data_4Y61 # _entry.id 4Y61 # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.284 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 4Y61 WWPDB D_1000206905 # _pdbx_database_status.status_code REL _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.entry_id 4Y61 _pdbx_database_status.recvd_initial_deposition_date 2015-02-12 _pdbx_database_status.SG_entry N _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site PDBJ _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? _pdbx_database_status.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Yamgata, A.' 1 'Sato, Y.' 2 'Goto-Ito, S.' 3 'Uemura, T.' 4 'Maeda, A.' 5 'Shiroshima, T.' 6 'Yoshida, T.' 7 'Fukai, S.' 8 # _citation.abstract ? _citation.abstract_id_CAS ? _citation.book_id_ISBN ? _citation.book_publisher ? _citation.book_publisher_city ? _citation.book_title ? _citation.coordinate_linkage ? _citation.country UK _citation.database_id_Medline ? _citation.details ? _citation.id primary _citation.journal_abbrev 'Sci Rep' _citation.journal_id_ASTM ? _citation.journal_id_CSD ? _citation.journal_id_ISSN 2045-2322 _citation.journal_full ? _citation.journal_issue ? _citation.journal_volume 5 _citation.language ? _citation.page_first 9686 _citation.page_last 9686 _citation.title 'Structure of Slitrk2-PTP delta complex reveals mechanisms for splicing-dependent trans-synaptic adhesion.' _citation.year 2015 _citation.database_id_CSD ? _citation.pdbx_database_id_DOI 10.1038/srep09686 _citation.pdbx_database_id_PubMed 25989451 _citation.unpublished_flag ? # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Yamagata, A.' 1 primary 'Sato, Y.' 2 primary 'Goto-Ito, S.' 3 primary 'Uemura, T.' 4 primary 'Maeda, A.' 5 primary 'Shiroshima, T.' 6 primary 'Yoshida, T.' 7 primary 'Fukai, S.' 8 # _cell.entry_id 4Y61 _cell.length_a 87.227 _cell.length_b 91.308 _cell.length_c 123.389 _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 4Y61 _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 # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer man 'Receptor-type tyrosine-protein phosphatase delta' 43772.168 1 3.1.3.48 ? 'UNP residues 21-411' ? 2 polymer man 'SLIT and NTRK-like protein 2' 31129.096 1 ? ? 'UNP residues 1-266' ? 3 non-polymer syn N-ACETYL-D-GLUCOSAMINE 221.208 4 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name R-PTP-delta # 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 ;ETPPRFTRTPVDQTGVSGGVASFICQATGDPRPKIVWNKKGKKVSNQRFEVIEFDDGSGSVLRIQPLRTPRDEAIYECVA SNNVGEISVSTRLTVLREDQIPRGFPTIDMGPQLKVVERTRTATMLCAASGNPDPEITWFKDFLPVDTSNNNGRIKQLRS ESIGGTPIRGALQIEQSEESDQGKYECVATNSAGTRYSAPANLYVRELREVRRVPPRFSIPPTNHEIMPGGSVNITCVAV GSPMPYVKWMLGAEDLTPEDDMPIGRNVLELNDVRQSANYTCVAMSTLGVIEAIAQITVKALPKPPGTPVVTESTATSIT LTWDSGNPEPVSYYIIQHKPKNSEEPYKEIDGIATTRYSVAGLSPYSDYEFRVVAVNNIGRGPASEPVLTQKHHHHHH ; ;ETPPRFTRTPVDQTGVSGGVASFICQATGDPRPKIVWNKKGKKVSNQRFEVIEFDDGSGSVLRIQPLRTPRDEAIYECVA SNNVGEISVSTRLTVLREDQIPRGFPTIDMGPQLKVVERTRTATMLCAASGNPDPEITWFKDFLPVDTSNNNGRIKQLRS ESIGGTPIRGALQIEQSEESDQGKYECVATNSAGTRYSAPANLYVRELREVRRVPPRFSIPPTNHEIMPGGSVNITCVAV GSPMPYVKWMLGAEDLTPEDDMPIGRNVLELNDVRQSANYTCVAMSTLGVIEAIAQITVKALPKPPGTPVVTESTATSIT LTWDSGNPEPVSYYIIQHKPKNSEEPYKEIDGIATTRYSVAGLSPYSDYEFRVVAVNNIGRGPASEPVLTQKHHHHHH ; A ? 2 'polypeptide(L)' no no ;MLSGVWFLSVLTVAGILQTESRKTAKDICKIRCLCEEKENVLNINCENKGFTTVSLLQPPQYRIYQLFLNGNLLTRLYPN EFVNYSNAVTLHLGNNGLQEIRPGAFSGLKTLKRLHLNNNKLEVLREDTFLGLESLEYLQADYNYISTIEAGAFSKLNKL KVLILNDNLLLSLPSNVFRFVLLTHLDLRGNRLKVMPFAGVLEHIGGIMEIQLEENPWNCTCDLLPLKAWLDTITVFVGE IVCETPFRLHGKDVTQLTRQDLCPRKHHHHHH ; ;MLSGVWFLSVLTVAGILQTESRKTAKDICKIRCLCEEKENVLNINCENKGFTTVSLLQPPQYRIYQLFLNGNLLTRLYPN EFVNYSNAVTLHLGNNGLQEIRPGAFSGLKTLKRLHLNNNKLEVLREDTFLGLESLEYLQADYNYISTIEAGAFSKLNKL KVLILNDNLLLSLPSNVFRFVLLTHLDLRGNRLKVMPFAGVLEHIGGIMEIQLEENPWNCTCDLLPLKAWLDTITVFVGE IVCETPFRLHGKDVTQLTRQDLCPRKHHHHHH ; B ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 GLU n 1 2 THR n 1 3 PRO n 1 4 PRO n 1 5 ARG n 1 6 PHE n 1 7 THR n 1 8 ARG n 1 9 THR n 1 10 PRO n 1 11 VAL n 1 12 ASP n 1 13 GLN n 1 14 THR n 1 15 GLY n 1 16 VAL n 1 17 SER n 1 18 GLY n 1 19 GLY n 1 20 VAL n 1 21 ALA n 1 22 SER n 1 23 PHE n 1 24 ILE n 1 25 CYS n 1 26 GLN n 1 27 ALA n 1 28 THR n 1 29 GLY n 1 30 ASP n 1 31 PRO n 1 32 ARG n 1 33 PRO n 1 34 LYS n 1 35 ILE n 1 36 VAL n 1 37 TRP n 1 38 ASN n 1 39 LYS n 1 40 LYS n 1 41 GLY n 1 42 LYS n 1 43 LYS n 1 44 VAL n 1 45 SER n 1 46 ASN n 1 47 GLN n 1 48 ARG n 1 49 PHE n 1 50 GLU n 1 51 VAL n 1 52 ILE n 1 53 GLU n 1 54 PHE n 1 55 ASP n 1 56 ASP n 1 57 GLY n 1 58 SER n 1 59 GLY n 1 60 SER n 1 61 VAL n 1 62 LEU n 1 63 ARG n 1 64 ILE n 1 65 GLN n 1 66 PRO n 1 67 LEU n 1 68 ARG n 1 69 THR n 1 70 PRO n 1 71 ARG n 1 72 ASP n 1 73 GLU n 1 74 ALA n 1 75 ILE n 1 76 TYR n 1 77 GLU n 1 78 CYS n 1 79 VAL n 1 80 ALA n 1 81 SER n 1 82 ASN n 1 83 ASN n 1 84 VAL n 1 85 GLY n 1 86 GLU n 1 87 ILE n 1 88 SER n 1 89 VAL n 1 90 SER n 1 91 THR n 1 92 ARG n 1 93 LEU n 1 94 THR n 1 95 VAL n 1 96 LEU n 1 97 ARG n 1 98 GLU n 1 99 ASP n 1 100 GLN n 1 101 ILE n 1 102 PRO n 1 103 ARG n 1 104 GLY n 1 105 PHE n 1 106 PRO n 1 107 THR n 1 108 ILE n 1 109 ASP n 1 110 MET n 1 111 GLY n 1 112 PRO n 1 113 GLN n 1 114 LEU n 1 115 LYS n 1 116 VAL n 1 117 VAL n 1 118 GLU n 1 119 ARG n 1 120 THR n 1 121 ARG n 1 122 THR n 1 123 ALA n 1 124 THR n 1 125 MET n 1 126 LEU n 1 127 CYS n 1 128 ALA n 1 129 ALA n 1 130 SER n 1 131 GLY n 1 132 ASN n 1 133 PRO n 1 134 ASP n 1 135 PRO n 1 136 GLU n 1 137 ILE n 1 138 THR n 1 139 TRP n 1 140 PHE n 1 141 LYS n 1 142 ASP n 1 143 PHE n 1 144 LEU n 1 145 PRO n 1 146 VAL n 1 147 ASP n 1 148 THR n 1 149 SER n 1 150 ASN n 1 151 ASN n 1 152 ASN n 1 153 GLY n 1 154 ARG n 1 155 ILE n 1 156 LYS n 1 157 GLN n 1 158 LEU n 1 159 ARG n 1 160 SER n 1 161 GLU n 1 162 SER n 1 163 ILE n 1 164 GLY n 1 165 GLY n 1 166 THR n 1 167 PRO n 1 168 ILE n 1 169 ARG n 1 170 GLY n 1 171 ALA n 1 172 LEU n 1 173 GLN n 1 174 ILE n 1 175 GLU n 1 176 GLN n 1 177 SER n 1 178 GLU n 1 179 GLU n 1 180 SER n 1 181 ASP n 1 182 GLN n 1 183 GLY n 1 184 LYS n 1 185 TYR n 1 186 GLU n 1 187 CYS n 1 188 VAL n 1 189 ALA n 1 190 THR n 1 191 ASN n 1 192 SER n 1 193 ALA n 1 194 GLY n 1 195 THR n 1 196 ARG n 1 197 TYR n 1 198 SER n 1 199 ALA n 1 200 PRO n 1 201 ALA n 1 202 ASN n 1 203 LEU n 1 204 TYR n 1 205 VAL n 1 206 ARG n 1 207 GLU n 1 208 LEU n 1 209 ARG n 1 210 GLU n 1 211 VAL n 1 212 ARG n 1 213 ARG n 1 214 VAL n 1 215 PRO n 1 216 PRO n 1 217 ARG n 1 218 PHE n 1 219 SER n 1 220 ILE n 1 221 PRO n 1 222 PRO n 1 223 THR n 1 224 ASN n 1 225 HIS n 1 226 GLU n 1 227 ILE n 1 228 MET n 1 229 PRO n 1 230 GLY n 1 231 GLY n 1 232 SER n 1 233 VAL n 1 234 ASN n 1 235 ILE n 1 236 THR n 1 237 CYS n 1 238 VAL n 1 239 ALA n 1 240 VAL n 1 241 GLY n 1 242 SER n 1 243 PRO n 1 244 MET n 1 245 PRO n 1 246 TYR n 1 247 VAL n 1 248 LYS n 1 249 TRP n 1 250 MET n 1 251 LEU n 1 252 GLY n 1 253 ALA n 1 254 GLU n 1 255 ASP n 1 256 LEU n 1 257 THR n 1 258 PRO n 1 259 GLU n 1 260 ASP n 1 261 ASP n 1 262 MET n 1 263 PRO n 1 264 ILE n 1 265 GLY n 1 266 ARG n 1 267 ASN n 1 268 VAL n 1 269 LEU n 1 270 GLU n 1 271 LEU n 1 272 ASN n 1 273 ASP n 1 274 VAL n 1 275 ARG n 1 276 GLN n 1 277 SER n 1 278 ALA n 1 279 ASN n 1 280 TYR n 1 281 THR n 1 282 CYS n 1 283 VAL n 1 284 ALA n 1 285 MET n 1 286 SER n 1 287 THR n 1 288 LEU n 1 289 GLY n 1 290 VAL n 1 291 ILE n 1 292 GLU n 1 293 ALA n 1 294 ILE n 1 295 ALA n 1 296 GLN n 1 297 ILE n 1 298 THR n 1 299 VAL n 1 300 LYS n 1 301 ALA n 1 302 LEU n 1 303 PRO n 1 304 LYS n 1 305 PRO n 1 306 PRO n 1 307 GLY n 1 308 THR n 1 309 PRO n 1 310 VAL n 1 311 VAL n 1 312 THR n 1 313 GLU n 1 314 SER n 1 315 THR n 1 316 ALA n 1 317 THR n 1 318 SER n 1 319 ILE n 1 320 THR n 1 321 LEU n 1 322 THR n 1 323 TRP n 1 324 ASP n 1 325 SER n 1 326 GLY n 1 327 ASN n 1 328 PRO n 1 329 GLU n 1 330 PRO n 1 331 VAL n 1 332 SER n 1 333 TYR n 1 334 TYR n 1 335 ILE n 1 336 ILE n 1 337 GLN n 1 338 HIS n 1 339 LYS n 1 340 PRO n 1 341 LYS n 1 342 ASN n 1 343 SER n 1 344 GLU n 1 345 GLU n 1 346 PRO n 1 347 TYR n 1 348 LYS n 1 349 GLU n 1 350 ILE n 1 351 ASP n 1 352 GLY n 1 353 ILE n 1 354 ALA n 1 355 THR n 1 356 THR n 1 357 ARG n 1 358 TYR n 1 359 SER n 1 360 VAL n 1 361 ALA n 1 362 GLY n 1 363 LEU n 1 364 SER n 1 365 PRO n 1 366 TYR n 1 367 SER n 1 368 ASP n 1 369 TYR n 1 370 GLU n 1 371 PHE n 1 372 ARG n 1 373 VAL n 1 374 VAL n 1 375 ALA n 1 376 VAL n 1 377 ASN n 1 378 ASN n 1 379 ILE n 1 380 GLY n 1 381 ARG n 1 382 GLY n 1 383 PRO n 1 384 ALA n 1 385 SER n 1 386 GLU n 1 387 PRO n 1 388 VAL n 1 389 LEU n 1 390 THR n 1 391 GLN n 1 392 LYS n 1 393 HIS n 1 394 HIS n 1 395 HIS n 1 396 HIS n 1 397 HIS n 1 398 HIS n 2 1 MET n 2 2 LEU n 2 3 SER n 2 4 GLY n 2 5 VAL n 2 6 TRP n 2 7 PHE n 2 8 LEU n 2 9 SER n 2 10 VAL n 2 11 LEU n 2 12 THR n 2 13 VAL n 2 14 ALA n 2 15 GLY n 2 16 ILE n 2 17 LEU n 2 18 GLN n 2 19 THR n 2 20 GLU n 2 21 SER n 2 22 ARG n 2 23 LYS n 2 24 THR n 2 25 ALA n 2 26 LYS n 2 27 ASP n 2 28 ILE n 2 29 CYS n 2 30 LYS n 2 31 ILE n 2 32 ARG n 2 33 CYS n 2 34 LEU n 2 35 CYS n 2 36 GLU n 2 37 GLU n 2 38 LYS n 2 39 GLU n 2 40 ASN n 2 41 VAL n 2 42 LEU n 2 43 ASN n 2 44 ILE n 2 45 ASN n 2 46 CYS n 2 47 GLU n 2 48 ASN n 2 49 LYS n 2 50 GLY n 2 51 PHE n 2 52 THR n 2 53 THR n 2 54 VAL n 2 55 SER n 2 56 LEU n 2 57 LEU n 2 58 GLN n 2 59 PRO n 2 60 PRO n 2 61 GLN n 2 62 TYR n 2 63 ARG n 2 64 ILE n 2 65 TYR n 2 66 GLN n 2 67 LEU n 2 68 PHE n 2 69 LEU n 2 70 ASN n 2 71 GLY n 2 72 ASN n 2 73 LEU n 2 74 LEU n 2 75 THR n 2 76 ARG n 2 77 LEU n 2 78 TYR n 2 79 PRO n 2 80 ASN n 2 81 GLU n 2 82 PHE n 2 83 VAL n 2 84 ASN n 2 85 TYR n 2 86 SER n 2 87 ASN n 2 88 ALA n 2 89 VAL n 2 90 THR n 2 91 LEU n 2 92 HIS n 2 93 LEU n 2 94 GLY n 2 95 ASN n 2 96 ASN n 2 97 GLY n 2 98 LEU n 2 99 GLN n 2 100 GLU n 2 101 ILE n 2 102 ARG n 2 103 PRO n 2 104 GLY n 2 105 ALA n 2 106 PHE n 2 107 SER n 2 108 GLY n 2 109 LEU n 2 110 LYS n 2 111 THR n 2 112 LEU n 2 113 LYS n 2 114 ARG n 2 115 LEU n 2 116 HIS n 2 117 LEU n 2 118 ASN n 2 119 ASN n 2 120 ASN n 2 121 LYS n 2 122 LEU n 2 123 GLU n 2 124 VAL n 2 125 LEU n 2 126 ARG n 2 127 GLU n 2 128 ASP n 2 129 THR n 2 130 PHE n 2 131 LEU n 2 132 GLY n 2 133 LEU n 2 134 GLU n 2 135 SER n 2 136 LEU n 2 137 GLU n 2 138 TYR n 2 139 LEU n 2 140 GLN n 2 141 ALA n 2 142 ASP n 2 143 TYR n 2 144 ASN n 2 145 TYR n 2 146 ILE n 2 147 SER n 2 148 THR n 2 149 ILE n 2 150 GLU n 2 151 ALA n 2 152 GLY n 2 153 ALA n 2 154 PHE n 2 155 SER n 2 156 LYS n 2 157 LEU n 2 158 ASN n 2 159 LYS n 2 160 LEU n 2 161 LYS n 2 162 VAL n 2 163 LEU n 2 164 ILE n 2 165 LEU n 2 166 ASN n 2 167 ASP n 2 168 ASN n 2 169 LEU n 2 170 LEU n 2 171 LEU n 2 172 SER n 2 173 LEU n 2 174 PRO n 2 175 SER n 2 176 ASN n 2 177 VAL n 2 178 PHE n 2 179 ARG n 2 180 PHE n 2 181 VAL n 2 182 LEU n 2 183 LEU n 2 184 THR n 2 185 HIS n 2 186 LEU n 2 187 ASP n 2 188 LEU n 2 189 ARG n 2 190 GLY n 2 191 ASN n 2 192 ARG n 2 193 LEU n 2 194 LYS n 2 195 VAL n 2 196 MET n 2 197 PRO n 2 198 PHE n 2 199 ALA n 2 200 GLY n 2 201 VAL n 2 202 LEU n 2 203 GLU n 2 204 HIS n 2 205 ILE n 2 206 GLY n 2 207 GLY n 2 208 ILE n 2 209 MET n 2 210 GLU n 2 211 ILE n 2 212 GLN n 2 213 LEU n 2 214 GLU n 2 215 GLU n 2 216 ASN n 2 217 PRO n 2 218 TRP n 2 219 ASN n 2 220 CYS n 2 221 THR n 2 222 CYS n 2 223 ASP n 2 224 LEU n 2 225 LEU n 2 226 PRO n 2 227 LEU n 2 228 LYS n 2 229 ALA n 2 230 TRP n 2 231 LEU n 2 232 ASP n 2 233 THR n 2 234 ILE n 2 235 THR n 2 236 VAL n 2 237 PHE n 2 238 VAL n 2 239 GLY n 2 240 GLU n 2 241 ILE n 2 242 VAL n 2 243 CYS n 2 244 GLU n 2 245 THR n 2 246 PRO n 2 247 PHE n 2 248 ARG n 2 249 LEU n 2 250 HIS n 2 251 GLY n 2 252 LYS n 2 253 ASP n 2 254 VAL n 2 255 THR n 2 256 GLN n 2 257 LEU n 2 258 THR n 2 259 ARG n 2 260 GLN n 2 261 ASP n 2 262 LEU n 2 263 CYS n 2 264 PRO n 2 265 ARG n 2 266 LYS n 2 267 HIS n 2 268 HIS n 2 269 HIS n 2 270 HIS n 2 271 HIS n 2 272 HIS n # loop_ _entity_src_gen.entity_id _entity_src_gen.pdbx_src_id _entity_src_gen.pdbx_alt_source_flag _entity_src_gen.pdbx_seq_type _entity_src_gen.pdbx_beg_seq_num _entity_src_gen.pdbx_end_seq_num _entity_src_gen.gene_src_common_name _entity_src_gen.gene_src_genus _entity_src_gen.pdbx_gene_src_gene _entity_src_gen.gene_src_species _entity_src_gen.gene_src_strain _entity_src_gen.gene_src_tissue _entity_src_gen.gene_src_tissue_fraction _entity_src_gen.gene_src_details _entity_src_gen.pdbx_gene_src_fragment _entity_src_gen.pdbx_gene_src_scientific_name _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id _entity_src_gen.pdbx_gene_src_variant _entity_src_gen.pdbx_gene_src_cell_line _entity_src_gen.pdbx_gene_src_atcc _entity_src_gen.pdbx_gene_src_organ _entity_src_gen.pdbx_gene_src_organelle _entity_src_gen.pdbx_gene_src_cell _entity_src_gen.pdbx_gene_src_cellular_location _entity_src_gen.host_org_common_name _entity_src_gen.pdbx_host_org_scientific_name _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id _entity_src_gen.host_org_genus _entity_src_gen.pdbx_host_org_gene _entity_src_gen.pdbx_host_org_organ _entity_src_gen.host_org_species _entity_src_gen.pdbx_host_org_tissue _entity_src_gen.pdbx_host_org_tissue_fraction _entity_src_gen.pdbx_host_org_strain _entity_src_gen.pdbx_host_org_variant _entity_src_gen.pdbx_host_org_cell_line _entity_src_gen.pdbx_host_org_atcc _entity_src_gen.pdbx_host_org_culture_collection _entity_src_gen.pdbx_host_org_cell _entity_src_gen.pdbx_host_org_organelle _entity_src_gen.pdbx_host_org_cellular_location _entity_src_gen.pdbx_host_org_vector_type _entity_src_gen.pdbx_host_org_vector _entity_src_gen.host_org_details _entity_src_gen.expression_system_id _entity_src_gen.plasmid_name _entity_src_gen.plasmid_details _entity_src_gen.pdbx_description 1 1 sample 'Biological sequence' 1 398 Mouse ? Ptprd ? ? ? ? ? ? 'Mus musculus' 10090 ? ? ? ? ? ? ? human 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? HEK293F ? ? ? ? ? plasmid ? ? ? pEBMulti-Neo ? ? 2 1 sample 'Biological sequence' 1 272 Mouse ? Slitrk2 ? ? ? ? ? ? 'Mus musculus' 10090 ? ? ? ? ? ? ? human 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? HEK293F ? ? ? ? ? plasmid ? ? ? ? ? ? # loop_ _struct_ref.db_code _struct_ref.db_name _struct_ref.details _struct_ref.entity_id _struct_ref.id _struct_ref.seq_align _struct_ref.seq_dif _struct_ref.pdbx_db_accession _struct_ref.pdbx_db_isoform _struct_ref.pdbx_seq_one_letter_code _struct_ref.pdbx_align_begin _struct_ref.pdbx_align_end PTPRD_MOUSE UNP ? 1 1 ? ? Q64487 ? ;ETPPRFTRTPVDQTGVSGGVASFICQATGDPRPKIVWNKKGKKVSNQRFEVIEFDDGSGSVLRIQPLRTPRDEAIYECVA SNNVGEISVSTRLTVLREDQIPRGFPTIDMGPQLKVVERTRTATMLCAASGNPDPEITWFKDFLPVDTSNNNGRIKQLRS ESIGGTPIRGALQIEQSEESDQGKYECVATNSAGTRYSAPANLYVRELREVRRVPPRFSIPPTNHEIMPGGSVNITCVAV GSPMPYVKWMLGAEDLTPEDDMPIGRNVLELNDVRQSANYTCVAMSTLGVIEAIAQITVKALPKPPGTPVVTESTATSIT LTWDSGNPEPVSYYIIQHKPKNSEEPYKEIDGIATTRYSVAGLSPYSDYEFRVVAVNNIGRGPASEPVLTQ ; 21 ? SLIK2_MOUSE UNP ? 2 2 ? ? Q810C0 ? ;MLSGVWFLSVLTVAGILQTESRKTAKDICKIRCLCEEKENVLNINCENKGFTTVSLLQPPQYRIYQLFLNGNLLTRLYPN EFVNYSNAVTLHLGNNGLQEIRPGAFSGLKTLKRLHLNNNKLEVLREDTFLGLESLEYLQADYNYISTIEAGAFSKLNKL KVLILNDNLLLSLPSNVFRFVLLTHLDLRGNRLKVMPFAGVLEHIGGIMEIQLEENPWNCTCDLLPLKAWLDTITVFVGE IVCETPFRLHGKDVTQLTRQDLCPRK ; 1 ? # loop_ _struct_ref_seq.align_id _struct_ref_seq.ref_id _struct_ref_seq.pdbx_PDB_id_code _struct_ref_seq.pdbx_strand_id _struct_ref_seq.seq_align_beg _struct_ref_seq.pdbx_seq_align_beg_ins_code _struct_ref_seq.seq_align_end _struct_ref_seq.pdbx_seq_align_end_ins_code _struct_ref_seq.pdbx_db_accession _struct_ref_seq.db_align_beg _struct_ref_seq.pdbx_db_align_beg_ins_code _struct_ref_seq.db_align_end _struct_ref_seq.pdbx_db_align_end_ins_code _struct_ref_seq.pdbx_auth_seq_align_beg _struct_ref_seq.pdbx_auth_seq_align_end 1 1 4Y61 A 1 ? 391 ? Q64487 21 ? 411 ? 28 418 2 2 4Y61 B 1 ? 266 ? Q810C0 1 ? 266 ? 1 266 # loop_ _struct_ref_seq_dif.align_id _struct_ref_seq_dif.pdbx_pdb_id_code _struct_ref_seq_dif.mon_id _struct_ref_seq_dif.pdbx_pdb_strand_id _struct_ref_seq_dif.seq_num _struct_ref_seq_dif.pdbx_pdb_ins_code _struct_ref_seq_dif.pdbx_seq_db_name _struct_ref_seq_dif.pdbx_seq_db_accession_code _struct_ref_seq_dif.db_mon_id _struct_ref_seq_dif.pdbx_seq_db_seq_num _struct_ref_seq_dif.details _struct_ref_seq_dif.pdbx_auth_seq_num _struct_ref_seq_dif.pdbx_ordinal 1 4Y61 LYS A 392 ? UNP Q64487 ? ? 'expression tag' 419 1 1 4Y61 HIS A 393 ? UNP Q64487 ? ? 'expression tag' 420 2 1 4Y61 HIS A 394 ? UNP Q64487 ? ? 'expression tag' 421 3 1 4Y61 HIS A 395 ? UNP Q64487 ? ? 'expression tag' 422 4 1 4Y61 HIS A 396 ? UNP Q64487 ? ? 'expression tag' 423 5 1 4Y61 HIS A 397 ? UNP Q64487 ? ? 'expression tag' 424 6 1 4Y61 HIS A 398 ? UNP Q64487 ? ? 'expression tag' 425 7 2 4Y61 HIS B 267 ? UNP Q810C0 ? ? 'expression tag' 267 8 2 4Y61 HIS B 268 ? UNP Q810C0 ? ? 'expression tag' 268 9 2 4Y61 HIS B 269 ? UNP Q810C0 ? ? 'expression tag' 269 10 2 4Y61 HIS B 270 ? UNP Q810C0 ? ? 'expression tag' 270 11 2 4Y61 HIS B 271 ? UNP Q810C0 ? ? 'expression tag' 271 12 2 4Y61 HIS B 272 ? UNP Q810C0 ? ? 'expression tag' 272 13 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 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 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.absorpt_coefficient_mu ? _exptl.absorpt_correction_T_max ? _exptl.absorpt_correction_T_min ? _exptl.absorpt_correction_type ? _exptl.absorpt_process_details ? _exptl.entry_id 4Y61 _exptl.crystals_number 1 _exptl.details ? _exptl.method 'X-RAY DIFFRACTION' _exptl.method_details ? # _exptl_crystal.colour ? _exptl_crystal.density_diffrn ? _exptl_crystal.density_Matthews 3.24 _exptl_crystal.density_method ? _exptl_crystal.density_percent_sol 62.09 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.id 1 _exptl_crystal.preparation ? _exptl_crystal.size_max ? _exptl_crystal.size_mid ? _exptl_crystal.size_min ? _exptl_crystal.size_rad ? _exptl_crystal.colour_lustre ? _exptl_crystal.colour_modifier ? _exptl_crystal.colour_primary ? _exptl_crystal.density_meas ? _exptl_crystal.density_meas_esd ? _exptl_crystal.density_meas_gt ? _exptl_crystal.density_meas_lt ? _exptl_crystal.density_meas_temp ? _exptl_crystal.density_meas_temp_esd ? _exptl_crystal.density_meas_temp_gt ? _exptl_crystal.density_meas_temp_lt ? _exptl_crystal.pdbx_crystal_image_url ? _exptl_crystal.pdbx_crystal_image_format ? _exptl_crystal.pdbx_mosaicity ? _exptl_crystal.pdbx_mosaicity_esd ? # _exptl_crystal_grow.apparatus ? _exptl_crystal_grow.atmosphere ? _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.details ? _exptl_crystal_grow.method 'VAPOR DIFFUSION, SITTING DROP' _exptl_crystal_grow.method_ref ? _exptl_crystal_grow.pH 6.0 _exptl_crystal_grow.pressure ? _exptl_crystal_grow.pressure_esd ? _exptl_crystal_grow.seeding ? _exptl_crystal_grow.seeding_ref ? _exptl_crystal_grow.temp 293 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.temp_esd ? _exptl_crystal_grow.time ? _exptl_crystal_grow.pdbx_details '15% PEG4000, 0.1 M sodium acetate, 0.1 M MES' _exptl_crystal_grow.pdbx_pH_range 6.0 # _diffrn.ambient_environment ? _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.ambient_temp_esd ? _diffrn.crystal_id 1 _diffrn.crystal_support ? _diffrn.crystal_treatment ? _diffrn.details ? _diffrn.id 1 _diffrn.ambient_pressure ? _diffrn.ambient_pressure_esd ? _diffrn.ambient_pressure_gt ? _diffrn.ambient_pressure_lt ? _diffrn.ambient_temp_gt ? _diffrn.ambient_temp_lt ? # _diffrn_detector.details ? _diffrn_detector.detector PIXEL _diffrn_detector.diffrn_id 1 _diffrn_detector.type 'DECTRIS PILATUS 6M' _diffrn_detector.area_resol_mean ? _diffrn_detector.dtime ? _diffrn_detector.pdbx_frames_total ? _diffrn_detector.pdbx_collection_time_total ? _diffrn_detector.pdbx_collection_date 2014-10-22 # _diffrn_radiation.collimation ? _diffrn_radiation.diffrn_id 1 _diffrn_radiation.filter_edge ? _diffrn_radiation.inhomogeneity ? _diffrn_radiation.monochromator ? _diffrn_radiation.polarisn_norm ? _diffrn_radiation.polarisn_ratio ? _diffrn_radiation.probe ? _diffrn_radiation.type ? _diffrn_radiation.xray_symbol ? _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.pdbx_wavelength_list ? _diffrn_radiation.pdbx_wavelength ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_analyzer ? _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.0000 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.current ? _diffrn_source.details ? _diffrn_source.diffrn_id 1 _diffrn_source.power ? _diffrn_source.size ? _diffrn_source.source SYNCHROTRON _diffrn_source.target ? _diffrn_source.type 'SPRING-8 BEAMLINE BL41XU' _diffrn_source.voltage ? _diffrn_source.take-off_angle ? _diffrn_source.pdbx_wavelength_list 1.0000 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_synchrotron_beamline BL41XU _diffrn_source.pdbx_synchrotron_site SPring-8 # _reflns.B_iso_Wilson_estimate ? _reflns.entry_id 4Y61 _reflns.data_reduction_details ? _reflns.data_reduction_method ? _reflns.d_resolution_high 3.35 _reflns.d_resolution_low 50 _reflns.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.number_all ? _reflns.number_obs 14509 _reflns.observed_criterion ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.observed_criterion_I_max ? _reflns.observed_criterion_I_min ? _reflns.observed_criterion_sigma_F ? _reflns.observed_criterion_sigma_I ? _reflns.percent_possible_obs 99.2 _reflns.R_free_details ? _reflns.Rmerge_F_all ? _reflns.Rmerge_F_obs ? _reflns.Friedel_coverage ? _reflns.number_gt ? _reflns.threshold_expression ? _reflns.pdbx_redundancy 9.5 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rmerge_I_all ? _reflns.pdbx_Rsym_value 0.13 _reflns.pdbx_netI_over_av_sigmaI ? _reflns.pdbx_netI_over_sigmaI 14.3 _reflns.pdbx_res_netI_over_av_sigmaI_2 ? _reflns.pdbx_res_netI_over_sigmaI_2 ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_d_res_high_opt ? _reflns.pdbx_d_res_low_opt ? _reflns.pdbx_d_res_opt_method ? _reflns.phase_calculation_details ? _reflns.pdbx_Rrim_I_all ? _reflns.pdbx_Rpim_I_all ? _reflns.pdbx_d_opt ? _reflns.pdbx_number_measured_all ? _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.pdbx_CC_half ? _reflns.pdbx_R_split ? # _reflns_shell.d_res_high 3.35 _reflns_shell.d_res_low 3.41 _reflns_shell.meanI_over_sigI_all ? _reflns_shell.meanI_over_sigI_obs 1.9 _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_possible ? _reflns_shell.number_unique_all ? _reflns_shell.number_unique_obs ? _reflns_shell.percent_possible_all 97.2 _reflns_shell.percent_possible_obs ? _reflns_shell.Rmerge_F_all ? _reflns_shell.Rmerge_F_obs ? _reflns_shell.Rmerge_I_all ? _reflns_shell.Rmerge_I_obs 0.407 _reflns_shell.meanI_over_sigI_gt ? _reflns_shell.meanI_over_uI_all ? _reflns_shell.meanI_over_uI_gt ? _reflns_shell.number_measured_gt ? _reflns_shell.number_unique_gt ? _reflns_shell.percent_possible_gt ? _reflns_shell.Rmerge_F_gt ? _reflns_shell.Rmerge_I_gt ? _reflns_shell.pdbx_redundancy 5.9 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_netI_over_sigmaI_all ? _reflns_shell.pdbx_netI_over_sigmaI_obs ? _reflns_shell.pdbx_Rrim_I_all ? _reflns_shell.pdbx_Rpim_I_all ? _reflns_shell.pdbx_rejects ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_CC_half ? _reflns_shell.pdbx_R_split ? # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 4Y61 _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 14477 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 1.48 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 45.654 _refine.ls_d_res_high 3.358 _refine.ls_percent_reflns_obs 99.08 _refine.ls_R_factor_obs 0.2373 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.2346 _refine.ls_R_factor_R_free 0.2865 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.03 _refine.ls_number_reflns_R_free 728 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.B_iso_mean ? _refine.aniso_B[1][1] ? _refine.aniso_B[2][2] ? _refine.aniso_B[3][3] ? _refine.aniso_B[1][2] ? _refine.aniso_B[1][3] ? _refine.aniso_B[2][3] ? _refine.solvent_model_details 'FLAT BULK SOLVENT MODEL' _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.11 _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii 0.90 _refine.pdbx_ls_cross_valid_method 'FREE R-VALUE' _refine.details ? _refine.pdbx_starting_model '2YD6, 2YD9, 2DJU, and 1OZN' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values ML _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details ? _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML 0.51 _refine.pdbx_overall_phase_error 30.07 _refine.overall_SU_B ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 4891 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 56 _refine_hist.number_atoms_solvent 0 _refine_hist.number_atoms_total 4947 _refine_hist.d_res_high 3.358 _refine_hist.d_res_low 45.654 # 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 f_bond_d 0.005 ? ? 5058 'X-RAY DIFFRACTION' ? f_angle_d 1.113 ? ? 6881 'X-RAY DIFFRACTION' ? f_dihedral_angle_d 16.147 ? ? 1901 'X-RAY DIFFRACTION' ? f_chiral_restr 0.040 ? ? 800 'X-RAY DIFFRACTION' ? f_plane_restr 0.005 ? ? 899 'X-RAY DIFFRACTION' ? # loop_ _refine_ls_shell.pdbx_refine_id _refine_ls_shell.pdbx_total_number_of_bins_used _refine_ls_shell.d_res_high _refine_ls_shell.d_res_low _refine_ls_shell.number_reflns_R_work _refine_ls_shell.R_factor_R_work _refine_ls_shell.percent_reflns_obs _refine_ls_shell.R_factor_R_free _refine_ls_shell.R_factor_R_free_error _refine_ls_shell.percent_reflns_R_free _refine_ls_shell.number_reflns_R_free _refine_ls_shell.number_reflns_all _refine_ls_shell.R_factor_all _refine_ls_shell.R_factor_obs _refine_ls_shell.number_reflns_obs 'X-RAY DIFFRACTION' . 3.3577 3.6168 2675 0.2919 98.00 0.3544 . . 141 . . . . 'X-RAY DIFFRACTION' . 3.6168 3.9806 2694 0.2620 99.00 0.2823 . . 149 . . . . 'X-RAY DIFFRACTION' . 3.9806 4.5562 2733 0.2119 100.00 0.3013 . . 153 . . . . 'X-RAY DIFFRACTION' . 4.5562 5.7385 2754 0.2097 99.00 0.2609 . . 143 . . . . 'X-RAY DIFFRACTION' . 5.7385 45.6582 2893 0.2370 99.00 0.2783 . . 142 . . . . # _struct.entry_id 4Y61 _struct.title 'Crystal structure of the complex between Slitrk2 LRR1 and PTP delta Ig1-Fn1' _struct.pdbx_descriptor 'Receptor-type tyrosine-protein phosphatase delta(E.C.3.1.3.48), SLIT and NTRK-like protein 2' _struct.pdbx_model_details ? _struct.pdbx_formula_weight ? _struct.pdbx_formula_weight_method ? _struct.pdbx_model_type_details ? _struct.pdbx_CASP_flag ? # _struct_keywords.entry_id 4Y61 _struct_keywords.text 'trans-synaptic complex, HYDROLASE-SIGNALING PROTEIN complex' _struct_keywords.pdbx_keywords 'HYDROLASE/SIGNALING PROTEIN' # 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 3 ? F N N 3 ? # 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 AA1 ARG A 97 ? ILE A 101 ? ARG A 124 ILE A 128 5 ? 5 HELX_P HELX_P2 AA2 GLU A 178 ? GLN A 182 ? GLU A 205 GLN A 209 5 ? 5 HELX_P HELX_P3 AA3 ALA B 151 ? SER B 155 ? ALA B 151 SER B 155 5 ? 5 HELX_P HELX_P4 AA4 GLY B 200 ? ILE B 205 ? GLY B 200 ILE B 205 1 ? 6 HELX_P HELX_P5 AA5 THR B 221 ? ASP B 223 ? THR B 221 ASP B 223 5 ? 3 HELX_P HELX_P6 AA6 LEU B 224 ? ILE B 234 ? LEU B 224 ILE B 234 1 ? 11 HELX_P HELX_P7 AA7 PRO B 246 ? HIS B 250 ? PRO B 246 HIS B 250 5 ? 5 HELX_P HELX_P8 AA8 THR B 258 ? CYS B 263 ? THR B 258 CYS B 263 1 ? 6 # _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 25 SG ? ? ? 1_555 A CYS 78 SG ? ? A CYS 52 A CYS 105 1_555 ? ? ? ? ? ? ? 2.034 ? disulf2 disulf ? ? A CYS 127 SG ? ? ? 1_555 A CYS 187 SG ? ? A CYS 154 A CYS 214 1_555 ? ? ? ? ? ? ? 2.031 ? disulf3 disulf ? ? A CYS 237 SG ? ? ? 1_555 A CYS 282 SG ? ? A CYS 264 A CYS 309 1_555 ? ? ? ? ? ? ? 2.033 ? disulf4 disulf ? ? B CYS 29 SG ? ? ? 1_555 B CYS 35 SG ? ? B CYS 29 B CYS 35 1_555 ? ? ? ? ? ? ? 2.028 ? disulf5 disulf ? ? B CYS 33 SG ? ? ? 1_555 B CYS 46 SG ? ? B CYS 33 B CYS 46 1_555 ? ? ? ? ? ? ? 2.027 ? disulf6 disulf ? ? B CYS 220 SG ? ? ? 1_555 B CYS 243 SG ? ? B CYS 220 B CYS 243 1_555 ? ? ? ? ? ? ? 2.029 ? disulf7 disulf ? ? B CYS 222 SG ? ? ? 1_555 B CYS 263 SG ? ? B CYS 222 B CYS 263 1_555 ? ? ? ? ? ? ? 2.033 ? covale1 covale one ? A ASN 234 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 261 A NAG 501 1_555 ? ? ? ? ? ? ? 1.442 ? covale2 covale one ? A ASN 279 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 306 A NAG 502 1_555 ? ? ? ? ? ? ? 1.453 ? covale3 covale one ? B ASN 84 ND2 ? ? ? 1_555 F NAG . C1 ? ? B ASN 84 B NAG 302 1_555 ? ? ? ? ? ? ? 1.438 ? covale4 covale one ? B ASN 219 ND2 ? ? ? 1_555 E NAG . C1 ? ? B ASN 219 B NAG 301 1_555 ? ? ? ? ? ? ? 1.434 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 ASP 30 A . ? ASP 57 A PRO 31 A ? PRO 58 A 1 5.57 2 GLN 65 A . ? GLN 92 A PRO 66 A ? PRO 93 A 1 -12.06 3 THR 69 A . ? THR 96 A PRO 70 A ? PRO 97 A 1 3.34 4 ASN 132 A . ? ASN 159 A PRO 133 A ? PRO 160 A 1 -1.26 5 SER 160 A . ? SER 187 A GLU 161 A ? GLU 188 A 1 7.12 6 ILE 163 A . ? ILE 190 A GLY 164 A ? GLY 191 A 1 0.73 7 GLY 230 A . ? GLY 257 A GLY 231 A ? GLY 258 A 1 -3.27 8 SER 242 A . ? SER 269 A PRO 243 A ? PRO 270 A 1 -2.22 9 THR 245 B . ? THR 245 B PRO 246 B ? PRO 246 B 1 -1.85 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA1 ? 4 ? AA2 ? 5 ? AA3 ? 4 ? AA4 ? 5 ? AA5 ? 4 ? AA6 ? 3 ? AA7 ? 5 ? AA8 ? 3 ? AA9 ? 4 ? AB1 ? 9 ? AB2 ? 2 ? AB3 ? 2 ? AB4 ? 2 ? # 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 AA1 1 2 ? anti-parallel AA1 2 3 ? anti-parallel AA1 3 4 ? anti-parallel AA2 1 2 ? parallel AA2 2 3 ? anti-parallel AA2 3 4 ? anti-parallel AA2 4 5 ? anti-parallel AA3 1 2 ? anti-parallel AA3 2 3 ? anti-parallel AA3 3 4 ? anti-parallel AA4 1 2 ? parallel AA4 2 3 ? anti-parallel AA4 3 4 ? anti-parallel AA4 4 5 ? anti-parallel AA5 1 2 ? parallel AA5 2 3 ? anti-parallel AA5 3 4 ? anti-parallel AA6 1 2 ? anti-parallel AA6 2 3 ? anti-parallel AA7 1 2 ? parallel AA7 2 3 ? anti-parallel AA7 3 4 ? anti-parallel AA7 4 5 ? anti-parallel AA8 1 2 ? anti-parallel AA8 2 3 ? anti-parallel AA9 1 2 ? anti-parallel AA9 2 3 ? anti-parallel AA9 3 4 ? anti-parallel AB1 1 2 ? anti-parallel AB1 2 3 ? parallel AB1 3 4 ? parallel AB1 4 5 ? parallel AB1 5 6 ? parallel AB1 6 7 ? parallel AB1 7 8 ? parallel AB1 8 9 ? parallel AB2 1 2 ? parallel AB3 1 2 ? parallel AB4 1 2 ? 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 AA1 1 THR A 2 ? ARG A 8 ? THR A 29 ARG A 35 AA1 2 ALA A 21 ? ASP A 30 ? ALA A 48 ASP A 57 AA1 3 GLY A 59 ? ILE A 64 ? GLY A 86 ILE A 91 AA1 4 PHE A 49 ? GLU A 53 ? PHE A 76 GLU A 80 AA2 1 GLN A 13 ? VAL A 16 ? GLN A 40 VAL A 43 AA2 2 GLY A 85 ? LEU A 96 ? GLY A 112 LEU A 123 AA2 3 ALA A 74 ? ASN A 82 ? ALA A 101 ASN A 109 AA2 4 LYS A 34 ? LYS A 39 ? LYS A 61 LYS A 66 AA2 5 LYS A 42 ? LYS A 43 ? LYS A 69 LYS A 70 AA3 1 THR A 107 ? MET A 110 ? THR A 134 MET A 137 AA3 2 ALA A 123 ? SER A 130 ? ALA A 150 SER A 157 AA3 3 ILE A 168 ? ILE A 174 ? ILE A 195 ILE A 201 AA3 4 ILE A 155 ? LEU A 158 ? ILE A 182 LEU A 185 AA4 1 LYS A 115 ? GLU A 118 ? LYS A 142 GLU A 145 AA4 2 ALA A 201 ? ARG A 206 ? ALA A 228 ARG A 233 AA4 3 GLY A 183 ? ASN A 191 ? GLY A 210 ASN A 218 AA4 4 GLU A 136 ? LYS A 141 ? GLU A 163 LYS A 168 AA4 5 LEU A 144 ? PRO A 145 ? LEU A 171 PRO A 172 AA5 1 LYS A 115 ? GLU A 118 ? LYS A 142 GLU A 145 AA5 2 ALA A 201 ? ARG A 206 ? ALA A 228 ARG A 233 AA5 3 GLY A 183 ? ASN A 191 ? GLY A 210 ASN A 218 AA5 4 GLY A 194 ? TYR A 197 ? GLY A 221 TYR A 224 AA6 1 VAL A 214 ? ILE A 220 ? VAL A 241 ILE A 247 AA6 2 VAL A 233 ? SER A 242 ? VAL A 260 SER A 269 AA6 3 ARG A 266 ? LEU A 271 ? ARG A 293 LEU A 298 AA7 1 HIS A 225 ? ILE A 227 ? HIS A 252 ILE A 254 AA7 2 GLY A 289 ? VAL A 299 ? GLY A 316 VAL A 326 AA7 3 ALA A 278 ? SER A 286 ? ALA A 305 SER A 313 AA7 4 TYR A 246 ? LEU A 251 ? TYR A 273 LEU A 278 AA7 5 GLU A 254 ? ASP A 255 ? GLU A 281 ASP A 282 AA8 1 GLY A 307 ? THR A 315 ? GLY A 334 THR A 342 AA8 2 SER A 318 ? ASP A 324 ? SER A 345 ASP A 351 AA8 3 ARG A 357 ? ALA A 361 ? ARG A 384 ALA A 388 AA9 1 LYS A 348 ? ILE A 353 ? LYS A 375 ILE A 380 AA9 2 TYR A 333 ? LYS A 339 ? TYR A 360 LYS A 366 AA9 3 TYR A 369 ? VAL A 376 ? TYR A 396 VAL A 403 AA9 4 VAL A 388 ? THR A 390 ? VAL A 415 THR A 417 AB1 1 LEU B 34 ? GLU B 37 ? LEU B 34 GLU B 37 AB1 2 LEU B 42 ? ASN B 45 ? LEU B 42 ASN B 45 AB1 3 TYR B 65 ? PHE B 68 ? TYR B 65 PHE B 68 AB1 4 ALA B 88 ? HIS B 92 ? ALA B 88 HIS B 92 AB1 5 ARG B 114 ? HIS B 116 ? ARG B 114 HIS B 116 AB1 6 TYR B 138 ? GLN B 140 ? TYR B 138 GLN B 140 AB1 7 VAL B 162 ? ILE B 164 ? VAL B 162 ILE B 164 AB1 8 HIS B 185 ? ASP B 187 ? HIS B 185 ASP B 187 AB1 9 GLU B 210 ? GLN B 212 ? GLU B 210 GLN B 212 AB2 1 ARG B 76 ? LEU B 77 ? ARG B 76 LEU B 77 AB2 2 GLU B 100 ? ILE B 101 ? GLU B 100 ILE B 101 AB3 1 VAL B 124 ? LEU B 125 ? VAL B 124 LEU B 125 AB3 2 THR B 148 ? ILE B 149 ? THR B 148 ILE B 149 AB4 1 TRP B 218 ? ASN B 219 ? TRP B 218 ASN B 219 AB4 2 CYS B 243 ? THR B 245 ? CYS B 243 THR B 245 # 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 AA1 1 2 N ARG A 5 ? N ARG A 32 O THR A 28 ? O THR A 55 AA1 2 3 N ALA A 21 ? N ALA A 48 O ILE A 64 ? O ILE A 91 AA1 3 4 O ARG A 63 ? O ARG A 90 N GLU A 50 ? N GLU A 77 AA2 1 2 N GLY A 15 ? N GLY A 42 O LEU A 96 ? O LEU A 123 AA2 2 3 O LEU A 93 ? O LEU A 120 N ALA A 74 ? N ALA A 101 AA2 3 4 O VAL A 79 ? O VAL A 106 N VAL A 36 ? N VAL A 63 AA2 4 5 N LYS A 39 ? N LYS A 66 O LYS A 42 ? O LYS A 69 AA3 1 2 N MET A 110 ? N MET A 137 O ALA A 128 ? O ALA A 155 AA3 2 3 N CYS A 127 ? N CYS A 154 O GLY A 170 ? O GLY A 197 AA3 3 4 O GLN A 173 ? O GLN A 200 N LYS A 156 ? N LYS A 183 AA4 1 2 N VAL A 117 ? N VAL A 144 O TYR A 204 ? O TYR A 231 AA4 2 3 O ALA A 201 ? O ALA A 228 N TYR A 185 ? N TYR A 212 AA4 3 4 O VAL A 188 ? O VAL A 215 N THR A 138 ? N THR A 165 AA4 4 5 N LYS A 141 ? N LYS A 168 O LEU A 144 ? O LEU A 171 AA5 1 2 N VAL A 117 ? N VAL A 144 O TYR A 204 ? O TYR A 231 AA5 2 3 O ALA A 201 ? O ALA A 228 N TYR A 185 ? N TYR A 212 AA5 3 4 N ALA A 189 ? N ALA A 216 O ARG A 196 ? O ARG A 223 AA6 1 2 N ARG A 217 ? N ARG A 244 O VAL A 240 ? O VAL A 267 AA6 2 3 N VAL A 233 ? N VAL A 260 O LEU A 271 ? O LEU A 298 AA7 1 2 N ILE A 227 ? N ILE A 254 O THR A 298 ? O THR A 325 AA7 2 3 O ILE A 291 ? O ILE A 318 N ALA A 284 ? N ALA A 311 AA7 3 4 O THR A 281 ? O THR A 308 N MET A 250 ? N MET A 277 AA7 4 5 N LEU A 251 ? N LEU A 278 O GLU A 254 ? O GLU A 281 AA8 1 2 N GLU A 313 ? N GLU A 340 O THR A 320 ? O THR A 347 AA8 2 3 N ILE A 319 ? N ILE A 346 O VAL A 360 ? O VAL A 387 AA9 1 2 O LYS A 348 ? O LYS A 375 N HIS A 338 ? N HIS A 365 AA9 2 3 N ILE A 335 ? N ILE A 362 O VAL A 374 ? O VAL A 401 AA9 3 4 N TYR A 369 ? N TYR A 396 O THR A 390 ? O THR A 417 AB1 1 2 N LEU B 34 ? N LEU B 34 O ASN B 45 ? O ASN B 45 AB1 2 3 N ILE B 44 ? N ILE B 44 O PHE B 68 ? O PHE B 68 AB1 3 4 N TYR B 65 ? N TYR B 65 O VAL B 89 ? O VAL B 89 AB1 4 5 O VAL B 89 ? O VAL B 89 N ARG B 114 ? N ARG B 114 AB1 5 6 N LEU B 115 ? N LEU B 115 O GLN B 140 ? O GLN B 140 AB1 6 7 N LEU B 139 ? N LEU B 139 O ILE B 164 ? O ILE B 164 AB1 7 8 N LEU B 163 ? N LEU B 163 O HIS B 185 ? O HIS B 185 AB1 8 9 N LEU B 186 ? N LEU B 186 O GLN B 212 ? O GLN B 212 AB2 1 2 N LEU B 77 ? N LEU B 77 O GLU B 100 ? O GLU B 100 AB3 1 2 N LEU B 125 ? N LEU B 125 O THR B 148 ? O THR B 148 AB4 1 2 N TRP B 218 ? N TRP B 218 O THR B 245 ? O THR B 245 # 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 A NAG 501 ? 1 'binding site for Mono-Saccharide NAG A 501 bound to ASN A 261' AC2 Software A NAG 502 ? 2 'binding site for Mono-Saccharide NAG A 502 bound to ASN A 306' AC3 Software B NAG 302 ? 3 'binding site for Mono-Saccharide NAG B 302 bound to ASN B 84' AC4 Software B NAG 301 ? 3 'binding site for Mono-Saccharide NAG B 301 bound to ASN B 219' # 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 1 ASN A 234 ? ASN A 261 . ? 1_555 ? 2 AC2 2 ASN A 279 ? ASN A 306 . ? 1_555 ? 3 AC2 2 GLN A 296 ? GLN A 323 . ? 1_555 ? 4 AC3 3 GLU B 81 ? GLU B 81 . ? 1_555 ? 5 AC3 3 VAL B 83 ? VAL B 83 . ? 1_555 ? 6 AC3 3 ASN B 84 ? ASN B 84 . ? 1_555 ? 7 AC4 3 LYS B 194 ? LYS B 194 . ? 1_555 ? 8 AC4 3 ASN B 219 ? ASN B 219 . ? 1_555 ? 9 AC4 3 THR B 221 ? THR B 221 . ? 1_555 ? # _atom_sites.entry_id 4Y61 _atom_sites.fract_transf_matrix[1][1] 0.011464 _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] 0.010952 _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] 0.008104 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . GLU A 1 1 ? -18.775 -48.710 21.984 1.00 120.30 ? 28 GLU A N 1 ATOM 2 C CA . GLU A 1 1 ? -17.725 -47.705 22.095 1.00 115.96 ? 28 GLU A CA 1 ATOM 3 C C . GLU A 1 1 ? -16.528 -48.006 21.208 1.00 112.05 ? 28 GLU A C 1 ATOM 4 O O . GLU A 1 1 ? -16.170 -49.165 21.009 1.00 114.70 ? 28 GLU A O 1 ATOM 5 C CB . GLU A 1 1 ? -17.237 -47.587 23.534 1.00 119.10 ? 28 GLU A CB 1 ATOM 6 C CG . GLU A 1 1 ? -18.138 -46.844 24.485 1.00 123.74 ? 28 GLU A CG 1 ATOM 7 C CD . GLU A 1 1 ? -17.598 -46.893 25.895 1.00 126.94 ? 28 GLU A CD 1 ATOM 8 O OE1 . GLU A 1 1 ? -16.767 -47.784 26.158 1.00 130.82 ? 28 GLU A OE1 1 ATOM 9 O OE2 . GLU A 1 1 ? -17.989 -46.049 26.729 1.00 125.74 ? 28 GLU A OE2 1 ATOM 10 N N . THR A 1 2 ? -15.938 -46.961 20.638 1.00 105.74 ? 29 THR A N 1 ATOM 11 C CA . THR A 1 2 ? -14.782 -47.135 19.769 1.00 98.84 ? 29 THR A CA 1 ATOM 12 C C . THR A 1 2 ? -13.744 -46.080 20.147 1.00 95.66 ? 29 THR A C 1 ATOM 13 O O . THR A 1 2 ? -14.095 -44.943 20.470 1.00 93.58 ? 29 THR A O 1 ATOM 14 C CB . THR A 1 2 ? -15.138 -47.001 18.278 1.00 99.06 ? 29 THR A CB 1 ATOM 15 O OG1 . THR A 1 2 ? -15.489 -45.646 17.982 1.00 102.61 ? 29 THR A OG1 1 ATOM 16 C CG2 . THR A 1 2 ? -16.300 -47.922 17.902 1.00 103.82 ? 29 THR A CG2 1 ATOM 17 N N . PRO A 1 3 ? -12.455 -46.449 20.098 1.00 95.18 ? 30 PRO A N 1 ATOM 18 C CA . PRO A 1 3 ? -11.362 -45.530 20.445 1.00 87.83 ? 30 PRO A CA 1 ATOM 19 C C . PRO A 1 3 ? -11.187 -44.437 19.386 1.00 89.80 ? 30 PRO A C 1 ATOM 20 O O . PRO A 1 3 ? -11.736 -44.584 18.289 1.00 90.74 ? 30 PRO A O 1 ATOM 21 C CB . PRO A 1 3 ? -10.134 -46.454 20.533 1.00 81.50 ? 30 PRO A CB 1 ATOM 22 C CG . PRO A 1 3 ? -10.516 -47.691 19.814 1.00 89.00 ? 30 PRO A CG 1 ATOM 23 C CD . PRO A 1 3 ? -11.990 -47.839 19.966 1.00 97.81 ? 30 PRO A CD 1 ATOM 24 N N . PRO A 1 4 ? -10.453 -43.352 19.706 1.00 91.62 ? 31 PRO A N 1 ATOM 25 C CA . PRO A 1 4 ? -10.309 -42.271 18.721 1.00 93.01 ? 31 PRO A CA 1 ATOM 26 C C . PRO A 1 4 ? -9.466 -42.642 17.501 1.00 98.81 ? 31 PRO A C 1 ATOM 27 O O . PRO A 1 4 ? -8.577 -43.486 17.603 1.00 96.66 ? 31 PRO A O 1 ATOM 28 C CB . PRO A 1 4 ? -9.616 -41.157 19.518 1.00 93.10 ? 31 PRO A CB 1 ATOM 29 C CG . PRO A 1 4 ? -9.801 -41.515 20.952 1.00 93.77 ? 31 PRO A CG 1 ATOM 30 C CD . PRO A 1 4 ? -9.831 -43.004 20.994 1.00 94.65 ? 31 PRO A CD 1 ATOM 31 N N . ARG A 1 5 ? -9.751 -41.998 16.370 1.00 108.98 ? 32 ARG A N 1 ATOM 32 C CA . ARG A 1 5 ? -9.004 -42.182 15.129 1.00 115.23 ? 32 ARG A CA 1 ATOM 33 C C . ARG A 1 5 ? -8.896 -40.871 14.366 1.00 112.85 ? 32 ARG A C 1 ATOM 34 O O . ARG A 1 5 ? -9.907 -40.201 14.154 1.00 115.89 ? 32 ARG A O 1 ATOM 35 C CB . ARG A 1 5 ? -9.678 -43.220 14.227 1.00 125.85 ? 32 ARG A CB 1 ATOM 36 C CG . ARG A 1 5 ? -9.711 -44.625 14.789 1.00 143.31 ? 32 ARG A CG 1 ATOM 37 C CD . ARG A 1 5 ? -8.310 -45.171 14.978 1.00 158.11 ? 32 ARG A CD 1 ATOM 38 N NE . ARG A 1 5 ? -8.334 -46.486 15.608 1.00 171.79 ? 32 ARG A NE 1 ATOM 39 C CZ . ARG A 1 5 ? -8.394 -46.687 16.921 1.00 180.98 ? 32 ARG A CZ 1 ATOM 40 N NH1 . ARG A 1 5 ? -8.437 -45.659 17.755 1.00 181.51 ? 32 ARG A NH1 1 ATOM 41 N NH2 . ARG A 1 5 ? -8.412 -47.921 17.403 1.00 186.90 ? 32 ARG A NH2 1 ATOM 42 N N . PHE A 1 6 ? -7.693 -40.503 13.941 1.00 96.82 ? 33 PHE A N 1 ATOM 43 C CA . PHE A 1 6 ? -7.514 -39.209 13.294 1.00 85.79 ? 33 PHE A CA 1 ATOM 44 C C . PHE A 1 6 ? -8.146 -39.247 11.907 1.00 83.85 ? 33 PHE A C 1 ATOM 45 O O . PHE A 1 6 ? -7.991 -40.233 11.183 1.00 88.86 ? 33 PHE A O 1 ATOM 46 C CB . PHE A 1 6 ? -6.032 -38.851 13.176 1.00 79.47 ? 33 PHE A CB 1 ATOM 47 C CG . PHE A 1 6 ? -5.372 -38.528 14.484 1.00 74.86 ? 33 PHE A CG 1 ATOM 48 C CD1 . PHE A 1 6 ? -5.704 -37.375 15.177 1.00 68.51 ? 33 PHE A CD1 1 ATOM 49 C CD2 . PHE A 1 6 ? -4.392 -39.362 15.002 1.00 72.14 ? 33 PHE A CD2 1 ATOM 50 C CE1 . PHE A 1 6 ? -5.087 -37.069 16.373 1.00 62.95 ? 33 PHE A CE1 1 ATOM 51 C CE2 . PHE A 1 6 ? -3.768 -39.061 16.199 1.00 65.22 ? 33 PHE A CE2 1 ATOM 52 C CZ . PHE A 1 6 ? -4.117 -37.913 16.886 1.00 64.08 ? 33 PHE A CZ 1 ATOM 53 N N . THR A 1 7 ? -8.885 -38.202 11.545 1.00 74.68 ? 34 THR A N 1 ATOM 54 C CA . THR A 1 7 ? -9.321 -38.049 10.163 1.00 77.33 ? 34 THR A CA 1 ATOM 55 C C . THR A 1 7 ? -8.529 -36.953 9.460 1.00 76.52 ? 34 THR A C 1 ATOM 56 O O . THR A 1 7 ? -8.486 -36.889 8.229 1.00 77.86 ? 34 THR A O 1 ATOM 57 C CB . THR A 1 7 ? -10.824 -37.718 10.083 1.00 79.36 ? 34 THR A CB 1 ATOM 58 O OG1 . THR A 1 7 ? -11.061 -36.390 10.572 1.00 77.96 ? 34 THR A OG1 1 ATOM 59 C CG2 . THR A 1 7 ? -11.629 -38.706 10.912 1.00 78.84 ? 34 THR A CG2 1 ATOM 60 N N . ARG A 1 8 ? -7.906 -36.093 10.263 1.00 63.99 ? 35 ARG A N 1 ATOM 61 C CA . ARG A 1 8 ? -7.004 -35.061 9.761 1.00 57.11 ? 35 ARG A CA 1 ATOM 62 C C . ARG A 1 8 ? -5.850 -34.834 10.725 1.00 60.12 ? 35 ARG A C 1 ATOM 63 O O . ARG A 1 8 ? -6.068 -34.444 11.873 1.00 63.09 ? 35 ARG A O 1 ATOM 64 C CB . ARG A 1 8 ? -7.743 -33.748 9.516 1.00 59.73 ? 35 ARG A CB 1 ATOM 65 C CG . ARG A 1 8 ? -6.867 -32.698 8.837 1.00 74.30 ? 35 ARG A CG 1 ATOM 66 C CD . ARG A 1 8 ? -7.678 -31.593 8.183 1.00 84.10 ? 35 ARG A CD 1 ATOM 67 N NE . ARG A 1 8 ? -6.869 -30.837 7.234 1.00 87.39 ? 35 ARG A NE 1 ATOM 68 C CZ . ARG A 1 8 ? -7.331 -29.841 6.488 1.00 93.27 ? 35 ARG A CZ 1 ATOM 69 N NH1 . ARG A 1 8 ? -8.602 -29.480 6.585 1.00 100.02 ? 35 ARG A NH1 1 ATOM 70 N NH2 . ARG A 1 8 ? -6.526 -29.208 5.647 1.00 90.65 ? 35 ARG A NH2 1 ATOM 71 N N . THR A 1 9 ? -4.627 -35.073 10.260 1.00 68.31 ? 36 THR A N 1 ATOM 72 C CA . THR A 1 9 ? -3.443 -34.845 11.079 1.00 72.88 ? 36 THR A CA 1 ATOM 73 C C . THR A 1 9 ? -2.680 -33.599 10.623 1.00 80.96 ? 36 THR A C 1 ATOM 74 O O . THR A 1 9 ? -2.628 -33.308 9.431 1.00 89.15 ? 36 THR A O 1 ATOM 75 C CB . THR A 1 9 ? -2.494 -36.050 11.014 1.00 73.13 ? 36 THR A CB 1 ATOM 76 O OG1 . THR A 1 9 ? -1.949 -36.159 9.690 1.00 83.57 ? 36 THR A OG1 1 ATOM 77 C CG2 . THR A 1 9 ? -3.232 -37.336 11.345 1.00 68.73 ? 36 THR A CG2 1 ATOM 78 N N . PRO A 1 10 ? -2.048 -32.890 11.573 1.00 79.35 ? 37 PRO A N 1 ATOM 79 C CA . PRO A 1 10 ? -1.272 -31.684 11.257 1.00 83.79 ? 37 PRO A CA 1 ATOM 80 C C . PRO A 1 10 ? 0.012 -32.002 10.498 1.00 86.78 ? 37 PRO A C 1 ATOM 81 O O . PRO A 1 10 ? 0.521 -33.114 10.618 1.00 91.08 ? 37 PRO A O 1 ATOM 82 C CB . PRO A 1 10 ? -0.965 -31.099 12.639 1.00 83.14 ? 37 PRO A CB 1 ATOM 83 C CG . PRO A 1 10 ? -0.987 -32.264 13.555 1.00 80.91 ? 37 PRO A CG 1 ATOM 84 C CD . PRO A 1 10 ? -2.057 -33.183 13.019 1.00 79.19 ? 37 PRO A CD 1 ATOM 85 N N . VAL A 1 11 ? 0.488 -31.064 9.684 1.00 80.33 ? 38 VAL A N 1 ATOM 86 C CA . VAL A 1 11 ? 1.751 -31.235 8.978 1.00 77.22 ? 38 VAL A CA 1 ATOM 87 C C . VAL A 1 11 ? 2.779 -30.192 9.389 1.00 74.67 ? 38 VAL A C 1 ATOM 88 O O . VAL A 1 11 ? 2.418 -29.077 9.773 1.00 73.32 ? 38 VAL A O 1 ATOM 89 C CB . VAL A 1 11 ? 1.563 -31.160 7.453 1.00 78.98 ? 38 VAL A CB 1 ATOM 90 C CG1 . VAL A 1 11 ? 0.944 -32.446 6.931 1.00 81.73 ? 38 VAL A CG1 1 ATOM 91 C CG2 . VAL A 1 11 ? 0.709 -29.957 7.082 1.00 82.54 ? 38 VAL A CG2 1 ATOM 92 N N . ASP A 1 12 ? 4.058 -30.563 9.320 1.00 63.97 ? 39 ASP A N 1 ATOM 93 C CA . ASP A 1 12 ? 5.137 -29.634 9.642 1.00 53.96 ? 39 ASP A CA 1 ATOM 94 C C . ASP A 1 12 ? 4.976 -28.328 8.877 1.00 65.56 ? 39 ASP A C 1 ATOM 95 O O . ASP A 1 12 ? 4.559 -28.322 7.720 1.00 75.92 ? 39 ASP A O 1 ATOM 96 C CB . ASP A 1 12 ? 6.502 -30.245 9.324 1.00 59.74 ? 39 ASP A CB 1 ATOM 97 C CG . ASP A 1 12 ? 6.787 -31.505 10.126 1.00 73.58 ? 39 ASP A CG 1 ATOM 98 O OD1 . ASP A 1 12 ? 6.207 -31.663 11.222 1.00 76.59 ? 39 ASP A OD1 1 ATOM 99 O OD2 . ASP A 1 12 ? 7.597 -32.339 9.662 1.00 81.61 ? 39 ASP A OD2 1 ATOM 100 N N . GLN A 1 13 ? 5.300 -27.224 9.532 1.00 71.58 ? 40 GLN A N 1 ATOM 101 C CA . GLN A 1 13 ? 5.117 -25.915 8.945 1.00 73.77 ? 40 GLN A CA 1 ATOM 102 C C . GLN A 1 13 ? 6.430 -25.147 8.997 1.00 74.14 ? 40 GLN A C 1 ATOM 103 O O . GLN A 1 13 ? 7.164 -25.213 9.982 1.00 77.18 ? 40 GLN A O 1 ATOM 104 C CB . GLN A 1 13 ? 4.011 -25.140 9.654 1.00 75.29 ? 40 GLN A CB 1 ATOM 105 C CG . GLN A 1 13 ? 2.626 -25.401 9.085 1.00 78.67 ? 40 GLN A CG 1 ATOM 106 C CD . GLN A 1 13 ? 1.815 -24.130 8.922 1.00 93.58 ? 40 GLN A CD 1 ATOM 107 O OE1 . GLN A 1 13 ? 1.297 -23.581 9.891 1.00 99.72 ? 40 GLN A OE1 1 ATOM 108 N NE2 . GLN A 1 13 ? 1.709 -23.652 7.691 1.00 100.30 ? 40 GLN A NE2 1 ATOM 109 N N . THR A 1 14 ? 6.718 -24.421 7.925 1.00 72.05 ? 41 THR A N 1 ATOM 110 C CA . THR A 1 14 ? 7.744 -23.398 7.981 1.00 67.58 ? 41 THR A CA 1 ATOM 111 C C . THR A 1 14 ? 7.096 -22.064 7.644 1.00 68.34 ? 41 THR A C 1 ATOM 112 O O . THR A 1 14 ? 6.630 -21.858 6.528 1.00 70.21 ? 41 THR A O 1 ATOM 113 C CB . THR A 1 14 ? 8.905 -23.704 7.026 1.00 64.71 ? 41 THR A CB 1 ATOM 114 O OG1 . THR A 1 14 ? 9.315 -25.069 7.184 1.00 65.19 ? 41 THR A OG1 1 ATOM 115 C CG2 . THR A 1 14 ? 10.088 -22.800 7.329 1.00 60.34 ? 41 THR A CG2 1 ATOM 116 N N . GLY A 1 15 ? 7.016 -21.187 8.639 1.00 69.70 ? 42 GLY A N 1 ATOM 117 C CA . GLY A 1 15 ? 6.432 -19.871 8.462 1.00 69.03 ? 42 GLY A CA 1 ATOM 118 C C . GLY A 1 15 ? 7.451 -18.752 8.554 1.00 70.60 ? 42 GLY A C 1 ATOM 119 O O . GLY A 1 15 ? 8.633 -18.996 8.763 1.00 72.97 ? 42 GLY A O 1 ATOM 120 N N . VAL A 1 16 ? 6.977 -17.517 8.419 1.00 74.16 ? 43 VAL A N 1 ATOM 121 C CA . VAL A 1 16 ? 7.824 -16.327 8.505 1.00 78.38 ? 43 VAL A CA 1 ATOM 122 C C . VAL A 1 16 ? 7.454 -15.545 9.767 1.00 75.38 ? 43 VAL A C 1 ATOM 123 O O . VAL A 1 16 ? 6.274 -15.434 10.104 1.00 75.76 ? 43 VAL A O 1 ATOM 124 C CB . VAL A 1 16 ? 7.680 -15.435 7.241 1.00 62.53 ? 43 VAL A CB 1 ATOM 125 C CG1 . VAL A 1 16 ? 6.222 -15.347 6.807 1.00 69.19 ? 43 VAL A CG1 1 ATOM 126 C CG2 . VAL A 1 16 ? 8.268 -14.045 7.466 1.00 61.95 ? 43 VAL A CG2 1 ATOM 127 N N . SER A 1 17 ? 8.471 -15.072 10.489 1.00 71.17 ? 44 SER A N 1 ATOM 128 C CA . SER A 1 17 ? 8.311 -14.233 11.674 1.00 75.97 ? 44 SER A CA 1 ATOM 129 C C . SER A 1 17 ? 7.368 -13.047 11.453 1.00 79.86 ? 44 SER A C 1 ATOM 130 O O . SER A 1 17 ? 7.473 -12.336 10.453 1.00 89.14 ? 44 SER A O 1 ATOM 131 C CB . SER A 1 17 ? 9.677 -13.723 12.144 1.00 85.14 ? 44 SER A CB 1 ATOM 132 O OG . SER A 1 17 ? 9.551 -12.957 13.334 1.00 92.49 ? 44 SER A OG 1 ATOM 133 N N . GLY A 1 18 ? 6.457 -12.836 12.406 1.00 81.22 ? 45 GLY A N 1 ATOM 134 C CA . GLY A 1 18 ? 5.467 -11.776 12.305 1.00 84.02 ? 45 GLY A CA 1 ATOM 135 C C . GLY A 1 18 ? 4.211 -12.293 11.643 1.00 84.73 ? 45 GLY A C 1 ATOM 136 O O . GLY A 1 18 ? 3.144 -11.687 11.739 1.00 85.90 ? 45 GLY A O 1 ATOM 137 N N . GLY A 1 19 ? 4.330 -13.442 10.991 1.00 80.45 ? 46 GLY A N 1 ATOM 138 C CA . GLY A 1 19 ? 3.222 -14.023 10.258 1.00 75.74 ? 46 GLY A CA 1 ATOM 139 C C . GLY A 1 19 ? 2.355 -14.959 11.075 1.00 68.95 ? 46 GLY A C 1 ATOM 140 O O . GLY A 1 19 ? 2.263 -14.822 12.293 1.00 66.05 ? 46 GLY A O 1 ATOM 141 N N . VAL A 1 20 ? 1.703 -15.895 10.390 1.00 72.81 ? 47 VAL A N 1 ATOM 142 C CA . VAL A 1 20 ? 0.802 -16.843 11.024 1.00 70.68 ? 47 VAL A CA 1 ATOM 143 C C . VAL A 1 20 ? 1.249 -18.263 10.714 1.00 63.84 ? 47 VAL A C 1 ATOM 144 O O . VAL A 1 20 ? 1.771 -18.545 9.635 1.00 61.18 ? 47 VAL A O 1 ATOM 145 C CB . VAL A 1 20 ? -0.654 -16.654 10.540 1.00 50.22 ? 47 VAL A CB 1 ATOM 146 C CG1 . VAL A 1 20 ? -1.602 -17.572 11.292 1.00 48.92 ? 47 VAL A CG1 1 ATOM 147 C CG2 . VAL A 1 20 ? -1.072 -15.203 10.704 1.00 55.14 ? 47 VAL A CG2 1 ATOM 148 N N . ALA A 1 21 ? 1.055 -19.157 11.671 1.00 61.46 ? 48 ALA A N 1 ATOM 149 C CA . ALA A 1 21 ? 1.068 -20.573 11.366 1.00 62.38 ? 48 ALA A CA 1 ATOM 150 C C . ALA A 1 21 ? -0.161 -21.212 11.980 1.00 68.99 ? 48 ALA A C 1 ATOM 151 O O . ALA A 1 21 ? -0.596 -20.822 13.058 1.00 75.79 ? 48 ALA A O 1 ATOM 152 C CB . ALA A 1 21 ? 2.341 -21.222 11.884 1.00 61.84 ? 48 ALA A CB 1 ATOM 153 N N . SER A 1 22 ? -0.738 -22.177 11.278 1.00 64.50 ? 49 SER A N 1 ATOM 154 C CA . SER A 1 22 ? -1.887 -22.890 11.800 1.00 64.21 ? 49 SER A CA 1 ATOM 155 C C . SER A 1 22 ? -1.638 -24.378 11.677 1.00 73.13 ? 49 SER A C 1 ATOM 156 O O . SER A 1 22 ? -1.099 -24.858 10.681 1.00 79.28 ? 49 SER A O 1 ATOM 157 C CB . SER A 1 22 ? -3.169 -22.490 11.066 1.00 61.78 ? 49 SER A CB 1 ATOM 158 O OG . SER A 1 22 ? -3.488 -21.127 11.282 1.00 59.75 ? 49 SER A OG 1 ATOM 159 N N . PHE A 1 23 ? -2.053 -25.101 12.706 1.00 71.08 ? 50 PHE A N 1 ATOM 160 C CA . PHE A 1 23 ? -2.022 -26.546 12.696 1.00 68.10 ? 50 PHE A CA 1 ATOM 161 C C . PHE A 1 23 ? -3.443 -27.048 12.865 1.00 70.88 ? 50 PHE A C 1 ATOM 162 O O . PHE A 1 23 ? -4.198 -26.548 13.705 1.00 67.94 ? 50 PHE A O 1 ATOM 163 C CB . PHE A 1 23 ? -1.117 -27.087 13.804 1.00 62.17 ? 50 PHE A CB 1 ATOM 164 C CG . PHE A 1 23 ? 0.338 -26.753 13.616 1.00 65.61 ? 50 PHE A CG 1 ATOM 165 C CD1 . PHE A 1 23 ? 1.140 -27.529 12.794 1.00 72.01 ? 50 PHE A CD1 1 ATOM 166 C CD2 . PHE A 1 23 ? 0.907 -25.673 14.269 1.00 67.12 ? 50 PHE A CD2 1 ATOM 167 C CE1 . PHE A 1 23 ? 2.479 -27.230 12.621 1.00 69.54 ? 50 PHE A CE1 1 ATOM 168 C CE2 . PHE A 1 23 ? 2.246 -25.369 14.100 1.00 68.47 ? 50 PHE A CE2 1 ATOM 169 C CZ . PHE A 1 23 ? 3.033 -26.149 13.275 1.00 68.12 ? 50 PHE A CZ 1 ATOM 170 N N . ILE A 1 24 ? -3.801 -28.034 12.058 1.00 74.44 ? 51 ILE A N 1 ATOM 171 C CA . ILE A 1 24 ? -5.159 -28.525 12.037 1.00 78.02 ? 51 ILE A CA 1 ATOM 172 C C . ILE A 1 24 ? -5.180 -29.965 12.523 1.00 79.66 ? 51 ILE A C 1 ATOM 173 O O . ILE A 1 24 ? -4.358 -30.782 12.093 1.00 87.28 ? 51 ILE A O 1 ATOM 174 C CB . ILE A 1 24 ? -5.762 -28.451 10.610 1.00 66.27 ? 51 ILE A CB 1 ATOM 175 C CG1 . ILE A 1 24 ? -5.574 -27.044 10.032 1.00 63.54 ? 51 ILE A CG1 1 ATOM 176 C CG2 . ILE A 1 24 ? -7.228 -28.855 10.609 1.00 66.43 ? 51 ILE A CG2 1 ATOM 177 C CD1 . ILE A 1 24 ? -5.915 -26.942 8.567 1.00 64.32 ? 51 ILE A CD1 1 ATOM 178 N N . CYS A 1 25 ? -6.133 -30.283 13.392 1.00 74.92 ? 52 CYS A N 1 ATOM 179 C CA . CYS A 1 25 ? -6.238 -31.640 13.894 1.00 64.77 ? 52 CYS A CA 1 ATOM 180 C C . CYS A 1 25 ? -7.706 -31.981 14.052 1.00 66.56 ? 52 CYS A C 1 ATOM 181 O O . CYS A 1 25 ? -8.496 -31.150 14.549 1.00 70.57 ? 52 CYS A O 1 ATOM 182 C CB . CYS A 1 25 ? -5.497 -31.800 15.230 1.00 57.50 ? 52 CYS A CB 1 ATOM 183 S SG . CYS A 1 25 ? -5.263 -33.505 15.803 1.00 72.50 ? 52 CYS A SG 1 ATOM 184 N N . GLN A 1 26 ? -8.063 -33.196 13.627 1.00 73.75 ? 53 GLN A N 1 ATOM 185 C CA . GLN A 1 26 ? -9.417 -33.699 13.757 1.00 74.98 ? 53 GLN A CA 1 ATOM 186 C C . GLN A 1 26 ? -9.365 -35.193 14.020 1.00 78.20 ? 53 GLN A C 1 ATOM 187 O O . GLN A 1 26 ? -8.509 -35.907 13.466 1.00 83.29 ? 53 GLN A O 1 ATOM 188 C CB . GLN A 1 26 ? -10.235 -33.429 12.497 1.00 75.82 ? 53 GLN A CB 1 ATOM 189 C CG . GLN A 1 26 ? -10.479 -31.959 12.177 1.00 74.03 ? 53 GLN A CG 1 ATOM 190 C CD . GLN A 1 26 ? -11.185 -31.764 10.837 1.00 79.65 ? 53 GLN A CD 1 ATOM 191 O OE1 . GLN A 1 26 ? -10.712 -32.227 9.796 1.00 86.21 ? 53 GLN A OE1 1 ATOM 192 N NE2 . GLN A 1 26 ? -12.329 -31.087 10.864 1.00 79.18 ? 53 GLN A NE2 1 ATOM 193 N N . ALA A 1 27 ? -10.298 -35.664 14.842 1.00 75.22 ? 54 ALA A N 1 ATOM 194 C CA . ALA A 1 27 ? -10.372 -37.058 15.214 1.00 77.26 ? 54 ALA A CA 1 ATOM 195 C C . ALA A 1 27 ? -11.828 -37.488 15.247 1.00 85.28 ? 54 ALA A C 1 ATOM 196 O O . ALA A 1 27 ? -12.736 -36.636 15.319 1.00 90.10 ? 54 ALA A O 1 ATOM 197 C CB . ALA A 1 27 ? -9.698 -37.290 16.598 1.00 91.14 ? 54 ALA A CB 1 ATOM 198 N N . THR A 1 28 ? -12.045 -38.797 15.130 1.00 88.95 ? 55 THR A N 1 ATOM 199 C CA . THR A 1 28 ? -13.367 -39.380 15.318 1.00 91.81 ? 55 THR A CA 1 ATOM 200 C C . THR A 1 28 ? -13.248 -40.514 16.314 1.00 88.41 ? 55 THR A C 1 ATOM 201 O O . THR A 1 28 ? -12.133 -40.997 16.549 1.00 85.67 ? 55 THR A O 1 ATOM 202 C CB . THR A 1 28 ? -13.966 -39.890 13.997 1.00 96.30 ? 55 THR A CB 1 ATOM 203 O OG1 . THR A 1 28 ? -15.362 -40.253 14.119 1.00 97.81 ? 55 THR A OG1 1 ATOM 204 C CG2 . THR A 1 28 ? -13.179 -41.115 13.503 1.00 99.20 ? 55 THR A CG2 1 ATOM 205 N N . GLY A 1 29 ? -14.398 -41.004 16.782 1.00 90.27 ? 56 GLY A N 1 ATOM 206 C CA . GLY A 1 29 ? -14.477 -42.086 17.744 1.00 97.23 ? 56 GLY A CA 1 ATOM 207 C C . GLY A 1 29 ? -15.830 -42.070 18.421 1.00 105.82 ? 56 GLY A C 1 ATOM 208 O O . GLY A 1 29 ? -16.698 -41.217 18.143 1.00 112.20 ? 56 GLY A O 1 ATOM 209 N N . ASP A 1 30 ? -16.031 -43.050 19.285 1.00 105.32 ? 57 ASP A N 1 ATOM 210 C CA . ASP A 1 30 ? -17.259 -43.155 20.017 1.00 101.51 ? 57 ASP A CA 1 ATOM 211 C C . ASP A 1 30 ? -17.022 -43.521 21.449 1.00 100.80 ? 57 ASP A C 1 ATOM 212 O O . ASP A 1 30 ? -16.612 -44.639 21.736 1.00 105.43 ? 57 ASP A O 1 ATOM 213 C CB . ASP A 1 30 ? -18.140 -44.171 19.335 1.00 95.90 ? 57 ASP A CB 1 ATOM 214 C CG . ASP A 1 30 ? -19.342 -44.583 20.171 1.00 95.02 ? 57 ASP A CG 1 ATOM 215 O OD1 . ASP A 1 30 ? -20.018 -43.716 20.773 1.00 97.42 ? 57 ASP A OD1 1 ATOM 216 O OD2 . ASP A 1 30 ? -19.610 -45.808 20.175 1.00 93.48 ? 57 ASP A OD2 1 ATOM 217 N N . PRO A 1 31 ? -17.246 -42.582 22.364 1.00 94.34 ? 58 PRO A N 1 ATOM 218 C CA . PRO A 1 31 ? -17.790 -41.217 22.348 1.00 91.92 ? 58 PRO A CA 1 ATOM 219 C C . PRO A 1 31 ? -16.881 -40.239 21.606 1.00 94.67 ? 58 PRO A C 1 ATOM 220 O O . PRO A 1 31 ? -15.722 -40.563 21.354 1.00 89.53 ? 58 PRO A O 1 ATOM 221 C CB . PRO A 1 31 ? -17.863 -40.877 23.839 1.00 83.69 ? 58 PRO A CB 1 ATOM 222 C CG . PRO A 1 31 ? -16.771 -41.701 24.441 1.00 83.88 ? 58 PRO A CG 1 ATOM 223 C CD . PRO A 1 31 ? -16.817 -42.994 23.706 1.00 90.28 ? 58 PRO A CD 1 ATOM 224 N N . ARG A 1 32 ? -17.419 -39.079 21.237 1.00 95.70 ? 59 ARG A N 1 ATOM 225 C CA . ARG A 1 32 ? -16.639 -38.066 20.542 1.00 93.70 ? 59 ARG A CA 1 ATOM 226 C C . ARG A 1 32 ? -15.443 -37.679 21.402 1.00 90.40 ? 59 ARG A C 1 ATOM 227 O O . ARG A 1 32 ? -15.586 -37.428 22.601 1.00 91.60 ? 59 ARG A O 1 ATOM 228 C CB . ARG A 1 32 ? -17.474 -36.823 20.233 1.00 103.10 ? 59 ARG A CB 1 ATOM 229 C CG . ARG A 1 32 ? -16.647 -35.531 20.211 1.00 118.43 ? 59 ARG A CG 1 ATOM 230 C CD . ARG A 1 32 ? -17.506 -34.307 19.954 1.00 129.04 ? 59 ARG A CD 1 ATOM 231 N NE . ARG A 1 32 ? -18.128 -34.351 18.635 1.00 137.59 ? 59 ARG A NE 1 ATOM 232 C CZ . ARG A 1 32 ? -19.399 -34.046 18.402 1.00 143.02 ? 59 ARG A CZ 1 ATOM 233 N NH1 . ARG A 1 32 ? -20.186 -33.670 19.401 1.00 143.68 ? 59 ARG A NH1 1 ATOM 234 N NH2 . ARG A 1 32 ? -19.885 -34.114 17.170 1.00 145.06 ? 59 ARG A NH2 1 ATOM 235 N N . PRO A 1 33 ? -14.262 -37.606 20.780 1.00 86.07 ? 60 PRO A N 1 ATOM 236 C CA . PRO A 1 33 ? -12.994 -37.367 21.462 1.00 83.18 ? 60 PRO A CA 1 ATOM 237 C C . PRO A 1 33 ? -12.806 -35.884 21.712 1.00 85.18 ? 60 PRO A C 1 ATOM 238 O O . PRO A 1 33 ? -13.476 -35.059 21.091 1.00 87.35 ? 60 PRO A O 1 ATOM 239 C CB . PRO A 1 33 ? -11.946 -37.883 20.464 1.00 81.20 ? 60 PRO A CB 1 ATOM 240 C CG . PRO A 1 33 ? -12.722 -38.552 19.352 1.00 84.57 ? 60 PRO A CG 1 ATOM 241 C CD . PRO A 1 33 ? -14.059 -37.893 19.354 1.00 88.87 ? 60 PRO A CD 1 ATOM 242 N N . LYS A 1 34 ? -11.941 -35.549 22.658 1.00 85.56 ? 61 LYS A N 1 ATOM 243 C CA . LYS A 1 34 ? -11.556 -34.160 22.811 1.00 81.82 ? 61 LYS A CA 1 ATOM 244 C C . LYS A 1 34 ? -10.144 -34.058 22.309 1.00 77.01 ? 61 LYS A C 1 ATOM 245 O O . LYS A 1 34 ? -9.442 -35.063 22.187 1.00 79.48 ? 61 LYS A O 1 ATOM 246 C CB . LYS A 1 34 ? -11.640 -33.702 24.272 1.00 90.32 ? 61 LYS A CB 1 ATOM 247 C CG . LYS A 1 34 ? -10.604 -34.352 25.188 1.00 98.82 ? 61 LYS A CG 1 ATOM 248 C CD . LYS A 1 34 ? -9.874 -33.334 26.064 1.00 100.17 ? 61 LYS A CD 1 ATOM 249 C CE . LYS A 1 34 ? -10.187 -33.551 27.543 1.00 95.86 ? 61 LYS A CE 1 ATOM 250 N NZ . LYS A 1 34 ? -9.235 -32.857 28.467 1.00 83.81 ? 61 LYS A NZ 1 ATOM 251 N N . ILE A 1 35 ? -9.708 -32.837 22.053 1.00 74.36 ? 62 ILE A N 1 ATOM 252 C CA . ILE A 1 35 ? -8.385 -32.628 21.508 1.00 75.99 ? 62 ILE A CA 1 ATOM 253 C C . ILE A 1 35 ? -7.692 -31.639 22.424 1.00 80.62 ? 62 ILE A C 1 ATOM 254 O O . ILE A 1 35 ? -8.297 -30.672 22.879 1.00 88.24 ? 62 ILE A O 1 ATOM 255 C CB . ILE A 1 35 ? -8.453 -32.108 20.067 1.00 72.10 ? 62 ILE A CB 1 ATOM 256 C CG1 . ILE A 1 35 ? -8.918 -33.242 19.139 1.00 71.50 ? 62 ILE A CG1 1 ATOM 257 C CG2 . ILE A 1 35 ? -7.114 -31.571 19.619 1.00 73.98 ? 62 ILE A CG2 1 ATOM 258 C CD1 . ILE A 1 35 ? -8.628 -32.992 17.676 1.00 80.64 ? 62 ILE A CD1 1 ATOM 259 N N . VAL A 1 36 ? -6.418 -31.894 22.699 1.00 75.90 ? 63 VAL A N 1 ATOM 260 C CA . VAL A 1 36 ? -5.587 -30.901 23.351 1.00 71.32 ? 63 VAL A CA 1 ATOM 261 C C . VAL A 1 36 ? -4.297 -30.691 22.574 1.00 75.21 ? 63 VAL A C 1 ATOM 262 O O . VAL A 1 36 ? -3.847 -31.582 21.851 1.00 87.36 ? 63 VAL A O 1 ATOM 263 C CB . VAL A 1 36 ? -5.263 -31.345 24.803 1.00 63.55 ? 63 VAL A CB 1 ATOM 264 C CG1 . VAL A 1 36 ? -4.515 -30.271 25.563 1.00 65.58 ? 63 VAL A CG1 1 ATOM 265 C CG2 . VAL A 1 36 ? -6.537 -31.725 25.546 1.00 67.88 ? 63 VAL A CG2 1 ATOM 266 N N . TRP A 1 37 ? -3.711 -29.510 22.735 1.00 70.11 ? 64 TRP A N 1 ATOM 267 C CA . TRP A 1 37 ? -2.437 -29.210 22.116 1.00 73.49 ? 64 TRP A CA 1 ATOM 268 C C . TRP A 1 37 ? -1.384 -29.064 23.206 1.00 71.13 ? 64 TRP A C 1 ATOM 269 O O . TRP A 1 37 ? -1.574 -28.317 24.170 1.00 68.29 ? 64 TRP A O 1 ATOM 270 C CB . TRP A 1 37 ? -2.543 -27.947 21.256 1.00 73.92 ? 64 TRP A CB 1 ATOM 271 C CG . TRP A 1 37 ? -3.490 -28.096 20.100 1.00 69.13 ? 64 TRP A CG 1 ATOM 272 C CD1 . TRP A 1 37 ? -4.843 -27.900 20.113 1.00 67.26 ? 64 TRP A CD1 1 ATOM 273 C CD2 . TRP A 1 37 ? -3.155 -28.480 18.759 1.00 64.99 ? 64 TRP A CD2 1 ATOM 274 N NE1 . TRP A 1 37 ? -5.368 -28.137 18.864 1.00 65.76 ? 64 TRP A NE1 1 ATOM 275 C CE2 . TRP A 1 37 ? -4.352 -28.494 18.016 1.00 66.31 ? 64 TRP A CE2 1 ATOM 276 C CE3 . TRP A 1 37 ? -1.960 -28.811 18.116 1.00 63.91 ? 64 TRP A CE3 1 ATOM 277 C CZ2 . TRP A 1 37 ? -4.387 -28.825 16.663 1.00 67.42 ? 64 TRP A CZ2 1 ATOM 278 C CZ3 . TRP A 1 37 ? -1.998 -29.142 16.773 1.00 67.68 ? 64 TRP A CZ3 1 ATOM 279 C CH2 . TRP A 1 37 ? -3.202 -29.147 16.062 1.00 66.00 ? 64 TRP A CH2 1 ATOM 280 N N . ASN A 1 38 ? -0.271 -29.769 23.042 1.00 71.65 ? 65 ASN A N 1 ATOM 281 C CA . ASN A 1 38 ? 0.807 -29.741 24.016 1.00 69.36 ? 65 ASN A CA 1 ATOM 282 C C . ASN A 1 38 ? 2.118 -29.286 23.413 1.00 77.99 ? 65 ASN A C 1 ATOM 283 O O . ASN A 1 38 ? 2.318 -29.351 22.187 1.00 83.01 ? 65 ASN A O 1 ATOM 284 C CB . ASN A 1 38 ? 1.013 -31.113 24.660 1.00 66.53 ? 65 ASN A CB 1 ATOM 285 C CG . ASN A 1 38 ? -0.240 -31.646 25.323 1.00 68.14 ? 65 ASN A CG 1 ATOM 286 O OD1 . ASN A 1 38 ? -1.011 -30.895 25.923 1.00 68.33 ? 65 ASN A OD1 1 ATOM 287 N ND2 . ASN A 1 38 ? -0.447 -32.953 25.219 1.00 71.51 ? 65 ASN A ND2 1 ATOM 288 N N . LYS A 1 39 ? 3.032 -28.881 24.291 1.00 78.80 ? 66 LYS A N 1 ATOM 289 C CA . LYS A 1 39 ? 4.437 -28.762 23.920 1.00 84.83 ? 66 LYS A CA 1 ATOM 290 C C . LYS A 1 39 ? 5.208 -29.462 25.036 1.00 86.55 ? 66 LYS A C 1 ATOM 291 O O . LYS A 1 39 ? 5.054 -29.132 26.215 1.00 81.14 ? 66 LYS A O 1 ATOM 292 C CB . LYS A 1 39 ? 4.848 -27.298 23.783 1.00 86.90 ? 66 LYS A CB 1 ATOM 293 C CG . LYS A 1 39 ? 6.324 -27.108 23.475 1.00 93.72 ? 66 LYS A CG 1 ATOM 294 C CD . LYS A 1 39 ? 6.629 -25.684 23.036 1.00 98.35 ? 66 LYS A CD 1 ATOM 295 C CE . LYS A 1 39 ? 7.105 -24.815 24.191 1.00 102.54 ? 66 LYS A CE 1 ATOM 296 N NZ . LYS A 1 39 ? 7.496 -23.451 23.728 1.00 107.18 ? 66 LYS A NZ 1 ATOM 297 N N . LYS A 1 40 ? 6.019 -30.433 24.638 1.00 96.80 ? 67 LYS A N 1 ATOM 298 C CA . LYS A 1 40 ? 6.845 -31.216 25.536 1.00 106.21 ? 67 LYS A CA 1 ATOM 299 C C . LYS A 1 40 ? 6.015 -31.786 26.693 1.00 103.22 ? 67 LYS A C 1 ATOM 300 O O . LYS A 1 40 ? 6.450 -31.875 27.838 1.00 103.99 ? 67 LYS A O 1 ATOM 301 C CB . LYS A 1 40 ? 8.021 -30.391 26.086 1.00 114.09 ? 67 LYS A CB 1 ATOM 302 C CG . LYS A 1 40 ? 9.320 -30.702 25.365 1.00 122.86 ? 67 LYS A CG 1 ATOM 303 C CD . LYS A 1 40 ? 9.516 -32.212 25.249 1.00 129.55 ? 67 LYS A CD 1 ATOM 304 C CE . LYS A 1 40 ? 10.498 -32.590 24.147 1.00 136.42 ? 67 LYS A CE 1 ATOM 305 N NZ . LYS A 1 40 ? 11.849 -32.012 24.366 1.00 140.96 ? 67 LYS A NZ 1 ATOM 306 N N . GLY A 1 41 ? 4.804 -32.205 26.337 1.00 101.46 ? 68 GLY A N 1 ATOM 307 C CA . GLY A 1 41 ? 3.901 -32.934 27.224 1.00 100.77 ? 68 GLY A CA 1 ATOM 308 C C . GLY A 1 41 ? 3.174 -32.024 28.200 1.00 100.55 ? 68 GLY A C 1 ATOM 309 O O . GLY A 1 41 ? 2.448 -32.501 29.065 1.00 102.97 ? 68 GLY A O 1 ATOM 310 N N . LYS A 1 42 ? 3.361 -30.713 28.064 1.00 99.07 ? 69 LYS A N 1 ATOM 311 C CA . LYS A 1 42 ? 2.650 -29.766 28.898 1.00 96.62 ? 69 LYS A CA 1 ATOM 312 C C . LYS A 1 42 ? 1.711 -28.984 28.001 1.00 86.37 ? 69 LYS A C 1 ATOM 313 O O . LYS A 1 42 ? 2.094 -28.585 26.902 1.00 83.00 ? 69 LYS A O 1 ATOM 314 C CB . LYS A 1 42 ? 3.612 -28.853 29.643 1.00 107.94 ? 69 LYS A CB 1 ATOM 315 C CG . LYS A 1 42 ? 4.538 -29.593 30.605 1.00 116.75 ? 69 LYS A CG 1 ATOM 316 C CD . LYS A 1 42 ? 5.947 -29.647 30.053 1.00 123.87 ? 69 LYS A CD 1 ATOM 317 C CE . LYS A 1 42 ? 6.829 -30.545 30.890 1.00 130.74 ? 69 LYS A CE 1 ATOM 318 N NZ . LYS A 1 42 ? 8.221 -30.559 30.370 1.00 134.35 ? 69 LYS A NZ 1 ATOM 319 N N . LYS A 1 43 ? 0.477 -28.784 28.455 1.00 88.32 ? 70 LYS A N 1 ATOM 320 C CA . LYS A 1 43 ? -0.511 -28.095 27.631 1.00 86.31 ? 70 LYS A CA 1 ATOM 321 C C . LYS A 1 43 ? -0.129 -26.646 27.353 1.00 90.79 ? 70 LYS A C 1 ATOM 322 O O . LYS A 1 43 ? 0.258 -25.906 28.254 1.00 85.72 ? 70 LYS A O 1 ATOM 323 C CB . LYS A 1 43 ? -1.894 -28.159 28.286 1.00 82.80 ? 70 LYS A CB 1 ATOM 324 C CG . LYS A 1 43 ? -3.011 -27.633 27.394 1.00 84.92 ? 70 LYS A CG 1 ATOM 325 C CD . LYS A 1 43 ? -3.548 -26.296 27.882 1.00 92.71 ? 70 LYS A CD 1 ATOM 326 C CE . LYS A 1 43 ? -4.601 -26.476 28.967 1.00 99.84 ? 70 LYS A CE 1 ATOM 327 N NZ . LYS A 1 43 ? -5.888 -27.015 28.433 1.00 98.91 ? 70 LYS A NZ 1 ATOM 328 N N . VAL A 1 44 ? -0.233 -26.262 26.089 1.00 100.83 ? 71 VAL A N 1 ATOM 329 C CA . VAL A 1 44 ? 0.145 -24.925 25.644 1.00 103.91 ? 71 VAL A CA 1 ATOM 330 C C . VAL A 1 44 ? -0.683 -23.840 26.331 1.00 96.98 ? 71 VAL A C 1 ATOM 331 O O . VAL A 1 44 ? -1.887 -24.005 26.551 1.00 92.36 ? 71 VAL A O 1 ATOM 332 C CB . VAL A 1 44 ? 0.035 -24.781 24.093 1.00 68.22 ? 71 VAL A CB 1 ATOM 333 C CG1 . VAL A 1 44 ? 0.676 -25.972 23.407 1.00 66.83 ? 71 VAL A CG1 1 ATOM 334 C CG2 . VAL A 1 44 ? -1.409 -24.635 23.647 1.00 68.47 ? 71 VAL A CG2 1 ATOM 335 N N . SER A 1 45 ? -0.037 -22.747 26.713 1.00 92.44 ? 72 SER A N 1 ATOM 336 C CA . SER A 1 45 ? -0.748 -21.618 27.311 1.00 91.35 ? 72 SER A CA 1 ATOM 337 C C . SER A 1 45 ? 0.093 -20.396 27.034 1.00 88.68 ? 72 SER A C 1 ATOM 338 O O . SER A 1 45 ? 1.110 -20.151 27.685 1.00 90.76 ? 72 SER A O 1 ATOM 339 C CB . SER A 1 45 ? -0.945 -21.805 28.819 1.00 96.21 ? 72 SER A CB 1 ATOM 340 O OG . SER A 1 45 ? -1.318 -20.584 29.435 1.00 99.06 ? 72 SER A OG 1 ATOM 341 N N . ASN A 1 46 ? -0.365 -19.622 26.062 1.00 88.14 ? 73 ASN A N 1 ATOM 342 C CA . ASN A 1 46 ? 0.355 -18.453 25.597 1.00 89.55 ? 73 ASN A CA 1 ATOM 343 C C . ASN A 1 46 ? -0.590 -17.475 24.915 1.00 91.74 ? 73 ASN A C 1 ATOM 344 O O . ASN A 1 46 ? -1.487 -17.885 24.176 1.00 97.87 ? 73 ASN A O 1 ATOM 345 C CB . ASN A 1 46 ? 1.476 -18.872 24.644 1.00 88.43 ? 73 ASN A CB 1 ATOM 346 C CG . ASN A 1 46 ? 2.414 -17.733 24.299 1.00 91.33 ? 73 ASN A CG 1 ATOM 347 O OD1 . ASN A 1 46 ? 2.006 -16.582 24.150 1.00 94.20 ? 73 ASN A OD1 1 ATOM 348 N ND2 . ASN A 1 46 ? 3.692 -18.061 24.153 1.00 91.95 ? 73 ASN A ND2 1 ATOM 349 N N . GLN A 1 47 ? -0.395 -16.187 25.174 1.00 91.78 ? 74 GLN A N 1 ATOM 350 C CA . GLN A 1 47 ? -1.239 -15.148 24.597 1.00 92.56 ? 74 GLN A CA 1 ATOM 351 C C . GLN A 1 47 ? -1.276 -15.199 23.069 1.00 89.40 ? 74 GLN A C 1 ATOM 352 O O . GLN A 1 47 ? -2.279 -14.829 22.464 1.00 83.19 ? 74 GLN A O 1 ATOM 353 C CB . GLN A 1 47 ? -0.765 -13.762 25.042 1.00 94.66 ? 74 GLN A CB 1 ATOM 354 C CG . GLN A 1 47 ? -1.569 -12.619 24.435 1.00 99.83 ? 74 GLN A CG 1 ATOM 355 C CD . GLN A 1 47 ? -2.931 -12.448 25.086 1.00 105.56 ? 74 GLN A CD 1 ATOM 356 O OE1 . GLN A 1 47 ? -3.086 -12.670 26.287 1.00 108.48 ? 74 GLN A OE1 1 ATOM 357 N NE2 . GLN A 1 47 ? -3.923 -12.041 24.297 1.00 105.20 ? 74 GLN A NE2 1 ATOM 358 N N . ARG A 1 48 ? -0.201 -15.676 22.440 1.00 86.02 ? 75 ARG A N 1 ATOM 359 C CA . ARG A 1 48 ? -0.187 -15.688 20.985 1.00 75.09 ? 75 ARG A CA 1 ATOM 360 C C . ARG A 1 48 ? -0.634 -17.005 20.382 1.00 73.87 ? 75 ARG A C 1 ATOM 361 O O . ARG A 1 48 ? -0.617 -17.168 19.162 1.00 70.05 ? 75 ARG A O 1 ATOM 362 C CB . ARG A 1 48 ? 1.212 -15.356 20.461 1.00 68.40 ? 75 ARG A CB 1 ATOM 363 C CG . ARG A 1 48 ? 1.672 -13.946 20.779 1.00 71.93 ? 75 ARG A CG 1 ATOM 364 C CD . ARG A 1 48 ? 3.078 -13.696 20.261 1.00 80.32 ? 75 ARG A CD 1 ATOM 365 N NE . ARG A 1 48 ? 4.050 -14.622 20.834 1.00 87.39 ? 75 ARG A NE 1 ATOM 366 C CZ . ARG A 1 48 ? 4.682 -15.568 20.147 1.00 91.73 ? 75 ARG A CZ 1 ATOM 367 N NH1 . ARG A 1 48 ? 4.449 -15.718 18.849 1.00 91.97 ? 75 ARG A NH1 1 ATOM 368 N NH2 . ARG A 1 48 ? 5.554 -16.361 20.756 1.00 94.50 ? 75 ARG A NH2 1 ATOM 369 N N . PHE A 1 49 ? -1.041 -17.954 21.216 1.00 77.27 ? 76 PHE A N 1 ATOM 370 C CA . PHE A 1 49 ? -1.462 -19.228 20.660 1.00 73.93 ? 76 PHE A CA 1 ATOM 371 C C . PHE A 1 49 ? -2.944 -19.269 21.001 1.00 76.65 ? 76 PHE A C 1 ATOM 372 O O . PHE A 1 49 ? -3.316 -19.083 22.161 1.00 85.45 ? 76 PHE A O 1 ATOM 373 C CB . PHE A 1 49 ? -0.693 -20.423 21.255 1.00 68.27 ? 76 PHE A CB 1 ATOM 374 C CG . PHE A 1 49 ? 0.793 -20.431 20.948 1.00 70.62 ? 76 PHE A CG 1 ATOM 375 C CD1 . PHE A 1 49 ? 1.614 -19.399 21.372 1.00 74.58 ? 76 PHE A CD1 1 ATOM 376 C CD2 . PHE A 1 49 ? 1.374 -21.492 20.272 1.00 68.84 ? 76 PHE A CD2 1 ATOM 377 C CE1 . PHE A 1 49 ? 2.976 -19.412 21.110 1.00 71.66 ? 76 PHE A CE1 1 ATOM 378 C CE2 . PHE A 1 49 ? 2.740 -21.507 20.005 1.00 66.22 ? 76 PHE A CE2 1 ATOM 379 C CZ . PHE A 1 49 ? 3.537 -20.467 20.425 1.00 67.08 ? 76 PHE A CZ 1 ATOM 380 N N . GLU A 1 50 ? -3.794 -19.491 20.009 1.00 78.09 ? 77 GLU A N 1 ATOM 381 C CA . GLU A 1 50 ? -5.228 -19.634 20.266 1.00 82.09 ? 77 GLU A CA 1 ATOM 382 C C . GLU A 1 50 ? -5.719 -20.924 19.638 1.00 79.66 ? 77 GLU A C 1 ATOM 383 O O . GLU A 1 50 ? -5.307 -21.285 18.539 1.00 80.78 ? 77 GLU A O 1 ATOM 384 C CB . GLU A 1 50 ? -6.077 -18.431 19.822 1.00 94.45 ? 77 GLU A CB 1 ATOM 385 C CG . GLU A 1 50 ? -5.681 -17.655 18.591 1.00 110.48 ? 77 GLU A CG 1 ATOM 386 C CD . GLU A 1 50 ? -6.485 -16.364 18.521 1.00 114.26 ? 77 GLU A CD 1 ATOM 387 O OE1 . GLU A 1 50 ? -7.625 -16.360 19.036 1.00 112.78 ? 77 GLU A OE1 1 ATOM 388 O OE2 . GLU A 1 50 ? -5.982 -15.360 17.979 1.00 111.91 ? 77 GLU A OE2 1 ATOM 389 N N . VAL A 1 51 ? -6.601 -21.618 20.340 1.00 68.07 ? 78 VAL A N 1 ATOM 390 C CA . VAL A 1 51 ? -7.204 -22.810 19.778 1.00 63.20 ? 78 VAL A CA 1 ATOM 391 C C . VAL A 1 51 ? -8.670 -22.566 19.457 1.00 68.20 ? 78 VAL A C 1 ATOM 392 O O . VAL A 1 51 ? -9.460 -22.151 20.307 1.00 71.06 ? 78 VAL A O 1 ATOM 393 C CB . VAL A 1 51 ? -7.081 -24.002 20.740 1.00 57.93 ? 78 VAL A CB 1 ATOM 394 C CG1 . VAL A 1 51 ? -7.864 -25.189 20.213 1.00 64.05 ? 78 VAL A CG1 1 ATOM 395 C CG2 . VAL A 1 51 ? -5.618 -24.363 20.943 1.00 53.00 ? 78 VAL A CG2 1 ATOM 396 N N . ILE A 1 52 ? -9.006 -22.835 18.196 1.00 71.64 ? 79 ILE A N 1 ATOM 397 C CA . ILE A 1 52 ? -10.330 -22.616 17.640 1.00 72.28 ? 79 ILE A CA 1 ATOM 398 C C . ILE A 1 52 ? -10.926 -23.963 17.250 1.00 70.35 ? 79 ILE A C 1 ATOM 399 O O . ILE A 1 52 ? -10.391 -24.669 16.394 1.00 60.21 ? 79 ILE A O 1 ATOM 400 C CB . ILE A 1 52 ? -10.271 -21.697 16.387 1.00 51.18 ? 79 ILE A CB 1 ATOM 401 C CG1 . ILE A 1 52 ? -9.457 -20.427 16.669 1.00 54.82 ? 79 ILE A CG1 1 ATOM 402 C CG2 . ILE A 1 52 ? -11.666 -21.358 15.891 1.00 55.57 ? 79 ILE A CG2 1 ATOM 403 C CD1 . ILE A 1 52 ? -8.021 -20.482 16.175 1.00 56.85 ? 79 ILE A CD1 1 ATOM 404 N N . GLU A 1 53 ? -12.038 -24.311 17.891 1.00 82.69 ? 80 GLU A N 1 ATOM 405 C CA . GLU A 1 53 ? -12.730 -25.573 17.644 1.00 87.77 ? 80 GLU A CA 1 ATOM 406 C C . GLU A 1 53 ? -13.625 -25.536 16.410 1.00 88.90 ? 80 GLU A C 1 ATOM 407 O O . GLU A 1 53 ? -14.179 -24.492 16.060 1.00 90.30 ? 80 GLU A O 1 ATOM 408 C CB . GLU A 1 53 ? -13.543 -25.963 18.876 1.00 91.84 ? 80 GLU A CB 1 ATOM 409 C CG . GLU A 1 53 ? -12.761 -25.789 20.162 1.00 97.06 ? 80 GLU A CG 1 ATOM 410 C CD . GLU A 1 53 ? -13.119 -26.817 21.209 1.00 108.05 ? 80 GLU A CD 1 ATOM 411 O OE1 . GLU A 1 53 ? -14.146 -26.638 21.895 1.00 115.73 ? 80 GLU A OE1 1 ATOM 412 O OE2 . GLU A 1 53 ? -12.371 -27.805 21.344 1.00 114.86 ? 80 GLU A OE2 1 ATOM 413 N N . PHE A 1 54 ? -13.752 -26.680 15.747 1.00 85.99 ? 81 PHE A N 1 ATOM 414 C CA . PHE A 1 54 ? -14.779 -26.838 14.731 1.00 91.33 ? 81 PHE A CA 1 ATOM 415 C C . PHE A 1 54 ? -16.142 -26.906 15.397 1.00 99.89 ? 81 PHE A C 1 ATOM 416 O O . PHE A 1 54 ? -16.289 -27.521 16.453 1.00 98.57 ? 81 PHE A O 1 ATOM 417 C CB . PHE A 1 54 ? -14.510 -28.089 13.895 1.00 93.62 ? 81 PHE A CB 1 ATOM 418 C CG . PHE A 1 54 ? -13.259 -28.005 13.075 1.00 92.95 ? 81 PHE A CG 1 ATOM 419 C CD1 . PHE A 1 54 ? -12.042 -28.394 13.603 1.00 92.63 ? 81 PHE A CD1 1 ATOM 420 C CD2 . PHE A 1 54 ? -13.296 -27.519 11.778 1.00 94.41 ? 81 PHE A CD2 1 ATOM 421 C CE1 . PHE A 1 54 ? -10.885 -28.313 12.851 1.00 92.77 ? 81 PHE A CE1 1 ATOM 422 C CE2 . PHE A 1 54 ? -12.140 -27.436 11.021 1.00 93.37 ? 81 PHE A CE2 1 ATOM 423 C CZ . PHE A 1 54 ? -10.934 -27.835 11.560 1.00 94.45 ? 81 PHE A CZ 1 ATOM 424 N N . ASP A 1 55 ? -17.142 -26.311 14.751 1.00 112.01 ? 82 ASP A N 1 ATOM 425 C CA . ASP A 1 55 ? -18.510 -26.305 15.266 1.00 118.23 ? 82 ASP A CA 1 ATOM 426 C C . ASP A 1 55 ? -19.060 -27.708 15.468 1.00 117.09 ? 82 ASP A C 1 ATOM 427 O O . ASP A 1 55 ? -19.902 -27.932 16.339 1.00 115.50 ? 82 ASP A O 1 ATOM 428 C CB . ASP A 1 55 ? -19.429 -25.519 14.329 1.00 128.53 ? 82 ASP A CB 1 ATOM 429 C CG . ASP A 1 55 ? -18.978 -24.086 14.139 1.00 136.97 ? 82 ASP A CG 1 ATOM 430 O OD1 . ASP A 1 55 ? -17.771 -23.869 13.902 1.00 139.34 ? 82 ASP A OD1 1 ATOM 431 O OD2 . ASP A 1 55 ? -19.827 -23.176 14.235 1.00 138.90 ? 82 ASP A OD2 1 ATOM 432 N N . ASP A 1 56 ? -18.579 -28.648 14.663 1.00 118.72 ? 83 ASP A N 1 ATOM 433 C CA . ASP A 1 56 ? -19.036 -30.021 14.753 1.00 116.81 ? 83 ASP A CA 1 ATOM 434 C C . ASP A 1 56 ? -18.437 -30.733 15.968 1.00 116.37 ? 83 ASP A C 1 ATOM 435 O O . ASP A 1 56 ? -18.993 -31.714 16.458 1.00 120.99 ? 83 ASP A O 1 ATOM 436 C CB . ASP A 1 56 ? -18.695 -30.781 13.465 1.00 117.34 ? 83 ASP A CB 1 ATOM 437 C CG . ASP A 1 56 ? -17.216 -30.706 13.107 1.00 120.15 ? 83 ASP A CG 1 ATOM 438 O OD1 . ASP A 1 56 ? -16.906 -30.692 11.901 1.00 119.22 ? 83 ASP A OD1 1 ATOM 439 O OD2 . ASP A 1 56 ? -16.367 -30.677 14.021 1.00 123.88 ? 83 ASP A OD2 1 ATOM 440 N N . GLY A 1 57 ? -17.295 -30.244 16.445 1.00 114.06 ? 84 GLY A N 1 ATOM 441 C CA . GLY A 1 57 ? -16.674 -30.792 17.642 1.00 111.74 ? 84 GLY A CA 1 ATOM 442 C C . GLY A 1 57 ? -15.649 -31.860 17.326 1.00 107.59 ? 84 GLY A C 1 ATOM 443 O O . GLY A 1 57 ? -14.974 -32.383 18.215 1.00 109.58 ? 84 GLY A O 1 ATOM 444 N N . SER A 1 58 ? -15.529 -32.171 16.043 1.00 101.35 ? 85 SER A N 1 ATOM 445 C CA . SER A 1 58 ? -14.562 -33.150 15.584 1.00 100.42 ? 85 SER A CA 1 ATOM 446 C C . SER A 1 58 ? -13.103 -32.816 15.923 1.00 86.42 ? 85 SER A C 1 ATOM 447 O O . SER A 1 58 ? -12.431 -33.613 16.561 1.00 88.68 ? 85 SER A O 1 ATOM 448 C CB . SER A 1 58 ? -14.675 -33.305 14.054 1.00 110.50 ? 85 SER A CB 1 ATOM 449 O OG . SER A 1 58 ? -14.370 -32.081 13.396 1.00 114.65 ? 85 SER A OG 1 ATOM 450 N N . GLY A 1 59 ? -12.628 -31.674 15.376 1.00 79.36 ? 86 GLY A N 1 ATOM 451 C CA . GLY A 1 59 ? -11.358 -31.071 15.772 1.00 71.14 ? 86 GLY A CA 1 ATOM 452 C C . GLY A 1 59 ? -11.184 -29.664 16.419 1.00 74.00 ? 86 GLY A C 1 ATOM 453 O O . GLY A 1 59 ? -12.080 -29.043 17.047 1.00 80.27 ? 86 GLY A O 1 ATOM 454 N N . SER A 1 60 ? -9.929 -29.221 16.275 1.00 67.23 ? 87 SER A N 1 ATOM 455 C CA . SER A 1 60 ? -9.376 -27.948 16.739 1.00 60.64 ? 87 SER A CA 1 ATOM 456 C C . SER A 1 60 ? -8.202 -27.519 15.793 1.00 53.49 ? 87 SER A C 1 ATOM 457 O O . SER A 1 60 ? -7.428 -28.345 15.245 1.00 53.89 ? 87 SER A O 1 ATOM 458 C CB . SER A 1 60 ? -8.913 -27.992 18.244 1.00 82.47 ? 87 SER A CB 1 ATOM 459 O OG . SER A 1 60 ? -7.690 -28.667 18.493 1.00 86.50 ? 87 SER A OG 1 ATOM 460 N N . VAL A 1 61 ? -8.089 -26.206 15.614 1.00 57.52 ? 88 VAL A N 1 ATOM 461 C CA . VAL A 1 61 ? -6.954 -25.604 14.922 1.00 57.87 ? 88 VAL A CA 1 ATOM 462 C C . VAL A 1 61 ? -6.259 -24.780 15.969 1.00 53.79 ? 88 VAL A C 1 ATOM 463 O O . VAL A 1 61 ? -6.877 -23.963 16.639 1.00 53.29 ? 88 VAL A O 1 ATOM 464 C CB . VAL A 1 61 ? -7.371 -24.651 13.757 1.00 72.96 ? 88 VAL A CB 1 ATOM 465 C CG1 . VAL A 1 61 ? -6.184 -23.821 13.279 1.00 70.16 ? 88 VAL A CG1 1 ATOM 466 C CG2 . VAL A 1 61 ? -8.014 -25.431 12.594 1.00 73.41 ? 88 VAL A CG2 1 ATOM 467 N N . LEU A 1 62 ? -4.951 -25.011 16.060 1.00 45.13 ? 89 LEU A N 1 ATOM 468 C CA . LEU A 1 62 ? -4.051 -24.172 16.818 1.00 53.74 ? 89 LEU A CA 1 ATOM 469 C C . LEU A 1 62 ? -3.437 -23.139 15.900 1.00 60.34 ? 89 LEU A C 1 ATOM 470 O O . LEU A 1 62 ? -2.721 -23.462 14.956 1.00 60.72 ? 89 LEU A O 1 ATOM 471 C CB . LEU A 1 62 ? -2.961 -25.021 17.467 1.00 49.67 ? 89 LEU A CB 1 ATOM 472 C CG . LEU A 1 62 ? -1.810 -24.319 18.186 1.00 57.12 ? 89 LEU A CG 1 ATOM 473 C CD1 . LEU A 1 62 ? -2.307 -23.557 19.403 1.00 59.13 ? 89 LEU A CD1 1 ATOM 474 C CD2 . LEU A 1 62 ? -0.711 -25.300 18.590 1.00 59.09 ? 89 LEU A CD2 1 ATOM 475 N N . ARG A 1 63 ? -3.702 -21.881 16.223 1.00 57.58 ? 90 ARG A N 1 ATOM 476 C CA . ARG A 1 63 ? -3.194 -20.769 15.455 1.00 54.81 ? 90 ARG A CA 1 ATOM 477 C C . ARG A 1 63 ? -2.225 -19.936 16.256 1.00 55.13 ? 90 ARG A C 1 ATOM 478 O O . ARG A 1 63 ? -2.489 -19.549 17.398 1.00 63.22 ? 90 ARG A O 1 ATOM 479 C CB . ARG A 1 63 ? -4.360 -19.905 14.984 1.00 57.44 ? 90 ARG A CB 1 ATOM 480 C CG . ARG A 1 63 ? -3.963 -18.582 14.376 1.00 68.16 ? 90 ARG A CG 1 ATOM 481 C CD . ARG A 1 63 ? -5.190 -17.708 14.170 1.00 76.56 ? 90 ARG A CD 1 ATOM 482 N NE . ARG A 1 63 ? -4.888 -16.490 13.428 1.00 75.04 ? 90 ARG A NE 1 ATOM 483 C CZ . ARG A 1 63 ? -4.904 -16.404 12.102 1.00 63.94 ? 90 ARG A CZ 1 ATOM 484 N NH1 . ARG A 1 63 ? -5.200 -17.472 11.374 1.00 66.44 ? 90 ARG A NH1 1 ATOM 485 N NH2 . ARG A 1 63 ? -4.620 -15.256 11.504 1.00 52.26 ? 90 ARG A NH2 1 ATOM 486 N N . ILE A 1 64 ? -1.092 -19.663 15.629 1.00 54.27 ? 91 ILE A N 1 ATOM 487 C CA . ILE A 1 64 ? -0.057 -18.871 16.247 1.00 58.01 ? 91 ILE A CA 1 ATOM 488 C C . ILE A 1 64 ? 0.163 -17.643 15.390 1.00 62.28 ? 91 ILE A C 1 ATOM 489 O O . ILE A 1 64 ? 0.466 -17.735 14.191 1.00 61.24 ? 91 ILE A O 1 ATOM 490 C CB . ILE A 1 64 ? 1.243 -19.676 16.364 1.00 54.16 ? 91 ILE A CB 1 ATOM 491 C CG1 . ILE A 1 64 ? 0.923 -21.098 16.839 1.00 48.82 ? 91 ILE A CG1 1 ATOM 492 C CG2 . ILE A 1 64 ? 2.242 -18.970 17.272 1.00 54.22 ? 91 ILE A CG2 1 ATOM 493 C CD1 . ILE A 1 64 ? 2.010 -22.106 16.575 1.00 49.03 ? 91 ILE A CD1 1 ATOM 494 N N . GLN A 1 65 ? -0.002 -16.494 16.028 1.00 64.05 ? 92 GLN A N 1 ATOM 495 C CA . GLN A 1 65 ? 0.134 -15.203 15.385 1.00 59.02 ? 92 GLN A CA 1 ATOM 496 C C . GLN A 1 65 ? 0.283 -14.166 16.490 1.00 64.08 ? 92 GLN A C 1 ATOM 497 O O . GLN A 1 65 ? -0.463 -14.203 17.470 1.00 71.34 ? 92 GLN A O 1 ATOM 498 C CB . GLN A 1 65 ? -1.080 -14.924 14.503 1.00 58.04 ? 92 GLN A CB 1 ATOM 499 C CG . GLN A 1 65 ? -1.179 -13.527 13.954 1.00 60.63 ? 92 GLN A CG 1 ATOM 500 C CD . GLN A 1 65 ? -2.555 -13.262 13.369 1.00 70.51 ? 92 GLN A CD 1 ATOM 501 O OE1 . GLN A 1 65 ? -3.513 -13.984 13.659 1.00 67.83 ? 92 GLN A OE1 1 ATOM 502 N NE2 . GLN A 1 65 ? -2.663 -12.227 12.543 1.00 83.89 ? 92 GLN A NE2 1 ATOM 503 N N . PRO A 1 66 ? 1.233 -13.233 16.344 1.00 67.71 ? 93 PRO A N 1 ATOM 504 C CA . PRO A 1 66 ? 2.315 -13.233 15.356 1.00 71.40 ? 93 PRO A CA 1 ATOM 505 C C . PRO A 1 66 ? 3.402 -14.250 15.681 1.00 75.99 ? 93 PRO A C 1 ATOM 506 O O . PRO A 1 66 ? 3.704 -14.469 16.854 1.00 86.17 ? 93 PRO A O 1 ATOM 507 C CB . PRO A 1 66 ? 2.859 -11.810 15.451 1.00 73.47 ? 93 PRO A CB 1 ATOM 508 C CG . PRO A 1 66 ? 2.632 -11.438 16.876 1.00 69.48 ? 93 PRO A CG 1 ATOM 509 C CD . PRO A 1 66 ? 1.321 -12.074 17.251 1.00 69.17 ? 93 PRO A CD 1 ATOM 510 N N . LEU A 1 67 ? 3.968 -14.872 14.652 1.00 75.01 ? 94 LEU A N 1 ATOM 511 C CA . LEU A 1 67 ? 5.058 -15.819 14.842 1.00 76.54 ? 94 LEU A CA 1 ATOM 512 C C . LEU A 1 67 ? 6.287 -15.118 15.429 1.00 76.22 ? 94 LEU A C 1 ATOM 513 O O . LEU A 1 67 ? 6.627 -14.004 15.038 1.00 84.92 ? 94 LEU A O 1 ATOM 514 C CB . LEU A 1 67 ? 5.413 -16.496 13.514 1.00 72.53 ? 94 LEU A CB 1 ATOM 515 C CG . LEU A 1 67 ? 4.333 -17.406 12.927 1.00 65.69 ? 94 LEU A CG 1 ATOM 516 C CD1 . LEU A 1 67 ? 4.717 -17.914 11.546 1.00 67.07 ? 94 LEU A CD1 1 ATOM 517 C CD2 . LEU A 1 67 ? 4.079 -18.566 13.866 1.00 63.24 ? 94 LEU A CD2 1 ATOM 518 N N . ARG A 1 68 ? 6.958 -15.799 16.349 1.00 61.88 ? 95 ARG A N 1 ATOM 519 C CA . ARG A 1 68 ? 8.204 -15.303 16.910 1.00 64.94 ? 95 ARG A CA 1 ATOM 520 C C . ARG A 1 68 ? 9.278 -16.370 16.764 1.00 76.05 ? 95 ARG A C 1 ATOM 521 O O . ARG A 1 68 ? 8.999 -17.560 16.888 1.00 80.18 ? 95 ARG A O 1 ATOM 522 C CB . ARG A 1 68 ? 8.039 -14.919 18.384 1.00 71.78 ? 95 ARG A CB 1 ATOM 523 C CG . ARG A 1 68 ? 8.015 -13.422 18.659 1.00 83.58 ? 95 ARG A CG 1 ATOM 524 C CD . ARG A 1 68 ? 6.627 -12.852 18.459 1.00 90.49 ? 95 ARG A CD 1 ATOM 525 N NE . ARG A 1 68 ? 6.596 -11.823 17.426 1.00 98.87 ? 95 ARG A NE 1 ATOM 526 C CZ . ARG A 1 68 ? 6.492 -10.521 17.672 1.00 104.04 ? 95 ARG A CZ 1 ATOM 527 N NH1 . ARG A 1 68 ? 6.409 -10.081 18.922 1.00 106.43 ? 95 ARG A NH1 1 ATOM 528 N NH2 . ARG A 1 68 ? 6.467 -9.658 16.665 1.00 101.29 ? 95 ARG A NH2 1 ATOM 529 N N . THR A 1 69 ? 10.497 -15.939 16.466 1.00 87.05 ? 96 THR A N 1 ATOM 530 C CA . THR A 1 69 ? 11.623 -16.849 16.318 1.00 89.84 ? 96 THR A CA 1 ATOM 531 C C . THR A 1 69 ? 12.795 -16.395 17.182 1.00 89.78 ? 96 THR A C 1 ATOM 532 O O . THR A 1 69 ? 13.113 -15.202 17.242 1.00 89.93 ? 96 THR A O 1 ATOM 533 C CB . THR A 1 69 ? 12.056 -16.965 14.848 1.00 96.48 ? 96 THR A CB 1 ATOM 534 O OG1 . THR A 1 69 ? 13.123 -17.915 14.738 1.00 100.22 ? 96 THR A OG1 1 ATOM 535 C CG2 . THR A 1 69 ? 12.510 -15.613 14.297 1.00 97.76 ? 96 THR A CG2 1 ATOM 536 N N . PRO A 1 70 ? 13.440 -17.338 17.888 1.00 85.43 ? 97 PRO A N 1 ATOM 537 C CA . PRO A 1 70 ? 13.234 -18.793 17.916 1.00 83.21 ? 97 PRO A CA 1 ATOM 538 C C . PRO A 1 70 ? 12.092 -19.264 18.811 1.00 83.77 ? 97 PRO A C 1 ATOM 539 O O . PRO A 1 70 ? 11.839 -20.469 18.874 1.00 82.85 ? 97 PRO A O 1 ATOM 540 C CB . PRO A 1 70 ? 14.574 -19.335 18.447 1.00 81.34 ? 97 PRO A CB 1 ATOM 541 C CG . PRO A 1 70 ? 15.458 -18.135 18.689 1.00 83.95 ? 97 PRO A CG 1 ATOM 542 C CD . PRO A 1 70 ? 14.570 -16.935 18.734 1.00 85.18 ? 97 PRO A CD 1 ATOM 543 N N . ARG A 1 71 ? 11.434 -18.327 19.488 1.00 83.52 ? 98 ARG A N 1 ATOM 544 C CA . ARG A 1 71 ? 10.419 -18.607 20.502 1.00 83.05 ? 98 ARG A CA 1 ATOM 545 C C . ARG A 1 71 ? 9.477 -19.753 20.136 1.00 83.83 ? 98 ARG A C 1 ATOM 546 O O . ARG A 1 71 ? 9.277 -20.682 20.922 1.00 87.94 ? 98 ARG A O 1 ATOM 547 C CB . ARG A 1 71 ? 9.587 -17.352 20.766 1.00 85.32 ? 98 ARG A CB 1 ATOM 548 C CG . ARG A 1 71 ? 10.312 -16.258 21.525 1.00 89.01 ? 98 ARG A CG 1 ATOM 549 C CD . ARG A 1 71 ? 9.418 -15.039 21.643 1.00 92.89 ? 98 ARG A CD 1 ATOM 550 N NE . ARG A 1 71 ? 10.030 -13.946 22.388 1.00 102.22 ? 98 ARG A NE 1 ATOM 551 C CZ . ARG A 1 71 ? 10.962 -13.134 21.896 1.00 108.74 ? 98 ARG A CZ 1 ATOM 552 N NH1 . ARG A 1 71 ? 11.406 -13.299 20.656 1.00 108.27 ? 98 ARG A NH1 1 ATOM 553 N NH2 . ARG A 1 71 ? 11.458 -12.161 22.647 1.00 111.94 ? 98 ARG A NH2 1 ATOM 554 N N . ASP A 1 72 ? 8.906 -19.678 18.939 1.00 76.65 ? 99 ASP A N 1 ATOM 555 C CA . ASP A 1 72 ? 7.845 -20.586 18.519 1.00 69.65 ? 99 ASP A CA 1 ATOM 556 C C . ASP A 1 72 ? 8.389 -21.844 17.853 1.00 79.79 ? 99 ASP A C 1 ATOM 557 O O . ASP A 1 72 ? 7.626 -22.766 17.572 1.00 82.45 ? 99 ASP A O 1 ATOM 558 C CB . ASP A 1 72 ? 6.885 -19.885 17.554 1.00 60.62 ? 99 ASP A CB 1 ATOM 559 C CG . ASP A 1 72 ? 6.238 -18.658 18.160 1.00 66.94 ? 99 ASP A CG 1 ATOM 560 O OD1 . ASP A 1 72 ? 6.155 -18.580 19.403 1.00 75.29 ? 99 ASP A OD1 1 ATOM 561 O OD2 . ASP A 1 72 ? 5.808 -17.774 17.392 1.00 65.32 ? 99 ASP A OD2 1 ATOM 562 N N . GLU A 1 73 ? 9.690 -21.884 17.576 1.00 81.39 ? 100 GLU A N 1 ATOM 563 C CA . GLU A 1 73 ? 10.235 -23.056 16.907 1.00 77.68 ? 100 GLU A CA 1 ATOM 564 C C . GLU A 1 73 ? 10.165 -24.230 17.863 1.00 85.41 ? 100 GLU A C 1 ATOM 565 O O . GLU A 1 73 ? 10.794 -24.191 18.921 1.00 90.98 ? 100 GLU A O 1 ATOM 566 C CB . GLU A 1 73 ? 11.689 -22.804 16.509 1.00 73.06 ? 100 GLU A CB 1 ATOM 567 C CG . GLU A 1 73 ? 12.032 -23.154 15.090 1.00 80.50 ? 100 GLU A CG 1 ATOM 568 C CD . GLU A 1 73 ? 12.628 -21.977 14.358 1.00 88.94 ? 100 GLU A CD 1 ATOM 569 O OE1 . GLU A 1 73 ? 13.559 -21.345 14.898 1.00 87.36 ? 100 GLU A OE1 1 ATOM 570 O OE2 . GLU A 1 73 ? 12.156 -21.672 13.248 1.00 95.74 ? 100 GLU A OE2 1 ATOM 571 N N . ALA A 1 74 ? 9.464 -25.296 17.472 1.00 91.33 ? 101 ALA A N 1 ATOM 572 C CA . ALA A 1 74 ? 9.260 -26.417 18.403 1.00 91.86 ? 101 ALA A CA 1 ATOM 573 C C . ALA A 1 74 ? 8.513 -27.606 17.812 1.00 91.25 ? 101 ALA A C 1 ATOM 574 O O . ALA A 1 74 ? 7.943 -27.522 16.732 1.00 91.49 ? 101 ALA A O 1 ATOM 575 C CB . ALA A 1 74 ? 8.510 -25.933 19.649 1.00 89.74 ? 101 ALA A CB 1 ATOM 576 N N . ILE A 1 75 ? 8.515 -28.715 18.546 1.00 85.42 ? 102 ILE A N 1 ATOM 577 C CA . ILE A 1 75 ? 7.577 -29.804 18.307 1.00 77.51 ? 102 ILE A CA 1 ATOM 578 C C . ILE A 1 75 ? 6.310 -29.622 19.137 1.00 82.45 ? 102 ILE A C 1 ATOM 579 O O . ILE A 1 75 ? 6.396 -29.412 20.346 1.00 86.86 ? 102 ILE A O 1 ATOM 580 C CB . ILE A 1 75 ? 8.197 -31.169 18.654 1.00 74.97 ? 102 ILE A CB 1 ATOM 581 C CG1 . ILE A 1 75 ? 9.612 -31.288 18.088 1.00 82.52 ? 102 ILE A CG1 1 ATOM 582 C CG2 . ILE A 1 75 ? 7.304 -32.300 18.172 1.00 74.25 ? 102 ILE A CG2 1 ATOM 583 C CD1 . ILE A 1 75 ? 9.669 -31.449 16.581 1.00 82.99 ? 102 ILE A CD1 1 ATOM 584 N N . TYR A 1 76 ? 5.143 -29.696 18.507 1.00 85.47 ? 103 TYR A N 1 ATOM 585 C CA . TYR A 1 76 ? 3.890 -29.646 19.253 1.00 80.24 ? 103 TYR A CA 1 ATOM 586 C C . TYR A 1 76 ? 3.144 -30.972 19.074 1.00 88.20 ? 103 TYR A C 1 ATOM 587 O O . TYR A 1 76 ? 3.391 -31.686 18.101 1.00 84.45 ? 103 TYR A O 1 ATOM 588 C CB . TYR A 1 76 ? 3.028 -28.467 18.782 1.00 59.29 ? 103 TYR A CB 1 ATOM 589 C CG . TYR A 1 76 ? 3.696 -27.115 18.930 1.00 50.57 ? 103 TYR A CG 1 ATOM 590 C CD1 . TYR A 1 76 ? 4.603 -26.652 17.981 1.00 60.39 ? 103 TYR A CD1 1 ATOM 591 C CD2 . TYR A 1 76 ? 3.410 -26.299 20.012 1.00 50.11 ? 103 TYR A CD2 1 ATOM 592 C CE1 . TYR A 1 76 ? 5.210 -25.416 18.114 1.00 68.89 ? 103 TYR A CE1 1 ATOM 593 C CE2 . TYR A 1 76 ? 4.009 -25.065 20.154 1.00 60.86 ? 103 TYR A CE2 1 ATOM 594 C CZ . TYR A 1 76 ? 4.908 -24.626 19.203 1.00 71.58 ? 103 TYR A CZ 1 ATOM 595 O OH . TYR A 1 76 ? 5.503 -23.394 19.352 1.00 77.28 ? 103 TYR A OH 1 ATOM 596 N N . GLU A 1 77 ? 2.238 -31.321 19.985 1.00 92.09 ? 104 GLU A N 1 ATOM 597 C CA . GLU A 1 77 ? 1.503 -32.570 19.784 1.00 95.45 ? 104 GLU A CA 1 ATOM 598 C C . GLU A 1 77 ? 0.000 -32.329 19.904 1.00 88.99 ? 104 GLU A C 1 ATOM 599 O O . GLU A 1 77 ? -0.460 -31.636 20.814 1.00 92.56 ? 104 GLU A O 1 ATOM 600 C CB . GLU A 1 77 ? 1.971 -33.675 20.741 1.00 109.28 ? 104 GLU A CB 1 ATOM 601 C CG . GLU A 1 77 ? 2.118 -33.283 22.188 1.00 120.79 ? 104 GLU A CG 1 ATOM 602 C CD . GLU A 1 77 ? 2.341 -34.496 23.069 1.00 128.95 ? 104 GLU A CD 1 ATOM 603 O OE1 . GLU A 1 77 ? 2.627 -34.316 24.267 1.00 130.56 ? 104 GLU A OE1 1 ATOM 604 O OE2 . GLU A 1 77 ? 2.225 -35.630 22.558 1.00 130.43 ? 104 GLU A OE2 1 ATOM 605 N N . CYS A 1 78 ? -0.758 -32.897 18.973 1.00 77.83 ? 105 CYS A N 1 ATOM 606 C CA . CYS A 1 78 ? -2.203 -33.032 19.120 1.00 75.06 ? 105 CYS A CA 1 ATOM 607 C C . CYS A 1 78 ? -2.607 -34.358 19.752 1.00 78.99 ? 105 CYS A C 1 ATOM 608 O O . CYS A 1 78 ? -2.260 -35.427 19.250 1.00 85.76 ? 105 CYS A O 1 ATOM 609 C CB . CYS A 1 78 ? -2.880 -32.875 17.760 1.00 74.99 ? 105 CYS A CB 1 ATOM 610 S SG . CYS A 1 78 ? -4.630 -33.266 17.721 1.00 82.12 ? 105 CYS A SG 1 ATOM 611 N N . VAL A 1 79 ? -3.369 -34.277 20.838 1.00 74.50 ? 106 VAL A N 1 ATOM 612 C CA . VAL A 1 79 ? -3.790 -35.468 21.563 1.00 71.81 ? 106 VAL A CA 1 ATOM 613 C C . VAL A 1 79 ? -5.305 -35.595 21.571 1.00 71.97 ? 106 VAL A C 1 ATOM 614 O O . VAL A 1 79 ? -5.995 -34.721 22.090 1.00 72.51 ? 106 VAL A O 1 ATOM 615 C CB . VAL A 1 79 ? -3.290 -35.454 23.019 1.00 73.53 ? 106 VAL A CB 1 ATOM 616 C CG1 . VAL A 1 79 ? -3.865 -36.633 23.794 1.00 76.14 ? 106 VAL A CG1 1 ATOM 617 C CG2 . VAL A 1 79 ? -1.769 -35.454 23.073 1.00 72.44 ? 106 VAL A CG2 1 ATOM 618 N N . ALA A 1 80 ? -5.825 -36.662 20.969 1.00 71.82 ? 107 ALA A N 1 ATOM 619 C CA . ALA A 1 80 ? -7.261 -36.911 20.994 1.00 73.43 ? 107 ALA A CA 1 ATOM 620 C C . ALA A 1 80 ? -7.595 -38.026 21.981 1.00 78.31 ? 107 ALA A C 1 ATOM 621 O O . ALA A 1 80 ? -6.978 -39.095 21.951 1.00 80.58 ? 107 ALA A O 1 ATOM 622 C CB . ALA A 1 80 ? -7.758 -37.261 19.608 1.00 72.67 ? 107 ALA A CB 1 ATOM 623 N N . SER A 1 81 ? -8.589 -37.787 22.834 1.00 83.27 ? 108 SER A N 1 ATOM 624 C CA . SER A 1 81 ? -8.935 -38.777 23.856 1.00 86.50 ? 108 SER A CA 1 ATOM 625 C C . SER A 1 81 ? -10.421 -38.979 24.163 1.00 84.61 ? 108 SER A C 1 ATOM 626 O O . SER A 1 81 ? -11.232 -38.062 24.010 1.00 75.68 ? 108 SER A O 1 ATOM 627 C CB . SER A 1 81 ? -8.221 -38.414 25.163 1.00 93.01 ? 108 SER A CB 1 ATOM 628 O OG . SER A 1 81 ? -8.390 -37.040 25.478 1.00 95.81 ? 108 SER A OG 1 ATOM 629 N N . ASN A 1 82 ? -10.768 -40.208 24.537 1.00 94.19 ? 109 ASN A N 1 ATOM 630 C CA . ASN A 1 82 ? -12.005 -40.473 25.257 1.00 93.46 ? 109 ASN A CA 1 ATOM 631 C C . ASN A 1 82 ? -11.754 -41.564 26.306 1.00 99.26 ? 109 ASN A C 1 ATOM 632 O O . ASN A 1 82 ? -10.626 -42.066 26.429 1.00 104.69 ? 109 ASN A O 1 ATOM 633 C CB . ASN A 1 82 ? -13.129 -40.878 24.301 1.00 80.77 ? 109 ASN A CB 1 ATOM 634 C CG . ASN A 1 82 ? -12.741 -42.013 23.382 1.00 75.39 ? 109 ASN A CG 1 ATOM 635 O OD1 . ASN A 1 82 ? -11.845 -42.802 23.681 1.00 72.19 ? 109 ASN A OD1 1 ATOM 636 N ND2 . ASN A 1 82 ? -13.423 -42.105 22.251 1.00 82.41 ? 109 ASN A ND2 1 ATOM 637 N N . ASN A 1 83 ? -12.810 -41.995 26.993 1.00 95.18 ? 110 ASN A N 1 ATOM 638 C CA . ASN A 1 83 ? -12.671 -42.994 28.053 1.00 97.10 ? 110 ASN A CA 1 ATOM 639 C C . ASN A 1 83 ? -12.300 -44.369 27.505 1.00 91.15 ? 110 ASN A C 1 ATOM 640 O O . ASN A 1 83 ? -11.931 -45.265 28.262 1.00 94.03 ? 110 ASN A O 1 ATOM 641 C CB . ASN A 1 83 ? -13.939 -43.070 28.920 1.00 106.05 ? 110 ASN A CB 1 ATOM 642 C CG . ASN A 1 83 ? -15.196 -43.273 28.115 1.00 116.43 ? 110 ASN A CG 1 ATOM 643 O OD1 . ASN A 1 83 ? -15.692 -42.346 27.476 1.00 121.69 ? 110 ASN A OD1 1 ATOM 644 N ND2 . ASN A 1 83 ? -15.746 -44.478 28.173 1.00 123.07 ? 110 ASN A ND2 1 ATOM 645 N N . VAL A 1 84 ? -12.358 -44.510 26.187 1.00 81.31 ? 111 VAL A N 1 ATOM 646 C CA . VAL A 1 84 ? -12.012 -45.753 25.535 1.00 76.49 ? 111 VAL A CA 1 ATOM 647 C C . VAL A 1 84 ? -10.550 -45.732 25.094 1.00 85.31 ? 111 VAL A C 1 ATOM 648 O O . VAL A 1 84 ? -9.955 -46.781 24.887 1.00 96.26 ? 111 VAL A O 1 ATOM 649 C CB . VAL A 1 84 ? -12.913 -46.038 24.323 1.00 79.48 ? 111 VAL A CB 1 ATOM 650 C CG1 . VAL A 1 84 ? -13.034 -47.527 24.068 1.00 83.14 ? 111 VAL A CG1 1 ATOM 651 C CG2 . VAL A 1 84 ? -14.288 -45.444 24.555 1.00 88.99 ? 111 VAL A CG2 1 ATOM 652 N N . GLY A 1 85 ? -9.970 -44.550 24.928 1.00 88.09 ? 112 GLY A N 1 ATOM 653 C CA . GLY A 1 85 ? -8.608 -44.508 24.437 1.00 90.03 ? 112 GLY A CA 1 ATOM 654 C C . GLY A 1 85 ? -7.981 -43.147 24.198 1.00 83.59 ? 112 GLY A C 1 ATOM 655 O O . GLY A 1 85 ? -8.628 -42.110 24.279 1.00 74.31 ? 112 GLY A O 1 ATOM 656 N N . GLU A 1 86 ? -6.703 -43.175 23.845 1.00 84.58 ? 113 GLU A N 1 ATOM 657 C CA . GLU A 1 86 ? -5.946 -41.954 23.620 1.00 81.24 ? 113 GLU A CA 1 ATOM 658 C C . GLU A 1 86 ? -4.956 -42.122 22.473 1.00 83.04 ? 113 GLU A C 1 ATOM 659 O O . GLU A 1 86 ? -4.327 -43.170 22.343 1.00 88.24 ? 113 GLU A O 1 ATOM 660 C CB . GLU A 1 86 ? -5.212 -41.563 24.893 1.00 83.99 ? 113 GLU A CB 1 ATOM 661 C CG . GLU A 1 86 ? -4.656 -40.165 24.915 1.00 93.62 ? 113 GLU A CG 1 ATOM 662 C CD . GLU A 1 86 ? -4.100 -39.809 26.276 1.00 101.94 ? 113 GLU A CD 1 ATOM 663 O OE1 . GLU A 1 86 ? -4.449 -38.729 26.800 1.00 105.25 ? 113 GLU A OE1 1 ATOM 664 O OE2 . GLU A 1 86 ? -3.304 -40.602 26.821 1.00 102.36 ? 113 GLU A OE2 1 ATOM 665 N N . ILE A 1 87 ? -4.818 -41.092 21.646 1.00 76.71 ? 114 ILE A N 1 ATOM 666 C CA . ILE A 1 87 ? -3.858 -41.130 20.551 1.00 75.33 ? 114 ILE A CA 1 ATOM 667 C C . ILE A 1 87 ? -3.215 -39.760 20.386 1.00 82.16 ? 114 ILE A C 1 ATOM 668 O O . ILE A 1 87 ? -3.888 -38.740 20.488 1.00 83.12 ? 114 ILE A O 1 ATOM 669 C CB . ILE A 1 87 ? -4.487 -41.555 19.213 1.00 68.90 ? 114 ILE A CB 1 ATOM 670 C CG1 . ILE A 1 87 ? -5.744 -40.726 18.923 1.00 67.01 ? 114 ILE A CG1 1 ATOM 671 C CG2 . ILE A 1 87 ? -4.801 -43.039 19.212 1.00 54.22 ? 114 ILE A CG2 1 ATOM 672 C CD1 . ILE A 1 87 ? -6.366 -41.025 17.581 1.00 69.19 ? 114 ILE A CD1 1 ATOM 673 N N . SER A 1 88 ? -1.918 -39.719 20.103 1.00 77.97 ? 115 SER A N 1 ATOM 674 C CA . SER A 1 88 ? -1.293 -38.423 19.900 1.00 81.98 ? 115 SER A CA 1 ATOM 675 C C . SER A 1 88 ? -0.475 -38.413 18.614 1.00 84.73 ? 115 SER A C 1 ATOM 676 O O . SER A 1 88 ? -0.016 -39.452 18.154 1.00 89.63 ? 115 SER A O 1 ATOM 677 C CB . SER A 1 88 ? -0.399 -38.063 21.084 1.00 87.48 ? 115 SER A CB 1 ATOM 678 O OG . SER A 1 88 ? 0.805 -38.796 21.037 1.00 91.58 ? 115 SER A OG 1 ATOM 679 N N . VAL A 1 89 ? -0.308 -37.218 18.050 1.00 80.60 ? 116 VAL A N 1 ATOM 680 C CA . VAL A 1 89 ? 0.577 -37.039 16.917 1.00 79.50 ? 116 VAL A CA 1 ATOM 681 C C . VAL A 1 89 ? 1.435 -35.781 17.048 1.00 78.23 ? 116 VAL A C 1 ATOM 682 O O . VAL A 1 89 ? 0.947 -34.742 17.497 1.00 79.53 ? 116 VAL A O 1 ATOM 683 C CB . VAL A 1 89 ? -0.230 -36.997 15.590 1.00 79.03 ? 116 VAL A CB 1 ATOM 684 C CG1 . VAL A 1 89 ? -1.316 -35.924 15.649 1.00 70.99 ? 116 VAL A CG1 1 ATOM 685 C CG2 . VAL A 1 89 ? 0.679 -36.796 14.392 1.00 92.11 ? 116 VAL A CG2 1 ATOM 686 N N . SER A 1 90 ? 2.704 -35.870 16.650 1.00 72.01 ? 117 SER A N 1 ATOM 687 C CA . SER A 1 90 ? 3.643 -34.767 16.801 1.00 68.69 ? 117 SER A CA 1 ATOM 688 C C . SER A 1 90 ? 3.726 -33.997 15.475 1.00 66.89 ? 117 SER A C 1 ATOM 689 O O . SER A 1 90 ? 3.389 -34.537 14.421 1.00 69.54 ? 117 SER A O 1 ATOM 690 C CB . SER A 1 90 ? 5.021 -35.279 17.245 1.00 75.67 ? 117 SER A CB 1 ATOM 691 O OG . SER A 1 90 ? 5.397 -36.452 16.543 1.00 81.28 ? 117 SER A OG 1 ATOM 692 N N . THR A 1 91 ? 4.153 -32.738 15.526 1.00 63.04 ? 118 THR A N 1 ATOM 693 C CA . THR A 1 91 ? 4.374 -31.923 14.331 1.00 68.71 ? 118 THR A CA 1 ATOM 694 C C . THR A 1 91 ? 5.411 -30.844 14.623 1.00 78.61 ? 118 THR A C 1 ATOM 695 O O . THR A 1 91 ? 5.621 -30.503 15.783 1.00 80.96 ? 118 THR A O 1 ATOM 696 C CB . THR A 1 91 ? 3.066 -31.257 13.821 1.00 83.03 ? 118 THR A CB 1 ATOM 697 O OG1 . THR A 1 91 ? 3.300 -30.616 12.560 1.00 80.45 ? 118 THR A OG1 1 ATOM 698 C CG2 . THR A 1 91 ? 2.565 -30.223 14.805 1.00 88.05 ? 118 THR A CG2 1 ATOM 699 N N . ARG A 1 92 ? 6.070 -30.308 13.597 1.00 84.48 ? 119 ARG A N 1 ATOM 700 C CA . ARG A 1 92 ? 7.133 -29.337 13.853 1.00 85.39 ? 119 ARG A CA 1 ATOM 701 C C . ARG A 1 92 ? 6.779 -27.968 13.284 1.00 85.80 ? 119 ARG A C 1 ATOM 702 O O . ARG A 1 92 ? 6.278 -27.848 12.169 1.00 89.43 ? 119 ARG A O 1 ATOM 703 C CB . ARG A 1 92 ? 8.460 -29.813 13.254 1.00 95.09 ? 119 ARG A CB 1 ATOM 704 C CG . ARG A 1 92 ? 9.558 -28.747 13.255 1.00 108.18 ? 119 ARG A CG 1 ATOM 705 C CD . ARG A 1 92 ? 10.787 -29.174 12.459 1.00 116.26 ? 119 ARG A CD 1 ATOM 706 N NE . ARG A 1 92 ? 11.401 -30.390 12.985 1.00 117.13 ? 119 ARG A NE 1 ATOM 707 C CZ . ARG A 1 92 ? 12.128 -30.443 14.098 1.00 110.65 ? 119 ARG A CZ 1 ATOM 708 N NH1 . ARG A 1 92 ? 12.329 -29.348 14.821 1.00 105.21 ? 119 ARG A NH1 1 ATOM 709 N NH2 . ARG A 1 92 ? 12.650 -31.596 14.496 1.00 112.05 ? 119 ARG A NH2 1 ATOM 710 N N . LEU A 1 93 ? 7.071 -26.937 14.070 1.00 79.73 ? 120 LEU A N 1 ATOM 711 C CA . LEU A 1 93 ? 7.016 -25.562 13.610 1.00 70.02 ? 120 LEU A CA 1 ATOM 712 C C . LEU A 1 93 ? 8.408 -24.948 13.517 1.00 69.56 ? 120 LEU A C 1 ATOM 713 O O . LEU A 1 93 ? 9.165 -24.902 14.504 1.00 69.64 ? 120 LEU A O 1 ATOM 714 C CB . LEU A 1 93 ? 6.135 -24.747 14.550 1.00 65.18 ? 120 LEU A CB 1 ATOM 715 C CG . LEU A 1 93 ? 6.086 -23.243 14.324 1.00 61.47 ? 120 LEU A CG 1 ATOM 716 C CD1 . LEU A 1 93 ? 5.456 -22.931 12.980 1.00 55.62 ? 120 LEU A CD1 1 ATOM 717 C CD2 . LEU A 1 93 ? 5.312 -22.595 15.446 1.00 61.27 ? 120 LEU A CD2 1 ATOM 718 N N . THR A 1 94 ? 8.686 -24.424 12.328 1.00 72.25 ? 121 THR A N 1 ATOM 719 C CA . THR A 1 94 ? 9.864 -23.626 12.024 1.00 72.69 ? 121 THR A CA 1 ATOM 720 C C . THR A 1 94 ? 9.483 -22.192 11.668 1.00 71.01 ? 121 THR A C 1 ATOM 721 O O . THR A 1 94 ? 8.459 -21.977 11.025 1.00 62.80 ? 121 THR A O 1 ATOM 722 C CB . THR A 1 94 ? 10.641 -24.241 10.831 1.00 78.22 ? 121 THR A CB 1 ATOM 723 O OG1 . THR A 1 94 ? 10.722 -25.662 10.982 1.00 78.87 ? 121 THR A OG1 1 ATOM 724 C CG2 . THR A 1 94 ? 12.041 -23.649 10.717 1.00 81.56 ? 121 THR A CG2 1 ATOM 725 N N . VAL A 1 95 ? 10.276 -21.213 12.105 1.00 80.58 ? 122 VAL A N 1 ATOM 726 C CA . VAL A 1 95 ? 9.982 -19.806 11.813 1.00 84.87 ? 122 VAL A CA 1 ATOM 727 C C . VAL A 1 95 ? 11.230 -19.078 11.301 1.00 80.72 ? 122 VAL A C 1 ATOM 728 O O . VAL A 1 95 ? 12.220 -18.938 12.023 1.00 75.22 ? 122 VAL A O 1 ATOM 729 C CB . VAL A 1 95 ? 9.463 -19.065 13.068 1.00 75.71 ? 122 VAL A CB 1 ATOM 730 C CG1 . VAL A 1 95 ? 9.003 -17.673 12.694 1.00 77.30 ? 122 VAL A CG1 1 ATOM 731 C CG2 . VAL A 1 95 ? 8.336 -19.843 13.740 1.00 65.53 ? 122 VAL A CG2 1 ATOM 732 N N . LEU A 1 96 ? 11.175 -18.605 10.058 1.00 85.28 ? 123 LEU A N 1 ATOM 733 C CA . LEU A 1 96 ? 12.298 -17.881 9.458 1.00 87.89 ? 123 LEU A CA 1 ATOM 734 C C . LEU A 1 96 ? 12.194 -16.366 9.608 1.00 92.93 ? 123 LEU A C 1 ATOM 735 O O . LEU A 1 96 ? 11.105 -15.805 9.517 1.00 91.78 ? 123 LEU A O 1 ATOM 736 C CB . LEU A 1 96 ? 12.402 -18.234 7.971 1.00 81.33 ? 123 LEU A CB 1 ATOM 737 C CG . LEU A 1 96 ? 12.275 -19.718 7.641 1.00 72.96 ? 123 LEU A CG 1 ATOM 738 C CD1 . LEU A 1 96 ? 12.356 -19.940 6.142 1.00 69.08 ? 123 LEU A CD1 1 ATOM 739 C CD2 . LEU A 1 96 ? 13.345 -20.517 8.366 1.00 82.69 ? 123 LEU A CD2 1 ATOM 740 N N . ARG A 1 97 ? 13.326 -15.704 9.833 1.00 97.57 ? 124 ARG A N 1 ATOM 741 C CA . ARG A 1 97 ? 13.385 -14.246 9.746 1.00 105.15 ? 124 ARG A CA 1 ATOM 742 C C . ARG A 1 97 ? 13.265 -13.743 8.309 1.00 112.33 ? 124 ARG A C 1 ATOM 743 O O . ARG A 1 97 ? 13.681 -14.429 7.368 1.00 114.70 ? 124 ARG A O 1 ATOM 744 C CB . ARG A 1 97 ? 14.690 -13.734 10.353 1.00 111.13 ? 124 ARG A CB 1 ATOM 745 C CG . ARG A 1 97 ? 15.068 -14.382 11.672 1.00 117.82 ? 124 ARG A CG 1 ATOM 746 C CD . ARG A 1 97 ? 16.514 -14.071 12.040 1.00 129.32 ? 124 ARG A CD 1 ATOM 747 N NE . ARG A 1 97 ? 16.859 -12.675 11.788 1.00 139.54 ? 124 ARG A NE 1 ATOM 748 C CZ . ARG A 1 97 ? 16.459 -11.657 12.543 1.00 144.82 ? 124 ARG A CZ 1 ATOM 749 N NH1 . ARG A 1 97 ? 15.686 -11.873 13.600 1.00 148.27 ? 124 ARG A NH1 1 ATOM 750 N NH2 . ARG A 1 97 ? 16.825 -10.419 12.236 1.00 142.38 ? 124 ARG A NH2 1 ATOM 751 N N . GLU A 1 98 ? 12.692 -12.555 8.142 1.00 115.11 ? 125 GLU A N 1 ATOM 752 C CA . GLU A 1 98 ? 12.590 -11.923 6.835 1.00 116.98 ? 125 GLU A CA 1 ATOM 753 C C . GLU A 1 98 ? 13.954 -11.732 6.196 1.00 119.57 ? 125 GLU A C 1 ATOM 754 O O . GLU A 1 98 ? 14.082 -11.701 4.970 1.00 121.53 ? 125 GLU A O 1 ATOM 755 C CB . GLU A 1 98 ? 11.867 -10.578 6.912 1.00 121.90 ? 125 GLU A CB 1 ATOM 756 C CG . GLU A 1 98 ? 11.949 -9.872 8.252 1.00 129.98 ? 125 GLU A CG 1 ATOM 757 C CD . GLU A 1 98 ? 10.879 -10.355 9.207 1.00 132.80 ? 125 GLU A CD 1 ATOM 758 O OE1 . GLU A 1 98 ? 10.035 -9.536 9.625 1.00 131.70 ? 125 GLU A OE1 1 ATOM 759 O OE2 . GLU A 1 98 ? 10.884 -11.558 9.541 1.00 135.61 ? 125 GLU A OE2 1 ATOM 760 N N . ASP A 1 99 ? 14.989 -11.587 7.019 1.00 121.02 ? 126 ASP A N 1 ATOM 761 C CA . ASP A 1 99 ? 16.307 -11.411 6.421 1.00 129.12 ? 126 ASP A CA 1 ATOM 762 C C . ASP A 1 99 ? 16.997 -12.727 6.080 1.00 131.18 ? 126 ASP A C 1 ATOM 763 O O . ASP A 1 99 ? 18.129 -12.735 5.593 1.00 136.46 ? 126 ASP A O 1 ATOM 764 C CB . ASP A 1 99 ? 17.199 -10.598 7.372 1.00 135.84 ? 126 ASP A CB 1 ATOM 765 C CG . ASP A 1 99 ? 16.563 -10.403 8.760 1.00 139.35 ? 126 ASP A CG 1 ATOM 766 O OD1 . ASP A 1 99 ? 15.363 -10.731 8.942 1.00 140.98 ? 126 ASP A OD1 1 ATOM 767 O OD2 . ASP A 1 99 ? 17.252 -9.889 9.665 1.00 139.90 ? 126 ASP A OD2 1 ATOM 768 N N . GLN A 1 100 ? 16.313 -13.841 6.304 1.00 129.12 ? 127 GLN A N 1 ATOM 769 C CA . GLN A 1 100 ? 16.836 -15.136 5.896 1.00 128.44 ? 127 GLN A CA 1 ATOM 770 C C . GLN A 1 100 ? 15.742 -15.856 5.118 1.00 121.20 ? 127 GLN A C 1 ATOM 771 O O . GLN A 1 100 ? 15.774 -17.080 4.993 1.00 121.56 ? 127 GLN A O 1 ATOM 772 C CB . GLN A 1 100 ? 17.358 -15.984 7.068 1.00 137.05 ? 127 GLN A CB 1 ATOM 773 C CG . GLN A 1 100 ? 16.828 -15.708 8.445 1.00 143.93 ? 127 GLN A CG 1 ATOM 774 C CD . GLN A 1 100 ? 17.200 -16.820 9.410 1.00 146.90 ? 127 GLN A CD 1 ATOM 775 O OE1 . GLN A 1 100 ? 16.632 -17.909 9.358 1.00 146.96 ? 127 GLN A OE1 1 ATOM 776 N NE2 . GLN A 1 100 ? 18.180 -16.563 10.271 1.00 147.85 ? 127 GLN A NE2 1 ATOM 777 N N . ILE A 1 101 ? 14.769 -15.103 4.607 1.00 110.17 ? 128 ILE A N 1 ATOM 778 C CA . ILE A 1 101 ? 13.742 -15.696 3.760 1.00 100.61 ? 128 ILE A CA 1 ATOM 779 C C . ILE A 1 101 ? 14.396 -16.172 2.479 1.00 102.68 ? 128 ILE A C 1 ATOM 780 O O . ILE A 1 101 ? 15.152 -15.425 1.865 1.00 113.41 ? 128 ILE A O 1 ATOM 781 C CB . ILE A 1 101 ? 12.609 -14.692 3.435 1.00 93.88 ? 128 ILE A CB 1 ATOM 782 C CG1 . ILE A 1 101 ? 11.574 -14.650 4.566 1.00 83.85 ? 128 ILE A CG1 1 ATOM 783 C CG2 . ILE A 1 101 ? 11.915 -15.057 2.135 1.00 94.52 ? 128 ILE A CG2 1 ATOM 784 C CD1 . ILE A 1 101 ? 10.415 -13.705 4.296 1.00 78.16 ? 128 ILE A CD1 1 ATOM 785 N N . PRO A 1 102 ? 14.138 -17.434 2.083 1.00 94.64 ? 129 PRO A N 1 ATOM 786 C CA . PRO A 1 102 ? 14.783 -17.814 0.823 1.00 104.57 ? 129 PRO A CA 1 ATOM 787 C C . PRO A 1 102 ? 14.126 -17.205 -0.409 1.00 108.55 ? 129 PRO A C 1 ATOM 788 O O . PRO A 1 102 ? 12.948 -16.843 -0.371 1.00 101.15 ? 129 PRO A O 1 ATOM 789 C CB . PRO A 1 102 ? 14.624 -19.345 0.795 1.00 97.69 ? 129 PRO A CB 1 ATOM 790 C CG . PRO A 1 102 ? 13.991 -19.736 2.116 1.00 87.02 ? 129 PRO A CG 1 ATOM 791 C CD . PRO A 1 102 ? 13.305 -18.515 2.630 1.00 83.65 ? 129 PRO A CD 1 ATOM 792 N N . ARG A 1 103 ? 14.901 -17.066 -1.482 1.00 115.06 ? 130 ARG A N 1 ATOM 793 C CA . ARG A 1 103 ? 14.354 -16.840 -2.809 1.00 119.78 ? 130 ARG A CA 1 ATOM 794 C C . ARG A 1 103 ? 13.422 -17.983 -3.203 1.00 115.41 ? 130 ARG A C 1 ATOM 795 O O . ARG A 1 103 ? 13.838 -19.138 -3.219 1.00 116.05 ? 130 ARG A O 1 ATOM 796 C CB . ARG A 1 103 ? 15.481 -16.698 -3.835 1.00 129.81 ? 130 ARG A CB 1 ATOM 797 C CG . ARG A 1 103 ? 16.649 -15.869 -3.334 1.00 139.28 ? 130 ARG A CG 1 ATOM 798 C CD . ARG A 1 103 ? 16.421 -14.392 -3.577 1.00 146.04 ? 130 ARG A CD 1 ATOM 799 N NE . ARG A 1 103 ? 16.822 -14.009 -4.926 1.00 154.42 ? 130 ARG A NE 1 ATOM 800 C CZ . ARG A 1 103 ? 16.519 -12.847 -5.494 1.00 159.60 ? 130 ARG A CZ 1 ATOM 801 N NH1 . ARG A 1 103 ? 15.797 -11.950 -4.835 1.00 160.13 ? 130 ARG A NH1 1 ATOM 802 N NH2 . ARG A 1 103 ? 16.932 -12.584 -6.726 1.00 164.19 ? 130 ARG A NH2 1 ATOM 803 N N . GLY A 1 104 ? 12.183 -17.665 -3.542 1.00 107.36 ? 131 GLY A N 1 ATOM 804 C CA . GLY A 1 104 ? 11.232 -18.685 -3.931 1.00 109.40 ? 131 GLY A CA 1 ATOM 805 C C . GLY A 1 104 ? 10.128 -18.902 -2.919 1.00 107.11 ? 131 GLY A C 1 ATOM 806 O O . GLY A 1 104 ? 9.081 -19.471 -3.245 1.00 106.30 ? 131 GLY A O 1 ATOM 807 N N . PHE A 1 105 ? 10.360 -18.441 -1.690 1.00 99.75 ? 132 PHE A N 1 ATOM 808 C CA . PHE A 1 105 ? 9.375 -18.573 -0.623 1.00 86.48 ? 132 PHE A CA 1 ATOM 809 C C . PHE A 1 105 ? 8.120 -17.875 -1.105 1.00 91.00 ? 132 PHE A C 1 ATOM 810 O O . PHE A 1 105 ? 8.233 -16.833 -1.753 1.00 103.96 ? 132 PHE A O 1 ATOM 811 C CB . PHE A 1 105 ? 9.893 -17.985 0.687 1.00 84.83 ? 132 PHE A CB 1 ATOM 812 C CG . PHE A 1 105 ? 9.132 -18.456 1.899 1.00 84.65 ? 132 PHE A CG 1 ATOM 813 C CD1 . PHE A 1 105 ? 7.994 -17.788 2.326 1.00 85.73 ? 132 PHE A CD1 1 ATOM 814 C CD2 . PHE A 1 105 ? 9.552 -19.566 2.612 1.00 82.77 ? 132 PHE A CD2 1 ATOM 815 C CE1 . PHE A 1 105 ? 7.288 -18.223 3.436 1.00 81.99 ? 132 PHE A CE1 1 ATOM 816 C CE2 . PHE A 1 105 ? 8.861 -20.002 3.717 1.00 79.31 ? 132 PHE A CE2 1 ATOM 817 C CZ . PHE A 1 105 ? 7.725 -19.335 4.132 1.00 79.19 ? 132 PHE A CZ 1 ATOM 818 N N . PRO A 1 106 ? 6.935 -18.455 -0.862 1.00 84.97 ? 133 PRO A N 1 ATOM 819 C CA . PRO A 1 106 ? 5.764 -17.796 -1.448 1.00 85.40 ? 133 PRO A CA 1 ATOM 820 C C . PRO A 1 106 ? 5.589 -16.340 -1.018 1.00 89.48 ? 133 PRO A C 1 ATOM 821 O O . PRO A 1 106 ? 5.849 -15.993 0.129 1.00 91.53 ? 133 PRO A O 1 ATOM 822 C CB . PRO A 1 106 ? 4.598 -18.645 -0.932 1.00 82.43 ? 133 PRO A CB 1 ATOM 823 C CG . PRO A 1 106 ? 5.187 -19.984 -0.647 1.00 77.49 ? 133 PRO A CG 1 ATOM 824 C CD . PRO A 1 106 ? 6.599 -19.726 -0.201 1.00 83.16 ? 133 PRO A CD 1 ATOM 825 N N . THR A 1 107 ? 5.125 -15.521 -1.959 1.00 90.36 ? 134 THR A N 1 ATOM 826 C CA . THR A 1 107 ? 4.769 -14.124 -1.723 1.00 90.19 ? 134 THR A CA 1 ATOM 827 C C . THR A 1 107 ? 3.278 -13.944 -2.030 1.00 85.40 ? 134 THR A C 1 ATOM 828 O O . THR A 1 107 ? 2.747 -14.637 -2.893 1.00 81.93 ? 134 THR A O 1 ATOM 829 C CB . THR A 1 107 ? 5.634 -13.160 -2.567 1.00 94.18 ? 134 THR A CB 1 ATOM 830 O OG1 . THR A 1 107 ? 4.893 -11.967 -2.853 1.00 102.93 ? 134 THR A OG1 1 ATOM 831 C CG2 . THR A 1 107 ? 6.038 -13.815 -3.883 1.00 93.84 ? 134 THR A CG2 1 ATOM 832 N N . ILE A 1 108 ? 2.603 -13.035 -1.330 1.00 84.68 ? 135 ILE A N 1 ATOM 833 C CA . ILE A 1 108 ? 1.267 -12.622 -1.750 1.00 85.28 ? 135 ILE A CA 1 ATOM 834 C C . ILE A 1 108 ? 1.273 -11.353 -2.604 1.00 90.58 ? 135 ILE A C 1 ATOM 835 O O . ILE A 1 108 ? 1.384 -10.242 -2.085 1.00 96.05 ? 135 ILE A O 1 ATOM 836 C CB . ILE A 1 108 ? 0.346 -12.395 -0.528 1.00 87.05 ? 135 ILE A CB 1 ATOM 837 C CG1 . ILE A 1 108 ? 0.199 -13.684 0.274 1.00 89.16 ? 135 ILE A CG1 1 ATOM 838 C CG2 . ILE A 1 108 ? -1.022 -11.891 -0.960 1.00 84.49 ? 135 ILE A CG2 1 ATOM 839 C CD1 . ILE A 1 108 ? -0.496 -14.803 -0.485 1.00 86.84 ? 135 ILE A CD1 1 ATOM 840 N N . ASP A 1 109 ? 1.138 -11.533 -3.917 1.00 94.88 ? 136 ASP A N 1 ATOM 841 C CA . ASP A 1 109 ? 1.198 -10.431 -4.871 1.00 103.35 ? 136 ASP A CA 1 ATOM 842 C C . ASP A 1 109 ? -0.043 -9.563 -4.763 1.00 109.44 ? 136 ASP A C 1 ATOM 843 O O . ASP A 1 109 ? 0.037 -8.334 -4.806 1.00 109.58 ? 136 ASP A O 1 ATOM 844 C CB . ASP A 1 109 ? 1.341 -10.964 -6.297 1.00 105.78 ? 136 ASP A CB 1 ATOM 845 C CG . ASP A 1 109 ? 2.431 -12.006 -6.415 1.00 108.15 ? 136 ASP A CG 1 ATOM 846 O OD1 . ASP A 1 109 ? 3.259 -11.914 -7.349 1.00 108.38 ? 136 ASP A OD1 1 ATOM 847 O OD2 . ASP A 1 109 ? 2.456 -12.923 -5.567 1.00 110.03 ? 136 ASP A OD2 1 ATOM 848 N N . MET A 1 110 ? -1.194 -10.207 -4.619 1.00 116.51 ? 137 MET A N 1 ATOM 849 C CA . MET A 1 110 ? -2.424 -9.471 -4.375 1.00 116.35 ? 137 MET A CA 1 ATOM 850 C C . MET A 1 110 ? -3.273 -10.349 -3.486 1.00 111.29 ? 137 MET A C 1 ATOM 851 O O . MET A 1 110 ? -3.238 -11.565 -3.595 1.00 112.78 ? 137 MET A O 1 ATOM 852 C CB . MET A 1 110 ? -3.150 -9.138 -5.692 1.00 122.11 ? 137 MET A CB 1 ATOM 853 C CG . MET A 1 110 ? -4.418 -8.331 -5.510 1.00 127.29 ? 137 MET A CG 1 ATOM 854 S SD . MET A 1 110 ? -4.420 -6.793 -6.449 1.00 162.46 ? 137 MET A SD 1 ATOM 855 C CE . MET A 1 110 ? -6.041 -6.149 -6.033 1.00 153.29 ? 137 MET A CE 1 ATOM 856 N N . GLY A 1 111 ? -4.038 -9.733 -2.599 1.00 102.60 ? 138 GLY A N 1 ATOM 857 C CA . GLY A 1 111 ? -4.786 -10.490 -1.618 1.00 89.02 ? 138 GLY A CA 1 ATOM 858 C C . GLY A 1 111 ? -6.265 -10.171 -1.688 1.00 77.02 ? 138 GLY A C 1 ATOM 859 O O . GLY A 1 111 ? -6.689 -9.247 -2.379 1.00 77.75 ? 138 GLY A O 1 ATOM 860 N N . PRO A 1 112 ? -7.066 -10.967 -0.971 1.00 73.84 ? 139 PRO A N 1 ATOM 861 C CA . PRO A 1 112 ? -8.518 -10.805 -1.030 1.00 75.29 ? 139 PRO A CA 1 ATOM 862 C C . PRO A 1 112 ? -8.876 -9.453 -0.474 1.00 77.64 ? 139 PRO A C 1 ATOM 863 O O . PRO A 1 112 ? -8.107 -8.862 0.293 1.00 71.42 ? 139 PRO A O 1 ATOM 864 C CB . PRO A 1 112 ? -9.041 -11.936 -0.141 1.00 71.84 ? 139 PRO A CB 1 ATOM 865 C CG . PRO A 1 112 ? -7.927 -12.190 0.812 1.00 75.26 ? 139 PRO A CG 1 ATOM 866 C CD . PRO A 1 112 ? -6.660 -11.977 0.025 1.00 74.54 ? 139 PRO A CD 1 ATOM 867 N N . GLN A 1 113 ? -10.026 -8.942 -0.879 1.00 80.03 ? 140 GLN A N 1 ATOM 868 C CA . GLN A 1 113 ? -10.404 -7.604 -0.501 1.00 81.00 ? 140 GLN A CA 1 ATOM 869 C C . GLN A 1 113 ? -11.760 -7.648 0.147 1.00 78.41 ? 140 GLN A C 1 ATOM 870 O O . GLN A 1 113 ? -12.540 -8.578 -0.074 1.00 79.62 ? 140 GLN A O 1 ATOM 871 C CB . GLN A 1 113 ? -10.456 -6.688 -1.725 1.00 88.96 ? 140 GLN A CB 1 ATOM 872 C CG . GLN A 1 113 ? -9.229 -6.750 -2.609 1.00 93.79 ? 140 GLN A CG 1 ATOM 873 C CD . GLN A 1 113 ? -8.108 -5.871 -2.102 1.00 96.39 ? 140 GLN A CD 1 ATOM 874 O OE1 . GLN A 1 113 ? -8.304 -4.683 -1.843 1.00 98.49 ? 140 GLN A OE1 1 ATOM 875 N NE2 . GLN A 1 113 ? -6.921 -6.450 -1.959 1.00 100.13 ? 140 GLN A NE2 1 ATOM 876 N N . LEU A 1 114 ? -11.996 -6.650 0.992 1.00 73.82 ? 141 LEU A N 1 ATOM 877 C CA . LEU A 1 114 ? -13.319 -6.366 1.506 1.00 69.68 ? 141 LEU A CA 1 ATOM 878 C C . LEU A 1 114 ? -14.299 -6.577 0.371 1.00 61.71 ? 141 LEU A C 1 ATOM 879 O O . LEU A 1 114 ? -14.086 -6.099 -0.743 1.00 65.57 ? 141 LEU A O 1 ATOM 880 C CB . LEU A 1 114 ? -13.400 -4.949 2.064 1.00 74.16 ? 141 LEU A CB 1 ATOM 881 C CG . LEU A 1 114 ? -14.564 -4.711 3.028 1.00 80.38 ? 141 LEU A CG 1 ATOM 882 C CD1 . LEU A 1 114 ? -14.166 -3.776 4.166 1.00 87.84 ? 141 LEU A CD1 1 ATOM 883 C CD2 . LEU A 1 114 ? -15.769 -4.167 2.283 1.00 80.63 ? 141 LEU A CD2 1 ATOM 884 N N . LYS A 1 115 ? -15.365 -7.310 0.646 1.00 59.21 ? 142 LYS A N 1 ATOM 885 C CA . LYS A 1 115 ? -16.359 -7.519 -0.386 1.00 61.88 ? 142 LYS A CA 1 ATOM 886 C C . LYS A 1 115 ? -17.735 -7.514 0.250 1.00 64.11 ? 142 LYS A C 1 ATOM 887 O O . LYS A 1 115 ? -17.948 -8.067 1.326 1.00 70.71 ? 142 LYS A O 1 ATOM 888 C CB . LYS A 1 115 ? -16.100 -8.835 -1.124 1.00 75.04 ? 142 LYS A CB 1 ATOM 889 C CG . LYS A 1 115 ? -17.146 -9.198 -2.168 1.00 92.27 ? 142 LYS A CG 1 ATOM 890 C CD . LYS A 1 115 ? -17.278 -8.136 -3.251 1.00 100.70 ? 142 LYS A CD 1 ATOM 891 C CE . LYS A 1 115 ? -18.346 -8.524 -4.268 1.00 101.73 ? 142 LYS A CE 1 ATOM 892 N NZ . LYS A 1 115 ? -18.742 -7.373 -5.128 1.00 103.09 ? 142 LYS A NZ 1 ATOM 893 N N . VAL A 1 116 ? -18.667 -6.878 -0.445 1.00 62.26 ? 143 VAL A N 1 ATOM 894 C CA . VAL A 1 116 ? -20.060 -6.918 -0.060 1.00 62.37 ? 143 VAL A CA 1 ATOM 895 C C . VAL A 1 116 ? -20.929 -7.607 -1.090 1.00 72.51 ? 143 VAL A C 1 ATOM 896 O O . VAL A 1 116 ? -20.955 -7.214 -2.256 1.00 77.41 ? 143 VAL A O 1 ATOM 897 C CB . VAL A 1 116 ? -20.592 -5.482 0.143 1.00 54.45 ? 143 VAL A CB 1 ATOM 898 C CG1 . VAL A 1 116 ? -22.021 -5.506 0.650 1.00 54.08 ? 143 VAL A CG1 1 ATOM 899 C CG2 . VAL A 1 116 ? -19.686 -4.705 1.085 1.00 55.00 ? 143 VAL A CG2 1 ATOM 900 N N . VAL A 1 117 ? -21.628 -8.652 -0.659 1.00 75.83 ? 144 VAL A N 1 ATOM 901 C CA . VAL A 1 117 ? -22.467 -9.402 -1.575 1.00 78.50 ? 144 VAL A CA 1 ATOM 902 C C . VAL A 1 117 ? -23.909 -9.371 -1.057 1.00 73.43 ? 144 VAL A C 1 ATOM 903 O O . VAL A 1 117 ? -24.149 -9.356 0.156 1.00 75.57 ? 144 VAL A O 1 ATOM 904 C CB . VAL A 1 117 ? -21.958 -10.858 -1.747 1.00 59.35 ? 144 VAL A CB 1 ATOM 905 C CG1 . VAL A 1 117 ? -22.338 -11.726 -0.555 1.00 55.37 ? 144 VAL A CG1 1 ATOM 906 C CG2 . VAL A 1 117 ? -22.481 -11.455 -3.034 1.00 70.27 ? 144 VAL A CG2 1 ATOM 907 N N . GLU A 1 118 ? -24.864 -9.313 -1.980 1.00 72.04 ? 145 GLU A N 1 ATOM 908 C CA . GLU A 1 118 ? -26.271 -9.430 -1.626 1.00 73.57 ? 145 GLU A CA 1 ATOM 909 C C . GLU A 1 118 ? -26.599 -10.890 -1.333 1.00 76.26 ? 145 GLU A C 1 ATOM 910 O O . GLU A 1 118 ? -26.075 -11.775 -2.009 1.00 81.50 ? 145 GLU A O 1 ATOM 911 C CB . GLU A 1 118 ? -27.162 -8.869 -2.742 1.00 76.39 ? 145 GLU A CB 1 ATOM 912 C CG . GLU A 1 118 ? -27.276 -7.351 -2.722 1.00 76.69 ? 145 GLU A CG 1 ATOM 913 C CD . GLU A 1 118 ? -27.486 -6.740 -4.095 1.00 76.53 ? 145 GLU A CD 1 ATOM 914 O OE1 . GLU A 1 118 ? -28.287 -7.285 -4.882 1.00 83.35 ? 145 GLU A OE1 1 ATOM 915 O OE2 . GLU A 1 118 ? -26.836 -5.715 -4.391 1.00 65.85 ? 145 GLU A OE2 1 ATOM 916 N N . ARG A 1 119 ? -27.412 -11.143 -0.308 1.00 66.76 ? 146 ARG A N 1 ATOM 917 C CA . ARG A 1 119 ? -27.826 -12.507 0.020 1.00 62.85 ? 