77 ? -5.792 29.305 54.174 1.00 97.21 ? 77 LYS A CG 1 ATOM 526 C CD . LYS A 1 77 ? -5.820 29.453 55.692 1.00 97.26 ? 77 LYS A CD 1 ATOM 527 C CE . LYS A 1 77 ? -5.506 28.146 56.404 1.00 97.17 ? 77 LYS A CE 1 ATOM 528 N NZ . LYS A 1 77 ? -4.091 27.733 56.214 1.00 97.89 ? 77 LYS A NZ 1 ATOM 529 N N . ALA A 1 78 ? -6.372 32.471 50.559 1.00 96.06 ? 78 ALA A N 1 ATOM 530 C CA . ALA A 1 78 ? -6.856 33.721 49.976 1.00 95.75 ? 78 ALA A CA 1 ATOM 531 C C . ALA A 1 78 ? -8.003 33.438 49.012 1.00 95.74 ? 78 ALA A C 1 ATOM 532 O O . ALA A 1 78 ? -8.440 32.297 48.882 1.00 95.13 ? 78 ALA A O 1 ATOM 533 C CB . ALA A 1 78 ? -5.725 34.425 49.248 1.00 96.27 ? 78 ALA A CB 1 ATOM 534 N N . HIS A 1 79 ? -8.491 34.468 48.329 1.00 96.47 ? 79 HIS A N 1 ATOM 535 C CA . HIS A 1 79 ? -9.592 34.274 47.392 1.00 97.48 ? 79 HIS A CA 1 ATOM 536 C C . HIS A 1 79 ? -9.192 34.277 45.925 1.00 96.26 ? 79 HIS A C 1 ATOM 537 O O . HIS A 1 79 ? -10.019 34.542 45.048 1.00 97.23 ? 79 HIS A O 1 ATOM 538 C CB . HIS A 1 79 ? -10.688 35.312 47.630 1.00 100.52 ? 79 HIS A CB 1 ATOM 539 C CG . HIS A 1 79 ? -11.529 35.020 48.833 1.00 104.36 ? 79 HIS A CG 1 ATOM 540 N ND1 . HIS A 1 79 ? -12.057 33.770 49.082 1.00 104.96 ? 79 HIS A ND1 1 ATOM 541 C CD2 . HIS A 1 79 ? -11.938 35.812 49.853 1.00 105.25 ? 79 HIS A CD2 1 ATOM 542 C CE1 . HIS A 1 79 ? -12.753 33.805 50.204 1.00 105.84 ? 79 HIS A CE1 1 ATOM 543 N NE2 . HIS A 1 79 ? -12.697 35.032 50.691 1.00 106.42 ? 79 HIS A NE2 1 ATOM 544 N N . LYS A 1 80 ? -7.922 33.982 45.667 1.00 93.35 ? 80 LYS A N 1 ATOM 545 C CA . LYS A 1 80 ? -7.391 33.912 44.311 1.00 88.82 ? 80 LYS A CA 1 ATOM 546 C C . LYS A 1 80 ? -6.317 32.854 44.308 1.00 85.53 ? 80 LYS A C 1 ATOM 547 O O . LYS A 1 80 ? -5.530 32.766 45.245 1.00 85.74 ? 80 LYS A O 1 ATOM 548 C CB . LYS A 1 80 ? -6.774 35.245 43.875 1.00 89.13 ? 80 LYS A CB 1 ATOM 549 C CG . LYS A 1 80 ? -7.787 36.344 43.613 1.00 91.10 ? 80 LYS A CG 1 ATOM 550 C CD . LYS A 1 80 ? -7.410 37.209 42.405 1.00 91.67 ? 80 LYS A CD 1 ATOM 551 C CE . LYS A 1 80 ? -6.088 37.946 42.597 1.00 91.35 ? 80 LYS A CE 1 ATOM 552 N NZ . LYS A 1 80 ? -5.821 38.904 41.484 1.00 88.50 ? 80 LYS A NZ 1 ATOM 553 N N . PRO A 1 81 ? -6.275 32.019 43.262 1.00 82.87 ? 81 PRO A N 1 ATOM 554 C CA . PRO A 1 81 ? -5.237 30.982 43.221 1.00 79.75 ? 81 PRO A CA 1 ATOM 555 C C . PRO A 1 81 ? -3.864 31.649 43.244 1.00 75.74 ? 81 PRO A C 1 ATOM 556 O O . PRO A 1 81 ? -3.685 32.726 42.675 1.00 73.54 ? 81 PRO A O 1 ATOM 557 C CB . PRO A 1 81 ? -5.528 30.245 41.912 1.00 80.21 ? 81 PRO A CB 1 ATOM 558 C CG . PRO A 1 81 ? -6.201 31.295 41.063 1.00 82.13 ? 81 PRO A CG 1 ATOM 559 C CD . PRO A 1 81 ? -7.101 32.006 42.042 1.00 82.32 ? 81 PRO A CD 1 ATOM 560 N N . LEU A 1 82 ? -2.907 31.021 43.919 1.00 72.44 ? 82 LEU A N 1 ATOM 561 C CA . LEU A 1 82 ? -1.565 31.582 44.026 1.00 70.00 ? 82 LEU A CA 1 ATOM 562 C C . LEU A 1 82 ? -0.513 30.477 43.971 1.00 68.87 ? 82 LEU A C 1 ATOM 563 O O . LEU A 1 82 ? -0.846 29.307 43.769 1.00 66.96 ? 82 LEU A O 1 ATOM 564 C CB . LEU A 1 82 ? -1.419 32.361 45.343 1.00 69.31 ? 82 LEU A CB 1 ATOM 565 C CG . LEU A 1 82 ? -2.387 33.492 45.720 1.00 65.66 ? 82 LEU A CG 1 ATOM 566 C CD1 . LEU A 1 82 ? -1.961 34.060 47.056 1.00 66.46 ? 82 LEU A CD1 1 ATOM 567 C CD2 . LEU A 1 82 ? -2.391 34.587 44.685 1.00 64.34 ? 82 LEU A CD2 1 ATOM 568 N N . SER A 1 83 ? 0.752 30.859 44.156 1.00 67.90 ? 83 SER A N 1 ATOM 569 C CA . SER A 1 83 ? 1.867 29.908 44.132 1.00 66.40 ? 83 SER A CA 1 ATOM 570 C C . SER A 1 83 ? 3.099 30.468 44.835 1.00 65.77 ? 83 SER A C 1 ATOM 571 O O . SER A 1 83 ? 3.130 31.640 45.225 1.00 65.61 ? 83 SER A O 1 ATOM 572 C CB . SER A 1 83 ? 2.245 29.567 42.691 1.00 65.99 ? 83 SER A CB 1 ATOM 573 O OG . SER A 1 83 ? 2.609 30.736 41.975 1.00 64.69 ? 83 SER A OG 1 ATOM 574 N N . ILE A 1 84 ? 4.108 29.616 44.993 1.00 63.11 ? 84 ILE A N 1 ATOM 575 C CA . ILE A 1 84 ? 5.365 30.002 45.624 1.00 61.26 ? 84 ILE A CA 1 ATOM 576 C C . ILE A 1 84 ? 6.396 30.114 44.520 1.00 59.16 ? 84 ILE A C 1 ATOM 577 O O . ILE A 1 84 ? 6.805 29.094 43.971 1.00 59.99 ? 84 ILE A O 1 ATOM 578 C CB . ILE A 1 84 ? 5.885 28.917 46.609 1.00 62.31 ? 84 ILE A CB 1 ATOM 579 C CG1 . ILE A 1 84 ? 4.921 28.741 47.788 1.00 62.35 ? 84 ILE A CG1 1 ATOM 580 C CG2 . ILE A 1 84 ? 7.288 29.306 47.107 1.00 62.54 ? 84 ILE A CG2 1 ATOM 581 C CD1 . ILE A 1 84 ? 5.175 29.672 48.978 1.00 60.97 ? 84 ILE A CD1 1 ATOM 582 N N . HIS A 1 85 ? 6.828 31.326 44.190 1.00 58.30 ? 85 HIS A N 1 ATOM 583 C CA . HIS A 1 85 ? 7.828 31.478 43.128 1.00 58.89 ? 85 HIS A CA 1 ATOM 584 C C . HIS A 1 85 ? 9.175 31.962 43.637 1.00 55.63 ? 85 HIS A C 1 ATOM 585 O O . HIS A 1 85 ? 9.470 33.155 43.629 1.00 53.21 ? 85 HIS A O 1 ATOM 586 C CB . HIS A 1 85 ? 7.327 32.425 42.026 1.00 63.07 ? 85 HIS A CB 1 ATOM 587 C CG . HIS A 1 85 ? 8.138 32.362 40.768 1.00 66.06 ? 85 HIS A CG 1 ATOM 588 N ND1 . HIS A 1 85 ? 9.376 32.958 40.648 1.00 68.54 ? 85 HIS A ND1 1 ATOM 589 C CD2 . HIS A 1 85 ? 7.919 31.714 39.600 1.00 67.17 ? 85 HIS A CD2 1 ATOM 590 C CE1 . HIS A 1 85 ? 9.886 32.676 39.462 1.00 67.97 ? 85 HIS A CE1 1 ATOM 591 N NE2 . HIS A 1 85 ? 9.022 31.922 38.808 1.00 67.44 ? 85 HIS A NE2 1 ATOM 592 N N . ALA A 1 86 ? 10.000 31.016 44.063 1.00 53.72 ? 86 ALA A N 1 ATOM 593 C CA . ALA A 1 86 ? 11.314 31.339 44.584 1.00 54.38 ? 86 ALA A CA 1 ATOM 594 C C . ALA A 1 86 ? 12.178 31.840 43.453 1.00 55.92 ? 86 ALA A C 1 ATOM 595 O O . ALA A 1 86 ? 12.253 31.196 42.406 1.00 56.30 ? 86 ALA A O 1 ATOM 596 C CB . ALA A 1 86 ? 11.951 30.104 45.201 1.00 51.35 ? 86 ALA A CB 1 ATOM 597 N N . GLN A 1 87 ? 12.825 32.986 43.642 1.00 56.11 ? 87 GLN A N 1 ATOM 598 C CA . GLN A 1 87 ? 13.706 33.483 42.596 1.00 55.99 ? 87 GLN A CA 1 ATOM 599 C C . GLN A 1 87 ? 15.143 33.363 43.062 1.00 55.06 ? 87 GLN A C 1 ATOM 600 O O . GLN A 1 87 ? 15.774 34.370 43.384 1.00 55.82 ? 87 GLN A O 1 ATOM 601 C CB . GLN A 1 87 ? 13.409 34.945 42.222 1.00 56.29 ? 87 GLN A CB 1 ATOM 602 C CG . GLN A 1 87 ? 13.694 35.960 43.317 1.00 58.43 ? 87 GLN A CG 1 ATOM 603 C CD . GLN A 1 87 ? 14.395 37.205 42.812 1.00 58.75 ? 87 GLN A CD 1 ATOM 604 O OE1 . GLN A 1 87 ? 13.859 37.958 41.992 1.00 56.17 ? 87 GLN A OE1 1 ATOM 605 N NE2 . GLN A 1 87 ? 15.609 37.431 43.308 1.00 60.63 ? 87 GLN A NE2 1 ATOM 606 N N . GLY A 1 88 ? 15.649 32.127 43.105 1.00 53.51 ? 88 GLY A N 1 ATOM 607 C CA . GLY A 1 88 ? 17.026 31.890 43.503 1.00 54.57 ? 88 GLY A CA 1 ATOM 608 C C . GLY A 1 88 ? 17.420 30.427 43.592 1.00 56.59 ? 88 GLY A C 1 ATOM 609 O O . GLY A 1 88 ? 18.503 30.097 44.074 1.00 58.46 ? 88 GLY A O 1 ATOM 610 N N . ILE A 1 89 ? 16.561 29.538 43.112 1.00 57.44 ? 89 ILE A N 1 ATOM 611 C CA . ILE A 1 89 ? 16.848 28.113 43.191 1.00 57.79 ? 89 ILE A CA 1 ATOM 612 C C . ILE A 1 89 ? 16.684 27.320 41.895 1.00 56.68 ? 89 ILE A C 1 ATOM 613 O O . ILE A 1 89 ? 15.899 27.680 41.018 1.00 55.93 ? 89 ILE A O 1 ATOM 614 C CB . ILE A 1 89 ? 15.987 27.481 44.305 1.00 59.44 ? 89 ILE A CB 1 ATOM 615 C CG1 . ILE A 1 89 ? 16.510 27.963 45.662 1.00 60.84 ? 89 ILE A CG1 1 ATOM 616 C CG2 . ILE A 1 89 ? 15.994 25.967 44.201 1.00 59.31 ? 89 ILE A CG2 1 ATOM 617 C CD1 . ILE A 1 89 ? 15.976 27.201 46.854 1.00 63.94 ? 89 ILE A CD1 1 ATOM 618 N N . LYS A 1 90 ? 17.436 26.233 41.778 1.00 55.03 ? 90 LYS A N 1 ATOM 619 C CA . LYS A 1 90 ? 17.358 25.401 40.591 1.00 55.95 ? 90 LYS A CA 1 ATOM 620 C C . LYS A 1 90 ? 16.260 24.364 40.770 1.00 55.38 ? 90 LYS A C 1 ATOM 621 O O . LYS A 1 90 ? 16.521 23.195 41.057 1.00 56.06 ? 90 LYS A O 1 ATOM 622 C CB . LYS A 1 90 ? 18.707 24.720 40.326 1.00 56.91 ? 90 LYS A CB 1 ATOM 623 C CG . LYS A 1 90 ? 19.814 25.682 39.909 1.00 59.37 ? 90 LYS A CG 1 ATOM 624 C CD . LYS A 1 90 ? 21.102 24.926 39.583 1.00 62.86 ? 90 LYS A CD 1 ATOM 625 C CE . LYS A 1 90 ? 22.104 25.778 38.783 1.00 64.51 ? 90 LYS A CE 1 ATOM 626 N NZ . LYS A 1 90 ? 22.708 26.930 39.528 1.00 63.45 ? 90 LYS A NZ 1 ATOM 627 N N . TYR A 1 91 ? 15.021 24.799 40.595 1.00 54.78 ? 91 TYR A N 1 ATOM 628 C CA . TYR A 1 91 ? 13.883 23.907 40.752 1.00 54.34 ? 91 TYR A CA 1 ATOM 629 C C . TYR A 1 91 ? 13.564 23.100 39.506 1.00 53.65 ? 91 TYR A C 1 ATOM 630 O O . TYR A 1 91 ? 14.267 23.161 38.509 1.00 52.42 ? 91 TYR A O 1 ATOM 631 C CB . TYR A 1 91 ? 12.647 24.702 41.183 1.00 54.64 ? 91 TYR A CB 1 ATOM 632 C CG . TYR A 1 91 ? 12.464 26.014 40.457 1.00 54.49 ? 91 TYR A CG 1 ATOM 633 C CD1 . TYR A 1 91 ? 12.372 26.058 39.064 1.00 56.86 ? 91 TYR A CD1 1 ATOM 634 C CD2 . TYR A 1 91 ? 12.374 27.218 41.162 1.00 53.44 ? 91 TYR A CD2 1 ATOM 635 C CE1 . TYR A 1 91 ? 12.195 27.278 38.384 1.00 57.85 ? 91 TYR A CE1 1 ATOM 636 C CE2 . TYR A 1 91 ? 12.195 28.438 40.496 1.00 53.24 ? 91 TYR A CE2 1 ATOM 637 C CZ . TYR A 1 91 ? 12.107 28.460 39.107 1.00 55.24 ? 91 TYR A CZ 1 ATOM 638 O OH . TYR A 1 91 ? 11.926 29.645 38.437 1.00 54.60 ? 91 TYR A OH 1 ATOM 639 N N . SER A 1 92 ? 12.501 22.316 39.591 1.00 55.14 ? 92 SER A N 1 ATOM 640 C CA . SER A 1 92 ? 12.072 21.505 38.475 1.00 57.58 ? 92 SER A CA 1 ATOM 641 C C . SER A 1 92 ? 10.707 22.011 38.110 1.00 58.09 ? 92 SER A C 1 ATOM 642 O O . SER A 1 92 ? 10.156 22.871 38.793 1.00 59.60 ? 92 SER A O 1 ATOM 643 C CB . SER A 1 92 ? 12.015 20.033 38.861 1.00 60.54 ? 92 SER A CB 1 ATOM 644 O OG . SER A 1 92 ? 13.328 19.528 39.035 1.00 64.07 ? 92 SER A OG 1 ATOM 645 N N . LYS A 1 93 ? 10.152 21.474 37.039 1.00 57.88 ? 93 LYS A N 1 ATOM 646 C CA . LYS A 1 93 ? 8.865 21.934 36.569 1.00 57.71 ? 93 LYS A CA 1 ATOM 647 C C . LYS A 1 93 ? 7.722 21.786 37.556 1.00 59.14 ? 93 LYS A C 1 ATOM 648 O O . LYS A 1 93 ? 6.815 22.614 37.590 1.00 60.47 ? 93 LYS A O 1 ATOM 649 C CB . LYS A 1 93 ? 8.559 21.249 35.243 1.00 55.52 ? 93 LYS A CB 1 ATOM 650 C CG . LYS A 1 93 ? 9.644 21.521 34.200 1.00 51.09 ? 93 LYS A CG 1 ATOM 651 C CD . LYS A 1 93 ? 9.817 23.022 33.931 1.00 50.74 ? 93 LYS A CD 1 ATOM 652 C CE . LYS A 1 93 ? 8.561 23.629 33.296 1.00 50.59 ? 93 LYS A CE 1 ATOM 653 N NZ . LYS A 1 93 ? 8.694 25.056 32.891 1.00 50.21 ? 93 LYS A NZ 1 ATOM 654 N N . PHE A 1 94 ? 7.767 20.748 38.377 1.00 62.20 ? 94 PHE A N 1 ATOM 655 C CA . PHE A 1 94 ? 6.715 20.531 39.357 1.00 62.47 ? 94 PHE A CA 1 ATOM 656 C C . PHE A 1 94 ? 7.061 21.161 40.695 1.00 61.71 ? 94 PHE A C 1 ATOM 657 O O . PHE A 1 94 ? 6.494 20.798 41.723 1.00 64.11 ? 94 PHE A O 1 ATOM 658 C CB . PHE A 1 94 ? 6.456 19.034 39.539 1.00 65.40 ? 94 PHE A CB 1 ATOM 659 C CG . PHE A 1 94 ? 7.702 18.214 39.649 1.00 69.35 ? 94 PHE A CG 1 ATOM 660 C CD1 . PHE A 1 94 ? 8.759 18.630 40.456 1.00 71.37 ? 94 PHE A CD1 1 ATOM 661 C CD2 . PHE A 1 94 ? 7.825 17.027 38.938 1.00 70.19 ? 94 PHE A CD2 1 ATOM 662 C CE1 . PHE A 1 94 ? 9.925 17.873 40.550 1.00 74.34 ? 94 PHE A CE1 1 ATOM 663 C CE2 . PHE A 1 94 ? 8.984 16.265 39.024 1.00 73.05 ? 94 PHE A CE2 1 ATOM 664 C CZ . PHE A 1 94 ? 10.039 16.688 39.832 1.00 74.14 ? 94 PHE A CZ 1 ATOM 665 N N . SER A 1 95 ? 7.989 22.109 40.678 1.00 61.04 ? 95 SER A N 1 ATOM 666 C CA . SER A 1 95 ? 8.410 22.797 41.897 1.00 59.54 ? 95 SER A CA 1 ATOM 667 C C . SER A 1 95 ? 8.792 24.244 41.591 1.00 57.58 ? 95 SER A C 1 ATOM 668 O O . SER A 1 95 ? 9.269 24.967 42.464 1.00 57.34 ? 95 SER A O 1 ATOM 669 C CB . SER A 1 95 ? 9.602 22.069 42.542 1.00 60.36 ? 95 SER A CB 1 ATOM 670 O OG . SER A 1 95 ? 9.262 20.759 42.984 1.00 60.85 ? 95 SER A OG 1 ATOM 671 N N . GLU A 1 96 ? 8.576 24.659 40.347 1.00 55.14 ? 96 GLU A N 1 ATOM 672 C CA . GLU A 1 96 ? 8.897 26.019 39.922 1.00 53.23 ? 96 GLU A CA 1 ATOM 673 C C . GLU A 1 96 ? 7.969 27.026 40.587 1.00 50.72 ? 96 GLU A C 1 ATOM 674 O O . GLU A 1 96 ? 8.371 27.700 41.530 1.00 50.46 ? 96 GLU A O 1 ATOM 675 C CB . GLU A 1 96 ? 8.782 26.127 38.400 1.00 55.33 ? 96 GLU A CB 1 ATOM 676 C CG . GLU A 1 96 ? 9.175 27.467 37.812 1.00 53.36 ? 96 GLU A CG 1 ATOM 677 C CD . GLU A 1 96 ? 9.049 27.480 36.299 1.00 56.13 ? 96 GLU A CD 1 ATOM 678 O OE1 . GLU A 1 96 ? 9.970 27.997 35.626 1.00 56.07 ? 96 GLU A OE1 1 ATOM 679 O OE2 . GLU A 1 96 ? 8.024 26.975 35.785 1.00 55.70 ? 96 GLU A OE2 1 ATOM 680 N N . GLY A 1 97 ? 6.734 27.117 40.096 1.00 49.78 ? 97 GLY A N 1 ATOM 681 C CA . GLY A 1 97 ? 5.762 28.041 40.665 1.00 50.21 ? 97 GLY A CA 1 ATOM 682 C C . GLY A 1 97 ? 5.283 29.106 39.691 1.00 50.32 ? 97 GLY A C 1 ATOM 683 O O . GLY A 1 97 ? 4.839 30.185 40.088 1.00 48.81 ? 97 GLY A O 1 ATOM 684 N N . ALA A 1 98 ? 5.371 28.796 38.404 1.00 50.08 ? 98 ALA A N 1 ATOM 685 C CA . ALA A 1 98 ? 4.967 29.730 37.368 1.00 49.97 ? 98 ALA A CA 1 ATOM 686 C C . ALA A 1 98 ? 4.167 29.029 36.281 1.00 50.18 ? 98 ALA A C 1 ATOM 687 O O . ALA A 1 98 ? 4.237 27.809 36.137 1.00 50.45 ? 98 ALA A O 1 ATOM 688 C CB . ALA A 1 98 ? 6.194 30.386 36.759 1.00 48.81 ? 98 ALA A CB 1 ATOM 689 N N . SER A 1 99 ? 3.408 29.809 35.517 1.00 48.42 ? 99 SER A N 1 ATOM 690 C CA . SER A 1 99 ? 2.624 29.250 34.440 1.00 47.89 ? 99 SER A CA 1 ATOM 691 C C . SER A 1 99 ? 2.893 29.959 33.130 1.00 49.42 ? 99 SER A C 1 ATOM 692 O O . SER A 1 99 ? 2.813 31.183 33.045 1.00 50.18 ? 99 SER A O 1 ATOM 693 C CB . SER A 1 99 ? 1.131 29.329 34.743 1.00 48.71 ? 99 SER A CB 1 ATOM 694 O OG . SER A 1 99 ? 0.370 28.676 33.732 1.00 43.91 ? 99 SER A OG 1 ATOM 695 N N . TYR A 1 100 ? 3.242 29.158 32.127 1.00 49.96 ? 100 TYR A N 1 ATOM 696 C CA . TYR A 1 100 ? 3.498 29.595 30.759 1.00 51.08 ? 100 TYR A CA 1 ATOM 697 C C . TYR A 1 100 ? 3.587 28.337 29.909 1.00 52.41 ? 100 TYR A C 1 ATOM 698 O O . TYR A 1 100 ? 3.622 27.218 30.430 1.00 51.65 ? 100 TYR A O 1 ATOM 699 C CB . TYR A 1 100 ? 4.791 30.450 30.613 1.00 49.88 ? 100 TYR A CB 1 ATOM 700 C CG . TYR A 1 100 ? 6.046 29.913 31.270 1.00 47.45 ? 100 TYR A CG 1 ATOM 701 C CD1 . TYR A 1 100 ? 6.362 30.228 32.588 1.00 45.55 ? 100 TYR A CD1 1 ATOM 702 C CD2 . TYR A 1 100 ? 6.884 29.042 30.588 1.00 46.44 ? 100 TYR A CD2 1 ATOM 703 C CE1 . TYR A 1 100 ? 7.483 29.677 33.215 1.00 46.86 ? 100 TYR A CE1 1 ATOM 704 C CE2 . TYR A 1 100 ? 8.001 28.485 31.201 1.00 47.53 ? 100 TYR A CE2 1 ATOM 705 C CZ . TYR A 1 100 ? 8.294 28.798 32.510 1.00 48.64 ? 100 TYR A CZ 1 ATOM 706 O OH . TYR A 1 100 ? 9.371 28.182 33.112 1.00 50.03 ? 100 TYR A OH 1 ATOM 707 N N . SER A 1 101 ? 3.595 28.518 28.597 1.00 55.21 ? 101 SER A N 1 ATOM 708 C CA . SER A 1 101 ? 3.678 27.388 27.697 1.00 55.85 ? 101 SER A CA 1 ATOM 709 C C . SER A 1 101 ? 5.034 26.728 27.791 1.00 55.56 ? 101 SER A C 1 ATOM 710 O O . SER A 1 101 ? 5.931 27.068 27.038 1.00 55.48 ? 101 SER A O 1 ATOM 711 C CB . SER A 1 101 ? 3.419 27.836 26.261 1.00 56.22 ? 101 SER A CB 1 ATOM 712 O OG . SER A 1 101 ? 2.061 28.201 26.086 1.00 58.81 ? 101 SER A OG 1 ATOM 713 N N . ASP A 1 102 ? 5.183 25.800 28.732 1.00 56.36 ? 102 ASP A N 1 ATOM 714 C CA . ASP A 1 102 ? 6.437 25.065 28.899 1.00 56.37 ? 102 ASP A CA 1 ATOM 715 C C . ASP A 1 102 ? 6.222 23.653 28.375 1.00 56.98 ? 102 ASP A C 1 ATOM 716 O O . ASP A 1 102 ? 7.108 22.794 28.472 1.00 56.77 ? 102 ASP A O 1 ATOM 717 C CB . ASP A 1 102 ? 6.878 25.018 30.371 1.00 56.72 ? 102 ASP A CB 1 ATOM 718 C CG . ASP A 1 102 ? 5.734 24.738 31.324 1.00 56.20 ? 102 ASP A CG 1 ATOM 719 O OD1 . ASP A 1 102 ? 4.748 24.089 30.913 1.00 58.55 ? 102 ASP A OD1 1 ATOM 720 O OD2 . ASP A 1 102 ? 5.832 25.160 32.493 1.00 54.78 ? 102 ASP A OD2 1 ATOM 721 N N . HIS A 1 103 ? 5.023 23.434 27.833 1.00 57.32 ? 103 HIS A N 1 ATOM 722 C CA . HIS A 1 103 ? 4.615 22.160 27.239 1.00 56.54 ? 103 HIS A CA 1 ATOM 723 C C . HIS A 1 103 ? 4.598 20.960 28.187 1.00 58.15 ? 103 HIS A C 1 ATOM 724 O O . HIS A 1 103 ? 4.544 19.813 27.728 1.00 57.50 ? 103 HIS A O 1 ATOM 725 C CB . HIS A 1 103 ? 5.510 21.860 26.033 1.00 54.13 ? 103 HIS A CB 1 ATOM 726 C CG . HIS A 1 103 ? 5.569 22.982 25.043 1.00 55.83 ? 103 HIS A CG 1 ATOM 727 N ND1 . HIS A 1 103 ? 4.503 23.319 24.236 1.00 55.15 ? 103 HIS A ND1 1 ATOM 728 C CD2 . HIS A 1 103 ? 6.536 23.897 24.790 1.00 56.31 ? 103 HIS A CD2 1 ATOM 729 C CE1 . HIS A 1 103 ? 4.809 24.397 23.535 1.00 56.37 ? 103 HIS A CE1 1 ATOM 730 N NE2 . HIS A 1 103 ? 6.036 24.768 23.852 1.00 55.53 ? 103 HIS A NE2 1 ATOM 731 N N . THR A 1 104 ? 4.625 21.213 29.499 1.00 57.91 ? 104 THR A N 1 ATOM 732 C CA . THR A 1 104 ? 4.618 20.118 30.471 1.00 58.82 ? 104 THR A CA 1 ATOM 733 C C . THR A 1 104 ? 3.219 19.539 30.652 1.00 60.84 ? 104 THR A C 1 ATOM 734 O O . THR A 1 104 ? 2.223 20.159 30.279 1.00 60.87 ? 104 THR A O 1 ATOM 735 C CB . THR A 1 104 ? 5.143 20.563 31.869 1.00 56.90 ? 104 THR A CB 1 ATOM 736 O OG1 . THR A 1 104 ? 4.340 21.637 32.368 1.00 55.09 ? 104 THR A OG1 1 ATOM 737 C CG2 . THR A 1 104 ? 6.600 20.999 31.797 1.00 53.63 ? 104 THR A CG2 1 ATOM 738 N N . LEU A 1 105 ? 3.152 18.349 31.239 1.00 63.39 ? 105 LEU A N 1 ATOM 739 C CA . LEU A 1 105 ? 1.876 17.679 31.481 1.00 65.79 ? 105 LEU A CA 1 ATOM 740 C C . LEU A 1 105 ? 1.277 18.153 32.811 1.00 66.72 ? 105 LEU A C 1 ATOM 741 O O . LEU A 1 105 ? 2.003 18.602 33.695 1.00 65.56 ? 105 LEU A O 1 ATOM 742 C CB . LEU A 1 105 ? 2.094 16.165 31.496 1.00 64.91 ? 105 LEU A CB 1 ATOM 743 C CG . LEU A 1 105 ? 3.029 15.644 30.394 1.00 64.95 ? 105 LEU A CG 1 ATOM 744 C CD1 . LEU A 1 105 ? 3.280 14.159 30.599 1.00 63.69 ? 105 LEU A CD1 1 ATOM 745 C CD2 . LEU A 1 105 ? 2.435 15.915 29.018 1.00 63.62 ? 105 LEU A CD2 1 ATOM 746 N N . PRO A 1 106 ? -0.058 18.048 32.971 1.00 69.08 ? 106 PRO A N 1 ATOM 747 C CA . PRO A 1 106 ? -0.768 18.471 34.188 1.00 69.61 ? 106 PRO A CA 1 ATOM 748 C C . PRO A 1 106 ? -0.153 18.029 35.509 1.00 69.49 ? 106 PRO A C 1 ATOM 749 O O . PRO A 1 106 ? -0.208 18.764 36.495 1.00 68.07 ? 106 PRO A O 1 ATOM 750 C CB . PRO A 1 106 ? -2.177 17.920 33.982 1.00 68.96 ? 106 PRO A CB 1 ATOM 751 C CG . PRO A 1 106 ? -1.950 16.735 33.114 1.00 70.78 ? 106 PRO A CG 1 ATOM 752 C CD . PRO A 1 106 ? -0.965 17.276 32.107 1.00 70.50 ? 106 PRO A CD 1 ATOM 753 N N . MET A 1 107 ? 0.431 16.840 35.545 1.00 69.99 ? 107 MET A N 1 ATOM 754 C CA . MET A 1 107 ? 1.051 16.402 36.782 1.00 72.30 ? 107 MET A CA 1 ATOM 755 C C . MET A 1 107 ? 2.099 17.439 37.185 1.00 72.08 ? 107 MET A C 1 ATOM 756 O O . MET A 1 107 ? 2.393 17.620 38.370 1.00 70.71 ? 107 MET A O 1 ATOM 757 C CB . MET A 1 107 ? 1.730 15.044 36.612 1.00 74.92 ? 107 MET A CB 1 ATOM 758 C CG . MET A 1 107 ? 2.043 14.375 37.948 1.00 78.76 ? 107 MET A CG 1 ATOM 759 S SD . MET A 1 107 ? 3.686 13.636 38.052 1.00 83.72 ? 107 MET A SD 1 ATOM 760 C CE . MET A 1 107 ? 4.645 15.049 38.739 1.00 83.02 ? 107 MET A CE 1 ATOM 761 N N . GLU A 1 108 ? 2.654 18.122 36.186 1.00 71.53 ? 108 GLU A N 1 ATOM 762 C CA . GLU A 1 108 ? 3.674 19.139 36.424 1.00 71.72 ? 108 GLU A CA 1 ATOM 763 C C . GLU A 1 108 ? 3.115 20.574 36.402 1.00 72.23 ? 108 GLU A C 1 ATOM 764 O O . GLU A 1 108 ? 3.836 21.539 36.675 1.00 70.93 ? 108 GLU A O 1 ATOM 765 C CB . GLU A 1 108 ? 4.814 18.983 35.399 1.00 69.12 ? 108 GLU A CB 1 ATOM 766 C CG . GLU A 1 108 ? 5.694 17.748 35.621 1.00 66.94 ? 108 GLU A CG 1 ATOM 767 C CD . GLU A 1 108 ? 6.812 17.602 34.586 1.00 67.59 ? 108 GLU A CD 1 ATOM 768 O OE1 . GLU A 1 108 ? 6.499 17.355 33.402 1.00 68.26 ? 108 GLU A OE1 1 ATOM 769 O OE2 . GLU A 1 108 ? 8.006 17.732 34.952 1.00 65.95 ? 108 GLU A OE2 1 ATOM 770 N N . LYS A 1 109 ? 1.826 20.701 36.096 1.00 73.40 ? 109 LYS A N 1 ATOM 771 C CA . LYS A 1 109 ? 1.164 22.002 36.036 1.00 74.61 ? 109 LYS A CA 1 ATOM 772 C C . LYS A 1 109 ? 0.555 22.361 37.386 1.00 75.57 ? 109 LYS A C 1 ATOM 773 O O . LYS A 1 109 ? 0.278 23.526 37.673 1.00 74.51 ? 109 LYS A O 1 ATOM 774 C CB . LYS A 1 109 ? 0.046 21.984 34.983 1.00 75.05 ? 109 LYS A CB 1 ATOM 775 C CG . LYS A 1 109 ? 0.483 21.638 33.555 1.00 76.69 ? 109 LYS A CG 1 ATOM 776 C CD . LYS A 1 109 ? 1.272 22.756 32.887 1.00 77.21 ? 109 LYS A CD 1 ATOM 777 C CE . LYS A 1 109 ? 0.437 24.015 32.734 1.00 78.80 ? 109 LYS A CE 1 ATOM 778 N NZ . LYS A 1 109 ? -0.772 23.782 31.894 1.00 79.64 ? 109 LYS A NZ 1 ATOM 779 N N . MET A 1 110 ? 0.340 21.349 38.216 1.00 78.32 ? 110 MET A N 1 ATOM 780 C CA . MET A 1 110 ? -0.265 21.573 39.523 1.00 80.38 ? 110 MET A CA 1 ATOM 781 C C . MET A 1 110 ? 0.740 22.021 40.581 1.00 80.95 ? 110 MET A C 1 ATOM 782 O O . MET A 1 110 ? 0.792 21.473 41.678 1.00 82.24 ? 110 MET A O 1 ATOM 783 C CB . MET A 1 110 ? -0.994 20.311 39.988 1.00 78.95 ? 110 MET A CB 1 ATOM 784 C CG . MET A 1 110 ? -0.092 19.118 40.151 1.00 79.24 ? 110 MET A CG 1 ATOM 785 S SD . MET A 1 110 ? -0.990 17.690 40.729 1.00 81.95 ? 110 MET A SD 1 ATOM 786 C CE . MET A 1 110 ? 0.129 16.354 40.236 1.00 80.30 ? 110 MET A CE 1 ATOM 787 N N . ASP A 1 111 ? 1.547 23.013 40.230 1.00 81.78 ? 111 ASP A N 1 ATOM 788 C CA . ASP A 1 111 ? 2.528 23.576 41.147 1.00 81.97 ? 111 ASP A CA 1 ATOM 789 C C . ASP A 1 111 ? 2.617 25.046 40.776 1.00 80.81 ? 111 ASP A C 1 ATOM 790 O O . ASP A 1 111 ? 3.178 25.865 41.501 1.00 80.20 ? 111 ASP A O 1 ATOM 791 C CB . ASP A 1 111 ? 3.902 22.881 41.012 1.00 83.52 ? 111 ASP A CB 1 ATOM 792 C CG . ASP A 1 111 ? 4.635 23.230 39.716 1.00 84.49 ? 111 ASP A CG 1 ATOM 793 O OD1 . ASP A 1 111 ? 4.190 22.784 38.636 1.00 86.43 ? 111 ASP A OD1 1 ATOM 794 O OD2 . ASP A 1 111 ? 5.666 23.941 39.781 1.00 82.44 ? 111 ASP A OD2 1 ATOM 795 N N . ASP A 1 112 ? 2.020 25.357 39.633 1.00 79.98 ? 112 ASP A N 1 ATOM 796 C CA . ASP A 1 112 ? 1.988 26.704 39.099 1.00 80.65 ? 112 ASP A CA 1 ATOM 797 C C . ASP A 1 112 ? 0.878 27.496 39.772 1.00 80.13 ? 112 ASP A C 1 ATOM 798 O O . ASP A 1 112 ? 1.085 28.617 40.226 1.00 79.63 ? 112 ASP A O 1 ATOM 799 C CB . ASP A 1 112 ? 1.726 26.650 37.592 1.00 81.79 ? 112 ASP A CB 1 ATOM 800 C CG . ASP A 1 112 ? 2.685 25.731 36.867 1.00 81.94 ? 112 ASP A CG 1 ATOM 801 O OD1 . ASP A 1 112 ? 2.510 25.527 35.650 1.00 82.94 ? 112 ASP A OD1 1 ATOM 802 O OD2 . ASP A 1 112 ? 3.616 25.215 37.510 1.00 83.00 ? 112 ASP A OD2 1 ATOM 803 N N . ALA A 1 113 ? -0.306 26.898 39.817 1.00 81.37 ? 113 ALA A N 1 ATOM 804 C CA . ALA A 1 113 ? -1.477 27.525 40.416 1.00 82.72 ? 113 ALA A CA 1 ATOM 805 C C . ALA A 1 113 ? -2.130 26.618 41.462 1.00 83.76 ? 113 ALA A C 1 ATOM 806 O O . ALA A 1 113 ? -2.570 25.510 41.151 1.00 84.07 ? 113 ALA A O 1 ATOM 807 C CB . ALA A 1 113 ? -2.489 27.879 39.321 1.00 81.14 ? 113 ALA A CB 1 ATOM 808 N N . VAL A 1 114 ? -2.185 27.100 42.700 1.00 85.32 ? 114 VAL A N 1 ATOM 809 C CA . VAL A 1 114 ? -2.794 26.359 43.802 1.00 86.49 ? 114 VAL A CA 1 ATOM 810 C C . VAL A 1 114 ? -4.111 27.057 44.134 1.00 87.87 ? 114 VAL A C 1 ATOM 811 O O . VAL A 1 114 ? -4.117 28.191 44.621 1.00 88.02 ? 114 VAL A O 1 ATOM 812 C CB . VAL A 1 114 ? -1.884 26.367 45.044 1.00 86.12 ? 114 VAL A CB 1 ATOM 813 C CG1 . VAL A 1 114 ? -2.421 25.410 46.093 1.00 84.71 ? 114 VAL A CG1 1 ATOM 814 C CG2 . VAL A 1 114 ? -0.471 25.991 44.645 1.00 85.25 ? 114 VAL A CG2 1 ATOM 815 N N . ALA A 1 115 ? -5.220 26.375 43.864 1.00 89.20 ? 115 ALA A N 1 ATOM 816 C CA . ALA A 1 115 ? -6.555 26.927 44.089 1.00 91.77 ? 115 ALA A CA 1 ATOM 817 C C . ALA A 1 115 ? -6.898 27.318 45.529 1.00 93.72 ? 115 ALA A C 1 ATOM 818 O O . ALA A 1 115 ? -6.423 26.703 46.493 1.00 94.07 ? 115 ALA A O 1 ATOM 819 C CB . ALA A 1 115 ? -7.603 25.956 43.560 1.00 91.81 ? 115 ALA A CB 1 ATOM 820 N N . PRO A 1 116 ? -7.745 28.353 45.686 1.00 94.40 ? 116 PRO A N 1 ATOM 821 C CA . PRO A 1 116 ? -8.185 28.864 46.988 1.00 94.34 ? 116 PRO A CA 1 ATOM 822 C C . PRO A 1 116 ? -8.703 27.770 47.913 1.00 94.10 ? 116 PRO A C 1 ATOM 823 O O . PRO A 1 116 ? -9.880 27.422 47.865 1.00 94.61 ? 116 PRO A O 1 ATOM 824 C CB . PRO A 1 116 ? -9.272 29.867 46.609 1.00 94.71 ? 116 PRO A CB 1 ATOM 825 C CG . PRO A 1 116 ? -8.755 30.429 45.322 1.00 94.61 ? 116 PRO A CG 1 ATOM 826 C CD . PRO A 1 116 ? -8.308 29.172 44.595 1.00 94.53 ? 116 PRO A CD 1 ATOM 827 N N . GLY A 1 117 ? -7.821 27.228 48.750 1.00 93.70 ? 117 GLY A N 1 ATOM 828 C CA . GLY A 1 117 ? -8.232 26.185 49.669 1.00 92.85 ? 117 GLY A CA 1 ATOM 829 C C . GLY A 1 117 ? -7.449 24.893 49.550 1.00 92.46 ? 117 GLY A C 1 ATOM 830 O O . GLY A 1 117 ? -7.623 23.988 50.364 1.00 90.48 ? 117 GLY A O 1 ATOM 831 N N . GLN A 1 118 ? -6.590 24.797 48.538 1.00 93.20 ? 118 GLN A N 1 ATOM 832 C CA . GLN A 1 118 ? -5.783 23.592 48.348 1.00 93.47 ? 118 GLN A CA 1 ATOM 833 C C . GLN A 1 118 ? -4.377 23.785 48.905 1.00 93.50 ? 118 GLN A C 1 ATOM 834 O O . GLN A 1 118 ? -3.922 24.916 49.083 1.00 93.25 ? 118 GLN A O 1 ATOM 835 C CB . GLN A 1 118 ? -5.702 23.226 46.863 1.00 92.79 ? 118 GLN A CB 1 ATOM 836 C CG . GLN A 1 118 ? -7.039 22.861 46.233 1.00 92.99 ? 118 GLN A CG 1 ATOM 837 C CD . GLN A 1 118 ? -7.681 21.631 46.859 1.00 93.17 ? 118 GLN A CD 1 ATOM 838 O OE1 . GLN A 1 118 ? -7.120 20.529 46.833 1.00 92.39 ? 118 GLN A OE1 1 ATOM 839 N NE2 . GLN A 1 118 ? -8.871 21.815 47.425 1.00 93.70 ? 118 GLN A NE2 1 ATOM 840 N N . GLU A 1 119 ? -3.694 22.680 49.190 1.00 93.78 ? 119 GLU A N 1 ATOM 841 C CA . GLU A 1 119 ? -2.343 22.757 49.724 1.00 94.88 ? 119 GLU A CA 1 ATOM 842 C C . GLU A 1 119 ? -1.364 21.788 49.063 1.00 94.23 ? 119 GLU A C 1 ATOM 843 O O . GLU A 1 119 ? -1.544 20.571 49.102 1.00 93.77 ? 119 GLU A O 1 ATOM 844 C CB . GLU A 1 119 ? -2.346 22.534 51.249 1.00 96.85 ? 119 GLU A CB 1 ATOM 845 C CG . GLU A 1 119 ? -2.841 21.165 51.728 1.00 99.67 ? 119 GLU A CG 1 ATOM 846 C CD . GLU A 1 119 ? -2.597 20.932 53.223 1.00 100.53 ? 119 GLU A CD 1 ATOM 847 O OE1 . GLU A 1 119 ? -1.426 20.984 53.654 1.00 100.90 ? 119 GLU A OE1 1 ATOM 848 O OE2 . GLU A 1 119 ? -3.574 20.692 53.965 1.00 101.11 ? 119 GLU A OE2 1 ATOM 849 N N . TYR A 1 120 ? -0.327 22.343 48.444 1.00 93.21 ? 120 TYR A N 1 ATOM 850 C CA . TYR A 1 120 ? 0.687 21.526 47.802 1.00 91.94 ? 120 TYR A CA 1 ATOM 851 C C . TYR A 1 120 ? 2.077 21.853 48.315 1.00 89.57 ? 120 TYR A C 1 ATOM 852 O O . TYR A 1 120 ? 2.316 22.935 48.848 1.00 89.31 ? 120 TYR A O 1 ATOM 853 C CB . TYR A 1 120 ? 0.614 21.658 46.282 1.00 95.35 ? 120 TYR A CB 1 ATOM 854 C CG . TYR A 1 120 ? 0.031 20.417 45.648 1.00 99.35 ? 120 TYR A CG 1 ATOM 855 C CD1 . TYR A 1 120 ? 0.032 20.240 44.267 1.00 100.24 ? 120 TYR A CD1 1 ATOM 856 C CD2 . TYR A 1 120 ? -0.479 19.386 46.445 1.00 100.79 ? 120 TYR A CD2 1 ATOM 857 C CE1 . TYR A 1 120 ? -0.455 19.060 43.693 1.00 102.42 ? 120 TYR A CE1 1 ATOM 858 C CE2 . TYR A 1 120 ? -0.966 18.208 45.886 1.00 102.41 ? 120 TYR A CE2 1 ATOM 859 C CZ . TYR A 1 120 ? -0.951 18.045 44.512 1.00 102.79 ? 120 TYR A CZ 1 ATOM 860 O OH . TYR A 1 120 ? -1.416 16.864 43.969 1.00 103.06 ? 120 TYR A OH 1 ATOM 861 N N . THR A 1 121 ? 2.995 20.908 48.148 1.00 86.95 ? 121 THR A N 1 ATOM 862 C CA . THR A 1 121 ? 4.351 21.067 48.660 1.00 84.15 ? 121 THR A CA 1 ATOM 863 C C . THR A 1 121 ? 5.483 21.173 47.632 1.00 80.61 ? 121 THR A C 1 ATOM 864 O O . THR A 1 121 ? 5.829 20.194 46.961 1.00 79.22 ? 121 THR A O 1 ATOM 865 C CB . THR A 1 121 ? 4.671 19.907 49.649 1.00 84.94 ? 121 THR A CB 1 ATOM 866 O OG1 . THR A 1 121 ? 6.016 20.027 50.126 1.00 87.40 ? 121 THR A OG1 1 ATOM 867 C CG2 . THR A 1 121 ? 4.494 18.561 48.970 1.00 83.72 ? 121 THR A CG2 1 ATOM 868 N N . TYR A 1 122 ? 6.063 22.368 47.529 1.00 75.99 ? 122 TYR A N 1 ATOM 869 C CA . TYR A 1 122 ? 7.170 22.606 46.617 1.00 73.14 ? 122 TYR A CA 1 ATOM 870 C C . TYR A 1 122 ? 8.425 21.972 47.208 1.00 73.04 ? 122 TYR A C 1 ATOM 871 O O . TYR A 1 122 ? 8.784 22.253 48.349 1.00 72.26 ? 122 TYR A O 1 ATOM 872 C CB . TYR A 1 122 ? 7.410 24.103 46.430 1.00 69.97 ? 122 TYR A CB 1 ATOM 873 C CG . TYR A 1 122 ? 6.271 24.874 45.790 1.00 69.32 ? 122 TYR A CG 1 ATOM 874 C CD1 . TYR A 1 122 ? 5.228 25.379 46.555 1.00 66.93 ? 122 TYR A CD1 1 ATOM 875 C CD2 . TYR A 1 122 ? 6.274 25.156 44.420 1.00 69.92 ? 122 TYR A CD2 1 ATOM 876 C CE1 . TYR A 1 122 ? 4.221 26.156 45.981 1.00 65.91 ? 122 TYR A CE1 1 ATOM 877 C CE2 . TYR A 1 122 ? 5.266 25.932 43.836 1.00 68.97 ? 122 TYR A CE2 1 ATOM 878 C CZ . TYR A 1 122 ? 4.247 26.434 44.628 1.00 67.41 ? 122 TYR A CZ 1 ATOM 879 O OH . TYR A 1 122 ? 3.289 27.261 44.079 1.00 66.08 ? 122 TYR A OH 1 ATOM 880 N N . GLU A 1 123 ? 9.091 21.127 46.425 1.00 73.81 ? 123 GLU A N 1 ATOM 881 C CA . GLU A 1 123 ? 10.303 20.435 46.861 1.00 74.33 ? 123 GLU A CA 1 ATOM 882 C C . GLU A 1 123 ? 11.545 20.965 46.133 1.00 74.32 ? 123 GLU A C 1 ATOM 883 O O . GLU A 1 123 ? 11.760 20.651 44.963 1.00 75.95 ? 123 GLU A O 1 ATOM 884 C CB . GLU A 1 123 ? 10.131 18.935 46.597 1.00 76.56 ? 123 GLU A CB 1 ATOM 885 C CG . GLU A 1 123 ? 11.273 18.038 47.061 1.00 80.84 ? 123 GLU A CG 1 ATOM 886 C CD . GLU A 1 123 ? 10.899 16.557 47.039 1.00 83.47 ? 123 GLU A CD 1 ATOM 887 O OE1 . GLU A 1 123 ? 11.760 15.716 47.380 1.00 84.31 ? 123 GLU A OE1 1 ATOM 888 O OE2 . GLU A 1 123 ? 9.740 16.234 46.685 1.00 84.65 ? 123 GLU A OE2 1 ATOM 889 N N . TRP A 1 124 ? 12.366 21.756 46.825 1.00 73.67 ? 124 TRP A N 1 ATOM 890 C CA . TRP A 1 124 ? 13.577 22.327 46.224 1.00 73.88 ? 124 TRP A CA 1 ATOM 891 C C . TRP A 1 124 ? 14.892 21.691 46.660 1.00 75.42 ? 124 TRP A C 1 ATOM 892 O O . TRP A 1 124 ? 15.286 21.778 47.822 1.00 76.58 ? 124 TRP A O 1 ATOM 893 C CB . TRP A 1 124 ? 13.670 23.824 46.511 1.00 72.17 ? 124 TRP A CB 1 ATOM 894 C CG . TRP A 1 124 ? 12.472 24.593 46.086 1.00 70.74 ? 124 TRP A CG 1 ATOM 895 C CD1 . TRP A 1 124 ? 11.680 24.345 45.002 1.00 69.32 ? 124 TRP A CD1 1 ATOM 896 C CD2 . TRP A 1 124 ? 11.958 25.780 46.699 1.00 69.19 ? 124 TRP A CD2 1 ATOM 897 N NE1 . TRP A 1 124 ? 10.708 25.308 44.900 1.00 69.63 ? 124 TRP A NE1 1 ATOM 898 C CE2 . TRP A 1 124 ? 10.854 26.202 45.928 1.00 68.96 ? 124 TRP A CE2 1 ATOM 899 C CE3 . TRP A 1 124 ? 12.324 26.529 47.824 1.00 69.59 ? 124 TRP A CE3 1 ATOM 900 C CZ2 . TRP A 1 124 ? 10.110 27.342 46.244 1.00 69.42 ? 124 TRP A CZ2 1 ATOM 901 C CZ3 . TRP A 1 124 ? 11.584 27.664 48.141 1.00 71.11 ? 124 TRP A CZ3 1 ATOM 902 C CH2 . TRP A 1 124 ? 10.487 28.059 47.351 1.00 70.93 ? 124 TRP A CH2 1 ATOM 903 N N . ILE A 1 125 ? 15.585 21.082 45.708 1.00 76.41 ? 125 ILE A N 1 ATOM 904 C CA . ILE A 1 125 ? 16.859 20.439 45.981 1.00 76.51 ? 125 ILE A CA 1 ATOM 905 C C . ILE A 1 125 ? 18.017 21.420 45.820 1.00 76.69 ? 125 ILE A C 1 ATOM 906 O O . ILE A 1 125 ? 18.824 21.279 44.906 1.00 76.56 ? 125 ILE A O 1 ATOM 907 C CB . ILE A 1 125 ? 17.074 19.253 45.023 1.00 77.21 ? 125 ILE A CB 1 ATOM 908 C CG1 . ILE A 1 125 ? 15.904 18.272 45.150 1.00 78.13 ? 125 ILE A CG1 1 ATOM 909 C CG2 . ILE A 1 125 ? 18.401 18.568 45.319 1.00 76.48 ? 125 ILE A CG2 1 ATOM 910 C CD1 . ILE A 1 125 ? 15.964 17.105 44.166 1.00 79.40 ? 125 ILE A CD1 1 ATOM 911 N N . ILE A 1 126 ? 18.094 22.414 46.702 1.00 77.95 ? 126 ILE A N 1 ATOM 912 C CA . ILE A 1 126 ? 19.172 23.404 46.652 1.00 79.78 ? 126 ILE A CA 1 ATOM 913 C C . ILE A 1 126 ? 20.529 22.700 46.630 1.00 81.03 ? 126 ILE A C 1 ATOM 914 O O . ILE A 1 126 ? 20.985 22.176 47.642 1.00 80.86 ? 126 ILE A O 1 ATOM 915 C CB . ILE A 1 126 ? 19.087 24.394 47.859 1.00 79.83 ? 126 ILE A CB 1 ATOM 916 C CG1 . ILE A 1 126 ? 20.479 24.897 48.251 1.00 79.65 ? 126 ILE A CG1 1 ATOM 917 C CG2 . ILE A 1 126 ? 18.399 23.733 49.032 1.00 81.17 ? 126 ILE A CG2 1 ATOM 918 C CD1 . ILE A 1 126 ? 21.163 25.722 47.193 1.00 80.08 ? 126 ILE A CD1 1 ATOM 919 N N . SER A 1 127 ? 21.167 22.705 45.461 1.00 83.09 ? 127 SER A N 1 ATOM 920 C CA . SER A 1 127 ? 22.455 22.039 45.261 1.00 84.76 ? 127 SER A CA 1 ATOM 921 C C . SER A 1 127 ? 23.686 22.911 45.450 1.00 85.62 ? 127 SER A C 1 ATOM 922 O O . SER A 1 127 ? 23.592 24.109 45.703 1.00 85.28 ? 127 SER A O 1 ATOM 923 C CB . SER A 1 127 ? 22.510 21.454 43.861 1.00 85.16 ? 127 SER A CB 1 ATOM 924 O OG . SER A 1 127 ? 22.543 22.503 42.913 1.00 86.65 ? 127 SER A OG 1 ATOM 925 N N . GLU A 1 128 ? 24.848 22.286 45.297 1.00 86.84 ? 128 GLU A N 1 ATOM 926 C CA . GLU A 1 128 ? 26.120 22.976 45.452 1.00 88.63 ? 128 GLU A CA 1 ATOM 927 C C . GLU A 1 128 ? 26.317 24.129 44.486 1.00 87.74 ? 128 GLU A C 1 ATOM 928 O O . GLU A 1 128 ? 26.466 25.269 44.915 1.00 87.41 ? 128 GLU A O 1 ATOM 929 C CB . GLU A 1 128 ? 27.286 21.993 45.300 1.00 91.70 ? 128 GLU A CB 1 ATOM 930 C CG . GLU A 1 128 ? 28.651 22.667 45.118 1.00 96.12 ? 128 GLU A CG 1 ATOM 931 C CD . GLU A 1 128 ? 28.987 23.648 46.238 1.00 99.24 ? 128 GLU A CD 1 ATOM 932 O OE1 . GLU A 1 128 ? 29.132 23.200 47.398 1.00 101.23 ? 128 GLU A OE1 1 ATOM 933 O OE2 . GLU A 1 128 ? 29.104 24.865 45.962 1.00 98.97 ? 128 GLU A OE2 1 ATOM 934 N N . HIS A 1 129 ? 26.326 23.835 43.188 1.00 88.04 ? 129 HIS A N 1 ATOM 935 C CA . HIS A 1 129 ? 26.535 24.870 42.180 1.00 87.74 ? 129 HIS A CA 1 ATOM 936 C C . HIS A 1 129 ? 25.319 25.746 41.940 1.00 87.73 ? 129 HIS A C 1 ATOM 937 O O . HIS A 1 129 ? 25.109 26.230 40.831 1.00 89.20 ? 129 HIS A O 1 ATOM 938 C CB . HIS A 1 129 ? 26.986 24.254 40.849 1.00 87.98 ? 129 HIS A CB 1 ATOM 939 C CG . HIS A 1 129 ? 25.939 23.429 40.162 1.00 88.21 ? 129 HIS A CG 1 ATOM 940 N ND1 . HIS A 1 129 ? 24.592 23.709 40.244 1.00 88.11 ? 129 HIS A ND1 1 ATOM 941 C CD2 . HIS A 1 129 ? 26.053 22.378 39.314 1.00 88.73 ? 129 HIS A CD2 1 ATOM 942 C CE1 . HIS A 1 129 ? 23.921 22.869 39.476 1.00 88.99 ? 129 HIS A CE1 1 ATOM 943 N NE2 . HIS A 1 129 ? 24.784 22.051 38.899 1.00 89.04 ? 129 HIS A NE2 1 ATOM 944 N N . SER A 1 130 ? 24.522 25.948 42.983 1.00 88.04 ? 130 SER A N 1 ATOM 945 C CA . SER A 1 130 ? 23.326 26.780 42.896 1.00 87.54 ? 130 SER A CA 1 ATOM 946 C C . SER A 1 130 ? 23.294 27.711 44.093 1.00 87.06 ? 130 SER A C 1 ATOM 947 O O . SER A 1 130 ? 22.314 28.420 44.315 1.00 85.64 ? 130 SER A O 1 ATOM 948 C CB . SER A 1 130 ? 22.068 25.908 42.888 1.00 88.33 ? 130 SER A CB 1 ATOM 949 O OG . SER A 1 130 ? 21.982 25.112 44.058 1.00 88.19 ? 130 SER A OG 1 ATOM 950 N N . GLY A 1 131 ? 24.390 27.702 44.849 1.00 87.92 ? 131 GLY A N 1 ATOM 951 C CA . GLY A 1 131 ? 24.497 28.528 46.035 1.00 91.07 ? 131 GLY A CA 1 ATOM 952 C C . GLY A 1 131 ? 25.617 29.552 46.003 1.00 92.91 ? 131 GLY A C 1 ATOM 953 O O . GLY A 1 131 ? 26.216 29.776 44.957 1.00 93.72 ? 131 GLY A O 1 ATOM 954 N N . PRO A 1 132 ? 25.933 30.181 47.150 1.00 94.48 ? 132 PRO A N 1 ATOM 955 C CA . PRO A 1 132 ? 26.980 31.197 47.287 1.00 95.27 ? 132 PRO A CA 1 ATOM 956 C C . PRO A 1 132 ? 28.291 30.824 46.630 1.00 95.87 ? 132 PRO A C 1 ATOM 957 O O . PRO A 1 132 ? 28.571 29.654 46.396 1.00 96.62 ? 132 PRO A O 1 ATOM 958 C CB . PRO A 1 132 ? 27.134 31.335 48.799 1.00 95.44 ? 132 PRO A CB 1 ATOM 959 C CG . PRO A 1 132 ? 25.777 31.034 49.304 1.00 95.87 ? 132 PRO A CG 1 ATOM 960 C CD . PRO A 1 132 ? 25.385 29.835 48.473 1.00 95.48 ? 132 PRO A CD 1 ATOM 961 N N . THR A 1 133 ? 29.090 31.837 46.327 1.00 96.80 ? 133 THR A N 1 ATOM 962 C CA . THR A 1 133 ? 30.393 31.616 45.725 1.00 98.35 ? 133 THR A CA 1 ATOM 963 C C . THR A 1 133 ? 31.323 31.465 46.926 1.00 98.97 ? 133 THR A C 1 ATOM 964 O O . THR A 1 133 ? 30.995 30.768 47.888 1.00 99.15 ? 133 THR A O 1 ATOM 965 C CB . THR A 1 133 ? 30.837 32.833 44.869 1.00 98.35 ? 133 THR A CB 1 ATOM 966 O OG1 . THR A 1 133 ? 29.798 33.178 43.943 1.00 98.54 ? 133 THR A OG1 1 ATOM 967 C CG2 . THR A 1 133 ? 32.096 32.504 44.083 1.00 99.34 ? 133 THR A CG2 1 ATOM 968 N N . HIS A 1 134 ? 32.471 32.123 46.874 1.00 99.14 ? 134 HIS A N 1 ATOM 969 C CA . HIS A 1 134 ? 33.424 32.077 47.968 1.00 99.80 ? 134 HIS A CA 1 ATOM 970 C C . HIS A 1 134 ? 33.809 33.507 48.305 1.00 99.30 ? 134 HIS A C 1 ATOM 971 O O . HIS A 1 134 ? 34.184 33.820 49.434 1.00 99.19 ? 134 HIS A O 1 ATOM 972 C CB . HIS A 1 134 ? 34.670 31.291 47.565 1.00 101.00 ? 134 HIS A CB 1 ATOM 973 C CG . HIS A 1 134 ? 35.841 31.535 48.462 1.00 104.20 ? 134 HIS A CG 1 ATOM 974 N ND1 . HIS A 1 134 ? 35.772 31.382 49.831 1.00 105.87 ? 134 HIS A ND1 1 ATOM 975 C CD2 . HIS A 1 134 ? 37.097 31.961 48.193 1.00 105.26 ? 134 HIS A CD2 1 ATOM 976 C CE1 . HIS A 1 134 ? 36.935 31.706 50.367 1.00 105.99 ? 134 HIS A CE1 1 ATOM 977 N NE2 . HIS A 1 134 ? 37.757 32.061 49.395 1.00 106.72 ? 134 HIS A NE2 1 ATOM 978 N N . ASP A 1 135 ? 33.687 34.370 47.305 1.00 98.77 ? 135 ASP A N 1 ATOM 979 C CA . ASP A 1 135 ? 34.028 35.779 47.422 1.00 98.02 ? 135 ASP A CA 1 ATOM 980 C C . ASP A 1 135 ? 32.788 36.612 47.766 1.00 97.69 ? 135 ASP A C 1 ATOM 981 O O . ASP A 1 135 ? 32.847 37.840 47.818 1.00 96.93 ? 135 ASP A O 1 ATOM 982 C CB . ASP A 1 135 ? 34.632 36.245 46.093 1.00 98.23 ? 135 ASP A CB 1 ATOM 983 C CG . ASP A 1 135 ? 35.396 37.545 46.214 1.00 98.91 ? 135 ASP A CG 1 ATOM 984 O OD1 . ASP A 1 135 ? 34.805 38.553 46.655 1.00 99.28 ? 135 ASP A OD1 1 ATOM 985 O OD2 . ASP A 1 135 ? 36.593 37.558 45.859 1.00 98.86 ? 135 ASP A OD2 1 ATOM 986 N N . ASP A 1 136 ? 31.670 35.937 48.011 1.00 97.97 ? 136 ASP A N 1 ATOM 987 C CA . ASP A 1 136 ? 30.417 36.616 48.337 1.00 98.62 ? 136 ASP A CA 1 ATOM 988 C C . ASP A 1 136 ? 29.975 36.349 49.777 1.00 98.05 ? 136 ASP A C 1 ATOM 989 O O . ASP A 1 136 ? 30.524 35.475 50.454 1.00 97.68 ? 136 ASP A O 1 ATOM 990 C CB . ASP A 1 136 ? 29.326 36.164 47.363 1.00 100.41 ? 136 ASP A CB 1 ATOM 991 C CG . ASP A 1 136 ? 29.090 34.670 47.411 1.00 102.11 ? 136 ASP A CG 1 ATOM 992 O OD1 . ASP A 1 136 ? 30.083 33.913 47.416 1.00 102.04 ? 136 ASP A OD1 1 ATOM 993 O OD2 . ASP A 1 136 ? 27.915 34.250 47.437 1.00 104.13 ? 136 ASP A OD2 1 ATOM 994 N N . PRO A 1 137 ? 28.973 37.102 50.264 1.00 97.22 ? 137 PRO A N 1 ATOM 995 C CA . PRO A 1 137 ? 28.466 36.937 51.632 1.00 96.27 ? 137 PRO A CA 1 ATOM 996 C C . PRO A 1 137 ? 28.324 35.480 52.077 1.00 95.05 ? 137 PRO A C 1 ATOM 997 O O . PRO A 1 137 ? 28.268 34.572 51.254 1.00 94.75 ? 137 PRO A O 1 ATOM 998 C CB . PRO A 1 137 ? 27.135 37.673 51.585 1.00 96.00 ? 137 PRO A CB 1 ATOM 999 C CG . PRO A 1 137 ? 27.465 38.832 50.696 1.00 96.28 ? 137 PRO A CG 1 ATOM 1000 C CD . PRO A 1 137 ? 28.244 38.178 49.567 1.00 96.51 ? 137 PRO A CD 1 ATOM 1001 N N . PRO A 1 138 ? 28.284 35.241 53.396 1.00 94.67 ? 138 PRO A N 1 ATOM 1002 C CA . PRO A 1 138 ? 28.150 33.872 53.902 1.00 93.78 ? 138 PRO A CA 1 ATOM 1003 C C . PRO A 1 138 ? 26.803 33.285 53.520 1.00 92.55 ? 138 PRO A C 1 ATOM 1004 O O . PRO A 1 138 ? 26.619 32.069 53.526 1.00 92.16 ? 138 PRO A O 1 ATOM 1005 C CB . PRO A 1 138 ? 28.304 34.044 55.409 1.00 93.89 ? 138 PRO A CB 1 ATOM 1006 C CG . PRO A 1 138 ? 29.189 35.256 55.519 1.00 93.67 ? 138 PRO A CG 1 ATOM 1007 C CD . PRO A 1 138 ? 28.568 36.173 54.499 1.00 94.29 ? 138 PRO A CD 1 ATOM 1008 N N . CYS A 1 139 ? 25.857 34.161 53.199 1.00 91.52 ? 139 CYS A N 1 ATOM 1009 C CA . CYS A 1 139 ? 24.538 33.708 52.796 1.00 91.11 ? 139 CYS A CA 1 ATOM 1010 C C . CYS A 1 139 ? 23.872 34.635 51.783 1.00 88.82 ? 139 CYS A C 1 ATOM 1011 O O . CYS A 1 139 ? 23.649 35.814 52.055 1.00 88.58 ? 139 CYS A O 1 ATOM 1012 C CB . CYS A 1 139 ? 23.619 33.542 54.009 1.00 92.69 ? 139 CYS A CB 1 ATOM 1013 S SG . CYS A 1 139 ? 22.266 32.394 53.605 1.00 97.61 ? 139 CYS A SG 1 ATOM 1014 N N . LEU A 1 140 ? 23.551 34.086 50.616 1.00 85.78 ? 140 LEU A N 1 ATOM 1015 C CA . LEU A 1 140 ? 22.906 34.848 49.556 1.00 83.74 ? 140 LEU A CA 1 ATOM 1016 C C . LEU A 1 140 ? 21.443 35.150 49.867 1.00 82.54 ? 140 LEU A C 1 ATOM 1017 O O . LEU A 1 140 ? 20.724 34.311 50.418 1.00 82.84 ? 140 LEU A O 1 ATOM 1018 C CB . LEU A 1 140 ? 22.996 34.084 48.239 1.00 82.18 ? 140 LEU A CB 1 ATOM 1019 C CG . LEU A 1 140 ? 24.423 33.899 47.738 1.00 81.09 ? 140 LEU A CG 1 ATOM 1020 C CD1 . LEU A 1 140 ? 24.406 33.012 46.510 1.00 80.89 ? 140 LEU A CD1 1 ATOM 1021 C CD2 . LEU A 1 140 ? 25.041 35.259 47.429 1.00 79.79 ? 140 LEU A CD2 1 ATOM 1022 N N . THR A 1 141 ? 21.003 36.348 49.500 1.00 80.33 ? 141 THR A N 1 ATOM 1023 C CA . THR A 1 141 ? 19.633 36.749 49.750 1.00 79.42 ? 141 THR A CA 1 ATOM 1024 C C . THR A 1 141 ? 18.817 36.810 48.468 1.00 77.95 ? 141 THR A C 1 ATOM 1025 O O . THR A 1 141 ? 19.201 37.459 47.497 1.00 77.53 ? 141 THR A O 1 ATOM 1026 C CB . THR A 1 141 ? 19.570 38.130 50.425 1.00 81.26 ? 141 THR A CB 1 ATOM 1027 O OG1 . THR A 1 141 ? 20.478 38.160 51.530 1.00 83.86 ? 141 THR A OG1 1 ATOM 1028 C CG2 . THR A 1 141 ? 18.162 38.408 50.942 1.00 80.93 ? 141 THR A CG2 1 ATOM 1029 N N . HIS A 1 142 ? 17.685 36.122 48.477 1.00 76.23 ? 142 HIS A N 1 ATOM 1030 C CA . HIS A 1 142 ? 16.797 36.106 47.333 1.00 74.44 ? 142 HIS A CA 1 ATOM 1031 C C . HIS A 1 142 ? 15.412 36.420 47.837 1.00 74.49 ? 142 HIS A C 1 ATOM 1032 O O . HIS A 1 142 ? 15.235 36.713 49.020 1.00 73.82 ? 142 HIS A O 1 ATOM 1033 C CB . HIS A 1 142 ? 16.825 34.743 46.642 1.00 72.38 ? 142 HIS A CB 1 ATOM 1034 C CG . HIS A 1 142 ? 18.139 34.434 45.997 1.00 72.58 ? 142 HIS A CG 1 ATOM 1035 N ND1 . HIS A 1 142 ? 18.839 35.366 45.257 1.00 71.30 ? 142 HIS A ND1 1 ATOM 1036 C CD2 . HIS A 1 142 ? 18.889 33.307 45.992 1.00 71.08 ? 142 HIS A CD2 1 ATOM 1037 C CE1 . HIS A 1 142 ? 19.965 34.826 44.829 1.00 71.64 ? 142 HIS A CE1 1 ATOM 1038 N NE2 . HIS A 1 142 ? 20.020 33.578 45.261 1.00 71.99 ? 142 HIS A NE2 1 ATOM 1039 N N . ILE A 1 143 ? 14.429 36.358 46.946 1.00 74.82 ? 143 ILE A N 1 ATOM 1040 C CA . ILE A 1 143 ? 13.058 36.671 47.316 1.00 74.58 ? 143 ILE A CA 1 ATOM 1041 C C . ILE A 1 143 ? 12.074 35.748 46.610 1.00 75.74 ? 143 ILE A C 1 ATOM 1042 O O . ILE A 1 143 ? 12.429 35.094 45.630 1.00 76.10 ? 143 ILE A O 1 ATOM 1043 C CB . ILE A 1 143 ? 12.741 38.152 46.960 1.00 73.21 ? 143 ILE A CB 1 ATOM 1044 C CG1 . ILE A 1 143 ? 12.451 38.306 45.474 1.00 72.32 ? 143 ILE A CG1 1 ATOM 1045 C CG2 . ILE A 1 143 ? 13.940 39.025 47.251 1.00 71.67 ? 143 ILE A CG2 1 ATOM 1046 C CD1 . ILE A 1 143 ? 11.006 38.111 45.118 1.00 74.81 ? 143 ILE A CD1 1 ATOM 1047 N N . TYR A 1 144 ? 10.848 35.668 47.126 1.00 76.88 ? 144 TYR A N 1 ATOM 1048 C CA . TYR A 1 144 ? 9.814 34.851 46.493 1.00 77.89 ? 144 TYR A CA 1 ATOM 1049 C C . TYR A 1 144 ? 8.507 35.619 46.496 1.00 76.19 ? 144 TYR A C 1 ATOM 1050 O O . TYR A 1 144 ? 8.359 36.609 47.199 1.00 75.50 ? 144 TYR A O 1 ATOM 1051 C CB . TYR A 1 144 ? 9.652 33.481 47.170 1.00 80.55 ? 144 TYR A CB 1 ATOM 1052 C CG . TYR A 1 144 ? 8.938 33.467 48.505 1.00 87.34 ? 144 TYR A CG 1 ATOM 1053 C CD1 . TYR A 1 144 ? 7.573 33.756 48.600 1.00 89.40 ? 144 TYR A CD1 1 ATOM 1054 C CD2 . TYR A 1 144 ? 9.624 33.133 49.678 1.00 88.59 ? 144 TYR A CD2 1 ATOM 1055 C CE1 . TYR A 1 144 ? 6.910 33.711 49.828 1.00 90.23 ? 144 TYR A CE1 1 ATOM 1056 C CE2 . TYR A 1 144 ? 8.972 33.084 50.906 1.00 90.21 ? 144 TYR A CE2 1 ATOM 1057 C CZ . TYR A 1 144 ? 7.618 33.373 50.973 1.00 90.92 ? 144 TYR A CZ 1 ATOM 1058 O OH . TYR A 1 144 ? 6.977 33.311 52.185 1.00 91.69 ? 144 TYR A OH 1 ATOM 1059 N N . TYR A 1 145 ? 7.567 35.165 45.685 1.00 75.48 ? 145 TYR A N 1 ATOM 1060 C CA . TYR A 1 145 ? 6.284 35.828 45.556 1.00 74.63 ? 145 TYR A CA 1 ATOM 1061 C C . TYR A 1 145 ? 5.412 34.899 44.744 1.00 72.81 ? 145 TYR A C 1 ATOM 1062 O O . TYR A 1 145 ? 5.834 33.788 44.420 1.00 72.76 ? 145 TYR A O 1 ATOM 1063 C CB . TYR A 1 145 ? 6.454 37.175 44.842 1.00 76.03 ? 145 TYR A CB 1 ATOM 1064 C CG . TYR A 1 145 ? 7.256 37.105 43.559 1.00 78.87 ? 145 TYR A CG 1 ATOM 1065 C CD1 . TYR A 1 145 ? 8.539 36.553 43.541 1.00 80.48 ? 145 TYR A CD1 1 ATOM 1066 C CD2 . TYR A 1 145 ? 6.731 37.578 42.359 1.00 81.19 ? 145 TYR A CD2 1 ATOM 1067 C CE1 . TYR A 1 145 ? 9.280 36.463 42.366 1.00 82.22 ? 145 TYR A CE1 1 ATOM 1068 C CE2 . TYR A 1 145 ? 7.465 37.496 41.172 1.00 83.23 ? 145 TYR A CE2 1 ATOM 1069 C CZ . TYR A 1 145 ? 8.738 36.933 41.184 1.00 84.32 ? 145 TYR A CZ 1 ATOM 1070 O OH . TYR A 1 145 ? 9.459 36.820 40.011 1.00 85.90 ? 145 TYR A OH 1 ATOM 1071 N N . SER A 1 146 ? 4.202 35.337 44.417 1.00 70.12 ? 146 SER A N 1 ATOM 1072 C CA . SER A 1 146 ? 3.300 34.487 43.656 1.00 67.20 ? 146 SER A CA 1 ATOM 1073 C C . SER A 1 146 ? 3.334 34.900 42.198 1.00 66.62 ? 146 SER A C 1 ATOM 1074 O O . SER A 1 146 ? 3.132 36.075 41.873 1.00 65.20 ? 146 SER A O 1 ATOM 1075 C CB . SER A 1 146 ? 1.875 34.585 44.213 1.00 65.72 ? 146 SER A CB 1 ATOM 1076 O OG . SER A 1 146 ? 1.066 33.498 43.777 1.00 60.87 ? 146 SER A OG 1 ATOM 1077 N N . TYR A 1 147 ? 3.598 33.927 41.325 1.00 65.33 ? 147 TYR A N 1 ATOM 1078 C CA . TYR A 1 147 ? 3.677 34.190 39.895 1.00 65.41 ? 147 TYR A CA 1 ATOM 1079 C C . TYR A 1 147 ? 2.301 34.206 39.243 1.00 65.06 ? 147 TYR A C 1 ATOM 1080 O O . TYR A 1 147 ? 2.093 34.929 38.270 1.00 67.18 ? 147 TYR A O 1 ATOM 1081 C CB . TYR A 1 147 ? 4.568 33.147 39.185 1.00 65.66 ? 147 TYR A CB 1 ATOM 1082 C CG . TYR A 1 147 ? 4.906 33.522 37.747 1.00 65.36 ? 147 TYR A CG 1 ATOM 1083 C CD1 . TYR A 1 147 ? 5.894 34.467 37.462 1.00 64.61 ? 147 TYR A CD1 1 ATOM 1084 C CD2 . TYR A 1 147 ? 4.177 32.999 36.677 1.00 65.31 ? 147 TYR A CD2 1 ATOM 1085 C CE1 . TYR A 1 147 ? 6.140 34.887 36.153 1.00 63.81 ? 147 TYR A CE1 1 ATOM 1086 C CE2 . TYR A 1 147 ? 4.415 33.416 35.362 1.00 63.65 ? 147 TYR A CE2 1 ATOM 1087 C CZ . TYR A 1 147 ? 5.392 34.364 35.107 1.00 63.32 ? 147 TYR A CZ 1 ATOM 1088 O OH . TYR A 1 147 ? 5.580 34.825 33.818 1.00 62.31 ? 147 TYR A OH 1 ATOM 1089 N N . VAL A 1 148 ? 1.367 33.422 39.781 1.00 63.89 ? 148 VAL A N 1 ATOM 1090 C CA . VAL A 1 148 ? 0.012 33.325 39.235 1.00 62.60 ? 148 VAL A CA 1 ATOM 1091 C C . VAL A 1 148 ? -0.523 34.643 38.699 1.00 62.26 ? 148 VAL A C 1 ATOM 1092 O O . VAL A 1 148 ? -1.375 34.667 37.813 1.00 61.57 ? 148 VAL A O 1 ATOM 1093 C CB . VAL A 1 148 ? -0.947 32.751 40.277 1.00 63.37 ? 148 VAL A CB 1 ATOM 1094 C CG1 . VAL A 1 148 ? -2.375 32.806 39.764 1.00 62.88 ? 148 VAL A CG1 1 ATOM 1095 C CG2 . VAL A 1 148 ? -0.548 31.308 40.576 1.00 61.96 ? 148 VAL A CG2 1 ATOM 1096 N N . ASN A 1 149 ? -0.019 35.733 39.261 1.00 62.42 ? 149 ASN A N 1 ATOM 1097 C CA . ASN A 1 149 ? -0.343 37.085 38.835 1.00 62.84 ? 149 ASN A CA 1 ATOM 1098 C C . ASN A 1 149 ? 0.720 37.934 39.503 1.00 63.49 ? 149 ASN A C 1 ATOM 1099 O O . ASN A 1 149 ? 0.798 37.994 40.719 1.00 64.69 ? 149 ASN A O 1 ATOM 1100 C CB . ASN A 1 149 ? -1.742 37.514 39.269 1.00 63.13 ? 149 ASN A CB 1 ATOM 1101 C CG . ASN A 1 149 ? -2.166 38.827 38.615 1.00 64.76 ? 149 ASN A CG 1 ATOM 1102 O OD1 . ASN A 1 149 ? -3.357 39.097 38.444 1.00 65.68 ? 149 ASN A OD1 1 ATOM 1103 N ND2 . ASN A 1 149 ? -1.183 39.653 38.247 1.00 61.85 ? 149 ASN A ND2 1 ATOM 1104 N N . LEU A 1 150 ? 1.555 38.576 38.701 1.00 64.18 ? 150 LEU A N 1 ATOM 1105 C CA . LEU A 1 150 ? 2.648 39.363 39.238 1.00 64.55 ? 150 LEU A CA 1 ATOM 1106 C C . LEU A 1 150 ? 2.297 40.722 39.816 1.00 64.21 ? 150 LEU A C 1 ATOM 1107 O O . LEU A 1 150 ? 2.769 41.068 40.893 1.00 63.45 ? 150 LEU A O 1 ATOM 1108 C CB . LEU A 1 150 ? 3.742 39.526 38.174 1.00 65.18 ? 150 LEU A CB 1 ATOM 1109 C CG . LEU A 1 150 ? 4.422 38.242 37.688 1.00 65.92 ? 150 LEU A CG 1 ATOM 1110 C CD1 . LEU A 1 150 ? 5.501 38.592 36.671 1.00 66.61 ? 150 LEU A CD1 1 ATOM 1111 C CD2 . LEU A 1 150 ? 5.026 37.484 38.868 1.00 67.04 ? 150 LEU A CD2 1 ATOM 1112 N N . VAL A 1 151 ? 1.486 41.497 39.108 1.00 64.53 ? 151 VAL A N 1 ATOM 1113 C CA . VAL A 1 151 ? 1.127 42.822 39.593 1.00 66.20 ? 151 VAL A CA 1 ATOM 1114 C C . VAL A 1 151 ? 0.184 42.787 40.795 1.00 68.36 ? 151 VAL A C 1 ATOM 1115 O O . VAL A 1 151 ? 0.277 43.629 41.684 1.00 71.53 ? 151 VAL A O 1 ATOM 1116 C CB . VAL A 1 151 ? 0.497 43.667 38.482 1.00 64.39 ? 151 VAL A CB 1 ATOM 1117 C CG1 . VAL A 1 151 ? 0.123 45.037 39.029 1.00 61.41 ? 151 VAL A CG1 1 ATOM 1118 C CG2 . VAL A 1 151 ? 1.474 43.796 37.324 1.00 62.75 ? 151 VAL A CG2 1 ATOM 1119 N N . GLU A 1 152 ? -0.722 41.818 40.824 1.00 69.60 ? 152 GLU A N 1 ATOM 1120 C CA . GLU A 1 152 ? -1.653 41.691 41.937 1.00 69.95 ? 152 GLU A CA 1 ATOM 1121 C C . GLU A 1 152 ? -0.916 41.123 43.142 1.00 69.43 ? 152 GLU A C 1 ATOM 1122 O O . GLU A 1 152 ? -0.402 41.865 43.976 1.00 69.61 ? 152 GLU A O 1 ATOM 1123 C CB . GLU A 1 152 ? -2.803 40.744 41.582 1.00 72.97 ? 152 GLU A CB 1 ATOM 1124 C CG . GLU A 1 152 ? -4.166 41.396 41.508 1.00 75.67 ? 152 GLU A CG 1 ATOM 1125 C CD . GLU A 1 152 ? -4.423 42.053 40.170 1.00 78.55 ? 152 GLU A CD 1 ATOM 1126 O OE1 . GLU A 1 152 ? -3.590 42.882 39.734 1.00 80.24 ? 152 GLU A OE1 1 ATOM 1127 O OE2 . GLU A 1 152 ? -5.465 41.736 39.558 1.00 79.82 ? 152 GLU A OE2 1 ATOM 1128 N N . ASP A 1 153 ? -0.861 39.795 43.201 1.00 67.80 ? 153 ASP A N 1 ATOM 1129 C CA . ASP A 1 153 ? -0.220 39.072 44.292 1.00 67.33 ? 153 ASP A CA 1 ATOM 1130 C C . ASP A 1 153 ? 0.747 39.895 45.149 1.00 67.60 ? 153 ASP A C 1 ATOM 1131 O O . ASP A 1 153 ? 0.510 40.064 46.352 1.00 67.02 ? 153 ASP A O 1 ATOM 1132 C CB . ASP A 1 153 ? 0.480 37.814 43.756 1.00 65.66 ? 153 ASP A CB 1 ATOM 1133 C CG . ASP A 1 153 ? -0.498 36.819 43.128 1.00 65.82 ? 153 ASP A CG 1 ATOM 1134 O OD1 . ASP A 1 153 ? -0.082 35.679 42.822 1.00 65.29 ? 153 ASP A OD1 1 ATOM 1135 O OD2 . ASP A 1 153 ? -1.681 37.171 42.929 1.00 64.00 ? 153 ASP A OD2 1 ATOM 1136 N N . PHE A 1 154 ? 1.821 40.410 44.551 1.00 67.09 ? 154 PHE A N 1 ATOM 1137 C CA . PHE A 1 154 ? 2.783 41.203 45.317 1.00 67.05 ? 154 PHE A CA 1 ATOM 1138 C C . PHE A 1 154 ? 2.090 42.333 46.051 1.00 66.21 ? 154 PHE A C 1 ATOM 1139 O O . PHE A 1 154 ? 2.125 42.398 47.274 1.00 65.36 ? 154 PHE A O 1 ATOM 1140 C CB . PHE A 1 154 ? 3.867 41.806 44.418 1.00 67.92 ? 154 PHE A CB 1 ATOM 1141 C CG . PHE A 1 154 ? 4.500 43.056 44.990 1.00 67.49 ? 154 PHE A CG 1 ATOM 1142 C CD1 . PHE A 1 154 ? 5.095 43.040 46.254 1.00 66.43 ? 154 PHE A CD1 1 ATOM 1143 C CD2 . PHE A 1 154 ? 4.442 44.261 44.294 1.00 66.41 ? 154 PHE A CD2 1 ATOM 1144 C CE1 . PHE A 1 154 ? 5.614 44.205 46.819 1.00 65.23 ? 154 PHE A CE1 1 ATOM 1145 C CE2 . PHE A 1 154 ? 4.959 45.430 44.852 1.00 67.60 ? 154 PHE A CE2 1 ATOM 1146 C CZ . PHE A 1 154 ? 5.545 45.401 46.120 1.00 66.56 ? 154 PHE A CZ 1 ATOM 1147 N N . ASN A 1 155 ? 1.482 43.231 45.283 1.00 66.48 ? 155 ASN A N 1 ATOM 1148 C CA . ASN A 1 155 ? 0.773 44.382 45.828 1.00 66.39 ? 155 ASN A CA 1 ATOM 1149 C C . ASN A 1 155 ? -0.177 44.012 46.966 1.00 66.87 ? 155 ASN A C 1 ATOM 1150 O O . ASN A 1 155 ? -0.208 44.684 48.004 1.00 67.33 ? 155 ASN A O 1 ATOM 1151 C CB . ASN A 1 155 ? 0.018 45.092 44.700 1.00 64.03 ? 155 ASN A CB 1 ATOM 1152 C CG . ASN A 1 155 ? 0.882 46.114 43.987 1.00 61.99 ? 155 ASN A CG 1 ATOM 1153 O OD1 . ASN A 1 155 ? 0.754 46.324 42.785 1.00 56.31 ? 155 ASN A OD1 1 ATOM 1154 N ND2 . ASN A 1 155 ? 1.766 46.770 44.740 1.00 62.44 ? 155 ASN A ND2 1 ATOM 1155 N N . SER A 1 156 ? -0.937 42.936 46.775 1.00 66.77 ? 156 SER A N 1 ATOM 1156 C CA . SER A 1 156 ? -1.875 42.465 47.793 1.00 66.62 ? 156 SER A CA 1 ATOM 1157 C C . SER A 1 156 ? -1.125 41.996 49.050 1.00 64.24 ? 156 SER A C 1 ATOM 1158 O O . SER A 1 156 ? -1.694 41.326 49.907 1.00 60.84 ? 156 SER A O 1 ATOM 1159 C CB . SER A 1 156 ? -2.740 41.323 47.230 1.00 68.21 ? 156 SER A CB 1 ATOM 1160 O OG . SER A 1 156 ? -3.718 40.884 48.165 1.00 69.07 ? 156 SER A OG 1 ATOM 1161 N N . GLY A 1 157 ? 0.158 42.348 49.133 1.00 63.74 ? 157 GLY A N 1 ATOM 1162 C CA . GLY A 1 157 ? 0.974 41.989 50.280 1.00 64.56 ? 157 GLY A CA 1 ATOM 1163 C C . GLY A 1 157 ? 1.848 40.748 50.205 1.00 64.24 ? 157 GLY A C 1 ATOM 1164 O O . GLY A 1 157 ? 2.645 40.504 51.108 1.00 63.99 ? 157 GLY A O 1 ATOM 1165 N N . LEU A 1 158 ? 1.711 39.964 49.142 1.00 65.41 ? 158 LEU A N 1 ATOM 1166 C CA . LEU A 1 158 ? 2.493 38.741 48.981 1.00 65.98 ? 158 LEU A CA 1 ATOM 1167 C C . LEU A 1 158 ? 3.963 39.007 48.642 1.00 67.51 ? 158 LEU A C 1 ATOM 1168 O O . LEU A 1 158 ? 4.265 39.845 47.791 1.00 68.67 ? 158 LEU A O 1 ATOM 1169 C CB . LEU A 1 158 ? 1.846 37.884 47.903 1.00 64.60 ? 158 LEU A CB 1 ATOM 1170 C CG . LEU A 1 158 ? 0.451 37.412 48.295 1.00 62.83 ? 158 LEU A CG 1 ATOM 1171 C CD1 . LEU A 1 158 ? -0.308 36.912 47.070 1.00 62.57 ? 158 LEU A CD1 1 ATOM 1172 C CD2 . LEU A 1 158 ? 0.586 36.324 49.357 1.00 61.02 ? 158 LEU A CD2 1 ATOM 1173 N N . ILE A 1 159 ? 4.865 38.291 49.317 1.00 67.88 ? 159 ILE A N 1 ATOM 1174 C CA . ILE A 1 159 ? 6.309 38.434 49.114 1.00 69.90 ? 159 ILE A CA 1 ATOM 1175 C C . ILE A 1 159 ? 7.051 37.749 50.269 1.00 71.75 ? 159 ILE A C 1 ATOM 1176 O O . ILE A 1 159 ? 6.438 37.436 51.282 1.00 73.82 ? 159 ILE A O 1 ATOM 1177 C CB . ILE A 1 159 ? 6.705 39.918 49.044 1.00 69.55 ? 159 ILE A CB 1 ATOM 1178 C CG1 . ILE A 1 159 ? 8.146 40.056 48.565 1.00 70.87 ? 159 ILE A CG1 1 ATOM 1179 C CG2 . ILE A 1 159 ? 6.521 40.564 50.392 1.00 69.40 ? 159 ILE A CG2 1 ATOM 1180 C CD1 . ILE A 1 159 ? 8.512 41.475 48.176 1.00 72.45 ? 159 ILE A CD1 1 ATOM 1181 N N . GLY A 1 160 ? 8.354 37.503 50.132 1.00 73.37 ? 160 GLY A N 1 ATOM 1182 C CA . GLY A 1 160 ? 9.073 36.835 51.211 1.00 75.84 ? 160 GLY A CA 1 ATOM 1183 C C . GLY A 1 160 ? 10.516 36.439 50.926 1.00 77.64 ? 160 GLY A C 1 ATOM 1184 O O . GLY A 1 160 ? 10.785 35.754 49.943 1.00 77.83 ? 160 GLY A O 1 ATOM 1185 N N . PRO A 1 161 ? 11.467 36.830 51.794 1.00 78.93 ? 161 PRO A N 1 ATOM 1186 C CA . PRO A 1 161 ? 12.905 36.552 51.680 1.00 78.58 ? 161 PRO A CA 1 ATOM 1187 C C . PRO A 1 161 ? 13.293 35.088 51.676 1.00 77.82 ? 161 PRO A C 1 ATOM 1188 O O . PRO A 1 161 ? 12.696 34.279 52.383 1.00 78.84 ? 161 PRO A O 1 ATOM 1189 C CB . PRO A 1 161 ? 13.496 37.266 52.893 1.00 79.80 ? 161 PRO A CB 1 ATOM 1190 C CG . PRO A 1 161 ? 12.497 38.350 53.185 1.00 80.56 ? 161 PRO A CG 1 ATOM 1191 C CD . PRO A 1 161 ? 11.198 37.630 52.999 1.00 80.11 ? 161 PRO A CD 1 ATOM 1192 N N . LEU A 1 162 ? 14.308 34.760 50.882 1.00 76.46 ? 162 LEU A N 1 ATOM 1193 C CA . LEU A 1 162 ? 14.818 33.397 50.804 1.00 76.02 ? 162 LEU A CA 1 ATOM 1194 C C . LEU A 1 162 ? 16.325 33.518 51.005 1.00 76.37 ? 162 LEU A C 1 ATOM 1195 O O . LEU A 1 162 ? 16.948 34.454 50.506 1.00 75.72 ? 162 LEU A O 1 ATOM 1196 C CB . LEU A 1 162 ? 14.488 32.772 49.442 1.00 76.31 ? 162 LEU A CB 1 ATOM 1197 C CG . LEU A 1 162 ? 14.609 31.247 49.288 1.00 74.54 ? 162 LEU A CG 1 ATOM 1198 C CD1 . LEU A 1 162 ? 13.680 30.793 48.190 1.00 73.01 ? 162 LEU A CD1 1 ATOM 1199 C CD2 . LEU A 1 162 ? 16.043 30.839 48.989 1.00 72.77 ? 162 LEU A CD2 1 ATOM 1200 N N . LEU A 1 163 ? 16.910 32.587 51.750 1.00 76.94 ? 163 LEU A N 1 ATOM 1201 C CA . LEU A 1 163 ? 18.339 32.652 52.025 1.00 77.21 ? 163 LEU A CA 1 ATOM 1202 C C . LEU A 1 163 ? 19.060 31.323 51.860 1.00 78.28 ? 163 LEU A C 1 ATOM 1203 O O . LEU A 1 163 ? 18.805 30.371 52.593 1.00 78.17 ? 163 LEU A O 1 ATOM 1204 C CB . LEU A 1 163 ? 18.567 33.168 53.448 1.00 75.26 ? 163 LEU A CB 1 ATOM 1205 C CG . LEU A 1 163 ? 17.803 34.423 53.875 1.00 72.97 ? 163 LEU A CG 1 ATOM 1206 C CD1 . LEU A 1 163 ? 18.264 34.806 55.259 1.00 71.93 ? 163 LEU A CD1 1 ATOM 1207 C CD2 . LEU A 1 163 ? 18.038 35.567 52.903 1.00 72.36 ? 163 LEU A CD2 1 ATOM 1208 N N . ILE A 1 164 ? 19.973 31.269 50.898 1.00 79.75 ? 164 ILE A N 1 ATOM 1209 C CA . ILE A 1 164 ? 20.748 30.062 50.651 1.00 81.40 ? 164 ILE A CA 1 ATOM 1210 C C . ILE A 1 164 ? 22.126 30.310 51.245 1.00 84.05 ? 164 ILE A C 1 ATOM 1211 O O . ILE A 1 164 ? 22.811 31.257 50.851 1.00 83.19 ? 164 ILE A O 1 ATOM 1212 C CB . ILE A 1 164 ? 20.881 29.792 49.149 1.00 80.15 ? 164 ILE A CB 1 ATOM 1213 C CG1 . ILE A 1 164 ? 19.492 29.678 48.520 1.00 79.60 ? 164 ILE A CG1 1 ATOM 1214 C CG2 . ILE A 1 164 ? 21.677 28.524 48.919 1.00 79.69 ? 164 ILE A CG2 1 ATOM 1215 C CD1 . ILE A 1 164 ? 18.640 28.569 49.101 1.00 79.61 ? 164 ILE A CD1 1 ATOM 1216 N N . CYS A 1 165 ? 22.525 29.466 52.194 1.00 87.37 ? 165 CYS A N 1 ATOM 1217 C CA . CYS A 1 165 ? 23.813 29.626 52.863 1.00 91.33 ? 165 CYS A CA 1 ATOM 1218 C C . CYS A 1 165 ? 24.837 28.526 52.583 1.00 93.03 ? 165 CYS A C 1 ATOM 1219 O O . CYS A 1 165 ? 24.532 27.520 51.941 1.00 92.35 ? 165 CYS A O 1 ATOM 1220 C CB . CYS A 1 165 ? 23.605 29.711 54.370 1.00 93.49 ? 165 CYS A CB 1 ATOM 1221 S SG . CYS A 1 165 ? 22.382 30.913 54.989 1.00 96.14 ? 165 CYS A SG 1 ATOM 1222 N N . LYS A 1 166 ? 26.049 28.724 53.100 1.00 95.56 ? 166 LYS A N 1 ATOM 1223 C CA . LYS A 1 166 ? 27.148 27.777 52.920 1.00 99.03 ? 166 LYS A CA 1 ATOM 1224 C C . LYS A 1 166 ? 27.300 26.754 54.043 1.00 100.83 ? 166 LYS A C 1 ATOM 1225 O O . LYS A 1 166 ? 26.554 26.781 55.018 1.00 102.07 ? 166 LYS A O 1 ATOM 1226 C CB . LYS A 1 166 ? 28.458 28.540 52.738 1.00 98.48 ? 166 LYS A CB 1 ATOM 1227 C CG . LYS A 1 166 ? 28.646 29.054 51.330 1.00 99.84 ? 166 LYS A CG 1 ATOM 1228 C CD . LYS A 1 166 ? 28.665 27.882 50.349 1.00 100.72 ? 166 LYS A CD 1 ATOM 1229 C CE . LYS A 1 166 ? 28.811 28.345 48.906 1.00 100.77 ? 166 LYS A CE 1 ATOM 1230 N NZ . LYS A 1 166 ? 28.916 27.192 47.966 1.00 99.98 ? 166 LYS A NZ 1 ATOM 1231 N N . LYS A 1 167 ? 28.274 25.856 53.895 1.00 102.55 ? 167 LYS A N 1 ATOM 1232 C CA . LYS A 1 167 ? 28.532 24.800 54.879 1.00 104.63 ? 167 LYS A CA 1 ATOM 1233 C C . LYS A 1 167 ? 28.667 25.313 56.310 1.00 106.50 ? 167 LYS A C 1 ATOM 1234 O O . LYS A 1 167 ? 29.494 26.181 56.591 1.00 107.48 ? 167 LYS A O 1 ATOM 1235 C CB . LYS A 1 167 ? 29.806 24.024 54.516 1.00 103.75 ? 167 LYS A CB 1 ATOM 1236 C CG . LYS A 1 167 ? 29.755 23.290 53.186 1.00 103.59 ? 167 LYS A CG 1 ATOM 1237 C CD . LYS A 1 167 ? 29.763 24.252 52.010 1.00 102.10 ? 167 LYS A CD 1 ATOM 1238 C CE . LYS A 1 167 ? 29.684 23.504 50.693 1.00 101.34 ? 167 LYS A CE 1 ATOM 1239 N NZ . LYS A 1 167 ? 29.751 24.441 49.543 1.00 100.65 ? 167 LYS A NZ 1 ATOM 1240 N N . GLY A 1 168 ? 27.860 24.762 57.212 1.00 107.64 ? 168 GLY A N 1 ATOM 1241 C CA . GLY A 1 168 ? 27.909 25.174 58.604 1.00 110.33 ? 168 GLY A CA 1 ATOM 1242 C C . GLY A 1 168 ? 27.925 26.679 58.795 1.00 112.56 ? 168 GLY A C 1 ATOM 1243 O O . GLY A 1 168 ? 28.821 27.220 59.443 1.00 112.62 ? 168 GLY A O 1 ATOM 1244 N N . THR A 1 169 ? 26.932 27.357 58.229 1.00 114.87 ? 169 THR A N 1 ATOM 1245 C CA . THR A 1 169 ? 26.826 28.811 58.334 1.00 117.64 ? 169 THR A CA 1 ATOM 1246 C C . THR A 1 169 ? 25.441 29.190 58.852 1.00 119.29 ? 169 THR A C 1 ATOM 1247 O O . THR A 1 169 ? 25.218 30.306 59.323 1.00 119.56 ? 169 THR A O 1 ATOM 1248 C CB . THR A 1 169 ? 27.060 29.490 56.959 1.00 117.38 ? 169 THR A CB 1 ATOM 1249 O OG1 . THR A 1 169 ? 28.400 29.231 56.521 1.00 117.45 ? 169 THR A OG1 1 ATOM 1250 C CG2 . THR A 1 169 ? 26.848 30.998 57.053 1.00 116.84 ? 169 THR A CG2 1 ATOM 1251 N N . LEU A 1 170 ? 24.509 28.251 58.758 1.00 120.79 ? 170 LEU A N 1 ATOM 1252 C CA . LEU A 1 170 ? 23.155 28.487 59.221 1.00 122.00 ? 170 LEU A CA 1 ATOM 1253 C C . LEU A 1 170 ? 22.990 27.707 60.518 1.00 123.65 ? 170 LEU A C 1 ATOM 1254 O O . LEU A 1 170 ? 23.706 26.734 60.762 1.00 123.36 ? 170 LEU A O 1 ATOM 1255 C CB . LEU A 1 170 ? 22.151 28.003 58.170 1.00 121.07 ? 170 LEU A CB 1 ATOM 1256 C CG . LEU A 1 170 ? 20.732 28.573 58.206 1.00 120.75 ? 170 LEU A CG 1 ATOM 1257 C CD1 . LEU A 1 170 ? 20.779 30.070 57.957 1.00 120.27 ? 170 LEU A CD1 1 ATOM 1258 C CD2 . LEU A 1 170 ? 19.878 27.895 57.150 1.00 120.09 ? 170 LEU A CD2 1 ATOM 1259 N N . THR A 1 171 ? 22.055 28.141 61.354 1.00 125.66 ? 171 THR A N 1 ATOM 1260 C CA . THR A 1 171 ? 21.808 27.479 62.627 1.00 127.53 ? 171 THR A CA 1 ATOM 1261 C C . THR A 1 171 ? 20.845 26.306 62.457 1.00 128.50 ? 171 THR A C 1 ATOM 1262 O O . THR A 1 171 ? 20.065 26.263 61.506 1.00 128.74 ? 171 THR A O 1 ATOM 1263 C CB . THR A 1 171 ? 21.221 28.470 63.648 1.00 127.59 ? 171 THR A CB 1 ATOM 1264 O OG1 . THR A 1 171 ? 22.104 29.590 63.779 1.00 127.98 ? 171 THR A OG1 1 ATOM 1265 C CG2 . THR A 1 171 ? 21.051 27.808 65.006 1.00 128.22 ? 171 THR A CG2 1 ATOM 1266 N N . GLU A 1 172 ? 20.909 25.350 63.379 1.00 129.60 ? 172 GLU A N 1 ATOM 1267 C CA . GLU A 1 172 ? 20.034 24.187 63.335 1.00 130.63 ? 172 GLU A CA 1 ATOM 1268 C C . GLU A 1 172 ? 18.600 24.592 63.674 1.00 131.48 ? 172 GLU A C 1 ATOM 1269 O O . GLU A 1 172 ? 17.674 23.790 63.554 1.00 131.34 ? 172 GLU A O 1 ATOM 1270 C CB . GLU A 1 172 ? 20.541 23.117 64.312 1.00 130.78 ? 172 GLU A CB 1 ATOM 1271 C CG . GLU A 1 172 ? 20.891 23.646 65.703 1.00 130.88 ? 172 GLU A CG 1 ATOM 1272 C CD . GLU A 1 172 ? 21.673 22.643 66.544 1.00 130.95 ? 172 GLU A CD 1 ATOM 1273 O OE1 . GLU A 1 172 ? 22.760 22.211 66.101 1.00 131.13 ? 172 GLU A OE1 1 ATOM 1274 O OE2 . GLU A 1 172 ? 21.209 22.291 67.650 1.00 130.20 ? 172 GLU A OE2 1 ATOM 1275 N N . ASP A 1 173 ? 18.428 25.848 64.086 1.00 132.63 ? 173 ASP A N 1 ATOM 1276 C CA . ASP A 1 173 ? 17.116 26.387 64.447 1.00 133.88 ? 173 ASP A CA 1 ATOM 1277 C C . ASP A 1 173 ? 16.677 27.503 63.504 1.00 133.75 ? 173 ASP A C 1 ATOM 1278 O O . ASP A 1 173 ? 15.776 28.281 63.824 1.00 133.94 ? 173 ASP A O 1 ATOM 1279 C CB . ASP A 1 173 ? 17.135 26.931 65.881 1.00 135.34 ? 173 ASP A CB 1 ATOM 1280 C CG . ASP A 1 173 ? 17.187 25.831 66.926 1.00 136.55 ? 173 ASP A CG 1 ATOM 1281 O OD1 . ASP A 1 173 ? 16.251 25.003 66.966 1.00 137.41 ? 173 ASP A OD1 1 ATOM 1282 O OD2 . ASP A 1 173 ? 18.161 25.797 67.709 1.00 136.76 ? 173 ASP A OD2 1 ATOM 1283 N N . GLY A 1 174 ? 17.321 27.583 62.346 1.00 133.31 ? 174 GLY A N 1 ATOM 1284 C CA . GLY A 1 174 ? 16.974 28.610 61.382 1.00 133.13 ? 174 GLY A CA 1 ATOM 1285 C C . GLY A 1 174 ? 17.358 30.012 61.819 1.00 133.02 ? 174 GLY A C 1 ATOM 1286 O O . GLY A 1 174 ? 16.493 30.837 62.121 1.00 133.28 ? 174 GLY A O 1 ATOM 1287 N N . THR A 1 175 ? 18.660 30.282 61.847 1.00 132.63 ? 175 THR A N 1 ATOM 1288 C CA . THR A 1 175 ? 19.176 31.587 62.247 1.00 131.70 ? 175 THR A CA 1 ATOM 1289 C C . THR A 1 175 ? 20.621 31.742 61.775 1.00 130.86 ? 175 THR A C 1 ATOM 1290 O O . THR A 1 175 ? 21.326 30.752 61.563 1.00 130.14 ? 175 THR A O 1 ATOM 1291 C CB . THR A 1 175 ? 19.141 31.756 63.785 1.00 131.83 ? 175 THR A CB 1 ATOM 1292 O OG1 . THR A 1 175 ? 17.819 31.484 64.270 1.00 131.90 ? 175 THR A OG1 1 ATOM 1293 C CG2 . THR A 1 175 ? 19.532 33.177 64.175 1.00 131.15 ? 175 THR A CG2 1 ATOM 1294 N N . GLN A 1 176 ? 21.055 32.988 61.610 1.00 129.96 ? 176 GLN A N 1 ATOM 1295 C CA . GLN A 1 176 ? 22.417 33.271 61.171 1.00 129.05 ? 176 GLN A CA 1 ATOM 1296 C C . GLN A 1 176 ? 23.388 32.670 62.189 1.00 128.72 ? 176 GLN A C 1 ATOM 1297 O O . GLN A 1 176 ? 23.091 32.628 63.382 1.00 129.13 ? 176 GLN A O 1 ATOM 1298 C CB . GLN A 1 176 ? 22.626 34.784 61.070 1.00 128.31 ? 176 GLN A CB 1 ATOM 1299 C CG . GLN A 1 176 ? 23.469 35.221 59.880 1.00 126.92 ? 176 GLN A CG 1 ATOM 1300 C CD . GLN A 1 176 ? 22.758 35.020 58.552 1.00 125.56 ? 176 GLN A CD 1 ATOM 1301 O OE1 . GLN A 1 176 ? 22.361 33.908 58.206 1.00 124.05 ? 176 GLN A OE1 1 ATOM 1302 N NE2 . GLN A 1 176 ? 22.597 36.104 57.799 1.00 125.73 ? 176 GLN A NE2 1 ATOM 1303 N N . LYS A 1 177 ? 24.544 32.204 61.723 1.00 127.92 ? 177 LYS A N 1 ATOM 1304 C CA . LYS A 1 177 ? 25.527 31.597 62.618 1.00 127.33 ? 177 LYS A CA 1 ATOM 1305 C C . LYS A 1 177 ? 26.466 32.622 63.257 1.00 127.29 ? 177 LYS A C 1 ATOM 1306 O O . LYS A 1 177 ? 26.025 33.506 63.994 1.00 127.43 ? 177 LYS A O 1 ATOM 1307 C CB . LYS A 1 177 ? 26.350 30.545 61.864 1.00 127.11 ? 177 LYS A CB 1 ATOM 1308 C CG . LYS A 1 177 ? 27.248 29.687 62.748 1.00 126.13 ? 177 LYS A CG 1 ATOM 1309 C CD . LYS A 1 177 ? 28.141 28.782 61.912 1.00 125.41 ? 177 LYS A CD 1 ATOM 1310 C CE . LYS A 1 177 ? 29.051 27.933 62.786 1.00 124.62 ? 177 LYS A CE 1 ATOM 1311 N NZ . LYS A 1 177 ? 28.278 27.015 63.666 1.00 124.11 ? 177 LYS A NZ 1 ATOM 1312 N N . MET A 1 178 ? 27.760 32.491 62.966 1.00 126.83 ? 178 MET A N 1 ATOM 1313 C CA . MET A 1 178 ? 28.802 33.369 63.504 1.00 125.90 ? 178 MET A CA 1 ATOM 1314 C C . MET A 1 178 ? 28.603 34.844 63.143 1.00 124.60 ? 178 MET A C 1 ATOM 1315 O O . MET A 1 178 ? 29.567 35.610 63.086 1.00 124.41 ? 178 MET A O 1 ATOM 1316 C CB . MET A 1 178 ? 30.176 32.915 62.991 1.00 126.93 ? 178 MET A CB 1 ATOM 1317 C CG . MET A 1 178 ? 30.510 31.444 63.228 1.00 127.71 ? 178 MET A CG 1 ATOM 1318 S SD . MET A 1 178 ? 30.859 31.038 64.951 1.00 128.96 ? 178 MET A SD 1 ATOM 1319 C CE . MET A 1 178 ? 29.358 30.158 65.416 1.00 128.70 ? 178 MET A CE 1 ATOM 1320 N N . PHE A 1 179 ? 27.356 35.237 62.906 1.00 122.82 ? 179 PHE A N 1 ATOM 1321 C CA . PHE A 1 179 ? 27.038 36.611 62.537 1.00 121.48 ? 179 PHE A CA 1 ATOM 1322 C C . PHE A 1 179 ? 25.855 37.082 63.387 1.00 121.02 ? 179 PHE A C 1 ATOM 1323 O O . PHE A 1 179 ? 25.907 38.146 64.008 1.00 121.03 ? 179 PHE A O 1 ATOM 1324 C CB . PHE A 1 179 ? 26.711 36.663 61.039 1.00 121.29 ? 179 PHE A CB 1 ATOM 1325 C CG . PHE A 1 179 ? 27.583 35.753 60.199 1.00 121.31 ? 179 PHE A CG 1 ATOM 1326 C CD1 . PHE A 1 179 ? 27.339 34.379 60.149 1.00 121.43 ? 179 PHE A CD1 1 ATOM 1327 C CD2 . PHE A 1 179 ? 28.683 36.257 59.510 1.00 121.07 ? 179 PHE A CD2 1 ATOM 1328 C CE1 . PHE A 1 179 ? 28.179 33.520 59.429 1.00 120.27 ? 179 PHE A CE1 1 ATOM 1329 C CE2 . PHE A 1 179 ? 29.530 35.404 58.787 1.00 120.45 ? 179 PHE A CE2 1 ATOM 1330 C CZ . PHE A 1 179 ? 29.276 34.035 58.749 1.00 120.01 ? 179 PHE A CZ 1 ATOM 1331 N N . GLU A 1 180 ? 24.802 36.265 63.408 1.00 120.15 ? 180 GLU A N 1 ATOM 1332 C CA . GLU A 1 180 ? 23.578 36.497 64.184 1.00 118.35 ? 180 GLU A CA 1 ATOM 1333 C C . GLU A 1 180 ? 23.010 37.919 64.275 1.00 117.56 ? 180 GLU A C 1 ATOM 1334 O O . GLU A 1 180 ? 23.747 38.904 64.361 1.00 118.07 ? 180 GLU A O 1 ATOM 1335 C CB . GLU A 1 180 ? 23.772 35.938 65.599 1.00 117.35 ? 180 GLU A CB 1 ATOM 1336 C CG . GLU A 1 180 ? 22.565 36.086 66.509 1.00 116.08 ? 180 GLU A CG 1 ATOM 1337 C CD . GLU A 1 180 ? 22.789 37.103 67.611 1.00 115.51 ? 180 GLU A CD 1 ATOM 1338 O OE1 . GLU A 1 180 ? 22.988 38.294 67.295 1.00 114.54 ? 180 GLU A OE1 1 ATOM 1339 O OE2 . GLU A 1 180 ? 22.767 36.707 68.796 1.00 115.55 ? 180 GLU A OE2 1 ATOM 1340 N N . LYS A 1 181 ? 21.680 37.995 64.265 1.00 115.88 ? 181 LYS A N 1 ATOM 1341 C CA . LYS A 1 181 ? 20.926 39.248 64.359 1.00 113.36 ? 181 LYS A CA 1 ATOM 1342 C C . LYS A 1 181 ? 20.912 40.094 63.084 1.00 111.21 ? 181 LYS A C 1 ATOM 1343 O O . LYS A 1 181 ? 21.139 41.306 63.125 1.00 109.94 ? 181 LYS A O 1 ATOM 1344 C CB . LYS A 1 181 ? 21.431 40.093 65.540 1.00 113.72 ? 181 LYS A CB 1 ATOM 1345 C CG . LYS A 1 181 ? 20.491 41.229 65.929 1.00 114.05 ? 181 LYS A CG 1 ATOM 1346 C CD . LYS A 1 181 ? 20.933 41.932 67.204 1.00 114.47 ? 181 LYS A CD 1 ATOM 1347 C CE . LYS A 1 181 ? 19.928 43.003 67.611 1.00 114.55 ? 181 LYS A CE 1 ATOM 1348 N NZ . LYS A 1 181 ? 20.341 43.756 68.827 1.00 114.02 ? 181 LYS A NZ 1 ATOM 1349 N N . GLN A 1 182 ? 20.649 39.448 61.951 1.00 109.09 ? 182 GLN A N 1 ATOM 1350 C CA . GLN A 1 182 ? 20.565 40.152 60.672 1.00 106.43 ? 182 GLN A CA 1 ATOM 1351 C C . GLN A 1 182 ? 19.079 40.429 60.443 1.00 105.18 ? 182 GLN A C 1 ATOM 1352 O O . GLN A 1 182 ? 18.234 39.576 60.721 1.00 104.25 ? 182 GLN A O 1 ATOM 1353 C CB . GLN A 1 182 ? 21.116 39.287 59.520 1.00 104.54 ? 182 GLN A CB 1 ATOM 1354 C CG . GLN A 1 182 ? 22.547 39.607 59.026 1.00 99.44 ? 182 GLN A CG 1 ATOM 1355 C CD . GLN A 1 182 ? 22.691 40.989 58.381 1.00 97.02 ? 182 GLN A CD 1 ATOM 1356 O OE1 . GLN A 1 182 ? 21.805 41.461 57.670 1.00 94.50 ? 182 GLN A OE1 1 ATOM 1357 N NE2 . GLN A 1 182 ? 23.827 41.628 58.618 1.00 95.42 ? 182 GLN A NE2 1 ATOM 1358 N N . HIS A 1 183 ? 18.761 41.622 59.951 1.00 104.05 ? 183 HIS A N 1 ATOM 1359 C CA . HIS A 1 183 ? 17.372 41.981 59.693 1.00 103.10 ? 183 HIS A CA 1 ATOM 1360 C C . HIS A 1 183 ? 16.989 41.842 58.219 1.00 101.43 ? 183 HIS A C 1 ATOM 1361 O O . HIS A 1 183 ? 17.790 41.406 57.393 1.00 101.15 ? 183 HIS A O 1 ATOM 1362 C CB . HIS A 1 183 ? 17.091 43.411 60.173 1.00 103.23 ? 183 HIS A CB 1 ATOM 1363 C CG . HIS A 1 183 ? 16.210 43.474 61.382 1.00 103.81 ? 183 HIS A CG 1 ATOM 1364 N ND1 . HIS A 1 183 ? 15.028 42.770 61.476 1.00 103.77 ? 183 HIS A ND1 1 ATOM 1365 C CD2 . HIS A 1 183 ? 16.330 44.164 62.540 1.00 103.59 ? 183 HIS A CD2 1 ATOM 1366 C CE1 . HIS A 1 183 ? 14.457 43.024 62.639 1.00 103.44 ? 183 HIS A CE1 1 ATOM 1367 N NE2 . HIS A 1 183 ? 15.227 43.868 63.304 1.00 104.12 ? 183 HIS A NE2 1 ATOM 1368 N N . VAL A 1 184 ? 15.757 42.217 57.892 1.00 99.81 ? 184 VAL A N 1 ATOM 1369 C CA . VAL A 1 184 ? 15.284 42.119 56.522 1.00 97.97 ? 184 VAL A CA 1 ATOM 1370 C C . VAL A 1 184 ? 14.377 43.284 56.126 1.00 96.48 ? 184 VAL A C 1 ATOM 1371 O O . VAL A 1 184 ? 13.151 43.163 56.159 1.00 95.96 ? 184 VAL A O 1 ATOM 1372 C CB . VAL A 1 184 ? 14.518 40.797 56.309 1.00 98.90 ? 184 VAL A CB 1 ATOM 1373 C CG1 . VAL A 1 184 ? 14.206 40.613 54.841 1.00 98.27 ? 184 VAL A CG1 1 ATOM 1374 C CG2 . VAL A 1 184 ? 15.334 39.624 56.840 1.00 98.32 ? 184 VAL A CG2 1 ATOM 1375 N N . LEU A 1 185 ? 14.985 44.412 55.760 1.00 95.25 ? 185 LEU A N 1 ATOM 1376 C CA . LEU A 1 185 ? 14.237 45.595 55.333 1.00 94.35 ? 185 LEU A CA 1 ATOM 1377 C C . LEU A 1 185 ? 13.755 45.375 53.906 1.00 94.32 ? 185 LEU A C 1 ATOM 1378 O O . LEU A 1 185 ? 14.497 44.838 53.085 1.00 94.07 ? 185 LEU A O 1 ATOM 1379 C CB . LEU A 1 185 ? 15.122 46.845 55.352 1.00 94.51 ? 185 LEU A CB 1 ATOM 1380 C CG . LEU A 1 185 ? 15.424 47.567 56.662 1.00 94.57 ? 185 LEU A CG 1 ATOM 1381 C CD1 . LEU A 1 185 ? 14.103 47.946 57.311 1.00 95.02 ? 185 LEU A CD1 1 ATOM 1382 C CD2 . LEU A 1 185 ? 16.270 46.688 57.580 1.00 94.64 ? 185 LEU A CD2 1 ATOM 1383 N N . MET A 1 186 ? 12.527 45.797 53.606 1.00 93.78 ? 186 MET A N 1 ATOM 1384 C CA . MET A 1 186 ? 11.975 45.629 52.263 1.00 92.94 ? 186 MET A CA 1 ATOM 1385 C C . MET A 1 186 ? 11.451 46.916 51.652 1.00 92.45 ? 186 MET A C 1 ATOM 1386 O O . MET A 1 186 ? 10.257 47.029 51.384 1.00 93.10 ? 186 MET A O 1 ATOM 1387 C CB . MET A 1 186 ? 10.841 44.591 52.257 1.00 92.62 ? 186 MET A CB 1 ATOM 1388 C CG . MET A 1 186 ? 10.218 44.368 50.869 1.00 90.86 ? 186 MET A CG 1 ATOM 1389 S SD . MET A 1 186 ? 8.762 43.300 50.873 1.00 89.54 ? 186 MET A SD 1 ATOM 1390 C CE . MET A 1 186 ? 7.443 44.520 50.889 1.00 90.38 ? 186 MET A CE 1 ATOM 1391 N N . PHE A 1 187 ? 12.335 47.883 51.431 1.00 91.53 ? 187 PHE A N 1 ATOM 1392 C CA . PHE A 1 187 ? 11.926 49.142 50.822 1.00 91.60 ? 187 PHE A CA 1 ATOM 1393 C C . PHE A 1 187 ? 11.100 48.824 49.578 1.00 90.36 ? 187 PHE A C 1 ATOM 1394 O O . PHE A 1 187 ? 11.638 48.696 48.479 1.00 90.98 ? 187 PHE A O 1 ATOM 1395 C CB . PHE A 1 187 ? 13.157 49.961 50.438 1.00 93.36 ? 187 PHE A CB 1 ATOM 1396 C CG . PHE A 1 187 ? 13.912 50.503 51.613 1.00 95.74 ? 187 PHE A CG 1 ATOM 1397 C CD1 . PHE A 1 187 ? 14.332 49.659 52.639 1.00 96.36 ? 187 PHE A CD1 1 ATOM 1398 C CD2 . PHE A 1 187 ? 14.207 51.862 51.697 1.00 96.16 ? 187 PHE A CD2 1 ATOM 1399 C CE1 . PHE A 1 187 ? 15.035 50.160 53.732 1.00 97.98 ? 187 PHE A CE1 1 ATOM 1400 C CE2 . PHE A 1 187 ? 14.909 52.373 52.783 1.00 97.52 ? 187 PHE A CE2 1 ATOM 1401 C CZ . PHE A 1 187 ? 15.324 51.521 53.803 1.00 98.04 ? 187 PHE A CZ 1 ATOM 1402 N N . ALA A 1 188 ? 9.788 48.708 49.758 1.00 87.97 ? 188 ALA A N 1 ATOM 1403 C CA . ALA A 1 188 ? 8.896 48.363 48.664 1.00 86.36 ? 188 ALA A CA 1 ATOM 1404 C C . ALA A 1 188 ? 7.665 49.252 48.569 1.00 84.49 ? 188 ALA A C 1 ATOM 1405 O O . ALA A 1 188 ? 6.809 49.225 49.443 1.00 85.84 ? 188 ALA A O 1 ATOM 1406 C CB . ALA A 1 188 ? 8.464 46.903 48.813 1.00 87.39 ? 188 ALA A CB 1 ATOM 1407 N N . VAL A 1 189 ? 7.561 50.024 47.495 1.00 82.64 ? 189 VAL A N 1 ATOM 1408 C CA . VAL A 1 189 ? 6.407 50.897 47.324 1.00 80.38 ? 189 VAL A CA 1 ATOM 1409 C C . VAL A 1 189 ? 5.203 50.093 46.834 1.00 80.65 ? 189 VAL A C 1 ATOM 1410 O O . VAL A 1 189 ? 5.323 49.274 45.916 1.00 82.15 ? 189 VAL A O 1 ATOM 1411 C CB . VAL A 1 189 ? 6.699 52.038 46.317 1.00 77.93 ? 189 VAL A CB 1 ATOM 1412 C CG1 . VAL A 1 189 ? 8.196 52.234 46.184 1.00 77.19 ? 189 VAL A CG1 1 ATOM 1413 C CG2 . VAL A 1 189 ? 6.055 51.752 44.975 1.00 75.03 ? 189 VAL A CG2 1 ATOM 1414 N N . PHE A 1 190 ? 4.049 50.309 47.466 1.00 78.48 ? 190 PHE A N 1 ATOM 1415 C CA . PHE A 1 190 ? 2.827 49.619 47.069 1.00 74.38 ? 190 PHE A CA 1 ATOM 1416 C C . PHE A 1 190 ? 1.874 50.609 46.420 1.00 74.20 ? 190 PHE A C 1 ATOM 1417 O O . PHE A 1 190 ? 2.024 51.824 46.563 1.00 73.36 ? 190 PHE A O 1 ATOM 1418 C CB . PHE A 1 190 ? 2.133 48.969 48.265 1.00 70.78 ? 190 PHE A CB 1 ATOM 1419 C CG . PHE A 1 190 ? 2.827 47.746 48.791 1.00 66.49 ? 190 PHE A CG 1 ATOM 1420 C CD1 . PHE A 1 190 ? 4.018 47.850 49.493 1.00 65.42 ? 190 PHE A CD1 1 ATOM 1421 C CD2 . PHE A 1 190 ? 2.266 46.489 48.608 1.00 65.21 ? 190 PHE A CD2 1 ATOM 1422 C CE1 . PHE A 1 190 ? 4.644 46.715 50.012 1.00 66.43 ? 190 PHE A CE1 1 ATOM 1423 C CE2 . PHE A 1 190 ? 2.883 45.347 49.122 1.00 65.92 ? 190 PHE A CE2 1 ATOM 1424 C CZ . PHE A 1 190 ? 4.073 45.459 49.825 1.00 65.09 ? 190 PHE A CZ 1 ATOM 1425 N N . ASP A 1 191 ? 0.909 50.073 45.685 1.00 74.13 ? 191 ASP A N 1 ATOM 1426 C CA . ASP A 1 191 ? -0.096 50.874 45.004 1.00 73.41 ? 191 ASP A CA 1 ATOM 1427 C C . ASP A 1 191 ? -1.373 50.052 44.999 1.00 74.24 ? 191 ASP A C 1 ATOM 1428 O O . ASP A 1 191 ? -1.583 49.210 44.124 1.00 73.65 ? 191 ASP A O 1 ATOM 1429 C CB . ASP A 1 191 ? 0.347 51.197 43.574 1.00 71.96 ? 191 ASP A CB 1 ATOM 1430 C CG . ASP A 1 191 ? -0.747 51.869 42.759 1.00 73.68 ? 191 ASP A CG 1 ATOM 1431 O OD1 . ASP A 1 191 ? -0.431 52.507 41.723 1.00 74.67 ? 191 ASP A OD1 1 ATOM 1432 O OD2 . ASP A 1 191 ? -1.927 51.754 43.149 1.00 71.18 ? 191 ASP A OD2 1 ATOM 1433 N N . GLU A 1 192 ? -2.218 50.294 45.997 1.00 74.39 ? 192 GLU A N 1 ATOM 1434 C CA . GLU A 1 192 ? -3.478 49.577 46.139 1.00 73.78 ? 192 GLU A CA 1 ATOM 1435 C C . GLU A 1 192 ? -4.376 49.682 44.902 1.00 74.52 ? 192 GLU A C 1 ATOM 1436 O O . GLU A 1 192 ? -5.311 48.900 44.749 1.00 74.00 ? 192 GLU A O 1 ATOM 1437 C CB . GLU A 1 192 ? -4.204 50.090 47.380 1.00 72.96 ? 192 GLU A CB 1 ATOM 1438 C CG . GLU A 1 192 ? -3.415 49.894 48.656 1.00 70.45 ? 192 GLU A CG 1 ATOM 1439 C CD . GLU A 1 192 ? -3.391 48.444 49.109 1.00 70.94 ? 192 GLU A CD 1 ATOM 1440 O OE1 . GLU A 1 192 ? -2.750 48.146 50.142 1.00 69.30 ? 192 GLU A OE1 1 ATOM 1441 O OE2 . GLU A 1 192 ? -4.019 47.602 48.437 1.00 70.64 ? 192 GLU A OE2 1 ATOM 1442 N N . SER A 1 193 ? -4.082 50.643 44.025 1.00 76.09 ? 193 SER A N 1 ATOM 1443 C CA . SER A 1 193 ? -4.852 50.836 42.798 1.00 79.07 ? 193 SER A CA 1 ATOM 1444 C C . SER A 1 193 ? -4.681 49.619 41.903 1.00 82.15 ? 193 SER A C 1 ATOM 1445 O O . SER A 1 193 ? -5.557 49.286 41.106 1.00 83.62 ? 193 SER A O 1 ATOM 1446 C CB . SER A 1 193 ? -4.356 52.060 42.034 1.00 78.90 ? 193 SER A CB 1 ATOM 1447 O OG . SER A 1 193 ? -4.111 53.150 42.903 1.00 81.14 ? 193 SER A OG 1 ATOM 1448 N N . LYS A 1 194 ? -3.534 48.966 42.041 1.00 84.58 ? 194 LYS A N 1 ATOM 1449 C CA . LYS A 1 194 ? -3.206 47.790 41.252 1.00 86.40 ? 194 LYS A CA 1 ATOM 1450 C C . LYS A 1 194 ? -3.139 46.578 42.165 1.00 89.15 ? 194 LYS A C 1 ATOM 1451 O O . LYS A 1 194 ? -2.054 46.119 42.504 1.00 90.01 ? 194 LYS A O 1 ATOM 1452 C CB . LYS A 1 194 ? -1.846 47.982 40.573 1.00 84.25 ? 194 LYS A CB 1 ATOM 1453 C CG . LYS A 1 194 ? -1.719 49.255 39.755 1.00 82.52 ? 194 LYS A CG 1 ATOM 1454 C CD . LYS A 1 194 ? -0.334 49.371 39.154 1.00 81.84 ? 194 LYS A CD 1 ATOM 1455 C CE . LYS A 1 194 ? -0.226 50.530 38.173 1.00 81.34 ? 194 LYS A CE 1 ATOM 1456 N NZ . LYS A 1 194 ? -0.301 51.859 38.835 1.00 83.28 ? 194 LYS A NZ 1 ATOM 1457 N N . SER A 1 195 ? -4.287 46.047 42.564 1.00 92.84 ? 195 SER A N 1 ATOM 1458 C CA . SER A 1 195 ? -4.272 44.894 43.449 1.00 97.18 ? 195 SER A CA 1 ATOM 1459 C C . SER A 1 195 ? -5.605 44.177 43.562 1.00 100.91 ? 195 SER A C 1 ATOM 1460 O O . SER A 1 195 ? -6.306 43.957 42.574 1.00 101.01 ? 195 SER A O 1 ATOM 1461 C CB . SER A 1 195 ? -3.829 45.329 44.845 1.00 96.90 ? 195 SER A CB 1 ATOM 1462 O OG . SER A 1 195 ? -4.739 46.276 45.384 1.00 95.89 ? 195 SER A OG 1 ATOM 1463 N N . TRP A 1 196 ? -5.926 43.811 44.798 1.00 106.05 ? 196 TRP A N 1 ATOM 1464 C CA . TRP A 1 196 ? -7.155 43.118 45.151 1.00 110.89 ? 196 TRP A CA 1 ATOM 1465 C C . TRP A 1 196 ? -8.335 44.035 44.837 1.00 113.72 ? 196 TRP A C 1 ATOM 1466 O O . TRP A 1 196 ? -9.209 43.697 44.037 1.00 114.90 ? 196 TRP A O 1 ATOM 1467 C CB . TRP A 1 196 ? -7.134 42.804 46.654 1.00 112.06 ? 196 TRP A CB 1 ATOM 1468 C CG . TRP A 1 196 ? -8.084 41.732 47.139 1.00 113.46 ? 196 TRP A CG 1 ATOM 1469 C CD1 . TRP A 1 196 ? -8.504 41.544 48.426 1.00 112.83 ? 196 TRP A CD1 1 ATOM 1470 C CD2 . TRP A 1 196 ? -8.660 40.663 46.371 1.00 114.17 ? 196 TRP A CD2 1 ATOM 1471 N NE1 . TRP A 1 196 ? -9.298 40.428 48.509 1.00 113.56 ? 196 TRP A NE1 1 ATOM 1472 C CE2 . TRP A 1 196 ? -9.411 39.867 47.265 1.00 114.06 ? 