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*** MADHURJA A1AT ***elNémo ID: 260222213347826239Job options:ID = 260222213347826239 JOBID = MADHURJA A1AT USERID = madhurja1207 PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER MADHURJA A1AT data_1QLP # _entry.id 1QLP # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.382 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code _database_2.pdbx_database_accession _database_2.pdbx_DOI PDB 1QLP pdb_00001qlp 10.2210/pdb1qlp/pdb PDBE EBI-4094 ? ? WWPDB D_1290004094 ? ? # _pdbx_database_PDB_obs_spr.id SPRSDE _pdbx_database_PDB_obs_spr.date 1999-09-27 _pdbx_database_PDB_obs_spr.pdb_id 1QLP _pdbx_database_PDB_obs_spr.replace_pdb_id 2PSI _pdbx_database_PDB_obs_spr.details ? # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.content_type _pdbx_database_related.details PDB 7API unspecified 'MODIFIED ALPHA-1-ANTITRYPSIN (TETRAGONAL FORM 1)' PDB 8API unspecified 'MODIFIED ALPHA-1-PROTEINASE INHIBITOR (HEXAGONAL)' PDB 9API unspecified 'MODIFIED ALPHA-1-ANTITRYPSIN (TETRAGONAL FORM 2)' PDB 1PSI unspecified 'INTACT RECOMBINED ALPHA-1-ANTITRYPSIN MUTANT PHE 51 TO LEU' PDB 2PSI unspecified 'INTACT WILDTYPE RECOMBINANT ALPHA-1-ANTITRYPSIN' PDB 1ATU unspecified 'UNCLEAVED ALPHA-1-ANTITRYPSIN' PDB 1KCT unspecified ALPHA1-ANTITRYPSIN # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 1QLP _pdbx_database_status.deposit_site PDBE _pdbx_database_status.process_site PDBE _pdbx_database_status.SG_entry . _pdbx_database_status.recvd_initial_deposition_date 1999-09-10 _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? _pdbx_database_status.status_code_nmr_data ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Elliott, P.R.' 1 'Pei, X.Y.' 2 'Dafforn, T.' 3 'Read, R.J.' 4 'Carrell, R.W.' 5 'Lomas, D.A.' 6 # loop_ _citation.id _citation.title _citation.journal_abbrev _citation.journal_volume _citation.page_first _citation.page_last _citation.year _citation.journal_id_ASTM _citation.country _citation.journal_id_ISSN _citation.journal_id_CSD _citation.book_publisher _citation.pdbx_database_id_PubMed _citation.pdbx_database_id_DOI primary 'Topography of a 2.0 A structure of alpha1-antitrypsin reveals targets for rational drug design to prevent conformational disease.' 'Protein Sci.' 9 1274 1281 2000 PRCIEI US 0961-8368 0795 ? 10933492 10.1110/ps.9.7.1274 1 'Wildtype Alpha1-Antitrypsin is in the Canonical Inhibitory Conformation' J.Mol.Biol. 275 419 ? 1998 JMOBAK UK 0022-2836 0070 ? 9466920 10.1006/JMBI.1997.1458 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal _citation_author.identifier_ORCID primary 'Elliott, P.R.' 1 ? primary 'Pei, X.Y.' 2 ? primary 'Dafforn, T.R.' 3 ? primary 'Lomas, D.A.' 4 ? 1 'Elliott, P.R.' 5 ? 1 'Abrahams, J.-P.' 6 ? 1 'Lomas, D.A.' 7 ? # _cell.entry_id 1QLP _cell.length_a 114.680 _cell.length_b 39.260 _cell.length_c 90.270 _cell.angle_alpha 90.00 _cell.angle_beta 104.21 _cell.angle_gamma 90.00 _cell.Z_PDB 4 _cell.pdbx_unique_axis ? # _symmetry.entry_id 1QLP _symmetry.space_group_name_H-M 'C 1 2 1' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 5 # 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 ALPHA-1-ANTITRYPSIN 44380.441 1 ? ? ? ? 2 water nat water 18.015 106 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'ALPHA-1-PROTEINASE INHIBITOR, ALPHA-1-ANTIPROTEINASE' # _entity_poly.entity_id 1 _entity_poly.type 'polypeptide(L)' _entity_poly.nstd_linkage no _entity_poly.nstd_monomer no _entity_poly.pdbx_seq_one_letter_code ;MDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGL NFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDY VEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVL LMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLKSVLGQLGITKVFSNGADLSG VTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK ; _entity_poly.pdbx_seq_one_letter_code_can ;MDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGL NFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDY VEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVL LMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLKSVLGQLGITKVFSNGADLSG VTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK ; _entity_poly.pdbx_strand_id A _entity_poly.pdbx_target_identifier ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 MET n 1 2 ASP n 1 3 PRO n 1 4 GLN n 1 5 GLY n 1 6 ASP n 1 7 ALA n 1 8 ALA n 1 9 GLN n 1 10 LYS n 1 11 THR n 1 12 ASP n 1 13 THR n 1 14 SER n 1 15 HIS n 1 16 HIS n 1 17 ASP n 1 18 GLN n 1 19 ASP n 1 20 HIS n 1 21 PRO n 1 22 THR n 1 23 PHE n 1 24 ASN n 1 25 LYS n 1 26 ILE n 1 27 THR n 1 28 PRO n 1 29 ASN n 1 30 LEU n 1 31 ALA n 1 32 GLU n 1 33 PHE n 1 34 ALA n 1 35 PHE n 1 36 SER n 1 37 LEU n 1 38 TYR n 1 39 ARG n 1 40 GLN n 1 41 LEU n 1 42 ALA n 1 43 HIS n 1 44 GLN n 1 45 SER n 1 46 ASN n 1 47 SER n 1 48 THR n 1 49 ASN n 1 50 ILE n 1 51 PHE n 1 52 PHE n 1 53 SER n 1 54 PRO n 1 55 VAL n 1 56 SER n 1 57 ILE n 1 58 ALA n 1 59 THR n 1 60 ALA n 1 61 PHE n 1 62 ALA n 1 63 MET n 1 64 LEU n 1 65 SER n 1 66 LEU n 1 67 GLY n 1 68 THR n 1 69 LYS n 1 70 ALA n 1 71 ASP n 1 72 THR n 1 73 HIS n 1 74 ASP n 1 75 GLU n 1 76 ILE n 1 77 LEU n 1 78 GLU n 1 79 GLY n 1 80 LEU n 1 81 ASN n 1 82 PHE n 1 83 ASN n 1 84 LEU n 1 85 THR n 1 86 GLU n 1 87 ILE n 1 88 PRO n 1 89 GLU n 1 90 ALA n 1 91 GLN n 1 92 ILE n 1 93 HIS n 1 94 GLU n 1 95 GLY n 1 96 PHE n 1 97 GLN n 1 98 GLU n 1 99 LEU n 1 100 LEU n 1 101 ARG n 1 102 THR n 1 103 LEU n 1 104 ASN n 1 105 GLN n 1 106 PRO n 1 107 ASP n 1 108 SER n 1 109 GLN n 1 110 LEU n 1 111 GLN n 1 112 LEU n 1 113 THR n 1 114 THR n 1 115 GLY n 1 116 ASN n 1 117 GLY n 1 118 LEU n 1 119 PHE n 1 120 LEU n 1 121 SER n 1 122 GLU n 1 123 GLY n 1 124 LEU n 1 125 LYS n 1 126 LEU n 1 127 VAL n 1 128 ASP n 1 129 LYS n 1 130 PHE n 1 131 LEU n 1 132 GLU n 1 133 ASP n 1 134 VAL n 1 135 LYS n 1 136 LYS n 1 137 LEU n 1 138 TYR n 1 139 HIS n 1 140 SER n 1 141 GLU n 1 142 ALA n 1 143 PHE n 1 144 THR n 1 145 VAL n 1 146 ASN n 1 147 PHE n 1 148 GLY n 1 149 ASP n 1 150 THR n 1 151 GLU n 1 152 GLU n 1 153 ALA n 1 154 LYS n 1 155 LYS n 1 156 GLN n 1 157 ILE n 1 158 ASN n 1 159 ASP n 1 160 TYR n 1 161 VAL n 1 162 GLU n 1 163 LYS n 1 164 GLY n 1 165 THR n 1 166 GLN n 1 167 GLY n 1 168 LYS n 1 169 ILE n 1 170 VAL n 1 171 ASP n 1 172 LEU n 1 173 VAL n 1 174 LYS n 1 175 GLU n 1 176 LEU n 1 177 ASP n 1 178 ARG n 1 179 ASP n 1 180 THR n 1 181 VAL n 1 182 PHE n 1 183 ALA n 1 184 LEU n 1 185 VAL n 1 186 ASN n 1 187 TYR n 1 188 ILE n 1 189 PHE n 1 190 PHE n 1 191 LYS n 1 192 GLY n 1 193 LYS n 1 194 TRP n 1 195 GLU n 1 196 ARG n 1 197 PRO n 1 198 PHE n 1 199 GLU n 1 200 VAL n 1 201 LYS n 1 202 ASP n 1 203 THR n 1 204 GLU n 1 205 GLU n 1 206 GLU n 1 207 ASP n 1 208 PHE n 1 209 HIS n 1 210 VAL n 1 211 ASP n 1 212 GLN n 1 213 VAL n 1 214 THR n 1 215 THR n 1 216 VAL n 1 217 LYS n 1 218 VAL n 1 219 PRO n 1 220 MET n 1 221 MET n 1 222 LYS n 1 223 ARG n 1 224 LEU n 1 225 GLY n 1 226 MET n 1 227 PHE n 1 228 ASN n 1 229 ILE n 1 230 GLN n 1 231 HIS n 1 232 CYS n 1 233 LYS n 1 234 LYS n 1 235 LEU n 1 236 SER n 1 237 SER n 1 238 TRP n 1 239 VAL n 1 240 LEU n 1 241 LEU n 1 242 MET n 1 243 LYS n 1 244 TYR n 1 245 LEU n 1 246 GLY n 1 247 ASN n 1 248 ALA n 1 249 THR n 1 250 ALA n 1 251 ILE n 1 252 PHE n 1 253 PHE n 1 254 LEU n 1 255 PRO n 1 256 ASP n 1 257 GLU n 1 258 GLY n 1 259 LYS n 1 260 LEU n 1 261 GLN n 1 262 HIS n 1 263 LEU n 1 264 GLU n 1 265 ASN n 1 266 GLU n 1 267 LEU n 1 268 THR n 1 269 HIS n 1 270 ASP n 1 271 ILE n 1 272 ILE n 1 273 THR n 1 274 LYS n 1 275 PHE n 1 276 LEU n 1 277 GLU n 1 278 ASN n 1 279 GLU n 1 280 ASP n 1 281 ARG n 1 282 ARG n 1 283 SER n 1 284 ALA n 1 285 SER n 1 286 LEU n 1 287 HIS n 1 288 LEU n 1 289 PRO n 1 290 LYS n 1 291 LEU n 1 292 SER n 1 293 ILE n 1 294 THR n 1 295 GLY n 1 296 THR n 1 297 TYR n 1 298 ASP n 1 299 LEU n 1 300 LYS n 1 301 SER n 1 302 VAL n 1 303 LEU n 1 304 GLY n 1 305 GLN n 1 306 LEU n 1 307 GLY n 1 308 ILE n 1 309 THR n 1 310 LYS n 1 311 VAL n 1 312 PHE n 1 313 SER n 1 314 ASN n 1 315 GLY n 1 316 ALA n 1 317 ASP n 1 318 LEU n 1 319 SER n 1 320 GLY n 1 321 VAL n 1 322 THR n 1 323 GLU n 1 324 GLU n 1 325 ALA n 1 326 PRO n 1 327 LEU n 1 328 LYS n 1 329 LEU n 1 330 SER n 1 331 LYS n 1 332 ALA n 1 333 VAL n 1 334 HIS n 1 335 LYS n 1 336 ALA n 1 337 VAL n 1 338 LEU n 1 339 THR n 1 340 ILE n 1 341 ASP n 1 342 GLU n 1 343 LYS n 1 344 GLY n 1 345 THR n 1 346 GLU n 1 347 ALA n 1 348 ALA n 1 349 GLY n 1 350 ALA n 1 351 MET n 1 352 PHE n 1 353 LEU n 1 354 GLU n 1 355 ALA n 1 356 ILE n 1 357 PRO n 1 358 MET n 1 359 SER n 1 360 ILE n 1 361 PRO n 1 362 PRO n 1 363 GLU n 1 364 VAL n 1 365 LYS n 1 366 PHE n 1 367 ASN n 1 368 LYS n 1 369 PRO n 1 370 PHE n 1 371 VAL n 1 372 PHE n 1 373 LEU n 1 374 MET n 1 375 ILE n 1 376 GLU n 1 377 GLN n 1 378 ASN n 1 379 THR n 1 380 LYS n 1 381 SER n 1 382 PRO n 1 383 LEU n 1 384 PHE n 1 385 MET n 1 386 GLY n 1 387 LYS n 1 388 VAL n 1 389 VAL n 1 390 ASN n 1 391 PRO n 1 392 THR n 1 393 GLN n 1 394 LYS n # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _entity_src_gen.pdbx_seq_type ? _entity_src_gen.pdbx_beg_seq_num ? _entity_src_gen.pdbx_end_seq_num ? _entity_src_gen.gene_src_common_name HUMAN _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene ALPHA-1-ANTITRYPSIN _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain ? _entity_src_gen.gene_src_tissue HEPATOCYTES _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 'HOMO SAPIENS' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 9606 _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 LIVER _entity_src_gen.pdbx_gene_src_organelle ? _entity_src_gen.pdbx_gene_src_cell NEUTROPHILS _entity_src_gen.pdbx_gene_src_cellular_location CYTOPLASM _entity_src_gen.host_org_common_name ? _entity_src_gen.pdbx_host_org_scientific_name 'ESCHERICHIA COLI' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 469008 _entity_src_gen.host_org_genus ? _entity_src_gen.pdbx_host_org_gene ALPHA-1-ANTITRYPSIN _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 'BL21(DE3)' _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 PTERMAT _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code A1AT_HUMAN _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ? _struct_ref.pdbx_align_begin ? _struct_ref.pdbx_db_accession P01009 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 1QLP _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 2 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 394 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession P01009 _struct_ref_seq.db_align_beg 26 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 418 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 2 _struct_ref_seq.pdbx_auth_seq_align_end 394 # _struct_ref_seq_dif.align_id 1 _struct_ref_seq_dif.pdbx_pdb_id_code 1QLP _struct_ref_seq_dif.mon_id MET _struct_ref_seq_dif.pdbx_pdb_strand_id A _struct_ref_seq_dif.seq_num 1 _struct_ref_seq_dif.pdbx_pdb_ins_code ? _struct_ref_seq_dif.pdbx_seq_db_name UNP _struct_ref_seq_dif.pdbx_seq_db_accession_code P01009 _struct_ref_seq_dif.db_mon_id ? _struct_ref_seq_dif.pdbx_seq_db_seq_num ? _struct_ref_seq_dif.details 'cloning artifact' _struct_ref_seq_dif.pdbx_auth_seq_num 1 _struct_ref_seq_dif.pdbx_ordinal 1 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 1QLP _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.6 _exptl_crystal.density_percent_sol 37.2 _exptl_crystal.description 'DATA WERE COLLECTED USING THE OSCILLATION METHOD.' # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method ? _exptl_crystal_grow.temp ? _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 6.00 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details '24% PEG 4000, 0.2 M SODIUM ACETATE, 0.1M TRIS-HCL PH 6.0, 2MM FESO4.7H20' # _diffrn.id 1 _diffrn.ambient_temp 100.0 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type MARRESEARCH _diffrn_detector.pdbx_collection_date 1998-09-09 _diffrn_detector.details MIRRORS # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator 'BENT CYLINDRICAL GE(111)' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.87 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'SRS BEAMLINE PX9.6' _diffrn_source.pdbx_synchrotron_site SRS _diffrn_source.pdbx_synchrotron_beamline PX9.6 _diffrn_source.pdbx_wavelength 0.87 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 1QLP _reflns.observed_criterion_sigma_I 2.000 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 25.000 _reflns.d_resolution_high 2.000 _reflns.number_obs 25057 _reflns.number_all ? _reflns.percent_possible_obs 93.6 _reflns.pdbx_Rmerge_I_obs 0.07900 _reflns.pdbx_Rsym_value 0.06700 _reflns.pdbx_netI_over_sigmaI 5.9000 _reflns.B_iso_Wilson_estimate 29.41 _reflns.pdbx_redundancy 3.300 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 2.00 _reflns_shell.d_res_low 2.05 _reflns_shell.percent_possible_all 95.2 _reflns_shell.Rmerge_I_obs 0.51400 _reflns_shell.pdbx_Rsym_value 0.41500 _reflns_shell.meanI_over_sigI_obs 1.600 _reflns_shell.pdbx_redundancy 2.40 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 1QLP _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 25039 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 0.0 _refine.pdbx_data_cutoff_high_absF 0.0 _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 25.0 _refine.ls_d_res_high 2.0 _refine.ls_percent_reflns_obs 93.6 _refine.ls_R_factor_obs 0.231 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.231 _refine.ls_R_factor_R_free 0.266 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 4.7 _refine.ls_number_reflns_R_free 1271 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.B_iso_mean 38.38 _refine.aniso_B[1][1] -4.094 _refine.aniso_B[2][2] 0.601 _refine.aniso_B[3][3] 3.493 _refine.aniso_B[1][2] 0.000 _refine.aniso_B[1][3] -6.005 _refine.aniso_B[2][3] 0.000 _refine.solvent_model_details CNS _refine.solvent_model_param_ksol 1.257 _refine.solvent_model_param_bsol 215 _refine.pdbx_solvent_vdw_probe_radii ? _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii ? _refine.pdbx_ls_cross_valid_method 'FREE R-VALUE' _refine.details 'THE N-TERMINAL RESIDUES 1-22 WERE NOT OBSERVED IN THE ELECTRON DENSITY MAPS' _refine.pdbx_starting_model 'THERMOSTABLE VARIANT ALPHA1-ANTITRYPSIN (PDB ENTRY 1PSI)' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model RESTRAINED _refine.pdbx_stereochemistry_target_values ? _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML ? _refine.pdbx_overall_phase_error ? _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_analyze.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_analyze.entry_id 1QLP _refine_analyze.Luzzati_coordinate_error_obs 0.28 _refine_analyze.Luzzati_sigma_a_obs 0.24 _refine_analyze.Luzzati_d_res_low_obs 0.0 _refine_analyze.Luzzati_coordinate_error_free 0.34 _refine_analyze.Luzzati_sigma_a_free 0.25 _refine_analyze.Luzzati_d_res_low_free ? _refine_analyze.number_disordered_residues ? _refine_analyze.occupancy_sum_hydrogen ? _refine_analyze.occupancy_sum_non_hydrogen ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 2956 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 0 _refine_hist.number_atoms_solvent 106 _refine_hist.number_atoms_total 3062 _refine_hist.d_res_high 2.0 _refine_hist.d_res_low 25.0 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function c_bond_d 0.006917 ? ? ? 'X-RAY DIFFRACTION' ? c_bond_d_na ? ? ? ? 'X-RAY DIFFRACTION' ? c_bond_d_prot ? ? ? ? 'X-RAY DIFFRACTION' ? c_angle_d ? ? ? ? 'X-RAY DIFFRACTION' ? c_angle_d_na ? ? ? ? 'X-RAY DIFFRACTION' ? c_angle_d_prot ? ? ? ? 'X-RAY DIFFRACTION' ? c_angle_deg 1.30665 ? ? ? 'X-RAY DIFFRACTION' ? c_angle_deg_na ? ? ? ? 'X-RAY DIFFRACTION' ? c_angle_deg_prot ? ? ? ? 'X-RAY DIFFRACTION' ? c_dihedral_angle_d 24.95182 ? ? ? 'X-RAY DIFFRACTION' ? c_dihedral_angle_d_na ? ? ? ? 'X-RAY DIFFRACTION' ? c_dihedral_angle_d_prot ? ? ? ? 'X-RAY DIFFRACTION' ? c_improper_angle_d 1.23128 ? ? ? 'X-RAY DIFFRACTION' ? c_improper_angle_d_na ? ? ? ? 'X-RAY DIFFRACTION' ? c_improper_angle_d_prot ? ? ? ? 'X-RAY DIFFRACTION' ? c_mcbond_it 3.502 1.5 ? ? 'X-RAY DIFFRACTION' ? c_mcangle_it 4.732 2.0 ? ? 'X-RAY DIFFRACTION' ? c_scbond_it 2.219 2.00 ? ? 'X-RAY DIFFRACTION' ? c_scangle_it 3.453 2.5 ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.pdbx_total_number_of_bins_used 10 _refine_ls_shell.d_res_high 2.0 _refine_ls_shell.d_res_low 2.07 _refine_ls_shell.number_reflns_R_work 1837 _refine_ls_shell.R_factor_R_work 0.297 _refine_ls_shell.percent_reflns_obs 72.9 _refine_ls_shell.R_factor_R_free 0.334 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free 4.7 _refine_ls_shell.number_reflns_R_free 96 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? # loop_ _pdbx_xplor_file.pdbx_refine_id _pdbx_xplor_file.serial_no _pdbx_xplor_file.param_file _pdbx_xplor_file.topol_file 'X-RAY DIFFRACTION' 1 CNS_TOPPAR:PROTEIN_REP.PARAM ? 'X-RAY DIFFRACTION' 2 CNS_TOPPAR:WATER_REP.PARAM ? # _struct.entry_id 1QLP _struct.title '2.0 ANGSTROM STRUCTURE OF INTACT ALPHA-1-ANTITRYPSIN: A CANONICAL TEMPLATE FOR ACTIVE SERPINS' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 1QLP _struct_keywords.pdbx_keywords 'SERINE PROTEASE INHIBITOR' _struct_keywords.text 'SERINE PROTEASE INHIBITOR, SERPIN, GLYCOPROTEIN, POLYMORPHISM, EMPHYSEMA, DISEASE MUTATION, ACUTE PHASE' # 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 ? # _struct_biol.id 1 # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 ILE A 26 ? SER A 45 ? ILE A 26 SER A 45 1 ? 20 HELX_P HELX_P2 2 SER A 53 ? LEU A 66 ? SER A 53 LEU A 66 1 ? 14 HELX_P HELX_P3 3 LYS A 69 ? LEU A 80 ? LYS A 69 LEU A 80 1 ? 12 HELX_P HELX_P4 4 PRO A 88 ? ASN A 104 ? PRO A 88 ASN A 104 1 ? 17 HELX_P HELX_P5 5 VAL A 127 ? LEU A 137 ? VAL A 127 LEU A 137 1 ? 11 HELX_P HELX_P6 6 ASP A 149 ? THR A 165 ? ASP A 149 THR A 165 1 ? 17 HELX_P HELX_P7 7 GLU A 199 ? THR A 203 ? GLU A 199 THR A 203 5 ? 5 HELX_P HELX_P8 8 LYS A 259 ? LEU A 267 ? LYS A 259 LEU A 267 1 ? 9 HELX_P HELX_P9 9 THR A 268 ? ASN A 278 ? THR A 268 ASN A 278 1 ? 11 HELX_P HELX_P10 10 LEU A 299 ? LEU A 303 ? LEU A 299 LEU A 303 1 ? 5 HELX_P HELX_P11 11 GLY A 304 ? GLY A 307 ? GLY A 304 GLY A 307 5 ? 4 HELX_P HELX_P12 12 THR A 309 ? SER A 313 ? THR A 309 SER A 313 5 ? 5 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 6 ? B ? 5 ? C ? 