146 ARG A CA 1 ATOM 918 C C . ARG A 1 119 ? -28.325 -13.237 -1.224 1.00 68.83 ? 146 ARG A C 1 ATOM 919 O O . ARG A 1 119 ? -29.005 -12.639 -2.059 1.00 74.02 ? 146 ARG A O 1 ATOM 920 C CB . ARG A 1 119 ? -28.918 -12.503 1.095 1.00 69.91 ? 146 ARG A CB 1 ATOM 921 C CG . ARG A 1 119 ? -29.504 -13.885 1.388 1.00 78.06 ? 146 ARG A CG 1 ATOM 922 C CD . ARG A 1 119 ? -30.696 -13.802 2.322 1.00 80.88 ? 146 ARG A CD 1 ATOM 923 N NE . ARG A 1 119 ? -31.716 -12.889 1.814 1.00 85.10 ? 146 ARG A NE 1 ATOM 924 C CZ . ARG A 1 119 ? -32.691 -13.244 0.985 1.00 90.50 ? 146 ARG A CZ 1 ATOM 925 N NH1 . ARG A 1 119 ? -32.782 -14.500 0.567 1.00 86.04 ? 146 ARG A NH1 1 ATOM 926 N NH2 . ARG A 1 119 ? -33.574 -12.343 0.575 1.00 92.86 ? 146 ARG A NH2 1 ATOM 927 N N . THR A 1 120 ? -27.903 -14.494 -1.366 1.00 80.16 ? 147 THR A N 1 ATOM 928 C CA . THR A 1 120 ? -28.249 -15.379 -2.491 1.00 84.16 ? 147 THR A CA 1 ATOM 929 C C . THR A 1 120 ? -27.372 -15.127 -3.729 1.00 88.79 ? 147 THR A C 1 ATOM 930 O O . THR A 1 120 ? -27.309 -15.972 -4.624 1.00 100.10 ? 147 THR A O 1 ATOM 931 C CB . THR A 1 120 ? -29.779 -15.285 -2.848 1.00 107.93 ? 147 THR A CB 1 ATOM 932 O OG1 . THR A 1 120 ? -30.407 -16.551 -2.607 1.00 117.63 ? 147 THR A OG1 1 ATOM 933 C CG2 . THR A 1 120 ? -30.023 -14.853 -4.298 1.00 103.81 ? 147 THR A CG2 1 ATOM 934 N N . ARG A 1 121 ? -26.628 -14.020 -3.745 1.00 83.74 ? 148 ARG A N 1 ATOM 935 C CA . ARG A 1 121 ? -25.693 -13.781 -4.844 1.00 86.58 ? 148 ARG A CA 1 ATOM 936 C C . ARG A 1 121 ? -24.347 -14.449 -4.601 1.00 81.72 ? 148 ARG A C 1 ATOM 937 O O . ARG A 1 121 ? -24.026 -14.816 -3.474 1.00 80.57 ? 148 ARG A O 1 ATOM 938 C CB . ARG A 1 121 ? -25.478 -12.278 -5.044 1.00 98.89 ? 148 ARG A CB 1 ATOM 939 C CG . ARG A 1 121 ? -26.724 -11.507 -5.427 1.00 113.01 ? 148 ARG A CG 1 ATOM 940 C CD . ARG A 1 121 ? -26.897 -11.464 -6.939 1.00 121.82 ? 148 ARG A CD 1 ATOM 941 N NE . ARG A 1 121 ? -28.140 -10.805 -7.335 1.00 125.48 ? 148 ARG A NE 1 ATOM 942 C CZ . ARG A 1 121 ? -28.244 -9.515 -7.649 1.00 128.12 ? 148 ARG A CZ 1 ATOM 943 N NH1 . ARG A 1 121 ? -27.175 -8.732 -7.621 1.00 128.26 ? 148 ARG A NH1 1 ATOM 944 N NH2 . ARG A 1 121 ? -29.421 -9.008 -7.994 1.00 128.14 ? 148 ARG A NH2 1 ATOM 945 N N . THR A 1 122 ? -23.563 -14.592 -5.667 1.00 72.55 ? 149 THR A N 1 ATOM 946 C CA . THR A 1 122 ? -22.250 -15.215 -5.585 1.00 71.54 ? 149 THR A CA 1 ATOM 947 C C . THR A 1 122 ? -21.215 -14.203 -5.100 1.00 68.85 ? 149 THR A C 1 ATOM 948 O O . THR A 1 122 ? -21.180 -13.069 -5.578 1.00 72.67 ? 149 THR A O 1 ATOM 949 C CB . THR A 1 122 ? -21.843 -15.810 -6.936 1.00 81.97 ? 149 THR A CB 1 ATOM 950 O OG1 . THR A 1 122 ? -22.809 -16.795 -7.330 1.00 87.19 ? 149 THR A OG1 1 ATOM 951 C CG2 . THR A 1 122 ? -20.474 -16.456 -6.840 1.00 88.11 ? 149 THR A CG2 1 ATOM 952 N N . ALA A 1 123 ? -20.370 -14.615 -4.158 1.00 66.86 ? 150 ALA A N 1 ATOM 953 C CA . ALA A 1 123 ? -19.210 -13.820 -3.743 1.00 67.16 ? 150 ALA A CA 1 ATOM 954 C C . ALA A 1 123 ? -17.889 -14.506 -4.095 1.00 69.87 ? 150 ALA A C 1 ATOM 955 O O . ALA A 1 123 ? -17.703 -15.670 -3.784 1.00 67.13 ? 150 ALA A O 1 ATOM 956 C CB . ALA A 1 123 ? -19.272 -13.531 -2.258 1.00 63.87 ? 150 ALA A CB 1 ATOM 957 N N . THR A 1 124 ? -16.957 -13.781 -4.704 1.00 72.63 ? 151 THR A N 1 ATOM 958 C CA . THR A 1 124 ? -15.666 -14.387 -4.992 1.00 70.14 ? 151 THR A CA 1 ATOM 959 C C . THR A 1 124 ? -14.533 -13.641 -4.305 1.00 69.61 ? 151 THR A C 1 ATOM 960 O O . THR A 1 124 ? -14.274 -12.464 -4.575 1.00 69.40 ? 151 THR A O 1 ATOM 961 C CB . THR A 1 124 ? -15.377 -14.440 -6.498 1.00 71.98 ? 151 THR A CB 1 ATOM 962 O OG1 . THR A 1 124 ? -16.450 -15.105 -7.170 1.00 80.59 ? 151 THR A OG1 1 ATOM 963 C CG2 . THR A 1 124 ? -14.079 -15.181 -6.775 1.00 68.00 ? 151 THR A CG2 1 ATOM 964 N N . MET A 1 125 ? -13.834 -14.361 -3.434 1.00 68.90 ? 152 MET A N 1 ATOM 965 C CA . MET A 1 125 ? -12.632 -13.837 -2.815 1.00 76.98 ? 152 MET A CA 1 ATOM 966 C C . MET A 1 125 ? -11.477 -14.229 -3.701 1.00 81.74 ? 152 MET A C 1 ATOM 967 O O . MET A 1 125 ? -11.451 -15.328 -4.250 1.00 87.51 ? 152 MET A O 1 ATOM 968 C CB . MET A 1 125 ? -12.458 -14.377 -1.396 1.00 76.25 ? 152 MET A CB 1 ATOM 969 C CG . MET A 1 125 ? -13.657 -14.153 -0.485 1.00 69.08 ? 152 MET A CG 1 ATOM 970 S SD . MET A 1 125 ? -14.136 -12.414 -0.341 1.00 106.69 ? 152 MET A SD 1 ATOM 971 C CE . MET A 1 125 ? -12.762 -11.747 0.591 1.00 68.65 ? 152 MET A CE 1 ATOM 972 N N . LEU A 1 126 ? -10.524 -13.325 -3.857 1.00 79.31 ? 153 LEU A N 1 ATOM 973 C CA . LEU A 1 126 ? -9.455 -13.538 -4.820 1.00 77.34 ? 153 LEU A CA 1 ATOM 974 C C . LEU A 1 126 ? -8.070 -13.475 -4.203 1.00 84.33 ? 153 LEU A C 1 ATOM 975 O O . LEU A 1 126 ? -7.863 -12.833 -3.183 1.00 94.17 ? 153 LEU A O 1 ATOM 976 C CB . LEU A 1 126 ? -9.550 -12.490 -5.930 1.00 72.60 ? 153 LEU A CB 1 ATOM 977 C CG . LEU A 1 126 ? -10.378 -12.828 -7.164 1.00 84.05 ? 153 LEU A CG 1 ATOM 978 C CD1 . LEU A 1 126 ? -10.668 -11.575 -7.983 1.00 91.99 ? 153 LEU A CD1 1 ATOM 979 C CD2 . LEU A 1 126 ? -9.672 -13.876 -8.022 1.00 90.02 ? 153 LEU A CD2 1 ATOM 980 N N . CYS A 1 127 ? -7.131 -14.186 -4.804 1.00 90.68 ? 154 CYS A N 1 ATOM 981 C CA . CYS A 1 127 ? -5.808 -14.173 -4.245 1.00 98.31 ? 154 CYS A CA 1 ATOM 982 C C . CYS A 1 127 ? -4.854 -14.396 -5.388 1.00 101.02 ? 154 CYS A C 1 ATOM 983 O O . CYS A 1 127 ? -5.071 -15.249 -6.215 1.00 106.57 ? 154 CYS A O 1 ATOM 984 C CB . CYS A 1 127 ? -5.699 -15.285 -3.199 1.00 101.73 ? 154 CYS A CB 1 ATOM 985 S SG . CYS A 1 127 ? -4.080 -15.658 -2.490 1.00 84.41 ? 154 CYS A SG 1 ATOM 986 N N . ALA A 1 128 ? -3.739 -13.692 -5.371 1.00 100.27 ? 155 ALA A N 1 ATOM 987 C CA . ALA A 1 128 ? -2.705 -13.895 -6.347 1.00 101.31 ? 155 ALA A CA 1 ATOM 988 C C . ALA A 1 128 ? -1.464 -14.108 -5.542 1.00 99.72 ? 155 ALA A C 1 ATOM 989 O O . ALA A 1 128 ? -1.059 -13.220 -4.767 1.00 100.92 ? 155 ALA A O 1 ATOM 990 C CB . ALA A 1 128 ? -2.579 -12.700 -7.278 1.00 107.70 ? 155 ALA A CB 1 ATOM 991 N N . ALA A 1 129 ? -0.818 -15.232 -5.786 1.00 98.51 ? 156 ALA A N 1 ATOM 992 C CA . ALA A 1 129 ? 0.340 -15.621 -5.019 1.00 100.08 ? 156 ALA A CA 1 ATOM 993 C C . ALA A 1 129 ? 1.385 -16.177 -5.951 1.00 106.15 ? 156 ALA A C 1 ATOM 994 O O . ALA A 1 129 ? 1.064 -16.805 -6.938 1.00 110.21 ? 156 ALA A O 1 ATOM 995 C CB . ALA A 1 129 ? -0.045 -16.645 -3.962 1.00 96.24 ? 156 ALA A CB 1 ATOM 996 N N . SER A 1 130 ? 2.646 -16.015 -5.607 1.00 105.50 ? 157 SER A N 1 ATOM 997 C CA . SER A 1 130 ? 3.686 -16.554 -6.453 1.00 106.23 ? 157 SER A CA 1 ATOM 998 C C . SER A 1 130 ? 4.792 -17.117 -5.588 1.00 112.20 ? 157 SER A C 1 ATOM 999 O O . SER A 1 130 ? 4.817 -16.904 -4.373 1.00 112.77 ? 157 SER A O 1 ATOM 1000 C CB . SER A 1 130 ? 4.233 -15.503 -7.419 1.00 106.11 ? 157 SER A CB 1 ATOM 1001 O OG . SER A 1 130 ? 4.465 -14.284 -6.740 1.00 105.61 ? 157 SER A OG 1 ATOM 1002 N N . GLY A 1 131 ? 5.719 -17.829 -6.210 1.00 117.41 ? 158 GLY A N 1 ATOM 1003 C CA . GLY A 1 131 ? 6.804 -18.436 -5.481 1.00 115.57 ? 158 GLY A CA 1 ATOM 1004 C C . GLY A 1 131 ? 7.540 -19.422 -6.354 1.00 111.56 ? 158 GLY A C 1 ATOM 1005 O O . GLY A 1 131 ? 7.179 -19.648 -7.513 1.00 107.74 ? 158 GLY A O 1 ATOM 1006 N N . ASN A 1 132 ? 8.583 -20.013 -5.784 1.00 112.49 ? 159 ASN A N 1 ATOM 1007 C CA . ASN A 1 132 ? 9.342 -21.048 -6.469 1.00 114.01 ? 159 ASN A CA 1 ATOM 1008 C C . ASN A 1 132 ? 9.720 -22.193 -5.526 1.00 102.86 ? 159 ASN A C 1 ATOM 1009 O O . ASN A 1 132 ? 10.529 -22.013 -4.618 1.00 102.81 ? 159 ASN A O 1 ATOM 1010 C CB . ASN A 1 132 ? 10.597 -20.442 -7.104 1.00 118.31 ? 159 ASN A CB 1 ATOM 1011 C CG . ASN A 1 132 ? 11.300 -21.412 -8.034 1.00 115.06 ? 159 ASN A CG 1 ATOM 1012 O OD1 . ASN A 1 132 ? 10.717 -22.399 -8.485 1.00 113.26 ? 159 ASN A OD1 1 ATOM 1013 N ND2 . ASN A 1 132 ? 12.563 -21.130 -8.329 1.00 117.33 ? 159 ASN A ND2 1 ATOM 1014 N N . PRO A 1 133 ? 9.147 -23.388 -5.752 1.00 95.62 ? 160 PRO A N 1 ATOM 1015 C CA . PRO A 1 133 ? 8.167 -23.748 -6.788 1.00 100.20 ? 160 PRO A CA 1 ATOM 1016 C C . PRO A 1 133 ? 6.830 -23.023 -6.717 1.00 103.71 ? 160 PRO A C 1 ATOM 1017 O O . PRO A 1 133 ? 6.498 -22.449 -5.680 1.00 102.47 ? 160 PRO A O 1 ATOM 1018 C CB . PRO A 1 133 ? 7.968 -25.247 -6.567 1.00 92.97 ? 160 PRO A CB 1 ATOM 1019 C CG . PRO A 1 133 ? 8.200 -25.424 -5.118 1.00 85.26 ? 160 PRO A CG 1 ATOM 1020 C CD . PRO A 1 133 ? 9.328 -24.491 -4.789 1.00 88.99 ? 160 PRO A CD 1 ATOM 1021 N N . ASP A 1 134 ? 6.091 -23.043 -7.819 1.00 105.20 ? 161 ASP A N 1 ATOM 1022 C CA . ASP A 1 134 ? 4.751 -22.480 -7.856 1.00 104.69 ? 161 ASP A CA 1 ATOM 1023 C C . ASP A 1 134 ? 3.925 -23.143 -6.741 1.00 99.86 ? 161 ASP A C 1 ATOM 1024 O O . ASP A 1 134 ? 3.762 -24.365 -6.737 1.00 100.78 ? 161 ASP A O 1 ATOM 1025 C CB . ASP A 1 134 ? 4.130 -22.663 -9.238 1.00 109.49 ? 161 ASP A CB 1 ATOM 1026 C CG . ASP A 1 134 ? 4.841 -21.848 -10.309 1.00 116.70 ? 161 ASP A CG 1 ATOM 1027 O OD1 . ASP A 1 134 ? 4.743 -20.601 -10.282 1.00 114.53 ? 161 ASP A OD1 1 ATOM 1028 O OD2 . ASP A 1 134 ? 5.508 -22.449 -11.179 1.00 123.28 ? 161 ASP A OD2 1 ATOM 1029 N N . PRO A 1 135 ? 3.429 -22.345 -5.778 1.00 91.39 ? 162 PRO A N 1 ATOM 1030 C CA . PRO A 1 135 ? 2.723 -22.813 -4.572 1.00 94.22 ? 162 PRO A CA 1 ATOM 1031 C C . PRO A 1 135 ? 1.244 -23.191 -4.735 1.00 98.72 ? 162 PRO A C 1 ATOM 1032 O O . PRO A 1 135 ? 0.560 -22.671 -5.609 1.00 101.82 ? 162 PRO A O 1 ATOM 1033 C CB . PRO A 1 135 ? 2.837 -21.606 -3.641 1.00 92.80 ? 162 PRO A CB 1 ATOM 1034 C CG . PRO A 1 135 ? 2.808 -20.444 -4.569 1.00 89.87 ? 162 PRO A CG 1 ATOM 1035 C CD . PRO A 1 135 ? 3.557 -20.875 -5.800 1.00 89.97 ? 162 PRO A CD 1 ATOM 1036 N N . GLU A 1 136 ? 0.764 -24.077 -3.860 1.00 102.78 ? 163 GLU A N 1 ATOM 1037 C CA . GLU A 1 136 ? -0.671 -24.324 -3.710 1.00 105.18 ? 163 GLU A CA 1 ATOM 1038 C C . GLU A 1 136 ? -1.336 -23.286 -2.802 1.00 99.95 ? 163 GLU A C 1 ATOM 1039 O O . GLU A 1 136 ? -0.752 -22.854 -1.810 1.00 99.01 ? 163 GLU A O 1 ATOM 1040 C CB . GLU A 1 136 ? -0.916 -25.741 -3.204 1.00 110.73 ? 163 GLU A CB 1 ATOM 1041 C CG . GLU A 1 136 ? -0.695 -26.792 -4.285 1.00 125.04 ? 163 GLU A CG 1 ATOM 1042 C CD . GLU A 1 136 ? -0.021 -28.040 -3.759 1.00 135.55 ? 163 GLU A CD 1 ATOM 1043 O OE1 . GLU A 1 136 ? 0.984 -28.472 -4.364 1.00 138.17 ? 163 GLU A OE1 1 ATOM 1044 O OE2 . GLU A 1 136 ? -0.499 -28.584 -2.742 1.00 137.10 ? 163 GLU A OE2 1 ATOM 1045 N N . ILE A 1 137 ? -2.539 -22.865 -3.182 1.00 92.13 ? 164 ILE A N 1 ATOM 1046 C CA . ILE A 1 137 ? -3.346 -21.934 -2.395 1.00 84.03 ? 164 ILE A CA 1 ATOM 1047 C C . ILE A 1 137 ? -4.519 -22.597 -1.663 1.00 83.38 ? 164 ILE A C 1 ATOM 1048 O O . ILE A 1 137 ? -5.347 -23.279 -2.271 1.00 82.85 ? 164 ILE A O 1 ATOM 1049 C CB . ILE A 1 137 ? -3.865 -20.799 -3.278 1.00 79.95 ? 164 ILE A CB 1 ATOM 1050 C CG1 . ILE A 1 137 ? -2.681 -20.007 -3.830 1.00 80.11 ? 164 ILE A CG1 1 ATOM 1051 C CG2 . ILE A 1 137 ? -4.795 -19.895 -2.491 1.00 81.60 ? 164 ILE A CG2 1 ATOM 1052 C CD1 . ILE A 1 137 ? -3.061 -18.841 -4.709 1.00 85.87 ? 164 ILE A CD1 1 ATOM 1053 N N . THR A 1 138 ? -4.579 -22.373 -0.352 1.00 85.68 ? 165 THR A N 1 ATOM 1054 C CA . THR A 1 138 ? -5.714 -22.786 0.486 1.00 83.92 ? 165 THR A CA 1 ATOM 1055 C C . THR A 1 138 ? -6.311 -21.607 1.248 1.00 77.77 ? 165 THR A C 1 ATOM 1056 O O . THR A 1 138 ? -5.720 -20.528 1.281 1.00 78.96 ? 165 THR A O 1 ATOM 1057 C CB . THR A 1 138 ? -5.293 -23.870 1.495 1.00 90.75 ? 165 THR A CB 1 ATOM 1058 O OG1 . THR A 1 138 ? -4.469 -23.283 2.510 1.00 91.54 ? 165 THR A OG1 1 ATOM 1059 C CG2 . THR A 1 138 ? -4.523 -24.978 0.800 1.00 95.05 ? 165 THR A CG2 1 ATOM 1060 N N . TRP A 1 139 ? -7.487 -21.797 1.838 1.00 71.80 ? 166 TRP A N 1 ATOM 1061 C CA . TRP A 1 139 ? -8.218 -20.694 2.451 1.00 66.76 ? 166 TRP A CA 1 ATOM 1062 C C . TRP A 1 139 ? -8.693 -20.930 3.890 1.00 62.22 ? 166 TRP A C 1 ATOM 1063 O O . TRP A 1 139 ? -9.169 -22.008 4.230 1.00 66.34 ? 166 TRP A O 1 ATOM 1064 C CB . TRP A 1 139 ? -9.442 -20.363 1.610 1.00 61.07 ? 166 TRP A CB 1 ATOM 1065 C CG . TRP A 1 139 ? -9.163 -19.716 0.300 1.00 67.83 ? 166 TRP A CG 1 ATOM 1066 C CD1 . TRP A 1 139 ? -8.864 -20.336 -0.876 1.00 74.84 ? 166 TRP A CD1 1 ATOM 1067 C CD2 . TRP A 1 139 ? -9.181 -18.314 0.022 1.00 69.23 ? 166 TRP A CD2 1 ATOM 1068 N NE1 . TRP A 1 139 ? -8.682 -19.405 -1.870 1.00 75.61 ? 166 TRP A NE1 1 ATOM 1069 C CE2 . TRP A 1 139 ? -8.872 -18.155 -1.342 1.00 74.48 ? 166 TRP A CE2 1 ATOM 1070 C CE3 . TRP A 1 139 ? -9.422 -17.177 0.797 1.00 67.10 ? 166 TRP A CE3 1 ATOM 1071 C CZ2 . TRP A 1 139 ? -8.797 -16.904 -1.948 1.00 74.84 ? 166 TRP A CZ2 1 ATOM 1072 C CZ3 . TRP A 1 139 ? -9.348 -15.936 0.195 1.00 69.68 ? 166 TRP A CZ3 1 ATOM 1073 C CH2 . TRP A 1 139 ? -9.038 -15.809 -1.164 1.00 72.68 ? 166 TRP A CH2 1 ATOM 1074 N N . PHE A 1 140 ? -8.581 -19.889 4.714 1.00 54.91 ? 167 PHE A N 1 ATOM 1075 C CA . PHE A 1 140 ? -9.110 -19.946 6.072 1.00 52.78 ? 167 PHE A CA 1 ATOM 1076 C C . PHE A 1 140 ? -10.186 -18.885 6.235 1.00 57.50 ? 167 PHE A C 1 ATOM 1077 O O . PHE A 1 140 ? -10.106 -17.811 5.637 1.00 57.23 ? 167 PHE A O 1 ATOM 1078 C CB . PHE A 1 140 ? -8.010 -19.728 7.113 1.00 60.86 ? 167 PHE A CB 1 ATOM 1079 C CG . PHE A 1 140 ? -7.112 -20.907 7.316 1.00 70.55 ? 167 PHE A CG 1 ATOM 1080 C CD1 . PHE A 1 140 ? -6.115 -21.197 6.402 1.00 78.77 ? 167 PHE A CD1 1 ATOM 1081 C CD2 . PHE A 1 140 ? -7.253 -21.721 8.424 1.00 71.58 ? 167 PHE A CD2 1 ATOM 1082 C CE1 . PHE A 1 140 ? -5.283 -22.283 6.590 1.00 79.50 ? 167 PHE A CE1 1 ATOM 1083 C CE2 . PHE A 1 140 ? -6.423 -22.809 8.615 1.00 71.70 ? 167 PHE A CE2 1 ATOM 1084 C CZ . PHE A 1 140 ? -5.438 -23.088 7.696 1.00 73.29 ? 167 PHE A CZ 1 ATOM 1085 N N . LYS A 1 141 ? -11.202 -19.206 7.026 1.00 58.19 ? 168 LYS A N 1 ATOM 1086 C CA . LYS A 1 141 ? -12.259 -18.259 7.357 1.00 56.56 ? 168 LYS A CA 1 ATOM 1087 C C . LYS A 1 141 ? -12.483 -18.272 8.860 1.00 67.05 ? 168 LYS A C 1 ATOM 1088 O O . LYS A 1 141 ? -12.789 -19.320 9.437 1.00 72.08 ? 168 LYS A O 1 ATOM 1089 C CB . LYS A 1 141 ? -13.551 -18.592 6.604 1.00 49.66 ? 168 LYS A CB 1 ATOM 1090 C CG . LYS A 1 141 ? -14.830 -18.533 7.438 1.00 51.29 ? 168 LYS A CG 1 ATOM 1091 C CD . LYS A 1 141 ? -15.756 -17.387 7.058 1.00 54.04 ? 168 LYS A CD 1 ATOM 1092 C CE . LYS A 1 141 ? -16.994 -17.352 7.955 1.00 63.43 ? 168 LYS A CE 1 ATOM 1093 N NZ . LYS A 1 141 ? -17.687 -18.671 8.022 1.00 66.36 ? 168 LYS A NZ 1 ATOM 1094 N N . ASP A 1 142 ? -12.340 -17.105 9.482 1.00 68.80 ? 169 ASP A N 1 ATOM 1095 C CA . ASP A 1 142 ? -12.517 -16.989 10.927 1.00 64.25 ? 169 ASP A CA 1 ATOM 1096 C C . ASP A 1 142 ? -11.653 -18.021 11.650 1.00 62.24 ? 169 ASP A C 1 ATOM 1097 O O . ASP A 1 142 ? -12.089 -18.660 12.609 1.00 70.63 ? 169 ASP A O 1 ATOM 1098 C CB . ASP A 1 142 ? -13.991 -17.122 11.301 1.00 66.33 ? 169 ASP A CB 1 ATOM 1099 C CG . ASP A 1 142 ? -14.789 -15.900 10.901 1.00 69.54 ? 169 ASP A CG 1 ATOM 1100 O OD1 . ASP A 1 142 ? -14.171 -14.822 10.761 1.00 66.76 ? 169 ASP A OD1 1 ATOM 1101 O OD2 . ASP A 1 142 ? -16.021 -16.007 10.726 1.00 73.65 ? 169 ASP A OD2 1 ATOM 1102 N N . PHE A 1 143 ? -10.444 -18.193 11.116 1.00 64.93 ? 170 PHE A N 1 ATOM 1103 C CA . PHE A 1 143 ? -9.354 -18.990 11.689 1.00 69.38 ? 170 PHE A CA 1 ATOM 1104 C C . PHE A 1 143 ? -9.488 -20.499 11.459 1.00 74.93 ? 170 PHE A C 1 ATOM 1105 O O . PHE A 1 143 ? -8.681 -21.262 11.994 1.00 80.01 ? 170 PHE A O 1 ATOM 1106 C CB . PHE A 1 143 ? -9.192 -18.733 13.190 1.00 68.66 ? 170 PHE A CB 1 ATOM 1107 C CG . PHE A 1 143 ? -8.835 -17.316 13.542 1.00 71.86 ? 170 PHE A CG 1 ATOM 1108 C CD1 . PHE A 1 143 ? -8.409 -16.420 12.577 1.00 75.76 ? 170 PHE A CD1 1 ATOM 1109 C CD2 . PHE A 1 143 ? -8.920 -16.885 14.854 1.00 70.76 ? 170 PHE A CD2 1 ATOM 1110 C CE1 . PHE A 1 143 ? -8.085 -15.120 12.916 1.00 74.57 ? 170 PHE A CE1 1 ATOM 1111 C CE2 . PHE A 1 143 ? -8.596 -15.591 15.197 1.00 68.61 ? 170 PHE A CE2 1 ATOM 1112 C CZ . PHE A 1 143 ? -8.178 -14.707 14.230 1.00 71.41 ? 170 PHE A CZ 1 ATOM 1113 N N . LEU A 1 144 ? -10.501 -20.947 10.714 1.00 66.16 ? 171 LEU A N 1 ATOM 1114 C CA . LEU A 1 144 ? -10.629 -22.385 10.468 1.00 56.05 ? 171 LEU A CA 1 ATOM 1115 C C . LEU A 1 144 ? -10.446 -22.603 8.968 1.00 57.83 ? 171 LEU A C 1 ATOM 1116 O O . LEU A 1 144 ? -10.885 -21.769 8.173 1.00 64.91 ? 171 LEU A O 1 ATOM 1117 C CB . LEU A 1 144 ? -11.983 -22.902 10.949 1.00 51.36 ? 171 LEU A CB 1 ATOM 1118 C CG . LEU A 1 144 ? -12.266 -22.774 12.446 1.00 45.06 ? 171 LEU A CG 1 ATOM 1119 C CD1 . LEU A 1 144 ? -13.758 -22.765 12.693 1.00 49.49 ? 171 LEU A CD1 1 ATOM 1120 C CD2 . LEU A 1 144 ? -11.615 -23.919 13.201 1.00 44.00 ? 171 LEU A CD2 1 ATOM 1121 N N . PRO A 1 145 ? -9.810 -23.718 8.564 1.00 56.83 ? 172 PRO A N 1 ATOM 1122 C CA . PRO A 1 145 ? -9.754 -23.955 7.114 1.00 59.14 ? 172 PRO A CA 1 ATOM 1123 C C . PRO A 1 145 ? -11.073 -24.095 6.345 1.00 61.30 ? 172 PRO A C 1 ATOM 1124 O O . PRO A 1 145 ? -11.988 -24.770 6.818 1.00 62.23 ? 172 PRO A O 1 ATOM 1125 C CB . PRO A 1 145 ? -8.990 -25.283 7.029 1.00 56.49 ? 172 PRO A CB 1 ATOM 1126 C CG . PRO A 1 145 ? -9.348 -25.986 8.304 1.00 53.16 ? 172 PRO A CG 1 ATOM 1127 C CD . PRO A 1 145 ? -9.390 -24.898 9.340 1.00 54.53 ? 172 PRO A CD 1 ATOM 1128 N N . VAL A 1 146 ? -11.152 -23.465 5.175 1.00 60.87 ? 173 VAL A N 1 ATOM 1129 C CA . VAL A 1 146 ? -12.309 -23.556 4.282 1.00 54.86 ? 173 VAL A CA 1 ATOM 1130 C C . VAL A 1 146 ? -12.398 -24.996 3.763 1.00 62.17 ? 173 VAL A C 1 ATOM 1131 O O . VAL A 1 146 ? -11.398 -25.495 3.250 1.00 66.11 ? 173 VAL A O 1 ATOM 1132 C CB . VAL A 1 146 ? -12.239 -22.541 3.138 1.00 57.17 ? 173 VAL A CB 1 ATOM 1133 C CG1 . VAL A 1 146 ? -13.384 -22.761 2.162 1.00 60.63 ? 173 VAL A CG1 1 ATOM 1134 C CG2 . VAL A 1 146 ? -12.299 -21.127 3.706 1.00 49.55 ? 173 VAL A CG2 1 ATOM 1135 N N . ASP A 1 147 ? -13.540 -25.668 3.823 1.00 69.72 ? 174 ASP A N 1 ATOM 1136 C CA . ASP A 1 147 ? -13.585 -26.984 3.182 1.00 80.79 ? 174 ASP A CA 1 ATOM 1137 C C . ASP A 1 147 ? -14.123 -26.893 1.757 1.00 84.57 ? 174 ASP A C 1 ATOM 1138 O O . ASP A 1 147 ? -15.258 -26.477 1.543 1.00 86.49 ? 174 ASP A O 1 ATOM 1139 C CB . ASP A 1 147 ? -14.426 -27.974 3.983 1.00 94.17 ? 174 ASP A CB 1 ATOM 1140 C CG . ASP A 1 147 ? -14.451 -29.356 3.345 1.00 104.58 ? 174 ASP A CG 1 ATOM 1141 O OD1 . ASP A 1 147 ? -13.364 -29.901 3.055 1.00 105.64 ? 174 ASP A OD1 1 ATOM 1142 O OD2 . ASP A 1 147 ? -15.558 -29.889 3.113 1.00 109.10 ? 174 ASP A OD2 1 ATOM 1143 N N . THR A 1 148 ? -13.300 -27.280 0.785 1.00 100.35 ? 175 THR A N 1 ATOM 1144 C CA . THR A 1 148 ? -13.726 -27.327 -0.613 1.00 116.40 ? 175 THR A CA 1 ATOM 1145 C C . THR A 1 148 ? -13.401 -28.675 -1.240 1.00 139.16 ? 175 THR A C 1 ATOM 1146 O O . THR A 1 148 ? -13.309 -28.789 -2.463 1.00 142.23 ? 175 THR A O 1 ATOM 1147 C CB . THR A 1 148 ? -13.064 -26.228 -1.468 1.00 109.71 ? 175 THR A CB 1 ATOM 1148 O OG1 . THR A 1 148 ? -11.664 -26.504 -1.611 1.00 106.38 ? 175 THR A OG1 1 ATOM 1149 C CG2 . THR A 1 148 ? -13.251 -24.860 -0.839 1.00 110.83 ? 175 THR A CG2 1 ATOM 1150 N N . SER A 1 149 ? -13.209 -29.684 -0.394 1.00 153.87 ? 176 SER A N 1 ATOM 1151 C CA . SER A 1 149 ? -12.962 -31.044 -0.855 1.00 164.29 ? 176 SER A CA 1 ATOM 1152 C C . SER A 1 149 ? -14.072 -31.467 -1.800 1.00 167.54 ? 176 SER A C 1 ATOM 1153 O O . SER A 1 149 ? -13.821 -31.951 -2.904 1.00 171.17 ? 176 SER A O 1 ATOM 1154 C CB . SER A 1 149 ? -12.874 -32.008 0.328 1.00 170.10 ? 176 SER A CB 1 ATOM 1155 O OG . SER A 1 149 ? -12.012 -31.503 1.333 1.00 172.61 ? 176 SER A OG 1 ATOM 1156 N N . ASN A 1 150 ? -15.305 -31.264 -1.356 1.00 170.96 ? 177 ASN A N 1 ATOM 1157 C CA . ASN A 1 150 ? -16.463 -31.529 -2.189 1.00 174.98 ? 177 ASN A CA 1 ATOM 1158 C C . ASN A 1 150 ? -16.544 -30.535 -3.340 1.00 173.18 ? 177 ASN A C 1 ATOM 1159 O O . ASN A 1 150 ? -17.055 -29.427 -3.185 1.00 172.94 ? 177 ASN A O 1 ATOM 1160 C CB . ASN A 1 150 ? -17.745 -31.485 -1.356 1.00 175.82 ? 177 ASN A CB 1 ATOM 1161 C CG . ASN A 1 150 ? -17.772 -30.318 -0.393 1.00 173.67 ? 177 ASN A CG 1 ATOM 1162 O OD1 . ASN A 1 150 ? -16.738 -29.921 0.144 1.00 174.13 ? 177 ASN A OD1 1 ATOM 1163 N ND2 . ASN A 1 150 ? -18.955 -29.758 -0.172 1.00 173.24 ? 177 ASN A ND2 1 ATOM 1164 N N . ASN A 1 151 ? -16.024 -30.943 -4.493 1.00 174.47 ? 178 ASN A N 1 ATOM 1165 C CA . ASN A 1 151 ? -16.145 -30.172 -5.723 1.00 175.91 ? 178 ASN A CA 1 ATOM 1166 C C . ASN A 1 151 ? -17.613 -29.877 -6.031 1.00 181.32 ? 178 ASN A C 1 ATOM 1167 O O . ASN A 1 151 ? -17.944 -28.879 -6.669 1.00 182.74 ? 178 ASN A O 1 ATOM 1168 C CB . ASN A 1 151 ? -15.466 -30.934 -6.873 1.00 173.78 ? 178 ASN A CB 1 ATOM 1169 C CG . ASN A 1 151 ? -16.224 -30.830 -8.189 1.00 174.15 ? 178 ASN A CG 1 ATOM 1170 O OD1 . ASN A 1 151 ? -16.366 -29.746 -8.758 1.00 175.56 ? 178 ASN A OD1 1 ATOM 1171 N ND2 . ASN A 1 151 ? -16.701 -31.967 -8.685 1.00 173.85 ? 178 ASN A ND2 1 ATOM 1172 N N . ASN A 1 152 ? -18.484 -30.743 -5.529 1.00 184.04 ? 179 ASN A N 1 ATOM 1173 C CA . ASN A 1 152 ? -19.918 -30.680 -5.772 1.00 183.13 ? 179 ASN A CA 1 ATOM 1174 C C . ASN A 1 152 ? -20.701 -29.771 -4.827 1.00 173.00 ? 179 ASN A C 1 ATOM 1175 O O . ASN A 1 152 ? -21.920 -29.900 -4.708 1.00 177.37 ? 179 ASN A O 1 ATOM 1176 C CB . ASN A 1 152 ? -20.487 -32.093 -5.683 1.00 190.56 ? 179 ASN A CB 1 ATOM 1177 C CG . ASN A 1 152 ? -19.782 -32.930 -4.631 1.00 196.28 ? 179 ASN A CG 1 ATOM 1178 O OD1 . ASN A 1 152 ? -18.554 -33.032 -4.626 1.00 197.96 ? 179 ASN A OD1 1 ATOM 1179 N ND2 . ASN A 1 152 ? -20.551 -33.514 -3.720 1.00 200.03 ? 179 ASN A ND2 1 ATOM 1180 N N . GLY A 1 153 ? -20.016 -28.853 -4.156 1.00 155.59 ? 180 GLY A N 1 ATOM 1181 C CA . GLY A 1 153 ? -20.666 -28.044 -3.142 1.00 135.50 ? 180 GLY A CA 1 ATOM 1182 C C . GLY A 1 153 ? -20.784 -26.562 -3.441 1.00 118.64 ? 180 GLY A C 1 ATOM 1183 O O . GLY A 1 153 ? -20.441 -26.092 -4.527 1.00 119.94 ? 180 GLY A O 1 ATOM 1184 N N . ARG A 1 154 ? -21.298 -25.834 -2.458 1.00 102.84 ? 181 ARG A N 1 ATOM 1185 C CA . ARG A 1 154 ? -21.604 -24.413 -2.584 1.00 88.30 ? 181 ARG A CA 1 ATOM 1186 C C . ARG A 1 154 ? -20.338 -23.567 -2.674 1.00 80.39 ? 181 ARG A C 1 ATOM 1187 O O . ARG A 1 154 ? -20.329 -22.534 -3.348 1.00 69.90 ? 181 ARG A O 1 ATOM 1188 C CB . ARG A 1 154 ? -22.479 -23.939 -1.425 1.00 81.93 ? 181 ARG A CB 1 ATOM 1189 C CG . ARG A 1 154 ? -23.558 -22.955 -1.861 1.00 81.39 ? 181 ARG A CG 1 ATOM 1190 C CD . ARG A 1 154 ? -24.324 -22.434 -0.658 1.00 83.49 ? 181 ARG A CD 1 ATOM 1191 N NE . ARG A 1 154 ? -23.549 -22.603 0.566 1.00 83.69 ? 181 ARG A NE 1 ATOM 1192 C CZ . ARG A 1 154 ? -23.163 -21.608 1.353 1.00 83.01 ? 181 ARG A CZ 1 ATOM 1193 N NH1 . ARG A 1 154 ? -23.496 -20.361 1.057 1.00 81.69 ? 181 ARG A NH1 1 ATOM 1194 N NH2 . ARG A 1 154 ? -22.455 -21.864 2.443 1.00 84.54 ? 181 ARG A NH2 1 ATOM 1195 N N . ILE A 1 155 ? -19.272 -23.991 -1.998 1.00 84.49 ? 182 ILE A N 1 ATOM 1196 C CA . ILE A 1 155 ? -18.029 -23.234 -2.047 1.00 85.88 ? 182 ILE A CA 1 ATOM 1197 C C . ILE A 1 155 ? -17.001 -24.039 -2.828 1.00 89.36 ? 182 ILE A C 1 ATOM 1198 O O . ILE A 1 155 ? -16.657 -25.180 -2.504 1.00 93.45 ? 182 ILE A O 1 ATOM 1199 C CB . ILE A 1 155 ? -17.507 -22.935 -0.623 1.00 82.35 ? 182 ILE A CB 1 ATOM 1200 C CG1 . ILE A 1 155 ? -18.489 -22.023 0.115 1.00 65.92 ? 182 ILE A CG1 1 ATOM 1201 C CG2 . ILE A 1 155 ? -16.111 -22.324 -0.677 1.00 90.00 ? 182 ILE A CG2 1 ATOM 1202 C CD1 . ILE A 1 155 ? -18.543 -22.251 1.607 1.00 65.19 ? 182 ILE A CD1 1 ATOM 1203 N N . LYS A 1 156 ? -16.511 -23.368 -3.861 1.00 84.50 ? 183 LYS A N 1 ATOM 1204 C CA . LYS A 1 156 ? -15.576 -23.879 -4.851 1.00 81.37 ? 183 LYS A CA 1 ATOM 1205 C C . LYS A 1 156 ? -14.252 -23.133 -4.931 1.00 73.36 ? 183 LYS A C 1 ATOM 1206 O O . LYS A 1 156 ? -14.223 -21.928 -4.767 1.00 62.31 ? 183 LYS A O 1 ATOM 1207 C CB . LYS A 1 156 ? -16.258 -23.895 -6.222 1.00 89.87 ? 183 LYS A CB 1 ATOM 1208 C CG . LYS A 1 156 ? -17.529 -24.738 -6.227 1.00 93.69 ? 183 LYS A CG 1 ATOM 1209 C CD . LYS A 1 156 ? -17.984 -25.115 -7.632 1.00 101.44 ? 183 LYS A CD 1 ATOM 1210 C CE . LYS A 1 156 ? -18.469 -23.909 -8.416 1.00 107.74 ? 183 LYS A CE 1 ATOM 1211 N NZ . LYS A 1 156 ? -18.917 -24.293 -9.781 1.00 107.53 ? 183 LYS A NZ 1 ATOM 1212 N N . GLN A 1 157 ? -13.145 -23.839 -5.120 1.00 80.81 ? 184 GLN A N 1 ATOM 1213 C CA . GLN A 1 157 ? -11.880 -23.142 -5.335 1.00 88.43 ? 184 GLN A CA 1 ATOM 1214 C C . GLN A 1 157 ? -11.527 -23.313 -6.811 1.00 90.86 ? 184 GLN A C 1 ATOM 1215 O O . GLN A 1 157 ? -11.756 -24.371 -7.396 1.00 92.33 ? 184 GLN A O 1 ATOM 1216 C CB . GLN A 1 157 ? -10.768 -23.693 -4.431 1.00 92.02 ? 184 GLN A CB 1 ATOM 1217 C CG . GLN A 1 157 ? -9.386 -23.187 -4.814 1.00 95.87 ? 184 GLN A CG 1 ATOM 1218 C CD . GLN A 1 157 ? -8.296 -23.662 -3.880 1.00 100.77 ? 184 GLN A CD 1 ATOM 1219 O OE1 . GLN A 1 157 ? -8.391 -23.497 -2.664 1.00 101.37 ? 184 GLN A OE1 1 ATOM 1220 N NE2 . GLN A 1 157 ? -7.250 -24.261 -4.444 1.00 104.37 ? 184 GLN A NE2 1 ATOM 1221 N N . LEU A 1 158 ? -10.971 -22.266 -7.414 1.00 93.62 ? 185 LEU A N 1 ATOM 1222 C CA . LEU A 1 158 ? -10.716 -22.306 -8.844 1.00 97.85 ? 185 LEU A CA 1 ATOM 1223 C C . LEU A 1 158 ? -9.228 -22.374 -9.141 1.00 117.32 ? 185 LEU A C 1 ATOM 1224 O O . LEU A 1 158 ? -8.391 -22.003 -8.315 1.00 120.92 ? 185 LEU A O 1 ATOM 1225 C CB . LEU A 1 158 ? -11.333 -21.079 -9.533 1.00 87.36 ? 185 LEU A CB 1 ATOM 1226 C CG . LEU A 1 158 ? -12.740 -20.648 -9.076 1.00 76.10 ? 185 LEU A CG 1 ATOM 1227 C CD1 . LEU A 1 158 ? -13.260 -19.487 -9.919 1.00 75.96 ? 185 LEU A CD1 1 ATOM 1228 C CD2 . LEU A 1 158 ? -13.717 -21.814 -9.094 1.00 66.63 ? 185 LEU A CD2 1 ATOM 1229 N N . ARG A 1 159 ? -8.908 -22.864 -10.333 1.00 131.30 ? 186 ARG A N 1 ATOM 1230 C CA . ARG A 1 159 ? -7.528 -22.957 -10.791 1.00 145.04 ? 186 ARG A CA 1 ATOM 1231 C C . ARG A 1 159 ? -7.017 -21.674 -11.455 1.00 155.89 ? 186 ARG A C 1 ATOM 1232 O O . ARG A 1 159 ? -7.748 -20.688 -11.566 1.00 150.62 ? 186 ARG A O 1 ATOM 1233 C CB . ARG A 1 159 ? -7.379 -24.145 -11.746 1.00 155.15 ? 186 ARG A CB 1 ATOM 1234 C CG . ARG A 1 159 ? -7.738 -25.491 -11.120 1.00 160.12 ? 186 ARG A CG 1 ATOM 1235 C CD . ARG A 1 159 ? -9.195 -25.878 -11.379 1.00 159.72 ? 186 ARG A CD 1 ATOM 1236 N NE . ARG A 1 159 ? -9.525 -27.220 -10.901 1.00 160.54 ? 186 ARG A NE 1 ATOM 1237 C CZ . ARG A 1 159 ? -9.317 -28.335 -11.596 1.00 163.59 ? 186 ARG A CZ 1 ATOM 1238 N NH1 . ARG A 1 159 ? -8.766 -28.278 -12.802 1.00 165.19 ? 186 ARG A NH1 1 ATOM 1239 N NH2 . ARG A 1 159 ? -9.656 -29.508 -11.080 1.00 163.68 ? 186 ARG A NH2 1 ATOM 1240 N N . SER A 1 160 ? -5.770 -21.704 -11.923 1.00 174.89 ? 187 SER A N 1 ATOM 1241 C CA . SER A 1 160 ? -5.203 -20.559 -12.645 1.00 186.70 ? 187 SER A CA 1 ATOM 1242 C C . SER A 1 160 ? -5.193 -20.571 -14.189 1.00 201.42 ? 187 SER A C 1 ATOM 1243 O O . SER A 1 160 ? -5.663 -19.601 -14.773 1.00 199.57 ? 187 SER A O 1 ATOM 1244 C CB . SER A 1 160 ? -3.774 -20.319 -12.142 1.00 184.41 ? 187 SER A CB 1 ATOM 1245 O OG . SER A 1 160 ? -3.469 -18.939 -12.141 1.00 183.40 ? 187 SER A OG 1 ATOM 1246 N N . GLU A 1 161 ? -4.681 -21.600 -14.876 1.00 220.20 ? 188 GLU A N 1 ATOM 1247 C CA . GLU A 1 161 ? -4.213 -22.872 -14.334 1.00 225.28 ? 188 GLU A CA 1 ATOM 1248 C C . GLU A 1 161 ? -2.690 -22.926 -14.178 1.00 227.81 ? 188 GLU A C 1 ATOM 1249 O O . GLU A 1 161 ? -2.183 -23.460 -13.192 1.00 230.92 ? 188 GLU A O 1 ATOM 1250 C CB . GLU A 1 161 ? -4.676 -24.020 -15.240 1.00 229.98 ? 188 GLU A CB 1 ATOM 1251 C CG . GLU A 1 161 ? -5.001 -25.313 -14.519 1.00 233.01 ? 188 GLU A CG 1 ATOM 1252 C CD . GLU A 1 161 ? -6.485 -25.620 -14.527 1.00 233.13 ? 188 GLU A CD 1 ATOM 1253 O OE1 . GLU A 1 161 ? -7.274 -24.739 -14.931 1.00 234.22 ? 188 GLU A OE1 1 ATOM 1254 O OE2 . GLU A 1 161 ? -6.864 -26.738 -14.120 1.00 234.15 ? 188 GLU A OE2 1 ATOM 1255 N N . SER A 1 162 ? -1.965 -22.371 -15.149 1.00 222.85 ? 189 SER A N 1 ATOM 1256 C CA . SER A 1 162 ? -0.505 -22.492 -15.171 1.00 218.88 ? 189 SER A CA 1 ATOM 1257 C C . SER A 1 162 ? 0.221 -21.152 -15.306 1.00 233.50 ? 189 SER A C 1 ATOM 1258 O O . SER A 1 162 ? 0.299 -20.580 -16.395 1.00 241.96 ? 189 SER A O 1 ATOM 1259 C CB . SER A 1 162 ? -0.076 -23.421 -16.310 1.00 204.14 ? 189 SER A CB 1 ATOM 1260 O OG . SER A 1 162 ? 1.332 -23.581 -16.333 1.00 200.09 ? 189 SER A OG 1 ATOM 1261 N N . ILE A 1 163 ? 0.757 -20.664 -14.189 1.00 230.76 ? 190 ILE A N 1 ATOM 1262 C CA . ILE A 1 163 ? 1.512 -19.411 -14.143 1.00 234.21 ? 190 ILE A CA 1 ATOM 1263 C C . ILE A 1 163 ? 2.823 -19.645 -13.384 1.00 231.97 ? 190 ILE A C 1 ATOM 1264 O O . ILE A 1 163 ? 2.818 -20.323 -12.356 1.00 229.16 ? 190 ILE A O 1 ATOM 1265 C CB . ILE A 1 163 ? 0.705 -18.282 -13.447 1.00 238.28 ? 190 ILE A CB 1 ATOM 1266 C CG1 . ILE A 1 163 ? -0.799 -18.499 -13.608 1.00 234.53 ? 190 ILE A CG1 1 ATOM 1267 C CG2 . ILE A 1 163 ? 1.077 -16.921 -14.001 1.00 240.99 ? 190 ILE A CG2 1 ATOM 1268 C CD1 . ILE A 1 163 ? -1.337 -18.104 -14.966 1.00 234.28 ? 190 ILE A CD1 1 ATOM 1269 N N . GLY A 1 164 ? 3.944 -19.106 -13.866 1.00 227.11 ? 191 GLY A N 1 ATOM 1270 C CA . GLY A 1 164 ? 4.010 -18.290 -15.066 1.00 217.95 ? 191 GLY A CA 1 ATOM 1271 C C . GLY A 1 164 ? 4.864 -17.052 -14.841 1.00 204.76 ? 191 GLY A C 1 ATOM 1272 O O . GLY A 1 164 ? 5.557 -16.947 -13.828 1.00 202.83 ? 191 GLY A O 1 ATOM 1273 N N . GLY A 1 165 ? 4.815 -16.112 -15.782 1.00 195.18 ? 192 GLY A N 1 ATOM 1274 C CA . GLY A 1 165 ? 5.570 -14.873 -15.678 1.00 193.54 ? 192 GLY A CA 1 ATOM 1275 C C . GLY A 1 165 ? 4.937 -13.900 -14.700 1.00 190.34 ? 192 GLY A C 1 ATOM 1276 O O . GLY A 1 165 ? 5.486 -12.835 -14.411 1.00 190.23 ? 192 GLY A O 1 ATOM 1277 N N . THR A 1 166 ? 3.766 -14.278 -14.201 1.00 186.10 ? 193 THR A N 1 ATOM 1278 C CA . THR A 1 166 ? 3.056 -13.534 -13.172 1.00 180.18 ? 193 THR A CA 1 ATOM 1279 C C . THR A 1 166 ? 2.752 -14.512 -12.028 1.00 177.44 ? 193 THR A C 1 ATOM 1280 O O . THR A 1 166 ? 3.207 -15.657 -12.065 1.00 178.18 ? 193 THR A O 1 ATOM 1281 C CB . THR A 1 166 ? 1.763 -12.886 -13.737 1.00 175.78 ? 193 THR A CB 1 ATOM 1282 O OG1 . THR A 1 166 ? 1.076 -13.820 -14.578 1.00 175.55 ? 193 THR A OG1 1 ATOM 1283 C CG2 . THR A 1 166 ? 2.096 -11.635 -14.538 1.00 175.48 ? 193 THR A CG2 1 ATOM 1284 N N . PRO A 1 167 ? 2.028 -14.064 -10.986 1.00 174.59 ? 194 PRO A N 1 ATOM 1285 C CA . PRO A 1 167 ? 1.633 -15.051 -9.973 1.00 165.99 ? 194 PRO A CA 1 ATOM 1286 C C . PRO A 1 167 ? 0.483 -15.991 -10.370 1.00 152.43 ? 194 PRO A C 1 ATOM 1287 O O . PRO A 1 167 ? -0.262 -15.748 -11.317 1.00 144.35 ? 194 PRO A O 1 ATOM 1288 C CB . PRO A 1 167 ? 1.209 -14.173 -8.786 1.00 162.99 ? 194 PRO A CB 1 ATOM 1289 C CG . PRO A 1 167 ? 0.933 -12.834 -9.370 1.00 163.79 ? 194 PRO A CG 1 ATOM 1290 C CD . PRO A 1 167 ? 1.937 -12.694 -10.453 1.00 172.75 ? 194 PRO A CD 1 ATOM 1291 N N . ILE A 1 168 ? 0.389 -17.087 -9.623 1.00 148.45 ? 195 ILE A N 1 ATOM 1292 C CA . ILE A 1 168 ? -0.726 -18.039 -9.621 1.00 146.76 ? 195 ILE A CA 1 ATOM 1293 C C . ILE A 1 168 ? -2.026 -17.496 -9.036 1.00 146.75 ? 195 ILE A C 1 ATOM 1294 O O . ILE A 1 168 ? -2.019 -16.893 -7.953 1.00 147.61 ? 195 ILE A O 1 ATOM 1295 C CB . ILE A 1 168 ? -0.379 -19.301 -8.779 1.00 79.60 ? 195 ILE A CB 1 ATOM 1296 C CG1 . ILE A 1 168 ? 0.715 -20.139 -9.434 1.00 92.51 ? 195 ILE A CG1 1 ATOM 1297 C CG2 . ILE A 1 168 ? -1.611 -20.169 -8.529 1.00 70.90 ? 195 ILE A CG2 1 ATOM 1298 C CD1 . ILE A 1 168 ? 0.960 -21.438 -8.710 1.00 92.71 ? 195 ILE A CD1 1 ATOM 1299 N N . ARG A 1 169 ? -3.127 -17.664 -9.769 1.00 145.97 ? 196 ARG A N 1 ATOM 1300 C CA . ARG A 1 169 ? -4.382 -17.080 -9.323 1.00 145.14 ? 196 ARG A CA 1 ATOM 1301 C C . ARG A 1 169 ? -5.153 -18.114 -8.509 1.00 136.39 ? 196 ARG A C 1 ATOM 1302 O O . ARG A 1 169 ? -5.411 -19.224 -8.999 1.00 135.01 ? 196 ARG A O 1 ATOM 1303 C CB . ARG A 1 169 ? -5.247 -16.652 -10.513 1.00 153.39 ? 196 ARG A CB 1 ATOM 1304 C CG . ARG A 1 169 ? -4.927 -15.303 -11.133 1.00 159.03 ? 196 ARG A CG 1 ATOM 1305 C CD . ARG A 1 169 ? -3.946 -15.407 -12.293 1.00 165.77 ? 196 ARG A CD 1 ATOM 1306 N NE . ARG A 1 169 ? -3.992 -14.214 -13.139 1.00 171.07 ? 196 ARG A NE 1 ATOM 1307 C CZ . ARG A 1 169 ? -3.530 -13.018 -12.782 1.00 171.92 ? 196 ARG A CZ 1 ATOM 1308 N NH1 . ARG A 1 169 ? -2.987 -12.839 -11.584 1.00 169.74 ? 196 ARG A NH1 1 ATOM 1309 N NH2 . ARG A 1 169 ? -3.615 -11.992 -13.620 1.00 172.43 ? 196 ARG A NH2 1 ATOM 1310 N N . GLY A 1 170 ? -5.551 -17.769 -7.291 1.00 135.63 ? 197 GLY A N 1 ATOM 1311 C CA . GLY A 1 170 ? -6.493 -18.595 -6.567 1.00 126.81 ? 197 GLY A CA 1 ATOM 1312 C C . GLY A 1 170 ? -7.820 -17.886 -6.427 1.00 121.41 ? 197 GLY A C 1 ATOM 1313 O O . GLY A 1 170 ? -7.842 -16.686 -6.140 1.00 124.64 ? 197 GLY A O 1 ATOM 1314 N N . ALA A 1 171 ? -8.922 -18.601 -6.602 1.00 105.37 ? 198 ALA A N 1 ATOM 1315 C CA . ALA A 1 171 ? -10.228 -17.991 -6.387 1.00 86.44 ? 198 ALA A CA 1 ATOM 1316 C C . ALA A 1 171 ? -11.028 -18.805 -5.378 1.00 75.88 ? 198 ALA A C 1 ATOM 1317 O O . ALA A 1 171 ? -11.122 -20.024 -5.517 1.00 86.30 ? 198 ALA A O 1 ATOM 1318 C CB . ALA A 1 171 ? -10.963 -17.869 -7.710 1.00 87.64 ? 198 ALA A CB 1 ATOM 1319 N N . LEU A 1 172 ? -11.602 -18.149 -4.376 1.00 64.49 ? 199 LEU A N 1 ATOM 1320 C CA . LEU A 1 172 ? -12.613 -18.777 -3.529 1.00 66.14 ? 199 LEU A CA 1 ATOM 1321 C C . LEU A 1 172 ? -14.030 -18.329 -3.874 1.00 68.48 ? 199 LEU A C 1 ATOM 1322 O O . LEU A 1 172 ? -14.439 -17.219 -3.523 1.00 74.32 ? 199 LEU A O 1 ATOM 1323 C CB . LEU A 1 172 ? -12.334 -18.504 -2.050 1.00 66.42 ? 199 LEU A CB 1 ATOM 1324 C CG . LEU A 1 172 ? -13.158 -19.385 -1.104 1.00 67.10 ? 199 LEU A CG 1 ATOM 1325 C CD1 . LEU A 1 172 ? -12.841 -20.846 -1.351 1.00 67.93 ? 199 LEU A CD1 1 ATOM 1326 C CD2 . LEU A 1 172 ? -12.937 -19.031 0.364 1.00 69.15 ? 199 LEU A CD2 1 ATOM 1327 N N . GLN A 1 173 ? -14.779 -19.199 -4.537 1.00 68.84 ? 200 GLN A N 1 ATOM 1328 C CA . GLN A 1 173 ? -16.118 -18.882 -5.026 1.00 75.24 ? 200 GLN A CA 1 ATOM 1329 C C . GLN A 1 173 ? -17.283 -19.409 -4.179 1.00 70.42 ? 200 GLN A C 1 ATOM 1330 O O . GLN A 1 173 ? -17.509 -20.622 -4.102 1.00 72.07 ? 200 GLN A O 1 ATOM 1331 C CB . GLN A 1 173 ? -16.286 -19.394 -6.447 1.00 88.39 ? 200 GLN A CB 1 ATOM 1332 C CG . GLN A 1 173 ? -17.532 -18.848 -7.102 1.00 88.06 ? 200 GLN A CG 1 ATOM 1333 C CD . GLN A 1 173 ? -17.802 -19.459 -8.454 1.00 84.85 ? 200 GLN A CD 1 ATOM 1334 O OE1 . GLN A 1 173 ? -18.280 -20.590 -8.551 1.00 91.59 ? 200 GLN A OE1 1 ATOM 1335 N NE2 . GLN A 1 173 ? -17.494 -18.716 -9.513 1.00 79.11 ? 200 GLN A NE2 1 ATOM 1336 N N . ILE A 1 174 ? -18.000 -18.486 -3.545 1.00 64.85 ? 201 ILE A N 1 ATOM 1337 C CA . ILE A 1 174 ? -19.103 -18.797 -2.641 1.00 71.64 ? 201 ILE A CA 1 ATOM 1338 C C . ILE A 1 174 ? -20.460 -18.511 -3.295 1.00 76.65 ? 201 ILE A C 1 ATOM 1339 O O . ILE A 1 174 ? -20.916 -17.361 -3.300 1.00 73.83 ? 201 ILE A O 1 ATOM 1340 C CB . ILE A 1 174 ? -19.027 -17.987 -1.327 1.00 67.81 ? 201 ILE A CB 1 ATOM 1341 C CG1 . ILE A 1 174 ? -17.649 -18.113 -0.677 1.00 75.85 ? 201 ILE A CG1 1 ATOM 1342 C CG2 . ILE A 1 174 ? -20.122 -18.423 -0.355 1.00 57.89 ? 201 ILE A CG2 1 ATOM 1343 C CD1 . ILE A 1 174 ? -17.528 -17.333 0.622 1.00 77.04 ? 201 ILE A CD1 1 ATOM 1344 N N . GLU A 1 175 ? -21.110 -19.540 -3.835 1.00 77.28 ? 202 GLU A N 1 ATOM 1345 C CA . GLU A 1 175 ? -22.427 -19.345 -4.452 1.00 80.87 ? 202 GLU A CA 1 ATOM 1346 C C . GLU A 1 175 ? -23.500 -19.292 -3.366 1.00 82.61 ? 202 GLU A C 1 ATOM 1347 O O . GLU A 1 175 ? -23.312 -19.847 -2.283 1.00 87.27 ? 202 GLU A O 1 ATOM 1348 C CB . GLU A 1 175 ? -22.734 -20.462 -5.448 1.00 92.02 ? 202 GLU A CB 1 ATOM 1349 C CG . GLU A 1 175 ? -21.725 -20.613 -6.572 1.00 98.67 ? 202 GLU A CG 1 ATOM 1350 C CD . GLU A 1 175 ? -21.974 -21.853 -7.407 1.00 106.69 ? 202 GLU A CD 1 ATOM 1351 O OE1 . GLU A 1 175 ? -21.925 -22.967 -6.845 1.00 114.16 ? 202 GLU A OE1 1 ATOM 1352 O OE2 . GLU A 1 175 ? -22.222 -21.716 -8.623 1.00 104.38 ? 202 GLU A OE2 1 ATOM 1353 N N . GLN A 1 176 ? -24.607 -18.616 -3.669 1.00 78.16 ? 203 GLN A N 1 ATOM 1354 C CA . GLN A 1 176 ? -25.786 -18.574 -2.805 1.00 76.87 ? 203 GLN A CA 1 ATOM 1355 C C . GLN A 1 176 ? -25.443 -18.159 -1.383 1.00 69.40 ? 203 GLN A C 1 ATOM 1356 O O . GLN A 1 176 ? -25.803 -18.839 -0.420 1.00 67.62 ? 203 GLN A O 1 ATOM 1357 C CB . GLN A 1 176 ? -26.495 -19.934 -2.803 1.00 85.39 ? 203 GLN A CB 1 ATOM 1358 C CG . GLN A 1 176 ? -27.311 -20.209 -4.047 1.00 92.44 ? 203 GLN A CG 1 ATOM 1359 C CD . GLN A 1 176 ? -28.429 -19.199 -4.239 1.00 95.96 ? 203 GLN A CD 1 ATOM 1360 O OE1 . GLN A 1 176 ? -28.673 -18.728 -5.350 1.00 100.50 ? 203 GLN A OE1 1 ATOM 1361 N NE2 . GLN A 1 176 ? -29.118 -18.867 -3.154 1.00 91.90 ? 203 GLN A NE2 1 ATOM 1362 N N . SER A 1 177 ? -24.760 -17.023 -1.273 1.00 65.46 ? 204 SER A N 1 ATOM 1363 C CA . SER A 1 177 ? -24.251 -16.494 -0.012 1.00 65.30 ? 204 SER A CA 1 ATOM 1364 C C . SER A 1 177 ? -25.306 -16.346 1.071 1.00 67.77 ? 204 SER A C 1 ATOM 1365 O O . SER A 1 177 ? -26.460 -16.035 0.781 1.00 75.92 ? 204 SER A O 1 ATOM 1366 C CB . SER A 1 177 ? -23.587 -15.142 -0.247 1.00 69.43 ? 204 SER A CB 1 ATOM 1367 O OG . SER A 1 177 ? -22.615 -15.216 -1.276 1.00 80.10 ? 204 SER A OG 1 ATOM 1368 N N . GLU A 1 178 ? -24.917 -16.592 2.316 1.00 66.67 ? 205 GLU A N 1 ATOM 1369 C CA . GLU A 1 178 ? -25.836 -16.445 3.434 1.00 72.44 ? 205 GLU A CA 1 ATOM 1370 C C . GLU A 1 178 ? -25.111 -15.750 4.576 1.00 74.08 ? 205 GLU A C 1 ATOM 1371 O O . GLU A 1 178 ? -23.893 -15.570 4.514 1.00 74.16 ? 205 GLU A O 1 ATOM 1372 C CB . GLU A 1 178 ? -26.397 -17.804 3.871 1.00 75.57 ? 205 GLU A CB 1 ATOM 1373 C CG . GLU A 1 178 ? -25.349 -18.899 4.001 1.00 75.50 ? 205 GLU A CG 1 ATOM 1374 C CD . GLU A 1 178 ? -25.949 -20.294 3.896 1.00 80.52 ? 205 GLU A CD 1 ATOM 1375 O OE1 . GLU A 1 178 ? -25.861 -20.899 2.804 1.00 83.20 ? 205 GLU A OE1 1 ATOM 1376 O OE2 . GLU A 1 178 ? -26.498 -20.789 4.904 1.00 82.63 ? 205 GLU A OE2 1 ATOM 1377 N N . GLU A 1 179 ? -25.857 -15.338 5.597 1.00 73.18 ? 206 GLU A N 1 ATOM 1378 C CA . GLU A 1 179 ? -25.287 -14.554 6.692 1.00 75.71 ? 206 GLU A CA 1 ATOM 1379 C C . GLU A 1 179 ? -24.073 -15.260 7.292 1.00 71.82 ? 206 GLU A C 1 ATOM 1380 O O . GLU A 1 179 ? -23.100 -14.617 7.658 1.00 70.32 ? 206 GLU A O 1 ATOM 1381 C CB . GLU A 1 179 ? -26.354 -14.261 7.754 1.00 92.01 ? 206 GLU A CB 1 ATOM 1382 C CG . GLU A 1 179 ? -25.992 -14.645 9.181 1.00 107.61 ? 206 GLU A CG 1 ATOM 1383 C CD . GLU A 1 179 ? -27.023 -14.154 10.182 1.00 122.09 ? 206 GLU A CD 1 ATOM 1384 O OE1 . GLU A 1 179 ? -27.550 -13.040 9.988 1.00 126.84 ? 206 GLU A OE1 1 ATOM 1385 O OE2 . GLU A 1 179 ? -27.307 -14.880 11.157 1.00 125.86 ? 206 GLU A OE2 1 ATOM 1386 N N . SER A 1 180 ? -24.145 -16.581 7.414 1.00 75.26 ? 207 SER A N 1 ATOM 1387 C CA . SER A 1 180 ? -23.061 -17.359 8.002 1.00 71.06 ? 207 SER A CA 1 ATOM 1388 C C . SER A 1 180 ? -21.765 -17.292 7.193 1.00 59.46 ? 207 SER A C 1 ATOM 1389 O O . SER A 1 180 ? -20.685 -17.569 7.712 1.00 60.46 ? 207 SER A O 1 ATOM 1390 C CB . SER A 1 180 ? -23.488 -18.813 8.165 1.00 81.28 ? 207 SER A CB 1 ATOM 1391 O OG . SER A 1 180 ? -23.891 -19.351 6.916 1.00 83.55 ? 207 SER A OG 1 ATOM 1392 N N . ASP A 1 181 ? -21.883 -16.945 5.914 1.00 63.97 ? 208 ASP A N 1 ATOM 1393 C CA . ASP A 1 181 ? -20.721 -16.774 5.042 1.00 70.81 ? 208 ASP A CA 1 ATOM 1394 C C . ASP A 1 181 ? -19.976 -15.482 5.359 1.00 66.54 ? 208 ASP A C 1 ATOM 1395 O O . ASP A 1 181 ? -18.820 -15.311 4.975 1.00 59.37 ? 208 ASP A O 1 ATOM 1396 C CB . ASP A 1 181 ? -21.127 -16.823 3.572 1.00 68.94 ? 208 ASP A CB 1 ATOM 1397 C CG . ASP A 1 181 ? -21.392 -18.234 3.092 1.00 70.29 ? 208 ASP A CG 1 ATOM 1398 O OD1 . ASP A 1 181 ? -20.811 -19.181 3.670 1.00 69.84 ? 208 ASP A OD1 1 ATOM 1399 O OD2 . ASP A 1 181 ? -22.187 -18.400 2.145 1.00 70.15 ? 208 ASP A OD2 1 ATOM 1400 N N . GLN A 1 182 ? -20.656 -14.581 6.066 1.00 69.13 ? 209 GLN A N 1 ATOM 1401 C CA . GLN A 1 182 ? -20.063 -13.321 6.495 1.00 65.09 ? 209 GLN A CA 1 ATOM 1402 C C . GLN A 1 182 ? -18.887 -13.648 7.396 1.00 57.01 ? 209 GLN A C 1 ATOM 1403 O O . GLN A 1 182 ? -18.960 -14.581 8.193 1.00 54.65 ? 209 GLN A O 1 ATOM 1404 C CB . GLN A 1 182 ? -21.098 -12.465 7.228 1.00 63.52 ? 209 GLN A CB 1 ATOM 1405 C CG . GLN A 1 182 ? -20.953 -10.965 7.096 1.00 67.89 ? 209 GLN A CG 1 ATOM 1406 C CD . GLN A 1 182 ? -22.184 -10.223 7.571 1.00 72.70 ? 209 GLN A CD 1 ATOM 1407 O OE1 . GLN A 1 182 ? -22.581 -9.221 6.979 1.00 70.57 ? 209 GLN A OE1 1 ATOM 1408 N NE2 . GLN A 1 182 ? -22.798 -10.714 8.640 1.00 80.63 ? 209 GLN A NE2 1 ATOM 1409 N N . GLY A 1 183 ? -17.785 -12.921 7.249 1.00 54.08 ? 210 GLY A N 1 ATOM 1410 C CA . GLY A 1 183 ? -16.673 -13.168 8.154 1.00 54.62 ? 210 GLY A CA 1 ATOM 1411 C C . GLY A 1 183 ? -15.318 -12.783 7.608 1.00 63.57 ? 210 GLY A C 1 ATOM 1412 O O . GLY A 1 183 ? -15.213 -12.077 6.609 1.00 66.64 ? 210 GLY A O 1 ATOM 1413 N N . LYS A 1 184 ? -14.272 -13.217 8.298 1.00 65.95 ? 211 LYS A N 1 ATOM 1414 C CA . LYS A 1 184 ? -12.939 -12.747 7.979 1.00 68.31 ? 211 LYS A CA 1 ATOM 1415 C C . LYS A 1 184 ? -12.159 -13.818 7.218 1.00 63.87 ? 211 LYS A C 1 ATOM 1416 O O . LYS A 1 184 ? -11.847 -14.877 7.765 1.00 63.68 ? 211 LYS A O 1 ATOM 1417 C CB . LYS A 1 184 ? -12.212 -12.360 9.270 1.00 80.07 ? 211 LYS A CB 1 ATOM 1418 C CG . LYS A 1 184 ? -10.902 -11.619 9.083 1.00 97.01 ? 211 LYS A CG 1 ATOM 1419 C CD . LYS A 1 184 ? -10.507 -10.901 10.370 1.00 106.24 ? 211 LYS A CD 1 ATOM 1420 C CE . LYS A 1 184 ? -11.606 -9.934 10.801 1.00 112.10 ? 211 LYS A CE 1 ATOM 1421 N NZ . LYS A 1 184 ? -11.314 -9.230 12.078 1.00 116.37 ? 211 LYS A NZ 1 ATOM 1422 N N . TYR A 1 185 ? -11.877 -13.559 5.945 1.00 54.29 ? 212 TYR A N 1 ATOM 1423 C CA . TYR A 1 185 ? -11.225 -14.555 5.103 1.00 54.53 ? 212 TYR A CA 1 ATOM 1424 C C . TYR A 1 185 ? -9.738 -14.232 4.909 1.00 55.05 ? 212 TYR A C 1 ATOM 1425 O O . TYR A 1 185 ? -9.359 -13.071 4.731 1.00 55.80 ? 212 TYR A O 1 ATOM 1426 C CB . TYR A 1 185 ? -11.924 -14.646 3.739 1.00 46.59 ? 212 TYR A CB 1 ATOM 1427 C CG . TYR A 1 185 ? -13.283 -15.324 3.769 1.00 49.04 ? 212 TYR A CG 1 ATOM 1428 C CD1 . TYR A 1 185 ? -14.406 -14.662 4.256 1.00 51.80 ? 212 TYR A CD1 1 ATOM 1429 C CD2 . TYR A 1 185 ? -13.446 -16.622 3.296 1.00 54.76 ? 212 TYR A CD2 1 ATOM 1430 C CE1 . TYR A 1 185 ? -15.652 -15.279 4.279 1.00 62.49 ? 212 TYR A CE1 1 ATOM 1431 C CE2 . TYR A 1 185 ? -14.689 -17.247 3.315 1.00 62.03 ? 212 TYR A CE2 1 ATOM 1432 C CZ . TYR A 1 185 ? -15.787 -16.569 3.807 1.00 66.82 ? 212 TYR A CZ 1 ATOM 1433 O OH . TYR A 1 185 ? -17.023 -17.181 3.834 1.00 65.53 ? 212 TYR A OH 1 ATOM 1434 N N . GLU A 1 186 ? -8.904 -15.264 4.914 1.00 52.17 ? 213 GLU A N 1 ATOM 1435 C CA . GLU A 1 186 ? -7.483 -15.118 4.607 1.00 60.04 ? 213 GLU A CA 1 ATOM 1436 C C . GLU A 1 186 ? -7.110 -16.202 3.614 1.00 58.97 ? 213 GLU A C 1 ATOM 1437 O O . GLU A 1 186 ? -7.524 -17.354 3.759 1.00 50.70 ? 213 GLU A O 1 ATOM 1438 C CB . GLU A 1 186 ? -6.588 -15.137 5.855 1.00 71.45 ? 213 GLU A CB 1 ATOM 1439 C CG . GLU A 1 186 ? -6.875 -16.185 6.906 1.00 75.92 ? 213 GLU A CG 1 ATOM 1440 C CD . GLU A 1 186 ? -6.106 -15.901 8.185 1.00 75.62 ? 213 GLU A CD 1 ATOM 1441 O OE1 . GLU A 1 186 ? -6.423 -16.510 9.225 1.00 79.47 ? 213 GLU A OE1 1 ATOM 1442 O OE2 . GLU A 1 186 ? -5.184 -15.058 8.145 1.00 66.00 ? 213 GLU A OE2 1 ATOM 1443 N N . CYS A 1 187 ? -6.356 -15.829 2.586 1.00 63.23 ? 214 CYS A N 1 ATOM 1444 C CA . CYS A 1 187 ? -5.735 -16.819 1.717 1.00 67.23 ? 214 CYS A CA 1 ATOM 1445 C C . CYS A 1 187 ? -4.283 -17.111 2.082 1.00 67.10 ? 214 CYS A C 1 ATOM 1446 O O . CYS A 1 187 ? -3.513 -16.228 2.461 1.00 60.62 ? 214 CYS A O 1 ATOM 1447 C CB . CYS A 1 187 ? -5.823 -16.375 0.256 1.00 72.45 ? 214 CYS A CB 1 ATOM 1448 S SG . CYS A 1 187 ? -4.274 -15.794 -0.473 1.00 94.44 ? 214 CYS A SG 1 ATOM 1449 N N . VAL A 1 188 ? -3.952 -18.394 1.973 1.00 68.10 ? 215 VAL A N 1 ATOM 1450 C CA . VAL A 1 188 ? -2.694 -18.967 2.427 1.00 63.87 ? 215 VAL A CA 1 ATOM 1451 C C . VAL A 1 188 ? -1.978 -19.693 1.290 1.00 67.71 ? 215 VAL A C 1 ATOM 1452 O O . VAL A 1 188 ? -2.569 -20.537 0.617 1.00 73.66 ? 215 VAL A O 1 ATOM 1453 C CB . VAL A 1 188 ? -2.931 -19.965 3.579 1.00 56.97 ? 215 VAL A CB 1 ATOM 1454 C CG1 . VAL A 1 188 ? -1.669 -20.726 3.902 1.00 52.73 ? 215 VAL A CG1 1 ATOM 1455 C CG2 . VAL A 1 188 ? -3.463 -19.255 4.802 1.00 66.29 ? 215 VAL A CG2 1 ATOM 1456 N N . ALA A 1 189 ? -0.717 -19.342 1.053 1.00 66.27 ? 216 ALA A N 1 ATOM 1457 C CA . ALA A 1 189 ? 0.063 -19.987 0.002 1.00 70.79 ? 216 ALA A CA 1 ATOM 1458 C C . ALA A 1 189 ? 1.188 -20.842 0.583 1.00 78.89 ? 216 ALA A C 1 ATOM 1459 O O . ALA A 1 189 ? 1.998 -20.369 1.386 1.00 82.40 ? 216 ALA A O 1 ATOM 1460 C CB . ALA A 1 189 ? 0.623 -18.945 -0.945 1.00 73.81 ? 216 ALA A CB 1 ATOM 1461 N N . THR A 1 190 ? 1.240 -22.097 0.147 1.00 78.50 ? 217 THR A N 1 ATOM 1462 C CA . THR A 1 190 ? 2.180 -23.070 0.690 1.00 77.82 ? 217 THR A CA 1 ATOM 1463 C C . THR A 1 190 ? 2.936 -23.844 -0.394 1.00 84.60 ? 217 THR A C 1 ATOM 1464 O O . THR A 1 190 ? 2.345 -24.298 -1.380 1.00 87.49 ? 217 THR A O 1 ATOM 1465 C CB . THR A 1 190 ? 1.455 -24.057 1.614 1.00 76.82 ? 217 THR A CB 1 ATOM 1466 O OG1 . THR A 1 190 ? 0.664 -23.325 2.558 1.00 77.48 ? 217 THR A OG1 1 ATOM 1467 C CG2 . THR A 1 190 ? 2.451 -24.913 2.373 1.00 78.16 ? 217 THR A CG2 1 ATOM 1468 N N . ASN A 1 191 ? 4.249 -23.958 -0.213 1.00 87.02 ? 218 ASN A N 1 ATOM 1469 C CA . ASN A 1 191 ? 5.046 -24.922 -0.956 1.00 83.77 ? 218 ASN A CA 1 ATOM 1470 C C . ASN A 1 191 ? 6.047 -25.615 -0.043 1.00 90.39 ? 218 ASN A C 1 ATOM 1471 O O . ASN A 1 191 ? 5.984 -25.479 1.178 1.00 90.20 ? 218 ASN A O 1 ATOM 1472 C CB . ASN A 1 191 ? 5.775 -24.255 -2.130 1.00 75.45 ? 218 ASN A CB 1 ATOM 1473 C CG . ASN A 1 191 ? 6.792 -23.203 -1.688 1.00 76.46 ? 218 ASN A CG 1 ATOM 1474 O OD1 . ASN A 1 191 ? 7.333 -23.255 -0.583 1.00 63.81 ? 218 ASN A OD1 1 ATOM 1475 N ND2 . ASN A 1 191 ? 7.060 -22.244 -2.566 1.00 80.89 ? 218 ASN A ND2 1 ATOM 1476 N N . SER A 1 192 ? 6.961 -26.363 -0.645 1.00 101.30 ? 219 SER A N 1 ATOM 1477 C CA . SER A 1 192 ? 7.920 -27.143 0.118 1.00 108.13 ? 219 SER A CA 1 ATOM 1478 C C . SER A 1 192 ? 8.879 -26.271 0.933 1.00 105.97 ? 219 SER A C 1 ATOM 1479 O O . SER A 1 192 ? 9.524 -26.758 1.862 1.00 104.73 ? 219 SER A O 1 ATOM 1480 C CB . SER A 1 192 ? 8.710 -28.056 -0.818 1.00 113.73 ? 219 SER A CB 1 ATOM 1481 O OG . SER A 1 192 ? 9.316 -27.316 -1.864 1.00 120.50 ? 219 SER A OG 1 ATOM 1482 N N . ALA A 1 193 ? 8.973 -24.987 0.594 1.00 98.58 ? 220 ALA A N 1 ATOM 1483 C CA . ALA A 1 193 ? 9.808 -24.060 1.354 1.00 88.48 ? 220 ALA A CA 1 ATOM 1484 C C . ALA A 1 193 ? 9.100 -23.514 2.589 1.00 88.59 ? 220 ALA A C 1 ATOM 1485 O O . ALA A 1 193 ? 9.742 -23.212 3.594 1.00 94.38 ? 220 ALA A O 1 ATOM 1486 C CB . ALA A 1 193 ? 10.269 -22.915 0.469 1.00 80.68 ? 220 ALA A CB 1 ATOM 1487 N N . GLY A 1 194 ? 7.779 -23.380 2.519 1.00 83.00 ? 221 GLY A N 1 ATOM 1488 C CA . GLY A 1 194 ? 7.028 -22.854 3.644 1.00 78.93 ? 221 GLY A CA 1 ATOM 1489 C C . GLY A 1 194 ? 5.670 -22.258 3.318 1.00 83.45 ? 221 GLY A C 1 ATOM 1490 O O . GLY A 1 194 ? 5.124 -22.466 2.236 1.00 88.80 ? 221 GLY A O 1 ATOM 1491 N N . THR A 1 195 ? 5.134 -21.505 4.276 1.00 84.79 ? 222 THR A N 1 ATOM 1492 C CA . THR A 1 195 ? 3.749 -21.046 4.250 1.00 80.06 ? 222 THR A CA 1 ATOM 1493 C C . THR A 1 195 ? 3.668 -19.535 4.495 1.00 75.51 ? 222 THR A C 1 ATOM 1494 O O . THR A 1 195 ? 4.343 -19.013 5.380 1.00 74.16 ? 222 THR A O 1 ATOM 1495 C CB . THR A 1 195 ? 2.906 -21.795 5.297 1.00 79.94 ? 222 THR A CB 1 ATOM 1496 O OG1 . THR A 1 195 ? 3.017 -23.208 5.080 1.00 82.70 ? 222 THR A OG1 1 ATOM 1497 C CG2 . THR A 1 195 ? 1.455 -21.397 5.208 1.00 74.91 ? 222 THR A CG2 1 ATOM 1498 N N . ARG A 1 196 ? 2.847 -18.840 3.707 1.00 82.51 ? 223 ARG A N 1 ATOM 1499 C CA . ARG A 1 196 ? 2.612 -17.402 3.885 1.00 83.39 ? 223 ARG A CA 1 ATOM 1500 C C . ARG A 1 196 ? 1.120 -17.040 3.870 1.00 88.59 ? 223 ARG A C 1 ATOM 1501 O O . ARG A 1 196 ? 0.360 -17.542 3.043 1.00 92.18 ? 223 ARG A O 1 ATOM 1502 C CB . ARG A 1 196 ? 3.351 -16.596 2.815 1.00 83.14 ? 223 ARG A CB 1 ATOM 1503 C CG . ARG A 1 196 ? 3.209 -15.093 2.994 1.00 85.94 ? 223 ARG A CG 1 ATOM 1504 C CD . ARG A 1 196 ? 3.894 -14.318 1.888 1.00 98.62 ? 223 ARG A CD 1 ATOM 1505 N NE . ARG A 1 196 ? 5.348 -14.440 1.941 1.00 107.92 ? 223 ARG A NE 1 ATOM 1506 C CZ . ARG A 1 196 ? 6.128 -13.695 2.717 1.00 111.40 ? 223 ARG A CZ 1 ATOM 1507 N NH1 . ARG A 1 196 ? 5.589 -12.782 3.515 1.00 111.81 ? 223 ARG A NH1 1 ATOM 1508 N NH2 . ARG A 1 196 ? 7.444 -13.864 2.703 1.00 112.51 ? 223 ARG A NH2 1 ATOM 1509 N N . TYR A 1 197 ? 0.711 -16.158 4.782 1.00 85.90 ? 224 TYR A N 1 ATOM 1510 C CA . TYR A 1 197 ? -0.675 -15.686 4.831 1.00 74.93 ? 224 TYR A CA 1 ATOM 1511 C C . TYR A 1 197 ? -0.871 -14.320 4.166 1.00 70.31 ? 224 TYR A C 1 ATOM 1512 O O . TYR A 1 197 ? 0.002 -13.454 4.221 1.00 74.12 ? 224 TYR A O 1 ATOM 1513 C CB . TYR A 1 197 ? -1.146 -15.610 6.290 1.00 69.37 ? 224 TYR A CB 1 ATOM 1514 C CG . TYR A 1 197 ? -1.460 -16.948 6.919 1.00 61.85 ? 224 TYR A CG 1 ATOM 1515 C CD1 . TYR A 1 197 ? -0.531 -17.978 6.912 1.00 59.25 ? 224 TYR A CD1 1 ATOM 1516 C CD2 . TYR A 1 197 ? -2.686 -17.174 7.531 1.00 58.48 ? 224 TYR A CD2 1 ATOM 1517 C CE1 . TYR A 1 197 ? -0.815 -19.196 7.481 1.00 56.77 ? 224 TYR A CE1 1 ATOM 1518 C CE2 . TYR A 1 197 ? -2.978 -18.391 8.107 1.00 55.11 ? 224 TYR A CE2 1 ATOM 1519 C CZ . TYR A 1 197 ? -2.037 -19.396 8.078 1.00 56.89 ? 224 TYR A CZ 1 ATOM 1520 O OH . TYR A 1 197 ? -2.322 -20.610 8.648 1.00 65.53 ? 224 TYR A OH 1 ATOM 1521 N N . SER A 1 198 ? -2.021 -14.147 3.521 1.00 62.51 ? 225 SER A N 1 ATOM 1522 C CA . SER A 1 198 ? -2.485 -12.826 3.112 1.00 67.19 ? 225 SER A CA 1 ATOM 1523 C C . SER A 1 198 ? -2.954 -12.002 4.301 1.00 70.27 ? 225 SER A C 1 ATOM 1524 O O . SER A 1 198 ? -3.197 -12.540 5.380 1.00 76.10 ? 225 SER A O 1 ATOM 1525 C CB . SER A 1 198 ? -3.619 -12.941 2.091 1.00 67.66 ? 225 SER A CB 1 ATOM 1526 O OG . SER A 1 198 ? -4.830 -13.326 2.720 1.00 59.41 ? 225 SER A OG 1 ATOM 1527 N N . ALA A 1 199 ? -3.097 -10.698 4.089 1.00 65.38 ? 226 ALA A N 1 ATOM 1528 C CA . ALA A 1 199 ? -3.852 -9.861 5.007 1.00 63.51 ? 226 ALA A CA 1 ATOM 1529 C C . ALA A 1 199 ? -5.290 -10.352 5.029 1.00 68.41 ? 226 ALA A C 1 ATOM 1530 O O . ALA A 1 199 ? -5.752 -10.941 4.053 1.00 74.26 ? 226 ALA A O 1 ATOM 1531 C CB . ALA A 1 199 ? -3.780 -8.400 4.598 1.00 63.00 ? 226 ALA A CB 1 ATOM 1532 N N . PRO A 1 200 ? -6.009 -10.114 6.139 1.00 69.14 ? 227 PRO A N 1 ATOM 1533 C CA . PRO A 1 200 ? -7.405 -10.554 6.148 1.00 68.39 ? 227 PRO A CA 1 ATOM 1534 C C . PRO A 1 200 ? -8.286 -9.629 5.319 1.00 77.35 ? 227 PRO A C 1 ATOM 1535 O O . PRO A 1 200 ? -7.954 -8.464 5.083 1.00 86.79 ? 227 PRO A O 1 ATOM 1536 C CB . PRO A 1 200 ? -7.782 -10.499 7.628 1.00 67.10 ? 227 PRO A CB 1 ATOM 1537 C CG . PRO A 1 200 ? -6.873 -9.487 8.208 1.00 69.63 ? 227 PRO A CG 1 ATOM 1538 C CD . PRO A 1 200 ? -5.573 -9.637 7.463 1.00 70.65 ? 227 PRO A CD 1 ATOM 1539 N N . ALA A 1 201 ? -9.414 -10.176 4.894 1.00 69.72 ? 228 ALA A N 1 ATOM 1540 C CA . ALA A 1 201 ? -10.396 -9.467 4.097 1.00 69.53 ? 228 ALA A CA 1 ATOM 1541 C C . ALA A 1 201 ? -11.776 -9.830 4.606 1.00 71.92 ? 228 ALA A C 1 ATOM 1542 O O . ALA A 1 201 ? -12.113 -11.002 4.688 1.00 76.39 ? 228 ALA A O 1 ATOM 1543 C CB . ALA A 1 201 ? -10.253 -9.814 2.634 1.00 65.90 ? 228 ALA A CB 1 ATOM 1544 N N . ASN A 1 202 ? -12.587 -8.833 4.931 1.00 69.29 ? 229 ASN A N 1 ATOM 1545 C CA . ASN A 1 202 ? -13.919 -9.159 5.409 1.00 69.75 ? 229 ASN A CA 1 ATOM 1546 C C . ASN A 1 202 ? -14.931 -9.282 4.279 1.00 69.21 ? 229 ASN A C 1 ATOM 1547 O O . ASN A 1 202 ? -14.899 -8.548 3.282 1.00 72.01 ? 229 ASN A O 1 ATOM 1548 C CB . ASN A 1 202 ? -14.395 -8.105 6.414 1.00 79.95 ? 229 ASN A CB 1 ATOM 1549 C CG . ASN A 1 202 ? -13.492 -8.011 7.627 1.00 85.54 ? 229 ASN A CG 1 ATOM 1550 O OD1 . ASN A 1 202 ? -13.012 -9.019 8.137 1.00 88.43 ? 229 ASN A OD1 1 ATOM 1551 N ND2 . ASN A 1 202 ? -13.267 -6.789 8.105 1.00 84.60 ? 229 ASN A ND2 1 ATOM 1552 N N . LEU A 1 203 ? -15.830 -10.242 4.468 1.00 59.35 ? 230 LEU A N 1 ATOM 1553 C CA . LEU A 1 203 ? -16.996 -10.438 3.627 1.00 55.00 ? 230 LEU A CA 1 ATOM 1554 C C . LEU A 1 203 ? -18.214 -10.015 4.425 1.00 64.49 ? 230 LEU A C 1 ATOM 1555 O O . LEU A 1 203 ? -18.430 -10.497 5.550 1.00 68.96 ? 230 LEU A O 1 ATOM 1556 C CB . LEU A 1 203 ? -17.115 -11.896 3.183 1.00 47.56 ? 230 LEU A CB 1 ATOM 1557 C CG . LEU A 1 203 ? -18.361 -12.250 2.372 1.00 56.03 ? 230 LEU A CG 1 ATOM 1558 C CD1 . LEU A 1 203 ? -18.377 -11.498 1.047 1.00 61.32 ? 230 LEU A CD1 1 ATOM 1559 C CD2 . LEU A 1 203 ? -18.462 -13.752 2.146 1.00 58.57 ? 230 LEU A CD2 1 ATOM 1560 N N . TYR A 1 204 ? -19.000 -9.133 3.804 1.00 64.48 ? 231 TYR A N 1 ATOM 1561 C CA . TYR A 1 204 ? -20.305 -8.675 4.280 1.00 57.79 ? 231 TYR A CA 1 ATOM 1562 C C . TYR A 1 204 ? -21.470 -9.136 3.428 1.00 60.59 ? 231 TYR A C 1 ATOM 1563 O O . TYR A 1 204 ? -21.369 -9.227 2.200 1.00 59.74 ? 231 TYR A O 1 ATOM 1564 C CB . TYR A 1 204 ? -20.372 -7.142 4.311 1.00 53.64 ? 231 TYR A CB 1 ATOM 1565 C CG . TYR A 1 204 ? -19.417 -6.462 5.248 1.00 58.38 ? 231 TYR A CG 1 ATOM 1566 C CD1 . TYR A 1 204 ? -19.772 -6.211 6.566 1.00 60.91 ? 231 TYR A CD1 1 ATOM 1567 C CD2 . TYR A 1 204 ? -18.179 -6.027 4.805 1.00 63.03 ? 231 TYR A CD2 1 ATOM 1568 C CE1 . TYR A 1 204 ? -18.906 -5.567 7.425 1.00 60.63 ? 231 TYR A CE1 1 ATOM 1569 C CE2 . TYR A 1 204 ? -17.304 -5.383 5.655 1.00 61.55 ? 231 TYR A CE2 1 ATOM 1570 C CZ . TYR A 1 204 ? -17.670 -5.155 6.963 1.00 57.79 ? 231 TYR A CZ 1 ATOM 1571 O OH . TYR A 1 204 ? -16.792 -4.512 7.804 1.00 57.26 ? 231 TYR A OH 1 ATOM 1572 N N . VAL A 1 205 ? -22.580 -9.421 4.101 1.00 61.59 ? 232 VAL A N 1 ATOM 1573 C CA . VAL A 1 205 ? -23.778 -9.885 3.431 1.00 60.84 ? 232 VAL A CA 1 ATOM 1574 C C . VAL A 1 205 ? -24.912 -8.910 3.693 1.00 67.25 ? 232 VAL A C 1 ATOM 1575 O O . VAL A 1 205 ? -25.394 -8.750 4.810 1.00 75.83 ? 232 VAL A O 1 ATOM 1576 C CB . VAL A 1 205 ? -24.186 -11.283 3.895 1.00 59.11 ? 232 VAL A CB 1 ATOM 1577 C CG1 . VAL A 1 205 ? -25.490 -11.691 3.242 1.00 55.58 ? 232 VAL A CG1 1 ATOM 1578 C CG2 . VAL A 1 205 ? -23.076 -12.279 3.567 1.00 66.15 ? 232 VAL A CG2 1 ATOM 1579 N N . ARG A 1 206 ? -25.337 -8.281 2.610 1.00 68.37 ? 233 ARG A N 1 ATOM 1580 C CA . ARG A 1 206 ? -26.303 -7.189 2.596 1.00 66.29 ? 233 ARG A CA 1 ATOM 1581 C C . ARG A 1 206 ? -27.602 -7.796 2.107 1.00 71.94 ? 233 ARG A C 1 ATOM 1582 O O . ARG A 1 206 ? -27.575 -8.751 1.329 1.00 66.24 ? 233 ARG A O 1 ATOM 1583 C CB . ARG A 1 206 ? -25.840 -6.018 1.735 1.00 67.88 ? 233 ARG A CB 1 ATOM 1584 C CG . ARG A 1 206 ? -25.673 -6.302 0.264 1.00 73.79 ? 233 ARG A CG 1 ATOM 1585 C CD . ARG A 1 206 ? -25.748 -4.999 -0.490 1.00 76.63 ? 233 ARG A CD 1 ATOM 1586 N NE . ARG A 1 206 ? -27.021 -4.337 -0.225 1.00 82.39 ? 233 ARG A NE 1 ATOM 1587 C CZ . ARG A 1 206 ? -27.331 -3.112 -0.637 1.00 86.86 ? 233 ARG A CZ 1 ATOM 1588 N NH1 . ARG A 1 206 ? -26.453 -2.405 -1.333 1.00 82.73 ? 233 ARG A NH1 1 ATOM 1589 N NH2 . ARG A 1 206 ? -28.520 -2.595 -0.349 1.00 87.06 ? 233 ARG A NH2 1 ATOM 1590 N N . GLU A 1 207 ? -28.740 -7.303 2.572 1.00 85.02 ? 234 GLU A N 1 ATOM 1591 C CA . GLU A 1 207 ? -29.998 -7.900 2.169 1.00 83.79 ? 234 GLU A CA 1 ATOM 1592 C C . GLU A 1 207 ? -30.327 -7.611 0.720 1.00 82.50 ? 234 GLU A C 1 ATOM 1593 O O . GLU A 1 207 ? -30.080 -6.520 0.207 1.00 84.21 ? 234 GLU A O 1 ATOM 1594 C CB . GLU A 1 207 ? -31.148 -7.357 3.030 1.00 89.50 ? 234 GLU A CB 1 ATOM 1595 C CG . GLU A 1 207 ? -31.158 -7.840 4.454 1.00 105.25 ? 234 GLU A CG 1 ATOM 1596 C CD . GLU A 1 207 ? -32.270 -8.834 4.702 1.00 118.57 ? 234 GLU A CD 1 ATOM 1597 O OE1 . GLU A 1 207 ? -32.675 -9.520 3.738 1.00 119.34 ? 234 GLU A OE1 1 ATOM 1598 O OE2 . GLU A 1 207 ? -32.748 -8.916 5.853 1.00 123.81 ? 234 GLU A OE2 1 ATOM 1599 N N . LEU A 1 208 ? -30.855 -8.642 0.066 1.00 81.81 ? 235 LEU A N 1 ATOM 1600 C CA . LEU A 1 208 ? -31.054 -8.644 -1.374 1.00 79.22 ? 235 LEU A CA 1 ATOM 1601 C C . LEU A 1 208 ? -31.881 -7.451 -1.821 1.00 86.31 ? 235 LEU A C 1 ATOM 1602 O O . LEU A 1 208 ? -32.963 -7.193 -1.294 1.00 92.21 ? 235 LEU A O 1 ATOM 1603 C CB . LEU A 1 208 ? -31.725 -9.942 -1.825 1.00 65.78 ? 235 LEU A CB 1 ATOM 1604 C CG . LEU A 1 208 ? -31.174 -10.612 -3.089 1.00 55.10 ? 235 LEU A CG 1 ATOM 1605 C CD1 . LEU A 1 208 ? -31.974 -11.859 -3.436 1.00 44.91 ? 235 LEU A CD1 1 ATOM 1606 C CD2 . LEU A 1 208 ? -31.129 -9.655 -4.276 1.00 50.37 ? 235 LEU A CD2 1 ATOM 1607 N N . ARG A 1 209 ? -31.352 -6.720 -2.794 1.00 85.62 ? 236 ARG A N 1 ATOM 1608 C CA . ARG A 1 209 ? -32.061 -5.593 -3.371 1.00 86.70 ? 236 ARG A CA 1 ATOM 1609 C C . ARG A 1 209 ? -32.719 -6.011 -4.672 1.00 98.76 ? 236 ARG A C 1 ATOM 1610 O O . ARG A 1 209 ? -32.043 -6.422 -5.614 1.00 100.75 ? 236 ARG A O 1 ATOM 1611 C CB . ARG A 1 209 ? -31.114 -4.427 -3.612 1.00 78.27 ? 236 ARG A CB 1 ATOM 1612 C CG . ARG A 1 209 ? -31.768 -3.253 -4.298 1.00 74.53 ? 236 ARG A CG 1 ATOM 1613 C CD . ARG A 1 209 ? -30.750 -2.173 -4.591 1.00 76.74 ? 236 ARG A CD 1 ATOM 1614 N NE . ARG A 1 209 ? -31.365 -1.030 -5.252 1.00 80.50 ? 236 ARG A NE 1 ATOM 1615 C CZ . ARG A 1 209 ? -31.645 -0.984 -6.549 1.00 82.28 ? 236 ARG A CZ 1 ATOM 1616 N NH1 . ARG A 1 209 ? -31.363 -2.022 -7.326 1.00 84.47 ? 236 ARG A NH1 1 ATOM 1617 N NH2 . ARG A 1 209 ? -32.209 0.097 -7.069 1.00 81.55 ? 236 ARG A NH2 1 ATOM 1618 N N . GLU A 1 210 ? -34.041 -5.904 -4.719 1.00 108.20 ? 237 GLU A N 1 ATOM 1619 C CA . GLU A 1 210 ? -34.789 -6.331 -5.890 1.00 120.74 ? 237 GLU A CA 1 ATOM 1620 C C . GLU A 1 210 ? -35.210 -5.144 -6.739 1.00 129.73 ? 237 GLU A C 1 ATOM 1621 O O . GLU A 1 210 ? -35.965 -4.278 -6.296 1.00 131.34 ? 237 GLU A O 1 ATOM 1622 C CB . GLU A 1 210 ? -36.006 -7.153 -5.469 1.00 121.03 ? 237 GLU A CB 1 ATOM 1623 C CG . GLU A 1 210 ? -35.628 -8.504 -4.883 1.00 119.05 ? 237 GLU A CG 1 ATOM 1624 C CD . GLU A 1 210 ? -36.817 -9.274 -4.351 1.00 115.86 ? 237 GLU A CD 1 ATOM 1625 O OE1 . GLU A 1 210 ? -37.927 -9.128 -4.908 1.00 119.57 ? 237 GLU A OE1 1 ATOM 1626 O OE2 . GLU A 1 210 ? -36.639 -10.028 -3.372 1.00 112.36 ? 237 GLU A OE2 1 ATOM 1627 N N . VAL A 1 211 ? -34.695 -5.116 -7.964 1.00 135.27 ? 238 VAL A N 1 ATOM 1628 C CA . VAL A 1 211 ? -34.968 -4.046 -8.911 1.00 138.47 ? 238 VAL A CA 1 ATOM 1629 C C . VAL A 1 211 ? -36.466 -3.907 -9.170 1.00 137.75 ? 238 VAL A C 1 ATOM 1630 O O . VAL A 1 211 ? -37.067 -4.709 -9.884 1.00 141.58 ? 238 VAL A O 1 ATOM 1631 C CB . VAL A 1 211 ? -34.219 -4.286 -10.240 1.00 150.16 ? 238 VAL A CB 1 ATOM 1632 C CG1 . VAL A 1 211 ? -32.761 -3.881 -10.101 1.00 150.28 ? 238 VAL A CG1 1 ATOM 1633 C CG2 . VAL A 1 211 ? -34.319 -5.749 -10.659 1.00 148.68 ? 238 VAL A CG2 1 ATOM 1634 N N . ARG A 1 212 ? -37.076 -2.890 -8.575 1.00 139.39 ? 239 ARG A N 1 ATOM 1635 C CA . ARG A 1 212 ? -38.514 -2.726 -8.710 1.00 133.79 ? 239 ARG A CA 1 ATOM 1636 C C . ARG A 1 212 ? -38.862 -2.188 -10.090 1.00 123.03 ? 239 ARG A C 1 ATOM 1637 O O . ARG A 1 212 ? -38.787 -0.985 -10.335 1.00 119.46 ? 239 ARG A O 1 ATOM 1638 C CB . ARG A 1 212 ? -39.068 -1.806 -7.620 1.00 132.98 ? 239 ARG A CB 1 ATOM 1639 C CG . ARG A 1 212 ? -40.527 -2.091 -7.297 1.00 133.53 ? 239 ARG A CG 1 ATOM 1640 C CD . ARG A 1 212 ? -40.742 -3.581 -7.044 1.00 133.27 ? 239 ARG A CD 1 ATOM 1641 N NE . ARG A 1 212 ? -40.965 -3.885 -5.632 1.00 129.73 ? 239 ARG A NE 1 ATOM 1642 C CZ . ARG A 1 212 ? -39.999 -3.995 -4.725 1.00 122.98 ? 239 ARG A CZ 1 ATOM 1643 N NH1 . ARG A 1 212 ? -38.732 -3.818 -5.072 1.00 124.87 ? 239 ARG A NH1 1 ATOM 1644 N NH2 . ARG A 1 212 ? -40.301 -4.275 -3.465 1.00 115.30 ? 239 ARG A NH2 1 ATOM 1645 N N . ARG A 1 213 ? -39.225 -3.094 -10.992 1.00 118.32 ? 240 ARG A N 1 ATOM 1646 C CA . ARG A 1 213 ? -39.693 -2.709 -12.317 1.00 113.08 ? 240 ARG A CA 1 ATOM 1647 C C . ARG A 1 213 ? -41.213 -2.618 -12.333 1.00 105.75 ? 240 ARG A C 1 ATOM 1648 O O . ARG A 1 213 ? -41.907 -3.512 -11.849 1.00 109.65 ? 240 ARG A O 1 ATOM 1649 C CB . ARG A 1 213 ? -39.212 -3.702 -13.378 1.00 114.25 ? 240 ARG A CB 1 ATOM 1650 C CG . ARG A 1 213 ? -37.726 -3.627 -13.677 1.00 115.81 ? 240 ARG A CG 1 ATOM 1651 C CD . ARG A 1 213 ? -37.369 -4.471 -14.890 1.00 118.84 ? 240 ARG A CD 1 ATOM 1652 N NE . ARG A 1 213 ? -35.998 -4.228 -15.331 1.00 124.83 ? 240 ARG A NE 1 ATOM 1653 C CZ . ARG A 1 213 ? -35.667 -3.440 -16.349 1.00 128.01 ? 240 ARG A CZ 1 ATOM 1654 N NH1 . ARG A 1 213 ? -36.607 -2.820 -17.049 1.00 127.72 ? 240 ARG A NH1 1 ATOM 1655 N NH2 . ARG A 1 213 ? -34.392 -3.278 -16.674 1.00 128.94 ? 240 ARG A NH2 1 ATOM 1656 N N . VAL A 1 214 ? -41.728 -1.523 -12.880 1.00 99.03 ? 241 VAL A N 1 ATOM 1657 C CA . VAL A 1 214 ? -43.167 -1.332 -12.977 1.00 95.45 ? 241 VAL A CA 1 ATOM 1658 C C . VAL A 1 214 ? -43.542 -0.865 -14.376 1.00 94.65 ? 241 VAL A C 1 ATOM 1659 O O . VAL A 1 214 ? -43.107 0.199 -14.817 1.00 91.83 ? 241 VAL A O 1 ATOM 1660 C CB . VAL A 1 214 ? -43.681 -0.311 -11.941 1.00 88.44 ? 241 VAL A CB 1 ATOM 1661 C CG1 . VAL A 1 214 ? -45.155 -0.021 -12.175 1.00 84.17 ? 241 VAL A CG1 1 ATOM 1662 C CG2 . VAL A 1 214 ? -43.450 -0.824 -10.524 1.00 85.69 ? 241 VAL A CG2 1 ATOM 1663 N N . PRO A 1 215 ? -44.344 -1.673 -15.085 1.00 94.14 ? 242 PRO A N 1 ATOM 1664 C CA . PRO A 1 215 ? -44.823 -1.313 -16.422 1.00 86.72 ? 242 PRO A CA 1 ATOM 1665 C C . PRO A 1 215 ? -45.569 0.014 -16.380 1.00 83.58 ? 242 PRO A C 1 ATOM 1666 O O . PRO A 1 215 ? -46.152 0.332 -15.343 1.00 81.82 ? 242 PRO A O 1 ATOM 1667 C CB . PRO A 1 215 ? -45.759 -2.469 -16.786 1.00 91.76 ? 242 PRO A CB 1 ATOM 1668 C CG . PRO A 1 215 ? -45.296 -3.614 -15.940 1.00 97.75 ? 242 PRO A CG 1 ATOM 1669 C CD . PRO A 1 215 ? -44.843 -2.990 -14.655 1.00 96.56 ? 242 PRO A CD 1 ATOM 1670 N N . PRO A 1 216 ? -45.543 0.780 -17.484 1.00 84.18 ? 243 PRO A N 1 ATOM 1671 C CA . PRO A 1 216 ? -46.123 2.129 -17.545 1.00 83.53 ? 243 PRO A CA 1 ATOM 1672 C C . PRO A 1 216 ? -47.582 2.196 -17.093 1.00 85.09 ? 243 PRO A C 1 ATOM 1673 O O . PRO A 1 216 ? -48.314 1.212 -17.192 1.00 81.24 ? 243 PRO A O 1 ATOM 1674 C CB . PRO A 1 216 ? -45.993 2.503 -19.030 1.00 77.96 ? 243 PRO A CB 1 ATOM 1675 C CG . PRO A 1 216 ? -45.732 1.219 -19.744 1.00 79.52 ? 243 PRO A CG 1 ATOM 1676 C CD . PRO A 1 216 ? -44.967 0.381 -18.777 1.00 83.12 ? 243 PRO A CD 1 ATOM 1677 N N . ARG A 1 217 ? -47.984 3.361 -16.596 1.00 90.13 ? 244 ARG A N 1 ATOM 1678 C CA . ARG A 1 217 ? -49.323 3.571 -16.057 1.00 92.94 ? 244 ARG A CA 1 ATOM 1679 C C . ARG A 1 217 ? -49.708 5.035 -16.215 1.00 91.43 ? 244 ARG A C 1 ATOM 1680 O O . ARG A 1 217 ? -48.934 5.923 -15.859 1.00 91.96 ? 244 ARG A O 1 ATOM 1681 C CB . ARG A 1 217 ? -49.384 3.154 -14.581 1.00 101.69 ? 244 ARG A CB 1 ATOM 1682 C CG . ARG A 1 217 ? -50.715 3.422 -13.881 1.00 105.76 ? 244 ARG A CG 1 ATOM 1683 C CD . ARG A 1 217 ? -50.595 3.204 -12.372 1.00 112.43 ? 244 ARG A CD 1 ATOM 1684 N NE . ARG A 1 217 ? -51.882 3.287 -11.682 1.00 119.94 ? 244 ARG A NE 1 ATOM 1685 C CZ . ARG A 1 217 ? -52.042 3.091 -10.375 1.00 122.50 ? 244 ARG A CZ 1 ATOM 1686 N NH1 . ARG A 1 217 ? -50.995 2.802 -9.614 1.00 126.38 ? 244 ARG A NH1 1 ATOM 1687 N NH2 . ARG A 1 217 ? -53.247 3.182 -9.828 1.00 118.37 ? 244 ARG A NH2 1 ATOM 1688 N N . PHE A 1 218 ? -50.896 5.292 -16.752 1.00 93.84 ? 245 PHE A N 1 ATOM 1689 C CA . PHE A 1 218 ? -51.338 6.667 -16.948 1.00 94.99 ? 245 PHE A CA 1 ATOM 1690 C C . PHE A 1 218 ? -51.685 7.326 -15.624 1.00 91.40 ? 245 PHE A C 1 ATOM 1691 O O . PHE A 1 218 ? -52.817 7.231 -15.149 1.00 91.77 ? 245 PHE A O 1 ATOM 1692 C CB . PHE A 1 218 ? -52.535 6.727 -17.899 1.00 96.29 ? 245 PHE A CB 1 ATOM 1693 C CG . PHE A 1 218 ? -52.160 6.582 -19.344 1.00 94.86 ? 245 PHE A CG 1 ATOM 1694 C CD1 . PHE A 1 218 ? -51.424 7.568 -19.980 1.00 93.87 ? 245 PHE A CD1 1 ATOM 1695 C CD2 . PHE A 1 218 ? -52.541 5.464 -20.067 1.00 96.36 ? 245 PHE A CD2 1 ATOM 1696 C CE1 . PHE A 1 218 ? -51.071 7.442 -21.309 1.00 94.15 ? 245 PHE A CE1 1 ATOM 1697 C CE2 . PHE A 1 218 ? -52.192 5.333 -21.399 1.00 100.05 ? 245 PHE A CE2 1 ATOM 1698 C CZ . PHE A 1 218 ? -51.456 6.324 -22.020 1.00 97.82 ? 245 PHE A CZ 1 ATOM 1699 N N . SER A 1 219 ? -50.691 7.984 -15.034 1.00 86.37 ? 246 SER A N 1 ATOM 1700 C CA . SER A 1 219 ? -50.886 8.763 -13.820 1.00 80.60 ? 246 SER A CA 1 ATOM 1701 C C . SER A 1 219 ? -51.954 9.828 -14.036 1.00 78.35 ? 246 SER A C 1 ATOM 1702 O O . SER A 1 219 ? -52.888 9.953 -13.246 1.00 78.77 ? 246 SER A O 1 ATOM 1703 C CB . SER A 1 219 ? -49.571 9.406 -13.383 1.00 88.40 ? 246 SER A CB 1 ATOM 1704 O OG . SER A 1 219 ? -49.808 10.519 -12.540 1.00 101.37 ? 246 SER A OG 1 ATOM 1705 N N . ILE A 1 220 ? -51.809 10.598 -15.110 1.00 78.05 ? 247 ILE A N 1 ATOM 1706 C CA . ILE A 1 220 ? -52.853 11.536 -15.504 1.00 76.31 ? 247 ILE A CA 1 ATOM 1707 C C . ILE A 1 220 ? -53.275 11.246 -16.941 1.00 79.93 ? 247 ILE A C 1 ATOM 1708 O O . ILE A 1 220 ? -52.715 11.800 -17.890 1.00 79.76 ? 247 ILE A O 1 ATOM 1709 C CB . ILE A 1 220 ? -52.400 13.003 -15.367 1.00 73.10 ? 247 ILE A CB 1 ATOM 1710 C CG1 . ILE A 1 220 ? -51.953 13.291 -13.930 1.00 77.76 ? 247 ILE A CG1 1 ATOM 1711 C CG2 . ILE A 1 220 ? -53.525 13.946 -15.753 1.00 72.93 ? 247 ILE A CG2 1 ATOM 1712 C CD1 . ILE A 1 220 ? -51.548 14.736 -13.691 1.00 86.82 ? 247 ILE A CD1 1 ATOM 1713 N N . PRO A 1 221 ? -54.250 10.342 -17.101 1.00 84.46 ? 248 PRO A N 1 ATOM 1714 C CA . PRO A 1 221 ? -54.825 10.039 -18.412 1.00 94.26 ? 248 PRO A CA 1 ATOM 1715 C C . PRO A 1 221 ? -55.528 11.267 -18.963 1.00 104.79 ? 248 PRO A C 1 ATOM 1716 O O . PRO A 1 221 ? -56.203 11.961 -18.203 1.00 105.54 ? 248 PRO A O 1 ATOM 1717 C CB . PRO A 1 221 ? -55.818 8.912 -18.114 1.00 91.00 ? 248 PRO A CB 1 ATOM 1718 C CG . PRO A 1 221 ? -56.155 9.082 -16.675 1.00 86.21 ? 248 PRO A CG 1 ATOM 1719 C CD . PRO A 1 221 ? -54.901 9.578 -16.024 1.00 84.27 ? 248 PRO A CD 1 ATOM 1720 N N . PRO A 1 222 ? -55.359 11.544 -20.263 1.00 112.36 ? 249 PRO A N 1 ATOM 1721 C CA . PRO A 1 222 ? -55.974 12.733 -20.858 1.00 112.90 ? 249 PRO A CA 1 ATOM 1722 C C . PRO A 1 222 ? -57.494 12.680 -20.758 1.00 112.45 ? 249 PRO A C 1 ATOM 1723 O O . PRO A 1 222 ? -58.093 11.632 -21.005 1.00 107.86 ? 249 PRO A O 1 ATOM 1724 C CB . PRO A 1 222 ? -55.510 12.680 -22.319 1.00 113.77 ? 249 PRO A CB 1 ATOM 1725 C CG . PRO A 1 222 ? -55.197 11.239 -22.567 1.00 113.52 ? 249 PRO A CG 1 ATOM 1726 C CD . PRO A 1 222 ? -54.664 10.717 -21.263 1.00 112.99 ? 249 PRO A CD 1 ATOM 1727 N N . THR A 1 223 ? -58.106 13.794 -20.374 1.00 120.07 ? 250 THR A N 1 ATOM 1728 C CA . THR A 1 223 ? -59.558 13.868 -20.291 1.00 122.70 ? 250 THR A CA 1 ATOM 1729 C C . THR A 1 223 ? -60.118 14.656 -21.467 1.00 120.73 ? 250 THR A C 1 ATOM 1730 O O . THR A 1 223 ? -59.494 15.595 -21.957 1.00 119.26 ? 250 THR A O 1 ATOM 1731 C CB . THR A 1 223 ? -60.024 14.509 -18.976 1.00 127.39 ? 250 THR A CB 1 ATOM 1732 O OG1 . THR A 1 223 ? -59.380 15.777 -18.808 1.00 128.42 ? 250 THR A OG1 1 ATOM 1733 C CG2 . THR A 1 223 ? -59.689 13.606 -17.795 1.00 130.88 ? 250 THR A CG2 1 ATOM 1734 N N . ASN A 1 224 ? -61.306 14.261 -21.908 1.00 120.82 ? 251 ASN A N 1 ATOM 1735 C CA . ASN A 1 224 ? -61.914 14.792 -23.120 1.00 118.78 ? 251 ASN A CA 1 ATOM 1736 C C . ASN A 1 224 ? -62.421 16.226 -22.971 1.00 118.37 ? 251 ASN A C 1 ATOM 1737 O O . ASN A 1 224 ? -62.780 16.658 -21.877 1.00 119.22 ? 251 ASN A O 1 ATOM 1738 C CB . ASN A 1 224 ? -63.052 13.869 -23.542 1.00 120.84 ? 251 ASN A CB 1 ATOM 1739 C CG . ASN A 1 224 ? -62.716 12.404 -23.324 1.00 124.98 ? 251 ASN A CG 1 ATOM 1740 O OD1 . ASN A 1 224 ? -62.090 11.764 -24.168 1.00 122.85 ? 251 ASN A OD1 1 ATOM 1741 N ND2 . ASN A 1 224 ? -63.118 11.871 -22.176 1.00 129.58 ? 251 ASN A ND2 1 ATOM 1742 N N . HIS A 1 225 ? -62.449 16.963 -24.077 1.00 121.14 ? 252 HIS A N 1 ATOM 1743 C CA . HIS A 1 225 ? -62.867 18.360 -24.050 1.00 124.44 ? 252 HIS A CA 1 ATOM 1744 C C . HIS A 1 225 ? -63.780 18.702 -25.217 1.00 139.12 ? 252 HIS A C 1 ATOM 1745 O O . HIS A 1 225 ? -63.690 18.101 -26.286 1.00 140.37 ? 252 HIS A O 1 ATOM 1746 C CB . HIS A 1 225 ? -61.647 19.282 -24.070 1.00 118.62 ? 252 HIS A CB 1 ATOM 1747 C CG . HIS A 1 225 ? -60.796 19.189 -22.842 1.00 128.51 ? 252 HIS A CG 1 ATOM 1748 N ND1 . HIS A 1 225 ? -61.292 18.793 -21.619 1.00 134.94 ? 252 HIS A ND1 1 ATOM 1749 C CD2 . HIS A 1 225 ? -59.479 19.439 -22.650 1.00 133.29 ? 252 HIS A CD2 1 ATOM 1750 C CE1 . HIS A 1 225 ? -60.318 18.806 -20.726 1.00 135.51 ? 252 HIS A CE1 1 ATOM 1751 N NE2 . HIS A 1 225 ? -59.208 19.196 -21.326 1.00 135.14 ? 252 HIS A NE2 1 ATOM 1752 N N . GLU A 1 226 ? -64.660 19.674 -25.008 1.00 148.48 ? 253 GLU A N 1 ATOM 1753 C CA . GLU A 1 226 ? -65.473 20.204 -26.091 1.00 152.36 ? 253 GLU A CA 1 ATOM 1754 C C . GLU A 1 226 ? -65.430 21.731 -26.040 1.00 151.91 ? 253 GLU A C 1 ATOM 1755 O O . GLU A 1 226 ? -65.610 22.330 -24.978 1.00 152.99 ? 253 GLU A O 1 ATOM 1756 C CB . GLU A 1 226 ? -66.910 19.671 -26.013 1.00 152.03 ? 253 GLU A CB 1 ATOM 1757 C CG . GLU A 1 226 ? -67.730 20.135 -24.831 1.00 151.60 ? 253 GLU A CG 1 ATOM 1758 C CD . GLU A 1 226 ? -68.776 21.149 -25.235 1.00 152.88 ? 253 GLU A CD 1 ATOM 1759 O OE1 . GLU A 1 226 ? -68.392 22.250 -25.675 1.00 155.57 ? 253 GLU A OE1 1 ATOM 1760 O OE2 . GLU A 1 226 ? -69.980 20.838 -25.126 1.00 151.69 ? 253 GLU A OE2 1 ATOM 1761 N N . ILE A 1 227 ? -65.153 22.357 -27.181 1.00 140.30 ? 254 ILE A N 1 ATOM 1762 C CA . ILE A 1 227 ? -64.959 23.805 -27.218 1.00 130.21 ? 254 ILE A CA 1 ATOM 1763 C C . ILE A 1 227 ? -65.522 24.455 -28.483 1.00 128.02 ? 254 ILE A C 1 ATOM 1764 O O . ILE A 1 227 ? -65.943 23.773 -29.418 1.00 128.51 ? 254 ILE A O 1 ATOM 1765 C CB . ILE A 1 227 ? -63.459 24.167 -27.099 1.00 121.01 ? 254 ILE A CB 1 ATOM 1766 C CG1 . ILE A 1 227 ? -62.608 23.224 -27.947 1.00 115.12 ? 254 ILE A CG1 1 ATOM 1767 C CG2 . ILE A 1 227 ? -63.003 24.117 -25.648 1.00 119.75 ? 254 ILE A CG2 1 ATOM 1768 C CD1 . ILE A 1 227 ? -62.443 23.671 -29.372 1.00 116.58 ? 254 ILE A CD1 1 ATOM 1769 N N . MET A 1 228 ? -65.518 25.784 -28.497 1.00 126.27 ? 255 MET A N 1 ATOM 1770 C CA . MET A 1 228 ? -65.968 26.557 -29.650 1.00 126.57 ? 255 MET A CA 1 ATOM 1771 C C . MET A 1 228 ? -64.850 26.678 -30.686 1.00 115.67 ? 255 MET A C 1 ATOM 1772 O O . MET A 1 228 ? -63.673 26.657 -30.327 1.00 116.20 ? 255 MET A O 1 ATOM 1773 C CB . MET A 1 228 ? -66.441 27.946 -29.210 1.00 139.11 ? 255 MET A CB 1 ATOM 1774 C CG . MET A 1 228 ? -67.732 27.942 -28.403 1.00 145.12 ? 255 MET A CG 1 ATOM 1775 S SD . MET A 1 228 ? -68.232 29.593 -27.878 1.00 212.19 ? 255 MET A SD 1 ATOM 1776 C CE . MET A 1 228 ? -66.759 30.122 -27.008 1.00 128.16 ? 255 MET A CE 1 ATOM 1777 N N . PRO A 1 229 ? -65.217 26.804 -31.974 1.00 111.51 ? 256 PRO A N 1 ATOM 1778 C CA . PRO A 1 229 ? -64.253 26.883 -33.080 1.00 113.77 ? 256 PRO A CA 1 ATOM 1779 C C . PRO A 1 229 ? -63.133 27.901 -32.869 1.00 117.42 ? 256 PRO A C 1 ATOM 1780 O O . PRO A 1 229 ? -63.393 29.104 -32.840 1.00 121.18 ? 256 PRO A O 1 ATOM 1781 C CB . PRO A 1 229 ? -65.126 27.296 -34.266 1.00 114.59 ? 256 PRO A CB 1 ATOM 1782 C CG . PRO A 1 229 ? -66.454 26.722 -33.955 1.00 112.01 ? 256 PRO A CG 1 ATOM 1783 C CD . PRO A 1 229 ? -66.608 26.818 -32.463 1.00 110.17 ? 256 PRO A CD 1 ATOM 1784 N N . GLY A 1 230 ? -61.908 27.403 -32.726 1.00 114.11 ? 257 GLY A N 1 ATOM 1785 C CA . GLY A 1 230 ? -60.717 28.231 -32.615 1.00 112.46 ? 257 GLY A CA 1 ATOM 1786 C C . GLY A 1 230 ? -60.761 29.381 -31.625 1.00 115.40 ? 257 GLY A C 1 ATOM 1787 O O . GLY A 1 230 ? -60.855 30.540 -32.031 1.00 117.39 ? 257 GLY A O 1 ATOM 1788 N N . GLY A 1 231 ? -60.695 29.074 -30.332 1.00 116.20 ? 258 GLY A N 1 ATOM 1789 C CA . GLY A 1 231 ? -60.655 27.704 -29.858 1.00 114.07 ? 258 GLY A CA 1 ATOM 1790 C C . GLY A 1 231 ? -59.264 27.174 -29.580 1.00 113.99 ? 258 GLY A C 1 ATOM 1791 O O . GLY A 1 231 ? -58.619 26.603 -30.457 1.00 112.85 ? 258 GLY A O 1 ATOM 1792 N N . SER A 1 232 ? -58.802 27.366 -28.350 1.00 118.51 ? 259 SER A N 1 ATOM 1793 C CA . SER A 1 232 ? -57.557 26.762 -27.895 1.00 120.91 ? 259 SER A CA 1 ATOM 1794 C C . SER A 1 232 ? -57.841 25.839 -26.715 1.00 127.48 ? 259 SER A C 1 ATOM 1795 O O . SER A 1 232 ? -58.920 25.905 -26.124 1.00 133.41 ? 259 SER A O 1 ATOM 1796 C CB . SER A 1 232 ? -56.537 27.834 -27.508 1.00 121.84 ? 259 SER A CB 1 ATOM 1797 O OG . SER A 1 232 ? -56.126 28.575 -28.644 1.00 123.64 ? 259 SER A OG 1 ATOM 1798 N N . VAL A 1 233 ? -56.876 24.983 -26.382 1.00 131.77 ? 260 VAL A N 1 ATOM 1799 C CA . VAL A 1 233 ? -57.009 24.049 -25.263 1.00 132.14 ? 260 VAL A CA 1 ATOM 1800 C C . VAL A 1 233 ? -55.688 23.318 -24.988 1.00 127.83 ? 260 VAL A C 1 ATOM 1801 O O . VAL A 1 233 ? -54.968 22.943 -25.915 1.00 125.72 ? 260 VAL A O 1 ATOM 1802 C CB . VAL A 1 233 ? -58.138 23.010 -25.519 1.00 104.77 ? 260 VAL A CB 1 ATOM 1803 C CG1 . VAL A 1 233 ? -57.817 22.133 -26.723 1.00 106.52 ? 260 VAL A CG1 1 ATOM 1804 C CG2 . VAL A 1 233 ? -58.392 22.171 -24.279 1.00 102.91 ? 260 VAL A CG2 1 ATOM 1805 N N . ASN A 1 234 ? -55.364 23.145 -23.708 1.00 124.11 ? 261 ASN A N 1 ATOM 1806 C CA . ASN A 1 234 ? -54.174 22.404 -23.294 1.00 122.09 ? 261 ASN A CA 1 ATOM 1807 C C . ASN A 1 234 ? -54.541 21.072 -22.655 1.00 123.88 ? 261 ASN A C 1 ATOM 1808 O O . ASN A 1 234 ? -55.015 21.042 -21.521 1.00 126.17 ? 261 ASN A O 1 ATOM 1809 C CB . ASN A 1 234 ? -53.342 23.214 -22.294 1.00 123.08 ? 261 ASN A CB 1 ATOM 1810 C CG . ASN A 1 234 ? -52.633 24.398 -22.925 1.00 124.77 ? 261 ASN A CG 1 ATOM 1811 O OD1 . ASN A 1 234 ? -52.338 24.405 -24.121 1.00 131.19 ? 261 ASN A OD1 1 ATOM 1812 N ND2 . ASN A 1 234 ? -52.349 25.412 -22.104 1.00 120.10 ? 261 ASN A ND2 1 ATOM 1813 N N . ILE A 1 235 ? -54.320 19.970 -23.362 1.00 122.55 ? 262 ILE A N 1 ATOM 1814 C CA . ILE A 1 235 ? -54.640 18.668 -22.781 1.00 112.84 ? 262 ILE A CA 1 ATOM 1815 C C . ILE A 1 235 ? -53.368 18.025 -22.239 1.00 103.18 ? 262 ILE A C 1 ATOM 1816 O O . ILE A 1 235 ? -52.345 18.022 -22.903 1.00 104.46 ? 262 ILE A O 1 ATOM 1817 C CB . ILE A 1 235 ? -55.329 17.734 -23.805 1.00 112.84 ? 262 ILE A CB 1 ATOM 1818 C CG1 . ILE A 1 235 ? -55.536 16.341 -23.206 1.00 124.15 ? 262 ILE A CG1 1 ATOM 1819 C CG2 . ILE A 1 235 ? -54.538 17.667 -25.102 1.00 103.11 ? 262 ILE A CG2 1 ATOM 1820 C CD1 . ILE A 1 235 ? -56.372 16.334 -21.939 1.00 130.46 ? 262 ILE A CD1 1 ATOM 1821 N N . THR A 1 236 ? -53.419 17.497 -21.023 1.00 96.50 ? 263 THR A N 1 ATOM 1822 C CA . THR A 1 236 ? -52.202 16.998 -20.391 1.00 93.08 ? 263 THR A CA 1 ATOM 1823 C C . THR A 1 236 ? -52.199 15.478 -20.221 1.00 96.48 ? 263 THR A C 1 ATOM 1824 O O . THR A 1 236 ? -53.218 14.878 -19.876 1.00 105.00 ? 263 THR A O 1 ATOM 1825 C CB . THR A 1 236 ? -51.990 17.663 -19.024 1.00 93.05 ? 263 THR A CB 1 ATOM 1826 O OG1 . THR A 1 236 ? -52.070 19.086 -19.172 1.00 93.48 ? 263 THR A OG1 1 ATOM 1827 C CG2 . THR A 1 236 ? -50.631 17.298 -18.455 1.00 94.58 ? 263 THR A CG2 1 ATOM 1828 N N . CYS A 1 237 ? -51.042 14.867 -20.472 1.00 89.07 ? 264 CYS A N 1 ATOM 1829 C CA . CYS A 1 237 ? -50.867 13.422 -20.347 1.00 88.17 ? 264 CYS A CA 1 ATOM 1830 C C . CYS A 1 237 ? -49.685 13.099 -19.434 1.00 90.74 ? 264 CYS A C 1 ATOM 1831 O O . CYS A 1 237 ? -48.605 13.661 -19.600 1.00 101.13 ? 264 CYS A O 1 ATOM 1832 C CB . CYS A 1 237 ? -50.658 12.793 -21.728 1.00 91.25 ? 264 CYS A CB 1 ATOM 1833 S SG . CYS A 1 237 ? -50.555 10.988 -21.749 1.00 84.72 ? 264 CYS A SG 1 ATOM 1834 N N . VAL A 1 238 ? -49.888 12.205 -18.467 1.00 85.72 ? 265 VAL A N 1 ATOM 1835 C CA . VAL A 1 238 ? -48.812 11.820 -17.546 1.00 84.55 ? 265 VAL A CA 1 ATOM 1836 C C . VAL A 1 238 ? -48.714 10.312 -17.308 1.00 88.85 ? 265 VAL A C 1 ATOM 1837 O O . VAL A 1 238 ? -49.691 9.668 -16.912 1.00 88.59 ? 265 VAL A O 1 ATOM 1838 C CB . VAL A 1 238 ? -48.967 12.495 -16.170 1.00 86.71 ? 265 VAL A CB 1 ATOM 1839 C CG1 . VAL A 1 238 ? -47.866 12.027 -15.229 1.00 87.90 ? 265 VAL A CG1 1 ATOM 1840 C CG2 . VAL A 1 238 ? -48.943 14.009 -16.305 1.00 90.65 ? 265 VAL A CG2 1 ATOM 1841 N N . ALA A 1 239 ? -47.516 9.773 -17.525 1.00 96.60 ? 266 ALA A N 1 ATOM 1842 C CA . ALA A 1 239 ? -47.232 8.352 -17.329 1.00 99.09 ? 266 ALA A CA 1 ATOM 1843 C C . ALA A 1 239 ? -46.160 8.116 -16.263 1.00 101.78 ? 266 ALA A C 1 ATOM 1844 O O . ALA A 1 239 ? -45.265 8.940 -16.074 1.00 99.23 ? 266 ALA A O 1 ATOM 1845 C CB . ALA A 1 239 ? -46.802 7.726 -18.635 1.00 96.11 ? 266 ALA A CB 1 ATOM 1846 N N . VAL A 1 240 ? -46.252 6.981 -15.574 1.00 105.33 ? 267 VAL A N 1 ATOM 1847 C CA . VAL A 1 240 ? -45.290 6.627 -14.532 1.00 99.73 ? 267 VAL A CA 1 ATOM 1848 C C . VAL A 1 240 ? -44.882 5.160 -14.623 1.00 100.05 ? 267 VAL A C 1 ATOM 1849 O O . VAL A 1 240 ? -45.585 4.350 -15.226 1.00 101.16 ? 267 VAL A O 1 ATOM 1850 C CB . VAL A 1 240 ? -45.855 6.891 -13.129 1.00 83.84 ? 267 VAL A CB 1 ATOM 1851 C CG1 . VAL A 1 240 ? -46.021 8.382 -12.893 1.00 89.88 ? 267 VAL A CG1 1 ATOM 1852 C CG2 . VAL A 1 240 ? -47.176 6.161 -12.949 1.00 67.85 ? 267 VAL A CG2 1 ATOM 1853 N N . GLY A 1 241 ? -43.748 4.820 -14.018 1.00 95.56 ? 268 GLY A N 1 ATOM 1854 C CA . GLY A 1 241 ? -43.281 3.446 -14.002 1.00 90.27 ? 268 GLY A CA 1 ATOM 1855 C C . GLY A 1 241 ? -41.769 3.337 -14.053 1.00 82.46 ? 268 GLY A C 1 ATOM 1856 O O . GLY A 1 241 ? -41.076 4.328 -14.280 1.00 82.33 ? 268 GLY A O 1 ATOM 1857 N N . SER A 1 242 ? -41.257 2.129 -13.841 1.00 80.29 ? 269 SER A N 1 ATOM 1858 C CA . SER A 1 242 ? -39.819 1.893 -13.850 1.00 80.42 ? 269 SER A CA 1 ATOM 1859 C C . SER A 1 242 ? -39.447 0.881 -14.927 1.00 86.83 ? 269 SER A C 1 ATOM 1860 O O . SER A 1 242 ? -39.899 -0.260 -14.879 1.00 90.37 ? 269 SER A O 1 ATOM 1861 C CB . SER A 1 242 ? -39.350 1.398 -12.485 1.00 81.48 ? 269 SER A CB 1 ATOM 1862 O OG . SER A 1 242 ? -40.199 1.882 -11.461 1.00 86.66 ? 269 SER A OG 1 ATOM 1863 N N . PRO A 1 243 ? -38.625 1.291 -15.909 1.00 90.40 ? 270 PRO A N 1 ATOM 1864 C CA . PRO A 1 243 ? -38.074 2.642 -16.083 1.00 92.85 ? 270 PRO A CA 1 ATOM 1865 C C . PRO A 1 243 ? -39.125 3.674 -16.490 1.00 97.19 ? 270 PRO A C 1 ATOM 1866 O O . PRO A 1 243 ? -40.205 3.308 -16.957 1.00 99.58 ? 270 PRO A O 1 ATOM 1867 C CB . PRO A 1 243 ? -37.039 2.455 -17.199 1.00 90.97 ? 270 PRO A CB 1 ATOM 1868 C CG . PRO A 1 243 ? -37.498 1.249 -17.945 1.00 87.30 ? 270 PRO A CG 1 ATOM 1869 C CD . PRO A 1 243 ? -38.087 0.348 -16.905 1.00 90.05 ? 270 PRO A CD 1 ATOM 1870 N N . MET A 1 244 ? -38.806 4.948 -16.283 1.00 100.72 ? 271 MET A N 1 ATOM 1871 C CA . MET A 1 244 ? -39.713 6.041 -16.608 1.00 94.90 ? 271 MET A CA 1 ATOM 1872 C C . MET A 1 244 ? -40.008 6.042 -18.105 1.00 88.84 ? 271 MET A C 1 ATOM 1873 O O . MET A 1 244 ? -39.097 5.888 -18.918 1.00 90.25 ? 271 MET A O 1 ATOM 1874 C CB . MET A 1 244 ? -39.112 7.379 -16.170 1.00 95.75 ? 271 MET A CB 1 ATOM 1875 C CG . MET A 1 244 ? -40.125 8.403 -15.689 1.00 93.93 ? 271 MET A CG 1 ATOM 1876 S SD . MET A 1 244 ? -40.949 7.949 -14.153 1.00 135.06 ? 271 MET A SD 1 ATOM 1877 C CE . MET A 1 244 ? -42.015 9.372 -13.930 1.00 112.43 ? 271 MET A CE 1 ATOM 1878 N N . PRO A 1 245 ? -41.289 6.203 -18.473 1.00 81.70 ? 272 PRO A N 1 ATOM 1879 C CA . PRO A 1 245 ? -41.722 6.076 -19.869 1.00 86.91 ? 272 PRO A CA 1 ATOM 1880 C C . PRO A 1 245 ? -41.751 7.386 -20.659 1.00 89.77 ? 272 PRO A C 1 ATOM 1881 O O . PRO A 1 245 ? -42.148 8.426 -20.132 1.00 90.22 ? 272 PRO A O 1 ATOM 1882 C CB . PRO A 1 245 ? -43.138 5.509 -19.734 1.00 84.34 ? 272 PRO A CB 1 ATOM 1883 C CG . PRO A 1 245 ? -43.605 5.921 -18.347 1.00 81.64 ? 272 PRO A CG 1 ATOM 1884 C CD . PRO A 1 245 ? -42.427 6.466 -17.577 1.00 78.28 ? 272 PRO A CD 1 ATOM 1885 N N . TYR A 1 246 ? -41.338 7.318 -21.922 1.00 88.67 ? 273 TYR A N 1 ATOM 1886 C CA . TYR A 1 246 ? -41.438 8.458 -22.828 1.00 87.46 ? 273 TYR A CA 1 ATOM 1887 C C . TYR A 1 246 ? -42.888 8.658 -23.257 1.00 88.98 ? 273 TYR A C 1 ATOM 1888 O O . TYR A 1 246 ? -43.621 7.687 -23.460 1.00 91.66 ? 273 TYR A O 1 ATOM 1889 C CB . TYR A 1 246 ? -40.546 8.264 -24.057 1.00 84.22 ? 273 TYR A CB 1 ATOM 1890 C CG . TYR A 1 246 ? -39.075 8.531 -23.818 1.00 80.58 ? 273 TYR A CG 1 ATOM 1891 C CD1 . TYR A 1 246 ? -38.556 9.816 -23.924 1.00 81.42 ? 273 TYR A CD1 1 ATOM 1892 C CD2 . TYR A 1 246 ? -38.202 7.496 -23.504 1.00 78.88 ? 273 TYR A CD2 1 ATOM 1893 C CE1 . TYR A 1 246 ? -37.212 10.064 -23.716 1.00 82.71 ? 273 TYR A CE1 1 ATOM 1894 C CE2 . TYR A 1 246 ? -36.857 7.735 -23.292 1.00 80.80 ? 273 TYR A CE2 1 ATOM 1895 C CZ . TYR A 1 246 ? -36.368 9.020 -23.398 1.00 84.91 ? 273 TYR A CZ 1 ATOM 1896 O OH . TYR A 1 246 ? -35.030 9.264 -23.186 1.00 93.80 ? 273 TYR A OH 1 ATOM 1897 N N . VAL A 1 247 ? -43.298 9.916 -23.397 1.00 82.63 ? 274 VAL A N 1 ATOM 1898 C CA . VAL A 1 247 ? -44.684 10.228 -23.727 1.00 74.67 ? 274 VAL A CA 1 ATOM 1899 C C . VAL A 1 247 ? -44.805 11.070 -24.999 1.00 76.35 ? 274 VAL A C 1 ATOM 1900 O O . VAL A 1 247 ? -44.305 12.194 -25.060 1.00 81.51 ? 274 VAL A O 1 ATOM 1901 C CB . VAL A 1 247 ? -45.380 10.977 -22.571 1.00 65.39 ? 274 VAL A CB 1 ATOM 1902 C CG1 . VAL A 1 247 ? -46.879 11.022 -22.803 1.00 62.88 ? 274 VAL A CG1 1 ATOM 1903 C CG2 . VAL A 1 247 ? -45.068 10.315 -21.234 1.00 60.42 ? 274 VAL A CG2 1 ATOM 1904 N N . LYS A 1 248 ? -45.475 10.522 -26.011 1.00 70.25 ? 275 LYS A N 1 ATOM 1905 C CA . LYS A 1 248 ? -45.701 11.241 -27.264 1.00 67.71 ? 275 LYS A CA 1 ATOM 1906 C C . LYS A 1 248 ? -47.194 11.379 -27.569 1.00 76.00 ? 275 LYS A C 1 ATOM 1907 O O . LYS A 1 248 ? -48.010 10.589 -27.092 1.00 79.04 ? 275 LYS A O 1 ATOM 1908 C CB . LYS A 1 248 ? -44.996 10.535 -28.428 1.00 68.95 ? 275 LYS A CB 1 ATOM 1909 C CG . LYS A 1 248 ? -45.622 9.202 -28.825 1.00 71.02 ? 275 LYS A CG 1 ATOM 1910 C CD . LYS A 1 248 ? -44.955 8.600 -30.056 1.00 74.74 ? 275 LYS A CD 1 ATOM 1911 C CE . LYS A 1 248 ? -45.644 7.306 -30.475 1.00 76.67 ? 275 LYS A CE 1 ATOM 1912 N NZ . LYS A 1 248 ? -45.009 6.670 -31.665 1.00 82.30 ? 275 LYS A NZ 1 ATOM 1913 N N . TRP A 1 249 ? -47.545 12.390 -28.361 1.00 79.51 ? 276 TRP A N 1 ATOM 1914 C CA . TRP A 1 249 ? -48.920 12.566 -28.828 1.00 73.31 ? 276 TRP A CA 1 ATOM 1915 C C . TRP A 1 249 ? -49.057 12.212 -30.310 1.00 75.49 ? 276 TRP A C 1 ATOM 1916 O O . TRP A 1 249 ? -48.158 12.469 -31.114 1.00 75.82 ? 276 TRP A O 1 ATOM 1917 C CB . TRP A 1 249 ? -49.401 14.000 -28.594 1.00 68.86 ? 276 TRP A CB 1 ATOM 1918 C CG . TRP A 1 249 ? -49.900 14.274 -27.204 1.00 63.10 ? 276 TRP A CG 1 ATOM 1919 C CD1 . TRP A 1 249 ? -49.226 14.904 -26.201 1.00 62.55 ? 276 TRP A CD1 1 ATOM 1920 C CD2 . TRP A 1 249 ? -51.189 13.941 -26.672 1.00 68.94 ? 276 TRP A CD2 1 ATOM 1921 N NE1 . TRP A 1 249 ? -50.011 14.982 -25.077 1.00 65.28 ? 276 TRP A NE1 1 ATOM 1922 C CE2 . TRP A 1 249 ? -51.222 14.397 -25.340 1.00 64.52 ? 276 TRP A CE2 1 ATOM 1923 C CE3 . TRP A 1 249 ? -52.317 13.300 -27.193 1.00 83.10 ? 276 TRP A CE3 1 ATOM 1924 C CZ2 . TRP A 1 249 ? -52.336 14.231 -24.521 1.00 67.28 ? 276 TRP A CZ2 1 ATOM 1925 C CZ3 . TRP A 1 249 ? -53.424 13.136 -26.377 1.00 86.27 ? 276 TRP A CZ3 1 ATOM 1926 C CH2 . TRP A 1 249 ? -53.425 13.599 -25.056 1.00 78.06 ? 276 TRP A CH2 1 ATOM 1927 N N . MET A 1 250 ? -50.195 11.620 -30.658 1.00 73.38 ? 277 MET A N 1 ATOM 1928 C CA . MET A 1 250 ? -50.473 11.179 -32.018 1.00 84.24 ? 277 MET A CA 1 ATOM 1929 C C . MET A 1 250 ? -51.856 11.619 -32.480 1.00 83.63 ? 277 MET A C 1 ATOM 1930 O O . MET A 1 250 ? -52.806 11.666 -31.687 1.00 91.55 ? 277 MET A O 1 ATOM 1931 C CB . MET A 1 250 ? -50.374 9.653 -32.130 1.00 102.41 ? 277 MET A CB 1 ATOM 1932 C CG . MET A 1 250 ? -48.966 9.089 -32.086 1.00 112.00 ? 277 MET A CG 1 ATOM 1933 S SD . MET A 1 250 ? -48.874 7.440 -32.815 1.00 83.93 ? 277 MET A SD 1 ATOM 1934 C CE . MET A 1 250 ? -50.250 6.638 -31.999 1.00 74.96 ? 277 MET A CE 1 ATOM 1935 N N . LEU A 1 251 ? -51.961 11.927 -33.770 1.00 77.96 ? 278 LEU A N 1 ATOM 1936 C CA . LEU A 1 251 ? -53.251 12.146 -34.407 1.00 75.01 ? 278 LEU A CA 1 ATOM 1937 C C . LEU A 1 251 ? -53.534 10.980 -35.340 1.00 75.35 ? 278 LEU A C 1 ATOM 1938 O O . LEU A 1 251 ? -53.231 11.037 -36.533 1.00 72.80 ? 278 LEU A O 1 ATOM 1939 C CB . LEU A 1 251 ? -53.274 13.468 -35.173 1.00 70.08 ? 278 LEU A CB 1 ATOM 1940 C CG . LEU A 1 251 ? -54.628 13.878 -35.748 1.00 70.41 ? 278 LEU A CG 1 ATOM 1941 C CD1 . LEU A 1 251 ? -55.676 13.908 -34.650 1.00 68.60 ? 278 LEU A CD1 1 ATOM 1942 C CD2 . LEU A 1 251 ? -54.529 15.231 -36.425 1.00 71.87 ? 278 LEU A CD2 1 ATOM 1943 N N . GLY A 1 252 ? -54.107 9.918 -34.784 1.00 87.33 ? 279 GLY A N 1 ATOM 1944 C CA . GLY A 1 252 ? -54.290 8.682 -35.516 1.00 89.11 ? 279 GLY A CA 1 ATOM 1945 C C . GLY A 1 252 ? -52.950 8.011 -35.738 1.00 91.97 ? 279 GLY A C 1 ATOM 1946 O O . GLY A 1 252 ? -52.346 7.487 -34.801 1.00 90.02 ? 279 GLY A O 1 ATOM 1947 N N . ALA A 1 253 ? -52.473 8.044 -36.979 1.00 96.49 ? 280 ALA A N 1 ATOM 1948 C CA . ALA A 1 253 ? -51.212 7.404 -37.328 1.00 95.29 ? 280 ALA A CA 1 ATOM 1949 C C . ALA A 1 253 ? -50.038 8.363 -37.172 1.00 102.03 ? 280 ALA A C 1 ATOM 1950 O O . ALA A 1 253 ? -48.964 7.972 -36.716 1.00 101.44 ? 280 ALA A O 1 ATOM 1951 C CB . ALA A 1 253 ? -51.268 6.865 -38.748 1.00 89.54 ? 280 ALA A CB 1 ATOM 1952 N N . GLU A 1 254 ? -50.249 9.618 -37.557 1.00 106.59 ? 281 GLU A N 1 ATOM 1953 C CA . GLU A 1 254 ? -49.188 10.616 -37.514 1.00 106.09 ? 281 GLU A CA 1 ATOM 1954 C C . GLU A 1 254 ? -48.728 10.902 -36.090 1.00 96.99 ? 281 GLU A C 1 ATOM 1955 O O . GLU A 1 254 ? -49.542 10.986 -35.171 1.00 95.44 ? 281 GLU A O 1 ATOM 1956 C CB . GLU A 1 254 ? -49.646 11.921 -38.170 1.00 111.44 ? 281 GLU A CB 1 ATOM 1957 C CG . GLU A 1 254 ? -48.608 13.033 -38.079 1.00 116.34 ? 281 GLU A CG 1 ATOM 1958 C CD . GLU A 1 254 ? -49.197 14.412 -38.263 1.00 118.56 ? 281 GLU A CD 1 ATOM 1959 O OE1 . GLU A 1 254 ? -50.164 14.546 -39.039 1.00 123.75 ? 281 GLU A OE1 1 ATOM 1960 O OE2 . GLU A 1 254 ? -48.690 15.364 -37.635 1.00 113.11 ? 281 GLU A OE2 1 ATOM 1961 N N . ASP A 1 255 ? -47.417 11.041 -35.915 1.00 97.59 ? 282 ASP A N 1 ATOM 1962 C CA . ASP A 1 255 ? -46.867 11.538 -34.662 1.00 100.80 ? 282 ASP A CA 1 ATOM 1963 C C . ASP A 1 255 ? -46.863 13.061 -34.672 1.00 110.73 ? 282 ASP A C 1 ATOM 1964 O O . ASP A 1 255 ? -46.436 13.683 -35.646 1.00 117.22 ? 282 ASP A O 1 ATOM 1965 C CB . ASP A 1 255 ? -45.450 11.010 -34.435 1.00 96.34 ? 282 ASP A CB 1 ATOM 1966 C CG . ASP A 1 255 ? -45.409 9.507 -34.256 1.00 93.75 ? 282 ASP A CG 1 ATOM 1967 O OD1 . ASP A 1 255 ? -45.023 8.800 -35.211 1.00 96.36 ? 282 ASP A OD1 1 ATOM 1968 O OD2 . ASP A 1 255 ? -45.766 9.033 -33.160 1.00 94.46 ? 282 ASP A OD2 1 ATOM 1969 N N . LEU A 1 256 ? -47.351 13.660 -33.593 1.00 110.65 ? 283 LEU A N 1 ATOM 1970 C CA . LEU A 1 256 ? -47.326 15.108 -33.453 1.00 110.54 ? 283 LEU A CA 1 ATOM 1971 C C . LEU A 1 256 ? -45.992 15.523 -32.854 1.00 114.66 ? 283 LEU A C 1 ATOM 1972 O O . LEU A 1 256 ? -45.295 16.385 -33.392 1.00 116.45 ? 283 LEU A O 1 ATOM 1973 C CB . LEU A 1 256 ? -48.485 15.590 -32.582 1.00 105.20 ? 283 LEU A CB 1 ATOM 1974 C CG . LEU A 1 256 ? -49.851 15.034 -32.990 1.00 102.62 ? 283 LEU A CG 1 ATOM 1975 C CD1 . LEU A 1 256 ? -50.954 15.563 -32.086 1.00 103.28 ? 283 LEU A CD1 1 ATOM 1976 C CD2 . LEU A 1 256 ? -50.144 15.354 -34.449 1.00 102.38 ? 283 LEU A CD2 1 ATOM 1977 N N . THR A 1 257 ? -45.646 14.888 -31.739 1.00 115.80 ? 284 THR A N 1 ATOM 1978 C CA . THR A 1 257 ? -44.364 15.106 -31.084 1.00 112.47 ? 284 THR A CA 1 ATOM 1979 C C . THR A 1 257 ? -43.222 14.646 -31.977 1.00 113.77 ? 284 THR A C 1 ATOM 1980 O O . THR A 1 257 ? -43.128 13.459 -32.296 1.00 112.08 ? 284 THR A O 1 ATOM 1981 C CB . THR A 1 257 ? -44.276 14.350 -29.747 1.00 105.46 ? 284 THR A CB 1 ATOM 1982 O OG1 . THR A 1 257 ? -45.506 14.497 -29.027 1.00 104.78 ? 284 THR A OG1 1 ATOM 1983 C CG2 . THR A 1 257 ? -43.125 14.879 -28.909 1.00 107.62 ? 284 THR A CG2 1 ATOM 1984 N N . PRO A 1 258 ? -42.355 15.584 -32.391 1.00 112.31 ? 285 PRO A N 1 ATOM 1985 C CA . PRO A 1 258 ? -41.167 15.194 -33.155 1.00 114.78 ? 285 PRO A CA 1 ATOM 1986 C C . PRO A 1 258 ? -40.325 14.220 -32.342 1.00 120.06 ? 285 PRO A C 1 ATOM 1987 O O . PRO A 1 258 ? -40.231 14.362 -31.123 1.00 120.18 ? 285 PRO A O 1 ATOM 1988 C CB . PRO A 1 258 ? -40.439 16.521 -33.395 1.00 110.64 ? 285 PRO A CB 1 ATOM 1989 C CG . PRO A 1 258 ? -40.985 17.458 -32.375 1.00 109.07 ? 285 PRO A CG 1 ATOM 1990 C CD . PRO A 1 258 ? -42.401 17.034 -32.140 1.00 109.65 ? 285 PRO A CD 1 ATOM 1991 N N . GLU A 1 259 ? -39.738 13.236 -33.013 1.00 127.59 ? 286 GLU A N 1 ATOM 1992 C CA . GLU A 1 259 ? -39.124 12.102 -32.333 1.00 130.22 ? 286 GLU A CA 1 ATOM 1993 C C . GLU A 1 259 ? -37.942 12.485 -31.446 1.00 127.72 ? 286 GLU A C 1 ATOM 1994 O O . GLU A 1 259 ? -37.830 12.013 -30.316 1.00 124.52 ? 286 GLU A O 1 ATOM 1995 C CB . GLU A 1 259 ? -38.671 11.060 -33.358 1.00 139.80 ? 286 GLU A CB 1 ATOM 1996 C CG . GLU A 1 259 ? -38.460 9.678 -32.771 1.00 142.44 ? 286 GLU A CG 1 ATOM 1997 C CD . GLU A 1 259 ? -37.544 8.819 -33.617 1.00 148.02 ? 286 GLU A CD 1 ATOM 1998 O OE1 . GLU A 1 259 ? -36.350 8.709 -33.269 1.00 148.28 ? 286 GLU A OE1 1 ATOM 1999 O OE2 . GLU A 1 259 ? -38.016 8.251 -34.625 1.00 150.56 ? 286 GLU A OE2 1 ATOM 2000 N N . ASP A 1 260 ? -37.067 13.344 -31.956 1.00 133.12 ? 287 ASP A N 1 ATOM 2001 C CA . ASP A 1 260 ? -35.808 13.638 -31.280 1.00 134.10 ? 287 ASP A CA 1 ATOM 2002 C C . ASP A 1 260 ? -35.958 14.666 -30.161 1.00 123.85 ? 287 ASP A C 1 ATOM 2003 O O . ASP A 1 260 ? -35.001 14.964 -29.448 1.00 123.57 ? 287 ASP A O 1 ATOM 2004 C CB . ASP A 1 260 ? -34.774 14.111 -32.299 1.00 145.14 ? 287 ASP A CB 1 ATOM 2005 C CG . ASP A 1 260 ? -34.572 13.109 -33.419 1.00 154.05 ? 287 ASP A CG 1 ATOM 2006 O OD1 . ASP A 1 260 ? -34.254 13.533 -34.549 1.00 160.83 ? 287 ASP A OD1 1 ATOM 2007 O OD2 . ASP A 1 260 ? -34.741 11.896 -33.169 1.00 154.40 ? 287 ASP A OD2 1 ATOM 2008 N N . ASP A 1 261 ? -37.163 15.206 -30.015 1.00 120.28 ? 288 ASP A N 1 ATOM 2009 C CA . ASP A 1 261 ? -37.493 16.047 -28.871 1.00 116.93 ? 288 ASP A CA 1 ATOM 2010 C C . ASP A 1 261 ? -38.760 15.521 -28.210 1.00 110.51 ? 288 ASP A C 1 ATOM 2011 O O . ASP A 1 261 ? -39.863 15.996 -28.485 1.00 113.87 ? 288 ASP A O 1 ATOM 2012 C CB . ASP A 1 261 ? -37.677 17.504 -29.288 1.00 122.79 ? 288 ASP A CB 1 ATOM 2013 C CG . ASP A 1 261 ? -38.101 18.385 -28.132 1.00 129.89 ? 288 ASP A CG 1 ATOM 2014 O OD1 . ASP A 1 261 ? -38.977 19.250 -28.337 1.00 132.38 ? 288 ASP A OD1 1 ATOM 2015 O OD2 . ASP A 1 261 ? -37.565 18.206 -27.017 1.00 132.57 ? 288 ASP A OD2 1 ATOM 2016 N N . MET A 1 262 ? -38.594 14.535 -27.336 1.00 101.27 ? 289 MET A N 1 ATOM 2017 C CA . MET A 1 262 ? -39.726 13.819 -26.766 1.00 96.40 ? 289 MET A CA 1 ATOM 2018 C C . MET A 1 262 ? -39.569 13.689 -25.255 1.00 100.83 ? 289 MET A C 1 ATOM 2019 O O . MET A 1 262 ? -38.647 13.025 -24.778 1.00 103.14 ? 289 MET A O 1 ATOM 2020 C CB . MET A 1 262 ? -39.855 12.444 -27.424 1.00 89.67 ? 289 MET A CB 1 ATOM 2021 C CG . MET A 1 262 ? -41.099 11.669 -27.049 1.00 85.18 ? 289 MET A CG 1 ATOM 2022 S SD . MET A 1 262 ? -41.223 10.126 -27.972 1.00 99.68 ? 289 MET A SD 1 ATOM 2023 C CE . MET A 1 262 ? -41.430 10.738 -29.643 1.00 101.93 ? 289 MET A CE 1 ATOM 2024 N N . PRO A 1 263 ? -40.478 14.324 -24.497 1.00 100.35 ? 290 PRO A N 1 ATOM 2025 C CA . PRO A 1 263 ? -40.385 14.444 -23.037 1.00 101.28 ? 290 PRO A CA 1 ATOM 2026 C C . PRO A 1 263 ? -40.581 13.123 -22.302 1.00 98.30 ? 290 PRO A C 1 ATOM 2027 O O . PRO A 1 263 ? -41.155 12.183 -22.852 1.00 102.34 ? 290 PRO A O 1 ATOM 2028 C CB . PRO A 1 263 ? -41.517 15.417 -22.697 1.00 98.49 ? 290 PRO A CB 1 ATOM 2029 C CG . PRO A 1 263 ? -42.519 15.198 -23.771 1.00 94.75 ? 290 PRO A CG 1 ATOM 2030 C CD . PRO A 1 263 ? -41.715 14.932 -25.017 1.00 95.78 ? 290 PRO A CD 1 ATOM 2031 N N . ILE A 1 264 ? -40.106 13.067 -21.062 1.00 90.52 ? 291 ILE A N 1 ATOM 2032 C CA . ILE A 1 264 ? -40.290 11.892 -20.217 1.00 88.67 ? 291 ILE A CA 1 ATOM 2033 C C . ILE A 1 264 ? -41.388 12.126 -19.185 1.00 100.81 ? 291 ILE A C 1 ATOM 2034 O O . ILE A 1 264 ? -41.473 13.200 -18.589 1.00 105.09 ? 291 ILE A O 1 ATOM 2035 C CB . ILE A 1 264 ? -38.981 11.507 -19.484 1.00 84.77 ? 291 ILE A CB 1 ATOM 2036 C CG1 . ILE A 1 264 ? -38.037 10.762 -20.424 1.00 78.87 ? 291 ILE A CG1 1 ATOM 2037 C CG2 . ILE A 1 264 ? -39.267 10.634 -18.274 1.00 82.94 ? 291 ILE A CG2 1 ATOM 2038 C CD1 . ILE A 1 264 ? -36.880 10.082 -19.713 1.00 66.59 ? 291 ILE A CD1 1 ATOM 2039 N N . GLY A 1 265 ? -42.246 11.126 -19.002 1.00 111.56 ? 292 GLY A N 1 ATOM 2040 C CA . GLY A 1 265 ? -43.163 11.096 -17.879 1.00 110.93 ? 292 GLY A CA 1 ATOM 2041 C C . GLY A 1 265 ? -44.290 12.107 -17.903 1.00 112.45 ? 292 GLY A C 1 ATOM 2042 O O . GLY A 1 265 ? -45.212 12.021 -17.092 1.00 114.21 ? 292 GLY A O 1 ATOM 2043 N N . ARG A 1 266 ? -44.225 13.063 -18.824 1.00 91.80 ? 293 ARG A N 1 ATOM 2044 C CA . ARG A 1 266 ? -45.264 14.076 -18.926 1.00 84.44 ? 293 ARG A CA 1 ATOM 2045 C C . ARG A 1 266 ? -45.203 14.813 -20.257 1.00 80.47 ? 293 ARG A C 1 ATOM 2046 O O . ARG A 1 266 ? -44.160 15.333 -20.651 1.00 83.06 ? 293 ARG A O 1 ATOM 2047 C CB . ARG A 1 266 ? -45.154 15.071 -17.770 1.00 90.12 ? 293 ARG A CB 1 ATOM 2048 C CG . ARG A 1 266 ? -46.322 16.030 -17.666 1.00 93.06 ? 293 ARG A CG 1 ATOM 2049 C CD . ARG A 1 266 ? -46.249 16.840 -16.383 1.00 95.11 ? 293 ARG A CD 1 ATOM 2050 N NE . ARG A 1 266 ? -47.006 18.083 -16.492 1.00 99.87 ? 293 ARG A NE 1 ATOM 2051 C CZ . ARG A 1 266 ? -46.556 19.171 -17.110 1.00 110.05 ? 293 ARG A CZ 1 ATOM 2052 N NH1 . ARG A 1 266 ? -45.355 19.166 -17.674 1.00 113.45 ? 293 ARG A NH1 1 ATOM 2053 N NH2 . ARG A 1 266 ? -47.306 20.263 -17.168 1.00 114.20 ? 293 ARG A NH2 1 ATOM 2054 N N . ASN A 1 267 ? -46.337 14.854 -20.943 1.00 78.43 ? 294 ASN A N 1 ATOM 2055 C CA . ASN A 1 267 ? -46.453 15.571 -22.201 1.00 85.86 ? 294 ASN A CA 1 ATOM 2056 C C . ASN A 1 267 ? -47.798 16.275 -22.262 1.00 97.57 ? 294 ASN A C 1 ATOM 2057 O O . ASN A 1 267 ? -48.849 15.633 -22.224 1.00 101.49 ? 294 ASN A O 1 ATOM 2058 C CB . ASN A 1 267 ? -46.286 14.617 -23.386 1.00 87.93 ? 294 ASN A CB 1 ATOM 2059 C CG . ASN A 1 267 ? -46.211 15.340 -24.725 1.00 96.47 ? 294 ASN A CG 1 ATOM 2060 O OD1 . ASN A 1 267 ? -46.887 16.345 -24.950 1.00 99.38 ? 294 ASN A OD1 1 ATOM 2061 N ND2 . ASN A 1 267 ? -45.384 14.821 -25.625 1.00 97.28 ? 294 ASN A ND2 1 ATOM 2062 N N . VAL A 1 268 ? -47.762 17.600 -22.340 1.00 103.11 ? 295 VAL A N 1 ATOM 2063 C CA . VAL A 1 268 ? -48.982 18.374 -22.491 1.00 103.02 ? 295 VAL A CA 1 ATOM 2064 C C . VAL A 1 268 ? -49.092 18.882 -23.923 1.00 108.96 ? 295 VAL A C 1 ATOM 2065 O O . VAL A 1 268 ? -48.254 19.648 -24.400 1.00 114.24 ? 295 VAL A O 1 ATOM 2066 C CB . VAL A 1 268 ? -49.050 19.552 -21.488 1.00 101.00 ? 295 VAL A CB 1 ATOM 2067 C CG1 . VAL A 1 268 ? -47.726 20.312 -21.433 1.00 99.59 ? 295 VAL A CG1 1 ATOM 2068 C CG2 . VAL A 1 268 ? -50.216 20.475 -21.826 1.00 101.19 ? 295 VAL A CG2 1 ATOM 2069 N N . LEU A 1 269 ? -50.123 18.411 -24.612 1.00 111.88 ? 296 LEU A N 1 ATOM 2070 C CA . LEU A 1 269 ? -50.419 18.829 -25.971 1.00 115.69 ? 296 LEU A CA 1 ATOM 2071 C C . LEU A 1 269 ? -51.136 20.174 -25.995 1.00 116.77 ? 296 LEU A C 1 ATOM 2072 O O . LEU A 1 269 ? -52.225 20.339 -25.421 1.00 117.17 ? 296 LEU A O 1 ATOM 2073 C CB . LEU A 1 269 ? -51.257 17.767 -26.684 1.00 116.70 ? 296 LEU A CB 1 ATOM 2074 C CG . LEU A 1 269 ? -51.607 18.035 -28.148 1.00 119.33 ? 296 LEU A CG 1 ATOM 2075 C CD1 . LEU A 1 269 ? -50.358 18.372 -28.945 1.00 122.55 ? 296 LEU A CD1 1 ATOM 2076 C CD2 . LEU A 1 269 ? -52.323 16.837 -28.753 1.00 118.51 ? 296 LEU A CD2 1 ATOM 2077 N N . GLU A 1 270 ? -50.491 21.127 -26.661 1.00 112.39 ? 297 GLU A N 1 ATOM 2078 C CA . GLU A 1 270 ? -51.019 22.469 -26.865 1.00 114.17 ? 297 GLU A CA 1 ATOM 2079 C C . GLU A 1 270 ? -51.776 22.538 -28.188 1.00 117.94 ? 297 GLU A C 1 ATOM 2080 O O . GLU A 1 270 ? -51.176 22.428 -29.257 1.00 119.09 ? 297 GLU A O 1 ATOM 2081 C CB . GLU A 1 270 ? -49.883 23.498 -26.856 1.00 119.96 ? 297 GLU A CB 1 ATOM 2082 C CG . GLU A 1 270 ? -49.037 23.502 -25.585 1.00 121.24 ? 297 GLU A CG 1 ATOM 2083 C CD . GLU A 1 270 ? -47.739 24.286 -25.740 1.00 120.98 ? 297 GLU A CD 1 ATOM 2084 O OE1 . GLU A 1 270 ? -47.165 24.286 -26.850 1.00 124.58 ? 297 GLU A OE1 1 ATOM 2085 O OE2 . GLU A 1 270 ? -47.293 24.902 -24.748 1.00 114.70 ? 297 GLU A OE2 1 ATOM 2086 N N . LEU A 1 271 ? -53.091 22.720 -28.114 1.00 120.39 ? 298 LEU A N 1 ATOM 2087 C CA . LEU A 1 271 ? -53.920 22.784 -29.313 1.00 119.93 ? 298 LEU A CA 1 ATOM 2088 C C . LEU A 1 271 ? -54.461 24.197 -29.534 1.00 132.39 ? 298 LEU A C 1 ATOM 2089 O O . LEU A 1 271 ? -55.104 24.768 -28.655 1.00 135.70 ? 298 LEU A O 1 ATOM 2090 C CB . LEU A 1 271 ? -55.068 21.776 -29.216 1.00 104.40 ? 298 LEU A CB 1 ATOM 2091 C CG . LEU A 1 271 ? -54.646 20.304 -29.234 1.00 94.91 ? 298 LEU A CG 1 ATOM 2092 C CD1 . LEU A 1 271 ? -55.825 19.385 -28.940 1.00 95.94 ? 298 LEU A CD1 1 ATOM 2093 C CD2 . LEU A 1 271 ? -54.013 19.950 -30.572 1.00 87.29 ? 298 LEU A CD2 1 ATOM 2094 N N . ASN A 1 272 ? -54.193 24.757 -30.711 1.00 137.57 ? 299 ASN A N 1 ATOM 2095 C CA . ASN A 1 272 ? -54.579 26.131 -31.013 1.00 139.18 ? 299 ASN A CA 1 ATOM 2096 C C . ASN A 1 272 ? -55.484 26.244 -32.235 1.00 136.28 ? 299 ASN A C 1 ATOM 2097 O O . ASN A 1 272 ? -55.351 25.476 -33.190 1.00 135.76 ? 299 ASN A O 1 ATOM 2098 C CB . ASN A 1 272 ? -53.328 26.987 -31.216 1.00 146.80 ? 299 ASN A CB 1 ATOM 2099 C CG . ASN A 1 272 ? -52.438 26.463 -32.328 1.00 155.29 ? 299 ASN A CG 1 ATOM 2100 O OD1 . ASN A 1 272 ? -52.666 25.380 -32.867 1.00 157.88 ? 299 ASN A OD1 1 ATOM 2101 N ND2 . ASN A 1 272 ? -51.395 27.214 -32.650 1.00 159.20 ? 299 ASN A ND2 1 ATOM 2102 N N . ASP A 1 273 ? -56.397 27.211 -32.192 1.00 133.11 ? 300 ASP A N 1 ATOM 2103 C CA . ASP A 1 273 ? -57.314 27.473 -33.296 1.00 130.21 ? 300 ASP A CA 1 ATOM 2104 C C . ASP A 1 273 ? -57.996 26.193 -33.769 1.00 128.33 ? 300 ASP A C 1 ATOM 2105 O O . ASP A 1 273 ? -57.895 25.818 -34.939 1.00 130.91 ? 300 ASP A O 1 ATOM 2106 C CB . ASP A 1 273 ? -56.575 28.138 -34.459 1.00 129.41 ? 300 ASP A CB 1 ATOM 2107 C CG . ASP A 1 273 ? -57.515 28.618 -35.546 1.00 127.66 ? 300 ASP A CG 1 ATOM 2108 O OD1 . ASP A 1 273 ? -58.595 29.146 -35.207 1.00 127.52 ? 300 ASP A OD1 1 ATOM 2109 O OD2 . ASP A 1 273 ? -57.176 28.454 -36.737 1.00 127.09 ? 300 ASP A OD2 1 ATOM 2110 N N . VAL A 1 274 ? -58.667 25.511 -32.847 1.00 124.16 ? 301 VAL A N 1 ATOM 2111 C CA . VAL A 1 274 ? -59.344 24.263 -33.173 1.00 120.30 ? 301 VAL A CA 1 ATOM 2112 C C . VAL A 1 274 ? -60.416 24.510 -34.225 1.00 121.11 ? 301 VAL A C 1 ATOM 2113 O O . VAL A 1 274 ? -61.172 25.478 -34.147 1.00 122.86 ? 301 VAL A O 1 ATOM 2114 C CB . VAL A 1 274 ? -59.976 23.618 -31.930 1.00 117.35 ? 301 VAL A CB 1 ATOM 2115 C CG1 . VAL A 1 274 ? -60.681 22.321 -32.298 1.00 116.23 ? 301 VAL A CG1 1 ATOM 2116 C CG2 . VAL A 1 274 ? -58.916 23.367 -30.867 1.00 114.28 ? 301 VAL A CG2 1 ATOM 2117 N N . ARG A 1 275 ? -60.466 23.634 -35.219 1.00 119.89 ? 302 ARG A N 1 ATOM 2118 C CA . ARG A 1 275 ? -61.374 23.811 -36.336 1.00 120.89 ? 302 ARG A CA 1 ATOM 2119 C C . ARG A 1 275 ? -62.448 22.728 -36.350 1.00 115.71 ? 302 ARG A C 1 ATOM 2120 O O . ARG A 1 275 ? -63.641 23.026 -36.296 1.00 111.42 ? 302 ARG A O 1 ATOM 2121 C CB . ARG A 1 275 ? -60.585 23.816 -37.643 1.00 131.82 ? 302 ARG A CB 1 ATOM 2122 C CG . ARG A 1 275 ? -61.423 24.017 -38.885 1.00 143.29 ? 302 ARG A CG 1 ATOM 2123 C CD . ARG A 1 275 ? -61.462 22.743 -39.702 1.00 149.80 ? 302 ARG A CD 1 ATOM 2124 N NE . ARG A 1 275 ? -61.923 22.978 -41.065 1.00 155.07 ? 302 ARG A NE 1 ATOM 2125 C CZ . ARG A 1 275 ? -61.861 22.072 -42.035 1.00 158.28 ? 302 ARG A CZ 1 ATOM 2126 N NH1 . ARG A 1 275 ? -61.354 20.871 -41.786 1.00 158.26 ? 302 ARG A NH1 1 ATOM 2127 N NH2 . ARG A 1 275 ? -62.299 22.365 -43.252 1.00 159.45 ? 302 ARG A NH2 1 ATOM 2128 N N . GLN A 1 276 ? -62.022 21.471 -36.414 1.00 120.50 ? 303 GLN A N 1 ATOM 2129 C CA . GLN A 1 276 ? -62.953 20.349 -36.388 1.00 122.97 ? 303 GLN A CA 1 ATOM 2130 C C . GLN A 1 276 ? -62.663 19.451 -35.185 1.00 121.04 ? 303 GLN A C 1 ATOM 2131 O O . GLN A 1 276 ? -61.607 19.560 -34.564 1.00 119.79 ? 303 GLN A O 1 ATOM 2132 C CB . GLN A 1 276 ? -62.869 19.554 -37.696 1.00 130.04 ? 303 GLN A CB 1 ATOM 2133 C CG . GLN A 1 276 ? -64.014 18.572 -37.922 1.00 141.24 ? 303 GLN A CG 1 ATOM 2134 C CD . GLN A 1 276 ? -64.070 18.053 -39.343 1.00 154.41 ? 303 GLN A CD 1 ATOM 2135 O OE1 . GLN A 1 276 ? -63.591 18.703 -40.273 1.00 161.00 ? 303 GLN A OE1 1 ATOM 2136 N NE2 . GLN A 1 276 ? -64.659 16.876 -39.521 1.00 156.73 ? 303 GLN A NE2 1 ATOM 2137 N N . SER A 1 277 ? -63.612 18.580 -34.851 1.00 115.60 ? 304 SER A N 1 ATOM 2138 C CA . SER A 1 277 ? -63.438 17.613 -33.773 1.00 107.05 ? 304 SER A CA 1 ATOM 2139 C C . SER A 1 277 ? -62.301 16.642 -34.078 1.00 108.18 ? 304 SER A C 1 ATOM 2140 O O . SER A 1 277 ? -61.943 16.444 -35.240 1.00 114.52 ? 304 SER A O 1 ATOM 2141 C CB . SER A 1 277 ? -64.736 16.840 -33.543 1.00 102.32 ? 304 SER A CB 1 ATOM 2142 O OG . SER A 1 277 ? -65.828 17.724 -33.364 1.00 102.32 ? 304 SER A OG 1 ATOM 2143 N N . ALA A 1 278 ? -61.740 16.031 -33.037 1.00 106.26 ? 305 ALA A N 1 ATOM 2144 C CA . ALA A 1 278 ? -60.643 15.089 -33.223 1.00 105.21 ? 305 ALA A CA 1 ATOM 2145 C C . ALA A 1 278 ? -60.417 14.132 -32.046 1.00 103.61 ? 305 ALA A C 1 ATOM 2146 O O . ALA A 1 278 ? -60.406 14.534 -30.875 1.00 103.25 ? 305 ALA A O 1 ATOM 2147 C CB . ALA A 1 278 ? -59.363 15.852 -33.515 1.00 106.52 ? 305 ALA A CB 1 ATOM 2148 N N . ASN A 1 279 ? -60.263 12.854 -32.392 1.00 100.44 ? 306 ASN A N 1 ATOM 2149 C CA . ASN A 1 279 ? -59.689 11.837 -31.518 1.00 91.02 ? 306 ASN A CA 1 ATOM 2150 C C . ASN A 1 279 ? -58.177 12.082 -31.403 1.00 80.71 ? 306 ASN A C 1 ATOM 2151 O O . ASN A 1 279 ? -57.498 12.165 -32.426 1.00 76.14 ? 306 ASN A O 1 ATOM 2152 C CB . ASN A 1 279 ? -59.953 10.430 -32.086 1.00 102.12 ? 306 ASN A CB 1 ATOM 2153 C CG . ASN A 1 279 ? -61.261 9.799 -31.591 1.00 113.99 ? 306 ASN A CG 1 ATOM 2154 O OD1 . ASN A 1 279 ? -61.245 8.984 -30.670 1.00 124.87 ? 306 ASN A OD1 1 ATOM 2155 N ND2 . ASN A 1 279 ? -62.387 10.160 -32.218 1.00 112.90 ? 306 ASN A ND2 1 ATOM 2156 N N . TYR A 1 280 ? -57.640 12.202 -30.188 1.00 80.73 ? 307 TYR A N 1 ATOM 2157 C CA . TYR A 1 280 ? -56.194 12.436 -30.020 1.00 74.91 ? 307 TYR A CA 1 ATOM 2158 C C . TYR A 1 280 ? -55.498 11.397 -29.137 1.00 84.86 ? 307 TYR A C 1 ATOM 2159 O O . TYR A 1 280 ? -55.675 11.401 -27.925 1.00 93.54 ? 307 TYR A O 1 ATOM 2160 C CB . TYR A 1 280 ? -55.941 13.824 -29.426 1.00 67.76 ? 307 TYR A CB 1 ATOM 2161 C CG . TYR A 1 280 ? -55.818 14.934 -30.445 1.00 76.38 ? 307 TYR A CG 1 ATOM 2162 C CD1 . TYR A 1 280 ? -56.869 15.813 -30.674 1.00 86.00 ? 307 TYR A CD1 1 ATOM 2163 C CD2 . TYR A 1 280 ? -54.648 15.108 -31.174 1.00 79.69 ? 307 TYR A CD2 1 ATOM 2164 C CE1 . TYR A 1 280 ? -56.757 16.835 -31.602 1.00 87.17 ? 307 TYR A CE1 1 ATOM 2165 C CE2 . TYR A 1 280 ? -54.530 16.128 -32.109 1.00 82.15 ? 307 TYR A CE2 1 ATOM 2166 C CZ . TYR A 1 280 ? -55.590 16.986 -32.319 1.00 83.57 ? 307 TYR A CZ 1 ATOM 2167 O OH . TYR A 1 280 ? -55.489 18.004 -33.244 1.00 76.34 ? 307 TYR A OH 1 ATOM 2168 N N . THR A 1 281 ? -54.672 10.534 -29.721 1.00 84.92 ? 308 THR A N 1 ATOM 2169 C CA . THR A 1 281 ? -54.068 9.456 -28.931 1.00 82.97 ? 308 THR A CA 1 ATOM 2170 C C . THR A 1 281 ? -52.820 9.911 -28.171 1.00 85.59 ? 308 THR A C 1 ATOM 2171 O O . THR A 1 281 ? -52.021 10.677 -28.693 1.00 81.94 ? 308 THR A O 1 ATOM 2172 C CB . THR A 1 281 ? -53.687 8.251 -29.812 1.00 82.23 ? 308 THR A CB 1 ATOM 2173 O OG1 . THR A 1 281 ? -54.657 8.086 -30.854 1.00 85.41 ? 308 THR A OG1 1 ATOM 2174 C CG2 . THR A 1 281 ? -53.617 6.982 -28.971 1.00 77.35 ? 308 THR A CG2 1 ATOM 2175 N N . CYS A 1 282 ? -52.660 9.438 -26.938 1.00 97.89 ? 309 CYS A N 1 ATOM 2176 C CA . CYS A 1 282 ? -51.444 9.693 -26.166 1.00 59.24 ? 309 CYS A CA 1 ATOM 2177 C C . CYS A 1 282 ? -50.742 8.392 -25.817 1.00 78.67 ? 309 CYS A C 1 ATOM 2178 O O . CYS A 1 282 ? -51.292 7.552 -25.105 1.00 80.91 ? 309 CYS A O 1 ATOM 2179 C CB . CYS A 1 282 ? -51.753 10.461 -24.883 1.00 58.30 ? 309 CYS A CB 1 ATOM 2180 S SG . CYS A 1 282 ? -50.361 10.545 -23.724 1.00 88.12 ? 309 CYS A SG 1 ATOM 2181 N N . VAL A 1 283 ? -49.518 8.235 -26.305 1.00 74.77 ? 310 VAL A N 1 ATOM 2182 C CA . VAL A 1 283 ? -48.790 6.991 -26.114 1.00 71.02 ? 310 VAL A CA 1 ATOM 2183 C C . VAL A 1 283 ? -47.639 7.143 -25.129 1.00 67.27 ? 310 VAL A C 1 ATOM 2184 O O . VAL A 1 283 ? -46.791 8.028 -25.260 1.00 70.56 ? 310 VAL A O 1 ATOM 2185 C CB . VAL A 1 283 ? -48.235 6.456 -27.448 1.00 76.13 ? 310 VAL A CB 1 ATOM 2186 C CG1 . VAL A 1 283 ? -47.507 5.141 -27.231 1.00 71.04 ? 310 VAL A CG1 1 ATOM 2187 C CG2 . VAL A 1 283 ? -49.359 6.286 -28.459 1.00 74.96 ? 310 VAL A CG2 1 ATOM 2188 N N . ALA A 1 284 ? -47.631 6.270 -24.132 1.00 69.50 ? 311 ALA A N 1 ATOM 2189 C CA . ALA A 1 284 ? -46.524 6.163 -23.199 1.00 73.16 ? 311 ALA A CA 1 ATOM 2190 C C . ALA A 1 284 ? -45.799 4.850 -23.433 1.00 70.96 ? 311 ALA A C 1 ATOM 2191 O O . ALA A 1 284 ? -46.434 3.799 -23.521 1.00 69.38 ? 311 ALA A O 1 ATOM 2192 C CB . ALA A 1 284 ? -47.020 6.248 -21.778 1.00 76.63 ? 311 ALA A CB 1 ATOM 2193 N N . MET A 1 285 ? -44.475 4.903 -23.543 1.00 74.83 ? 312 MET A N 1 ATOM 2194 C CA . MET A 1 285 ? -43.704 3.682 -23.739 1.00 77.38 ? 312 MET A CA 1 ATOM 2195 C C . MET A 1 285 ? -42.477 3.594 -22.846 1.00 71.84 ? 312 MET A C 1 ATOM 2196 O O . MET A 1 285 ? -41.708 4.547 -22.724 1.00 67.47 ? 312 MET A O 1 ATOM 2197 C CB . MET A 1 285 ? -43.277 3.539 -25.203 1.00 74.09 ? 312 MET A CB 1 ATOM 2198 C CG . MET A 1 285 ? -43.172 4.834 -25.986 1.00 66.05 ? 312 MET A CG 1 ATOM 2199 S SD . MET A 1 285 ? -42.820 4.459 -27.713 1.00 139.88 ? 312 MET A SD 1 ATOM 2200 C CE . MET A 1 285 ? -42.898 6.085 -28.452 1.00 104.01 ? 312 MET A CE 1 ATOM 2201 N N . SER A 1 286 ? -42.311 2.435 -22.217 1.00 75.04 ? 313 SER A N 1 ATOM 2202 C CA . SER A 1 286 ? -41.060 2.121 -21.540 1.00 80.43 ? 313 SER A CA 1 ATOM 2203 C C . SER A 1 286 ? -40.451 0.906 -22.222 1.00 80.69 ? 313 SER A C 1 ATOM 2204 O O . SER A 1 286 ? -40.912 0.483 -23.283 1.00 77.10 ? 313 SER A O 1 ATOM 2205 C CB . SER A 1 286 ? -41.275 1.860 -20.044 1.00 81.04 ? 313 SER A CB 1 ATOM 2206 O OG . SER A 1 286 ? -41.975 0.651 -19.816 1.00 79.29 ? 313 SER A OG 1 ATOM 2207 N N . THR A 1 287 ? -39.417 0.341 -21.617 1.00 83.95 ? 314 THR A N 1 ATOM 2208 C CA . THR A 1 287 ? -38.834 -0.878 -22.147 1.00 81.74 ? 314 THR A CA 1 ATOM 2209 C C . THR A 1 287 ? -39.752 -2.052 -21.785 1.00 80.86 ? 314 THR A C 1 ATOM 2210 O O . THR A 1 287 ? -39.628 -3.154 -22.328 1.00 83.79 ? 314 THR A O 1 ATOM 2211 C CB . THR A 1 287 ? -37.387 -1.080 -21.617 1.00 109.85 ? 314 THR A CB 1 ATOM 2212 O OG1 . THR A 1 287 ? -36.500 -1.325 -22.716 1.00 114.82 ? 314 THR A OG1 1 ATOM 2213 C CG2 . THR A 1 287 ? -37.297 -2.224 -20.613 1.00 111.92 ? 314 THR A CG2 1 ATOM 2214 N N . LEU A 1 288 ? -40.707 -1.782 -20.895 1.00 80.47 ? 315 LEU A N 1 ATOM 2215 C CA . LEU A 1 288 ? -41.647 -2.791 -20.409 1.00 78.87 ? 315 LEU A CA 1 ATOM 2216 C C . LEU A 1 288 ? -43.052 -2.629 -20.977 1.00 80.01 ? 315 LEU A C 1 ATOM 2217 O O . LEU A 1 288 ? -44.037 -2.900 -20.289 1.00 80.44 ? 315 LEU A O 1 ATOM 2218 C CB . LEU A 1 288 ? -41.731 -2.745 -18.887 1.00 79.73 ? 315 LEU A CB 1 ATOM 2219 C CG . LEU A 1 288 ? -40.450 -3.026 -18.115 1.00 83.33 ? 315 LEU A CG 1 ATOM 2220 C CD1 . LEU A 1 288 ? -40.671 -2.706 -16.656 1.00 84.09 ? 315 LEU A CD1 1 ATOM 2221 C CD2 . LEU A 1 288 ? -40.026 -4.477 -18.295 1.00 84.93 ? 315 LEU A CD2 1 ATOM 2222 N N . GLY A 1 289 ? -43.150 -2.174 -22.220 1.00 81.51 ? 316 GLY A N 1 ATOM 2223 C CA . GLY A 1 289 ? -44.442 -2.070 -22.867 1.00 78.17 ? 316 GLY A CA 1 ATOM 2224 C C . GLY A 1 289 ? -44.860 -0.686 -23.326 1.00 77.27 ? 316 GLY A C 1 ATOM 2225 O O . GLY A 1 289 ? -44.228 0.332 -23.005 1.00 77.46 ? 316 GLY A O 1 ATOM 2226 N N . VAL A 1 290 ? -45.953 -0.676 -24.084 1.00 72.99 ? 317 VAL A N 1 ATOM 2227 C CA . VAL A 1 290 ? -46.512 0.514 -24.710 1.00 71.86 ? 317 VAL A CA 1 ATOM 2228 C C . VAL A 1 290 ? -48.009 0.610 -24.434 1.00 72.79 ? 317 VAL A C 1 ATOM 2229 O O . VAL A 1 290 ? -48.765 -0.305 -24.763 1.00 77.04 ? 317 VAL A O 1 ATOM 2230 C CB . VAL A 1 290 ? -46.293 0.502 -26.238 1.00 59.51 ? 317 VAL A CB 1 ATOM 2231 C CG1 . VAL A 1 290 ? -47.135 1.577 -26.909 1.00 76.93 ? 317 VAL A CG1 1 ATOM 2232 C CG2 . VAL A 1 290 ? -44.821 0.659 -26.580 1.00 60.26 ? 317 VAL A CG2 1 ATOM 2233 N N . ILE A 1 291 ? -48.437 1.718 -23.840 1.00 71.35 ? 318 ILE A N 1 ATOM 2234 C CA . ILE A 1 291 ? -49.855 1.938 -23.577 1.00 72.22 ? 318 ILE A CA 1 ATOM 2235 C C . ILE A 1 291 ? -50.327 3.229 -24.234 1.00 77.10 ? 318 ILE A C 1 ATOM 2236 O O . ILE A 1 291 ? -49.537 4.141 -24.461 1.00 78.04 ? 318 ILE A O 1 ATOM 2237 C CB . ILE A 1 291 ? -50.145 1.994 -22.069 1.00 68.71 ? 