196 TRP A CE2 1 ATOM 1473 C CE3 . TRP A 1 196 ? -8.611 40.297 45.017 1.00 114.84 ? 196 TRP A CE3 1 ATOM 1474 C CZ2 . TRP A 1 196 ? -10.110 38.726 46.850 1.00 114.88 ? 196 TRP A CZ2 1 ATOM 1475 C CZ3 . TRP A 1 196 ? -9.306 39.163 44.604 1.00 115.35 ? 196 TRP A CZ3 1 ATOM 1476 C CH2 . TRP A 1 196 ? -10.046 38.391 45.521 1.00 115.66 ? 196 TRP A CH2 1 ATOM 1477 N N . ASN A 1 197 ? -8.339 45.204 45.472 1.00 116.24 ? 197 ASN A N 1 ATOM 1478 C CA . ASN A 1 197 ? -9.403 46.186 45.299 1.00 118.02 ? 197 ASN A CA 1 ATOM 1479 C C . ASN A 1 197 ? -8.995 47.390 44.466 1.00 117.77 ? 197 ASN A C 1 ATOM 1480 O O . ASN A 1 197 ? -7.819 47.744 44.390 1.00 117.50 ? 197 ASN A O 1 ATOM 1481 C CB . ASN A 1 197 ? -9.875 46.682 46.666 1.00 120.20 ? 197 ASN A CB 1 ATOM 1482 C CG . ASN A 1 197 ? -10.712 45.657 47.406 1.00 123.14 ? 197 ASN A CG 1 ATOM 1483 O OD1 . ASN A 1 197 ? -10.399 44.464 47.404 1.00 122.56 ? 197 ASN A OD1 1 ATOM 1484 N ND2 . ASN A 1 197 ? -11.774 46.127 48.056 1.00 126.26 ? 197 ASN A ND2 1 ATOM 1485 N N . GLN A 1 198 ? -9.986 48.018 43.844 1.00 117.74 ? 198 GLN A N 1 ATOM 1486 C CA . GLN A 1 198 ? -9.749 49.209 43.045 1.00 117.68 ? 198 GLN A CA 1 ATOM 1487 C C . GLN A 1 198 ? -9.654 50.364 44.042 1.00 116.63 ? 198 GLN A C 1 ATOM 1488 O O . GLN A 1 198 ? -10.471 51.287 44.023 1.00 117.29 ? 198 GLN A O 1 ATOM 1489 C CB . GLN A 1 198 ? -10.913 49.440 42.070 1.00 118.66 ? 198 GLN A CB 1 ATOM 1490 C CG . GLN A 1 198 ? -11.054 48.377 40.976 1.00 119.80 ? 198 GLN A CG 1 ATOM 1491 C CD . GLN A 1 198 ? -10.004 48.504 39.876 1.00 120.68 ? 198 GLN A CD 1 ATOM 1492 O OE1 . GLN A 1 198 ? -10.015 49.458 39.094 1.00 120.47 ? 198 GLN A OE1 1 ATOM 1493 N NE2 . GLN A 1 198 ? -9.091 47.537 39.814 1.00 121.24 ? 198 GLN A NE2 1 ATOM 1494 N N . THR A 1 199 ? -8.658 50.292 44.921 1.00 114.66 ? 199 THR A N 1 ATOM 1495 C CA . THR A 1 199 ? -8.447 51.312 45.942 1.00 112.73 ? 199 THR A CA 1 ATOM 1496 C C . THR A 1 199 ? -7.233 52.189 45.649 1.00 111.13 ? 199 THR A C 1 ATOM 1497 O O . THR A 1 199 ? -6.098 51.774 45.863 1.00 110.79 ? 199 THR A O 1 ATOM 1498 C CB . THR A 1 199 ? -8.265 50.664 47.327 1.00 112.65 ? 199 THR A CB 1 ATOM 1499 O OG1 . THR A 1 199 ? -7.263 49.641 47.247 1.00 112.49 ? 199 THR A OG1 1 ATOM 1500 C CG2 . THR A 1 199 ? -9.574 50.052 47.805 1.00 112.12 ? 199 THR A CG2 1 ATOM 1501 N N . SER A 1 200 ? -7.491 53.405 45.166 1.00 109.72 ? 200 SER A N 1 ATOM 1502 C CA . SER A 1 200 ? -6.447 54.377 44.827 1.00 107.83 ? 200 SER A CA 1 ATOM 1503 C C . SER A 1 200 ? -5.619 54.830 46.027 1.00 106.64 ? 200 SER A C 1 ATOM 1504 O O . SER A 1 200 ? -6.018 55.744 46.746 1.00 106.65 ? 200 SER A O 1 ATOM 1505 C CB . SER A 1 200 ? -7.080 55.605 44.173 1.00 107.72 ? 200 SER A CB 1 ATOM 1506 O OG . SER A 1 200 ? -6.172 56.693 44.159 1.00 108.07 ? 200 SER A OG 1 ATOM 1507 N N . SER A 1 201 ? -4.457 54.214 46.225 1.00 105.36 ? 201 SER A N 1 ATOM 1508 C CA . SER A 1 201 ? -3.603 54.563 47.358 1.00 104.35 ? 201 SER A CA 1 ATOM 1509 C C . SER A 1 201 ? -2.117 54.246 47.156 1.00 102.57 ? 201 SER A C 1 ATOM 1510 O O . SER A 1 201 ? -1.690 53.103 47.337 1.00 101.85 ? 201 SER A O 1 ATOM 1511 C CB . SER A 1 201 ? -4.114 53.844 48.619 1.00 105.18 ? 201 SER A CB 1 ATOM 1512 O OG . SER A 1 201 ? -3.307 54.115 49.755 1.00 105.09 ? 201 SER A OG 1 ATOM 1513 N N . LEU A 1 202 ? -1.331 55.255 46.781 1.00 99.99 ? 202 LEU A N 1 ATOM 1514 C CA . LEU A 1 202 ? 0.103 55.060 46.597 1.00 98.08 ? 202 LEU A CA 1 ATOM 1515 C C . LEU A 1 202 ? 0.640 54.938 48.016 1.00 96.08 ? 202 LEU A C 1 ATOM 1516 O O . LEU A 1 202 ? -0.076 55.268 48.955 1.00 96.90 ? 202 LEU A O 1 ATOM 1517 C CB . LEU A 1 202 ? 0.718 56.265 45.887 1.00 99.12 ? 202 LEU A CB 1 ATOM 1518 C CG . LEU A 1 202 ? 1.844 55.940 44.895 1.00 100.28 ? 202 LEU A CG 1 ATOM 1519 C CD1 . LEU A 1 202 ? 2.119 57.164 44.037 1.00 100.58 ? 202 LEU A CD1 1 ATOM 1520 C CD2 . LEU A 1 202 ? 3.100 55.486 45.630 1.00 99.38 ? 202 LEU A CD2 1 ATOM 1521 N N . MET A 1 203 ? 1.874 54.480 48.199 1.00 93.35 ? 203 MET A N 1 ATOM 1522 C CA . MET A 1 203 ? 2.378 54.332 49.562 1.00 91.40 ? 203 MET A CA 1 ATOM 1523 C C . MET A 1 203 ? 3.820 53.852 49.707 1.00 88.91 ? 203 MET A C 1 ATOM 1524 O O . MET A 1 203 ? 4.055 52.681 49.995 1.00 87.78 ? 203 MET A O 1 ATOM 1525 C CB . MET A 1 203 ? 1.461 53.372 50.331 1.00 94.33 ? 203 MET A CB 1 ATOM 1526 C CG . MET A 1 203 ? 0.767 53.981 51.543 1.00 97.13 ? 203 MET A CG 1 ATOM 1527 S SD . MET A 1 203 ? -0.616 52.972 52.120 1.00 100.55 ? 203 MET A SD 1 ATOM 1528 C CE . MET A 1 203 ? 0.236 51.472 52.698 1.00 99.67 ? 203 MET A CE 1 ATOM 1529 N N . TYR A 1 204 ? 4.780 54.753 49.537 1.00 86.66 ? 204 TYR A N 1 ATOM 1530 C CA . TYR A 1 204 ? 6.187 54.390 49.669 1.00 85.45 ? 204 TYR A CA 1 ATOM 1531 C C . TYR A 1 204 ? 6.481 53.926 51.091 1.00 83.55 ? 204 TYR A C 1 ATOM 1532 O O . TYR A 1 204 ? 6.700 54.748 51.975 1.00 84.45 ? 204 TYR A O 1 ATOM 1533 C CB . TYR A 1 204 ? 7.074 55.584 49.334 1.00 86.47 ? 204 TYR A CB 1 ATOM 1534 C CG . TYR A 1 204 ? 6.875 56.108 47.934 1.00 88.72 ? 204 TYR A CG 1 ATOM 1535 C CD1 . TYR A 1 204 ? 6.941 55.256 46.833 1.00 88.58 ? 204 TYR A CD1 1 ATOM 1536 C CD2 . TYR A 1 204 ? 6.624 57.458 47.708 1.00 90.40 ? 204 TYR A CD2 1 ATOM 1537 C CE1 . TYR A 1 204 ? 6.759 55.733 45.542 1.00 89.48 ? 204 TYR A CE1 1 ATOM 1538 C CE2 . TYR A 1 204 ? 6.442 57.948 46.417 1.00 91.52 ? 204 TYR A CE2 1 ATOM 1539 C CZ . TYR A 1 204 ? 6.509 57.082 45.339 1.00 90.97 ? 204 TYR A CZ 1 ATOM 1540 O OH . TYR A 1 204 ? 6.323 57.576 44.065 1.00 91.84 ? 204 TYR A OH 1 ATOM 1541 N N . THR A 1 205 ? 6.512 52.612 51.298 1.00 81.13 ? 205 THR A N 1 ATOM 1542 C CA . THR A 1 205 ? 6.748 52.048 52.622 1.00 79.43 ? 205 THR A CA 1 ATOM 1543 C C . THR A 1 205 ? 8.153 51.523 52.911 1.00 78.86 ? 205 THR A C 1 ATOM 1544 O O . THR A 1 205 ? 9.133 51.929 52.287 1.00 78.19 ? 205 THR A O 1 ATOM 1545 C CB . THR A 1 205 ? 5.766 50.891 52.916 1.00 79.89 ? 205 THR A CB 1 ATOM 1546 O OG1 . THR A 1 205 ? 6.307 49.662 52.416 1.00 76.01 ? 205 THR A OG1 1 ATOM 1547 C CG2 . THR A 1 205 ? 4.418 51.152 52.258 1.00 80.45 ? 205 THR A CG2 1 ATOM 1548 N N . VAL A 1 206 ? 8.213 50.625 53.896 1.00 78.20 ? 206 VAL A N 1 ATOM 1549 C CA . VAL A 1 206 ? 9.430 49.964 54.366 1.00 77.04 ? 206 VAL A CA 1 ATOM 1550 C C . VAL A 1 206 ? 8.968 48.779 55.216 1.00 77.31 ? 206 VAL A C 1 ATOM 1551 O O . VAL A 1 206 ? 9.237 48.728 56.407 1.00 77.05 ? 206 VAL A O 1 ATOM 1552 C CB . VAL A 1 206 ? 10.300 50.892 55.261 1.00 75.48 ? 206 VAL A CB 1 ATOM 1553 C CG1 . VAL A 1 206 ? 11.486 50.114 55.813 1.00 74.70 ? 206 VAL A CG1 1 ATOM 1554 C CG2 . VAL A 1 206 ? 10.799 52.089 54.467 1.00 73.86 ? 206 VAL A CG2 1 ATOM 1555 N N . ASN A 1 207 ? 8.268 47.840 54.580 1.00 78.81 ? 207 ASN A N 1 ATOM 1556 C CA . ASN A 1 207 ? 7.708 46.631 55.206 1.00 79.53 ? 207 ASN A CA 1 ATOM 1557 C C . ASN A 1 207 ? 6.215 46.825 55.387 1.00 80.22 ? 207 ASN A C 1 ATOM 1558 O O . ASN A 1 207 ? 5.581 46.160 56.204 1.00 78.73 ? 207 ASN A O 1 ATOM 1559 C CB . ASN A 1 207 ? 8.345 46.313 56.565 1.00 79.15 ? 207 ASN A CB 1 ATOM 1560 C CG . ASN A 1 207 ? 9.753 45.760 56.437 1.00 80.14 ? 207 ASN A CG 1 ATOM 1561 O OD1 . ASN A 1 207 ? 10.688 46.483 56.099 1.00 81.49 ? 207 ASN A OD1 1 ATOM 1562 N ND2 . ASN A 1 207 ? 9.906 44.466 56.699 1.00 79.87 ? 207 ASN A ND2 1 ATOM 1563 N N . GLY A 1 208 ? 5.673 47.751 54.600 1.00 82.40 ? 208 GLY A N 1 ATOM 1564 C CA . GLY A 1 208 ? 4.257 48.063 54.645 1.00 84.45 ? 208 GLY A CA 1 ATOM 1565 C C . GLY A 1 208 ? 4.007 49.379 55.357 1.00 86.23 ? 208 GLY A C 1 ATOM 1566 O O . GLY A 1 208 ? 3.185 50.196 54.928 1.00 86.40 ? 208 GLY A O 1 ATOM 1567 N N . TYR A 1 209 ? 4.729 49.575 56.455 1.00 87.39 ? 209 TYR A N 1 ATOM 1568 C CA . TYR A 1 209 ? 4.612 50.775 57.267 1.00 88.57 ? 209 TYR A CA 1 ATOM 1569 C C . TYR A 1 209 ? 5.091 52.000 56.501 1.00 90.62 ? 209 TYR A C 1 ATOM 1570 O O . TYR A 1 209 ? 6.158 51.985 55.896 1.00 90.25 ? 209 TYR A O 1 ATOM 1571 C CB . TYR A 1 209 ? 5.422 50.598 58.552 1.00 86.57 ? 209 TYR A CB 1 ATOM 1572 C CG . TYR A 1 209 ? 5.104 49.312 59.283 1.00 85.51 ? 209 TYR A CG 1 ATOM 1573 C CD1 . TYR A 1 209 ? 3.787 48.985 59.618 1.00 85.39 ? 209 TYR A CD1 1 ATOM 1574 C CD2 . TYR A 1 209 ? 6.113 48.417 59.634 1.00 84.30 ? 209 TYR A CD2 1 ATOM 1575 C CE1 . TYR A 1 209 ? 3.482 47.801 60.283 1.00 83.82 ? 209 TYR A CE1 1 ATOM 1576 C CE2 . TYR A 1 209 ? 5.819 47.231 60.299 1.00 84.17 ? 209 TYR A CE2 1 ATOM 1577 C CZ . TYR A 1 209 ? 4.501 46.929 60.621 1.00 83.85 ? 209 TYR A CZ 1 ATOM 1578 O OH . TYR A 1 209 ? 4.205 45.761 61.291 1.00 82.73 ? 209 TYR A OH 1 ATOM 1579 N N . VAL A 1 210 ? 4.294 53.061 56.534 1.00 94.17 ? 210 VAL A N 1 ATOM 1580 C CA . VAL A 1 210 ? 4.627 54.295 55.829 1.00 97.44 ? 210 VAL A CA 1 ATOM 1581 C C . VAL A 1 210 ? 5.665 55.149 56.556 1.00 98.37 ? 210 VAL A C 1 ATOM 1582 O O . VAL A 1 210 ? 6.669 54.634 57.045 1.00 99.74 ? 210 VAL A O 1 ATOM 1583 C CB . VAL A 1 210 ? 3.355 55.140 55.579 1.00 98.22 ? 210 VAL A CB 1 ATOM 1584 C CG1 . VAL A 1 210 ? 2.438 54.412 54.609 1.00 98.44 ? 210 VAL A CG1 1 ATOM 1585 C CG2 . VAL A 1 210 ? 2.628 55.388 56.893 1.00 98.49 ? 210 VAL A CG2 1 ATOM 1586 N N . ASN A 1 211 ? 5.412 56.454 56.614 1.00 98.76 ? 211 ASN A N 1 ATOM 1587 C CA . ASN A 1 211 ? 6.300 57.422 57.262 1.00 98.88 ? 211 ASN A CA 1 ATOM 1588 C C . ASN A 1 211 ? 6.810 56.968 58.634 1.00 100.10 ? 211 ASN A C 1 ATOM 1589 O O . ASN A 1 211 ? 7.886 57.372 59.079 1.00 99.50 ? 211 ASN A O 1 ATOM 1590 C CB . ASN A 1 211 ? 5.568 58.758 57.409 1.00 96.38 ? 211 ASN A CB 1 ATOM 1591 C CG . ASN A 1 211 ? 4.486 58.947 56.357 1.00 94.01 ? 211 ASN A CG 1 ATOM 1592 O OD1 . ASN A 1 211 ? 3.562 58.135 56.254 1.00 92.73 ? 211 ASN A OD1 1 ATOM 1593 N ND2 . ASN A 1 211 ? 4.590 60.016 55.573 1.00 91.42 ? 211 ASN A ND2 1 ATOM 1594 N N . GLY A 1 212 ? 6.027 56.135 59.304 1.00 102.19 ? 212 GLY A N 1 ATOM 1595 C CA . GLY A 1 212 ? 6.425 55.658 60.610 1.00 106.02 ? 212 GLY A CA 1 ATOM 1596 C C . GLY A 1 212 ? 5.714 54.375 60.973 1.00 109.21 ? 212 GLY A C 1 ATOM 1597 O O . GLY A 1 212 ? 5.491 53.519 60.120 1.00 109.66 ? 212 GLY A O 1 ATOM 1598 N N . THR A 1 213 ? 5.360 54.246 62.247 1.00 112.68 ? 213 THR A N 1 ATOM 1599 C CA . THR A 1 213 ? 4.671 53.065 62.753 1.00 115.74 ? 213 THR A CA 1 ATOM 1600 C C . THR A 1 213 ? 5.330 51.757 62.328 1.00 117.00 ? 213 THR A C 1 ATOM 1601 O O . THR A 1 213 ? 4.666 50.851 61.826 1.00 117.47 ? 213 THR A O 1 ATOM 1602 C CB . THR A 1 213 ? 3.182 53.046 62.318 1.00 116.72 ? 213 THR A CB 1 ATOM 1603 O OG1 . THR A 1 213 ? 3.073 53.388 60.928 1.00 117.32 ? 213 THR A OG1 1 ATOM 1604 C CG2 . THR A 1 213 ? 2.372 54.025 63.161 1.00 117.28 ? 213 THR A CG2 1 ATOM 1605 N N . MET A 1 214 ? 6.640 51.668 62.536 1.00 118.47 ? 214 MET A N 1 ATOM 1606 C CA . MET A 1 214 ? 7.399 50.469 62.199 1.00 119.90 ? 214 MET A CA 1 ATOM 1607 C C . MET A 1 214 ? 8.337 50.168 63.354 1.00 120.95 ? 214 MET A C 1 ATOM 1608 O O . MET A 1 214 ? 9.339 50.853 63.545 1.00 120.77 ? 214 MET A O 1 ATOM 1609 C CB . MET A 1 214 ? 8.210 50.676 60.921 1.00 119.81 ? 214 MET A CB 1 ATOM 1610 C CG . MET A 1 214 ? 7.944 51.998 60.238 1.00 120.66 ? 214 MET A CG 1 ATOM 1611 S SD . MET A 1 214 ? 8.452 53.386 61.259 1.00 119.91 ? 214 MET A SD 1 ATOM 1612 C CE . MET A 1 214 ? 10.117 53.563 60.695 1.00 121.79 ? 214 MET A CE 1 ATOM 1613 N N . PRO A 1 215 ? 8.013 49.136 64.146 1.00 122.63 ? 215 PRO A N 1 ATOM 1614 C CA . PRO A 1 215 ? 8.800 48.704 65.307 1.00 124.17 ? 215 PRO A CA 1 ATOM 1615 C C . PRO A 1 215 ? 10.283 48.480 65.002 1.00 125.16 ? 215 PRO A C 1 ATOM 1616 O O . PRO A 1 215 ? 10.684 47.384 64.615 1.00 125.61 ? 215 PRO A O 1 ATOM 1617 C CB . PRO A 1 215 ? 8.099 47.415 65.734 1.00 123.97 ? 215 PRO A CB 1 ATOM 1618 C CG . PRO A 1 215 ? 6.673 47.671 65.355 1.00 123.63 ? 215 PRO A CG 1 ATOM 1619 C CD . PRO A 1 215 ? 6.815 48.292 63.985 1.00 122.95 ? 215 PRO A CD 1 ATOM 1620 N N . ASP A 1 216 ? 11.093 49.518 65.187 1.00 125.87 ? 216 ASP A N 1 ATOM 1621 C CA . ASP A 1 216 ? 12.523 49.416 64.929 1.00 126.68 ? 216 ASP A CA 1 ATOM 1622 C C . ASP A 1 216 ? 13.168 48.523 65.982 1.00 127.20 ? 216 ASP A C 1 ATOM 1623 O O . ASP A 1 216 ? 12.496 47.686 66.583 1.00 127.03 ? 216 ASP A O 1 ATOM 1624 C CB . ASP A 1 216 ? 13.156 50.805 64.957 1.00 127.29 ? 216 ASP A CB 1 ATOM 1625 C CG . ASP A 1 216 ? 12.334 51.828 64.194 1.00 128.15 ? 216 ASP A CG 1 ATOM 1626 O OD1 . ASP A 1 216 ? 11.267 52.238 64.703 1.00 128.89 ? 216 ASP A OD1 1 ATOM 1627 O OD2 . ASP A 1 216 ? 12.744 52.215 63.082 1.00 127.59 ? 216 ASP A OD2 1 ATOM 1628 N N . ILE A 1 217 ? 14.466 48.695 66.202 1.00 128.32 ? 217 ILE A N 1 ATOM 1629 C CA . ILE A 1 217 ? 15.178 47.893 67.195 1.00 130.07 ? 217 ILE A CA 1 ATOM 1630 C C . ILE A 1 217 ? 16.569 48.451 67.485 1.00 132.11 ? 217 ILE A C 1 ATOM 1631 O O . ILE A 1 217 ? 17.420 48.506 66.596 1.00 132.78 ? 217 ILE A O 1 ATOM 1632 C CB . ILE A 1 217 ? 15.311 46.421 66.733 1.00 128.37 ? 217 ILE A CB 1 ATOM 1633 C CG1 . ILE A 1 217 ? 16.292 45.669 67.640 1.00 127.04 ? 217 ILE A CG1 1 ATOM 1634 C CG2 . ILE A 1 217 ? 15.742 46.374 65.276 1.00 128.21 ? 217 ILE A CG2 1 ATOM 1635 C CD1 . ILE A 1 217 ? 15.858 45.580 69.088 1.00 125.75 ? 217 ILE A CD1 1 ATOM 1636 N N . THR A 1 218 ? 16.792 48.864 68.733 1.00 133.76 ? 218 THR A N 1 ATOM 1637 C CA . THR A 1 218 ? 18.082 49.419 69.139 1.00 134.76 ? 218 THR A CA 1 ATOM 1638 C C . THR A 1 218 ? 19.200 48.401 68.908 1.00 135.41 ? 218 THR A C 1 ATOM 1639 O O . THR A 1 218 ? 18.945 47.195 68.796 1.00 135.38 ? 218 THR A O 1 ATOM 1640 C CB . THR A 1 218 ? 18.071 49.852 70.630 1.00 134.96 ? 218 THR A CB 1 ATOM 1641 O OG1 . THR A 1 218 ? 17.749 48.730 71.461 1.00 134.92 ? 218 THR A OG1 1 ATOM 1642 C CG2 . THR A 1 218 ? 17.046 50.960 70.855 1.00 134.70 ? 218 THR A CG2 1 ATOM 1643 N N . VAL A 1 219 ? 20.435 48.893 68.834 1.00 135.77 ? 219 VAL A N 1 ATOM 1644 C CA . VAL A 1 219 ? 21.589 48.033 68.586 1.00 135.59 ? 219 VAL A CA 1 ATOM 1645 C C . VAL A 1 219 ? 22.500 47.861 69.795 1.00 135.23 ? 219 VAL A C 1 ATOM 1646 O O . VAL A 1 219 ? 22.583 48.730 70.666 1.00 134.67 ? 219 VAL A O 1 ATOM 1647 C CB . VAL A 1 219 ? 22.443 48.573 67.407 1.00 135.72 ? 219 VAL A CB 1 ATOM 1648 C CG1 . VAL A 1 219 ? 23.549 47.580 67.057 1.00 134.95 ? 219 VAL A CG1 1 ATOM 1649 C CG2 . VAL A 1 219 ? 21.557 48.834 66.198 1.00 135.22 ? 219 VAL A CG2 1 ATOM 1650 N N . CYS A 1 220 ? 23.183 46.722 69.828 1.00 135.26 ? 220 CYS A N 1 ATOM 1651 C CA . CYS A 1 220 ? 24.108 46.393 70.899 1.00 135.51 ? 220 CYS A CA 1 ATOM 1652 C C . CYS A 1 220 ? 25.517 46.773 70.453 1.00 135.42 ? 220 CYS A C 1 ATOM 1653 O O . CYS A 1 220 ? 26.470 46.011 70.629 1.00 135.17 ? 220 CYS A O 1 ATOM 1654 C CB . CYS A 1 220 ? 24.035 44.895 71.202 1.00 135.74 ? 220 CYS A CB 1 ATOM 1655 S SG . CYS A 1 220 ? 22.366 44.306 71.595 1.00 136.65 ? 220 CYS A SG 1 ATOM 1656 N N . ALA A 1 221 ? 25.631 47.962 69.866 1.00 135.37 ? 221 ALA A N 1 ATOM 1657 C CA . ALA A 1 221 ? 26.906 48.478 69.380 1.00 135.16 ? 221 ALA A CA 1 ATOM 1658 C C . ALA A 1 221 ? 26.748 49.930 68.930 1.00 134.88 ? 221 ALA A C 1 ATOM 1659 O O . ALA A 1 221 ? 25.788 50.609 69.305 1.00 133.98 ? 221 ALA A O 1 ATOM 1660 C CB . ALA A 1 221 ? 27.413 47.618 68.218 1.00 135.07 ? 221 ALA A CB 1 ATOM 1661 N N . HIS A 1 228 ? 20.330 41.931 54.919 1.00 67.80 ? 228 HIS A N 1 ATOM 1662 C CA . HIS A 1 228 ? 19.376 41.223 54.070 1.00 68.05 ? 228 HIS A CA 1 ATOM 1663 C C . HIS A 1 228 ? 18.272 42.149 53.558 1.00 66.70 ? 228 HIS A C 1 ATOM 1664 O O . HIS A 1 228 ? 17.131 42.065 54.007 1.00 66.04 ? 228 HIS A O 1 ATOM 1665 C CB . HIS A 1 228 ? 18.747 40.060 54.840 1.00 68.82 ? 228 HIS A CB 1 ATOM 1666 C CG . HIS A 1 228 ? 19.642 38.869 54.981 1.00 71.15 ? 228 HIS A CG 1 ATOM 1667 N ND1 . HIS A 1 228 ? 19.757 37.904 54.003 1.00 71.17 ? 228 HIS A ND1 1 ATOM 1668 C CD2 . HIS A 1 228 ? 20.465 38.485 55.987 1.00 72.20 ? 228 HIS A CD2 1 ATOM 1669 C CE1 . HIS A 1 228 ? 20.612 36.976 54.400 1.00 72.42 ? 228 HIS A CE1 1 ATOM 1670 N NE2 . HIS A 1 228 ? 21.055 37.306 55.601 1.00 73.05 ? 228 HIS A NE2 1 ATOM 1671 N N . LEU A 1 229 ? 18.622 43.017 52.610 1.00 65.60 ? 229 LEU A N 1 ATOM 1672 C CA . LEU A 1 229 ? 17.685 43.967 52.015 1.00 65.65 ? 229 LEU A CA 1 ATOM 1673 C C . LEU A 1 229 ? 16.927 43.401 50.806 1.00 65.53 ? 229 LEU A C 1 ATOM 1674 O O . LEU A 1 229 ? 17.355 42.436 50.179 1.00 66.84 ? 229 LEU A O 1 ATOM 1675 C CB . LEU A 1 229 ? 18.426 45.235 51.587 1.00 67.62 ? 229 LEU A CB 1 ATOM 1676 C CG . LEU A 1 229 ? 19.123 46.085 52.655 1.00 70.27 ? 229 LEU A CG 1 ATOM 1677 C CD1 . LEU A 1 229 ? 20.121 45.234 53.434 1.00 71.19 ? 229 LEU A CD1 1 ATOM 1678 C CD2 . LEU A 1 229 ? 19.826 47.262 51.989 1.00 69.20 ? 229 LEU A CD2 1 ATOM 1679 N N . ILE A 1 230 ? 15.805 44.033 50.479 1.00 64.16 ? 230 ILE A N 1 ATOM 1680 C CA . ILE A 1 230 ? 14.943 43.634 49.371 1.00 61.85 ? 230 ILE A CA 1 ATOM 1681 C C . ILE A 1 230 ? 14.407 44.940 48.800 1.00 61.75 ? 230 ILE A C 1 ATOM 1682 O O . ILE A 1 230 ? 14.473 45.960 49.468 1.00 62.80 ? 230 ILE A O 1 ATOM 1683 C CB . ILE A 1 230 ? 13.772 42.745 49.895 1.00 60.52 ? 230 ILE A CB 1 ATOM 1684 C CG1 . ILE A 1 230 ? 14.300 41.352 50.239 1.00 60.36 ? 230 ILE A CG1 1 ATOM 1685 C CG2 . ILE A 1 230 ? 12.654 42.664 48.887 1.00 59.76 ? 230 ILE A CG2 1 ATOM 1686 C CD1 . ILE A 1 230 ? 13.251 40.391 50.787 1.00 60.02 ? 230 ILE A CD1 1 ATOM 1687 N N . GLY A 1 231 ? 13.893 44.930 47.577 1.00 61.38 ? 231 GLY A N 1 ATOM 1688 C CA . GLY A 1 231 ? 13.384 46.171 47.018 1.00 62.72 ? 231 GLY A CA 1 ATOM 1689 C C . GLY A 1 231 ? 12.289 46.021 45.979 1.00 63.85 ? 231 GLY A C 1 ATOM 1690 O O . GLY A 1 231 ? 12.450 46.445 44.839 1.00 63.90 ? 231 GLY A O 1 ATOM 1691 N N . MET A 1 232 ? 11.161 45.439 46.370 1.00 64.34 ? 232 MET A N 1 ATOM 1692 C CA . MET A 1 232 ? 10.053 45.240 45.444 1.00 64.13 ? 232 MET A CA 1 ATOM 1693 C C . MET A 1 232 ? 9.366 46.555 45.080 1.00 63.93 ? 232 MET A C 1 ATOM 1694 O O . MET A 1 232 ? 9.619 47.590 45.699 1.00 62.05 ? 232 MET A O 1 ATOM 1695 C CB . MET A 1 232 ? 9.036 44.277 46.054 1.00 64.93 ? 232 MET A CB 1 ATOM 1696 C CG . MET A 1 232 ? 8.166 43.579 45.030 1.00 65.75 ? 232 MET A CG 1 ATOM 1697 S SD . MET A 1 232 ? 9.143 42.594 43.906 1.00 66.12 ? 232 MET A SD 1 ATOM 1698 C CE . MET A 1 232 ? 9.831 41.352 45.005 1.00 67.21 ? 232 MET A CE 1 ATOM 1699 N N . SER A 1 233 ? 8.514 46.517 44.059 1.00 63.92 ? 233 SER A N 1 ATOM 1700 C CA . SER A 1 233 ? 7.794 47.713 43.653 1.00 63.75 ? 233 SER A CA 1 ATOM 1701 C C . SER A 1 233 ? 6.951 47.567 42.399 1.00 65.38 ? 233 SER A C 1 ATOM 1702 O O . SER A 1 233 ? 6.435 48.563 41.886 1.00 66.45 ? 233 SER A O 1 ATOM 1703 C CB . SER A 1 233 ? 8.749 48.881 43.469 1.00 62.59 ? 233 SER A CB 1 ATOM 1704 O OG . SER A 1 233 ? 8.038 50.020 43.016 1.00 64.62 ? 233 SER A OG 1 ATOM 1705 N N . SER A 1 234 ? 6.832 46.339 41.894 1.00 65.24 ? 234 SER A N 1 ATOM 1706 C CA . SER A 1 234 ? 6.006 46.045 40.715 1.00 65.28 ? 234 SER A CA 1 ATOM 1707 C C . SER A 1 234 ? 6.314 46.808 39.405 1.00 64.86 ? 234 SER A C 1 ATOM 1708 O O . SER A 1 234 ? 6.233 46.233 38.312 1.00 64.64 ? 234 SER A O 1 ATOM 1709 C CB . SER A 1 234 ? 4.526 46.235 41.090 1.00 64.68 ? 234 SER A CB 1 ATOM 1710 O OG . SER A 1 234 ? 3.674 46.012 39.981 1.00 66.04 ? 234 SER A OG 1 ATOM 1711 N N . GLY A 1 235 ? 6.643 48.093 39.509 1.00 62.26 ? 235 GLY A N 1 ATOM 1712 C CA . GLY A 1 235 ? 6.956 48.873 38.324 1.00 62.25 ? 235 GLY A CA 1 ATOM 1713 C C . GLY A 1 235 ? 8.436 49.225 38.314 1.00 62.44 ? 235 GLY A C 1 ATOM 1714 O O . GLY A 1 235 ? 9.145 48.906 39.269 1.00 59.18 ? 235 GLY A O 1 ATOM 1715 N N . PRO A 1 236 ? 8.935 49.889 37.262 1.00 63.45 ? 236 PRO A N 1 ATOM 1716 C CA . PRO A 1 236 ? 10.359 50.243 37.223 1.00 66.42 ? 236 PRO A CA 1 ATOM 1717 C C . PRO A 1 236 ? 10.659 51.010 38.500 1.00 69.00 ? 236 PRO A C 1 ATOM 1718 O O . PRO A 1 236 ? 9.863 51.860 38.892 1.00 69.68 ? 236 PRO A O 1 ATOM 1719 C CB . PRO A 1 236 ? 10.467 51.147 35.995 1.00 65.96 ? 236 PRO A CB 1 ATOM 1720 C CG . PRO A 1 236 ? 9.272 50.781 35.163 1.00 65.80 ? 236 PRO A CG 1 ATOM 1721 C CD . PRO A 1 236 ? 8.194 50.561 36.186 1.00 63.66 ? 236 PRO A CD 1 ATOM 1722 N N . GLU A 1 237 ? 11.783 50.721 39.152 1.00 71.33 ? 237 GLU A N 1 ATOM 1723 C CA . GLU A 1 237 ? 12.110 51.424 40.391 1.00 74.01 ? 237 GLU A CA 1 ATOM 1724 C C . GLU A 1 237 ? 13.491 51.105 40.970 1.00 74.46 ? 237 GLU A C 1 ATOM 1725 O O . GLU A 1 237 ? 13.985 49.977 40.861 1.00 73.41 ? 237 GLU A O 1 ATOM 1726 C CB . GLU A 1 237 ? 11.029 51.128 41.441 1.00 74.97 ? 237 GLU A CB 1 ATOM 1727 C CG . GLU A 1 237 ? 11.135 51.929 42.735 1.00 78.35 ? 237 GLU A CG 1 ATOM 1728 C CD . GLU A 1 237 ? 10.944 53.427 42.532 1.00 81.55 ? 237 GLU A CD 1 ATOM 1729 O OE1 . GLU A 1 237 ? 11.810 54.066 41.887 1.00 82.77 ? 237 GLU A OE1 1 ATOM 1730 O OE2 . GLU A 1 237 ? 9.924 53.964 43.018 1.00 83.44 ? 237 GLU A OE2 1 ATOM 1731 N N . LEU A 1 238 ? 14.102 52.117 41.587 1.00 76.06 ? 238 LEU A N 1 ATOM 1732 C CA . LEU A 1 238 ? 15.421 51.989 42.219 1.00 78.47 ? 238 LEU A CA 1 ATOM 1733 C C . LEU A 1 238 ? 15.423 52.619 43.615 1.00 77.91 ? 238 LEU A C 1 ATOM 1734 O O . LEU A 1 238 ? 15.053 53.771 43.778 1.00 77.57 ? 238 LEU A O 1 ATOM 1735 C CB . LEU A 1 238 ? 16.503 52.651 41.353 1.00 79.63 ? 238 LEU A CB 1 ATOM 1736 C CG . LEU A 1 238 ? 16.461 54.163 41.090 1.00 81.65 ? 238 LEU A CG 1 ATOM 1737 C CD1 . LEU A 1 238 ? 17.664 54.540 40.232 1.00 81.03 ? 238 LEU A CD1 1 ATOM 1738 C CD2 . LEU A 1 238 ? 15.161 54.563 40.390 1.00 81.84 ? 238 LEU A CD2 1 ATOM 1739 N N . PHE A 1 239 ? 15.850 51.852 44.611 1.00 79.35 ? 239 PHE A N 1 ATOM 1740 C CA . PHE A 1 239 ? 15.898 52.310 45.999 1.00 81.19 ? 239 PHE A CA 1 ATOM 1741 C C . PHE A 1 239 ? 17.337 52.527 46.488 1.00 82.17 ? 239 PHE A C 1 ATOM 1742 O O . PHE A 1 239 ? 18.184 51.653 46.326 1.00 82.23 ? 239 PHE A O 1 ATOM 1743 C CB . PHE A 1 239 ? 15.229 51.270 46.893 1.00 81.50 ? 239 PHE A CB 1 ATOM 1744 C CG . PHE A 1 239 ? 13.880 50.828 46.405 1.00 82.10 ? 239 PHE A CG 1 ATOM 1745 C CD1 . PHE A 1 239 ? 12.802 51.705 46.408 1.00 82.69 ? 239 PHE A CD1 1 ATOM 1746 C CD2 . PHE A 1 239 ? 13.681 49.526 45.961 1.00 81.99 ? 239 PHE A CD2 1 ATOM 1747 C CE1 . PHE A 1 239 ? 11.542 51.293 45.982 1.00 82.91 ? 239 PHE A CE1 1 ATOM 1748 C CE2 . PHE A 1 239 ? 12.425 49.105 45.532 1.00 81.90 ? 239 PHE A CE2 1 ATOM 1749 C CZ . PHE A 1 239 ? 11.353 49.989 45.543 1.00 82.63 ? 239 PHE A CZ 1 ATOM 1750 N N . SER A 1 240 ? 17.606 53.682 47.099 1.00 84.09 ? 240 SER A N 1 ATOM 1751 C CA . SER A 1 240 ? 18.946 53.991 47.611 1.00 85.05 ? 240 SER A CA 1 ATOM 1752 C C . SER A 1 240 ? 18.977 54.043 49.140 1.00 86.76 ? 240 SER A C 1 ATOM 1753 O O . SER A 1 240 ? 19.066 55.116 49.729 1.00 87.40 ? 240 SER A O 1 ATOM 1754 C CB . SER A 1 240 ? 19.434 55.332 47.054 1.00 83.30 ? 240 SER A CB 1 ATOM 1755 O OG . SER A 1 240 ? 19.374 55.360 45.640 1.00 80.93 ? 240 SER A OG 1 ATOM 1756 N N . ILE A 1 241 ? 18.908 52.881 49.778 1.00 89.63 ? 241 ILE A N 1 ATOM 1757 C CA . ILE A 1 241 ? 18.930 52.800 51.237 1.00 92.40 ? 241 ILE A CA 1 ATOM 1758 C C . ILE A 1 241 ? 20.209 53.384 51.833 1.00 95.11 ? 241 ILE A C 1 ATOM 1759 O O . ILE A 1 241 ? 21.286 52.793 51.704 1.00 93.59 ? 241 ILE A O 1 ATOM 1760 C CB . ILE A 1 241 ? 18.824 51.344 51.716 1.00 91.87 ? 241 ILE A CB 1 ATOM 1761 C CG1 . ILE A 1 241 ? 17.500 50.738 51.266 1.00 92.60 ? 241 ILE A CG1 1 ATOM 1762 C CG2 . ILE A 1 241 ? 18.936 51.286 53.229 1.00 92.51 ? 241 ILE A CG2 1 ATOM 1763 C CD1 . ILE A 1 241 ? 17.372 49.265 51.589 1.00 93.82 ? 241 ILE A CD1 1 ATOM 1764 N N . HIS A 1 242 ? 20.084 54.535 52.494 1.00 99.03 ? 242 HIS A N 1 ATOM 1765 C CA . HIS A 1 242 ? 21.229 55.193 53.128 1.00 102.65 ? 242 HIS A CA 1 ATOM 1766 C C . HIS A 1 242 ? 21.235 54.946 54.641 1.00 103.78 ? 242 HIS A C 1 ATOM 1767 O O . HIS A 1 242 ? 20.385 55.458 55.371 1.00 104.31 ? 242 HIS A O 1 ATOM 1768 C CB . HIS A 1 242 ? 21.206 56.706 52.859 1.00 103.69 ? 242 HIS A CB 1 ATOM 1769 C CG . HIS A 1 242 ? 22.364 57.445 53.461 1.00 105.09 ? 242 HIS A CG 1 ATOM 1770 N ND1 . HIS A 1 242 ? 22.400 58.820 53.560 1.00 105.30 ? 242 HIS A ND1 1 ATOM 1771 C CD2 . HIS A 1 242 ? 23.530 57.002 53.989 1.00 105.80 ? 242 HIS A CD2 1 ATOM 1772 C CE1 . HIS A 1 242 ? 23.536 59.191 54.124 1.00 105.13 ? 242 HIS A CE1 1 ATOM 1773 N NE2 . HIS A 1 242 ? 24.240 58.106 54.394 1.00 105.08 ? 242 HIS A NE2 1 ATOM 1774 N N . PHE A 1 243 ? 22.200 54.152 55.098 1.00 104.98 ? 243 PHE A N 1 ATOM 1775 C CA . PHE A 1 243 ? 22.340 53.830 56.514 1.00 105.86 ? 243 PHE A CA 1 ATOM 1776 C C . PHE A 1 243 ? 23.099 54.966 57.199 1.00 107.82 ? 243 PHE A C 1 ATOM 1777 O O . PHE A 1 243 ? 23.768 55.765 56.537 1.00 106.97 ? 243 PHE A O 1 ATOM 1778 C CB . PHE A 1 243 ? 23.134 52.527 56.678 1.00 104.62 ? 243 PHE A CB 1 ATOM 1779 C CG . PHE A 1 243 ? 22.324 51.368 57.193 1.00 103.38 ? 243 PHE A CG 1 ATOM 1780 C CD1 . PHE A 1 243 ? 21.188 50.936 56.520 1.00 103.57 ? 243 PHE A CD1 1 ATOM 1781 C CD2 . PHE A 1 243 ? 22.726 50.681 58.334 1.00 102.99 ? 243 PHE A CD2 1 ATOM 1782 C CE1 . PHE A 1 243 ? 20.463 49.834 56.976 1.00 103.23 ? 243 PHE A CE1 1 ATOM 1783 C CE2 . PHE A 1 243 ? 22.009 49.577 58.799 1.00 103.23 ? 243 PHE A CE2 1 ATOM 1784 C CZ . PHE A 1 243 ? 20.876 49.152 58.119 1.00 102.68 ? 243 PHE A CZ 1 ATOM 1785 N N . ASN A 1 244 ? 22.982 55.038 58.523 1.00 110.05 ? 244 ASN A N 1 ATOM 1786 C CA . ASN A 1 244 ? 23.680 56.051 59.312 1.00 111.23 ? 244 ASN A CA 1 ATOM 1787 C C . ASN A 1 244 ? 24.509 55.339 60.376 1.00 112.79 ? 244 ASN A C 1 ATOM 1788 O O . ASN A 1 244 ? 24.282 55.478 61.577 1.00 112.25 ? 244 ASN A O 1 ATOM 1789 C CB . ASN A 1 244 ? 22.691 57.024 59.959 1.00 110.12 ? 244 ASN A CB 1 ATOM 1790 C CG . ASN A 1 244 ? 22.144 58.044 58.969 1.00 109.82 ? 244 ASN A CG 1 ATOM 1791 O OD1 . ASN A 1 244 ? 21.276 57.735 58.151 1.00 109.04 ? 244 ASN A OD1 1 ATOM 1792 N ND2 . ASN A 1 244 ? 22.665 59.265 59.033 1.00 109.17 ? 244 ASN A ND2 1 ATOM 1793 N N . GLY A 1 245 ? 25.471 54.564 59.889 1.00 114.47 ? 245 GLY A N 1 ATOM 1794 C CA . GLY A 1 245 ? 26.360 53.794 60.735 1.00 116.35 ? 245 GLY A CA 1 ATOM 1795 C C . GLY A 1 245 ? 27.165 52.914 59.799 1.00 117.89 ? 245 GLY A C 1 ATOM 1796 O O . GLY A 1 245 ? 26.596 52.137 59.034 1.00 117.31 ? 245 GLY A O 1 ATOM 1797 N N . GLN A 1 246 ? 28.486 53.051 59.849 1.00 119.92 ? 246 GLN A N 1 ATOM 1798 C CA . GLN A 1 246 ? 29.403 52.290 58.998 1.00 121.70 ? 246 GLN A CA 1 ATOM 1799 C C . GLN A 1 246 ? 29.384 50.765 59.203 1.00 122.60 ? 246 GLN A C 1 ATOM 1800 O O . GLN A 1 246 ? 30.438 50.124 59.227 1.00 122.43 ? 246 GLN A O 1 ATOM 1801 C CB . GLN A 1 246 ? 30.833 52.834 59.186 1.00 122.12 ? 246 GLN A CB 1 ATOM 1802 C CG . GLN A 1 246 ? 31.206 53.143 60.651 1.00 122.08 ? 246 GLN A CG 1 ATOM 1803 C CD . GLN A 1 246 ? 32.559 53.834 60.809 1.00 121.13 ? 246 GLN A CD 1 ATOM 1804 O OE1 . GLN A 1 246 ? 32.801 54.898 60.237 1.00 120.44 ? 246 GLN A OE1 1 ATOM 1805 N NE2 . GLN A 1 246 ? 33.441 53.232 61.600 1.00 120.67 ? 246 GLN A NE2 1 ATOM 1806 N N . VAL A 1 247 ? 28.188 50.191 59.340 1.00 123.78 ? 247 VAL A N 1 ATOM 1807 C CA . VAL A 1 247 ? 28.038 48.744 59.528 1.00 124.32 ? 247 VAL A CA 1 ATOM 1808 C C . VAL A 1 247 ? 27.777 48.036 58.194 1.00 125.85 ? 247 VAL A C 1 ATOM 1809 O O . VAL A 1 247 ? 27.700 46.805 58.142 1.00 126.98 ? 247 VAL A O 1 ATOM 1810 C CB . VAL A 1 247 ? 26.874 48.403 60.514 1.00 122.92 ? 247 VAL A CB 1 ATOM 1811 C CG1 . VAL A 1 247 ? 25.535 48.836 59.929 1.00 121.87 ? 247 VAL A CG1 1 ATOM 1812 C CG2 . VAL A 1 247 ? 26.865 46.908 60.819 1.00 120.96 ? 247 VAL A CG2 1 ATOM 1813 N N . LEU A 1 248 ? 27.643 48.814 57.119 1.00 126.19 ? 248 LEU A N 1 ATOM 1814 C CA . LEU A 1 248 ? 27.394 48.241 55.799 1.00 125.91 ? 248 LEU A CA 1 ATOM 1815 C C . LEU A 1 248 ? 28.710 47.954 55.092 1.00 126.21 ? 248 LEU A C 1 ATOM 1816 O O . LEU A 1 248 ? 29.349 48.846 54.536 1.00 125.90 ? 248 LEU A O 1 ATOM 1817 C CB . LEU A 1 248 ? 26.525 49.175 54.945 1.00 125.43 ? 248 LEU A CB 1 ATOM 1818 C CG . LEU A 1 248 ? 27.073 50.495 54.394 1.00 125.64 ? 248 LEU A CG 1 ATOM 1819 C CD1 . LEU A 1 248 ? 26.011 51.122 53.508 1.00 125.87 ? 248 LEU A CD1 1 ATOM 1820 C CD2 . LEU A 1 248 ? 27.458 51.444 55.518 1.00 125.73 ? 248 LEU A CD2 1 ATOM 1821 N N . GLU A 1 249 ? 29.106 46.688 55.133 1.00 126.98 ? 249 GLU A N 1 ATOM 1822 C CA . GLU A 1 249 ? 30.341 46.228 54.518 1.00 127.77 ? 249 GLU A CA 1 ATOM 1823 C C . GLU A 1 249 ? 30.037 45.228 53.410 1.00 127.64 ? 249 GLU A C 1 ATOM 1824 O O . GLU A 1 249 ? 29.629 44.100 53.690 1.00 127.69 ? 249 GLU A O 1 ATOM 1825 C CB . GLU A 1 249 ? 31.224 45.553 55.575 1.00 129.00 ? 249 GLU A CB 1 ATOM 1826 C CG . GLU A 1 249 ? 32.344 46.416 56.127 1.00 130.81 ? 249 GLU A CG 1 ATOM 1827 C CD . GLU A 1 249 ? 33.458 46.633 55.118 1.00 132.18 ? 249 GLU A CD 1 ATOM 1828 O OE1 . GLU A 1 249 ? 33.963 45.631 54.564 1.00 132.15 ? 249 GLU A OE1 1 ATOM 1829 O OE2 . GLU A 1 249 ? 33.835 47.800 54.882 1.00 132.62 ? 249 GLU A OE2 1 ATOM 1830 N N . GLN A 1 250 ? 30.224 45.637 52.157 1.00 127.50 ? 250 GLN A N 1 ATOM 1831 C CA . GLN A 1 250 ? 29.980 44.735 51.035 1.00 126.93 ? 250 GLN A CA 1 ATOM 1832 C C . GLN A 1 250 ? 31.259 43.982 50.687 1.00 126.80 ? 250 GLN A C 1 ATOM 1833 O O . GLN A 1 250 ? 32.181 44.534 50.086 1.00 126.25 ? 250 GLN A O 1 ATOM 1834 C CB . GLN A 1 250 ? 29.469 45.500 49.809 1.00 126.89 ? 250 GLN A CB 1 ATOM 1835 C CG . GLN A 1 250 ? 28.080 46.107 49.985 1.00 125.98 ? 250 GLN A CG 1 ATOM 1836 C CD . GLN A 1 250 ? 27.382 46.379 48.663 1.00 125.19 ? 250 GLN A CD 1 ATOM 1837 O OE1 . GLN A 1 250 ? 27.911 47.077 47.797 1.00 124.71 ? 250 GLN A OE1 1 ATOM 1838 N NE2 . GLN A 1 250 ? 26.185 45.827 48.504 1.00 124.09 ? 250 GLN A NE2 1 ATOM 1839 N N . ASN A 1 251 ? 31.301 42.716 51.086 1.00 127.17 ? 251 ASN A N 1 ATOM 1840 C CA . ASN A 1 251 ? 32.446 41.850 50.846 1.00 127.79 ? 251 ASN A CA 1 ATOM 1841 C C . ASN A 1 251 ? 33.655 42.287 51.660 1.00 128.37 ? 251 ASN A C 1 ATOM 1842 O O . ASN A 1 251 ? 33.685 42.109 52.877 1.00 128.56 ? 251 ASN A O 1 ATOM 1843 C CB . ASN A 1 251 ? 32.788 41.830 49.359 1.00 127.13 ? 251 ASN A CB 1 ATOM 1844 C CG . ASN A 1 251 ? 31.606 41.435 48.506 1.00 126.77 ? 251 ASN A CG 1 ATOM 1845 O OD1 . ASN A 1 251 ? 30.619 42.163 48.421 1.00 126.46 ? 251 ASN A OD1 1 ATOM 1846 N ND2 . ASN A 1 251 ? 31.693 40.271 47.880 1.00 126.81 ? 251 ASN A ND2 1 ATOM 1847 N N . HIS A 1 252 ? 34.652 42.858 50.996 1.00 129.14 ? 252 HIS A N 1 ATOM 1848 C CA . HIS A 1 252 ? 35.847 43.299 51.701 1.00 129.79 ? 252 HIS A CA 1 ATOM 1849 C C . HIS A 1 252 ? 36.050 44.805 51.553 1.00 129.10 ? 252 HIS A C 1 ATOM 1850 O O . HIS A 1 252 ? 37.181 45.285 51.470 1.00 129.32 ? 252 HIS A O 1 ATOM 1851 C CB . HIS A 1 252 ? 37.077 42.542 51.179 1.00 131.36 ? 252 HIS A CB 1 ATOM 1852 C CG . HIS A 1 252 ? 38.139 42.316 52.215 1.00 132.44 ? 252 HIS A CG 1 ATOM 1853 N ND1 . HIS A 1 252 ? 38.743 43.345 52.905 1.00 132.56 ? 252 HIS A ND1 1 ATOM 1854 C CD2 . HIS A 1 252 ? 38.710 41.174 52.669 1.00 132.43 ? 252 HIS A CD2 1 ATOM 1855 C CE1 . HIS A 1 252 ? 39.639 42.848 53.739 1.00 132.58 ? 252 HIS A CE1 1 ATOM 1856 N NE2 . HIS A 1 252 ? 39.639 41.533 53.615 1.00 132.60 ? 252 HIS A NE2 1 ATOM 1857 N N . HIS A 1 253 ? 34.948 45.548 51.512 1.00 127.93 ? 253 HIS A N 1 ATOM 1858 C CA . HIS A 1 253 ? 35.027 46.998 51.398 1.00 127.07 ? 253 HIS A CA 1 ATOM 1859 C C . HIS A 1 253 ? 33.674 47.657 51.631 1.00 124.64 ? 253 HIS A C 1 ATOM 1860 O O . HIS A 1 253 ? 32.647 47.201 51.128 1.00 124.00 ? 253 HIS A O 1 ATOM 1861 C CB . HIS A 1 253 ? 35.582 47.408 50.031 1.00 129.96 ? 253 HIS A CB 1 ATOM 1862 C CG . HIS A 1 253 ? 36.018 48.840 49.966 1.00 133.11 ? 253 HIS A CG 1 ATOM 1863 N ND1 . HIS A 1 253 ? 35.128 49.893 49.997 1.00 134.76 ? 253 HIS A ND1 1 ATOM 1864 C CD2 . HIS A 1 253 ? 37.253 49.394 49.907 1.00 134.40 ? 253 HIS A CD2 1 ATOM 1865 C CE1 . HIS A 1 253 ? 35.795 51.034 49.961 1.00 135.05 ? 253 HIS A CE1 1 ATOM 1866 N NE2 . HIS A 1 253 ? 37.086 50.759 49.906 1.00 135.80 ? 253 HIS A NE2 1 ATOM 1867 N N . LYS A 1 254 ? 33.692 48.744 52.396 1.00 122.01 ? 254 LYS A N 1 ATOM 1868 C CA . LYS A 1 254 ? 32.483 49.477 52.737 1.00 118.96 ? 254 LYS A CA 1 ATOM 1869 C C . LYS A 1 254 ? 31.981 50.401 51.639 1.00 116.21 ? 254 LYS A C 1 ATOM 1870 O O . LYS A 1 254 ? 32.742 50.862 50.786 1.00 115.39 ? 254 LYS A O 1 ATOM 1871 C CB . LYS A 1 254 ? 32.709 50.288 54.021 1.00 119.72 ? 254 LYS A CB 1 ATOM 1872 C CG . LYS A 1 254 ? 33.738 51.416 53.907 1.00 120.24 ? 254 LYS A CG 1 ATOM 1873 C CD . LYS A 1 254 ? 33.161 52.661 53.227 1.00 120.75 ? 254 LYS A CD 1 ATOM 1874 C CE . LYS A 1 254 ? 31.983 53.240 54.014 1.00 120.51 ? 254 LYS A CE 1 ATOM 1875 N NZ . LYS A 1 254 ? 31.364 54.423 53.344 1.00 120.22 ? 254 LYS A NZ 1 ATOM 1876 N N . ILE A 1 255 ? 30.682 50.670 51.684 1.00 113.10 ? 255 ILE A N 1 ATOM 1877 C CA . ILE A 1 255 ? 30.032 51.554 50.732 1.00 109.57 ? 255 ILE A CA 1 ATOM 1878 C C . ILE A 1 255 ? 29.138 52.506 51.524 1.00 106.24 ? 255 ILE A C 1 ATOM 1879 O O . ILE A 1 255 ? 28.499 52.108 52.497 1.00 105.61 ? 255 ILE A O 1 ATOM 1880 C CB . ILE A 1 255 ? 29.169 50.759 49.728 1.00 109.91 ? 255 ILE A CB 1 ATOM 1881 C CG1 . ILE A 1 255 ? 28.027 50.055 50.462 1.00 110.17 ? 255 ILE A CG1 1 ATOM 1882 C CG2 . ILE A 1 255 ? 30.030 49.727 49.010 1.00 110.70 ? 255 ILE A CG2 1 ATOM 1883 C CD1 . ILE A 1 255 ? 27.049 49.359 49.548 1.00 109.66 ? 255 ILE A CD1 1 ATOM 1884 N N . SER A 1 256 ? 29.107 53.768 51.123 1.00 102.55 ? 256 SER A N 1 ATOM 1885 C CA . SER A 1 256 ? 28.279 54.737 51.820 1.00 99.60 ? 256 SER A CA 1 ATOM 1886 C C . SER A 1 256 ? 26.853 54.206 51.909 1.00 96.90 ? 256 SER A C 1 ATOM 1887 O O . SER A 1 256 ? 26.316 54.018 52.999 1.00 96.72 ? 256 SER A O 1 ATOM 1888 C CB . SER A 1 256 ? 28.297 56.072 51.077 1.00 99.41 ? 256 SER A CB 1 ATOM 1889 O OG . SER A 1 256 ? 29.630 56.512 50.884 1.00 99.93 ? 256 SER A OG 1 ATOM 1890 N N . ALA A 1 257 ? 26.254 53.948 50.752 1.00 94.34 ? 257 ALA A N 1 ATOM 1891 C CA . ALA A 1 257 ? 24.887 53.444 50.692 1.00 91.55 ? 257 ALA A CA 1 ATOM 1892 C C . ALA A 1 257 ? 24.730 52.251 49.749 1.00 88.37 ? 257 ALA A C 1 ATOM 1893 O O . ALA A 1 257 ? 25.635 51.918 48.987 1.00 88.21 ? 257 ALA A O 1 ATOM 1894 C CB . ALA A 1 257 ? 23.940 54.564 50.267 1.00 92.31 ? 257 ALA A CB 1 ATOM 1895 N N . ILE A 1 258 ? 23.567 51.615 49.817 1.00 84.44 ? 258 ILE A N 1 ATOM 1896 C CA . ILE A 1 258 ? 23.255 50.468 48.981 1.00 80.40 ? 258 ILE A CA 1 ATOM 1897 C C . ILE A 1 258 ? 22.157 50.856 47.995 1.00 78.57 ? 258 ILE A C 1 ATOM 1898 O O . ILE A 1 258 ? 21.328 51.720 48.283 1.00 77.99 ? 258 ILE A O 1 ATOM 1899 C CB . ILE A 1 258 ? 22.738 49.277 49.826 1.00 80.73 ? 258 ILE A CB 1 ATOM 1900 C CG1 . ILE A 1 258 ? 23.771 48.896 50.883 1.00 81.00 ? 258 ILE A CG1 1 ATOM 1901 C CG2 . ILE A 1 258 ? 22.445 48.076 48.929 1.00 79.54 ? 258 ILE A CG2 1 ATOM 1902 C CD1 . ILE A 1 258 ? 23.373 47.701 51.719 1.00 81.82 ? 258 ILE A CD1 1 ATOM 1903 N N . THR A 1 259 ? 22.162 50.225 46.824 1.00 76.05 ? 259 THR A N 1 ATOM 1904 C CA . THR A 1 259 ? 21.137 50.492 45.823 1.00 71.58 ? 259 THR A CA 1 ATOM 1905 C C . THR A 1 259 ? 20.413 49.207 45.440 1.00 67.99 ? 259 THR A C 1 ATOM 1906 O O . THR A 1 259 ? 21.015 48.139 45.306 1.00 67.27 ? 259 THR A O 1 ATOM 1907 C CB . THR A 1 259 ? 21.716 51.141 44.556 1.00 70.85 ? 259 THR A CB 1 ATOM 1908 O OG1 . THR A 1 259 ? 22.314 52.399 44.894 1.00 71.86 ? 259 THR A OG1 1 ATOM 1909 C CG2 . THR A 1 259 ? 20.613 51.384 43.546 1.00 70.25 ? 259 THR A CG2 1 ATOM 1910 N N . LEU A 1 260 ? 19.104 49.322 45.288 1.00 63.27 ? 260 LEU A N 1 ATOM 1911 C CA . LEU A 1 260 ? 18.286 48.192 44.920 1.00 59.74 ? 260 LEU A CA 1 ATOM 1912 C C . LEU A 1 260 ? 17.337 48.641 43.831 1.00 57.61 ? 260 LEU A C 1 ATOM 1913 O O . LEU A 1 260 ? 17.200 49.833 43.567 1.00 56.75 ? 260 LEU A O 1 ATOM 1914 C CB . LEU A 1 260 ? 17.492 47.695 46.126 1.00 59.41 ? 260 LEU A CB 1 ATOM 1915 C CG . LEU A 1 260 ? 18.344 47.210 47.294 1.00 61.16 ? 260 LEU A CG 1 ATOM 1916 C CD1 . LEU A 1 260 ? 17.459 46.717 48.449 1.00 60.65 ? 260 LEU A CD1 1 ATOM 1917 C CD2 . LEU A 1 260 ? 19.244 46.102 46.793 1.00 62.60 ? 260 LEU A CD2 1 ATOM 1918 N N . VAL A 1 261 ? 16.699 47.677 43.183 1.00 55.94 ? 261 VAL A N 1 ATOM 1919 C CA . VAL A 1 261 ? 15.743 47.980 42.137 1.00 52.33 ? 261 VAL A CA 1 ATOM 1920 C C . VAL A 1 261 ? 14.552 47.063 42.306 1.00 51.26 ? 261 VAL A C 1 ATOM 1921 O O . VAL A 1 261 ? 14.653 45.987 42.903 1.00 48.09 ? 261 VAL A O 1 ATOM 1922 C CB . VAL A 1 261 ? 16.366 47.807 40.723 1.00 52.74 ? 261 VAL A CB 1 ATOM 1923 C CG1 . VAL A 1 261 ? 17.109 49.086 40.326 1.00 46.53 ? 261 VAL A CG1 1 ATOM 1924 C CG2 . VAL A 1 261 ? 17.325 46.595 40.709 1.00 50.06 ? 261 VAL A CG2 1 ATOM 1925 N N . SER A 1 262 ? 13.431 47.518 41.766 1.00 52.75 ? 262 SER A N 1 ATOM 1926 C CA . SER A 1 262 ? 12.147 46.836 41.817 1.00 55.22 ? 262 SER A CA 1 ATOM 1927 C C . SER A 1 262 ? 12.066 45.366 42.236 1.00 57.47 ? 262 SER A C 1 ATOM 1928 O O . SER A 1 262 ? 11.100 44.979 42.894 1.00 60.17 ? 262 SER A O 1 ATOM 1929 C CB . SER A 1 262 ? 11.446 47.027 40.488 1.00 55.32 ? 262 SER A CB 1 ATOM 1930 O OG . SER A 1 262 ? 11.386 48.407 40.185 1.00 56.60 ? 262 SER A OG 1 ATOM 1931 N N . ALA A 1 263 ? 13.033 44.529 41.883 1.00 55.77 ? 263 ALA A N 1 ATOM 1932 C CA . ALA A 1 263 ? 12.910 43.146 42.317 1.00 57.02 ? 263 ALA A CA 1 ATOM 1933 C C . ALA A 1 263 ? 14.241 42.494 42.585 1.00 58.25 ? 263 ALA A C 1 ATOM 1934 O O . ALA A 1 263 ? 14.420 41.298 42.320 1.00 57.03 ? 263 ALA A O 1 ATOM 1935 C CB . ALA A 1 263 ? 12.127 42.337 41.285 1.00 55.97 ? 263 ALA A CB 1 ATOM 1936 N N . THR A 1 264 ? 15.162 43.273 43.143 1.00 59.65 ? 264 THR A N 1 ATOM 1937 C CA . THR A 1 264 ? 16.502 42.771 43.436 1.00 62.75 ? 264 THR A CA 1 ATOM 1938 C C . THR A 1 264 ? 16.929 42.874 44.894 1.00 64.28 ? 264 THR A C 1 ATOM 1939 O O . THR A 1 264 ? 17.297 43.950 45.352 1.00 65.40 ? 264 THR A O 1 ATOM 1940 C CB . THR A 1 264 ? 17.566 43.507 42.593 1.00 61.96 ? 264 THR A CB 1 ATOM 1941 O OG1 . THR A 1 264 ? 17.648 44.879 43.006 1.00 57.60 ? 264 THR A OG1 1 ATOM 1942 C CG2 . THR A 1 264 ? 17.193 43.440 41.115 1.00 61.06 ? 264 THR A CG2 1 ATOM 1943 N N . SER A 1 265 ? 16.904 41.751 45.607 1.00 65.10 ? 265 SER A N 1 ATOM 1944 C CA . SER A 1 265 ? 17.317 41.732 47.003 1.00 67.31 ? 265 SER A CA 1 ATOM 1945 C C . SER A 1 265 ? 18.841 41.707 47.085 1.00 69.71 ? 265 SER A C 1 ATOM 1946 O O . SER A 1 265 ? 19.517 41.510 46.075 1.00 68.63 ? 265 SER A O 1 ATOM 1947 C CB . SER A 1 265 ? 16.753 40.499 47.717 1.00 68.67 ? 265 SER A CB 1 ATOM 1948 O OG . SER A 1 265 ? 17.395 39.305 47.297 1.00 69.56 ? 265 SER A OG 1 ATOM 1949 N N . THR A 1 266 ? 19.375 41.902 48.291 1.00 73.21 ? 266 THR A N 1 ATOM 1950 C CA . THR A 1 266 ? 20.823 41.902 48.503 1.00 75.90 ? 266 THR A CA 1 ATOM 1951 C C . THR A 1 266 ? 21.214 41.407 49.888 1.00 75.56 ? 266 THR A C 1 ATOM 1952 O O . THR A 1 266 ? 20.521 41.669 50.862 1.00 76.33 ? 266 THR A O 1 ATOM 1953 C CB . THR A 1 266 ? 21.416 43.310 48.317 1.00 77.02 ? 266 THR A CB 1 ATOM 1954 O OG1 . THR A 1 266 ? 21.048 43.812 47.026 1.00 77.79 ? 266 THR A OG1 1 ATOM 1955 C CG2 . THR A 1 266 ? 22.942 43.262 48.420 1.00 77.48 ? 266 THR A CG2 1 ATOM 1956 N N . THR A 1 267 ? 22.332 40.693 49.966 1.00 75.57 ? 267 THR A N 1 ATOM 1957 C CA . THR A 1 267 ? 22.824 40.163 51.237 1.00 76.24 ? 267 THR A CA 1 ATOM 1958 C C . THR A 1 267 ? 24.089 40.877 51.698 1.00 75.77 ? 267 THR A C 1 ATOM 1959 O O . THR A 1 267 ? 24.216 42.087 51.540 1.00 74.99 ? 267 THR A O 1 ATOM 1960 C CB . THR A 1 267 ? 23.137 38.651 51.147 1.00 77.31 ? 267 THR A CB 1 ATOM 1961 O OG1 . THR A 1 267 ? 24.274 38.353 51.971 1.00 77.76 ? 267 THR A OG1 1 ATOM 1962 C CG2 . THR A 1 267 ? 23.413 38.233 49.701 1.00 78.11 ? 267 THR A CG2 1 ATOM 1963 N N . GLY A 1 276 ? 21.016 51.747 70.738 1.00 115.12 ? 276 GLY A N 1 ATOM 1964 C CA . GLY A 1 276 ? 21.243 52.617 69.596 1.00 115.28 ? 276 GLY A CA 1 ATOM 1965 C C . GLY A 1 276 ? 19.953 53.123 68.976 1.00 115.21 ? 276 GLY A C 1 ATOM 1966 O O . GLY A 1 276 ? 18.932 52.437 69.013 1.00 114.68 ? 276 GLY A O 1 ATOM 1967 N N . ARG A 1 277 ? 19.994 54.325 68.406 1.00 115.40 ? 277 ARG A N 1 ATOM 1968 C CA . ARG A 1 277 ? 18.813 54.907 67.778 1.00 115.81 ? 277 ARG A CA 1 ATOM 1969 C C . ARG A 1 277 ? 19.140 55.925 66.684 1.00 115.81 ? 277 ARG A C 1 ATOM 1970 O O . ARG A 1 277 ? 19.423 57.092 66.968 1.00 115.13 ? 277 ARG A O 1 ATOM 1971 C CB . ARG A 1 277 ? 17.922 55.569 68.836 1.00 116.06 ? 277 ARG A CB 1 ATOM 1972 C CG . ARG A 1 277 ? 17.214 54.603 69.779 1.00 116.79 ? 277 ARG A CG 1 ATOM 1973 C CD . ARG A 1 277 ? 16.108 53.832 69.070 1.00 118.31 ? 277 ARG A CD 1 ATOM 1974 N NE . ARG A 1 277 ? 15.098 54.722 68.496 1.00 119.91 ? 277 ARG A NE 1 ATOM 1975 C CZ . ARG A 1 277 ? 13.983 54.310 67.896 1.00 120.11 ? 277 ARG A CZ 1 ATOM 1976 N NH1 . ARG A 1 277 ? 13.725 53.014 67.787 1.00 120.18 ? 277 ARG A NH1 1 ATOM 1977 N NH2 . ARG A 1 277 ? 13.126 55.194 67.397 1.00 119.88 ? 277 ARG A NH2 1 ATOM 1978 N N . TRP A 1 278 ? 19.102 55.470 65.433 1.00 115.76 ? 278 TRP A N 1 ATOM 1979 C CA . TRP A 1 278 ? 19.358 56.331 64.279 1.00 115.83 ? 278 TRP A CA 1 ATOM 1980 C C . TRP A 1 278 ? 18.347 56.079 63.161 1.00 114.74 ? 278 TRP A C 1 ATOM 1981 O O . TRP A 1 278 ? 17.384 55.343 63.351 1.00 114.18 ? 278 TRP A O 1 ATOM 1982 C CB . TRP A 1 278 ? 20.779 56.136 63.747 1.00 117.06 ? 278 TRP A CB 1 ATOM 1983 C CG . TRP A 1 278 ? 21.778 57.072 64.367 1.00 117.61 ? 278 TRP A CG 1 ATOM 1984 C CD1 . TRP A 1 278 ? 22.357 56.959 65.599 1.00 118.00 ? 278 TRP A CD1 1 ATOM 1985 C CD2 . TRP A 1 278 ? 22.315 58.265 63.778 1.00 117.34 ? 278 TRP A CD2 1 ATOM 1986 N NE1 . TRP A 1 278 ? 23.224 58.007 65.812 1.00 118.50 ? 278 TRP A NE1 1 ATOM 1987 C CE2 . TRP A 1 278 ? 23.217 58.822 64.710 1.00 117.66 ? 278 TRP A CE2 1 ATOM 1988 C CE3 . TRP A 1 278 ? 22.120 58.917 62.553 1.00 116.86 ? 278 TRP A CE3 1 ATOM 1989 C CZ2 . TRP A 1 278 ? 23.927 60.002 64.454 1.00 117.32 ? 278 TRP A CZ2 1 ATOM 1990 C CZ3 . TRP A 1 278 ? 22.827 60.092 62.299 1.00 116.57 ? 278 TRP A CZ3 1 ATOM 1991 C CH2 . TRP A 1 278 ? 23.719 60.620 63.247 1.00 116.87 ? 278 TRP A CH2 1 ATOM 1992 N N . THR A 1 279 ? 18.564 56.686 61.998 1.00 113.28 ? 279 THR A N 1 ATOM 1993 C CA . THR A 1 279 ? 17.630 56.529 60.891 1.00 112.17 ? 279 THR A CA 1 ATOM 1994 C C . THR A 1 279 ? 18.221 55.918 59.626 1.00 112.25 ? 279 THR A C 1 ATOM 1995 O O . THR A 1 279 ? 19.402 56.091 59.322 1.00 112.19 ? 279 THR A O 1 ATOM 1996 C CB . THR A 1 279 ? 17.001 57.884 60.516 1.00 111.63 ? 279 THR A CB 1 ATOM 1997 O OG1 . THR A 1 279 ? 16.434 58.486 61.685 1.00 111.72 ? 279 THR A OG1 1 ATOM 1998 C CG2 . THR A 1 279 ? 15.905 57.696 59.484 1.00 111.10 ? 279 THR A CG2 1 ATOM 1999 N N . ILE A 1 280 ? 17.374 55.197 58.896 1.00 111.90 ? 280 ILE A N 1 ATOM 2000 C CA . ILE A 1 280 ? 17.753 54.558 57.643 1.00 110.83 ? 280 ILE A CA 1 ATOM 2001 C C . ILE A 1 280 ? 16.801 55.095 56.586 1.00 110.83 ? 280 ILE A C 1 ATOM 2002 O O . ILE A 1 280 ? 15.704 54.571 56.419 1.00 110.30 ? 280 ILE A O 1 ATOM 2003 C CB . ILE A 1 280 ? 17.587 53.028 57.712 1.00 109.77 ? 280 ILE A CB 1 ATOM 2004 C CG1 . ILE A 1 280 ? 18.438 52.457 58.842 1.00 109.71 ? 280 ILE A CG1 1 ATOM 2005 C CG2 . ILE A 1 280 ? 18.012 52.403 56.403 1.00 109.55 ? 280 ILE A CG2 1 ATOM 2006 C CD1 . ILE A 1 280 ? 18.208 50.986 59.086 1.00 109.41 ? 280 ILE A CD1 1 ATOM 2007 N N . ALA A 1 281 ? 17.219 56.147 55.887 1.00 111.32 ? 281 ALA A N 1 ATOM 2008 C CA . ALA A 1 281 ? 16.390 56.759 54.852 1.00 112.06 ? 281 ALA A CA 1 ATOM 2009 C C . ALA A 1 281 ? 17.002 56.607 53.468 1.00 112.99 ? 281 ALA A C 1 ATOM 2010 O O . ALA A 1 281 ? 18.181 56.286 53.334 1.00 113.59 ? 281 ALA A O 1 ATOM 2011 C CB . ALA A 1 281 ? 16.187 58.228 55.157 1.00 111.22 ? 281 ALA A CB 1 ATOM 2012 N N . SER A 1 282 ? 16.189 56.840 52.442 1.00 113.89 ? 282 SER A N 1 ATOM 2013 C CA . SER A 1 282 ? 16.643 56.744 51.056 1.00 114.89 ? 282 SER A CA 1 ATOM 2014 C C . SER A 1 282 ? 16.617 58.133 50.425 1.00 114.91 ? 282 SER A C 1 ATOM 2015 O O . SER A 1 282 ? 15.594 58.554 49.885 1.00 114.26 ? 282 SER A O 1 ATOM 2016 C CB . SER A 1 282 ? 15.737 55.792 50.262 1.00 115.48 ? 282 SER A CB 1 ATOM 2017 O OG . SER A 1 282 ? 15.882 54.449 50.698 1.00 115.65 ? 282 SER A OG 1 ATOM 2018 N N . LEU A 1 283 ? 17.749 58.833 50.487 1.00 115.41 ? 283 LEU A N 1 ATOM 2019 C CA . LEU A 1 283 ? 17.845 60.188 49.949 1.00 116.16 ? 283 LEU A CA 1 ATOM 2020 C C . LEU A 1 283 ? 17.562 60.281 48.450 1.00 115.69 ? 283 LEU A C 1 ATOM 2021 O O . LEU A 1 283 ? 18.461 60.488 47.631 1.00 115.54 ? 283 LEU A O 1 ATOM 2022 C CB . LEU A 1 283 ? 19.219 60.799 50.269 1.00 117.28 ? 283 LEU A CB 1 ATOM 2023 C CG . LEU A 1 283 ? 19.216 62.292 50.654 1.00 117.72 ? 283 LEU A CG 1 ATOM 2024 C CD1 . LEU A 1 283 ? 20.595 62.708 51.165 1.00 117.66 ? 283 LEU A CD1 1 ATOM 2025 C CD2 . LEU A 1 283 ? 18.798 63.140 49.457 1.00 117.36 ? 283 LEU A CD2 1 ATOM 2026 N N . ILE A 1 284 ? 16.289 60.128 48.110 1.00 114.53 ? 284 ILE A N 1 ATOM 2027 C CA . ILE A 1 284 ? 15.831 60.210 46.739 1.00 113.50 ? 284 ILE A CA 1 ATOM 2028 C C . ILE A 1 284 ? 14.585 61.084 46.778 1.00 113.41 ? 284 ILE A C 1 ATOM 2029 O O . ILE A 1 284 ? 13.672 60.838 47.564 1.00 112.11 ? 284 ILE A O 1 ATOM 2030 C CB . ILE A 1 284 ? 15.469 58.815 46.183 1.00 113.16 ? 284 ILE A CB 1 ATOM 2031 C CG1 . ILE A 1 284 ? 16.658 57.866 46.355 1.00 112.08 ? 284 ILE A CG1 1 ATOM 2032 C CG2 . ILE A 1 284 ? 15.100 58.918 44.705 1.00 112.35 ? 284 ILE A CG2 1 ATOM 2033 C CD1 . ILE A 1 284 ? 16.397 56.453 45.885 1.00 110.36 ? 284 ILE A CD1 1 ATOM 2034 N N . PRO A 1 285 ? 14.544 62.127 45.938 1.00 114.06 ? 285 PRO A N 1 ATOM 2035 C CA . PRO A 1 285 ? 13.450 63.096 45.809 1.00 115.21 ? 285 PRO A CA 1 ATOM 2036 C C . PRO A 1 285 ? 12.015 62.592 45.988 1.00 115.91 ? 285 PRO A C 1 ATOM 2037 O O . PRO A 1 285 ? 11.082 63.393 46.006 1.00 116.76 ? 285 PRO A O 1 ATOM 2038 C CB . PRO A 1 285 ? 13.691 63.682 44.425 1.00 114.90 ? 285 PRO A CB 1 ATOM 2039 C CG . PRO A 1 285 ? 15.179 63.772 44.398 1.00 114.69 ? 285 PRO A CG 1 ATOM 2040 C CD . PRO A 1 285 ? 15.613 62.428 44.969 1.00 114.15 ? 285 PRO A CD 1 ATOM 2041 N N . ARG A 1 286 ? 11.830 61.281 46.112 1.00 116.45 ? 286 ARG A N 1 ATOM 2042 C CA . ARG A 1 286 ? 10.494 60.724 46.303 1.00 117.30 ? 286 ARG A CA 1 ATOM 2043 C C . ARG A 1 286 ? 10.449 59.551 47.286 1.00 117.12 ? 286 ARG A C 1 ATOM 2044 O O . ARG A 1 286 ? 9.479 58.793 47.304 1.00 117.56 ? 286 ARG A O 1 ATOM 2045 C CB . ARG A 1 286 ? 9.884 60.293 44.957 1.00 118.74 ? 286 ARG A CB 1 ATOM 2046 C CG . ARG A 1 286 ? 9.240 61.429 44.154 1.00 120.62 ? 286 ARG A CG 1 ATOM 2047 C CD . ARG A 1 286 ? 8.375 60.905 43.000 1.00 122.08 ? 286 ARG A CD 1 ATOM 2048 N NE . ARG A 1 286 ? 7.650 61.983 42.319 1.00 123.81 ? 286 ARG A NE 1 ATOM 2049 C CZ . ARG A 1 286 ? 6.761 61.800 41.344 1.00 123.73 ? 286 ARG A CZ 1 ATOM 2050 N NH1 . ARG A 1 286 ? 6.474 60.576 40.921 1.00 123.33 ? 286 ARG A NH1 1 ATOM 2051 N NH2 . ARG A 1 286 ? 6.152 62.842 40.793 1.00 123.76 ? 286 ARG A NH2 1 ATOM 2052 N N . HIS A 1 287 ? 11.489 59.404 48.104 1.00 116.20 ? 287 HIS A N 1 ATOM 2053 C CA . HIS A 1 287 ? 11.541 58.321 49.086 1.00 115.42 ? 287 HIS A CA 1 ATOM 2054 C C . HIS A 1 287 ? 11.670 58.855 50.506 1.00 114.74 ? 287 HIS A C 1 ATOM 2055 O O . HIS A 1 287 ? 10.929 58.458 51.406 1.00 113.54 ? 287 HIS A O 1 ATOM 2056 C CB . HIS A 1 287 ? 12.717 57.384 48.799 1.00 116.26 ? 287 HIS A CB 1 ATOM 2057 C CG . HIS A 1 287 ? 12.497 56.474 47.631 1.00 117.39 ? 287 HIS A CG 1 ATOM 2058 N ND1 . HIS A 1 287 ? 13.408 55.508 47.262 1.00 117.07 ? 287 HIS A ND1 1 ATOM 2059 C CD2 . HIS A 1 287 ? 11.475 56.386 46.747 1.00 117.96 ? 287 HIS A CD2 1 ATOM 2060 C CE1 . HIS A 1 287 ? 12.956 54.866 46.200 1.00 118.06 ? 287 HIS A CE1 1 ATOM 2061 N NE2 . HIS A 1 287 ? 11.786 55.379 45.867 1.00 117.74 ? 287 HIS A NE2 1 ATOM 2062 N N . PHE A 1 288 ? 12.634 59.748 50.698 1.00 114.49 ? 288 PHE A N 1 ATOM 2063 C CA . PHE A 1 288 ? 12.882 60.362 51.996 1.00 113.95 ? 288 PHE A CA 1 ATOM 2064 C C . PHE A 1 288 ? 11.893 61.511 52.216 1.00 113.66 ? 288 PHE A C 1 ATOM 2065 O O . PHE A 1 288 ? 11.596 61.877 53.356 1.00 113.91 ? 288 PHE A O 1 ATOM 2066 C CB . PHE A 1 288 ? 14.326 60.875 52.051 1.00 113.53 ? 288 PHE A CB 1 ATOM 2067 C CG . PHE A 1 288 ? 14.624 61.739 53.241 1.00 113.11 ? 288 PHE A CG 1 ATOM 2068 C CD1 . PHE A 1 288 ? 14.458 61.251 54.532 1.00 112.58 ? 288 PHE A CD1 1 ATOM 2069 C CD2 . PHE A 1 288 ? 15.075 63.046 53.068 1.00 112.92 ? 288 PHE A CD2 1 ATOM 2070 C CE1 . PHE A 1 288 ? 14.735 62.054 55.635 1.00 112.81 ? 288 PHE A CE1 1 ATOM 2071 C CE2 . PHE A 1 288 ? 15.355 63.856 54.162 1.00 112.29 ? 288 PHE A CE2 1 ATOM 2072 C CZ . PHE A 1 288 ? 15.184 63.361 55.448 1.00 112.30 ? 288 PHE A CZ 1 ATOM 2073 N N . GLN A 1 289 ? 11.383 62.065 51.114 1.00 111.93 ? 289 GLN A N 1 ATOM 2074 C CA . GLN A 1 289 ? 10.424 63.165 51.160 1.00 109.92 ? 289 GLN A CA 1 ATOM 2075 C C . GLN A 1 289 ? 9.000 62.611 51.099 1.00 108.88 ? 289 GLN A C 1 ATOM 2076 O O . GLN A 1 289 ? 8.074 63.300 50.673 1.00 108.46 ? 289 GLN A O 1 ATOM 2077 C CB . GLN A 1 289 ? 10.664 64.118 49.983 1.00 109.65 ? 289 GLN A CB 1 ATOM 2078 C CG . GLN A 1 289 ? 9.944 65.456 50.098 1.00 112.77 ? 289 GLN A CG 1 ATOM 2079 C CD . GLN A 1 289 ? 10.269 66.199 51.396 1.00 114.21 ? 289 GLN A CD 1 ATOM 2080 O OE1 . GLN A 1 289 ? 11.436 66.455 51.707 1.00 114.35 ? 289 GLN A OE1 1 ATOM 2081 N NE2 . GLN A 1 289 ? 9.232 66.551 52.154 1.00 113.65 ? 289 GLN A NE2 1 ATOM 2082 N N . ALA A 1 290 ? 8.837 61.362 51.535 1.00 107.84 ? 290 ALA A N 1 ATOM 2083 C CA . ALA A 1 290 ? 7.536 60.700 51.522 1.00 106.74 ? 290 ALA A CA 1 ATOM 2084 C C . ALA A 1 290 ? 7.403 59.634 52.602 1.00 106.45 ? 290 ALA A C 1 ATOM 2085 O O . ALA A 1 290 ? 6.496 58.798 52.547 1.00 106.07 ? 290 ALA A O 1 ATOM 2086 C CB . ALA A 1 290 ? 7.277 60.081 50.157 1.00 107.40 ? 290 ALA A CB 1 ATOM 2087 N N . GLY A 1 291 ? 8.321 59.639 53.564 1.00 106.31 ? 291 GLY A N 1 ATOM 2088 C CA . GLY A 1 291 ? 8.234 58.687 54.658 1.00 107.65 ? 291 GLY A CA 1 ATOM 2089 C C . GLY A 1 291 ? 9.094 57.436 54.686 1.00 108.59 ? 291 GLY A C 1 ATOM 2090 O O . GLY A 1 291 ? 9.190 56.797 55.732 1.00 108.52 ? 291 GLY A O 1 ATOM 2091 N N . MET A 1 292 ? 9.710 57.065 53.568 1.00 109.50 ? 292 MET A N 1 ATOM 2092 C CA . MET A 1 292 ? 10.544 55.866 53.556 1.00 110.32 ? 292 MET A CA 1 ATOM 2093 C C . MET A 1 292 ? 11.782 56.033 54.433 1.00 110.28 ? 292 MET A C 1 ATOM 2094 O O . MET A 1 292 ? 12.784 56.615 54.010 1.00 110.20 ? 292 MET A O 1 ATOM 2095 C CB . MET A 1 292 ? 10.970 55.515 52.126 1.00 111.89 ? 292 MET A CB 1 ATOM 2096 C CG . MET A 1 292 ? 9.860 54.919 51.261 1.00 112.60 ? 292 MET A CG 1 ATOM 2097 S SD . MET A 1 292 ? 10.426 54.477 49.597 1.00 111.72 ? 292 MET A SD 1 ATOM 2098 C CE . MET A 1 292 ? 11.181 52.878 49.923 1.00 111.38 ? 292 MET A CE 1 ATOM 2099 N N . GLN A 1 293 ? 11.700 55.523 55.659 1.00 109.98 ? 293 GLN A N 1 ATOM 2100 C CA . GLN A 1 293 ? 12.811 55.599 56.603 1.00 109.65 ? 293 GLN A CA 1 ATOM 2101 C C . GLN A 1 293 ? 12.647 54.598 57.736 1.00 108.61 ? 293 GLN A C 1 ATOM 2102 O O . GLN A 1 293 ? 11.638 54.597 58.432 1.00 108.43 ? 293 GLN A O 1 ATOM 2103 C CB . GLN A 1 293 ? 12.937 57.018 57.175 1.00 110.77 ? 293 GLN A CB 1 ATOM 2104 C CG . GLN A 1 293 ? 11.769 57.494 58.032 1.00 111.57 ? 293 GLN A CG 1 ATOM 2105 C CD . GLN A 1 293 ? 11.935 58.939 58.494 1.00 112.99 ? 293 GLN A CD 1 ATOM 2106 O OE1 . GLN A 1 293 ? 11.173 59.431 59.329 1.00 112.89 ? 293 GLN A OE1 1 ATOM 2107 N NE2 . GLN A 1 293 ? 12.933 59.625 57.944 1.00 113.83 ? 293 GLN A NE2 1 ATOM 2108 N N . ALA A 1 294 ? 13.643 53.738 57.910 1.00 108.34 ? 294 ALA A N 1 ATOM 2109 C CA . ALA A 1 294 ? 13.602 52.736 58.963 1.00 108.78 ? 294 ALA A CA 1 ATOM 2110 C C . ALA A 1 294 ? 14.657 53.056 60.013 1.00 109.83 ? 294 ALA A C 1 ATOM 2111 O O . ALA A 1 294 ? 15.808 52.637 59.900 1.00 110.08 ? 294 ALA A O 1 ATOM 2112 C CB . ALA A 1 294 ? 13.845 51.353 58.382 1.00 107.94 ? 294 ALA A CB 1 ATOM 2113 N N . TYR A 1 295 ? 14.246 53.804 61.034 1.00 110.32 ? 295 TYR A N 1 ATOM 2114 C CA . TYR A 1 295 ? 15.124 54.210 62.128 1.00 110.63 ? 295 TYR A CA 1 ATOM 2115 C C . TYR A 1 295 ? 15.837 53.014 62.764 1.00 111.29 ? 295 TYR A C 1 ATOM 2116 O O . TYR A 1 295 ? 15.196 52.060 63.209 1.00 110.77 ? 295 TYR A O 1 ATOM 2117 C CB . TYR A 1 295 ? 14.306 54.942 63.195 1.00 109.36 ? 295 TYR A CB 1 ATOM 2118 C CG . TYR A 1 295 ? 13.153 55.746 62.628 1.00 109.61 ? 295 TYR A CG 1 ATOM 2119 C CD1 . TYR A 1 295 ? 13.378 56.835 61.784 1.00 108.80 ? 295 TYR A CD1 1 ATOM 2120 C CD2 . TYR A 1 295 ? 11.831 55.398 62.914 1.00 109.61 ? 295 TYR A CD2 1 ATOM 2121 C CE1 . TYR A 1 295 ? 12.313 57.552 61.236 1.00 108.40 ? 295 TYR A CE1 1 ATOM 2122 C CE2 . TYR A 1 295 ? 10.760 56.111 62.369 1.00 109.00 ? 295 TYR A CE2 1 ATOM 2123 C CZ . TYR A 1 295 ? 11.006 57.182 61.530 1.00 108.48 ? 295 TYR A CZ 1 ATOM 2124 O OH . TYR A 1 295 ? 9.942 57.860 60.973 1.00 107.51 ? 295 TYR A OH 1 ATOM 2125 N N . ILE A 1 296 ? 17.167 53.074 62.805 1.00 112.45 ? 296 ILE A N 1 ATOM 2126 C CA . ILE A 1 296 ? 17.969 52.003 63.387 1.00 113.22 ? 296 ILE A CA 1 ATOM 2127 C C . ILE A 1 296 ? 17.515 51.747 64.820 1.00 113.68 ? 296 ILE A C 1 ATOM 2128 O O . ILE A 1 296 ? 16.775 52.595 65.362 1.00 113.83 ? 296 ILE A O 1 ATOM 2129 C CB . ILE A 1 296 ? 19.473 52.373 63.406 1.00 113.77 ? 296 ILE A CB 1 ATOM 2130 C CG1 . ILE A 1 296 ? 19.931 52.791 62.006 1.00 114.84 ? 296 ILE A CG1 1 ATOM 2131 C CG2 . ILE A 1 296 ? 20.298 51.184 63.878 1.00 113.68 ? 296 ILE A CG2 1 ATOM 2132 C CD1 . ILE A 1 296 ? 21.379 53.256 61.943 1.00 114.30 ? 296 ILE A CD1 1 ATOM 2133 N N . ASN B 2 2 ? 52.032 41.567 18.437 1.00 72.55 ? 1538 ASN B N 1 ATOM 2134 C CA . ASN B 2 2 ? 52.312 41.896 17.004 1.00 74.44 ? 1538 ASN B CA 1 ATOM 2135 C C . ASN B 2 2 ? 51.075 41.548 16.170 1.00 75.48 ? 1538 ASN B C 1 ATOM 2136 O O . ASN B 2 2 ? 51.085 41.637 14.933 1.00 73.29 ? 1538 ASN B O 1 ATOM 2137 C CB . ASN B 2 2 ? 53.527 41.085 16.521 1.00 73.06 ? 1538 ASN B CB 1 ATOM 2138 C CG . ASN B 2 2 ? 53.193 39.624 16.250 1.00 71.28 ? 1538 ASN B CG 1 ATOM 2139 O OD1 . ASN B 2 2 ? 52.634 39.293 15.203 1.00 69.41 ? 1538 ASN B OD1 1 ATOM 2140 N ND2 . ASN B 2 2 ? 53.524 38.748 17.197 1.00 67.70 ? 1538 ASN B ND2 1 ATOM 2141 N N . THR B 2 3 ? 50.018 41.160 16.891 1.00 77.16 ? 1539 THR B N 1 ATOM 2142 C CA . THR B 2 3 ? 48.718 40.746 16.347 1.00 76.40 ? 1539 THR B CA 1 ATOM 2143 C C . THR B 2 3 ? 48.025 41.689 15.356 1.00 76.34 ? 1539 THR B C 1 ATOM 2144 O O . THR B 2 3 ? 47.883 41.352 14.178 1.00 76.36 ? 1539 THR B O 1 ATOM 2145 C CB . THR B 2 3 ? 47.739 40.445 17.507 1.00 77.94 ? 1539 THR B CB 1 ATOM 2146 O OG1 . THR B 2 3 ? 48.107 41.234 18.650 1.00 78.26 ? 1539 THR B OG1 1 ATOM 2147 C CG2 . THR B 2 3 ? 47.763 38.954 17.871 1.00 77.72 ? 1539 THR B CG2 1 ATOM 2148 N N . GLY B 2 4 ? 47.573 42.847 15.836 1.00 74.90 ? 1540 GLY B N 1 ATOM 2149 C CA . GLY B 2 4 ? 46.903 43.811 14.974 1.00 72.98 ? 1540 GLY B CA 1 ATOM 2150 C C . GLY B 2 4 ? 46.096 43.285 13.783 1.00 72.75 ? 1540 GLY B C 1 ATOM 2151 O O . GLY B 2 4 ? 45.992 43.987 12.763 1.00 73.03 ? 1540 GLY B O 1 ATOM 2152 N N . ASN B 2 5 ? 45.525 42.077 13.895 1.00 70.14 ? 1541 ASN B N 1 ATOM 2153 C CA . ASN B 2 5 ? 44.716 41.483 12.816 1.00 66.76 ? 1541 ASN B CA 1 ATOM 2154 C C . ASN B 2 5 ? 43.532 42.364 12.426 1.00 66.03 ? 1541 ASN B C 1 ATOM 2155 O O . ASN B 2 5 ? 42.790 42.843 13.285 1.00 66.55 ? 1541 ASN B O 1 ATOM 2156 C CB . ASN B 2 5 ? 44.176 40.111 13.230 1.00 65.07 ? 1541 ASN B CB 1 ATOM 2157 C CG . ASN B 2 5 ? 45.000 38.955 12.673 1.00 65.35 ? 1541 ASN B CG 1 ATOM 2158 O OD1 . ASN B 2 5 ? 44.940 38.642 11.470 1.00 61.60 ? 1541 ASN B OD1 1 ATOM 2159 N ND2 . ASN B 2 5 ? 45.778 38.313 13.548 1.00 61.58 ? 1541 ASN B ND2 1 ATOM 2160 N N . ARG B 2 6 ? 43.354 42.583 11.128 1.00 64.05 ? 1542 ARG B N 1 ATOM 2161 C CA . ARG B 2 6 ? 42.240 43.395 10.646 1.00 63.42 ? 1542 ARG B CA 1 ATOM 2162 C C . ARG B 2 6 ? 41.016 42.506 10.546 1.00 62.47 ? 1542 ARG B C 1 ATOM 2163 O O . ARG B 2 6 ? 41.083 41.403 9.993 1.00 61.86 ? 1542 ARG B O 1 ATOM 2164 C CB . ARG B 2 6 ? 42.507 43.976 9.250 1.00 62.44 ? 1542 ARG B CB 1 ATOM 2165 C CG . ARG B 2 6 ? 43.801 44.749 9.104 1.00 64.16 ? 1542 ARG B CG 1 ATOM 2166 C CD . ARG B 2 6 ? 44.990 43.864 8.691 1.00 69.22 ? 1542 ARG B CD 1 ATOM 2167 N NE . ARG B 2 6 ? 45.157 42.644 9.491 1.00 72.30 ? 1542 ARG B NE 1 ATOM 2168 C CZ . ARG B 2 6 ? 44.681 41.439 9.165 1.00 72.16 ? 1542 ARG B CZ 1 ATOM 2169 N NH1 . ARG B 2 6 ? 43.997 41.260 8.042 1.00 69.36 ? 1542 ARG B NH1 1 ATOM 2170 N NH2 . ARG B 2 6 ? 44.884 40.405 9.973 1.00 73.19 ? 1542 ARG B NH2 1 ATOM 2171 N N . LYS B 2 7 ? 39.901 42.969 11.090 1.00 58.77 ? 1543 LYS B N 1 ATOM 2172 C CA . LYS B 2 7 ? 38.681 42.209 10.989 1.00 57.25 ? 1543 LYS B CA 1 ATOM 2173 C C . LYS B 2 7 ? 37.748 43.020 10.099 1.00 54.70 ? 1543 LYS B C 1 ATOM 2174 O O . LYS B 2 7 ? 37.294 44.095 10.473 1.00 52.38 ? 1543 LYS B O 1 ATOM 2175 C CB . LYS B 2 7 ? 38.098 41.973 12.374 1.00 58.99 ? 1543 LYS B CB 1 ATOM 2176 C CG . LYS B 2 7 ? 38.851 40.921 13.185 1.00 60.67 ? 1543 LYS B CG 1 ATOM 2177 C CD . LYS B 2 7 ? 38.331 39.504 12.911 1.00 66.02 ? 1543 LYS B CD 1 ATOM 2178 C CE . LYS B 2 7 ? 38.974 38.859 11.666 1.00 69.27 ? 1543 LYS B CE 1 ATOM 2179 N NZ . LYS B 2 7 ? 38.362 37.545 11.223 1.00 64.58 ? 1543 LYS B NZ 1 ATOM 2180 N N . TYR B 2 8 ? 37.501 42.503 8.898 1.00 52.64 ? 1544 TYR B N 1 ATOM 2181 C CA . TYR B 2 8 ? 36.643 43.159 7.916 1.00 49.97 ? 1544 TYR B CA 1 ATOM 2182 C C . TYR B 2 8 ? 35.147 42.863 8.094 1.00 47.06 ? 1544 TYR B C 1 ATOM 2183 O O . TYR B 2 8 ? 34.731 41.721 8.280 1.00 44.40 ? 1544 TYR B O 1 ATOM 2184 C CB . TYR B 2 8 ? 37.052 42.744 6.496 1.00 53.58 ? 1544 TYR B CB 1 ATOM 2185 C CG . TYR B 2 8 ? 38.445 43.159 6.052 1.00 55.32 ? 1544 TYR B CG 1 ATOM 2186 C CD1 . TYR B 2 8 ? 38.694 44.444 5.555 1.00 53.51 ? 1544 TYR B CD1 1 ATOM 2187 C CD2 . TYR B 2 8 ? 39.512 42.249 6.098 1.00 56.48 ? 1544 TYR B CD2 1 ATOM 2188 C CE1 . TYR B 2 8 ? 39.962 44.809 5.111 1.00 52.99 ? 1544 TYR B CE1 1 ATOM 2189 C CE2 . TYR B 2 8 ? 40.789 42.607 5.657 1.00 54.62 ? 1544 TYR B CE2 1 ATOM 2190 C CZ . TYR B 2 8 ? 41.004 43.885 5.163 1.00 54.91 ? 1544 TYR B CZ 1 ATOM 2191 O OH . TYR B 2 8 ? 42.256 44.225 4.710 1.00 54.84 ? 1544 TYR B OH 1 ATOM 2192 N N . TYR B 2 9 ? 34.353 43.921 8.018 1.00 45.40 ? 1545 TYR B N 1 ATOM 2193 C CA . TYR B 2 9 ? 32.910 43.840 8.131 1.00 42.13 ? 1545 TYR B CA 1 ATOM 2194 C C . TYR B 2 9 ? 32.357 44.835 7.138 1.00 43.04 ? 1545 TYR B C 1 ATOM 2195 O O . TYR B 2 9 ? 32.870 45.950 7.028 1.00 42.69 ? 1545 TYR B O 1 ATOM 2196 C CB . TYR B 2 9 ? 32.445 44.242 9.524 1.00 39.15 ? 1545 TYR B CB 1 ATOM 2197 C CG . TYR B 2 9 ? 32.759 43.226 10.585 1.00 41.09 ? 1545 TYR B CG 1 ATOM 2198 C CD1 . TYR B 2 9 ? 31.958 42.085 10.748 1.00 40.80 ? 1545 TYR B CD1 1 ATOM 2199 C CD2 . TYR B 2 9 ? 33.861 43.384 11.411 1.00 36.39 ? 1545 TYR B CD2 1 ATOM 2200 C CE1 . TYR B 2 9 ? 32.254 41.140 11.708 1.00 41.44 ? 1545 TYR B CE1 1 ATOM 2201 C CE2 . TYR B 2 9 ? 34.168 42.442 12.373 1.00 40.36 ? 1545 TYR B CE2 1 ATOM 2202 C CZ . TYR B 2 9 ? 33.365 41.321 12.522 1.00 41.92 ? 1545 TYR B CZ 1 ATOM 2203 O OH . TYR B 2 9 ? 33.686 40.390 13.491 1.00 42.64 ? 1545 TYR B OH 1 ATOM 2204 N N . TYR B 2 10 ? 31.337 44.408 6.400 1.00 42.75 ? 1546 TYR B N 1 ATOM 2205 C CA . TYR B 2 10 ? 30.654 45.252 5.443 1.00 42.34 ? 1546 TYR B CA 1 ATOM 2206 C C . TYR B 2 10 ? 29.216 45.265 5.958 1.00 43.73 ? 1546 TYR B C 1 ATOM 2207 O O . TYR B 2 10 ? 28.454 44.320 5.744 1.00 45.63 ? 1546 TYR B O 1 ATOM 2208 C CB . TYR B 2 10 ? 30.718 44.651 4.044 1.00 42.40 ? 1546 TYR B CB 1 ATOM 2209 C CG . TYR B 2 10 ? 32.101 44.209 3.624 1.00 46.35 ? 1546 TYR B CG 1 ATOM 2210 C CD1 . TYR B 2 10 ? 32.596 42.951 3.987 1.00 44.93 ? 1546 TYR B CD1 1 ATOM 2211 C CD2 . TYR B 2 10 ? 32.926 45.049 2.858 1.00 46.98 ? 1546 TYR B CD2 1 ATOM 2212 C CE1 . TYR B 2 10 ? 33.872 42.539 3.601 1.00 45.44 ? 1546 TYR B CE1 1 ATOM 2213 C CE2 . TYR B 2 10 ? 34.209 44.640 2.466 1.00 47.44 ? 1546 TYR B CE2 1 ATOM 2214 C CZ . TYR B 2 10 ? 34.672 43.386 2.843 1.00 46.93 ? 1546 TYR B CZ 1 ATOM 2215 O OH . TYR B 2 10 ? 35.934 42.978 2.466 1.00 50.18 ? 1546 TYR B OH 1 ATOM 2216 N N . ILE B 2 11 ? 28.859 46.333 6.657 1.00 43.66 ? 1547 ILE B N 1 ATOM 2217 C CA . ILE B 2 11 ? 27.533 46.471 7.246 1.00 44.61 ? 1547 ILE B CA 1 ATOM 2218 C C . ILE B 2 11 ? 26.752 47.630 6.649 1.00 44.95 ? 1547 ILE B C 1 ATOM 2219 O O . ILE B 2 11 ? 27.301 48.705 6.454 1.00 46.55 ? 1547 ILE B O 1 ATOM 2220 C CB . ILE B 2 11 ? 27.664 46.708 8.744 1.00 43.43 ? 1547 ILE B CB 1 ATOM 2221 C CG1 . ILE B 2 11 ? 28.610 45.660 9.329 1.00 44.78 ? 1547 ILE B CG1 1 ATOM 2222 C CG2 . ILE B 2 11 ? 26.307 46.644 9.401 1.00 45.65 ? 1547 ILE B CG2 1 ATOM 2223 C CD1 . ILE B 2 11 ? 28.879 45.825 10.807 1.00 47.53 ? 1547 ILE B CD1 1 ATOM 2224 N N . ALA B 2 12 ? 25.473 47.419 6.356 1.00 44.66 ? 1548 ALA B N 1 ATOM 2225 C CA . ALA B 2 12 ? 24.664 48.497 5.801 1.00 45.03 ? 1548 ALA B CA 1 ATOM 2226 C C . ALA B 2 12 ? 23.425 48.783 6.641 1.00 47.48 ? 1548 ALA B C 1 ATOM 2227 O O . ALA B 2 12 ? 22.957 47.929 7.412 1.00 48.41 ? 1548 ALA B O 1 ATOM 2228 C CB . ALA B 2 12 ? 24.259 48.173 4.391 1.00 43.34 ? 1548 ALA B CB 1 ATOM 2229 N N . ALA B 2 13 ? 22.912 50.003 6.512 1.00 47.04 ? 1549 ALA B N 1 ATOM 2230 C CA . ALA B 2 13 ? 21.706 50.394 7.223 1.00 47.07 ? 1549 ALA B CA 1 ATOM 2231 C C . ALA B 2 13 ? 20.586 50.257 6.199 1.00 48.74 ? 1549 ALA B C 1 ATOM 2232 O O . ALA B 2 13 ? 20.662 50.822 5.105 1.00 47.07 ? 1549 ALA B O 1 ATOM 2233 C CB . ALA B 2 13 ? 21.817 51.815 7.696 1.00 47.33 ? 1549 ALA B CB 1 ATOM 2234 N N . GLU B 2 14 ? 19.556 49.489 6.544 1.00 50.21 ? 1550 GLU B N 1 ATOM 2235 C CA . GLU B 2 14 ? 18.445 49.260 5.625 1.00 51.20 ? 1550 GLU B CA 1 ATOM 2236 C C . GLU B 2 14 ? 17.057 49.368 6.235 1.00 49.59 ? 1550 GLU B C 1 ATOM 2237 O O . GLU B 2 14 ? 16.841 49.079 7.416 1.00 47.73 ? 1550 GLU B O 1 ATOM 2238 C CB . GLU B 2 14 ? 18.571 47.883 4.977 1.00 53.26 ? 1550 GLU B CB 1 ATOM 2239 C CG . GLU B 2 14 ? 19.766 47.708 4.076 1.00 55.62 ? 1550 GLU B CG 1 ATOM 2240 C CD . GLU B 2 14 ? 19.947 46.260 3.660 1.00 58.91 ? 1550 GLU B CD 1 ATOM 2241 O OE1 . GLU B 2 14 ? 19.001 45.660 3.091 1.00 59.23 ? 1550 GLU B OE1 1 ATOM 2242 O OE2 . GLU B 2 14 ? 21.042 45.722 3.912 1.00 58.73 ? 1550 GLU B OE2 1 ATOM 2243 N N . GLU B 2 15 ? 16.120 49.778 5.393 1.00 48.43 ? 1551 GLU B N 1 ATOM 2244 C CA . GLU B 2 15 ? 14.736 49.928 5.786 1.00 48.82 ? 1551 GLU B CA 1 ATOM 2245 C C . GLU B 2 15 ? 14.053 48.600 5.535 1.00 46.33 ? 1551 GLU B C 1 ATOM 2246 O O . GLU B 2 15 ? 14.226 47.997 4.482 1.00 47.42 ? 1551 GLU B O 1 ATOM 2247 C CB . GLU B 2 15 ? 14.082 51.041 4.967 1.00 51.48 ? 1551 GLU B CB 1 ATOM 2248 C CG . GLU B 2 15 ? 14.094 52.395 5.659 1.00 55.28 ? 1551 GLU B CG 1 ATOM 2249 C CD . GLU B 2 15 ? 14.199 53.564 4.693 1.00 56.83 ? 1551 GLU B CD 1 ATOM 2250 O OE1 . GLU B 2 15 ? 13.426 53.615 3.709 1.00 56.88 ? 1551 GLU B OE1 1 ATOM 2251 O OE2 . GLU B 2 15 ? 15.059 54.438 4.931 1.00 57.30 ? 1551 GLU B OE2 1 ATOM 2252 N N . ILE B 2 16 ? 13.296 48.137 6.520 1.00 43.24 ? 1552 ILE B N 1 ATOM 2253 C CA . ILE B 2 16 ? 12.605 46.866 6.415 1.00 39.63 ? 1552 ILE B CA 1 ATOM 2254 C C . ILE B 2 16 ? 11.301 47.015 7.165 1.00 40.02 ? 1552 ILE B C 1 ATOM 2255 O O . ILE B 2 16 ? 11.066 48.044 7.791 1.00 43.41 ? 1552 ILE B O 1 ATOM 2256 C CB . ILE B 2 16 ? 13.412 45.742 7.106 1.00 36.96 ? 1552 ILE B CB 1 ATOM 2257 C CG1 . ILE B 2 16 ? 13.428 45.972 8.621 1.00 37.42 ? 1552 ILE B CG1 1 ATOM 2258 C CG2 . ILE B 2 16 ? 14.840 45.719 6.597 1.00 29.71 ? 1552 ILE B CG2 1 ATOM 2259 C CD1 . ILE B 2 16 ? 14.101 44.854 9.420 1.00 33.78 ? 1552 ILE B CD1 1 ATOM 2260 N N . SER B 2 17 ? 10.430 46.022 7.084 1.00 38.19 ? 1553 SER B N 1 ATOM 2261 C CA . SER B 2 17 ? 9.210 46.091 7.878 1.00 37.28 ? 1553 SER B CA 1 ATOM 2262 C C . SER B 2 17 ? 9.551 45.141 9.004 1.00 37.08 ? 1553 SER B C 1 ATOM 2263 O O . SER B 2 17 ? 10.137 44.088 8.761 1.00 38.12 ? 1553 SER B O 1 ATOM 2264 C CB . SER B 2 17 ? 7.978 45.592 7.127 1.00 33.21 ? 1553 SER B CB 1 ATOM 2265 O OG . SER B 2 17 ? 7.606 46.524 6.130 1.00 34.06 ? 1553 SER B OG 1 ATOM 2266 N N . TRP B 2 18 ? 9.226 45.519 10.233 1.00 35.14 ? 1554 TRP B N 1 ATOM 2267 C CA . TRP B 2 18 ? 9.526 44.671 11.363 1.00 33.89 ? 1554 TRP B CA 1 ATOM 2268 C C . TRP B 2 18 ? 8.277 44.300 12.128 1.00 34.88 ? 1554 TRP B C 1 ATOM 2269 O O . TRP B 2 18 ? 7.515 45.160 12.541 1.00 36.88 ? 1554 TRP B O 1 ATOM 2270 C CB . TRP B 2 18 ? 10.510 45.375 12.286 1.00 32.11 ? 1554 TRP B CB 1 ATOM 2271 C CG . TRP B 2 18 ? 10.849 44.611 13.488 1.00 29.16 ? 1554 TRP B CG 1 ATOM 2272 C CD1 . TRP B 2 18 ? 10.340 44.778 14.740 1.00 31.47 ? 1554 TRP B CD1 1 ATOM 2273 C CD2 . TRP B 2 18 ? 11.778 43.538 13.568 1.00 29.85 ? 1554 TRP B CD2 1 ATOM 2274 N NE1 . TRP B 2 18 ? 10.904 43.867 15.610 1.00 30.13 ? 1554 TRP B NE1 1 ATOM 2275 C CE2 . TRP B 2 18 ? 11.790 43.091 14.911 1.00 30.97 ? 1554 TRP B CE2 1 ATOM 2276 C CE3 . TRP B 2 18 ? 12.607 42.902 12.635 1.00 29.66 ? 1554 TRP B CE3 1 ATOM 2277 C CZ2 . TRP B 2 18 ? 12.600 42.034 15.341 1.00 30.49 ? 1554 TRP B CZ2 1 ATOM 2278 C CZ3 . TRP B 2 18 ? 13.415 41.847 13.069 1.00 29.21 ? 1554 TRP B CZ3 1 ATOM 2279 C CH2 . TRP B 2 18 ? 13.403 41.427 14.406 1.00 26.52 ? 1554 TRP B CH2 1 ATOM 2280 N N . ASP B 2 19 ? 8.061 43.010 12.312 1.00 34.96 ? 1555 ASP B N 1 ATOM 2281 C CA . ASP B 2 19 ? 6.906 42.573 13.049 1.00 37.60 ? 1555 ASP B CA 1 ATOM 2282 C C . ASP B 2 19 ? 7.308 42.029 14.437 1.00 38.85 ? 1555 ASP B C 1 ATOM 2283 O O . ASP B 2 19 ? 7.817 40.917 14.553 1.00 40.81 ? 1555 ASP B O 1 ATOM 2284 C CB . ASP B 2 19 ? 6.152 41.529 12.212 1.00 39.20 ? 1555 ASP B CB 1 ATOM 2285 C CG . ASP B 2 19 ? 5.047 40.798 12.991 1.00 44.82 ? 1555 ASP B CG 1 ATOM 2286 O OD1 . ASP B 2 19 ? 4.373 41.412 13.856 1.00 45.63 ? 1555 ASP B OD1 1 ATOM 2287 O OD2 . ASP B 2 19 ? 4.829 39.593 12.708 1.00 46.18 ? 1555 ASP B OD2 1 ATOM 2288 N N . TYR B 2 20 ? 7.131 42.846 15.478 1.00 37.31 ? 1556 TYR B N 1 ATOM 2289 C CA . TYR B 2 20 ? 7.391 42.412 16.839 1.00 36.17 ? 1556 TYR B CA 1 ATOM 2290 C C . TYR B 2 20 ? 6.317 41.325 16.946 1.00 39.91 ? 1556 TYR B C 1 ATOM 2291 O O . TYR B 2 20 ? 5.449 41.238 16.070 1.00 43.67 ? 1556 TYR B O 1 ATOM 2292 C CB . TYR B 2 20 ? 7.055 43.519 17.847 1.00 38.72 ? 1556 TYR B CB 1 ATOM 2293 C CG . TYR B 2 20 ? 7.820 44.835 17.733 1.00 37.97 ? 1556 TYR B CG 1 ATOM 2294 C CD1 . TYR B 2 20 ? 7.455 45.810 16.799 1.00 36.11 ? 1556 TYR B CD1 1 ATOM 2295 C CD2 . TYR B 2 20 ? 8.900 45.114 18.587 1.00 38.16 ? 1556 TYR B CD2 1 ATOM 2296 C CE1 . TYR B 2 20 ? 8.150 47.033 16.718 1.00 35.28 ? 1556 TYR B CE1 1 ATOM 2297 C CE2 . TYR B 2 20 ? 9.600 46.330 18.516 1.00 34.48 ? 1556 TYR B CE2 1 ATOM 2298 C CZ . TYR B 2 20 ? 9.220 47.283 17.583 1.00 36.46 ? 1556 TYR B CZ 1 ATOM 2299 O OH . TYR B 2 20 ? 9.903 48.488 17.526 1.00 35.71 ? 1556 TYR B OH 1 ATOM 2300 N N . SER B 2 21 ? 6.327 40.506 17.991 1.00 39.32 ? 1557 SER B N 1 ATOM 2301 C CA . SER B 2 21 ? 5.309 39.448 18.115 1.00 41.26 ? 1557 SER B CA 1 ATOM 2302 C C . SER B 2 21 ? 5.235 38.340 17.026 1.00 41.94 ? 1557 SER B C 1 ATOM 2303 O O . SER B 2 21 ? 4.739 37.256 17.302 1.00 44.35 ? 1557 SER B O 1 ATOM 2304 C CB . SER B 2 21 ? 3.912 40.060 18.263 1.00 40.67 ? 1557 SER B CB 1 ATOM 2305 O OG . SER B 2 21 ? 3.344 40.358 17.007 1.00 37.63 ? 1557 SER B OG 1 ATOM 2306 N N . LYS B 2 22 ? 5.716 38.587 15.813 1.00 41.50 ? 1558 LYS B N 1 ATOM 2307 C CA . LYS B 2 22 ? 5.671 37.573 14.757 1.00 43.86 ? 1558 LYS B CA 1 ATOM 2308 C C . LYS B 2 22 ? 5.570 36.098 15.211 1.00 44.17 ? 1558 LYS B C 1 ATOM 2309 O O . LYS B 2 22 ? 4.750 35.336 14.688 1.00 43.91 ? 1558 LYS B O 1 ATOM 2310 C CB . LYS B 2 22 ? 6.869 37.729 13.813 1.00 43.76 ? 1558 LYS B CB 1 ATOM 2311 C CG . LYS B 2 22 ? 6.995 36.560 12.843 1.00 47.28 ? 1558 LYS B CG 1 ATOM 2312 C CD . LYS B 2 22 ? 7.953 36.808 11.682 1.00 50.50 ? 1558 LYS B CD 1 ATOM 2313 C CE . LYS B 2 22 ? 7.885 35.621 10.699 1.00 54.32 ? 1558 LYS B CE 1 ATOM 2314 N NZ . LYS B 2 22 ? 8.437 35.867 9.329 1.00 54.87 ? 1558 LYS B NZ 1 ATOM 2315 N N . PHE B 2 23 ? 6.394 35.689 16.169 1.00 44.96 ? 1559 PHE B N 1 ATOM 2316 C CA . PHE B 2 23 ? 6.349 34.314 16.660 1.00 45.30 ? 1559 PHE B CA 1 ATOM 2317 C C . PHE B 2 23 ? 5.487 34.113 17.891 1.00 46.71 ? 1559 PHE B C 1 ATOM 2318 O O . PHE B 2 23 ? 5.795 33.258 18.713 1.00 45.90 ? 1559 PHE B O 1 ATOM 2319 C CB . PHE B 2 23 ? 7.741 33.808 16.996 1.00 45.56 ? 1559 PHE B CB 1 ATOM 2320 C CG . PHE B 2 23 ? 8.691 33.882 15.862 1.00 49.56 ? 1559 PHE B CG 1 ATOM 2321 C CD1 . PHE B 2 23 ? 9.422 35.036 15.632 1.00 50.04 ? 1559 PHE B CD1 1 ATOM 2322 C CD2 . PHE B 2 23 ? 8.857 32.798 15.011 1.00 51.80 ? 1559 PHE B CD2 1 ATOM 2323 C CE1 . PHE B 2 23 ? 10.304 35.112 14.583 1.00 51.41 ? 1559 PHE B CE1 1 ATOM 2324 C CE2 . PHE B 2 23 ? 9.740 32.864 13.954 1.00 51.89 ? 1559 PHE B CE2 1 ATOM 2325 C CZ . PHE B 2 23 ? 10.464 34.024 13.740 1.00 53.20 ? 1559 PHE B CZ 1 ATOM 2326 N N . VAL B 2 24 ? 4.420 34.889 18.035 1.00 49.51 ? 1560 VAL B N 1 ATOM 2327 C CA . VAL B 2 24 ? 3.554 34.727 19.193 1.00 53.79 ? 1560 VAL B CA 1 ATOM 2328 C C . VAL B 2 24 ? 2.250 34.042 18.804 1.00 55.14 ? 1560 VAL B C 1 ATOM 2329 O O . VAL B 2 24 ? 1.937 32.959 19.311 1.00 59.37 ? 1560 VAL B O 1 ATOM 2330 C CB . VAL B 2 24 ? 3.222 36.076 19.856 1.00 55.16 ? 1560 VAL B CB 1 ATOM 2331 C CG1 . VAL B 2 24 ? 2.310 36.887 18.951 1.00 58.28 ? 1560 VAL B CG1 1 ATOM 2332 C CG2 . VAL B 2 24 ? 2.550 35.835 21.209 1.00 54.47 ? 1560 VAL B CG2 1 ATOM 2333 N N . PRO B 2 33 ? -1.747 42.441 21.095 1.00 66.53 ? 1569 PRO B N 1 ATOM 2334 C CA . PRO B 2 33 ? -1.011 42.532 19.833 1.00 66.95 ? 1569 PRO B CA 1 ATOM 2335 C C . PRO B 2 33 ? -1.905 42.913 18.640 1.00 67.60 ? 1569 PRO B C 1 ATOM 2336 O O . PRO B 2 33 ? -2.514 43.988 18.634 1.00 67.99 ? 1569 PRO B O 1 ATOM 2337 C CB . PRO B 2 33 ? -0.402 41.135 19.702 1.00 66.82 ? 1569 PRO B CB 1 ATOM 2338 C CG . PRO B 2 33 ? -0.108 40.777 21.120 1.00 66.44 ? 1569 PRO B CG 1 ATOM 2339 C CD . PRO B 2 33 ? -1.381 41.215 21.827 1.00 66.93 ? 1569 PRO B CD 1 ATOM 2340 N N . GLU B 2 34 ? -1.963 42.035 17.634 1.00 67.47 ? 1570 GLU B N 1 ATOM 2341 C CA . GLU B 2 34 ? -2.772 42.246 16.426 1.00 66.15 ? 1570 GLU B CA 1 ATOM 2342 C C . GLU B 2 34 ? -2.151 43.359 15.582 1.00 63.92 ? 1570 GLU B C 1 ATOM 2343 O O . GLU B 2 34 ? -2.337 44.549 15.860 1.00 65.78 ? 1570 GLU B O 1 ATOM 2344 C CB . GLU B 2 34 ? -4.206 42.604 16.827 1.00 70.59 ? 1570 GLU B CB 1 ATOM 2345 C CG . GLU B 2 34 ? -5.262 42.423 15.744 1.00 76.81 ? 1570 GLU B CG 1 ATOM 2346 C CD . GLU B 2 34 ? -6.683 42.674 16.273 1.00 81.30 ? 1570 GLU B CD 1 ATOM 2347 O OE1 . GLU B 2 34 ? -7.642 42.615 15.467 1.00 80.82 ? 1570 GLU B OE1 1 ATOM 2348 O OE2 . GLU B 2 34 ? -6.837 42.927 17.496 1.00 81.95 ? 1570 GLU B OE2 1 ATOM 2349 N N . ASP B 2 35 ? -1.409 42.970 14.552 1.00 58.19 ? 1571 ASP B N 1 ATOM 2350 C CA . ASP B 2 35 ? -0.733 43.934 13.690 1.00 53.50 ? 1571 ASP B CA 1 ATOM 2351 C C . ASP B 2 35 ? 0.281 44.832 14.426 1.00 49.33 ? 1571 ASP B C 1 ATOM 2352 O O . ASP B 2 35 ? -0.003 45.968 14.778 1.00 46.83 ? 1571 ASP B O 1 ATOM 2353 C CB . ASP B 2 35 ? -1.746 44.813 12.959 1.00 54.14 ? 1571 ASP B CB 1 ATOM 2354 C CG . ASP B 2 35 ? -1.083 45.797 12.001 1.00 56.25 ? 1571 ASP B CG 1 ATOM 2355 O OD1 . ASP B 2 35 ? 0.170 45.840 11.946 1.00 53.42 ? 1571 ASP B OD1 1 ATOM 2356 O OD2 . ASP B 2 35 ? -1.824 46.532 11.303 1.00 57.76 ? 1571 ASP B OD2 1 ATOM 2357 N N . THR B 2 36 ? 1.478 44.305 14.628 1.00 45.56 ? 1572 THR B N 1 ATOM 2358 C CA . THR B 2 36 ? 2.533 45.041 15.281 1.00 40.55 ? 1572 THR B CA 1 ATOM 2359 C C . THR B 2 36 ? 3.728 45.168 14.323 1.00 39.93 ? 1572 THR B C 1 ATOM 2360 O O . THR B 2 36 ? 4.864 44.862 14.686 1.00 39.35 ? 1572 THR B O 1 ATOM 2361 C CB . THR B 2 36 ? 2.982 44.324 16.595 1.00 41.92 ? 1572 THR B CB 1 ATOM 2362 O OG1 . THR B 2 36 ? 3.592 43.068 16.282 1.00 41.81 ? 1572 THR B OG1 1 ATOM 2363 C CG2 . THR B 2 36 ? 1.787 44.045 17.490 1.00 39.17 ? 1572 THR B CG2 1 ATOM 2364 N N . VAL B 2 37 ? 3.491 45.590 13.086 1.00 37.13 ? 1573 VAL B N 1 ATOM 2365 C CA . VAL B 2 37 ? 4.619 45.749 12.193 1.00 37.09 ? 1573 VAL B CA 1 ATOM 2366 C C . VAL B 2 37 ? 4.779 47.206 11.790 1.00 39.49 ? 1573 VAL B C 1 ATOM 2367 O O . VAL B 2 37 ? 3.836 47.856 11.322 1.00 40.03 ? 1573 VAL B O 1 ATOM 2368 C CB . VAL B 2 37 ? 4.537 44.817 10.934 1.00 34.64 ? 1573 VAL B CB 1 ATOM 2369 C CG1 . VAL B 2 37 ? 3.421 43.805 11.094 1.00 33.37 ? 1573 VAL B CG1 1 ATOM 2370 C CG2 . VAL B 2 37 ? 4.401 45.618 9.673 1.00 34.84 ? 1573 VAL B CG2 1 ATOM 2371 N N . TYR B 2 38 ? 5.992 47.714 11.997 1.00 40.34 ? 1574 TYR B N 1 ATOM 2372 C CA . TYR B 2 38 ? 6.330 49.095 11.691 1.00 41.37 ? 1574 TYR B CA 1 ATOM 2373 C C . TYR B 2 38 ? 7.529 49.165 10.799 1.00 40.40 ? 1574 TYR B C 1 ATOM 2374 O O . TYR B 2 38 ? 8.364 48.281 10.829 1.00 42.20 ? 1574 TYR B O 1 ATOM 2375 C CB . TYR B 2 38 ? 6.690 49.842 12.960 1.00 41.58 ? 1574 TYR B CB 1 ATOM 2376 C CG . TYR B 2 38 ? 5.630 49.776 13.997 1.00 45.86 ? 1574 TYR B CG 1 ATOM 2377 C CD1 . TYR B 2 38 ? 4.857 50.897 14.299 1.00 47.13 ? 1574 TYR B CD1 1 ATOM 2378 C CD2 . TYR B 2 38 ? 5.393 48.595 14.692 1.00 46.43 ? 1574 TYR B CD2 1 ATOM 2379 C CE1 . TYR B 2 38 ? 3.874 50.847 15.278 1.00 48.49 ? 1574 TYR B CE1 1 ATOM 2380 C CE2 . TYR B 2 38 ? 4.414 48.531 15.666 1.00 51.01 ? 1574 TYR B CE2 1 ATOM 2381 C CZ . TYR B 2 38 ? 3.659 49.661 15.959 1.00 51.10 ? 1574 TYR B CZ 1 ATOM 2382 O OH . TYR B 2 38 ? 2.703 49.597 16.944 1.00 53.66 ? 1574 TYR B OH 1 ATOM 2383 N N . LYS B 2 39 ? 7.617 50.231 10.016 1.00 39.55 ? 1575 LYS B N 1 ATOM 2384 C CA . LYS B 2 39 ? 8.768 50.437 9.159 1.00 40.08 ? 1575 LYS B CA 1 ATOM 2385 C C . LYS B 2 39 ? 9.926 50.671 10.140 1.00 39.94 ? 1575 LYS B C 1 ATOM 2386 O O . LYS B 2 39 ? 9.744 51.322 11.181 1.00 41.41 ? 1575 LYS B O 1 ATOM 2387 C CB . LYS B 2 39 ? 8.539 51.671 8.292 1.00 40.66 ? 1575 LYS B CB 1 ATOM 2388 C CG . LYS B 2 39 ? 9.722 52.061 7.444 1.00 44.85 ? 1575 LYS B CG 1 ATOM 2389 C CD . LYS B 2 39 ? 9.327 53.133 6.452 1.00 48.28 ? 1575 LYS B CD 1 ATOM 2390 C CE . LYS B 2 39 ? 10.491 53.553 5.589 1.00 48.21 ? 1575 LYS B CE 1 ATOM 2391 N NZ . LYS B 2 39 ? 9.988 54.146 4.316 1.00 51.21 ? 1575 LYS B NZ 1 ATOM 2392 N N . LYS B 2 40 ? 11.103 50.135 9.830 1.00 36.39 ? 1576 LYS B N 1 ATOM 2393 C CA . LYS B 2 40 ? 12.256 50.288 10.713 1.00 36.34 ? 1576 LYS B CA 1 ATOM 2394 C C . LYS B 2 40 ? 13.540 50.311 9.923 1.00 38.80 ? 1576 LYS B C 1 ATOM 2395 O O . LYS B 2 40 ? 13.539 50.026 8.721 1.00 40.11 ? 1576 LYS B O 1 ATOM 2396 C CB . LYS B 2 40 ? 12.326 49.131 11.701 1.00 34.61 ? 1576 LYS B CB 1 ATOM 2397 C CG . LYS B 2 40 ? 11.236 49.133 12.727 1.00 35.77 ? 1576 LYS B CG 1 ATOM 2398 C CD . LYS B 2 40 ? 11.525 50.184 13.801 1.00 43.03 ? 1576 LYS B CD 1 ATOM 2399 C CE . LYS B 2 40 ? 12.097 49.504 14.997 1.00 37.22 ? 1576 LYS B CE 1 ATOM 2400 N NZ . LYS B 2 40 ? 11.189 48.371 15.201 1.00 39.86 ? 1576 LYS B NZ 1 ATOM 2401 N N . VAL B 2 41 ? 14.639 50.653 10.590 1.00 38.12 ? 1577 VAL B N 1 ATOM 2402 C CA . VAL B 2 41 ? 15.934 50.662 9.919 1.00 39.87 ? 1577 VAL B CA 1 ATOM 2403 C C . VAL B 2 41 ? 16.930 49.872 10.769 1.00 39.34 ? 1577 VAL B C 1 ATOM 2404 O O . VAL B 2 41 ? 17.157 50.178 11.946 1.00 40.94 ? 1577 VAL B O 1 ATOM 2405 C CB . VAL B 2 41 ? 16.441 52.104 9.629 1.00 38.51 ? 1577 VAL B CB 1 ATOM 2406 C CG1 . VAL B 2 41 ? 16.582 52.905 10.906 1.00 40.15 ? 1577 VAL B CG1 1 ATOM 2407 C CG2 . VAL B 2 41 ? 17.763 52.030 8.899 1.00 41.41 ? 1577 VAL B CG2 1 ATOM 2408 N N . VAL B 2 42 ? 