4 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? anti-parallel A 2 3 ? anti-parallel A 3 4 ? anti-parallel A 4 5 ? anti-parallel A 5 6 ? anti-parallel B 1 2 ? parallel B 2 3 ? anti-parallel B 3 4 ? parallel B 4 5 ? anti-parallel C 1 2 ? anti-parallel C 2 3 ? anti-parallel C 3 4 ? parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 ILE A 50 ? PHE A 52 ? ILE A 50 PHE A 52 A 2 PRO A 382 ? VAL A 388 ? PRO A 382 VAL A 388 A 3 PHE A 370 ? GLU A 376 ? PHE A 370 GLU A 376 A 4 ALA A 248 ? PRO A 255 ? ALA A 248 PRO A 255 A 5 SER A 237 ? TYR A 244 ? SER A 237 TYR A 244 A 6 ASN A 228 ? CYS A 232 ? ASN A 228 CYS A 232 B 1 GLU A 141 ? VAL A 145 ? GLU A 141 VAL A 145 B 2 LEU A 112 ? SER A 121 ? LEU A 112 SER A 121 B 3 PHE A 182 ? PHE A 190 ? PHE A 182 PHE A 190 B 4 LYS A 331 ? ILE A 340 ? LYS A 331 ILE A 340 B 5 LEU A 291 ? ASP A 298 ? LEU A 291 ASP A 298 C 1 GLU A 204 ? HIS A 209 ? GLU A 204 HIS A 209 C 2 THR A 215 ? PHE A 227 ? THR A 215 PHE A 227 C 3 ARG A 282 ? PRO A 289 ? ARG A 282 PRO A 289 C 4 PRO A 362 ? LYS A 365 ? PRO A 362 LYS A 365 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 O ILE A 50 ? O ILE A 50 N LYS A 387 ? N LYS A 387 A 2 3 O LEU A 383 ? O LEU A 383 N MET A 374 ? N MET A 374 A 3 4 O VAL A 371 ? O VAL A 371 N PHE A 253 ? N PHE A 253 A 4 5 O ALA A 248 ? O ALA A 248 N TYR A 244 ? N TYR A 244 A 5 6 O SER A 237 ? O SER A 237 N CYS A 232 ? N CYS A 232 B 1 2 O GLU A 141 ? O GLU A 141 N LEU A 118 ? N LEU A 118 B 2 3 O THR A 113 ? O THR A 113 N PHE A 189 ? N PHE A 189 B 3 4 O LEU A 184 ? O LEU A 184 N LYS A 331 ? N LYS A 331 B 4 5 O HIS A 334 ? O HIS A 334 N TYR A 297 ? N TYR A 297 C 1 2 O GLU A 204 ? O GLU A 204 N MET A 220 ? N MET A 220 C 2 3 O MET A 221 ? O MET A 221 N LEU A 288 ? N LEU A 288 C 3 4 O SER A 285 ? O SER A 285 N PRO A 362 ? N PRO A 362 # _database_PDB_matrix.entry_id 1QLP _database_PDB_matrix.origx[1][1] 1.000000 _database_PDB_matrix.origx[1][2] 0.000000 _database_PDB_matrix.origx[1][3] 0.000000 _database_PDB_matrix.origx[2][1] 0.000000 _database_PDB_matrix.origx[2][2] 1.000000 _database_PDB_matrix.origx[2][3] 0.000000 _database_PDB_matrix.origx[3][1] 0.000000 _database_PDB_matrix.origx[3][2] 0.000000 _database_PDB_matrix.origx[3][3] 1.000000 _database_PDB_matrix.origx_vector[1] 0.00000 _database_PDB_matrix.origx_vector[2] 0.00000 _database_PDB_matrix.origx_vector[3] 0.00000 # _atom_sites.entry_id 1QLP _atom_sites.fract_transf_matrix[1][1] 0.008720 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.002208 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.025471 _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] 0.011427 _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 . PHE A 1 23 ? 8.404 13.439 14.171 1.00 73.50 ? 23 PHE A N 1 ATOM 2 C CA . PHE A 1 23 ? 8.944 14.771 13.781 1.00 74.67 ? 23 PHE A CA 1 ATOM 3 C C . PHE A 1 23 ? 10.393 14.658 13.315 1.00 71.16 ? 23 PHE A C 1 ATOM 4 O O . PHE A 1 23 ? 11.275 15.387 13.757 1.00 70.18 ? 23 PHE A O 1 ATOM 5 C CB . PHE A 1 23 ? 8.823 15.773 14.924 1.00 76.76 ? 23 PHE A CB 1 ATOM 6 C CG . PHE A 1 23 ? 8.650 17.194 14.463 1.00 79.59 ? 23 PHE A CG 1 ATOM 7 C CD1 . PHE A 1 23 ? 7.385 17.695 14.203 1.00 80.15 ? 23 PHE A CD1 1 ATOM 8 C CD2 . PHE A 1 23 ? 9.745 18.023 14.291 1.00 80.49 ? 23 PHE A CD2 1 ATOM 9 C CE1 . PHE A 1 23 ? 7.214 18.999 13.780 1.00 81.46 ? 23 PHE A CE1 1 ATOM 10 C CE2 . PHE A 1 23 ? 9.581 19.327 13.868 1.00 82.12 ? 23 PHE A CE2 1 ATOM 11 C CZ . PHE A 1 23 ? 8.314 19.816 13.612 1.00 82.36 ? 23 PHE A CZ 1 ATOM 12 N N . ASN A 1 24 ? 10.623 13.719 12.412 1.00 63.74 ? 24 ASN A N 1 ATOM 13 C CA . ASN A 1 24 ? 11.941 13.470 11.843 1.00 60.42 ? 24 ASN A CA 1 ATOM 14 C C . ASN A 1 24 ? 11.772 12.629 10.576 1.00 56.00 ? 24 ASN A C 1 ATOM 15 O O . ASN A 1 24 ? 10.941 11.722 10.547 1.00 53.92 ? 24 ASN A O 1 ATOM 16 C CB . ASN A 1 24 ? 12.867 12.784 12.835 1.00 60.68 ? 24 ASN A CB 1 ATOM 17 C CG . ASN A 1 24 ? 14.281 12.618 12.314 1.00 60.90 ? 24 ASN A CG 1 ATOM 18 O OD1 . ASN A 1 24 ? 14.500 11.985 11.279 1.00 61.47 ? 24 ASN A OD1 1 ATOM 19 N ND2 . ASN A 1 24 ? 15.249 13.183 13.026 1.00 60.40 ? 24 ASN A ND2 1 ATOM 20 N N . LYS A 1 25 ? 12.534 12.952 9.548 1.00 51.32 ? 25 LYS A N 1 ATOM 21 C CA . LYS A 1 25 ? 12.467 12.268 8.274 1.00 48.21 ? 25 LYS A CA 1 ATOM 22 C C . LYS A 1 25 ? 12.601 10.760 8.393 1.00 42.21 ? 25 LYS A C 1 ATOM 23 O O . LYS A 1 25 ? 11.996 10.028 7.601 1.00 43.46 ? 25 LYS A O 1 ATOM 24 C CB . LYS A 1 25 ? 13.551 12.810 7.326 1.00 49.26 ? 25 LYS A CB 1 ATOM 25 C CG . LYS A 1 25 ? 13.096 12.970 5.891 1.00 51.15 ? 25 LYS A CG 1 ATOM 26 C CD . LYS A 1 25 ? 12.500 11.697 5.322 1.00 51.76 ? 25 LYS A CD 1 ATOM 27 C CE . LYS A 1 25 ? 12.130 11.879 3.854 1.00 52.81 ? 25 LYS A CE 1 ATOM 28 N NZ . LYS A 1 25 ? 11.199 10.814 3.387 1.00 52.89 ? 25 LYS A NZ 1 ATOM 29 N N . ILE A 1 26 ? 13.389 10.280 9.355 1.00 34.41 ? 26 ILE A N 1 ATOM 30 C CA . ILE A 1 26 ? 13.588 8.839 9.477 1.00 34.25 ? 26 ILE A CA 1 ATOM 31 C C . ILE A 1 26 ? 12.711 8.197 10.532 1.00 31.85 ? 26 ILE A C 1 ATOM 32 O O . ILE A 1 26 ? 12.796 6.983 10.737 1.00 30.80 ? 26 ILE A O 1 ATOM 33 C CB . ILE A 1 26 ? 15.064 8.486 9.711 1.00 32.35 ? 26 ILE A CB 1 ATOM 34 C CG1 . ILE A 1 26 ? 15.501 8.839 11.131 1.00 32.68 ? 26 ILE A CG1 1 ATOM 35 C CG2 . ILE A 1 26 ? 15.940 9.201 8.683 1.00 32.86 ? 26 ILE A CG2 1 ATOM 36 C CD1 . ILE A 1 26 ? 16.824 8.220 11.531 1.00 30.40 ? 26 ILE A CD1 1 ATOM 37 N N . THR A 1 27 ? 11.860 8.972 11.188 1.00 34.50 ? 27 THR A N 1 ATOM 38 C CA . THR A 1 27 ? 10.975 8.442 12.222 1.00 34.39 ? 27 THR A CA 1 ATOM 39 C C . THR A 1 27 ? 10.067 7.338 11.730 1.00 33.40 ? 27 THR A C 1 ATOM 40 O O . THR A 1 27 ? 9.965 6.280 12.365 1.00 37.57 ? 27 THR A O 1 ATOM 41 C CB . THR A 1 27 ? 10.161 9.556 12.900 1.00 33.68 ? 27 THR A CB 1 ATOM 42 O OG1 . THR A 1 27 ? 10.995 10.189 13.887 1.00 35.78 ? 27 THR A OG1 1 ATOM 43 C CG2 . THR A 1 27 ? 8.928 8.995 13.587 1.00 33.91 ? 27 THR A CG2 1 ATOM 44 N N . PRO A 1 28 ? 9.411 7.535 10.597 1.00 36.60 ? 28 PRO A N 1 ATOM 45 C CA . PRO A 1 28 ? 8.539 6.533 10.013 1.00 33.20 ? 28 PRO A CA 1 ATOM 46 C C . PRO A 1 28 ? 9.267 5.217 9.788 1.00 32.76 ? 28 PRO A C 1 ATOM 47 O O . PRO A 1 28 ? 8.703 4.139 9.995 1.00 29.95 ? 28 PRO A O 1 ATOM 48 C CB . PRO A 1 28 ? 8.074 7.148 8.707 1.00 35.63 ? 28 PRO A CB 1 ATOM 49 C CG . PRO A 1 28 ? 8.315 8.609 8.843 1.00 39.38 ? 28 PRO A CG 1 ATOM 50 C CD . PRO A 1 28 ? 9.483 8.767 9.778 1.00 35.35 ? 28 PRO A CD 1 ATOM 51 N N . ASN A 1 29 ? 10.525 5.298 9.361 1.00 28.20 ? 29 ASN A N 1 ATOM 52 C CA . ASN A 1 29 ? 11.342 4.122 9.104 1.00 26.54 ? 29 ASN A CA 1 ATOM 53 C C . ASN A 1 29 ? 11.688 3.373 10.393 1.00 23.06 ? 29 ASN A C 1 ATOM 54 O O . ASN A 1 29 ? 11.623 2.142 10.425 1.00 21.81 ? 29 ASN A O 1 ATOM 55 C CB . ASN A 1 29 ? 12.642 4.516 8.390 1.00 27.00 ? 29 ASN A CB 1 ATOM 56 C CG . ASN A 1 29 ? 12.387 5.272 7.099 1.00 25.94 ? 29 ASN A CG 1 ATOM 57 O OD1 . ASN A 1 29 ? 12.124 4.671 6.055 1.00 27.92 ? 29 ASN A OD1 1 ATOM 58 N ND2 . ASN A 1 29 ? 12.458 6.588 7.169 1.00 27.04 ? 29 ASN A ND2 1 ATOM 59 N N . LEU A 1 30 ? 12.099 4.114 11.408 1.00 24.15 ? 30 LEU A N 1 ATOM 60 C CA . LEU A 1 30 ? 12.439 3.561 12.709 1.00 26.20 ? 30 LEU A CA 1 ATOM 61 C C . LEU A 1 30 ? 11.230 2.898 13.360 1.00 23.19 ? 30 LEU A C 1 ATOM 62 O O . LEU A 1 30 ? 11.376 1.865 14.016 1.00 26.39 ? 30 LEU A O 1 ATOM 63 C CB . LEU A 1 30 ? 12.984 4.651 13.640 1.00 28.68 ? 30 LEU A CB 1 ATOM 64 C CG . LEU A 1 30 ? 14.330 5.259 13.236 1.00 31.23 ? 30 LEU A CG 1 ATOM 65 C CD1 . LEU A 1 30 ? 14.560 6.582 13.943 1.00 32.37 ? 30 LEU A CD1 1 ATOM 66 C CD2 . LEU A 1 30 ? 15.458 4.279 13.529 1.00 31.83 ? 30 LEU A CD2 1 ATOM 67 N N . ALA A 1 31 ? 10.048 3.471 13.146 1.00 27.36 ? 31 ALA A N 1 ATOM 68 C CA . ALA A 1 31 ? 8.815 2.880 13.706 1.00 24.97 ? 31 ALA A CA 1 ATOM 69 C C . ALA A 1 31 ? 8.528 1.577 12.978 1.00 26.09 ? 31 ALA A C 1 ATOM 70 O O . ALA A 1 31 ? 8.137 0.566 13.578 1.00 31.27 ? 31 ALA A O 1 ATOM 71 C CB . ALA A 1 31 ? 7.664 3.854 13.579 1.00 26.56 ? 31 ALA A CB 1 ATOM 72 N N . GLU A 1 32 ? 8.771 1.561 11.664 1.00 23.55 ? 32 GLU A N 1 ATOM 73 C CA . GLU A 1 32 ? 8.548 0.318 10.910 1.00 24.72 ? 32 GLU A CA 1 ATOM 74 C C . GLU A 1 32 ? 9.553 -0.740 11.361 1.00 22.45 ? 32 GLU A C 1 ATOM 75 O O . GLU A 1 32 ? 9.225 -1.920 11.458 1.00 24.43 ? 32 GLU A O 1 ATOM 76 C CB . GLU A 1 32 ? 8.625 0.552 9.407 1.00 28.93 ? 32 GLU A CB 1 ATOM 77 C CG . GLU A 1 32 ? 7.421 1.289 8.835 1.00 33.92 ? 32 GLU A CG 1 ATOM 78 C CD . GLU A 1 32 ? 6.109 0.810 9.430 1.00 40.14 ? 32 GLU A CD 1 ATOM 79 O OE1 . GLU A 1 32 ? 5.836 -0.413 9.355 1.00 43.05 ? 32 GLU A OE1 1 ATOM 80 O OE2 . GLU A 1 32 ? 5.349 1.645 9.973 1.00 38.72 ? 32 GLU A OE2 1 ATOM 81 N N . PHE A 1 33 ? 10.782 -0.312 11.643 1.00 22.92 ? 33 PHE A N 1 ATOM 82 C CA . PHE A 1 33 ? 11.831 -1.233 12.071 1.00 25.16 ? 33 PHE A CA 1 ATOM 83 C C . PHE A 1 33 ? 11.491 -1.797 13.449 1.00 18.71 ? 33 PHE A C 1 ATOM 84 O O . PHE A 1 33 ? 11.599 -2.994 13.689 1.00 19.85 ? 33 PHE A O 1 ATOM 85 C CB . PHE A 1 33 ? 13.195 -0.545 12.075 1.00 22.08 ? 33 PHE A CB 1 ATOM 86 C CG . PHE A 1 33 ? 14.299 -1.368 12.666 1.00 23.93 ? 33 PHE A CG 1 ATOM 87 C CD1 . PHE A 1 33 ? 14.729 -2.532 12.037 1.00 24.40 ? 33 PHE A CD1 1 ATOM 88 C CD2 . PHE A 1 33 ? 14.916 -0.987 13.841 1.00 25.22 ? 33 PHE A CD2 1 ATOM 89 C CE1 . PHE A 1 33 ? 15.743 -3.291 12.581 1.00 23.14 ? 33 PHE A CE1 1 ATOM 90 C CE2 . PHE A 1 33 ? 15.933 -1.747 14.389 1.00 23.25 ? 33 PHE A CE2 1 ATOM 91 C CZ . PHE A 1 33 ? 16.344 -2.900 13.760 1.00 22.65 ? 33 PHE A CZ 1 ATOM 92 N N . ALA A 1 34 ? 11.054 -0.916 14.342 1.00 20.87 ? 34 ALA A N 1 ATOM 93 C CA . ALA A 1 34 ? 10.658 -1.337 15.683 1.00 24.66 ? 34 ALA A CA 1 ATOM 94 C C . ALA A 1 34 ? 9.613 -2.445 15.588 1.00 18.95 ? 34 ALA A C 1 ATOM 95 O O . ALA A 1 34 ? 9.690 -3.423 16.324 1.00 22.61 ? 34 ALA A O 1 ATOM 96 C CB . ALA A 1 34 ? 10.071 -0.137 16.444 1.00 17.66 ? 34 ALA A CB 1 ATOM 97 N N . PHE A 1 35 ? 8.626 -2.270 14.707 1.00 22.70 ? 35 PHE A N 1 ATOM 98 C CA . PHE A 1 35 ? 7.560 -3.262 14.573 1.00 28.59 ? 35 PHE A CA 1 ATOM 99 C C . PHE A 1 35 ? 8.037 -4.563 13.963 1.00 29.34 ? 35 PHE A C 1 ATOM 100 O O . PHE A 1 35 ? 7.769 -5.633 14.524 1.00 29.01 ? 35 PHE A O 1 ATOM 101 C CB . PHE A 1 35 ? 6.370 -2.704 13.783 1.00 32.22 ? 35 PHE A CB 1 ATOM 102 C CG . PHE A 1 35 ? 5.705 -1.525 14.431 1.00 37.77 ? 35 PHE A CG 1 ATOM 103 C CD1 . PHE A 1 35 ? 5.432 -1.530 15.791 1.00 40.43 ? 35 PHE A CD1 1 ATOM 104 C CD2 . PHE A 1 35 ? 5.349 -0.412 13.691 1.00 37.17 ? 35 PHE A CD2 1 ATOM 105 C CE1 . PHE A 1 35 ? 4.822 -0.443 16.391 1.00 42.87 ? 35 PHE A CE1 1 ATOM 106 C CE2 . PHE A 1 35 ? 4.741 0.673 14.279 1.00 39.56 ? 35 PHE A CE2 1 ATOM 107 C CZ . PHE A 1 35 ? 4.474 0.660 15.634 1.00 40.56 ? 35 PHE A CZ 1 ATOM 108 N N . SER A 1 36 ? 8.745 -4.509 12.830 1.00 25.45 ? 36 SER A N 1 ATOM 109 C CA . SER A 1 36 ? 9.210 -5.776 12.231 1.00 29.34 ? 36 SER A CA 1 ATOM 110 C C . SER A 1 36 ? 10.054 -6.541 13.238 1.00 27.09 ? 36 SER A C 1 ATOM 111 O O . SER A 1 36 ? 9.913 -7.755 13.392 1.00 26.43 ? 36 SER A O 1 ATOM 112 C CB . SER A 1 36 ? 9.891 -5.570 10.901 1.00 31.92 ? 36 SER A CB 1 ATOM 113 O OG . SER A 1 36 ? 11.049 -4.787 10.953 1.00 35.43 ? 36 SER A OG 1 ATOM 114 N N . LEU A 1 37 ? 10.864 -5.822 14.008 1.00 28.22 ? 37 LEU A N 1 ATOM 115 C CA . LEU A 1 37 ? 11.710 -6.439 15.032 1.00 28.29 ? 37 LEU A CA 1 ATOM 116 C C . LEU A 1 37 ? 10.851 -7.020 16.147 1.00 29.53 ? 37 LEU A C 1 ATOM 117 O O . LEU A 1 37 ? 11.024 -8.164 16.565 1.00 23.11 ? 37 LEU A O 1 ATOM 118 C CB . LEU A 1 37 ? 12.700 -5.412 15.556 1.00 31.84 ? 37 LEU A CB 1 ATOM 119 C CG . LEU A 1 37 ? 13.887 -5.878 16.383 1.00 34.33 ? 37 LEU A CG 1 ATOM 120 C CD1 . LEU A 1 37 ? 14.554 -7.099 15.766 1.00 36.00 ? 37 LEU A CD1 1 ATOM 121 C CD2 . LEU A 1 37 ? 14.906 -4.748 16.527 1.00 37.00 ? 37 LEU A CD2 1 ATOM 122 N N . TYR A 1 38 ? 9.884 -6.228 16.623 1.00 28.39 ? 38 TYR A N 1 ATOM 123 C CA . TYR A 1 38 ? 8.991 -6.678 17.673 1.00 25.36 ? 38 TYR A CA 1 ATOM 124 C C . TYR A 1 38 ? 8.226 -7.930 17.263 1.00 25.38 ? 38 TYR A C 1 ATOM 125 O O . TYR A 1 38 ? 8.208 -8.924 17.997 1.00 26.56 ? 38 TYR A O 1 ATOM 126 C CB . TYR A 1 38 ? 7.990 -5.580 18.081 1.00 27.24 ? 38 TYR A CB 1 ATOM 127 C CG . TYR A 1 38 ? 7.061 -6.074 19.182 1.00 25.36 ? 38 TYR A CG 1 ATOM 128 C CD1 . TYR A 1 38 ? 7.398 -5.910 20.517 1.00 25.74 ? 38 TYR A CD1 1 ATOM 129 C CD2 . TYR A 1 38 ? 5.871 -6.709 18.873 1.00 27.15 ? 38 TYR A CD2 1 ATOM 130 C CE1 . TYR A 1 38 ? 6.556 -6.365 21.522 1.00 27.61 ? 38 TYR A CE1 1 ATOM 131 C CE2 . TYR A 1 38 ? 5.026 -7.168 19.870 1.00 26.30 ? 38 TYR A CE2 1 ATOM 132 C CZ . TYR A 1 38 ? 5.378 -6.991 21.189 1.00 25.89 ? 38 TYR A CZ 1 ATOM 133 O OH . TYR A 1 38 ? 4.541 -7.451 22.185 1.00 31.95 ? 38 TYR A OH 1 ATOM 134 N N . ARG A 1 39 ? 7.593 -7.883 16.091 1.00 27.29 ? 39 ARG A N 1 ATOM 135 C CA . ARG A 1 39 ? 6.797 -9.028 15.636 1.00 33.13 ? 39 ARG A CA 1 ATOM 136 C C . ARG A 1 39 ? 7.656 -10.255 15.410 1.00 36.05 ? 39 ARG A C 1 ATOM 137 O O . ARG A 1 39 ? 7.192 -11.392 15.520 1.00 31.37 ? 39 ARG A O 1 ATOM 138 C CB . ARG A 1 39 ? 5.976 -8.647 14.403 1.00 32.82 ? 39 ARG A CB 1 ATOM 139 C CG . ARG A 1 39 ? 4.764 -7.802 14.789 1.00 32.72 ? 39 ARG A CG 1 ATOM 140 C CD . ARG A 1 39 ? 4.253 -6.954 13.638 1.00 33.26 ? 39 ARG A CD 1 ATOM 141 N NE . ARG A 1 39 ? 3.102 -6.154 14.061 1.00 31.48 ? 39 ARG A NE 1 ATOM 142 C CZ . ARG A 1 39 ? 2.745 -5.000 13.526 1.00 32.65 ? 39 ARG A CZ 1 ATOM 143 N NH1 . ARG A 1 39 ? 3.449 -4.484 12.523 1.00 31.94 ? 39 ARG A NH1 1 ATOM 144 N NH2 . ARG A 1 39 ? 1.681 -4.357 13.989 1.00 31.27 ? 39 ARG A NH2 1 ATOM 145 N N . GLN A 1 40 ? 8.931 -10.018 15.110 1.00 36.34 ? 40 GLN A N 1 ATOM 146 C CA . GLN A 1 40 ? 9.875 -11.114 14.903 1.00 42.33 ? 40 GLN A CA 1 ATOM 147 C C . GLN A 1 40 ? 10.077 -11.830 16.242 1.00 42.10 ? 40 GLN A C 1 ATOM 148 O O . GLN A 1 40 ? 9.886 -13.033 16.364 1.00 42.38 ? 40 GLN A O 1 ATOM 149 C CB . GLN A 1 40 ? 11.205 -10.561 14.395 1.00 44.54 ? 40 GLN A CB 1 ATOM 150 C CG . GLN A 1 40 ? 12.352 -11.554 14.410 1.00 48.01 ? 40 GLN A CG 1 ATOM 151 C CD . GLN A 1 40 ? 12.186 -12.630 13.357 1.00 49.57 ? 40 GLN A CD 1 ATOM 152 O OE1 . GLN A 1 40 ? 12.208 -12.348 12.157 1.00 50.91 ? 40 GLN A OE1 1 ATOM 153 N NE2 . GLN A 1 40 ? 12.019 -13.866 13.802 1.00 51.21 ? 40 GLN A NE2 1 ATOM 154 N N . LEU A 1 41 ? 10.418 -11.035 17.255 1.00 37.92 ? 41 LEU A N 1 ATOM 155 C CA . LEU A 1 41 ? 10.658 -11.556 18.589 1.00 35.63 ? 41 LEU A CA 1 ATOM 156 C C . LEU A 1 41 ? 9.408 -12.156 19.209 1.00 37.17 ? 41 LEU A C 1 ATOM 157 O O . LEU A 1 41 ? 9.485 -13.192 19.871 1.00 42.12 ? 41 LEU A O 1 ATOM 158 C CB . LEU A 1 41 ? 11.236 -10.463 19.492 1.00 35.25 ? 41 LEU A CB 1 ATOM 159 C CG . LEU A 1 41 ? 12.613 -9.934 19.079 1.00 34.97 ? 41 LEU A CG 1 ATOM 160 C CD1 . LEU A 1 41 ? 13.039 -8.785 19.972 1.00 34.96 ? 41 LEU A CD1 1 ATOM 161 C CD2 . LEU A 1 41 ? 13.641 -11.063 19.113 1.00 35.35 ? 41 LEU A CD2 1 ATOM 162 N N . ALA A 1 42 ? 8.263 -11.518 18.999 1.00 38.85 ? 42 ALA A N 1 ATOM 163 C CA . ALA A 1 42 ? 7.007 -12.011 19.554 1.00 38.75 ? 42 ALA A CA 1 ATOM 164 C C . ALA A 1 42 ? 6.640 -13.360 18.937 1.00 42.41 ? 42 ALA A C 1 ATOM 165 O O . ALA A 1 42 ? 5.994 -14.190 19.574 1.00 43.39 ? 42 ALA A O 1 ATOM 166 C CB . ALA A 1 42 ? 5.889 -11.009 19.319 1.00 36.25 ? 42 ALA A CB 1 ATOM 167 N N . HIS A 1 43 ? 7.065 -13.560 17.698 1.00 50.09 ? 43 HIS A N 1 ATOM 168 C CA . HIS A 1 43 ? 6.783 -14.792 16.973 1.00 56.37 ? 43 HIS A CA 1 ATOM 169 C C . HIS A 1 43 ? 7.620 -15.955 17.484 1.00 54.55 ? 43 HIS A C 1 ATOM 170 O O . HIS A 1 43 ? 7.103 -17.056 17.672 1.00 53.63 ? 43 HIS A O 1 ATOM 171 C CB . HIS A 1 43 ? 7.017 -14.576 15.474 1.00 58.24 ? 43 HIS A CB 1 ATOM 172 C CG . HIS A 1 43 ? 5.901 -15.082 14.613 1.00 60.66 ? 43 HIS A CG 1 ATOM 173 N ND1 . HIS A 1 43 ? 5.954 -15.066 13.238 1.00 62.26 ? 43 HIS A ND1 1 ATOM 174 C CD2 . HIS A 1 43 ? 4.701 -15.622 14.937 1.00 61.92 ? 43 HIS A CD2 1 ATOM 175 C CE1 . HIS A 1 43 ? 4.834 -15.570 12.747 1.00 62.69 ? 43 HIS A CE1 1 ATOM 176 N NE2 . HIS A 1 43 ? 4.057 -15.917 13.759 1.00 62.78 ? 43 HIS A NE2 1 ATOM 177 N N . GLN A 1 44 ? 8.907 -15.721 17.715 1.00 59.16 ? 44 GLN A N 1 ATOM 178 C CA . GLN A 1 44 ? 9.791 -16.774 18.211 1.00 59.61 ? 44 GLN A CA 1 ATOM 179 C C . GLN A 1 44 ? 9.147 -17.496 19.394 1.00 63.26 ? 44 GLN A C 1 ATOM 180 O O . GLN A 1 44 ? 9.079 -18.724 19.427 1.00 59.70 ? 44 GLN A O 1 ATOM 181 C CB . GLN A 1 44 ? 11.143 -16.202 18.616 1.00 60.45 ? 44 GLN A CB 1 ATOM 182 C CG . GLN A 1 44 ? 11.883 -15.465 17.511 1.00 60.60 ? 44 GLN A CG 1 ATOM 183 C CD . GLN A 1 44 ? 13.260 -15.010 17.962 1.00 61.04 ? 44 GLN A CD 1 ATOM 184 O OE1 . GLN A 1 44 ? 13.966 -14.296 17.251 1.00 60.26 ? 44 GLN A OE1 1 ATOM 185 N NE2 . GLN A 1 44 ? 13.644 -15.432 19.162 1.00 60.66 ? 44 GLN A NE2 1 ATOM 186 N N . SER A 1 45 ? 8.672 -16.715 20.358 1.00 69.16 ? 45 SER A N 1 ATOM 187 C CA . SER A 1 45 ? 8.023 -17.244 21.548 1.00 70.80 ? 45 SER A CA 1 ATOM 188 C C . SER A 1 45 ? 7.147 -16.175 22.204 1.00 70.47 ? 45 SER A C 1 ATOM 189 O O . SER A 1 45 ? 7.486 -14.991 22.161 1.00 70.43 ? 45 SER A O 1 ATOM 190 C CB . SER A 1 45 ? 9.064 -17.711 22.572 1.00 71.33 ? 45 SER A CB 1 ATOM 191 O OG . SER A 1 45 ? 9.459 -16.621 23.395 1.00 72.00 ? 45 SER A OG 1 ATOM 192 N N . ASN A 1 46 ? 6.045 -16.597 22.811 1.00 67.36 ? 46 ASN A N 1 ATOM 193 C CA . ASN A 1 46 ? 5.142 -15.668 23.474 1.00 66.65 ? 46 ASN A CA 1 ATOM 194 C C . ASN A 1 46 ? 5.127 -15.839 24.985 1.00 64.39 ? 46 ASN A C 1 ATOM 195 O O . ASN A 1 46 ? 4.210 -15.334 25.647 1.00 60.43 ? 46 ASN A O 1 ATOM 196 C CB . ASN A 1 46 ? 3.719 -15.807 22.923 1.00 67.44 ? 46 ASN A CB 1 ATOM 197 C CG . ASN A 1 46 ? 3.261 -14.579 22.165 1.00 69.21 ? 46 ASN A CG 1 ATOM 198 O OD1 . ASN A 1 46 ? 2.069 -14.415 21.894 1.00 69.24 ? 46 ASN A OD1 1 ATOM 199 N ND2 . ASN A 1 46 ? 4.202 -13.705 21.823 1.00 69.32 ? 46 ASN A ND2 1 ATOM 200 N N . SER A 1 47 ? 6.121 -16.529 25.545 1.00 59.42 ? 47 SER A N 1 ATOM 201 C CA . SER A 1 47 ? 6.152 -16.729 26.992 1.00 58.14 ? 47 SER A CA 1 ATOM 202 C C . SER A 1 47 ? 7.343 -16.060 27.653 1.00 52.68 ? 47 SER A C 1 ATOM 203 O O . SER A 1 47 ? 7.676 -16.367 28.802 1.00 52.08 ? 47 SER A O 1 ATOM 204 C CB . SER A 1 47 ? 6.090 -18.214 27.346 1.00 57.63 ? 47 SER A CB 1 ATOM 205 O OG . SER A 1 47 ? 7.221 -18.911 26.858 1.00 61.08 ? 47 SER A OG 1 ATOM 206 N N . THR A 1 48 ? 7.980 -15.124 26.960 1.00 48.27 ? 48 THR A N 1 ATOM 207 C CA . THR A 1 48 ? 9.123 -14.406 27.515 1.00 46.27 ? 48 THR A CA 1 ATOM 208 C C . THR A 1 48 ? 8.904 -12.896 27.444 1.00 43.38 ? 48 THR A C 1 ATOM 209 O O . THR A 1 48 ? 8.244 -12.413 26.525 1.00 45.00 ? 48 THR A O 1 ATOM 210 C CB . THR A 1 48 ? 10.426 -14.745 26.769 1.00 47.16 ? 48 THR A CB 1 ATOM 211 O OG1 . THR A 1 48 ? 10.715 -16.142 26.902 1.00 49.24 ? 48 THR A OG1 1 ATOM 212 C CG2 . THR A 1 48 ? 11.588 -13.938 27.326 1.00 47.60 ? 48 THR A CG2 1 ATOM 213 N N . ASN A 1 49 ? 9.451 -12.169 28.412 1.00 37.77 ? 49 ASN A N 1 ATOM 214 C CA . ASN A 1 49 ? 9.344 -10.712 28.409 1.00 36.68 ? 49 ASN A CA 1 ATOM 215 C C . ASN A 1 49 ? 10.218 -10.153 27.275 1.00 38.99 ? 49 ASN A C 1 ATOM 216 O O . ASN A 1 49 ? 11.336 -10.625 27.071 1.00 42.81 ? 49 ASN A O 1 ATOM 217 C CB . ASN A 1 49 ? 9.809 -10.107 29.720 1.00 36.15 ? 49 ASN A CB 1 ATOM 218 C CG . ASN A 1 49 ? 8.897 -10.303 30.897 1.00 35.31 ? 49 ASN A CG 1 ATOM 219 O OD1 . ASN A 1 49 ? 7.674 -10.409 30.781 1.00 34.77 ? 49 ASN A OD1 1 ATOM 220 N ND2 . ASN A 1 49 ? 9.493 -10.350 32.089 1.00 36.70 ? 49 ASN A ND2 1 ATOM 221 N N . ILE A 1 50 ? 9.700 -9.159 26.567 1.00 34.49 ? 50 ILE A N 1 ATOM 222 C CA . ILE A 1 50 ? 10.465 -8.560 25.475 1.00 33.54 ? 50 ILE A CA 1 ATOM 223 C C . ILE A 1 50 ? 10.781 -7.105 25.783 1.00 33.96 ? 50 ILE A C 1 ATOM 224 O O . ILE A 1 50 ? 9.923 -6.341 26.228 1.00 31.94 ? 50 ILE A O 1 ATOM 225 C CB . ILE A 1 50 ? 9.728 -8.672 24.133 1.00 33.95 ? 50 ILE A CB 1 ATOM 226 C CG1 . ILE A 1 50 ? 9.585 -10.140 23.726 1.00 34.39 ? 50 ILE A CG1 1 ATOM 227 C CG2 . ILE A 1 50 ? 10.450 -7.879 23.055 1.00 34.83 ? 50 ILE A CG2 1 ATOM 228 C CD1 . ILE A 1 50 ? 