318 ILE A CB 1 ATOM 2238 C CG1 . ILE A 1 291 ? -49.382 3.153 -21.423 1.00 66.62 ? 318 ILE A CG1 1 ATOM 2239 C CG2 . ILE A 1 291 ? -49.757 0.686 -21.412 1.00 61.76 ? 318 ILE A CG2 1 ATOM 2240 C CD1 . ILE A 1 291 ? -49.585 3.257 -19.932 1.00 59.09 ? 318 ILE A CD1 1 ATOM 2241 N N . GLU A 1 292 ? -51.615 3.302 -24.553 1.00 80.66 ? 319 GLU A N 1 ATOM 2242 C CA . GLU A 1 292 ? -52.157 4.497 -25.189 1.00 82.50 ? 319 GLU A CA 1 ATOM 2243 C C . GLU A 1 292 ? -53.524 4.875 -24.623 1.00 72.88 ? 319 GLU A C 1 ATOM 2244 O O . GLU A 1 292 ? -54.274 4.023 -24.150 1.00 71.89 ? 319 GLU A O 1 ATOM 2245 C CB . GLU A 1 292 ? -52.238 4.307 -26.711 1.00 90.91 ? 319 GLU A CB 1 ATOM 2246 C CG . GLU A 1 292 ? -53.105 3.144 -27.176 1.00 96.13 ? 319 GLU A CG 1 ATOM 2247 C CD . GLU A 1 292 ? -53.079 2.964 -28.686 1.00 103.46 ? 319 GLU A CD 1 ATOM 2248 O OE1 . GLU A 1 292 ? -52.059 3.324 -29.309 1.00 106.98 ? 319 GLU A OE1 1 ATOM 2249 O OE2 . GLU A 1 292 ? -54.079 2.472 -29.250 1.00 105.63 ? 319 GLU A OE2 1 ATOM 2250 N N . ALA A 1 293 ? -53.831 6.168 -24.662 1.00 68.60 ? 320 ALA A N 1 ATOM 2251 C CA . ALA A 1 293 ? -55.113 6.670 -24.172 1.00 70.02 ? 320 ALA A CA 1 ATOM 2252 C C . ALA A 1 293 ? -55.565 7.895 -24.963 1.00 78.03 ? 320 ALA A C 1 ATOM 2253 O O . ALA A 1 293 ? -54.820 8.859 -25.120 1.00 83.36 ? 320 ALA A O 1 ATOM 2254 C CB . ALA A 1 293 ? -55.025 6.996 -22.693 1.00 68.74 ? 320 ALA A CB 1 ATOM 2255 N N . ILE A 1 294 ? -56.802 7.851 -25.442 1.00 78.77 ? 321 ILE A N 1 ATOM 2256 C CA . ILE A 1 294 ? -57.330 8.864 -26.348 1.00 77.45 ? 321 ILE A CA 1 ATOM 2257 C C . ILE A 1 294 ? -57.898 10.065 -25.581 1.00 76.93 ? 321 ILE A C 1 ATOM 2258 O O . ILE A 1 294 ? -58.237 9.956 -24.403 1.00 77.39 ? 321 ILE A O 1 ATOM 2259 C CB . ILE A 1 294 ? -58.424 8.250 -27.274 1.00 92.86 ? 321 ILE A CB 1 ATOM 2260 C CG1 . ILE A 1 294 ? -57.923 6.958 -27.929 1.00 105.01 ? 321 ILE A CG1 1 ATOM 2261 C CG2 . ILE A 1 294 ? -58.858 9.219 -28.362 1.00 82.37 ? 321 ILE A CG2 1 ATOM 2262 C CD1 . ILE A 1 294 ? -58.344 5.678 -27.222 1.00 107.88 ? 321 ILE A CD1 1 ATOM 2263 N N . ALA A 1 295 ? -57.968 11.210 -26.257 1.00 79.53 ? 322 ALA A N 1 ATOM 2264 C CA . ALA A 1 295 ? -58.602 12.414 -25.742 1.00 78.76 ? 322 ALA A CA 1 ATOM 2265 C C . ALA A 1 295 ? -59.596 12.936 -26.775 1.00 87.89 ? 322 ALA A C 1 ATOM 2266 O O . ALA A 1 295 ? -59.240 13.183 -27.933 1.00 94.86 ? 322 ALA A O 1 ATOM 2267 C CB . ALA A 1 295 ? -57.562 13.473 -25.411 1.00 66.72 ? 322 ALA A CB 1 ATOM 2268 N N . GLN A 1 296 ? -60.845 13.092 -26.350 1.00 92.06 ? 323 GLN A N 1 ATOM 2269 C CA . GLN A 1 296 ? -61.925 13.437 -27.264 1.00 97.57 ? 323 GLN A CA 1 ATOM 2270 C C . GLN A 1 296 ? -62.128 14.935 -27.356 1.00 99.04 ? 323 GLN A C 1 ATOM 2271 O O . GLN A 1 296 ? -62.860 15.515 -26.557 1.00 97.89 ? 323 GLN A O 1 ATOM 2272 C CB . GLN A 1 296 ? -63.229 12.772 -26.823 1.00 105.26 ? 323 GLN A CB 1 ATOM 2273 C CG . GLN A 1 296 ? -64.188 12.473 -27.947 1.00 116.37 ? 323 GLN A CG 1 ATOM 2274 C CD . GLN A 1 296 ? -63.656 11.401 -28.865 1.00 125.72 ? 323 GLN A CD 1 ATOM 2275 O OE1 . GLN A 1 296 ? -62.789 11.657 -29.702 1.00 127.45 ? 323 GLN A OE1 1 ATOM 2276 N NE2 . GLN A 1 296 ? -64.164 10.184 -28.707 1.00 126.45 ? 323 GLN A NE2 1 ATOM 2277 N N . ILE A 1 297 ? -61.481 15.565 -28.329 1.00 100.94 ? 324 ILE A N 1 ATOM 2278 C CA . ILE A 1 297 ? -61.750 16.969 -28.594 1.00 98.27 ? 324 ILE A CA 1 ATOM 2279 C C . ILE A 1 297 ? -62.959 17.042 -29.510 1.00 100.47 ? 324 ILE A C 1 ATOM 2280 O O . ILE A 1 297 ? -63.029 16.315 -30.494 1.00 105.12 ? 324 ILE A O 1 ATOM 2281 C CB . ILE A 1 297 ? -60.553 17.679 -29.247 1.00 92.28 ? 324 ILE A CB 1 ATOM 2282 C CG1 . ILE A 1 297 ? -59.324 17.590 -28.344 1.00 94.04 ? 324 ILE A CG1 1 ATOM 2283 C CG2 . ILE A 1 297 ? -60.889 19.131 -29.532 1.00 88.19 ? 324 ILE A CG2 1 ATOM 2284 C CD1 . ILE A 1 297 ? -59.485 18.314 -27.028 1.00 97.53 ? 324 ILE A CD1 1 ATOM 2285 N N . THR A 1 298 ? -63.932 17.881 -29.176 1.00 97.59 ? 325 THR A N 1 ATOM 2286 C CA . THR A 1 298 ? -65.053 18.090 -30.085 1.00 98.04 ? 325 THR A CA 1 ATOM 2287 C C . THR A 1 298 ? -65.375 19.571 -30.202 1.00 95.52 ? 325 THR A C 1 ATOM 2288 O O . THR A 1 298 ? -65.108 20.354 -29.291 1.00 91.44 ? 325 THR A O 1 ATOM 2289 C CB . THR A 1 298 ? -66.326 17.320 -29.648 1.00 109.29 ? 325 THR A CB 1 ATOM 2290 O OG1 . THR A 1 298 ? -66.780 17.797 -28.378 1.00 107.04 ? 325 THR A OG1 1 ATOM 2291 C CG2 . THR A 1 298 ? -66.061 15.820 -29.567 1.00 108.33 ? 325 THR A CG2 1 ATOM 2292 N N . VAL A 1 299 ? -65.938 19.951 -31.343 1.00 99.61 ? 326 VAL A N 1 ATOM 2293 C CA . VAL A 1 299 ? -66.334 21.331 -31.570 1.00 102.62 ? 326 VAL A CA 1 ATOM 2294 C C . VAL A 1 299 ? -67.852 21.453 -31.583 1.00 113.02 ? 326 VAL A C 1 ATOM 2295 O O . VAL A 1 299 ? -68.511 21.021 -32.528 1.00 119.45 ? 326 VAL A O 1 ATOM 2296 C CB . VAL A 1 299 ? -65.768 21.870 -32.889 1.00 94.78 ? 326 VAL A CB 1 ATOM 2297 C CG1 . VAL A 1 299 ? -66.269 23.277 -33.129 1.00 99.72 ? 326 VAL A CG1 1 ATOM 2298 C CG2 . VAL A 1 299 ? -64.249 21.839 -32.863 1.00 81.31 ? 326 VAL A CG2 1 ATOM 2299 N N . LYS A 1 300 ? -68.402 22.037 -30.524 1.00 116.54 ? 327 LYS A N 1 ATOM 2300 C CA . LYS A 1 300 ? -69.848 22.167 -30.391 1.00 124.66 ? 327 LYS A CA 1 ATOM 2301 C C . LYS A 1 300 ? -70.319 23.490 -30.982 1.00 134.31 ? 327 LYS A C 1 ATOM 2302 O O . LYS A 1 300 ? -69.686 24.527 -30.783 1.00 137.47 ? 327 LYS A O 1 ATOM 2303 C CB . LYS A 1 300 ? -70.262 22.062 -28.920 1.00 124.89 ? 327 LYS A CB 1 ATOM 2304 C CG . LYS A 1 300 ? -71.730 21.722 -28.690 1.00 125.92 ? 327 LYS A CG 1 ATOM 2305 C CD . LYS A 1 300 ? -71.996 20.230 -28.793 1.00 127.41 ? 327 LYS A CD 1 ATOM 2306 C CE . LYS A 1 300 ? -73.191 19.826 -27.939 1.00 130.43 ? 327 LYS A CE 1 ATOM 2307 N NZ . LYS A 1 300 ? -74.366 20.718 -28.149 1.00 134.33 ? 327 LYS A NZ 1 ATOM 2308 N N . ALA A 1 301 ? -71.425 23.447 -31.717 1.00 135.83 ? 328 ALA A N 1 ATOM 2309 C CA . ALA A 1 301 ? -71.988 24.648 -32.321 1.00 133.76 ? 328 ALA A CA 1 ATOM 2310 C C . ALA A 1 301 ? -73.285 25.038 -31.622 1.00 141.93 ? 328 ALA A C 1 ATOM 2311 O O . ALA A 1 301 ? -74.276 24.309 -31.699 1.00 145.48 ? 328 ALA A O 1 ATOM 2312 C CB . ALA A 1 301 ? -72.227 24.435 -33.808 1.00 128.95 ? 328 ALA A CB 1 ATOM 2313 N N . LEU A 1 302 ? -73.266 26.183 -30.939 1.00 145.74 ? 329 LEU A N 1 ATOM 2314 C CA . LEU A 1 302 ? -74.433 26.682 -30.214 1.00 143.36 ? 329 LEU A CA 1 ATOM 2315 C C . LEU A 1 302 ? -75.637 26.782 -31.161 1.00 161.30 ? 329 LEU A C 1 ATOM 2316 O O . LEU A 1 302 ? -75.469 27.062 -32.348 1.00 166.49 ? 329 LEU A O 1 ATOM 2317 C CB . LEU A 1 302 ? -74.111 28.030 -29.544 1.00 123.17 ? 329 LEU A CB 1 ATOM 2318 C CG . LEU A 1 302 ? -73.449 29.158 -30.333 1.00 109.53 ? 329 LEU A CG 1 ATOM 2319 C CD1 . LEU A 1 302 ? -74.442 30.275 -30.597 1.00 107.94 ? 329 LEU A CD1 1 ATOM 2320 C CD2 . LEU A 1 302 ? -72.235 29.686 -29.584 1.00 97.43 ? 329 LEU A CD2 1 ATOM 2321 N N . PRO A 1 303 ? -76.851 26.533 -30.632 1.00 169.74 ? 330 PRO A N 1 ATOM 2322 C CA . PRO A 1 303 ? -78.057 26.174 -31.393 1.00 173.06 ? 330 PRO A CA 1 ATOM 2323 C C . PRO A 1 303 ? -78.351 26.957 -32.672 1.00 177.17 ? 330 PRO A C 1 ATOM 2324 O O . PRO A 1 303 ? -78.059 28.148 -32.775 1.00 180.12 ? 330 PRO A O 1 ATOM 2325 C CB . PRO A 1 303 ? -79.179 26.420 -30.382 1.00 174.53 ? 330 PRO A CB 1 ATOM 2326 C CG . PRO A 1 303 ? -78.554 26.162 -29.076 1.00 174.94 ? 330 PRO A CG 1 ATOM 2327 C CD . PRO A 1 303 ? -77.151 26.677 -29.194 1.00 174.65 ? 330 PRO A CD 1 ATOM 2328 N N . LYS A 1 304 ? -78.937 26.253 -33.638 1.00 179.31 ? 331 LYS A N 1 ATOM 2329 C CA . LYS A 1 304 ? -79.534 26.860 -34.822 1.00 177.61 ? 331 LYS A CA 1 ATOM 2330 C C . LYS A 1 304 ? -80.884 27.471 -34.450 1.00 170.65 ? 331 LYS A C 1 ATOM 2331 O O . LYS A 1 304 ? -81.401 27.203 -33.365 1.00 175.76 ? 331 LYS A O 1 ATOM 2332 C CB . LYS A 1 304 ? -79.708 25.816 -35.933 1.00 179.51 ? 331 LYS A CB 1 ATOM 2333 C CG . LYS A 1 304 ? -78.552 25.736 -36.913 1.00 180.07 ? 331 LYS A CG 1 ATOM 2334 C CD . LYS A 1 304 ? -78.872 24.795 -38.064 1.00 179.78 ? 331 LYS A CD 1 ATOM 2335 C CE . LYS A 1 304 ? -79.131 23.387 -37.562 1.00 178.74 ? 331 LYS A CE 1 ATOM 2336 N NZ . LYS A 1 304 ? -79.402 22.430 -38.669 1.00 181.34 ? 331 LYS A NZ 1 ATOM 2337 N N . PRO A 1 305 ? -81.459 28.303 -35.337 1.00 167.75 ? 332 PRO A N 1 ATOM 2338 C CA . PRO A 1 305 ? -82.811 28.797 -35.057 1.00 166.88 ? 332 PRO A CA 1 ATOM 2339 C C . PRO A 1 305 ? -83.848 27.674 -35.040 1.00 173.64 ? 332 PRO A C 1 ATOM 2340 O O . PRO A 1 305 ? -83.902 26.885 -35.984 1.00 172.85 ? 332 PRO A O 1 ATOM 2341 C CB . PRO A 1 305 ? -83.078 29.769 -36.211 1.00 157.62 ? 332 PRO A CB 1 ATOM 2342 C CG . PRO A 1 305 ? -82.110 29.382 -37.277 1.00 155.57 ? 332 PRO A CG 1 ATOM 2343 C CD . PRO A 1 305 ? -80.891 28.931 -36.542 1.00 160.35 ? 332 PRO A CD 1 ATOM 2344 N N . PRO A 1 306 ? -84.653 27.597 -33.967 1.00 178.27 ? 333 PRO A N 1 ATOM 2345 C CA . PRO A 1 306 ? -85.712 26.590 -33.821 1.00 179.79 ? 333 PRO A CA 1 ATOM 2346 C C . PRO A 1 306 ? -86.748 26.627 -34.945 1.00 185.45 ? 333 PRO A C 1 ATOM 2347 O O . PRO A 1 306 ? -86.915 27.653 -35.604 1.00 184.97 ? 333 PRO A O 1 ATOM 2348 C CB . PRO A 1 306 ? -86.357 26.957 -32.479 1.00 179.27 ? 333 PRO A CB 1 ATOM 2349 C CG . PRO A 1 306 ? -85.273 27.635 -31.720 1.00 179.18 ? 333 PRO A CG 1 ATOM 2350 C CD . PRO A 1 306 ? -84.500 28.411 -32.748 1.00 178.57 ? 333 PRO A CD 1 ATOM 2351 N N . GLY A 1 307 ? -87.432 25.505 -35.154 1.00 193.10 ? 334 GLY A N 1 ATOM 2352 C CA . GLY A 1 307 ? -88.462 25.410 -36.173 1.00 197.44 ? 334 GLY A CA 1 ATOM 2353 C C . GLY A 1 307 ? -89.753 26.083 -35.748 1.00 200.02 ? 334 GLY A C 1 ATOM 2354 O O . GLY A 1 307 ? -90.374 25.673 -34.768 1.00 206.49 ? 334 GLY A O 1 ATOM 2355 N N . THR A 1 308 ? -90.138 27.110 -36.506 1.00 188.54 ? 335 THR A N 1 ATOM 2356 C CA . THR A 1 308 ? -91.305 27.969 -36.257 1.00 202.56 ? 335 THR A CA 1 ATOM 2357 C C . THR A 1 308 ? -92.447 27.352 -35.443 1.00 212.17 ? 335 THR A C 1 ATOM 2358 O O . THR A 1 308 ? -92.955 26.283 -35.786 1.00 210.97 ? 335 THR A O 1 ATOM 2359 C CB . THR A 1 308 ? -91.893 28.458 -37.599 1.00 207.66 ? 335 THR A CB 1 ATOM 2360 O OG1 . THR A 1 308 ? -90.896 29.197 -38.315 1.00 211.38 ? 335 THR A OG1 1 ATOM 2361 C CG2 . THR A 1 308 ? -93.110 29.344 -37.373 1.00 211.09 ? 335 THR A CG2 1 ATOM 2362 N N . PRO A 1 309 ? -92.850 28.036 -34.359 1.00 213.48 ? 336 PRO A N 1 ATOM 2363 C CA . PRO A 1 309 ? -93.918 27.600 -33.450 1.00 215.10 ? 336 PRO A CA 1 ATOM 2364 C C . PRO A 1 309 ? -95.297 27.566 -34.106 1.00 215.21 ? 336 PRO A C 1 ATOM 2365 O O . PRO A 1 309 ? -95.539 28.261 -35.093 1.00 216.00 ? 336 PRO A O 1 ATOM 2366 C CB . PRO A 1 309 ? -93.878 28.650 -32.335 1.00 217.18 ? 336 PRO A CB 1 ATOM 2367 C CG . PRO A 1 309 ? -93.279 29.853 -32.973 1.00 217.54 ? 336 PRO A CG 1 ATOM 2368 C CD . PRO A 1 309 ? -92.261 29.317 -33.931 1.00 215.47 ? 336 PRO A CD 1 ATOM 2369 N N . VAL A 1 310 ? -96.190 26.753 -33.547 1.00 204.33 ? 337 VAL A N 1 ATOM 2370 C CA . VAL A 1 310 ? -97.541 26.592 -34.074 1.00 199.09 ? 337 VAL A CA 1 ATOM 2371 C C . VAL A 1 310 ? -98.566 26.729 -32.947 1.00 213.84 ? 337 VAL A C 1 ATOM 2372 O O . VAL A 1 310 ? -98.341 26.251 -31.835 1.00 221.51 ? 337 VAL A O 1 ATOM 2373 C CB . VAL A 1 310 ? -97.713 25.222 -34.772 1.00 185.51 ? 337 VAL A CB 1 ATOM 2374 C CG1 . VAL A 1 310 ? -99.081 25.119 -35.427 1.00 187.25 ? 337 VAL A CG1 1 ATOM 2375 C CG2 . VAL A 1 310 ? -96.614 25.000 -35.804 1.00 177.25 ? 337 VAL A CG2 1 ATOM 2376 N N . VAL A 1 311 ? -99.686 27.385 -33.235 1.00 217.20 ? 338 VAL A N 1 ATOM 2377 C CA . VAL A 1 311 ? -100.732 27.602 -32.238 1.00 222.30 ? 338 VAL A CA 1 ATOM 2378 C C . VAL A 1 311 ? -101.687 26.411 -32.153 1.00 226.45 ? 338 VAL A C 1 ATOM 2379 O O . VAL A 1 311 ? -102.534 26.224 -33.027 1.00 227.06 ? 338 VAL A O 1 ATOM 2380 C CB . VAL A 1 311 ? -101.541 28.877 -32.550 1.00 221.35 ? 338 VAL A CB 1 ATOM 2381 C CG1 . VAL A 1 311 ? -102.599 29.113 -31.482 1.00 223.70 ? 338 VAL A CG1 1 ATOM 2382 C CG2 . VAL A 1 311 ? -100.614 30.077 -32.666 1.00 220.56 ? 338 VAL A CG2 1 ATOM 2383 N N . THR A 1 312 ? -101.555 25.613 -31.096 1.00 231.10 ? 339 THR A N 1 ATOM 2384 C CA . THR A 1 312 ? -102.373 24.411 -30.942 1.00 227.85 ? 339 THR A CA 1 ATOM 2385 C C . THR A 1 312 ? -103.627 24.632 -30.099 1.00 225.52 ? 339 THR A C 1 ATOM 2386 O O . THR A 1 312 ? -104.693 24.107 -30.421 1.00 228.06 ? 339 THR A O 1 ATOM 2387 C CB . THR A 1 312 ? -101.568 23.259 -30.312 1.00 220.77 ? 339 THR A CB 1 ATOM 2388 O OG1 . THR A 1 312 ? -100.868 23.734 -29.155 1.00 217.51 ? 339 THR A OG1 1 ATOM 2389 C CG2 . THR A 1 312 ? -100.572 22.703 -31.311 1.00 218.36 ? 339 THR A CG2 1 ATOM 2390 N N . GLU A 1 313 ? -103.501 25.389 -29.014 1.00 219.04 ? 340 GLU A N 1 ATOM 2391 C CA . GLU A 1 313 ? -104.635 25.628 -28.122 1.00 213.73 ? 340 GLU A CA 1 ATOM 2392 C C . GLU A 1 313 ? -104.668 27.063 -27.613 1.00 207.98 ? 340 GLU A C 1 ATOM 2393 O O . GLU A 1 313 ? -103.827 27.460 -26.812 1.00 214.28 ? 340 GLU A O 1 ATOM 2394 C CB . GLU A 1 313 ? -104.596 24.667 -26.931 1.00 217.71 ? 340 GLU A CB 1 ATOM 2395 C CG . GLU A 1 313 ? -104.741 23.199 -27.292 1.00 219.74 ? 340 GLU A CG 1 ATOM 2396 C CD . GLU A 1 313 ? -104.683 22.298 -26.076 1.00 218.00 ? 340 GLU A CD 1 ATOM 2397 O OE1 . GLU A 1 313 ? -105.182 22.709 -25.007 1.00 217.35 ? 340 GLU A OE1 1 ATOM 2398 O OE2 . GLU A 1 313 ? -104.131 21.184 -26.186 1.00 216.19 ? 340 GLU A OE2 1 ATOM 2399 N N . SER A 1 314 ? -105.651 27.835 -28.062 1.00 204.78 ? 341 SER A N 1 ATOM 2400 C CA . SER A 1 314 ? -105.749 29.232 -27.657 1.00 201.95 ? 341 SER A CA 1 ATOM 2401 C C . SER A 1 314 ? -107.034 29.536 -26.891 1.00 207.54 ? 341 SER A C 1 ATOM 2402 O O . SER A 1 314 ? -108.138 29.316 -27.389 1.00 211.03 ? 341 SER A O 1 ATOM 2403 C CB . SER A 1 314 ? -105.639 30.145 -28.880 1.00 194.17 ? 341 SER A CB 1 ATOM 2404 O OG . SER A 1 314 ? -106.455 29.679 -29.941 1.00 191.95 ? 341 SER A OG 1 ATOM 2405 N N . THR A 1 315 ? -106.872 30.038 -25.670 1.00 206.82 ? 342 THR A N 1 ATOM 2406 C CA . THR A 1 315 ? -107.986 30.511 -24.858 1.00 213.25 ? 342 THR A CA 1 ATOM 2407 C C . THR A 1 315 ? -107.835 32.006 -24.589 1.00 221.53 ? 342 THR A C 1 ATOM 2408 O O . THR A 1 315 ? -106.748 32.563 -24.755 1.00 219.80 ? 342 THR A O 1 ATOM 2409 C CB . THR A 1 315 ? -108.078 29.763 -23.516 1.00 213.05 ? 342 THR A CB 1 ATOM 2410 O OG1 . THR A 1 315 ? -107.065 30.245 -22.624 1.00 212.06 ? 342 THR A OG1 1 ATOM 2411 C CG2 . THR A 1 315 ? -107.905 28.267 -23.723 1.00 214.21 ? 342 THR A CG2 1 ATOM 2412 N N . ALA A 1 316 ? -108.926 32.633 -24.151 1.00 234.49 ? 343 ALA A N 1 ATOM 2413 C CA . ALA A 1 316 ? -109.004 34.083 -23.962 1.00 241.87 ? 343 ALA A CA 1 ATOM 2414 C C . ALA A 1 316 ? -107.786 34.683 -23.262 1.00 247.00 ? 343 ALA A C 1 ATOM 2415 O O . ALA A 1 316 ? -107.364 35.794 -23.583 1.00 245.92 ? 343 ALA A O 1 ATOM 2416 C CB . ALA A 1 316 ? -110.269 34.433 -23.187 1.00 244.27 ? 343 ALA A CB 1 ATOM 2417 N N . THR A 1 317 ? -107.219 33.944 -22.314 1.00 254.74 ? 344 THR A N 1 ATOM 2418 C CA . THR A 1 317 ? -106.070 34.436 -21.565 1.00 253.29 ? 344 THR A CA 1 ATOM 2419 C C . THR A 1 317 ? -104.893 33.460 -21.560 1.00 249.90 ? 344 THR A C 1 ATOM 2420 O O . THR A 1 317 ? -104.040 33.523 -20.675 1.00 254.93 ? 344 THR A O 1 ATOM 2421 C CB . THR A 1 317 ? -106.447 34.745 -20.103 1.00 257.23 ? 344 THR A CB 1 ATOM 2422 O OG1 . THR A 1 317 ? -106.908 33.549 -19.464 1.00 261.37 ? 344 THR A OG1 1 ATOM 2423 C CG2 . THR A 1 317 ? -107.539 35.803 -20.040 1.00 260.76 ? 344 THR A CG2 1 ATOM 2424 N N . SER A 1 318 ? -104.840 32.564 -22.541 1.00 232.99 ? 345 SER A N 1 ATOM 2425 C CA . SER A 1 318 ? -103.720 31.627 -22.630 1.00 219.09 ? 345 SER A CA 1 ATOM 2426 C C . SER A 1 318 ? -103.440 31.223 -24.071 1.00 206.45 ? 345 SER A C 1 ATOM 2427 O O . SER A 1 318 ? -104.348 31.168 -24.892 1.00 209.26 ? 345 SER A O 1 ATOM 2428 C CB . SER A 1 318 ? -103.991 30.379 -21.788 1.00 222.28 ? 345 SER A CB 1 ATOM 2429 O OG . SER A 1 318 ? -104.853 29.485 -22.470 1.00 225.50 ? 345 SER A OG 1 ATOM 2430 N N . ILE A 1 319 ? -102.176 30.949 -24.378 1.00 193.23 ? 346 ILE A N 1 ATOM 2431 C CA . ILE A 1 319 ? -101.808 30.494 -25.714 1.00 185.07 ? 346 ILE A CA 1 ATOM 2432 C C . ILE A 1 319 ? -100.749 29.396 -25.664 1.00 183.74 ? 346 ILE A C 1 ATOM 2433 O O . ILE A 1 319 ? -99.614 29.617 -25.234 1.00 177.68 ? 346 ILE A O 1 ATOM 2434 C CB . ILE A 1 319 ? -101.302 31.655 -26.591 1.00 181.60 ? 346 ILE A CB 1 ATOM 2435 C CG1 . ILE A 1 319 ? -102.473 32.542 -27.018 1.00 183.04 ? 346 ILE A CG1 1 ATOM 2436 C CG2 . ILE A 1 319 ? -100.612 31.122 -27.830 1.00 180.98 ? 346 ILE A CG2 1 ATOM 2437 C CD1 . ILE A 1 319 ? -102.080 33.674 -27.933 1.00 183.95 ? 346 ILE A CD1 1 ATOM 2438 N N . THR A 1 320 ? -101.141 28.208 -26.110 1.00 190.22 ? 347 THR A N 1 ATOM 2439 C CA . THR A 1 320 ? -100.261 27.051 -26.110 1.00 193.60 ? 347 THR A CA 1 ATOM 2440 C C . THR A 1 320 ? -99.428 26.996 -27.383 1.00 202.73 ? 347 THR A C 1 ATOM 2441 O O . THR A 1 320 ? -99.949 27.135 -28.491 1.00 203.40 ? 347 THR A O 1 ATOM 2442 C CB . THR A 1 320 ? -101.056 25.742 -25.968 1.00 186.99 ? 347 THR A CB 1 ATOM 2443 O OG1 . THR A 1 320 ? -101.896 25.814 -24.808 1.00 184.69 ? 347 THR A OG1 1 ATOM 2444 C CG2 . THR A 1 320 ? -100.111 24.560 -25.832 1.00 183.65 ? 347 THR A CG2 1 ATOM 2445 N N . LEU A 1 321 ? -98.129 26.787 -27.210 1.00 210.73 ? 348 LEU A N 1 ATOM 2446 C CA . LEU A 1 321 ? -97.193 26.757 -28.322 1.00 212.11 ? 348 LEU A CA 1 ATOM 2447 C C . LEU A 1 321 ? -96.485 25.414 -28.424 1.00 209.71 ? 348 LEU A C 1 ATOM 2448 O O . LEU A 1 321 ? -95.908 24.938 -27.446 1.00 214.37 ? 348 LEU A O 1 ATOM 2449 C CB . LEU A 1 321 ? -96.163 27.875 -28.169 1.00 213.55 ? 348 LEU A CB 1 ATOM 2450 C CG . LEU A 1 321 ? -96.276 29.063 -29.121 1.00 219.18 ? 348 LEU A CG 1 ATOM 2451 C CD1 . LEU A 1 321 ? -97.720 29.503 -29.267 1.00 223.87 ? 348 LEU A CD1 1 ATOM 2452 C CD2 . LEU A 1 321 ? -95.418 30.210 -28.620 1.00 220.75 ? 348 LEU A CD2 1 ATOM 2453 N N . THR A 1 322 ? -96.536 24.809 -29.608 1.00 185.96 ? 349 THR A N 1 ATOM 2454 C CA . THR A 1 322 ? -95.790 23.586 -29.883 1.00 170.97 ? 349 THR A CA 1 ATOM 2455 C C . THR A 1 322 ? -94.844 23.805 -31.056 1.00 168.65 ? 349 THR A C 1 ATOM 2456 O O . THR A 1 322 ? -95.267 24.188 -32.146 1.00 175.28 ? 349 THR A O 1 ATOM 2457 C CB . THR A 1 322 ? -96.717 22.397 -30.200 1.00 166.15 ? 349 THR A CB 1 ATOM 2458 O OG1 . THR A 1 322 ? -97.387 22.628 -31.445 1.00 165.98 ? 349 THR A OG1 1 ATOM 2459 C CG2 . THR A 1 322 ? -97.742 22.205 -29.098 1.00 166.36 ? 349 THR A CG2 1 ATOM 2460 N N . TRP A 1 323 ? -93.559 23.560 -30.831 1.00 161.49 ? 350 TRP A N 1 ATOM 2461 C CA . TRP A 1 323 ? -92.565 23.781 -31.868 1.00 166.66 ? 350 TRP A CA 1 ATOM 2462 C C . TRP A 1 323 ? -91.650 22.577 -32.035 1.00 167.62 ? 350 TRP A C 1 ATOM 2463 O O . TRP A 1 323 ? -91.839 21.540 -31.398 1.00 163.66 ? 350 TRP A O 1 ATOM 2464 C CB . TRP A 1 323 ? -91.736 25.034 -31.554 1.00 172.90 ? 350 TRP A CB 1 ATOM 2465 C CG . TRP A 1 323 ? -90.964 24.976 -30.253 1.00 175.69 ? 350 TRP A CG 1 ATOM 2466 C CD1 . TRP A 1 323 ? -89.694 24.504 -30.073 1.00 174.95 ? 350 TRP A CD1 1 ATOM 2467 C CD2 . TRP A 1 323 ? -91.408 25.426 -28.964 1.00 173.96 ? 350 TRP A CD2 1 ATOM 2468 N NE1 . TRP A 1 323 ? -89.325 24.625 -28.754 1.00 173.32 ? 350 TRP A NE1 1 ATOM 2469 C CE2 . TRP A 1 323 ? -90.359 25.188 -28.053 1.00 171.82 ? 350 TRP A CE2 1 ATOM 2470 C CE3 . TRP A 1 323 ? -92.592 26.002 -28.492 1.00 172.21 ? 350 TRP A CE3 1 ATOM 2471 C CZ2 . TRP A 1 323 ? -90.458 25.505 -26.699 1.00 169.27 ? 350 TRP A CZ2 1 ATOM 2472 C CZ3 . TRP A 1 323 ? -92.689 26.316 -27.147 1.00 169.84 ? 350 TRP A CZ3 1 ATOM 2473 C CH2 . TRP A 1 323 ? -91.628 26.067 -26.267 1.00 168.96 ? 350 TRP A CH2 1 ATOM 2474 N N . ASP A 1 324 ? -90.668 22.719 -32.915 1.00 174.59 ? 351 ASP A N 1 ATOM 2475 C CA . ASP A 1 324 ? -89.594 21.747 -33.020 1.00 176.28 ? 351 ASP A CA 1 ATOM 2476 C C . ASP A 1 324 ? -88.304 22.441 -32.604 1.00 174.42 ? 351 ASP A C 1 ATOM 2477 O O . ASP A 1 324 ? -88.190 23.660 -32.724 1.00 183.12 ? 351 ASP A O 1 ATOM 2478 C CB . ASP A 1 324 ? -89.486 21.186 -34.436 1.00 180.01 ? 351 ASP A CB 1 ATOM 2479 C CG . ASP A 1 324 ? -88.666 19.913 -34.494 1.00 183.45 ? 351 ASP A CG 1 ATOM 2480 O OD1 . ASP A 1 324 ? -88.990 18.962 -33.752 1.00 186.66 ? 351 ASP A OD1 1 ATOM 2481 O OD2 . ASP A 1 324 ? -87.690 19.867 -35.271 1.00 182.63 ? 351 ASP A OD2 1 ATOM 2482 N N . SER A 1 325 ? -87.340 21.671 -32.111 1.00 158.54 ? 352 SER A N 1 ATOM 2483 C CA . SER A 1 325 ? -86.112 22.246 -31.571 1.00 141.51 ? 352 SER A CA 1 ATOM 2484 C C . SER A 1 325 ? -85.339 23.041 -32.620 1.00 135.81 ? 352 SER A C 1 ATOM 2485 O O . SER A 1 325 ? -84.643 23.998 -32.288 1.00 128.45 ? 352 SER A O 1 ATOM 2486 C CB . SER A 1 325 ? -85.218 21.149 -30.991 1.00 136.21 ? 352 SER A CB 1 ATOM 2487 O OG . SER A 1 325 ? -84.392 20.582 -31.990 1.00 136.85 ? 352 SER A OG 1 ATOM 2488 N N . GLY A 1 326 ? -85.471 22.644 -33.883 1.00 149.77 ? 353 GLY A N 1 ATOM 2489 C CA . GLY A 1 326 ? -84.758 23.293 -34.969 1.00 152.73 ? 353 GLY A CA 1 ATOM 2490 C C . GLY A 1 326 ? -83.267 23.071 -34.835 1.00 151.99 ? 353 GLY A C 1 ATOM 2491 O O . GLY A 1 326 ? -82.459 23.937 -35.172 1.00 152.72 ? 353 GLY A O 1 ATOM 2492 N N . ASN A 1 327 ? -82.910 21.893 -34.338 1.00 152.98 ? 354 ASN A N 1 ATOM 2493 C CA . ASN A 1 327 ? -81.527 21.573 -34.018 1.00 161.46 ? 354 ASN A CA 1 ATOM 2494 C C . ASN A 1 327 ? -81.199 20.111 -34.267 1.00 170.16 ? 354 ASN A C 1 ATOM 2495 O O . ASN A 1 327 ? -82.067 19.248 -34.140 1.00 174.88 ? 354 ASN A O 1 ATOM 2496 C CB . ASN A 1 327 ? -81.232 21.912 -32.557 1.00 160.94 ? 354 ASN A CB 1 ATOM 2497 C CG . ASN A 1 327 ? -80.652 23.295 -32.385 1.00 158.29 ? 354 ASN A CG 1 ATOM 2498 O OD1 . ASN A 1 327 ? -79.459 23.447 -32.132 1.00 154.06 ? 354 ASN A OD1 1 ATOM 2499 N ND2 . ASN A 1 327 ? -81.491 24.314 -32.524 1.00 161.15 ? 354 ASN A ND2 1 ATOM 2500 N N . PRO A 1 328 ? -79.941 19.828 -34.634 1.00 174.07 ? 355 PRO A N 1 ATOM 2501 C CA . PRO A 1 328 ? -79.461 18.445 -34.680 1.00 178.76 ? 355 PRO A CA 1 ATOM 2502 C C . PRO A 1 328 ? -79.032 17.952 -33.294 1.00 186.39 ? 355 PRO A C 1 ATOM 2503 O O . PRO A 1 328 ? -79.357 16.827 -32.913 1.00 188.44 ? 355 PRO A O 1 ATOM 2504 C CB . PRO A 1 328 ? -78.272 18.519 -35.641 1.00 176.52 ? 355 PRO A CB 1 ATOM 2505 C CG . PRO A 1 328 ? -77.768 19.915 -35.506 1.00 173.96 ? 355 PRO A CG 1 ATOM 2506 C CD . PRO A 1 328 ? -78.963 20.778 -35.193 1.00 172.59 ? 355 PRO A CD 1 ATOM 2507 N N . GLU A 1 329 ? -78.324 18.799 -32.550 1.00 188.81 ? 356 GLU A N 1 ATOM 2508 C CA . GLU A 1 329 ? -77.825 18.451 -31.223 1.00 189.00 ? 356 GLU A CA 1 ATOM 2509 C C . GLU A 1 329 ? -78.873 18.685 -30.136 1.00 185.11 ? 356 GLU A C 1 ATOM 2510 O O . GLU A 1 329 ? -79.747 19.541 -30.289 1.00 186.31 ? 356 GLU A O 1 ATOM 2511 C CB . GLU A 1 329 ? -76.558 19.254 -30.912 1.00 197.91 ? 356 GLU A CB 1 ATOM 2512 C CG . GLU A 1 329 ? -75.297 18.696 -31.554 1.00 206.96 ? 356 GLU A CG 1 ATOM 2513 C CD . GLU A 1 329 ? -74.838 17.404 -30.905 1.00 214.47 ? 356 GLU A CD 1 ATOM 2514 O OE1 . GLU A 1 329 ? -74.642 17.393 -29.671 1.00 215.05 ? 356 GLU A OE1 1 ATOM 2515 O OE2 . GLU A 1 329 ? -74.674 16.399 -31.627 1.00 219.53 ? 356 GLU A OE2 1 ATOM 2516 N N . PRO A 1 330 ? -78.791 17.912 -29.037 1.00 180.63 ? 357 PRO A N 1 ATOM 2517 C CA . PRO A 1 330 ? -79.698 18.048 -27.891 1.00 181.14 ? 357 PRO A CA 1 ATOM 2518 C C . PRO A 1 330 ? -79.808 19.481 -27.380 1.00 185.76 ? 357 PRO A C 1 ATOM 2519 O O . PRO A 1 330 ? -78.799 20.104 -27.045 1.00 187.33 ? 357 PRO A O 1 ATOM 2520 C CB . PRO A 1 330 ? -79.055 17.147 -26.835 1.00 173.65 ? 357 PRO A CB 1 ATOM 2521 C CG . PRO A 1 330 ? -78.368 16.099 -27.620 1.00 171.57 ? 357 PRO A CG 1 ATOM 2522 C CD . PRO A 1 330 ? -77.861 16.782 -28.863 1.00 174.55 ? 357 PRO A CD 1 ATOM 2523 N N . VAL A 1 331 ? -81.034 19.990 -27.327 1.00 183.86 ? 358 VAL A N 1 ATOM 2524 C CA . VAL A 1 331 ? -81.288 21.335 -26.832 1.00 188.99 ? 358 VAL A CA 1 ATOM 2525 C C . VAL A 1 331 ? -81.647 21.290 -25.352 1.00 192.94 ? 358 VAL A C 1 ATOM 2526 O O . VAL A 1 331 ? -82.664 20.709 -24.970 1.00 202.67 ? 358 VAL A O 1 ATOM 2527 C CB . VAL A 1 331 ? -82.418 22.018 -27.616 1.00 189.92 ? 358 VAL A CB 1 ATOM 2528 C CG1 . VAL A 1 331 ? -82.433 23.508 -27.321 1.00 192.98 ? 358 VAL A CG1 1 ATOM 2529 C CG2 . VAL A 1 331 ? -82.239 21.773 -29.101 1.00 192.18 ? 358 VAL A CG2 1 ATOM 2530 N N . SER A 1 332 ? -80.808 21.908 -24.526 1.00 185.11 ? 359 SER A N 1 ATOM 2531 C CA . SER A 1 332 ? -80.941 21.811 -23.075 1.00 173.09 ? 359 SER A CA 1 ATOM 2532 C C . SER A 1 332 ? -82.235 22.443 -22.559 1.00 169.33 ? 359 SER A C 1 ATOM 2533 O O . SER A 1 332 ? -82.872 21.890 -21.663 1.00 171.83 ? 359 SER A O 1 ATOM 2534 C CB . SER A 1 332 ? -79.727 22.443 -22.394 1.00 163.06 ? 359 SER A CB 1 ATOM 2535 O OG . SER A 1 332 ? -78.546 21.726 -22.719 1.00 157.12 ? 359 SER A OG 1 ATOM 2536 N N . TYR A 1 333 ? -82.620 23.588 -23.121 1.00 163.31 ? 360 TYR A N 1 ATOM 2537 C CA . TYR A 1 333 ? -83.935 24.175 -22.842 1.00 161.98 ? 360 TYR A CA 1 ATOM 2538 C C . TYR A 1 333 ? -84.292 25.325 -23.784 1.00 169.28 ? 360 TYR A C 1 ATOM 2539 O O . TYR A 1 333 ? -83.468 25.773 -24.582 1.00 171.63 ? 360 TYR A O 1 ATOM 2540 C CB . TYR A 1 333 ? -84.022 24.658 -21.391 1.00 156.30 ? 360 TYR A CB 1 ATOM 2541 C CG . TYR A 1 333 ? -82.913 25.586 -20.957 1.00 152.49 ? 360 TYR A CG 1 ATOM 2542 C CD1 . TYR A 1 333 ? -81.739 25.088 -20.407 1.00 149.57 ? 360 TYR A CD1 1 ATOM 2543 C CD2 . TYR A 1 333 ? -83.049 26.961 -21.078 1.00 150.58 ? 360 TYR A CD2 1 ATOM 2544 C CE1 . TYR A 1 333 ? -80.726 25.934 -20.003 1.00 146.56 ? 360 TYR A CE1 1 ATOM 2545 C CE2 . TYR A 1 333 ? -82.044 27.814 -20.676 1.00 148.90 ? 360 TYR A CE2 1 ATOM 2546 C CZ . TYR A 1 333 ? -80.886 27.296 -20.139 1.00 146.69 ? 360 TYR A CZ 1 ATOM 2547 O OH . TYR A 1 333 ? -79.886 28.150 -19.741 1.00 146.87 ? 360 TYR A OH 1 ATOM 2548 N N . TYR A 1 334 ? -85.530 25.799 -23.673 1.00 173.68 ? 361 TYR A N 1 ATOM 2549 C CA . TYR A 1 334 ? -86.055 26.819 -24.575 1.00 181.12 ? 361 TYR A CA 1 ATOM 2550 C C . TYR A 1 334 ? -86.573 28.054 -23.838 1.00 191.97 ? 361 TYR A C 1 ATOM 2551 O O . TYR A 1 334 ? -87.091 27.958 -22.726 1.00 190.20 ? 361 TYR A O 1 ATOM 2552 C CB . TYR A 1 334 ? -87.181 26.240 -25.434 1.00 185.31 ? 361 TYR A CB 1 ATOM 2553 C CG . TYR A 1 334 ? -86.853 24.925 -26.105 1.00 189.97 ? 361 TYR A CG 1 ATOM 2554 C CD1 . TYR A 1 334 ? -87.240 23.717 -25.537 1.00 193.41 ? 361 TYR A CD1 1 ATOM 2555 C CD2 . TYR A 1 334 ? -86.170 24.890 -27.313 1.00 191.31 ? 361 TYR A CD2 1 ATOM 2556 C CE1 . TYR A 1 334 ? -86.950 22.510 -26.151 1.00 193.93 ? 361 TYR A CE1 1 ATOM 2557 C CE2 . TYR A 1 334 ? -85.877 23.687 -27.936 1.00 193.44 ? 361 TYR A CE2 1 ATOM 2558 C CZ . TYR A 1 334 ? -86.269 22.500 -27.348 1.00 191.46 ? 361 TYR A CZ 1 ATOM 2559 O OH . TYR A 1 334 ? -85.983 21.299 -27.955 1.00 187.58 ? 361 TYR A OH 1 ATOM 2560 N N . ILE A 1 335 ? -86.435 29.208 -24.486 1.00 207.71 ? 362 ILE A N 1 ATOM 2561 C CA . ILE A 1 335 ? -86.899 30.492 -23.973 1.00 223.25 ? 362 ILE A CA 1 ATOM 2562 C C . ILE A 1 335 ? -87.905 31.112 -24.937 1.00 267.84 ? 362 ILE A C 1 ATOM 2563 O O . ILE A 1 335 ? -87.581 31.359 -26.095 1.00 270.26 ? 362 ILE A O 1 ATOM 2564 C CB . ILE A 1 335 ? -85.737 31.487 -23.785 1.00 201.33 ? 362 ILE A CB 1 ATOM 2565 C CG1 . ILE A 1 335 ? -84.473 30.774 -23.310 1.00 187.68 ? 362 ILE A CG1 1 ATOM 2566 C CG2 . ILE A 1 335 ? -86.128 32.604 -22.830 1.00 201.50 ? 362 ILE A CG2 1 ATOM 2567 C CD1 . ILE A 1 335 ? -83.283 31.696 -23.229 1.00 182.85 ? 362 ILE A CD1 1 ATOM 2568 N N . ILE A 1 336 ? -89.117 31.379 -24.462 1.00 311.81 ? 363 ILE A N 1 ATOM 2569 C CA . ILE A 1 336 ? -90.164 31.932 -25.319 1.00 318.35 ? 363 ILE A CA 1 ATOM 2570 C C . ILE A 1 336 ? -90.239 33.458 -25.241 1.00 317.89 ? 363 ILE A C 1 ATOM 2571 O O . ILE A 1 336 ? -90.299 34.026 -24.153 1.00 322.92 ? 363 ILE A O 1 ATOM 2572 C CB . ILE A 1 336 ? -91.542 31.339 -24.958 1.00 328.45 ? 363 ILE A CB 1 ATOM 2573 C CG1 . ILE A 1 336 ? -91.684 29.937 -25.549 1.00 326.52 ? 363 ILE A CG1 1 ATOM 2574 C CG2 . ILE A 1 336 ? -92.669 32.228 -25.460 1.00 330.25 ? 363 ILE A CG2 1 ATOM 2575 C CD1 . ILE A 1 336 ? -93.052 29.335 -25.342 1.00 328.57 ? 363 ILE A CD1 1 ATOM 2576 N N . GLN A 1 337 ? -90.233 34.117 -26.398 1.00 286.54 ? 364 GLN A N 1 ATOM 2577 C CA . GLN A 1 337 ? -90.380 35.570 -26.454 1.00 272.26 ? 364 GLN A CA 1 ATOM 2578 C C . GLN A 1 337 ? -91.810 35.975 -26.812 1.00 284.41 ? 364 GLN A C 1 ATOM 2579 O O . GLN A 1 337 ? -92.389 35.448 -27.765 1.00 297.56 ? 364 GLN A O 1 ATOM 2580 C CB . GLN A 1 337 ? -89.409 36.175 -27.470 1.00 253.52 ? 364 GLN A CB 1 ATOM 2581 C CG . GLN A 1 337 ? -87.940 36.035 -27.117 1.00 232.06 ? 364 GLN A CG 1 ATOM 2582 C CD . GLN A 1 337 ? -87.054 36.827 -28.055 1.00 206.91 ? 364 GLN A CD 1 ATOM 2583 O OE1 . GLN A 1 337 ? -87.531 37.421 -29.023 1.00 198.94 ? 364 GLN A OE1 1 ATOM 2584 N NE2 . GLN A 1 337 ? -85.758 36.845 -27.772 1.00 194.32 ? 364 GLN A NE2 1 ATOM 2585 N N . HIS A 1 338 ? -92.371 36.918 -26.057 1.00 278.94 ? 365 HIS A N 1 ATOM 2586 C CA . HIS A 1 338 ? -93.732 37.388 -26.309 1.00 277.70 ? 365 HIS A CA 1 ATOM 2587 C C . HIS A 1 338 ? -93.921 38.890 -26.065 1.00 276.42 ? 365 HIS A C 1 ATOM 2588 O O . HIS A 1 338 ? -93.350 39.464 -25.131 1.00 274.87 ? 365 HIS A O 1 ATOM 2589 C CB . HIS A 1 338 ? -94.734 36.591 -25.461 1.00 279.66 ? 365 HIS A CB 1 ATOM 2590 C CG . HIS A 1 338 ? -94.628 36.831 -23.985 1.00 282.54 ? 365 HIS A CG 1 ATOM 2591 N ND1 . HIS A 1 338 ? -95.509 37.639 -23.299 1.00 284.54 ? 365 HIS A ND1 1 ATOM 2592 C CD2 . HIS A 1 338 ? -93.765 36.347 -23.061 1.00 282.88 ? 365 HIS A CD2 1 ATOM 2593 C CE1 . HIS A 1 338 ? -95.184 37.654 -22.018 1.00 285.74 ? 365 HIS A CE1 1 ATOM 2594 N NE2 . HIS A 1 338 ? -94.128 36.879 -21.848 1.00 284.53 ? 365 HIS A NE2 1 ATOM 2595 N N . LYS A 1 339 ? -94.723 39.508 -26.934 1.00 242.84 ? 366 LYS A N 1 ATOM 2596 C CA . LYS A 1 339 ? -95.099 40.917 -26.832 1.00 223.27 ? 366 LYS A CA 1 ATOM 2597 C C . LYS A 1 339 ? -96.288 41.223 -27.761 1.00 218.69 ? 366 LYS A C 1 ATOM 2598 O O . LYS A 1 339 ? -96.570 40.451 -28.701 1.00 225.14 ? 366 LYS A O 1 ATOM 2599 C CB . LYS A 1 339 ? -93.908 41.831 -27.163 1.00 213.70 ? 366 LYS A CB 1 ATOM 2600 C CG . LYS A 1 339 ? -93.594 41.978 -28.648 1.00 203.00 ? 366 LYS A CG 1 ATOM 2601 C CD . LYS A 1 339 ? -92.613 43.124 -28.888 1.00 191.08 ? 366 LYS A CD 1 ATOM 2602 C CE . LYS A 1 339 ? -92.152 43.189 -30.339 1.00 181.96 ? 366 LYS A CE 1 ATOM 2603 N NZ . LYS A 1 339 ? -93.283 43.366 -31.295 1.00 180.30 ? 366 LYS A NZ 1 ATOM 2604 N N . PRO A 1 340 ? -97.003 42.335 -27.489 1.00 205.08 ? 367 PRO A N 1 ATOM 2605 C CA . PRO A 1 340 ? -98.085 42.819 -28.358 1.00 200.77 ? 367 PRO A CA 1 ATOM 2606 C C . PRO A 1 340 ? -97.610 43.129 -29.779 1.00 199.61 ? 367 PRO A C 1 ATOM 2607 O O . PRO A 1 340 ? -96.421 43.367 -29.993 1.00 201.31 ? 367 PRO A O 1 ATOM 2608 C CB . PRO A 1 340 ? -98.556 44.095 -27.653 1.00 200.35 ? 367 PRO A CB 1 ATOM 2609 C CG . PRO A 1 340 ? -98.220 43.874 -26.227 1.00 198.75 ? 367 PRO A CG 1 ATOM 2610 C CD . PRO A 1 340 ? -96.932 43.108 -26.234 1.00 198.80 ? 367 PRO A CD 1 ATOM 2611 N N . LYS A 1 341 ? -98.538 43.135 -30.731 1.00 195.80 ? 368 LYS A N 1 ATOM 2612 C CA . LYS A 1 341 ? -98.193 43.249 -32.147 1.00 189.27 ? 368 LYS A CA 1 ATOM 2613 C C . LYS A 1 341 ? -97.797 44.667 -32.558 1.00 188.73 ? 368 LYS A C 1 ATOM 2614 O O . LYS A 1 341 ? -96.847 44.853 -33.321 1.00 185.18 ? 368 LYS A O 1 ATOM 2615 C CB . LYS A 1 341 ? -99.360 42.763 -33.011 1.00 186.13 ? 368 LYS A CB 1 ATOM 2616 C CG . LYS A 1 341 ? -99.017 42.597 -34.483 1.00 182.72 ? 368 LYS A CG 1 ATOM 2617 C CD . LYS A 1 341 ? -100.106 41.835 -35.222 1.00 179.39 ? 368 LYS A CD 1 ATOM 2618 C CE . LYS A 1 341 ? -101.391 42.641 -35.313 1.00 177.87 ? 368 LYS A CE 1 ATOM 2619 N NZ . LYS A 1 341 ? -101.240 43.832 -36.194 1.00 177.23 ? 368 LYS A NZ 1 ATOM 2620 N N . ASN A 1 342 ? -98.526 45.664 -32.064 1.00 192.30 ? 369 ASN A N 1 ATOM 2621 C CA . ASN A 1 342 ? -98.202 47.057 -32.361 1.00 193.43 ? 369 ASN A CA 1 ATOM 2622 C C . ASN A 1 342 ? -97.180 47.620 -31.384 1.00 207.51 ? 369 ASN A C 1 ATOM 2623 O O . ASN A 1 342 ? -96.787 48.782 -31.484 1.00 207.76 ? 369 ASN A O 1 ATOM 2624 C CB . ASN A 1 342 ? -99.462 47.926 -32.348 1.00 183.17 ? 369 ASN A CB 1 ATOM 2625 C CG . ASN A 1 342 ? -100.235 47.856 -33.651 1.00 175.41 ? 369 ASN A CG 1 ATOM 2626 O OD1 . ASN A 1 342 ? -99.748 47.323 -34.649 1.00 174.41 ? 369 ASN A OD1 1 ATOM 2627 N ND2 . ASN A 1 342 ? -101.443 48.408 -33.652 1.00 170.06 ? 369 ASN A ND2 1 ATOM 2628 N N . SER A 1 343 ? -96.755 46.789 -30.438 1.00 220.92 ? 370 SER A N 1 ATOM 2629 C CA . SER A 1 343 ? -95.767 47.200 -29.450 1.00 222.65 ? 370 SER A CA 1 ATOM 2630 C C . SER A 1 343 ? -94.391 47.351 -30.083 1.00 221.00 ? 370 SER A C 1 ATOM 2631 O O . SER A 1 343 ? -94.008 46.576 -30.960 1.00 222.20 ? 370 SER A O 1 ATOM 2632 C CB . SER A 1 343 ? -95.702 46.196 -28.299 1.00 223.72 ? 370 SER A CB 1 ATOM 2633 O OG . SER A 1 343 ? -94.662 46.527 -27.395 1.00 226.99 ? 370 SER A OG 1 ATOM 2634 N N . GLU A 1 344 ? -93.653 48.361 -29.636 1.00 218.72 ? 371 GLU A N 1 ATOM 2635 C CA . GLU A 1 344 ? -92.306 48.600 -30.133 1.00 212.88 ? 371 GLU A CA 1 ATOM 2636 C C . GLU A 1 344 ? -91.324 48.651 -28.962 1.00 206.97 ? 371 GLU A C 1 ATOM 2637 O O . GLU A 1 344 ? -90.593 49.626 -28.783 1.00 210.59 ? 371 GLU A O 1 ATOM 2638 C CB . GLU A 1 344 ? -92.265 49.890 -30.955 1.00 211.28 ? 371 GLU A CB 1 ATOM 2639 C CG . GLU A 1 344 ? -93.477 50.047 -31.870 1.00 207.63 ? 371 GLU A CG 1 ATOM 2640 C CD . GLU A 1 344 ? -93.205 50.907 -33.085 1.00 205.69 ? 371 GLU A CD 1 ATOM 2641 O OE1 . GLU A 1 344 ? -92.306 51.771 -33.021 1.00 206.83 ? 371 GLU A OE1 1 ATOM 2642 O OE2 . GLU A 1 344 ? -93.893 50.711 -34.110 1.00 203.87 ? 371 GLU A OE2 1 ATOM 2643 N N . GLU A 1 345 ? -91.329 47.581 -28.170 1.00 195.17 ? 372 GLU A N 1 ATOM 2644 C CA . GLU A 1 345 ? -90.496 47.460 -26.976 1.00 180.39 ? 372 GLU A CA 1 ATOM 2645 C C . GLU A 1 345 ? -89.780 46.108 -26.972 1.00 170.81 ? 372 GLU A C 1 ATOM 2646 O O . GLU A 1 345 ? -90.165 45.209 -27.722 1.00 169.47 ? 372 GLU A O 1 ATOM 2647 C CB . GLU A 1 345 ? -91.349 47.619 -25.711 1.00 181.59 ? 372 GLU A CB 1 ATOM 2648 C CG . GLU A 1 345 ? -91.921 49.012 -25.507 1.00 186.08 ? 372 GLU A CG 1 ATOM 2649 C CD . GLU A 1 345 ? -92.588 49.175 -24.153 1.00 185.37 ? 372 GLU A CD 1 ATOM 2650 O OE1 . GLU A 1 345 ? -92.747 48.161 -23.442 1.00 181.49 ? 372 GLU A OE1 1 ATOM 2651 O OE2 . GLU A 1 345 ? -92.949 50.318 -23.798 1.00 187.40 ? 372 GLU A OE2 1 ATOM 2652 N N . PRO A 1 346 ? -88.727 45.960 -26.143 1.00 177.47 ? 373 PRO A N 1 ATOM 2653 C CA . PRO A 1 346 ? -88.045 44.664 -26.026 1.00 175.68 ? 373 PRO A CA 1 ATOM 2654 C C . PRO A 1 346 ? -88.994 43.527 -25.653 1.00 187.56 ? 373 PRO A C 1 ATOM 2655 O O . PRO A 1 346 ? -89.872 43.712 -24.809 1.00 185.10 ? 373 PRO A O 1 ATOM 2656 C CB . PRO A 1 346 ? -87.026 44.906 -24.911 1.00 162.37 ? 373 PRO A CB 1 ATOM 2657 C CG . PRO A 1 346 ? -86.728 46.354 -24.994 1.00 163.73 ? 373 PRO A CG 1 ATOM 2658 C CD . PRO A 1 346 ? -88.019 47.017 -25.396 1.00 174.53 ? 373 PRO A CD 1 ATOM 2659 N N . TYR A 1 347 ? -88.813 42.373 -26.289 1.00 201.19 ? 374 TYR A N 1 ATOM 2660 C CA . TYR A 1 347 ? -89.656 41.202 -26.056 1.00 212.36 ? 374 TYR A CA 1 ATOM 2661 C C . TYR A 1 347 ? -89.637 40.762 -24.591 1.00 224.67 ? 374 TYR A C 1 ATOM 2662 O O . TYR A 1 347 ? -88.576 40.732 -23.966 1.00 230.33 ? 374 TYR A O 1 ATOM 2663 C CB . TYR A 1 347 ? -89.204 40.033 -26.944 1.00 209.22 ? 374 TYR A CB 1 ATOM 2664 C CG . TYR A 1 347 ? -89.351 40.252 -28.439 1.00 207.21 ? 374 TYR A CG 1 ATOM 2665 C CD1 . TYR A 1 347 ? -90.491 39.832 -29.113 1.00 205.52 ? 374 TYR A CD1 1 ATOM 2666 C CD2 . TYR A 1 347 ? -88.340 40.856 -29.178 1.00 205.98 ? 374 TYR A CD2 1 ATOM 2667 C CE1 . TYR A 1 347 ? -90.627 40.020 -30.477 1.00 204.20 ? 374 TYR A CE1 1 ATOM 2668 C CE2 . TYR A 1 347 ? -88.469 41.048 -30.543 1.00 204.73 ? 374 TYR A CE2 1 ATOM 2669 C CZ . TYR A 1 347 ? -89.615 40.629 -31.186 1.00 203.52 ? 374 TYR A CZ 1 ATOM 2670 O OH . TYR A 1 347 ? -89.752 40.816 -32.543 1.00 202.90 ? 374 TYR A OH 1 ATOM 2671 N N . LYS A 1 348 ? -90.804 40.422 -24.045 1.00 230.15 ? 375 LYS A N 1 ATOM 2672 C CA . LYS A 1 348 ? -90.875 39.833 -22.706 1.00 232.32 ? 375 LYS A CA 1 ATOM 2673 C C . LYS A 1 348 ? -90.515 38.349 -22.783 1.00 231.37 ? 375 LYS A C 1 ATOM 2674 O O . LYS A 1 348 ? -91.056 37.629 -23.613 1.00 234.41 ? 375 LYS A O 1 ATOM 2675 C CB . LYS A 1 348 ? -92.270 40.008 -22.093 1.00 232.74 ? 375 LYS A CB 1 ATOM 2676 C CG . LYS A 1 348 ? -92.583 41.401 -21.559 1.00 233.84 ? 375 LYS A CG 1 ATOM 2677 C CD . LYS A 1 348 ? -93.869 41.376 -20.737 1.00 231.42 ? 375 LYS A CD 1 ATOM 2678 C CE . LYS A 1 348 ? -94.214 42.743 -20.166 1.00 230.50 ? 375 LYS A CE 1 ATOM 2679 N NZ . LYS A 1 348 ? -94.605 43.715 -21.224 1.00 230.10 ? 375 LYS A NZ 1 ATOM 2680 N N . GLU A 1 349 ? -89.611 37.882 -21.926 1.00 223.16 ? 376 GLU A N 1 ATOM 2681 C CA . GLU A 1 349 ? -89.145 36.499 -22.038 1.00 208.94 ? 376 GLU A CA 1 ATOM 2682 C C . GLU A 1 349 ? -89.623 35.576 -20.912 1.00 209.23 ? 376 GLU A C 1 ATOM 2683 O O . GLU A 1 349 ? -89.615 35.942 -19.735 1.00 214.51 ? 376 GLU A O 1 ATOM 2684 C CB . GLU A 1 349 ? -87.613 36.460 -22.111 1.00 193.85 ? 376 GLU A CB 1 ATOM 2685 C CG . GLU A 1 349 ? -87.035 36.996 -23.418 1.00 179.48 ? 376 GLU A CG 1 ATOM 2686 C CD . GLU A 1 349 ? -85.546 36.732 -23.558 1.00 160.80 ? 376 GLU A CD 1 ATOM 2687 O OE1 . GLU A 1 349 ? -84.998 35.956 -22.747 1.00 150.72 ? 376 GLU A OE1 1 ATOM 2688 O OE2 . GLU A 1 349 ? -84.923 37.301 -24.480 1.00 154.22 ? 376 GLU A OE2 1 ATOM 2689 N N . ILE A 1 350 ? -90.046 34.377 -21.305 1.00 206.04 ? 377 ILE A N 1 ATOM 2690 C CA . ILE A 1 350 ? -90.337 33.288 -20.379 1.00 208.24 ? 377 ILE A CA 1 ATOM 2691 C C . ILE A 1 350 ? -89.227 32.248 -20.499 1.00 208.81 ? 377 ILE A C 1 ATOM 2692 O O . ILE A 1 350 ? -88.943 31.762 -21.594 1.00 210.80 ? 377 ILE A O 1 ATOM 2693 C CB . ILE A 1 350 ? -91.698 32.624 -20.669 1.00 205.82 ? 377 ILE A CB 1 ATOM 2694 C CG1 . ILE A 1 350 ? -92.806 33.673 -20.766 1.00 204.03 ? 377 ILE A CG1 1 ATOM 2695 C CG2 . ILE A 1 350 ? -92.024 31.584 -19.605 1.00 207.16 ? 377 ILE A CG2 1 ATOM 2696 C CD1 . ILE A 1 350 ? -94.166 33.088 -21.080 1.00 202.41 ? 377 ILE A CD1 1 ATOM 2697 N N . ASP A 1 351 ? -88.603 31.902 -19.378 1.00 207.06 ? 378 ASP A N 1 ATOM 2698 C CA . ASP A 1 351 ? -87.409 31.064 -19.405 1.00 195.03 ? 378 ASP A CA 1 ATOM 2699 C C . ASP A 1 351 ? -87.663 29.643 -18.897 1.00 192.67 ? 378 ASP A C 1 ATOM 2700 O O . ASP A 1 351 ? -88.664 29.378 -18.231 1.00 193.23 ? 378 ASP A O 1 ATOM 2701 C CB . ASP A 1 351 ? -86.299 31.727 -18.579 1.00 191.54 ? 378 ASP A CB 1 ATOM 2702 C CG . ASP A 1 351 ? -84.959 31.035 -18.735 1.00 189.10 ? 378 ASP A CG 1 ATOM 2703 O OD1 . ASP A 1 351 ? -84.717 30.442 -19.808 1.00 185.23 ? 378 ASP A OD1 1 ATOM 2704 O OD2 . ASP A 1 351 ? -84.149 31.081 -17.783 1.00 190.71 ? 378 ASP A OD2 1 ATOM 2705 N N . GLY A 1 352 ? -86.758 28.730 -19.241 1.00 189.50 ? 379 GLY A N 1 ATOM 2706 C CA . GLY A 1 352 ? -86.717 27.410 -18.638 1.00 178.85 ? 379 GLY A CA 1 ATOM 2707 C C . GLY A 1 352 ? -87.767 26.416 -19.090 1.00 167.65 ? 379 GLY A C 1 ATOM 2708 O O . GLY A 1 352 ? -88.136 25.516 -18.337 1.00 171.95 ? 379 GLY A O 1 ATOM 2709 N N . ILE A 1 353 ? -88.249 26.567 -20.317 1.00 155.06 ? 380 ILE A N 1 ATOM 2710 C CA . ILE A 1 353 ? -89.210 25.622 -20.870 1.00 154.21 ? 380 ILE A CA 1 ATOM 2711 C C . ILE A 1 353 ? -88.471 24.419 -21.448 1.00 159.46 ? 380 ILE A C 1 ATOM 2712 O O . ILE A 1 353 ? -88.014 24.446 -22.591 1.00 162.07 ? 380 ILE A O 1 ATOM 2713 C CB . ILE A 1 353 ? -90.084 26.284 -21.941 1.00 148.60 ? 380 ILE A CB 1 ATOM 2714 C CG1 . ILE A 1 353 ? -90.809 27.483 -21.328 1.00 146.89 ? 380 ILE A CG1 1 ATOM 2715 C CG2 . ILE A 1 353 ? -91.074 25.284 -22.521 1.00 144.13 ? 380 ILE A CG2 1 ATOM 2716 C CD1 . ILE A 1 353 ? -91.251 28.508 -22.328 1.00 145.39 ? 380 ILE A CD1 1 ATOM 2717 N N . ALA A 1 354 ? -88.358 23.366 -20.642 1.00 160.10 ? 381 ALA A N 1 ATOM 2718 C CA . ALA A 1 354 ? -87.521 22.214 -20.971 1.00 161.15 ? 381 ALA A CA 1 ATOM 2719 C C . ALA A 1 354 ? -88.109 21.330 -22.071 1.00 170.85 ? 381 ALA A C 1 ATOM 2720 O O . ALA A 1 354 ? -87.443 20.413 -22.555 1.00 169.14 ? 381 ALA A O 1 ATOM 2721 C CB . ALA A 1 354 ? -87.266 21.385 -19.718 1.00 152.03 ? 381 ALA A CB 1 ATOM 2722 N N . THR A 1 355 ? -89.351 21.602 -22.461 1.00 176.70 ? 382 THR A N 1 ATOM 2723 C CA . THR A 1 355 ? -89.996 20.850 -23.533 1.00 175.40 ? 382 THR A CA 1 ATOM 2724 C C . THR A 1 355 ? -90.305 21.754 -24.721 1.00 178.73 ? 382 THR A C 1 ATOM 2725 O O . THR A 1 355 ? -90.138 22.971 -24.646 1.00 183.40 ? 382 THR A O 1 ATOM 2726 C CB . THR A 1 355 ? -91.298 20.178 -23.056 1.00 173.11 ? 382 THR A CB 1 ATOM 2727 O OG1 . THR A 1 355 ? -92.226 21.181 -22.623 1.00 174.78 ? 382 THR A OG1 1 ATOM 2728 C CG2 . THR A 1 355 ? -91.014 19.218 -21.909 1.00 171.93 ? 382 THR A CG2 1 ATOM 2729 N N . THR A 1 356 ? -90.760 21.153 -25.816 1.00 174.86 ? 383 THR A N 1 ATOM 2730 C CA . THR A 1 356 ? -91.095 21.911 -27.015 1.00 165.73 ? 383 THR A CA 1 ATOM 2731 C C . THR A 1 356 ? -92.572 22.305 -27.034 1.00 157.22 ? 383 THR A C 1 ATOM 2732 O O . THR A 1 356 ? -93.137 22.579 -28.093 1.00 156.11 ? 383 THR A O 1 ATOM 2733 C CB . THR A 1 356 ? -90.761 21.120 -28.297 1.00 164.19 ? 383 THR A CB 1 ATOM 2734 O OG1 . THR A 1 356 ? -91.432 19.854 -28.273 1.00 165.55 ? 383 THR A OG1 1 ATOM 2735 C CG2 . THR A 1 356 ? -89.257 20.894 -28.410 1.00 160.94 ? 383 THR A CG2 1 ATOM 2736 N N . ARG A 1 357 ? -93.192 22.330 -25.857 1.00 152.72 ? 384 ARG A N 1 ATOM 2737 C CA . ARG A 1 357 ? -94.571 22.788 -25.719 1.00 154.87 ? 384 ARG A CA 1 ATOM 2738 C C . ARG A 1 357 ? -94.743 23.619 -24.450 1.00 160.31 ? 384 ARG A C 1 ATOM 2739 O O . ARG A 1 357 ? -94.221 23.256 -23.396 1.00 161.48 ? 384 ARG A O 1 ATOM 2740 C CB . ARG A 1 357 ? -95.544 21.605 -25.711 1.00 157.71 ? 384 ARG A CB 1 ATOM 2741 C CG . ARG A 1 357 ? -96.972 21.996 -25.345 1.00 161.55 ? 384 ARG A CG 1 ATOM 2742 C CD . ARG A 1 357 ? -97.985 20.926 -25.725 1.00 163.84 ? 384 ARG A CD 1 ATOM 2743 N NE . ARG A 1 357 ? -99.337 21.293 -25.306 1.00 168.83 ? 384 ARG A NE 1 ATOM 2744 C CZ . ARG A 1 357 ? -100.426 21.143 -26.055 1.00 174.95 ? 384 ARG A CZ 1 ATOM 2745 N NH1 . ARG A 1 357 ? -100.336 20.632 -27.276 1.00 174.51 ? 384 ARG A NH1 1 ATOM 2746 N NH2 . ARG A 1 357 ? -101.610 21.509 -25.583 1.00 179.15 ? 384 ARG A NH2 1 ATOM 2747 N N . TYR A 1 358 ? -95.469 24.733 -24.550 1.00 166.07 ? 385 TYR A N 1 ATOM 2748 C CA . TYR A 1 358 ? -95.676 25.598 -23.386 1.00 172.21 ? 385 TYR A CA 1 ATOM 2749 C C . TYR A 1 358 ? -96.870 26.546 -23.526 1.00 174.44 ? 385 TYR A C 1 ATOM 2750 O O . TYR A 1 358 ? -97.049 27.188 -24.562 1.00 172.71 ? 385 TYR A O 1 ATOM 2751 C CB . TYR A 1 358 ? -94.412 26.416 -23.114 1.00 173.12 ? 385 TYR A CB 1 ATOM 2752 C CG . TYR A 1 358 ? -94.316 26.958 -21.706 1.00 171.55 ? 385 TYR A CG 1 ATOM 2753 C CD1 . TYR A 1 358 ? -94.602 28.290 -21.430 1.00 172.07 ? 385 TYR A CD1 1 ATOM 2754 C CD2 . TYR A 1 358 ? -93.938 26.137 -20.651 1.00 167.00 ? 385 TYR A CD2 1 ATOM 2755 C CE1 . TYR A 1 358 ? -94.508 28.788 -20.143 1.00 169.37 ? 385 TYR A CE1 1 ATOM 2756 C CE2 . TYR A 1 358 ? -93.842 26.626 -19.364 1.00 164.89 ? 385 TYR A CE2 1 ATOM 2757 C CZ . TYR A 1 358 ? -94.129 27.951 -19.116 1.00 164.23 ? 385 TYR A CZ 1 ATOM 2758 O OH . TYR A 1 358 ? -94.035 28.437 -17.833 1.00 164.06 ? 385 TYR A OH 1 ATOM 2759 N N . SER A 1 359 ? -97.672 26.645 -22.468 1.00 176.72 ? 386 SER A N 1 ATOM 2760 C CA . SER A 1 359 ? -98.843 27.519 -22.469 1.00 178.90 ? 386 SER A CA 1 ATOM 2761 C C . SER A 1 359 ? -98.558 28.874 -21.822 1.00 183.21 ? 386 SER A C 1 ATOM 2762 O O . SER A 1 359 ? -98.546 29.001 -20.595 1.00 180.41 ? 386 SER A O 1 ATOM 2763 C CB . SER A 1 359 ? -100.015 26.842 -21.753 1.00 179.20 ? 386 SER A CB 1 ATOM 2764 O OG . SER A 1 359 ? -100.392 25.644 -22.408 1.00 179.44 ? 386 SER A OG 1 ATOM 2765 N N . VAL A 1 360 ? -98.333 29.883 -22.657 1.00 190.78 ? 387 VAL A N 1 ATOM 2766 C CA . VAL A 1 360 ? -98.149 31.251 -22.188 1.00 196.03 ? 387 VAL A CA 1 ATOM 2767 C C . VAL A 1 360 ? -99.453 31.796 -21.616 1.00 209.06 ? 387 VAL A C 1 ATOM 2768 O O . VAL A 1 360 ? -100.411 32.037 -22.352 1.00 212.10 ? 387 VAL A O 1 ATOM 2769 C CB . VAL A 1 360 ? -97.663 32.177 -23.316 1.00 188.22 ? 387 VAL A CB 1 ATOM 2770 C CG1 . VAL A 1 360 ? -97.497 33.600 -22.804 1.00 186.55 ? 387 VAL A CG1 1 ATOM 2771 C CG2 . VAL A 1 360 ? -96.360 31.658 -23.899 1.00 184.30 ? 387 VAL A CG2 1 ATOM 2772 N N . ALA A 1 361 ? -99.483 31.993 -20.302 1.00 219.54 ? 388 ALA A N 1 ATOM 2773 C CA . ALA A 1 361 ? -100.700 32.416 -19.617 1.00 225.00 ? 388 ALA A CA 1 ATOM 2774 C C . ALA A 1 361 ? -100.593 33.840 -19.077 1.00 236.68 ? 388 ALA A C 1 ATOM 2775 O O . ALA A 1 361 ? -99.514 34.288 -18.692 1.00 233.40 ? 388 ALA A O 1 ATOM 2776 C CB . ALA A 1 361 ? -101.024 31.452 -18.487 1.00 223.19 ? 388 ALA A CB 1 ATOM 2777 N N . GLY A 1 362 ? -101.723 34.544 -19.052 1.00 252.03 ? 389 GLY A N 1 ATOM 2778 C CA . GLY A 1 362 ? -101.788 35.883 -18.493 1.00 263.28 ? 389 GLY A CA 1 ATOM 2779 C C . GLY A 1 362 ? -102.163 36.951 -19.504 1.00 274.47 ? 389 GLY A C 1 ATOM 2780 O O . GLY A 1 362 ? -102.156 38.142 -19.193 1.00 279.46 ? 389 GLY A O 1 ATOM 2781 N N . LEU A 1 363 ? -102.503 36.522 -20.715 1.00 280.04 ? 390 LEU A N 1 ATOM 2782 C CA . LEU A 1 363 ? -102.752 37.440 -21.823 1.00 277.26 ? 390 LEU A CA 1 ATOM 2783 C C . LEU A 1 363 ? -104.117 38.123 -21.739 1.00 277.30 ? 390 LEU A C 1 ATOM 2784 O O . LEU A 1 363 ? -105.069 37.567 -21.192 1.00 279.09 ? 390 LEU A O 1 ATOM 2785 C CB . LEU A 1 363 ? -102.628 36.691 -23.149 1.00 274.70 ? 390 LEU A CB 1 ATOM 2786 C CG . LEU A 1 363 ? -101.369 35.834 -23.292 1.00 273.39 ? 390 LEU A CG 1 ATOM 2787 C CD1 . LEU A 1 363 ? -101.460 34.948 -24.519 1.00 272.56 ? 390 LEU A CD1 1 ATOM 2788 C CD2 . LEU A 1 363 ? -100.124 36.705 -23.351 1.00 273.24 ? 390 LEU A CD2 1 ATOM 2789 N N . SER A 1 364 ? -104.203 39.333 -22.289 1.00 257.10 ? 391 SER A N 1 ATOM 2790 C CA . SER A 1 364 ? -105.458 40.079 -22.335 1.00 247.41 ? 391 SER A CA 1 ATOM 2791 C C . SER A 1 364 ? -106.439 39.453 -23.322 1.00 251.97 ? 391 SER A C 1 ATOM 2792 O O . SER A 1 364 ? -106.027 38.867 -24.325 1.00 258.23 ? 391 SER A O 1 ATOM 2793 C CB . SER A 1 364 ? -105.203 41.543 -22.708 1.00 239.38 ? 391 SER A CB 1 ATOM 2794 O OG . SER A 1 364 ? -104.945 42.329 -21.558 1.00 240.24 ? 391 SER A OG 1 ATOM 2795 N N . PRO A 1 365 ? -107.745 39.571 -23.035 1.00 247.96 ? 392 PRO A N 1 ATOM 2796 C CA . PRO A 1 365 ? -108.779 39.048 -23.934 1.00 253.07 ? 392 PRO A CA 1 ATOM 2797 C C . PRO A 1 365 ? -108.843 39.835 -25.237 1.00 257.66 ? 392 PRO A C 1 ATOM 2798 O O . PRO A 1 365 ? -108.664 41.054 -25.211 1.00 256.71 ? 392 PRO A O 1 ATOM 2799 C CB . PRO A 1 365 ? -110.075 39.226 -23.130 1.00 255.16 ? 392 PRO A CB 1 ATOM 2800 C CG . PRO A 1 365 ? -109.640 39.440 -21.712 1.00 255.44 ? 392 PRO A CG 1 ATOM 2801 C CD . PRO A 1 365 ? -108.324 40.138 -21.805 1.00 251.03 ? 392 PRO A CD 1 ATOM 2802 N N . TYR A 1 366 ? -109.083 39.143 -26.349 1.00 258.89 ? 393 TYR A N 1 ATOM 2803 C CA . TYR A 1 366 ? -109.276 39.791 -27.645 1.00 258.53 ? 393 TYR A CA 1 ATOM 2804 C C . TYR A 1 366 ? -108.046 40.609 -28.039 1.00 256.40 ? 393 TYR A C 1 ATOM 2805 O O . TYR A 1 366 ? -108.159 41.654 -28.681 1.00 258.24 ? 393 TYR A O 1 ATOM 2806 C CB . TYR A 1 366 ? -110.531 40.672 -27.603 1.00 265.11 ? 393 TYR A CB 1 ATOM 2807 C CG . TYR A 1 366 ? -111.092 41.075 -28.948 1.00 266.03 ? 393 TYR A CG 1 ATOM 2808 C CD1 . TYR A 1 366 ? -111.393 40.122 -29.912 1.00 264.50 ? 393 TYR A CD1 1 ATOM 2809 C CD2 . TYR A 1 366 ? -111.353 42.407 -29.240 1.00 267.25 ? 393 TYR A CD2 1 ATOM 2810 C CE1 . TYR A 1 366 ? -111.917 40.489 -31.138 1.00 264.98 ? 393 TYR A CE1 1 ATOM 2811 C CE2 . TYR A 1 366 ? -111.878 42.783 -30.460 1.00 267.64 ? 393 TYR A CE2 1 ATOM 2812 C CZ . TYR A 1 366 ? -112.158 41.821 -31.406 1.00 266.08 ? 393 TYR A CZ 1 ATOM 2813 O OH . TYR A 1 366 ? -112.681 42.193 -32.622 1.00 264.67 ? 393 TYR A OH 1 ATOM 2814 N N . SER A 1 367 ? -106.870 40.124 -27.651 1.00 239.43 ? 394 SER A N 1 ATOM 2815 C CA . SER A 1 367 ? -105.624 40.840 -27.904 1.00 228.14 ? 394 SER A CA 1 ATOM 2816 C C . SER A 1 367 ? -104.665 40.029 -28.770 1.00 222.78 ? 394 SER A C 1 ATOM 2817 O O . SER A 1 367 ? -104.403 38.858 -28.494 1.00 228.58 ? 394 SER A O 1 ATOM 2818 C CB . SER A 1 367 ? -104.943 41.208 -26.583 1.00 221.79 ? 394 SER A CB 1 ATOM 2819 O OG . SER A 1 367 ? -105.731 42.120 -25.839 1.00 220.65 ? 394 SER A OG 1 ATOM 2820 N N . ASP A 1 368 ? -104.145 40.661 -29.818 1.00 211.22 ? 395 ASP A N 1 ATOM 2821 C CA . ASP A 1 368 ? -103.170 40.020 -30.693 1.00 206.92 ? 395 ASP A CA 1 ATOM 2822 C C . ASP A 1 368 ? -101.806 39.933 -30.024 1.00 212.18 ? 395 ASP A C 1 ATOM 2823 O O . ASP A 1 368 ? -101.488 40.727 -29.140 1.00 216.06 ? 395 ASP A O 1 ATOM 2824 C CB . ASP A 1 368 ? -103.046 40.779 -32.014 1.00 203.73 ? 395 ASP A CB 1 ATOM 2825 C CG . ASP A 1 368 ? -104.306 40.713 -32.845 1.00 202.56 ? 395 ASP A CG 1 ATOM 2826 O OD1 . ASP A 1 368 ? -105.108 39.781 -32.634 1.00 201.75 ? 395 ASP A OD1 1 ATOM 2827 O OD2 . ASP A 1 368 ? -104.492 41.591 -33.713 1.00 202.01 ? 395 ASP A OD2 1 ATOM 2828 N N . TYR A 1 369 ? -101.003 38.966 -30.453 1.00 212.48 ? 396 TYR A N 1 ATOM 2829 C CA . TYR A 1 369 ? -99.647 38.808 -29.947 1.00 213.09 ? 396 TYR A CA 1 ATOM 2830 C C . TYR A 1 369 ? -98.706 38.220 -31.002 1.00 218.26 ? 396 TYR A C 1 ATOM 2831 O O . TYR A 1 369 ? -99.146 37.541 -31.950 1.00 220.50 ? 396 TYR A O 1 ATOM 2832 C CB . TYR A 1 369 ? -99.635 37.919 -28.698 1.00 206.75 ? 396 TYR A CB 1 ATOM 2833 C CG . TYR A 1 369 ? -100.366 38.486 -27.497 1.00 203.25 ? 396 TYR A CG 1 ATOM 2834 C CD1 . TYR A 1 369 ? -101.668 38.100 -27.209 1.00 203.30 ? 396 TYR A CD1 1 ATOM 2835 C CD2 . TYR A 1 369 ? -99.750 39.395 -26.647 1.00 201.09 ? 396 TYR A CD2 1 ATOM 2836 C CE1 . TYR A 1 369 ? -102.339 38.607 -26.113 1.00 203.56 ? 396 TYR A CE1 1 ATOM 2837 C CE2 . TYR A 1 369 ? -100.414 39.908 -25.546 1.00 201.53 ? 396 TYR A CE2 1 ATOM 2838 C CZ . TYR A 1 369 ? -101.708 39.510 -25.285 1.00 202.68 ? 396 TYR A CZ 1 ATOM 2839 O OH . TYR A 1 369 ? -102.378 40.013 -24.193 1.00 204.61 ? 396 TYR A OH 1 ATOM 2840 N N . GLU A 1 370 ? -97.410 38.483 -30.818 1.00 219.36 ? 397 GLU A N 1 ATOM 2841 C CA . GLU A 1 370 ? -96.362 37.934 -31.688 1.00 219.71 ? 397 GLU A CA 1 ATOM 2842 C C . GLU A 1 370 ? -95.354 37.104 -30.882 1.00 222.62 ? 397 GLU A C 1 ATOM 2843 O O . GLU A 1 370 ? -94.760 37.611 -29.934 1.00 226.64 ? 397 GLU A O 1 ATOM 2844 C CB . GLU A 1 370 ? -95.643 39.067 -32.430 1.00 216.64 ? 397 GLU A CB 1 ATOM 2845 C CG . GLU A 1 370 ? -94.427 38.628 -33.228 1.00 212.29 ? 397 GLU A CG 1 ATOM 2846 C CD . GLU A 1 370 ? -93.736 39.784 -33.928 1.00 211.23 ? 397 GLU A CD 1 ATOM 2847 O OE1 . GLU A 1 370 ? -92.491 39.761 -34.020 1.00 208.70 ? 397 GLU A OE1 1 ATOM 2848 O OE2 . GLU A 1 370 ? -94.434 40.711 -34.390 1.00 213.48 ? 397 GLU A OE2 1 ATOM 2849 N N . PHE A 1 371 ? -95.151 35.839 -31.258 1.00 219.42 ? 398 PHE A N 1 ATOM 2850 C CA . PHE A 1 371 ? -94.318 34.925 -30.458 1.00 217.25 ? 398 PHE A CA 1 ATOM 2851 C C . PHE A 1 371 ? -93.035 34.439 -31.155 1.00 218.86 ? 398 PHE A C 1 ATOM 2852 O O . PHE A 1 371 ? -93.009 34.279 -32.373 1.00 215.78 ? 398 PHE A O 1 ATOM 2853 C CB . PHE A 1 371 ? -95.142 33.701 -30.033 1.00 215.58 ? 398 PHE A CB 1 ATOM 2854 C CG . PHE A 1 371 ? -96.280 34.019 -29.099 1.00 215.16 ? 398 PHE A CG 1 ATOM 2855 C CD1 . PHE A 1 371 ? -96.046 34.264 -27.756 1.00 214.62 ? 398 PHE A CD1 1 ATOM 2856 C CD2 . PHE A 1 371 ? -97.585 34.053 -29.561 1.00 216.20 ? 398 PHE A CD2 1 ATOM 2857 C CE1 . PHE A 1 371 ? -97.091 34.549 -26.892 1.00 215.70 ? 398 PHE A CE1 1 ATOM 2858 C CE2 . PHE A 1 371 ? -98.633 34.338 -28.702 1.00 218.12 ? 398 PHE A CE2 1 ATOM 2859 C CZ . PHE A 1 371 ? -98.384 34.587 -27.366 1.00 217.67 ? 398 PHE A CZ 1 ATOM 2860 N N . ARG A 1 372 ? -91.984 34.191 -30.367 1.00 226.05 ? 399 ARG A N 1 ATOM 2861 C CA . ARG A 1 372 ? -90.709 33.660 -30.880 1.00 228.85 ? 399 ARG A CA 1 ATOM 2862 C C . ARG A 1 372 ? -90.107 32.569 -29.980 1.00 233.84 ? 399 ARG A C 1 ATOM 2863 O O . ARG A 1 372 ? -90.417 32.493 -28.791 1.00 234.77 ? 399 ARG A O 1 ATOM 2864 C CB . ARG A 1 372 ? -89.687 34.788 -31.052 1.00 227.01 ? 399 ARG A CB 1 ATOM 2865 C CG . ARG A 1 372 ? -90.010 35.771 -32.166 1.00 228.51 ? 399 ARG A CG 1 ATOM 2866 C CD . ARG A 1 372 ? -88.934 36.840 -32.286 1.00 228.99 ? 399 ARG A CD 1 ATOM 2867 N NE . ARG A 1 372 ? -89.277 37.845 -33.287 1.00 230.74 ? 399 ARG A NE 1 ATOM 2868 C CZ . ARG A 1 372 ? -88.968 37.751 -34.576 1.00 230.73 ? 399 ARG A CZ 1 ATOM 2869 N NH1 . ARG A 1 372 ? -88.303 36.695 -35.024 1.00 231.69 ? 399 ARG A NH1 1 ATOM 2870 N NH2 . ARG A 1 372 ? -89.322 38.713 -35.418 1.00 229.18 ? 399 ARG A NH2 1 ATOM 2871 N N . VAL A 1 373 ? -89.236 31.735 -30.550 1.00 238.53 ? 400 VAL A N 1 ATOM 2872 C CA . VAL A 1 373 ? -88.613 30.636 -29.805 1.00 232.29 ? 400 VAL A CA 1 ATOM 2873 C C . VAL A 1 373 ? -87.081 30.678 -29.846 1.00 225.44 ? 400 VAL A C 1 ATOM 2874 O O . VAL A 1 373 ? -86.476 30.630 -30.917 1.00 223.59 ? 400 VAL A O 1 ATOM 2875 C CB . VAL A 1 373 ? -89.071 29.262 -30.336 1.00 233.19 ? 400 VAL A CB 1 ATOM 2876 C CG1 . VAL A 1 373 ? -88.484 28.145 -29.485 1.00 232.76 ? 400 VAL A CG1 1 ATOM 2877 C CG2 . VAL A 1 373 ? -90.590 29.176 -30.360 1.00 237.79 ? 400 VAL A CG2 1 ATOM 2878 N N . VAL A 1 374 ? -86.466 30.740 -28.668 1.00 212.24 ? 401 VAL A N 1 ATOM 2879 C CA . VAL A 1 374 ? -85.013 30.835 -28.536 1.00 184.93 ? 401 VAL A CA 1 ATOM 2880 C C . VAL A 1 374 ? -84.416 29.578 -27.901 1.00 184.25 ? 401 VAL A C 1 ATOM 2881 O O . VAL A 1 374 ? -84.800 29.196 -26.805 1.00 188.46 ? 401 VAL A O 1 ATOM 2882 C CB . VAL A 1 374 ? -84.616 32.053 -27.684 1.00 156.82 ? 401 VAL A CB 1 ATOM 2883 C CG1 . VAL A 1 374 ? -83.130 32.030 -27.396 1.00 150.65 ? 401 VAL A CG1 1 ATOM 2884 C CG2 . VAL A 1 374 ? -85.018 33.347 -28.375 1.00 147.89 ? 401 VAL A CG2 1 ATOM 2885 N N . ALA A 1 375 ? -83.464 28.945 -28.576 1.00 172.02 ? 402 ALA A N 1 ATOM 2886 C CA . ALA A 1 375 ? -82.906 27.686 -28.085 1.00 171.18 ? 402 ALA A CA 1 ATOM 2887 C C . ALA A 1 375 ? -81.637 27.883 -27.253 1.00 170.69 ? 402 ALA A C 1 ATOM 2888 O O . ALA A 1 375 ? -80.842 28.782 -27.521 1.00 170.97 ? 402 ALA A O 1 ATOM 2889 C CB . ALA A 1 375 ? -82.625 26.755 -29.248 1.00 170.02 ? 402 ALA A CB 1 ATOM 2890 N N . VAL A 1 376 ? -81.453 27.039 -26.239 1.00 152.37 ? 403 VAL A N 1 ATOM 2891 C CA . VAL A 1 376 ? -80.249 27.088 -25.409 1.00 139.08 ? 403 VAL A CA 1 ATOM 2892 C C . VAL A 1 376 ? -79.710 25.693 -25.067 1.00 129.99 ? 403 VAL A C 1 ATOM 2893 O O . VAL A 1 376 ? -80.460 24.811 -24.647 1.00 134.61 ? 403 VAL A O 1 ATOM 2894 C CB . VAL A 1 376 ? -80.499 27.851 -24.081 1.00 104.45 ? 403 VAL A CB 1 ATOM 2895 C CG1 . VAL A 1 376 ? -79.236 27.877 -23.240 1.00 97.84 ? 403 VAL A CG1 1 ATOM 2896 C CG2 . VAL A 1 376 ? -80.975 29.271 -24.346 1.00 109.11 ? 403 VAL A CG2 1 ATOM 2897 N N . ASN A 1 377 ? -78.407 25.497 -25.257 1.00 125.08 ? 404 ASN A N 1 ATOM 2898 C CA . ASN A 1 377 ? -77.725 24.323 -24.715 1.00 139.14 ? 404 ASN A CA 1 ATOM 2899 C C . ASN A 1 377 ? -76.617 24.733 -23.740 1.00 152.25 ? 404 ASN A C 1 ATOM 2900 O O . ASN A 1 377 ? -76.735 25.742 -23.044 1.00 155.94 ? 404 ASN A O 1 ATOM 2901 C CB . ASN A 1 377 ? -77.164 23.434 -25.838 1.00 145.22 ? 404 ASN A CB 1 ATOM 2902 C CG . ASN A 1 377 ? -76.154 24.149 -26.731 1.00 150.20 ? 404 ASN A CG 1 ATOM 2903 O OD1 . ASN A 1 377 ? -75.353 24.963 -26.273 1.00 151.27 ? 404 ASN A OD1 1 ATOM 2904 N ND2 . ASN A 1 377 ? -76.182 23.825 -28.019 1.00 150.54 ? 404 ASN A ND2 1 ATOM 2905 N N . ASN A 1 378 ? -75.543 23.951 -23.696 1.00 158.30 ? 405 ASN A N 1 ATOM 2906 C CA . ASN A 1 378 ? -74.426 24.237 -22.802 1.00 160.39 ? 405 ASN A CA 1 ATOM 2907 C C . ASN A 1 378 ? -73.546 25.373 -23.318 1.00 158.93 ? 405 ASN A C 1 ATOM 2908 O O . ASN A 1 378 ? -72.974 26.130 -22.536 1.00 158.53 ? 405 ASN A O 1 ATOM 2909 C CB . ASN A 1 378 ? -73.574 22.980 -22.593 1.00 167.20 ? 405 ASN A CB 1 ATOM 2910 C CG . ASN A 1 378 ? -74.347 21.849 -21.939 1.00 174.35 ? 405 ASN A CG 1 ATOM 2911 O OD1 . ASN A 1 378 ? -75.563 21.929 -21.769 1.00 179.65 ? 405 ASN A OD1 1 ATOM 2912 N ND2 . ASN A 1 378 ? -73.642 20.782 -21.575 1.00 174.38 ? 405 ASN A ND2 1 ATOM 2913 N N . ILE A 1 379 ? -73.449 25.489 -24.639 1.00 155.70 ? 406 ILE A N 1 ATOM 2914 C CA . ILE A 1 379 ? -72.529 26.431 -25.272 1.00 157.26 ? 406 ILE A CA 1 ATOM 2915 C C . ILE A 1 379 ? -72.997 27.872 -25.231 1.00 155.87 ? 406 ILE A C 1 ATOM 2916 O O . ILE A 1 379 ? -72.250 28.772 -24.847 1.00 154.97 ? 406 ILE A O 1 ATOM 2917 C CB . ILE A 1 379 ? -72.294 26.065 -26.738 1.00 164.35 ? 406 ILE A CB 1 ATOM 2918 C CG1 . ILE A 1 379 ? -71.854 24.615 -26.833 1.00 164.85 ? 406 ILE A CG1 1 ATOM 2919 C CG2 . ILE A 1 379 ? -71.237 26.968 -27.346 1.00 167.53 ? 406 ILE A CG2 1 ATOM 2920 C CD1 . ILE A 1 379 ? -70.613 24.339 -26.043 1.00 164.87 ? 406 ILE A CD1 1 ATOM 2921 N N . GLY A 1 380 ? -74.233 28.091 -25.656 1.00 163.57 ? 407 GLY A N 1 ATOM 2922 C CA . GLY A 1 380 ? -74.757 29.434 -25.735 1.00 165.94 ? 407 GLY A CA 1 ATOM 2923 C C . GLY A 1 380 ? -76.195 29.473 -26.190 1.00 165.15 ? 407 GLY A C 1 ATOM 2924 O O . GLY A 1 380 ? -76.820 28.444 -26.440 1.00 165.73 ? 407 GLY A O 1 ATOM 2925 N N . ARG A 1 381 ? -76.709 30.690 -26.299 1.00 161.57 ? 408 ARG A N 1 ATOM 2926 C CA . ARG A 1 381 ? -78.096 30.942 -26.649 1.00 165.48 ? 408 ARG A CA 1 ATOM 2927 C C . ARG A 1 381 ? -78.258 31.079 -28.160 1.00 166.66 ? 408 ARG A C 1 ATOM 2928 O O . ARG A 1 381 ? -77.759 32.029 -28.762 1.00 166.80 ? 408 ARG A O 1 ATOM 2929 C CB . ARG A 1 381 ? -78.569 32.201 -25.917 1.00 165.58 ? 408 ARG A CB 1 ATOM 2930 C CG . ARG A 1 381 ? -79.845 32.841 -26.410 1.00 168.94 ? 408 ARG A CG 1 ATOM 2931 C CD . ARG A 1 381 ? -80.158 34.052 -25.538 1.00 171.22 ? 408 ARG A CD 1 ATOM 2932 N NE . ARG A 1 381 ? -81.050 35.014 -26.177 1.00 175.96 ? 408 ARG A NE 1 ATOM 2933 C CZ . ARG A 1 381 ? -82.250 35.344 -25.708 1.00 176.32 ? 408 ARG A CZ 1 ATOM 2934 N NH1 . ARG A 1 381 ? -82.707 34.788 -24.594 1.00 176.70 ? 408 ARG A NH1 1 ATOM 2935 N NH2 . ARG A 1 381 ? -82.994 36.233 -26.351 1.00 175.06 ? 408 ARG A NH2 1 ATOM 2936 N N . GLY A 1 382 ? -78.940 30.115 -28.773 1.00 163.40 ? 409 GLY A N 1 ATOM 2937 C CA . GLY A 1 382 ? -79.165 30.141 -30.207 1.00 165.99 ? 409 GLY A CA 1 ATOM 2938 C C . GLY A 1 382 ? -80.066 31.291 -30.613 1.00 175.50 ? 409 GLY A C 1 ATOM 2939 O O . GLY A 1 382 ? -80.744 31.872 -29.766 1.00 170.06 ? 409 GLY A O 1 ATOM 2940 N N . PRO A 1 383 ? -80.071 31.640 -31.910 1.00 196.36 ? 410 PRO A N 1 ATOM 2941 C CA . PRO A 1 383 ? -80.942 32.716 -32.394 1.00 220.42 ? 410 PRO A CA 1 ATOM 2942 C C . PRO A 1 383 ? -82.419 32.343 -32.285 1.00 263.42 ? 410 PRO A C 1 ATOM 2943 O O . PRO A 1 383 ? -82.751 31.158 -32.238 1.00 261.14 ? 410 PRO A O 1 ATOM 2944 C CB . PRO A 1 383 ? -80.522 32.881 -33.861 1.00 200.38 ? 410 PRO A CB 1 ATOM 2945 C CG . PRO A 1 383 ? -79.160 32.274 -33.944 1.00 193.03 ? 410 PRO A CG 1 ATOM 2946 C CD . PRO A 1 383 ? -79.178 31.140 -32.967 1.00 194.19 ? 410 PRO A CD 1 ATOM 2947 N N . ALA A 1 384 ? -83.289 33.348 -32.244 1.00 300.74 ? 411 ALA A N 1 ATOM 2948 C CA . ALA A 1 384 ? -84.723 33.120 -32.098 1.00 303.99 ? 411 ALA A CA 1 ATOM 2949 C C . ALA A 1 384 ? -85.320 32.452 -33.331 1.00 307.54 ? 411 ALA A C 1 ATOM 2950 O O . ALA A 1 384 ? -84.612 32.140 -34.291 1.00 316.77 ? 411 ALA A O 1 ATOM 2951 C CB . ALA A 1 384 ? -85.441 34.434 -31.814 1.00 306.20 ? 411 ALA A CB 1 ATOM 2952 N N . SER A 1 385 ? -86.629 32.232 -33.298 1.00 274.76 ? 412 SER A N 1 ATOM 2953 C CA . SER A 1 385 ? -87.329 31.635 -34.426 1.00 251.78 ? 412 SER A CA 1 ATOM 2954 C C . SER A 1 385 ? -88.122 32.692 -35.183 1.00 244.83 ? 412 SER A C 1 ATOM 2955 O O . SER A 1 385 ? -88.395 33.771 -34.655 1.00 250.93 ? 412 SER A O 1 ATOM 2956 C CB . SER A 1 385 ? -88.265 30.520 -33.958 1.00 244.78 ? 412 SER A CB 1 ATOM 2957 O OG . SER A 1 385 ? -89.569 31.022 -33.717 1.00 244.47 ? 412 SER A OG 1 ATOM 2958 N N . GLU A 1 386 ? -88.480 32.378 -36.425 1.00 233.75 ? 413 GLU A N 1 ATOM 2959 C CA . GLU A 1 386 ? -89.377 33.223 -37.202 1.00 226.96 ? 413 GLU A CA 1 ATOM 2960 C C . GLU A 1 386 ? -90.700 33.318 -36.446 1.00 235.93 ? 413 GLU A C 1 ATOM 2961 O O . GLU A 1 386 ? -91.253 32.298 -36.034 1.00 238.22 ? 413 GLU A O 1 ATOM 2962 C CB . GLU A 1 386 ? -89.580 32.655 -38.609 1.00 212.50 ? 413 GLU A CB 1 ATOM 2963 C CG . GLU A 1 386 ? -90.187 33.630 -39.610 1.00 199.22 ? 413 GLU A CG 1 ATOM 2964 C CD . GLU A 1 386 ? -89.220 34.724 -40.026 1.00 184.88 ? 413 GLU A CD 1 ATOM 2965 O OE1 . GLU A 1 386 ? -89.687 35.810 -40.426 1.00 181.58 ? 413 GLU A OE1 1 ATOM 2966 O OE2 . GLU A 1 386 ? -87.994 34.494 -39.960 1.00 177.10 ? 413 GLU A OE2 1 ATOM 2967 N N . PRO A 1 387 ? -91.205 34.545 -36.249 1.00 243.29 ? 414 PRO A N 1 ATOM 2968 C CA . PRO A 1 387 ? -92.313 34.764 -35.313 1.00 249.21 ? 414 PRO A CA 1 ATOM 2969 C C . PRO A 1 387 ? -93.656 34.212 -35.783 1.00 256.38 ? 414 PRO A C 1 ATOM 2970 O O . PRO A 1 387 ? -93.890 34.088 -36.984 1.00 264.91 ? 414 PRO A O 1 ATOM 2971 C CB . PRO A 1 387 ? -92.374 36.289 -35.205 1.00 249.82 ? 414 PRO A CB 1 ATOM 2972 C CG . PRO A 1 387 ? -91.877 36.768 -36.519 1.00 249.82 ? 414 PRO A CG 1 ATOM 2973 C CD . PRO A 1 387 ? -90.798 35.794 -36.919 1.00 246.39 ? 414 PRO A CD 1 ATOM 2974 N N . VAL A 1 388 ? -94.528 33.880 -34.835 1.00 253.96 ? 415 VAL A N 1 ATOM 2975 C CA . VAL A 1 388 ? -95.891 33.503 -35.184 1.00 231.35 ? 415 VAL A CA 1 ATOM 2976 C C . VAL A 1 388 ? -96.864 34.570 -34.677 1.00 221.61 ? 415 VAL A C 1 ATOM 2977 O O . VAL A 1 388 ? -96.771 35.035 -33.538 1.00 223.61 ? 415 VAL A O 1 ATOM 2978 C CB . VAL A 1 388 ? -96.270 32.099 -34.632 1.00 177.90 ? 415 VAL A CB 1 ATOM 2979 C CG1 . VAL A 1 388 ? -96.222 32.058 -33.108 1.00 176.13 ? 415 VAL A CG1 1 ATOM 2980 C CG2 . VAL A 1 388 ? -97.638 31.669 -35.151 1.00 178.08 ? 415 VAL A CG2 1 ATOM 2981 N N . LEU A 1 389 ? -97.772 34.984 -35.554 1.00 211.63 ? 416 LEU A N 1 ATOM 2982 C CA . LEU A 1 389 ? -98.779 35.987 -35.225 1.00 192.68 ? 416 LEU A CA 1 ATOM 2983 C C . LEU A 1 389 ? -100.081 35.308 -34.848 1.00 192.47 ? 416 LEU A C 1 ATOM 2984 O O . LEU A 1 389 ? -100.532 34.416 -35.565 1.00 191.15 ? 416 LEU A O 1 ATOM 2985 C CB . LEU A 1 389 ? -99.024 36.927 -36.409 1.00 171.67 ? 416 LEU A CB 1 ATOM 2986 C CG . LEU A 1 389 ? -98.000 38.006 -36.746 1.00 154.77 ? 416 LEU A CG 1 ATOM 2987 C CD1 . LEU A 1 389 ? -98.487 38.839 -37.924 1.00 150.96 ? 416 LEU A CD1 1 ATOM 2988 C CD2 . LEU A 1 389 ? -97.755 38.885 -35.537 1.00 150.30 ? 416 LEU A CD2 1 ATOM 2989 N N . THR A 1 390 ? -100.700 35.715 -33.744 1.00 194.11 ? 417 THR A N 1 ATOM 2990 C CA . THR A 1 390 ? -102.025 35.169 -33.450 1.00 204.68 ? 417 THR A CA 1 ATOM 2991 C C . THR A 1 390 ? -102.846 36.013 -32.486 1.00 205.12 ? 417 THR A C 1 ATOM 2992 O O . THR A 1 390 ? -102.436 37.098 -32.089 1.00 206.63 ? 417 THR A O 1 ATOM 2993 C CB . THR A 1 390 ? -101.933 33.739 -32.881 1.00 214.64 ? 417 THR A CB 1 ATOM 2994 O OG1 . THR A 1 390 ? -103.247 33.174 -32.799 1.00 225.44 ? 417 THR A OG1 1 ATOM 2995 C CG2 . THR A 1 390 ? -101.287 33.741 -31.505 1.00 217.50 ? 417 THR A CG2 1 ATOM 2996 N N . GLN A 1 391 ? -104.018 35.501 -32.127 1.00 203.80 ? 418 GLN A N 1 ATOM 2997 C CA . GLN A 1 391 ? -104.945 36.213 -31.259 1.00 198.56 ? 418 GLN A CA 1 ATOM 2998 C C . GLN A 1 391 ? -105.502 35.288 -30.181 1.00 199.94 ? 418 GLN A C 1 ATOM 2999 O O . GLN A 1 391 ? -105.893 34.155 -30.464 1.00 200.38 ? 418 GLN A O 1 ATOM 3000 C CB . GLN A 1 391 ? -106.084 36.817 -32.083 1.00 188.08 ? 418 GLN A CB 1 ATOM 3001 C CG . GLN A 1 391 ? -107.086 37.615 -31.271 1.00 180.73 ? 418 GLN A CG 1 ATOM 3002 C CD . GLN A 1 391 ? -108.099 38.327 -32.144 1.00 177.92 ? 418 GLN A CD 1 ATOM 3003 O OE1 . GLN A 1 391 ? -109.278 37.975 -32.160 1.00 178.86 ? 418 GLN A OE1 1 ATOM 3004 N NE2 . GLN A 1 391 ? -107.643 39.338 -32.875 1.00 177.06 ? 418 GLN A NE2 1 ATOM 3005 N N . CYS B 2 29 ? -31.160 -7.080 29.049 1.00 127.00 ? 29 CYS B N 1 ATOM 3006 C CA . CYS B 2 29 ? -31.307 -7.973 27.903 1.00 128.24 ? 29 CYS B CA 1 ATOM 3007 C C . CYS B 2 29 ? -32.671 -8.683 27.865 1.00 132.44 ? 29 CYS B C 1 ATOM 3008 O O . CYS B 2 29 ? -33.540 -8.298 27.100 1.00 130.58 ? 29 CYS B O 1 ATOM 3009 C CB . CYS B 2 29 ? -30.186 -9.015 27.907 1.00 129.53 ? 29 CYS B CB 1 ATOM 3010 S SG . CYS B 2 29 ? -30.531 -10.548 27.001 1.00 103.46 ? 29 CYS B SG 1 ATOM 3011 N N . LYS B 2 30 ? -32.839 -9.691 28.719 1.00 138.62 ? 30 LYS B N 1 ATOM 3012 C CA . LYS B 2 30 ? -33.879 -10.701 28.494 1.00 142.26 ? 30 LYS B CA 1 ATOM 3013 C C . LYS B 2 30 ? -35.337 -10.256 28.581 1.00 142.24 ? 30 LYS B C 1 ATOM 3014 O O . LYS B 2 30 ? -36.193 -10.858 27.930 1.00 148.63 ? 30 LYS B O 1 ATOM 3015 C CB . LYS B 2 30 ? -33.679 -11.864 29.478 1.00 148.30 ? 30 LYS B CB 1 ATOM 3016 C CG . LYS B 2 30 ? -33.379 -13.203 28.809 1.00 147.37 ? 30 LYS B CG 1 ATOM 3017 C CD . LYS B 2 30 ? -34.447 -13.601 27.801 1.00 141.34 ? 30 LYS B CD 1 ATOM 3018 C CE . LYS B 2 30 ? -33.914 -13.518 26.381 1.00 129.13 ? 30 LYS B CE 1 ATOM 3019 N NZ . LYS B 2 30 ? -32.722 -14.385 26.192 1.00 128.81 ? 30 LYS B NZ 1 ATOM 3020 N N . ILE B 2 31 ? -35.639 -9.218 29.361 1.00 133.06 ? 31 ILE B N 1 ATOM 3021 C CA . ILE B 2 31 ? -37.040 -8.942 29.715 1.00 122.71 ? 31 ILE B CA 1 ATOM 3022 C C . ILE B 2 31 ? -37.897 -8.375 28.576 1.00 121.93 ? 31 ILE B C 1 ATOM 3023 O O . ILE B 2 31 ? -38.989 -8.886 28.303 1.00 117.26 ? 31 ILE B O 1 ATOM 3024 C CB . ILE B 2 31 ? -37.124 -7.996 30.935 1.00 119.99 ? 31 ILE B CB 1 ATOM 3025 C CG1 . ILE B 2 31 ? -38.595 -7.711 31.255 1.00 120.77 ? 31 ILE B CG1 1 ATOM 3026 C CG2 . ILE B 2 31 ? -36.344 -6.702 30.702 1.00 117.86 ? 31 ILE B CG2 1 ATOM 3027 C CD1 . ILE B 2 31 ? -38.844 -7.229 32.666 1.00 125.47 ? 31 ILE B CD1 1 ATOM 3028 N N . ARG B 2 32 ? -37.417 -7.338 27.896 1.00 126.02 ? 32 ARG B N 1 ATOM 3029 C CA . ARG B 2 32 ? -38.161 -6.731 26.796 1.00 120.90 ? 32 ARG B CA 1 ATOM 3030 C C . ARG B 2 32 ? -37.415 -6.932 25.486 1.00 115.77 ? 32 ARG B C 1 ATOM 3031 O O . ARG B 2 32 ? -37.553 -6.138 24.560 1.00 124.87 ? 32 ARG B O 1 ATOM 3032 C CB . ARG B 2 32 ? -38.384 -5.239 27.049 1.00 123.42 ? 32 ARG B CB 1 ATOM 3033 C CG . ARG B 2 32 ? -39.732 -4.892 27.679 1.00 135.87 ? 32 ARG B CG 1 ATOM 3034 C CD . ARG B 2 32 ? -40.864 -4.912 26.655 1.00 141.63 ? 32 ARG B CD 1 ATOM 3035 N NE . ARG B 2 32 ? -42.029 -4.157 27.118 1.00 149.27 ? 32 ARG B NE 1 ATOM 3036 C CZ . ARG B 2 32 ? -43.053 -4.685 27.784 1.00 153.11 ? 32 ARG B CZ 1 ATOM 3037 N NH1 . ARG B 2 32 ? -43.065 -5.980 28.067 1.00 153.12 ? 32 ARG B NH1 1 ATOM 3038 N NH2 . ARG B 2 32 ? -44.067 -3.919 28.166 1.00 154.75 ? 32 ARG B NH2 1 ATOM 3039 N N . CYS B 2 33 ? -36.632 -8.004 25.414 1.00 113.22 ? 33 CYS B N 1 ATOM 3040 C CA . CYS B 2 33 ? -35.687 -8.189 24.318 1.00 103.61 ? 33 CYS B CA 1 ATOM 3041 C C . CYS B 2 33 ? -35.168 -9.631 24.313 1.00 105.83 ? 33 CYS B C 1 ATOM 3042 O O . CYS B 2 33 ? -35.193 -10.298 25.350 1.00 112.21 ? 33 CYS B O 1 ATOM 3043 C CB . CYS B 2 33 ? -34.544 -7.186 24.464 1.00 92.81 ? 33 CYS B CB 1 ATOM 3044 S SG . CYS B 2 33 ? -33.470 -7.003 23.055 1.00 141.76 ? 33 CYS B SG 1 ATOM 3045 N N . LEU B 2 34 ? -34.716 -10.135 23.166 1.00 98.69 ? 34 LEU B N 1 ATOM 3046 C CA . LEU B 2 34 ? -34.272 -11.532 23.127 1.00 100.57 ? 34 LEU B CA 1 ATOM 3047 C C . LEU B 2 34 ? -32.788 -11.635 22.780 1.00 95.49 ? 34 LEU B C 1 ATOM 3048 O O . LEU B 2 34 ? -32.338 -11.126 21.759 1.00 87.39 ? 34 LEU B O 1 ATOM 3049 C CB . LEU B 2 34 ? -35.123 -12.347 22.139 1.00 109.61 ? 34 LEU B CB 1 ATOM 3050 C CG . LEU B 2 34 ? -34.942 -12.227 20.621 1.00 115.71 ? 34 LEU B CG 1 ATOM 3051 C CD1 . LEU B 2 34 ? -34.008 -13.312 20.083 1.00 118.85 ? 34 LEU B CD1 1 ATOM 3052 C CD2 . LEU B 2 34 ? -36.279 -12.259 19.903 1.00 118.29 ? 34 LEU B CD2 1 ATOM 3053 N N . CYS B 2 35 ? -32.016 -12.289 23.638 1.00 100.09 ? 35 CYS B N 1 ATOM 3054 C CA . CYS B 2 35 ? -30.579 -12.353 23.413 1.00 94.58 ? 35 CYS B CA 1 ATOM 3055 C C . CYS B 2 35 ? -30.112 -13.773 23.102 1.00 90.91 ? 35 CYS B C 1 ATOM 3056 O O . CYS B 2 35 ? -30.347 -14.708 23.873 1.00 88.52 ? 35 CYS B O 1 ATOM 3057 C CB . CYS B 2 35 ? -29.822 -11.814 24.624 1.00 94.42 ? 35 CYS B CB 1 ATOM 3058 S SG . CYS B 2 35 ? -30.209 -10.091 25.052 1.00 122.09 ? 35 CYS B SG 1 ATOM 3059 N N . GLU B 2 36 ? -29.454 -13.924 21.957 1.00 93.11 ? 36 GLU B N 1 ATOM 3060 C CA . GLU B 2 36 ? -28.845 -15.188 21.572 1.00 99.51 ? 36 GLU B CA 1 ATOM 3061 C C . GLU B 2 36 ? -27.325 -15.101 21.688 1.00 98.87 ? 36 GLU B C 1 ATOM 3062 O O . GLU B 2 36 ? -26.677 -14.278 21.031 1.00 92.06 ? 36 GLU B O 1 ATOM 3063 C CB . GLU B 2 36 ? -29.248 -15.572 20.146 1.00 107.25 ? 36 GLU B CB 1 ATOM 3064 C CG . GLU B 2 36 ? -28.873 -17.002 19.764 1.00 115.84 ? 36 GLU B CG 1 ATOM 3065 C CD . GLU B 2 36 ? -29.559 -17.485 18.497 1.00 118.75 ? 36 GLU B CD 1 ATOM 3066 O OE1 . GLU B 2 36 ? -29.655 -16.706 17.526 1.00 120.15 ? 36 GLU B OE1 1 ATOM 3067 O OE2 . GLU B 2 36 ? -30.005 -18.652 18.476 1.00 119.04 ? 36 GLU B OE2 1 ATOM 3068 N N . GLU B 2 37 ? -26.768 -15.945 22.548 1.00 112.76 ? 37 GLU B N 1 ATOM 3069 C CA . GLU B 2 37 ? -25.324 -16.082 22.676 0.50 117.93 ? 37 GLU B CA 1 ATOM 3070 C C . GLU B 2 37 ? -24.762 -16.696 21.406 1.00 126.35 ? 37 GLU B C 1 ATOM 3071 O O . GLU B 2 37 ? -24.781 -17.915 21.244 1.00 130.46 ? 37 GLU B O 1 ATOM 3072 C CB . GLU B 2 37 ? -24.961 -16.954 23.882 1.00 126.52 ? 37 GLU B CB 1 ATOM 3073 C CG . GLU B 2 37 ? -25.055 -16.265 25.229 1.00 132.94 ? 37 GLU B CG 1 ATOM 3074 C CD . GLU B 2 37 ? -23.716 -15.736 25.703 1.00 134.19 ? 37 GLU B CD 1 ATOM 3075 O OE1 . GLU B 2 37 ? -23.107 -14.928 24.972 1.00 125.68 ? 37 GLU B OE1 1 ATOM 3076 O OE2 . GLU B 2 37 ? -23.270 -16.135 26.802 1.00 141.78 ? 37 GLU B OE2 1 ATOM 3077 N N . LYS B 2 38 ? -24.274 -15.864 20.495 1.00 137.67 ? 38 LYS B N 1 ATOM 3078 C CA . LYS B 2 38 ? -23.682 -16.397 19.276 1.00 143.40 ? 38 LYS B CA 1 ATOM 3079 C C . LYS B 2 38 ? -22.300 -16.960 19.575 1.00 161.22 ? 38 LYS B C 1 ATOM 3080 O O . LYS B 2 38 ? -21.725 -16.678 20.624 1.00 160.02 ? 38 LYS B O 1 ATOM 3081 C CB . LYS B 2 38 ? -23.610 -15.333 18.182 1.00 127.46 ? 38 LYS B CB 1 ATOM 3082 C CG . LYS B 2 38 ? -24.686 -15.505 17.118 1.00 115.29 ? 38 LYS B CG 1 ATOM 3083 C CD . LYS B 2 38 ? -24.593 -16.879 16.462 1.00 109.22 ? 38 LYS B CD 1 ATOM 3084 C CE . LYS B 2 38 ? -25.918 -17.303 15.843 1.00 102.72 ? 38 LYS B CE 1 ATOM 3085 N NZ . LYS B 2 38 ? -26.449 -16.304 14.878 1.00 95.07 ? 38 LYS B NZ 1 ATOM 3086 N N . GLU B 2 39 ? -21.791 -17.765 18.649 1.00 180.31 ? 39 GLU B N 1 ATOM 3087 C CA . GLU B 2 39 ? -20.516 -18.457 18.807 1.00 184.73 ? 39 GLU B CA 1 ATOM 3088 C C . GLU B 2 39 ? -19.350 -17.543 19.197 1.00 183.07 ? 39 GLU B C 1 ATOM 3089 O O . GLU B 2 39 ? -18.489 -17.930 19.981 1.00 184.10 ? 39 GLU B O 1 ATOM 3090 C CB . GLU B 2 39 ? -20.170 -19.197 17.511 1.00 186.62 ? 39 GLU B CB 1 ATOM 3091 C CG . GLU B 2 39 ? -21.019 -18.799 16.303 1.00 188.58 ? 39 GLU B CG 1 ATOM 3092 C CD . GLU B 2 39 ? -20.765 -17.381 15.832 1.00 188.45 ? 39 GLU B CD 1 ATOM 3093 O OE1 . GLU B 2 39 ? -21.660 -16.802 15.188 1.00 185.16 ? 39 GLU B OE1 1 ATOM 3094 O OE2 . GLU B 2 39 ? -19.668 -16.850 16.089 1.00 191.42 ? 39 GLU B OE2 1 ATOM 3095 N N . ASN B 2 40 ? -19.322 -16.335 18.644 1.00 163.57 ? 40 ASN B N 1 ATOM 3096 C CA . ASN B 2 40 ? -18.227 -15.408 18.927 1.00 145.69 ? 40 ASN B CA 1 ATOM 3097 C C . ASN B 2 40 ? -18.644 -14.269 19.847 1.00 135.49 ? 40 ASN B C 1 ATOM 3098 O O . ASN B 2 40 ? -18.067 -14.085 20.920 1.00 142.60 ? 40 ASN B O 1 ATOM 3099 C CB . ASN B 2 40 ? -17.667 -14.838 17.622 1.00 143.49 ? 40 ASN B CB 1 ATOM 3100 C CG . ASN B 2 40 ? -16.148 -14.841 17.580 1.00 143.04 ? 40 ASN B CG 1 ATOM 3101 O OD1 . ASN B 2 40 ? -15.485 -15.027 18.600 1.00 144.31 ? 40 ASN B OD1 1 ATOM 3102 N ND2 . ASN B 2 40 ? -15.590 -14.628 16.394 1.00 139.47 ? 40 ASN B ND2 1 ATOM 3103 N N . VAL B 2 41 ? -19.629 -13.486 19.418 1.00 115.17 ? 41 VAL B N 1 ATOM 3104 C CA . VAL B 2 41 ? -20.113 -12.350 20.194 1.00 95.94 ? 41 VAL B CA 1 ATOM 3105 C C . VAL B 2 41 ? -21.532 -12.589 20.698 1.00 83.98 ? 41 VAL B C 1 ATOM 3106 O O . VAL B 2 41 ? -22.090 -13.682 20.560 1.00 86.28 ? 41 VAL B O 1 ATOM 3107 C CB . VAL B 2 41 ? -20.080 -11.053 19.361 1.00 80.89 ? 41 VAL B CB 1 ATOM 3108 C CG1 . VAL B 2 41 ? -18.671 -10.808 18.830 1.00 83.30 ? 41 VAL B CG1 1 ATOM 3109 C CG2 . VAL B 2 41 ? -21.094 -11.140 18.217 1.00 61.63 ? 41 VAL B CG2 1 ATOM 3110 N N . LEU B 2 42 ? -22.112 -11.552 21.283 1.00 69.80 ? 42 LEU B N 1 ATOM 3111 C CA . LEU B 2 42 ? -23.465 -11.645 21.790 1.00 71.83 ? 42 LEU B CA 1 ATOM 3112 C C . LEU B 2 42 ? -24.454 -10.933 20.880 1.00 77.06 ? 42 LEU B C 1 ATOM 3113 O O . LEU B 2 42 ? -24.253 -9.775 20.527 1.00 85.38 ? 42 LEU B O 1 ATOM 3114 C CB . LEU B 2 42 ? -23.547 -11.063 23.200 1.00 71.56 ? 42 LEU B CB 1 ATOM 3115 C CG . LEU B 2 42 ? -24.967 -11.047 23.768 1.00 68.53 ? 42 LEU B CG 1 ATOM 3116 C CD1 . LEU B 2 42 ? -25.538 -12.456 23.845 1.00 61.52 ? 42 LEU B CD1 1 ATOM 3117 C CD2 . LEU B 2 42 ? -25.027 -10.371 25.131 1.00 75.16 ? 42 LEU B CD2 1 ATOM 3118 N N . ASN B 2 43 ? -25.529 -11.626 20.517 1.00 75.93 ? 43 ASN B N 1 ATOM 3119 C CA . ASN B 2 43 ? -26.556 -11.040 19.664 1.00 70.29 ? 43 ASN B CA 1 ATOM 3120 C C . ASN B 2 43 ? -27.767 -10.564 20.465 1.00 68.79 ? 43 ASN B C 1 ATOM 3121 O O . ASN B 2 43 ? -28.475 -11.368 21.069 1.00 71.67 ? 43 ASN B O 1 ATOM 3122 C CB . ASN B 2 43 ? -26.999 -12.048 18.597 1.00 77.38 ? 43 ASN B CB 1 ATOM 3123 C CG . ASN B 2 43 ? -26.204 -11.929 17.305 1.00 77.67 ? 43 ASN B CG 1 ATOM 3124 O OD1 . ASN B 2 43 ? -26.774 -11.913 16.214 1.00 76.57 ? 43 ASN B OD1 1 ATOM 3125 N ND2 . ASN B 2 43 ? -24.883 -11.839 17.424 1.00 80.75 ? 43 ASN B ND2 1 ATOM 3126 N N . ILE B 2 44 ? -28.006 -9.256 20.469 1.00 69.20 ? 44 ILE B N 1 ATOM 3127 C CA . ILE B 2 44 ? -29.152 -8.692 21.178 1.00 70.93 ? 44 ILE B CA 1 ATOM 3128 C C . ILE B 2 44 ? -30.233 -8.235 20.207 1.00 68.35 ? 44 ILE B C 1 ATOM 3129 O O . ILE B 2 44 ? -30.043 -7.295 19.444 1.00 74.75 ? 44 ILE B O 1 ATOM 3130 C CB . ILE B 2 44 ? -28.749 -7.508 22.067 1.00 69.13 ? 44 ILE B CB 1 ATOM 3131 C CG1 . ILE B 2 44 ? -27.640 -7.926 23.034 1.00 74.77 ? 44 ILE B CG1 1 ATOM 3132 C CG2 . ILE B 2 44 ? -29.955 -6.985 22.833 1.00 59.78 ? 44 ILE B CG2 1 ATOM 3133 C CD1 . ILE B 2 44 ? -27.065 -6.784 23.844 1.00 70.63 ? 44 ILE B CD1 1 ATOM 3134 N N . ASN B 2 45 ? -31.374 -8.908 20.263 1.00 68.83 ? 45 ASN B N 1 ATOM 3135 C CA . ASN B 2 45 ? -32.472 -8.698 19.331 1.00 85.33 ? 45 ASN B CA 1 ATOM 3136 C C . ASN B 2 45 ? -33.633 -7.971 20.006 1.00 96.35 ? 45 ASN B C 1 ATOM 3137 O O . ASN B 2 45 ? -34.489 -8.597 20.645 1.00 99.37 ? 45 ASN B O 1 ATOM 3138 C CB . ASN B 2 45 ? -32.917 -10.053 18.763 1.00 96.97 ? 45 ASN B CB 1 ATOM 3139 C CG . ASN B 2 45 ? -33.966 -9.933 17.665 1.00 102.07 ? 45 ASN B CG 1 ATOM 3140 O OD1 . ASN B 2 45 ? -34.925 -9.173 17.775 1.00 101.35 ? 45 ASN B OD1 1 ATOM 3141 N ND2 . ASN B 2 45 ? -33.793 -10.714 16.604 1.00 104.51 ? 45 ASN B ND2 1 ATOM 3142 N N . CYS B 2 46 ? -33.633 -6.643 19.883 1.00 100.78 ? 46 CYS B N 1 ATOM 3143 C CA . CYS B 2 46 ? -34.719 -5.803 20.386 1.00 106.11 ? 46 CYS B CA 1 ATOM 3144 C C . CYS B 2 46 ? -35.580 -5.330 19.222 1.00 99.31 ? 46 CYS B C 1 ATOM 3145 O O . CYS B 2 46 ? -36.201 -4.267 19.270 1.00 93.98 ? 46 CYS B O 1 ATOM 3146 C CB . CYS B 2 46 ? -34.173 -4.605 21.168 1.00 107.34 ? 46 CYS B CB 1 ATOM 3147 S SG . CYS B 2 46 ? -33.604 -4.992 22.837 1.00 76.83 ? 46 CYS B SG 1 ATOM 3148 N N . GLU B 2 47 ? -35.602 -6.147 18.177 1.00 96.32 ? 47 GLU B N 1 ATOM 3149 C CA . GLU B 2 47 ? -36.340 -5.866 16.958 1.00 98.39 ? 47 GLU B CA 1 ATOM 3150 C C . GLU B 2 47 ? -37.846 -5.780 17.207 1.00 98.07 ? 47 GLU B C 1 ATOM 3151 O O . GLU B 2 47 ? -38.409 -6.578 17.960 1.00 101.63 ? 47 GLU B O 1 ATOM 3152 C CB . GLU B 2 47 ? -36.034 -6.958 15.927 1.00 107.55 ? 47 GLU B CB 1 ATOM 3153 C CG . GLU B 2 47 ? -36.364 -6.637 14.482 1.00 122.53 ? 47 GLU B CG 1 ATOM 3154 C CD . GLU B 2 47 ? -35.564 -7.505 13.521 1.00 131.61 ? 47 GLU B CD 1 ATOM 3155 O OE1 . GLU B 2 47 ? -34.348 -7.263 13.378 1.00 130.52 ? 47 GLU B OE1 1 ATOM 3156 O OE2 . GLU B 2 47 ? -36.145 -8.429 12.915 1.00 137.12 ? 47 GLU B OE2 1 ATOM 3157 N N . ASN B 2 48 ? -38.481 -4.790 16.590 1.00 96.19 ? 48 ASN B N 1 ATOM 3158 C CA . ASN B 2 48 ? -39.927 -4.744 16.466 1.00 98.37 ? 48 ASN B CA 1 ATOM 3159 C C . ASN B 2 48 ? -40.696 -4.706 17.782 1.00 92.34 ? 48 ASN B C 1 ATOM 3160 O O . ASN B 2 48 ? -41.847 -5.143 17.851 1.00 91.35 ? 48 ASN B O 1 ATOM 3161 C CB . ASN B 2 48 ? -40.409 -5.948 15.656 1.00 103.44 ? 48 ASN B CB 1 ATOM 3162 C CG . ASN B 2 48 ? -41.461 -5.573 14.635 1.00 106.78 ? 48 ASN B CG 1 ATOM 3163 O OD1 . ASN B 2 48 ? -41.150 -4.976 13.604 1.00 98.57 ? 48 ASN B OD1 1 ATOM 3164 N ND2 . ASN B 2 48 ? -42.711 -5.929 14.908 1.00 115.97 ? 48 ASN B ND2 1 ATOM 3165 N N . LYS B 2 49 ? -40.080 -4.183 18.831 1.00 90.60 ? 49 LYS B N 1 ATOM 3166 C CA . LYS B 2 49 ? -40.722 -4.157 20.136 1.00 92.57 ? 49 LYS B CA 1 ATOM 3167 C C . LYS B 2 49 ? -41.406 -2.838 20.423 1.00 76.06 ? 49 LYS B C 1 ATOM 3168 O O . LYS B 2 49 ? -41.872 -2.592 21.542 1.00 67.80 ? 49 LYS B O 1 ATOM 3169 C CB . LYS B 2 49 ? -39.709 -4.462 21.237 1.00 104.31 ? 49 LYS B CB 1 ATOM 3170 C CG . LYS B 2 49 ? -39.263 -5.898 21.198 1.00 110.35 ? 49 LYS B CG 1 ATOM 3171 C CD . LYS B 2 49 ? -40.077 -6.759 22.160 1.00 108.41 ? 49 LYS B CD 1 ATOM 3172 C CE . LYS B 2 49 ? -40.141 -8.200 21.684 1.00 112.59 ? 49 LYS B CE 1 ATOM 3173 N NZ . LYS B 2 49 ? -38.766 -8.595 21.309 1.00 117.27 ? 49 LYS B NZ 1 ATOM 3174 N N . GLY B 2 50 ? -41.463 -1.978 19.421 1.00 72.81 ? 50 GLY B N 1 ATOM 3175 C CA . GLY B 2 50 ? -42.161 -0.721 19.541 1.00 76.04 ? 50 GLY B CA 1 ATOM 3176 C C . GLY B 2 50 ? -41.578 0.230 20.568 1.00 82.78 ? 50 GLY B C 1 ATOM 3177 O O . GLY B 2 50 ? -42.318 0.983 21.208 1.00 85.37 ? 50 GLY B O 1 ATOM 3178 N N . PHE B 2 51 ? -40.257 0.212 20.730 1.00 87.44 ? 51 PHE B N 1 ATOM 3179 C CA . PHE B 2 51 ? -39.578 1.163 21.608 1.00 89.21 ? 51 PHE B CA 1 ATOM 3180 C C . PHE B 2 51 ? -39.494 2.515 20.917 1.00 92.11 ? 51 PHE B C 1 ATOM 3181 O O . PHE B 2 51 ? -39.163 2.590 19.735 1.00 89.06 ? 51 PHE B O 1 ATOM 3182 C CB . PHE B 2 51 ? -38.172 0.684 21.974 1.00 89.72 ? 51 PHE B CB 1 ATOM 3183 C CG . PHE B 2 51 ? -38.140 -0.592 22.787 1.00 96.64 ? 51 PHE B CG 1 ATOM 3184 C CD1 . PHE B 2 51 ? -36.929 -1.202 23.069 1.00 96.92 ? 51 PHE B CD1 1 ATOM 3185 C CD2 . PHE B 2 51 ? -39.304 -1.177 23.245 1.00 108.25 ? 51 PHE B CD2 1 ATOM 3186 C CE1 . PHE B 2 51 ? -36.878 -2.376 23.805 1.00 105.27 ? 51 PHE B CE1 1 ATOM 3187 C CE2 . PHE B 2 51 ? -39.256 -2.351 24.006 1.00 118.33 ? 51 PHE B CE2 1 ATOM 3188 C CZ . PHE B 2 51 ? -38.045 -2.945 24.273 1.00 119.43 ? 51 PHE B CZ 1 ATOM 3189 N N . THR B 2 52 ? -39.792 3.587 21.641 1.00 102.32 ? 52 THR B N 1 ATOM 3190 C CA . THR B 2 52 ? -39.700 4.927 21.088 1.00 108.93 ? 52 THR B CA 1 ATOM 3191 C C . THR B 2 52 ? -38.395 5.566 21.562 1.00 105.50 ? 52 THR B C 1 ATOM 3192 O O . THR B 2 52 ? -38.013 6.655 21.134 1.00 101.78 ? 52 THR B O 1 ATOM 3193 C CB . THR B 2 52 ? -40.907 5.785 21.508 1.00 116.84 ? 52 THR B CB 1 ATOM 3194 O OG1 . THR B 2 52 ? -42.121 5.041 21.319 1.00 129.51 ? 52 THR B OG1 1 ATOM 3195 C CG2 . THR B 2 52 ? -40.979 7.079 20.707 1.00 112.81 ? 52 THR B CG2 1 ATOM 3196 N N . THR B 2 53 ? -37.713 4.871 22.465 1.00 105.73 ? 53 THR B N 1 ATOM 3197 C CA . THR B 2 53 ? -36.517 5.415 23.090 1.00 102.37 ? 53 THR B CA 1 ATOM 3198 C C . THR B 2 53 ? -35.572 4.307 23.528 1.00 103.48 ? 53 THR B C 1 ATOM 3199 O O . THR B 2 53 ? -35.989 3.173 23.740 1.00 111.20 ? 53 THR B O 1 ATOM 3200 C CB . THR B 2 53 ? -36.878 6.279 24.308 1.00 116.28 ? 53 THR B CB 1 ATOM 3201 O OG1 . THR B 2 53 ? -38.017 7.090 23.994 1.00 128.42 ? 53 THR B OG1 1 ATOM 3202 C CG2 . THR B 2 53 ? -35.714 7.182 24.713 1.00 119.79 ? 53 THR B CG2 1 ATOM 3203 N N . VAL B 2 54 ? -34.295 4.639 23.661 1.00 105.50 ? 54 VAL B N 1 ATOM 3204 C CA . VAL B 2 54 ? -33.305 3.668 24.088 1.00 105.77 ? 54 VAL B CA 1 ATOM 3205 C C . VAL B 2 54 ? -32.982 3.869 25.561 1.00 107.27 ? 54 VAL B C 1 ATOM 3206 O O . VAL B 2 54 ? -32.033 3.290 26.082 1.00 106.88 ? 54 VAL B O 1 ATOM 3207 C CB . VAL B 2 54 ? -32.027 3.783 23.248 1.00 100.73 ? 54 VAL B CB 1 ATOM 3208 C CG1 . VAL B 2 54 ? -31.347 2.430 23.112 1.00 98.09 ? 54 VAL B CG1 1 ATOM 3209 C CG2 . VAL B 2 54 ? -32.369 4.336 21.879 1.00 100.16 ? 54 VAL B CG2 1 ATOM 3210 N N . SER B 2 55 ? -33.785 4.690 26.230 1.00 109.34 ? 55 SER B N 1 ATOM 3211 C CA . SER B 2 55 ? -33.564 5.001 27.636 1.00 117.19 ? 55 SER B CA 1 ATOM 3212 C C . SER B 2 55 ? -33.803 3.794 28.534 1.00 118.06 ? 55 SER B C 1 ATOM 3213 O O . SER B 2 55 ? -33.157 3.645 29.570 1.00 120.33 ? 55 SER B O 1 ATOM 3214 C CB . SER B 2 55 ? -34.470 6.154 28.075 1.00 124.20 ? 55 SER B CB 1 ATOM 3215 O OG . SER B 2 55 ? -34.139 7.356 27.400 1.00 127.47 ? 55 SER B OG 1 ATOM 3216 N N . LEU B 2 56 ? -34.724 2.928 28.125 1.00 118.21 ? 56 LEU B N 1 ATOM 3217 C CA . LEU B 2 56 ? -35.201 1.853 28.989 1.00 116.03 ? 56 LEU B CA 1 ATOM 3218 C C . LEU B 2 56 ? -34.155 0.777 29.263 1.00 115.15 ? 56 LEU B C 1 ATOM 3219 O O . LEU B 2 56 ? -33.959 0.388 30.410 1.00 123.10 ? 56 LEU B O 1 ATOM 3220 C CB . LEU B 2 56 ? -36.454 1.210 28.384 1.00 108.37 ? 56 LEU B CB 1 ATOM 3221 C CG . LEU B 2 56 ? -37.025 -0.045 29.050 1.00 111.16 ? 56 LEU B CG 1 ATOM 3222 C CD1 . LEU B 2 56 ? -37.248 0.167 30.544 1.00 118.33 ? 56 LEU B CD1 1 ATOM 3223 C CD2 . LEU B 2 56 ? -38.323 -0.454 28.360 1.00 110.93 ? 56 LEU B CD2 1 ATOM 3224 N N . LEU B 2 57 ? -33.486 0.295 28.223 1.00 106.13 ? 57 LEU B N 1 ATOM 3225 C CA . LEU B 2 57 ? -32.647 -0.889 28.371 1.00 98.79 ? 57 LEU B CA 1 ATOM 3226 C C . LEU B 2 57 ? -31.174 -0.598 28.643 1.00 101.51 ? 57 LEU B C 1 ATOM 3227 O O . LEU B 2 57 ? -30.551 0.249 27.999 1.00 92.86 ? 57 LEU B O 1 ATOM 3228 C CB . LEU B 2 57 ? -32.775 -1.767 27.130 1.00 84.75 ? 57 LEU B CB 1 ATOM 3229 C CG . LEU B 2 57 ? -33.180 -1.045 25.847 1.00 73.48 ? 57 LEU B CG 1 ATOM 3230 C CD1 . LEU B 2 57 ? -32.042 -0.211 25.302 1.00 53.79 ? 57 LEU B CD1 1 ATOM 3231 C CD2 . LEU B 2 57 ? -33.622 -2.060 24.829 1.00 53.88 ? 57 LEU B CD2 1 ATOM 3232 N N . GLN B 2 58 ? -30.631 -1.321 29.617 1.00 108.02 ? 58 GLN B N 1 ATOM 3233 C CA . GLN B 2 58 ? -29.217 -1.244 29.947 1.00 113.69 ? 58 GLN B CA 1 ATOM 3234 C C . GLN B 2 58 ? -28.431 -2.261 29.134 1.00 110.72 ? 58 GLN B C 1 ATOM 3235 O O . GLN B 2 58 ? -28.564 -3.465 29.351 1.00 119.78 ? 58 GLN B O 1 ATOM 3236 C CB . GLN B 2 58 ? -28.995 -1.496 31.437 1.00 123.10 ? 58 GLN B CB 1 ATOM 3237 C CG . GLN B 2 58 ? -29.861 -0.659 32.354 1.00 132.65 ? 58 GLN B CG 1 ATOM 3238 C CD . GLN B 2 58 ? -30.145 -1.365 33.663 1.00 146.79 ? 58 GLN B CD 1 ATOM 3239 O OE1 . GLN B 2 58 ? -30.652 -2.488 33.677 1.00 150.46 ? 58 GLN B OE1 1 ATOM 3240 N NE2 . GLN B 2 58 ? -29.810 -0.716 34.773 1.00 154.47 ? 58 GLN B NE2 1 ATOM 3241 N N . PRO B 2 59 ? -27.608 -1.783 28.192 1.00 96.78 ? 59 PRO B N 1 ATOM 3242 C CA . PRO B 2 59 ? -26.747 -2.695 27.439 1.00 86.12 ? 59 PRO B CA 1 ATOM 3243 C C . PRO B 2 59 ? -25.673 -3.275 28.342 1.00 85.35 ? 59 PRO B C 1 ATOM 3244 O O . PRO B 2 59 ? -25.440 -2.725 29.417 1.00 94.05 ? 59 PRO B O 1 ATOM 3245 C CB . PRO B 2 59 ? -26.127 -1.788 26.380 1.00 82.74 ? 59 PRO B CB 1 ATOM 3246 C CG . PRO B 2 59 ? -26.062 -0.460 27.060 1.00 90.30 ? 59 PRO B CG 1 ATOM 3247 C CD . PRO B 2 59 ? -27.344 -0.375 27.848 1.00 98.94 ? 59 PRO B CD 1 ATOM 3248 N N . PRO B 2 60 ? -25.030 -4.374 27.926 1.00 79.24 ? 60 PRO B N 1 ATOM 3249 C CA . PRO B 2 60 ? -23.839 -4.797 28.666 1.00 81.52 ? 60 PRO B CA 1 ATOM 3250 C C . PRO B 2 60 ? -22.706 -3.803 28.432 1.00 85.10 ? 60 PRO B C 1 ATOM 3251 O O . PRO B 2 60 ? -22.648 -3.183 27.367 1.00 73.77 ? 60 PRO B O 1 ATOM 3252 C CB . PRO B 2 60 ? -23.523 -6.175 28.080 1.00 76.24 ? 60 PRO B CB 1 ATOM 3253 C CG . PRO B 2 60 ? -24.150 -6.166 26.733 1.00 75.27 ? 60 PRO B CG 1 ATOM 3254 C CD . PRO B 2 60 ? -25.376 -5.310 26.844 1.00 76.78 ? 60 PRO B CD 1 ATOM 3255 N N . GLN B 2 61 ? -21.825 -3.643 29.414 1.00 94.60 ? 61 GLN B N 1 ATOM 3256 C CA . GLN B 2 61 ? -20.836 -2.574 29.355 1.00 100.30 ? 61 GLN B CA 1 ATOM 3257 C C . GLN B 2 61 ? -19.441 -3.050 28.970 1.00 105.51 ? 61 GLN B C 1 ATOM 3258 O O . GLN B 2 61 ? -18.699 -2.321 28.311 1.00 112.42 ? 61 GLN B O 1 ATOM 3259 C CB . GLN B 2 61 ? -20.783 -1.834 30.693 1.00 100.87 ? 61 GLN B CB 1 ATOM 3260 C CG . GLN B 2 61 ? -22.039 -1.028 30.979 1.00 97.90 ? 61 GLN B CG 1 ATOM 3261 C CD . GLN B 2 61 ? -22.417 -0.112 29.826 1.00 93.65 ? 61 GLN B CD 1 ATOM 3262 O OE1 . GLN B 2 61 ? -21.570 0.591 29.272 1.00 102.77 ? 61 GLN B OE1 1 ATOM 3263 N NE2 . GLN B 2 61 ? -23.693 -0.123 29.454 1.00 85.73 ? 61 GLN B NE2 1 ATOM 3264 N N . TYR B 2 62 ? -19.077 -4.264 29.370 1.00 108.53 ? 62 TYR B N 1 ATOM 3265 C CA . TYR B 2 62 ? -17.757 -4.773 29.016 1.00 115.28 ? 62 TYR B CA 1 ATOM 3266 C C . TYR B 2 62 ? -17.797 -5.896 27.978 1.00 110.03 ? 62 TYR B C 1 ATOM 3267 O O . TYR B 2 62 ? -16.761 -6.262 27.422 1.00 115.58 ? 62 TYR B O 1 ATOM 3268 C CB . TYR B 2 62 ? -17.002 -5.256 30.258 1.00 136.99 ? 62 TYR B CB 1 ATOM 3269 C CG . TYR B 2 62 ? -15.658 -5.855 29.908 1.00 154.70 ? 62 TYR B CG 1 ATOM 3270 C CD1 . TYR B 2 62 ? -14.644 -5.069 29.370 1.00 162.81 ? 62 TYR B CD1 1 ATOM 3271 C CD2 . TYR B 2 62 ? -15.419 -7.211 30.070 1.00 159.20 ? 62 TYR B CD2 1 ATOM 3272 C CE1 . TYR B 2 62 ? -13.420 -5.616 29.028 1.00 167.64 ? 62 TYR B CE1 1 ATOM 3273 C CE2 . TYR B 2 62 ? -14.203 -7.766 29.726 1.00 165.55 ? 62 TYR B CE2 1 ATOM 3274 C CZ . TYR B 2 62 ? -13.203 -6.965 29.211 1.00 169.27 ? 62 TYR B CZ 1 ATOM 3275 O OH . TYR B 2 62 ? -11.985 -7.515 28.875 1.00 169.30 ? 62 TYR B OH 1 ATOM 3276 N N . ARG B 2 63 ? -18.970 -6.444 27.683 1.00 103.83 ? 63 ARG B N 1 ATOM 3277 C CA . ARG B 2 63 ? -18.995 -7.470 26.649 1.00 94.43 ? 63 ARG B CA 1 ATOM 3278 C C . ARG B 2 63 ? -19.329 -6.901 25.272 1.00 86.28 ? 63 ARG B C 1 ATOM 3279 O O . ARG B 2 63 ? -20.168 -6.012 25.128 1.00 76.43 ? 63 ARG B O 1 ATOM 3280 C CB . ARG B 2 63 ? -19.974 -8.588 26.993 1.00 90.23 ? 63 ARG B CB 1 ATOM 3281 C CG . ARG B 2 63 ? -19.734 -9.819 26.137 1.00 88.61 ? 63 ARG B CG 1 ATOM 3282 C CD . ARG B 2 63 ? -20.903 -10.756 26.162 1.00 94.24 ? 63 ARG B CD 1 ATOM 3283 N NE . ARG B 2 63 ? -20.695 -11.853 27.098 1.00 100.44 ? 63 ARG B NE 1 ATOM 3284 C CZ . ARG B 2 63 ? -21.529 -12.877 27.219 1.00 113.59 ? 63 ARG B CZ 1 ATOM 3285 N NH1 . ARG B 2 63 ? -22.616 -12.931 26.464 1.00 117.88 ? 63 ARG B NH1 1 ATOM 3286 N NH2 . ARG B 2 63 ? -21.276 -13.843 28.087 1.00 119.72 ? 63 ARG B NH2 1 ATOM 3287 N N . ILE B 2 64 ? -18.652 -7.434 24.264 1.00 89.18 ? 64 ILE B N 1 ATOM 3288 C CA . ILE B 2 64 ? -18.858 -7.026 22.888 1.00 90.17 ? 64 ILE B CA 1 ATOM 3289 C C . ILE B 2 64 ? -20.172 -7.631 22.377 1.00 89.67 ? 64 ILE B C 1 ATOM 3290 O O . ILE B 2 64 ? -20.534 -8.748 22.753 1.00 87.83 ? 64 ILE B O 1 ATOM 3291 C CB . ILE B 2 64 ? -17.646 -7.445 22.017 1.00 93.91 ? 64 ILE B CB 1 ATOM 3292 C CG1 . ILE B 2 64 ? -17.561 -6.593 20.755 1.00 97.81 ? 64 ILE B CG1 1 ATOM 3293 C CG2 . ILE B 2 64 ? -17.652 -8.943 21.726 1.00 97.89 ? 64 ILE B CG2 1 ATOM 3294 C CD1 . ILE B 2 64 ? -17.204 -5.146 21.024 1.00 102.12 ? 64 ILE B CD1 1 ATOM 3295 N N . TYR B 2 65 ? -20.904 -6.885 21.550 1.00 87.15 ? 65 TYR B N 1 ATOM 3296 C CA . TYR B 2 65 ? -22.231 -7.325 21.116 1.00 84.23 ? 65 TYR B CA 1 ATOM 3297 C C . TYR B 2 65 ? -22.749 -6.652 19.842 1.00 87.22 ? 65 TYR B C 1 ATOM 3298 O O . TYR B 2 65 ? -22.144 -5.712 19.320 1.00 90.11 ? 65 TYR B O 1 ATOM 3299 C CB . TYR B 2 65 ? -23.249 -7.095 22.238 1.00 83.54 ? 65 TYR B CB 1 ATOM 3300 C CG . TYR B 2 65 ? -23.387 -5.645 22.661 1.00 90.02 ? 65 TYR B CG 1 ATOM 3301 C CD1 . TYR B 2 65 ? -24.251 -4.780 21.998 1.00 92.72 ? 65 TYR B CD1 1 ATOM 3302 C CD2 . TYR B 2 65 ? -22.656 -5.145 23.728 1.00 98.40 ? 65 TYR B CD2 1 ATOM 3303 C CE1 . TYR B 2 65 ? -24.376 -3.455 22.387 1.00 95.21 ? 65 TYR B CE1 1 ATOM 3304 C CE2 . TYR B 2 65 ? -22.775 -3.824 24.126 1.00 103.70 ? 65 TYR B CE2 1 ATOM 3305 C CZ . TYR B 2 65 ? -23.635 -2.985 23.453 1.00 102.70 ? 65 TYR B CZ 1 ATOM 3306 O OH . TYR B 2 65 ? -23.753 -1.672 23.849 1.00 107.21 ? 65 TYR B OH 1 ATOM 3307 N N . GLN B 2 66 ? -23.889 -7.148 19.364 1.00 84.52 ? 66 GLN B N 1 ATOM 3308 C CA . GLN B 2 66 ? -24.623 -6.553 18.247 1.00 82.30 ? 66 GLN B CA 1 ATOM 3309 C C . GLN B 2 66 ? -26.041 -6.206 18.690 1.00 77.98 ? 66 GLN B C 1 ATOM 3310 O O . GLN B 2 66 ? -26.632 -6.926 19.490 1.00 78.52 ? 66 GLN B O 1 ATOM 3311 C CB . GLN B 2 66 ? -24.677 -7.505 17.051 1.00 88.25 ? 66 GLN B CB 1 ATOM 3312 C CG . GLN B 2 66 ? -23.335 -7.855 16.437 1.00 89.78 ? 66 GLN B CG 1 ATOM 3313 C CD . GLN B 2 66 ? -23.488 -8.573 15.109 1.00 86.05 ? 66 GLN B CD 1 ATOM 3314 O OE1 . GLN B 2 66 ? -24.504 -9.219 14.854 1.00 88.36 ? 66 GLN B OE1 1 ATOM 3315 N NE2 . GLN B 2 66 ? -22.482 -8.453 14.250 1.00 83.44 ? 66 GLN B NE2 1 ATOM 3316 N N . LEU B 2 67 ? -26.599 -5.119 18.166 1.00 67.90 ? 67 LEU B N 1 ATOM 3317 C CA . LEU B 2 67 ? -27.917 -4.673 18.614 1.00 64.83 ? 67 LEU B CA 1 ATOM 3318 C C . LEU B 2 67 ? -28.898 -4.456 17.460 1.00 70.76 ? 67 LEU B C 1 ATOM 3319 O O . LEU B 2 67 ? -28.695 -3.584 16.616 1.00 66.91 ? 67 LEU B O 1 ATOM 3320 C CB . LEU B 2 67 ? -27.778 -3.387 19.431 1.00 58.29 ? 67 LEU B CB 1 ATOM 3321 C CG . LEU B 2 67 ? -29.057 -2.813 20.038 1.00 57.00 ? 67 LEU B CG 1 ATOM 3322 C CD1 . LEU B 2 67 ? -29.742 -3.852 20.909 1.00 59.51 ? 67 LEU B CD1 1 ATOM 3323 C CD2 . LEU B 2 67 ? -28.747 -1.561 20.838 1.00 59.48 ? 67 LEU B CD2 1 ATOM 3324 N N . PHE B 2 68 ? -29.964 -5.252 17.433 1.00 78.74 ? 68 PHE B N 1 ATOM 3325 C CA . PHE B 2 68 ? -30.991 -5.147 16.398 1.00 82.31 ? 68 PHE B CA 1 ATOM 3326 C C . PHE B 2 68 ? -32.160 -4.317 16.923 1.00 86.98 ? 68 PHE B C 1 ATOM 3327 O O . PHE B 2 68 ? -32.830 -4.718 17.877 1.00 89.00 ? 68 PHE B O 1 ATOM 3328 C CB . PHE B 2 68 ? -31.498 -6.531 15.961 1.00 85.51 ? 68 PHE B CB 1 ATOM 3329 C CG . PHE B 2 68 ? -30.420 -7.475 15.483 1.00 81.27 ? 68 PHE B CG 1 ATOM 3330 C CD1 . PHE B 2 68 ? -30.698 -8.827 15.330 1.00 89.75 ? 68 PHE B CD1 1 ATOM 3331 C CD2 . PHE B 2 68 ? -29.144 -7.023 15.182 1.00 72.55 ? 68 PHE B CD2 1 ATOM 3332 C CE1 . PHE B 2 68 ? -29.728 -9.707 14.895 1.00 93.60 ? 68 PHE B CE1 1 ATOM 3333 C CE2 . PHE B 2 68 ? -28.168 -7.898 14.750 1.00 71.99 ? 68 PHE B CE2 1 ATOM 3334 C CZ . PHE B 2 68 ? -28.460 -9.241 14.604 1.00 86.23 ? 68 PHE B CZ 1 ATOM 3335 N N . LEU B 2 69 ? -32.409 -3.167 16.302 1.00 82.92 ? 69 LEU B N 1 ATOM 3336 C CA . LEU B 2 69 ? -33.466 -2.269 16.765 1.00 78.46 ? 69 LEU B CA 1 ATOM 3337 C C . LEU B 2 69 ? -34.460 -1.905 15.667 1.00 83.29 ? 69 LEU B C 1 ATOM 3338 O O . LEU B 2 69 ? -35.102 -0.857 15.725 1.00 87.11 ? 69 LEU B O 1 ATOM 3339 C CB . LEU B 2 69 ? -32.856 -0.995 17.350 1.00 67.10 ? 69 LEU B CB 1 ATOM 3340 C CG . LEU B 2 69 ? -32.418 -1.088 18.811 1.00 67.62 ? 69 LEU B CG 1 ATOM 3341 C CD1 . LEU B 2 69 ? -31.553 0.102 19.183 1.00 62.46 ? 69 LEU B CD1 1 ATOM 3342 C CD2 . LEU B 2 69 ? -33.640 -1.167 19.711 1.00 76.92 ? 69 LEU B CD2 1 ATOM 3343 N N . ASN B 2 70 ? -34.587 -2.778 14.673 1.00 86.83 ? 70 ASN B N 1 ATOM 3344 C CA . ASN B 2 70 ? -35.542 -2.575 13.590 1.00 87.56 ? 70 ASN B CA 1 ATOM 3345 C C . ASN B 2 70 ? -36.981 -2.501 14.102 1.00 87.95 ? 70 ASN B C 1 ATOM 3346 O O . ASN B 2 70 ? -37.278 -2.959 15.204 1.00 96.55 ? 70 ASN B O 1 ATOM 3347 C CB . ASN B 2 70 ? -35.417 -3.700 12.560 1.00 93.19 ? 70 ASN B CB 1 ATOM 3348 C CG . ASN B 2 70 ? -34.007 -3.847 12.021 1.00 102.35 ? 70 ASN B CG 1 ATOM 3349 O OD1 . ASN B 2 70 ? -33.316 -2.859 11.781 1.00 109.61 ? 70 ASN B OD1 1 ATOM 3350 N ND2 . ASN B 2 70 ? -33.572 -5.088 11.829 1.00 102.21 ? 70 ASN B ND2 1 ATOM 3351 N N . GLY B 2 71 ? -37.866 -1.914 13.301 1.00 82.35 ? 71 GLY B N 1 ATOM 3352 C CA . GLY B 2 71 ? -39.291 -1.920 13.588 1.00 83.91 ? 71 GLY B CA 1 ATOM 3353 C C . GLY B 2 71 ? -39.727 -1.254 14.882 1.00 80.65 ? 71 GLY B C 1 ATOM 3354 O O . GLY B 2 71 ? -40.767 -1.603 15.447 1.00 78.59 ? 71 GLY B O 1 ATOM 3355 N N . ASN B 2 72 ? -38.936 -0.294 15.353 1.00 77.57 ? 72 ASN B N 1 ATOM 3356 C CA . ASN B 2 72 ? -39.279 0.486 16.541 1.00 79.54 ? 72 ASN B CA 1 ATOM 3357 C C . ASN B 2 72 ? -39.545 1.951 16.201 1.00 79.06 ? 72 ASN B C 1 ATOM 3358 O O . ASN B 2 72 ? -38.688 2.633 15.636 1.00 86.79 ? 72 ASN B O 1 ATOM 3359 C CB . ASN B 2 72 ? -38.164 0.398 17.585 1.00 80.15 ? 72 ASN B CB 1 ATOM 3360 C CG . ASN B 2 72 ? -38.110 -0.950 18.275 1.00 80.85 ? 72 ASN B CG 1 ATOM 3361 O OD1 . ASN B 2 72 ? -39.140 -1.578 18.523 1.00 84.08 ? 72 ASN B OD1 1 ATOM 3362 N ND2 . ASN B 2 72 ? -36.902 -1.401 18.593 1.00 80.87 ? 72 ASN B ND2 1 ATOM 3363 N N . LEU B 2 73 ? -40.730 2.431 16.559 1.00 74.00 ? 73 LEU B N 1 ATOM 3364 C CA . LEU B 2 73 ? -41.149 3.786 16.217 1.00 79.74 ? 73 LEU B CA 1 ATOM 3365 C C . LEU B 2 73 ? -40.446 4.880 17.021 1.00 86.04 ? 73 LEU B C 1 ATOM 3366 O O . LEU B 2 73 ? -40.902 5.247 18.098 1.00 89.88 ? 73 LEU B O 1 ATOM 3367 C CB . LEU B 2 73 ? -42.666 3.936 16.396 1.00 81.51 ? 73 LEU B CB 1 ATOM 3368 C CG . LEU B 2 73 ? -43.469 3.010 17.315 1.00 86.77 ? 73 LEU B CG 1 ATOM 3369 C CD1 . LEU B 2 73 ? -42.974 3.020 18.755 1.00 94.62 ? 73 LEU B CD1 1 ATOM 3370 C CD2 . LEU B 2 73 ? -44.944 3.401 17.248 1.00 90.66 ? 73 LEU B CD2 1 ATOM 3371 N N . LEU B 2 74 ? -39.338 5.402 16.503 1.00 90.83 ? 74 LEU B N 1 ATOM 3372 C CA . LEU B 2 74 ? -38.805 6.652 17.034 1.00 97.95 ? 74 LEU B CA 1 ATOM 3373 C C . LEU B 2 74 ? -38.713 7.687 15.915 1.00 108.51 ? 74 LEU B C 1 ATOM 3374 O O . LEU B 2 74 ? -38.080 7.461 14.884 1.00 105.19 ? 74 LEU B O 1 ATOM 3375 C CB . LEU B 2 74 ? -37.442 6.464 17.724 1.00 84.37 ? 74 LEU B CB 1 ATOM 3376 C CG . LEU B 2 74 ? -36.310 5.493 17.357 1.00 65.00 ? 74 LEU B CG 1 ATOM 3377 C CD1 . LEU B 2 74 ? -36.497 4.118 17.994 1.00 46.42 ? 74 LEU B CD1 1 ATOM 3378 C CD2 . LEU B 2 74 ? -36.112 5.379 15.866 1.00 69.72 ? 74 LEU B CD2 1 ATOM 3379 N N . THR B 2 75 ? -39.387 8.812 16.113 1.00 120.18 ? 75 THR B N 1 ATOM 3380 C CA . THR B 2 75 ? -39.375 9.883 15.132 1.00 126.75 ? 75 THR B CA 1 ATOM 3381 C C . THR B 2 75 ? -37.966 10.431 14.965 1.00 125.66 ? 75 THR B C 1 ATOM 3382 O O . THR B 2 75 ? -37.486 10.607 13.847 1.00 129.16 ? 75 THR B O 1 ATOM 3383 C CB . THR B 2 75 ? -40.332 11.022 15.530 1.00 148.16 ? 75 THR B CB 1 ATOM 3384 O OG1 . THR B 2 75 ? -40.456 11.065 16.957 1.00 151.05 ? 75 THR B OG1 1 ATOM 3385 C CG2 . THR B 2 75 ? -41.705 10.795 14.923 1.00 149.85 ? 75 THR B CG2 1 ATOM 3386 N N . ARG B 2 76 ? -37.301 10.688 16.085 1.00 112.02 ? 76 ARG B N 1 ATOM 3387 C CA . ARG B 2 76 ? -35.996 11.332 16.052 1.00 100.96 ? 76 ARG B CA 1 ATOM 3388 C C . ARG B 2 76 ? -34.986 10.643 16.962 1.00 84.46 ? 76 ARG B C 1 ATOM 3389 O O . ARG B 2 76 ? -35.342 9.819 17.807 1.00 80.80 ? 76 ARG B O 1 ATOM 3390 C CB . ARG B 2 76 ? -36.127 12.812 16.447 1.00 113.28 ? 76 ARG B CB 1 ATOM 3391 C CG . ARG B 2 76 ? -37.534 13.373 16.269 1.00 120.75 ? 76 ARG B CG 1 ATOM 3392 C CD . ARG B 2 76 ? -37.604 14.893 16.350 1.00 124.53 ? 76 ARG B CD 1 ATOM 3393 N NE . ARG B 2 76 ? -38.081 15.480 15.098 1.00 126.02 ? 76 ARG B NE 1 ATOM 3394 C CZ . ARG B 2 76 ? -39.326 15.376 14.639 1.00 123.92 ? 76 ARG B CZ 1 ATOM 3395 N NH1 . ARG B 2 76 ? -40.241 14.698 15.320 1.00 122.65 ? 76 ARG B NH1 1 ATOM 3396 N NH2 . ARG B 2 76 ? -39.657 15.947 13.488 1.00 120.19 ? 76 ARG B NH2 1 ATOM 3397 N N . LEU B 2 77 ? -33.718 10.982 16.758 1.00 80.71 ? 77 LEU B N 1 ATOM 3398 C CA . LEU B 2 77 ? -32.649 10.593 17.664 1.00 75.19 ? 77 LEU B CA 1 ATOM 3399 C C . LEU B 2 77 ? -32.106 11.849 18.327 1.00 88.87 ? 77 LEU B C 1 ATOM 3400 O O . LEU B 2 77 ? -31.853 12.854 17.663 1.00 89.19 ? 77 LEU B O 1 ATOM 3401 C CB . LEU B 2 77 ? -31.541 9.845 16.926 1.00 60.60 ? 77 LEU B CB 1 ATOM 3402 C CG . LEU B 2 77 ? -31.952 8.482 16.375 1.00 58.13 ? 77 LEU B CG 1 ATOM 3403 C CD1 . LEU B 2 77 ? -30.769 7.778 15.745 1.00 55.40 ? 77 LEU B CD1 1 ATOM 3404 C CD2 . LEU B 2 77 ? -32.561 7.630 17.480 1.00 61.36 ? 77 LEU B CD2 1 ATOM 3405 N N . TYR B 2 78 ? -31.935 11.794 19.641 1.00 100.10 ? 78 TYR B N 1 ATOM 3406 C CA . TYR B 2 78 ? -31.614 12.991 20.403 1.00 108.65 ? 78 TYR B CA 1 ATOM 3407 C C . TYR B 2 78 ? -30.120 13.056 20.699 1.00 106.14 ? 78 TYR B C 1 ATOM 3408 O O . TYR B 2 78 ? -29.451 12.026 20.720 1.00 103.33 ? 78 TYR B O 1 ATOM 3409 C CB . TYR B 2 78 ? -32.454 13.027 21.685 1.00 119.25 ? 78 TYR B CB 1 ATOM 3410 C CG . TYR B 2 78 ? -33.929 13.254 21.409 1.00 130.72 ? 78 TYR B CG 1 ATOM 3411 C CD1 . TYR B 2 78 ? -34.865 13.237 22.433 1.00 143.71 ? 78 TYR B CD1 1 ATOM 3412 C CD2 . TYR B 2 78 ? -34.381 13.488 20.114 1.00 132.01 ? 78 TYR B CD2 1 ATOM 3413 C CE1 . TYR B 2 78 ? -36.211 13.448 22.172 1.00 149.49 ? 78 TYR B CE1 1 ATOM 3414 C CE2 . TYR B 2 78 ? -35.714 13.693 19.844 1.00 140.32 ? 78 TYR B CE2 1 ATOM 3415 C CZ . TYR B 2 78 ? -36.626 13.675 20.873 1.00 149.73 ? 78 TYR B CZ 1 ATOM 3416 O OH . TYR B 2 78 ? -37.954 13.885 20.588 1.00 155.72 ? 78 TYR B OH 1 ATOM 3417 N N . PRO B 2 79 ? -29.583 14.274 20.892 1.00 117.36 ? 79 PRO B N 1 ATOM 3418 C CA . PRO B 2 79 ? -28.138 14.415 21.098 1.00 117.43 ? 79 PRO B CA 1 ATOM 3419 C C . PRO B 2 79 ? -27.647 13.613 22.293 1.00 120.61 ? 79 PRO B C 1 ATOM 3420 O O . PRO B 2 79 ? -28.219 13.717 23.380 1.00 126.29 ? 79 PRO B O 1 ATOM 3421 C CB . PRO B 2 79 ? -27.958 15.918 21.335 1.00 124.36 ? 79 PRO B CB 1 ATOM 3422 C CG . PRO B 2 79 ? -29.311 16.412 21.738 1.00 129.41 ? 79 PRO B CG 1 ATOM 3423 C CD . PRO B 2 79 ? -30.273 15.574 20.966 1.00 127.49 ? 79 PRO B CD 1 ATOM 3424 N N . ASN B 2 80 ? -26.617 12.803 22.069 1.00 108.84 ? 80 ASN B N 1 ATOM 3425 C CA . ASN B 2 80 ? -26.019 11.972 23.108 1.00 105.82 ? 80 ASN B CA 1 ATOM 3426 C C . ASN B 2 80 ? -26.992 10.928 23.665 1.00 99.77 ? 80 ASN B C 1 ATOM 3427 O O . ASN B 2 80 ? -26.858 10.484 24.806 1.00 97.64 ? 80 ASN B O 1 ATOM 3428 C CB . ASN B 2 80 ? -25.477 12.855 24.237 1.00 111.98 ? 80 ASN B CB 1 ATOM 3429 C CG . ASN B 2 80 ? -24.359 12.191 25.013 1.00 115.33 ? 80 ASN B CG 1 ATOM 3430 O OD1 . ASN B 2 80 ? -23.241 12.703 25.079 1.00 116.83 ? 80 ASN B OD1 1 ATOM 3431 N ND2 . ASN B 2 80 ? -24.658 11.047 25.610 1.00 114.68 ? 80 ASN B ND2 1 ATOM 3432 N N . GLU B 2 81 ? -27.968 10.536 22.850 1.00 94.20 ? 81 GLU B N 1 ATOM 3433 C CA . GLU B 2 81 ? -28.917 9.485 23.215 1.00 86.11 ? 81 GLU B CA 1 ATOM 3434 C C . GLU B 2 81 ? -28.198 8.156 23.427 1.00 82.85 ? 81 GLU B C 1 ATOM 3435 O O . GLU B 2 81 ? -28.530 7.392 24.332 1.00 85.33 ? 81 GLU B O 1 ATOM 3436 C CB . GLU B 2 81 ? -29.991 9.349 22.134 1.00 86.40 ? 81 GLU B CB 1 ATOM 3437 C CG . GLU B 2 81 ? -30.967 8.201 22.313 1.00 87.98 ? 81 GLU B CG 1 ATOM 3438 C CD . GLU B 2 81 ? -32.126 8.286 21.335 1.00 85.89 ? 81 GLU B CD 1 ATOM 3439 O OE1 . GLU B 2 81 ? -32.299 9.352 20.705 1.00 94.33 ? 81 GLU B OE1 1 ATOM 3440 O OE2 . GLU B 2 81 ? -32.869 7.295 21.192 1.00 80.04 ? 81 GLU B OE2 1 ATOM 3441 N N . PHE B 2 82 ? -27.206 7.896 22.582 1.00 85.81 ? 82 PHE B N 1 ATOM 3442 C CA . PHE B 2 82 ? -26.355 6.719 22.713 1.00 87.33 ? 82 PHE B CA 1 ATOM 3443 C C . PHE B 2 82 ? -25.045 7.117 23.366 1.00 92.27 ? 82 PHE B C 1 ATOM 3444 O O . PHE B 2 82 ? -24.312 7.951 22.832 1.00 94.93 ? 82 PHE B O 1 ATOM 3445 C CB . PHE B 2 82 ? -26.083 6.082 21.351 1.00 83.69 ? 82 PHE B CB 1 ATOM 3446 C CG . PHE B 2 82 ? -27.301 5.515 20.686 1.00 86.87 ? 82 PHE B CG 1 ATOM 3447 C CD1 . PHE B 2 82 ? -27.529 4.151 20.680 1.00 90.51 ? 82 PHE B CD1 1 ATOM 3448 C CD2 . PHE B 2 82 ? -28.217 6.344 20.058 1.00 88.88 ? 82 PHE B CD2 1 ATOM 3449 C CE1 . PHE B 2 82 ? -28.645 3.623 20.065 1.00 87.57 ? 82 PHE B CE1 1 ATOM 3450 C CE2 . PHE B 2 82 ? -29.336 5.822 19.443 1.00 85.82 ? 82 PHE B CE2 1 ATOM 3451 C CZ . PHE B 2 82 ? -29.550 4.460 19.445 1.00 82.60 ? 82 PHE B CZ 1 ATOM 3452 N N . VAL B 2 83 ? -24.741 6.527 24.515 1.00 92.86 ? 83 VAL B N 1 ATOM 3453 C CA . VAL B 2 83 ? -23.547 6.927 25.244 1.00 87.34 ? 83 VAL B CA 1 ATOM 3454 C C . VAL B 2 83 ? -22.904 5.746 25.958 1.00 93.26 ? 83 VAL B C 1 ATOM 3455 O O . VAL B 2 83 ? -21.692 5.715 26.163 1.00 90.79 ? 83 VAL B O 1 ATOM 3456 C CB . VAL B 2 83 ? -23.870 8.044 26.267 1.00 77.45 ? 83 VAL B CB 1 ATOM 3457 C CG1 . VAL B 2 83 ? -24.723 7.517 27.411 1.00 83.89 ? 83 VAL B CG1 1 ATOM 3458 C CG2 . VAL B 2 83 ? -22.594 8.683 26.791 1.00 73.89 ? 83 VAL B CG2 1 ATOM 3459 N N . ASN B 2 84 ? -23.715 4.755 26.307 1.00 98.43 ? 84 ASN B N 1 ATOM 3460 C CA . ASN B 2 84 ? -23.238 3.644 27.119 1.00 104.34 ? 84 ASN B CA 1 ATOM 3461 C C . ASN B 2 84 ? -22.998 2.397 26.303 1.00 97.39 ? 84 ASN B C 1 ATOM 3462 O O . ASN B 2 84 ? -22.895 1.292 26.834 1.00 97.30 ? 84 ASN B O 1 ATOM 3463 C CB . ASN B 2 84 ? -24.228 3.361 28.232 1.00 115.48 ? 84 ASN B CB 1 ATOM 3464 C CG . ASN B 2 84 ? -24.260 4.467 29.244 1.00 121.78 ? 84 ASN B CG 1 ATOM 3465 O OD1 . ASN B 2 84 ? -23.213 4.994 29.629 1.00 117.25 ? 84 ASN B OD1 1 ATOM 3466 N ND2 . ASN B 2 84 ? -25.453 4.847 29.675 1.00 129.64 ? 84 ASN B ND2 1 ATOM 3467 N N . TYR B 2 85 ? -22.907 2.589 24.998 1.00 95.57 ? 85 TYR B N 1 ATOM 3468 C CA . TYR B 2 85 ? -22.650 1.501 24.084 1.00 91.82 ? 85 TYR B CA 1 ATOM 3469 C C . TYR B 2 85 ? -21.238 1.614 23.566 1.00 96.28 ? 85 TYR B C 1 ATOM 3470 O O . TYR B 2 85 ? -21.007 1.601 22.359 1.00 93.13 ? 85 TYR B O 1 ATOM 3471 C CB . TYR B 2 85 ? -23.656 1.532 22.950 1.00 86.90 ? 85 TYR B CB 1 ATOM 3472 C CG . TYR B 2 85 ? -25.067 1.692 23.460 1.00 87.79 ? 85 TYR B CG 1 ATOM 3473 C CD1 . TYR B 2 85 ? -25.873 0.584 23.669 1.00 86.20 ? 85 TYR B CD1 1 ATOM 3474 C CD2 . TYR B 2 85 ? -25.590 2.949 23.755 1.00 91.31 ? 85 TYR B CD2 1 ATOM 3475 C CE1 . TYR B 2 85 ? -27.164 0.720 24.140 1.00 88.71 ? 85 TYR B CE1 1 ATOM 3476 C CE2 . TYR B 2 85 ? -26.879 3.091 24.234 1.00 94.83 ? 85 TYR B CE2 1 ATOM 3477 C CZ . TYR B 2 85 ? -27.658 1.973 24.423 1.00 95.16 ? 85 TYR B CZ 1 ATOM 3478 O OH . TYR B 2 85 ? -28.937 2.104 24.902 1.00 101.38 ? 85 TYR B OH 1 ATOM 3479 N N . SER B 2 86 ? -20.306 1.751 24.503 1.00 111.08 ? 86 SER B N 1 ATOM 3480 C CA . SER B 2 86 ? -18.887 1.834 24.200 1.00 112.63 ? 86 SER B CA 1 ATOM 3481 C C . SER B 2 86 ? -18.481 0.752 23.214 1.00 112.10 ? 86 SER B C 1 ATOM 3482 O O . SER B 2 86 ? -17.876 1.029 22.179 1.00 116.92 ? 86 SER B O 1 ATOM 3483 C CB . SER B 2 86 ? -18.064 1.701 25.483 1.00 118.20 ? 86 SER B CB 1 ATOM 3484 O OG . SER B 2 86 ? -18.614 2.474 26.536 1.00 121.53 ? 86 SER B OG 1 ATOM 3485 N N . ASN B 2 87 ? -18.841 -0.482 23.543 1.00 111.47 ? 87 ASN B N 1 ATOM 3486 C CA . ASN B 2 87 ? -18.466 -1.629 22.734 1.00 106.80 ? 87 ASN B CA 1 ATOM 3487 C C . ASN B 2 87 ? -19.654 -2.289 22.044 1.00 100.10 ? 87 ASN B C 1 ATOM 3488 O O . ASN B 2 87 ? -20.154 -3.320 22.489 1.00 98.74 ? 87 ASN B O 1 ATOM 3489 C CB . ASN B 2 87 ? -17.728 -2.648 23.598 1.00 102.39 ? 87 ASN B CB 1 ATOM 3490 C CG . ASN B 2 87 ? -18.413 -2.884 24.925 1.00 95.17 ? 87 ASN B CG 1 ATOM 3491 O OD1 . ASN B 2 87 ? -19.343 -2.164 25.295 1.00 93.55 ? 87 ASN B OD1 1 ATOM 3492 N ND2 . ASN B 2 87 ? -17.951 -3.887 25.655 1.00 94.85 ? 87 ASN B ND2 1 ATOM 3493 N N . ALA B 2 88 ? -20.103 -1.683 20.952 1.00 94.05 ? 88 ALA B N 1 ATOM 3494 C CA . ALA B 2 88 ? -21.114 -2.294 20.101 1.00 82.66 ? 88 ALA B CA 1 ATOM 3495 C C . ALA B 2 88 ? -20.565 -2.396 18.685 1.00 91.86 ? 88 ALA B C 1 ATOM 3496 O O . ALA B 2 88 ? -20.185 -1.390 18.092 1.00 97.41 ? 88 ALA B O 1 ATOM 3497 C CB . ALA B 2 88 ? -22.398 -1.491 20.129 1.00 67.01 ? 88 ALA B CB 1 ATOM 3498 N N . VAL B 2 89 ? -20.506 -3.609 18.148 1.00 87.34 ? 89 VAL B N 1 ATOM 3499 C CA . VAL B 2 89 ? -19.916 -3.808 16.830 1.00 82.86 ? 89 VAL B CA 1 ATOM 3500 C C . VAL B 2 89 ? -20.854 -3.364 15.714 1.00 79.13 ? 89 VAL B C 1 ATOM 3501 O O . VAL B 2 89 ? -20.463 -2.601 14.830 1.00 79.71 ? 89 VAL B O 1 ATOM 3502 C CB . VAL B 2 89 ? -19.527 -5.276 16.596 1.00 85.00 ? 89 VAL B CB 1 ATOM 3503 C CG1 . VAL B 2 89 ? -19.071 -5.477 15.158 1.00 95.63 ? 89 VAL B CG1 1 ATOM 3504 C CG2 . VAL B 2 89 ? -18.430 -5.679 17.549 1.00 80.59 ? 89 VAL B CG2 1 ATOM 3505 N N . THR B 2 90 ? -22.091 -3.849 15.748 1.00 75.10 ? 90 THR B N 1 ATOM 3506 C CA . THR B 2 90 ? -23.074 -3.474 14.738 1.00 72.13 ? 90 THR B CA 1 ATOM 3507 C C . THR B 2 90 ? -24.380 -2.981 15.360 1.00 70.61 ? 90 THR B C 1 ATOM 3508 O O . THR B 2 90 ? -24.783 -3.427 16.435 1.00 71.35 ? 90 THR B O 1 ATOM 3509 C CB . THR B 2 90 ? -23.395 -4.649 13.784 1.00 74.79 ? 90 THR B CB 1 ATOM 3510 O OG1 . THR B 2 90 ? -24.199 -5.620 14.462 1.00 74.08 ? 90 THR B OG1 1 ATOM 3511 C CG2 . THR B 2 90 ? -22.122 -5.310 13.286 1.00 80.66 ? 90 THR B CG2 1 ATOM 3512 N N . LEU B 2 91 ? -25.038 -2.060 14.665 1.00 68.26 ? 91 LEU B N 1 ATOM 3513 C CA . LEU B 2 91 ? -26.320 -1.521 15.103 1.00 66.50 ? 91 LEU B CA 1 ATOM 3514 C C . LEU B 2 91 ? -27.277 -1.347 13.924 1.00 72.37 ? 91 LEU B C 1 ATOM 3515 O O . LEU B 2 91 ? -26.948 -0.684 12.941 1.00 76.54 ? 91 LEU B O 1 ATOM 3516 C CB . LEU B 2 91 ? -26.118 -0.184 15.820 1.00 61.19 ? 91 LEU B CB 1 ATOM 3517 C CG . LEU B 2 91 ? -27.350 0.709 16.010 1.00 58.04 ? 91 LEU B CG 1 ATOM 3518 C CD1 . LEU B 2 91 ? -28.369 0.045 16.918 1.00 64.21 ? 91 LEU B CD1 1 ATOM 3519 C CD2 . LEU B 2 91 ? -26.956 2.073 16.555 1.00 57.61 ? 91 LEU B CD2 1 ATOM 3520 N N . HIS B 2 92 ? -28.460 -1.946 14.032 1.00 74.71 ? 92 HIS B N 1 ATOM 3521 C CA . HIS B 2 92 ? -29.492 -1.848 13.001 1.00 74.11 ? 92 HIS B CA 1 ATOM 3522 C C . HIS B 2 92 ? -30.605 -0.881 13.400 1.00 74.89 ? 92 HIS B C 1 ATOM 3523 O O . HIS B 2 92 ? -31.195 -1.019 14.470 1.00 77.23 ? 92 HIS B O 1 ATOM 3524 C CB . HIS B 2 92 ? -30.096 -3.225 12.720 1.00 81.67 ? 92 HIS B CB 1 ATOM 3525 C CG . HIS B 2 92 ? -29.306 -4.053 11.756 1.00 87.64 ? 92 HIS B CG 1 ATOM 3526 N ND1 . HIS B 2 92 ? -29.739 -4.310 10.473 1.00 94.85 ? 92 HIS B ND1 1 ATOM 3527 C CD2 . HIS B 2 92 ? -28.117 -4.687 11.887 1.00 90.47 ? 92 HIS B CD2 1 ATOM 3528 C CE1 . HIS B 2 92 ? -28.849 -5.065 9.854 1.00 97.83 ? 92 HIS B CE1 1 ATOM 3529 N NE2 . HIS B 2 92 ? -27.855 -5.309 10.690 1.00 95.61 ? 92 HIS B NE2 1 ATOM 3530 N N . LEU B 2 93 ? -30.899 0.086 12.534 1.00 74.21 ? 93 LEU B N 1 ATOM 3531 C CA . LEU B 2 93 ? -31.964 1.055 12.794 1.00 72.74 ? 93 LEU B CA 1 ATOM 3532 C C . LEU B 2 93 ? -32.952 1.171 11.631 1.00 75.63 ? 93 LEU B C 1 ATOM 3533 O O . LEU B 2 93 ? -33.440 2.261 11.330 1.00 74.41 ? 93 LEU B O 1 ATOM 3534 C CB . LEU B 2 93 ? -31.376 2.437 13.094 1.00 67.69 ? 93 LEU B CB 1 ATOM 3535 C CG . LEU B 2 93 ? -30.510 2.599 14.343 1.00 61.42 ? 93 LEU B CG 1 ATOM 3536 C CD1 . LEU B 2 93 ? -30.149 4.064 14.553 1.00 63.15 ? 93 LEU B CD1 1 ATOM 3537 C CD2 . LEU B 2 93 ? -31.222 2.042 15.559 1.00 58.58 ? 93 LEU B CD2 1 ATOM 3538 N N . GLY B 2 94 ? -33.255 0.049 10.988 1.00 76.69 ? 94 GLY B N 1 ATOM 3539 C CA . GLY B 2 94 ? -34.151 0.055 9.846 1.00 76.39 ? 94 GLY B CA 1 ATOM 3540 C C . GLY B 2 94 ? -35.619 0.056 10.225 1.00 79.93 ? 94 GLY B C 1 ATOM 3541 O O . GLY B 2 94 ? -35.987 -0.421 11.297 1.00 88.85 ? 94 GLY B O 1 ATOM 3542 N N . ASN B 2 95 ? -36.453 0.599 9.341 1.00 71.60 ? 95 ASN B N 1 ATOM 3543 C CA . ASN B 2 95 ? -37.906 0.597 9.516 1.00 81.94 ? 95 ASN B CA 1 ATOM 3544 C C . ASN B 2 95 ? -38.328 1.285 10.808 1.00 81.22 ? 95 ASN B C 1 ATOM 3545 O O . ASN B 2 95 ? -39.244 0.837 11.496 1.00 76.52 ? 95 ASN B O 1 ATOM 3546 C CB . ASN B 2 95 ? -38.444 -0.836 9.482 1.00 94.81 ? 95 ASN B CB 1 ATOM 3547 C CG . ASN B 2 95 ? -38.029 -1.584 8.228 1.00 107.13 ? 95 ASN B CG 1 ATOM 3548 O OD1 . ASN B 2 95 ? -38.776 -1.648 7.251 1.00 111.08 ? 95 ASN B OD1 1 ATOM 3549 N ND2 . ASN B 2 95 ? -36.828 -2.150 8.247 1.00 109.37 ? 95 ASN B ND2 1 ATOM 3550 N N . ASN B 2 96 ? -37.644 2.379 11.126 1.00 86.18 ? 96 ASN B N 1 ATOM 3551 C CA . ASN B 2 96 ? -37.874 3.113 12.365 1.00 83.74 ? 96 ASN B CA 1 ATOM 3552 C C . ASN B 2 96 ? -38.596 4.427 12.123 1.00 81.38 ? 96 ASN B C 1 ATOM 3553 O O . ASN B 2 96 ? -38.982 5.115 13.068 1.00 86.07 ? 96 ASN B O 1 ATOM 3554 C CB . ASN B 2 96 ? -36.548 3.386 13.076 1.00 89.71 ? 96 ASN B CB 1 ATOM 3555 C CG . ASN B 2 96 ? -36.054 2.197 13.866 1.00 96.04 ? 96 ASN B CG 1 ATOM 3556 O OD1 . ASN B 2 96 ? -34.896 1.805 13.764 1.00 99.52 ? 96 ASN B OD1 1 ATOM 3557 N ND2 . ASN B 2 96 ? -36.932 1.619 14.662 1.00 95.99 ? 