17.519 48.846 10.159 1.00 37.07 ? 1578 VAL B N 1 ATOM 2409 C CA . VAL B 2 42 ? 18.438 47.952 10.865 1.00 31.18 ? 1578 VAL B CA 1 ATOM 2410 C C . VAL B 2 42 ? 19.836 47.765 10.248 1.00 30.27 ? 1578 VAL B C 1 ATOM 2411 O O . VAL B 2 42 ? 20.069 48.083 9.086 1.00 30.60 ? 1578 VAL B O 1 ATOM 2412 C CB . VAL B 2 42 ? 17.760 46.590 10.997 1.00 26.52 ? 1578 VAL B CB 1 ATOM 2413 C CG1 . VAL B 2 42 ? 16.530 46.716 11.837 1.00 23.55 ? 1578 VAL B CG1 1 ATOM 2414 C CG2 . VAL B 2 42 ? 17.365 46.090 9.633 1.00 13.95 ? 1578 VAL B CG2 1 ATOM 2415 N N . PHE B 2 43 ? 20.771 47.266 11.041 1.00 30.33 ? 1579 PHE B N 1 ATOM 2416 C CA . PHE B 2 43 ? 22.118 47.007 10.539 1.00 34.31 ? 1579 PHE B CA 1 ATOM 2417 C C . PHE B 2 43 ? 22.128 45.629 9.886 1.00 36.59 ? 1579 PHE B C 1 ATOM 2418 O O . PHE B 2 43 ? 21.894 44.638 10.558 1.00 39.87 ? 1579 PHE B O 1 ATOM 2419 C CB . PHE B 2 43 ? 23.152 47.046 11.682 1.00 31.50 ? 1579 PHE B CB 1 ATOM 2420 C CG . PHE B 2 43 ? 23.439 48.432 12.197 1.00 30.06 ? 1579 PHE B CG 1 ATOM 2421 C CD1 . PHE B 2 43 ? 23.731 49.463 11.320 1.00 28.38 ? 1579 PHE B CD1 1 ATOM 2422 C CD2 . PHE B 2 43 ? 23.398 48.709 13.553 1.00 32.16 ? 1579 PHE B CD2 1 ATOM 2423 C CE1 . PHE B 2 43 ? 23.976 50.742 11.784 1.00 28.74 ? 1579 PHE B CE1 1 ATOM 2424 C CE2 . PHE B 2 43 ? 23.644 49.998 14.021 1.00 31.76 ? 1579 PHE B CE2 1 ATOM 2425 C CZ . PHE B 2 43 ? 23.933 51.013 13.127 1.00 28.04 ? 1579 PHE B CZ 1 ATOM 2426 N N . ARG B 2 44 ? 22.400 45.568 8.585 1.00 37.95 ? 1580 ARG B N 1 ATOM 2427 C CA . ARG B 2 44 ? 22.417 44.303 7.843 1.00 39.73 ? 1580 ARG B CA 1 ATOM 2428 C C . ARG B 2 44 ? 23.832 43.925 7.388 1.00 40.68 ? 1580 ARG B C 1 ATOM 2429 O O . ARG B 2 44 ? 24.589 44.792 6.949 1.00 43.83 ? 1580 ARG B O 1 ATOM 2430 C CB . ARG B 2 44 ? 21.521 44.431 6.615 1.00 41.09 ? 1580 ARG B CB 1 ATOM 2431 C CG . ARG B 2 44 ? 20.605 43.259 6.371 1.00 44.29 ? 1580 ARG B CG 1 ATOM 2432 C CD . ARG B 2 44 ? 19.650 43.096 7.536 1.00 48.40 ? 1580 ARG B CD 1 ATOM 2433 N NE . ARG B 2 44 ? 18.432 42.377 7.165 1.00 53.48 ? 1580 ARG B NE 1 ATOM 2434 C CZ . ARG B 2 44 ? 17.771 42.554 6.021 1.00 54.44 ? 1580 ARG B CZ 1 ATOM 2435 N NH1 . ARG B 2 44 ? 18.210 43.416 5.111 1.00 51.39 ? 1580 ARG B NH1 1 ATOM 2436 N NH2 . ARG B 2 44 ? 16.638 41.896 5.806 1.00 55.01 ? 1580 ARG B NH2 1 ATOM 2437 N N . LYS B 2 45 ? 24.182 42.639 7.459 1.00 40.68 ? 1581 LYS B N 1 ATOM 2438 C CA . LYS B 2 45 ? 25.525 42.192 7.066 1.00 41.71 ? 1581 LYS B CA 1 ATOM 2439 C C . LYS B 2 45 ? 25.684 41.736 5.615 1.00 44.60 ? 1581 LYS B C 1 ATOM 2440 O O . LYS B 2 45 ? 24.995 40.829 5.156 1.00 44.95 ? 1581 LYS B O 1 ATOM 2441 C CB . LYS B 2 45 ? 26.003 41.070 7.984 1.00 40.77 ? 1581 LYS B CB 1 ATOM 2442 C CG . LYS B 2 45 ? 27.484 40.780 7.873 1.00 37.16 ? 1581 LYS B CG 1 ATOM 2443 C CD . LYS B 2 45 ? 27.928 39.721 8.844 1.00 31.09 ? 1581 LYS B CD 1 ATOM 2444 C CE . LYS B 2 45 ? 29.425 39.602 8.793 1.00 36.31 ? 1581 LYS B CE 1 ATOM 2445 N NZ . LYS B 2 45 ? 29.990 38.610 9.753 1.00 39.25 ? 1581 LYS B NZ 1 ATOM 2446 N N . TYR B 2 46 ? 26.606 42.366 4.891 1.00 46.69 ? 1582 TYR B N 1 ATOM 2447 C CA . TYR B 2 46 ? 26.828 41.997 3.504 1.00 47.69 ? 1582 TYR B CA 1 ATOM 2448 C C . TYR B 2 46 ? 28.102 41.194 3.314 1.00 49.22 ? 1582 TYR B C 1 ATOM 2449 O O . TYR B 2 46 ? 28.986 41.198 4.162 1.00 49.63 ? 1582 TYR B O 1 ATOM 2450 C CB . TYR B 2 46 ? 26.826 43.237 2.616 1.00 47.41 ? 1582 TYR B CB 1 ATOM 2451 C CG . TYR B 2 46 ? 25.426 43.714 2.334 1.00 45.19 ? 1582 TYR B CG 1 ATOM 2452 C CD1 . TYR B 2 46 ? 24.713 44.429 3.289 1.00 41.62 ? 1582 TYR B CD1 1 ATOM 2453 C CD2 . TYR B 2 46 ? 24.782 43.368 1.139 1.00 43.08 ? 1582 TYR B CD2 1 ATOM 2454 C CE1 . TYR B 2 46 ? 23.401 44.785 3.072 1.00 43.37 ? 1582 TYR B CE1 1 ATOM 2455 C CE2 . TYR B 2 46 ? 23.467 43.714 0.908 1.00 43.57 ? 1582 TYR B CE2 1 ATOM 2456 C CZ . TYR B 2 46 ? 22.775 44.426 1.880 1.00 45.71 ? 1582 TYR B CZ 1 ATOM 2457 O OH . TYR B 2 46 ? 21.460 44.781 1.661 1.00 45.29 ? 1582 TYR B OH 1 ATOM 2458 N N . LEU B 2 47 ? 28.188 40.498 2.192 1.00 50.10 ? 1583 LEU B N 1 ATOM 2459 C CA . LEU B 2 47 ? 29.341 39.666 1.937 1.00 52.08 ? 1583 LEU B CA 1 ATOM 2460 C C . LEU B 2 47 ? 30.580 40.434 1.479 1.00 52.61 ? 1583 LEU B C 1 ATOM 2461 O O . LEU B 2 47 ? 31.701 39.986 1.727 1.00 53.46 ? 1583 LEU B O 1 ATOM 2462 C CB . LEU B 2 47 ? 28.957 38.566 0.933 1.00 53.78 ? 1583 LEU B CB 1 ATOM 2463 C CG . LEU B 2 47 ? 29.371 37.109 1.220 1.00 55.59 ? 1583 LEU B CG 1 ATOM 2464 C CD1 . LEU B 2 47 ? 29.192 36.765 2.703 1.00 54.51 ? 1583 LEU B CD1 1 ATOM 2465 C CD2 . LEU B 2 47 ? 28.536 36.171 0.349 1.00 55.79 ? 1583 LEU B CD2 1 ATOM 2466 N N . ASP B 2 48 ? 30.397 41.587 0.836 1.00 52.57 ? 1584 ASP B N 1 ATOM 2467 C CA . ASP B 2 48 ? 31.546 42.361 0.381 1.00 54.14 ? 1584 ASP B CA 1 ATOM 2468 C C . ASP B 2 48 ? 31.263 43.808 -0.007 1.00 55.09 ? 1584 ASP B C 1 ATOM 2469 O O . ASP B 2 48 ? 30.156 44.301 0.166 1.00 56.60 ? 1584 ASP B O 1 ATOM 2470 C CB . ASP B 2 48 ? 32.212 41.645 -0.787 1.00 56.19 ? 1584 ASP B CB 1 ATOM 2471 C CG . ASP B 2 48 ? 31.253 41.383 -1.932 1.00 60.15 ? 1584 ASP B CG 1 ATOM 2472 O OD1 . ASP B 2 48 ? 30.538 42.331 -2.327 1.00 61.67 ? 1584 ASP B OD1 1 ATOM 2473 O OD2 . ASP B 2 48 ? 31.219 40.238 -2.444 1.00 60.41 ? 1584 ASP B OD2 1 ATOM 2474 N N . SER B 2 49 ? 32.287 44.469 -0.542 1.00 56.33 ? 1585 SER B N 1 ATOM 2475 C CA . SER B 2 49 ? 32.246 45.872 -0.973 1.00 56.51 ? 1585 SER B CA 1 ATOM 2476 C C . SER B 2 49 ? 31.116 46.301 -1.883 1.00 57.29 ? 1585 SER B C 1 ATOM 2477 O O . SER B 2 49 ? 30.764 47.478 -1.920 1.00 57.32 ? 1585 SER B O 1 ATOM 2478 C CB . SER B 2 49 ? 33.552 46.244 -1.678 1.00 57.10 ? 1585 SER B CB 1 ATOM 2479 O OG . SER B 2 49 ? 34.653 46.203 -0.791 1.00 62.21 ? 1585 SER B OG 1 ATOM 2480 N N . THR B 2 50 ? 30.559 45.367 -2.640 1.00 59.90 ? 1586 THR B N 1 ATOM 2481 C CA . THR B 2 50 ? 29.490 45.714 -3.569 1.00 61.91 ? 1586 THR B CA 1 ATOM 2482 C C . THR B 2 50 ? 28.144 45.834 -2.875 1.00 63.13 ? 1586 THR B C 1 ATOM 2483 O O . THR B 2 50 ? 27.225 46.469 -3.400 1.00 65.28 ? 1586 THR B O 1 ATOM 2484 C CB . THR B 2 50 ? 29.370 44.673 -4.719 1.00 62.44 ? 1586 THR B CB 1 ATOM 2485 O OG1 . THR B 2 50 ? 28.822 43.446 -4.217 1.00 63.06 ? 1586 THR B OG1 1 ATOM 2486 C CG2 . THR B 2 50 ? 30.743 44.396 -5.333 1.00 62.65 ? 1586 THR B CG2 1 ATOM 2487 N N . PHE B 2 51 ? 28.024 45.234 -1.694 1.00 61.60 ? 1587 PHE B N 1 ATOM 2488 C CA . PHE B 2 51 ? 26.770 45.288 -0.969 1.00 58.83 ? 1587 PHE B CA 1 ATOM 2489 C C . PHE B 2 51 ? 25.674 44.770 -1.885 1.00 60.02 ? 1587 PHE B C 1 ATOM 2490 O O . PHE B 2 51 ? 24.594 45.354 -1.955 1.00 60.84 ? 1587 PHE B O 1 ATOM 2491 C CB . PHE B 2 51 ? 26.469 46.727 -0.562 1.00 56.43 ? 1587 PHE B CB 1 ATOM 2492 C CG . PHE B 2 51 ? 27.375 47.249 0.514 1.00 54.76 ? 1587 PHE B CG 1 ATOM 2493 C CD1 . PHE B 2 51 ? 27.108 46.987 1.856 1.00 55.63 ? 1587 PHE B CD1 1 ATOM 2494 C CD2 . PHE B 2 51 ? 28.515 47.965 0.191 1.00 51.88 ? 1587 PHE B CD2 1 ATOM 2495 C CE1 . PHE B 2 51 ? 27.971 47.432 2.864 1.00 54.62 ? 1587 PHE B CE1 1 ATOM 2496 C CE2 . PHE B 2 51 ? 29.380 48.411 1.185 1.00 51.65 ? 1587 PHE B CE2 1 ATOM 2497 C CZ . PHE B 2 51 ? 29.109 48.143 2.525 1.00 53.68 ? 1587 PHE B CZ 1 ATOM 2498 N N . THR B 2 52 ? 25.962 43.683 -2.601 1.00 60.21 ? 1588 THR B N 1 ATOM 2499 C CA . THR B 2 52 ? 24.981 43.093 -3.506 1.00 62.47 ? 1588 THR B CA 1 ATOM 2500 C C . THR B 2 52 ? 24.324 41.898 -2.856 1.00 62.46 ? 1588 THR B C 1 ATOM 2501 O O . THR B 2 52 ? 23.102 41.838 -2.734 1.00 64.19 ? 1588 THR B O 1 ATOM 2502 C CB . THR B 2 52 ? 25.608 42.621 -4.844 1.00 62.95 ? 1588 THR B CB 1 ATOM 2503 O OG1 . THR B 2 52 ? 26.788 41.850 -4.587 1.00 62.99 ? 1588 THR B OG1 1 ATOM 2504 C CG2 . THR B 2 52 ? 25.939 43.806 -5.725 1.00 62.82 ? 1588 THR B CG2 1 ATOM 2505 N N . LYS B 2 53 ? 25.143 40.938 -2.451 1.00 62.20 ? 1589 LYS B N 1 ATOM 2506 C CA . LYS B 2 53 ? 24.633 39.744 -1.803 1.00 61.87 ? 1589 LYS B CA 1 ATOM 2507 C C . LYS B 2 53 ? 24.903 39.893 -0.313 1.00 59.86 ? 1589 LYS B C 1 ATOM 2508 O O . LYS B 2 53 ? 25.973 40.358 0.078 1.00 59.96 ? 1589 LYS B O 1 ATOM 2509 C CB . LYS B 2 53 ? 25.340 38.503 -2.355 1.00 63.07 ? 1589 LYS B CB 1 ATOM 2510 C CG . LYS B 2 53 ? 24.642 37.185 -2.013 1.00 67.18 ? 1589 LYS B CG 1 ATOM 2511 C CD . LYS B 2 53 ? 25.320 35.992 -2.686 1.00 70.61 ? 1589 LYS B CD 1 ATOM 2512 C CE . LYS B 2 53 ? 24.638 34.698 -2.303 1.00 70.50 ? 1589 LYS B CE 1 ATOM 2513 N NZ . LYS B 2 53 ? 24.481 34.651 -0.828 1.00 73.90 ? 1589 LYS B NZ 1 ATOM 2514 N N . LEU B 2 54 ? 23.938 39.516 0.520 1.00 57.48 ? 1590 LEU B N 1 ATOM 2515 C CA . LEU B 2 54 ? 24.137 39.636 1.956 1.00 57.93 ? 1590 LEU B CA 1 ATOM 2516 C C . LEU B 2 54 ? 24.474 38.318 2.647 1.00 55.81 ? 1590 LEU B C 1 ATOM 2517 O O . LEU B 2 54 ? 24.148 37.250 2.159 1.00 55.91 ? 1590 LEU B O 1 ATOM 2518 C CB . LEU B 2 54 ? 22.917 40.309 2.607 1.00 59.52 ? 1590 LEU B CB 1 ATOM 2519 C CG . LEU B 2 54 ? 21.506 39.786 2.350 1.00 59.40 ? 1590 LEU B CG 1 ATOM 2520 C CD1 . LEU B 2 54 ? 21.295 38.481 3.115 1.00 62.01 ? 1590 LEU B CD1 1 ATOM 2521 C CD2 . LEU B 2 54 ? 20.497 40.833 2.796 1.00 56.65 ? 1590 LEU B CD2 1 ATOM 2522 N N . ASP B 2 55 ? 25.149 38.413 3.784 1.00 55.13 ? 1591 ASP B N 1 ATOM 2523 C CA . ASP B 2 55 ? 25.555 37.253 4.548 1.00 54.92 ? 1591 ASP B CA 1 ATOM 2524 C C . ASP B 2 55 ? 24.378 36.703 5.341 1.00 56.80 ? 1591 ASP B C 1 ATOM 2525 O O . ASP B 2 55 ? 24.018 37.234 6.394 1.00 54.97 ? 1591 ASP B O 1 ATOM 2526 C CB . ASP B 2 55 ? 26.676 37.637 5.501 1.00 55.51 ? 1591 ASP B CB 1 ATOM 2527 C CG . ASP B 2 55 ? 27.381 36.433 6.081 1.00 58.26 ? 1591 ASP B CG 1 ATOM 2528 O OD1 . ASP B 2 55 ? 26.688 35.448 6.426 1.00 57.01 ? 1591 ASP B OD1 1 ATOM 2529 O OD2 . ASP B 2 55 ? 28.630 36.479 6.200 1.00 59.94 ? 1591 ASP B OD2 1 ATOM 2530 N N . PRO B 2 56 ? 23.773 35.609 4.854 1.00 58.54 ? 1592 PRO B N 1 ATOM 2531 C CA . PRO B 2 56 ? 22.626 34.984 5.519 1.00 58.23 ? 1592 PRO B CA 1 ATOM 2532 C C . PRO B 2 56 ? 22.894 34.795 7.000 1.00 57.80 ? 1592 PRO B C 1 ATOM 2533 O O . PRO B 2 56 ? 24.006 34.465 7.386 1.00 59.15 ? 1592 PRO B O 1 ATOM 2534 C CB . PRO B 2 56 ? 22.489 33.651 4.789 1.00 58.24 ? 1592 PRO B CB 1 ATOM 2535 C CG . PRO B 2 56 ? 23.007 33.958 3.419 1.00 60.01 ? 1592 PRO B CG 1 ATOM 2536 C CD . PRO B 2 56 ? 24.238 34.775 3.731 1.00 58.76 ? 1592 PRO B CD 1 ATOM 2537 N N . GLN B 2 57 ? 21.870 35.000 7.819 1.00 57.55 ? 1593 GLN B N 1 ATOM 2538 C CA . GLN B 2 57 ? 21.992 34.853 9.264 1.00 56.47 ? 1593 GLN B CA 1 ATOM 2539 C C . GLN B 2 57 ? 21.819 33.385 9.675 1.00 56.75 ? 1593 GLN B C 1 ATOM 2540 O O . GLN B 2 57 ? 20.752 32.780 9.475 1.00 57.16 ? 1593 GLN B O 1 ATOM 2541 C CB . GLN B 2 57 ? 20.953 35.745 9.942 1.00 57.87 ? 1593 GLN B CB 1 ATOM 2542 C CG . GLN B 2 57 ? 20.966 35.723 11.465 1.00 61.16 ? 1593 GLN B CG 1 ATOM 2543 C CD . GLN B 2 57 ? 20.241 36.925 12.047 1.00 61.98 ? 1593 GLN B CD 1 ATOM 2544 O OE1 . GLN B 2 57 ? 20.783 38.026 12.079 1.00 65.85 ? 1593 GLN B OE1 1 ATOM 2545 N NE2 . GLN B 2 57 ? 19.002 36.723 12.488 1.00 61.47 ? 1593 GLN B NE2 1 ATOM 2546 N N . GLY B 2 58 ? 22.878 32.823 10.256 1.00 53.65 ? 1594 GLY B N 1 ATOM 2547 C CA . GLY B 2 58 ? 22.856 31.428 10.653 1.00 53.29 ? 1594 GLY B CA 1 ATOM 2548 C C . GLY B 2 58 ? 21.952 31.056 11.804 1.00 52.24 ? 1594 GLY B C 1 ATOM 2549 O O . GLY B 2 58 ? 21.040 31.799 12.136 1.00 54.81 ? 1594 GLY B O 1 ATOM 2550 N N . GLU B 2 59 ? 22.211 29.893 12.403 1.00 50.13 ? 1595 GLU B N 1 ATOM 2551 C CA . GLU B 2 59 ? 21.426 29.399 13.535 1.00 45.35 ? 1595 GLU B CA 1 ATOM 2552 C C . GLU B 2 59 ? 22.020 29.929 14.822 1.00 44.75 ? 1595 GLU B C 1 ATOM 2553 O O . GLU B 2 59 ? 21.334 30.051 15.825 1.00 44.23 ? 1595 GLU B O 1 ATOM 2554 C CB . GLU B 2 59 ? 21.429 27.860 13.581 1.00 41.60 ? 1595 GLU B CB 1 ATOM 2555 C CG . GLU B 2 59 ? 20.436 27.177 12.646 1.00 38.14 ? 1595 GLU B CG 1 ATOM 2556 C CD . GLU B 2 59 ? 20.815 27.295 11.173 1.00 38.42 ? 1595 GLU B CD 1 ATOM 2557 O OE1 . GLU B 2 59 ? 19.978 26.925 10.318 1.00 36.76 ? 1595 GLU B OE1 1 ATOM 2558 O OE2 . GLU B 2 59 ? 21.943 27.754 10.869 1.00 36.01 ? 1595 GLU B OE2 1 ATOM 2559 N N . TYR B 2 60 ? 23.310 30.231 14.783 1.00 46.19 ? 1596 TYR B N 1 ATOM 2560 C CA . TYR B 2 60 ? 24.032 30.750 15.941 1.00 48.78 ? 1596 TYR B CA 1 ATOM 2561 C C . TYR B 2 60 ? 23.558 32.165 16.342 1.00 46.43 ? 1596 TYR B C 1 ATOM 2562 O O . TYR B 2 60 ? 23.602 32.522 17.514 1.00 42.46 ? 1596 TYR B O 1 ATOM 2563 C CB . TYR B 2 60 ? 25.543 30.767 15.640 1.00 56.54 ? 1596 TYR B CB 1 ATOM 2564 C CG . TYR B 2 60 ? 25.920 31.646 14.445 1.00 67.56 ? 1596 TYR B CG 1 ATOM 2565 C CD1 . TYR B 2 60 ? 27.174 32.281 14.377 1.00 70.93 ? 1596 TYR B CD1 1 ATOM 2566 C CD2 . TYR B 2 60 ? 24.992 31.918 13.422 1.00 70.48 ? 1596 TYR B CD2 1 ATOM 2567 C CE1 . TYR B 2 60 ? 27.483 33.177 13.325 1.00 73.73 ? 1596 TYR B CE1 1 ATOM 2568 C CE2 . TYR B 2 60 ? 25.291 32.807 12.375 1.00 74.33 ? 1596 TYR B CE2 1 ATOM 2569 C CZ . TYR B 2 60 ? 26.531 33.435 12.335 1.00 74.71 ? 1596 TYR B CZ 1 ATOM 2570 O OH . TYR B 2 60 ? 26.795 34.330 11.321 1.00 76.04 ? 1596 TYR B OH 1 ATOM 2571 N N . GLU B 2 61 ? 23.119 32.969 15.373 1.00 44.32 ? 1597 GLU B N 1 ATOM 2572 C CA . GLU B 2 61 ? 22.650 34.310 15.677 1.00 46.14 ? 1597 GLU B CA 1 ATOM 2573 C C . GLU B 2 61 ? 21.167 34.568 15.292 1.00 45.86 ? 1597 GLU B C 1 ATOM 2574 O O . GLU B 2 61 ? 20.780 35.689 14.949 1.00 47.16 ? 1597 GLU B O 1 ATOM 2575 C CB . GLU B 2 61 ? 23.616 35.396 15.088 1.00 48.11 ? 1597 GLU B CB 1 ATOM 2576 C CG . GLU B 2 61 ? 23.756 35.570 13.551 1.00 52.90 ? 1597 GLU B CG 1 ATOM 2577 C CD . GLU B 2 61 ? 24.685 36.776 13.143 1.00 60.77 ? 1597 GLU B CD 1 ATOM 2578 O OE1 . GLU B 2 61 ? 25.865 36.846 13.577 1.00 62.60 ? 1597 GLU B OE1 1 ATOM 2579 O OE2 . GLU B 2 61 ? 24.241 37.669 12.373 1.00 62.61 ? 1597 GLU B OE2 1 ATOM 2580 N N . GLU B 2 62 ? 20.341 33.526 15.387 1.00 41.66 ? 1598 GLU B N 1 ATOM 2581 C CA . GLU B 2 62 ? 18.909 33.611 15.095 1.00 38.54 ? 1598 GLU B CA 1 ATOM 2582 C C . GLU B 2 62 ? 18.189 34.391 16.208 1.00 37.38 ? 1598 GLU B C 1 ATOM 2583 O O . GLU B 2 62 ? 17.162 35.053 15.990 1.00 36.31 ? 1598 GLU B O 1 ATOM 2584 C CB . GLU B 2 62 ? 18.318 32.199 14.982 1.00 36.53 ? 1598 GLU B CB 1 ATOM 2585 C CG . GLU B 2 62 ? 16.832 32.151 14.723 1.00 37.91 ? 1598 GLU B CG 1 ATOM 2586 C CD . GLU B 2 62 ? 16.270 30.738 14.766 1.00 43.77 ? 1598 GLU B CD 1 ATOM 2587 O OE1 . GLU B 2 62 ? 16.943 29.824 15.300 1.00 45.21 ? 1598 GLU B OE1 1 ATOM 2588 O OE2 . GLU B 2 62 ? 15.140 30.540 14.277 1.00 45.02 ? 1598 GLU B OE2 1 ATOM 2589 N N . HIS B 2 63 ? 18.746 34.314 17.409 1.00 37.57 ? 1599 HIS B N 1 ATOM 2590 C CA . HIS B 2 63 ? 18.181 35.000 18.554 1.00 35.77 ? 1599 HIS B CA 1 ATOM 2591 C C . HIS B 2 63 ? 18.434 36.497 18.515 1.00 35.14 ? 1599 HIS B C 1 ATOM 2592 O O . HIS B 2 63 ? 17.776 37.243 19.219 1.00 38.07 ? 1599 HIS B O 1 ATOM 2593 C CB . HIS B 2 63 ? 18.748 34.412 19.848 1.00 37.98 ? 1599 HIS B CB 1 ATOM 2594 C CG . HIS B 2 63 ? 20.229 34.589 20.015 1.00 40.23 ? 1599 HIS B CG 1 ATOM 2595 N ND1 . HIS B 2 63 ? 20.818 35.817 20.219 1.00 42.97 ? 1599 HIS B ND1 1 ATOM 2596 C CD2 . HIS B 2 63 ? 21.230 33.682 20.078 1.00 43.40 ? 1599 HIS B CD2 1 ATOM 2597 C CE1 . HIS B 2 63 ? 22.115 35.659 20.408 1.00 41.30 ? 1599 HIS B CE1 1 ATOM 2598 N NE2 . HIS B 2 63 ? 22.392 34.374 20.330 1.00 42.02 ? 1599 HIS B NE2 1 ATOM 2599 N N . LEU B 2 64 ? 19.379 36.932 17.689 1.00 34.29 ? 1600 LEU B N 1 ATOM 2600 C CA . LEU B 2 64 ? 19.720 38.346 17.577 1.00 33.18 ? 1600 LEU B CA 1 ATOM 2601 C C . LEU B 2 64 ? 18.526 39.265 17.245 1.00 33.95 ? 1600 LEU B C 1 ATOM 2602 O O . LEU B 2 64 ? 18.504 40.440 17.632 1.00 32.81 ? 1600 LEU B O 1 ATOM 2603 C CB . LEU B 2 64 ? 20.859 38.521 16.556 1.00 30.87 ? 1600 LEU B CB 1 ATOM 2604 C CG . LEU B 2 64 ? 22.231 38.931 17.141 1.00 30.74 ? 1600 LEU B CG 1 ATOM 2605 C CD1 . LEU B 2 64 ? 22.440 38.279 18.494 1.00 26.04 ? 1600 LEU B CD1 1 ATOM 2606 C CD2 . LEU B 2 64 ? 23.369 38.556 16.173 1.00 27.07 ? 1600 LEU B CD2 1 ATOM 2607 N N . GLY B 2 65 ? 17.535 38.736 16.542 1.00 31.11 ? 1601 GLY B N 1 ATOM 2608 C CA . GLY B 2 65 ? 16.365 39.529 16.229 1.00 31.16 ? 1601 GLY B CA 1 ATOM 2609 C C . GLY B 2 65 ? 16.617 40.848 15.529 1.00 33.42 ? 1601 GLY B C 1 ATOM 2610 O O . GLY B 2 65 ? 17.096 40.868 14.392 1.00 36.20 ? 1601 GLY B O 1 ATOM 2611 N N . ILE B 2 66 ? 16.303 41.949 16.214 1.00 32.23 ? 1602 ILE B N 1 ATOM 2612 C CA . ILE B 2 66 ? 16.453 43.294 15.668 1.00 31.87 ? 1602 ILE B CA 1 ATOM 2613 C C . ILE B 2 66 ? 17.889 43.766 15.580 1.00 31.13 ? 1602 ILE B C 1 ATOM 2614 O O . ILE B 2 66 ? 18.215 44.582 14.722 1.00 33.68 ? 1602 ILE B O 1 ATOM 2615 C CB . ILE B 2 66 ? 15.640 44.327 16.489 1.00 32.33 ? 1602 ILE B CB 1 ATOM 2616 C CG1 . ILE B 2 66 ? 15.509 45.632 15.713 1.00 28.80 ? 1602 ILE B CG1 1 ATOM 2617 C CG2 . ILE B 2 66 ? 16.312 44.599 17.810 1.00 33.91 ? 1602 ILE B CG2 1 ATOM 2618 C CD1 . ILE B 2 66 ? 14.538 45.533 14.576 1.00 31.51 ? 1602 ILE B CD1 1 ATOM 2619 N N . LEU B 2 67 ? 18.742 43.261 16.466 1.00 31.73 ? 1603 LEU B N 1 ATOM 2620 C CA . LEU B 2 67 ? 20.161 43.632 16.476 1.00 32.21 ? 1603 LEU B CA 1 ATOM 2621 C C . LEU B 2 67 ? 20.846 43.343 15.141 1.00 32.23 ? 1603 LEU B C 1 ATOM 2622 O O . LEU B 2 67 ? 20.354 42.539 14.345 1.00 33.06 ? 1603 LEU B O 1 ATOM 2623 C CB . LEU B 2 67 ? 20.913 42.892 17.600 1.00 30.49 ? 1603 LEU B CB 1 ATOM 2624 C CG . LEU B 2 67 ? 20.797 43.398 19.048 1.00 27.82 ? 1603 LEU B CG 1 ATOM 2625 C CD1 . LEU B 2 67 ? 19.332 43.557 19.402 1.00 29.83 ? 1603 LEU B CD1 1 ATOM 2626 C CD2 . LEU B 2 67 ? 21.455 42.403 20.016 1.00 25.91 ? 1603 LEU B CD2 1 ATOM 2627 N N . GLY B 2 68 ? 21.982 44.005 14.911 1.00 32.83 ? 1604 GLY B N 1 ATOM 2628 C CA . GLY B 2 68 ? 22.751 43.826 13.685 1.00 32.85 ? 1604 GLY B CA 1 ATOM 2629 C C . GLY B 2 68 ? 23.800 42.730 13.828 1.00 33.94 ? 1604 GLY B C 1 ATOM 2630 O O . GLY B 2 68 ? 23.885 42.090 14.872 1.00 35.46 ? 1604 GLY B O 1 ATOM 2631 N N . PRO B 2 69 ? 24.627 42.485 12.808 1.00 32.27 ? 1605 PRO B N 1 ATOM 2632 C CA . PRO B 2 69 ? 25.614 41.424 12.976 1.00 32.03 ? 1605 PRO B CA 1 ATOM 2633 C C . PRO B 2 69 ? 26.571 41.737 14.118 1.00 34.78 ? 1605 PRO B C 1 ATOM 2634 O O . PRO B 2 69 ? 26.938 42.896 14.313 1.00 38.05 ? 1605 PRO B O 1 ATOM 2635 C CB . PRO B 2 69 ? 26.283 41.374 11.614 1.00 29.32 ? 1605 PRO B CB 1 ATOM 2636 C CG . PRO B 2 69 ? 26.244 42.761 11.186 1.00 33.26 ? 1605 PRO B CG 1 ATOM 2637 C CD . PRO B 2 69 ? 24.837 43.190 11.539 1.00 33.48 ? 1605 PRO B CD 1 ATOM 2638 N N . VAL B 2 70 ? 26.971 40.712 14.871 1.00 34.87 ? 1606 VAL B N 1 ATOM 2639 C CA . VAL B 2 70 ? 27.858 40.914 16.009 1.00 36.35 ? 1606 VAL B CA 1 ATOM 2640 C C . VAL B 2 70 ? 29.309 41.166 15.669 1.00 39.56 ? 1606 VAL B C 1 ATOM 2641 O O . VAL B 2 70 ? 30.061 40.229 15.452 1.00 44.25 ? 1606 VAL B O 1 ATOM 2642 C CB . VAL B 2 70 ? 27.800 39.729 17.010 1.00 32.40 ? 1606 VAL B CB 1 ATOM 2643 C CG1 . VAL B 2 70 ? 27.855 38.437 16.283 1.00 40.43 ? 1606 VAL B CG1 1 ATOM 2644 C CG2 . VAL B 2 70 ? 28.965 39.796 17.958 1.00 30.40 ? 1606 VAL B CG2 1 ATOM 2645 N N . ILE B 2 71 ? 29.703 42.438 15.625 1.00 42.32 ? 1607 ILE B N 1 ATOM 2646 C CA . ILE B 2 71 ? 31.093 42.788 15.349 1.00 42.40 ? 1607 ILE B CA 1 ATOM 2647 C C . ILE B 2 71 ? 31.864 42.210 16.520 1.00 43.80 ? 1607 ILE B C 1 ATOM 2648 O O . ILE B 2 71 ? 31.412 42.275 17.655 1.00 43.29 ? 1607 ILE B O 1 ATOM 2649 C CB . ILE B 2 71 ? 31.294 44.299 15.289 1.00 40.01 ? 1607 ILE B CB 1 ATOM 2650 C CG1 . ILE B 2 71 ? 30.378 44.888 14.217 1.00 39.34 ? 1607 ILE B CG1 1 ATOM 2651 C CG2 . ILE B 2 71 ? 32.750 44.605 15.002 1.00 37.78 ? 1607 ILE B CG2 1 ATOM 2652 C CD1 . ILE B 2 71 ? 30.449 46.388 14.089 1.00 41.11 ? 1607 ILE B CD1 1 ATOM 2653 N N . ARG B 2 72 ? 33.027 41.644 16.252 1.00 46.10 ? 1608 ARG B N 1 ATOM 2654 C CA . ARG B 2 72 ? 33.789 40.998 17.306 1.00 50.48 ? 1608 ARG B CA 1 ATOM 2655 C C . ARG B 2 72 ? 35.276 41.092 17.035 1.00 53.28 ? 1608 ARG B C 1 ATOM 2656 O O . ARG B 2 72 ? 35.693 41.177 15.876 1.00 54.88 ? 1608 ARG B O 1 ATOM 2657 C CB . ARG B 2 72 ? 33.343 39.539 17.375 1.00 50.33 ? 1608 ARG B CB 1 ATOM 2658 C CG . ARG B 2 72 ? 34.156 38.634 18.255 1.00 52.96 ? 1608 ARG B CG 1 ATOM 2659 C CD . ARG B 2 72 ? 33.305 37.438 18.644 1.00 55.19 ? 1608 ARG B CD 1 ATOM 2660 N NE . ARG B 2 72 ? 32.388 37.064 17.572 1.00 56.28 ? 1608 ARG B NE 1 ATOM 2661 C CZ . ARG B 2 72 ? 31.240 36.423 17.768 1.00 55.41 ? 1608 ARG B CZ 1 ATOM 2662 N NH1 . ARG B 2 72 ? 30.879 36.091 19.000 1.00 54.33 ? 1608 ARG B NH1 1 ATOM 2663 N NH2 . ARG B 2 72 ? 30.454 36.123 16.738 1.00 53.07 ? 1608 ARG B NH2 1 ATOM 2664 N N . ALA B 2 73 ? 36.076 41.057 18.096 1.00 55.40 ? 1609 ALA B N 1 ATOM 2665 C CA . ALA B 2 73 ? 37.519 41.174 17.934 1.00 56.72 ? 1609 ALA B CA 1 ATOM 2666 C C . ALA B 2 73 ? 38.321 41.009 19.218 1.00 56.93 ? 1609 ALA B C 1 ATOM 2667 O O . ALA B 2 73 ? 37.840 41.295 20.304 1.00 55.78 ? 1609 ALA B O 1 ATOM 2668 C CB . ALA B 2 73 ? 37.842 42.533 17.303 1.00 56.83 ? 1609 ALA B CB 1 ATOM 2669 N N . GLU B 2 74 ? 39.560 40.555 19.069 1.00 60.23 ? 1610 GLU B N 1 ATOM 2670 C CA . GLU B 2 74 ? 40.463 40.376 20.200 1.00 62.57 ? 1610 GLU B CA 1 ATOM 2671 C C . GLU B 2 74 ? 41.150 41.722 20.458 1.00 62.12 ? 1610 GLU B C 1 ATOM 2672 O O . GLU B 2 74 ? 40.954 42.684 19.720 1.00 59.87 ? 1610 GLU B O 1 ATOM 2673 C CB . GLU B 2 74 ? 41.530 39.308 19.892 1.00 64.01 ? 1610 GLU B CB 1 ATOM 2674 C CG . GLU B 2 74 ? 40.992 37.984 19.352 1.00 67.59 ? 1610 GLU B CG 1 ATOM 2675 C CD . GLU B 2 74 ? 42.060 36.893 19.251 1.00 70.35 ? 1610 GLU B CD 1 ATOM 2676 O OE1 . GLU B 2 74 ? 43.216 37.205 18.894 1.00 71.03 ? 1610 GLU B OE1 1 ATOM 2677 O OE2 . GLU B 2 74 ? 41.738 35.714 19.515 1.00 71.63 ? 1610 GLU B OE2 1 ATOM 2678 N N . VAL B 2 75 ? 41.957 41.778 21.508 1.00 63.43 ? 1611 VAL B N 1 ATOM 2679 C CA . VAL B 2 75 ? 42.674 42.992 21.859 1.00 64.29 ? 1611 VAL B CA 1 ATOM 2680 C C . VAL B 2 75 ? 43.821 43.249 20.869 1.00 66.02 ? 1611 VAL B C 1 ATOM 2681 O O . VAL B 2 75 ? 44.399 42.311 20.317 1.00 66.72 ? 1611 VAL B O 1 ATOM 2682 C CB . VAL B 2 75 ? 43.209 42.884 23.297 1.00 61.73 ? 1611 VAL B CB 1 ATOM 2683 C CG1 . VAL B 2 75 ? 43.820 44.200 23.741 1.00 64.20 ? 1611 VAL B CG1 1 ATOM 2684 C CG2 . VAL B 2 75 ? 42.075 42.504 24.222 1.00 60.69 ? 1611 VAL B CG2 1 ATOM 2685 N N . ASP B 2 76 ? 44.127 44.526 20.644 1.00 67.11 ? 1612 ASP B N 1 ATOM 2686 C CA . ASP B 2 76 ? 45.176 44.953 19.715 1.00 69.76 ? 1612 ASP B CA 1 ATOM 2687 C C . ASP B 2 76 ? 44.756 44.728 18.269 1.00 69.21 ? 1612 ASP B C 1 ATOM 2688 O O . ASP B 2 76 ? 45.456 45.104 17.325 1.00 70.20 ? 1612 ASP B O 1 ATOM 2689 C CB . ASP B 2 76 ? 46.501 44.225 19.993 1.00 73.14 ? 1612 ASP B CB 1 ATOM 2690 C CG . ASP B 2 76 ? 47.233 44.777 21.219 1.00 76.84 ? 1612 ASP B CG 1 ATOM 2691 O OD1 . ASP B 2 76 ? 47.378 46.022 21.328 1.00 76.93 ? 1612 ASP B OD1 1 ATOM 2692 O OD2 . ASP B 2 76 ? 47.673 43.962 22.067 1.00 78.30 ? 1612 ASP B OD2 1 ATOM 2693 N N . ASP B 2 77 ? 43.595 44.114 18.108 1.00 68.74 ? 1613 ASP B N 1 ATOM 2694 C CA . ASP B 2 77 ? 43.046 43.838 16.793 1.00 68.21 ? 1613 ASP B CA 1 ATOM 2695 C C . ASP B 2 77 ? 42.608 45.149 16.158 1.00 65.66 ? 1613 ASP B C 1 ATOM 2696 O O . ASP B 2 77 ? 42.501 46.170 16.827 1.00 66.71 ? 1613 ASP B O 1 ATOM 2697 C CB . ASP B 2 77 ? 41.850 42.904 16.933 1.00 73.48 ? 1613 ASP B CB 1 ATOM 2698 C CG . ASP B 2 77 ? 42.002 41.637 16.128 1.00 77.76 ? 1613 ASP B CG 1 ATOM 2699 O OD1 . ASP B 2 77 ? 43.152 41.181 15.941 1.00 82.32 ? 1613 ASP B OD1 1 ATOM 2700 O OD2 . ASP B 2 77 ? 40.965 41.086 15.698 1.00 80.60 ? 1613 ASP B OD2 1 ATOM 2701 N N . VAL B 2 78 ? 42.351 45.122 14.862 1.00 61.53 ? 1614 VAL B N 1 ATOM 2702 C CA . VAL B 2 78 ? 41.926 46.321 14.179 1.00 58.16 ? 1614 VAL B CA 1 ATOM 2703 C C . VAL B 2 78 ? 40.612 46.024 13.468 1.00 56.31 ? 1614 VAL B C 1 ATOM 2704 O O . VAL B 2 78 ? 40.526 45.133 12.624 1.00 52.74 ? 1614 VAL B O 1 ATOM 2705 C CB . VAL B 2 78 ? 43.009 46.786 13.169 1.00 59.01 ? 1614 VAL B CB 1 ATOM 2706 C CG1 . VAL B 2 78 ? 42.642 48.143 12.568 1.00 55.28 ? 1614 VAL B CG1 1 ATOM 2707 C CG2 . VAL B 2 78 ? 44.361 46.864 13.876 1.00 60.37 ? 1614 VAL B CG2 1 ATOM 2708 N N . ILE B 2 79 ? 39.580 46.768 13.833 1.00 54.21 ? 1615 ILE B N 1 ATOM 2709 C CA . ILE B 2 79 ? 38.280 46.564 13.230 1.00 53.53 ? 1615 ILE B CA 1 ATOM 2710 C C . ILE B 2 79 ? 38.032 47.579 12.129 1.00 53.81 ? 1615 ILE B C 1 ATOM 2711 O O . ILE B 2 79 ? 38.092 48.777 12.363 1.00 55.05 ? 1615 ILE B O 1 ATOM 2712 C CB . ILE B 2 79 ? 37.149 46.668 14.291 1.00 51.84 ? 1615 ILE B CB 1 ATOM 2713 C CG1 . ILE B 2 79 ? 37.422 45.682 15.442 1.00 54.01 ? 1615 ILE B CG1 1 ATOM 2714 C CG2 . ILE B 2 79 ? 35.813 46.366 13.651 1.00 49.10 ? 1615 ILE B CG2 1 ATOM 2715 C CD1 . ILE B 2 79 ? 36.299 45.559 16.470 1.00 52.26 ? 1615 ILE B CD1 1 ATOM 2716 N N . GLN B 2 80 ? 37.772 47.100 10.920 1.00 52.98 ? 1616 GLN B N 1 ATOM 2717 C CA . GLN B 2 80 ? 37.487 47.994 9.814 1.00 52.58 ? 1616 GLN B CA 1 ATOM 2718 C C . GLN B 2 80 ? 36.125 47.638 9.236 1.00 52.80 ? 1616 GLN B C 1 ATOM 2719 O O . GLN B 2 80 ? 35.953 46.575 8.642 1.00 53.42 ? 1616 GLN B O 1 ATOM 2720 C CB . GLN B 2 80 ? 38.555 47.866 8.732 1.00 54.11 ? 1616 GLN B CB 1 ATOM 2721 C CG . GLN B 2 80 ? 38.292 48.767 7.526 1.00 54.27 ? 1616 GLN B CG 1 ATOM 2722 C CD . GLN B 2 80 ? 39.442 48.768 6.541 1.00 55.62 ? 1616 GLN B CD 1 ATOM 2723 O OE1 . GLN B 2 80 ? 40.609 48.674 6.941 1.00 57.98 ? 1616 GLN B OE1 1 ATOM 2724 N NE2 . GLN B 2 80 ? 39.128 48.894 5.251 1.00 49.69 ? 1616 GLN B NE2 1 ATOM 2725 N N . VAL B 2 81 ? 35.151 48.521 9.407 1.00 51.80 ? 1617 VAL B N 1 ATOM 2726 C CA . VAL B 2 81 ? 33.823 48.243 8.891 1.00 51.92 ? 1617 VAL B CA 1 ATOM 2727 C C . VAL B 2 81 ? 33.445 49.208 7.760 1.00 53.58 ? 1617 VAL B C 1 ATOM 2728 O O . VAL B 2 81 ? 33.574 50.426 7.886 1.00 52.74 ? 1617 VAL B O 1 ATOM 2729 C CB . VAL B 2 81 ? 32.757 48.287 10.040 1.00 50.94 ? 1617 VAL B CB 1 ATOM 2730 C CG1 . VAL B 2 81 ? 33.368 47.771 11.343 1.00 47.28 ? 1617 VAL B CG1 1 ATOM 2731 C CG2 . VAL B 2 81 ? 32.226 49.681 10.230 1.00 51.14 ? 1617 VAL B CG2 1 ATOM 2732 N N . ARG B 2 82 ? 33.001 48.645 6.641 1.00 55.02 ? 1618 ARG B N 1 ATOM 2733 C CA . ARG B 2 82 ? 32.598 49.438 5.495 1.00 56.29 ? 1618 ARG B CA 1 ATOM 2734 C C . ARG B 2 82 ? 31.100 49.641 5.560 1.00 55.57 ? 1618 ARG B C 1 ATOM 2735 O O . ARG B 2 82 ? 30.326 48.769 5.181 1.00 55.57 ? 1618 ARG B O 1 ATOM 2736 C CB . ARG B 2 82 ? 32.948 48.725 4.194 1.00 60.91 ? 1618 ARG B CB 1 ATOM 2737 C CG . ARG B 2 82 ? 32.570 49.513 2.943 1.00 64.21 ? 1618 ARG B CG 1 ATOM 2738 C CD . ARG B 2 82 ? 33.485 50.709 2.752 1.00 68.51 ? 1618 ARG B CD 1 ATOM 2739 N NE . ARG B 2 82 ? 34.537 50.462 1.766 1.00 72.23 ? 1618 ARG B NE 1 ATOM 2740 C CZ . ARG B 2 82 ? 34.319 50.328 0.459 1.00 74.23 ? 1618 ARG B CZ 1 ATOM 2741 N NH1 . ARG B 2 82 ? 33.085 50.416 -0.029 1.00 73.24 ? 1618 ARG B NH1 1 ATOM 2742 N NH2 . ARG B 2 82 ? 35.335 50.112 -0.361 1.00 75.40 ? 1618 ARG B NH2 1 ATOM 2743 N N . PHE B 2 83 ? 30.705 50.812 6.032 1.00 55.12 ? 1619 PHE B N 1 ATOM 2744 C CA . PHE B 2 83 ? 29.303 51.164 6.182 1.00 55.06 ? 1619 PHE B CA 1 ATOM 2745 C C . PHE B 2 83 ? 28.722 51.740 4.905 1.00 53.95 ? 1619 PHE B C 1 ATOM 2746 O O . PHE B 2 83 ? 29.221 52.739 4.402 1.00 52.99 ? 1619 PHE B O 1 ATOM 2747 C CB . PHE B 2 83 ? 29.168 52.177 7.315 1.00 56.61 ? 1619 PHE B CB 1 ATOM 2748 C CG . PHE B 2 83 ? 27.769 52.584 7.597 1.00 57.29 ? 1619 PHE B CG 1 ATOM 2749 C CD1 . PHE B 2 83 ? 26.797 51.628 7.844 1.00 57.15 ? 1619 PHE B CD1 1 ATOM 2750 C CD2 . PHE B 2 83 ? 27.426 53.926 7.646 1.00 59.56 ? 1619 PHE B CD2 1 ATOM 2751 C CE1 . PHE B 2 83 ? 25.505 51.998 8.140 1.00 58.51 ? 1619 PHE B CE1 1 ATOM 2752 C CE2 . PHE B 2 83 ? 26.138 54.314 7.941 1.00 59.69 ? 1619 PHE B CE2 1 ATOM 2753 C CZ . PHE B 2 83 ? 25.170 53.347 8.190 1.00 60.01 ? 1619 PHE B CZ 1 ATOM 2754 N N . LYS B 2 84 ? 27.658 51.116 4.396 1.00 54.50 ? 1620 LYS B N 1 ATOM 2755 C CA . LYS B 2 84 ? 27.017 51.571 3.168 1.00 54.40 ? 1620 LYS B CA 1 ATOM 2756 C C . LYS B 2 84 ? 25.866 52.512 3.391 1.00 56.29 ? 1620 LYS B C 1 ATOM 2757 O O . LYS B 2 84 ? 25.858 53.609 2.842 1.00 61.00 ? 1620 LYS B O 1 ATOM 2758 C CB . LYS B 2 84 ? 26.510 50.398 2.348 1.00 55.19 ? 1620 LYS B CB 1 ATOM 2759 C CG . LYS B 2 84 ? 25.689 50.784 1.109 1.00 53.23 ? 1620 LYS B CG 1 ATOM 2760 C CD . LYS B 2 84 ? 26.543 51.439 0.028 1.00 53.22 ? 1620 LYS B CD 1 ATOM 2761 C CE . LYS B 2 84 ? 25.823 51.533 -1.322 1.00 50.49 ? 1620 LYS B CE 1 ATOM 2762 N NZ . LYS B 2 84 ? 25.620 50.204 -1.964 1.00 51.01 ? 1620 LYS B NZ 1 ATOM 2763 N N . ASN B 2 85 ? 24.885 52.102 4.176 1.00 55.44 ? 1621 ASN B N 1 ATOM 2764 C CA . ASN B 2 85 ? 23.723 52.962 4.421 1.00 58.14 ? 1621 ASN B CA 1 ATOM 2765 C C . ASN B 2 85 ? 22.798 53.070 3.213 1.00 57.70 ? 1621 ASN B C 1 ATOM 2766 O O . ASN B 2 85 ? 22.958 53.963 2.373 1.00 55.57 ? 1621 ASN B O 1 ATOM 2767 C CB . ASN B 2 85 ? 24.137 54.380 4.815 1.00 58.90 ? 1621 ASN B CB 1 ATOM 2768 C CG . ASN B 2 85 ? 22.959 55.352 4.780 1.00 64.63 ? 1621 ASN B CG 1 ATOM 2769 O OD1 . ASN B 2 85 ? 21.791 54.936 4.747 1.00 64.52 ? 1621 ASN B OD1 1 ATOM 2770 N ND2 . ASN B 2 85 ? 23.258 56.653 4.799 1.00 67.91 ? 1621 ASN B ND2 1 ATOM 2771 N N . LEU B 2 86 ? 21.808 52.181 3.164 1.00 55.82 ? 1622 LEU B N 1 ATOM 2772 C CA . LEU B 2 86 ? 20.860 52.137 2.067 1.00 53.64 ? 1622 LEU B CA 1 ATOM 2773 C C . LEU B 2 86 ? 19.511 52.739 2.432 1.00 52.35 ? 1622 LEU B C 1 ATOM 2774 O O . LEU B 2 86 ? 18.522 52.522 1.733 1.00 52.80 ? 1622 LEU B O 1 ATOM 2775 C CB . LEU B 2 86 ? 20.677 50.683 1.625 1.00 53.34 ? 1622 LEU B CB 1 ATOM 2776 C CG . LEU B 2 86 ? 21.970 49.927 1.295 1.00 53.93 ? 1622 LEU B CG 1 ATOM 2777 C CD1 . LEU B 2 86 ? 21.692 48.428 1.267 1.00 53.76 ? 1622 LEU B CD1 1 ATOM 2778 C CD2 . LEU B 2 86 ? 22.534 50.407 -0.041 1.00 53.62 ? 1622 LEU B CD2 1 ATOM 2779 N N . ALA B 2 87 ? 19.461 53.495 3.519 1.00 50.65 ? 1623 ALA B N 1 ATOM 2780 C CA . ALA B 2 87 ? 18.190 54.079 3.929 1.00 52.98 ? 1623 ALA B CA 1 ATOM 2781 C C . ALA B 2 87 ? 17.911 55.427 3.265 1.00 54.18 ? 1623 ALA B C 1 ATOM 2782 O O . ALA B 2 87 ? 18.702 55.915 2.460 1.00 54.33 ? 1623 ALA B O 1 ATOM 2783 C CB . ALA B 2 87 ? 18.128 54.207 5.458 1.00 52.45 ? 1623 ALA B CB 1 ATOM 2784 N N . SER B 2 88 ? 16.781 56.019 3.624 1.00 54.95 ? 1624 SER B N 1 ATOM 2785 C CA . SER B 2 88 ? 16.343 57.281 3.056 1.00 56.90 ? 1624 SER B CA 1 ATOM 2786 C C . SER B 2 88 ? 16.932 58.544 3.680 1.00 58.60 ? 1624 SER B C 1 ATOM 2787 O O . SER B 2 88 ? 16.931 59.605 3.048 1.00 59.06 ? 1624 SER B O 1 ATOM 2788 C CB . SER B 2 88 ? 14.816 57.358 3.110 1.00 56.75 ? 1624 SER B CB 1 ATOM 2789 O OG . SER B 2 88 ? 14.349 57.318 4.450 1.00 58.06 ? 1624 SER B OG 1 ATOM 2790 N N . ARG B 2 89 ? 17.433 58.445 4.906 1.00 58.37 ? 1625 ARG B N 1 ATOM 2791 C CA . ARG B 2 89 ? 17.992 59.612 5.557 1.00 57.28 ? 1625 ARG B CA 1 ATOM 2792 C C . ARG B 2 89 ? 19.414 59.357 6.026 1.00 58.93 ? 1625 ARG B C 1 ATOM 2793 O O . ARG B 2 89 ? 19.935 58.254 5.871 1.00 60.05 ? 1625 ARG B O 1 ATOM 2794 C CB . ARG B 2 89 ? 17.114 60.019 6.734 1.00 57.09 ? 1625 ARG B CB 1 ATOM 2795 C CG . ARG B 2 89 ? 17.320 59.217 7.992 1.00 61.16 ? 1625 ARG B CG 1 ATOM 2796 C CD . ARG B 2 89 ? 16.479 59.784 9.123 1.00 63.72 ? 1625 ARG B CD 1 ATOM 2797 N NE . ARG B 2 89 ? 16.912 61.123 9.530 1.00 67.71 ? 1625 ARG B NE 1 ATOM 2798 C CZ . ARG B 2 89 ? 17.766 61.378 10.525 1.00 70.00 ? 1625 ARG B CZ 1 ATOM 2799 N NH1 . ARG B 2 89 ? 18.305 60.386 11.241 1.00 69.35 ? 1625 ARG B NH1 1 ATOM 2800 N NH2 . ARG B 2 89 ? 18.067 62.638 10.818 1.00 67.81 ? 1625 ARG B NH2 1 ATOM 2801 N N . PRO B 2 90 ? 20.075 60.385 6.591 1.00 59.47 ? 1626 PRO B N 1 ATOM 2802 C CA . PRO B 2 90 ? 21.448 60.191 7.061 1.00 56.57 ? 1626 PRO B CA 1 ATOM 2803 C C . PRO B 2 90 ? 21.474 59.304 8.291 1.00 54.03 ? 1626 PRO B C 1 ATOM 2804 O O . PRO B 2 90 ? 20.544 59.336 9.097 1.00 53.41 ? 1626 PRO B O 1 ATOM 2805 C CB . PRO B 2 90 ? 21.910 61.618 7.383 1.00 57.28 ? 1626 PRO B CB 1 ATOM 2806 C CG . PRO B 2 90 ? 21.093 62.462 6.471 1.00 58.57 ? 1626 PRO B CG 1 ATOM 2807 C CD . PRO B 2 90 ? 19.735 61.822 6.581 1.00 59.96 ? 1626 PRO B CD 1 ATOM 2808 N N . TYR B 2 91 ? 22.538 58.513 8.422 1.00 52.68 ? 1627 TYR B N 1 ATOM 2809 C CA . TYR B 2 91 ? 22.741 57.628 9.578 1.00 49.83 ? 1627 TYR B CA 1 ATOM 2810 C C . TYR B 2 91 ? 24.243 57.457 9.757 1.00 49.71 ? 1627 TYR B C 1 ATOM 2811 O O . TYR B 2 91 ? 25.021 57.892 8.904 1.00 49.05 ? 1627 TYR B O 1 ATOM 2812 C CB . TYR B 2 91 ? 22.080 56.266 9.360 1.00 43.20 ? 1627 TYR B CB 1 ATOM 2813 C CG . TYR B 2 91 ? 20.573 56.280 9.476 1.00 37.90 ? 1627 TYR B CG 1 ATOM 2814 C CD1 . TYR B 2 91 ? 19.941 56.529 10.695 1.00 36.89 ? 1627 TYR B CD1 1 ATOM 2815 C CD2 . TYR B 2 91 ? 19.780 56.034 8.367 1.00 37.04 ? 1627 TYR B CD2 1 ATOM 2816 C CE1 . TYR B 2 91 ? 18.551 56.528 10.795 1.00 34.88 ? 1627 TYR B CE1 1 ATOM 2817 C CE2 . TYR B 2 91 ? 18.402 56.028 8.457 1.00 38.60 ? 1627 TYR B CE2 1 ATOM 2818 C CZ . TYR B 2 91 ? 17.795 56.272 9.670 1.00 38.55 ? 1627 TYR B CZ 1 ATOM 2819 O OH . TYR B 2 91 ? 16.425 56.215 9.730 1.00 43.20 ? 1627 TYR B OH 1 ATOM 2820 N N . SER B 2 92 ? 24.649 56.835 10.857 1.00 49.26 ? 1628 SER B N 1 ATOM 2821 C CA . SER B 2 92 ? 26.067 56.635 11.132 1.00 50.04 ? 1628 SER B CA 1 ATOM 2822 C C . SER B 2 92 ? 26.269 55.365 11.919 1.00 52.80 ? 1628 SER B C 1 ATOM 2823 O O . SER B 2 92 ? 25.316 54.794 12.456 1.00 55.24 ? 1628 SER B O 1 ATOM 2824 C CB . SER B 2 92 ? 26.612 57.779 11.965 1.00 50.41 ? 1628 SER B CB 1 ATOM 2825 O OG . SER B 2 92 ? 26.130 57.671 13.295 1.00 48.35 ? 1628 SER B OG 1 ATOM 2826 N N . LEU B 2 93 ? 27.523 54.944 12.028 1.00 52.48 ? 1629 LEU B N 1 ATOM 2827 C CA . LEU B 2 93 ? 27.846 53.725 12.755 1.00 50.61 ? 1629 LEU B CA 1 ATOM 2828 C C . LEU B 2 93 ? 28.857 54.059 13.816 1.00 51.56 ? 1629 LEU B C 1 ATOM 2829 O O . LEU B 2 93 ? 30.049 54.090 13.547 1.00 53.83 ? 1629 LEU B O 1 ATOM 2830 C CB . LEU B 2 93 ? 28.436 52.695 11.797 1.00 48.53 ? 1629 LEU B CB 1 ATOM 2831 C CG . LEU B 2 93 ? 28.410 51.220 12.170 1.00 45.66 ? 1629 LEU B CG 1 ATOM 2832 C CD1 . LEU B 2 93 ? 29.039 50.457 11.038 1.00 42.64 ? 1629 LEU B CD1 1 ATOM 2833 C CD2 . LEU B 2 93 ? 29.152 50.969 13.464 1.00 44.30 ? 1629 LEU B CD2 1 ATOM 2834 N N . HIS B 2 94 ? 28.385 54.318 15.024 1.00 53.01 ? 1630 HIS B N 1 ATOM 2835 C CA . HIS B 2 94 ? 29.280 54.653 16.114 1.00 53.67 ? 1630 HIS B CA 1 ATOM 2836 C C . HIS B 2 94 ? 29.534 53.392 16.925 1.00 55.73 ? 1630 HIS B C 1 ATOM 2837 O O . HIS B 2 94 ? 28.610 52.633 17.212 1.00 55.89 ? 1630 HIS B O 1 ATOM 2838 C CB . HIS B 2 94 ? 28.646 55.737 16.987 1.00 52.85 ? 1630 HIS B CB 1 ATOM 2839 C CG . HIS B 2 94 ? 29.490 56.162 18.152 1.00 56.52 ? 1630 HIS B CG 1 ATOM 2840 N ND1 . HIS B 2 94 ? 30.075 55.263 19.020 1.00 60.40 ? 1630 HIS B ND1 1 ATOM 2841 C CD2 . HIS B 2 94 ? 29.793 57.393 18.629 1.00 56.59 ? 1630 HIS B CD2 1 ATOM 2842 C CE1 . HIS B 2 94 ? 30.698 55.920 19.982 1.00 59.56 ? 1630 HIS B CE1 1 ATOM 2843 N NE2 . HIS B 2 94 ? 30.541 57.214 19.769 1.00 58.21 ? 1630 HIS B NE2 1 ATOM 2844 N N . ALA B 2 95 ? 30.793 53.163 17.277 1.00 58.18 ? 1631 ALA B N 1 ATOM 2845 C CA . ALA B 2 95 ? 31.160 52.004 18.073 1.00 60.46 ? 1631 ALA B CA 1 ATOM 2846 C C . ALA B 2 95 ? 31.438 52.449 19.501 1.00 63.15 ? 1631 ALA B C 1 ATOM 2847 O O . ALA B 2 95 ? 32.538 52.871 19.840 1.00 64.91 ? 1631 ALA B O 1 ATOM 2848 C CB . ALA B 2 95 ? 32.385 51.327 17.491 1.00 59.45 ? 1631 ALA B CB 1 ATOM 2849 N N . HIS B 2 96 ? 30.417 52.352 20.334 1.00 67.47 ? 1632 HIS B N 1 ATOM 2850 C CA . HIS B 2 96 ? 30.516 52.731 21.732 1.00 70.87 ? 1632 HIS B CA 1 ATOM 2851 C C . HIS B 2 96 ? 31.581 51.912 22.459 1.00 73.15 ? 1632 HIS B C 1 ATOM 2852 O O . HIS B 2 96 ? 31.376 50.736 22.760 1.00 74.26 ? 1632 HIS B O 1 ATOM 2853 C CB . HIS B 2 96 ? 29.155 52.528 22.384 1.00 69.75 ? 1632 HIS B CB 1 ATOM 2854 C CG . HIS B 2 96 ? 29.082 52.982 23.803 1.00 69.80 ? 1632 HIS B CG 1 ATOM 2855 N ND1 . HIS B 2 96 ? 29.777 52.363 24.818 1.00 70.22 ? 1632 HIS B ND1 1 ATOM 2856 C CD2 . HIS B 2 96 ? 28.357 53.965 24.386 1.00 70.24 ? 1632 HIS B CD2 1 ATOM 2857 C CE1 . HIS B 2 96 ? 29.478 52.942 25.968 1.00 71.69 ? 1632 HIS B CE1 1 ATOM 2858 N NE2 . HIS B 2 96 ? 28.618 53.917 25.733 1.00 73.25 ? 1632 HIS B NE2 1 ATOM 2859 N N . GLY B 2 97 ? 32.721 52.540 22.732 1.00 75.99 ? 1633 GLY B N 1 ATOM 2860 C CA . GLY B 2 97 ? 33.793 51.855 23.433 1.00 81.08 ? 1633 GLY B CA 1 ATOM 2861 C C . GLY B 2 97 ? 35.144 51.965 22.749 1.00 83.96 ? 1633 GLY B C 1 ATOM 2862 O O . GLY B 2 97 ? 36.086 51.248 23.105 1.00 83.06 ? 1633 GLY B O 1 ATOM 2863 N N . LEU B 2 98 ? 35.242 52.858 21.765 1.00 86.41 ? 1634 LEU B N 1 ATOM 2864 C CA . LEU B 2 98 ? 36.490 53.052 21.035 1.00 88.22 ? 1634 LEU B CA 1 ATOM 2865 C C . LEU B 2 98 ? 37.647 53.245 22.021 1.00 90.86 ? 1634 LEU B C 1 ATOM 2866 O O . LEU B 2 98 ? 38.415 52.309 22.281 1.00 91.29 ? 1634 LEU B O 1 ATOM 2867 C CB . LEU B 2 98 ? 36.366 54.264 20.098 1.00 86.61 ? 1634 LEU B CB 1 ATOM 2868 C CG . LEU B 2 98 ? 37.568 54.674 19.230 1.00 86.00 ? 1634 LEU B CG 1 ATOM 2869 C CD1 . LEU B 2 98 ? 37.074 55.383 17.985 1.00 85.09 ? 1634 LEU B CD1 1 ATOM 2870 C CD2 . LEU B 2 98 ? 38.516 55.575 20.011 1.00 84.78 ? 1634 LEU B CD2 1 ATOM 2871 N N . SER B 2 99 ? 37.750 54.452 22.580 1.00 92.38 ? 1635 SER B N 1 ATOM 2872 C CA . SER B 2 99 ? 38.803 54.799 23.539 1.00 93.17 ? 1635 SER B CA 1 ATOM 2873 C C . SER B 2 99 ? 40.182 54.843 22.882 1.00 93.06 ? 1635 SER B C 1 ATOM 2874 O O . SER B 2 99 ? 40.997 55.718 23.180 1.00 93.28 ? 1635 SER B O 1 ATOM 2875 C CB . SER B 2 99 ? 38.818 53.799 24.701 1.00 93.73 ? 1635 SER B CB 1 ATOM 2876 O OG . SER B 2 99 ? 37.579 53.789 25.389 1.00 94.75 ? 1635 SER B OG 1 ATOM 2877 N N . ASN B 2 121 ? 29.246 64.314 10.823 1.00 69.46 ? 1657 ASN B N 1 ATOM 2878 C CA . ASN B 2 121 ? 29.811 63.019 10.459 1.00 69.00 ? 1657 ASN B CA 1 ATOM 2879 C C . ASN B 2 121 ? 28.718 62.097 9.922 1.00 68.51 ? 1657 ASN B C 1 ATOM 2880 O O . ASN B 2 121 ? 28.950 60.917 9.646 1.00 69.88 ? 1657 ASN B O 1 ATOM 2881 C CB . ASN B 2 121 ? 30.500 62.372 11.672 1.00 69.73 ? 1657 ASN B CB 1 ATOM 2882 C CG . ASN B 2 121 ? 29.525 62.013 12.791 1.00 71.14 ? 1657 ASN B CG 1 ATOM 2883 O OD1 . ASN B 2 121 ? 29.934 61.510 13.845 1.00 70.83 ? 1657 ASN B OD1 1 ATOM 2884 N ND2 . ASN B 2 121 ? 28.235 62.267 12.568 1.00 70.48 ? 1657 ASN B ND2 1 ATOM 2885 N N . ALA B 2 122 ? 27.526 62.656 9.761 1.00 65.96 ? 1658 ALA B N 1 ATOM 2886 C CA . ALA B 2 122 ? 26.385 61.906 9.268 1.00 62.63 ? 1658 ALA B CA 1 ATOM 2887 C C . ALA B 2 122 ? 26.569 61.437 7.837 1.00 60.88 ? 1658 ALA B C 1 ATOM 2888 O O . ALA B 2 122 ? 26.695 62.246 6.923 1.00 61.07 ? 1658 ALA B O 1 ATOM 2889 C CB . ALA B 2 122 ? 25.127 62.754 9.378 1.00 61.41 ? 1658 ALA B CB 1 ATOM 2890 N N . ILE B 2 123 ? 26.583 60.123 7.644 1.00 60.11 ? 1659 ILE B N 1 ATOM 2891 C CA . ILE B 2 123 ? 26.725 59.567 6.305 1.00 59.37 ? 1659 ILE B CA 1 ATOM 2892 C C . ILE B 2 123 ? 25.398 59.731 5.576 1.00 61.04 ? 1659 ILE B C 1 ATOM 2893 O O . ILE B 2 123 ? 24.341 59.408 6.115 1.00 63.91 ? 1659 ILE B O 1 ATOM 2894 C CB . ILE B 2 123 ? 27.071 58.081 6.337 1.00 55.54 ? 1659 ILE B CB 1 ATOM 2895 C CG1 . ILE B 2 123 ? 28.390 57.867 7.082 1.00 53.80 ? 1659 ILE B CG1 1 ATOM 2896 C CG2 . ILE B 2 123 ? 27.128 57.548 4.920 1.00 51.89 ? 1659 ILE B CG2 1 ATOM 2897 C CD1 . ILE B 2 123 ? 29.574 58.557 6.449 1.00 52.80 ? 1659 ILE B CD1 1 ATOM 2898 N N . GLN B 2 124 ? 25.455 60.230 4.348 1.00 61.40 ? 1660 GLN B N 1 ATOM 2899 C CA . GLN B 2 124 ? 24.246 60.446 3.578 1.00 60.78 ? 1660 GLN B CA 1 ATOM 2900 C C . GLN B 2 124 ? 23.780 59.185 2.865 1.00 60.65 ? 1660 GLN B C 1 ATOM 2901 O O . GLN B 2 124 ? 24.583 58.313 2.535 1.00 61.24 ? 1660 GLN B O 1 ATOM 2902 C CB . GLN B 2 124 ? 24.467 61.584 2.571 1.00 60.50 ? 1660 GLN B CB 1 ATOM 2903 C CG . GLN B 2 124 ? 23.643 62.840 2.864 1.00 59.68 ? 1660 GLN B CG 1 ATOM 2904 C CD . GLN B 2 124 ? 23.880 63.393 4.261 1.00 60.21 ? 1660 GLN B CD 1 ATOM 2905 O OE1 . GLN B 2 124 ? 23.011 64.041 4.836 1.00 62.59 ? 1660 GLN B OE1 1 ATOM 2906 N NE2 . GLN B 2 124 ? 25.064 63.146 4.807 1.00 60.68 ? 1660 GLN B NE2 1 ATOM 2907 N N . PRO B 2 125 ? 22.461 59.069 2.634 1.00 59.24 ? 1661 PRO B N 1 ATOM 2908 C CA . PRO B 2 125 ? 21.881 57.910 1.954 1.00 57.08 ? 1661 PRO B CA 1 ATOM 2909 C C . PRO B 2 125 ? 22.692 57.503 0.736 1.00 58.20 ? 1661 PRO B C 1 ATOM 2910 O O . PRO B 2 125 ? 23.480 58.286 0.221 1.00 57.03 ? 1661 PRO B O 1 ATOM 2911 C CB . PRO B 2 125 ? 20.491 58.403 1.582 1.00 56.50 ? 1661 PRO B CB 1 ATOM 2912 C CG . PRO B 2 125 ? 20.127 59.262 2.783 1.00 55.12 ? 1661 PRO B CG 1 ATOM 2913 C CD . PRO B 2 125 ? 21.410 60.013 3.073 1.00 56.93 ? 1661 PRO B CD 1 ATOM 2914 N N . ASN B 2 126 ? 22.495 56.264 0.295 1.00 62.33 ? 1662 ASN B N 1 ATOM 2915 C CA . ASN B 2 126 ? 23.169 55.716 -0.875 1.00 63.95 ? 1662 ASN B CA 1 ATOM 2916 C C . ASN B 2 126 ? 24.685 55.942 -0.897 1.00 64.27 ? 1662 ASN B C 1 ATOM 2917 O O . ASN B 2 126 ? 25.324 55.654 -1.900 1.00 64.45 ? 1662 ASN B O 1 ATOM 2918 C CB . ASN B 2 126 ? 22.548 56.315 -2.140 1.00 69.62 ? 1662 ASN B CB 1 ATOM 2919 C CG . ASN B 2 126 ? 22.440 55.316 -3.286 1.00 78.05 ? 1662 ASN B CG 1 ATOM 2920 O OD1 . ASN B 2 126 ? 23.254 54.400 -3.401 1.00 79.09 ? 1662 ASN B OD1 1 ATOM 2921 N ND2 . ASN B 2 126 ? 21.461 55.518 -4.167 1.00 87.03 ? 1662 ASN B ND2 1 ATOM 2922 N N . LYS B 2 127 ? 25.270 56.450 0.188 1.00 65.71 ? 1663 LYS B N 1 ATOM 2923 C CA . LYS B 2 127 ? 26.724 56.682 0.220 1.00 67.21 ? 1663 LYS B CA 1 ATOM 2924 C C . LYS B 2 127 ? 27.485 55.869 1.277 1.00 67.05 ? 1663 LYS B C 1 ATOM 2925 O O . LYS B 2 127 ? 27.014 55.670 2.391 1.00 67.94 ? 1663 LYS B O 1 ATOM 2926 C CB . LYS B 2 127 ? 27.033 58.182 0.385 1.00 69.04 ? 1663 LYS B CB 1 ATOM 2927 C CG . LYS B 2 127 ? 26.531 59.043 -0.794 1.00 70.95 ? 1663 LYS B CG 1 ATOM 2928 C CD . LYS B 2 127 ? 27.290 60.363 -0.947 1.00 70.07 ? 1663 LYS B CD 1 ATOM 2929 C CE . LYS B 2 127 ? 28.718 60.123 -1.412 1.00 71.38 ? 1663 LYS B CE 1 ATOM 2930 N NZ . LYS B 2 127 ? 29.527 61.369 -1.501 1.00 72.33 ? 1663 LYS B NZ 1 ATOM 2931 N N . THR B 2 128 ? 28.679 55.417 0.904 1.00 66.49 ? 1664 THR B N 1 ATOM 2932 C CA . THR B 2 128 ? 29.539 54.590 1.751 1.00 63.48 ? 1664 THR B CA 1 ATOM 2933 C C . THR B 2 128 ? 30.524 55.391 2.611 1.00 62.70 ? 1664 THR B C 1 ATOM 2934 O O . THR B 2 128 ? 30.615 56.607 2.498 1.00 62.42 ? 1664 THR B O 1 ATOM 2935 C CB . THR B 2 128 ? 30.339 53.602 0.863 1.00 63.78 ? 1664 THR B CB 1 ATOM 2936 O OG1 . THR B 2 128 ? 29.492 53.112 -0.190 1.00 61.32 ? 1664 THR B OG1 1 ATOM 2937 C CG2 . THR B 2 128 ? 30.841 52.419 1.679 1.00 64.55 ? 1664 THR B CG2 1 ATOM 2938 N N . TYR B 2 129 ? 31.248 54.685 3.476 1.00 63.02 ? 1665 TYR B N 1 ATOM 2939 C CA . TYR B 2 129 ? 32.251 55.267 4.368 1.00 62.80 ? 1665 TYR B CA 1 ATOM 2940 C C . TYR B 2 129 ? 32.818 54.222 5.339 1.00 62.20 ? 1665 TYR B C 1 ATOM 2941 O O . TYR B 2 129 ? 32.088 53.629 6.121 1.00 62.02 ? 1665 TYR B O 1 ATOM 2942 C CB . TYR B 2 129 ? 31.678 56.432 5.173 1.00 64.81 ? 1665 TYR B CB 1 ATOM 2943 C CG . TYR B 2 129 ? 32.726 57.108 6.039 1.00 68.92 ? 1665 TYR B CG 1 ATOM 2944 C CD1 . TYR B 2 129 ? 33.113 56.560 7.266 1.00 67.54 ? 1665 TYR B CD1 1 ATOM 2945 C CD2 . TYR B 2 129 ? 33.388 58.256 5.592 1.00 70.07 ? 1665 TYR B CD2 1 ATOM 2946 C CE1 . TYR B 2 129 ? 34.134 57.135 8.018 1.00 69.89 ? 1665 TYR B CE1 1 ATOM 2947 C CE2 . TYR B 2 129 ? 34.409 58.837 6.335 1.00 70.43 ? 1665 TYR B CE2 1 ATOM 2948 C CZ . TYR B 2 129 ? 34.780 58.273 7.542 1.00 70.49 ? 1665 TYR B CZ 1 ATOM 2949 O OH . TYR B 2 129 ? 35.813 58.834 8.254 1.00 69.30 ? 1665 TYR B OH 1 ATOM 2950 N N . THR B 2 130 ? 34.134 54.034 5.292 1.00 61.82 ? 1666 THR B N 1 ATOM 2951 C CA . THR B 2 130 ? 34.842 53.066 6.122 1.00 59.31 ? 1666 THR B CA 1 ATOM 2952 C C . THR B 2 130 ? 35.322 53.597 7.475 1.00 58.04 ? 1666 THR B C 1 ATOM 2953 O O . THR B 2 130 ? 35.989 54.629 7.556 1.00 58.22 ? 1666 THR B O 1 ATOM 2954 C CB . THR B 2 130 ? 36.072 52.540 5.378 1.00 60.69 ? 1666 THR B CB 1 ATOM 2955 O OG1 . THR B 2 130 ? 35.686 52.104 4.071 1.00 62.40 ? 1666 THR B OG1 1 ATOM 2956 C CG2 . THR B 2 130 ? 36.708 51.382 6.141 1.00 61.23 ? 1666 THR B CG2 1 ATOM 2957 N N . TYR B 2 131 ? 34.991 52.882 8.540 1.00 54.73 ? 1667 TYR B N 1 ATOM 2958 C CA . TYR B 2 131 ? 35.425 53.284 9.866 1.00 52.21 ? 1667 TYR B CA 1 ATOM 2959 C C . TYR B 2 131 ? 36.647 52.436 10.148 1.00 51.73 ? 1667 TYR B C 1 ATOM 2960 O O . TYR B 2 131 ? 36.906 51.493 9.424 1.00 53.58 ? 1667 TYR B O 1 ATOM 2961 C CB . TYR B 2 131 ? 34.333 52.994 10.903 1.00 50.27 ? 1667 TYR B CB 1 ATOM 2962 C CG . TYR B 2 131 ? 33.144 53.924 10.836 1.00 48.39 ? 1667 TYR B CG 1 ATOM 2963 C CD1 . TYR B 2 131 ? 33.015 54.990 11.723 1.00 49.70 ? 1667 TYR B CD1 1 ATOM 2964 C CD2 . TYR B 2 131 ? 32.164 53.762 9.864 1.00 49.91 ? 1667 TYR B CD2 1 ATOM 2965 C CE1 . TYR B 2 131 ? 31.935 55.877 11.640 1.00 49.63 ? 1667 TYR B CE1 1 ATOM 2966 C CE2 . TYR B 2 131 ? 31.082 54.644 9.771 1.00 50.41 ? 1667 TYR B CE2 1 ATOM 2967 C CZ . TYR B 2 131 ? 30.978 55.696 10.657 1.00 49.03 ? 1667 TYR B CZ 1 ATOM 2968 O OH . TYR B 2 131 ? 29.931 56.573 10.537 1.00 50.71 ? 1667 TYR B OH 1 ATOM 2969 N N . VAL B 2 132 ? 37.403 52.775 11.182 1.00 51.95 ? 1668 VAL B N 1 ATOM 2970 C CA . VAL B 2 132 ? 38.585 52.013 11.556 1.00 52.97 ? 1668 VAL B CA 1 ATOM 2971 C C . VAL B 2 132 ? 38.778 52.140 13.065 1.00 56.53 ? 1668 VAL B C 1 ATOM 2972 O O . VAL B 2 132 ? 39.166 53.195 13.566 1.00 57.52 ? 1668 VAL B O 1 ATOM 2973 C CB . VAL B 2 132 ? 39.851 52.525 10.826 1.00 51.37 ? 1668 VAL B CB 1 ATOM 2974 C CG1 . VAL B 2 132 ? 41.107 51.890 11.436 1.00 49.72 ? 1668 VAL B CG1 1 ATOM 2975 C CG2 . VAL B 2 132 ? 39.770 52.185 9.341 1.00 49.94 ? 1668 VAL B CG2 1 ATOM 2976 N N . TRP B 2 133 ? 38.498 51.058 13.784 1.00 59.25 ? 1669 TRP B N 1 ATOM 2977 C CA . TRP B 2 133 ? 38.618 51.048 15.231 1.00 62.86 ? 1669 TRP B CA 1 ATOM 2978 C C . TRP B 2 133 ? 39.732 50.125 15.667 1.00 64.93 ? 1669 TRP B C 1 ATOM 2979 O O . TRP B 2 133 ? 39.894 49.036 15.117 1.00 65.24 ? 1669 TRP B O 1 ATOM 2980 C CB . TRP B 2 133 ? 37.297 50.603 15.867 1.00 64.21 ? 1669 TRP B CB 1 ATOM 2981 C CG . TRP B 2 133 ? 36.102 51.353 15.334 1.00 66.11 ? 1669 TRP B CG 1 ATOM 2982 C CD1 . TRP B 2 133 ? 36.030 52.685 15.073 1.00 66.52 ? 1669 TRP B CD1 1 ATOM 2983 C CD2 . TRP B 2 133 ? 34.806 50.816 15.029 1.00 67.13 ? 1669 TRP B CD2 1 ATOM 2984 N NE1 . TRP B 2 133 ? 34.776 53.016 14.625 1.00 67.83 ? 1669 TRP B NE1 1 ATOM 2985 C CE2 . TRP B 2 133 ? 34.003 51.889 14.588 1.00 67.18 ? 1669 TRP B CE2 1 ATOM 2986 C CE3 . TRP B 2 133 ? 34.245 49.534 15.089 1.00 66.61 ? 1669 TRP B CE3 1 ATOM 2987 C CZ2 . TRP B 2 133 ? 32.668 51.723 14.208 1.00 68.19 ? 1669 TRP B CZ2 1 ATOM 2988 C CZ3 . TRP B 2 133 ? 32.913 49.370 14.711 1.00 67.18 ? 1669 TRP B CZ3 1 ATOM 2989 C CH2 . TRP B 2 133 ? 32.142 50.459 14.277 1.00 66.91 ? 1669 TRP B CH2 1 ATOM 2990 N N . HIS B 2 134 ? 40.489 50.574 16.665 1.00 67.15 ? 1670 HIS B N 1 ATOM 2991 C CA . HIS B 2 134 ? 41.612 49.824 17.210 1.00 68.67 ? 1670 HIS B CA 1 ATOM 2992 C C . HIS B 2 134 ? 41.235 49.309 18.602 1.00 68.07 ? 1670 HIS B C 1 ATOM 2993 O O . HIS B 2 134 ? 41.300 50.045 19.578 1.00 69.16 ? 1670 HIS B O 1 ATOM 2994 C CB . HIS B 2 134 ? 42.843 50.742 17.289 1.00 73.40 ? 1670 HIS B CB 1 ATOM 2995 C CG . HIS B 2 134 ? 44.133 50.062 16.939 1.00 81.11 ? 1670 HIS B CG 1 ATOM 2996 N ND1 . HIS B 2 134 ? 44.714 49.099 17.741 1.00 83.50 ? 1670 HIS B ND1 1 ATOM 2997 C CD2 . HIS B 2 134 ? 44.942 50.190 15.859 1.00 82.73 ? 1670 HIS B CD2 1 ATOM 2998 C CE1 . HIS B 2 134 ? 45.823 48.662 17.167 1.00 83.90 ? 1670 HIS B CE1 1 ATOM 2999 N NE2 . HIS B 2 134 ? 45.985 49.307 16.024 1.00 84.41 ? 1670 HIS B NE2 1 ATOM 3000 N N . ALA B 2 135 ? 40.839 48.043 18.687 1.00 67.15 ? 1671 ALA B N 1 ATOM 3001 C CA . ALA B 2 135 ? 40.440 47.436 19.953 1.00 66.41 ? 1671 ALA B CA 1 ATOM 3002 C C . ALA B 2 135 ? 41.543 47.444 21.022 1.00 67.96 ? 1671 ALA B C 1 ATOM 3003 O O . ALA B 2 135 ? 42.277 46.464 21.174 1.00 68.02 ? 1671 ALA B O 1 ATOM 3004 C CB . ALA B 2 135 ? 39.978 46.021 19.700 1.00 65.43 ? 1671 ALA B CB 1 ATOM 3005 N N . THR B 2 136 ? 41.639 48.543 21.771 1.00 68.37 ? 1672 THR B N 1 ATOM 3006 C CA . THR B 2 136 ? 42.644 48.701 22.827 1.00 69.03 ? 1672 THR B CA 1 ATOM 3007 C C . THR B 2 136 ? 42.375 47.807 24.035 1.00 70.18 ? 1672 THR B C 1 ATOM 3008 O O . THR B 2 136 ? 41.306 47.220 24.166 1.00 70.09 ? 1672 THR B O 1 ATOM 3009 C CB . THR B 2 136 ? 42.685 50.147 23.362 1.00 68.73 ? 1672 THR B CB 1 ATOM 3010 O OG1 . THR B 2 136 ? 41.608 50.341 24.286 1.00 67.23 ? 1672 THR B OG1 1 ATOM 3011 C CG2 . THR B 2 136 ? 42.543 51.154 22.227 1.00 68.47 ? 1672 THR B CG2 1 ATOM 3012 N N . THR B 2 137 ? 43.352 47.726 24.929 1.00 72.84 ? 1673 THR B N 1 ATOM 3013 C CA . THR B 2 137 ? 43.218 46.929 26.139 1.00 74.89 ? 1673 THR B CA 1 ATOM 3014 C C . THR B 2 137 ? 42.076 47.462 27.003 1.00 75.89 ? 1673 THR B C 1 ATOM 3015 O O . THR B 2 137 ? 41.414 46.703 27.709 1.00 75.72 ? 1673 THR B O 1 ATOM 3016 C CB . THR B 2 137 ? 44.515 46.960 26.972 1.00 75.68 ? 1673 THR B CB 1 ATOM 3017 O OG1 . THR B 2 137 ? 45.549 46.242 26.282 1.00 77.83 ? 1673 THR B OG1 1 ATOM 3018 C CG2 . THR B 2 137 ? 44.283 46.337 28.342 1.00 74.80 ? 1673 THR B CG2 1 ATOM 3019 N N . ARG B 2 138 ? 41.855 48.771 26.946 1.00 77.72 ? 1674 ARG B N 1 ATOM 3020 C CA . ARG B 2 138 ? 40.790 49.407 27.722 1.00 80.25 ? 1674 ARG B CA 1 ATOM 3021 C C . ARG B 2 138 ? 39.410 48.852 27.363 1.00 79.86 ? 1674 ARG B C 1 ATOM 3022 O O . ARG B 2 138 ? 38.450 48.999 28.121 1.00 80.76 ? 1674 ARG B O 1 ATOM 3023 C CB . ARG B 2 138 ? 40.799 50.928 27.490 1.00 83.46 ? 1674 ARG B CB 1 ATOM 3024 C CG . ARG B 2 138 ? 41.800 51.712 28.343 1.00 86.75 ? 1674 ARG B CG 1 ATOM 3025 C CD . ARG B 2 138 ? 41.870 53.182 27.932 1.00 88.96 ? 1674 ARG B CD 1 ATOM 3026 N NE . ARG B 2 138 ? 42.602 53.368 26.678 1.00 91.24 ? 1674 ARG B NE 1 ATOM 3027 C CZ . ARG B 2 138 ? 42.692 54.524 26.025 1.00 91.83 ? 1674 ARG B CZ 1 ATOM 3028 N NH1 . ARG B 2 138 ? 42.093 55.609 26.501 1.00 92.04 ? 1674 ARG B NH1 1 ATOM 3029 N NH2 . ARG B 2 138 ? 43.384 54.598 24.895 1.00 91.43 ? 1674 ARG B NH2 1 ATOM 3030 N N . SER B 2 139 ? 39.316 48.214 26.205 1.00 78.61 ? 1675 SER B N 1 ATOM 3031 C CA . SER B 2 139 ? 38.055 47.658 25.743 1.00 76.29 ? 1675 SER B CA 1 ATOM 3032 C C . SER B 2 139 ? 37.896 46.194 26.137 1.00 75.01 ? 1675 SER B C 1 ATOM 3033 O O . SER B 2 139 ? 36.786 45.723 26.382 1.00 73.58 ? 1675 SER B O 1 ATOM 3034 C CB . SER B 2 139 ? 37.970 47.807 24.227 1.00 76.24 ? 1675 SER B CB 1 ATOM 3035 O OG . SER B 2 139 ? 38.233 49.148 23.848 1.00 76.05 ? 1675 SER B OG 1 ATOM 3036 N N . GLY B 2 140 ? 39.013 45.481 26.202 1.00 74.54 ? 1676 GLY B N 1 ATOM 3037 C CA . GLY B 2 140 ? 38.978 44.075 26.556 1.00 76.63 ? 1676 GLY B CA 1 ATOM 3038 C C . GLY B 2 140 ? 38.350 43.767 27.904 1.00 77.01 ? 1676 GLY B C 1 ATOM 3039 O O . GLY B 2 140 ? 37.900 44.675 28.601 1.00 78.17 ? 1676 GLY B O 1 ATOM 3040 N N . PRO B 2 141 ? 38.296 42.482 28.292 1.00 77.05 ? 1677 PRO B N 1 ATOM 3041 C CA . PRO B 2 141 ? 37.725 42.020 29.558 1.00 79.08 ? 1677 PRO B CA 1 ATOM 3042 C C . PRO B 2 141 ? 38.714 42.207 30.698 1.00 81.60 ? 1677 PRO B C 1 ATOM 3043 O O . PRO B 2 141 ? 39.676 42.967 30.578 1.00 80.71 ? 1677 PRO B O 1 ATOM 3044 C CB . PRO B 2 141 ? 37.462 40.536 29.305 1.00 78.72 ? 1677 PRO B CB 1 ATOM 3045 C CG . PRO B 2 141 ? 37.487 40.403 27.812 1.00 77.72 ? 1677 PRO B CG 1 ATOM 3046 C CD . PRO B 2 141 ? 38.577 41.334 27.421 1.00 76.69 ? 1677 PRO B CD 1 ATOM 3047 N N . GLU B 2 142 ? 38.470 41.501 31.800 1.00 84.82 ? 1678 GLU B N 1 ATOM 3048 C CA . GLU B 2 142 ? 39.351 41.564 32.956 1.00 88.26 ? 1678 GLU B CA 1 ATOM 3049 C C . GLU B 2 142 ? 40.267 40.352 33.018 1.00 90.40 ? 1678 GLU B C 1 ATOM 3050 O O . GLU B 2 142 ? 39.926 39.269 32.541 1.00 90.18 ? 1678 GLU B O 1 ATOM 3051 C CB . GLU B 2 142 ? 38.549 41.685 34.253 1.00 89.04 ? 1678 GLU B CB 1 ATOM 3052 C CG . GLU B 2 142 ? 38.050 43.101 34.519 1.00 91.22 ? 1678 GLU B CG 1 ATOM 3053 C CD . GLU B 2 142 ? 39.150 44.150 34.361 1.00 92.13 ? 1678 GLU B CD 1 ATOM 3054 O OE1 . GLU B 2 142 ? 40.167 44.078 35.086 1.00 92.55 ? 1678 GLU B OE1 1 ATOM 3055 O OE2 . GLU B 2 142 ? 39.000 45.051 33.505 1.00 93.23 ? 1678 GLU B OE2 1 ATOM 3056 N N . ASN B 2 143 ? 41.438 40.564 33.611 1.00 93.51 ? 1679 ASN B N 1 ATOM 3057 C CA . ASN B 2 143 ? 42.476 39.546 33.750 1.00 96.43 ? 1679 ASN B CA 1 ATOM 3058 C C . ASN B 2 143 ? 41.991 38.184 34.245 1.00 97.16 ? 1679 ASN B C 1 ATOM 3059 O O . ASN B 2 143 ? 42.504 37.143 33.817 1.00 98.25 ? 1679 ASN B O 1 ATOM 3060 C CB . ASN B 2 143 ? 43.572 40.059 34.689 1.00 98.69 ? 1679 ASN B CB 1 ATOM 3061 C CG . ASN B 2 143 ? 44.029 41.472 34.341 1.00 101.02 ? 1679 ASN B CG 1 ATOM 3062 O OD1 . ASN B 2 143 ? 43.219 42.404 34.274 1.00 101.39 ? 1679 ASN B OD1 1 ATOM 3063 N ND2 . ASN B 2 143 ? 45.334 41.637 34.128 1.00 101.05 ? 1679 ASN B ND2 1 ATOM 3064 N N . PRO B 2 144 ? 41.010 38.170 35.164 1.00 96.68 ? 1680 PRO B N 1 ATOM 3065 C CA . PRO B 2 144 ? 40.507 36.894 35.680 1.00 96.04 ? 1680 PRO B CA 1 ATOM 3066 C C . PRO B 2 144 ? 39.498 36.125 34.820 1.00 95.16 ? 1680 PRO B C 1 ATOM 3067 O O . PRO B 2 144 ? 39.870 35.171 34.133 1.00 95.99 ? 1680 PRO B O 1 ATOM 3068 C CB . PRO B 2 144 ? 39.924 37.277 37.039 1.00 96.19 ? 1680 PRO B CB 1 ATOM 3069 C CG . PRO B 2 144 ? 40.703 38.493 37.412 1.00 96.39 ? 1680 PRO B CG 1 ATOM 3070 C CD . PRO B 2 144 ? 40.711 39.247 36.118 1.00 96.65 ? 1680 PRO B CD 1 ATOM 3071 N N . GLY B 2 145 ? 38.231 36.537 34.845 1.00 92.64 ? 1681 GLY B N 1 ATOM 3072 C CA . GLY B 2 145 ? 37.216 35.802 34.101 1.00 88.37 ? 1681 GLY B CA 1 ATOM 3073 C C . GLY B 2 145 ? 36.566 36.343 32.838 1.00 85.43 ? 1681 GLY B C 1 ATOM 3074 O O . GLY B 2 145 ? 36.832 37.465 32.398 1.00 85.01 ? 1681 GLY B O 1 ATOM 3075 N N . SER B 2 146 ? 35.685 35.513 32.280 1.00 82.18 ? 1682 SER B N 1 ATOM 3076 C CA . SER B 2 146 ? 34.947 35.803 31.056 1.00 79.27 ? 1682 SER B CA 1 ATOM 3077 C C . SER B 2 146 ? 35.930 36.239 29.986 1.00 76.55 ? 1682 SER B C 1 ATOM 3078 O O . SER B 2 146 ? 36.479 37.336 30.034 1.00 76.86 ? 1682 SER B O 1 ATOM 3079 C CB . SER B 2 146 ? 33.888 36.885 31.292 1.00 80.08 ? 1682 SER B CB 1 ATOM 3080 O OG . SER B 2 146 ? 34.476 38.165 31.440 1.00 84.94 ? 1682 SER B OG 1 ATOM 3081 N N . ALA B 2 147 ? 36.149 35.360 29.017 1.00 73.87 ? 1683 ALA B N 1 ATOM 3082 C CA . ALA B 2 147 ? 37.086 35.616 27.935 1.00 71.16 ? 1683 ALA B CA 1 ATOM 3083 C C . ALA B 2 147 ? 36.699 36.780 27.036 1.00 70.11 ? 1683 ALA B C 1 ATOM 3084 O O . ALA B 2 147 ? 37.544 37.315 26.313 1.00 69.45 ? 1683 ALA B O 1 ATOM 3085 C CB . ALA B 2 147 ? 37.251 34.360 27.099 1.00 70.29 ? 1683 ALA B CB 1 ATOM 3086 N N . CYS B 2 148 ? 35.433 37.182 27.077 1.00 68.59 ? 1684 CYS B N 1 ATOM 3087 C CA . CYS B 2 148 ? 34.991 38.265 26.215 1.00 68.05 ? 1684 CYS B CA 1 ATOM 3088 C C . CYS B 2 148 ? 34.057 39.274 26.906 1.00 65.82 ? 1684 CYS B C 1 ATOM 3089 O O . CYS B 2 148 ? 33.249 38.900 27.748 1.00 68.01 ? 1684 CYS B O 1 ATOM 3090 C CB . CYS B 2 148 ? 34.337 37.664 24.954 1.00 67.79 ? 1684 CYS B CB 1 ATOM 3091 S SG . CYS B 2 148 ? 34.638 38.699 23.482 1.00 75.42 ? 1684 CYS B SG 1 ATOM 3092 N N . ARG B 2 149 ? 34.184 40.551 26.545 1.00 63.02 ? 1685 ARG B N 1 ATOM 3093 C CA . ARG B 2 149 ? 33.376 41.637 27.120 1.00 59.87 ? 1685 ARG B CA 1 ATOM 3094 C C . ARG B 2 149 ? 32.434 42.280 26.102 1.00 54.54 ? 1685 ARG B C 1 ATOM 3095 O O . ARG B 2 149 ? 32.777 42.428 24.933 1.00 53.98 ? 1685 ARG B O 1 ATOM 3096 C CB . ARG B 2 149 ? 34.294 42.723 27.698 1.00 65.08 ? 1685 ARG B CB 1 ATOM 3097 C CG . ARG B 2 149 ? 33.591 44.049 28.003 1.00 70.19 ? 1685 ARG B CG 1 ATOM 3098 C CD . ARG B 2 149 ? 32.466 43.820 29.007 1.00 76.02 ? 1685 ARG B CD 1 ATOM 3099 N NE . ARG B 2 149 ? 31.864 45.053 29.506 1.00 78.33 ? 1685 ARG B NE 1 ATOM 3100 C CZ . ARG B 2 149 ? 31.090 45.103 30.585 1.00 79.74 ? 1685 ARG B CZ 1 ATOM 3101 N NH1 . ARG B 2 149 ? 30.835 43.987 31.259 1.00 79.45 ? 1685 ARG B NH1 1 ATOM 3102 N NH2 . ARG B 2 149 ? 30.587 46.263 30.995 1.00 79.69 ? 1685 ARG B NH2 1 ATOM 3103 N N . ALA B 2 150 ? 31.264 42.701 26.561 1.00 50.10 ? 1686 ALA B N 1 ATOM 3104 C CA . ALA B 2 150 ? 30.272 43.296 25.678 1.00 48.42 ? 1686 ALA B CA 1 ATOM 3105 C C . ALA B 2 150 ? 30.195 44.808 25.652 1.00 48.80 ? 1686 ALA B C 1 ATOM 3106 O O . ALA B 2 150 ? 30.328 45.470 26.683 1.00 49.48 ? 1686 ALA B O 1 ATOM 3107 C CB . ALA B 2 150 ? 28.912 42.755 26.014 1.00 49.69 ? 1686 ALA B CB 1 ATOM 3108 N N . TRP B 2 151 ? 29.977 45.336 24.449 1.00 47.74 ? 1687 TRP B N 1 ATOM 3109 C CA . TRP B 2 151 ? 29.813 46.766 24.193 1.00 45.58 ? 1687 TRP B CA 1 ATOM 3110 C C . TRP B 2 151 ? 28.768 46.797 23.110 1.00 42.70 ? 1687 TRP B C 1 ATOM 3111 O O . TRP B 2 151 ? 28.190 45.766 22.796 1.00 42.02 ? 1687 TRP B O 1 ATOM 3112 C CB . TRP B 2 151 ? 31.085 47.420 23.672 1.00 48.63 ? 1687 TRP B CB 1 ATOM 3113 C CG . TRP B 2 151 ? 32.255 47.256 24.569 1.00 51.85 ? 1687 TRP B CG 1 ATOM 3114 C CD1 . TRP B 2 151 ? 33.183 46.259 24.529 1.00 52.72 ? 1687 TRP B CD1 1 ATOM 3115 C CD2 . TRP B 2 151 ? 32.626 48.107 25.648 1.00 52.67 ? 1687 TRP B CD2 1 ATOM 3116 N NE1 . TRP B 2 151 ? 34.115 46.439 25.516 1.00 55.08 ? 1687 TRP B NE1 1 ATOM 3117 C CE2 . TRP B 2 151 ? 33.794 47.568 26.223 1.00 53.97 ? 1687 TRP B CE2 1 ATOM 3118 C CE3 . TRP B 2 151 ? 32.080 49.276 26.193 1.00 55.72 ? 1687 TRP B CE3 1 ATOM 3119 C CZ2 . TRP B 2 151 ? 34.432 48.155 27.318 1.00 54.20 ? 1687 TRP B CZ2 1 ATOM 3120 C CZ3 . TRP B 2 151 ? 32.711 49.862 27.283 1.00 55.38 ? 1687 TRP B CZ3 1 ATOM 3121 C CH2 . TRP B 2 151 ? 33.877 49.298 27.833 1.00 57.06 ? 1687 TRP B CH2 1 ATOM 3122 N N . ALA B 2 152 ? 28.533 47.956 22.516 1.00 41.35 ? 1688 ALA B N 1 ATOM 3123 C CA . ALA B 2 152 ? 27.504 48.047 21.488 1.00 41.08 ? 1688 ALA B CA 1 ATOM 3124 C C . ALA B 2 152 ? 27.782 49.148 20.488 1.00 42.25 ? 1688 ALA B C 1 ATOM 3125 O O . ALA B 2 152 ? 28.415 50.140 20.818 1.00 43.93 ? 1688 ALA B O 1 ATOM 3126 C CB . ALA B 2 152 ? 26.147 48.285 22.145 1.00 38.29 ? 1688 ALA B CB 1 ATOM 3127 N N . TYR B 2 153 ? 27.322 48.956 19.259 1.00 42.82 ? 1689 TYR B N 1 ATOM 3128 C CA . TYR B 2 153 ? 27.487 49.963 18.225 1.00 44.25 ? 1689 TYR B CA 1 ATOM 3129 C C . TYR B 2 153 ? 26.080 50.355 17.782 1.00 46.79 ? 1689 TYR B C 1 ATOM 3130 O O . TYR B 2 153 ? 25.140 49.581 17.945 1.00 46.29 ? 1689 TYR B O 1 ATOM 3131 C CB . TYR B 2 153 ? 28.347 49.438 17.057 1.00 41.49 ? 1689 TYR B CB 1 ATOM 3132 C CG . TYR B 2 153 ? 27.752 48.356 16.184 1.00 41.09 ? 1689 TYR B CG 1 ATOM 3133 C CD1 . TYR B 2 153 ? 26.940 48.668 15.104 1.00 40.37 ? 1689 TYR B CD1 1 ATOM 3134 C CD2 . TYR B 2 153 ? 28.021 47.015 16.428 1.00 41.93 ? 1689 TYR B CD2 1 ATOM 3135 C CE1 . TYR B 2 153 ? 26.418 47.666 14.288 1.00 38.66 ? 1689 TYR B CE1 1 ATOM 3136 C CE2 . TYR B 2 153 ? 27.499 46.015 15.620 1.00 38.84 ? 1689 TYR B CE2 1 ATOM 3137 C CZ . TYR B 2 153 ? 26.705 46.343 14.553 1.00 38.01 ? 1689 TYR B CZ 1 ATOM 3138 O OH . TYR B 2 153 ? 26.230 45.338 13.728 1.00 39.13 ? 1689 TYR B OH 1 ATOM 3139 N N . TYR B 2 154 ? 25.929 51.570 17.259 1.00 48.98 ? 1690 TYR B N 1 ATOM 3140 C CA . TYR B 2 154 ? 24.623 52.071 16.839 1.00 48.89 ? 1690 TYR B CA 1 ATOM 3141 C C . TYR B 2 154 ? 24.834 53.359 16.077 1.00 48.45 ? 1690 TYR B C 1 ATOM 3142 O O . TYR B 2 154 ? 25.935 53.891 16.086 1.00 45.74 ? 1690 TYR B O 1 ATOM 3143 C CB . TYR B 2 154 ? 23.763 52.352 18.068 1.00 50.64 ? 1690 TYR B CB 1 ATOM 3144 C CG . TYR B 2 154 ? 24.518 53.061 19.164 1.00 51.05 ? 1690 TYR B CG 1 ATOM 3145 C CD1 . TYR B 2 154 ? 25.343 52.356 20.034 1.00 53.95 ? 1690 TYR B CD1 1 ATOM 3146 C CD2 . TYR B 2 154 ? 24.442 54.440 19.306 1.00 54.30 ? 1690 TYR B CD2 1 ATOM 3147 C CE1 . TYR B 2 154 ? 26.077 53.008 21.025 1.00 56.97 ? 1690 TYR B CE1 1 ATOM 3148 C CE2 . TYR B 2 154 ? 25.171 55.109 20.289 1.00 57.34 ? 1690 TYR B CE2 1 ATOM 3149 C CZ . TYR B 2 154 ? 25.988 54.387 21.149 1.00 58.18 ? 1690 TYR B CZ 1 ATOM 3150 O OH . TYR B 2 154 ? 26.699 55.039 22.137 1.00 58.48 ? 1690 TYR B OH 1 ATOM 3151 N N . SER B 2 155 ? 23.794 53.852 15.409 1.00 50.12 ? 1691 SER B N 1 ATOM 3152 C CA . SER B 2 155 ? 23.921 55.103 14.670 1.00 53.57 ? 1691 SER B CA 1 ATOM 3153 C C . SER B 2 155 ? 23.995 56.180 15.726 1.00 54.98 ? 1691 SER B C 1 ATOM 3154 O O . SER B 2 155 ? 23.442 56.024 16.810 1.00 54.36 ? 1691 SER B O 1 ATOM 3155 C CB . SER B 2 155 ? 22.717 55.340 13.756 1.00 56.03 ? 1691 SER B CB 1 ATOM 3156 O OG . SER B 2 155 ? 22.926 56.458 12.904 1.00 55.68 ? 1691 SER B OG 1 ATOM 3157 N N . ALA B 2 156 ? 24.685 57.271 15.428 1.00 58.29 ? 1692 ALA B N 1 ATOM 3158 C CA . ALA B 2 156 ? 24.831 58.328 16.420 1.00 60.44 ? 1692 ALA B CA 1 ATOM 3159 C C . ALA B 2 156 ? 24.353 59.709 15.970 1.00 62.09 ? 1692 ALA B C 1 ATOM 3160 O O . ALA B 2 156 ? 24.305 60.636 16.777 1.00 64.33 ? 1692 ALA B O 1 ATOM 3161 C CB . ALA B 2 156 ? 26.281 58.391 16.891 1.00 59.60 ? 1692 ALA B CB 1 ATOM 3162 N N . VAL B 2 157 ? 24.001 59.855 14.693 1.00 62.13 ? 1693 VAL B N 1 ATOM 3163 C CA . VAL B 2 157 ? 23.499 61.131 14.199 1.00 61.36 ? 1693 VAL B CA 1 ATOM 3164 C C . VAL B 2 157 ? 22.513 61.685 15.234 1.00 62.72 ? 1693 VAL B C 1 ATOM 3165 O O . VAL B 2 157 ? 22.579 62.856 15.606 1.00 64.83 ? 1693 VAL B O 1 ATOM 3166 C CB . VAL B 2 157 ? 22.805 60.943 12.850 1.00 60.83 ? 1693 VAL B CB 1 ATOM 3167 C CG1 . VAL B 2 157 ? 21.977 62.167 12.502 1.00 60.60 ? 1693 VAL B CG1 1 ATOM 3168 C CG2 . VAL B 2 157 ? 23.853 60.683 11.782 1.00 61.47 ? 1693 VAL B CG2 1 ATOM 3169 N N . ASN B 2 158 ? 21.613 60.826 15.700 1.00 61.75 ? 1694 ASN B N 1 ATOM 3170 C CA . ASN B 2 158 ? 20.638 61.177 16.721 1.00 60.97 ? 1694 ASN B CA 1 ATOM 3171 C C . ASN B 2 158 ? 20.382 59.907 17.519 1.00 60.09 ? 1694 ASN B C 1 ATOM 3172 O O . ASN B 2 158 ? 19.328 59.275 17.392 1.00 61.05 ? 1694 ASN B O 1 ATOM 3173 C CB . ASN B 2 158 ? 19.323 61.676 16.107 1.00 63.90 ? 1694 ASN B CB 1 ATOM 3174 C CG . ASN B 2 158 ? 18.318 62.164 17.172 1.00 68.72 ? 1694 ASN B CG 1 ATOM 3175 O OD1 . ASN B 2 158 ? 17.336 62.838 16.852 1.00 70.72 ? 1694 ASN B OD1 1 ATOM 3176 N ND2 . ASN B 2 158 ? 18.568 61.822 18.439 1.00 70.55 ? 1694 ASN B ND2 1 ATOM 3177 N N . PRO B 2 159 ? 21.344 59.528 18.371 1.00 57.78 ? 1695 PRO B N 1 ATOM 3178 C CA . PRO B 2 159 ? 21.247 58.327 19.203 1.00 57.06 ? 1695 PRO B CA 1 ATOM 3179 C C . PRO B 2 159 ? 19.826 57.841 19.483 1.00 56.48 ? 1695 PRO B C 1 ATOM 3180 O O . PRO B 2 159 ? 19.352 56.906 18.848 1.00 58.08 ? 1695 PRO B O 1 ATOM 3181 C CB . PRO B 2 159 ? 21.998 58.734 20.466 1.00 56.10 ? 1695 PRO B CB 1 ATOM 3182 C CG . PRO B 2 159 ? 23.104 59.556 19.916 1.00 54.92 ? 1695 PRO B CG 1 ATOM 3183 C CD . PRO B 2 159 ? 22.409 60.418 18.871 1.00 56.91 ? 1695 PRO B CD 1 ATOM 3184 N N . GLU B 2 160 ? 19.141 58.489 20.413 1.00 57.27 ? 1696 GLU B N 1 ATOM 3185 C CA . GLU B 2 160 ? 17.790 58.081 20.782 1.00 59.09 ? 1696 GLU B CA 1 ATOM 3186 C C . GLU B 2 160 ? 16.838 57.803 19.615 1.00 57.26 ? 1696 GLU B C 1 ATOM 3187 O O . GLU B 2 160 ? 16.321 56.700 19.503 1.00 55.06 ? 1696 GLU B O 1 ATOM 3188 C CB . GLU B 2 160 ? 17.154 59.113 21.723 1.00 61.86 ? 1696 GLU B CB 1 ATOM 3189 C CG . GLU B 2 160 ? 16.476 58.474 22.935 1.00 66.92 ? 1696 GLU B CG 1 ATOM 3190 C CD . GLU B 2 160 ? 15.195 59.180 23.372 1.00 69.39 ? 1696 GLU B CD 1 ATOM 3191 O OE1 . GLU B 2 160 ? 14.694 58.858 24.478 1.00 70.58 ? 1696 GLU B OE1 1 ATOM 3192 O OE2 . GLU B 2 160 ? 14.686 60.040 22.612 1.00 69.91 ? 1696 GLU B OE2 1 ATOM 3193 N N . LYS B 2 161 ? 16.590 58.793 18.758 1.00 55.78 ? 1697 LYS B N 1 ATOM 3194 C CA . LYS B 2 161 ? 15.683 58.574 17.637 1.00 55.62 ? 1697 LYS B CA 1 ATOM 3195 C C . LYS B 2 161 ? 16.186 57.473 16.700 1.00 55.08 ? 1697 LYS B C 1 ATOM 3196 O O . LYS B 2 161 ? 15.417 56.861 15.957 1.00 53.15 ? 1697 LYS B O 1 ATOM 3197 C CB . LYS B 2 161 ? 15.469 59.865 16.839 1.00 57.03 ? 1697 LYS B CB 1 ATOM 3198 C CG . LYS B 2 161 ? 14.516 60.857 17.489 1.00 58.21 ? 1697 LYS B CG 1 ATOM 3199 C CD . LYS B 2 161 ? 13.878 61.782 16.461 1.00 57.33 ? 1697 LYS B CD 1 ATOM 3200 C CE . LYS B 2 161 ? 12.786 61.071 15.676 1.00 58.77 ? 1697 LYS B CE 1 ATOM 3201 N NZ . LYS B 2 161 ? 12.087 61.962 14.689 1.00 57.26 ? 1697 LYS B NZ 1 ATOM 3202 N N . ASP B 2 162 ? 17.482 57.212 16.742 1.00 52.44 ? 1698 ASP B N 1 ATOM 3203 C CA . ASP B 2 162 ? 18.039 56.192 15.888 1.00 49.01 ? 1698 ASP B CA 1 ATOM 3204 C C . ASP B 2 162 ? 17.982 54.795 16.495 1.00 46.85 ? 1698 ASP B C 1 ATOM 3205 O O . ASP B 2 162 ? 17.582 53.847 15.836 1.00 45.74 ? 1698 ASP B O 1 ATOM 3206 C CB . ASP B 2 162 ? 19.456 56.593 15.501 1.00 47.47 ? 1698 ASP B CB 1 ATOM 3207 C CG . ASP B 2 162 ? 19.465 57.712 14.484 1.00 45.72 ? 1698 ASP B CG 1 ATOM 3208 O OD1 . ASP B 2 162 ? 18.361 58.203 14.154 1.00 43.46 ? 1698 ASP B OD1 1 ATOM 3209 O OD2 . ASP B 2 162 ? 20.556 58.093 14.015 1.00 44.27 ? 1698 ASP B OD2 1 ATOM 3210 N N . ILE B 2 163 ? 18.367 54.653 17.750 1.00 44.67 ? 1699 ILE B N 1 ATOM 3211 C CA . ILE B 2 163 ? 18.300 53.340 18.355 1.00 44.98 ? 1699 ILE B CA 1 ATOM 3212 C C . ILE B 2 163 ? 16.848 52.886 18.305 1.00 45.42 ? 1699 ILE B C 1 ATOM 3213 O O . ILE B 2 163 ? 16.557 51.768 17.909 1.00 49.21 ? 1699 ILE B O 1 ATOM 3214 C CB . ILE B 2 163 ? 18.819 53.370 19.792 1.00 43.73 ? 1699 ILE B CB 1 ATOM 3215 C CG1 . ILE B 2 163 ? 20.298 53.772 19.776 1.00 43.65 ? 1699 ILE B CG1 1 ATOM 3216 C CG2 . ILE B 2 163 ? 18.656 52.001 20.441 1.00 46.62 ? 1699 ILE B CG2 1 ATOM 3217 C CD1 . ILE B 2 163 ? 20.951 53.821 21.135 1.00 43.37 ? 1699 ILE B CD1 1 ATOM 3218 N N . HIS B 2 164 ? 15.934 53.765 18.682 1.00 46.87 ? 1700 HIS B N 1 ATOM 3219 C CA . HIS B 2 164 ? 14.506 53.464 18.637 1.00 46.29 ? 1700 HIS B CA 1 ATOM 3220 C C . HIS B 2 164 ? 13.992 53.144 17.235 1.00 45.21 ? 1700 HIS B C 1 ATOM 3221 O O . HIS B 2 164 ? 12.886 52.637 17.066 1.00 44.52 ? 1700 HIS B O 1 ATOM 3222 C CB . HIS B 2 164 ? 13.708 54.636 19.209 1.00 45.71 ? 1700 HIS B CB 1 ATOM 3223 C CG . HIS B 2 164 ? 13.606 54.603 20.694 1.00 45.25 ? 1700 HIS B CG 1 ATOM 3224 N ND1 . HIS B 2 164 ? 12.744 53.758 21.355 1.00 48.48 ? 1700 HIS B ND1 1 ATOM 3225 C CD2 . HIS B 2 164 ? 14.334 55.222 21.650 1.00 46.59 ? 1700 HIS B CD2 1 ATOM 3226 C CE1 . HIS B 2 164 ? 12.948 53.851 22.655 1.00 47.93 ? 1700 HIS B CE1 1 ATOM 3227 N NE2 . HIS B 2 164 ? 13.908 54.733 22.861 1.00 48.89 ? 1700 HIS B NE2 1 ATOM 3228 N N . SER B 2 165 ? 14.783 53.456 16.223 1.00 44.14 ? 1701 SER B N 1 ATOM 3229 C CA . SER B 2 165 ? 14.362 53.155 14.869 1.00 44.08 ? 1701 SER B CA 1 ATOM 3230 C C . SER B 2 165 ? 14.811 51.749 14.493 1.00 42.10 ? 1701 SER B C 1 ATOM 3231 O O . SER B 2 165 ? 14.267 51.144 13.577 1.00 41.41 ? 1701 SER B O 1 ATOM 3232 C CB . SER B 2 165 ? 14.949 54.177 13.909 1.00 45.06 ? 1701 SER B CB 1 ATOM 3233 O OG . SER B 2 165 ? 14.599 55.480 14.337 1.00 47.95 ? 1701 SER B OG 1 ATOM 3234 N N . GLY B 2 166 ? 15.808 51.246 15.219 1.00 42.33 ? 1702 GLY B N 1 ATOM 3235 C CA . GLY B 2 166 ? 16.334 49.907 14.984 1.00 42.65 ? 1702 GLY B CA 1 ATOM 3236 C C . GLY B 2 166 ? 17.829 49.744 14.689 1.00 41.81 ? 1702 GLY B C 1 ATOM 3237 O O . GLY B 2 166 ? 18.296 48.620 14.467 1.00 41.14 ? 1702 GLY B O 1 ATOM 3238 N N . LEU B 2 167 ? 18.583 50.842 14.684 1.00 39.44 ? 1703 LEU B N 1 ATOM 3239 C CA . LEU B 2 167 ? 20.003 50.774 14.390 1.00 34.40 ? 1703 LEU B CA 1 ATOM 3240 C C . LEU B 2 167 ? 20.850 50.575 15.610 1.00 33.74 ? 1703 LEU B C 1 ATOM 3241 O O . LEU B 2 167 ? 21.346 51.534 16.180 1.00 38.36 ? 1703 LEU B O 1 ATOM 3242 C CB . LEU B 2 167 ? 20.463 52.028 13.654 1.00 33.43 ? 1703 LEU B CB 1 ATOM 3243 C CG . LEU B 2 167 ? 19.843 52.191 12.264 1.00 33.03 ? 1703 LEU B CG 1 ATOM 3244 C CD1 . LEU B 2 167 ? 20.566 53.291 11.487 1.00 31.12 ? 1703 LEU B CD1 1 ATOM 3245 C CD2 . LEU B 2 167 ? 19.954 50.889 11.513 1.00 33.11 ? 1703 LEU B CD2 1 ATOM 3246 N N . ILE B 2 168 ? 21.023 49.317 15.992 1.00 31.87 ? 1704 ILE B N 1 ATOM 3247 C CA . ILE B 2 168 ? 21.826 48.938 17.149 1.00 32.87 ? 1704 ILE B CA 1 ATOM 3248 C C . ILE B 2 168 ? 22.334 47.494 16.994 1.00 33.36 ? 1704 ILE B C 1 ATOM 3249 O O . ILE B 2 168 ? 21.634 46.635 16.475 1.00 34.48 ? 1704 ILE B O 1 ATOM 3250 C CB . ILE B 2 168 ? 21.013 49.027 18.456 1.00 32.06 ? 1704 ILE B CB 1 ATOM 3251 C CG1 . ILE B 2 168 ? 21.910 48.703 19.649 1.00 32.64 ? 1704 ILE B CG1 1 ATOM 3252 C CG2 . ILE B 2 168 ? 19.854 48.050 18.417 1.00 31.61 ? 1704 ILE B CG2 1 ATOM 3253 C CD1 . ILE B 2 168 ? 21.129 48.372 20.913 1.00 35.12 ? 1704 ILE B CD1 1 ATOM 3254 N N . GLY B 2 169 ? 23.549 47.229 17.452 1.00 31.83 ? 1705 GLY B N 1 ATOM 3255 C CA . GLY B 2 169 ? 24.077 45.892 17.322 1.00 33.14 ? 1705 GLY B CA 1 ATOM 3256 C C . GLY B 2 169 ? 25.066 45.592 18.420 1.00 32.68 ? 1705 GLY B C 1 ATOM 3257 O O . GLY B 2 169 ? 25.538 46.513 19.075 1.00 34.36 ? 1705 GLY B O 1 ATOM 3258 N N . PRO B 2 170 ? 25.394 44.314 18.656 1.00 30.47 ? 1706 PRO B N 1 ATOM 3259 C CA . PRO B 2 170 ? 26.346 43.931 19.700 1.00 33.00 ? 1706 PRO B CA 1 ATOM 3260 C C . PRO B 2 170 ? 27.787 44.004 19.195 1.00 36.05 ? 1706 PRO B C 1 ATOM 3261 O O . PRO B 2 170 ? 28.056 43.666 18.045 1.00 35.58 ? 1706 PRO B O 1 ATOM 3262 C CB . PRO B 2 170 ? 25.920 42.510 20.038 1.00 32.35 ? 1706 PRO B CB 1 ATOM 3263 C CG . PRO B 2 170 ? 25.475 42.001 18.742 1.00 30.05 ? 1706 PRO B CG 1 ATOM 3264 C CD . PRO B 2 170 ? 24.724 43.136 18.096 1.00 27.06 ? 1706 PRO B CD 1 ATOM 3265 N N . LEU B 2 171 ? 28.696 44.472 20.049 1.00 38.51 ? 1707 LEU B N 1 ATOM 3266 C CA . LEU B 2 171 ? 30.118 44.588 19.709 1.00 41.50 ? 1707 LEU B CA 1 ATOM 3267 C C . LEU B 2 171 ? 30.883 43.874 20.818 1.00 41.40 ? 1707 LEU B C 1 ATOM 3268 O O . LEU B 2 171 ? 30.853 44.310 21.957 1.00 43.29 ? 1707 LEU B O 1 ATOM 3269 C CB . LEU B 2 171 ? 30.543 46.057 19.668 1.00 43.22 ? 1707 LEU B CB 1 ATOM 3270 C CG . LEU B 2 171 ? 31.863 46.546 19.038 1.00 45.86 ? 1707 LEU B CG 1 ATOM 3271 C CD1 . LEU B 2 171 ? 32.307 47.780 19.832 1.00 46.46 ? 1707 LEU B CD1 1 ATOM 3272 C CD2 . LEU B 2 171 ? 32.965 45.495 19.074 1.00 44.30 ? 1707 LEU B CD2 1 ATOM 3273 N N . LEU B 2 172 ? 31.558 42.779 20.489 1.00 41.90 ? 1708 LEU B N 1 ATOM 3274 C CA . LEU B 2 172 ? 32.297 42.022 21.487 1.00 43.86 ? 1708 LEU B CA 1 ATOM 3275 C C . LEU B 2 172 ? 33.808 42.143 21.328 1.00 45.67 ? 1708 LEU B C 1 ATOM 3276 O O . LEU B 2 172 ? 34.334 42.144 20.207 1.00 44.93 ? 1708 LEU B O 1 ATOM 3277 C CB . LEU B 2 172 ? 31.894 40.550 21.424 1.00 44.81 ? 1708 LEU B CB 1 ATOM 3278 C CG . LEU B 2 172 ? 30.644 40.040 22.155 1.00 47.53 ? 1708 LEU B CG 1 ATOM 3279 C CD1 . LEU B 2 172 ? 29.793 41.183 22.705 1.00 48.09 ? 1708 LEU B CD1 1 ATOM 3280 C CD2 . LEU B 2 172 ? 29.849 39.188 21.182 1.00 46.55 ? 1708 LEU B CD2 1 ATOM 3281 N N . ILE B 2 173 ? 34.494 42.247 22.463 1.00 44.44 ? 1709 ILE B N 1 ATOM 3282 C CA . ILE B 2 173 ? 35.947 42.361 22.491 1.00 45.63 ? 1709 ILE B CA 1 ATOM 3283 C C . ILE B 2 173 ? 36.476 41.271 23.429 1.00 48.62 ? 1709 ILE B C 1 ATOM 3284 O O . ILE B 2 173 ? 36.208 41.288 24.634 1.00 47.19 ? 1709 ILE B O 1 ATOM 3285 C CB . ILE B 2 173 ? 36.395 43.739 23.013 1.00 42.39 ? 1709 ILE B CB 1 ATOM 3286 C CG1 . ILE B 2 173 ? 35.662 44.865 22.277 1.00 42.51 ? 1709 ILE B CG1 1 ATOM 3287 C CG2 . ILE B 2 173 ? 37.857 43.903 22.811 1.00 44.24 ? 1709 ILE B CG2 1 ATOM 3288 C CD1 . ILE B 2 173 ? 35.832 44.868 20.782 1.00 41.43 ? 1709 ILE B CD1 1 ATOM 3289 N N . CYS B 2 174 ? 37.210 40.318 22.855 1.00 51.85 ? 1710 CYS B N 1 ATOM 3290 C CA . CYS B 2 174 ? 37.772 39.181 23.582 1.00 53.46 ? 1710 CYS B CA 1 ATOM 3291 C C . CYS B 2 174 ? 39.274 39.314 23.756 1.00 52.63 ? 1710 CYS B C 1 ATOM 3292 O O . CYS B 2 174 ? 39.914 40.109 23.075 1.00 51.22 ? 1710 CYS B O 1 ATOM 3293 C CB . CYS B 2 174 ? 37.509 37.891 22.811 1.00 58.55 ? 1710 CYS B CB 1 ATOM 3294 S SG . CYS B 2 174 ? 35.809 37.614 22.226 1.00 66.36 ? 1710 CYS B SG 1 ATOM 3295 N N . ARG B 2 175 ? 39.843 38.519 24.653 1.00 53.30 ? 1711 ARG B N 1 ATOM 3296 C CA . ARG B 2 175 ? 41.282 38.577 24.852 1.00 57.20 ? 1711 ARG B CA 1 ATOM 3297 C C . ARG B 2 175 ? 41.926 37.613 23.880 1.00 58.41 ? 1711 ARG B C 1 ATOM 3298 O O . ARG B 2 175 ? 41.367 36.557 23.606 1.00 58.21 ? 1711 ARG B O 1 ATOM 3299 C CB . ARG B 2 175 ? 41.663 38.199 26.282 1.00 59.37 ? 1711 ARG B CB 1 ATOM 3300 C CG . ARG B 2 175 ? 41.392 36.762 26.668 1.00 59.24 ? 1711 ARG B CG 1 ATOM 3301 C CD . ARG B 2 175 ? 42.128 36.419 27.970 1.00 61.83 ? 1711 ARG B CD 1 ATOM 3302 N NE . ARG B 2 175 ? 41.271 35.794 28.979 1.00 62.70 ? 1711 ARG B NE 1 ATOM 3303 C CZ . ARG B 2 175 ? 40.714 36.435 30.005 1.00 62.84 ? 1711 ARG B CZ 1 ATOM 3304 N NH1 . ARG B 2 175 ? 40.918 37.739 30.181 1.00 59.31 ? 1711 ARG B NH1 1 ATOM 3305 N NH2 . ARG B 2 175 ? 39.949 35.763 30.859 1.00 62.18 ? 1711 ARG B NH2 1 ATOM 3306 N N . LYS B 2 176 ? 43.094 37.988 23.361 1.00 60.36 ? 1712 LYS B N 1 ATOM 3307 C CA . LYS B 2 176 ? 43.834 37.169 22.400 1.00 61.27 ? 1712 LYS B CA 1 ATOM 3308 C C . LYS B 2 176 ? 43.601 35.675 22.549 1.00 61.58 ? 1712 LYS B C 1 ATOM 3309 O O . LYS B 2 176 ? 43.609 35.146 23.662 1.00 61.71 ? 1712 LYS B O 1 ATOM 3310 C CB . LYS B 2 176 ? 45.336 37.426 22.516 1.00 63.04 ? 1712 LYS B CB 1 ATOM 3311 C CG . LYS B 2 176 ? 45.761 38.850 22.248 1.00 67.45 ? 1712 LYS B CG 1 ATOM 3312 C CD . LYS B 2 176 ? 47.273 38.944 22.104 1.00 70.26 ? 1712 LYS B CD 1 ATOM 3313 C CE . LYS B 2 176 ? 47.725 40.395 21.994 1.00 73.45 ? 1712 LYS B CE 1 ATOM 3314 N NZ . LYS B 2 176 ? 47.033 41.121 20.892 1.00 75.22 ? 1712 LYS B NZ 1 ATOM 3315 N N . GLY B 2 177 ? 43.399 35.004 21.417 1.00 61.95 ? 1713 GLY B N 1 ATOM 3316 C CA . GLY B 2 177 ? 43.194 33.564 21.416 1.00 62.01 ? 1713 GLY B CA 1 ATOM 3317 C C . GLY B 2 177 ? 41.803 33.044 21.739 1.00 61.95 ? 1713 GLY B C 1 ATOM 3318 O O . GLY B 2 177 ? 41.611 31.839 21.912 1.00 62.01 ? 1713 GLY B O 1 ATOM 3319 N N . THR B 2 178 ? 40.824 33.931 21.822 1.00 61.49 ? 1714 THR B N 1 ATOM 3320 C CA . THR B 2 178 ? 39.482 33.481 22.124 1.00 61.01 ? 1714 THR B CA 1 ATOM 3321 C C . THR B 2 178 ? 38.732 33.198 20.832 1.00 60.89 ? 1714 THR B C 1 ATOM 3322 O O . THR B 2 178 ? 37.888 32.307 20.790 1.00 60.34 ? 1714 THR B O 1 ATOM 3323 C CB . THR B 2 178 ? 38.707 34.524 22.960 1.00 61.64 ? 1714 THR B CB 1 ATOM 3324 O OG1 . THR B 2 178 ? 39.451 34.831 24.142 1.00 62.00 ? 1714 THR B OG1 1 ATOM 3325 C CG2 . THR B 2 178 ? 37.348 33.971 23.378 1.00 61.08 ? 1714 THR B CG2 1 ATOM 3326 N N . LEU B 2 179 ? 39.040 33.947 19.776 1.00 60.10 ? 1715 LEU B N 1 ATOM 3327 C CA . LEU B 2 179 ? 38.360 33.740 18.501 1.00 60.24 ? 1715 LEU B CA 1 ATOM 3328 C C . LEU B 2 179 ? 39.140 32.808 17.573 1.00 62.17 ? 1715 LEU B C 1 ATOM 3329 O O . LEU B 2 179 ? 40.372 32.788 17.564 1.00 62.69 ? 1715 LEU B O 1 ATOM 3330 C CB . LEU B 2 179 ? 38.110 35.077 17.809 1.00 57.66 ? 1715 LEU B CB 1 ATOM 3331 C CG . LEU B 2 179 ? 37.569 36.182 18.711 1.00 57.69 ? 1715 LEU B CG 1 ATOM 3332 C CD1 . LEU B 2 179 ? 37.334 37.418 17.855 1.00 57.10 ? 1715 LEU B CD1 1 ATOM 3333 C CD2 . LEU B 2 179 ? 36.287 35.742 19.406 1.00 54.01 ? 1715 LEU B CD2 1 ATOM 3334 N N . ASP B 2 180 ? 38.399 32.040 16.788 1.00 64.40 ? 1716 ASP B N 1 ATOM 3335 C CA . ASP B 2 180 ? 38.971 31.079 15.861 1.00 66.47 ? 1716 ASP B CA 1 ATOM 3336 C C . ASP B 2 180 ? 39.127 31.661 14.460 1.00 69.02 ? 1716 ASP B C 1 ATOM 3337 O O . ASP B 2 180 ? 38.473 32.644 14.127 1.00 68.22 ? 1716 ASP B O 1 ATOM 3338 C CB . ASP B 2 180 ? 38.069 29.844 15.830 1.00 66.57 ? 1716 ASP B CB 1 ATOM 3339 C CG . ASP B 2 180 ? 38.454 28.869 14.754 1.00 65.02 ? 1716 ASP B CG 1 ATOM 3340 O OD1 . ASP B 2 180 ? 38.067 29.083 13.586 1.00 63.43 ? 