8.680 -10.372 22.535 1.00 32.63 ? 50 ILE A CD1 1 ATOM 229 N N . PHE A 1 51 ? 12.037 -6.729 25.565 1.00 28.39 ? 51 PHE A N 1 ATOM 230 C CA . PHE A 1 51 ? 12.480 -5.368 25.788 1.00 27.08 ? 51 PHE A CA 1 ATOM 231 C C . PHE A 1 51 ? 13.737 -5.085 24.971 1.00 26.28 ? 51 PHE A C 1 ATOM 232 O O . PHE A 1 51 ? 14.770 -5.727 25.167 1.00 29.02 ? 51 PHE A O 1 ATOM 233 C CB . PHE A 1 51 ? 12.716 -5.052 27.264 1.00 26.74 ? 51 PHE A CB 1 ATOM 234 C CG . PHE A 1 51 ? 13.041 -3.593 27.484 1.00 25.09 ? 51 PHE A CG 1 ATOM 235 C CD1 . PHE A 1 51 ? 12.070 -2.620 27.302 1.00 24.43 ? 51 PHE A CD1 1 ATOM 236 C CD2 . PHE A 1 51 ? 14.311 -3.212 27.867 1.00 22.62 ? 51 PHE A CD2 1 ATOM 237 C CE1 . PHE A 1 51 ? 12.379 -1.280 27.504 1.00 24.44 ? 51 PHE A CE1 1 ATOM 238 C CE2 . PHE A 1 51 ? 14.621 -1.884 28.065 1.00 23.09 ? 51 PHE A CE2 1 ATOM 239 C CZ . PHE A 1 51 ? 13.655 -0.909 27.885 1.00 23.31 ? 51 PHE A CZ 1 ATOM 240 N N . PHE A 1 52 ? 13.628 -4.129 24.058 1.00 24.72 ? 52 PHE A N 1 ATOM 241 C CA . PHE A 1 52 ? 14.746 -3.756 23.207 1.00 23.08 ? 52 PHE A CA 1 ATOM 242 C C . PHE A 1 52 ? 14.626 -2.309 22.750 1.00 27.08 ? 52 PHE A C 1 ATOM 243 O O . PHE A 1 52 ? 13.560 -1.703 22.842 1.00 31.84 ? 52 PHE A O 1 ATOM 244 C CB . PHE A 1 52 ? 14.809 -4.676 21.973 1.00 22.87 ? 52 PHE A CB 1 ATOM 245 C CG . PHE A 1 52 ? 13.658 -4.479 21.027 1.00 23.53 ? 52 PHE A CG 1 ATOM 246 C CD1 . PHE A 1 52 ? 12.451 -5.122 21.245 1.00 24.30 ? 52 PHE A CD1 1 ATOM 247 C CD2 . PHE A 1 52 ? 13.778 -3.646 19.925 1.00 23.51 ? 52 PHE A CD2 1 ATOM 248 C CE1 . PHE A 1 52 ? 11.388 -4.947 20.384 1.00 24.44 ? 52 PHE A CE1 1 ATOM 249 C CE2 . PHE A 1 52 ? 12.720 -3.463 19.057 1.00 24.07 ? 52 PHE A CE2 1 ATOM 250 C CZ . PHE A 1 52 ? 11.522 -4.113 19.287 1.00 26.39 ? 52 PHE A CZ 1 ATOM 251 N N . SER A 1 53 ? 15.723 -1.769 22.232 1.00 18.60 ? 53 SER A N 1 ATOM 252 C CA . SER A 1 53 ? 15.764 -0.421 21.728 1.00 25.27 ? 53 SER A CA 1 ATOM 253 C C . SER A 1 53 ? 15.895 -0.368 20.214 1.00 29.68 ? 53 SER A C 1 ATOM 254 O O . SER A 1 53 ? 16.977 -0.594 19.671 1.00 25.59 ? 53 SER A O 1 ATOM 255 C CB . SER A 1 53 ? 16.925 0.370 22.357 1.00 20.93 ? 53 SER A CB 1 ATOM 256 O OG . SER A 1 53 ? 16.907 1.701 21.851 1.00 27.25 ? 53 SER A OG 1 ATOM 257 N N . PRO A 1 54 ? 14.795 -0.067 19.536 1.00 26.23 ? 54 PRO A N 1 ATOM 258 C CA . PRO A 1 54 ? 14.793 0.063 18.093 1.00 26.24 ? 54 PRO A CA 1 ATOM 259 C C . PRO A 1 54 ? 15.811 1.121 17.679 1.00 30.37 ? 54 PRO A C 1 ATOM 260 O O . PRO A 1 54 ? 16.574 0.944 16.735 1.00 23.44 ? 54 PRO A O 1 ATOM 261 C CB . PRO A 1 54 ? 13.367 0.515 17.778 1.00 30.30 ? 54 PRO A CB 1 ATOM 262 C CG . PRO A 1 54 ? 12.560 -0.047 18.916 1.00 29.83 ? 54 PRO A CG 1 ATOM 263 C CD . PRO A 1 54 ? 13.453 0.179 20.127 1.00 20.07 ? 54 PRO A CD 1 ATOM 264 N N . VAL A 1 55 ? 15.839 2.225 18.427 1.00 24.34 ? 55 VAL A N 1 ATOM 265 C CA . VAL A 1 55 ? 16.751 3.319 18.160 1.00 26.25 ? 55 VAL A CA 1 ATOM 266 C C . VAL A 1 55 ? 18.221 2.996 18.353 1.00 30.69 ? 55 VAL A C 1 ATOM 267 O O . VAL A 1 55 ? 19.035 3.412 17.508 1.00 22.80 ? 55 VAL A O 1 ATOM 268 C CB . VAL A 1 55 ? 16.370 4.561 18.995 1.00 27.27 ? 55 VAL A CB 1 ATOM 269 C CG1 . VAL A 1 55 ? 17.464 5.607 18.982 1.00 26.36 ? 55 VAL A CG1 1 ATOM 270 C CG2 . VAL A 1 55 ? 15.065 5.157 18.459 1.00 27.98 ? 55 VAL A CG2 1 ATOM 271 N N . SER A 1 56 ? 18.601 2.301 19.424 1.00 23.23 ? 56 SER A N 1 ATOM 272 C CA . SER A 1 56 ? 20.013 2.002 19.659 1.00 31.21 ? 56 SER A CA 1 ATOM 273 C C . SER A 1 56 ? 20.557 1.026 18.616 1.00 28.43 ? 56 SER A C 1 ATOM 274 O O . SER A 1 56 ? 21.681 1.170 18.145 1.00 28.96 ? 56 SER A O 1 ATOM 275 C CB . SER A 1 56 ? 20.268 1.495 21.071 1.00 26.16 ? 56 SER A CB 1 ATOM 276 O OG . SER A 1 56 ? 19.877 0.144 21.227 1.00 29.39 ? 56 SER A OG 1 ATOM 277 N N . ILE A 1 57 ? 19.750 0.049 18.253 1.00 25.30 ? 57 ILE A N 1 ATOM 278 C CA . ILE A 1 57 ? 20.116 -0.959 17.277 1.00 20.80 ? 57 ILE A CA 1 ATOM 279 C C . ILE A 1 57 ? 20.250 -0.382 15.877 1.00 26.40 ? 57 ILE A C 1 ATOM 280 O O . ILE A 1 57 ? 21.233 -0.645 15.171 1.00 30.55 ? 57 ILE A O 1 ATOM 281 C CB . ILE A 1 57 ? 19.116 -2.123 17.274 1.00 21.48 ? 57 ILE A CB 1 ATOM 282 C CG1 . ILE A 1 57 ? 19.167 -2.874 18.606 1.00 22.39 ? 57 ILE A CG1 1 ATOM 283 C CG2 . ILE A 1 57 ? 19.435 -3.056 16.112 1.00 20.49 ? 57 ILE A CG2 1 ATOM 284 C CD1 . ILE A 1 57 ? 18.015 -3.837 18.817 1.00 23.55 ? 57 ILE A CD1 1 ATOM 285 N N . ALA A 1 58 ? 19.280 0.406 15.451 1.00 25.83 ? 58 ALA A N 1 ATOM 286 C CA . ALA A 1 58 ? 19.274 1.021 14.136 1.00 24.89 ? 58 ALA A CA 1 ATOM 287 C C . ALA A 1 58 ? 20.436 2.003 13.975 1.00 29.39 ? 58 ALA A C 1 ATOM 288 O O . ALA A 1 58 ? 21.051 2.076 12.912 1.00 28.61 ? 58 ALA A O 1 ATOM 289 C CB . ALA A 1 58 ? 17.963 1.752 13.883 1.00 22.35 ? 58 ALA A CB 1 ATOM 290 N N . THR A 1 59 ? 20.715 2.752 15.025 1.00 26.65 ? 59 THR A N 1 ATOM 291 C CA . THR A 1 59 ? 21.788 3.737 15.023 1.00 28.13 ? 59 THR A CA 1 ATOM 292 C C . THR A 1 59 ? 23.142 3.055 14.881 1.00 29.00 ? 59 THR A C 1 ATOM 293 O O . THR A 1 59 ? 24.016 3.515 14.146 1.00 24.75 ? 59 THR A O 1 ATOM 294 C CB . THR A 1 59 ? 21.751 4.583 16.309 1.00 30.29 ? 59 THR A CB 1 ATOM 295 O OG1 . THR A 1 59 ? 20.595 5.437 16.265 1.00 31.37 ? 59 THR A OG1 1 ATOM 296 C CG2 . THR A 1 59 ? 22.992 5.449 16.437 1.00 30.14 ? 59 THR A CG2 1 ATOM 297 N N . ALA A 1 60 ? 23.318 1.957 15.588 1.00 24.83 ? 60 ALA A N 1 ATOM 298 C CA . ALA A 1 60 ? 24.548 1.181 15.556 1.00 26.36 ? 60 ALA A CA 1 ATOM 299 C C . ALA A 1 60 ? 24.823 0.652 14.146 1.00 32.61 ? 60 ALA A C 1 ATOM 300 O O . ALA A 1 60 ? 25.942 0.719 13.646 1.00 27.09 ? 60 ALA A O 1 ATOM 301 C CB . ALA A 1 60 ? 24.413 -0.031 16.491 1.00 25.51 ? 60 ALA A CB 1 ATOM 302 N N . PHE A 1 61 ? 23.772 0.095 13.539 1.00 29.16 ? 61 PHE A N 1 ATOM 303 C CA . PHE A 1 61 ? 23.906 -0.488 12.214 1.00 29.10 ? 61 PHE A CA 1 ATOM 304 C C . PHE A 1 61 ? 24.030 0.532 11.115 1.00 30.67 ? 61 PHE A C 1 ATOM 305 O O . PHE A 1 61 ? 24.758 0.283 10.138 1.00 31.68 ? 61 PHE A O 1 ATOM 306 C CB . PHE A 1 61 ? 22.838 -1.563 11.991 1.00 25.90 ? 61 PHE A CB 1 ATOM 307 C CG . PHE A 1 61 ? 23.351 -2.881 12.536 1.00 29.52 ? 61 PHE A CG 1 ATOM 308 C CD1 . PHE A 1 61 ? 23.476 -3.058 13.904 1.00 29.64 ? 61 PHE A CD1 1 ATOM 309 C CD2 . PHE A 1 61 ? 23.736 -3.895 11.684 1.00 30.56 ? 61 PHE A CD2 1 ATOM 310 C CE1 . PHE A 1 61 ? 23.954 -4.256 14.411 1.00 29.96 ? 61 PHE A CE1 1 ATOM 311 C CE2 . PHE A 1 61 ? 24.216 -5.092 12.185 1.00 31.25 ? 61 PHE A CE2 1 ATOM 312 C CZ . PHE A 1 61 ? 24.325 -5.269 13.551 1.00 31.81 ? 61 PHE A CZ 1 ATOM 313 N N . ALA A 1 62 ? 23.401 1.697 11.265 1.00 28.00 ? 62 ALA A N 1 ATOM 314 C CA . ALA A 1 62 ? 23.536 2.740 10.249 1.00 32.57 ? 62 ALA A CA 1 ATOM 315 C C . ALA A 1 62 ? 25.004 3.203 10.248 1.00 32.35 ? 62 ALA A C 1 ATOM 316 O O . ALA A 1 62 ? 25.614 3.422 9.210 1.00 31.03 ? 62 ALA A O 1 ATOM 317 C CB . ALA A 1 62 ? 22.609 3.898 10.520 1.00 32.03 ? 62 ALA A CB 1 ATOM 318 N N . MET A 1 63 ? 25.540 3.349 11.454 1.00 35.00 ? 63 MET A N 1 ATOM 319 C CA . MET A 1 63 ? 26.931 3.769 11.634 1.00 34.88 ? 63 MET A CA 1 ATOM 320 C C . MET A 1 63 ? 27.875 2.762 10.979 1.00 34.11 ? 63 MET A C 1 ATOM 321 O O . MET A 1 63 ? 28.833 3.123 10.292 1.00 26.79 ? 63 MET A O 1 ATOM 322 C CB . MET A 1 63 ? 27.226 3.905 13.118 1.00 36.30 ? 63 MET A CB 1 ATOM 323 C CG . MET A 1 63 ? 28.643 4.302 13.488 1.00 38.32 ? 63 MET A CG 1 ATOM 324 S SD . MET A 1 63 ? 29.166 3.476 15.015 1.00 40.36 ? 63 MET A SD 1 ATOM 325 C CE . MET A 1 63 ? 29.365 1.802 14.401 1.00 39.69 ? 63 MET A CE 1 ATOM 326 N N . LEU A 1 64 ? 27.597 1.489 11.189 1.00 30.98 ? 64 LEU A N 1 ATOM 327 C CA . LEU A 1 64 ? 28.385 0.401 10.634 1.00 31.74 ? 64 LEU A CA 1 ATOM 328 C C . LEU A 1 64 ? 28.371 0.394 9.111 1.00 38.26 ? 64 LEU A C 1 ATOM 329 O O . LEU A 1 64 ? 29.396 0.142 8.472 1.00 30.45 ? 64 LEU A O 1 ATOM 330 C CB . LEU A 1 64 ? 27.842 -0.925 11.167 1.00 30.89 ? 64 LEU A CB 1 ATOM 331 C CG . LEU A 1 64 ? 28.451 -2.206 10.620 1.00 34.69 ? 64 LEU A CG 1 ATOM 332 C CD1 . LEU A 1 64 ? 29.934 -2.287 10.963 1.00 33.78 ? 64 LEU A CD1 1 ATOM 333 C CD2 . LEU A 1 64 ? 27.709 -3.427 11.157 1.00 31.31 ? 64 LEU A CD2 1 ATOM 334 N N . SER A 1 65 ? 27.212 0.657 8.517 1.00 29.67 ? 65 SER A N 1 ATOM 335 C CA . SER A 1 65 ? 27.075 0.650 7.072 1.00 31.26 ? 65 SER A CA 1 ATOM 336 C C . SER A 1 65 ? 28.102 1.567 6.410 1.00 29.94 ? 65 SER A C 1 ATOM 337 O O . SER A 1 65 ? 28.493 1.326 5.269 1.00 29.44 ? 65 SER A O 1 ATOM 338 C CB . SER A 1 65 ? 25.660 0.999 6.626 1.00 26.68 ? 65 SER A CB 1 ATOM 339 O OG . SER A 1 65 ? 25.335 2.354 6.862 1.00 26.89 ? 65 SER A OG 1 ATOM 340 N N . LEU A 1 66 ? 28.528 2.583 7.132 1.00 27.91 ? 66 LEU A N 1 ATOM 341 C CA . LEU A 1 66 ? 29.487 3.558 6.676 1.00 34.34 ? 66 LEU A CA 1 ATOM 342 C C . LEU A 1 66 ? 30.806 2.921 6.242 1.00 32.75 ? 66 LEU A C 1 ATOM 343 O O . LEU A 1 66 ? 31.532 3.492 5.434 1.00 35.20 ? 66 LEU A O 1 ATOM 344 C CB . LEU A 1 66 ? 29.761 4.593 7.775 1.00 33.06 ? 66 LEU A CB 1 ATOM 345 C CG . LEU A 1 66 ? 28.646 5.604 8.043 1.00 35.20 ? 66 LEU A CG 1 ATOM 346 C CD1 . LEU A 1 66 ? 29.081 6.612 9.098 1.00 36.09 ? 66 LEU A CD1 1 ATOM 347 C CD2 . LEU A 1 66 ? 28.233 6.304 6.756 1.00 34.71 ? 66 LEU A CD2 1 ATOM 348 N N . GLY A 1 67 ? 31.102 1.759 6.795 1.00 30.87 ? 67 GLY A N 1 ATOM 349 C CA . GLY A 1 67 ? 32.323 1.038 6.490 1.00 34.79 ? 67 GLY A CA 1 ATOM 350 C C . GLY A 1 67 ? 32.067 -0.120 5.537 1.00 33.61 ? 67 GLY A C 1 ATOM 351 O O . GLY A 1 67 ? 32.930 -0.984 5.359 1.00 31.10 ? 67 GLY A O 1 ATOM 352 N N . THR A 1 68 ? 30.870 -0.148 4.942 1.00 25.83 ? 68 THR A N 1 ATOM 353 C CA . THR A 1 68 ? 30.542 -1.251 4.036 1.00 26.79 ? 68 THR A CA 1 ATOM 354 C C . THR A 1 68 ? 30.193 -0.700 2.654 1.00 23.87 ? 68 THR A C 1 ATOM 355 O O . THR A 1 68 ? 29.953 0.491 2.525 1.00 29.85 ? 68 THR A O 1 ATOM 356 C CB . THR A 1 68 ? 29.337 -2.059 4.562 1.00 27.47 ? 68 THR A CB 1 ATOM 357 O OG1 . THR A 1 68 ? 28.168 -1.213 4.505 1.00 26.13 ? 68 THR A OG1 1 ATOM 358 C CG2 . THR A 1 68 ? 29.556 -2.508 5.990 1.00 25.77 ? 68 THR A CG2 1 ATOM 359 N N . LYS A 1 69 ? 30.049 -1.591 1.671 1.00 30.06 ? 69 LYS A N 1 ATOM 360 C CA . LYS A 1 69 ? 29.703 -1.143 0.324 1.00 36.12 ? 69 LYS A CA 1 ATOM 361 C C . LYS A 1 69 ? 28.827 -2.146 -0.402 1.00 25.70 ? 69 LYS A C 1 ATOM 362 O O . LYS A 1 69 ? 28.674 -3.286 0.025 1.00 28.22 ? 69 LYS A O 1 ATOM 363 C CB . LYS A 1 69 ? 31.013 -0.935 -0.476 1.00 40.57 ? 69 LYS A CB 1 ATOM 364 C CG . LYS A 1 69 ? 31.972 0.014 0.222 1.00 45.89 ? 69 LYS A CG 1 ATOM 365 C CD . LYS A 1 69 ? 33.168 0.340 -0.664 1.00 51.35 ? 69 LYS A CD 1 ATOM 366 C CE . LYS A 1 69 ? 34.231 1.089 0.135 1.00 53.07 ? 69 LYS A CE 1 ATOM 367 N NZ . LYS A 1 69 ? 35.550 1.057 -0.562 1.00 55.06 ? 69 LYS A NZ 1 ATOM 368 N N . ALA A 1 70 ? 28.242 -1.715 -1.511 1.00 32.04 ? 70 ALA A N 1 ATOM 369 C CA . ALA A 1 70 ? 27.404 -2.534 -2.353 1.00 35.30 ? 70 ALA A CA 1 ATOM 370 C C . ALA A 1 70 ? 26.294 -3.275 -1.617 1.00 41.01 ? 70 ALA A C 1 ATOM 371 O O . ALA A 1 70 ? 25.652 -2.759 -0.709 1.00 42.54 ? 70 ALA A O 1 ATOM 372 C CB . ALA A 1 70 ? 28.263 -3.545 -3.120 1.00 35.33 ? 70 ALA A CB 1 ATOM 373 N N . ASP A 1 71 ? 26.060 -4.513 -2.049 1.00 39.88 ? 71 ASP A N 1 ATOM 374 C CA . ASP A 1 71 ? 25.036 -5.366 -1.492 1.00 42.56 ? 71 ASP A CA 1 ATOM 375 C C . ASP A 1 71 ? 25.119 -5.459 0.028 1.00 43.54 ? 71 ASP A C 1 ATOM 376 O O . ASP A 1 71 ? 24.080 -5.425 0.689 1.00 32.88 ? 71 ASP A O 1 ATOM 377 C CB . ASP A 1 71 ? 25.086 -6.764 -2.112 1.00 45.28 ? 71 ASP A CB 1 ATOM 378 C CG . ASP A 1 71 ? 25.033 -6.738 -3.628 1.00 48.42 ? 71 ASP A CG 1 ATOM 379 O OD1 . ASP A 1 71 ? 24.345 -5.866 -4.200 1.00 48.82 ? 71 ASP A OD1 1 ATOM 380 O OD2 . ASP A 1 71 ? 25.684 -7.599 -4.258 1.00 49.65 ? 71 ASP A OD2 1 ATOM 381 N N . THR A 1 72 ? 26.327 -5.593 0.563 1.00 37.37 ? 72 THR A N 1 ATOM 382 C CA . THR A 1 72 ? 26.515 -5.688 2.012 1.00 34.45 ? 72 THR A CA 1 ATOM 383 C C . THR A 1 72 ? 25.906 -4.456 2.685 1.00 31.89 ? 72 THR A C 1 ATOM 384 O O . THR A 1 72 ? 25.189 -4.524 3.675 1.00 32.32 ? 72 THR A O 1 ATOM 385 C CB . THR A 1 72 ? 28.009 -5.772 2.376 1.00 34.73 ? 72 THR A CB 1 ATOM 386 O OG1 . THR A 1 72 ? 28.581 -6.974 1.843 1.00 31.70 ? 72 THR A OG1 1 ATOM 387 C CG2 . THR A 1 72 ? 28.195 -5.783 3.889 1.00 33.61 ? 72 THR A CG2 1 ATOM 388 N N . HIS A 1 73 ? 26.211 -3.308 2.106 1.00 31.29 ? 73 HIS A N 1 ATOM 389 C CA . HIS A 1 73 ? 25.729 -2.022 2.583 1.00 37.74 ? 73 HIS A CA 1 ATOM 390 C C . HIS A 1 73 ? 24.210 -1.924 2.454 1.00 41.94 ? 73 HIS A C 1 ATOM 391 O O . HIS A 1 73 ? 23.483 -1.677 3.422 1.00 28.76 ? 73 HIS A O 1 ATOM 392 C CB . HIS A 1 73 ? 26.393 -0.918 1.763 1.00 36.68 ? 73 HIS A CB 1 ATOM 393 C CG . HIS A 1 73 ? 25.825 0.447 1.944 1.00 35.63 ? 73 HIS A CG 1 ATOM 394 N ND1 . HIS A 1 73 ? 24.721 0.896 1.250 1.00 34.96 ? 73 HIS A ND1 1 ATOM 395 C CD2 . HIS A 1 73 ? 26.224 1.481 2.726 1.00 35.57 ? 73 HIS A CD2 1 ATOM 396 C CE1 . HIS A 1 73 ? 24.458 2.139 1.606 1.00 34.85 ? 73 HIS A CE1 1 ATOM 397 N NE2 . HIS A 1 73 ? 25.359 2.519 2.497 1.00 36.65 ? 73 HIS A NE2 1 ATOM 398 N N . ASP A 1 74 ? 23.743 -2.137 1.231 1.00 39.66 ? 74 ASP A N 1 ATOM 399 C CA . ASP A 1 74 ? 22.331 -2.083 0.911 1.00 43.49 ? 74 ASP A CA 1 ATOM 400 C C . ASP A 1 74 ? 21.482 -2.976 1.802 1.00 35.54 ? 74 ASP A C 1 ATOM 401 O O . ASP A 1 74 ? 20.401 -2.545 2.233 1.00 40.25 ? 74 ASP A O 1 ATOM 402 C CB . ASP A 1 74 ? 22.108 -2.454 -0.566 1.00 42.91 ? 74 ASP A CB 1 ATOM 403 C CG . ASP A 1 74 ? 22.603 -1.377 -1.507 1.00 42.87 ? 74 ASP A CG 1 ATOM 404 O OD1 . ASP A 1 74 ? 22.891 -0.251 -1.045 1.00 42.55 ? 74 ASP A OD1 1 ATOM 405 O OD2 . ASP A 1 74 ? 22.704 -1.654 -2.725 1.00 45.51 ? 74 ASP A OD2 1 ATOM 406 N N . GLU A 1 75 ? 21.930 -4.187 2.072 1.00 31.32 ? 75 GLU A N 1 ATOM 407 C CA . GLU A 1 75 ? 21.180 -5.108 2.920 1.00 35.51 ? 75 GLU A CA 1 ATOM 408 C C . GLU A 1 75 ? 20.900 -4.468 4.287 1.00 33.56 ? 75 GLU A C 1 ATOM 409 O O . GLU A 1 75 ? 19.790 -4.536 4.793 1.00 28.00 ? 75 GLU A O 1 ATOM 410 C CB . GLU A 1 75 ? 21.947 -6.399 3.139 1.00 35.66 ? 75 GLU A CB 1 ATOM 411 C CG . GLU A 1 75 ? 21.704 -7.515 2.147 1.00 37.12 ? 75 GLU A CG 1 ATOM 412 C CD . GLU A 1 75 ? 22.171 -8.850 2.715 1.00 37.56 ? 75 GLU A CD 1 ATOM 413 O OE1 . GLU A 1 75 ? 22.991 -8.820 3.660 1.00 37.58 ? 75 GLU A OE1 1 ATOM 414 O OE2 . GLU A 1 75 ? 21.723 -9.898 2.221 1.00 38.19 ? 75 GLU A OE2 1 ATOM 415 N N . ILE A 1 76 ? 21.938 -3.869 4.862 1.00 29.77 ? 76 ILE A N 1 ATOM 416 C CA . ILE A 1 76 ? 21.846 -3.228 6.160 1.00 29.73 ? 76 ILE A CA 1 ATOM 417 C C . ILE A 1 76 ? 20.814 -2.116 6.212 1.00 26.14 ? 76 ILE A C 1 ATOM 418 O O . ILE A 1 76 ? 19.993 -2.092 7.131 1.00 28.74 ? 76 ILE A O 1 ATOM 419 C CB . ILE A 1 76 ? 23.208 -2.665 6.618 1.00 27.46 ? 76 ILE A CB 1 ATOM 420 C CG1 . ILE A 1 76 ? 24.190 -3.817 6.888 1.00 27.03 ? 76 ILE A CG1 1 ATOM 421 C CG2 . ILE A 1 76 ? 23.042 -1.820 7.865 1.00 27.04 ? 76 ILE A CG2 1 ATOM 422 C CD1 . ILE A 1 76 ? 25.595 -3.343 7.209 1.00 25.86 ? 76 ILE A CD1 1 ATOM 423 N N . LEU A 1 77 ? 20.835 -1.190 5.260 1.00 24.29 ? 77 LEU A N 1 ATOM 424 C CA . LEU A 1 77 ? 19.865 -0.101 5.273 1.00 30.37 ? 77 LEU A CA 1 ATOM 425 C C . LEU A 1 77 ? 18.454 -0.599 4.998 1.00 29.69 ? 77 LEU A C 1 ATOM 426 O O . LEU A 1 77 ? 17.513 -0.097 5.636 1.00 31.42 ? 77 LEU A O 1 ATOM 427 C CB . LEU A 1 77 ? 20.260 1.053 4.376 1.00 29.81 ? 77 LEU A CB 1 ATOM 428 C CG . LEU A 1 77 ? 21.639 1.674 4.682 1.00 28.79 ? 77 LEU A CG 1 ATOM 429 C CD1 . LEU A 1 77 ? 21.855 2.916 3.843 1.00 27.42 ? 77 LEU A CD1 1 ATOM 430 C CD2 . LEU A 1 77 ? 21.765 1.970 6.160 1.00 29.45 ? 77 LEU A CD2 1 ATOM 431 N N . GLU A 1 78 ? 18.293 -1.577 4.127 1.00 29.64 ? 78 GLU A N 1 ATOM 432 C CA . GLU A 1 78 ? 16.972 -2.115 3.824 1.00 33.05 ? 78 GLU A CA 1 ATOM 433 C C . GLU A 1 78 ? 16.425 -2.922 5.001 1.00 31.83 ? 78 GLU A C 1 ATOM 434 O O . GLU A 1 78 ? 15.215 -2.947 5.211 1.00 28.53 ? 78 GLU A O 1 ATOM 435 C CB . GLU A 1 78 ? 16.967 -2.974 2.569 1.00 33.05 ? 78 GLU A CB 1 ATOM 436 C CG . GLU A 1 78 ? 17.366 -2.224 1.301 1.00 38.68 ? 78 GLU A CG 1 ATOM 437 C CD . GLU A 1 78 ? 17.465 -3.177 0.119 1.00 40.91 ? 78 GLU A CD 1 ATOM 438 O OE1 . GLU A 1 78 ? 17.889 -4.332 0.323 1.00 43.14 ? 78 GLU A OE1 1 ATOM 439 O OE2 . GLU A 1 78 ? 17.111 -2.766 -1.004 1.00 44.43 ? 78 GLU A OE2 1 ATOM 440 N N . GLY A 1 79 ? 17.318 -3.562 5.737 1.00 29.56 ? 79 GLY A N 1 ATOM 441 C CA . GLY A 1 79 ? 16.930 -4.356 6.901 1.00 28.10 ? 79 GLY A CA 1 ATOM 442 C C . GLY A 1 79 ? 16.525 -3.415 8.042 1.00 29.61 ? 79 GLY A C 1 ATOM 443 O O . GLY A 1 79 ? 15.941 -3.845 9.032 1.00 31.85 ? 79 GLY A O 1 ATOM 444 N N . LEU A 1 80 ? 16.861 -2.140 7.887 1.00 27.74 ? 80 LEU A N 1 ATOM 445 C CA . LEU A 1 80 ? 16.509 -1.127 8.880 1.00 27.28 ? 80 LEU A CA 1 ATOM 446 C C . LEU A 1 80 ? 15.263 -0.373 8.387 1.00 23.38 ? 80 LEU A C 1 ATOM 447 O O . LEU A 1 80 ? 14.887 0.681 8.896 1.00 25.70 ? 80 LEU A O 1 ATOM 448 C CB . LEU A 1 80 ? 17.635 -0.160 9.182 1.00 26.35 ? 80 LEU A CB 1 ATOM 449 C CG . LEU A 1 80 ? 18.911 -0.744 9.803 1.00 30.57 ? 80 LEU A CG 1 ATOM 450 C CD1 . LEU A 1 80 ? 19.947 0.349 10.022 1.00 27.61 ? 80 LEU A CD1 1 ATOM 451 C CD2 . LEU A 1 80 ? 18.589 -1.476 11.096 1.00 30.61 ? 80 LEU A CD2 1 ATOM 452 N N . ASN A 1 81 ? 14.617 -0.967 7.391 1.00 25.24 ? 81 ASN A N 1 ATOM 453 C CA . ASN A 1 81 ? 13.386 -0.472 6.828 1.00 31.46 ? 81 ASN A CA 1 ATOM 454 C C . ASN A 1 81 ? 13.509 0.797 6.017 1.00 29.24 ? 81 ASN A C 1 ATOM 455 O O . ASN A 1 81 ? 12.554 1.583 5.946 1.00 25.98 ? 81 ASN A O 1 ATOM 456 C CB . ASN A 1 81 ? 12.315 -0.302 7.934 1.00 25.75 ? 81 ASN A CB 1 ATOM 457 C CG . ASN A 1 81 ? 11.831 -1.651 8.437 1.00 29.95 ? 81 ASN A CG 1 ATOM 458 O OD1 . ASN A 1 81 ? 10.775 -2.151 8.038 1.00 33.68 ? 81 ASN A OD1 1 ATOM 459 N ND2 . ASN A 1 81 ? 12.598 -2.281 9.312 1.00 26.55 ? 81 ASN A ND2 1 ATOM 460 N N . PHE A 1 82 ? 14.655 1.037 5.387 1.00 27.13 ? 82 PHE A N 1 ATOM 461 C CA . PHE A 1 82 ? 14.815 2.226 4.550 1.00 28.45 ? 82 PHE A CA 1 ATOM 462 C C . PHE A 1 82 ? 14.738 1.769 3.084 1.00 27.36 ? 82 PHE A C 1 ATOM 463 O O . PHE A 1 82 ? 15.398 0.801 2.723 1.00 32.19 ? 82 PHE A O 1 ATOM 464 C CB . PHE A 1 82 ? 16.134 2.950 4.764 1.00 29.97 ? 82 PHE A CB 1 ATOM 465 C CG . PHE A 1 82 ? 16.304 3.620 6.093 1.00 29.08 ? 82 PHE A CG 1 ATOM 466 C CD1 . PHE A 1 82 ? 15.740 4.862 6.331 1.00 28.69 ? 82 PHE A CD1 1 ATOM 467 C CD2 . PHE A 1 82 ? 17.025 3.010 7.107 1.00 28.06 ? 82 PHE A CD2 1 ATOM 468 C CE1 . PHE A 1 82 ? 15.890 5.481 7.556 1.00 29.22 ? 82 PHE A CE1 1 ATOM 469 C CE2 . PHE A 1 82 ? 17.178 3.625 8.336 1.00 28.93 ? 82 PHE A CE2 1 ATOM 470 C CZ . PHE A 1 82 ? 16.608 4.861 8.560 1.00 28.94 ? 82 PHE A CZ 1 ATOM 471 N N . ASN A 1 83 ? 13.939 2.456 2.289 1.00 34.77 ? 83 ASN A N 1 ATOM 472 C CA . ASN A 1 83 ? 13.812 2.118 0.867 1.00 35.07 ? 83 ASN A CA 1 ATOM 473 C C . ASN A 1 83 ? 14.762 3.026 0.085 1.00 35.24 ? 83 ASN A C 1 ATOM 474 O O . ASN A 1 83 ? 14.448 4.183 -0.169 1.00 32.76 ? 83 ASN A O 1 ATOM 475 C CB . ASN A 1 83 ? 12.372 2.264 0.410 1.00 37.11 ? 83 ASN A CB 1 ATOM 476 C CG . ASN A 1 83 ? 12.121 1.820 -1.012 1.00 37.66 ? 83 ASN A CG 1 ATOM 477 O OD1 . ASN A 1 83 ? 13.011 1.877 -1.859 1.00 35.26 ? 83 ASN A OD1 1 ATOM 478 N ND2 . ASN A 1 83 ? 10.892 1.377 -1.286 1.00 37.26 ? 83 ASN A ND2 1 ATOM 479 N N . LEU A 1 84 ? 