96 ASN B ND2 1 ATOM 3558 N N . GLY B 2 97 ? -38.767 4.774 10.853 1.00 80.90 ? 97 GLY B N 1 ATOM 3559 C CA . GLY B 2 97 ? -39.364 6.042 10.486 1.00 81.21 ? 97 GLY B CA 1 ATOM 3560 C C . GLY B 2 97 ? -38.548 7.220 10.982 1.00 79.24 ? 97 GLY B C 1 ATOM 3561 O O . GLY B 2 97 ? -39.104 8.269 11.304 1.00 84.45 ? 97 GLY B O 1 ATOM 3562 N N . LEU B 2 98 ? -37.231 7.041 11.056 1.00 66.63 ? 98 LEU B N 1 ATOM 3563 C CA . LEU B 2 98 ? -36.335 8.106 11.496 1.00 70.38 ? 98 LEU B CA 1 ATOM 3564 C C . LEU B 2 98 ? -36.523 9.347 10.637 1.00 77.90 ? 98 LEU B C 1 ATOM 3565 O O . LEU B 2 98 ? -36.671 9.248 9.424 1.00 80.18 ? 98 LEU B O 1 ATOM 3566 C CB . LEU B 2 98 ? -34.875 7.653 11.444 1.00 66.57 ? 98 LEU B CB 1 ATOM 3567 C CG . LEU B 2 98 ? -34.176 7.435 12.786 1.00 70.78 ? 98 LEU B CG 1 ATOM 3568 C CD1 . LEU B 2 98 ? -32.702 7.804 12.683 1.00 65.21 ? 98 LEU B CD1 1 ATOM 3569 C CD2 . LEU B 2 98 ? -34.858 8.221 13.899 1.00 79.47 ? 98 LEU B CD2 1 ATOM 3570 N N . GLN B 2 99 ? -36.528 10.515 11.266 1.00 82.25 ? 99 GLN B N 1 ATOM 3571 C CA . GLN B 2 99 ? -36.752 11.751 10.534 1.00 83.35 ? 99 GLN B CA 1 ATOM 3572 C C . GLN B 2 99 ? -35.541 12.661 10.619 1.00 85.65 ? 99 GLN B C 1 ATOM 3573 O O . GLN B 2 99 ? -35.176 13.313 9.639 1.00 93.00 ? 99 GLN B O 1 ATOM 3574 C CB . GLN B 2 99 ? -37.994 12.470 11.059 1.00 85.65 ? 99 GLN B CB 1 ATOM 3575 C CG . GLN B 2 99 ? -39.284 11.706 10.816 1.00 89.52 ? 99 GLN B CG 1 ATOM 3576 C CD . GLN B 2 99 ? -40.517 12.531 11.119 1.00 101.11 ? 99 GLN B CD 1 ATOM 3577 O OE1 . GLN B 2 99 ? -40.508 13.381 12.011 1.00 109.43 ? 99 GLN B OE1 1 ATOM 3578 N NE2 . GLN B 2 99 ? -41.588 12.288 10.371 1.00 102.59 ? 99 GLN B NE2 1 ATOM 3579 N N . GLU B 2 100 ? -34.916 12.706 11.790 1.00 82.63 ? 100 GLU B N 1 ATOM 3580 C CA . GLU B 2 100 ? -33.714 13.508 11.949 1.00 87.35 ? 100 GLU B CA 1 ATOM 3581 C C . GLU B 2 100 ? -32.738 12.892 12.938 1.00 83.89 ? 100 GLU B C 1 ATOM 3582 O O . GLU B 2 100 ? -33.106 12.068 13.776 1.00 79.98 ? 100 GLU B O 1 ATOM 3583 C CB . GLU B 2 100 ? -34.064 14.935 12.390 1.00 92.73 ? 100 GLU B CB 1 ATOM 3584 C CG . GLU B 2 100 ? -34.410 15.083 13.863 1.00 97.95 ? 100 GLU B CG 1 ATOM 3585 C CD . GLU B 2 100 ? -34.457 16.536 14.302 1.00 107.89 ? 100 GLU B CD 1 ATOM 3586 O OE1 . GLU B 2 100 ? -33.503 17.281 13.993 1.00 108.94 ? 100 GLU B OE1 1 ATOM 3587 O OE2 . GLU B 2 100 ? -35.449 16.933 14.948 1.00 113.65 ? 100 GLU B OE2 1 ATOM 3588 N N . ILE B 2 101 ? -31.482 13.296 12.808 1.00 83.48 ? 101 ILE B N 1 ATOM 3589 C CA . ILE B 2 101 ? -30.454 12.987 13.783 1.00 79.75 ? 101 ILE B CA 1 ATOM 3590 C C . ILE B 2 101 ? -29.902 14.305 14.286 1.00 86.39 ? 101 ILE B C 1 ATOM 3591 O O . ILE B 2 101 ? -29.108 14.951 13.600 1.00 96.81 ? 101 ILE B O 1 ATOM 3592 C CB . ILE B 2 101 ? -29.319 12.136 13.191 1.00 75.52 ? 101 ILE B CB 1 ATOM 3593 C CG1 . ILE B 2 101 ? -29.849 10.787 12.712 1.00 74.25 ? 101 ILE B CG1 1 ATOM 3594 C CG2 . ILE B 2 101 ? -28.217 11.932 14.207 1.00 73.63 ? 101 ILE B CG2 1 ATOM 3595 C CD1 . ILE B 2 101 ? -30.048 10.713 11.220 1.00 76.95 ? 101 ILE B CD1 1 ATOM 3596 N N . ARG B 2 102 ? -30.350 14.716 15.466 1.00 90.22 ? 102 ARG B N 1 ATOM 3597 C CA . ARG B 2 102 ? -29.883 15.957 16.062 1.00 102.00 ? 102 ARG B CA 1 ATOM 3598 C C . ARG B 2 102 ? -28.367 15.886 16.248 1.00 97.35 ? 102 ARG B C 1 ATOM 3599 O O . ARG B 2 102 ? -27.829 14.809 16.509 1.00 95.47 ? 102 ARG B O 1 ATOM 3600 C CB . ARG B 2 102 ? -30.609 16.214 17.385 1.00 115.93 ? 102 ARG B CB 1 ATOM 3601 C CG . ARG B 2 102 ? -32.121 16.292 17.219 1.00 124.27 ? 102 ARG B CG 1 ATOM 3602 C CD . ARG B 2 102 ? -32.802 16.971 18.395 1.00 135.07 ? 102 ARG B CD 1 ATOM 3603 N NE . ARG B 2 102 ? -34.195 17.284 18.088 1.00 143.48 ? 102 ARG B NE 1 ATOM 3604 C CZ . ARG B 2 102 ? -34.594 18.408 17.501 1.00 153.11 ? 102 ARG B CZ 1 ATOM 3605 N NH1 . ARG B 2 102 ? -33.708 19.334 17.161 1.00 156.04 ? 102 ARG B NH1 1 ATOM 3606 N NH2 . ARG B 2 102 ? -35.882 18.609 17.257 1.00 157.49 ? 102 ARG B NH2 1 ATOM 3607 N N . PRO B 2 103 ? -27.678 17.031 16.081 1.00 104.16 ? 103 PRO B N 1 ATOM 3608 C CA . PRO B 2 103 ? -26.214 17.118 16.043 1.00 108.88 ? 103 PRO B CA 1 ATOM 3609 C C . PRO B 2 103 ? -25.503 16.237 17.067 1.00 106.25 ? 103 PRO B C 1 ATOM 3610 O O . PRO B 2 103 ? -25.684 16.408 18.272 1.00 105.01 ? 103 PRO B O 1 ATOM 3611 C CB . PRO B 2 103 ? -25.957 18.595 16.333 1.00 120.84 ? 103 PRO B CB 1 ATOM 3612 C CG . PRO B 2 103 ? -27.130 19.279 15.730 1.00 122.76 ? 103 PRO B CG 1 ATOM 3613 C CD . PRO B 2 103 ? -28.302 18.362 15.945 1.00 116.42 ? 103 PRO B CD 1 ATOM 3614 N N . GLY B 2 104 ? -24.714 15.290 16.571 1.00 109.29 ? 104 GLY B N 1 ATOM 3615 C CA . GLY B 2 104 ? -23.914 14.425 17.416 1.00 111.31 ? 104 GLY B CA 1 ATOM 3616 C C . GLY B 2 104 ? -24.722 13.498 18.301 1.00 113.57 ? 104 GLY B C 1 ATOM 3617 O O . GLY B 2 104 ? -24.536 13.476 19.518 1.00 122.62 ? 104 GLY B O 1 ATOM 3618 N N . ALA B 2 105 ? -25.612 12.721 17.694 1.00 105.08 ? 105 ALA B N 1 ATOM 3619 C CA . ALA B 2 105 ? -26.444 11.798 18.455 1.00 103.57 ? 105 ALA B CA 1 ATOM 3620 C C . ALA B 2 105 ? -25.645 10.583 18.917 1.00 92.32 ? 105 ALA B C 1 ATOM 3621 O O . ALA B 2 105 ? -25.699 10.201 20.085 1.00 80.50 ? 105 ALA B O 1 ATOM 3622 C CB . ALA B 2 105 ? -27.642 11.363 17.634 1.00 103.42 ? 105 ALA B CB 1 ATOM 3623 N N . PHE B 2 106 ? -24.900 9.981 17.997 1.00 91.69 ? 106 PHE B N 1 ATOM 3624 C CA . PHE B 2 106 ? -24.098 8.803 18.311 1.00 94.79 ? 106 PHE B CA 1 ATOM 3625 C C . PHE B 2 106 ? -22.854 9.164 19.112 1.00 97.34 ? 106 PHE B C 1 ATOM 3626 O O . PHE B 2 106 ? -21.745 8.812 18.722 1.00 100.16 ? 106 PHE B O 1 ATOM 3627 C CB . PHE B 2 106 ? -23.670 8.083 17.032 1.00 96.74 ? 106 PHE B CB 1 ATOM 3628 C CG . PHE B 2 106 ? -24.749 7.976 15.998 1.00 101.68 ? 106 PHE B CG 1 ATOM 3629 C CD1 . PHE B 2 106 ? -25.638 6.916 16.013 1.00 102.80 ? 106 PHE B CD1 1 ATOM 3630 C CD2 . PHE B 2 106 ? -24.866 8.927 15.000 1.00 105.11 ? 106 PHE B CD2 1 ATOM 3631 C CE1 . PHE B 2 106 ? -26.628 6.810 15.058 1.00 103.20 ? 106 PHE B CE1 1 ATOM 3632 C CE2 . PHE B 2 106 ? -25.855 8.827 14.042 1.00 103.34 ? 106 PHE B CE2 1 ATOM 3633 C CZ . PHE B 2 106 ? -26.737 7.766 14.071 1.00 99.76 ? 106 PHE B CZ 1 ATOM 3634 N N . SER B 2 107 ? -23.035 9.857 20.230 1.00 96.19 ? 107 SER B N 1 ATOM 3635 C CA . SER B 2 107 ? -21.901 10.391 20.976 1.00 100.96 ? 107 SER B CA 1 ATOM 3636 C C . SER B 2 107 ? -20.997 9.309 21.565 1.00 99.52 ? 107 SER B C 1 ATOM 3637 O O . SER B 2 107 ? -19.773 9.434 21.533 1.00 104.70 ? 107 SER B O 1 ATOM 3638 C CB . SER B 2 107 ? -22.396 11.316 22.090 1.00 111.07 ? 107 SER B CB 1 ATOM 3639 O OG . SER B 2 107 ? -22.854 12.548 21.558 1.00 110.85 ? 107 SER B OG 1 ATOM 3640 N N . GLY B 2 108 ? -21.594 8.243 22.087 1.00 99.11 ? 108 GLY B N 1 ATOM 3641 C CA . GLY B 2 108 ? -20.840 7.244 22.823 1.00 106.85 ? 108 GLY B CA 1 ATOM 3642 C C . GLY B 2 108 ? -20.404 6.001 22.066 1.00 108.95 ? 108 GLY B C 1 ATOM 3643 O O . GLY B 2 108 ? -19.622 5.207 22.589 1.00 112.65 ? 108 GLY B O 1 ATOM 3644 N N . LEU B 2 109 ? -20.898 5.825 20.842 1.00 105.10 ? 109 LEU B N 1 ATOM 3645 C CA . LEU B 2 109 ? -20.585 4.635 20.047 1.00 96.93 ? 109 LEU B CA 1 ATOM 3646 C C . LEU B 2 109 ? -19.119 4.606 19.622 1.00 99.89 ? 109 LEU B C 1 ATOM 3647 O O . LEU B 2 109 ? -18.801 4.746 18.442 1.00 98.57 ? 109 LEU B O 1 ATOM 3648 C CB . LEU B 2 109 ? -21.483 4.565 18.811 1.00 88.27 ? 109 LEU B CB 1 ATOM 3649 C CG . LEU B 2 109 ? -22.990 4.600 19.065 1.00 87.18 ? 109 LEU B CG 1 ATOM 3650 C CD1 . LEU B 2 109 ? -23.765 4.501 17.762 1.00 79.92 ? 109 LEU B CD1 1 ATOM 3651 C CD2 . LEU B 2 109 ? -23.393 3.485 20.011 1.00 90.59 ? 109 LEU B CD2 1 ATOM 3652 N N . LYS B 2 110 ? -18.234 4.409 20.593 1.00 103.28 ? 110 LYS B N 1 ATOM 3653 C CA . LYS B 2 110 ? -16.797 4.495 20.363 1.00 100.53 ? 110 LYS B CA 1 ATOM 3654 C C . LYS B 2 110 ? -16.297 3.455 19.368 1.00 93.66 ? 110 LYS B C 1 ATOM 3655 O O . LYS B 2 110 ? -15.555 3.776 18.440 1.00 93.51 ? 110 LYS B O 1 ATOM 3656 C CB . LYS B 2 110 ? -16.046 4.348 21.692 1.00 108.41 ? 110 LYS B CB 1 ATOM 3657 C CG . LYS B 2 110 ? -15.318 5.610 22.140 1.00 117.50 ? 110 LYS B CG 1 ATOM 3658 C CD . LYS B 2 110 ? -16.236 6.823 22.097 1.00 122.98 ? 110 LYS B CD 1 ATOM 3659 C CE . LYS B 2 110 ? -15.440 8.117 21.976 1.00 127.54 ? 110 LYS B CE 1 ATOM 3660 N NZ . LYS B 2 110 ? -16.304 9.276 21.607 1.00 126.83 ? 110 LYS B NZ 1 ATOM 3661 N N . THR B 2 111 ? -16.718 2.211 19.556 1.00 84.87 ? 111 THR B N 1 ATOM 3662 C CA . THR B 2 111 ? -16.159 1.102 18.798 1.00 85.37 ? 111 THR B CA 1 ATOM 3663 C C . THR B 2 111 ? -17.137 0.513 17.789 1.00 88.80 ? 111 THR B C 1 ATOM 3664 O O . THR B 2 111 ? -17.083 -0.681 17.499 1.00 92.86 ? 111 THR B O 1 ATOM 3665 C CB . THR B 2 111 ? -15.698 -0.026 19.733 1.00 90.66 ? 111 THR B CB 1 ATOM 3666 O OG1 . THR B 2 111 ? -16.838 -0.766 20.187 1.00 84.58 ? 111 THR B OG1 1 ATOM 3667 C CG2 . THR B 2 111 ? -14.947 0.545 20.933 1.00 98.27 ? 111 THR B CG2 1 ATOM 3668 N N . LEU B 2 112 ? -18.029 1.340 17.254 1.00 86.48 ? 112 LEU B N 1 ATOM 3669 C CA . LEU B 2 112 ? -18.993 0.862 16.268 1.00 72.05 ? 112 LEU B CA 1 ATOM 3670 C C . LEU B 2 112 ? -18.340 0.714 14.902 1.00 72.28 ? 112 LEU B C 1 ATOM 3671 O O . LEU B 2 112 ? -17.574 1.576 14.473 1.00 81.02 ? 112 LEU B O 1 ATOM 3672 C CB . LEU B 2 112 ? -20.194 1.800 16.174 1.00 63.73 ? 112 LEU B CB 1 ATOM 3673 C CG . LEU B 2 112 ? -21.327 1.312 15.267 1.00 56.20 ? 112 LEU B CG 1 ATOM 3674 C CD1 . LEU B 2 112 ? -21.941 0.029 15.810 1.00 52.43 ? 112 LEU B CD1 1 ATOM 3675 C CD2 . LEU B 2 112 ? -22.390 2.383 15.090 1.00 56.39 ? 112 LEU B CD2 1 ATOM 3676 N N . LYS B 2 113 ? -18.651 -0.384 14.223 1.00 71.02 ? 113 LYS B N 1 ATOM 3677 C CA . LYS B 2 113 ? -18.041 -0.693 12.938 1.00 71.52 ? 113 LYS B CA 1 ATOM 3678 C C . LYS B 2 113 ? -19.072 -0.688 11.817 1.00 72.74 ? 113 LYS B C 1 ATOM 3679 O O . LYS B 2 113 ? -18.830 -0.143 10.741 1.00 76.00 ? 113 LYS B O 1 ATOM 3680 C CB . LYS B 2 113 ? -17.339 -2.052 12.997 1.00 76.65 ? 113 LYS B CB 1 ATOM 3681 C CG . LYS B 2 113 ? -16.265 -2.147 14.066 1.00 87.09 ? 113 LYS B CG 1 ATOM 3682 C CD . LYS B 2 113 ? -14.886 -1.832 13.513 1.00 97.14 ? 113 LYS B CD 1 ATOM 3683 C CE . LYS B 2 113 ? -13.975 -1.300 14.606 1.00 108.00 ? 113 LYS B CE 1 ATOM 3684 N NZ . LYS B 2 113 ? -14.179 -2.008 15.899 1.00 109.40 ? 113 LYS B NZ 1 ATOM 3685 N N . ARG B 2 114 ? -20.223 -1.298 12.076 1.00 68.88 ? 114 ARG B N 1 ATOM 3686 C CA . ARG B 2 114 ? -21.268 -1.421 11.068 1.00 58.69 ? 114 ARG B CA 1 ATOM 3687 C C . ARG B 2 114 ? -22.565 -0.756 11.512 1.00 63.76 ? 114 ARG B C 1 ATOM 3688 O O . ARG B 2 114 ? -23.039 -0.987 12.623 1.00 68.65 ? 114 ARG B O 1 ATOM 3689 C CB . ARG B 2 114 ? -21.516 -2.895 10.751 1.00 51.04 ? 114 ARG B CB 1 ATOM 3690 C CG . ARG B 2 114 ? -22.653 -3.152 9.784 1.00 49.24 ? 114 ARG B CG 1 ATOM 3691 C CD . ARG B 2 114 ? -22.726 -4.622 9.411 1.00 57.46 ? 114 ARG B CD 1 ATOM 3692 N NE . ARG B 2 114 ? -23.374 -4.827 8.119 1.00 62.77 ? 114 ARG B NE 1 ATOM 3693 C CZ . ARG B 2 114 ? -23.633 -6.020 7.593 1.00 67.96 ? 114 ARG B CZ 1 ATOM 3694 N NH1 . ARG B 2 114 ? -23.303 -7.124 8.250 1.00 75.20 ? 114 ARG B NH1 1 ATOM 3695 N NH2 . ARG B 2 114 ? -24.225 -6.110 6.410 1.00 62.56 ? 114 ARG B NH2 1 ATOM 3696 N N . LEU B 2 115 ? -23.139 0.065 10.639 1.00 68.89 ? 115 LEU B N 1 ATOM 3697 C CA . LEU B 2 115 ? -24.372 0.784 10.956 1.00 71.06 ? 115 LEU B CA 1 ATOM 3698 C C . LEU B 2 115 ? -25.374 0.760 9.802 1.00 69.34 ? 115 LEU B C 1 ATOM 3699 O O . LEU B 2 115 ? -25.010 0.960 8.642 1.00 70.00 ? 115 LEU B O 1 ATOM 3700 C CB . LEU B 2 115 ? -24.060 2.234 11.337 1.00 71.94 ? 115 LEU B CB 1 ATOM 3701 C CG . LEU B 2 115 ? -25.270 3.147 11.557 1.00 67.73 ? 115 LEU B CG 1 ATOM 3702 C CD1 . LEU B 2 115 ? -26.131 2.613 12.689 1.00 69.25 ? 115 LEU B CD1 1 ATOM 3703 C CD2 . LEU B 2 115 ? -24.843 4.583 11.828 1.00 67.06 ? 115 LEU B CD2 1 ATOM 3704 N N . HIS B 2 116 ? -26.637 0.508 10.135 1.00 67.44 ? 116 HIS B N 1 ATOM 3705 C CA . HIS B 2 116 ? -27.715 0.529 9.157 1.00 65.80 ? 116 HIS B CA 1 ATOM 3706 C C . HIS B 2 116 ? -28.722 1.623 9.500 1.00 64.43 ? 116 HIS B C 1 ATOM 3707 O O . HIS B 2 116 ? -29.028 1.859 10.667 1.00 59.78 ? 116 HIS B O 1 ATOM 3708 C CB . HIS B 2 116 ? -28.409 -0.834 9.088 1.00 67.76 ? 116 HIS B CB 1 ATOM 3709 C CG . HIS B 2 116 ? -27.492 -1.962 8.728 1.00 75.33 ? 116 HIS B CG 1 ATOM 3710 N ND1 . HIS B 2 116 ? -27.466 -2.531 7.473 1.00 72.39 ? 116 HIS B ND1 1 ATOM 3711 C CD2 . HIS B 2 116 ? -26.565 -2.625 9.460 1.00 84.07 ? 116 HIS B CD2 1 ATOM 3712 C CE1 . HIS B 2 116 ? -26.565 -3.497 7.448 1.00 71.14 ? 116 HIS B CE1 1 ATOM 3713 N NE2 . HIS B 2 116 ? -26.003 -3.574 8.640 1.00 79.03 ? 116 HIS B NE2 1 ATOM 3714 N N . LEU B 2 117 ? -29.223 2.295 8.471 1.00 69.65 ? 117 LEU B N 1 ATOM 3715 C CA . LEU B 2 117 ? -30.183 3.377 8.641 1.00 68.32 ? 117 LEU B CA 1 ATOM 3716 C C . LEU B 2 117 ? -31.282 3.265 7.595 1.00 69.26 ? 117 LEU B C 1 ATOM 3717 O O . LEU B 2 117 ? -31.946 4.246 7.267 1.00 71.30 ? 117 LEU B O 1 ATOM 3718 C CB . LEU B 2 117 ? -29.484 4.733 8.538 1.00 69.31 ? 117 LEU B CB 1 ATOM 3719 C CG . LEU B 2 117 ? -28.618 5.122 9.733 1.00 74.07 ? 117 LEU B CG 1 ATOM 3720 C CD1 . LEU B 2 117 ? -27.672 6.254 9.373 1.00 75.49 ? 117 LEU B CD1 1 ATOM 3721 C CD2 . LEU B 2 117 ? -29.512 5.517 10.895 1.00 79.97 ? 117 LEU B CD2 1 ATOM 3722 N N . ASN B 2 118 ? -31.469 2.051 7.089 1.00 61.06 ? 118 ASN B N 1 ATOM 3723 C CA . ASN B 2 118 ? -32.333 1.799 5.941 1.00 60.78 ? 118 ASN B CA 1 ATOM 3724 C C . ASN B 2 118 ? -33.818 2.049 6.183 1.00 64.17 ? 118 ASN B C 1 ATOM 3725 O O . ASN B 2 118 ? -34.293 2.001 7.316 1.00 68.12 ? 118 ASN B O 1 ATOM 3726 C CB . ASN B 2 118 ? -32.139 0.357 5.465 1.00 67.51 ? 118 ASN B CB 1 ATOM 3727 C CG . ASN B 2 118 ? -32.426 -0.661 6.552 1.00 79.25 ? 118 ASN B CG 1 ATOM 3728 O OD1 . ASN B 2 118 ? -33.577 -1.039 6.776 1.00 88.21 ? 118 ASN B OD1 1 ATOM 3729 N ND2 . ASN B 2 118 ? -31.379 -1.115 7.230 1.00 80.57 ? 118 ASN B ND2 1 ATOM 3730 N N . ASN B 2 119 ? -34.533 2.326 5.095 1.00 71.54 ? 119 ASN B N 1 ATOM 3731 C CA . ASN B 2 119 ? -35.990 2.423 5.096 1.00 71.72 ? 119 ASN B CA 1 ATOM 3732 C C . ASN B 2 119 ? -36.563 3.379 6.141 1.00 79.24 ? 119 ASN B C 1 ATOM 3733 O O . ASN B 2 119 ? -37.483 3.023 6.874 1.00 90.18 ? 119 ASN B O 1 ATOM 3734 C CB . ASN B 2 119 ? -36.600 1.034 5.297 1.00 72.55 ? 119 ASN B CB 1 ATOM 3735 C CG . ASN B 2 119 ? -36.117 0.030 4.267 1.00 75.80 ? 119 ASN B CG 1 ATOM 3736 O OD1 . ASN B 2 119 ? -36.682 -0.082 3.180 1.00 84.58 ? 119 ASN B OD1 1 ATOM 3737 N ND2 . ASN B 2 119 ? -35.071 -0.710 4.607 1.00 74.02 ? 119 ASN B ND2 1 ATOM 3738 N N . ASN B 2 120 ? -36.015 4.587 6.214 1.00 75.82 ? 120 ASN B N 1 ATOM 3739 C CA . ASN B 2 120 ? -36.549 5.601 7.116 1.00 80.64 ? 120 ASN B CA 1 ATOM 3740 C C . ASN B 2 120 ? -36.931 6.858 6.340 1.00 79.74 ? 120 ASN B C 1 ATOM 3741 O O . ASN B 2 120 ? -37.216 6.781 5.147 1.00 84.69 ? 120 ASN B O 1 ATOM 3742 C CB . ASN B 2 120 ? -35.545 5.929 8.224 1.00 80.02 ? 120 ASN B CB 1 ATOM 3743 C CG . ASN B 2 120 ? -35.347 4.777 9.190 1.00 77.13 ? 120 ASN B CG 1 ATOM 3744 O OD1 . ASN B 2 120 ? -36.224 4.476 9.997 1.00 83.09 ? 120 ASN B OD1 1 ATOM 3745 N ND2 . ASN B 2 120 ? -34.189 4.132 9.119 1.00 72.60 ? 120 ASN B ND2 1 ATOM 3746 N N . LYS B 2 121 ? -36.939 8.009 7.007 1.00 68.90 ? 121 LYS B N 1 ATOM 3747 C CA . LYS B 2 121 ? -37.365 9.252 6.363 1.00 76.73 ? 121 LYS B CA 1 ATOM 3748 C C . LYS B 2 121 ? -36.338 10.376 6.510 1.00 80.62 ? 121 LYS B C 1 ATOM 3749 O O . LYS B 2 121 ? -36.670 11.468 6.971 1.00 82.95 ? 121 LYS B O 1 ATOM 3750 C CB . LYS B 2 121 ? -38.708 9.714 6.935 1.00 90.72 ? 121 LYS B CB 1 ATOM 3751 C CG . LYS B 2 121 ? -39.873 8.759 6.711 1.00 95.30 ? 121 LYS B CG 1 ATOM 3752 C CD . LYS B 2 121 ? -41.162 9.338 7.285 1.00 98.87 ? 121 LYS B CD 1 ATOM 3753 C CE . LYS B 2 121 ? -42.368 8.478 6.950 1.00 103.15 ? 121 LYS B CE 1 ATOM 3754 N NZ . LYS B 2 121 ? -43.638 9.118 7.395 1.00 104.73 ? 121 LYS B NZ 1 ATOM 3755 N N . LEU B 2 122 ? -35.099 10.113 6.106 1.00 83.41 ? 122 LEU B N 1 ATOM 3756 C CA . LEU B 2 122 ? -34.018 11.090 6.230 1.00 83.46 ? 122 LEU B CA 1 ATOM 3757 C C . LEU B 2 122 ? -33.805 11.877 4.940 1.00 84.85 ? 122 LEU B C 1 ATOM 3758 O O . LEU B 2 122 ? -33.617 11.292 3.881 1.00 82.83 ? 122 LEU B O 1 ATOM 3759 C CB . LEU B 2 122 ? -32.714 10.390 6.614 1.00 75.88 ? 122 LEU B CB 1 ATOM 3760 C CG . LEU B 2 122 ? -32.730 9.487 7.846 1.00 70.13 ? 122 LEU B CG 1 ATOM 3761 C CD1 . LEU B 2 122 ? -31.463 8.652 7.904 1.00 68.93 ? 122 LEU B CD1 1 ATOM 3762 C CD2 . LEU B 2 122 ? -32.886 10.310 9.103 1.00 81.21 ? 122 LEU B CD2 1 ATOM 3763 N N . GLU B 2 123 ? -33.807 13.201 5.017 1.00 95.56 ? 123 GLU B N 1 ATOM 3764 C CA . GLU B 2 123 ? -33.623 13.989 3.803 1.00 96.72 ? 123 GLU B CA 1 ATOM 3765 C C . GLU B 2 123 ? -32.230 14.612 3.703 1.00 91.94 ? 123 GLU B C 1 ATOM 3766 O O . GLU B 2 123 ? -31.704 14.790 2.604 1.00 91.50 ? 123 GLU B O 1 ATOM 3767 C CB . GLU B 2 123 ? -34.700 15.070 3.711 1.00 102.64 ? 123 GLU B CB 1 ATOM 3768 C CG . GLU B 2 123 ? -35.271 15.489 5.047 1.00 110.60 ? 123 GLU B CG 1 ATOM 3769 C CD . GLU B 2 123 ? -36.539 16.292 4.891 1.00 117.76 ? 123 GLU B CD 1 ATOM 3770 O OE1 . GLU B 2 123 ? -36.984 16.477 3.738 1.00 119.88 ? 123 GLU B OE1 1 ATOM 3771 O OE2 . GLU B 2 123 ? -37.089 16.735 5.920 1.00 121.78 ? 123 GLU B OE2 1 ATOM 3772 N N . VAL B 2 124 ? -31.626 14.928 4.843 1.00 80.44 ? 124 VAL B N 1 ATOM 3773 C CA . VAL B 2 124 ? -30.332 15.601 4.845 1.00 70.92 ? 124 VAL B CA 1 ATOM 3774 C C . VAL B 2 124 ? -29.304 14.887 5.723 1.00 63.70 ? 124 VAL B C 1 ATOM 3775 O O . VAL B 2 124 ? -29.618 14.433 6.822 1.00 62.75 ? 124 VAL B O 1 ATOM 3776 C CB . VAL B 2 124 ? -30.471 17.062 5.324 1.00 73.06 ? 124 VAL B CB 1 ATOM 3777 C CG1 . VAL B 2 124 ? -29.129 17.769 5.278 1.00 75.46 ? 124 VAL B CG1 1 ATOM 3778 C CG2 . VAL B 2 124 ? -31.495 17.809 4.481 1.00 76.86 ? 124 VAL B CG2 1 ATOM 3779 N N . LEU B 2 125 ? -28.077 14.784 5.222 1.00 66.48 ? 125 LEU B N 1 ATOM 3780 C CA . LEU B 2 125 ? -26.958 14.293 6.016 1.00 72.54 ? 125 LEU B CA 1 ATOM 3781 C C . LEU B 2 125 ? -26.067 15.449 6.454 1.00 78.72 ? 125 LEU B C 1 ATOM 3782 O O . LEU B 2 125 ? -25.129 15.815 5.747 1.00 83.12 ? 125 LEU B O 1 ATOM 3783 C CB . LEU B 2 125 ? -26.134 13.273 5.228 1.00 75.27 ? 125 LEU B CB 1 ATOM 3784 C CG . LEU B 2 125 ? -26.728 11.874 5.073 1.00 70.30 ? 125 LEU B CG 1 ATOM 3785 C CD1 . LEU B 2 125 ? -25.837 10.995 4.209 1.00 67.66 ? 125 LEU B CD1 1 ATOM 3786 C CD2 . LEU B 2 125 ? -26.930 11.251 6.436 1.00 69.56 ? 125 LEU B CD2 1 ATOM 3787 N N . ARG B 2 126 ? -26.369 16.020 7.616 1.00 86.73 ? 126 ARG B N 1 ATOM 3788 C CA . ARG B 2 126 ? -25.572 17.109 8.176 1.00 95.69 ? 126 ARG B CA 1 ATOM 3789 C C . ARG B 2 126 ? -24.120 16.680 8.372 1.00 93.12 ? 126 ARG B C 1 ATOM 3790 O O . ARG B 2 126 ? -23.835 15.502 8.587 1.00 93.19 ? 126 ARG B O 1 ATOM 3791 C CB . ARG B 2 126 ? -26.170 17.584 9.503 1.00 107.14 ? 126 ARG B CB 1 ATOM 3792 C CG . ARG B 2 126 ? -27.534 18.236 9.371 1.00 112.33 ? 126 ARG B CG 1 ATOM 3793 C CD . ARG B 2 126 ? -27.432 19.591 8.688 1.00 120.51 ? 126 ARG B CD 1 ATOM 3794 N NE . ARG B 2 126 ? -28.549 19.825 7.777 1.00 127.30 ? 126 ARG B NE 1 ATOM 3795 C CZ . ARG B 2 126 ? -29.763 20.203 8.161 1.00 133.77 ? 126 ARG B CZ 1 ATOM 3796 N NH1 . ARG B 2 126 ? -30.027 20.391 9.448 1.00 139.03 ? 126 ARG B NH1 1 ATOM 3797 N NH2 . ARG B 2 126 ? -30.717 20.390 7.258 1.00 133.63 ? 126 ARG B NH2 1 ATOM 3798 N N . GLU B 2 127 ? -23.205 17.640 8.298 1.00 89.76 ? 127 GLU B N 1 ATOM 3799 C CA . GLU B 2 127 ? -21.782 17.326 8.336 1.00 94.01 ? 127 GLU B CA 1 ATOM 3800 C C . GLU B 2 127 ? -21.350 16.806 9.703 1.00 92.38 ? 127 GLU B C 1 ATOM 3801 O O . GLU B 2 127 ? -20.356 16.090 9.817 1.00 89.17 ? 127 GLU B O 1 ATOM 3802 C CB . GLU B 2 127 ? -20.948 18.553 7.959 1.00 101.69 ? 127 GLU B CB 1 ATOM 3803 C CG . GLU B 2 127 ? -20.760 19.547 9.088 1.00 111.20 ? 127 GLU B CG 1 ATOM 3804 C CD . GLU B 2 127 ? -19.722 20.601 8.767 1.00 120.88 ? 127 GLU B CD 1 ATOM 3805 O OE1 . GLU B 2 127 ? -19.079 21.107 9.711 1.00 125.78 ? 127 GLU B OE1 1 ATOM 3806 O OE2 . GLU B 2 127 ? -19.549 20.924 7.571 1.00 121.93 ? 127 GLU B OE2 1 ATOM 3807 N N . ASP B 2 128 ? -22.106 17.162 10.735 1.00 96.63 ? 128 ASP B N 1 ATOM 3808 C CA . ASP B 2 128 ? -21.760 16.791 12.100 1.00 101.51 ? 128 ASP B CA 1 ATOM 3809 C C . ASP B 2 128 ? -22.656 15.677 12.630 1.00 98.53 ? 128 ASP B C 1 ATOM 3810 O O . ASP B 2 128 ? -22.644 15.379 13.824 1.00 101.62 ? 128 ASP B O 1 ATOM 3811 C CB . ASP B 2 128 ? -21.845 18.015 13.015 1.00 109.18 ? 128 ASP B CB 1 ATOM 3812 C CG . ASP B 2 128 ? -23.100 18.835 12.776 1.00 117.78 ? 128 ASP B CG 1 ATOM 3813 O OD1 . ASP B 2 128 ? -23.147 19.999 13.227 1.00 120.66 ? 128 ASP B OD1 1 ATOM 3814 O OD2 . ASP B 2 128 ? -24.037 18.321 12.129 1.00 120.39 ? 128 ASP B OD2 1 ATOM 3815 N N . THR B 2 129 ? -23.428 15.066 11.735 1.00 96.01 ? 129 THR B N 1 ATOM 3816 C CA . THR B 2 129 ? -24.372 14.019 12.117 1.00 98.13 ? 129 THR B CA 1 ATOM 3817 C C . THR B 2 129 ? -23.669 12.804 12.718 1.00 102.02 ? 129 THR B C 1 ATOM 3818 O O . THR B 2 129 ? -24.045 12.327 13.789 1.00 107.41 ? 129 THR B O 1 ATOM 3819 C CB . THR B 2 129 ? -25.223 13.566 10.916 1.00 94.20 ? 129 THR B CB 1 ATOM 3820 O OG1 . THR B 2 129 ? -26.140 14.608 10.559 1.00 98.21 ? 129 THR B OG1 1 ATOM 3821 C CG2 . THR B 2 129 ? -26.010 12.313 11.258 1.00 90.80 ? 129 THR B CG2 1 ATOM 3822 N N . PHE B 2 130 ? -22.647 12.308 12.030 1.00 98.01 ? 130 PHE B N 1 ATOM 3823 C CA . PHE B 2 130 ? -21.885 11.168 12.526 1.00 99.16 ? 130 PHE B CA 1 ATOM 3824 C C . PHE B 2 130 ? -20.708 11.628 13.372 1.00 108.67 ? 130 PHE B C 1 ATOM 3825 O O . PHE B 2 130 ? -19.552 11.413 13.011 1.00 113.90 ? 130 PHE B O 1 ATOM 3826 C CB . PHE B 2 130 ? -21.382 10.312 11.368 1.00 92.85 ? 130 PHE B CB 1 ATOM 3827 C CG . PHE B 2 130 ? -22.439 9.973 10.364 1.00 89.20 ? 130 PHE B CG 1 ATOM 3828 C CD1 . PHE B 2 130 ? -23.377 8.993 10.631 1.00 85.62 ? 130 PHE B CD1 1 ATOM 3829 C CD2 . PHE B 2 130 ? -22.491 10.628 9.147 1.00 84.70 ? 130 PHE B CD2 1 ATOM 3830 C CE1 . PHE B 2 130 ? -24.350 8.674 9.706 1.00 72.75 ? 130 PHE B CE1 1 ATOM 3831 C CE2 . PHE B 2 130 ? -23.461 10.313 8.219 1.00 77.28 ? 130 PHE B CE2 1 ATOM 3832 C CZ . PHE B 2 130 ? -24.392 9.333 8.499 1.00 72.98 ? 130 PHE B CZ 1 ATOM 3833 N N . LEU B 2 131 ? -21.005 12.259 14.502 1.00 108.67 ? 131 LEU B N 1 ATOM 3834 C CA . LEU B 2 131 ? -19.965 12.862 15.322 1.00 112.18 ? 131 LEU B CA 1 ATOM 3835 C C . LEU B 2 131 ? -19.113 11.820 16.035 1.00 112.26 ? 131 LEU B C 1 ATOM 3836 O O . LEU B 2 131 ? -17.889 11.933 16.078 1.00 115.03 ? 131 LEU B O 1 ATOM 3837 C CB . LEU B 2 131 ? -20.582 13.810 16.352 1.00 115.16 ? 131 LEU B CB 1 ATOM 3838 C CG . LEU B 2 131 ? -19.953 15.199 16.503 1.00 119.46 ? 131 LEU B CG 1 ATOM 3839 C CD1 . LEU B 2 131 ? -20.286 15.789 17.865 1.00 122.87 ? 131 LEU B CD1 1 ATOM 3840 C CD2 . LEU B 2 131 ? -18.447 15.168 16.277 1.00 121.64 ? 131 LEU B CD2 1 ATOM 3841 N N . GLY B 2 132 ? -19.763 10.804 16.586 1.00 109.10 ? 132 GLY B N 1 ATOM 3842 C CA . GLY B 2 132 ? -19.109 9.914 17.527 1.00 112.93 ? 132 GLY B CA 1 ATOM 3843 C C . GLY B 2 132 ? -18.083 8.924 17.005 1.00 111.27 ? 132 GLY B C 1 ATOM 3844 O O . GLY B 2 132 ? -17.139 8.579 17.717 1.00 115.63 ? 132 GLY B O 1 ATOM 3845 N N . LEU B 2 133 ? -18.249 8.470 15.769 1.00 106.94 ? 133 LEU B N 1 ATOM 3846 C CA . LEU B 2 133 ? -17.502 7.309 15.298 1.00 105.29 ? 133 LEU B CA 1 ATOM 3847 C C . LEU B 2 133 ? -16.092 7.640 14.808 1.00 117.15 ? 133 LEU B C 1 ATOM 3848 O O . LEU B 2 133 ? -15.870 8.643 14.129 1.00 119.14 ? 133 LEU B O 1 ATOM 3849 C CB . LEU B 2 133 ? -18.278 6.604 14.181 1.00 91.16 ? 133 LEU B CB 1 ATOM 3850 C CG . LEU B 2 133 ? -19.720 7.037 13.887 1.00 80.19 ? 133 LEU B CG 1 ATOM 3851 C CD1 . LEU B 2 133 ? -20.142 6.522 12.524 1.00 80.64 ? 133 LEU B CD1 1 ATOM 3852 C CD2 . LEU B 2 133 ? -20.694 6.551 14.955 1.00 74.64 ? 133 LEU B CD2 1 ATOM 3853 N N . GLU B 2 134 ? -15.141 6.789 15.176 1.00 127.04 ? 134 GLU B N 1 ATOM 3854 C CA . GLU B 2 134 ? -13.805 6.836 14.603 1.00 131.27 ? 134 GLU B CA 1 ATOM 3855 C C . GLU B 2 134 ? -13.510 5.490 13.970 1.00 128.32 ? 134 GLU B C 1 ATOM 3856 O O . GLU B 2 134 ? -12.592 5.356 13.161 1.00 136.64 ? 134 GLU B O 1 ATOM 3857 C CB . GLU B 2 134 ? -12.744 7.152 15.658 1.00 142.04 ? 134 GLU B CB 1 ATOM 3858 C CG . GLU B 2 134 ? -12.926 8.463 16.395 1.00 149.17 ? 134 GLU B CG 1 ATOM 3859 C CD . GLU B 2 134 ? -11.727 8.793 17.261 1.00 152.68 ? 134 GLU B CD 1 ATOM 3860 O OE1 . GLU B 2 134 ? -10.646 8.215 17.019 1.00 150.25 ? 134 GLU B OE1 1 ATOM 3861 O OE2 . GLU B 2 134 ? -11.862 9.624 18.182 1.00 156.59 ? 134 GLU B OE2 1 ATOM 3862 N N . SER B 2 135 ? -14.307 4.496 14.348 1.00 111.59 ? 135 SER B N 1 ATOM 3863 C CA . SER B 2 135 ? -13.995 3.105 14.048 1.00 107.88 ? 135 SER B CA 1 ATOM 3864 C C . SER B 2 135 ? -14.880 2.475 12.976 1.00 94.73 ? 135 SER B C 1 ATOM 3865 O O . SER B 2 135 ? -14.645 1.336 12.574 1.00 86.61 ? 135 SER B O 1 ATOM 3866 C CB . SER B 2 135 ? -14.091 2.269 15.328 1.00 115.41 ? 135 SER B CB 1 ATOM 3867 O OG . SER B 2 135 ? -13.126 2.676 16.284 1.00 122.21 ? 135 SER B OG 1 ATOM 3868 N N . LEU B 2 136 ? -15.886 3.207 12.509 1.00 89.19 ? 136 LEU B N 1 ATOM 3869 C CA . LEU B 2 136 ? -16.879 2.647 11.589 1.00 81.35 ? 136 LEU B CA 1 ATOM 3870 C C . LEU B 2 136 ? -16.360 2.430 10.165 1.00 79.07 ? 136 LEU B C 1 ATOM 3871 O O . LEU B 2 136 ? -15.754 3.323 9.578 1.00 77.10 ? 136 LEU B O 1 ATOM 3872 C CB . LEU B 2 136 ? -18.109 3.552 11.549 1.00 74.37 ? 136 LEU B CB 1 ATOM 3873 C CG . LEU B 2 136 ? -19.267 3.090 10.667 1.00 69.73 ? 136 LEU B CG 1 ATOM 3874 C CD1 . LEU B 2 136 ? -20.496 2.819 11.517 1.00 69.43 ? 136 LEU B CD1 1 ATOM 3875 C CD2 . LEU B 2 136 ? -19.568 4.120 9.595 1.00 61.06 ? 136 LEU B CD2 1 ATOM 3876 N N . GLU B 2 137 ? -16.616 1.247 9.609 1.00 81.14 ? 137 GLU B N 1 ATOM 3877 C CA . GLU B 2 137 ? -16.191 0.954 8.240 1.00 78.07 ? 137 GLU B CA 1 ATOM 3878 C C . GLU B 2 137 ? -17.351 0.506 7.348 1.00 69.14 ? 137 GLU B C 1 ATOM 3879 O O . GLU B 2 137 ? -17.148 0.079 6.211 1.00 66.11 ? 137 GLU B O 1 ATOM 3880 C CB . GLU B 2 137 ? -15.086 -0.107 8.236 1.00 91.89 ? 137 GLU B CB 1 ATOM 3881 C CG . GLU B 2 137 ? -15.554 -1.546 8.342 1.00 101.72 ? 137 GLU B CG 1 ATOM 3882 C CD . GLU B 2 137 ? -14.465 -2.528 7.945 1.00 110.56 ? 137 GLU B CD 1 ATOM 3883 O OE1 . GLU B 2 137 ? -13.304 -2.100 7.778 1.00 112.27 ? 137 GLU B OE1 1 ATOM 3884 O OE2 . GLU B 2 137 ? -14.767 -3.728 7.794 1.00 111.93 ? 137 GLU B OE2 1 ATOM 3885 N N . TYR B 2 138 ? -18.569 0.625 7.861 1.00 63.51 ? 138 TYR B N 1 ATOM 3886 C CA . TYR B 2 138 ? -19.750 0.209 7.119 1.00 61.62 ? 138 TYR B CA 1 ATOM 3887 C C . TYR B 2 138 ? -20.913 1.143 7.414 1.00 62.39 ? 138 TYR B C 1 ATOM 3888 O O . TYR B 2 138 ? -21.191 1.456 8.572 1.00 73.14 ? 138 TYR B O 1 ATOM 3889 C CB . TYR B 2 138 ? -20.119 -1.231 7.475 1.00 61.64 ? 138 TYR B CB 1 ATOM 3890 C CG . TYR B 2 138 ? -21.207 -1.848 6.621 1.00 68.70 ? 138 TYR B CG 1 ATOM 3891 C CD1 . TYR B 2 138 ? -20.901 -2.794 5.652 1.00 69.44 ? 138 TYR B CD1 1 ATOM 3892 C CD2 . TYR B 2 138 ? -22.542 -1.504 6.799 1.00 72.89 ? 138 TYR B CD2 1 ATOM 3893 C CE1 . TYR B 2 138 ? -21.892 -3.369 4.877 1.00 65.49 ? 138 TYR B CE1 1 ATOM 3894 C CE2 . TYR B 2 138 ? -23.537 -2.072 6.030 1.00 68.69 ? 138 TYR B CE2 1 ATOM 3895 C CZ . TYR B 2 138 ? -23.208 -3.003 5.071 1.00 68.68 ? 138 TYR B CZ 1 ATOM 3896 O OH . TYR B 2 138 ? -24.202 -3.569 4.305 1.00 73.56 ? 138 TYR B OH 1 ATOM 3897 N N . LEU B 2 139 ? -21.602 1.576 6.366 1.00 53.68 ? 139 LEU B N 1 ATOM 3898 C CA . LEU B 2 139 ? -22.730 2.483 6.530 1.00 49.97 ? 139 LEU B CA 1 ATOM 3899 C C . LEU B 2 139 ? -23.802 2.246 5.480 1.00 54.28 ? 139 LEU B C 1 ATOM 3900 O O . LEU B 2 139 ? -23.578 2.466 4.289 1.00 57.47 ? 139 LEU B O 1 ATOM 3901 C CB . LEU B 2 139 ? -22.264 3.936 6.466 1.00 49.19 ? 139 LEU B CB 1 ATOM 3902 C CG . LEU B 2 139 ? -23.402 4.954 6.527 1.00 52.60 ? 139 LEU B CG 1 ATOM 3903 C CD1 . LEU B 2 139 ? -24.247 4.725 7.775 1.00 57.23 ? 139 LEU B CD1 1 ATOM 3904 C CD2 . LEU B 2 139 ? -22.858 6.372 6.496 1.00 51.35 ? 139 LEU B CD2 1 ATOM 3905 N N . GLN B 2 140 ? -24.971 1.813 5.934 1.00 61.28 ? 140 GLN B N 1 ATOM 3906 C CA . GLN B 2 140 ? -26.087 1.530 5.044 1.00 65.68 ? 140 GLN B CA 1 ATOM 3907 C C . GLN B 2 140 ? -27.226 2.506 5.312 1.00 68.52 ? 140 GLN B C 1 ATOM 3908 O O . GLN B 2 140 ? -27.712 2.609 6.438 1.00 72.11 ? 140 GLN B O 1 ATOM 3909 C CB . GLN B 2 140 ? -26.560 0.085 5.221 1.00 69.88 ? 140 GLN B CB 1 ATOM 3910 C CG . GLN B 2 140 ? -27.320 -0.472 4.032 1.00 73.86 ? 140 GLN B CG 1 ATOM 3911 C CD . GLN B 2 140 ? -27.614 -1.953 4.166 1.00 78.32 ? 140 GLN B CD 1 ATOM 3912 O OE1 . GLN B 2 140 ? -26.759 -2.730 4.590 1.00 78.64 ? 140 GLN B OE1 1 ATOM 3913 N NE2 . GLN B 2 140 ? -28.830 -2.351 3.804 1.00 83.23 ? 140 GLN B NE2 1 ATOM 3914 N N . ALA B 2 141 ? -27.645 3.228 4.278 1.00 71.51 ? 141 ALA B N 1 ATOM 3915 C CA . ALA B 2 141 ? -28.660 4.265 4.439 1.00 73.59 ? 141 ALA B CA 1 ATOM 3916 C C . ALA B 2 141 ? -29.656 4.271 3.286 1.00 76.86 ? 141 ALA B C 1 ATOM 3917 O O . ALA B 2 141 ? -30.120 5.327 2.861 1.00 86.35 ? 141 ALA B O 1 ATOM 3918 C CB . ALA B 2 141 ? -27.999 5.627 4.566 1.00 72.87 ? 141 ALA B CB 1 ATOM 3919 N N . ASP B 2 142 ? -29.994 3.087 2.793 1.00 66.67 ? 142 ASP B N 1 ATOM 3920 C CA . ASP B 2 142 ? -30.862 2.955 1.630 1.00 67.28 ? 142 ASP B CA 1 ATOM 3921 C C . ASP B 2 142 ? -32.327 3.308 1.904 1.00 73.77 ? 142 ASP B C 1 ATOM 3922 O O . ASP B 2 142 ? -32.801 3.220 3.038 1.00 73.72 ? 142 ASP B O 1 ATOM 3923 C CB . ASP B 2 142 ? -30.768 1.530 1.078 1.00 69.52 ? 142 ASP B CB 1 ATOM 3924 C CG . ASP B 2 142 ? -30.493 0.506 2.158 1.00 77.69 ? 142 ASP B CG 1 ATOM 3925 O OD1 . ASP B 2 142 ? -29.968 0.905 3.215 1.00 80.29 ? 142 ASP B OD1 1 ATOM 3926 O OD2 . ASP B 2 142 ? -30.788 -0.692 1.954 1.00 84.17 ? 142 ASP B OD2 1 ATOM 3927 N N . TYR B 2 143 ? -33.017 3.728 0.844 1.00 81.38 ? 143 TYR B N 1 ATOM 3928 C CA . TYR B 2 143 ? -34.464 3.963 0.835 1.00 84.46 ? 143 TYR B CA 1 ATOM 3929 C C . TYR B 2 143 ? -34.923 5.153 1.668 1.00 88.72 ? 143 TYR B C 1 ATOM 3930 O O . TYR B 2 143 ? -36.097 5.238 2.019 1.00 93.46 ? 143 TYR B O 1 ATOM 3931 C CB . TYR B 2 143 ? -35.208 2.714 1.319 1.00 79.82 ? 143 TYR B CB 1 ATOM 3932 C CG . TYR B 2 143 ? -34.973 1.488 0.477 1.00 80.01 ? 143 TYR B CG 1 ATOM 3933 C CD1 . TYR B 2 143 ? -35.624 1.324 -0.737 1.00 80.39 ? 143 TYR B CD1 1 ATOM 3934 C CD2 . TYR B 2 143 ? -34.114 0.487 0.901 1.00 80.20 ? 143 TYR B CD2 1 ATOM 3935 C CE1 . TYR B 2 143 ? -35.418 0.201 -1.509 1.00 80.99 ? 143 TYR B CE1 1 ATOM 3936 C CE2 . TYR B 2 143 ? -33.902 -0.640 0.136 1.00 81.98 ? 143 TYR B CE2 1 ATOM 3937 C CZ . TYR B 2 143 ? -34.556 -0.778 -1.068 1.00 82.90 ? 143 TYR B CZ 1 ATOM 3938 O OH . TYR B 2 143 ? -34.351 -1.898 -1.838 1.00 86.54 ? 143 TYR B OH 1 ATOM 3939 N N . ASN B 2 144 ? -34.022 6.085 1.956 1.00 89.89 ? 144 ASN B N 1 ATOM 3940 C CA . ASN B 2 144 ? -34.274 7.042 3.032 1.00 96.86 ? 144 ASN B CA 1 ATOM 3941 C C . ASN B 2 144 ? -34.803 8.432 2.668 1.00 102.24 ? 144 ASN B C 1 ATOM 3942 O O . ASN B 2 144 ? -35.082 9.211 3.574 1.00 118.74 ? 144 ASN B O 1 ATOM 3943 C CB . ASN B 2 144 ? -32.993 7.220 3.841 1.00 99.49 ? 144 ASN B CB 1 ATOM 3944 C CG . ASN B 2 144 ? -33.138 6.725 5.255 1.00 101.18 ? 144 ASN B CG 1 ATOM 3945 O OD1 . ASN B 2 144 ? -33.910 7.275 6.034 1.00 102.03 ? 144 ASN B OD1 1 ATOM 3946 N ND2 . ASN B 2 144 ? -32.398 5.681 5.598 1.00 106.19 ? 144 ASN B ND2 1 ATOM 3947 N N . TYR B 2 145 ? -34.947 8.728 1.375 1.00 90.05 ? 145 TYR B N 1 ATOM 3948 C CA . TYR B 2 145 ? -35.385 10.048 0.868 1.00 83.59 ? 145 TYR B CA 1 ATOM 3949 C C . TYR B 2 145 ? -34.331 11.158 0.977 1.00 84.84 ? 145 TYR B C 1 ATOM 3950 O O . TYR B 2 145 ? -34.693 12.329 1.090 1.00 90.09 ? 145 TYR B O 1 ATOM 3951 C CB . TYR B 2 145 ? -36.648 10.564 1.585 1.00 73.86 ? 145 TYR B CB 1 ATOM 3952 C CG . TYR B 2 145 ? -37.875 9.679 1.567 1.00 78.04 ? 145 TYR B CG 1 ATOM 3953 C CD1 . TYR B 2 145 ? -38.033 8.668 0.629 1.00 92.10 ? 145 TYR B CD1 1 ATOM 3954 C CD2 . TYR B 2 145 ? -38.890 9.875 2.496 1.00 75.96 ? 145 TYR B CD2 1 ATOM 3955 C CE1 . TYR B 2 145 ? -39.168 7.869 0.625 1.00 96.33 ? 145 TYR B CE1 1 ATOM 3956 C CE2 . TYR B 2 145 ? -40.022 9.088 2.501 1.00 85.37 ? 145 TYR B CE2 1 ATOM 3957 C CZ . TYR B 2 145 ? -40.158 8.087 1.565 1.00 93.82 ? 145 TYR B CZ 1 ATOM 3958 O OH . TYR B 2 145 ? -41.289 7.302 1.574 1.00 97.06 ? 145 TYR B OH 1 ATOM 3959 N N . ILE B 2 146 ? -33.046 10.820 0.939 1.00 81.31 ? 146 ILE B N 1 ATOM 3960 C CA . ILE B 2 146 ? -32.004 11.844 1.066 1.00 82.80 ? 146 ILE B CA 1 ATOM 3961 C C . ILE B 2 146 ? -31.834 12.657 -0.215 1.00 91.05 ? 146 ILE B C 1 ATOM 3962 O O . ILE B 2 146 ? -31.394 12.138 -1.238 1.00 97.98 ? 146 ILE B O 1 ATOM 3963 C CB . ILE B 2 146 ? -30.644 11.236 1.435 1.00 81.54 ? 146 ILE B CB 1 ATOM 3964 C CG1 . ILE B 2 146 ? -30.739 10.483 2.760 1.00 76.57 ? 146 ILE B CG1 1 ATOM 3965 C CG2 . ILE B 2 146 ? -29.586 12.331 1.519 1.00 86.13 ? 146 ILE B CG2 1 ATOM 3966 C CD1 . ILE B 2 146 ? -29.445 9.824 3.176 1.00 75.08 ? 146 ILE B CD1 1 ATOM 3967 N N . SER B 2 147 ? -32.170 13.940 -0.144 1.00 93.53 ? 147 SER B N 1 ATOM 3968 C CA . SER B 2 147 ? -32.111 14.811 -1.310 1.00 97.08 ? 147 SER B CA 1 ATOM 3969 C C . SER B 2 147 ? -30.761 15.508 -1.443 1.00 101.87 ? 147 SER B C 1 ATOM 3970 O O . SER B 2 147 ? -30.233 15.652 -2.547 1.00 101.17 ? 147 SER B O 1 ATOM 3971 C CB . SER B 2 147 ? -33.235 15.846 -1.244 1.00 96.31 ? 147 SER B CB 1 ATOM 3972 O OG . SER B 2 147 ? -33.386 16.345 0.074 1.00 95.61 ? 147 SER B OG 1 ATOM 3973 N N . THR B 2 148 ? -30.205 15.942 -0.318 1.00 106.48 ? 148 THR B N 1 ATOM 3974 C CA . THR B 2 148 ? -28.944 16.672 -0.334 1.00 108.72 ? 148 THR B CA 1 ATOM 3975 C C . THR B 2 148 ? -28.020 16.282 0.814 1.00 101.51 ? 148 THR B C 1 ATOM 3976 O O . THR B 2 148 ? -28.289 16.589 1.973 1.00 101.19 ? 148 THR B O 1 ATOM 3977 C CB . THR B 2 148 ? -29.172 18.198 -0.269 1.00 113.87 ? 148 THR B CB 1 ATOM 3978 O OG1 . THR B 2 148 ? -30.036 18.508 0.831 1.00 107.76 ? 148 THR B OG1 1 ATOM 3979 C CG2 . THR B 2 148 ? -29.794 18.712 -1.563 1.00 118.44 ? 148 THR B CG2 1 ATOM 3980 N N . ILE B 2 149 ? -26.930 15.600 0.484 1.00 101.44 ? 149 ILE B N 1 ATOM 3981 C CA . ILE B 2 149 ? -25.859 15.380 1.445 1.00 94.91 ? 149 ILE B CA 1 ATOM 3982 C C . ILE B 2 149 ? -25.038 16.662 1.527 1.00 98.53 ? 149 ILE B C 1 ATOM 3983 O O . ILE B 2 149 ? -24.968 17.412 0.554 1.00 100.35 ? 149 ILE B O 1 ATOM 3984 C CB . ILE B 2 149 ? -24.956 14.191 1.043 1.00 79.27 ? 149 ILE B CB 1 ATOM 3985 C CG1 . ILE B 2 149 ? -25.773 12.908 0.921 1.00 76.30 ? 149 ILE B CG1 1 ATOM 3986 C CG2 . ILE B 2 149 ? -23.842 13.976 2.049 1.00 67.90 ? 149 ILE B CG2 1 ATOM 3987 C CD1 . ILE B 2 149 ? -24.932 11.695 0.580 1.00 72.37 ? 149 ILE B CD1 1 ATOM 3988 N N . GLU B 2 150 ? -24.452 16.936 2.688 1.00 95.59 ? 150 GLU B N 1 ATOM 3989 C CA . GLU B 2 150 ? -23.510 18.039 2.821 1.00 90.51 ? 150 GLU B CA 1 ATOM 3990 C C . GLU B 2 150 ? -22.091 17.508 2.645 1.00 87.92 ? 150 GLU B C 1 ATOM 3991 O O . GLU B 2 150 ? -21.841 16.322 2.852 1.00 86.97 ? 150 GLU B O 1 ATOM 3992 C CB . GLU B 2 150 ? -23.677 18.737 4.171 1.00 89.38 ? 150 GLU B CB 1 ATOM 3993 C CG . GLU B 2 150 ? -25.056 19.357 4.359 1.00 98.23 ? 150 GLU B CG 1 ATOM 3994 C CD . GLU B 2 150 ? -25.237 20.008 5.717 1.00 108.09 ? 150 GLU B CD 1 ATOM 3995 O OE1 . GLU B 2 150 ? -24.432 19.724 6.630 1.00 112.96 ? 150 GLU B OE1 1 ATOM 3996 O OE2 . GLU B 2 150 ? -26.185 20.807 5.869 1.00 108.70 ? 150 GLU B OE2 1 ATOM 3997 N N . ALA B 2 151 ? -21.169 18.385 2.261 1.00 90.41 ? 151 ALA B N 1 ATOM 3998 C CA . ALA B 2 151 ? -19.819 17.976 1.877 1.00 87.52 ? 151 ALA B CA 1 ATOM 3999 C C . ALA B 2 151 ? -19.056 17.263 2.993 1.00 85.69 ? 151 ALA B C 1 ATOM 4000 O O . ALA B 2 151 ? -18.580 16.140 2.815 1.00 82.80 ? 151 ALA B O 1 ATOM 4001 C CB . ALA B 2 151 ? -19.029 19.185 1.400 1.00 85.74 ? 151 ALA B CB 1 ATOM 4002 N N . GLY B 2 152 ? -18.944 17.917 4.143 1.00 88.20 ? 152 GLY B N 1 ATOM 4003 C CA . GLY B 2 152 ? -18.137 17.398 5.232 1.00 90.09 ? 152 GLY B CA 1 ATOM 4004 C C . GLY B 2 152 ? -18.783 16.299 6.056 1.00 92.10 ? 152 GLY B C 1 ATOM 4005 O O . GLY B 2 152 ? -18.306 15.985 7.148 1.00 94.23 ? 152 GLY B O 1 ATOM 4006 N N . ALA B 2 153 ? -19.852 15.706 5.530 1.00 82.70 ? 153 ALA B N 1 ATOM 4007 C CA . ALA B 2 153 ? -20.621 14.699 6.260 1.00 72.76 ? 153 ALA B CA 1 ATOM 4008 C C . ALA B 2 153 ? -19.790 13.485 6.651 1.00 71.51 ? 153 ALA B C 1 ATOM 4009 O O . ALA B 2 153 ? -19.803 13.062 7.807 1.00 70.25 ? 153 ALA B O 1 ATOM 4010 C CB . ALA B 2 153 ? -21.822 14.260 5.438 1.00 64.50 ? 153 ALA B CB 1 ATOM 4011 N N . PHE B 2 154 ? -19.068 12.925 5.688 1.00 72.35 ? 154 PHE B N 1 ATOM 4012 C CA . PHE B 2 154 ? -18.332 11.689 5.924 1.00 74.29 ? 154 PHE B CA 1 ATOM 4013 C C . PHE B 2 154 ? -16.883 11.947 6.308 1.00 83.67 ? 154 PHE B C 1 ATOM 4014 O O . PHE B 2 154 ? -16.084 11.016 6.415 1.00 80.02 ? 154 PHE B O 1 ATOM 4015 C CB . PHE B 2 154 ? -18.403 10.796 4.691 1.00 68.64 ? 154 PHE B CB 1 ATOM 4016 C CG . PHE B 2 154 ? -19.796 10.600 4.179 1.00 71.46 ? 154 PHE B CG 1 ATOM 4017 C CD1 . PHE B 2 154 ? -20.738 9.936 4.946 1.00 68.17 ? 154 PHE B CD1 1 ATOM 4018 C CD2 . PHE B 2 154 ? -20.171 11.089 2.940 1.00 77.58 ? 154 PHE B CD2 1 ATOM 4019 C CE1 . PHE B 2 154 ? -22.027 9.757 4.486 1.00 66.72 ? 154 PHE B CE1 1 ATOM 4020 C CE2 . PHE B 2 154 ? -21.459 10.912 2.472 1.00 77.21 ? 154 PHE B CE2 1 ATOM 4021 C CZ . PHE B 2 154 ? -22.388 10.244 3.247 1.00 71.46 ? 154 PHE B CZ 1 ATOM 4022 N N . SER B 2 155 ? -16.548 13.214 6.520 1.00 91.63 ? 155 SER B N 1 ATOM 4023 C CA . SER B 2 155 ? -15.241 13.564 7.048 1.00 91.20 ? 155 SER B CA 1 ATOM 4024 C C . SER B 2 155 ? -15.133 13.011 8.462 1.00 104.29 ? 155 SER B C 1 ATOM 4025 O O . SER B 2 155 ? -16.154 12.795 9.122 1.00 109.92 ? 155 SER B O 1 ATOM 4026 C CB . SER B 2 155 ? -15.035 15.077 7.034 1.00 88.33 ? 155 SER B CB 1 ATOM 4027 O OG . SER B 2 155 ? -15.232 15.599 5.733 1.00 89.29 ? 155 SER B OG 1 ATOM 4028 N N . LYS B 2 156 ? -13.903 12.765 8.907 1.00 107.92 ? 156 LYS B N 1 ATOM 4029 C CA . LYS B 2 156 ? -13.629 12.228 10.240 1.00 105.74 ? 156 LYS B CA 1 ATOM 4030 C C . LYS B 2 156 ? -14.187 10.815 10.420 1.00 99.36 ? 156 LYS B C 1 ATOM 4031 O O . LYS B 2 156 ? -14.442 10.376 11.543 1.00 99.95 ? 156 LYS B O 1 ATOM 4032 C CB . LYS B 2 156 ? -14.186 13.160 11.322 1.00 107.28 ? 156 LYS B CB 1 ATOM 4033 C CG . LYS B 2 156 ? -13.714 14.595 11.180 1.00 112.37 ? 156 LYS B CG 1 ATOM 4034 C CD . LYS B 2 156 ? -14.188 15.450 12.335 1.00 117.66 ? 156 LYS B CD 1 ATOM 4035 C CE . LYS B 2 156 ? -13.504 16.802 12.319 1.00 128.83 ? 156 LYS B CE 1 ATOM 4036 N NZ . LYS B 2 156 ? -13.678 17.514 13.611 1.00 137.52 ? 156 LYS B NZ 1 ATOM 4037 N N . LEU B 2 157 ? -14.367 10.110 9.308 1.00 95.16 ? 157 LEU B N 1 ATOM 4038 C CA . LEU B 2 157 ? -14.749 8.702 9.335 1.00 86.08 ? 157 LEU B CA 1 ATOM 4039 C C . LEU B 2 157 ? -13.751 7.886 8.524 1.00 79.96 ? 157 LEU B C 1 ATOM 4040 O O . LEU B 2 157 ? -14.134 7.155 7.614 1.00 78.81 ? 157 LEU B O 1 ATOM 4041 C CB . LEU B 2 157 ? -16.161 8.501 8.780 1.00 83.32 ? 157 LEU B CB 1 ATOM 4042 C CG . LEU B 2 157 ? -17.333 9.201 9.470 1.00 79.44 ? 157 LEU B CG 1 ATOM 4043 C CD1 . LEU B 2 157 ? -18.639 8.845 8.775 1.00 67.12 ? 157 LEU B CD1 1 ATOM 4044 C CD2 . LEU B 2 157 ? -17.391 8.839 10.946 1.00 86.11 ? 157 LEU B CD2 1 ATOM 4045 N N . ASN B 2 158 ? -12.472 8.022 8.863 1.00 88.09 ? 158 ASN B N 1 ATOM 4046 C CA . ASN B 2 158 ? -11.381 7.408 8.107 1.00 89.59 ? 158 ASN B CA 1 ATOM 4047 C C . ASN B 2 158 ? -11.577 5.933 7.794 1.00 85.87 ? 158 ASN B C 1 ATOM 4048 O O . ASN B 2 158 ? -11.308 5.482 6.681 1.00 92.25 ? 158 ASN B O 1 ATOM 4049 C CB . ASN B 2 158 ? -10.062 7.571 8.861 1.00 104.93 ? 158 ASN B CB 1 ATOM 4050 C CG . ASN B 2 158 ? -9.515 8.977 8.779 1.00 118.10 ? 158 ASN B CG 1 ATOM 4051 O OD1 . ASN B 2 158 ? -9.853 9.736 7.871 1.00 118.96 ? 158 ASN B OD1 1 ATOM 4052 N ND2 . ASN B 2 158 ? -8.649 9.328 9.722 1.00 124.10 ? 158 ASN B ND2 1 ATOM 4053 N N . LYS B 2 159 ? -12.048 5.184 8.779 1.00 80.73 ? 159 LYS B N 1 ATOM 4054 C CA . LYS B 2 159 ? -12.130 3.741 8.646 1.00 81.50 ? 159 LYS B CA 1 ATOM 4055 C C . LYS B 2 159 ? -13.217 3.290 7.671 1.00 72.00 ? 159 LYS B C 1 ATOM 4056 O O . LYS B 2 159 ? -13.212 2.141 7.238 1.00 69.57 ? 159 LYS B O 1 ATOM 4057 C CB . LYS B 2 159 ? -12.357 3.106 10.018 1.00 87.99 ? 159 LYS B CB 1 ATOM 4058 C CG . LYS B 2 159 ? -11.225 3.363 11.004 1.00 97.30 ? 159 LYS B CG 1 ATOM 4059 C CD . LYS B 2 159 ? -9.904 2.826 10.474 1.00 104.86 ? 159 LYS B CD 1 ATOM 4060 C CE . LYS B 2 159 ? -8.793 2.964 11.502 1.00 112.66 ? 159 LYS B CE 1 ATOM 4061 N NZ . LYS B 2 159 ? -7.512 2.377 11.018 1.00 113.20 ? 159 LYS B NZ 1 ATOM 4062 N N . LEU B 2 160 ? -14.132 4.189 7.314 1.00 65.59 ? 160 LEU B N 1 ATOM 4063 C CA . LEU B 2 160 ? -15.251 3.830 6.439 1.00 62.11 ? 160 LEU B CA 1 ATOM 4064 C C . LEU B 2 160 ? -14.792 3.293 5.090 1.00 63.38 ? 160 LEU B C 1 ATOM 4065 O O . LEU B 2 160 ? -14.024 3.939 4.378 1.00 61.22 ? 160 LEU B O 1 ATOM 4066 C CB . LEU B 2 160 ? -16.182 5.025 6.223 1.00 56.85 ? 160 LEU B CB 1 ATOM 4067 C CG . LEU B 2 160 ? -17.387 4.731 5.322 1.00 53.95 ? 160 LEU B CG 1 ATOM 4068 C CD1 . LEU B 2 160 ? -18.668 5.290 5.918 1.00 52.45 ? 160 LEU B CD1 1 ATOM 4069 C CD2 . LEU B 2 160 ? -17.171 5.287 3.923 1.00 56.42 ? 160 LEU B CD2 1 ATOM 4070 N N . LYS B 2 161 ? -15.279 2.107 4.743 1.00 72.01 ? 161 LYS B N 1 ATOM 4071 C CA . LYS B 2 161 ? -14.924 1.478 3.478 1.00 73.09 ? 161 LYS B CA 1 ATOM 4072 C C . LYS B 2 161 ? -16.152 1.135 2.646 1.00 72.50 ? 161 LYS B C 1 ATOM 4073 O O . LYS B 2 161 ? -16.042 0.871 1.450 1.00 79.33 ? 161 LYS B O 1 ATOM 4074 C CB . LYS B 2 161 ? -14.093 0.217 3.723 1.00 73.55 ? 161 LYS B CB 1 ATOM 4075 C CG . LYS B 2 161 ? -12.700 0.495 4.258 1.00 81.46 ? 161 LYS B CG 1 ATOM 4076 C CD . LYS B 2 161 ? -11.973 1.489 3.367 1.00 95.47 ? 161 LYS B CD 1 ATOM 4077 C CE . LYS B 2 161 ? -10.594 1.822 3.903 1.00 102.16 ? 161 LYS B CE 1 ATOM 4078 N NZ . LYS B 2 161 ? -9.649 0.691 3.727 1.00 108.07 ? 161 LYS B NZ 1 ATOM 4079 N N . VAL B 2 162 ? -17.320 1.137 3.278 1.00 61.59 ? 162 VAL B N 1 ATOM 4080 C CA . VAL B 2 162 ? -18.552 0.813 2.571 1.00 54.35 ? 162 VAL B CA 1 ATOM 4081 C C . VAL B 2 162 ? -19.613 1.878 2.782 1.00 55.84 ? 162 VAL B C 1 ATOM 4082 O O . VAL B 2 162 ? -19.945 2.230 3.913 1.00 63.57 ? 162 VAL B O 1 ATOM 4083 C CB . VAL B 2 162 ? -19.119 -0.548 3.005 1.00 47.97 ? 162 VAL B CB 1 ATOM 4084 C CG1 . VAL B 2 162 ? -20.543 -0.716 2.496 1.00 47.16 ? 162 VAL B CG1 1 ATOM 4085 C CG2 . VAL B 2 162 ? -18.242 -1.665 2.496 1.00 41.69 ? 162 VAL B CG2 1 ATOM 4086 N N . LEU B 2 163 ? -20.140 2.383 1.674 1.00 51.45 ? 163 LEU B N 1 ATOM 4087 C CA . LEU B 2 163 ? -21.176 3.398 1.705 1.00 50.79 ? 163 LEU B CA 1 ATOM 4088 C C . LEU B 2 163 ? -22.333 2.995 0.794 1.00 53.78 ? 163 LEU B C 1 ATOM 4089 O O . LEU B 2 163 ? -22.164 2.864 -0.420 1.00 53.75 ? 163 LEU B O 1 ATOM 4090 C CB . LEU B 2 163 ? -20.599 4.748 1.284 1.00 50.84 ? 163 LEU B CB 1 ATOM 4091 C CG . LEU B 2 163 ? -21.532 5.951 1.375 1.00 54.94 ? 163 LEU B CG 1 ATOM 4092 C CD1 . LEU B 2 163 ? -22.080 6.072 2.781 1.00 56.05 ? 163 LEU B CD1 1 ATOM 4093 C CD2 . LEU B 2 163 ? -20.788 7.211 0.978 1.00 57.83 ? 163 LEU B CD2 1 ATOM 4094 N N . ILE B 2 164 ? -23.506 2.795 1.385 1.00 51.42 ? 164 ILE B N 1 ATOM 4095 C CA . ILE B 2 164 ? -24.677 2.345 0.639 1.00 48.44 ? 164 ILE B CA 1 ATOM 4096 C C . ILE B 2 164 ? -25.816 3.355 0.745 1.00 58.26 ? 164 ILE B C 1 ATOM 4097 O O . ILE B 2 164 ? -26.329 3.606 1.835 1.00 60.27 ? 164 ILE B O 1 ATOM 4098 C CB . ILE B 2 164 ? -25.159 0.972 1.137 1.00 42.46 ? 164 ILE B CB 1 ATOM 4099 C CG1 . ILE B 2 164 ? -24.086 -0.086 0.883 1.00 37.57 ? 164 ILE B CG1 1 ATOM 4100 C CG2 . ILE B 2 164 ? -26.456 0.584 0.457 1.00 48.65 ? 164 ILE B CG2 1 ATOM 4101 C CD1 . ILE B 2 164 ? -24.531 -1.497 1.192 1.00 36.06 ? 164 ILE B CD1 1 ATOM 4102 N N . LEU B 2 165 ? -26.209 3.926 -0.391 1.00 66.12 ? 165 LEU B N 1 ATOM 4103 C CA . LEU B 2 165 ? -27.166 5.028 -0.410 1.00 69.32 ? 165 LEU B CA 1 ATOM 4104 C C . LEU B 2 165 ? -28.243 4.869 -1.482 1.00 71.94 ? 165 LEU B C 1 ATOM 4105 O O . LEU B 2 165 ? -28.845 5.854 -1.911 1.00 75.05 ? 165 LEU B O 1 ATOM 4106 C CB . LEU B 2 165 ? -26.430 6.353 -0.635 1.00 62.62 ? 165 LEU B CB 1 ATOM 4107 C CG . LEU B 2 165 ? -25.267 6.696 0.296 1.00 56.65 ? 165 LEU B CG 1 ATOM 4108 C CD1 . LEU B 2 165 ? -24.456 7.846 -0.262 1.00 59.38 ? 165 LEU B CD1 1 ATOM 4109 C CD2 . LEU B 2 165 ? -25.788 7.039 1.676 1.00 62.20 ? 165 LEU B CD2 1 ATOM 4110 N N . ASN B 2 166 ? -28.488 3.638 -1.913 1.00 70.33 ? 166 ASN B N 1 ATOM 4111 C CA . ASN B 2 166 ? -29.370 3.418 -3.051 1.00 67.66 ? 166 ASN B CA 1 ATOM 4112 C C . ASN B 2 166 ? -30.830 3.759 -2.767 1.00 69.61 ? 166 ASN B C 1 ATOM 4113 O O . ASN B 2 166 ? -31.248 3.845 -1.614 1.00 68.73 ? 166 ASN B O 1 ATOM 4114 C CB . ASN B 2 166 ? -29.259 1.970 -3.540 1.00 67.90 ? 166 ASN B CB 1 ATOM 4115 C CG . ASN B 2 166 ? -29.442 0.954 -2.430 1.00 75.68 ? 166 ASN B CG 1 ATOM 4116 O OD1 . ASN B 2 166 ? -28.476 0.373 -1.935 1.00 78.28 ? 166 ASN B OD1 1 ATOM 4117 N ND2 . ASN B 2 166 ? -30.688 0.717 -2.051 1.00 77.73 ? 166 ASN B ND2 1 ATOM 4118 N N . ASP B 2 167 ? -31.585 3.972 -3.842 1.00 75.98 ? 167 ASP B N 1 ATOM 4119 C CA . ASP B 2 167 ? -33.022 4.232 -3.779 1.00 79.40 ? 167 ASP B CA 1 ATOM 4120 C C . ASP B 2 167 ? -33.367 5.446 -2.918 1.00 84.70 ? 167 ASP B C 1 ATOM 4121 O O . ASP B 2 167 ? -34.282 5.402 -2.096 1.00 94.83 ? 167 ASP B O 1 ATOM 4122 C CB . ASP B 2 167 ? -33.748 2.990 -3.268 1.00 80.54 ? 167 ASP B CB 1 ATOM 4123 C CG . ASP B 2 167 ? -33.248 1.722 -3.926 1.00 85.05 ? 167 ASP B CG 1 ATOM 4124 O OD1 . ASP B 2 167 ? -33.141 1.697 -5.168 1.00 84.80 ? 167 ASP B OD1 1 ATOM 4125 O OD2 . ASP B 2 167 ? -32.937 0.757 -3.202 1.00 95.74 ? 167 ASP B OD2 1 ATOM 4126 N N . ASN B 2 168 ? -32.624 6.530 -3.120 1.00 79.98 ? 168 ASN B N 1 ATOM 4127 C CA . ASN B 2 168 ? -32.894 7.790 -2.439 1.00 73.54 ? 168 ASN B CA 1 ATOM 4128 C C . ASN B 2 168 ? -33.202 8.908 -3.428 1.00 70.76 ? 168 ASN B C 1 ATOM 4129 O O . ASN B 2 168 ? -33.692 8.659 -4.528 1.00 71.74 ? 168 ASN B O 1 ATOM 4130 C CB . ASN B 2 168 ? -31.713 8.192 -1.553 1.00 69.58 ? 168 ASN B CB 1 ATOM 4131 C CG . ASN B 2 168 ? -31.702 7.459 -0.231 1.00 70.66 ? 168 ASN B CG 1 ATOM 4132 O OD1 . ASN B 2 168 ? -32.323 7.898 0.734 1.00 75.84 ? 168 ASN B OD1 1 ATOM 4133 N ND2 . ASN B 2 168 ? -30.994 6.338 -0.178 1.00 69.84 ? 168 ASN B ND2 1 ATOM 4134 N N . LEU B 2 169 ? -32.906 10.140 -3.032 1.00 63.07 ? 169 LEU B N 1 ATOM 4135 C CA . LEU B 2 169 ? -33.305 11.311 -3.803 1.00 71.26 ? 169 LEU B CA 1 ATOM 4136 C C . LEU B 2 169 ? -32.106 12.152 -4.243 1.00 82.97 ? 169 LEU B C 1 ATOM 4137 O O . LEU B 2 169 ? -32.232 13.355 -4.480 1.00 87.19 ? 169 LEU B O 1 ATOM 4138 C CB . LEU B 2 169 ? -34.271 12.171 -2.980 1.00 73.60 ? 169 LEU B CB 1 ATOM 4139 C CG . LEU B 2 169 ? -35.786 11.928 -3.045 1.00 68.85 ? 169 LEU B CG 1 ATOM 4140 C CD1 . LEU B 2 169 ? -36.148 10.452 -2.960 1.00 59.98 ? 169 LEU B CD1 1 ATOM 4141 C CD2 . LEU B 2 169 ? -36.481 12.712 -1.935 1.00 74.60 ? 169 LEU B CD2 1 ATOM 4142 N N . LEU B 2 170 ? -30.945 11.516 -4.354 1.00 83.99 ? 170 LEU B N 1 ATOM 4143 C CA . LEU B 2 170 ? -29.716 12.231 -4.680 1.00 79.30 ? 170 LEU B CA 1 ATOM 4144 C C . LEU B 2 170 ? -29.727 12.776 -6.101 1.00 81.99 ? 170 LEU B C 1 ATOM 4145 O O . LEU B 2 170 ? -29.629 12.021 -7.065 1.00 77.32 ? 170 LEU B O 1 ATOM 4146 C CB . LEU B 2 170 ? -28.497 11.326 -4.487 1.00 73.38 ? 170 LEU B CB 1 ATOM 4147 C CG . LEU B 2 170 ? -27.522 11.762 -3.391 1.00 73.86 ? 170 LEU B CG 1 ATOM 4148 C CD1 . LEU B 2 170 ? -27.355 13.268 -3.419 1.00 85.34 ? 170 LEU B CD1 1 ATOM 4149 C CD2 . LEU B 2 170 ? -27.982 11.307 -2.021 1.00 67.54 ? 170 LEU B CD2 1 ATOM 4150 N N . LEU B 2 171 ? -29.850 14.092 -6.224 1.00 96.19 ? 171 LEU B N 1 ATOM 4151 C CA . LEU B 2 171 ? -29.758 14.743 -7.523 1.00 97.15 ? 171 LEU B CA 1 ATOM 4152 C C . LEU B 2 171 ? -28.304 15.014 -7.866 1.00 87.69 ? 171 LEU B C 1 ATOM 4153 O O . LEU B 2 171 ? -27.865 14.795 -8.994 1.00 87.97 ? 171 LEU B O 1 ATOM 4154 C CB . LEU B 2 171 ? -30.559 16.048 -7.542 1.00 111.79 ? 171 LEU B CB 1 ATOM 4155 C CG . LEU B 2 171 ? -30.941 16.727 -6.220 1.00 124.99 ? 171 LEU B CG 1 ATOM 4156 C CD1 . LEU B 2 171 ? -29.741 17.290 -5.461 1.00 125.87 ? 171 LEU B CD1 1 ATOM 4157 C CD2 . LEU B 2 171 ? -31.962 17.823 -6.483 1.00 128.70 ? 171 LEU B CD2 1 ATOM 4158 N N . SER B 2 172 ? -27.560 15.483 -6.872 1.00 78.33 ? 172 SER B N 1 ATOM 4159 C CA . SER B 2 172 ? -26.170 15.858 -7.053 1.00 76.12 ? 172 SER B CA 1 ATOM 4160 C C . SER B 2 172 ? -25.398 15.650 -5.762 1.00 77.84 ? 172 SER B C 1 ATOM 4161 O O . SER B 2 172 ? -25.961 15.699 -4.668 1.00 84.79 ? 172 SER B O 1 ATOM 4162 C CB . SER B 2 172 ? -26.056 17.314 -7.507 1.00 77.80 ? 172 SER B CB 1 ATOM 4163 O OG . SER B 2 172 ? -26.475 18.205 -6.486 1.00 74.33 ? 172 SER B OG 1 ATOM 4164 N N . LEU B 2 173 ? -24.097 15.437 -5.900 1.00 76.22 ? 173 LEU B N 1 ATOM 4165 C CA . LEU B 2 173 ? -23.244 15.088 -4.776 1.00 74.29 ? 173 LEU B CA 1 ATOM 4166 C C . LEU B 2 173 ? -22.189 16.170 -4.546 1.00 85.70 ? 173 LEU B C 1 ATOM 4167 O O . LEU B 2 173 ? -21.327 16.380 -5.401 1.00 93.05 ? 173 LEU B O 1 ATOM 4168 C CB . LEU B 2 173 ? -22.595 13.731 -5.048 1.00 62.52 ? 173 LEU B CB 1 ATOM 4169 C CG . LEU B 2 173 ? -21.999 12.898 -3.923 1.00 52.17 ? 173 LEU B CG 1 ATOM 4170 C CD1 . LEU B 2 173 ? -22.663 13.225 -2.614 1.00 63.89 ? 173 LEU B CD1 1 ATOM 4171 C CD2 . LEU B 2 173 ? -22.196 11.429 -4.252 1.00 43.99 ? 173 LEU B CD2 1 ATOM 4172 N N . PRO B 2 174 ? -22.264 16.872 -3.399 1.00 91.09 ? 174 PRO B N 1 ATOM 4173 C CA . PRO B 2 174 ? -21.329 17.955 -3.065 1.00 89.40 ? 174 PRO B CA 1 ATOM 4174 C C . PRO B 2 174 ? -19.879 17.526 -3.210 1.00 83.31 ? 174 PRO B C 1 ATOM 4175 O O . PRO B 2 174 ? -19.504 16.479 -2.695 1.00 75.87 ? 174 PRO B O 1 ATOM 4176 C CB . PRO B 2 174 ? -21.657 18.268 -1.599 1.00 93.69 ? 174 PRO B CB 1 ATOM 4177 C CG . PRO B 2 174 ? -22.425 17.081 -1.110 1.00 93.02 ? 174 PRO B CG 1 ATOM 4178 C CD . PRO B 2 174 ? -23.203 16.622 -2.295 1.00 97.37 ? 174 PRO B CD 1 ATOM 4179 N N . SER B 2 175 ? -19.082 18.324 -3.911 1.00 91.86 ? 175 SER B N 1 ATOM 4180 C CA . SER B 2 175 ? -17.701 17.959 -4.204 1.00 96.16 ? 175 SER B CA 1 ATOM 4181 C C . SER B 2 175 ? -16.871 17.834 -2.933 1.00 86.66 ? 175 SER B C 1 ATOM 4182 O O . SER B 2 175 ? -17.159 18.480 -1.924 1.00 75.97 ? 175 SER B O 1 ATOM 4183 C CB . SER B 2 175 ? -17.066 18.983 -5.146 1.00 102.87 ? 175 SER B CB 1 ATOM 4184 O OG . SER B 2 175 ? -16.952 20.247 -4.520 1.00 107.35 ? 175 SER B OG 1 ATOM 4185 N N . ASN B 2 176 ? -15.845 16.988 -3.005 1.00 87.52 ? 176 ASN B N 1 ATOM 4186 C CA . ASN B 2 176 ? -14.962 16.691 -1.879 1.00 85.21 ? 176 ASN B CA 1 ATOM 4187 C C . ASN B 2 176 ? -15.679 16.024 -0.708 1.00 86.83 ? 176 ASN B C 1 ATOM 4188 O O . ASN B 2 176 ? -15.263 16.166 0.439 1.00 88.77 ? 176 ASN B O 1 ATOM 4189 C CB . ASN B 2 176 ? -14.252 17.964 -1.400 1.00 82.20 ? 176 ASN B CB 1 ATOM 4190 C CG . ASN B 2 176 ? -13.050 18.318 -2.257 1.00 89.08 ? 176 ASN B CG 1 ATOM 4191 O OD1 . ASN B 2 176 ? -11.908 18.039 -1.891 1.00 90.04 ? 176 ASN B OD1 1 ATOM 4192 N ND2 . ASN B 2 176 ? -13.303 18.929 -3.408 1.00 94.94 ? 176 ASN B ND2 1 ATOM 4193 N N . VAL B 2 177 ? -16.750 15.290 -0.995 1.00 81.22 ? 177 VAL B N 1 ATOM 4194 C CA . VAL B 2 177 ? -17.375 14.469 0.033 1.00 71.06 ? 177 VAL B CA 1 ATOM 4195 C C . VAL B 2 177 ? -16.460 13.309 0.374 1.00 72.16 ? 177 VAL B C 1 ATOM 4196 O O . VAL B 2 177 ? -16.251 12.989 1.545 1.00 74.73 ? 177 VAL B O 1 ATOM 4197 C CB . VAL B 2 177 ? -18.746 13.910 -0.401 1.00 63.31 ? 177 VAL B CB 1 ATOM 4198 C CG1 . VAL B 2 177 ? -19.856 14.873 -0.033 1.00 74.70 ? 177 VAL B CG1 1 ATOM 4199 C CG2 . VAL B 2 177 ? -18.755 13.586 -1.888 1.00 58.04 ? 177 VAL B CG2 1 ATOM 4200 N N . PHE B 2 178 ? -15.901 12.697 -0.664 1.00 72.70 ? 178 PHE B N 1 ATOM 4201 C CA . PHE B 2 178 ? -15.120 11.476 -0.520 1.00 74.52 ? 178 PHE B CA 1 ATOM 4202 C C . PHE B 2 178 ? -13.620 11.736 -0.475 1.00 84.33 ? 178 PHE B C 1 ATOM 4203 O O . PHE B 2 178 ? -12.828 10.808 -0.620 1.00 93.81 ? 178 PHE B O 1 ATOM 4204 C CB . PHE B 2 178 ? -15.416 10.514 -1.675 1.00 67.83 ? 178 PHE B CB 1 ATOM 4205 C CG . PHE B 2 178 ? -16.873 10.187 -1.846 1.00 65.52 ? 178 PHE B CG 1 ATOM 4206 C CD1 . PHE B 2 178 ? -17.704 10.054 -0.748 1.00 74.87 ? 178 PHE B CD1 1 ATOM 4207 C CD2 . PHE B 2 178 ? -17.411 10.015 -3.111 1.00 65.89 ? 178 PHE B CD2 1 ATOM 4208 C CE1 . PHE B 2 178 ? -19.043 9.752 -0.909 1.00 80.39 ? 178 PHE B CE1 1 ATOM 4209 C CE2 . PHE B 2 178 ? -18.747 9.713 -3.278 1.00 69.70 ? 178 PHE B CE2 1 ATOM 4210 C CZ . PHE B 2 178 ? -19.565 9.582 -2.175 1.00 78.74 ? 178 PHE B CZ 1 ATOM 4211 N N . ARG B 2 179 ? -13.223 12.987 -0.285 1.00 82.88 ? 179 ARG B N 1 ATOM 4212 C CA . ARG B 2 179 ? -11.809 13.320 -0.384 1.00 88.49 ? 179 ARG B CA 1 ATOM 4213 C C . ARG B 2 179 ? -11.003 12.807 0.804 1.00 86.89 ? 179 ARG B C 1 ATOM 4214 O O . ARG B 2 179 ? -9.799 12.581 0.691 1.00 89.09 ? 179 ARG B O 1 ATOM 4215 C CB . ARG B 2 179 ? -11.632 14.828 -0.525 1.00 107.25 ? 179 ARG B CB 1 ATOM 4216 C CG . ARG B 2 179 ? -12.139 15.629 0.633 1.00 128.91 ? 179 ARG B CG 1 ATOM 4217 C CD . ARG B 2 179 ? -10.977 16.159 1.435 1.00 143.86 ? 179 ARG B CD 1 ATOM 4218 N NE . ARG B 2 179 ? -11.372 17.275 2.280 1.00 153.34 ? 179 ARG B NE 1 ATOM 4219 C CZ . ARG B 2 179 ? -11.025 18.538 2.057 1.00 161.49 ? 179 ARG B CZ 1 ATOM 4220 N NH1 . ARG B 2 179 ? -10.268 18.846 1.010 1.00 166.01 ? 179 ARG B NH1 1 ATOM 4221 N NH2 . ARG B 2 179 ? -11.429 19.495 2.884 1.00 162.37 ? 179 ARG B NH2 1 ATOM 4222 N N . PHE B 2 180 ? -11.669 12.612 1.937 1.00 81.15 ? 180 PHE B N 1 ATOM 4223 C CA . PHE B 2 180 ? -10.969 12.250 3.166 1.00 81.57 ? 180 PHE B CA 1 ATOM 4224 C C . PHE B 2 180 ? -11.047 10.762 3.487 1.00 79.95 ? 180 PHE B C 1 ATOM 4225 O O . PHE B 2 180 ? -10.323 10.266 4.352 1.00 81.33 ? 180 PHE B O 1 ATOM 4226 C CB . PHE B 2 180 ? -11.511 13.070 4.334 1.00 81.22 ? 180 PHE B CB 1 ATOM 4227 C CG . PHE B 2 180 ? -10.808 14.379 4.515 1.00 80.74 ? 180 PHE B CG 1 ATOM 4228 C CD1 . PHE B 2 180 ? -9.490 14.524 4.115 1.00 75.30 ? 180 PHE B CD1 1 ATOM 4229 C CD2 . PHE B 2 180 ? -11.459 15.463 5.075 1.00 91.74 ? 180 PHE B CD2 1 ATOM 4230 C CE1 . PHE B 2 180 ? -8.832 15.725 4.274 1.00 81.52 ? 180 PHE B CE1 1 ATOM 4231 C CE2 . PHE B 2 180 ? -10.805 16.668 5.240 1.00 95.09 ? 180 PHE B CE2 1 ATOM 4232 C CZ . PHE B 2 180 ? -9.490 16.800 4.836 1.00 91.59 ? 180 PHE B CZ 1 ATOM 4233 N N . VAL B 2 181 ? -11.920 10.051 2.786 1.00 77.07 ? 181 VAL B N 1 ATOM 4234 C CA . VAL B 2 181 ? -11.993 8.604 2.922 1.00 75.87 ? 181 VAL B CA 1 ATOM 4235 C C . VAL B 2 181 ? -11.554 7.927 1.631 1.00 88.12 ? 181 VAL B C 1 ATOM 4236 O O . VAL B 2 181 ? -11.519 8.552 0.571 1.00 94.17 ? 181 VAL B O 1 ATOM 4237 C CB . VAL B 2 181 ? -13.416 8.134 3.275 1.00 64.51 ? 181 VAL B CB 1 ATOM 4238 C CG1 . VAL B 2 181 ? -13.939 8.892 4.482 1.00 72.34 ? 181 VAL B CG1 1 ATOM 4239 C CG2 . VAL B 2 181 ? -14.346 8.320 2.086 1.00 53.06 ? 181 VAL B CG2 1 ATOM 4240 N N . LEU B 2 182 ? -11.203 6.651 1.724 1.00 93.62 ? 182 LEU B N 1 ATOM 4241 C CA . LEU B 2 182 ? -11.019 5.840 0.530 1.00 95.92 ? 182 LEU B CA 1 ATOM 4242 C C . LEU B 2 182 ? -11.824 4.560 0.650 1.00 95.03 ? 182 LEU B C 1 ATOM 4243 O O . LEU B 2 182 ? -11.286 3.505 0.969 1.00 99.38 ? 182 LEU B O 1 ATOM 4244 C CB . LEU B 2 182 ? -9.543 5.514 0.277 1.00 103.21 ? 182 LEU B CB 1 ATOM 4245 C CG . LEU B 2 182 ? -8.455 5.464 1.353 1.00 115.07 ? 182 LEU B CG 1 ATOM 4246 C CD1 . LEU B 2 182 ? -8.840 4.646 2.576 1.00 117.20 ? 182 LEU B CD1 1 ATOM 4247 C CD2 . LEU B 2 182 ? -7.188 4.904 0.718 1.00 121.76 ? 182 LEU B CD2 1 ATOM 4248 N N . LEU B 2 183 ? -13.122 4.664 0.399 1.00 81.54 ? 183 LEU B N 1 ATOM 4249 C CA . LEU B 2 183 ? -13.992 3.499 0.447 1.00 73.95 ? 183 LEU B CA 1 ATOM 4250 C C . LEU B 2 183 ? -13.716 2.579 -0.736 1.00 69.49 ? 183 LEU B C 1 ATOM 4251 O O . LEU B 2 183 ? -13.046 2.969 -1.692 1.00 68.81 ? 183 LEU B O 1 ATOM 4252 C CB . LEU B 2 183 ? -15.460 3.924 0.471 1.00 72.77 ? 183 LEU B CB 1 ATOM 4253 C CG . LEU B 2 183 ? -15.777 5.310 -0.091 1.00 76.56 ? 183 LEU B CG 1 ATOM 4254 C CD1 . LEU B 2 183 ? -15.528 5.377 -1.592 1.00 82.15 ? 183 LEU B CD1 1 ATOM 4255 C CD2 . LEU B 2 183 ? -17.212 5.687 0.236 1.00 76.11 ? 183 LEU B CD2 1 ATOM 4256 N N . THR B 2 184 ? -14.224 1.354 -0.657 1.00 68.69 ? 184 THR B N 1 ATOM 4257 C CA . THR B 2 184 ? -14.002 0.363 -1.700 1.00 74.72 ? 184 THR B CA 1 ATOM 4258 C C . THR B 2 184 ? -15.319 -0.046 -2.355 1.00 80.34 ? 184 THR B C 1 ATOM 4259 O O . THR B 2 184 ? -15.338 -0.502 -3.498 1.00 84.63 ? 184 THR B O 1 ATOM 4260 C CB . THR B 2 184 ? -13.294 -0.884 -1.145 1.00 76.80 ? 184 THR B CB 1 ATOM 4261 O OG1 . THR B 2 184 ? -14.148 -1.543 -0.201 1.00 68.95 ? 184 THR B OG1 1 ATOM 4262 C CG2 . THR B 2 184 ? -11.991 -0.491 -0.460 1.00 83.81 ? 184 THR B CG2 1 ATOM 4263 N N . HIS B 2 185 ? -16.415 0.122 -1.622 1.00 78.74 ? 185 HIS B N 1 ATOM 4264 C CA . HIS B 2 185 ? -17.744 -0.163 -2.147 1.00 68.77 ? 185 HIS B CA 1 ATOM 4265 C C . HIS B 2 185 ? -18.652 1.049 -1.992 1.00 61.20 ? 185 HIS B C 1 ATOM 4266 O O . HIS B 2 185 ? -18.845 1.559 -0.889 1.00 58.36 ? 185 HIS B O 1 ATOM 4267 C CB . HIS B 2 185 ? -18.359 -1.378 -1.446 1.00 69.83 ? 185 HIS B CB 1 ATOM 4268 C CG . HIS B 2 185 ? -17.652 -2.666 -1.738 1.00 83.56 ? 185 HIS B CG 1 ATOM 4269 N ND1 . HIS B 2 185 ? -18.069 -3.539 -2.720 1.00 87.83 ? 185 HIS B ND1 1 ATOM 4270 C CD2 . HIS B 2 185 ? -16.554 -3.227 -1.178 1.00 87.45 ? 185 HIS B CD2 1 ATOM 4271 C CE1 . HIS B 2 185 ? -17.259 -4.582 -2.753 1.00 82.13 ? 185 HIS B CE1 1 ATOM 4272 N NE2 . HIS B 2 185 ? -16.331 -4.417 -1.827 1.00 84.75 ? 185 HIS B NE2 1 ATOM 4273 N N . LEU B 2 186 ? -19.197 1.514 -3.108 1.00 63.70 ? 186 LEU B N 1 ATOM 4274 C CA . LEU B 2 186 ? -20.150 2.612 -3.090 1.00 59.91 ? 186 LEU B CA 1 ATOM 4275 C C . LEU B 2 186 ? -21.366 2.255 -3.931 1.00 61.96 ? 186 LEU B C 1 ATOM 4276 O O . LEU B 2 186 ? -21.244 1.967 -5.120 1.00 65.68 ? 186 LEU B O 1 ATOM 4277 C CB . LEU B 2 186 ? -19.510 3.901 -3.604 1.00 58.79 ? 186 LEU B CB 1 ATOM 4278 C CG . LEU B 2 186 ? -20.456 5.094 -3.736 1.00 53.06 ? 186 LEU B CG 1 ATOM 4279 C CD1 . LEU B 2 186 ? -21.032 5.469 -2.385 1.00 49.96 ? 186 LEU B CD1 1 ATOM 4280 C CD2 . LEU B 2 186 ? -19.742 6.276 -4.354 1.00 55.95 ? 186 LEU B CD2 1 ATOM 4281 N N . ASP B 2 187 ? -22.537 2.263 -3.304 1.00 63.00 ? 187 ASP B N 1 ATOM 4282 C CA . ASP B 2 187 ? -23.781 1.950 -3.996 1.00 69.20 ? 187 ASP B CA 1 ATOM 4283 C C . ASP B 2 187 ? -24.624 3.207 -4.143 1.00 67.34 ? 187 ASP B C 1 ATOM 4284 O O . ASP B 2 187 ? -25.095 3.765 -3.152 1.00 67.66 ? 187 ASP B O 1 ATOM 4285 C CB . ASP B 2 187 ? -24.563 0.872 -3.239 1.00 79.81 ? 187 ASP B CB 1 ATOM 4286 C CG . ASP B 2 187 ? -25.761 0.351 -4.020 1.00 86.19 ? 187 ASP B CG 1 ATOM 4287 O OD1 . ASP B 2 187 ? -26.121 0.945 -5.058 1.00 93.03 ? 187 ASP B OD1 1 ATOM 4288 O OD2 . ASP B 2 187 ? -26.353 -0.660 -3.584 1.00 83.44 ? 187 ASP B OD2 1 ATOM 4289 N N . LEU B 2 188 ? -24.815 3.649 -5.382 1.00 64.19 ? 188 LEU B N 1 ATOM 4290 C CA . LEU B 2 188 ? -25.615 4.839 -5.647 1.00 64.01 ? 188 LEU B CA 1 ATOM 4291 C C . LEU B 2 188 ? -26.788 4.538 -6.575 1.00 62.36 ? 188 LEU B C 1 ATOM 4292 O O . LEU B 2 188 ? -27.371 5.454 -7.154 1.00 64.27 ? 188 LEU B O 1 ATOM 4293 C CB . LEU B 2 188 ? -24.750 5.951 -6.247 1.00 66.40 ? 188 LEU B CB 1 ATOM 4294 C CG . LEU B 2 188 ? -23.641 6.555 -5.381 1.00 68.06 ? 188 LEU B CG 1 ATOM 4295 C CD1 . LEU B 2 188 ? -22.915 7.647 -6.145 1.00 68.53 ? 188 LEU B CD1 1 ATOM 4296 C CD2 . LEU B 2 188 ? -24.196 7.101 -4.078 1.00 69.14 ? 188 LEU B CD2 1 ATOM 4297 N N . ARG B 2 189 ? -27.132 3.258 -6.702 1.00 67.79 ? 189 ARG B N 1 ATOM 4298 C CA . ARG B 2 189 ? -28.253 2.827 -7.540 1.00 66.40 ? 189 ARG B CA 1 ATOM 4299 C C . ARG B 2 189 ? -29.557 3.517 -7.156 1.00 75.63 ? 189 ARG B C 1 ATOM 4300 O O . ARG B 2 189 ? -29.671 4.088 -6.076 1.00 75.47 ? 189 ARG B O 1 ATOM 4301 C CB . ARG B 2 189 ? -28.444 1.310 -7.447 1.00 60.32 ? 189 ARG B CB 1 ATOM 4302 C CG . ARG B 2 189 ? -27.313 0.489 -8.024 1.00 58.10 ? 189 ARG B CG 1 ATOM 4303 C CD . ARG B 2 189 ? -27.599 -1.006 -7.931 1.00 63.35 ? 189 ARG B CD 1 ATOM 4304 N NE . ARG B 2 189 ? -27.505 -1.521 -6.567 1.00 68.11 ? 189 ARG B NE 1 ATOM 4305 C CZ . ARG B 2 189 ? -27.653 -2.802 -6.242 1.00 69.05 ? 189 ARG B CZ 1 ATOM 4306 N NH1 . ARG B 2 189 ? -27.902 -3.702 -7.184 1.00 68.97 ? 189 ARG B NH1 1 ATOM 4307 N NH2 . ARG B 2 189 ? -27.550 -3.186 -4.976 1.00 66.25 ? 189 ARG B NH2 1 ATOM 4308 N N . GLY B 2 190 ? -30.535 3.470 -8.053 1.00 90.33 ? 190 GLY B N 1 ATOM 4309 C CA . GLY B 2 190 ? -31.876 3.935 -7.748 1.00 93.25 ? 190 GLY B CA 1 ATOM 4310 C C . GLY B 2 190 ? -32.029 5.371 -7.277 1.00 91.74 ? 190 GLY B C 1 ATOM 4311 O O . GLY B 2 190 ? -33.094 5.748 -6.786 1.00 101.99 ? 190 GLY B O 1 ATOM 4312 N N . ASN B 2 191 ? -30.980 6.175 -7.411 1.00 72.20 ? 191 ASN B N 1 ATOM 4313 C CA . ASN B 2 191 ? -31.071 7.582 -7.043 1.00 69.86 ? 191 ASN B CA 1 ATOM 4314 C C . ASN B 2 191 ? -31.522 8.441 -8.215 1.00 66.20 ? 191 ASN B C 1 ATOM 4315 O O . ASN B 2 191 ? -31.932 7.925 -9.251 1.00 66.49 ? 191 ASN B O 1 ATOM 4316 C CB . ASN B 2 191 ? -29.737 8.092 -6.502 1.00 73.79 ? 191 ASN B CB 1 ATOM 4317 C CG . ASN B 2 191 ? -29.611 7.904 -5.008 1.00 73.71 ? 191 ASN B CG 1 ATOM 4318 O OD1 . ASN B 2 191 ? -30.180 8.667 -4.230 1.00 69.11 ? 191 ASN B OD1 1 ATOM 4319 N ND2 . ASN B 2 191 ? -28.868 6.885 -4.598 1.00 76.52 ? 191 ASN B ND2 1 ATOM 4320 N N . ARG B 2 192 ? -31.442 9.755 -8.046 1.00 70.07 ? 192 ARG B N 1 ATOM 4321 C CA . ARG B 2 192 ? -31.924 10.674 -9.064 1.00 76.46 ? 192 ARG B CA 1 ATOM 4322 C C . ARG B 2 192 ? -30.767 11.432 -9.710 1.00 81.83 ? 192 ARG B C 1 ATOM 4323 O O . ARG B 2 192 ? -30.806 12.655 -9.856 1.00 93.45 ? 192 ARG B O 1 ATOM 4324 C CB . ARG B 2 192 ? -32.934 11.643 -8.457 1.00 82.85 ? 192 ARG B CB 1 ATOM 4325 C CG . ARG B 2 192 ? -33.989 12.108 -9.435 1.00 101.07 ? 192 ARG B CG 1 ATOM 4326 C CD . ARG B 2 192 ? -34.805 13.250 -8.865 1.00 115.09 ? 192 ARG B CD 1 ATOM 4327 N NE . ARG B 2 192 ? -35.252 14.157 -9.916 1.00 125.31 ? 192 ARG B NE 1 ATOM 4328 C CZ . ARG B 2 192 ? -34.551 15.202 -10.346 1.00 130.22 ? 192 ARG B CZ 1 ATOM 4329 N NH1 . ARG B 2 192 ? -33.369 15.476 -9.812 1.00 127.64 ? 192 ARG B NH1 1 ATOM 4330 N NH2 . ARG B 2 192 ? -35.030 15.976 -11.310 1.00 135.95 ? 192 ARG B NH2 1 ATOM 4331 N N . LEU B 2 193 ? -29.734 10.691 -10.092 1.00 77.59 ? 193 LEU B N 1 ATOM 4332 C CA . LEU B 2 193 ? -28.534 11.280 -10.672 1.00 79.86 ? 193 LEU B CA 1 ATOM 4333 C C . LEU B 2 193 ? -28.584 11.296 -12.193 1.00 90.93 ? 193 LEU B C 1 ATOM 4334 O O . LEU B 2 193 ? -28.885 10.284 -12.826 1.00 95.20 ? 193 LEU B O 1 ATOM 4335 C CB . LEU B 2 193 ? -27.296 10.517 -10.208 1.00 70.00 ? 193 LEU B CB 1 ATOM 4336 C CG . LEU B 2 193 ? -27.008 10.568 -8.712 1.00 68.49 ? 193 LEU B CG 1 ATOM 4337 C CD1 . LEU B 2 193 ? -26.181 9.366 -8.312 1.00 67.63 ? 193 LEU B CD1 1 ATOM 4338 C CD2 . LEU B 2 193 ? -26.288 11.859 -8.361 1.00 71.40 ? 193 LEU B CD2 1 ATOM 4339 N N . LYS B 2 194 ? -28.274 12.446 -12.780 1.00 93.30 ? 194 LYS B N 1 ATOM 4340 C CA . LYS B 2 194 ? -28.250 12.567 -14.231 1.00 97.13 ? 194 LYS B CA 1 ATOM 4341 C C . LYS B 2 194 ? -26.828 12.744 -14.753 1.00 96.06 ? 194 LYS B C 1 ATOM 4342 O O . LYS B 2 194 ? -26.519 12.338 -15.870 1.00 93.69 ? 194 LYS B O 1 ATOM 4343 C CB . LYS B 2 194 ? -29.133 13.732 -14.681 1.00 102.50 ? 194 LYS B CB 1 ATOM 4344 C CG . LYS B 2 194 ? -28.905 15.017 -13.907 1.00 115.78 ? 194 LYS B CG 1 ATOM 4345 C CD . LYS B 2 194 ? -29.832 16.119 -14.391 1.00 126.48 ? 194 LYS B CD 1 ATOM 4346 C CE . LYS B 2 194 ? -29.590 17.419 -13.638 1.00 132.26 ? 194 LYS B CE 1 ATOM 4347 N NZ . LYS B 2 194 ? -28.215 17.948 -13.857 1.00 135.11 ? 194 LYS B NZ 1 ATOM 4348 N N . VAL B 2 195 ? -25.969 13.356 -13.942 1.00 100.48 ? 195 VAL B N 1 ATOM 4349 C CA . VAL B 2 195 ? -24.583 13.632 -14.324 1.00 99.92 ? 195 VAL B CA 1 ATOM 4350 C C . VAL B 2 195 ? -23.672 13.451 -13.103 1.00 97.00 ? 195 VAL B C 1 ATOM 4351 O O . VAL B 2 195 ? -24.120 13.606 -11.964 1.00 97.00 ? 195 VAL B O 1 ATOM 4352 C CB . VAL B 2 195 ? -24.427 15.073 -14.904 1.00 112.21 ? 195 VAL B CB 1 ATOM 4353 C CG1 . VAL B 2 195 ? -22.989 15.362 -15.316 1.00 113.83 ? 195 VAL B CG1 1 ATOM 4354 C CG2 . VAL B 2 195 ? -25.358 15.290 -16.092 1.00 114.22 ? 195 VAL B CG2 1 ATOM 4355 N N . MET B 2 196 ? -22.406 13.108 -13.334 1.00 93.59 ? 196 MET B N 1 ATOM 4356 C CA . MET B 2 196 ? -21.438 12.985 -12.248 1.00 83.78 ? 196 MET B CA 1 ATOM 4357 C C . MET B 2 196 ? -20.054 13.489 -12.671 1.00 86.97 ? 196 MET B C 1 ATOM 4358 O O . MET B 2 196 ? -19.388 12.860 -13.493 1.00 89.44 ? 196 MET B O 1 ATOM 4359 C CB . MET B 2 196 ? -21.359 11.535 -11.778 1.00 74.64 ? 196 MET B CB 1 ATOM 4360 C CG . MET B 2 196 ? -20.682 11.362 -10.439 1.00 74.23 ? 196 MET B CG 1 ATOM 4361 S SD . MET B 2 196 ? -21.082 9.777 -9.692 1.00 92.05 ? 196 MET B SD 1 ATOM 4362 C CE . MET B 2 196 ? -22.781 10.059 -9.217 1.00 116.24 ? 196 MET B CE 1 ATOM 4363 N N . PRO B 2 197 ? -19.617 14.623 -12.095 1.00 87.57 ? 197 PRO B N 1 ATOM 4364 C CA . PRO B 2 197 ? -18.416 15.359 -12.513 1.00 87.09 ? 197 PRO B CA 1 ATOM 4365 C C . PRO B 2 197 ? -17.110 14.748 -12.011 1.00 83.79 ? 197 PRO B C 1 ATOM 4366 O O . PRO B 2 197 ? -17.097 14.128 -10.947 1.00 78.53 ? 197 PRO B O 1 ATOM 4367 C CB . PRO B 2 197 ? -18.631 16.735 -11.886 1.00 91.22 ? 197 PRO B CB 1 ATOM 4368 C CG . PRO B 2 197 ? -19.361 16.432 -10.622 1.00 90.15 ? 197 PRO B CG 1 ATOM 4369 C CD . PRO B 2 197 ? -20.274 15.269 -10.942 1.00 90.68 ? 197 PRO B CD 1 ATOM 4370 N N . PHE B 2 198 ? -16.023 14.931 -12.759 1.00 91.21 ? 198 PHE B N 1 ATOM 4371 C CA . PHE B 2 198 ? -14.729 14.406 -12.332 1.00 92.29 ? 198 PHE B CA 1 ATOM 4372 C C . PHE B 2 198 ? -14.124 15.255 -11.225 1.00 100.21 ? 198 PHE B C 1 ATOM 4373 O O . PHE B 2 198 ? -13.613 14.728 -10.237 1.00 95.84 ? 198 PHE B O 1 ATOM 4374 C CB . PHE B 2 198 ? -13.742 14.313 -13.498 1.00 90.21 ? 198 PHE B CB 1 ATOM 4375 C CG . PHE B 2 198 ? -12.421 13.700 -13.115 1.00 85.74 ? 198 PHE B CG 1 ATOM 4376 C CD1 . PHE B 2 198 ? -12.226 12.331 -13.204 1.00 84.05 ? 198 PHE B CD1 1 ATOM 4377 C CD2 . PHE B 2 198 ? -11.379 14.491 -12.650 1.00 83.47 ? 198 PHE B CD2 1 ATOM 4378 C CE1 . PHE B 2 198 ? -11.017 11.762 -12.846 1.00 85.66 ? 198 PHE B CE1 1 ATOM 4379 C CE2 . PHE B 2 198 ? -10.170 13.929 -12.285 1.00 82.72 ? 198 PHE B CE2 1 ATOM 4380 C CZ . PHE B 2 198 ? -9.988 12.564 -12.386 1.00 85.08 ? 198 PHE B CZ 1 ATOM 4381 N N . ALA B 2 199 ? -14.177 16.571 -11.404 1.00 113.19 ? 199 ALA B N 1 ATOM 4382 C CA . ALA B 2 199 ? -13.556 17.503 -10.471 1.00 117.39 ? 199 ALA B CA 1 ATOM 4383 C C . ALA B 2 199 ? -14.237 17.480 -9.112 1.00 117.76 ? 199 ALA B C 1 ATOM 4384 O O . ALA B 2 199 ? -15.347 17.986 -8.947 1.00 118.67 ? 199 ALA B O 1 ATOM 4385 C CB . ALA B 2 199 ? -13.574 18.910 -11.038 1.00 120.86 ? 199 ALA B CB 1 ATOM 4386 N N . GLY B 2 200 ? -13.558 16.896 -8.134 1.00 108.16 ? 200 GLY B N 1 ATOM 4387 C CA . GLY B 2 200 ? -14.109 16.814 -6.800 1.00 107.12 ? 200 GLY B CA 1 ATOM 4388 C C . GLY B 2 200 ? -14.643 15.428 -6.538 1.00 109.54 ? 200 GLY B C 1 ATOM 4389 O O . GLY B 2 200 ? -13.940 14.588 -5.985 1.00 120.95 ? 200 GLY B O 1 ATOM 4390 N N . VAL B 2 201 ? -15.878 15.185 -6.956 1.00 97.24 ? 201 VAL B N 1 ATOM 4391 C CA . VAL B 2 201 ? -16.543 13.937 -6.633 1.00 87.21 ? 201 VAL B CA 1 ATOM 4392 C C . VAL B 2 201 ? -15.744 12.720 -7.086 1.00 82.97 ? 201 VAL B C 1 ATOM 4393 O O . VAL B 2 201 ? -15.534 11.799 -6.306 1.00 83.41 ? 201 VAL B O 1 ATOM 4394 C CB . VAL B 2 201 ? -17.939 13.879 -7.255 1.00 82.30 ? 201 VAL B CB 1 ATOM 4395 C CG1 . VAL B 2 201 ? -18.667 12.637 -6.783 1.00 82.15 ? 201 VAL B CG1 1 ATOM 4396 C CG2 . VAL B 2 201 ? -18.724 15.124 -6.876 1.00 87.44 ? 201 VAL B CG2 1 ATOM 4397 N N . LEU B 2 202 ? -15.260 12.744 -8.324 1.00 78.09 ? 202 LEU B N 1 ATOM 4398 C CA . LEU B 2 202 ? -14.725 11.540 -8.952 1.00 75.38 ? 202 LEU B CA 1 ATOM 4399 C C . LEU B 2 202 ? -13.246 11.256 -8.687 1.00 75.73 ? 202 LEU B C 1 ATOM 4400 O O . LEU B 2 202 ? -12.849 10.096 -8.579 1.00 76.30 ? 202 LEU B O 1 ATOM 4401 C CB . LEU B 2 202 ? -14.952 11.608 -10.462 1.00 76.75 ? 202 LEU B CB 1 ATOM 4402 C CG . LEU B 2 202 ? -15.789 10.492 -11.089 1.00 76.46 ? 202 LEU B CG 1 ATOM 4403 C CD1 . LEU B 2 202 ? -15.686 9.223 -10.263 1.00 78.97 ? 202 LEU B CD1 1 ATOM 4404 C CD2 . LEU B 2 202 ? -17.243 10.930 -11.278 1.00 69.70 ? 202 LEU B CD2 1 ATOM 4405 N N . GLU B 2 203 ? -12.434 12.304 -8.579 1.00 76.97 ? 203 GLU B N 1 ATOM 4406 C CA . GLU B 2 203 ? -10.985 12.127 -8.485 1.00 84.18 ? 203 GLU B CA 1 ATOM 4407 C C . GLU B 2 203 ? -10.584 11.369 -7.223 1.00 92.44 ? 203 GLU B C 1 ATOM 4408 O O . GLU B 2 203 ? -9.501 10.783 -7.157 1.00 97.00 ? 203 GLU B O 1 ATOM 4409 C CB . GLU B 2 203 ? -10.275 13.479 -8.533 1.00 83.20 ? 203 GLU B CB 1 ATOM 4410 C CG . GLU B 2 203 ? -10.739 14.463 -7.485 1.00 79.67 ? 203 GLU B CG 1 ATOM 4411 C CD . GLU B 2 203 ? -10.062 15.809 -7.624 1.00 85.61 ? 203 GLU B CD 1 ATOM 4412 O OE1 . GLU B 2 203 ? -10.726 16.833 -7.360 1.00 83.47 ? 203 GLU B OE1 1 ATOM 4413 O OE2 . GLU B 2 203 ? -8.871 15.842 -8.004 1.00 91.51 ? 203 GLU B OE2 1 ATOM 4414 N N . HIS B 2 204 ? -11.474 11.371 -6.235 1.00 96.32 ? 204 HIS B N 1 ATOM 4415 C CA . HIS B 2 204 ? -11.261 10.660 -4.979 1.00 97.32 ? 204 HIS B CA 1 ATOM 4416 C C . HIS B 2 204 ? -11.615 9.184 -5.125 1.00 101.39 ? 204 HIS B C 1 ATOM 4417 O O . HIS B 2 204 ? -10.968 8.311 -4.547 1.00 103.64 ? 204 HIS B O 1 ATOM 4418 C CB . HIS B 2 204 ? -12.088 11.309 -3.872 1.00 90.28 ? 204 HIS B CB 1 ATOM 4419 C CG . HIS B 2 204 ? -11.922 12.792 -3.802 1.00 87.04 ? 204 HIS B CG 1 ATOM 4420 N ND1 . HIS B 2 204 ? -12.967 13.651 -3.537 1.00 89.85 ? 204 HIS B ND1 1 ATOM 4421 C CD2 . HIS B 2 204 ? -10.830 13.572 -3.985 1.00 84.19 ? 204 HIS B CD2 1 ATOM 4422 C CE1 . HIS B 2 204 ? -12.522 14.895 -3.550 1.00 88.58 ? 204 HIS B CE1 1 ATOM 4423 N NE2 . HIS B 2 204 ? -11.228 14.875 -3.818 1.00 85.31 ? 204 HIS B NE2 1 ATOM 4424 N N . ILE B 2 205 ? -12.656 8.921 -5.905 1.00 100.29 ? 205 ILE B N 1 ATOM 4425 C CA . ILE B 2 205 ? -13.019 7.568 -6.301 1.00 93.93 ? 205 ILE B CA 1 ATOM 4426 C C . ILE B 2 205 ? -11.968 7.067 -7.294 1.00 103.03 ? 205 ILE B C 1 ATOM 4427 O O . ILE B 2 205 ? -11.166 7.852 -7.797 1.00 113.70 ? 205 ILE B O 1 ATOM 4428 C CB . ILE B 2 205 ? -14.434 7.545 -6.915 1.00 88.83 ? 205 ILE B CB 1 ATOM 4429 C CG1 . ILE B 2 205 ? -15.406 8.274 -5.998 1.00 90.67 ? 205 ILE B CG1 1 ATOM 4430 C CG2 . ILE B 2 205 ? -14.954 6.147 -7.067 1.00 86.02 ? 205 ILE B CG2 1 ATOM 4431 C CD1 . ILE B 2 205 ? -15.741 7.482 -4.751 1.00 94.61 ? 205 ILE B CD1 1 ATOM 4432 N N . GLY B 2 206 ? -11.957 5.771 -7.569 1.00 102.86 ? 206 GLY B N 1 ATOM 4433 C CA . GLY B 2 206 ? -10.963 5.207 -8.458 1.00 107.21 ? 206 GLY B CA 1 ATOM 4434 C C . GLY B 2 206 ? -10.200 4.159 -7.687 1.00 111.85 ? 206 GLY B C 1 ATOM 4435 O O . GLY B 2 206 ? -9.657 3.212 -8.256 1.00 116.85 ? 206 GLY B O 1 ATOM 4436 N N . GLY B 2 207 ? -10.167 4.341 -6.372 1.00 111.00 ? 207 GLY B N 1 ATOM 4437 C CA . GLY B 2 207 ? -9.590 3.358 -5.478 1.00 110.94 ? 207 GLY B CA 1 ATOM 4438 C C . GLY B 2 207 ? -10.619 2.314 -5.093 1.00 112.39 ? 207 GLY B C 1 ATOM 4439 O O . GLY B 2 207 ? -10.308 1.348 -4.399 1.00 115.66 ? 207 GLY B O 1 ATOM 4440 N N . ILE B 2 208 ? -11.850 2.516 -5.548 1.00 99.80 ? 208 ILE B N 1 ATOM 4441 C CA . ILE B 2 208 ? -12.940 1.581 -5.296 1.00 83.96 ? 208 ILE B CA 1 ATOM 4442 C C . ILE B 2 208 ? -12.766 0.264 -6.043 1.00 82.22 ? 208 ILE B C 1 ATOM 4443 O O . ILE B 2 208 ? -12.190 0.225 -7.130 1.00 78.23 ? 208 ILE B O 1 ATOM 4444 C CB . ILE B 2 208 ? -14.279 2.172 -5.721 1.00 63.27 ? 208 ILE B CB 1 ATOM 4445 C CG1 . ILE B 2 208 ? -14.102 2.835 -7.081 1.00 48.26 ? 208 ILE B CG1 1 ATOM 4446 C CG2 . ILE B 2 208 ? -14.786 3.168 -4.687 1.00 59.93 ? 208 ILE B CG2 1 ATOM 4447 C CD1 . ILE B 2 208 ? -15.306 2.760 -7.952 1.00 49.86 ? 208 ILE B CD1 1 ATOM 4448 N N . MET B 2 209 ? -13.288 -0.810 -5.462 1.00 84.45 ? 209 MET B N 1 ATOM 4449 C CA . MET B 2 209 ? -13.326 -2.093 -6.144 1.00 84.17 ? 209 MET B CA 1 ATOM 4450 C C . MET B 2 209 ? -14.678 -2.241 -6.838 1.00 80.86 ? 209 MET B C 1 ATOM 4451 O O . MET B 2 209 ? -14.756 -2.671 -7.984 1.00 89.08 ? 209 MET B O 1 ATOM 4452 C CB . MET B 2 209 ? -13.098 -3.253 -5.170 1.00 97.67 ? 209 MET B CB 1 ATOM 4453 C CG . MET B 2 209 ? -12.166 -2.958 -3.999 1.00 100.94 ? 209 MET B CG 1 ATOM 4454 S SD . MET B 2 209 ? -10.440 -2.675 -4.436 1.00 107.99 ? 209 MET B SD 1 ATOM 4455 C CE . MET B 2 209 ? -10.137 -4.027 -5.574 1.00 114.26 ? 209 MET B CE 1 ATOM 4456 N N . GLU B 2 210 ? -15.743 -1.872 -6.134 1.00 61.27 ? 210 GLU B N 1 ATOM 4457 C CA . GLU B 2 210 ? -17.088 -1.955 -6.691 1.00 63.85 ? 210 GLU B CA 1 ATOM 4458 C C . GLU B 2 210 ? -17.818 -0.618 -6.602 1.00 73.44 ? 210 GLU B C 1 ATOM 4459 O O . GLU B 2 210 ? -17.665 0.126 -5.632 1.00 74.85 ? 210 GLU B O 1 ATOM 4460 C CB . GLU B 2 210 ? -17.902 -3.040 -5.978 1.00 59.18 ? 210 GLU B CB 1 ATOM 4461 C CG . GLU B 2 210 ? -19.261 -3.319 -6.611 1.00 61.29 ? 210 GLU B CG 1 ATOM 4462 C CD . GLU B 2 210 ? -20.102 -4.295 -5.804 1.00 72.14 ? 210 GLU B CD 1 ATOM 4463 O OE1 . GLU B 2 210 ? -20.433 -3.983 -4.640 1.00 83.84 ? 210 GLU B OE1 1 ATOM 4464 O OE2 . GLU B 2 210 ? -20.431 -5.374 -6.336 1.00 65.83 ? 210 GLU B OE2 1 ATOM 4465 N N . ILE B 2 211 ? -18.607 -0.321 -7.627 1.00 71.96 ? 211 ILE B N 1 ATOM 4466 C CA . ILE B 2 211 ? -19.477 0.843 -7.618 1.00 64.92 ? 211 ILE B CA 1 ATOM 4467 C C . ILE B 2 211 ? -20.737 0.522 -8.412 1.00 62.16 ? 211 ILE B C 1 ATOM 4468 O O . ILE B 2 211 ? -20.684 -0.188 -9.415 1.00 65.18 ? 211 ILE B O 1 ATOM 4469 C CB . ILE B 2 211 ? -18.774 2.088 -8.195 1.00 63.91 ? 211 ILE B CB 1 ATOM 4470 C CG1 . ILE B 2 211 ? -19.697 3.307 -8.168 1.00 66.45 ? 211 ILE B CG1 1 ATOM 4471 C CG2 . ILE B 2 211 ? -18.286 1.823 -9.601 1.00 64.15 ? 211 ILE B CG2 1 ATOM 4472 C CD1 . ILE B 2 211 ? -18.996 4.601 -8.503 1.00 69.88 ? 211 ILE B CD1 1 ATOM 4473 N N . GLN B 2 212 ? -21.873 1.028 -7.951 1.00 60.02 ? 212 GLN B N 1 ATOM 4474 C CA . GLN B 2 212 ? -23.141 0.713 -8.585 1.00 62.77 ? 212 GLN B CA 1 ATOM 4475 C C . GLN B 2 212 ? -23.939 1.973 -8.912 1.00 62.54 ? 212 GLN B C 1 ATOM 4476 O O . GLN B 2 212 ? -24.211 2.794 -8.037 1.00 61.49 ? 212 GLN B O 1 ATOM 4477 C CB . GLN B 2 212 ? -23.949 -0.226 -7.689 1.00 64.96 ? 212 GLN B CB 1 ATOM 4478 C CG . GLN B 2 212 ? -23.645 -1.699 -7.917 1.00 72.98 ? 212 GLN B CG 1 ATOM 4479 C CD . GLN B 2 212 ? -23.764 -2.520 -6.651 1.00 86.45 ? 212 GLN B CD 1 ATOM 4480 O OE1 . GLN B 2 212 ? -23.556 -2.013 -5.550 1.00 95.53 ? 212 GLN B OE1 1 ATOM 4481 N NE2 . GLN B 2 212 ? -24.101 -3.796 -6.800 1.00 89.08 ? 212 GLN B NE2 1 ATOM 4482 N N . LEU B 2 213 ? -24.305 2.113 -10.183 1.00 65.58 ? 213 LEU B N 1 ATOM 4483 C CA . LEU B 2 213 ? -25.012 3.293 -10.670 1.00 63.53 ? 213 LEU B CA 1 ATOM 4484 C C . LEU B 2 213 ? -26.228 2.895 -11.510 1.00 65.21 ? 213 LEU B C 1 ATOM 4485 O O . LEU B 2 213 ? -26.700 3.668 -12.341 1.00 72.20 ? 213 LEU B O 1 ATOM 4486 C CB . LEU B 2 213 ? -24.065 4.168 -11.497 1.00 65.15 ? 213 LEU B CB 1 ATOM 4487 C CG . LEU B 2 213 ? -22.686 4.461 -10.893 1.00 66.86 ? 213 LEU B CG 1 ATOM 4488 C CD1 . LEU B 2 213 ? -21.643 4.674 -11.981 1.00 65.86 ? 213 LEU B CD1 1 ATOM 4489 C CD2 . LEU B 2 213 ? -22.743 5.666 -9.965 1.00 65.02 ? 213 LEU B CD2 1 ATOM 4490 N N . GLU B 2 214 ? -26.735 1.692 -11.256 1.00 62.82 ? 214 GLU B N 1 ATOM 4491 C CA . GLU B 2 214 ? -27.658 0.993 -12.155 1.00 67.54 ? 214 GLU B CA 1 ATOM 4492 C C . GLU B 2 214 ? -28.967 1.702 -12.509 1.00 71.95 ? 214 GLU B C 1 ATOM 4493 O O . GLU B 2 214 ? -29.284 1.850 -13.689 1.00 81.59 ? 214 GLU B O 1 ATOM 4494 C CB . GLU B 2 214 ? -27.986 -0.380 -11.560 1.00 77.70 ? 214 GLU B CB 1 ATOM 4495 C CG . GLU B 2 214 ? -26.998 -1.486 -11.933 1.00 88.66 ? 214 GLU B CG 1 ATOM 4496 C CD . GLU B 2 214 ? -25.610 -1.296 -11.336 1.00 98.08 ? 214 GLU B CD 1 ATOM 4497 O OE1 . GLU B 2 214 ? -25.379 -0.296 -10.628 1.00 104.50 ? 214 GLU B OE1 1 ATOM 4498 O OE2 . GLU B 2 214 ? -24.743 -2.160 -11.575 1.00 104.10 ? 214 GLU B OE2 1 ATOM 4499 N N . GLU B 2 215 ? -29.736 2.124 -11.512 1.00 70.66 ? 215 GLU B N 1 ATOM 4500 C CA . GLU B 2 215 ? -31.059 2.669 -11.801 1.00 72.29 ? 215 GLU B CA 1 ATOM 4501 C C . GLU B 2 215 ? -31.137 4.182 -11.611 1.00 73.94 ? 215 GLU B C 1 ATOM 4502 O O . GLU B 2 215 ? -31.880 4.675 -10.766 1.00 74.91 ? 215 GLU B O 1 ATOM 4503 C CB . GLU B 2 215 ? -32.114 1.967 -10.942 1.00 73.81 ? 215 GLU B CB 1 ATOM 4504 C CG . GLU B 2 215 ? -32.396 0.540 -11.403 1.00 79.30 ? 215 GLU B CG 1 ATOM 4505 C CD . GLU B 2 215 ? -33.351 -0.213 -10.493 1.00 87.03 ? 215 GLU B CD 1 ATOM 4506 O OE1 . GLU B 2 215 ? -33.376 0.069 -9.278 1.00 83.81 ? 215 GLU B OE1 1 ATOM 4507 O OE2 . GLU B 2 215 ? -34.077 -1.093 -10.997 1.00 97.04 ? 215 GLU B OE2 1 ATOM 4508 N N . ASN B 2 216 ? -30.385 4.911 -12.430 1.00 72.32 ? 216 ASN B N 1 ATOM 4509 C CA . ASN B 2 216 ? -30.335 6.366 -12.348 1.00 62.47 ? 216 ASN B CA 1 ATOM 4510 C C . ASN B 2 216 ? -30.753 7.039 -13.654 1.00 56.41 ? 216 ASN B C 1 ATOM 4511 O O . ASN B 2 216 ? -30.567 6.473 -14.731 1.00 53.60 ? 216 ASN B O 1 ATOM 4512 C CB . ASN B 2 216 ? -28.929 6.818 -11.954 1.00 64.28 ? 216 ASN B CB 1 ATOM 4513 C CG . ASN B 2 216 ? -28.650 6.627 -10.481 1.00 63.97 ? 216 ASN B CG 1 ATOM 4514 O OD1 . ASN B 2 216 ? -28.902 7.519 -9.671 1.00 63.07 ? 216 ASN B OD1 1 ATOM 4515 N ND2 . ASN B 2 216 ? -28.132 5.457 -10.123 1.00 68.37 ? 216 ASN B ND2 1 ATOM 4516 N N . PRO B 2 217 ? -31.324 8.253 -13.560 1.00 62.45 ? 217 PRO B N 1 ATOM 4517 C CA . PRO B 2 217 ? -31.780 9.024 -14.723 1.00 68.50 ? 217 PRO B CA 1 ATOM 4518 C C . PRO B 2 217 ? -30.638 9.669 -15.499 1.00 72.06 ? 217 PRO B C 1 ATOM 4519 O O . PRO B 2 217 ? -30.575 10.895 -15.595 1.00 79.73 ? 217 PRO B O 1 ATOM 4520 C CB . PRO B 2 217 ? -32.666 10.099 -14.096 1.00 70.72 ? 217 PRO B CB 1 ATOM 4521 C CG . PRO B 2 217 ? -32.079 10.305 -12.752 1.00 64.73 ? 217 PRO B CG 1 ATOM 4522 C CD . PRO B 2 217 ? -31.666 8.932 -12.299 1.00 62.54 ? 217 PRO B CD 1 ATOM 4523 N N . TRP B 2 218 ? -29.758 8.849 -16.056 1.00 68.00 ? 218 TRP B N 1 ATOM 4524 C CA . TRP B 2 218 ? -28.595 9.358 -16.760 1.00 66.94 ? 218 TRP B CA 1 ATOM 4525 C C . TRP B 2 218 ? -28.959 10.096 -18.042 1.00 69.36 ? 218 TRP B C 1 ATOM 4526 O O . TRP B 2 218 ? -29.652 9.569 -18.910 1.00 77.35 ? 218 TRP B O 1 ATOM 4527 C CB . TRP B 2 218 ? -27.626 8.213 -17.066 1.00 71.50 ? 218 TRP B CB 1 ATOM 4528 C CG . TRP B 2 218 ? -27.064 7.562 -15.835 1.00 71.40 ? 218 TRP B CG 1 ATOM 4529 C CD1 . TRP B 2 218 ? -27.240 6.270 -15.437 1.00 71.65 ? 218 TRP B CD1 1 ATOM 4530 C CD2 . TRP B 2 218 ? -26.246 8.182 -14.835 1.00 70.27 ? 218 TRP B CD2 1 ATOM 4531 N NE1 . TRP B 2 218 ? -26.571 6.041 -14.260 1.00 70.14 ? 218 TRP B NE1 1 ATOM 4532 C CE2 . TRP B 2 218 ? -25.955 7.200 -13.867 1.00 69.75 ? 218 TRP B CE2 1 ATOM 4533 C CE3 . TRP B 2 218 ? -25.728 9.470 -14.666 1.00 71.19 ? 218 TRP B CE3 1 ATOM 4534 C CZ2 . TRP B 2 218 ? -25.171 7.466 -12.746 1.00 69.32 ? 218 TRP B CZ2 1 ATOM 4535 C CZ3 . TRP B 2 218 ? -24.950 9.732 -13.554 1.00 74.46 ? 218 TRP B CZ3 1 ATOM 4536 C CH2 . TRP B 2 218 ? -24.679 8.734 -12.608 1.00 72.35 ? 218 TRP B CH2 1 ATOM 4537 N N . ASN B 2 219 ? -28.478 11.327 -18.147 1.00 65.57 ? 219 ASN B N 1 ATOM 4538 C CA . ASN B 2 219 ? -28.693 12.161 -19.318 1.00 67.59 ? 219 ASN B CA 1 ATOM 4539 C C . ASN B 2 219 ? -27.438 12.141 -20.182 1.00 68.79 ? 219 ASN B C 1 ATOM 4540 O O . ASN B 2 219 ? -26.461 12.833 -19.893 1.00 73.18 ? 219 ASN B O 1 ATOM 4541 C CB . ASN B 2 219 ? -29.047 13.580 -18.859 1.00 75.28 ? 219 ASN B CB 1 ATOM 4542 C CG . ASN B 2 219 ? -29.320 14.549 -20.007 1.00 78.78 ? 219 ASN B CG 1 ATOM 4543 O OD1 . ASN B 2 219 ? -29.351 14.173 -21.175 1.00 77.48 ? 219 ASN B OD1 1 ATOM 4544 N ND2 . ASN B 2 219 ? -29.537 15.813 -19.658 1.00 82.69 ? 219 ASN B ND2 1 ATOM 4545 N N . CYS B 2 220 ? -27.464 11.330 -21.235 1.00 68.50 ? 220 CYS B N 1 ATOM 4546 C CA . CYS B 2 220 ? -26.277 11.088 -22.051 1.00 68.91 ? 220 CYS B CA 1 ATOM 4547 C C . CYS B 2 220 ? -26.043 12.180 -23.083 1.00 83.58 ? 220 CYS B C 1 ATOM 4548 O O . CYS B 2 220 ? -26.442 12.055 -24.238 1.00 98.78 ? 220 CYS B O 1 ATOM 4549 C CB . CYS B 2 220 ? -26.382 9.732 -22.752 1.00 66.85 ? 220 CYS B CB 1 ATOM 4550 S SG . CYS B 2 220 ? -26.406 8.323 -21.627 1.00 72.54 ? 220 CYS B SG 1 ATOM 4551 N N . THR B 2 221 ? -25.377 13.245 -22.654 1.00 88.72 ? 221 THR B N 1 ATOM 4552 C CA . THR B 2 221 ? -24.913 14.294 -23.549 1.00 96.57 ? 221 THR B CA 1 ATOM 4553 C C . THR B 2 221 ? -23.403 14.441 -23.357 1.00 101.85 ? 221 THR B C 1 ATOM 4554 O O . THR B 2 221 ? -22.825 13.750 -22.517 1.00 98.73 ? 221 THR B O 1 ATOM 4555 C CB . THR B 2 221 ? -25.630 15.629 -23.280 1.00 94.87 ? 221 THR B CB 1 ATOM 4556 O OG1 . THR B 2 221 ? -25.318 16.082 -21.958 1.00 95.15 ? 221 THR B OG1 1 ATOM 4557 C CG2 . THR B 2 221 ? -27.139 15.454 -23.398 1.00 91.28 ? 221 THR B CG2 1 ATOM 4558 N N . CYS B 2 222 ? -22.769 15.323 -24.130 1.00 108.72 ? 222 CYS B N 1 ATOM 4559 C CA . CYS B 2 222 ? -21.333 15.585 -23.992 1.00 114.46 ? 222 CYS B CA 1 ATOM 4560 C C . CYS B 2 222 ? -20.989 15.954 -22.551 1.00 116.55 ? 222 CYS B C 1 ATOM 4561 O O . CYS B 2 222 ? -19.900 15.666 -22.060 1.00 116.83 ? 222 CYS B O 1 ATOM 4562 C CB . CYS B 2 222 ? -20.885 16.705 -24.936 1.00 115.45 ? 222 CYS B CB 1 ATOM 4563 S SG . CYS B 2 222 ? -20.822 16.264 -26.685 1.00 144.95 ? 222 CYS B SG 1 ATOM 4564 N N . ASP B 2 223 ? -21.951 16.574 -21.877 1.00 116.26 ? 223 ASP B N 1 ATOM 4565 C CA . ASP B 2 223 ? -21.830 16.958 -20.477 1.00 116.53 ? 223 ASP B CA 1 ATOM 4566 C C . ASP B 2 223 ? -21.728 15.729 -19.550 1.00 106.80 ? 223 ASP B C 1 ATOM 4567 O O . ASP B 2 223 ? -21.380 15.849 -18.372 1.00 103.98 ? 223 ASP B O 1 ATOM 4568 C CB . ASP B 2 223 ? -23.018 17.868 -20.117 1.00 126.55 ? 223 ASP B CB 1 ATOM 4569 C CG . ASP B 2 223 ? -23.608 17.579 -18.755 1.00 143.47 ? 223 ASP B CG 1 ATOM 4570 O OD1 . ASP B 2 223 ? -23.136 18.172 -17.761 1.00 149.22 ? 223 ASP B OD1 1 ATOM 4571 O OD2 . ASP B 2 223 ? -24.556 16.770 -18.687 1.00 151.55 ? 223 ASP B OD2 1 ATOM 4572 N N . LEU B 2 224 ? -21.987 14.543 -20.099 1.00 99.95 ? 224 LEU B N 1 ATOM 4573 C CA . LEU B 2 224 ? -21.829 13.289 -19.355 1.00 90.84 ? 224 LEU B CA 1 ATOM 4574 C C . LEU B 2 224 ? -20.536 12.553 -19.735 1.00 89.25 ? 224 LEU B C 1 ATOM 4575 O O . LEU B 2 224 ? -20.306 11.421 -19.313 1.00 89.14 ? 224 LEU B O 1 ATOM 4576 C CB . LEU B 2 224 ? -23.043 12.376 -19.585 1.00 80.46 ? 224 LEU B CB 1 ATOM 4577 C CG . LEU B 2 224 ? -23.236 11.108 -18.737 1.00 68.95 ? 224 LEU B CG 1 ATOM 4578 C CD1 . LEU B 2 224 ? -24.587 11.097 -18.057 1.00 77.70 ? 224 LEU B CD1 1 ATOM 4579 C CD2 . LEU B 2 224 ? -23.070 9.860 -19.588 1.00 62.47 ? 224 LEU B CD2 1 ATOM 4580 N N . LEU B 2 225 ? -19.686 13.194 -20.528 1.00 90.12 ? 225 LEU B N 1 ATOM 4581 C CA . LEU B 2 225 ? -18.440 12.551 -20.954 1.00 91.78 ? 225 LEU B CA 1 ATOM 4582 C C . LEU B 2 225 ? -17.440 12.183 -19.837 1.00 80.42 ? 225 LEU B C 1 ATOM 4583 O O . LEU B 2 225 ? -16.892 11.082 -19.879 1.00 72.46 ? 225 LEU B O 1 ATOM 4584 C CB . LEU B 2 225 ? -17.731 13.422 -21.998 1.00 105.54 ? 225 LEU B CB 1 ATOM 4585 C CG . LEU B 2 225 ? -18.338 13.305 -23.404 1.00 118.20 ? 225 LEU B CG 1 ATOM 4586 C CD1 . LEU B 2 225 ? -17.587 14.149 -24.425 1.00 126.25 ? 225 LEU B CD1 1 ATOM 4587 C CD2 . LEU B 2 225 ? -18.399 11.852 -23.846 1.00 120.03 ? 225 LEU B CD2 1 ATOM 4588 N N . PRO B 2 226 ? -17.191 13.081 -18.851 1.00 83.10 ? 226 PRO B N 1 ATOM 4589 C CA . PRO B 2 226 ? -16.137 12.756 -17.876 1.00 83.23 ? 226 PRO B CA 1 ATOM 4590 C C . PRO B 2 226 ? -16.317 11.384 -17.250 1.00 86.60 ? 226 PRO B C 1 ATOM 4591 O O . PRO B 2 226 ? -15.402 10.556 -17.295 1.00 91.66 ? 226 PRO B O 1 ATOM 4592 C CB . PRO B 2 226 ? -16.290 13.847 -16.812 1.00 80.96 ? 226 PRO B CB 1 ATOM 4593 C CG . PRO B 2 226 ? -16.917 14.974 -17.518 1.00 84.69 ? 226 PRO B CG 1 ATOM 4594 C CD . PRO B 2 226 ? -17.844 14.363 -18.521 1.00 85.35 ? 226 PRO B CD 1 ATOM 4595 N N . LEU B 2 227 ? -17.506 11.164 -16.696 1.00 82.01 ? 227 LEU B N 1 ATOM 4596 C CA . LEU B 2 227 ? -17.917 9.877 -16.150 1.00 71.44 ? 227 LEU B CA 1 ATOM 4597 C C . LEU B 2 227 ? -17.535 8.732 -17.080 1.00 65.88 ? 227 LEU B C 1 ATOM 4598 O O . LEU B 2 227 ? -16.790 7.827 -16.692 1.00 67.03 ? 227 LEU B O 1 ATOM 4599 C CB . LEU B 2 227 ? -19.425 9.881 -15.900 1.00 65.30 ? 227 LEU B CB 1 ATOM 4600 C CG . LEU B 2 227 ? -20.092 8.564 -15.512 1.00 62.29 ? 227 LEU B CG 1 ATOM 4601 C CD1 . LEU B 2 227 ? -19.430 7.963 -14.279 1.00 59.79 ? 227 LEU B CD1 1 ATOM 4602 C CD2 . LEU B 2 227 ? -21.578 8.784 -15.275 1.00 61.17 ? 227 LEU B CD2 1 ATOM 4603 N N . LYS B 2 228 ? -18.040 8.797 -18.308 1.00 60.13 ? 228 LYS B N 1 ATOM 4604 C CA . LYS B 2 228 ? -17.703 7.834 -19.352 1.00 74.18 ? 228 LYS B CA 1 ATOM 4605 C C . LYS B 2 228 ? -16.199 7.581 -19.408 1.00 85.89 ? 228 LYS B C 1 ATOM 4606 O O . LYS B 2 228 ? -15.752 6.436 -19.296 1.00 90.57 ? 228 LYS B O 1 ATOM 4607 C CB . LYS B 2 228 ? -18.216 8.331 -20.709 1.00 79.64 ? 228 LYS B CB 1 ATOM 4608 C CG . LYS B 2 228 ? -17.726 7.545 -21.923 1.00 79.17 ? 228 LYS B CG 1 ATOM 4609 C CD . LYS B 2 228 ? -18.201 6.101 -21.900 1.00 70.24 ? 228 LYS B CD 1 ATOM 4610 C CE . LYS B 2 228 ? -18.035 5.438 -23.261 1.00 66.58 ? 228 LYS B CE 1 ATOM 4611 N NZ . LYS B 2 228 ? -16.641 5.512 -23.783 1.00 67.62 ? 228 LYS B NZ 1 ATOM 4612 N N . ALA B 2 229 ? -15.424 8.655 -19.544 1.00 91.59 ? 229 ALA B N 1 ATOM 4613 C CA . ALA B 2 229 ? -13.973 8.531 -19.619 1.00 97.78 ? 229 ALA B CA 1 ATOM 4614 C C . ALA B 2 229 ? -13.438 7.859 -18.368 1.00 92.76 ? 229 ALA B C 1 ATOM 4615 O O . ALA B 2 229 ? -12.617 6.940 -18.444 1.00 89.79 ? 229 ALA B O 1 ATOM 4616 C CB . ALA B 2 229 ? -13.327 9.890 -19.806 1.00 105.41 ? 229 ALA B CB 1 ATOM 4617 N N . TRP B 2 230 ? -13.934 8.302 -17.216 1.00 92.78 ? 230 TRP B N 1 ATOM 4618 C CA . TRP B 2 230 ? -13.468 7.776 -15.941 1.00 89.92 ? 230 TRP B CA 1 ATOM 4619 C C . TRP B 2 230 ? -13.753 6.282 -15.834 1.00 88.12 ? 230 TRP B C 1 ATOM 4620 O O . TRP B 2 230 ? -13.095 5.563 -15.079 1.00 85.41 ? 230 TRP B O 1 ATOM 4621 C CB . TRP B 2 230 ? -14.120 8.524 -14.777 1.00 88.79 ? 230 TRP B CB 1 ATOM 4622 C CG . TRP B 2 230 ? -13.717 7.989 -13.444 1.00 93.08 ? 230 TRP B CG 1 ATOM 4623 C CD1 . TRP B 2 230 ? -12.558 8.246 -12.772 1.00 98.82 ? 230 TRP B CD1 1 ATOM 4624 C CD2 . TRP B 2 230 ? -14.468 7.092 -12.620 1.00 89.39 ? 230 TRP B CD2 1 ATOM 4625 N NE1 . TRP B 2 230 ? -12.543 7.568 -11.579 1.00 95.22 ? 230 TRP B NE1 1 ATOM 4626 C CE2 . TRP B 2 230 ? -13.704 6.850 -11.464 1.00 90.07 ? 230 TRP B CE2 1 ATOM 4627 C CE3 . TRP B 2 230 ? -15.717 6.476 -12.744 1.00 91.96 ? 230 TRP B CE3 1 ATOM 4628 C CZ2 . TRP B 2 230 ? -14.147 6.022 -10.439 1.00 91.84 ? 230 TRP B CZ2 1 ATOM 4629 C CZ3 . TRP B 2 230 ? -16.153 5.649 -11.724 1.00 91.68 ? 230 TRP B CZ3 1 ATOM 4630 C CH2 . TRP B 2 230 ? -15.370 5.431 -10.588 1.00 90.37 ? 230 TRP B CH2 1 ATOM 4631 N N . LEU B 2 231 ? -14.722 5.810 -16.611 1.00 87.51 ? 231 LEU B N 1 ATOM 4632 C CA . LEU B 2 231 ? -15.109 4.410 -16.541 1.00 91.68 ? 231 LEU B CA 1 ATOM 4633 C C . LEU B 2 231 ? -14.128 3.505 -17.283 1.00 98.59 ? 231 LEU B C 1 ATOM 4634 O O . LEU B 2 231 ? -14.112 2.291 -17.072 1.00 93.04 ? 231 LEU B O 1 ATOM 4635 C CB . LEU B 2 231 ? -16.525 4.222 -17.079 1.00 93.63 ? 231 LEU B CB 1 ATOM 4636 C CG . LEU B 2 231 ? -17.615 4.765 -16.151 1.00 94.96 ? 231 LEU B CG 1 ATOM 4637 C CD1 . LEU B 2 231 ? -18.994 4.554 -16.750 1.00 102.49 ? 231 LEU B CD1 1 ATOM 4638 C CD2 . LEU B 2 231 ? -17.523 4.118 -14.781 1.00 91.85 ? 231 LEU B CD2 1 ATOM 4639 N N . ASP B 2 232 ? -13.300 4.093 -18.141 1.00 114.30 ? 232 ASP B N 1 ATOM 4640 C CA . ASP B 2 232 ? -12.268 3.309 -18.806 1.00 117.69 ? 232 ASP B CA 1 ATOM 4641 C C . ASP B 2 232 ? -11.042 3.224 -17.909 1.00 117.61 ? 232 ASP B C 1 ATOM 4642 O O . ASP B 2 232 ? -10.432 2.163 -17.770 1.00 120.96 ? 232 ASP B O 1 ATOM 4643 C CB . ASP B 2 232 ? -11.904 3.912 -20.164 1.00 126.32 ? 232 ASP B CB 1 ATOM 4644 C CG . ASP B 2 232 ? -13.066 3.899 -21.135 1.00 131.40 ? 232 ASP B CG 1 ATOM 4645 O OD1 . ASP B 2 232 ? -14.189 4.252 -20.721 1.00 129.59 ? 232 ASP B OD1 1 ATOM 4646 O OD2 . ASP B 2 232 ? -12.861 3.527 -22.310 1.00 136.43 ? 232 ASP B OD2 1 ATOM 4647 N N . THR B 2 233 ? -10.700 4.348 -17.289 1.00 114.58 ? 233 THR B N 1 ATOM 4648 C CA . THR B 2 233 ? -9.542 4.426 -16.407 1.00 114.83 ? 233 THR B CA 1 ATOM 4649 C C . THR B 2 233 ? -9.725 3.560 -15.164 1.00 116.98 ? 233 THR B C 1 ATOM 4650 O O . THR B 2 233 ? -8.772 2.941 -14.686 1.00 117.11 ? 233 THR B O 1 ATOM 4651 C CB . THR B 2 233 ? -9.270 5.872 -15.967 1.00 111.87 ? 233 THR B CB 1 ATOM 4652 O OG1 . THR B 2 233 ? -10.210 6.250 -14.954 1.00 105.44 ? 233 THR B OG1 1 ATOM 4653 C CG2 . THR B 2 233 ? -9.390 6.820 -17.152 1.00 115.63 ? 233 THR B CG2 1 ATOM 4654 N N . ILE B 2 234 ? -10.948 3.526 -14.639 1.00 124.89 ? 234 ILE B N 1 ATOM 4655 C CA . ILE B 2 234 ? -11.255 2.694 -13.479 1.00 133.94 ? 234 ILE B CA 1 ATOM 4656 C C . ILE B 2 234 ? -11.149 1.227 -13.870 1.00 136.56 ? 234 ILE B C 1 ATOM 4657 O O . ILE B 2 234 ? -11.435 0.848 -15.007 1.00 136.44 ? 234 ILE B O 1 ATOM 4658 C CB . ILE B 2 234 ? -12.670 2.996 -12.891 1.00 115.40 ? 234 ILE B CB 1 ATOM 4659 C CG1 . ILE B 2 234 ? -12.890 2.291 -11.546 1.00 107.21 ? 234 ILE B CG1 1 ATOM 4660 C CG2 . ILE B 2 234 ? -13.762 2.557 -13.838 1.00 118.68 ? 234 ILE B CG2 1 ATOM 4661 C CD1 . ILE B 2 234 ? -11.772 2.456 -10.550 1.00 107.48 ? 234 ILE B CD1 1 ATOM 4662 N N . THR B 2 235 ? -10.698 0.413 -12.925 1.00 136.49 ? 235 THR B N 1 ATOM 4663 C CA . THR B 2 235 ? -10.572 -1.017 -13.136 1.00 141.84 ? 235 THR B CA 1 ATOM 4664 C C . THR B 2 235 ? -11.504 -1.759 -12.187 1.00 147.14 ? 235 THR B C 1 ATOM 4665 O O . THR B 2 235 ? -12.040 -1.168 -11.248 1.00 151.34 ? 235 THR B O 1 ATOM 4666 C CB . THR B 2 235 ? -9.129 -1.494 -12.914 1.00 143.45 ? 235 THR B CB 1 ATOM 4667 O OG1 . THR B 2 235 ? -8.833 -1.482 -11.511 1.00 140.79 ? 235 THR B OG1 1 ATOM 4668 C CG2 . THR B 2 235 ? -8.149 -0.584 -13.644 1.00 146.07 ? 235 THR B CG2 1 ATOM 4669 N N . VAL B 2 236 ? -11.676 -3.056 -12.435 1.00 148.81 ? 236 VAL B N 1 ATOM 4670 C CA . VAL B 2 236 ? -12.509 -3.936 -11.610 1.00 148.24 ? 236 VAL B CA 1 ATOM 4671 C C . VAL B 2 236 ? -13.958 -3.429 -11.518 1.00 144.73 ? 236 VAL B C 1 ATOM 4672 O O . VAL B 2 236 ? -14.645 -3.646 -10.522 1.00 140.30 ? 236 VAL B O 1 ATOM 4673 C CB . VAL B 2 236 ? -11.914 -4.111 -10.179 1.00 177.29 ? 236 VAL B CB 1 ATOM 4674 C CG1 . VAL B 2 236 ? -12.408 -5.404 -9.541 1.00 175.59 ? 236 VAL B CG1 1 ATOM 4675 C CG2 . VAL B 2 236 ? -10.388 -4.122 -10.220 1.00 179.06 ? 236 VAL B CG2 1 ATOM 4676 N N . PHE B 2 237 ? -14.427 -2.769 -12.571 1.00 145.63 ? 237 PHE B N 1 ATOM 4677 C CA . PHE B 2 237 ? -15.792 -2.252 -12.589 1.00 141.10 ? 237 PHE B CA 1 ATOM 4678 C C . PHE B 2 237 ? -16.783 -3.231 -13.208 1.00 132.13 ? 237 PHE B C 1 ATOM 4679 O O . PHE B 2 237 ? -16.510 -3.827 -14.249 1.00 132.90 ? 237 PHE B O 1 ATOM 4680 C CB . PHE B 2 237 ? -15.855 -0.928 -13.350 1.00 145.10 ? 237 PHE B CB 1 ATOM 4681 C CG . PHE B 2 237 ? -17.256 -0.435 -13.584 1.00 146.12 ? 237 PHE B CG 1 ATOM 4682 C CD1 . PHE B 2 237 ? -17.885 0.354 -12.641 1.00 144.36 ? 237 PHE B CD1 1 ATOM 4683 C CD2 . PHE B 2 237 ? -17.946 -0.764 -14.742 1.00 146.99 ? 237 PHE B CD2 1 ATOM 4684 C CE1 . PHE B 2 237 ? -19.172 0.808 -12.843 1.00 143.07 ? 237 PHE B CE1 1 ATOM 4685 C CE2 . PHE B 2 237 ? -19.235 -0.318 -14.945 1.00 145.94 ? 237 PHE B CE2 1 ATOM 4686 C CZ . PHE B 2 237 ? -19.845 0.469 -13.993 1.00 143.66 ? 237 PHE B CZ 1 ATOM 4687 N N . VAL B 2 238 ? -17.944 -3.379 -12.574 1.00 129.71 ? 238 VAL B N 1 ATOM 4688 C CA . VAL B 2 238 ? -19.037 -4.174 -13.132 1.00 129.04 ? 238 VAL B CA 1 ATOM 4689 C C . VAL B 2 238 ? -20.367 -3.448 -12.919 1.00 131.36 ? 238 VAL B C 1 ATOM 4690 O O . VAL B 2 238 ? -20.578 -2.813 -11.885 1.00 136.56 ? 238 VAL B O 1 ATOM 4691 C CB . VAL B 2 238 ? -19.114 -5.589 -12.501 1.00 127.68 ? 238 VAL B CB 1 ATOM 4692 C CG1 . VAL B 2 238 ? -20.202 -6.419 -13.171 1.00 128.44 ? 238 VAL B CG1 1 ATOM 4693 C CG2 . VAL B 2 238 ? -17.778 -6.309 -12.602 1.00 129.01 ? 238 VAL B CG2 1 ATOM 4694 N N . GLY B 2 239 ? -21.257 -3.537 -13.902 1.00 122.85 ? 239 GLY B N 1 ATOM 4695 C CA . GLY B 2 239 ? -22.573 -2.933 -13.800 1.00 111.75 ? 239 GLY B CA 1 ATOM 4696 C C . GLY B 2 239 ? -22.988 -2.248 -15.086 1.00 105.74 ? 239 GLY B C 1 ATOM 4697 O O . GLY B 2 239 ? -22.155 -1.990 -15.953 1.00 108.39 ? 239 GLY B O 1 ATOM 4698 N N . GLU B 2 240 ? -24.277 -1.953 -15.217 1.00 95.27 ? 240 GLU B N 1 ATOM 4699 C CA . GLU B 2 240 ? -24.761 -1.273 -16.411 1.00 94.05 ? 240 GLU B CA 1 ATOM 4700 C C . GLU B 2 240 ? -25.202 0.152 -16.105 1.00 90.84 ? 240 GLU B C 1 ATOM 4701 O O . GLU B 2 240 ? -25.761 0.434 -15.046 1.00 93.82 ? 240 GLU B O 1 ATOM 4702 C CB . GLU B 2 240 ? -25.909 -2.054 -17.058 1.00 104.86 ? 240 GLU B CB 1 ATOM 4703 C CG . GLU B 2 240 ? -27.126 -2.270 -16.177 1.00 111.63 ? 240 GLU B CG 1 ATOM 4704 C CD . GLU B 2 240 ? -28.241 -2.996 -16.908 1.00 120.87 ? 240 GLU B CD 1 ATOM 4705 O OE1 . GLU B 2 240 ? -28.250 -2.972 -18.158 1.00 125.80 ? 240 GLU B OE1 1 ATOM 4706 O OE2 . GLU B 2 240 ? -29.104 -3.595 -16.235 1.00 118.84 ? 240 GLU B OE2 1 ATOM 4707 N N . ILE B 2 241 ? -24.931 1.046 -17.048 1.00 92.66 ? 241 ILE B N 1 ATOM 4708 C CA . ILE B 2 241 ? -25.321 2.444 -16.945 1.00 90.71 ? 241 ILE B CA 1 ATOM 4709 C C . ILE B 2 241 ? -26.078 2.821 -18.212 1.00 93.64 ? 241 ILE B C 1 ATOM 4710 O O . ILE B 2 241 ? -25.474 3.168 -19.227 1.00 97.84 ? 241 ILE B O 1 ATOM 4711 C CB . ILE B 2 241 ? -24.100 3.373 -16.760 1.00 91.59 ? 241 ILE B CB 1 ATOM 4712 C CG1 . ILE B 2 241 ? -23.292 2.964 -15.531 1.00 93.37 ? 241 ILE B CG1 1 ATOM 4713 C CG2 . ILE B 2 241 ? -24.527 4.821 -16.644 1.00 93.23 ? 241 ILE B CG2 1 ATOM 4714 C CD1 . ILE B 2 241 ? -22.138 2.053 -15.856 1.00 99.44 ? 241 ILE B CD1 1 ATOM 4715 N N . VAL B 2 242 ? -27.402 2.735 -18.155 1.00 89.87 ? 242 VAL B N 1 ATOM 4716 C CA . VAL B 2 242 ? -28.227 2.956 -19.336 1.00 86.70 ? 242 VAL B CA 1 ATOM 4717 C C . VAL B 2 242 ? -28.713 4.399 -19.433 1.00 79.49 ? 242 VAL B C 1 ATOM 4718 O O . VAL B 2 242 ? -29.113 5.004 -18.437 1.00 79.21 ? 242 VAL B O 1 ATOM 4719 C CB . VAL B 2 242 ? -29.436 2.002 -19.350 1.00 94.61 ? 242 VAL B CB 1 ATOM 4720 C CG1 . VAL B 2 242 ? -28.977 0.578 -19.612 1.00 95.54 ? 242 VAL B CG1 1 ATOM 4721 C CG2 . VAL B 2 242 ? -30.201 2.084 -18.033 1.00 100.29 ? 242 VAL B CG2 1 ATOM 4722 N N . CYS B 2 243 ? -28.668 4.948 -20.642 1.00 82.04 ? 243 CYS B N 1 ATOM 4723 C CA . CYS B 2 243 ? -29.098 6.320 -20.870 1.00 84.49 ? 243 CYS B CA 1 ATOM 4724 C C . CYS B 2 243 ? -30.598 6.455 -20.691 1.00 84.37 ? 243 CYS B C 1 ATOM 4725 O O . CYS B 2 243 ? -31.381 5.814 -21.393 1.00 97.94 ? 243 CYS B O 1 ATOM 4726 C CB . CYS B 2 243 ? -28.708 6.792 -22.271 1.00 90.01 ? 243 CYS B CB 1 ATOM 4727 S SG . CYS B 2 243 ? -26.953 6.664 -22.659 1.00 105.14 ? 243 CYS B SG 1 ATOM 4728 N N . GLU B 2 244 ? -30.995 7.290 -19.742 1.00 80.52 ? 244 GLU B N 1 ATOM 4729 C CA . GLU B 2 244 ? -32.393 7.636 -19.562 1.00 81.41 ? 244 GLU B CA 1 ATOM 4730 C C . GLU B 2 244 ? -32.766 8.729 -20.561 1.00 81.81 ? 244 GLU B C 1 ATOM 4731 O O . GLU B 2 244 ? -33.850 8.717 -21.145 1.00 82.96 ? 244 GLU B O 1 ATOM 4732 C CB . GLU B 2 244 ? -32.647 8.091 -18.122 1.00 88.10 ? 244 GLU B CB 1 ATOM 4733 C CG . GLU B 2 244 ? -34.015 8.698 -17.874 1.00 96.27 ? 244 GLU B CG 1 ATOM 4734 C CD . GLU B 2 244 ? -34.843 7.894 -16.892 1.00 100.71 ? 244 GLU B CD 1 ATOM 4735 O OE1 . GLU B 2 244 ? -34.853 6.649 -16.996 1.00 105.42 ? 244 GLU B OE1 1 ATOM 4736 O OE2 . GLU B 2 244 ? -35.481 8.511 -16.016 1.00 99.95 ? 244 GLU B OE2 1 ATOM 4737 N N . THR B 2 245 ? -31.836 9.659 -20.761 1.00 83.51 ? 245 THR B N 1 ATOM 4738 C CA . THR B 2 245 ? -32.020 10.809 -21.640 1.00 79.68 ? 245 THR B CA 1 ATOM 4739 C C . THR B 2 245 ? -30.822 10.892 -22.588 1.00 80.38 ? 245 THR B C 1 ATOM 4740 O O . THR B 2 245 ? -29.690 10.669 -22.158 1.00 80.14 ? 245 THR B O 1 ATOM 4741 C CB . THR B 2 245 ? -32.147 12.120 -20.823 1.00 82.72 ? 245 THR B CB 1 ATOM 4742 O OG1 . THR B 2 245 ? -33.015 11.907 -19.703 1.00 79.36 ? 245 THR B OG1 1 ATOM 4743 C CG2 . THR B 2 245 ? -32.691 13.261 -21.668 1.00 92.04 ? 245 THR B CG2 1 ATOM 4744 N N . PRO B 2 246 ? -31.054 11.199 -23.879 1.00 86.25 ? 246 PRO B N 1 ATOM 4745 C CA . PRO B 2 246 ? -32.325 11.446 -24.574 1.00 88.42 ? 246 PRO B CA 1 ATOM 4746 C C . PRO B 2 246 ? -32.925 10.213 -25.256 1.00 89.39 ? 246 PRO B C 1 ATOM 4747 O O . PRO B 2 246 ? -32.377 9.114 -25.142 1.00 89.29 ? 246 PRO B O 1 ATOM 4748 C CB . PRO B 2 246 ? -31.937 12.492 -25.615 1.00 92.05 ? 246 PRO B CB 1 ATOM 4749 C CG . PRO B 2 246 ? -30.533 12.128 -25.972 1.00 93.07 ? 246 PRO B CG 1 ATOM 4750 C CD . PRO B 2 246 ? -29.900 11.544 -24.730 1.00 88.67 ? 246 PRO B CD 1 ATOM 4751 N N . PHE B 2 247 ? -34.040 10.415 -25.962 1.00 85.88 ? 247 PHE B N 1 ATOM 4752 C CA . PHE B 2 247 ? -34.792 9.328 -26.599 1.00 84.52 ? 247 PHE B CA 1 ATOM 4753 C C . PHE B 2 247 ? -33.948 8.518 -27.575 1.00 84.78 ? 247 PHE B C 1 ATOM 4754 O O . PHE B 2 247 ? -34.089 7.298 -27.670 1.00 82.71 ? 247 PHE B O 1 ATOM 4755 C CB . PHE B 2 247 ? -36.022 9.882 -27.332 1.00 88.20 ? 247 PHE B CB 1 ATOM 4756 C CG . PHE B 2 247 ? -36.820 8.830 -28.067 1.00 95.56 ? 247 PHE B CG 1 ATOM 4757 C CD1 . PHE B 2 247 ? -37.816 8.117 -27.418 1.00 98.56 ? 247 PHE B CD1 1 ATOM 4758 C CD2 . PHE B 2 247 ? -36.575 8.557 -29.405 1.00 105.04 ? 247 PHE B CD2 1 ATOM 4759 C CE1 . PHE B 2 247 ? -38.548 7.152 -28.089 1.00 99.61 ? 247 PHE B CE1 1 ATOM 4760 C CE2 . PHE B 2 247 ? -37.302 7.590 -30.078 1.00 110.71 ? 247 PHE B CE2 1 ATOM 4761 C CZ . PHE B 2 247 ? -38.291 6.889 -29.419 1.00 104.73 ? 247 PHE B CZ 1 ATOM 4762 N N . ARG B 2 248 ? -33.092 9.210 -28.316 1.00 83.08 ? 248 ARG B N 1 ATOM 4763 C CA . ARG B 2 248 ? -32.203 8.556 -29.263 1.00 89.20 ? 248 ARG B CA 1 ATOM 4764 C C . ARG B 2 248 ? -31.313 7.520 -28.578 1.00 85.56 ? 248 ARG B C 1 ATOM 4765 O O . ARG B 2 248 ? -31.124 6.416 -29.087 1.00 84.13 ? 248 ARG B O 1 ATOM 4766 C CB . ARG B 2 248 ? -31.344 9.598 -29.980 1.00 101.37 ? 248 ARG B CB 1 ATOM 4767 C CG . ARG B 2 248 ? -32.042 10.290 -31.137 1.00 115.89 ? 248 ARG B CG 1 ATOM 4768 C CD . ARG B 2 248 ? -31.046 11.073 -31.977 1.00 128.59 ? 248 ARG B CD 1 ATOM 4769 N NE . ARG B 2 248 ? -31.553 11.348 -33.320 1.00 140.38 ? 248 ARG B NE 1 ATOM 4770 C CZ . ARG B 2 248 ? -30.834 11.909 -34.288 1.00 149.41 ? 248 ARG B CZ 1 ATOM 4771 N NH1 . ARG B 2 248 ? -29.573 12.255 -34.063 1.00 148.37 ? 248 ARG B NH1 1 ATOM 4772 N NH2 . ARG B 2 248 ? -31.373 12.121 -35.482 1.00 156.53 ? 248 ARG B NH2 1 ATOM 4773 N N . LEU B 2 249 ? -30.788 7.877 -27.412 1.00 86.95 ? 249 LEU B N 1 ATOM 4774 C CA . LEU B 2 249 ? -29.846 7.019 -26.706 1.00 91.31 ? 249 LEU B CA 1 ATOM 4775 C C . LEU B 2 249 ? -30.514 6.185 -25.617 1.00 94.94 ? 249 LEU B C 1 ATOM 4776 O O . LEU B 2 249 ? -29.840 5.473 -24.875 1.00 95.94 ? 249 LEU B O 1 ATOM 4777 C CB . LEU B 2 249 ? -28.725 7.865 -26.106 1.00 95.69 ? 249 LEU B CB 1 ATOM 4778 C CG . LEU B 2 249 ? -27.898 8.614 -27.150 1.00 96.68 ? 249 LEU B CG 1 ATOM 4779 C CD1 . LEU B 2 249 ? -26.858 9.501 -26.485 1.00 101.11 ? 249 LEU B CD1 1 ATOM 4780 C CD2 . LEU B 2 249 ? -27.240 7.629 -28.102 1.00 92.00 ? 249 LEU B CD2 1 ATOM 4781 N N . HIS B 2 250 ? -31.838 6.284 -25.537 1.00 102.09 ? 250 HIS B N 1 ATOM 4782 C CA . HIS B 2 250 ? -32.644 5.502 -24.601 1.00 104.47 ? 250 HIS B CA 1 ATOM 4783 C C . HIS B 2 250 ? -32.230 4.030 -24.557 1.00 105.39 ? 250 HIS B C 1 ATOM 4784 O O . HIS B 2 250 ? -32.151 3.367 -25.590 1.00 113.64 ? 250 HIS B O 1 ATOM 4785 C CB . HIS B 2 250 ? -34.124 5.622 -24.979 1.00 109.56 ? 250 HIS B CB 1 ATOM 4786 C CG . HIS B 2 250 ? -35.041 4.771 -24.155 1.00 122.92 ? 250 HIS B CG 1 ATOM 4787 N ND1 . HIS B 2 250 ? -36.226 4.270 -24.649 1.00 128.27 ? 250 HIS B ND1 1 ATOM 4788 C CD2 . HIS B 2 250 ? -34.959 4.347 -22.872 1.00 127.61 ? 250 HIS B CD2 1 ATOM 4789 C CE1 . HIS B 2 250 ? -36.830 3.566 -23.708 1.00 132.76 ? 250 HIS B CE1 1 ATOM 4790 N NE2 . HIS B 2 250 ? -36.082 3.596 -22.620 1.00 130.61 ? 250 HIS B NE2 1 ATOM 4791 N N . GLY B 2 251 ? -31.939 3.536 -23.356 1.00 95.83 ? 251 GLY B N 1 ATOM 4792 C CA . GLY B 2 251 ? -31.643 2.127 -23.154 1.00 97.44 ? 251 GLY B CA 1 ATOM 4793 C C . GLY B 2 251 ? -30.196 1.728 -23.382 1.00 99.85 ? 251 GLY B C 1 ATOM 4794 O O . GLY B 2 251 ? -29.733 0.724 -22.839 1.00 97.40 ? 251 GLY B O 1 ATOM 4795 N N . LYS B 2 252 ? -29.485 2.510 -24.188 1.00 102.39 ? 252 LYS B N 1 ATOM 4796 C CA . LYS B 2 252 ? -28.101 2.204 -24.537 1.00 108.33 ? 252 LYS B CA 1 ATOM 4797 C C . LYS B 2 252 ? -27.177 2.265 -23.322 1.00 105.68 ? 252 LYS B C 1 ATOM 4798 O O . LYS B 2 252 ? -27.219 3.220 -22.549 1.00 105.93 ? 252 LYS B O 1 ATOM 4799 C CB . LYS B 2 252 ? -27.601 3.170 -25.613 1.00 122.14 ? 252 LYS B CB 1 ATOM 4800 C CG . LYS B 2 252 ? -28.415 3.163 -26.902 1.00 134.23 ? 252 LYS B CG 1 ATOM 4801 C CD . LYS B 2 252 ? -27.876 2.149 -27.902 1.00 142.33 ? 252 LYS B CD 1 ATOM 4802 C CE . LYS B 2 252 ? -28.509 2.331 -29.275 1.00 144.04 ? 252 LYS B CE 1 ATOM 4803 N NZ . LYS B 2 252 ? -29.985 2.144 -29.237 1.00 141.67 ? 252 LYS B NZ 1 ATOM 4804 N N . ASP B 2 253 ? -26.341 1.244 -23.162 1.00 111.43 ? 253 ASP B N 1 ATOM 4805 C CA . ASP B 2 253 ? -25.395 1.198 -22.051 1.00 108.25 ? 253 ASP B CA 1 ATOM 4806 C C . ASP B 2 253 ? -24.172 2.052 -22.365 1.00 102.25 ? 253 ASP B C 1 ATOM 4807 O O . ASP B 2 253 ? -23.421 1.749 -23.290 1.00 104.29 ? 253 ASP B O 1 ATOM 4808 C CB . ASP B 2 253 ? -24.980 -0.245 -21.757 1.00 116.69 ? 253 ASP B CB 1 ATOM 4809 C CG . ASP B 2 253 ? -24.459 -0.429 -20.346 1.00 121.86 ? 253 ASP B CG 1 ATOM 4810 O OD1 . ASP B 2 253 ? -24.070 0.577 -19.717 1.00 123.46 ? 253 ASP B OD1 1 ATOM 4811 O OD2 . ASP B 2 253 ? -24.436 -1.581 -19.865 1.00 126.10 ? 253 ASP B OD2 1 ATOM 4812 N N . VAL B 2 254 ? -23.982 3.112 -21.583 1.00 90.06 ? 254 VAL B N 1 ATOM 4813 C CA . VAL B 2 254 ? -22.925 4.101 -21.801 1.00 87.94 ? 254 VAL B CA 1 ATOM 4814 C C . VAL B 2 254 ? -21.554 3.481 -22.075 1.00 93.08 ? 254 VAL B C 1 ATOM 4815 O O . VAL B 2 254 ? -20.807 3.960 -22.929 1.00 96.71 ? 254 VAL B O 1 ATOM 4816 C CB . VAL B 2 254 ? -22.812 5.048 -20.587 1.00 83.25 ? 254 VAL B CB 1 ATOM 4817 C CG1 . VAL B 2 254 ? -21.614 5.976 -20.727 1.00 81.20 ? 254 VAL B CG1 1 ATOM 4818 C CG2 . VAL B 2 254 ? -24.092 5.851 -20.426 1.00 83.33 ? 254 VAL B CG2 1 ATOM 4819 N N . THR B 2 255 ? -21.237 2.408 -21.360 1.00 97.64 ? 255 THR B N 1 ATOM 4820 C CA . THR B 2 255 ? -19.983 1.689 -21.560 1.00 106.67 ? 255 THR B CA 1 ATOM 4821 C C . THR B 2 255 ? -19.810 1.235 -23.010 1.00 115.83 ? 255 THR B C 1 ATOM 4822 O O . THR B 2 255 ? -18.712 1.298 -23.562 1.00 106.07 ? 255 THR B O 1 ATOM 4823 C CB . THR B 2 255 ? -19.894 0.465 -20.640 1.00 103.66 ? 255 THR B CB 1 ATOM 4824 O OG1 . THR B 2 255 ? -21.025 -0.386 -20.871 1.00 103.66 ? 255 THR B OG1 1 ATOM 4825 C CG2 . THR B 2 255 ? -19.883 0.900 -19.183 1.00 98.63 ? 255 THR B CG2 1 ATOM 4826 N N . GLN B 2 256 ? -20.901 0.782 -23.621 1.00 132.84 ? 256 GLN B N 1 ATOM 4827 C CA . GLN B 2 256 ? -20.883 0.386 -25.025 1.00 140.00 ? 256 GLN B CA 1 ATOM 4828 C C . GLN B 2 256 ? -20.728 1.598 -25.934 1.00 136.18 ? 256 GLN B C 1 ATOM 4829 O O . GLN B 2 256 ? -20.199 1.493 -27.040 1.00 139.44 ? 256 GLN B O 1 ATOM 4830 C CB . GLN B 2 256 ? -22.165 -0.356 -25.400 1.00 151.70 ? 256 GLN B CB 1 ATOM 4831 C CG . GLN B 2 256 ? -22.596 -1.428 -24.424 1.00 160.17 ? 256 GLN B CG 1 ATOM 4832 C CD . GLN B 2 256 ? -24.061 -1.778 -24.583 1.00 168.18 ? 256 GLN B CD 1 ATOM 4833 O OE1 . GLN B 2 256 ? -24.855 -0.968 -25.063 1.00 172.75 ? 256 GLN B OE1 1 ATOM 4834 N NE2 . GLN B 2 256 ? -24.431 -2.986 -24.177 1.00 171.02 ? 256 GLN B NE2 1 ATOM 4835 N N . LEU B 2 257 ? -21.205 2.744 -25.458 1.00 117.60 ? 257 LEU B N 1 ATOM 4836 C CA . LEU B 2 257 ? -21.263 3.956 -26.269 1.00 107.06 ? 257 LEU B CA 1 ATOM 4837 C C . LEU B 2 257 ? -19.894 4.558 -26.545 1.00 106.93 ? 257 LEU B C 1 ATOM 4838 O O . LEU B 2 257 ? -18.890 4.145 -25.968 1.00 106.31 ? 257 LEU B O 1 ATOM 4839 C CB . LEU B 2 257 ? -22.151 5.005 -25.598 1.00 94.85 ? 257 LEU B CB 1 ATOM 4840 C CG . LEU B 2 257 ? -23.646 4.890 -25.893 1.00 87.35 ? 257 LEU B CG 1 ATOM 4841 C CD1 . LEU B 2 257 ? -24.390 6.109 -25.380 1.00 81.13 ? 257 LEU B CD1 1 ATOM 4842 C CD2 . LEU B 2 257 ? -23.870 4.710 -27.384 1.00 89.62 ? 257 LEU B CD2 1 ATOM 4843 N N . THR B 2 258 ? -19.871 5.542 -27.437 1.00 108.52 ? 258 THR B N 1 ATOM 4844 C CA . THR B 2 258 ? -18.632 6.187 -27.848 1.00 107.49 ? 258 THR B CA 1 ATOM 4845 C C . THR B 2 258 ? -18.710 7.704 -27.674 1.00 109.34 ? 258 THR B C 1 ATOM 4846 O O . THR B 2 258 ? -19.796 8.268 -27.525 1.00 113.87 ? 258 THR B O 1 ATOM 4847 C CB . THR B 2 258 ? -18.293 5.855 -29.313 1.00 110.73 ? 258 THR B CB 1 ATOM 4848 O OG1 . THR B 2 258 ? -19.283 6.425 -30.176 1.00 113.99 ? 258 THR B OG1 1 ATOM 4849 C CG2 . THR B 2 258 ? -18.252 4.348 -29.523 1.00 112.90 ? 258 THR B CG2 1 ATOM 4850 N N . ARG B 2 259 ? -17.551 8.355 -27.698 1.00 106.69 ? 259 ARG B N 1 ATOM 4851 C CA . ARG B 2 259 ? -17.452 9.795 -27.466 1.00 100.78 ? 259 ARG B CA 1 ATOM 4852 C C . ARG B 2 259 ? -18.121 10.590 -28.583 1.00 105.72 ? 259 ARG B C 1 ATOM 4853 O O . ARG B 2 259 ? -18.540 11.734 -28.388 1.00 108.46 ? 259 ARG B O 1 ATOM 4854 C CB . ARG B 2 259 ? -15.980 10.203 -27.329 1.00 101.46 ? 259 ARG B CB 1 ATOM 4855 C CG . ARG B 2 259 ? -15.053 9.025 -27.028 1.00 110.59 ? 259 ARG B CG 1 ATOM 4856 C CD . ARG B 2 259 ? -13.999 9.354 -25.973 1.00 123.02 ? 259 ARG B CD 1 ATOM 4857 N NE . ARG B 2 259 ? -14.084 8.460 -24.817 1.00 132.80 ? 259 ARG B NE 1 ATOM 4858 C CZ . ARG B 2 259 ? -13.116 8.294 -23.919 1.00 136.90 ? 259 ARG B CZ 1 ATOM 4859 N NH1 . ARG B 2 259 ? -11.973 8.955 -24.043 1.00 139.79 ? 259 ARG B NH1 1 ATOM 4860 N NH2 . ARG B 2 259 ? -13.287 7.459 -22.900 1.00 133.26 ? 259 ARG B NH2 1 ATOM 4861 N N . GLN B 2 260 ? -18.227 9.963 -29.750 1.00 109.09 ? 260 GLN B N 1 ATOM 4862 C CA . GLN B 2 260 ? -18.780 10.598 -30.940 1.00 111.97 ? 260 GLN B CA 1 ATOM 4863 C C . GLN B 2 260 ? -20.291 10.386 -30.979 1.00 109.99 ? 260 GLN B C 1 ATOM 4864 O O . GLN B 2 260 ? -21.037 11.214 -31.501 1.00 112.44 ? 260 GLN B O 1 ATOM 4865 C CB . GLN B 2 260 ? -18.117 10.043 -32.206 1.00 117.25 ? 260 GLN B CB 1 ATOM 4866 C CG . GLN B 2 260 ? -16.582 10.087 -32.197 1.00 119.65 ? 260 GLN B CG 1 ATOM 4867 C CD . GLN B 2 260 ? -15.954 9.008 -31.315 1.00 118.14 ? 260 GLN B CD 1 ATOM 4868 O OE1 . GLN B 2 260 ? -16.598 8.015 -30.976 1.00 117.62 ? 260 GLN B OE1 1 ATOM 4869 N NE2 . GLN B 2 260 ? -14.698 9.212 -30.928 1.00 116.78 ? 260 GLN B NE2 1 ATOM 4870 N N . ASP B 2 261 ? -20.726 9.264 -30.411 1.00 109.56 ? 261 ASP B N 1 ATOM 4871 C CA . ASP B 2 261 ? -22.146 8.998 -30.205 1.00 110.38 ? 261 ASP B CA 1 ATOM 4872 C C . ASP B 2 261 ? -22.740 10.014 -29.232 1.00 111.38 ? 261 ASP B C 1 ATOM 4873 O O . ASP B 2 261 ? -23.949 10.214 -29.192 1.00 116.66 ? 261 ASP B O 1 ATOM 4874 C CB . ASP B 2 261 ? -22.363 7.581 -29.667 1.00 115.66 ? 261 ASP B CB 1 ATOM 4875 C CG . ASP B 2 261 ? -22.481 6.538 -30.768 1.00 126.64 ? 261 ASP B CG 1 ATOM 4876 O OD1 . ASP B 2 261 ? -23.192 6.795 -31.764 1.00 130.35 ? 261 ASP B OD1 1 ATOM 4877 O OD2 . ASP B 2 261 ? -21.872 5.459 -30.632 1.00 130.79 ? 261 ASP B OD2 1 ATOM 4878 N N . LEU B 2 262 ? -21.863 10.644 -28.454 1.00 111.23 ? 262 LEU B N 1 ATOM 4879 C CA . LEU B 2 262 ? -22.289 11.564 -27.402 1.00 101.31 ? 262 LEU B CA 1 ATOM 4880 C C . LEU B 2 262 ? -22.177 13.029 -27.808 1.00 111.29 ? 262 LEU B C 1 ATOM 4881 O O . LEU B 2 262 ? -22.805 13.889 -27.197 1.00 108.48 ? 262 LEU B O 1 ATOM 4882 C CB . LEU B 2 262 ? -21.470 11.296 -26.137 1.00 89.21 ? 262 LEU B CB 1 ATOM 4883 C CG . LEU B 2 262 ? -22.156 10.289 -25.211 1.00 89.06 ? 262 LEU B CG 1 ATOM 4884 C CD1 . LEU B 2 262 ? -21.184 9.633 -24.245 1.00 84.36 ? 262 LEU B CD1 1 ATOM 4885 C CD2 . LEU B 2 262 ? -23.253 10.999 -24.457 1.00 94.43 ? 262 LEU B CD2 1 ATOM 4886 N N . CYS B 2 263 ? -21.391 13.314 -28.844 1.00 126.33 ? 263 CYS B N 1 ATOM 4887 C CA . CYS B 2 263 ? -21.273 14.676 -29.354 1.00 135.70 ? 263 CYS B CA 1 ATOM 4888 C C . CYS B 2 263 ? -21.732 14.756 -30.802 1.00 85.77 ? 