1716 ASP B OD1 1 ATOM 3341 O OD2 . ASP B 2 180 ? 39.150 27.891 15.088 1.00 66.59 ? 1716 ASP B OD2 1 ATOM 3342 N N . LYS B 2 181 ? 40.000 31.046 13.658 1.00 71.85 ? 1717 LYS B N 1 ATOM 3343 C CA . LYS B 2 181 ? 40.271 31.457 12.279 1.00 74.87 ? 1717 LYS B CA 1 ATOM 3344 C C . LYS B 2 181 ? 39.141 32.281 11.662 1.00 77.19 ? 1717 LYS B C 1 ATOM 3345 O O . LYS B 2 181 ? 39.386 33.319 11.038 1.00 77.95 ? 1717 LYS B O 1 ATOM 3346 C CB . LYS B 2 181 ? 40.527 30.221 11.424 1.00 76.99 ? 1717 LYS B CB 1 ATOM 3347 C CG . LYS B 2 181 ? 41.729 29.396 11.879 1.00 81.23 ? 1717 LYS B CG 1 ATOM 3348 C CD . LYS B 2 181 ? 42.898 29.456 10.880 1.00 83.81 ? 1717 LYS B CD 1 ATOM 3349 C CE . LYS B 2 181 ? 43.438 30.879 10.688 1.00 85.13 ? 1717 LYS B CE 1 ATOM 3350 N NZ . LYS B 2 181 ? 43.995 31.471 11.942 1.00 84.17 ? 1717 LYS B NZ 1 ATOM 3351 N N . GLU B 2 182 ? 37.907 31.805 11.836 1.00 78.59 ? 1718 GLU B N 1 ATOM 3352 C CA . GLU B 2 182 ? 36.710 32.497 11.341 1.00 78.01 ? 1718 GLU B CA 1 ATOM 3353 C C . GLU B 2 182 ? 35.871 33.090 12.505 1.00 76.37 ? 1718 GLU B C 1 ATOM 3354 O O . GLU B 2 182 ? 34.679 32.795 12.655 1.00 76.50 ? 1718 GLU B O 1 ATOM 3355 C CB . GLU B 2 182 ? 35.868 31.532 10.494 1.00 77.19 ? 1718 GLU B CB 1 ATOM 3356 C CG . GLU B 2 182 ? 35.778 30.114 11.046 1.00 77.84 ? 1718 GLU B CG 1 ATOM 3357 C CD . GLU B 2 182 ? 35.228 30.053 12.461 1.00 76.86 ? 1718 GLU B CD 1 ATOM 3358 O OE1 . GLU B 2 182 ? 35.966 30.386 13.412 1.00 76.44 ? 1718 GLU B OE1 1 ATOM 3359 O OE2 . GLU B 2 182 ? 34.051 29.679 12.620 1.00 76.42 ? 1718 GLU B OE2 1 ATOM 3360 N N . THR B 2 183 ? 36.534 33.929 13.304 1.00 73.88 ? 1719 THR B N 1 ATOM 3361 C CA . THR B 2 183 ? 35.995 34.629 14.485 1.00 71.33 ? 1719 THR B CA 1 ATOM 3362 C C . THR B 2 183 ? 34.699 34.189 15.187 1.00 70.47 ? 1719 THR B C 1 ATOM 3363 O O . THR B 2 183 ? 33.630 34.734 14.923 1.00 71.30 ? 1719 THR B O 1 ATOM 3364 C CB . THR B 2 183 ? 35.887 36.147 14.207 1.00 68.85 ? 1719 THR B CB 1 ATOM 3365 O OG1 . THR B 2 183 ? 35.194 36.370 12.974 1.00 67.88 ? 1719 THR B OG1 1 ATOM 3366 C CG2 . THR B 2 183 ? 37.266 36.757 14.129 1.00 67.88 ? 1719 THR B CG2 1 ATOM 3367 N N . ASN B 2 184 ? 34.822 33.229 16.107 1.00 69.13 ? 1720 ASN B N 1 ATOM 3368 C CA . ASN B 2 184 ? 33.709 32.696 16.912 1.00 68.69 ? 1720 ASN B CA 1 ATOM 3369 C C . ASN B 2 184 ? 34.375 32.178 18.194 1.00 69.02 ? 1720 ASN B C 1 ATOM 3370 O O . ASN B 2 184 ? 35.561 31.869 18.180 1.00 68.46 ? 1720 ASN B O 1 ATOM 3371 C CB . ASN B 2 184 ? 33.016 31.531 16.181 1.00 68.84 ? 1720 ASN B CB 1 ATOM 3372 C CG . ASN B 2 184 ? 31.589 31.867 15.707 1.00 69.70 ? 1720 ASN B CG 1 ATOM 3373 O OD1 . ASN B 2 184 ? 31.348 32.903 15.084 1.00 70.46 ? 1720 ASN B OD1 1 ATOM 3374 N ND2 . ASN B 2 184 ? 30.646 30.970 15.985 1.00 67.24 ? 1720 ASN B ND2 1 ATOM 3375 N N . MET B 2 185 ? 33.647 32.097 19.299 1.00 69.76 ? 1721 MET B N 1 ATOM 3376 C CA . MET B 2 185 ? 34.244 31.587 20.535 1.00 74.63 ? 1721 MET B CA 1 ATOM 3377 C C . MET B 2 185 ? 34.233 30.043 20.534 1.00 75.75 ? 1721 MET B C 1 ATOM 3378 O O . MET B 2 185 ? 33.205 29.419 20.255 1.00 75.82 ? 1721 MET B O 1 ATOM 3379 C CB . MET B 2 185 ? 33.462 32.101 21.759 1.00 78.78 ? 1721 MET B CB 1 ATOM 3380 C CG . MET B 2 185 ? 34.238 32.110 23.123 1.00 83.59 ? 1721 MET B CG 1 ATOM 3381 S SD . MET B 2 185 ? 34.695 30.555 24.042 1.00 85.75 ? 1721 MET B SD 1 ATOM 3382 C CE . MET B 2 185 ? 35.574 31.266 25.523 1.00 79.31 ? 1721 MET B CE 1 ATOM 3383 N N . PRO B 2 186 ? 35.378 29.409 20.847 1.00 76.08 ? 1722 PRO B N 1 ATOM 3384 C CA . PRO B 2 186 ? 35.460 27.946 20.874 1.00 76.35 ? 1722 PRO B CA 1 ATOM 3385 C C . PRO B 2 186 ? 35.336 27.372 22.284 1.00 76.14 ? 1722 PRO B C 1 ATOM 3386 O O . PRO B 2 186 ? 34.625 26.390 22.507 1.00 77.17 ? 1722 PRO B O 1 ATOM 3387 C CB . PRO B 2 186 ? 36.837 27.681 20.285 1.00 75.82 ? 1722 PRO B CB 1 ATOM 3388 C CG . PRO B 2 186 ? 37.642 28.747 20.940 1.00 76.76 ? 1722 PRO B CG 1 ATOM 3389 C CD . PRO B 2 186 ? 36.733 29.989 20.837 1.00 76.98 ? 1722 PRO B CD 1 ATOM 3390 N N . VAL B 2 187 ? 36.041 27.992 23.228 1.00 75.15 ? 1723 VAL B N 1 ATOM 3391 C CA . VAL B 2 187 ? 36.046 27.547 24.619 1.00 74.68 ? 1723 VAL B CA 1 ATOM 3392 C C . VAL B 2 187 ? 34.664 27.592 25.276 1.00 71.35 ? 1723 VAL B C 1 ATOM 3393 O O . VAL B 2 187 ? 33.796 26.782 24.948 1.00 68.38 ? 1723 VAL B O 1 ATOM 3394 C CB . VAL B 2 187 ? 37.048 28.384 25.465 1.00 77.32 ? 1723 VAL B CB 1 ATOM 3395 C CG1 . VAL B 2 187 ? 37.183 27.783 26.872 1.00 78.07 ? 1723 VAL B CG1 1 ATOM 3396 C CG2 . VAL B 2 187 ? 38.414 28.423 24.767 1.00 77.72 ? 1723 VAL B CG2 1 ATOM 3397 N N . ASP B 2 188 ? 34.462 28.523 26.208 1.00 69.63 ? 1724 ASP B N 1 ATOM 3398 C CA . ASP B 2 188 ? 33.164 28.635 26.884 1.00 67.73 ? 1724 ASP B CA 1 ATOM 3399 C C . ASP B 2 188 ? 32.107 28.420 25.819 1.00 64.88 ? 1724 ASP B C 1 ATOM 3400 O O . ASP B 2 188 ? 31.094 27.774 26.053 1.00 64.50 ? 1724 ASP B O 1 ATOM 3401 C CB . ASP B 2 188 ? 32.972 30.016 27.525 1.00 64.18 ? 1724 ASP B CB 1 ATOM 3402 C CG . ASP B 2 188 ? 31.562 30.224 28.039 1.00 61.22 ? 1724 ASP B CG 1 ATOM 3403 O OD1 . ASP B 2 188 ? 31.232 29.759 29.145 1.00 58.62 ? 1724 ASP B OD1 1 ATOM 3404 O OD2 . ASP B 2 188 ? 30.768 30.849 27.319 1.00 61.05 ? 1724 ASP B OD2 1 ATOM 3405 N N . MET B 2 189 ? 32.387 28.959 24.640 1.00 63.66 ? 1725 MET B N 1 ATOM 3406 C CA . MET B 2 189 ? 31.513 28.840 23.495 1.00 64.28 ? 1725 MET B CA 1 ATOM 3407 C C . MET B 2 189 ? 30.076 29.060 23.901 1.00 59.39 ? 1725 MET B C 1 ATOM 3408 O O . MET B 2 189 ? 29.749 29.136 25.066 1.00 58.65 ? 1725 MET B O 1 ATOM 3409 C CB . MET B 2 189 ? 31.675 27.447 22.857 1.00 72.18 ? 1725 MET B CB 1 ATOM 3410 C CG . MET B 2 189 ? 30.827 27.204 21.591 1.00 78.78 ? 1725 MET B CG 1 ATOM 3411 S SD . MET B 2 189 ? 30.670 25.444 21.146 1.00 84.77 ? 1725 MET B SD 1 ATOM 3412 C CE . MET B 2 189 ? 29.585 24.838 22.464 1.00 83.18 ? 1725 MET B CE 1 ATOM 3413 N N . ARG B 2 190 ? 29.216 29.157 22.910 1.00 57.91 ? 1726 ARG B N 1 ATOM 3414 C CA . ARG B 2 190 ? 27.805 29.368 23.143 1.00 54.47 ? 1726 ARG B CA 1 ATOM 3415 C C . ARG B 2 190 ? 27.589 30.705 23.865 1.00 52.47 ? 1726 ARG B C 1 ATOM 3416 O O . ARG B 2 190 ? 27.472 30.776 25.103 1.00 50.02 ? 1726 ARG B O 1 ATOM 3417 C CB . ARG B 2 190 ? 27.226 28.185 23.930 1.00 51.26 ? 1726 ARG B CB 1 ATOM 3418 C CG . ARG B 2 190 ? 25.718 28.017 23.767 1.00 47.94 ? 1726 ARG B CG 1 ATOM 3419 C CD . ARG B 2 190 ? 25.333 28.261 22.344 1.00 47.03 ? 1726 ARG B CD 1 ATOM 3420 N NE . ARG B 2 190 ? 24.598 27.155 21.722 1.00 52.44 ? 1726 ARG B NE 1 ATOM 3421 C CZ . ARG B 2 190 ? 24.969 25.872 21.709 1.00 49.71 ? 1726 ARG B CZ 1 ATOM 3422 N NH1 . ARG B 2 190 ? 26.072 25.456 22.306 1.00 49.37 ? 1726 ARG B NH1 1 ATOM 3423 N NH2 . ARG B 2 190 ? 24.258 24.998 21.021 1.00 53.71 ? 1726 ARG B NH2 1 ATOM 3424 N N . GLU B 2 191 ? 27.573 31.767 23.062 1.00 47.64 ? 1727 GLU B N 1 ATOM 3425 C CA . GLU B 2 191 ? 27.351 33.108 23.567 1.00 45.59 ? 1727 GLU B CA 1 ATOM 3426 C C . GLU B 2 191 ? 25.938 33.507 23.213 1.00 44.67 ? 1727 GLU B C 1 ATOM 3427 O O . GLU B 2 191 ? 25.367 33.011 22.249 1.00 45.68 ? 1727 GLU B O 1 ATOM 3428 C CB . GLU B 2 191 ? 28.316 34.119 22.929 1.00 44.85 ? 1727 GLU B CB 1 ATOM 3429 C CG . GLU B 2 191 ? 29.719 34.118 23.516 1.00 45.94 ? 1727 GLU B CG 1 ATOM 3430 C CD . GLU B 2 191 ? 30.589 35.205 22.930 1.00 48.30 ? 1727 GLU B CD 1 ATOM 3431 O OE1 . GLU B 2 191 ? 30.721 35.246 21.688 1.00 49.65 ? 1727 GLU B OE1 1 ATOM 3432 O OE2 . GLU B 2 191 ? 31.140 36.017 23.706 1.00 46.38 ? 1727 GLU B OE2 1 ATOM 3433 N N . PHE B 2 192 ? 25.361 34.390 24.008 1.00 42.47 ? 1728 PHE B N 1 ATOM 3434 C CA . PHE B 2 192 ? 24.036 34.873 23.707 1.00 40.13 ? 1728 PHE B CA 1 ATOM 3435 C C . PHE B 2 192 ? 24.078 36.364 23.928 1.00 38.79 ? 1728 PHE B C 1 ATOM 3436 O O . PHE B 2 192 ? 24.809 36.844 24.777 1.00 38.84 ? 1728 PHE B O 1 ATOM 3437 C CB . PHE B 2 192 ? 22.993 34.180 24.581 1.00 36.23 ? 1728 PHE B CB 1 ATOM 3438 C CG . PHE B 2 192 ? 22.644 32.794 24.108 1.00 34.00 ? 1728 PHE B CG 1 ATOM 3439 C CD1 . PHE B 2 192 ? 22.310 32.570 22.770 1.00 34.77 ? 1728 PHE B CD1 1 ATOM 3440 C CD2 . PHE B 2 192 ? 22.624 31.722 24.987 1.00 29.35 ? 1728 PHE B CD2 1 ATOM 3441 C CE1 . PHE B 2 192 ? 21.956 31.294 22.318 1.00 32.15 ? 1728 PHE B CE1 1 ATOM 3442 C CE2 . PHE B 2 192 ? 22.275 30.444 24.549 1.00 30.11 ? 1728 PHE B CE2 1 ATOM 3443 C CZ . PHE B 2 192 ? 21.940 30.224 23.221 1.00 31.24 ? 1728 PHE B CZ 1 ATOM 3444 N N . VAL B 2 193 ? 23.333 37.109 23.131 1.00 38.45 ? 1729 VAL B N 1 ATOM 3445 C CA . VAL B 2 193 ? 23.342 38.545 23.276 1.00 38.72 ? 1729 VAL B CA 1 ATOM 3446 C C . VAL B 2 193 ? 21.917 39.013 23.382 1.00 39.55 ? 1729 VAL B C 1 ATOM 3447 O O . VAL B 2 193 ? 21.214 39.108 22.383 1.00 42.80 ? 1729 VAL B O 1 ATOM 3448 C CB . VAL B 2 193 ? 24.007 39.232 22.064 1.00 37.10 ? 1729 VAL B CB 1 ATOM 3449 C CG1 . VAL B 2 193 ? 24.083 40.725 22.308 1.00 39.48 ? 1729 VAL B CG1 1 ATOM 3450 C CG2 . VAL B 2 193 ? 25.388 38.669 21.825 1.00 32.27 ? 1729 VAL B CG2 1 ATOM 3451 N N . LEU B 2 194 ? 21.472 39.299 24.594 1.00 40.25 ? 1730 LEU B N 1 ATOM 3452 C CA . LEU B 2 194 ? 20.107 39.768 24.767 1.00 40.23 ? 1730 LEU B CA 1 ATOM 3453 C C . LEU B 2 194 ? 20.048 41.254 25.114 1.00 40.18 ? 1730 LEU B C 1 ATOM 3454 O O . LEU B 2 194 ? 20.676 41.708 26.061 1.00 43.67 ? 1730 LEU B O 1 ATOM 3455 C CB . LEU B 2 194 ? 19.406 38.971 25.862 1.00 38.45 ? 1730 LEU B CB 1 ATOM 3456 C CG . LEU B 2 194 ? 19.266 37.458 25.701 1.00 38.16 ? 1730 LEU B CG 1 ATOM 3457 C CD1 . LEU B 2 194 ? 18.683 37.137 24.342 1.00 35.52 ? 1730 LEU B CD1 1 ATOM 3458 C CD2 . LEU B 2 194 ? 20.602 36.802 25.892 1.00 37.53 ? 1730 LEU B CD2 1 ATOM 3459 N N . LEU B 2 195 ? 19.297 42.009 24.329 1.00 39.52 ? 1731 LEU B N 1 ATOM 3460 C CA . LEU B 2 195 ? 19.117 43.431 24.575 1.00 38.95 ? 1731 LEU B CA 1 ATOM 3461 C C . LEU B 2 195 ? 17.727 43.630 25.217 1.00 39.07 ? 1731 LEU B C 1 ATOM 3462 O O . LEU B 2 195 ? 16.697 43.388 24.572 1.00 39.38 ? 1731 LEU B O 1 ATOM 3463 C CB . LEU B 2 195 ? 19.214 44.217 23.244 1.00 34.67 ? 1731 LEU B CB 1 ATOM 3464 C CG . LEU B 2 195 ? 18.665 45.649 23.149 1.00 29.11 ? 1731 LEU B CG 1 ATOM 3465 C CD1 . LEU B 2 195 ? 19.492 46.583 23.991 1.00 29.62 ? 1731 LEU B CD1 1 ATOM 3466 C CD2 . LEU B 2 195 ? 18.696 46.123 21.718 1.00 28.45 ? 1731 LEU B CD2 1 ATOM 3467 N N . PHE B 2 196 ? 17.691 44.025 26.491 1.00 37.84 ? 1732 PHE B N 1 ATOM 3468 C CA . PHE B 2 196 ? 16.405 44.276 27.142 1.00 37.69 ? 1732 PHE B CA 1 ATOM 3469 C C . PHE B 2 196 ? 16.149 45.743 26.977 1.00 37.96 ? 1732 PHE B C 1 ATOM 3470 O O . PHE B 2 196 ? 16.905 46.563 27.486 1.00 38.71 ? 1732 PHE B O 1 ATOM 3471 C CB . PHE B 2 196 ? 16.431 43.947 28.627 1.00 38.05 ? 1732 PHE B CB 1 ATOM 3472 C CG . PHE B 2 196 ? 16.620 42.502 28.907 1.00 43.56 ? 1732 PHE B CG 1 ATOM 3473 C CD1 . PHE B 2 196 ? 17.861 41.907 28.726 1.00 44.43 ? 1732 PHE B CD1 1 ATOM 3474 C CD2 . PHE B 2 196 ? 15.547 41.713 29.291 1.00 43.93 ? 1732 PHE B CD2 1 ATOM 3475 C CE1 . PHE B 2 196 ? 18.026 40.552 28.918 1.00 47.10 ? 1732 PHE B CE1 1 ATOM 3476 C CE2 . PHE B 2 196 ? 15.706 40.354 29.486 1.00 46.03 ? 1732 PHE B CE2 1 ATOM 3477 C CZ . PHE B 2 196 ? 16.949 39.771 29.299 1.00 48.30 ? 1732 PHE B CZ 1 ATOM 3478 N N . MET B 2 197 ? 15.083 46.076 26.262 1.00 37.07 ? 1733 MET B N 1 ATOM 3479 C CA . MET B 2 197 ? 14.770 47.460 26.029 1.00 37.04 ? 1733 MET B CA 1 ATOM 3480 C C . MET B 2 197 ? 13.355 47.653 25.515 1.00 37.80 ? 1733 MET B C 1 ATOM 3481 O O . MET B 2 197 ? 12.721 46.715 25.037 1.00 34.61 ? 1733 MET B O 1 ATOM 3482 C CB . MET B 2 197 ? 15.772 48.037 25.029 1.00 38.17 ? 1733 MET B CB 1 ATOM 3483 C CG . MET B 2 197 ? 15.701 49.540 24.845 1.00 37.76 ? 1733 MET B CG 1 ATOM 3484 S SD . MET B 2 197 ? 16.910 50.097 23.665 1.00 46.42 ? 1733 MET B SD 1 ATOM 3485 C CE . MET B 2 197 ? 15.869 50.547 22.251 1.00 42.72 ? 1733 MET B CE 1 ATOM 3486 N N . VAL B 2 198 ? 12.862 48.885 25.646 1.00 37.55 ? 1734 VAL B N 1 ATOM 3487 C CA . VAL B 2 198 ? 11.544 49.232 25.164 1.00 37.15 ? 1734 VAL B CA 1 ATOM 3488 C C . VAL B 2 198 ? 11.677 50.046 23.897 1.00 38.01 ? 1734 VAL B C 1 ATOM 3489 O O . VAL B 2 198 ? 12.344 51.063 23.885 1.00 40.47 ? 1734 VAL B O 1 ATOM 3490 C CB . VAL B 2 198 ? 10.763 50.062 26.164 1.00 34.58 ? 1734 VAL B CB 1 ATOM 3491 C CG1 . VAL B 2 198 ? 9.614 50.761 25.441 1.00 35.29 ? 1734 VAL B CG1 1 ATOM 3492 C CG2 . VAL B 2 198 ? 10.210 49.169 27.265 1.00 31.96 ? 1734 VAL B CG2 1 ATOM 3493 N N . PHE B 2 199 ? 11.068 49.599 22.813 1.00 38.02 ? 1735 PHE B N 1 ATOM 3494 C CA . PHE B 2 199 ? 11.170 50.394 21.614 1.00 40.01 ? 1735 PHE B CA 1 ATOM 3495 C C . PHE B 2 199 ? 9.885 51.163 21.564 1.00 43.85 ? 1735 PHE B C 1 ATOM 3496 O O . PHE B 2 199 ? 8.799 50.582 21.648 1.00 46.10 ? 1735 PHE B O 1 ATOM 3497 C CB . PHE B 2 199 ? 11.315 49.537 20.351 1.00 37.89 ? 1735 PHE B CB 1 ATOM 3498 C CG . PHE B 2 199 ? 12.674 48.911 20.187 1.00 33.40 ? 1735 PHE B CG 1 ATOM 3499 C CD1 . PHE B 2 199 ? 12.986 47.717 20.821 1.00 29.27 ? 1735 PHE B CD1 1 ATOM 3500 C CD2 . PHE B 2 199 ? 13.646 49.535 19.410 1.00 31.41 ? 1735 PHE B CD2 1 ATOM 3501 C CE1 . PHE B 2 199 ? 14.243 47.157 20.681 1.00 33.07 ? 1735 PHE B CE1 1 ATOM 3502 C CE2 . PHE B 2 199 ? 14.912 48.981 19.263 1.00 30.03 ? 1735 PHE B CE2 1 ATOM 3503 C CZ . PHE B 2 199 ? 15.212 47.793 19.898 1.00 32.75 ? 1735 PHE B CZ 1 ATOM 3504 N N . ASP B 2 200 ? 10.016 52.477 21.454 1.00 45.84 ? 1736 ASP B N 1 ATOM 3505 C CA . ASP B 2 200 ? 8.872 53.357 21.390 1.00 47.70 ? 1736 ASP B CA 1 ATOM 3506 C C . ASP B 2 200 ? 8.811 53.853 19.969 1.00 47.72 ? 1736 ASP B C 1 ATOM 3507 O O . ASP B 2 200 ? 9.534 54.780 19.616 1.00 48.87 ? 1736 ASP B O 1 ATOM 3508 C CB . ASP B 2 200 ? 9.086 54.537 22.321 1.00 52.42 ? 1736 ASP B CB 1 ATOM 3509 C CG . ASP B 2 200 ? 7.819 55.308 22.569 1.00 57.12 ? 1736 ASP B CG 1 ATOM 3510 O OD1 . ASP B 2 200 ? 7.911 56.481 22.998 1.00 59.63 ? 1736 ASP B OD1 1 ATOM 3511 O OD2 . ASP B 2 200 ? 6.733 54.729 22.342 1.00 60.33 ? 1736 ASP B OD2 1 ATOM 3512 N N . GLU B 2 201 ? 7.954 53.261 19.145 1.00 46.78 ? 1737 GLU B N 1 ATOM 3513 C CA . GLU B 2 201 ? 7.900 53.695 17.753 1.00 48.48 ? 1737 GLU B CA 1 ATOM 3514 C C . GLU B 2 201 ? 7.599 55.173 17.638 1.00 48.35 ? 1737 GLU B C 1 ATOM 3515 O O . GLU B 2 201 ? 7.715 55.753 16.563 1.00 48.51 ? 1737 GLU B O 1 ATOM 3516 C CB . GLU B 2 201 ? 6.872 52.890 16.944 1.00 47.60 ? 1737 GLU B CB 1 ATOM 3517 C CG . GLU B 2 201 ? 7.305 51.458 16.569 1.00 47.09 ? 1737 GLU B CG 1 ATOM 3518 C CD . GLU B 2 201 ? 8.601 51.385 15.758 1.00 45.54 ? 1737 GLU B CD 1 ATOM 3519 O OE1 . GLU B 2 201 ? 8.742 52.111 14.755 1.00 44.92 ? 1737 GLU B OE1 1 ATOM 3520 O OE2 . GLU B 2 201 ? 9.485 50.577 16.118 1.00 47.29 ? 1737 GLU B OE2 1 ATOM 3521 N N . LYS B 2 202 ? 7.229 55.787 18.755 1.00 50.09 ? 1738 LYS B N 1 ATOM 3522 C CA . LYS B 2 202 ? 6.903 57.204 18.752 1.00 52.71 ? 1738 LYS B CA 1 ATOM 3523 C C . LYS B 2 202 ? 8.152 58.042 18.558 1.00 54.54 ? 1738 LYS B C 1 ATOM 3524 O O . LYS B 2 202 ? 8.101 59.269 18.645 1.00 56.28 ? 1738 LYS B O 1 ATOM 3525 C CB . LYS B 2 202 ? 6.234 57.612 20.061 1.00 51.57 ? 1738 LYS B CB 1 ATOM 3526 C CG . LYS B 2 202 ? 4.963 56.870 20.392 1.00 51.21 ? 1738 LYS B CG 1 ATOM 3527 C CD . LYS B 2 202 ? 4.161 57.671 21.390 1.00 51.41 ? 1738 LYS B CD 1 ATOM 3528 C CE . LYS B 2 202 ? 3.300 56.785 22.248 1.00 52.68 ? 1738 LYS B CE 1 ATOM 3529 N NZ . LYS B 2 202 ? 4.114 55.743 22.918 1.00 51.19 ? 1738 LYS B NZ 1 ATOM 3530 N N . LYS B 2 203 ? 9.275 57.388 18.280 1.00 54.39 ? 1739 LYS B N 1 ATOM 3531 C CA . LYS B 2 203 ? 10.513 58.123 18.098 1.00 53.73 ? 1739 LYS B CA 1 ATOM 3532 C C . LYS B 2 203 ? 11.310 57.700 16.881 1.00 55.44 ? 1739 LYS B C 1 ATOM 3533 O O . LYS B 2 203 ? 12.520 57.591 16.986 1.00 56.86 ? 1739 LYS B O 1 ATOM 3534 C CB . LYS B 2 203 ? 11.384 57.950 19.335 1.00 49.50 ? 1739 LYS B CB 1 ATOM 3535 C CG . LYS B 2 203 ? 10.606 57.964 20.632 1.00 43.97 ? 1739 LYS B CG 1 ATOM 3536 C CD . LYS B 2 203 ? 11.540 57.773 21.816 1.00 43.27 ? 1739 LYS B CD 1 ATOM 3537 C CE . LYS B 2 203 ? 10.785 57.729 23.133 1.00 40.16 ? 1739 LYS B CE 1 ATOM 3538 N NZ . LYS B 2 203 ? 11.656 57.271 24.250 1.00 41.08 ? 1739 LYS B NZ 1 ATOM 3539 N N . SER B 2 204 ? 10.668 57.511 15.725 1.00 58.27 ? 1740 SER B N 1 ATOM 3540 C CA . SER B 2 204 ? 11.403 57.054 14.539 1.00 61.23 ? 1740 SER B CA 1 ATOM 3541 C C . SER B 2 204 ? 10.887 57.476 13.141 1.00 64.76 ? 1740 SER B C 1 ATOM 3542 O O . SER B 2 204 ? 11.150 58.585 12.665 1.00 61.49 ? 1740 SER B O 1 ATOM 3543 C CB . SER B 2 204 ? 11.472 55.534 14.611 1.00 59.19 ? 1740 SER B CB 1 ATOM 3544 O OG . SER B 2 204 ? 12.248 55.012 13.564 1.00 61.46 ? 1740 SER B OG 1 ATOM 3545 N N . TRP B 2 205 ? 10.219 56.533 12.463 1.00 69.41 ? 1741 TRP B N 1 ATOM 3546 C CA . TRP B 2 205 ? 9.609 56.753 11.142 1.00 70.97 ? 1741 TRP B CA 1 ATOM 3547 C C . TRP B 2 205 ? 8.131 56.816 11.493 1.00 75.16 ? 1741 TRP B C 1 ATOM 3548 O O . TRP B 2 205 ? 7.274 56.442 10.687 1.00 75.70 ? 1741 TRP B O 1 ATOM 3549 C CB . TRP B 2 205 ? 9.809 55.558 10.183 1.00 65.38 ? 1741 TRP B CB 1 ATOM 3550 C CG . TRP B 2 205 ? 11.220 55.073 10.040 1.00 63.67 ? 1741 TRP B CG 1 ATOM 3551 C CD1 . TRP B 2 205 ? 11.954 54.427 10.986 1.00 63.22 ? 1741 TRP B CD1 1 ATOM 3552 C CD2 . TRP B 2 205 ? 12.101 55.270 8.921 1.00 61.75 ? 1741 TRP B CD2 1 ATOM 3553 N NE1 . TRP B 2 205 ? 13.235 54.219 10.542 1.00 61.75 ? 1741 TRP B NE1 1 ATOM 3554 C CE2 . TRP B 2 205 ? 13.356 54.728 9.279 1.00 59.99 ? 1741 TRP B CE2 1 ATOM 3555 C CE3 . TRP B 2 205 ? 11.955 55.853 7.660 1.00 60.13 ? 1741 TRP B CE3 1 ATOM 3556 C CZ2 . TRP B 2 205 ? 14.459 54.756 8.424 1.00 58.47 ? 1741 TRP B CZ2 1 ATOM 3557 C CZ3 . TRP B 2 205 ? 13.059 55.877 6.807 1.00 60.90 ? 1741 TRP B CZ3 1 ATOM 3558 C CH2 . TRP B 2 205 ? 14.294 55.332 7.201 1.00 57.79 ? 1741 TRP B CH2 1 ATOM 3559 N N . TYR B 2 206 ? 7.853 57.265 12.718 1.00 79.52 ? 1742 TYR B N 1 ATOM 3560 C CA . TYR B 2 206 ? 6.490 57.361 13.227 1.00 84.80 ? 1742 TYR B CA 1 ATOM 3561 C C . TYR B 2 206 ? 5.594 57.856 12.117 1.00 87.91 ? 1742 TYR B C 1 ATOM 3562 O O . TYR B 2 206 ? 4.761 57.104 11.605 1.00 88.06 ? 1742 TYR B O 1 ATOM 3563 C CB . TYR B 2 206 ? 6.431 58.314 14.420 1.00 86.47 ? 1742 TYR B CB 1 ATOM 3564 C CG . TYR B 2 206 ? 5.201 58.160 15.288 1.00 88.80 ? 1742 TYR B CG 1 ATOM 3565 C CD1 . TYR B 2 206 ? 4.896 56.939 15.891 1.00 89.85 ? 1742 TYR B CD1 1 ATOM 3566 C CD2 . TYR B 2 206 ? 4.360 59.245 15.539 1.00 90.47 ? 1742 TYR B CD2 1 ATOM 3567 C CE1 . TYR B 2 206 ? 3.781 56.801 16.726 1.00 91.05 ? 1742 TYR B CE1 1 ATOM 3568 C CE2 . TYR B 2 206 ? 3.241 59.118 16.374 1.00 91.36 ? 1742 TYR B CE2 1 ATOM 3569 C CZ . TYR B 2 206 ? 2.959 57.894 16.963 1.00 91.38 ? 1742 TYR B CZ 1 ATOM 3570 O OH . TYR B 2 206 ? 1.862 57.768 17.787 1.00 91.20 ? 1742 TYR B OH 1 ATOM 3571 N N . TYR B 2 207 ? 5.772 59.119 11.739 1.00 91.47 ? 1743 TYR B N 1 ATOM 3572 C CA . TYR B 2 207 ? 4.986 59.704 10.661 1.00 95.82 ? 1743 TYR B CA 1 ATOM 3573 C C . TYR B 2 207 ? 3.499 59.652 11.022 1.00 97.53 ? 1743 TYR B C 1 ATOM 3574 O O . TYR B 2 207 ? 2.663 60.255 10.350 1.00 98.17 ? 1743 TYR B O 1 ATOM 3575 C CB . TYR B 2 207 ? 5.261 58.918 9.370 1.00 98.11 ? 1743 TYR B CB 1 ATOM 3576 C CG . TYR B 2 207 ? 4.981 59.656 8.081 1.00 101.05 ? 1743 TYR B CG 1 ATOM 3577 C CD1 . TYR B 2 207 ? 5.418 60.968 7.899 1.00 102.90 ? 1743 TYR B CD1 1 ATOM 3578 C CD2 . TYR B 2 207 ? 4.327 59.025 7.022 1.00 102.08 ? 1743 TYR B CD2 1 ATOM 3579 C CE1 . TYR B 2 207 ? 5.214 61.639 6.694 1.00 104.09 ? 1743 TYR B CE1 1 ATOM 3580 C CE2 . TYR B 2 207 ? 4.118 59.684 5.810 1.00 104.21 ? 1743 TYR B CE2 1 ATOM 3581 C CZ . TYR B 2 207 ? 4.565 60.995 5.652 1.00 104.86 ? 1743 TYR B CZ 1 ATOM 3582 O OH . TYR B 2 207 ? 4.368 61.665 4.459 1.00 105.14 ? 1743 TYR B OH 1 ATOM 3583 N N . ASP B 2 208 ? 3.194 58.931 12.100 1.00 99.07 ? 1744 ASP B N 1 ATOM 3584 C CA . ASP B 2 208 ? 1.833 58.751 12.602 1.00 100.22 ? 1744 ASP B CA 1 ATOM 3585 C C . ASP B 2 208 ? 0.937 57.995 11.622 1.00 100.12 ? 1744 ASP B C 1 ATOM 3586 O O . ASP B 2 208 ? 0.262 57.032 11.997 1.00 99.16 ? 1744 ASP B O 1 ATOM 3587 C CB . ASP B 2 208 ? 1.202 60.104 12.946 1.00 100.41 ? 1744 ASP B CB 1 ATOM 3588 C CG . ASP B 2 208 ? -0.154 59.958 13.611 1.00 101.22 ? 1744 ASP B CG 1 ATOM 3589 O OD1 . ASP B 2 208 ? -1.125 59.582 12.919 1.00 101.52 ? 1744 ASP B OD1 1 ATOM 3590 O OD2 . ASP B 2 208 ? -0.246 60.207 14.831 1.00 101.78 ? 1744 ASP B OD2 1 ATOM 3591 N N . ASN B 2 224 ? -2.047 56.556 20.895 1.00 93.62 ? 1760 ASN B N 1 ATOM 3592 C CA . ASN B 2 224 ? -1.973 55.171 21.359 1.00 92.98 ? 1760 ASN B CA 1 ATOM 3593 C C . ASN B 2 224 ? -0.532 54.808 21.719 1.00 90.67 ? 1760 ASN B C 1 ATOM 3594 O O . ASN B 2 224 ? 0.413 55.329 21.118 1.00 91.41 ? 1760 ASN B O 1 ATOM 3595 C CB . ASN B 2 224 ? -2.493 54.218 20.273 1.00 94.85 ? 1760 ASN B CB 1 ATOM 3596 C CG . ASN B 2 224 ? -2.635 52.789 20.767 1.00 95.01 ? 1760 ASN B CG 1 ATOM 3597 O OD1 . ASN B 2 224 ? -1.657 52.153 21.170 1.00 94.71 ? 1760 ASN B OD1 1 ATOM 3598 N ND2 . ASN B 2 224 ? -3.860 52.278 20.741 1.00 95.27 ? 1760 ASN B ND2 1 ATOM 3599 N N . SER B 2 225 ? -0.372 53.916 22.699 1.00 86.43 ? 1761 SER B N 1 ATOM 3600 C CA . SER B 2 225 ? 0.951 53.482 23.153 1.00 80.90 ? 1761 SER B CA 1 ATOM 3601 C C . SER B 2 225 ? 1.599 52.506 22.188 1.00 77.03 ? 1761 SER B C 1 ATOM 3602 O O . SER B 2 225 ? 1.224 51.332 22.118 1.00 76.42 ? 1761 SER B O 1 ATOM 3603 C CB . SER B 2 225 ? 0.859 52.827 24.529 1.00 81.68 ? 1761 SER B CB 1 ATOM 3604 O OG . SER B 2 225 ? 2.080 52.192 24.859 1.00 80.77 ? 1761 SER B OG 1 ATOM 3605 N N . HIS B 2 226 ? 2.572 53.008 21.439 1.00 71.82 ? 1762 HIS B N 1 ATOM 3606 C CA . HIS B 2 226 ? 3.292 52.196 20.474 1.00 65.24 ? 1762 HIS B CA 1 ATOM 3607 C C . HIS B 2 226 ? 4.615 51.840 21.128 1.00 61.15 ? 1762 HIS B C 1 ATOM 3608 O O . HIS B 2 226 ? 5.685 52.209 20.649 1.00 61.80 ? 1762 HIS B O 1 ATOM 3609 C CB . HIS B 2 226 ? 3.515 52.991 19.182 1.00 64.80 ? 1762 HIS B CB 1 ATOM 3610 C CG . HIS B 2 226 ? 2.249 53.315 18.447 1.00 63.59 ? 1762 HIS B CG 1 ATOM 3611 N ND1 . HIS B 2 226 ? 1.464 52.351 17.856 1.00 63.81 ? 1762 HIS B ND1 1 ATOM 3612 C CD2 . HIS B 2 226 ? 1.620 54.493 18.227 1.00 64.95 ? 1762 HIS B CD2 1 ATOM 3613 C CE1 . HIS B 2 226 ? 0.406 52.917 17.306 1.00 64.22 ? 1762 HIS B CE1 1 ATOM 3614 N NE2 . HIS B 2 226 ? 0.476 54.218 17.517 1.00 64.90 ? 1762 HIS B NE2 1 ATOM 3615 N N . GLU B 2 227 ? 4.519 51.133 22.245 1.00 55.68 ? 1763 GLU B N 1 ATOM 3616 C CA . GLU B 2 227 ? 5.686 50.723 23.000 1.00 53.35 ? 1763 GLU B CA 1 ATOM 3617 C C . GLU B 2 227 ? 5.772 49.220 23.020 1.00 51.48 ? 1763 GLU B C 1 ATOM 3618 O O . GLU B 2 227 ? 4.745 48.548 23.105 1.00 53.79 ? 1763 GLU B O 1 ATOM 3619 C CB . GLU B 2 227 ? 5.589 51.229 24.438 1.00 54.12 ? 1763 GLU B CB 1 ATOM 3620 C CG . GLU B 2 227 ? 6.031 52.681 24.644 1.00 57.03 ? 1763 GLU B CG 1 ATOM 3621 C CD . GLU B 2 227 ? 5.484 53.282 25.937 1.00 57.23 ? 1763 GLU B CD 1 ATOM 3622 O OE1 . GLU B 2 227 ? 5.586 52.628 27.007 1.00 56.19 ? 1763 GLU B OE1 1 ATOM 3623 O OE2 . GLU B 2 227 ? 4.953 54.413 25.874 1.00 56.68 ? 1763 GLU B OE2 1 ATOM 3624 N N . PHE B 2 228 ? 6.993 48.693 22.946 1.00 46.49 ? 1764 PHE B N 1 ATOM 3625 C CA . PHE B 2 228 ? 7.205 47.251 22.981 1.00 38.49 ? 1764 PHE B CA 1 ATOM 3626 C C . PHE B 2 228 ? 8.269 46.824 23.983 1.00 37.49 ? 1764 PHE B C 1 ATOM 3627 O O . PHE B 2 228 ? 9.455 47.070 23.804 1.00 35.41 ? 1764 PHE B O 1 ATOM 3628 C CB . PHE B 2 228 ? 7.528 46.770 21.580 1.00 33.80 ? 1764 PHE B CB 1 ATOM 3629 C CG . PHE B 2 228 ? 6.445 47.067 20.612 1.00 28.75 ? 1764 PHE B CG 1 ATOM 3630 C CD1 . PHE B 2 228 ? 6.455 48.245 19.887 1.00 26.03 ? 1764 PHE B CD1 1 ATOM 3631 C CD2 . PHE B 2 228 ? 5.344 46.211 20.506 1.00 27.19 ? 1764 PHE B CD2 1 ATOM 3632 C CE1 . PHE B 2 228 ? 5.372 48.581 19.064 1.00 27.35 ? 1764 PHE B CE1 1 ATOM 3633 C CE2 . PHE B 2 228 ? 4.263 46.532 19.693 1.00 27.02 ? 1764 PHE B CE2 1 ATOM 3634 C CZ . PHE B 2 228 ? 4.270 47.712 18.973 1.00 26.71 ? 1764 PHE B CZ 1 ATOM 3635 N N . HIS B 2 229 ? 7.815 46.213 25.066 1.00 39.39 ? 1765 HIS B N 1 ATOM 3636 C CA . HIS B 2 229 ? 8.703 45.754 26.128 1.00 42.05 ? 1765 HIS B CA 1 ATOM 3637 C C . HIS B 2 229 ? 9.237 44.450 25.591 1.00 40.40 ? 1765 HIS B C 1 ATOM 3638 O O . HIS B 2 229 ? 8.661 43.375 25.789 1.00 38.82 ? 1765 HIS B O 1 ATOM 3639 C CB . HIS B 2 229 ? 7.905 45.583 27.431 1.00 47.56 ? 1765 HIS B CB 1 ATOM 3640 C CG . HIS B 2 229 ? 7.160 46.824 27.831 1.00 53.90 ? 1765 HIS B CG 1 ATOM 3641 N ND1 . HIS B 2 229 ? 6.126 47.345 27.079 1.00 55.97 ? 1765 HIS B ND1 1 ATOM 3642 C CD2 . HIS B 2 229 ? 7.361 47.700 28.845 1.00 56.19 ? 1765 HIS B CD2 1 ATOM 3643 C CE1 . HIS B 2 229 ? 5.726 48.487 27.609 1.00 55.92 ? 1765 HIS B CE1 1 ATOM 3644 N NE2 . HIS B 2 229 ? 6.459 48.726 28.681 1.00 55.87 ? 1765 HIS B NE2 1 ATOM 3645 N N . ALA B 2 230 ? 10.360 44.583 24.895 1.00 39.08 ? 1766 ALA B N 1 ATOM 3646 C CA . ALA B 2 230 ? 10.980 43.478 24.202 1.00 36.91 ? 1766 ALA B CA 1 ATOM 3647 C C . ALA B 2 230 ? 12.396 43.037 24.561 1.00 36.35 ? 1766 ALA B C 1 ATOM 3648 O O . ALA B 2 230 ? 13.103 43.641 25.364 1.00 36.48 ? 1766 ALA B O 1 ATOM 3649 C CB . ALA B 2 230 ? 10.920 43.787 22.716 1.00 34.25 ? 1766 ALA B CB 1 ATOM 3650 N N . ILE B 2 231 ? 12.783 41.936 23.932 1.00 36.01 ? 1767 ILE B N 1 ATOM 3651 C CA . ILE B 2 231 ? 14.108 41.370 24.057 1.00 34.30 ? 1767 ILE B CA 1 ATOM 3652 C C . ILE B 2 231 ? 14.494 41.246 22.590 1.00 34.20 ? 1767 ILE B C 1 ATOM 3653 O O . ILE B 2 231 ? 13.746 40.693 21.799 1.00 35.09 ? 1767 ILE B O 1 ATOM 3654 C CB . ILE B 2 231 ? 14.078 40.008 24.723 1.00 31.34 ? 1767 ILE B CB 1 ATOM 3655 C CG1 . ILE B 2 231 ? 13.436 40.113 26.110 1.00 29.83 ? 1767 ILE B CG1 1 ATOM 3656 C CG2 . ILE B 2 231 ? 15.473 39.522 24.904 1.00 34.98 ? 1767 ILE B CG2 1 ATOM 3657 C CD1 . ILE B 2 231 ? 13.101 38.786 26.748 1.00 28.34 ? 1767 ILE B CD1 1 ATOM 3658 N N . ASN B 2 232 ? 15.639 41.808 22.221 1.00 35.25 ? 1768 ASN B N 1 ATOM 3659 C CA . ASN B 2 232 ? 16.080 41.785 20.846 1.00 32.54 ? 1768 ASN B CA 1 ATOM 3660 C C . ASN B 2 232 ? 14.945 42.181 19.918 1.00 35.06 ? 1768 ASN B C 1 ATOM 3661 O O . ASN B 2 232 ? 14.815 41.651 18.831 1.00 38.61 ? 1768 ASN B O 1 ATOM 3662 C CB . ASN B 2 232 ? 16.623 40.412 20.501 1.00 32.60 ? 1768 ASN B CB 1 ATOM 3663 C CG . ASN B 2 232 ? 17.896 40.106 21.259 1.00 40.00 ? 1768 ASN B CG 1 ATOM 3664 O OD1 . ASN B 2 232 ? 18.351 40.921 22.068 1.00 41.26 ? 1768 ASN B OD1 1 ATOM 3665 N ND2 . ASN B 2 232 ? 18.486 38.939 21.006 1.00 39.23 ? 1768 ASN B ND2 1 ATOM 3666 N N . GLY B 2 233 ? 14.112 43.116 20.370 1.00 37.21 ? 1769 GLY B N 1 ATOM 3667 C CA . GLY B 2 233 ? 13.009 43.636 19.570 1.00 31.76 ? 1769 GLY B CA 1 ATOM 3668 C C . GLY B 2 233 ? 11.856 42.702 19.318 1.00 30.86 ? 1769 GLY B C 1 ATOM 3669 O O . GLY B 2 233 ? 11.104 42.853 18.349 1.00 31.20 ? 1769 GLY B O 1 ATOM 3670 N N . MET B 2 234 ? 11.690 41.743 20.207 1.00 29.85 ? 1770 MET B N 1 ATOM 3671 C CA . MET B 2 234 ? 10.630 40.767 20.042 1.00 32.78 ? 1770 MET B CA 1 ATOM 3672 C C . MET B 2 234 ? 9.835 40.757 21.337 1.00 30.87 ? 1770 MET B C 1 ATOM 3673 O O . MET B 2 234 ? 10.406 40.905 22.405 1.00 24.04 ? 1770 MET B O 1 ATOM 3674 C CB . MET B 2 234 ? 11.276 39.390 19.805 1.00 39.69 ? 1770 MET B CB 1 ATOM 3675 C CG . MET B 2 234 ? 10.573 38.445 18.832 1.00 44.59 ? 1770 MET B CG 1 ATOM 3676 S SD . MET B 2 234 ? 11.060 38.662 17.108 1.00 53.15 ? 1770 MET B SD 1 ATOM 3677 C CE . MET B 2 234 ? 12.667 37.985 17.104 1.00 43.14 ? 1770 MET B CE 1 ATOM 3678 N N . ILE B 2 235 ? 8.519 40.594 21.257 1.00 33.27 ? 1771 ILE B N 1 ATOM 3679 C CA . ILE B 2 235 ? 7.707 40.538 22.483 1.00 32.72 ? 1771 ILE B CA 1 ATOM 3680 C C . ILE B 2 235 ? 7.111 39.138 22.660 1.00 33.92 ? 1771 ILE B C 1 ATOM 3681 O O . ILE B 2 235 ? 6.605 38.556 21.705 1.00 34.43 ? 1771 ILE B O 1 ATOM 3682 C CB . ILE B 2 235 ? 6.527 41.560 22.463 1.00 31.67 ? 1771 ILE B CB 1 ATOM 3683 C CG1 . ILE B 2 235 ? 5.595 41.258 21.288 1.00 33.88 ? 1771 ILE B CG1 1 ATOM 3684 C CG2 . ILE B 2 235 ? 7.056 42.984 22.345 1.00 26.92 ? 1771 ILE B CG2 1 ATOM 3685 C CD1 . ILE B 2 235 ? 4.261 41.960 21.367 1.00 32.11 ? 1771 ILE B CD1 1 ATOM 3686 N N . TYR B 2 236 ? 7.204 38.611 23.883 1.00 35.50 ? 1772 TYR B N 1 ATOM 3687 C CA . TYR B 2 236 ? 6.666 37.309 24.288 1.00 33.98 ? 1772 TYR B CA 1 ATOM 3688 C C . TYR B 2 236 ? 7.410 36.107 23.795 1.00 34.63 ? 1772 TYR B C 1 ATOM 3689 O O . TYR B 2 236 ? 7.528 35.118 24.517 1.00 38.65 ? 1772 TYR B O 1 ATOM 3690 C CB . TYR B 2 236 ? 5.194 37.171 23.880 1.00 33.54 ? 1772 TYR B CB 1 ATOM 3691 C CG . TYR B 2 236 ? 4.281 38.102 24.625 1.00 36.97 ? 1772 TYR B CG 1 ATOM 3692 C CD1 . TYR B 2 236 ? 4.016 37.909 25.987 1.00 41.83 ? 1772 TYR B CD1 1 ATOM 3693 C CD2 . TYR B 2 236 ? 3.709 39.198 23.994 1.00 37.70 ? 1772 TYR B CD2 1 ATOM 3694 C CE1 . TYR B 2 236 ? 3.210 38.783 26.698 1.00 39.63 ? 1772 TYR B CE1 1 ATOM 3695 C CE2 . TYR B 2 236 ? 2.900 40.082 24.696 1.00 40.24 ? 1772 TYR B CE2 1 ATOM 3696 C CZ . TYR B 2 236 ? 2.656 39.871 26.050 1.00 40.71 ? 1772 TYR B CZ 1 ATOM 3697 O OH . TYR B 2 236 ? 1.879 40.763 26.765 1.00 42.45 ? 1772 TYR B OH 1 ATOM 3698 N N . ASN B 2 237 ? 7.904 36.161 22.568 1.00 33.40 ? 1773 ASN B N 1 ATOM 3699 C CA . ASN B 2 237 ? 8.623 35.016 22.037 1.00 30.92 ? 1773 ASN B CA 1 ATOM 3700 C C . ASN B 2 237 ? 9.763 35.371 21.115 1.00 28.98 ? 1773 ASN B C 1 ATOM 3701 O O . ASN B 2 237 ? 9.542 35.936 20.044 1.00 32.03 ? 1773 ASN B O 1 ATOM 3702 C CB . ASN B 2 237 ? 7.639 34.091 21.313 1.00 35.90 ? 1773 ASN B CB 1 ATOM 3703 C CG . ASN B 2 237 ? 8.266 32.770 20.902 1.00 40.76 ? 1773 ASN B CG 1 ATOM 3704 O OD1 . ASN B 2 237 ? 8.730 32.611 19.775 1.00 49.29 ? 1773 ASN B OD1 1 ATOM 3705 N ND2 . ASN B 2 237 ? 8.289 31.815 21.823 1.00 42.99 ? 1773 ASN B ND2 1 ATOM 3706 N N . LEU B 2 238 ? 10.978 35.040 21.538 1.00 27.29 ? 1774 LEU B N 1 ATOM 3707 C CA . LEU B 2 238 ? 12.195 35.259 20.744 1.00 30.62 ? 1774 LEU B CA 1 ATOM 3708 C C . LEU B 2 238 ? 12.822 33.878 20.473 1.00 36.12 ? 1774 LEU B C 1 ATOM 3709 O O . LEU B 2 238 ? 13.443 33.281 21.363 1.00 40.47 ? 1774 LEU B O 1 ATOM 3710 C CB . LEU B 2 238 ? 13.205 36.083 21.521 1.00 27.44 ? 1774 LEU B CB 1 ATOM 3711 C CG . LEU B 2 238 ? 14.530 36.341 20.812 1.00 27.36 ? 1774 LEU B CG 1 ATOM 3712 C CD1 . LEU B 2 238 ? 14.376 37.542 19.911 1.00 26.91 ? 1774 LEU B CD1 1 ATOM 3713 C CD2 . LEU B 2 238 ? 15.628 36.577 21.811 1.00 25.75 ? 1774 LEU B CD2 1 ATOM 3714 N N . PRO B 2 239 ? 12.682 33.351 19.248 1.00 35.41 ? 1775 PRO B N 1 ATOM 3715 C CA . PRO B 2 239 ? 13.257 32.036 18.946 1.00 35.39 ? 1775 PRO B CA 1 ATOM 3716 C C . PRO B 2 239 ? 14.779 32.039 18.793 1.00 34.56 ? 1775 PRO B C 1 ATOM 3717 O O . PRO B 2 239 ? 15.390 33.078 18.622 1.00 37.11 ? 1775 PRO B O 1 ATOM 3718 C CB . PRO B 2 239 ? 12.544 31.654 17.658 1.00 37.61 ? 1775 PRO B CB 1 ATOM 3719 C CG . PRO B 2 239 ? 12.427 32.988 16.956 1.00 40.92 ? 1775 PRO B CG 1 ATOM 3720 C CD . PRO B 2 239 ? 11.955 33.891 18.088 1.00 38.43 ? 1775 PRO B CD 1 ATOM 3721 N N . GLY B 2 240 ? 15.398 30.874 18.874 1.00 33.80 ? 1776 GLY B N 1 ATOM 3722 C CA . GLY B 2 240 ? 16.831 30.825 18.710 1.00 33.09 ? 1776 GLY B CA 1 ATOM 3723 C C . GLY B 2 240 ? 17.638 30.578 19.959 1.00 34.71 ? 1776 GLY B C 1 ATOM 3724 O O . GLY B 2 240 ? 18.857 30.504 19.890 1.00 36.47 ? 1776 GLY B O 1 ATOM 3725 N N . LEU B 2 241 ? 16.979 30.447 21.101 1.00 35.59 ? 1777 LEU B N 1 ATOM 3726 C CA . LEU B 2 241 ? 17.687 30.211 22.349 1.00 35.71 ? 1777 LEU B CA 1 ATOM 3727 C C . LEU B 2 241 ? 17.675 28.725 22.717 1.00 37.40 ? 1777 LEU B C 1 ATOM 3728 O O . LEU B 2 241 ? 16.711 28.225 23.296 1.00 37.84 ? 1777 LEU B O 1 ATOM 3729 C CB . LEU B 2 241 ? 17.035 31.036 23.456 1.00 38.61 ? 1777 LEU B CB 1 ATOM 3730 C CG . LEU B 2 241 ? 17.093 32.570 23.341 1.00 38.12 ? 1777 LEU B CG 1 ATOM 3731 C CD1 . LEU B 2 241 ? 16.319 33.226 24.473 1.00 33.47 ? 1777 LEU B CD1 1 ATOM 3732 C CD2 . LEU B 2 241 ? 18.550 33.009 23.382 1.00 39.36 ? 1777 LEU B CD2 1 ATOM 3733 N N . ARG B 2 242 ? 18.737 28.009 22.360 1.00 38.52 ? 1778 ARG B N 1 ATOM 3734 C CA . ARG B 2 242 ? 18.834 26.577 22.666 1.00 37.78 ? 1778 ARG B CA 1 ATOM 3735 C C . ARG B 2 242 ? 20.207 26.243 23.226 1.00 37.34 ? 1778 ARG B C 1 ATOM 3736 O O . ARG B 2 242 ? 21.226 26.677 22.694 1.00 37.81 ? 1778 ARG B O 1 ATOM 3737 C CB . ARG B 2 242 ? 18.585 25.727 21.416 1.00 36.03 ? 1778 ARG B CB 1 ATOM 3738 C CG . ARG B 2 242 ? 17.367 26.134 20.644 1.00 35.92 ? 1778 ARG B CG 1 ATOM 3739 C CD . ARG B 2 242 ? 16.999 25.141 19.562 1.00 41.08 ? 1778 ARG B CD 1 ATOM 3740 N NE . ARG B 2 242 ? 16.024 25.726 18.649 1.00 44.52 ? 1778 ARG B NE 1 ATOM 3741 C CZ . ARG B 2 242 ? 16.347 26.549 17.655 1.00 49.04 ? 1778 ARG B CZ 1 ATOM 3742 N NH1 . ARG B 2 242 ? 17.625 26.860 17.443 1.00 46.85 ? 1778 ARG B NH1 1 ATOM 3743 N NH2 . ARG B 2 242 ? 15.391 27.100 16.903 1.00 49.90 ? 1778 ARG B NH2 1 ATOM 3744 N N . MET B 2 243 ? 20.242 25.473 24.304 1.00 37.91 ? 1779 MET B N 1 ATOM 3745 C CA . MET B 2 243 ? 21.523 25.120 24.899 1.00 40.33 ? 1779 MET B CA 1 ATOM 3746 C C . MET B 2 243 ? 21.433 23.754 25.517 1.00 40.58 ? 1779 MET B C 1 ATOM 3747 O O . MET B 2 243 ? 20.337 23.238 25.695 1.00 41.77 ? 1779 MET B O 1 ATOM 3748 C CB . MET B 2 243 ? 21.892 26.144 25.964 1.00 43.29 ? 1779 MET B CB 1 ATOM 3749 C CG . MET B 2 243 ? 20.848 26.286 27.043 1.00 45.37 ? 1779 MET B CG 1 ATOM 3750 S SD . MET B 2 243 ? 20.965 27.897 27.748 1.00 54.42 ? 1779 MET B SD 1 ATOM 3751 C CE . MET B 2 243 ? 19.787 28.796 26.762 1.00 52.24 ? 1779 MET B CE 1 ATOM 3752 N N . TYR B 2 244 ? 22.577 23.169 25.848 1.00 42.19 ? 1780 TYR B N 1 ATOM 3753 C CA . TYR B 2 244 ? 22.591 21.842 26.462 1.00 45.62 ? 1780 TYR B CA 1 ATOM 3754 C C . TYR B 2 244 ? 22.625 21.826 27.989 1.00 47.11 ? 1780 TYR B C 1 ATOM 3755 O O . TYR B 2 244 ? 23.307 22.614 28.627 1.00 47.13 ? 1780 TYR B O 1 ATOM 3756 C CB . TYR B 2 244 ? 23.774 21.014 25.951 1.00 45.13 ? 1780 TYR B CB 1 ATOM 3757 C CG . TYR B 2 244 ? 23.637 20.507 24.536 1.00 44.99 ? 1780 TYR B CG 1 ATOM 3758 C CD1 . TYR B 2 244 ? 22.614 19.637 24.186 1.00 45.18 ? 1780 TYR B CD1 1 ATOM 3759 C CD2 . TYR B 2 244 ? 24.559 20.871 23.555 1.00 43.73 ? 1780 TYR B CD2 1 ATOM 3760 C CE1 . TYR B 2 244 ? 22.510 19.136 22.887 1.00 46.37 ? 1780 TYR B CE1 1 ATOM 3761 C CE2 . TYR B 2 244 ? 24.465 20.376 22.268 1.00 46.31 ? 1780 TYR B CE2 1 ATOM 3762 C CZ . TYR B 2 244 ? 23.439 19.509 21.937 1.00 45.39 ? 1780 TYR B CZ 1 ATOM 3763 O OH . TYR B 2 244 ? 23.347 19.022 20.658 1.00 47.12 ? 1780 TYR B OH 1 ATOM 3764 N N . GLU B 2 245 ? 21.876 20.891 28.560 1.00 52.11 ? 1781 GLU B N 1 ATOM 3765 C CA . GLU B 2 245 ? 21.809 20.697 30.001 1.00 53.83 ? 1781 GLU B CA 1 ATOM 3766 C C . GLU B 2 245 ? 23.213 20.555 30.588 1.00 53.80 ? 1781 GLU B C 1 ATOM 3767 O O . GLU B 2 245 ? 24.017 19.749 30.112 1.00 54.78 ? 1781 GLU B O 1 ATOM 3768 C CB . GLU B 2 245 ? 20.992 19.443 30.287 1.00 55.67 ? 1781 GLU B CB 1 ATOM 3769 C CG . GLU B 2 245 ? 21.248 18.798 31.622 1.00 59.18 ? 1781 GLU B CG 1 ATOM 3770 C CD . GLU B 2 245 ? 20.842 17.347 31.600 1.00 63.25 ? 1781 GLU B CD 1 ATOM 3771 O OE1 . GLU B 2 245 ? 19.633 17.061 31.470 1.00 64.56 ? 1781 GLU B OE1 1 ATOM 3772 O OE2 . GLU B 2 245 ? 21.740 16.486 31.690 1.00 66.44 ? 1781 GLU B OE2 1 ATOM 3773 N N . GLN B 2 246 ? 23.481 21.345 31.625 1.00 53.13 ? 1782 GLN B N 1 ATOM 3774 C CA . GLN B 2 246 ? 24.762 21.371 32.326 1.00 53.23 ? 1782 GLN B CA 1 ATOM 3775 C C . GLN B 2 246 ? 25.889 21.901 31.452 1.00 54.00 ? 1782 GLN B C 1 ATOM 3776 O O . GLN B 2 246 ? 27.042 21.507 31.620 1.00 55.41 ? 1782 GLN B O 1 ATOM 3777 C CB . GLN B 2 246 ? 25.140 19.985 32.864 1.00 53.67 ? 1782 GLN B CB 1 ATOM 3778 C CG . GLN B 2 246 ? 24.307 19.477 34.056 1.00 59.84 ? 1782 GLN B CG 1 ATOM 3779 C CD . GLN B 2 246 ? 24.458 20.317 35.336 1.00 63.31 ? 1782 GLN B CD 1 ATOM 3780 O OE1 . GLN B 2 246 ? 23.505 20.970 35.782 1.00 63.41 ? 1782 GLN B OE1 1 ATOM 3781 N NE2 . GLN B 2 246 ? 25.654 20.295 35.932 1.00 63.89 ? 1782 GLN B NE2 1 ATOM 3782 N N . GLU B 2 247 ? 25.549 22.798 30.525 1.00 52.20 ? 1783 GLU B N 1 ATOM 3783 C CA . GLU B 2 247 ? 26.527 23.421 29.627 1.00 51.19 ? 1783 GLU B CA 1 ATOM 3784 C C . GLU B 2 247 ? 26.698 24.905 29.959 1.00 50.40 ? 1783 GLU B C 1 ATOM 3785 O O . GLU B 2 247 ? 25.725 25.612 30.189 1.00 49.24 ? 1783 GLU B O 1 ATOM 3786 C CB . GLU B 2 247 ? 26.072 23.272 28.171 1.00 51.53 ? 1783 GLU B CB 1 ATOM 3787 C CG . GLU B 2 247 ? 26.721 24.236 27.178 1.00 50.82 ? 1783 GLU B CG 1 ATOM 3788 C CD . GLU B 2 247 ? 26.069 24.194 25.793 1.00 49.72 ? 1783 GLU B CD 1 ATOM 3789 O OE1 . GLU B 2 247 ? 24.829 24.310 25.721 1.00 49.21 ? 1783 GLU B OE1 1 ATOM 3790 O OE2 . GLU B 2 247 ? 26.795 24.056 24.781 1.00 46.76 ? 1783 GLU B OE2 1 ATOM 3791 N N . TRP B 2 248 ? 27.941 25.371 29.982 1.00 50.64 ? 1784 TRP B N 1 ATOM 3792 C CA . TRP B 2 248 ? 28.233 26.772 30.272 1.00 49.34 ? 1784 TRP B CA 1 ATOM 3793 C C . TRP B 2 248 ? 28.044 27.666 29.065 1.00 49.78 ? 1784 TRP B C 1 ATOM 3794 O O . TRP B 2 248 ? 28.730 27.501 28.067 1.00 51.88 ? 1784 TRP B O 1 ATOM 3795 C CB . TRP B 2 248 ? 29.673 26.935 30.759 1.00 49.04 ? 1784 TRP B CB 1 ATOM 3796 C CG . TRP B 2 248 ? 29.835 26.569 32.169 1.00 50.01 ? 1784 TRP B CG 1 ATOM 3797 C CD1 . TRP B 2 248 ? 30.223 25.361 32.664 1.00 50.75 ? 1784 TRP B CD1 1 ATOM 3798 C CD2 . TRP B 2 248 ? 29.481 27.373 33.294 1.00 51.53 ? 1784 TRP B CD2 1 ATOM 3799 N NE1 . TRP B 2 248 ? 30.121 25.356 34.038 1.00 52.67 ? 1784 TRP B NE1 1 ATOM 3800 C CE2 . TRP B 2 248 ? 29.666 26.583 34.450 1.00 53.48 ? 1784 TRP B CE2 1 ATOM 3801 C CE3 . TRP B 2 248 ? 29.015 28.687 33.440 1.00 51.17 ? 1784 TRP B CE3 1 ATOM 3802 C CZ2 . TRP B 2 248 ? 29.401 27.065 35.738 1.00 52.53 ? 1784 TRP B CZ2 1 ATOM 3803 C CZ3 . TRP B 2 248 ? 28.751 29.164 34.715 1.00 52.99 ? 1784 TRP B CZ3 1 ATOM 3804 C CH2 . TRP B 2 248 ? 28.944 28.353 35.849 1.00 50.59 ? 1784 TRP B CH2 1 ATOM 3805 N N . VAL B 2 249 ? 27.114 28.608 29.153 1.00 49.53 ? 1785 VAL B N 1 ATOM 3806 C CA . VAL B 2 249 ? 26.881 29.555 28.068 1.00 47.52 ? 1785 VAL B CA 1 ATOM 3807 C C . VAL B 2 249 ? 27.314 30.928 28.597 1.00 47.58 ? 1785 VAL B C 1 ATOM 3808 O O . VAL B 2 249 ? 27.319 31.158 29.810 1.00 45.36 ? 1785 VAL B O 1 ATOM 3809 C CB . VAL B 2 249 ? 25.380 29.636 27.680 1.00 46.29 ? 1785 VAL B CB 1 ATOM 3810 C CG1 . VAL B 2 249 ? 24.869 28.291 27.303 1.00 48.28 ? 1785 VAL B CG1 1 ATOM 3811 C CG2 . VAL B 2 249 ? 24.566 30.157 28.842 1.00 49.04 ? 1785 VAL B CG2 1 ATOM 3812 N N . ARG B 2 250 ? 27.678 31.833 27.697 1.00 45.32 ? 1786 ARG B N 1 ATOM 3813 C CA . ARG B 2 250 ? 28.071 33.169 28.107 1.00 43.21 ? 1786 ARG B CA 1 ATOM 3814 C C . ARG B 2 250 ? 27.001 34.156 27.671 1.00 41.99 ? 1786 ARG B C 1 ATOM 3815 O O . ARG B 2 250 ? 26.643 34.209 26.504 1.00 41.08 ? 1786 ARG B O 1 ATOM 3816 C CB . ARG B 2 250 ? 29.416 33.552 27.491 1.00 43.92 ? 1786 ARG B CB 1 ATOM 3817 C CG . ARG B 2 250 ? 29.965 34.889 27.971 1.00 44.74 ? 1786 ARG B CG 1 ATOM 3818 C CD . ARG B 2 250 ? 31.440 34.996 27.654 1.00 46.99 ? 1786 ARG B CD 1 ATOM 3819 N NE . ARG B 2 250 ? 31.697 34.866 26.224 1.00 51.44 ? 1786 ARG B NE 1 ATOM 3820 C CZ . ARG B 2 250 ? 32.641 34.092 25.690 1.00 54.77 ? 1786 ARG B CZ 1 ATOM 3821 N NH1 . ARG B 2 250 ? 33.447 33.352 26.448 1.00 54.95 ? 1786 ARG B NH1 1 ATOM 3822 N NH2 . ARG B 2 250 ? 32.777 34.056 24.379 1.00 57.30 ? 1786 ARG B NH2 1 ATOM 3823 N N . LEU B 2 251 ? 26.491 34.938 28.612 1.00 41.67 ? 1787 LEU B N 1 ATOM 3824 C CA . LEU B 2 251 ? 25.458 35.909 28.298 1.00 41.70 ? 1787 LEU B CA 1 ATOM 3825 C C . LEU B 2 251 ? 25.988 37.327 28.206 1.00 41.07 ? 1787 LEU B C 1 ATOM 3826 O O . LEU B 2 251 ? 26.725 37.768 29.078 1.00 44.61 ? 1787 LEU B O 1 ATOM 3827 C CB . LEU B 2 251 ? 24.366 35.900 29.372 1.00 42.53 ? 1787 LEU B CB 1 ATOM 3828 C CG . LEU B 2 251 ? 23.552 34.658 29.719 1.00 44.83 ? 1787 LEU B CG 1 ATOM 3829 C CD1 . LEU B 2 251 ? 23.007 34.045 28.435 1.00 45.92 ? 1787 LEU B CD1 1 ATOM 3830 C CD2 . LEU B 2 251 ? 24.402 33.668 30.475 1.00 47.15 ? 1787 LEU B CD2 1 ATOM 3831 N N . HIS B 2 252 ? 25.603 38.044 27.159 1.00 37.93 ? 1788 HIS B N 1 ATOM 3832 C CA . HIS B 2 252 ? 25.989 39.444 27.029 1.00 37.05 ? 1788 HIS B CA 1 ATOM 3833 C C . HIS B 2 252 ? 24.683 40.223 27.093 1.00 37.99 ? 1788 HIS B C 1 ATOM 3834 O O . HIS B 2 252 ? 23.915 40.276 26.118 1.00 35.84 ? 1788 HIS B O 1 ATOM 3835 C CB . HIS B 2 252 ? 26.691 39.726 25.705 1.00 36.32 ? 1788 HIS B CB 1 ATOM 3836 C CG . HIS B 2 252 ? 27.976 38.985 25.542 1.00 37.14 ? 1788 HIS B CG 1 ATOM 3837 N ND1 . HIS B 2 252 ? 29.020 39.114 26.427 1.00 33.50 ? 1788 HIS B ND1 1 ATOM 3838 C CD2 . HIS B 2 252 ? 28.367 38.071 24.622 1.00 33.91 ? 1788 HIS B CD2 1 ATOM 3839 C CE1 . HIS B 2 252 ? 29.999 38.308 26.062 1.00 32.06 ? 1788 HIS B CE1 1 ATOM 3840 N NE2 . HIS B 2 252 ? 29.628 37.664 24.971 1.00 32.04 ? 1788 HIS B NE2 1 ATOM 3841 N N . LEU B 2 253 ? 24.428 40.807 28.261 1.00 38.45 ? 1789 LEU B N 1 ATOM 3842 C CA . LEU B 2 253 ? 23.214 41.588 28.489 1.00 39.05 ? 1789 LEU B CA 1 ATOM 3843 C C . LEU B 2 253 ? 23.524 43.068 28.286 1.00 38.23 ? 1789 LEU B C 1 ATOM 3844 O O . LEU B 2 253 ? 24.450 43.589 28.914 1.00 35.80 ? 1789 LEU B O 1 ATOM 3845 C CB . LEU B 2 253 ? 22.719 41.366 29.919 1.00 37.28 ? 1789 LEU B CB 1 ATOM 3846 C CG . LEU B 2 253 ? 22.711 39.906 30.384 1.00 38.02 ? 1789 LEU B CG 1 ATOM 3847 C CD1 . LEU B 2 253 ? 22.506 39.837 31.887 1.00 31.52 ? 1789 LEU B CD1 1 ATOM 3848 C CD2 . LEU B 2 253 ? 21.641 39.144 29.622 1.00 36.28 ? 1789 LEU B CD2 1 ATOM 3849 N N . LEU B 2 254 ? 22.770 43.728 27.405 1.00 36.23 ? 1790 LEU B N 1 ATOM 3850 C CA . LEU B 2 254 ? 22.962 45.150 27.155 1.00 42.73 ? 1790 LEU B CA 1 ATOM 3851 C C . LEU B 2 254 ? 21.661 45.955 27.095 1.00 44.90 ? 1790 LEU B C 1 ATOM 3852 O O . LEU B 2 254 ? 20.781 45.643 26.315 1.00 47.57 ? 1790 LEU B O 1 ATOM 3853 C CB . LEU B 2 254 ? 23.785 45.372 25.866 1.00 43.06 ? 1790 LEU B CB 1 ATOM 3854 C CG . LEU B 2 254 ? 23.610 44.512 24.615 1.00 46.19 ? 1790 LEU B CG 1 ATOM 3855 C CD1 . LEU B 2 254 ? 22.305 44.825 23.931 1.00 46.76 ? 1790 LEU B CD1 1 ATOM 3856 C CD2 . LEU B 2 254 ? 24.756 44.778 23.674 1.00 43.71 ? 1790 LEU B CD2 1 ATOM 3857 N N . ASN B 2 255 ? 21.549 46.992 27.922 1.00 46.57 ? 1791 ASN B N 1 ATOM 3858 C CA . ASN B 2 255 ? 20.354 47.846 27.953 1.00 48.33 ? 1791 ASN B CA 1 ATOM 3859 C C . ASN B 2 255 ? 20.695 49.294 27.617 1.00 47.55 ? 1791 ASN B C 1 ATOM 3860 O O . ASN B 2 255 ? 21.249 50.010 28.432 1.00 45.13 ? 1791 ASN B O 1 ATOM 3861 C CB . ASN B 2 255 ? 19.683 47.755 29.339 1.00 51.16 ? 1791 ASN B CB 1 ATOM 3862 C CG . ASN B 2 255 ? 18.702 48.903 29.623 1.00 49.01 ? 1791 ASN B CG 1 ATOM 3863 O OD1 . ASN B 2 255 ? 18.271 49.636 28.724 1.00 40.23 ? 1791 ASN B OD1 1 ATOM 3864 N ND2 . ASN B 2 255 ? 18.341 49.046 30.900 1.00 51.40 ? 1791 ASN B ND2 1 ATOM 3865 N N . LEU B 2 256 ? 20.344 49.704 26.402 1.00 50.42 ? 1792 LEU B N 1 ATOM 3866 C CA . LEU B 2 256 ? 20.603 51.050 25.899 1.00 52.23 ? 1792 LEU B CA 1 ATOM 3867 C C . LEU B 2 256 ? 19.350 51.921 25.897 1.00 55.10 ? 1792 LEU B C 1 ATOM 3868 O O . LEU B 2 256 ? 19.200 52.802 25.053 1.00 54.73 ? 1792 LEU B O 1 ATOM 3869 C CB . LEU B 2 256 ? 21.139 50.980 24.468 1.00 52.00 ? 1792 LEU B CB 1 ATOM 3870 C CG . LEU B 2 256 ? 22.545 50.456 24.193 1.00 52.64 ? 1792 LEU B CG 1 ATOM 3871 C CD1 . LEU B 2 256 ? 22.835 50.560 22.707 1.00 52.23 ? 1792 LEU B CD1 1 ATOM 3872 C CD2 . LEU B 2 256 ? 23.551 51.274 24.975 1.00 52.99 ? 1792 LEU B CD2 1 ATOM 3873 N N . GLY B 2 257 ? 18.446 51.677 26.836 1.00 59.56 ? 1793 GLY B N 1 ATOM 3874 C CA . GLY B 2 257 ? 17.234 52.470 26.892 1.00 64.64 ? 1793 GLY B CA 1 ATOM 3875 C C . GLY B 2 257 ? 17.273 53.586 27.922 1.00 69.23 ? 1793 GLY B C 1 ATOM 3876 O O . GLY B 2 257 ? 18.228 53.704 28.714 1.00 69.01 ? 1793 GLY B O 1 ATOM 3877 N N . GLY B 2 258 ? 16.217 54.399 27.910 1.00 71.61 ? 1794 GLY B N 1 ATOM 3878 C CA . GLY B 2 258 ? 16.101 55.515 28.833 1.00 73.94 ? 1794 GLY B CA 1 ATOM 3879 C C . GLY B 2 258 ? 16.249 55.186 30.311 1.00 75.75 ? 1794 GLY B C 1 ATOM 3880 O O . GLY B 2 258 ? 16.672 54.087 30.694 1.00 74.10 ? 1794 GLY B O 1 ATOM 3881 N N . SER B 2 259 ? 15.888 56.163 31.141 1.00 77.89 ? 1795 SER B N 1 ATOM 3882 C CA . SER B 2 259 ? 15.972 56.057 32.603 1.00 79.16 ? 1795 SER B CA 1 ATOM 3883 C C . SER B 2 259 ? 14.864 55.228 33.234 1.00 78.25 ? 1795 SER B C 1 ATOM 3884 O O . SER B 2 259 ? 15.041 54.661 34.312 1.00 76.98 ? 1795 SER B O 1 ATOM 3885 C CB . SER B 2 259 ? 15.969 57.460 33.218 1.00 79.92 ? 1795 SER B CB 1 ATOM 3886 O OG . SER B 2 259 ? 14.971 58.276 32.620 1.00 81.89 ? 1795 SER B OG 1 ATOM 3887 N N . ARG B 2 260 ? 13.720 55.168 32.558 1.00 78.91 ? 1796 ARG B N 1 ATOM 3888 C CA . ARG B 2 260 ? 12.579 54.407 33.047 1.00 78.47 ? 1796 ARG B CA 1 ATOM 3889 C C . ARG B 2 260 ? 12.644 52.941 32.652 1.00 76.64 ? 1796 ARG B C 1 ATOM 3890 O O . ARG B 2 260 ? 11.674 52.207 32.835 1.00 78.02 ? 1796 ARG B O 1 ATOM 3891 C CB . ARG B 2 260 ? 11.272 55.019 32.539 1.00 80.91 ? 1796 ARG B CB 1 ATOM 3892 C CG . ARG B 2 260 ? 11.328 55.542 31.115 1.00 84.86 ? 1796 ARG B CG 1 ATOM 3893 C CD . ARG B 2 260 ? 10.032 56.261 30.783 1.00 88.11 ? 1796 ARG B CD 1 ATOM 3894 N NE . ARG B 2 260 ? 10.138 57.124 29.609 1.00 91.34 ? 1796 ARG B NE 1 ATOM 3895 C CZ . ARG B 2 260 ? 10.934 58.188 29.522 1.00 93.38 ? 1796 ARG B CZ 1 ATOM 3896 N NH1 . ARG B 2 260 ? 11.713 58.530 30.544 1.00 94.20 ? 1796 ARG B NH1 1 ATOM 3897 N NH2 . ARG B 2 260 ? 10.938 58.925 28.416 1.00 92.95 ? 1796 ARG B NH2 1 ATOM 3898 N N . ASP B 2 261 ? 13.780 52.512 32.110 1.00 73.14 ? 1797 ASP B N 1 ATOM 3899 C CA . ASP B 2 261 ? 13.929 51.119 31.722 1.00 69.78 ? 1797 ASP B CA 1 ATOM 3900 C C . ASP B 2 261 ? 14.127 50.211 32.928 1.00 67.63 ? 1797 ASP B C 1 ATOM 3901 O O . ASP B 2 261 ? 13.149 49.727 33.492 1.00 68.75 ? 1797 ASP B O 1 ATOM 3902 C CB . ASP B 2 261 ? 15.067 50.950 30.724 1.00 69.62 ? 1797 ASP B CB 1 ATOM 3903 C CG . ASP B 2 261 ? 14.571 50.981 29.284 1.00 72.38 ? 1797 ASP B CG 1 ATOM 3904 O OD1 . ASP B 2 261 ? 14.187 52.072 28.796 1.00 70.46 ? 1797 ASP B OD1 1 ATOM 3905 O OD2 . ASP B 2 261 ? 14.543 49.902 28.647 1.00 71.47 ? 1797 ASP B OD2 1 ATOM 3906 N N . ILE B 2 262 ? 15.368 49.978 33.336 1.00 63.21 ? 1798 ILE B N 1 ATOM 3907 C CA . ILE B 2 262 ? 15.611 49.122 34.499 1.00 58.95 ? 1798 ILE B CA 1 ATOM 3908 C C . ILE B 2 262 ? 14.957 47.768 34.254 1.00 55.26 ? 1798 ILE B C 1 ATOM 3909 O O . ILE B 2 262 ? 13.738 47.641 34.343 1.00 52.39 ? 1798 ILE B O 1 ATOM 3910 C CB . ILE B 2 262 ? 14.983 49.696 35.801 1.00 59.92 ? 1798 ILE B CB 1 ATOM 3911 C CG1 . ILE B 2 262 ? 15.318 51.176 35.953 1.00 62.22 ? 1798 ILE B CG1 1 ATOM 3912 C CG2 . ILE B 2 262 ? 15.506 48.936 37.013 1.00 56.61 ? 1798 ILE B CG2 1 ATOM 3913 C CD1 . ILE B 2 262 ? 14.809 51.764 37.250 1.00 64.26 ? 1798 ILE B CD1 1 ATOM 3914 N N . HIS B 2 263 ? 15.771 46.753 33.976 1.00 50.53 ? 1799 HIS B N 1 ATOM 3915 C CA . HIS B 2 263 ? 15.244 45.435 33.700 1.00 44.38 ? 1799 HIS B CA 1 ATOM 3916 C C . HIS B 2 263 ? 15.996 44.370 34.478 1.00 43.67 ? 1799 HIS B C 1 ATOM 3917 O O . HIS B 2 263 ? 17.206 44.263 34.385 1.00 45.55 ? 1799 HIS B O 1 ATOM 3918 C CB . HIS B 2 263 ? 15.336 45.185 32.211 1.00 38.26 ? 1799 HIS B CB 1 ATOM 3919 C CG . HIS B 2 263 ? 14.747 46.281 31.389 1.00 33.08 ? 1799 HIS B CG 1 ATOM 3920 N ND1 . HIS B 2 263 ? 13.404 46.583 31.411 1.00 32.92 ? 1799 HIS B ND1 1 ATOM 3921 C CD2 . HIS B 2 263 ? 15.312 47.142 30.510 1.00 31.03 ? 1799 HIS B CD2 1 ATOM 3922 C CE1 . HIS B 2 263 ? 13.164 47.579 30.577 1.00 31.18 ? 1799 HIS B CE1 1 ATOM 3923 N NE2 . HIS B 2 263 ? 14.307 47.936 30.017 1.00 31.85 ? 1799 HIS B NE2 1 ATOM 3924 N N . VAL B 2 264 ? 15.259 43.574 35.236 1.00 41.80 ? 1800 VAL B N 1 ATOM 3925 C CA . VAL B 2 264 ? 15.846 42.533 36.057 1.00 40.53 ? 1800 VAL B CA 1 ATOM 3926 C C . VAL B 2 264 ? 15.768 41.201 35.329 1.00 41.62 ? 1800 VAL B C 1 ATOM 3927 O O . VAL B 2 264 ? 14.833 40.431 35.514 1.00 40.48 ? 1800 VAL B O 1 ATOM 3928 C CB . VAL B 2 264 ? 15.095 42.452 37.404 1.00 38.05 ? 1800 VAL B CB 1 ATOM 3929 C CG1 . VAL B 2 264 ? 15.749 41.447 38.322 1.00 36.11 ? 1800 VAL B CG1 1 ATOM 3930 C CG2 . VAL B 2 264 ? 15.050 43.832 38.033 1.00 34.81 ? 1800 VAL B CG2 1 ATOM 3931 N N . VAL B 2 265 ? 16.768 40.929 34.501 1.00 43.80 ? 1801 VAL B N 1 ATOM 3932 C CA . VAL B 2 265 ? 16.798 39.701 33.720 1.00 43.72 ? 1801 VAL B CA 1 ATOM 3933 C C . VAL B 2 265 ? 16.770 38.464 34.611 1.00 45.75 ? 1801 VAL B C 1 ATOM 3934 O O . VAL B 2 265 ? 17.627 38.278 35.470 1.00 46.30 ? 1801 VAL B O 1 ATOM 3935 C CB . VAL B 2 265 ? 18.036 39.676 32.802 1.00 44.20 ? 1801 VAL B CB 1 ATOM 3936 C CG1 . VAL B 2 265 ? 18.164 41.021 32.086 1.00 42.45 ? 1801 VAL B CG1 1 ATOM 3937 C CG2 . VAL B 2 265 ? 19.291 39.380 33.605 1.00 43.35 ? 1801 VAL B CG2 1 ATOM 3938 N N . HIS B 2 266 ? 15.763 37.621 34.398 1.00 46.06 ? 1802 HIS B N 1 ATOM 3939 C CA . HIS B 2 266 ? 15.593 36.405 35.176 1.00 44.87 ? 1802 HIS B CA 1 ATOM 3940 C C . HIS B 2 266 ? 15.493 35.150 34.295 1.00 45.64 ? 1802 HIS B C 1 ATOM 3941 O O . HIS B 2 266 ? 14.604 35.049 33.446 1.00 44.05 ? 1802 HIS B O 1 ATOM 3942 C CB . HIS B 2 266 ? 14.334 36.535 36.035 1.00 44.55 ? 1802 HIS B CB 1 ATOM 3943 C CG . HIS B 2 266 ? 14.095 35.367 36.933 1.00 44.83 ? 1802 HIS B CG 1 ATOM 3944 N ND1 . HIS B 2 266 ? 12.854 34.788 37.083 1.00 43.92 ? 1802 HIS B ND1 1 ATOM 3945 C CD2 . HIS B 2 266 ? 14.948 34.635 37.689 1.00 43.90 ? 1802 HIS B CD2 1 ATOM 3946 C CE1 . HIS B 2 266 ? 12.955 33.742 37.884 1.00 45.58 ? 1802 HIS B CE1 1 ATOM 3947 N NE2 . HIS B 2 266 ? 14.215 33.628 38.265 1.00 45.51 ? 1802 HIS B NE2 1 ATOM 3948 N N . PHE B 2 267 ? 16.417 34.210 34.515 1.00 46.87 ? 1803 PHE B N 1 ATOM 3949 C CA . PHE B 2 267 ? 16.484 32.926 33.793 1.00 46.79 ? 1803 PHE B CA 1 ATOM 3950 C C . PHE B 2 267 ? 15.907 31.838 34.705 1.00 48.68 ? 1803 PHE B C 1 ATOM 3951 O O . PHE B 2 267 ? 16.583 31.338 35.605 1.00 47.56 ? 1803 PHE B O 1 ATOM 3952 C CB . PHE B 2 267 ? 17.943 32.567 33.443 1.00 43.47 ? 1803 PHE B CB 1 ATOM 3953 C CG . PHE B 2 267 ? 18.519 33.362 32.295 1.00 41.16 ? 1803 PHE B CG 1 ATOM 3954 C CD1 . PHE B 2 267 ? 18.191 33.055 30.978 1.00 39.70 ? 1803 PHE B CD1 1 ATOM 3955 C CD2 . PHE B 2 267 ? 19.367 34.438 32.531 1.00 39.37 ? 1803 PHE B CD2 1 ATOM 3956 C CE1 . PHE B 2 267 ? 18.695 33.807 29.922 1.00 34.90 ? 1803 PHE B CE1 1 ATOM 3957 C CE2 . PHE B 2 267 ? 19.872 35.191 31.467 1.00 37.14 ? 1803 PHE B CE2 1 ATOM 3958 C CZ . PHE B 2 267 ? 19.528 34.867 30.164 1.00 32.09 ? 1803 PHE B CZ 1 ATOM 3959 N N . HIS B 2 268 ? 14.654 31.472 34.468 1.00 50.89 ? 1804 HIS B N 1 ATOM 3960 C CA . HIS B 2 268 ? 13.989 30.470 35.289 1.00 51.69 ? 1804 HIS B CA 1 ATOM 3961 C C . HIS B 2 268 ? 14.761 29.182 35.520 1.00 50.60 ? 1804 HIS B C 1 ATOM 3962 O O . HIS B 2 268 ? 15.348 28.608 34.601 1.00 50.98 ? 1804 HIS B O 1 ATOM 3963 C CB . HIS B 2 268 ? 12.618 30.134 34.707 1.00 54.59 ? 1804 HIS B CB 1 ATOM 3964 C CG . HIS B 2 268 ? 11.617 31.239 34.848 1.00 56.53 ? 1804 HIS B CG 1 ATOM 3965 N ND1 . HIS B 2 268 ? 10.260 31.037 34.698 1.00 55.87 ? 1804 HIS B ND1 1 ATOM 3966 C CD2 . HIS B 2 268 ? 11.775 32.555 35.125 1.00 57.40 ? 1804 HIS B CD2 1 ATOM 3967 C CE1 . HIS B 2 268 ? 9.628 32.183 34.877 1.00 59.06 ? 1804 HIS B CE1 1 ATOM 3968 N NE2 . HIS B 2 268 ? 10.523 33.120 35.138 1.00 59.22 ? 1804 HIS B NE2 1 ATOM 3969 N N . GLY B 2 269 ? 14.738 28.729 36.766 1.00 48.60 ? 1805 GLY B N 1 ATOM 3970 C CA . GLY B 2 269 ? 15.424 27.505 37.119 1.00 47.04 ? 1805 GLY B CA 1 ATOM 3971 C C . GLY B 2 269 ? 16.920 27.568 36.902 1.00 46.69 ? 1805 GLY B C 1 ATOM 3972 O O . GLY B 2 269 ? 17.590 26.541 36.958 1.00 46.06 ? 1805 GLY B O 1 ATOM 3973 N N . GLN B 2 270 ? 17.457 28.762 36.673 1.00 47.03 ? 1806 GLN B N 1 ATOM 3974 C CA . GLN B 2 270 ? 18.891 28.902 36.439 1.00 48.24 ? 1806 GLN B CA 1 ATOM 3975 C C . GLN B 2 270 ? 19.559 29.843 37.442 1.00 49.78 ? 1806 GLN B C 1 ATOM 3976 O O . GLN B 2 270 ? 18.900 30.559 38.189 1.00 48.29 ? 1806 GLN B O 1 ATOM 3977 C CB . GLN B 2 270 ? 19.152 29.417 35.013 1.00 47.89 ? 1806 GLN B CB 1 ATOM 3978 C CG . GLN B 2 270 ? 18.322 28.760 33.929 1.00 45.35 ? 1806 GLN B CG 1 ATOM 3979 C CD . GLN B 2 270 ? 18.470 27.258 33.925 1.00 47.72 ? 1806 GLN B CD 1 ATOM 3980 O OE1 . GLN B 2 270 ? 19.583 26.737 33.912 1.00 47.16 ? 1806 GLN B OE1 1 ATOM 3981 N NE2 . GLN B 2 270 ? 17.346 26.550 33.934 1.00 47.44 ? 1806 GLN B NE2 1 ATOM 3982 N N . THR B 2 271 ? 20.885 29.839 37.431 1.00 52.73 ? 1807 THR B N 1 ATOM 3983 C CA . THR B 2 271 ? 21.671 30.676 38.322 1.00 55.15 ? 1807 THR B CA 1 ATOM 3984 C C . THR B 2 271 ? 22.798 31.351 37.550 1.00 54.37 ? 1807 THR B C 1 ATOM 3985 O O . THR B 2 271 ? 23.705 30.679 37.046 1.00 55.19 ? 1807 THR B O 1 ATOM 3986 C CB . THR B 2 271 ? 22.270 29.826 39.447 1.00 58.60 ? 1807 THR B CB 1 ATOM 3987 O OG1 . THR B 2 271 ? 21.214 29.395 40.316 1.00 62.24 ? 1807 THR B OG1 1 ATOM 3988 C CG2 . THR B 2 271 ? 23.315 30.609 40.228 1.00 59.96 ? 1807 THR B CG2 1 ATOM 3989 N N . LEU B 2 272 ? 22.733 32.676 37.461 1.00 52.05 ? 1808 LEU B N 1 ATOM 3990 C CA . LEU B 2 272 ? 23.736 33.460 36.759 1.00 50.78 ? 1808 LEU B CA 1 ATOM 3991 C C . LEU B 2 272 ? 25.017 33.546 37.578 1.00 52.88 ? 1808 LEU B C 1 ATOM 3992 O O . LEU B 2 272 ? 24.973 33.481 38.797 1.00 54.48 ? 1808 LEU B O 1 ATOM 3993 C CB . LEU B 2 272 ? 23.194 34.863 36.497 1.00 49.13 ? 1808 LEU B CB 1 ATOM 3994 C CG . LEU B 2 272 ? 22.254 35.094 35.312 1.00 46.37 ? 1808 LEU B CG 1 ATOM 3995 C CD1 . LEU B 2 272 ? 21.515 33.837 34.976 1.00 47.90 ? 1808 LEU B CD1 1 ATOM 3996 C CD2 . LEU B 2 272 ? 21.297 36.216 35.635 1.00 43.37 ? 1808 LEU B CD2 1 ATOM 3997 N N . LEU B 2 273 ? 26.156 33.687 36.903 1.00 55.24 ? 1809 LEU B N 1 ATOM 3998 C CA . LEU B 2 273 ? 27.456 33.782 37.567 1.00 56.78 ? 1809 LEU B CA 1 ATOM 3999 C C . LEU B 2 273 ? 28.251 35.006 37.132 1.00 59.02 ? 1809 LEU B C 1 ATOM 4000 O O . LEU B 2 273 ? 28.356 35.279 35.948 1.00 59.84 ? 1809 LEU B O 1 ATOM 4001 C CB . LEU B 2 273 ? 28.304 32.542 37.269 1.00 54.74 ? 1809 LEU B CB 1 ATOM 4002 C CG . LEU B 2 273 ? 29.749 32.619 37.783 1.00 52.11 ? 1809 LEU B CG 1 ATOM 4003 C CD1 . LEU B 2 273 ? 29.736 32.611 39.297 1.00 50.67 ? 1809 LEU B CD1 1 ATOM 4004 C CD2 . LEU B 2 273 ? 30.562 31.456 37.269 1.00 49.42 ? 1809 LEU B CD2 1 ATOM 4005 N N . GLU B 2 274 ? 28.818 35.739 38.086 1.00 62.22 ? 1810 GLU B N 1 ATOM 4006 C CA . GLU B 2 274 ? 29.631 36.900 37.746 1.00 65.03 ? 1810 GLU B CA 1 ATOM 4007 C C . GLU B 2 274 ? 31.093 36.474 37.800 1.00 67.18 ? 1810 GLU B C 1 ATOM 4008 O O . GLU B 2 274 ? 31.632 36.230 38.880 1.00 67.32 ? 1810 GLU B O 1 ATOM 4009 C CB . GLU B 2 274 ? 29.392 38.046 38.723 1.00 65.63 ? 1810 GLU B CB 1 ATOM 4010 C CG . GLU B 2 274 ? 30.094 39.335 38.322 1.00 68.41 ? 1810 GLU B CG 1 ATOM 4011 C CD . GLU B 2 274 ? 29.584 40.551 39.083 1.00 71.29 ? 1810 GLU B CD 1 ATOM 4012 O OE1 . GLU B 2 274 ? 30.014 41.681 38.755 1.00 70.94 ? 1810 GLU B OE1 1 ATOM 4013 O OE2 . GLU B 2 274 ? 28.754 40.378 40.007 1.00 72.64 ? 1810 GLU B OE2 1 ATOM 4014 N N . ASN B 2 275 ? 31.717 36.372 36.626 1.00 69.55 ? 1811 ASN B N 1 ATOM 4015 C CA . ASN B 2 275 ? 33.115 35.958 36.502 1.00 72.51 ? 1811 ASN B CA 1 ATOM 4016 C C . ASN B 2 275 ? 34.020 37.179 36.293 1.00 74.99 ? 1811 ASN B C 1 ATOM 4017 O O . ASN B 2 275 ? 33.832 37.962 35.357 1.00 75.74 ? 1811 ASN B O 1 ATOM 4018 C CB . ASN B 2 275 ? 33.269 34.993 35.315 1.00 72.98 ? 1811 ASN B CB 1 ATOM 4019 C CG . ASN B 2 275 ? 34.496 34.084 35.433 1.00 74.95 ? 1811 ASN B CG 1 ATOM 4020 O OD1 . ASN B 2 275 ? 35.481 34.429 36.092 1.00 74.63 ? 1811 ASN B OD1 1 ATOM 4021 N ND2 . ASN B 2 275 ? 34.422 32.926 34.773 1.00 74.65 ? 1811 ASN B ND2 1 ATOM 4022 N N . GLY B 2 276 ? 35.000 37.333 37.174 1.00 76.93 ? 1812 GLY B N 1 ATOM 4023 C CA . GLY B 2 276 ? 35.929 38.443 37.081 1.00 80.07 ? 1812 GLY B CA 1 ATOM 4024 C C . GLY B 2 276 ? 36.971 38.254 38.163 1.00 82.89 ? 1812 GLY B C 1 ATOM 4025 O O . GLY B 2 276 ? 37.225 37.121 38.577 1.00 84.35 ? 1812 GLY B O 1 ATOM 4026 N N . THR B 2 277 ? 37.581 39.342 38.624 1.00 84.12 ? 1813 THR B N 1 ATOM 4027 C CA . THR B 2 277 ? 38.572 39.248 39.693 1.00 84.51 ? 1813 THR B CA 1 ATOM 4028 C C . THR B 2 277 ? 37.803 38.826 40.932 1.00 84.04 ? 1813 THR B C 1 ATOM 4029 O O . THR B 2 277 ? 38.374 38.611 41.995 1.00 84.37 ? 1813 THR B O 1 ATOM 4030 C CB . THR B 2 277 ? 39.230 40.608 39.978 1.00 85.48 ? 1813 THR B CB 1 ATOM 4031 O OG1 . THR B 2 277 ? 39.757 41.147 38.759 1.00 87.22 ? 1813 THR B OG1 1 ATOM 4032 C CG2 . THR B 2 277 ? 40.356 40.456 40.996 1.00 84.66 ? 1813 THR B CG2 1 ATOM 4033 N N . GLN B 2 278 ? 36.491 38.717 40.764 1.00 85.14 ? 1814 GLN B N 1 ATOM 4034 C CA . GLN B 2 278 ? 35.576 38.344 41.830 1.00 86.15 ? 1814 GLN B CA 1 ATOM 4035 C C . GLN B 2 278 ? 34.445 37.490 41.251 1.00 83.84 ? 1814 GLN B C 1 ATOM 4036 O O . GLN B 2 278 ? 33.950 37.749 40.153 1.00 82.37 ? 1814 GLN B O 1 ATOM 4037 C CB . GLN B 2 278 ? 34.993 39.611 42.473 1.00 89.67 ? 1814 GLN B CB 1 ATOM 4038 C CG . GLN B 2 278 ? 33.928 40.340 41.624 1.00 94.53 ? 1814 GLN B CG 1 ATOM 4039 C CD . GLN B 2 278 ? 34.363 40.627 40.181 1.00 96.92 ? 1814 GLN B CD 1 ATOM 4040 O OE1 . GLN B 2 278 ? 35.373 41.300 39.940 1.00 97.89 ? 1814 GLN B OE1 1 ATOM 4041 N NE2 . GLN B 2 278 ? 33.590 40.120 39.217 1.00 97.34 ? 1814 GLN B NE2 1 ATOM 4042 N N . GLN B 2 279 ? 34.034 36.472 41.990 1.00 81.76 ? 1815 GLN B N 1 ATOM 4043 C CA . GLN B 2 279 ? 32.964 35.612 41.523 1.00 81.00 ? 1815 GLN B CA 1 ATOM 4044 C C . GLN B 2 279 ? 31.770 35.669 42.467 1.00 79.30 ? 1815 GLN B C 1 ATOM 4045 O O . GLN B 2 279 ? 31.906 35.475 43.676 1.00 78.37 ? 1815 GLN B O 1 ATOM 4046 C CB . GLN B 2 279 ? 33.471 34.180 41.389 1.00 82.49 ? 1815 GLN B CB 1 ATOM 4047 C CG . GLN B 2 279 ? 34.618 34.040 40.409 1.00 84.87 ? 1815 GLN B CG 1 ATOM 4048 C CD . GLN B 2 279 ? 34.982 32.596 40.154 1.00 86.59 ? 1815 GLN B CD 1 ATOM 4049 O OE1 . GLN B 2 279 ? 35.835 32.295 39.319 1.00 87.48 ? 1815 GLN B OE1 1 ATOM 4050 N NE2 . GLN B 2 279 ? 34.335 31.688 40.877 1.00 87.79 ? 1815 GLN B NE2 1 ATOM 4051 N N . HIS B 2 280 ? 30.598 35.932 41.899 1.00 76.45 ? 1816 HIS B N 1 ATOM 4052 C CA . HIS B 2 280 ? 29.378 36.037 42.678 1.00 74.03 ? 1816 HIS B CA 1 ATOM 4053 C C . HIS B 2 280 ? 28.237 35.282 42.013 1.00 72.21 ? 1816 HIS B C 1 ATOM 4054 O O . HIS B 2 280 ? 28.039 35.395 40.807 1.00 72.41 ? 1816 HIS B O 1 ATOM 4055 C CB . HIS B 2 280 ? 28.993 37.507 42.807 1.00 76.22 ? 1816 HIS B CB 1 ATOM 4056 C CG . HIS B 2 280 ? 30.121 38.393 43.236 1.00 76.97 ? 1816 HIS B CG 1 ATOM 4057 N ND1 . HIS B 2 280 ? 30.713 38.296 44.478 1.00 75.26 ? 1816 HIS B ND1 1 ATOM 4058 C CD2 . HIS B 2 280 ? 30.764 39.393 42.589 1.00 76.61 ? 1816 HIS B CD2 1 ATOM 4059 C CE1 . HIS B 2 280 ? 31.670 39.200 44.576 1.00 75.21 ? 1816 HIS B CE1 1 ATOM 4060 N NE2 . HIS B 2 280 ? 31.723 39.879 43.445 1.00 75.14 ? 1816 HIS B NE2 1 ATOM 4061 N N . GLN B 2 281 ? 27.481 34.520 42.797 1.00 69.84 ? 1817 GLN B N 1 ATOM 4062 C CA . GLN B 2 281 ? 26.356 33.770 42.258 1.00 67.40 ? 1817 GLN B CA 1 ATOM 4063 C C . GLN B 2 281 ? 25.052 34.545 42.416 1.00 64.65 ? 1817 GLN B C 1 ATOM 4064 O O . GLN B 2 281 ? 24.449 34.565 43.486 1.00 64.22 ? 1817 GLN B O 1 ATOM 4065 C CB . GLN B 2 281 ? 26.226 32.404 42.945 1.00 70.38 ? 1817 GLN B CB 1 ATOM 4066 C CG . GLN B 2 281 ? 27.286 31.364 42.560 1.00 76.26 ? 1817 GLN B CG 1 ATOM 4067 C CD . GLN B 2 281 ? 27.175 30.875 41.115 1.00 80.03 ? 1817 GLN B CD 1 ATOM 4068 O OE1 . GLN B 2 281 ? 27.860 29.925 40.708 1.00 80.36 ? 1817 GLN B OE1 1 ATOM 4069 N NE2 . GLN B 2 281 ? 26.318 31.524 40.334 1.00 82.33 ? 1817 GLN B NE2 1 ATOM 4070 N N . LEU B 2 282 ? 24.625 35.184 41.334 1.00 62.40 ? 1818 LEU B N 1 ATOM 4071 C CA . LEU B 2 282 ? 23.393 35.955 41.309 1.00 59.34 ? 1818 LEU B CA 1 ATOM 4072 C C . LEU B 2 282 ? 22.238 35.045 40.875 1.00 58.26 ? 1818 LEU B C 1 ATOM 4073 O O . LEU B 2 282 ? 22.461 34.011 40.251 1.00 60.42 ? 1818 LEU B O 1 ATOM 4074 C CB . LEU B 2 282 ? 23.538 37.117 40.328 1.00 59.16 ? 1818 LEU B CB 1 ATOM 4075 C CG . LEU B 2 282 ? 24.576 38.213 40.617 1.00 59.78 ? 1818 LEU B CG 1 ATOM 4076 C CD1 . LEU B 2 282 ? 24.190 38.946 41.880 1.00 59.07 ? 1818 LEU B CD1 1 ATOM 4077 C CD2 . LEU B 2 282 ? 25.962 37.624 40.749 1.00 58.46 ? 1818 LEU B CD2 1 ATOM 4078 N N . GLY B 2 283 ? 21.009 35.422 41.215 1.00 55.69 ? 1819 GLY B N 1 ATOM 4079 C CA . GLY B 2 283 ? 19.847 34.631 40.836 1.00 51.43 ? 1819 GLY B CA 1 ATOM 4080 C C . GLY B 2 283 ? 19.012 35.380 39.812 1.00 49.49 ? 1819 GLY B C 1 ATOM 4081 O O . GLY B 2 283 ? 18.093 34.831 39.201 1.00 50.05 ? 1819 GLY B O 1 ATOM 4082 N N . VAL B 2 284 ? 19.338 36.657 39.651 1.00 46.97 ? 1820 VAL B N 1 ATOM 4083 C CA . VAL B 2 284 ? 18.692 37.557 38.705 1.00 47.65 ? 1820 VAL B CA 1 ATOM 4084 C C . VAL B 2 284 ? 19.696 38.690 38.634 1.00 47.31 ? 1820 VAL B C 1 ATOM 4085 O O . VAL B 2 284 ? 20.480 38.836 39.552 1.00 50.59 ? 1820 VAL B O 1 ATOM 4086 C CB . VAL B 2 284 ? 17.335 38.104 39.230 1.00 47.48 ? 1820 VAL B CB 1 ATOM 4087 C CG1 . VAL B 2 284 ? 16.491 36.977 39.825 1.00 46.55 ? 1820 VAL B CG1 1 ATOM 4088 C CG2 . VAL B 2 284 ? 17.568 39.187 40.224 1.00 45.41 ? 1820 VAL B CG2 1 ATOM 4089 N N . TRP B 2 285 ? 19.711 39.481 37.568 1.00 47.38 ? 1821 TRP B N 1 ATOM 4090 C CA . TRP B 2 285 ? 20.681 40.567 37.509 1.00 45.76 ? 1821 TRP B CA 1 ATOM 4091 C C . TRP B 2 285 ? 20.084 41.931 37.186 1.00 46.34 ? 1821 TRP B C 1 ATOM 4092 O O . TRP B 2 285 ? 19.335 42.100 36.221 1.00 45.00 ? 1821 TRP B O 1 ATOM 4093 C CB . TRP B 2 285 ? 21.803 40.253 36.511 1.00 49.20 ? 1821 TRP B CB 1 ATOM 4094 C CG . TRP B 2 285 ? 23.008 41.130 36.747 1.00 49.43 ? 1821 TRP B CG 1 ATOM 4095 C CD1 . TRP B 2 285 ? 23.877 41.078 37.821 1.00 50.13 ? 1821 TRP B CD1 1 ATOM 4096 C CD2 . TRP B 2 285 ? 23.351 42.303 36.015 1.00 45.83 ? 1821 TRP B CD2 1 ATOM 4097 N NE1 . TRP B 2 285 ? 24.721 42.170 37.802 1.00 49.67 ? 1821 TRP B NE1 1 ATOM 4098 C CE2 . TRP B 2 285 ? 24.418 42.937 36.707 1.00 48.61 ? 1821 TRP B CE2 1 ATOM 4099 C CE3 . TRP B 2 285 ? 22.856 42.887 34.851 1.00 40.42 ? 1821 TRP B CE3 1 ATOM 4100 C CZ2 . TRP B 2 285 ? 24.989 44.135 36.266 1.00 49.41 ? 1821 TRP B CZ2 1 ATOM 4101 C CZ3 . TRP B 2 285 ? 23.420 44.074 34.412 1.00 48.62 ? 1821 TRP B CZ3 1 ATOM 4102 C CH2 . TRP B 2 285 ? 24.478 44.693 35.120 1.00 49.18 ? 1821 TRP B CH2 1 ATOM 4103 N N . PRO B 2 286 ? 20.396 42.931 38.021 1.00 47.18 ? 1822 PRO B N 1 ATOM 4104 C CA . PRO B 2 286 ? 19.871 44.280 37.794 1.00 46.29 ? 1822 PRO B CA 1 ATOM 4105 C C . PRO B 2 286 ? 20.563 44.926 36.617 1.00 46.27 ? 1822 PRO B C 1 ATOM 4106 O O . PRO B 2 286 ? 21.690 45.387 36.729 1.00 48.87 ? 1822 PRO B O 1 ATOM 4107 C CB . PRO B 2 286 ? 20.165 44.998 39.108 1.00 42.88 ? 1822 PRO B CB 1 ATOM 4108 C CG . PRO B 2 286 ? 20.153 43.878 40.112 1.00 45.13 ? 1822 PRO B CG 1 ATOM 4109 C CD . PRO B 2 286 ? 20.910 42.794 39.396 1.00 46.64 ? 1822 PRO B CD 1 ATOM 4110 N N . LEU B 2 287 ? 19.881 44.947 35.484 1.00 46.73 ? 1823 LEU B N 1 ATOM 4111 C CA . LEU B 2 287 ? 20.423 45.534 34.274 1.00 47.42 ? 1823 LEU B CA 1 ATOM 4112 C C . LEU B 2 287 ? 19.926 46.971 34.179 1.00 48.63 ? 1823 LEU B C 1 ATOM 4113 O O . LEU B 2 287 ? 18.782 47.214 33.784 1.00 49.63 ? 1823 LEU B O 1 ATOM 4114 C CB . LEU B 2 287 ? 19.955 44.734 33.048 1.00 44.96 ? 1823 LEU B CB 1 ATOM 4115 C CG . LEU B 2 287 ? 20.909 44.468 31.876 1.00 43.31 ? 1823 LEU B CG 1 ATOM 4116 C CD1 . LEU B 2 287 ? 20.094 44.439 30.582 1.00 45.68 ? 1823 LEU B CD1 1 ATOM 4117 C CD2 . LEU B 2 287 ? 21.955 45.529 31.777 1.00 41.96 ? 1823 LEU B CD2 1 ATOM 4118 N N . LEU B 2 288 ? 20.792 47.918 34.530 1.00 48.92 ? 1824 LEU B N 1 ATOM 4119 C CA . LEU B 2 288 ? 20.441 49.341 34.495 1.00 48.27 ? 1824 LEU B CA 1 ATOM 4120 C C . LEU B 2 288 ? 20.686 49.994 33.136 1.00 48.30 ? 1824 LEU B C 1 ATOM 4121 O O . LEU B 2 288 ? 21.502 49.517 32.350 1.00 51.21 ? 1824 LEU B O 1 ATOM 4122 C CB . LEU B 2 288 ? 21.213 50.065 35.593 1.00 47.79 ? 1824 LEU B CB 1 ATOM 4123 C CG . LEU B 2 288 ? 20.818 49.505 36.967 1.00 50.59 ? 1824 LEU B CG 1 ATOM 4124 C CD1 . LEU B 2 288 ? 21.778 49.983 38.047 1.00 52.30 ? 1824 LEU B CD1 1 ATOM 4125 C CD2 . LEU B 2 288 ? 19.376 49.918 37.278 1.00 47.37 ? 1824 LEU B CD2 1 ATOM 4126 N N . PRO B 2 289 ? 19.980 51.097 32.837 1.00 47.19 ? 1825 PRO B N 1 ATOM 4127 C CA . PRO B 2 289 ? 20.138 51.798 31.554 1.00 46.25 ? 1825 PRO B CA 1 ATOM 4128 C C . PRO B 2 289 ? 21.594 52.088 31.179 1.00 45.14 ? 1825 PRO B C 1 ATOM 4129 O O . PRO B 2 289 ? 22.458 52.146 32.034 1.00 47.04 ? 1825 PRO B O 1 ATOM 4130 C CB . PRO B 2 289 ? 19.328 53.072 31.758 1.00 47.70 ? 1825 PRO B CB 1 ATOM 4131 C CG . PRO B 2 289 ? 18.254 52.630 32.711 1.00 48.14 ? 1825 PRO B CG 1 ATOM 4132 C CD . PRO B 2 289 ? 19.022 51.801 33.703 1.00 46.98 ? 1825 PRO B CD 1 ATOM 4133 N N . GLY B 2 290 ? 21.859 52.265 29.891 1.00 45.49 ? 1826 GLY B N 1 ATOM 4134 C CA . GLY B 2 290 ? 23.209 52.540 29.439 1.00 43.70 ? 1826 GLY B CA 1 ATOM 4135 C C . GLY B 2 290 ? 24.250 51.524 29.874 1.00 44.84 ? 1826 GLY B C 1 ATOM 4136 O O . GLY B 2 290 ? 25.445 51.790 29.780 1.00 47.35 ? 1826 GLY B O 1 ATOM 4137 N N . SER B 2 291 ? 23.825 50.349 30.324 1.00 44.06 ? 1827 SER B N 1 ATOM 4138 C CA . SER B 2 291 ? 24.800 49.366 30.775 1.00 43.61 ? 1827 SER B CA 1 ATOM 4139 C C . SER B 2 291 ? 24.942 48.090 29.962 1.00 43.70 ? 1827 SER B C 1 ATOM 4140 O O . SER B 2 291 ? 24.019 47.640 29.287 1.00 43.45 ? 1827 SER B O 1 ATOM 4141 C CB . SER B 2 291 ? 24.538 48.989 32.238 1.00 42.96 ? 1827 SER B CB 1 ATOM 4142 O OG . SER B 2 291 ? 23.406 48.160 32.371 1.00 38.98 ? 1827 SER B OG 1 ATOM 4143 N N . PHE B 2 292 ? 26.132 47.516 30.056 1.00 43.86 ? 1828 PHE B N 1 ATOM 4144 C CA . PHE B 2 292 ? 26.483 46.290 29.372 1.00 43.71 ? 1828 PHE B CA 1 ATOM 4145 C C . PHE B 2 292 ? 27.099 45.409 30.436 1.00 45.70 ? 1828 PHE B C 1 ATOM 4146 O O . PHE B 2 292 ? 27.918 45.872 31.237 1.00 48.02 ? 1828 PHE B O 1 ATOM 4147 C CB . PHE B 2 292 ? 27.530 46.555 28.306 1.00 42.88 ? 1828 PHE B CB 1 ATOM 4148 C CG . PHE B 2 292 ? 27.250 47.758 27.465 1.00 44.95 ? 1828 PHE B CG 1 ATOM 4149 C CD1 . PHE B 2 292 ? 25.991 47.964 26.917 1.00 47.74 ? 1828 PHE B CD1 1 ATOM 4150 C CD2 . PHE B 2 292 ? 28.261 48.657 27.168 1.00 44.79 ? 1828 PHE B CD2 1 ATOM 4151 C CE1 . PHE B 2 292 ? 25.742 49.050 26.079 1.00 49.08 ? 1828 PHE B CE1 1 ATOM 4152 C CE2 . PHE B 2 292 ? 28.026 49.743 26.330 1.00 47.94 ? 1828 PHE B CE2 1 ATOM 4153 C CZ . PHE B 2 292 ? 26.765 49.941 25.783 1.00 47.35 ? 1828 PHE B CZ 1 ATOM 4154 N N . LYS B 2 293 ? 26.715 44.143 30.456 1.00 44.97 ? 1829 LYS B N 1 ATOM 4155 C CA . LYS B 2 293 ? 27.264 43.239 31.444 1.00 43.96 ? 1829 LYS B CA 1 ATOM 4156 C C . LYS B 2 293 ? 27.313 41.841 30.863 1.00 42.91 ? 1829 LYS B C 1 ATOM 4157 O O . LYS B 2 293 ? 26.464 41.479 30.053 1.00 43.64 ? 1829 LYS B O 1 ATOM 4158 C CB . LYS B 2 293 ? 26.406 43.259 32.708 1.00 43.20 ? 1829 LYS B CB 1 ATOM 4159 C CG . LYS B 2 293 ? 26.963 42.432 33.863 1.00 45.21 ? 1829 LYS B CG 1 ATOM 4160 C CD . LYS B 2 293 ? 28.378 42.867 34.198 1.00 46.38 ? 1829 LYS B CD 1 ATOM 4161 C CE . LYS B 2 293 ? 28.882 42.135 35.409 1.00 47.44 ? 1829 LYS B CE 1 ATOM 4162 N NZ . LYS B 2 293 ? 28.077 42.536 36.582 1.00 53.83 ? 1829 LYS B NZ 1 ATOM 4163 N N . THR B 2 294 ? 28.312 41.072 31.278 1.00 40.87 ? 1830 THR B N 1 ATOM 4164 C CA . THR B 2 294 ? 28.477 39.716 30.810 1.00 42.15 ? 1830 THR B CA 1 ATOM 4165 C C . THR B 2 294 ? 28.622 38.818 32.011 1.00 42.86 ? 1830 THR B C 1 ATOM 4166 O O . THR B 2 294 ? 29.352 39.118 32.948 1.00 43.21 ? 1830 THR B O 1 ATOM 4167 C CB . THR B 2 294 ? 29.723 39.572 29.882 1.00 43.48 ? 1830 THR B CB 1 ATOM 4168 O OG1 . THR B 2 294 ? 29.903 38.200 29.537 1.00 46.43 ? 1830 THR B OG1 1 ATOM 4169 C CG2 . THR B 2 294 ? 30.972 40.044 30.566 1.00 48.98 ? 1830 THR B CG2 1 ATOM 4170 N N . LEU B 2 295 ? 27.903 37.711 31.988 1.00 44.14 ? 1831 LEU B N 1 ATOM 4171 C CA . LEU B 2 295 ? 27.958 36.776 33.084 1.00 46.95 ? 1831 LEU B CA 1 ATOM 4172 C C . LEU B 2 295 ? 27.559 35.394 32.584 1.00 49.08 ? 1831 LEU B C 1 ATOM 4173 O O . LEU B 2 295 ? 26.474 35.217 32.045 1.00 52.86 ? 1831 LEU B O 1 ATOM 4174 C CB . LEU B 2 295 ? 27.023 37.229 34.221 1.00 47.33 ? 1831 LEU B CB 1 ATOM 4175 C CG . LEU B 2 295 ? 25.552 37.524 33.907 1.00 49.43 ? 1831 LEU B CG 1 ATOM 4176 C CD1 . LEU B 2 295 ? 24.735 37.555 35.190 1.00 49.87 ? 1831 LEU B CD1 1 ATOM 4177 C CD2 . LEU B 2 295 ? 25.436 38.856 33.187 1.00 49.63 ? 1831 LEU B CD2 1 ATOM 4178 N N . GLU B 2 296 ? 28.442 34.416 32.749 1.00 48.36 ? 1832 GLU B N 1 ATOM 4179 C CA . GLU B 2 296 ? 28.137 33.067 32.314 1.00 48.58 ? 1832 GLU B CA 1 ATOM 4180 C C . GLU B 2 296 ? 26.935 32.471 33.072 1.00 48.72 ? 1832 GLU B C 1 ATOM 4181 O O . GLU B 2 296 ? 26.337 33.112 33.936 1.00 46.83 ? 1832 GLU B O 1 ATOM 4182 C CB . GLU B 2 296 ? 29.365 32.163 32.477 1.00 50.64 ? 1832 GLU B CB 1 ATOM 4183 C CG . GLU B 2 296 ? 30.520 32.760 33.267 1.00 55.53 ? 1832 GLU B CG 1 ATOM 4184 C CD . GLU B 2 296 ? 31.607 33.381 32.390 1.00 58.19 ? 1832 GLU B CD 1 ATOM 4185 O OE1 . GLU B 2 296 ? 31.408 34.507 31.879 1.00 59.71 ? 1832 GLU B OE1 1 ATOM 4186 O OE2 . GLU B 2 296 ? 32.666 32.734 32.217 1.00 58.61 ? 1832 GLU B OE2 1 ATOM 4187 N N . MET B 2 297 ? 26.596 31.232 32.732 1.00 48.15 ? 1833 MET B N 1 ATOM 4188 C CA . MET B 2 297 ? 25.475 30.521 33.328 1.00 46.04 ? 1833 MET B CA 1 ATOM 4189 C C . MET B 2 297 ? 25.564 29.048 32.934 1.00 44.89 ? 1833 MET B C 1 ATOM 4190 O O . MET B 2 297 ? 25.801 28.717 31.779 1.00 44.19 ? 1833 MET B O 1 ATOM 4191 C CB . MET B 2 297 ? 24.157 31.119 32.822 1.00 46.20 ? 1833 MET B CB 1 ATOM 4192 C CG . MET B 2 297 ? 22.971 30.173 32.885 1.00 47.53 ? 1833 MET B CG 1 ATOM 4193 S SD . MET B 2 297 ? 21.439 30.914 32.293 1.00 54.06 ? 1833 MET B SD 1 ATOM 4194 C CE . MET B 2 297 ? 21.648 30.860 30.583 1.00 51.59 ? 1833 MET B CE 1 ATOM 4195 N N . LYS B 2 298 ? 25.388 28.162 33.896 1.00 45.16 ? 1834 LYS B N 1 ATOM 4196 C CA . LYS B 2 298 ? 25.443 26.740 33.610 1.00 45.63 ? 1834 LYS B CA 1 ATOM 4197 C C . LYS B 2 298 ? 24.013 26.235 33.600 1.00 44.42 ? 1834 LYS B C 1 ATOM 4198 O O . LYS B 2 298 ? 23.422 26.040 34.653 1.00 48.03 ? 1834 LYS B O 1 ATOM 4199 C CB . LYS B 2 298 ? 26.260 26.031 34.693 1.00 46.81 ? 1834 LYS B CB 1 ATOM 4200 C CG . LYS B 2 298 ? 26.521 24.564 34.447 1.00 48.80 ? 1834 LYS B CG 1 ATOM 4201 C CD . LYS B 2 298 ? 27.498 24.009 35.482 1.00 55.21 ? 1834 LYS B CD 1 ATOM 4202 C CE . LYS B 2 298 ? 27.778 22.514 35.259 1.00 59.25 ? 1834 LYS B CE 1 ATOM 4203 N NZ . LYS B 2 298 ? 28.814 21.939 36.181 1.00 61.10 ? 1834 LYS B NZ 1 ATOM 4204 N N . ALA B 2 299 ? 23.439 26.041 32.422 1.00 42.53 ? 1835 ALA B N 1 ATOM 4205 C CA . ALA B 2 299 ? 22.057 25.572 32.352 1.00 44.29 ? 1835 ALA B CA 1 ATOM 4206 C C . ALA B 2 299 ? 21.871 24.246 33.088 1.00 45.60 ? 1835 ALA B C 1 ATOM 4207 O O . ALA B 2 299 ? 22.769 23.412 33.110 1.00 48.80 ? 1835 ALA B O 1 ATOM 4208 C CB . ALA B 2 299 ? 21.628 25.429 30.901 1.00 40.86 ? 1835 ALA B CB 1 ATOM 4209 N N . SER B 2 300 ? 20.713 24.050 33.701 1.00 45.98 ? 1836 SER B N 1 ATOM 4210 C CA . SER B 2 300 ? 20.453 22.801 34.409 1.00 46.65 ? 1836 SER B CA 1 ATOM 4211 C C . SER B 2 300 ? 19.029 22.307 34.190 1.00 46.40 ? 1836 SER B C 1 ATOM 4212 O O . SER B 2 300 ? 18.060 23.056 34.357 1.00 48.43 ? 1836 SER B O 1 ATOM 4213 C CB . SER B 2 300 ? 20.689 22.975 35.908 1.00 49.80 ? 1836 SER B CB 1 ATOM 4214 O OG . SER B 2 300 ? 19.699 23.802 36.492 1.00 50.07 ? 1836 SER B OG 1 ATOM 4215 N N . LYS B 2 301 ? 18.912 21.044 33.814 1.00 44.15 ? 1837 LYS B N 1 ATOM 4216 C CA . LYS B 2 301 ? 17.620 20.412 33.579 1.00 43.47 ? 1837 LYS B CA 1 ATOM 4217 C C . LYS B 2 301 ? 16.919 20.832 32.307 1.00 41.67 ? 1837 LYS B C 1 ATOM 4218 O O . LYS B 2 301 ? 16.723 22.022 32.048 1.00 41.13 ? 1837 LYS B O 1 ATOM 4219 C CB . LYS B 2 301 ? 16.672 20.640 34.761 1.00 45.22 ? 1837 LYS B CB 1 ATOM 4220 C CG . LYS B 2 301 ? 17.125 19.990 36.053 1.00 48.84 ? 1837 LYS B CG 1 ATOM 4221 C CD . LYS B 2 301 ? 16.255 20.433 37.214 1.00 53.15 ? 1837 LYS B CD 1 ATOM 4222 C CE . LYS B 2 301 ? 16.808 19.944 38.527 1.00 54.47 ? 1837 LYS B CE 1 ATOM 4223 N NZ . LYS B 2 301 ? 18.210 20.394 38.719 1.00 58.05 ? 1837 LYS B NZ 1 ATOM 4224 N N . PRO B 2 302 ? 16.533 19.836 31.493 1.00 39.78 ? 1838 PRO B N 1 ATOM 4225 C CA . PRO B 2 302 ? 15.835 19.919 30.206 1.00 39.73 ? 1838 PRO B CA 1 ATOM 4226 C C . PRO B 2 302 ? 14.456 20.512 30.363 1.00 41.43 ? 1838 PRO B C 1 ATOM 4227 O O . PRO B 2 302 ? 13.907 20.512 31.458 1.00 44.01 ? 1838 PRO B O 1 ATOM 4228 C CB . PRO B 2 302 ? 15.751 18.467 29.764 1.00 38.42 ? 1838 PRO B CB 1 ATOM 4229 C CG . PRO B 2 302 ? 16.978 17.868 30.355 1.00 39.75 ? 1838 PRO B CG 1 ATOM 4230 C CD . PRO B 2 302 ? 17.012 18.464 31.731 1.00 37.46 ? 1838 PRO B CD 1 ATOM 4231 N N . GLY B 2 303 ? 13.897 21.004 29.263 1.00 42.59 ? 1839 GLY B N 1 ATOM 4232 C CA . GLY B 2 303 ? 12.569 21.579 29.296 1.00 41.66 ? 1839 GLY B CA 1 ATOM 4233 C C . GLY B 2 303 ? 12.511 22.993 28.776 1.00 41.97 ? 1839 GLY B C 1 ATOM 4234 O O . GLY B 2 303 ? 13.513 23.525 28.323 1.00 42.19 ? 1839 GLY B O 1 ATOM 4235 N N . TRP B 2 304 ? 11.321 23.584 28.804 1.00 43.11 ? 1840 TRP B N 1 ATOM 4236 C CA . TRP B 2 304 ? 11.139 24.961 28.378 1.00 44.45 ? 1840 TRP B CA 1 ATOM 4237 C C . TRP B 2 304 ? 11.040 25.862 29.604 1.00 46.24 ? 1840 TRP B C 1 ATOM 4238 O O . TRP B 2 304 ? 10.139 25.728 30.431 1.00 48.44 ? 1840 TRP B O 1 ATOM 4239 C CB . TRP B 2 304 ? 9.881 25.121 27.547 1.00 44.96 ? 1840 TRP B CB 1 ATOM 4240 C CG . TRP B 2 304 ? 9.963 24.451 26.238 1.00 48.68 ? 1840 TRP B CG 1 ATOM 4241 C CD1 . TRP B 2 304 ? 9.615 23.165 25.950 1.00 49.92 ? 1840 TRP B CD1 1 ATOM 4242 C CD2 . TRP B 2 304 ? 10.405 25.032 25.014 1.00 51.11 ? 1840 TRP B CD2 1 ATOM 4243 N NE1 . TRP B 2 304 ? 9.807 22.907 24.615 1.00 49.97 ? 1840 TRP B NE1 1 ATOM 4244 C CE2 . TRP B 2 304 ? 10.293 24.037 24.015 1.00 51.34 ? 1840 TRP B CE2 1 ATOM 4245 C CE3 . TRP B 2 304 ? 10.888 26.299 24.658 1.00 52.39 ? 1840 TRP B CE3 1 ATOM 4246 C CZ2 . TRP B 2 304 ? 10.642 24.270 22.683 1.00 51.25 ? 1840 TRP B CZ2 1 ATOM 4247 C CZ3 . TRP B 2 304 ? 11.237 26.532 23.330 1.00 52.30 ? 1840 TRP B CZ3 1 ATOM 4248 C CH2 . TRP B 2 304 ? 11.111 25.522 22.361 1.00 52.95 ? 1840 TRP B CH2 1 ATOM 4249 N N . TRP B 2 305 ? 11.985 26.778 29.721 1.00 45.07 ? 1841 TRP B N 1 ATOM 4250 C CA . TRP B 2 305 ? 12.004 27.695 30.830 1.00 44.10 ? 1841 TRP B CA 1 ATOM 4251 C C . TRP B 2 305 ? 11.794 29.088 30.271 1.00 43.11 ? 1841 TRP B C 1 ATOM 4252 O O . TRP B 2 305 ? 11.937 29.299 29.079 1.00 45.01 ? 1841 TRP B O 1 ATOM 4253 C CB . TRP B 2 305 ? 13.334 27.568 31.551 1.00 43.69 ? 1841 TRP B CB 1 ATOM 4254 C CG . TRP B 2 305 ? 13.618 26.166 31.890 1.00 43.97 ? 1841 TRP B CG 1 ATOM 4255 C CD1 . TRP B 2 305 ? 14.216 25.241 31.099 1.00 46.49 ? 1841 TRP B CD1 1 ATOM 4256 C CD2 . TRP B 2 305 ? 13.289 25.502 33.111 1.00 47.00 ? 1841 TRP B CD2 1 ATOM 4257 N NE1 . TRP B 2 305 ? 14.291 24.030 31.749 1.00 46.59 ? 1841 TRP B NE1 1 ATOM 4258 C CE2 . TRP B 2 305 ? 13.729 24.164 32.990 1.00 47.03 ? 1841 TRP B CE2 1 ATOM 4259 C CE3 . TRP B 2 305 ? 12.663 25.906 34.299 1.00 46.66 ? 1841 TRP B CE3 1 ATOM 4260 C CZ2 . TRP B 2 305 ? 13.568 23.225 34.014 1.00 46.88 ? 1841 TRP B CZ2 1 ATOM 4261 C CZ3 . TRP B 2 305 ? 12.499 24.970 35.317 1.00 46.49 ? 1841 TRP B CZ3 1 ATOM 4262 C CH2 . TRP B 2 305 ? 12.953 23.644 35.165 1.00 47.13 ? 1841 TRP B CH2 1 ATOM 4263 N N . LEU B 2 306 ? 11.448 30.037 31.128 1.00 42.81 ? 1842 LEU B N 1 ATOM 4264 C CA . LEU B 2 306 ? 11.181 31.395 30.684 1.00 40.39 ? 1842 LEU B CA 1 ATOM 4265 C C . LEU B 2 306 ? 