15.928 2.488 -0.263 1.00 35.04 ? 84 LEU A N 1 ATOM 480 C CA . LEU A 1 84 ? 16.940 3.263 -0.968 1.00 33.16 ? 84 LEU A CA 1 ATOM 481 C C . LEU A 1 84 ? 16.517 3.841 -2.291 1.00 36.17 ? 84 LEU A C 1 ATOM 482 O O . LEU A 1 84 ? 17.150 4.797 -2.785 1.00 35.84 ? 84 LEU A O 1 ATOM 483 C CB . LEU A 1 84 ? 18.233 2.434 -1.070 1.00 31.96 ? 84 LEU A CB 1 ATOM 484 C CG . LEU A 1 84 ? 18.693 1.878 0.298 1.00 34.46 ? 84 LEU A CG 1 ATOM 485 C CD1 . LEU A 1 84 ? 19.927 1.024 0.153 1.00 32.52 ? 84 LEU A CD1 1 ATOM 486 C CD2 . LEU A 1 84 ? 18.912 3.021 1.283 1.00 29.62 ? 84 LEU A CD2 1 ATOM 487 N N . THR A 1 85 ? 15.443 3.346 -2.896 1.00 39.17 ? 85 THR A N 1 ATOM 488 C CA . THR A 1 85 ? 14.979 3.909 -4.164 1.00 43.63 ? 85 THR A CA 1 ATOM 489 C C . THR A 1 85 ? 14.201 5.195 -3.920 1.00 42.75 ? 85 THR A C 1 ATOM 490 O O . THR A 1 85 ? 13.974 5.979 -4.838 1.00 43.49 ? 85 THR A O 1 ATOM 491 C CB . THR A 1 85 ? 14.110 2.918 -4.954 1.00 45.56 ? 85 THR A CB 1 ATOM 492 O OG1 . THR A 1 85 ? 12.840 2.760 -4.307 1.00 47.43 ? 85 THR A OG1 1 ATOM 493 C CG2 . THR A 1 85 ? 14.792 1.563 -5.041 1.00 43.76 ? 85 THR A CG2 1 ATOM 494 N N . GLU A 1 86 ? 13.808 5.425 -2.664 1.00 41.21 ? 86 GLU A N 1 ATOM 495 C CA . GLU A 1 86 ? 13.025 6.603 -2.329 1.00 40.95 ? 86 GLU A CA 1 ATOM 496 C C . GLU A 1 86 ? 13.703 7.601 -1.429 1.00 35.57 ? 86 GLU A C 1 ATOM 497 O O . GLU A 1 86 ? 13.411 8.810 -1.540 1.00 33.38 ? 86 GLU A O 1 ATOM 498 C CB . GLU A 1 86 ? 11.672 6.153 -1.733 1.00 43.64 ? 86 GLU A CB 1 ATOM 499 C CG . GLU A 1 86 ? 10.848 5.338 -2.723 1.00 47.80 ? 86 GLU A CG 1 ATOM 500 C CD . GLU A 1 86 ? 9.633 4.681 -2.108 1.00 51.80 ? 86 GLU A CD 1 ATOM 501 O OE1 . GLU A 1 86 ? 9.788 3.895 -1.148 1.00 53.30 ? 86 GLU A OE1 1 ATOM 502 O OE2 . GLU A 1 86 ? 8.505 4.944 -2.584 1.00 53.37 ? 86 GLU A OE2 1 ATOM 503 N N . ILE A 1 87 ? 14.582 7.180 -0.521 1.00 33.10 ? 87 ILE A N 1 ATOM 504 C CA . ILE A 1 87 ? 15.237 8.132 0.372 1.00 31.67 ? 87 ILE A CA 1 ATOM 505 C C . ILE A 1 87 ? 16.751 8.121 0.214 1.00 33.15 ? 87 ILE A C 1 ATOM 506 O O . ILE A 1 87 ? 17.393 7.085 0.394 1.00 33.89 ? 87 ILE A O 1 ATOM 507 C CB . ILE A 1 87 ? 14.906 7.875 1.857 1.00 32.93 ? 87 ILE A CB 1 ATOM 508 C CG1 . ILE A 1 87 ? 15.420 9.047 2.703 1.00 34.32 ? 87 ILE A CG1 1 ATOM 509 C CG2 . ILE A 1 87 ? 15.540 6.574 2.323 1.00 34.25 ? 87 ILE A CG2 1 ATOM 510 C CD1 . ILE A 1 87 ? 15.100 8.950 4.178 1.00 37.71 ? 87 ILE A CD1 1 ATOM 511 N N . PRO A 1 88 ? 17.322 9.274 -0.094 1.00 32.39 ? 88 PRO A N 1 ATOM 512 C CA . PRO A 1 88 ? 18.757 9.421 -0.272 1.00 33.80 ? 88 PRO A CA 1 ATOM 513 C C . PRO A 1 88 ? 19.523 9.109 1.001 1.00 33.90 ? 88 PRO A C 1 ATOM 514 O O . PRO A 1 88 ? 19.132 9.519 2.100 1.00 32.19 ? 88 PRO A O 1 ATOM 515 C CB . PRO A 1 88 ? 18.940 10.884 -0.668 1.00 36.12 ? 88 PRO A CB 1 ATOM 516 C CG . PRO A 1 88 ? 17.600 11.328 -1.147 1.00 34.06 ? 88 PRO A CG 1 ATOM 517 C CD . PRO A 1 88 ? 16.603 10.550 -0.321 1.00 30.66 ? 88 PRO A CD 1 ATOM 518 N N . GLU A 1 89 ? 20.636 8.402 0.864 1.00 35.89 ? 89 GLU A N 1 ATOM 519 C CA . GLU A 1 89 ? 21.473 8.019 1.981 1.00 37.84 ? 89 GLU A CA 1 ATOM 520 C C . GLU A 1 89 ? 21.884 9.186 2.859 1.00 41.23 ? 89 GLU A C 1 ATOM 521 O O . GLU A 1 89 ? 21.917 9.055 4.094 1.00 34.66 ? 89 GLU A O 1 ATOM 522 C CB . GLU A 1 89 ? 22.702 7.246 1.486 1.00 38.79 ? 89 GLU A CB 1 ATOM 523 C CG . GLU A 1 89 ? 22.384 5.811 1.069 1.00 40.74 ? 89 GLU A CG 1 ATOM 524 C CD . GLU A 1 89 ? 23.620 5.059 0.612 1.00 43.44 ? 89 GLU A CD 1 ATOM 525 O OE1 . GLU A 1 89 ? 24.733 5.453 1.018 1.00 44.00 ? 89 GLU A OE1 1 ATOM 526 O OE2 . GLU A 1 89 ? 23.487 4.078 -0.152 1.00 43.58 ? 89 GLU A OE2 1 ATOM 527 N N . ALA A 1 90 ? 22.195 10.334 2.262 1.00 36.54 ? 90 ALA A N 1 ATOM 528 C CA . ALA A 1 90 ? 22.610 11.498 3.040 1.00 38.98 ? 90 ALA A CA 1 ATOM 529 C C . ALA A 1 90 ? 21.525 11.905 4.033 1.00 38.96 ? 90 ALA A C 1 ATOM 530 O O . ALA A 1 90 ? 21.823 12.401 5.119 1.00 36.60 ? 90 ALA A O 1 ATOM 531 C CB . ALA A 1 90 ? 22.951 12.671 2.135 1.00 36.91 ? 90 ALA A CB 1 ATOM 532 N N . GLN A 1 91 ? 20.270 11.712 3.633 1.00 39.17 ? 91 GLN A N 1 ATOM 533 C CA . GLN A 1 91 ? 19.149 12.063 4.500 1.00 41.88 ? 91 GLN A CA 1 ATOM 534 C C . GLN A 1 91 ? 19.054 11.081 5.664 1.00 39.99 ? 91 GLN A C 1 ATOM 535 O O . GLN A 1 91 ? 18.663 11.446 6.770 1.00 39.92 ? 91 GLN A O 1 ATOM 536 C CB . GLN A 1 91 ? 17.842 12.093 3.713 1.00 43.42 ? 91 GLN A CB 1 ATOM 537 C CG . GLN A 1 91 ? 17.860 13.036 2.520 1.00 46.97 ? 91 GLN A CG 1 ATOM 538 C CD . GLN A 1 91 ? 16.518 13.706 2.298 1.00 48.10 ? 91 GLN A CD 1 ATOM 539 O OE1 . GLN A 1 91 ? 15.469 13.062 2.335 1.00 48.67 ? 91 GLN A OE1 1 ATOM 540 N NE2 . GLN A 1 91 ? 16.549 15.014 2.068 1.00 48.94 ? 91 GLN A NE2 1 ATOM 541 N N . ILE A 1 92 ? 19.419 9.834 5.393 1.00 38.58 ? 92 ILE A N 1 ATOM 542 C CA . ILE A 1 92 ? 19.388 8.793 6.418 1.00 36.82 ? 92 ILE A CA 1 ATOM 543 C C . ILE A 1 92 ? 20.360 9.119 7.540 1.00 38.96 ? 92 ILE A C 1 ATOM 544 O O . ILE A 1 92 ? 19.976 9.151 8.711 1.00 35.08 ? 92 ILE A O 1 ATOM 545 C CB . ILE A 1 92 ? 19.694 7.412 5.811 1.00 35.86 ? 92 ILE A CB 1 ATOM 546 C CG1 . ILE A 1 92 ? 18.621 7.056 4.780 1.00 34.18 ? 92 ILE A CG1 1 ATOM 547 C CG2 . ILE A 1 92 ? 19.761 6.353 6.903 1.00 35.99 ? 92 ILE A CG2 1 ATOM 548 C CD1 . ILE A 1 92 ? 18.833 5.762 4.038 1.00 31.84 ? 92 ILE A CD1 1 ATOM 549 N N . HIS A 1 93 ? 21.614 9.402 7.189 1.00 40.86 ? 93 HIS A N 1 ATOM 550 C CA . HIS A 1 93 ? 22.630 9.719 8.186 1.00 38.95 ? 93 HIS A CA 1 ATOM 551 C C . HIS A 1 93 ? 22.359 11.019 8.912 1.00 42.66 ? 93 HIS A C 1 ATOM 552 O O . HIS A 1 93 ? 22.564 11.099 10.135 1.00 42.13 ? 93 HIS A O 1 ATOM 553 C CB . HIS A 1 93 ? 24.028 9.700 7.569 1.00 38.99 ? 93 HIS A CB 1 ATOM 554 C CG . HIS A 1 93 ? 24.398 8.350 7.024 1.00 37.02 ? 93 HIS A CG 1 ATOM 555 N ND1 . HIS A 1 93 ? 24.524 7.240 7.834 1.00 37.42 ? 93 HIS A ND1 1 ATOM 556 C CD2 . HIS A 1 93 ? 24.663 7.934 5.767 1.00 36.86 ? 93 HIS A CD2 1 ATOM 557 C CE1 . HIS A 1 93 ? 24.853 6.196 7.094 1.00 35.62 ? 93 HIS A CE1 1 ATOM 558 N NE2 . HIS A 1 93 ? 24.941 6.587 5.837 1.00 36.07 ? 93 HIS A NE2 1 ATOM 559 N N . GLU A 1 94 ? 21.894 12.041 8.197 1.00 43.87 ? 94 GLU A N 1 ATOM 560 C CA . GLU A 1 94 ? 21.580 13.313 8.868 1.00 46.75 ? 94 GLU A CA 1 ATOM 561 C C . GLU A 1 94 ? 20.436 13.068 9.850 1.00 44.96 ? 94 GLU A C 1 ATOM 562 O O . GLU A 1 94 ? 20.368 13.655 10.925 1.00 40.91 ? 94 GLU A O 1 ATOM 563 C CB . GLU A 1 94 ? 21.247 14.398 7.867 1.00 48.84 ? 94 GLU A CB 1 ATOM 564 C CG . GLU A 1 94 ? 20.040 14.138 6.990 1.00 52.97 ? 94 GLU A CG 1 ATOM 565 C CD . GLU A 1 94 ? 18.746 14.638 7.600 1.00 55.40 ? 94 GLU A CD 1 ATOM 566 O OE1 . GLU A 1 94 ? 18.789 15.661 8.319 1.00 57.07 ? 94 GLU A OE1 1 ATOM 567 O OE2 . GLU A 1 94 ? 17.687 14.016 7.365 1.00 55.48 ? 94 GLU A OE2 1 ATOM 568 N N . GLY A 1 95 ? 19.541 12.156 9.461 1.00 40.50 ? 95 GLY A N 1 ATOM 569 C CA . GLY A 1 95 ? 18.406 11.806 10.310 1.00 41.10 ? 95 GLY A CA 1 ATOM 570 C C . GLY A 1 95 ? 18.914 11.237 11.636 1.00 36.20 ? 95 GLY A C 1 ATOM 571 O O . GLY A 1 95 ? 18.447 11.612 12.708 1.00 39.50 ? 95 GLY A O 1 ATOM 572 N N . PHE A 1 96 ? 19.886 10.330 11.539 1.00 36.03 ? 96 PHE A N 1 ATOM 573 C CA . PHE A 1 96 ? 20.458 9.731 12.742 1.00 35.90 ? 96 PHE A CA 1 ATOM 574 C C . PHE A 1 96 ? 21.248 10.781 13.517 1.00 40.39 ? 96 PHE A C 1 ATOM 575 O O . PHE A 1 96 ? 21.243 10.790 14.749 1.00 38.63 ? 96 PHE A O 1 ATOM 576 C CB . PHE A 1 96 ? 21.301 8.508 12.415 1.00 32.24 ? 96 PHE A CB 1 ATOM 577 C CG . PHE A 1 96 ? 20.487 7.266 12.165 1.00 30.57 ? 96 PHE A CG 1 ATOM 578 C CD1 . PHE A 1 96 ? 19.901 6.587 13.219 1.00 28.49 ? 96 PHE A CD1 1 ATOM 579 C CD2 . PHE A 1 96 ? 20.312 6.780 10.880 1.00 27.05 ? 96 PHE A CD2 1 ATOM 580 C CE1 . PHE A 1 96 ? 19.151 5.447 12.995 1.00 26.97 ? 96 PHE A CE1 1 ATOM 581 C CE2 . PHE A 1 96 ? 19.567 5.644 10.650 1.00 27.43 ? 96 PHE A CE2 1 ATOM 582 C CZ . PHE A 1 96 ? 18.984 4.974 11.712 1.00 27.60 ? 96 PHE A CZ 1 ATOM 583 N N . GLN A 1 97 ? 21.894 11.689 12.785 1.00 46.99 ? 97 GLN A N 1 ATOM 584 C CA . GLN A 1 97 ? 22.664 12.754 13.415 1.00 49.89 ? 97 GLN A CA 1 ATOM 585 C C . GLN A 1 97 ? 21.776 13.624 14.302 1.00 51.16 ? 97 GLN A C 1 ATOM 586 O O . GLN A 1 97 ? 22.091 13.843 15.473 1.00 51.19 ? 97 GLN A O 1 ATOM 587 C CB . GLN A 1 97 ? 23.385 13.617 12.384 1.00 51.42 ? 97 GLN A CB 1 ATOM 588 C CG . GLN A 1 97 ? 24.844 13.277 12.165 1.00 52.70 ? 97 GLN A CG 1 ATOM 589 C CD . GLN A 1 97 ? 25.126 12.562 10.865 1.00 54.01 ? 97 GLN A CD 1 ATOM 590 O OE1 . GLN A 1 97 ? 25.337 11.349 10.828 1.00 54.51 ? 97 GLN A OE1 1 ATOM 591 N NE2 . GLN A 1 97 ? 25.143 13.311 9.763 1.00 53.86 ? 97 GLN A NE2 1 ATOM 592 N N . GLU A 1 98 ? 20.677 14.124 13.745 1.00 52.56 ? 98 GLU A N 1 ATOM 593 C CA . GLU A 1 98 ? 19.762 14.964 14.512 1.00 53.97 ? 98 GLU A CA 1 ATOM 594 C C . GLU A 1 98 ? 19.221 14.204 15.721 1.00 54.10 ? 98 GLU A C 1 ATOM 595 O O . GLU A 1 98 ? 19.009 14.783 16.786 1.00 56.48 ? 98 GLU A O 1 ATOM 596 C CB . GLU A 1 98 ? 18.600 15.457 13.656 1.00 54.73 ? 98 GLU A CB 1 ATOM 597 C CG . GLU A 1 98 ? 18.885 16.693 12.829 1.00 56.39 ? 98 GLU A CG 1 ATOM 598 C CD . GLU A 1 98 ? 19.434 17.842 13.650 1.00 57.17 ? 98 GLU A CD 1 ATOM 599 O OE1 . GLU A 1 98 ? 20.633 17.800 14.005 1.00 58.80 ? 98 GLU A OE1 1 ATOM 600 O OE2 . GLU A 1 98 ? 18.682 18.791 13.943 1.00 56.24 ? 98 GLU A OE2 1 ATOM 601 N N . LEU A 1 99 ? 18.994 12.907 15.539 1.00 52.11 ? 99 LEU A N 1 ATOM 602 C CA . LEU A 1 99 ? 18.475 12.076 16.623 1.00 52.21 ? 99 LEU A CA 1 ATOM 603 C C . LEU A 1 99 ? 19.463 12.053 17.786 1.00 52.98 ? 99 LEU A C 1 ATOM 604 O O . LEU A 1 99 ? 19.089 12.210 18.946 1.00 52.36 ? 99 LEU A O 1 ATOM 605 C CB . LEU A 1 99 ? 18.202 10.656 16.132 1.00 51.45 ? 99 LEU A CB 1 ATOM 606 C CG . LEU A 1 99 ? 17.549 9.698 17.129 1.00 52.73 ? 99 LEU A CG 1 ATOM 607 C CD1 . LEU A 1 99 ? 16.059 9.980 17.252 1.00 52.90 ? 99 LEU A CD1 1 ATOM 608 C CD2 . LEU A 1 99 ? 17.789 8.250 16.732 1.00 52.07 ? 99 LEU A CD2 1 ATOM 609 N N . LEU A 1 100 ? 20.738 11.862 17.456 1.00 54.53 ? 100 LEU A N 1 ATOM 610 C CA . LEU A 1 100 ? 21.788 11.808 18.461 1.00 57.64 ? 100 LEU A CA 1 ATOM 611 C C . LEU A 1 100 ? 22.002 13.145 19.149 1.00 58.53 ? 100 LEU A C 1 ATOM 612 O O . LEU A 1 100 ? 22.138 13.195 20.376 1.00 57.69 ? 100 LEU A O 1 ATOM 613 C CB . LEU A 1 100 ? 23.090 11.287 17.850 1.00 56.43 ? 100 LEU A CB 1 ATOM 614 C CG . LEU A 1 100 ? 23.031 9.850 17.315 1.00 57.67 ? 100 LEU A CG 1 ATOM 615 C CD1 . LEU A 1 100 ? 24.425 9.329 17.012 1.00 57.56 ? 100 LEU A CD1 1 ATOM 616 C CD2 . LEU A 1 100 ? 22.316 8.939 18.301 1.00 56.32 ? 100 LEU A CD2 1 ATOM 617 N N . ARG A 1 101 ? 22.025 14.229 18.383 1.00 63.40 ? 101 ARG A N 1 ATOM 618 C CA . ARG A 1 101 ? 22.218 15.558 18.958 1.00 68.16 ? 101 ARG A CA 1 ATOM 619 C C . ARG A 1 101 ? 21.102 15.889 19.943 1.00 70.22 ? 101 ARG A C 1 ATOM 620 O O . ARG A 1 101 ? 21.194 16.847 20.707 1.00 67.22 ? 101 ARG A O 1 ATOM 621 C CB . ARG A 1 101 ? 22.291 16.617 17.859 1.00 68.79 ? 101 ARG A CB 1 ATOM 622 C CG . ARG A 1 101 ? 23.526 16.499 16.972 1.00 70.96 ? 101 ARG A CG 1 ATOM 623 C CD . ARG A 1 101 ? 23.302 17.184 15.634 1.00 72.66 ? 101 ARG A CD 1 ATOM 624 N NE . ARG A 1 101 ? 24.444 17.046 14.737 1.00 74.39 ? 101 ARG A NE 1 ATOM 625 C CZ . ARG A 1 101 ? 24.361 17.188 13.415 1.00 76.08 ? 101 ARG A CZ 1 ATOM 626 N NH1 . ARG A 1 101 ? 23.187 17.467 12.860 1.00 76.78 ? 101 ARG A NH1 1 ATOM 627 N NH2 . ARG A 1 101 ? 25.439 17.050 12.655 1.00 75.09 ? 101 ARG A NH2 1 ATOM 628 N N . THR A 1 102 ? 20.046 15.082 19.925 1.00 73.26 ? 102 THR A N 1 ATOM 629 C CA . THR A 1 102 ? 18.908 15.286 20.808 1.00 74.54 ? 102 THR A CA 1 ATOM 630 C C . THR A 1 102 ? 18.973 14.399 22.044 1.00 74.94 ? 102 THR A C 1 ATOM 631 O O . THR A 1 102 ? 18.752 14.858 23.165 1.00 75.67 ? 102 THR A O 1 ATOM 632 C CB . THR A 1 102 ? 17.580 15.007 20.069 1.00 74.87 ? 102 THR A CB 1 ATOM 633 O OG1 . THR A 1 102 ? 17.414 15.958 19.011 1.00 75.32 ? 102 THR A OG1 1 ATOM 634 C CG2 . THR A 1 102 ? 16.408 15.101 21.029 1.00 74.68 ? 102 THR A CG2 1 ATOM 635 N N . LEU A 1 103 ? 19.267 13.123 21.841 1.00 74.98 ? 103 LEU A N 1 ATOM 636 C CA . LEU A 1 103 ? 19.335 12.149 22.909 1.00 75.70 ? 103 LEU A CA 1 ATOM 637 C C . LEU A 1 103 ? 20.370 12.462 23.972 1.00 77.26 ? 103 LEU A C 1 ATOM 638 O O . LEU A 1 103 ? 20.223 12.007 25.116 1.00 77.15 ? 103 LEU A O 1 ATOM 639 C CB . LEU A 1 103 ? 19.596 10.742 22.346 1.00 75.52 ? 103 LEU A CB 1 ATOM 640 C CG . LEU A 1 103 ? 18.532 10.201 21.383 1.00 75.13 ? 103 LEU A CG 1 ATOM 641 C CD1 . LEU A 1 103 ? 18.794 8.726 21.085 1.00 74.67 ? 103 LEU A CD1 1 ATOM 642 C CD2 . LEU A 1 103 ? 17.143 10.367 21.995 1.00 74.82 ? 103 LEU A CD2 1 ATOM 643 N N . ASN A 1 104 ? 21.421 13.204 23.629 1.00 80.97 ? 104 ASN A N 1 ATOM 644 C CA . ASN A 1 104 ? 22.451 13.512 24.615 1.00 84.80 ? 104 ASN A CA 1 ATOM 645 C C . ASN A 1 104 ? 22.875 14.969 24.608 1.00 85.26 ? 104 ASN A C 1 ATOM 646 O O . ASN A 1 104 ? 23.879 15.342 24.002 1.00 85.72 ? 104 ASN A O 1 ATOM 647 C CB . ASN A 1 104 ? 23.657 12.591 24.446 1.00 85.27 ? 104 ASN A CB 1 ATOM 648 C CG . ASN A 1 104 ? 24.313 12.697 23.088 1.00 85.75 ? 104 ASN A CG 1 ATOM 649 O OD1 . ASN A 1 104 ? 23.809 12.166 22.098 1.00 86.23 ? 104 ASN A OD1 1 ATOM 650 N ND2 . ASN A 1 104 ? 25.448 13.384 23.031 1.00 85.96 ? 104 ASN A ND2 1 ATOM 651 N N . GLN A 1 105 ? 22.103 15.799 25.304 1.00 87.58 ? 105 GLN A N 1 ATOM 652 C CA . GLN A 1 105 ? 22.404 17.225 25.408 1.00 88.37 ? 105 GLN A CA 1 ATOM 653 C C . GLN A 1 105 ? 22.720 17.566 26.860 1.00 89.69 ? 105 GLN A C 1 ATOM 654 O O . GLN A 1 105 ? 22.198 16.935 27.781 1.00 87.67 ? 105 GLN A O 1 ATOM 655 C CB . GLN A 1 105 ? 21.287 18.081 24.836 1.00 88.31 ? 105 GLN A CB 1 ATOM 656 C CG . GLN A 1 105 ? 21.296 18.131 23.310 1.00 87.89 ? 105 GLN A CG 1 ATOM 657 C CD . GLN A 1 105 ? 20.150 18.938 22.745 1.00 88.41 ? 105 GLN A CD 1 ATOM 658 O OE1 . GLN A 1 105 ? 18.983 18.595 22.943 1.00 88.59 ? 105 GLN A OE1 1 ATOM 659 N NE2 . GLN A 1 105 ? 20.475 20.017 22.037 1.00 88.18 ? 105 GLN A NE2 1 ATOM 660 N N . PRO A 1 106 ? 23.604 18.530 27.069 1.00 91.15 ? 106 PRO A N 1 ATOM 661 C CA . PRO A 1 106 ? 24.051 18.936 28.373 1.00 92.12 ? 106 PRO A CA 1 ATOM 662 C C . PRO A 1 106 ? 22.990 19.212 29.412 1.00 92.38 ? 106 PRO A C 1 ATOM 663 O O . PRO A 1 106 ? 22.570 18.327 30.164 1.00 90.97 ? 106 PRO A O 1 ATOM 664 C CB . PRO A 1 106 ? 24.878 20.198 28.099 1.00 91.82 ? 106 PRO A CB 1 ATOM 665 C CG . PRO A 1 106 ? 25.368 20.021 26.705 1.00 91.65 ? 106 PRO A CG 1 ATOM 666 C CD . PRO A 1 106 ? 24.276 19.291 25.977 1.00 90.53 ? 106 PRO A CD 1 ATOM 667 N N . ASP A 1 107 ? 22.549 20.458 29.500 1.00 94.77 ? 107 ASP A N 1 ATOM 668 C CA . ASP A 1 107 ? 21.578 20.933 30.448 1.00 96.37 ? 107 ASP A CA 1 ATOM 669 C C . ASP A 1 107 ? 20.325 20.106 30.624 1.00 95.90 ? 107 ASP A C 1 ATOM 670 O O . ASP A 1 107 ? 19.595 20.328 31.609 1.00 96.40 ? 107 ASP A O 1 ATOM 671 C CB . ASP A 1 107 ? 21.184 22.390 30.111 1.00 96.33 ? 107 ASP A CB 1 ATOM 672 C CG . ASP A 1 107 ? 20.795 23.160 31.360 1.00 96.61 ? 107 ASP A CG 1 ATOM 673 O OD1 . ASP A 1 107 ? 21.394 22.903 32.427 1.00 96.42 ? 107 ASP A OD1 1 ATOM 674 O OD2 . ASP A 1 107 ? 19.894 24.018 31.275 1.00 96.92 ? 107 ASP A OD2 1 ATOM 675 N N . SER A 1 108 ? 20.031 19.174 29.730 1.00 93.90 ? 108 SER A N 1 ATOM 676 C CA . SER A 1 108 ? 18.823 18.356 29.858 1.00 92.30 ? 108 SER A CA 1 ATOM 677 C C . SER A 1 108 ? 19.139 16.871 29.778 1.00 89.78 ? 108 SER A C 1 ATOM 678 O O . SER A 1 108 ? 19.769 16.423 28.816 1.00 90.41 ? 108 SER A O 1 ATOM 679 C CB . SER A 1 108 ? 17.822 18.736 28.762 1.00 92.72 ? 108 SER A CB 1 ATOM 680 O OG . SER A 1 108 ? 17.575 20.130 28.762 1.00 93.43 ? 108 SER A OG 1 ATOM 681 N N . GLN A 1 109 ? 18.697 16.098 30.773 1.00 85.21 ? 109 GLN A N 1 ATOM 682 C CA . GLN A 1 109 ? 18.973 14.670 30.759 1.00 82.88 ? 109 GLN A CA 1 ATOM 683 C C . GLN A 1 109 ? 17.786 13.794 31.116 1.00 81.06 ? 109 GLN A C 1 ATOM 684 O O . GLN A 1 109 ? 17.207 13.858 32.195 1.00 78.50 ? 109 GLN A O 1 ATOM 685 C CB . GLN A 1 109 ? 20.176 14.344 31.645 1.00 83.26 ? 109 GLN A CB 1 ATOM 686 C CG . GLN A 1 109 ? 20.197 15.066 32.979 1.00 83.49 ? 109 GLN A CG 1 ATOM 687 C CD . GLN A 1 109 ? 21.539 14.943 33.677 1.00 83.78 ? 109 GLN A CD 1 ATOM 688 O OE1 . GLN A 1 109 ? 21.785 15.604 34.685 1.00 84.07 ? 109 GLN A OE1 1 ATOM 689 N NE2 . GLN A 1 109 ? 22.410 14.097 33.138 1.00 83.38 ? 109 GLN A NE2 1 ATOM 690 N N . LEU A 1 110 ? 17.439 12.930 30.162 1.00 76.34 ? 110 LEU A N 1 ATOM 691 C CA . LEU A 1 110 ? 16.349 11.971 30.324 1.00 73.82 ? 110 LEU A CA 1 ATOM 692 C C . LEU A 1 110 ? 16.887 10.778 31.127 1.00 73.05 ? 110 LEU A C 1 ATOM 693 O O . LEU A 1 110 ? 16.194 9.825 31.438 1.00 73.66 ? 110 LEU A O 1 ATOM 694 C CB . LEU A 1 110 ? 15.868 11.507 28.954 1.00 73.51 ? 110 LEU A CB 1 ATOM 695 C CG . LEU A 1 110 ? 14.809 10.407 28.914 1.00 73.24 ? 110 LEU A CG 1 ATOM 696 C CD1 . LEU A 1 110 ? 13.557 10.838 29.662 1.00 73.51 ? 110 LEU A CD1 1 ATOM 697 C CD2 . LEU A 1 110 ? 14.476 10.046 27.473 1.00 73.46 ? 110 LEU A CD2 1 ATOM 698 N N . GLN A 1 111 ? 18.176 10.879 31.442 1.00 70.72 ? 111 GLN A N 1 ATOM 699 C CA . GLN A 1 111 ? 18.883 9.860 32.195 1.00 71.09 ? 111 GLN A CA 1 ATOM 700 C C . GLN A 1 111 ? 18.946 8.552 31.413 1.00 69.57 ? 111 GLN A C 1 ATOM 701 O O . GLN A 1 111 ? 18.434 7.522 31.845 1.00 69.08 ? 111 GLN A O 1 ATOM 702 C CB . GLN A 1 111 ? 18.248 9.642 33.567 1.00 71.76 ? 111 GLN A CB 1 ATOM 703 C CG . GLN A 1 111 ? 19.272 9.405 34.672 1.00 73.24 ? 111 GLN A CG 1 ATOM 704 C CD . GLN A 1 111 ? 20.313 10.508 34.726 1.00 73.59 ? 111 GLN A CD 1 ATOM 705 O OE1 . GLN A 1 111 ? 20.017 11.632 35.132 1.00 74.30 ? 111 GLN A OE1 1 ATOM 706 N NE2 . GLN A 1 111 ? 21.535 10.192 34.315 1.00 73.54 ? 111 GLN A NE2 1 ATOM 707 N N . LEU A 1 112 ? 19.584 8.619 30.246 1.00 63.86 ? 112 LEU A N 1 ATOM 708 C CA . LEU A 1 112 ? 19.724 7.449 29.388 1.00 61.26 ? 112 LEU A CA 1 ATOM 709 C C . LEU A 1 112 ? 21.180 7.000 29.315 1.00 58.79 ? 112 LEU A C 1 ATOM 710 O O . LEU A 1 112 ? 22.041 7.729 28.823 1.00 59.61 ? 112 LEU A O 1 ATOM 711 C CB . LEU A 1 112 ? 19.191 7.753 27.987 1.00 61.19 ? 112 LEU A CB 1 ATOM 712 C CG . LEU A 1 112 ? 18.941 6.550 27.076 1.00 61.65 ? 112 LEU A CG 1 ATOM 713 C CD1 . LEU A 1 112 ? 17.832 5.672 27.636 1.00 61.23 ? 112 LEU A CD1 1 ATOM 714 C CD2 . LEU A 1 112 ? 18.604 7.008 25.664 1.00 61.80 ? 112 LEU A CD2 1 ATOM 715 N N . THR A 1 113 ? 21.447 5.800 29.815 1.00 52.79 ? 113 THR A N 1 ATOM 716 C CA . THR A 1 113 ? 22.807 5.251 29.792 1.00 48.96 ? 113 THR A CA 1 ATOM 717 C C . THR A 1 113 ? 22.921 4.276 28.622 1.00 47.98 ? 113 THR A C 1 ATOM 718 O O . THR A 1 113 ? 22.429 3.151 28.694 1.00 44.37 ? 113 THR A O 1 ATOM 719 C CB . THR A 1 113 ? 23.158 4.557 31.111 1.00 50.16 ? 113 THR A CB 1 ATOM 720 O OG1 . THR A 1 113 ? 23.223 5.537 32.162 1.00 49.33 ? 113 THR A OG1 1 ATOM 721 C CG2 . THR A 1 113 ? 24.492 3.836 31.028 1.00 50.04 ? 113 THR A CG2 1 ATOM 722 N N . THR A 1 114 ? 23.540 4.734 27.540 1.00 45.12 ? 114 THR A N 1 ATOM 723 C CA . THR A 1 114 ? 23.685 3.926 26.339 1.00 46.01 ? 114 THR A CA 1 ATOM 724 C C . THR A 1 114 ? 25.101 3.953 25.787 1.00 45.33 ? 114 THR A C 1 ATOM 725 O O . THR A 1 114 ? 25.889 4.852 26.083 1.00 43.67 ? 