263 CYS B C 1 ATOM 4889 O O . CYS B 2 263 ? -22.291 15.765 -31.229 1.00 87.86 ? 263 CYS B O 1 ATOM 4890 C CB . CYS B 2 263 ? -19.833 15.174 -29.231 1.00 133.44 ? 263 CYS B CB 1 ATOM 4891 S SG . CYS B 2 263 ? -19.248 15.285 -27.520 1.00 167.69 ? 263 CYS B SG 1 HETATM 4892 C C1 . NAG C 3 . ? -51.674 26.630 -22.479 1.00 110.96 ? 501 NAG A C1 1 HETATM 4893 C C2 . NAG C 3 . ? -52.504 27.864 -22.123 1.00 107.19 ? 501 NAG A C2 1 HETATM 4894 C C3 . NAG C 3 . ? -51.738 29.134 -22.478 1.00 107.03 ? 501 NAG A C3 1 HETATM 4895 C C4 . NAG C 3 . ? -50.381 29.132 -21.787 1.00 106.13 ? 501 NAG A C4 1 HETATM 4896 C C5 . NAG C 3 . ? -49.612 27.869 -22.162 1.00 109.10 ? 501 NAG A C5 1 HETATM 4897 C C6 . NAG C 3 . ? -48.298 27.737 -21.425 1.00 105.55 ? 501 NAG A C6 1 HETATM 4898 C C7 . NAG C 3 . ? -54.884 27.273 -22.249 1.00 110.43 ? 501 NAG A C7 1 HETATM 4899 C C8 . NAG C 3 . ? -56.137 27.341 -23.070 1.00 112.79 ? 501 NAG A C8 1 HETATM 4900 N N2 . NAG C 3 . ? -53.798 27.840 -22.786 1.00 106.27 ? 501 NAG A N2 1 HETATM 4901 O O3 . NAG C 3 . ? -52.492 30.275 -22.083 1.00 107.56 ? 501 NAG A O3 1 HETATM 4902 O O4 . NAG C 3 . ? -49.630 30.281 -22.161 1.00 99.35 ? 501 NAG A O4 1 HETATM 4903 O O5 . NAG C 3 . ? -50.390 26.707 -21.833 1.00 107.70 ? 501 NAG A O5 1 HETATM 4904 O O6 . NAG C 3 . ? -48.242 28.593 -20.291 1.00 95.48 ? 501 NAG A O6 1 HETATM 4905 O O7 . NAG C 3 . ? -54.857 26.728 -21.150 1.00 111.92 ? 501 NAG A O7 1 HETATM 4906 C C1 . NAG D 3 . ? -63.716 9.661 -31.910 1.00 106.94 ? 502 NAG A C1 1 HETATM 4907 C C2 . NAG D 3 . ? -64.635 9.748 -33.141 1.00 106.68 ? 502 NAG A C2 1 HETATM 4908 C C3 . NAG D 3 . ? -66.023 9.173 -32.831 1.00 108.06 ? 502 NAG A C3 1 HETATM 4909 C C4 . NAG D 3 . ? -65.917 7.793 -32.197 1.00 110.80 ? 502 NAG A C4 1 HETATM 4910 C C5 . NAG D 3 . ? -65.009 7.863 -30.977 1.00 108.34 ? 502 NAG A C5 1 HETATM 4911 C C6 . NAG D 3 . ? -64.813 6.526 -30.298 1.00 103.51 ? 502 NAG A C6 1 HETATM 4912 C C7 . NAG D 3 . ? -63.791 11.768 -34.275 1.00 101.60 ? 502 NAG A C7 1 HETATM 4913 C C8 . NAG D 3 . ? -64.103 13.180 -34.674 1.00 101.89 ? 502 NAG A C8 1 HETATM 4914 N N2 . NAG D 3 . ? -64.753 11.123 -33.604 1.00 105.32 ? 502 NAG A N2 1 HETATM 4915 O O3 . NAG D 3 . ? -66.773 9.084 -34.038 1.00 109.41 ? 502 NAG A O3 1 HETATM 4916 O O4 . NAG D 3 . ? -67.208 7.330 -31.818 1.00 109.70 ? 502 NAG A O4 1 HETATM 4917 O O5 . NAG D 3 . ? -63.715 8.318 -31.395 1.00 107.72 ? 502 NAG A O5 1 HETATM 4918 O O6 . NAG D 3 . ? -63.999 6.642 -29.138 1.00 93.66 ? 502 NAG A O6 1 HETATM 4919 O O7 . NAG D 3 . ? -62.717 11.241 -34.543 1.00 99.16 ? 502 NAG A O7 1 HETATM 4920 C C1 . NAG E 3 . ? -29.834 16.865 -20.586 1.00 88.02 ? 301 NAG B C1 1 HETATM 4921 C C2 . NAG E 3 . ? -30.792 17.835 -19.888 1.00 89.16 ? 301 NAG B C2 1 HETATM 4922 C C3 . NAG E 3 . ? -31.069 19.049 -20.771 1.00 90.88 ? 301 NAG B C3 1 HETATM 4923 C C4 . NAG E 3 . ? -29.761 19.696 -21.210 1.00 87.94 ? 301 NAG B C4 1 HETATM 4924 C C5 . NAG E 3 . ? -28.860 18.665 -21.879 1.00 86.81 ? 301 NAG B C5 1 HETATM 4925 C C6 . NAG E 3 . ? -27.499 19.222 -22.233 1.00 89.44 ? 301 NAG B C6 1 HETATM 4926 C C7 . NAG E 3 . ? -32.297 16.808 -18.250 1.00 104.83 ? 301 NAG B C7 1 HETATM 4927 C C8 . NAG E 3 . ? -33.613 16.141 -18.026 1.00 107.73 ? 301 NAG B C8 1 HETATM 4928 N N2 . NAG E 3 . ? -32.033 17.175 -19.510 1.00 91.96 ? 301 NAG B N2 1 HETATM 4929 O O3 . NAG E 3 . ? -31.866 19.986 -20.053 1.00 97.41 ? 301 NAG B O3 1 HETATM 4930 O O4 . NAG E 3 . ? -30.012 20.772 -22.108 1.00 92.42 ? 301 NAG B O4 1 HETATM 4931 O O5 . NAG E 3 . ? -28.644 17.562 -20.985 1.00 91.35 ? 301 NAG B O5 1 HETATM 4932 O O6 . NAG E 3 . ? -26.445 18.491 -21.618 1.00 98.08 ? 301 NAG B O6 1 HETATM 4933 O O7 . NAG E 3 . ? -31.495 16.995 -17.330 1.00 116.22 ? 301 NAG B O7 1 HETATM 4934 C C1 . NAG F 3 . ? -25.497 5.900 30.654 1.00 135.76 ? 302 NAG B C1 1 HETATM 4935 C C2 . NAG F 3 . ? -26.867 6.526 30.881 1.00 138.33 ? 302 NAG B C2 1 HETATM 4936 C C3 . NAG F 3 . ? -26.755 7.678 31.884 1.00 137.27 ? 302 NAG B C3 1 HETATM 4937 C C4 . NAG F 3 . ? -26.054 7.211 33.155 1.00 139.07 ? 302 NAG B C4 1 HETATM 4938 C C5 . NAG F 3 . ? -24.732 6.526 32.812 1.00 133.79 ? 302 NAG B C5 1 HETATM 4939 C C6 . NAG F 3 . ? -24.047 5.920 34.016 1.00 132.08 ? 302 NAG B C6 1 HETATM 4940 C C7 . NAG F 3 . ? -28.171 6.202 28.817 1.00 136.72 ? 302 NAG B C7 1 HETATM 4941 C C8 . NAG F 3 . ? -28.720 6.857 27.584 1.00 131.84 ? 302 NAG B C8 1 HETATM 4942 N N2 . NAG F 3 . ? -27.454 6.987 29.632 1.00 137.50 ? 302 NAG B N2 1 HETATM 4943 O O3 . NAG F 3 . ? -28.053 8.175 32.191 1.00 137.09 ? 302 NAG B O3 1 HETATM 4944 O O4 . NAG F 3 . ? -25.795 8.321 34.006 1.00 146.11 ? 302 NAG B O4 1 HETATM 4945 O O5 . NAG F 3 . ? -24.971 5.455 31.888 1.00 137.25 ? 302 NAG B O5 1 HETATM 4946 O O6 . NAG F 3 . ? -24.252 6.720 35.172 1.00 141.78 ? 302 NAG B O6 1 HETATM 4947 O O7 . NAG F 3 . ? -28.365 5.019 29.061 1.00 139.64 ? 302 NAG B O7 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . GLU A 1 ? 1.2611 1.3076 2.0024 0.0254 -0.0097 0.3075 28 GLU A N 2 C CA . GLU A 1 ? 1.2213 1.2806 1.9039 0.0373 0.0115 0.2798 28 GLU A CA 3 C C . GLU A 1 ? 1.1967 1.2167 1.8439 0.0417 0.0026 0.2425 28 GLU A C 4 O O . GLU A 1 ? 1.2327 1.2259 1.8994 0.0415 -0.0135 0.2428 28 GLU A O 5 C CB . GLU A 1 ? 1.2458 1.3518 1.9276 0.0498 0.0356 0.3011 28 GLU A CB 6 C CG . GLU A 1 ? 1.2838 1.4393 1.9783 0.0532 0.0525 0.3295 28 GLU A CG 7 C CD . GLU A 1 ? 1.3097 1.5096 2.0039 0.0685 0.0738 0.3501 28 GLU A CD 8 O OE1 . GLU A 1 ? 1.3597 1.5504 2.0605 0.0723 0.0718 0.3515 28 GLU A OE1 9 O OE2 . GLU A 1 ? 1.2827 1.5262 1.9688 0.0781 0.0916 0.3637 28 GLU A OE2 10 N N . THR A 2 ? 1.1349 1.1514 1.7314 0.0461 0.0118 0.2111 29 THR A N 11 C CA . THR A 2 ? 1.0700 1.0554 1.6302 0.0521 0.0057 0.1767 29 THR A CA 12 C C . THR A 2 ? 1.0367 1.0473 1.5508 0.0621 0.0294 0.1607 29 THR A C 13 O O . THR A 2 ? 1.0063 1.0428 1.5065 0.0616 0.0433 0.1629 29 THR A O 14 C CB . THR A 2 ? 1.0906 1.0368 1.6366 0.0462 -0.0140 0.1508 29 THR A CB 15 O OG1 . THR A 2 ? 1.1398 1.1004 1.6587 0.0435 -0.0028 0.1407 29 THR A OG1 16 C CG2 . THR A 2 ? 1.1432 1.0644 1.7372 0.0353 -0.0399 0.1667 29 THR A CG2 17 N N . PRO A 3 ? 1.0408 1.0435 1.5323 0.0716 0.0326 0.1444 30 PRO A N 18 C CA . PRO A 3 ? 0.9535 0.9788 1.4048 0.0807 0.0528 0.1297 30 PRO A CA 19 C C . PRO A 3 ? 0.9945 1.0095 1.4080 0.0787 0.0533 0.1023 30 PRO A C 20 O O . PRO A 3 ? 1.0157 1.0018 1.4302 0.0726 0.0370 0.0912 30 PRO A O 21 C CB . PRO A 3 ? 0.8791 0.8938 1.3237 0.0903 0.0517 0.1216 30 PRO A CB 22 C CG . PRO A 3 ? 0.9785 0.9551 1.4481 0.0867 0.0275 0.1213 30 PRO A CG 23 C CD . PRO A 3 ? 1.0765 1.0535 1.5863 0.0749 0.0178 0.1451 30 PRO A CD 24 N N . PRO A 4 ? 1.0202 1.0585 1.4026 0.0838 0.0703 0.0924 31 PRO A N 25 C CA . PRO A 4 ? 1.0509 1.0817 1.4012 0.0810 0.0707 0.0699 31 PRO A CA 26 C C . PRO A 4 ? 1.1414 1.1446 1.4683 0.0852 0.0615 0.0454 31 PRO A C 27 O O . PRO A 4 ? 1.1169 1.1140 1.4419 0.0933 0.0605 0.0418 31 PRO A O 28 C CB . PRO A 4 ? 1.0485 1.1115 1.3773 0.0863 0.0892 0.0682 31 PRO A CB 29 C CG . PRO A 4 ? 1.0406 1.1303 1.3919 0.0913 0.0982 0.0919 31 PRO A CG 30 C CD . PRO A 4 ? 1.0483 1.1216 1.4262 0.0921 0.0884 0.1028 31 PRO A CD 31 N N . ARG A 5 ? 1.2811 1.2699 1.5896 0.0811 0.0553 0.0294 32 ARG A N 32 C CA . ARG A 5 ? 1.3762 1.3438 1.6583 0.0875 0.0477 0.0060 32 ARG A CA 33 C C . ARG A 5 ? 1.3533 1.3276 1.6069 0.0848 0.0535 -0.0074 32 ARG A C 34 O O . ARG A 5 ? 1.3904 1.3638 1.6492 0.0758 0.0507 -0.0041 32 ARG A O 35 C CB . ARG A 5 ? 1.5182 1.4495 1.8140 0.0871 0.0248 0.0004 32 ARG A CB 36 C CG . ARG A 5 ? 1.7338 1.6522 2.0593 0.0899 0.0145 0.0121 32 ARG A CG 37 C CD . ARG A 5 ? 1.9256 1.8474 2.2346 0.1031 0.0207 0.0036 32 ARG A CD 38 N NE . ARG A 5 ? 2.0924 2.0032 2.4317 0.1056 0.0114 0.0167 32 ARG A NE 39 C CZ . ARG A 5 ? 2.1931 2.1267 2.5567 0.1031 0.0222 0.0401 32 ARG A CZ 40 N NH1 . ARG A 5 ? 2.1899 2.1578 2.5488 0.0994 0.0418 0.0509 32 ARG A NH1 41 N NH2 . ARG A 5 ? 2.2622 2.1843 2.6548 0.1053 0.0123 0.0528 32 ARG A NH2 42 N N . PHE A 6 ? 1.1571 1.1392 1.3825 0.0926 0.0612 -0.0211 33 PHE A N 43 C CA . PHE A 6 ? 1.0217 1.0141 1.2236 0.0896 0.0676 -0.0302 33 PHE A CA 44 C C . PHE A 6 ? 1.0085 0.9765 1.2007 0.0889 0.0535 -0.0428 33 PHE A C 45 O O . PHE A 6 ? 1.0807 1.0265 1.2689 0.0975 0.0410 -0.0530 33 PHE A O 46 C CB . PHE A 6 ? 0.9438 0.9536 1.1222 0.0980 0.0788 -0.0383 33 PHE A CB 47 C CG . PHE A 6 ? 0.8746 0.9106 1.0590 0.0983 0.0926 -0.0279 33 PHE A CG 48 C CD1 . PHE A 6 ? 0.7868 0.8418 0.9746 0.0907 0.1002 -0.0206 33 PHE A CD1 49 C CD2 . PHE A 6 ? 0.8381 0.8796 1.0233 0.1078 0.0968 -0.0269 33 PHE A CD2 50 C CE1 . PHE A 6 ? 0.7073 0.7857 0.8989 0.0933 0.1108 -0.0131 33 PHE A CE1 51 C CE2 . PHE A 6 ? 0.7408 0.8067 0.9306 0.1092 0.1086 -0.0183 33 PHE A CE2 52 C CZ . PHE A 6 ? 0.7192 0.8036 0.9120 0.1023 0.1152 -0.0118 33 PHE A CZ 53 N N . THR A 7 ? 0.8927 0.8638 1.0810 0.0799 0.0540 -0.0427 34 THR A N 54 C CA . THR A 7 ? 0.9373 0.8898 1.1109 0.0808 0.0427 -0.0560 34 THR A CA 55 C C . THR A 7 ? 0.9311 0.8998 1.0766 0.0834 0.0524 -0.0643 34 THR A C 56 O O . THR A 7 ? 0.9578 0.9164 1.0842 0.0893 0.0457 -0.0765 34 THR A O 57 C CB . THR A 7 ? 0.9609 0.9029 1.1516 0.0689 0.0341 -0.0496 34 THR A CB 58 O OG1 . THR A 7 ? 0.9364 0.9003 1.1253 0.0601 0.0460 -0.0422 34 THR A OG1 59 C CG2 . THR A 7 ? 0.9461 0.8786 1.1707 0.0646 0.0260 -0.0356 34 THR A CG2 60 N N . ARG A 8 ? 0.7641 0.7588 0.9085 0.0797 0.0671 -0.0566 35 ARG A N 61 C CA . ARG A 8 ? 0.6775 0.6911 0.8013 0.0811 0.0764 -0.0605 35 ARG A CA 62 C C . ARG A 8 ? 0.7072 0.7449 0.8322 0.0834 0.0892 -0.0544 35 ARG A C 63 O O . ARG A 8 ? 0.7364 0.7851 0.8756 0.0772 0.0942 -0.0451 35 ARG A O 64 C CB . ARG A 8 ? 0.7095 0.7279 0.8323 0.0698 0.0770 -0.0579 35 ARG A CB 65 C CG . ARG A 8 ? 0.8939 0.9302 0.9988 0.0705 0.0842 -0.0601 35 ARG A CG 66 C CD . ARG A 8 ? 1.0201 1.0542 1.1213 0.0614 0.0809 -0.0601 35 ARG A CD 67 N NE . ARG A 8 ? 1.0624 1.1112 1.1468 0.0643 0.0854 -0.0615 35 ARG A NE 68 C CZ . ARG A 8 ? 1.1385 1.1884 1.2170 0.0581 0.0834 -0.0609 35 ARG A CZ 69 N NH1 . ARG A 8 ? 1.2258 1.2619 1.3124 0.0489 0.0768 -0.0607 35 ARG A NH1 70 N NH2 . ARG A 8 ? 1.1039 1.1707 1.1697 0.0614 0.0883 -0.0589 35 ARG A NH2 71 N N . THR A 9 ? 0.8128 0.8601 0.9225 0.0937 0.0939 -0.0595 36 THR A N 72 C CA . THR A 9 ? 0.8624 0.9335 0.9733 0.0961 0.1052 -0.0540 36 THR A CA 73 C C . THR A 9 ? 0.9607 1.0540 1.0614 0.0930 0.1122 -0.0520 36 THR A C 74 O O . THR A 9 ? 1.0694 1.1622 1.1558 0.0958 0.1103 -0.0564 36 THR A O 75 C CB . THR A 9 ? 0.8680 0.9379 0.9725 0.1104 0.1062 -0.0586 36 THR A CB 76 O OG1 . THR A 9 ? 1.0074 1.0775 1.0905 0.1211 0.1045 -0.0675 36 THR A OG1 77 C CG2 . THR A 9 ? 0.8163 0.8616 0.9335 0.1134 0.0965 -0.0598 36 THR A CG2 78 N N . PRO A 10 ? 0.9306 1.0443 1.0399 0.0882 0.1195 -0.0446 37 PRO A N 79 C CA . PRO A 10 ? 0.9808 1.1160 1.0868 0.0837 0.1241 -0.0402 37 PRO A CA 80 C C . PRO A 10 ? 1.0174 1.1687 1.1111 0.0945 0.1299 -0.0404 37 PRO A C 81 O O . PRO A 10 ? 1.0741 1.2232 1.1632 0.1059 0.1318 -0.0441 37 PRO A O 82 C CB . PRO A 10 ? 0.9633 1.1119 1.0838 0.0781 0.1270 -0.0340 37 PRO A CB 83 C CG . PRO A 10 ? 0.9351 1.0779 1.0613 0.0854 0.1286 -0.0346 37 PRO A CG 84 C CD . PRO A 10 ? 0.9223 1.0402 1.0463 0.0875 0.1222 -0.0393 37 PRO A CD 85 N N . VAL A 11 ? 0.9318 1.0998 1.0207 0.0917 0.1323 -0.0354 38 VAL A N 86 C CA . VAL A 11 ? 0.8881 1.0787 0.9673 0.1026 0.1393 -0.0318 38 VAL A CA 87 C C . VAL A 11 ? 0.8417 1.0610 0.9345 0.0951 0.1445 -0.0191 38 VAL A C 88 O O . VAL A 11 ? 0.8197 1.0401 0.9259 0.0811 0.1406 -0.0140 38 VAL A O 89 C CB . VAL A 11 ? 0.9161 1.1073 0.9775 0.1098 0.1380 -0.0341 38 VAL A CB 90 C CG1 . VAL A 11 ? 0.9648 1.1304 1.0103 0.1231 0.1316 -0.0483 38 VAL A CG1 91 C CG2 . VAL A 11 ? 0.9608 1.1480 1.0274 0.0957 0.1335 -0.0300 38 VAL A CG2 92 N N . ASP A 12 ? 0.6991 0.9413 0.7900 0.1049 0.1519 -0.0141 39 ASP A N 93 C CA . ASP A 12 ? 0.5572 0.8288 0.6642 0.0981 0.1557 -0.0002 39 ASP A CA 94 C C . ASP A 12 ? 0.6982 0.9807 0.8120 0.0871 0.1531 0.0103 39 ASP A C 95 O O . ASP A 12 ? 0.8347 1.1153 0.9346 0.0917 0.1534 0.0096 39 ASP A O 96 C CB . ASP A 12 ? 0.6234 0.9215 0.7248 0.1123 0.1647 0.0055 39 ASP A CB 97 C CG . ASP A 12 ? 0.8034 1.0923 0.8999 0.1232 0.1670 -0.0036 39 ASP A CG 98 O OD1 . ASP A 12 ? 0.8449 1.1154 0.9499 0.1167 0.1627 -0.0094 39 ASP A OD1 99 O OD2 . ASP A 12 ? 0.9052 1.2066 0.9892 0.1394 0.1732 -0.0043 39 ASP A OD2 100 N N . GLN A 13 ? 0.7636 1.0568 0.8995 0.0733 0.1490 0.0197 40 GLN A N 101 C CA . GLN A 13 ? 0.7848 1.0860 0.9321 0.0609 0.1442 0.0307 40 GLN A CA 102 C C . GLN A 13 ? 0.7712 1.1055 0.9405 0.0557 0.1455 0.0491 40 GLN A C 103 O O . GLN A 13 ? 0.8026 1.1448 0.9851 0.0546 0.1446 0.0503 40 GLN A O 104 C CB . GLN A 13 ? 0.8092 1.0861 0.9655 0.0474 0.1331 0.0241 40 GLN A CB 105 C CG . GLN A 13 ? 0.8661 1.1172 1.0058 0.0482 0.1306 0.0134 40 GLN A CG 106 C CD . GLN A 13 ? 1.0548 1.2969 1.2039 0.0342 0.1214 0.0164 40 GLN A CD 107 O OE1 . GLN A 13 ? 1.1333 1.3627 1.2930 0.0263 0.1132 0.0120 40 GLN A OE1 108 N NE2 . GLN A 13 ? 1.1388 1.3886 1.2834 0.0328 0.1224 0.0242 40 GLN A NE2 109 N N . THR A 14 ? 0.7359 1.0908 0.9107 0.0526 0.1471 0.0647 41 THR A N 110 C CA . THR A 14 ? 0.6599 1.0440 0.8639 0.0423 0.1444 0.0857 41 THR A CA 111 C C . THR A 14 ? 0.6666 1.0439 0.8861 0.0262 0.1338 0.0936 41 THR A C 112 O O . THR A 14 ? 0.6927 1.0731 0.9020 0.0279 0.1368 0.0988 41 THR A O 113 C CB . THR A 14 ? 0.6106 1.0346 0.8135 0.0539 0.1568 0.1037 41 THR A CB 114 O OG1 . THR A 14 ? 0.6233 1.0486 0.8050 0.0721 0.1664 0.0927 41 THR A OG1 115 C CG2 . THR A 14 ? 0.5328 0.9883 0.7715 0.0429 0.1533 0.1267 41 THR A CG2 116 N N . GLY A 15 ? 0.6799 1.0461 0.9224 0.0120 0.1201 0.0928 42 GLY A N 117 C CA . GLY A 15 ? 0.6687 1.0257 0.9284 -0.0035 0.1070 0.0991 42 GLY A CA 118 C C . GLY A 15 ? 0.6679 1.0489 0.9656 -0.0164 0.0975 0.1213 42 GLY A C 119 O O . GLY A 15 ? 0.6848 1.0916 0.9961 -0.0136 0.1018 0.1326 42 GLY A O 120 N N . VAL A 16 ? 0.7098 1.0814 1.0265 -0.0309 0.0833 0.1279 43 VAL A N 121 C CA . VAL A 16 ? 0.7435 1.1332 1.1015 -0.0457 0.0696 0.1497 43 VAL A CA 122 C C . VAL A 16 ? 0.7097 1.0707 1.0836 -0.0552 0.0473 0.1355 43 VAL A C 123 O O . VAL A 16 ? 0.7307 1.0605 1.0875 -0.0547 0.0413 0.1162 43 VAL A O 124 C CB . VAL A 16 ? 0.5331 0.9379 0.9050 -0.0545 0.0688 0.1725 43 VAL A CB 125 C CG1 . VAL A 16 ? 0.6356 1.0110 0.9821 -0.0538 0.0683 0.1572 43 VAL A CG1 126 C CG2 . VAL A 16 ? 0.5071 0.9203 0.9263 -0.0731 0.0486 0.1930 43 VAL A CG2 127 N N . SER A 17 ? 0.6420 1.0148 1.0475 -0.0618 0.0350 0.1442 44 SER A N 128 C CA . SER A 17 ? 0.7045 1.0535 1.1285 -0.0692 0.0103 0.1320 44 SER A CA 129 C C . SER A 17 ? 0.7584 1.0839 1.1920 -0.0803 -0.0074 0.1306 44 SER A C 130 O O . SER A 17 ? 0.8652 1.2039 1.3179 -0.0909 -0.0092 0.1523 44 SER A O 131 C CB . SER A 17 ? 0.8000 1.1704 1.2643 -0.0771 -0.0027 0.1485 44 SER A CB 132 O OG . SER A 17 ? 0.8961 1.2418 1.3764 -0.0814 -0.0289 0.1338 44 SER A OG 133 N N . GLY A 18 ? 0.7911 1.0837 1.2114 -0.0767 -0.0204 0.1057 45 GLY A N 134 C CA . GLY A 18 ? 0.8333 1.1008 1.2582 -0.0845 -0.0375 0.1004 45 GLY A CA 135 C C . GLY A 18 ? 0.8583 1.1129 1.2481 -0.0783 -0.0219 0.0906 45 GLY A C 136 O O . GLY A 18 ? 0.8837 1.1135 1.2665 -0.0802 -0.0327 0.0794 45 GLY A O 137 N N . GLY A 19 ? 0.8062 1.0770 1.1735 -0.0699 0.0026 0.0940 46 GLY A N 138 C CA . GLY A 19 ? 0.7607 1.0208 1.0964 -0.0637 0.0169 0.0859 46 GLY A CA 139 C C . GLY A 19 ? 0.6918 0.9309 0.9972 -0.0511 0.0230 0.0611 46 GLY A C 140 O O . GLY A 19 ? 0.6586 0.8848 0.9664 -0.0476 0.0119 0.0474 46 GLY A O 141 N N . VAL A 20 ? 0.7506 0.9871 1.0287 -0.0433 0.0397 0.0562 47 VAL A N 142 C CA . VAL A 20 ? 0.7384 0.9563 0.9909 -0.0323 0.0461 0.0364 47 VAL A CA 143 C C . VAL A 20 ? 0.6534 0.8836 0.8885 -0.0211 0.0646 0.0360 47 VAL A C 144 O O . VAL A 20 ? 0.6148 0.8627 0.8471 -0.0199 0.0747 0.0480 47 VAL A O 145 C CB . VAL A 20 ? 0.4915 0.6881 0.7284 -0.0336 0.0448 0.0284 47 VAL A CB 146 C CG1 . VAL A 20 ? 0.4876 0.6672 0.7039 -0.0233 0.0496 0.0110 47 VAL A CG1 147 C CG2 . VAL A 20 ? 0.5521 0.7369 0.8059 -0.0441 0.0259 0.0297 47 VAL A CG2 148 N N . ALA A 21 ? 0.6300 0.8517 0.8534 -0.0115 0.0686 0.0227 48 ALA A N 149 C CA . ALA A 21 ? 0.6476 0.8715 0.8511 -0.0002 0.0839 0.0184 48 ALA A CA 150 C C . ALA A 21 ? 0.7440 0.9451 0.9321 0.0058 0.0844 0.0034 48 ALA A C 151 O O . ALA A 21 ? 0.8316 1.0234 1.0248 0.0057 0.0760 -0.0038 48 ALA A O 152 C CB . ALA A 21 ? 0.6327 0.8755 0.8415 0.0064 0.0902 0.0220 48 ALA A CB 153 N N . SER A 22 ? 0.6956 0.8889 0.8661 0.0118 0.0932 -0.0007 49 SER A N 154 C CA . SER A 22 ? 0.7019 0.8757 0.8620 0.0169 0.0937 -0.0117 49 SER A CA 155 C C . SER A 22 ? 0.8187 0.9925 0.9673 0.0278 0.1037 -0.0150 49 SER A C 156 O O . SER A 22 ? 0.8969 1.0783 1.0371 0.0321 0.1099 -0.0120 49 SER A O 157 C CB . SER A 22 ? 0.6790 0.8362 0.8323 0.0117 0.0893 -0.0144 49 SER A CB 158 O OG . SER A 22 ? 0.6505 0.8051 0.8146 0.0025 0.0786 -0.0126 49 SER A OG 159 N N . PHE A 23 ? 0.7955 0.9614 0.9438 0.0335 0.1047 -0.0208 50 PHE A N 160 C CA . PHE A 23 ? 0.7621 0.9232 0.9021 0.0433 0.1116 -0.0243 50 PHE A CA 161 C C . PHE A 23 ? 0.8048 0.9458 0.9425 0.0437 0.1087 -0.0290 50 PHE A C 162 O O . PHE A 23 ? 0.7665 0.9038 0.9110 0.0409 0.1044 -0.0293 50 PHE A O 163 C CB . PHE A 23 ? 0.6811 0.8542 0.8269 0.0503 0.1160 -0.0234 50 PHE A CB 164 C CG . PHE A 23 ? 0.7162 0.9106 0.8662 0.0505 0.1191 -0.0175 50 PHE A CG 165 C CD1 . PHE A 23 ? 0.7972 1.0003 0.9386 0.0577 0.1265 -0.0156 50 PHE A CD1 166 C CD2 . PHE A 23 ? 0.7267 0.9332 0.8902 0.0447 0.1134 -0.0136 50 PHE A CD2 167 C CE1 . PHE A 23 ? 0.7562 0.9828 0.9033 0.0586 0.1302 -0.0077 50 PHE A CE1 168 C CE2 . PHE A 23 ? 0.7342 0.9616 0.9059 0.0438 0.1152 -0.0059 50 PHE A CE2 169 C CZ . PHE A 23 ? 0.7283 0.9675 0.8923 0.0505 0.1246 -0.0018 50 PHE A CZ 170 N N . ILE A 24 ? 0.8569 0.9858 0.9856 0.0482 0.1100 -0.0324 51 ILE A N 171 C CA . ILE A 24 ? 0.9084 1.0179 1.0382 0.0472 0.1055 -0.0353 51 ILE A CA 172 C C . ILE A 24 ? 0.9305 1.0330 1.0633 0.0556 0.1075 -0.0362 51 ILE A C 173 O O . ILE A 24 ? 1.0290 1.1327 1.1547 0.0634 0.1105 -0.0388 51 ILE A O 174 C CB . ILE A 24 ? 0.7675 0.8639 0.8866 0.0449 0.1011 -0.0393 51 ILE A CB 175 C CG1 . ILE A 24 ? 0.7305 0.8363 0.8474 0.0370 0.0997 -0.0363 51 ILE A CG1 176 C CG2 . ILE A 24 ? 0.7747 0.8511 0.8983 0.0422 0.0945 -0.0414 51 ILE A CG2 177 C CD1 . ILE A 24 ? 0.7469 0.8456 0.8512 0.0370 0.0971 -0.0389 51 ILE A CD1 178 N N . CYS A 25 ? 0.8688 0.9649 1.0130 0.0548 0.1054 -0.0328 52 CYS A N 179 C CA . CYS A 25 ? 0.7398 0.8295 0.8916 0.0616 0.1062 -0.0306 52 CYS A CA 180 C C . CYS A 25 ? 0.7631 0.8388 0.9269 0.0578 0.1001 -0.0263 52 CYS A C 181 O O . CYS A 25 ? 0.8102 0.8911 0.9799 0.0528 0.0992 -0.0220 52 CYS A O 182 C CB . CYS A 25 ? 0.6396 0.7468 0.7985 0.0672 0.1130 -0.0252 52 CYS A CB 183 S SG . CYS A 25 ? 0.8279 0.9304 0.9961 0.0767 0.1151 -0.0211 52 CYS A SG 184 N N . GLN A 26 ? 0.8584 0.9169 1.0271 0.0607 0.0948 -0.0271 53 GLN A N 185 C CA . GLN A 26 ? 0.8728 0.9179 1.0582 0.0568 0.0875 -0.0207 53 GLN A CA 186 C C . GLN A 26 ? 0.9126 0.9473 1.1115 0.0625 0.0838 -0.0167 53 GLN A C 187 O O . GLN A 26 ? 0.9830 1.0095 1.1720 0.0694 0.0822 -0.0250 53 GLN A O 188 C CB . GLN A 26 ? 0.8917 0.9184 1.0707 0.0511 0.0780 -0.0279 53 GLN A CB 189 C CG . GLN A 26 ? 0.8699 0.9044 1.0385 0.0443 0.0798 -0.0303 53 GLN A CG 190 C CD . GLN A 26 ? 0.9499 0.9665 1.1101 0.0401 0.0707 -0.0379 53 GLN A CD 191 O OE1 . GLN A 26 ? 1.0410 1.0469 1.1876 0.0453 0.0669 -0.0473 53 GLN A OE1 192 N NE2 . GLN A 26 ? 0.9424 0.9566 1.1094 0.0325 0.0670 -0.0341 53 GLN A NE2 193 N N . ALA A 27 ? 0.8667 0.9024 1.0890 0.0602 0.0818 -0.0030 54 ALA A N 194 C CA . ALA A 27 ? 0.8891 0.9157 1.1308 0.0641 0.0770 0.0049 54 ALA A CA 195 C C . ALA A 27 ? 0.9856 1.0013 1.2532 0.0572 0.0670 0.0170 54 ALA A C 196 O O . ALA A 27 ? 1.0433 1.0661 1.3142 0.0508 0.0677 0.0219 54 ALA A O 197 C CB . ALA A 27 ? 1.0545 1.1045 1.3038 0.0708 0.0885 0.0160 54 ALA A CB 198 N N . THR A 28 ? 1.0318 1.0293 1.3187 0.0583 0.0563 0.0216 55 THR A N 199 C CA . THR A 28 ? 1.0597 1.0491 1.3796 0.0514 0.0457 0.0378 55 THR A CA 200 C C . THR A 28 ? 1.0053 1.0009 1.3529 0.0551 0.0462 0.0558 55 THR A C 201 O O . THR A 28 ? 0.9735 0.9704 1.3113 0.0633 0.0508 0.0503 55 THR A O 202 C CB . THR A 28 ? 1.1272 1.0823 1.4494 0.0473 0.0258 0.0263 55 THR A CB 203 O OG1 . THR A 28 ? 1.1371 1.0858 1.4935 0.0383 0.0145 0.0429 55 THR A OG1 204 C CG2 . THR A 28 ? 1.1726 1.1039 1.4925 0.0555 0.0148 0.0153 55 THR A CG2 205 N N . GLY A 29 ? 1.0162 1.0140 1.3998 0.0490 0.0397 0.0776 56 GLY A N 206 C CA . GLY A 29 ? 1.0906 1.0965 1.5074 0.0511 0.0392 0.1002 56 GLY A CA 207 C C . GLY A 29 ? 1.1814 1.2052 1.6342 0.0445 0.0388 0.1284 56 GLY A C 208 O O . GLY A 29 ? 1.2613 1.2903 1.7116 0.0387 0.0388 0.1288 56 GLY A O 209 N N . ASP A 30 ? 1.1598 1.1939 1.6481 0.0456 0.0378 0.1536 57 ASP A N 210 C CA . ASP A 30 ? 1.0909 1.1479 1.6180 0.0409 0.0386 0.1855 57 ASP A CA 211 C C . ASP A 30 ? 1.0639 1.1569 1.6091 0.0497 0.0532 0.2119 57 ASP A C 212 O O . ASP A 30 ? 1.1181 1.2035 1.6844 0.0513 0.0478 0.2220 57 ASP A O 213 C CB . ASP A 30 ? 1.0169 1.0440 1.5828 0.0297 0.0147 0.1950 57 ASP A CB 214 C CG . ASP A 30 ? 0.9803 1.0327 1.5973 0.0244 0.0138 0.2350 57 ASP A CG 215 O OD1 . ASP A 30 ? 0.9991 1.0860 1.6166 0.0260 0.0276 0.2497 57 ASP A OD1 216 O OD2 . ASP A 30 ? 0.9525 0.9889 1.6106 0.0190 -0.0024 0.2518 57 ASP A OD2 217 N N . PRO A 31 ? 0.9721 1.1047 1.5077 0.0571 0.0711 0.2226 58 PRO A N 218 C CA . PRO A 31 ? 0.9429 1.0928 1.4569 0.0582 0.0794 0.2162 58 PRO A CA 219 C C . PRO A 31 ? 0.9993 1.1326 1.4649 0.0595 0.0820 0.1800 58 PRO A C 220 O O . PRO A 31 ? 0.9456 1.0637 1.3926 0.0628 0.0820 0.1628 58 PRO A O 221 C CB . PRO A 31 ? 0.8208 1.0197 1.3392 0.0722 0.0979 0.2391 58 PRO A CB 222 C CG . PRO A 31 ? 0.8219 1.0239 1.3412 0.0801 0.1029 0.2416 58 PRO A CG 223 C CD . PRO A 31 ? 0.9054 1.0719 1.4528 0.0689 0.0851 0.2445 58 PRO A CD 224 N N . ARG A 32 ? 1.0173 1.1539 1.4650 0.0570 0.0836 0.1702 59 ARG A N 225 C CA . ARG A 32 ? 1.0101 1.1338 1.4161 0.0574 0.0857 0.1397 59 ARG A CA 226 C C . ARG A 32 ? 0.9691 1.1136 1.3522 0.0697 0.0996 0.1332 59 ARG A C 227 O O . ARG A 32 ? 0.9714 1.1492 1.3597 0.0801 0.1105 0.1489 59 ARG A O 228 C CB . ARG A 32 ? 1.1313 1.2608 1.5252 0.0540 0.0861 0.1346 59 ARG A CB 229 C CG . ARG A 32 ? 1.3364 1.4718 1.6914 0.0594 0.0941 0.1126 59 ARG A CG 230 C CD . ARG A 32 ? 1.4725 1.6130 1.8173 0.0568 0.0933 0.1085 59 ARG A CD 231 N NE . ARG A 32 ? 1.5898 1.7011 1.9368 0.0439 0.0807 0.0998 59 ARG A NE 232 C CZ . ARG A 32 ? 1.6535 1.7663 2.0142 0.0383 0.0755 0.1089 59 ARG A CZ 233 N NH1 . ARG A 32 ? 1.6474 1.7911 2.0205 0.0452 0.0827 0.1279 59 ARG A NH1 234 N NH2 . ARG A 32 ? 1.6885 1.7733 2.0497 0.0274 0.0631 0.0992 59 ARG A NH2 235 N N . PRO A 33 ? 0.9288 1.0552 1.2862 0.0699 0.0988 0.1100 60 PRO A N 236 C CA . PRO A 33 ? 0.8937 1.0355 1.2314 0.0802 0.1096 0.1024 60 PRO A CA 237 C C . PRO A 33 ? 0.9223 1.0798 1.2344 0.0843 0.1161 0.0910 60 PRO A C 238 O O . PRO A 33 ? 0.9546 1.1048 1.2595 0.0777 0.1116 0.0842 60 PRO A O 239 C CB . PRO A 33 ? 0.8828 0.9967 1.2057 0.0774 0.1037 0.0830 60 PRO A CB 240 C CG . PRO A 33 ? 0.9309 1.0144 1.2678 0.0675 0.0887 0.0816 60 PRO A CG 241 C CD . PRO A 33 ? 0.9794 1.0698 1.3274 0.0613 0.0864 0.0913 60 PRO A CD 242 N N . LYS A 34 ? 0.9239 1.1031 1.2240 0.0955 0.1253 0.0894 61 LYS A N 243 C CA . LYS A 34 ? 0.8814 1.0703 1.1570 0.0992 0.1279 0.0750 61 LYS A CA 244 C C . LYS A 34 ? 0.8307 1.0082 1.0871 0.0979 0.1280 0.0568 61 LYS A C 245 O O . LYS A 34 ? 0.8631 1.0330 1.1240 0.0986 0.1290 0.0573 61 LYS A O 246 C CB . LYS A 34 ? 0.9779 1.2009 1.2529 0.1149 0.1358 0.0850 61 LYS A CB 247 C CG . LYS A 34 ? 1.0804 1.3187 1.3557 0.1261 0.1431 0.0892 61 LYS A CG 248 C CD . LYS A 34 ? 1.0976 1.3561 1.3525 0.1393 0.1464 0.0788 61 LYS A CD 249 C CE . LYS A 34 ? 1.0287 1.3221 1.2914 0.1581 0.1542 0.0965 61 LYS A CE 250 N NZ . LYS A 34 ? 0.8764 1.1880 1.1200 0.1734 0.1561 0.0854 61 LYS A NZ 251 N N . ILE A 35 ? 0.8036 0.9815 1.0403 0.0966 0.1266 0.0419 62 ILE A N 252 C CA . ILE A 35 ? 0.8321 1.0023 1.0530 0.0944 0.1265 0.0270 62 ILE A CA 253 C C . ILE A 35 ? 0.8877 1.0779 1.0977 0.1029 0.1289 0.0215 62 ILE A C 254 O O . ILE A 35 ? 0.9822 1.1817 1.1888 0.1062 0.1264 0.0210 62 ILE A O 255 C CB . ILE A 35 ? 0.7934 0.9421 1.0038 0.0825 0.1199 0.0147 62 ILE A CB 256 C CG1 . ILE A 35 ? 0.7901 0.9170 1.0094 0.0768 0.1155 0.0170 62 ILE A CG1 257 C CG2 . ILE A 35 ? 0.8223 0.9714 1.0172 0.0814 0.1207 0.0023 62 ILE A CG2 258 C CD1 . ILE A 35 ? 0.9171 1.0244 1.1224 0.0693 0.1100 0.0036 62 ILE A CD1 259 N N . VAL A 36 ? 0.8276 1.0239 1.0322 0.1075 0.1325 0.0170 63 VAL A N 260 C CA . VAL A 36 ? 0.7683 0.9790 0.9627 0.1136 0.1314 0.0088 63 VAL A CA 261 C C . VAL A 36 ? 0.8226 1.0264 1.0087 0.1072 0.1301 -0.0017 63 VAL A C 262 O O . VAL A 36 ? 0.9796 1.1734 1.1663 0.1036 0.1331 -0.0015 63 VAL A O 263 C CB . VAL A 36 ? 0.6609 0.8946 0.8592 0.1294 0.1372 0.0165 63 VAL A CB 264 C CG1 . VAL A 36 ? 0.6853 0.9331 0.8735 0.1376 0.1330 0.0068 63 VAL A CG1 265 C CG2 . VAL A 36 ? 0.7081 0.9535 0.9174 0.1371 0.1404 0.0316 63 VAL A CG2 266 N N . TRP A 37 ? 0.7581 0.9682 0.9377 0.1067 0.1247 -0.0101 64 TRP A N 267 C CA . TRP A 37 ? 0.8024 1.0119 0.9780 0.1011 0.1235 -0.0166 64 TRP A CA 268 C C . TRP A 37 ? 0.7664 0.9938 0.9425 0.1109 0.1236 -0.0184 64 TRP A C 269 O O . TRP A 37 ? 0.7274 0.9646 0.9028 0.1187 0.1179 -0.0211 64 TRP A O 270 C CB . TRP A 37 ? 0.8117 1.0129 0.9840 0.0900 0.1149 -0.0228 64 TRP A CB 271 C CG . TRP A 37 ? 0.7575 0.9413 0.9279 0.0808 0.1146 -0.0218 64 TRP A CG 272 C CD1 . TRP A 37 ? 0.7359 0.9120 0.9075 0.0794 0.1118 -0.0199 64 TRP A CD1 273 C CD2 . TRP A 37 ? 0.7099 0.8833 0.8761 0.0733 0.1166 -0.0229 64 TRP A CD2 274 N NE1 . TRP A 37 ? 0.7231 0.8829 0.8925 0.0703 0.1111 -0.0203 64 TRP A NE1 275 C CE2 . TRP A 37 ? 0.7323 0.8900 0.8971 0.0674 0.1139 -0.0227 64 TRP A CE2 276 C CE3 . TRP A 37 ? 0.6960 0.8736 0.8587 0.0728 0.1204 -0.0238 64 TRP A CE3 277 C CZ2 . TRP A 37 ? 0.7526 0.8976 0.9115 0.0619 0.1138 -0.0249 64 TRP A CZ2 278 C CZ3 . TRP A 37 ? 0.7495 0.9165 0.9054 0.0685 0.1214 -0.0251 64 TRP A CZ3 279 C CH2 . TRP A 37 ? 0.7347 0.8849 0.8881 0.0635 0.1176 -0.0264 64 TRP A CH2 280 N N . ASN A 38 ? 0.7713 1.0032 0.9478 0.1120 0.1292 -0.0176 65 ASN A N 281 C CA . ASN A 38 ? 0.7361 0.9851 0.9140 0.1211 0.1295 -0.0190 65 ASN A CA 282 C C . ASN A 38 ? 0.8436 1.0969 1.0226 0.1145 0.1270 -0.0225 65 ASN A C 283 O O . ASN A 38 ? 0.9104 1.1558 1.0879 0.1051 0.1288 -0.0218 65 ASN A O 284 C CB . ASN A 38 ? 0.6973 0.9533 0.8772 0.1316 0.1394 -0.0122 65 ASN A CB 285 C CG . ASN A 38 ? 0.7164 0.9729 0.8999 0.1386 0.1426 -0.0041 65 ASN A CG 286 O OD1 . ASN A 38 ? 0.7173 0.9792 0.8998 0.1430 0.1379 -0.0045 65 ASN A OD1 287 N ND2 . ASN A 38 ? 0.7588 1.0105 0.9479 0.1405 0.1498 0.0043 65 ASN A ND2 288 N N . LYS A 39 ? 0.8478 1.1159 1.0302 0.1207 0.1229 -0.0252 66 LYS A N 289 C CA . LYS A 39 ? 0.9195 1.1970 1.1067 0.1167 0.1226 -0.0249 66 LYS A CA 290 C C . LYS A 39 ? 0.9360 1.2286 1.1240 0.1298 0.1271 -0.0242 66 LYS A C 291 O O . LYS A 39 ? 0.8649 1.1652 1.0528 0.1399 0.1217 -0.0276 66 LYS A O 292 C CB . LYS A 39 ? 0.9423 1.2220 1.1377 0.1083 0.1086 -0.0286 66 LYS A CB 293 C CG . LYS A 39 ? 1.0207 1.3143 1.2261 0.1038 0.1074 -0.0251 66 LYS A CG 294 C CD . LYS A 39 ? 1.0750 1.3685 1.2934 0.0917 0.0928 -0.0248 66 LYS A CD 295 C CE . LYS A 39 ? 1.1227 1.4224 1.3510 0.0965 0.0766 -0.0312 66 LYS A CE 296 N NZ . LYS A 39 ? 1.1761 1.4744 1.4220 0.0834 0.0599 -0.0294 66 LYS A NZ 297 N N . LYS A 40 ? 1.0643 1.3617 1.2519 0.1312 0.1367 -0.0201 67 LYS A N 298 C CA . LYS A 40 ? 1.1786 1.4899 1.3669 0.1429 0.1423 -0.0185 67 LYS A CA 299 C C . LYS A 40 ? 1.1412 1.4541 1.3265 0.1555 0.1454 -0.0167 67 LYS A C 300 O O . LYS A 40 ? 1.1459 1.4733 1.3320 0.1673 0.1449 -0.0173 67 LYS A O 301 C CB . LYS A 40 ? 1.2704 1.5979 1.4667 0.1437 0.1337 -0.0215 67 LYS A CB 302 C CG . LYS A 40 ? 1.3764 1.7142 1.5774 0.1395 0.1387 -0.0172 67 LYS A CG 303 C CD . LYS A 40 ? 1.4635 1.8014 1.6572 0.1479 0.1526 -0.0134 67 LYS A CD 304 C CE . LYS A 40 ? 1.5484 1.8930 1.7421 0.1445 0.1589 -0.0092 67 LYS A CE 305 N NZ . LYS A 40 ? 1.5949 1.9609 1.7999 0.1432 0.1549 -0.0065 67 LYS A NZ 306 N N . GLY A 41 ? 1.1243 1.4236 1.3073 0.1533 0.1488 -0.0132 68 GLY A N 307 C CA . GLY A 41 ? 1.1144 1.4162 1.2981 0.1639 0.1538 -0.0064 68 GLY A CA 308 C C . GLY A 41 ? 1.1094 1.4197 1.2914 0.1716 0.1469 -0.0086 68 GLY A C 309 O O . GLY A 41 ? 1.1369 1.4557 1.3198 0.1830 0.1513 -0.0011 68 GLY A O 310 N N . LYS A 42 ? 1.0917 1.4007 1.2718 0.1666 0.1355 -0.0180 69 LYS A N 311 C CA . LYS A 42 ? 1.0601 1.3746 1.2364 0.1753 0.1263 -0.0227 69 LYS A CA 312 C C . LYS A 42 ? 0.9360 1.2339 1.1117 0.1630 0.1202 -0.0254 69 LYS A C 313 O O . LYS A 42 ? 0.8963 1.1825 1.0746 0.1480 0.1170 -0.0283 69 LYS A O 314 C CB . LYS A 42 ? 1.2001 1.5254 1.3759 0.1823 0.1141 -0.0329 69 LYS A CB 315 C CG . LYS A 42 ? 1.3057 1.6489 1.4815 0.1960 0.1195 -0.0308 69 LYS A CG 316 C CD . LYS A 42 ? 1.3933 1.7372 1.5759 0.1864 0.1188 -0.0327 69 LYS A CD 317 C CE . LYS A 42 ? 1.4748 1.8354 1.6574 0.1991 0.1261 -0.0294 69 LYS A CE 318 N NZ . LYS A 42 ? 1.5168 1.8810 1.7070 0.1907 0.1253 -0.0304 69 LYS A NZ 319 N N . LYS A 43 ? 0.9614 1.2604 1.1338 0.1701 0.1193 -0.0231 70 LYS A N 320 C CA . LYS A 43 ? 0.9415 1.2250 1.1130 0.1592 0.1140 -0.0250 70 LYS A CA 321 C C . LYS A 43 ? 1.0008 1.2775 1.1714 0.1526 0.0984 -0.0371 70 LYS A C 322 O O . LYS A 43 ? 0.9344 1.2199 1.1025 0.1636 0.0876 -0.0452 70 LYS A O 323 C CB . LYS A 43 ? 0.8956 1.1858 1.0647 0.1703 0.1163 -0.0188 70 LYS A CB 324 C CG . LYS A 43 ? 0.9277 1.2019 1.0969 0.1589 0.1126 -0.0189 70 LYS A CG 325 C CD . LYS A 43 ? 1.0281 1.3045 1.1901 0.1666 0.0996 -0.0283 70 LYS A CD 326 C CE . LYS A 43 ? 1.1134 1.4083 1.2717 0.1861 0.1034 -0.0209 70 LYS A CE 327 N NZ . LYS A 43 ? 1.1011 1.3914 1.2658 0.1796 0.1113 -0.0082 70 LYS A NZ 328 N N . VAL A 44 ? 1.1324 1.3930 1.3058 0.1353 0.0961 -0.0377 71 VAL A N 329 C CA . VAL A 44 ? 1.1728 1.4258 1.3497 0.1259 0.0812 -0.0458 71 VAL A CA 330 C C . VAL A 44 ? 1.0872 1.3385 1.2593 0.1348 0.0675 -0.0539 71 VAL A C 331 O O . VAL A 44 ? 1.0309 1.2816 1.1968 0.1413 0.0714 -0.0513 71 VAL A O 332 C CB . VAL A 44 ? 0.7245 0.9628 0.9048 0.1069 0.0831 -0.0423 71 VAL A CB 333 C CG1 . VAL A 44 ? 0.7061 0.9461 0.8872 0.1024 0.0969 -0.0352 71 VAL A CG1 334 C CG2 . VAL A 44 ? 0.7335 0.9593 0.9088 0.1036 0.0837 -0.0412 71 VAL A CG2 335 N N . SER A 45 ? 1.0284 1.2795 1.2043 0.1364 0.0504 -0.0635 72 SER A N 336 C CA . SER A 45 ? 1.0179 1.2647 1.1885 0.1461 0.0338 -0.0739 72 SER A CA 337 C C . SER A 45 ? 0.9831 1.2207 1.1654 0.1365 0.0134 -0.0818 72 SER A C 338 O O . SER A 45 ? 1.0053 1.2499 1.1935 0.1422 0.0032 -0.0872 72 SER A O 339 C CB . SER A 45 ? 1.0773 1.3409 1.2371 0.1720 0.0322 -0.0790 72 SER A CB 340 O OG . SER A 45 ? 1.1167 1.3763 1.2708 0.1840 0.0117 -0.0926 72 SER A OG 341 N N . ASN A 46 ? 0.9799 1.2019 1.1672 0.1216 0.0065 -0.0813 73 ASN A N 342 C CA . ASN A 46 ? 0.9957 1.2079 1.1990 0.1087 -0.0128 -0.0846 73 ASN A CA 343 C C . ASN A 46 ? 1.0289 1.2239 1.2327 0.1001 -0.0231 -0.0869 73 ASN A C 344 O O . ASN A 46 ? 1.1107 1.3009 1.3072 0.0939 -0.0097 -0.0806 73 ASN A O 345 C CB . ASN A 46 ? 0.9749 1.1924 1.1928 0.0912 -0.0039 -0.0726 73 ASN A CB 346 C CG . ASN A 46 ? 1.0055 1.2190 1.2458 0.0785 -0.0240 -0.0719 73 ASN A CG 347 O OD1 . ASN A 46 ? 1.0443 1.2438 1.2911 0.0739 -0.0426 -0.0770 73 ASN A OD1 348 N ND2 . ASN A 46 ? 1.0045 1.2308 1.2586 0.0724 -0.0209 -0.0641 73 ASN A ND2 349 N N . GLN A 47 ? 1.0298 1.2145 1.2429 0.1001 -0.0482 -0.0962 74 GLN A N 350 C CA . GLN A 47 ? 1.0450 1.2121 1.2597 0.0929 -0.0611 -0.0994 74 GLN A CA 351 C C . GLN A 47 ? 1.0037 1.1652 1.2279 0.0696 -0.0506 -0.0852 74 GLN A C 352 O O . GLN A 47 ? 0.9307 1.0807 1.1494 0.0646 -0.0504 -0.0848 74 GLN A O 353 C CB . GLN A 47 ? 1.0709 1.2261 1.2996 0.0943 -0.0930 -0.1106 74 GLN A CB 354 C CG . GLN A 47 ? 1.1418 1.2770 1.3744 0.0863 -0.1087 -0.1137 74 GLN A CG 355 C CD . GLN A 47 ? 1.2237 1.3543 1.4329 0.1063 -0.1108 -0.1260 74 GLN A CD 356 O OE1 . GLN A 47 ? 1.2627 1.4024 1.4568 0.1300 -0.1136 -0.1370 74 GLN A OE1 357 N NE2 . GLN A 47 ? 1.2242 1.3429 1.4300 0.0980 -0.1094 -0.1232 74 GLN A NE2 358 N N . ARG A 48 ? 0.9533 1.1245 1.1904 0.0570 -0.0413 -0.0734 75 ARG A N 359 C CA . ARG A 48 ? 0.8132 0.9822 1.0578 0.0380 -0.0320 -0.0598 75 ARG A CA 360 C C . ARG A 48 ? 0.8009 0.9758 1.0301 0.0380 -0.0060 -0.0529 75 ARG A C 361 O O . ARG A 48 ? 0.7517 0.9264 0.9833 0.0255 0.0033 -0.0427 75 ARG A O 362 C CB . ARG A 48 ? 0.7170 0.8958 0.9861 0.0242 -0.0374 -0.0482 75 ARG A CB 363 C CG . ARG A 48 ? 0.7570 0.9271 1.0489 0.0191 -0.0665 -0.0515 75 ARG A CG 364 C CD . ARG A 48 ? 0.8491 1.0330 1.1697 0.0047 -0.0708 -0.0359 75 ARG A CD 365 N NE . ARG A 48 ? 0.9328 1.1348 1.2528 0.0122 -0.0604 -0.0347 75 ARG A NE 366 C CZ . ARG A 48 ? 0.9820 1.2021 1.3013 0.0076 -0.0388 -0.0212 75 ARG A CZ 367 N NH1 . ARG A 48 ? 0.9843 1.2077 1.3024 -0.0032 -0.0255 -0.0081 75 ARG A NH1 368 N NH2 . ARG A 48 ? 1.0121 1.2475 1.3308 0.0155 -0.0311 -0.0212 75 ARG A NH2 369 N N . PHE A 49 ? 0.8473 1.0275 1.0612 0.0530 0.0049 -0.0580 76 PHE A N 370 C CA . PHE A 49 ? 0.8078 0.9909 1.0104 0.0527 0.0266 -0.0515 76 PHE A CA 371 C C . PHE A 49 ? 0.8494 1.0241 1.0390 0.0609 0.0277 -0.0566 76 PHE A C 372 O O . PHE A 49 ? 0.9615 1.1396 1.1455 0.0758 0.0214 -0.0642 76 PHE A O 373 C CB . PHE A 49 ? 0.7321 0.9298 0.9320 0.0617 0.0393 -0.0492 76 PHE A CB 374 C CG . PHE A 49 ? 0.7537 0.9628 0.9668 0.0548 0.0391 -0.0431 76 PHE A CG 375 C CD1 . PHE A 49 ? 0.7976 1.0097 1.0262 0.0523 0.0214 -0.0455 76 PHE A CD1 376 C CD2 . PHE A 49 ? 0.7291 0.9465 0.9401 0.0521 0.0554 -0.0349 76 PHE A CD2 377 C CE1 . PHE A 49 ? 0.7511 0.9765 0.9952 0.0457 0.0211 -0.0375 76 PHE A CE1 378 C CE2 . PHE A 49 ? 0.6870 0.9187 0.9103 0.0474 0.0561 -0.0279 76 PHE A CE2 379 C CZ . PHE A 49 ? 0.6904 0.9271 0.9312 0.0435 0.0396 -0.0281 76 PHE A CZ 380 N N . GLU A 50 ? 0.8722 1.0377 1.0570 0.0527 0.0351 -0.0521 77 GLU A N 381 C CA . GLU A 50 ? 0.9283 1.0879 1.1030 0.0596 0.0376 -0.0544 77 GLU A CA 382 C C . GLU A 50 ? 0.8995 1.0579 1.0693 0.0570 0.0543 -0.0470 77 GLU A C 383 O O . GLU A 50 ? 0.9144 1.0691 1.0856 0.0465 0.0603 -0.0423 77 GLU A O 384 C CB . GLU A 50 ? 1.0893 1.2353 1.2640 0.0538 0.0248 -0.0584 77 GLU A CB 385 C CG . GLU A 50 ? 1.2924 1.4295 1.4757 0.0366 0.0185 -0.0546 77 GLU A CG 386 C CD . GLU A 50 ? 1.3444 1.4685 1.5285 0.0345 0.0025 -0.0603 77 GLU A CD 387 O OE1 . GLU A 50 ? 1.3299 1.4511 1.5040 0.0446 0.0021 -0.0652 77 GLU A OE1 388 O OE2 . GLU A 50 ? 1.3128 1.4309 1.5086 0.0237 -0.0100 -0.0588 77 GLU A OE2 389 N N . VAL A 51 ? 0.7530 0.9156 0.9180 0.0679 0.0608 -0.0454 78 VAL A N 390 C CA . VAL A 51 ? 0.6928 0.8516 0.8569 0.0651 0.0731 -0.0381 78 VAL A CA 391 C C . VAL A 51 ? 0.7598 0.9096 0.9219 0.0631 0.0712 -0.0367 78 VAL A C 392 O O . VAL A 51 ? 0.7945 0.9504 0.9549 0.0731 0.0673 -0.0375 78 VAL A O 393 C CB . VAL A 51 ? 0.6214 0.7929 0.7870 0.0772 0.0830 -0.0328 78 VAL A CB 394 C CG1 . VAL A 51 ? 0.7001 0.8650 0.8686 0.0742 0.0920 -0.0246 78 VAL A CG1 395 C CG2 . VAL A 51 ? 0.5556 0.7354 0.7229 0.0786 0.0860 -0.0338 78 VAL A CG2 396 N N . ILE A 52 ? 0.8079 0.9446 0.9695 0.0513 0.0736 -0.0345 79 ILE A N 397 C CA . ILE A 52 ? 0.8199 0.9460 0.9805 0.0467 0.0712 -0.0331 79 ILE A CA 398 C C . ILE A 52 ? 0.7958 0.9170 0.9602 0.0456 0.0794 -0.0261 79 ILE A C 399 O O . ILE A 52 ? 0.6702 0.7841 0.8334 0.0402 0.0830 -0.0262 79 ILE A O 400 C CB . ILE A 52 ? 0.5579 0.6712 0.7154 0.0338 0.0645 -0.0369 79 ILE A CB 401 C CG1 . ILE A 52 ? 0.6024 0.7191 0.7613 0.0326 0.0544 -0.0420 79 ILE A CG1 402 C CG2 . ILE A 52 ? 0.6176 0.7204 0.7736 0.0299 0.0609 -0.0363 79 ILE A CG2 403 C CD1 . ILE A 52 ? 0.6256 0.7469 0.7877 0.0267 0.0562 -0.0405 79 ILE A CD1 404 N N . GLU A 53 ? 0.9485 1.0747 1.1185 0.0520 0.0810 -0.0196 80 GLU A N 405 C CA . GLU A 53 ? 1.0114 1.1329 1.1907 0.0506 0.0859 -0.0108 80 GLU A CA 406 C C . GLU A 53 ? 1.0317 1.1351 1.2111 0.0398 0.0813 -0.0117 80 GLU A C 407 O O . GLU A 53 ? 1.0525 1.1516 1.2268 0.0358 0.0755 -0.0157 80 GLU A O 408 C CB . GLU A 53 ? 1.0539 1.1926 1.2432 0.0620 0.0897 0.0005 80 GLU A CB 409 C CG . GLU A 53 ? 1.1144 1.2729 1.3005 0.0755 0.0929 0.0000 80 GLU A CG 410 C CD . GLU A 53 ? 1.2434 1.4200 1.4418 0.0868 0.1007 0.0146 80 GLU A CD 411 O OE1 . GLU A 53 ? 1.3340 1.5254 1.5376 0.0955 0.1015 0.0238 80 GLU A OE1 412 O OE2 . GLU A 53 ? 1.3277 1.5053 1.5310 0.0877 0.1061 0.0181 80 GLU A OE2 413 N N . PHE A 54 ? 0.9967 1.0886 1.1819 0.0359 0.0825 -0.0087 81 PHE A N 414 C CA . PHE A 54 ? 1.0689 1.1443 1.2570 0.0279 0.0768 -0.0085 81 PHE A CA 415 C C . PHE A 54 ? 1.1700 1.2529 1.3725 0.0302 0.0758 0.0029 81 PHE A C 416 O O . PHE A 54 ? 1.1442 1.2421 1.3591 0.0379 0.0807 0.0139 81 PHE A O 417 C CB . PHE A 54 ? 1.1023 1.1621 1.2928 0.0255 0.0754 -0.0100 81 PHE A CB 418 C CG . PHE A 54 ? 1.1008 1.1555 1.2755 0.0248 0.0766 -0.0203 81 PHE A CG 419 C CD1 . PHE A 54 ? 1.0941 1.1590 1.2664 0.0309 0.0828 -0.0209 81 PHE A CD1 420 C CD2 . PHE A 54 ? 1.1273 1.1700 1.2899 0.0191 0.0719 -0.0282 81 PHE A CD2 421 C CE1 . PHE A 54 ? 1.1005 1.1646 1.2597 0.0312 0.0846 -0.0282 81 PHE A CE1 422 C CE2 . PHE A 54 ? 1.1185 1.1618 1.2674 0.0203 0.0741 -0.0348 81 PHE A CE2 423 C CZ . PHE A 54 ? 1.1287 1.1833 1.2764 0.0263 0.0806 -0.0344 81 PHE A CZ 424 N N . ASP A 55 ? 1.3266 1.4008 1.5284 0.0240 0.0699 0.0017 82 ASP A N 425 C CA . ASP A 55 ? 1.3978 1.4807 1.6139 0.0259 0.0687 0.0136 82 ASP A CA 426 C C . ASP A 55 ? 1.3757 1.4585 1.6147 0.0257 0.0690 0.0277 82 ASP A C 427 O O . ASP A 55 ? 1.3441 1.4445 1.5999 0.0311 0.0716 0.0433 82 ASP A O 428 C CB . ASP A 55 ? 1.5339 1.6043 1.7453 0.0179 0.0613 0.0089 82 ASP A CB 429 C CG . ASP A 55 ? 1.6472 1.7173 1.8398 0.0174 0.0592 -0.0029 82 ASP A CG 430 O OD1 . ASP A 55 ? 1.6819 1.7489 1.8633 0.0165 0.0605 -0.0114 82 ASP A OD1 431 O OD2 . ASP A 55 ? 1.6712 1.7445 1.8620 0.0181 0.0556 -0.0026 82 ASP A OD2 432 N N . ASP A 56 ? 1.4021 1.4662 1.6426 0.0205 0.0655 0.0230 83 ASP A N 433 C CA . ASP A 56 ? 1.3717 1.4305 1.6361 0.0193 0.0622 0.0352 83 ASP A CA 434 C C . ASP A 56 ? 1.3564 1.4338 1.6315 0.0283 0.0706 0.0464 83 ASP A C 435 O O . ASP A 56 ? 1.4046 1.4872 1.7053 0.0291 0.0697 0.0633 83 ASP A O 436 C CB . ASP A 56 ? 1.3893 1.4196 1.6495 0.0134 0.0530 0.0237 83 ASP A CB 437 C CG . ASP A 56 ? 1.4339 1.4601 1.6713 0.0171 0.0573 0.0090 83 ASP A CG 438 O OD1 . ASP A 56 ? 1.4331 1.4411 1.6558 0.0143 0.0514 -0.0042 83 ASP A OD1 439 O OD2 . ASP A 56 ? 1.4765 1.5192 1.7110 0.0238 0.0663 0.0115 83 ASP A OD2 440 N N . GLY A 57 ? 1.3296 1.4173 1.5868 0.0350 0.0780 0.0380 84 GLY A N 441 C CA . GLY A 57 ? 1.2915 1.3986 1.5557 0.0450 0.0864 0.0474 84 GLY A CA 442 C C . GLY A 57 ? 1.2431 1.3374 1.5073 0.0448 0.0862 0.0428 84 GLY A C 443 O O . GLY A 57 ? 1.2623 1.3705 1.5309 0.0528 0.0930 0.0490 84 GLY A O 444 N N . SER A 58 ? 1.1748 1.2434 1.4328 0.0374 0.0781 0.0313 85 SER A N 445 C CA . SER A 58 ? 1.1689 1.2234 1.4233 0.0391 0.0763 0.0243 85 SER A CA 446 C C . SER A 58 ? 0.9940 1.0598 1.2297 0.0457 0.0851 0.0156 85 SER A C 447 O O . SER A 58 ? 1.0185 1.0907 1.2602 0.0520 0.0895 0.0203 85 SER A O 448 C CB . SER A 58 ? 1.3090 1.3360 1.5533 0.0332 0.0654 0.0104 85 SER A CB 449 O OG . SER A 58 ? 1.3691 1.3969 1.5902 0.0306 0.0673 -0.0019 85 SER A OG 450 N N . GLY A 59 ? 0.9113 0.9778 1.1261 0.0433 0.0862 0.0033 86 GLY A N 451 C CA . GLY A 59 ? 0.8073 0.8880 1.0078 0.0479 0.0934 -0.0028 86 GLY A CA 452 C C . GLY A 59 ? 0.8405 0.9382 1.0331 0.0490 0.0963 -0.0047 86 GLY A C 453 O O . GLY A 59 ? 0.9153 1.0217 1.1131 0.0501 0.0954 0.0008 86 GLY A O 454 N N . SER A 60 ? 0.7570 0.8599 0.9375 0.0501 0.0989 -0.0124 87 SER A N 455 C CA . SER A 60 ? 0.6717 0.7874 0.8451 0.0508 0.0987 -0.0166 87 SER A CA 456 C C . SER A 60 ? 0.5854 0.6990 0.7479 0.0462 0.0984 -0.0240 87 SER A C 457 O O . SER A 60 ? 0.5926 0.7034 0.7515 0.0479 0.1019 -0.0256 87 SER A O 458 C CB . SER A 60 ? 0.9400 1.0756 1.1180 0.0616 0.1032 -0.0124 87 SER A CB 459 O OG . SER A 60 ? 0.9892 1.1313 1.1661 0.0664 0.1085 -0.0130 87 SER A OG 460 N N . VAL A 61 ? 0.6368 0.7532 0.7954 0.0411 0.0937 -0.0275 88 VAL A N 461 C CA . VAL A 61 ? 0.6416 0.7623 0.7950 0.0367 0.0932 -0.0303 88 VAL A CA 462 C C . VAL A 61 ? 0.5837 0.7184 0.7417 0.0397 0.0904 -0.0309 88 VAL A C 463 O O . VAL A 61 ? 0.5763 0.7118 0.7367 0.0408 0.0841 -0.0325 88 VAL A O 464 C CB . VAL A 61 ? 0.8371 0.9491 0.9858 0.0271 0.0874 -0.0320 88 VAL A CB 465 C CG1 . VAL A 61 ? 0.7982 0.9204 0.9469 0.0226 0.0862 -0.0307 88 VAL A CG1 466 C CG2 . VAL A 61 ? 0.8499 0.9473 0.9920 0.0255 0.0884 -0.0333 88 VAL A CG2 467 N N . LEU A 62 ? 0.4701 0.6157 0.6290 0.0419 0.0941 -0.0302 89 LEU A N 468 C CA . LEU A 62 ? 0.5730 0.7312 0.7378 0.0430 0.0892 -0.0311 89 LEU A CA 469 C C . LEU A 62 ? 0.6548 0.8147 0.8229 0.0328 0.0835 -0.0292 89 LEU A C 470 O O . LEU A 62 ? 0.6587 0.8232 0.8250 0.0297 0.0889 -0.0251 89 LEU A O 471 C CB . LEU A 62 ? 0.5165 0.6875 0.6831 0.0510 0.0961 -0.0296 89 LEU A CB 472 C CG . LEU A 62 ? 0.6036 0.7888 0.7778 0.0525 0.0908 -0.0303 89 LEU A CG 473 C CD1 . LEU A 62 ? 0.6279 0.8143 0.8045 0.0588 0.0812 -0.0354 89 LEU A CD1 474 C CD2 . LEU A 62 ? 0.6241 0.8219 0.7990 0.0598 0.0993 -0.0280 89 LEU A CD2 475 N N . ARG A 63 ? 0.6187 0.7763 0.7926 0.0288 0.0719 -0.0315 90 ARG A N 476 C CA . ARG A 63 ? 0.5805 0.7396 0.7623 0.0180 0.0639 -0.0276 90 ARG A CA 477 C C . ARG A 63 ? 0.5770 0.7455 0.7724 0.0178 0.0532 -0.0278 90 ARG A C 478 O O . ARG A 63 ? 0.6796 0.8462 0.8763 0.0250 0.0445 -0.0351 90 ARG A O 479 C CB . ARG A 63 ? 0.6193 0.7641 0.7991 0.0118 0.0560 -0.0297 90 ARG A CB 480 C CG . ARG A 63 ? 0.7512 0.8962 0.9425 0.0006 0.0447 -0.0249 90 ARG A CG 481 C CD . ARG A 63 ? 0.8634 0.9931 1.0523 -0.0034 0.0352 -0.0289 90 ARG A CD 482 N NE . ARG A 63 ? 0.8405 0.9690 1.0417 -0.0151 0.0245 -0.0224 90 ARG A NE 483 C CZ . ARG A 63 ? 0.6997 0.8296 0.9000 -0.0234 0.0294 -0.0136 90 ARG A CZ 484 N NH1 . ARG A 63 ? 0.7360 0.8664 0.9219 -0.0202 0.0434 -0.0129 90 ARG A NH1 485 N NH2 . ARG A 63 ? 0.5468 0.6776 0.7612 -0.0340 0.0191 -0.0052 90 ARG A NH2 486 N N . ILE A 64 ? 0.5586 0.7388 0.7647 0.0107 0.0532 -0.0191 91 ILE A N 487 C CA . ILE A 64 ? 0.5968 0.7866 0.8206 0.0084 0.0413 -0.0171 91 ILE A CA 488 C C . ILE A 64 ? 0.6457 0.8352 0.8855 -0.0055 0.0302 -0.0080 91 ILE A C 489 O O . ILE A 64 ? 0.6292 0.8271 0.8707 -0.0124 0.0381 0.0036 91 ILE A O 490 C CB . ILE A 64 ? 0.5405 0.7491 0.7685 0.0121 0.0509 -0.0111 91 ILE A CB 491 C CG1 . ILE A 64 ? 0.4788 0.6865 0.6896 0.0245 0.0652 -0.0171 91 ILE A CG1 492 C CG2 . ILE A 64 ? 0.5319 0.7494 0.7787 0.0118 0.0371 -0.0111 91 ILE A CG2 493 C CD1 . ILE A 64 ? 0.4765 0.7002 0.6862 0.0286 0.0779 -0.0110 91 ILE A CD1 494 N N . GLN A 65 ? 0.6671 0.8476 0.9188 -0.0079 0.0109 -0.0132 92 GLN A N 495 C CA . GLN A 65 ? 0.5981 0.7753 0.8690 -0.0213 -0.0040 -0.0048 92 GLN A CA 496 C C . GLN A 65 ? 0.6604 0.8285 0.9457 -0.0193 -0.0280 -0.0139 92 GLN A C 497 O O . GLN A 65 ? 0.7607 0.9175 1.0323 -0.0072 -0.0332 -0.0294 92 GLN A O 498 C CB . GLN A 65 ? 0.5940 0.7574 0.8538 -0.0260 -0.0018 -0.0050 92 GLN A CB 499 C CG . GLN A 65 ? 0.6231 0.7793 0.9015 -0.0387 -0.0189 0.0021 92 GLN A CG 500 C CD . GLN A 65 ? 0.7585 0.8981 1.0225 -0.0402 -0.0182 -0.0025 92 GLN A CD 501 O OE1 . GLN A 65 ? 0.7345 0.8658 0.9769 -0.0308 -0.0092 -0.0134 92 GLN A OE1 502 N NE2 . GLN A 65 ? 0.9245 1.0602 1.2026 -0.0522 -0.0282 0.0073 92 GLN A NE2 503 N N . PRO A 66 ? 0.6951 0.8688 1.0089 -0.0301 -0.0439 -0.0038 93 PRO A N 504 C CA . PRO A 66 ? 0.7283 0.9228 1.0620 -0.0423 -0.0373 0.0177 93 PRO A CA 505 C C . PRO A 66 ? 0.7793 0.9950 1.1128 -0.0361 -0.0238 0.0218 93 PRO A C 506 O O . PRO A 66 ? 0.9093 1.1235 1.2413 -0.0265 -0.0300 0.0101 93 PRO A O 507 C CB . PRO A 66 ? 0.7443 0.9349 1.1125 -0.0542 -0.0642 0.0252 93 PRO A CB 508 C CG . PRO A 66 ? 0.7003 0.8739 1.0659 -0.0433 -0.0837 0.0043 93 PRO A CG 509 C CD . PRO A 66 ? 0.7125 0.8728 1.0428 -0.0293 -0.0723 -0.0132 93 PRO A CD 510 N N . LEU A 67 ? 0.7603 0.9964 1.0935 -0.0397 -0.0057 0.0377 94 LEU A N 511 C CA . LEU A 67 ? 0.7722 1.0302 1.1057 -0.0336 0.0073 0.0431 94 LEU A CA 512 C C . LEU A 67 ? 0.7530 1.0235 1.1195 -0.0397 -0.0095 0.0516 94 LEU A C 513 O O . LEU A 67 ? 0.8526 1.1260 1.2481 -0.0531 -0.0253 0.0650 94 LEU A O 514 C CB . LEU A 67 ? 0.7169 0.9955 1.0435 -0.0344 0.0279 0.0590 94 LEU A CB 515 C CG . LEU A 67 ? 0.6452 0.9121 0.9388 -0.0264 0.0443 0.0497 94 LEU A CG 516 C CD1 . LEU A 67 ? 0.6581 0.9453 0.9450 -0.0254 0.0608 0.0647 94 LEU A CD1 517 C CD2 . LEU A 67 ? 0.6239 0.8826 0.8964 -0.0125 0.0528 0.0331 94 LEU A CD2 518 N N . ARG A 68 ? 0.5696 0.8480 0.9334 -0.0302 -0.0065 0.0448 95 ARG A N 519 C CA . ARG A 68 ? 0.5934 0.8858 0.9881 -0.0349 -0.0212 0.0528 95 ARG A CA 520 C C . ARG A 68 ? 0.7255 1.0455 1.1186 -0.0293 -0.0023 0.0628 95 ARG A C 521 O O . ARG A 68 ? 0.7873 1.1073 1.1517 -0.0167 0.0166 0.0535 95 ARG A O 522 C CB . ARG A 68 ? 0.6860 0.9602 1.0812 -0.0267 -0.0417 0.0322 95 ARG A CB 523 C CG . ARG A 68 ? 0.8310 1.0901 1.2545 -0.0366 -0.0733 0.0315 95 ARG A CG 524 C CD . ARG A 68 ? 0.9321 1.1656 1.3403 -0.0366 -0.0797 0.0205 95 ARG A CD 525 N NE . ARG A 68 ? 1.0304 1.2626 1.4634 -0.0541 -0.0899 0.0376 95 ARG A NE 526 C CZ . ARG A 68 ? 1.0936 1.3087 1.5508 -0.0618 -0.1195 0.0356 95 ARG A CZ 527 N NH1 . ARG A 68 ? 1.1296 1.3270 1.5871 -0.0518 -0.1426 0.0152 95 ARG A NH1 528 N NH2 . ARG A 68 ? 1.0506 1.2666 1.5315 -0.0782 -0.1269 0.0541 95 ARG A NH2 529 N N . THR A 69 ? 0.8458 1.1901 1.2715 -0.0386 -0.0079 0.0831 96 THR A N 530 C CA . THR A 69 ? 0.8707 1.2446 1.2981 -0.0331 0.0087 0.0946 96 THR A CA 531 C C . THR A 69 ? 0.8550 1.2410 1.3151 -0.0369 -0.0087 0.0998 96 THR A C 532 O O . THR A 69 ? 0.8458 1.2302 1.3410 -0.0503 -0.0321 0.1093 96 THR A O 533 C CB . THR A 69 ? 0.9434 1.3452 1.3772 -0.0385 0.0249 0.1199 96 THR A CB 534 O OG1 . THR A 69 ? 0.9815 1.4129 1.4135 -0.0300 0.0416 0.1295 96 THR A OG1 535 C CG2 . THR A 69 ? 0.9416 1.3551 1.4176 -0.0566 0.0075 0.1435 96 THR A CG2 536 N N . PRO A 70 ? 0.7997 1.1964 1.2498 -0.0251 0.0006 0.0932 97 PRO A N 537 C CA . PRO A 70 ? 0.7829 1.1823 1.1965 -0.0092 0.0258 0.0833 97 PRO A CA 538 C C . PRO A 70 ? 0.8102 1.1802 1.1924 0.0028 0.0262 0.0570 97 PRO A C 539 O O . PRO A 70 ? 0.8078 1.1775 1.1625 0.0153 0.0450 0.0493 97 PRO A O 540 C CB . PRO A 70 ? 0.7465 1.1711 1.1730 -0.0039 0.0292 0.0899 97 PRO A CB 541 C CG . PRO A 70 ? 0.7611 1.1962 1.2324 -0.0179 0.0051 0.1037 97 PRO A CG 542 C CD . PRO A 70 ? 0.7823 1.1907 1.2634 -0.0280 -0.0168 0.0972 97 PRO A CD 543 N N . ARG A 71 ? 0.8127 1.1600 1.2006 0.0000 0.0049 0.0446 98 ARG A N 544 C CA . ARG A 71 ? 0.8231 1.1470 1.1855 0.0129 0.0022 0.0214 98 ARG A CA 545 C C . ARG A 71 ? 0.8468 1.1635 1.1751 0.0221 0.0254 0.0152 98 ARG A C 546 O O . ARG A 71 ? 0.9059 1.2203 1.2150 0.0360 0.0344 0.0042 98 ARG A O 547 C CB . ARG A 71 ? 0.8572 1.1577 1.2268 0.0076 -0.0211 0.0123 98 ARG A CB 548 C CG . ARG A 71 ? 0.8945 1.1933 1.2944 0.0033 -0.0503 0.0105 98 ARG A CG 549 C CD . ARG A 71 ? 0.9503 1.2237 1.3553 -0.0009 -0.0736 0.0010 98 ARG A CD 550 N NE . ARG A 71 ? 1.0609 1.3277 1.4951 -0.0038 -0.1060 -0.0034 98 ARG A NE 551 C CZ . ARG A 71 ? 1.1270 1.4033 1.6013 -0.0207 -0.1217 0.0147 98 ARG A CZ 552 N NH1 . ARG A 71 ? 1.1096 1.4063 1.5978 -0.0348 -0.1056 0.0398 98 ARG A NH1 553 N NH2 . ARG A 71 ? 1.1617 1.4282 1.6633 -0.0225 -0.1546 0.0086 98 ARG A NH2 554 N N . ASP A 72 ? 0.7587 1.0722 1.0815 0.0145 0.0337 0.0230 99 ASP A N 555 C CA . ASP A 72 ? 0.6838 0.9854 0.9773 0.0214 0.0505 0.0161 99 ASP A CA 556 C C . ASP A 72 ? 0.8109 1.1284 1.0923 0.0276 0.0720 0.0234 99 ASP A C 557 O O . ASP A 72 ? 0.8557 1.1630 1.1141 0.0349 0.0848 0.0171 99 ASP A O 558 C CB . ASP A 72 ? 0.5745 0.8628 0.8661 0.0117 0.0472 0.0189 99 ASP A CB 559 C CG . ASP A 72 ? 0.6575 0.9274 0.9585 0.0071 0.0254 0.0103 99 ASP A CG 560 O OD1 . ASP A 72 ? 0.7662 1.0293 1.0653 0.0161 0.0154 -0.0027 99 ASP A OD1 561 O OD2 . ASP A 72 ? 0.6364 0.8993 0.9460 -0.0040 0.0177 0.0163 99 ASP A OD2 562 N N . GLU A 73 ? 0.8175 1.1599 1.1151 0.0254 0.0749 0.0370 100 GLU A N 563 C CA . GLU A 73 ? 0.7695 1.1281 1.0539 0.0337 0.0945 0.0433 100 GLU A CA 564 C C . GLU A 73 ? 0.8753 1.2276 1.1422 0.0480 0.1025 0.0302 100 GLU A C 565 O O . GLU A 73 ? 0.9406 1.2991 1.2172 0.0514 0.0962 0.0271 100 GLU A O 566 C CB . GLU A 73 ? 0.6927 1.0833 1.0001 0.0296 0.0956 0.0621 100 GLU A CB 567 C CG . GLU A 73 ? 0.7821 1.1927 1.0840 0.0312 0.1102 0.0771 100 GLU A CG 568 C CD . GLU A 73 ? 0.8719 1.3037 1.2038 0.0173 0.1023 0.0991 100 GLU A CD 569 O OE1 . GLU A 73 ? 0.8368 1.2839 1.1985 0.0100 0.0910 0.1090 100 GLU A OE1 570 O OE2 . GLU A 73 ? 0.9590 1.3924 1.2862 0.0136 0.1063 0.1072 100 GLU A OE2 571 N N . ALA A 74 ? 0.9622 1.3032 1.2049 0.0566 0.1155 0.0237 101 ALA A N 572 C CA . ALA A 74 ? 0.9762 1.3092 1.2047 0.0694 0.1221 0.0129 101 ALA A CA 573 C C . ALA A 74 ? 0.9805 1.2999 1.1866 0.0774 0.1342 0.0078 101 ALA A C 574 O O . ALA A 74 ? 0.9886 1.3007 1.1870 0.0738 0.1363 0.0094 101 ALA A O 575 C CB . ALA A 74 ? 0.9539 1.2719 1.1841 0.0701 0.1106 0.0022 101 ALA A CB 576 N N . ILE A 75 ? 0.9110 1.2266 1.1081 0.0888 0.1406 0.0018 102 ILE A N 577 C CA . ILE A 75 ? 0.8227 1.1193 1.0031 0.0957 0.1472 -0.0045 102 ILE A CA 578 C C . ILE A 75 ? 0.8916 1.1701 1.0712 0.0945 0.1413 -0.0110 102 ILE A C 579 O O . ILE A 75 ? 0.9439 1.2269 1.1297 0.0980 0.1373 -0.0132 102 ILE A O 580 C CB . ILE A 75 ? 0.7912 1.0926 0.9647 0.1089 0.1565 -0.0056 102 ILE A CB 581 C CG1 . ILE A 75 ? 0.8780 1.2033 1.0539 0.1125 0.1623 0.0016 102 ILE A CG1 582 C CG2 . ILE A 75 ? 0.7937 1.0743 0.9532 0.1151 0.1607 -0.0108 102 ILE A CG2 583 C CD1 . ILE A 75 ? 0.8868 1.2144 1.0521 0.1138 0.1671 0.0048 102 ILE A CD1 584 N N . TYR A 76 ? 0.9384 1.1986 1.1104 0.0911 0.1405 -0.0137 103 TYR A N 585 C CA . TYR A 76 ? 0.8772 1.1228 1.0487 0.0915 0.1364 -0.0178 103 TYR A CA 586 C C . TYR A 76 ? 0.9855 1.2163 1.1494 0.0977 0.1423 -0.0189 103 TYR A C 587 O O . TYR A 76 ? 0.9421 1.1681 1.0985 0.0999 0.1465 -0.0193 103 TYR A O 588 C CB . TYR A 76 ? 0.6145 0.8507 0.7876 0.0808 0.1279 -0.0190 103 TYR A CB 589 C CG . TYR A 76 ? 0.4965 0.7441 0.6809 0.0736 0.1187 -0.0174 103 TYR A CG 590 C CD1 . TYR A 76 ? 0.6152 0.8743 0.8051 0.0668 0.1188 -0.0108 103 TYR A CD1 591 C CD2 . TYR A 76 ? 0.4886 0.7362 0.6793 0.0745 0.1086 -0.0216 103 TYR A CD2 592 C CE1 . TYR A 76 ? 0.7143 0.9834 0.9197 0.0587 0.1083 -0.0069 103 TYR A CE1 593 C CE2 . TYR A 76 ? 0.6182 0.8728 0.8215 0.0680 0.0965 -0.0210 103 TYR A CE2 594 C CZ . TYR A 76 ? 0.7474 1.0121 0.9601 0.0588 0.0960 -0.0129 103 TYR A CZ 595 O OH . TYR A 76 ? 0.8116 1.0829 1.0420 0.0508 0.0820 -0.0101 103 TYR A OH 596 N N . GLU A 77 ? 1.0361 1.2602 1.2027 0.1017 0.1417 -0.0187 104 GLU A N 597 C CA . GLU A 77 ? 1.0842 1.2935 1.2490 0.1059 0.1451 -0.0173 104 GLU A CA 598 C C . GLU A 77 ? 1.0054 1.2020 1.1737 0.1016 0.1405 -0.0159 104 GLU A C 599 O O . GLU A 77 ? 1.0468 1.2506 1.2194 0.1024 0.1379 -0.0145 104 GLU A O 600 C CB . GLU A 77 ? 1.2557 1.4720 1.4246 0.1169 0.1509 -0.0136 104 GLU A CB 601 C CG . GLU A 77 ? 1.3939 1.6267 1.5688 0.1228 0.1512 -0.0108 104 GLU A CG 602 C CD . GLU A 77 ? 1.4938 1.7321 1.6734 0.1339 0.1574 -0.0050 104 GLU A CD 603 O OE1 . GLU A 77 ? 1.5078 1.7624 1.6905 0.1417 0.1587 -0.0026 104 GLU A OE1 604 O OE2 . GLU A 77 ? 1.5166 1.7424 1.6967 0.1356 0.1598 -0.0030 104 GLU A OE2 605 N N . CYS A 78 ? 0.8710 1.0491 1.0370 0.0983 0.1388 -0.0167 105 CYS A N 606 C CA . CYS A 78 ? 0.8377 1.0037 1.0104 0.0954 0.1351 -0.0129 105 CYS A CA 607 C C . CYS A 78 ? 0.8853 1.0472 1.0688 0.1022 0.1374 -0.0052 105 CYS A C 608 O O . CYS A 78 ? 0.9747 1.1260 1.1577 0.1055 0.1374 -0.0065 105 CYS A O 609 C CB . CYS A 78 ? 0.8450 0.9924 1.0119 0.0875 0.1296 -0.0176 105 CYS A CB 610 S SG . CYS A 78 ? 0.9374 1.0676 1.1150 0.0833 0.1239 -0.0123 105 CYS A SG 611 N N . VAL A 79 ? 0.8218 0.9929 1.0159 0.1051 0.1384 0.0036 106 VAL A N 612 C CA . VAL A 79 ? 0.7825 0.9545 0.9913 0.1114 0.1409 0.0153 106 VAL A CA 613 C C . VAL A 79 ? 0.7826 0.9470 1.0049 0.1070 0.1367 0.0249 106 VAL A C 614 O O . VAL A 79 ? 0.7854 0.9611 1.0085 0.1070 0.1368 0.0282 106 VAL A O 615 C CB . VAL A 79 ? 0.7950 0.9917 1.0073 0.1224 0.1476 0.0222 106 VAL A CB 616 C CG1 . VAL A 79 ? 0.8206 1.0213 1.0512 0.1287 0.1506 0.0383 106 VAL A CG1 617 C CG2 . VAL A 79 ? 0.7818 0.9867 0.9839 0.1269 0.1512 0.0143 106 VAL A CG2 618 N N . ALA A 80 ? 0.7835 0.9286 1.0169 0.1037 0.1317 0.0290 107 ALA A N 619 C CA . ALA A 80 ? 0.7999 0.9386 1.0514 0.0989 0.1267 0.0408 107 ALA A CA 620 C C . ALA A 80 ? 0.8508 0.9986 1.1262 0.1050 0.1292 0.0600 107 ALA A C 621 O O . ALA A 80 ? 0.8803 1.0199 1.1613 0.1085 0.1283 0.0612 107 ALA A O 622 C CB . ALA A 80 ? 0.8001 0.9097 1.0512 0.0903 0.1161 0.0330 107 ALA A CB 623 N N . SER A 81 ? 0.9026 1.0684 1.1928 0.1070 0.1320 0.0763 108 SER A N 624 C CA . SER A 81 ? 0.9301 1.1110 1.2456 0.1136 0.1357 0.0990 108 SER A CA 625 C C . SER A 81 ? 0.8946 1.0832 1.2369 0.1105 0.1332 0.1208 108 SER A C 626 O O . SER A 81 ? 0.7815 0.9747 1.1194 0.1073 0.1322 0.1198 108 SER A O 627 C CB . SER A 81 ? 1.0048 1.2174 1.3119 0.1276 0.1472 0.1030 108 SER A CB 628 O OG . SER A 81 ? 1.0407 1.2688 1.3306 0.1311 0.1499 0.0953 108 SER A OG 629 N N . ASN A 82 ? 1.0060 1.1950 1.3780 0.1110 0.1311 0.1414 109 ASN A N 630 C CA . ASN A 82 ? 0.9795 1.1894 1.3822 0.1121 0.1326 0.1700 109 ASN A CA 631 C C . ASN A 82 ? 1.0386 1.2675 1.4654 0.1209 0.1383 0.1937 109 ASN A C 632 O O . ASN A 82 ? 1.1124 1.3356 1.5298 0.1258 0.1405 0.1852 109 ASN A O 633 C CB . ASN A 82 ? 0.8194 1.0044 1.2449 0.0977 0.1186 0.1757 109 ASN A CB 634 C CG . ASN A 82 ? 0.7605 0.9082 1.1957 0.0900 0.1049 0.1677 109 ASN A CG 635 O OD1 . ASN A 82 ? 0.7204 0.8654 1.1570 0.0957 0.1063 0.1677 109 ASN A OD1 636 N ND2 . ASN A 82 ? 0.8571 0.9755 1.2985 0.0784 0.0903 0.1599 109 ASN A ND2 637 N N . ASN A 83 ? 0.9684 1.2194 1.4285 0.1225 0.1400 0.2248 110 ASN A N 638 C CA . ASN A 83 ? 0.9762 1.2504 1.4628 0.1315 0.1462 0.2522 110 ASN A CA 639 C C . ASN A 83 ? 0.9040 1.1463 1.4131 0.1229 0.1340 0.2545 110 ASN A C 640 O O . ASN A 83 ? 0.9298 1.1848 1.4580 0.1296 0.1378 0.2729 110 ASN A O 641 C CB . ASN A 83 ? 1.0664 1.3775 1.5856 0.1362 0.1516 0.2887 110 ASN A CB 642 C CG . ASN A 83 ? 1.1941 1.4876 1.7419 0.1203 0.1386 0.2995 110 ASN A CG 643 O OD1 . ASN A 83 ? 1.2694 1.5539 1.8003 0.1147 0.1354 0.2841 110 ASN A OD1 644 N ND2 . ASN A 83 ? 1.2643 1.5538 1.8580 0.1131 0.1302 0.3275 110 ASN A ND2 645 N N . VAL A 84 ? 0.7947 0.9953 1.2994 0.1097 0.1188 0.2344 111 VAL A N 646 C CA . VAL A 84 ? 0.7397 0.9050 1.2616 0.1033 0.1038 0.2314 111 VAL A CA 647 C C . VAL A 84 ? 0.8695 1.0168 1.3550 0.1089 0.1053 0.2012 111 VAL A C 648 O O . VAL A 84 ? 1.0121 1.1388 1.5066 0.1100 0.0972 0.1990 111 VAL A O 649 C CB . VAL A 84 ? 0.7841 0.9132 1.3227 0.0885 0.0835 0.2264 111 VAL A CB 650 C CG1 . VAL A 84 ? 0.8269 0.9288 1.4031 0.0831 0.0654 0.2388 111 VAL A CG1 651 C CG2 . VAL A 84 ? 0.8911 1.0410 1.4492 0.0829 0.0852 0.2465 111 VAL A CG2 652 N N . GLY A 85 ? 0.9153 1.0703 1.3616 0.1127 0.1147 0.1785 112 GLY A N 653 C CA . GLY A 85 ? 0.9552 1.0955 1.3701 0.1172 0.1159 0.1521 112 GLY A CA 654 C C . GLY A 85 ? 0.8837 1.0327 1.2597 0.1195 0.1245 0.1292 112 GLY A C 655 O O . GLY A 85 ? 0.7641 0.9260 1.1333 0.1170 0.1280 0.1293 112 GLY A O 656 N N . GLU A 86 ? 0.9070 1.0478 1.2589 0.1242 0.1265 0.1098 113 GLU A N 657 C CA . GLU A 86 ? 0.8728 1.0224 1.1917 0.1260 0.1335 0.0900 113 GLU A CA 658 C C . GLU A 86 ? 0.9104 1.0368 1.2079 0.1254 0.1283 0.0674 113 GLU A C 659 O O . GLU A 86 ? 0.9790 1.0934 1.2803 0.1304 0.1249 0.0660 113 GLU A O 660 C CB . GLU A 86 ? 0.8991 1.0814 1.2106 0.1373 0.1468 0.0952 113 GLU A CB 661 C CG . GLU A 86 ? 1.0256 1.2212 1.3104 0.1388 0.1522 0.0794 113 GLU A CG 662 C CD . GLU A 86 ? 1.1217 1.3493 1.4022 0.1515 0.1625 0.0855 113 GLU A CD 663 O OE1 . GLU A 86 ? 1.1603 1.4058 1.4330 0.1547 0.1651 0.0847 113 GLU A OE1 664 O OE2 . GLU A 86 ? 1.1234 1.3580 1.4076 0.1595 0.1669 0.0901 113 GLU A OE2 665 N N . ILE A 87 ? 0.8392 0.9610 1.1145 0.1207 0.1277 0.0509 114 ILE A N 666 C CA . ILE A 87 ? 0.8341 0.9405 1.0875 0.1221 0.1246 0.0314 114 ILE A CA 667 C C . ILE A 87 ? 0.9230 1.0452 1.1535 0.1208 0.1317 0.0201 114 ILE A C 668 O O . ILE A 87 ? 0.9331 1.0626 1.1624 0.1147 0.1324 0.0215 114 ILE A O 669 C CB . ILE A 87 ? 0.7633 0.8382 1.0165 0.1168 0.1105 0.0224 114 ILE A CB 670 C CG1 . ILE A 87 ? 0.7386 0.8108 0.9969 0.1063 0.1066 0.0254 114 ILE A CG1 671 C CG2 . ILE A 87 ? 0.5770 0.6311 0.8520 0.1195 0.0997 0.0297 114 ILE A CG2 672 C CD1 . ILE A 87 ? 0.7770 0.8189 1.0331 0.1015 0.0921 0.0151 114 ILE A CD1 673 N N . SER A 88 ? 0.8737 1.0012 1.0875 0.1265 0.1359 0.0098 115 SER A N 674 C CA . SER A 88 ? 0.9252 1.0675 1.1222 0.1238 0.1408 0.0015 115 SER A CA 675 C C . SER A 88 ? 0.9688 1.1028 1.1477 0.1252 0.1389 -0.0116 115 SER A C 676 O O . SER A 88 ? 1.0358 1.1583 1.2115 0.1326 0.1364 -0.0157 115 SER A O 677 C CB . SER A 88 ? 0.9863 1.1548 1.1829 0.1300 0.1496 0.0053 115 SER A CB 678 O OG . SER A 88 ? 1.0390 1.2107 1.2300 0.1382 0.1532 0.0019 115 SER A OG 679 N N . VAL A 89 ? 0.9179 1.0590 1.0855 0.1192 0.1397 -0.0172 116 VAL A N 680 C CA . VAL A 89 ? 0.9092 1.0513 1.0601 0.1218 0.1403 -0.0262 116 VAL A CA 681 C C . VAL A 89 ? 0.8869 1.0526 1.0329 0.1181 0.1458 -0.0258 116 VAL A C 682 O O . VAL A 89 ? 0.8996 1.0713 1.0510 0.1100 0.1446 -0.0230 116 VAL A O 683 C CB . VAL A 89 ? 0.9127 1.0343 1.0557 0.1181 0.1321 -0.0330 116 VAL A CB 684 C CG1 . VAL A 89 ? 0.8096 0.9294 0.9580 0.1060 0.1292 -0.0301 116 VAL A CG1 685 C CG2 . VAL A 89 ? 1.0827 1.2099 1.2070 0.1236 0.1337 -0.0407 116 VAL A CG2 686 N N . SER A 90 ? 0.8067 0.9857 0.9439 0.1244 0.1506 -0.0280 117 SER A N 687 C CA . SER A 90 ? 0.7565 0.9593 0.8941 0.1206 0.1544 -0.0252 117 SER A CA 688 C C . SER A 90 ? 0.7360 0.9410 0.8644 0.1158 0.1529 -0.0268 117 SER A C 689 O O . SER A 90 ? 0.7778 0.9694 0.8951 0.1201 0.1507 -0.0318 117 SER A O 690 C CB . SER A 90 ? 0.8389 1.0600 0.9762 0.1301 0.1611 -0.0233 117 SER A CB 691 O OG . SER A 90 ? 0.9161 1.1294 1.0428 0.1415 0.1627 -0.0276 117 SER A OG 692 N N . THR A 91 ? 0.6798 0.9016 0.8139 0.1075 0.1527 -0.0222 118 THR A N 693 C CA . THR A 91 ? 0.7507 0.9803 0.8797 0.1027 0.1521 -0.0197 118 THR A CA 694 C C . THR A 91 ? 0.8636 1.1186 1.0045 0.0966 0.1528 -0.0113 118 THR A C 695 O O . THR A 91 ? 0.8877 1.1482 1.0402 0.0939 0.1506 -0.0102 118 THR A O 696 C CB . THR A 91 ? 0.9383 1.1504 1.0661 0.0930 0.1453 -0.0221 118 THR A CB 697 O OG1 . THR A 91 ? 0.9049 1.1253 1.0263 0.0904 0.1455 -0.0189 118 THR A OG1 698 C CG2 . THR A 91 ? 0.9974 1.2096 1.1384 0.0827 0.1399 -0.0201 118 THR A CG2 699 N N . ARG A 92 ? 0.9328 1.2046 1.0723 0.0952 0.1550 -0.0044 119 ARG A N 700 C CA . ARG A 92 ? 0.9302 1.2278 1.0862 0.0887 0.1544 0.0063 119 ARG A CA 701 C C . ARG A 92 ? 0.9315 1.2314 1.0971 0.0751 0.1475 0.0131 119 ARG A C 702 O O . ARG A 92 ? 0.9822 1.2777 1.1381 0.0746 0.1483 0.0141 119 ARG A O 703 C CB . ARG A 92 ? 1.0454 1.3693 1.1984 0.0987 0.1633 0.0142 119 ARG A CB 704 C CG . ARG A 92 ? 1.1943 1.5480 1.3681 0.0906 0.1620 0.0295 119 ARG A CG 705 C CD . ARG A 92 ? 1.2875 1.6717 1.4580 0.1015 0.1722 0.0404 119 ARG A CD 706 N NE . ARG A 92 ? 1.3007 1.6875 1.4621 0.1158 0.1790 0.0343 119 ARG A NE 707 C CZ . ARG A 92 ? 1.2110 1.6072 1.3859 0.1150 0.1783 0.0357 119 ARG A CZ 708 N NH1 . ARG A 92 ? 1.1324 1.5347 1.3304 0.1013 0.1694 0.0417 119 ARG A NH1 709 N NH2 . ARG A 92 ? 1.2313 1.6293 1.3966 0.1289 0.1849 0.0304 119 ARG A NH2 710 N N . LEU A 93 ? 0.8458 1.1527 1.0310 0.0651 0.1393 0.0176 120 LEU A N 711 C CA . LEU A 93 ? 0.7160 1.0286 0.9160 0.0517 0.1309 0.0267 120 LEU A CA 712 C C . LEU A 93 ? 0.6930 1.0359 0.9142 0.0475 0.1301 0.0425 120 LEU A C 713 O O . LEU A 93 ? 0.6865 1.0385 0.9210 0.0478 0.1265 0.0430 120 LEU A O 714 C CB . LEU A 93 ? 0.6584 0.9517 0.8664 0.0435 0.1181 0.0188 120 LEU A CB 715 C CG . LEU A 93 ? 0.6043 0.8999 0.8313 0.0294 0.1052 0.0265 120 LEU A CG 716 C CD1 . LEU A 93 ? 0.5341 0.8258 0.7537 0.0245 0.1076 0.0317 120 LEU A CD1 717 C CD2 . LEU A 93 ? 0.6064 0.8833 0.8381 0.0263 0.0919 0.0157 120 LEU A CD2 718 N N . THR A 94 ? 0.7200 1.0792 0.9459 0.0432 0.1324 0.0564 121 THR A N 719 C CA . THR A 94 ? 0.7067 1.0972 0.9582 0.0362 0.1303 0.0768 121 THR A CA 720 C C . THR A 94 ? 0.6794 1.0675 0.9512 0.0198 0.1175 0.0867 121 THR A C 721 O O . THR A 94 ? 0.5849 0.9567 0.8444 0.0174 0.1169 0.0824 121 THR A O 722 C CB . THR A 94 ? 0.7700 1.1898 1.0120 0.0474 0.1454 0.0900 121 THR A CB 723 O OG1 . THR A 94 ? 0.7884 1.2029 1.0056 0.0645 0.1562 0.0772 121 THR A OG1 724 C CG2 . THR A 94 ? 0.7898 1.2481 1.0609 0.0426 0.1454 0.1134 121 THR A CG2 725 N N . VAL A 95 ? 0.7850 1.1876 1.0892 0.0084 0.1057 0.0995 122 VAL A N 726 C CA . VAL A 95 ? 0.8324 1.2316 1.1605 -0.0078 0.0906 0.1100 122 VAL A CA 727 C C . VAL A 95 ? 0.7563 1.1917 1.1191 -0.0166 0.0878 0.1384 122 VAL A C 728 O O . VAL A 95 ? 0.6742 1.1237 1.0599 -0.0192 0.0813 0.1445 122 VAL A O 729 C CB . VAL A 95 ? 0.7218 1.0938 1.0610 -0.0153 0.0704 0.0952 122 VAL A CB 730 C CG1 . VAL A 95 ? 0.7379 1.1012 1.0980 -0.0305 0.0538 0.1034 122 VAL A CG1 731 C CG2 . VAL A 95 ? 0.6130 0.9554 0.9213 -0.0050 0.0741 0.0702 122 VAL A CG2 732 N N . LEU A 96 ? 0.8067 1.2586 1.1750 -0.0210 0.0923 0.1571 123 LEU A N 733 C CA . LEU A 96 ? 0.8148 1.3054 1.2191 -0.0297 0.0906 0.1890 123 LEU A CA 734 C C . LEU A 96 ? 0.8683 1.3516 1.3112 -0.0502 0.0677 0.2011 123 LEU A C 735 O O . LEU A 96 ? 0.8654 1.3205 1.3012 -0.0564 0.0586 0.1908 123 LEU A O 736 C CB . LEU A 96 ? 0.7268 1.2464 1.1168 -0.0203 0.1093 0.2064 123 LEU A CB 737 C CG . LEU A 96 ? 0.6349 1.1552 0.9819 0.0020 0.1295 0.1911 123 LEU A CG 738 C CD1 . LEU A 96 ? 0.5811 1.1302 0.9134 0.0133 0.1450 0.2075 123 LEU A CD1 739 C CD2 . LEU A 96 ? 0.7519 1.2886 1.1013 0.0110 0.1355 0.1898 123 LEU A CD2 740 N N . ARG A 97 ? 0.9045 1.4129 1.3899 -0.0607 0.0570 0.2235 124 ARG A N 741 C CA . ARG A 97 ? 0.9864 1.4937 1.5150 -0.0807 0.0344 0.2415 124 ARG A CA 742 C C . ARG A 97 ? 1.0663 1.5976 1.6039 -0.0856 0.0425 0.2690 124 ARG A C 743 O O . ARG A 97 ? 1.0899 1.6551 1.6130 -0.0738 0.0650 0.2839 124 ARG A O 744 C CB . ARG A 97 ? 1.0391 1.5686 1.6148 -0.0908 0.0195 0.2601 124 ARG A CB 745 C CG . ARG A 97 ? 1.1312 1.6478 1.6978 -0.0826 0.0155 0.2373 124 ARG A CG 746 C CD . ARG A 97 ? 1.2513 1.7992 1.8630 -0.0902 0.0057 0.2599 124 ARG A CD 747 N NE . ARG A 97 ? 1.3604 1.9158 2.0255 -0.1110 -0.0180 0.2857 124 ARG A NE 748 C CZ . ARG A 97 ? 1.4313 1.9529 2.1182 -0.1230 -0.0487 0.2739 124 ARG A CZ 749 N NH1 . ARG A 97 ? 1.4984 1.9792 2.1560 -0.1147 -0.0578 0.2370 124 ARG A NH1 750 N NH2 . ARG A 97 ? 1.3807 1.9099 2.1192 -0.1423 -0.0711 0.2998 124 ARG A NH2 751 N N . GLU A 98 ? 1.0998 1.6141 1.6598 -0.1012 0.0238 0.2751 125 GLU A N 752 C CA . GLU A 98 ? 1.1111 1.6485 1.6852 -0.1077 0.0287 0.3039 125 GLU A CA 753 C C . GLU A 98 ? 1.1127 1.7052 1.7253 -0.1113 0.0353 0.3452 125 GLU A C 754 O O . GLU A 98 ? 1.1261 1.7528 1.7388 -0.1074 0.0507 0.3711 125 GLU A O 755 C CB . GLU A 98 ? 1.1745 1.6834 1.7738 -0.1257 0.0033 0.3051 125 GLU A CB 756 C CG . GLU A 98 ? 1.2784 1.7560 1.9041 -0.1369 -0.0269 0.2899 125 GLU A CG 757 C CD . GLU A 98 ? 1.3433 1.7751 1.9274 -0.1268 -0.0300 0.2470 125 GLU A CD 758 O OE1 . GLU A 98 ? 1.3399 1.7364 1.9276 -0.1339 -0.0509 0.2323 125 GLU A OE1 759 O OE2 . GLU A 98 ? 1.3904 1.8228 1.9392 -0.1109 -0.0117 0.2291 125 GLU A OE2 760 N N . ASP A 99 ? 1.1160 1.7199 1.7625 -0.1179 0.0235 0.3529 126 ASP A N 761 C CA . ASP A 99 ? 1.1865 1.8465 1.8731 -0.1215 0.0300 0.3951 126 ASP A CA 762 C C . ASP A 99 ? 1.2103 1.9063 1.8675 -0.0997 0.0591 0.3975 126 ASP A C 763 O O . ASP A 99 ? 1.2507 1.9979 1.9362 -0.0987 0.0679 0.4319 126 ASP A O 764 C CB . ASP A 99 ? 1.2526 1.9129 1.9957 -0.1395 0.0022 0.4068 126 ASP A CB 765 C CG . ASP A 99 ? 1.3193 1.9228 2.0528 -0.1433 -0.0219 0.3668 126 ASP A CG 766 O OD1 . ASP A 99 ? 1.3677 1.9325 2.0564 -0.1350 -0.0182 0.3340 126 ASP A OD1 767 O OD2 . ASP A 99 ? 1.3150 1.9138 2.0870 -0.1539 -0.0455 0.3688 126 ASP A OD2 768 N N . GLN A 100 ? 1.2114 1.8818 1.8127 -0.0816 0.0735 0.3624 127 GLN A N 769 C CA . GLN A 100 ? 1.2041 1.9037 1.7725 -0.0587 0.1002 0.3615 127 GLN A CA 770 C C . GLN A 100 ? 1.1361 1.8188 1.6503 -0.0419 0.1169 0.3413 127 GLN A C 771 O O . GLN A 100 ? 1.1528 1.8388 1.6271 -0.0209 0.1349 0.3254 127 GLN A O 772 C CB . GLN A 100 ? 1.3200 2.0089 1.8782 -0.0511 0.1002 0.3396 127 GLN A CB 773 C CG . GLN A 100 ? 1.4229 2.0625 1.9832 -0.0610 0.0784 0.3095 127 GLN A CG 774 C CD . GLN A 100 ? 1.4709 2.1026 2.0082 -0.0474 0.0852 0.2863 127 GLN A CD 775 O OE1 . GLN A 100 ? 1.4921 2.1086 1.9831 -0.0303 0.1011 0.2631 127 GLN A OE1 776 N NE2 . GLN A 100 ? 1.4679 2.1106 2.0391 -0.0546 0.0726 0.2936 127 GLN A NE2 777 N N . ILE A 101 ? 1.0031 1.6663 1.5166 -0.0511 0.1093 0.3413 128 ILE A N 778 C CA . ILE A 101 ? 0.9022 1.5521 1.3682 -0.0360 0.1236 0.3253 128 ILE A CA 779 C C . ILE A 101 ? 0.9145 1.6168 1.3699 -0.0178 0.1459 0.3509 128 ILE A C 780 O O . ILE A 101 ? 1.0236 1.7693 1.5163 -0.0248 0.1465 0.3892 128 ILE A O 781 C CB . ILE A 101 ? 0.8248 1.4463 1.2958 -0.0503 0.1102 0.3231 128 ILE A CB 782 C CG1 . ILE A 101 ? 0.7220 1.2854 1.1787 -0.0575 0.0943 0.2861 128 ILE A CG1 783 C CG2 . ILE A 101 ? 0.8420 1.4719 1.2775 -0.0354 0.1265 0.3238 128 ILE A CG2 784 C CD1 . ILE A 101 ? 0.6590 1.1928 1.1179 -0.0698 0.0810 0.2815 128 ILE A CD1 785 N N . PRO A 102 ? 0.8299 1.5303 1.2357 0.0069 0.1637 0.3307 129 PRO A N 786 C CA . PRO A 102 ? 0.9415 1.6950 1.3366 0.0272 0.1836 0.3556 129 PRO A CA 787 C C . PRO A 102 ? 0.9902 1.7548 1.3795 0.0285 0.1868 0.3707 129 PRO A C 788 O O . PRO A 102 ? 0.9143 1.6372 1.2918 0.0193 0.1768 0.3519 129 PRO A O 789 C CB . PRO A 102 ? 0.8760 1.6176 1.2181 0.0544 0.1978 0.3254 129 PRO A CB 790 C CG . PRO A 102 ? 0.7629 1.4488 1.0948 0.0456 0.1857 0.2890 129 PRO A CG 791 C CD . PRO A 102 ? 0.7205 1.3764 1.0813 0.0188 0.1659 0.2891 129 PRO A CD 792 N N . ARG A 103 ? 1.0499 1.8731 1.4488 0.0405 0.2008 0.4063 130 ARG A N 793 C CA . ARG A 103 ? 1.1098 1.9513 1.4901 0.0521 0.2097 0.4184 130 ARG A CA 794 C C . ARG A 103 ? 1.0858 1.8965 1.4029 0.0767 0.2179 0.3801 130 ARG A C 795 O O . ARG A 103 ? 1.1013 1.9207 1.3875 0.1003 0.2294 0.3659 130 ARG A O 796 C CB . ARG A 103 ? 1.2060 2.1230 1.6034 0.0668 0.2262 0.4634 130 ARG A CB 797 C CG . ARG A 103 ? 1.2928 2.2453 1.7539 0.0459 0.2193 0.5014 130 ARG A CG 798 C CD . ARG A 103 ? 1.3606 2.3178 1.8705 0.0189 0.2049 0.5320 130 ARG A CD 799 N NE . ARG A 103 ? 1.4552 2.4510 1.9612 0.0331 0.2110 0.5645 130 ARG A NE 800 C CZ . ARG A 103 ? 1.5098 2.5099 2.0442 0.0179 0.2009 0.5902 130 ARG A CZ 801 N NH1 . ARG A 103 ? 1.5172 2.4822 2.0848 -0.0123 0.1829 0.5854 130 ARG A NH1 802 N NH2 . ARG A 103 ? 1.5565 2.5958 2.0860 0.0341 0.2075 0.6204 130 ARG A NH2 803 N N . GLY A 104 ? 1.0013 1.7769 1.3010 0.0716 0.2109 0.3641 131 GLY A N 804 C CA . GLY A 104 ? 1.0561 1.8002 1.3004 0.0928 0.2154 0.3286 131 GLY A CA 805 C C . GLY A 104 ? 1.0535 1.7305 1.2857 0.0789 0.2010 0.2900 131 GLY A C 806 O O . GLY A 104 ? 1.0667 1.7111 1.2612 0.0895 0.2001 0.2627 131 GLY A O 807 N N . PHE A 105 ? 0.9556 1.6138 1.2206 0.0561 0.1889 0.2884 132 PHE A N 808 C CA . PHE A 105 ? 0.8097 1.4093 1.0667 0.0434 0.1753 0.2549 132 PHE A CA 809 C C . PHE A 105 ? 0.8779 1.4511 1.1287 0.0340 0.1670 0.2491 132 PHE A C 810 O O . PHE A 105 ? 1.0261 1.6226 1.3014 0.0243 0.1648 0.2765 132 PHE A O 811 C CB . PHE A 105 ? 0.7790 1.3692 1.0752 0.0217 0.1623 0.2586 132 PHE A CB 812 C CG . PHE A 105 ? 0.7983 1.3373 1.0806 0.0166 0.1526 0.2235 132 PHE A CG 813 C CD1 . PHE A 105 ? 0.8244 1.3231 1.1097 0.0012 0.1380 0.2090 132 PHE A CD1 814 C CD2 . PHE A 105 ? 0.7817 1.3149 1.0481 0.0283 0.1583 0.2064 132 PHE A CD2 815 C CE1 . PHE A 105 ? 0.7952 1.2520 1.0680 -0.0014 0.1302 0.1794 132 PHE A CE1 816 C CE2 . PHE A 105 ? 0.7559 1.2464 1.0111 0.0246 0.1503 0.1775 132 PHE A CE2 817 C CZ . PHE A 105 ? 0.7657 1.2193 1.0240 0.0103 0.1367 0.1646 132 PHE A CZ 818 N N . PRO A 106 ? 0.8271 1.3546 1.0467 0.0376 0.1626 0.2160 133 PRO A N 819 C CA . PRO A 106 ? 0.8417 1.3485 1.0546 0.0304 0.1558 0.2125 133 PRO A CA 820 C C . PRO A 106 ? 0.8825 1.3816 1.1356 0.0037 0.1408 0.2277 133 PRO A C 821 O O . PRO A 106 ? 0.9051 1.3896 1.1829 -0.0111 0.1298 0.2241 133 PRO A O 822 C CB . PRO A 106 ? 0.8311 1.2883 1.0125 0.0349 0.1511 0.1750 133 PRO A CB 823 C CG . PRO A 106 ? 0.7742 1.2356 0.9346 0.0535 0.1603 0.1616 133 PRO A CG 824 C CD . PRO A 106 ? 0.8243 1.3212 1.0142 0.0494 0.1643 0.1840 133 PRO A CD 825 N N . THR A 107 ? 0.8890 1.3970 1.1471 -0.0007 0.1392 0.2433 134 THR A N 826 C CA . THR A 107 ? 0.8792 1.3755 1.1721 -0.0247 0.1232 0.2561 134 THR A CA 827 C C . THR A 107 ? 0.8387 1.2977 1.1084 -0.0265 0.1170 0.2360 134 THR A C 828 O O . THR A 107 ? 0.8064 1.2659 1.0406 -0.0092 0.1270 0.2261 134 THR A O 829 C CB . THR A 107 ? 0.9019 1.4464 1.2301 -0.0308 0.1256 0.2992 134 THR A CB 830 O OG1 . THR A 107 ? 1.0112 1.5415 1.3583 -0.0475 0.1126 0.3085 134 THR A OG1 831 C CG2 . THR A 107 ? 0.8917 1.4793 1.1944 -0.0062 0.1461 0.3137 134 THR A CG2 832 N N . ILE A 108 ? 0.8338 1.2608 1.1229 -0.0459 0.0995 0.2292 135 ILE A N 833 C CA . ILE A 108 ? 0.8558 1.2546 1.1298 -0.0494 0.0932 0.2175 135 ILE A CA 834 C C . ILE A 108 ? 0.9078 1.3258 1.2080 -0.0607 0.0879 0.2469 135 ILE A C 835 O O . ILE A 108 ? 0.9674 1.3778 1.3043 -0.0800 0.0716 0.2583 135 ILE A O 836 C CB . ILE A 108 ? 0.8938 1.2449 1.1688 -0.0610 0.0773 0.1907 135 ILE A CB 837 C CG1 . ILE A 108 ? 0.9356 1.2678 1.1841 -0.0493 0.0831 0.1628 135 ILE A CG1 838 C CG2 . ILE A 108 ? 0.8746 1.1989 1.1368 -0.0652 0.0703 0.1806 135 ILE A CG2 839 C CD1 . ILE A 108 ? 0.9222 1.2477 1.1295 -0.0312 0.0952 0.1463 135 ILE A CD1 840 N N . ASP A 109 ? 0.9606 1.4029 1.2415 -0.0474 0.1004 0.2588 136 ASP A N 841 C CA . ASP A 109 ? 1.0518 1.5194 1.3557 -0.0550 0.0985 0.2905 136 ASP A CA 842 C C . ASP A 109 ? 1.1406 1.5701 1.4477 -0.0694 0.0829 0.2796 136 ASP A C 843 O O . ASP A 109 ? 1.1290 1.5620 1.4725 -0.0868 0.0704 0.3014 136 ASP A O 844 C CB . ASP A 109 ? 1.0792 1.5844 1.3556 -0.0324 0.1171 0.3035 136 ASP A CB 845 C CG . ASP A 109 ? 1.1020 1.6415 1.3657 -0.0130 0.1332 0.3080 136 ASP A CG 846 O OD1 . ASP A 109 ? 1.0855 1.6764 1.3559 -0.0017 0.1457 0.3391 136 ASP A OD1 847 O OD2 . ASP A 109 ? 1.1390 1.6554 1.3861 -0.0081 0.1335 0.2812 136 ASP A OD2 848 N N . MET A 110 ? 1.2545 1.6474 1.5249 -0.0619 0.0828 0.2464 137 MET A N 849 C CA . MET A 110 ? 1.2649 1.6196 1.5362 -0.0744 0.0680 0.2327 137 MET A CA 850 C C . MET A 110 ? 1.2235 1.5380 1.4670 -0.0694 0.0656 0.1949 137 MET A C 851 O O . MET A 110 ? 1.2517 1.5678 1.4658 -0.0531 0.0774 0.1799 137 MET A O 852 C CB . MET A 110 ? 1.3403 1.7032 1.5962 -0.0687 0.0724 0.2417 137 MET A CB 853 C CG . MET A 110 ? 1.4178 1.7434 1.6754 -0.0812 0.0573 0.2294 137 MET A CG 854 S SD . MET A 110 ? 1.8459 2.1912 2.1357 -0.0945 0.0496 0.2651 137 MET A SD 855 C CE . MET A 110 ? 1.7497 2.0431 2.0315 -0.1052 0.0323 0.2400 137 MET A CE 856 N N . GLY A 111 ? 1.1219 1.4011 1.3754 -0.0826 0.0496 0.1804 138 GLY A N 857 C CA . GLY A 111 ? 0.9680 1.2132 1.2010 -0.0786 0.0470 0.1486 138 GLY A CA 858 C C . GLY A 111 ? 0.8315 1.0447 1.0500 -0.0815 0.0389 0.1321 138 GLY A C 859 O O . GLY A 111 ? 0.8377 1.0517 1.0646 -0.0885 0.0331 0.1441 138 GLY A O 860 N N . PRO A 112 ? 0.8072 0.9935 1.0049 -0.0758 0.0387 0.1055 139 PRO A N 861 C CA . PRO A 112 ? 0.8399 0.9978 1.0229 -0.0770 0.0323 0.0896 139 PRO A CA 862 C C . PRO A 112 ? 0.8669 1.0095 1.0734 -0.0913 0.0151 0.0930 139 PRO A C 863 O O . PRO A 112 ? 0.7786 0.9247 1.0105 -0.0991 0.0061 0.1001 139 PRO A O 864 C CB . PRO A 112 ? 0.8090 0.9469 0.9737 -0.0690 0.0351 0.0653 139 PRO A CB 865 C CG . PRO A 112 ? 0.8442 0.9924 1.0231 -0.0692 0.0362 0.0675 139 PRO A CG 866 C CD . PRO A 112 ? 0.8198 1.0016 1.0109 -0.0691 0.0432 0.0910 139 PRO A CD 867 N N . GLN A 113 ? 0.9055 1.0309 1.1045 -0.0941 0.0089 0.0878 140 GLN A N 868 C CA . GLN A 113 ? 0.9156 1.0263 1.1358 -0.1063 -0.0086 0.0914 140 GLN A CA 869 C C . GLN A 113 ? 0.8977 0.9782 1.1032 -0.1041 -0.0156 0.0687 140 GLN A C 870 O O . GLN A 113 ? 0.9238 0.9969 1.1044 -0.0954 -0.0067 0.0552 140 GLN A O 871 C CB . GLN A 113 ? 1.0091 1.1318 1.2390 -0.1127 -0.0106 0.1125 140 GLN A CB 872 C CG . GLN A 113 ? 1.0542 1.2138 1.2953 -0.1117 0.0000 0.1386 140 GLN A CG 873 C CD . GLN A 113 ? 1.0701 1.2419 1.3504 -0.1239 -0.0110 0.1581 140 GLN A CD 874 O OE1 . GLN A 113 ? 1.0929 1.2515 1.3977 -0.1362 -0.0289 0.1644 140 GLN A OE1 875 N NE2 . GLN A 113 ? 1.1068 1.3032 1.3943 -0.1202 -0.0018 0.1676 140 GLN A NE2 876 N N . LEU A 114 ? 0.8395 0.9033 1.0619 -0.1110 -0.0329 0.0648 141 LEU A N 877 C CA . LEU A 114 ? 0.7992 0.8374 1.0111 -0.1091 -0.0419 0.0473 141 LEU A CA 878 C C . LEU A 114 ? 0.7053 0.7411 0.8982 -0.1071 -0.0345 0.0472 141 LEU A C 879 O O . LEU A 114 ? 0.7487 0.7963 0.9466 -0.1118 -0.0328 0.0637 141 LEU A O 880 C CB . LEU A 114 ? 0.8532 0.8769 1.0875 -0.1171 -0.0639 0.0489 141 LEU A CB 881 C CG . LEU A 114 ? 0.9436 0.9429 1.1676 -0.1110 -0.0746 0.0280 141 LEU A CG 882 C CD1 . LEU A 114 ? 1.0352 1.0230 1.2791 -0.1122 -0.0957 0.0229 141 LEU A CD1 883 C CD2 . LEU A 114 ? 0.9538 0.9410 1.1690 -0.1130 -0.0781 0.0271 141 LEU A CD2 884 N N . LYS A 115 ? 0.6851 0.7073 0.8574 -0.0996 -0.0303 0.0299 142 LYS A N 885 C CA . LYS A 115 ? 0.7261 0.7438 0.8812 -0.0975 -0.0255 0.0282 142 LYS A CA 886 C C . LYS A 115 ? 0.7644 0.7610 0.9105 -0.0944 -0.0317 0.0118 142 LYS A C 887 O O . LYS A 115 ? 0.8510 0.8415 0.9943 -0.0889 -0.0313 -0.0001 142 LYS A O 888 C CB . LYS A 115 ? 0.8947 0.9248 1.0315 -0.0889 -0.0098 0.0273 142 LYS A CB 889 C CG . LYS A 115 ? 1.1216 1.1455 1.2388 -0.0846 -0.0064 0.0226 142 LYS A CG 890 C CD . LYS A 115 ? 1.2251 1.2547 1.3465 -0.0903 -0.0106 0.0367 142 LYS A CD 891 C CE . LYS A 115 ? 1.2472 1.2702 1.3477 -0.0846 -0.0081 0.0304 142 LYS A CE 892 N NZ . LYS A 115 ? 1.2625 1.2867 1.3676 -0.0906 -0.0142 0.0421 142 LYS A NZ 893 N N . VAL A 116 ? 0.7453 0.7330 0.8873 -0.0974 -0.0371 0.0128 143 VAL A N 894 C CA . VAL A 116 ? 0.7554 0.7264 0.8878 -0.0939 -0.0415 -0.0005 143 VAL A CA 895 C C . VAL A 116 ? 0.8903 0.8594 1.0052 -0.0907 -0.0342 -0.0034 143 VAL A C 896 O O . VAL A 116 ? 0.9521 0.9256 1.0635 -0.0936 -0.0337 0.0054 143 VAL A O 897 C CB . VAL A 116 ? 0.6558 0.6142 0.7988 -0.0992 -0.0574 0.0005 143 VAL A CB 898 C CG1 . VAL A 116 ? 0.6592 0.6033 0.7924 -0.0936 -0.0616 -0.0128 143 VAL A CG1 899 C CG2 . VAL A 116 ? 0.6566 0.6144 0.8187 -0.1020 -0.0687 0.0029 143 VAL A CG2 900 N N . VAL A 117 ? 0.9376 0.9009 1.0427 -0.0842 -0.0295 -0.0150 144 VAL A N 901 C CA . VAL A 117 ? 0.9775 0.9368 1.0682 -0.0808 -0.0254 -0.0193 144 VAL A CA 902 C C . VAL A 117 ? 0.9181 0.8640 1.0079 -0.0795 -0.0312 -0.0281 144 VAL A C 903 O O . VAL A 117 ? 0.9437 0.8872 1.0404 -0.0771 -0.0336 -0.0328 144 VAL A O 904 C CB . VAL A 117 ? 0.7359 0.7013 0.8179 -0.0739 -0.0155 -0.0231 144 VAL A CB 905 C CG1 . VAL A 117 ? 0.6860 0.6461 0.7718 -0.0699 -0.0141 -0.0319 144 VAL A CG1 906 C CG2 . VAL A 117 ? 0.8801 0.8431 0.9467 -0.0696 -0.0138 -0.0257 144 VAL A CG2 907 N N . GLU A 118 ? 0.9055 0.8447 0.9870 -0.0801 -0.0337 -0.0294 145 GLU A N 908 C CA . GLU A 118 ? 0.9283 0.8574 1.0097 -0.0785 -0.0384 -0.0362 145 GLU A CA 909 C C . GLU A 118 ? 0.9631 0.8914 1.0433 -0.0734 -0.0333 -0.0421 145 GLU A C 910 O O . GLU A 118 ? 1.0310 0.9614 1.1040 -0.0709 -0.0286 -0.0432 145 GLU A O 911 C CB . GLU A 118 ? 0.9686 0.8909 1.0428 -0.0812 -0.0436 -0.0351 145 GLU A CB 912 C CG . GLU A 118 ? 0.9716 0.8909 1.0513 -0.0862 -0.0519 -0.0300 145 GLU A CG 913 C CD . GLU A 118 ? 0.9723 0.8907 1.0449 -0.0895 -0.0543 -0.0240 145 GLU A CD 914 O OE1 . GLU A 118 ? 1.0634 0.9780 1.1257 -0.0871 -0.0538 -0.0280 145 GLU A OE1 915 O OE2 . GLU A 118 ? 0.8337 0.7559 0.9123 -0.0945 -0.0577 -0.0144 145 GLU A OE2 916 N N . ARG A 119 ? 0.8406 0.7672 0.9287 -0.0709 -0.0349 -0.0449 146 ARG A N 917 C CA . ARG A 119 ? 0.7898 0.7160 0.8821 -0.0672 -0.0316 -0.0475 146 ARG A CA 918 C C . ARG A 119 ? 0.8708 0.7885 0.9558 -0.0676 -0.0342 -0.0508 146 ARG A C 919 O O . ARG A 119 ? 0.9404 0.8524 1.0197 -0.0701 -0.0396 -0.0512 146 ARG A O 920 C CB . ARG A 119 ? 0.8748 0.8034 0.9782 -0.0643 -0.0339 -0.0464 146 ARG A CB 921 C CG . ARG A 119 ? 0.9744 0.9037 1.0877 -0.0620 -0.0320 -0.0453 146 ARG A CG 922 C CD . ARG A 119 ? 1.0036 0.9399 1.1296 -0.0587 -0.0338 -0.0403 146 ARG A CD 923 N NE . ARG A 119 ? 1.0596 0.9912 1.1825 -0.0608 -0.0405 -0.0407 146 ARG A NE 924 C CZ . ARG A 119 ? 1.1297 1.0537 1.2551 -0.0645 -0.0458 -0.0405 146 ARG A CZ 925 N NH1 . ARG A 119 ? 1.0728 0.9916 1.2049 -0.0661 -0.0469 -0.0406 146 ARG A NH1 926 N NH2 . ARG A 119 ? 1.1619 1.0826 1.2840 -0.0659 -0.0516 -0.0407 146 ARG A NH2 927 N N . THR A 120 ? 1.0149 0.9315 1.0994 -0.0642 -0.0313 -0.0537 147 THR A N 928 C CA . THR A 120 ? 1.0713 0.9781 1.1484 -0.0617 -0.0361 -0.0594 147 THR A CA 929 C C . THR A 120 ? 1.1354 1.0445 1.1938 -0.0584 -0.0343 -0.0612 147 THR A C 930 O O . THR A 120 ? 1.2841 1.1873 1.3322 -0.0522 -0.0375 -0.0676 147 THR A O 931 C CB . THR A 120 ? 1.3738 1.2711 1.4561 -0.0645 -0.0453 -0.0605 147 THR A CB 932 O OG1 . THR A 120 ? 1.4946 1.3849 1.5898 -0.0633 -0.0503 -0.0622 147 THR A OG1 933 C CG2 . THR A 120 ? 1.3291 1.2199 1.3952 -0.0638 -0.0507 -0.0645 147 THR A CG2 934 N N . ARG A 121 ? 1.0693 0.9883 1.1242 -0.0612 -0.0297 -0.0548 148 ARG A N 935 C CA . ARG A 121 ? 1.1072 1.0347 1.1476 -0.0574 -0.0262 -0.0521 148 ARG A CA 936 C C . ARG A 121 ? 1.0429 0.9809 1.0811 -0.0522 -0.0181 -0.0510 148 ARG A C 937 O O . ARG A 121 ? 1.0242 0.9635 1.0736 -0.0535 -0.0150 -0.0511 148 ARG A O 938 C CB . ARG A 121 ? 1.2602 1.1950 1.3022 -0.0637 -0.0262 -0.0423 148 ARG A CB 939 C CG . ARG A 121 ? 1.4422 1.3676 1.4840 -0.0679 -0.0340 -0.0428 148 ARG A CG 940 C CD . ARG A 121 ? 1.5589 1.4852 1.5843 -0.0632 -0.0359 -0.0429 148 ARG A CD 941 N NE . ARG A 121 ? 1.6087 1.5255 1.6336 -0.0669 -0.0437 -0.0440 148 ARG A NE 942 C CZ . ARG A 121 ? 1.6406 1.5604 1.6670 -0.0722 -0.0459 -0.0356 148 ARG A CZ 943 N NH1 . ARG A 121 ? 1.6367 1.5688 1.6678 -0.0753 -0.0417 -0.0242 148 ARG A NH1 944 N NH2 . ARG A 121 ? 1.6443 1.5548 1.6696 -0.0746 -0.0532 -0.0376 148 ARG A NH2 945 N N . THR A 122 ? 0.9285 0.8761 0.9519 -0.0449 -0.0145 -0.0493 149 THR A N 946 C CA . THR A 122 ? 0.9127 0.8731 0.9323 -0.0381 -0.0065 -0.0475 149 THR A CA 947 C C . THR A 122 ? 0.8696 0.8466 0.8997 -0.0447 -0.0002 -0.0341 149 THR A C 948 O O . THR A 122 ? 0.9150 0.8991 0.9470 -0.0498 -0.0012 -0.0242 149 THR A O 949 C CB . THR A 122 ? 1.0498 1.0167 1.0478 -0.0243 -0.0055 -0.0509 149 THR A CB 950 O OG1 . THR A 122 ? 1.1249 1.0727 1.1152 -0.0180 -0.0150 -0.0652 149 THR A OG1 951 C CG2 . THR A 122 ? 1.1242 1.1062 1.1176 -0.0157 0.0031 -0.0487 149 THR A CG2 952 N N . ALA A 123 ? 0.8396 0.8225 0.8783 -0.0447 0.0050 -0.0332 150 ALA A N 953 C CA . ALA A 123 ? 0.8342 0.8338 0.8839 -0.0496 0.0099 -0.0208 150 ALA A CA 954 C C . ALA A 123 ? 0.8647 0.8824 0.9077 -0.0407 0.0189 -0.0167 150 ALA A C 955 O O . ALA A 123 ? 0.8331 0.8468 0.8707 -0.0333 0.0215 -0.0257 150 ALA A O 956 C CB . ALA A 123 ? 0.7888 0.7825 0.8555 -0.0567 0.0074 -0.0224 150 ALA A CB 957 N N . THR A 124 ? 0.8918 0.9306 0.9370 -0.0412 0.0234 -0.0017 151 THR A N 958 C CA . THR A 124 ? 0.8550 0.9150 0.8949 -0.0318 0.0327 0.0042 151 THR A CA 959 C C . THR A 124 ? 0.8357 0.9125 0.8968 -0.0403 0.0356 0.0192 151 THR A C 960 O O . THR A 124 ? 0.8249 0.9126 0.8995 -0.0488 0.0332 0.0348 151 THR A O 961 C CB . THR A 124 ? 0.8783 0.9564 0.9001 -0.0198 0.0373 0.0112 151 THR A CB 962 O OG1 . THR A 124 ? 0.9998 1.0603 1.0019 -0.0111 0.0319 -0.0042 151 THR A OG1 963 C CG2 . THR A 124 ? 0.8226 0.9243 0.8366 -0.0067 0.0474 0.0162 151 THR A CG2 964 N N . MET A 125 ? 0.8244 0.9036 0.8899 -0.0377 0.0398 0.0149 152 MET A N 965 C CA . MET A 125 ? 0.9145 1.0111 0.9993 -0.0436 0.0423 0.0282 152 MET A CA 966 C C . MET A 125 ? 0.9676 1.0931 1.0451 -0.0331 0.0528 0.0402 152 MET A C 967 O O . MET A 125 ? 1.0473 1.1744 1.1035 -0.0185 0.0584 0.0312 152 MET A O 968 C CB . MET A 125 ? 0.9059 0.9922 0.9990 -0.0452 0.0414 0.0180 152 MET A CB 969 C CG . MET A 125 ? 0.8221 0.8833 0.9194 -0.0514 0.0324 0.0058 152 MET A CG 970 S SD . MET A 125 ? 1.2946 1.3497 1.4092 -0.0651 0.0203 0.0140 152 MET A SD 971 C CE . MET A 125 ? 0.8002 0.8692 0.9392 -0.0714 0.0173 0.0248 152 MET A CE 972 N N . LEU A 126 ? 0.9227 1.0718 1.0189 -0.0395 0.0544 0.0614 153 LEU A N 973 C CA . LEU A 126 ? 0.8882 1.0712 0.9791 -0.0287 0.0651 0.0777 153 LEU A CA 974 C C . LEU A 126 ? 0.9625 1.1679 1.0737 -0.0316 0.0697 0.0914 153 LEU A C 975 O O . LEU A 126 ? 1.0817 1.2794 1.2171 -0.0454 0.0621 0.0941 153 LEU A O 976 C CB . LEU A 126 ? 0.8207 1.0209 0.9167 -0.0317 0.0645 0.0976 153 LEU A CB 977 C CG . LEU A 126 ? 0.9758 1.1740 1.0436 -0.0188 0.0666 0.0909 153 LEU A CG 978 C CD1 . LEU A 126 ? 1.0693 1.2785 1.1475 -0.0263 0.0632 0.1103 153 LEU A CD1 979 C CD2 . LEU A 126 ? 1.0514 1.2740 1.0949 0.0039 0.0782 0.0911 153 LEU A CD2 980 N N . CYS A 127 ? 1.0373 1.2703 1.1376 -0.0169 0.0814 0.0989 154 CYS A N 981 C CA . CYS A 127 ? 1.1197 1.3759 1.2396 -0.0191 0.0861 0.1127 154 CYS A CA 982 C C . CYS A 127 ? 1.1428 1.4404 1.2549 -0.0040 0.0988 0.1322 154 CYS A C 983 O O . CYS A 127 ? 1.2219 1.5235 1.3037 0.0150 0.1054 0.1228 154 CYS A O 984 C CB . CYS A 127 ? 1.1716 1.4105 1.2832 -0.0141 0.0873 0.0919 154 CYS A CB 985 S SG . CYS A 127 ? 0.9378 1.2034 1.0660 -0.0119 0.0947 0.1031 154 CYS A SG 986 N N . ALA A 128 ? 1.1134 1.4429 1.2536 -0.0109 0.1016 0.1592 155 ALA A N 987 C CA . ALA A 128 ? 1.1124 1.4879 1.2489 0.0042 0.1149 0.1816 155 ALA A CA 988 C C . ALA A 128 ? 1.0794 1.4731 1.2366 0.0014 0.1186 0.1909 155 ALA A C 989 O O . ALA A 128 ? 1.0827 1.4758 1.2762 -0.0182 0.1098 0.2037 155 ALA A O 990 C CB . ALA A 128 ? 1.1775 1.5812 1.3333 -0.0022 0.1150 0.2126 155 ALA A CB 991 N N . ALA A 129 ? 1.0653 1.4769 1.2007 0.0219 0.1304 0.1857 156 ALA A N 992 C CA . ALA A 129 ? 1.0748 1.5027 1.2252 0.0221 0.1349 0.1914 156 ALA A CA 993 C C . ALA A 129 ? 1.1398 1.6154 1.2779 0.0446 0.1506 0.2088 156 ALA A C 994 O O . ALA A 129 ? 1.2002 1.6828 1.3045 0.0663 0.1575 0.2013 156 ALA A O 995 C CB . ALA A 129 ? 1.0438 1.4346 1.1783 0.0242 0.1313 0.1593 156 ALA A CB 996 N N . SER A 130 ? 1.1119 1.6204 1.2761 0.0416 0.1558 0.2307 157 SER A N 997 C CA . SER A 130 ? 1.1084 1.6665 1.2613 0.0648 0.1717 0.2488 157 SER A CA 998 C C . SER A 130 ? 1.1757 1.7463 1.3410 0.0661 0.1759 0.2501 157 SER A C 999 O O . SER A 130 ? 1.1840 1.7290 1.3716 0.0470 0.1660 0.2415 157 SER A O 1000 C CB . SER A 130 ? 1.0823 1.6895 1.2600 0.0626 0.1773 0.2901 157 SER A CB 1001 O OG . SER A 130 ? 1.0603 1.6653 1.2871 0.0331 0.1657 0.3104 157 SER A OG 1002 N N . GLY A 131 ? 1.2331 1.8448 1.3831 0.0903 0.1905 0.2607 158 GLY A N 1003 C CA . GLY A 131 ? 1.2018 1.8286 1.3609 0.0943 0.1958 0.2623 158 GLY A CA 1004 C C . GLY A 131 ? 1.1481 1.8142 1.2765 0.1281 0.2118 0.2661 158 GLY A C 1005 O O . GLY A 131 ? 1.1051 1.7851 1.2034 0.1495 0.2179 0.2658 158 GLY A O 1006 N N . ASN A 132 ? 1.1517 1.8358 1.2866 0.1344 0.2180 0.2690 159 ASN A N 1007 C CA . ASN A 132 ? 1.1694 1.8888 1.2738 0.1685 0.2324 0.2696 159 ASN A CA 1008 C C . ASN A 132 ? 1.0396 1.7374 1.1312 0.1757 0.2321 0.2445 159 ASN A C 1009 O O . ASN A 132 ? 1.0256 1.7327 1.1479 0.1616 0.2319 0.2554 159 ASN A O 1010 C CB . ASN A 132 ? 1.1914 1.9816 1.3224 0.1744 0.2454 0.3149 159 ASN A CB 1011 C CG . ASN A 132 ? 1.1477 1.9812 1.2428 0.2145 0.2613 0.3180 159 ASN A CG 1012 O OD1 . ASN A 132 ? 1.1483 1.9593 1.1958 0.2397 0.2611 0.2873 159 ASN A OD1 1013 N ND2 . ASN A 132 ? 1.1475 2.0441 1.2663 0.2217 0.2740 0.3557 159 ASN A ND2 1014 N N . PRO A 133 ? 0.9724 1.6413 1.0195 0.1984 0.2310 0.2111 160 PRO A N 1015 C CA . PRO A 133 ? 1.0487 1.7017 1.0567 0.2175 0.2286 0.1933 160 PRO A CA 1016 C C . PRO A 133 ? 1.1049 1.7166 1.1190 0.1949 0.2160 0.1832 160 PRO A C 1017 O O . PRO A 133 ? 1.0889 1.6723 1.1321 0.1655 0.2070 0.1811 160 PRO A O 1018 C CB . PRO A 133 ? 0.9802 1.6013 0.9511 0.2396 0.2252 0.1573 160 PRO A CB 1019 C CG . PRO A 133 ? 0.8829 1.4785 0.8779 0.2183 0.2205 0.1491 160 PRO A CG 1020 C CD . PRO A 133 ? 0.9016 1.5419 0.9377 0.2030 0.2283 0.1850 160 PRO A CD 1021 N N . ASP A 134 ? 1.1335 1.7437 1.1197 0.2105 0.2151 0.1771 161 ASP A N 1022 C CA . ASP A 134 ? 1.1402 1.7105 1.1269 0.1929 0.2032 0.1649 161 ASP A CA 1023 C C . ASP A 134 ? 1.1003 1.6106 1.0833 0.1801 0.1905 0.1310 161 ASP A C 1024 O O . ASP A 134 ? 1.1286 1.6182 1.0823 0.1994 0.1880 0.1051 161 ASP A O 1025 C CB . ASP A 134 ? 1.2107 1.7881 1.1613 0.2176 0.2038 0.1589 161 ASP A CB 1026 C CG . ASP A 134 ? 1.2788 1.9180 1.2371 0.2280 0.2166 0.1966 161 ASP A CG 1027 O OD1 . ASP A 134 ? 1.2364 1.8868 1.2284 0.2038 0.2157 0.2219 161 ASP A OD1 1028 O OD2 . ASP A 134 ? 1.3581 2.0362 1.2897 0.2615 0.2270 0.2020 161 ASP A OD2 1029 N N . PRO A 135 ? 0.9917 1.4755 1.0053 0.1486 0.1820 0.1321 162 PRO A N 1030 C CA . PRO A 135 ? 1.0431 1.4769 1.0600 0.1342 0.1713 0.1060 162 PRO A CA 1031 C C . PRO A 135 ? 1.1227 1.5103 1.1181 0.1343 0.1600 0.0790 162 PRO A C 1032 O O . PRO A 135 ? 1.1648 1.5524 1.1516 0.1354 0.1575 0.0819 162 PRO A O 1033 C CB . PRO A 135 ? 1.0117 1.4443 1.0700 0.1036 0.1666 0.1224 162 PRO A CB 1034 C CG . PRO A 135 ? 0.9616 1.4209 1.0320 0.0980 0.1683 0.1476 162 PRO A CG 1035 C CD . PRO A 135 ? 0.9552 1.4588 1.0043 0.1258 0.1814 0.1610 162 PRO A CD 1036 N N . GLU A 136 ? 1.1885 1.5384 1.1783 0.1325 0.1531 0.0548 163 GLU A N 1037 C CA . GLU A 136 ? 1.2371 1.5416 1.2177 0.1259 0.1408 0.0324 163 GLU A CA 1038 C C . GLU A 136 ? 1.1677 1.4532 1.1768 0.0969 0.1341 0.0369 163 GLU A C 1039 O O . GLU A 136 ? 1.1453 1.4374 1.1792 0.0828 0.1355 0.0462 163 GLU A O 1040 C CB . GLU A 136 ? 1.3225 1.5971 1.2878 0.1371 0.1355 0.0076 163 GLU A CB 1041 C CG . GLU A 136 ? 1.5129 1.7939 1.4440 0.1681 0.1360 -0.0042 163 GLU A CG 1042 C CD . GLU A 136 ? 1.6504 1.9265 1.5734 0.1825 0.1371 -0.0162 163 GLU A CD 1043 O OE1 . GLU A 136 ? 1.6788 1.9853 1.5857 0.2053 0.1451 -0.0113 163 GLU A OE1 1044 O OE2 . GLU A 136 ? 1.6775 1.9210 1.6107 0.1718 0.1300 -0.0293 163 GLU A OE2 1045 N N . ILE A 137 ? 1.0777 1.3408 1.0820 0.0899 0.1259 0.0299 164 ILE A N 1046 C CA . ILE A 137 ? 0.9748 1.2167 1.0013 0.0658 0.1180 0.0308 164 ILE A CA 1047 C C . ILE A 137 ? 0.9818 1.1820 1.0042 0.0611 0.1085 0.0083 164 ILE A C 1048 O O . ILE A 137 ? 0.9883 1.1690 0.9907 0.0712 0.1031 -0.0068 164 ILE A O 1049 C CB . ILE A 137 ? 0.9197 1.1693 0.9489 0.0588 0.1157 0.0431 164 ILE A CB 1050 C CG1 . ILE A 137 ? 0.9025 1.1963 0.9450 0.0596 0.1247 0.0710 164 ILE A CG1 1051 C CG2 . ILE A 137 ? 0.9423 1.1668 0.9913 0.0364 0.1058 0.0410 164 ILE A CG2 1052 C CD1 . ILE A 137 ? 0.9691 1.2753 1.0181 0.0526 0.1230 0.0876 164 ILE A CD1 1053 N N . THR A 138 ? 1.0081 1.1965 1.0509 0.0465 0.1056 0.0072 165 THR A N 1054 C CA . THR A 138 ? 0.9963 1.1507 1.0415 0.0397 0.0973 -0.0087 165 THR A CA 1055 C C . THR A 138 ? 0.9145 1.0603 0.9802 0.0206 0.0912 -0.0038 165 THR A C 1056 O O . THR A 138 ? 0.9186 1.0822 0.9994 0.0117 0.0920 0.0110 165 THR A O 1057 C CB . THR A 138 ? 1.0844 1.2319 1.1317 0.0450 0.0994 -0.0172 165 THR A CB 1058 O OG1 . THR A 138 ? 1.0827 1.2448 1.1504 0.0355 0.1027 -0.0070 165 THR A OG1 1059 C CG2 . THR A 138 ? 1.1418 1.2999 1.1698 0.0651 0.1048 -0.0216 165 THR A CG2 1060 N N . TRP A 139 ? 0.8472 0.9663 0.9145 0.0151 0.0840 -0.0153 166 TRP A N 1061 C CA . TRP A 139 ? 0.7816 0.8912 0.8639 0.0004 0.0770 -0.0127 166 TRP A CA 1062 C C . TRP A 139 ? 0.7252 0.8204 0.8185 -0.0040 0.0735 -0.0199 166 TRP A C 1063 O O . TRP A 139 ? 0.7835 0.8654 0.8716 0.0020 0.0736 -0.0293 166 TRP A O 1064 C CB . TRP A 139 ? 0.7174 0.8120 0.7908 -0.0019 0.0709 -0.0169 166 TRP A CB 1065 C CG . TRP A 139 ? 0.8004 0.9105 0.8664 -0.0002 0.0728 -0.0070 166 TRP A CG 1066 C CD1 . TRP A 139 ? 0.8925 1.0120 0.9391 0.0138 0.0772 -0.0079 166 TRP A CD1 1067 C CD2 . TRP A 139 ? 0.8111 0.9300 0.8891 -0.0114 0.0696 0.0059 166 TRP A CD2 1068 N NE1 . TRP A 139 ? 0.8967 1.0338 0.9422 0.0124 0.0787 0.0054 166 TRP A NE1 1069 C CE2 . TRP A 139 ? 0.8758 1.0120 0.9420 -0.0042 0.0739 0.0148 166 TRP A CE2 1070 C CE3 . TRP A 139 ? 0.7794 0.8932 0.8770 -0.0256 0.0624 0.0108 166 TRP A CE3 1071 C CZ2 . TRP A 139 ? 0.8726 1.0221 0.9487 -0.0124 0.0721 0.0307 166 TRP A CZ2 1072 C CZ3 . TRP A 139 ? 0.8055 0.9290 0.9129 -0.0340 0.0587 0.0246 166 TRP A CZ3 1073 C CH2 . TRP A 139 ? 0.8407 0.9823 0.9387 -0.0283 0.0640 0.0356 166 TRP A CH2 1074 N N . PHE A 140 ? 0.6261 0.7247 0.7354 -0.0136 0.0692 -0.0147 167 PHE A N 1075 C CA . PHE A 140 ? 0.5998 0.6877 0.7178 -0.0154 0.0653 -0.0210 167 PHE A CA 1076 C C . PHE A 140 ? 0.6618 0.7380 0.7850 -0.0235 0.0561 -0.0221 167 PHE A C 1077 O O . PHE A 140 ? 0.6557 0.7356 0.7830 -0.0305 0.0516 -0.0155 167 PHE A O 1078 C CB . PHE A 140 ? 0.6934 0.7949 0.8240 -0.0157 0.0664 -0.0170 167 PHE A CB 1079 C CG . PHE A 140 ? 0.8145 0.9252 0.9409 -0.0065 0.0752 -0.0180 167 PHE A CG 1080 C CD1 . PHE A 140 ? 0.9153 1.0418 1.0359 -0.0021 0.0819 -0.0117 167 PHE A CD1 1081 C CD2 . PHE A 140 ? 0.8286 0.9342 0.9568 -0.0011 0.0770 -0.0241 167 PHE A CD2 1082 C CE1 . PHE A 140 ? 0.9235 1.0582 1.0391 0.0077 0.0896 -0.0133 167 PHE A CE1 1083 C CE2 . PHE A 140 ? 0.8288 0.9418 0.9535 0.0075 0.0845 -0.0249 167 PHE A CE2 1084 C CZ . PHE A 140 ? 0.8467 0.9732 0.9647 0.0119 0.0904 -0.0204 167 PHE A CZ 1085 N N . LYS A 141 ? 0.6745 0.7380 0.7984 -0.0218 0.0533 -0.0291 168 LYS A N 1086 C CA . LYS A 141 ? 0.6557 0.7095 0.7839 -0.0269 0.0447 -0.0309 168 LYS A CA 1087 C C . LYS A 141 ? 0.7859 0.8404 0.9214 -0.0224 0.0425 -0.0345 168 LYS A C 1088 O O . LYS A 141 ? 0.8502 0.9037 0.9849 -0.0159 0.0475 -0.0368 168 LYS A O 1089 C CB . LYS A 141 ? 0.5758 0.6154 0.6958 -0.0275 0.0431 -0.0346 168 LYS A CB 1090 C CG . LYS A 141 ? 0.5980 0.6286 0.7223 -0.0265 0.0386 -0.0382 168 LYS A CG 1091 C CD . LYS A 141 ? 0.6355 0.6583 0.7596 -0.0324 0.0304 -0.0383 168 LYS A CD 1092 C CE . LYS A 141 ? 0.7545 0.7726 0.8829 -0.0291 0.0269 -0.0407 168 LYS A CE 1093 N NZ . LYS A 141 ? 0.7926 0.8069 0.9220 -0.0252 0.0313 -0.0408 168 LYS A NZ 1094 N N . ASP A 142 ? 0.8048 0.8612 0.9480 -0.0248 0.0340 -0.0345 169 ASP A N 1095 C CA . ASP A 142 ? 0.7448 0.8039 0.8925 -0.0173 0.0304 -0.0388 169 ASP A CA 1096 C C . ASP A 142 ? 0.7153 0.7851 0.8643 -0.0101 0.0388 -0.0385 169 ASP A C 1097 O O . ASP A 142 ? 0.8207 0.8933 0.9696 -0.0015 0.0420 -0.0404 169 ASP A O 1098 C CB . ASP A 142 ? 0.7747 0.8265 0.9189 -0.0129 0.0290 -0.0420 169 ASP A CB 1099 C CG . ASP A 142 ? 0.8187 0.8610 0.9624 -0.0179 0.0187 -0.0436 169 ASP A CG 1100 O OD1 . ASP A 142 ? 0.7821 0.8238 0.9307 -0.0229 0.0099 -0.0433 169 ASP A OD1 1101 O OD2 . ASP A 142 ? 0.8741 0.9099 1.0144 -0.0172 0.0184 -0.0443 169 ASP A OD2 1102 N N . PHE A 143 ? 0.7462 0.8238 0.8969 -0.0134 0.0428 -0.0344 170 PHE A N 1103 C CA . PHE A 143 ? 0.7979 0.8873 0.9508 -0.0076 0.0498 -0.0333 170 PHE A CA 1104 C C . PHE A 143 ? 0.8710 0.9591 1.0168 -0.0021 0.0605 -0.0336 170 PHE A C 1105 O O . PHE A 143 ? 0.9321 1.0289 1.0791 0.0038 0.0666 -0.0331 170 PHE A O 1106 C CB . PHE A 143 ? 0.7850 0.8800 0.9436 -0.0001 0.0451 -0.0372 170 PHE A CB 1107 C CG . PHE A 143 ? 0.8226 0.9178 0.9899 -0.0035 0.0312 -0.0388 170 PHE A CG 1108 C CD1 . PHE A 143 ? 0.8702 0.9640 1.0442 -0.0147 0.0252 -0.0333 170 PHE A CD1 1109 C CD2 . PHE A 143 ? 0.8072 0.9045 0.9769 0.0056 0.0230 -0.0452 170 PHE A CD2 1110 C CE1 . PHE A 143 ? 0.8519 0.9436 1.0378 -0.0186 0.0096 -0.0339 170 PHE A CE1 1111 C CE2 . PHE A 143 ? 0.7780 0.8723 0.9563 0.0037 0.0068 -0.0486 170 PHE A CE2 1112 C CZ . PHE A 143 ? 0.8117 0.9018 0.9996 -0.0094 -0.0007 -0.0428 170 PHE A CZ 1113 N N . LEU A 144 ? 0.7660 0.8423 0.9054 -0.0035 0.0615 -0.0349 171 LEU A N 1114 C CA . LEU A 144 ? 0.6410 0.7127 0.7760 0.0019 0.0681 -0.0359 171 LEU A CA 1115 C C . LEU A 144 ? 0.6684 0.7354 0.7933 -0.0002 0.0692 -0.0364 171 LEU A C 1116 O O . LEU A 144 ? 0.7606 0.8233 0.8822 -0.0063 0.0647 -0.0358 171 LEU A O 1117 C CB . LEU A 144 ? 0.5834 0.6457 0.7223 0.0040 0.0664 -0.0364 171 LEU A CB 1118 C CG . LEU A 144 ? 0.4979 0.5689 0.6451 0.0098 0.0664 -0.0344 171 LEU A CG 1119 C CD1 . LEU A 144 ? 0.5544 0.6197 0.7062 0.0100 0.0632 -0.0322 171 LEU A CD1 1120 C CD2 . LEU A 144 ? 0.4805 0.5595 0.6318 0.0175 0.0735 -0.0320 171 LEU A CD2 1121 N N . PRO A 145 ? 0.6574 0.7256 0.7762 0.0064 0.0747 -0.0378 172 PRO A N 1122 C CA . PRO A 145 ? 0.6924 0.7565 0.7983 0.0081 0.0746 -0.0399 172 PRO A CA 1123 C C . PRO A 145 ? 0.7276 0.7734 0.8282 0.0062 0.0680 -0.0445 172 PRO A C 1124 O O . PRO A 145 ? 0.7415 0.7747 0.8482 0.0068 0.0647 -0.0471 172 PRO A O 1125 C CB . PRO A 145 ? 0.6602 0.7260 0.7602 0.0187 0.0796 -0.0429 172 PRO A CB 1126 C CG . PRO A 145 ? 0.6159 0.6767 0.7273 0.0203 0.0799 -0.0433 172 PRO A CG 1127 C CD . PRO A 145 ? 0.6266 0.6968 0.7486 0.0141 0.0795 -0.0388 172 PRO A CD 1128 N N . VAL A 146 ? 0.7252 0.7715 0.8163 0.0041 0.0660 -0.0441 173 VAL A N 1129 C CA . VAL A 146 ? 0.6567 0.6867 0.7408 0.0033 0.0592 -0.0491 173 VAL A CA 1130 C C . VAL A 146 ? 0.7563 0.7740 0.8318 0.0136 0.0568 -0.0573 173 VAL A C 1131 O O . VAL A 146 ? 0.8070 0.8333 0.8715 0.0231 0.0610 -0.0590 173 VAL A O 1132 C CB . VAL A 146 ? 0.6870 0.7234 0.7619 0.0003 0.0582 -0.0456 173 VAL A CB 1133 C CG1 . VAL A 146 ? 0.7395 0.7590 0.8051 0.0015 0.0508 -0.0523 173 VAL A CG1 1134 C CG2 . VAL A 146 ? 0.5841 0.6276 0.6709 -0.0107 0.0568 -0.0382 173 VAL A CG2 1135 N N . ASP A 147 ? 0.8566 0.8550 0.9374 0.0130 0.0489 -0.0622 174 ASP A N 1136 C CA . ASP A 147 ? 1.0042 0.9882 1.0774 0.0233 0.0429 -0.0712 174 ASP A CA 1137 C C . ASP A 147 ? 1.0608 1.0344 1.1181 0.0275 0.0349 -0.0787 174 ASP A C 1138 O O . ASP A 147 ? 1.0872 1.0499 1.1492 0.0203 0.0281 -0.0790 174 ASP A O 1139 C CB . ASP A 147 ? 1.1730 1.1411 1.2641 0.0215 0.0364 -0.0714 174 ASP A CB 1140 C CG . ASP A 147 ? 1.3126 1.2621 1.3988 0.0322 0.0267 -0.0814 174 ASP A CG 1141 O OD1 . ASP A 147 ? 1.3285 1.2833 1.4020 0.0434 0.0301 -0.0861 174 ASP A OD1 1142 O OD2 . ASP A 147 ? 1.3734 1.3029 1.4689 0.0300 0.0143 -0.0845 174 ASP A OD2 1143 N N . THR A 148 ? 1.2655 1.2441 1.3031 0.0408 0.0359 -0.0846 175 THR A N 1144 C CA . THR A 148 ? 1.4779 1.4479 1.4968 0.0493 0.0277 -0.0932 175 THR A CA 1145 C C . THR A 148 ? 1.7749 1.7326 1.7797 0.0673 0.0196 -0.1066 175 THR A C 1146 O O . THR A 148 ? 1.8214 1.7787 1.8040 0.0811 0.0148 -0.1148 175 THR A O 1147 C CB . THR A 148 ? 1.3904 1.3839 1.3941 0.0516 0.0361 -0.0865 175 THR A CB 1148 O OG1 . THR A 148 ? 1.3448 1.3591 1.3381 0.0634 0.0455 -0.0838 175 THR A OG1 1149 C CG2 . THR A 148 ? 1.3959 1.4005 1.4145 0.0345 0.0421 -0.0737 175 THR A CG2 1150 N N . SER A 149 ? 1.9603 1.9086 1.9775 0.0688 0.0176 -0.1086 176 SER A N 1151 C CA . SER A 149 ? 2.1010 2.0330 2.1082 0.0856 0.0069 -0.1221 176 SER A CA 1152 C C . SER A 149 ? 2.1528 2.0586 2.1545 0.0904 -0.0120 -0.1347 176 SER A C 1153 O O . SER A 149 ? 2.2085 2.1085 2.1866 0.1090 -0.0204 -0.1481 176 SER A O 1154 C CB . SER A 149 ? 2.1708 2.0930 2.1994 0.0823 0.0054 -0.1198 176 SER A CB 1155 O OG . SER A 149 ? 2.1921 2.1379 2.2286 0.0757 0.0220 -0.1075 176 SER A OG 1156 N N . ASN A 150 ? 2.1937 2.0851 2.2170 0.0747 -0.0190 -0.1303 177 ASN A N 1157 C CA . ASN A 150 ? 2.2529 2.1202 2.2752 0.0762 -0.0375 -0.1404 177 ASN A CA 1158 C C . ASN A 150 ? 2.2345 2.1126 2.2330 0.0806 -0.0350 -0.1432 177 ASN A C 1159 O O . ASN A 150 ? 2.2261 2.1139 2.2311 0.0667 -0.0282 -0.1333 177 ASN A O 1160 C CB . ASN A 150 ? 2.2572 2.1117 2.3115 0.0575 -0.0438 -0.1314 177 ASN A CB 1161 C CG . ASN A 150 ? 2.2184 2.0954 2.2848 0.0416 -0.0266 -0.1148 177 ASN A CG 1162 O OD1 . ASN A 150 ? 2.2188 2.1167 2.2805 0.0421 -0.0113 -0.1084 177 ASN A OD1 1163 N ND2 . ASN A 150 ? 2.2093 2.0818 2.2913 0.0286 -0.0304 -0.1083 177 ASN A ND2 1164 N N . ASN A 151 ? 2.2605 2.1379 2.2307 0.1017 -0.0409 -0.1565 178 ASN A N 1165 C CA . ASN A 151 ? 2.2836 2.1708 2.2293 0.1100 -0.0407 -0.1599 178 ASN A CA 1166 C C . ASN A 151 ? 2.3555 2.2224 2.3113 0.0993 -0.0545 -0.1628 178 ASN A C 1167 O O . ASN A 151 ? 2.3734 2.2510 2.3190 0.0965 -0.0506 -0.1590 178 ASN A O 1168 C CB . ASN A 151 ? 2.2676 2.1543 2.1811 0.1390 -0.0485 -0.1763 178 ASN A CB 1169 C CG . ASN A 151 ? 2.2827 2.1583 2.1757 0.1512 -0.0633 -0.1891 178 ASN A CG 1170 O OD1 . ASN A 151 ? 2.2980 2.1918 2.1808 0.1483 -0.0548 -0.1813 178 ASN A OD1 1171 N ND2 . ASN A 151 ? 2.2911 2.1362 2.1783 0.1657 -0.0868 -0.2091 178 ASN A ND2 1172 N N . ASN A 152 ? 2.3916 2.2307 2.3704 0.0924 -0.0704 -0.1676 179 ASN A N 1173 C CA . ASN A 152 ? 2.3824 2.2003 2.3754 0.0827 -0.0863 -0.1703 179 ASN A CA 1174 C C . ASN A 152 ? 2.2428 2.0684 2.2621 0.0587 -0.0770 -0.1529 179 ASN A C 1175 O O . ASN A 152 ? 2.2971 2.1056 2.3367 0.0485 -0.0898 -0.1519 179 ASN A O 1176 C CB . ASN A 152 ? 2.4818 2.2668 2.4918 0.0867 -0.1100 -0.1815 179 ASN A CB 1177 C CG . ASN A 152 ? 2.5487 2.3337 2.5752 0.0857 -0.1053 -0.1764 179 ASN A CG 1178 O OD1 . ASN A 152 ? 2.5710 2.3717 2.5790 0.0976 -0.0935 -0.1781 179 ASN A OD1 1179 N ND2 . ASN A 152 ? 2.5893 2.3590 2.6518 0.0716 -0.1140 -0.1681 179 ASN A ND2 1180 N N . GLY A 153 ? 2.0135 1.8652 2.0331 0.0507 -0.0562 -0.1393 180 GLY A N 1181 C CA . GLY A 153 ? 1.7486 1.6080 1.7918 0.0312 -0.0481 -0.1243 180 GLY A CA 1182 C C . GLY A 153 ? 1.5325 1.4089 1.5663 0.0241 -0.0380 -0.1169 180 GLY A C 1183 O O . GLY A 153 ? 1.5545 1.4380 1.5646 0.0330 -0.0369 -0.1216 180 GLY A O 1184 N N . ARG A 154 ? 1.3235 1.2070 1.3768 0.0089 -0.0315 -0.1047 181 ARG A N 1185 C CA . ARG A 154 ? 1.1366 1.0322 1.1864 0.0003 -0.0249 -0.0974 181 ARG A CA 1186 C C . ARG A 154 ? 1.0333 0.9518 1.0692 0.0028 -0.0106 -0.0916 181 ARG A C 1187 O O . ARG A 154 ? 0.9010 0.8287 0.9262 0.0012 -0.0078 -0.0883 181 ARG A O 1188 C CB . ARG A 154 ? 1.0473 0.9444 1.1214 -0.0134 -0.0231 -0.0870 181 ARG A CB 1189 C CG . ARG A 154 ? 1.0414 0.9357 1.1155 -0.0208 -0.0276 -0.0851 181 ARG A CG 1190 C CD . ARG A 154 ? 1.0589 0.9588 1.1546 -0.0312 -0.0247 -0.0745 181 ARG A CD 1191 N NE . ARG A 154 ? 1.0542 0.9666 1.1593 -0.0312 -0.0147 -0.0681 181 ARG A NE 1192 C CZ . ARG A 154 ? 1.0399 0.9674 1.1466 -0.0349 -0.0058 -0.0614 181 ARG A CZ 1193 N NH1 . ARG A 154 ? 1.0239 0.9550 1.1248 -0.0395 -0.0059 -0.0597 181 ARG A NH1 1194 N NH2 . ARG A 154 ? 1.0532 0.9913 1.1677 -0.0332 0.0018 -0.0570 181 ARG A NH2 1195 N N . ILE A 155 ? 1.0810 1.0097 1.1194 0.0062 -0.0022 -0.0890 182 ILE A N 1196 C CA . ILE A 155 ? 1.0941 1.0458 1.1234 0.0078 0.0103 -0.0817 182 ILE A CA 1197 C C . ILE A 155 ? 1.1426 1.1001 1.1528 0.0243 0.0121 -0.0881 182 ILE A C 1198 O O . ILE A 155 ? 1.1964 1.1465 1.2079 0.0318 0.0099 -0.0944 182 ILE A O 1199 C CB . ILE A 155 ? 1.0398 1.0026 1.0864 -0.0003 0.0191 -0.0727 182 ILE A CB 1200 C CG1 . ILE A 155 ? 0.8276 0.7876 0.8895 -0.0132 0.0172 -0.0669 182 ILE A CG1 1201 C CG2 . ILE A 155 ? 1.1311 1.1169 1.1715 0.0018 0.0300 -0.0651 182 ILE A CG2 1202 C CD1 . ILE A 155 ? 0.8114 0.7738 0.8918 -0.0174 0.0204 -0.0625 182 ILE A CD1 1203 N N . LYS A 156 ? 1.0816 1.0546 1.0745 0.0305 0.0162 -0.0850 183 LYS A N 1204 C CA . LYS A 156 ? 1.0456 1.0305 1.0157 0.0492 0.0188 -0.0892 183 LYS A CA 1205 C C . LYS A 156 ? 0.9343 0.9515 0.9014 0.0509 0.0333 -0.0747 183 LYS A C 1206 O O . LYS A 156 ? 0.7868 0.8164 0.7641 0.0384 0.0384 -0.0617 183 LYS A O 1207 C CB . LYS A 156 ? 1.1624 1.1397 1.1124 0.0599 0.0093 -0.0980 183 LYS A CB 1208 C CG . LYS A 156 ? 1.2201 1.1647 1.1749 0.0593 -0.0077 -0.1126 183 LYS A CG 1209 C CD . LYS A 156 ? 1.3294 1.2644 1.2603 0.0761 -0.0200 -0.1260 183 LYS A CD 1210 C CE . LYS A 156 ? 1.4084 1.3537 1.3315 0.0720 -0.0180 -0.1190 183 LYS A CE 1211 N NZ . LYS A 156 ? 1.4169 1.3537 1.3149 0.0904 -0.0305 -0.1329 183 LYS A NZ 1212 N N . GLN A 157 ? 1.0279 1.0588 0.9836 0.0658 0.0390 -0.0760 184 GLN A N 1213 C CA . GLN A 157 ? 1.1136 1.1788 1.0677 0.0685 0.0524 -0.0599 184 GLN A CA 1214 C C . GLN A 157 ? 1.1480 1.2296 1.0745 0.0902 0.0533 -0.0614 184 GLN A C 1215 O O . GLN A 157 ? 1.1779 1.2456 1.0847 0.1081 0.0451 -0.0781 184 GLN A O 1216 C CB . GLN A 157 ? 1.1526 1.2285 1.1151 0.0704 0.0603 -0.0569 184 GLN A CB 1217 C CG . GLN A 157 ? 1.1899 1.3035 1.1495 0.0770 0.0731 -0.0403 184 GLN A CG 1218 C CD . GLN A 157 ? 1.2449 1.3695 1.2146 0.0776 0.0807 -0.0367 184 GLN A CD 1219 O OE1 . GLN A 157 ? 1.2487 1.3638 1.2391 0.0625 0.0803 -0.0353 184 GLN A OE1 1220 N NE2 . GLN A 157 ? 1.2883 1.4347 1.2424 0.0968 0.0875 -0.0351 184 GLN A NE2 1221 N N . LEU A 158 ? 1.1732 1.2849 1.0989 0.0896 0.0624 -0.0432 185 LEU A N 1222 C CA . LEU A 158 ? 1.2289 1.3608 1.1282 0.1112 0.0643 -0.0419 185 LEU A CA 1223 C C . LEU A 158 ? 1.4644 1.6357 1.3575 0.1258 0.0779 -0.0275 185 LEU A C 1224 O O . LEU A 158 ? 1.4978 1.6846 1.4119 0.1141 0.0866 -0.0132 185 LEU A O 1225 C CB . LEU A 158 ? 1.0927 1.2323 0.9942 0.1026 0.0638 -0.0299 185 LEU A CB 1226 C CG . LEU A 158 ? 0.9566 1.0633 0.8714 0.0830 0.0527 -0.0377 185 LEU A CG 1227 C CD1 . LEU A 158 ? 0.9521 1.0688 0.8653 0.0782 0.0524 -0.0260 185 LEU A CD1 1228 C CD2 . LEU A 158 ? 0.8525 0.9236 0.7557 0.0905 0.0387 -0.0628 185 LEU A CD2 1229 N N . ARG A 159 ? 1.6457 1.8340 1.5092 0.1531 0.0789 -0.0316 186 ARG A N 1230 C CA . ARG A 159 ? 1.8086 2.0397 1.6626 0.1717 0.0925 -0.0168 186 ARG A CA 1231 C C . ARG A 159 ? 1.9291 2.2025 1.7915 0.1685 0.1042 0.0134 186 ARG A C 1232 O O . ARG A 159 ? 1.8603 2.1275 1.7353 0.1515 0.1011 0.0216 186 ARG A O 1233 C CB . ARG A 159 ? 1.9490 2.1808 1.7650 0.2069 0.0875 -0.0358 186 ARG A CB 1234 C CG . ARG A 159 ? 2.0272 2.2188 1.8377 0.2116 0.0746 -0.0637 186 ARG A CG 1235 C CD . ARG A 159 ? 2.0393 2.1875 1.8419 0.2099 0.0553 -0.0866 186 ARG A CD 1236 N NE . ARG A 159 ? 2.0631 2.1743 1.8623 0.2163 0.0409 -0.1113 186 ARG A NE 1237 C CZ . ARG A 159 ? 2.1137 2.2180 1.8841 0.2465 0.0310 -0.1308 186 ARG A CZ 1238 N NH1 . ARG A 159 ? 2.1340 2.2689 1.8736 0.2754 0.0354 -0.1291 186 ARG A NH1 1239 N NH2 . ARG A 159 ? 2.1260 2.1938 1.8993 0.2490 0.0160 -0.1515 186 ARG A NH2 1240 N N . SER A 160 ? 2.1569 2.4748 2.0132 0.1857 0.1174 0.0309 187 SER A N 1241 C CA . SER A 160 ? 2.2879 2.6519 2.1539 0.1853 0.1289 0.0635 187 SER A CA 1242 C C . SER A 160 ? 2.4748 2.8696 2.3088 0.2154 0.1328 0.0687 187 SER A C 1243 O O . SER A 160 ? 2.4460 2.8510 2.2858 0.2080 0.1331 0.0836 187 SER A O 1244 C CB . SER A 160 ? 2.2384 2.6409 2.1273 0.1814 0.1425 0.0885 187 SER A CB 1245 O OG . SER A 160 ? 2.2060 2.6351 2.1272 0.1611 0.1482 0.1210 187 SER A OG 1246 N N . GLU A 161 ? 2.7187 3.1295 2.5185 0.2502 0.1352 0.0573 188 GLU A N 1247 C CA . GLU A 161 ? 2.7922 3.1879 2.5796 0.2636 0.1325 0.0361 188 GLU A CA 1248 C C . GLU A 161 ? 2.8056 3.2488 2.6014 0.2732 0.1490 0.0589 188 GLU A C 1249 O O . GLU A 161 ? 2.8445 3.2762 2.6531 0.2653 0.1497 0.0528 188 GLU A O 1250 C CB . GLU A 161 ? 2.8722 3.2515 2.6145 0.2989 0.1210 0.0057 188 GLU A CB 1251 C CG . GLU A 161 ? 2.9288 3.2608 2.6636 0.3015 0.1068 -0.0273 188 GLU A CG 1252 C CD . GLU A 161 ? 2.9501 3.2287 2.6793 0.2934 0.0864 -0.0543 188 GLU A CD 1253 O OE1 . GLU A 161 ? 2.9630 3.2392 2.6973 0.2812 0.0843 -0.0470 188 GLU A OE1 1254 O OE2 . GLU A 161 ? 2.9784 3.2179 2.7004 0.2986 0.0720 -0.0814 188 GLU A OE2 1255 N N . SER A 162 ? 2.7262 3.2250 2.5159 0.2907 0.1624 0.0867 189 SER A N 1256 C CA . SER A 162 ? 2.6571 3.2076 2.4520 0.3050 0.1786 0.1099 189 SER A CA 1257 C C . SER A 162 ? 2.8132 3.4148 2.6439 0.2888 0.1929 0.1557 189 SER A C 1258 O O . SER A 162 ? 2.9099 3.5514 2.7320 0.3037 0.2003 0.1773 189 SER A O 1259 C CB . SER A 162 ? 2.4765 3.0553 2.2244 0.3530 0.1820 0.1000 189 SER A CB 1260 O OG . SER A 162 ? 2.4066 3.0375 2.1584 0.3689 0.1982 0.1227 189 SER A OG 1261 N N . ILE A 163 ? 2.7651 3.3656 2.6373 0.2588 0.1956 0.1709 190 ILE A N 1262 C CA . ILE A 163 ? 2.7800 3.4245 2.6942 0.2396 0.2057 0.2146 190 ILE A CA 1263 C C . ILE A 163 ? 2.7353 3.4062 2.6724 0.2364 0.2147 0.2297 190 ILE A C 1264 O O . ILE A 163 ? 2.7111 3.3462 2.6498 0.2278 0.2086 0.2063 190 ILE A O 1265 C CB . ILE A 163 ? 2.8307 3.4414 2.7815 0.1993 0.1949 0.2193 190 ILE A CB 1266 C CG1 . ILE A 163 ? 2.8089 3.3670 2.7354 0.1973 0.1808 0.1867 190 ILE A CG1 1267 C CG2 . ILE A 163 ? 2.8396 3.4943 2.8226 0.1875 0.2015 0.2627 190 ILE A CG2 1268 C CD1 . ILE A 163 ? 2.8065 3.3842 2.7109 0.2146 0.1825 0.1948 190 ILE A CD1 1269 N N . GLY A 164 ? 2.6462 3.3805 2.6025 0.2435 0.2292 0.2698 191 GLY A N 1270 C CA . GLY A 164 ? 2.5138 3.2958 2.4714 0.2541 0.2376 0.3021 191 GLY A CA 1271 C C . GLY A 164 ? 2.3137 3.1387 2.3275 0.2293 0.2441 0.3504 191 GLY A C 1272 O O . GLY A 164 ? 2.2787 3.1018 2.3260 0.2093 0.2431 0.3581 191 GLY A O 1273 N N . GLY A 165 ? 2.1756 3.0391 2.2013 0.2306 0.2496 0.3837 192 GLY A N 1274 C CA . GLY A 165 ? 2.1218 3.0270 2.2050 0.2066 0.2536 0.4330 192 GLY A CA 1275 C C . GLY A 165 ? 2.0837 2.9402 2.2083 0.1627 0.2361 0.4302 192 GLY A C 1276 O O . GLY A 165 ? 2.0572 2.9358 2.2348 0.1375 0.2337 0.4667 192 GLY A O 1277 N N . THR A 166 ? 2.0600 2.8504 2.1606 0.1547 0.2227 0.3867 193 THR A N 1278 C CA . THR A 166 ? 1.9923 2.7303 2.1236 0.1175 0.2052 0.3756 193 THR A CA 1279 C C . THR A 166 ? 1.9808 2.6661 2.0949 0.1137 0.1974 0.3329 193 THR A C 1280 O O . THR A 166 ? 1.9974 2.6905 2.0823 0.1376 0.2054 0.3173 193 THR A O 1281 C CB . THR A 166 ? 1.9486 2.6599 2.0701 0.1104 0.1964 0.3684 193 THR A CB 1282 O OG1 . THR A 166 ? 1.9671 2.6695 2.0333 0.1409 0.2003 0.3410 193 THR A OG1 1283 C CG2 . THR A 166 ? 1.9180 2.6760 2.0733 0.1029 0.2004 0.4158 193 THR A CG2 1284 N N . PRO A 167 ? 1.9555 2.5892 2.0888 0.0849 0.1816 0.3153 194 PRO A N 1285 C CA . PRO A 167 ? 1.8689 2.4548 1.9830 0.0843 0.1751 0.2755 194 PRO A CA 1286 C C . PRO A 167 ? 1.7255 2.2746 1.7914 0.1021 0.1719 0.2379 194 PRO A C 1287 O O . PRO A 167 ? 1.6294 2.1785 1.6768 0.1104 0.1711 0.2373 194 PRO A O 1288 C CB . PRO A 167 ? 1.8315 2.3795 1.9820 0.0501 0.1593 0.2718 194 PRO A CB 1289 C CG . PRO A 167 ? 1.8284 2.3898 2.0050 0.0354 0.1544 0.2992 194 PRO A CG 1290 C CD . PRO A 167 ? 1.9189 2.5441 2.1008 0.0520 0.1696 0.3360 194 PRO A CD 1291 N N . ILE A 168 ? 1.6913 2.2099 1.7390 0.1079 0.1694 0.2075 195 ILE A N 1292 C CA . ILE A 168 ? 1.6971 2.1703 1.7087 0.1183 0.1617 0.1691 195 ILE A CA 1293 C C . ILE A 168 ? 1.7100 2.1349 1.7312 0.0946 0.1474 0.1531 195 ILE A C 1294 O O . ILE A 168 ? 1.7161 2.1244 1.7682 0.0698 0.1408 0.1560 195 ILE A O 1295 C CB . ILE A 168 ? 0.8571 1.3111 0.8562 0.1267 0.1618 0.1451 195 ILE A CB 1296 C CG1 . ILE A 168 ? 1.0141 1.5087 0.9921 0.1570 0.1746 0.1517 195 ILE A CG1 1297 C CG2 . ILE A 168 ? 0.7730 1.1744 0.7466 0.1299 0.1504 0.1078 195 ILE A CG2 1298 C CD1 . ILE A 168 ? 1.0292 1.5017 0.9917 0.1675 0.1732 0.1261 195 ILE A CD1 1299 N N . ARG A 169 ? 1.7156 2.1201 1.7107 0.1032 0.1419 0.1370 196 ARG A N 1300 C CA . ARG A 169 ? 1.7156 2.0791 1.7198 0.0821 0.1291 0.1247 196 ARG A CA 1301 C C . ARG A 169 ? 1.6249 1.9423 1.6150 0.0819 0.1205 0.0907 196 ARG A C 1302 O O . ARG A 169 ? 1.6211 1.9288 1.5799 0.1033 0.1198 0.0707 196 ARG A O 1303 C CB . ARG A 169 ? 1.8255 2.1904 1.8121 0.0896 0.1267 0.1263 196 ARG A CB 1304 C CG . ARG A 169 ? 1.8779 2.2767 1.8876 0.0802 0.1307 0.1606 196 ARG A CG 1305 C CD . ARG A 169 ? 1.9490 2.4028 1.9466 0.1046 0.1449 0.1843 196 ARG A CD 1306 N NE . ARG A 169 ? 2.0015 2.4842 2.0142 0.0993 0.1473 0.2146 196 ARG A NE 1307 C CZ . ARG A 169 ? 1.9924 2.4912 2.0484 0.0757 0.1462 0.2446 196 ARG A CZ 1308 N NH1 . ARG A 169 ? 1.9581 2.4464 2.0449 0.0560 0.1420 0.2467 196 ARG A NH1 1309 N NH2 . ARG A 169 ? 1.9858 2.5105 2.0553 0.0722 0.1477 0.2726 196 ARG A NH2 1310 N N . GLY A 170 ? 1.6171 1.9062 1.6300 0.0593 0.1128 0.0842 197 GLY A N 1311 C CA . GLY A 170 ? 1.5229 1.7695 1.5258 0.0573 0.1040 0.0557 197 GLY A CA 1312 C C . GLY A 170 ? 1.4622 1.6795 1.4714 0.0414 0.0933 0.0490 197 GLY A C 1313 O O . GLY A 170 ? 1.4937 1.7153 1.5268 0.0236 0.0905 0.0641 197 GLY A O 1314 N N . ALA A 171 ? 1.2754 1.4627 1.2655 0.0475 0.0858 0.0267 198 ALA A N 1315 C CA . ALA A 171 ? 1.0426 1.2022 1.0395 0.0327 0.0756 0.0199 198 ALA A CA 1316 C C . ALA A 171 ? 0.9200 1.0449 0.9182 0.0281 0.0681 -0.0011 198 ALA A C 1317 O O . ALA A 171 ? 1.0611 1.1750 1.0427 0.0420 0.0666 -0.0165 198 ALA A O 1318 C CB . ALA A 171 ? 