12.297 32.364 31.036 1.00 39.24 ? 1842 LEU B C 1 ATOM 4266 O O . LEU B 2 306 ? 13.025 32.171 32.009 1.00 38.69 ? 1842 LEU B O 1 ATOM 4267 C CB . LEU B 2 306 ? 9.867 31.862 31.304 1.00 42.22 ? 1842 LEU B CB 1 ATOM 4268 C CG . LEU B 2 306 ? 9.207 33.191 30.956 1.00 40.00 ? 1842 LEU B CG 1 ATOM 4269 C CD1 . LEU B 2 306 ? 8.503 33.081 29.624 1.00 39.63 ? 1842 LEU B CD1 1 ATOM 4270 C CD2 . LEU B 2 306 ? 8.203 33.518 32.055 1.00 38.60 ? 1842 LEU B CD2 1 ATOM 4271 N N . LEU B 2 307 ? 12.406 33.412 30.228 1.00 39.12 ? 1843 LEU B N 1 ATOM 4272 C CA . LEU B 2 307 ? 13.401 34.455 30.390 1.00 39.10 ? 1843 LEU B CA 1 ATOM 4273 C C . LEU B 2 307 ? 12.641 35.749 30.447 1.00 40.81 ? 1843 LEU B C 1 ATOM 4274 O O . LEU B 2 307 ? 11.930 36.067 29.497 1.00 41.75 ? 1843 LEU B O 1 ATOM 4275 C CB . LEU B 2 307 ? 14.338 34.488 29.187 1.00 39.88 ? 1843 LEU B CB 1 ATOM 4276 C CG . LEU B 2 307 ? 15.231 35.728 29.089 1.00 41.79 ? 1843 LEU B CG 1 ATOM 4277 C CD1 . LEU B 2 307 ? 16.149 35.781 30.315 1.00 41.44 ? 1843 LEU B CD1 1 ATOM 4278 C CD2 . LEU B 2 307 ? 16.032 35.692 27.799 1.00 37.93 ? 1843 LEU B CD2 1 ATOM 4279 N N . ASP B 2 308 ? 12.801 36.503 31.537 1.00 44.50 ? 1844 ASP B N 1 ATOM 4280 C CA . ASP B 2 308 ? 12.090 37.780 31.707 1.00 46.35 ? 1844 ASP B CA 1 ATOM 4281 C C . ASP B 2 308 ? 12.799 38.821 32.563 1.00 46.92 ? 1844 ASP B C 1 ATOM 4282 O O . ASP B 2 308 ? 13.772 38.532 33.253 1.00 45.32 ? 1844 ASP B O 1 ATOM 4283 C CB . ASP B 2 308 ? 10.701 37.532 32.315 1.00 49.74 ? 1844 ASP B CB 1 ATOM 4284 C CG . ASP B 2 308 ? 10.754 36.728 33.635 1.00 53.43 ? 1844 ASP B CG 1 ATOM 4285 O OD1 . ASP B 2 308 ? 11.864 36.492 34.163 1.00 57.45 ? 1844 ASP B OD1 1 ATOM 4286 O OD2 . ASP B 2 308 ? 9.681 36.333 34.147 1.00 51.83 ? 1844 ASP B OD2 1 ATOM 4287 N N . THR B 2 309 ? 12.266 40.039 32.517 1.00 50.88 ? 1845 THR B N 1 ATOM 4288 C CA . THR B 2 309 ? 12.766 41.177 33.288 1.00 52.64 ? 1845 THR B CA 1 ATOM 4289 C C . THR B 2 309 ? 12.221 41.201 34.702 1.00 53.37 ? 1845 THR B C 1 ATOM 4290 O O . THR B 2 309 ? 12.666 41.997 35.516 1.00 54.52 ? 1845 THR B O 1 ATOM 4291 C CB . THR B 2 309 ? 12.341 42.484 32.695 1.00 54.33 ? 1845 THR B CB 1 ATOM 4292 O OG1 . THR B 2 309 ? 12.532 43.521 33.675 1.00 56.29 ? 1845 THR B OG1 1 ATOM 4293 C CG2 . THR B 2 309 ? 10.870 42.412 32.307 1.00 55.27 ? 1845 THR B CG2 1 ATOM 4294 N N . GLU B 2 310 ? 11.236 40.353 34.970 1.00 54.27 ? 1846 GLU B N 1 ATOM 4295 C CA . GLU B 2 310 ? 10.608 40.218 36.285 1.00 56.93 ? 1846 GLU B CA 1 ATOM 4296 C C . GLU B 2 310 ? 10.242 41.480 37.075 1.00 55.66 ? 1846 GLU B C 1 ATOM 4297 O O . GLU B 2 310 ? 10.043 41.445 38.289 1.00 53.27 ? 1846 GLU B O 1 ATOM 4298 C CB . GLU B 2 310 ? 11.420 39.268 37.169 1.00 59.99 ? 1846 GLU B CB 1 ATOM 4299 C CG . GLU B 2 310 ? 12.505 39.871 38.016 1.00 62.41 ? 1846 GLU B CG 1 ATOM 4300 C CD . GLU B 2 310 ? 13.099 38.812 38.933 1.00 67.85 ? 1846 GLU B CD 1 ATOM 4301 O OE1 . GLU B 2 310 ? 12.315 38.132 39.632 1.00 70.02 ? 1846 GLU B OE1 1 ATOM 4302 O OE2 . GLU B 2 310 ? 14.339 38.645 38.954 1.00 71.12 ? 1846 GLU B OE2 1 ATOM 4303 N N . VAL B 2 311 ? 10.181 42.599 36.371 1.00 54.77 ? 1847 VAL B N 1 ATOM 4304 C CA . VAL B 2 311 ? 9.721 43.825 36.960 1.00 50.97 ? 1847 VAL B CA 1 ATOM 4305 C C . VAL B 2 311 ? 8.308 43.646 36.430 1.00 51.82 ? 1847 VAL B C 1 ATOM 4306 O O . VAL B 2 311 ? 7.971 44.092 35.334 1.00 51.80 ? 1847 VAL B O 1 ATOM 4307 C CB . VAL B 2 311 ? 10.380 45.055 36.336 1.00 51.84 ? 1847 VAL B CB 1 ATOM 4308 C CG1 . VAL B 2 311 ? 9.547 46.304 36.621 1.00 51.12 ? 1847 VAL B CG1 1 ATOM 4309 C CG2 . VAL B 2 311 ? 11.768 45.226 36.913 1.00 50.15 ? 1847 VAL B CG2 1 ATOM 4310 N N . GLY B 2 312 ? 7.528 42.905 37.206 1.00 51.52 ? 1848 GLY B N 1 ATOM 4311 C CA . GLY B 2 312 ? 6.149 42.582 36.889 1.00 52.11 ? 1848 GLY B CA 1 ATOM 4312 C C . GLY B 2 312 ? 5.401 43.312 35.799 1.00 54.10 ? 1848 GLY B C 1 ATOM 4313 O O . GLY B 2 312 ? 5.046 42.711 34.790 1.00 55.06 ? 1848 GLY B O 1 ATOM 4314 N N . GLU B 2 313 ? 5.139 44.598 35.993 1.00 55.76 ? 1849 GLU B N 1 ATOM 4315 C CA . GLU B 2 313 ? 4.380 45.356 35.006 1.00 58.35 ? 1849 GLU B CA 1 ATOM 4316 C C . GLU B 2 313 ? 4.945 45.271 33.591 1.00 58.64 ? 1849 GLU B C 1 ATOM 4317 O O . GLU B 2 313 ? 4.187 45.202 32.626 1.00 58.58 ? 1849 GLU B O 1 ATOM 4318 C CB . GLU B 2 313 ? 4.264 46.823 35.444 1.00 60.46 ? 1849 GLU B CB 1 ATOM 4319 C CG . GLU B 2 313 ? 3.244 47.063 36.562 1.00 63.88 ? 1849 GLU B CG 1 ATOM 4320 C CD . GLU B 2 313 ? 3.491 48.362 37.331 1.00 65.27 ? 1849 GLU B CD 1 ATOM 4321 O OE1 . GLU B 2 313 ? 3.601 49.434 36.688 1.00 65.06 ? 1849 GLU B OE1 1 ATOM 4322 O OE2 . GLU B 2 313 ? 3.569 48.302 38.580 1.00 62.26 ? 1849 GLU B OE2 1 ATOM 4323 N N . ILE B 2 314 ? 6.272 45.277 33.478 1.00 58.66 ? 1850 ILE B N 1 ATOM 4324 C CA . ILE B 2 314 ? 6.951 45.212 32.186 1.00 56.90 ? 1850 ILE B CA 1 ATOM 4325 C C . ILE B 2 314 ? 6.936 43.791 31.616 1.00 54.50 ? 1850 ILE B C 1 ATOM 4326 O O . ILE B 2 314 ? 6.648 43.586 30.444 1.00 52.96 ? 1850 ILE B O 1 ATOM 4327 C CB . ILE B 2 314 ? 8.415 45.704 32.316 1.00 58.28 ? 1850 ILE B CB 1 ATOM 4328 C CG1 . ILE B 2 314 ? 8.432 47.119 32.896 1.00 60.54 ? 1850 ILE B CG1 1 ATOM 4329 C CG2 . ILE B 2 314 ? 9.089 45.733 30.954 1.00 60.04 ? 1850 ILE B CG2 1 ATOM 4330 C CD1 . ILE B 2 314 ? 9.829 47.684 33.136 1.00 59.70 ? 1850 ILE B CD1 1 ATOM 4331 N N . GLN B 2 315 ? 7.236 42.815 32.461 1.00 54.07 ? 1851 GLN B N 1 ATOM 4332 C CA . GLN B 2 315 ? 7.258 41.429 32.048 1.00 52.89 ? 1851 GLN B CA 1 ATOM 4333 C C . GLN B 2 315 ? 5.959 41.044 31.372 1.00 55.90 ? 1851 GLN B C 1 ATOM 4334 O O . GLN B 2 315 ? 5.969 40.455 30.292 1.00 57.04 ? 1851 GLN B O 1 ATOM 4335 C CB . GLN B 2 315 ? 7.490 40.533 33.247 1.00 49.73 ? 1851 GLN B CB 1 ATOM 4336 C CG . GLN B 2 315 ? 7.970 39.136 32.881 1.00 45.07 ? 1851 GLN B CG 1 ATOM 4337 C CD . GLN B 2 315 ? 6.928 38.074 33.128 1.00 43.14 ? 1851 GLN B CD 1 ATOM 4338 O OE1 . GLN B 2 315 ? 7.245 36.958 33.566 1.00 32.95 ? 1851 GLN B OE1 1 ATOM 4339 N NE2 . GLN B 2 315 ? 5.669 38.409 32.839 1.00 44.89 ? 1851 GLN B NE2 1 ATOM 4340 N N . ARG B 2 316 ? 4.832 41.383 31.985 1.00 57.77 ? 1852 ARG B N 1 ATOM 4341 C CA . ARG B 2 316 ? 3.548 41.038 31.379 1.00 58.34 ? 1852 ARG B CA 1 ATOM 4342 C C . ARG B 2 316 ? 3.282 41.793 30.073 1.00 54.99 ? 1852 ARG B C 1 ATOM 4343 O O . ARG B 2 316 ? 2.468 41.357 29.263 1.00 58.08 ? 1852 ARG B O 1 ATOM 4344 C CB . ARG B 2 316 ? 2.399 41.248 32.377 1.00 61.82 ? 1852 ARG B CB 1 ATOM 4345 C CG . ARG B 2 316 ? 2.217 42.668 32.871 1.00 70.79 ? 1852 ARG B CG 1 ATOM 4346 C CD . ARG B 2 316 ? 1.243 43.457 31.999 1.00 76.50 ? 1852 ARG B CD 1 ATOM 4347 N NE . ARG B 2 316 ? -0.125 42.949 32.093 1.00 79.91 ? 1852 ARG B NE 1 ATOM 4348 C CZ . ARG B 2 316 ? -1.168 43.483 31.462 1.00 82.18 ? 1852 ARG B CZ 1 ATOM 4349 N NH1 . ARG B 2 316 ? -1.000 44.547 30.683 1.00 84.08 ? 1852 ARG B NH1 1 ATOM 4350 N NH2 . ARG B 2 316 ? -2.379 42.956 31.612 1.00 82.13 ? 1852 ARG B NH2 1 ATOM 4351 N N . ALA B 2 317 ? 3.975 42.907 29.856 1.00 50.33 ? 1853 ALA B N 1 ATOM 4352 C CA . ALA B 2 317 ? 3.796 43.680 28.625 1.00 47.13 ? 1853 ALA B CA 1 ATOM 4353 C C . ALA B 2 317 ? 4.524 43.005 27.465 1.00 46.44 ? 1853 ALA B C 1 ATOM 4354 O O . ALA B 2 317 ? 4.418 43.440 26.322 1.00 45.99 ? 1853 ALA B O 1 ATOM 4355 C CB . ALA B 2 317 ? 4.322 45.091 28.810 1.00 43.07 ? 1853 ALA B CB 1 ATOM 4356 N N . GLY B 2 318 ? 5.290 41.961 27.774 1.00 45.69 ? 1854 GLY B N 1 ATOM 4357 C CA . GLY B 2 318 ? 6.000 41.241 26.737 1.00 45.20 ? 1854 GLY B CA 1 ATOM 4358 C C . GLY B 2 318 ? 7.478 40.954 26.944 1.00 45.76 ? 1854 GLY B C 1 ATOM 4359 O O . GLY B 2 318 ? 8.034 40.112 26.245 1.00 44.93 ? 1854 GLY B O 1 ATOM 4360 N N . MET B 2 319 ? 8.136 41.619 27.887 1.00 44.45 ? 1855 MET B N 1 ATOM 4361 C CA . MET B 2 319 ? 9.559 41.363 28.054 1.00 40.61 ? 1855 MET B CA 1 ATOM 4362 C C . MET B 2 319 ? 9.797 39.989 28.625 1.00 40.28 ? 1855 MET B C 1 ATOM 4363 O O . MET B 2 319 ? 10.169 39.833 29.799 1.00 37.94 ? 1855 MET B O 1 ATOM 4364 C CB . MET B 2 319 ? 10.221 42.424 28.930 1.00 39.77 ? 1855 MET B CB 1 ATOM 4365 C CG . MET B 2 319 ? 11.750 42.353 28.884 1.00 37.81 ? 1855 MET B CG 1 ATOM 4366 S SD . MET B 2 319 ? 12.577 43.845 29.517 1.00 38.42 ? 1855 MET B SD 1 ATOM 4367 C CE . MET B 2 319 ? 11.991 45.081 28.365 1.00 20.05 ? 1855 MET B CE 1 ATOM 4368 N N . GLN B 2 320 ? 9.606 38.986 27.768 1.00 39.50 ? 1856 GLN B N 1 ATOM 4369 C CA . GLN B 2 320 ? 9.775 37.585 28.168 1.00 37.93 ? 1856 GLN B CA 1 ATOM 4370 C C . GLN B 2 320 ? 9.847 36.690 26.946 1.00 36.19 ? 1856 GLN B C 1 ATOM 4371 O O . GLN B 2 320 ? 9.337 37.046 25.884 1.00 37.98 ? 1856 GLN B O 1 ATOM 4372 C CB . GLN B 2 320 ? 8.590 37.151 29.046 1.00 35.29 ? 1856 GLN B CB 1 ATOM 4373 C CG . GLN B 2 320 ? 7.249 37.504 28.426 1.00 35.01 ? 1856 GLN B CG 1 ATOM 4374 C CD . GLN B 2 320 ? 6.080 36.952 29.187 1.00 33.28 ? 1856 GLN B CD 1 ATOM 4375 O OE1 . GLN B 2 320 ? 6.062 35.788 29.522 1.00 37.91 ? 1856 GLN B OE1 1 ATOM 4376 N NE2 . GLN B 2 320 ? 5.085 37.788 29.452 1.00 37.79 ? 1856 GLN B NE2 1 ATOM 4377 N N . THR B 2 321 ? 10.469 35.527 27.096 1.00 34.12 ? 1857 THR B N 1 ATOM 4378 C CA . THR B 2 321 ? 10.586 34.587 25.987 1.00 35.92 ? 1857 THR B CA 1 ATOM 4379 C C . THR B 2 321 ? 10.928 33.196 26.482 1.00 37.63 ? 1857 THR B C 1 ATOM 4380 O O . THR B 2 321 ? 11.621 33.028 27.474 1.00 37.34 ? 1857 THR B O 1 ATOM 4381 C CB . THR B 2 321 ? 11.701 34.990 24.993 1.00 36.31 ? 1857 THR B CB 1 ATOM 4382 O OG1 . THR B 2 321 ? 11.645 34.146 23.837 1.00 39.33 ? 1857 THR B OG1 1 ATOM 4383 C CG2 . THR B 2 321 ? 13.067 34.811 25.633 1.00 36.65 ? 1857 THR B CG2 1 ATOM 4384 N N . PRO B 2 322 ? 10.430 32.167 25.803 1.00 37.38 ? 1858 PRO B N 1 ATOM 4385 C CA . PRO B 2 322 ? 10.817 30.861 26.332 1.00 37.21 ? 1858 PRO B CA 1 ATOM 4386 C C . PRO B 2 322 ? 12.230 30.585 25.813 1.00 37.89 ? 1858 PRO B C 1 ATOM 4387 O O . PRO B 2 322 ? 12.654 31.194 24.831 1.00 39.34 ? 1858 PRO B O 1 ATOM 4388 C CB . PRO B 2 322 ? 9.790 29.915 25.712 1.00 39.22 ? 1858 PRO B CB 1 ATOM 4389 C CG . PRO B 2 322 ? 8.616 30.804 25.407 1.00 41.42 ? 1858 PRO B CG 1 ATOM 4390 C CD . PRO B 2 322 ? 9.267 32.069 24.910 1.00 36.99 ? 1858 PRO B CD 1 ATOM 4391 N N . PHE B 2 323 ? 12.971 29.708 26.483 1.00 37.03 ? 1859 PHE B N 1 ATOM 4392 C CA . PHE B 2 323 ? 14.303 29.337 26.033 1.00 36.94 ? 1859 PHE B CA 1 ATOM 4393 C C . PHE B 2 323 ? 14.451 27.846 26.323 1.00 38.18 ? 1859 PHE B C 1 ATOM 4394 O O . PHE B 2 323 ? 14.088 27.370 27.394 1.00 37.99 ? 1859 PHE B O 1 ATOM 4395 C CB . PHE B 2 323 ? 15.381 30.182 26.707 1.00 34.29 ? 1859 PHE B CB 1 ATOM 4396 C CG . PHE B 2 323 ? 15.695 29.790 28.113 1.00 37.21 ? 1859 PHE B CG 1 ATOM 4397 C CD1 . PHE B 2 323 ? 16.525 28.705 28.381 1.00 37.88 ? 1859 PHE B CD1 1 ATOM 4398 C CD2 . PHE B 2 323 ? 15.250 30.567 29.178 1.00 37.81 ? 1859 PHE B CD2 1 ATOM 4399 C CE1 . PHE B 2 323 ? 16.917 28.408 29.691 1.00 37.79 ? 1859 PHE B CE1 1 ATOM 4400 C CE2 . PHE B 2 323 ? 15.640 30.272 30.481 1.00 37.62 ? 1859 PHE B CE2 1 ATOM 4401 C CZ . PHE B 2 323 ? 16.476 29.192 30.734 1.00 35.60 ? 1859 PHE B CZ 1 ATOM 4402 N N . LEU B 2 324 ? 14.981 27.114 25.347 1.00 38.40 ? 1860 LEU B N 1 ATOM 4403 C CA . LEU B 2 324 ? 15.104 25.671 25.436 1.00 37.72 ? 1860 LEU B CA 1 ATOM 4404 C C . LEU B 2 324 ? 16.423 25.092 25.901 1.00 37.99 ? 1860 LEU B C 1 ATOM 4405 O O . LEU B 2 324 ? 17.485 25.483 25.417 1.00 38.83 ? 1860 LEU B O 1 ATOM 4406 C CB . LEU B 2 324 ? 14.757 25.083 24.073 1.00 37.10 ? 1860 LEU B CB 1 ATOM 4407 C CG . LEU B 2 324 ? 14.769 23.577 23.886 1.00 35.94 ? 1860 LEU B CG 1 ATOM 4408 C CD1 . LEU B 2 324 ? 13.676 22.960 24.747 1.00 37.05 ? 1860 LEU B CD1 1 ATOM 4409 C CD2 . LEU B 2 324 ? 14.541 23.263 22.408 1.00 35.37 ? 1860 LEU B CD2 1 ATOM 4410 N N . ILE B 2 325 ? 16.333 24.149 26.842 1.00 37.19 ? 1861 ILE B N 1 ATOM 4411 C CA . ILE B 2 325 ? 17.490 23.432 27.372 1.00 35.35 ? 1861 ILE B CA 1 ATOM 4412 C C . ILE B 2 325 ? 17.300 21.990 26.936 1.00 37.03 ? 1861 ILE B C 1 ATOM 4413 O O . ILE B 2 325 ? 16.314 21.352 27.310 1.00 36.07 ? 1861 ILE B O 1 ATOM 4414 C CB . ILE B 2 325 ? 17.548 23.437 28.902 1.00 36.42 ? 1861 ILE B CB 1 ATOM 4415 C CG1 . ILE B 2 325 ? 17.632 24.873 29.422 1.00 32.02 ? 1861 ILE B CG1 1 ATOM 4416 C CG2 . ILE B 2 325 ? 18.727 22.568 29.377 1.00 33.25 ? 1861 ILE B CG2 1 ATOM 4417 C CD1 . ILE B 2 325 ? 18.016 24.951 30.879 1.00 28.03 ? 1861 ILE B CD1 1 ATOM 4418 N N . VAL B 2 326 ? 18.254 21.494 26.150 1.00 39.85 ? 1862 VAL B N 1 ATOM 4419 C CA . VAL B 2 326 ? 18.252 20.139 25.586 1.00 41.37 ? 1862 VAL B CA 1 ATOM 4420 C C . VAL B 2 326 ? 18.849 19.104 26.527 1.00 42.66 ? 1862 VAL B C 1 ATOM 4421 O O . VAL B 2 326 ? 19.667 19.444 27.378 1.00 44.24 ? 1862 VAL B O 1 ATOM 4422 C CB . VAL B 2 326 ? 19.061 20.131 24.265 1.00 43.48 ? 1862 VAL B CB 1 ATOM 4423 C CG1 . VAL B 2 326 ? 19.061 18.746 23.640 1.00 45.30 ? 1862 VAL B CG1 1 ATOM 4424 C CG2 . VAL B 2 326 ? 18.468 21.156 23.291 1.00 44.28 ? 1862 VAL B CG2 1 ATOM 4425 N N . ASP B 2 327 ? 18.437 17.844 26.386 1.00 44.61 ? 1863 ASP B N 1 ATOM 4426 C CA . ASP B 2 327 ? 18.973 16.767 27.231 1.00 45.31 ? 1863 ASP B CA 1 ATOM 4427 C C . ASP B 2 327 ? 20.491 16.702 27.013 1.00 45.37 ? 1863 ASP B C 1 ATOM 4428 O O . ASP B 2 327 ? 20.968 16.919 25.916 1.00 43.28 ? 1863 ASP B O 1 ATOM 4429 C CB . ASP B 2 327 ? 18.350 15.403 26.862 1.00 47.11 ? 1863 ASP B CB 1 ATOM 4430 C CG . ASP B 2 327 ? 16.861 15.287 27.233 1.00 47.24 ? 1863 ASP B CG 1 ATOM 4431 O OD1 . ASP B 2 327 ? 16.341 16.126 27.993 1.00 47.06 ? 1863 ASP B OD1 1 ATOM 4432 O OD2 . ASP B 2 327 ? 16.209 14.326 26.769 1.00 44.62 ? 1863 ASP B OD2 1 ATOM 4433 N N . ARG B 2 328 ? 21.246 16.395 28.056 1.00 49.63 ? 1864 ARG B N 1 ATOM 4434 C CA . ARG B 2 328 ? 22.706 16.333 27.944 1.00 53.57 ? 1864 ARG B CA 1 ATOM 4435 C C . ARG B 2 328 ? 23.206 15.358 26.889 1.00 51.93 ? 1864 ARG B C 1 ATOM 4436 O O . ARG B 2 328 ? 24.135 15.667 26.154 1.00 52.85 ? 1864 ARG B O 1 ATOM 4437 C CB . ARG B 2 328 ? 23.337 15.982 29.300 1.00 57.42 ? 1864 ARG B CB 1 ATOM 4438 C CG . ARG B 2 328 ? 24.857 16.096 29.343 1.00 62.23 ? 1864 ARG B CG 1 ATOM 4439 C CD . ARG B 2 328 ? 25.376 15.815 30.752 1.00 68.71 ? 1864 ARG B CD 1 ATOM 4440 N NE . ARG B 2 328 ? 26.815 16.060 30.887 1.00 73.79 ? 1864 ARG B NE 1 ATOM 4441 C CZ . ARG B 2 328 ? 27.495 15.975 32.033 1.00 75.34 ? 1864 ARG B CZ 1 ATOM 4442 N NH1 . ARG B 2 328 ? 26.875 15.649 33.161 1.00 76.58 ? 1864 ARG B NH1 1 ATOM 4443 N NH2 . ARG B 2 328 ? 28.800 16.216 32.054 1.00 75.53 ? 1864 ARG B NH2 1 ATOM 4444 N N . GLU B 2 329 ? 22.595 14.184 26.810 1.00 53.34 ? 1865 GLU B N 1 ATOM 4445 C CA . GLU B 2 329 ? 23.013 13.175 25.839 1.00 54.51 ? 1865 GLU B CA 1 ATOM 4446 C C . GLU B 2 329 ? 21.983 13.008 24.732 1.00 52.97 ? 1865 GLU B C 1 ATOM 4447 O O . GLU B 2 329 ? 21.439 11.928 24.529 1.00 52.37 ? 1865 GLU B O 1 ATOM 4448 C CB . GLU B 2 329 ? 23.256 11.839 26.544 1.00 53.86 ? 1865 GLU B CB 1 ATOM 4449 C CG . GLU B 2 329 ? 24.389 11.887 27.530 1.00 63.05 ? 1865 GLU B CG 1 ATOM 4450 C CD . GLU B 2 329 ? 24.491 10.623 28.366 1.00 73.04 ? 1865 GLU B CD 1 ATOM 4451 O OE1 . GLU B 2 329 ? 24.751 9.540 27.781 1.00 77.29 ? 1865 GLU B OE1 1 ATOM 4452 O OE2 . GLU B 2 329 ? 24.305 10.705 29.610 1.00 74.56 ? 1865 GLU B OE2 1 ATOM 4453 N N . CYS B 2 330 ? 21.716 14.095 24.023 1.00 51.88 ? 1866 CYS B N 1 ATOM 4454 C CA . CYS B 2 330 ? 20.759 14.071 22.933 1.00 51.95 ? 1866 CYS B CA 1 ATOM 4455 C C . CYS B 2 330 ? 21.550 13.859 21.642 1.00 54.26 ? 1866 CYS B C 1 ATOM 4456 O O . CYS B 2 330 ? 22.173 14.789 21.104 1.00 51.38 ? 1866 CYS B O 1 ATOM 4457 C CB . CYS B 2 330 ? 19.973 15.386 22.912 1.00 48.67 ? 1866 CYS B CB 1 ATOM 4458 S SG . CYS B 2 330 ? 18.799 15.608 21.541 1.00 46.78 ? 1866 CYS B SG 1 ATOM 4459 N N . LYS B 2 331 ? 21.542 12.610 21.173 1.00 55.37 ? 1867 LYS B N 1 ATOM 4460 C CA . LYS B 2 331 ? 22.259 12.223 19.964 1.00 56.72 ? 1867 LYS B CA 1 ATOM 4461 C C . LYS B 2 331 ? 21.969 10.754 19.660 1.00 54.98 ? 1867 LYS B C 1 ATOM 4462 O O . LYS B 2 331 ? 22.797 10.031 19.117 1.00 57.16 ? 1867 LYS B O 1 ATOM 4463 C CB . LYS B 2 331 ? 23.767 12.443 20.162 1.00 58.97 ? 1867 LYS B CB 1 ATOM 4464 C CG . LYS B 2 331 ? 24.603 12.234 18.911 1.00 63.35 ? 1867 LYS B CG 1 ATOM 4465 C CD . LYS B 2 331 ? 26.044 12.706 19.096 1.00 67.40 ? 1867 LYS B CD 1 ATOM 4466 C CE . LYS B 2 331 ? 26.173 14.235 18.975 1.00 69.62 ? 1867 LYS B CE 1 ATOM 4467 N NZ . LYS B 2 331 ? 25.865 14.767 17.608 1.00 69.09 ? 1867 LYS B NZ 1 ATOM 4468 N N . MET B 2 332 ? 20.774 10.314 20.000 1.00 52.47 ? 1868 MET B N 1 ATOM 4469 C CA . MET B 2 332 ? 20.419 8.931 19.762 1.00 52.08 ? 1868 MET B CA 1 ATOM 4470 C C . MET B 2 332 ? 19.830 8.731 18.365 1.00 51.23 ? 1868 MET B C 1 ATOM 4471 O O . MET B 2 332 ? 19.192 9.628 17.824 1.00 51.61 ? 1868 MET B O 1 ATOM 4472 C CB . MET B 2 332 ? 19.451 8.468 20.857 1.00 51.11 ? 1868 MET B CB 1 ATOM 4473 C CG . MET B 2 332 ? 18.165 9.250 20.944 1.00 52.18 ? 1868 MET B CG 1 ATOM 4474 S SD . MET B 2 332 ? 17.277 8.873 22.480 1.00 51.41 ? 1868 MET B SD 1 ATOM 4475 C CE . MET B 2 332 ? 17.886 10.201 23.531 1.00 56.41 ? 1868 MET B CE 1 ATOM 4476 N N . PRO B 2 333 ? 20.052 7.549 17.756 1.00 50.58 ? 1869 PRO B N 1 ATOM 4477 C CA . PRO B 2 333 ? 19.538 7.252 16.415 1.00 49.51 ? 1869 PRO B CA 1 ATOM 4478 C C . PRO B 2 333 ? 18.066 7.547 16.299 1.00 48.81 ? 1869 PRO B C 1 ATOM 4479 O O . PRO B 2 333 ? 17.276 7.043 17.077 1.00 49.23 ? 1869 PRO B O 1 ATOM 4480 C CB . PRO B 2 333 ? 19.852 5.772 16.249 1.00 48.54 ? 1869 PRO B CB 1 ATOM 4481 C CG . PRO B 2 333 ? 21.134 5.645 16.984 1.00 50.34 ? 1869 PRO B CG 1 ATOM 4482 C CD . PRO B 2 333 ? 20.844 6.414 18.257 1.00 48.99 ? 1869 PRO B CD 1 ATOM 4483 N N . MET B 2 334 ? 17.710 8.364 15.313 1.00 51.03 ? 1870 MET B N 1 ATOM 4484 C CA . MET B 2 334 ? 16.328 8.762 15.085 1.00 51.37 ? 1870 MET B CA 1 ATOM 4485 C C . MET B 2 334 ? 15.494 7.607 14.504 1.00 51.16 ? 1870 MET B C 1 ATOM 4486 O O . MET B 2 334 ? 14.261 7.664 14.476 1.00 51.86 ? 1870 MET B O 1 ATOM 4487 C CB . MET B 2 334 ? 16.299 10.001 14.181 1.00 51.33 ? 1870 MET B CB 1 ATOM 4488 C CG . MET B 2 334 ? 15.166 10.973 14.497 1.00 57.00 ? 1870 MET B CG 1 ATOM 4489 S SD . MET B 2 334 ? 15.319 12.663 13.764 1.00 61.77 ? 1870 MET B SD 1 ATOM 4490 C CE . MET B 2 334 ? 16.031 13.567 15.162 1.00 58.49 ? 1870 MET B CE 1 ATOM 4491 N N . GLY B 2 335 ? 16.155 6.556 14.039 1.00 48.53 ? 1871 GLY B N 1 ATOM 4492 C CA . GLY B 2 335 ? 15.393 5.429 13.545 1.00 50.52 ? 1871 GLY B CA 1 ATOM 4493 C C . GLY B 2 335 ? 15.598 4.912 12.135 1.00 50.56 ? 1871 GLY B C 1 ATOM 4494 O O . GLY B 2 335 ? 14.927 3.968 11.731 1.00 51.57 ? 1871 GLY B O 1 ATOM 4495 N N . LEU B 2 336 ? 16.497 5.514 11.371 1.00 49.67 ? 1872 LEU B N 1 ATOM 4496 C CA . LEU B 2 336 ? 16.730 5.041 10.016 1.00 47.72 ? 1872 LEU B CA 1 ATOM 4497 C C . LEU B 2 336 ? 17.456 3.685 10.000 1.00 47.30 ? 1872 LEU B C 1 ATOM 4498 O O . LEU B 2 336 ? 17.129 2.805 9.201 1.00 46.17 ? 1872 LEU B O 1 ATOM 4499 C CB . LEU B 2 336 ? 17.537 6.083 9.230 1.00 44.33 ? 1872 LEU B CB 1 ATOM 4500 C CG . LEU B 2 336 ? 16.694 7.195 8.610 1.00 46.38 ? 1872 LEU B CG 1 ATOM 4501 C CD1 . LEU B 2 336 ? 17.565 8.255 8.030 1.00 44.29 ? 1872 LEU B CD1 1 ATOM 4502 C CD2 . LEU B 2 336 ? 15.819 6.624 7.526 1.00 46.19 ? 1872 LEU B CD2 1 ATOM 4503 N N . SER B 2 337 ? 18.418 3.517 10.905 1.00 45.86 ? 1873 SER B N 1 ATOM 4504 C CA . SER B 2 337 ? 19.220 2.308 10.968 1.00 44.86 ? 1873 SER B CA 1 ATOM 4505 C C . SER B 2 337 ? 18.686 1.209 11.881 1.00 46.90 ? 1873 SER B C 1 ATOM 4506 O O . SER B 2 337 ? 19.265 0.129 11.944 1.00 47.61 ? 1873 SER B O 1 ATOM 4507 C CB . SER B 2 337 ? 20.625 2.664 11.420 1.00 41.86 ? 1873 SER B CB 1 ATOM 4508 O OG . SER B 2 337 ? 20.624 2.977 12.801 1.00 38.29 ? 1873 SER B OG 1 ATOM 4509 N N . THR B 2 338 ? 17.595 1.478 12.588 1.00 47.15 ? 1874 THR B N 1 ATOM 4510 C CA . THR B 2 338 ? 17.034 0.489 13.496 1.00 46.73 ? 1874 THR B CA 1 ATOM 4511 C C . THR B 2 338 ? 15.614 0.066 13.151 1.00 46.98 ? 1874 THR B C 1 ATOM 4512 O O . THR B 2 338 ? 15.060 -0.826 13.791 1.00 49.55 ? 1874 THR B O 1 ATOM 4513 C CB . THR B 2 338 ? 17.014 1.008 14.923 1.00 46.50 ? 1874 THR B CB 1 ATOM 4514 O OG1 . THR B 2 338 ? 16.124 2.128 15.000 1.00 50.41 ? 1874 THR B OG1 1 ATOM 4515 C CG2 . THR B 2 338 ? 18.400 1.421 15.349 1.00 47.21 ? 1874 THR B CG2 1 ATOM 4516 N N . GLY B 2 339 ? 15.018 0.702 12.152 1.00 45.45 ? 1875 GLY B N 1 ATOM 4517 C CA . GLY B 2 339 ? 13.668 0.339 11.774 1.00 43.72 ? 1875 GLY B CA 1 ATOM 4518 C C . GLY B 2 339 ? 12.569 1.237 12.308 1.00 45.34 ? 1875 GLY B C 1 ATOM 4519 O O . GLY B 2 339 ? 11.430 1.138 11.854 1.00 45.45 ? 1875 GLY B O 1 ATOM 4520 N N . LEU B 2 340 ? 12.901 2.117 13.255 1.00 45.59 ? 1876 LEU B N 1 ATOM 4521 C CA . LEU B 2 340 ? 11.919 3.026 13.844 1.00 44.17 ? 1876 LEU B CA 1 ATOM 4522 C C . LEU B 2 340 ? 11.302 3.953 12.797 1.00 45.01 ? 1876 LEU B C 1 ATOM 4523 O O . LEU B 2 340 ? 10.122 4.303 12.890 1.00 47.44 ? 1876 LEU B O 1 ATOM 4524 C CB . LEU B 2 340 ? 12.564 3.843 14.970 1.00 43.07 ? 1876 LEU B CB 1 ATOM 4525 C CG . LEU B 2 340 ? 13.077 3.069 16.195 1.00 43.42 ? 1876 LEU B CG 1 ATOM 4526 C CD1 . LEU B 2 340 ? 14.125 3.910 16.928 1.00 46.56 ? 1876 LEU B CD1 1 ATOM 4527 C CD2 . LEU B 2 340 ? 11.934 2.713 17.125 1.00 37.65 ? 1876 LEU B CD2 1 ATOM 4528 N N . ILE B 2 341 ? 12.092 4.353 11.803 1.00 42.71 ? 1877 ILE B N 1 ATOM 4529 C CA . ILE B 2 341 ? 11.591 5.220 10.740 1.00 41.46 ? 1877 ILE B CA 1 ATOM 4530 C C . ILE B 2 341 ? 11.153 4.321 9.566 1.00 42.40 ? 1877 ILE B C 1 ATOM 4531 O O . ILE B 2 341 ? 11.970 3.610 8.976 1.00 41.38 ? 1877 ILE B O 1 ATOM 4532 C CB . ILE B 2 341 ? 12.688 6.216 10.288 1.00 39.75 ? 1877 ILE B CB 1 ATOM 4533 C CG1 . ILE B 2 341 ? 13.034 7.164 11.443 1.00 37.37 ? 1877 ILE B CG1 1 ATOM 4534 C CG2 . ILE B 2 341 ? 12.217 7.005 9.068 1.00 39.82 ? 1877 ILE B CG2 1 ATOM 4535 C CD1 . ILE B 2 341 ? 14.002 8.300 11.066 1.00 31.90 ? 1877 ILE B CD1 1 ATOM 4536 N N . ALA B 2 342 ? 9.865 4.345 9.239 1.00 42.70 ? 1878 ALA B N 1 ATOM 4537 C CA . ALA B 2 342 ? 9.328 3.499 8.166 1.00 46.55 ? 1878 ALA B CA 1 ATOM 4538 C C . ALA B 2 342 ? 9.692 3.927 6.738 1.00 48.62 ? 1878 ALA B C 1 ATOM 4539 O O . ALA B 2 342 ? 9.942 5.104 6.481 1.00 49.36 ? 1878 ALA B O 1 ATOM 4540 C CB . ALA B 2 342 ? 7.814 3.399 8.302 1.00 43.96 ? 1878 ALA B CB 1 ATOM 4541 N N . ASP B 2 343 ? 9.713 2.960 5.819 1.00 49.94 ? 1879 ASP B N 1 ATOM 4542 C CA . ASP B 2 343 ? 10.029 3.227 4.412 1.00 52.60 ? 1879 ASP B CA 1 ATOM 4543 C C . ASP B 2 343 ? 9.136 4.347 3.907 1.00 52.66 ? 1879 ASP B C 1 ATOM 4544 O O . ASP B 2 343 ? 9.532 5.145 3.052 1.00 52.88 ? 1879 ASP B O 1 ATOM 4545 C CB . ASP B 2 343 ? 9.786 1.991 3.527 1.00 56.38 ? 1879 ASP B CB 1 ATOM 4546 C CG . ASP B 2 343 ? 10.630 0.789 3.929 1.00 61.29 ? 1879 ASP B CG 1 ATOM 4547 O OD1 . ASP B 2 343 ? 10.343 0.165 4.977 1.00 66.05 ? 1879 ASP B OD1 1 ATOM 4548 O OD2 . ASP B 2 343 ? 11.584 0.462 3.194 1.00 65.12 ? 1879 ASP B OD2 1 ATOM 4549 N N . SER B 2 344 ? 7.920 4.387 4.439 1.00 51.96 ? 1880 SER B N 1 ATOM 4550 C CA . SER B 2 344 ? 6.940 5.398 4.063 1.00 51.35 ? 1880 SER B CA 1 ATOM 4551 C C . SER B 2 344 ? 7.491 6.804 4.277 1.00 49.56 ? 1880 SER B C 1 ATOM 4552 O O . SER B 2 344 ? 7.342 7.673 3.429 1.00 51.05 ? 1880 SER B O 1 ATOM 4553 C CB . SER B 2 344 ? 5.676 5.227 4.907 1.00 54.06 ? 1880 SER B CB 1 ATOM 4554 O OG . SER B 2 344 ? 5.340 3.856 5.056 1.00 58.40 ? 1880 SER B OG 1 ATOM 4555 N N . GLN B 2 345 ? 8.148 7.010 5.413 1.00 46.80 ? 1881 GLN B N 1 ATOM 4556 C CA . GLN B 2 345 ? 8.694 8.312 5.772 1.00 44.40 ? 1881 GLN B CA 1 ATOM 4557 C C . GLN B 2 345 ? 9.899 8.804 4.965 1.00 44.76 ? 1881 GLN B C 1 ATOM 4558 O O . GLN B 2 345 ? 10.277 9.979 5.055 1.00 44.09 ? 1881 GLN B O 1 ATOM 4559 C CB . GLN B 2 345 ? 9.025 8.315 7.264 1.00 42.95 ? 1881 GLN B CB 1 ATOM 4560 C CG . GLN B 2 345 ? 7.814 8.226 8.192 1.00 41.03 ? 1881 GLN B CG 1 ATOM 4561 C CD . GLN B 2 345 ? 8.209 7.844 9.604 1.00 45.36 ? 1881 GLN B CD 1 ATOM 4562 O OE1 . GLN B 2 345 ? 8.189 6.670 9.971 1.00 45.52 ? 1881 GLN B OE1 1 ATOM 4563 N NE2 . GLN B 2 345 ? 8.598 8.836 10.401 1.00 46.93 ? 1881 GLN B NE2 1 ATOM 4564 N N . ILE B 2 346 ? 10.506 7.917 4.183 1.00 43.28 ? 1882 ILE B N 1 ATOM 4565 C CA . ILE B 2 346 ? 11.652 8.296 3.371 1.00 41.76 ? 1882 ILE B CA 1 ATOM 4566 C C . ILE B 2 346 ? 11.107 8.600 1.980 1.00 43.20 ? 1882 ILE B C 1 ATOM 4567 O O . ILE B 2 346 ? 10.168 7.954 1.535 1.00 44.31 ? 1882 ILE B O 1 ATOM 4568 C CB . ILE B 2 346 ? 12.689 7.155 3.339 1.00 39.93 ? 1882 ILE B CB 1 ATOM 4569 C CG1 . ILE B 2 346 ? 12.916 6.653 4.772 1.00 39.42 ? 1882 ILE B CG1 1 ATOM 4570 C CG2 . ILE B 2 346 ? 14.011 7.661 2.749 1.00 35.79 ? 1882 ILE B CG2 1 ATOM 4571 C CD1 . ILE B 2 346 ? 13.911 5.511 4.918 1.00 36.04 ? 1882 ILE B CD1 1 ATOM 4572 N N . GLN B 2 347 ? 11.684 9.589 1.305 1.00 45.30 ? 1883 GLN B N 1 ATOM 4573 C CA . GLN B 2 347 ? 11.218 10.005 -0.019 1.00 48.13 ? 1883 GLN B CA 1 ATOM 4574 C C . GLN B 2 347 ? 12.266 10.898 -0.711 1.00 48.25 ? 1883 GLN B C 1 ATOM 4575 O O . GLN B 2 347 ? 12.859 11.749 -0.076 1.00 48.87 ? 1883 GLN B O 1 ATOM 4576 C CB . GLN B 2 347 ? 9.903 10.765 0.163 1.00 50.24 ? 1883 GLN B CB 1 ATOM 4577 C CG . GLN B 2 347 ? 9.391 11.503 -1.051 1.00 59.18 ? 1883 GLN B CG 1 ATOM 4578 C CD . GLN B 2 347 ? 8.327 12.549 -0.703 1.00 62.54 ? 1883 GLN B CD 1 ATOM 4579 O OE1 . GLN B 2 347 ? 7.348 12.254 -0.012 1.00 63.94 ? 1883 GLN B OE1 1 ATOM 4580 N NE2 . GLN B 2 347 ? 8.515 13.773 -1.194 1.00 62.71 ? 1883 GLN B NE2 1 ATOM 4581 N N . ALA B 2 348 ? 12.502 10.709 -2.006 1.00 49.38 ? 1884 ALA B N 1 ATOM 4582 C CA . ALA B 2 348 ? 13.495 11.524 -2.711 1.00 49.57 ? 1884 ALA B CA 1 ATOM 4583 C C . ALA B 2 348 ? 12.896 12.211 -3.905 1.00 50.13 ? 1884 ALA B C 1 ATOM 4584 O O . ALA B 2 348 ? 11.738 11.987 -4.237 1.00 52.85 ? 1884 ALA B O 1 ATOM 4585 C CB . ALA B 2 348 ? 14.655 10.671 -3.175 1.00 49.25 ? 1884 ALA B CB 1 ATOM 4586 N N . SER B 2 349 ? 13.700 13.042 -4.556 1.00 49.38 ? 1885 SER B N 1 ATOM 4587 C CA . SER B 2 349 ? 13.264 13.768 -5.740 1.00 50.30 ? 1885 SER B CA 1 ATOM 4588 C C . SER B 2 349 ? 13.650 12.971 -6.982 1.00 51.72 ? 1885 SER B C 1 ATOM 4589 O O . SER B 2 349 ? 13.193 13.251 -8.091 1.00 51.95 ? 1885 SER B O 1 ATOM 4590 C CB . SER B 2 349 ? 13.946 15.120 -5.789 1.00 50.32 ? 1885 SER B CB 1 ATOM 4591 O OG . SER B 2 349 ? 15.344 14.930 -5.870 1.00 52.73 ? 1885 SER B OG 1 ATOM 4592 N N . GLU B 2 350 ? 14.517 11.987 -6.783 1.00 53.18 ? 1886 GLU B N 1 ATOM 4593 C CA . GLU B 2 350 ? 14.977 11.127 -7.859 1.00 54.24 ? 1886 GLU B CA 1 ATOM 4594 C C . GLU B 2 350 ? 15.970 10.106 -7.323 1.00 53.48 ? 1886 GLU B C 1 ATOM 4595 O O . GLU B 2 350 ? 16.605 10.310 -6.293 1.00 54.13 ? 1886 GLU B O 1 ATOM 4596 C CB . GLU B 2 350 ? 15.642 11.946 -8.957 1.00 55.18 ? 1886 GLU B CB 1 ATOM 4597 C CG . GLU B 2 350 ? 17.028 12.399 -8.602 1.00 59.45 ? 1886 GLU B CG 1 ATOM 4598 C CD . GLU B 2 350 ? 17.786 12.924 -9.798 1.00 61.47 ? 1886 GLU B CD 1 ATOM 4599 O OE1 . GLU B 2 350 ? 17.466 14.035 -10.272 1.00 61.60 ? 1886 GLU B OE1 1 ATOM 4600 O OE2 . GLU B 2 350 ? 18.702 12.212 -10.270 1.00 65.47 ? 1886 GLU B OE2 1 ATOM 4601 N N . PHE B 2 351 ? 16.111 9.012 -8.048 1.00 53.61 ? 1887 PHE B N 1 ATOM 4602 C CA . PHE B 2 351 ? 17.006 7.947 -7.654 1.00 55.10 ? 1887 PHE B CA 1 ATOM 4603 C C . PHE B 2 351 ? 17.401 7.138 -8.883 1.00 55.16 ? 1887 PHE B C 1 ATOM 4604 O O . PHE B 2 351 ? 16.573 6.832 -9.714 1.00 57.18 ? 1887 PHE B O 1 ATOM 4605 C CB . PHE B 2 351 ? 16.311 7.050 -6.636 1.00 55.71 ? 1887 PHE B CB 1 ATOM 4606 C CG . PHE B 2 351 ? 14.986 6.523 -7.105 1.00 58.22 ? 1887 PHE B CG 1 ATOM 4607 C CD1 . PHE B 2 351 ? 13.973 7.396 -7.507 1.00 58.22 ? 1887 PHE B CD1 1 ATOM 4608 C CD2 . PHE B 2 351 ? 14.743 5.157 -7.143 1.00 56.83 ? 1887 PHE B CD2 1 ATOM 4609 C CE1 . PHE B 2 351 ? 12.747 6.910 -7.938 1.00 57.13 ? 1887 PHE B CE1 1 ATOM 4610 C CE2 . PHE B 2 351 ? 13.516 4.669 -7.573 1.00 57.60 ? 1887 PHE B CE2 1 ATOM 4611 C CZ . PHE B 2 351 ? 12.521 5.541 -7.970 1.00 57.21 ? 1887 PHE B CZ 1 ATOM 4612 N N . TRP B 2 352 ? 18.678 6.803 -8.981 1.00 55.30 ? 1888 TRP B N 1 ATOM 4613 C CA . TRP B 2 352 ? 19.214 6.042 -10.093 1.00 55.25 ? 1888 TRP B CA 1 ATOM 4614 C C . TRP B 2 352 ? 18.759 4.596 -10.059 1.00 54.79 ? 1888 TRP B C 1 ATOM 4615 O O . TRP B 2 352 ? 19.196 3.824 -9.213 1.00 54.06 ? 1888 TRP B O 1 ATOM 4616 C CB . TRP B 2 352 ? 20.730 6.106 -10.034 1.00 59.06 ? 1888 TRP B CB 1 ATOM 4617 C CG . TRP B 2 352 ? 21.452 5.533 -11.196 1.00 59.47 ? 1888 TRP B CG 1 ATOM 4618 C CD1 . TRP B 2 352 ? 21.214 5.778 -12.516 1.00 59.57 ? 1888 TRP B CD1 1 ATOM 4619 C CD2 . TRP B 2 352 ? 22.627 4.725 -11.139 1.00 60.09 ? 1888 TRP B CD2 1 ATOM 4620 N NE1 . TRP B 2 352 ? 22.177 5.177 -13.287 1.00 61.86 ? 1888 TRP B NE1 1 ATOM 4621 C CE2 . TRP B 2 352 ? 23.058 4.522 -12.466 1.00 61.81 ? 1888 TRP B CE2 1 ATOM 4622 C CE3 . TRP B 2 352 ? 23.362 4.153 -10.093 1.00 60.75 ? 1888 TRP B CE3 1 ATOM 4623 C CZ2 . TRP B 2 352 ? 24.197 3.768 -12.776 1.00 63.05 ? 1888 TRP B CZ2 1 ATOM 4624 C CZ3 . TRP B 2 352 ? 24.494 3.400 -10.402 1.00 61.89 ? 1888 TRP B CZ3 1 ATOM 4625 C CH2 . TRP B 2 352 ? 24.900 3.216 -11.732 1.00 62.25 ? 1888 TRP B CH2 1 ATOM 4626 N N . GLY B 2 353 ? 17.882 4.251 -10.997 1.00 55.54 ? 1889 GLY B N 1 ATOM 4627 C CA . GLY B 2 353 ? 17.333 2.909 -11.128 1.00 55.47 ? 1889 GLY B CA 1 ATOM 4628 C C . GLY B 2 353 ? 17.713 1.799 -10.163 1.00 55.46 ? 1889 GLY B C 1 ATOM 4629 O O . GLY B 2 353 ? 18.778 1.192 -10.273 1.00 56.37 ? 1889 GLY B O 1 ATOM 4630 N N . TYR B 2 354 ? 16.803 1.523 -9.239 1.00 56.74 ? 1890 TYR B N 1 ATOM 4631 C CA . TYR B 2 354 ? 16.935 0.487 -8.213 1.00 58.97 ? 1890 TYR B CA 1 ATOM 4632 C C . TYR B 2 354 ? 17.611 0.879 -6.909 1.00 56.82 ? 1890 TYR B C 1 ATOM 4633 O O . TYR B 2 354 ? 17.478 0.167 -5.913 1.00 56.84 ? 1890 TYR B O 1 ATOM 4634 C CB . TYR B 2 354 ? 17.557 -0.806 -8.762 1.00 63.18 ? 1890 TYR B CB 1 ATOM 4635 C CG . TYR B 2 354 ? 16.601 -1.966 -8.556 1.00 73.08 ? 1890 TYR B CG 1 ATOM 4636 C CD1 . TYR B 2 354 ? 15.885 -2.520 -9.631 1.00 76.85 ? 1890 TYR B CD1 1 ATOM 4637 C CD2 . TYR B 2 354 ? 16.277 -2.400 -7.257 1.00 77.70 ? 1890 TYR B CD2 1 ATOM 4638 C CE1 . TYR B 2 354 ? 14.855 -3.467 -9.413 1.00 79.95 ? 1890 TYR B CE1 1 ATOM 4639 C CE2 . TYR B 2 354 ? 15.250 -3.340 -7.026 1.00 79.19 ? 1890 TYR B CE2 1 ATOM 4640 C CZ . TYR B 2 354 ? 14.539 -3.863 -8.104 1.00 80.79 ? 1890 TYR B CZ 1 ATOM 4641 O OH . TYR B 2 354 ? 13.479 -4.721 -7.866 1.00 80.57 ? 1890 TYR B OH 1 ATOM 4642 N N . TRP B 2 355 ? 18.327 1.998 -6.900 1.00 53.38 ? 1891 TRP B N 1 ATOM 4643 C CA . TRP B 2 355 ? 18.936 2.481 -5.664 1.00 51.86 ? 1891 TRP B CA 1 ATOM 4644 C C . TRP B 2 355 ? 17.897 3.437 -5.045 1.00 51.11 ? 1891 TRP B C 1 ATOM 4645 O O . TRP B 2 355 ? 18.085 4.648 -4.960 1.00 48.80 ? 1891 TRP B O 1 ATOM 4646 C CB . TRP B 2 355 ? 20.244 3.217 -5.956 1.00 50.80 ? 1891 TRP B CB 1 ATOM 4647 C CG . TRP B 2 355 ? 21.322 2.324 -6.497 1.00 47.62 ? 1891 TRP B CG 1 ATOM 4648 C CD1 . TRP B 2 355 ? 21.664 2.141 -7.812 1.00 45.16 ? 1891 TRP B CD1 1 ATOM 4649 C CD2 . TRP B 2 355 ? 22.198 1.488 -5.737 1.00 44.05 ? 1891 TRP B CD2 1 ATOM 4650 N NE1 . TRP B 2 355 ? 22.700 1.246 -7.910 1.00 43.04 ? 1891 TRP B NE1 1 ATOM 4651 C CE2 . TRP B 2 355 ? 23.047 0.829 -6.653 1.00 43.22 ? 1891 TRP B CE2 1 ATOM 4652 C CE3 . TRP B 2 355 ? 22.349 1.233 -4.373 1.00 42.68 ? 1891 TRP B CE3 1 ATOM 4653 C CZ2 . TRP B 2 355 ? 24.032 -0.068 -6.245 1.00 42.09 ? 1891 TRP B CZ2 1 ATOM 4654 C CZ3 . TRP B 2 355 ? 23.331 0.338 -3.967 1.00 43.39 ? 1891 TRP B CZ3 1 ATOM 4655 C CH2 . TRP B 2 355 ? 24.160 -0.303 -4.901 1.00 41.42 ? 1891 TRP B CH2 1 ATOM 4656 N N . GLU B 2 356 ? 16.786 2.853 -4.623 1.00 50.99 ? 1892 GLU B N 1 ATOM 4657 C CA . GLU B 2 356 ? 15.668 3.580 -4.053 1.00 50.96 ? 1892 GLU B CA 1 ATOM 4658 C C . GLU B 2 356 ? 15.921 4.171 -2.667 1.00 50.32 ? 1892 GLU B C 1 ATOM 4659 O O . GLU B 2 356 ? 16.592 3.564 -1.842 1.00 49.03 ? 1892 GLU B O 1 ATOM 4660 C CB . GLU B 2 356 ? 14.463 2.645 -4.012 1.00 52.79 ? 1892 GLU B CB 1 ATOM 4661 C CG . GLU B 2 356 ? 13.944 2.271 -5.385 1.00 54.75 ? 1892 GLU B CG 1 ATOM 4662 C CD . GLU B 2 356 ? 13.033 1.074 -5.343 1.00 57.13 ? 1892 GLU B CD 1 ATOM 4663 O OE1 . GLU B 2 356 ? 12.460 0.805 -4.273 1.00 57.89 ? 1892 GLU B OE1 1 ATOM 4664 O OE2 . GLU B 2 356 ? 12.877 0.400 -6.376 1.00 57.98 ? 1892 GLU B OE2 1 ATOM 4665 N N . PRO B 2 357 ? 15.352 5.359 -2.396 1.00 49.01 ? 1893 PRO B N 1 ATOM 4666 C CA . PRO B 2 357 ? 15.480 6.087 -1.131 1.00 46.89 ? 1893 PRO B CA 1 ATOM 4667 C C . PRO B 2 357 ? 15.212 5.237 0.096 1.00 47.02 ? 1893 PRO B C 1 ATOM 4668 O O . PRO B 2 357 ? 15.885 5.361 1.119 1.00 46.52 ? 1893 PRO B O 1 ATOM 4669 C CB . PRO B 2 357 ? 14.473 7.220 -1.286 1.00 46.77 ? 1893 PRO B CB 1 ATOM 4670 C CG . PRO B 2 357 ? 14.523 7.499 -2.750 1.00 48.51 ? 1893 PRO B CG 1 ATOM 4671 C CD . PRO B 2 357 ? 14.514 6.116 -3.346 1.00 48.50 ? 1893 PRO B CD 1 ATOM 4672 N N . LYS B 2 358 ? 14.228 4.362 -0.005 1.00 48.65 ? 1894 LYS B N 1 ATOM 4673 C CA . LYS B 2 358 ? 13.875 3.497 1.115 1.00 50.16 ? 1894 LYS B CA 1 ATOM 4674 C C . LYS B 2 358 ? 15.085 2.696 1.599 1.00 49.63 ? 1894 LYS B C 1 ATOM 4675 O O . LYS B 2 358 ? 15.050 2.064 2.655 1.00 50.77 ? 1894 LYS B O 1 ATOM 4676 C CB . LYS B 2 358 ? 12.748 2.552 0.679 1.00 53.35 ? 1894 LYS B CB 1 ATOM 4677 C CG . LYS B 2 358 ? 11.386 3.257 0.464 1.00 58.73 ? 1894 LYS B CG 1 ATOM 4678 C CD . LYS B 2 358 ? 11.445 4.550 -0.397 1.00 55.87 ? 1894 LYS B CD 1 ATOM 4679 C CE . LYS B 2 358 ? 11.953 4.274 -1.814 1.00 57.99 ? 1894 LYS B CE 1 ATOM 4680 N NZ . LYS B 2 358 ? 11.852 5.475 -2.701 1.00 58.10 ? 1894 LYS B NZ 1 ATOM 4681 N N . LEU B 2 359 ? 16.162 2.759 0.826 1.00 48.13 ? 1895 LEU B N 1 ATOM 4682 C CA . LEU B 2 359 ? 17.387 2.030 1.107 1.00 44.91 ? 1895 LEU B CA 1 ATOM 4683 C C . LEU B 2 359 ? 18.469 2.782 1.886 1.00 44.66 ? 1895 LEU B C 1 ATOM 4684 O O . LEU B 2 359 ? 19.344 2.160 2.487 1.00 47.01 ? 1895 LEU B O 1 ATOM 4685 C CB . LEU B 2 359 ? 17.964 1.526 -0.215 1.00 41.79 ? 1895 LEU B CB 1 ATOM 4686 C CG . LEU B 2 359 ? 17.471 0.210 -0.855 1.00 43.56 ? 1895 LEU B CG 1 ATOM 4687 C CD1 . LEU B 2 359 ? 16.005 -0.076 -0.559 1.00 42.20 ? 1895 LEU B CD1 1 ATOM 4688 C CD2 . LEU B 2 359 ? 17.723 0.295 -2.356 1.00 40.58 ? 1895 LEU B CD2 1 ATOM 4689 N N . ALA B 2 360 ? 18.407 4.105 1.907 1.00 42.63 ? 1896 ALA B N 1 ATOM 4690 C CA . ALA B 2 360 ? 19.435 4.897 2.593 1.00 42.33 ? 1896 ALA B CA 1 ATOM 4691 C C . ALA B 2 360 ? 19.550 4.714 4.090 1.00 40.11 ? 1896 ALA B C 1 ATOM 4692 O O . ALA B 2 360 ? 19.451 5.677 4.816 1.00 42.34 ? 1896 ALA B O 1 ATOM 4693 C CB . ALA B 2 360 ? 19.235 6.376 2.291 1.00 41.81 ? 1896 ALA B CB 1 ATOM 4694 N N . ARG B 2 361 ? 19.796 3.502 4.559 1.00 39.32 ? 1897 ARG B N 1 ATOM 4695 C CA . ARG B 2 361 ? 19.901 3.273 5.994 1.00 40.87 ? 1897 ARG B CA 1 ATOM 4696 C C . ARG B 2 361 ? 21.291 2.807 6.453 1.00 42.58 ? 1897 ARG B C 1 ATOM 4697 O O . ARG B 2 361 ? 21.780 1.780 5.984 1.00 45.16 ? 1897 ARG B O 1 ATOM 4698 C CB . ARG B 2 361 ? 18.858 2.237 6.393 1.00 39.51 ? 1897 ARG B CB 1 ATOM 4699 C CG . ARG B 2 361 ? 17.466 2.626 5.989 1.00 37.15 ? 1897 ARG B CG 1 ATOM 4700 C CD . ARG B 2 361 ? 16.563 1.431 5.928 1.00 37.28 ? 1897 ARG B CD 1 ATOM 4701 N NE . ARG B 2 361 ? 15.183 1.838 5.719 1.00 38.32 ? 1897 ARG B NE 1 ATOM 4702 C CZ . ARG B 2 361 ? 14.396 2.270 6.696 1.00 40.16 ? 1897 ARG B CZ 1 ATOM 4703 N NH1 . ARG B 2 361 ? 14.862 2.335 7.935 1.00 33.87 ? 1897 ARG B NH1 1 ATOM 4704 N NH2 . ARG B 2 361 ? 13.153 2.651 6.433 1.00 42.76 ? 1897 ARG B NH2 1 ATOM 4705 N N . LEU B 2 362 ? 21.913 3.541 7.375 1.00 41.52 ? 1898 LEU B N 1 ATOM 4706 C CA . LEU B 2 362 ? 23.244 3.184 7.886 1.00 42.35 ? 1898 LEU B CA 1 ATOM 4707 C C . LEU B 2 362 ? 23.400 1.687 8.126 1.00 43.69 ? 1898 LEU B C 1 ATOM 4708 O O . LEU B 2 362 ? 22.605 1.059 8.819 1.00 45.25 ? 1898 LEU B O 1 ATOM 4709 C CB . LEU B 2 362 ? 23.551 3.942 9.194 1.00 43.05 ? 1898 LEU B CB 1 ATOM 4710 C CG . LEU B 2 362 ? 24.809 4.830 9.320 1.00 41.75 ? 1898 LEU B CG 1 ATOM 4711 C CD1 . LEU B 2 362 ? 25.889 4.141 10.094 1.00 40.57 ? 1898 LEU B CD1 1 ATOM 4712 C CD2 . LEU B 2 362 ? 25.306 5.205 7.945 1.00 42.28 ? 1898 LEU B CD2 1 ATOM 4713 N N . ASN B 2 363 ? 24.436 1.122 7.525 1.00 46.70 ? 1899 ASN B N 1 ATOM 4714 C CA . ASN B 2 363 ? 24.751 -0.294 7.641 1.00 49.53 ? 1899 ASN B CA 1 ATOM 4715 C C . ASN B 2 363 ? 23.908 -1.282 6.838 1.00 52.99 ? 1899 ASN B C 1 ATOM 4716 O O . ASN B 2 363 ? 24.387 -2.363 6.488 1.00 54.27 ? 1899 ASN B O 1 ATOM 4717 C CB . ASN B 2 363 ? 24.773 -0.682 9.105 1.00 45.29 ? 1899 ASN B CB 1 ATOM 4718 C CG . ASN B 2 363 ? 25.832 0.064 9.856 1.00 43.83 ? 1899 ASN B CG 1 ATOM 4719 O OD1 . ASN B 2 363 ? 26.976 0.123 9.414 1.00 44.72 ? 1899 ASN B OD1 1 ATOM 4720 N ND2 . ASN B 2 363 ? 25.466 0.650 10.991 1.00 44.14 ? 1899 ASN B ND2 1 ATOM 4721 N N . ASN B 2 364 ? 22.665 -0.930 6.536 1.00 57.07 ? 1900 ASN B N 1 ATOM 4722 C CA . ASN B 2 364 ? 21.826 -1.829 5.745 1.00 59.21 ? 1900 ASN B CA 1 ATOM 4723 C C . ASN B 2 364 ? 22.681 -2.400 4.617 1.00 60.32 ? 1900 ASN B C 1 ATOM 4724 O O . ASN B 2 364 ? 23.239 -1.649 3.818 1.00 60.29 ? 1900 ASN B O 1 ATOM 4725 C CB . ASN B 2 364 ? 20.617 -1.055 5.204 1.00 58.86 ? 1900 ASN B CB 1 ATOM 4726 C CG . ASN B 2 364 ? 20.161 -1.539 3.850 1.00 58.06 ? 1900 ASN B CG 1 ATOM 4727 O OD1 . ASN B 2 364 ? 20.677 -1.093 2.827 1.00 58.19 ? 1900 ASN B OD1 1 ATOM 4728 N ND2 . ASN B 2 364 ? 19.186 -2.454 3.831 1.00 56.94 ? 1900 ASN B ND2 1 ATOM 4729 N N . GLY B 2 365 ? 22.811 -3.726 4.574 1.00 61.52 ? 1901 GLY B N 1 ATOM 4730 C CA . GLY B 2 365 ? 23.628 -4.357 3.543 1.00 62.74 ? 1901 GLY B CA 1 ATOM 4731 C C . GLY B 2 365 ? 22.868 -5.089 2.453 1.00 62.90 ? 1901 GLY B C 1 ATOM 4732 O O . GLY B 2 365 ? 21.718 -5.476 2.654 1.00 63.44 ? 1901 GLY B O 1 ATOM 4733 N N . GLY B 2 366 ? 23.509 -5.284 1.298 1.00 63.29 ? 1902 GLY B N 1 ATOM 4734 C CA . GLY B 2 366 ? 22.859 -5.978 0.190 1.00 61.34 ? 1902 GLY B CA 1 ATOM 4735 C C . GLY B 2 366 ? 23.322 -5.530 -1.188 1.00 60.64 ? 1902 GLY B C 1 ATOM 4736 O O . GLY B 2 366 ? 24.171 -4.648 -1.305 1.00 61.58 ? 1902 GLY B O 1 ATOM 4737 N N . SER B 2 367 ? 22.770 -6.129 -2.239 1.00 58.70 ? 1903 SER B N 1 ATOM 4738 C CA . SER B 2 367 ? 23.167 -5.764 -3.596 1.00 57.25 ? 1903 SER B CA 1 ATOM 4739 C C . SER B 2 367 ? 22.780 -4.321 -3.826 1.00 55.01 ? 1903 SER B C 1 ATOM 4740 O O . SER B 2 367 ? 23.539 -3.534 -4.391 1.00 52.75 ? 1903 SER B O 1 ATOM 4741 C CB . SER B 2 367 ? 22.474 -6.664 -4.621 1.00 59.48 ? 1903 SER B CB 1 ATOM 4742 O OG . SER B 2 367 ? 22.860 -6.327 -5.943 1.00 58.50 ? 1903 SER B OG 1 ATOM 4743 N N . TYR B 2 368 ? 21.570 -3.997 -3.394 1.00 54.68 ? 1904 TYR B N 1 ATOM 4744 C CA . TYR B 2 368 ? 21.040 -2.645 -3.483 1.00 53.66 ? 1904 TYR B CA 1 ATOM 4745 C C . TYR B 2 368 ? 20.763 -2.267 -2.038 1.00 51.39 ? 1904 TYR B C 1 ATOM 4746 O O . TYR B 2 368 ? 19.731 -2.639 -1.464 1.00 53.16 ? 1904 TYR B O 1 ATOM 4747 C CB . TYR B 2 368 ? 19.761 -2.623 -4.307 1.00 54.33 ? 1904 TYR B CB 1 ATOM 4748 C CG . TYR B 2 368 ? 20.020 -2.873 -5.762 1.00 58.35 ? 1904 TYR B CG 1 ATOM 4749 C CD1 . TYR B 2 368 ? 20.166 -4.170 -6.257 1.00 59.60 ? 1904 TYR B CD1 1 ATOM 4750 C CD2 . TYR B 2 368 ? 20.175 -1.805 -6.648 1.00 61.18 ? 1904 TYR B CD2 1 ATOM 4751 C CE1 . TYR B 2 368 ? 20.465 -4.391 -7.611 1.00 62.07 ? 1904 TYR B CE1 1 ATOM 4752 C CE2 . TYR B 2 368 ? 20.474 -2.012 -7.996 1.00 61.70 ? 1904 TYR B CE2 1 ATOM 4753 C CZ . TYR B 2 368 ? 20.619 -3.302 -8.468 1.00 61.55 ? 1904 TYR B CZ 1 ATOM 4754 O OH . TYR B 2 368 ? 20.945 -3.493 -9.788 1.00 63.27 ? 1904 TYR B OH 1 ATOM 4755 N N . ASN B 2 369 ? 21.701 -1.541 -1.443 1.00 46.17 ? 1905 ASN B N 1 ATOM 4756 C CA . ASN B 2 369 ? 21.561 -1.178 -0.052 1.00 41.53 ? 1905 ASN B CA 1 ATOM 4757 C C . ASN B 2 369 ? 21.737 0.306 0.233 1.00 39.47 ? 1905 ASN B C 1 ATOM 4758 O O . ASN B 2 369 ? 22.139 0.675 1.329 1.00 38.75 ? 1905 ASN B O 1 ATOM 4759 C CB . ASN B 2 369 ? 22.568 -1.986 0.773 1.00 39.13 ? 1905 ASN B CB 1 ATOM 4760 C CG . ASN B 2 369 ? 24.025 -1.631 0.444 1.00 39.48 ? 1905 ASN B CG 1 ATOM 4761 O OD1 . ASN B 2 369 ? 24.915 -1.793 1.292 1.00 40.40 ? 1905 ASN B OD1 1 ATOM 4762 N ND2 . ASN B 2 369 ? 24.273 -1.155 -0.783 1.00 28.15 ? 1905 ASN B ND2 1 ATOM 4763 N N . ALA B 2 370 ? 21.441 1.169 -0.730 1.00 37.75 ? 1906 ALA B N 1 ATOM 4764 C CA . ALA B 2 370 ? 21.611 2.592 -0.477 1.00 36.93 ? 1906 ALA B CA 1 ATOM 4765 C C . ALA B 2 370 ? 20.930 3.465 -1.510 1.00 36.94 ? 1906 ALA B C 1 ATOM 4766 O O . ALA B 2 370 ? 20.553 2.979 -2.573 1.00 39.99 ? 1906 ALA B O 1 ATOM 4767 C CB . ALA B 2 370 ? 23.081 2.911 -0.437 1.00 36.57 ? 1906 ALA B CB 1 ATOM 4768 N N . TRP B 2 371 ? 20.754 4.749 -1.196 1.00 35.68 ? 1907 TRP B N 1 ATOM 4769 C CA . TRP B 2 371 ? 20.156 5.683 -2.152 1.00 35.92 ? 1907 TRP B CA 1 ATOM 4770 C C . TRP B 2 371 ? 21.267 6.302 -3.015 1.00 37.18 ? 1907 TRP B C 1 ATOM 4771 O O . TRP B 2 371 ? 22.269 6.783 -2.494 1.00 41.26 ? 1907 TRP B O 1 ATOM 4772 C CB . TRP B 2 371 ? 19.406 6.809 -1.429 1.00 32.55 ? 1907 TRP B CB 1 ATOM 4773 C CG . TRP B 2 371 ? 18.919 7.917 -2.370 1.00 26.58 ? 1907 TRP B CG 1 ATOM 4774 C CD1 . TRP B 2 371 ? 18.073 7.767 -3.424 1.00 26.98 ? 1907 TRP B CD1 1 ATOM 4775 C CD2 . TRP B 2 371 ? 19.320 9.295 -2.375 1.00 22.54 ? 1907 TRP B CD2 1 ATOM 4776 N NE1 . TRP B 2 371 ? 17.930 8.960 -4.102 1.00 25.69 ? 1907 TRP B NE1 1 ATOM 4777 C CE2 . TRP B 2 371 ? 18.683 9.915 -3.482 1.00 23.17 ? 1907 TRP B CE2 1 ATOM 4778 C CE3 . TRP B 2 371 ? 20.151 10.068 -1.557 1.00 25.53 ? 1907 TRP B CE3 1 ATOM 4779 C CZ2 . TRP B 2 371 ? 18.856 11.269 -3.797 1.00 23.18 ? 1907 TRP B CZ2 1 ATOM 4780 C CZ3 . TRP B 2 371 ? 20.326 11.425 -1.865 1.00 24.98 ? 1907 TRP B CZ3 1 ATOM 4781 C CH2 . TRP B 2 371 ? 19.680 12.010 -2.981 1.00 24.75 ? 1907 TRP B CH2 1 ATOM 4782 N N . ILE B 2 372 ? 21.101 6.273 -4.327 1.00 37.37 ? 1908 ILE B N 1 ATOM 4783 C CA . ILE B 2 372 ? 22.076 6.870 -5.231 1.00 38.29 ? 1908 ILE B CA 1 ATOM 4784 C C . ILE B 2 372 ? 21.324 7.747 -6.233 1.00 39.63 ? 1908 ILE B C 1 ATOM 4785 O O . ILE B 2 372 ? 20.255 7.383 -6.704 1.00 38.46 ? 1908 ILE B O 1 ATOM 4786 C CB . ILE B 2 372 ? 22.856 5.798 -6.030 1.00 40.57 ? 1908 ILE B CB 1 ATOM 4787 C CG1 . ILE B 2 372 ? 23.558 4.817 -5.094 1.00 40.87 ? 1908 ILE B CG1 1 ATOM 4788 C CG2 . ILE B 2 372 ? 23.860 6.472 -6.928 1.00 43.24 ? 1908 ILE B CG2 1 ATOM 4789 C CD1 . ILE B 2 372 ? 24.485 3.836 -5.807 1.00 39.55 ? 1908 ILE B CD1 1 ATOM 4790 N N . ALA B 2 373 ? 21.864 8.914 -6.544 1.00 43.27 ? 1909 ALA B N 1 ATOM 4791 C CA . ALA B 2 373 ? 21.231 9.798 -7.518 1.00 47.64 ? 1909 ALA B CA 1 ATOM 4792 C C . ALA B 2 373 ? 22.108 9.769 -8.774 1.00 53.04 ? 1909 ALA B C 1 ATOM 4793 O O . ALA B 2 373 ? 23.333 9.774 -8.684 1.00 52.61 ? 1909 ALA B O 1 ATOM 4794 C CB . ALA B 2 373 ? 21.133 11.208 -6.965 1.00 43.40 ? 1909 ALA B CB 1 ATOM 4795 N N . GLU B 2 374 ? 21.494 9.733 -9.950 1.00 60.99 ? 1910 GLU B N 1 ATOM 4796 C CA . GLU B 2 374 ? 22.275 9.671 -11.179 1.00 66.63 ? 1910 GLU B CA 1 ATOM 4797 C C . GLU B 2 374 ? 23.178 10.885 -11.346 1.00 67.82 ? 1910 GLU B C 1 ATOM 4798 O O . GLU B 2 374 ? 24.229 10.794 -11.977 1.00 68.96 ? 1910 GLU B O 1 ATOM 4799 C CB . GLU B 2 374 ? 21.355 9.551 -12.395 1.00 70.77 ? 1910 GLU B CB 1 ATOM 4800 C CG . GLU B 2 374 ? 22.069 9.135 -13.676 1.00 76.54 ? 1910 GLU B CG 1 ATOM 4801 C CD . GLU B 2 374 ? 21.469 9.775 -14.934 1.00 80.90 ? 1910 GLU B CD 1 ATOM 4802 O OE1 . GLU B 2 374 ? 21.761 9.279 -16.052 1.00 82.80 ? 1910 GLU B OE1 1 ATOM 4803 O OE2 . GLU B 2 374 ? 20.720 10.777 -14.810 1.00 80.02 ? 1910 GLU B OE2 1 ATOM 4804 N N . LYS B 2 375 ? 22.777 12.013 -10.771 1.00 68.26 ? 1911 LYS B N 1 ATOM 4805 C CA . LYS B 2 375 ? 23.556 13.237 -10.894 1.00 70.34 ? 1911 LYS B CA 1 ATOM 4806 C C . LYS B 2 375 ? 23.423 14.148 -9.681 1.00 72.03 ? 1911 LYS B C 1 ATOM 4807 O O . LYS B 2 375 ? 22.351 14.261 -9.092 1.00 72.53 ? 1911 LYS B O 1 ATOM 4808 C CB . LYS B 2 375 ? 23.106 13.997 -12.139 1.00 71.78 ? 1911 LYS B CB 1 ATOM 4809 C CG . LYS B 2 375 ? 21.617 14.376 -12.138 1.00 73.66 ? 1911 LYS B CG 1 ATOM 4810 C CD . LYS B 2 375 ? 21.298 15.564 -11.225 1.00 74.22 ? 1911 LYS B CD 1 ATOM 4811 C CE . LYS B 2 375 ? 19.791 15.799 -11.132 1.00 75.78 ? 1911 LYS B CE 1 ATOM 4812 N NZ . LYS B 2 375 ? 19.431 17.049 -10.397 1.00 74.91 ? 1911 LYS B NZ 1 ATOM 4813 N N . LEU B 2 376 ? 24.513 14.807 -9.314 1.00 73.67 ? 1912 LEU B N 1 ATOM 4814 C CA . LEU B 2 376 ? 24.481 15.709 -8.182 1.00 76.46 ? 1912 LEU B CA 1 ATOM 4815 C C . LEU B 2 376 ? 24.543 17.137 -8.670 1.00 79.60 ? 1912 LEU B C 1 ATOM 4816 O O . LEU B 2 376 ? 25.059 18.010 -7.976 1.00 81.37 ? 1912 LEU B O 1 ATOM 4817 C CB . LEU B 2 376 ? 25.643 15.434 -7.219 1.00 74.32 ? 1912 LEU B CB 1 ATOM 4818 C CG . LEU B 2 376 ? 27.114 15.474 -7.641 1.00 71.69 ? 1912 LEU B CG 1 ATOM 4819 C CD1 . LEU B 2 376 ? 27.529 16.830 -8.146 1.00 68.51 ? 1912 LEU B CD1 1 ATOM 4820 C CD2 . LEU B 2 376 ? 27.942 15.101 -6.428 1.00 72.32 ? 1912 LEU B CD2 1 ATOM 4821 N N . SER B 2 377 ? 23.997 17.369 -9.861 1.00 82.61 ? 1913 SER B N 1 ATOM 4822 C CA . SER B 2 377 ? 23.987 18.700 -10.475 1.00 84.58 ? 1913 SER B CA 1 ATOM 4823 C C . SER B 2 377 ? 23.578 19.811 -9.495 1.00 85.20 ? 1913 SER B C 1 ATOM 4824 O O . SER B 2 377 ? 23.646 20.994 -9.827 1.00 85.05 ? 1913 SER B O 1 ATOM 4825 C CB . SER B 2 377 ? 23.056 18.700 -11.698 1.00 84.56 ? 1913 SER B CB 1 ATOM 4826 O OG . SER B 2 377 ? 23.210 19.875 -12.476 1.00 83.84 ? 1913 SER B OG 1 ATOM 4827 N N . THR B 2 378 ? 23.168 19.421 -8.288 1.00 86.34 ? 1914 THR B N 1 ATOM 4828 C CA . THR B 2 378 ? 22.760 20.362 -7.244 1.00 87.26 ? 1914 THR B CA 1 ATOM 4829 C C . THR B 2 378 ? 23.803 21.421 -6.860 1.00 88.00 ? 1914 THR B C 1 ATOM 4830 O O . THR B 2 378 ? 24.738 21.153 -6.101 1.00 85.39 ? 1914 THR B O 1 ATOM 4831 C CB . THR B 2 378 ? 22.340 19.611 -5.967 1.00 85.57 ? 1914 THR B CB 1 ATOM 4832 O OG1 . THR B 2 378 ? 22.474 20.472 -4.832 1.00 84.41 ? 1914 THR B OG1 1 ATOM 4833 C CG2 . THR B 2 378 ? 23.188 18.388 -5.783 1.00 85.04 ? 1914 THR B CG2 1 ATOM 4834 N N . GLU B 2 379 ? 23.611 22.626 -7.399 1.00 89.99 ? 1915 GLU B N 1 ATOM 4835 C CA . GLU B 2 379 ? 24.468 23.784 -7.148 1.00 92.26 ? 1915 GLU B CA 1 ATOM 4836 C C . GLU B 2 379 ? 23.602 24.818 -6.412 1.00 92.88 ? 1915 GLU B C 1 ATOM 4837 O O . GLU B 2 379 ? 23.223 24.594 -5.259 1.00 92.11 ? 1915 GLU B O 1 ATOM 4838 C CB . GLU B 2 379 ? 24.984 24.337 -8.483 1.00 93.63 ? 1915 GLU B CB 1 ATOM 4839 C CG . GLU B 2 379 ? 23.946 24.368 -9.616 1.00 96.30 ? 1915 GLU B CG 1 ATOM 4840 C CD . GLU B 2 379 ? 24.381 23.575 -10.859 1.00 98.09 ? 1915 GLU B CD 1 ATOM 4841 O OE1 . GLU B 2 379 ? 25.533 23.750 -11.318 1.00 97.99 ? 1915 GLU B OE1 1 ATOM 4842 O OE2 . GLU B 2 379 ? 23.566 22.785 -11.386 1.00 97.54 ? 1915 GLU B OE2 1 ATOM 4843 N N . PHE B 2 380 ? 23.285 25.942 -7.056 1.00 93.32 ? 1916 PHE B N 1 ATOM 4844 C CA . PHE B 2 380 ? 22.403 26.933 -6.429 1.00 93.21 ? 1916 PHE B CA 1 ATOM 4845 C C . PHE B 2 380 ? 20.992 26.339 -6.494 1.00 90.82 ? 1916 PHE B C 1 ATOM 4846 O O . PHE B 2 380 ? 19.979 27.045 -6.449 1.00 89.58 ? 1916 PHE B O 1 ATOM 4847 C CB . PHE B 2 380 ? 22.440 28.273 -7.178 1.00 96.33 ? 1916 PHE B CB 1 ATOM 4848 C CG . PHE B 2 380 ? 23.466 29.245 -6.649 1.00 99.39 ? 1916 PHE B CG 1 ATOM 4849 C CD1 . PHE B 2 380 ? 23.502 30.557 -7.117 1.00 99.16 ? 1916 PHE B CD1 1 ATOM 4850 C CD2 . PHE B 2 380 ? 24.393 28.853 -5.677 1.00 100.53 ? 1916 PHE B CD2 1 ATOM 4851 C CE1 . PHE B 2 380 ? 24.444 31.467 -6.627 1.00 100.48 ? 1916 PHE B CE1 1 ATOM 4852 C CE2 . PHE B 2 380 ? 25.341 29.756 -5.181 1.00 100.76 ? 1916 PHE B CE2 1 ATOM 4853 C CZ . PHE B 2 380 ? 25.365 31.066 -5.657 1.00 100.74 ? 1916 PHE B CZ 1 ATOM 4854 N N . ASN B 2 381 ? 20.970 25.016 -6.620 1.00 88.02 ? 1917 ASN B N 1 ATOM 4855 C CA . ASN B 2 381 ? 19.761 24.215 -6.698 1.00 84.54 ? 1917 ASN B CA 1 ATOM 4856 C C . ASN B 2 381 ? 19.981 23.047 -5.750 1.00 82.82 ? 1917 ASN B C 1 ATOM 4857 O O . ASN B 2 381 ? 21.093 22.534 -5.629 1.00 81.96 ? 1917 ASN B O 1 ATOM 4858 C CB . ASN B 2 381 ? 19.559 23.703 -8.128 1.00 83.02 ? 1917 ASN B CB 1 ATOM 4859 C CG . ASN B 2 381 ? 18.463 22.656 -8.234 1.00 80.64 ? 1917 ASN B CG 1 ATOM 4860 O OD1 . ASN B 2 381 ? 17.396 22.790 -7.645 1.00 80.37 ? 1917 ASN B OD1 1 ATOM 4861 N ND2 . ASN B 2 381 ? 18.719 21.617 -9.006 1.00 81.23 ? 1917 ASN B ND2 1 ATOM 4862 N N . PRO B 2 382 ? 18.928 22.632 -5.039 1.00 81.04 ? 1918 PRO B N 1 ATOM 4863 C CA . PRO B 2 382 ? 19.062 21.519 -4.107 1.00 79.34 ? 1918 PRO B CA 1 ATOM 4864 C C . PRO B 2 382 ? 18.235 20.358 -4.609 1.00 77.99 ? 1918 PRO B C 1 ATOM 4865 O O . PRO B 2 382 ? 17.769 19.553 -3.809 1.00 77.36 ? 1918 PRO B O 1 ATOM 4866 C CB . PRO B 2 382 ? 18.454 22.089 -2.851 1.00 81.01 ? 1918 PRO B CB 1 ATOM 4867 C CG . PRO B 2 382 ? 17.212 22.751 -3.428 1.00 79.79 ? 1918 PRO B CG 1 ATOM 4868 C CD . PRO B 2 382 ? 17.725 23.422 -4.712 1.00 79.76 ? 1918 PRO B CD 1 ATOM 4869 N N . GLU B 2 383 ? 18.055 20.260 -5.922 1.00 76.90 ? 1919 GLU B N 1 ATOM 4870 C CA . GLU B 2 383 ? 17.200 19.208 -6.451 1.00 75.86 ? 1919 GLU B CA 1 ATOM 4871 C C . GLU B 2 383 ? 17.518 17.799 -5.990 1.00 72.02 ? 1919 GLU B C 1 ATOM 4872 O O . GLU B 2 383 ? 16.672 17.149 -5.371 1.00 73.66 ? 1919 GLU B O 1 ATOM 4873 C CB . GLU B 2 383 ? 17.137 19.254 -7.972 1.00 80.48 ? 1919 GLU B CB 1 ATOM 4874 C CG . GLU B 2 383 ? 15.867 18.594 -8.507 1.00 84.46 ? 1919 GLU B CG 1 ATOM 4875 C CD . GLU B 2 383 ? 14.619 19.076 -7.772 1.00 84.76 ? 1919 GLU B CD 1 ATOM 4876 O OE1 . GLU B 2 383 ? 14.427 20.303 -7.676 1.00 84.61 ? 1919 GLU B OE1 1 ATOM 4877 O OE2 . GLU B 2 383 ? 13.831 18.236 -7.290 1.00 86.83 ? 1919 GLU B OE2 1 ATOM 4878 N N . PRO B 2 384 ? 18.728 17.296 -6.274 1.00 66.41 ? 1920 PRO B N 1 ATOM 4879 C CA . PRO B 2 384 ? 18.969 15.926 -5.795 1.00 61.26 ? 1920 PRO B CA 1 ATOM 4880 C C . PRO B 2 384 ? 18.879 15.936 -4.264 1.00 56.30 ? 1920 PRO B C 1 ATOM 4881 O O . PRO B 2 384 ? 19.707 16.569 -3.614 1.00 55.82 ? 1920 PRO B O 1 ATOM 4882 C CB . PRO B 2 384 ? 20.390 15.618 -6.287 1.00 59.77 ? 1920 PRO B CB 1 ATOM 4883 C CG . PRO B 2 384 ? 20.613 16.604 -7.397 1.00 63.31 ? 1920 PRO B CG 1 ATOM 4884 C CD . PRO B 2 384 ? 19.923 17.859 -6.917 1.00 62.85 ? 1920 PRO B CD 1 ATOM 4885 N N . TRP B 2 385 ? 17.869 15.271 -3.697 1.00 51.62 ? 1921 TRP B N 1 ATOM 4886 C CA . TRP B 2 385 ? 17.703 15.214 -2.235 1.00 46.67 ? 1921 TRP B CA 1 ATOM 4887 C C . TRP B 2 385 ? 16.928 14.001 -1.744 1.00 42.50 ? 1921 TRP B C 1 ATOM 4888 O O . TRP B 2 385 ? 16.115 13.425 -2.466 1.00 41.71 ? 1921 TRP B O 1 ATOM 4889 C CB . TRP B 2 385 ? 16.963 16.459 -1.707 1.00 49.06 ? 1921 TRP B CB 1 ATOM 4890 C CG . TRP B 2 385 ? 15.426 16.423 -1.879 1.00 52.84 ? 1921 TRP B CG 1 ATOM 4891 C CD1 . TRP B 2 385 ? 14.544 15.489 -1.369 1.00 55.58 ? 1921 TRP B CD1 1 ATOM 4892 C CD2 . TRP B 2 385 ? 14.628 17.339 -2.626 1.00 51.80 ? 1921 TRP B CD2 1 ATOM 4893 N NE1 . TRP B 2 385 ? 13.258 15.773 -1.765 1.00 53.03 ? 1921 TRP B NE1 1 ATOM 4894 C CE2 . TRP B 2 385 ? 13.284 16.903 -2.535 1.00 53.51 ? 1921 TRP B CE2 1 ATOM 4895 C CE3 . TRP B 2 385 ? 14.916 18.486 -3.363 1.00 54.51 ? 1921 TRP B CE3 1 ATOM 4896 C CZ2 . TRP B 2 385 ? 12.241 17.579 -3.155 1.00 56.66 ? 1921 TRP B CZ2 1 ATOM 4897 C CZ3 . TRP B 2 385 ? 13.880 19.161 -3.980 1.00 58.98 ? 1921 TRP B CZ3 1 ATOM 4898 C CH2 . TRP B 2 385 ? 12.555 18.706 -3.873 1.00 60.20 ? 1921 TRP B CH2 1 ATOM 4899 N N . ILE B 2 386 ? 17.177 13.620 -0.502 1.00 38.63 ? 1922 ILE B N 1 ATOM 4900 C CA . ILE B 2 386 ? 16.418 12.544 0.116 1.00 36.31 ? 1922 ILE B CA 1 ATOM 4901 C C . ILE B 2 386 ? 15.751 13.251 1.324 1.00 37.82 ? 1922 ILE B C 1 ATOM 4902 O O . ILE B 2 386 ? 16.380 14.059 2.014 1.00 39.43 ? 1922 ILE B O 1 ATOM 4903 C CB . ILE B 2 386 ? 17.328 11.331 0.514 1.00 31.62 ? 1922 ILE B CB 1 ATOM 4904 C CG1 . ILE B 2 386 ? 16.471 10.202 1.082 1.00 31.07 ? 1922 ILE B CG1 1 ATOM 4905 C CG2 . ILE B 2 386 ? 18.358 11.731 1.506 1.00 22.52 ? 1922 ILE B CG2 1 ATOM 4906 C CD1 . ILE B 2 386 ? 17.207 8.858 1.194 1.00 27.94 ? 1922 ILE B CD1 1 ATOM 4907 N N . GLN B 2 387 ? 14.465 12.997 1.538 1.00 37.26 ? 1923 GLN B N 1 ATOM 4908 C CA . GLN B 2 387 ? 13.715 13.642 2.621 1.00 36.76 ? 1923 GLN B CA 1 ATOM 4909 C C . GLN B 2 387 ? 13.241 12.657 3.690 1.00 37.35 ? 1923 GLN B C 1 ATOM 4910 O O . GLN B 2 387 ? 12.664 11.611 3.387 1.00 38.19 ? 1923 GLN B O 1 ATOM 4911 C CB . GLN B 2 387 ? 12.491 14.376 2.038 1.00 35.91 ? 1923 GLN B CB 1 ATOM 4912 C CG . GLN B 2 387 ? 11.754 15.349 2.966 1.00 35.32 ? 1923 GLN B CG 1 ATOM 4913 C CD . GLN B 2 387 ? 10.399 15.798 2.396 1.00 37.87 ? 1923 GLN B CD 1 ATOM 4914 O OE1 . GLN B 2 387 ? 9.400 15.096 2.525 1.00 42.13 ? 1923 GLN B OE1 1 ATOM 4915 N NE2 . GLN B 2 387 ? 10.370 16.959 1.752 1.00 34.69 ? 1923 GLN B NE2 1 ATOM 4916 N N . VAL B 2 388 ? 13.491 12.993 4.946 1.00 37.98 ? 1924 VAL B N 1 ATOM 4917 C CA . VAL B 2 388 ? 13.047 12.153 6.036 1.00 40.53 ? 1924 VAL B CA 1 ATOM 4918 C C . VAL B 2 388 ? 11.991 12.961 6.818 1.00 42.65 ? 1924 VAL B C 1 ATOM 4919 O O . VAL B 2 388 ? 12.212 14.129 7.157 1.00 42.10 ? 1924 VAL B O 1 ATOM 4920 C CB . VAL B 2 388 ? 14.230 11.738 6.947 1.00 41.67 ? 1924 VAL B CB 1 ATOM 4921 C CG1 . VAL B 2 388 ? 13.731 10.852 8.067 1.00 42.67 ? 1924 VAL B CG1 1 ATOM 4922 C CG2 . VAL B 2 388 ? 15.281 10.988 6.137 1.00 38.96 ? 1924 VAL B CG2 1 ATOM 4923 N N . ASP B 2 389 ? 10.835 12.340 7.059 1.00 42.65 ? 1925 ASP B N 1 ATOM 4924 C CA . ASP B 2 389 ? 9.732 12.981 7.764 1.00 42.77 ? 1925 ASP B CA 1 ATOM 4925 C C . ASP B 2 389 ? 9.445 12.302 9.086 1.00 43.27 ? 1925 ASP B C 1 ATOM 4926 O O . ASP B 2 389 ? 8.836 11.235 9.132 1.00 42.43 ? 1925 ASP B O 1 ATOM 4927 C CB . ASP B 2 389 ? 8.468 12.969 6.908 1.00 44.83 ? 1925 ASP B CB 1 ATOM 4928 C CG . ASP B 2 389 ? 7.252 13.436 7.672 1.00 49.79 ? 1925 ASP B CG 1 ATOM 4929 O OD1 . ASP B 2 389 ? 7.420 13.914 8.812 1.00 55.12 ? 1925 ASP B OD1 1 ATOM 4930 O OD2 . ASP B 2 389 ? 6.124 13.337 7.141 1.00 53.23 ? 1925 ASP B OD2 1 ATOM 4931 N N . MET B 2 390 ? 9.872 12.952 10.165 1.00 43.69 ? 1926 MET B N 1 ATOM 4932 C CA . MET B 2 390 ? 9.700 12.440 11.511 1.00 42.85 ? 1926 MET B CA 1 ATOM 4933 C C . MET B 2 390 ? 8.233 12.372 11.914 1.00 45.74 ? 1926 MET B C 1 ATOM 4934 O O . MET B 2 390 ? 7.894 11.886 12.994 1.00 45.08 ? 1926 MET B O 1 ATOM 4935 C CB . MET B 2 390 ? 10.467 13.317 12.480 1.00 40.42 ? 1926 MET B CB 1 ATOM 4936 C CG . MET B 2 390 ? 11.921 13.492 12.123 1.00 41.44 ? 1926 MET B CG 1 ATOM 4937 S SD . MET B 2 390 ? 12.754 11.925 11.979 1.00 40.25 ? 1926 MET B SD 1 ATOM 4938 C CE . MET B 2 390 ? 12.063 11.067 13.461 1.00 43.11 ? 1926 MET B CE 1 ATOM 4939 N N . GLN B 2 391 ? 7.360 12.865 11.042 1.00 48.53 ? 1927 GLN B N 1 ATOM 4940 C CA . GLN B 2 391 ? 5.928 12.834 11.298 1.00 49.31 ? 1927 GLN B CA 1 ATOM 4941 C C . GLN B 2 391 ? 5.529 13.758 12.435 1.00 50.53 ? 1927 GLN B C 1 ATOM 4942 O O . GLN B 2 391 ? 4.347 14.060 12.629 1.00 50.93 ? 1927 GLN B O 1 ATOM 4943 C CB . GLN B 2 391 ? 5.486 11.399 11.578 1.00 48.24 ? 1927 GLN B CB 1 ATOM 4944 C CG . GLN B 2 391 ? 5.674 10.508 10.373 1.00 48.80 ? 1927 GLN B CG 1 ATOM 4945 C CD . GLN B 2 391 ? 5.002 9.161 10.499 1.00 50.60 ? 1927 GLN B CD 1 ATOM 4946 O OE1 . GLN B 2 391 ? 4.997 8.374 9.546 1.00 55.27 ? 1927 GLN B OE1 1 ATOM 4947 N NE2 . GLN B 2 391 ? 4.435 8.877 11.667 1.00 49.99 ? 1927 GLN B NE2 1 ATOM 4948 N N . LYS B 2 392 ? 6.533 14.206 13.181 1.00 51.06 ? 1928 LYS B N 1 ATOM 4949 C CA . LYS B 2 392 ? 6.333 15.135 14.273 1.00 50.19 ? 1928 LYS B CA 1 ATOM 4950 C C . LYS B 2 392 ? 7.660 15.862 14.492 1.00 48.88 ? 1928 LYS B C 1 ATOM 4951 O O . LYS B 2 392 ? 8.690 15.427 13.991 1.00 46.59 ? 1928 LYS B O 1 ATOM 4952 C CB . LYS B 2 392 ? 5.854 14.391 15.518 1.00 52.74 ? 1928 LYS B CB 1 ATOM 4953 C CG . LYS B 2 392 ? 4.592 15.055 16.132 1.00 62.63 ? 1928 LYS B CG 1 ATOM 4954 C CD . LYS B 2 392 ? 3.531 14.055 16.645 1.00 64.81 ? 1928 LYS B CD 1 ATOM 4955 C CE . LYS B 2 392 ? 3.894 13.458 18.009 1.00 67.63 ? 1928 LYS B CE 1 ATOM 4956 N NZ . LYS B 2 392 ? 3.029 12.294 18.374 1.00 68.08 ? 1928 LYS B NZ 1 ATOM 4957 N N . GLU B 2 393 ? 7.640 16.984 15.199 1.00 47.52 ? 1929 GLU B N 1 ATOM 4958 C CA . GLU B 2 393 ? 8.870 17.736 15.427 1.00 45.72 ? 1929 GLU B CA 1 ATOM 4959 C C . GLU B 2 393 ? 9.761 17.060 16.445 1.00 43.11 ? 1929 GLU B C 1 ATOM 4960 O O . GLU B 2 393 ? 9.284 16.511 17.434 1.00 42.12 ? 1929 GLU B O 1 ATOM 4961 C CB . GLU B 2 393 ? 8.545 19.158 15.874 1.00 47.34 ? 1929 GLU B CB 1 ATOM 4962 C CG . GLU B 2 393 ? 7.779 19.927 14.826 1.00 53.25 ? 1929 GLU B CG 1 ATOM 4963 C CD . GLU B 2 393 ? 6.942 21.041 15.407 1.00 55.68 ? 1929 GLU B CD 1 ATOM 4964 O OE1 . GLU B 2 393 ? 6.050 21.552 14.682 1.00 58.38 ? 1929 GLU B OE1 1 ATOM 4965 O OE2 . GLU B 2 393 ? 7.179 21.403 16.580 1.00 55.70 ? 1929 GLU B OE2 1 ATOM 4966 N N . VAL B 2 394 ? 11.064 17.098 16.178 1.00 41.25 ? 1930 VAL B N 1 ATOM 4967 C CA . VAL B 2 394 ? 12.076 16.489 17.043 1.00 37.99 ? 1930 VAL B CA 1 ATOM 4968 C C . VAL B 2 394 ? 13.312 17.379 17.039 1.00 38.32 ? 1930 VAL B C 1 ATOM 4969 O O . VAL B 2 394 ? 13.389 18.359 16.273 1.00 39.77 ? 1930 VAL B O 1 ATOM 4970 C CB . VAL B 2 394 ? 12.516 15.086 16.518 1.00 36.04 ? 1930 VAL B CB 1 ATOM 4971 C CG1 . VAL B 2 394 ? 11.330 14.144 16.460 1.00 32.11 ? 1930 VAL B CG1 1 ATOM 4972 C CG2 . VAL B 2 394 ? 13.152 15.215 15.137 1.00 33.48 ? 1930 VAL B CG2 1 ATOM 4973 N N . LEU B 2 395 ? 14.286 17.031 17.872 1.00 33.75 ? 1931 LEU B N 1 ATOM 4974 C CA . LEU B 2 395 ? 15.530 17.790 17.931 1.00 32.35 ? 1931 LEU B CA 1 ATOM 4975 C C . LEU B 2 395 ? 16.627 17.038 17.180 1.00 30.63 ? 1931 LEU B C 1 ATOM 4976 O O . LEU B 2 395 ? 16.933 15.899 17.510 1.00 32.67 ? 1931 LEU B O 1 ATOM 4977 C CB . LEU B 2 395 ? 15.941 17.992 19.388 1.00 33.97 ? 1931 LEU B CB 1 ATOM 4978 C CG . LEU B 2 395 ? 15.826 19.401 19.949 1.00 32.66 ? 1931 LEU B CG 1 ATOM 4979 C CD1 . LEU B 2 395 ? 15.743 19.331 21.447 1.00 32.99 ? 1931 LEU B CD1 1 ATOM 4980 C CD2 . LEU B 2 395 ? 17.007 20.221 19.515 1.00 34.30 ? 1931 LEU B CD2 1 ATOM 4981 N N . LEU B 2 396 ? 17.215 17.677 16.179 1.00 28.45 ? 1932 LEU B N 1 ATOM 4982 C CA . LEU B 2 396 ? 18.269 17.068 15.369 1.00 29.41 ? 1932 LEU B CA 1 ATOM 4983 C C . LEU B 2 396 ? 19.626 17.602 15.786 1.00 28.70 ? 1932 LEU B C 1 ATOM 4984 O O . LEU B 2 396 ? 19.873 18.794 15.663 1.00 27.86 ? 1932 LEU B O 1 ATOM 4985 C CB . LEU B 2 396 ? 18.047 17.387 13.875 1.00 30.34 ? 1932 LEU B CB 1 ATOM 4986 C CG . LEU B 2 396 ? 19.241 17.095 12.932 1.00 32.58 ? 1932 LEU B CG 1 ATOM 4987 C CD1 . LEU B 2 396 ? 19.156 15.646 12.424 1.00 24.82 ? 1932 LEU B CD1 1 ATOM 4988 C CD2 . LEU B 2 396 ? 19.254 18.099 11.748 1.00 25.82 ? 1932 LEU B CD2 1 ATOM 4989 N N . THR B 2 397 ? 20.516 16.727 16.254 1.00 28.66 ? 1933 THR B N 1 ATOM 4990 C CA . THR B 2 397 ? 21.836 17.175 16.694 1.00 27.51 ? 1933 THR B CA 1 ATOM 4991 C C . THR B 2 397 ? 23.023 16.521 15.992 1.00 26.41 ? 1933 THR B C 1 ATOM 4992 O O . THR B 2 397 ? 24.171 16.768 16.341 1.00 24.35 ? 1933 THR B O 1 ATOM 4993 C CB . THR B 2 397 ? 22.002 16.963 18.177 1.00 26.57 ? 1933 THR B CB 1 ATOM 4994 O OG1 . THR B 2 397 ? 22.510 15.652 18.406 1.00 33.03 ? 1933 THR B OG1 1 ATOM 4995 C CG2 . THR B 2 397 ? 20.659 17.094 18.872 1.00 29.20 ? 1933 THR B CG2 1 ATOM 4996 N N . GLY B 2 398 ? 22.753 15.698 14.993 1.00 26.47 ? 1934 GLY B N 1 ATOM 4997 C CA . GLY B 2 398 ? 23.846 15.057 14.297 1.00 26.51 ? 1934 GLY B CA 1 ATOM 4998 C C . GLY B 2 398 ? 23.402 14.241 13.112 1.00 28.42 ? 1934 GLY B C 1 ATOM 4999 O O . GLY B 2 398 ? 22.242 13.847 13.009 1.00 28.63 ? 1934 GLY B O 1 ATOM 5000 N N . ILE B 2 399 ? 24.329 13.995 12.199 1.00 29.44 ? 1935 ILE B N 1 ATOM 5001 C CA . ILE B 2 399 ? 24.028 13.191 11.031 1.00 31.03 ? 1935 ILE B CA 1 ATOM 5002 C C . ILE B 2 399 ? 25.198 12.273 10.693 1.00 32.01 ? 1935 ILE B C 1 ATOM 5003 O O . ILE B 2 399 ? 26.350 12.697 10.731 1.00 31.94 ? 1935 ILE B O 1 ATOM 5004 C CB . ILE B 2 399 ? 23.741 14.070 9.838 1.00 31.12 ? 1935 ILE B CB 1 ATOM 5005 C CG1 . ILE B 2 399 ? 23.464 13.204 8.620 1.00 33.33 ? 1935 ILE B CG1 1 ATOM 5006 C CG2 . ILE B 2 399 ? 24.931 14.929 9.552 1.00 35.25 ? 1935 ILE B CG2 1 ATOM 5007 C CD1 . ILE B 2 399 ? 22.874 13.959 7.476 1.00 35.03 ? 1935 ILE B CD1 1 ATOM 5008 N N . GLN B 2 400 ? 24.902 11.013 10.374 1.00 32.32 ? 1936 GLN B N 1 ATOM 5009 C CA . GLN B 2 400 ? 25.944 10.043 10.007 1.00 31.42 ? 1936 GLN B CA 1 ATOM 5010 C C . GLN B 2 400 ? 25.665 9.544 8.609 1.00 32.49 ? 1936 GLN B C 1 ATOM 5011 O O . GLN B 2 400 ? 24.535 9.198 8.294 1.00 34.23 ? 1936 GLN B O 1 ATOM 5012 C CB . GLN B 2 400 ? 25.939 8.850 10.950 1.00 30.82 ? 1936 GLN B CB 1 ATOM 5013 C CG . GLN B 2 400 ? 26.230 9.197 12.372 1.00 35.53 ? 1936 GLN B CG 1 ATOM 5014 C CD . GLN B 2 400 ? 26.090 8.010 13.306 1.00 40.73 ? 1936 GLN B CD 1 ATOM 5015 O OE1 . GLN B 2 400 ? 25.019 7.398 13.414 1.00 41.80 ? 1936 GLN B OE1 1 ATOM 5016 N NE2 . GLN B 2 400 ? 27.175 7.682 13.995 1.00 44.97 ? 1936 GLN B NE2 1 ATOM 5017 N N . THR B 2 401 ? 26.689 9.500 7.769 1.00 33.93 ? 1937 THR B N 1 ATOM 5018 C CA . THR B 2 401 ? 26.522 9.029 6.396 1.00 33.09 ? 1937 THR B CA 1 ATOM 5019 C C . THR B 2 401 ? 27.503 7.907 6.067 1.00 34.26 ? 1937 THR B C 1 ATOM 5020 O O . THR B 2 401 ? 28.540 7.764 6.720 1.00 33.47 ? 1937 THR B O 1 ATOM 5021 C CB . THR B 2 401 ? 26.773 10.149 5.402 1.00 31.88 ? 1937 THR B CB 1 ATOM 5022 O OG1 . THR B 2 401 ? 28.153 10.538 5.462 1.00 34.15 ? 1937 THR B OG1 1 ATOM 5023 C CG2 . THR B 2 401 ? 25.926 11.335 5.741 1.00 35.77 ? 1937 THR B CG2 1 ATOM 5024 N N . GLN B 2 402 ? 27.156 7.131 5.040 1.00 34.63 ? 1938 GLN B N 1 ATOM 5025 C CA . GLN B 2 402 ? 27.955 6.016 4.540 1.00 35.55 ? 1938 GLN B CA 1 ATOM 5026 C C . GLN B 2 402 ? 27.692 5.931 3.067 1.00 37.44 ? 1938 GLN B C 1 ATOM 5027 O O . GLN B 2 402 ? 26.709 6.481 2.581 1.00 39.84 ? 1938 GLN B O 1 ATOM 5028 C CB . GLN B 2 402 ? 27.494 4.691 5.119 1.00 35.65 ? 1938 GLN B CB 1 ATOM 5029 C CG . GLN B 2 402 ? 28.292 4.173 6.257 1.00 40.35 ? 1938 GLN B CG 1 ATOM 5030 C CD . GLN B 2 402 ? 27.736 2.868 6.724 1.00 43.63 ? 1938 GLN B CD 1 ATOM 5031 O OE1 . GLN B 2 402 ? 26.540 2.756 6.979 1.00 47.93 ? 1938 GLN B OE1 1 ATOM 5032 N NE2 . GLN B 2 402 ? 28.588 1.864 6.833 1.00 43.66 ? 1938 GLN B NE2 1 ATOM 5033 N N . GLY B 2 403 ? 28.553 5.210 2.360 1.00 39.54 ? 1939 GLY B N 1 ATOM 5034 C CA . GLY B 2 403 ? 28.363 5.029 0.932 1.00 38.48 ? 1939 GLY B CA 1 ATOM 5035 C C . GLY B 2 403 ? 27.833 3.634 0.665 1.00 38.46 ? 1939 GLY B C 1 ATOM 5036 O O . GLY B 2 403 ? 27.304 2.976 1.555 1.00 38.06 ? 1939 GLY B O 1 ATOM 5037 N N . ALA B 2 404 ? 27.979 3.184 -0.570 1.00 38.97 ? 1940 ALA B N 1 ATOM 5038 C CA . ALA B 2 404 ? 27.533 1.859 -0.977 1.00 41.16 ? 1940 ALA B CA 1 ATOM 5039 C C . ALA B 2 404 ? 28.616 1.298 -1.871 1.00 44.80 ? 1940 ALA B C 1 ATOM 5040 O O . ALA B 2 404 ? 29.547 2.007 -2.254 1.00 44.86 ? 1940 ALA B O 1 ATOM 5041 C CB . ALA B 2 404 ? 26.227 1.942 -1.739 1.00 35.72 ? 1940 ALA B CB 1 ATOM 5042 N N . LYS B 2 405 ? 28.490 0.022 -2.207 1.00 50.42 ? 1941 LYS B N 1 ATOM 5043 C CA . LYS B 2 405 ? 29.466 -0.653 -3.055 1.00 53.93 ? 1941 LYS B CA 1 ATOM 5044 C C . LYS B 2 405 ? 28.719 -1.637 -3.937 1.00 56.12 ? 1941 LYS B C 1 ATOM 5045 O O . LYS B 2 405 ? 28.176 -2.619 -3.439 1.00 57.48 ? 1941 LYS B O 1 ATOM 5046 C CB . LYS B 2 405 ? 30.471 -1.398 -2.177 1.00 53.43 ? 1941 LYS B CB 1 ATOM 5047 C CG . LYS B 2 405 ? 31.814 -1.624 -2.824 1.00 55.80 ? 1941 LYS B CG 1 ATOM 5048 C CD . LYS B 2 405 ? 32.828 -2.169 -1.826 1.00 55.20 ? 1941 LYS B CD 1 ATOM 5049 C CE . LYS B 2 405 ? 34.189 -2.387 -2.479 1.00 55.02 ? 1941 LYS B CE 1 ATOM 5050 N NZ . LYS B 2 405 ? 35.238 -2.841 -1.523 1.00 54.81 ? 1941 LYS B NZ 1 ATOM 5051 N N . HIS B 2 406 ? 28.660 -1.352 -5.234 1.00 59.89 ? 1942 HIS B N 1 ATOM 5052 C CA . HIS B 2 406 ? 27.984 -2.235 -6.181 1.00 63.19 ? 1942 HIS B CA 1 ATOM 5053 C C . HIS B 2 406 ? 28.602 -3.598 -5.936 1.00 64.06 ? 1942 HIS B C 1 ATOM 5054 O O . HIS B 2 406 ? 27.965 -4.487 -5.373 1.00 67.66 ? 1942 HIS B O 1 ATOM 5055 C CB . HIS B 2 406 ? 28.267 -1.797 -7.613 1.00 67.12 ? 1942 HIS B CB 1 ATOM 5056 C CG . HIS B 2 406 ? 27.258 -2.283 -8.602 1.00 72.47 ? 1942 HIS B CG 1 ATOM 5057 N ND1 . HIS B 2 406 ? 26.875 -3.605 -8.688 1.00 75.57 ? 1942 HIS B ND1 1 ATOM 5058 C CD2 . HIS B 2 406 ? 26.556 -1.624 -9.554 1.00 73.17 ? 1942 HIS B CD2 1 ATOM 5059 C CE1 . HIS B 2 406 ? 25.981 -3.739 -9.652 1.00 77.10 ? 1942 HIS B CE1 1 ATOM 5060 N NE2 . HIS B 2 406 ? 25.770 -2.553 -10.193 1.00 77.66 ? 1942 HIS B NE2 1 ATOM 5061 N N . TYR B 2 407 ? 29.846 -3.761 -6.368 1.00 62.57 ? 1943 TYR B N 1 ATOM 5062 C CA . TYR B 2 407 ? 30.576 -5.002 -6.133 1.00 62.85 ? 1943 TYR B CA 1 ATOM 5063 C C . TYR B 2 407 ? 31.953 -4.587 -5.637 1.00 59.48 ? 1943 TYR B C 1 ATOM 5064 O O . TYR B 2 407 ? 32.289 -4.775 -4.467 1.00 58.02 ? 1943 TYR B O 1 ATOM 5065 C CB . TYR B 2 407 ? 30.717 -5.834 -7.414 1.00 67.10 ? 1943 TYR B CB 1 ATOM 5066 C CG . TYR B 2 407 ? 29.497 -6.662 -7.777 1.00 72.86 ? 1943 TYR B CG 1 ATOM 5067 C CD1 . TYR B 2 407 ? 28.361 -6.066 -8.338 1.00 74.25 ? 1943 TYR B CD1 1 ATOM 5068 C CD2 . TYR B 2 407 ? 29.483 -8.050 -7.574 1.00 74.63 ? 1943 TYR B CD2 1 ATOM 5069 C CE1 . TYR B 2 407 ? 27.245 -6.828 -8.689 1.00 75.88 ? 1943 TYR B CE1 1 ATOM 5070 C CE2 . TYR B 2 407 ? 28.368 -8.823 -7.924 1.00 75.82 ? 1943 TYR B CE2 1 ATOM 5071 C CZ . TYR B 2 407 ? 27.256 -8.204 -8.479 1.00 76.69 ? 1943 TYR B CZ 1 ATOM 5072 O OH . TYR B 2 407 ? 26.154 -8.952 -8.817 1.00 78.48 ? 1943 TYR B OH 1 ATOM 5073 N N . LEU B 2 408 ? 32.734 -4.012 -6.548 1.00 55.65 ? 1944 LEU B N 1 ATOM 5074 C CA . LEU B 2 408 ? 34.072 -3.520 -6.254 1.00 50.71 ? 1944 LEU B CA 1 ATOM 5075 C C . LEU B 2 408 ? 34.115 -2.026 -6.568 1.00 48.82 ? 1944 LEU B C 1 ATOM 5076 O O . LEU B 2 408 ? 35.077 -1.355 -6.221 1.00 50.14 ? 1944 LEU B O 1 ATOM 5077 C CB . LEU B 2 408 ? 35.123 -4.220 -7.116 1.00 48.97 ? 1944 LEU B CB 1 ATOM 5078 C CG . LEU B 2 408 ? 35.457 -5.712 -7.017 1.00 48.74 ? 1944 LEU B CG 1 ATOM 5079 C CD1 . LEU B 2 408 ? 36.472 -6.025 -8.104 1.00 46.45 ? 1944 LEU B CD1 1 ATOM 5080 C CD2 . LEU B 2 408 ? 36.023 -6.082 -5.650 1.00 46.79 ? 1944 LEU B CD2 1 ATOM 5081 N N . LYS B 2 409 ? 33.086 -1.508 -7.237 1.00 44.57 ? 1945 LYS B N 1 ATOM 5082 C CA . LYS B 2 409 ? 33.054 -0.087 -7.582 1.00 42.24 ? 1945 LYS B CA 1 ATOM 5083 C C . LYS B 2 409 ? 32.483 0.706 -6.420 1.00 40.65 ? 1945 LYS B C 1 ATOM 5084 O O . LYS B 2 409 ? 31.303 0.591 -6.088 1.00 40.10 ? 1945 LYS B O 1 ATOM 5085 C CB . LYS B 2 409 ? 32.207 0.155 -8.831 1.00 40.99 ? 1945 LYS B CB 1 ATOM 5086 C CG . LYS B 2 409 ? 32.379 1.527 -9.451 1.00 39.44 ? 1945 LYS B CG 1 ATOM 5087 C CD . LYS B 2 409 ? 31.507 1.660 -10.689 1.00 42.74 ? 1945 LYS B CD 1 ATOM 5088 C CE . LYS B 2 409 ? 31.675 2.997 -11.404 1.00 45.78 ? 1945 LYS B CE 1 ATOM 5089 N NZ . LYS B 2 409 ? 32.952 3.152 -12.194 1.00 51.79 ? 1945 LYS B NZ 1 ATOM 5090 N N . PRO B 2 410 ? 33.318 1.528 -5.784 1.00 38.73 ? 1946 PRO B N 1 ATOM 5091 C CA . PRO B 2 410 ? 32.838 2.320 -4.649 1.00 38.55 ? 1946 PRO B CA 1 ATOM 5092 C C . PRO B 2 410 ? 31.889 3.453 -5.036 1.00 38.15 ? 1946 PRO B C 1 ATOM 5093 O O . PRO B 2 410 ? 31.939 3.987 -6.143 1.00 39.77 ? 1946 PRO B O 1 ATOM 5094 C CB . PRO B 2 410 ? 34.134 2.849 -4.017 1.00 38.17 ? 1946 PRO B CB 1 ATOM 5095 C CG . PRO B 2 410 ? 35.205 1.911 -4.522 1.00 37.38 ? 1946 PRO B CG 1 ATOM 5096 C CD . PRO B 2 410 ? 34.775 1.642 -5.933 1.00 36.58 ? 1946 PRO B CD 1 ATOM 5097 N N . TYR B 2 411 ? 31.011 3.814 -4.113 1.00 37.73 ? 1947 TYR B N 1 ATOM 5098 C CA . TYR B 2 411 ? 30.086 4.921 -4.334 1.00 35.53 ? 1947 TYR B CA 1 ATOM 5099 C C . TYR B 2 411 ? 29.926 5.676 -3.015 1.00 34.66 ? 1947 TYR B C 1 ATOM 5100 O O . TYR B 2 411 ? 29.727 5.067 -1.966 1.00 34.22 ? 1947 TYR B O 1 ATOM 5101 C CB . TYR B 2 411 ? 28.720 4.416 -4.793 1.00 34.52 ? 1947 TYR B CB 1 ATOM 5102 C CG . TYR B 2 411 ? 28.677 3.891 -6.203 1.00 32.37 ? 1947 TYR B CG 1 ATOM 5103 C CD1 . TYR B 2 411 ? 28.442 2.538 -6.458 1.00 31.38 ? 1947 TYR B CD1 1 ATOM 5104 C CD2 . TYR B 2 411 ? 28.829 4.744 -7.287 1.00 31.40 ? 1947 TYR B CD2 1 ATOM 5105 C CE1 . TYR B 2 411 ? 28.357 2.053 -7.761 1.00 28.89 ? 1947 TYR B CE1 1 ATOM 5106 C CE2 . TYR B 2 411 ? 28.744 4.267 -8.596 1.00 29.85 ? 1947 TYR B CE2 1 ATOM 5107 C CZ . TYR B 2 411 ? 28.509 2.926 -8.823 1.00 27.23 ? 1947 TYR B CZ 1 ATOM 5108 O OH . TYR B 2 411 ? 28.415 2.456 -10.112 1.00 30.76 ? 1947 TYR B OH 1 ATOM 5109 N N . TYR B 2 412 ? 30.048 6.994 -3.052 1.00 33.98 ? 1948 TYR B N 1 ATOM 5110 C CA . TYR B 2 412 ? 29.864 7.757 -1.835 1.00 33.96 ? 1948 TYR B CA 1 ATOM 5111 C C . TYR B 2 412 ? 29.795 9.262 -2.021 1.00 33.67 ? 1948 TYR B C 1 ATOM 5112 O O . TYR B 2 412 ? 30.206 9.808 -3.045 1.00 32.51 ? 1948 TYR B O 1 ATOM 5113 C CB . TYR B 2 412 ? 30.925 7.387 -0.790 1.00 34.78 ? 1948 TYR B CB 1 ATOM 5114 C CG . TYR B 2 412 ? 32.346 7.459 -1.256 1.00 38.57 ? 1948 TYR B CG 1 ATOM 5115 C CD1 . TYR B 2 412 ? 33.044 8.660 -1.259 1.00 38.50 ? 1948 TYR B CD1 1 ATOM 5116 C CD2 . TYR B 2 412 ? 32.994 6.318 -1.712 1.00 40.95 ? 1948 TYR B CD2 1 ATOM 5117 C CE1 . TYR B 2 412 ? 34.363 8.718 -1.706 1.00 41.53 ? 1948 TYR B CE1 1 ATOM 5118 C CE2 . TYR B 2 412 ? 34.296 6.363 -2.165 1.00 41.27 ? 1948 TYR B CE2 1 ATOM 5119 C CZ . TYR B 2 412 ? 34.979 7.557 -2.161 1.00 41.31 ? 1948 TYR B CZ 1 ATOM 5120 O OH . TYR B 2 412 ? 36.273 7.573 -2.619 1.00 40.76 ? 1948 TYR B OH 1 ATOM 5121 N N . THR B 2 413 ? 29.216 9.912 -1.020 1.00 32.58 ? 1949 THR B N 1 ATOM 5122 C CA . THR B 2 413 ? 29.065 11.349 -1.015 1.00 32.99 ? 1949 THR B CA 1 ATOM 5123 C C . THR B 2 413 ? 30.295 11.906 -0.311 1.00 32.35 ? 1949 THR B C 1 ATOM 5124 O O . THR B 2 413 ? 30.715 11.416 0.743 1.00 32.50 ? 1949 THR B O 1 ATOM 5125 C CB . THR B 2 413 ? 27.762 11.747 -0.288 1.00 35.60 ? 1949 THR B CB 1 ATOM 5126 O OG1 . THR B 2 413 ? 26.646 11.119 -0.943 1.00 37.88 ? 1949 THR B OG1 1 ATOM 5127 C CG2 . THR B 2 413 ? 27.564 13.253 -0.320 1.00 36.88 ? 1949 THR B CG2 1 ATOM 5128 N N . THR B 2 414 ? 30.895 12.911 -0.930 1.00 31.56 ? 1950 THR B N 1 ATOM 5129 C CA . THR B 2 414 ? 32.096 13.532 -0.406 1.00 30.64 ? 1950 THR B CA 1 ATOM 5130 C C . THR B 2 414 ? 31.739 14.910 0.164 1.00 34.05 ? 1950 THR B C 1 ATOM 5131 O O . THR B 2 414 ? 32.594 15.633 0.664 1.00 34.63 ? 1950 THR B O 1 ATOM 5132 C CB . THR B 2 414 ? 33.109 13.721 -1.537 1.00 28.63 ? 1950 THR B CB 1 ATOM 5133 O OG1 . THR B 2 414 ? 32.475 14.444 -2.601 1.00 23.45 ? 1950 THR B OG1 1 ATOM 5134 C CG2 . THR B 2 414 ? 33.604 12.370 -2.069 1.00 25.09 ? 1950 THR B CG2 1 ATOM 5135 N N . GLU B 2 415 ? 30.470 15.275 0.079 1.00 35.66 ? 1951 GLU B N 1 ATOM 5136 C CA . GLU B 2 415 ? 30.039 16.573 0.570 1.00 39.36 ? 1951 GLU B CA 1 ATOM 5137 C C . GLU B 2 415 ? 28.531 16.779 0.392 1.00 37.91 ? 1951 GLU B C 1 ATOM 5138 O O . GLU B 2 415 ? 27.958 16.407 -0.637 1.00 36.86 ? 1951 GLU B O 1 ATOM 5139 C CB . GLU B 2 415 ? 30.798 17.671 -0.176 1.00 41.49 ? 1951 GLU B CB 1 ATOM 5140 C CG . GLU B 2 415 ? 30.535 19.078 0.313 1.00 40.28 ? 1951 GLU B CG 1 ATOM 5141 C CD . GLU B 2 415 ? 31.195 20.085 -0.577 1.00 41.76 ? 1951 GLU B CD 1 ATOM 5142 O OE1 . GLU B 2 415 ? 30.689 20.284 -1.697 1.00 46.87 ? 1951 GLU B OE1 1 ATOM 5143 O OE2 . GLU B 2 415 ? 32.231 20.657 -0.176 1.00 43.91 ? 1951 GLU B OE2 1 ATOM 5144 N N . PHE B 2 416 ? 27.898 17.393 1.383 1.00 33.93 ? 1952 PHE B N 1 ATOM 5145 C CA . PHE B 2 416 ? 26.475 17.612 1.296 1.00 34.34 ? 1952 PHE B CA 1 ATOM 5146 C C . PHE B 2 416 ? 25.996 18.797 2.133 1.00 36.32 ? 1952 PHE B C 1 ATOM 5147 O O . PHE B 2 416 ? 26.763 19.401 2.885 1.00 37.24 ? 1952 PHE B O 1 ATOM 5148 C CB . PHE B 2 416 ? 25.743 16.329 1.714 1.00 30.85 ? 1952 PHE B CB 1 ATOM 5149 C CG . PHE B 2 416 ? 25.949 15.942 3.156 1.00 27.65 ? 1952 PHE B CG 1 ATOM 5150 C CD1 . PHE B 2 416 ? 25.075 16.378 4.142 1.00 27.50 ? 1952 PHE B CD1 1 ATOM 5151 C CD2 . PHE B 2 416 ? 27.026 15.151 3.531 1.00 28.07 ? 1952 PHE B CD2 1 ATOM 5152 C CE1 . PHE B 2 416 ? 25.271 16.034 5.478 1.00 24.20 ? 1952 PHE B CE1 1 ATOM 5153 C CE2 . PHE B 2 416 ? 27.228 14.804 4.859 1.00 25.81 ? 1952 PHE B CE2 1 ATOM 5154 C CZ . PHE B 2 416 ? 26.348 15.250 5.832 1.00 25.03 ? 1952 PHE B CZ 1 ATOM 5155 N N . CYS B 2 417 ? 24.714 19.107 1.979 1.00 35.04 ? 1953 CYS B N 1 ATOM 5156 C CA . CYS B 2 417 ? 24.057 20.182 2.688 1.00 34.02 ? 1953 CYS B CA 1 ATOM 5157 C C . CYS B 2 417 ? 22.831 19.603 3.358 1.00 33.15 ? 1953 CYS B C 1 ATOM 5158 O O . CYS B 2 417 ? 22.249 18.652 2.864 1.00 34.55 ? 1953 CYS B O 1 ATOM 5159 C CB . CYS B 2 417 ? 23.639 21.273 1.716 1.00 35.49 ? 1953 CYS B CB 1 ATOM 5160 S SG . CYS B 2 417 ? 25.007 22.260 1.157 1.00 42.39 ? 1953 CYS B SG 1 ATOM 5161 N N . VAL B 2 418 ? 22.434 20.201 4.471 1.00 33.67 ? 1954 VAL B N 1 ATOM 5162 C CA . VAL B 2 418 ? 21.287 19.748 5.240 1.00 33.74 ? 1954 VAL B CA 1 ATOM 5163 C C . VAL B 2 418 ? 20.252 20.836 5.447 1.00 33.71 ? 1954 VAL B C 1 ATOM 5164 O O . VAL B 2 418 ? 20.545 21.862 6.063 1.00 35.90 ? 1954 VAL B O 1 ATOM 5165 C CB . VAL B 2 418 ? 21.748 19.268 6.622 1.00 37.09 ? 1954 VAL B CB 1 ATOM 5166 C CG1 . VAL B 2 418 ? 20.552 19.075 7.560 1.00 32.59 ? 1954 VAL B CG1 1 ATOM 5167 C CG2 . VAL B 2 418 ? 22.547 17.976 6.458 1.00 41.37 ? 1954 VAL B CG2 1 ATOM 5168 N N . ALA B 2 419 ? 19.040 20.608 4.950 1.00 32.11 ? 1955 ALA B N 1 ATOM 5169 C CA . ALA B 2 419 ? 17.960 21.565 5.118 1.00 32.56 ? 1955 ALA B CA 1 ATOM 5170 C C . ALA B 2 419 ? 16.840 20.976 5.977 1.00 34.94 ? 1955 ALA B C 1 ATOM 5171 O O . ALA B 2 419 ? 16.623 19.768 5.967 1.00 32.95 ? 1955 ALA B O 1 ATOM 5172 C CB . ALA B 2 419 ? 17.424 21.979 3.788 1.00 27.06 ? 1955 ALA B CB 1 ATOM 5173 N N . TYR B 2 420 ? 16.154 21.840 6.732 1.00 39.07 ? 1956 TYR B N 1 ATOM 5174 C CA . TYR B 2 420 ? 15.046 21.426 7.610 1.00 39.24 ? 1956 TYR B CA 1 ATOM 5175 C C . TYR B 2 420 ? 13.825 22.356 7.515 1.00 40.03 ? 1956 TYR B C 1 ATOM 5176 O O . TYR B 2 420 ? 13.923 23.511 7.085 1.00 38.52 ? 1956 TYR B O 1 ATOM 5177 C CB . TYR B 2 420 ? 15.505 21.332 9.081 1.00 35.28 ? 1956 TYR B CB 1 ATOM 5178 C CG . TYR B 2 420 ? 16.067 22.618 9.660 1.00 30.25 ? 1956 TYR B CG 1 ATOM 5179 C CD1 . TYR B 2 420 ? 17.380 22.991 9.437 1.00 27.43 ? 1956 TYR B CD1 1 ATOM 5180 C CD2 . TYR B 2 420 ? 15.271 23.459 10.433 1.00 29.76 ? 1956 TYR B CD2 1 ATOM 5181 C CE1 . TYR B 2 420 ? 17.887 24.169 9.975 1.00 29.69 ? 1956 TYR B CE1 1 ATOM 5182 C CE2 . TYR B 2 420 ? 15.764 24.634 10.968 1.00 26.64 ? 1956 TYR B CE2 1 ATOM 5183 C CZ . TYR B 2 420 ? 17.065 24.984 10.741 1.00 28.58 ? 1956 TYR B CZ 1 ATOM 5184 O OH . TYR B 2 420 ? 17.545 26.151 11.282 1.00 33.49 ? 1956 TYR B OH 1 ATOM 5185 N N . SER B 2 421 ? 12.685 21.828 7.939 1.00 41.39 ? 1957 SER B N 1 ATOM 5186 C CA . SER B 2 421 ? 11.419 22.525 7.889 1.00 44.58 ? 1957 SER B CA 1 ATOM 5187 C C . SER B 2 421 ? 10.454 21.919 8.916 1.00 48.35 ? 1957 SER B C 1 ATOM 5188 O O . SER B 2 421 ? 10.595 20.756 9.311 1.00 48.12 ? 1957 SER B O 1 ATOM 5189 C CB . SER B 2 421 ? 10.837 22.383 6.483 1.00 46.10 ? 1957 SER B CB 1 ATOM 5190 O OG . SER B 2 421 ? 9.590 23.040 6.348 1.00 52.04 ? 1957 SER B OG 1 ATOM 5191 N N . LEU B 2 422 ? 9.472 22.709 9.343 1.00 51.09 ? 1958 LEU B N 1 ATOM 5192 C CA . LEU B 2 422 ? 8.493 22.246 10.318 1.00 55.40 ? 1958 LEU B CA 1 ATOM 5193 C C . LEU B 2 422 ? 7.192 21.924 9.599 1.00 58.52 ? 1958 LEU B C 1 ATOM 5194 O O . LEU B 2 422 ? 6.434 21.053 10.029 1.00 59.31 ? 1958 LEU B O 1 ATOM 5195 C CB . LEU B 2 422 ? 8.210 23.335 11.362 1.00 54.62 ? 1958 LEU B CB 1 ATOM 5196 C CG . LEU B 2 422 ? 9.340 24.123 12.035 1.00 54.20 ? 