114 THR A O 1 ATOM 726 C CB . THR A 1 114 ? 22.712 4.427 25.245 1.00 45.93 ? 114 THR A CB 1 ATOM 727 O OG1 . THR A 1 114 ? 22.680 3.502 24.156 1.00 47.11 ? 114 THR A OG1 1 ATOM 728 C CG2 . THR A 1 114 ? 23.163 5.789 24.741 1.00 47.50 ? 114 THR A CG2 1 ATOM 729 N N . GLY A 1 115 ? 25.427 2.949 24.962 1.00 41.40 ? 115 GLY A N 1 ATOM 730 C CA . GLY A 1 115 ? 26.749 2.875 24.373 1.00 30.77 ? 115 GLY A CA 1 ATOM 731 C C . GLY A 1 115 ? 26.842 1.812 23.283 1.00 31.02 ? 115 GLY A C 1 ATOM 732 O O . GLY A 1 115 ? 26.079 0.852 23.238 1.00 29.19 ? 115 GLY A O 1 ATOM 733 N N . ASN A 1 116 ? 27.795 2.028 22.384 1.00 29.16 ? 116 ASN A N 1 ATOM 734 C CA . ASN A 1 116 ? 28.046 1.089 21.289 1.00 34.99 ? 116 ASN A CA 1 ATOM 735 C C . ASN A 1 116 ? 29.565 0.930 21.166 1.00 34.94 ? 116 ASN A C 1 ATOM 736 O O . ASN A 1 116 ? 30.271 1.922 20.984 1.00 33.21 ? 116 ASN A O 1 ATOM 737 C CB . ASN A 1 116 ? 27.428 1.566 19.988 1.00 38.54 ? 116 ASN A CB 1 ATOM 738 C CG . ASN A 1 116 ? 27.386 0.504 18.909 1.00 40.74 ? 116 ASN A CG 1 ATOM 739 O OD1 . ASN A 1 116 ? 26.577 -0.420 18.933 1.00 37.96 ? 116 ASN A OD1 1 ATOM 740 N ND2 . ASN A 1 116 ? 28.277 0.629 17.930 1.00 42.29 ? 116 ASN A ND2 1 ATOM 741 N N . GLY A 1 117 ? 30.046 -0.303 21.293 1.00 34.25 ? 117 GLY A N 1 ATOM 742 C CA . GLY A 1 117 ? 31.480 -0.546 21.227 1.00 30.32 ? 117 GLY A CA 1 ATOM 743 C C . GLY A 1 117 ? 31.866 -1.473 20.074 1.00 30.20 ? 117 GLY A C 1 ATOM 744 O O . GLY A 1 117 ? 31.299 -2.540 19.890 1.00 26.16 ? 117 GLY A O 1 ATOM 745 N N . LEU A 1 118 ? 32.849 -1.032 19.307 1.00 24.10 ? 118 LEU A N 1 ATOM 746 C CA . LEU A 1 118 ? 33.369 -1.800 18.176 1.00 31.09 ? 118 LEU A CA 1 ATOM 747 C C . LEU A 1 118 ? 34.732 -2.388 18.580 1.00 30.67 ? 118 LEU A C 1 ATOM 748 O O . LEU A 1 118 ? 35.609 -1.625 18.980 1.00 31.56 ? 118 LEU A O 1 ATOM 749 C CB . LEU A 1 118 ? 33.556 -0.907 16.969 1.00 30.06 ? 118 LEU A CB 1 ATOM 750 C CG . LEU A 1 118 ? 32.355 -0.289 16.279 1.00 34.85 ? 118 LEU A CG 1 ATOM 751 C CD1 . LEU A 1 118 ? 32.770 0.367 14.969 1.00 35.48 ? 118 LEU A CD1 1 ATOM 752 C CD2 . LEU A 1 118 ? 31.262 -1.325 16.018 1.00 35.97 ? 118 LEU A CD2 1 ATOM 753 N N . PHE A 1 119 ? 34.882 -3.698 18.491 1.00 32.80 ? 119 PHE A N 1 ATOM 754 C CA . PHE A 1 119 ? 36.155 -4.333 18.869 1.00 28.69 ? 119 PHE A CA 1 ATOM 755 C C . PHE A 1 119 ? 36.768 -5.012 17.652 1.00 29.81 ? 119 PHE A C 1 ATOM 756 O O . PHE A 1 119 ? 36.239 -5.998 17.152 1.00 24.81 ? 119 PHE A O 1 ATOM 757 C CB . PHE A 1 119 ? 35.910 -5.307 20.027 1.00 29.74 ? 119 PHE A CB 1 ATOM 758 C CG . PHE A 1 119 ? 35.483 -4.573 21.282 1.00 31.29 ? 119 PHE A CG 1 ATOM 759 C CD1 . PHE A 1 119 ? 34.154 -4.259 21.496 1.00 31.13 ? 119 PHE A CD1 1 ATOM 760 C CD2 . PHE A 1 119 ? 36.418 -4.193 22.226 1.00 31.07 ? 119 PHE A CD2 1 ATOM 761 C CE1 . PHE A 1 119 ? 33.766 -3.583 22.641 1.00 33.72 ? 119 PHE A CE1 1 ATOM 762 C CE2 . PHE A 1 119 ? 36.040 -3.516 23.370 1.00 32.13 ? 119 PHE A CE2 1 ATOM 763 C CZ . PHE A 1 119 ? 34.708 -3.207 23.581 1.00 32.13 ? 119 PHE A CZ 1 ATOM 764 N N . LEU A 1 120 ? 37.871 -4.458 17.161 1.00 30.27 ? 120 LEU A N 1 ATOM 765 C CA . LEU A 1 120 ? 38.558 -4.955 15.986 1.00 31.02 ? 120 LEU A CA 1 ATOM 766 C C . LEU A 1 120 ? 39.931 -5.544 16.283 1.00 30.39 ? 120 LEU A C 1 ATOM 767 O O . LEU A 1 120 ? 40.722 -4.987 17.045 1.00 29.03 ? 120 LEU A O 1 ATOM 768 C CB . LEU A 1 120 ? 38.738 -3.797 14.981 1.00 30.42 ? 120 LEU A CB 1 ATOM 769 C CG . LEU A 1 120 ? 37.465 -3.311 14.281 1.00 29.13 ? 120 LEU A CG 1 ATOM 770 C CD1 . LEU A 1 120 ? 37.666 -1.907 13.728 1.00 29.75 ? 120 LEU A CD1 1 ATOM 771 C CD2 . LEU A 1 120 ? 37.083 -4.279 13.168 1.00 30.01 ? 120 LEU A CD2 1 ATOM 772 N N . SER A 1 121 ? 40.237 -6.656 15.630 1.00 31.47 ? 121 SER A N 1 ATOM 773 C CA . SER A 1 121 ? 41.506 -7.339 15.787 1.00 33.04 ? 121 SER A CA 1 ATOM 774 C C . SER A 1 121 ? 42.698 -6.405 15.641 1.00 32.50 ? 121 SER A C 1 ATOM 775 O O . SER A 1 121 ? 42.749 -5.581 14.726 1.00 31.93 ? 121 SER A O 1 ATOM 776 C CB . SER A 1 121 ? 41.622 -8.458 14.727 1.00 33.81 ? 121 SER A CB 1 ATOM 777 O OG . SER A 1 121 ? 42.979 -8.851 14.600 1.00 36.59 ? 121 SER A OG 1 ATOM 778 N N . GLU A 1 122 ? 43.654 -6.521 16.561 1.00 39.87 ? 122 GLU A N 1 ATOM 779 C CA . GLU A 1 122 ? 44.876 -5.700 16.447 1.00 46.07 ? 122 GLU A CA 1 ATOM 780 C C . GLU A 1 122 ? 45.657 -6.290 15.266 1.00 46.14 ? 122 GLU A C 1 ATOM 781 O O . GLU A 1 122 ? 45.461 -7.479 14.978 1.00 48.44 ? 122 GLU A O 1 ATOM 782 C CB . GLU A 1 122 ? 45.707 -5.766 17.715 1.00 46.53 ? 122 GLU A CB 1 ATOM 783 C CG . GLU A 1 122 ? 46.393 -7.104 17.939 1.00 48.94 ? 122 GLU A CG 1 ATOM 784 C CD . GLU A 1 122 ? 47.180 -7.166 19.231 1.00 49.83 ? 122 GLU A CD 1 ATOM 785 O OE1 . GLU A 1 122 ? 47.983 -8.111 19.393 1.00 51.66 ? 122 GLU A OE1 1 ATOM 786 O OE2 . GLU A 1 122 ? 47.006 -6.277 20.089 1.00 50.06 ? 122 GLU A OE2 1 ATOM 787 N N . GLY A 1 123 ? 46.480 -5.503 14.603 1.00 44.35 ? 123 GLY A N 1 ATOM 788 C CA . GLY A 1 123 ? 47.223 -6.057 13.452 1.00 49.67 ? 123 GLY A CA 1 ATOM 789 C C . GLY A 1 123 ? 46.434 -5.769 12.173 1.00 50.05 ? 123 GLY A C 1 ATOM 790 O O . GLY A 1 123 ? 46.907 -6.008 11.069 1.00 49.86 ? 123 GLY A O 1 ATOM 791 N N . LEU A 1 124 ? 45.221 -5.249 12.352 1.00 48.86 ? 124 LEU A N 1 ATOM 792 C CA . LEU A 1 124 ? 44.378 -4.881 11.224 1.00 48.30 ? 124 LEU A CA 1 ATOM 793 C C . LEU A 1 124 ? 44.673 -3.425 10.839 1.00 46.45 ? 124 LEU A C 1 ATOM 794 O O . LEU A 1 124 ? 44.776 -2.574 11.721 1.00 43.25 ? 124 LEU A O 1 ATOM 795 C CB . LEU A 1 124 ? 42.898 -5.001 11.565 1.00 49.49 ? 124 LEU A CB 1 ATOM 796 C CG . LEU A 1 124 ? 42.195 -6.325 11.296 1.00 49.31 ? 124 LEU A CG 1 ATOM 797 C CD1 . LEU A 1 124 ? 40.716 -6.218 11.646 1.00 48.59 ? 124 LEU A CD1 1 ATOM 798 C CD2 . LEU A 1 124 ? 42.366 -6.753 9.844 1.00 49.42 ? 124 LEU A CD2 1 ATOM 799 N N . LYS A 1 125 ? 44.819 -3.172 9.549 1.00 43.37 ? 125 LYS A N 1 ATOM 800 C CA . LYS A 1 125 ? 45.055 -1.803 9.086 1.00 42.93 ? 125 LYS A CA 1 ATOM 801 C C . LYS A 1 125 ? 43.687 -1.135 8.897 1.00 44.72 ? 125 LYS A C 1 ATOM 802 O O . LYS A 1 125 ? 43.030 -1.366 7.885 1.00 47.17 ? 125 LYS A O 1 ATOM 803 C CB . LYS A 1 125 ? 45.848 -1.793 7.790 1.00 44.12 ? 125 LYS A CB 1 ATOM 804 C CG . LYS A 1 125 ? 46.336 -0.416 7.354 1.00 45.75 ? 125 LYS A CG 1 ATOM 805 C CD . LYS A 1 125 ? 46.927 -0.492 5.944 1.00 50.21 ? 125 LYS A CD 1 ATOM 806 C CE . LYS A 1 125 ? 47.211 0.889 5.386 1.00 50.08 ? 125 LYS A CE 1 ATOM 807 N NZ . LYS A 1 125 ? 47.780 0.836 4.013 1.00 51.03 ? 125 LYS A NZ 1 ATOM 808 N N . LEU A 1 126 ? 43.271 -0.358 9.889 1.00 41.29 ? 126 LEU A N 1 ATOM 809 C CA . LEU A 1 126 ? 41.979 0.312 9.846 1.00 41.05 ? 126 LEU A CA 1 ATOM 810 C C . LEU A 1 126 ? 42.004 1.573 9.003 1.00 42.26 ? 126 LEU A C 1 ATOM 811 O O . LEU A 1 126 ? 43.025 2.254 8.912 1.00 47.32 ? 126 LEU A O 1 ATOM 812 C CB . LEU A 1 126 ? 41.527 0.657 11.281 1.00 37.85 ? 126 LEU A CB 1 ATOM 813 C CG . LEU A 1 126 ? 41.588 -0.520 12.258 1.00 35.86 ? 126 LEU A CG 1 ATOM 814 C CD1 . LEU A 1 126 ? 41.199 -0.097 13.663 1.00 36.90 ? 126 LEU A CD1 1 ATOM 815 C CD2 . LEU A 1 126 ? 40.710 -1.664 11.776 1.00 34.56 ? 126 LEU A CD2 1 ATOM 816 N N . VAL A 1 127 ? 40.879 1.877 8.373 1.00 45.49 ? 127 VAL A N 1 ATOM 817 C CA . VAL A 1 127 ? 40.751 3.074 7.544 1.00 44.16 ? 127 VAL A CA 1 ATOM 818 C C . VAL A 1 127 ? 40.371 4.262 8.421 1.00 46.83 ? 127 VAL A C 1 ATOM 819 O O . VAL A 1 127 ? 39.352 4.225 9.112 1.00 43.23 ? 127 VAL A O 1 ATOM 820 C CB . VAL A 1 127 ? 39.695 2.886 6.447 1.00 44.22 ? 127 VAL A CB 1 ATOM 821 C CG1 . VAL A 1 127 ? 39.525 4.160 5.634 1.00 45.46 ? 127 VAL A CG1 1 ATOM 822 C CG2 . VAL A 1 127 ? 40.076 1.720 5.546 1.00 45.35 ? 127 VAL A CG2 1 ATOM 823 N N . ASP A 1 128 ? 41.193 5.302 8.396 1.00 46.57 ? 128 ASP A N 1 ATOM 824 C CA . ASP A 1 128 ? 40.967 6.486 9.201 1.00 49.94 ? 128 ASP A CA 1 ATOM 825 C C . ASP A 1 128 ? 39.560 7.041 9.113 1.00 49.41 ? 128 ASP A C 1 ATOM 826 O O . ASP A 1 128 ? 38.906 7.222 10.149 1.00 49.65 ? 128 ASP A O 1 ATOM 827 C CB . ASP A 1 128 ? 42.006 7.566 8.875 1.00 51.16 ? 128 ASP A CB 1 ATOM 828 C CG . ASP A 1 128 ? 43.370 7.228 9.458 1.00 52.80 ? 128 ASP A CG 1 ATOM 829 O OD1 . ASP A 1 128 ? 43.456 7.059 10.694 1.00 53.78 ? 128 ASP A OD1 1 ATOM 830 O OD2 . ASP A 1 128 ? 44.344 7.130 8.689 1.00 52.96 ? 128 ASP A OD2 1 ATOM 831 N N . LYS A 1 129 ? 39.076 7.336 7.915 1.00 46.52 ? 129 LYS A N 1 ATOM 832 C CA . LYS A 1 129 ? 37.745 7.897 7.731 1.00 44.48 ? 129 LYS A CA 1 ATOM 833 C C . LYS A 1 129 ? 36.699 7.167 8.559 1.00 44.36 ? 129 LYS A C 1 ATOM 834 O O . LYS A 1 129 ? 35.862 7.800 9.208 1.00 42.48 ? 129 LYS A O 1 ATOM 835 C CB . LYS A 1 129 ? 37.352 7.899 6.253 1.00 46.61 ? 129 LYS A CB 1 ATOM 836 C CG . LYS A 1 129 ? 36.083 8.676 5.945 1.00 47.43 ? 129 LYS A CG 1 ATOM 837 C CD . LYS A 1 129 ? 36.322 10.176 6.001 1.00 48.51 ? 129 LYS A CD 1 ATOM 838 C CE . LYS A 1 129 ? 35.031 10.956 5.816 1.00 49.12 ? 129 LYS A CE 1 ATOM 839 N NZ . LYS A 1 129 ? 34.147 10.866 7.012 1.00 50.68 ? 129 LYS A NZ 1 ATOM 840 N N . PHE A 1 130 ? 36.739 5.835 8.546 1.00 41.77 ? 130 PHE A N 1 ATOM 841 C CA . PHE A 1 130 ? 35.785 5.047 9.310 1.00 39.49 ? 130 PHE A CA 1 ATOM 842 C C . PHE A 1 130 ? 35.853 5.389 10.798 1.00 43.39 ? 130 PHE A C 1 ATOM 843 O O . PHE A 1 130 ? 34.832 5.676 11.419 1.00 42.06 ? 130 PHE A O 1 ATOM 844 C CB . PHE A 1 130 ? 35.992 3.546 9.115 1.00 39.01 ? 130 PHE A CB 1 ATOM 845 C CG . PHE A 1 130 ? 35.025 2.720 9.921 1.00 38.00 ? 130 PHE A CG 1 ATOM 846 C CD1 . PHE A 1 130 ? 33.662 2.819 9.696 1.00 37.64 ? 130 PHE A CD1 1 ATOM 847 C CD2 . PHE A 1 130 ? 35.479 1.854 10.903 1.00 38.05 ? 130 PHE A CD2 1 ATOM 848 C CE1 . PHE A 1 130 ? 32.769 2.065 10.437 1.00 37.28 ? 130 PHE A CE1 1 ATOM 849 C CE2 . PHE A 1 130 ? 34.594 1.102 11.642 1.00 36.41 ? 130 PHE A CE2 1 ATOM 850 C CZ . PHE A 1 130 ? 33.235 1.206 11.408 1.00 37.80 ? 130 PHE A CZ 1 ATOM 851 N N . LEU A 1 131 ? 37.057 5.348 11.352 1.00 43.62 ? 131 LEU A N 1 ATOM 852 C CA . LEU A 1 131 ? 37.269 5.647 12.761 1.00 46.53 ? 131 LEU A CA 1 ATOM 853 C C . LEU A 1 131 ? 36.804 7.059 13.094 1.00 48.15 ? 131 LEU A C 1 ATOM 854 O O . LEU A 1 131 ? 36.344 7.321 14.203 1.00 45.38 ? 131 LEU A O 1 ATOM 855 C CB . LEU A 1 131 ? 38.738 5.451 13.137 1.00 46.70 ? 131 LEU A CB 1 ATOM 856 C CG . LEU A 1 131 ? 39.300 4.047 12.875 1.00 45.78 ? 131 LEU A CG 1 ATOM 857 C CD1 . LEU A 1 131 ? 40.665 3.889 13.521 1.00 46.13 ? 131 LEU A CD1 1 ATOM 858 C CD2 . LEU A 1 131 ? 38.328 2.990 13.378 1.00 45.02 ? 131 LEU A CD2 1 ATOM 859 N N . GLU A 1 132 ? 36.914 7.957 12.118 1.00 49.20 ? 132 GLU A N 1 ATOM 860 C CA . GLU A 1 132 ? 36.478 9.337 12.287 1.00 49.98 ? 132 GLU A CA 1 ATOM 861 C C . GLU A 1 132 ? 34.947 9.390 12.363 1.00 47.72 ? 132 GLU A C 1 ATOM 862 O O . GLU A 1 132 ? 34.379 10.012 13.254 1.00 47.54 ? 132 GLU A O 1 ATOM 863 C CB . GLU A 1 132 ? 36.945 10.209 11.124 1.00 50.81 ? 132 GLU A CB 1 ATOM 864 C CG . GLU A 1 132 ? 38.442 10.394 10.996 1.00 53.58 ? 132 GLU A CG 1 ATOM 865 C CD . GLU A 1 132 ? 38.853 10.905 9.625 1.00 54.04 ? 132 GLU A CD 1 ATOM 866 O OE1 . GLU A 1 132 ? 38.148 11.770 9.069 1.00 53.87 ? 132 GLU A OE1 1 ATOM 867 O OE2 . GLU A 1 132 ? 39.885 10.435 9.101 1.00 55.67 ? 132 GLU A OE2 1 ATOM 868 N N . ASP A 1 133 ? 34.302 8.732 11.405 1.00 48.55 ? 133 ASP A N 1 ATOM 869 C CA . ASP A 1 133 ? 32.844 8.697 11.352 1.00 50.61 ? 133 ASP A CA 1 ATOM 870 C C . ASP A 1 133 ? 32.275 8.150 12.662 1.00 49.10 ? 133 ASP A C 1 ATOM 871 O O . ASP A 1 133 ? 31.425 8.766 13.297 1.00 49.64 ? 133 ASP A O 1 ATOM 872 C CB . ASP A 1 133 ? 32.355 7.845 10.187 1.00 51.44 ? 133 ASP A CB 1 ATOM 873 C CG . ASP A 1 133 ? 32.629 8.419 8.818 1.00 52.69 ? 133 ASP A CG 1 ATOM 874 O OD1 . ASP A 1 133 ? 32.544 9.650 8.634 1.00 53.03 ? 133 ASP A OD1 1 ATOM 875 O OD2 . ASP A 1 133 ? 32.933 7.627 7.892 1.00 53.47 ? 133 ASP A OD2 1 ATOM 876 N N . VAL A 1 134 ? 32.758 6.981 13.056 1.00 45.78 ? 134 VAL A N 1 ATOM 877 C CA . VAL A 1 134 ? 32.313 6.324 14.274 1.00 44.85 ? 134 VAL A CA 1 ATOM 878 C C . VAL A 1 134 ? 32.340 7.245 15.482 1.00 48.29 ? 134 VAL A C 1 ATOM 879 O O . VAL A 1 134 ? 31.322 7.454 16.148 1.00 51.11 ? 134 VAL A O 1 ATOM 880 C CB . VAL A 1 134 ? 33.179 5.077 14.564 1.00 43.42 ? 134 VAL A CB 1 ATOM 881 C CG1 . VAL A 1 134 ? 32.871 4.510 15.936 1.00 42.56 ? 134 VAL A CG1 1 ATOM 882 C CG2 . VAL A 1 134 ? 32.959 4.031 13.479 1.00 43.13 ? 134 VAL A CG2 1 ATOM 883 N N . LYS A 1 135 ? 33.505 7.801 15.784 1.00 51.30 ? 135 LYS A N 1 ATOM 884 C CA . LYS A 1 135 ? 33.693 8.672 16.923 1.00 56.52 ? 135 LYS A CA 1 ATOM 885 C C . LYS A 1 135 ? 33.143 10.073 16.760 1.00 56.05 ? 135 LYS A C 1 ATOM 886 O O . LYS A 1 135 ? 32.580 10.619 17.724 1.00 58.03 ? 135 LYS A O 1 ATOM 887 C CB . LYS A 1 135 ? 35.194 8.733 17.283 1.00 56.68 ? 135 LYS A CB 1 ATOM 888 C CG . LYS A 1 135 ? 35.774 7.368 17.630 1.00 58.12 ? 135 LYS A CG 1 ATOM 889 C CD . LYS A 1 135 ? 37.294 7.392 17.630 1.00 59.84 ? 135 LYS A CD 1 ATOM 890 C CE . LYS A 1 135 ? 37.868 5.983 17.679 1.00 60.07 ? 135 LYS A CE 1 ATOM 891 N NZ . LYS A 1 135 ? 39.357 5.993 17.659 1.00 60.83 ? 135 LYS A NZ 1 ATOM 892 N N . LYS A 1 136 ? 33.283 10.686 15.592 1.00 57.53 ? 136 LYS A N 1 ATOM 893 C CA . LYS A 1 136 ? 32.813 12.039 15.372 1.00 58.10 ? 136 LYS A CA 1 ATOM 894 C C . LYS A 1 136 ? 31.343 12.163 15.026 1.00 57.17 ? 136 LYS A C 1 ATOM 895 O O . LYS A 1 136 ? 30.631 12.970 15.640 1.00 58.92 ? 136 LYS A O 1 ATOM 896 C CB . LYS A 1 136 ? 33.650 12.748 14.288 1.00 58.73 ? 136 LYS A CB 1 ATOM 897 C CG . LYS A 1 136 ? 33.222 14.199 14.094 1.00 60.31 ? 136 LYS A CG 1 ATOM 898 C CD . LYS A 1 136 ? 34.221 14.980 13.258 1.00 61.27 ? 136 LYS A CD 1 ATOM 899 C CE . LYS A 1 136 ? 33.766 16.418 13.065 1.00 62.55 ? 136 LYS A CE 1 ATOM 900 N NZ . LYS A 1 136 ? 34.706 17.195 12.207 1.00 63.25 ? 136 LYS A NZ 1 ATOM 901 N N . LEU A 1 137 ? 30.870 11.424 14.031 1.00 56.72 ? 137 LEU A N 1 ATOM 902 C CA . LEU A 1 137 ? 29.480 11.503 13.611 1.00 56.29 ? 137 LEU A CA 1 ATOM 903 C C . LEU A 1 137 ? 28.532 10.777 14.552 1.00 55.65 ? 137 LEU A C 1 ATOM 904 O O . LEU A 1 137 ? 27.574 11.369 15.054 1.00 59.48 ? 137 LEU A O 1 ATOM 905 C CB . LEU A 1 137 ? 29.317 10.954 12.188 1.00 56.60 ? 137 LEU A CB 1 ATOM 906 C CG . LEU A 1 137 ? 29.858 11.836 11.059 1.00 56.99 ? 137 LEU A CG 1 ATOM 907 C CD1 . LEU A 1 137 ? 29.539 11.222 9.703 1.00 57.07 ? 137 LEU A CD1 1 ATOM 908 C CD2 . LEU A 1 137 ? 29.293 13.244 11.163 1.00 56.35 ? 137 LEU A CD2 1 ATOM 909 N N . TYR A 1 138 ? 28.785 9.496 14.788 1.00 54.16 ? 138 TYR A N 1 ATOM 910 C CA . TYR A 1 138 ? 27.940 8.689 15.655 1.00 53.12 ? 138 TYR A CA 1 ATOM 911 C C . TYR A 1 138 ? 28.430 8.631 17.089 1.00 54.89 ? 138 TYR A C 1 ATOM 912 O O . TYR A 1 138 ? 27.901 7.871 17.908 1.00 54.18 ? 138 TYR A O 1 ATOM 913 C CB . TYR A 1 138 ? 27.809 7.272 15.074 1.00 50.29 ? 138 TYR A CB 1 ATOM 914 C CG . TYR A 1 138 ? 26.898 7.227 13.863 1.00 50.98 ? 138 TYR A CG 1 ATOM 915 C CD1 . TYR A 1 138 ? 27.336 7.651 12.618 1.00 49.38 ? 138 TYR A CD1 1 ATOM 916 C CD2 . TYR A 1 138 ? 25.596 6.760 13.977 1.00 50.96 ? 138 TYR A CD2 1 ATOM 917 C CE1 . TYR A 1 138 ? 26.500 7.611 11.517 1.00 48.54 ? 138 TYR A CE1 1 ATOM 918 C CE2 . TYR A 1 138 ? 24.755 6.715 12.882 1.00 49.66 ? 138 TYR A CE2 1 ATOM 919 C CZ . TYR A 1 138 ? 25.213 7.141 11.655 1.00 48.67 ? 138 TYR A CZ 1 ATOM 920 O OH . TYR A 1 138 ? 24.371 7.096 10.566 1.00 49.24 ? 138 TYR A OH 1 ATOM 921 N N . HIS A 1 139 ? 29.429 9.444 17.412 1.00 59.21 ? 139 HIS A N 1 ATOM 922 C CA . HIS A 1 139 ? 29.979 9.494 18.758 1.00 61.26 ? 139 HIS A CA 1 ATOM 923 C C . HIS A 1 139 ? 29.965 8.121 19.418 1.00 60.46 ? 139 HIS A C 1 ATOM 924 O O . HIS A 1 139 ? 29.424 7.954 20.509 1.00 62.32 ? 139 HIS A O 1 ATOM 925 C CB . HIS A 1 139 ? 29.200 10.493 19.620 1.00 62.47 ? 139 HIS A CB 1 ATOM 926 C CG . HIS A 1 139 ? 29.186 11.878 19.047 1.00 64.14 ? 139 HIS A CG 1 ATOM 927 N ND1 . HIS A 1 139 ? 28.489 12.197 17.902 1.00 65.35 ? 139 HIS A ND1 1 ATOM 928 C CD2 . HIS A 1 139 ? 29.781 13.021 19.458 1.00 64.75 ? 139 HIS A CD2 1 ATOM 929 C CE1 . HIS A 1 139 ? 28.655 13.480 17.631 1.00 65.30 ? 139 HIS A CE1 1 ATOM 930 N NE2 . HIS A 1 139 ? 29.435 14.003 18.560 1.00 64.93 ? 139 HIS A NE2 1 ATOM 931 N N . SER A 1 140 ? 30.563 7.149 18.741 1.00 56.97 ? 140 SER A N 1 ATOM 932 C CA . SER A 1 140 ? 30.633 5.787 19.264 1.00 54.49 ? 140 SER A CA 1 ATOM 933 C C . SER A 1 140 ? 32.078 5.470 19.643 1.00 52.22 ? 140 SER A C 1 ATOM 934 O O . SER A 1 140 ? 32.942 6.345 19.528 1.00 49.74 ? 140 SER A O 1 ATOM 935 C CB . SER A 1 140 ? 30.099 4.786 18.248 1.00 54.75 ? 140 SER A CB 1 ATOM 936 O OG . SER A 1 140 ? 29.511 3.674 18.905 1.00 56.62 ? 140 SER A OG 1 ATOM 937 N N . GLU A 1 141 ? 32.335 4.252 20.093 1.00 47.40 ? 141 GLU A N 1 ATOM 938 C CA . GLU A 1 141 ? 33.684 3.876 20.499 1.00 47.98 ? 141 GLU A CA 1 ATOM 939 C C . GLU A 1 141 ? 34.220 2.678 19.735 1.00 45.01 ? 141 GLU A C 1 ATOM 940 O O . GLU A 1 141 ? 33.543 1.675 19.535 1.00 45.61 ? 141 GLU A O 1 ATOM 941 C CB . GLU A 1 141 ? 33.706 3.621 22.011 1.00 48.36 ? 141 GLU A CB 1 ATOM 942 C CG . GLU A 1 141 ? 33.356 4.866 22.823 1.00 50.25 ? 141 GLU A CG 1 ATOM 943 C CD . GLU A 1 141 ? 33.129 4.557 24.289 1.00 51.15 ? 141 GLU A CD 1 ATOM 944 O OE1 . GLU A 1 141 ? 34.119 4.463 25.045 1.00 52.44 ? 141 GLU A OE1 1 ATOM 945 O OE2 . GLU A 1 141 ? 31.955 4.407 24.684 1.00 51.18 ? 141 GLU A OE2 1 ATOM 946 N N . ALA A 1 142 ? 35.469 2.794 19.295 1.00 42.18 ? 142 ALA A N 1 ATOM 947 C CA . ALA A 1 142 ? 36.141 1.725 18.563 1.00 37.01 ? 142 ALA A CA 1 ATOM 948 C C . ALA A 1 142 ? 37.436 1.379 19.307 1.00 40.48 ? 142 ALA A C 1 ATOM 949 O O . ALA A 1 142 ? 38.160 2.271 19.737 1.00 39.33 ? 142 ALA A O 1 ATOM 950 C CB . ALA A 1 142 ? 36.422 2.110 17.134 1.00 35.03 ? 142 ALA A CB 1 ATOM 951 N N . PHE A 1 143 ? 37.672 0.087 19.503 1.00 41.55 ? 143 PHE A N 1 ATOM 952 C CA . PHE A 1 143 ? 38.853 -0.353 20.225 1.00 40.55 ? 143 PHE A CA 1 ATOM 953 C C . PHE A 1 143 ? 39.573 -1.462 19.457 1.00 37.45 ? 143 PHE A C 1 ATOM 954 O O . PHE A 1 143 ? 38.962 -2.165 18.671 1.00 34.70 ? 143 PHE A O 1 ATOM 955 C CB . PHE A 1 143 ? 38.473 -0.895 21.611 1.00 39.42 ? 143 PHE A CB 1 ATOM 956 C CG . PHE A 1 143 ? 37.843 0.123 22.513 1.00 41.86 ? 143 PHE A CG 1 ATOM 957 C CD1 . PHE A 1 143 ? 38.627 1.020 23.218 1.00 39.74 ? 143 PHE A CD1 1 ATOM 958 C CD2 . PHE A 1 143 ? 36.463 0.181 22.660 1.00 42.03 ? 143 PHE A CD2 1 ATOM 959 C CE1 . PHE A 1 143 ? 38.052 1.957 24.052 1.00 42.72 ? 143 PHE A CE1 1 ATOM 960 C CE2 . PHE A 1 143 ? 35.886 1.117 23.494 1.00 42.66 ? 143 PHE A CE2 1 ATOM 961 C CZ . PHE A 1 143 ? 36.678 2.005 24.192 1.00 42.69 ? 143 PHE A CZ 1 ATOM 962 N N . THR A 1 144 ? 40.866 -1.597 19.734 1.00 34.47 ? 144 THR A N 1 ATOM 963 C CA . THR A 1 144 ? 41.628 -2.689 19.111 1.00 41.73 ? 144 THR A CA 1 ATOM 964 C C . THR A 1 144 ? 41.963 -3.704 20.199 1.00 38.82 ? 144 THR A C 1 ATOM 965 O O . THR A 1 144 ? 42.324 -3.303 21.313 1.00 41.71 ? 144 THR A O 1 ATOM 966 C CB . THR A 1 144 ? 42.882 -2.191 18.398 1.00 40.65 ? 144 THR A CB 1 ATOM 967 O OG1 . THR A 1 144 ? 43.527 -3.299 17.744 1.00 45.68 ? 144 THR A OG1 1 ATOM 968 C CG2 . THR A 1 144 ? 43.859 -1.558 19.371 1.00 42.03 ? 144 THR A CG2 1 ATOM 969 N N . VAL A 1 145 ? 41.752 -4.987 19.933 1.00 34.65 ? 