1.0648 1.2244 1.0407 0.0430 0.0725 0.0174 198 ALA A CB 1319 N N . LEU A 172 ? 0.7743 0.8831 0.7927 0.0101 0.0626 -0.0011 199 LEU A N 1320 C CA . LEU A 172 ? 0.8046 0.8830 0.8253 0.0057 0.0552 -0.0179 199 LEU A CA 1321 C C . LEU A 172 ? 0.8417 0.9001 0.8602 -0.0006 0.0460 -0.0239 199 LEU A C 1322 O O . LEU A 172 ? 0.9118 0.9678 0.9443 -0.0139 0.0426 -0.0168 199 LEU A O 1323 C CB . LEU A 172 ? 0.8018 0.8773 0.8444 -0.0062 0.0554 -0.0154 199 LEU A CB 1324 C CG . LEU A 172 ? 0.8176 0.8690 0.8629 -0.0070 0.0506 -0.0298 199 LEU A CG 1325 C CD1 . LEU A 172 ? 0.8339 0.8816 0.8655 0.0075 0.0527 -0.0399 199 LEU A CD1 1326 C CD2 . LEU A 172 ? 0.8371 0.8882 0.9019 -0.0163 0.0508 -0.0271 199 LEU A CD2 1327 N N . GLN A 173 ? 0.8570 0.8998 0.8587 0.0095 0.0405 -0.0375 200 GLN A N 1328 C CA . GLN A 173 ? 0.9453 0.9702 0.9432 0.0055 0.0314 -0.0435 200 GLN A CA 1329 C C . GLN A 173 ? 0.8898 0.8880 0.8979 -0.0013 0.0229 -0.0548 200 GLN A C 1330 O O . GLN A 173 ? 0.9167 0.9012 0.9205 0.0065 0.0185 -0.0663 200 GLN A O 1331 C CB . GLN A 173 ? 1.1198 1.1456 1.0930 0.0219 0.0283 -0.0506 200 GLN A CB 1332 C CG . GLN A 173 ? 1.1215 1.1339 1.0904 0.0178 0.0196 -0.0539 200 GLN A CG 1333 C CD . GLN A 173 ? 1.0902 1.1002 1.0334 0.0360 0.0139 -0.0641 200 GLN A CD 1334 O OE1 . GLN A 173 ? 1.1848 1.1748 1.1203 0.0449 0.0046 -0.0806 200 GLN A OE1 1335 N NE2 . GLN A 173 ? 1.0147 1.0457 0.9452 0.0426 0.0184 -0.0540 200 GLN A NE2 1336 N N . ILE A 174 ? 0.8162 0.8085 0.8392 -0.0150 0.0199 -0.0503 201 ILE A N 1337 C CA . ILE A 174 ? 0.9043 0.8778 0.9399 -0.0217 0.0135 -0.0566 201 ILE A CA 1338 C C . ILE A 174 ? 0.9737 0.9327 1.0060 -0.0245 0.0043 -0.0610 201 ILE A C 1339 O O . ILE A 174 ? 0.9358 0.8964 0.9728 -0.0329 0.0028 -0.0550 201 ILE A O 1340 C CB . ILE A 174 ? 0.8482 0.8263 0.9021 -0.0323 0.0159 -0.0495 201 ILE A CB 1341 C CG1 . ILE A 174 ? 0.9432 0.9368 1.0018 -0.0304 0.0241 -0.0443 201 ILE A CG1 1342 C CG2 . ILE A 174 ? 0.7230 0.6872 0.7893 -0.0358 0.0110 -0.0540 201 ILE A CG2 1343 C CD1 . ILE A 174 ? 0.9515 0.9489 1.0267 -0.0383 0.0242 -0.0394 201 ILE A CD1 1344 N N . GLU A 175 ? 0.9890 0.9328 1.0144 -0.0175 -0.0034 -0.0716 202 GLU A N 1345 C CA . GLU A 175 ? 1.0399 0.9693 1.0635 -0.0201 -0.0136 -0.0762 202 GLU A CA 1346 C C . GLU A 175 ? 1.0582 0.9777 1.1029 -0.0304 -0.0177 -0.0743 202 GLU A C 1347 O O . GLU A 175 ? 1.1125 1.0327 1.1708 -0.0319 -0.0147 -0.0726 202 GLU A O 1348 C CB . GLU A 175 ? 1.1902 1.1060 1.2002 -0.0080 -0.0233 -0.0889 202 GLU A CB 1349 C CG . GLU A 175 ? 1.2785 1.2064 1.2642 0.0070 -0.0197 -0.0917 202 GLU A CG 1350 C CD . GLU A 175 ? 1.3901 1.3021 1.3615 0.0222 -0.0318 -0.1075 202 GLU A CD 1351 O OE1 . GLU A 175 ? 1.4860 1.3855 1.4661 0.0249 -0.0368 -0.1142 202 GLU A OE1 1352 O OE2 . GLU A 175 ? 1.3675 1.2791 1.3193 0.0325 -0.0375 -0.1132 202 GLU A OE2 1353 N N . GLN A 176 ? 1.0033 0.9162 1.0503 -0.0362 -0.0239 -0.0737 203 GLN A N 1354 C CA . GLN A 176 ? 0.9831 0.8889 1.0489 -0.0438 -0.0286 -0.0712 203 GLN A CA 1355 C C . GLN A 176 ? 0.8801 0.7970 0.9597 -0.0482 -0.0209 -0.0635 203 GLN A C 1356 O O . GLN A 176 ? 0.8526 0.7687 0.9477 -0.0487 -0.0209 -0.0613 203 GLN A O 1357 C CB . GLN A 176 ? 1.0926 0.9836 1.1683 -0.0411 -0.0379 -0.0769 203 GLN A CB 1358 C CG . GLN A 176 ? 1.1898 1.0659 1.2567 -0.0379 -0.0504 -0.0853 203 GLN A CG 1359 C CD . GLN A 176 ? 1.2336 1.1087 1.3039 -0.0452 -0.0542 -0.0816 203 GLN A CD 1360 O OE1 . GLN A 176 ? 1.2974 1.1690 1.3522 -0.0427 -0.0588 -0.0860 203 GLN A OE1 1361 N NE2 . GLN A 176 ? 1.1743 1.0538 1.2639 -0.0527 -0.0524 -0.0732 203 GLN A NE2 1362 N N . SER A 177 ? 0.8282 0.7559 0.9031 -0.0509 -0.0154 -0.0587 204 SER A N 1363 C CA . SER A 177 ? 0.8194 0.7575 0.9043 -0.0531 -0.0100 -0.0533 204 SER A CA 1364 C C . SER A 177 ? 0.8461 0.7835 0.9454 -0.0550 -0.0126 -0.0509 204 SER A C 1365 O O . SER A 177 ? 0.9507 0.8818 1.0521 -0.0575 -0.0187 -0.0510 204 SER A O 1366 C CB . SER A 177 ? 0.8706 0.8167 0.9509 -0.0569 -0.0087 -0.0485 204 SER A CB 1367 O OG . SER A 177 ? 1.0076 0.9598 1.0762 -0.0543 -0.0050 -0.0471 204 SER A OG 1368 N N . GLU A 178 ? 0.8262 0.7722 0.9349 -0.0523 -0.0079 -0.0481 205 GLU A N 1369 C CA . GLU A 178 ? 0.8934 0.8444 1.0147 -0.0508 -0.0090 -0.0441 205 GLU A CA 1370 C C . GLU A 178 ? 0.9098 0.8722 1.0328 -0.0472 -0.0055 -0.0427 205 GLU A C 1371 O O . GLU A 178 ? 0.9114 0.8771 1.0293 -0.0475 -0.0024 -0.0440 205 GLU A O 1372 C CB . GLU A 178 ? 0.9285 0.8793 1.0633 -0.0483 -0.0083 -0.0408 205 GLU A CB 1373 C CG . GLU A 178 ? 0.9273 0.8789 1.0625 -0.0452 -0.0032 -0.0421 205 GLU A CG 1374 C CD . GLU A 178 ? 0.9891 0.9331 1.1372 -0.0447 -0.0070 -0.0401 205 GLU A CD 1375 O OE1 . GLU A 178 ? 1.0299 0.9603 1.1711 -0.0451 -0.0125 -0.0468 205 GLU A OE1 1376 O OE2 . GLU A 178 ? 1.0071 0.9594 1.1731 -0.0430 -0.0056 -0.0315 205 GLU A OE2 1377 N N . GLU A 179 ? 0.8936 0.8633 1.0237 -0.0426 -0.0070 -0.0399 206 GLU A N 1378 C CA . GLU A 179 ? 0.9225 0.9017 1.0524 -0.0367 -0.0070 -0.0409 206 GLU A CA 1379 C C . GLU A 179 ? 0.8701 0.8569 1.0018 -0.0334 -0.0002 -0.0406 206 GLU A C 1380 O O . GLU A 179 ? 0.8510 0.8410 0.9799 -0.0322 -0.0013 -0.0432 206 GLU A O 1381 C CB . GLU A 179 ? 1.1236 1.1129 1.2595 -0.0278 -0.0088 -0.0378 206 GLU A CB 1382 C CG . GLU A 179 ? 1.3140 1.3196 1.4551 -0.0164 -0.0037 -0.0351 206 GLU A CG 1383 C CD . GLU A 179 ? 1.4921 1.5111 1.6358 -0.0043 -0.0059 -0.0320 206 GLU A CD 1384 O OE1 . GLU A 179 ? 1.5562 1.5698 1.6934 -0.0032 -0.0139 -0.0365 206 GLU A OE1 1385 O OE2 . GLU A 179 ? 1.5312 1.5674 1.6833 0.0053 0.0003 -0.0243 206 GLU A OE2 1386 N N . SER A 180 ? 0.9106 0.8999 1.0491 -0.0319 0.0055 -0.0370 207 SER A N 1387 C CA . SER A 180 ? 0.8543 0.8508 0.9950 -0.0281 0.0123 -0.0363 207 SER A CA 1388 C C . SER A 180 ? 0.7118 0.7038 0.8435 -0.0327 0.0139 -0.0404 207 SER A C 1389 O O . SER A 180 ? 0.7218 0.7213 0.8540 -0.0296 0.0185 -0.0405 207 SER A O 1390 C CB . SER A 180 ? 0.9797 0.9771 1.1315 -0.0264 0.0161 -0.0308 207 SER A CB 1391 O OG . SER A 180 ? 1.0140 0.9966 1.1640 -0.0327 0.0122 -0.0330 207 SER A OG 1392 N N . ASP A 181 ? 0.7748 0.7569 0.8987 -0.0391 0.0104 -0.0426 208 ASP A N 1393 C CA . ASP A 181 ? 0.8643 0.8466 0.9797 -0.0422 0.0123 -0.0436 208 ASP A CA 1394 C C . ASP A 181 ? 0.8078 0.7962 0.9243 -0.0446 0.0094 -0.0421 208 ASP A C 1395 O O . ASP A 181 ? 0.7156 0.7098 0.8304 -0.0466 0.0118 -0.0397 208 ASP A O 1396 C CB . ASP A 181 ? 0.8469 0.8196 0.9530 -0.0458 0.0095 -0.0453 208 ASP A CB 1397 C CG . ASP A 181 ? 0.8670 0.8324 0.9712 -0.0423 0.0106 -0.0485 208 ASP A CG 1398 O OD1 . ASP A 181 ? 0.8587 0.8279 0.9671 -0.0378 0.0152 -0.0486 208 ASP A OD1 1399 O OD2 . ASP A 181 ? 0.8705 0.8254 0.9697 -0.0435 0.0053 -0.0515 208 ASP A OD2 1400 N N . GLN A 182 ? 0.8396 0.8269 0.9602 -0.0437 0.0029 -0.0431 209 GLN A N 1401 C CA . GLN A 182 ? 0.7865 0.7761 0.9106 -0.0450 -0.0041 -0.0432 209 GLN A CA 1402 C C . GLN A 182 ? 0.6792 0.6789 0.8080 -0.0406 -0.0005 -0.0431 209 GLN A C 1403 O O . GLN A 182 ? 0.6470 0.6525 0.7770 -0.0335 0.0055 -0.0441 209 GLN A O 1404 C CB . GLN A 182 ? 0.7672 0.7533 0.8929 -0.0407 -0.0127 -0.0466 209 GLN A CB 1405 C CG . GLN A 182 ? 0.8239 0.8037 0.9517 -0.0445 -0.0250 -0.0476 209 GLN A CG 1406 C CD . GLN A 182 ? 0.8872 0.8618 1.0132 -0.0388 -0.0336 -0.0520 209 GLN A CD 1407 O OE1 . GLN A 182 ? 0.8636 0.8288 0.9890 -0.0438 -0.0426 -0.0521 209 GLN A OE1 1408 N NE2 . GLN A 182 ? 0.9853 0.9677 1.1106 -0.0274 -0.0307 -0.0545 209 GLN A NE2 1409 N N . GLY A 183 ? 0.6394 0.6425 0.7728 -0.0451 -0.0044 -0.0405 210 GLY A N 1410 C CA . GLY A 183 ? 0.6411 0.6540 0.7802 -0.0408 -0.0024 -0.0408 210 GLY A CA 1411 C C . GLY A 183 ? 0.7500 0.7697 0.8958 -0.0477 -0.0029 -0.0340 210 GLY A C 1412 O O . GLY A 183 ? 0.7888 0.8066 0.9367 -0.0559 -0.0066 -0.0278 210 GLY A O 1413 N N . LYS A 184 ? 0.7752 0.8049 0.9258 -0.0441 0.0006 -0.0335 211 LYS A N 1414 C CA . LYS A 184 ? 0.7984 0.8376 0.9596 -0.0502 -0.0014 -0.0255 211 LYS A CA 1415 C C . LYS A 184 ? 0.7399 0.7908 0.8959 -0.0498 0.0125 -0.0195 211 LYS A C 1416 O O . LYS A 184 ? 0.7374 0.7932 0.8891 -0.0426 0.0208 -0.0231 211 LYS A O 1417 C CB . LYS A 184 ? 0.9424 0.9855 1.1143 -0.0460 -0.0096 -0.0292 211 LYS A CB 1418 C CG . LYS A 184 ? 1.1484 1.2000 1.3376 -0.0538 -0.0166 -0.0199 211 LYS A CG 1419 C CD . LYS A 184 ? 1.2626 1.3111 1.4631 -0.0495 -0.0319 -0.0267 211 LYS A CD 1420 C CE . LYS A 184 ? 1.3429 1.3750 1.5412 -0.0463 -0.0469 -0.0360 211 LYS A CE 1421 N NZ . LYS A 184 ? 1.3961 1.4236 1.6020 -0.0383 -0.0643 -0.0458 211 LYS A NZ 1422 N N . TYR A 185 ? 0.6172 0.6732 0.7723 -0.0557 0.0149 -0.0103 212 TYR A N 1423 C CA . TYR A 185 ? 0.6192 0.6871 0.7655 -0.0520 0.0275 -0.0057 212 TYR A CA 1424 C C . TYR A 185 ? 0.6149 0.7030 0.7739 -0.0550 0.0295 0.0072 212 TYR A C 1425 O O . TYR A 185 ? 0.6175 0.7103 0.7923 -0.0636 0.0208 0.0174 212 TYR A O 1426 C CB . TYR A 185 ? 0.5242 0.5882 0.6577 -0.0524 0.0303 -0.0039 212 TYR A CB 1427 C CG . TYR A 185 ? 0.5653 0.6119 0.6863 -0.0483 0.0303 -0.0156 212 TYR A CG 1428 C CD1 . TYR A 185 ? 0.6038 0.6366 0.7279 -0.0516 0.0217 -0.0206 212 TYR A CD1 1429 C CD2 . TYR A 185 ? 0.6430 0.6872 0.7505 -0.0404 0.0377 -0.0210 212 TYR A CD2 1430 C CE1 . TYR A 185 ? 0.7462 0.7661 0.8623 -0.0484 0.0217 -0.0285 212 TYR A CE1 1431 C CE2 . TYR A 185 ? 0.7425 0.7708 0.8435 -0.0379 0.0356 -0.0298 212 TYR A CE2 1432 C CZ . TYR A 185 ? 0.8050 0.8226 0.9113 -0.0425 0.0282 -0.0323 212 TYR A CZ 1433 O OH . TYR A 185 ? 0.7940 0.7987 0.8973 -0.0405 0.0261 -0.0384 212 TYR A OH 1434 N N . GLU A 186 ? 0.5760 0.6764 0.7297 -0.0479 0.0401 0.0080 213 GLU A N 1435 C CA . GLU A 186 ? 0.6643 0.7880 0.8290 -0.0492 0.0442 0.0219 213 GLU A CA 1436 C C . GLU A 186 ? 0.6523 0.7884 0.7998 -0.0393 0.0576 0.0239 213 GLU A C 1437 O O . GLU A 186 ? 0.5561 0.6824 0.6879 -0.0302 0.0630 0.0118 213 GLU A O 1438 C CB . GLU A 186 ? 0.8020 0.9318 0.9810 -0.0490 0.0415 0.0211 213 GLU A CB 1439 C CG . GLU A 186 ? 0.8649 0.9854 1.0342 -0.0401 0.0455 0.0067 213 GLU A CG 1440 C CD . GLU A 186 ? 0.8545 0.9799 1.0389 -0.0402 0.0395 0.0056 213 GLU A CD 1441 O OE1 . GLU A 186 ? 0.9074 1.0257 1.0866 -0.0331 0.0404 -0.0052 213 GLU A OE1 1442 O OE2 . GLU A 186 ? 0.7225 0.8598 0.9255 -0.0472 0.0330 0.0166 213 GLU A OE2 1443 N N . CYS A 187 ? 0.6979 0.8557 0.8489 -0.0398 0.0618 0.0399 214 CYS A N 1444 C CA . CYS A 187 ? 0.7481 0.9234 0.8828 -0.0269 0.0743 0.0429 214 CYS A CA 1445 C C . CYS A 187 ? 0.7347 0.9345 0.8802 -0.0236 0.0809 0.0528 214 CYS A C 1446 O O . CYS A 187 ? 0.6399 0.8534 0.8098 -0.0332 0.0763 0.0667 214 CYS A O 1447 C CB . CYS A 187 ? 0.8119 1.0013 0.9394 -0.0248 0.0772 0.0551 214 CYS A CB 1448 S SG . CYS A 187 ? 1.0704 1.3033 1.2147 -0.0246 0.0845 0.0839 214 CYS A SG 1449 N N . VAL A 188 ? 0.7521 0.9556 0.8798 -0.0094 0.0902 0.0448 215 VAL A N 1450 C CA . VAL A 188 ? 0.6902 0.9133 0.8233 -0.0033 0.0974 0.0496 215 VAL A CA 1451 C C . VAL A 188 ? 0.7364 0.9839 0.8523 0.0129 0.1090 0.0563 215 VAL A C 1452 O O . VAL A 188 ? 0.8237 1.0604 0.9147 0.0254 0.1115 0.0440 215 VAL A O 1453 C CB . VAL A 188 ? 0.6113 0.8149 0.7386 0.0011 0.0972 0.0319 215 VAL A CB 1454 C CG1 . VAL A 188 ? 0.5506 0.7739 0.6790 0.0101 0.1057 0.0355 215 VAL A CG1 1455 C CG2 . VAL A 188 ? 0.7296 0.9157 0.8733 -0.0110 0.0867 0.0267 215 VAL A CG2 1456 N N . ALA A 189 ? 0.7022 0.9836 0.8322 0.0135 0.1149 0.0761 216 ALA A N 1457 C CA . ALA A 189 ? 0.7551 1.0657 0.8688 0.0316 0.1269 0.0845 216 ALA A CA 1458 C C . ALA A 189 ? 0.8523 1.1783 0.9668 0.0411 0.1343 0.0843 216 ALA A C 1459 O O . ALA A 189 ? 0.8841 1.2226 1.0241 0.0309 0.1330 0.0952 216 ALA A O 1460 C CB . ALA A 189 ? 0.7770 1.1220 0.9054 0.0280 0.1300 0.1118 216 ALA A CB 1461 N N . THR A 190 ? 0.8571 1.1817 0.9438 0.0613 0.1408 0.0714 217 THR A N 1462 C CA . THR A 190 ? 0.8464 1.1807 0.9296 0.0725 0.1474 0.0675 217 THR A CA 1463 C C . THR A 190 ? 0.9304 1.2934 0.9907 0.0974 0.1581 0.0718 217 THR A C 1464 O O . THR A 190 ? 0.9781 1.3343 1.0119 0.1122 0.1578 0.0622 217 THR A O 1465 C CB . THR A 190 ? 0.8497 1.1462 0.9229 0.0737 0.1419 0.0428 217 THR A CB 1466 O OG1 . THR A 190 ? 0.8599 1.1327 0.9512 0.0540 0.1324 0.0389 217 THR A OG1 1467 C CG2 . THR A 190 ? 0.8629 1.1688 0.9380 0.0819 0.1477 0.0406 217 THR A CG2 1468 N N . ASN A 191 ? 0.9465 1.3426 1.0172 0.1029 0.1667 0.0864 218 ASN A N 1469 C CA . ASN A 191 ? 0.9047 1.3262 0.9519 0.1297 0.1768 0.0867 218 ASN A CA 1470 C C . ASN A 191 ? 0.9833 1.4132 1.0377 0.1338 0.1815 0.0854 218 ASN A C 1471 O O . ASN A 191 ? 0.9808 1.3919 1.0546 0.1173 0.1761 0.0805 218 ASN A O 1472 C CB . ASN A 191 ? 0.7823 1.2525 0.8319 0.1386 0.1863 0.1139 218 ASN A CB 1473 C CG . ASN A 191 ? 0.7704 1.2748 0.8600 0.1212 0.1896 0.1439 218 ASN A CG 1474 O OD1 . ASN A 191 ? 0.6047 1.1055 0.7143 0.1106 0.1877 0.1437 218 ASN A OD1 1475 N ND2 . ASN A 191 ? 0.8106 1.3495 0.9135 0.1186 0.1935 0.1709 218 ASN A ND2 1476 N N . SER A 192 ? 1.1175 1.5767 1.1548 0.1578 0.1914 0.0893 219 SER A N 1477 C CA . SER A 192 ? 1.2001 1.6680 1.2403 0.1651 0.1963 0.0869 219 SER A CA 1478 C C . SER A 192 ? 1.1513 1.6452 1.2299 0.1463 0.1989 0.1098 219 SER A C 1479 O O . SER A 192 ? 1.1329 1.6266 1.2199 0.1459 0.2002 0.1063 219 SER A O 1480 C CB . SER A 192 ? 1.2706 1.7679 1.2828 0.1974 0.2062 0.0875 219 SER A CB 1481 O OG . SER A 192 ? 1.3391 1.8843 1.3551 0.2047 0.2154 0.1141 219 SER A OG 1482 N N . ALA A 193 ? 1.0424 1.5577 1.1456 0.1309 0.1981 0.1332 220 ALA A N 1483 C CA . ALA A 193 ? 0.8939 1.4301 1.0378 0.1110 0.1962 0.1550 220 ALA A CA 1484 C C . ALA A 193 ? 0.9017 1.3988 1.0653 0.0867 0.1822 0.1428 220 ALA A C 1485 O O . ALA A 193 ? 0.9651 1.4665 1.1546 0.0750 0.1781 0.1485 220 ALA A O 1486 C CB . ALA A 193 ? 0.7739 1.3511 0.9404 0.1048 0.1994 0.1879 220 ALA A CB 1487 N N . GLY A 194 ? 0.8476 1.3078 0.9984 0.0807 0.1742 0.1260 221 GLY A N 1488 C CA . GLY A 194 ? 0.8025 1.2277 0.9689 0.0608 0.1612 0.1144 221 GLY A CA 1489 C C . GLY A 194 ? 0.8711 1.2678 1.0318 0.0511 0.1526 0.1061 221 GLY A C 1490 O O . GLY A 194 ? 0.9463 1.3425 1.0853 0.0611 0.1562 0.1038 221 GLY A O 1491 N N . THR A 195 ? 0.8896 1.2630 1.0692 0.0330 0.1404 0.1012 222 THR A N 1492 C CA . THR A 195 ? 0.8425 1.1836 1.0160 0.0241 0.1311 0.0892 222 THR A CA 1493 C C . THR A 195 ? 0.7744 1.1163 0.9783 0.0041 0.1190 0.1027 222 THR A C 1494 O O . THR A 195 ? 0.7468 1.0948 0.9763 -0.0054 0.1121 0.1092 222 THR A O 1495 C CB . THR A 195 ? 0.8568 1.1622 1.0183 0.0254 0.1267 0.0647 222 THR A CB 1496 O OG1 . THR A 195 ? 0.9008 1.2039 1.0377 0.0433 0.1357 0.0531 222 THR A OG1 1497 C CG2 . THR A 195 ? 0.8055 1.0807 0.9599 0.0181 0.1183 0.0535 222 THR A CG2 1498 N N . ARG A 196 ? 0.8663 1.2009 1.0677 -0.0015 0.1149 0.1063 223 ARG A N 1499 C CA . ARG A 196 ? 0.8698 1.2000 1.0988 -0.0201 0.1012 0.1173 223 ARG A CA 1500 C C . ARG A 196 ? 0.9509 1.2469 1.1683 -0.0257 0.0926 0.1020 223 ARG A C 1501 O O . ARG A 196 ? 1.0073 1.2955 1.1997 -0.0171 0.0986 0.0944 223 ARG A O 1502 C CB . ARG A 196 ? 0.8483 1.2142 1.0963 -0.0241 0.1041 0.1470 223 ARG A CB 1503 C CG . ARG A 196 ? 0.8741 1.2355 1.1556 -0.0441 0.0877 0.1607 223 ARG A CG 1504 C CD . ARG A 196 ? 1.0151 1.4139 1.3183 -0.0484 0.0909 0.1936 223 ARG A CD 1505 N NE . ARG A 196 ? 1.1127 1.5499 1.4379 -0.0465 0.0970 0.2152 223 ARG A NE 1506 C CZ . ARG A 196 ? 1.1415 1.5854 1.5059 -0.0609 0.0842 0.2280 223 ARG A CZ 1507 N NH1 . ARG A 196 ? 1.1506 1.5637 1.5339 -0.0766 0.0636 0.2193 223 ARG A NH1 1508 N NH2 . ARG A 196 ? 1.1364 1.6176 1.5209 -0.0586 0.0906 0.2488 223 ARG A NH2 1509 N N . TYR A 197 ? 0.9173 1.1936 1.1529 -0.0388 0.0775 0.0972 224 TYR A N 1510 C CA . TYR A 197 ? 0.7911 1.0374 1.0185 -0.0442 0.0684 0.0844 224 TYR A CA 1511 C C . TYR A 197 ? 0.7249 0.9748 0.9716 -0.0571 0.0584 0.1006 224 TYR A C 1512 O O . TYR A 197 ? 0.7574 1.0246 1.0341 -0.0669 0.0511 0.1193 224 TYR A O 1513 C CB . TYR A 197 ? 0.7278 0.9490 0.9589 -0.0469 0.0574 0.0666 224 TYR A CB 1514 C CG . TYR A 197 ? 0.6438 0.8537 0.8527 -0.0346 0.0661 0.0485 224 TYR A CG 1515 C CD1 . TYR A 197 ? 0.6072 0.8343 0.8096 -0.0246 0.0781 0.0504 224 TYR A CD1 1516 C CD2 . TYR A 197 ? 0.6141 0.7974 0.8103 -0.0326 0.0620 0.0310 224 TYR A CD2 1517 C CE1 . TYR A 197 ? 0.5854 0.8013 0.7703 -0.0139 0.0847 0.0352 224 TYR A CE1 1518 C CE2 . TYR A 197 ? 0.5796 0.7543 0.7601 -0.0222 0.0692 0.0178 224 TYR A CE2 1519 C CZ . TYR A 197 ? 0.5988 0.7886 0.7741 -0.0133 0.0801 0.0199 224 TYR A CZ 1520 O OH . TYR A 197 ? 0.7159 0.8961 0.8780 -0.0035 0.0861 0.0079 224 TYR A OH 1521 N N . SER A 198 ? 0.6367 0.8704 0.8678 -0.0573 0.0575 0.0943 225 SER A N 1522 C CA . SER A 198 ? 0.6922 0.9205 0.9402 -0.0700 0.0453 0.1048 225 SER A CA 1523 C C . SER A 198 ? 0.7346 0.9372 0.9980 -0.0794 0.0266 0.0937 225 SER A C 1524 O O . SER A 198 ? 0.8166 1.0037 1.0713 -0.0741 0.0250 0.0753 225 SER A O 1525 C CB . SER A 198 ? 0.7094 0.9274 0.9340 -0.0660 0.0498 0.0997 225 SER A CB 1526 O OG . SER A 198 ? 0.6214 0.8078 0.8281 -0.0633 0.0459 0.0759 225 SER A OG 1527 N N . ALA A 199 ? 0.6665 0.8653 0.9524 -0.0919 0.0120 0.1050 226 ALA A N 1528 C CA . ALA A 199 ? 0.6497 0.8198 0.9436 -0.0978 -0.0072 0.0914 226 ALA A CA 1529 C C . ALA A 199 ? 0.7298 0.8762 0.9933 -0.0904 -0.0030 0.0707 226 ALA A C 1530 O O . ALA A 199 ? 0.8091 0.9598 1.0525 -0.0855 0.0101 0.0717 226 ALA A O 1531 C CB . ALA A 199 ? 0.6337 0.8032 0.9569 -0.1120 -0.0242 0.1084 226 ALA A CB 1532 N N . PRO A 200 ? 0.7480 0.8706 1.0085 -0.0885 -0.0148 0.0524 227 PRO A N 1533 C CA . PRO A 200 ? 0.7533 0.8568 0.9886 -0.0819 -0.0108 0.0360 227 PRO A CA 1534 C C . PRO A 200 ? 0.8700 0.9630 1.1062 -0.0891 -0.0182 0.0405 227 PRO A C 1535 O O . PRO A 200 ? 0.9816 1.0756 1.2403 -0.0992 -0.0315 0.0528 227 PRO A O 1536 C CB . PRO A 200 ? 0.7427 0.8301 0.9769 -0.0760 -0.0210 0.0184 227 PRO A CB 1537 C CG . PRO A 200 ? 0.7649 0.8546 1.0263 -0.0826 -0.0383 0.0246 227 PRO A CG 1538 C CD . PRO A 200 ? 0.7641 0.8791 1.0410 -0.0889 -0.0304 0.0449 227 PRO A CD 1539 N N . ALA A 201 ? 0.7845 0.8670 0.9977 -0.0838 -0.0105 0.0309 228 ALA A N 1540 C CA . ALA A 201 ? 0.7868 0.8586 0.9964 -0.0887 -0.0158 0.0329 228 ALA A CA 1541 C C . ALA A 201 ? 0.8299 0.8814 1.0212 -0.0821 -0.0166 0.0145 228 ALA A C 1542 O O . ALA A 201 ? 0.8923 0.9435 1.0667 -0.0739 -0.0049 0.0061 228 ALA A O 1543 C CB . ALA A 201 ? 0.7387 0.8258 0.9394 -0.0887 -0.0033 0.0455 228 ALA A CB 1544 N N . ASN A 202 ? 0.8005 0.8356 0.9965 -0.0851 -0.0309 0.0094 229 ASN A N 1545 C CA . ASN A 202 ? 0.8167 0.8366 0.9967 -0.0779 -0.0309 -0.0057 229 ASN A CA 1546 C C . ASN A 202 ? 0.8162 0.8307 0.9829 -0.0796 -0.0257 -0.0046 229 ASN A C 1547 O O . ASN A 202 ? 0.8494 0.8656 1.0212 -0.0871 -0.0291 0.0060 229 ASN A O 1548 C CB . ASN A 202 ? 0.9481 0.9536 1.1360 -0.0763 -0.0490 -0.0144 229 ASN A CB 1549 C CG . ASN A 202 ? 1.0140 1.0232 1.2130 -0.0719 -0.0563 -0.0186 229 ASN A CG 1550 O OD1 . ASN A 202 ? 1.0491 1.0680 1.2428 -0.0656 -0.0455 -0.0214 229 ASN A OD1 1551 N ND2 . ASN A 202 ? 0.9999 0.9999 1.2146 -0.0746 -0.0764 -0.0198 229 ASN A ND2 1552 N N . LEU A 203 ? 0.6984 0.7072 0.8495 -0.0722 -0.0181 -0.0147 230 LEU A N 1553 C CA . LEU A 203 ? 0.6502 0.6506 0.7888 -0.0722 -0.0156 -0.0172 230 LEU A CA 1554 C C . LEU A 203 ? 0.7753 0.7625 0.9125 -0.0688 -0.0241 -0.0267 230 LEU A C 1555 O O . LEU A 203 ? 0.8321 0.8195 0.9685 -0.0611 -0.0230 -0.0341 230 LEU A O 1556 C CB . LEU A 203 ? 0.5594 0.5632 0.6845 -0.0664 -0.0027 -0.0204 230 LEU A CB 1557 C CG . LEU A 203 ? 0.6741 0.6677 0.7871 -0.0654 -0.0019 -0.0245 230 LEU A CG 1558 C CD1 . LEU A 203 ? 0.7416 0.7368 0.8516 -0.0709 -0.0041 -0.0165 230 LEU A CD1 1559 C CD2 . LEU A 203 ? 0.7095 0.7031 0.8126 -0.0587 0.0070 -0.0296 230 LEU A CD2 1560 N N . TYR A 204 ? 0.7784 0.7566 0.9149 -0.0734 -0.0318 -0.0253 231 TYR A N 1561 C CA . TYR A 204 ? 0.6987 0.6653 0.8317 -0.0697 -0.0395 -0.0331 231 TYR A CA 1562 C C . TYR A 204 ? 0.7396 0.7008 0.8617 -0.0700 -0.0349 -0.0344 231 TYR A C 1563 O O . TYR A 204 ? 0.7302 0.6923 0.8474 -0.0751 -0.0311 -0.0287 231 TYR A O 1564 C CB . TYR A 204 ? 0.6460 0.6038 0.7882 -0.0742 -0.0555 -0.0316 231 TYR A CB 1565 C CG . TYR A 204 ? 0.7014 0.6598 0.8570 -0.0733 -0.0663 -0.0325 231 TYR A CG 1566 C CD1 . TYR A 204 ? 0.7352 0.6891 0.8901 -0.0625 -0.0749 -0.0438 231 TYR A CD1 1567 C CD2 . TYR A 204 ? 0.7535 0.7182 0.9233 -0.0821 -0.0692 -0.0214 231 TYR A CD2 1568 C CE1 . TYR A 204 ? 0.7282 0.6808 0.8947 -0.0603 -0.0876 -0.0466 231 TYR A CE1 1569 C CE2 . TYR A 204 ? 0.7298 0.6938 0.9150 -0.0821 -0.0817 -0.0221 231 TYR A CE2 1570 C CZ . TYR A 204 ? 0.6855 0.6418 0.8683 -0.0710 -0.0918 -0.0360 231 TYR A CZ 1571 O OH . TYR A 204 ? 0.6747 0.6287 0.8722 -0.0696 -0.1068 -0.0385 231 TYR A OH 1572 N N . VAL A 205 ? 0.7548 0.7119 0.8735 -0.0634 -0.0356 -0.0411 232 VAL A N 1573 C CA . VAL A 205 ? 0.7494 0.7012 0.8611 -0.0637 -0.0330 -0.0422 232 VAL A CA 1574 C C . VAL A 205 ? 0.8330 0.7774 0.9448 -0.0619 -0.0429 -0.0452 232 VAL A C 1575 O O . VAL A 205 ? 0.9402 0.8869 1.0541 -0.0535 -0.0462 -0.0494 232 VAL A O 1576 C CB . VAL A 205 ? 0.7263 0.6823 0.8372 -0.0578 -0.0245 -0.0445 232 VAL A CB 1577 C CG1 . VAL A 205 ? 0.6848 0.6343 0.7926 -0.0588 -0.0251 -0.0450 232 VAL A CG1 1578 C CG2 . VAL A 205 ? 0.8142 0.7759 0.9235 -0.0584 -0.0158 -0.0427 232 VAL A CG2 1579 N N . ARG A 206 ? 0.8508 0.7878 0.9592 -0.0683 -0.0472 -0.0426 233 ARG A N 1580 C CA . ARG A 206 ? 0.8274 0.7559 0.9355 -0.0680 -0.0578 -0.0445 233 ARG A CA 1581 C C . ARG A 206 ? 0.9016 0.8277 1.0041 -0.0670 -0.0545 -0.0457 233 ARG A C 1582 O O . ARG A 206 ? 0.8305 0.7575 0.9290 -0.0698 -0.0473 -0.0441 233 ARG A O 1583 C CB . ARG A 206 ? 0.8486 0.7710 0.9595 -0.0765 -0.0659 -0.0389 233 ARG A CB 1584 C CG . ARG A 206 ? 0.9247 0.8488 1.0300 -0.0835 -0.0599 -0.0318 233 ARG A CG 1585 C CD . ARG A 206 ? 0.9616 0.8796 1.0705 -0.0902 -0.0695 -0.0252 233 ARG A CD 1586 N NE . ARG A 206 ? 1.0388 0.9460 1.1456 -0.0873 -0.0786 -0.0312 233 ARG A NE 1587 C CZ . ARG A 206 ? 1.0971 0.9957 1.2076 -0.0915 -0.0898 -0.0278 233 ARG A CZ 1588 N NH1 . ARG A 206 ? 1.0413 0.9417 1.1604 -0.0996 -0.0935 -0.0165 233 ARG A NH1 1589 N NH2 . ARG A 206 ? 1.1036 0.9933 1.2107 -0.0870 -0.0975 -0.0342 233 ARG A NH2 1590 N N . GLU A 207 ? 1.0681 0.9916 1.1706 -0.0619 -0.0605 -0.0487 234 GLU A N 1591 C CA . GLU A 207 ? 1.0533 0.9763 1.1541 -0.0613 -0.0581 -0.0482 234 GLU A CA 1592 C C . GLU A 207 ? 1.0419 0.9559 1.1366 -0.0694 -0.0606 -0.0464 234 GLU A C 1593 O O . GLU A 207 ? 1.0663 0.9744 1.1589 -0.0736 -0.0672 -0.0449 234 GLU A O 1594 C CB . GLU A 207 ? 1.1240 1.0498 1.2266 -0.0525 -0.0637 -0.0502 234 GLU A CB 1595 C CG . GLU A 207 ? 1.3173 1.2567 1.4250 -0.0410 -0.0597 -0.0506 234 GLU A CG 1596 C CD . GLU A 207 ? 1.4804 1.4301 1.5948 -0.0371 -0.0538 -0.0453 234 GLU A CD 1597 O OE1 . GLU A 207 ? 1.4912 1.4355 1.6078 -0.0453 -0.0516 -0.0425 234 GLU A OE1 1598 O OE2 . GLU A 207 ? 1.5405 1.5046 1.6590 -0.0250 -0.0522 -0.0432 234 GLU A OE2 1599 N N . LEU A 208 ? 1.0341 0.9473 1.1270 -0.0709 -0.0563 -0.0462 235 LEU A N 1600 C CA . LEU A 208 ? 1.0063 0.9126 1.0910 -0.0762 -0.0579 -0.0456 235 LEU A CA 1601 C C . LEU A 208 ? 1.0992 0.9990 1.1812 -0.0783 -0.0661 -0.0449 235 LEU A C 1602 O O . LEU A 208 ? 1.1727 1.0721 1.2586 -0.0750 -0.0702 -0.0462 235 LEU A O 1603 C CB . LEU A 208 ? 0.8367 0.7408 0.9218 -0.0753 -0.0560 -0.0478 235 LEU A CB 1604 C CG . LEU A 208 ? 0.7061 0.6066 0.7807 -0.0764 -0.0542 -0.0497 235 LEU A CG 1605 C CD1 . LEU A 208 ? 0.5780 0.4726 0.6556 -0.0747 -0.0569 -0.0537 235 LEU A CD1 1606 C CD2 . LEU A 208 ? 0.6509 0.5484 0.7143 -0.0792 -0.0576 -0.0478 235 LEU A CD2 1607 N N . ARG A 209 ? 1.0935 0.9903 1.1694 -0.0832 -0.0683 -0.0415 236 ARG A N 1608 C CA . ARG A 209 ? 1.1103 1.0002 1.1836 -0.0858 -0.0764 -0.0397 236 ARG A CA 1609 C C . ARG A 209 ? 1.2672 1.1538 1.3312 -0.0872 -0.0763 -0.0400 236 ARG A C 1610 O O . ARG A 209 ? 1.2940 1.1837 1.3502 -0.0878 -0.0721 -0.0378 236 ARG A O 1611 C CB . ARG A 209 ? 1.0028 0.8923 1.0788 -0.0905 -0.0806 -0.0331 236 ARG A CB 1612 C CG . ARG A 209 ? 0.9585 0.8404 1.0330 -0.0938 -0.0895 -0.0297 236 ARG A CG 1613 C CD . ARG A 209 ? 0.9839 0.8662 1.0657 -0.0997 -0.0945 -0.0199 236 ARG A CD 1614 N NE . ARG A 209 ? 1.0339 0.9084 1.1162 -0.1031 -0.1039 -0.0153 236 ARG A NE 1615 C CZ . ARG A 209 ? 1.0584 0.9353 1.1327 -0.1055 -0.1016 -0.0092 236 ARG A CZ 1616 N NH1 . ARG A 209 ? 1.0864 0.9727 1.1503 -0.1034 -0.0913 -0.0084 236 ARG A NH1 1617 N NH2 . ARG A 209 ? 1.0509 0.9207 1.1267 -0.1084 -0.1106 -0.0045 236 ARG A NH2 1618 N N . GLU A 210 ? 1.3884 1.2699 1.4528 -0.0861 -0.0815 -0.0429 237 GLU A N 1619 C CA . GLU A 210 ? 1.5512 1.4284 1.6078 -0.0866 -0.0835 -0.0447 237 GLU A CA 1620 C C . GLU A 210 ? 1.6688 1.5413 1.7192 -0.0892 -0.0898 -0.0412 237 GLU A C 1621 O O . GLU A 210 ? 1.6889 1.5577 1.7438 -0.0893 -0.0959 -0.0411 237 GLU A O 1622 C CB . GLU A 210 ? 1.5528 1.4286 1.6170 -0.0842 -0.0858 -0.0486 237 GLU A CB 1623 C CG . GLU A 210 ? 1.5241 1.4038 1.5953 -0.0821 -0.0804 -0.0504 237 GLU A CG 1624 C CD . GLU A 210 ? 1.4787 1.3598 1.5636 -0.0807 -0.0832 -0.0501 237 GLU A CD 1625 O OE1 . GLU A 210 ? 1.5268 1.4036 1.6128 -0.0819 -0.0899 -0.0504 237 GLU A OE1 1626 O OE2 . GLU A 210 ? 1.4283 1.3162 1.5246 -0.0785 -0.0788 -0.0481 237 GLU A OE2 1627 N N . VAL A 211 ? 1.7419 1.6161 1.7817 -0.0900 -0.0882 -0.0380 238 VAL A N 1628 C CA . VAL A 211 ? 1.7851 1.6573 1.8190 -0.0922 -0.0931 -0.0323 238 VAL A CA 1629 C C . VAL A 211 ? 1.7791 1.6433 1.8113 -0.0915 -0.1003 -0.0370 238 VAL A C 1630 O O . VAL A 211 ? 1.8306 1.6928 1.8559 -0.0886 -0.1015 -0.0423 238 VAL A O 1631 C CB . VAL A 211 ? 1.9349 1.8150 1.9557 -0.0898 -0.0886 -0.0273 238 VAL A CB 1632 C CG1 . VAL A 211 ? 1.9311 1.8220 1.9568 -0.0922 -0.0829 -0.0169 238 VAL A CG1 1633 C CG2 . VAL A 211 ? 1.9192 1.7993 1.9305 -0.0832 -0.0859 -0.0366 238 VAL A CG2 1634 N N . ARG A 212 ? 1.7991 1.6587 1.8383 -0.0931 -0.1064 -0.0358 239 ARG A N 1635 C CA . ARG A 212 ? 1.7300 1.5843 1.7690 -0.0917 -0.1128 -0.0394 239 ARG A CA 1636 C C . ARG A 212 ? 1.5983 1.4496 1.6265 -0.0929 -0.1168 -0.0362 239 ARG A C 1637 O O . ARG A 212 ? 1.5540 1.4028 1.5822 -0.0953 -0.1212 -0.0300 239 ARG A O 1638 C CB . ARG A 212 ? 1.7177 1.5694 1.7654 -0.0901 -0.1184 -0.0398 239 ARG A CB 1639 C CG . ARG A 212 ? 1.7232 1.5754 1.7750 -0.0864 -0.1219 -0.0435 239 ARG A CG 1640 C CD . ARG A 212 ? 1.7160 1.5739 1.7738 -0.0853 -0.1167 -0.0462 239 ARG A CD 1641 N NE . ARG A 212 ? 1.6644 1.5308 1.7340 -0.0804 -0.1141 -0.0459 239 ARG A NE 1642 C CZ . ARG A 212 ? 1.5764 1.4473 1.6490 -0.0783 -0.1091 -0.0459 239 ARG A CZ 1643 N NH1 . ARG A 212 ? 1.6035 1.4709 1.6700 -0.0820 -0.1064 -0.0456 239 ARG A NH1 1644 N NH2 . ARG A 212 ? 1.4726 1.3536 1.5547 -0.0718 -0.1066 -0.0451 239 ARG A NH2 1645 N N . ARG A 213 ? 1.5416 1.3929 1.5611 -0.0903 -0.1165 -0.0406 240 ARG A N 1646 C CA . ARG A 213 ? 1.4798 1.3295 1.4872 -0.0890 -0.1208 -0.0391 240 ARG A CA 1647 C C . ARG A 213 ? 1.3881 1.2311 1.3987 -0.0887 -0.1288 -0.0438 240 ARG A C 1648 O O . ARG A 213 ? 1.4354 1.2769 1.4541 -0.0878 -0.1307 -0.0497 240 ARG A O 1649 C CB . ARG A 213 ? 1.4981 1.3517 1.4914 -0.0833 -0.1180 -0.0427 240 ARG A CB 1650 C CG . ARG A 213 ? 1.5162 1.3807 1.5035 -0.0818 -0.1096 -0.0351 240 ARG A CG 1651 C CD . ARG A 213 ? 1.5587 1.4291 1.5276 -0.0721 -0.1080 -0.0388 240 ARG A CD 1652 N NE . ARG A 213 ? 1.6315 1.5174 1.5940 -0.0691 -0.0993 -0.0280 240 ARG A NE 1653 C CZ . ARG A 213 ? 1.6710 1.5685 1.6244 -0.0661 -0.0974 -0.0161 240 ARG A CZ 1654 N NH1 . ARG A 213 ? 1.6705 1.5639 1.6183 -0.0656 -0.1040 -0.0152 240 ARG A NH1 1655 N NH2 . ARG A 213 ? 1.6775 1.5930 1.6287 -0.0633 -0.0888 -0.0035 240 ARG A NH2 1656 N N . VAL A 214 ? 1.3053 1.1456 1.3118 -0.0897 -0.1340 -0.0395 241 VAL A N 1657 C CA . VAL A 214 ? 1.2609 1.0962 1.2698 -0.0891 -0.1417 -0.0429 241 VAL A CA 1658 C C . VAL A 214 ? 1.2558 1.0894 1.2510 -0.0874 -0.1463 -0.0411 241 VAL A C 1659 O O . VAL A 214 ? 1.2213 1.0560 1.2118 -0.0888 -0.1462 -0.0327 241 VAL A O 1660 C CB . VAL A 214 ? 1.1693 1.0025 1.1886 -0.0901 -0.1452 -0.0404 241 VAL A CB 1661 C CG1 . VAL A 214 ? 1.1157 0.9461 1.1363 -0.0885 -0.1528 -0.0424 241 VAL A CG1 1662 C CG2 . VAL A 214 ? 1.1290 0.9664 1.1605 -0.0889 -0.1410 -0.0427 241 VAL A CG2 1663 N N . PRO A 215 ? 1.2519 1.0831 1.2419 -0.0840 -0.1514 -0.0483 242 PRO A N 1664 C CA . PRO A 215 ? 1.1631 0.9932 1.1388 -0.0804 -0.1568 -0.0482 242 PRO A CA 1665 C C . PRO A 215 ? 1.1232 0.9505 1.1019 -0.0832 -0.1613 -0.0422 242 PRO A C 1666 O O . PRO A 215 ? 1.0974 0.9221 1.0894 -0.0860 -0.1632 -0.0424 242 PRO A O 1667 C CB . PRO A 215 ? 1.2283 1.0534 1.2048 -0.0771 -0.1648 -0.0591 242 PRO A CB 1668 C CG . PRO A 215 ? 1.3005 1.1257 1.2880 -0.0781 -0.1614 -0.0635 242 PRO A CG 1669 C CD . PRO A 215 ? 1.2801 1.1093 1.2797 -0.0833 -0.1538 -0.0565 242 PRO A CD 1670 N N . PRO A 216 ? 1.1346 0.9634 1.1006 -0.0811 -0.1632 -0.0364 243 PRO A N 1671 C CA . PRO A 216 ? 1.1268 0.9520 1.0951 -0.0836 -0.1681 -0.0295 243 PRO A CA 1672 C C . PRO A 216 ? 1.1458 0.9651 1.1222 -0.0838 -0.1759 -0.0357 243 PRO A C 1673 O O . PRO A 216 ? 1.0966 0.9153 1.0747 -0.0819 -0.1792 -0.0439 243 PRO A O 1674 C CB . PRO A 216 ? 1.0600 0.8904 1.0116 -0.0790 -0.1689 -0.0235 243 PRO A CB 1675 C CG . PRO A 216 ? 1.0825 0.9177 1.0213 -0.0718 -0.1671 -0.0318 243 PRO A CG 1676 C CD . PRO A 216 ? 1.1249 0.9606 1.0727 -0.0742 -0.1611 -0.0358 243 PRO A CD 1677 N N . ARG A 217 ? 1.2089 1.0240 1.1915 -0.0856 -0.1797 -0.0310 244 ARG A N 1678 C CA . ARG A 217 ? 1.2426 1.0552 1.2333 -0.0841 -0.1862 -0.0351 244 ARG A CA 1679 C C . ARG A 217 ? 1.2261 1.0329 1.2150 -0.0837 -0.1926 -0.0293 244 ARG A C 1680 O O . ARG A 217 ? 1.2331 1.0360 1.2248 -0.0857 -0.1928 -0.0234 244 ARG A O 1681 C CB . ARG A 217 ? 1.3478 1.1634 1.3527 -0.0836 -0.1835 -0.0383 244 ARG A CB 1682 C CG . ARG A 217 ? 1.3953 1.2135 1.4096 -0.0797 -0.1888 -0.0399 244 ARG A CG 1683 C CD . ARG A 217 ? 1.4735 1.2983 1.5000 -0.0764 -0.1849 -0.0407 244 ARG A CD 1684 N NE . ARG A 217 ? 1.5626 1.3959 1.5986 -0.0703 -0.1884 -0.0405 244 ARG A NE 1685 C CZ . ARG A 217 ? 1.5881 1.4320 1.6344 -0.0642 -0.1852 -0.0398 244 ARG A CZ 1686 N NH1 . ARG A 217 ? 1.6362 1.4813 1.6844 -0.0640 -0.1793 -0.0407 244 ARG A NH1 1687 N NH2 . ARG A 217 ? 1.5290 1.3848 1.5839 -0.0570 -0.1877 -0.0373 244 ARG A NH2 1688 N N . PHE A 218 ? 1.2581 1.0636 1.2439 -0.0813 -0.1992 -0.0309 245 PHE A N 1689 C CA . PHE A 218 ? 1.2754 1.0746 1.2593 -0.0803 -0.2062 -0.0258 245 PHE A CA 1690 C C . PHE A 218 ? 1.2276 1.0234 1.2219 -0.0771 -0.2101 -0.0278 245 PHE A C 1691 O O . PHE A 218 ? 1.2295 1.0290 1.2284 -0.0724 -0.2134 -0.0321 245 PHE A O 1692 C CB . PHE A 218 ? 1.2940 1.0936 1.2711 -0.0777 -0.2123 -0.0274 245 PHE A CB 1693 C CG . PHE A 218 ? 1.2799 1.0816 1.2427 -0.0776 -0.2113 -0.0240 245 PHE A CG 1694 C CD1 . PHE A 218 ? 1.2698 1.0702 1.2266 -0.0789 -0.2109 -0.0129 245 PHE A CD1 1695 C CD2 . PHE A 218 ? 1.2998 1.1056 1.2558 -0.0750 -0.2118 -0.0311 245 PHE A CD2 1696 C CE1 . PHE A 218 ? 1.2758 1.0829 1.2184 -0.0762 -0.2087 -0.0077 245 PHE A CE1 1697 C CE2 . PHE A 218 ? 1.3508 1.1602 1.2904 -0.0713 -0.2115 -0.0292 245 PHE A CE2 1698 C CZ . PHE A 218 ? 1.3243 1.1362 1.2562 -0.0712 -0.2088 -0.0169 245 PHE A CZ 1699 N N . SER A 219 ? 1.1645 0.9546 1.1627 -0.0785 -0.2104 -0.0244 246 SER A N 1700 C CA . SER A 219 ? 1.0908 0.8756 1.0960 -0.0729 -0.2168 -0.0276 246 SER A CA 1701 C C . SER A 219 ? 1.0655 0.8436 1.0680 -0.0677 -0.2273 -0.0276 246 SER A C 1702 O O . SER A 219 ? 1.0688 0.8504 1.0737 -0.0590 -0.2309 -0.0333 246 SER A O 1703 C CB . SER A 219 ? 1.1906 0.9671 1.2010 -0.0761 -0.2190 -0.0236 246 SER A CB 1704 O OG . SER A 219 ? 1.3570 1.1229 1.3717 -0.0694 -0.2307 -0.0268 246 SER A OG 1705 N N . ILE A 220 ? 1.0657 0.8365 1.0635 -0.0721 -0.2320 -0.0201 247 ILE A N 1706 C CA . ILE A 220 ? 1.0468 0.8114 1.0411 -0.0678 -0.2417 -0.0194 247 ILE A CA 1707 C C . ILE A 220 ? 1.0941 0.8637 1.0793 -0.0714 -0.2390 -0.0147 247 ILE A C 1708 O O . ILE A 220 ? 1.0941 0.8603 1.0759 -0.0760 -0.2402 -0.0048 247 ILE A O 1709 C CB . ILE A 220 ? 1.0100 0.7584 1.0090 -0.0677 -0.2539 -0.0141 247 ILE A CB 1710 C CG1 . ILE A 220 ? 1.0687 0.8107 1.0752 -0.0618 -0.2591 -0.0212 247 ILE A CG1 1711 C CG2 . ILE A 220 ? 1.0115 0.7531 1.0065 -0.0622 -0.2644 -0.0142 247 ILE A CG2 1712 C CD1 . ILE A 220 ? 1.1876 0.9102 1.2011 -0.0606 -0.2755 -0.0183 247 ILE A CD1 1713 N N . PRO A 221 ? 1.1491 0.9283 1.1318 -0.0687 -0.2360 -0.0209 248 PRO A N 1714 C CA . PRO A 221 ? 1.2750 1.0580 1.2483 -0.0698 -0.2362 -0.0193 248 PRO A CA 1715 C C . PRO A 221 ? 1.4122 1.1880 1.3813 -0.0671 -0.2455 -0.0148 248 PRO A C 1716 O O . PRO A 221 ? 1.4216 1.1928 1.3955 -0.0618 -0.2522 -0.0177 248 PRO A O 1717 C CB . PRO A 221 ? 1.2289 1.0216 1.2069 -0.0673 -0.2347 -0.0274 248 PRO A CB 1718 C CG . PRO A 221 ? 1.1638 0.9590 1.1529 -0.0624 -0.2354 -0.0305 248 PRO A CG 1719 C CD . PRO A 221 ? 1.1412 0.9290 1.1317 -0.0639 -0.2334 -0.0285 248 PRO A CD 1720 N N . PRO A 222 ? 1.5113 1.2872 1.4707 -0.0691 -0.2460 -0.0075 249 PRO A N 1721 C CA . PRO A 222 ? 1.5216 1.2908 1.4775 -0.0669 -0.2547 -0.0015 249 PRO A CA 1722 C C . PRO A 222 ? 1.5154 1.2866 1.4706 -0.0610 -0.2604 -0.0093 249 PRO A C 1723 O O . PRO A 222 ? 1.4547 1.2351 1.4082 -0.0602 -0.2577 -0.0158 249 PRO A O 1724 C CB . PRO A 222 ? 1.5343 1.3096 1.4787 -0.0687 -0.2513 0.0078 249 PRO A CB 1725 C CG . PRO A 222 ? 1.5297 1.3154 1.4682 -0.0686 -0.2429 0.0009 249 PRO A CG 1726 C CD . PRO A 222 ? 1.5197 1.3039 1.4696 -0.0713 -0.2386 -0.0048 249 PRO A CD 1727 N N . THR A 223 ? 1.6138 1.3766 1.5718 -0.0566 -0.2694 -0.0086 250 THR A N 1728 C CA . THR A 223 ? 1.6459 1.4127 1.6036 -0.0499 -0.2749 -0.0141 250 THR A CA 1729 C C . THR A 223 ? 1.6252 1.3880 1.5741 -0.0489 -0.2814 -0.0082 250 THR A C 1730 O O . THR A 223 ? 1.6104 1.3639 1.5570 -0.0513 -0.2849 0.0011 250 THR A O 1731 C CB . THR A 223 ? 1.7040 1.4671 1.6690 -0.0417 -0.2807 -0.0191 250 THR A CB 1732 O OG1 . THR A 223 ? 1.7224 1.4689 1.6880 -0.0412 -0.2889 -0.0146 250 THR A OG1 1733 C CG2 . THR A 223 ? 1.7426 1.5143 1.7159 -0.0405 -0.2735 -0.0248 250 THR A CG2 1734 N N . ASN A 224 ? 1.6245 1.3953 1.5706 -0.0454 -0.2836 -0.0125 251 ASN A N 1735 C CA . ASN A 224 ? 1.6024 1.3721 1.5387 -0.0438 -0.2891 -0.0081 251 ASN A CA 1736 C C . ASN A 224 ? 1.6006 1.3596 1.5372 -0.0388 -0.2989 -0.0041 251 ASN A C 1737 O O . ASN A 224 ? 1.6103 1.3656 1.5539 -0.0333 -0.3031 -0.0086 251 ASN A O 1738 C CB . ASN A 224 ? 1.6249 1.4060 1.5605 -0.0415 -0.2903 -0.0149 251 ASN A CB 1739 C CG . ASN A 224 ? 1.6728 1.4622 1.6135 -0.0453 -0.2838 -0.0211 251 ASN A CG 1740 O OD1 . ASN A 224 ? 1.6483 1.4393 1.5802 -0.0478 -0.2805 -0.0214 251 ASN A OD1 1741 N ND2 . ASN A 224 ? 1.7242 1.5202 1.6791 -0.0445 -0.2821 -0.0255 251 ASN A ND2 1742 N N . HIS A 225 ? 1.6399 1.3946 1.5683 -0.0392 -0.3031 0.0045 252 HIS A N 1743 C CA . HIS A 225 ? 1.6854 1.4278 1.6148 -0.0350 -0.3138 0.0094 252 HIS A CA 1744 C C . HIS A 225 ? 1.8734 1.6192 1.7932 -0.0318 -0.3183 0.0131 252 HIS A C 1745 O O . HIS A 225 ? 1.8893 1.6445 1.7997 -0.0337 -0.3135 0.0158 252 HIS A O 1746 C CB . HIS A 225 ? 1.6143 1.3436 1.5490 -0.0402 -0.3167 0.0213 252 HIS A CB 1747 C CG . HIS A 225 ? 1.7382 1.4610 1.6835 -0.0421 -0.3158 0.0172 252 HIS A CG 1748 N ND1 . HIS A 225 ? 1.8178 1.5426 1.7667 -0.0357 -0.3159 0.0041 252 HIS A ND1 1749 C CD2 . HIS A 225 ? 1.7984 1.5143 1.7518 -0.0489 -0.3149 0.0254 252 HIS A CD2 1750 C CE1 . HIS A 225 ? 1.8246 1.5429 1.7815 -0.0378 -0.3154 0.0028 252 HIS A CE1 1751 N NE2 . HIS A 225 ? 1.8208 1.5327 1.7813 -0.0465 -0.3153 0.0153 252 HIS A NE2 1752 N N . GLU A 226 ? 1.9942 1.7323 1.9150 -0.0252 -0.3284 0.0124 253 GLU A N 1753 C CA . GLU A 226 ? 2.0459 1.7852 1.9581 -0.0219 -0.3340 0.0173 253 GLU A CA 1754 C C . GLU A 226 ? 2.0448 1.7668 1.9603 -0.0192 -0.3454 0.0256 253 GLU A C 1755 O O . GLU A 226 ? 2.0598 1.7708 1.9823 -0.0139 -0.3530 0.0198 253 GLU A O 1756 C CB . GLU A 226 ? 2.0384 1.7890 1.9491 -0.0154 -0.3358 0.0071 253 GLU A CB 1757 C CG . GLU A 226 ? 2.0312 1.7797 1.9493 -0.0068 -0.3420 0.0001 253 GLU A CG 1758 C CD . GLU A 226 ? 2.0503 1.7945 1.9639 0.0011 -0.3523 0.0020 253 GLU A CD 1759 O OE1 . GLU A 226 ? 2.0904 1.8195 2.0010 0.0009 -0.3592 0.0101 253 GLU A OE1 1760 O OE2 . GLU A 226 ? 2.0307 1.7873 1.9455 0.0074 -0.3539 -0.0034 253 GLU A OE2 1761 N N . ILE A 227 ? 1.9001 1.6198 1.8110 -0.0219 -0.3475 0.0394 254 ILE A N 1762 C CA . ILE A 227 ? 1.7759 1.4779 1.6938 -0.0213 -0.3596 0.0505 254 ILE A CA 1763 C C . ILE A 227 ? 1.7499 1.4542 1.6600 -0.0190 -0.3639 0.0617 254 ILE A C 1764 O O . ILE A 227 ? 1.7549 1.4754 1.6525 -0.0175 -0.3569 0.0613 254 ILE A O 1765 C CB . ILE A 227 ? 1.6581 1.3517 1.5880 -0.0304 -0.3591 0.0639 254 ILE A CB 1766 C CG1 . ILE A 227 ? 1.5793 1.2914 1.5032 -0.0368 -0.3443 0.0724 254 ILE A CG1 1767 C CG2 . ILE A 227 ? 1.6423 1.3246 1.5830 -0.0302 -0.3624 0.0531 254 ILE A CG2 1768 C CD1 . ILE A 227 ? 1.5967 1.3177 1.5149 -0.0375 -0.3429 0.0915 254 ILE A CD1 1769 N N . MET A 228 ? 1.7309 1.4181 1.6489 -0.0178 -0.3768 0.0715 255 MET A N 1770 C CA . MET A 228 ? 1.7360 1.4239 1.6491 -0.0157 -0.3819 0.0850 255 MET A CA 1771 C C . MET A 228 ? 1.5941 1.2907 1.5101 -0.0235 -0.3755 0.1080 255 MET A C 1772 O O . MET A 228 ? 1.5976 1.2913 1.5260 -0.0313 -0.3729 0.1163 255 MET A O 1773 C CB . MET A 228 ? 1.8996 1.5644 1.8218 -0.0107 -0.4001 0.0864 255 MET A CB 1774 C CG . MET A 228 ? 1.9788 1.6402 1.8948 0.0011 -0.4064 0.0662 255 MET A CG 1775 S SD . MET A 228 ? 2.8350 2.4680 2.7592 0.0103 -0.4297 0.0661 255 MET A SD 1776 C CE . MET A 228 ? 1.7716 1.3822 1.7159 0.0029 -0.4386 0.0715 255 MET A CE 1777 N N . PRO A 229 ? 1.5408 1.2506 1.4457 -0.0203 -0.3728 0.1193 256 PRO A N 1778 C CA . PRO A 229 ? 1.5642 1.2893 1.4692 -0.0242 -0.3650 0.1434 256 PRO A CA 1779 C C . PRO A 229 ? 1.6063 1.3195 1.5357 -0.0332 -0.3718 0.1660 256 PRO A C 1780 O O . PRO A 229 ? 1.6554 1.3513 1.5975 -0.0336 -0.3863 0.1759 256 PRO A O 1781 C CB . PRO A 229 ? 1.5760 1.3103 1.4677 -0.0165 -0.3674 0.1510 256 PRO A CB 1782 C CG . PRO A 229 ? 1.5481 1.2814 1.4263 -0.0091 -0.3696 0.1259 256 PRO A CG 1783 C CD . PRO A 229 ? 1.5271 1.2412 1.4176 -0.0112 -0.3765 0.1099 256 PRO A CD 1784 N N . GLY A 230 ? 1.5588 1.2808 1.4960 -0.0403 -0.3625 0.1744 257 GLY A N 1785 C CA . GLY A 230 ? 1.5314 1.2467 1.4948 -0.0501 -0.3679 0.1990 257 GLY A CA 1786 C C . GLY A 230 ? 1.5719 1.2544 1.5584 -0.0543 -0.3886 0.1977 257 GLY A C 1787 O O . GLY A 230 ? 1.5960 1.2678 1.5967 -0.0558 -0.4016 0.2158 257 GLY A O 1788 N N . GLY A 231 ? 1.5862 1.2526 1.5765 -0.0549 -0.3930 0.1763 258 GLY A N 1789 C CA . GLY A 231 ? 1.5601 1.2394 1.5348 -0.0530 -0.3781 0.1560 258 GLY A CA 1790 C C . GLY A 231 ? 1.5525 1.2399 1.5387 -0.0620 -0.3691 0.1646 258 GLY A C 1791 O O . GLY A 231 ? 1.5319 1.2435 1.5125 -0.0641 -0.3547 0.1791 258 GLY A O 1792 N N . SER A 232 ? 1.6111 1.2791 1.6124 -0.0656 -0.3781 0.1554 259 SER A N 1793 C CA . SER A 232 ? 1.6360 1.3105 1.6474 -0.0734 -0.3699 0.1590 259 SER A CA 1794 C C . SER A 232 ? 1.7240 1.3943 1.7252 -0.0689 -0.3657 0.1304 259 SER A C 1795 O O . SER A 232 ? 1.8058 1.4656 1.7977 -0.0601 -0.3725 0.1106 259 SER A O 1796 C CB . SER A 232 ? 1.6432 1.2996 1.6864 -0.0830 -0.3854 0.1777 259 SER A CB 1797 O OG . SER A 232 ? 1.6583 1.3244 1.7150 -0.0885 -0.3869 0.2095 259 SER A OG 1798 N N . VAL A 233 ? 1.7741 1.4549 1.7777 -0.0742 -0.3542 0.1298 260 VAL A N 1799 C CA . VAL A 233 ? 1.7817 1.4611 1.7780 -0.0707 -0.3490 0.1057 260 VAL A CA 1800 C C . VAL A 233 ? 1.7212 1.4106 1.7252 -0.0784 -0.3382 0.1109 260 VAL A C 1801 O O . VAL A 233 ? 1.6885 1.3972 1.6911 -0.0830 -0.3265 0.1276 260 VAL A O 1802 C CB . VAL A 233 ? 1.4380 1.1322 1.4107 -0.0626 -0.3381 0.0883 260 VAL A CB 1803 C CG1 . VAL A 233 ? 1.4563 1.1751 1.4160 -0.0642 -0.3222 0.0975 260 VAL A CG1 1804 C CG2 . VAL A 233 ? 1.4160 1.1088 1.3855 -0.0585 -0.3348 0.0660 260 VAL A CG2 1805 N N . ASN A 234 ? 1.6756 1.3530 1.6869 -0.0783 -0.3425 0.0969 261 ASN A N 1806 C CA . ASN A 234 ? 1.6449 1.3307 1.6631 -0.0848 -0.3327 0.0989 261 ASN A CA 1807 C C . ASN A 234 ? 1.6695 1.3653 1.6721 -0.0795 -0.3202 0.0771 261 ASN A C 1808 O O . ASN A 234 ? 1.7022 1.3870 1.7046 -0.0733 -0.3264 0.0595 261 ASN A O 1809 C CB . ASN A 234 ? 1.6568 1.3214 1.6984 -0.0893 -0.3482 0.1013 261 ASN A CB 1810 C CG . ASN A 234 ? 1.6730 1.3299 1.7380 -0.0982 -0.3603 0.1281 261 ASN A CG 1811 O OD1 . ASN A 234 ? 1.7481 1.4232 1.8134 -0.1030 -0.3514 0.1497 261 ASN A OD1 1812 N ND2 . ASN A 234 ? 1.6156 1.2461 1.7015 -0.0996 -0.3821 0.1273 261 ASN A ND2 1813 N N . ILE A 235 ? 1.6496 1.3668 1.6398 -0.0807 -0.3036 0.0788 262 ILE A N 1814 C CA . ILE A 235 ? 1.5275 1.2534 1.5067 -0.0768 -0.2932 0.0599 262 ILE A CA 1815 C C . ILE A 235 ? 1.4009 1.1317 1.3878 -0.0826 -0.2851 0.0615 262 ILE A C 1816 O O . ILE A 235 ? 1.4125 1.1530 1.4038 -0.0884 -0.2791 0.0780 262 ILE A O 1817 C CB . ILE A 235 ? 1.5280 1.2711 1.4882 -0.0728 -0.2830 0.0561 262 ILE A CB 1818 C CG1 . ILE A 235 ? 1.6707 1.4219 1.6245 -0.0705 -0.2740 0.0389 262 ILE A CG1 1819 C CG2 . ILE A 235 ? 1.4014 1.1598 1.3565 -0.0754 -0.2752 0.0743 262 ILE A CG2 1820 C CD1 . ILE A 235 ? 1.7519 1.4945 1.7106 -0.0657 -0.2799 0.0233 262 ILE A CD1 1821 N N . THR A 236 ? 1.3171 1.0434 1.3061 -0.0801 -0.2845 0.0456 263 THR A N 1822 C CA . THR A 236 ? 1.2701 0.9989 1.2678 -0.0853 -0.2785 0.0467 263 THR A CA 1823 C C . THR A 236 ? 1.3116 1.0553 1.2989 -0.0837 -0.2640 0.0353 263 THR A C 1824 O O . THR A 236 ? 1.4211 1.1674 1.4009 -0.0777 -0.2626 0.0212 263 THR A O 1825 C CB . THR A 236 ? 1.2712 0.9820 1.2823 -0.0835 -0.2910 0.0391 263 THR A CB 1826 O OG1 . THR A 236 ? 1.2788 0.9724 1.3007 -0.0842 -0.3079 0.0481 263 THR A OG1 1827 C CG2 . THR A 236 ? 1.2862 0.9989 1.3085 -0.0898 -0.2866 0.0427 263 THR A CG2 1828 N N . CYS A 237 ? 1.2137 0.9678 1.2026 -0.0889 -0.2540 0.0427 264 CYS A N 1829 C CA . CYS A 237 ? 1.2010 0.9677 1.1815 -0.0876 -0.2414 0.0329 264 CYS A CA 1830 C C . CYS A 237 ? 1.2300 0.9964 1.2212 -0.0919 -0.2373 0.0329 264 CYS A C 1831 O O . CYS A 237 ? 1.3581 1.1246 1.3598 -0.0977 -0.2381 0.0474 264 CYS A O 1832 C CB . CYS A 237 ? 1.2393 1.0221 1.2058 -0.0865 -0.2322 0.0400 264 CYS A CB 1833 S SG . CYS A 237 ? 1.1563 0.9515 1.1111 -0.0830 -0.2205 0.0261 264 CYS A SG 1834 N N . VAL A 238 ? 1.1663 0.9336 1.1571 -0.0891 -0.2331 0.0183 265 VAL A N 1835 C CA . VAL A 238 ? 1.1483 0.9160 1.1482 -0.0922 -0.2289 0.0169 265 VAL A CA 1836 C C . VAL A 238 ? 1.2010 0.9801 1.1948 -0.0907 -0.2170 0.0072 265 VAL A C 1837 O O . VAL A 238 ? 1.1983 0.9792 1.1887 -0.0860 -0.2164 -0.0044 265 VAL A O 1838 C CB . VAL A 238 ? 1.1768 0.9307 1.1872 -0.0889 -0.2394 0.0091 265 VAL A CB 1839 C CG1 . VAL A 238 ? 1.1885 0.9438 1.2074 -0.0911 -0.2351 0.0068 265 VAL A CG1 1840 C CG2 . VAL A 238 ? 1.2287 0.9675 1.2480 -0.0902 -0.2544 0.0177 265 VAL A CG2 1841 N N . ALA A 239 ? 1.2961 1.0834 1.2906 -0.0946 -0.2084 0.0133 266 ALA A N 1842 C CA . ALA A 239 ? 1.3263 1.1230 1.3158 -0.0933 -0.1981 0.0050 266 ALA A CA 1843 C C . ALA A 239 ? 1.3568 1.1533 1.3570 -0.0962 -0.1943 0.0044 266 ALA A C 1844 O O . ALA A 239 ? 1.3224 1.1152 1.3326 -0.1006 -0.1977 0.0143 266 ALA A O 1845 C CB . ALA A 239 ? 1.2887 1.0977 1.2654 -0.0921 -0.1905 0.0106 266 ALA A CB 1846 N N . VAL A 240 ? 1.4006 1.2012 1.4004 -0.0939 -0.1883 -0.0064 267 VAL A N 1847 C CA . VAL A 240 ? 1.3264 1.1280 1.3351 -0.0955 -0.1841 -0.0082 267 VAL A CA 1848 C C . VAL A 240 ? 1.3288 1.1403 1.3325 -0.0948 -0.1734 -0.0132 267 VAL A C 1849 O O . VAL A 240 ? 1.3443 1.1593 1.3399 -0.0921 -0.1717 -0.0188 267 VAL A O 1850 C CB . VAL A 240 ? 1.1245 0.9198 1.1413 -0.0910 -0.1898 -0.0171 267 VAL A CB 1851 C CG1 . VAL A 240 ? 1.2033 0.9861 1.2256 -0.0901 -0.2027 -0.0137 267 VAL A CG1 1852 C CG2 . VAL A 240 ? 0.9215 0.7214 0.9352 -0.0857 -0.1888 -0.0259 267 VAL A CG2 1853 N N . GLY A 241 ? 1.2688 1.0837 1.2784 -0.0970 -0.1677 -0.0116 268 GLY A N 1854 C CA . GLY A 241 ? 1.2003 1.0233 1.2062 -0.0958 -0.1584 -0.0167 268 GLY A CA 1855 C C . GLY A 241 ? 1.0984 0.9283 1.1063 -0.0988 -0.1516 -0.0088 268 GLY A C 1856 O O . GLY A 241 ? 1.0950 0.9250 1.1084 -0.1027 -0.1540 0.0030 268 GLY A O 1857 N N . SER A 242 ? 1.0697 0.9058 1.0753 -0.0970 -0.1437 -0.0142 269 SER A N 1858 C CA . SER A 242 ? 1.0679 0.9126 1.0751 -0.0987 -0.1361 -0.0072 269 SER A CA 1859 C C . SER A 242 ? 1.1506 1.0056 1.1429 -0.0934 -0.1291 -0.0079 269 SER A C 1860 O O . SER A 242 ? 1.1978 1.0510 1.1847 -0.0892 -0.1280 -0.0195 269 SER A O 1861 C CB . SER A 242 ? 1.0782 0.9217 1.0959 -0.0996 -0.1332 -0.0131 269 SER A CB 1862 O OG . SER A 242 ? 1.1440 0.9787 1.1699 -0.0989 -0.1403 -0.0191 269 SER A OG 1863 N N . PRO A 243 ? 1.1939 1.0606 1.1803 -0.0923 -0.1252 0.0051 270 PRO A N 1864 C CA . PRO A 243 ? 1.2204 1.0904 1.2172 -0.0982 -0.1278 0.0225 270 PRO A CA 1865 C C . PRO A 243 ? 1.2782 1.1393 1.2752 -0.0998 -0.1372 0.0251 270 PRO A C 1866 O O . PRO A 243 ? 1.3139 1.1706 1.2991 -0.0951 -0.1400 0.0155 270 PRO A O 1867 C CB . PRO A 243 ? 1.1926 1.0833 1.1806 -0.0935 -0.1190 0.0363 270 PRO A CB 1868 C CG . PRO A 243 ? 1.1522 1.0464 1.1184 -0.0825 -0.1157 0.0233 270 PRO A CG 1869 C CD . PRO A 243 ? 1.1906 1.0703 1.1603 -0.0836 -0.1181 0.0047 270 PRO A CD 1870 N N . MET A 244 ? 1.3192 1.1766 1.3312 -0.1066 -0.1436 0.0381 271 MET A N 1871 C CA . MET A 244 ? 1.2479 1.0956 1.2622 -0.1084 -0.1538 0.0417 271 MET A CA 1872 C C . MET A 244 ? 1.1724 1.0317 1.1713 -0.1032 -0.1506 0.0497 271 MET A C 1873 O O . MET A 244 ? 1.1856 1.0632 1.1804 -0.1007 -0.1426 0.0633 271 MET A O 1874 C CB . MET A 244 ? 1.2537 1.0949 1.2894 -0.1165 -0.1629 0.0558 271 MET A CB 1875 C CG . MET A 244 ? 1.2350 1.0569 1.2771 -0.1177 -0.1773 0.0504 271 MET A CG 1876 S SD . MET A 244 ? 1.7610 1.5684 1.8022 -0.1129 -0.1816 0.0268 271 MET A SD 1877 C CE . MET A 244 ? 1.4787 1.2676 1.5254 -0.1117 -0.1990 0.0251 271 MET A CE 1878 N N . PRO A 245 ? 1.0879 0.9387 1.0776 -0.1000 -0.1567 0.0416 272 PRO A N 1879 C CA . PRO A 245 ? 1.1564 1.0174 1.1284 -0.0928 -0.1547 0.0454 272 PRO A CA 1880 C C . PRO A 245 ? 1.1897 1.0544 1.1667 -0.0952 -0.1594 0.0644 272 PRO A C 1881 O O . PRO A 245 ? 1.1954 1.0459 1.1865 -0.1017 -0.1694 0.0674 272 PRO A O 1882 C CB . PRO A 245 ? 1.1310 0.9799 1.0937 -0.0888 -0.1601 0.0260 272 PRO A CB 1883 C CG . PRO A 245 ? 1.0968 0.9299 1.0752 -0.0948 -0.1667 0.0184 272 PRO A CG 1884 C CD . PRO A 245 ? 1.0489 0.8819 1.0435 -0.1012 -0.1658 0.0281 272 PRO A CD 1885 N N . TYR A 246 ? 1.1732 1.0578 1.1380 -0.0884 -0.1529 0.0775 273 TYR A N 1886 C CA . TYR A 246 ? 1.1543 1.0462 1.1225 -0.0891 -0.1564 0.0975 273 TYR A CA 1887 C C . TYR A 246 ? 1.1816 1.0618 1.1374 -0.0850 -0.1643 0.0863 273 TYR A C 1888 O O . TYR A 246 ? 1.2223 1.0999 1.1603 -0.0773 -0.1637 0.0675 273 TYR A O 1889 C CB . TYR A 246 ? 1.1069 1.0288 1.0644 -0.0802 -0.1456 0.1164 273 TYR A CB 1890 C CG . TYR A 246 ? 1.0490 0.9871 1.0255 -0.0860 -0.1390 0.1378 273 TYR A CG 1891 C CD1 . TYR A 246 ? 1.0496 0.9929 1.0511 -0.0955 -0.1435 0.1648 273 TYR A CD1 1892 C CD2 . TYR A 246 ? 1.0257 0.9741 0.9973 -0.0821 -0.1294 0.1320 273 TYR A CD2 1893 C CE1 . TYR A 246 ? 1.0535 1.0127 1.0765 -0.1017 -0.1389 0.1864 273 TYR A CE1 1894 C CE2 . TYR A 246 ? 1.0383 1.0032 1.0286 -0.0873 -0.1235 0.1525 273 TYR A CE2 1895 C CZ . TYR A 246 ? 1.0796 1.0503 1.0964 -0.0975 -0.1284 0.1801 273 TYR A CZ 1896 O OH . TYR A 246 ? 1.1789 1.1670 1.2182 -0.1037 -0.1238 0.2023 273 TYR A OH 1897 N N . VAL A 247 ? 1.0999 0.9727 1.0670 -0.0904 -0.1730 0.0982 274 VAL A N 1898 C CA . VAL A 247 ? 1.0061 0.8673 0.9637 -0.0872 -0.1813 0.0885 274 VAL A CA 1899 C C . VAL A 247 ? 1.0247 0.8986 0.9777 -0.0835 -0.1823 0.1082 274 VAL A C 1900 O O . VAL A 247 ? 1.0833 0.9586 1.0550 -0.0906 -0.1862 0.1297 274 VAL A O 1901 C CB . VAL A 247 ? 0.8914 0.7280 0.8650 -0.0949 -0.1934 0.0799 274 VAL A CB 1902 C CG1 . VAL A 247 ? 0.8667 0.6934 0.8289 -0.0901 -0.2004 0.0665 274 VAL A CG1 1903 C CG2 . VAL A 247 ? 0.8288 0.6565 0.8103 -0.0982 -0.1920 0.0654 274 VAL A CG2 1904 N N . LYS A 248 ? 0.9524 0.8353 0.8816 -0.0720 -0.1800 0.1011 275 LYS A N 1905 C CA . LYS A 248 ? 0.9182 0.8149 0.8396 -0.0659 -0.1805 0.1184 275 LYS A CA 1906 C C . LYS A 248 ? 1.0317 0.9149 0.9412 -0.0619 -0.1897 0.1040 275 LYS A C 1907 O O . LYS A 248 ? 1.0770 0.9470 0.9791 -0.0602 -0.1933 0.0802 275 LYS A O 1908 C CB . LYS A 248 ? 0.9309 0.8573 0.8316 -0.0515 -0.1689 0.1269 275 LYS A CB 1909 C CG . LYS A 248 ? 0.9664 0.8926 0.8394 -0.0380 -0.1684 0.1011 275 LYS A CG 1910 C CD . LYS A 248 ? 1.0115 0.9675 0.8607 -0.0197 -0.1590 0.1087 275 LYS A CD 1911 C CE . LYS A 248 ? 1.0465 0.9978 0.8687 -0.0051 -0.1629 0.0808 275 LYS A CE 1912 N NZ . LYS A 248 ? 1.1174 1.0970 0.9126 0.0167 -0.1557 0.0847 275 LYS A NZ 1913 N N . TRP A 249 ? 1.0743 0.9623 0.9844 -0.0606 -0.1938 0.1201 276 TRP A N 1914 C CA . TRP A 249 ? 1.0030 0.8819 0.9006 -0.0554 -0.2021 0.1090 276 TRP A CA 1915 C C . TRP A 249 ? 1.0317 0.9328 0.9036 -0.0396 -0.1975 0.1135 276 TRP A C 1916 O O . TRP A 249 ? 1.0288 0.9542 0.8979 -0.0340 -0.1893 0.1358 276 TRP A O 1917 C CB . TRP A 249 ? 0.9454 0.8100 0.8609 -0.0640 -0.2125 0.1210 276 TRP A CB 1918 C CG . TRP A 249 ? 0.8759 0.7141 0.8076 -0.0735 -0.2217 0.1064 276 TRP A CG 1919 C CD1 . TRP A 249 ? 0.8651 0.6916 0.8201 -0.0838 -0.2259 0.1131 276 TRP A CD1 1920 C CD2 . TRP A 249 ? 0.9571 0.7795 0.8829 -0.0716 -0.2286 0.0834 276 TRP A CD2 1921 N NE1 . TRP A 249 ? 0.9048 0.7097 0.8657 -0.0864 -0.2346 0.0945 276 TRP A NE1 1922 C CE2 . TRP A 249 ? 0.9013 0.7050 0.8453 -0.0792 -0.2355 0.0775 276 TRP A CE2 1923 C CE3 . TRP A 249 ? 1.1420 0.9653 1.0500 -0.0635 -0.2305 0.0680 276 TRP A CE3 1924 C CZ2 . TRP A 249 ? 0.9408 0.7306 0.8849 -0.0778 -0.2421 0.0585 276 TRP A CZ2 1925 C CZ3 . TRP A 249 ? 1.1860 0.9944 1.0976 -0.0645 -0.2378 0.0502 276 TRP A CZ3 1926 C CH2 . TRP A 249 ? 1.0811 0.8746 1.0102 -0.0711 -0.2425 0.0464 276 TRP A CH2 1927 N N . MET A 250 ? 1.0134 0.9074 0.8673 -0.0316 -0.2034 0.0928 277 MET A N 1928 C CA . MET A 250 ? 1.1540 1.0659 0.9807 -0.0142 -0.2021 0.0913 277 MET A CA 1929 C C . MET A 250 ? 1.1520 1.0540 0.9716 -0.0112 -0.2128 0.0839 277 MET A C 1930 O O . MET A 250 ? 1.2563 1.1363 1.0861 -0.0196 -0.2215 0.0690 277 MET A O 1931 C CB . MET A 250 ? 1.3896 1.3042 1.1975 -0.0033 -0.2004 0.0690 277 MET A CB 1932 C CG . MET A 250 ? 1.5059 1.4378 1.3119 0.0005 -0.1886 0.0768 277 MET A CG 1933 S SD . MET A 250 ? 1.1577 1.0991 0.9322 0.0219 -0.1887 0.0538 277 MET A SD 1934 C CE . MET A 250 ? 1.0527 0.9616 0.8336 0.0142 -0.2034 0.0220 277 MET A CE 1935 N N . LEU A 251 ? 1.0800 1.0006 0.8815 0.0022 -0.2118 0.0951 278 LEU A N 1936 C CA . LEU A 251 ? 1.0487 0.9634 0.8381 0.0087 -0.2218 0.0862 278 LEU A CA 1937 C C . LEU A 251 ? 1.0595 0.9845 0.8190 0.0281 -0.2241 0.0679 278 LEU A C 1938 O O . LEU A 251 ? 1.0264 0.9749 0.7647 0.0450 -0.2202 0.0784 278 LEU A O 1939 C CB . LEU A 251 ? 0.9813 0.9080 0.7732 0.0100 -0.2212 0.1125 278 LEU A CB 1940 C CG . LEU A 251 ? 0.9913 0.9104 0.7735 0.0151 -0.2318 0.1053 278 LEU A CG 1941 C CD1 . LEU A 251 ? 0.9730 0.8628 0.7706 0.0022 -0.2422 0.0861 278 LEU A CD1 1942 C CD2 . LEU A 251 ? 1.0040 0.9348 0.7921 0.0151 -0.2307 0.1343 278 LEU A CD2 1943 N N . GLY A 252 ? 1.2172 1.1250 0.9760 0.0266 -0.2315 0.0412 279 GLY A N 1944 C CA . GLY A 252 ? 1.2463 1.1590 0.9805 0.0441 -0.2369 0.0210 279 GLY A CA 1945 C C . GLY A 252 ? 1.2803 1.2112 1.0028 0.0542 -0.2261 0.0252 279 GLY A C 1946 O O . GLY A 252 ? 1.2537 1.1770 0.9897 0.0446 -0.2217 0.0206 279 GLY A O 1947 N N . ALA A 253 ? 1.3374 1.2944 1.0344 0.0748 -0.2215 0.0350 280 ALA A N 1948 C CA . ALA A 253 ? 1.3197 1.2990 1.0020 0.0888 -0.2109 0.0399 280 ALA A CA 1949 C C . ALA A 253 ? 1.3927 1.3932 1.0907 0.0810 -0.1947 0.0739 280 ALA A C 1950 O O . ALA A 253 ? 1.3805 1.3891 1.0846 0.0788 -0.1852 0.0792 280 ALA A O 1951 C CB . ALA A 253 ? 1.2524 1.2526 0.8971 0.1190 -0.2146 0.0325 280 ALA A CB 1952 N N . GLU A 254 ? 1.4448 1.4541 1.1512 0.0765 -0.1928 0.0975 281 GLU A N 1953 C CA . GLU A 254 ? 1.4252 1.4553 1.1505 0.0688 -0.1800 0.1332 281 GLU A CA 1954 C C . GLU A 254 ? 1.3054 1.3152 1.0647 0.0436 -0.1784 0.1367 281 GLU A C 1955 O O . GLU A 254 ? 1.2911 1.2700 1.0651 0.0284 -0.1879 0.1202 281 GLU A O 1956 C CB . GLU A 254 ? 1.4881 1.5271 1.2190 0.0677 -0.1815 0.1571 281 GLU A CB 1957 C CG . GLU A 254 ? 1.5349 1.5929 1.2927 0.0569 -0.1714 0.1966 281 GLU A CG 1958 C CD . GLU A 254 ? 1.5590 1.6114 1.3343 0.0469 -0.1773 0.2169 281 GLU A CD 1959 O OE1 . GLU A 254 ? 1.6309 1.6837 1.3873 0.0580 -0.1836 0.2099 281 GLU A OE1 1960 O OE2 . GLU A 254 ? 1.4807 1.5276 1.2894 0.0282 -0.1769 0.2395 281 GLU A OE2 1961 N N . ASP A 255 ? 1.3025 1.3317 1.0739 0.0408 -0.1665 0.1584 282 ASP A N 1962 C CA . ASP A 255 ? 1.3370 1.3503 1.1426 0.0177 -0.1656 0.1671 282 ASP A CA 1963 C C . ASP A 255 ? 1.4539 1.4677 1.2857 0.0047 -0.1681 0.1965 282 ASP A C 1964 O O . ASP A 255 ? 1.5270 1.5697 1.3573 0.0131 -0.1620 0.2250 282 ASP A O 1965 C CB . ASP A 255 ? 1.2724 1.3057 1.0824 0.0196 -0.1532 0.1777 282 ASP A CB 1966 C CG . ASP A 255 ? 1.2486 1.2767 1.0367 0.0305 -0.1525 0.1477 282 ASP A CG 1967 O OD1 . ASP A 255 ? 1.2824 1.3359 1.0429 0.0529 -0.1465 0.1465 282 ASP A OD1 1968 O OD2 . ASP A 255 ? 1.2636 1.2630 1.0623 0.0179 -0.1585 0.1257 282 ASP A OD2 1969 N N . LEU A 256 ? 1.4553 1.4376 1.3112 -0.0145 -0.1780 0.1898 283 LEU A N 1970 C CA . LEU A 256 ? 1.4466 1.4232 1.3303 -0.0278 -0.1839 0.2151 283 LEU A CA 1971 C C . LEU A 256 ? 1.4863 1.4704 1.3999 -0.0403 -0.1792 0.2383 283 LEU A C 1972 O O . LEU A 256 ? 1.4961 1.5012 1.4271 -0.0425 -0.1761 0.2728 283 LEU A O 1973 C CB . LEU A 256 ? 1.3878 1.3273 1.2819 -0.0395 -0.1985 0.1960 283 LEU A CB 1974 C CG . LEU A 256 ? 1.3670 1.2971 1.2349 -0.0290 -0.2041 0.1699 283 LEU A CG 1975 C CD1 . LEU A 256 ? 1.3820 1.2796 1.2624 -0.0399 -0.2175 0.1542 283 LEU A CD1 1976 C CD2 . LEU A 256 ? 1.3625 1.3159 1.2114 -0.0141 -0.2019 0.1845 283 LEU A CD2 1977 N N . THR A 257 ? 1.5038 1.4714 1.4246 -0.0484 -0.1791 0.2203 284 THR A N 1978 C CA . THR A 257 ? 1.4508 1.4243 1.3984 -0.0596 -0.1753 0.2380 284 THR A CA 1979 C C . THR A 257 ? 1.4563 1.4710 1.3955 -0.0476 -0.1595 0.2601 284 THR A C 1980 O O . THR A 257 ? 1.4401 1.4669 1.3515 -0.0331 -0.1508 0.2431 284 THR A O 1981 C CB . THR A 257 ? 1.3685 1.3183 1.3203 -0.0674 -0.1773 0.2112 284 THR A CB 1982 O OG1 . THR A 257 ? 1.3712 1.2883 1.3218 -0.0724 -0.1896 0.1865 284 THR A OG1 1983 C CG2 . THR A 257 ? 1.3854 1.3332 1.3705 -0.0820 -0.1785 0.2288 284 THR A CG2 1984 N N . PRO A 258 ? 1.4219 1.4593 1.3862 -0.0527 -0.1567 0.2988 285 PRO A N 1985 C CA . PRO A 258 ? 1.4399 1.5212 1.4001 -0.0411 -0.1407 0.3239 285 PRO A CA 1986 C C . PRO A 258 ? 1.5069 1.5872 1.4675 -0.0431 -0.1340 0.3099 285 PRO A C 1987 O O . PRO A 258 ? 1.5110 1.5621 1.4933 -0.0601 -0.1423 0.2986 285 PRO A O 1988 C CB . PRO A 258 ? 1.3686 1.4670 1.3683 -0.0529 -0.1428 0.3691 285 PRO A CB 1989 C CG . PRO A 258 ? 1.3535 1.4088 1.3820 -0.0741 -0.1617 0.3619 285 PRO A CG 1990 C CD . PRO A 258 ? 1.3807 1.4048 1.3808 -0.0692 -0.1692 0.3224 285 PRO A CD 1991 N N . GLU A 259 ? 1.6003 1.7122 1.5354 -0.0242 -0.1197 0.3098 286 GLU A N 1992 C CA . GLU A 259 ? 1.6372 1.7462 1.5642 -0.0223 -0.1135 0.2899 286 GLU A CA 1993 C C . GLU A 259 ? 1.5925 1.7035 1.5569 -0.0397 -0.1120 0.3095 286 GLU A C 1994 O O . GLU A 259 ? 1.5579 1.6437 1.5294 -0.0499 -0.1158 0.2880 286 GLU A O 1995 C CB . GLU A 259 ? 1.7581 1.9037 1.6498 0.0045 -0.0995 0.2887 286 GLU A CB 1996 C CG . GLU A 259 ? 1.8016 1.9360 1.6745 0.0107 -0.0966 0.2568 286 GLU A CG 1997 C CD . GLU A 259 ? 1.8668 2.0423 1.7148 0.0352 -0.0821 0.2644 286 GLU A CD 1998 O OE1 . GLU A 259 ? 1.8583 2.0529 1.7226 0.0318 -0.0728 0.2814 286 GLU A OE1 1999 O OE2 . GLU A 259 ? 1.9067 2.0956 1.7184 0.0592 -0.0809 0.2526 286 GLU A OE2 2000 N N . ASP A 260 ? 1.6420 1.7841 1.6320 -0.0429 -0.1072 0.3515 287 ASP A N 2001 C CA . ASP A 260 ? 1.6392 1.7905 1.6656 -0.0572 -0.1052 0.3742 287 ASP A CA 2002 C C . ASP A 260 ? 1.5087 1.6222 1.5750 -0.0830 -0.1233 0.3756 287 ASP A C 2003 O O . ASP A 260 ? 1.4940 1.6075 1.5934 -0.0969 -0.1260 0.3906 287 ASP A O 2004 C CB . ASP A 260 ? 1.7564 1.9605 1.7977 -0.0498 -0.0930 0.4220 287 ASP A CB 2005 C CG . ASP A 260 ? 1.8697 2.1145 1.8690 -0.0201 -0.0754 0.4207 287 ASP A CG 2006 O OD1 . ASP A 260 ? 1.9415 2.2293 1.9399 -0.0070 -0.0663 0.4548 287 ASP A OD1 2007 O OD2 . ASP A 260 ? 1.8884 2.1225 1.8555 -0.0087 -0.0717 0.3855 287 ASP A OD2 2008 N N . ASP A 261 ? 1.4755 1.5568 1.5380 -0.0879 -0.1369 0.3594 288 ASP A N 2009 C CA . ASP A 261 ? 1.4369 1.4769 1.5289 -0.1079 -0.1560 0.3514 288 ASP A CA 2010 C C . ASP A 261 ? 1.3767 1.3791 1.4431 -0.1057 -0.1634 0.3073 288 ASP A C 2011 O O . ASP A 261 ? 1.4275 1.4139 1.4850 -0.1041 -0.1719 0.2991 288 ASP A O 2012 C CB . ASP A 261 ? 1.5018 1.5400 1.6236 -0.1177 -0.1684 0.3817 288 ASP A CB 2013 C CG . ASP A 261 ? 1.5979 1.5906 1.7468 -0.1351 -0.1911 0.3698 288 ASP A CG 2014 O OD1 . ASP A 261 ? 1.6340 1.6087 1.7871 -0.1378 -0.2037 0.3710 288 ASP A OD1 2015 O OD2 . ASP A 261 ? 1.6324 1.6077 1.7969 -0.1445 -0.1967 0.3584 288 ASP A OD2 2016 N N . MET A 262 ? 1.2671 1.2574 1.3232 -0.1053 -0.1599 0.2808 289 MET A N 2017 C CA . MET A 262 ? 1.2230 1.1853 1.2543 -0.1011 -0.1639 0.2414 289 MET A CA 2018 C C . MET A 262 ? 1.2833 1.2175 1.3302 -0.1124 -0.1719 0.2225 289 MET A C 2019 O O . MET A 262 ? 1.3084 1.2512 1.3592 -0.1134 -0.1644 0.2212 289 MET A O 2020 C CB . MET A 262 ? 1.1441 1.1246 1.1384 -0.0834 -0.1500 0.2248 289 MET A CB 2021 C CG . MET A 262 ? 1.1034 1.0590 1.0739 -0.0784 -0.1546 0.1880 289 MET A CG 2022 S SD . MET A 262 ? 1.2939 1.2695 1.2240 -0.0568 -0.1427 0.1705 289 MET A SD 2023 C CE . MET A 262 ? 1.3178 1.3221 1.2330 -0.0429 -0.1393 0.1940 289 MET A CE 2024 N N . PRO A 263 ? 1.2854 1.1872 1.3401 -0.1191 -0.1873 0.2075 290 PRO A N 2025 C CA . PRO A 263 ? 1.3007 1.1756 1.3717 -0.1281 -0.1978 0.1916 290 PRO A CA 2026 C C . PRO A 263 ? 1.2713 1.1409 1.3228 -0.1224 -0.1900 0.1624 290 PRO A C 2027 O O . PRO A 263 ? 1.3287 1.2066 1.3533 -0.1121 -0.1809 0.1488 290 PRO A O 2028 C CB . PRO A 263 ? 1.2730 1.1199 1.3493 -0.1308 -0.2150 0.1828 290 PRO A CB 2029 C CG . PRO A 263 ? 1.2312 1.0868 1.2819 -0.1210 -0.2097 0.1792 290 PRO A CG 2030 C CD . PRO A 263 ? 1.2345 1.1250 1.2796 -0.1158 -0.1955 0.2036 290 PRO A CD 2031 N N . ILE A 264 ? 1.1725 1.0278 1.2390 -0.1288 -0.1950 0.1534 291 ILE A N 2032 C CA . ILE A 264 ? 1.1559 1.0051 1.2081 -0.1244 -0.1889 0.1274 291 ILE A CA 2033 C C . ILE A 264 ? 1.3189 1.1411 1.3703 -0.1239 -0.2009 0.1048 291 ILE A C 2034 O O . ILE A 264 ? 1.3730 1.1774 1.4424 -0.1291 -0.2158 0.1076 291 ILE A O 2035 C CB . ILE A 264 ? 1.0995 0.9551 1.1663 -0.1294 -0.1842 0.1317 291 ILE A CB 2036 C CG1 . ILE A 264 ? 1.0174 0.9038 1.0755 -0.1248 -0.1677 0.1464 291 ILE A CG1 2037 C CG2 . ILE A 264 ? 1.0832 0.9253 1.1427 -0.1269 -0.1833 0.1052 291 ILE A CG2 2038 C CD1 . ILE A 264 ? 0.8566 0.7507 0.9229 -0.1272 -0.1606 0.1459 291 ILE A CD1 2039 N N . GLY A 265 ? 1.4624 1.2827 1.4937 -0.1166 -0.1953 0.0833 292 GLY A N 2040 C CA . GLY A 265 ? 1.4608 1.2622 1.4917 -0.1143 -0.2032 0.0627 292 GLY A CA 2041 C C . GLY A 265 ? 1.4849 1.2710 1.5167 -0.1128 -0.2164 0.0600 292 GLY A C 2042 O O . GLY A 265 ? 1.5121 1.2869 1.5403 -0.1080 -0.2217 0.0432 292 GLY A O 2043 N N . ARG A 266 ? 1.2211 1.0086 1.2583 -0.1159 -0.2216 0.0778 293 ARG A N 2044 C CA . ARG A 266 ? 1.1324 0.9051 1.1707 -0.1142 -0.2348 0.0765 293 ARG A CA 2045 C C . ARG A 266 ? 1.0788 0.8601 1.1187 -0.1166 -0.2358 0.0981 293 ARG A C 2046 O O . ARG A 266 ? 1.1036 0.8929 1.1595 -0.1232 -0.2360 0.1201 293 ARG A O 2047 C CB . ARG A 266 ? 1.2055 0.9562 1.2625 -0.1165 -0.2518 0.0728 293 ARG A CB 2048 C CG . ARG A 266 ? 1.2490 0.9822 1.3048 -0.1118 -0.2666 0.0665 293 ARG A CG 2049 C CD . ARG A 266 ? 1.2776 0.9885 1.3475 -0.1098 -0.2844 0.0573 293 ARG A CD 2050 N NE . ARG A 266 ? 1.3424 1.0352 1.4171 -0.1069 -0.3022 0.0585 293 ARG A NE 2051 C CZ . ARG A 266 ? 1.4680 1.1530 1.5605 -0.1145 -0.3140 0.0781 293 ARG A CZ 2052 N NH1 . ARG A 266 ? 1.5019 1.1987 1.6099 -0.1252 -0.3087 0.0997 293 ARG A NH1 2053 N NH2 . ARG A 266 ? 1.5253 1.1922 1.6215 -0.1109 -0.3311 0.0775 293 ARG A NH2 2054 N N . ASN A 267 ? 1.0580 0.8395 1.0824 -0.1108 -0.2364 0.0932 294 ASN A N 2055 C CA . ASN A 267 ? 1.1497 0.9395 1.1732 -0.1110 -0.2378 0.1126 294 ASN A CA 2056 C C . ASN A 267 ? 1.3048 1.0792 1.3232 -0.1072 -0.2493 0.1045 294 ASN A C 2057 O O . ASN A 267 ? 1.3605 1.1339 1.3617 -0.1003 -0.2469 0.0863 294 ASN A O 2058 C CB . ASN A 267 ? 1.1741 0.9894 1.1774 -0.1047 -0.2222 0.1173 294 ASN A CB 2059 C CG . ASN A 267 ? 1.2777 1.1077 1.2802 -0.1033 -0.2216 0.1411 294 ASN A CG 2060 O OD1 . ASN A 267 ? 1.3163 1.1353 1.3245 -0.1045 -0.2325 0.1469 294 ASN A OD1 2061 N ND2 . ASN A 267 ? 1.2816 1.1383 1.2764 -0.0990 -0.2087 0.1557 294 ASN A ND2 2062 N N . VAL A 268 ? 1.3732 1.1356 1.4088 -0.1117 -0.2631 0.1188 295 VAL A N 2063 C CA . VAL A 268 ? 1.3782 1.1264 1.4095 -0.1075 -0.2747 0.1134 295 VAL A CA 2064 C C . VAL A 268 ? 1.4502 1.2117 1.4782 -0.1074 -0.2727 0.1346 295 VAL A C 2065 O O . VAL A 268 ? 1.5092 1.2759 1.5557 -0.1140 -0.2759 0.1599 295 VAL A O 2066 C CB . VAL A 268 ? 1.3551 1.0762 1.4063 -0.1100 -0.2952 0.1107 295 VAL A CB 2067 C CG1 . VAL A 268 ? 1.3289 1.0469 1.4083 -0.1206 -0.3028 0.1331 295 VAL A CG1 2068 C CG2 . VAL A 268 ? 1.3631 1.0711 1.4106 -0.1052 -0.3077 0.1093 295 VAL A CG2 2069 N N . LEU A 269 ? 1.4922 1.2611 1.4976 -0.0993 -0.2674 0.1251 296 LEU A N 2070 C CA . LEU A 269 ? 1.5386 1.3208 1.5363 -0.0960 -0.2655 0.1418 296 LEU A CA 2071 C C . LEU A 269 ? 1.5549 1.3186 1.5634 -0.0974 -0.2821 0.1479 296 LEU A C 2072 O O . LEU A 269 ? 1.5676 1.3141 1.5703 -0.0931 -0.2909 0.1290 296 LEU A O 2073 C CB . LEU A 269 ? 1.5565 1.3521 1.5257 -0.0859 -0.2558 0.1270 296 LEU A CB 2074 C CG . LEU A 269 ? 1.5888 1.4009 1.5445 -0.0792 -0.2529 0.1414 296 LEU A CG 2075 C CD1 . LEU A 269 ? 1.6192 1.4531 1.5840 -0.0813 -0.2455 0.1714 296 LEU A CD1 2076 C CD2 . LEU A 269 ? 1.5837 1.4073 1.5118 -0.0684 -0.2454 0.1234 296 LEU A CD2 2077 N N . GLU A 270 ? 1.4919 1.2607 1.5177 -0.1029 -0.2863 0.1762 297 GLU A N 2078 C CA . GLU A 270 ? 1.5153 1.2681 1.5545 -0.1048 -0.3027 0.1874 297 GLU A CA 2079 C C . GLU A 270 ? 1.5638 1.3325 1.5848 -0.0973 -0.2973 0.1957 297 GLU A C 2080 O O . GLU A 270 ? 1.5705 1.3652 1.5892 -0.0961 -0.2866 0.2182 297 GLU A O 2081 C CB . GLU A 270 ? 1.5784 1.3279 1.6518 -0.1160 -0.3124 0.2165 297 GLU A CB 2082 C CG . GLU A 270 ? 1.5931 1.3266 1.6868 -0.1235 -0.3199 0.2097 297 GLU A CG 2083 C CD . GLU A 270 ? 1.5765 1.3140 1.7060 -0.1356 -0.3269 0.2421 297 GLU A CD 2084 O OE1 . GLU A 270 ? 1.6113 1.3772 1.7450 -0.1374 -0.3156 0.2707 297 GLU A OE1 2085 O OE2 . GLU A 270 ? 1.4968 1.2101 1.6510 -0.1423 -0.3443 0.2397 297 GLU A OE2 2086 N N . LEU A 271 ? 1.6039 1.3589 1.6115 -0.0908 -0.3047 0.1782 298 LEU A N 2087 C CA . LEU A 271 ? 1.5998 1.3679 1.5892 -0.0829 -0.3013 0.1832 298 LEU A CA 2088 C C . LEU A 271 ? 1.7585 1.5104 1.7615 -0.0845 -0.3176 0.1960 298 LEU A C 2089 O O . LEU A 271 ? 1.8068 1.5325 1.8165 -0.0846 -0.3323 0.1815 298 LEU A O 2090 C CB . LEU A 271 ? 1.4118 1.1805 1.3746 -0.0736 -0.2964 0.1542 298 LEU A CB 2091 C CG . LEU A 271 ? 1.2910 1.0769 1.2384 -0.0705 -0.2811 0.1422 298 LEU A CG 2092 C CD1 . LEU A 271 ? 1.3113 1.0933 1.2406 -0.0636 -0.2805 0.1142 298 LEU A CD1 2093 C CD2 . LEU A 271 ? 1.1889 1.0035 1.1242 -0.0652 -0.2689 0.1605 298 LEU A CD2 2094 N N . ASN A 272 ? 1.8171 1.5859 1.8239 -0.0843 -0.3153 0.2238 299 ASN A N 2095 C CA . ASN A 272 ? 1.8366 1.5915 1.8599 -0.0868 -0.3310 0.2406 299 ASN A CA 2096 C C . ASN A 272 ? 1.8018 1.5714 1.8047 -0.0771 -0.3271 0.2461 299 ASN A C 2097 O O . ASN A 272 ? 1.7923 1.5909 1.7751 -0.0696 -0.3114 0.2512 299 ASN A O 2098 C CB . ASN A 272 ? 1.9203 1.6798 1.9775 -0.0979 -0.3359 0.2760 299 ASN A CB 2099 C CG . ASN A 272 ? 2.0161 1.8155 2.0686 -0.0958 -0.3168 0.3019 299 ASN A CG 2100 O OD1 . ASN A 272 ? 2.0518 1.8730 2.0739 -0.0854 -0.3005 0.2899 299 ASN A OD1 2101 N ND2 . ASN A 272 ? 2.0517 1.8617 2.1356 -0.1049 -0.3197 0.3380 299 ASN A ND2 2102 N N . ASP A 273 ? 1.7670 1.5162 1.7745 -0.0758 -0.3425 0.2443 300 ASP A N 2103 C CA . ASP A 273 ? 1.7322 1.4924 1.7227 -0.0668 -0.3415 0.2499 300 ASP A CA 2104 C C . ASP A 273 ? 1.7139 1.4925 1.6696 -0.0555 -0.3273 0.2282 300 ASP A C 2105 O O . ASP A 273 ? 1.7429 1.5489 1.6823 -0.0478 -0.3160 0.2402 300 ASP A O 2106 C CB . ASP A 273 ? 1.7101 1.4930 1.7140 -0.0688 -0.3378 0.2896 300 ASP A CB 2107 C CG . ASP A 273 ? 1.6897 1.4814 1.6794 -0.0596 -0.3394 0.2979 300 ASP A CG 2108 O OD1 . ASP A 273 ? 1.6968 1.4647 1.6836 -0.0573 -0.3528 0.2823 300 ASP A OD1 2109 O OD2 . ASP A 273 ? 1.6748 1.4990 1.6550 -0.0530 -0.3271 0.3199 300 ASP A OD2 2110 N N . VAL A 274 ? 1.6692 1.4335 1.6147 -0.0535 -0.3289 0.1968 301 VAL A N 2111 C CA . VAL A 274 ? 1.6250 1.4032 1.5427 -0.0443 -0.3188 0.1751 301 VAL A CA 2112 C C . VAL A 274 ? 1.6384 1.4243 1.5387 -0.0345 -0.3212 0.1760 301 VAL A C 2113 O O . VAL A 274 ? 1.6637 1.4340 1.5705 -0.0343 -0.3335 0.1777 301 VAL A O 2114 C CB . VAL A 274 ? 1.5939 1.3554 1.5094 -0.0447 -0.3220 0.1448 301 VAL A CB 2115 C CG1 . VAL A 274 ? 1.5830 1.3584 1.4750 -0.0365 -0.3139 0.1247 301 VAL A CG1 2116 C CG2 . VAL A 274 ? 1.5521 1.3063 1.4837 -0.0532 -0.3197 0.1432 301 VAL A CG2 2117 N N . ARG A 275 ? 1.6227 1.4326 1.5002 -0.0252 -0.3106 0.1742 302 ARG A N 2118 C CA . ARG A 275 ? 1.6378 1.4583 1.4970 -0.0144 -0.3126 0.1762 302 ARG A CA 2119 C C . ARG A 275 ? 1.5791 1.4000 1.4173 -0.0064 -0.3130 0.1466 302 ARG A C 2120 O O . ARG A 275 ? 1.5294 1.3398 1.3643 -0.0035 -0.3222 0.1355 302 ARG A O 2121 C CB . ARG A 275 ? 1.7695 1.6200 1.6188 -0.0068 -0.3023 0.2013 302 ARG A CB 2122 C CG . ARG A 275 ? 1.9170 1.7817 1.7457 0.0065 -0.3039 0.2054 302 ARG A CG 2123 C CD . ARG A 275 ? 2.0019 1.8892 1.8005 0.0213 -0.2952 0.1917 302 ARG A CD 2124 N NE . ARG A 275 ? 2.0687 1.9766 1.8466 0.0366 -0.2949 0.2020 302 ARG A NE 2125 C CZ . ARG A 275 ? 2.1109 2.0427 1.8604 0.0538 -0.2888 0.1954 302 ARG A CZ 2126 N NH1 . ARG A 275 ? 2.1123 2.0488 1.8519 0.0568 -0.2830 0.1787 302 ARG A NH1 2127 N NH2 . ARG A 275 ? 2.1259 2.0765 1.8562 0.0691 -0.2895 0.2050 302 ARG A NH2 2128 N N . GLN A 276 ? 1.6399 1.4729 1.4658 -0.0029 -0.3042 0.1346 303 GLN A N 2129 C CA . GLN A 276 ? 1.6764 1.5089 1.4871 0.0033 -0.3065 0.1074 303 GLN A CA 2130 C C . GLN A 276 ? 1.6519 1.4746 1.4724 -0.0044 -0.3039 0.0901 303 GLN A C 2131 O O . GLN A 276 ? 1.6325 1.4528 1.4660 -0.0122 -0.2982 0.0987 303 GLN A O 2132 C CB . GLN A 276 ? 1.7670 1.6224 1.5515 0.0179 -0.3017 0.1059 303 GLN A CB 2133 C CG . GLN A 276 ? 1.9144 1.7680 1.6842 0.0257 -0.3091 0.0797 303 GLN A CG 2134 C CD . GLN A 276 ? 2.0836 1.9577 1.8257 0.0432 -0.3087 0.0786 303 GLN A CD 2135 O OE1 . GLN A 276 ? 2.1646 2.0555 1.8970 0.0512 -0.3037 0.0997 303 GLN A OE1 2136 N NE2 . GLN A 276 ? 2.1172 1.9906 1.8472 0.0503 -0.3150 0.0545 303 GLN A NE2 2137 N N . SER A 277 ? 1.5859 1.4039 1.4023 -0.0023 -0.3086 0.0671 304 SER A N 2138 C CA . SER A 277 ? 1.4767 1.2884 1.3024 -0.0084 -0.3061 0.0512 304 SER A CA 2139 C C . SER A 277 ? 1.4899 1.3138 1.3067 -0.0062 -0.2964 0.0512 304 SER A C 2140 O O . SER A 277 ? 1.5710 1.4106 1.3696 0.0037 -0.2930 0.0576 304 SER A O 2141 C CB . SER A 277 ? 1.4181 1.2264 1.2432 -0.0059 -0.3140 0.0304 304 SER A CB 2142 O OG . SER A 277 ? 1.4187 1.2192 1.2499 -0.0057 -0.3226 0.0310 304 SER A OG 2143 N N . ALA A 278 ? 1.4635 1.2816 1.2921 -0.0137 -0.2919 0.0439 305 ALA A N 2144 C CA . ALA A 278 ? 1.4492 1.2780 1.2705 -0.0116 -0.2828 0.0430 305 ALA A CA 2145 C C . ALA A 278 ? 1.4275 1.2485 1.2608 -0.0186 -0.2805 0.0285 305 ALA A C 2146 O O . ALA A 278 ? 1.4207 1.2302 1.2722 -0.0278 -0.2809 0.0286 305 ALA A O 2147 C CB . ALA A 278 ? 1.4619 1.2997 1.2857 -0.0135 -0.2743 0.0668 305 ALA A CB 2148 N N . ASN A 279 ? 1.3887 1.2165 1.2109 -0.0128 -0.2792 0.0156 306 ASN A N 2149 C CA . ASN A 279 ? 1.2677 1.0924 1.0984 -0.0178 -0.2747 0.0056 306 ASN A CA 2150 C C . ASN A 279 ? 1.1344 0.9662 0.9661 -0.0205 -0.2630 0.0204 306 ASN A C 2151 O O . ASN A 279 ? 1.0767 0.9233 0.8930 -0.0121 -0.2579 0.0310 306 ASN A O 2152 C CB . ASN A 279 ? 1.4112 1.2399 1.2292 -0.0091 -0.2794 -0.0120 306 ASN A CB 2153 C CG . ASN A 279 ? 1.5606 1.3798 1.3907 -0.0123 -0.2907 -0.0283 306 ASN A CG 2154 O OD1 . ASN A 279 ? 1.6952 1.5092 1.5401 -0.0186 -0.2906 -0.0370 306 ASN A OD1 2155 N ND2 . ASN A 279 ? 1.5486 1.3672 1.3740 -0.0076 -0.3005 -0.0308 306 ASN A ND2 2156 N N . TYR A 280 ? 1.1313 0.9549 0.9813 -0.0310 -0.2589 0.0221 307 TYR A N 2157 C CA . TYR A 280 ? 1.0538 0.8840 0.9083 -0.0347 -0.2490 0.0366 307 TYR A CA 2158 C C . TYR A 280 ? 1.1783 1.0068 1.0393 -0.0388 -0.2431 0.0267 307 TYR A C 2159 O O . TYR A 280 ? 1.2866 1.1034 1.1640 -0.0469 -0.2447 0.0205 307 TYR A O 2160 C CB . TYR A 280 ? 0.9603 0.7815 0.8326 -0.0438 -0.2509 0.0525 307 TYR A CB 2161 C CG . TYR A 280 ? 1.0683 0.8973 0.9367 -0.0408 -0.2520 0.0732 307 TYR A CG 2162 C CD1 . TYR A 280 ? 1.1925 1.0132 1.0618 -0.0399 -0.2614 0.0747 307 TYR A CD1 2163 C CD2 . TYR A 280 ? 1.1053 0.9522 0.9705 -0.0384 -0.2434 0.0932 307 TYR A CD2 2164 C CE1 . TYR A 280 ? 1.2056 1.0337 1.0729 -0.0373 -0.2627 0.0953 307 TYR A CE1 2165 C CE2 . TYR A 280 ? 1.1332 0.9903 0.9976 -0.0355 -0.2440 0.1158 307 TYR A CE2 2166 C CZ . TYR A 280 ? 1.1543 1.0011 1.0199 -0.0353 -0.2539 0.1165 307 TYR A CZ 2167 O OH . TYR A 280 ? 1.0590 0.9161 0.9254 -0.0327 -0.2550 0.1402 307 TYR A OH 2168 N N . THR A 281 ? 1.1791 1.0205 1.0269 -0.0320 -0.2363 0.0258 308 THR A N 2169 C CA . THR A 281 ? 1.1533 0.9926 1.0065 -0.0350 -0.2315 0.0151 308 THR A CA 2170 C C . THR A 281 ? 1.1813 1.0220 1.0488 -0.0436 -0.2229 0.0287 308 THR A C 2171 O O . THR A 281 ? 1.1316 0.9830 0.9987 -0.0432 -0.2180 0.0481 308 THR A O 2172 C CB . THR A 281 ? 1.1470 0.9978 0.9795 -0.0224 -0.2295 0.0059 308 THR A CB 2173 O OG1 . THR A 281 ? 1.1922 1.0449 1.0080 -0.0116 -0.2385 -0.0022 308 THR A OG1 2174 C CG2 . THR A 281 ? 1.0855 0.9283 0.9251 -0.0254 -0.2300 -0.0113 308 THR A CG2 2175 N N . CYS A 282 ? 1.3355 1.1667 1.2173 -0.0511 -0.2217 0.0196 309 CYS A N 2176 C CA . CYS A 282 ? 0.8413 0.6733 0.7364 -0.0585 -0.2146 0.0296 309 CYS A CA 2177 C C . CYS A 282 ? 1.0868 0.9234 0.9790 -0.0569 -0.2077 0.0196 309 CYS A C 2178 O O . CYS A 282 ? 1.1163 0.9446 1.0131 -0.0583 -0.2104 0.0037 309 CYS A O 2179 C CB . CYS A 282 ? 0.8280 0.6442 0.7432 -0.0677 -0.2199 0.0289 309 CYS A CB 2180 S SG . CYS A 282 ? 1.2004 1.0145 1.1330 -0.0761 -0.2140 0.0352 309 CYS A SG 2181 N N . VAL A 283 ? 1.0346 0.8858 0.9207 -0.0536 -0.1988 0.0307 310 VAL A N 2182 C CA . VAL A 283 ? 0.9869 0.8438 0.8676 -0.0500 -0.1923 0.0215 310 VAL A CA 2183 C C . VAL A 283 ? 0.9339 0.7911 0.8311 -0.0589 -0.1852 0.0298 310 VAL A C 2184 O O . VAL A 283 ? 0.9700 0.8355 0.8753 -0.0627 -0.1813 0.0494 310 VAL A O 2185 C CB . VAL A 283 ? 1.0530 0.9293 0.9102 -0.0354 -0.1873 0.0250 310 VAL A CB 2186 C CG1 . VAL A 283 ? 0.9894 0.8697 0.8402 -0.0302 -0.1822 0.0136 310 VAL A CG1 2187 C CG2 . VAL A 283 ? 1.0445 0.9200 0.8838 -0.0249 -0.1961 0.0153 310 VAL A CG2 2188 N N . ALA A 284 ? 0.9625 0.8113 0.8669 -0.0624 -0.1845 0.0157 311 ALA A N 2189 C CA . ALA A 284 ? 1.0041 0.8539 0.9217 -0.0689 -0.1777 0.0202 311 ALA A CA 2190 C C . ALA A 284 ? 0.9769 0.8363 0.8831 -0.0618 -0.1706 0.0127 311 ALA A C 2191 O O . ALA A 284 ? 0.9612 0.8156 0.8594 -0.0565 -0.1744 -0.0041 311 ALA A O 2192 C CB . ALA A 284 ? 1.0475 0.8817 0.9824 -0.0770 -0.1822 0.0111 311 ALA A CB 2193 N N . MET A 285 ? 1.0209 0.8942 0.9281 -0.0614 -0.1615 0.0256 312 MET A N 2194 C CA . MET A 285 ? 1.0538 0.9369 0.9494 -0.0533 -0.1546 0.0187 312 MET A CA 2195 C C . MET A 285 ? 0.9775 0.8649 0.8873 -0.0600 -0.1465 0.0257 312 MET A C 2196 O O . MET A 285 ? 0.9154 0.8102 0.8380 -0.0665 -0.1431 0.0446 312 MET A O 2197 C CB . MET A 285 ? 1.0127 0.9169 0.8857 -0.0383 -0.1502 0.0265 312 MET A CB 2198 C CG . MET A 285 ? 0.9061 0.8231 0.7801 -0.0384 -0.1490 0.0491 312 MET A CG 2199 S SD . MET A 285 ? 1.8421 1.7874 1.6851 -0.0159 -0.1437 0.0558 312 MET A SD 2200 C CE . MET A 285 ? 1.3810 1.3394 1.2316 -0.0192 -0.1434 0.0846 312 MET A CE 2201 N N . SER A 286 ? 1.0199 0.9021 0.9293 -0.0588 -0.1447 0.0109 313 SER A N 2202 C CA . SER A 286 ? 1.0829 0.9720 1.0011 -0.0621 -0.1361 0.0160 313 SER A CA 2203 C C . SER A 286 ? 1.0884 0.9899 0.9875 -0.0486 -0.1306 0.0091 313 SER A C 2204 O O . SER A 286 ? 1.0483 0.9540 0.9271 -0.0361 -0.1340 0.0024 313 SER A O 2205 C CB . SER A 286 ? 1.0899 0.9631 1.0260 -0.0718 -0.1384 0.0057 313 SER A CB 2206 O OG . SER A 286 ? 1.0726 0.9367 1.0036 -0.0678 -0.1419 -0.0131 313 SER A OG 2207 N N . THR A 287 ? 1.1261 1.0330 1.0306 -0.0496 -0.1231 0.0097 314 THR A N 2208 C CA . THR A 287 ? 1.1009 1.0175 0.9873 -0.0357 -0.1189 0.0010 314 THR A CA 2209 C C . THR A 287 ? 1.0973 0.9942 0.9808 -0.0336 -0.1280 -0.0230 314 THR A C 2210 O O . THR A 287 ? 1.1395 1.0376 1.0065 -0.0205 -0.1302 -0.0356 314 THR A O 2211 C CB . THR A 287 ? 1.4499 1.3799 1.3440 -0.0375 -0.1079 0.0108 314 THR A CB 2212 O OG1 . THR A 287 ? 1.5107 1.4660 1.3860 -0.0219 -0.1001 0.0200 314 THR A OG1 2213 C CG2 . THR A 287 ? 1.4785 1.3954 1.3784 -0.0397 -0.1084 -0.0060 314 THR A CG2 2214 N N . LEU A 288 ? 1.0925 0.9719 0.9931 -0.0456 -0.1345 -0.0284 315 LEU A N 2215 C CA . LEU A 288 ? 1.0760 0.9388 0.9818 -0.0464 -0.1434 -0.0464 315 LEU A CA 2216 C C . LEU A 288 ? 1.0948 0.9479 0.9970 -0.0449 -0.1552 -0.0535 315 LEU A C 2217 O O . LEU A 288 ? 1.0996 0.9401 1.0165 -0.0516 -0.1624 -0.0611 315 LEU A O 2218 C CB . LEU A 288 ? 1.0818 0.9360 1.0114 -0.0591 -0.1416 -0.0464 315 LEU A CB 2219 C CG . LEU A 288 ? 1.1229 0.9839 1.0592 -0.0617 -0.1316 -0.0418 315 LEU A CG 2220 C CD1 . LEU A 288 ? 1.1278 0.9814 1.0858 -0.0726 -0.1310 -0.0406 315 LEU A CD1 2221 C CD2 . LEU A 288 ? 1.1462 1.0070 1.0739 -0.0529 -0.1314 -0.0535 315 LEU A CD2 2222 N N . GLY A 289 ? 1.1174 0.9787 1.0011 -0.0357 -0.1569 -0.0496 316 GLY A N 2223 C CA . GLY A 289 ? 1.0796 0.9325 0.9578 -0.0327 -0.1687 -0.0572 316 GLY A CA 2224 C C . GLY A 289 ? 1.0671 0.9247 0.9440 -0.0358 -0.1684 -0.0440 316 GLY A C 2225 O O . GLY A 289 ? 1.0645 0.9295 0.9494 -0.0428 -0.1604 -0.0278 316 GLY A O 2226 N N . VAL A 290 ? 1.0176 0.8698 0.8858 -0.0304 -0.1790 -0.0514 317 VAL A N 2227 C CA . VAL A 290 ? 1.0036 0.8593 0.8675 -0.0309 -0.1809 -0.0412 317 VAL A CA 2228 C C . VAL A 290 ? 1.0167 0.8576 0.8912 -0.0367 -0.1927 -0.0499 317 VAL A C 2229 O O . VAL A 290 ? 1.0744 0.9075 0.9453 -0.0313 -0.2034 -0.0649 317 VAL A O 2230 C CB . VAL A 290 ? 0.8515 0.7215 0.6881 -0.0138 -0.1816 -0.0394 317 VAL A CB 2231 C CG1 . VAL A 290 ? 1.0731 0.9443 0.9057 -0.0138 -0.1863 -0.0316 317 VAL A CG1 2232 C CG2 . VAL A 290 ? 0.8570 0.7481 0.6844 -0.0074 -0.1682 -0.0248 317 VAL A CG2 2233 N N . ILE A 291 ? 0.9950 0.8323 0.8835 -0.0469 -0.1919 -0.0403 318 ILE A N 2234 C CA . ILE A 291 ? 1.0062 0.8330 0.9047 -0.0513 -0.2019 -0.0461 318 ILE A CA 2235 C C . ILE A 291 ? 1.0692 0.8984 0.9618 -0.0507 -0.2041 -0.0358 318 ILE A C 2236 O O . ILE A 291 ? 1.0795 0.9163 0.9692 -0.0517 -0.1974 -0.0212 318 ILE A O 2237 C CB . ILE A 291 ? 0.9562 0.7760 0.8784 -0.0621 -0.2007 -0.0465 318 ILE A CB 2238 C CG1 . ILE A 291 ? 0.9266 0.7486 0.8560 -0.0684 -0.1931 -0.0330 318 ILE A CG1 2239 C CG2 . ILE A 291 ? 0.8661 0.6842 0.7962 -0.0628 -0.1989 -0.0554 318 ILE A CG2 2240 C CD1 . ILE A 291 ? 0.8265 0.6431 0.7756 -0.0754 -0.1923 -0.0343 318 ILE A CD1 2241 N N . GLU A 292 ? 1.1163 0.9394 1.0090 -0.0495 -0.2144 -0.0423 319 GLU A N 2242 C CA . GLU A 292 ? 1.1410 0.9655 1.0280 -0.0484 -0.2175 -0.0333 319 GLU A CA 2243 C C . GLU A 292 ? 1.0176 0.8330 0.9186 -0.0537 -0.2259 -0.0372 319 GLU A C 2244 O O . GLU A 292 ? 1.0031 0.8138 0.9145 -0.0553 -0.2318 -0.0480 319 GLU A O 2245 C CB . GLU A 292 ? 1.2528 1.0853 1.1160 -0.0354 -0.2212 -0.0352 319 GLU A CB 2246 C CG . GLU A 292 ? 1.3229 1.1494 1.1801 -0.0283 -0.2331 -0.0536 319 GLU A CG 2247 C CD . GLU A 292 ? 1.4220 1.2569 1.2521 -0.0121 -0.2377 -0.0570 319 GLU A CD 2248 O OE1 . GLU A 292 ? 1.4669 1.3163 1.2815 -0.0046 -0.2283 -0.0459 319 GLU A OE1 2249 O OE2 . GLU A 292 ? 1.4533 1.2818 1.2782 -0.0061 -0.2512 -0.0700 319 GLU A OE2 2250 N N . ALA A 293 ? 0.9632 0.7773 0.8659 -0.0561 -0.2269 -0.0270 320 ALA A N 2251 C CA . ALA A 293 ? 0.9797 0.7872 0.8936 -0.0590 -0.2346 -0.0295 320 ALA A CA 2252 C C . ALA A 293 ? 1.0840 0.8912 0.9896 -0.0564 -0.2389 -0.0206 320 ALA A C 2253 O O . ALA A 293 ? 1.1516 0.9600 1.0555 -0.0580 -0.2349 -0.0076 320 ALA A O 2254 C CB . ALA A 293 ? 0.9588 0.7619 0.8911 -0.0655 -0.2318 -0.0279 320 ALA A CB 2255 N N . ILE A 294 ? 1.0947 0.9005 0.9977 -0.0529 -0.2478 -0.0267 321 ILE A N 2256 C CA . ILE A 294 ? 1.0812 0.8874 0.9742 -0.0491 -0.2526 -0.0196 321 ILE A CA 2257 C C . ILE A 294 ? 1.0729 0.8719 0.9783 -0.0533 -0.2560 -0.0136 321 ILE A C 2258 O O . ILE A 294 ? 1.0750 0.8701 0.9953 -0.0568 -0.2565 -0.0182 321 ILE A O 2259 C CB . ILE A 294 ? 1.2789 1.0868 1.1626 -0.0422 -0.2623 -0.0299 321 ILE A CB 2260 C CG1 . ILE A 294 ? 1.4353 1.2475 1.3069 -0.0358 -0.2624 -0.0397 321 ILE A CG1 2261 C CG2 . ILE A 294 ? 1.1498 0.9603 1.0197 -0.0364 -0.2665 -0.0223 321 ILE A CG2 2262 C CD1 . ILE A 294 ? 1.4683 1.2759 1.3547 -0.0391 -0.2673 -0.0530 321 ILE A CD1 2263 N N . ALA A 295 ? 1.1084 0.9063 1.0072 -0.0515 -0.2586 -0.0028 322 ALA A N 2264 C CA . ALA A 295 ? 1.0985 0.8879 1.0062 -0.0531 -0.2647 0.0019 322 ALA A CA 2265 C C . ALA A 295 ? 1.2171 1.0076 1.1146 -0.0477 -0.2720 0.0037 322 ALA A C 2266 O O . ALA A 295 ? 1.3077 1.1045 1.1919 -0.0440 -0.2708 0.0121 322 ALA A O 2267 C CB . ALA A 295 ? 0.9457 0.7293 0.8601 -0.0576 -0.2627 0.0155 322 ALA A CB 2268 N N . GLN A 296 ? 1.2690 1.0561 1.1729 -0.0460 -0.2793 -0.0033 323 GLN A N 2269 C CA . GLN A 296 ? 1.3410 1.1299 1.2364 -0.0407 -0.2870 -0.0037 323 GLN A CA 2270 C C . GLN A 296 ? 1.3619 1.1432 1.2578 -0.0398 -0.2920 0.0070 323 GLN A C 2271 O O . GLN A 296 ? 1.3463 1.1212 1.2516 -0.0390 -0.2975 0.0044 323 GLN A O 2272 C CB . GLN A 296 ? 1.4346 1.2261 1.3388 -0.0392 -0.2930 -0.0154 323 GLN A CB 2273 C CG . GLN A 296 ? 1.5769 1.3731 1.4714 -0.0339 -0.3007 -0.0199 323 GLN A CG 2274 C CD . GLN A 296 ? 1.6979 1.4992 1.5799 -0.0312 -0.2995 -0.0256 323 GLN A CD 2275 O OE1 . GLN A 296 ? 1.7241 1.5282 1.5903 -0.0277 -0.2951 -0.0189 323 GLN A OE1 2276 N NE2 . GLN A 296 ? 1.7037 1.5072 1.5937 -0.0317 -0.3043 -0.0373 323 GLN A NE2 2277 N N . ILE A 297 ? 1.3886 1.1717 1.2750 -0.0390 -0.2904 0.0201 324 ILE A N 2278 C CA . ILE A 297 ? 1.3567 1.1325 1.2446 -0.0381 -0.2970 0.0317 324 ILE A CA 2279 C C . ILE A 297 ? 1.3868 1.1670 1.2636 -0.0313 -0.3034 0.0284 324 ILE A C 2280 O O . ILE A 297 ? 1.4467 1.2378 1.3096 -0.0266 -0.3014 0.0255 324 ILE A O 2281 C CB . ILE A 297 ? 1.2803 1.0586 1.1673 -0.0407 -0.2931 0.0514 324 ILE A CB 2282 C CG1 . ILE A 297 ? 1.2996 1.0739 1.1996 -0.0480 -0.2878 0.0552 324 ILE A CG1 2283 C CG2 . ILE A 297 ? 1.2299 0.9992 1.1216 -0.0404 -0.3021 0.0646 324 ILE A CG2 2284 C CD1 . ILE A 297 ? 1.3442 1.1011 1.2605 -0.0514 -0.2955 0.0511 324 ILE A CD1 2285 N N . THR A 298 ? 1.3513 1.1233 1.2334 -0.0292 -0.3121 0.0273 325 THR A N 2286 C CA . THR A 298 ? 1.3589 1.1351 1.2311 -0.0228 -0.3186 0.0260 325 THR A CA 2287 C C . THR A 298 ? 1.3295 1.0956 1.2042 -0.0211 -0.3263 0.0370 325 THR A C 2288 O O . THR A 298 ? 1.2780 1.0314 1.1649 -0.0237 -0.3299 0.0400 325 THR A O 2289 C CB . THR A 298 ? 1.4987 1.2787 1.3752 -0.0201 -0.3232 0.0104 325 THR A CB 2290 O OG1 . THR A 298 ? 1.4678 1.2407 1.3583 -0.0204 -0.3264 0.0070 325 THR A OG1 2291 C CG2 . THR A 298 ? 1.4837 1.2719 1.3606 -0.0222 -0.3182 -0.0001 325 THR A CG2 2292 N N . VAL A 299 ? 1.3834 1.1547 1.2465 -0.0157 -0.3302 0.0426 326 VAL A N 2293 C CA . VAL A 299 ? 1.4239 1.1859 1.2893 -0.0136 -0.3385 0.0535 326 VAL A CA 2294 C C . VAL A 299 ? 1.5566 1.3184 1.4193 -0.0071 -0.3469 0.0433 326 VAL A C 2295 O O . VAL A 299 ? 1.6385 1.4109 1.4892 -0.0020 -0.3480 0.0400 326 VAL A O 2296 C CB . VAL A 299 ? 1.3253 1.0949 1.1810 -0.0118 -0.3364 0.0723 326 VAL A CB 2297 C CG1 . VAL A 299 ? 1.3899 1.1491 1.2500 -0.0098 -0.3464 0.0840 326 VAL A CG1 2298 C CG2 . VAL A 299 ? 1.1517 0.9245 1.0133 -0.0180 -0.3280 0.0860 326 VAL A CG2 2299 N N . LYS A 300 ? 1.6012 1.3520 1.4749 -0.0058 -0.3535 0.0380 327 LYS A N 2300 C CA . LYS A 300 ? 1.7034 1.4565 1.5767 0.0013 -0.3609 0.0293 327 LYS A CA 2301 C C . LYS A 300 ? 1.8298 1.5742 1.6991 0.0061 -0.3702 0.0391 327 LYS A C 2302 O O . LYS A 300 ? 1.8728 1.6027 1.7478 0.0044 -0.3746 0.0494 327 LYS A O 2303 C CB . LYS A 300 ? 1.7032 1.4534 1.5888 0.0036 -0.3626 0.0187 327 LYS A CB 2304 C CG . LYS A 300 ? 1.7117 1.4732 1.5997 0.0105 -0.3666 0.0095 327 LYS A CG 2305 C CD . LYS A 300 ? 1.7240 1.5017 1.6153 0.0069 -0.3609 0.0017 327 LYS A CD 2306 C CE . LYS A 300 ? 1.7539 1.5442 1.6578 0.0121 -0.3634 -0.0053 327 LYS A CE 2307 N NZ . LYS A 300 ? 1.8036 1.5950 1.7052 0.0210 -0.3723 -0.0038 327 LYS A NZ 2308 N N . ALA A 301 ? 1.8490 1.6017 1.7102 0.0120 -0.3744 0.0362 328 ALA A N 2309 C CA . ALA A 301 ? 1.8266 1.5723 1.6833 0.0175 -0.3834 0.0450 328 ALA A CA 2310 C C . ALA A 301 ? 1.9293 1.6728 1.7907 0.0254 -0.3919 0.0356 328 ALA A C 2311 O O . ALA A 301 ? 1.9700 1.7272 1.8303 0.0288 -0.3919 0.0263 328 ALA A O 2312 C CB . ALA A 301 ? 1.7667 1.5246 1.6084 0.0202 -0.3822 0.0508 328 ALA A CB 2313 N N . LEU A 302 ? 1.9810 1.7078 1.8487 0.0291 -0.4002 0.0384 329 LEU A N 2314 C CA . LEU A 302 ? 1.9505 1.6756 1.8211 0.0399 -0.4088 0.0299 329 LEU A CA 2315 C C . LEU A 302 ? 2.1770 1.9125 2.0392 0.0456 -0.4129 0.0305 329 LEU A C 2316 O O . LEU A 302 ? 2.2457 1.9810 2.0993 0.0434 -0.4134 0.0404 329 LEU A O 2317 C CB . LEU A 302 ? 1.7007 1.4024 1.5767 0.0448 -0.4203 0.0332 329 LEU A CB 2318 C CG . LEU A 302 ? 1.5338 1.2178 1.4102 0.0409 -0.4278 0.0493 329 LEU A CG 2319 C CD1 . LEU A 302 ? 1.5177 1.1925 1.3909 0.0512 -0.4412 0.0510 329 LEU A CD1 2320 C CD2 . LEU A 302 ? 1.3832 1.0472 1.2716 0.0359 -0.4324 0.0535 329 LEU A CD2 2321 N N . PRO A 303 ? 2.2789 2.0261 2.1443 0.0538 -0.4156 0.0210 330 PRO A N 2322 C CA . PRO A 303 ? 2.3170 2.0803 2.1783 0.0577 -0.4178 0.0188 330 PRO A CA 2323 C C . PRO A 303 ? 2.3745 2.1330 2.2241 0.0602 -0.4240 0.0275 330 PRO A C 2324 O O . PRO A 303 ? 2.4184 2.1598 2.2654 0.0629 -0.4305 0.0356 330 PRO A O 2325 C CB . PRO A 303 ? 2.3304 2.1013 2.1994 0.0692 -0.4227 0.0119 330 PRO A CB 2326 C CG . PRO A 303 ? 2.3335 2.1022 2.2112 0.0692 -0.4181 0.0070 330 PRO A CG 2327 C CD . PRO A 303 ? 2.3383 2.0850 2.2125 0.0619 -0.4177 0.0127 330 PRO A CD 2328 N N . LYS A 304 ? 2.3987 2.1721 2.2422 0.0595 -0.4232 0.0258 331 LYS A N 2329 C CA . LYS A 304 ? 2.3806 2.1550 2.2126 0.0647 -0.4296 0.0320 331 LYS A CA 2330 C C . LYS A 304 ? 2.2903 2.0677 2.1261 0.0749 -0.4384 0.0283 331 LYS A C 2331 O O . LYS A 304 ? 2.3489 2.1329 2.1960 0.0783 -0.4383 0.0209 331 LYS A O 2332 C CB . LYS A 304 ? 2.4025 2.1921 2.2258 0.0626 -0.4275 0.0288 331 LYS A CB 2333 C CG . LYS A 304 ? 2.4147 2.2023 2.2249 0.0589 -0.4218 0.0377 331 LYS A CG 2334 C CD . LYS A 304 ? 2.4101 2.2126 2.2080 0.0618 -0.4228 0.0321 331 LYS A CD 2335 C CE . LYS A 304 ? 2.3905 2.2022 2.1986 0.0576 -0.4220 0.0173 331 LYS A CE 2336 N NZ . LYS A 304 ? 2.4235 2.2463 2.2202 0.0613 -0.4265 0.0096 331 LYS A NZ 2337 N N . PRO A 305 ? 2.2576 2.0322 2.0839 0.0810 -0.4457 0.0346 332 PRO A N 2338 C CA . PRO A 305 ? 2.2436 2.0239 2.0730 0.0917 -0.4539 0.0307 332 PRO A CA 2339 C C . PRO A 305 ? 2.3188 2.1228 2.1559 0.0922 -0.4534 0.0220 332 PRO A C 2340 O O . PRO A 305 ? 2.3073 2.1206 2.1396 0.0878 -0.4528 0.0205 332 PRO A O 2341 C CB . PRO A 305 ? 2.1330 1.9063 1.9497 0.0964 -0.4609 0.0404 332 PRO A CB 2342 C CG . PRO A 305 ? 2.1101 1.8840 1.9168 0.0888 -0.4549 0.0479 332 PRO A CG 2343 C CD . PRO A 305 ? 2.1706 1.9378 1.9843 0.0799 -0.4467 0.0473 332 PRO A CD 2344 N N . PRO A 306 ? 2.3696 2.1841 2.2196 0.0985 -0.4547 0.0169 333 PRO A N 2345 C CA . PRO A 306 ? 2.3759 2.2155 2.2398 0.0988 -0.4553 0.0121 333 PRO A CA 2346 C C . PRO A 306 ? 2.4459 2.2951 2.3052 0.1022 -0.4636 0.0129 333 PRO A C 2347 O O . PRO A 306 ? 2.4480 2.2866 2.2935 0.1084 -0.4690 0.0174 333 PRO A O 2348 C CB . PRO A 306 ? 2.3624 2.2112 2.2380 0.1094 -0.4555 0.0109 333 PRO A CB 2349 C CG . PRO A 306 ? 2.3701 2.1980 2.2400 0.1107 -0.4526 0.0107 333 PRO A CG 2350 C CD . PRO A 306 ? 2.3756 2.1800 2.2293 0.1064 -0.4558 0.0161 333 PRO A CD 2351 N N . GLY A 307 ? 2.5318 2.4006 2.4043 0.0982 -0.4657 0.0091 334 GLY A N 2352 C CA . GLY A 307 ? 2.5839 2.4631 2.4547 0.1014 -0.4753 0.0085 334 GLY A CA 2353 C C . GLY A 307 ? 2.6095 2.5018 2.4887 0.1126 -0.4809 0.0117 334 GLY A C 2354 O O . GLY A 307 ? 2.6782 2.5894 2.5781 0.1146 -0.4793 0.0126 334 GLY A O 2355 N N . THR A 308 ? 2.4721 2.3563 2.3353 0.1206 -0.4871 0.0147 335 THR A N 2356 C CA . THR A 308 ? 2.6457 2.5390 2.5116 0.1335 -0.4932 0.0178 335 THR A CA 2357 C C . THR A 308 ? 2.7492 2.6719 2.6404 0.1371 -0.4943 0.0186 335 THR A C 2358 O O . THR A 308 ? 2.7229 2.6629 2.6303 0.1299 -0.4979 0.0175 335 THR A O 2359 C CB . THR A 308 ? 2.7159 2.6068 2.5675 0.1377 -0.5023 0.0195 335 THR A CB 2360 O OG1 . THR A 308 ? 2.7782 2.6454 2.6078 0.1367 -0.5008 0.0230 335 THR A OG1 2361 C CG2 . THR A 308 ? 2.7553 2.6558 2.6093 0.1515 -0.5089 0.0227 335 THR A CG2 2362 N N . PRO A 309 ? 2.7621 2.6915 2.6578 0.1495 -0.4923 0.0211 336 PRO A N 2363 C CA . PRO A 309 ? 2.7637 2.7257 2.6835 0.1564 -0.4915 0.0253 336 PRO A CA 2364 C C . PRO A 309 ? 2.7547 2.7379 2.6842 0.1608 -0.5008 0.0293 336 PRO A C 2365 O O . PRO A 309 ? 2.7746 2.7452 2.6870 0.1642 -0.5080 0.0280 336 PRO A O 2366 C CB . PRO A 309 ? 2.7940 2.7521 2.7059 0.1734 -0.4887 0.0255 336 PRO A CB 2367 C CG . PRO A 309 ? 2.8187 2.7427 2.7041 0.1768 -0.4938 0.0224 336 PRO A CG 2368 C CD . PRO A 309 ? 2.8012 2.7069 2.6789 0.1592 -0.4918 0.0207 336 PRO A CD 2369 N N . VAL A 310 ? 2.5960 2.6128 2.5546 0.1608 -0.5006 0.0356 337 VAL A N 2370 C CA . VAL A 310 ? 2.5164 2.5576 2.4907 0.1638 -0.5100 0.0411 337 VAL A CA 2371 C C . VAL A 310 ? 2.6841 2.7613 2.6796 0.1781 -0.5068 0.0517 337 VAL A C 2372 O O . VAL A 310 ? 2.7706 2.8640 2.7818 0.1790 -0.4979 0.0565 337 VAL A O 2373 C CB . VAL A 310 ? 2.3338 2.3844 2.3302 0.1466 -0.5170 0.0408 337 VAL A CB 2374 C CG1 . VAL A 310 ? 2.3432 2.4157 2.3556 0.1493 -0.5294 0.0458 337 VAL A CG1 2375 C CG2 . VAL A 310 ? 2.2477 2.2659 2.2213 0.1355 -0.5189 0.0299 337 VAL A CG2 2376 N N . VAL A 311 ? 2.7218 2.8136 2.7172 0.1905 -0.5136 0.0561 338 VAL A N 2377 C CA . VAL A 311 ? 2.7677 2.8974 2.7812 0.2074 -0.5105 0.0674 338 VAL A CA 2378 C C . VAL A 311 ? 2.7924 2.9629 2.8486 0.1986 -0.5135 0.0808 338 VAL A C 2379 O O . VAL A 311 ? 2.7932 2.9732 2.8608 0.1942 -0.5245 0.0837 338 VAL A O 2380 C CB . VAL A 311 ? 2.7623 2.8910 2.7572 0.2264 -0.5169 0.0669 338 VAL A CB 2381 C CG1 . VAL A 311 ? 2.7724 2.9431 2.7839 0.2471 -0.5131 0.0787 338 VAL A CG1 2382 C CG2 . VAL A 311 ? 2.7790 2.8655 2.7358 0.2342 -0.5169 0.0552 338 VAL A CG2 2383 N N . THR A 312 ? 2.8346 3.0297 2.9163 0.1962 -0.5046 0.0901 339 THR A N 2384 C CA . THR A 312 ? 2.7648 2.9991 2.8932 0.1858 -0.5080 0.1059 339 THR A CA 2385 C C . THR A 312 ? 2.7104 2.9952 2.8631 0.2040 -0.5046 0.1249 339 THR A C 2386 O O . THR A 312 ? 2.7211 3.0366 2.9074 0.1992 -0.5129 0.1383 339 THR A O 2387 C CB . THR A 312 ? 2.6673 2.9043 2.8165 0.1710 -0.5009 0.1090 339 THR A CB 2388 O OG1 . THR A 312 ? 2.6320 2.8677 2.7646 0.1843 -0.4866 0.1077 339 THR A OG1 2389 C CG2 . THR A 312 ? 2.6547 2.8512 2.7908 0.1506 -0.5074 0.0935 339 THR A CG2 2390 N N . GLU A 313 ? 2.6302 2.9252 2.7670 0.2259 -0.4932 0.1265 340 GLU A N 2391 C CA . GLU A 313 ? 2.5391 2.8859 2.6957 0.2475 -0.4882 0.1450 340 GLU A CA 2392 C C . GLU A 313 ? 2.4816 2.8207 2.6001 0.2772 -0.4844 0.1364 340 GLU A C 2393 O O . GLU A 313 ? 2.5738 2.8979 2.6700 0.2882 -0.4764 0.1278 340 GLU A O 2394 C CB . GLU A 313 ? 2.5647 2.9515 2.7559 0.2469 -0.4768 0.1630 340 GLU A CB 2395 C CG . GLU A 313 ? 2.5700 2.9714 2.8075 0.2194 -0.4824 0.1755 340 GLU A CG 2396 C CD . GLU A 313 ? 2.5228 2.9646 2.7956 0.2195 -0.4707 0.1956 340 GLU A CD 2397 O OE1 . GLU A 313 ? 2.4998 2.9823 2.7761 0.2440 -0.4597 0.2096 340 GLU A OE1 2398 O OE2 . GLU A 313 ? 2.4948 2.9284 2.7911 0.1964 -0.4726 0.1974 340 GLU A OE2 2399 N N . SER A 314 ? 2.4399 2.7890 2.5517 0.2911 -0.4917 0.1383 341 SER A N 2400 C CA . SER A 314 ? 2.4195 2.7587 2.4950 0.3204 -0.4913 0.1290 341 SER A CA 2401 C C . SER A 314 ? 2.4666 2.8617 2.5574 0.3479 -0.4877 0.1463 341 SER A C 2402 O O . SER A 314 ? 2.4926 2.9178 2.6078 0.3457 -0.4932 0.1597 341 SER A O 2403 C CB . SER A 314 ? 2.3463 2.6404 2.3908 0.3170 -0.5034 0.1130 341 SER A CB 2404 O OG . SER A 314 ? 2.3074 2.6128 2.3729 0.3021 -0.5126 0.1201 341 SER A OG 2405 N N . THR A 315 ? 2.4574 2.8674 2.5335 0.3751 -0.4790 0.1458 342 THR A N 2406 C CA . THR A 315 ? 2.5197 2.9815 2.6012 0.4082 -0.4750 0.1598 342 THR A CA 2407 C C . THR A 315 ? 2.6499 3.0827 2.6845 0.4380 -0.4793 0.1405 342 THR A C 2408 O O . THR A 315 ? 2.6567 3.0354 2.6590 0.4352 -0.4850 0.1191 342 THR A O 2409 C CB . THR A 315 ? 2.4908 3.0059 2.5982 0.4201 -0.4603 0.1789 342 THR A CB 2410 O OG1 . THR A 315 ? 2.4970 2.9884 2.5721 0.4366 -0.4550 0.1629 342 THR A OG1 2411 C CG2 . THR A 315 ? 2.4853 3.0159 2.6377 0.3863 -0.4565 0.1947 342 THR A CG2 2412 N N . ALA A 316 ? 2.8041 3.2670 2.8386 0.4588 -0.4714 0.1483 343 ALA A N 2413 C CA . ALA A 316 ? 2.9207 3.3537 2.9154 0.4813 -0.4718 0.1303 343 ALA A CA 2414 C C . ALA A 316 ? 3.0112 3.4020 2.9718 0.4914 -0.4707 0.1087 343 ALA A C 2415 O O . ALA A 316 ? 3.0249 3.3669 2.9519 0.4978 -0.4797 0.0884 343 ALA A O 2416 C CB . ALA A 316 ? 2.9322 3.4137 2.9351 0.5055 -0.4595 0.1434 343 ALA A CB 2417 N N . THR A 317 ? 3.0994 3.5090 3.0708 0.4922 -0.4604 0.1139 344 THR A N 2418 C CA . THR A 317 ? 3.1030 3.4759 3.0448 0.5020 -0.4594 0.0942 344 THR A CA 2419 C C . THR A 317 ? 3.0613 3.4205 3.0132 0.4813 -0.4606 0.0937 344 THR A C 2420 O O . THR A 317 ? 3.1339 3.4803 3.0718 0.4897 -0.4556 0.0839 344 THR A O 2421 C CB . THR A 317 ? 3.1443 3.5503 3.0789 0.5321 -0.4439 0.0956 344 THR A CB 2422 O OG1 . THR A 317 ? 3.1645 3.6306 3.1357 0.5293 -0.4291 0.1210 344 THR A OG1 2423 C CG2 . THR A 317 ? 3.1910 3.6064 3.1105 0.5555 -0.4433 0.0926 344 THR A CG2 2424 N N . SER A 318 ? 2.8389 3.1994 2.8142 0.4549 -0.4683 0.1028 345 SER A N 2425 C CA . SER A 318 ? 2.6661 3.0064 2.6518 0.4276 -0.4652 0.1007 345 SER A CA 2426 C C . SER A 318 ? 2.5149 2.8206 2.5085 0.3908 -0.4718 0.0977 345 SER A C 2427 O O . SER A 318 ? 2.5415 2.8609 2.5486 0.3843 -0.4772 0.1059 345 SER A O 2428 C CB . SER A 318 ? 2.6754 3.0717 2.6987 0.4245 -0.4505 0.1229 345 SER A CB 2429 O OG . SER A 318 ? 2.6924 3.1206 2.7551 0.4037 -0.4499 0.1429 345 SER A OG 2430 N N . ILE A 319 ? 2.3650 2.6273 2.3495 0.3683 -0.4719 0.0857 346 ILE A N 2431 C CA . ILE A 319 ? 2.2702 2.5016 2.2600 0.3355 -0.4774 0.0825 346 ILE A CA 2432 C C . ILE A 319 ? 2.2529 2.4723 2.2560 0.3096 -0.4703 0.0820 346 ILE A C 2433 O O . ILE A 319 ? 2.1924 2.3817 2.1768 0.3093 -0.4677 0.0703 346 ILE A O 2434 C CB . ILE A 319 ? 2.2560 2.4332 2.2110 0.3352 -0.4892 0.0652 346 ILE A CB 2435 C CG1 . ILE A 319 ? 2.2731 2.4613 2.2204 0.3534 -0.4981 0.0673 346 ILE A CG1 2436 C CG2 . ILE A 319 ? 2.2585 2.4030 2.2150 0.3030 -0.4924 0.0610 346 ILE A CG2 2437 C CD1 . ILE A 319 ? 2.3115 2.4494 2.2283 0.3528 -0.5104 0.0535 346 ILE A CD1 2438 N N . THR A 320 ? 2.3160 2.5588 2.3529 0.2882 -0.4686 0.0948 347 THR A N 2439 C CA . THR A 320 ? 2.3560 2.5907 2.4093 0.2636 -0.4631 0.0955 347 THR A CA 2440 C C . THR A 320 ? 2.4930 2.6793 2.5304 0.2400 -0.4705 0.0817 347 THR A C 2441 O O . THR A 320 ? 2.5045 2.6829 2.5407 0.2328 -0.4801 0.0806 347 THR A O 2442 C CB . THR A 320 ? 2.2408 2.5227 2.3414 0.2517 -0.4603 0.1162 347 THR A CB 2443 O OG1 . THR A 320 ? 2.1889 2.5224 2.3061 0.2754 -0.4523 0.1329 347 THR A OG1 2444 C CG2 . THR A 320 ? 2.1958 2.4688 2.3132 0.2287 -0.4552 0.1165 347 THR A CG2 2445 N N . LEU A 321 ? 2.6085 2.7649 2.6334 0.2295 -0.4658 0.0719 348 LEU A N 2446 C CA . LEU A 321 ? 2.6463 2.7590 2.6540 0.2097 -0.4709 0.0600 348 LEU A CA 2447 C C . LEU A 321 ? 2.6100 2.7214 2.6367 0.1866 -0.4666 0.0611 348 LEU A C 2448 O O . LEU A 321 ? 2.6636 2.7830 2.6985 0.1866 -0.4573 0.0632 348 LEU A O 2449 C CB . LEU A 321 ? 2.6897 2.7620 2.6624 0.2181 -0.4711 0.0467 348 LEU A CB 2450 C CG . LEU A 321 ? 2.7793 2.8224 2.7259 0.2235 -0.4815 0.0397 348 LEU A CG 2451 C CD1 . LEU A 321 ? 2.8277 2.8980 2.7806 0.2388 -0.4874 0.0466 348 LEU A CD1 2452 C CD2 . LEU A 321 ? 2.8192 2.8294 2.7389 0.2361 -0.4832 0.0299 348 LEU A CD2 2453 N N . THR A 322 ? 2.3106 2.4118 2.3434 0.1686 -0.4744 0.0590 349 THR A N 2454 C CA . THR A 322 ? 2.1188 2.2120 2.1651 0.1474 -0.4732 0.0569 349 THR A CA 2455 C C . THR A 322 ? 2.1126 2.1646 2.1308 0.1366 -0.4778 0.0435 349 THR A C 2456 O O . THR A 322 ? 2.2035 2.2459 2.2105 0.1364 -0.4872 0.0402 349 THR A O 2457 C CB . THR A 322 ? 2.0351 2.1577 2.1201 0.1358 -0.4806 0.0672 349 THR A CB 2458 O OG1 . THR A 322 ? 2.0370 2.1528 2.1166 0.1335 -0.4937 0.0637 349 THR A OG1 2459 C CG2 . THR A 322 ? 2.0116 2.1812 2.1281 0.1470 -0.4758 0.0851 349 THR A CG2 2460 N N . TRP A 323 ? 2.0330 2.0629 2.0401 0.1286 -0.4707 0.0369 350 TRP A N 2461 C CA . TRP A 323 ? 2.1189 2.1135 2.0998 0.1199 -0.4731 0.0268 350 TRP A CA 2462 C C . TRP A 323 ? 2.1311 2.1179 2.1197 0.1032 -0.4704 0.0226 350 TRP A C 2463 O O . TRP A 323 ? 2.0649 2.0721 2.0812 0.0969 -0.4681 0.0275 350 TRP A O 2464 C CB . TRP A 323 ? 2.2160 2.1846 2.1687 0.1293 -0.4684 0.0226 350 TRP A CB 2465 C CG . TRP A 323 ? 2.2507 2.2186 2.2062 0.1321 -0.4583 0.0223 350 TRP A CG 2466 C CD1 . TRP A 323 ? 2.2484 2.1993 2.1995 0.1212 -0.4516 0.0179 350 TRP A CD1 2467 C CD2 . TRP A 323 ? 2.2207 2.2067 2.1823 0.1488 -0.4542 0.0260 350 TRP A CD2 2468 N NE1 . TRP A 323 ? 2.2246 2.1809 2.1797 0.1290 -0.4440 0.0185 350 TRP A NE1 2469 C CE2 . TRP A 323 ? 2.1966 2.1746 2.1571 0.1468 -0.4455 0.0231 350 TRP A CE2 2470 C CE3 . TRP A 323 ? 2.1887 2.1986 2.1557 0.1668 -0.4570 0.0315 350 TRP A CE3 2471 C CZ2 . TRP A 323 ? 2.1584 2.1511 2.1218 0.1633 -0.4403 0.0247 350 TRP A CZ2 2472 C CZ3 . TRP A 323 ? 2.1526 2.1784 2.1220 0.1840 -0.4513 0.0335 350 TRP A CZ3 2473 C CH2 . TRP A 323 ? 2.1452 2.1621 2.1122 0.1826 -0.4433 0.0297 350 TRP A CH2 2474 N N . ASP A 324 ? 2.2367 2.1954 2.2014 0.0969 -0.4709 0.0148 351 ASP A N 2475 C CA . ASP A 324 ? 2.2616 2.2093 2.2271 0.0840 -0.4669 0.0096 351 ASP A CA 2476 C C . ASP A 324 ? 2.2527 2.1774 2.1970 0.0852 -0.4569 0.0073 351 ASP A C 2477 O O . ASP A 324 ? 2.3739 2.2847 2.2990 0.0939 -0.4572 0.0082 351 ASP A O 2478 C CB . ASP A 324 ? 2.3152 2.2529 2.2716 0.0769 -0.4764 0.0027 351 ASP A CB 2479 C CG . ASP A 324 ? 2.3577 2.2908 2.3219 0.0648 -0.4753 -0.0030 351 ASP A CG 2480 O OD1 . ASP A 324 ? 2.3829 2.3329 2.3766 0.0588 -0.4755 0.0001 351 ASP A OD1 2481 O OD2 . ASP A 324 ? 2.3612 2.2751 2.3028 0.0621 -0.4741 -0.0095 351 ASP A OD2 2482 N N . SER A 325 ? 2.0512 1.9715 2.0009 0.0763 -0.4495 0.0050 352 SER A N 2483 C CA . SER A 325 ? 1.8471 1.7480 1.7816 0.0768 -0.4404 0.0037 352 SER A CA 2484 C C . SER A 325 ? 1.7923 1.6682 1.6996 0.0763 -0.4420 0.0022 352 SER A C 2485 O O . SER A 325 ? 1.7088 1.5679 1.6038 0.0801 -0.4388 0.0040 352 SER A O 2486 C CB . SER A 325 ? 1.7760 1.6777 1.7216 0.0663 -0.4327 0.0014 352 SER A CB 2487 O OG . SER A 325 ? 1.7926 1.6803 1.7267 0.0569 -0.4335 -0.0037 352 SER A OG 2488 N N . GLY A 326 ? 1.9722 1.8468 1.8717 0.0724 -0.4481 -0.0002 353 GLY A N 2489 C CA . GLY A 326 ? 2.0239 1.8806 1.8986 0.0730 -0.4488 0.0010 353 GLY A CA 2490 C C . GLY A 326 ? 2.0217 1.8646 1.8885 0.0657 -0.4396 0.0011 353 GLY A C 2491 O O . GLY A 326 ? 2.0413 1.8687 1.8927 0.0668 -0.4369 0.0067 353 GLY A O 2492 N N . ASN A 327 ? 2.0277 1.8771 1.9076 0.0581 -0.4354 -0.0040 354 ASN A N 2493 C CA . ASN A 327 ? 2.1400 1.9789 2.0157 0.0512 -0.4260 -0.0043 354 ASN A CA 2494 C C . ASN A 327 ? 2.2459 2.0911 2.1281 0.0436 -0.4256 -0.0116 354 ASN A C 2495 O O . ASN A 327 ? 2.2954 2.1541 2.1952 0.0418 -0.4319 -0.0158 354 ASN A O 2496 C CB . ASN A 327 ? 2.1303 1.9672 2.0176 0.0516 -0.4194 -0.0024 354 ASN A CB 2497 C CG . ASN A 327 ? 2.1068 1.9258 1.9818 0.0563 -0.4184 0.0035 354 ASN A CG 2498 O OD1 . ASN A 327 ? 2.0588 1.8650 1.9296 0.0515 -0.4125 0.0057 354 ASN A OD1 2499 N ND2 . ASN A 327 ? 2.1449 1.9623 2.0158 0.0655 -0.4256 0.0065 354 ASN A ND2 2500 N N . PRO A 328 ? 2.3030 2.1385 2.1724 0.0395 -0.4193 -0.0123 355 PRO A N 2501 C CA . PRO A 328 ? 2.3592 2.1981 2.2346 0.0331 -0.4184 -0.0201 355 PRO A CA 2502 C C . PRO A 328 ? 2.4489 2.2897 2.3433 0.0264 -0.4103 -0.0201 355 PRO A C 2503 O O . PRO A 328 ? 2.4656 2.3156 2.3787 0.0216 -0.4130 -0.0250 355 PRO A O 2504 C CB . PRO A 328 ? 2.3418 2.1719 2.1930 0.0344 -0.4139 -0.0189 355 PRO A CB 2505 C CG . PRO A 328 ? 2.3158 2.1364 2.1574 0.0366 -0.4078 -0.0073 355 PRO A CG 2506 C CD . PRO A 328 ? 2.2954 2.1180 2.1443 0.0415 -0.4143 -0.0045 355 PRO A CD 2507 N N . GLU A 329 ? 2.4836 2.3157 2.3746 0.0266 -0.4017 -0.0142 356 GLU A N 2508 C CA . GLU A 329 ? 2.4807 2.3141 2.3864 0.0223 -0.3936 -0.0143 356 GLU A CA 2509 C C . GLU A 329 ? 2.4209 2.2671 2.3451 0.0272 -0.3952 -0.0122 356 GLU A C 2510 O O . GLU A 329 ? 2.4364 2.2849 2.3577 0.0350 -0.4008 -0.0093 356 GLU A O 2511 C CB . GLU A 329 ? 2.6024 2.4203 2.4968 0.0213 -0.3858 -0.0095 356 GLU A CB 2512 C CG . GLU A 329 ? 2.7231 2.5345 2.6060 0.0154 -0.3801 -0.0101 356 GLU A CG 2513 C CD . GLU A 329 ? 2.8121 2.6290 2.7077 0.0087 -0.3749 -0.0163 356 GLU A CD 2514 O OE1 . GLU A 329 ? 2.8148 2.6327 2.7234 0.0069 -0.3697 -0.0157 356 GLU A OE1 2515 O OE2 . GLU A 329 ? 2.8763 2.6964 2.7683 0.0064 -0.3770 -0.0221 356 GLU A OE2 2516 N N . PRO A 330 ? 2.3545 2.2111 2.2976 0.0240 -0.3898 -0.0127 357 PRO A N 2517 C CA . PRO A 330 ? 2.3490 2.2232 2.3102 0.0308 -0.3892 -0.0086 357 PRO A CA 2518 C C . PRO A 330 ? 2.4137 2.2807 2.3637 0.0425 -0.3893 -0.0063 357 PRO A C 2519 O O . PRO A 330 ? 2.4431 2.2931 2.3815 0.0431 -0.3854 -0.0073 357 PRO A O 2520 C CB . PRO A 330 ? 2.2468 2.1279 2.2231 0.0255 -0.3806 -0.0086 357 PRO A CB 2521 C CG . PRO A 330 ? 2.2235 2.0972 2.1983 0.0143 -0.3810 -0.0135 357 PRO A CG 2522 C CD . PRO A 330 ? 2.2762 2.1312 2.2248 0.0147 -0.3841 -0.0163 357 PRO A CD 2523 N N . VAL A 331 ? 2.3838 2.2635 2.3384 0.0520 -0.3952 -0.0033 358 VAL A N 2524 C CA . VAL A 331 ? 2.4544 2.3278 2.3987 0.0658 -0.3978 -0.0024 358 VAL A CA 2525 C C . VAL A 331 ? 2.4937 2.3860 2.4512 0.0767 -0.3932 -0.0006 358 VAL A C 2526 O O . VAL A 331 ? 2.6014 2.5215 2.5777 0.0804 -0.3927 0.0046 358 VAL A O 2527 C CB . VAL A 331 ? 2.4667 2.3437 2.4057 0.0729 -0.4070 -0.0003 358 VAL A CB 2528 C CG1 . VAL A 331 ? 2.5154 2.3774 2.4395 0.0862 -0.4118 -0.0007 358 VAL A CG1 2529 C CG2 . VAL A 331 ? 2.5022 2.3687 2.4310 0.0632 -0.4113 -0.0014 358 VAL A CG2 2530 N N . SER A 332 ? 2.4022 2.2805 2.3506 0.0828 -0.3905 -0.0040 359 SER A N 2531 C CA . SER A 332 ? 2.2410 2.1368 2.1987 0.0950 -0.3855 -0.0036 359 SER A CA 2532 C C . SER A 332 ? 2.1857 2.1023 2.1458 0.1147 -0.3899 -0.0006 359 SER A C 2533 O O . SER A 332 ? 2.2016 2.1494 2.1779 0.1231 -0.3845 0.0051 359 SER A O 2534 C CB . SER A 332 ? 2.1260 1.9985 2.0711 0.0986 -0.3848 -0.0098 359 SER A CB 2535 O OG . SER A 332 ? 2.0549 1.9144 2.0006 0.0814 -0.3787 -0.0109 359 SER A OG 2536 N N . TYR A 333 ? 2.1197 2.0209 2.0645 0.1227 -0.3995 -0.0031 360 TYR A N 2537 C CA . TYR A 333 ? 2.0956 2.0170 2.0418 0.1412 -0.4046 -0.0002 360 TYR A CA 2538 C C . TYR A 333 ? 2.2006 2.1010 2.1302 0.1453 -0.4159 -0.0026 360 TYR A C 2539 O O . TYR A 333 ? 2.2448 2.1147 2.1618 0.1349 -0.4199 -0.0055 360 TYR A O 2540 C CB . TYR A 333 ? 2.0208 1.9538 1.9639 0.1640 -0.4034 -0.0030 360 TYR A CB 2541 C CG . TYR A 333 ? 1.9901 1.8891 1.9147 0.1701 -0.4092 -0.0135 360 TYR A CG 2542 C CD1 . TYR A 333 ? 1.9557 1.8452 1.8820 0.1619 -0.4029 -0.0168 360 TYR A CD1 2543 C CD2 . TYR A 333 ? 1.9794 1.8554 1.8866 0.1841 -0.4224 -0.0199 360 TYR A CD2 2544 C CE1 . TYR A 333 ? 1.9326 1.7910 1.8451 0.1669 -0.4100 -0.0258 360 TYR A CE1 2545 C CE2 . TYR A 333 ? 1.9733 1.8166 1.8676 0.1890 -0.4308 -0.0289 360 TYR A CE2 2546 C CZ . TYR A 333 ? 1.9470 1.7819 1.8446 0.1802 -0.4247 -0.0317 360 TYR A CZ 2547 O OH . TYR A 333 ? 1.9636 1.7656 1.8510 0.1845 -0.4349 -0.0401 360 TYR A OH 2548 N N . TYR A 334 ? 2.2496 2.1688 2.1805 0.1611 -0.4207 0.0003 361 TYR A N 2549 C CA . TYR A 334 ? 2.3535 2.2572 2.2710 0.1658 -0.4315 -0.0008 361 TYR A CA 2550 C C . TYR A 334 ? 2.4958 2.3972 2.4009 0.1917 -0.4400 -0.0054 361 TYR A C 2551 O O . TYR A 334 ? 2.4630 2.3903 2.3736 0.2097 -0.4366 -0.0049 361 TYR A O 2552 C CB . TYR A 334 ? 2.3947 2.3216 2.3246 0.1596 -0.4320 0.0066 361 TYR A CB 2553 C CG . TYR A 334 ? 2.4473 2.3796 2.3911 0.1373 -0.4264 0.0098 361 TYR A CG 2554 C CD1 . TYR A 334 ? 2.4723 2.4357 2.4408 0.1330 -0.4194 0.0160 361 TYR A CD1 2555 C CD2 . TYR A 334 ? 2.4762 2.3837 2.4090 0.1220 -0.4291 0.0071 361 TYR A CD2 2556 C CE1 . TYR A 334 ? 2.4737 2.4392 2.4557 0.1136 -0.4172 0.0175 361 TYR A CE1 2557 C CE2 . TYR A 334 ? 2.4983 2.4102 2.4413 0.1048 -0.4259 0.0079 361 TYR A CE2 2558 C CZ . TYR A 334 ? 2.4561 2.3949 2.4237 0.1004 -0.4209 0.0120 361 TYR A CZ 2559 O OH . TYR A 334 ? 2.4026 2.3431 2.3813 0.0841 -0.4204 0.0114 361 TYR A OH 2560 N N . ILE A 335 ? 2.7106 2.5819 2.5995 0.1947 -0.4516 -0.0092 362 ILE A N 2561 C CA . ILE A 335 ? 2.9152 2.7770 2.7905 0.2192 -0.4635 -0.0151 362 ILE A CA 2562 C C . ILE A 335 ? 3.4813 3.3437 3.3517 0.2231 -0.4716 -0.0114 362 ILE A C 2563 O O . ILE A 335 ? 3.5208 3.3615 3.3863 0.2082 -0.4755 -0.0086 362 ILE A O 2564 C CB . ILE A 335 ? 2.6562 2.4753 2.5181 0.2208 -0.4742 -0.0232 362 ILE A CB 2565 C CG1 . ILE A 335 ? 2.4840 2.2953 2.3515 0.2071 -0.4659 -0.0250 362 ILE A CG1 2566 C CG2 . ILE A 335 ? 2.6648 2.4769 2.5145 0.2504 -0.4872 -0.0327 362 ILE A CG2 2567 C CD1 . ILE A 335 ? 2.4396 2.2091 2.2985 0.2052 -0.4773 -0.0306 362 ILE A CD1 2568 N N . ILE A 336 ? 4.0291 3.9178 3.9003 0.2443 -0.4738 -0.0106 363 ILE A N 2569 C CA . ILE A 336 ? 4.1119 4.0047 3.9792 0.2493 -0.4812 -0.0068 363 ILE A CA 2570 C C . ILE A 336 ? 4.1220 3.9862 3.9702 0.2687 -0.4973 -0.0145 363 ILE A C 2571 O O . ILE A 336 ? 4.1883 4.0525 4.0286 0.2922 -0.5028 -0.0224 363 ILE A O 2572 C CB . ILE A 336 ? 4.2188 4.1599 4.1009 0.2608 -0.4750 0.0009 363 ILE A CB 2573 C CG1 . ILE A 336 ? 4.1796 4.1433 4.0835 0.2373 -0.4646 0.0104 363 ILE A CG1 2574 C CG2 . ILE A 336 ? 4.2429 4.1881 4.1171 0.2758 -0.4849 0.0021 363 ILE A CG2 2575 C CD1 . ILE A 336 ? 4.1830 4.1939 4.1072 0.2449 -0.4606 0.0213 363 ILE A CD1 2576 N N . GLN A 337 ? 3.7356 3.5753 3.5762 0.2601 -0.5060 -0.0122 364 GLN A N 2577 C CA . GLN A 337 ? 3.5693 3.3807 3.3947 0.2770 -0.5232 -0.0177 364 GLN A CA 2578 C C . GLN A 337 ? 3.7173 3.5493 3.5398 0.2923 -0.5278 -0.0148 364 GLN A C 2579 O O . GLN A 337 ? 3.8758 3.7245 3.7054 0.2794 -0.5223 -0.0063 364 GLN A O 2580 C CB . GLN A 337 ? 3.3473 3.1178 3.1676 0.2591 -0.5310 -0.0145 364 GLN A CB 2581 C CG . GLN A 337 ? 3.0829 2.8285 2.9056 0.2462 -0.5297 -0.0167 364 GLN A CG 2582 C CD . GLN A 337 ? 2.7781 2.4855 2.5980 0.2323 -0.5394 -0.0105 364 GLN A CD 2583 O OE1 . GLN A 337 ? 2.6810 2.3814 2.4966 0.2314 -0.5460 -0.0040 364 GLN A OE1 2584 N NE2 . GLN A 337 ? 2.6250 2.3094 2.4488 0.2215 -0.5404 -0.0108 364 GLN A NE2 2585 N N . HIS A 338 ? 3.6522 3.4826 3.4638 0.3210 -0.5390 -0.0225 365 HIS A N 2586 C CA . HIS A 338 ? 3.6311 3.4815 3.4388 0.3387 -0.5441 -0.0201 365 HIS A CA 2587 C C . HIS A 338 ? 3.6305 3.4518 3.4203 0.3637 -0.5643 -0.0298 365 HIS A C 2588 O O . HIS A 338 ? 3.6208 3.4215 3.4015 0.3798 -0.5739 -0.0412 365 HIS A O 2589 C CB . HIS A 338 ? 3.6345 3.5381 3.4530 0.3538 -0.5322 -0.0162 365 HIS A CB 2590 C CG . HIS A 338 ? 3.6705 3.5830 3.4816 0.3811 -0.5337 -0.0254 365 HIS A CG 2591 N ND1 . HIS A 338 ? 3.6955 3.6216 3.4942 0.4160 -0.5425 -0.0312 365 HIS A ND1 2592 C CD2 . HIS A 338 ? 3.6742 3.5864 3.4875 0.3807 -0.5275 -0.0301 365 HIS A CD2 2593 C CE1 . HIS A 338 ? 3.7098 3.6435 3.5033 0.4343 -0.5385 -0.0396 365 HIS A CE1 2594 N NE2 . HIS A 338 ? 3.6947 3.6199 3.4962 0.4157 -0.5331 -0.0389 365 HIS A NE2 2595 N N . LYS A 339 ? 3.2078 3.0263 2.9928 0.3671 -0.5720 -0.0257 366 LYS A N 2596 C CA . LYS A 339 ? 2.9732 2.7669 2.7431 0.3901 -0.5901 -0.0338 366 LYS A CA 2597 C C . LYS A 339 ? 2.9104 2.7192 2.6794 0.3923 -0.5906 -0.0265 366 LYS A C 2598 O O . LYS A 339 ? 2.9831 2.8099 2.7615 0.3735 -0.5831 -0.0150 366 LYS A O 2599 C CB . LYS A 339 ? 2.8723 2.6102 2.6370 0.3801 -0.6057 -0.0376 366 LYS A CB 2600 C CG . LYS A 339 ? 2.7425 2.4599 2.5108 0.3554 -0.6088 -0.0249 366 LYS A CG 2601 C CD . LYS A 339 ? 2.6102 2.2747 2.3755 0.3518 -0.6283 -0.0259 366 LYS A CD 2602 C CE . LYS A 339 ? 2.4978 2.1469 2.2689 0.3251 -0.6264 -0.0101 366 LYS A CE 2603 N NZ . LYS A 339 ? 2.4726 2.1386 2.2393 0.3282 -0.6258 -0.0029 366 LYS A NZ 2604 N N . PRO A 340 ? 2.7437 2.5461 2.5023 0.4137 -0.5961 -0.0342 367 PRO A N 2605 C CA . PRO A 340 ? 2.6870 2.4982 2.4433 0.4174 -0.5984 -0.0283 367 PRO A CA 2606 C C . PRO A 340 ? 2.6829 2.4626 2.4389 0.3957 -0.6083 -0.0193 367 PRO A C 2607 O O . PRO A 340 ? 2.7169 2.4596 2.4725 0.3821 -0.6164 -0.0191 367 PRO A O 2608 C CB . PRO A 340 ? 2.6907 2.4881 2.4337 0.4442 -0.6057 -0.0417 367 PRO A CB 2609 C CG . PRO A 340 ? 2.6681 2.4752 2.4084 0.4598 -0.6002 -0.0529 367 PRO A CG 2610 C CD . PRO A 340 ? 2.6711 2.4630 2.4193 0.4383 -0.5995 -0.0501 367 PRO A CD 2611 N N . LYS A 341 ? 2.6288 2.4250 2.3857 0.3932 -0.6073 -0.0108 368 LYS A N 2612 C CA . LYS A 341 ? 2.5532 2.3287 2.3096 0.3732 -0.6139 -0.0001 368 LYS A CA 2613 C C . LYS A 341 ? 2.5642 2.2945 2.3122 0.3758 -0.6288 -0.0012 368 LYS A C 2614 O O . LYS A 341 ? 2.5287 2.2296 2.2778 0.3584 -0.6357 0.0071 368 LYS A O 2615 C CB . LYS A 341 ? 2.5007 2.3105 2.2609 0.3709 -0.6086 0.0085 368 LYS A CB 2616 C CG . LYS A 341 ? 2.4617 2.2591 2.2216 0.3487 -0.6103 0.0195 368 LYS A CG 2617 C CD . LYS A 341 ? 2.4046 2.2402 2.1714 0.3439 -0.6025 0.0257 368 LYS A CD 2618 C CE . LYS A 341 ? 2.3832 2.2306 2.1446 0.3646 -0.6092 0.0252 368 LYS A CE 2619 N NZ . LYS A 341 ? 2.3903 2.2036 2.1400 0.3646 -0.6198 0.0285 368 LYS A NZ 2620 N N . ASN A 342 ? 2.6131 2.3391 2.3541 0.3976 -0.6340 -0.0103 369 ASN A N 2621 C CA . ASN A 342 ? 2.6440 2.3260 2.3793 0.4013 -0.6502 -0.0123 369 ASN A CA 2622 C C . ASN A 342 ? 2.8342 2.4811 2.5692 0.4062 -0.6600 -0.0240 369 ASN A C 2623 O O . ASN A 342 ? 2.8512 2.4580 2.5849 0.4087 -0.6759 -0.0268 369 ASN A O 2624 C CB . ASN A 342 ? 2.5140 2.2043 2.2412 0.4226 -0.6535 -0.0177 369 ASN A CB 2625 C CG . ASN A 342 ? 2.4105 2.1163 2.1382 0.4147 -0.6514 -0.0044 369 ASN A CG 2626 O OD1 . ASN A 342 ? 2.3968 2.1009 2.1291 0.3936 -0.6498 0.0086 369 ASN A OD1 2627 N ND2 . ASN A 342 ? 2.3395 2.0608 2.0614 0.4325 -0.6516 -0.0078 369 ASN A ND2 2628 N N . SER A 343 ? 2.9982 2.6602 2.7356 0.4073 -0.6513 -0.0306 370 SER A N 2629 C CA . SER A 343 ? 3.0304 2.6618 2.7674 0.4121 -0.6600 -0.0429 370 SER A CA 2630 C C . SER A 343 ? 3.0192 2.6121 2.7659 0.3878 -0.6700 -0.0327 370 SER A C 2631 O O . SER A 343 ? 3.0291 2.6311 2.7823 0.3665 -0.6633 -0.0175 370 SER A O 2632 C CB . SER A 343 ? 3.0336 2.6959 2.7708 0.4198 -0.6465 -0.0509 370 SER A CB 2633 O OG . SER A 343 ? 3.0853 2.7175 2.8220 0.4230 -0.6552 -0.0627 370 SER A OG 2634 N N . GLU A 344 ? 3.0038 2.5541 2.7522 0.3914 -0.6868 -0.0409 371 GLU A N 2635 C CA . GLU A 344 ? 2.9377 2.4514 2.6993 0.3689 -0.6974 -0.0296 371 GLU A CA 2636 C C . GLU A 344 ? 2.8688 2.3611 2.6339 0.3722 -0.7042 -0.0434 371 GLU A C 2637 O O . GLU A 344 ? 2.9261 2.3765 2.6988 0.3702 -0.7228 -0.0469 371 GLU A O 2638 C CB . GLU A 344 ? 2.9274 2.4059 2.6943 0.3650 -0.7147 -0.0212 371 GLU A CB 2639 C CG . GLU A 344 ? 2.8765 2.3764 2.6359 0.3701 -0.7095 -0.0135 371 GLU A CG 2640 C CD . GLU A 344 ? 2.8577 2.3312 2.6262 0.3563 -0.7210 0.0051 371 GLU A CD 2641 O OE1 . GLU A 344 ? 2.8814 2.3150 2.6623 0.3493 -0.7375 0.0079 371 GLU A OE1 2642 O OE2 . GLU A 344 ? 2.8292 2.3234 2.5937 0.3523 -0.7137 0.0177 371 GLU A OE2 2643 N N . GLU A 345 ? 2.7108 2.2332 2.4718 0.3769 -0.6895 -0.0506 372 GLU A N 2644 C CA . GLU A 345 ? 2.5273 2.0371 2.2893 0.3824 -0.6930 -0.0648 372 GLU A CA 2645 C C . GLU A 345 ? 2.3968 1.9274 2.1659 0.3647 -0.6784 -0.0558 372 GLU A C 2646 O O . GLU A 345 ? 2.3693 1.9301 2.1396 0.3533 -0.6647 -0.0426 372 GLU A O 2647 C CB . GLU A 345 ? 2.5414 2.0702 2.2878 0.4139 -0.6896 -0.0867 372 GLU A CB 2648 C CG . GLU A 345 ? 2.6100 2.1131 2.3471 0.4341 -0.7067 -0.1001 372 GLU A CG 2649 C CD . GLU A 345 ? 