1958 LEU B CG 1 ATOM 5197 C CD1 . LEU B 2 422 ? 8.776 25.448 12.527 1.00 54.50 ? 1958 LEU B CD1 1 ATOM 5198 C CD2 . LEU B 2 422 ? 9.964 23.340 13.172 1.00 53.48 ? 1958 LEU B CD2 1 ATOM 5199 N N . ASP B 2 423 ? 6.956 22.641 8.500 1.00 62.42 ? 1959 ASP B N 1 ATOM 5200 C CA . ASP B 2 423 ? 5.740 22.518 7.694 1.00 66.00 ? 1959 ASP B CA 1 ATOM 5201 C C . ASP B 2 423 ? 5.898 21.751 6.390 1.00 67.94 ? 1959 ASP B C 1 ATOM 5202 O O . ASP B 2 423 ? 4.943 21.142 5.908 1.00 70.00 ? 1959 ASP B O 1 ATOM 5203 C CB . ASP B 2 423 ? 5.200 23.918 7.376 1.00 66.81 ? 1959 ASP B CB 1 ATOM 5204 C CG . ASP B 2 423 ? 6.262 24.831 6.769 1.00 70.00 ? 1959 ASP B CG 1 ATOM 5205 O OD1 . ASP B 2 423 ? 6.050 26.069 6.718 1.00 70.25 ? 1959 ASP B OD1 1 ATOM 5206 O OD2 . ASP B 2 423 ? 7.315 24.311 6.339 1.00 71.06 ? 1959 ASP B OD2 1 ATOM 5207 N N . ARG B 2 424 ? 7.098 21.801 5.825 1.00 69.00 ? 1960 ARG B N 1 ATOM 5208 C CA . ARG B 2 424 ? 7.432 21.147 4.562 1.00 70.62 ? 1960 ARG B CA 1 ATOM 5209 C C . ARG B 2 424 ? 7.354 22.181 3.440 1.00 70.72 ? 1960 ARG B C 1 ATOM 5210 O O . ARG B 2 424 ? 7.723 21.910 2.296 1.00 69.92 ? 1960 ARG B O 1 ATOM 5211 C CB . ARG B 2 424 ? 6.496 19.966 4.280 1.00 72.03 ? 1960 ARG B CB 1 ATOM 5212 C CG . ARG B 2 424 ? 7.159 18.822 3.527 1.00 75.36 ? 1960 ARG B CG 1 ATOM 5213 C CD . ARG B 2 424 ? 7.068 19.003 2.025 1.00 77.68 ? 1960 ARG B CD 1 ATOM 5214 N NE . ARG B 2 424 ? 5.754 18.609 1.522 1.00 80.18 ? 1960 ARG B NE 1 ATOM 5215 C CZ . ARG B 2 424 ? 5.341 17.349 1.425 1.00 80.31 ? 1960 ARG B CZ 1 ATOM 5216 N NH1 . ARG B 2 424 ? 6.143 16.357 1.792 1.00 79.15 ? 1960 ARG B NH1 1 ATOM 5217 N NH2 . ARG B 2 424 ? 4.122 17.083 0.967 1.00 80.59 ? 1960 ARG B NH2 1 ATOM 5218 N N . LYS B 2 425 ? 6.888 23.379 3.792 1.00 70.80 ? 1961 LYS B N 1 ATOM 5219 C CA . LYS B 2 425 ? 6.778 24.490 2.845 1.00 69.51 ? 1961 LYS B CA 1 ATOM 5220 C C . LYS B 2 425 ? 7.987 25.430 2.944 1.00 66.26 ? 1961 LYS B C 1 ATOM 5221 O O . LYS B 2 425 ? 8.572 25.795 1.936 1.00 65.72 ? 1961 LYS B O 1 ATOM 5222 C CB . LYS B 2 425 ? 5.481 25.275 3.089 1.00 71.55 ? 1961 LYS B CB 1 ATOM 5223 C CG . LYS B 2 425 ? 4.208 24.569 2.599 1.00 73.36 ? 1961 LYS B CG 1 ATOM 5224 C CD . LYS B 2 425 ? 4.072 24.594 1.069 1.00 73.56 ? 1961 LYS B CD 1 ATOM 5225 C CE . LYS B 2 425 ? 3.828 26.008 0.537 1.00 73.76 ? 1961 LYS B CE 1 ATOM 5226 N NZ . LYS B 2 425 ? 3.581 26.039 -0.933 1.00 71.99 ? 1961 LYS B NZ 1 ATOM 5227 N N . ASN B 2 426 ? 8.369 25.820 4.153 1.00 62.81 ? 1962 ASN B N 1 ATOM 5228 C CA . ASN B 2 426 ? 9.520 26.705 4.300 1.00 60.21 ? 1962 ASN B CA 1 ATOM 5229 C C . ASN B 2 426 ? 10.760 25.983 4.788 1.00 56.27 ? 1962 ASN B C 1 ATOM 5230 O O . ASN B 2 426 ? 10.819 25.549 5.932 1.00 57.21 ? 1962 ASN B O 1 ATOM 5231 C CB . ASN B 2 426 ? 9.217 27.850 5.265 1.00 61.69 ? 1962 ASN B CB 1 ATOM 5232 C CG . ASN B 2 426 ? 8.322 28.899 4.658 1.00 64.18 ? 1962 ASN B CG 1 ATOM 5233 O OD1 . ASN B 2 426 ? 7.116 28.707 4.535 1.00 68.69 ? 1962 ASN B OD1 1 ATOM 5234 N ND2 . ASN B 2 426 ? 8.911 30.017 4.261 1.00 64.88 ? 1962 ASN B ND2 1 ATOM 5235 N N . TRP B 2 427 ? 11.759 25.881 3.925 1.00 50.14 ? 1963 TRP B N 1 ATOM 5236 C CA . TRP B 2 427 ? 12.999 25.214 4.286 1.00 44.69 ? 1963 TRP B CA 1 ATOM 5237 C C . TRP B 2 427 ? 14.097 26.160 4.716 1.00 43.58 ? 1963 TRP B C 1 ATOM 5238 O O . TRP B 2 427 ? 14.077 27.348 4.421 1.00 44.03 ? 1963 TRP B O 1 ATOM 5239 C CB . TRP B 2 427 ? 13.511 24.387 3.114 1.00 41.03 ? 1963 TRP B CB 1 ATOM 5240 C CG . TRP B 2 427 ? 12.619 23.271 2.805 1.00 39.37 ? 1963 TRP B CG 1 ATOM 5241 C CD1 . TRP B 2 427 ? 11.526 23.290 1.988 1.00 39.52 ? 1963 TRP B CD1 1 ATOM 5242 C CD2 . TRP B 2 427 ? 12.684 21.956 3.361 1.00 39.82 ? 1963 TRP B CD2 1 ATOM 5243 N NE1 . TRP B 2 427 ? 10.903 22.065 2.000 1.00 39.69 ? 1963 TRP B NE1 1 ATOM 5244 C CE2 . TRP B 2 427 ? 11.594 21.227 2.834 1.00 37.73 ? 1963 TRP B CE2 1 ATOM 5245 C CE3 . TRP B 2 427 ? 13.558 21.320 4.254 1.00 39.43 ? 1963 TRP B CE3 1 ATOM 5246 C CZ2 . TRP B 2 427 ? 11.359 19.906 3.164 1.00 34.13 ? 1963 TRP B CZ2 1 ATOM 5247 C CZ3 . TRP B 2 427 ? 13.322 20.009 4.578 1.00 38.91 ? 1963 TRP B CZ3 1 ATOM 5248 C CH2 . TRP B 2 427 ? 12.229 19.313 4.031 1.00 37.78 ? 1963 TRP B CH2 1 ATOM 5249 N N . ARG B 2 428 ? 15.066 25.621 5.432 1.00 42.45 ? 1964 ARG B N 1 ATOM 5250 C CA . ARG B 2 428 ? 16.192 26.422 5.855 1.00 42.22 ? 1964 ARG B CA 1 ATOM 5251 C C . ARG B 2 428 ? 17.432 25.566 5.671 1.00 40.66 ? 1964 ARG B C 1 ATOM 5252 O O . ARG B 2 428 ? 17.515 24.465 6.224 1.00 40.97 ? 1964 ARG B O 1 ATOM 5253 C CB . ARG B 2 428 ? 16.041 26.848 7.321 1.00 43.16 ? 1964 ARG B CB 1 ATOM 5254 C CG . ARG B 2 428 ? 14.946 27.875 7.564 1.00 45.40 ? 1964 ARG B CG 1 ATOM 5255 C CD . ARG B 2 428 ? 15.090 28.542 8.923 1.00 47.07 ? 1964 ARG B CD 1 ATOM 5256 N NE . ARG B 2 428 ? 14.260 27.930 9.960 1.00 49.56 ? 1964 ARG B NE 1 ATOM 5257 C CZ . ARG B 2 428 ? 14.325 28.252 11.253 1.00 49.84 ? 1964 ARG B CZ 1 ATOM 5258 N NH1 . ARG B 2 428 ? 15.183 29.177 11.661 1.00 46.97 ? 1964 ARG B NH1 1 ATOM 5259 N NH2 . ARG B 2 428 ? 13.536 27.649 12.140 1.00 47.39 ? 1964 ARG B NH2 1 ATOM 5260 N N . ILE B 2 429 ? 18.366 26.046 4.856 1.00 37.05 ? 1965 ILE B N 1 ATOM 5261 C CA . ILE B 2 429 ? 19.599 25.318 4.644 1.00 35.79 ? 1965 ILE B CA 1 ATOM 5262 C C . ILE B 2 429 ? 20.402 25.595 5.904 1.00 35.12 ? 1965 ILE B C 1 ATOM 5263 O O . ILE B 2 429 ? 20.598 26.745 6.271 1.00 34.86 ? 1965 ILE B O 1 ATOM 5264 C CB . ILE B 2 429 ? 20.397 25.827 3.422 1.00 37.89 ? 1965 ILE B CB 1 ATOM 5265 C CG1 . ILE B 2 429 ? 19.726 25.425 2.104 1.00 37.45 ? 1965 ILE B CG1 1 ATOM 5266 C CG2 . ILE B 2 429 ? 21.764 25.174 3.414 1.00 39.31 ? 1965 ILE B CG2 1 ATOM 5267 C CD1 . ILE B 2 429 ? 18.373 26.016 1.852 1.00 41.12 ? 1965 ILE B CD1 1 ATOM 5268 N N . PHE B 2 430 ? 20.855 24.544 6.581 1.00 33.50 ? 1966 PHE B N 1 ATOM 5269 C CA . PHE B 2 430 ? 21.606 24.735 7.802 1.00 33.33 ? 1966 PHE B CA 1 ATOM 5270 C C . PHE B 2 430 ? 22.965 25.387 7.645 1.00 35.48 ? 1966 PHE B C 1 ATOM 5271 O O . PHE B 2 430 ? 23.694 25.161 6.668 1.00 36.22 ? 1966 PHE B O 1 ATOM 5272 C CB . PHE B 2 430 ? 21.765 23.417 8.524 1.00 31.27 ? 1966 PHE B CB 1 ATOM 5273 C CG . PHE B 2 430 ? 22.548 23.514 9.796 1.00 29.63 ? 1966 PHE B CG 1 ATOM 5274 C CD1 . PHE B 2 430 ? 23.930 23.326 9.797 1.00 29.23 ? 1966 PHE B CD1 1 ATOM 5275 C CD2 . PHE B 2 430 ? 21.903 23.797 11.000 1.00 27.68 ? 1966 PHE B CD2 1 ATOM 5276 C CE1 . PHE B 2 430 ? 24.660 23.419 10.988 1.00 30.41 ? 1966 PHE B CE1 1 ATOM 5277 C CE2 . PHE B 2 430 ? 22.614 23.894 12.191 1.00 26.70 ? 1966 PHE B CE2 1 ATOM 5278 C CZ . PHE B 2 430 ? 23.994 23.706 12.191 1.00 29.00 ? 1966 PHE B CZ 1 ATOM 5279 N N . LYS B 2 431 ? 23.292 26.197 8.641 1.00 35.98 ? 1967 LYS B N 1 ATOM 5280 C CA . LYS B 2 431 ? 24.553 26.916 8.708 1.00 38.58 ? 1967 LYS B CA 1 ATOM 5281 C C . LYS B 2 431 ? 24.929 26.922 10.191 1.00 41.95 ? 1967 LYS B C 1 ATOM 5282 O O . LYS B 2 431 ? 24.118 26.569 11.044 1.00 44.14 ? 1967 LYS B O 1 ATOM 5283 C CB . LYS B 2 431 ? 24.350 28.338 8.186 1.00 36.66 ? 1967 LYS B CB 1 ATOM 5284 C CG . LYS B 2 431 ? 25.580 29.204 8.229 1.00 40.51 ? 1967 LYS B CG 1 ATOM 5285 C CD . LYS B 2 431 ? 25.280 30.658 7.827 1.00 41.77 ? 1967 LYS B CD 1 ATOM 5286 C CE . LYS B 2 431 ? 26.541 31.530 7.935 1.00 46.11 ? 1967 LYS B CE 1 ATOM 5287 N NZ . LYS B 2 431 ? 26.393 32.906 7.372 1.00 43.68 ? 1967 LYS B NZ 1 ATOM 5288 N N . GLY B 2 432 ? 26.155 27.303 10.501 1.00 43.94 ? 1968 GLY B N 1 ATOM 5289 C CA . GLY B 2 432 ? 26.589 27.357 11.888 1.00 45.91 ? 1968 GLY B CA 1 ATOM 5290 C C . GLY B 2 432 ? 27.983 27.913 11.766 1.00 49.57 ? 1968 GLY B C 1 ATOM 5291 O O . GLY B 2 432 ? 28.180 29.067 11.397 1.00 51.49 ? 1968 GLY B O 1 ATOM 5292 N N . ASN B 2 433 ? 28.963 27.092 12.073 1.00 51.85 ? 1969 ASN B N 1 ATOM 5293 C CA . ASN B 2 433 ? 30.337 27.497 11.895 1.00 55.32 ? 1969 ASN B CA 1 ATOM 5294 C C . ASN B 2 433 ? 30.485 28.092 10.495 1.00 56.84 ? 1969 ASN B C 1 ATOM 5295 O O . ASN B 2 433 ? 30.903 29.241 10.326 1.00 58.11 ? 1969 ASN B O 1 ATOM 5296 C CB . ASN B 2 433 ? 31.235 26.274 11.955 1.00 58.26 ? 1969 ASN B CB 1 ATOM 5297 C CG . ASN B 2 433 ? 31.764 26.030 13.308 1.00 62.20 ? 1969 ASN B CG 1 ATOM 5298 O OD1 . ASN B 2 433 ? 32.638 26.751 13.751 1.00 66.39 ? 1969 ASN B OD1 1 ATOM 5299 N ND2 . ASN B 2 433 ? 31.223 25.031 13.986 1.00 66.77 ? 1969 ASN B ND2 1 ATOM 5300 N N . SER B 2 434 ? 30.119 27.279 9.504 1.00 55.41 ? 1970 SER B N 1 ATOM 5301 C CA . SER B 2 434 ? 30.258 27.595 8.081 1.00 57.43 ? 1970 SER B CA 1 ATOM 5302 C C . SER B 2 434 ? 30.753 28.973 7.667 1.00 58.33 ? 1970 SER B C 1 ATOM 5303 O O . SER B 2 434 ? 30.183 30.003 8.033 1.00 59.44 ? 1970 SER B O 1 ATOM 5304 C CB . SER B 2 434 ? 28.967 27.295 7.327 1.00 58.30 ? 1970 SER B CB 1 ATOM 5305 O OG . SER B 2 434 ? 29.219 27.344 5.929 1.00 53.22 ? 1970 SER B OG 1 ATOM 5306 N N . THR B 2 435 ? 31.818 28.977 6.875 1.00 58.91 ? 1971 THR B N 1 ATOM 5307 C CA . THR B 2 435 ? 32.399 30.222 6.387 1.00 59.53 ? 1971 THR B CA 1 ATOM 5308 C C . THR B 2 435 ? 31.694 30.632 5.093 1.00 58.00 ? 1971 THR B C 1 ATOM 5309 O O . THR B 2 435 ? 31.871 31.739 4.585 1.00 57.99 ? 1971 THR B O 1 ATOM 5310 C CB . THR B 2 435 ? 33.901 30.060 6.118 1.00 59.86 ? 1971 THR B CB 1 ATOM 5311 O OG1 . THR B 2 435 ? 34.533 29.507 7.279 1.00 62.95 ? 1971 THR B OG1 1 ATOM 5312 C CG2 . THR B 2 435 ? 34.530 31.407 5.824 1.00 62.75 ? 1971 THR B CG2 1 ATOM 5313 N N . ARG B 2 436 ? 30.880 29.730 4.570 1.00 55.86 ? 1972 ARG B N 1 ATOM 5314 C CA . ARG B 2 436 ? 30.152 30.009 3.352 1.00 54.15 ? 1972 ARG B CA 1 ATOM 5315 C C . ARG B 2 436 ? 28.701 30.352 3.697 1.00 52.21 ? 1972 ARG B C 1 ATOM 5316 O O . ARG B 2 436 ? 28.304 30.308 4.858 1.00 51.42 ? 1972 ARG B O 1 ATOM 5317 C CB . ARG B 2 436 ? 30.213 28.794 2.420 1.00 54.92 ? 1972 ARG B CB 1 ATOM 5318 C CG . ARG B 2 436 ? 31.611 28.196 2.227 1.00 53.96 ? 1972 ARG B CG 1 ATOM 5319 C CD . ARG B 2 436 ? 31.726 27.681 0.803 1.00 58.58 ? 1972 ARG B CD 1 ATOM 5320 N NE . ARG B 2 436 ? 32.174 26.291 0.677 1.00 59.14 ? 1972 ARG B NE 1 ATOM 5321 C CZ . ARG B 2 436 ? 31.860 25.514 -0.359 1.00 57.12 ? 1972 ARG B CZ 1 ATOM 5322 N NH1 . ARG B 2 436 ? 31.102 25.995 -1.335 1.00 58.02 ? 1972 ARG B NH1 1 ATOM 5323 N NH2 . ARG B 2 436 ? 32.304 24.269 -0.431 1.00 57.03 ? 1972 ARG B NH2 1 ATOM 5324 N N . ASN B 2 437 ? 27.914 30.693 2.685 1.00 51.04 ? 1973 ASN B N 1 ATOM 5325 C CA . ASN B 2 437 ? 26.520 31.052 2.895 1.00 51.35 ? 1973 ASN B CA 1 ATOM 5326 C C . ASN B 2 437 ? 25.754 29.972 3.640 1.00 49.85 ? 1973 ASN B C 1 ATOM 5327 O O . ASN B 2 437 ? 24.767 30.266 4.330 1.00 49.58 ? 1973 ASN B O 1 ATOM 5328 C CB . ASN B 2 437 ? 25.855 31.332 1.556 1.00 56.13 ? 1973 ASN B CB 1 ATOM 5329 C CG . ASN B 2 437 ? 26.486 32.512 0.835 1.00 63.56 ? 1973 ASN B CG 1 ATOM 5330 O OD1 . ASN B 2 437 ? 26.161 32.792 -0.326 1.00 67.17 ? 1973 ASN B OD1 1 ATOM 5331 N ND2 . ASN B 2 437 ? 27.394 33.218 1.521 1.00 62.69 ? 1973 ASN B ND2 1 ATOM 5332 N N . VAL B 2 438 ? 26.211 28.725 3.489 1.00 45.32 ? 1974 VAL B N 1 ATOM 5333 C CA . VAL B 2 438 ? 25.603 27.568 4.145 1.00 39.45 ? 1974 VAL B CA 1 ATOM 5334 C C . VAL B 2 438 ? 26.669 26.577 4.556 1.00 37.32 ? 1974 VAL B C 1 ATOM 5335 O O . VAL B 2 438 ? 27.794 26.638 4.094 1.00 36.24 ? 1974 VAL B O 1 ATOM 5336 C CB . VAL B 2 438 ? 24.623 26.813 3.231 1.00 38.18 ? 1974 VAL B CB 1 ATOM 5337 C CG1 . VAL B 2 438 ? 23.537 27.730 2.770 1.00 37.24 ? 1974 VAL B CG1 1 ATOM 5338 C CG2 . VAL B 2 438 ? 25.362 26.202 2.063 1.00 36.82 ? 1974 VAL B CG2 1 ATOM 5339 N N . MET B 2 439 ? 26.301 25.655 5.430 1.00 35.07 ? 1975 MET B N 1 ATOM 5340 C CA . MET B 2 439 ? 27.233 24.643 5.880 1.00 34.81 ? 1975 MET B CA 1 ATOM 5341 C C . MET B 2 439 ? 27.425 23.578 4.800 1.00 35.55 ? 1975 MET B C 1 ATOM 5342 O O . MET B 2 439 ? 26.459 23.017 4.273 1.00 33.80 ? 1975 MET B O 1 ATOM 5343 C CB . MET B 2 439 ? 26.702 23.992 7.153 1.00 35.28 ? 1975 MET B CB 1 ATOM 5344 C CG . MET B 2 439 ? 27.519 22.837 7.645 1.00 34.47 ? 1975 MET B CG 1 ATOM 5345 S SD . MET B 2 439 ? 29.167 23.342 8.015 1.00 39.54 ? 1975 MET B SD 1 ATOM 5346 C CE . MET B 2 439 ? 29.065 23.714 9.760 1.00 34.55 ? 1975 MET B CE 1 ATOM 5347 N N . TYR B 2 440 ? 28.675 23.313 4.448 1.00 35.63 ? 1976 TYR B N 1 ATOM 5348 C CA . TYR B 2 440 ? 28.934 22.270 3.466 1.00 34.51 ? 1976 TYR B CA 1 ATOM 5349 C C . TYR B 2 440 ? 29.612 21.126 4.189 1.00 31.80 ? 1976 TYR B C 1 ATOM 5350 O O . TYR B 2 440 ? 30.825 21.047 4.234 1.00 34.72 ? 1976 TYR B O 1 ATOM 5351 C CB . TYR B 2 440 ? 29.810 22.801 2.327 1.00 36.53 ? 1976 TYR B CB 1 ATOM 5352 C CG . TYR B 2 440 ? 29.051 23.685 1.347 1.00 36.39 ? 1976 TYR B CG 1 ATOM 5353 C CD1 . TYR B 2 440 ? 29.150 25.081 1.402 1.00 35.50 ? 1976 TYR B CD1 1 ATOM 5354 C CD2 . TYR B 2 440 ? 28.198 23.120 0.395 1.00 32.93 ? 1976 TYR B CD2 1 ATOM 5355 C CE1 . TYR B 2 440 ? 28.413 25.895 0.530 1.00 35.83 ? 1976 TYR B CE1 1 ATOM 5356 C CE2 . TYR B 2 440 ? 27.463 23.908 -0.469 1.00 35.37 ? 1976 TYR B CE2 1 ATOM 5357 C CZ . TYR B 2 440 ? 27.569 25.297 -0.403 1.00 39.27 ? 1976 TYR B CZ 1 ATOM 5358 O OH . TYR B 2 440 ? 26.822 26.071 -1.271 1.00 43.31 ? 1976 TYR B OH 1 ATOM 5359 N N . PHE B 2 441 ? 28.809 20.251 4.776 1.00 30.93 ? 1977 PHE B N 1 ATOM 5360 C CA . PHE B 2 441 ? 29.322 19.109 5.525 1.00 29.71 ? 1977 PHE B CA 1 ATOM 5361 C C . PHE B 2 441 ? 30.244 18.239 4.668 1.00 31.54 ? 1977 PHE B C 1 ATOM 5362 O O . PHE B 2 441 ? 30.007 18.052 3.473 1.00 34.68 ? 1977 PHE B O 1 ATOM 5363 C CB . PHE B 2 441 ? 28.164 18.247 6.060 1.00 26.87 ? 1977 PHE B CB 1 ATOM 5364 C CG . PHE B 2 441 ? 27.279 18.940 7.091 1.00 24.17 ? 1977 PHE B CG 1 ATOM 5365 C CD1 . PHE B 2 441 ? 26.039 19.479 6.728 1.00 23.20 ? 1977 PHE B CD1 1 ATOM 5366 C CD2 . PHE B 2 441 ? 27.666 19.022 8.430 1.00 22.57 ? 1977 PHE B CD2 1 ATOM 5367 C CE1 . PHE B 2 441 ? 25.208 20.076 7.677 1.00 19.88 ? 1977 PHE B CE1 1 ATOM 5368 C CE2 . PHE B 2 441 ? 26.833 19.628 9.390 1.00 20.48 ? 1977 PHE B CE2 1 ATOM 5369 C CZ . PHE B 2 441 ? 25.609 20.149 9.011 1.00 18.75 ? 1977 PHE B CZ 1 ATOM 5370 N N . GLY B 2 442 ? 31.304 17.724 5.283 1.00 31.02 ? 1978 GLY B N 1 ATOM 5371 C CA . GLY B 2 442 ? 32.233 16.866 4.578 1.00 30.24 ? 1978 GLY B CA 1 ATOM 5372 C C . GLY B 2 442 ? 31.681 15.461 4.649 1.00 33.24 ? 1978 GLY B C 1 ATOM 5373 O O . GLY B 2 442 ? 31.276 14.999 5.718 1.00 32.55 ? 1978 GLY B O 1 ATOM 5374 N N . GLY B 2 443 ? 31.648 14.779 3.510 1.00 35.41 ? 1979 GLY B N 1 ATOM 5375 C CA . GLY B 2 443 ? 31.119 13.422 3.486 1.00 39.17 ? 1979 GLY B CA 1 ATOM 5376 C C . GLY B 2 443 ? 32.092 12.275 3.723 1.00 38.29 ? 1979 GLY B C 1 ATOM 5377 O O . GLY B 2 443 ? 33.050 12.374 4.499 1.00 37.23 ? 1979 GLY B O 1 ATOM 5378 N N . ASN B 2 444 ? 31.849 11.168 3.036 1.00 38.02 ? 1980 ASN B N 1 ATOM 5379 C CA . ASN B 2 444 ? 32.709 10.014 3.207 1.00 38.68 ? 1980 ASN B CA 1 ATOM 5380 C C . ASN B 2 444 ? 33.946 9.961 2.308 1.00 37.70 ? 1980 ASN B C 1 ATOM 5381 O O . ASN B 2 444 ? 34.023 10.629 1.286 1.00 37.80 ? 1980 ASN B O 1 ATOM 5382 C CB . ASN B 2 444 ? 31.886 8.741 3.046 1.00 39.20 ? 1980 ASN B CB 1 ATOM 5383 C CG . ASN B 2 444 ? 30.835 8.582 4.136 1.00 37.33 ? 1980 ASN B CG 1 ATOM 5384 O OD1 . ASN B 2 444 ? 29.672 8.933 3.953 1.00 38.27 ? 1980 ASN B OD1 1 ATOM 5385 N ND2 . ASN B 2 444 ? 31.247 8.055 5.270 1.00 34.69 ? 1980 ASN B ND2 1 ATOM 5386 N N . SER B 2 445 ? 34.925 9.172 2.738 1.00 40.21 ? 1981 SER B N 1 ATOM 5387 C CA . SER B 2 445 ? 36.179 8.975 2.016 1.00 41.82 ? 1981 SER B CA 1 ATOM 5388 C C . SER B 2 445 ? 36.120 7.636 1.284 1.00 43.10 ? 1981 SER B C 1 ATOM 5389 O O . SER B 2 445 ? 36.590 7.520 0.162 1.00 45.42 ? 1981 SER B O 1 ATOM 5390 C CB . SER B 2 445 ? 37.350 8.968 2.992 1.00 42.92 ? 1981 SER B CB 1 ATOM 5391 O OG . SER B 2 445 ? 37.595 10.265 3.501 1.00 45.20 ? 1981 SER B OG 1 ATOM 5392 N N . ASP B 2 446 ? 35.534 6.634 1.936 1.00 42.55 ? 1982 ASP B N 1 ATOM 5393 C CA . ASP B 2 446 ? 35.372 5.310 1.364 1.00 40.89 ? 1982 ASP B CA 1 ATOM 5394 C C . ASP B 2 446 ? 33.892 4.898 1.378 1.00 41.90 ? 1982 ASP B C 1 ATOM 5395 O O . ASP B 2 446 ? 33.038 5.644 1.852 1.00 42.74 ? 1982 ASP B O 1 ATOM 5396 C CB . ASP B 2 446 ? 36.190 4.311 2.153 1.00 40.55 ? 1982 ASP B CB 1 ATOM 5397 C CG . ASP B 2 446 ? 35.820 4.284 3.603 1.00 42.33 ? 1982 ASP B CG 1 ATOM 5398 O OD1 . ASP B 2 446 ? 34.608 4.279 3.904 1.00 42.75 ? 1982 ASP B OD1 1 ATOM 5399 O OD2 . ASP B 2 446 ? 36.744 4.256 4.445 1.00 45.55 ? 1982 ASP B OD2 1 ATOM 5400 N N . ALA B 2 447 ? 33.583 3.707 0.881 1.00 41.44 ? 1983 ALA B N 1 ATOM 5401 C CA . ALA B 2 447 ? 32.195 3.271 0.834 1.00 41.47 ? 1983 ALA B CA 1 ATOM 5402 C C . ALA B 2 447 ? 31.644 2.496 2.028 1.00 42.28 ? 1983 ALA B C 1 ATOM 5403 O O . ALA B 2 447 ? 30.494 2.065 1.990 1.00 41.42 ? 1983 ALA B O 1 ATOM 5404 C CB . ALA B 2 447 ? 31.954 2.484 -0.428 1.00 42.79 ? 1983 ALA B CB 1 ATOM 5405 N N . SER B 2 448 ? 32.431 2.325 3.087 1.00 43.76 ? 1984 SER B N 1 ATOM 5406 C CA . SER B 2 448 ? 31.935 1.594 4.257 1.00 45.61 ? 1984 SER B CA 1 ATOM 5407 C C . SER B 2 448 ? 32.083 2.318 5.605 1.00 45.19 ? 1984 SER B C 1 ATOM 5408 O O . SER B 2 448 ? 31.229 2.170 6.480 1.00 45.85 ? 1984 SER B O 1 ATOM 5409 C CB . SER B 2 448 ? 32.600 0.221 4.352 1.00 44.51 ? 1984 SER B CB 1 ATOM 5410 O OG . SER B 2 448 ? 33.967 0.361 4.689 1.00 51.40 ? 1984 SER B OG 1 ATOM 5411 N N . THR B 2 449 ? 33.148 3.093 5.786 1.00 42.97 ? 1985 THR B N 1 ATOM 5412 C CA . THR B 2 449 ? 33.327 3.788 7.053 1.00 43.86 ? 1985 THR B CA 1 ATOM 5413 C C . THR B 2 449 ? 32.227 4.812 7.329 1.00 43.59 ? 1985 THR B C 1 ATOM 5414 O O . THR B 2 449 ? 31.679 5.435 6.417 1.00 43.70 ? 1985 THR B O 1 ATOM 5415 C CB . THR B 2 449 ? 34.669 4.508 7.111 1.00 45.60 ? 1985 THR B CB 1 ATOM 5416 O OG1 . THR B 2 449 ? 35.699 3.641 6.621 1.00 49.40 ? 1985 THR B OG1 1 ATOM 5417 C CG2 . THR B 2 449 ? 34.986 4.899 8.551 1.00 45.32 ? 1985 THR B CG2 1 ATOM 5418 N N . ILE B 2 450 ? 31.898 4.984 8.599 1.00 43.02 ? 1986 ILE B N 1 ATOM 5419 C CA . ILE B 2 450 ? 30.867 5.940 8.968 1.00 41.74 ? 1986 ILE B CA 1 ATOM 5420 C C . ILE B 2 450 ? 31.460 7.305 9.235 1.00 41.47 ? 1986 ILE B C 1 ATOM 5421 O O . ILE B 2 450 ? 32.434 7.432 9.967 1.00 40.51 ? 1986 ILE B O 1 ATOM 5422 C CB . ILE B 2 450 ? 30.131 5.531 10.234 1.00 38.13 ? 1986 ILE B CB 1 ATOM 5423 C CG1 . ILE B 2 450 ? 29.512 4.143 10.059 1.00 40.89 ? 1986 ILE B CG1 1 ATOM 5424 C CG2 . ILE B 2 450 ? 29.052 6.539 10.526 1.00 38.25 ? 1986 ILE B CG2 1 ATOM 5425 C CD1 . ILE B 2 450 ? 28.898 3.563 11.339 1.00 33.57 ? 1986 ILE B CD1 1 ATOM 5426 N N . LYS B 2 451 ? 30.851 8.323 8.640 1.00 42.66 ? 1987 LYS B N 1 ATOM 5427 C CA . LYS B 2 451 ? 31.275 9.704 8.827 1.00 42.47 ? 1987 LYS B CA 1 ATOM 5428 C C . LYS B 2 451 ? 30.302 10.414 9.775 1.00 41.83 ? 1987 LYS B C 1 ATOM 5429 O O . LYS B 2 451 ? 29.105 10.522 9.508 1.00 43.44 ? 1987 LYS B O 1 ATOM 5430 C CB . LYS B 2 451 ? 31.325 10.431 7.480 1.00 42.62 ? 1987 LYS B CB 1 ATOM 5431 C CG . LYS B 2 451 ? 31.630 11.919 7.576 1.00 40.98 ? 1987 LYS B CG 1 ATOM 5432 C CD . LYS B 2 451 ? 32.922 12.173 8.299 1.00 39.52 ? 1987 LYS B CD 1 ATOM 5433 C CE . LYS B 2 451 ? 33.333 13.627 8.227 1.00 39.77 ? 1987 LYS B CE 1 ATOM 5434 N NZ . LYS B 2 451 ? 34.493 13.870 9.138 1.00 41.17 ? 1987 LYS B NZ 1 ATOM 5435 N N . GLU B 2 452 ? 30.839 10.889 10.885 1.00 41.36 ? 1988 GLU B N 1 ATOM 5436 C CA . GLU B 2 452 ? 30.079 11.591 11.905 1.00 42.92 ? 1988 GLU B CA 1 ATOM 5437 C C . GLU B 2 452 ? 30.112 13.116 11.696 1.00 41.93 ? 1988 GLU B C 1 ATOM 5438 O O . GLU B 2 452 ? 31.174 13.707 11.489 1.00 44.47 ? 1988 GLU B O 1 ATOM 5439 C CB . GLU B 2 452 ? 30.652 11.231 13.274 1.00 46.21 ? 1988 GLU B CB 1 ATOM 5440 C CG . GLU B 2 452 ? 32.177 11.427 13.372 1.00 54.18 ? 1988 GLU B CG 1 ATOM 5441 C CD . GLU B 2 452 ? 33.001 10.376 12.601 1.00 57.23 ? 1988 GLU B CD 1 ATOM 5442 O OE1 . GLU B 2 452 ? 32.969 9.175 12.977 1.00 58.40 ? 1988 GLU B OE1 1 ATOM 5443 O OE2 . GLU B 2 452 ? 33.686 10.758 11.625 1.00 56.48 ? 1988 GLU B OE2 1 ATOM 5444 N N . ASN B 2 453 ? 28.942 13.743 11.737 1.00 38.29 ? 1989 ASN B N 1 ATOM 5445 C CA . ASN B 2 453 ? 28.829 15.182 11.563 1.00 34.52 ? 1989 ASN B CA 1 ATOM 5446 C C . ASN B 2 453 ? 27.874 15.776 12.600 1.00 34.95 ? 1989 ASN B C 1 ATOM 5447 O O . ASN B 2 453 ? 26.736 15.346 12.759 1.00 33.24 ? 1989 ASN B O 1 ATOM 5448 C CB . ASN B 2 453 ? 28.319 15.519 10.157 1.00 36.54 ? 1989 ASN B CB 1 ATOM 5449 C CG . ASN B 2 453 ? 29.438 15.861 9.169 1.00 38.00 ? 1989 ASN B CG 1 ATOM 5450 O OD1 . ASN B 2 453 ? 30.165 16.841 9.339 1.00 37.52 ? 1989 ASN B OD1 1 ATOM 5451 N ND2 . ASN B 2 453 ? 29.554 15.063 8.109 1.00 37.74 ? 1989 ASN B ND2 1 ATOM 5452 N N . GLN B 2 454 ? 28.344 16.790 13.300 1.00 38.14 ? 1990 GLN B N 1 ATOM 5453 C CA . GLN B 2 454 ? 27.544 17.464 14.308 1.00 41.47 ? 1990 GLN B CA 1 ATOM 5454 C C . GLN B 2 454 ? 26.730 18.616 13.720 1.00 40.57 ? 1990 GLN B C 1 ATOM 5455 O O . GLN B 2 454 ? 27.024 19.110 12.643 1.00 41.27 ? 1990 GLN B O 1 ATOM 5456 C CB . GLN B 2 454 ? 28.482 18.003 15.386 1.00 47.33 ? 1990 GLN B CB 1 ATOM 5457 C CG . GLN B 2 454 ? 27.811 18.726 16.526 1.00 52.59 ? 1990 GLN B CG 1 ATOM 5458 C CD . GLN B 2 454 ? 28.731 18.858 17.716 1.00 55.80 ? 1990 GLN B CD 1 ATOM 5459 O OE1 . GLN B 2 454 ? 29.803 19.466 17.627 1.00 58.24 ? 1990 GLN B OE1 1 ATOM 5460 N NE2 . GLN B 2 454 ? 28.326 18.282 18.838 1.00 56.37 ? 1990 GLN B NE2 1 ATOM 5461 N N . ILE B 2 455 ? 25.687 19.026 14.428 1.00 43.21 ? 1991 ILE B N 1 ATOM 5462 C CA . ILE B 2 455 ? 24.866 20.168 14.015 1.00 45.84 ? 1991 ILE B CA 1 ATOM 5463 C C . ILE B 2 455 ? 25.284 21.255 15.045 1.00 47.93 ? 1991 ILE B C 1 ATOM 5464 O O . ILE B 2 455 ? 24.979 21.103 16.225 1.00 47.62 ? 1991 ILE B O 1 ATOM 5465 C CB . ILE B 2 455 ? 23.359 19.789 14.110 1.00 42.57 ? 1991 ILE B CB 1 ATOM 5466 C CG1 . ILE B 2 455 ? 22.770 19.603 12.716 1.00 39.60 ? 1991 ILE B CG1 1 ATOM 5467 C CG2 . ILE B 2 455 ? 22.585 20.842 14.831 1.00 48.55 ? 1991 ILE B CG2 1 ATOM 5468 C CD1 . ILE B 2 455 ? 23.303 18.407 11.962 1.00 34.32 ? 1991 ILE B CD1 1 ATOM 5469 N N . ASP B 2 456 ? 25.992 22.319 14.614 1.00 51.26 ? 1992 ASP B N 1 ATOM 5470 C CA . ASP B 2 456 ? 26.509 23.355 15.563 1.00 50.26 ? 1992 ASP B CA 1 ATOM 5471 C C . ASP B 2 456 ? 25.522 23.607 16.679 1.00 44.08 ? 1992 ASP B C 1 ATOM 5472 O O . ASP B 2 456 ? 25.837 23.325 17.856 1.00 43.92 ? 1992 ASP B O 1 ATOM 5473 C CB . ASP B 2 456 ? 26.937 24.689 14.860 1.00 54.35 ? 1992 ASP B CB 1 ATOM 5474 C CG . ASP B 2 456 ? 27.638 25.726 15.844 1.00 61.76 ? 1992 ASP B CG 1 ATOM 5475 O OD1 . ASP B 2 456 ? 27.046 26.792 16.209 1.00 59.27 ? 1992 ASP B OD1 1 ATOM 5476 O OD2 . ASP B 2 456 ? 28.804 25.478 16.244 1.00 62.04 ? 1992 ASP B OD2 1 ATOM 5477 N N . PRO B 2 457 ? 24.346 24.180 16.352 1.00 37.86 ? 1993 PRO B N 1 ATOM 5478 C CA . PRO B 2 457 ? 23.321 24.437 17.379 1.00 34.32 ? 1993 PRO B CA 1 ATOM 5479 C C . PRO B 2 457 ? 22.120 23.544 17.065 1.00 31.74 ? 1993 PRO B C 1 ATOM 5480 O O . PRO B 2 457 ? 21.643 23.511 15.933 1.00 29.34 ? 1993 PRO B O 1 ATOM 5481 C CB . PRO B 2 457 ? 22.979 25.926 17.188 1.00 30.37 ? 1993 PRO B CB 1 ATOM 5482 C CG . PRO B 2 457 ? 24.028 26.438 16.208 1.00 28.68 ? 1993 PRO B CG 1 ATOM 5483 C CD . PRO B 2 457 ? 24.282 25.238 15.341 1.00 32.57 ? 1993 PRO B CD 1 ATOM 5484 N N . PRO B 2 458 ? 21.615 22.811 18.059 1.00 32.57 ? 1994 PRO B N 1 ATOM 5485 C CA . PRO B 2 458 ? 20.465 21.928 17.849 1.00 34.47 ? 1994 PRO B CA 1 ATOM 5486 C C . PRO B 2 458 ? 19.331 22.614 17.091 1.00 36.25 ? 1994 PRO B C 1 ATOM 5487 O O . PRO B 2 458 ? 19.036 23.790 17.345 1.00 40.36 ? 1994 PRO B O 1 ATOM 5488 C CB . PRO B 2 458 ? 20.057 21.564 19.271 1.00 33.25 ? 1994 PRO B CB 1 ATOM 5489 C CG . PRO B 2 458 ? 21.355 21.516 19.985 1.00 32.74 ? 1994 PRO B CG 1 ATOM 5490 C CD . PRO B 2 458 ? 22.058 22.763 19.461 1.00 35.13 ? 1994 PRO B CD 1 ATOM 5491 N N . VAL B 2 459 ? 18.697 21.903 16.160 1.00 32.32 ? 1995 VAL B N 1 ATOM 5492 C CA . VAL B 2 459 ? 17.585 22.510 15.421 1.00 32.10 ? 1995 VAL B CA 1 ATOM 5493 C C . VAL B 2 459 ? 16.297 21.712 15.585 1.00 32.20 ? 1995 VAL B C 1 ATOM 5494 O O . VAL B 2 459 ? 16.325 20.513 15.831 1.00 36.23 ? 1995 VAL B O 1 ATOM 5495 C CB . VAL B 2 459 ? 17.895 22.681 13.883 1.00 27.34 ? 1995 VAL B CB 1 ATOM 5496 C CG1 . VAL B 2 459 ? 19.175 23.506 13.684 1.00 21.16 ? 1995 VAL B CG1 1 ATOM 5497 C CG2 . VAL B 2 459 ? 17.999 21.326 13.204 1.00 24.85 ? 1995 VAL B CG2 1 ATOM 5498 N N . VAL B 2 460 ? 15.160 22.379 15.484 1.00 31.93 ? 1996 VAL B N 1 ATOM 5499 C CA . VAL B 2 460 ? 13.897 21.668 15.603 1.00 31.05 ? 1996 VAL B CA 1 ATOM 5500 C C . VAL B 2 460 ? 13.351 21.462 14.194 1.00 32.23 ? 1996 VAL B C 1 ATOM 5501 O O . VAL B 2 460 ? 13.322 22.382 13.360 1.00 29.67 ? 1996 VAL B O 1 ATOM 5502 C CB . VAL B 2 460 ? 12.882 22.437 16.515 1.00 31.44 ? 1996 VAL B CB 1 ATOM 5503 C CG1 . VAL B 2 460 ? 11.473 21.867 16.352 1.00 24.75 ? 1996 VAL B CG1 1 ATOM 5504 C CG2 . VAL B 2 460 ? 13.316 22.317 17.990 1.00 28.56 ? 1996 VAL B CG2 1 ATOM 5505 N N . ALA B 2 461 ? 12.943 20.233 13.916 1.00 32.84 ? 1997 ALA B N 1 ATOM 5506 C CA . ALA B 2 461 ? 12.451 19.929 12.602 1.00 32.78 ? 1997 ALA B CA 1 ATOM 5507 C C . ALA B 2 461 ? 11.652 18.669 12.611 1.00 37.21 ? 1997 ALA B C 1 ATOM 5508 O O . ALA B 2 461 ? 11.791 17.839 13.511 1.00 41.04 ? 1997 ALA B O 1 ATOM 5509 C CB . ALA B 2 461 ? 13.619 19.768 11.666 1.00 33.34 ? 1997 ALA B CB 1 ATOM 5510 N N . ARG B 2 462 ? 10.820 18.532 11.584 1.00 40.57 ? 1998 ARG B N 1 ATOM 5511 C CA . ARG B 2 462 ? 9.997 17.355 11.373 1.00 40.16 ? 1998 ARG B CA 1 ATOM 5512 C C . ARG B 2 462 ? 10.405 16.772 10.018 1.00 42.09 ? 1998 ARG B C 1 ATOM 5513 O O . ARG B 2 462 ? 10.222 15.589 9.769 1.00 43.18 ? 1998 ARG B O 1 ATOM 5514 C CB . ARG B 2 462 ? 8.522 17.728 11.335 1.00 42.74 ? 1998 ARG B CB 1 ATOM 5515 C CG . ARG B 2 462 ? 7.623 16.541 11.027 1.00 46.68 ? 1998 ARG B CG 1 ATOM 5516 C CD . ARG B 2 462 ? 6.248 16.963 10.566 1.00 48.20 ? 1998 ARG B CD 1 ATOM 5517 N NE . ARG B 2 462 ? 5.356 15.814 10.522 1.00 50.33 ? 1998 ARG B NE 1 ATOM 5518 C CZ . ARG B 2 462 ? 4.191 15.782 9.882 1.00 51.16 ? 1998 ARG B CZ 1 ATOM 5519 N NH1 . ARG B 2 462 ? 3.766 16.853 9.214 1.00 48.53 ? 1998 ARG B NH1 1 ATOM 5520 N NH2 . ARG B 2 462 ? 3.450 14.674 9.918 1.00 47.82 ? 1998 ARG B NH2 1 ATOM 5521 N N . TYR B 2 463 ? 10.949 17.620 9.144 1.00 42.76 ? 1999 TYR B N 1 ATOM 5522 C CA . TYR B 2 463 ? 11.397 17.208 7.812 1.00 41.78 ? 1999 TYR B CA 1 ATOM 5523 C C . TYR B 2 463 ? 12.862 17.588 7.628 1.00 42.42 ? 1999 TYR B C 1 ATOM 5524 O O . TYR B 2 463 ? 13.220 18.768 7.655 1.00 43.59 ? 1999 TYR B O 1 ATOM 5525 C CB . TYR B 2 463 ? 10.585 17.899 6.719 1.00 40.27 ? 1999 TYR B CB 1 ATOM 5526 C CG . TYR B 2 463 ? 9.106 17.638 6.778 1.00 45.36 ? 1999 TYR B CG 1 ATOM 5527 C CD1 . TYR B 2 463 ? 8.262 18.451 7.539 1.00 49.47 ? 1999 TYR B CD1 1 ATOM 5528 C CD2 . TYR B 2 463 ? 8.540 16.574 6.087 1.00 47.22 ? 1999 TYR B CD2 1 ATOM 5529 C CE1 . TYR B 2 463 ? 6.894 18.211 7.609 1.00 47.47 ? 1999 TYR B CE1 1 ATOM 5530 C CE2 . TYR B 2 463 ? 7.178 16.325 6.154 1.00 48.29 ? 1999 TYR B CE2 1 ATOM 5531 C CZ . TYR B 2 463 ? 6.364 17.146 6.919 1.00 47.15 ? 1999 TYR B CZ 1 ATOM 5532 O OH . TYR B 2 463 ? 5.025 16.881 7.011 1.00 48.08 ? 1999 TYR B OH 1 ATOM 5533 N N . ILE B 2 464 ? 13.708 16.583 7.446 1.00 41.22 ? 2000 ILE B N 1 ATOM 5534 C CA . ILE B 2 464 ? 15.135 16.807 7.254 1.00 38.44 ? 2000 ILE B CA 1 ATOM 5535 C C . ILE B 2 464 ? 15.322 16.536 5.775 1.00 39.35 ? 2000 ILE B C 1 ATOM 5536 O O . ILE B 2 464 ? 14.823 15.533 5.273 1.00 39.05 ? 2000 ILE B O 1 ATOM 5537 C CB . ILE B 2 464 ? 16.015 15.780 8.057 1.00 37.69 ? 2000 ILE B CB 1 ATOM 5538 C CG1 . ILE B 2 464 ? 15.470 15.558 9.483 1.00 32.28 ? 2000 ILE B CG1 1 ATOM 5539 C CG2 . ILE B 2 464 ? 17.452 16.249 8.097 1.00 37.34 ? 2000 ILE B CG2 1 ATOM 5540 C CD1 . ILE B 2 464 ? 15.310 16.761 10.282 1.00 26.83 ? 2000 ILE B CD1 1 ATOM 5541 N N . ARG B 2 465 ? 16.020 17.421 5.071 1.00 40.31 ? 2001 ARG B N 1 ATOM 5542 C CA . ARG B 2 465 ? 16.237 17.220 3.644 1.00 41.85 ? 2001 ARG B CA 1 ATOM 5543 C C . ARG B 2 465 ? 17.718 17.235 3.324 1.00 40.03 ? 2001 ARG B C 1 ATOM 5544 O O . ARG B 2 465 ? 18.381 18.246 3.468 1.00 40.16 ? 2001 ARG B O 1 ATOM 5545 C CB . ARG B 2 465 ? 15.518 18.295 2.833 1.00 44.32 ? 2001 ARG B CB 1 ATOM 5546 C CG . ARG B 2 465 ? 14.976 17.775 1.512 1.00 50.93 ? 2001 ARG B CG 1 ATOM 5547 C CD . ARG B 2 465 ? 14.060 18.783 0.860 1.00 52.00 ? 2001 ARG B CD 1 ATOM 5548 N NE . ARG B 2 465 ? 14.752 20.038 0.588 1.00 52.84 ? 2001 ARG B NE 1 ATOM 5549 C CZ . ARG B 2 465 ? 14.209 21.039 -0.095 1.00 54.95 ? 2001 ARG B CZ 1 ATOM 5550 N NH1 . ARG B 2 465 ? 12.971 20.914 -0.562 1.00 53.57 ? 2001 ARG B NH1 1 ATOM 5551 N NH2 . ARG B 2 465 ? 14.900 22.155 -0.318 1.00 53.56 ? 2001 ARG B NH2 1 ATOM 5552 N N . ILE B 2 466 ? 18.231 16.096 2.885 1.00 39.83 ? 2002 ILE B N 1 ATOM 5553 C CA . ILE B 2 466 ? 19.646 15.975 2.560 1.00 38.43 ? 2002 ILE B CA 1 ATOM 5554 C C . ILE B 2 466 ? 19.872 15.949 1.070 1.00 39.30 ? 2002 ILE B C 1 ATOM 5555 O O . ILE B 2 466 ? 19.136 15.293 0.331 1.00 38.82 ? 2002 ILE B O 1 ATOM 5556 C CB . ILE B 2 466 ? 20.235 14.699 3.167 1.00 36.06 ? 2002 ILE B CB 1 ATOM 5557 C CG1 . ILE B 2 466 ? 20.093 14.753 4.679 1.00 29.95 ? 2002 ILE B CG1 1 ATOM 5558 C CG2 . ILE B 2 466 ? 21.674 14.554 2.765 1.00 35.71 ? 2002 ILE B CG2 1 ATOM 5559 C CD1 . ILE B 2 466 ? 20.672 13.602 5.341 1.00 33.63 ? 2002 ILE B CD1 1 ATOM 5560 N N . SER B 2 467 ? 20.892 16.677 0.633 1.00 40.44 ? 2003 SER B N 1 ATOM 5561 C CA . SER B 2 467 ? 21.230 16.749 -0.787 1.00 41.74 ? 2003 SER B CA 1 ATOM 5562 C C . SER B 2 467 ? 22.752 16.765 -1.006 1.00 40.34 ? 2003 SER B C 1 ATOM 5563 O O . SER B 2 467 ? 23.454 17.646 -0.506 1.00 40.74 ? 2003 SER B O 1 ATOM 5564 C CB . SER B 2 467 ? 20.579 17.989 -1.404 1.00 40.54 ? 2003 SER B CB 1 ATOM 5565 O OG . SER B 2 467 ? 20.834 19.123 -0.615 1.00 43.83 ? 2003 SER B OG 1 ATOM 5566 N N . PRO B 2 468 ? 23.273 15.782 -1.755 1.00 37.82 ? 2004 PRO B N 1 ATOM 5567 C CA . PRO B 2 468 ? 24.699 15.642 -2.058 1.00 36.52 ? 2004 PRO B CA 1 ATOM 5568 C C . PRO B 2 468 ? 25.236 16.760 -2.929 1.00 34.93 ? 2004 PRO B C 1 ATOM 5569 O O . PRO B 2 468 ? 24.651 17.085 -3.938 1.00 37.19 ? 2004 PRO B O 1 ATOM 5570 C CB . PRO B 2 468 ? 24.773 14.296 -2.787 1.00 36.28 ? 2004 PRO B CB 1 ATOM 5571 C CG . PRO B 2 468 ? 23.566 13.579 -2.361 1.00 38.39 ? 2004 PRO B CG 1 ATOM 5572 C CD . PRO B 2 468 ? 22.521 14.664 -2.338 1.00 39.04 ? 2004 PRO B CD 1 ATOM 5573 N N . THR B 2 469 ? 26.370 17.328 -2.567 1.00 33.89 ? 2005 THR B N 1 ATOM 5574 C CA . THR B 2 469 ? 26.927 18.387 -3.383 1.00 34.82 ? 2005 THR B CA 1 ATOM 5575 C C . THR B 2 469 ? 28.308 17.998 -3.931 1.00 37.66 ? 2005 THR B C 1 ATOM 5576 O O . THR B 2 469 ? 28.966 18.783 -4.623 1.00 40.41 ? 2005 THR B O 1 ATOM 5577 C CB . THR B 2 469 ? 27.005 19.721 -2.585 1.00 34.41 ? 2005 THR B CB 1 ATOM 5578 O OG1 . THR B 2 469 ? 27.922 19.594 -1.493 1.00 36.80 ? 2005 THR B OG1 1 ATOM 5579 C CG2 . THR B 2 469 ? 25.629 20.086 -2.045 1.00 30.58 ? 2005 THR B CG2 1 ATOM 5580 N N . GLY B 2 470 ? 28.732 16.776 -3.626 1.00 37.16 ? 2006 GLY B N 1 ATOM 5581 C CA . GLY B 2 470 ? 30.009 16.278 -4.105 1.00 36.61 ? 2006 GLY B CA 1 ATOM 5582 C C . GLY B 2 470 ? 30.099 14.767 -3.981 1.00 37.24 ? 2006 GLY B C 1 ATOM 5583 O O . GLY B 2 470 ? 29.613 14.186 -3.004 1.00 36.35 ? 2006 GLY B O 1 ATOM 5584 N N . SER B 2 471 ? 30.723 14.104 -4.949 1.00 38.11 ? 2007 SER B N 1 ATOM 5585 C CA . SER B 2 471 ? 30.816 12.650 -4.848 1.00 38.69 ? 2007 SER B CA 1 ATOM 5586 C C . SER B 2 471 ? 31.935 12.000 -5.644 1.00 37.27 ? 2007 SER B C 1 ATOM 5587 O O . SER B 2 471 ? 32.636 12.661 -6.418 1.00 36.47 ? 2007 SER B O 1 ATOM 5588 C CB . SER B 2 471 ? 29.492 12.032 -5.288 1.00 40.56 ? 2007 SER B CB 1 ATOM 5589 O OG . SER B 2 471 ? 29.328 12.213 -6.682 1.00 42.66 ? 2007 SER B OG 1 ATOM 5590 N N . TYR B 2 472 ? 32.097 10.695 -5.417 1.00 36.56 ? 2008 TYR B N 1 ATOM 5591 C CA . TYR B 2 472 ? 33.067 9.850 -6.133 1.00 37.48 ? 2008 TYR B CA 1 ATOM 5592 C C . TYR B 2 472 ? 32.171 8.901 -6.941 1.00 34.77 ? 2008 TYR B C 1 ATOM 5593 O O . TYR B 2 472 ? 31.544 8.018 -6.379 1.00 32.55 ? 2008 TYR B O 1 ATOM 5594 C CB . TYR B 2 472 ? 33.937 9.051 -5.150 1.00 40.02 ? 2008 TYR B CB 1 ATOM 5595 C CG . TYR B 2 472 ? 34.969 8.142 -5.801 1.00 45.59 ? 2008 TYR B CG 1 ATOM 5596 C CD1 . TYR B 2 472 ? 36.155 8.649 -6.323 1.00 46.82 ? 2008 TYR B CD1 1 ATOM 5597 C CD2 . TYR B 2 472 ? 34.761 6.760 -5.870 1.00 48.64 ? 2008 TYR B CD2 1 ATOM 5598 C CE1 . TYR B 2 472 ? 37.112 7.801 -6.892 1.00 49.29 ? 2008 TYR B CE1 1 ATOM 5599 C CE2 . TYR B 2 472 ? 35.699 5.914 -6.429 1.00 49.27 ? 2008 TYR B CE2 1 ATOM 5600 C CZ . TYR B 2 472 ? 36.872 6.436 -6.936 1.00 52.33 ? 2008 TYR B CZ 1 ATOM 5601 O OH . TYR B 2 472 ? 37.808 5.577 -7.471 1.00 57.68 ? 2008 TYR B OH 1 ATOM 5602 N N . ASN B 2 473 ? 32.110 9.112 -8.254 1.00 36.97 ? 2009 ASN B N 1 ATOM 5603 C CA . ASN B 2 473 ? 31.264 8.330 -9.157 1.00 38.80 ? 2009 ASN B CA 1 ATOM 5604 C C . ASN B 2 473 ? 29.823 8.796 -9.045 1.00 41.25 ? 2009 ASN B C 1 ATOM 5605 O O . ASN B 2 473 ? 29.321 9.530 -9.905 1.00 42.98 ? 2009 ASN B O 1 ATOM 5606 C CB . ASN B 2 473 ? 31.363 6.839 -8.847 1.00 39.72 ? 2009 ASN B CB 1 ATOM 5607 C CG . ASN B 2 473 ? 32.652 6.234 -9.359 1.00 39.62 ? 2009 ASN B CG 1 ATOM 5608 O OD1 . ASN B 2 473 ? 33.149 5.267 -8.805 1.00 39.59 ? 2009 ASN B OD1 1 ATOM 5609 N ND2 . ASN B 2 473 ? 33.190 6.801 -10.434 1.00 34.80 ? 2009 ASN B ND2 1 ATOM 5610 N N . LYS B 2 474 ? 29.149 8.386 -7.985 1.00 40.13 ? 2010 LYS B N 1 ATOM 5611 C CA . LYS B 2 474 ? 27.777 8.815 -7.798 1.00 43.31 ? 2010 LYS B CA 1 ATOM 5612 C C . LYS B 2 474 ? 27.515 9.018 -6.322 1.00 44.99 ? 2010 LYS B C 1 ATOM 5613 O O . LYS B 2 474 ? 28.039 8.286 -5.485 1.00 47.23 ? 2010 LYS B O 1 ATOM 5614 C CB . LYS B 2 474 ? 26.809 7.782 -8.383 1.00 43.40 ? 2010 LYS B CB 1 ATOM 5615 C CG . LYS B 2 474 ? 26.526 7.960 -9.863 1.00 43.06 ? 2010 LYS B CG 1 ATOM 5616 C CD . LYS B 2 474 ? 25.990 6.682 -10.473 1.00 45.31 ? 2010 LYS B CD 1 ATOM 5617 C CE . LYS B 2 474 ? 25.412 6.918 -11.859 1.00 43.25 ? 2010 LYS B CE 1 ATOM 5618 N NZ . LYS B 2 474 ? 26.295 7.777 -12.682 1.00 48.81 ? 2010 LYS B NZ 1 ATOM 5619 N N . PRO B 2 475 ? 26.701 10.023 -5.978 1.00 45.63 ? 2011 PRO B N 1 ATOM 5620 C CA . PRO B 2 475 ? 26.376 10.316 -4.581 1.00 44.97 ? 2011 PRO B CA 1 ATOM 5621 C C . PRO B 2 475 ? 25.544 9.189 -3.986 1.00 44.04 ? 2011 PRO B C 1 ATOM 5622 O O . PRO B 2 475 ? 24.338 9.146 -4.182 1.00 46.32 ? 2011 PRO B O 1 ATOM 5623 C CB . PRO B 2 475 ? 25.556 11.597 -4.670 1.00 45.36 ? 2011 PRO B CB 1 ATOM 5624 C CG . PRO B 2 475 ? 25.862 12.143 -6.040 1.00 48.84 ? 2011 PRO B CG 1 ATOM 5625 C CD . PRO B 2 475 ? 25.970 10.922 -6.878 1.00 46.59 ? 2011 PRO B CD 1 ATOM 5626 N N . ALA B 2 476 ? 26.178 8.267 -3.288 1.00 39.55 ? 2012 ALA B N 1 ATOM 5627 C CA . ALA B 2 476 ? 25.427 7.198 -2.680 1.00 41.30 ? 2012 ALA B CA 1 ATOM 5628 C C . ALA B 2 476 ? 25.283 7.672 -1.270 1.00 43.28 ? 2012 ALA B C 1 ATOM 5629 O O . ALA B 2 476 ? 26.093 8.475 -0.816 1.00 47.77 ? 2012 ALA B O 1 ATOM 5630 C CB . ALA B 2 476 ? 26.214 5.891 -2.707 1.00 39.47 ? 2012 ALA B CB 1 ATOM 5631 N N . LEU B 2 477 ? 24.261 7.198 -0.569 1.00 40.24 ? 2013 LEU B N 1 ATOM 5632 C CA . LEU B 2 477 ? 24.094 7.581 0.816 1.00 35.32 ? 2013 LEU B CA 1 ATOM 5633 C C . LEU B 2 477 ? 23.309 6.567 1.581 1.00 35.09 ? 2013 LEU B C 1 ATOM 5634 O O . LEU B 2 477 ? 22.252 6.133 1.146 1.00 34.08 ? 2013 LEU B O 1 ATOM 5635 C CB . LEU B 2 477 ? 23.362 8.917 0.967 1.00 37.76 ? 2013 LEU B CB 1 ATOM 5636 C CG . LEU B 2 477 ? 24.040 10.282 0.815 1.00 36.98 ? 2013 LEU B CG 1 ATOM 5637 C CD1 . LEU B 2 477 ? 22.981 11.366 0.975 1.00 35.01 ? 2013 LEU B CD1 1 ATOM 5638 C CD2 . LEU B 2 477 ? 25.149 10.447 1.839 1.00 33.99 ? 2013 LEU B CD2 1 ATOM 5639 N N . ARG B 2 478 ? 23.870 6.174 2.714 1.00 34.93 ? 2014 ARG B N 1 ATOM 5640 C CA . ARG B 2 478 ? 23.215 5.294 3.663 1.00 35.89 ? 2014 ARG B CA 1 ATOM 5641 C C . ARG B 2 478 ? 23.424 6.242 4.829 1.00 36.32 ? 2014 ARG B C 1 ATOM 5642 O O . ARG B 2 478 ? 24.554 6.656 5.091 1.00 34.64 ? 2014 ARG B O 1 ATOM 5643 C CB . ARG B 2 478 ? 23.959 3.967 3.865 1.00 35.34 ? 2014 ARG B CB 1 ATOM 5644 C CG . ARG B 2 478 ? 23.493 2.878 2.898 1.00 37.43 ? 2014 ARG B CG 1 ATOM 5645 C CD . ARG B 2 478 ? 24.235 1.551 3.093 1.00 35.88 ? 2014 ARG B CD 1 ATOM 5646 N NE . ARG B 2 478 ? 25.668 1.714 2.898 1.00 32.18 ? 2014 ARG B NE 1 ATOM 5647 C CZ . ARG B 2 478 ? 26.601 1.059 3.577 1.00 30.05 ? 2014 ARG B CZ 1 ATOM 5648 N NH1 . ARG B 2 478 ? 26.259 0.170 4.504 1.00 24.12 ? 2014 ARG B NH1 1 ATOM 5649 N NH2 . ARG B 2 478 ? 27.882 1.348 3.362 1.00 31.21 ? 2014 ARG B NH2 1 ATOM 5650 N N . LEU B 2 479 ? 22.342 6.630 5.496 1.00 36.17 ? 2015 LEU B N 1 ATOM 5651 C CA . LEU B 2 479 ? 22.477 7.586 6.569 1.00 36.70 ? 2015 LEU B CA 1 ATOM 5652 C C . LEU B 2 479 ? 21.659 7.336 7.819 1.00 35.63 ? 2015 LEU B C 1 ATOM 5653 O O . LEU B 2 479 ? 20.765 6.511 7.839 1.00 38.91 ? 2015 LEU B O 1 ATOM 5654 C CB . LEU B 2 479 ? 22.171 8.988 6.013 1.00 36.65 ? 2015 LEU B CB 1 ATOM 5655 C CG . LEU B 2 479 ? 20.752 9.263 5.511 1.00 37.84 ? 2015 LEU B CG 1 ATOM 5656 C CD1 . LEU B 2 479 ? 19.916 9.653 6.691 1.00 38.69 ? 2015 LEU B CD1 1 ATOM 5657 C CD2 . LEU B 2 479 ? 20.720 10.393 4.493 1.00 32.89 ? 2015 LEU B CD2 1 ATOM 5658 N N . GLU B 2 480 ? 22.017 8.043 8.879 1.00 33.28 ? 2016 GLU B N 1 ATOM 5659 C CA . GLU B 2 480 ? 21.295 7.986 10.132 1.00 33.45 ? 2016 GLU B CA 1 ATOM 5660 C C . GLU B 2 480 ? 21.255 9.402 10.698 1.00 33.71 ? 2016 GLU B C 1 ATOM 5661 O O . GLU B 2 480 ? 22.250 10.132 10.619 1.00 36.89 ? 2016 GLU B O 1 ATOM 5662 C CB . GLU B 2 480 ? 21.981 7.066 11.133 1.00 33.26 ? 2016 GLU B CB 1 ATOM 5663 C CG . GLU B 2 480 ? 21.235 6.985 12.456 1.00 31.95 ? 2016 GLU B CG 1 ATOM 5664 C CD . GLU B 2 480 ? 19.766 6.609 12.278 1.00 35.44 ? 2016 GLU B CD 1 ATOM 5665 O OE1 . GLU B 2 480 ? 19.359 5.533 12.776 1.00 36.59 ? 2016 GLU B OE1 1 ATOM 5666 O OE2 . GLU B 2 480 ? 19.012 7.383 11.634 1.00 37.69 ? 2016 GLU B OE2 1 ATOM 5667 N N . LEU B 2 481 ? 20.110 9.811 11.236 1.00 32.16 ? 2017 LEU B N 1 ATOM 5668 C CA . LEU B 2 481 ? 19.998 11.138 11.847 1.00 30.06 ? 2017 LEU B CA 1 ATOM 5669 C C . LEU B 2 481 ? 20.091 10.916 13.358 1.00 31.34 ? 2017 LEU B C 1 ATOM 5670 O O . LEU B 2 481 ? 19.766 9.844 13.857 1.00 29.33 ? 2017 LEU B O 1 ATOM 5671 C CB . LEU B 2 481 ? 18.660 11.796 11.496 1.00 27.65 ? 2017 LEU B CB 1 ATOM 5672 C CG . LEU B 2 481 ? 18.277 11.969 10.017 1.00 27.04 ? 2017 LEU B CG 1 ATOM 5673 C CD1 . LEU B 2 481 ? 16.800 12.274 9.926 1.00 25.43 ? 2017 LEU B CD1 1 ATOM 5674 C CD2 . LEU B 2 481 ? 19.085 13.080 9.349 1.00 28.08 ? 2017 LEU B CD2 1 ATOM 5675 N N . GLN B 2 482 ? 20.557 11.916 14.089 1.00 33.48 ? 2018 GLN B N 1 ATOM 5676 C CA . GLN B 2 482 ? 20.673 11.782 15.530 1.00 35.37 ? 2018 GLN B CA 1 ATOM 5677 C C . GLN B 2 482 ? 19.990 12.939 16.247 1.00 35.60 ? 2018 GLN B C 1 ATOM 5678 O O . GLN B 2 482 ? 19.992 14.068 15.758 1.00 35.79 ? 2018 GLN B O 1 ATOM 5679 C CB . GLN B 2 482 ? 22.143 11.714 15.929 1.00 37.44 ? 2018 GLN B CB 1 ATOM 5680 C CG . GLN B 2 482 ? 22.922 10.591 15.261 1.00 40.05 ? 2018 GLN B CG 1 ATOM 5681 C CD . GLN B 2 482 ? 24.411 10.806 15.378 1.00 43.07 ? 2018 GLN B CD 1 ATOM 5682 O OE1 . GLN B 2 482 ? 24.969 11.717 14.756 1.00 46.89 ? 2018 GLN B OE1 1 ATOM 5683 N NE2 . GLN B 2 482 ? 25.068 9.985 16.186 1.00 44.68 ? 2018 GLN B NE2 1 ATOM 5684 N N . GLY B 2 483 ? 19.401 12.641 17.405 1.00 36.54 ? 2019 GLY B N 1 ATOM 5685 C CA . GLY B 2 483 ? 18.716 13.656 18.185 1.00 37.82 ? 2019 GLY B CA 1 ATOM 5686 C C . GLY B 2 483 ? 17.962 13.139 19.397 1.00 37.44 ? 2019 GLY B C 1 ATOM 5687 O O . GLY B 2 483 ? 18.453 12.290 20.132 1.00 37.20 ? 2019 GLY B O 1 ATOM 5688 N N . CYS B 2 484 ? 16.767 13.678 19.611 1.00 38.39 ? 2020 CYS B N 1 ATOM 5689 C CA . CYS B 2 484 ? 15.910 13.299 20.737 1.00 39.03 ? 2020 CYS B CA 1 ATOM 5690 C C . CYS B 2 484 ? 14.591 14.053 20.644 1.00 37.89 ? 2020 CYS B C 1 ATOM 5691 O O . CYS B 2 484 ? 14.295 14.693 19.646 1.00 36.38 ? 2020 CYS B O 1 ATOM 5692 C CB . CYS B 2 484 ? 16.573 13.632 22.082 1.00 38.94 ? 2020 CYS B CB 1 ATOM 5693 S SG . CYS B 2 484 ? 16.934 15.403 22.332 1.00 39.31 ? 2020 CYS B SG 1 ATOM 5694 N N . GLU B 2 485 ? 13.804 13.967 21.702 1.00 39.26 ? 2021 GLU B N 1 ATOM 5695 C CA . GLU B 2 485 ? 12.516 14.634 21.755 1.00 38.79 ? 2021 GLU B CA 1 ATOM 5696 C C . GLU B 2 485 ? 12.773 16.056 22.211 1.00 37.27 ? 2021 GLU B C 1 ATOM 5697 O O . GLU B 2 485 ? 13.603 16.295 23.091 1.00 37.48 ? 2021 GLU B O 1 ATOM 5698 C CB . GLU B 2 485 ? 11.602 13.885 22.726 1.00 41.15 ? 2021 GLU B CB 1 ATOM 5699 C CG . GLU B 2 485 ? 11.292 12.461 22.269 1.00 44.21 ? 2021 GLU B CG 1 ATOM 5700 C CD . GLU B 2 485 ? 10.177 12.399 21.222 1.00 50.03 ? 2021 GLU B CD 1 ATOM 5701 O OE1 . GLU B 2 485 ? 10.131 11.424 20.437 1.00 49.21 ? 2021 GLU B OE1 1 ATOM 5702 O OE2 . GLU B 2 485 ? 9.330 13.322 21.192 1.00 52.70 ? 2021 GLU B OE2 1 ATOM 5703 N N . VAL B 2 486 ? 12.067 16.999 21.603 1.00 36.88 ? 2022 VAL B N 1 ATOM 5704 C CA . VAL B 2 486 ? 12.246 18.411 21.920 1.00 37.19 ? 2022 VAL B CA 1 ATOM 5705 C C . VAL B 2 486 ? 11.970 18.739 23.380 1.00 41.01 ? 2022 VAL B C 1 ATOM 5706 O O . VAL B 2 486 ? 12.637 19.596 23.962 1.00 41.14 ? 2022 VAL B O 1 ATOM 5707 C CB . VAL B 2 486 ? 11.336 19.309 21.068 1.00 32.25 ? 2022 VAL B CB 1 ATOM 5708 C CG1 . VAL B 2 486 ? 11.555 20.734 21.445 1.00 34.57 ? 2022 VAL B CG1 1 ATOM 5709 C CG2 . VAL B 2 486 ? 11.637 19.134 19.604 1.00 33.22 ? 2022 VAL B CG2 1 ATOM 5710 N N . ASN B 2 487 ? 10.991 18.058 23.974 1.00 41.80 ? 2023 ASN B N 1 ATOM 5711 C CA . ASN B 2 487 ? 10.643 18.334 25.350 1.00 41.89 ? 2023 ASN B CA 1 ATOM 5712 C C . ASN B 2 487 ? 11.541 17.698 26.379 1.00 44.41 ? 2023 ASN B C 1 ATOM 5713 O O . ASN B 2 487 ? 11.285 17.788 27.575 1.00 45.60 ? 2023 ASN B O 1 ATOM 5714 C CB . ASN B 2 487 ? 9.195 17.972 25.589 1.00 39.61 ? 2023 ASN B CB 1 ATOM 5715 C CG . ASN B 2 487 ? 8.263 18.975 24.973 1.00 40.74 ? 2023 ASN B CG 1 ATOM 5716 O OD1 . ASN B 2 487 ? 7.053 18.776 24.920 1.00 42.70 ? 2023 ASN B OD1 1 ATOM 5717 N ND2 . ASN B 2 487 ? 8.829 20.079 24.495 1.00 40.97 ? 2023 ASN B ND2 1 ATOM 5718 N N . GLY B 2 488 ? 12.619 17.081 25.920 1.00 46.45 ? 2024 GLY B N 1 ATOM 5719 C CA . GLY B 2 488 ? 13.548 16.485 26.856 1.00 48.99 ? 2024 GLY B CA 1 ATOM 5720 C C . GLY B 2 488 ? 13.007 15.339 27.677 1.00 50.80 ? 2024 GLY B C 1 ATOM 5721 O O . GLY B 2 488 ? 11.864 14.916 27.518 1.00 50.28 ? 2024 GLY B O 1 ATOM 5722 N N . CYS B 2 489 ? 13.849 14.863 28.586 1.00 54.68 ? 2025 CYS B N 1 ATOM 5723 C CA . CYS B 2 489 ? 13.531 13.729 29.433 1.00 57.30 ? 2025 CYS B CA 1 ATOM 5724 C C . CYS B 2 489 ? 13.120 12.625 28.465 1.00 57.91 ? 2025 CYS B C 1 ATOM 5725 O O . CYS B 2 489 ? 11.983 12.154 28.469 1.00 58.67 ? 2025 CYS B O 1 ATOM 5726 C CB . CYS B 2 489 ? 12.407 14.068 30.410 1.00 60.46 ? 2025 CYS B CB 1 ATOM 5727 S SG . CYS B 2 489 ? 12.283 12.904 31.818 1.00 69.03 ? 2025 CYS B SG 1 ATOM 5728 N N . SER B 2 490 ? 14.072 12.233 27.620 1.00 56.90 ? 2026 SER B N 1 ATOM 5729 C CA . SER B 2 490 ? 13.839 11.210 26.618 1.00 55.69 ? 2026 SER B CA 1 ATOM 5730 C C . SER B 2 490 ? 15.101 10.447 26.211 1.00 54.31 ? 2026 SER B C 1 ATOM 5731 O O . SER B 2 490 ? 15.168 9.908 25.116 1.00 52.07 ? 2026 SER B O 1 ATOM 5732 C CB . SER B 2 490 ? 13.216 11.850 25.382 1.00 55.93 ? 2026 SER B CB 1 ATOM 5733 O OG . SER B 2 490 ? 14.089 12.822 24.831 1.00 55.73 ? 2026 SER B OG 1 ATOM 5734 N N . THR B 2 491 ? 16.088 10.399 27.099 1.00 54.66 ? 2027 THR B N 1 ATOM 5735 C CA . THR B 2 491 ? 17.348 9.704 26.844 1.00 54.88 ? 2027 THR B CA 1 ATOM 5736 C C . THR B 2 491 ? 17.387 8.329 27.546 1.00 56.20 ? 2027 THR B C 1 ATOM 5737 O O . THR B 2 491 ? 16.636 8.073 28.498 1.00 54.26 ? 2027 THR B O 1 ATOM 5738 C CB . THR B 2 491 ? 18.544 10.559 27.335 1.00 55.46 ? 2027 THR B CB 1 ATOM 5739 O OG1 . THR B 2 491 ? 18.210 11.158 28.592 1.00 57.80 ? 2027 THR B OG1 1 ATOM 5740 C CG2 . THR B 2 491 ? 18.858 11.669 26.354 1.00 56.85 ? 2027 THR B CG2 1 ATOM 5741 N N . PRO B 2 492 ? 18.268 7.424 27.078 1.00 55.94 ? 2028 PRO B N 1 ATOM 5742 C CA . PRO B 2 492 ? 18.409 6.080 27.649 1.00 54.23 ? 2028 PRO B CA 1 ATOM 5743 C C . PRO B 2 492 ? 18.683 6.110 29.149 1.00 54.64 ? 2028 PRO B C 1 ATOM 5744 O O . PRO B 2 492 ? 19.329 7.029 29.652 1.00 53.62 ? 2028 PRO B O 1 ATOM 5745 C CB . PRO B 2 492 ? 19.591 5.501 26.877 1.00 53.81 ? 2028 PRO B CB 1 ATOM 5746 C CG . PRO B 2 492 ? 19.513 6.179 25.565 1.00 52.37 ? 2028 PRO B CG 1 ATOM 5747 C CD . PRO B 2 492 ? 19.197 7.605 25.949 1.00 54.47 ? 2028 PRO B CD 1 ATOM 5748 N N . LEU B 2 493 ? 18.210 5.087 29.855 1.00 55.60 ? 2029 LEU B N 1 ATOM 5749 C CA . LEU B 2 493 ? 18.414 5.004 31.295 1.00 54.16 ? 2029 LEU B CA 1 ATOM 5750 C C . LEU B 2 493 ? 19.554 4.094 31.758 1.00 54.06 ? 2029 LEU B C 1 ATOM 5751 O O . LEU B 2 493 ? 19.934 4.154 32.920 1.00 57.31 ? 2029 LEU B O 1 ATOM 5752 C CB . LEU B 2 493 ? 17.111 4.597 31.984 1.00 53.57 ? 2029 LEU B CB 1 ATOM 5753 C CG . LEU B 2 493 ? 16.082 5.726 32.057 1.00 52.51 ? 2029 LEU B CG 1 ATOM 5754 C CD1 . LEU B 2 493 ? 14.722 5.192 32.464 1.00 50.68 ? 2029 LEU B CD1 1 ATOM 5755 C CD2 . LEU B 2 493 ? 16.580 6.773 33.037 1.00 52.02 ? 2029 LEU B CD2 1 ATOM 5756 N N . GLY B 2 494 ? 20.098 3.255 30.879 1.00 52.94 ? 2030 GLY B N 1 ATOM 5757 C CA . GLY B 2 494 ? 21.205 2.401 31.294 1.00 52.95 ? 2030 GLY B CA 1 ATOM 5758 C C . GLY B 2 494 ? 21.312 0.984 30.731 1.00 52.50 ? 2030 GLY B C 1 ATOM 5759 O O . GLY B 2 494 ? 22.324 0.302 30.917 1.00 49.73 ? 2030 GLY B O 1 ATOM 5760 N N . MET B 2 495 ? 20.276 0.531 30.038 1.00 52.14 ? 2031 MET B N 1 ATOM 5761 C CA . MET B 2 495 ? 20.291 -0.803 29.466 1.00 51.37 ? 2031 MET B CA 1 ATOM 5762 C C . MET B 2 495 ? 21.429 -0.987 28.482 1.00 50.64 ? 2031 MET B C 1 ATOM 5763 O O . MET B 2 495 ? 22.225 -1.911 28.613 1.00 50.74 ? 2031 MET B O 1 ATOM 5764 C CB . MET B 2 495 ? 18.957 -1.107 28.766 1.00 52.36 ? 2031 MET B CB 1 ATOM 5765 C CG . MET B 2 495 ? 17.762 -1.172 29.710 1.00 53.85 ? 2031 MET B CG 1 ATOM 5766 S SD . MET B 2 495 ? 18.054 -2.345 31.071 1.00 54.63 ? 2031 MET B SD 1 ATOM 5767 C CE . MET B 2 495 ? 17.464 -3.894 30.287 1.00 53.77 ? 2031 MET B CE 1 ATOM 5768 N N . GLU B 2 496 ? 21.526 -0.107 27.496 1.00 51.27 ? 2032 GLU B N 1 ATOM 5769 C CA . GLU B 2 496 ? 22.574 -0.261 26.504 1.00 50.81 ? 2032 GLU B CA 1 ATOM 5770 C C . GLU B 2 496 ? 23.976 0.198 26.885 1.00 51.17 ? 2032 GLU B C 1 ATOM 5771 O O . GLU B 2 496 ? 24.944 -0.381 26.408 1.00 52.09 ? 2032 GLU B O 1 ATOM 5772 C CB . GLU B 2 496 ? 22.159 0.392 25.195 1.00 49.31 ? 2032 GLU B CB 1 ATOM 5773 C CG . GLU B 2 496 ? 23.264 0.371 24.175 1.00 52.36 ? 2032 GLU B CG 1 ATOM 5774 C CD . GLU B 2 496 ? 22.783 0.639 22.775 1.00 53.79 ? 2032 GLU B CD 1 ATOM 5775 O OE1 . GLU B 2 496 ? 23.600 0.479 21.839 1.00 54.24 ? 2032 GLU B OE1 1 ATOM 5776 O OE2 . GLU B 2 496 ? 21.595 1.002 22.614 1.00 55.95 ? 2032 GLU B OE2 1 ATOM 5777 N N . SER B 2 497 ? 24.109 1.214 27.734 1.00 52.16 ? 2033 SER B N 1 ATOM 5778 C CA . SER B 2 497 ? 25.448 1.679 28.122 1.00 53.17 ? 2033 SER B CA 1 ATOM 5779 C C . SER B 2 497 ? 26.049 0.773 29.168 1.00 56.33 ? 2033 SER B C 1 ATOM 5780 O O . SER B 2 497 ? 27.129 0.218 28.984 1.00 58.71 ? 2033 SER B O 1 ATOM 5781 C CB . SER B 2 497 ? 25.409 3.099 28.696 1.00 52.43 ? 2033 SER B CB 1 ATOM 5782 O OG . SER B 2 497 ? 24.744 3.150 29.944 1.00 44.14 ? 2033 SER B OG 1 ATOM 5783 N N . GLY B 2 498 ? 25.329 0.632 30.273 1.00 58.55 ? 2034 GLY B N 1 ATOM 5784 C CA . GLY B 2 498 ? 25.789 -0.190 31.371 1.00 60.33 ? 2034 GLY B CA 1 ATOM 5785 C C . GLY B 2 498 ? 25.554 0.542 32.678 1.00 61.26 ? 2034 GLY B C 1 ATOM 5786 O O . GLY B 2 498 ? 25.690 -0.036 33.758 1.00 61.16 ? 2034 GLY B O 1 ATOM 5787 N N . LYS B 2 499 ? 25.205 1.821 32.583 1.00 62.43 ? 2035 LYS B N 1 ATOM 5788 C CA . LYS B 2 499 ? 24.946 2.612 33.774 1.00 65.10 ? 2035 LYS B CA 1 ATOM 5789 C C . LYS B 2 499 ? 24.033 1.747 34.637 1.00 66.07 ? 2035 LYS B C 1 ATOM 5790 O O . LYS B 2 499 ? 24.147 1.735 35.864 1.00 67.56 ? 2035 LYS B O 1 ATOM 5791 C CB . LYS B 2 499 ? 24.289 3.949 33.394 1.00 66.72 ? 2035 LYS B CB 1 ATOM 5792 C CG . LYS B 2 499 ? 25.236 4.909 32.632 1.00 68.96 ? 2035 LYS B CG 1 ATOM 5793 C CD . LYS B 2 499 ? 24.503 6.104 31.994 1.00 68.94 ? 2035 LYS B CD 1 ATOM 5794 C CE . LYS B 2 499 ? 23.676 5.685 30.775 1.00 69.67 ? 2035 LYS B CE 1 ATOM 5795 N NZ . LYS B 2 499 ? 22.497 6.581 30.548 1.00 71.00 ? 2035 LYS B NZ 1 ATOM 5796 N N . ILE B 2 500 ? 23.135 1.013 33.985 1.00 65.02 ? 2036 ILE B N 1 ATOM 5797 C CA . ILE B 2 500 ? 22.252 0.093 34.694 1.00 64.91 ? 2036 ILE B CA 1 ATOM 5798 C C . ILE B 2 500 ? 23.051 -1.201 34.766 1.00 65.85 ? 2036 ILE B C 1 ATOM 5799 O O . ILE B 2 500 ? 23.253 -1.868 33.746 1.00 65.72 ? 2036 ILE B O 1 ATOM 5800 C CB . ILE B 2 500 ? 20.942 -0.208 33.918 1.00 64.34 ? 2036 ILE B CB 1 ATOM 5801 C CG1 . ILE B 2 500 ? 20.003 1.002 33.948 1.00 61.68 ? 2036 ILE B CG1 1 ATOM 5802 C CG2 . ILE B 2 500 ? 20.260 -1.431 34.518 1.00 62.83 ? 2036 ILE B CG2 1 ATOM 5803 C CD1 . ILE B 2 500 ? 18.734 0.795 33.151 1.00 57.37 ? 2036 ILE B CD1 1 ATOM 5804 N N . GLU B 2 501 ? 23.512 -1.551 35.960 1.00 66.25 ? 2037 GLU B N 1 ATOM 5805 C CA . GLU B 2 501 ? 24.299 -2.763 36.134 1.00 67.53 ? 2037 GLU B CA 1 ATOM 5806 C C . GLU B 2 501 ? 23.475 -4.049 36.168 1.00 67.47 ? 2037 GLU B C 1 ATOM 5807 O O . GLU B 2 501 ? 22.299 -4.038 36.524 1.00 66.60 ? 2037 GLU B O 1 ATOM 5808 C CB . GLU B 2 501 ? 25.148 -2.638 37.395 1.00 69.18 ? 2037 GLU B CB 1 ATOM 5809 C CG . GLU B 2 501 ? 26.205 -1.561 37.274 1.00 69.56 ? 2037 GLU B CG 1 ATOM 5810 C CD . GLU B 2 501 ? 27.160 -1.561 38.435 1.00 69.56 ? 2037 GLU B CD 1 ATOM 5811 O OE1 . GLU B 2 501 ? 28.233 -0.922 38.330 1.00 70.49 ? 2037 GLU B OE1 1 ATOM 5812 O OE2 . GLU B 2 501 ? 26.831 -2.201 39.452 1.00 69.70 ? 2037 GLU B OE2 1 ATOM 5813 N N . ASN B 2 502 ? 24.113 -5.151 35.788 1.00 68.58 ? 2038 ASN B N 1 ATOM 5814 C CA . ASN B 2 502 ? 23.476 -6.468 35.742 1.00 71.36 ? 2038 ASN B CA 1 ATOM 5815 C C . ASN B 2 502 ? 22.649 -6.809 36.975 1.00 72.28 ? 2038 ASN B C 1 ATOM 5816 O O . ASN B 2 502 ? 21.495 -7.223 36.861 1.00 73.04 ? 2038 ASN B O 1 ATOM 5817 C CB . ASN B 2 502 ? 24.535 -7.545 35.531 1.00 71.08 ? 2038 ASN B CB 1 ATOM 5818 C CG . ASN B 2 502 ? 25.494 -7.195 34.416 1.00 73.82 ? 2038 ASN B CG 1 ATOM 5819 O OD1 . ASN B 2 502 ? 26.209 -6.187 34.495 1.00 74.93 ? 2038 ASN B OD1 1 ATOM 5820 N ND2 . ASN B 2 502 ? 25.513 -8.014 33.364 1.00 72.70 ? 2038 ASN B ND2 1 ATOM 5821 N N . LYS B 2 503 ? 23.242 -6.637 38.151 1.00 73.36 ? 2039 LYS B N 1 ATOM 5822 C CA . LYS B 2 503 ? 22.559 -6.926 39.407 1.00 73.62 ? 2039 LYS B CA 1 ATOM 5823 C C . LYS B 2 503 ? 21.348 -6.021 39.624 1.00 73.84 ? 2039 LYS B C 1 ATOM 5824 O O . LYS B 2 503 ? 21.055 -5.628 40.754 1.00 74.09 ? 2039 LYS B O 1 ATOM 5825 C CB . LYS B 2 503 ? 23.534 -6.775 40.576 1.00 74.14 ? 2039 LYS B CB 1 ATOM 5826 C CG . LYS B 2 503 ? 24.190 -5.402 40.661 1.00 75.33 ? 2039 LYS B CG 1 ATOM 5827 C CD . LYS B 2 503 ? 25.721 -5.472 40.514 1.00 75.89 ? 2039 LYS B CD 1 ATOM 5828 C CE . LYS B 2 503 ? 26.183 -5.855 39.096 1.00 73.33 ? 2039 LYS B CE 1 ATOM 5829 N NZ . LYS B 2 503 ? 25.977 -7.295 38.745 1.00 71.28 ? 2039 LYS B NZ 1 ATOM 5830 N N . GLN B 2 504 ? 20.648 -5.704 38.536 1.00 73.86 ? 2040 GLN B N 1 ATOM 5831 C CA . GLN B 2 504 ? 19.463 -4.849 38.567 1.00 73.67 ? 2040 GLN B CA 1 ATOM 5832 C C . GLN B 2 504 ? 18.357 -5.443 37.713 1.00 74.35 ? 2040 GLN B C 1 ATOM 5833 O O . GLN B 2 504 ? 17.180 -5.134 37.895 1.00 75.04 ? 2040 GLN B O 1 ATOM 5834 C CB . GLN B 2 504 ? 19.801 -3.456 38.044 1.00 72.16 ? 2040 GLN B CB 1 ATOM 5835 C CG . GLN B 2 504 ? 20.082 -2.427 39.115 1.00 71.61 ? 2040 GLN B CG 1 ATOM 5836 C CD . GLN B 2 504 ? 20.840 -1.235 38.567 1.00 73.29 ? 2040 GLN B CD 1 ATOM 5837 O OE1 . GLN B 2 504 ? 22.053 -1.298 38.357 1.00 72.78 ? 2040 GLN B OE1 1 ATOM 5838 N NE2 . GLN B 2 504 ? 20.125 -0.143 38.316 1.00 73.19 ? 2040 GLN B NE2 1 ATOM 5839 N N . ILE B 2 505 ? 18.745 -6.293 36.772 1.00 74.78 ? 2041 ILE B N 1 ATOM 5840 C CA . ILE B 2 505 ? 17.786 -6.929 35.887 1.00 75.51 ? 2041 ILE B CA 1 ATOM 5841 C C . ILE B 2 505 ? 17.567 -8.342 36.393 1.00 76.25 ? 2041 ILE B C 1 ATOM 5842 O O . ILE B 2 505 ? 18.507 -9.132 36.488 1.00 76.29 ? 2041 ILE B O 1 ATOM 5843 C CB . ILE B 2 505 ? 18.313 -6.975 34.437 1.00 76.42 ? 2041 ILE B CB 1 ATOM 5844 C CG1 . ILE B 2 505 ? 18.646 -5.562 33.968 1.00 77.43 ? 2041 ILE B CG1 1 ATOM 5845 C CG2 . ILE B 2 505 ? 17.267 -7.576 33.511 1.00 75.61 ? 2041 ILE B CG2 1 ATOM 5846 C CD1 . ILE B 2 505 ? 19.319 -5.518 32.622 1.00 79.72 ? 2041 ILE B CD1 1 ATOM 5847 N N . THR B 2 506 ? 16.323 -8.659 36.722 1.00 76.12 ? 2042 THR B N 1 ATOM 5848 C CA . THR B 2 506 ? 15.997 -9.978 37.230 1.00 75.48 ? 2042 THR B CA 1 ATOM 5849 C C . THR B 2 506 ? 14.671 -10.420 36.654 1.00 76.15 ? 2042 THR B C 1 ATOM 5850 O O . THR B 2 506 ? 13.689 -9.688 36.727 1.00 77.53 ? 2042 THR B O 1 ATOM 5851 C CB . THR B 2 506 ? 15.881 -9.951 38.748 1.00 75.02 ? 2042 THR B CB 1 ATOM 5852 O OG1 . THR B 2 506 ? 14.898 -8.976 39.122 1.00 75.37 ? 2042 THR B OG1 1 ATOM 5853 C CG2 . THR B 2 506 ? 17.221 -9.598 39.379 1.00 71.95 ? 2042 THR B CG2 1 ATOM 5854 N N . ALA B 2 507 ? 14.643 -11.620 36.081 1.00 76.50 ? 2043 ALA B N 1 ATOM 5855 C CA . ALA B 2 507 ? 13.423 -12.147 35.483 1.00 75.63 ? 2043 ALA B CA 1 ATOM 5856 C C . ALA B 2 507 ? 12.914 -13.404 36.174 1.00 75.74 ? 2043 ALA B C 1 ATOM 5857 O O . ALA B 2 507 ? 13.658 -14.118 36.853 1.00 74.05 ? 2043 ALA B O 1 ATOM 5858 C CB . ALA B 2 507 ? 13.651 -12.432 34.007 1.00 75.29 ? 2043 ALA B CB 1 ATOM 5859 N N . SER B 2 508 ? 11.628 -13.665 35.985 1.00 76.24 ? 2044 SER B N 1 ATOM 5860 C CA . SER B 2 508 ? 10.993 -14.833 36.557 1.00 76.75 ? 2044 SER B CA 1 ATOM 5861 C C . SER B 2 508 ? 11.801 -16.088 36.224 1.00 78.12 ? 2044 SER B C 1 ATOM 5862 O O . SER B 2 508 ? 12.322 -16.759 37.115 1.00 79.01 ? 2044 SER B O 1 ATOM 5863 C CB . SER B 2 508 ? 9.568 -14.947 36.017 1.00 76.20 ? 2044 SER B CB 1 ATOM 5864 O OG . SER B 2 508 ? 9.524 -14.730 34.616 1.00 77.03 ? 2044 SER B OG 1 ATOM 5865 N N . SER B 2 509 ? 11.921 -16.395 34.937 1.00 79.11 ? 2045 SER B N 1 ATOM 5866 C CA . SER B 2 509 ? 12.672 -17.571 34.512 1.00 79.93 ? 2045 SER B CA 1 ATOM 5867 C C . SER B 2 509 ? 13.660 -17.218 33.412 1.00 79.98 ? 2045 SER B C 1 ATOM 5868 O O . SER B 2 509 ? 13.583 -16.144 32.824 1.00 79.46 ? 2045 SER B O 1 ATOM 5869 C CB . SER B 2 509 ? 11.716 -18.658 33.997 1.00 80.78 ? 2045 SER B CB 1 ATOM 5870 O OG . SER B 2 509 ? 11.052 -18.261 32.802 1.00 80.35 ? 2045 SER B OG 1 ATOM 5871 N N . PHE B 2 510 ? 14.594 -18.129 33.151 1.00 80.45 ? 2046 PHE B N 1 ATOM 5872 C CA . PHE B 2 510 ? 15.582 -17.951 32.093 1.00 81.33 ? 2046 PHE B CA 1 ATOM 5873 C C . PHE B 2 510 ? 16.130 -19.308 31.645 1.00 81.83 ? 2046 PHE B C 1 ATOM 5874 O O . PHE B 2 510 ? 15.981 -20.309 32.350 1.00 81.73 ? 2046 PHE B O 1 ATOM 5875 C CB . PHE B 2 510 ? 16.725 -17.023 32.540 1.00 80.71 ? 2046 PHE B CB 1 ATOM 5876 C CG . PHE B 2 510 ? 17.600 -17.590 33.615 1.00 79.99 ? 2046 PHE B CG 1 ATOM 5877 C CD1 . PHE B 2 510 ? 17.204 -17.552 34.947 1.00 81.77 ? 2046 PHE B CD1 1 ATOM 5878 C CD2 . PHE B 2 510 ? 18.826 -18.158 33.296 1.00 79.89 ? 2046 PHE B CD2 1 ATOM 5879 C CE1 . PHE B 2 510 ? 18.023 -18.076 35.952 1.00 82.95 ? 2046 PHE B CE1 1 ATOM 5880 C CE2 . PHE B 2 510 ? 19.650 -18.683 34.289 1.00 81.77 ? 2046 PHE B CE2 1 ATOM 5881 C CZ . PHE B 2 510 ? 19.248 -18.643 35.621 1.00 82.24 ? 2046 PHE B CZ 1 ATOM 5882 N N . LYS B 2 511 ? 16.743 -19.346 30.466 1.00 82.10 ? 2047 LYS B N 1 ATOM 5883 C CA . LYS B 2 511 ? 17.290 -20.589 29.944 1.00 82.57 ? 2047 LYS B CA 1 ATOM 5884 C C . LYS B 2 511 ? 18.760 -20.807 30.264 1.00 85.31 ? 2047 LYS B C 1 ATOM 5885 O O . LYS B 2 511 ? 19.474 -19.880 30.659 1.00 84.18 ? 2047 LYS B O 1 ATOM 5886 C CB . LYS B 2 511 ? 17.101 -20.663 28.434 1.00 80.82 ? 2047 LYS B CB 1 ATOM 5887 C CG . LYS B 2 511 ? 15.675 -20.902 27.994 1.00 80.23 ? 2047 LYS B CG 1 ATOM 5888 C CD . LYS B 2 511 ? 15.657 -21.412 26.568 1.00 79.32 ? 2047 LYS B CD 1 ATOM 5889 C CE . LYS B 2 511 ? 14.261 -21.766 26.119 1.00 78.36 ? 2047 LYS B CE 1 ATOM 5890 N NZ . LYS B 2 511 ? 14.285 -22.362 24.749 1.00 80.03 ? 2047 LYS B NZ 1 ATOM 5891 N N . LYS B 2 512 ? 19.189 -22.055 30.084 1.00 89.40 ? 2048 LYS B N 1 ATOM 5892 C CA . LYS B 2 512 ? 20.564 -22.492 30.328 1.00 93.47 ? 2048 LYS B CA 1 ATOM 5893 C C . LYS B 2 512 ? 20.794 -23.888 29.730 1.00 95.67 ? 2048 LYS B C 1 ATOM 5894 O O . LYS B 2 512 ? 21.096 -24.837 30.461 1.00 95.74 ? 2048 LYS B O 1 ATOM 5895 C CB . LYS B 2 512 ? 20.859 -22.550 31.836 1.00 94.51 ? 2048 LYS B CB 1 ATOM 5896 C CG . LYS B 2 512 ? 21.327 -21.245 32.482 1.00 96.04 ? 2048 LYS B CG 1 ATOM 5897 C CD . LYS B 2 512 ? 21.526 -21.420 33.994 1.00 95.48 ? 2048 LYS B CD 1 ATOM 5898 C CE . LYS B 2 512 ? 22.529 -22.525 34.317 1.00 96.18 ? 2048 LYS B CE 1 ATOM 5899 N NZ . LYS B 2 512 ? 22.477 -22.942 35.749 1.00 94.58 ? 2048 LYS B NZ 1 ATOM 5900 N N . SER B 2 513 ? 20.651 -24.016 28.411 1.00 97.70 ? 2049 SER B N 1 ATOM 5901 C CA . SER B 2 513 ? 20.854 -25.308 27.754 1.00 100.08 ? 2049 SER B CA 1 ATOM 5902 C C . SER B 2 513 ? 22.295 -25.776 27.974 1.00 102.31 ? 2049 SER B C 1 ATOM 5903 O O . SER B 2 513 ? 23.242 -25.007 27.774 1.00 103.03 ? 2049 SER B O 1 ATOM 5904 C CB . SER B 2 513 ? 20.556 -25.200 26.258 1.00 98.68 ? 2049 SER B CB 1 ATOM 5905 O OG . SER B 2 513 ? 21.511 -24.393 25.594 1.00 98.49 ? 2049 SER B OG 1 ATOM 5906 N N . TRP B 2 514 ? 22.450 -27.039 28.379 1.00 103.95 ? 2050 TRP B N 1 ATOM 5907 C CA . TRP B 2 514 ? 23.763 -27.631 28.665 1.00 104.60 ? 2050 TRP B CA 1 ATOM 5908 C C . TRP B 2 514 ? 24.776 -27.613 27.526 1.00 103.40 ? 2050 TRP B C 1 ATOM 5909 O O . TRP B 2 514 ? 25.795 -28.303 27.589 1.00 102.44 ? 2050 TRP B O 1 ATOM 5910 C CB . TRP B 2 514 ? 23.603 -29.070 29.190 1.00 107.06 ? 2050 TRP B CB 1 ATOM 5911 C CG . TRP B 2 514 ? 22.885 -30.010 28.263 1.00 109.75 ? 2050 TRP B CG 1 ATOM 5912 C CD1 . TRP B 2 514 ? 23.431 -31.039 27.542 1.00 109.52 ? 2050 TRP B CD1 1 ATOM 5913 C CD2 . TRP B 2 514 ? 21.487 -30.001 27.953 1.00 111.68 ? 2050 TRP B CD2 1 ATOM 5914 N NE1 . TRP B 2 514 ? 22.459 -31.668 26.803 1.00 110.39 ? 2050 TRP B NE1 1 ATOM 5915 C CE2 . TRP B 2 514 ? 21.256 -31.052 27.036 1.00 111.98 ? 2050 TRP B CE2 1 ATOM 5916 C CE3 . TRP B 2 514 ? 20.404 -29.202 28.360 1.00 112.51 ? 2050 TRP B CE3 1 ATOM 5917 C CZ2 . TRP B 2 514 ? 19.983 -31.328 26.517 1.00 113.21 ? 2050 TRP B CZ2 1 ATOM 5918 C CZ3 . TRP B 2 514 ? 19.136 -29.475 27.842 1.00 113.36 ? 2050 TRP B CZ3 1 ATOM 5919 C CH2 . TRP B 2 514 ? 18.939 -30.531 26.929 1.00 113.89 ? 2050 TRP B CH2 1 ATOM 5920 N N . TRP B 2 515 ? 24.498 -26.824 26.494 1.00 102.80 ? 2051 TRP B N 1 ATOM 5921 C CA . TRP B 2 515 ? 25.404 -26.708 25.362 1.00 102.76 ? 2051 TRP B CA 1 ATOM 5922 C C . TRP B 2 515 ? 26.139 -25.386 25.513 1.00 102.53 ? 2051 TRP B C 1 ATOM 5923 O O . TRP B 2 515 ? 26.516 -24.750 24.527 1.00 103.12 ? 2051 TRP B O 1 ATOM 5924 C CB . TRP B 2 515 ? 24.626 -26.751 24.042 1.00 101.89 ? 2051 TRP B CB 1 ATOM 5925 C CG . TRP B 2 515 ? 23.776 -27.972 23.931 1.00 101.62 ? 2051 TRP B CG 1 ATOM 5926 C CD1 . TRP B 2 515 ? 24.199 -29.272 23.937 1.00 102.07 ? 2051 TRP B CD1 1 ATOM 5927 C CD2 . TRP B 2 515 ? 22.347 -28.016 23.895 1.00 102.03 ? 2051 TRP B CD2 1 ATOM 5928 N NE1 . TRP B 2 515 ? 23.120 -30.123 23.917 1.00 101.71 ? 2051 TRP B NE1 1 ATOM 5929 C CE2 . TRP B 2 515 ? 21.971 -29.378 23.891 1.00 101.75 ? 2051 TRP B CE2 1 ATOM 5930 C CE3 . TRP B 2 515 ? 21.345 -27.036 23.869 1.00 102.24 ? 2051 TRP B CE3 1 ATOM 5931 C CZ2 . TRP B 2 515 ? 20.635 -29.785 23.864 1.00 101.20 ? 2051 TRP B CZ2 1 ATOM 5932 C CZ3 . TRP B 2 515 ? 20.014 -27.443 23.843 1.00 101.89 ? 2051 TRP B CZ3 1 ATOM 5933 C CH2 . TRP B 2 515 ? 19.674 -28.807 23.841 1.00 100.99 ? 2051 TRP B CH2 1 ATOM 5934 N N . GLY B 2 516 ? 26.331 -24.984 26.767 1.00 101.77 ? 2052 GLY B N 1 ATOM 5935 C CA . GLY B 2 516 ? 27.022 -23.745 27.064 1.00 101.85 ? 2052 GLY B CA 1 ATOM 5936 C C . GLY B 2 516 ? 26.233 -22.494 26.710 1.00 101.69 ? 2052 GLY B C 1 ATOM 5937 O O . GLY B 2 516 ? 26.816 -21.416 26.544 1.00 101.75 ? 2052 GLY B O 1 ATOM 5938 N N . ASN B 2 517 ? 24.912 -22.627 26.598 1.00 100.12 ? 2053 ASN B N 1 ATOM 5939 C CA . ASN B 2 517 ? 24.058 -21.492 26.262 1.00 97.51 ? 2053 ASN B CA 1 ATOM 5940 C C . ASN B 2 517 ? 23.157 -21.076 27.417 1.00 95.81 ? 2053 ASN B C 1 ATOM 5941 O O . ASN B 2 517 ? 22.165 -21.745 27.714 1.00 94.72 ? 2053 ASN B O 1 ATOM 5942 C CB . ASN B 2 517 ? 23.206 -21.817 25.035 1.00 98.63 ? 2053 ASN B CB 1 ATOM 5943 C CG . ASN B 2 517 ? 24.040 -22.014 23.785 1.00 99.54 ? 2053 ASN B CG 1 ATOM 5944 O OD1 . ASN B 2 517 ? 24.916 -21.203 23.476 1.00 98.98 ? 2053 ASN B OD1 1 ATOM 5945 N ND2 . ASN B 2 517 ? 23.768 -23.091 23.052 1.00 99.87 ? 2053 ASN B ND2 1 ATOM 5946 N N . TYR B 2 518 ? 23.515 -19.961 28.056 1.00 93.53 ? 2054 TYR B N 1 ATOM 5947 C CA . TYR B 2 518 ? 22.770 -19.417 29.191 1.00 91.07 ? 2054 TYR B CA 1 ATOM 5948 C C . TYR B 2 518 ? 22.269 -18.016 28.858 1.00 88.60 ? 2054 TYR B C 1 ATOM 5949 O O . TYR B 2 518 ? 23.058 -17.114 28.575 1.00 89.75 ? 2054 TYR B O 1 ATOM 5950 C CB . TYR B 2 518 ? 23.665 -19.346 30.427 1.00 91.86 ? 2054 TYR B CB 1 ATOM 5951 C CG . TYR B 2 518 ? 24.642 -20.488 30.517 1.00 94.63 ? 2054 TYR B CG 1 ATOM 5952 C CD1 . TYR B 2 518 ? 25.709 -20.583 29.622 1.00 95.63 ? 2054 TYR B CD1 1 ATOM 5953 C CD2 . TYR B 2 518 ? 24.492 -21.492 31.476 1.00 95.28 ? 2054 TYR B CD2 1 ATOM 5954 C CE1 . TYR B 2 518 ? 26.600 -21.646 29.677 1.00 96.97 ? 2054 TYR B CE1 1 ATOM 5955 C CE2 . TYR B 2 518 ? 25.381 -22.562 31.540 1.00 95.85 ? 2054 TYR B CE2 1 ATOM 5956 C CZ . TYR B 2 518 ? 26.432 -22.632 30.634 1.00 96.75 ? 2054 TYR B CZ 1 ATOM 5957 O OH . TYR B 2 518 ? 27.311 -23.687 30.670 1.00 98.86 ? 2054 TYR B OH 1 ATOM 5958 N N . TRP B 2 519 ? 20.956 -17.830 28.905 1.00 84.04 ? 2055 TRP B N 1 ATOM 5959 C CA . TRP B 2 519 ? 20.385 -16.535 28.590 1.00 78.93 ? 2055 TRP B CA 1 ATOM 5960 C C . TRP B 2 519 ? 19.897 -15.794 29.831 1.00 77.34 ? 2055 TRP B C 1 ATOM 5961 O O . TRP B 2 519 ? 18.696 -15.616 30.015 1.00 76.32 ? 2055 TRP B O 1 ATOM 5962 C CB . TRP B 2 519 ? 19.225 -16.699 27.604 1.00 75.91 ? 2055 TRP B CB 1 ATOM 5963 C CG . TRP B 2 519 ? 19.480 -17.698 26.496 1.00 72.91 ? 2055 TRP B CG 1 ATOM 5964 C CD1 . TRP B 2 519 ? 19.472 -19.062 26.601 1.00 71.98 ? 2055 TRP B CD1 1 ATOM 5965 C CD2 . TRP B 2 519 ? 19.754 -17.407 25.121 1.00 70.51 ? 2055 TRP B CD2 1 ATOM 5966 N NE1 . TRP B 2 519 ? 19.721 -19.637 25.379 1.00 68.36 ? 2055 TRP B NE1 1 ATOM 5967 C CE2 . TRP B 2 519 ? 19.899 -18.647 24.451 1.00 69.51 ? 2055 TRP B CE2 1 ATOM 5968 C CE3 . TRP B 2 519 ? 19.893 -16.222 24.389 1.00 67.72 ? 2055 TRP B CE3 1 ATOM 5969 C CZ2 . TRP B 2 519 ? 20.176 -18.736 23.083 1.00 69.56 ? 2055 TRP B CZ2 1 ATOM 5970 C CZ3 . TRP B 2 519 ? 20.171 -16.309 23.025 1.00 69.31 ? 2055 TRP B CZ3 1 ATOM 5971 C CH2 . TRP B 2 519 ? 20.308 -17.559 22.387 1.00 69.10 ? 2055 TRP B CH2 1 ATOM 5972 N N . GLU B 2 520 ? 20.827 -15.361 30.677 1.00 76.42 ? 2056 GLU B N 1 ATOM 5973 C CA . GLU B 2 520 ? 20.472 -14.618 31.886 1.00 78.49 ? 2056 GLU B CA 1 ATOM 5974 C C . GLU B 2 520 ? 19.675 -13.347 31.530 1.00 79.38 ? 2056 GLU B C 1 ATOM 5975 O O . GLU B 2 520 ? 19.876 -12.757 30.466 1.00 80.12 ? 2056 GLU B O 1 ATOM 5976 C CB . GLU B 2 520 ? 21.745 -14.238 32.657 1.00 79.89 ? 2056 GLU B CB 1 ATOM 5977 C CG . GLU B 2 520 ? 22.397 -15.376 33.437 1.00 81.03 ? 2056 GLU B CG 1 ATOM 5978 C CD . GLU B 2 520 ? 21.725 -15.620 34.780 1.00 82.25 ? 2056 GLU B CD 1 ATOM 5979 O OE1 . GLU B 2 520 ? 20.549 -16.038 34.798 1.00 82.86 ? 2056 GLU B OE1 1 ATOM 5980 O OE2 . GLU B 2 520 ? 22.372 -15.384 35.823 1.00 81.82 ? 2056 GLU B OE2 1 ATOM 5981 N N . PRO B 2 521 ? 18.763 -12.913 32.421 1.00 78.87 ? 2057 PRO B N 1 ATOM 5982 C CA . PRO B 2 521 ? 17.905 -11.730 32.266 1.00 77.70 ? 2057 PRO B CA 1 ATOM 5983 C C . PRO B 2 521 ? 18.617 -10.404 32.034 1.00 76.39 ? 2057 PRO B C 1 ATOM 5984 O O . PRO B 2 521 ? 18.149 -9.578 31.256 1.00 75.30 ? 2057 PRO B O 1 ATOM 5985 C CB . PRO B 2 521 ? 17.109 -11.715 33.565 1.00 79.12 ? 2057 PRO B CB 1 ATOM 5986 C CG . PRO B 2 521 ? 16.969 -13.156 33.872 1.00 79.71 ? 2057 PRO B CG 1 ATOM 5987 C CD . PRO B 2 521 ? 18.375 -13.660 33.627 1.00 79.76 ? 2057 PRO B CD 1 ATOM 5988 N N . PHE B 2 522 ? 19.739 -10.199 32.716 1.00 75.59 ? 2058 PHE B N 1 ATOM 5989 C CA . PHE B 2 522 ? 20.497 -8.959 32.579 1.00 75.44 ? 2058 PHE B CA 1 ATOM 5990 C C . PHE B 2 522 ? 21.197 -8.824 31.221 1.00 75.25 ? 2058 PHE B C 1 ATOM 5991 O O . PHE B 2 522 ? 22.113 -8.018 31.066 1.00 76.12 ? 2058 PHE B O 1 ATOM 5992 C CB . PHE B 2 522 ? 21.532 -8.842 33.710 1.00 74.68 ? 2058 PHE B CB 1 ATOM 5993 C CG . PHE B 2 522 ? 22.516 -9.983 33.762 1.00 75.99 ? 2058 PHE B CG 1 ATOM 5994 C CD1 . PHE B 2 522 ? 23.319 -10.291 32.658 1.00 75.24 ? 2058 PHE B CD1 1 ATOM 5995 C CD2 . PHE B 2 522 ? 22.645 -10.753 34.918 1.00 75.87 ? 2058 PHE B CD2 1 ATOM 5996 C CE1 . PHE B 2 522 ? 24.231 -11.347 32.707 1.00 74.80 ? 2058 PHE B CE1 1 ATOM 5997 C CE2 . PHE B 2 522 ? 23.556 -11.813 34.974 1.00 74.88 ? 2058 PHE B CE2 1 ATOM 5998 C CZ . PHE B 2 522 ? 24.348 -12.109 33.870 1.00 74.96 ? 2058 PHE B CZ 1 ATOM 5999 N N . LEU B 2 523 ? 20.771 -9.617 30.243 1.00 74.57 ? 2059 LEU B N 1 ATOM 6000 C CA . LEU B 2 523 ? 21.364 -9.572 28.908 1.00 72.36 ? 2059 LEU B CA 1 ATOM 6001 C C . LEU B 2 523 ? 20.396 -8.910 27.944 1.00 70.45 ? 2059 LEU B C 1 ATOM 6002 O O . LEU B 2 523 ? 20.717 -8.701 26.776 1.00 69.79 ? 2059 LEU B O 1 ATOM 6003 C CB . LEU B 2 523 ? 21.678 -10.984 28.414 1.00 74.28 ? 2059 LEU B CB 1 ATOM 6004 C CG . LEU B 2 523 ? 22.602 -11.821 29.302 1.00 74.76 ? 2059 LEU B CG 1 ATOM 6005 C CD1 . LEU B 2 523 ? 22.533 -13.271 28.863 1.00 74.73 ? 2059 LEU B CD1 1 ATOM 6006 C CD2 . LEU B 2 523 ? 24.019 -11.293 29.224 1.00 73.28 ? 2059 LEU B CD2 1 ATOM 6007 N N . ALA B 2 524 ? 19.202 -8.599 28.440 1.00 67.85 ? 2060 ALA B N 1 ATOM 6008 C CA . ALA B 2 524 ? 18.182 -7.947 27.630 1.00 64.72 ? 2060 ALA B CA 1 ATOM 6009 C C . ALA B 2 524 ? 18.587 -6.489 27.432 1.00 62.54 ? 2060 ALA B C 1 ATOM 6010 O O . ALA B 2 524 ? 17.839 -5.573 27.766 1.00 63.54 ? 2060 ALA B O 1 ATOM 6011 C CB . ALA B 2 524 ? 16.827 -8.038 28.326 1.00 62.30 ? 2060 ALA B CB 1 ATOM 6012 N N . ARG B 2 525 ? 19.790 -6.290 26.906 1.00 60.50 ? 2061 ARG B N 1 ATOM 6013 C CA . ARG B 2 525 ? 20.320 -4.960 26.647 1.00 58.98 ? 2061 ARG B CA 1 ATOM 6014 C C . ARG B 2 525 ? 20.265 -4.635 25.157 1.00 59.15 ? 2061 ARG B C 1 ATOM 6015 O O . ARG B 2 525 ? 21.044 -5.167 24.365 1.00 57.32 ? 2061 ARG B O 1 ATOM 6016 C CB . ARG B 2 525 ? 21.769 -4.857 27.109 1.00 58.39 ? 2061 ARG B CB 1 ATOM 6017 C CG . ARG B 2 525 ? 21.991 -5.012 28.592 1.00 60.85 ? 2061 ARG B CG 1 ATOM 6018 C CD . ARG B 2 525 ? 23.464 -4.813 28.916 1.00 61.86 ? 2061 ARG B CD 1 ATOM 6019 N NE . ARG B 2 525 ? 23.790 -5.188 30.290 1.00 63.92 ? 2061 ARG B NE 1 ATOM 6020 C CZ . ARG B 2 525 ? 23.518 -4.452 31.361 1.00 64.09 ? 2061 ARG B CZ 1 ATOM 6021 N NH1 . ARG B 2 525 ? 22.913 -3.285 31.231 1.00 64.31 ? 2061 ARG B NH1 1 ATOM 6022 N NH2 . ARG B 2 525 ? 23.854 -4.888 32.568 1.00 65.20 ? 2061 ARG B NH2 1 ATOM 6023 N N . LEU B 2 526 ? 19.339 -3.749 24.796 1.00 58.88 ? 2062 LEU B N 1 ATOM 6024 C CA . LEU B 2 526 ? 19.134 -3.287 23.423 1.00 55.23 ? 2062 LEU B CA 1 ATOM 6025 C C . LEU B 2 526 ? 20.466 -3.186 22.676 1.00 55.29 ? 2062 LEU B C 1 ATOM 6026 O O . LEU B 2 526 ? 21.391 -2.517 23.134 1.00 53.08 ? 2062 LEU B O 1 ATOM 6027 C CB . LEU B 2 526 ? 18.427 -1.935 23.490 1.00 51.10 ? 2062 LEU B CB 1 ATOM 6028 C CG . LEU B 2 526 ? 17.900 -1.207 22.262 1.00 49.10 ? 2062 LEU B CG 1 ATOM 6029 C CD1 . LEU B 2 526 ? 19.047 -0.554 21.535 1.00 47.00 ? 2062 LEU B CD1 1 ATOM 6030 C CD2 . LEU B 2 526 ? 17.129 -2.170 21.391 1.00 47.72 ? 2062 LEU B CD2 1 ATOM 6031 N N . ASN B 2 527 ? 20.556 -3.870 21.536 1.00 57.15 ? 2063 ASN B N 1 ATOM 6032 C CA . ASN B 2 527 ? 21.773 -3.900 20.704 1.00 61.06 ? 2063 ASN B CA 1 ATOM 6033 C C . ASN B 2 527 ? 22.895 -4.787 21.251 1.00 62.70 ? 2063 ASN B C 1 ATOM 6034 O O . ASN B 2 527 ? 24.049 -4.370 21.299 1.00 63.30 ? 2063 ASN B O 1 ATOM 6035 C CB . ASN B 2 527 ? 22.345 -2.489 20.497 1.00 60.87 ? 2063 ASN B CB 1 ATOM 6036 C CG . ASN B 2 527 ? 21.575 -1.690 19.477 1.00 60.49 ? 2063 ASN B CG 1 ATOM 6037 O OD1 . ASN B 2 527 ? 21.057 -2.239 18.505 1.00 59.92 ? 2063 ASN B OD1 1 ATOM 6038 N ND2 . ASN B 2 527 ? 21.509 -0.382 19.681 1.00 59.68 ? 2063 ASN B ND2 1 ATOM 6039 N N . ALA B 2 528 ? 22.565 -6.011 21.645 1.00 65.55 ? 2064 ALA B N 1 ATOM 6040 C CA . ALA B 2 528 ? 23.559 -6.925 22.198 1.00 68.27 ? 2064 ALA B CA 1 ATOM 6041 C C . ALA B 2 528 ? 24.143 -7.819 21.119 1.00 70.08 ? 2064 ALA B C 1 ATOM 6042 O O . ALA B 2 528 ? 23.456 -8.166 20.162 1.00 71.49 ? 2064 ALA B O 1 ATOM 6043 C CB . ALA B 2 528 ? 22.926 -7.775 23.287 1.00 68.23 ? 2064 ALA B CB 1 ATOM 6044 N N . GLN B 2 529 ? 25.408 -8.200 21.267 1.00 71.99 ? 2065 GLN B N 1 ATOM 6045 C CA . GLN B 2 529 ? 26.034 -9.068 20.275 1.00 75.41 ? 2065 GLN B CA 1 ATOM 6046 C C . GLN B 2 529 ? 26.944 -10.148 20.866 1.00 76.50 ? 2065 GLN B C 1 ATOM 6047 O O . GLN B 2 529 ? 27.371 -10.069 22.028 1.00 75.25 ? 2065 GLN B O 1 ATOM 6048 C CB . GLN B 2 529 ? 26.815 -8.228 19.254 1.00 77.26 ? 2065 GLN B CB 1 ATOM 6049 C CG . GLN B 2 529 ? 25.953 -7.210 18.515 1.00 80.36 ? 2065 GLN B CG 1 ATOM 6050 C CD . GLN B 2 529 ? 24.772 -7.845 17.787 1.00 82.59 ? 2065 GLN B CD 1 ATOM 6051 O OE1 . GLN B 2 529 ? 23.754 -7.191 17.545 1.00 83.13 ? 2065 GLN B OE1 1 ATOM 6052 N NE2 . GLN B 2 529 ? 24.906 -9.120 17.429 1.00 83.74 ? 2065 GLN B NE2 1 ATOM 6053 N N . GLY B 2 530 ? 27.217 -11.171 20.056 1.00 77.74 ? 2066 GLY B N 1 ATOM 6054 C CA . GLY B 2 530 ? 28.083 -12.253 20.490 1.00 78.92 ? 2066 GLY B CA 1 ATOM 6055 C C . GLY B 2 530 ? 27.418 -13.589 20.768 1.00 78.70 ? 2066 GLY B C 1 ATOM 6056 O O . GLY B 2 530 ? 26.523 -14.025 20.030 1.00 76.42 ? 2066 GLY B O 1 ATOM 6057 N N . ARG B 2 531 ? 27.881 -14.230 21.842 1.00 79.30 ? 2067 ARG B N 1 ATOM 6058 C CA . ARG B 2 531 ? 27.389 -15.536 22.283 1.00 81.26 ? 2067 ARG B CA 1 ATOM 6059 C C . ARG B 2 531 ? 25.884 -15.515 22.580 1.00 79.94 ? 2067 ARG B C 1 ATOM 6060 O O . ARG B 2 531 ? 25.055 -15.661 21.677 1.00 80.18 ? 2067 ARG B O 1 ATOM 6061 C CB . ARG B 2 531 ? 28.154 -15.972 23.537 1.00 83.59 ? 2067 ARG B CB 1 ATOM 6062 C CG . ARG B 2 531 ? 28.306 -17.478 23.675 1.00 88.84 ? 2067 ARG B CG 1 ATOM 6063 C CD . ARG B 2 531 ? 29.261 -18.041 22.619 1.00 91.03 ? 2067 ARG B CD 1 ATOM 6064 N NE . ARG B 2 531 ? 28.750 -19.261 21.994 1.00 93.12 ? 2067 ARG B NE 1 ATOM 6065 C CZ . ARG B 2 531 ? 27.692 -19.300 21.187 1.00 93.61 ? 2067 ARG B CZ 1 ATOM 6066 N NH1 . ARG B 2 531 ? 27.029 -18.185 20.906 1.00 93.96 ? 2067 ARG B NH1 1 ATOM 6067 N NH2 . ARG B 2 531 ? 27.299 -20.452 20.655 1.00 93.13 ? 2067 ARG B NH2 1 ATOM 6068 N N . VAL B 2 532 ? 25.533 -15.366 23.851 1.00 77.49 ? 2068 VAL B N 1 ATOM 6069 C CA . VAL B 2 532 ? 24.132 -15.293 24.231 1.00 75.80 ? 2068 VAL B CA 1 ATOM 6070 C C . VAL B 2 532 ? 23.863 -13.811 24.403 1.00 75.08 ? 2068 VAL B C 1 ATOM 6071 O O . VAL B 2 532 ? 24.279 -13.195 25.385 1.00 74.47 ? 2068 VAL B O 1 ATOM 6072 C CB . VAL B 2 532 ? 23.850 -16.065 25.540 1.00 76.34 ? 2068 VAL B CB 1 ATOM 6073 C CG1 . VAL B 2 532 ? 23.917 -17.555 25.261 1.00 74.61 ? 2068 VAL B CG1 1 ATOM 6074 C CG2 . VAL B 2 532 ? 24.862 -15.680 26.629 1.00 75.66 ? 2068 VAL B CG2 1 ATOM 6075 N N . ASN B 2 533 ? 23.169 -13.246 23.422 1.00 74.51 ? 2069 ASN B N 1 ATOM 6076 C CA . ASN B 2 533 ? 22.873 -11.820 23.384 1.00 73.45 ? 2069 ASN B CA 1 ATOM 6077 C C . ASN B 2 533 ? 21.456 -11.410 23.741 1.00 73.85 ? 2069 ASN B C 1 ATOM 6078 O O . ASN B 2 533 ? 20.885 -10.562 23.063 1.00 76.05 ? 2069 ASN B O 1 ATOM 6079 C CB . ASN B 2 533 ? 23.172 -11.307 21.986 1.00 70.56 ? 2069 ASN B CB 1 ATOM 6080 C CG . ASN B 2 533 ? 22.350 -12.020 20.932 1.00 70.41 ? 2069 ASN B CG 1 ATOM 6081 O OD1 . ASN B 2 533 ? 22.366 -13.246 20.854 1.00 71.87 ? 2069 ASN B OD1 1 ATOM 6082 N ND2 . ASN B 2 533 ? 21.624 -11.259 20.115 1.00 68.32 ? 2069 ASN B ND2 1 ATOM 6083 N N . ALA B 2 534 ? 20.877 -11.977 24.790 1.00 73.56 ? 2070 ALA B N 1 ATOM 6084 C CA . ALA B 2 534 ? 19.517 -11.587 25.147 1.00 73.22 ? 2070 ALA B CA 1 ATOM 6085 C C . ALA B 2 534 ? 18.968 -12.337 26.347 1.00 72.65 ? 2070 ALA B C 1 ATOM 6086 O O . ALA B 2 534 ? 19.709 -12.996 27.068 1.00 72.02 ? 2070 ALA B O 1 ATOM 6087 C CB . ALA B 2 534 ? 18.591 -11.787 23.949 1.00 73.65 ? 2070 ALA B CB 1 ATOM 6088 N N . TRP B 2 535 ? 17.660 -12.203 26.552 1.00 72.65 ? 2071 TRP B N 1 ATOM 6089 C CA . TRP B 2 535 ? 16.954 -12.866 27.638 1.00 72.99 ? 2071 TRP B CA 1 ATOM 6090 C C . TRP B 2 535 ? 16.045 -13.931 27.051 1.00 74.08 ? 2071 TRP B C 1 ATOM 6091 O O . TRP B 2 535 ? 15.233 -13.650 26.172 1.00 73.88 ? 2071 TRP B O 1 ATOM 6092 C CB . TRP B 2 535 ? 16.104 -11.868 28.425 1.00 73.42 ? 2071 TRP B CB 1 ATOM 6093 C CG . TRP B 2 535 ? 15.100 -12.519 29.345 1.00 76.55 ? 2071 TRP B CG 1 ATOM 6094 C CD1 . TRP B 2 535 ? 15.363 -13.391 30.367 1.00 78.10 ? 2071 TRP B CD1 1 ATOM 6095 C CD2 . TRP B 2 535 ? 13.671 -12.374 29.303 1.00 77.81 ? 2071 TRP B CD2 1 ATOM 6096 N NE1 . TRP B 2 535 ? 14.190 -13.798 30.958 1.00 77.40 ? 2071 TRP B NE1 1 ATOM 6097 C CE2 . TRP B 2 535 ? 13.137 -13.191 30.326 1.00 76.60 ? 2071 TRP B CE2 1 ATOM 6098 C CE3 . TRP B 2 535 ? 12.790 -11.634 28.501 1.00 78.91 ? 2071 TRP B CE3 1 ATOM 6099 C CZ2 . TRP B 2 535 ? 11.764 -13.290 30.568 1.00 76.68 ? 2071 TRP B CZ2 1 ATOM 6100 C CZ3 . TRP B 2 535 ? 11.417 -11.734 28.743 1.00 78.65 ? 2071 TRP B CZ3 1 ATOM 6101 C CH2 . TRP B 2 535 ? 10.922 -12.558 29.769 1.00 77.93 ? 2071 TRP B CH2 1 ATOM 6102 N N . GLN B 2 536 ? 16.186 -15.157 27.533 1.00 74.36 ? 2072 GLN B N 1 ATOM 6103 C CA . GLN B 2 536 ? 15.356 -16.247 27.055 1.00 75.19 ? 2072 GLN B CA 1 ATOM 6104 C C . GLN B 2 536 ? 14.425 -16.685 28.172 1.00 76.64 ? 2072 GLN B C 1 ATOM 6105 O O . GLN B 2 536 ? 14.869 -16.931 29.288 1.00 76.23 ? 2072 GLN B O 1 ATOM 6106 C CB . GLN B 2 536 ? 16.233 -17.418 26.621 1.00 75.27 ? 2072 GLN B CB 1 ATOM 6107 C CG . GLN B 2 536 ? 16.524 -17.452 25.145 1.00 73.46 ? 2072 GLN B CG 1 ATOM 6108 C CD . GLN B 2 536 ? 15.320 -17.885 24.374 1.00 74.60 ? 2072 GLN B CD 1 ATOM 6109 O OE1 . GLN B 2 536 ? 14.218 -17.394 24.618 1.00 76.37 ? 2072 GLN B OE1 1 ATOM 6110 N NE2 . GLN B 2 536 ? 15.508 -18.811 23.438 1.00 73.78 ? 2072 GLN B NE2 1 ATOM 6111 N N . ALA B 2 537 ? 13.133 -16.767 27.876 1.00 78.88 ? 2073 ALA B N 1 ATOM 6112 C CA . ALA B 2 537 ? 12.160 -17.196 28.874 1.00 80.46 ? 2073 ALA B CA 1 ATOM 6113 C C . ALA B 2 537 ? 12.204 -18.713 28.949 1.00 82.19 ? 2073 ALA B C 1 ATOM 6114 O O . ALA B 2 537 ? 11.882 -19.395 27.970 1.00 82.21 ? 2073 ALA B O 1 ATOM 6115 C CB . ALA B 2 537 ? 10.765 -16.738 28.484 1.00 80.43 ? 2073 ALA B CB 1 ATOM 6116 N N . LYS B 2 538 ? 12.608 -19.237 30.106 1.00 83.83 ? 2074 LYS B N 1 ATOM 6117 C CA . LYS B 2 538 ? 12.699 -20.680 30.313 1.00 84.75 ? 2074 LYS B CA 1 ATOM 6118 C C . LYS B 2 538 ? 11.409 -21.364 29.869 1.00 85.42 ? 2074 LYS B C 1 ATOM 6119 O O . LYS B 2 538 ? 11.412 -22.524 29.456 1.00 85.17 ? 2074 LYS B O 1 ATOM 6120 C CB . LYS B 2 538 ? 12.971 -20.981 31.785 1.00 85.01 ? 2074 LYS B CB 1 ATOM 6121 C CG . LYS B 2 538 ? 13.385 -22.408 32.049 1.00 85.59 ? 2074 LYS B CG 1 ATOM 6122 C CD . LYS B 2 538 ? 13.977 -22.551 33.443 1.00 87.51 ? 2074 LYS B CD 1 ATOM 6123 C CE . LYS B 2 538 ? 14.563 -23.940 33.650 1.00 88.08 ? 