145 VAL A N 1 ATOM 970 C CA . VAL A 1 145 ? 42.042 -6.012 20.927 1.00 37.80 ? 145 VAL A CA 1 ATOM 971 C C . VAL A 1 145 ? 42.718 -7.228 20.304 1.00 37.85 ? 145 VAL A C 1 ATOM 972 O O . VAL A 1 145 ? 42.684 -7.419 19.089 1.00 39.68 ? 145 VAL A O 1 ATOM 973 C CB . VAL A 1 145 ? 40.796 -6.484 21.694 1.00 37.05 ? 145 VAL A CB 1 ATOM 974 C CG1 . VAL A 1 145 ? 40.213 -5.351 22.523 1.00 37.87 ? 145 VAL A CG1 1 ATOM 975 C CG2 . VAL A 1 145 ? 39.759 -7.058 20.743 1.00 36.19 ? 145 VAL A CG2 1 ATOM 976 N N . ASN A 1 146 ? 43.324 -8.048 21.162 1.00 35.69 ? 146 ASN A N 1 ATOM 977 C CA . ASN A 1 146 ? 43.995 -9.255 20.680 1.00 37.85 ? 146 ASN A CA 1 ATOM 978 C C . ASN A 1 146 ? 43.037 -10.440 20.750 1.00 35.09 ? 146 ASN A C 1 ATOM 979 O O . ASN A 1 146 ? 42.885 -11.058 21.799 1.00 32.72 ? 146 ASN A O 1 ATOM 980 C CB . ASN A 1 146 ? 45.269 -9.542 21.459 1.00 38.11 ? 146 ASN A CB 1 ATOM 981 C CG . ASN A 1 146 ? 45.887 -10.885 21.110 1.00 39.29 ? 146 ASN A CG 1 ATOM 982 O OD1 . ASN A 1 146 ? 45.761 -11.379 19.992 1.00 38.85 ? 146 ASN A OD1 1 ATOM 983 N ND2 . ASN A 1 146 ? 46.560 -11.488 22.081 1.00 39.51 ? 146 ASN A ND2 1 ATOM 984 N N . PHE A 1 147 ? 42.388 -10.729 19.621 1.00 33.72 ? 147 PHE A N 1 ATOM 985 C CA . PHE A 1 147 ? 41.446 -11.843 19.574 1.00 33.75 ? 147 PHE A CA 1 ATOM 986 C C . PHE A 1 147 ? 42.168 -13.179 19.622 1.00 32.11 ? 147 PHE A C 1 ATOM 987 O O . PHE A 1 147 ? 41.534 -14.230 19.722 1.00 34.05 ? 147 PHE A O 1 ATOM 988 C CB . PHE A 1 147 ? 40.521 -11.735 18.367 1.00 34.37 ? 147 PHE A CB 1 ATOM 989 C CG . PHE A 1 147 ? 39.379 -10.774 18.588 1.00 32.80 ? 147 PHE A CG 1 ATOM 990 C CD1 . PHE A 1 147 ? 38.477 -10.987 19.617 1.00 33.03 ? 147 PHE A CD1 1 ATOM 991 C CD2 . PHE A 1 147 ? 39.216 -9.671 17.772 1.00 32.13 ? 147 PHE A CD2 1 ATOM 992 C CE1 . PHE A 1 147 ? 37.425 -10.110 19.830 1.00 30.68 ? 147 PHE A CE1 1 ATOM 993 C CE2 . PHE A 1 147 ? 38.167 -8.792 17.977 1.00 32.22 ? 147 PHE A CE2 1 ATOM 994 C CZ . PHE A 1 147 ? 37.275 -9.014 19.006 1.00 30.76 ? 147 PHE A CZ 1 ATOM 995 N N . GLY A 1 148 ? 43.498 -13.129 19.581 1.00 33.71 ? 148 GLY A N 1 ATOM 996 C CA . GLY A 1 148 ? 44.296 -14.364 19.663 1.00 31.47 ? 148 GLY A CA 1 ATOM 997 C C . GLY A 1 148 ? 44.063 -14.991 21.046 1.00 31.68 ? 148 GLY A C 1 ATOM 998 O O . GLY A 1 148 ? 44.178 -16.196 21.221 1.00 31.92 ? 148 GLY A O 1 ATOM 999 N N . ASP A 1 149 ? 43.729 -14.138 22.005 1.00 31.64 ? 149 ASP A N 1 ATOM 1000 C CA . ASP A 1 149 ? 43.428 -14.565 23.374 1.00 33.08 ? 149 ASP A CA 1 ATOM 1001 C C . ASP A 1 149 ? 41.934 -14.316 23.623 1.00 36.97 ? 149 ASP A C 1 ATOM 1002 O O . ASP A 1 149 ? 41.533 -13.254 24.093 1.00 32.47 ? 149 ASP A O 1 ATOM 1003 C CB . ASP A 1 149 ? 44.285 -13.805 24.375 1.00 34.39 ? 149 ASP A CB 1 ATOM 1004 C CG . ASP A 1 149 ? 44.140 -14.273 25.808 1.00 35.47 ? 149 ASP A CG 1 ATOM 1005 O OD1 . ASP A 1 149 ? 43.059 -14.777 26.177 1.00 33.81 ? 149 ASP A OD1 1 ATOM 1006 O OD2 . ASP A 1 149 ? 45.111 -14.138 26.590 1.00 34.98 ? 149 ASP A OD2 1 ATOM 1007 N N . THR A 1 150 ? 41.110 -15.288 23.264 1.00 40.18 ? 150 THR A N 1 ATOM 1008 C CA . THR A 1 150 ? 39.671 -15.195 23.381 1.00 43.62 ? 150 THR A CA 1 ATOM 1009 C C . THR A 1 150 ? 39.155 -14.782 24.743 1.00 43.20 ? 150 THR A C 1 ATOM 1010 O O . THR A 1 150 ? 38.316 -13.871 24.833 1.00 40.54 ? 150 THR A O 1 ATOM 1011 C CB . THR A 1 150 ? 38.981 -16.509 22.947 1.00 43.66 ? 150 THR A CB 1 ATOM 1012 O OG1 . THR A 1 150 ? 39.388 -16.844 21.617 1.00 45.03 ? 150 THR A OG1 1 ATOM 1013 C CG2 . THR A 1 150 ? 37.468 -16.334 22.960 1.00 45.43 ? 150 THR A CG2 1 ATOM 1014 N N . GLU A 1 151 ? 39.601 -15.436 25.809 1.00 42.72 ? 151 GLU A N 1 ATOM 1015 C CA . GLU A 1 151 ? 39.131 -15.105 27.150 1.00 46.05 ? 151 GLU A CA 1 ATOM 1016 C C . GLU A 1 151 ? 39.440 -13.667 27.529 1.00 40.65 ? 151 GLU A C 1 ATOM 1017 O O . GLU A 1 151 ? 38.594 -12.987 28.116 1.00 33.92 ? 151 GLU A O 1 ATOM 1018 C CB . GLU A 1 151 ? 39.690 -16.079 28.185 1.00 48.16 ? 151 GLU A CB 1 ATOM 1019 C CG . GLU A 1 151 ? 39.122 -17.488 28.063 1.00 52.12 ? 151 GLU A CG 1 ATOM 1020 C CD . GLU A 1 151 ? 37.707 -17.591 28.596 1.00 55.48 ? 151 GLU A CD 1 ATOM 1021 O OE1 . GLU A 1 151 ? 36.902 -18.364 28.033 1.00 55.84 ? 151 GLU A OE1 1 ATOM 1022 O OE2 . GLU A 1 151 ? 37.394 -16.895 29.585 1.00 57.70 ? 151 GLU A OE2 1 ATOM 1023 N N . GLU A 1 152 ? 40.639 -13.196 27.198 1.00 34.00 ? 152 GLU A N 1 ATOM 1024 C CA . GLU A 1 152 ? 41.014 -11.818 27.532 1.00 34.13 ? 152 GLU A CA 1 ATOM 1025 C C . GLU A 1 152 ? 40.203 -10.835 26.696 1.00 34.62 ? 152 GLU A C 1 ATOM 1026 O O . GLU A 1 152 ? 39.809 -9.773 27.184 1.00 32.61 ? 152 GLU A O 1 ATOM 1027 C CB . GLU A 1 152 ? 42.505 -11.601 27.373 1.00 32.52 ? 152 GLU A CB 1 ATOM 1028 C CG . GLU A 1 152 ? 43.037 -10.278 27.861 1.00 32.75 ? 152 GLU A CG 1 ATOM 1029 C CD . GLU A 1 152 ? 42.748 -9.990 29.320 1.00 33.54 ? 152 GLU A CD 1 ATOM 1030 O OE1 . GLU A 1 152 ? 42.485 -10.926 30.102 1.00 32.63 ? 152 GLU A OE1 1 ATOM 1031 O OE2 . GLU A 1 152 ? 42.784 -8.796 29.690 1.00 35.03 ? 152 GLU A OE2 1 ATOM 1032 N N . ALA A 1 153 ? 39.940 -11.202 25.441 1.00 28.39 ? 153 ALA A N 1 ATOM 1033 C CA . ALA A 1 153 ? 39.141 -10.347 24.565 1.00 30.89 ? 153 ALA A CA 1 ATOM 1034 C C . ALA A 1 153 ? 37.738 -10.169 25.163 1.00 27.35 ? 153 ALA A C 1 ATOM 1035 O O . ALA A 1 153 ? 37.200 -9.072 25.201 1.00 25.09 ? 153 ALA A O 1 ATOM 1036 C CB . ALA A 1 153 ? 39.024 -10.947 23.175 1.00 29.91 ? 153 ALA A CB 1 ATOM 1037 N N . LYS A 1 154 ? 37.174 -11.278 25.616 1.00 30.00 ? 154 LYS A N 1 ATOM 1038 C CA . LYS A 1 154 ? 35.846 -11.279 26.214 1.00 37.53 ? 154 LYS A CA 1 ATOM 1039 C C . LYS A 1 154 ? 35.820 -10.431 27.481 1.00 35.28 ? 154 LYS A C 1 ATOM 1040 O O . LYS A 1 154 ? 34.877 -9.680 27.722 1.00 35.30 ? 154 LYS A O 1 ATOM 1041 C CB . LYS A 1 154 ? 35.408 -12.713 26.524 1.00 37.70 ? 154 LYS A CB 1 ATOM 1042 C CG . LYS A 1 154 ? 33.992 -12.824 27.048 1.00 41.06 ? 154 LYS A CG 1 ATOM 1043 C CD . LYS A 1 154 ? 33.503 -14.261 27.062 1.00 42.27 ? 154 LYS A CD 1 ATOM 1044 C CE . LYS A 1 154 ? 34.139 -15.054 28.191 1.00 44.79 ? 154 LYS A CE 1 ATOM 1045 N NZ . LYS A 1 154 ? 33.318 -16.248 28.547 1.00 46.32 ? 154 LYS A NZ 1 ATOM 1046 N N . LYS A 1 155 ? 36.875 -10.545 28.282 1.00 35.47 ? 155 LYS A N 1 ATOM 1047 C CA . LYS A 1 155 ? 36.978 -9.775 29.516 1.00 38.69 ? 155 LYS A CA 1 ATOM 1048 C C . LYS A 1 155 ? 36.981 -8.278 29.230 1.00 38.93 ? 155 LYS A C 1 ATOM 1049 O O . LYS A 1 155 ? 36.260 -7.525 29.884 1.00 35.83 ? 155 LYS A O 1 ATOM 1050 C CB . LYS A 1 155 ? 38.228 -10.170 30.302 1.00 40.77 ? 155 LYS A CB 1 ATOM 1051 C CG . LYS A 1 155 ? 38.527 -9.274 31.490 1.00 41.90 ? 155 LYS A CG 1 ATOM 1052 C CD . LYS A 1 155 ? 39.283 -10.029 32.579 1.00 43.14 ? 155 LYS A CD 1 ATOM 1053 C CE . LYS A 1 155 ? 39.380 -9.184 33.843 1.00 41.96 ? 155 LYS A CE 1 ATOM 1054 N NZ . LYS A 1 155 ? 39.838 -7.797 33.533 1.00 41.10 ? 155 LYS A NZ 1 ATOM 1055 N N . GLN A 1 156 ? 37.788 -7.858 28.262 1.00 31.53 ? 156 GLN A N 1 ATOM 1056 C CA . GLN A 1 156 ? 37.890 -6.455 27.889 1.00 37.19 ? 156 GLN A CA 1 ATOM 1057 C C . GLN A 1 156 ? 36.554 -5.920 27.389 1.00 37.14 ? 156 GLN A C 1 ATOM 1058 O O . GLN A 1 156 ? 36.123 -4.832 27.772 1.00 39.56 ? 156 GLN A O 1 ATOM 1059 C CB . GLN A 1 156 ? 38.982 -6.252 26.831 1.00 38.84 ? 156 GLN A CB 1 ATOM 1060 C CG . GLN A 1 156 ? 40.381 -6.533 27.351 1.00 42.57 ? 156 GLN A CG 1 ATOM 1061 C CD . GLN A 1 156 ? 41.421 -6.693 26.269 1.00 43.78 ? 156 GLN A CD 1 ATOM 1062 O OE1 . GLN A 1 156 ? 41.307 -7.546 25.385 1.00 46.04 ? 156 GLN A OE1 1 ATOM 1063 N NE2 . GLN A 1 156 ? 42.465 -5.874 26.324 1.00 43.76 ? 156 GLN A NE2 1 ATOM 1064 N N . ILE A 1 157 ? 35.887 -6.695 26.548 1.00 31.30 ? 157 ILE A N 1 ATOM 1065 C CA . ILE A 1 157 ? 34.576 -6.326 26.030 1.00 32.82 ? 157 ILE A CA 1 ATOM 1066 C C . ILE A 1 157 ? 33.567 -6.189 27.169 1.00 32.44 ? 157 ILE A C 1 ATOM 1067 O O . ILE A 1 157 ? 32.867 -5.184 27.277 1.00 34.00 ? 157 ILE A O 1 ATOM 1068 C CB . ILE A 1 157 ? 34.069 -7.378 25.026 1.00 31.24 ? 157 ILE A CB 1 ATOM 1069 C CG1 . ILE A 1 157 ? 34.865 -7.301 23.722 1.00 31.30 ? 157 ILE A CG1 1 ATOM 1070 C CG2 . ILE A 1 157 ? 32.582 -7.202 24.770 1.00 32.17 ? 157 ILE A CG2 1 ATOM 1071 C CD1 . ILE A 1 157 ? 34.579 -8.437 22.761 1.00 29.52 ? 157 ILE A CD1 1 ATOM 1072 N N . ASN A 1 158 ? 33.493 -7.207 28.022 1.00 29.88 ? 158 ASN A N 1 ATOM 1073 C CA . ASN A 1 158 ? 32.567 -7.193 29.146 1.00 33.11 ? 158 ASN A CA 1 ATOM 1074 C C . ASN A 1 158 ? 32.895 -6.099 30.151 1.00 34.10 ? 158 ASN A C 1 ATOM 1075 O O . ASN A 1 158 ? 31.977 -5.492 30.710 1.00 31.31 ? 158 ASN A O 1 ATOM 1076 C CB . ASN A 1 158 ? 32.498 -8.561 29.823 1.00 32.28 ? 158 ASN A CB 1 ATOM 1077 C CG . ASN A 1 158 ? 31.842 -9.599 28.925 1.00 33.78 ? 158 ASN A CG 1 ATOM 1078 O OD1 . ASN A 1 158 ? 31.157 -9.245 27.960 1.00 34.43 ? 158 ASN A OD1 1 ATOM 1079 N ND2 . ASN A 1 158 ? 32.042 -10.870 29.233 1.00 30.70 ? 158 ASN A ND2 1 ATOM 1080 N N . ASP A 1 159 ? 34.174 -5.829 30.379 1.00 33.60 ? 159 ASP A N 1 ATOM 1081 C CA . ASP A 1 159 ? 34.579 -4.781 31.305 1.00 37.20 ? 159 ASP A CA 1 ATOM 1082 C C . ASP A 1 159 ? 34.123 -3.412 30.787 1.00 38.74 ? 159 ASP A C 1 ATOM 1083 O O . ASP A 1 159 ? 33.796 -2.525 31.574 1.00 36.32 ? 159 ASP A O 1 ATOM 1084 C CB . ASP A 1 159 ? 36.090 -4.776 31.522 1.00 37.82 ? 159 ASP A CB 1 ATOM 1085 C CG . ASP A 1 159 ? 36.563 -5.948 32.363 1.00 37.88 ? 159 ASP A CG 1 ATOM 1086 O OD1 . ASP A 1 159 ? 35.717 -6.605 33.000 1.00 36.61 ? 159 ASP A OD1 1 ATOM 1087 O OD2 . ASP A 1 159 ? 37.786 -6.207 32.381 1.00 39.17 ? 159 ASP A OD2 1 ATOM 1088 N N . TYR A 1 160 ? 34.118 -3.279 29.470 1.00 36.52 ? 160 TYR A N 1 ATOM 1089 C CA . TYR A 1 160 ? 33.709 -2.062 28.788 1.00 36.80 ? 160 TYR A CA 1 ATOM 1090 C C . TYR A 1 160 ? 32.236 -1.765 29.075 1.00 39.65 ? 160 TYR A C 1 ATOM 1091 O O . TYR A 1 160 ? 31.864 -0.659 29.452 1.00 40.37 ? 160 TYR A O 1 ATOM 1092 C CB . TYR A 1 160 ? 33.911 -2.211 27.272 1.00 36.95 ? 160 TYR A CB 1 ATOM 1093 C CG . TYR A 1 160 ? 33.086 -1.239 26.456 1.00 35.99 ? 160 TYR A CG 1 ATOM 1094 C CD1 . TYR A 1 160 ? 33.450 0.100 26.359 1.00 37.37 ? 160 TYR A CD1 1 ATOM 1095 C CD2 . TYR A 1 160 ? 31.948 -1.660 25.787 1.00 37.80 ? 160 TYR A CD2 1 ATOM 1096 C CE1 . TYR A 1 160 ? 32.696 0.989 25.612 1.00 37.02 ? 160 TYR A CE1 1 ATOM 1097 C CE2 . TYR A 1 160 ? 31.185 -0.780 25.040 1.00 36.96 ? 160 TYR A CE2 1 ATOM 1098 C CZ . TYR A 1 160 ? 31.566 0.544 24.960 1.00 40.45 ? 160 TYR A CZ 1 ATOM 1099 O OH . TYR A 1 160 ? 30.805 1.414 24.213 1.00 40.97 ? 160 TYR A OH 1 ATOM 1100 N N . VAL A 1 161 ? 31.411 -2.796 28.914 1.00 35.91 ? 161 VAL A N 1 ATOM 1101 C CA . VAL A 1 161 ? 29.983 -2.659 29.179 1.00 36.19 ? 161 VAL A CA 1 ATOM 1102 C C . VAL A 1 161 ? 29.762 -2.366 30.665 1.00 39.90 ? 161 VAL A C 1 ATOM 1103 O O . VAL A 1 161 ? 29.127 -1.367 30.990 1.00 42.31 ? 161 VAL A O 1 ATOM 1104 C CB . VAL A 1 161 ? 29.187 -3.894 28.755 1.00 35.34 ? 161 VAL A CB 1 ATOM 1105 C CG1 . VAL A 1 161 ? 27.699 -3.714 29.029 1.00 34.89 ? 161 VAL A CG1 1 ATOM 1106 C CG2 . VAL A 1 161 ? 29.416 -4.190 27.273 1.00 35.93 ? 161 VAL A CG2 1 ATOM 1107 N N . GLU A 1 162 ? 30.307 -3.205 31.538 1.00 44.18 ? 162 GLU A N 1 ATOM 1108 C CA . GLU A 1 162 ? 30.163 -3.036 32.976 1.00 45.87 ? 162 GLU A CA 1 ATOM 1109 C C . GLU A 1 162 ? 30.490 -1.608 33.401 1.00 44.53 ? 162 GLU A C 1 ATOM 1110 O O . GLU A 1 162 ? 29.706 -0.966 34.100 1.00 46.99 ? 162 GLU A O 1 ATOM 1111 C CB . GLU A 1 162 ? 31.027 -4.031 33.755 1.00 47.99 ? 162 GLU A CB 1 ATOM 1112 C CG . GLU A 1 162 ? 30.700 -4.091 35.240 1.00 50.96 ? 162 GLU A CG 1 ATOM 1113 C CD . GLU A 1 162 ? 31.544 -5.073 36.020 1.00 53.30 ? 162 GLU A CD 1 ATOM 1114 O OE1 . GLU A 1 162 ? 31.597 -6.266 35.647 1.00 53.92 ? 162 GLU A OE1 1 ATOM 1115 O OE2 . GLU A 1 162 ? 32.167 -4.666 37.029 1.00 54.26 ? 162 GLU A OE2 1 ATOM 1116 N N . LYS A 1 163 ? 31.637 -1.113 32.971 1.00 37.70 ? 163 LYS A N 1 ATOM 1117 C CA . LYS A 1 163 ? 32.087 0.228 33.276 1.00 47.96 ? 163 LYS A CA 1 ATOM 1118 C C . LYS A 1 163 ? 31.132 1.287 32.733 1.00 47.89 ? 163 LYS A C 1 ATOM 1119 O O . LYS A 1 163 ? 30.890 2.299 33.387 1.00 46.56 ? 163 LYS A O 1 ATOM 1120 C CB . LYS A 1 163 ? 33.492 0.466 32.711 1.00 47.67 ? 163 LYS A CB 1 ATOM 1121 C CG . LYS A 1 163 ? 33.956 1.913 32.781 1.00 50.47 ? 163 LYS A CG 1 ATOM 1122 C CD . LYS A 1 163 ? 35.096 2.164 31.807 1.00 52.25 ? 163 LYS A CD 1 ATOM 1123 C CE . LYS A 1 163 ? 35.885 3.407 32.171 1.00 53.42 ? 163 LYS A CE 1 ATOM 1124 N NZ . LYS A 1 163 ? 37.233 3.407 31.536 1.00 54.87 ? 163 LYS A NZ 1 ATOM 1125 N N . GLY A 1 164 ? 30.591 1.063 31.543 1.00 53.36 ? 164 GLY A N 1 ATOM 1126 C CA . GLY A 1 164 ? 29.681 2.014 30.922 1.00 48.26 ? 164 GLY A CA 1 ATOM 1127 C C . GLY A 1 164 ? 28.329 2.071 31.608 1.00 45.95 ? 164 GLY A C 1 ATOM 1128 O O . GLY A 1 164 ? 27.631 3.090 31.523 1.00 45.26 ? 164 GLY A O 1 ATOM 1129 N N . THR A 1 165 ? 27.940 0.985 32.271 1.00 41.11 ? 165 THR A N 1 ATOM 1130 C CA . THR A 1 165 ? 26.656 0.937 32.959 1.00 43.04 ? 165 THR A CA 1 ATOM 1131 C C . THR A 1 165 ? 26.858 0.995 34.476 1.00 41.07 ? 165 THR A C 1 ATOM 1132 O O . THR A 1 165 ? 25.971 0.661 35.246 1.00 38.15 ? 165 THR A O 1 ATOM 1133 C CB . THR A 1 165 ? 25.857 -0.326 32.604 1.00 43.10 ? 165 THR A CB 1 ATOM 1134 O OG1 . THR A 1 165 ? 26.553 -1.477 33.093 1.00 43.85 ? 165 THR A OG1 1 ATOM 1135 C CG2 . THR A 1 165 ? 25.685 -0.449 31.095 1.00 42.86 ? 165 THR A CG2 1 ATOM 1136 N N . GLN A 1 166 ? 28.055 1.400 34.884 1.00 43.00 ? 166 GLN A N 1 ATOM 1137 C CA . GLN A 1 166 ? 28.403 1.494 36.286 1.00 51.34 ? 166 GLN A CA 1 ATOM 1138 C C . GLN A 1 166 ? 28.024 0.238 37.059 1.00 51.04 ? 166 GLN A C 1 ATOM 1139 O O . GLN A 1 166 ? 27.590 0.345 38.208 1.00 49.60 ? 166 GLN A O 1 ATOM 1140 C CB . GLN A 1 166 ? 27.731 2.709 36.941 1.00 52.78 ? 166 GLN A CB 1 ATOM 1141 C CG . GLN A 1 166 ? 28.144 4.041 36.333 1.00 54.88 ? 166 GLN A CG 1 ATOM 1142 C CD . GLN A 1 166 ? 29.635 4.289 36.456 1.00 56.62 ? 166 GLN A CD 1 ATOM 1143 O OE1 . GLN A 1 166 ? 30.069 5.368 36.862 1.00 57.32 ? 166 GLN A OE1 1 ATOM 1144 N NE2 . GLN A 1 166 ? 30.429 3.283 36.104 1.00 56.46 ? 166 GLN A NE2 1 ATOM 1145 N N . GLY A 1 167 ? 28.166 -0.931 36.449 1.00 42.35 ? 167 GLY A N 1 ATOM 1146 C CA . GLY A 1 167 ? 27.867 -2.182 37.101 1.00 40.69 ? 167 GLY A CA 1 ATOM 1147 C C . GLY A 1 167 ? 26.493 -2.753 36.903 1.00 36.85 ? 167 GLY A C 1 ATOM 1148 O O . GLY A 1 167 ? 26.174 -3.787 37.525 1.00 38.49 ? 167 GLY A O 1 ATOM 1149 N N . LYS A 1 168 ? 25.652 -2.165 36.057 1.00 42.54 ? 168 LYS A N 1 ATOM 1150 C CA . LYS A 1 168 ? 24.302 -2.706 35.862 1.00 42.93 ? 168 LYS A CA 1 ATOM 1151 C C . LYS A 1 168 ? 24.290 -3.873 34.890 1.00 40.12 ? 168 LYS A C 1 ATOM 1152 O O . LYS A 1 168 ? 23.467 -4.787 35.009 1.00 35.27 ? 168 LYS A O 1 ATOM 1153 C CB . LYS A 1 168 ? 23.321 -1.623 35.433 1.00 46.24 ? 168 LYS A CB 1 ATOM 1154 C CG . LYS A 1 168 ? 21.861 -2.065 35.458 1.00 51.49 ? 168 LYS A CG 1 ATOM 1155 C CD . LYS A 1 168 ? 21.431 -2.495 36.850 1.00 55.11 ? 168 LYS A CD 1 ATOM 1156 C CE . LYS A 1 168 ? 19.917 -2.526 36.991 1.00 57.29 ? 168 LYS A CE 1 ATOM 1157 N NZ . LYS A 1 168 ? 19.318 -3.710 36.310 1.00 57.74 ? 168 LYS A NZ 1 ATOM 1158 N N . ILE A 1 169 ? 25.200 -3.861 33.925 1.00 41.06 ? 169 ILE A N 1 ATOM 1159 C CA . ILE A 1 169 ? 25.291 -4.946 32.945 1.00 37.28 ? 169 ILE A CA 1 ATOM 1160 C C . ILE A 1 169 ? 26.658 -5.617 33.053 1.00 36.96 ? 169 ILE A C 1 ATOM 1161 O O . ILE A 1 169 ? 27.668 -5.014 32.681 1.00 33.81 ? 169 ILE A O 1 ATOM 1162 C CB . ILE A 1 169 ? 25.090 -4.428 31.511 1.00 38.45 ? 169 ILE A CB 1 ATOM 1163 C CG1 . ILE A 1 169 ? 23.670 -3.890 31.316 1.00 37.18 ? 169 ILE A CG1 1 ATOM 1164 C CG2 . ILE A 1 169 ? 25.374 -5.537 30.503 1.00 37.23 ? 169 ILE A CG2 1 ATOM 1165 C CD1 . ILE A 1 169 ? 23.472 -3.178 29.992 1.00 37.57 ? 169 ILE A CD1 1 ATOM 1166 N N . VAL A 1 170 ? 26.703 -6.834 33.578 1.00 37.43 ? 170 VAL A N 1 ATOM 1167 C CA . VAL A 1 170 ? 27.964 -7.545 33.735 1.00 39.90 ? 170 VAL A CA 1 ATOM 1168 C C . VAL A 1 170 ? 27.992 -8.850 32.944 1.00 39.49 ? 170 VAL A C 1 ATOM 1169 O O . VAL A 1 170 ? 26.966 -9.477 32.707 1.00 34.41 ? 170 VAL A O 1 ATOM 1170 C CB . VAL A 1 170 ? 28.252 -7.877 35.214 1.00 40.31 ? 170 VAL A CB 1 ATOM 1171 C CG1 . VAL A 1 170 ? 28.491 -6.616 36.024 1.00 41.99 ? 170 VAL A CG1 1 ATOM 1172 C CG2 . VAL A 1 170 ? 27.102 -8.689 35.797 1.00 39.69 ? 170 VAL A CG2 1 ATOM 1173 N N . ASP A 1 171 ? 29.194 -9.264 32.559 1.00 44.40 ? 171 ASP A N 1 ATOM 1174 C CA . ASP A 1 171 ? 29.375 -10.504 31.811 1.00 47.09 ? 171 ASP A CA 1 ATOM 1175 C C . ASP A 1 171 ? 28.351 -10.632 30.690 1.00 44.18 ? 171 ASP A C 1 ATOM 1176 O O . ASP A 1 171 ? 27.639 -11.632 30.599 1.00 47.39 ? 171 ASP A O 1 ATOM 1177 C CB . ASP A 1 171 ? 29.276 -11.698 32.763 1.00 49.66 ? 171 ASP A CB 1 ATOM 1178 C CG . ASP A 1 171 ? 30.174 -12.852 32.370 1.00 51.83 ? 171 ASP A CG 1 ATOM 1179 O OD1 . ASP A 1 171 ? 31.331 -12.608 31.961 1.00 53.32 ? 171 ASP A OD1 1 ATOM 1180 O OD2 . ASP A 1 171 ? 29.730 -14.016 32.470 1.00 52.46 ? 171 ASP A OD2 1 ATOM 1181 N N . LEU A 1 172 ? 28.273 -9.619 29.833 1.00 37.33 ? 172 LEU A N 1 ATOM 1182 C CA . LEU A 1 172 ? 27.337 -9.616 28.718 1.00 34.45 ? 172 LEU A CA 1 ATOM 1183 C C . LEU A 1 172 ? 27.650 -10.729 27.722 1.00 34.32 ? 172 LEU A C 1 ATOM 1184 O O . LEU A 1 172 ? 26.833 -11.625 27.508 1.00 34.71 ? 172 LEU A O 1 ATOM 1185 C CB . LEU A 1 172 ? 27.365 -8.264 28.000 1.00 35.04 ? 172 LEU A CB 1 ATOM 1186 C CG . LEU A 1 172 ? 26.482 -8.143 26.754 1.00 35.77 ? 172 LEU A CG 1 ATOM 1187 C CD1 . LEU A 1 172 ? 25.011 -8.291 27.113 1.00 35.64 ? 172 LEU A CD1 1 ATOM 1188 C CD2 . LEU A 1 172 ? 26.732 -6.825 26.043 1.00 36.04 ? 172 LEU A CD2 1 ATOM 1189 N N . VAL A 1 173 ? 28.833 -10.667 27.115 1.00 34.78 ? 173 VAL A N 1 ATOM 1190 C CA . VAL A 1 173 ? 29.227 -11.690 26.140 1.00 32.50 ? 173 VAL A CA 1 ATOM 1191 C C . VAL A 1 173 ? 29.658 -12.962 26.860 1.00 34.96 ? 173 VAL A C 1 ATOM 1192 O O . VAL A 1 173 ? 30.607 -12.928 27.643 1.00 39.81 ? 173 VAL A O 1 ATOM 1193 C CB . VAL A 1 173 ? 30.380 -11.213 25.246 1.00 33.72 ? 173 VAL A CB 1 ATOM 1194 C CG1 . VAL A 1 173 ? 30.757 -12.298 24.233 1.00 32.89 ? 173 VAL A CG1 1 ATOM 1195 C CG2 . VAL A 1 173 ? 30.020 -9.921 24.535 1.00 32.34 ? 173 VAL A CG2 1 ATOM 1196 N N . LYS A 1 174 ? 28.982 -14.070 26.583 1.00 43.36 ? 174 LYS A N 1 ATOM 1197 C CA . LYS A 1 174 ? 29.302 -15.339 27.220 1.00 45.04 ? 174 LYS A CA 1 ATOM 1198 C C . LYS A 1 174 ? 30.329 -16.140 26.435 1.00 47.82 ? 174 LYS A C 1 ATOM 1199 O O . LYS A 1 174 ? 30.984 -17.025 26.999 1.00 46.27 ? 174 LYS A O 1 ATOM 1200 C CB . LYS A 1 174 ? 28.033 -16.164 27.443 1.00 45.95 ? 174 LYS A CB 1 ATOM 1201 C CG . LYS A 1 174 ? 27.053 -15.524 28.420 1.00 47.57 ? 174 LYS A CG 1 ATOM 1202 C CD . LYS A 1 174 ? 27.700 -15.338 29.787 1.00 47.73 ? 174 LYS A CD 1 ATOM 1203 C CE . LYS A 1 174 ? 26.711 -14.797 30.804 1.00 48.85 ? 174 LYS A CE 1 ATOM 1204 N NZ . LYS A 1 174 ? 26.059 -13.542 30.339 1.00 48.28 ? 174 LYS A NZ 1 ATOM 1205 N N . GLU A 1 175 ? 30.481 -15.850 25.144 1.00 50.90 ? 175 GLU A N 1 ATOM 1206 C CA . GLU A 1 175 ? 31.458 -16.583 24.340 1.00 55.31 ? 175 GLU A CA 1 ATOM 1207 C C . GLU A 1 175 ? 31.729 -15.925 23.000 1.00 52.99 ? 