2.6010 2.1213 2.3208 0.4666 -0.7040 -0.1228 372 GLU A CD 2650 O OE1 . GLU A 345 ? 2.5404 2.0988 2.2566 0.4735 -0.6862 -0.1250 372 GLU A OE1 2651 O OE2 . GLU A 345 ? 2.6382 2.1346 2.3477 0.4857 -0.7198 -0.1381 372 GLU A OE2 2652 N N . PRO A 346 ? 2.4851 1.9987 2.2592 0.3621 -0.6826 -0.0636 373 PRO A N 2653 C CA . PRO A 346 ? 2.4537 1.9875 2.2339 0.3470 -0.6689 -0.0567 373 PRO A CA 2654 C C . PRO A 346 ? 2.5892 2.1753 2.3621 0.3570 -0.6484 -0.0589 373 PRO A C 2655 O O . PRO A 346 ? 2.5549 2.1606 2.3175 0.3817 -0.6445 -0.0721 373 PRO A O 2656 C CB . PRO A 346 ? 2.2925 1.8010 2.0757 0.3517 -0.6782 -0.0706 373 PRO A CB 2657 C CG . PRO A 346 ? 2.3239 1.7863 2.1110 0.3548 -0.7011 -0.0756 373 PRO A CG 2658 C CD . PRO A 346 ? 2.4613 1.9323 2.2377 0.3700 -0.7025 -0.0779 373 PRO A CD 2659 N N . TYR A 347 ? 2.7509 2.3619 2.5317 0.3341 -0.6298 -0.0458 374 TYR A N 2660 C CA . TYR A 347 ? 2.8755 2.5370 2.6562 0.3366 -0.6078 -0.0448 374 TYR A CA 2661 C C . TYR A 347 ? 3.0263 2.7066 2.8036 0.3563 -0.6038 -0.0576 374 TYR A C 2662 O O . TYR A 347 ? 3.1038 2.7640 2.8835 0.3527 -0.6074 -0.0637 374 TYR A O 2663 C CB . TYR A 347 ? 2.8262 2.5043 2.6188 0.3043 -0.5871 -0.0312 374 TYR A CB 2664 C CG . TYR A 347 ? 2.8027 2.4734 2.5970 0.2868 -0.5872 -0.0175 374 TYR A CG 2665 C CD1 . TYR A 347 ? 2.7714 2.4729 2.5647 0.2872 -0.5787 -0.0119 374 TYR A CD1 2666 C CD2 . TYR A 347 ? 2.7977 2.4327 2.5958 0.2703 -0.5958 -0.0088 374 TYR A CD2 2667 C CE1 . TYR A 347 ? 2.7566 2.4525 2.5495 0.2732 -0.5791 -0.0002 374 TYR A CE1 2668 C CE2 . TYR A 347 ? 2.7827 2.4147 2.5814 0.2565 -0.5949 0.0052 374 TYR A CE2 2669 C CZ . TYR A 347 ? 2.7587 2.4207 2.5532 0.2587 -0.5866 0.0084 374 TYR A CZ 2670 O OH . TYR A 347 ? 2.7520 2.4120 2.5452 0.2470 -0.5862 0.0214 374 TYR A OH 2671 N N . LYS A 348 ? 3.0838 2.8046 2.8563 0.3777 -0.5962 -0.0603 375 LYS A N 2672 C CA . LYS A 348 ? 3.1022 2.8517 2.8731 0.3960 -0.5874 -0.0684 375 LYS A CA 2673 C C . LYS A 348 ? 3.0750 2.8541 2.8619 0.3713 -0.5639 -0.0580 375 LYS A C 2674 O O . LYS A 348 ? 3.1020 2.9053 2.8993 0.3542 -0.5509 -0.0457 375 LYS A O 2675 C CB . LYS A 348 ? 3.0967 2.8851 2.8612 0.4233 -0.5786 -0.0720 375 LYS A CB 2676 C CG . LYS A 348 ? 3.1239 2.8886 2.8724 0.4481 -0.5902 -0.0881 375 LYS A CG 2677 C CD . LYS A 348 ? 3.0800 2.8909 2.8219 0.4769 -0.5780 -0.0911 375 LYS A CD 2678 C CE . LYS A 348 ? 3.0822 2.8702 2.8054 0.5038 -0.5901 -0.1093 375 LYS A CE 2679 N NZ . LYS A 348 ? 3.0878 2.8470 2.8080 0.4987 -0.6037 -0.1079 375 LYS A NZ 2680 N N . GLU A 349 ? 2.9711 2.7475 2.7604 0.3696 -0.5592 -0.0636 376 GLU A N 2681 C CA . GLU A 349 ? 2.7781 2.5772 2.5834 0.3442 -0.5381 -0.0541 376 GLU A CA 2682 C C . GLU A 349 ? 2.7642 2.6104 2.5752 0.3592 -0.5233 -0.0532 376 GLU A C 2683 O O . GLU A 349 ? 2.8330 2.6837 2.6336 0.3868 -0.5291 -0.0638 376 GLU A O 2684 C CB . GLU A 349 ? 2.5983 2.3606 2.4066 0.3233 -0.5406 -0.0566 376 GLU A CB 2685 C CG . GLU A 349 ? 2.4279 2.1537 2.2379 0.3000 -0.5485 -0.0498 376 GLU A CG 2686 C CD . GLU A 349 ? 2.1976 1.8970 2.0150 0.2767 -0.5466 -0.0477 376 GLU A CD 2687 O OE1 . GLU A 349 ? 2.0644 1.7759 1.8863 0.2748 -0.5366 -0.0513 376 GLU A OE1 2688 O OE2 . GLU A 349 ? 2.1239 1.7924 1.9433 0.2607 -0.5547 -0.0411 376 GLU A OE2 2689 N N . ILE A 350 ? 2.7061 2.5879 2.5345 0.3415 -0.5053 -0.0399 377 ILE A N 2690 C CA . ILE A 350 ? 2.7145 2.6418 2.5559 0.3474 -0.4890 -0.0339 377 ILE A CA 2691 C C . ILE A 350 ? 2.7199 2.6400 2.5741 0.3186 -0.4774 -0.0304 377 ILE A C 2692 O O . ILE A 350 ? 2.7457 2.6552 2.6086 0.2905 -0.4734 -0.0238 377 ILE A O 2693 C CB . ILE A 350 ? 2.6623 2.6382 2.5197 0.3487 -0.4788 -0.0192 377 ILE A CB 2694 C CG1 . ILE A 350 ? 2.6421 2.6235 2.4867 0.3745 -0.4904 -0.0216 377 ILE A CG1 2695 C CG2 . ILE A 350 ? 2.6573 2.6829 2.5311 0.3575 -0.4633 -0.0101 377 ILE A CG2 2696 C CD1 . ILE A 350 ? 2.5997 2.6292 2.4618 0.3759 -0.4818 -0.0061 377 ILE A CD1 2697 N N . ASP A 351 ? 2.6954 2.6223 2.5495 0.3273 -0.4724 -0.0352 378 ASP A N 2698 C CA . ASP A 351 ? 2.5442 2.4586 2.4075 0.3023 -0.4635 -0.0342 378 ASP A CA 2699 C C . ASP A 351 ? 2.4924 2.4516 2.3767 0.2957 -0.4448 -0.0226 378 ASP A C 2700 O O . ASP A 351 ? 2.4828 2.4849 2.3744 0.3150 -0.4388 -0.0154 378 ASP A O 2701 C CB . ASP A 351 ? 2.5157 2.3974 2.3646 0.3131 -0.4734 -0.0487 378 ASP A CB 2702 C CG . ASP A 351 ? 2.4885 2.3509 2.3454 0.2863 -0.4663 -0.0481 378 ASP A CG 2703 O OD1 . ASP A 351 ? 2.4379 2.2952 2.3049 0.2582 -0.4595 -0.0395 378 ASP A OD1 2704 O OD2 . ASP A 351 ? 2.5136 2.3666 2.3657 0.2948 -0.4681 -0.0567 378 ASP A OD2 2705 N N . GLY A 352 ? 2.4514 2.4017 2.3471 0.2685 -0.4360 -0.0194 379 GLY A N 2706 C CA . GLY A 352 ? 2.2982 2.2831 2.2141 0.2614 -0.4203 -0.0100 379 GLY A CA 2707 C C . GLY A 352 ? 2.1351 2.1594 2.0755 0.2513 -0.4115 0.0061 379 GLY A C 2708 O O . GLY A 352 ? 2.1699 2.2337 2.1296 0.2552 -0.4005 0.0169 379 GLY A O 2709 N N . ILE A 353 ? 1.9786 1.9927 1.9201 0.2383 -0.4172 0.0086 380 ILE A N 2710 C CA . ILE A 353 ? 1.9486 1.9955 1.9152 0.2264 -0.4122 0.0227 380 ILE A CA 2711 C C . ILE A 353 ? 2.0127 2.0516 1.9946 0.1968 -0.4062 0.0256 380 ILE A C 2712 O O . ILE A 353 ? 2.0578 2.0676 2.0324 0.1786 -0.4111 0.0207 380 ILE A O 2713 C CB . ILE A 353 ? 1.8817 1.9221 1.8421 0.2269 -0.4222 0.0232 380 ILE A CB 2714 C CG1 . ILE A 353 ? 1.8630 1.9108 1.8074 0.2583 -0.4290 0.0196 380 ILE A CG1 2715 C CG2 . ILE A 353 ? 1.8049 1.8781 1.7934 0.2143 -0.4194 0.0373 380 ILE A CG2 2716 C CD1 . ILE A 353 ? 1.8572 1.8815 1.7856 0.2606 -0.4414 0.0147 380 ILE A CD1 2717 N N . ALA A 354 ? 2.0046 2.0710 2.0075 0.1937 -0.3957 0.0339 381 ALA A N 2718 C CA . ALA A 354 ? 2.0163 2.0739 2.0327 0.1686 -0.3902 0.0349 381 ALA A CA 2719 C C . ALA A 354 ? 2.1295 2.1952 2.1667 0.1485 -0.3937 0.0422 381 ALA A C 2720 O O . ALA A 354 ? 2.1091 2.1629 2.1547 0.1280 -0.3922 0.0408 381 ALA A O 2721 C CB . ALA A 354 ? 1.8858 1.9713 1.9196 0.1730 -0.3789 0.0425 381 ALA A CB 2722 N N . THR A 355 ? 2.1944 2.2798 2.2395 0.1557 -0.3996 0.0493 382 THR A N 2723 C CA . THR A 355 ? 2.1692 2.2613 2.2339 0.1386 -0.4061 0.0550 382 THR A CA 2724 C C . THR A 355 ? 2.2265 2.2947 2.2698 0.1390 -0.4167 0.0471 382 THR A C 2725 O O . THR A 355 ? 2.3006 2.3503 2.3175 0.1531 -0.4191 0.0394 382 THR A O 2726 C CB . THR A 355 ? 2.1115 2.2532 2.2127 0.1434 -0.4049 0.0739 382 THR A CB 2727 O OG1 . THR A 355 ? 2.1286 2.2904 2.2219 0.1675 -0.4057 0.0782 382 THR A OG1 2728 C CG2 . THR A 355 ? 2.0793 2.2481 2.2052 0.1424 -0.3940 0.0851 382 THR A CG2 2729 N N . THR A 356 ? 2.1735 2.2416 2.2288 0.1243 -0.4245 0.0488 383 THR A N 2730 C CA . THR A 356 ? 2.0709 2.1191 2.1070 0.1246 -0.4346 0.0424 383 THR A CA 2731 C C . THR A 356 ? 1.9494 2.0266 1.9975 0.1374 -0.4402 0.0517 383 THR A C 2732 O O . THR A 356 ? 1.9394 2.0100 1.9823 0.1349 -0.4499 0.0497 383 THR A O 2733 C CB . THR A 356 ? 2.0567 2.0873 2.0943 0.1046 -0.4417 0.0369 383 THR A CB 2734 O OG1 . THR A 356 ? 2.0531 2.1105 2.1267 0.0945 -0.4453 0.0459 383 THR A OG1 2735 C CG2 . THR A 356 ? 2.0312 2.0318 2.0518 0.0941 -0.4362 0.0274 383 THR A CG2 2736 N N . ARG A 357 ? 1.8758 1.9874 1.9396 0.1524 -0.4338 0.0625 384 ARG A N 2737 C CA . ARG A 357 ? 1.8888 2.0323 1.9632 0.1683 -0.4375 0.0728 384 ARG A CA 2738 C C . ARG A 357 ? 1.9555 2.1164 2.0193 0.1950 -0.4303 0.0752 384 ARG A C 2739 O O . ARG A 357 ? 1.9646 2.1369 2.0339 0.1996 -0.4207 0.0779 384 ARG A O 2740 C CB . ARG A 357 ? 1.8967 2.0805 2.0151 0.1587 -0.4394 0.0902 384 ARG A CB 2741 C CG . ARG A 357 ? 1.9258 2.1516 2.0606 0.1766 -0.4407 0.1051 384 ARG A CG 2742 C CD . ARG A 357 ? 1.9290 2.1878 2.1086 0.1632 -0.4476 0.1221 384 ARG A CD 2743 N NE . ARG A 357 ? 1.9711 2.2748 2.1689 0.1811 -0.4476 0.1391 384 ARG A NE 2744 C CZ . ARG A 357 ? 2.0360 2.3565 2.2549 0.1765 -0.4587 0.1477 384 ARG A CZ 2745 N NH1 . ARG A 357 ? 2.0375 2.3324 2.2607 0.1555 -0.4720 0.1392 384 ARG A NH1 2746 N NH2 . ARG A 357 ? 2.0691 2.4334 2.3043 0.1945 -0.4572 0.1646 384 ARG A NH2 2747 N N . TYR A 358 ? 2.0332 2.1960 2.0805 0.2142 -0.4357 0.0733 385 TYR A N 2748 C CA . TYR A 358 ? 2.1106 2.2885 2.1440 0.2437 -0.4315 0.0730 385 TYR A CA 2749 C C . TYR A 358 ? 2.1359 2.3302 2.1620 0.2652 -0.4382 0.0761 385 TYR A C 2750 O O . TYR A 358 ? 2.1275 2.2962 2.1384 0.2611 -0.4481 0.0687 385 TYR A O 2751 C CB . TYR A 358 ? 2.1480 2.2819 2.1478 0.2488 -0.4325 0.0552 385 TYR A CB 2752 C CG . TYR A 358 ? 2.1271 2.2753 2.1157 0.2771 -0.4278 0.0530 385 TYR A CG 2753 C CD1 . TYR A 358 ? 2.1462 2.2833 2.1085 0.3037 -0.4359 0.0436 385 TYR A CD1 2754 C CD2 . TYR A 358 ? 2.0563 2.2289 2.0600 0.2787 -0.4163 0.0597 385 TYR A CD2 2755 C CE1 . TYR A 358 ? 2.1121 2.2614 2.0616 0.3327 -0.4338 0.0392 385 TYR A CE1 2756 C CE2 . TYR A 358 ? 2.0289 2.2161 2.0201 0.3072 -0.4126 0.0568 385 TYR A CE2 2757 C CZ . TYR A 358 ? 2.0338 2.2091 1.9971 0.3349 -0.4218 0.0457 385 TYR A CZ 2758 O OH . TYR A 358 ? 2.0319 2.2212 1.9805 0.3662 -0.4201 0.0407 385 TYR A OH 2759 N N . SER A 359 ? 2.1465 2.3854 2.1827 0.2898 -0.4324 0.0875 386 SER A N 2760 C CA . SER A 359 ? 2.1691 2.4292 2.1989 0.3139 -0.4378 0.0915 386 SER A CA 2761 C C . SER A 359 ? 2.2431 2.4829 2.2353 0.3440 -0.4420 0.0760 386 SER A C 2762 O O . SER A 359 ? 2.2010 2.4648 2.1891 0.3684 -0.4356 0.0777 386 SER A O 2763 C CB . SER A 359 ? 2.1390 2.4658 2.2040 0.3255 -0.4297 0.1158 386 SER A CB 2764 O OG . SER A 359 ? 2.1235 2.4677 2.2269 0.2979 -0.4299 0.1306 386 SER A OG 2765 N N . VAL A 360 ? 2.3626 2.5582 2.3280 0.3432 -0.4541 0.0612 387 VAL A N 2766 C CA . VAL A 360 ? 2.4484 2.6197 2.3801 0.3711 -0.4629 0.0460 387 VAL A CA 2767 C C . VAL A 360 ? 2.5997 2.8129 2.5307 0.4046 -0.4639 0.0534 387 VAL A C 2768 O O . VAL A 360 ? 2.6328 2.8571 2.5690 0.4048 -0.4690 0.0596 387 VAL A O 2769 C CB . VAL A 360 ? 2.3759 2.4915 2.2843 0.3602 -0.4765 0.0321 387 VAL A CB 2770 C CG1 . VAL A 360 ? 2.3740 2.4627 2.2513 0.3892 -0.4887 0.0169 387 VAL A CG1 2771 C CG2 . VAL A 360 ? 2.3387 2.4166 2.2472 0.3292 -0.4747 0.0266 387 VAL A CG2 2772 N N . ALA A 361 ? 2.7268 2.9647 2.6502 0.4344 -0.4593 0.0525 388 ALA A N 2773 C CA . ALA A 361 ? 2.7803 3.0649 2.7039 0.4678 -0.4561 0.0613 388 ALA A CA 2774 C C . ALA A 361 ? 2.9503 3.2043 2.8383 0.4925 -0.4591 0.0409 388 ALA A C 2775 O O . ALA A 361 ? 2.9292 3.1427 2.7960 0.4951 -0.4644 0.0231 388 ALA A O 2776 C CB . ALA A 361 ? 2.7292 3.0732 2.6779 0.4767 -0.4380 0.0800 388 ALA A CB 2777 N N . GLY A 362 ? 3.1400 3.4131 3.0230 0.5106 -0.4570 0.0435 389 GLY A N 2778 C CA . GLY A 362 ? 3.3012 3.5501 3.1520 0.5369 -0.4606 0.0242 389 GLY A CA 2779 C C . GLY A 362 ? 3.4601 3.6733 3.2953 0.5358 -0.4750 0.0145 389 GLY A C 2780 O O . GLY A 362 ? 3.5416 3.7265 3.3502 0.5556 -0.4818 -0.0034 389 GLY A O 2781 N N . LEU A 363 ? 3.5246 3.7391 3.3766 0.5133 -0.4803 0.0259 390 LEU A N 2782 C CA . LEU A 363 ? 3.5059 3.6842 3.3444 0.5081 -0.4943 0.0183 390 LEU A CA 2783 C C . LEU A 363 ? 3.4983 3.7043 3.3337 0.5296 -0.4910 0.0223 390 LEU A C 2784 O O . LEU A 363 ? 3.4959 3.7584 3.3499 0.5400 -0.4775 0.0386 390 LEU A O 2785 C CB . LEU A 363 ? 3.4701 3.6410 3.3261 0.4772 -0.5011 0.0283 390 LEU A CB 2786 C CG . LEU A 363 ? 3.4585 3.6083 3.3208 0.4543 -0.5035 0.0268 390 LEU A CG 2787 C CD1 . LEU A 363 ? 3.4404 3.5924 3.3234 0.4233 -0.5054 0.0377 390 LEU A CD1 2788 C CD2 . LEU A 363 ? 3.4860 3.5735 3.3224 0.4517 -0.5148 0.0073 390 LEU A CD2 2789 N N . SER A 364 ? 3.2631 3.4293 3.0764 0.5358 -0.5035 0.0085 391 SER A N 2790 C CA . SER A 364 ? 3.1355 3.3217 2.9434 0.5554 -0.5025 0.0103 391 SER A CA 2791 C C . SER A 364 ? 3.1741 3.3932 3.0066 0.5402 -0.5007 0.0303 391 SER A C 2792 O O . SER A 364 ? 3.2544 3.4588 3.0985 0.5135 -0.5072 0.0356 391 SER A O 2793 C CB . SER A 364 ? 3.0619 3.1924 2.8409 0.5646 -0.5184 -0.0101 391 SER A CB 2794 O OG . SER A 364 ? 3.0848 3.2022 2.8412 0.5914 -0.5190 -0.0279 391 SER A OG 2795 N N . PRO A 365 ? 3.1055 3.3697 2.9462 0.5575 -0.4924 0.0412 392 PRO A N 2796 C CA . PRO A 365 ? 3.1510 3.4480 3.0167 0.5449 -0.4920 0.0602 392 PRO A CA 2797 C C . PRO A 365 ? 3.2274 3.4831 3.0794 0.5349 -0.5072 0.0519 392 PRO A C 2798 O O . PRO A 365 ? 3.2374 3.4549 3.0615 0.5490 -0.5151 0.0347 392 PRO A O 2799 C CB . PRO A 365 ? 3.1574 3.5074 3.0300 0.5706 -0.4796 0.0710 392 PRO A CB 2800 C CG . PRO A 365 ? 3.1645 3.5196 3.0213 0.5937 -0.4701 0.0614 392 PRO A CG 2801 C CD . PRO A 365 ? 3.1402 3.4295 2.9681 0.5904 -0.4827 0.0366 392 PRO A CD 2802 N N . TYR A 366 ? 3.2341 3.4967 3.1058 0.5113 -0.5122 0.0638 393 TYR A N 2803 C CA . TYR A 366 ? 3.2437 3.4744 3.1047 0.5017 -0.5251 0.0590 393 TYR A CA 2804 C C . TYR A 366 ? 3.2482 3.4125 3.0812 0.4954 -0.5369 0.0399 393 TYR A C 2805 O O . TYR A 366 ? 3.2884 3.4201 3.1033 0.4993 -0.5466 0.0316 393 TYR A O 2806 C CB . TYR A 366 ? 3.3228 3.5724 3.1777 0.5233 -0.5240 0.0607 393 TYR A CB 2807 C CG . TYR A 366 ? 3.3396 3.5754 3.1930 0.5133 -0.5346 0.0626 393 TYR A CG 2808 C CD1 . TYR A 366 ? 3.3063 3.5600 3.1834 0.4906 -0.5378 0.0759 393 TYR A CD1 2809 C CD2 . TYR A 366 ? 3.3734 3.5790 3.2020 0.5276 -0.5422 0.0509 393 TYR A CD2 2810 C CE1 . TYR A 366 ? 3.3172 3.5591 3.1915 0.4826 -0.5474 0.0770 393 TYR A CE1 2811 C CE2 . TYR A 366 ? 3.3825 3.5771 3.2096 0.5193 -0.5512 0.0535 393 TYR A CE2 2812 C CZ . TYR A 366 ? 3.3491 3.5624 3.1982 0.4970 -0.5532 0.0665 393 TYR A CZ 2813 O OH . TYR A 366 ? 3.3357 3.5385 3.1819 0.4896 -0.5621 0.0684 393 TYR A OH 2814 N N . SER A 367 ? 3.0401 3.1854 2.8719 0.4853 -0.5361 0.0346 394 SER A N 2815 C CA . SER A 367 ? 2.9247 3.0092 2.7342 0.4786 -0.5470 0.0188 394 SER A CA 2816 C C . SER A 367 ? 2.8616 2.9246 2.6786 0.4488 -0.5520 0.0220 394 SER A C 2817 O O . SER A 367 ? 2.9210 3.0080 2.7559 0.4376 -0.5453 0.0294 394 SER A O 2818 C CB . SER A 367 ? 2.8525 2.9253 2.6490 0.4961 -0.5436 0.0062 394 SER A CB 2819 O OG . SER A 367 ? 2.8386 2.9228 2.6225 0.5252 -0.5415 -0.0006 394 SER A OG 2820 N N . ASP A 368 ? 2.7345 2.7528 2.5381 0.4364 -0.5638 0.0171 395 ASP A N 2821 C CA . ASP A 368 ? 2.6870 2.6812 2.4936 0.4094 -0.5689 0.0194 395 ASP A CA 2822 C C . ASP A 368 ? 2.7653 2.7309 2.5658 0.4046 -0.5693 0.0113 395 ASP A C 2823 O O . ASP A 368 ? 2.8242 2.7726 2.6127 0.4213 -0.5705 0.0009 395 ASP A O 2824 C CB . ASP A 368 ? 2.6627 2.6214 2.4569 0.3994 -0.5802 0.0193 395 ASP A CB 2825 C CG . ASP A 368 ? 2.6365 2.6223 2.4376 0.4001 -0.5806 0.0276 395 ASP A CG 2826 O OD1 . ASP A 368 ? 2.6046 2.6357 2.4252 0.4000 -0.5735 0.0358 395 ASP A OD1 2827 O OD2 . ASP A 368 ? 2.6413 2.6039 2.4303 0.4004 -0.5887 0.0271 395 ASP A OD2 2828 N N . TYR A 369 ? 2.7676 2.7280 2.5778 0.3796 -0.5655 0.0152 396 TYR A N 2829 C CA . TYR A 369 ? 2.7855 2.7186 2.5923 0.3697 -0.5627 0.0089 396 TYR A CA 2830 C C . TYR A 369 ? 2.8567 2.7682 2.6679 0.3371 -0.5583 0.0128 396 TYR A C 2831 O O . TYR A 369 ? 2.8764 2.8042 2.6974 0.3213 -0.5540 0.0203 396 TYR A O 2832 C CB . TYR A 369 ? 2.6896 2.6565 2.5095 0.3763 -0.5505 0.0093 396 TYR A CB 2833 C CG . TYR A 369 ? 2.6399 2.6296 2.4533 0.4108 -0.5520 0.0049 396 TYR A CG 2834 C CD1 . TYR A 369 ? 2.6186 2.6598 2.4460 0.4230 -0.5430 0.0147 396 TYR A CD1 2835 C CD2 . TYR A 369 ? 2.6275 2.5887 2.4242 0.4262 -0.5554 -0.0086 396 TYR A CD2 2836 C CE1 . TYR A 369 ? 2.6154 2.6808 2.4382 0.4505 -0.5357 0.0118 396 TYR A CE1 2837 C CE2 . TYR A 369 ? 2.6281 2.6105 2.4186 0.4544 -0.5496 -0.0144 396 TYR A CE2 2838 C CZ . TYR A 369 ? 2.6209 2.6564 2.4235 0.4667 -0.5388 -0.0037 396 TYR A CZ 2839 O OH . TYR A 369 ? 2.6399 2.6990 2.4352 0.4956 -0.5320 -0.0083 396 TYR A OH 2840 N N . GLU A 370 ? 2.8851 2.7607 2.6890 0.3286 -0.5603 0.0075 397 GLU A N 2841 C CA . GLU A 370 ? 2.8950 2.7512 2.7018 0.3002 -0.5550 0.0116 397 GLU A CA 2842 C C . GLU A 370 ? 2.9290 2.7856 2.7439 0.2899 -0.5448 0.0085 397 GLU A C 2843 O O . GLU A 370 ? 2.9876 2.8270 2.7965 0.3011 -0.5490 0.0011 397 GLU A O 2844 C CB . GLU A 370 ? 2.8756 2.6874 2.6685 0.2964 -0.5672 0.0123 397 GLU A CB 2845 C CG . GLU A 370 ? 2.8264 2.6186 2.6209 0.2705 -0.5616 0.0179 397 GLU A CG 2846 C CD . GLU A 370 ? 2.8295 2.5820 2.6144 0.2675 -0.5736 0.0229 397 GLU A CD 2847 O OE1 . GLU A 370 ? 2.8043 2.5344 2.5909 0.2532 -0.5721 0.0261 397 GLU A OE1 2848 O OE2 . GLU A 370 ? 2.8630 2.6080 2.6404 0.2791 -0.5848 0.0252 397 GLU A OE2 2849 N N . PHE A 371 ? 2.8780 2.7528 2.7062 0.2695 -0.5329 0.0133 398 PHE A N 2850 C CA . PHE A 371 ? 2.8454 2.7259 2.6833 0.2602 -0.5222 0.0111 398 PHE A CA 2851 C C . PHE A 371 ? 2.8738 2.7311 2.7109 0.2354 -0.5174 0.0125 398 PHE A C 2852 O O . PHE A 371 ? 2.8373 2.6895 2.6718 0.2221 -0.5181 0.0173 398 PHE A O 2853 C CB . PHE A 371 ? 2.8021 2.7281 2.6608 0.2590 -0.5118 0.0159 398 PHE A CB 2854 C CG . PHE A 371 ? 2.7853 2.7420 2.6479 0.2847 -0.5131 0.0168 398 PHE A CG 2855 C CD1 . PHE A 371 ? 2.7779 2.7394 2.6372 0.3032 -0.5112 0.0116 398 PHE A CD1 2856 C CD2 . PHE A 371 ? 2.7874 2.7707 2.6567 0.2919 -0.5161 0.0233 398 PHE A CD2 2857 C CE1 . PHE A 371 ? 2.7802 2.7740 2.6413 0.3301 -0.5117 0.0132 398 PHE A CE1 2858 C CE2 . PHE A 371 ? 2.7996 2.8152 2.6729 0.3171 -0.5164 0.0259 398 PHE A CE2 2859 C CZ . PHE A 371 ? 2.7934 2.8153 2.6619 0.3371 -0.5138 0.0211 398 PHE A CZ 2860 N N . ARG A 372 ? 2.9681 2.8139 2.8068 0.2311 -0.5125 0.0085 399 ARG A N 2861 C CA . ARG A 372 ? 3.0096 2.8370 2.8487 0.2091 -0.5066 0.0103 399 ARG A CA 2862 C C . ARG A 372 ? 3.0644 2.9052 2.9154 0.2017 -0.4950 0.0076 399 ARG A C 2863 O O . ARG A 372 ? 3.0692 2.9257 2.9254 0.2158 -0.4928 0.0038 399 ARG A O 2864 C CB . ARG A 372 ? 3.0038 2.7906 2.8310 0.2084 -0.5157 0.0102 399 ARG A CB 2865 C CG . ARG A 372 ? 3.0318 2.8019 2.8488 0.2101 -0.5262 0.0162 399 ARG A CG 2866 C CD . ARG A 372 ? 3.0528 2.7837 2.8641 0.2076 -0.5361 0.0194 399 ARG A CD 2867 N NE . ARG A 372 ? 3.0826 2.7984 2.8862 0.2105 -0.5469 0.0271 399 ARG A NE 2868 C CZ . ARG A 372 ? 3.0842 2.7976 2.8849 0.1967 -0.5439 0.0384 399 ARG A CZ 2869 N NH1 . ARG A 372 ? 3.0917 2.8161 2.8953 0.1800 -0.5312 0.0417 399 ARG A NH1 2870 N NH2 . ARG A 372 ? 3.0708 2.7720 2.8650 0.2012 -0.5540 0.0465 399 ARG A NH2 2871 N N . VAL A 373 ? 3.1243 2.9599 2.9787 0.1812 -0.4875 0.0099 400 VAL A N 2872 C CA . VAL A 373 ? 3.0375 2.8845 2.9038 0.1724 -0.4766 0.0078 400 VAL A CA 2873 C C . VAL A 373 ? 2.9620 2.7811 2.8226 0.1598 -0.4738 0.0068 400 VAL A C 2874 O O . VAL A 373 ? 2.9452 2.7505 2.7997 0.1465 -0.4735 0.0111 400 VAL A O 2875 C CB . VAL A 373 ? 3.0353 2.9088 2.9161 0.1592 -0.4697 0.0111 400 VAL A CB 2876 C CG1 . VAL A 373 ? 3.0210 2.9067 2.9161 0.1512 -0.4593 0.0097 400 VAL A CG1 2877 C CG2 . VAL A 373 ? 3.0804 2.9835 2.9712 0.1697 -0.4733 0.0144 400 VAL A CG2 2878 N N . VAL A 374 ? 2.7959 2.6094 2.6587 0.1653 -0.4716 0.0019 401 VAL A N 2879 C CA . VAL A 374 ? 2.4596 2.2474 2.3194 0.1548 -0.4700 0.0011 401 VAL A CA 2880 C C . VAL A 374 ? 2.4425 2.2447 2.3134 0.1449 -0.4573 -0.0009 401 VAL A C 2881 O O . VAL A 374 ? 2.4868 2.3082 2.3655 0.1549 -0.4534 -0.0045 401 VAL A O 2882 C CB . VAL A 374 ? 2.1142 1.8770 1.9672 0.1694 -0.4811 -0.0042 401 VAL A CB 2883 C CG1 . VAL A 374 ? 2.0432 1.7830 1.8977 0.1581 -0.4795 -0.0046 401 VAL A CG1 2884 C CG2 . VAL A 374 ? 2.0111 1.7537 1.8544 0.1772 -0.4954 -0.0013 401 VAL A CG2 2885 N N . ALA A 375 ? 2.2901 2.0844 2.1614 0.1266 -0.4510 0.0022 402 ALA A N 2886 C CA . ALA A 375 ? 2.2716 2.0790 2.1536 0.1164 -0.4395 0.0004 402 ALA A CA 2887 C C . ALA A 375 ? 2.2718 2.0606 2.1530 0.1144 -0.4374 -0.0026 402 ALA A C 2888 O O . ALA A 375 ? 2.2869 2.0488 2.1603 0.1125 -0.4438 -0.0006 402 ALA A O 2889 C CB . ALA A 375 ? 2.2552 2.0669 2.1377 0.0998 -0.4343 0.0038 402 ALA A CB 2890 N N . VAL A 376 ? 2.0313 1.8354 1.9225 0.1148 -0.4291 -0.0062 403 VAL A N 2891 C CA . VAL A 376 ? 1.8681 1.6569 1.7594 0.1128 -0.4266 -0.0098 403 VAL A CA 2892 C C . VAL A 376 ? 1.7441 1.5484 1.6465 0.1008 -0.4137 -0.0100 403 VAL A C 2893 O O . VAL A 376 ? 1.7894 1.6213 1.7037 0.1031 -0.4077 -0.0094 403 VAL A O 2894 C CB . VAL A 376 ? 1.4308 1.2180 1.3198 0.1338 -0.4332 -0.0168 403 VAL A CB 2895 C CG1 . VAL A 376 ? 1.3525 1.1232 1.2418 0.1318 -0.4322 -0.0215 403 VAL A CG1 2896 C CG2 . VAL A 376 ? 1.4998 1.2682 1.3778 0.1471 -0.4484 -0.0182 403 VAL A CG2 2897 N N . ASN A 377 ? 1.6883 1.4754 1.5887 0.0880 -0.4098 -0.0094 404 ASN A N 2898 C CA . ASN A 377 ? 1.8599 1.6572 1.7697 0.0790 -0.3987 -0.0109 404 ASN A CA 2899 C C . ASN A 377 ? 2.0320 1.8124 1.9404 0.0815 -0.3991 -0.0148 404 ASN A C 2900 O O . ASN A 377 ? 2.0840 1.8535 1.9877 0.0959 -0.4082 -0.0189 404 ASN A O 2901 C CB . ASN A 377 ? 1.9371 1.7340 1.8466 0.0614 -0.3926 -0.0073 404 ASN A CB 2902 C CG . ASN A 377 ? 2.0121 1.7847 1.9101 0.0538 -0.3956 -0.0025 404 ASN A CG 2903 O OD1 . ASN A 377 ? 2.0328 1.7862 1.9286 0.0555 -0.3994 -0.0017 404 ASN A OD1 2904 N ND2 . ASN A 377 ? 2.0178 1.7924 1.9096 0.0461 -0.3946 0.0017 404 ASN A ND2 2905 N N . ASN A 378 ? 2.1082 1.8859 2.0205 0.0686 -0.3905 -0.0143 405 ASN A N 2906 C CA . ASN A 378 ? 2.1397 1.9021 2.0524 0.0694 -0.3908 -0.0177 405 ASN A CA 2907 C C . ASN A 378 ? 2.1334 1.8655 2.0397 0.0653 -0.4005 -0.0139 405 ASN A C 2908 O O . ASN A 378 ? 2.1341 1.8485 2.0406 0.0720 -0.4087 -0.0178 405 ASN A O 2909 C CB . ASN A 378 ? 2.2205 1.9916 2.1407 0.0567 -0.3782 -0.0176 405 ASN A CB 2910 C CG . ASN A 378 ? 2.2974 2.0980 2.2289 0.0601 -0.3698 -0.0192 405 ASN A CG 2911 O OD1 . ASN A 378 ? 2.3577 2.1756 2.2925 0.0707 -0.3724 -0.0187 405 ASN A OD1 2912 N ND2 . ASN A 378 ? 2.2927 2.1006 2.2322 0.0511 -0.3600 -0.0196 405 ASN A ND2 2913 N N . ILE A 379 ? 2.0956 1.8227 1.9976 0.0551 -0.4006 -0.0056 406 ILE A N 2914 C CA . ILE A 379 ? 2.1241 1.8270 2.0240 0.0484 -0.4077 0.0031 406 ILE A CA 2915 C C . ILE A 379 ? 2.1137 1.7977 2.0109 0.0596 -0.4243 0.0038 406 ILE A C 2916 O O . ILE A 379 ? 2.1086 1.7692 2.0101 0.0606 -0.4351 0.0054 406 ILE A O 2917 C CB . ILE A 379 ? 2.2138 1.9220 2.1088 0.0363 -0.4015 0.0137 406 ILE A CB 2918 C CG1 . ILE A 379 ? 2.2140 1.9391 2.1105 0.0269 -0.3874 0.0113 406 ILE A CG1 2919 C CG2 . ILE A 379 ? 2.2602 1.9486 2.1567 0.0290 -0.4070 0.0269 406 ILE A CG2 2920 C CD1 . ILE A 379 ? 2.2143 1.9324 2.1177 0.0210 -0.3825 0.0105 406 ILE A CD1 2921 N N . GLY A 380 ? 2.2100 1.9035 2.1014 0.0679 -0.4276 0.0028 407 GLY A N 2922 C CA . GLY A 380 ? 2.2470 1.9231 2.1348 0.0791 -0.4436 0.0036 407 GLY A CA 2923 C C . GLY A 380 ? 2.2339 1.9259 2.1153 0.0883 -0.4448 0.0020 407 GLY A C 2924 O O . GLY A 380 ? 2.2328 1.9497 2.1144 0.0856 -0.4341 0.0007 407 GLY A O 2925 N N . ARG A 381 ? 2.1951 1.8714 2.0725 0.0992 -0.4595 0.0026 408 ARG A N 2926 C CA . ARG A 381 ? 2.2425 1.9314 2.1137 0.1105 -0.4632 0.0010 408 ARG A CA 2927 C C . ARG A 381 ? 2.2589 1.9478 2.1256 0.1006 -0.4624 0.0128 408 ARG A C 2928 O O . ARG A 381 ? 2.2680 1.9354 2.1343 0.0971 -0.4716 0.0222 408 ARG A O 2929 C CB . ARG A 381 ? 2.2508 1.9223 2.1183 0.1302 -0.4806 -0.0060 408 ARG A CB 2930 C CG . ARG A 381 ? 2.2941 1.9704 2.1545 0.1423 -0.4884 -0.0056 408 ARG A CG 2931 C CD . ARG A 381 ? 2.3309 1.9877 2.1869 0.1639 -0.5069 -0.0148 408 ARG A CD 2932 N NE . ARG A 381 ? 2.3956 2.0448 2.2453 0.1735 -0.5190 -0.0120 408 ARG A NE 2933 C CZ . ARG A 381 ? 2.3983 2.0601 2.2408 0.1949 -0.5245 -0.0200 408 ARG A CZ 2934 N NH1 . ARG A 381 ? 2.3957 2.0808 2.2372 0.2096 -0.5183 -0.0299 408 ARG A NH1 2935 N NH2 . ARG A 381 ? 2.3871 2.0404 2.2239 0.2027 -0.5357 -0.0170 408 ARG A NH2 2936 N N . GLY A 382 ? 2.2100 1.9238 2.0748 0.0965 -0.4525 0.0131 409 GLY A N 2937 C CA . GLY A 382 ? 2.2438 1.9609 2.1020 0.0897 -0.4518 0.0224 409 GLY A CA 2938 C C . GLY A 382 ? 2.3689 2.0779 2.2214 0.1010 -0.4644 0.0252 409 GLY A C 2939 O O . GLY A 382 ? 2.3008 2.0069 2.1538 0.1156 -0.4726 0.0177 409 GLY A O 2940 N N . PRO A 383 ? 2.6362 2.3424 2.4822 0.0961 -0.4662 0.0361 410 PRO A N 2941 C CA . PRO A 383 ? 2.9452 2.6441 2.7857 0.1064 -0.4781 0.0399 410 PRO A CA 2942 C C . PRO A 383 ? 3.4834 3.2043 3.3213 0.1171 -0.4782 0.0311 410 PRO A C 2943 O O . PRO A 383 ? 3.4457 3.1895 3.2868 0.1130 -0.4686 0.0259 410 PRO A O 2944 C CB . PRO A 383 ? 2.6938 2.3916 2.5281 0.0975 -0.4762 0.0549 410 PRO A CB 2945 C CG . PRO A 383 ? 2.5999 2.2963 2.4379 0.0840 -0.4663 0.0608 410 PRO A CG 2946 C CD . PRO A 383 ? 2.6088 2.3180 2.4515 0.0825 -0.4577 0.0466 410 PRO A CD 2947 N N . ALA A 384 ? 3.9594 3.6738 3.7936 0.1306 -0.4898 0.0304 411 ALA A N 2948 C CA . ALA A 384 ? 3.9935 3.7301 3.8268 0.1423 -0.4908 0.0239 411 ALA A CA 2949 C C . ALA A 384 ? 4.0333 3.7889 3.8629 0.1357 -0.4862 0.0282 411 ALA A C 2950 O O . ALA A 384 ? 4.1527 3.9052 3.9778 0.1239 -0.4816 0.0352 411 ALA A O 2951 C CB . ALA A 384 ? 4.0275 3.7508 3.8560 0.1597 -0.5054 0.0223 411 ALA A CB 2952 N N . SER A 385 ? 3.6104 3.3871 3.4421 0.1448 -0.4881 0.0241 412 SER A N 2953 C CA . SER A 385 ? 3.3144 3.1086 3.1437 0.1404 -0.4869 0.0265 412 SER A CA 2954 C C . SER A 385 ? 3.2313 3.0200 3.0510 0.1502 -0.4973 0.0313 412 SER A C 2955 O O . SER A 385 ? 3.3136 3.0895 3.1311 0.1624 -0.5056 0.0310 412 SER A O 2956 C CB . SER A 385 ? 3.2110 3.0355 3.0540 0.1414 -0.4828 0.0206 412 SER A CB 2957 O OG . SER A 385 ? 3.2018 3.0397 3.0473 0.1559 -0.4895 0.0200 412 SER A OG 2958 N N . GLU A 386 ? 3.0901 2.8879 2.9034 0.1461 -0.4978 0.0350 413 GLU A N 2959 C CA . GLU A 386 ? 3.0071 2.8045 2.8119 0.1555 -0.5070 0.0394 413 GLU A CA 2960 C C . GLU A 386 ? 3.1123 2.9268 2.9254 0.1686 -0.5115 0.0334 413 GLU A C 2961 O O . GLU A 386 ? 3.1291 2.9675 2.9547 0.1668 -0.5071 0.0284 413 GLU A O 2962 C CB . GLU A 386 ? 2.8228 2.6317 2.6194 0.1501 -0.5065 0.0424 413 GLU A CB 2963 C CG . GLU A 386 ? 2.6601 2.4646 2.4446 0.1584 -0.5151 0.0497 413 GLU A CG 2964 C CD . GLU A 386 ? 2.4896 2.2695 2.2653 0.1573 -0.5170 0.0623 413 GLU A CD 2965 O OE1 . GLU A 386 ? 2.4528 2.2236 2.2227 0.1659 -0.5258 0.0692 413 GLU A OE1 2966 O OE2 . GLU A 386 ? 2.3940 2.1645 2.1704 0.1476 -0.5103 0.0667 413 GLU A OE2 2967 N N . PRO A 387 ? 3.2111 3.0143 3.0186 0.1825 -0.5209 0.0350 414 PRO A N 2968 C CA . PRO A 387 ? 3.2786 3.0976 3.0927 0.1984 -0.5246 0.0295 414 PRO A CA 2969 C C . PRO A 387 ? 3.3572 3.2064 3.1776 0.2019 -0.5256 0.0297 414 PRO A C 2970 O O . PRO A 387 ? 3.4665 3.3177 3.2810 0.1962 -0.5282 0.0333 414 PRO A O 2971 C CB . PRO A 387 ? 3.2982 3.0921 3.1017 0.2124 -0.5366 0.0311 414 PRO A CB 2972 C CG . PRO A 387 ? 3.3075 3.0835 3.1011 0.2035 -0.5400 0.0406 414 PRO A CG 2973 C CD . PRO A 387 ? 3.2631 3.0399 3.0588 0.1850 -0.5292 0.0432 414 PRO A CD 2974 N N . VAL A 388 ? 3.3139 3.1883 3.1470 0.2119 -0.5241 0.0267 415 VAL A N 2975 C CA . VAL A 388 ? 3.0144 2.9188 2.8572 0.2168 -0.5270 0.0289 415 VAL A CA 2976 C C . VAL A 388 ? 2.8906 2.8004 2.7290 0.2392 -0.5343 0.0290 415 VAL A C 2977 O O . VAL A 388 ? 2.9168 2.8248 2.7544 0.2529 -0.5340 0.0256 415 VAL A O 2978 C CB . VAL A 388 ? 2.3183 2.2557 2.1852 0.2096 -0.5195 0.0294 415 VAL A CB 2979 C CG1 . VAL A 388 ? 2.2887 2.2384 2.1651 0.2202 -0.5134 0.0283 415 VAL A CG1 2980 C CG2 . VAL A 388 ? 2.3061 2.2735 2.1868 0.2117 -0.5247 0.0336 415 VAL A CG2 2981 N N . LEU A 389 ? 2.7638 2.6795 2.5976 0.2443 -0.5419 0.0322 416 LEU A N 2982 C CA . LEU A 389 ? 2.5234 2.4454 2.3522 0.2661 -0.5497 0.0325 416 LEU A CA 2983 C C . LEU A 389 ? 2.4995 2.4654 2.3479 0.2732 -0.5475 0.0362 416 LEU A C 2984 O O . LEU A 389 ? 2.4723 2.4569 2.3337 0.2607 -0.5469 0.0398 416 LEU A O 2985 C CB . LEU A 389 ? 2.2690 2.1719 2.0816 0.2686 -0.5597 0.0353 416 LEU A CB 2986 C CG . LEU A 389 ? 2.0749 1.9358 1.8697 0.2677 -0.5656 0.0358 416 LEU A CG 2987 C CD1 . LEU A 389 ? 2.0341 1.8849 1.8168 0.2716 -0.5750 0.0413 416 LEU A CD1 2988 C CD2 . LEU A 389 ? 2.0252 1.8699 1.8157 0.2844 -0.5706 0.0301 416 LEU A CD2 2989 N N . THR A 390 ? 2.5133 2.4970 2.3651 0.2940 -0.5474 0.0359 417 THR A N 2990 C CA . THR A 390 ? 2.6249 2.6546 2.4974 0.3022 -0.5456 0.0432 417 THR A CA 2991 C C . THR A 390 ? 2.6261 2.6733 2.4941 0.3318 -0.5482 0.0434 417 THR A C 2992 O O . THR A 390 ? 2.6615 2.6813 2.5083 0.3473 -0.5540 0.0356 417 THR A O 2993 C CB . THR A 390 ? 2.7320 2.7914 2.6317 0.2891 -0.5351 0.0484 417 THR A CB 2994 O OG1 . THR A 390 ? 2.8454 2.9501 2.7703 0.2937 -0.5352 0.0590 417 THR A OG1 2995 C CG2 . THR A 390 ? 2.7682 2.8286 2.6673 0.2987 -0.5272 0.0454 417 THR A CG2 2996 N N . GLN A 391 ? 2.5868 2.6807 2.4761 0.3403 -0.5451 0.0528 418 GLN A N 2997 C CA . GLN A 391 ? 2.5129 2.6323 2.3991 0.3709 -0.5468 0.0550 418 GLN A CA 2998 C C . GLN A 391 ? 2.5038 2.6756 2.4176 0.3779 -0.5357 0.0665 418 GLN A C 2999 O O . GLN A 391 ? 2.4899 2.6907 2.4331 0.3601 -0.5311 0.0778 418 GLN A O 3000 C CB . GLN A 391 ? 2.3782 2.5068 2.2613 0.3799 -0.5561 0.0589 418 GLN A CB 3001 C CG . GLN A 391 ? 2.2776 2.4324 2.1570 0.4097 -0.5535 0.0610 418 GLN A CG 3002 C CD . GLN A 391 ? 2.2430 2.3999 2.1173 0.4149 -0.5593 0.0633 418 GLN A CD 3003 O OE1 . GLN A 391 ? 2.2336 2.4339 2.1282 0.4198 -0.5564 0.0752 418 GLN A OE1 3004 N NE2 . GLN A 391 ? 2.2558 2.3667 2.1050 0.4136 -0.5678 0.0535 418 GLN A NE2 3005 N N . CYS B 29 ? 1.7361 1.6633 1.4261 -0.1862 0.1917 0.2697 29 CYS B N 3006 C CA . CYS B 29 ? 1.7242 1.6586 1.4896 -0.1780 0.1754 0.2778 29 CYS B CA 3007 C C . CYS B 29 ? 1.7610 1.7009 1.5700 -0.1774 0.1981 0.2959 29 CYS B C 3008 O O . CYS B 29 ? 1.7214 1.6666 1.5735 -0.1697 0.2137 0.2825 29 CYS B O 3009 C CB . CYS B 29 ? 1.7389 1.6729 1.5096 -0.1801 0.1388 0.2961 29 CYS B CB 3010 S SG . CYS B 29 ? 1.3793 1.3187 1.2331 -0.1738 0.1224 0.3174 29 CYS B SG 3011 N N . LYS B 30 ? 1.8437 1.7826 1.6409 -0.1860 0.1993 0.3273 30 LYS B N 3012 C CA . LYS B 30 ? 1.8688 1.8133 1.7230 -0.1860 0.2097 0.3494 30 LYS B CA 3013 C C . LYS B 30 ? 1.8600 1.8116 1.7328 -0.1853 0.2493 0.3455 30 LYS B C 3014 O O . LYS B 30 ? 1.9166 1.8754 1.8553 -0.1817 0.2538 0.3531 30 LYS B O 3015 C CB . LYS B 30 ? 1.9537 1.8938 1.7873 -0.1967 0.2023 0.3868 30 LYS B CB 3016 C CG . LYS B 30 ? 1.9218 1.8611 1.8165 -0.1939 0.1726 0.4058 30 LYS B CG 3017 C CD . LYS B 30 ? 1.8174 1.7626 1.7904 -0.1861 0.1802 0.3987 30 LYS B CD 3018 C CE . LYS B 30 ? 1.6452 1.5936 1.6673 -0.1748 0.1551 0.3783 30 LYS B CE 3019 N NZ . LYS B 30 ? 1.6406 1.5830 1.6704 -0.1734 0.1180 0.3882 30 LYS B NZ 3020 N N . ILE B 31 ? 1.7623 1.7124 1.5811 -0.1884 0.2776 0.3327 31 ILE B N 3021 C CA . ILE B 31 ? 1.6240 1.5827 1.4559 -0.1892 0.3150 0.3309 31 ILE B CA 3022 C C . ILE B 31 ? 1.5895 1.5572 1.4860 -0.1769 0.3245 0.3087 31 ILE B C 3023 O O . ILE B 31 ? 1.5085 1.4877 1.4592 -0.1749 0.3317 0.3131 31 ILE B O 3024 C CB . ILE B 31 ? 1.6150 1.5728 1.3712 -0.1950 0.3400 0.3204 31 ILE B CB 3025 C CG1 . ILE B 31 ? 1.6111 1.5858 1.3917 -0.1931 0.3712 0.3134 31 ILE B CG1 3026 C CG2 . ILE B 31 ? 1.6061 1.5508 1.3214 -0.1902 0.3395 0.2905 31 ILE B CG2 3027 C CD1 . ILE B 31 ? 1.6903 1.6714 1.4057 -0.1992 0.3944 0.3131 31 ILE B CD1 3028 N N . ARG B 32 ? 1.6448 1.6072 1.5363 -0.1687 0.3201 0.2823 32 ARG B N 3029 C CA . ARG B 32 ? 1.5586 1.5278 1.5072 -0.1568 0.3273 0.2620 32 ARG B CA 3030 C C . ARG B 32 ? 1.4813 1.4495 1.4679 -0.1488 0.2905 0.2519 32 ARG B C 3031 O O . ARG B 32 ? 1.5879 1.5571 1.5994 -0.1390 0.2886 0.2294 32 ARG B O 3032 C CB . ARG B 32 ? 1.6035 1.5682 1.5176 -0.1525 0.3517 0.2343 32 ARG B CB 3033 C CG . ARG B 32 ? 1.7543 1.7311 1.6770 -0.1508 0.3842 0.2307 32 ARG B CG 3034 C CD . ARG B 32 ? 1.7960 1.7860 1.7991 -0.1398 0.3876 0.2248 32 ARG B CD 3035 N NE . ARG B 32 ? 1.8876 1.8868 1.8970 -0.1344 0.4180 0.2121 32 ARG B NE 3036 C CZ . ARG B 32 ? 1.9264 1.9398 1.9512 -0.1378 0.4350 0.2248 32 ARG B CZ 3037 N NH1 . ARG B 32 ? 1.9214 1.9401 1.9561 -0.1475 0.4241 0.2508 32 ARG B NH1 3038 N NH2 . ARG B 32 ? 1.9420 1.9637 1.9740 -0.1317 0.4630 0.2115 32 ARG B NH2 3039 N N . CYS B 33 ? 1.4482 1.4142 1.4394 -0.1528 0.2620 0.2691 33 CYS B N 3040 C CA . CYS B 33 ? 1.3193 1.2835 1.3340 -0.1459 0.2269 0.2584 33 CYS B CA 3041 C C . CYS B 33 ? 1.3407 1.3042 1.3760 -0.1499 0.2010 0.2826 33 CYS B C 3042 O O . CYS B 33 ? 1.4308 1.3915 1.4414 -0.1596 0.2066 0.3070 33 CYS B O 3043 C CB . CYS B 33 ? 1.2038 1.1596 1.1632 -0.1459 0.2170 0.2383 33 CYS B CB 3044 S SG . CYS B 33 ? 1.8150 1.7710 1.8002 -0.1365 0.1827 0.2187 33 CYS B SG 3045 N N . LEU B 34 ? 1.2347 1.2000 1.3149 -0.1424 0.1734 0.2764 34 LEU B N 3046 C CA . LEU B 34 ? 1.2506 1.2138 1.3567 -0.1450 0.1492 0.2979 34 LEU B CA 3047 C C . LEU B 34 ? 1.1929 1.1522 1.2830 -0.1418 0.1173 0.2900 34 LEU B C 3048 O O . LEU B 34 ? 1.0846 1.0466 1.1891 -0.1331 0.1050 0.2670 34 LEU B O 3049 C CB . LEU B 34 ? 1.3378 1.3068 1.5201 -0.1396 0.1439 0.3010 34 LEU B CB 3050 C CG . LEU B 34 ? 1.3990 1.3721 1.6253 -0.1276 0.1243 0.2777 34 LEU B CG 3051 C CD1 . LEU B 34 ? 1.4318 1.4010 1.6829 -0.1246 0.0910 0.2823 34 LEU B CD1 3052 C CD2 . LEU B 34 ? 1.4101 1.3914 1.6930 -0.1232 0.1365 0.2733 34 LEU B CD2 3053 N N . CYS B 35 ? 1.2629 1.2165 1.3235 -0.1490 0.1039 0.3100 35 CYS B N 3054 C CA . CYS B 35 ? 1.1986 1.1504 1.2446 -0.1462 0.0743 0.3031 35 CYS B CA 3055 C C . CYS B 35 ? 1.1386 1.0882 1.2274 -0.1439 0.0471 0.3206 35 CYS B C 3056 O O . CYS B 35 ? 1.1097 1.0539 1.1998 -0.1509 0.0466 0.3492 35 CYS B O 3057 C CB . CYS B 35 ? 1.2222 1.1693 1.1959 -0.1552 0.0752 0.3081 35 CYS B CB 3058 S SG . CYS B 35 ? 1.5912 1.5375 1.5100 -0.1579 0.1052 0.2839 35 CYS B SG 3059 N N . GLU B 36 ? 1.1533 1.1067 1.2777 -0.1339 0.0253 0.3032 36 GLU B N 3060 C CA . GLU B 36 ? 1.2214 1.1724 1.3870 -0.1296 -0.0023 0.3142 36 GLU B CA 3061 C C . GLU B 36 ? 1.2208 1.1733 1.3623 -0.1278 -0.0265 0.3096 36 GLU B C 3062 O O . GLU B 36 ? 1.1350 1.0943 1.2685 -0.1222 -0.0312 0.2846 36 GLU B O 3063 C CB . GLU B 36 ? 1.2972 1.2519 1.5261 -0.1189 -0.0095 0.2975 36 GLU B CB 3064 C CG . GLU B 36 ? 1.3909 1.3405 1.6699 -0.1145 -0.0346 0.3090 36 GLU B CG 3065 C CD . GLU B 36 ? 1.4067 1.3580 1.7474 -0.1061 -0.0385 0.2948 36 GLU B CD 3066 O OE1 . GLU B 36 ? 1.4203 1.3794 1.7655 -0.0989 -0.0348 0.2682 36 GLU B OE1 3067 O OE2 . GLU B 36 ? 1.3981 1.3421 1.7827 -0.1072 -0.0462 0.3107 36 GLU B OE2 3068 N N . GLU B 37 ? 1.4022 1.3487 1.5333 -0.1329 -0.0419 0.3351 37 GLU B N 3069 C CA . GLU B 37 ? 1.4709 1.4200 1.5900 -0.1306 -0.0688 0.3346 37 GLU B CA 3070 C C . GLU B 37 ? 1.5562 1.5100 1.7347 -0.1177 -0.0897 0.3195 37 GLU B C 3071 O O . GLU B 37 ? 1.5955 1.5433 1.8181 -0.1141 -0.1042 0.3343 37 GLU B O 3072 C CB . GLU B 37 ? 1.5890 1.5299 1.6884 -0.1385 -0.0818 0.3690 37 GLU B CB 3073 C CG . GLU B 37 ? 1.6957 1.6336 1.7217 -0.1513 -0.0676 0.3815 37 GLU B CG 3074 C CD . GLU B 37 ? 1.7241 1.6667 1.7078 -0.1535 -0.0874 0.3759 37 GLU B CD 3075 O OE1 . GLU B 37 ? 1.6123 1.5639 1.5990 -0.1478 -0.0916 0.3473 37 GLU B OE1 3076 O OE2 . GLU B 37 ? 1.8338 1.7714 1.7819 -0.1613 -0.0994 0.4011 37 GLU B OE2 3077 N N . LYS B 38 ? 1.6955 1.6593 1.8760 -0.1107 -0.0905 0.2900 38 LYS B N 3078 C CA . LYS B 38 ? 1.7489 1.7187 1.9808 -0.0982 -0.1086 0.2736 38 LYS B CA 3079 C C . LYS B 38 ? 1.9720 1.9451 2.2085 -0.0956 -0.1356 0.2815 38 LYS B C 3080 O O . LYS B 38 ? 1.9710 1.9440 2.1651 -0.1036 -0.1408 0.2949 38 LYS B O 3081 C CB . LYS B 38 ? 1.5438 1.5239 1.7752 -0.0920 -0.0997 0.2415 38 LYS B CB 3082 C CG . LYS B 38 ? 1.3768 1.3560 1.6477 -0.0855 -0.0895 0.2292 38 LYS B CG 3083 C CD . LYS B 38 ? 1.2816 1.2576 1.6105 -0.0770 -0.1082 0.2319 38 LYS B CD 3084 C CE . LYS B 38 ? 1.1888 1.1595 1.5548 -0.0749 -0.0988 0.2298 38 LYS B CE 3085 N NZ . LYS B 38 ? 1.0904 1.0688 1.4528 -0.0708 -0.0850 0.2049 38 LYS B NZ 3086 N N . GLU B 39 ? 2.1952 2.1715 2.4841 -0.0840 -0.1531 0.2724 39 GLU B N 3087 C CA . GLU B 39 ? 2.2438 2.2241 2.5512 -0.0789 -0.1797 0.2793 39 GLU B CA 3088 C C . GLU B 39 ? 2.2312 2.2244 2.5004 -0.0822 -0.1867 0.2718 39 GLU B C 3089 O O . GLU B 39 ? 2.2465 2.2407 2.5079 -0.0845 -0.2060 0.2888 39 GLU B O 3090 C CB . GLU B 39 ? 2.2457 2.2302 2.6146 -0.0641 -0.1921 0.2607 39 GLU B CB 3091 C CG . GLU B 39 ? 2.2641 2.2511 2.6499 -0.0588 -0.1755 0.2352 39 GLU B CG 3092 C CD . GLU B 39 ? 2.2694 2.2697 2.6211 -0.0597 -0.1619 0.2115 39 GLU B CD 3093 O OE1 . GLU B 39 ? 2.2288 2.2289 2.5774 -0.0593 -0.1447 0.1974 39 GLU B OE1 3094 O OE2 . GLU B 39 ? 2.3104 2.3214 2.6413 -0.0608 -0.1695 0.2073 39 GLU B OE2 3095 N N . ASN B 40 ? 1.9882 1.9910 2.2357 -0.0827 -0.1723 0.2470 40 ASN B N 3096 C CA . ASN B 40 ? 1.7682 1.7835 1.9838 -0.0867 -0.1785 0.2375 40 ASN B CA 3097 C C . ASN B 40 ? 1.6619 1.6723 1.8137 -0.1002 -0.1616 0.2401 40 ASN B C 3098 O O . ASN B 40 ? 1.7644 1.7745 1.8793 -0.1089 -0.1714 0.2532 40 ASN B O 3099 C CB . ASN B 40 ? 1.7276 1.7580 1.9663 -0.0779 -0.1764 0.2072 40 ASN B CB 3100 C CG . ASN B 40 ? 1.7124 1.7591 1.9635 -0.0747 -0.1970 0.2019 40 ASN B CG 3101 O OD1 . ASN B 40 ? 1.7338 1.7812 1.9680 -0.0806 -0.2131 0.2192 40 ASN B OD1 3102 N ND2 . ASN B 40 ? 1.6523 1.7134 1.9333 -0.0655 -0.1966 0.1783 40 ASN B ND2 3103 N N . VAL B 41 ? 1.4101 1.4167 1.5491 -0.1014 -0.1371 0.2263 41 VAL B N 3104 C CA . VAL B 41 ? 1.1875 1.1883 1.2696 -0.1126 -0.1180 0.2248 41 VAL B CA 3105 C C . VAL B 41 ? 1.0438 1.0315 1.1155 -0.1170 -0.0979 0.2395 41 VAL B C 3106 O O . VAL B 41 ? 1.0628 1.0454 1.1702 -0.1131 -0.1009 0.2541 41 VAL B O 3107 C CB . VAL B 41 ? 0.9976 1.0048 1.0711 -0.1111 -0.1039 0.1965 41 VAL B CB 3108 C CG1 . VAL B 41 ? 1.0185 1.0407 1.1056 -0.1076 -0.1217 0.1826 41 VAL B CG1 3109 C CG2 . VAL B 41 ? 0.7423 0.7481 0.8510 -0.1023 -0.0894 0.1852 41 VAL B CG2 3110 N N . LEU B 42 ? 0.8815 0.8640 0.9065 -0.1252 -0.0766 0.2350 42 LEU B N 3111 C CA . LEU B 42 ? 0.9142 0.8868 0.9283 -0.1296 -0.0538 0.2472 42 LEU B CA 3112 C C . LEU B 42 ? 0.9746 0.9477 1.0057 -0.1244 -0.0316 0.2277 42 LEU B C 3113 O O . LEU B 42 ? 1.0852 1.0610 1.0977 -0.1242 -0.0236 0.2065 42 LEU B O 3114 C CB . LEU B 42 ? 0.9348 0.9005 0.8835 -0.1423 -0.0431 0.2575 42 LEU B CB 3115 C CG . LEU B 42 ? 0.9039 0.8614 0.8387 -0.1472 -0.0148 0.2688 42 LEU B CG 3116 C CD1 . LEU B 42 ? 0.8034 0.7575 0.7767 -0.1459 -0.0192 0.2950 42 LEU B CD1 3117 C CD2 . LEU B 42 ? 1.0134 0.9643 0.8779 -0.1592 -0.0016 0.2748 42 LEU B CD2 3118 N N . ASN B 43 ? 0.9488 0.9192 1.0169 -0.1207 -0.0227 0.2358 43 ASN B N 3119 C CA . ASN B 43 ? 0.8701 0.8418 0.9588 -0.1154 -0.0037 0.2197 43 ASN B CA 3120 C C . ASN B 43 ? 0.8613 0.8271 0.9252 -0.1223 0.0248 0.2273 43 ASN B C 3121 O O . ASN B 43 ? 0.8960 0.8580 0.9690 -0.1266 0.0313 0.2489 43 ASN B O 3122 C CB . ASN B 43 ? 0.9382 0.9125 1.0894 -0.1063 -0.0131 0.2197 43 ASN B CB 3123 C CG . ASN B 43 ? 0.9306 0.9131 1.1074 -0.0961 -0.0290 0.1977 43 ASN B CG 3124 O OD1 . ASN B 43 ? 0.9046 0.8903 1.1146 -0.0885 -0.0264 0.1844 43 ASN B OD1 3125 N ND2 . ASN B 43 ? 0.9732 0.9604 1.1345 -0.0963 -0.0454 0.1940 43 ASN B ND2 3126 N N . ILE B 44 ? 0.8765 0.8415 0.9112 -0.1232 0.0426 0.2098 44 ILE B N 3127 C CA . ILE B 44 ? 0.9073 0.8676 0.9201 -0.1282 0.0721 0.2131 44 ILE B CA 3128 C C . ILE B 44 ? 0.8610 0.8246 0.9113 -0.1202 0.0874 0.1995 44 ILE B C 3129 O O . ILE B 44 ? 0.9416 0.9065 0.9921 -0.1147 0.0882 0.1783 44 ILE B O 3130 C CB . ILE B 44 ? 0.9074 0.8619 0.8572 -0.1355 0.0836 0.2033 44 ILE B CB 3131 C CG1 . ILE B 44 ? 0.9927 0.9449 0.9032 -0.1438 0.0653 0.2166 44 ILE B CG1 3132 C CG2 . ILE B 44 ? 0.7977 0.7477 0.7259 -0.1397 0.1162 0.2059 44 ILE B CG2 3133 C CD1 . ILE B 44 ? 0.9629 0.9094 0.8112 -0.1515 0.0708 0.2041 44 ILE B CD1 3134 N N . ASN B 45 ? 0.8556 0.8209 0.9387 -0.1201 0.0992 0.2131 45 ASN B N 3135 C CA . ASN B 45 ? 1.0479 1.0183 1.1758 -0.1124 0.1099 0.2036 45 ASN B CA 3136 C C . ASN B 45 ? 1.1922 1.1619 1.3067 -0.1155 0.1426 0.2045 45 ASN B C 3137 O O . ASN B 45 ? 1.2257 1.1971 1.3527 -0.1205 0.1569 0.2230 45 ASN B O 3138 C CB . ASN B 45 ? 1.1749 1.1491 1.3604 -0.1096 0.0965 0.2166 45 ASN B CB 3139 C CG . ASN B 45 ? 1.2204 1.2012 1.4566 -0.1014 0.1012 0.2057 45 ASN B CG 3140 O OD1 . ASN B 45 ? 1.2102 1.1933 1.4475 -0.1007 0.1239 0.2011 45 ASN B OD1 3141 N ND2 . ASN B 45 ? 1.2358 1.2196 1.5154 -0.0949 0.0789 0.2014 45 ASN B ND2 3142 N N . CYS B 46 ? 1.2574 1.2244 1.3473 -0.1127 0.1550 0.1847 46 CYS B N 3143 C CA . CYS B 46 ? 1.3281 1.2943 1.4094 -0.1130 0.1867 0.1804 46 CYS B CA 3144 C C . CYS B 46 ? 1.2239 1.1959 1.3536 -0.1023 0.1909 0.1672 46 CYS B C 3145 O O . CYS B 46 ? 1.1588 1.1290 1.2829 -0.0988 0.2116 0.1551 46 CYS B O 3146 C CB . CYS B 46 ? 1.3675 1.3240 1.3868 -0.1174 0.1988 0.1671 46 CYS B CB 3147 S SG . CYS B 46 ? 1.0046 0.9548 0.9598 -0.1312 0.2035 0.1838 46 CYS B SG 3148 N N . GLU B 47 ? 1.1679 1.1464 1.3452 -0.0969 0.1698 0.1696 47 GLU B N 3149 C CA . GLU B 47 ? 1.1763 1.1612 1.4008 -0.0868 0.1671 0.1585 47 GLU B CA 3150 C C . GLU B 47 ? 1.1589 1.1506 1.4167 -0.0857 0.1917 0.1646 47 GLU B C 3151 O O . GLU B 47 ? 1.1988 1.1943 1.4682 -0.0923 0.2024 0.1828 47 GLU B O 3152 C CB . GLU B 47 ? 1.2770 1.2671 1.5422 -0.0828 0.1387 0.1608 47 GLU B CB 3153 C CG . GLU B 47 ? 1.4529 1.4483 1.7543 -0.0721 0.1270 0.1457 47 GLU B CG 3154 C CD . GLU B 47 ? 1.5613 1.5587 1.8808 -0.0684 0.0973 0.1419 47 GLU B CD 3155 O OE1 . GLU B 47 ? 1.5590 1.5528 1.8473 -0.0683 0.0854 0.1341 47 GLU B OE1 3156 O OE2 . GLU B 47 ? 1.6135 1.6164 1.9800 -0.0657 0.0860 0.1458 47 GLU B OE2 3157 N N . ASN B 48 ? 1.1290 1.1228 1.4032 -0.0774 0.2010 0.1504 48 ASN B N 3158 C CA . ASN B 48 ? 1.1373 1.1411 1.4592 -0.0734 0.2183 0.1540 48 ASN B CA 3159 C C . ASN B 48 ? 1.0637 1.0699 1.3749 -0.0802 0.2509 0.1655 48 ASN B C 3160 O O . ASN B 48 ? 1.0319 1.0497 1.3893 -0.0801 0.2639 0.1757 48 ASN B O 3161 C CB . ASN B 48 ? 1.1785 1.1926 1.5593 -0.0718 0.1989 0.1632 48 ASN B CB 3162 C CG . ASN B 48 ? 1.1998 1.2237 1.6336 -0.0620 0.1977 0.1551 48 ASN B CG 3163 O OD1 . ASN B 48 ? 1.0963 1.1181 1.5308 -0.0537 0.1822 0.1404 48 ASN B OD1 3164 N ND2 . ASN B 48 ? 1.2972 1.3326 1.7766 -0.0632 0.2133 0.1656 48 ASN B ND2 3165 N N . LYS B 49 ? 1.0653 1.0613 1.3160 -0.0864 0.2647 0.1636 49 LYS B N 3166 C CA . LYS B 49 ? 1.0961 1.0938 1.3273 -0.0934 0.2968 0.1739 49 LYS B CA 3167 C C . LYS B 49 ? 0.8905 0.8864 1.1132 -0.0876 0.3260 0.1582 49 LYS B C 3168 O O . LYS B 49 ? 0.7941 0.7902 0.9917 -0.0925 0.3562 0.1618 49 LYS B O 3169 C CB . LYS B 49 ? 1.2696 1.2574 1.4363 -0.1046 0.2952 0.1826 49 LYS B CB 3170 C CG . LYS B 49 ? 1.3405 1.3308 1.5217 -0.1109 0.2723 0.2032 49 LYS B CG 3171 C CD . LYS B 49 ? 1.3103 1.3074 1.5015 -0.1198 0.2928 0.2279 49 LYS B CD 3172 C CE . LYS B 49 ? 1.3452 1.3474 1.5855 -0.1224 0.2706 0.2469 49 LYS B CE 3173 N NZ . LYS B 49 ? 1.4147 1.4077 1.6334 -0.1224 0.2371 0.2446 49 LYS B NZ 3174 N N . GLY B 50 ? 0.8433 0.8370 1.0861 -0.0769 0.3176 0.1408 50 GLY B N 3175 C CA . GLY B 50 ? 0.8843 0.8753 1.1294 -0.0694 0.3427 0.1255 50 GLY B CA 3176 C C . GLY B 50 ? 0.9975 0.9727 1.1748 -0.0737 0.3610 0.1129 50 GLY B C 3177 O O . GLY B 50 ? 1.0323 1.0065 1.2049 -0.0709 0.3922 0.1049 50 GLY B O 3178 N N . PHE B 51 ? 1.0776 1.0408 1.2039 -0.0803 0.3417 0.1097 51 PHE B N 3179 C CA . PHE B 51 ? 1.1273 1.0740 1.1882 -0.0851 0.3534 0.0950 51 PHE B CA 3180 C C . PHE B 51 ? 1.1665 1.1017 1.2315 -0.0758 0.3531 0.0726 51 PHE B C 3181 O O . PHE B 51 ? 1.1187 1.0543 1.2109 -0.0698 0.3293 0.0696 51 PHE B O 3182 C CB . PHE B 51 ? 1.1530 1.0925 1.1635 -0.0956 0.3300 0.0997 51 PHE B CB 3183 C CG . PHE B 51 ? 1.2421 1.1893 1.2406 -0.1056 0.3296 0.1231 51 PHE B CG 3184 C CD1 . PHE B 51 ? 1.2590 1.2020 1.2214 -0.1141 0.3053 0.1311 51 PHE B CD1 3185 C CD2 . PHE B 51 ? 1.3759 1.3349 1.4023 -0.1064 0.3527 0.1381 51 PHE B CD2 3186 C CE1 . PHE B 51 ? 1.3664 1.3147 1.3186 -0.1230 0.3031 0.1547 51 PHE B CE1 3187 C CE2 . PHE B 51 ? 1.5056 1.4702 1.5202 -0.1166 0.3523 0.1622 51 PHE B CE2 3188 C CZ . PHE B 51 ? 1.5341 1.4923 1.5112 -0.1245 0.3269 0.1708 51 PHE B CZ 3189 N N . THR B 52 ? 1.3088 1.2326 1.3463 -0.0745 0.3797 0.0569 52 THR B N 3190 C CA . THR B 52 ? 1.3966 1.3059 1.4364 -0.0662 0.3806 0.0359 52 THR B CA 3191 C C . THR B 52 ? 1.3810 1.2711 1.3566 -0.0748 0.3711 0.0221 52 THR B C 3192 O O . THR B 52 ? 1.3410 1.2158 1.3102 -0.0709 0.3670 0.0051 52 THR B O 3193 C CB . THR B 52 ? 1.4912 1.3987 1.5497 -0.0576 0.4161 0.0248 52 THR B CB 3194 O OG1 . THR B 52 ? 1.6254 1.5543 1.7412 -0.0524 0.4274 0.0400 52 THR B OG1 3195 C CG2 . THR B 52 ? 1.4383 1.3318 1.5162 -0.0465 0.4141 0.0068 52 THR B CG2 3196 N N . THR B 53 ? 1.3990 1.2899 1.3283 -0.0870 0.3666 0.0305 53 THR B N 3197 C CA . THR B 53 ? 1.3829 1.2573 1.2492 -0.0966 0.3580 0.0178 53 THR B CA 3198 C C . THR B 53 ? 1.4050 1.2861 1.2407 -0.1082 0.3364 0.0343 53 THR B C 3199 O O . THR B 53 ? 1.4928 1.3881 1.3440 -0.1102 0.3372 0.0549 53 THR B O 3200 C CB . THR B 53 ? 1.5787 1.4395 1.4000 -0.0994 0.3895 0.0012 53 THR B CB 3201 O OG1 . THR B 53 ? 1.7202 1.5787 1.5806 -0.0869 0.4142 -0.0101 53 THR B OG1 3202 C CG2 . THR B 53 ? 1.6487 1.4888 1.4141 -0.1073 0.3792 -0.0186 53 THR B CG2 3203 N N . VAL B 54 ? 1.4476 1.3183 1.2427 -0.1159 0.3164 0.0257 54 VAL B N 3204 C CA . VAL B 54 ? 1.4585 1.3351 1.2250 -0.1263 0.2935 0.0404 54 VAL B CA 3205 C C . VAL B 54 ? 1.5037 1.3708 1.2011 -0.1377 0.3048 0.0362 54 VAL B C 3206 O O . VAL B 54 ? 1.5100 1.3785 1.1725 -0.1475 0.2851 0.0454 54 VAL B O 3207 C CB . VAL B 54 ? 1.3938 1.2690 1.1644 -0.1278 0.2611 0.0356 54 VAL B CB 3208 C CG1 . VAL B 54 ? 1.3529 1.2420 1.1321 -0.1319 0.2350 0.0566 54 VAL B CG1 3209 C CG2 . VAL B 54 ? 1.3694 1.2451 1.1910 -0.1163 0.2582 0.0275 54 VAL B CG2 3210 N N . SER B 55 ? 1.5397 1.3972 1.2175 -0.1359 0.3365 0.0218 55 SER B N 3211 C CA . SER B 55 ? 1.6661 1.5131 1.2735 -0.1462 0.3504 0.0140 55 SER B CA 3212 C C . SER B 55 ? 1.6807 1.5396 1.2655 -0.1536 0.3555 0.0394 55 SER B C 3213 O O . SER B 55 ? 1.7319 1.5856 1.2546 -0.1650 0.3503 0.0415 55 SER B O 3214 C CB . SER B 55 ? 1.7625 1.5969 1.3596 -0.1407 0.3863 -0.0090 55 SER B CB 3215 O OG . SER B 55 ? 1.8051 1.6240 1.4143 -0.1356 0.3808 -0.0329 55 SER B OG 3216 N N . LEU B 56 ? 1.6603 1.5350 1.2963 -0.1477 0.3642 0.0595 56 LEU B N 3217 C CA . LEU B 56 ? 1.6340 1.5194 1.2554 -0.1542 0.3761 0.0847 56 LEU B CA 3218 C C . LEU B 56 ? 1.6293 1.5186 1.2272 -0.1641 0.3443 0.1066 56 LEU B C 3219 O O . LEU B 56 ? 1.7489 1.6363 1.2919 -0.1745 0.3491 0.1182 56 LEU B O 3220 C CB . LEU B 56 ? 1.5083 1.4098 1.1996 -0.1457 0.3916 0.1003 56 LEU B CB 3221 C CG . LEU B 56 ? 1.5384 1.4530 1.2323 -0.1522 0.4021 0.1307 56 LEU B CG 3222 C CD1 . LEU B 56 ? 1.6495 1.5643 1.2822 -0.1580 0.4214 0.1294 56 LEU B CD1 3223 C CD2 . LEU B 56 ? 1.5040 1.4353 1.2757 -0.1425 0.4159 0.1400 56 LEU B CD2 3224 N N . LEU B 57 ? 1.4997 1.3943 1.1384 -0.1606 0.3122 0.1126 57 LEU B N 3225 C CA . LEU B 57 ? 1.4070 1.3075 1.0392 -0.1675 0.2830 0.1363 57 LEU B CA 3226 C C . LEU B 57 ? 1.4593 1.3520 1.0457 -0.1750 0.2542 0.1280 57 LEU B C 3227 O O . LEU B 57 ? 1.3497 1.2367 0.9418 -0.1720 0.2422 0.1066 57 LEU B O 3228 C CB . LEU B 57 ? 1.2007 1.1132 0.9062 -0.1594 0.2646 0.1492 57 LEU B CB 3229 C CG . LEU B 57 ? 1.0404 0.9540 0.7977 -0.1473 0.2668 0.1302 57 LEU B CG 3230 C CD1 . LEU B 57 ? 0.7982 0.7038 0.5417 -0.1466 0.2455 0.1097 57 LEU B CD1 3231 C CD2 . LEU B 57 ? 0.7650 0.6915 0.5906 -0.1402 0.2549 0.1455 57 LEU B CD2 3232 N N . GLN B 58 ? 1.5563 1.4493 1.0986 -0.1854 0.2429 0.1466 58 GLN B N 3233 C CA . GLN B 58 ? 1.6428 1.5315 1.1453 -0.1932 0.2118 0.1434 58 GLN B CA 3234 C C . GLN B 58 ? 1.5864 1.4856 1.1347 -0.1902 0.1772 0.1599 58 GLN B C 3235 O O . GLN B 58 ? 1.6945 1.6004 1.2562 -0.1917 0.1698 0.1875 58 GLN B O 3236 C CB . GLN B 58 ? 1.7882 1.6720 1.2169 -0.2058 0.2146 0.1557 58 GLN B CB 3237 C CG . GLN B 58 ? 1.9286 1.8030 1.3085 -0.2089 0.2524 0.1414 58 GLN B CG 3238 C CD . GLN B 58 ? 2.1256 2.0007 1.4509 -0.2189 0.2636 0.1652 58 GLN B CD 3239 O OE1 . GLN B 58 ? 2.1598 2.0444 1.5124 -0.2187 0.2665 0.1949 58 GLN B OE1 3240 N NE2 . GLN B 58 ? 2.2501 2.1162 1.5029 -0.2260 0.2676 0.1518 58 GLN B NE2 3241 N N . PRO B 59 ? 1.4012 1.3014 0.9747 -0.1859 0.1567 0.1432 59 PRO B N 3242 C CA . PRO B 59 ? 1.2491 1.1599 0.8633 -0.1827 0.1241 0.1557 59 PRO B CA 3243 C C . PRO B 59 ? 1.2524 1.1641 0.8262 -0.1925 0.0983 0.1708 59 PRO B C 3244 O O . PRO B 59 ? 1.3864 1.2897 0.8974 -0.2022 0.1028 0.1654 59 PRO B O 3245 C CB . PRO B 59 ? 1.1982 1.1090 0.8364 -0.1774 0.1141 0.1309 59 PRO B CB 3246 C CG . PRO B 59 ? 1.3160 1.2134 0.9016 -0.1840 0.1285 0.1084 59 PRO B CG 3247 C CD . PRO B 59 ? 1.4352 1.3264 0.9977 -0.1847 0.1621 0.1123 59 PRO B CD 3248 N N . PRO B 60 ? 1.1602 1.0815 0.7693 -0.1898 0.0710 0.1889 60 PRO B N 3249 C CA . PRO B 60 ? 1.1993 1.1225 0.7754 -0.1980 0.0417 0.2007 60 PRO B CA 3250 C C . PRO B 60 ? 1.2493 1.1729 0.8113 -0.2010 0.0248 0.1762 60 PRO B C 3251 O O . PRO B 60 ? 1.0929 1.0189 0.6910 -0.1941 0.0278 0.1565 60 PRO B O 3252 C CB . PRO B 60 ? 1.1110 1.0441 0.7416 -0.1915 0.0189 0.2232 60 PRO B CB 3253 C CG . PRO B 60 ? 1.0763 1.0140 0.7697 -0.1796 0.0295 0.2123 60 PRO B CG 3254 C CD . PRO B 60 ? 1.1027 1.0329 0.7815 -0.1793 0.0651 0.1997 60 PRO B CD 3255 N N . GLN B 61 ? 1.3877 1.3089 0.8979 -0.2117 0.0070 0.1780 61 GLN B N 3256 C CA . GLN B 61 ? 1.4664 1.3866 0.9578 -0.2171 -0.0062 0.1532 61 GLN B CA 3257 C C . GLN B 61 ? 1.5183 1.4524 1.0382 -0.2170 -0.0439 0.1583 61 GLN B C 3258 O O . GLN B 61 ? 1.5980 1.5367 1.1368 -0.2168 -0.0533 0.1382 61 GLN B O 3259 C CB . GLN B 61 ? 1.5043 1.4119 0.9164 -0.2300 -0.0001 0.1449 61 GLN B CB 3260 C CG . GLN B 61 ? 1.4803 1.3740 0.8655 -0.2295 0.0395 0.1303 61 GLN B CG 3261 C CD . GLN B 61 ? 1.4130 1.3039 0.8413 -0.2209 0.0559 0.1057 61 GLN B CD 3262 O OE1 . GLN B 61 ? 1.5237 1.4156 0.9653 -0.2220 0.0412 0.0874 61 GLN B OE1 3263 N NE2 . GLN B 61 ? 1.3056 1.1938 0.7577 -0.2125 0.0859 0.1066 61 GLN B NE2 3264 N N . TYR B 62 ? 1.5521 1.4934 1.0780 -0.2171 -0.0649 0.1858 62 TYR B N 3265 C CA . TYR B 62 ? 1.6220 1.5779 1.1803 -0.2156 -0.1006 0.1912 62 TYR B CA 3266 C C . TYR B 62 ? 1.5278 1.4947 1.1582 -0.2024 -0.1083 0.2049 62 TYR B C 3267 O O . TYR B 62 ? 1.5804 1.5611 1.2501 -0.1982 -0.1336 0.2049 62 TYR B O 3268 C CB . TYR B 62 ? 1.9117 1.8685 1.4247 -0.2257 -0.1272 0.2104 62 TYR B CB 3269 C CG . TYR B 62 ? 2.1169 2.0907 1.6704 -0.2229 -0.1648 0.2178 62 TYR B CG 3270 C CD1 . TYR B 62 ? 2.2100 2.1941 1.7818 -0.2245 -0.1788 0.1950 62 TYR B CD1 3271 C CD2 . TYR B 62 ? 2.1634 2.1432 1.7422 -0.2181 -0.1852 0.2477 62 TYR B CD2 3272 C CE1 . TYR B 62 ? 2.2511 2.2534 1.8650 -0.2214 -0.2114 0.2012 62 TYR B CE1 3273 C CE2 . TYR B 62 ? 2.2244 2.2204 1.8455 -0.2140 -0.2187 0.2536 62 TYR B CE2 3274 C CZ . TYR B 62 ? 2.2614 2.2699 1.9002 -0.2155 -0.2313 0.2299 62 TYR B CZ 3275 O OH . TYR B 62 ? 2.2402 2.2674 1.9250 -0.2110 -0.2632 0.2354 62 TYR B OH 3276 N N . ARG B 63 ? 1.4441 1.4056 1.0952 -0.1957 -0.0868 0.2152 63 ARG B N 3277 C CA . ARG B 63 ? 1.2993 1.2697 1.0191 -0.1834 -0.0952 0.2246 63 ARG B CA 3278 C C . ARG B 63 ? 1.1801 1.1545 0.9436 -0.1740 -0.0804 0.2012 63 ARG B C 3279 O O . ARG B 63 ? 1.0632 1.0294 0.8112 -0.1746 -0.0542 0.1861 63 ARG B O 3280 C CB . ARG B 63 ? 1.2451 1.2090 0.9742 -0.1812 -0.0861 0.2514 63 ARG B CB 3281 C CG . ARG B 63 ? 1.1993 1.1712 0.9961 -0.1701 -0.1035 0.2637 63 ARG B CG 3282 C CD . ARG B 63 ? 1.2659 1.2303 1.0844 -0.1670 -0.0890 0.2840 63 ARG B CD 3283 N NE . ARG B 63 ? 1.3494 1.3096 1.1572 -0.1715 -0.1057 0.3167 63 ARG B NE 3284 C CZ . ARG B 63 ? 1.5106 1.4641 1.3412 -0.1701 -0.0990 0.3403 63 ARG B CZ 3285 N NH1 . ARG B 63 ? 1.5536 1.5054 1.4201 -0.1644 -0.0768 0.3331 63 ARG B NH1 3286 N NH2 . ARG B 63 ? 1.5936 1.5420 1.4132 -0.1747 -0.1154 0.3719 63 ARG B NH2 3287 N N . ILE B 64 ? 1.1944 1.1815 1.0124 -0.1648 -0.0977 0.1985 64 ILE B N 3288 C CA . ILE B 64 ? 1.1913 1.1837 1.0512 -0.1553 -0.0873 0.1785 64 ILE B CA 3289 C C . ILE B 64 ? 1.1770 1.1638 1.0664 -0.1474 -0.0690 0.1856 64 ILE B C 3290 O O . ILE B 64 ? 1.1505 1.1345 1.0522 -0.1460 -0.0741 0.2076 64 ILE B O 3291 C CB . ILE B 64 ? 1.2175 1.2269 1.1237 -0.1483 -0.1113 0.1732 64 ILE B CB 3292 C CG1 . ILE B 64 ? 1.2568 1.2724 1.1871 -0.1427 -0.1008 0.1484 64 ILE B CG1 3293 C CG2 . ILE B 64 ? 1.2512 1.2650 1.2032 -0.1390 -0.1257 0.1915 64 ILE B CG2 3294 C CD1 . ILE B 64 ? 1.3252 1.3375 1.2173 -0.1524 -0.0934 0.1304 64 ILE B CD1 3295 N N . TYR B 65 ? 1.1420 1.1263 1.0430 -0.1427 -0.0484 0.1681 65 TYR B N 3296 C CA . TYR B 65 ? 1.0978 1.0773 1.0251 -0.1363 -0.0305 0.1733 65 TYR B CA 3297 C C . TYR B 65 ? 1.1256 1.1072 1.0809 -0.1280 -0.0171 0.1531 65 TYR B C 3298 O O . TYR B 65 ? 1.1630 1.1480 1.1127 -0.1280 -0.0179 0.1347 65 TYR B O 3299 C CB . TYR B 65 ? 1.1067 1.0742 0.9932 -0.1442 -0.0088 0.1837 65 TYR B CB 3300 C CG . TYR B 65 ? 1.2066 1.1666 1.0472 -0.1506 0.0092 0.1657 65 TYR B CG 3301 C CD1 . TYR B 65 ? 1.2387 1.1947 1.0897 -0.1458 0.0315 0.1491 65 TYR B CD1 3302 C CD2 . TYR B 65 ? 1.3318 1.2876 1.1193 -0.1614 0.0026 0.1649 65 TYR B CD2 3303 C CE1 . TYR B 65 ? 1.2862 1.2331 1.0983 -0.1510 0.0478 0.1321 65 TYR B CE1 3304 C CE2 . TYR B 65 ? 1.4158 1.3625 1.1619 -0.1674 0.0185 0.1464 65 TYR B CE2 3305 C CZ . TYR B 65 ? 1.4002 1.3418 1.1599 -0.1619 0.0417 0.1299 65 TYR B CZ 3306 O OH . TYR B 65 ? 1.4738 1.4043 1.1955 -0.1673 0.0574 0.1109 65 TYR B OH 3307 N N . GLN B 66 ? 1.0819 1.0614 1.0678 -0.1217 -0.0053 0.1579 66 GLN B N 3308 C CA . GLN B 66 ? 1.0455 1.0257 1.0559 -0.1140 0.0083 0.1419 66 GLN B CA 3309 C C . GLN B 66 ? 0.9968 0.9684 0.9978 -0.1157 0.0342 0.1456 66 GLN B C 3310 O O . GLN B 66 ? 1.0059 0.9740 1.0035 -0.1195 0.0396 0.1639 66 GLN B O 3311 C CB . GLN B 66 ? 1.1000 1.0884 1.1648 -0.1032 -0.0043 0.1412 66 GLN B CB 3312 C CG . GLN B 66 ? 1.1101 1.1092 1.1917 -0.0992 -0.0271 0.1347 66 GLN B CG 3313 C CD . GLN B 66 ? 1.0439 1.0502 1.1753 -0.0876 -0.0352 0.1278 66 GLN B CD 3314 O OE1 . GLN B 66 ? 1.0656 1.0682 1.2234 -0.0836 -0.0307 0.1338 66 GLN B OE1 3315 N NE2 . GLN B 66 ? 1.0030 1.0200 1.1475 -0.0825 -0.0469 0.1142 66 GLN B NE2 3316 N N . LEU B 67 ? 0.8707 0.8392 0.8699 -0.1126 0.0505 0.1295 67 LEU B N 3317 C CA . LEU B 67 ? 0.8366 0.7981 0.8286 -0.1135 0.0766 0.1312 67 LEU B CA 3318 C C . LEU B 67 ? 0.8969 0.8613 0.9305 -0.1035 0.0851 0.1228 67 LEU B C 3319 O O . LEU B 67 ? 0.8469 0.8113 0.8841 -0.0989 0.0850 0.1066 67 LEU B O 3320 C CB . LEU B 67 ? 0.7740 0.7256 0.7152 -0.1207 0.0918 0.1201 67 LEU B CB 3321 C CG . LEU B 67 ? 0.7643 0.7083 0.6929 -0.1216 0.1215 0.1195 67 LEU B CG 3322 C CD1 . LEU B 67 ? 0.7954 0.7411 0.7246 -0.1256 0.1292 0.1415 67 LEU B CD1 3323 C CD2 . LEU B 67 ? 0.8170 0.7495 0.6935 -0.1285 0.1339 0.1054 67 LEU B CD2 3324 N N . PHE B 68 ? 0.9864 0.9535 1.0519 -0.1008 0.0919 0.1349 68 PHE B N 3325 C CA . PHE B 68 ? 1.0162 0.9872 1.1241 -0.0918 0.0980 0.1287 68 PHE B CA 3326 C C . PHE B 68 ? 1.0796 1.0460 1.1795 -0.0925 0.1263 0.1269 68 PHE B C 3327 O O . PHE B 68 ? 1.1072 1.0727 1.2018 -0.0978 0.1411 0.1406 68 PHE B O 3328 C CB . PHE B 68 ? 1.0384 1.0162 1.1943 -0.0884 0.0869 0.1413 68 PHE B CB 3329 C CG . PHE B 68 ? 0.9790 0.9607 1.1481 -0.0865 0.0601 0.1429 68 PHE B CG 3330 C CD1 . PHE B 68 ? 1.0729 1.0571 1.2803 -0.0851 0.0483 0.1557 68 PHE B CD1 3331 C CD2 . PHE B 68 ? 0.8754 0.8585 1.0227 -0.0860 0.0471 0.1315 68 PHE B CD2 3332 C CE1 . PHE B 68 ? 1.1155 1.1025 1.3384 -0.0821 0.0244 0.1559 68 PHE B CE1 3333 C CE2 . PHE B 68 ? 0.8611 0.8495 1.0245 -0.0832 0.0241 0.1323 68 PHE B CE2 3334 C CZ . PHE B 68 ? 1.0285 1.0184 1.2295 -0.0807 0.0128 0.1439 68 PHE B CZ 3335 N N . LEU B 69 ? 1.0289 0.9924 1.1292 -0.0870 0.1345 0.1109 69 LEU B N 3336 C CA . LEU B 69 ? 0.9760 0.9344 1.0709 -0.0861 0.1616 0.1067 69 LEU B CA 3337 C C . LEU B 69 ? 1.0207 0.9837 1.1603 -0.0754 0.1653 0.1001 69 LEU B C 3338 O O . LEU B 69 ? 1.0716 1.0293 1.2088 -0.0719 0.1837 0.0913 69 LEU B O 3339 C CB . LEU B 69 ? 0.8526 0.7988 0.8980 -0.0905 0.1715 0.0930 69 LEU B CB 3340 C CG . LEU B 69 ? 0.8778 0.8178 0.8736 -0.1017 0.1794 0.0991 69 LEU B CG 3341 C CD1 . LEU B 69 ? 0.8320 0.7600 0.7814 -0.1066 0.1808 0.0827 69 LEU B CD1 3342 C CD2 . LEU B 69 ? 0.9958 0.9358 0.9910 -0.1033 0.2070 0.1074 69 LEU B CD2 3343 N N . ASN B 70 ? 1.0486 1.0210 1.2294 -0.0701 0.1469 0.1041 70 ASN B N 3344 C CA . ASN B 70 ? 1.0413 1.0196 1.2660 -0.0603 0.1461 0.0993 70 ASN B CA 3345 C C . ASN B 70 ? 1.0364 1.0183 1.2870 -0.0591 0.1691 0.1060 70 ASN B C 3346 O O . ASN B 70 ? 1.1483 1.1306 1.3896 -0.0662 0.1836 0.1175 70 ASN B O 3347 C CB . ASN B 70 ? 1.0973 1.0848 1.3589 -0.0562 0.1212 0.1021 70 ASN B CB 3348 C CG . ASN B 70 ? 1.2205 1.2070 1.4612 -0.0564 0.1001 0.0951 70 ASN B CG 3349 O OD1 . ASN B 70 ? 1.3235 1.3048 1.5362 -0.0558 0.1004 0.0842 70 ASN B OD1 3350 N ND2 . ASN B 70 ? 1.2114 1.2031 1.4688 -0.0573 0.0821 0.1012 70 ASN B ND2 3351 N N . GLY B 71 ? 0.9533 0.9388 1.2369 -0.0501 0.1726 0.0996 71 GLY B N 3352 C CA . GLY B 71 ? 0.9580 0.9509 1.2792 -0.0473 0.1918 0.1058 71 GLY B CA 3353 C C . GLY B 71 ? 0.9269 0.9145 1.2231 -0.0515 0.2237 0.1065 71 GLY B C 3354 O O . GLY B 71 ? 0.8891 0.8851 1.2118 -0.0527 0.2423 0.1160 71 GLY B O 3355 N N . ASN B 72 ? 0.9093 0.8831 1.1549 -0.0540 0.2307 0.0958 72 ASN B N 3356 C CA . ASN B 72 ? 0.9469 0.9130 1.1624 -0.0572 0.2610 0.0917 72 ASN B CA 3357 C C . ASN B 72 ? 0.9447 0.9006 1.1588 -0.0488 0.2721 0.0750 72 ASN B C 3358 O O . ASN B 72 ? 1.0531 0.9985 1.2461 -0.0474 0.2583 0.0644 72 ASN B O 3359 C CB . ASN B 72 ? 0.9784 0.9346 1.1322 -0.0685 0.2612 0.0922 72 ASN B CB 3360 C CG . ASN B 72 ? 0.9853 0.9494 1.1372 -0.0773 0.2582 0.1114 72 ASN B CG 3361 O OD1 . ASN B 72 ? 1.0114 0.9861 1.1973 -0.0773 0.2712 0.1239 72 ASN B OD1 3362 N ND2 . ASN B 72 ? 0.9996 0.9589 1.1143 -0.0849 0.2408 0.1150 72 ASN B ND2 3363 N N . LEU B 73 ? 0.8712 0.8304 1.1100 -0.0434 0.2979 0.0734 73 LEU B N 3364 C CA . LEU B 73 ? 0.9442 0.8937 1.1917 -0.0336 0.3092 0.0589 73 LEU B CA 3365 C C . LEU B 73 ? 1.0499 0.9787 1.2406 -0.0378 0.3232 0.0434 73 LEU B C 3366 O O . LEU B 73 ? 1.1058 1.0306 1.2785 -0.0398 0.3514 0.0386 73 LEU B O 3367 C CB . LEU B 73 ? 0.9463 0.9072 1.2433 -0.0256 0.3336 0.0615 73 LEU B CB 3368 C CG . LEU B 73 ? 1.0025 0.9789 1.3154 -0.0312 0.3541 0.0751 73 LEU B CG 3369 C CD1 . LEU B 73 ? 1.1253 1.0927 1.3771 -0.0423 0.3749 0.0738 73 LEU B CD1 3370 C CD2 . LEU B 73 ? 1.0286 1.0171 1.3991 -0.0209 0.3766 0.0746 73 LEU B CD2 3371 N N . LEU B 74 ? 1.1242 1.0402 1.2869 -0.0396 0.3040 0.0350 74 LEU B N 3372 C CA . LEU B 74 ? 1.2354 1.1300 1.3561 -0.0418 0.3156 0.0178 74 LEU B CA 3373 C C . LEU B 74 ? 1.3664 1.2503 1.5062 -0.0328 0.3050 0.0091 74 LEU B C 3374 O O . LEU B 74 ? 1.3208 1.2078 1.4679 -0.0323 0.2793 0.0134 74 LEU B O 3375 C CB . LEU B 74 ? 1.0861 0.9724 1.1473 -0.0553 0.3055 0.0150 74 LEU B CB 3376 C CG . LEU B 74 ? 0.8425 0.7367 0.8905 -0.0629 0.2763 0.0248 74 LEU B CG 3377 C CD1 . LEU B 74 ? 0.6020 0.5109 0.6507 -0.0688 0.2762 0.0416 74 LEU B CD1 3378 C CD2 . LEU B 74 ? 0.8884 0.7889 0.9719 -0.0557 0.2524 0.0278 74 LEU B CD2 3379 N N . THR B 75 ? 1.5152 1.3866 1.6644 -0.0253 0.3257 -0.0026 75 THR B N 3380 C CA . THR B 75 ? 1.5965 1.4550 1.7643 -0.0165 0.3176 -0.0093 75 THR B CA 3381 C C . THR B 75 ? 1.6028 1.4444 1.7272 -0.0252 0.3019 -0.0172 75 THR B C 3382 O O . THR B 75 ? 1.6439 1.4845 1.7789 -0.0229 0.2807 -0.0134 75 THR B O 3383 C CB . THR B 75 ? 1.8662 1.7117 2.0516 -0.0068 0.3447 -0.0215 75 THR B CB 3384 O OG1 . THR B 75 ? 1.9156 1.7563 2.0675 -0.0129 0.3715 -0.0309 75 THR B OG1 3385 C CG2 . THR B 75 ? 1.8603 1.7227 2.1106 0.0067 0.3490 -0.0120 75 THR B CG2 3386 N N . ARG B 76 ? 1.4505 1.2799 1.5257 -0.0357 0.3123 -0.0280 76 ARG B N 3387 C CA . ARG B 76 ? 1.3290 1.1417 1.3653 -0.0449 0.2996 -0.0376 76 ARG B CA 3388 C C . ARG B 76 ? 1.1349 0.9512 1.1230 -0.0595 0.2930 -0.0375 76 ARG B C 3389 O O . ARG B 76 ? 1.0885 0.9157 1.0659 -0.0628 0.3028 -0.0316 76 ARG B O 3390 C CB . ARG B 76 ? 1.4979 1.2835 1.5226 -0.0426 0.3173 -0.0566 76 ARG B CB 3391 C CG . ARG B 76 ? 1.5787 1.3617 1.6475 -0.0274 0.3374 -0.0588 76 ARG B CG 3392 C CD . ARG B 76 ? 1.6368 1.3908 1.7038 -0.0230 0.3500 -0.0765 76 ARG B CD 3393 N NE . ARG B 76 ? 1.6414 1.3916 1.7552 -0.0105 0.3408 -0.0695 76 ARG B NE 3394 C CZ . ARG B 76 ? 1.5938 1.3556 1.7590 0.0039 0.3478 -0.0615 76 ARG B CZ 3395 N NH1 . ARG B 76 ? 1.5670 1.3461 1.7469 0.0073 0.3660 -0.0594 76 ARG B NH1 3396 N NH2 . ARG B 76 ? 1.5355 1.2925 1.7386 0.0144 0.3359 -0.0543 76 ARG B NH2 3397 N N . LEU B 77 ? 1.0993 0.9070 1.0603 -0.0684 0.2756 -0.0426 77 LEU B N 3398 C CA . LEU B 77 ? 1.0453 0.8529 0.9586 -0.0826 0.2680 -0.0455 77 LEU B CA 3399 C C . LEU B 77 ? 1.2392 1.0213 1.1160 -0.0898 0.2763 -0.0660 77 LEU B C 3400 O O . LEU B 77 ? 1.2447 1.0119 1.1323 -0.0877 0.2728 -0.0739 77 LEU B O 3401 C CB . LEU B 77 ? 0.8552 0.6768 0.7703 -0.0879 0.2393 -0.0348 77 LEU B CB 3402 C CG . LEU B 77 ? 0.8055 0.6509 0.7523 -0.0824 0.2291 -0.0165 77 LEU B CG 3403 C CD1 . LEU B 77 ? 0.7672 0.6251 0.7127 -0.0875 0.2023 -0.0092 77 LEU B CD1 3404 C CD2 . LEU B 77 ? 0.8476 0.7009 0.7829 -0.0849 0.2423 -0.0095 77 LEU B CD2 3405 N N . TYR B 78 ? 1.3981 1.1745 1.2307 -0.0986 0.2868 -0.0744 78 TYR B N 3406 C CA . TYR B 78 ? 1.5268 1.2775 1.3237 -0.1049 0.2978 -0.0971 78 TYR B CA 3407 C C . TYR B 78 ? 1.5092 1.2559 1.2678 -0.1203 0.2758 -0.1025 78 TYR B C 3408 O O . TYR B 78 ? 1.4702 1.2354 1.2204 -0.1266 0.2573 -0.0887 78 TYR B O 3409 C CB . TYR B 78 ? 1.6719 1.4173 1.4418 -0.1044 0.3259 -0.1064 78 TYR B CB 3410 C CG . TYR B 78 ? 1.8024 1.5492 1.6151 -0.0887 0.3506 -0.1055 78 TYR B CG 3411 C CD1 . TYR B 78 ? 1.9717 1.7178 1.7707 -0.0858 0.3801 -0.1121 78 TYR B CD1 3412 C CD2 . TYR B 78 ? 1.7995 1.5493 1.6669 -0.0769 0.3441 -0.0977 78 TYR B CD2 3413 C CE1 . TYR B 78 ? 2.0287 1.7785 1.8728 -0.0711 0.4028 -0.1113 78 TYR B CE1 3414 C CE2 . TYR B 78 ? 1.8894 1.6421 1.7998 -0.0624 0.3640 -0.0962 78 TYR B CE2 3415 C CZ . TYR B 78 ? 2.0115 1.7647 1.9129 -0.0594 0.3934 -0.1032 78 TYR B CZ 3416 O OH . TYR B 78 ? 2.0694 1.8277 2.0197 -0.0445 0.4133 -0.1016 78 TYR B OH 3417 N N . PRO B 79 ? 1.6656 1.3880 1.4053 -0.1265 0.2767 -0.1224 79 PRO B N 3418 C CA . PRO B 79 ? 1.6775 1.3969 1.3873 -0.1418 0.2543 -0.1279 79 PRO B CA 3419 C C . PRO B 79 ? 1.7305 1.4593 1.3927 -0.1529 0.2483 -0.1264 79 PRO B C 3420 O O . PRO B 79 ? 1.8164 1.5366 1.4453 -0.1539 0.2674 -0.1363 79 PRO B O 3421 C CB . PRO B 79 ? 1.7801 1.4680 1.4770 -0.1459 0.2629 -0.1524 79 PRO B CB 3422 C CG . PRO B 79 ? 1.8465 1.5209 1.5497 -0.1340 0.2933 -0.1626 79 PRO B CG 3423 C CD . PRO B 79 ? 1.8001 1.4963 1.5475 -0.1198 0.2981 -0.1412 79 PRO B CD 3424 N N . ASN B 80 ? 1.5760 1.3231 1.2362 -0.1605 0.2224 -0.1134 80 ASN B N 3425 C CA . ASN B 80 ? 1.5483 1.3058 1.1666 -0.1712 0.2111 -0.1082 80 ASN B CA 3426 C C . ASN B 80 ? 1.4690 1.2396 1.0821 -0.1650 0.2253 -0.0934 80 ASN B C 3427 O O . ASN B 80 ? 1.4565 1.2284 1.0251 -0.1730 0.2261 -0.0923 80 ASN B O 3428 C CB . ASN B 80 ? 1.6510 1.3874 1.2161 -0.1842 0.2125 -0.1313 80 ASN B CB 3429 C CG . ASN B 80 ? 1.7027 1.4501 1.2293 -0.1982 0.1884 -0.1263 80 ASN B CG 3430 O OD1 . ASN B 80 ? 1.7276 1.4697 1.2417 -0.2098 0.1692 -0.1368 80 ASN B OD1 3431 N ND2 . ASN B 80 ? 1.6948 1.4578 1.2048 -0.1974 0.1887 -0.1093 80 ASN B ND2 3432 N N . GLU B 81 ? 1.3799 1.1602 1.0390 -0.1515 0.2358 -0.0812 81 GLU B N 3433 C CA . GLU B 81 ? 1.2705 1.0654 0.9360 -0.1458 0.2484 -0.0646 81 GLU B CA 3434 C C . GLU B 81 ? 1.2257 1.0401 0.8822 -0.1523 0.2258 -0.0445 81 GLU B C 3435 O O . GLU B 81 ? 1.2631 1.0838 0.8952 -0.1555 0.2326 -0.0339 81 GLU B O 3436 C CB . GLU B 81 ? 1.2522 1.0548 0.9760 -0.1306 0.2586 -0.0558 81 GLU B CB 3437 C CG . GLU B 81 ? 1.2599 1.0800 1.0027 -0.1248 0.2690 -0.0368 81 GLU B CG 3438 C CD . GLU B 81 ? 1.2128 1.0382 1.0125 -0.1102 0.2808 -0.0325 81 GLU B CD 3439 O OE1 . GLU B 81 ? 1.3180 1.1304 1.1357 -0.1040 0.2856 -0.0454 81 GLU B OE1 3440 O OE2 . GLU B 81 ? 1.1238 0.9657 0.9518 -0.1051 0.2843 -0.0157 81 GLU B OE2 3441 N N . PHE B 82 ? 1.2530 1.0769 0.9305 -0.1540 0.1996 -0.0390 82 PHE B N 3442 C CA . PHE B 82 ? 1.2678 1.1093 0.9412 -0.1597 0.1752 -0.0221 82 PHE B CA 3443 C C . PHE B 82 ? 1.3457 1.1818 0.9784 -0.1735 0.1569 -0.0320 82 PHE B C 3444 O O . PHE B 82 ? 1.3791 1.2089 1.0188 -0.1768 0.1475 -0.0449 82 PHE B O 3445 C CB . PHE B 82 ? 1.1987 1.0568 0.9243 -0.1519 0.1582 -0.0103 82 PHE B CB 3446 C CG . PHE B 82 ? 1.2223 1.0884 0.9899 -0.1392 0.1707 0.0009 82 PHE B CG 3447 C CD1 . PHE B 82 ? 1.2572 1.1393 1.0425 -0.1366 0.1632 0.0206 82 PHE B CD1 3448 C CD2 . PHE B 82 ? 1.2426 1.0999 1.0346 -0.1300 0.1885 -0.0081 82 PHE B CD2 3449 C CE1 . PHE B 82 ? 1.2036 1.0933 1.0303 -0.1260 0.1730 0.0301 82 PHE B CE1 3450 C CE2 . PHE B 82 ? 1.1872 1.0533 1.0203 -0.1187 0.1977 0.0021 82 PHE B CE2 3451 C CZ . PHE B 82 ? 1.1351 1.0178 0.9856 -0.1172 0.1899 0.0207 82 PHE B CZ 3452 N N . VAL B 83 ? 1.3663 1.2049 0.9570 -0.1822 0.1508 -0.0250 83 VAL B N 3453 C CA . VAL B 83 ? 1.3121 1.1454 0.8610 -0.1961 0.1322 -0.0351 83 VAL B CA 3454 C C . VAL B 83 ? 1.3894 1.2372 0.9170 -0.2027 0.1109 -0.0158 83 VAL B C 3455 O O . VAL B 83 ? 1.3607 1.2137 0.8754 -0.2120 0.0852 -0.0170 83 VAL B O 3456 C CB . VAL B 83 ? 1.2117 1.0217 0.7092 -0.2029 0.1511 -0.0578 83 VAL B CB 3457 C CG1 . VAL B 83 ? 1.3071 1.1154 0.7649 -0.2035 0.1699 -0.0500 83 VAL B CG1 3458 C CG2 . VAL B 83 ? 1.1809 0.9834 0.6433 -0.2174 0.1297 -0.0730 83 VAL B CG2 3459 N N . ASN B 84 ? 1.4524 1.3073 0.9803 -0.1980 0.1210 0.0034 84 ASN B N 3460 C CA . ASN B 84 ? 1.5319 1.3973 1.0352 -0.2044 0.1032 0.0239 84 ASN B CA 3461 C C . ASN B 84 ? 1.4206 1.3051 0.9749 -0.1971 0.0852 0.0463 84 ASN B C 3462 O O . ASN B 84 ? 1.4190 1.3121 0.9657 -0.1991 0.0742 0.0681 84 ASN B O 3463 C CB . ASN B 84 ? 1.6889 1.5476 1.1511 -0.2063 0.1265 0.0319 84 ASN B CB 3464 C CG . ASN B 84 ? 1.7953 1.6354 1.1963 -0.2152 0.1403 0.0093 84 ASN B CG 3465 O OD1 . ASN B 84 ? 1.7502 1.5849 1.1200 -0.2254 0.1207 -0.0035 84 ASN B OD1 3466 N ND2 . ASN B 84 ? 1.9036 1.7337 1.2886 -0.2114 0.1742 0.0026 84 ASN B ND2 3467 N N . TYR B 85 ? 1.3783 1.2687 0.9842 -0.1887 0.0820 0.0405 85 TYR B N 3468 C CA . TYR B 85 ? 1.3081 1.2160 0.9648 -0.1809 0.0655 0.0569 85 TYR B CA 3469 C C . TYR B 85 ? 1.3564 1.2741 1.0277 -0.1843 0.0384 0.0513 85 TYR B C 3470 O O . TYR B 85 ? 1.2985 1.2252 1.0148 -0.1768 0.0332 0.0481 85 TYR B O 3471 C CB . TYR B 85 ? 1.2294 1.1386 0.9337 -0.1681 0.0823 0.0554 85 TYR B CB 3472 C CG . TYR B 85 ? 1.2479 1.1475 0.9403 -0.1652 0.1120 0.0566 85 TYR B CG 3473 C CD1 . TYR B 85 ? 1.2204 1.1268 0.9279 -0.1614 0.1184 0.0770 85 TYR B CD1 3474 C CD2 . TYR B 85 ? 1.3058 1.1894 0.9742 -0.1665 0.1343 0.0373 85 TYR B CD2 3475 C CE1 . TYR B 85 ? 1.2567 1.1569 0.9572 -0.1591 0.1471 0.0787 85 TYR B CE1 3476 C CE2 . TYR B 85 ? 1.3552 1.2319 1.0160 -0.1630 0.1632 0.0377 85 TYR B CE2 3477 C CZ . TYR B 85 ? 1.3506 1.2369 1.0279 -0.1595 0.1698 0.0588 85 TYR B CZ 3478 O OH . TYR B 85 ? 1.4322 1.3142 1.1057 -0.1565 0.1999 0.0599 85 TYR B OH 3479 N N . SER B 86 ? 1.5571 1.4740 1.1893 -0.1959 0.0217 0.0498 86 SER B N 3480 C CA . SER B 86 ? 1.5687 1.4972 1.2135 -0.2010 -0.0054 0.0455 86 SER B CA 3481 C C . SER B 86 ? 1.5369 1.4852 1.2372 -0.1913 -0.0213 0.0594 86 SER B C 3482 O O . SER B 86 ? 1.5827 1.5405 1.3191 -0.1879 -0.0281 0.0509 86 SER B O 3483 C CB . SER B 86 ? 1.6551 1.5833 1.2526 -0.2138 -0.0253 0.0497 86 SER B CB 3484 O OG . SER B 86 ? 1.7229 1.6320 1.2625 -0.2219 -0.0087 0.0389 86 SER B OG 3485 N N . ASN B 87 ? 1.5251 1.4787 1.2317 -0.1871 -0.0260 0.0808 87 ASN B N 3486 C CA . ASN B 87 ? 1.4433 1.4136 1.2011 -0.1778 -0.0422 0.0940 87 ASN B CA 3487 C C . ASN B 87 ? 1.3474 1.3168 1.1390 -0.1660 -0.0260 0.1023 87 ASN B C 3488 O O . ASN B 87 ? 1.3294 1.2986 1.1237 -0.1639 -0.0270 0.1215 87 ASN B O 3489 C CB . ASN B 87 ? 1.3883 1.3664 1.1355 -0.1822 -0.0673 0.1135 87 ASN B CB 3490 C CG . ASN B 87 ? 1.3180 1.2834 1.0147 -0.1891 -0.0589 0.1271 87 ASN B CG 3491 O OD1 . ASN B 87 ? 1.3126 1.2638 0.9781 -0.1918 -0.0338 0.1186 87 ASN B OD1 3492 N ND2 . ASN B 87 ? 1.3150 1.2855 1.0033 -0.1919 -0.0795 0.1487 87 ASN B ND2 3493 N N . ALA B 88 ? 1.2623 1.2308 1.0803 -0.1589 -0.0120 0.0884 88 ALA B N 3494 C CA . ALA B 88 ? 1.1045 1.0748 0.9614 -0.1473 -0.0010 0.0940 88 ALA B CA 3495 C C . ALA B 88 ? 1.2016 1.1849 1.1040 -0.1387 -0.0107 0.0857 88 ALA B C 3496 O O . ALA B 88 ? 1.2719 1.2551 1.1741 -0.1397 -0.0071 0.0700 88 ALA B O 3497 C CB . ALA B 88 ? 0.9150 0.8716 0.7595 -0.1458 0.0271 0.0863 88 ALA B CB 3498 N N . VAL B 89 ? 1.1280 1.1218 1.0687 -0.1305 -0.0228 0.0963 89 VAL B N 3499 C CA . VAL B 89 ? 1.0532 1.0606 1.0346 -0.1220 -0.0323 0.0878 89 VAL B CA 3500 C C . VAL B 89 ? 1.0004 1.0046 1.0016 -0.1137 -0.0159 0.0779 89 VAL B C 3501 O O . VAL B 89 ? 1.0039 1.0123 1.0122 -0.1119 -0.0137 0.0644 89 VAL B O 3502 C CB . VAL B 89 ? 1.0645 1.0831 1.0821 -0.1149 -0.0511 0.0999 89 VAL B CB 3503 C CG1 . VAL B 89 ? 1.1809 1.2130 1.2396 -0.1048 -0.0569 0.0884 89 VAL B CG1 3504 C CG2 . VAL B 89 ? 1.0113 1.0356 1.0151 -0.1219 -0.0711 0.1097 89 VAL B CG2 3505 N N . THR B 90 ? 0.9483 0.9458 0.9596 -0.1090 -0.0051 0.0858 90 THR B N 3506 C CA . THR B 90 ? 0.9047 0.8996 0.9363 -0.1010 0.0085 0.0779 90 THR B CA 3507 C C . THR B 90 ? 0.8956 0.8770 0.9102 -0.1030 0.0300 0.0808 90 THR B C 3508 O O . THR B 90 ? 0.9121 0.8883 0.9107 -0.1081 0.0345 0.0932 90 THR B O 3509 C CB . THR B 90 ? 0.9205 0.9241 0.9970 -0.0903 -0.0010 0.0816 90 THR B CB 3510 O OG1 . THR B 90 ? 0.9101 0.9091 0.9954 -0.0905 0.0003 0.0974 90 THR B OG1 3511 C CG2 . THR B 90 ? 0.9839 1.0012 1.0796 -0.0872 -0.0214 0.0792 90 THR B CG2 3512 N N . LEU B 91 ? 0.8659 0.8424 0.8853 -0.0988 0.0438 0.0701 91 LEU B N 3513 C CA . LEU B 91 ? 0.8501 0.8156 0.8613 -0.0986 0.0655 0.0707 91 LEU B CA 3514 C C . LEU B 91 ? 0.9124 0.8796 0.9578 -0.0881 0.0717 0.0660 91 LEU B C 3515 O O . LEU B 91 ? 0.9627 0.9312 1.0144 -0.0842 0.0687 0.0555 91 LEU B O 3516 C CB . LEU B 91 ? 0.8005 0.7534 0.7710 -0.1063 0.0785 0.0605 91 LEU B CB 3517 C CG . LEU B 91 ? 0.7663 0.7071 0.7318 -0.1039 0.1029 0.0552 91 LEU B CG 3518 C CD1 . LEU B 91 ? 0.8453 0.7849 0.8096 -0.1048 0.1161 0.0676 91 LEU B CD1 3519 C CD2 . LEU B 91 ? 0.7780 0.7047 0.7060 -0.1110 0.1127 0.0414 91 LEU B CD2 3520 N N . HIS B 92 ? 0.9345 0.9020 1.0020 -0.0842 0.0799 0.0749 92 HIS B N 3521 C CA . HIS B 92 ? 0.9146 0.8846 1.0169 -0.0746 0.0843 0.0717 92 HIS B CA 3522 C C . HIS B 92 ? 0.9294 0.8901 1.0261 -0.0737 0.1077 0.0690 92 HIS B C 3523 O O . HIS B 92 ? 0.9639 0.9207 1.0497 -0.0782 0.1223 0.0764 92 HIS B O 3524 C CB . HIS B 92 ? 0.9945 0.9730 1.1353 -0.0702 0.0755 0.0825 92 HIS B CB 3525 C CG . HIS B 92 ? 1.0601 1.0481 1.2218 -0.0656 0.0530 0.0796 92 HIS B CG 3526 N ND1 . HIS B 92 ? 1.1384 1.1325 1.3329 -0.0564 0.0446 0.0735 92 HIS B ND1 3527 C CD2 . HIS B 92 ? 1.0965 1.0892 1.2516 -0.0682 0.0372 0.0811 92 HIS B CD2 3528 C CE1 . HIS B 92 ? 1.1701 1.1718 1.3754 -0.0536 0.0262 0.0700 92 HIS B CE1 3529 N NE2 . HIS B 92 ? 1.1489 1.1504 1.3333 -0.0602 0.0217 0.0748 92 HIS B NE2 3530 N N . LEU B 93 ? 0.9192 0.8764 1.0240 -0.0676 0.1117 0.0590 93 LEU B N 3531 C CA . LEU B 93 ? 0.9032 0.8515 1.0092 -0.0647 0.1331 0.0553 93 LEU B CA 3532 C C . LEU B 93 ? 0.9246 0.8776 1.0713 -0.0537 0.1316 0.0545 93 LEU B C 3533 O O . LEU B 93 ? 0.9111 0.8562 1.0599 -0.0490 0.1419 0.0480 93 LEU B O 3534 C CB . LEU B 93 ? 0.8558 0.7898 0.9265 -0.0690 0.1418 0.0434 93 LEU B CB 3535 C CG . LEU B 93 ? 0.7936 0.7204 0.8198 -0.0805 0.1450 0.0414 93 LEU B CG 3536 C CD1 . LEU B 93 ? 0.8302 0.7408 0.8283 -0.0841 0.1549 0.0273 93 LEU B CD1 3537 C CD2 . LEU B 93 ? 0.7607 0.6873 0.7778 -0.0844 0.1596 0.0502 93 LEU B CD2 3538 N N . GLY B 94 ? 0.9229 0.8881 1.1027 -0.0494 0.1175 0.0610 94 GLY B N 3539 C CA . GLY B 94 ? 0.9043 0.8756 1.1224 -0.0394 0.1119 0.0600 94 GLY B CA 3540 C C . GLY B 94 ? 0.9385 0.9117 1.1866 -0.0360 0.1277 0.0659 94 GLY B C 3541 O O . GLY B 94 ? 1.0517 1.0258 1.2986 -0.0414 0.1405 0.0736 94 GLY B O 3542 N N . ASN B 95 ? 0.8232 0.7983 1.0991 -0.0269 0.1270 0.0629 95 ASN B N 3543 C CA . ASN B 95 ? 0.9394 0.9198 1.2541 -0.0220 0.1398 0.0681 95 ASN B CA 3544 C C . ASN B 95 ? 0.9384 0.9107 1.2369 -0.0256 0.1685 0.0683 95 ASN B C 3545 O O . ASN B 95 ? 0.8691 0.8482 1.1901 -0.0268 0.1831 0.0758 95 ASN B O 3546 C CB . ASN B 95 ? 1.0857 1.0796 1.4369 -0.0233 0.1304 0.0777 95 ASN B CB 3547 C CG . ASN B 95 ? 1.2344 1.2354 1.6008 -0.0195 0.1021 0.0747 95 ASN B CG 3548 O OD1 . ASN B 95 ? 1.2704 1.2786 1.6714 -0.0120 0.0910 0.0733 95 ASN B OD1 3549 N ND2 . ASN B 95 ? 1.2719 1.2713 1.6125 -0.0244 0.0900 0.0731 95 ASN B ND2 3550 N N . ASN B 96 ? 1.0192 0.9770 1.2785 -0.0277 0.1769 0.0593 96 ASN B N 3551 C CA . ASN B 96 ? 0.9998 0.9470 1.2349 -0.0316 0.2035 0.0555 96 ASN B CA 3552 C C . ASN B 96 ? 0.9687 0.9066 1.2167 -0.0229 0.2178 0.0474 96 ASN B C 3553 O O . ASN B 96 ? 1.0354 0.9644 1.2704 -0.0237 0.2421 0.0419 96 ASN B O 3554 C CB . ASN B 96 ? 1.0977 1.0334 1.2775 -0.0418 0.2028 0.0497 96 ASN B CB 3555 C CG . ASN B 96 ? 1.1810 1.1236 1.3444 -0.0511 0.1981 0.0593 96 ASN B CG 3556 O OD1 . ASN B 96 ? 1.2326 1.1753 1.3734 -0.0567 0.1808 0.0594 96 ASN B OD1 3557 N ND2 . ASN B 96 ? 1.1739 1.1227 1.3506 -0.0529 0.2139 0.0685 96 ASN B ND2 3558 N N . GLY B 97 ? 0.9538 0.8932 1.2267 -0.0142 0.2022 0.0465 97 GLY B N 3559 C CA . GLY B 97 ? 0.9565 0.8855 1.2435 -0.0051 0.2115 0.0405 97 GLY B CA 3560 C C . GLY B 97 ? 0.9532 0.8606 1.1968 -0.0095 0.2219 0.0292 97 GLY B C 3561 O O . GLY B 97 ? 1.0217 0.9166 1.2703 -0.0043 0.2399 0.0222 97 GLY B O 3562 N N . LEU B 98 ? 0.8083 0.7113 1.0121 -0.0190 0.2102 0.0266 98 LEU B N 3563 C CA . LEU B 98 ? 0.8760 0.7590 1.0391 -0.0252 0.2167 0.0155 98 LEU B CA 3564 C C . LEU B 98 ? 0.9716 0.8407 1.1475 -0.0172 0.2156 0.0114 98 LEU B C 3565 O O . LEU B 98 ? 0.9901 0.8664 1.1899 -0.0104 0.1989 0.0182 98 LEU B O 3566 C CB . LEU B 98 ? 0.8386 0.7235 0.9673 -0.0359 0.1993 0.0152 98 LEU B CB 3567 C CG . LEU B 98 ? 0.9073 0.7876 0.9946 -0.0479 0.2074 0.0108 98 LEU B CG 3568 C CD1 . LEU B 98 ? 0.8504 0.7236 0.9036 -0.0572 0.1942 0.0048 98 LEU B CD1 3569 C CD2 . LEU B 98 ? 1.0261 0.8924 1.1009 -0.0480 0.2344 0.0019 98 LEU B CD2 3570 N N . GLN B 99 ? 1.0390 0.8874 1.1985 -0.0180 0.2330 0.0004 99 GLN B N 3571 C CA . GLN B 99 ? 1.0536 0.8856 1.2275 -0.0103 0.2333 -0.0026 99 GLN B CA 3572 C C . GLN B 99 ? 1.1020 0.9137 1.2384 -0.0196 0.2305 -0.0115 99 GLN B C 3573 O O . GLN B 99 ? 1.1964 0.9998 1.3375 -0.0174 0.2190 -0.0083 99 GLN B O 3574 C CB . GLN B 99 ? 1.0771 0.9001 1.2770 -0.0004 0.2567 -0.0082 99 GLN B CB 3575 C CG . GLN B 99 ? 1.1033 0.9475 1.3507 0.0097 0.2588 0.0017 99 GLN B CG 3576 C CD . GLN B 99 ? 1.2410 1.0779 1.5230 0.0217 0.2805 -0.0032 99 GLN B CD 3577 O OE1 . GLN B 99 ? 1.3586 1.1769 1.6223 0.0205 0.3020 -0.0168 99 GLN B OE1 3578 N NE2 . GLN B 99 ? 1.2374 1.0891 1.5713 0.0335 0.2745 0.0068 99 GLN B NE2 3579 N N . GLU B 100 ? 1.0790 0.8828 1.1780 -0.0306 0.2406 -0.0221 100 GLU B N 3580 C CA . GLU B 100 ? 1.1561 0.9420 1.2206 -0.0413 0.2365 -0.0315 100 GLU B CA 3581 C C . GLU B 100 ? 1.1242 0.9151 1.1481 -0.0554 0.2339 -0.0365 100 GLU B C 3582 O O . GLU B 100 ? 1.0736 0.8755 1.0900 -0.0569 0.2415 -0.0351 100 GLU B O 3583 C CB . GLU B 100 ? 1.2345 0.9918 1.2971 -0.0387 0.2546 -0.0453 100 GLU B CB 3584 C CG . GLU B 100 ? 1.3112 1.0595 1.3509 -0.0420 0.2775 -0.0600 100 GLU B CG 3585 C CD . GLU B 100 ? 1.4505 1.1672 1.4816 -0.0417 0.2928 -0.0777 100 GLU B CD 3586 O OE1 . GLU B 100 ? 1.4744 1.1746 1.4902 -0.0495 0.2827 -0.0825 100 GLU B OE1 3587 O OE2 . GLU B 100 ? 1.5225 1.2310 1.5645 -0.0336 0.3156 -0.0871 100 GLU B OE2 3588 N N . ILE B 101 ? 1.1298 0.9132 1.1290 -0.0660 0.2222 -0.0410 101 ILE B N 3589 C CA . ILE B 101 ? 1.0955 0.8796 1.0550 -0.0802 0.2184 -0.0479 101 ILE B CA 3590 C C . ILE B 101 ? 1.1966 0.9539 1.1321 -0.0883 0.2253 -0.0644 101 ILE B C 3591 O O . ILE B 101 ? 1.3307 1.0802 1.2675 -0.0930 0.2148 -0.0649 101 ILE B O 3592 C CB . ILE B 101 ? 1.0367 0.8403 0.9924 -0.0868 0.1952 -0.0385 101 ILE B CB 3593 C CG1 . ILE B 101 ? 1.0043 0.8324 0.9843 -0.0790 0.1874 -0.0241 101 ILE B CG1 3594 C CG2 . ILE B 101 ? 1.0256 0.8292 0.9429 -0.1014 0.1893 -0.0456 101 ILE B CG2 3595 C CD1 . ILE B 101 ? 1.0248 0.8617 1.0371 -0.0698 0.1760 -0.0146 101 ILE B CD1 3596 N N . ARG B 102 ? 1.2570 0.9997 1.1712 -0.0900 0.2438 -0.0782 102 ARG B N 3597 C CA . ARG B 102 ? 1.4237 1.1385 1.3133 -0.0980 0.2511 -0.0972 102 ARG B CA 3598 C C . ARG B 102 ? 1.3739 1.0909 1.2341 -0.1145 0.2321 -0.1003 102 ARG B C 3599 O O . ARG B 102 ? 1.3475 1.0858 1.1941 -0.1202 0.2198 -0.0921 102 ARG B O 3600 C CB . ARG B 102 ? 1.6121 1.3143 1.4785 -0.0972 0.2747 -0.1128 102 ARG B CB 3601 C CG . ARG B 102 ? 1.7060 1.4085 1.6073 -0.0806 0.2950 -0.1099 102 ARG B CG 3602 C CD . ARG B 102 ? 1.8555 1.5389 1.7376 -0.0788 0.3222 -0.1301 102 ARG B CD 3603 N NE . ARG B 102 ? 1.9484 1.6302 1.8731 -0.0617 0.3415 -0.1287 102 ARG B NE 3604 C CZ . ARG B 102 ? 2.0674 1.7284 2.0215 -0.0526 0.3470 -0.1349 102 ARG B CZ 3605 N NH1 . ARG B 102 ? 2.1152 1.7540 2.0595 -0.0598 0.3357 -0.1426 102 ARG B NH1 3606 N NH2 . ARG B 102 ? 2.1084 1.7710 2.1045 -0.0365 0.3634 -0.1325 102 ARG B NH2 3607 N N . PRO B 103 ? 1.4691 1.1645 1.3240 -0.1221 0.2289 -0.1112 103 PRO B N 3608 C CA . PRO B 103 ? 1.5337 1.2318 1.3714 -0.1377 0.2099 -0.1133 103 PRO B CA 3609 C C . PRO B 103 ? 1.5073 1.2203 1.3095 -0.1488 0.2003 -0.1156 103 PRO B C 3610 O O . PRO B 103 ? 1.5065 1.2078 1.2754 -0.1536 0.2101 -0.1298 103 PRO B O 3611 C CB . PRO B 103 ? 1.6993 1.3639 1.5282 -0.1446 0.2169 -0.1320 103 PRO B CB 3612 C CG . PRO B 103 ? 1.7184 1.3672 1.5788 -0.1294 0.2327 -0.1303 103 PRO B CG 3613 C CD . PRO B 103 ? 1.6295 1.2952 1.4987 -0.1159 0.2442 -0.1226 103 PRO B CD 3614 N N . GLY B 104 ? 1.5349 1.2737 1.3441 -0.1523 0.1811 -0.1015 104 GLY B N 3615 C CA . GLY B 104 ? 1.5646 1.3191 1.3456 -0.1626 0.1678 -0.1006 104 GLY B CA 3616 C C . GLY B 104 ? 1.5961 1.3590 1.3600 -0.1576 0.1769 -0.0964 104 GLY B C 3617 O O . GLY B 104 ? 1.7259 1.4825 1.4505 -0.1661 0.1789 -0.1058 104 GLY B O 3618 N N . ALA B 105 ? 1.4743 1.2515 1.2667 -0.1445 0.1819 -0.0816 105 ALA B N 3619 C CA . ALA B 105 ? 1.4554 1.2418 1.2379 -0.1398 0.1918 -0.0748 105 ALA B CA 3620 C C . ALA B 105 ? 1.3116 1.1184 1.0777 -0.1473 0.1734 -0.0636 105 ALA B C 3621 O O . ALA B 105 ? 1.1735 0.9797 0.9052 -0.1531 0.1772 -0.0647 105 ALA B O 3622 C CB . ALA B 105 ? 1.4370 1.2325 1.2602 -0.1243 0.2014 -0.0627 105 ALA B CB 3623 N N . PHE B 106 ? 1.2894 1.1143 1.0800 -0.1468 0.1536 -0.0527 106 PHE B N 3624 C CA . PHE B 106 ? 1.3245 1.1694 1.1078 -0.1522 0.1343 -0.0414 106 PHE B CA 3625 C C . PHE B 106 ? 1.3695 1.2106 1.1183 -0.1674 0.1205 -0.0507 106 PHE B C 3626 O O . PHE B 106 ? 1.3970 1.2526 1.1561 -0.1724 0.1000 -0.0464 106 PHE B O 3627 C CB . PHE B 106 ? 1.3292 1.1946 1.1518 -0.1459 0.1186 -0.0294 106 PHE B CB 3628 C CG . PHE B 106 ? 1.3790 1.2466 1.2377 -0.1318 0.1286 -0.0233 106 PHE B CG 3629 C CD1 . PHE B 106 ? 1.3842 1.2626 1.2592 -0.1235 0.1320 -0.0112 106 PHE B CD1 3630 C CD2 . PHE B 106 ? 1.4191 1.2782 1.2965 -0.1275 0.1330 -0.0286 106 PHE B CD2 3631 C CE1 . PHE B 106 ? 1.3766 1.2581 1.2864 -0.1111 0.1387 -0.0061 106 PHE B CE1 3632 C CE2 . PHE B 106 ? 1.3851 1.2469 1.2945 -0.1146 0.1394 -0.0223 106 PHE B CE2 3633 C CZ . PHE B 106 ? 1.3302 1.2038 1.2563 -0.1064 0.1417 -0.0118 106 PHE B CZ 3634 N N . SER B 107 ? 1.3744 1.1967 1.0835 -0.1747 0.1313 -0.0643 107 SER B N 3635 C CA . SER B 107 ? 1.4484 1.2638 1.1239 -0.1899 0.1177 -0.0766 107 SER B CA 3636 C C . SER B 107 ? 1.4288 1.2636 1.0889 -0.1973 0.0948 -0.0650 107 SER B C 3637 O O . SER B 107 ? 1.4922 1.3341 1.1517 -0.2072 0.0741 -0.0680 107 SER B O 3638 C CB . SER B 107 ? 1.5992 1.3891 1.2319 -0.1953 0.1353 -0.0956 107 SER B CB 3639 O OG . SER B 107 ? 1.5983 1.3672 1.2462 -0.1914 0.1509 -0.1099 107 SER B OG 3640 N N . GLY B 108 ? 1.4235 1.2673 1.0747 -0.1927 0.0980 -0.0505 108 GLY B N 3641 C CA . GLY B 108 ? 1.5233 1.3817 1.1548 -0.1997 0.0771 -0.0383 108 GLY B CA 3642 C C . GLY B 108 ? 1.5285 1.4115 1.1997 -0.1933 0.0590 -0.0187 108 GLY B C 3643 O O . GLY B 108 ? 1.5745 1.4701 1.2356 -0.1989 0.0383 -0.0084 108 GLY B O 3644 N N . LEU B 109 ? 1.4625 1.3521 1.1788 -0.1815 0.0657 -0.0141 109 LEU B N 3645 C CA . LEU B 109 ? 1.3387 1.2501 1.0943 -0.1740 0.0505 0.0019 109 LEU B CA 3646 C C . LEU B 109 ? 1.3663 1.2924 1.1367 -0.1797 0.0269 0.0000 109 LEU B C 3647 O O . LEU B 109 ? 1.3347 1.2698 1.1405 -0.1745 0.0244 -0.0021 109 LEU B O 3648 C CB . LEU B 109 ? 1.2146 1.1283 1.0111 -0.1604 0.0632 0.0043 109 LEU B CB 3649 C CG . LEU B 109 ? 1.2056 1.1080 0.9990 -0.1533 0.0870 0.0064 109 LEU B CG 3650 C CD1 . LEU B 109 ? 1.0974 1.0045 0.9349 -0.1403 0.0942 0.0092 109 LEU B CD1 3651 C CD2 . LEU B 109 ? 1.2519 1.1592 1.0308 -0.1542 0.0865 0.0218 109 LEU B CD2 3652 N N . LYS B 110 ? 1.4169 1.3468 1.1605 -0.1905 0.0096 0.0014 110 LYS B N 3653 C CA . LYS B 110 ? 1.3728 1.3172 1.1296 -0.1978 -0.0130 -0.0018 110 LYS B CA 3654 C C . LYS B 110 ? 1.2618 1.2300 1.0668 -0.1884 -0.0263 0.0100 110 LYS B C 3655 O O . LYS B 110 ? 1.2463 1.2259 1.0809 -0.1881 -0.0316 0.0042 110 LYS B O 3656 C CB . LYS B 110 ? 1.4854 1.4301 1.2035 -0.2104 -0.0313 -0.0004 110 LYS B CB 3657 C CG . LYS B 110 ? 1.6126 1.5466 1.3052 -0.2247 -0.0359 -0.0193 110 LYS B CG 3658 C CD . LYS B 110 ? 1.6966 1.6051 1.3710 -0.2250 -0.0097 -0.0359 110 LYS B CD 3659 C CE . LYS B 110 ? 1.7581 1.6576 1.4302 -0.2367 -0.0137 -0.0550 110 LYS B CE 3660 N NZ . LYS B 110 ? 1.7581 1.6335 1.4275 -0.2340 0.0116 -0.0694 110 LYS B NZ 3661 N N . THR B 111 ? 1.1453 1.1207 0.9587 -0.1809 -0.0306 0.0262 111 THR B N 3662 C CA . THR B 111 ? 1.1299 1.1269 0.9867 -0.1724 -0.0461 0.0366 111 THR B CA 3663 C C . THR B 111 ? 1.1621 1.1606 1.0513 -0.1581 -0.0335 0.0415 111 THR B C 3664 O O . THR B 111 ? 1.2003 1.2107 1.1172 -0.1501 -0.0438 0.0530 111 THR B O 3665 C CB . THR B 111 ? 1.1967 1.2020 1.0459 -0.1746 -0.0665 0.0527 111 THR B CB 3666 O OG1 . THR B 111 ? 1.1263 1.1222 0.9651 -0.1694 -0.0563 0.0661 111 THR B OG1 3667 C CG2 . THR B 111 ? 1.3086 1.3095 1.1159 -0.1895 -0.0790 0.0488 111 THR B CG2 3668 N N . LEU B 112 ? 1.1376 1.1234 1.0249 -0.1548 -0.0127 0.0325 112 LEU B N 3669 C CA . LEU B 112 ? 0.9442 0.9315 0.8619 -0.1418 -0.0023 0.0362 112 LEU B CA 3670 C C . LEU B 112 ? 0.9290 0.9326 0.8846 -0.1350 -0.0096 0.0318 112 LEU B C 3671 O O . LEU B 112 ? 1.0385 1.0453 0.9945 -0.1400 -0.0104 0.0218 112 LEU B O 3672 C CB . LEU B 112 ? 0.8492 0.8182 0.7540 -0.1399 0.0212 0.0291 112 LEU B CB 3673 C CG . LEU B 112 ? 0.7433 0.7135 0.6784 -0.1270 0.0309 0.0337 112 LEU B CG 3674 C CD1 . LEU B 112 ? 0.6922 0.6654 0.6343 -0.1232 0.0280 0.0487 112 LEU B CD1 3675 C CD2 . LEU B 112 ? 0.7539 0.7075 0.6811 -0.1247 0.0525 0.0259 112 LEU B CD2 3676 N N . LYS B 113 ? 0.8991 0.9128 0.8864 -0.1239 -0.0143 0.0388 113 LYS B N 3677 C CA . LYS B 113 ? 0.8884 0.9189 0.9102 -0.1164 -0.0211 0.0341 113 LYS B CA 3678 C C . LYS B 113 ? 0.8989 0.9262 0.9387 -0.1056 -0.0093 0.0312 113 LYS B C 3679 O O . LYS B 113 ? 0.9349 0.9675 0.9853 -0.1025 -0.0053 0.0231 113 LYS B O 3680 C CB . LYS B 113 ? 0.9394 0.9862 0.9867 -0.1118 -0.0401 0.0421 113 LYS B CB 3681 C CG . LYS B 113 ? 1.0745 1.1269 1.1077 -0.1216 -0.0556 0.0466 113 LYS B CG 3682 C CD . LYS B 113 ? 1.1895 1.2607 1.2407 -0.1242 -0.0654 0.0382 113 LYS B CD 3683 C CE . LYS B 113 ? 1.3347 1.4067 1.3620 -0.1380 -0.0764 0.0384 113 LYS B CE 3684 N NZ . LYS B 113 ? 1.3618 1.4266 1.3684 -0.1414 -0.0873 0.0520 113 LYS B NZ 3685 N N . ARG B 114 ? 0.8515 0.8706 0.8949 -0.1004 -0.0041 0.0388 114 ARG B N 3686 C CA . ARG B 114 ? 0.7163 0.7334 0.7801 -0.0900 0.0039 0.0370 114 ARG B CA 3687 C C . ARG B 114 ? 0.7914 0.7914 0.8397 -0.0909 0.0214 0.0386 114 ARG B C 3688 O O . ARG B 114 ? 0.8611 0.8531 0.8943 -0.0954 0.0260 0.0463 114 ARG B O 3689 C CB . ARG B 114 ? 0.6061 0.6319 0.7011 -0.0813 -0.0072 0.0437 114 ARG B CB 3690 C CG . ARG B 114 ? 0.5765 0.6005 0.6938 -0.0713 -0.0019 0.0418 114 ARG B CG 3691 C CD . ARG B 114 ? 0.6668 0.6990 0.8173 -0.0634 -0.0154 0.0457 114 ARG B CD 3692 N NE . ARG B 114 ? 0.7252 0.7608 0.8989 -0.0534 -0.0156 0.0383 114 ARG B NE 3693 C CZ . ARG B 114 ? 0.7790 0.8195 0.9836 -0.0456 -0.0264 0.0381 114 ARG B CZ 3694 N NH1 . ARG B 114 ? 0.8656 0.9073 1.0845 -0.0463 -0.0372 0.0465 114 ARG B NH1 3695 N NH2 . ARG B 114 ? 0.7042 0.7473 0.9254 -0.0373 -0.0275 0.0297 114 ARG B NH2 3696 N N . LEU B 115 ? 0.8566 0.8516 0.9093 -0.0864 0.0316 0.0319 115 LEU B N 3697 C CA . LEU B 115 ? 0.8922 0.8719 0.9360 -0.0856 0.0488 0.0321 115 LEU B CA 3698 C C . LEU B 115 ? 0.8612 0.8420 0.9312 -0.0746 0.0522 0.0313 115 LEU B C 3699 O O . LEU B 115 ? 0.8639 0.8514 0.9442 -0.0700 0.0466 0.0261 115 LEU B O 3700 C CB . LEU B 115 ? 0.9172 0.8837 0.9325 -0.0935 0.0594 0.0239 115 LEU B CB 3701 C CG . LEU B 115 ? 0.8717 0.8214 0.8805 -0.0913 0.0784 0.0215 115 LEU B CG 3702 C CD1 . LEU B 115 ? 0.8948 0.8397 0.8966 -0.0924 0.0873 0.0285 115 LEU B CD1 3703 C CD2 . LEU B 115 ? 0.8765 0.8113 0.8603 -0.0988 0.0870 0.0116 115 LEU B CD2 3704 N N . HIS B 116 ? 0.8355 0.8107 0.9160 -0.0708 0.0612 0.0369 116 HIS B N 3705 C CA . HIS B 116 ? 0.8057 0.7818 0.9125 -0.0609 0.0637 0.0366 116 HIS B CA 3706 C C . HIS B 116 ? 0.7952 0.7573 0.8956 -0.0603 0.0822 0.0353 116 HIS B C 3707 O O . HIS B 116 ? 0.7447 0.6981 0.8284 -0.0658 0.0950 0.0373 116 HIS B O 3708 C CB . HIS B 116 ? 0.8178 0.8022 0.9546 -0.0558 0.0563 0.0443 116 HIS B CB 3709 C CG . HIS B 116 ? 0.9059 0.9024 1.0540 -0.0548 0.0380 0.0445 116 HIS B CG 3710 N ND1 . HIS B 116 ? 0.8574 0.8635 1.0295 -0.0465 0.0255 0.0395 116 HIS B ND1 3711 C CD2 . HIS B 116 ? 1.0182 1.0184 1.1574 -0.0605 0.0299 0.0486 116 HIS B CD2 3712 C CE1 . HIS B 116 ? 0.8362 0.8512 1.0157 -0.0466 0.0119 0.0393 116 HIS B CE1 3713 N NE2 . HIS B 116 ? 0.9431 0.9549 1.1046 -0.0548 0.0136 0.0457 116 HIS B NE2 3714 N N . LEU B 117 ? 0.8579 0.8177 0.9709 -0.0531 0.0836 0.0319 117 LEU B N 3715 C CA . LEU B 117 ? 0.8453 0.7919 0.9586 -0.0504 0.1000 0.0304 117 LEU B CA 3716 C C . LEU B 117 ? 0.8444 0.7958 0.9912 -0.0392 0.0965 0.0332 117 LEU B C 3717 O O . LEU B 117 ? 0.8714 0.8136 1.0240 -0.0343 0.1048 0.0319 117 LEU B O 3718 C CB . LEU B 117 ? 0.8704 0.8041 0.9591 -0.0548 0.1053 0.0231 117 LEU B CB 3719 C CG . LEU B 117 ? 0.9447 0.8699 0.9998 -0.0666 0.1113 0.0184 117 LEU B CG 3720 C CD1 . LEU B 117 ? 0.9717 0.8880 1.0086 -0.0721 0.1106 0.0113 117 LEU B CD1 3721 C CD2 . LEU B 117 ? 1.0266 0.9393 1.0728 -0.0680 0.1303 0.0172 117 LEU B CD2 3722 N N . ASN B 118 ? 0.7283 0.6934 0.8983 -0.0351 0.0829 0.0369 118 ASN B N 3723 C CA . ASN B 118 ? 0.7121 0.6843 0.9130 -0.0252 0.0736 0.0382 118 ASN B CA 3724 C C . ASN B 118 ? 0.7470 0.7163 0.9747 -0.0197 0.0847 0.0426 118 ASN B C 3725 O O . ASN B 118 ? 0.7981 0.7637 1.0264 -0.0235 0.0998 0.0459 118 ASN B O 3726 C CB . ASN B 118 ? 0.7864 0.7727 1.0060 -0.0232 0.0560 0.0389 118 ASN B CB 3727 C CG . ASN B 118 ? 0.9306 0.9194 1.1613 -0.0278 0.0594 0.0457 118 ASN B CG 3728 O OD1 . ASN B 118 ? 1.0340 1.0249 1.2926 -0.0252 0.0640 0.0513 118 ASN B OD1 3729 N ND2 . ASN B 118 ? 0.9537 0.9432 1.1644 -0.0349 0.0569 0.0463 118 ASN B ND2 3730 N N . ASN B 119 ? 0.8321 0.8043 1.0819 -0.0108 0.0770 0.0428 119 ASN B N 3731 C CA . ASN B 119 ? 0.8218 0.7959 1.1074 -0.0040 0.0829 0.0473 119 ASN B CA 3732 C C . ASN B 119 ? 0.9220 0.8844 1.2043 -0.0051 0.1071 0.0480 119 ASN B C 3733 O O . ASN B 119 ? 1.0516 1.0179 1.3568 -0.0048 0.1190 0.0522 119 ASN B O 3734 C CB . ASN B 119 ? 0.8174 0.8045 1.1348 -0.0042 0.0763 0.0520 119 ASN B CB 3735 C CG . ASN B 119 ? 0.8528 0.8503 1.1770 -0.0022 0.0523 0.0488 119 ASN B CG 3736 O OD1 . ASN B 119 ? 0.9547 0.9585 1.3006 0.0051 0.0379 0.0474 119 ASN B OD1 3737 N ND2 . ASN B 119 ? 0.8358 0.8351 1.1416 -0.0084 0.0473 0.0471 119 ASN B ND2 3738 N N . ASN B 120 ? 0.8929 0.8406 1.1474 -0.0066 0.1153 0.0433 120 ASN B N 3739 C CA . ASN B 120 ? 0.9596 0.8936 1.2106 -0.0064 0.1382 0.0409 120 ASN B CA 3740 C C . ASN B 120 ? 0.9492 0.8721 1.2087 0.0017 0.1389 0.0399 120 ASN B C 3741 O O . ASN B 120 ? 1.0034 0.9329 1.2815 0.0090 0.1223 0.0441 120 ASN B O 3742 C CB . ASN B 120 ? 0.9699 0.8925 1.1782 -0.0175 0.1499 0.0348 120 ASN B CB 3743 C CG . ASN B 120 ? 0.9327 0.8644 1.1335 -0.0250 0.1521 0.0382 120 ASN B CG 3744 O OD1 . ASN B 120 ? 1.0025 0.9370 1.2176 -0.0247 0.1667 0.0417 120 ASN B OD1 3745 N ND2 . ASN B 120 ? 0.8807 0.8174 1.0604 -0.0318 0.1379 0.0381 120 ASN B ND2 3746 N N . LYS B 121 ? 0.8227 0.7275 1.0678 0.0007 0.1571 0.0344 121 LYS B N 3747 C CA . LYS B 121 ? 0.9224 0.8137 1.1792 0.0089 0.1589 0.0346 121 LYS B CA 3748 C C . LYS B 121 ? 0.9909 0.8610 1.2115 0.0023 0.1640 0.0280 121 LYS B C 3749 O O . LYS B 121 ? 1.0263 0.8780 1.2476 0.0047 0.1798 0.0227 121 LYS B O 3750 C CB . LYS B 121 ? 1.0897 0.9776 1.3797 0.0174 0.1777 0.0339 121 LYS B CB 3751 C CG . LYS B 121 ? 1.1255 1.0346 1.4608 0.0244 0.1731 0.0414 121 LYS B CG 3752 C CD . LYS B 121 ? 1.1595 1.0663 1.5307 0.0331 0.1942 0.0403 121 LYS B CD 3753 C CE . LYS B 121 ? 1.1887 1.1180 1.6124 0.0402 0.1881 0.0486 121 LYS B CE 3754 N NZ . LYS B 121 ? 1.1950 1.1242 1.6602 0.0501 0.2084 0.0479 121 LYS B NZ 3755 N N . LEU B 122 ? 1.0346 0.9076 1.2270 -0.0058 0.1509 0.0278 122 LEU B N 3756 C CA . LEU B 122 ? 1.0518 0.9071 1.2121 -0.0142 0.1542 0.0221 122 LEU B CA 3757 C C . LEU B 122 ? 1.0707 0.9190 1.2341 -0.0100 0.1432 0.0287 122 LEU B C 3758 O O . LEU B 122 ? 1.0389 0.9018 1.2064 -0.0072 0.1263 0.0357 122 LEU B O 3759 C CB . LEU B 122 ? 0.9632 0.8270 1.0929 -0.0265 0.1475 0.0185 122 LEU B CB 3760 C CG . LEU B 122 ? 0.8906 0.7623 1.0116 -0.0322 0.1546 0.0150 122 LEU B CG 3761 C CD1 . LEU B 122 ? 0.8787 0.7626 0.9779 -0.0417 0.1416 0.0147 122 LEU B CD1 3762 C CD2 . LEU B 122 ? 1.0429 0.8961 1.1467 -0.0367 0.1752 0.0054 122 LEU B CD2 3763 N N . GLU B 123 ? 1.2153 1.0404 1.3750 -0.0098 0.1527 0.0265 123 GLU B N 3764 C CA . GLU B 123 ? 1.2321 1.0488 1.3941 -0.0063 0.1427 0.0356 123 GLU B CA 3765 C C . GLU B 123 ? 1.1856 0.9914 1.3164 -0.0189 0.1417 0.0334 123 GLU B C 3766 O O . GLU B 123 ? 1.1811 0.9899 1.3057 -0.0197 0.1302 0.0424 123 GLU B O 3767 C CB . GLU B 123 ? 1.3045 1.1022 1.4930 0.0046 0.1511 0.0386 123 GLU B CB 3768 C CG . GLU B 123 ? 1.4078 1.1918 1.6026 0.0053 0.1729 0.0263 123 GLU B CG 3769 C CD . GLU B 123 ? 1.4903 1.2621 1.7220 0.0195 0.1803 0.0295 123 GLU B CD 3770 O OE1 . GLU B 123 ? 1.5093 1.2839 1.7616 0.0286 0.1661 0.0429 123 GLU B OE1 3771 O OE2 . GLU B 123 ? 1.5425 1.3022 1.7824 0.0218 0.2003 0.0186 123 GLU B OE2 3772 N N . VAL B 124 ? 1.0504 0.8447 1.1614 -0.0294 0.1536 0.0214 124 VAL B N 3773 C CA . VAL B 124 ? 0.9418 0.7250 1.0278 -0.0425 0.1529 0.0182 124 VAL B CA 3774 C C . VAL B 124 ? 0.8547 0.6494 0.9162 -0.0552 0.1521 0.0088 124 VAL B C 3775 O O . VAL B 124 ? 0.8439 0.6402 0.9003 -0.0563 0.1600 0.0003 124 VAL B O 3776 C CB . VAL B 124 ? 0.9797 0.7304 1.0657 -0.0444 0.1664 0.0119 124 VAL B CB 3777 C CG1 . VAL B 124 ? 1.0213 0.7605 1.0855 -0.0592 0.1645 0.0093 124 VAL B CG1 3778 C CG2 . VAL B 124 ? 1.0229 0.7609 1.1364 -0.0309 0.1662 0.0227 124 VAL B CG2 3779 N N . LEU B 125 ? 0.8919 0.6954 0.9388 -0.0647 0.1426 0.0112 125 LEU B N 3780 C CA . LEU B 125 ? 0.9725 0.7852 0.9983 -0.0776 0.1401 0.0028 125 LEU B CA 3781 C C . LEU B 125 ? 1.0629 0.8551 1.0731 -0.0908 0.1453 -0.0047 125 LEU B C 3782 O O . LEU B 125 ? 1.1187 0.9134 1.1259 -0.0981 0.1395 0.0002 125 LEU B O 3783 C CB . LEU B 125 ? 0.9982 0.8384 1.0232 -0.0792 0.1258 0.0090 125 LEU B CB 3784 C CG . LEU B 125 ? 0.9239 0.7862 0.9610 -0.0698 0.1184 0.0124 125 LEU B CG 3785 C CD1 . LEU B 125 ? 0.8825 0.7691 0.9193 -0.0709 0.1050 0.0162 125 LEU B CD1 3786 C CD2 . LEU B 125 ? 0.9164 0.7800 0.9465 -0.0729 0.1232 0.0051 125 LEU B CD2 3787 N N . ARG B 126 ? 1.1743 0.9464 1.1749 -0.0943 0.1569 -0.0170 126 ARG B N 3788 C CA . ARG B 126 ? 1.3001 1.0502 1.2856 -0.1076 0.1612 -0.0274 126 ARG B CA 3789 C C . ARG B 126 ? 1.2674 1.0337 1.2370 -0.1224 0.1501 -0.0301 126 ARG B C 3790 O O . ARG B 126 ? 1.2617 1.0524 1.2266 -0.1224 0.1421 -0.0285 126 ARG B O 3791 C CB . ARG B 126 ? 1.4562 1.1849 1.4299 -0.1083 0.1753 -0.0434 126 ARG B CB 3792 C CG . ARG B 126 ? 1.5214 1.2312 1.5152 -0.0942 0.1885 -0.0430 126 ARG B CG 3793 C CD . ARG B 126 ? 1.6297 1.3135 1.6357 -0.0949 0.1905 -0.0402 126 ARG B CD 3794 N NE . ARG B 126 ? 1.7071 1.3873 1.7422 -0.0787 0.1926 -0.0275 126 ARG B NE 3795 C CZ . ARG B 126 ? 1.7883 1.4544 1.8401 -0.0665 0.2055 -0.0324 126 ARG B CZ 3796 N NH1 . ARG B 126 ? 1.8633 1.5170 1.9022 -0.0687 0.2199 -0.0507 126 ARG B NH1 3797 N NH2 . ARG B 126 ? 1.7769 1.4422 1.8582 -0.0519 0.2041 -0.0191 126 ARG B NH2 3798 N N . GLU B 127 ? 1.2309 0.9836 1.1958 -0.1350 0.1492 -0.0336 127 GLU B N 3799 C CA . GLU B 127 ? 1.2817 1.0518 1.2387 -0.1492 0.1381 -0.0346 127 GLU B CA 3800 C C . GLU B 127 ? 1.2664 1.0415 1.2020 -0.1577 0.1344 -0.0479 127 GLU B C 3801 O O . GLU B 127 ? 1.2195 1.0173 1.1513 -0.1654 0.1226 -0.0471 127 GLU B O 3802 C CB . GLU B 127 ? 1.3832 1.1365 1.3440 -0.1618 0.1388 -0.0348 127 GLU B CB 3803 C CG . GLU B 127 ? 1.5179 1.2423 1.4650 -0.1733 0.1441 -0.0523 127 GLU B CG 3804 C CD . GLU B 127 ? 1.6425 1.3543 1.5961 -0.1890 0.1417 -0.0526 127 GLU B CD 3805 O OE1 . GLU B 127 ? 1.7130 1.4119 1.6543 -0.2034 0.1395 -0.0680 127 GLU B OE1 3806 O OE2 . GLU B 127 ? 1.6491 1.3639 1.6196 -0.1877 0.1419 -0.0371 127 GLU B OE2 3807 N N . ASP B 128 ? 1.3318 1.0863 1.2533 -0.1560 0.1445 -0.0598 128 ASP B N 3808 C CA . ASP B 128 ? 1.4023 1.1578 1.2970 -0.1647 0.1419 -0.0726 128 ASP B CA 3809 C C . ASP B 128 ? 1.3623 1.1307 1.2509 -0.1540 0.1455 -0.0696 128 ASP B C 3810 O O . ASP B 128 ? 1.4105 1.1770 1.2737 -0.1591 0.1466 -0.0788 128 ASP B O 3811 C CB . ASP B 128 ? 1.5164 1.2386 1.3935 -0.1728 0.1516 -0.0910 128 ASP B CB 3812 C CG . ASP B 128 ? 1.6295 1.3262 1.5193 -0.1605 0.1688 -0.0928 128 ASP B CG 3813 O OD1 . ASP B 128 ? 1.6782 1.3447 1.5617 -0.1658 0.1771 -0.1070 128 ASP B OD1 3814 O OD2 . ASP B 128 ? 1.6530 1.3598 1.5615 -0.1454 0.1732 -0.0806 128 ASP B OD2 3815 N N . THR B 129 ? 1.3184 1.0998 1.2298 -0.1399 0.1468 -0.0563 129 THR B N 3816 C CA . THR B 129 ? 1.3409 1.1342 1.2535 -0.1296 0.1507 -0.0517 129 THR B CA 3817 C C . THR B 129 ? 1.3871 1.2030 1.2861 -0.1355 0.1380 -0.0490 129 THR B C 3818 O O . THR B 129 ? 1.4618 1.2772 1.3422 -0.1364 0.1426 -0.0524 129 THR B O 3819 C CB . THR B 129 ? 1.2771 1.0818 1.2204 -0.1145 0.1505 -0.0380 129 THR B CB 3820 O OG1 . THR B 129 ? 1.3307 1.1136 1.2873 -0.1067 0.1632 -0.0394 129 THR B OG1 3821 C CG2 . THR B 129 ? 1.2267 1.0480 1.1755 -0.1062 0.1510 -0.0320 129 THR B CG2 3822 N N . PHE B 130 ? 1.3265 1.1623 1.2352 -0.1394 0.1226 -0.0423 130 PHE B N 3823 C CA . PHE B 130 ? 1.3364 1.1938 1.2374 -0.1443 0.1086 -0.0390 130 PHE B CA 3824 C C . PHE B 130 ? 1.4658 1.3192 1.3440 -0.1606 0.1005 -0.0489 130 PHE B C 3825 O O . PHE B 130 ? 1.5239 1.3935 1.4103 -0.1675 0.0867 -0.0467 130 PHE B O 3826 C CB . PHE B 130 ? 1.2395 1.1224 1.1658 -0.1390 0.0963 -0.0283 130 PHE B CB 3827 C CG . PHE B 130 ? 1.1845 1.0711 1.1336 -0.1241 0.1013 -0.0199 130 PHE B CG 3828 C CD1 . PHE B 130 ? 1.1347 1.0279 1.0905 -0.1150 0.1029 -0.0144 130 PHE B CD1 3829 C CD2 . PHE B 130 ? 1.1234 1.0071 1.0877 -0.1199 0.1035 -0.0166 130 PHE B CD2 3830 C CE1 . PHE B 130 ? 0.9626 0.8600 0.9417 -0.1020 0.1054 -0.0075 130 PHE B CE1 3831 C CE2 . PHE B 130 ? 1.0216 0.9093 1.0052 -0.1065 0.1056 -0.0090 130 PHE B CE2 3832 C CZ . PHE B 130 ? 0.9620 0.8568 0.9540 -0.0975 0.1058 -0.0053 130 PHE B CZ 3833 N N . LEU B 131 ? 1.4821 1.3145 1.3325 -0.1667 0.1090 -0.0607 131 LEU B N 3834 C CA . LEU B 131 ? 1.5369 1.3616 1.3639 -0.1829 0.1009 -0.0727 131 LEU B CA 3835 C C . LEU B 131 ? 1.5353 1.3810 1.3491 -0.1898 0.0829 -0.0687 131 LEU B C 3836 O O . LEU B 131 ? 1.5668 1.4220 1.3816 -0.2012 0.0677 -0.0714 131 LEU B O 3837 C CB . LEU B 131 ? 1.5943 1.3893 1.3919 -0.1867 0.1155 -0.0888 131 LEU B CB 3838 C CG . LEU B 131 ? 1.6591 1.4312 1.4487 -0.1993 0.1159 -0.1045 131 LEU B CG 3839 C CD1 . LEU B 131 ? 1.7233 1.4712 1.4739 -0.2057 0.1248 -0.1232 131 LEU B CD1 3840 C CD2 . LEU B 131 ? 1.6791 1.4669 1.4759 -0.2130 0.0956 -0.1034 131 LEU B CD2 3841 N N . GLY B 132 ? 1.4959 1.3492 1.3001 -0.1829 0.0844 -0.0612 132 GLY B N 3842 C CA . GLY B 132 ? 1.5465 1.4135 1.3308 -0.1898 0.0687 -0.0573 132 GLY B CA 3843 C C . GLY B 132 ? 1.5079 1.4034 1.3164 -0.1900 0.0479 -0.0460 132 GLY B C 3844 O O . GLY B 132 ? 1.5645 1.4696 1.3595 -0.1997 0.0307 -0.0460 132 GLY B O 3845 N N . LEU B 133 ? 1.4365 1.3457 1.2808 -0.1792 0.0487 -0.0371 133 LEU B N 3846 C CA . LEU B 133 ? 1.3983 1.3349 1.2672 -0.1758 0.0317 -0.0264 133 LEU B CA 3847 C C . LEU B 133 ? 1.5381 1.4893 1.4236 -0.1844 0.0185 -0.0300 133 LEU B C 3848 O O . LEU B 133 ? 1.5627 1.5071 1.4569 -0.1880 0.0255 -0.0362 133 LEU B O 3849 C CB . LEU B 133 ? 1.2063 1.1520 1.1053 -0.1603 0.0378 -0.0172 133 LEU B CB 3850 C CG . LEU B 133 ? 1.0733 1.0016 0.9721 -0.1511 0.0574 -0.0177 133 LEU B CG 3851 C CD1 . LEU B 133 ? 1.0639 1.0042 0.9960 -0.1382 0.0582 -0.0108 133 LEU B CD1 3852 C CD2 . LEU B 133 ? 1.0126 0.9320 0.8915 -0.1489 0.0651 -0.0142 133 LEU B CD2 3853 N N . GLU B 134 ? 1.6546 1.6261 1.5465 -0.1880 -0.0006 -0.0249 134 GLU B N 3854 C CA . GLU B 134 ? 1.6924 1.6849 1.6103 -0.1937 -0.0134 -0.0260 134 GLU B CA 3855 C C . GLU B 134 ? 1.6358 1.6543 1.5855 -0.1825 -0.0233 -0.0155 134 GLU B C 3856 O O . GLU B 134 ? 1.7242 1.7636 1.7039 -0.1821 -0.0293 -0.0155 134 GLU B O 3857 C CB . GLU B 134 ? 1.8335 1.8284 1.7349 -0.2094 -0.0301 -0.0318 134 GLU B CB 3858 C CG . GLU B 134 ? 1.9439 1.9120 1.8120 -0.2219 -0.0228 -0.0452 134 GLU B CG 3859 C CD . GLU B 134 ? 1.9900 1.9636 1.8473 -0.2385 -0.0424 -0.0522 134 GLU B CD 3860 O OE1 . GLU B 134 ? 1.9410 1.9415 1.8262 -0.2405 -0.0597 -0.0468 134 GLU B OE1 3861 O OE2 . GLU B 134 ? 2.0586 2.0101 1.8808 -0.2493 -0.0410 -0.0641 134 GLU B OE2 3862 N N . SER B 135 ? 1.4264 1.4430 1.3707 -0.1734 -0.0239 -0.0069 135 SER B N 3863 C CA . SER B 135 ? 1.3630 1.4010 1.3349 -0.1639 -0.0367 0.0028 135 SER B CA 3864 C C . SER B 135 ? 1.1882 1.2287 1.1827 -0.1486 -0.0269 0.0068 135 SER B C 3865 O O . SER B 135 ? 1.0710 1.1280 1.0920 -0.1397 -0.0366 0.0127 135 SER B O 3866 C CB . SER B 135 ? 1.4655 1.5012 1.4181 -0.1660 -0.0491 0.0121 135 SER B CB 3867 O OG . SER B 135 ? 1.5573 1.5950 1.4912 -0.1798 -0.0634 0.0089 135 SER B OG 3868 N N . LEU B 136 ? 1.1265 1.1503 1.1121 -0.1453 -0.0091 0.0031 136 LEU B N 3869 C CA . LEU B 136 ? 1.0210 1.0451 1.0247 -0.1313 -0.0012 0.0068 136 LEU B CA 3870 C C . LEU B 136 ? 0.9760 1.0183 1.0098 -0.1240 -0.0028 0.0042 136 LEU B C 3871 O O . LEU B 136 ? 0.9497 0.9949 0.9850 -0.1292 0.0018 -0.0015 136 LEU B O 3872 C CB . LEU B 136 ? 0.9458 0.9473 0.9327 -0.1299 0.0172 0.0040 136 LEU B CB 3873 C CG . LEU B 136 ? 0.8815 0.8817 0.8862 -0.1164 0.0247 0.0078 136 LEU B CG 3874 C CD1 . LEU B 136 ? 0.8864 0.8724 0.8791 -0.1140 0.0328 0.0129 136 LEU B CD1 3875 C CD2 . LEU B 136 ? 0.7727 0.7662 0.7811 -0.1137 0.0359 0.0028 136 LEU B CD2 3876 N N . GLU B 137 ? 0.9908 1.0445 1.0479 -0.1123 -0.0084 0.0081 137 GLU B N 3877 C CA . GLU B 137 ? 0.9375 1.0085 1.0202 -0.1042 -0.0090 0.0039 137 GLU B CA 3878 C C . GLU B 137 ? 0.8227 0.8892 0.9151 -0.0915 -0.0032 0.0044 137 GLU B C 3879 O O . GLU B 137 ? 0.7736 0.8536 0.8847 -0.0831 -0.0046 0.0003 137 GLU B O 3880 C CB . GLU B 137 ? 1.0965 1.1904 1.2045 -0.1015 -0.0244 0.0042 137 GLU B CB 3881 C CG . GLU B 137 ? 1.2139 1.3107 1.3403 -0.0910 -0.0339 0.0095 137 GLU B CG 3882 C CD . GLU B 137 ? 1.3072 1.4274 1.4659 -0.0850 -0.0469 0.0070 137 GLU B CD 3883 O OE1 . GLU B 137 ? 1.3213 1.4572 1.4874 -0.0904 -0.0489 0.0024 137 GLU B OE1 3884 O OE2 . GLU B 137 ? 1.3166 1.4397 1.4964 -0.0749 -0.0548 0.0093 137 GLU B OE2 3885 N N . TYR B 138 ? 0.7617 0.8100 0.8415 -0.0904 0.0035 0.0088 138 TYR B N 3886 C CA . TYR B 138 ? 0.7353 0.7792 0.8269 -0.0793 0.0073 0.0099 138 TYR B CA 3887 C C . TYR B 138 ? 0.7575 0.7810 0.8321 -0.0808 0.0211 0.0117 138 TYR B C 3888 O O . TYR B 138 ? 0.9037 0.9148 0.9605 -0.0876 0.0259 0.0147 138 TYR B O 3889 C CB . TYR B 138 ? 0.7278 0.7761 0.8380 -0.0729 -0.0029 0.0154 138 TYR B CB 3890 C CG . TYR B 138 ? 0.8113 0.8585 0.9406 -0.0616 -0.0027 0.0150 138 TYR B CG 3891 C CD1 . TYR B 138 ? 0.8078 0.8690 0.9614 -0.0525 -0.0126 0.0097 138 TYR B CD1 3892 C CD2 . TYR B 138 ? 0.8707 0.9034 0.9955 -0.0600 0.0067 0.0190 138 TYR B CD2 3893 C CE1 . TYR B 138 ? 0.7526 0.8123 0.9232 -0.0429 -0.0146 0.0078 138 TYR B CE1 3894 C CE2 . TYR B 138 ? 0.8105 0.8436 0.9559 -0.0505 0.0047 0.0187 138 TYR B CE2 3895 C CZ . TYR B 138 ? 0.7988 0.8448 0.9659 -0.0424 -0.0068 0.0129 138 TYR B CZ 3896 O OH . TYR B 138 ? 0.8541 0.8998 1.0410 -0.0336 -0.0108 0.0110 138 TYR B OH 3897 N N . LEU B 139 ? 0.6465 0.6667 0.7265 -0.0739 0.0273 0.0098 139 LEU B N 3898 C CA . LEU B 139 ? 0.6089 0.6106 0.6790 -0.0734 0.0399 0.0115 139 LEU B CA 3899 C C . LEU B 139 ? 0.6577 0.6598 0.7450 -0.0619 0.0400 0.0126 139 LEU B C 3900 O O . LEU B 139 ? 0.6945 0.7033 0.7857 -0.0575 0.0376 0.0099 139 LEU B O 3901 C CB . LEU B 139 ? 0.6088 0.6001 0.6601 -0.0812 0.0489 0.0079 139 LEU B CB 3902 C CG . LEU B 139 ? 0.6609 0.6319 0.7056 -0.0792 0.0622 0.0088 139 LEU B CG 3903 C CD1 . LEU B 139 ? 0.7250 0.6854 0.7641 -0.0803 0.0688 0.0108 139 LEU B CD1 3904 C CD2 . LEU B 139 ? 0.6548 0.6131 0.6832 -0.0876 0.0700 0.0052 139 LEU B CD2 3905 N N . GLN B 140 ? 0.7451 0.7408 0.8424 -0.0577 0.0428 0.0171 140 GLN B N 3906 C CA . GLN B 140 ? 0.7938 0.7905 0.9114 -0.0472 0.0409 0.0184 140 GLN B CA 3907 C C . GLN B 140 ? 0.8357 0.8166 0.9511 -0.0459 0.0542 0.0213 140 GLN B C 3908 O O . GLN B 140 ? 0.8858 0.8578 0.9965 -0.0498 0.0639 0.0240 140 GLN B O 3909 C CB . GLN B 140 ? 0.8364 0.8413 0.9775 -0.0426 0.0316 0.0214 140 GLN B CB 3910 C CG . GLN B 140 ? 0.8766 0.8881 1.0415 -0.0321 0.0227 0.0195 140 GLN B CG 3911 C CD . GLN B 140 ? 0.9221 0.9409 1.1127 -0.0286 0.0116 0.0210 140 GLN B CD 3912 O OE1 . GLN B 140 ? 0.9238 0.9487 1.1155 -0.0315 0.0049 0.0208 140 GLN B OE1 3913 N NE2 . GLN B 140 ? 0.9765 0.9947 1.1912 -0.0225 0.0088 0.0229 140 GLN B NE2 3914 N N . ALA B 141 ? 0.8736 0.8513 0.9922 -0.0402 0.0550 0.0208 141 ALA B N 3915 C CA . ALA B 141 ? 0.9047 0.8669 1.0246 -0.0378 0.0671 0.0234 141 ALA B CA 3916 C C . ALA B 141 ? 0.9382 0.9032 1.0790 -0.0268 0.0609 0.0264 141 ALA B C 3917 O O . ALA B 141 ? 1.0623 1.0166 1.2019 -0.0237 0.0662 0.0287 141 ALA B O 3918 C CB . ALA B 141 ? 0.9078 0.8565 1.0045 -0.0446 0.0762 0.0210 141 ALA B CB 3919 N N . ASP B 142 ? 0.7979 0.7765 0.9586 -0.0211 0.0483 0.0263 142 ASP B N 3920 C CA . ASP B 142 ? 0.7977 0.7812 0.9773 -0.0112 0.0382 0.0278 142 ASP B CA 3921 C C . ASP B 142 ? 0.8743 0.8508 1.0777 -0.0057 0.0446 0.0331 142 ASP B C 3922 O O . ASP B 142 ? 0.8726 0.8445 1.0840 -0.0087 0.0564 0.0351 142 ASP B O 3923 C CB . ASP B 142 ? 0.8157 0.8148 1.0110 -0.0074 0.0220 0.0237 142 ASP B CB 3924 C CG . ASP B 142 ? 0.9154 0.9181 1.1182 -0.0126 0.0229 0.0236 142 ASP B CG 3925 O OD1 . ASP B 142 ? 0.9563 0.9521 1.1421 -0.0205 0.0342 0.0254 142 ASP B OD1 3926 O OD2 . ASP B 142 ? 0.9872 0.9987 1.2124 -0.0092 0.0114 0.0221 142 ASP B OD2 3927 N N . TYR B 143 ? 0.9671 0.9438 1.1814 0.0025 0.0370 0.0357 143 TYR B N 3928 C CA . TYR B 143 ? 0.9966 0.9709 1.2415 0.0099 0.0386 0.0409 143 TYR B CA 3929 C C . TYR B 143 ? 1.0560 1.0143 1.3005 0.0091 0.0581 0.0440 143 TYR B C 3930 O O . TYR B 143 ? 1.1066 1.0643 1.3803 0.0142 0.0642 0.0474 143 TYR B O 3931 C CB . TYR B 143 ? 0.9237 0.9089 1.2001 0.0107 0.0349 0.0410 143 TYR B CB 3932 C CG . TYR B 143 ? 0.9187 0.9179 1.2034 0.0129 0.0145 0.0364 143 TYR B CG 3933 C CD1 . TYR B 143 ? 0.9159 0.9220 1.2166 0.0211 -0.0028 0.0358 143 TYR B CD1 3934 C CD2 . TYR B 143 ? 0.9218 0.9266 1.1988 0.0072 0.0116 0.0321 143 TYR B CD2 3935 C CE1 . TYR B 143 ? 0.9175 0.9352 1.2245 0.0232 -0.0215 0.0287 143 TYR B CE1 3936 C CE2 . TYR B 143 ? 0.9373 0.9532 1.2242 0.0101 -0.0065 0.0259 143 TYR B CE2 3937 C CZ . TYR B 143 ? 0.9423 0.9642 1.2433 0.0179 -0.0225 0.0232 143 TYR B CZ 3938 O OH . TYR B 143 ? 0.9824 1.0141 1.2917 0.0208 -0.0406 0.0143 143 TYR B OH 3939 N N . ASN B 144 ? 1.0852 1.0308 1.2995 0.0029 0.0678 0.0421 144 ASN B N 3940 C CA . ASN B 144 ? 1.1804 1.1094 1.3902 0.0000 0.0880 0.0412 144 ASN B CA 3941 C C . ASN B 144 ? 1.2524 1.1650 1.4673 0.0058 0.0945 0.0446 144 ASN B C 3942 O O . ASN B 144 ? 1.4667 1.3644 1.6807 0.0044 0.1120 0.0416 144 ASN B O 3943 C CB . ASN B 144 ? 1.2274 1.1499 1.4029 -0.0119 0.0958 0.0353 144 ASN B CB 3944 C CG . ASN B 144 ? 1.2495 1.1718 1.4230 -0.0175 0.1082 0.0324 144 ASN B CG 3945 O OD1 . ASN B 144 ? 1.2613 1.1734 1.4419 -0.0160 0.1243 0.0314 144 ASN B OD1 3946 N ND2 . ASN B 144 ? 1.3125 1.2460 1.4762 -0.0237 0.1011 0.0313 144 ASN B ND2 3947 N N . TYR B 145 ? 1.0959 1.0102 1.3154 0.0124 0.0804 0.0507 145 TYR B N 3948 C CA . TYR B 145 ? 1.0178 0.9157 1.2424 0.0184 0.0831 0.0569 145 TYR B CA 3949 C C . TYR B 145 ? 1.0502 0.9294 1.2438 0.0103 0.0917 0.0558 145 TYR B C 3950 O O . TYR B 145 ? 1.1213 0.9810 1.3205 0.0132 0.1008 0.0584 145 TYR B O 3951 C CB . TYR B 145 ? 0.8869 0.7761 1.1433 0.0257 0.0969 0.0573 145 TYR B CB 3952 C CG . TYR B 145 ? 0.9209 0.8272 1.2171 0.0338 0.0915 0.0596 145 TYR B CG 3953 C CD1 . TYR B 145 ? 1.0893 1.0144 1.3957 0.0370 0.0701 0.0628 145 TYR B CD1 3954 C CD2 . TYR B 145 ? 0.8858 0.7894 1.2109 0.0380 0.1085 0.0579 145 TYR B CD2 3955 C CE1 . TYR B 145 ? 1.1243 1.0648 1.4711 0.0433 0.0642 0.0647 145 TYR B CE1 3956 C CE2 . TYR B 145 ? 0.9857 0.9062 1.3517 0.0445 0.1047 0.0609 145 TYR B CE2 3957 C CZ . TYR B 145 ? 1.0827 1.0214 1.4607 0.0466 0.0817 0.0646 145 TYR B CZ 3958 O OH . TYR B 145 ? 1.1033 1.0588 1.5256 0.0519 0.0768 0.0673 145 TYR B OH 3959 N N . ILE B 146 ? 1.0133 0.8981 1.1780 0.0003 0.0887 0.0519 146 ILE B N 3960 C CA . ILE B 146 ? 1.0462 0.9149 1.1850 -0.0091 0.0965 0.0508 146 ILE B CA 3961 C C . ILE B 146 ? 1.1550 1.0169 1.2877 -0.0062 0.0885 0.0617 146 ILE B C 3962 O O . ILE B 146 ? 1.2411 1.1179 1.3637 -0.0055 0.0755 0.0661 146 ILE B O 3963 C CB . ILE B 146 ? 1.0351 0.9142 1.1490 -0.0211 0.0955 0.0438 146 ILE B CB 3964 C CG1 . ILE B 146 ? 0.9699 0.8537 1.0855 -0.0250 0.1028 0.0351 146 ILE B CG1 3965 C CG2 . ILE B 146 ? 1.1057 0.9693 1.1976 -0.0316 0.1025 0.0430 146 ILE B CG2 3966 C CD1 . ILE B 146 ? 0.9543 0.8492 1.0492 -0.0358 0.0995 0.0293 146 ILE B CD1 3967 N N . SER B 147 ? 1.1926 1.0310 1.3303 -0.0045 0.0968 0.0662 147 SER B N 3968 C CA . SER B 147 ? 1.2422 1.0708 1.3756 -0.0015 0.0897 0.0798 147 SER B CA 3969 C C . SER B 147 ? 1.3151 1.1341 1.4212 -0.0146 0.0946 0.0811 147 SER B C 3970 O O . SER B 147 ? 1.3094 1.1334 1.4010 -0.0162 0.0864 0.0915 147 SER B O 3971 C CB . SER B 147 ? 1.2311 1.0382 1.3900 0.0084 0.0946 0.0861 147 SER B CB 3972 O OG . SER B 147 ? 1.2257 1.0160 1.3911 0.0053 0.1126 0.0744 147 SER B OG 3973 N N . THR B 148 ? 1.3804 1.1862 1.4792 -0.0246 0.1081 0.0703 148 THR B N 3974 C CA . THR B 148 ? 1.4190 1.2147 1.4972 -0.0384 0.1129 0.0706 148 THR B CA 3975 C C . THR B 148 ? 1.3307 1.1313 1.3951 -0.0510 0.1197 0.0554 148 THR B C 3976 O O . THR B 148 ? 1.3305 1.1168 1.3974 -0.0533 0.1300 0.0444 148 THR B O 3977 C CB . THR B 148 ? 1.4930 1.2556 1.5779 -0.0392 0.1215 0.0759 148 THR B CB 3978 O OG1 . THR B 148 ? 1.4156 1.1621 1.5166 -0.0341 0.1324 0.0649 148 THR B OG1 3979 C CG2 . THR B 148 ? 1.5498 1.3067 1.6438 -0.0291 0.1124 0.0951 148 THR B CG2 3980 N N . ILE B 149 ? 1.3277 1.1492 1.3773 -0.0588 0.1136 0.0547 149 ILE B N 3981 C CA . ILE B 149 ? 1.2478 1.0738 1.2845 -0.0722 0.1175 0.0428 149 ILE B CA 3982 C C . ILE B 149 ? 1.3031 1.1085 1.3319 -0.0848 0.1244 0.0436 149 ILE B C 3983 O O . ILE B 149 ? 1.3287 1.1255 1.3586 -0.0845 0.1239 0.0562 149 ILE B O 3984 C CB . ILE B 149 ? 1.0419 0.8988 1.0713 -0.0753 0.1082 0.0416 149 ILE B CB 3985 C CG1 . ILE B 149 ? 0.9947 0.8699 1.0345 -0.0633 0.1002 0.0405 149 ILE B CG1 3986 C CG2 . ILE B 149 ? 0.8994 0.7618 0.9187 -0.0887 0.1100 0.0306 149 ILE B CG2 3987 C CD1 . ILE B 149 ? 0.9368 0.8402 0.9726 -0.0650 0.0911 0.0374 149 ILE B CD1 3988 N N . GLU B 150 ? 1.2717 1.0679 1.2925 -0.0962 0.1302 0.0308 150 GLU B N 3989 C CA . GLU B 150 ? 1.2151 0.9941 1.2297 -0.1108 0.1348 0.0295 150 GLU B CA 3990 C C . GLU B 150 ? 1.1769 0.9803 1.1835 -0.1230 0.1288 0.0287 150 GLU B C 3991 O O . GLU B 150 ? 1.1572 0.9859 1.1612 -0.1210 0.1223 0.0242 150 GLU B O 3992 C CB . GLU B 150 ? 1.2108 0.9641 1.2212 -0.1168 0.1436 0.0141 150 GLU B CB 3993 C CG . GLU B 150 ? 1.3271 1.0558 1.3495 -0.1042 0.1520 0.0136 150 GLU B CG 3994 C CD . GLU B 150 ? 1.4624 1.1662 1.4782 -0.1094 0.1627 -0.0044 150 GLU B CD 3995 O OE1 . GLU B 150 ? 1.5281 1.2373 1.5266 -0.1214 0.1615 -0.0171 150 GLU B OE1 3996 O OE2 . GLU B 150 ? 1.4745 1.1532 1.5024 -0.1010 0.1719 -0.0064 150 GLU B OE2 3997 N N . ALA B 151 ? 1.2111 1.0070 1.2171 -0.1354 0.1311 0.0335 151 ALA B N 3998 C CA . ALA B 151 ? 1.1666 0.9881 1.1706 -0.1464 0.1269 0.0353 151 ALA B CA 3999 C C . ALA B 151 ? 1.1398 0.9765 1.1395 -0.1550 0.1218 0.0205 151 ALA B C 4000 O O . ALA B 151 ? 1.0929 0.9594 1.0937 -0.1527 0.1150 0.0198 151 ALA B O 4001 C CB . ALA B 151 ? 1.1476 0.9550 1.1551 -0.1600 0.1322 0.0434 151 ALA B CB 4002 N N . GLY B 152 ? 1.1805 0.9959 1.1749 -0.1645 0.1245 0.0083 152 GLY B N 4003 C CA . GLY B 152 ? 