2074 LYS B CE 1 ATOM 6124 N NZ . LYS B 2 538 ? 13.552 -25.009 33.400 1.00 88.93 ? 2074 LYS B NZ 1 ATOM 6125 N N . ALA B 2 539 ? 10.310 -20.624 29.948 1.00 86.29 ? 2075 ALA B N 1 ATOM 6126 C CA . ALA B 2 539 ? 9.005 -21.121 29.545 1.00 86.82 ? 2075 ALA B CA 1 ATOM 6127 C C . ALA B 2 539 ? 8.308 -20.073 28.685 1.00 87.50 ? 2075 ALA B C 1 ATOM 6128 O O . ALA B 2 539 ? 8.442 -18.874 28.923 1.00 87.80 ? 2075 ALA B O 1 ATOM 6129 C CB . ALA B 2 539 ? 8.163 -21.428 30.775 1.00 86.63 ? 2075 ALA B CB 1 ATOM 6130 N N . ASN B 2 540 ? 7.580 -20.525 27.674 1.00 89.16 ? 2076 ASN B N 1 ATOM 6131 C CA . ASN B 2 540 ? 6.849 -19.616 26.804 1.00 91.66 ? 2076 ASN B CA 1 ATOM 6132 C C . ASN B 2 540 ? 5.356 -19.820 27.055 1.00 93.70 ? 2076 ASN B C 1 ATOM 6133 O O . ASN B 2 540 ? 4.645 -20.439 26.257 1.00 93.51 ? 2076 ASN B O 1 ATOM 6134 C CB . ASN B 2 540 ? 7.196 -19.880 25.336 1.00 90.74 ? 2076 ASN B CB 1 ATOM 6135 C CG . ASN B 2 540 ? 8.645 -19.549 25.010 1.00 90.72 ? 2076 ASN B CG 1 ATOM 6136 O OD1 . ASN B 2 540 ? 9.032 -19.502 23.844 1.00 91.07 ? 2076 ASN B OD1 1 ATOM 6137 N ND2 . ASN B 2 540 ? 9.452 -19.322 26.041 1.00 89.72 ? 2076 ASN B ND2 1 ATOM 6138 N N . ASN B 2 541 ? 4.898 -19.287 28.185 1.00 95.69 ? 2077 ASN B N 1 ATOM 6139 C CA . ASN B 2 541 ? 3.508 -19.397 28.609 1.00 97.46 ? 2077 ASN B CA 1 ATOM 6140 C C . ASN B 2 541 ? 2.703 -18.110 28.440 1.00 98.53 ? 2077 ASN B C 1 ATOM 6141 O O . ASN B 2 541 ? 2.107 -17.873 27.391 1.00 98.71 ? 2077 ASN B O 1 ATOM 6142 C CB . ASN B 2 541 ? 3.457 -19.847 30.076 1.00 97.73 ? 2077 ASN B CB 1 ATOM 6143 C CG . ASN B 2 541 ? 4.461 -19.108 30.957 1.00 97.99 ? 2077 ASN B CG 1 ATOM 6144 O OD1 . ASN B 2 541 ? 4.410 -17.884 31.099 1.00 98.14 ? 2077 ASN B OD1 1 ATOM 6145 N ND2 . ASN B 2 541 ? 5.382 -19.857 31.553 1.00 98.25 ? 2077 ASN B ND2 1 ATOM 6146 N N . ASN B 2 542 ? 2.682 -17.291 29.488 1.00 99.18 ? 2078 ASN B N 1 ATOM 6147 C CA . ASN B 2 542 ? 1.949 -16.036 29.480 1.00 99.18 ? 2078 ASN B CA 1 ATOM 6148 C C . ASN B 2 542 ? 2.274 -15.204 30.717 1.00 98.53 ? 2078 ASN B C 1 ATOM 6149 O O . ASN B 2 542 ? 2.282 -13.973 30.661 1.00 99.25 ? 2078 ASN B O 1 ATOM 6150 C CB . ASN B 2 542 ? 0.448 -16.309 29.419 1.00 100.50 ? 2078 ASN B CB 1 ATOM 6151 C CG . ASN B 2 542 ? -0.374 -15.056 29.593 1.00 101.84 ? 2078 ASN B CG 1 ATOM 6152 O OD1 . ASN B 2 542 ? -0.153 -14.052 28.912 1.00 103.46 ? 2078 ASN B OD1 1 ATOM 6153 N ND2 . ASN B 2 542 ? -1.336 -15.103 30.508 1.00 103.05 ? 2078 ASN B ND2 1 ATOM 6154 N N . ASN B 2 543 ? 2.542 -15.869 31.835 1.00 97.50 ? 2079 ASN B N 1 ATOM 6155 C CA . ASN B 2 543 ? 2.884 -15.144 33.052 1.00 96.65 ? 2079 ASN B CA 1 ATOM 6156 C C . ASN B 2 543 ? 4.383 -15.192 33.333 1.00 94.59 ? 2079 ASN B C 1 ATOM 6157 O O . ASN B 2 543 ? 4.828 -15.718 34.357 1.00 93.85 ? 2079 ASN B O 1 ATOM 6158 C CB . ASN B 2 543 ? 2.125 -15.691 34.262 1.00 99.05 ? 2079 ASN B CB 1 ATOM 6159 C CG . ASN B 2 543 ? 2.190 -14.748 35.461 1.00 100.78 ? 2079 ASN B CG 1 ATOM 6160 O OD1 . ASN B 2 543 ? 1.768 -15.097 36.569 1.00 101.73 ? 2079 ASN B OD1 1 ATOM 6161 N ND2 . ASN B 2 543 ? 2.714 -13.541 35.237 1.00 100.40 ? 2079 ASN B ND2 1 ATOM 6162 N N . GLN B 2 544 ? 5.155 -14.656 32.396 1.00 91.70 ? 2080 GLN B N 1 ATOM 6163 C CA . GLN B 2 544 ? 6.600 -14.578 32.531 1.00 88.42 ? 2080 GLN B CA 1 ATOM 6164 C C . GLN B 2 544 ? 6.884 -13.093 32.684 1.00 86.16 ? 2080 GLN B C 1 ATOM 6165 O O . GLN B 2 544 ? 6.084 -12.262 32.254 1.00 85.21 ? 2080 GLN B O 1 ATOM 6166 C CB . GLN B 2 544 ? 7.291 -15.103 31.272 1.00 88.50 ? 2080 GLN B CB 1 ATOM 6167 C CG . GLN B 2 544 ? 7.492 -16.606 31.238 1.00 88.36 ? 2080 GLN B CG 1 ATOM 6168 C CD . GLN B 2 544 ? 8.400 -17.092 32.351 1.00 89.04 ? 2080 GLN B CD 1 ATOM 6169 O OE1 . GLN B 2 544 ? 9.312 -16.382 32.775 1.00 89.01 ? 2080 GLN B OE1 1 ATOM 6170 N NE2 . GLN B 2 544 ? 8.165 -18.312 32.819 1.00 88.71 ? 2080 GLN B NE2 1 ATOM 6171 N N . TRP B 2 545 ? 8.001 -12.744 33.305 1.00 83.07 ? 2081 TRP B N 1 ATOM 6172 C CA . TRP B 2 545 ? 8.309 -11.335 33.449 1.00 80.38 ? 2081 TRP B CA 1 ATOM 6173 C C . TRP B 2 545 ? 9.779 -10.974 33.525 1.00 79.86 ? 2081 TRP B C 1 ATOM 6174 O O . TRP B 2 545 ? 10.614 -11.740 34.020 1.00 79.29 ? 2081 TRP B O 1 ATOM 6175 C CB . TRP B 2 545 ? 7.594 -10.751 34.662 1.00 78.46 ? 2081 TRP B CB 1 ATOM 6176 C CG . TRP B 2 545 ? 7.842 -11.493 35.912 1.00 76.86 ? 2081 TRP B CG 1 ATOM 6177 C CD1 . TRP B 2 545 ? 7.024 -12.417 36.486 1.00 77.20 ? 2081 TRP B CD1 1 ATOM 6178 C CD2 . TRP B 2 545 ? 8.976 -11.365 36.775 1.00 75.08 ? 2081 TRP B CD2 1 ATOM 6179 N NE1 . TRP B 2 545 ? 7.571 -12.869 37.659 1.00 76.33 ? 2081 TRP B NE1 1 ATOM 6180 C CE2 . TRP B 2 545 ? 8.771 -12.241 37.861 1.00 74.63 ? 2081 TRP B CE2 1 ATOM 6181 C CE3 . TRP B 2 545 ? 10.143 -10.595 36.739 1.00 74.46 ? 2081 TRP B CE3 1 ATOM 6182 C CZ2 . TRP B 2 545 ? 9.691 -12.369 38.902 1.00 72.50 ? 2081 TRP B CZ2 1 ATOM 6183 C CZ3 . TRP B 2 545 ? 11.058 -10.722 37.776 1.00 73.49 ? 2081 TRP B CZ3 1 ATOM 6184 C CH2 . TRP B 2 545 ? 10.824 -11.604 38.843 1.00 73.72 ? 2081 TRP B CH2 1 ATOM 6185 N N . LEU B 2 546 ? 10.069 -9.781 33.013 1.00 78.42 ? 2082 LEU B N 1 ATOM 6186 C CA . LEU B 2 546 ? 11.406 -9.215 33.004 1.00 76.65 ? 2082 LEU B CA 1 ATOM 6187 C C . LEU B 2 546 ? 11.249 -7.872 33.706 1.00 76.12 ? 2082 LEU B C 1 ATOM 6188 O O . LEU B 2 546 ? 10.419 -7.053 33.307 1.00 75.55 ? 2082 LEU B O 1 ATOM 6189 C CB . LEU B 2 546 ? 11.889 -9.018 31.557 1.00 75.39 ? 2082 LEU B CB 1 ATOM 6190 C CG . LEU B 2 546 ? 13.330 -8.577 31.250 1.00 74.37 ? 2082 LEU B CG 1 ATOM 6191 C CD1 . LEU B 2 546 ? 13.531 -7.134 31.643 1.00 73.70 ? 2082 LEU B CD1 1 ATOM 6192 C CD2 . LEU B 2 546 ? 14.323 -9.471 31.974 1.00 73.50 ? 2082 LEU B CD2 1 ATOM 6193 N N . GLN B 2 547 ? 12.010 -7.661 34.774 1.00 75.36 ? 2083 GLN B N 1 ATOM 6194 C CA . GLN B 2 547 ? 11.937 -6.396 35.488 1.00 75.36 ? 2083 GLN B CA 1 ATOM 6195 C C . GLN B 2 547 ? 13.315 -5.795 35.713 1.00 75.30 ? 2083 GLN B C 1 ATOM 6196 O O . GLN B 2 547 ? 14.320 -6.512 35.813 1.00 73.54 ? 2083 GLN B O 1 ATOM 6197 C CB . GLN B 2 547 ? 11.221 -6.553 36.835 1.00 76.35 ? 2083 GLN B CB 1 ATOM 6198 C CG . GLN B 2 547 ? 11.880 -7.499 37.814 1.00 75.21 ? 2083 GLN B CG 1 ATOM 6199 C CD . GLN B 2 547 ? 11.451 -7.234 39.239 1.00 74.79 ? 2083 GLN B CD 1 ATOM 6200 O OE1 . GLN B 2 547 ? 12.049 -6.414 39.933 1.00 74.12 ? 2083 GLN B OE1 1 ATOM 6201 N NE2 . GLN B 2 547 ? 10.398 -7.915 39.680 1.00 73.78 ? 2083 GLN B NE2 1 ATOM 6202 N N . ILE B 2 548 ? 13.342 -4.466 35.791 1.00 75.66 ? 2084 ILE B N 1 ATOM 6203 C CA . ILE B 2 548 ? 14.573 -3.710 35.991 1.00 75.13 ? 2084 ILE B CA 1 ATOM 6204 C C . ILE B 2 548 ? 14.460 -2.843 37.240 1.00 75.77 ? 2084 ILE B C 1 ATOM 6205 O O . ILE B 2 548 ? 13.394 -2.286 37.532 1.00 75.32 ? 2084 ILE B O 1 ATOM 6206 C CB . ILE B 2 548 ? 14.866 -2.802 34.768 1.00 73.99 ? 2084 ILE B CB 1 ATOM 6207 C CG1 . ILE B 2 548 ? 14.846 -3.644 33.491 1.00 71.88 ? 2084 ILE B CG1 1 ATOM 6208 C CG2 . ILE B 2 548 ? 16.214 -2.107 34.941 1.00 71.90 ? 2084 ILE B CG2 1 ATOM 6209 C CD1 . ILE B 2 548 ? 14.834 -2.849 32.228 1.00 72.88 ? 2084 ILE B CD1 1 ATOM 6210 N N . ASP B 2 549 ? 15.571 -2.733 37.964 1.00 76.60 ? 2085 ASP B N 1 ATOM 6211 C CA . ASP B 2 549 ? 15.634 -1.953 39.198 1.00 76.53 ? 2085 ASP B CA 1 ATOM 6212 C C . ASP B 2 549 ? 16.354 -0.637 38.927 1.00 74.85 ? 2085 ASP B C 1 ATOM 6213 O O . ASP B 2 549 ? 17.581 -0.584 38.904 1.00 74.07 ? 2085 ASP B O 1 ATOM 6214 C CB . ASP B 2 549 ? 16.393 -2.746 40.270 1.00 79.90 ? 2085 ASP B CB 1 ATOM 6215 C CG . ASP B 2 549 ? 16.099 -2.266 41.691 1.00 83.47 ? 2085 ASP B CG 1 ATOM 6216 O OD1 . ASP B 2 549 ? 16.053 -1.032 41.916 1.00 84.37 ? 2085 ASP B OD1 1 ATOM 6217 O OD2 . ASP B 2 549 ? 15.932 -3.132 42.588 1.00 82.20 ? 2085 ASP B OD2 1 ATOM 6218 N N . LEU B 2 550 ? 15.582 0.423 38.720 1.00 73.86 ? 2086 LEU B N 1 ATOM 6219 C CA . LEU B 2 550 ? 16.141 1.742 38.450 1.00 72.73 ? 2086 LEU B CA 1 ATOM 6220 C C . LEU B 2 550 ? 16.782 2.345 39.699 1.00 73.20 ? 2086 LEU B C 1 ATOM 6221 O O . LEU B 2 550 ? 17.125 3.532 39.727 1.00 73.67 ? 2086 LEU B O 1 ATOM 6222 C CB . LEU B 2 550 ? 15.043 2.664 37.906 1.00 69.96 ? 2086 LEU B CB 1 ATOM 6223 C CG . LEU B 2 550 ? 14.490 2.236 36.541 1.00 66.59 ? 2086 LEU B CG 1 ATOM 6224 C CD1 . LEU B 2 550 ? 13.198 2.966 36.221 1.00 64.13 ? 2086 LEU B CD1 1 ATOM 6225 C CD2 . LEU B 2 550 ? 15.541 2.496 35.485 1.00 64.93 ? 2086 LEU B CD2 1 ATOM 6226 N N . LEU B 2 551 ? 16.942 1.504 40.720 1.00 73.69 ? 2087 LEU B N 1 ATOM 6227 C CA . LEU B 2 551 ? 17.540 1.876 42.004 1.00 73.22 ? 2087 LEU B CA 1 ATOM 6228 C C . LEU B 2 551 ? 16.918 3.088 42.698 1.00 73.52 ? 2087 LEU B C 1 ATOM 6229 O O . LEU B 2 551 ? 17.086 3.266 43.901 1.00 75.02 ? 2087 LEU B O 1 ATOM 6230 C CB . LEU B 2 551 ? 19.051 2.079 41.838 1.00 72.86 ? 2087 LEU B CB 1 ATOM 6231 C CG . LEU B 2 551 ? 19.865 0.799 41.578 1.00 71.69 ? 2087 LEU B CG 1 ATOM 6232 C CD1 . LEU B 2 551 ? 21.260 1.131 41.075 1.00 71.55 ? 2087 LEU B CD1 1 ATOM 6233 C CD2 . LEU B 2 551 ? 19.951 -0.003 42.852 1.00 70.64 ? 2087 LEU B CD2 1 ATOM 6234 N N . LYS B 2 552 ? 16.192 3.910 41.948 1.00 73.72 ? 2088 LYS B N 1 ATOM 6235 C CA . LYS B 2 552 ? 15.538 5.099 42.497 1.00 72.98 ? 2088 LYS B CA 1 ATOM 6236 C C . LYS B 2 552 ? 14.271 5.328 41.683 1.00 72.12 ? 2088 LYS B C 1 ATOM 6237 O O . LYS B 2 552 ? 14.037 4.639 40.691 1.00 72.70 ? 2088 LYS B O 1 ATOM 6238 C CB . LYS B 2 552 ? 16.441 6.330 42.349 1.00 73.94 ? 2088 LYS B CB 1 ATOM 6239 C CG . LYS B 2 552 ? 17.853 6.175 42.910 1.00 75.51 ? 2088 LYS B CG 1 ATOM 6240 C CD . LYS B 2 552 ? 18.799 7.284 42.416 1.00 75.06 ? 2088 LYS B CD 1 ATOM 6241 C CE . LYS B 2 552 ? 18.318 8.676 42.817 1.00 75.07 ? 2088 LYS B CE 1 ATOM 6242 N NZ . LYS B 2 552 ? 19.228 9.752 42.317 1.00 75.16 ? 2088 LYS B NZ 1 ATOM 6243 N N . ILE B 2 553 ? 13.444 6.279 42.100 1.00 69.90 ? 2089 ILE B N 1 ATOM 6244 C CA . ILE B 2 553 ? 12.249 6.577 41.332 1.00 68.67 ? 2089 ILE B CA 1 ATOM 6245 C C . ILE B 2 553 ? 12.714 7.454 40.175 1.00 69.11 ? 2089 ILE B C 1 ATOM 6246 O O . ILE B 2 553 ? 13.371 8.472 40.391 1.00 71.05 ? 2089 ILE B O 1 ATOM 6247 C CB . ILE B 2 553 ? 11.206 7.345 42.162 1.00 68.62 ? 2089 ILE B CB 1 ATOM 6248 C CG1 . ILE B 2 553 ? 10.192 6.368 42.744 1.00 68.42 ? 2089 ILE B CG1 1 ATOM 6249 C CG2 . ILE B 2 553 ? 10.504 8.384 41.301 1.00 67.86 ? 2089 ILE B CG2 1 ATOM 6250 C CD1 . ILE B 2 553 ? 8.968 7.056 43.326 1.00 71.40 ? 2089 ILE B CD1 1 ATOM 6251 N N . LYS B 2 554 ? 12.389 7.050 38.950 1.00 67.38 ? 2090 LYS B N 1 ATOM 6252 C CA . LYS B 2 554 ? 12.778 7.797 37.760 1.00 63.52 ? 2090 LYS B CA 1 ATOM 6253 C C . LYS B 2 554 ? 11.522 8.208 36.997 1.00 63.56 ? 2090 LYS B C 1 ATOM 6254 O O . LYS B 2 554 ? 10.404 7.870 37.394 1.00 63.60 ? 2090 LYS B O 1 ATOM 6255 C CB . LYS B 2 554 ? 13.647 6.920 36.857 1.00 61.80 ? 2090 LYS B CB 1 ATOM 6256 C CG . LYS B 2 554 ? 15.007 6.556 37.416 1.00 59.98 ? 2090 LYS B CG 1 ATOM 6257 C CD . LYS B 2 554 ? 15.972 7.722 37.358 1.00 59.58 ? 2090 LYS B CD 1 ATOM 6258 C CE . LYS B 2 554 ? 17.391 7.322 37.763 1.00 59.12 ? 2090 LYS B CE 1 ATOM 6259 N NZ . LYS B 2 554 ? 18.021 6.334 36.841 1.00 58.32 ? 2090 LYS B NZ 1 ATOM 6260 N N . LYS B 2 555 ? 11.714 8.940 35.899 1.00 62.42 ? 2091 LYS B N 1 ATOM 6261 C CA . LYS B 2 555 ? 10.607 9.370 35.047 1.00 59.25 ? 2091 LYS B CA 1 ATOM 6262 C C . LYS B 2 555 ? 10.737 8.560 33.748 1.00 57.99 ? 2091 LYS B C 1 ATOM 6263 O O . LYS B 2 555 ? 11.551 8.889 32.900 1.00 56.25 ? 2091 LYS B O 1 ATOM 6264 C CB . LYS B 2 555 ? 10.723 10.868 34.763 1.00 56.46 ? 2091 LYS B CB 1 ATOM 6265 C CG . LYS B 2 555 ? 9.451 11.528 34.224 1.00 58.25 ? 2091 LYS B CG 1 ATOM 6266 C CD . LYS B 2 555 ? 9.667 13.033 34.008 1.00 59.97 ? 2091 LYS B CD 1 ATOM 6267 C CE . LYS B 2 555 ? 8.404 13.741 33.539 1.00 61.76 ? 2091 LYS B CE 1 ATOM 6268 N NZ . LYS B 2 555 ? 7.920 13.232 32.226 1.00 64.24 ? 2091 LYS B NZ 1 ATOM 6269 N N . ILE B 2 556 ? 9.942 7.498 33.609 1.00 56.49 ? 2092 ILE B N 1 ATOM 6270 C CA . ILE B 2 556 ? 9.996 6.633 32.428 1.00 56.51 ? 2092 ILE B CA 1 ATOM 6271 C C . ILE B 2 556 ? 9.090 7.139 31.304 1.00 57.30 ? 2092 ILE B C 1 ATOM 6272 O O . ILE B 2 556 ? 7.873 7.079 31.426 1.00 56.67 ? 2092 ILE B O 1 ATOM 6273 C CB . ILE B 2 556 ? 9.582 5.170 32.781 1.00 56.83 ? 2092 ILE B CB 1 ATOM 6274 C CG1 . ILE B 2 556 ? 10.189 4.744 34.127 1.00 56.06 ? 2092 ILE B CG1 1 ATOM 6275 C CG2 . ILE B 2 556 ? 10.050 4.217 31.695 1.00 55.37 ? 2092 ILE B CG2 1 ATOM 6276 C CD1 . ILE B 2 556 ? 11.678 5.016 34.265 1.00 56.17 ? 2092 ILE B CD1 1 ATOM 6277 N N . THR B 2 557 ? 9.687 7.621 30.209 1.00 57.62 ? 2093 THR B N 1 ATOM 6278 C CA . THR B 2 557 ? 8.925 8.159 29.076 1.00 56.63 ? 2093 THR B CA 1 ATOM 6279 C C . THR B 2 557 ? 8.699 7.197 27.901 1.00 55.42 ? 2093 THR B C 1 ATOM 6280 O O . THR B 2 557 ? 7.752 7.377 27.118 1.00 54.77 ? 2093 THR B O 1 ATOM 6281 C CB . THR B 2 557 ? 9.569 9.474 28.531 1.00 57.16 ? 2093 THR B CB 1 ATOM 6282 O OG1 . THR B 2 557 ? 10.996 9.402 28.647 1.00 58.13 ? 2093 THR B OG1 1 ATOM 6283 C CG2 . THR B 2 557 ? 9.063 10.684 29.302 1.00 57.42 ? 2093 THR B CG2 1 ATOM 6284 N N . ALA B 2 558 ? 9.556 6.185 27.769 1.00 51.91 ? 2094 ALA B N 1 ATOM 6285 C CA . ALA B 2 558 ? 9.393 5.221 26.688 1.00 49.75 ? 2094 ALA B CA 1 ATOM 6286 C C . ALA B 2 558 ? 10.193 3.933 26.856 1.00 49.78 ? 2094 ALA B C 1 ATOM 6287 O O . ALA B 2 558 ? 10.921 3.749 27.840 1.00 46.62 ? 2094 ALA B O 1 ATOM 6288 C CB . ALA B 2 558 ? 9.733 5.870 25.364 1.00 50.14 ? 2094 ALA B CB 1 ATOM 6289 N N . ILE B 2 559 ? 10.051 3.055 25.863 1.00 50.46 ? 2095 ILE B N 1 ATOM 6290 C CA . ILE B 2 559 ? 10.713 1.754 25.832 1.00 51.05 ? 2095 ILE B CA 1 ATOM 6291 C C . ILE B 2 559 ? 10.967 1.282 24.392 1.00 52.31 ? 2095 ILE B C 1 ATOM 6292 O O . ILE B 2 559 ? 10.169 1.558 23.479 1.00 52.38 ? 2095 ILE B O 1 ATOM 6293 C CB . ILE B 2 559 ? 9.849 0.695 26.555 1.00 51.55 ? 2095 ILE B CB 1 ATOM 6294 C CG1 . ILE B 2 559 ? 10.560 -0.656 26.564 1.00 52.46 ? 2095 ILE B CG1 1 ATOM 6295 C CG2 . ILE B 2 559 ? 8.492 0.567 25.867 1.00 50.64 ? 2095 ILE B CG2 1 ATOM 6296 C CD1 . ILE B 2 559 ? 9.914 -1.683 27.498 1.00 50.93 ? 2095 ILE B CD1 1 ATOM 6297 N N . VAL B 2 560 ? 12.086 0.584 24.193 1.00 51.73 ? 2096 VAL B N 1 ATOM 6298 C CA . VAL B 2 560 ? 12.451 0.047 22.877 1.00 51.72 ? 2096 VAL B CA 1 ATOM 6299 C C . VAL B 2 560 ? 12.658 -1.470 23.011 1.00 53.32 ? 2096 VAL B C 1 ATOM 6300 O O . VAL B 2 560 ? 13.438 -1.939 23.842 1.00 53.91 ? 2096 VAL B O 1 ATOM 6301 C CB . VAL B 2 560 ? 13.747 0.704 22.326 1.00 48.83 ? 2096 VAL B CB 1 ATOM 6302 C CG1 . VAL B 2 560 ? 14.211 -0.015 21.069 1.00 47.55 ? 2096 VAL B CG1 1 ATOM 6303 C CG2 . VAL B 2 560 ? 13.488 2.146 22.003 1.00 44.74 ? 2096 VAL B CG2 1 ATOM 6304 N N . THR B 2 561 ? 11.959 -2.244 22.194 1.00 52.30 ? 2097 THR B N 1 ATOM 6305 C CA . THR B 2 561 ? 12.091 -3.682 22.304 1.00 51.82 ? 2097 THR B CA 1 ATOM 6306 C C . THR B 2 561 ? 12.707 -4.292 21.055 1.00 51.69 ? 2097 THR B C 1 ATOM 6307 O O . THR B 2 561 ? 12.467 -3.832 19.946 1.00 50.83 ? 2097 THR B O 1 ATOM 6308 C CB . THR B 2 561 ? 10.719 -4.337 22.596 1.00 51.28 ? 2097 THR B CB 1 ATOM 6309 O OG1 . THR B 2 561 ? 10.303 -5.106 21.461 1.00 50.60 ? 2097 THR B OG1 1 ATOM 6310 C CG2 . THR B 2 561 ? 9.665 -3.258 22.904 1.00 49.04 ? 2097 THR B CG2 1 ATOM 6311 N N . GLN B 2 562 ? 13.501 -5.340 21.252 1.00 51.93 ? 2098 GLN B N 1 ATOM 6312 C CA . GLN B 2 562 ? 14.178 -6.005 20.156 1.00 51.64 ? 2098 GLN B CA 1 ATOM 6313 C C . GLN B 2 562 ? 14.293 -7.519 20.365 1.00 54.76 ? 2098 GLN B C 1 ATOM 6314 O O . GLN B 2 562 ? 14.570 -8.007 21.471 1.00 52.86 ? 2098 GLN B O 1 ATOM 6315 C CB . GLN B 2 562 ? 15.556 -5.385 19.997 1.00 48.61 ? 2098 GLN B CB 1 ATOM 6316 C CG . GLN B 2 562 ? 16.380 -5.957 18.887 1.00 46.41 ? 2098 GLN B CG 1 ATOM 6317 C CD . GLN B 2 562 ? 17.733 -5.298 18.816 1.00 43.90 ? 2098 GLN B CD 1 ATOM 6318 O OE1 . GLN B 2 562 ? 18.420 -5.175 19.824 1.00 44.05 ? 2098 GLN B OE1 1 ATOM 6319 N NE2 . GLN B 2 562 ? 18.124 -4.868 17.626 1.00 40.71 ? 2098 GLN B NE2 1 ATOM 6320 N N . GLY B 2 563 ? 14.083 -8.262 19.284 1.00 58.21 ? 2099 GLY B N 1 ATOM 6321 C CA . GLY B 2 563 ? 14.154 -9.712 19.354 1.00 60.21 ? 2099 GLY B CA 1 ATOM 6322 C C . GLY B 2 563 ? 15.562 -10.253 19.474 1.00 61.18 ? 2099 GLY B C 1 ATOM 6323 O O . GLY B 2 563 ? 16.425 -9.639 20.098 1.00 61.22 ? 2099 GLY B O 1 ATOM 6324 N N . CYS B 2 564 ? 15.785 -11.414 18.873 1.00 62.23 ? 2100 CYS B N 1 ATOM 6325 C CA . CYS B 2 564 ? 17.087 -12.065 18.895 1.00 63.69 ? 2100 CYS B CA 1 ATOM 6326 C C . CYS B 2 564 ? 17.165 -13.155 17.838 1.00 65.42 ? 2100 CYS B C 1 ATOM 6327 O O . CYS B 2 564 ? 16.248 -13.964 17.703 1.00 66.05 ? 2100 CYS B O 1 ATOM 6328 C CB . CYS B 2 564 ? 17.354 -12.676 20.255 1.00 63.81 ? 2100 CYS B CB 1 ATOM 6329 S SG . CYS B 2 564 ? 18.619 -13.932 20.171 1.00 64.37 ? 2100 CYS B SG 1 ATOM 6330 N N . LYS B 2 565 ? 18.271 -13.177 17.102 1.00 66.65 ? 2101 LYS B N 1 ATOM 6331 C CA . LYS B 2 565 ? 18.469 -14.147 16.033 1.00 67.48 ? 2101 LYS B CA 1 ATOM 6332 C C . LYS B 2 565 ? 19.680 -15.024 16.298 1.00 68.17 ? 2101 LYS B C 1 ATOM 6333 O O . LYS B 2 565 ? 20.759 -14.807 15.744 1.00 67.32 ? 2101 LYS B O 1 ATOM 6334 C CB . LYS B 2 565 ? 18.640 -13.406 14.708 1.00 69.47 ? 2101 LYS B CB 1 ATOM 6335 C CG . LYS B 2 565 ? 18.741 -14.280 13.483 1.00 70.42 ? 2101 LYS B CG 1 ATOM 6336 C CD . LYS B 2 565 ? 18.530 -13.427 12.244 1.00 73.70 ? 2101 LYS B CD 1 ATOM 6337 C CE . LYS B 2 565 ? 18.345 -14.271 10.984 1.00 76.55 ? 2101 LYS B CE 1 ATOM 6338 N NZ . LYS B 2 565 ? 17.989 -13.435 9.792 1.00 76.51 ? 2101 LYS B NZ 1 ATOM 6339 N N . SER B 2 566 ? 19.496 -16.017 17.156 1.00 69.02 ? 2102 SER B N 1 ATOM 6340 C CA . SER B 2 566 ? 20.578 -16.922 17.487 1.00 70.16 ? 2102 SER B CA 1 ATOM 6341 C C . SER B 2 566 ? 20.185 -18.352 17.190 1.00 70.85 ? 2102 SER B C 1 ATOM 6342 O O . SER B 2 566 ? 18.998 -18.684 17.155 1.00 70.35 ? 2102 SER B O 1 ATOM 6343 C CB . SER B 2 566 ? 20.959 -16.772 18.955 1.00 70.67 ? 2102 SER B CB 1 ATOM 6344 O OG . SER B 2 566 ? 21.543 -15.499 19.184 1.00 69.68 ? 2102 SER B OG 1 ATOM 6345 N N . LEU B 2 567 ? 21.194 -19.191 16.971 1.00 72.21 ? 2103 LEU B N 1 ATOM 6346 C CA . LEU B 2 567 ? 20.986 -20.599 16.650 1.00 73.19 ? 2103 LEU B CA 1 ATOM 6347 C C . LEU B 2 567 ? 20.042 -20.720 15.458 1.00 74.34 ? 2103 LEU B C 1 ATOM 6348 O O . LEU B 2 567 ? 19.214 -21.625 15.402 1.00 75.27 ? 2103 LEU B O 1 ATOM 6349 C CB . LEU B 2 567 ? 20.395 -21.332 17.851 1.00 71.35 ? 2103 LEU B CB 1 ATOM 6350 C CG . LEU B 2 567 ? 21.208 -21.169 19.130 1.00 70.92 ? 2103 LEU B CG 1 ATOM 6351 C CD1 . LEU B 2 567 ? 20.576 -21.997 20.249 1.00 69.63 ? 2103 LEU B CD1 1 ATOM 6352 C CD2 . LEU B 2 567 ? 22.649 -21.597 18.866 1.00 68.51 ? 2103 LEU B CD2 1 ATOM 6353 N N . SER B 2 568 ? 20.171 -19.793 14.513 1.00 74.39 ? 2104 SER B N 1 ATOM 6354 C CA . SER B 2 568 ? 19.333 -19.778 13.320 1.00 74.61 ? 2104 SER B CA 1 ATOM 6355 C C . SER B 2 568 ? 17.833 -19.814 13.596 1.00 73.39 ? 2104 SER B C 1 ATOM 6356 O O . SER B 2 568 ? 17.079 -20.386 12.817 1.00 72.49 ? 2104 SER B O 1 ATOM 6357 C CB . SER B 2 568 ? 19.702 -20.940 12.396 1.00 76.04 ? 2104 SER B CB 1 ATOM 6358 O OG . SER B 2 568 ? 20.967 -20.730 11.792 1.00 80.73 ? 2104 SER B OG 1 ATOM 6359 N N . SER B 2 569 ? 17.394 -19.195 14.687 1.00 73.09 ? 2105 SER B N 1 ATOM 6360 C CA . SER B 2 569 ? 15.971 -19.179 15.010 1.00 73.95 ? 2105 SER B CA 1 ATOM 6361 C C . SER B 2 569 ? 15.482 -17.807 15.462 1.00 73.63 ? 2105 SER B C 1 ATOM 6362 O O . SER B 2 569 ? 15.785 -17.362 16.570 1.00 73.44 ? 2105 SER B O 1 ATOM 6363 C CB . SER B 2 569 ? 15.653 -20.210 16.097 1.00 75.80 ? 2105 SER B CB 1 ATOM 6364 O OG . SER B 2 569 ? 14.275 -20.179 16.432 1.00 76.90 ? 2105 SER B OG 1 ATOM 6365 N N . GLU B 2 570 ? 14.702 -17.161 14.600 1.00 72.82 ? 2106 GLU B N 1 ATOM 6366 C CA . GLU B 2 570 ? 14.147 -15.842 14.872 1.00 71.72 ? 2106 GLU B CA 1 ATOM 6367 C C . GLU B 2 570 ? 12.988 -15.849 15.878 1.00 69.46 ? 2106 GLU B C 1 ATOM 6368 O O . GLU B 2 570 ? 11.834 -16.107 15.534 1.00 66.52 ? 2106 GLU B O 1 ATOM 6369 C CB . GLU B 2 570 ? 13.716 -15.204 13.555 1.00 73.74 ? 2106 GLU B CB 1 ATOM 6370 C CG . GLU B 2 570 ? 14.865 -15.129 12.554 1.00 77.76 ? 2106 GLU B CG 1 ATOM 6371 C CD . GLU B 2 570 ? 14.484 -14.484 11.229 1.00 79.81 ? 2106 GLU B CD 1 ATOM 6372 O OE1 . GLU B 2 570 ? 15.368 -14.387 10.345 1.00 79.25 ? 2106 GLU B OE1 1 ATOM 6373 O OE2 . GLU B 2 570 ? 13.309 -14.074 11.072 1.00 81.59 ? 2106 GLU B OE2 1 ATOM 6374 N N . MET B 2 571 ? 13.327 -15.550 17.129 1.00 67.92 ? 2107 MET B N 1 ATOM 6375 C CA . MET B 2 571 ? 12.374 -15.506 18.231 1.00 66.47 ? 2107 MET B CA 1 ATOM 6376 C C . MET B 2 571 ? 12.326 -14.083 18.795 1.00 64.32 ? 2107 MET B C 1 ATOM 6377 O O . MET B 2 571 ? 13.361 -13.439 18.933 1.00 63.62 ? 2107 MET B O 1 ATOM 6378 C CB . MET B 2 571 ? 12.823 -16.483 19.320 1.00 66.14 ? 2107 MET B CB 1 ATOM 6379 C CG . MET B 2 571 ? 14.227 -16.197 19.816 1.00 68.31 ? 2107 MET B CG 1 ATOM 6380 S SD . MET B 2 571 ? 15.004 -17.515 20.763 1.00 69.08 ? 2107 MET B SD 1 ATOM 6381 C CE . MET B 2 571 ? 16.109 -18.198 19.507 1.00 70.13 ? 2107 MET B CE 1 ATOM 6382 N N . TYR B 2 572 ? 11.131 -13.598 19.123 1.00 62.69 ? 2108 TYR B N 1 ATOM 6383 C CA . TYR B 2 572 ? 10.982 -12.254 19.669 1.00 60.83 ? 2108 TYR B CA 1 ATOM 6384 C C . TYR B 2 572 ? 9.622 -11.996 20.308 1.00 60.48 ? 2108 TYR B C 1 ATOM 6385 O O . TYR B 2 572 ? 8.649 -12.656 19.974 1.00 62.27 ? 2108 TYR B O 1 ATOM 6386 C CB . TYR B 2 572 ? 11.234 -11.220 18.568 1.00 59.29 ? 2108 TYR B CB 1 ATOM 6387 C CG . TYR B 2 572 ? 10.415 -11.407 17.312 1.00 56.19 ? 2108 TYR B CG 1 ATOM 6388 C CD1 . TYR B 2 572 ? 9.107 -10.929 17.221 1.00 54.41 ? 2108 TYR B CD1 1 ATOM 6389 C CD2 . TYR B 2 572 ? 10.959 -12.060 16.201 1.00 55.62 ? 2108 TYR B CD2 1 ATOM 6390 C CE1 . TYR B 2 572 ? 8.357 -11.096 16.040 1.00 55.29 ? 2108 TYR B CE1 1 ATOM 6391 C CE2 . TYR B 2 572 ? 10.220 -12.234 15.018 1.00 54.66 ? 2108 TYR B CE2 1 ATOM 6392 C CZ . TYR B 2 572 ? 8.925 -11.753 14.942 1.00 55.48 ? 2108 TYR B CZ 1 ATOM 6393 O OH . TYR B 2 572 ? 8.213 -11.930 13.771 1.00 56.14 ? 2108 TYR B OH 1 ATOM 6394 N N . VAL B 2 573 ? 9.569 -11.028 21.224 1.00 59.53 ? 2109 VAL B N 1 ATOM 6395 C CA . VAL B 2 573 ? 8.332 -10.655 21.914 1.00 56.52 ? 2109 VAL B CA 1 ATOM 6396 C C . VAL B 2 573 ? 7.447 -9.785 21.020 1.00 56.82 ? 2109 VAL B C 1 ATOM 6397 O O . VAL B 2 573 ? 7.822 -8.674 20.660 1.00 54.83 ? 2109 VAL B O 1 ATOM 6398 C CB . VAL B 2 573 ? 8.635 -9.864 23.196 1.00 54.96 ? 2109 VAL B CB 1 ATOM 6399 C CG1 . VAL B 2 573 ? 7.356 -9.611 23.971 1.00 52.66 ? 2109 VAL B CG1 1 ATOM 6400 C CG2 . VAL B 2 573 ? 9.630 -10.616 24.035 1.00 54.35 ? 2109 VAL B CG2 1 ATOM 6401 N N . LYS B 2 574 ? 6.267 -10.291 20.674 1.00 59.10 ? 2110 LYS B N 1 ATOM 6402 C CA . LYS B 2 574 ? 5.338 -9.568 19.811 1.00 61.64 ? 2110 LYS B CA 1 ATOM 6403 C C . LYS B 2 574 ? 4.385 -8.600 20.531 1.00 62.19 ? 2110 LYS B C 1 ATOM 6404 O O . LYS B 2 574 ? 3.839 -7.689 19.903 1.00 63.92 ? 2110 LYS B O 1 ATOM 6405 C CB . LYS B 2 574 ? 4.533 -10.563 18.974 1.00 62.65 ? 2110 LYS B CB 1 ATOM 6406 C CG . LYS B 2 574 ? 5.308 -11.173 17.816 1.00 67.40 ? 2110 LYS B CG 1 ATOM 6407 C CD . LYS B 2 574 ? 4.561 -12.351 17.158 1.00 70.36 ? 2110 LYS B CD 1 ATOM 6408 C CE . LYS B 2 574 ? 3.098 -12.034 16.844 1.00 72.96 ? 2110 LYS B CE 1 ATOM 6409 N NZ . LYS B 2 574 ? 2.929 -10.816 15.991 1.00 77.16 ? 2110 LYS B NZ 1 ATOM 6410 N N . SER B 2 575 ? 4.183 -8.790 21.833 1.00 61.44 ? 2111 SER B N 1 ATOM 6411 C CA . SER B 2 575 ? 3.304 -7.919 22.612 1.00 60.89 ? 2111 SER B CA 1 ATOM 6412 C C . SER B 2 575 ? 3.594 -8.049 24.086 1.00 61.09 ? 2111 SER B C 1 ATOM 6413 O O . SER B 2 575 ? 3.978 -9.118 24.555 1.00 60.81 ? 2111 SER B O 1 ATOM 6414 C CB . SER B 2 575 ? 1.843 -8.267 22.383 1.00 61.94 ? 2111 SER B CB 1 ATOM 6415 O OG . SER B 2 575 ? 1.494 -8.049 21.036 1.00 63.44 ? 2111 SER B OG 1 ATOM 6416 N N . TYR B 2 576 ? 3.401 -6.957 24.818 1.00 61.53 ? 2112 TYR B N 1 ATOM 6417 C CA . TYR B 2 576 ? 3.651 -6.956 26.250 1.00 62.45 ? 2112 TYR B CA 1 ATOM 6418 C C . TYR B 2 576 ? 2.680 -6.098 27.053 1.00 63.56 ? 2112 TYR B C 1 ATOM 6419 O O . TYR B 2 576 ? 1.660 -5.627 26.538 1.00 63.06 ? 2112 TYR B O 1 ATOM 6420 C CB . TYR B 2 576 ? 5.093 -6.526 26.547 1.00 60.52 ? 2112 TYR B CB 1 ATOM 6421 C CG . TYR B 2 576 ? 5.567 -5.294 25.817 1.00 62.17 ? 2112 TYR B CG 1 ATOM 6422 C CD1 . TYR B 2 576 ? 6.167 -4.240 26.503 1.00 63.97 ? 2112 TYR B CD1 1 ATOM 6423 C CD2 . TYR B 2 576 ? 5.476 -5.203 24.428 1.00 65.69 ? 2112 TYR B CD2 1 ATOM 6424 C CE1 . TYR B 2 576 ? 6.674 -3.124 25.821 1.00 64.61 ? 2112 TYR B CE1 1 ATOM 6425 C CE2 . TYR B 2 576 ? 5.977 -4.094 23.733 1.00 66.56 ? 2112 TYR B CE2 1 ATOM 6426 C CZ . TYR B 2 576 ? 6.578 -3.064 24.437 1.00 66.44 ? 2112 TYR B CZ 1 ATOM 6427 O OH . TYR B 2 576 ? 7.108 -2.001 23.746 1.00 67.55 ? 2112 TYR B OH 1 ATOM 6428 N N . THR B 2 577 ? 3.010 -5.927 28.328 1.00 64.41 ? 2113 THR B N 1 ATOM 6429 C CA . THR B 2 577 ? 2.224 -5.147 29.270 1.00 66.68 ? 2113 THR B CA 1 ATOM 6430 C C . THR B 2 577 ? 3.194 -4.659 30.339 1.00 67.57 ? 2113 THR B C 1 ATOM 6431 O O . THR B 2 577 ? 4.105 -5.382 30.741 1.00 68.10 ? 2113 THR B O 1 ATOM 6432 C CB . THR B 2 577 ? 1.108 -6.016 29.901 1.00 67.87 ? 2113 THR B CB 1 ATOM 6433 O OG1 . THR B 2 577 ? -0.098 -5.860 29.141 1.00 68.68 ? 2113 THR B OG1 1 ATOM 6434 C CG2 . THR B 2 577 ? 0.855 -5.627 31.354 1.00 70.20 ? 2113 THR B CG2 1 ATOM 6435 N N . ILE B 2 578 ? 3.006 -3.435 30.810 1.00 68.08 ? 2114 ILE B N 1 ATOM 6436 C CA . ILE B 2 578 ? 3.924 -2.898 31.797 1.00 68.86 ? 2114 ILE B CA 1 ATOM 6437 C C . ILE B 2 578 ? 3.323 -2.793 33.196 1.00 71.07 ? 2114 ILE B C 1 ATOM 6438 O O . ILE B 2 578 ? 2.152 -2.461 33.362 1.00 72.00 ? 2114 ILE B O 1 ATOM 6439 C CB . ILE B 2 578 ? 4.455 -1.506 31.335 1.00 66.24 ? 2114 ILE B CB 1 ATOM 6440 C CG1 . ILE B 2 578 ? 4.983 -1.600 29.899 1.00 62.90 ? 2114 ILE B CG1 1 ATOM 6441 C CG2 . ILE B 2 578 ? 5.581 -1.032 32.245 1.00 65.62 ? 2114 ILE B CG2 1 ATOM 6442 C CD1 . ILE B 2 578 ? 6.180 -2.521 29.730 1.00 60.70 ? 2114 ILE B CD1 1 ATOM 6443 N N . HIS B 2 579 ? 4.149 -3.101 34.191 1.00 72.19 ? 2115 HIS B N 1 ATOM 6444 C CA . HIS B 2 579 ? 3.784 -3.042 35.599 1.00 73.28 ? 2115 HIS B CA 1 ATOM 6445 C C . HIS B 2 579 ? 4.918 -2.277 36.281 1.00 75.28 ? 2115 HIS B C 1 ATOM 6446 O O . HIS B 2 579 ? 6.095 -2.528 36.006 1.00 76.11 ? 2115 HIS B O 1 ATOM 6447 C CB . HIS B 2 579 ? 3.711 -4.450 36.206 1.00 75.49 ? 2115 HIS B CB 1 ATOM 6448 C CG . HIS B 2 579 ? 2.548 -5.271 35.737 1.00 76.29 ? 2115 HIS B CG 1 ATOM 6449 N ND1 . HIS B 2 579 ? 2.279 -6.528 36.241 1.00 75.69 ? 2115 HIS B ND1 1 ATOM 6450 C CD2 . HIS B 2 579 ? 1.576 -5.016 34.829 1.00 76.10 ? 2115 HIS B CD2 1 ATOM 6451 C CE1 . HIS B 2 579 ? 1.192 -7.008 35.665 1.00 76.01 ? 2115 HIS B CE1 1 ATOM 6452 N NE2 . HIS B 2 579 ? 0.745 -6.111 34.804 1.00 75.86 ? 2115 HIS B NE2 1 ATOM 6453 N N . TYR B 2 580 ? 4.577 -1.348 37.167 1.00 76.30 ? 2116 TYR B N 1 ATOM 6454 C CA . TYR B 2 580 ? 5.593 -0.571 37.865 1.00 76.99 ? 2116 TYR B CA 1 ATOM 6455 C C . TYR B 2 580 ? 5.383 -0.548 39.372 1.00 80.59 ? 2116 TYR B C 1 ATOM 6456 O O . TYR B 2 580 ? 4.250 -0.476 39.861 1.00 82.29 ? 2116 TYR B O 1 ATOM 6457 C CB . TYR B 2 580 ? 5.635 0.861 37.332 1.00 74.02 ? 2116 TYR B CB 1 ATOM 6458 C CG . TYR B 2 580 ? 4.295 1.557 37.271 1.00 72.03 ? 2116 TYR B CG 1 ATOM 6459 C CD1 . TYR B 2 580 ? 3.335 1.178 36.337 1.00 72.46 ? 2116 TYR B CD1 1 ATOM 6460 C CD2 . TYR B 2 580 ? 4.006 2.628 38.110 1.00 71.37 ? 2116 TYR B CD2 1 ATOM 6461 C CE1 . TYR B 2 580 ? 2.120 1.854 36.231 1.00 71.89 ? 2116 TYR B CE1 1 ATOM 6462 C CE2 . TYR B 2 580 ? 2.794 3.313 38.014 1.00 71.15 ? 2116 TYR B CE2 1 ATOM 6463 C CZ . TYR B 2 580 ? 1.857 2.922 37.069 1.00 71.50 ? 2116 TYR B CZ 1 ATOM 6464 O OH . TYR B 2 580 ? 0.669 3.606 36.944 1.00 70.65 ? 2116 TYR B OH 1 ATOM 6465 N N . SER B 2 581 ? 6.490 -0.604 40.105 1.00 83.03 ? 2117 SER B N 1 ATOM 6466 C CA . SER B 2 581 ? 6.463 -0.600 41.562 1.00 84.71 ? 2117 SER B CA 1 ATOM 6467 C C . SER B 2 581 ? 7.424 0.448 42.099 1.00 85.59 ? 2117 SER B C 1 ATOM 6468 O O . SER B 2 581 ? 8.407 0.782 41.442 1.00 85.91 ? 2117 SER B O 1 ATOM 6469 C CB . SER B 2 581 ? 6.864 -1.980 42.088 1.00 85.98 ? 2117 SER B CB 1 ATOM 6470 O OG . SER B 2 581 ? 7.153 -1.940 43.476 1.00 87.51 ? 2117 SER B OG 1 ATOM 6471 N N . ASP B 2 582 ? 7.141 0.961 43.293 1.00 87.21 ? 2118 ASP B N 1 ATOM 6472 C CA . ASP B 2 582 ? 7.992 1.971 43.920 1.00 89.01 ? 2118 ASP B CA 1 ATOM 6473 C C . ASP B 2 582 ? 8.882 1.366 44.997 1.00 89.55 ? 2118 ASP B C 1 ATOM 6474 O O . ASP B 2 582 ? 10.066 1.688 45.097 1.00 89.13 ? 2118 ASP B O 1 ATOM 6475 C CB . ASP B 2 582 ? 7.141 3.077 44.549 1.00 91.37 ? 2118 ASP B CB 1 ATOM 6476 C CG . ASP B 2 582 ? 6.375 3.891 43.519 1.00 92.88 ? 2118 ASP B CG 1 ATOM 6477 O OD1 . ASP B 2 582 ? 5.593 3.297 42.744 1.00 94.84 ? 2118 ASP B OD1 1 ATOM 6478 O OD2 . ASP B 2 582 ? 6.554 5.129 43.493 1.00 92.79 ? 2118 ASP B OD2 1 ATOM 6479 N N . GLN B 2 583 ? 8.303 0.488 45.807 1.00 91.37 ? 2119 GLN B N 1 ATOM 6480 C CA . GLN B 2 583 ? 9.042 -0.149 46.889 1.00 92.83 ? 2119 GLN B CA 1 ATOM 6481 C C . GLN B 2 583 ? 9.583 -1.534 46.513 1.00 93.74 ? 2119 GLN B C 1 ATOM 6482 O O . GLN B 2 583 ? 10.632 -1.946 47.007 1.00 93.53 ? 2119 GLN B O 1 ATOM 6483 C CB . GLN B 2 583 ? 8.153 -0.257 48.133 1.00 92.60 ? 2119 GLN B CB 1 ATOM 6484 C CG . GLN B 2 583 ? 7.605 1.073 48.662 1.00 91.23 ? 2119 GLN B CG 1 ATOM 6485 C CD . GLN B 2 583 ? 8.694 2.054 49.057 1.00 90.85 ? 2119 GLN B CD 1 ATOM 6486 O OE1 . GLN B 2 583 ? 9.849 1.672 49.251 1.00 90.31 ? 2119 GLN B OE1 1 ATOM 6487 N NE2 . GLN B 2 583 ? 8.326 3.325 49.194 1.00 90.20 ? 2119 GLN B NE2 1 ATOM 6488 N N . GLY B 2 584 ? 8.872 -2.247 45.643 1.00 94.78 ? 2120 GLY B N 1 ATOM 6489 C CA . GLY B 2 584 ? 9.318 -3.570 45.232 1.00 97.02 ? 2120 GLY B CA 1 ATOM 6490 C C . GLY B 2 584 ? 8.171 -4.496 44.860 1.00 99.11 ? 2120 GLY B C 1 ATOM 6491 O O . GLY B 2 584 ? 8.070 -4.952 43.718 1.00 99.57 ? 2120 GLY B O 1 ATOM 6492 N N . THR B 2 585 ? 7.310 -4.780 45.834 1.00 100.36 ? 2121 THR B N 1 ATOM 6493 C CA . THR B 2 585 ? 6.145 -5.637 45.633 1.00 99.71 ? 2121 THR B CA 1 ATOM 6494 C C . THR B 2 585 ? 4.936 -4.774 45.265 1.00 99.49 ? 2121 THR B C 1 ATOM 6495 O O . THR B 2 585 ? 5.014 -3.546 45.291 1.00 98.83 ? 2121 THR B O 1 ATOM 6496 C CB . THR B 2 585 ? 5.828 -6.429 46.911 1.00 100.27 ? 2121 THR B CB 1 ATOM 6497 O OG1 . THR B 2 585 ? 4.588 -7.125 46.746 1.00 100.17 ? 2121 THR B OG1 1 ATOM 6498 C CG2 . THR B 2 585 ? 5.736 -5.489 48.112 1.00 100.37 ? 2121 THR B CG2 1 ATOM 6499 N N . ASP B 2 586 ? 3.820 -5.413 44.930 1.00 99.91 ? 2122 ASP B N 1 ATOM 6500 C CA . ASP B 2 586 ? 2.604 -4.693 44.546 1.00 100.45 ? 2122 ASP B CA 1 ATOM 6501 C C . ASP B 2 586 ? 2.817 -4.006 43.200 1.00 98.71 ? 2122 ASP B C 1 ATOM 6502 O O . ASP B 2 586 ? 3.672 -3.131 43.069 1.00 98.65 ? 2122 ASP B O 1 ATOM 6503 C CB . ASP B 2 586 ? 2.229 -3.643 45.602 1.00 103.79 ? 2122 ASP B CB 1 ATOM 6504 C CG . ASP B 2 586 ? 1.823 -4.263 46.936 1.00 106.58 ? 2122 ASP B CG 1 ATOM 6505 O OD1 . ASP B 2 586 ? 2.677 -4.902 47.596 1.00 107.25 ? 2122 ASP B OD1 1 ATOM 6506 O OD2 . ASP B 2 586 ? 0.642 -4.105 47.324 1.00 107.85 ? 2122 ASP B OD2 1 ATOM 6507 N N . TRP B 2 587 ? 2.030 -4.402 42.205 1.00 96.45 ? 2123 TRP B N 1 ATOM 6508 C CA . TRP B 2 587 ? 2.159 -3.838 40.869 1.00 94.00 ? 2123 TRP B CA 1 ATOM 6509 C C . TRP B 2 587 ? 0.864 -3.228 40.337 1.00 92.91 ? 2123 TRP B C 1 ATOM 6510 O O . TRP B 2 587 ? -0.230 -3.700 40.637 1.00 93.22 ? 2123 TRP B O 1 ATOM 6511 C CB . TRP B 2 587 ? 2.662 -4.918 39.912 1.00 92.06 ? 2123 TRP B CB 1 ATOM 6512 C CG . TRP B 2 587 ? 3.870 -5.631 40.430 1.00 90.12 ? 2123 TRP B CG 1 ATOM 6513 C CD1 . TRP B 2 587 ? 3.895 -6.611 41.372 1.00 89.78 ? 2123 TRP B CD1 1 ATOM 6514 C CD2 . TRP B 2 587 ? 5.236 -5.397 40.057 1.00 89.98 ? 2123 TRP B CD2 1 ATOM 6515 N NE1 . TRP B 2 587 ? 5.190 -7.006 41.612 1.00 89.85 ? 2123 TRP B NE1 1 ATOM 6516 C CE2 . TRP B 2 587 ? 6.033 -6.276 40.818 1.00 89.18 ? 2123 TRP B CE2 1 ATOM 6517 C CE3 . TRP B 2 587 ? 5.864 -4.528 39.153 1.00 89.37 ? 2123 TRP B CE3 1 ATOM 6518 C CZ2 . TRP B 2 587 ? 7.425 -6.314 40.704 1.00 88.46 ? 2123 TRP B CZ2 1 ATOM 6519 C CZ3 . TRP B 2 587 ? 7.249 -4.567 39.041 1.00 87.96 ? 2123 TRP B CZ3 1 ATOM 6520 C CH2 . TRP B 2 587 ? 8.013 -5.453 39.813 1.00 88.52 ? 2123 TRP B CH2 1 ATOM 6521 N N . LYS B 2 588 ? 0.998 -2.165 39.550 1.00 91.68 ? 2124 LYS B N 1 ATOM 6522 C CA . LYS B 2 588 ? -0.155 -1.488 38.972 1.00 90.96 ? 2124 LYS B CA 1 ATOM 6523 C C . LYS B 2 588 ? -0.043 -1.520 37.453 1.00 90.40 ? 2124 LYS B C 1 ATOM 6524 O O . LYS B 2 588 ? 0.697 -0.740 36.855 1.00 89.67 ? 2124 LYS B O 1 ATOM 6525 C CB . LYS B 2 588 ? -0.218 -0.035 39.454 1.00 90.80 ? 2124 LYS B CB 1 ATOM 6526 C CG . LYS B 2 588 ? -1.426 0.749 38.940 1.00 91.05 ? 2124 LYS B CG 1 ATOM 6527 C CD . LYS B 2 588 ? -1.277 2.243 39.227 1.00 90.42 ? 2124 LYS B CD 1 ATOM 6528 C CE . LYS B 2 588 ? -2.507 3.045 38.806 1.00 89.64 ? 2124 LYS B CE 1 ATOM 6529 N NZ . LYS B 2 588 ? -2.769 3.000 37.346 1.00 88.47 ? 2124 LYS B NZ 1 ATOM 6530 N N . PRO B 2 589 ? -0.774 -2.437 36.809 1.00 90.22 ? 2125 PRO B N 1 ATOM 6531 C CA . PRO B 2 589 ? -0.744 -2.558 35.350 1.00 89.94 ? 2125 PRO B CA 1 ATOM 6532 C C . PRO B 2 589 ? -0.992 -1.217 34.666 1.00 89.56 ? 2125 PRO B C 1 ATOM 6533 O O . PRO B 2 589 ? -2.020 -0.582 34.891 1.00 90.51 ? 2125 PRO B O 1 ATOM 6534 C CB . PRO B 2 589 ? -1.859 -3.560 35.066 1.00 90.09 ? 2125 PRO B CB 1 ATOM 6535 C CG . PRO B 2 589 ? -1.828 -4.439 36.277 1.00 90.78 ? 2125 PRO B CG 1 ATOM 6536 C CD . PRO B 2 589 ? -1.678 -3.438 37.402 1.00 90.26 ? 2125 PRO B CD 1 ATOM 6537 N N . TYR B 2 590 ? -0.047 -0.791 33.836 1.00 88.73 ? 2126 TYR B N 1 ATOM 6538 C CA . TYR B 2 590 ? -0.177 0.471 33.119 1.00 87.88 ? 2126 TYR B CA 1 ATOM 6539 C C . TYR B 2 590 ? -1.454 0.440 32.287 1.00 89.36 ? 2126 TYR B C 1 ATOM 6540 O O . TYR B 2 590 ? -1.621 -0.432 31.440 1.00 88.54 ? 2126 TYR B O 1 ATOM 6541 C CB . TYR B 2 590 ? 1.026 0.685 32.194 1.00 84.74 ? 2126 TYR B CB 1 ATOM 6542 C CG . TYR B 2 590 ? 1.064 2.058 31.549 1.00 80.23 ? 2126 TYR B CG 1 ATOM 6543 C CD1 . TYR B 2 590 ? 1.600 3.154 32.226 1.00 77.05 ? 2126 TYR B CD1 1 ATOM 6544 C CD2 . TYR B 2 590 ? 0.532 2.265 30.276 1.00 77.55 ? 2126 TYR B CD2 1 ATOM 6545 C CE1 . TYR B 2 590 ? 1.605 4.412 31.653 1.00 74.50 ? 2126 TYR B CE1 1 ATOM 6546 C CE2 . TYR B 2 590 ? 0.530 3.519 29.697 1.00 75.02 ? 2126 TYR B CE2 1 ATOM 6547 C CZ . TYR B 2 590 ? 1.069 4.586 30.390 1.00 74.65 ? 2126 TYR B CZ 1 ATOM 6548 O OH . TYR B 2 590 ? 1.089 5.825 29.806 1.00 76.06 ? 2126 TYR B OH 1 ATOM 6549 N N . ARG B 2 591 ? -2.349 1.392 32.532 1.00 92.26 ? 2127 ARG B N 1 ATOM 6550 C CA . ARG B 2 591 ? -3.610 1.462 31.801 1.00 96.53 ? 2127 ARG B CA 1 ATOM 6551 C C . ARG B 2 591 ? -3.762 2.816 31.114 1.00 98.84 ? 2127 ARG B C 1 ATOM 6552 O O . ARG B 2 591 ? -3.131 3.796 31.509 1.00 99.19 ? 2127 ARG B O 1 ATOM 6553 C CB . ARG B 2 591 ? -4.781 1.232 32.758 1.00 98.35 ? 2127 ARG B CB 1 ATOM 6554 C CG . ARG B 2 591 ? -4.712 -0.081 33.524 1.00 101.51 ? 2127 ARG B CG 1 ATOM 6555 C CD . ARG B 2 591 ? -5.852 -0.201 34.532 1.00 105.48 ? 2127 ARG B CD 1 ATOM 6556 N NE . ARG B 2 591 ? -5.814 0.840 35.560 1.00 107.61 ? 2127 ARG B NE 1 ATOM 6557 C CZ . ARG B 2 591 ? -6.699 0.948 36.548 1.00 108.93 ? 2127 ARG B CZ 1 ATOM 6558 N NH1 . ARG B 2 591 ? -7.698 0.079 36.648 1.00 108.69 ? 2127 ARG B NH1 1 ATOM 6559 N NH2 . ARG B 2 591 ? -6.584 1.925 37.440 1.00 109.28 ? 2127 ARG B NH2 1 ATOM 6560 N N . GLU B 2 592 ? -4.607 2.867 30.089 1.00 101.47 ? 2128 GLU B N 1 ATOM 6561 C CA . GLU B 2 592 ? -4.829 4.100 29.341 1.00 104.26 ? 2128 GLU B CA 1 ATOM 6562 C C . GLU B 2 592 ? -5.495 5.198 30.171 1.00 106.21 ? 2128 GLU B C 1 ATOM 6563 O O . GLU B 2 592 ? -5.920 4.973 31.309 1.00 105.50 ? 2128 GLU B O 1 ATOM 6564 C CB . GLU B 2 592 ? -5.677 3.816 28.098 1.00 105.04 ? 2128 GLU B CB 1 ATOM 6565 C CG . GLU B 2 592 ? -4.985 4.098 26.764 1.00 106.39 ? 2128 GLU B CG 1 ATOM 6566 C CD . GLU B 2 592 ? -4.712 5.578 26.525 1.00 106.98 ? 2128 GLU B CD 1 ATOM 6567 O OE1 . GLU B 2 592 ? -5.651 6.392 26.675 1.00 106.71 ? 2128 GLU B OE1 1 ATOM 6568 O OE2 . GLU B 2 592 ? -3.562 5.928 26.176 1.00 106.72 ? 2128 GLU B OE2 1 ATOM 6569 N N . LYS B 2 593 ? -5.578 6.386 29.572 1.00 108.57 ? 2129 LYS B N 1 ATOM 6570 C CA . LYS B 2 593 ? -6.178 7.567 30.190 1.00 109.75 ? 2129 LYS B CA 1 ATOM 6571 C C . LYS B 2 593 ? -7.532 7.243 30.814 1.00 110.44 ? 2129 LYS B C 1 ATOM 6572 O O . LYS B 2 593 ? -7.993 7.947 31.715 1.00 110.33 ? 2129 LYS B O 1 ATOM 6573 C CB . LYS B 2 593 ? -6.361 8.667 29.135 1.00 110.02 ? 2129 LYS B CB 1 ATOM 6574 C CG . LYS B 2 593 ? -5.124 8.933 28.291 1.00 109.95 ? 2129 LYS B CG 1 ATOM 6575 C CD . LYS B 2 593 ? -4.047 9.660 29.077 1.00 111.29 ? 2129 LYS B CD 1 ATOM 6576 C CE . LYS B 2 593 ? -4.343 11.146 29.162 1.00 111.63 ? 2129 LYS B CE 1 ATOM 6577 N NZ . LYS B 2 593 ? -4.379 11.766 27.801 1.00 111.67 ? 2129 LYS B NZ 1 ATOM 6578 N N . SER B 2 594 ? -8.166 6.177 30.330 1.00 111.12 ? 2130 SER B N 1 ATOM 6579 C CA . SER B 2 594 ? -9.470 5.771 30.839 1.00 112.02 ? 2130 SER B CA 1 ATOM 6580 C C . SER B 2 594 ? -9.803 4.304 30.526 1.00 112.86 ? 2130 SER B C 1 ATOM 6581 O O . SER B 2 594 ? -10.213 3.975 29.408 1.00 113.57 ? 2130 SER B O 1 ATOM 6582 C CB . SER B 2 594 ? -10.551 6.682 30.248 1.00 111.84 ? 2130 SER B CB 1 ATOM 6583 O OG . SER B 2 594 ? -10.211 8.052 30.398 1.00 110.47 ? 2130 SER B OG 1 ATOM 6584 N N . SER B 2 595 ? -9.622 3.430 31.516 1.00 112.87 ? 2131 SER B N 1 ATOM 6585 C CA . SER B 2 595 ? -9.915 2.001 31.366 1.00 112.51 ? 2131 SER B CA 1 ATOM 6586 C C . SER B 2 595 ? -9.592 1.220 32.643 1.00 112.17 ? 2131 SER B C 1 ATOM 6587 O O . SER B 2 595 ? -9.122 1.788 33.633 1.00 111.82 ? 2131 SER B O 1 ATOM 6588 C CB . SER B 2 595 ? -9.127 1.401 30.193 1.00 112.57 ? 2131 SER B CB 1 ATOM 6589 O OG . SER B 2 595 ? -7.739 1.338 30.473 1.00 112.98 ? 2131 SER B OG 1 ATOM 6590 N N . MET B 2 596 ? -9.863 -0.084 32.614 1.00 111.58 ? 2132 MET B N 1 ATOM 6591 C CA . MET B 2 596 ? -9.596 -0.960 33.755 1.00 110.68 ? 2132 MET B CA 1 ATOM 6592 C C . MET B 2 596 ? -8.753 -2.147 33.296 1.00 109.00 ? 2132 MET B C 1 ATOM 6593 O O . MET B 2 596 ? -8.150 -2.851 34.112 1.00 108.73 ? 2132 MET B O 1 ATOM 6594 C CB . MET B 2 596 ? -10.906 -1.466 34.380 1.00 111.61 ? 2132 MET B CB 1 ATOM 6595 C CG . MET B 2 596 ? -11.735 -2.380 33.485 1.00 112.43 ? 2132 MET B CG 1 ATOM 6596 S SD . MET B 2 596 ? -12.499 -1.538 32.080 1.00 112.85 ? 2132 MET B SD 1 ATOM 6597 C CE . MET B 2 596 ? -14.226 -1.460 32.627 1.00 112.53 ? 2132 MET B CE 1 ATOM 6598 N N . VAL B 2 597 ? -8.722 -2.365 31.984 1.00 106.38 ? 2133 VAL B N 1 ATOM 6599 C CA . VAL B 2 597 ? -7.944 -3.451 31.408 1.00 103.38 ? 2133 VAL B CA 1 ATOM 6600 C C . VAL B 2 597 ? -6.503 -2.979 31.285 1.00 101.22 ? 2133 VAL B C 1 ATOM 6601 O O . VAL B 2 597 ? -6.243 -1.779 31.194 1.00 101.40 ? 2133 VAL B O 1 ATOM 6602 C CB . VAL B 2 597 ? -8.466 -3.845 30.004 1.00 103.38 ? 2133 VAL B CB 1 ATOM 6603 C CG1 . VAL B 2 597 ? -9.926 -4.247 30.092 1.00 104.06 ? 2133 VAL B CG1 1 ATOM 6604 C CG2 . VAL B 2 597 ? -8.293 -2.689 29.033 1.00 103.01 ? 2133 VAL B CG2 1 ATOM 6605 N N . ASP B 2 598 ? -5.571 -3.924 31.288 1.00 98.26 ? 2134 ASP B N 1 ATOM 6606 C CA . ASP B 2 598 ? -4.156 -3.599 31.176 1.00 94.50 ? 2134 ASP B CA 1 ATOM 6607 C C . ASP B 2 598 ? -3.825 -3.120 29.766 1.00 91.66 ? 2134 ASP B C 1 ATOM 6608 O O . ASP B 2 598 ? -4.551 -3.411 28.810 1.00 91.18 ? 2134 ASP B O 1 ATOM 6609 C CB . ASP B 2 598 ? -3.315 -4.824 31.532 1.00 95.71 ? 2134 ASP B CB 1 ATOM 6610 C CG . ASP B 2 598 ? -3.599 -5.332 32.931 1.00 97.01 ? 2134 ASP B CG 1 ATOM 6611 O OD1 . ASP B 2 598 ? -3.134 -6.438 33.268 1.00 97.87 ? 2134 ASP B OD1 1 ATOM 6612 O OD2 . ASP B 2 598 ? -4.288 -4.624 33.697 1.00 97.92 ? 2134 ASP B OD2 1 ATOM 6613 N N . LYS B 2 599 ? -2.723 -2.385 29.650 1.00 88.18 ? 2135 LYS B N 1 ATOM 6614 C CA . LYS B 2 599 ? -2.278 -1.834 28.376 1.00 83.86 ? 2135 LYS B CA 1 ATOM 6615 C C . LYS B 2 599 ? -1.513 -2.846 27.535 1.00 81.75 ? 2135 LYS B C 1 ATOM 6616 O O . LYS B 2 599 ? -0.585 -3.504 28.014 1.00 79.52 ? 2135 LYS B O 1 ATOM 6617 C CB . LYS B 2 599 ? -1.397 -0.607 28.629 1.00 83.18 ? 2135 LYS B CB 1 ATOM 6618 C CG . LYS B 2 599 ? -0.854 0.073 27.388 1.00 80.91 ? 2135 LYS B CG 1 ATOM 6619 C CD . LYS B 2 599 ? -1.945 0.746 26.593 1.00 81.53 ? 2135 LYS B CD 1 ATOM 6620 C CE . LYS B 2 599 ? -1.370 1.423 25.357 1.00 81.69 ? 2135 LYS B CE 1 ATOM 6621 N NZ . LYS B 2 599 ? -2.419 2.084 24.533 1.00 81.65 ? 2135 LYS B NZ 1 ATOM 6622 N N . ILE B 2 600 ? -1.920 -2.961 26.275 1.00 79.15 ? 2136 ILE B N 1 ATOM 6623 C CA . ILE B 2 600 ? -1.281 -3.867 25.338 1.00 78.11 ? 2136 ILE B CA 1 ATOM 6624 C C . ILE B 2 600 ? -0.442 -3.068 24.348 1.00 76.60 ? 2136 ILE B C 1 ATOM 6625 O O . ILE B 2 600 ? -0.968 -2.464 23.416 1.00 75.97 ? 2136 ILE B O 1 ATOM 6626 C CB . ILE B 2 600 ? -2.323 -4.698 24.559 1.00 79.21 ? 2136 ILE B CB 1 ATOM 6627 C CG1 . ILE B 2 600 ? -3.006 -5.686 25.505 1.00 78.72 ? 2136 ILE B CG1 1 ATOM 6628 C CG2 . ILE B 2 600 ? -1.651 -5.441 23.400 1.00 78.89 ? 2136 ILE B CG2 1 ATOM 6629 C CD1 . ILE B 2 600 ? -4.011 -6.589 24.822 1.00 79.85 ? 2136 ILE B CD1 1 ATOM 6630 N N . PHE B 2 601 ? 0.868 -3.070 24.564 1.00 75.67 ? 2137 PHE B N 1 ATOM 6631 C CA . PHE B 2 601 ? 1.803 -2.353 23.705 1.00 74.46 ? 2137 PHE B CA 1 ATOM 6632 C C . PHE B 2 601 ? 2.250 -3.244 22.559 1.00 74.36 ? 2137 PHE B C 1 ATOM 6633 O O . PHE B 2 601 ? 2.721 -4.355 22.794 1.00 74.41 ? 2137 PHE B O 1 ATOM 6634 C CB . PHE B 2 601 ? 3.044 -1.946 24.496 1.00 73.30 ? 2137 PHE B CB 1 ATOM 6635 C CG . PHE B 2 601 ? 2.793 -0.898 25.543 1.00 73.01 ? 2137 PHE B CG 1 ATOM 6636 C CD1 . PHE B 2 601 ? 3.072 -1.157 26.884 1.00 71.27 ? 2137 PHE B CD1 1 ATOM 6637 C CD2 . PHE B 2 601 ? 2.341 0.371 25.186 1.00 73.37 ? 2137 PHE B CD2 1 ATOM 6638 C CE1 . PHE B 2 601 ? 2.909 -0.167 27.848 1.00 72.73 ? 2137 PHE B CE1 1 ATOM 6639 C CE2 . PHE B 2 601 ? 2.175 1.372 26.154 1.00 72.89 ? 2137 PHE B CE2 1 ATOM 6640 C CZ . PHE B 2 601 ? 2.461 1.102 27.483 1.00 72.27 ? 2137 PHE B CZ 1 ATOM 6641 N N . GLU B 2 602 ? 2.109 -2.767 21.324 1.00 74.98 ? 2138 GLU B N 1 ATOM 6642 C CA . GLU B 2 602 ? 2.546 -3.555 20.175 1.00 75.66 ? 2138 GLU B CA 1 ATOM 6643 C C . GLU B 2 602 ? 4.067 -3.588 20.154 1.00 74.51 ? 2138 GLU B C 1 ATOM 6644 O O . GLU B 2 602 ? 4.720 -2.547 20.205 1.00 74.62 ? 2138 GLU B O 1 ATOM 6645 C CB . GLU B 2 602 ? 2.057 -2.957 18.853 1.00 79.10 ? 2138 GLU B CB 1 ATOM 6646 C CG . GLU B 2 602 ? 0.576 -3.126 18.558 1.00 84.38 ? 2138 GLU B CG 1 ATOM 6647 C CD . GLU B 2 602 ? 0.273 -3.096 17.055 1.00 88.11 ? 2138 GLU B CD 1 ATOM 6648 O OE1 . GLU B 2 602 ? -0.908 -2.900 16.684 1.00 89.83 ? 2138 GLU B OE1 1 ATOM 6649 O OE2 . GLU B 2 602 ? 1.215 -3.280 16.247 1.00 88.73 ? 2138 GLU B OE2 1 ATOM 6650 N N . GLY B 2 603 ? 4.624 -4.791 20.080 1.00 73.18 ? 2139 GLY B N 1 ATOM 6651 C CA . GLY B 2 603 ? 6.067 -4.946 20.051 1.00 70.73 ? 2139 GLY B CA 1 ATOM 6652 C C . GLY B 2 603 ? 6.593 -5.070 18.636 1.00 68.45 ? 2139 GLY B C 1 ATOM 6653 O O . GLY B 2 603 ? 5.995 -4.536 17.697 1.00 68.06 ? 2139 GLY B O 1 ATOM 6654 N N . ASN B 2 604 ? 7.700 -5.786 18.472 1.00 65.93 ? 2140 ASN B N 1 ATOM 6655 C CA . ASN B 2 604 ? 8.295 -5.936 17.154 1.00 64.50 ? 2140 ASN B CA 1 ATOM 6656 C C . ASN B 2 604 ? 7.700 -7.038 16.306 1.00 62.51 ? 2140 ASN B C 1 ATOM 6657 O O . ASN B 2 604 ? 7.042 -7.945 16.804 1.00 63.61 ? 2140 ASN B O 1 ATOM 6658 C CB . ASN B 2 604 ? 9.805 -6.145 17.269 1.00 65.39 ? 2140 ASN B CB 1 ATOM 6659 C CG . ASN B 2 604 ? 10.218 -6.597 18.633 1.00 65.31 ? 2140 ASN B CG 1 ATOM 6660 O OD1 . ASN B 2 604 ? 9.553 -7.428 19.246 1.00 66.77 ? 2140 ASN B OD1 1 ATOM 6661 N ND2 . ASN B 2 604 ? 11.327 -6.060 19.123 1.00 65.17 ? 2140 ASN B ND2 1 ATOM 6662 N N . ASN B 2 605 ? 7.948 -6.938 15.009 1.00 59.68 ? 2141 ASN B N 1 ATOM 6663 C CA . ASN B 2 605 ? 7.454 -7.901 14.053 1.00 58.50 ? 2141 ASN B CA 1 ATOM 6664 C C . ASN B 2 605 ? 8.609 -8.575 13.315 1.00 56.32 ? 2141 ASN B C 1 ATOM 6665 O O . ASN B 2 605 ? 8.422 -9.134 12.234 1.00 56.66 ? 2141 ASN B O 1 ATOM 6666 C CB . ASN B 2 605 ? 6.513 -7.206 13.060 1.00 60.85 ? 2141 ASN B CB 1 ATOM 6667 C CG . ASN B 2 605 ? 6.995 -5.818 12.672 1.00 63.42 ? 2141 ASN B CG 1 ATOM 6668 O OD1 . ASN B 2 605 ? 6.433 -4.809 13.110 1.00 65.88 ? 2141 ASN B OD1 1 ATOM 6669 N ND2 . ASN B 2 605 ? 8.049 -5.757 11.859 1.00 62.72 ? 2141 ASN B ND2 1 ATOM 6670 N N . ASN B 2 606 ? 9.804 -8.509 13.898 1.00 54.13 ? 2142 ASN B N 1 ATOM 6671 C CA . ASN B 2 606 ? 10.989 -9.139 13.311 1.00 50.60 ? 2142 ASN B CA 1 ATOM 6672 C C . ASN B 2 606 ? 12.105 -9.289 14.328 1.00 49.79 ? 2142 ASN B C 1 ATOM 6673 O O . ASN B 2 606 ? 12.062 -8.704 15.409 1.00 48.84 ? 2142 ASN B O 1 ATOM 6674 C CB . ASN B 2 606 ? 11.506 -8.352 12.110 1.00 49.24 ? 2142 ASN B CB 1 ATOM 6675 C CG . ASN B 2 606 ? 11.826 -6.912 12.450 1.00 51.27 ? 2142 ASN B CG 1 ATOM 6676 O OD1 . ASN B 2 606 ? 12.257 -6.591 13.569 1.00 51.72 ? 2142 ASN B OD1 1 ATOM 6677 N ND2 . ASN B 2 606 ? 11.628 -6.031 11.480 1.00 50.74 ? 2142 ASN B ND2 1 ATOM 6678 N N . VAL B 2 607 ? 13.121 -10.050 13.942 1.00 51.11 ? 2143 VAL B N 1 ATOM 6679 C CA . VAL B 2 607 ? 14.274 -10.360 14.785 1.00 53.80 ? 2143 VAL B CA 1 ATOM 6680 C C . VAL B 2 607 ? 15.230 -9.241 15.207 1.00 55.17 ? 2143 VAL B C 1 ATOM 6681 O O . VAL B 2 607 ? 15.635 -9.180 16.371 1.00 56.37 ? 2143 VAL B O 1 ATOM 6682 C CB . VAL B 2 607 ? 15.133 -11.477 14.129 1.00 55.55 ? 2143 VAL B CB 1 ATOM 6683 C CG1 . VAL B 2 607 ? 15.145 -12.719 15.006 1.00 54.11 ? 2143 VAL B CG1 1 ATOM 6684 C CG2 . VAL B 2 607 ? 14.582 -11.813 12.747 1.00 55.54 ? 2143 VAL B CG2 1 ATOM 6685 N N . ARG B 2 608 ? 15.609 -8.369 14.278 1.00 56.77 ? 2144 ARG B N 1 ATOM 6686 C CA . ARG B 2 608 ? 16.555 -7.297 14.600 1.00 57.37 ? 2144 ARG B CA 1 ATOM 6687 C C . ARG B 2 608 ? 15.961 -5.893 14.791 1.00 55.57 ? 2144 ARG B C 1 ATOM 6688 O O . ARG B 2 608 ? 16.495 -5.082 15.546 1.00 54.13 ? 2144 ARG B O 1 ATOM 6689 C CB . ARG B 2 608 ? 17.637 -7.243 13.520 1.00 59.64 ? 2144 ARG B CB 1 ATOM 6690 C CG . ARG B 2 608 ? 18.239 -8.607 13.177 1.00 65.30 ? 2144 ARG B CG 1 ATOM 6691 C CD . ARG B 2 608 ? 19.438 -8.463 12.236 1.00 69.08 ? 2144 ARG B CD 1 ATOM 6692 N NE . ARG B 2 608 ? 19.960 -9.745 11.760 1.00 70.51 ? 2144 ARG B NE 1 ATOM 6693 C CZ . ARG B 2 608 ? 19.321 -10.547 10.912 1.00 71.91 ? 2144 ARG B CZ 1 ATOM 6694 N NH1 . ARG B 2 608 ? 18.124 -10.213 10.440 1.00 71.28 ? 2144 ARG B NH1 1 ATOM 6695 N NH2 . ARG B 2 608 ? 19.888 -11.675 10.516 1.00 71.96 ? 2144 ARG B NH2 1 ATOM 6696 N N . GLY B 2 609 ? 14.853 -5.615 14.115 1.00 53.71 ? 2145 GLY B N 1 ATOM 6697 C CA . GLY B 2 609 ? 14.246 -4.302 14.209 1.00 52.36 ? 2145 GLY B CA 1 ATOM 6698 C C . GLY B 2 609 ? 13.859 -3.800 15.584 1.00 52.37 ? 2145 GLY B C 1 ATOM 6699 O O . GLY B 2 609 ? 13.540 -4.581 16.487 1.00 55.41 ? 2145 GLY B O 1 ATOM 6700 N N . HIS B 2 610 ? 13.881 -2.478 15.733 1.00 49.36 ? 2146 HIS B N 1 ATOM 6701 C CA . HIS B 2 610 ? 13.516 -1.825 16.987 1.00 46.09 ? 2146 HIS B CA 1 ATOM 6702 C C . HIS B 2 610 ? 12.078 -1.359 16.878 1.00 44.56 ? 2146 HIS B C 1 ATOM 6703 O O . HIS B 2 610 ? 11.581 -1.124 15.782 1.00 46.44 ? 2146 HIS B O 1 ATOM 6704 C CB . HIS B 2 610 ? 14.375 -0.580 17.225 1.00 47.23 ? 2146 HIS B CB 1 ATOM 6705 C CG . HIS B 2 610 ? 15.752 -0.857 17.740 1.00 46.76 ? 2146 HIS B CG 1 ATOM 6706 N ND1 . HIS B 2 610 ? 16.461 -1.993 17.418 1.00 45.29 ? 2146 HIS B ND1 1 ATOM 6707 C CD2 . HIS B 2 610 ? 16.580 -0.100 18.498 1.00 46.15 ? 2146 HIS B CD2 1 ATOM 6708 C CE1 . HIS B 2 610 ? 17.667 -1.924 17.951 1.00 45.54 ? 2146 HIS B CE1 1 ATOM 6709 N NE2 . HIS B 2 610 ? 17.764 -0.784 18.611 1.00 46.56 ? 2146 HIS B NE2 1 ATOM 6710 N N . VAL B 2 611 ? 11.411 -1.235 18.017 1.00 43.04 ? 2147 VAL B N 1 ATOM 6711 C CA . VAL B 2 611 ? 10.051 -0.729 18.062 1.00 43.30 ? 2147 VAL B CA 1 ATOM 6712 C C . VAL B 2 611 ? 9.951 0.089 19.339 1.00 45.39 ? 2147 VAL B C 1 ATOM 6713 O O . VAL B 2 611 ? 10.281 -0.389 20.434 1.00 45.88 ? 2147 VAL B O 1 ATOM 6714 C CB . VAL B 2 611 ? 9.002 -1.847 18.051 1.00 43.45 ? 2147 VAL B CB 1 ATOM 6715 C CG1 . VAL B 2 611 ? 7.641 -1.298 18.478 1.00 40.72 ? 2147 VAL B CG1 1 ATOM 6716 C CG2 . VAL B 2 611 ? 8.884 -2.412 16.645 1.00 43.63 ? 2147 VAL B CG2 1 ATOM 6717 N N . LYS B 2 612 ? 9.521 1.336 19.182 1.00 46.11 ? 2148 LYS B N 1 ATOM 6718 C CA . LYS B 2 612 ? 9.417 2.261 20.304 1.00 47.47 ? 2148 LYS B CA 1 ATOM 6719 C C . LYS B 2 612 ? 7.991 2.524 20.762 1.00 48.71 ? 2148 LYS B C 1 ATOM 6720 O O . LYS B 2 612 ? 7.067 2.732 19.956 1.00 45.96 ? 2148 LYS B O 1 ATOM 6721 C CB . LYS B 2 612 ? 10.085 3.605 19.951 1.00 43.81 ? 2148 LYS B CB 1 ATOM 6722 C CG . LYS B 2 612 ? 10.664 4.372 21.141 1.00 41.14 ? 2148 LYS B CG 1 ATOM 6723 C CD . LYS B 2 612 ? 11.087 5.785 20.730 1.00 43.17 ? 2148 LYS B CD 1 ATOM 6724 C CE . LYS B 2 612 ? 11.866 6.539 21.805 1.00 38.66 ? 2148 LYS B CE 1 ATOM 6725 N NZ . LYS B 2 612 ? 13.324 6.263 21.744 1.00 38.84 ? 2148 LYS B NZ 1 ATOM 6726 N N . ASN B 2 613 ? 7.829 2.509 22.080 1.00 50.78 ? 2149 ASN B N 1 ATOM 6727 C CA . ASN B 2 613 ? 6.543 2.792 22.681 1.00 53.23 ? 2149 ASN B CA 1 ATOM 6728 C C . ASN B 2 613 ? 6.744 3.904 23.694 1.00 54.05 ? 2149 ASN B C 1 ATOM 6729 O O . ASN B 2 613 ? 7.729 3.916 24.440 1.00 52.64 ? 2149 ASN B O 1 ATOM 6730 C CB . ASN B 2 613 ? 5.943 1.533 23.323 1.00 53.35 ? 2149 ASN B CB 1 ATOM 6731 C CG . ASN B 2 613 ? 5.295 0.622 22.295 1.00 54.11 ? 2149 ASN B CG 1 ATOM 6732 O OD1 . ASN B 2 613 ? 4.428 1.057 21.532 1.00 56.89 ? 2149 ASN B OD1 1 ATOM 6733 N ND2 . ASN B 2 613 ? 5.713 -0.638 22.261 1.00 51.54 ? 2149 ASN B ND2 1 ATOM 6734 N N . PHE B 2 614 ? 5.825 4.864 23.666 1.00 55.42 ? 2150 PHE B N 1 ATOM 6735 C CA . PHE B 2 614 ? 5.867 6.007 24.564 1.00 58.01 ? 2150 PHE B CA 1 ATOM 6736 C C . PHE B 2 614 ? 4.757 5.875 25.594 1.00 59.89 ? 2150 PHE B C 1 ATOM 6737 O O . PHE B 2 614 ? 3.691 5.338 25.299 1.00 60.37 ? 2150 PHE B O 1 ATOM 6738 C CB . PHE B 2 614 ? 5.660 7.302 23.773 1.00 56.86 ? 2150 PHE B CB 1 ATOM 6739 C CG . PHE B 2 614 ? 6.825 7.687 22.915 1.00 55.61 ? 2150 PHE B CG 1 ATOM 6740 C CD1 . PHE B 2 614 ? 7.951 8.272 23.474 1.00 54.01 ? 2150 PHE B CD1 1 ATOM 6741 C CD2 . PHE B 2 614 ? 6.792 7.477 21.540 1.00 57.56 ? 2150 PHE B CD2 1 ATOM 6742 C CE1 . PHE B 2 614 ? 9.032 8.647 22.677 1.00 55.21 ? 2150 PHE B CE1 1 ATOM 6743 C CE2 . PHE B 2 614 ? 7.868 7.848 20.732 1.00 55.89 ? 2150 PHE B CE2 1 ATOM 6744 C CZ . PHE B 2 614 ? 8.990 8.435 21.302 1.00 54.83 ? 2150 PHE B CZ 1 ATOM 6745 N N . PHE B 2 615 ? 5.004 6.358 26.805 1.00 62.72 ? 2151 PHE B N 1 ATOM 6746 C CA . PHE B 2 615 ? 3.983 6.306 27.843 1.00 64.53 ? 2151 PHE B CA 1 ATOM 6747 C C . PHE B 2 615 ? 3.343 7.692 27.871 1.00 66.17 ? 2151 PHE B C 1 ATOM 6748 O O . PHE B 2 615 ? 3.974 8.632 28.337 1.00 64.83 ? 2151 PHE B O 1 ATOM 6749 C CB . PHE B 2 615 ? 4.620 5.995 29.208 1.00 64.56 ? 2151 PHE B CB 1 ATOM 6750 C CG . PHE B 2 615 ? 5.493 4.762 29.214 1.00 64.62 ? 2151 PHE B CG 1 ATOM 6751 C CD1 . PHE B 2 615 ? 5.002 3.536 28.770 1.00 66.01 ? 2151 PHE B CD1 1 ATOM 6752 C CD2 . PHE B 2 615 ? 6.812 4.829 29.646 1.00 64.22 ? 2151 PHE B CD2 1 ATOM 6753 C CE1 . PHE B 2 615 ? 5.813 2.403 28.752 1.00 66.74 ? 2151 PHE B CE1 1 ATOM 6754 C CE2 . PHE B 2 615 ? 7.631 3.697 29.633 1.00 63.37 ? 2151 PHE B CE2 1 ATOM 6755 C CZ . PHE B 2 615 ? 7.133 2.487 29.185 1.00 65.58 ? 2151 PHE B CZ 1 ATOM 6756 N N . ASN B 2 616 ? 2.118 7.828 27.351 1.00 69.48 ? 2152 ASN B N 1 ATOM 6757 C CA . ASN B 2 616 ? 1.428 9.128 27.346 1.00 72.28 ? 2152 ASN B CA 1 ATOM 6758 C C . ASN B 2 616 ? 1.665 9.708 28.737 1.00 71.61 ? 2152 ASN B C 1 ATOM 6759 O O . ASN B 2 616 ? 2.328 10.736 28.880 1.00 74.24 ? 2152 ASN B O 1 ATOM 6760 C CB . ASN B 2 616 ? -0.075 8.961 27.073 1.00 76.76 ? 2152 ASN B CB 1 ATOM 6761 C CG . ASN B 2 616 ? -0.364 8.282 25.740 1.00 80.98 ? 2152 ASN B CG 1 ATOM 6762 O OD1 . ASN B 2 616 ? -0.067 8.824 24.667 1.00 82.08 ? 2152 ASN B OD1 1 ATOM 6763 N ND2 . ASN B 2 616 ? -0.951 7.085 25.804 1.00 83.07 ? 2152 ASN B ND2 1 ATOM 6764 N N . PRO B 2 617 ? 1.090 9.087 29.778 1.00 68.82 ? 2153 PRO B N 1 ATOM 6765 C CA . PRO B 2 617 ? 1.384 9.673 31.087 1.00 65.92 ? 2153 PRO B CA 1 ATOM 6766 C C . PRO B 2 617 ? 2.648 8.931 31.532 1.00 63.09 ? 2153 PRO B C 1 ATOM 6767 O O . PRO B 2 617 ? 2.654 7.703 31.627 1.00 62.08 ? 2153 PRO B O 1 ATOM 6768 C CB . PRO B 2 617 ? 0.171 9.281 31.935 1.00 67.03 ? 2153 PRO B CB 1 ATOM 6769 C CG . PRO B 2 617 ? -0.913 9.018 30.920 1.00 68.89 ? 2153 PRO B CG 1 ATOM 6770 C CD . PRO B 2 617 ? -0.156 8.302 29.840 1.00 68.33 ? 2153 PRO B CD 1 ATOM 6771 N N . PRO B 2 618 ? 3.742 9.657 31.778 1.00 60.65 ? 2154 PRO B N 1 ATOM 6772 C CA . PRO B 2 618 ? 4.984 9.008 32.208 1.00 59.17 ? 2154 PRO B CA 1 ATOM 6773 C C . PRO B 2 618 ? 4.820 8.044 33.381 1.00 57.89 ? 2154 PRO B C 1 ATOM 6774 O O . PRO B 2 618 ? 3.823 8.068 34.091 1.00 58.75 ? 2154 PRO B O 1 ATOM 6775 C CB . PRO B 2 618 ? 5.873 10.190 32.562 1.00 57.12 ? 2154 PRO B CB 1 ATOM 6776 C CG . PRO B 2 618 ? 5.455 11.199 31.563 1.00 59.38 ? 2154 PRO B CG 1 ATOM 6777 C CD . PRO B 2 618 ? 3.948 11.099 31.590 1.00 59.65 ? 2154 PRO B CD 1 ATOM 6778 N N . ILE B 2 619 ? 5.805 7.184 33.572 1.00 56.91 ? 2155 ILE B N 1 ATOM 6779 C CA . ILE B 2 619 ? 5.772 6.247 34.677 1.00 58.41 ? 2155 ILE B CA 1 ATOM 6780 C C . ILE B 2 619 ? 6.731 6.772 35.732 1.00 60.06 ? 2155 ILE B C 1 ATOM 6781 O O . ILE B 2 619 ? 7.877 7.106 35.435 1.00 61.32 ? 2155 ILE B O 1 ATOM 6782 C CB . ILE B 2 619 ? 6.215 4.832 34.237 1.00 58.66 ? 2155 ILE B CB 1 ATOM 6783 C CG1 . ILE B 2 619 ? 5.070 4.130 33.502 1.00 58.24 ? 2155 ILE B CG1 1 ATOM 6784 C CG2 . ILE B 2 619 ? 6.656 4.018 35.444 1.00 59.55 ? 2155 ILE B CG2 1 ATOM 6785 C CD1 . ILE B 2 619 ? 5.473 2.809 32.891 1.00 57.36 ? 2155 ILE B CD1 1 ATOM 6786 N N . ILE B 2 620 ? 6.264 6.865 36.965 1.00 60.54 ? 2156 ILE B N 1 ATOM 6787 C CA . ILE B 2 620 ? 7.118 7.357 38.024 1.00 61.80 ? 2156 ILE B CA 1 ATOM 6788 C C . ILE B 2 620 ? 7.279 6.214 38.992 1.00 63.80 ? 2156 ILE B C 1 ATOM 6789 O O . ILE B 2 620 ? 6.376 5.915 39.762 1.00 67.90 ? 2156 ILE B O 1 ATOM 6790 C CB . ILE B 2 620 ? 6.476 8.554 38.745 1.00 62.34 ? 2156 ILE B CB 1 ATOM 6791 C CG1 . ILE B 2 620 ? 6.010 9.589 37.718 1.00 62.08 ? 2156 ILE B CG1 1 ATOM 6792 C CG2 . ILE B 2 620 ? 7.471 9.172 39.724 1.00 59.91 ? 2156 ILE B CG2 1 ATOM 6793 C CD1 . ILE B 2 620 ? 7.125 10.220 36.931 1.00 64.75 ? 2156 ILE B CD1 1 ATOM 6794 N N . SER B 2 621 ? 8.423 5.554 38.949 1.00 64.57 ? 2157 SER B N 1 ATOM 6795 C CA . SER B 2 621 ? 8.640 4.431 39.839 1.00 65.05 ? 2157 SER B CA 1 ATOM 6796 C C . SER B 2 621 ? 10.088 4.014 39.836 1.00 65.54 ? 2157 SER B C 1 ATOM 6797 O O . SER B 2 621 ? 10.947 4.698 39.288 1.00 66.62 ? 2157 SER B O 1 ATOM 6798 C CB . SER B 2 621 ? 7.767 3.249 39.416 1.00 64.70 ? 2157 SER B CB 1 ATOM 6799 O OG . SER B 2 621 ? 8.042 2.874 38.078 1.00 65.39 ? 2157 SER B OG 1 ATOM 6800 N N . ARG B 2 622 ? 10.351 2.873 40.448 1.00 65.48 ? 2158 ARG B N 1 ATOM 6801 C CA . ARG B 2 622 ? 11.700 2.356 40.535 1.00 66.27 ? 2158 ARG B CA 1 ATOM 6802 C C . ARG B 2 622 ? 11.795 0.999 39.844 1.00 66.66 ? 2158 ARG B C 1 ATOM 6803 O O . ARG B 2 622 ? 12.859 0.603 39.368 1.00 67.72 ? 2158 ARG B O 1 ATOM 6804 C CB . ARG B 2 622 ? 12.089 2.240 42.006 1.00 66.86 ? 2158 ARG B CB 1 ATOM 6805 C CG . ARG B 2 622 ? 13.351 1.459 42.257 1.00 69.39 ? 2158 ARG B CG 1 ATOM 6806 C CD . ARG B 2 622 ? 13.623 1.335 43.738 1.00 70.58 ? 2158 ARG B CD 1 ATOM 6807 N NE . ARG B 2 622 ? 14.643 0.324 43.993 1.00 71.31 ? 2158 ARG B NE 1 ATOM 6808 C CZ . ARG B 2 622 ? 15.432 0.313 45.060 1.00 70.50 ? 2158 ARG B CZ 1 ATOM 6809 N NH1 . ARG B 2 622 ? 15.326 1.263 45.985 1.00 69.15 ? 2158 ARG B NH1 1 ATOM 6810 N NH2 . ARG B 2 622 ? 16.337 -0.643 45.191 1.00 68.58 ? 2158 ARG B NH2 1 ATOM 6811 N N . PHE B 2 623 ? 10.669 0.298 39.778 1.00 66.18 ? 2159 PHE B N 1 ATOM 6812 C CA . PHE B 2 623 ? 10.620 -1.019 39.163 1.00 64.77 ? 2159 PHE B CA 1 ATOM 6813 C C . PHE B 2 623 ? 9.717 -1.020 37.953 1.00 64.41 ? 2159 PHE B C 1 ATOM 6814 O O . PHE B 2 623 ? 8.608 -0.492 38.000 1.00 64.96 ? 2159 PHE B O 1 ATOM 6815 C CB . PHE B 2 623 ? 10.106 -2.052 40.176 1.00 66.44 ? 2159 PHE B CB 1 ATOM 6816 C CG . PHE B 2 623 ? 11.116 -2.433 41.216 1.00 66.18 ? 2159 PHE B CG 1 ATOM 6817 C CD1 . PHE B 2 623 ? 11.929 -3.547 41.034 1.00 65.15 ? 2159 PHE B CD1 1 ATOM 6818 C CD2 . PHE B 2 623 ? 11.293 -1.647 42.350 1.00 65.09 ? 2159 PHE B CD2 1 ATOM 6819 C CE1 . PHE B 2 623 ? 12.907 -3.872 41.960 1.00 65.42 ? 2159 PHE B CE1 1 ATOM 6820 C CE2 . PHE B 2 623 ? 12.269 -1.962 43.285 1.00 66.14 ? 2159 PHE B CE2 1 ATOM 6821 C CZ . PHE B 2 623 ? 13.079 -3.076 43.091 1.00 66.60 ? 2159 PHE B CZ 1 ATOM 6822 N N . ILE B 2 624 ? 10.195 -1.618 36.868 1.00 63.53 ? 2160 ILE B N 1 ATOM 6823 C CA . ILE B 2 624 ? 9.410 -1.711 35.650 1.00 63.32 ? 2160 ILE B CA 1 ATOM 6824 C C . ILE B 2 624 ? 9.388 -3.170 35.236 1.00 64.12 ? 2160 ILE B C 1 ATOM 6825 O O . ILE B 2 624 ? 10.408 -3.866 35.313 1.00 63.78 ? 2160 ILE B O 1 ATOM 6826 C CB . ILE B 2 624 ? 10.020 -0.862 34.517 1.00 63.28 ? 2160 ILE B CB 1 ATOM 6827 C CG1 . ILE B 2 624 ? 10.000 0.614 34.909 1.00 63.98 ? 2160 ILE B CG1 1 ATOM 6828 C CG2 . ILE B 2 624 ? 9.225 -1.049 33.232 1.00 62.96 ? 2160 ILE B CG2 1 ATOM 6829 C CD1 . ILE B 2 624 ? 8.611 1.186 35.066 1.00 65.73 ? 2160 ILE B CD1 1 ATOM 6830 N N . ARG B 2 625 ? 8.222 -3.632 34.806 1.00 63.59 ? 2161 ARG B N 1 ATOM 6831 C CA . ARG B 2 625 ? 8.064 -5.015 34.396 1.00 64.55 ? 2161 ARG B CA 1 ATOM 6832 C C . ARG B 2 625 ? 7.443 -5.190 33.019 1.00 64.65 ? 2161 ARG B C 1 ATOM 6833 O O . ARG B 2 625 ? 6.404 -4.605 32.701 1.00 65.38 ? 2161 ARG B O 1 ATOM 6834 C CB . ARG B 2 625 ? 7.206 -5.767 35.409 1.00 66.83 ? 2161 ARG B CB 1 ATOM 6835 C CG . ARG B 2 625 ? 7.973 -6.484 36.484 1.00 68.30 ? 2161 ARG B CG 1 ATOM 6836 C CD . ARG B 2 625 ? 7.062 -7.486 37.145 1.00 69.17 ? 2161 ARG B CD 1 ATOM 6837 N NE . ARG B 2 625 ? 7.762 -8.282 38.140 1.00 72.57 ? 2161 ARG B NE 1 ATOM 6838 C CZ . ARG B 2 625 ? 7.192 -9.256 38.836 1.00 74.06 ? 2161 ARG B CZ 1 ATOM 6839 N NH1 . ARG B 2 625 ? 5.910 -9.543 38.637 1.00 75.42 ? 2161 ARG B NH1 1 ATOM 6840 N NH2 . ARG B 2 625 ? 7.902 -9.950 39.716 1.00 72.99 ? 2161 ARG B NH2 1 ATOM 6841 N N . ILE B 2 626 ? 8.073 -6.022 32.207 1.00 64.19 ? 2162 ILE B N 1 ATOM 6842 C CA . ILE B 2 626 ? 7.562 -6.275 30.878 1.00 64.45 ? 2162 ILE B CA 1 ATOM 6843 C C . ILE B 2 626 ? 6.927 -7.657 30.933 1.00 64.79 ? 2162 ILE B C 1 ATOM 6844 O O . ILE B 2 626 ? 7.572 -8.626 31.327 1.00 65.93 ? 2162 ILE B O 1 ATOM 6845 C CB . ILE B 2 626 ? 8.686 -6.241 29.842 1.00 64.32 ? 2162 ILE B CB 1 ATOM 6846 C CG1 . ILE B 2 626 ? 9.518 -4.972 30.016 1.00 68.00 ? 2162 ILE B CG1 1 ATOM 6847 C CG2 . ILE B 2 626 ? 8.103 -6.204 28.460 1.00 64.98 ? 2162 ILE B CG2 1 ATOM 6848 C CD1 . ILE B 2 626 ? 10.349 -4.919 31.295 1.00 70.13 ? 2162 ILE B CD1 1 ATOM 6849 N N . ILE B 2 627 ? 5.657 -7.738 30.556 1.00 63.08 ? 2163 ILE B N 1 ATOM 6850 C CA . ILE B 2 627 ? 4.928 -8.991 30.596 1.00 61.08 ? 2163 ILE B CA 1 ATOM 6851 C C . ILE B 2 627 ? 4.585 -9.484 29.204 1.00 60.42 ? 2163 ILE B C 1 ATOM 6852 O O . ILE B 2 627 ? 3.561 -9.099 28.639 1.00 58.98 ? 2163 ILE B O 1 ATOM 6853 C CB . ILE B 2 627 ? 3.599 -8.838 31.372 1.00 62.73 ? 2163 ILE B CB 1 ATOM 6854 C CG1 . ILE B 2 627 ? 3.852 -8.213 32.747 1.00 62.26 ? 2163 ILE B CG1 1 ATOM 6855 C CG2 . ILE B 2 627 ? 2.903 -10.194 31.487 1.00 64.54 ? 2163 ILE B CG2 1 ATOM 6856 C CD1 . ILE B 2 627 ? 4.802 -8.980 33.613 1.00 63.96 ? 2163 ILE B CD1 1 ATOM 6857 N N . PRO B 2 628 ? 5.436 -10.345 28.627 1.00 59.72 ? 2164 PRO B N 1 ATOM 6858 C CA . PRO B 2 628 ? 5.158 -10.862 27.286 1.00 60.08 ? 2164 PRO B CA 1 ATOM 6859 C C . PRO B 2 628 ? 3.747 -11.466 27.241 1.00 61.46 ? 2164 PRO B C 1 ATOM 6860 O O . PRO B 2 628 ? 3.357 -12.204 28.148 1.00 63.38 ? 2164 PRO B O 1 ATOM 6861 C CB . PRO B 2 628 ? 6.253 -11.906 27.095 1.00 58.67 ? 2164 PRO B CB 1 ATOM 6862 C CG . PRO B 2 628 ? 7.396 -11.320 27.860 1.00 57.95 ? 2164 PRO B CG 1 ATOM 6863 C CD . PRO B 2 628 ? 6.732 -10.836 29.125 1.00 58.50 ? 2164 PRO B CD 1 ATOM 6864 N N . LYS B 2 629 ? 2.991 -11.137 26.197 1.00 61.50 ? 2165 LYS B N 1 ATOM 6865 C CA . LYS B 2 629 ? 1.627 -11.625 26.021 1.00 62.42 ? 2165 LYS B CA 1 ATOM 6866 C C . LYS B 2 629 ? 1.529 -12.444 24.737 1.00 65.06 ? 2165 LYS B C 1 ATOM 6867 O O . LYS B 2 629 ? 0.695 -13.346 24.618 1.00 67.23 ? 2165 LYS B O 1 ATOM 6868 C CB . LYS B 2 629 ? 0.644 -10.451 25.940 1.00 62.39 ? 2165 LYS B CB 1 ATOM 6869 C CG . LYS B 2 629 ? -0.362 -10.394 27.064 1.00 61.89 ? 2165 LYS B CG 1 ATOM 6870 C CD . LYS B 2 629 ? 0.330 -10.201 28.411 1.00 63.82 ? 2165 LYS B CD 1 ATOM 6871 C CE . LYS B 2 629 ? -0.678 -10.246 29.540 1.00 62.94 ? 2165 LYS B CE 1 ATOM 6872 N NZ . LYS B 2 629 ? -1.828 -9.345 29.247 1.00 63.53 ? 2165 LYS B NZ 1 ATOM 6873 N N . THR B 2 630 ? 2.365 -12.108 23.762 1.00 64.91 ? 2166 THR B N 1 ATOM 6874 C CA . THR B 2 630 ? 2.371 -12.837 22.509 1.00 65.41 ? 2166 THR B CA 1 ATOM 6875 C C . THR B 2 630 ? 3.780 -12.758 21.922 1.00 66.91 ? 2166 THR B C 1 ATOM 6876 O O . THR B 2 630 ? 4.558 -11.892 22.313 1.00 66.04 ? 2166 THR B O 1 ATOM 6877 C CB . THR B 2 630 ? 1.318 -12.278 21.539 1.00 64.58 ? 2166 THR B CB 1 ATOM 6878 O OG1 . THR B 2 630 ? 1.005 -13.275 20.558 1.00 63.29 ? 2166 THR B OG1 1 ATOM 6879 C CG2 . THR B 2 630 ? 1.827 -11.023 20.848 1.00 63.76 ? 2166 THR B CG2 1 ATOM 6880 N N . TRP B 2 631 ? 4.113 -13.660 21.001 1.00 68.55 ? 2167 TRP B N 1 ATOM 6881 C CA . TRP B 2 631 ? 5.460 -13.694 20.437 1.00 71.16 ? 2167 TRP B CA 1 ATOM 6882 C C . TRP B 2 631 ? 5.570 -14.563 19.194 1.00 72.48 ? 2167 TRP B C 1 ATOM 6883 O O . TRP B 2 631 ? 4.565 -14.935 18.594 1.00 72.69 ? 2167 TRP B O 1 ATOM 6884 C CB . TRP B 2 631 ? 6.421 -14.231 21.496 1.00 72.48 ? 2167 TRP B CB 1 ATOM 6885 C CG . TRP B 2 631 ? 5.911 -15.495 22.109 1.00 75.22 ? 2167 TRP B CG 1 ATOM 6886 C CD1 . TRP B 2 631 ? 6.044 -16.765 21.616 1.00 76.13 ? 2167 TRP B CD1 1 ATOM 6887 C CD2 . TRP B 2 631 ? 5.109 -15.606 23.290 1.00 75.61 ? 2167 TRP B CD2 1 ATOM 6888 N NE1 . TRP B 2 631 ? 5.372 -17.657 22.419 1.00 75.78 ? 2167 TRP B NE1 1 ATOM 6889 C CE2 . TRP B 2 631 ? 4.791 -16.969 23.454 1.00 76.01 ? 2167 TRP B CE2 1 ATOM 6890 C CE3 . TRP B 2 631 ? 4.624 -14.682 24.225 1.00 76.06 ? 2167 TRP B CE3 1 ATOM 6891 C CZ2 . TRP B 2 631 ? 4.013 -17.430 24.518 1.00 76.69 ? 2167 TRP B CZ2 1 ATOM 6892 C CZ3 . TRP B 2 631 ? 3.850 -15.140 25.278 1.00 76.73 ? 2167 TRP B CZ3 1 ATOM 6893 C CH2 . TRP B 2 631 ? 3.553 -16.501 25.417 1.00 76.93 ? 2167 TRP B CH2 1 ATOM 6894 N N . ASN B 2 632 ? 6.808 -14.882 18.820 1.00 73.80 ? 2168 ASN B N 1 ATOM 6895 C CA . ASN B 2 632 ? 7.082 -15.716 17.655 1.00 75.20 ? 2168 ASN B CA 1 ATOM 6896 C C . ASN B 2 632 ? 8.174 -16.735 17.984 1.00 76.96 ? 2168 ASN B C 1 ATOM 6897 O O . ASN B 2 632 ? 9.303 -16.367 18.307 1.00 77.16 ? 2168 ASN B O 1 ATOM 6898 C CB . ASN B 2 632 ? 7.504 -14.844 16.468 1.00 73.65 ? 2168 ASN B CB 1 ATOM 6899 C CG . ASN B 2 632 ? 7.743 -15.653 15.201 1.00 74.21 ? 2168 ASN B CG 1 ATOM 6900 O OD1 . ASN B 2 632 ? 7.634 -15.136 14.090 1.00 72.37 ? 2168 ASN B OD1 1 ATOM 6901 N ND2 . ASN B 2 632 ? 8.081 -16.925 15.366 1.00 74.03 ? 2168 ASN B ND2 1 ATOM 6902 N N . GLN B 2 633 ? 7.813 -18.015 17.901 1.00 78.58 ? 2169 GLN B N 1 ATOM 6903 C CA . GLN B 2 633 ? 8.712 -19.133 18.189 1.00 80.43 ? 2169 GLN B CA 1 ATOM 6904 C C . GLN B 2 633 ? 9.239 -19.266 19.616 1.00 80.65 ? 2169 GLN B C 1 ATOM 6905 O O . GLN B 2 633 ? 9.214 -20.365 20.174 1.00 81.93 ? 2169 GLN B O 1 ATOM 6906 C CB . GLN B 2 633 ? 9.892 -19.149 17.217 1.00 82.15 ? 2169 GLN B CB 1 ATOM 6907 C CG . GLN B 2 633 ? 9.574 -19.883 15.928 1.00 85.79 ? 2169 GLN B CG 1 ATOM 6908 C CD . GLN B 2 633 ? 8.794 -21.176 16.175 1.00 88.32 ? 2169 GLN B CD 1 ATOM 6909 O OE1 . GLN B 2 633 ? 9.173 -21.999 17.021 1.00 88.80 ? 2169 GLN B OE1 1 ATOM 6910 N NE2 . GLN B 2 633 ? 7.700 -21.358 15.435 1.00 88.10 ? 2169 GLN B NE2 1 ATOM 6911 N N . SER B 2 634 ? 9.719 -18.172 20.204 1.00 80.05 ? 2170 SER B N 1 ATOM 6912 C CA . SER B 2 634 ? 10.244 -18.209 21.573 1.00 78.77 ? 2170 SER B CA 1 ATOM 6913 C C . SER B 2 634 ? 10.331 -16.813 22.180 1.00 77.07 ? 2170 SER B C 1 ATOM 6914 O O . SER B 2 634 ? 10.590 -15.839 21.474 1.00 75.84 ? 2170 SER B O 1 ATOM 6915 C CB . SER B 2 634 ? 11.639 -18.847 21.606 1.00 80.20 ? 2170 SER B CB 1 ATOM 6916 O OG . SER B 2 634 ? 11.641 -20.146 21.030 1.00 85.25 ? 2170 SER B OG 1 ATOM 6917 N N . ILE B 2 635 ? 10.129 -16.733 23.493 1.00 73.92 ? 2171 ILE B N 1 ATOM 6918 C CA . ILE B 2 635 ? 10.181 -15.468 24.209 1.00 71.17 ? 2171 ILE B CA 1 ATOM 6919 C C . ILE B 2 635 ? 11.603 -15.081 24.598 1.00 71.26 ? 2171 ILE B C 1 ATOM 6920 O O . ILE B 2 635 ? 12.168 -15.617 25.560 1.00 71.10 ? 2171 ILE B O 1 ATOM 6921 C CB . ILE B 2 635 ? 9.334 -15.516 25.496 1.00 71.58 ? 2171 ILE B CB 1 ATOM 6922 C CG1 . ILE B 2 635 ? 7.845 -15.547 25.140 1.00 71.86 ? 2171 ILE B CG1 1 ATOM 6923 C CG2 . ILE B 2 635 ? 9.661 -14.322 26.388 1.00 68.43 ? 2171 ILE B CG2 1 ATOM 6924 C CD1 . ILE B 2 635 ? 6.936 -15.795 26.343 1.00 69.90 ? 2171 ILE B CD1 1 ATOM 6925 N N . ALA B 2 636 ? 12.166 -14.136 23.845 1.00 69.13 ? 2172 ALA B N 1 ATOM 6926 C CA . ALA B 2 636 ? 13.514 -13.622 24.082 1.00 65.60 ? 2172 ALA B CA 1 ATOM 6927 C C . ALA B 2 636 ? 13.474 -12.097 24.023 1.00 63.58 ? 2172 ALA B C 1 ATOM 6928 O O . ALA B 2 636 ? 12.578 -11.516 23.401 1.00 64.08 ? 2172 ALA B O 1 ATOM 6929 C CB . ALA B 2 636 ? 14.478 -14.160 23.029 1.00 66.14 ? 2172 ALA B CB 1 ATOM 6930 N N . LEU B 2 637 ? 14.436 -11.439 24.659 1.00 60.27 ? 2173 LEU B N 1 ATOM 6931 C CA . LEU B 2 637 ? 14.437 -9.990 24.641 1.00 58.57 ? 2173 LEU B CA 1 ATOM 6932 C C . LEU B 2 637 ? 15.766 -9.275 24.735 1.00 58.26 ? 2173 LEU B C 1 ATOM 6933 O O . LEU B 2 637 ? 16.766 -9.821 25.192 1.00 58.03 ? 2173 LEU B O 1 ATOM 6934 C CB . LEU B 2 637 ? 13.538 -9.442 25.749 1.00 59.91 ? 2173 LEU B CB 1 ATOM 6935 C CG . LEU B 2 637 ? 12.117 -9.037 25.365 1.00 60.30 ? 2173 LEU B CG 1 ATOM 6936 C CD1 . LEU B 2 637 ? 11.470 -8.321 26.541 1.00 60.90 ? 2173 LEU B CD1 1 ATOM 6937 C CD2 . LEU B 2 637 ? 12.148 -8.129 24.154 1.00 59.78 ? 2173 LEU B CD2 1 ATOM 6938 N N . ARG B 2 638 ? 15.717 -8.025 24.282 1.00 57.95 ? 2174 ARG B N 1 ATOM 6939 C CA . ARG B 2 638 ? 16.807 -7.051 24.278 1.00 55.54 ? 2174 ARG B CA 1 ATOM 6940 C C . ARG B 2 638 ? 16.046 -5.732 24.295 1.00 55.25 ? 2174 ARG B C 1 ATOM 6941 O O . ARG B 2 638 ? 15.311 -5.438 23.347 1.00 53.92 ? 2174 ARG B O 1 ATOM 6942 C CB . ARG B 2 638 ? 17.640 -7.144 22.996 1.00 52.86 ? 2174 ARG B CB 1 ATOM 6943 C CG . ARG B 2 638 ? 18.739 -8.195 23.030 1.00 51.52 ? 2174 ARG B CG 1 ATOM 6944 C CD . ARG B 2 638 ? 19.606 -8.111 21.794 1.00 47.93 ? 2174 ARG B CD 1 ATOM 6945 N NE . ARG B 2 638 ? 18.811 -8.301 20.589 1.00 46.58 ? 2174 ARG B NE 1 ATOM 6946 C CZ . ARG B 2 638 ? 19.239 -8.016 19.367 1.00 46.29 ? 2174 ARG B CZ 1 ATOM 6947 N NH1 . ARG B 2 638 ? 20.458 -7.528 19.190 1.00 44.06 ? 2174 ARG B NH1 1 ATOM 6948 N NH2 . ARG B 2 638 ? 18.449 -8.220 18.324 1.00 47.50 ? 2174 ARG B NH2 1 ATOM 6949 N N . LEU B 2 639 ? 16.186 -4.949 25.364 1.00 55.37 ? 2175 LEU B N 1 ATOM 6950 C CA . LEU B 2 639 ? 15.463 -3.678 25.436 1.00 56.06 ? 2175 LEU B CA 1 ATOM 6951 C C . LEU B 2 639 ? 16.237 -2.513 26.048 1.00 54.92 ? 2175 LEU B C 1 ATOM 6952 O O . LEU B 2 639 ? 17.354 -2.684 26.541 1.00 57.51 ? 2175 LEU B O 1 ATOM 6953 C CB . LEU B 2 639 ? 14.155 -3.866 26.206 1.00 56.42 ? 2175 LEU B CB 1 ATOM 6954 C CG . LEU B 2 639 ? 14.272 -4.147 27.701 1.00 59.17 ? 2175 LEU B CG 1 ATOM 6955 C CD1 . LEU B 2 639 ? 13.549 -3.038 28.479 1.00 60.83 ? 2175 LEU B CD1 1 ATOM 6956 C CD2 . LEU B 2 639 ? 13.673 -5.511 28.013 1.00 59.14 ? 2175 LEU B CD2 1 ATOM 6957 N N . GLU B 2 640 ? 15.631 -1.327 25.993 1.00 51.47 ? 2176 GLU B N 1 ATOM 6958 C CA . GLU B 2 640 ? 16.215 -0.110 26.550 1.00 50.55 ? 2176 GLU B CA 1 ATOM 6959 C C . GLU B 2 640 ? 15.057 0.779 26.957 1.00 50.64 ? 2176 GLU B C 1 ATOM 6960 O O . GLU B 2 640 ? 14.018 0.785 26.303 1.00 51.61 ? 2176 GLU B O 1 ATOM 6961 C CB . GLU B 2 640 ? 17.108 0.597 25.516 1.00 48.71 ? 2176 GLU B CB 1 ATOM 6962 C CG . GLU B 2 640 ? 17.655 1.979 25.914 1.00 48.37 ? 2176 GLU B CG 1 ATOM 6963 C CD . GLU B 2 640 ? 18.461 1.989 27.215 1.00 50.35 ? 2176 GLU B CD 1 ATOM 6964 O OE1 . GLU B 2 640 ? 17.850 1.920 28.310 1.00 51.50 ? 2176 GLU B OE1 1 ATOM 6965 O OE2 . GLU B 2 640 ? 19.710 2.071 27.149 1.00 50.39 ? 2176 GLU B OE2 1 ATOM 6966 N N . LEU B 2 641 ? 15.231 1.505 28.055 1.00 50.27 ? 2177 LEU B N 1 ATOM 6967 C CA . LEU B 2 641 ? 14.201 2.392 28.578 1.00 52.37 ? 2177 LEU B CA 1 ATOM 6968 C C . LEU B 2 641 ? 14.574 3.850 28.306 1.00 54.76 ? 2177 LEU B C 1 ATOM 6969 O O . LEU B 2 641 ? 15.705 4.145 27.914 1.00 57.31 ? 2177 LEU B O 1 ATOM 6970 C CB . LEU B 2 641 ? 14.071 2.185 30.095 1.00 49.24 ? 2177 LEU B CB 1 ATOM 6971 C CG . LEU B 2 641 ? 13.562 0.868 30.695 1.00 47.53 ? 2177 LEU B CG 1 ATOM 6972 C CD1 . LEU B 2 641 ? 14.114 0.725 32.084 1.00 46.29 ? 2177 LEU B CD1 1 ATOM 6973 C CD2 . LEU B 2 641 ? 12.048 0.836 30.731 1.00 46.39 ? 2177 LEU B CD2 1 ATOM 6974 N N . PHE B 2 642 ? 13.627 4.762 28.512 1.00 55.46 ? 2178 PHE B N 1 ATOM 6975 C CA . PHE B 2 642 ? 13.901 6.184 28.324 1.00 56.32 ? 2178 PHE B CA 1 ATOM 6976 C C . PHE B 2 642 ? 13.208 7.024 29.378 1.00 57.19 ? 2178 PHE B C 1 ATOM 6977 O O . PHE B 2 642 ? 12.053 6.780 29.735 1.00 55.30 ? 2178 PHE B O 1 ATOM 6978 C CB . PHE B 2 642 ? 13.474 6.650 26.931 1.00 57.24 ? 2178 PHE B CB 1 ATOM 6979 C CG . PHE B 2 642 ? 14.064 5.832 25.835 1.00 58.24 ? 2178 PHE B CG 1 ATOM 6980 C CD1 . PHE B 2 642 ? 13.408 4.691 25.380 1.00 58.51 ? 2178 PHE B CD1 1 ATOM 6981 C CD2 . PHE B 2 642 ? 15.330 6.126 25.338 1.00 57.86 ? 2178 PHE B CD2 1 ATOM 6982 C CE1 . PHE B 2 642 ? 14.007 3.851 24.458 1.00 58.54 ? 2178 PHE B CE1 1 ATOM 6983 C CE2 . PHE B 2 642 ? 15.942 5.289 24.412 1.00 58.86 ? 2178 PHE B CE2 1 ATOM 6984 C CZ . PHE B 2 642 ? 15.280 4.146 23.972 1.00 58.62 ? 2178 PHE B CZ 1 ATOM 6985 N N . GLY B 2 643 ? 13.937 8.015 29.873 1.00 58.77 ? 2179 GLY B N 1 ATOM 6986 C CA . GLY B 2 643 ? 13.412 8.903 30.886 1.00 61.25 ? 2179 GLY B CA 1 ATOM 6987 C C . GLY B 2 643 ? 14.550 9.659 31.530 1.00 63.99 ? 2179 GLY B C 1 ATOM 6988 O O . GLY B 2 643 ? 15.678 9.620 31.048 1.00 65.76 ? 2179 GLY B O 1 ATOM 6989 N N . CYS B 2 644 ? 14.266 10.335 32.634 1.00 66.19 ? 2180 CYS B N 1 ATOM 6990 C CA . CYS B 2 644 ? 15.284 11.110 33.313 1.00 66.93 ? 2180 CYS B CA 1 ATOM 6991 C C . CYS B 2 644 ? 15.119 11.071 34.839 1.00 69.16 ? 2180 CYS B C 1 ATOM 6992 O O . CYS B 2 644 ? 14.155 10.500 35.357 1.00 69.08 ? 2180 CYS B O 1 ATOM 6993 C CB . CYS B 2 644 ? 15.232 12.551 32.785 1.00 66.34 ? 2180 CYS B CB 1 ATOM 6994 S SG . CYS B 2 644 ? 13.711 13.490 33.162 1.00 67.76 ? 2180 CYS B SG 1 ATOM 6995 N N . ASP B 2 645 ? 16.077 11.658 35.555 1.00 71.03 ? 2181 ASP B N 1 ATOM 6996 C CA . ASP B 2 645 ? 16.035 11.723 37.017 1.00 72.44 ? 2181 ASP B CA 1 ATOM 6997 C C . ASP B 2 645 ? 14.908 12.648 37.470 1.00 74.44 ? 2181 ASP B C 1 ATOM 6998 O O . ASP B 2 645 ? 14.371 13.419 36.678 1.00 73.19 ? 2181 ASP B O 1 ATOM 6999 C CB . ASP B 2 645 ? 17.362 12.261 37.560 1.00 72.00 ? 2181 ASP B CB 1 ATOM 7000 C CG . ASP B 2 645 ? 18.289 11.166 38.029 1.00 72.06 ? 2181 ASP B CG 1 ATOM 7001 O OD1 . ASP B 2 645 ? 19.500 11.439 38.175 1.00 71.10 ? 2181 ASP B OD1 1 ATOM 7002 O OD2 . ASP B 2 645 ? 17.809 10.038 38.263 1.00 72.36 ? 2181 ASP B OD2 1 ATOM 7003 N N . MET B 2 646 ? 14.560 12.587 38.751 1.00 78.19 ? 2182 MET B N 1 ATOM 7004 C CA . MET B 2 646 ? 13.496 13.441 39.268 1.00 80.89 ? 2182 MET B CA 1 ATOM 7005 C C . MET B 2 646 ? 13.917 14.230 40.517 1.00 82.11 ? 2182 MET B C 1 ATOM 7006 O O . MET B 2 646 ? 13.897 15.486 40.452 1.00 82.10 ? 2182 MET B O 1 ATOM 7007 C CB . MET B 2 646 ? 12.253 12.589 39.552 1.00 81.72 ? 2182 MET B CB 1 ATOM 7008 C CG . MET B 2 646 ? 10.966 13.387 39.671 1.00 83.16 ? 2182 MET B CG 1 ATOM 7009 S SD . MET B 2 646 ? 9.511 12.452 39.130 1.00 84.20 ? 2182 MET B SD 1 ATOM 7010 C CE . MET B 2 646 ? 9.047 13.354 37.648 1.00 84.32 ? 2182 MET B CE 1 HETATM 7011 C C1 . NAG C 3 . ? -12.762 46.930 47.357 1.00 128.53 ? 2185 NAG A C1 1 HETATM 7012 C C2 . NAG C 3 . ? -13.743 46.018 46.607 1.00 129.35 ? 2185 NAG A C2 1 HETATM 7013 C C3 . NAG C 3 . ? -14.794 45.436 47.575 1.00 129.46 ? 2185 NAG A C3 1 HETATM 7014 C C4 . NAG C 3 . ? -14.366 45.620 49.037 1.00 129.30 ? 2185 NAG A C4 1 HETATM 7015 C C5 . NAG C 3 . ? -14.126 47.106 49.360 1.00 128.78 ? 2185 NAG A C5 1 HETATM 7016 C C6 . NAG C 3 . ? -13.270 47.314 50.594 1.00 128.51 ? 2185 NAG A C6 1 HETATM 7017 C C7 . NAG C 3 . ? -13.732 47.085 44.433 1.00 128.32 ? 2185 NAG A C7 1 HETATM 7018 C C8 . NAG C 3 . ? -13.105 48.471 44.384 1.00 127.39 ? 2185 NAG A C8 1 HETATM 7019 N N2 . NAG C 3 . ? -14.399 46.757 45.539 1.00 129.31 ? 2185 NAG A N2 1 HETATM 7020 O O3 . NAG C 3 . ? -14.977 44.050 47.309 1.00 129.20 ? 2185 NAG A O3 1 HETATM 7021 O O4 . NAG C 3 . ? -15.372 45.105 49.898 1.00 130.30 ? 2185 NAG A O4 1 HETATM 7022 O O5 . NAG C 3 . ? -13.471 47.799 48.262 1.00 128.75 ? 2185 NAG A O5 1 HETATM 7023 O O6 . NAG C 3 . ? -13.547 48.569 51.200 1.00 128.06 ? 2185 NAG A O6 1 HETATM 7024 O O7 . NAG C 3 . ? -13.616 46.324 43.470 1.00 127.55 ? 2185 NAG A O7 1 HETATM 7025 C C1 . NAG D 3 . ? 3.758 60.106 54.391 1.00 89.82 ? 2186 NAG A C1 1 HETATM 7026 C C2 . NAG D 3 . ? 4.271 61.196 53.451 1.00 89.60 ? 2186 NAG A C2 1 HETATM 7027 C C3 . NAG D 3 . ? 3.329 61.290 52.242 1.00 88.40 ? 2186 NAG A C3 1 HETATM 7028 C C4 . NAG D 3 . ? 3.211 59.910 51.563 1.00 87.52 ? 2186 NAG A C4 1 HETATM 7029 C C5 . NAG D 3 . ? 2.818 58.839 52.590 1.00 87.08 ? 2186 NAG A C5 1 HETATM 7030 C C6 . NAG D 3 . ? 2.870 57.445 52.019 1.00 86.89 ? 2186 NAG A C6 1 HETATM 7031 C C7 . NAG D 3 . ? 5.470 63.180 54.129 1.00 90.96 ? 2186 NAG A C7 1 HETATM 7032 C C8 . NAG D 3 . ? 5.597 64.242 53.045 1.00 90.54 ? 2186 NAG A C8 1 HETATM 7033 N N2 . NAG D 3 . ? 4.344 62.467 54.148 1.00 91.06 ? 2186 NAG A N2 1 HETATM 7034 O O3 . NAG D 3 . ? 3.827 62.251 51.319 1.00 86.92 ? 2186 NAG A O3 1 HETATM 7035 O O4 . NAG D 3 . ? 2.235 59.956 50.531 1.00 86.96 ? 2186 NAG A O4 1 HETATM 7036 O O5 . NAG D 3 . ? 3.730 58.849 53.708 1.00 88.54 ? 2186 NAG A O5 1 HETATM 7037 O O6 . NAG D 3 . ? 3.542 56.564 52.909 1.00 86.01 ? 2186 NAG A O6 1 HETATM 7038 O O7 . NAG D 3 . ? 6.385 63.014 54.941 1.00 88.80 ? 2186 NAG A O7 1 HETATM 7039 CA CA . CA E 4 . ? 5.215 24.131 37.135 1.00 68.70 ? 2184 CA A CA 1 HETATM 7040 C C1 . NDG F 5 . ? 20.077 55.166 -3.876 1.00 94.03 ? 2187 NDG B C1 1 HETATM 7041 C C2 . NDG F 5 . ? 19.210 55.457 -5.104 1.00 96.95 ? 2187 NDG B C2 1 HETATM 7042 C C3 . NDG F 5 . ? 19.349 56.950 -5.445 1.00 98.17 ? 2187 NDG B C3 1 HETATM 7043 C C4 . NDG F 5 . ? 18.984 57.825 -4.230 1.00 97.78 ? 2187 NDG B C4 1 HETATM 7044 C C5 . NDG F 5 . ? 19.711 57.359 -2.958 1.00 97.83 ? 2187 NDG B C5 1 HETATM 7045 C C6 . NDG F 5 . ? 19.172 58.028 -1.704 1.00 98.73 ? 2187 NDG B C6 1 HETATM 7046 C C7 . NDG F 5 . ? 18.843 54.529 -7.310 1.00 101.07 ? 2187 NDG B C7 1 HETATM 7047 C C8 . NDG F 5 . ? 19.228 55.374 -8.519 1.00 101.28 ? 2187 NDG B C8 1 HETATM 7048 O O . NDG F 5 . ? 19.572 55.928 -2.768 1.00 96.65 ? 2187 NDG B O 1 HETATM 7049 O O3 . NDG F 5 . ? 18.502 57.277 -6.539 1.00 100.46 ? 2187 NDG B O3 1 HETATM 7050 O O4 . NDG F 5 . ? 19.342 59.176 -4.493 1.00 95.98 ? 2187 NDG B O4 1 HETATM 7051 O O6 . NDG F 5 . ? 17.772 58.253 -1.795 1.00 99.60 ? 