175 GLU A C 1 ATOM 1208 O O . GLU A 1 175 ? 30.957 -15.098 22.519 1.00 56.23 ? 175 GLU A O 1 ATOM 1209 C CB . GLU A 1 175 ? 31.036 -18.038 24.179 1.00 57.90 ? 175 GLU A CB 1 ATOM 1210 C CG . GLU A 1 175 ? 29.652 -18.262 23.619 1.00 60.55 ? 175 GLU A CG 1 ATOM 1211 C CD . GLU A 1 175 ? 29.302 -19.727 23.461 1.00 64.86 ? 175 GLU A CD 1 ATOM 1212 O OE1 . GLU A 1 175 ? 29.534 -20.510 24.409 1.00 66.17 ? 175 GLU A OE1 1 ATOM 1213 O OE2 . GLU A 1 175 ? 28.790 -20.112 22.386 1.00 66.54 ? 175 GLU A OE2 1 ATOM 1214 N N . LEU A 1 176 ? 32.856 -16.289 22.392 1.00 49.52 ? 176 LEU A N 1 ATOM 1215 C CA . LEU A 1 176 ? 33.266 -15.748 21.109 1.00 46.23 ? 176 LEU A CA 1 ATOM 1216 C C . LEU A 1 176 ? 33.616 -16.864 20.124 1.00 50.35 ? 176 LEU A C 1 ATOM 1217 O O . LEU A 1 176 ? 34.045 -17.942 20.532 1.00 47.40 ? 176 LEU A O 1 ATOM 1218 C CB . LEU A 1 176 ? 34.487 -14.836 21.273 1.00 45.28 ? 176 LEU A CB 1 ATOM 1219 C CG . LEU A 1 176 ? 34.262 -13.515 22.010 1.00 44.03 ? 176 LEU A CG 1 ATOM 1220 C CD1 . LEU A 1 176 ? 35.558 -12.721 22.094 1.00 42.58 ? 176 LEU A CD1 1 ATOM 1221 C CD2 . LEU A 1 176 ? 33.176 -12.702 21.321 1.00 41.94 ? 176 LEU A CD2 1 ATOM 1222 N N . ASP A 1 177 ? 33.411 -16.590 18.840 1.00 48.89 ? 177 ASP A N 1 ATOM 1223 C CA . ASP A 1 177 ? 33.742 -17.579 17.807 1.00 54.24 ? 177 ASP A CA 1 ATOM 1224 C C . ASP A 1 177 ? 35.272 -17.699 17.758 1.00 54.18 ? 177 ASP A C 1 ATOM 1225 O O . ASP A 1 177 ? 35.967 -16.749 18.136 1.00 41.79 ? 177 ASP A O 1 ATOM 1226 C CB . ASP A 1 177 ? 33.184 -17.186 16.455 1.00 54.72 ? 177 ASP A CB 1 ATOM 1227 C CG . ASP A 1 177 ? 31.710 -17.435 16.249 1.00 57.88 ? 177 ASP A CG 1 ATOM 1228 O OD1 . ASP A 1 177 ? 31.202 -18.511 16.641 1.00 59.06 ? 177 ASP A OD1 1 ATOM 1229 O OD2 . ASP A 1 177 ? 31.019 -16.557 15.679 1.00 57.30 ? 177 ASP A OD2 1 ATOM 1230 N N . ARG A 1 178 ? 35.765 -18.845 17.324 1.00 52.36 ? 178 ARG A N 1 ATOM 1231 C CA . ARG A 1 178 ? 37.200 -19.078 17.249 1.00 54.97 ? 178 ARG A CA 1 ATOM 1232 C C . ARG A 1 178 ? 37.900 -18.056 16.367 1.00 47.57 ? 178 ARG A C 1 ATOM 1233 O O . ARG A 1 178 ? 39.001 -17.597 16.676 1.00 52.44 ? 178 ARG A O 1 ATOM 1234 C CB . ARG A 1 178 ? 37.469 -20.484 16.678 1.00 57.98 ? 178 ARG A CB 1 ATOM 1235 C CG . ARG A 1 178 ? 38.931 -20.727 16.323 1.00 60.24 ? 178 ARG A CG 1 ATOM 1236 C CD . ARG A 1 178 ? 39.695 -21.306 17.498 1.00 62.37 ? 178 ARG A CD 1 ATOM 1237 N NE . ARG A 1 178 ? 41.030 -21.771 17.137 1.00 62.53 ? 178 ARG A NE 1 ATOM 1238 C CZ . ARG A 1 178 ? 41.806 -22.477 17.958 1.00 63.32 ? 178 ARG A CZ 1 ATOM 1239 N NH1 . ARG A 1 178 ? 41.369 -22.792 19.173 1.00 65.08 ? 178 ARG A NH1 1 ATOM 1240 N NH2 . ARG A 1 178 ? 43.009 -22.869 17.573 1.00 62.92 ? 178 ARG A NH2 1 ATOM 1241 N N . ASP A 1 179 ? 37.267 -17.708 15.253 1.00 45.04 ? 179 ASP A N 1 ATOM 1242 C CA . ASP A 1 179 ? 37.870 -16.799 14.288 1.00 43.71 ? 179 ASP A CA 1 ATOM 1243 C C . ASP A 1 179 ? 37.366 -15.376 14.394 1.00 39.99 ? 179 ASP A C 1 ATOM 1244 O O . ASP A 1 179 ? 37.397 -14.622 13.415 1.00 38.54 ? 179 ASP A O 1 ATOM 1245 C CB . ASP A 1 179 ? 37.670 -17.350 12.878 1.00 46.95 ? 179 ASP A CB 1 ATOM 1246 C CG . ASP A 1 179 ? 36.249 -17.232 12.368 1.00 51.55 ? 179 ASP A CG 1 ATOM 1247 O OD1 . ASP A 1 179 ? 35.292 -17.325 13.169 1.00 52.52 ? 179 ASP A OD1 1 ATOM 1248 O OD2 . ASP A 1 179 ? 36.092 -17.043 11.138 1.00 52.78 ? 179 ASP A OD2 1 ATOM 1249 N N . THR A 1 180 ? 36.924 -14.977 15.582 1.00 38.17 ? 180 THR A N 1 ATOM 1250 C CA . THR A 1 180 ? 36.425 -13.624 15.785 1.00 34.16 ? 180 THR A CA 1 ATOM 1251 C C . THR A 1 180 ? 37.508 -12.589 15.509 1.00 31.64 ? 180 THR A C 1 ATOM 1252 O O . THR A 1 180 ? 38.580 -12.626 16.115 1.00 32.76 ? 180 THR A O 1 ATOM 1253 C CB . THR A 1 180 ? 35.926 -13.411 17.232 1.00 35.17 ? 180 THR A CB 1 ATOM 1254 O OG1 . THR A 1 180 ? 34.994 -14.431 17.581 1.00 36.54 ? 180 THR A OG1 1 ATOM 1255 C CG2 . THR A 1 180 ? 35.283 -12.041 17.353 1.00 34.09 ? 180 THR A CG2 1 ATOM 1256 N N . VAL A 1 181 ? 37.213 -11.647 14.629 1.00 28.09 ? 181 VAL A N 1 ATOM 1257 C CA . VAL A 1 181 ? 38.129 -10.573 14.300 1.00 29.30 ? 181 VAL A CA 1 ATOM 1258 C C . VAL A 1 181 ? 37.461 -9.212 14.475 1.00 27.22 ? 181 VAL A C 1 ATOM 1259 O O . VAL A 1 181 ? 38.135 -8.187 14.472 1.00 27.71 ? 181 VAL A O 1 ATOM 1260 C CB . VAL A 1 181 ? 38.668 -10.688 12.863 1.00 32.14 ? 181 VAL A CB 1 ATOM 1261 C CG1 . VAL A 1 181 ? 39.535 -11.933 12.716 1.00 32.25 ? 181 VAL A CG1 1 ATOM 1262 C CG2 . VAL A 1 181 ? 37.530 -10.718 11.854 1.00 33.82 ? 181 VAL A CG2 1 ATOM 1263 N N . PHE A 1 182 ? 36.141 -9.220 14.612 1.00 30.85 ? 182 PHE A N 1 ATOM 1264 C CA . PHE A 1 182 ? 35.368 -7.978 14.749 1.00 27.34 ? 182 PHE A CA 1 ATOM 1265 C C . PHE A 1 182 ? 34.094 -8.223 15.538 1.00 30.14 ? 182 PHE A C 1 ATOM 1266 O O . PHE A 1 182 ? 33.285 -9.086 15.183 1.00 28.85 ? 182 PHE A O 1 ATOM 1267 C CB . PHE A 1 182 ? 35.081 -7.458 13.343 1.00 28.92 ? 182 PHE A CB 1 ATOM 1268 C CG . PHE A 1 182 ? 34.295 -6.196 13.212 1.00 28.51 ? 182 PHE A CG 1 ATOM 1269 C CD1 . PHE A 1 182 ? 34.272 -5.249 14.222 1.00 27.59 ? 182 PHE A CD1 1 ATOM 1270 C CD2 . PHE A 1 182 ? 33.578 -5.934 12.051 1.00 28.27 ? 182 PHE A CD2 1 ATOM 1271 C CE1 . PHE A 1 182 ? 33.547 -4.081 14.087 1.00 29.21 ? 182 PHE A CE1 1 ATOM 1272 C CE2 . PHE A 1 182 ? 32.850 -4.770 11.908 1.00 27.07 ? 182 PHE A CE2 1 ATOM 1273 C CZ . PHE A 1 182 ? 32.833 -3.840 12.930 1.00 28.41 ? 182 PHE A CZ 1 ATOM 1274 N N . ALA A 1 183 ? 33.896 -7.480 16.632 1.00 32.40 ? 183 ALA A N 1 ATOM 1275 C CA . ALA A 1 183 ? 32.709 -7.652 17.463 1.00 28.46 ? 183 ALA A CA 1 ATOM 1276 C C . ALA A 1 183 ? 32.033 -6.332 17.808 1.00 28.71 ? 183 ALA A C 1 ATOM 1277 O O . ALA A 1 183 ? 32.683 -5.306 17.991 1.00 28.00 ? 183 ALA A O 1 ATOM 1278 C CB . ALA A 1 183 ? 33.067 -8.398 18.746 1.00 29.36 ? 183 ALA A CB 1 ATOM 1279 N N . LEU A 1 184 ? 30.705 -6.368 17.899 1.00 30.75 ? 184 LEU A N 1 ATOM 1280 C CA . LEU A 1 184 ? 29.926 -5.177 18.220 1.00 29.47 ? 184 LEU A CA 1 ATOM 1281 C C . LEU A 1 184 ? 29.062 -5.395 19.457 1.00 32.32 ? 184 LEU A C 1 ATOM 1282 O O . LEU A 1 184 ? 28.378 -6.409 19.593 1.00 23.89 ? 184 LEU A O 1 ATOM 1283 C CB . LEU A 1 184 ? 29.045 -4.772 17.038 1.00 32.23 ? 184 LEU A CB 1 ATOM 1284 C CG . LEU A 1 184 ? 28.159 -3.541 17.213 1.00 32.39 ? 184 LEU A CG 1 ATOM 1285 C CD1 . LEU A 1 184 ? 27.705 -3.008 15.859 1.00 33.57 ? 184 LEU A CD1 1 ATOM 1286 C CD2 . LEU A 1 184 ? 26.940 -3.873 18.070 1.00 34.70 ? 184 LEU A CD2 1 ATOM 1287 N N . VAL A 1 185 ? 29.106 -4.419 20.363 1.00 31.28 ? 185 VAL A N 1 ATOM 1288 C CA . VAL A 1 185 ? 28.302 -4.507 21.583 1.00 35.34 ? 185 VAL A CA 1 ATOM 1289 C C . VAL A 1 185 ? 27.439 -3.251 21.698 1.00 32.57 ? 185 VAL A C 1 ATOM 1290 O O . VAL A 1 185 ? 27.931 -2.134 21.573 1.00 33.11 ? 185 VAL A O 1 ATOM 1291 C CB . VAL A 1 185 ? 29.133 -4.724 22.844 1.00 35.56 ? 185 VAL A CB 1 ATOM 1292 C CG1 . VAL A 1 185 ? 28.337 -4.350 24.087 1.00 39.52 ? 185 VAL A CG1 1 ATOM 1293 C CG2 . VAL A 1 185 ? 29.572 -6.187 22.939 1.00 37.27 ? 185 VAL A CG2 1 ATOM 1294 N N . ASN A 1 186 ? 26.146 -3.470 21.886 1.00 31.93 ? 186 ASN A N 1 ATOM 1295 C CA . ASN A 1 186 ? 25.199 -2.346 21.980 1.00 28.82 ? 186 ASN A CA 1 ATOM 1296 C C . ASN A 1 186 ? 24.377 -2.487 23.250 1.00 22.02 ? 186 ASN A C 1 ATOM 1297 O O . ASN A 1 186 ? 23.624 -3.445 23.409 1.00 25.15 ? 186 ASN A O 1 ATOM 1298 C CB . ASN A 1 186 ? 24.329 -2.354 20.732 1.00 31.22 ? 186 ASN A CB 1 ATOM 1299 C CG . ASN A 1 186 ? 23.399 -1.164 20.624 1.00 33.01 ? 186 ASN A CG 1 ATOM 1300 O OD1 . ASN A 1 186 ? 22.252 -1.255 21.069 1.00 30.96 ? 186 ASN A OD1 1 ATOM 1301 N ND2 . ASN A 1 186 ? 23.898 -0.091 20.037 1.00 30.35 ? 186 ASN A ND2 1 ATOM 1302 N N . TYR A 1 187 ? 24.552 -1.528 24.168 1.00 27.52 ? 187 TYR A N 1 ATOM 1303 C CA . TYR A 1 187 ? 23.832 -1.586 25.432 1.00 32.02 ? 187 TYR A CA 1 ATOM 1304 C C . TYR A 1 187 ? 23.044 -0.321 25.732 1.00 29.32 ? 187 TYR A C 1 ATOM 1305 O O . TYR A 1 187 ? 23.335 0.781 25.260 1.00 27.16 ? 187 TYR A O 1 ATOM 1306 C CB . TYR A 1 187 ? 24.804 -1.876 26.590 1.00 28.89 ? 187 TYR A CB 1 ATOM 1307 C CG . TYR A 1 187 ? 25.751 -0.737 26.889 1.00 34.68 ? 187 TYR A CG 1 ATOM 1308 C CD1 . TYR A 1 187 ? 25.387 0.274 27.773 1.00 36.03 ? 187 TYR A CD1 1 ATOM 1309 C CD2 . TYR A 1 187 ? 27.006 -0.665 26.304 1.00 36.82 ? 187 TYR A CD2 1 ATOM 1310 C CE1 . TYR A 1 187 ? 26.245 1.316 28.055 1.00 35.41 ? 187 TYR A CE1 1 ATOM 1311 C CE2 . TYR A 1 187 ? 27.875 0.375 26.577 1.00 36.86 ? 187 TYR A CE2 1 ATOM 1312 C CZ . TYR A 1 187 ? 27.482 1.366 27.458 1.00 40.76 ? 187 TYR A CZ 1 ATOM 1313 O OH . TYR A 1 187 ? 28.333 2.410 27.742 1.00 37.63 ? 187 TYR A OH 1 ATOM 1314 N N . ILE A 1 188 ? 22.003 -0.495 26.550 1.00 29.54 ? 188 ILE A N 1 ATOM 1315 C CA . ILE A 1 188 ? 21.175 0.659 26.930 1.00 30.88 ? 188 ILE A CA 1 ATOM 1316 C C . ILE A 1 188 ? 20.452 0.389 28.232 1.00 28.69 ? 188 ILE A C 1 ATOM 1317 O O . ILE A 1 188 ? 19.875 -0.674 28.469 1.00 27.45 ? 188 ILE A O 1 ATOM 1318 C CB . ILE A 1 188 ? 20.245 1.092 25.804 1.00 32.69 ? 188 ILE A CB 1 ATOM 1319 C CG1 . ILE A 1 188 ? 19.563 2.434 26.149 1.00 32.50 ? 188 ILE A CG1 1 ATOM 1320 C CG2 . ILE A 1 188 ? 19.223 0.020 25.491 1.00 32.40 ? 188 ILE A CG2 1 ATOM 1321 C CD1 . ILE A 1 188 ? 18.976 3.116 24.926 1.00 31.89 ? 188 ILE A CD1 1 ATOM 1322 N N . PHE A 1 189 ? 20.536 1.367 29.139 1.00 36.01 ? 189 PHE A N 1 ATOM 1323 C CA . PHE A 1 189 ? 19.895 1.230 30.444 1.00 38.31 ? 189 PHE A CA 1 ATOM 1324 C C . PHE A 1 189 ? 19.059 2.474 30.726 1.00 33.66 ? 189 PHE A C 1 ATOM 1325 O O . PHE A 1 189 ? 19.566 3.590 30.645 1.00 28.58 ? 189 PHE A O 1 ATOM 1326 C CB . PHE A 1 189 ? 20.910 0.980 31.557 1.00 42.13 ? 189 PHE A CB 1 ATOM 1327 C CG . PHE A 1 189 ? 20.292 1.096 32.926 1.00 48.00 ? 189 PHE A CG 1 ATOM 1328 C CD1 . PHE A 1 189 ? 19.673 0.010 33.507 1.00 50.38 ? 189 PHE A CD1 1 ATOM 1329 C CD2 . PHE A 1 189 ? 20.323 2.299 33.614 1.00 50.39 ? 189 PHE A CD2 1 ATOM 1330 C CE1 . PHE A 1 189 ? 19.096 0.111 34.760 1.00 54.16 ? 189 PHE A CE1 1 ATOM 1331 C CE2 . PHE A 1 189 ? 19.749 2.405 34.867 1.00 52.05 ? 189 PHE A CE2 1 ATOM 1332 C CZ . PHE A 1 189 ? 19.134 1.309 35.442 1.00 53.22 ? 189 PHE A CZ 1 ATOM 1333 N N . PHE A 1 190 ? 17.777 2.255 31.027 1.00 31.84 ? 190 PHE A N 1 ATOM 1334 C CA . PHE A 1 190 ? 16.884 3.369 31.298 1.00 35.13 ? 190 PHE A CA 1 ATOM 1335 C C . PHE A 1 190 ? 16.125 3.238 32.611 1.00 25.23 ? 190 PHE A C 1 ATOM 1336 O O . PHE A 1 190 ? 15.467 2.245 32.891 1.00 24.65 ? 190 PHE A O 1 ATOM 1337 C CB . PHE A 1 190 ? 15.874 3.536 30.152 1.00 34.87 ? 190 PHE A CB 1 ATOM 1338 C CG . PHE A 1 190 ? 14.901 4.662 30.355 1.00 37.01 ? 190 PHE A CG 1 ATOM 1339 C CD1 . PHE A 1 190 ? 15.329 5.978 30.348 1.00 38.83 ? 190 PHE A CD1 1 ATOM 1340 C CD2 . PHE A 1 190 ? 13.553 4.406 30.547 1.00 37.38 ? 190 PHE A CD2 1 ATOM 1341 C CE1 . PHE A 1 190 ? 14.435 7.016 30.533 1.00 39.68 ? 190 PHE A CE1 1 ATOM 1342 C CE2 . PHE A 1 190 ? 12.654 5.437 30.731 1.00 37.55 ? 190 PHE A CE2 1 ATOM 1343 C CZ . PHE A 1 190 ? 13.095 6.747 30.724 1.00 38.09 ? 190 PHE A CZ 1 ATOM 1344 N N . LYS A 1 191 ? 16.205 4.284 33.410 1.00 36.51 ? 191 LYS A N 1 ATOM 1345 C CA . LYS A 1 191 ? 15.505 4.393 34.682 1.00 40.97 ? 191 LYS A CA 1 ATOM 1346 C C . LYS A 1 191 ? 14.985 5.841 34.757 1.00 38.89 ? 191 LYS A C 1 ATOM 1347 O O . LYS A 1 191 ? 15.678 6.716 35.253 1.00 40.98 ? 191 LYS A O 1 ATOM 1348 C CB . LYS A 1 191 ? 16.385 4.089 35.877 1.00 42.95 ? 191 LYS A CB 1 ATOM 1349 C CG . LYS A 1 191 ? 15.663 4.214 37.216 1.00 47.09 ? 191 LYS A CG 1 ATOM 1350 C CD . LYS A 1 191 ? 16.618 3.982 38.376 1.00 49.07 ? 191 LYS A CD 1 ATOM 1351 C CE . LYS A 1 191 ? 15.934 4.247 39.710 1.00 49.43 ? 191 LYS A CE 1 ATOM 1352 N NZ . LYS A 1 191 ? 16.894 4.143 40.846 1.00 50.02 ? 191 LYS A NZ 1 ATOM 1353 N N . GLY A 1 192 ? 13.816 6.063 34.173 1.00 37.38 ? 192 GLY A N 1 ATOM 1354 C CA . GLY A 1 192 ? 13.248 7.390 34.090 1.00 40.89 ? 192 GLY A CA 1 ATOM 1355 C C . GLY A 1 192 ? 12.502 7.854 35.320 1.00 35.85 ? 192 GLY A C 1 ATOM 1356 O O . GLY A 1 192 ? 12.088 7.081 36.182 1.00 35.57 ? 192 GLY A O 1 ATOM 1357 N N . LYS A 1 193 ? 12.323 9.170 35.394 1.00 38.28 ? 193 LYS A N 1 ATOM 1358 C CA . LYS A 1 193 ? 11.599 9.802 36.495 1.00 39.79 ? 193 LYS A CA 1 ATOM 1359 C C . LYS A 1 193 ? 10.256 10.303 35.961 1.00 35.28 ? 193 LYS A C 1 ATOM 1360 O O . LYS A 1 193 ? 10.242 11.026 34.961 1.00 29.57 ? 193 LYS A O 1 ATOM 1361 C CB . LYS A 1 193 ? 12.401 10.974 37.060 1.00 43.23 ? 193 LYS A CB 1 ATOM 1362 C CG . LYS A 1 193 ? 13.715 10.590 37.712 1.00 47.63 ? 193 LYS A CG 1 ATOM 1363 C CD . LYS A 1 193 ? 14.500 11.812 38.167 1.00 50.39 ? 193 LYS A CD 1 ATOM 1364 C CE . LYS A 1 193 ? 15.044 12.603 36.990 1.00 51.15 ? 193 LYS A CE 1 ATOM 1365 N NZ . LYS A 1 193 ? 15.986 13.671 37.434 1.00 51.82 ? 193 LYS A NZ 1 ATOM 1366 N N . TRP A 1 194 ? 9.159 9.914 36.597 1.00 30.35 ? 194 TRP A N 1 ATOM 1367 C CA . TRP A 1 194 ? 7.844 10.358 36.133 1.00 27.01 ? 194 TRP A CA 1 ATOM 1368 C C . TRP A 1 194 ? 7.653 11.848 36.419 1.00 29.87 ? 194 TRP A C 1 ATOM 1369 O O . TRP A 1 194 ? 8.090 12.332 37.465 1.00 33.90 ? 194 TRP A O 1 ATOM 1370 C CB . TRP A 1 194 ? 6.728 9.578 36.820 1.00 26.25 ? 194 TRP A CB 1 ATOM 1371 C CG . TRP A 1 194 ? 6.703 8.107 36.557 1.00 25.76 ? 194 TRP A CG 1 ATOM 1372 C CD1 . TRP A 1 194 ? 6.796 7.107 37.486 1.00 23.77 ? 194 TRP A CD1 1 ATOM 1373 C CD2 . TRP A 1 194 ? 6.563 7.462 35.287 1.00 25.91 ? 194 TRP A CD2 1 ATOM 1374 N NE1 . TRP A 1 194 ? 6.727 5.886 36.868 1.00 25.71 ? 194 TRP A NE1 1 ATOM 1375 C CE2 . TRP A 1 194 ? 6.588 6.072 35.517 1.00 27.50 ? 194 TRP A CE2 1 ATOM 1376 C CE3 . TRP A 1 194 ? 6.426 7.927 33.973 1.00 27.10 ? 194 TRP A CE3 1 ATOM 1377 C CZ2 . TRP A 1 194 ? 6.475 5.144 34.484 1.00 26.84 ? 194 TRP A CZ2 1 ATOM 1378 C CZ3 . TRP A 1 194 ? 6.318 7.002 32.950 1.00 27.97 ? 194 TRP A CZ3 1 ATOM 1379 C CH2 . TRP A 1 194 ? 6.343 5.629 33.212 1.00 27.52 ? 194 TRP A CH2 1 ATOM 1380 N N . GLU A 1 195 ? 6.978 12.549 35.508 1.00 33.48 ? 195 GLU A N 1 ATOM 1381 C CA . GLU A 1 195 ? 6.673 13.965 35.768 1.00 31.92 ? 195 GLU A CA 1 ATOM 1382 C C . GLU A 1 195 ? 5.648 13.998 36.916 1.00 30.63 ? 195 GLU A C 1 ATOM 1383 O O . GLU A 1 195 ? 5.616 14.914 37.716 1.00 26.29 ? 195 GLU A O 1 ATOM 1384 C CB . GLU A 1 195 ? 6.107 14.670 34.552 1.00 30.99 ? 195 GLU A CB 1 ATOM 1385 C CG . GLU A 1 195 ? 7.115 14.964 33.459 1.00 34.35 ? 195 GLU A CG 1 ATOM 1386 C CD . GLU A 1 195 ? 6.678 16.047 32.496 1.00 34.87 ? 195 GLU A CD 1 ATOM 1387 O OE1 . GLU A 1 195 ? 5.487 16.408 32.462 1.00 32.93 ? 195 GLU A OE1 1 ATOM 1388 O OE2 . GLU A 1 195 ? 7.549 16.550 31.750 1.00 38.18 ? 195 GLU A OE2 1 ATOM 1389 N N . ARG A 1 196 ? 4.830 12.953 36.945 1.00 29.72 ? 196 ARG A N 1 ATOM 1390 C CA . ARG A 1 196 ? 3.795 12.791 37.970 1.00 31.82 ? 196 ARG A CA 1 ATOM 1391 C C . ARG A 1 196 ? 3.975 11.416 38.609 1.00 28.49 ? 196 ARG A C 1 ATOM 1392 O O . ARG A 1 196 ? 3.503 10.403 38.106 1.00 22.64 ? 196 ARG A O 1 ATOM 1393 C CB . ARG A 1 196 ? 2.415 12.983 37.345 1.00 33.07 ? 196 ARG A CB 1 ATOM 1394 C CG . ARG A 1 196 ? 2.381 14.217 36.441 1.00 33.63 ? 196 ARG A CG 1 ATOM 1395 C CD . ARG A 1 196 ? 0.965 14.598 36.030 1.00 34.57 ? 196 ARG A CD 1 ATOM 1396 N NE . ARG A 1 196 ? 0.981 15.731 35.123 1.00 34.23 ? 196 ARG A NE 1 ATOM 1397 C CZ . ARG A 1 196 ? 0.039 16.610 34.865 1.00 32.92 ? 196 ARG A CZ 1 ATOM 1398 N NH1 . ARG A 1 196 ? -1.145 16.565 35.463 1.00 34.06 ? 196 ARG A NH1 1 ATOM 1399 N NH2 . ARG A 1 196 ? 0.291 17.581 33.978 1.00 30.43 ? 196 ARG A NH2 1 ATOM 1400 N N . PRO A 1 197 ? 4.737 11.378 39.698 1.00 31.82 ? 197 PRO A N 1 ATOM 1401 C CA . PRO A 1 197 ? 5.137 10.162 40.355 1.00 30.24 ? 197 PRO A CA 1 ATOM 1402 C C . PRO A 1 197 ? 4.116 9.484 41.236 1.00 28.42 ? 197 PRO A C 1 ATOM 1403 O O . PRO A 1 197 ? 3.114 10.054 41.646 1.00 22.95 ? 197 PRO A O 1 ATOM 1404 C CB . PRO A 1 197 ? 6.333 10.598 41.217 1.00 31.68 ? 197 PRO A CB 1 ATOM 1405 C CG . PRO A 1 197 ? 6.014 12.021 41.553 1.00 34.98 ? 197 PRO A CG 1 ATOM 1406 C CD . PRO A 1 197 ? 5.365 12.582 40.316 1.00 29.21 ? 197 PRO A CD 1 ATOM 1407 N N . PHE A 1 198 ? 4.401 8.212 41.534 1.00 26.56 ? 198 PHE A N 1 ATOM 1408 C CA . PHE A 1 198 ? 3.557 7.402 42.396 1.00 25.88 ? 198 PHE A CA 1 ATOM 1409 C C . PHE A 1 198 ? 4.065 7.560 43.841 1.00 30.27 ? 198 PHE A C 1 ATOM 1410 O O . PHE A 1 198 ? 5.219 7.949 44.036 1.00 27.31 ? 198 PHE A O 1 ATOM 1411 C CB . PHE A 1 198 ? 3.647 5.916 42.029 1.00 25.82 ? 198 PHE A CB 1 ATOM 1412 C CG . PHE A 1 198 ? 3.008 5.550 40.724 1.00 22.25 ? 198 PHE A CG 1 ATOM 1413 C CD1 . PHE A 1 198 ? 1.682 5.158 40.673 1.00 20.28 ? 198 PHE A CD1 1 ATOM 1414 C CD2 . PHE A 1 198 ? 3.735 5.593 39.542 1.00 21.45 ? 198 PHE A CD2 1 ATOM 1415 C CE1 . PHE A 1 198 ? 1.088 4.819 39.476 1.00 21.19 ? 198 PHE A CE1 1 ATOM 1416 C CE2 . PHE A 1 198 ? 3.146 5.255 38.340 1.00 20.40 ? 198 PHE A CE2 1 ATOM 1417 C CZ . PHE A 1 198 ? 1.822 4.864 38.301 1.00 20.98 ? 198 PHE A CZ 1 ATOM 1418 N N . GLU A 1 199 ? 3.206 7.263 44.799 1.00 30.17 ? 199 GLU A N 1 ATOM 1419 C CA . GLU A 1 199 ? 3.597 7.342 46.207 1.00 33.70 ? 199 GLU A CA 1 ATOM 1420 C C . GLU A 1 199 ? 4.020 5.950 46.678 1.00 25.86 ? 199 GLU A C 1 ATOM 1421 O O . GLU A 1 199 ? 3.245 5.000 46.554 1.00 27.09 ? 199 GLU A O 1 ATOM 1422 C CB . GLU A 1 199 ? 2.446 7.865 47.065 1.00 31.62 ? 199 GLU A CB 1 ATOM 1423 C CG . GLU A 1 199 ? 2.126 9.336 46.846 1.00 36.15 ? 199 GLU A CG 1 ATOM 1424 C CD . GLU A 1 199 ? 0.965 9.806 47.701 1.00 39.01 ? 199 GLU A CD 1 ATOM 1425 O OE1 . GLU A 1 199 ? 0.902 9.399 48.883 1.00 41.66 ? 199 GLU A OE1 1 ATOM 1426 O OE2 . GLU A 1 199 ? 0.115 10.570 47.200 1.00 40.42 ? 199 GLU A OE2 1 ATOM 1427 N N . VAL A 1 200 ? 5.230 5.830 47.190 1.00 27.56 ? 200 VAL A N 1 ATOM 1428 C CA . VAL A 1 200 ? 5.741 4.540 47.656 1.00 29.69 ? 200 VAL A CA 1 ATOM 1429 C C . VAL A 1 200 ? 4.839 3.882 48.679 1.00 32.13 ? 200 VAL A C 1 ATOM 1430 O O . VAL A 1 200 ? 4.601 2.662 48.654 1.00 29.96 ? 200 VAL A O 1 ATOM 1431 C CB . VAL A 1 200 ? 7.162 4.723 48.228 1.00 32.03 ? 200 VAL A CB 1 ATOM 1432 C CG1 . VAL A 1 200 ? 7.742 3.396 48.675 1.00 34.49 ? 200 VAL A CG1 1 ATOM 1433 C CG2 . VAL A 1 200 ? 8.059 5.389 47.184 1.00 31.64 ? 200 VAL A CG2 1 ATOM 1434 N N . LYS A 1 201 ? 4.291 4.658 49.614 1.00 33.76 ? 201 LYS A N 1 ATOM 1435 C CA . LYS A 1 201 ? 3.419 4.085 50.640 1.00 34.94 ? 201 LYS A CA 1 ATOM 1436 C C . LYS A 1 201 ? 2.213 3.383 50.039 1.00 35.10 ? 201 LYS A C 1 ATOM 1437 O O . LYS A 1 201 ? 1.615 2.527 50.700 1.00 32.70 ? 201 LYS A O 1 ATOM 1438 C CB . LYS A 1 201 ? 2.969 5.145 51.639 1.00 36.73 ? 201 LYS A CB 1 ATOM 1439 C CG . LYS A 1 201 ? 1.884 6.067 51.104 1.00 40.80 ? 201 LYS A CG 1 ATOM 1440 C CD . LYS A 1 201 ? 1.063 6.660 52.244 1.00 43.84 ? 201 LYS A CD 1 ATOM 1441 C CE . LYS A 1 201 ? 0.118 7.735 51.723 1.00 44.01 ? 201 LYS A CE 1 ATOM 1442 N NZ . LYS A 1 201 ? 0.875 8.835 51.058 1.00 44.70 ? 201 LYS A NZ 1 ATOM 1443 N N . ASP A 1 202 ? 1.857 3.713 48.798 1.00 30.78 ? 202 ASP A N 1 ATOM 1444 C CA . ASP A 1 202 ? 0.702 3.108 48.155 1.00 27.11 ? 202 ASP A CA 1 ATOM 1445 C C . ASP A 1 202 ? 1.041 1.862 47.354 1.00 25.81 ? 202 ASP A C 1 ATOM 1446 O O . ASP A 1 202 ? 0.138 1.179 46.846 1.00 25.41 ? 202 ASP A O 1 ATOM 1447 C CB . ASP A 1 202 ? -0.005 4.133 47.256 1.00 31.59 ? 