1.2026 1.0301 1.1901 -0.1747 0.1179 -0.0048 152 GLY B CA 4004 C C . GLY B 152 ? 1.2278 1.0646 1.2068 -0.1653 0.1140 -0.0120 152 GLY B C 4005 O O . GLY B 152 ? 1.2571 1.0974 1.2259 -0.1733 0.1088 -0.0229 152 GLY B O 4006 N N . ALA B 153 ? 1.1058 0.9470 1.0893 -0.1491 0.1156 -0.0051 153 ALA B N 4007 C CA . ALA B 153 ? 0.9793 0.8272 0.9582 -0.1399 0.1136 -0.0098 153 ALA B CA 4008 C C . ALA B 153 ? 0.9547 0.8305 0.9317 -0.1435 0.1024 -0.0124 153 ALA B C 4009 O O . ALA B 153 ? 0.9429 0.8180 0.9083 -0.1467 0.0999 -0.0202 153 ALA B O 4010 C CB . ALA B 153 ? 0.8699 0.7209 0.8600 -0.1229 0.1153 -0.0006 153 ALA B CB 4011 N N . PHE B 154 ? 0.9535 0.8538 0.9417 -0.1425 0.0959 -0.0058 154 PHE B N 4012 C CA . PHE B 154 ? 0.9674 0.8954 0.9599 -0.1431 0.0848 -0.0075 154 PHE B CA 4013 C C . PHE B 154 ? 1.0826 1.0206 1.0758 -0.1586 0.0790 -0.0122 154 PHE B C 4014 O O . PHE B 154 ? 1.0254 0.9882 1.0268 -0.1598 0.0690 -0.0130 154 PHE B O 4015 C CB . PHE B 154 ? 0.8837 0.8343 0.8901 -0.1316 0.0810 -0.0002 154 PHE B CB 4016 C CG . PHE B 154 ? 0.9214 0.8634 0.9303 -0.1171 0.0845 0.0048 154 PHE B CG 4017 C CD1 . PHE B 154 ? 0.8815 0.8189 0.8896 -0.1101 0.0835 0.0026 154 PHE B CD1 4018 C CD2 . PHE B 154 ? 0.9987 0.9377 1.0111 -0.1110 0.0884 0.0126 154 PHE B CD2 4019 C CE1 . PHE B 154 ? 0.8627 0.7941 0.8781 -0.0973 0.0861 0.0071 154 PHE B CE1 4020 C CE2 . PHE B 154 ? 0.9949 0.9271 1.0118 -0.0978 0.0891 0.0173 154 PHE B CE2 4021 C CZ . PHE B 154 ? 0.9217 0.8508 0.9424 -0.0910 0.0879 0.0140 154 PHE B CZ 4022 N N . SER B 155 ? 1.1917 1.1104 1.1796 -0.1705 0.0846 -0.0154 155 SER B N 4023 C CA . SER B 155 ? 1.1833 1.1088 1.1731 -0.1871 0.0781 -0.0214 155 SER B CA 4024 C C . SER B 155 ? 1.3538 1.2796 1.3293 -0.1912 0.0687 -0.0306 155 SER B C 4025 O O . SER B 155 ? 1.4351 1.3463 1.3951 -0.1841 0.0721 -0.0333 155 SER B O 4026 C CB . SER B 155 ? 1.1561 1.0561 1.1438 -0.1994 0.0859 -0.0238 155 SER B CB 4027 O OG . SER B 155 ? 1.1657 1.0630 1.1638 -0.1951 0.0947 -0.0124 155 SER B OG 4028 N N . LYS B 156 ? 1.3918 1.3356 1.3731 -0.2027 0.0568 -0.0343 156 LYS B N 4029 C CA . LYS B 156 ? 1.3683 1.3148 1.3346 -0.2081 0.0446 -0.0413 156 LYS B CA 4030 C C . LYS B 156 ? 1.2830 1.2438 1.2484 -0.1943 0.0392 -0.0357 156 LYS B C 4031 O O . LYS B 156 ? 1.2986 1.2543 1.2449 -0.1954 0.0332 -0.0388 156 LYS B O 4032 C CB . LYS B 156 ? 1.4081 1.3217 1.3463 -0.2154 0.0498 -0.0523 156 LYS B CB 4033 C CG . LYS B 156 ? 1.4781 1.3726 1.4188 -0.2291 0.0549 -0.0588 156 LYS B CG 4034 C CD . LYS B 156 ? 1.5654 1.4273 1.4777 -0.2363 0.0588 -0.0731 156 LYS B CD 4035 C CE . LYS B 156 ? 1.7112 1.5550 1.6287 -0.2526 0.0598 -0.0814 156 LYS B CE 4036 N NZ . LYS B 156 ? 1.8405 1.6560 1.7286 -0.2623 0.0591 -0.0995 156 LYS B NZ 4037 N N . LEU B 157 ? 1.2173 1.1955 1.2027 -0.1821 0.0413 -0.0275 157 LEU B N 4038 C CA . LEU B 157 ? 1.0950 1.0889 1.0867 -0.1696 0.0345 -0.0222 157 LEU B CA 4039 C C . LEU B 157 ? 0.9977 1.0234 1.0171 -0.1665 0.0260 -0.0188 157 LEU B C 4040 O O . LEU B 157 ? 0.9747 1.0118 1.0080 -0.1537 0.0280 -0.0145 157 LEU B O 4041 C CB . LEU B 157 ? 1.0644 1.0468 1.0546 -0.1552 0.0452 -0.0177 157 LEU B CB 4042 C CG . LEU B 157 ? 1.0322 0.9852 1.0009 -0.1545 0.0564 -0.0208 157 LEU B CG 4043 C CD1 . LEU B 157 ? 0.8749 0.8235 0.8517 -0.1393 0.0644 -0.0149 157 LEU B CD1 4044 C CD2 . LEU B 157 ? 1.1258 1.0727 1.0733 -0.1600 0.0511 -0.0245 157 LEU B CD2 4045 N N . ASN B 158 ? 1.0926 1.1330 1.1213 -0.1782 0.0164 -0.0219 158 ASN B N 4046 C CA . ASN B 158 ? 1.0908 1.1632 1.1500 -0.1766 0.0103 -0.0201 158 ASN B CA 4047 C C . ASN B 158 ? 1.0325 1.1230 1.1073 -0.1615 0.0035 -0.0164 158 ASN B C 4048 O O . ASN B 158 ? 1.1001 1.2094 1.1957 -0.1532 0.0070 -0.0155 158 ASN B O 4049 C CB . ASN B 158 ? 1.2773 1.3637 1.3460 -0.1911 -0.0031 -0.0238 158 ASN B CB 4050 C CG . ASN B 158 ? 1.4477 1.5246 1.5149 -0.2069 0.0033 -0.0279 158 ASN B CG 4051 O OD1 . ASN B 158 ? 1.4618 1.5291 1.5289 -0.2062 0.0183 -0.0259 158 ASN B OD1 4052 N ND2 . ASN B 158 ? 1.5230 1.6024 1.5898 -0.2217 -0.0093 -0.0331 158 ASN B ND2 4053 N N . LYS B 159 ? 0.9731 1.0572 1.0371 -0.1582 -0.0060 -0.0144 159 LYS B N 4054 C CA . LYS B 159 ? 0.9717 1.0715 1.0536 -0.1455 -0.0152 -0.0104 159 LYS B CA 4055 C C . LYS B 159 ? 0.8517 0.9468 0.9373 -0.1308 -0.0056 -0.0087 159 LYS B C 4056 O O . LYS B 159 ? 0.8093 0.9189 0.9151 -0.1196 -0.0118 -0.0076 159 LYS B O 4057 C CB . LYS B 159 ? 1.0613 1.1534 1.1287 -0.1475 -0.0277 -0.0062 159 LYS B CB 4058 C CG . LYS B 159 ? 1.1776 1.2773 1.2420 -0.1612 -0.0421 -0.0076 159 LYS B CG 4059 C CD . LYS B 159 ? 1.2502 1.3817 1.3524 -0.1602 -0.0528 -0.0083 159 LYS B CD 4060 C CE . LYS B 159 ? 1.3453 1.4866 1.4488 -0.1733 -0.0707 -0.0086 159 LYS B CE 4061 N NZ . LYS B 159 ? 1.3264 1.5014 1.4731 -0.1711 -0.0814 -0.0088 159 LYS B NZ 4062 N N . LEU B 160 ? 0.7830 0.8579 0.8511 -0.1307 0.0082 -0.0090 160 LEU B N 4063 C CA . LEU B 160 ? 0.7400 0.8094 0.8107 -0.1173 0.0153 -0.0070 160 LEU B CA 4064 C C . LEU B 160 ? 0.7415 0.8327 0.8340 -0.1085 0.0154 -0.0092 160 LEU B C 4065 O O . LEU B 160 ? 0.7094 0.8106 0.8062 -0.1133 0.0213 -0.0111 160 LEU B O 4066 C CB . LEU B 160 ? 0.6876 0.7331 0.7394 -0.1190 0.0292 -0.0064 160 LEU B CB 4067 C CG . LEU B 160 ? 0.6514 0.6914 0.7069 -0.1056 0.0347 -0.0037 160 LEU B CG 4068 C CD1 . LEU B 160 ? 0.6461 0.6607 0.6861 -0.1047 0.0428 -0.0016 160 LEU B CD1 4069 C CD2 . LEU B 160 ? 0.6794 0.7257 0.7388 -0.1030 0.0415 -0.0036 160 LEU B CD2 4070 N N . LYS B 161 ? 0.8440 0.9421 0.9500 -0.0959 0.0096 -0.0091 161 LYS B N 4071 C CA . LYS B 161 ? 0.8449 0.9628 0.9695 -0.0860 0.0095 -0.0138 161 LYS B CA 4072 C C . LYS B 161 ? 0.8410 0.9504 0.9633 -0.0740 0.0124 -0.0141 161 LYS B C 4073 O O . LYS B 161 ? 0.9212 1.0428 1.0502 -0.0663 0.0146 -0.0189 161 LYS B O 4074 C CB . LYS B 161 ? 0.8351 0.9735 0.9857 -0.0814 -0.0034 -0.0168 161 LYS B CB 4075 C CG . LYS B 161 ? 0.9270 1.0810 1.0873 -0.0918 -0.0079 -0.0175 161 LYS B CG 4076 C CD . LYS B 161 ? 1.1010 1.2658 1.2607 -0.0980 0.0041 -0.0206 161 LYS B CD 4077 C CE . LYS B 161 ? 1.1754 1.3570 1.3492 -0.1098 -0.0005 -0.0213 161 LYS B CE 4078 N NZ . LYS B 161 ? 1.2296 1.4391 1.4374 -0.1024 -0.0099 -0.0257 161 LYS B NZ 4079 N N . VAL B 162 ? 0.7125 0.8022 0.8255 -0.0727 0.0124 -0.0093 162 VAL B N 4080 C CA . VAL B 162 ? 0.6227 0.7049 0.7374 -0.0620 0.0133 -0.0091 162 VAL B CA 4081 C C . VAL B 162 ? 0.6549 0.7148 0.7519 -0.0647 0.0229 -0.0038 162 VAL B C 4082 O O . VAL B 162 ? 0.7607 0.8065 0.8482 -0.0711 0.0257 -0.0001 162 VAL B O 4083 C CB . VAL B 162 ? 0.5358 0.6186 0.6681 -0.0544 0.0026 -0.0084 162 VAL B CB 4084 C CG1 . VAL B 162 ? 0.5284 0.6003 0.6631 -0.0460 0.0036 -0.0071 162 VAL B CG1 4085 C CG2 . VAL B 162 ? 0.4421 0.5454 0.5966 -0.0480 -0.0070 -0.0154 162 VAL B CG2 4086 N N . LEU B 163 ? 0.6019 0.6589 0.6942 -0.0594 0.0278 -0.0036 163 LEU B N 4087 C CA . LEU B 163 ? 0.6043 0.6409 0.6847 -0.0598 0.0361 0.0017 163 LEU B CA 4088 C C . LEU B 163 ? 0.6399 0.6753 0.7284 -0.0478 0.0322 0.0025 163 LEU B C 4089 O O . LEU B 163 ? 0.6362 0.6820 0.7241 -0.0421 0.0293 0.0000 163 LEU B O 4090 C CB . LEU B 163 ? 0.6118 0.6429 0.6769 -0.0675 0.0455 0.0039 163 LEU B CB 4091 C CG . LEU B 163 ? 0.6751 0.6827 0.7295 -0.0687 0.0546 0.0095 163 LEU B CG 4092 C CD1 . LEU B 163 ? 0.6953 0.6872 0.7472 -0.0727 0.0580 0.0092 163 LEU B CD1 4093 C CD2 . LEU B 163 ? 0.7177 0.7196 0.7599 -0.0776 0.0628 0.0123 163 LEU B CD2 4094 N N . ILE B 164 ? 0.6114 0.6350 0.7073 -0.0444 0.0321 0.0059 164 ILE B N 4095 C CA . ILE B 164 ? 0.5694 0.5927 0.6784 -0.0336 0.0264 0.0067 164 ILE B CA 4096 C C . ILE B 164 ? 0.7005 0.7061 0.8071 -0.0322 0.0343 0.0131 164 ILE B C 4097 O O . ILE B 164 ? 0.7294 0.7232 0.8376 -0.0356 0.0417 0.0159 164 ILE B O 4098 C CB . ILE B 164 ? 0.4847 0.5134 0.6153 -0.0293 0.0175 0.0051 164 ILE B CB 4099 C CG1 . ILE B 164 ? 0.4146 0.4604 0.5525 -0.0282 0.0081 -0.0020 164 ILE B CG1 4100 C CG2 . ILE B 164 ? 0.5579 0.5853 0.7054 -0.0196 0.0110 0.0058 164 ILE B CG2 4101 C CD1 . ILE B 164 ? 0.3860 0.4359 0.5484 -0.0231 -0.0025 -0.0033 164 ILE B CD1 4102 N N . LEU B 165 ? 0.8019 0.8058 0.9046 -0.0267 0.0328 0.0156 165 LEU B N 4103 C CA . LEU B 165 ? 0.8483 0.8351 0.9503 -0.0247 0.0397 0.0227 165 LEU B CA 4104 C C . LEU B 165 ? 0.8769 0.8658 0.9907 -0.0137 0.0301 0.0258 165 LEU B C 4105 O O . LEU B 165 ? 0.9208 0.8983 1.0323 -0.0106 0.0328 0.0328 165 LEU B O 4106 C CB . LEU B 165 ? 0.7738 0.7507 0.8549 -0.0317 0.0488 0.0263 165 LEU B CB 4107 C CG . LEU B 165 ? 0.7031 0.6778 0.7717 -0.0441 0.0568 0.0227 165 LEU B CG 4108 C CD1 . LEU B 165 ? 0.7450 0.7141 0.7973 -0.0509 0.0630 0.0264 165 LEU B CD1 4109 C CD2 . LEU B 165 ? 0.7781 0.7369 0.8483 -0.0481 0.0656 0.0220 165 LEU B CD2 4110 N N . ASN B 166 ? 0.8471 0.8500 0.9749 -0.0076 0.0174 0.0206 166 ASN B N 4111 C CA . ASN B 166 ? 0.8090 0.8162 0.9455 0.0021 0.0049 0.0215 166 ASN B CA 4112 C C . ASN B 166 ? 0.8295 0.8267 0.9885 0.0075 0.0050 0.0283 166 ASN B C 4113 O O . ASN B 166 ? 0.8166 0.8063 0.9886 0.0044 0.0151 0.0302 166 ASN B O 4114 C CB . ASN B 166 ? 0.8029 0.8262 0.9507 0.0068 -0.0095 0.0116 166 ASN B CB 4115 C CG . ASN B 166 ? 0.8932 0.9182 1.0640 0.0046 -0.0096 0.0087 166 ASN B CG 4116 O OD1 . ASN B 166 ? 0.9254 0.9564 1.0927 -0.0001 -0.0080 0.0039 166 ASN B OD1 4117 N ND2 . ASN B 166 ? 0.9120 0.9328 1.1084 0.0080 -0.0118 0.0127 166 ASN B ND2 4118 N N . ASP B 167 ? 0.9085 0.9069 1.0717 0.0155 -0.0061 0.0319 167 ASP B N 4119 C CA . ASP B 167 ? 0.9444 0.9372 1.1350 0.0222 -0.0093 0.0383 167 ASP B CA 4120 C C . ASP B 167 ? 1.0164 0.9918 1.2098 0.0199 0.0079 0.0459 167 ASP B C 4121 O O . ASP B 167 ? 1.1372 1.1089 1.3569 0.0217 0.0145 0.0475 167 ASP B O 4122 C CB . ASP B 167 ? 0.9450 0.9469 1.1682 0.0243 -0.0157 0.0334 167 ASP B CB 4123 C CG . ASP B 167 ? 0.9980 1.0144 1.2193 0.0254 -0.0309 0.0230 167 ASP B CG 4124 O OD1 . ASP B 167 ? 0.9974 1.0197 1.2050 0.0303 -0.0441 0.0202 167 ASP B OD1 4125 O OD2 . ASP B 167 ? 1.1282 1.1493 1.3603 0.0217 -0.0296 0.0177 167 ASP B OD2 4126 N N . ASN B 168 ? 0.9691 0.9337 1.1362 0.0157 0.0159 0.0501 168 ASN B N 4127 C CA . ASN B 168 ? 0.8936 0.8387 1.0618 0.0139 0.0312 0.0559 168 ASN B CA 4128 C C . ASN B 168 ? 0.8640 0.7983 1.0262 0.0191 0.0269 0.0668 168 ASN B C 4129 O O . ASN B 168 ? 0.8725 0.8151 1.0383 0.0267 0.0108 0.0713 168 ASN B O 4130 C CB . ASN B 168 ? 0.8537 0.7909 0.9990 0.0022 0.0460 0.0513 168 ASN B CB 4131 C CG . ASN B 168 ? 0.8636 0.8039 1.0173 -0.0026 0.0540 0.0440 168 ASN B CG 4132 O OD1 . ASN B 168 ? 0.9295 0.8584 1.0938 -0.0029 0.0666 0.0439 168 ASN B OD1 4133 N ND2 . ASN B 168 ? 0.8498 0.8054 0.9985 -0.0061 0.0472 0.0380 168 ASN B ND2 4134 N N . LEU B 169 ? 0.7763 0.6913 0.9288 0.0148 0.0405 0.0712 169 LEU B N 4135 C CA . LEU B 169 ? 0.8852 0.7855 1.0369 0.0199 0.0379 0.0839 169 LEU B CA 4136 C C . LEU B 169 ? 1.0474 0.9382 1.1670 0.0111 0.0431 0.0891 169 LEU B C 4137 O O . LEU B 169 ? 1.1078 0.9793 1.2259 0.0117 0.0473 0.0995 169 LEU B O 4138 C CB . LEU B 169 ? 0.9122 0.7939 1.0902 0.0246 0.0497 0.0861 169 LEU B CB 4139 C CG . LEU B 169 ? 0.8374 0.7240 1.0545 0.0372 0.0426 0.0894 169 LEU B CG 4140 C CD1 . LEU B 169 ? 0.7124 0.6223 0.9444 0.0389 0.0332 0.0819 169 LEU B CD1 4141 C CD2 . LEU B 169 ? 0.9081 0.7775 1.1489 0.0397 0.0611 0.0871 169 LEU B CD2 4142 N N . LEU B 170 ? 1.0630 0.9678 1.1605 0.0029 0.0430 0.0824 170 LEU B N 4143 C CA . LEU B 170 ? 1.0144 0.9137 1.0851 -0.0072 0.0499 0.0865 170 LEU B CA 4144 C C . LEU B 170 ? 1.0540 0.9522 1.1091 -0.0035 0.0411 0.1011 170 LEU B C 4145 O O . LEU B 170 ? 0.9926 0.9092 1.0360 0.0005 0.0292 0.1009 170 LEU B O 4146 C CB . LEU B 170 ? 0.9379 0.8563 0.9939 -0.0157 0.0514 0.0755 170 LEU B CB 4147 C CG . LEU B 170 ? 0.9489 0.8591 0.9985 -0.0286 0.0654 0.0691 170 LEU B CG 4148 C CD1 . LEU B 170 ? 1.1043 0.9903 1.1478 -0.0342 0.0748 0.0786 170 LEU B CD1 4149 C CD2 . LEU B 170 ? 0.8646 0.7716 0.9298 -0.0289 0.0705 0.0589 170 LEU B CD2 4150 N N . LEU B 171 ? 1.2417 1.1172 1.2957 -0.0048 0.0469 0.1137 171 LEU B N 4151 C CA . LEU B 171 ? 1.2613 1.1329 1.2971 -0.0031 0.0400 0.1310 171 LEU B CA 4152 C C . LEU B 171 ? 1.1493 1.0253 1.1571 -0.0162 0.0489 0.1333 171 LEU B C 4153 O O . LEU B 171 ? 1.1562 1.0457 1.1405 -0.0162 0.0431 0.1403 171 LEU B O 4154 C CB . LEU B 171 ? 1.4511 1.2948 1.5016 0.0018 0.0413 0.1459 171 LEU B CB 4155 C CG . LEU B 171 ? 1.6175 1.4389 1.6929 0.0005 0.0550 0.1390 171 LEU B CG 4156 C CD1 . LEU B 171 ? 1.6365 1.4466 1.6992 -0.0149 0.0714 0.1325 171 LEU B CD1 4157 C CD2 . LEU B 171 ? 1.6656 1.4631 1.7612 0.0101 0.0521 0.1538 171 LEU B CD2 4158 N N . SER B 172 ? 1.0332 0.8988 1.0441 -0.0275 0.0634 0.1267 172 SER B N 4159 C CA . SER B 172 ? 1.0106 0.8794 1.0023 -0.0415 0.0732 0.1290 172 SER B CA 4160 C C . SER B 172 ? 1.0295 0.8998 1.0283 -0.0522 0.0834 0.1127 172 SER B C 4161 O O . SER B 172 ? 1.1161 0.9742 1.1314 -0.0505 0.0865 0.1036 172 SER B O 4162 C CB . SER B 172 ? 1.0420 0.8857 1.0283 -0.0466 0.0788 0.1479 172 SER B CB 4163 O OG . SER B 172 ? 1.0008 0.8164 1.0070 -0.0484 0.0864 0.1455 172 SER B OG 4164 N N . LEU B 173 ? 1.0080 0.8939 0.9940 -0.0633 0.0887 0.1095 173 LEU B N 4165 C CA . LEU B 173 ? 0.9795 0.8720 0.9710 -0.0735 0.0950 0.0944 173 LEU B CA 4166 C C . LEU B 173 ? 1.1294 1.0096 1.1173 -0.0896 0.1059 0.0987 173 LEU B C 4167 O O . LEU B 173 ? 1.2225 1.1136 1.1994 -0.0963 0.1095 0.1075 173 LEU B O 4168 C CB . LEU B 173 ? 0.8212 0.7464 0.8081 -0.0720 0.0898 0.0844 173 LEU B CB 4169 C CG . LEU B 173 ? 0.6828 0.6207 0.6788 -0.0771 0.0901 0.0682 173 LEU B CG 4170 C CD1 . LEU B 173 ? 0.8347 0.7516 0.8414 -0.0778 0.0927 0.0621 173 LEU B CD1 4171 C CD2 . LEU B 173 ? 0.5700 0.5324 0.5689 -0.0669 0.0801 0.0598 173 LEU B CD2 4172 N N . PRO B 174 ? 1.2020 1.0594 1.1996 -0.0962 0.1119 0.0921 174 PRO B N 4173 C CA . PRO B 174 ? 1.1857 1.0278 1.1834 -0.1124 0.1209 0.0942 174 PRO B CA 4174 C C . PRO B 174 ? 1.1013 0.9694 1.0947 -0.1248 0.1231 0.0906 174 PRO B C 4175 O O . PRO B 174 ? 0.9991 0.8891 0.9945 -0.1243 0.1190 0.0776 174 PRO B O 4176 C CB . PRO B 174 ? 1.2440 1.0655 1.2504 -0.1156 0.1242 0.0795 174 PRO B CB 4177 C CG . PRO B 174 ? 1.2299 1.0654 1.2392 -0.1035 0.1180 0.0691 174 PRO B CG 4178 C CD . PRO B 174 ? 1.2816 1.1277 1.2903 -0.0893 0.1108 0.0805 174 PRO B CD 4179 N N . SER B 175 ? 1.2114 1.0776 1.2014 -0.1356 0.1297 0.1032 175 SER B N 4180 C CA . SER B 175 ? 1.2566 1.1506 1.2463 -0.1469 0.1336 0.1018 175 SER B CA 4181 C C . SER B 175 ? 1.1312 1.0292 1.1325 -0.1592 0.1334 0.0853 175 SER B C 4182 O O . SER B 175 ? 1.0027 0.8750 1.0089 -0.1641 0.1337 0.0783 175 SER B O 4183 C CB . SER B 175 ? 1.3449 1.2332 1.3307 -0.1577 0.1428 0.1205 175 SER B CB 4184 O OG . SER B 175 ? 1.4088 1.2654 1.4046 -0.1699 0.1477 0.1231 175 SER B OG 4185 N N . ASN B 176 ? 1.1297 1.0605 1.1353 -0.1635 0.1325 0.0789 176 ASN B N 4186 C CA . ASN B 176 ? 1.0930 1.0340 1.1105 -0.1743 0.1293 0.0642 176 ASN B CA 4187 C C . ASN B 176 ? 1.1163 1.0504 1.1323 -0.1666 0.1205 0.0498 176 ASN B C 4188 O O . ASN B 176 ? 1.1415 1.0697 1.1617 -0.1763 0.1175 0.0388 176 ASN B O 4189 C CB . ASN B 176 ? 1.0585 0.9802 1.0844 -0.1933 0.1348 0.0658 176 ASN B CB 4190 C CG . ASN B 176 ? 1.1363 1.0773 1.1712 -0.2059 0.1431 0.0763 176 ASN B CG 4191 O OD1 . ASN B 176 ? 1.1359 1.0994 1.1857 -0.2170 0.1421 0.0692 176 ASN B OD1 4192 N ND2 . ASN B 176 ? 1.2157 1.1491 1.2426 -0.2042 0.1514 0.0944 176 ASN B ND2 4193 N N . VAL B 177 ? 1.0469 0.9824 1.0566 -0.1499 0.1162 0.0502 177 VAL B N 4194 C CA . VAL B 177 ? 0.9185 0.8531 0.9285 -0.1426 0.1089 0.0382 177 VAL B CA 4195 C C . VAL B 177 ? 0.9197 0.8849 0.9371 -0.1445 0.1019 0.0293 177 VAL B C 4196 O O . VAL B 177 ? 0.9518 0.9166 0.9708 -0.1491 0.0966 0.0194 177 VAL B O 4197 C CB . VAL B 177 ? 0.8226 0.7536 0.8294 -0.1248 0.1055 0.0415 177 VAL B CB 4198 C CG1 . VAL B 177 ? 0.9786 0.8762 0.9835 -0.1216 0.1099 0.0444 177 VAL B CG1 4199 C CG2 . VAL B 177 ? 0.7516 0.6992 0.7546 -0.1169 0.1049 0.0514 177 VAL B CG2 4200 N N . PHE B 178 ? 0.9163 0.9081 0.9377 -0.1407 0.1019 0.0330 178 PHE B N 4201 C CA . PHE B 178 ? 0.9255 0.9479 0.9580 -0.1389 0.0951 0.0247 178 PHE B CA 4202 C C . PHE B 178 ? 1.0393 1.0804 1.0846 -0.1533 0.0979 0.0233 178 PHE B C 4203 O O . PHE B 178 ? 1.1452 1.2154 1.2039 -0.1513 0.0941 0.0181 178 PHE B O 4204 C CB . PHE B 178 ? 0.8345 0.8766 0.8661 -0.1245 0.0934 0.0261 178 PHE B CB 4205 C CG . PHE B 178 ? 0.8129 0.8404 0.8363 -0.1103 0.0889 0.0277 178 PHE B CG 4206 C CD1 . PHE B 178 ? 0.9367 0.9469 0.9610 -0.1079 0.0842 0.0234 178 PHE B CD1 4207 C CD2 . PHE B 178 ? 0.8188 0.8510 0.8338 -0.0999 0.0893 0.0334 178 PHE B CD2 4208 C CE1 . PHE B 178 ? 1.0110 1.0103 1.0331 -0.0954 0.0807 0.0253 178 PHE B CE1 4209 C CE2 . PHE B 178 ? 0.8721 0.8927 0.8836 -0.0874 0.0833 0.0348 178 PHE B CE2 4210 C CZ . PHE B 178 ? 0.9899 0.9945 1.0075 -0.0852 0.0793 0.0309 178 PHE B CZ 4211 N N . ARG B 179 ? 1.0264 1.0514 1.0712 -0.1676 0.1044 0.0278 179 ARG B N 4212 C CA . ARG B 179 ? 1.0858 1.1298 1.1467 -0.1824 0.1081 0.0282 179 ARG B CA 4213 C C . ARG B 179 ? 1.0565 1.1136 1.1315 -0.1900 0.0971 0.0166 179 ARG B C 4214 O O . ARG B 179 ? 1.0685 1.1527 1.1637 -0.1977 0.0966 0.0149 179 ARG B O 4215 C CB . ARG B 179 ? 1.3317 1.3526 1.3906 -0.1967 0.1174 0.0369 179 ARG B CB 4216 C CG . ARG B 179 ? 1.6198 1.6066 1.6718 -0.2036 0.1137 0.0311 179 ARG B CG 4217 C CD . ARG B 179 ? 1.8032 1.7930 1.8698 -0.2230 0.1105 0.0245 179 ARG B CD 4218 N NE . ARG B 179 ? 1.9383 1.8909 1.9970 -0.2324 0.1106 0.0200 179 ARG B NE 4219 C CZ . ARG B 179 ? 2.0457 1.9794 2.1107 -0.2463 0.1179 0.0260 179 ARG B CZ 4220 N NH1 . ARG B 179 ? 2.0930 2.0431 2.1717 -0.2532 0.1265 0.0387 179 ARG B NH1 4221 N NH2 . ARG B 179 ? 2.0710 1.9690 2.1291 -0.2536 0.1174 0.0189 179 ARG B NH2 4222 N N . PHE B 180 ? 0.9931 1.0322 1.0580 -0.1876 0.0882 0.0093 180 PHE B N 4223 C CA . PHE B 180 ? 0.9931 1.0402 1.0658 -0.1960 0.0762 -0.0003 180 PHE B CA 4224 C C . PHE B 180 ? 0.9641 1.0315 1.0420 -0.1838 0.0650 -0.0050 180 PHE B C 4225 O O . PHE B 180 ? 0.9740 1.0546 1.0616 -0.1893 0.0532 -0.0107 180 PHE B O 4226 C CB . PHE B 180 ? 1.0058 1.0194 1.0609 -0.2039 0.0739 -0.0060 180 PHE B CB 4227 C CG . PHE B 180 ? 1.0025 1.0029 1.0623 -0.2224 0.0778 -0.0067 180 PHE B CG 4228 C CD1 . PHE B 180 ? 0.9176 0.9426 1.0009 -0.2343 0.0776 -0.0045 180 PHE B CD1 4229 C CD2 . PHE B 180 ? 1.1593 1.1230 1.2034 -0.2281 0.0820 -0.0100 180 PHE B CD2 4230 C CE1 . PHE B 180 ? 0.9977 1.0106 1.0891 -0.2527 0.0807 -0.0048 180 PHE B CE1 4231 C CE2 . PHE B 180 ? 1.2044 1.1536 1.2551 -0.2458 0.0847 -0.0116 180 PHE B CE2 4232 C CZ . PHE B 180 ? 1.1439 1.1177 1.2186 -0.2587 0.0836 -0.0085 180 PHE B CZ 4233 N N . VAL B 181 ? 0.9288 0.9979 1.0015 -0.1676 0.0674 -0.0020 181 VAL B N 4234 C CA . VAL B 181 ? 0.9043 0.9923 0.9860 -0.1555 0.0574 -0.0058 181 VAL B CA 4235 C C . VAL B 181 ? 1.0454 1.1608 1.1421 -0.1464 0.0615 -0.0048 181 VAL B C 4236 O O . VAL B 181 ? 1.1231 1.2392 1.2157 -0.1470 0.0732 0.0005 181 VAL B O 4237 C CB . VAL B 181 ? 0.7721 0.8405 0.8385 -0.1435 0.0550 -0.0055 181 VAL B CB 4238 C CG1 . VAL B 181 ? 0.8866 0.9269 0.9351 -0.1516 0.0548 -0.0074 181 VAL B CG1 4239 C CG2 . VAL B 181 ? 0.6320 0.6929 0.6911 -0.1328 0.0639 -0.0001 181 VAL B CG2 4240 N N . LEU B 182 ? 1.1022 1.2395 1.2155 -0.1379 0.0522 -0.0099 182 LEU B N 4241 C CA . LEU B 182 ? 1.1198 1.2800 1.2446 -0.1258 0.0558 -0.0121 182 LEU B CA 4242 C C . LEU B 182 ? 1.1081 1.2675 1.2350 -0.1106 0.0459 -0.0161 182 LEU B C 4243 O O . LEU B 182 ? 1.1505 1.3276 1.2980 -0.1057 0.0361 -0.0213 182 LEU B O 4244 C CB . LEU B 182 ? 1.1917 1.3853 1.3445 -0.1301 0.0563 -0.0162 182 LEU B CB 4245 C CG . LEU B 182 ? 1.3306 1.5369 1.5046 -0.1413 0.0458 -0.0186 182 LEU B CG 4246 C CD1 . LEU B 182 ? 1.3607 1.5582 1.5343 -0.1374 0.0285 -0.0206 182 LEU B CD1 4247 C CD2 . LEU B 182 ? 1.3918 1.6358 1.5989 -0.1394 0.0485 -0.0231 182 LEU B CD2 4248 N N . LEU B 183 ? 0.9504 1.0887 1.0589 -0.1032 0.0478 -0.0131 183 LEU B N 4249 C CA . LEU B 183 ? 0.8538 0.9898 0.9661 -0.0896 0.0389 -0.0162 183 LEU B CA 4250 C C . LEU B 183 ? 0.7858 0.9439 0.9106 -0.0777 0.0389 -0.0231 183 LEU B C 4251 O O . LEU B 183 ? 0.7725 0.9454 0.8966 -0.0792 0.0486 -0.0242 183 LEU B O 4252 C CB . LEU B 183 ? 0.8541 0.9635 0.9475 -0.0856 0.0412 -0.0112 183 LEU B CB 4253 C CG . LEU B 183 ? 0.9133 1.0073 0.9882 -0.0911 0.0531 -0.0046 183 LEU B CG 4254 C CD1 . LEU B 183 ? 0.9804 1.0886 1.0522 -0.0859 0.0597 -0.0041 183 LEU B CD1 4255 C CD2 . LEU B 183 ? 0.9205 0.9881 0.9831 -0.0871 0.0537 -0.0001 183 LEU B CD2 4256 N N . THR B 184 ? 0.7713 0.9312 0.9074 -0.0662 0.0287 -0.0281 184 THR B N 4257 C CA . THR B 184 ? 0.8370 1.0159 0.9860 -0.0538 0.0271 -0.0378 184 THR B CA 4258 C C . THR B 184 ? 0.9159 1.0820 1.0548 -0.0427 0.0238 -0.0395 184 THR B C 4259 O O . THR B 184 ? 0.9668 1.1440 1.1048 -0.0334 0.0252 -0.0476 184 THR B O 4260 C CB . THR B 184 ? 0.8481 1.0429 1.0272 -0.0490 0.0158 -0.0444 184 THR B CB 4261 O OG1 . THR B 184 ? 0.7529 0.9309 0.9359 -0.0461 0.0038 -0.0407 184 THR B OG1 4262 C CG2 . THR B 184 ? 0.9276 1.1367 1.1199 -0.0602 0.0163 -0.0422 184 THR B CG2 4263 N N . HIS B 185 ? 0.9054 1.0492 1.0370 -0.0438 0.0194 -0.0326 185 HIS B N 4264 C CA . HIS B 185 ? 0.7854 0.9167 0.9110 -0.0345 0.0154 -0.0327 185 HIS B CA 4265 C C . HIS B 185 ? 0.7034 0.8132 0.8088 -0.0397 0.0221 -0.0224 185 HIS B C 4266 O O . HIS B 185 ? 0.6730 0.7689 0.7754 -0.0475 0.0240 -0.0159 185 HIS B O 4267 C CB . HIS B 185 ? 0.7938 0.9202 0.9394 -0.0283 0.0028 -0.0348 185 HIS B CB 4268 C CG . HIS B 185 ? 0.9538 1.0982 1.1228 -0.0205 -0.0054 -0.0458 185 HIS B CG 4269 N ND1 . HIS B 185 ? 1.0035 1.1530 1.1805 -0.0087 -0.0115 -0.0565 185 HIS B ND1 4270 C CD2 . HIS B 185 ? 0.9921 1.1502 1.1802 -0.0222 -0.0093 -0.0485 185 HIS B CD2 4271 C CE1 . HIS B 185 ? 0.9187 1.0830 1.1191 -0.0031 -0.0175 -0.0662 185 HIS B CE1 4272 N NE2 . HIS B 185 ? 0.9470 1.1174 1.1559 -0.0108 -0.0164 -0.0607 185 HIS B NE2 4273 N N . LEU B 186 ? 0.7409 0.8478 0.8318 -0.0350 0.0253 -0.0211 186 LEU B N 4274 C CA . LEU B 186 ? 0.7047 0.7909 0.7806 -0.0375 0.0302 -0.0109 186 LEU B CA 4275 C C . LEU B 186 ? 0.7327 0.8141 0.8074 -0.0263 0.0226 -0.0115 186 LEU B C 4276 O O . LEU B 186 ? 0.7786 0.8714 0.8456 -0.0199 0.0201 -0.0166 186 LEU B O 4277 C CB . LEU B 186 ? 0.6972 0.7820 0.7546 -0.0457 0.0421 -0.0042 186 LEU B CB 4278 C CG . LEU B 186 ? 0.6368 0.6991 0.6802 -0.0471 0.0468 0.0069 186 LEU B CG 4279 C CD1 . LEU B 186 ? 0.6021 0.6449 0.6514 -0.0519 0.0482 0.0100 186 LEU B CD1 4280 C CD2 . LEU B 186 ? 0.6791 0.7404 0.7063 -0.0553 0.0579 0.0146 186 LEU B CD2 4281 N N . ASP B 187 ? 0.7484 0.8141 0.8311 -0.0241 0.0190 -0.0069 187 ASP B N 4282 C CA . ASP B 187 ? 0.8270 0.8882 0.9141 -0.0142 0.0101 -0.0068 187 ASP B CA 4283 C C . ASP B 187 ? 0.8128 0.8567 0.8892 -0.0151 0.0154 0.0047 187 ASP B C 4284 O O . ASP B 187 ? 0.8201 0.8491 0.9017 -0.0193 0.0215 0.0106 187 ASP B O 4285 C CB . ASP B 187 ? 0.9538 1.0127 1.0659 -0.0101 0.0012 -0.0099 187 ASP B CB 4286 C CG . ASP B 187 ? 1.0313 1.0896 1.1540 -0.0001 -0.0107 -0.0120 187 ASP B CG 4287 O OD1 . ASP B 187 ? 1.1231 1.1803 1.2313 0.0038 -0.0126 -0.0096 187 ASP B OD1 4288 O OD2 . ASP B 187 ? 0.9885 1.0471 1.1348 0.0033 -0.0191 -0.0154 187 ASP B OD2 4289 N N . LEU B 188 ? 0.7775 0.8230 0.8384 -0.0106 0.0130 0.0078 188 LEU B N 4290 C CA . LEU B 188 ? 0.7835 0.8123 0.8362 -0.0101 0.0160 0.0202 188 LEU B CA 4291 C C . LEU B 188 ? 0.7613 0.7904 0.8177 0.0009 0.0022 0.0214 188 LEU B C 4292 O O . LEU B 188 ? 0.7920 0.8108 0.8391 0.0032 0.0014 0.0323 188 LEU B O 4293 C CB . LEU B 188 ? 0.8225 0.8495 0.8507 -0.0168 0.0262 0.0280 188 LEU B CB 4294 C CG . LEU B 188 ? 0.8456 0.8696 0.8707 -0.0294 0.0395 0.0288 188 LEU B CG 4295 C CD1 . LEU B 188 ? 0.8591 0.8813 0.8633 -0.0360 0.0488 0.0382 188 LEU B CD1 4296 C CD2 . LEU B 188 ? 0.8620 0.8664 0.8987 -0.0336 0.0448 0.0318 188 LEU B CD2 4297 N N . ARG B 189 ? 0.8213 0.8613 0.8932 0.0073 -0.0099 0.0107 189 ARG B N 4298 C CA . ARG B 189 ? 0.8006 0.8424 0.8798 0.0170 -0.0260 0.0094 189 ARG B CA 4299 C C . ARG B 189 ? 0.9169 0.9436 1.0132 0.0198 -0.0273 0.0208 189 ARG B C 4300 O O . ARG B 189 ? 0.9155 0.9305 1.0216 0.0148 -0.0153 0.0266 189 ARG B O 4301 C CB . ARG B 189 ? 0.7126 0.7655 0.8137 0.0217 -0.0381 -0.0047 189 ARG B CB 4302 C CG . ARG B 189 ? 0.6833 0.7521 0.7722 0.0224 -0.0396 -0.0186 189 ARG B CG 4303 C CD . ARG B 189 ? 0.7387 0.8149 0.8534 0.0277 -0.0529 -0.0326 189 ARG B CD 4304 N NE . ARG B 189 ? 0.7916 0.8641 0.9322 0.0231 -0.0483 -0.0317 189 ARG B NE 4305 C CZ . ARG B 189 ? 0.7935 0.8698 0.9603 0.0258 -0.0578 -0.0409 189 ARG B CZ 4306 N NH1 . ARG B 189 ? 0.7882 0.8716 0.9606 0.0333 -0.0727 -0.0542 189 ARG B NH1 4307 N NH2 . ARG B 189 ? 0.7529 0.8250 0.9394 0.0209 -0.0529 -0.0367 189 ARG B NH2 4308 N N . GLY B 190 ? 1.1015 1.1291 1.2014 0.0280 -0.0422 0.0233 190 GLY B N 4309 C CA . GLY B 190 ? 1.1337 1.1508 1.2585 0.0324 -0.0460 0.0326 190 GLY B CA 4310 C C . GLY B 190 ? 1.1217 1.1211 1.2430 0.0295 -0.0321 0.0466 190 GLY B C 4311 O O . GLY B 190 ? 1.2457 1.2363 1.3930 0.0332 -0.0315 0.0529 190 GLY B O 4312 N N . ASN B 191 ? 0.8854 0.8797 0.9782 0.0228 -0.0205 0.0510 191 ASN B N 4313 C CA . ASN B 191 ? 0.8634 0.8383 0.9527 0.0196 -0.0082 0.0636 191 ASN B CA 4314 C C . ASN B 191 ? 0.8236 0.7920 0.8996 0.0252 -0.0169 0.0775 191 ASN B C 4315 O O . ASN B 191 ? 0.8256 0.8047 0.8959 0.0322 -0.0339 0.0770 191 ASN B O 4316 C CB . ASN B 191 ? 0.9211 0.8918 0.9907 0.0081 0.0085 0.0624 191 ASN B CB 4317 C CG . ASN B 191 ? 0.9166 0.8822 1.0020 0.0021 0.0202 0.0555 191 ASN B CG 4318 O OD1 . ASN B 191 ? 0.8599 0.8088 0.9572 0.0015 0.0292 0.0598 191 ASN B OD1 4319 N ND2 . ASN B 191 ? 0.9476 0.9272 1.0325 -0.0019 0.0200 0.0445 191 ASN B ND2 4320 N N . ARG B 192 ? 0.8808 0.8304 0.9511 0.0220 -0.0063 0.0898 192 ARG B N 4321 C CA . ARG B 192 ? 0.9683 0.9082 1.0286 0.0274 -0.0145 0.1064 192 ARG B CA 4322 C C . ARG B 192 ? 1.0497 0.9854 1.0739 0.0191 -0.0063 0.1154 192 ARG B C 4323 O O . ARG B 192 ? 1.2048 1.1216 1.2244 0.0174 -0.0009 0.1307 192 ARG B O 4324 C CB . ARG B 192 ? 1.0467 0.9659 1.1353 0.0320 -0.0102 0.1159 192 ARG B CB 4325 C CG . ARG B 192 ? 1.2765 1.1913 1.3724 0.0430 -0.0274 0.1307 192 ARG B CG 4326 C CD . ARG B 192 ? 1.4523 1.3443 1.5762 0.0475 -0.0204 0.1411 192 ARG B CD 4327 N NE . ARG B 192 ? 1.5876 1.4687 1.7049 0.0540 -0.0327 0.1613 192 ARG B NE 4328 C CZ . ARG B 192 ? 1.6637 1.5286 1.7556 0.0484 -0.0261 0.1754 192 ARG B CZ 4329 N NH1 . ARG B 192 ? 1.6393 1.4981 1.7124 0.0357 -0.0075 0.1700 192 ARG B NH1 4330 N NH2 . ARG B 192 ? 1.7413 1.5960 1.8280 0.0549 -0.0390 0.1959 192 ARG B NH2 4331 N N . LEU B 193 ? 0.9976 0.9515 0.9992 0.0141 -0.0048 0.1059 193 LEU B N 4332 C CA . LEU B 193 ? 1.0366 0.9914 1.0065 0.0051 0.0054 0.1131 193 LEU B CA 4333 C C . LEU B 193 ? 1.1842 1.1473 1.1234 0.0099 -0.0062 0.1228 193 LEU B C 4334 O O . LEU B 193 ? 1.2346 1.2147 1.1678 0.0171 -0.0203 0.1131 193 LEU B O 4335 C CB . LEU B 193 ? 0.9079 0.8794 0.8724 -0.0033 0.0158 0.0975 193 LEU B CB 4336 C CG . LEU B 193 ? 0.8840 0.8477 0.8705 -0.0104 0.0278 0.0891 193 LEU B CG 4337 C CD1 . LEU B 193 ? 0.8653 0.8500 0.8544 -0.0135 0.0292 0.0718 193 LEU B CD1 4338 C CD2 . LEU B 193 ? 0.9290 0.8757 0.9082 -0.0217 0.0431 0.0992 193 LEU B CD2 4339 N N . LYS B 194 ? 1.2253 1.1757 1.1440 0.0055 -0.0005 0.1421 194 LYS B N 4340 C CA . LYS B 194 ? 1.2834 1.2406 1.1666 0.0087 -0.0100 0.1542 194 LYS B CA 4341 C C . LYS B 194 ? 1.2770 1.2450 1.1278 -0.0022 0.0058 0.1568 194 LYS B C 4342 O O . LYS B 194 ? 1.2526 1.2368 1.0703 -0.0002 0.0013 0.1571 194 LYS B O 4343 C CB . LYS B 194 ? 1.3588 1.2935 1.2424 0.0135 -0.0184 0.1786 194 LYS B CB 4344 C CG . LYS B 194 ? 1.5302 1.4391 1.4297 0.0056 -0.0027 0.1912 194 LYS B CG 4345 C CD . LYS B 194 ? 1.6720 1.5578 1.5759 0.0122 -0.0127 0.2156 194 LYS B CD 4346 C CE . LYS B 194 ? 1.7491 1.6061 1.6701 0.0045 0.0031 0.2267 194 LYS B CE 4347 N NZ . LYS B 194 ? 1.7941 1.6502 1.6894 -0.0106 0.0204 0.2338 194 LYS B NZ 4348 N N . VAL B 195 ? 1.3324 1.2922 1.1932 -0.0140 0.0246 0.1580 195 VAL B N 4349 C CA . VAL B 195 ? 1.3294 1.2997 1.1673 -0.0260 0.0416 0.1617 195 VAL B CA 4350 C C . VAL B 195 ? 1.2834 1.2576 1.1445 -0.0361 0.0563 0.1470 195 VAL B C 4351 O O . VAL B 195 ? 1.2789 1.2383 1.1683 -0.0363 0.0561 0.1414 195 VAL B O 4352 C CB . VAL B 195 ? 1.4975 1.4477 1.3184 -0.0330 0.0485 0.1897 195 VAL B CB 4353 C CG1 . VAL B 195 ? 1.5207 1.4836 1.3208 -0.0467 0.0677 0.1948 195 VAL B CG1 4354 C CG2 . VAL B 195 ? 1.5326 1.4779 1.3295 -0.0227 0.0316 0.2068 195 VAL B CG2 4355 N N . MET B 196 ? 1.2372 1.2324 1.0864 -0.0444 0.0687 0.1403 196 MET B N 4356 C CA . MET B 196 ? 1.1040 1.1048 0.9746 -0.0549 0.0810 0.1281 196 MET B CA 4357 C C . MET B 196 ? 1.1447 1.1571 1.0026 -0.0684 0.0987 0.1355 196 MET B C 4358 O O . MET B 196 ? 1.1733 1.2114 1.0135 -0.0675 0.1032 0.1303 196 MET B O 4359 C CB . MET B 196 ? 0.9765 0.9983 0.8612 -0.0483 0.0746 0.1041 196 MET B CB 4360 C CG . MET B 196 ? 0.9621 0.9852 0.8729 -0.0568 0.0817 0.0922 196 MET B CG 4361 S SD . MET B 196 ? 1.1762 1.2129 1.1085 -0.0468 0.0695 0.0692 196 MET B SD 4362 C CE . MET B 196 ? 1.4869 1.4977 1.4318 -0.0378 0.0573 0.0747 196 MET B CE 4363 N N . PRO B 197 ? 1.1547 1.1488 1.0237 -0.0814 0.1094 0.1465 197 PRO B N 4364 C CA . PRO B 197 ? 1.1493 1.1495 1.0100 -0.0962 0.1263 0.1585 197 PRO B CA 4365 C C . PRO B 197 ? 1.0935 1.1204 0.9698 -0.1052 0.1368 0.1424 197 PRO B C 4366 O O . PRO B 197 ? 1.0183 1.0481 0.9172 -0.1038 0.1315 0.1247 197 PRO B O 4367 C CB . PRO B 197 ? 1.2084 1.1745 1.0829 -0.1057 0.1300 0.1730 197 PRO B CB 4368 C CG . PRO B 197 ? 1.1914 1.1437 1.0901 -0.1000 0.1206 0.1573 197 PRO B CG 4369 C CD . PRO B 197 ? 1.1959 1.1611 1.0885 -0.0828 0.1061 0.1467 197 PRO B CD 4370 N N . PHE B 198 ? 1.1845 1.2311 1.0499 -0.1143 0.1516 0.1494 198 PHE B N 4371 C CA . PHE B 198 ? 1.1825 1.2566 1.0674 -0.1228 0.1619 0.1353 198 PHE B CA 4372 C C . PHE B 198 ? 1.2783 1.3383 1.1909 -0.1390 0.1674 0.1372 198 PHE B C 4373 O O . PHE B 198 ? 1.2113 1.2816 1.1485 -0.1421 0.1649 0.1204 198 PHE B O 4374 C CB . PHE B 198 ? 1.1524 1.2553 1.0199 -0.1273 0.1782 0.1414 198 PHE B CB 4375 C CG . PHE B 198 ? 1.0767 1.2117 0.9693 -0.1343 0.1886 0.1260 198 PHE B CG 4376 C CD1 . PHE B 198 ? 1.0448 1.2071 0.9418 -0.1225 0.1845 0.1044 198 PHE B CD1 4377 C CD2 . PHE B 198 ? 1.0396 1.1769 0.9551 -0.1526 0.2013 0.1330 198 PHE B CD2 4378 C CE1 . PHE B 198 ? 1.0460 1.2381 0.9703 -0.1277 0.1931 0.0908 198 PHE B CE1 4379 C CE2 . PHE B 198 ? 1.0105 1.1790 0.9535 -0.1587 0.2092 0.1193 198 PHE B CE2 4380 C CZ . PHE B 198 ? 1.0294 1.2258 0.9773 -0.1457 0.2052 0.0986 198 PHE B CZ 4381 N N . ALA B 199 ? 1.4523 1.4877 1.3606 -0.1495 0.1739 0.1577 199 ALA B N 4382 C CA . ALA B 199 ? 1.5025 1.5223 1.4356 -0.1666 0.1797 0.1600 199 ALA B CA 4383 C C . ALA B 199 ? 1.5091 1.5059 1.4594 -0.1635 0.1671 0.1461 199 ALA B C 4384 O O . ALA B 199 ? 1.5325 1.4991 1.4773 -0.1568 0.1598 0.1522 199 ALA B O 4385 C CB . ALA B 199 ? 1.5575 1.5524 1.4822 -0.1773 0.1885 0.1860 199 ALA B CB 4386 N N . GLY B 200 ? 1.3753 1.3874 1.3468 -0.1684 0.1650 0.1278 200 GLY B N 4387 C CA . GLY B 200 ? 1.3643 1.3573 1.3485 -0.1665 0.1544 0.1141 200 GLY B CA 4388 C C . GLY B 200 ? 1.3901 1.3991 1.3730 -0.1508 0.1432 0.0981 200 GLY B C 4389 O O . GLY B 200 ? 1.5224 1.5541 1.5192 -0.1523 0.1405 0.0839 200 GLY B O 4390 N N . VAL B 201 ? 1.2428 1.2402 1.2116 -0.1358 0.1359 0.1014 201 VAL B N 4391 C CA . VAL B 201 ? 1.1118 1.1193 1.0825 -0.1214 0.1243 0.0871 201 VAL B CA 4392 C C . VAL B 201 ? 1.0451 1.0894 1.0182 -0.1175 0.1242 0.0764 201 VAL B C 4393 O O . VAL B 201 ? 1.0416 1.0981 1.0293 -0.1149 0.1177 0.0616 201 VAL B O 4394 C CB . VAL B 201 ? 1.0589 1.0523 1.0159 -0.1065 0.1163 0.0940 201 VAL B CB 4395 C CG1 . VAL B 201 ? 1.0518 1.0533 1.0163 -0.0935 0.1043 0.0792 201 VAL B CG1 4396 C CG2 . VAL B 201 ? 1.1355 1.0929 1.0940 -0.1090 0.1173 0.1051 201 VAL B CG2 4397 N N . LEU B 202 ? 0.9822 1.0436 0.9412 -0.1174 0.1323 0.0841 202 LEU B N 4398 C CA . LEU B 202 ? 0.9371 1.0319 0.8950 -0.1097 0.1325 0.0727 202 LEU B CA 4399 C C . LEU B 202 ? 0.9255 1.0480 0.9038 -0.1197 0.1415 0.0648 202 LEU B C 4400 O O . LEU B 202 ? 0.9208 1.0669 0.9114 -0.1127 0.1375 0.0495 202 LEU B O 4401 C CB . LEU B 202 ? 0.9616 1.0637 0.8908 -0.1032 0.1373 0.0827 202 LEU B CB 4402 C CG . LEU B 202 ? 0.9598 1.0701 0.8754 -0.0856 0.1253 0.0726 202 LEU B CG 4403 C CD1 . LEU B 202 ? 0.9791 1.1027 0.9186 -0.0790 0.1161 0.0515 202 LEU B CD1 4404 C CD2 . LEU B 202 ? 0.8880 0.9706 0.7894 -0.0775 0.1137 0.0829 202 LEU B CD2 4405 N N . GLU B 203 ? 0.9400 1.0595 0.9251 -0.1361 0.1530 0.0753 203 GLU B N 4406 C CA . GLU B 203 ? 1.0141 1.1631 1.0213 -0.1465 0.1627 0.0700 203 GLU B CA 4407 C C . GLU B 203 ? 1.1064 1.2644 1.1415 -0.1470 0.1518 0.0533 203 GLU B C 4408 O O . GLU B 203 ? 1.1468 1.3349 1.2038 -0.1497 0.1553 0.0447 203 GLU B O 4409 C CB . GLU B 203 ? 1.0026 1.1434 1.0153 -0.1657 0.1757 0.0856 203 GLU B CB 4410 C CG . GLU B 203 ? 0.9679 1.0728 0.9862 -0.1750 0.1691 0.0899 203 GLU B CG 4411 C CD . GLU B 203 ? 1.0445 1.1389 1.0696 -0.1942 0.1815 0.1054 203 GLU B CD 4412 O OE1 . GLU B 203 ? 1.0315 1.0903 1.0495 -0.1987 0.1797 0.1153 203 GLU B OE1 4413 O OE2 . GLU B 203 ? 1.1050 1.2268 1.1452 -0.2046 0.1933 0.1077 203 GLU B OE2 4414 N N . HIS B 204 ? 1.1644 1.2968 1.1986 -0.1438 0.1388 0.0495 204 HIS B N 4415 C CA . HIS B 204 ? 1.1689 1.3056 1.2233 -0.1438 0.1269 0.0359 204 HIS B CA 4416 C C . HIS B 204 ? 1.2141 1.3671 1.2713 -0.1268 0.1175 0.0237 204 HIS B C 4417 O O . HIS B 204 ? 1.2290 1.4013 1.3077 -0.1256 0.1110 0.0128 204 HIS B O 4418 C CB . HIS B 204 ? 1.0931 1.1952 1.1421 -0.1478 0.1193 0.0372 204 HIS B CB 4419 C CG . HIS B 204 ? 1.0605 1.1406 1.1058 -0.1627 0.1278 0.0485 204 HIS B CG 4420 N ND1 . HIS B 204 ? 1.1126 1.1572 1.1441 -0.1622 0.1270 0.0549 204 HIS B ND1 4421 C CD2 . HIS B 204 ? 1.0178 1.1062 1.0747 -0.1786 0.1375 0.0545 204 HIS B CD2 4422 C CE1 . HIS B 204 ? 1.1006 1.1305 1.1346 -0.1770 0.1352 0.0640 204 HIS B CE1 4423 N NE2 . HIS B 204 ? 1.0454 1.1013 1.0946 -0.1879 0.1416 0.0644 204 HIS B NE2 4424 N N . ILE B 205 ? 1.2099 1.3541 1.2467 -0.1140 0.1156 0.0259 205 ILE B N 4425 C CA . ILE B 205 ? 1.1239 1.2830 1.1620 -0.0980 0.1076 0.0143 205 ILE B CA 4426 C C . ILE B 205 ? 1.2264 1.4187 1.2694 -0.0960 0.1176 0.0088 205 ILE B C 4427 O O . ILE B 205 ? 1.3592 1.5610 1.4000 -0.1064 0.1318 0.0170 205 ILE B O 4428 C CB . ILE B 205 ? 1.0732 1.2133 1.0885 -0.0863 0.1018 0.0186 205 ILE B CB 4429 C CG1 . ILE B 205 ? 1.1082 1.2161 1.1208 -0.0896 0.0964 0.0256 205 ILE B CG1 4430 C CG2 . ILE B 205 ? 1.0325 1.1824 1.0533 -0.0711 0.0902 0.0053 205 ILE B CG2 4431 C CD1 . ILE B 205 ? 1.1540 1.2575 1.1832 -0.0864 0.0849 0.0159 205 ILE B CD1 4432 N N . GLY B 206 ? 1.2156 1.4257 1.2670 -0.0829 0.1114 -0.0053 206 GLY B N 4433 C CA . GLY B 206 ? 1.2575 1.5001 1.3160 -0.0793 0.1218 -0.0138 206 GLY B CA 4434 C C . GLY B 206 ? 1.2979 1.5600 1.3921 -0.0761 0.1144 -0.0276 206 GLY B C 4435 O O . GLY B 206 ? 1.3488 1.6357 1.4552 -0.0667 0.1172 -0.0407 206 GLY B O 4436 N N . GLY B 207 ? 1.2857 1.5356 1.3961 -0.0839 0.1046 -0.0248 207 GLY B N 4437 C CA . GLY B 207 ? 1.2696 1.5332 1.4123 -0.0810 0.0935 -0.0349 207 GLY B CA 4438 C C . GLY B 207 ? 1.2927 1.5423 1.4352 -0.0679 0.0774 -0.0417 207 GLY B C 4439 O O . GLY B 207 ? 1.3230 1.5809 1.4908 -0.0632 0.0662 -0.0491 207 GLY B O 4440 N N . ILE B 208 ? 1.1492 1.3776 1.2651 -0.0623 0.0758 -0.0379 208 ILE B N 4441 C CA . ILE B 208 ? 0.9529 1.1677 1.0694 -0.0505 0.0615 -0.0433 208 ILE B CA 4442 C C . ILE B 208 ? 0.9204 1.1539 1.0496 -0.0361 0.0576 -0.0589 208 ILE B C 4443 O O . ILE B 208 ? 0.8654 1.1180 0.9889 -0.0326 0.0684 -0.0652 208 ILE B O 4444 C CB . ILE B 208 ? 0.7084 0.8988 0.7969 -0.0480 0.0608 -0.0354 208 ILE B CB 4445 C CG1 . ILE B 208 ? 0.5237 0.7216 0.5885 -0.0482 0.0737 -0.0320 208 ILE B CG1 4446 C CG2 . ILE B 208 ? 0.6766 0.8421 0.7583 -0.0585 0.0601 -0.0232 208 ILE B CG2 4447 C CD1 . ILE B 208 ? 0.5558 0.7412 0.5976 -0.0384 0.0686 -0.0311 208 ILE B CD1 4448 N N . MET B 209 ? 0.9452 1.1722 1.0912 -0.0278 0.0428 -0.0652 209 MET B N 4449 C CA . MET B 209 ? 0.9336 1.1723 1.0923 -0.0133 0.0368 -0.0811 209 MET B CA 4450 C C . MET B 209 ? 0.9044 1.1263 1.0416 -0.0052 0.0308 -0.0828 209 MET B C 4451 O O . MET B 209 ? 1.0088 1.2398 1.1361 0.0040 0.0326 -0.0944 209 MET B O 4452 C CB . MET B 209 ? 1.0923 1.3331 1.2856 -0.0086 0.0229 -0.0865 209 MET B CB 4453 C CG . MET B 209 ? 1.1255 1.3725 1.3374 -0.0193 0.0218 -0.0785 209 MET B CG 4454 S SD . MET B 209 ? 1.1973 1.4785 1.4275 -0.0237 0.0354 -0.0839 209 MET B SD 4455 C CE . MET B 209 ? 1.2637 1.5653 1.5124 -0.0052 0.0361 -0.1053 209 MET B CE 4456 N N . GLU B 210 ? 0.6665 0.8646 0.7969 -0.0088 0.0237 -0.0717 210 GLU B N 4457 C CA . GLU B 210 ? 0.7094 0.8918 0.8246 -0.0020 0.0164 -0.0716 210 GLU B CA 4458 C C . GLU B 210 ? 0.8452 1.0090 0.9363 -0.0098 0.0218 -0.0555 210 GLU B C 4459 O O . GLU B 210 ? 0.8657 1.0201 0.9583 -0.0199 0.0261 -0.0448 210 GLU B O 4460 C CB . GLU B 210 ? 0.6463 0.8176 0.7848 0.0041 0.0007 -0.0752 210 GLU B CB 4461 C CG . GLU B 210 ? 0.6797 0.8385 0.8104 0.0118 -0.0090 -0.0777 210 GLU B CG 4462 C CD . GLU B 210 ? 0.8123 0.9593 0.9693 0.0155 -0.0230 -0.0783 210 GLU B CD 4463 O OE1 . GLU B 210 ? 0.9623 1.0971 1.1260 0.0085 -0.0226 -0.0658 210 GLU B OE1 4464 O OE2 . GLU B 210 ? 0.7270 0.8766 0.8977 0.0249 -0.0340 -0.0914 210 GLU B OE2 4465 N N . ILE B 211 ? 0.8355 0.9937 0.9049 -0.0046 0.0205 -0.0545 211 ILE B N 4466 C CA . ILE B 211 ? 0.7591 0.8979 0.8098 -0.0092 0.0229 -0.0393 211 ILE B CA 4467 C C . ILE B 211 ? 0.7295 0.8605 0.7718 0.0007 0.0110 -0.0416 211 ILE B C 4468 O O . ILE B 211 ? 0.7661 0.9090 0.8016 0.0090 0.0059 -0.0538 211 ILE B O 4469 C CB . ILE B 211 ? 0.7529 0.8951 0.7800 -0.0176 0.0379 -0.0294 211 ILE B CB 4470 C CG1 . ILE B 211 ? 0.7981 0.9174 0.8092 -0.0215 0.0394 -0.0130 211 ILE B CG1 4471 C CG2 . ILE B 211 ? 0.7562 0.9169 0.7646 -0.0119 0.0423 -0.0372 211 ILE B CG2 4472 C CD1 . ILE B 211 ? 0.8481 0.9661 0.8409 -0.0319 0.0541 -0.0005 211 ILE B CD1 4473 N N . GLN B 212 ? 0.7082 0.8197 0.7525 0.0000 0.0063 -0.0309 212 GLN B N 4474 C CA . GLN B 212 ? 0.7457 0.8504 0.7888 0.0090 -0.0072 -0.0322 212 GLN B CA 4475 C C . GLN B 212 ? 0.7537 0.8430 0.7794 0.0073 -0.0053 -0.0161 212 GLN B C 4476 O O . GLN B 212 ? 0.7434 0.8179 0.7750 0.0012 0.0013 -0.0047 212 GLN B O 4477 C CB . GLN B 212 ? 0.7653 0.8634 0.8397 0.0124 -0.0183 -0.0364 212 GLN B CB 4478 C CG . GLN B 212 ? 0.8569 0.9679 0.9483 0.0193 -0.0281 -0.0540 212 GLN B CG 4479 C CD . GLN B 212 ? 1.0184 1.1249 1.1416 0.0177 -0.0322 -0.0548 212 GLN B CD 4480 O OE1 . GLN B 212 ? 1.1343 1.2337 1.2616 0.0097 -0.0240 -0.0447 212 GLN B OE1 4481 N NE2 . GLN B 212 ? 1.0433 1.1531 1.1883 0.0248 -0.0454 -0.0667 212 GLN B NE2 4482 N N . LEU B 213 ? 0.7986 0.8911 0.8022 0.0132 -0.0116 -0.0158 213 LEU B N 4483 C CA . LEU B 213 ? 0.7831 0.8619 0.7690 0.0129 -0.0118 0.0009 213 LEU B CA 4484 C C . LEU B 213 ? 0.8054 0.8826 0.7895 0.0231 -0.0308 -0.0011 213 LEU B C 4485 O O . LEU B 213 ? 0.9031 0.9744 0.8658 0.0252 -0.0349 0.0105 213 LEU B O 4486 C CB . LEU B 213 ? 0.8127 0.8970 0.7657 0.0074 0.0009 0.0089 213 LEU B CB 4487 C CG . LEU B 213 ? 0.8313 0.9228 0.7864 -0.0031 0.0187 0.0086 213 LEU B CG 4488 C CD1 . LEU B 213 ? 0.8224 0.9306 0.7493 -0.0056 0.0293 0.0084 213 LEU B CD1 4489 C CD2 . LEU B 213 ? 0.8121 0.8844 0.7740 -0.0126 0.0282 0.0237 213 LEU B CD2 4490 N N . GLU B 214 ? 0.7655 0.8473 0.7741 0.0289 -0.0435 -0.0150 214 GLU B N 4491 C CA . GLU B 214 ? 0.8241 0.9095 0.8327 0.0382 -0.0638 -0.0233 214 GLU B CA 4492 C C . GLU B 214 ? 0.8836 0.9572 0.8931 0.0422 -0.0758 -0.0094 214 GLU B C 4493 O O . GLU B 214 ? 1.0130 1.0898 0.9972 0.0472 -0.0872 -0.0084 214 GLU B O 4494 C CB . GLU B 214 ? 0.9397 1.0289 0.9836 0.0417 -0.0740 -0.0389 214 GLU B CB 4495 C CG . GLU B 214 ? 1.0748 1.1792 1.1149 0.0442 -0.0741 -0.0593 214 GLU B CG 4496 C CD . GLU B 214 ? 1.1930 1.3040 1.2296 0.0373 -0.0547 -0.0591 214 GLU B CD 4497 O OE1 . GLU B 214 ? 1.2777 1.3808 1.3123 0.0296 -0.0416 -0.0438 214 GLU B OE1 4498 O OE2 . GLU B 214 ? 1.2644 1.3888 1.3024 0.0399 -0.0532 -0.0752 214 GLU B OE2 4499 N N . GLU B 215 ? 0.8619 0.9226 0.9002 0.0404 -0.0735 0.0011 215 GLU B N 4500 C CA . GLU B 215 ? 0.8822 0.9337 0.9308 0.0458 -0.0862 0.0128 215 GLU B CA 4501 C C . GLU B 215 ? 0.9115 0.9478 0.9502 0.0423 -0.0745 0.0332 215 GLU B C 4502 O O . GLU B 215 ? 0.9187 0.9431 0.9844 0.0422 -0.0706 0.0418 215 GLU B O 4503 C CB . GLU B 215 ? 0.8868 0.9361 0.9813 0.0483 -0.0942 0.0089 215 GLU B CB 4504 C CG . GLU B 215 ? 0.9480 1.0092 1.0558 0.0533 -0.1126 -0.0092 215 GLU B CG 4505 C CD . GLU B 215 ? 1.0303 1.0899 1.1865 0.0540 -0.1185 -0.0119 215 GLU B CD 4506 O OE1 . GLU B 215 ? 0.9855 1.0378 1.1611 0.0491 -0.1033 -0.0044 215 GLU B OE1 4507 O OE2 . GLU B 215 ? 1.1489 1.2147 1.3234 0.0589 -0.1384 -0.0216 215 GLU B OE2 4508 N N . ASN B 216 ? 0.9036 0.9401 0.9043 0.0397 -0.0685 0.0408 216 ASN B N 4509 C CA . ASN B 216 ? 0.7877 0.8083 0.7776 0.0357 -0.0574 0.0607 216 ASN B CA 4510 C C . ASN B 216 ? 0.7213 0.7389 0.6831 0.0406 -0.0695 0.0748 216 ASN B C 4511 O O . ASN B 216 ? 0.6902 0.7211 0.6253 0.0441 -0.0804 0.0680 216 ASN B O 4512 C CB . ASN B 216 ? 0.8163 0.8370 0.7889 0.0250 -0.0358 0.0613 216 ASN B CB 4513 C CG . ASN B 216 ? 0.8048 0.8211 0.8048 0.0190 -0.0233 0.0546 216 ASN B CG 4514 O OD1 . ASN B 216 ? 0.7948 0.7943 0.8072 0.0153 -0.0138 0.0641 216 ASN B OD1 4515 N ND2 . ASN B 216 ? 0.8527 0.8834 0.8616 0.0184 -0.0238 0.0380 216 ASN B ND2 4516 N N . PRO B 217 ? 0.8020 0.8015 0.7694 0.0412 -0.0679 0.0945 217 PRO B N 4517 C CA . PRO B 217 ? 0.8888 0.8824 0.8316 0.0459 -0.0802 0.1125 217 PRO B CA 4518 C C . PRO B 217 ? 0.9489 0.9430 0.8462 0.0387 -0.0684 0.1227 217 PRO B C 4519 O O . PRO B 217 ? 1.0543 1.0316 0.9433 0.0353 -0.0612 0.1433 217 PRO B O 4520 C CB . PRO B 217 ? 0.9140 0.8862 0.8869 0.0484 -0.0786 0.1291 217 PRO B CB 4521 C CG . PRO B 217 ? 0.8344 0.7986 0.8264 0.0401 -0.0561 0.1229 217 PRO B CG 4522 C CD . PRO B 217 ? 0.7980 0.7806 0.7978 0.0383 -0.0553 0.1003 217 PRO B CD 4523 N N . TRP B 218 ? 0.9000 0.9132 0.7703 0.0364 -0.0658 0.1085 218 TRP B N 4524 C CA . TRP B 218 ? 0.8988 0.9166 0.7279 0.0289 -0.0513 0.1165 218 TRP B CA 4525 C C . TRP B 218 ? 0.9436 0.9562 0.7356 0.0321 -0.0622 0.1374 218 TRP B C 4526 O O . TRP B 218 ? 1.0473 1.0675 0.8241 0.0408 -0.0834 0.1339 218 TRP B O 4527 C CB . TRP B 218 ? 0.9541 0.9959 0.7666 0.0275 -0.0457 0.0940 218 TRP B CB 4528 C CG . TRP B 218 ? 0.9402 0.9871 0.7857 0.0231 -0.0338 0.0767 218 TRP B CG 4529 C CD1 . TRP B 218 ? 0.9320 0.9903 0.7999 0.0281 -0.0421 0.0545 218 TRP B CD1 4530 C CD2 . TRP B 218 ? 0.9234 0.9632 0.7833 0.0125 -0.0132 0.0813 218 TRP B CD2 4531 N NE1 . TRP B 218 ? 0.9042 0.9634 0.7975 0.0216 -0.0279 0.0466 218 TRP B NE1 4532 C CE2 . TRP B 218 ? 0.9045 0.9531 0.7927 0.0120 -0.0106 0.0619 218 TRP B CE2 4533 C CE3 . TRP B 218 ? 0.9422 0.9684 0.7943 0.0030 0.0022 0.1000 218 TRP B CE3 4534 C CZ2 . TRP B 218 ? 0.8942 0.9395 0.8001 0.0025 0.0057 0.0606 218 TRP B CZ2 4535 C CZ3 . TRP B 218 ? 0.9783 1.0008 0.8500 -0.0068 0.0186 0.0968 218 TRP B CZ3 4536 C CH2 . TRP B 218 ? 0.9398 0.9725 0.8367 -0.0069 0.0197 0.0771 218 TRP B CH2 4537 N N . ASN B 219 ? 0.9052 0.9038 0.6826 0.0245 -0.0484 0.1597 219 ASN B N 4538 C CA . ASN B 219 ? 0.9456 0.9368 0.6857 0.0258 -0.0561 0.1842 219 ASN B CA 4539 C C . ASN B 219 ? 0.9715 0.9781 0.6641 0.0179 -0.0405 0.1858 219 ASN B C 4540 O O . ASN B 219 ? 1.0295 1.0317 0.7192 0.0065 -0.0180 0.1950 219 ASN B O 4541 C CB . ASN B 219 ? 1.0461 1.0089 0.8052 0.0227 -0.0511 0.2099 219 ASN B CB 4542 C CG . ASN B 219 ? 1.1059 1.0572 0.8303 0.0240 -0.0601 0.2399 219 ASN B CG 4543 O OD1 . ASN B 219 ? 1.0989 1.0635 0.7817 0.0277 -0.0720 0.2424 219 ASN B OD1 4544 N ND2 . ASN B 219 ? 1.1586 1.0835 0.8999 0.0211 -0.0548 0.2629 219 ASN B ND2 4545 N N . CYS B 220 ? 0.9736 0.9988 0.6302 0.0237 -0.0521 0.1755 220 CYS B N 4546 C CA . CYS B 220 ? 0.9871 1.0318 0.5994 0.0177 -0.0358 0.1711 220 CYS B CA 4547 C C . CYS B 220 ? 1.1907 1.2278 0.7571 0.0127 -0.0310 0.2019 220 CYS B C 4548 O O . CYS B 220 ? 1.3958 1.4383 0.9191 0.0185 -0.0462 0.2080 220 CYS B O 4549 C CB . CYS B 220 ? 0.9607 1.0280 0.5515 0.0265 -0.0490 0.1443 220 CYS B CB 4550 S SG . CYS B 220 ? 1.0121 1.0905 0.6537 0.0308 -0.0513 0.1079 220 CYS B SG 4551 N N . THR B 221 ? 1.2572 1.2813 0.8325 0.0012 -0.0102 0.2215 221 THR B N 4552 C CA . THR B 221 ? 1.3725 1.3900 0.9069 -0.0067 0.0000 0.2520 221 THR B CA 4553 C C . THR B 221 ? 1.4361 1.4670 0.9669 -0.0209 0.0322 0.2494 221 THR B C 4554 O O . THR B 221 ? 1.3820 1.4259 0.9434 -0.0231 0.0430 0.2245 221 THR B O 4555 C CB . THR B 221 ? 1.3558 1.3402 0.9087 -0.0079 -0.0071 0.2833 221 THR B CB 4556 O OG1 . THR B 221 ? 1.3475 1.3179 0.9500 -0.0153 0.0076 0.2797 221 THR B OG1 4557 C CG2 . THR B 221 ? 1.3097 1.2835 0.8750 0.0068 -0.0392 0.2848 221 THR B CG2 4558 N N . CYS B 222 ? 1.5355 1.5643 1.0310 -0.0306 0.0471 0.2758 222 CYS B N 4559 C CA . CYS B 222 ? 1.6038 1.6459 1.0994 -0.0455 0.0785 0.2770 222 CYS B CA 4560 C C . CYS B 222 ? 1.6152 1.6446 1.1685 -0.0537 0.0890 0.2710 222 CYS B C 4561 O O . CYS B 222 ? 1.6073 1.6538 1.1779 -0.0626 0.1092 0.2568 222 CYS B O 4562 C CB . CYS B 222 ? 1.6320 1.6667 1.0879 -0.0561 0.0916 0.3131 222 CYS B CB 4563 S SG . CYS B 222 ? 2.0244 2.0816 1.4013 -0.0510 0.0893 0.3193 222 CYS B SG 4564 N N . ASP B 223 ? 1.6115 1.6113 1.1947 -0.0500 0.0742 0.2810 223 ASP B N 4565 C CA . ASP B 223 ? 1.6030 1.5867 1.2380 -0.0562 0.0808 0.2744 223 ASP B CA 4566 C C . ASP B 223 ? 1.4637 1.4652 1.1290 -0.0511 0.0789 0.2388 223 ASP B C 4567 O O . ASP B 223 ? 1.4175 1.4126 1.1208 -0.0575 0.0871 0.2290 223 ASP B O 4568 C CB . ASP B 223 ? 1.7347 1.6831 1.3904 -0.0507 0.0646 0.2927 223 ASP B CB 4569 C CG . ASP B 223 ? 1.9363 1.8739 1.6410 -0.0456 0.0578 0.2727 223 ASP B CG 4570 O OD1 . ASP B 223 ? 2.0036 1.9275 1.7386 -0.0557 0.0711 0.2717 223 ASP B OD1 4571 O OD2 . ASP B 223 ? 2.0343 1.9771 1.7467 -0.0321 0.0390 0.2583 223 ASP B OD2 4572 N N . LEU B 224 ? 1.3758 1.3993 1.0227 -0.0401 0.0678 0.2197 224 LEU B N 4573 C CA . LEU B 224 ? 1.2456 1.2872 0.9188 -0.0351 0.0659 0.1871 224 LEU B CA 4574 C C . LEU B 224 ? 1.2198 1.2931 0.8782 -0.0399 0.0839 0.1711 224 LEU B C 4575 O O . LEU B 224 ? 1.2066 1.2977 0.8824 -0.0348 0.0822 0.1442 224 LEU B O 4576 C CB . LEU B 224 ? 1.1138 1.1570 0.7863 -0.0191 0.0400 0.1734 224 LEU B CB 4577 C CG . LEU B 224 ? 0.9532 1.0077 0.6588 -0.0123 0.0325 0.1429 224 LEU B CG 4578 C CD1 . LEU B 224 ? 1.0599 1.0954 0.7968 -0.0038 0.0129 0.1428 224 LEU B CD1 4579 C CD2 . LEU B 224 ? 0.8708 0.9510 0.5517 -0.0042 0.0261 0.1216 224 LEU B CD2 4580 N N . LEU B 225 ? 1.2382 1.3191 0.8669 -0.0495 0.1018 0.1881 225 LEU B N 4581 C CA . LEU B 225 ? 1.2525 1.3659 0.8686 -0.0538 0.1215 0.1737 225 LEU B CA 4582 C C . LEU B 225 ? 1.0897 1.2161 0.7498 -0.0613 0.1358 0.1557 225 LEU B C 4583 O O . LEU B 225 ? 0.9785 1.1311 0.6434 -0.0564 0.1398 0.1310 225 LEU B O 4584 C CB . LEU B 225 ? 1.4381 1.5568 1.0153 -0.0642 0.1405 0.1989 225 LEU B CB 4585 C CG . LEU B 225 ? 1.6165 1.7382 1.1365 -0.0554 0.1300 0.2082 225 LEU B CG 4586 C CD1 . LEU B 225 ? 1.7301 1.8582 1.2088 -0.0667 0.1510 0.2350 225 LEU B CD1 4587 C CD2 . LEU B 225 ? 1.6362 1.7833 1.1410 -0.0423 0.1223 0.1759 225 LEU B CD2 4588 N N . PRO B 226 ? 1.1189 1.2272 0.8112 -0.0730 0.1424 0.1671 226 PRO B N 4589 C CA . PRO B 226 ? 1.1030 1.2263 0.8331 -0.0814 0.1552 0.1512 226 PRO B CA 4590 C C . PRO B 226 ? 1.1335 1.2704 0.8863 -0.0701 0.1435 0.1210 226 PRO B C 4591 O O . PRO B 226 ? 1.1855 1.3507 0.9467 -0.0697 0.1533 0.1031 226 PRO B O 4592 C CB . PRO B 226 ? 1.0743 1.1683 0.8336 -0.0920 0.1550 0.1648 226 PRO B CB 4593 C CG . PRO B 226 ? 1.1382 1.2078 0.8719 -0.0940 0.1528 0.1936 226 PRO B CG 4594 C CD . PRO B 226 ? 1.1569 1.2304 0.8556 -0.0785 0.1372 0.1922 226 PRO B CD 4595 N N . LEU B 227 ? 1.0783 1.1950 0.8426 -0.0608 0.1232 0.1168 227 LEU B N 4596 C CA . LEU B 227 ? 0.9350 1.0599 0.7195 -0.0495 0.1092 0.0915 227 LEU B CA 4597 C C . LEU B 227 ? 0.8616 1.0149 0.6267 -0.0405 0.1101 0.0729 227 LEU B C 4598 O O . LEU B 227 ? 0.8623 1.0360 0.6486 -0.0392 0.1152 0.0527 227 LEU B O 4599 C CB . LEU B 227 ? 0.8639 0.9648 0.6523 -0.0396 0.0875 0.0945 227 LEU B CB 4600 C CG . LEU B 227 ? 0.8179 0.9246 0.6242 -0.0272 0.0706 0.0716 227 LEU B CG 4601 C CD1 . LEU B 227 ? 0.7712 0.8858 0.6146 -0.0312 0.0755 0.0557 227 LEU B CD1 4602 C CD2 . LEU B 227 ? 0.8091 0.8922 0.6227 -0.0196 0.0516 0.0788 227 LEU B CD2 4603 N N . LYS B 228 ? 0.8022 0.9561 0.5265 -0.0342 0.1049 0.0799 228 LYS B N 4604 C CA . LYS B 228 ? 0.9807 1.1599 0.6777 -0.0258 0.1069 0.0625 228 LYS B CA 4605 C C . LYS B 228 ? 1.1170 1.3245 0.8217 -0.0327 0.1314 0.0530 228 LYS B C 4606 O O . LYS B 228 ? 1.1643 1.3920 0.8849 -0.0257 0.1320 0.0274 228 LYS B O 4607 C CB . LYS B 228 ? 1.0690 1.2441 0.7129 -0.0229 0.1031 0.0786 228 LYS B CB 4608 C CG . LYS B 228 ? 1.0670 1.2687 0.6723 -0.0164 0.1100 0.0629 228 LYS B CG 4609 C CD . LYS B 228 ? 0.9476 1.1578 0.5632 -0.0021 0.0924 0.0310 228 LYS B CD 4610 C CE . LYS B 228 ? 0.9108 1.1407 0.4784 0.0060 0.0941 0.0162 228 LYS B CE 4611 N NZ . LYS B 228 ? 0.9201 1.1768 0.4723 -0.0004 0.1247 0.0137 228 LYS B NZ 4612 N N . ALA B 229 ? 1.1910 1.3998 0.8894 -0.0465 0.1512 0.0739 229 ALA B N 4613 C CA . ALA B 229 ? 1.2560 1.4936 0.9656 -0.0545 0.1760 0.0675 229 ALA B CA 4614 C C . ALA B 229 ? 1.1722 1.4182 0.9342 -0.0551 0.1745 0.0485 229 ALA B C 4615 O O . ALA B 229 ? 1.1205 1.3941 0.8970 -0.0508 0.1830 0.0277 229 ALA B O 4616 C CB . ALA B 229 ? 1.3565 1.5899 1.0585 -0.0713 0.1955 0.0957 229 ALA B CB 4617 N N . TRP B 230 ? 1.1712 1.3929 0.9611 -0.0596 0.1630 0.0555 230 TRP B N 4618 C CA . TRP B 230 ? 1.1180 1.3445 0.9542 -0.0617 0.1600 0.0410 230 TRP B CA 4619 C C . TRP B 230 ? 1.0872 1.3253 0.9356 -0.0464 0.1465 0.0143 230 TRP B C 4620 O O . TRP B 230 ? 1.0365 1.2886 0.9199 -0.0459 0.1469 -0.0009 230 TRP B O 4621 C CB . TRP B 230 ? 1.1074 1.3030 0.9632 -0.0682 0.1492 0.0527 230 TRP B CB 4622 C CG . TRP B 230 ? 1.1468 1.3458 1.0443 -0.0704 0.1443 0.0389 230 TRP B CG 4623 C CD1 . TRP B 230 ? 1.2060 1.4177 1.1310 -0.0825 0.1555 0.0384 230 TRP B CD1 4624 C CD2 . TRP B 230 ? 1.0967 1.2868 1.0130 -0.0606 0.1259 0.0248 230 TRP B CD2 4625 N NE1 . TRP B 230 ? 1.1502 1.3610 1.1069 -0.0805 0.1441 0.0251 230 TRP B NE1 4626 C CE2 . TRP B 230 ? 1.0913 1.2886 1.0426 -0.0673 0.1269 0.0172 230 TRP B CE2 4627 C CE3 . TRP B 230 ? 1.1363 1.3136 1.0443 -0.0476 0.1083 0.0188 230 TRP B CE3 4628 C CZ2 . TRP B 230 ? 1.1080 1.2990 1.0826 -0.0613 0.1119 0.0054 230 TRP B CZ2 4629 C CZ3 . TRP B 230 ? 1.1256 1.2973 1.0606 -0.0422 0.0947 0.0065 230 TRP B CZ3 4630 C CH2 . TRP B 230 ? 1.0965 1.2746 1.0626 -0.0490 0.0970 0.0006 230 TRP B CH2 4631 N N . LEU B 231 ? 1.0910 1.3228 0.9113 -0.0342 0.1335 0.0091 231 LEU B N 4632 C CA . LEU B 231 ? 1.1374 1.3761 0.9700 -0.0201 0.1187 -0.0161 231 LEU B CA 4633 C C . LEU B 231 ? 1.2153 1.4859 1.0447 -0.0140 0.1314 -0.0367 231 LEU B C 4634 O O . LEU B 231 ? 1.1351 1.4146 0.9855 -0.0036 0.1226 -0.0598 231 LEU B O 4635 C CB . LEU B 231 ? 1.1764 1.3970 0.9842 -0.0099 0.0983 -0.0156 231 LEU B CB 4636 C CG . LEU B 231 ? 1.1977 1.3886 1.0218 -0.0120 0.0830 -0.0020 231 LEU B CG 4637 C CD1 . LEU B 231 ? 1.3045 1.4812 1.1086 -0.0016 0.0624 -0.0016 231 LEU B CD1 4638 C CD2 . LEU B 231 ? 1.1440 1.3326 1.0131 -0.0121 0.0771 -0.0133 231 LEU B CD2 4639 N N . ASP B 232 ? 1.4168 1.7044 1.2218 -0.0204 0.1529 -0.0284 232 ASP B N 4640 C CA . ASP B 232 ? 1.4488 1.7691 1.2537 -0.0151 0.1692 -0.0482 232 ASP B CA 4641 C C . ASP B 232 ? 1.4255 1.7645 1.2788 -0.0227 0.1822 -0.0522 232 ASP B C 4642 O O . ASP B 232 ? 1.4520 1.8115 1.3326 -0.0144 0.1839 -0.0751 232 ASP B O 4643 C CB . ASP B 232 ? 1.5700 1.9036 1.3261 -0.0185 0.1887 -0.0380 232 ASP B CB 4644 C CG . ASP B 232 ? 1.6564 1.9745 1.3618 -0.0100 0.1738 -0.0356 232 ASP B CG 4645 O OD1 . ASP B 232 ? 1.6432 1.9329 1.3476 -0.0095 0.1528 -0.0239 232 ASP B OD1 4646 O OD2 . ASP B 232 ? 1.7272 2.0623 1.3941 -0.0036 0.1827 -0.0462 232 ASP B OD2 4647 N N . THR B 233 ? 1.3858 1.7164 1.2512 -0.0382 0.1897 -0.0302 233 THR B N 4648 C CA . THR B 233 ? 1.3682 1.7155 1.2793 -0.0477 0.2000 -0.0312 233 THR B CA 4649 C C . THR B 233 ? 1.3836 1.7245 1.3364 -0.0420 0.1808 -0.0455 233 THR B C 4650 O O . THR B 233 ? 1.3652 1.7283 1.3562 -0.0412 0.1851 -0.0583 233 THR B O 4651 C CB . THR B 233 ? 1.3340 1.6686 1.2479 -0.0666 0.2087 -0.0047 233 THR B CB 4652 O OG1 . THR B 233 ? 1.2610 1.5623 1.1828 -0.0690 0.1890 0.0036 233 THR B OG1 4653 C CG2 . THR B 233 ? 1.3979 1.7296 1.2659 -0.0724 0.2234 0.0149 233 THR B CG2 4654 N N . ILE B 234 ? 1.4958 1.8068 1.4425 -0.0380 0.1597 -0.0422 234 ILE B N 4655 C CA . ILE B 234 ? 1.6017 1.9042 1.5832 -0.0327 0.1413 -0.0534 234 ILE B CA 4656 C C . ILE B 234 ? 1.6256 1.9450 1.6183 -0.0168 0.1357 -0.0790 234 ILE B C 4657 O O . ILE B 234 ? 1.6316 1.9571 1.5954 -0.0074 0.1382 -0.0886 234 ILE B O 4658 C CB . ILE B 234 ? 1.3818 1.6493 1.3536 -0.0318 0.1222 -0.0436 234 ILE B CB 4659 C CG1 . ILE B 234 ? 1.2689 1.5277 1.2768 -0.0296 0.1063 -0.0510 234 ILE B CG1 4660 C CG2 . ILE B 234 ? 1.4366 1.6951 1.3776 -0.0194 0.1117 -0.0493 234 ILE B CG2 4661 C CD1 . ILE B 234 ? 1.2573 1.5278 1.2986 -0.0400 0.1121 -0.0495 234 ILE B CD1 4662 N N . THR B 235 ? 1.6082 1.9348 1.6430 -0.0139 0.1280 -0.0902 235 THR B N 4663 C CA . THR B 235 ? 1.6653 2.0050 1.7191 0.0013 0.1210 -0.1144 235 THR B CA 4664 C C . THR B 235 ? 1.7335 2.0508 1.8065 0.0071 0.0971 -0.1180 235 THR B C 4665 O O . THR B 235 ? 1.7928 2.0891 1.8685 -0.0013 0.0886 -0.1024 235 THR B O 4666 C CB . THR B 235 ? 1.6622 2.0331 1.7551 0.0014 0.1328 -0.1252 235 THR B CB 4667 O OG1 . THR B 235 ? 1.6178 1.9834 1.7480 -0.0057 0.1225 -0.1179 235 THR B OG1 4668 C CG2 . THR B 235 ? 1.6920 2.0857 1.7722 -0.0082 0.1587 -0.1169 235 THR B CG2 4669 N N . VAL B 236 ? 1.7485 2.0702 1.8355 0.0213 0.0872 -0.1389 236 VAL B N 4670 C CA . VAL B 236 ? 1.7402 2.0428 1.8496 0.0276 0.0651 -0.1435 236 VAL B CA 4671 C C . VAL B 236 ? 1.7139 1.9876 1.7977 0.0251 0.0528 -0.1307 236 VAL B C 4672 O O . VAL B 236 ? 1.6582 1.9135 1.7592 0.0237 0.0387 -0.1243 236 VAL B O 4673 C CB . VAL B 236 ? 2.0941 2.3975 2.2445 0.0216 0.0595 -0.1368 236 VAL B CB 4674 C CG1 . VAL B 236 ? 2.0661 2.3591 2.2466 0.0313 0.0399 -0.1470 236 VAL B CG1 4675 C CG2 . VAL B 236 ? 2.0984 2.4322 2.2730 0.0194 0.0745 -0.1421 236 VAL B CG2 4676 N N . PHE B 237 ? 1.7397 2.0104 1.7832 0.0249 0.0585 -0.1265 237 PHE B N 4677 C CA . PHE B 237 ? 1.6981 1.9435 1.7197 0.0237 0.0466 -0.1142 237 PHE B CA 4678 C C . PHE B 237 ? 1.5886 1.8267 1.6049 0.0363 0.0296 -0.1299 237 PHE B C 4679 O O . PHE B 237 ? 1.5985 1.8503 1.6009 0.0449 0.0319 -0.1478 237 PHE B O 4680 C CB . PHE B 237 ? 1.7628 2.0058 1.7444 0.0162 0.0588 -0.0975 237 PHE B CB 4681 C CG . PHE B 237 ? 1.7910 2.0106 1.7501 0.0173 0.0460 -0.0862 237 PHE B CG 4682 C CD1 . PHE B 237 ? 1.7731 1.9716 1.7403 0.0096 0.0418 -0.0680 237 PHE B CD1 4683 C CD2 . PHE B 237 ? 1.8117 2.0308 1.7423 0.0264 0.0375 -0.0945 237 PHE B CD2 4684 C CE1 . PHE B 237 ? 1.7685 1.9469 1.7205 0.0116 0.0304 -0.0577 237 PHE B CE1 4685 C CE2 . PHE B 237 ? 1.8105 2.0098 1.7249 0.0277 0.0237 -0.0834 237 PHE B CE2 4686 C CZ . PHE B 237 ? 1.7838 1.9633 1.7113 0.0206 0.0206 -0.0646 237 PHE B CZ 4687 N N . VAL B 238 ? 1.5614 1.7781 1.5889 0.0369 0.0128 -0.1237 238 VAL B N 4688 C CA . VAL B 238 ? 1.5570 1.7645 1.5814 0.0468 -0.0054 -0.1359 238 VAL B CA 4689 C C . VAL B 238 ? 1.5969 1.7828 1.6114 0.0433 -0.0159 -0.1184 238 VAL B C 4690 O O . VAL B 238 ? 1.6624 1.8365 1.6897 0.0353 -0.0134 -0.1015 238 VAL B O 4691 C CB . VAL B 238 ? 1.5266 1.7325 1.5924 0.0539 -0.0187 -0.1520 238 VAL B CB 4692 C CG1 . VAL B 238 ? 1.5396 1.7367 1.6038 0.0633 -0.0380 -0.1664 238 VAL B CG1 4693 C CG2 . VAL B 238 ? 1.5306 1.7575 1.6136 0.0583 -0.0089 -0.1687 238 VAL B CG2 4694 N N . GLY B 239 ? 1.4981 1.6795 1.4901 0.0495 -0.0277 -0.1232 239 GLY B N 4695 C CA . GLY B 239 ? 1.3653 1.5283 1.3525 0.0481 -0.0396 -0.1079 239 GLY B CA 4696 C C . GLY B 239 ? 1.3036 1.4669 1.2472 0.0502 -0.0421 -0.1029 239 GLY B C 4697 O O . GLY B 239 ? 1.3430 1.5200 1.2552 0.0501 -0.0299 -0.1065 239 GLY B O 4698 N N . GLU B 240 ? 1.1762 1.3253 1.1182 0.0521 -0.0580 -0.0937 240 GLU B N 4699 C CA . GLU B 240 ? 1.1750 1.3229 1.0757 0.0544 -0.0638 -0.0862 240 GLU B CA 4700 C C . GLU B 240 ? 1.1417 1.2753 1.0347 0.0477 -0.0585 -0.0581 240 GLU B C 4701 O O . GLU B 240 ? 1.1735 1.2940 1.0974 0.0444 -0.0598 -0.0476 240 GLU B O 4702 C CB . GLU B 240 ? 1.3125 1.4570 1.2147 0.0632 -0.0897 -0.0989 240 GLU B CB 4703 C CG . GLU B 240 ? 1.3890 1.5193 1.3333 0.0637 -0.1052 -0.0930 240 GLU B CG 4704 C CD . GLU B 240 ? 1.5055 1.6342 1.4527 0.0714 -0.1320 -0.1054 240 GLU B CD 4705 O OE1 . GLU B 240 ? 1.5792 1.7143 1.4865 0.0757 -0.1400 -0.1125 240 GLU B OE1 4706 O OE2 . GLU B 240 ? 1.4683 1.5898 1.4572 0.0725 -0.1451 -0.1080 240 GLU B OE2 4707 N N . ILE B 241 ? 1.1779 1.3137 1.0290 0.0457 -0.0517 -0.0461 241 ILE B N 4708 C CA . ILE B 241 ? 1.1616 1.2825 1.0023 0.0400 -0.0474 -0.0189 241 ILE B CA 4709 C C . ILE B 241 ? 1.2120 1.3302 1.0156 0.0454 -0.0625 -0.0108 241 ILE B C 4710 O O . ILE B 241 ? 1.2766 1.4037 1.0370 0.0443 -0.0548 -0.0073 241 ILE B O 4711 C CB . ILE B 241 ? 1.1764 1.3004 1.0034 0.0296 -0.0220 -0.0062 241 ILE B CB 4712 C CG1 . ILE B 241 ? 1.1855 1.3141 1.0479 0.0242 -0.0095 -0.0150 241 ILE B CG1 4713 C CG2 . ILE B 241 ? 1.2059 1.3112 1.0251 0.0238 -0.0184 0.0215 241 ILE B CG2 4714 C CD1 . ILE B 241 ? 1.2560 1.4072 1.1150 0.0258 -0.0001 -0.0353 241 ILE B CD1 4715 N N . VAL B 242 ? 1.1622 1.2695 0.9830 0.0511 -0.0843 -0.0074 242 VAL B N 4716 C CA . VAL B 242 ? 1.1330 1.2386 0.9225 0.0572 -0.1041 -0.0012 242 VAL B CA 4717 C C . VAL B 242 ? 1.0506 1.1401 0.8294 0.0543 -0.1035 0.0295 242 VAL B C 4718 O O . VAL B 242 ? 1.0404 1.1157 0.8534 0.0514 -0.0989 0.0423 242 VAL B O 4719 C CB . VAL B 242 ? 1.2245 1.3292 1.0412 0.0655 -0.1316 -0.0155 242 VAL B CB 4720 C CG1 . VAL B 242 ? 1.2311 1.3504 1.0487 0.0695 -0.1357 -0.0466 242 VAL B CG1 4721 C CG2 . VAL B 242 ? 1.2821 1.3744 1.1541 0.0642 -0.1332 -0.0086 242 VAL B CG2 4722 N N . CYS B 243 ? 1.0984 1.1897 0.8288 0.0553 -0.1078 0.0412 243 CYS B N 4723 C CA . CYS B 243 ? 1.1391 1.2142 0.8568 0.0531 -0.1087 0.0722 243 CYS B CA 4724 C C . CYS B 243 ? 1.1316 1.1944 0.8796 0.0605 -0.1339 0.0803 243 CYS B C 4725 O O . CYS B 243 ? 1.3038 1.3728 1.0448 0.0683 -0.1590 0.0710 243 CYS B O 4726 C CB . CYS B 243 ? 1.2279 1.3087 0.8833 0.0526 -0.1089 0.0840 243 CYS B CB 4727 S SG . CYS B 243 ? 1.4258 1.5251 1.0438 0.0442 -0.0775 0.0754 243 CYS B SG 4728 N N . GLU B 244 ? 1.0766 1.1225 0.8603 0.0581 -0.1272 0.0966 244 GLU B N 4729 C CA . GLU B 244 ? 1.0812 1.1152 0.8967 0.0652 -0.1476 0.1082 244 GLU B CA 4730 C C . GLU B 244 ? 1.1007 1.1245 0.8831 0.0674 -0.1582 0.1354 244 GLU B C 4731 O O . GLU B 244 ? 1.1145 1.1374 0.9001 0.0757 -0.1848 0.1416 244 GLU B O 4732 C CB . GLU B 244 ? 1.1537 1.1736 1.0201 0.0623 -0.1338 0.1130 244 GLU B CB 4733 C CG . GLU B 244 ? 1.2499 1.2562 1.1520 0.0694 -0.1491 0.1282 244 GLU B CG 4734 C CD . GLU B 244 ? 1.2867 1.2966 1.2434 0.0731 -0.1548 0.1132 244 GLU B CD 4735 O OE1 . GLU B 244 ? 1.3397 1.3649 1.3010 0.0747 -0.1642 0.0919 244 GLU B OE1 4736 O OE2 . GLU B 244 ? 1.2684 1.2653 1.2640 0.0744 -0.1490 0.1227 244 GLU B OE2 4737 N N . THR B 245 ? 1.1348 1.1517 0.8866 0.0596 -0.1380 0.1523 245 THR B N 4738 C CA . THR B 245 ? 1.1012 1.1058 0.8203 0.0598 -0.1439 0.1821 245 THR B CA 4739 C C . THR B 245 ? 1.1267 1.1418 0.7854 0.0527 -0.1295 0.1853 245 THR B C 4740 O O . THR B 245 ? 1.1218 1.1451 0.7781 0.0445 -0.1048 0.1738 245 THR B O 4741 C CB . THR B 245 ? 1.1379 1.1177 0.8872 0.0560 -0.1306 0.2052 245 THR B CB 4742 O OG1 . THR B 245 ? 1.0779 1.0512 0.8861 0.0610 -0.1351 0.1961 245 THR B OG1 4743 C CG2 . THR B 245 ? 1.2684 1.2320 0.9969 0.0593 -0.1438 0.2378 245 THR B CG2 4744 N N . PRO B 246 ? 1.2169 1.2335 0.8268 0.0559 -0.1447 0.2010 246 PRO B N 4745 C CA . PRO B 246 ? 1.2482 1.2577 0.8536 0.0657 -0.1772 0.2159 246 PRO B CA 4746 C C . PRO B 246 ? 1.2590 1.2868 0.8508 0.0743 -0.2043 0.1921 246 PRO B C 4747 O O . PRO B 246 ? 1.2530 1.2978 0.8419 0.0732 -0.1971 0.1623 246 PRO B O 4748 C CB . PRO B 246 ? 1.3152 1.3167 0.8656 0.0615 -0.1741 0.2474 246 PRO B CB 4749 C CG . PRO B 246 ? 1.3369 1.3548 0.8445 0.0524 -0.1480 0.2357 246 PRO B CG 4750 C CD . PRO B 246 ? 1.2642 1.2882 0.8165 0.0477 -0.1261 0.2106 246 PRO B CD 4751 N N . PHE B 247 ? 1.2179 1.2417 0.8033 0.0827 -0.2362 0.2053 247 PHE B N 4752 C CA . PHE B 247 ? 1.1982 1.2370 0.7762 0.0908 -0.2673 0.1840 247 PHE B CA 4753 C C . PHE B 247 ? 1.2165 1.2739 0.7311 0.0886 -0.2638 0.1636 247 PHE B C 4754 O O . PHE B 247 ? 1.1839 1.2556 0.7032 0.0923 -0.2754 0.1321 247 PHE B O 4755 C CB . PHE B 247 ? 1.2486 1.2798 0.8226 0.0992 -0.3027 0.2070 247 PHE B CB 4756 C CG . PHE B 247 ? 1.3401 1.3865 0.9045 0.1067 -0.3381 0.1861 247 PHE B CG 4757 C CD1 . PHE B 247 ? 1.3555 1.4059 0.9834 0.1125 -0.3568 0.1688 247 PHE B CD1 4758 C CD2 . PHE B 247 ? 1.4809 1.5375 0.9724 0.1074 -0.3525 0.1833 247 PHE B CD2 4759 C CE1 . PHE B 247 ? 1.3661 1.4300 0.9887 0.1183 -0.3906 0.1489 247 PHE B CE1 4760 C CE2 . PHE B 247 ? 1.5517 1.6212 1.0335 0.1137 -0.3865 0.1618 247 PHE B CE2 4761 C CZ . PHE B 247 ? 1.4524 1.5251 1.0016 0.1190 -0.4064 0.1445 247 PHE B CZ 4762 N N . ARG B 248 ? 1.2147 1.2713 0.6707 0.0827 -0.2476 0.1819 248 ARG B N 4763 C CA . ARG B 248 ? 1.3074 1.3823 0.6995 0.0803 -0.2391 0.1642 248 ARG B CA 4764 C C . ARG B 248 ? 1.2492 1.3384 0.6632 0.0772 -0.2157 0.1293 248 ARG B C 4765 O O . ARG B 248 ? 1.2332 1.3387 0.6246 0.0808 -0.2221 0.0990 248 ARG B O 4766 C CB . ARG B 248 ? 1.4822 1.5533 0.8161 0.0725 -0.2185 0.1936 248 ARG B CB 4767 C CG . ARG B 248 ? 1.6851 1.7488 0.9693 0.0763 -0.2449 0.2226 248 ARG B CG 4768 C CD . ARG B 248 ? 1.8682 1.9327 1.0850 0.0676 -0.2219 0.2471 248 ARG B CD 4769 N NE . ARG B 248 ? 2.0397 2.1043 1.1899 0.0714 -0.2479 0.2661 248 ARG B NE 4770 C CZ . ARG B 248 ? 2.1769 2.2443 1.2557 0.0649 -0.2335 0.2875 248 ARG B CZ 4771 N NH1 . ARG B 248 ? 2.1654 2.2370 1.2350 0.0539 -0.1926 0.2923 248 ARG B NH1 4772 N NH2 . ARG B 248 ? 2.2879 2.3542 1.3055 0.0688 -0.2600 0.3045 248 ARG B NH2 4773 N N . LEU B 249 ? 1.2541 1.3362 0.7133 0.0710 -0.1899 0.1331 249 LEU B N 4774 C CA . LEU B 249 ? 1.2978 1.3926 0.7789 0.0674 -0.1665 0.1046 249 LEU B CA 4775 C C . LEU B 249 ? 1.3221 1.4152 0.8700 0.0719 -0.1775 0.0835 249 LEU B C 4776 O O . LEU B 249 ? 1.3232 1.4243 0.8976 0.0694 -0.1606 0.0619 249 LEU B O 4777 C CB . LEU B 249 ? 1.3529 1.4434 0.8393 0.0564 -0.1310 0.1205 249 LEU B CB 4778 C CG . LEU B 249 ? 1.3854 1.4802 0.8078 0.0500 -0.1149 0.1407 249 LEU B CG 4779 C CD1 . LEU B 249 ? 1.4386 1.5278 0.8751 0.0380 -0.0816 0.1575 249 LEU B CD1 4780 C CD2 . LEU B 249 ? 1.3346 1.4532 0.7078 0.0524 -0.1106 0.1146 249 LEU B CD2 4781 N N . HIS B 250 ? 1.4067 1.4900 0.9823 0.0785 -0.2058 0.0912 250 HIS B N 4782 C CA . HIS B 250 ? 1.4161 1.4984 1.0549 0.0829 -0.2187 0.0737 250 HIS B CA 4783 C C . HIS B 250 ? 1.4208 1.5190 1.0648 0.0846 -0.2187 0.0364 250 HIS B C 4784 O O . HIS B 250 ? 1.5351 1.6448 1.1380 0.0883 -0.2318 0.0195 250 HIS B O 4785 C CB . HIS B 250 ? 1.4772 1.5537 1.1319 0.0909 -0.2545 0.0834 250 HIS B CB 4786 C CG . HIS B 250 ? 1.6245 1.7023 1.3435 0.0952 -0.2696 0.0659 250 HIS B CG 4787 N ND1 . HIS B 250 ? 1.6864 1.7681 1.4192 0.1024 -0.3048 0.0596 250 HIS B ND1 4788 C CD2 . HIS B 250 ? 1.6664 1.7425 1.4399 0.0926 -0.2546 0.0549 250 HIS B CD2 4789 C CE1 . HIS B 250 ? 1.7220 1.8048 1.5176 0.1037 -0.3093 0.0456 250 HIS B CE1 4790 N NE2 . HIS B 250 ? 1.6881 1.7671 1.5073 0.0979 -0.2789 0.0430 250 HIS B NE2 4791 N N . GLY B 251 ? 1.2832 1.3813 0.9766 0.0818 -0.2038 0.0236 251 GLY B N 4792 C CA . GLY B 251 ? 1.2941 1.4042 1.0041 0.0839 -0.2052 -0.0099 251 GLY B CA 4793 C C . GLY B 251 ? 1.3306 1.4536 1.0096 0.0804 -0.1803 -0.0258 251 GLY B C 4794 O O . GLY B 251 ? 1.2885 1.4186 0.9938 0.0808 -0.1733 -0.0497 251 GLY B O 4795 N N . LYS B 252 ? 1.3795 1.5059 1.0048 0.0770 -0.1665 -0.0116 252 LYS B N 4796 C CA . LYS B 252 ? 1.4602 1.6020 1.0539 0.0738 -0.1413 -0.0254 252 LYS B CA 4797 C C . LYS B 252 ? 1.4133 1.5558 1.0462 0.0669 -0.1139 -0.0257 252 LYS B C 4798 O O . LYS B 252 ? 1.4134 1.5434 1.0682 0.0608 -0.1039 -0.0025 252 LYS B O 4799 C CB . LYS B 252 ? 1.6555 1.8001 1.1852 0.0702 -0.1308 -0.0047 252 LYS B CB 4800 C CG . LYS B 252 ? 1.8248 1.9697 1.3058 0.0765 -0.1580 -0.0026 252 LYS B CG 4801 C CD . LYS B 252 ? 1.9362 2.0995 1.3723 0.0811 -0.1583 -0.0334 252 LYS B CD 4802 C CE . LYS B 252 ? 1.9784 2.1424 1.3521 0.0856 -0.1821 -0.0278 252 LYS B CE 4803 N NZ . LYS B 252 ? 1.9434 2.0961 1.3433 0.0917 -0.2209 -0.0265 252 LYS B NZ 4804 N N . ASP B 253 ? 1.4783 1.6351 1.1205 0.0683 -0.1027 -0.0527 253 ASP B N 4805 C CA . ASP B 253 ? 1.4249 1.5849 1.1033 0.0621 -0.0789 -0.0547 253 ASP B CA 4806 C C . ASP B 253 ? 1.3564 1.5254 1.0033 0.0540 -0.0502 -0.0409 253 ASP B C 4807 O O . ASP B 253 ? 1.3893 1.5751 0.9980 0.0556 -0.0398 -0.0528 253 ASP B O 4808 C CB . ASP B 253 ? 1.5191 1.6907 1.2241 0.0675 -0.0798 -0.0879 253 ASP B CB 4809 C CG . ASP B 253 ? 1.5679 1.7377 1.3246 0.0626 -0.0663 -0.0883 253 ASP B CG 4810 O OD1 . ASP B 253 ? 1.5879 1.7520 1.3511 0.0539 -0.0501 -0.0665 253 ASP B OD1 4811 O OD2 . ASP B 253 ? 1.6092 1.7824 1.3995 0.0671 -0.0727 -0.1104 253 ASP B OD2 4812 N N . VAL B 254 ? 1.2000 1.3577 0.8644 0.0451 -0.0370 -0.0165 254 VAL B N 4813 C CA . VAL B 254 ? 1.1794 1.3423 0.8197 0.0352 -0.0109 0.0016 254 VAL B CA 4814 C C . VAL B 254 ? 1.2392 1.4270 0.8705 0.0338 0.0112 -0.0176 254 VAL B C 4815 O O . VAL B 254 ? 1.2946 1.4941 0.8859 0.0296 0.0284 -0.0097 254 VAL B O 4816 C CB . VAL B 254 ? 1.1131 1.2604 0.7896 0.0256 -0.0001 0.0219 254 VAL B CB 4817 C CG1 . VAL B 254 ? 1.0908 1.2444 0.7501 0.0139 0.0272 0.0380 254 VAL B CG1 4818 C CG2 . VAL B 254 ? 1.1202 1.2433 0.8028 0.0271 -0.0179 0.0434 254 VAL B CG2 4819 N N . THR B 255 ? 1.2812 1.4773 0.9512 0.0376 0.0110 -0.0420 255 THR B N 4820 C CA . THR B 255 ? 1.3874 1.6079 1.0577 0.0385 0.0301 -0.0631 255 THR B CA 4821 C C . THR B 255 ? 1.5153 1.7515 1.1342 0.0455 0.0310 -0.0782 255 THR B C 4822 O O . THR B 255 ? 1.3922 1.6486 0.9895 0.0429 0.0546 -0.0823 255 THR B O 4823 C CB . THR B 255 ? 1.3314 1.5552 1.0520 0.0442 0.0230 -0.0879 255 THR B CB 4824 O OG1 . THR B 255 ? 1.3334 1.5480 1.0571 0.0543 -0.0038 -0.1031 255 THR B OG1 4825 C CG2 . THR B 255 ? 1.2566 1.4678 1.0232 0.0363 0.0256 -0.0738 255 THR B CG2 4826 N N . GLN B 256 ? 1.7402 1.9677 1.3394 0.0542 0.0055 -0.0868 256 GLN B N 4827 C CA . GLN B 256 ? 1.8453 2.0850 1.3893 0.0610 0.0027 -0.1014 256 GLN B CA 4828 C C . GLN B 256 ? 1.8154 2.0556 1.3032 0.0542 0.0139 -0.0734 256 GLN B C 4829 O O . GLN B 256 ? 1.8681 2.1244 1.3055 0.0560 0.0255 -0.0811 256 GLN B O 4830 C CB . GLN B 256 ? 1.9985 2.2272 1.5381 0.0709 -0.0313 -0.1166 256 GLN B CB 4831 C CG . GLN B 256 ? 2.0882 2.3103 1.6873 0.0762 -0.0468 -0.1374 256 GLN B CG 4832 C CD . GLN B 256 ? 2.1930 2.3997 1.7973 0.0821 -0.0815 -0.1408 256 GLN B CD 4833 O OE1 . GLN B 256 ? 2.2635 2.4601 1.8402 0.0807 -0.0947 -0.1194 256 GLN B OE1 4834 N NE2 . GLN B 256 ? 2.2168 2.4215 1.8596 0.0886 -0.0970 -0.1666 256 GLN B NE2 4835 N N . LEU B 257 ? 1.5833 1.8049 1.0800 0.0465 0.0107 -0.0408 257 LEU B N 4836 C CA . LEU B 257 ? 1.4681 1.6842 0.9155 0.0401 0.0163 -0.0097 257 LEU B CA 4837 C C . LEU B 257 ? 1.4673 1.7001 0.8954 0.0301 0.0516 0.0012 257 LEU B C 4838 O O . LEU B 257 ? 1.4436 1.6919 0.9037 0.0274 0.0719 -0.0133 257 LEU B O 4839 C CB . LEU B 257 ? 1.3146 1.5041 0.7850 0.0354 0.0033 0.0211 257 LEU B CB 4840 C CG . LEU B 257 ? 1.2268 1.4002 0.6918 0.0440 -0.0318 0.0238 257 LEU B CG 4841 C CD1 . LEU B 257 ? 1.1502 1.2991 0.6332 0.0393 -0.0396 0.0575 257 LEU B CD1 4842 C CD2 . LEU B 257 ? 1.2750 1.4570 0.6732 0.0495 -0.0426 0.0204 257 LEU B CD2 4843 N N . THR B 258 ? 1.5054 1.7355 0.8826 0.0244 0.0582 0.0283 258 THR B N 4844 C CA . THR B 258 ? 1.4946 1.7410 0.8486 0.0138 0.0922 0.0423 258 THR B CA 4845 C C . THR B 258 ? 1.5254 1.7523 0.8768 0.0013 0.0984 0.0847 258 THR B C 4846 O O . THR B 258 ? 1.5904 1.7921 0.9440 0.0030 0.0752 0.1036 258 THR B O 4847 C CB . THR B 258 ? 1.5521 1.8185 0.8366 0.0179 0.1009 0.0333 258 THR B CB 4848 O OG1 . THR B 258 ? 1.6160 1.8663 0.8489 0.0200 0.0793 0.0549 258 THR B OG1 4849 C CG2 . THR B 258 ? 1.5732 1.8563 0.8602 0.0310 0.0936 -0.0111 258 THR B CG2 4850 N N . ARG B 259 ? 1.4883 1.7272 0.8382 -0.0111 0.1300 0.0991 259 ARG B N 4851 C CA . ARG B 259 ? 1.4183 1.6388 0.7721 -0.0247 0.1393 0.1381 259 ARG B CA 4852 C C . ARG B 259 ? 1.5056 1.7123 0.7991 -0.0250 0.1289 0.1680 259 ARG B C 4853 O O . ARG B 259 ? 1.5470 1.7286 0.8454 -0.0319 0.1238 0.2009 259 ARG B O 4854 C CB . ARG B 259 ? 1.4161 1.6564 0.7826 -0.0386 0.1761 0.1443 259 ARG B CB 4855 C CG . ARG B 259 ? 1.5125 1.7835 0.9061 -0.0342 0.1910 0.1076 259 ARG B CG 4856 C CD . ARG B 259 ? 1.6483 1.9271 1.0987 -0.0465 0.2121 0.1095 259 ARG B CD 4857 N NE . ARG B 259 ? 1.7536 2.0325 1.2597 -0.0397 0.1998 0.0822 259 ARG B NE 4858 C CZ . ARG B 259 ? 1.7842 2.0771 1.3403 -0.0462 0.2147 0.0725 259 ARG B CZ 4859 N NH1 . ARG B 259 ? 1.8136 2.1230 1.3747 -0.0600 0.2429 0.0864 259 ARG B NH1 4860 N NH2 . ARG B 259 ? 1.7235 2.0145 1.3252 -0.0393 0.2007 0.0498 259 ARG B NH2 4861 N N . GLN B 260 ? 1.5619 1.7844 0.7986 -0.0169 0.1249 0.1556 260 GLN B N 4862 C CA . GLN B 260 ? 1.6236 1.8371 0.7937 -0.0167 0.1148 0.1823 260 GLN B CA 4863 C C . GLN B 260 ? 1.6064 1.7984 0.7742 -0.0045 0.0732 0.1810 260 GLN B C 4864 O O . GLN B 260 ? 1.6538 1.8266 0.7916 -0.0050 0.0566 0.2119 260 GLN B O 4865 C CB . GLN B 260 ? 1.7028 1.9406 0.8116 -0.0145 0.1313 0.1676 260 GLN B CB 4866 C CG . GLN B 260 ? 1.7221 1.9774 0.8466 -0.0247 0.1724 0.1612 260 GLN B CG 4867 C CD . GLN B 260 ? 1.6772 1.9606 0.8510 -0.0202 0.1833 0.1243 260 GLN B CD 4868 O OE1 . GLN B 260 ? 1.6647 1.9505 0.8539 -0.0076 0.1608 0.0956 260 GLN B OE1 4869 N NE2 . GLN B 260 ? 1.6441 1.9416 0.8514 -0.0304 0.2154 0.1242 260 GLN B NE2 4870 N N . ASP B 261 ? 1.5879 1.7838 0.7911 0.0062 0.0563 0.1459 261 ASP B N 4871 C CA . ASP B 261 ? 1.5993 1.7763 0.8182 0.0169 0.0178 0.1422 261 ASP B CA 4872 C C . ASP B 261 ? 1.6053 1.7540 0.8726 0.0122 0.0097 0.1699 261 ASP B C 4873 O O . ASP B 261 ? 1.6758 1.8056 0.9513 0.0190 -0.0199 0.1797 261 ASP B O 4874 C CB . ASP B 261 ? 1.6506 1.8378 0.9061 0.0273 0.0056 0.0993 261 ASP B CB 4875 C CG . ASP B 261 ? 1.8008 2.0054 1.0056 0.0371 -0.0054 0.0712 261 ASP B CG 4876 O OD1 . ASP B 261 ? 1.8672 2.0662 1.0193 0.0408 -0.0256 0.0837 261 ASP B OD1 4877 O OD2 . ASP B 261 ? 1.8426 2.0660 1.0607 0.0414 0.0051 0.0360 261 ASP B OD2 4878 N N . LEU B 262 ? 1.5931 1.7397 0.8935 0.0006 0.0364 0.1810 262 LEU B N 4879 C CA . LEU B 262 ? 1.4597 1.5797 0.8100 -0.0045 0.0326 0.2020 262 LEU B CA 4880 C C . LEU B 262 ? 1.5996 1.7016 0.9272 -0.0147 0.0414 0.2448 262 LEU B C 4881 O O . LEU B 262 ? 1.5626 1.6377 0.9215 -0.0163 0.0318 0.2656 262 LEU B O 4882 C CB . LEU B 262 ? 1.2854 1.4115 0.6925 -0.0108 0.0525 0.1847 262 LEU B CB 4883 C CG . LEU B 262 ? 1.2684 1.3929 0.7227 -0.0008 0.0336 0.1557 262 LEU B CG 4884 C CD1 . LEU B 262 ? 1.1898 1.3297 0.6858 -0.0049 0.0525 0.1316 262 LEU B CD1 4885 C CD2 . LEU B 262 ? 1.3344 1.4295 0.8241 0.0010 0.0153 0.1731 262 LEU B CD2 4886 N N . CYS B 263 ? 1.8034 1.9194 1.0771 -0.0215 0.0602 0.2580 263 CYS B N 4887 C CA . CYS B 263 ? 1.9367 2.0356 1.1838 -0.0318 0.0685 0.3012 263 CYS B CA 4888 C C . CYS B 263 ? 1.3280 1.4296 0.5013 -0.0268 0.0547 0.3177 263 CYS B C 4889 O O . CYS B 263 ? 1.3685 1.4476 0.5221 -0.0287 0.0430 0.3541 263 CYS B O 4890 C CB . CYS B 263 ? 1.9025 2.0139 1.1539 -0.0483 0.1072 0.3103 263 CYS B CB 4891 S SG . CYS B 263 ? 2.3101 2.4156 1.6457 -0.0566 0.1218 0.2963 263 CYS B SG 4892 C C1 . NAG C . ? 1.4945 1.1121 1.6095 -0.1088 -0.3991 0.1521 501 NAG A C1 4893 C C2 . NAG C . ? 1.4547 1.0420 1.5760 -0.1021 -0.4246 0.1446 501 NAG A C2 4894 C C3 . NAG C . ? 1.4460 1.0176 1.6031 -0.1131 -0.4451 0.1721 501 NAG A C3 4895 C C4 . NAG C . ? 1.4278 0.9934 1.6113 -0.1229 -0.4519 0.1791 501 NAG A C4 4896 C C5 . NAG C . ? 1.4570 1.0568 1.6317 -0.1289 -0.4235 0.1869 501 NAG A C5 4897 C C6 . NAG C . ? 1.4052 1.0017 1.6036 -0.1377 -0.4280 0.1919 501 NAG A C6 4898 C C7 . NAG C . ? 1.5092 1.1039 1.5825 -0.0804 -0.4140 0.1118 501 NAG A C7 4899 C C8 . NAG C . ? 1.5429 1.1454 1.5974 -0.0733 -0.4097 0.1101 501 NAG A C8 4900 N N2 . NAG C . ? 1.4485 1.0424 1.5469 -0.0933 -0.4190 0.1385 501 NAG A N2 4901 O O3 . NAG C . ? 1.4613 1.0013 1.6242 -0.1056 -0.4714 0.1627 501 NAG A O3 4902 O O4 . NAG C . ? 1.3333 0.8863 1.5553 -0.1350 -0.4718 0.2081 501 NAG A O4 4903 O O5 . NAG C . ? 1.4470 1.0586 1.5864 -0.1178 -0.4052 0.1595 501 NAG A O5 4904 O O6 . NAG C . ? 1.2838 0.8442 1.4996 -0.1350 -0.4569 0.1779 501 NAG A O6 4905 O O7 . NAG C . ? 1.5313 1.1224 1.5986 -0.0745 -0.4129 0.0914 501 NAG A O7 4906 C C1 . NAG D . ? 1.4705 1.2835 1.3090 -0.0099 -0.3124 -0.0430 502 NAG A C1 4907 C C2 . NAG D . ? 1.4713 1.2874 1.2948 0.0005 -0.3241 -0.0480 502 NAG A C2 4908 C C3 . NAG D . ? 1.4845 1.2959 1.3253 -0.0027 -0.3378 -0.0594 502 NAG A C3 4909 C C4 . NAG D . ? 1.5152 1.3230 1.3718 -0.0074 -0.3415 -0.0710 502 NAG A C4 4910 C C5 . NAG D . ? 1.4801 1.2869 1.3493 -0.0168 -0.3275 -0.0639 502 NAG A C5 4911 C C6 . NAG D . ? 1.4145 1.2184 1.3000 -0.0217 -0.3298 -0.0732 502 NAG A C6 4912 C C7 . NAG D . ? 1.4116 1.2384 1.2103 0.0081 -0.3125 -0.0203 502 NAG A C7 4913 C C8 . NAG D . ? 1.4158 1.2440 1.2116 0.0089 -0.3123 -0.0048 502 NAG A C8 4914 N N2 . NAG D . ? 1.4560 1.2750 1.2709 0.0028 -0.3211 -0.0337 502 NAG A N2 4915 O O3 . NAG D . ? 1.5058 1.3194 1.3317 0.0079 -0.3502 -0.0663 502 NAG A O3 4916 O O4 . NAG D . ? 1.4944 1.3005 1.3733 -0.0120 -0.3540 -0.0770 502 NAG A O4 4917 O O5 . NAG D . ? 1.4777 1.2876 1.3276 -0.0128 -0.3160 -0.0560 502 NAG A O5 4918 O O6 . NAG D . ? 1.2859 1.0899 1.1826 -0.0297 -0.3167 -0.0663 502 NAG A O6 4919 O O7 . NAG D . ? 1.3819 1.2154 1.1704 0.0123 -0.3054 -0.0193 502 NAG A O7 4920 C C1 . NAG E . ? 1.2399 1.1486 0.9560 0.0220 -0.0631 0.2952 301 NAG B C1 4921 C C2 . NAG E . ? 1.2491 1.1285 1.0102 0.0274 -0.0692 0.3100 301 NAG B C2 4922 C C3 . NAG E . ? 1.2849 1.1430 1.0252 0.0281 -0.0774 0.3467 301 NAG B C3 4923 C C4 . NAG E . ? 1.2610 1.1160 0.9642 0.0128 -0.0550 0.3626 301 NAG B C4 4924 C C5 . NAG E . ? 1.2508 1.1383 0.9091 0.0079 -0.0481 0.3463 301 NAG B C5 4925 C C6 . NAG E . ? 1.2940 1.1831 0.9211 -0.0081 -0.0224 0.3595 301 NAG B C6 4926 C C7 . NAG E . ? 1.4191 1.3019 1.2620 0.0420 -0.0822 0.2756 301 NAG B C7 4927 C C8 . NAG E . ? 1.4418 1.3313 1.3201 0.0555 -0.1037 0.2647 301 NAG B C8 4928 N N2 . NAG E . ? 1.2711 1.1551 1.0680 0.0408 -0.0896 0.2960 301 NAG B N2 4929 O O3 . NAG E . ? 1.3616 1.1912 1.1484 0.0332 -0.0802 0.3587 301 NAG B O3 4930 O O4 . NAG E . ? 1.3320 1.1674 1.0123 0.0131 -0.0635 0.3993 301 NAG B O4 4931 O O5 . NAG E . ? 1.2937 1.1995 0.9778 0.0085 -0.0418 0.3110 301 NAG B O5 4932 O O6 . NAG E . ? 1.3943 1.3041 1.0282 -0.0167 -0.0015 0.3327 301 NAG B O6 4933 O O7 . NAG E . ? 1.5611 1.4385 1.4163 0.0321 -0.0592 0.2665 301 NAG B O7 4934 C C1 . NAG F . ? 2.0074 1.8184 1.3325 -0.2192 0.1887 -0.0216 302 NAG B C1 4935 C C2 . NAG F . ? 2.0450 1.8446 1.3661 -0.2119 0.2300 -0.0345 302 NAG B C2 4936 C C3 . NAG F . ? 2.0602 1.8381 1.3173 -0.2203 0.2424 -0.0639 302 NAG B C3 4937 C C4 . NAG F . ? 2.1066 1.8851 1.2921 -0.2345 0.2265 -0.0568 302 NAG B C4 4938 C C5 . NAG F . ? 2.0308 1.8228 1.2299 -0.2409 0.1831 -0.0407 302 NAG B C5 4939 C C6 . NAG F . ? 2.0297 1.8249 1.1638 -0.2541 0.1634 -0.0283 302 NAG B C6 4940 C C7 . NAG F . ? 1.9793 1.7937 1.4216 -0.1882 0.2463 -0.0217 302 NAG B C7 4941 C C8 . NAG F . ? 1.8989 1.7106 1.3998 -0.1758 0.2559 -0.0319 302 NAG B C8 4942 N N2 . NAG F . ? 2.0129 1.8124 1.3991 -0.1990 0.2410 -0.0413 302 NAG B N2 4943 O O3 . NAG F . ? 2.0625 1.8313 1.3152 -0.2127 0.2829 -0.0753 302 NAG B O3 4944 O O4 . NAG F . ? 2.2228 1.9803 1.3484 -0.2433 0.2328 -0.0875 302 NAG B O4 4945 O O5 . NAG F . ? 2.0474 1.8585 1.3091 -0.2314 0.1766 -0.0134 302 NAG B O5 4946 O O6 . NAG F . ? 2.1831 1.9601 1.2439 -0.2623 0.1801 -0.0507 302 NAG B O6 4947 O O7 . NAG F . ? 2.0104 1.8391 1.4563 -0.1888 0.2425 0.0035 302 NAG B O7 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 GLU 1 28 28 GLU GLU A . n A 1 2 THR 2 29 29 THR THR A . n A 1 3 PRO 3 30 30 PRO PRO A . n A 1 4 PRO 4 31 31 PRO PRO A . n A 1 5 ARG 5 32 32 ARG ARG A . n A 1 6 PHE 6 33 33 PHE PHE A . n A 1 7 THR 7 34 34 THR THR A . n A 1 8 ARG 8 35 35 ARG ARG A . n A 1 9 THR 9 36 36 THR THR A . n A 1 10 PRO 10 37 37 PRO PRO A . n A 1 11 VAL 11 38 38 VAL VAL A . n A 1 12 ASP 12 39 39 ASP ASP A . n A 1 13 GLN 13 40 40 GLN GLN A . n A 1 14 THR 14 41 41 THR THR A . n A 1 15 GLY 15 42 42 GLY GLY A . n A 1 16 VAL 16 43 43 VAL VAL A . n A 1 17 SER 17 44 44 SER SER A . n A 1 18 GLY 18 45 45 GLY GLY A . n A 1 19 GLY 19 46 46 GLY GLY A . n A 1 20 VAL 20 47 47 VAL VAL A . n A 1 21 ALA 21 48 48 ALA ALA A . n A 1 22 SER 22 49 49 SER SER A . n A 1 23 PHE 23 50 50 PHE PHE A . n A 1 24 ILE 24 51 51 ILE ILE A . n A 1 25 CYS 25 52 52 CYS CYS A . n A 1 26 GLN 26 53 53 GLN GLN A . n A 1 27 ALA 27 54 54 ALA ALA A . n A 1 28 THR 28 55 55 THR THR A . n A 1 29 GLY 29 56 56 GLY GLY A . n A 1 30 ASP 30 57 57 ASP ASP A . n A 1 31 PRO 31 58 58 PRO PRO A . n A 1 32 ARG 32 59 59 ARG ARG A . n A 1 33 PRO 33 60 60 PRO PRO A . n A 1 34 LYS 34 61 61 LYS LYS A . n A 1 35 ILE 35 62 62 ILE ILE A . n A 1 36 VAL 36 63 63 VAL VAL A . n A 1 37 TRP 37 64 64 TRP TRP A . n A 1 38 ASN 38 65 65 ASN ASN A . n A 1 39 LYS 39 66 66 LYS LYS A . n A 1 40 LYS 40 67 67 LYS LYS A . n A 1 41 GLY 41 68 68 GLY GLY A . n A 1 42 LYS 42 69 69 LYS LYS A . n A 1 43 LYS 43 70 70 LYS LYS A . n A 1 44 VAL 44 71 71 VAL VAL A . n A 1 45 SER 45 72 72 SER SER A . n A 1 46 ASN 46 73 73 ASN ASN A . n A 1 47 GLN 47 74 74 GLN GLN A . n A 1 48 ARG 48 75 75 ARG ARG A . n A 1 49 PHE 49 76 76 PHE PHE A . n A 1 50 GLU 50 77 77 GLU GLU A . n A 1 51 VAL 51 78 78 VAL VAL A . n A 1 52 ILE 52 79 79 ILE ILE A . n A 1 53 GLU 53 80 80 GLU GLU A . n A 1 54 PHE 54 81 81 PHE PHE A . n A 1 55 ASP 55 82 82 ASP ASP A . n A 1 56 ASP 56 83 83 ASP ASP A . n A 1 57 GLY 57 84 84 GLY GLY A . n A 1 58 SER 58 85 85 SER SER A . n A 1 59 GLY 59 86 86 GLY GLY A . n A 1 60 SER 60 87 87 SER SER A . n A 1 61 VAL 61 88 88 VAL VAL A . n A 1 62 LEU 62 89 89 LEU LEU A . n A 1 63 ARG 63 90 90 ARG ARG A . n A 1 64 ILE 64 91 91 ILE ILE A . n A 1 65 GLN 65 92 92 GLN GLN A . n A 1 66 PRO 66 93 93 PRO PRO A . n A 1 67 LEU 67 94 94 LEU LEU A . n A 1 68 ARG 68 95 95 ARG ARG A . n A 1 69 THR 69 96 96 THR THR A . n A 1 70 PRO 70 97 97 PRO PRO A . n A 1 71 ARG 71 98 98 ARG ARG A . n A 1 72 ASP 72 99 99 ASP ASP A . n A 1 73 GLU 73 100 100 GLU GLU A . n A 1 74 ALA 74 101 101 ALA ALA A . n A 1 75 ILE 75 102 102 ILE ILE A . n A 1 76 TYR 76 103 103 TYR TYR A . n A 1 77 GLU 77 104 104 GLU GLU A . n A 1 78 CYS 78 105 105 CYS CYS A . n A 1 79 VAL 79 106 106 VAL VAL A . n A 1 80 ALA 80 107 107 ALA ALA A . n A 1 81 SER 81 108 108 SER SER A . n A 1 82 ASN 82 109 109 ASN ASN A . n A 1 83 ASN 83 110 110 ASN ASN A . n A 1 84 VAL 84 111 111 VAL VAL A . n A 1 85 GLY 85 112 112 GLY GLY A . n A 1 86 GLU 86 113 113 GLU GLU A . n A 1 87 ILE 87 114 114 ILE ILE A . n A 1 88 SER 88 115 115 SER SER A . n A 1 89 VAL 89 116 116 VAL VAL A . n A 1 90 SER 90 117 117 SER SER A . n A 1 91 THR 91 118 118 THR THR A . n A 1 92 ARG 92 119 119 ARG ARG A . n A 1 93 LEU 93 120 120 LEU LEU A . n A 1 94 THR 94 121 121 THR THR A . n A 1 95 VAL 95 122 122 VAL VAL A . n A 1 96 LEU 96 123 123 LEU LEU A . n A 1 97 ARG 97 124 124 ARG ARG A . n A 1 98 GLU 98 125 125 GLU GLU A . n A 1 99 ASP 99 126 126 ASP ASP A . n A 1 100 GLN 100 127 127 GLN GLN A . n A 1 101 ILE 101 128 128 ILE ILE A . n A 1 102 PRO 102 129 129 PRO PRO A . n A 1 103 ARG 103 130 130 ARG ARG A . n A 1 104 GLY 104 131 131 GLY GLY A . n A 1 105 PHE 105 132 132 PHE PHE A . n A 1 106 PRO 106 133 133 PRO PRO A . n A 1 107 THR 107 134 134 THR THR A . n A 1 108 ILE 108 135 135 ILE ILE A . n A 1 109 ASP 109 136 136 ASP ASP A . n A 1 110 MET 110 137 137 MET MET A . n A 1 111 GLY 111 138 138 GLY GLY A . n A 1 112 PRO 112 139 139 PRO PRO A . n A 1 113 GLN 113 140 140 GLN GLN A . n A 1 114 LEU 114 141 141 LEU LEU A . n A 1 115 LYS 115 142 142 LYS LYS A . n A 1 116 VAL 116 143 143 VAL VAL A . n A 1 117 VAL 117 144 144 VAL VAL A . n A 1 118 GLU 118 145 145 GLU GLU A . n A 1 119 ARG 119 146 146 ARG ARG A . n A 1 120 THR 120 147 147 THR THR A . n A 1 121 ARG 121 148 148 ARG ARG A . n A 1 122 THR 122 149 149 THR THR A . n A 1 123 ALA 123 150 150 ALA ALA A . n A 1 124 THR 124 151 151 THR THR A . n A 1 125 MET 125 152 152 MET MET A . n A 1 126 LEU 126 153 153 LEU LEU A . n A 1 127 CYS 127 154 154 CYS CYS A . n A 1 128 ALA 128 155 155 ALA ALA A . n A 1 129 ALA 129 156 156 ALA ALA A . n A 1 130 SER 130 157 157 SER SER A . n A 1 131 GLY 131 158 158 GLY GLY A . n A 1 132 ASN 132 159 159 ASN ASN A . n A 1 133 PRO 133 160 160 PRO PRO A . n A 1 134 ASP 134 161 161 ASP ASP A . n A 1 135 PRO 135 162 162 PRO PRO A . n A 1 136 GLU 136 163 163 GLU GLU A . n A 1 137 ILE 137 164 164 ILE ILE A . n A 1 138 THR 138 165 165 THR THR A . n A 1 139 TRP 139 166 166 TRP TRP A . n A 1 140 PHE 140 167 167 PHE PHE A . n A 1 141 LYS 141 168 168 LYS LYS A . n A 1 142 ASP 142 169 169 ASP ASP A . n A 1 143 PHE 143 170 170 PHE PHE A . n A 1 144 LEU 144 171 171 LEU LEU A . n A 1 145 PRO 145 172 172 PRO PRO A . n A 1 146 VAL 146 173 173 VAL VAL A . n A 1 147 ASP 147 174 174 ASP ASP A . n A 1 148 THR 148 175 175 THR THR A . n A 1 149 SER 149 176 176 SER SER A . n A 1 150 ASN 150 177 177 ASN ASN A . n A 1 151 ASN 151 178 178 ASN ASN A . n A 1 152 ASN 152 179 179 ASN ASN A . n A 1 153 GLY 153 180 180 GLY GLY A . n A 1 154 ARG 154 181 181 ARG ARG A . n A 1 155 ILE 155 182 182 ILE ILE A . n A 1 156 LYS 156 183 183 LYS LYS A . n A 1 157 GLN 157 184 184 GLN GLN A . n A 1 158 LEU 158 185 185 LEU LEU A . n A 1 159 ARG 159 186 186 ARG ARG A . n A 1 160 SER 160 187 187 SER SER A . n A 1 161 GLU 161 188 188 GLU GLU A . n A 1 162 SER 162 189 189 SER SER A . n A 1 163 ILE 163 190 190 ILE ILE A . n A 1 164 GLY 164 191 191 GLY GLY A . n A 1 165 GLY 165 192 192 GLY GLY A . n A 1 166 THR 166 193 193 THR THR A . n A 1 167 PRO 167 194 194 PRO PRO A . n A 1 168 ILE 168 195 195 ILE ILE A . n A 1 169 ARG 169 196 196 ARG ARG A . n A 1 170 GLY 170 197 197 GLY GLY A . n A 1 171 ALA 171 198 198 ALA ALA A . n A 1 172 LEU 172 199 199 LEU LEU A . n A 1 173 GLN 173 200 200 GLN GLN A . n A 1 174 ILE 174 201 201 ILE ILE A . n A 1 175 GLU 175 202 202 GLU GLU A . n A 1 176 GLN 176 203 203 GLN GLN A . n A 1 177 SER 177 204 204 SER SER A . n A 1 178 GLU 178 205 205 GLU GLU A . n A 1 179 GLU 179 206 206 GLU GLU A . n A 1 180 SER 180 207 207 SER SER A . n A 1 181 ASP 181 208 208 ASP ASP A . n A 1 182 GLN 182 209 209 GLN GLN A . n A 1 183 GLY 183 210 210 GLY GLY A . n A 1 184 LYS 184 211 211 LYS LYS A . n A 1 185 TYR 185 212 212 TYR TYR A . n A 1 186 GLU 186 213 213 GLU GLU A . n A 1 187 CYS 187 214 214 CYS CYS A . n A 1 188 VAL 188 215 215 VAL VAL A . n A 1 189 ALA 189 216 216 ALA ALA A . n A 1 190 THR 190 217 217 THR THR A . n A 1 191 ASN 191 218 218 ASN ASN A . n A 1 192 SER 192 219 219 SER SER A . n A 1 193 ALA 193 220 220 ALA ALA A . n A 1 194 GLY 194 221 221 GLY GLY A . n A 1 195 THR 195 222 222 THR THR A . n A 1 196 ARG 196 223 223 ARG ARG A . n A 1 197 TYR 197 224 224 TYR TYR A . n A 1 198 SER 198 225 225 SER SER A . n A 1 199 ALA 199 226 226 ALA ALA A . n A 1 200 PRO 200 227 227 PRO PRO A . n A 1 201 ALA 201 228 228 ALA ALA A . n A 1 202 ASN 202 229 229 ASN ASN A . n A 1 203 LEU 203 230 230 LEU LEU A . n A 1 204 TYR 204 231 231 TYR TYR A . n A 1 205 VAL 205 232 232 VAL VAL A . n A 1 206 ARG 206 233 233 ARG ARG A . n A 1 207 GLU 207 234 234 GLU GLU A . n A 1 208 LEU 208 235 235 LEU LEU A . n A 1 209 ARG 209 236 236 ARG ARG A . n A 1 210 GLU 210 237 237 GLU GLU A . n A 1 211 VAL 211 238 238 VAL VAL A . n A 1 212 ARG 212 239 239 ARG ARG A . n A 1 213 ARG 213 240 240 ARG ARG A . n A 1 214 VAL 214 241 241 VAL VAL A . n A 1 215 PRO 215 242 242 PRO PRO A . n A 1 216 PRO 216 243 243 PRO PRO A . n A 1 217 ARG 217 244 244 ARG ARG A . n A 1 218 PHE 218 245 245 PHE PHE A . n A 1 219 SER 219 246 246 SER SER A . n A 1 220 ILE 220 247 247 ILE ILE A . n A 1 221 PRO 221 248 248 PRO PRO A . n A 1 222 PRO 222 249 249 PRO PRO A . n A 1 223 THR 223 250 250 THR THR A . n A 1 224 ASN 224 251 251 ASN ASN A . n A 1 225 HIS 225 252 252 HIS HIS A . n A 1 226 GLU 226 253 253 GLU GLU A . n A 1 227 ILE 227 254 254 ILE ILE A . n A 1 228 MET 228 255 255 MET MET A . n A 1 229 PRO 229 256 256 PRO PRO A . n A 1 230 GLY 230 257 257 GLY GLY A . n A 1 231 GLY 231 258 258 GLY GLY A . n A 1 232 SER 232 259 259 SER SER A . n A 1 233 VAL 233 260 260 VAL VAL A . n A 1 234 ASN 234 261 261 ASN ASN A . n A 1 235 ILE 235 262 262 ILE ILE A . n A 1 236 THR 236 263 263 THR THR A . n A 1 237 CYS 237 264 264 CYS CYS A . n A 1 238 VAL 238 265 265 VAL VAL A . n A 1 239 ALA 239 266 266 ALA ALA A . n A 1 240 VAL 240 267 267 VAL VAL A . n A 1 241 GLY 241 268 268 GLY GLY A . n A 1 242 SER 242 269 269 SER SER A . n A 1 243 PRO 243 270 270 PRO PRO A . n A 1 244 MET 244 271 271 MET MET A . n A 1 245 PRO 245 272 272 PRO PRO A . n A 1 246 TYR 246 273 273 TYR TYR A . n A 1 247 VAL 247 274 274 VAL VAL A . n A 1 248 LYS 248 275 275 LYS LYS A . n A 1 249 TRP 249 276 276 TRP TRP A . n A 1 250 MET 250 277 277 MET MET A . n A 1 251 LEU 251 278 278 LEU LEU A . n A 1 252 GLY 252 279 279 GLY GLY A . n A 1 253 ALA 253 280 280 ALA ALA A . n A 1 254 GLU 254 281 281 GLU GLU A . n A 1 255 ASP 255 282 282 ASP ASP A . n A 1 256 LEU 256 283 283 LEU LEU A . n A 1 257 THR 257 284 284 THR THR A . n A 1 258 PRO 258 285 285 PRO PRO A . n A 1 259 GLU 259 286 286 GLU GLU A . n A 1 260 ASP 260 287 287 ASP ASP A . n A 1 261 ASP 261 288 288 ASP ASP A . n A 1 262 MET 262 289 289 MET MET A . n A 1 263 PRO 263 290 290 PRO PRO A . n A 1 264 ILE 264 291 291 ILE ILE A . n A 1 265 GLY 265 292 292 GLY GLY A . n A 1 266 ARG 266 293 293 ARG ARG A . n A 1 267 ASN 267 294 294 ASN ASN A . n A 1 268 VAL 268 295 295 VAL VAL A . n A 1 269 LEU 269 296 296 LEU LEU A . n A 1 270 GLU 270 297 297 GLU GLU A . n A 1 271 LEU 271 298 298 LEU LEU A . n A 1 272 ASN 272 299 299 ASN ASN A . n A 1 273 ASP 273 300 300 ASP ASP A . n A 1 274 VAL 274 301 301 VAL VAL A . n A 1 275 ARG 275 302 302 ARG ARG A . n A 1 276 GLN 276 303 303 GLN GLN A . n A 1 277 SER 277 304 304 SER SER A . n A 1 278 ALA 278 305 305 ALA ALA A . n A 1 279 ASN 279 306 306 ASN ASN A . n A 1 280 TYR 280 307 307 TYR TYR A . n A 1 281 THR 281 308 308 THR THR A . n A 1 282 CYS 282 309 309 CYS CYS A . n A 1 283 VAL 283 310 310 VAL VAL A . n A 1 284 ALA 284 311 311 ALA ALA A . n A 1 285 MET 285 312 312 MET MET A . n A 1 286 SER 286 313 313 SER SER A . n A 1 287 THR 287 314 314 THR THR A . n A 1 288 LEU 288 315 315 LEU LEU A . n A 1 289 GLY 289 316 316 GLY GLY A . n A 1 290 VAL 290 317 317 VAL VAL A . n A 1 291 ILE 291 318 318 ILE ILE A . n A 1 292 GLU 292 319 319 GLU GLU A . n A 1 293 ALA 293 320 320 ALA ALA A . n A 1 294 ILE 294 321 321 ILE ILE A . n A 1 295 ALA 295 322 322 ALA ALA A . n A 1 296 GLN 296 323 323 GLN GLN A . n A 1 297 ILE 297 324 324 ILE ILE A . n A 1 298 THR 298 325 325 THR THR A . n A 1 299 VAL 299 326 326 VAL VAL A . n A 1 300 LYS 300 327 327 LYS LYS A . n A 1 301 ALA 301 328 328 ALA ALA A . n A 1 302 LEU 302 329 329 LEU LEU A . n A 1 303 PRO 303 330 330 PRO PRO A . n A 1 304 LYS 304 331 331 LYS LYS A . n A 1 305 PRO 305 332 332 PRO PRO A . n A 1 306 PRO 306 333 333 PRO PRO A . n A 1 307 GLY 307 334 334 GLY GLY A . n A 1 308 THR 308 335 335 THR THR A . n A 1 309 PRO 309 336 336 PRO PRO A . n A 1 310 VAL 310 337 337 VAL VAL A . n A 1 311 VAL 311 338 338 VAL VAL A . n A 1 312 THR 312 339 339 THR THR A . n A 1 313 GLU 313 340 340 GLU GLU A . n A 1 314 SER 314 341 341 SER SER A . n A 1 315 THR 315 342 342 THR THR A . n A 1 316 ALA 316 343 343 ALA ALA A . n A 1 317 THR 317 344 344 THR THR A . n A 1 318 SER 318 345 345 SER SER A . n A 1 319 ILE 319 346 346 ILE ILE A . n A 1 320 THR 320 347 347 THR THR A . n A 1 321 LEU 321 348 348 LEU LEU A . n A 1 322 THR 322 349 349 THR THR A . n A 1 323 TRP 323 350 350 TRP TRP A . n A 1 324 ASP 324 351 351 ASP ASP A . n A 1 325 SER 325 352 352 SER SER A . n A 1 326 GLY 326 353 353 GLY GLY A . n A 1 327 ASN 327 354 354 ASN ASN A . n A 1 328 PRO 328 355 355 PRO PRO A . n A 1 329 GLU 329 356 356 GLU GLU A . n A 1 330 PRO 330 357 357 PRO PRO A . n A 1 331 VAL 331 358 358 VAL VAL A . n A 1 332 SER 332 359 359 SER SER A . n A 1 333 TYR 333 360 360 TYR TYR A . n A 1 334 TYR 334 361 361 TYR TYR A . n A 1 335 ILE 335 362 362 ILE ILE A . n A 1 336 ILE 336 363 363 ILE ILE A . n A 1 337 GLN 337 364 364 GLN GLN A . n A 1 338 HIS 338 365 365 HIS HIS A . n A 1 339 LYS 339 366 366 LYS LYS A . n A 1 340 PRO 340 367 367 PRO PRO A . n A 1 341 LYS 341 368 368 LYS LYS A . n A 1 342 ASN 342 369 369 ASN ASN A . n A 1 343 SER 343 370 370 SER SER A . n A 1 344 GLU 344 371 371 GLU GLU A . n A 1 345 GLU 345 372 372 GLU GLU A . n A 1 346 PRO 346 373 373 PRO PRO A . n A 1 347 TYR 347 374 374 TYR TYR A . n A 1 348 LYS 348 375 375 LYS LYS A . n A 1 349 GLU 349 376 376 GLU GLU A . n A 1 350 ILE 350 377 377 ILE ILE A . n A 1 351 ASP 351 378 378 ASP ASP A . n A 1 352 GLY 352 379 379 GLY GLY A . n A 1 353 ILE 353 380 380 ILE ILE A . n A 1 354 ALA 354 381 381 ALA ALA A . n A 1 355 THR 355 382 382 THR THR A . n A 1 356 THR 356 383 383 THR THR A . n A 1 357 ARG 357 384 384 ARG ARG A . n A 1 358 TYR 358 385 385 TYR TYR A . n A 1 359 SER 359 386 386 SER SER A . n A 1 360 VAL 360 387 387 VAL VAL A . n A 1 361 ALA 361 388 388 ALA ALA A . n A 1 362 GLY 362 389 389 GLY GLY A . n A 1 363 LEU 363 390 390 LEU LEU A . n A 1 364 SER 364 391 391 SER SER A . n A 1 365 PRO 365 392 392 PRO PRO A . n A 1 366 TYR 366 393 393 TYR TYR A . n A 1 367 SER 367 394 394 SER SER A . n A 1 368 ASP 368 395 395 ASP ASP A . n A 1 369 TYR 369 396 396 TYR TYR A . n A 1 370 GLU 370 397 397 GLU GLU A . n A 1 371 PHE 371 398 398 PHE PHE A . n A 1 372 ARG 372 399 399 ARG ARG A . n A 1 373 VAL 373 400 400 VAL VAL A . n A 1 374 VAL 374 401 401 VAL VAL A . n A 1 375 ALA 375 402 402 ALA ALA A . n A 1 376 VAL 376 403 403 VAL VAL A . n A 1 377 ASN 377 404 404 ASN ASN A . n A 1 378 ASN 378 405 405 ASN ASN A . n A 1 379 ILE 379 406 406 ILE ILE A . n A 1 380 GLY 380 407 407 GLY GLY A . n A 1 381 ARG 381 408 408 ARG ARG A . n A 1 382 GLY 382 409 409 GLY GLY A . n A 1 383 PRO 383 410 410 PRO PRO A . n A 1 384 ALA 384 411 411 ALA ALA A . n A 1 385 SER 385 412 412 SER SER A . n A 1 386 GLU 386 413 413 GLU GLU A . n A 1 387 PRO 387 414 414 PRO PRO A . n A 1 388 VAL 388 415 415 VAL VAL A . n A 1 389 LEU 389 416 416 LEU LEU A . n A 1 390 THR 390 417 417 THR THR A . n A 1 391 GLN 391 418 418 GLN GLN A . n A 1 392 LYS 392 419 ? ? ? A . n A 1 393 HIS 393 420 ? ? ? A . n A 1 394 HIS 394 421 ? ? ? A . n A 1 395 HIS 395 422 ? ? ? A . n A 1 396 HIS 396 423 ? ? ? A . n A 1 397 HIS 397 424 ? ? ? A . n A 1 398 HIS 398 425 ? ? ? A . n B 2 1 MET 1 1 ? ? ? B . n B 2 2 LEU 2 2 ? ? ? B . n B 2 3 SER 3 3 ? ? ? B . n B 2 4 GLY 4 4 ? ? ? B . n B 2 5 VAL 5 5 ? ? ? B . n B 2 6 TRP 6 6 ? ? ? B . n B 2 7 PHE 7 7 ? ? ? B . n B 2 8 LEU 8 8 ? ? ? B . n B 2 9 SER 9 9 ? ? ? B . n B 2 10 VAL 10 10 ? ? ? B . n B 2 11 LEU 11 11 ? ? ? B . n B 2 12 THR 12 12 ? ? ? B . n B 2 13 VAL 13 13 ? ? ? B . n B 2 14 ALA 14 14 ? ? ? B . n B 2 15 GLY 15 15 ? ? ? B . n B 2 16 ILE 16 16 ? ? ? B . n B 2 17 LEU 17 17 ? ? ? B . n B 2 18 GLN 18 18 ? ? ? B . n B 2 19 THR 19 19 ? ? ? B . n B 2 20 GLU 20 20 ? ? ? B . n B 2 21 SER 21 21 ? ? ? B . n B 2 22 ARG 22 22 ? ? ? B . n B 2 23 LYS 23 23 ? ? ? B . n B 2 24 THR 24 24 ? ? ? B . n B 2 25 ALA 25 25 ? ? ? B . n B 2 26 LYS 26 26 ? ? ? B . n B 2 27 ASP 27 27 ? ? ? B . n B 2 28 ILE 28 28 ? ? ? B . n B 2 29 CYS 29 29 29 CYS CYS B . n B 2 30 LYS 30 30 30 LYS LYS B . n B 2 31 ILE 31 31 31 ILE ILE B . n B 2 32 ARG 32 32 32 ARG ARG B . n B 2 33 CYS 33 33 33 CYS CYS B . n B 2 34 LEU 34 34 34 LEU LEU B . n B 2 35 CYS 35 35 35 CYS CYS B . n B 2 36 GLU 36 36 36 GLU GLU B . n B 2 37 GLU 37 37 37 GLU GLU B . n B 2 38 LYS 38 38 38 LYS LYS B . n B 2 39 GLU 39 39 39 GLU GLU B . n B 2 40 ASN 40 40 40 ASN ASN B . n B 2 41 VAL 41 41 41 VAL VAL B . n B 2 42 LEU 42 42 42 LEU LEU B . n B 2 43 ASN 43 43 43 ASN ASN B . n B 2 44 ILE 44 44 44 ILE ILE B . n B 2 45 ASN 45 45 45 ASN ASN B . n B 2 46 CYS 46 46 46 CYS CYS B . n B 2 47 GLU 47 47 47 GLU GLU B . n B 2 48 ASN 48 48 48 ASN ASN B . n B 2 49 LYS 49 49 49 LYS LYS B . n B 2 50 GLY 50 50 50 GLY GLY B . n B 2 51 PHE 51 51 51 PHE PHE B . n B 2 52 THR 52 52 52 THR THR B . n B 2 53 THR 53 53 53 THR THR B . n B 2 54 VAL 54 54 54 VAL VAL B . n B 2 55 SER 55 55 55 SER SER B . n B 2 56 LEU 56 56 56 LEU LEU B . n B 2 57 LEU 57 57 57 LEU LEU B . n B 2 58 GLN 58 58 58 GLN GLN B . n B 2 59 PRO 59 59 59 PRO PRO B . n B 2 60 PRO 60 60 60 PRO PRO B . n B 2 61 GLN 61 61 61 GLN GLN B . n B 2 62 TYR 62 62 62 TYR TYR B . n B 2 63 ARG 63 63 63 ARG ARG B . n B 2 64 ILE 64 64 64 ILE ILE B . n B 2 65 TYR 65 65 65 TYR TYR B . n B 2 66 GLN 66 66 66 GLN GLN B . n B 2 67 LEU 67 67 67 LEU LEU B . n B 2 68 PHE 68 68 68 PHE PHE B . n B 2 69 LEU 69 69 69 LEU LEU B . n B 2 70 ASN 70 70 70 ASN ASN B . n B 2 71 GLY 71 71 71 GLY GLY B . n B 2 72 ASN 72 72 72 ASN ASN B . n B 2 73 LEU 73 73 73 LEU LEU B . n B 2 74 LEU 74 74 74 LEU LEU B . n B 2 75 THR 75 75 75 THR THR B . n B 2 76 ARG 76 76 76 ARG ARG B . n B 2 77 LEU 77 77 77 LEU LEU B . n B 2 78 TYR 78 78 78 TYR TYR B . n B 2 79 PRO 79 79 79 PRO PRO B . n B 2 80 ASN 80 80 80 ASN ASN B . n B 2 81 GLU 81 81 81 GLU GLU B . n B 2 82 PHE 82 82 82 PHE PHE B . n B 2 83 VAL 83 83 83 VAL VAL B . n B 2 84 ASN 84 84 84 ASN ASN B . n B 2 85 TYR 85 85 85 TYR TYR B . n B 2 86 SER 86 86 86 SER SER B . n B 2 87 ASN 87 87 87 ASN ASN B . n B 2 88 ALA 88 88 88 ALA ALA B . n B 2 89 VAL 89 89 89 VAL VAL B . n B 2 90 THR 90 90 90 THR THR B . n B 2 91 LEU 91 91 91 LEU LEU B . n B 2 92 HIS 92 92 92 HIS HIS B . n B 2 93 LEU 93 93 93 LEU LEU B . n B 2 94 GLY 94 94 94 GLY GLY B . n B 2 95 ASN 95 95 95 ASN ASN B . n B 2 96 ASN 96 96 96 ASN ASN B . n B 2 97 GLY 97 97 97 GLY GLY B . n B 2 98 LEU 98 98 98 LEU LEU B . n B 2 99 GLN 99 99 99 GLN GLN B . n B 2 100 GLU 100 100 100 GLU GLU B . n B 2 101 ILE 101 101 101 ILE ILE B . n B 2 102 ARG 102 102 102 ARG ARG B . n B 2 103 PRO 103 103 103 PRO PRO B . n B 2 104 GLY 104 104 104 GLY GLY B . n B 2 105 ALA 105 105 105 ALA ALA B . n B 2 106 PHE 106 106 106 PHE PHE B . n B 2 107 SER 107 107 107 SER SER B . n B 2 108 GLY 108 108 108 GLY GLY B . n B 2 109 LEU 109 109 109 LEU LEU B . n B 2 110 LYS 110 110 110 LYS LYS B . n B 2 111 THR 111 111 111 THR THR B . n B 2 112 LEU 112 112 112 LEU LEU B . n B 2 113 LYS 113 113 113 LYS LYS B . n B 2 114 ARG 114 114 114 ARG ARG B . n B 2 115 LEU 115 115 115 LEU LEU B . n B 2 116 HIS 116 116 116 HIS HIS B . n B 2 117 LEU 117 117 117 LEU LEU B . n B 2 118 ASN 118 118 118 ASN ASN B . n B 2 119 ASN 119 119 119 ASN ASN B . n B 2 120 ASN 120 120 120 ASN ASN B . n B 2 121 LYS 121 121 121 LYS LYS B . n B 2 122 LEU 122 122 122 LEU LEU B . n B 2 123 GLU 123 123 123 GLU GLU B . n B 2 124 VAL 124 124 124 VAL VAL B . n B 2 125 LEU 125 125 125 LEU LEU B . n B 2 126 ARG 126 126 126 ARG ARG B . n B 2 127 GLU 127 127 127 GLU GLU B . n B 2 128 ASP 128 128 128 ASP ASP B . n B 2 129 THR 129 129 129 THR THR B . n B 2 130 PHE 130 130 130 PHE PHE B . n B 2 131 LEU 131 131 131 LEU LEU B . n B 2 132 GLY 132 132 132 GLY GLY B . n B 2 133 LEU 133 133 133 LEU LEU B . n B 2 134 GLU 134 134 134 GLU GLU B . n B 2 135 SER 135 135 135 SER SER B . n B 2 136 LEU 136 136 136 LEU LEU B . n B 2 137 GLU 137 137 137 GLU GLU B . n B 2 138 TYR 138 138 138 TYR TYR B . n B 2 139 LEU 139 139 139 LEU LEU B . n B 2 140 GLN 140 140 140 GLN GLN B . n B 2 141 ALA 141 141 141 ALA ALA B . n B 2 142 ASP 142 142 142 ASP ASP B . n B 2 143 TYR 143 143 143 TYR TYR B . n B 2 144 ASN 144 144 144 ASN ASN B . n B 2 145 TYR 145 145 145 TYR TYR B . n B 2 146 ILE 146 146 146 ILE ILE B . n B 2 147 SER 147 147 147 SER SER B . n B 2 148 THR 148 148 148 THR THR B . n B 2 149 ILE 149 149 149 ILE ILE B . n B 2 150 GLU 150 150 150 GLU GLU B . n B 2 151 ALA 151 151 151 ALA ALA B . n B 2 152 GLY 152 152 152 GLY GLY B . n B 2 153 ALA 153 153 153 ALA ALA B . n B 2 154 PHE 154 154 154 PHE PHE B . n B 2 155 SER 155 155 155 SER SER B . n B 2 156 LYS 156 156 156 LYS LYS B . n B 2 157 LEU 157 157 157 LEU LEU B . n B 2 158 ASN 158 158 158 ASN ASN B . n B 2 159 LYS 159 159 159 LYS LYS B . n B 2 160 LEU 160 160 160 LEU LEU B . n B 2 161 LYS 161 161 161 LYS LYS B . n B 2 162 VAL 162 162 162 VAL VAL B . n B 2 163 LEU 163 163 163 LEU LEU B . n B 2 164 ILE 164 164 164 ILE ILE B . n B 2 165 LEU 165 165 165 LEU LEU B . n B 2 166 ASN 166 166 166 ASN ASN B . n B 2 167 ASP 167 167 167 ASP ASP B . n B 2 168 ASN 168 168 168 ASN ASN B . n B 2 169 LEU 169 169 169 LEU LEU B . n B 2 170 LEU 170 170 170 LEU LEU B . n B 2 171 LEU 171 171 171 LEU LEU B . n B 2 172 SER 172 172 172 SER SER B . n B 2 173 LEU 173 173 173 LEU LEU B . n B 2 174 PRO 174 174 174 PRO PRO B . n B 2 175 SER 175 175 175 SER SER B . n B 2 176 ASN 176 176 176 ASN ASN B . n B 2 177 VAL 177 177 177 VAL VAL B . n B 2 178 PHE 178 178 178 PHE PHE B . n B 2 179 ARG 179 179 179 ARG ARG B . n B 2 180 PHE 180 180 180 PHE PHE B . n B 2 181 VAL 181 181 181 VAL VAL B . n B 2 182 LEU 182 182 182 LEU LEU B . n B 2 183 LEU 183 183 183 LEU LEU B . n B 2 184 THR 184 184 184 THR THR B . n B 2 185 HIS 185 185 185 HIS HIS B . n B 2 186 LEU 186 186 186 LEU LEU B . n B 2 187 ASP 187 187 187 ASP ASP B . n B 2 188 LEU 188 188 188 LEU LEU B . n B 2 189 ARG 189 189 189 ARG ARG B . n B 2 190 GLY 190 190 190 GLY GLY B . n B 2 191 ASN 191 191 191 ASN ASN B . n B 2 192 ARG 192 192 192 ARG ARG B . n B 2 193 LEU 193 193 193 LEU LEU B . n B 2 194 LYS 194 194 194 LYS LYS B . n B 2 195 VAL 195 195 195 VAL VAL B . n B 2 196 MET 196 196 196 MET MET B . n B 2 197 PRO 197 197 197 PRO PRO B . n B 2 198 PHE 198 198 198 PHE PHE B . n B 2 199 ALA 199 199 199 ALA ALA B . n B 2 200 GLY 200 200 200 GLY GLY B . n B 2 201 VAL 201 201 201 VAL VAL B . n B 2 202 LEU 202 202 202 LEU LEU B . n B 2 203 GLU 203 203 203 GLU GLU B . n B 2 204 HIS 204 204 204 HIS HIS B . n B 2 205 ILE 205 205 205 ILE ILE B . n B 2 206 GLY 206 206 206 GLY GLY B . n B 2 207 GLY 207 207 207 GLY GLY B . n B 2 208 ILE 208 208 208 ILE ILE B . n B 2 209 MET 209 209 209 MET MET B . n B 2 210 GLU 210 210 210 GLU GLU B . n B 2 211 ILE 211 211 211 ILE ILE B . n B 2 212 GLN 212 212 212 GLN GLN B . n B 2 213 LEU 213 213 213 LEU LEU B . n B 2 214 GLU 214 214 214 GLU GLU B . n B 2 215 GLU 215 215 215 GLU GLU B . n B 2 216 ASN 216 216 216 ASN ASN B . n B 2 217 PRO 217 217 217 PRO PRO B . n B 2 218 TRP 218 218 218 TRP TRP B . n B 2 219 ASN 219 219 219 ASN ASN B . n B 2 220 CYS 220 220 220 CYS CYS B . n B 2 221 THR 221 221 221 THR THR B . n B 2 222 CYS 222 222 222 CYS CYS B . n B 2 223 ASP 223 223 223 ASP ASP B . n B 2 224 LEU 224 224 224 LEU LEU B . n B 2 225 LEU 225 225 225 LEU LEU B . n B 2 226 PRO 226 226 226 PRO PRO B . n B 2 227 LEU 227 227 227 LEU LEU B . n B 2 228 LYS 228 228 228 LYS LYS B . n B 2 229 ALA 229 229 229 ALA ALA B . n B 2 230 TRP 230 230 230 TRP TRP B . n B 2 231 LEU 231 231 231 LEU LEU B . n B 2 232 ASP 232 232 232 ASP ASP B . n B 2 233 THR 233 233 233 THR THR B . n B 2 234 ILE 234 234 234 ILE ILE B . n B 2 235 THR 235 235 235 THR THR B . n B 2 236 VAL 236 236 236 VAL VAL B . n B 2 237 PHE 237 237 237 PHE PHE B . n B 2 238 VAL 238 238 238 VAL VAL B . n B 2 239 GLY 239 239 239 GLY GLY B . n B 2 240 GLU 240 240 240 GLU GLU B . n B 2 241 ILE 241 241 241 ILE ILE B . n B 2 242 VAL 242 242 242 VAL VAL B . n B 2 243 CYS 243 243 243 CYS CYS B . n B 2 244 GLU 244 244 244 GLU GLU B . n B 2 245 THR 245 245 245 THR THR B . n B 2 246 PRO 246 246 246 PRO PRO B . n B 2 247 PHE 247 247 247 PHE PHE B . n B 2 248 ARG 248 248 248 ARG ARG B . n B 2 249 LEU 249 249 249 LEU LEU B . n B 2 250 HIS 250 250 250 HIS HIS B . n B 2 251 GLY 251 251 251 GLY GLY B . n B 2 252 LYS 252 252 252 LYS LYS B . n B 2 253 ASP 253 253 253 ASP ASP B . n B 2 254 VAL 254 254 254 VAL VAL B . n B 2 255 THR 255 255 255 THR THR B . n B 2 256 GLN 256 256 256 GLN GLN B . n B 2 257 LEU 257 257 257 LEU LEU B . n B 2 258 THR 258 258 258 THR THR B . n B 2 259 ARG 259 259 259 ARG ARG B . n B 2 260 GLN 260 260 260 GLN GLN B . n B 2 261 ASP 261 261 261 ASP ASP B . n B 2 262 LEU 262 262 262 LEU LEU B . n B 2 263 CYS 263 263 263 CYS CYS B . n B 2 264 PRO 264 264 ? ? ? B . n B 2 265 ARG 265 265 ? ? ? B . n B 2 266 LYS 266 266 ? ? ? B . n B 2 267 HIS 267 267 ? ? ? B . n B 2 268 HIS 268 268 ? ? ? B . n B 2 269 HIS 269 269 ? ? ? B . n B 2 270 HIS 270 270 ? ? ? B . n B 2 271 HIS 271 271 ? ? ? B . n B 2 272 HIS 272 272 ? ? ? B . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code C 3 NAG 1 501 1002 NAG NAG A . D 3 NAG 1 502 1001 NAG NAG A . E 3 NAG 1 301 1003 NAG NAG B . F 3 NAG 1 302 1004 NAG NAG B . # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_defined_assembly _pdbx_struct_assembly.method_details ? _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 # 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)' 2990 ? 1 MORE 14 ? 1 'SSA (A^2)' 32540 ? # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2015-06-03 2 'Structure model' 1 1 2017-10-04 # _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' 'Data collection' 2 2 'Structure model' 'Derived calculations' 3 2 'Structure model' 'Source and taxonomy' # loop_ _pdbx_audit_revision_category.ordinal _pdbx_audit_revision_category.revision_ordinal _pdbx_audit_revision_category.data_content_type _pdbx_audit_revision_category.category 1 2 'Structure model' diffrn_detector 2 2 'Structure model' diffrn_source 3 2 'Structure model' entity_src_gen 4 2 'Structure model' pdbx_struct_assembly 5 2 'Structure model' pdbx_struct_assembly_gen 6 2 'Structure model' pdbx_struct_assembly_prop 7 2 'Structure model' pdbx_struct_oper_list # loop_ _pdbx_audit_revision_item.ordinal _pdbx_audit_revision_item.revision_ordinal _pdbx_audit_revision_item.data_content_type _pdbx_audit_revision_item.item 1 2 'Structure model' '_diffrn_detector.detector' 2 2 'Structure model' '_diffrn_source.pdbx_synchrotron_site' 3 2 'Structure model' '_entity_src_gen.pdbx_alt_source_flag' 4 2 'Structure model' '_pdbx_struct_assembly.oligomeric_details' 5 2 'Structure model' '_pdbx_struct_assembly_gen.asym_id_list' 6 2 'Structure model' '_pdbx_struct_assembly_prop.type' 7 2 'Structure model' '_pdbx_struct_assembly_prop.value' 8 2 'Structure model' '_pdbx_struct_oper_list.symmetry_operation' # loop_ _pdbx_refine_tls.pdbx_refine_id _pdbx_refine_tls.id _pdbx_refine_tls.details _pdbx_refine_tls.method _pdbx_refine_tls.origin_x _pdbx_refine_tls.origin_y _pdbx_refine_tls.origin_z _pdbx_refine_tls.T[1][1] _pdbx_refine_tls.T[2][2] _pdbx_refine_tls.T[3][3] _pdbx_refine_tls.T[1][2] _pdbx_refine_tls.T[1][3] _pdbx_refine_tls.T[2][3] _pdbx_refine_tls.L[1][1] _pdbx_refine_tls.L[2][2] _pdbx_refine_tls.L[3][3] _pdbx_refine_tls.L[1][2] _pdbx_refine_tls.L[1][3] _pdbx_refine_tls.L[2][3] _pdbx_refine_tls.S[1][1] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[2][2] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] _pdbx_refine_tls.S[3][3] 'X-RAY DIFFRACTION' 1 ? refined -36.2835 -1.7626 -8.2660 0.6270 0.4864 0.6714 -0.0963 -0.1087 -0.0290 2.3945 1.0839 1.2439 -1.4851 1.3090 -0.8769 -0.1223 0.2352 0.1782 -0.2073 -0.0580 -0.0392 -0.0972 0.1218 -0.0018 'X-RAY DIFFRACTION' 2 ? refined -25.0977 4.8135 3.3499 0.3496 0.3295 0.4292 -0.0532 0.0560 0.0145 2.8087 2.7843 1.2989 0.1489 0.2641 -0.0873 0.2358 0.0483 0.0253 0.1191 -0.0450 0.2376 -0.3172 0.1843 0.1979 # loop_ _pdbx_refine_tls_group.pdbx_refine_id _pdbx_refine_tls_group.id _pdbx_refine_tls_group.refine_tls_id _pdbx_refine_tls_group.beg_auth_asym_id _pdbx_refine_tls_group.beg_auth_seq_id _pdbx_refine_tls_group.beg_label_asym_id _pdbx_refine_tls_group.beg_label_seq_id _pdbx_refine_tls_group.end_auth_asym_id _pdbx_refine_tls_group.end_auth_seq_id _pdbx_refine_tls_group.end_label_asym_id _pdbx_refine_tls_group.end_label_seq_id _pdbx_refine_tls_group.selection _pdbx_refine_tls_group.selection_details 'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? '(chain A and (resseq 28:418 or resseq 501:502))' 'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? '(chain B and (resseq 29:263 or resseq 301:302))' # loop_ _software.citation_id _software.classification _software.compiler_name _software.compiler_version _software.contact_author _software.contact_author_email _software.date _software.description _software.dependencies _software.hardware _software.language _software.location _software.mods _software.name _software.os _software.os_version _software.type _software.version _software.pdbx_ordinal ? refinement ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.9_1692 1 ? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? . 2 ? 'data scaling' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? . 3 ? phasing ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? . 4 # _pdbx_validate_close_contact.id 1 _pdbx_validate_close_contact.PDB_model_num 1 _pdbx_validate_close_contact.auth_atom_id_1 OH _pdbx_validate_close_contact.auth_asym_id_1 A _pdbx_validate_close_contact.auth_comp_id_1 TYR _pdbx_validate_close_contact.auth_seq_id_1 231 _pdbx_validate_close_contact.PDB_ins_code_1 ? _pdbx_validate_close_contact.label_alt_id_1 ? _pdbx_validate_close_contact.auth_atom_id_2 OE2 _pdbx_validate_close_contact.auth_asym_id_2 B _pdbx_validate_close_contact.auth_comp_id_2 GLU _pdbx_validate_close_contact.auth_seq_id_2 137 _pdbx_validate_close_contact.PDB_ins_code_2 ? _pdbx_validate_close_contact.label_alt_id_2 ? _pdbx_validate_close_contact.dist 2.17 # 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 LEU A 141 ? ? -39.07 131.74 2 1 THR A 147 ? ? 81.82 -12.88 3 1 ASN A 177 ? ? -68.65 95.92 4 1 VAL A 238 ? ? -57.72 103.67 5 1 VAL A 260 ? ? -172.39 139.47 6 1 SER A 313 ? ? -117.46 -169.68 7 1 THR A 335 ? ? -25.33 126.18 8 1 ASN A 404 ? ? -119.38 -147.14 9 1 ALA A 411 ? ? -67.90 -178.60 10 1 GLU B 37 ? ? -67.45 96.43 11 1 VAL B 83 ? ? -145.50 -27.52 12 1 TYR B 85 ? ? -107.51 51.13 13 1 ASN B 87 ? ? -112.18 78.71 14 1 LEU B 109 ? ? -68.15 69.14 15 1 ASN B 120 ? ? -123.03 -154.83 16 1 ASN B 168 ? ? -119.52 -152.18 17 1 GLU B 215 ? ? -107.78 64.40 # 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 LYS 419 ? A LYS 392 2 1 Y 1 A HIS 420 ? A HIS 393 3 1 Y 1 A HIS 421 ? A HIS 394 4 1 Y 1 A HIS 422 ? A HIS 395 5 1 Y 1 A HIS 423 ? A HIS 396 6 1 Y 1 A HIS 424 ? A HIS 397 7 1 Y 1 A HIS 425 ? A HIS 398 8 1 Y 1 B MET 1 ? B MET 1 9 1 Y 1 B LEU 2 ? B LEU 2 10 1 Y 1 B SER 3 ? B SER 3 11 1 Y 1 B GLY 4 ? B GLY 4 12 1 Y 1 B VAL 5 ? B VAL 5 13 1 Y 1 B TRP 6 ? B TRP 6 14 1 Y 1 B PHE 7 ? B PHE 7 15 1 Y 1 B LEU 8 ? B LEU 8 16 1 Y 1 B SER 9 ? B SER 9 17 1 Y 1 B VAL 10 ? B VAL 10 18 1 Y 1 B LEU 11 ? B LEU 11 19 1 Y 1 B THR 12 ? B THR 12 20 1 Y 1 B VAL 13 ? B VAL 13 21 1 Y 1 B ALA 14 ? B ALA 14 22 1 Y 1 B GLY 15 ? B GLY 15 23 1 Y 1 B ILE 16 ? B ILE 16 24 1 Y 1 B LEU 17 ? B LEU 17 25 1 Y 1 B GLN 18 ? B GLN 18 26 1 Y 1 B THR 19 ? B THR 19 27 1 Y 1 B GLU 20 ? B GLU 20 28 1 Y 1 B SER 21 ? B SER 21 29 1 Y 1 B ARG 22 ? B ARG 22 30 1 Y 1 B LYS 23 ? B LYS 23 31 1 Y 1 B THR 24 ? B THR 24 32 1 Y 1 B ALA 25 ? B ALA 25 33 1 Y 1 B LYS 26 ? B LYS 26 34 1 Y 1 B ASP 27 ? B ASP 27 35 1 Y 1 B ILE 28 ? B ILE 28 36 1 Y 1 B PRO 264 ? B PRO 264 37 1 Y 1 B ARG 265 ? B ARG 265 38 1 Y 1 B LYS 266 ? B LYS 266 39 1 Y 1 B HIS 267 ? B HIS 267 40 1 Y 1 B HIS 268 ? B HIS 268 41 1 Y 1 B HIS 269 ? B HIS 269 42 1 Y 1 B HIS 270 ? B HIS 270 43 1 Y 1 B HIS 271 ? B HIS 271 44 1 Y 1 B HIS 272 ? B HIS 272 # _pdbx_audit_support.funding_organization ? _pdbx_audit_support.country Japan _pdbx_audit_support.grant_number ? _pdbx_audit_support.ordinal 1 # _pdbx_entity_nonpoly.entity_id 3 _pdbx_entity_nonpoly.name N-ACETYL-D-GLUCOSAMINE _pdbx_entity_nonpoly.comp_id NAG #