2187 NDG B O6 1 HETATM 7052 O O7 . NDG F 5 . ? 17.850 53.796 -7.369 1.00 101.63 ? 2187 NDG B O7 1 HETATM 7053 N N2 . NDG F 5 . ? 19.615 54.626 -6.227 1.00 99.30 ? 2187 NDG B N2 1 HETATM 7054 C C1 . NAG G 3 . ? 35.585 32.073 34.590 1.00 74.44 ? 2188 NAG B C1 1 HETATM 7055 C C2 . NAG G 3 . ? 35.145 30.817 33.827 1.00 74.98 ? 2188 NAG B C2 1 HETATM 7056 C C3 . NAG G 3 . ? 36.344 29.933 33.429 1.00 74.40 ? 2188 NAG B C3 1 HETATM 7057 C C4 . NAG G 3 . ? 37.403 30.767 32.718 1.00 73.69 ? 2188 NAG B C4 1 HETATM 7058 C C5 . NAG G 3 . ? 37.780 31.945 33.606 1.00 74.79 ? 2188 NAG B C5 1 HETATM 7059 C C6 . NAG G 3 . ? 38.820 32.833 32.956 1.00 76.86 ? 2188 NAG B C6 1 HETATM 7060 C C7 . NAG G 3 . ? 32.988 29.814 34.198 1.00 75.45 ? 2188 NAG B C7 1 HETATM 7061 C C8 . NAG G 3 . ? 32.303 28.558 34.715 1.00 73.75 ? 2188 NAG B C8 1 HETATM 7062 N N2 . NAG G 3 . ? 34.215 30.064 34.646 1.00 75.02 ? 2188 NAG B N2 1 HETATM 7063 O O3 . NAG G 3 . ? 35.906 28.899 32.558 1.00 74.36 ? 2188 NAG B O3 1 HETATM 7064 O O4 . NAG G 3 . ? 38.550 29.972 32.441 1.00 73.90 ? 2188 NAG B O4 1 HETATM 7065 O O5 . NAG G 3 . ? 36.613 32.764 33.861 1.00 76.01 ? 2188 NAG B O5 1 HETATM 7066 O O6 . NAG G 3 . ? 38.547 33.018 31.574 1.00 78.25 ? 2188 NAG B O6 1 HETATM 7067 O O7 . NAG G 3 . ? 32.407 30.544 33.390 1.00 74.71 ? 2188 NAG B O7 1 HETATM 7068 C C1 . NDG H 5 . ? 32.054 24.076 14.688 1.00 70.39 ? 2189 NDG B C1 1 HETATM 7069 C C2 . NDG H 5 . ? 33.061 24.785 15.613 1.00 72.56 ? 2189 NDG B C2 1 HETATM 7070 C C3 . NDG H 5 . ? 34.421 24.898 14.930 1.00 74.34 ? 2189 NDG B C3 1 HETATM 7071 C C4 . NDG H 5 . ? 34.980 23.506 14.611 1.00 72.90 ? 2189 NDG B C4 1 HETATM 7072 C C5 . NDG H 5 . ? 33.856 22.501 14.305 1.00 73.72 ? 2189 NDG B C5 1 HETATM 7073 C C6 . NDG H 5 . ? 33.402 21.653 15.497 1.00 72.85 ? 2189 NDG B C6 1 HETATM 7074 C C7 . NDG H 5 . ? 33.000 26.732 17.059 1.00 72.90 ? 2189 NDG B C7 1 HETATM 7075 C C8 . NDG H 5 . ? 32.140 27.879 17.561 1.00 71.56 ? 2189 NDG B C8 1 HETATM 7076 O O . NDG H 5 . ? 32.696 23.187 13.760 1.00 71.55 ? 2189 NDG B O 1 HETATM 7077 O O3 . NDG H 5 . ? 35.329 25.597 15.776 1.00 76.94 ? 2189 NDG B O3 1 HETATM 7078 O O4 . NDG H 5 . ? 35.846 23.602 13.491 1.00 72.31 ? 2189 NDG B O4 1 HETATM 7079 O O6 . NDG H 5 . ? 33.998 22.095 16.710 1.00 71.93 ? 2189 NDG B O6 1 HETATM 7080 O O7 . NDG H 5 . ? 34.030 26.425 17.657 1.00 73.11 ? 2189 NDG B O7 1 HETATM 7081 N N2 . NDG H 5 . ? 32.574 26.107 15.963 1.00 73.81 ? 2189 NDG B N2 1 HETATM 7082 CU CU . CU I 6 . ? 11.021 35.558 35.977 1.00 65.70 ? 2190 CU B CU 1 HETATM 7083 O O . HOH J 7 . ? 20.183 46.359 59.220 1.00 65.01 ? 2190 HOH A O 1 HETATM 7084 O O . HOH J 7 . ? 7.316 27.722 22.717 1.00 69.51 ? 2197 HOH A O 1 HETATM 7085 O O . HOH J 7 . ? 24.760 44.850 53.248 1.00 46.52 ? 2201 HOH A O 1 HETATM 7086 O O . HOH J 7 . ? 21.471 38.055 44.602 1.00 51.55 ? 2206 HOH A O 1 HETATM 7087 O O . HOH J 7 . ? 28.028 43.834 57.427 1.00 64.11 ? 2207 HOH A O 1 HETATM 7088 O O . HOH J 7 . ? 3.042 20.887 43.918 1.00 43.75 ? 2209 HOH A O 1 HETATM 7089 O O . HOH J 7 . ? -1.180 34.302 65.654 1.00 61.26 ? 2215 HOH A O 1 HETATM 7090 O O . HOH J 7 . ? -8.354 40.819 42.013 1.00 69.64 ? 2231 HOH A O 1 HETATM 7091 O O . HOH J 7 . ? -3.954 20.842 39.063 1.00 77.71 ? 2234 HOH A O 1 HETATM 7092 O O . HOH J 7 . ? 34.435 57.753 60.416 1.00 65.43 ? 2235 HOH A O 1 HETATM 7093 O O . HOH J 7 . ? 6.409 15.256 51.304 1.00 62.41 ? 2243 HOH A O 1 HETATM 7094 O O . HOH J 7 . ? -3.785 35.696 41.794 1.00 57.80 ? 2246 HOH A O 1 HETATM 7095 O O . HOH J 7 . ? -7.335 46.728 61.573 1.00 58.57 ? 2250 HOH A O 1 HETATM 7096 O O . HOH J 7 . ? 38.057 28.318 46.708 1.00 63.81 ? 2252 HOH A O 1 HETATM 7097 O O . HOH J 7 . ? -2.492 20.375 36.154 1.00 68.93 ? 2254 HOH A O 1 HETATM 7098 O O . HOH J 7 . ? 6.120 51.273 41.181 1.00 49.26 ? 2256 HOH A O 1 HETATM 7099 O O . HOH J 7 . ? 34.795 27.940 47.940 1.00 51.22 ? 2262 HOH A O 1 HETATM 7100 O O . HOH J 7 . ? 22.177 61.015 47.890 1.00 64.94 ? 2268 HOH A O 1 HETATM 7101 O O . HOH J 7 . ? 0.780 59.633 48.107 1.00 64.43 ? 2269 HOH A O 1 HETATM 7102 O O . HOH J 7 . ? 33.237 32.667 65.714 1.00 77.49 ? 2274 HOH A O 1 HETATM 7103 O O . HOH J 7 . ? 17.957 38.515 65.151 1.00 52.38 ? 2276 HOH A O 1 HETATM 7104 O O . HOH J 7 . ? 1.749 23.390 28.029 1.00 66.21 ? 2277 HOH A O 1 HETATM 7105 O O . HOH J 7 . ? -10.052 51.485 37.182 1.00 80.50 ? 2282 HOH A O 1 HETATM 7106 O O . HOH J 7 . ? 37.602 48.444 52.918 1.00 81.12 ? 2286 HOH A O 1 HETATM 7107 O O . HOH J 7 . ? 24.850 42.211 63.029 1.00 60.56 ? 2293 HOH A O 1 HETATM 7108 O O . HOH J 7 . ? 5.091 59.831 43.204 1.00 47.74 ? 2297 HOH A O 1 HETATM 7109 O O . HOH J 7 . ? 18.796 14.516 53.228 1.00 52.55 ? 2298 HOH A O 1 HETATM 7110 O O . HOH J 7 . ? 39.201 45.903 49.201 1.00 72.62 ? 2299 HOH A O 1 HETATM 7111 O O . HOH J 7 . ? 2.851 20.943 22.510 1.00 74.11 ? 2302 HOH A O 1 HETATM 7112 O O . HOH J 7 . ? -8.915 21.664 53.611 1.00 61.94 ? 2303 HOH A O 1 HETATM 7113 O O . HOH J 7 . ? -14.794 48.668 53.544 1.00 69.91 ? 2305 HOH A O 1 HETATM 7114 O O . HOH J 7 . ? 25.582 58.589 59.572 1.00 75.05 ? 2311 HOH A O 1 HETATM 7115 O O . HOH J 7 . ? 31.227 58.219 52.704 1.00 41.47 ? 2312 HOH A O 1 HETATM 7116 O O . HOH J 7 . ? 31.856 25.546 58.485 1.00 59.78 ? 2313 HOH A O 1 HETATM 7117 O O . HOH J 7 . ? 23.595 19.451 65.293 1.00 64.46 ? 2319 HOH A O 1 HETATM 7118 O O . HOH J 7 . ? 27.648 48.929 63.919 1.00 60.85 ? 2327 HOH A O 1 HETATM 7119 O O . HOH J 7 . ? -14.644 51.726 52.443 1.00 64.01 ? 2336 HOH A O 1 HETATM 7120 O O . HOH J 7 . ? 24.781 41.599 43.837 1.00 49.72 ? 2339 HOH A O 1 HETATM 7121 O O . HOH J 7 . ? 7.787 18.035 59.775 1.00 70.29 ? 2343 HOH A O 1 HETATM 7122 O O . HOH J 7 . ? 32.004 51.319 63.267 1.00 68.00 ? 2344 HOH A O 1 HETATM 7123 O O . HOH J 7 . ? 14.692 65.129 50.400 1.00 49.18 ? 2348 HOH A O 1 HETATM 7124 O O . HOH J 7 . ? -12.580 32.425 46.457 1.00 65.23 ? 2350 HOH A O 1 HETATM 7125 O O . HOH J 7 . ? 11.185 14.708 43.930 1.00 65.65 ? 2354 HOH A O 1 HETATM 7126 O O . HOH J 7 . ? 7.300 53.648 36.816 1.00 57.76 ? 2357 HOH A O 1 HETATM 7127 O O . HOH J 7 . ? 5.831 65.383 38.697 1.00 81.55 ? 2359 HOH A O 1 HETATM 7128 O O . HOH J 7 . ? 32.090 23.260 56.400 1.00 62.45 ? 2363 HOH A O 1 HETATM 7129 O O . HOH J 7 . ? 32.118 45.348 58.969 1.00 69.52 ? 2369 HOH A O 1 HETATM 7130 O O . HOH K 7 . ? 4.886 2.239 18.414 1.00 79.21 ? 2191 HOH B O 1 HETATM 7131 O O . HOH K 7 . ? 33.504 20.129 2.525 1.00 42.30 ? 2192 HOH B O 1 HETATM 7132 O O . HOH K 7 . ? 12.463 26.067 18.641 1.00 71.93 ? 2193 HOH B O 1 HETATM 7133 O O . HOH K 7 . ? 15.692 62.209 12.920 1.00 56.01 ? 2194 HOH B O 1 HETATM 7134 O O . HOH K 7 . ? 5.660 53.502 7.845 1.00 59.27 ? 2195 HOH B O 1 HETATM 7135 O O . HOH K 7 . ? 26.421 34.840 19.363 1.00 41.39 ? 2196 HOH B O 1 HETATM 7136 O O . HOH K 7 . ? 36.190 2.549 -1.139 1.00 38.84 ? 2198 HOH B O 1 HETATM 7137 O O . HOH K 7 . ? 15.515 11.583 17.519 1.00 56.48 ? 2199 HOH B O 1 HETATM 7138 O O . HOH K 7 . ? 14.061 7.849 17.647 1.00 53.00 ? 2200 HOH B O 1 HETATM 7139 O O . HOH K 7 . ? 32.136 17.034 13.722 1.00 58.22 ? 2202 HOH B O 1 HETATM 7140 O O . HOH K 7 . ? 24.761 -7.911 2.149 1.00 52.13 ? 2203 HOH B O 1 HETATM 7141 O O . HOH K 7 . ? 34.915 38.758 9.944 1.00 71.98 ? 2204 HOH B O 1 HETATM 7142 O O . HOH K 7 . ? 27.737 11.767 14.365 1.00 62.95 ? 2205 HOH B O 1 HETATM 7143 O O . HOH K 7 . ? 20.063 -0.945 8.430 1.00 61.27 ? 2208 HOH B O 1 HETATM 7144 O O . HOH K 7 . ? 15.936 64.581 19.799 1.00 54.70 ? 2210 HOH B O 1 HETATM 7145 O O . HOH K 7 . ? 3.727 11.841 6.067 1.00 60.24 ? 2211 HOH B O 1 HETATM 7146 O O . HOH K 7 . ? 10.523 29.271 18.794 1.00 55.11 ? 2212 HOH B O 1 HETATM 7147 O O . HOH K 7 . ? 9.893 7.483 13.399 1.00 39.05 ? 2213 HOH B O 1 HETATM 7148 O O . HOH K 7 . ? 24.639 31.050 19.756 1.00 43.56 ? 2214 HOH B O 1 HETATM 7149 O O . HOH K 7 . ? 26.790 18.176 23.159 1.00 65.58 ? 2216 HOH B O 1 HETATM 7150 O O . HOH K 7 . ? 38.403 5.713 -3.613 1.00 63.31 ? 2217 HOH B O 1 HETATM 7151 O O . HOH K 7 . ? 21.023 37.647 -0.680 1.00 70.52 ? 2218 HOH B O 1 HETATM 7152 O O . HOH K 7 . ? 36.432 40.226 3.924 1.00 55.69 ? 2219 HOH B O 1 HETATM 7153 O O . HOH K 7 . ? 11.822 30.613 13.580 1.00 71.07 ? 2220 HOH B O 1 HETATM 7154 O O . HOH K 7 . ? 28.977 21.015 24.237 1.00 66.69 ? 2221 HOH B O 1 HETATM 7155 O O . HOH K 7 . ? 9.210 23.887 18.250 1.00 61.67 ? 2222 HOH B O 1 HETATM 7156 O O . HOH K 7 . ? 25.737 15.355 35.757 1.00 63.96 ? 2223 HOH B O 1 HETATM 7157 O O . HOH K 7 . ? 47.704 39.855 32.603 1.00 60.53 ? 2224 HOH B O 1 HETATM 7158 O O . HOH K 7 . ? 29.367 22.878 -4.046 1.00 57.89 ? 2225 HOH B O 1 HETATM 7159 O O . HOH K 7 . ? 3.111 36.893 33.048 1.00 61.27 ? 2226 HOH B O 1 HETATM 7160 O O . HOH K 7 . ? 19.534 -5.891 10.094 1.00 59.95 ? 2227 HOH B O 1 HETATM 7161 O O . HOH K 7 . ? 22.944 40.423 8.998 1.00 58.54 ? 2228 HOH B O 1 HETATM 7162 O O . HOH K 7 . ? 28.107 8.086 17.286 1.00 79.10 ? 2229 HOH B O 1 HETATM 7163 O O . HOH K 7 . ? 3.585 19.678 8.110 1.00 68.57 ? 2230 HOH B O 1 HETATM 7164 O O . HOH K 7 . ? 9.739 20.955 -1.480 1.00 98.19 ? 2232 HOH B O 1 HETATM 7165 O O . HOH K 7 . ? 32.900 17.903 8.255 1.00 52.56 ? 2233 HOH B O 1 HETATM 7166 O O . HOH K 7 . ? 18.928 -5.394 5.275 1.00 61.99 ? 2236 HOH B O 1 HETATM 7167 O O . HOH K 7 . ? 27.146 54.719 28.305 1.00 55.65 ? 2237 HOH B O 1 HETATM 7168 O O . HOH K 7 . ? 19.983 1.587 18.034 1.00 45.64 ? 2238 HOH B O 1 HETATM 7169 O O . HOH K 7 . ? 42.310 40.056 29.280 1.00 57.67 ? 2239 HOH B O 1 HETATM 7170 O O . HOH K 7 . ? 27.856 -27.323 21.982 1.00 59.29 ? 2240 HOH B O 1 HETATM 7171 O O . HOH K 7 . ? 35.808 49.885 20.368 1.00 50.30 ? 2241 HOH B O 1 HETATM 7172 O O . HOH K 7 . ? 10.852 29.031 15.993 1.00 64.38 ? 2242 HOH B O 1 HETATM 7173 O O . HOH K 7 . ? 21.719 6.779 22.378 1.00 60.94 ? 2244 HOH B O 1 HETATM 7174 O O . HOH K 7 . ? 34.741 46.449 29.900 1.00 56.53 ? 2245 HOH B O 1 HETATM 7175 O O . HOH K 7 . ? 3.516 5.274 21.572 1.00 48.10 ? 2247 HOH B O 1 HETATM 7176 O O . HOH K 7 . ? 28.326 20.765 21.449 1.00 53.68 ? 2248 HOH B O 1 HETATM 7177 O O . HOH K 7 . ? 6.747 33.561 26.878 1.00 51.21 ? 2249 HOH B O 1 HETATM 7178 O O . HOH K 7 . ? 44.560 38.765 31.662 1.00 80.82 ? 2251 HOH B O 1 HETATM 7179 O O . HOH K 7 . ? 28.315 38.428 12.983 1.00 66.88 ? 2253 HOH B O 1 HETATM 7180 O O . HOH K 7 . ? 27.253 65.955 9.812 1.00 55.61 ? 2255 HOH B O 1 HETATM 7181 O O . HOH K 7 . ? 10.988 44.091 4.485 1.00 60.39 ? 2257 HOH B O 1 HETATM 7182 O O . HOH K 7 . ? 39.431 4.291 -0.030 1.00 68.96 ? 2258 HOH B O 1 HETATM 7183 O O . HOH K 7 . ? 27.951 -7.219 23.705 1.00 51.44 ? 2259 HOH B O 1 HETATM 7184 O O . HOH K 7 . ? 11.274 17.154 -7.283 1.00 71.63 ? 2260 HOH B O 1 HETATM 7185 O O . HOH K 7 . ? 12.917 30.392 5.707 1.00 66.98 ? 2261 HOH B O 1 HETATM 7186 O O . HOH K 7 . ? 3.489 -1.024 14.642 1.00 70.87 ? 2263 HOH B O 1 HETATM 7187 O O . HOH K 7 . ? 2.184 46.184 22.389 1.00 63.24 ? 2264 HOH B O 1 HETATM 7188 O O . HOH K 7 . ? -0.386 -9.089 37.548 1.00 85.21 ? 2265 HOH B O 1 HETATM 7189 O O . HOH K 7 . ? 22.930 -10.807 12.178 1.00 52.75 ? 2266 HOH B O 1 HETATM 7190 O O . HOH K 7 . ? 8.393 -8.009 47.119 1.00 72.44 ? 2267 HOH B O 1 HETATM 7191 O O . HOH K 7 . ? 37.593 10.758 -3.226 1.00 68.99 ? 2270 HOH B O 1 HETATM 7192 O O . HOH K 7 . ? 42.006 48.518 3.182 1.00 61.67 ? 2271 HOH B O 1 HETATM 7193 O O . HOH K 7 . ? 41.848 45.259 37.356 1.00 72.75 ? 2272 HOH B O 1 HETATM 7194 O O . HOH K 7 . ? 41.186 28.574 16.864 1.00 74.63 ? 2273 HOH B O 1 HETATM 7195 O O . HOH K 7 . ? 11.080 9.181 -4.037 1.00 58.18 ? 2275 HOH B O 1 HETATM 7196 O O . HOH K 7 . ? 13.225 56.428 38.030 1.00 56.94 ? 2278 HOH B O 1 HETATM 7197 O O . HOH K 7 . ? -2.910 46.619 31.146 1.00 99.92 ? 2279 HOH B O 1 HETATM 7198 O O . HOH K 7 . ? 33.278 25.090 9.156 1.00 40.92 ? 2280 HOH B O 1 HETATM 7199 O O . HOH K 7 . ? 28.118 60.194 2.570 1.00 68.86 ? 2281 HOH B O 1 HETATM 7200 O O . HOH K 7 . ? 1.312 50.362 12.030 1.00 57.38 ? 2283 HOH B O 1 HETATM 7201 O O . HOH K 7 . ? -0.424 45.068 34.447 1.00 53.86 ? 2284 HOH B O 1 HETATM 7202 O O . HOH K 7 . ? 31.534 24.640 5.819 1.00 56.38 ? 2285 HOH B O 1 HETATM 7203 O O . HOH K 7 . ? 24.978 15.002 23.357 1.00 61.07 ? 2287 HOH B O 1 HETATM 7204 O O . HOH K 7 . ? 31.785 17.193 30.099 1.00 70.28 ? 2288 HOH B O 1 HETATM 7205 O O . HOH K 7 . ? 11.020 47.439 3.128 1.00 68.34 ? 2289 HOH B O 1 HETATM 7206 O O . HOH K 7 . ? 5.469 31.165 24.416 1.00 79.99 ? 2290 HOH B O 1 HETATM 7207 O O . HOH K 7 . ? -1.342 6.542 32.751 1.00 55.88 ? 2291 HOH B O 1 HETATM 7208 O O . HOH K 7 . ? 33.142 55.910 -0.643 1.00 52.42 ? 2292 HOH B O 1 HETATM 7209 O O . HOH K 7 . ? -1.214 49.189 13.700 1.00 61.23 ? 2294 HOH B O 1 HETATM 7210 O O . HOH K 7 . ? 32.981 6.955 -13.387 1.00 54.58 ? 2295 HOH B O 1 HETATM 7211 O O . HOH K 7 . ? 19.499 29.207 8.468 1.00 44.95 ? 2296 HOH B O 1 HETATM 7212 O O . HOH K 7 . ? 18.092 42.757 12.070 1.00 49.91 ? 2300 HOH B O 1 HETATM 7213 O O . HOH K 7 . ? 21.168 5.834 35.171 1.00 69.13 ? 2301 HOH B O 1 HETATM 7214 O O . HOH K 7 . ? 37.722 60.163 5.651 1.00 86.33 ? 2304 HOH B O 1 HETATM 7215 O O . HOH K 7 . ? 24.432 -3.489 23.926 1.00 58.87 ? 2306 HOH B O 1 HETATM 7216 O O . HOH K 7 . ? 26.335 27.150 -7.620 1.00 81.40 ? 2307 HOH B O 1 HETATM 7217 O O . HOH K 7 . ? -3.400 58.026 12.339 1.00 74.45 ? 2308 HOH B O 1 HETATM 7218 O O . HOH K 7 . ? 9.767 11.038 25.151 1.00 63.94 ? 2309 HOH B O 1 HETATM 7219 O O . HOH K 7 . ? 5.887 -21.495 20.471 1.00 53.28 ? 2310 HOH B O 1 HETATM 7220 O O . HOH K 7 . ? 38.758 12.978 3.400 1.00 72.95 ? 2314 HOH B O 1 HETATM 7221 O O . HOH K 7 . ? 6.834 -21.929 33.799 1.00 61.39 ? 2315 HOH B O 1 HETATM 7222 O O . HOH K 7 . ? 23.201 3.928 14.956 1.00 47.30 ? 2316 HOH B O 1 HETATM 7223 O O . HOH K 7 . ? 22.541 44.849 -5.988 1.00 62.94 ? 2317 HOH B O 1 HETATM 7224 O O . HOH K 7 . ? 13.331 25.316 14.302 1.00 57.82 ? 2318 HOH B O 1 HETATM 7225 O O . HOH K 7 . ? 19.767 -6.780 -2.185 1.00 68.75 ? 2320 HOH B O 1 HETATM 7226 O O . HOH K 7 . ? 9.965 -6.182 8.711 1.00 57.09 ? 2321 HOH B O 1 HETATM 7227 O O . HOH K 7 . ? 10.694 10.961 -8.168 1.00 89.34 ? 2322 HOH B O 1 HETATM 7228 O O . HOH K 7 . ? 10.888 61.029 30.995 1.00 56.06 ? 2323 HOH B O 1 HETATM 7229 O O . HOH K 7 . ? -0.944 34.037 21.093 1.00 60.72 ? 2324 HOH B O 1 HETATM 7230 O O . HOH K 7 . ? 35.706 3.707 -9.883 1.00 44.41 ? 2325 HOH B O 1 HETATM 7231 O O . HOH K 7 . ? 36.132 0.349 6.555 1.00 79.73 ? 2326 HOH B O 1 HETATM 7232 O O . HOH K 7 . ? 22.109 -17.112 13.906 1.00 90.31 ? 2328 HOH B O 1 HETATM 7233 O O . HOH K 7 . ? 1.645 60.249 21.492 1.00 59.47 ? 2329 HOH B O 1 HETATM 7234 O O . HOH K 7 . ? 14.471 -1.204 3.589 1.00 65.69 ? 2330 HOH B O 1 HETATM 7235 O O . HOH K 7 . ? -6.369 -8.757 26.663 1.00 68.28 ? 2331 HOH B O 1 HETATM 7236 O O . HOH K 7 . ? 32.223 31.570 11.417 1.00 54.13 ? 2332 HOH B O 1 HETATM 7237 O O . HOH K 7 . ? 17.819 -25.607 28.641 1.00 44.64 ? 2333 HOH B O 1 HETATM 7238 O O . HOH K 7 . ? 7.523 51.760 3.779 1.00 50.52 ? 2334 HOH B O 1 HETATM 7239 O O . HOH K 7 . ? 28.559 31.979 10.261 1.00 58.97 ? 2335 HOH B O 1 HETATM 7240 O O . HOH K 7 . ? 8.025 12.538 17.348 1.00 45.68 ? 2337 HOH B O 1 HETATM 7241 O O . HOH K 7 . ? 26.083 10.950 23.056 1.00 70.92 ? 2338 HOH B O 1 HETATM 7242 O O . HOH K 7 . ? -13.346 0.663 29.458 1.00 56.69 ? 2340 HOH B O 1 HETATM 7243 O O . HOH K 7 . ? 36.504 31.129 42.747 1.00 69.33 ? 2341 HOH B O 1 HETATM 7244 O O . HOH K 7 . ? 39.284 41.453 2.289 1.00 62.44 ? 2342 HOH B O 1 HETATM 7245 O O . HOH K 7 . ? 43.609 52.658 15.013 1.00 61.46 ? 2345 HOH B O 1 HETATM 7246 O O . HOH K 7 . ? 41.030 35.643 14.567 1.00 86.65 ? 2346 HOH B O 1 HETATM 7247 O O . HOH K 7 . ? 32.418 23.041 36.068 1.00 67.21 ? 2347 HOH B O 1 HETATM 7248 O O . HOH K 7 . ? 51.585 45.146 14.198 1.00 73.21 ? 2349 HOH B O 1 HETATM 7249 O O . HOH K 7 . ? 10.183 40.075 12.208 1.00 54.83 ? 2351 HOH B O 1 HETATM 7250 O O . HOH K 7 . ? 2.340 16.156 2.888 1.00 84.03 ? 2352 HOH B O 1 HETATM 7251 O O . HOH K 7 . ? 5.061 18.156 17.224 1.00 80.19 ? 2353 HOH B O 1 HETATM 7252 O O . HOH K 7 . ? 34.964 10.440 -9.371 1.00 73.72 ? 2355 HOH B O 1 HETATM 7253 O O . HOH K 7 . ? 28.672 21.049 28.366 1.00 71.63 ? 2356 HOH B O 1 HETATM 7254 O O . HOH K 7 . ? 40.248 38.850 14.593 1.00 80.70 ? 2358 HOH B O 1 HETATM 7255 O O . HOH K 7 . ? 17.676 34.339 11.377 1.00 57.52 ? 2360 HOH B O 1 HETATM 7256 O O . HOH K 7 . ? 31.298 24.736 28.337 1.00 61.08 ? 2361 HOH B O 1 HETATM 7257 O O . HOH K 7 . ? 32.063 59.836 21.961 1.00 73.57 ? 2362 HOH B O 1 HETATM 7258 O O . HOH K 7 . ? 1.974 36.837 15.967 1.00 60.12 ? 2364 HOH B O 1 HETATM 7259 O O . HOH K 7 . ? -3.731 42.067 23.883 1.00 65.44 ? 2365 HOH B O 1 HETATM 7260 O O . HOH K 7 . ? 17.661 -21.368 34.414 1.00 49.91 ? 2366 HOH B O 1 HETATM 7261 O O . HOH K 7 . ? 5.560 52.071 10.642 1.00 62.56 ? 2367 HOH B O 1 HETATM 7262 O O . HOH K 7 . ? 41.317 37.571 9.935 1.00 43.09 ? 2368 HOH B O 1 HETATM 7263 O O . HOH K 7 . ? 19.106 -4.396 1.409 1.00 63.64 ? 2370 HOH B O 1 HETATM 7264 O O . HOH K 7 . ? -1.570 -14.754 36.300 1.00 74.85 ? 2371 HOH B O 1 HETATM 7265 O O . HOH K 7 . ? 8.753 40.926 9.845 1.00 72.06 ? 2372 HOH B O 1 HETATM 7266 O O . HOH K 7 . ? -0.360 45.582 19.867 1.00 54.34 ? 2373 HOH B O 1 HETATM 7267 O O . HOH K 7 . ? 35.308 59.194 11.356 1.00 62.49 ? 2374 HOH B O 1 HETATM 7268 O O . HOH K 7 . ? 17.519 13.204 41.234 1.00 81.15 ? 2375 HOH B O 1 HETATM 7269 O O . HOH K 7 . ? -2.587 4.964 22.973 1.00 73.14 ? 2376 HOH B O 1 HETATM 7270 O O . HOH K 7 . ? 3.802 22.066 16.966 1.00 61.05 ? 2377 HOH B O 1 HETATM 7271 O O . HOH K 7 . ? 26.310 28.567 38.240 1.00 56.99 ? 2378 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 ALA 1 1 1 ALA ALA A . n A 1 2 LYS 2 2 2 LYS LYS A . n A 1 3 LEU 3 3 3 LEU LEU A . n A 1 4 ARG 4 4 4 ARG ARG A . n A 1 5 GLN 5 5 5 GLN GLN A . n A 1 6 PHE 6 6 6 PHE PHE A . n A 1 7 TYR 7 7 7 TYR TYR A . n A 1 8 VAL 8 8 8 VAL VAL A . n A 1 9 ALA 9 9 9 ALA ALA A . n A 1 10 ALA 10 10 10 ALA ALA A . n A 1 11 GLN 11 11 11 GLN GLN A . n A 1 12 SER 12 12 12 SER SER A . n A 1 13 ILE 13 13 13 ILE ILE A . n A 1 14 ARG 14 14 14 ARG ARG A . n A 1 15 TRP 15 15 15 TRP TRP A . n A 1 16 ASN 16 16 16 ASN ASN A . n A 1 17 TYR 17 17 ? ? ? A . n A 1 18 ARG 18 18 ? ? ? A . n A 1 19 PRO 19 19 ? ? ? A . n A 1 20 GLU 20 20 ? ? ? A . n A 1 21 SER 21 21 ? ? ? A . n A 1 22 THR 22 22 ? ? ? A . n A 1 23 HIS 23 23 ? ? ? A . n A 1 24 LEU 24 24 ? ? ? A . n A 1 25 SER 25 25 ? ? ? A . n A 1 26 SER 26 26 ? ? ? A . n A 1 27 LYS 27 27 ? ? ? A . n A 1 28 PRO 28 28 ? ? ? A . n A 1 29 PHE 29 29 ? ? ? A . n A 1 30 GLU 30 30 ? ? ? A . n A 1 31 THR 31 31 31 THR THR A . n A 1 32 SER 32 32 32 SER SER A . n A 1 33 PHE 33 33 33 PHE PHE A . n A 1 34 LYS 34 34 34 LYS LYS A . n A 1 35 LYS 35 35 35 LYS LYS A . n A 1 36 ILE 36 36 36 ILE ILE A . n A 1 37 VAL 37 37 37 VAL VAL A . n A 1 38 TYR 38 38 38 TYR TYR A . n A 1 39 ARG 39 39 39 ARG ARG A . n A 1 40 GLU 40 40 40 GLU GLU A . n A 1 41 TYR 41 41 41 TYR TYR A . n A 1 42 GLU 42 42 42 GLU GLU A . n A 1 43 ALA 43 43 43 ALA ALA A . n A 1 44 TYR 44 44 44 TYR TYR A . n A 1 45 PHE 45 45 45 PHE PHE A . n A 1 46 GLN 46 46 46 GLN GLN A . n A 1 47 LYS 47 47 47 LYS LYS A . n A 1 48 GLU 48 48 48 GLU GLU A . n A 1 49 LYS 49 49 49 LYS LYS A . n A 1 50 PRO 50 50 50 PRO PRO A . n A 1 51 GLN 51 51 51 GLN GLN A . n A 1 52 SER 52 52 52 SER SER A . n A 1 53 ARG 53 53 53 ARG ARG A . n A 1 54 THR 54 54 54 THR THR A . n A 1 55 SER 55 55 55 SER SER A . n A 1 56 GLY 56 56 56 GLY GLY A . n A 1 57 LEU 57 57 57 LEU LEU A . n A 1 58 LEU 58 58 58 LEU LEU A . n A 1 59 GLY 59 59 59 GLY GLY A . n A 1 60 PRO 60 60 60 PRO PRO A . n A 1 61 THR 61 61 61 THR THR A . n A 1 62 LEU 62 62 62 LEU LEU A . n A 1 63 TYR 63 63 63 TYR TYR A . n A 1 64 ALA 64 64 64 ALA ALA A . n A 1 65 GLU 65 65 65 GLU GLU A . n A 1 66 VAL 66 66 66 VAL VAL A . n A 1 67 GLY 67 67 67 GLY GLY A . n A 1 68 ASP 68 68 68 ASP ASP A . n A 1 69 ILE 69 69 69 ILE ILE A . n A 1 70 MET 70 70 70 MET MET A . n A 1 71 LYS 71 71 71 LYS LYS A . n A 1 72 VAL 72 72 72 VAL VAL A . n A 1 73 HIS 73 73 73 HIS HIS A . n A 1 74 PHE 74 74 74 PHE PHE A . n A 1 75 LYS 75 75 75 LYS LYS A . n A 1 76 ASN 76 76 76 ASN ASN A . n A 1 77 LYS 77 77 77 LYS LYS A . n A 1 78 ALA 78 78 78 ALA ALA A . n A 1 79 HIS 79 79 79 HIS HIS A . n A 1 80 LYS 80 80 80 LYS LYS A . n A 1 81 PRO 81 81 81 PRO PRO A . n A 1 82 LEU 82 82 82 LEU LEU A . n A 1 83 SER 83 83 83 SER SER A . n A 1 84 ILE 84 84 84 ILE ILE A . n A 1 85 HIS 85 85 85 HIS HIS A . n A 1 86 ALA 86 86 86 ALA ALA A . n A 1 87 GLN 87 87 87 GLN GLN A . n A 1 88 GLY 88 88 88 GLY GLY A . n A 1 89 ILE 89 89 89 ILE ILE A . n A 1 90 LYS 90 90 90 LYS LYS A . n A 1 91 TYR 91 91 91 TYR TYR A . n A 1 92 SER 92 92 92 SER SER A . n A 1 93 LYS 93 93 93 LYS LYS A . n A 1 94 PHE 94 94 94 PHE PHE A . n A 1 95 SER 95 95 95 SER SER A . n A 1 96 GLU 96 96 96 GLU GLU A . n A 1 97 GLY 97 97 97 GLY GLY A . n A 1 98 ALA 98 98 98 ALA ALA A . n A 1 99 SER 99 99 99 SER SER A . n A 1 100 TYR 100 100 100 TYR TYR A . n A 1 101 SER 101 101 101 SER SER A . n A 1 102 ASP 102 102 102 ASP ASP A . n A 1 103 HIS 103 103 103 HIS HIS A . n A 1 104 THR 104 104 104 THR THR A . n A 1 105 LEU 105 105 105 LEU LEU A . n A 1 106 PRO 106 106 106 PRO PRO A . n A 1 107 MET 107 107 107 MET MET A . n A 1 108 GLU 108 108 108 GLU GLU A . n A 1 109 LYS 109 109 109 LYS LYS A . n A 1 110 MET 110 110 110 MET MET A . n A 1 111 ASP 111 111 111 ASP ASP A . n A 1 112 ASP 112 112 112 ASP ASP A . n A 1 113 ALA 113 113 113 ALA ALA A . n A 1 114 VAL 114 114 114 VAL VAL A . n A 1 115 ALA 115 115 115 ALA ALA A . n A 1 116 PRO 116 116 116 PRO PRO A . n A 1 117 GLY 117 117 117 GLY GLY A . n A 1 118 GLN 118 118 118 GLN GLN A . n A 1 119 GLU 119 119 119 GLU GLU A . n A 1 120 TYR 120 120 120 TYR TYR A . n A 1 121 THR 121 121 121 THR THR A . n A 1 122 TYR 122 122 122 TYR TYR A . n A 1 123 GLU 123 123 123 GLU GLU A . n A 1 124 TRP 124 124 124 TRP TRP A . n A 1 125 ILE 125 125 125 ILE ILE A . n A 1 126 ILE 126 126 126 ILE ILE A . n A 1 127 SER 127 127 127 SER SER A . n A 1 128 GLU 128 128 128 GLU GLU A . n A 1 129 HIS 129 129 129 HIS HIS A . n A 1 130 SER 130 130 130 SER SER A . n A 1 131 GLY 131 131 131 GLY GLY A . n A 1 132 PRO 132 132 132 PRO PRO A . n A 1 133 THR 133 133 133 THR THR A . n A 1 134 HIS 134 134 134 HIS HIS A . n A 1 135 ASP 135 135 135 ASP ASP A . n A 1 136 ASP 136 136 136 ASP ASP A . n A 1 137 PRO 137 137 137 PRO PRO A . n A 1 138 PRO 138 138 138 PRO PRO A . n A 1 139 CYS 139 139 139 CYS CYS A . n A 1 140 LEU 140 140 140 LEU LEU A . n A 1 141 THR 141 141 141 THR THR A . n A 1 142 HIS 142 142 142 HIS HIS A . n A 1 143 ILE 143 143 143 ILE ILE A . n A 1 144 TYR 144 144 144 TYR TYR A . n A 1 145 TYR 145 145 145 TYR TYR 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 VAL 148 148 148 VAL VAL A . n A 1 149 ASN 149 149 149 ASN ASN A . n A 1 150 LEU 150 150 150 LEU LEU A . n A 1 151 VAL 151 151 151 VAL VAL A . n A 1 152 GLU 152 152 152 GLU GLU A . n A 1 153 ASP 153 153 153 ASP ASP A . n A 1 154 PHE 154 154 154 PHE PHE A . n A 1 155 ASN 155 155 155 ASN ASN A . n A 1 156 SER 156 156 156 SER SER A . n A 1 157 GLY 157 157 157 GLY GLY A . n A 1 158 LEU 158 158 158 LEU LEU A . n A 1 159 ILE 159 159 159 ILE ILE A . n A 1 160 GLY 160 160 160 GLY GLY A . n A 1 161 PRO 161 161 161 PRO PRO A . n A 1 162 LEU 162 162 162 LEU LEU A . n A 1 163 LEU 163 163 163 LEU LEU A . n A 1 164 ILE 164 164 164 ILE ILE A . n A 1 165 CYS 165 165 165 CYS CYS A . n A 1 166 LYS 166 166 166 LYS LYS A . n A 1 167 LYS 167 167 167 LYS LYS A . n A 1 168 GLY 168 168 168 GLY GLY A . n A 1 169 THR 169 169 169 THR THR A . n A 1 170 LEU 170 170 170 LEU LEU A . n A 1 171 THR 171 171 171 THR THR A . n A 1 172 GLU 172 172 172 GLU GLU A . n A 1 173 ASP 173 173 173 ASP ASP A . n A 1 174 GLY 174 174 174 GLY GLY A . n A 1 175 THR 175 175 175 THR THR A . n A 1 176 GLN 176 176 176 GLN GLN A . n A 1 177 LYS 177 177 177 LYS LYS A . n A 1 178 MET 178 178 178 MET MET A . n A 1 179 PHE 179 179 179 PHE PHE A . n A 1 180 GLU 180 180 180 GLU GLU A . n A 1 181 LYS 181 181 181 LYS LYS A . n A 1 182 GLN 182 182 182 GLN GLN A . n A 1 183 HIS 183 183 183 HIS HIS A . n A 1 184 VAL 184 184 184 VAL VAL A . n A 1 185 LEU 185 185 185 LEU LEU A . n A 1 186 MET 186 186 186 MET MET A . n A 1 187 PHE 187 187 187 PHE PHE A . n A 1 188 ALA 188 188 188 ALA ALA A . n A 1 189 VAL 189 189 189 VAL VAL A . n A 1 190 PHE 190 190 190 PHE PHE A . n A 1 191 ASP 191 191 191 ASP ASP A . n A 1 192 GLU 192 192 192 GLU GLU A . n A 1 193 SER 193 193 193 SER SER A . n A 1 194 LYS 194 194 194 LYS LYS A . n A 1 195 SER 195 195 195 SER SER A . n A 1 196 TRP 196 196 196 TRP TRP A . n A 1 197 ASN 197 197 197 ASN ASN A . n A 1 198 GLN 198 198 198 GLN GLN A . n A 1 199 THR 199 199 199 THR THR A . n A 1 200 SER 200 200 200 SER SER A . n A 1 201 SER 201 201 201 SER SER A . n A 1 202 LEU 202 202 202 LEU LEU A . n A 1 203 MET 203 203 203 MET MET A . n A 1 204 TYR 204 204 204 TYR TYR A . n A 1 205 THR 205 205 205 THR THR A . n A 1 206 VAL 206 206 206 VAL VAL A . n A 1 207 ASN 207 207 207 ASN ASN A . n A 1 208 GLY 208 208 208 GLY GLY A . n A 1 209 TYR 209 209 209 TYR TYR A . n A 1 210 VAL 210 210 210 VAL VAL A . n A 1 211 ASN 211 211 211 ASN ASN A . n A 1 212 GLY 212 212 212 GLY GLY A . n A 1 213 THR 213 213 213 THR THR A . n A 1 214 MET 214 214 214 MET MET A . n A 1 215 PRO 215 215 215 PRO PRO A . n A 1 216 ASP 216 216 216 ASP ASP A . n A 1 217 ILE 217 217 217 ILE ILE A . n A 1 218 THR 218 218 218 THR THR A . n A 1 219 VAL 219 219 219 VAL VAL A . n A 1 220 CYS 220 220 220 CYS CYS A . n A 1 221 ALA 221 221 221 ALA ALA A . n A 1 222 HIS 222 222 ? ? ? A . n A 1 223 ASP 223 223 ? ? ? A . n A 1 224 HIS 224 224 ? ? ? A . n A 1 225 ILE 225 225 ? ? ? A . n A 1 226 SER 226 226 ? ? ? A . n A 1 227 TRP 227 227 ? ? ? A . n A 1 228 HIS 228 228 228 HIS HIS A . n A 1 229 LEU 229 229 229 LEU LEU A . n A 1 230 ILE 230 230 230 ILE ILE A . n A 1 231 GLY 231 231 231 GLY GLY A . n A 1 232 MET 232 232 232 MET MET A . n A 1 233 SER 233 233 233 SER SER A . n A 1 234 SER 234 234 234 SER SER A . n A 1 235 GLY 235 235 235 GLY GLY A . n A 1 236 PRO 236 236 236 PRO PRO A . n A 1 237 GLU 237 237 237 GLU GLU A . n A 1 238 LEU 238 238 238 LEU LEU A . n A 1 239 PHE 239 239 239 PHE PHE A . n A 1 240 SER 240 240 240 SER SER A . n A 1 241 ILE 241 241 241 ILE ILE A . n A 1 242 HIS 242 242 242 HIS HIS A . n A 1 243 PHE 243 243 243 PHE PHE A . n A 1 244 ASN 244 244 244 ASN ASN A . n A 1 245 GLY 245 245 245 GLY GLY A . n A 1 246 GLN 246 246 246 GLN GLN A . n A 1 247 VAL 247 247 247 VAL VAL A . n A 1 248 LEU 248 248 248 LEU LEU A . n A 1 249 GLU 249 249 249 GLU GLU A . n A 1 250 GLN 250 250 250 GLN GLN A . n A 1 251 ASN 251 251 251 ASN ASN A . n A 1 252 HIS 252 252 252 HIS HIS A . n A 1 253 HIS 253 253 253 HIS HIS A . n A 1 254 LYS 254 254 254 LYS LYS A . n A 1 255 ILE 255 255 255 ILE ILE A . n A 1 256 SER 256 256 256 SER SER A . n A 1 257 ALA 257 257 257 ALA ALA A . n A 1 258 ILE 258 258 258 ILE ILE A . n A 1 259 THR 259 259 259 THR THR A . n A 1 260 LEU 260 260 260 LEU LEU A . n A 1 261 VAL 261 261 261 VAL VAL A . n A 1 262 SER 262 262 262 SER SER A . n A 1 263 ALA 263 263 263 ALA ALA A . n A 1 264 THR 264 264 264 THR THR A . n A 1 265 SER 265 265 265 SER SER A . n A 1 266 THR 266 266 266 THR THR A . n A 1 267 THR 267 267 267 THR THR A . n A 1 268 ALA 268 268 ? ? ? A . n A 1 269 ASN 269 269 ? ? ? A . n A 1 270 MET 270 270 ? ? ? A . n A 1 271 THR 271 271 ? ? ? A . n A 1 272 VAL 272 272 ? ? ? A . n A 1 273 SER 273 273 ? ? ? A . n A 1 274 PRO 274 274 ? ? ? A . n A 1 275 GLU 275 275 ? ? ? A . n A 1 276 GLY 276 276 276 GLY GLY A . n A 1 277 ARG 277 277 277 ARG ARG A . n A 1 278 TRP 278 278 278 TRP TRP A . n A 1 279 THR 279 279 279 THR THR A . n A 1 280 ILE 280 280 280 ILE ILE A . n A 1 281 ALA 281 281 281 ALA ALA A . n A 1 282 SER 282 282 282 SER SER A . n A 1 283 LEU 283 283 283 LEU LEU A . n A 1 284 ILE 284 284 284 ILE ILE A . n A 1 285 PRO 285 285 285 PRO PRO A . n A 1 286 ARG 286 286 286 ARG ARG A . n A 1 287 HIS 287 287 287 HIS HIS A . n A 1 288 PHE 288 288 288 PHE PHE A . n A 1 289 GLN 289 289 289 GLN GLN A . n A 1 290 ALA 290 290 290 ALA ALA A . n A 1 291 GLY 291 291 291 GLY GLY A . n A 1 292 MET 292 292 292 MET MET A . n A 1 293 GLN 293 293 293 GLN GLN A . n A 1 294 ALA 294 294 294 ALA ALA A . n A 1 295 TYR 295 295 295 TYR TYR A . n A 1 296 ILE 296 296 296 ILE ILE A . n A 1 297 ASP 297 297 ? ? ? A . n A 1 298 ILE 298 298 ? ? ? A . n A 1 299 LYS 299 299 ? ? ? A . n A 1 300 ASN 300 300 ? ? ? A . n A 1 301 CYS 301 301 ? ? ? A . n A 1 302 ALA 302 302 ? ? ? A . n A 1 303 LYS 303 303 ? ? ? A . n A 1 304 LYS 304 304 ? ? ? A . n A 1 305 THR 305 305 ? ? ? A . n A 1 306 ARG 306 306 ? ? ? A . n B 2 1 SER 1 1537 ? ? ? B . n B 2 2 ASN 2 1538 1538 ASN ASN B . n B 2 3 THR 3 1539 1539 THR THR B . n B 2 4 GLY 4 1540 1540 GLY GLY B . n B 2 5 ASN 5 1541 1541 ASN ASN B . n B 2 6 ARG 6 1542 1542 ARG ARG B . n B 2 7 LYS 7 1543 1543 LYS LYS B . n B 2 8 TYR 8 1544 1544 TYR TYR B . n B 2 9 TYR 9 1545 1545 TYR TYR B . n B 2 10 TYR 10 1546 1546 TYR TYR B . n B 2 11 ILE 11 1547 1547 ILE ILE B . n B 2 12 ALA 12 1548 1548 ALA ALA B . n B 2 13 ALA 13 1549 1549 ALA ALA B . n B 2 14 GLU 14 1550 1550 GLU GLU B . n B 2 15 GLU 15 1551 1551 GLU GLU B . n B 2 16 ILE 16 1552 1552 ILE ILE B . n B 2 17 SER 17 1553 1553 SER SER B . n B 2 18 TRP 18 1554 1554 TRP TRP B . n B 2 19 ASP 19 1555 1555 ASP ASP B . n B 2 20 TYR 20 1556 1556 TYR TYR B . n B 2 21 SER 21 1557 1557 SER SER B . n B 2 22 LYS 22 1558 1558 LYS LYS B . n B 2 23 PHE 23 1559 1559 PHE PHE B . n B 2 24 VAL 24 1560 1560 VAL VAL B . n B 2 25 GLN 25 1561 ? ? ? B . n B 2 26 SER 26 1562 ? ? ? B . n B 2 27 ASP 27 1563 ? ? ? B . n B 2 28 ASP 28 1564 ? ? ? B . n B 2 29 VAL 29 1565 ? ? ? B . n B 2 30 ASP 30 1566 ? ? ? B . n B 2 31 TYR 31 1567 ? ? ? B . n B 2 32 VAL 32 1568 ? ? ? B . n B 2 33 PRO 33 1569 1569 PRO PRO B . n B 2 34 GLU 34 1570 1570 GLU GLU B . n B 2 35 ASP 35 1571 1571 ASP ASP B . n B 2 36 THR 36 1572 1572 THR THR B . n B 2 37 VAL 37 1573 1573 VAL VAL B . n B 2 38 TYR 38 1574 1574 TYR TYR B . n B 2 39 LYS 39 1575 1575 LYS LYS B . n B 2 40 LYS 40 1576 1576 LYS LYS B . n B 2 41 VAL 41 1577 1577 VAL VAL B . n B 2 42 VAL 42 1578 1578 VAL VAL B . n B 2 43 PHE 43 1579 1579 PHE PHE B . n B 2 44 ARG 44 1580 1580 ARG ARG B . n B 2 45 LYS 45 1581 1581 LYS LYS B . n B 2 46 TYR 46 1582 1582 TYR TYR B . n B 2 47 LEU 47 1583 1583 LEU LEU B . n B 2 48 ASP 48 1584 1584 ASP ASP B . n B 2 49 SER 49 1585 1585 SER SER B . n B 2 50 THR 50 1586 1586 THR THR B . n B 2 51 PHE 51 1587 1587 PHE PHE B . n B 2 52 THR 52 1588 1588 THR THR B . n B 2 53 LYS 53 1589 1589 LYS LYS B . n B 2 54 LEU 54 1590 1590 LEU LEU B . n B 2 55 ASP 55 1591 1591 ASP ASP B . n B 2 56 PRO 56 1592 1592 PRO PRO B . n B 2 57 GLN 57 1593 1593 GLN GLN B . n B 2 58 GLY 58 1594 1594 GLY GLY B . n B 2 59 GLU 59 1595 1595 GLU GLU B . n B 2 60 TYR 60 1596 1596 TYR TYR B . n B 2 61 GLU 61 1597 1597 GLU GLU B . n B 2 62 GLU 62 1598 1598 GLU GLU B . n B 2 63 HIS 63 1599 1599 HIS HIS B . n B 2 64 LEU 64 1600 1600 LEU LEU B . n B 2 65 GLY 65 1601 1601 GLY GLY B . n B 2 66 ILE 66 1602 1602 ILE ILE B . n B 2 67 LEU 67 1603 1603 LEU LEU B . n B 2 68 GLY 68 1604 1604 GLY GLY B . n B 2 69 PRO 69 1605 1605 PRO PRO B . n B 2 70 VAL 70 1606 1606 VAL VAL B . n B 2 71 ILE 71 1607 1607 ILE ILE B . n B 2 72 ARG 72 1608 1608 ARG ARG B . n B 2 73 ALA 73 1609 1609 ALA ALA B . n B 2 74 GLU 74 1610 1610 GLU GLU B . n B 2 75 VAL 75 1611 1611 VAL VAL B . n B 2 76 ASP 76 1612 1612 ASP ASP B . n B 2 77 ASP 77 1613 1613 ASP ASP B . n B 2 78 VAL 78 1614 1614 VAL VAL B . n B 2 79 ILE 79 1615 1615 ILE ILE B . n B 2 80 GLN 80 1616 1616 GLN GLN B . n B 2 81 VAL 81 1617 1617 VAL VAL B . n B 2 82 ARG 82 1618 1618 ARG ARG B . n B 2 83 PHE 83 1619 1619 PHE PHE B . n B 2 84 LYS 84 1620 1620 LYS LYS B . n B 2 85 ASN 85 1621 1621 ASN ASN B . n B 2 86 LEU 86 1622 1622 LEU LEU B . n B 2 87 ALA 87 1623 1623 ALA ALA B . n B 2 88 SER 88 1624 1624 SER SER B . n B 2 89 ARG 89 1625 1625 ARG ARG B . n B 2 90 PRO 90 1626 1626 PRO PRO B . n B 2 91 TYR 91 1627 1627 TYR TYR B . n B 2 92 SER 92 1628 1628 SER SER B . n B 2 93 LEU 93 1629 1629 LEU LEU B . n B 2 94 HIS 94 1630 1630 HIS HIS B . n B 2 95 ALA 95 1631 1631 ALA ALA B . n B 2 96 HIS 96 1632 1632 HIS HIS B . n B 2 97 GLY 97 1633 1633 GLY GLY B . n B 2 98 LEU 98 1634 1634 LEU LEU B . n B 2 99 SER 99 1635 1635 SER SER B . n B 2 100 TYR 100 1636 ? ? ? B . n B 2 101 GLU 101 1637 ? ? ? B . n B 2 102 LYS 102 1638 ? ? ? B . n B 2 103 SER 103 1639 ? ? ? B . n B 2 104 SER 104 1640 ? ? ? B . n B 2 105 GLU 105 1641 ? ? ? B . n B 2 106 GLY 106 1642 ? ? ? B . n B 2 107 LYS 107 1643 ? ? ? B . n B 2 108 THR 108 1644 ? ? ? B . n B 2 109 TYR 109 1645 ? ? ? B . n B 2 110 GLU 110 1646 ? ? ? B . n B 2 111 ASP 111 1647 ? ? ? B . n B 2 112 ASP 112 1648 ? ? ? B . n B 2 113 SER 113 1649 ? ? ? B . n B 2 114 PRO 114 1650 ? ? ? B . n B 2 115 GLU 115 1651 ? ? ? B . n B 2 116 TRP 116 1652 ? ? ? B . n B 2 117 PHE 117 1653 ? ? ? B . n B 2 118 LYS 118 1654 ? ? ? B . n B 2 119 GLU 119 1655 ? ? ? B . n B 2 120 ASP 120 1656 ? ? ? B . n B 2 121 ASN 121 1657 1657 ASN ASN B . n B 2 122 ALA 122 1658 1658 ALA ALA B . n B 2 123 ILE 123 1659 1659 ILE ILE B . n B 2 124 GLN 124 1660 1660 GLN GLN B . n B 2 125 PRO 125 1661 1661 PRO PRO B . n B 2 126 ASN 126 1662 1662 ASN ASN B . n B 2 127 LYS 127 1663 1663 LYS LYS B . n B 2 128 THR 128 1664 1664 THR THR B . n B 2 129 TYR 129 1665 1665 TYR TYR B . n B 2 130 THR 130 1666 1666 THR THR B . n B 2 131 TYR 131 1667 1667 TYR TYR B . n B 2 132 VAL 132 1668 1668 VAL VAL B . n B 2 133 TRP 133 1669 1669 TRP TRP B . n B 2 134 HIS 134 1670 1670 HIS HIS B . n B 2 135 ALA 135 1671 1671 ALA ALA B . n B 2 136 THR 136 1672 1672 THR THR B . n B 2 137 THR 137 1673 1673 THR THR B . n B 2 138 ARG 138 1674 1674 ARG ARG B . n B 2 139 SER 139 1675 1675 SER SER B . n B 2 140 GLY 140 1676 1676 GLY GLY B . n B 2 141 PRO 141 1677 1677 PRO PRO B . n B 2 142 GLU 142 1678 1678 GLU GLU B . n B 2 143 ASN 143 1679 1679 ASN ASN B . n B 2 144 PRO 144 1680 1680 PRO PRO B . n B 2 145 GLY 145 1681 1681 GLY GLY B . n B 2 146 SER 146 1682 1682 SER SER B . n B 2 147 ALA 147 1683 1683 ALA ALA B . n B 2 148 CYS 148 1684 1684 CYS CYS B . n B 2 149 ARG 149 1685 1685 ARG ARG B . n B 2 150 ALA 150 1686 1686 ALA ALA B . n B 2 151 TRP 151 1687 1687 TRP TRP B . n B 2 152 ALA 152 1688 1688 ALA ALA B . n B 2 153 TYR 153 1689 1689 TYR TYR B . n B 2 154 TYR 154 1690 1690 TYR TYR B . n B 2 155 SER 155 1691 1691 SER SER B . n B 2 156 ALA 156 1692 1692 ALA ALA B . n B 2 157 VAL 157 1693 1693 VAL VAL B . n B 2 158 ASN 158 1694 1694 ASN ASN B . n B 2 159 PRO 159 1695 1695 PRO PRO B . n B 2 160 GLU 160 1696 1696 GLU GLU B . n B 2 161 LYS 161 1697 1697 LYS LYS B . n B 2 162 ASP 162 1698 1698 ASP ASP B . n B 2 163 ILE 163 1699 1699 ILE ILE B . n B 2 164 HIS 164 1700 1700 HIS HIS B . n B 2 165 SER 165 1701 1701 SER SER B . n B 2 166 GLY 166 1702 1702 GLY GLY B . n B 2 167 LEU 167 1703 1703 LEU LEU B . n B 2 168 ILE 168 1704 1704 ILE ILE B . n B 2 169 GLY 169 1705 1705 GLY GLY B . n B 2 170 PRO 170 1706 1706 PRO PRO B . n B 2 171 LEU 171 1707 1707 LEU LEU B . n B 2 172 LEU 172 1708 1708 LEU LEU B . n B 2 173 ILE 173 1709 1709 ILE ILE B . n B 2 174 CYS 174 1710 1710 CYS CYS B . n B 2 175 ARG 175 1711 1711 ARG ARG B . n B 2 176 LYS 176 1712 1712 LYS LYS B . n B 2 177 GLY 177 1713 1713 GLY GLY B . n B 2 178 THR 178 1714 1714 THR THR B . n B 2 179 LEU 179 1715 1715 LEU LEU B . n B 2 180 ASP 180 1716 1716 ASP ASP B . n B 2 181 LYS 181 1717 1717 LYS LYS B . n B 2 182 GLU 182 1718 1718 GLU GLU B . n B 2 183 THR 183 1719 1719 THR THR B . n B 2 184 ASN 184 1720 1720 ASN ASN B . n B 2 185 MET 185 1721 1721 MET MET B . n B 2 186 PRO 186 1722 1722 PRO PRO B . n B 2 187 VAL 187 1723 1723 VAL VAL B . n B 2 188 ASP 188 1724 1724 ASP ASP B . n B 2 189 MET 189 1725 1725 MET MET B . n B 2 190 ARG 190 1726 1726 ARG ARG B . n B 2 191 GLU 191 1727 1727 GLU GLU B . n B 2 192 PHE 192 1728 1728 PHE PHE B . n B 2 193 VAL 193 1729 1729 VAL VAL B . n B 2 194 LEU 194 1730 1730 LEU LEU B . n B 2 195 LEU 195 1731 1731 LEU LEU B . n B 2 196 PHE 196 1732 1732 PHE PHE B . n B 2 197 MET 197 1733 1733 MET MET B . n B 2 198 VAL 198 1734 1734 VAL VAL B . n B 2 199 PHE 199 1735 1735 PHE PHE B . n B 2 200 ASP 200 1736 1736 ASP ASP B . n B 2 201 GLU 201 1737 1737 GLU GLU B . n B 2 202 LYS 202 1738 1738 LYS LYS B . n B 2 203 LYS 203 1739 1739 LYS LYS B . n B 2 204 SER 204 1740 1740 SER SER B . n B 2 205 TRP 205 1741 1741 TRP TRP B . n B 2 206 TYR 206 1742 1742 TYR TYR B . n B 2 207 TYR 207 1743 1743 TYR TYR B . n B 2 208 ASP 208 1744 1744 ASP ASP B . n B 2 209 LYS 209 1745 ? ? ? B . n B 2 210 LYS 210 1746 ? ? ? B . n B 2 211 PRO 211 1747 ? ? ? B . n B 2 212 THR 212 1748 ? ? ? B . n B 2 213 ARG 213 1749 ? ? ? B . n B 2 214 SER 214 1750 ? ? ? B . n B 2 215 TRP 215 1751 ? ? ? B . n B 2 216 ARG 216 1752 ? ? ? B . n B 2 217 ARG 217 1753 ? ? ? B . n B 2 218 ALA 218 1754 ? ? ? B . n B 2 219 SER 219 1755 ? ? ? B . n B 2 220 SER 220 1756 ? ? ? B . n B 2 221 GLU 221 1757 ? ? ? B . n B 2 222 VAL 222 1758 ? ? ? B . n B 2 223 LYS 223 1759 ? ? ? B . n B 2 224 ASN 224 1760 1760 ASN ASN B . n B 2 225 SER 225 1761 1761 SER SER B . n B 2 226 HIS 226 1762 1762 HIS HIS B . n B 2 227 GLU 227 1763 1763 GLU GLU B . n B 2 228 PHE 228 1764 1764 PHE PHE B . n B 2 229 HIS 229 1765 1765 HIS HIS B . n B 2 230 ALA 230 1766 1766 ALA ALA B . n B 2 231 ILE 231 1767 1767 ILE ILE B . n B 2 232 ASN 232 1768 1768 ASN ASN B . n B 2 233 GLY 233 1769 1769 GLY GLY B . n B 2 234 MET 234 1770 1770 MET MET B . n B 2 235 ILE 235 1771 1771 ILE ILE B . n B 2 236 TYR 236 1772 1772 TYR TYR B . n B 2 237 ASN 237 1773 1773 ASN ASN B . n B 2 238 LEU 238 1774 1774 LEU LEU B . n B 2 239 PRO 239 1775 1775 PRO PRO B . n B 2 240 GLY 240 1776 1776 GLY GLY B . n B 2 241 LEU 241 1777 1777 LEU LEU B . n B 2 242 ARG 242 1778 1778 ARG ARG B . n B 2 243 MET 243 1779 1779 MET MET B . n B 2 244 TYR 244 1780 1780 TYR TYR B . n B 2 245 GLU 245 1781 1781 GLU GLU B . n B 2 246 GLN 246 1782 1782 GLN GLN B . n B 2 247 GLU 247 1783 1783 GLU GLU B . n B 2 248 TRP 248 1784 1784 TRP TRP B . n B 2 249 VAL 249 1785 1785 VAL VAL B . n B 2 250 ARG 250 1786 1786 ARG ARG B . n B 2 251 LEU 251 1787 1787 LEU LEU B . n B 2 252 HIS 252 1788 1788 HIS HIS B . n B 2 253 LEU 253 1789 1789 LEU LEU B . n B 2 254 LEU 254 1790 1790 LEU LEU B . n B 2 255 ASN 255 1791 1791 ASN ASN B . n B 2 256 LEU 256 1792 1792 LEU LEU B . n B 2 257 GLY 257 1793 1793 GLY GLY B . n B 2 258 GLY 258 1794 1794 GLY GLY B . n B 2 259 SER 259 1795 1795 SER SER B . n B 2 260 ARG 260 1796 1796 ARG ARG B . n B 2 261 ASP 261 1797 1797 ASP ASP B . n B 2 262 ILE 262 1798 1798 ILE ILE B . n B 2 263 HIS 263 1799 1799 HIS HIS B . n B 2 264 VAL 264 1800 1800 VAL VAL B . n B 2 265 VAL 265 1801 1801 VAL VAL B . n B 2 266 HIS 266 1802 1802 HIS HIS B . n B 2 267 PHE 267 1803 1803 PHE PHE B . n B 2 268 HIS 268 1804 1804 HIS HIS B . n B 2 269 GLY 269 1805 1805 GLY GLY B . n B 2 270 GLN 270 1806 1806 GLN GLN B . n B 2 271 THR 271 1807 1807 THR THR B . n B 2 272 LEU 272 1808 1808 LEU LEU B . n B 2 273 LEU 273 1809 1809 LEU LEU B . n B 2 274 GLU 274 1810 1810 GLU GLU B . n B 2 275 ASN 275 1811 1811 ASN ASN B . n B 2 276 GLY 276 1812 1812 GLY GLY B . n B 2 277 THR 277 1813 1813 THR THR B . n B 2 278 GLN 278 1814 1814 GLN GLN B . n B 2 279 GLN 279 1815 1815 GLN GLN B . n B 2 280 HIS 280 1816 1816 HIS HIS B . n B 2 281 GLN 281 1817 1817 GLN GLN B . n B 2 282 LEU 282 1818 1818 LEU LEU B . n B 2 283 GLY 283 1819 1819 GLY GLY B . n B 2 284 VAL 284 1820 1820 VAL VAL B . n B 2 285 TRP 285 1821 1821 TRP TRP B . n B 2 286 PRO 286 1822 1822 PRO PRO B . n B 2 287 LEU 287 1823 1823 LEU LEU B . n B 2 288 LEU 288 1824 1824 LEU LEU B . n B 2 289 PRO 289 1825 1825 PRO PRO B . n B 2 290 GLY 290 1826 1826 GLY GLY B . n B 2 291 SER 291 1827 1827 SER SER B . n B 2 292 PHE 292 1828 1828 PHE PHE B . n B 2 293 LYS 293 1829 1829 LYS LYS B . n B 2 294 THR 294 1830 1830 THR THR B . n B 2 295 LEU 295 1831 1831 LEU LEU B . n B 2 296 GLU 296 1832 1832 GLU GLU B . n B 2 297 MET 297 1833 1833 MET MET B . n B 2 298 LYS 298 1834 1834 LYS LYS B . n B 2 299 ALA 299 1835 1835 ALA ALA B . n B 2 300 SER 300 1836 1836 SER SER B . n B 2 301 LYS 301 1837 1837 LYS LYS B . n B 2 302 PRO 302 1838 1838 PRO PRO B . n B 2 303 GLY 303 1839 1839 GLY GLY B . n B 2 304 TRP 304 1840 1840 TRP TRP B . n B 2 305 TRP 305 1841 1841 TRP TRP B . n B 2 306 LEU 306 1842 1842 LEU LEU B . n B 2 307 LEU 307 1843 1843 LEU LEU B . n B 2 308 ASP 308 1844 1844 ASP ASP B . n B 2 309 THR 309 1845 1845 THR THR B . n B 2 310 GLU 310 1846 1846 GLU GLU B . n B 2 311 VAL 311 1847 1847 VAL VAL B . n B 2 312 GLY 312 1848 1848 GLY GLY B . n B 2 313 GLU 313 1849 1849 GLU GLU B . n B 2 314 ILE 314 1850 1850 ILE ILE B . n B 2 315 GLN 315 1851 1851 GLN GLN B . n B 2 316 ARG 316 1852 1852 ARG ARG B . n B 2 317 ALA 317 1853 1853 ALA ALA B . n B 2 318 GLY 318 1854 1854 GLY GLY B . n B 2 319 MET 319 1855 1855 MET MET B . n B 2 320 GLN 320 1856 1856 GLN GLN B . n B 2 321 THR 321 1857 1857 THR THR B . n B 2 322 PRO 322 1858 1858 PRO PRO B . n B 2 323 PHE 323 1859 1859 PHE PHE B . n B 2 324 LEU 324 1860 1860 LEU LEU B . n B 2 325 ILE 325 1861 1861 ILE ILE B . n B 2 326 VAL 326 1862 1862 VAL VAL B . n B 2 327 ASP 327 1863 1863 ASP ASP B . n B 2 328 ARG 328 1864 1864 ARG ARG B . n B 2 329 GLU 329 1865 1865 GLU GLU B . n B 2 330 CYS 330 1866 1866 CYS CYS B . n B 2 331 LYS 331 1867 1867 LYS LYS B . n B 2 332 MET 332 1868 1868 MET MET B . n B 2 333 PRO 333 1869 1869 PRO PRO B . n B 2 334 MET 334 1870 1870 MET MET B . n B 2 335 GLY 335 1871 1871 GLY GLY B . n B 2 336 LEU 336 1872 1872 LEU LEU B . n B 2 337 SER 337 1873 1873 SER SER B . n B 2 338 THR 338 1874 1874 THR THR B . n B 2 339 GLY 339 1875 1875 GLY GLY B . n B 2 340 LEU 340 1876 1876 LEU LEU B . n B 2 341 ILE 341 1877 1877 ILE ILE B . n B 2 342 ALA 342 1878 1878 ALA ALA B . n B 2 343 ASP 343 1879 1879 ASP ASP B . n B 2 344 SER 344 1880 1880 SER SER B . n B 2 345 GLN 345 1881 1881 GLN GLN B . n B 2 346 ILE 346 1882 1882 ILE ILE B . n B 2 347 GLN 347 1883 1883 GLN GLN B . n B 2 348 ALA 348 1884 1884 ALA ALA B . n B 2 349 SER 349 1885 1885 SER SER B . n B 2 350 GLU 350 1886 1886 GLU GLU B . n B 2 351 PHE 351 1887 1887 PHE PHE B . n B 2 352 TRP 352 1888 1888 TRP TRP B . n B 2 353 GLY 353 1889 1889 GLY GLY B . n B 2 354 TYR 354 1890 1890 TYR TYR B . n B 2 355 TRP 355 1891 1891 TRP TRP B . n B 2 356 GLU 356 1892 1892 GLU GLU B . n B 2 357 PRO 357 1893 1893 PRO PRO B . n B 2 358 LYS 358 1894 1894 LYS LYS B . n B 2 359 LEU 359 1895 1895 LEU LEU B . n B 2 360 ALA 360 1896 1896 ALA ALA B . n B 2 361 ARG 361 1897 1897 ARG ARG B . n B 2 362 LEU 362 1898 1898 LEU LEU B . n B 2 363 ASN 363 1899 1899 ASN ASN B . n B 2 364 ASN 364 1900 1900 ASN ASN B . n B 2 365 GLY 365 1901 1901 GLY GLY B . n B 2 366 GLY 366 1902 1902 GLY GLY B . n B 2 367 SER 367 1903 1903 SER SER B . n B 2 368 TYR 368 1904 1904 TYR TYR B . n B 2 369 ASN 369 1905 1905 ASN ASN B . n B 2 370 ALA 370 1906 1906 ALA ALA B . n B 2 371 TRP 371 1907 1907 TRP TRP B . n B 2 372 ILE 372 1908 1908 ILE ILE B . n B 2 373 ALA 373 1909 1909 ALA ALA B . n B 2 374 GLU 374 1910 1910 GLU GLU B . n B 2 375 LYS 375 1911 1911 LYS LYS B . n B 2 376 LEU 376 1912 1912 LEU LEU B . n B 2 377 SER 377 1913 1913 SER SER B . n B 2 378 THR 378 1914 1914 THR THR B . n B 2 379 GLU 379 1915 1915 GLU GLU B . n B 2 380 PHE 380 1916 1916 PHE PHE B . n B 2 381 ASN 381 1917 1917 ASN ASN B . n B 2 382 PRO 382 1918 1918 PRO PRO B . n B 2 383 GLU 383 1919 1919 GLU GLU B . n B 2 384 PRO 384 1920 1920 PRO PRO B . n B 2 385 TRP 385 1921 1921 TRP TRP B . n B 2 386 ILE 386 1922 1922 ILE ILE B . n B 2 387 GLN 387 1923 1923 GLN GLN B . n B 2 388 VAL 388 1924 1924 VAL VAL B . n B 2 389 ASP 389 1925 1925 ASP ASP B . n B 2 390 MET 390 1926 1926 MET MET B . n B 2 391 GLN 391 1927 1927 GLN GLN B . n B 2 392 LYS 392 1928 1928 LYS LYS B . n B 2 393 GLU 393 1929 1929 GLU GLU B . n B 2 394 VAL 394 1930 1930 VAL VAL B . n B 2 395 LEU 395 1931 1931 LEU LEU B . n B 2 396 LEU 396 1932 1932 LEU LEU B . n B 2 397 THR 397 1933 1933 THR THR B . n B 2 398 GLY 398 1934 1934 GLY GLY B . n B 2 399 ILE 399 1935 1935 ILE ILE B . n B 2 400 GLN 400 1936 1936 GLN GLN B . n B 2 401 THR 401 1937 1937 THR THR B . n B 2 402 GLN 402 1938 1938 GLN GLN B . n B 2 403 GLY 403 1939 1939 GLY GLY B . n B 2 404 ALA 404 1940 1940 ALA ALA B . n B 2 405 LYS 405 1941 1941 LYS LYS B . n B 2 406 HIS 406 1942 1942 HIS HIS B . n B 2 407 TYR 407 1943 1943 TYR TYR B . n B 2 408 LEU 408 1944 1944 LEU LEU B . n B 2 409 LYS 409 1945 1945 LYS LYS B . n B 2 410 PRO 410 1946 1946 PRO PRO B . n B 2 411 TYR 411 1947 1947 TYR TYR B . n B 2 412 TYR 412 1948 1948 TYR TYR B . n B 2 413 THR 413 1949 1949 THR THR B . n B 2 414 THR 414 1950 1950 THR THR B . n B 2 415 GLU 415 1951 1951 GLU GLU B . n B 2 416 PHE 416 1952 1952 PHE PHE B . n B 2 417 CYS 417 1953 1953 CYS CYS B . n B 2 418 VAL 418 1954 1954 VAL VAL B . n B 2 419 ALA 419 1955 1955 ALA ALA B . n B 2 420 TYR 420 1956 1956 TYR TYR B . n B 2 421 SER 421 1957 1957 SER SER B . n B 2 422 LEU 422 1958 1958 LEU LEU B . n B 2 423 ASP 423 1959 1959 ASP ASP B . n B 2 424 ARG 424 1960 1960 ARG ARG B . n B 2 425 LYS 425 1961 1961 LYS LYS B . n B 2 426 ASN 426 1962 1962 ASN ASN B . n B 2 427 TRP 427 1963 1963 TRP TRP B . n B 2 428 ARG 428 1964 1964 ARG ARG B . n B 2 429 ILE 429 1965 1965 ILE ILE B . n B 2 430 PHE 430 1966 1966 PHE PHE B . n B 2 431 LYS 431 1967 1967 LYS LYS B . n B 2 432 GLY 432 1968 1968 GLY GLY B . n B 2 433 ASN 433 1969 1969 ASN ASN B . n B 2 434 SER 434 1970 1970 SER SER B . n B 2 435 THR 435 1971 1971 THR THR B . n B 2 436 ARG 436 1972 1972 ARG ARG B . n B 2 437 ASN 437 1973 1973 ASN ASN B . n B 2 438 VAL 438 1974 1974 VAL VAL B . n B 2 439 MET 439 1975 1975 MET MET B . n B 2 440 TYR 440 1976 1976 TYR TYR B . n B 2 441 PHE 441 1977 1977 PHE PHE B . n B 2 442 GLY 442 1978 1978 GLY GLY B . n B 2 443 GLY 443 1979 1979 GLY GLY B . n B 2 444 ASN 444 1980 1980 ASN ASN B . n B 2 445 SER 445 1981 1981 SER SER B . n B 2 446 ASP 446 1982 1982 ASP ASP B . n B 2 447 ALA 447 1983 1983 ALA ALA B . n B 2 448 SER 448 1984 1984 SER SER B . n B 2 449 THR 449 1985 1985 THR THR B . n B 2 450 ILE 450 1986 1986 ILE ILE B . n B 2 451 LYS 451 1987 1987 LYS LYS B . n B 2 452 GLU 452 1988 1988 GLU GLU B . n B 2 453 ASN 453 1989 1989 ASN ASN B . n B 2 454 GLN 454 1990 1990 GLN GLN B . n B 2 455 ILE 455 1991 1991 ILE ILE B . n B 2 456 ASP 456 1992 1992 ASP ASP B . n B 2 457 PRO 457 1993 1993 PRO PRO B . n B 2 458 PRO 458 1994 1994 PRO PRO B . n B 2 459 VAL 459 1995 1995 VAL VAL B . n B 2 460 VAL 460 1996 1996 VAL VAL B . n B 2 461 ALA 461 1997 1997 ALA ALA B . n B 2 462 ARG 462 1998 1998 ARG ARG B . n B 2 463 TYR 463 1999 1999 TYR TYR B . n B 2 464 ILE 464 2000 2000 ILE ILE B . n B 2 465 ARG 465 2001 2001 ARG ARG B . n B 2 466 ILE 466 2002 2002 ILE ILE B . n B 2 467 SER 467 2003 2003 SER SER B . n B 2 468 PRO 468 2004 2004 PRO PRO B . n B 2 469 THR 469 2005 2005 THR THR B . n B 2 470 GLY 470 2006 2006 GLY GLY B . n B 2 471 SER 471 2007 2007 SER SER B . n B 2 472 TYR 472 2008 2008 TYR TYR B . n B 2 473 ASN 473 2009 2009 ASN ASN B . n B 2 474 LYS 474 2010 2010 LYS LYS B . n B 2 475 PRO 475 2011 2011 PRO PRO B . n B 2 476 ALA 476 2012 2012 ALA ALA B . n B 2 477 LEU 477 2013 2013 LEU LEU B . n B 2 478 ARG 478 2014 2014 ARG ARG B . n B 2 479 LEU 479 2015 2015 LEU LEU B . n B 2 480 GLU 480 2016 2016 GLU GLU B . n B 2 481 LEU 481 2017 2017 LEU LEU B . n B 2 482 GLN 482 2018 2018 GLN GLN B . n B 2 483 GLY 483 2019 2019 GLY GLY B . n B 2 484 CYS 484 2020 2020 CYS CYS B . n B 2 485 GLU 485 2021 2021 GLU GLU B . n B 2 486 VAL 486 2022 2022 VAL VAL B . n B 2 487 ASN 487 2023 2023 ASN ASN B . n B 2 488 GLY 488 2024 2024 GLY GLY B . n B 2 489 CYS 489 2025 2025 CYS CYS B . n B 2 490 SER 490 2026 2026 SER SER B . n B 2 491 THR 491 2027 2027 THR THR B . n B 2 492 PRO 492 2028 2028 PRO PRO B . n B 2 493 LEU 493 2029 2029 LEU LEU B . n B 2 494 GLY 494 2030 2030 GLY GLY B . n B 2 495 MET 495 2031 2031 MET MET B . n B 2 496 GLU 496 2032 2032 GLU GLU B . n B 2 497 SER 497 2033 2033 SER SER B . n B 2 498 GLY 498 2034 2034 GLY GLY B . n B 2 499 LYS 499 2035 2035 LYS LYS B . n B 2 500 ILE 500 2036 2036 ILE ILE B . n B 2 501 GLU 501 2037 2037 GLU GLU B . n B 2 502 ASN 502 2038 2038 ASN ASN B . n B 2 503 LYS 503 2039 2039 LYS LYS B . n B 2 504 GLN 504 2040 2040 GLN GLN B . n B 2 505 ILE 505 2041 2041 ILE ILE B . n B 2 506 THR 506 2042 2042 THR THR B . n B 2 507 ALA 507 2043 2043 ALA ALA B . n B 2 508 SER 508 2044 2044 SER SER B . n B 2 509 SER 509 2045 2045 SER SER B . n B 2 510 PHE 510 2046 2046 PHE PHE B . n B 2 511 LYS 511 2047 2047 LYS LYS B . n B 2 512 LYS 512 2048 2048 LYS LYS B . n B 2 513 SER 513 2049 2049 SER SER B . n B 2 514 TRP 514 2050 2050 TRP TRP B . n B 2 515 TRP 515 2051 2051 TRP TRP B . n B 2 516 GLY 516 2052 2052 GLY GLY B . n B 2 517 ASN 517 2053 2053 ASN ASN B . n B 2 518 TYR 518 2054 2054 TYR TYR B . n B 2 519 TRP 519 2055 2055 TRP TRP B . n B 2 520 GLU 520 2056 2056 GLU GLU B . n B 2 521 PRO 521 2057 2057 PRO PRO B . n B 2 522 PHE 522 2058 2058 PHE PHE B . n B 2 523 LEU 523 2059 2059 LEU LEU B . n B 2 524 ALA 524 2060 2060 ALA ALA B . n B 2 525 ARG 525 2061 2061 ARG ARG B . n B 2 526 LEU 526 2062 2062 LEU LEU B . n B 2 527 ASN 527 2063 2063 ASN ASN B . n B 2 528 ALA 528 2064 2064 ALA ALA B . n B 2 529 GLN 529 2065 2065 GLN GLN B . n B 2 530 GLY 530 2066 2066 GLY GLY B . n B 2 531 ARG 531 2067 2067 ARG ARG B . n B 2 532 VAL 532 2068 2068 VAL VAL B . n B 2 533 ASN 533 2069 2069 ASN ASN B . n B 2 534 ALA 534 2070 2070 ALA ALA B . n B 2 535 TRP 535 2071 2071 TRP TRP B . n B 2 536 GLN 536 2072 2072 GLN GLN B . n B 2 537 ALA 537 2073 2073 ALA ALA B . n B 2 538 LYS 538 2074 2074 LYS LYS B . n B 2 539 ALA 539 2075 2075 ALA ALA B . n B 2 540 ASN 540 2076 2076 ASN ASN B . n B 2 541 ASN 541 2077 2077 ASN ASN B . n B 2 542 ASN 542 2078 2078 ASN ASN B . n B 2 543 ASN 543 2079 2079 ASN ASN B . n B 2 544 GLN 544 2080 2080 GLN GLN B . n B 2 545 TRP 545 2081 2081 TRP TRP B . n B 2 546 LEU 546 2082 2082 LEU LEU B . n B 2 547 GLN 547 2083 2083 GLN GLN B . n B 2 548 ILE 548 2084 2084 ILE ILE B . n B 2 549 ASP 549 2085 2085 ASP ASP B . n B 2 550 LEU 550 2086 2086 LEU LEU B . n B 2 551 LEU 551 2087 2087 LEU LEU B . n B 2 552 LYS 552 2088 2088 LYS LYS B . n B 2 553 ILE 553 2089 2089 ILE ILE B . n B 2 554 LYS 554 2090 2090 LYS LYS B . n B 2 555 LYS 555 2091 2091 LYS LYS B . n B 2 556 ILE 556 2092 2092 ILE ILE B . n B 2 557 THR 557 2093 2093 THR THR B . n B 2 558 ALA 558 2094 2094 ALA ALA B . n B 2 559 ILE 559 2095 2095 ILE ILE B . n B 2 560 VAL 560 2096 2096 VAL VAL B . n B 2 561 THR 561 2097 2097 THR THR B . n B 2 562 GLN 562 2098 2098 GLN GLN B . n B 2 563 GLY 563 2099 2099 GLY GLY B . n B 2 564 CYS 564 2100 2100 CYS CYS B . n B 2 565 LYS 565 2101 2101 LYS LYS B . n B 2 566 SER 566 2102 2102 SER SER B . n B 2 567 LEU 567 2103 2103 LEU LEU B . n B 2 568 SER 568 2104 2104 SER SER B . n B 2 569 SER 569 2105 2105 SER SER B . n B 2 570 GLU 570 2106 2106 GLU GLU B . n B 2 571 MET 571 2107 2107 MET MET B . n B 2 572 TYR 572 2108 2108 TYR TYR B . n B 2 573 VAL 573 2109 2109 VAL VAL B . n B 2 574 LYS 574 2110 2110 LYS LYS B . n B 2 575 SER 575 2111 2111 SER SER B . n B 2 576 TYR 576 2112 2112 TYR TYR B . n B 2 577 THR 577 2113 2113 THR THR B . n B 2 578 ILE 578 2114 2114 ILE ILE B . n B 2 579 HIS 579 2115 2115 HIS HIS B . n B 2 580 TYR 580 2116 2116 TYR TYR B . n B 2 581 SER 581 2117 2117 SER SER B . n B 2 582 ASP 582 2118 2118 ASP ASP B . n B 2 583 GLN 583 2119 2119 GLN GLN B . n B 2 584 GLY 584 2120 2120 GLY GLY B . n B 2 585 THR 585 2121 2121 THR THR B . n B 2 586 ASP 586 2122 2122 ASP ASP B . n B 2 587 TRP 587 2123 2123 TRP TRP B . n B 2 588 LYS 588 2124 2124 LYS LYS B . n B 2 589 PRO 589 2125 2125 PRO PRO B . n B 2 590 TYR 590 2126 2126 TYR TYR B . n B 2 591 ARG 591 2127 2127 ARG ARG B . n B 2 592 GLU 592 2128 2128 GLU GLU B . n B 2 593 LYS 593 2129 2129 LYS LYS B . n B 2 594 SER 594 2130 2130 SER SER B . n B 2 595 SER 595 2131 2131 SER SER B . n B 2 596 MET 596 2132 2132 MET MET B . n B 2 597 VAL 597 2133 2133 VAL VAL B . n B 2 598 ASP 598 2134 2134 ASP ASP B . n B 2 599 LYS 599 2135 2135 LYS LYS B . n B 2 600 ILE 600 2136 2136 ILE ILE B . n B 2 601 PHE 601 2137 2137 PHE PHE B . n B 2 602 GLU 602 2138 2138 GLU GLU B . n B 2 603 GLY 603 2139 2139 GLY GLY B . n B 2 604 ASN 604 2140 2140 ASN ASN B . n B 2 605 ASN 605 2141 2141 ASN ASN B . n B 2 606 ASN 606 2142 2142 ASN ASN B . n B 2 607 VAL 607 2143 2143 VAL VAL B . n B 2 608 ARG 608 2144 2144 ARG ARG B . n B 2 609 GLY 609 2145 2145 GLY GLY B . n B 2 610 HIS 610 2146 2146 HIS HIS B . n B 2 611 VAL 611 2147 2147 VAL VAL B . n B 2 612 LYS 612 2148 2148 LYS LYS B . n B 2 613 ASN 613 2149 2149 ASN ASN B . n B 2 614 PHE 614 2150 2150 PHE PHE B . n B 2 615 PHE 615 2151 2151 PHE PHE B . n B 2 616 ASN 616 2152 2152 ASN ASN B . n B 2 617 PRO 617 2153 2153 PRO PRO B . n B 2 618 PRO 618 2154 2154 PRO PRO B . n B 2 619 ILE 619 2155 2155 ILE ILE B . n B 2 620 ILE 620 2156 2156 ILE ILE B . n B 2 621 SER 621 2157 2157 SER SER B . n B 2 622 ARG 622 2158 2158 ARG ARG B . n B 2 623 PHE 623 2159 2159 PHE PHE B . n B 2 624 ILE 624 2160 2160 ILE ILE B . n B 2 625 ARG 625 2161 2161 ARG ARG B . n B 2 626 ILE 626 2162 2162 ILE ILE B . n B 2 627 ILE 627 2163 2163 ILE ILE B . n B 2 628 PRO 628 2164 2164 PRO PRO B . n B 2 629 LYS 629 2165 2165 LYS LYS B . n B 2 630 THR 630 2166 2166 THR THR B . n B 2 631 TRP 631 2167 2167 TRP TRP B . n B 2 632 ASN 632 2168 2168 ASN ASN B . n B 2 633 GLN 633 2169 2169 GLN GLN B . n B 2 634 SER 634 2170 2170 SER SER B . n B 2 635 ILE 635 2171 2171 ILE ILE B . n B 2 636 ALA 636 2172 2172 ALA ALA B . n B 2 637 LEU 637 2173 2173 LEU LEU B . n B 2 638 ARG 638 2174 2174 ARG ARG B . n B 2 639 LEU 639 2175 2175 LEU LEU B . n B 2 640 GLU 640 2176 2176 GLU GLU B . n B 2 641 LEU 641 2177 2177 LEU LEU B . n B 2 642 PHE 642 2178 2178 PHE PHE B . n B 2 643 GLY 643 2179 2179 GLY GLY B . n B 2 644 CYS 644 2180 2180 CYS CYS B . n B 2 645 ASP 645 2181 2181 ASP ASP B . n B 2 646 MET 646 2182 2182 MET MET B . n B 2 647 TYR 647 2183 ? ? ? B . n # 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 197 A ASN 197 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 211 A ASN 211 ? ASN 'GLYCOSYLATION SITE' 3 B ASN 275 B ASN 1811 ? ASN 'GLYCOSYLATION SITE' 4 B ASN 126 B ASN 1662 ? ASN 'GLYCOSYLATION SITE' 5 B ASN 433 B ASN 1969 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA,PQS _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,J,K # 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)' 4750 ? 1 MORE -25 ? 1 'SSA (A^2)' 37640 ? # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_struct_conn_angle.id _pdbx_struct_conn_angle.ptnr1_label_atom_id _pdbx_struct_conn_angle.ptnr1_label_alt_id _pdbx_struct_conn_angle.ptnr1_label_asym_id _pdbx_struct_conn_angle.ptnr1_label_comp_id _pdbx_struct_conn_angle.ptnr1_label_seq_id _pdbx_struct_conn_angle.ptnr1_auth_atom_id _pdbx_struct_conn_angle.ptnr1_auth_asym_id _pdbx_struct_conn_angle.ptnr1_auth_comp_id _pdbx_struct_conn_angle.ptnr1_auth_seq_id _pdbx_struct_conn_angle.ptnr1_PDB_ins_code _pdbx_struct_conn_angle.ptnr1_symmetry _pdbx_struct_conn_angle.ptnr2_label_atom_id _pdbx_struct_conn_angle.ptnr2_label_alt_id _pdbx_struct_conn_angle.ptnr2_label_asym_id _pdbx_struct_conn_angle.ptnr2_label_comp_id _pdbx_struct_conn_angle.ptnr2_label_seq_id _pdbx_struct_conn_angle.ptnr2_auth_atom_id _pdbx_struct_conn_angle.ptnr2_auth_asym_id _pdbx_struct_conn_angle.ptnr2_auth_comp_id _pdbx_struct_conn_angle.ptnr2_auth_seq_id _pdbx_struct_conn_angle.ptnr2_PDB_ins_code _pdbx_struct_conn_angle.ptnr2_symmetry _pdbx_struct_conn_angle.ptnr3_label_atom_id _pdbx_struct_conn_angle.ptnr3_label_alt_id _pdbx_struct_conn_angle.ptnr3_label_asym_id _pdbx_struct_conn_angle.ptnr3_label_comp_id _pdbx_struct_conn_angle.ptnr3_label_seq_id _pdbx_struct_conn_angle.ptnr3_auth_atom_id _pdbx_struct_conn_angle.ptnr3_auth_asym_id _pdbx_struct_conn_angle.ptnr3_auth_comp_id _pdbx_struct_conn_angle.ptnr3_auth_seq_id _pdbx_struct_conn_angle.ptnr3_PDB_ins_code _pdbx_struct_conn_angle.ptnr3_symmetry _pdbx_struct_conn_angle.value _pdbx_struct_conn_angle.value_esd 1 O ? A LYS 93 ? A LYS 93 ? 1_555 CA ? E CA . ? A CA 2184 ? 1_555 O ? A GLU 108 ? A GLU 108 ? 1_555 76.9 ? 2 O ? A LYS 93 ? A LYS 93 ? 1_555 CA ? E CA . ? A CA 2184 ? 1_555 OD1 ? A ASP 111 ? A ASP 111 ? 1_555 77.7 ? 3 O ? A GLU 108 ? A GLU 108 ? 1_555 CA ? E CA . ? A CA 2184 ? 1_555 OD1 ? A ASP 111 ? A ASP 111 ? 1_555 51.2 ? 4 O ? A LYS 93 ? A LYS 93 ? 1_555 CA ? E CA . ? A CA 2184 ? 1_555 OD2 ? A ASP 111 ? A ASP 111 ? 1_555 68.6 ? 5 O ? A GLU 108 ? A GLU 108 ? 1_555 CA ? E CA . ? A CA 2184 ? 1_555 OD2 ? A ASP 111 ? A ASP 111 ? 1_555 99.7 ? 6 OD1 ? A ASP 111 ? A ASP 111 ? 1_555 CA ? E CA . ? A CA 2184 ? 1_555 OD2 ? A ASP 111 ? A ASP 111 ? 1_555 51.8 ? 7 O ? A LYS 93 ? A LYS 93 ? 1_555 CA ? E CA . ? A CA 2184 ? 1_555 OD2 ? A ASP 112 ? A ASP 112 ? 1_555 155.5 ? 8 O ? A GLU 108 ? A GLU 108 ? 1_555 CA ? E CA . ? A CA 2184 ? 1_555 OD2 ? A ASP 112 ? A ASP 112 ? 1_555 97.6 ? 9 OD1 ? A ASP 111 ? A ASP 111 ? 1_555 CA ? E CA . ? A CA 2184 ? 1_555 OD2 ? A ASP 112 ? A ASP 112 ? 1_555 80.4 ? 10 OD2 ? A ASP 111 ? A ASP 111 ? 1_555 CA ? E CA . ? A CA 2184 ? 1_555 OD2 ? A ASP 112 ? A ASP 112 ? 1_555 89.3 ? 11 O ? A LYS 93 ? A LYS 93 ? 1_555 CA ? E CA . ? A CA 2184 ? 1_555 OD1 ? A ASP 112 ? A ASP 112 ? 1_555 159.1 ? 12 O ? A GLU 108 ? A GLU 108 ? 1_555 CA ? E CA . ? A CA 2184 ? 1_555 OD1 ? A ASP 112 ? A ASP 112 ? 1_555 85.5 ? 13 OD1 ? A ASP 111 ? A ASP 111 ? 1_555 CA ? E CA . ? A CA 2184 ? 1_555 OD1 ? A ASP 112 ? A ASP 112 ? 1_555 100.0 ? 14 OD2 ? A ASP 111 ? A ASP 111 ? 1_555 CA ? E CA . ? A CA 2184 ? 1_555 OD1 ? A ASP 112 ? A ASP 112 ? 1_555 126.4 ? 15 OD2 ? A ASP 112 ? A ASP 112 ? 1_555 CA ? E CA . ? A CA 2184 ? 1_555 OD1 ? A ASP 112 ? A ASP 112 ? 1_555 37.6 ? 16 ND1 ? B HIS 266 ? B HIS 1802 ? 1_555 CU ? I CU . ? B CU 2190 ? 1_555 OD1 ? B ASP 308 ? B ASP 1844 ? 1_555 103.6 ? 17 ND1 ? B HIS 266 ? B HIS 1802 ? 1_555 CU ? I CU . ? B CU 2190 ? 1_555 OD2 ? B ASP 308 ? B ASP 1844 ? 1_555 158.6 ? 18 OD1 ? B ASP 308 ? B ASP 1844 ? 1_555 CU ? I CU . ? B CU 2190 ? 1_555 OD2 ? B ASP 308 ? B ASP 1844 ? 1_555 56.6 ? 19 ND1 ? B HIS 266 ? B HIS 1802 ? 1_555 CU ? I CU . ? B CU 2190 ? 1_555 CG ? B ASP 308 ? B ASP 1844 ? 1_555 131.7 ? 20 OD1 ? B ASP 308 ? B ASP 1844 ? 1_555 CU ? I CU . ? B CU 2190 ? 1_555 CG ? B ASP 308 ? B ASP 1844 ? 1_555 28.3 ? 21 OD2 ? B ASP 308 ? B ASP 1844 ? 1_555 CU ? I CU . ? B CU 2190 ? 1_555 CG ? B ASP 308 ? B ASP 1844 ? 1_555 28.4 ? 22 ND1 ? B HIS 266 ? B HIS 1802 ? 1_555 CU ? I CU . ? B CU 2190 ? 1_555 NE2 ? B HIS 268 ? B HIS 1804 ? 1_555 89.7 ? 23 OD1 ? B ASP 308 ? B ASP 1844 ? 1_555 CU ? I CU . ? B CU 2190 ? 1_555 NE2 ? B HIS 268 ? B HIS 1804 ? 1_555 101.7 ? 24 OD2 ? B ASP 308 ? B ASP 1844 ? 1_555 CU ? I CU . ? B CU 2190 ? 1_555 NE2 ? B HIS 268 ? B HIS 1804 ? 1_555 87.1 ? 25 CG ? B ASP 308 ? B ASP 1844 ? 1_555 CU ? I CU . ? B CU 2190 ? 1_555 NE2 ? B HIS 268 ? B HIS 1804 ? 1_555 96.3 ? # 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 2004-06-29 2 'Structure model' 1 1 2007-10-16 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' 'Derived calculations' 3 3 'Structure model' 'Version format compliance' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal DENZO 'data reduction' . ? 1 SCALEPACK 'data scaling' . ? 2 MLPHARE phasing . ? 3 CNS refinement . ? 4 # loop_ _pdbx_validate_rmsd_angle.id _pdbx_validate_rmsd_angle.PDB_model_num _pdbx_validate_rmsd_angle.auth_atom_id_1 _pdbx_validate_rmsd_angle.auth_asym_id_1 _pdbx_validate_rmsd_angle.auth_comp_id_1 _pdbx_validate_rmsd_angle.auth_seq_id_1 _pdbx_validate_rmsd_angle.PDB_ins_code_1 _pdbx_validate_rmsd_angle.label_alt_id_1 _pdbx_validate_rmsd_angle.auth_atom_id_2 _pdbx_validate_rmsd_angle.auth_asym_id_2 _pdbx_validate_rmsd_angle.auth_comp_id_2 _pdbx_validate_rmsd_angle.auth_seq_id_2 _pdbx_validate_rmsd_angle.PDB_ins_code_2 _pdbx_validate_rmsd_angle.label_alt_id_2 _pdbx_validate_rmsd_angle.auth_atom_id_3 _pdbx_validate_rmsd_angle.auth_asym_id_3 _pdbx_validate_rmsd_angle.auth_comp_id_3 _pdbx_validate_rmsd_angle.auth_seq_id_3 _pdbx_validate_rmsd_angle.PDB_ins_code_3 _pdbx_validate_rmsd_angle.label_alt_id_3 _pdbx_validate_rmsd_angle.angle_value _pdbx_validate_rmsd_angle.angle_target_value _pdbx_validate_rmsd_angle.angle_deviation _pdbx_validate_rmsd_angle.angle_standard_deviation _pdbx_validate_rmsd_angle.linker_flag 1 1 C B LYS 1837 ? ? N B PRO 1838 ? ? CA B PRO 1838 ? ? 128.81 119.30 9.51 1.50 Y 2 1 N B VAL 1847 ? ? CA B VAL 1847 ? ? C B VAL 1847 ? ? 93.11 111.00 -17.89 2.70 N 3 1 N B ARG 2014 ? ? CA B ARG 2014 ? ? C B ARG 2014 ? ? 93.53 111.00 -17.47 2.70 N # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 LYS A 2 ? ? -61.74 -172.85 2 1 TYR A 41 ? ? 60.12 157.63 3 1 ALA A 43 ? ? 32.34 -105.79 4 1 PHE A 45 ? ? 77.20 49.51 5 1 PRO A 50 ? ? -35.00 176.19 6 1 ARG A 53 ? ? -59.07 93.00 7 1 THR A 54 ? ? 63.52 -135.99 8 1 SER A 55 ? ? 38.08 44.92 9 1 PRO A 60 ? ? -54.61 -126.22 10 1 THR A 61 ? ? 178.52 90.76 11 1 GLN A 87 ? ? -109.69 72.57 12 1 GLU A 96 ? ? -68.56 -76.69 13 1 SER A 101 ? ? -68.39 86.72 14 1 MET A 110 ? ? -82.88 48.62 15 1 ASP A 111 ? ? -147.07 -11.69 16 1 PRO A 116 ? ? -50.38 92.94 17 1 ILE A 126 ? ? -52.96 106.19 18 1 HIS A 129 ? ? -76.12 31.37 19 1 PRO A 132 ? ? -46.61 157.94 20 1 THR A 133 ? ? -89.27 -134.87 21 1 PRO A 137 ? ? -41.68 159.40 22 1 TYR A 145 ? ? -170.39 -175.63 23 1 VAL A 148 ? ? -36.65 -27.22 24 1 ASN A 149 ? ? -165.72 116.11 25 1 GLU A 152 ? ? -74.93 -86.93 26 1 ASP A 153 ? ? -17.69 -62.17 27 1 SER A 156 ? ? -64.98 13.86 28 1 ILE A 159 ? ? 165.73 165.29 29 1 LYS A 177 ? ? -86.45 -118.04 30 1 MET A 178 ? ? -59.45 26.36 31 1 PHE A 179 ? ? -133.02 -50.33 32 1 GLU A 180 ? ? 39.68 142.97 33 1 LYS A 181 ? ? 75.20 46.80 34 1 PHE A 187 ? ? -48.97 90.47 35 1 LYS A 194 ? ? -113.41 77.11 36 1 SER A 195 ? ? -165.82 -137.58 37 1 SER A 200 ? ? -63.61 96.95 38 1 MET A 203 ? ? -177.75 79.65 39 1 TYR A 204 ? ? -62.93 98.68 40 1 THR A 205 ? ? -101.52 -157.62 41 1 VAL A 206 ? ? -165.19 62.85 42 1 ASN A 207 ? ? 103.87 21.08 43 1 VAL A 210 ? ? -78.25 -135.71 44 1 PRO A 215 ? ? -51.70 91.78 45 1 ASP A 216 ? ? -69.91 -156.38 46 1 ILE A 217 ? ? -168.07 117.36 47 1 CYS A 220 ? ? -95.99 44.68 48 1 SER A 233 ? ? 174.66 7.54 49 1 SER A 234 ? ? 57.14 -38.92 50 1 GLU A 237 ? ? -174.14 145.97 51 1 SER A 240 ? ? -111.91 73.71 52 1 GLN A 246 ? ? -62.88 42.76 53 1 ASN A 251 ? ? 68.50 -107.67 54 1 SER A 262 ? ? -14.15 -35.87 55 1 ALA A 263 ? ? -147.61 37.37 56 1 LEU A 283 ? ? -60.38 72.68 57 1 PRO A 285 ? ? -35.36 -6.86 58 1 ARG A 286 ? ? -141.23 17.61 59 1 HIS A 287 ? ? -120.95 -50.36 60 1 ALA A 290 ? ? -152.40 13.97 61 1 MET A 292 ? ? -66.38 97.61 62 1 SER B 1557 ? ? 61.82 -23.61 63 1 LYS B 1558 ? ? -22.95 -47.36 64 1 PHE B 1559 ? ? -94.45 31.81 65 1 GLU B 1570 ? ? 70.42 99.54 66 1 ASP B 1571 ? ? 60.18 82.18 67 1 ASP B 1612 ? ? 71.73 -4.66 68 1 ASN B 1621 ? ? 72.47 91.57 69 1 HIS B 1632 ? ? -59.83 105.11 70 1 LEU B 1634 ? ? -50.24 -78.10 71 1 PRO B 1661 ? ? -43.94 160.68 72 1 ASN B 1662 ? ? 48.38 8.08 73 1 TYR B 1665 ? ? 174.46 121.69 74 1 ALA B 1671 ? ? -59.69 86.05 75 1 PRO B 1680 ? ? -80.18 -78.96 76 1 SER B 1682 ? ? 51.04 107.66 77 1 PRO B 1695 ? ? -23.64 -78.41 78 1 LYS B 1712 ? ? -29.06 135.47 79 1 LYS B 1717 ? ? -21.67 -46.59 80 1 GLU B 1718 ? ? -109.60 56.56 81 1 THR B 1719 ? ? 17.54 85.37 82 1 VAL B 1723 ? ? -61.30 -109.41 83 1 MET B 1725 ? ? 43.41 171.01 84 1 ARG B 1726 ? ? 61.79 82.65 85 1 SER B 1740 ? ? -150.75 -102.56 86 1 TYR B 1743 ? ? 59.90 -9.71 87 1 HIS B 1762 ? ? -101.39 61.48 88 1 TYR B 1772 ? ? 73.80 -37.83 89 1 ASP B 1797 ? ? -74.93 -90.46 90 1 ILE B 1798 ? ? 56.19 106.30 91 1 PRO B 1825 ? ? -49.40 156.66 92 1 GLU B 1832 ? ? -62.87 -179.76 93 1 LYS B 1837 ? ? 73.66 126.84 94 1 GLU B 1846 ? ? 44.21 17.89 95 1 GLU B 1865 ? ? -109.29 59.29 96 1 LYS B 1867 ? ? -176.36 32.44 97 1 GLU B 1886 ? ? 179.55 157.64 98 1 TYR B 1890 ? ? 88.08 -16.59 99 1 LYS B 1894 ? ? -55.48 -9.63 100 1 ALA B 1896 ? ? -63.65 58.27 101 1 ASN B 1899 ? ? 76.39 -27.00 102 1 SER B 1913 ? ? -45.44 -6.33 103 1 THR B 1914 ? ? -56.35 100.53 104 1 GLU B 1915 ? ? -115.03 -111.59 105 1 PHE B 1916 ? ? -74.22 22.30 106 1 GLN B 1927 ? ? 68.41 -13.78 107 1 HIS B 1942 ? ? -52.75 -72.70 108 1 TYR B 1943 ? ? -133.63 -69.79 109 1 GLU B 1951 ? ? -179.13 140.53 110 1 ARG B 1960 ? ? 98.29 -6.32 111 1 SER B 1970 ? ? -4.80 124.60 112 1 ASN B 2009 ? ? 77.71 -77.21 113 1 PRO B 2011 ? ? -67.30 96.80 114 1 CYS B 2020 ? ? -177.15 -169.93 115 1 SER B 2026 ? ? -153.03 25.24 116 1 LYS B 2039 ? ? -63.60 36.22 117 1 LYS B 2048 ? ? -167.32 61.69 118 1 TRP B 2050 ? ? -57.66 14.08 119 1 TRP B 2055 ? ? -105.98 68.95 120 1 LEU B 2062 ? ? -35.42 124.41 121 1 ASN B 2063 ? ? 75.80 47.74 122 1 ARG B 2067 ? ? -58.77 -97.59 123 1 ASN B 2069 ? ? -104.36 43.99 124 1 ALA B 2070 ? ? 178.68 -167.79 125 1 ASN B 2076 ? ? -111.40 75.54 126 1 ASN B 2077 ? ? -105.38 -91.31 127 1 ASN B 2078 ? ? -171.12 -32.61 128 1 ASN B 2079 ? ? -103.24 60.76 129 1 LEU B 2087 ? ? 53.47 -18.89 130 1 LYS B 2101 ? ? -119.04 79.43 131 1 ASP B 2122 ? ? 68.85 117.69 132 1 SER B 2130 ? ? -160.07 100.30 133 1 SER B 2131 ? ? 178.85 178.13 134 1 SER B 2157 ? ? -167.95 -169.76 135 1 TRP B 2167 ? ? -166.89 -165.03 136 1 GLN B 2169 ? ? 63.86 -47.05 # _pdbx_validate_planes.id 1 _pdbx_validate_planes.PDB_model_num 1 _pdbx_validate_planes.auth_comp_id TYR _pdbx_validate_planes.auth_asym_id B _pdbx_validate_planes.auth_seq_id 1890 _pdbx_validate_planes.PDB_ins_code ? _pdbx_validate_planes.label_alt_id ? _pdbx_validate_planes.rmsd 0.069 _pdbx_validate_planes.type 'SIDE CHAIN' # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A TYR 17 ? A TYR 17 2 1 Y 1 A ARG 18 ? A ARG 18 3 1 Y 1 A PRO 19 ? A PRO 19 4 1 Y 1 A GLU 20 ? A GLU 20 5 1 Y 1 A SER 21 ? A SER 21 6 1 Y 1 A THR 22 ? A THR 22 7 1 Y 1 A HIS 23 ? A HIS 23 8 1 Y 1 A LEU 24 ? A LEU 24 9 1 Y 1 A SER 25 ? A SER 25 10 1 Y 1 A SER 26 ? A SER 26 11 1 Y 1 A LYS 27 ? A LYS 27 12 1 Y 1 A PRO 28 ? A PRO 28 13 1 Y 1 A PHE 29 ? A PHE 29 14 1 Y 1 A GLU 30 ? A GLU 30 15 1 Y 1 A HIS 222 ? A HIS 222 16 1 Y 1 A ASP 223 ? A ASP 223 17 1 Y 1 A HIS 224 ? A HIS 224 18 1 Y 1 A ILE 225 ? A ILE 225 19 1 Y 1 A SER 226 ? A SER 226 20 1 Y 1 A TRP 227 ? A TRP 227 21 1 Y 1 A ALA 268 ? A ALA 268 22 1 Y 1 A ASN 269 ? A ASN 269 23 1 Y 1 A MET 270 ? A MET 270 24 1 Y 1 A THR 271 ? A THR 271 25 1 Y 1 A VAL 272 ? A VAL 272 26 1 Y 1 A SER 273 ? A SER 273 27 1 Y 1 A PRO 274 ? A PRO 274 28 1 Y 1 A GLU 275 ? A GLU 275 29 1 Y 1 A ASP 297 ? A ASP 297 30 1 Y 1 A ILE 298 ? A ILE 298 31 1 Y 1 A LYS 299 ? A LYS 299 32 1 Y 1 A ASN 300 ? A ASN 300 33 1 Y 1 A CYS 301 ? A CYS 301 34 1 Y 1 A ALA 302 ? A ALA 302 35 1 Y 1 A LYS 303 ? A LYS 303 36 1 Y 1 A LYS 304 ? A LYS 304 37 1 Y 1 A THR 305 ? A THR 305 38 1 Y 1 A ARG 306 ? A ARG 306 39 1 Y 1 B SER 1537 ? B SER 1 40 1 Y 1 B GLN 1561 ? B GLN 25 41 1 Y 1 B SER 1562 ? B SER 26 42 1 Y 1 B ASP 1563 ? B ASP 27 43 1 Y 1 B ASP 1564 ? B ASP 28 44 1 Y 1 B VAL 1565 ? B VAL 29 45 1 Y 1 B ASP 1566 ? B ASP 30 46 1 Y 1 B TYR 1567 ? B TYR 31 47 1 Y 1 B VAL 1568 ? B VAL 32 48 1 Y 1 B TYR 1636 ? B TYR 100 49 1 Y 1 B GLU 1637 ? B GLU 101 50 1 Y 1 B LYS 1638 ? B LYS 102 51 1 Y 1 B SER 1639 ? B SER 103 52 1 Y 1 B SER 1640 ? B SER 104 53 1 Y 1 B GLU 1641 ? B GLU 105 54 1 Y 1 B GLY 1642 ? B GLY 106 55 1 Y 1 B LYS 1643 ? B LYS 107 56 1 Y 1 B THR 1644 ? B THR 108 57 1 Y 1 B TYR 1645 ? B TYR 109 58 1 Y 1 B GLU 1646 ? B GLU 110 59 1 Y 1 B ASP 1647 ? B ASP 111 60 1 Y 1 B ASP 1648 ? B ASP 112 61 1 Y 1 B SER 1649 ? B SER 113 62 1 Y 1 B PRO 1650 ? B PRO 114 63 1 Y 1 B GLU 1651 ? B GLU 115 64 1 Y 1 B TRP 1652 ? B TRP 116 65 1 Y 1 B PHE 1653 ? B PHE 117 66 1 Y 1 B LYS 1654 ? B LYS 118 67 1 Y 1 B GLU 1655 ? B GLU 119 68 1 Y 1 B ASP 1656 ? B ASP 120 69 1 Y 1 B LYS 1745 ? B LYS 209 70 1 Y 1 B LYS 1746 ? B LYS 210 71 1 Y 1 B PRO 1747 ? B PRO 211 72 1 Y 1 B THR 1748 ? B THR 212 73 1 Y 1 B ARG 1749 ? B ARG 213 74 1 Y 1 B SER 1750 ? B SER 214 75 1 Y 1 B TRP 1751 ? B TRP 215 76 1 Y 1 B ARG 1752 ? B ARG 216 77 1 Y 1 B ARG 1753 ? B ARG 217 78 1 Y 1 B ALA 1754 ? B ALA 218 79 1 Y 1 B SER 1755 ? B SER 219 80 1 Y 1 B SER 1756 ? B SER 220 81 1 Y 1 B GLU 1757 ? B GLU 221 82 1 Y 1 B VAL 1758 ? B VAL 222 83 1 Y 1 B LYS 1759 ? B LYS 223 84 1 Y 1 B TYR 2183 ? B TYR 647 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 3 N-ACETYL-D-GLUCOSAMINE NAG 4 'CALCIUM ION' CA 5 '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' NDG 6 'COPPER (II) ION' CU 7 water HOH # 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 2185 2185 NAG NAG A . D 3 NAG 1 2186 2186 NAG NAG A . E 4 CA 1 2184 2184 CA CA A . F 5 NDG 1 2187 2187 NDG NAG B . G 3 NAG 1 2188 2188 NAG NAG B . H 5 NDG 1 2189 2189 NDG NAG B . I 6 CU 1 2190 2183 CU CU B . J 7 HOH 1 2190 2190 HOH HOH A . J 7 HOH 2 2197 2197 HOH HOH A . J 7 HOH 3 2201 2201 HOH HOH A . J 7 HOH 4 2206 2206 HOH HOH A . J 7 HOH 5 2207 2207 HOH HOH A . J 7 HOH 6 2209 2209 HOH HOH A . J 7 HOH 7 2215 2215 HOH HOH A . J 7 HOH 8 2231 2231 HOH HOH A . J 7 HOH 9 2234 2234 HOH HOH A . J 7 HOH 10 2235 2235 HOH HOH A . J 7 HOH 11 2243 2243 HOH HOH A . J 7 HOH 12 2246 2246 HOH HOH A . J 7 HOH 13 2250 2250 HOH HOH A . J 7 HOH 14 2252 2252 HOH HOH A . J 7 HOH 15 2254 2254 HOH HOH A . J 7 HOH 16 2256 2256 HOH HOH A . J 7 HOH 17 2262 2262 HOH HOH A . J 7 HOH 18 2268 2268 HOH HOH A . J 7 HOH 19 2269 2269 HOH HOH A . J 7 HOH 20 2274 2274 HOH HOH A . J 7 HOH 21 2276 2276 HOH HOH A . J 7 HOH 22 2277 2277 HOH HOH A . J 7 HOH 23 2282 2282 HOH HOH A . J 7 HOH 24 2286 2286 HOH HOH A . J 7 HOH 25 2293 2293 HOH HOH A . J 7 HOH 26 2297 2297 HOH HOH A . J 7 HOH 27 2298 2298 HOH HOH A . J 7 HOH 28 2299 2299 HOH HOH A . J 7 HOH 29 2302 2302 HOH HOH A . J 7 HOH 30 2303 2303 HOH HOH A . J 7 HOH 31 2305 2305 HOH HOH A . J 7 HOH 32 2311 2311 HOH HOH A . J 7 HOH 33 2312 2312 HOH HOH A . J 7 HOH 34 2313 2313 HOH HOH A . J 7 HOH 35 2319 2319 HOH HOH A . J 7 HOH 36 2327 2327 HOH HOH A . J 7 HOH 37 2336 2336 HOH HOH A . J 7 HOH 38 2339 2339 HOH HOH A . J 7 HOH 39 2343 2343 HOH HOH A . J 7 HOH 40 2344 2344 HOH HOH A . J 7 HOH 41 2348 2348 HOH HOH A . J 7 HOH 42 2350 2350 HOH HOH A . J 7 HOH 43 2354 2354 HOH HOH A . J 7 HOH 44 2357 2357 HOH HOH A . J 7 HOH 45 2359 2359 HOH HOH A . J 7 HOH 46 2363 2363 HOH HOH A . J 7 HOH 47 2369 2369 HOH HOH A . K 7 HOH 1 2191 2191 HOH HOH B . K 7 HOH 2 2192 2192 HOH HOH B . K 7 HOH 3 2193 2193 HOH HOH B . K 7 HOH 4 2194 2194 HOH HOH B . K 7 HOH 5 2195 2195 HOH HOH B . K 7 HOH 6 2196 2196 HOH HOH B . K 7 HOH 7 2198 2198 HOH HOH B . K 7 HOH 8 2199 2199 HOH HOH B . K 7 HOH 9 2200 2200 HOH HOH B . K 7 HOH 10 2202 2202 HOH HOH B . K 7 HOH 11 2203 2203 HOH HOH B . K 7 HOH 12 2204 2204 HOH HOH B . K 7 HOH 13 2205 2205 HOH HOH B . K 7 HOH 14 2208 2208 HOH HOH B . K 7 HOH 15 2210 2210 HOH HOH B . K 7 HOH 16 2211 2211 HOH HOH B . K 7 HOH 17 2212 2212 HOH HOH B . K 7 HOH 18 2213 2213 HOH HOH B . K 7 HOH 19 2214 2214 HOH HOH B . K 7 HOH 20 2216 2216 HOH HOH B . K 7 HOH 21 2217 2217 HOH HOH B . K 7 HOH 22 2218 2218 HOH HOH B . K 7 HOH 23 2219 2219 HOH HOH B . K 7 HOH 24 2220 2220 HOH HOH B . K 7 HOH 25 2221 2221 HOH HOH B . K 7 HOH 26 2222 2222 HOH HOH B . K 7 HOH 27 2223 2223 HOH HOH B . K 7 HOH 28 2224 2224 HOH HOH B . K 7 HOH 29 2225 2225 HOH HOH B . K 7 HOH 30 2226 2226 HOH HOH B . K 7 HOH 31 2227 2227 HOH HOH B . K 7 HOH 32 2228 2228 HOH HOH B . K 7 HOH 33 2229 2229 HOH HOH B . K 7 HOH 34 2230 2230 HOH HOH B . K 7 HOH 35 2232 2232 HOH HOH B . K 7 HOH 36 2233 2233 HOH HOH B . K 7 HOH 37 2236 2236 HOH HOH B . K 7 HOH 38 2237 2237 HOH HOH B . K 7 HOH 39 2238 2238 HOH HOH B . K 7 HOH 40 2239 2239 HOH HOH B . K 7 HOH 41 2240 2240 HOH HOH B . K 7 HOH 42 2241 2241 HOH HOH B . K 7 HOH 43 2242 2242 HOH HOH B . K 7 HOH 44 2244 2244 HOH HOH B . K 7 HOH 45 2245 2245 HOH HOH B . K 7 HOH 46 2247 2247 HOH HOH B . K 7 HOH 47 2248 2248 HOH HOH B . K 7 HOH 48 2249 2249 HOH HOH B . K 7 HOH 49 2251 2251 HOH HOH B . K 7 HOH 50 2253 2253 HOH HOH B . K 7 HOH 51 2255 2255 HOH HOH B . K 7 HOH 52 2257 2257 HOH HOH B . K 7 HOH 53 2258 2258 HOH HOH B . K 7 HOH 54 2259 2259 HOH HOH B . K 7 HOH 55 2260 2260 HOH HOH B . K 7 HOH 56 2261 2261 HOH HOH B . K 7 HOH 57 2263 2263 HOH HOH B . K 7 HOH 58 2264 2264 HOH HOH B . K 7 HOH 59 2265 2265 HOH HOH B . K 7 HOH 60 2266 2266 HOH HOH B . K 7 HOH 61 2267 2267 HOH HOH B . K 7 HOH 62 2270 2270 HOH HOH B . K 7 HOH 63 2271 2271 HOH HOH B . K 7 HOH 64 2272 2272 HOH HOH B . K 7 HOH 65 2273 2273 HOH HOH B . K 7 HOH 66 2275 2275 HOH HOH B . K 7 HOH 67 2278 2278 HOH HOH B . K 7 HOH 68 2279 2279 HOH HOH B . K 7 HOH 69 2280 2280 HOH HOH B . K 7 HOH 70 2281 2281 HOH HOH B . K 7 HOH 71 2283 2283 HOH HOH B . K 7 HOH 72 2284 2284 HOH HOH B . K 7 HOH 73 2285 2285 HOH HOH B . K 7 HOH 74 2287 2287 HOH HOH B . K 7 HOH 75 2288 2288 HOH HOH B . K 7 HOH 76 2289 2289 HOH HOH B . K 7 HOH 77 2290 2290 HOH HOH B . K 7 HOH 78 2291 2291 HOH HOH B . K 7 HOH 79 2292 2292 HOH HOH B . K 7 HOH 80 2294 2294 HOH HOH B . K 7 HOH 81 2295 2295 HOH HOH B . K 7 HOH 82 2296 2296 HOH HOH B . K 7 HOH 83 2300 2300 HOH HOH B . K 7 HOH 84 2301 2301 HOH HOH B . K 7 HOH 85 2304 2304 HOH HOH B . K 7 HOH 86 2306 2306 HOH HOH B . K 7 HOH 87 2307 2307 HOH HOH B . K 7 HOH 88 2308 2308 HOH HOH B . K 7 HOH 89 2309 2309 HOH HOH B . K 7 HOH 90 2310 2310 HOH HOH B . K 7 HOH 91 2314 2314 HOH HOH B . K 7 HOH 92 2315 2315 HOH HOH B . K 7 HOH 93 2316 2316 HOH HOH B . K 7 HOH 94 2317 2317 HOH HOH B . K 7 HOH 95 2318 2318 HOH HOH B . K 7 HOH 96 2320 2320 HOH HOH B . K 7 HOH 97 2321 2321 HOH HOH B . K 7 HOH 98 2322 2322 HOH HOH B . K 7 HOH 99 2323 2323 HOH HOH B . K 7 HOH 100 2324 2324 HOH HOH B . K 7 HOH 101 2325 2325 HOH HOH B . K 7 HOH 102 2326 2326 HOH HOH B . K 7 HOH 103 2328 2328 HOH HOH B . K 7 HOH 104 2329 2329 HOH HOH B . K 7 HOH 105 2330 2330 HOH HOH B . K 7 HOH 106 2331 2331 HOH HOH B . K 7 HOH 107 2332 2332 HOH HOH B . K 7 HOH 108 2333 2333 HOH HOH B . K 7 HOH 109 2334 2334 HOH HOH B . K 7 HOH 110 2335 2335 HOH HOH B . K 7 HOH 111 2337 2337 HOH HOH B . K 7 HOH 112 2338 2338 HOH HOH B . K 7 HOH 113 2340 2340 HOH HOH B . K 7 HOH 114 2341 2341 HOH HOH B . K 7 HOH 115 2342 2342 HOH HOH B . K 7 HOH 116 2345 2345 HOH HOH B . K 7 HOH 117 2346 2346 HOH HOH B . K 7 HOH 118 2347 2347 HOH HOH B . K 7 HOH 119 2349 2349 HOH HOH B . K 7 HOH 120 2351 2351 HOH HOH B . K 7 HOH 121 2352 2352 HOH HOH B . K 7 HOH 122 2353 2353 HOH HOH B . K 7 HOH 123 2355 2355 HOH HOH B . K 7 HOH 124 2356 2356 HOH HOH B . K 7 HOH 125 2358 2358 HOH HOH B . K 7 HOH 126 2360 2360 HOH HOH B . K 7 HOH 127 2361 2361 HOH HOH B . K 7 HOH 128 2362 2362 HOH HOH B . K 7 HOH 129 2364 2364 HOH HOH B . K 7 HOH 130 2365 2365 HOH HOH B . K 7 HOH 131 2366 2366 HOH HOH B . K 7 HOH 132 2367 2367 HOH HOH B . K 7 HOH 133 2368 2368 HOH HOH B . K 7 HOH 134 2370 2370 HOH HOH B . K 7 HOH 135 2371 2371 HOH HOH B . K 7 HOH 136 2372 2372 HOH HOH B . K 7 HOH 137 2373 2373 HOH HOH B . K 7 HOH 138 2374 2374 HOH HOH B . K 7 HOH 139 2375 2375 HOH HOH B . K 7 HOH 140 2376 2376 HOH HOH B . K 7 HOH 141 2377 2377 HOH HOH B . K 7 HOH 142 2378 2378 HOH HOH B . #