202 ASP A CB 1 ATOM 1448 C CG . ASP A 1 202 ? -0.592 5.272 48.078 1.00 34.41 ? 202 ASP A CG 1 ATOM 1449 O OD1 . ASP A 1 202 ? -1.218 4.970 49.114 1.00 32.92 ? 202 ASP A OD1 1 ATOM 1450 O OD2 . ASP A 1 202 ? -0.420 6.439 47.684 1.00 35.49 ? 202 ASP A OD2 1 ATOM 1451 N N . THR A 1 203 ? 2.322 1.542 47.249 1.00 21.51 ? 203 THR A N 1 ATOM 1452 C CA . THR A 1 203 ? 2.722 0.324 46.520 1.00 27.23 ? 203 THR A CA 1 ATOM 1453 C C . THR A 1 203 ? 2.517 -0.919 47.384 1.00 30.05 ? 203 THR A C 1 ATOM 1454 O O . THR A 1 203 ? 3.123 -1.014 48.451 1.00 38.12 ? 203 THR A O 1 ATOM 1455 C CB . THR A 1 203 ? 4.202 0.426 46.117 1.00 28.12 ? 203 THR A CB 1 ATOM 1456 O OG1 . THR A 1 203 ? 4.349 1.529 45.200 1.00 27.67 ? 203 THR A OG1 1 ATOM 1457 C CG2 . THR A 1 203 ? 4.675 -0.853 45.436 1.00 27.08 ? 203 THR A CG2 1 ATOM 1458 N N . GLU A 1 204 ? 1.682 -1.858 46.950 1.00 28.39 ? 204 GLU A N 1 ATOM 1459 C CA . GLU A 1 204 ? 1.466 -3.098 47.690 1.00 35.18 ? 204 GLU A CA 1 ATOM 1460 C C . GLU A 1 204 ? 1.447 -4.312 46.765 1.00 36.41 ? 204 GLU A C 1 ATOM 1461 O O . GLU A 1 204 ? 1.432 -4.179 45.539 1.00 29.45 ? 204 GLU A O 1 ATOM 1462 C CB . GLU A 1 204 ? 0.230 -3.048 48.563 1.00 38.18 ? 204 GLU A CB 1 ATOM 1463 C CG . GLU A 1 204 ? -1.080 -2.670 47.911 1.00 43.37 ? 204 GLU A CG 1 ATOM 1464 C CD . GLU A 1 204 ? -2.041 -2.018 48.895 1.00 49.39 ? 204 GLU A CD 1 ATOM 1465 O OE1 . GLU A 1 204 ? -1.633 -1.770 50.051 1.00 51.11 ? 204 GLU A OE1 1 ATOM 1466 O OE2 . GLU A 1 204 ? -3.205 -1.745 48.534 1.00 50.14 ? 204 GLU A OE2 1 ATOM 1467 N N . GLU A 1 205 ? 1.479 -5.510 47.346 1.00 36.73 ? 205 GLU A N 1 ATOM 1468 C CA . GLU A 1 205 ? 1.486 -6.750 46.586 1.00 35.80 ? 205 GLU A CA 1 ATOM 1469 C C . GLU A 1 205 ? 0.115 -7.055 45.996 1.00 35.20 ? 205 GLU A C 1 ATOM 1470 O O . GLU A 1 205 ? -0.896 -6.989 46.691 1.00 34.03 ? 205 GLU A O 1 ATOM 1471 C CB . GLU A 1 205 ? 1.944 -7.929 47.451 1.00 39.02 ? 205 GLU A CB 1 ATOM 1472 C CG . GLU A 1 205 ? 3.402 -7.890 47.861 1.00 41.52 ? 205 GLU A CG 1 ATOM 1473 C CD . GLU A 1 205 ? 4.357 -7.968 46.689 1.00 44.28 ? 205 GLU A CD 1 ATOM 1474 O OE1 . GLU A 1 205 ? 4.343 -8.986 45.966 1.00 45.55 ? 205 GLU A OE1 1 ATOM 1475 O OE2 . GLU A 1 205 ? 5.129 -7.007 46.484 1.00 45.29 ? 205 GLU A OE2 1 ATOM 1476 N N . GLU A 1 206 ? 0.080 -7.377 44.707 1.00 30.78 ? 206 GLU A N 1 ATOM 1477 C CA . GLU A 1 206 ? -1.161 -7.691 44.022 1.00 33.05 ? 206 GLU A CA 1 ATOM 1478 C C . GLU A 1 206 ? -0.974 -8.870 43.061 1.00 29.91 ? 206 GLU A C 1 ATOM 1479 O O . GLU A 1 206 ? 0.147 -9.230 42.722 1.00 28.74 ? 206 GLU A O 1 ATOM 1480 C CB . GLU A 1 206 ? -1.673 -6.498 43.216 1.00 34.90 ? 206 GLU A CB 1 ATOM 1481 C CG . GLU A 1 206 ? -2.107 -5.289 44.023 1.00 39.30 ? 206 GLU A CG 1 ATOM 1482 C CD . GLU A 1 206 ? -2.839 -4.270 43.162 1.00 40.83 ? 206 GLU A CD 1 ATOM 1483 O OE1 . GLU A 1 206 ? -3.454 -4.675 42.151 1.00 40.47 ? 206 GLU A OE1 1 ATOM 1484 O OE2 . GLU A 1 206 ? -2.806 -3.071 43.492 1.00 40.56 ? 206 GLU A OE2 1 ATOM 1485 N N . ASP A 1 207 ? -2.089 -9.437 42.614 1.00 26.81 ? 207 ASP A N 1 ATOM 1486 C CA . ASP A 1 207 ? -2.044 -10.551 41.675 1.00 30.65 ? 207 ASP A CA 1 ATOM 1487 C C . ASP A 1 207 ? -1.811 -10.054 40.241 1.00 30.68 ? 207 ASP A C 1 ATOM 1488 O O . ASP A 1 207 ? -2.267 -8.974 39.880 1.00 26.87 ? 207 ASP A O 1 ATOM 1489 C CB . ASP A 1 207 ? -3.362 -11.320 41.699 1.00 30.61 ? 207 ASP A CB 1 ATOM 1490 C CG . ASP A 1 207 ? -3.591 -12.108 42.975 1.00 29.61 ? 207 ASP A CG 1 ATOM 1491 O OD1 . ASP A 1 207 ? -2.625 -12.569 43.604 1.00 27.30 ? 207 ASP A OD1 1 ATOM 1492 O OD2 . ASP A 1 207 ? -4.774 -12.257 43.333 1.00 32.67 ? 207 ASP A OD2 1 ATOM 1493 N N . PHE A 1 208 ? -1.141 -10.862 39.450 1.00 26.86 ? 208 PHE A N 1 ATOM 1494 C CA . PHE A 1 208 ? -0.851 -10.600 38.049 1.00 30.35 ? 208 PHE A CA 1 ATOM 1495 C C . PHE A 1 208 ? -1.219 -11.876 37.266 1.00 29.80 ? 208 PHE A C 1 ATOM 1496 O O . PHE A 1 208 ? -0.642 -12.929 37.509 1.00 30.89 ? 208 PHE A O 1 ATOM 1497 C CB . PHE A 1 208 ? 0.620 -10.258 37.826 1.00 29.69 ? 208 PHE A CB 1 ATOM 1498 C CG . PHE A 1 208 ? 0.937 -9.752 36.441 1.00 30.92 ? 208 PHE A CG 1 ATOM 1499 C CD1 . PHE A 1 208 ? 0.979 -10.616 35.365 1.00 31.56 ? 208 PHE A CD1 1 ATOM 1500 C CD2 . PHE A 1 208 ? 1.190 -8.407 36.226 1.00 31.63 ? 208 PHE A CD2 1 ATOM 1501 C CE1 . PHE A 1 208 ? 1.268 -10.155 34.092 1.00 33.20 ? 208 PHE A CE1 1 ATOM 1502 C CE2 . PHE A 1 208 ? 1.478 -7.934 34.957 1.00 33.38 ? 208 PHE A CE2 1 ATOM 1503 C CZ . PHE A 1 208 ? 1.520 -8.812 33.890 1.00 32.09 ? 208 PHE A CZ 1 ATOM 1504 N N . HIS A 1 209 ? -2.233 -11.791 36.427 1.00 31.10 ? 209 HIS A N 1 ATOM 1505 C CA . HIS A 1 209 ? -2.749 -12.911 35.677 1.00 31.62 ? 209 HIS A CA 1 ATOM 1506 C C . HIS A 1 209 ? -1.896 -13.313 34.487 1.00 35.95 ? 209 HIS A C 1 ATOM 1507 O O . HIS A 1 209 ? -1.969 -12.693 33.416 1.00 30.52 ? 209 HIS A O 1 ATOM 1508 C CB . HIS A 1 209 ? -4.184 -12.590 35.201 1.00 35.12 ? 209 HIS A CB 1 ATOM 1509 C CG . HIS A 1 209 ? -5.126 -12.322 36.335 1.00 38.86 ? 209 HIS A CG 1 ATOM 1510 N ND1 . HIS A 1 209 ? -6.178 -13.154 36.648 1.00 38.98 ? 209 HIS A ND1 1 ATOM 1511 C CD2 . HIS A 1 209 ? -5.163 -11.311 37.236 1.00 39.90 ? 209 HIS A CD2 1 ATOM 1512 C CE1 . HIS A 1 209 ? -6.828 -12.669 37.692 1.00 38.70 ? 209 HIS A CE1 1 ATOM 1513 N NE2 . HIS A 1 209 ? -6.234 -11.551 38.068 1.00 40.63 ? 209 HIS A NE2 1 ATOM 1514 N N . VAL A 1 210 ? -1.101 -14.369 34.652 1.00 37.22 ? 210 VAL A N 1 ATOM 1515 C CA . VAL A 1 210 ? -0.258 -14.850 33.550 1.00 38.75 ? 210 VAL A CA 1 ATOM 1516 C C . VAL A 1 210 ? -1.099 -15.679 32.584 1.00 39.95 ? 210 VAL A C 1 ATOM 1517 O O . VAL A 1 210 ? -0.917 -15.633 31.372 1.00 42.71 ? 210 VAL A O 1 ATOM 1518 C CB . VAL A 1 210 ? 0.967 -15.623 34.024 1.00 39.32 ? 210 VAL A CB 1 ATOM 1519 C CG1 . VAL A 1 210 ? 1.946 -14.681 34.725 1.00 37.44 ? 210 VAL A CG1 1 ATOM 1520 C CG2 . VAL A 1 210 ? 0.594 -16.778 34.943 1.00 36.52 ? 210 VAL A CG2 1 ATOM 1521 N N . ASP A 1 211 ? -2.035 -16.422 33.134 1.00 39.60 ? 211 ASP A N 1 ATOM 1522 C CA . ASP A 1 211 ? -2.990 -17.252 32.432 1.00 42.07 ? 211 ASP A CA 1 ATOM 1523 C C . ASP A 1 211 ? -4.392 -16.711 32.818 1.00 37.06 ? 211 ASP A C 1 ATOM 1524 O O . ASP A 1 211 ? -4.473 -15.903 33.743 1.00 37.84 ? 211 ASP A O 1 ATOM 1525 C CB . ASP A 1 211 ? -2.982 -18.714 32.933 1.00 41.18 ? 211 ASP A CB 1 ATOM 1526 C CG . ASP A 1 211 ? -1.762 -19.520 32.644 1.00 42.98 ? 211 ASP A CG 1 ATOM 1527 O OD1 . ASP A 1 211 ? -0.719 -19.369 33.319 1.00 43.19 ? 211 ASP A OD1 1 ATOM 1528 O OD2 . ASP A 1 211 ? -1.792 -20.372 31.711 1.00 51.53 ? 211 ASP A OD2 1 ATOM 1529 N N . GLN A 1 212 ? -5.428 -17.211 32.175 1.00 38.22 ? 212 GLN A N 1 ATOM 1530 C CA . GLN A 1 212 ? -6.785 -16.802 32.543 1.00 40.25 ? 212 GLN A CA 1 ATOM 1531 C C . GLN A 1 212 ? -7.224 -17.548 33.799 1.00 43.45 ? 212 GLN A C 1 ATOM 1532 O O . GLN A 1 212 ? -8.305 -17.305 34.339 1.00 35.99 ? 212 GLN A O 1 ATOM 1533 C CB . GLN A 1 212 ? -7.757 -17.002 31.388 1.00 42.52 ? 212 GLN A CB 1 ATOM 1534 C CG . GLN A 1 212 ? -7.573 -15.971 30.277 1.00 46.06 ? 212 GLN A CG 1 ATOM 1535 C CD . GLN A 1 212 ? -8.765 -15.874 29.353 1.00 47.84 ? 212 GLN A CD 1 ATOM 1536 O OE1 . GLN A 1 212 ? -9.909 -15.765 29.803 1.00 49.00 ? 212 GLN A OE1 1 ATOM 1537 N NE2 . GLN A 1 212 ? -8.509 -15.908 28.050 1.00 48.35 ? 212 GLN A NE2 1 ATOM 1538 N N . VAL A 1 213 ? -6.363 -18.451 34.293 1.00 34.12 ? 213 VAL A N 1 ATOM 1539 C CA . VAL A 1 213 ? -6.695 -19.186 35.511 1.00 31.61 ? 213 VAL A CA 1 ATOM 1540 C C . VAL A 1 213 ? -5.551 -19.226 36.506 1.00 28.64 ? 213 VAL A C 1 ATOM 1541 O O . VAL A 1 213 ? -5.643 -19.896 37.550 1.00 32.71 ? 213 VAL A O 1 ATOM 1542 C CB . VAL A 1 213 ? -7.157 -20.624 35.190 1.00 33.66 ? 213 VAL A CB 1 ATOM 1543 C CG1 . VAL A 1 213 ? -8.308 -20.595 34.184 1.00 31.90 ? 213 VAL A CG1 1 ATOM 1544 C CG2 . VAL A 1 213 ? -6.001 -21.460 34.673 1.00 27.80 ? 213 VAL A CG2 1 ATOM 1545 N N . THR A 1 214 ? -4.469 -18.524 36.235 1.00 22.12 ? 214 THR A N 1 ATOM 1546 C CA . THR A 1 214 ? -3.283 -18.509 37.066 1.00 28.20 ? 214 THR A CA 1 ATOM 1547 C C . THR A 1 214 ? -2.802 -17.099 37.406 1.00 31.55 ? 214 THR A C 1 ATOM 1548 O O . THR A 1 214 ? -2.641 -16.265 36.514 1.00 28.08 ? 214 THR A O 1 ATOM 1549 C CB . THR A 1 214 ? -2.119 -19.208 36.312 1.00 29.64 ? 214 THR A CB 1 ATOM 1550 O OG1 . THR A 1 214 ? -2.601 -20.396 35.696 1.00 26.13 ? 214 THR A OG1 1 ATOM 1551 C CG2 . THR A 1 214 ? -0.983 -19.534 37.257 1.00 34.90 ? 214 THR A CG2 1 ATOM 1552 N N . THR A 1 215 ? -2.497 -16.871 38.674 1.00 30.77 ? 215 THR A N 1 ATOM 1553 C CA . THR A 1 215 ? -1.995 -15.587 39.128 1.00 30.49 ? 215 THR A CA 1 ATOM 1554 C C . THR A 1 215 ? -0.683 -15.721 39.891 1.00 28.99 ? 215 THR A C 1 ATOM 1555 O O . THR A 1 215 ? -0.313 -16.774 40.409 1.00 31.02 ? 215 THR A O 1 ATOM 1556 C CB . THR A 1 215 ? -3.026 -14.886 40.047 1.00 29.67 ? 215 THR A CB 1 ATOM 1557 O OG1 . THR A 1 215 ? -3.354 -15.772 41.128 1.00 30.55 ? 215 THR A OG1 1 ATOM 1558 C CG2 . THR A 1 215 ? -4.302 -14.564 39.289 1.00 29.33 ? 215 THR A CG2 1 ATOM 1559 N N . VAL A 1 216 ? 0.029 -14.613 39.985 1.00 32.23 ? 216 VAL A N 1 ATOM 1560 C CA . VAL A 1 216 ? 1.273 -14.497 40.722 1.00 31.30 ? 216 VAL A CA 1 ATOM 1561 C C . VAL A 1 216 ? 1.348 -13.082 41.309 1.00 30.73 ? 216 VAL A C 1 ATOM 1562 O O . VAL A 1 216 ? 0.859 -12.141 40.681 1.00 31.88 ? 216 VAL A O 1 ATOM 1563 C CB . VAL A 1 216 ? 2.515 -14.779 39.877 1.00 30.82 ? 216 VAL A CB 1 ATOM 1564 C CG1 . VAL A 1 216 ? 3.781 -14.351 40.601 1.00 29.84 ? 216 VAL A CG1 1 ATOM 1565 C CG2 . VAL A 1 216 ? 2.593 -16.258 39.513 1.00 32.48 ? 216 VAL A CG2 1 ATOM 1566 N N . LYS A 1 217 ? 1.917 -12.957 42.493 1.00 30.68 ? 217 LYS A N 1 ATOM 1567 C CA . LYS A 1 217 ? 2.000 -11.672 43.172 1.00 35.50 ? 217 LYS A CA 1 ATOM 1568 C C . LYS A 1 217 ? 3.209 -10.857 42.730 1.00 34.46 ? 217 LYS A C 1 ATOM 1569 O O . LYS A 1 217 ? 4.287 -11.393 42.497 1.00 35.17 ? 217 LYS A O 1 ATOM 1570 C CB . LYS A 1 217 ? 2.062 -11.863 44.696 1.00 33.66 ? 217 LYS A CB 1 ATOM 1571 C CG . LYS A 1 217 ? 1.016 -12.797 45.259 1.00 38.02 ? 217 LYS A CG 1 ATOM 1572 C CD . LYS A 1 217 ? -0.392 -12.226 45.130 1.00 38.77 ? 217 LYS A CD 1 ATOM 1573 C CE . LYS A 1 217 ? -1.295 -12.807 46.214 1.00 40.78 ? 217 LYS A CE 1 ATOM 1574 N NZ . LYS A 1 217 ? -2.696 -12.323 46.100 1.00 39.87 ? 217 LYS A NZ 1 ATOM 1575 N N . VAL A 1 218 ? 3.005 -9.545 42.630 1.00 35.06 ? 218 VAL A N 1 ATOM 1576 C CA . VAL A 1 218 ? 4.054 -8.615 42.243 1.00 35.40 ? 218 VAL A CA 1 ATOM 1577 C C . VAL A 1 218 ? 3.791 -7.245 42.882 1.00 31.11 ? 218 VAL A C 1 ATOM 1578 O O . VAL A 1 218 ? 2.637 -6.888 43.109 1.00 27.50 ? 218 VAL A O 1 ATOM 1579 C CB . VAL A 1 218 ? 4.100 -8.406 40.716 1.00 37.16 ? 218 VAL A CB 1 ATOM 1580 C CG1 . VAL A 1 218 ? 4.236 -9.735 39.990 1.00 38.47 ? 218 VAL A CG1 1 ATOM 1581 C CG2 . VAL A 1 218 ? 2.857 -7.657 40.251 1.00 35.99 ? 218 VAL A CG2 1 ATOM 1582 N N . PRO A 1 219 ? 4.842 -6.496 43.140 1.00 22.72 ? 219 PRO A N 1 ATOM 1583 C CA . PRO A 1 219 ? 4.696 -5.159 43.711 1.00 30.56 ? 219 PRO A CA 1 ATOM 1584 C C . PRO A 1 219 ? 3.895 -4.314 42.726 1.00 31.04 ? 219 PRO A C 1 ATOM 1585 O O . PRO A 1 219 ? 4.221 -4.271 41.531 1.00 28.15 ? 219 PRO A O 1 ATOM 1586 C CB . PRO A 1 219 ? 6.098 -4.677 43.926 1.00 31.53 ? 219 PRO A CB 1 ATOM 1587 C CG . PRO A 1 219 ? 7.005 -5.612 43.223 1.00 26.90 ? 219 PRO A CG 1 ATOM 1588 C CD . PRO A 1 219 ? 6.247 -6.853 42.892 1.00 25.60 ? 219 PRO A CD 1 ATOM 1589 N N . MET A 1 220 ? 2.818 -3.702 43.197 1.00 25.12 ? 220 MET A N 1 ATOM 1590 C CA . MET A 1 220 ? 1.961 -2.912 42.330 1.00 26.38 ? 220 MET A CA 1 ATOM 1591 C C . MET A 1 220 ? 1.815 -1.461 42.758 1.00 32.67 ? 220 MET A C 1 ATOM 1592 O O . MET A 1 220 ? 1.271 -1.145 43.818 1.00 24.59 ? 220 MET A O 1 ATOM 1593 C CB . MET A 1 220 ? 0.573 -3.548 42.197 1.00 25.18 ? 220 MET A CB 1 ATOM 1594 C CG . MET A 1 220 ? -0.301 -2.893 41.138 1.00 27.87 ? 220 MET A CG 1 ATOM 1595 S SD . MET A 1 220 ? 0.082 -3.415 39.452 1.00 27.93 ? 220 MET A SD 1 ATOM 1596 C CE . MET A 1 220 ? -0.379 -5.143 39.516 1.00 30.55 ? 220 MET A CE 1 ATOM 1597 N N . MET A 1 221 ? 2.282 -0.557 41.887 1.00 25.64 ? 221 MET A N 1 ATOM 1598 C CA . MET A 1 221 ? 2.161 0.868 42.187 1.00 17.77 ? 221 MET A CA 1 ATOM 1599 C C . MET A 1 221 ? 0.729 1.292 41.924 1.00 14.07 ? 221 MET A C 1 ATOM 1600 O O . MET A 1 221 ? 0.024 0.660 41.132 1.00 20.68 ? 221 MET A O 1 ATOM 1601 C CB . MET A 1 221 ? 3.164 1.709 41.403 1.00 24.27 ? 221 MET A CB 1 ATOM 1602 C CG . MET A 1 221 ? 4.618 1.289 41.592 1.00 23.65 ? 221 MET A CG 1 ATOM 1603 S SD . MET A 1 221 ? 5.761 2.286 40.582 1.00 23.76 ? 221 MET A SD 1 ATOM 1604 C CE . MET A 1 221 ? 4.952 2.177 39.000 1.00 22.27 ? 221 MET A CE 1 ATOM 1605 N N . LYS A 1 222 ? 0.224 2.282 42.686 1.00 18.52 ? 222 LYS A N 1 ATOM 1606 C CA . LYS A 1 222 ? -1.152 2.702 42.414 1.00 24.45 ? 222 LYS A CA 1 ATOM 1607 C C . LYS A 1 222 ? -1.331 4.177 42.744 1.00 20.40 ? 222 LYS A C 1 ATOM 1608 O O . LYS A 1 222 ? -0.623 4.717 43.584 1.00 18.94 ? 222 LYS A O 1 ATOM 1609 C CB . LYS A 1 222 ? -2.188 1.825 43.073 1.00 29.25 ? 222 LYS A CB 1 ATOM 1610 C CG . LYS A 1 222 ? -2.327 1.906 44.581 1.00 30.22 ? 222 LYS A CG 1 ATOM 1611 C CD . LYS A 1 222 ? -3.402 0.916 45.054 1.00 30.23 ? 222 LYS A CD 1 ATOM 1612 C CE . LYS A 1 222 ? -3.362 0.715 46.555 1.00 28.57 ? 222 LYS A CE 1 ATOM 1613 N NZ . LYS A 1 222 ? -2.032 0.221 47.025 1.00 30.49 ? 222 LYS A NZ 1 ATOM 1614 N N . ARG A 1 223 ? -2.245 4.810 42.018 1.00 20.39 ? 223 ARG A N 1 ATOM 1615 C CA . ARG A 1 223 ? -2.529 6.213 42.196 1.00 23.87 ? 223 ARG A CA 1 ATOM 1616 C C . ARG A 1 223 ? -3.858 6.619 41.562 1.00 22.86 ? 223 ARG A C 1 ATOM 1617 O O . ARG A 1 223 ? -4.238 6.162 40.492 1.00 22.29 ? 223 ARG A O 1 ATOM 1618 C CB . ARG A 1 223 ? -1.411 7.095 41.616 1.00 25.70 ? 223 ARG A CB 1 ATOM 1619 C CG . ARG A 1 223 ? -1.783 8.577 41.602 1.00 25.90 ? 223 ARG A CG 1 ATOM 1620 C CD . ARG A 1 223 ? -0.534 9.451 41.546 1.00 29.09 ? 223 ARG A CD 1 ATOM 1621 N NE . ARG A 1 223 ? -0.032 9.521 40.165 1.00 32.64 ? 223 ARG A NE 1 ATOM 1622 C CZ . ARG A 1 223 ? -0.544 10.387 39.286 1.00 32.96 ? 223 ARG A CZ 1 ATOM 1623 N NH1 . ARG A 1 223 ? -1.519 11.199 39.675 1.00 33.03 ? 223 ARG A NH1 1 ATOM 1624 N NH2 . ARG A 1 223 ? -0.079 10.429 38.050 1.00 32.07 ? 223 ARG A NH2 1 ATOM 1625 N N . LEU A 1 224 ? -4.536 7.514 42.261 1.00 19.82 ? 224 LEU A N 1 ATOM 1626 C CA . LEU A 1 224 ? -5.784 8.100 41.800 1.00 21.56 ? 224 LEU A CA 1 ATOM 1627 C C . LEU A 1 224 ? -5.456 9.519 41.302 1.00 22.69 ? 224 LEU A C 1 ATOM 1628 O O . LEU A 1 224 ? -4.907 10.323 42.062 1.00 21.04 ? 224 LEU A O 1 ATOM 1629 C CB . LEU A 1 224 ? -6.799 8.197 42.939 1.00 25.50 ? 224 LEU A CB 1 ATOM 1630 C CG . LEU A 1 224 ? -8.090 8.964 42.611 1.00 29.00 ? 224 LEU A CG 1 ATOM 1631 C CD1 . LEU A 1 224 ? -8.734 8.384 41.363 1.00 29.64 ? 224 LEU A CD1 1 ATOM 1632 C CD2 . LEU A 1 224 ? -9.050 8.907 43.794 1.00 29.41 ? 224 LEU A CD2 1 ATOM 1633 N N . GLY A 1 225 ? -5.745 9.781 40.038 1.00 25.84 ? 225 GLY A N 1 ATOM 1634 C CA . GLY A 1 225 ? -5.433 11.104 39.493 1.00 23.66 ? 225 GLY A CA 1 ATOM 1635 C C . GLY A 1 225 ? -6.035 11.276 38.105 1.00 23.42 ? 225 GLY A C 1 ATOM 1636 O O . GLY A 1 225 ? -6.913 10.531 37.692 1.00 22.72 ? 225 GLY A O 1 ATOM 1637 N N . MET A 1 226 ? -5.552 12.296 37.414 1.00 22.06 ? 226 MET A N 1 ATOM 1638 C CA . MET A 1 226 ? -5.996 12.627 36.068 1.00 19.91 ? 226 MET A CA 1 ATOM 1639 C C . MET A 1 226 ? -4.941 12.114 35.088 1.00 24.71 ? 226 MET A C 1 ATOM 1640 O O . MET A 1 226 ? -3.845 12.658 35.001 1.00 26.91 ? 226 MET A O 1 ATOM 1641 C CB . MET A 1 226 ? -6.189 14.136 35.929 1.00 20.58 ? 226 MET A CB 1 ATOM 1642 C CG . MET A 1 226 ? -7.179 14.699 36.962 1.00 21.21 ? 226 MET A CG 1 ATOM 1643 S SD . MET A 1 226 ? -8.808 13.941 36.814 1.00 22.70 ? 226 MET A SD 1 ATOM 1644 C CE . MET A 1 226 ? -9.412 14.691 35.314 1.00 24.53 ? 226 MET A CE 1 ATOM 1645 N N . PHE A 1 227 ? -5.283 11.034 34.397 1.00 24.01 ? 227 PHE A N 1 ATOM 1646 C CA . PHE A 1 227 ? -4.370 10.411 33.463 1.00 22.93 ? 227 PHE A CA 1 ATOM 1647 C C . PHE A 1 227 ? -4.844 10.529 32.022 1.00 23.81 ? 227 PHE A C 1 ATOM 1648 O O . PHE A 1 227 ? -6.050 10.599 31.749 1.00 24.66 ? 227 PHE A O 1 ATOM 1649 C CB . PHE A 1 227 ? -4.305 8.889 33.760 1.00 21.03 ? 227 PHE A CB 1 ATOM 1650 C CG . PHE A 1 227 ? -3.623 8.548 35.085 1.00 19.14 ? 227 PHE A CG 1 ATOM 1651 C CD1 . PHE A 1 227 ? -2.227 8.525 35.169 1.00 20.46 ? 227 PHE A CD1 1 ATOM 1652 C CD2 . PHE A 1 227 ? -4.398 8.251 36.212 1.00 18.02 ? 227 PHE A CD2 1 ATOM 1653 C CE1 . PHE A 1 227 ? -1.604 8.207 36.381 1.00 19.25 ? 227 PHE A CE1 1 ATOM 1654 C CE2 . PHE A 1 227 ? -3.776 7.933 37.425 1.00 18.13 ? 227 PHE A CE2 1 ATOM 1655 C CZ . PHE A 1 227 ? -2.378 7.910 37.509 1.00 16.57 ? 227 PHE A CZ 1 ATOM 1656 N N . ASN A 1 228 ? -3.856 10.542 31.149 1.00 28.21 ? 228 ASN A N 1 ATOM 1657 C CA . ASN A 1 228 ? -4.080 10.534 29.705 1.00 25.84 ? 228 ASN A CA 1 ATOM 1658 C C . ASN A 1 228 ? -4.255 9.077 29.306 1.00 24.93 ? 228 ASN A C 1 ATOM 1659 O O . ASN A 1 228 ? -3.333 8.447 28.767 1.00 23.43 ? 228 ASN A O 1 ATOM 1660 C CB . ASN A 1 228 ? -2.882 11.147 28.978 1.00 26.67 ? 228 ASN A CB 1 ATOM 1661 C CG . ASN A 1 228 ? -3.039 11.122 27.455 1.00 27.31 ? 228 ASN A CG 1 ATOM 1662 O OD1 . ASN A 1 228 ? -2.343 11.853 26.753 1.00 32.18 ? 228 ASN A OD1 1 ATOM 1663 N ND2 . ASN A 1 228 ? -3.923 10.316 26.896 1.00 24.96 ? 228 ASN A ND2 1 ATOM 1664 N N . ILE A 1 229 ? -5.442 8.592 29.607 1.00 20.26 ? 229 ILE A N 1 ATOM 1665 C CA . ILE A 1 229 ? -5.790 7.191 29.397 1.00 22.89 ? 229 ILE A CA 1 ATOM 1666 C C . ILE A 1 229 ? -7.144 7.037 28.746 1.00 26.89 ? 229 ILE A C 1 ATOM 1667 O O . ILE A 1 229 ? -8.048 7.854 28.963 1.00 28.57 ? 229 ILE A O 1 ATOM 1668 C CB . ILE A 1 229 ? -5.817 6.485 30.757 1.00 22.20 ? 229 ILE A CB 1 ATOM 1669 C CG1 . ILE A 1 229 ? -6.001 4.972 30.660 1.00 24.79 ? 229 ILE A CG1 1 ATOM 1670 C CG2 . ILE A 1 229 ? -6.947 6.978 31.664 1.00 24.99 ? 229 ILE A CG2 1 ATOM 1671 C CD1 . ILE A 1 229 ? -5.765 4.258 31.995 1.00 23.30 ? 229 ILE A CD1 1 ATOM 1672 N N . GLN A 1 230 ? -7.289 6.002 27.929 1.00 30.49 ? 230 GLN A N 1 ATOM 1673 C CA . GLN A 1 230 ? -8.545 5.775 27.226 1.00 31.75 ? 230 GLN A CA 1 ATOM 1674 C C . GLN A 1 230 ? -8.635 4.337 26.732 1.00 34.06 ? 230 GLN A C 1 ATOM 1675 O O . GLN A 1 230 ? -7.632 3.625 26.676 1.00 32.52 ? 230 GLN A O 1 ATOM 1676 C CB . GLN A 1 230 ? -8.641 6.734 26.028 1.00 34.64 ? 230 GLN A CB 1 ATOM 1677 C CG . GLN A 1 230 ? -7.389 6.760 25.165 1.00 37.21 ? 230 GLN A CG 1 ATOM 1678 C CD . GLN A 1 230 ? -6.372 7.785 25.615 1.00 40.79 ? 230 GLN A CD 1 ATOM 1679 O OE1 . GLN A 1 230 ? -5.258 7.453 26.036 1.00 41.24 ? 230 GLN A OE1 1 ATOM 1680 N NE2 . GLN A 1 230 ? -6.741 9.061 25.524 1.00 39.95 ? 230 GLN A NE2 1 ATOM 1681 N N . HIS A 1 231 ? -9.853 3.928 26.396 1.00 32.76 ? 231 HIS A N 1 ATOM 1682 C CA . HIS A 1 231 ? -10.078 2.594 25.860 1.00 35.13 ? 231 HIS A CA 1 ATOM 1683 C C . HIS A 1 231 ? -10.259 2.735 24.344 1.00 42.06 ? 231 HIS A C 1 ATOM 1684 O O . HIS A 1 231 ? -11.062 3.555 23.903 1.00 41.00 ? 231 HIS A O 1 ATOM 1685 C CB . HIS A 1 231 ? -11.271 1.890 26.498 1.00 38.02 ? 231 HIS A CB 1 ATOM 1686 C CG . HIS A 1 231 ? -11.273 0.419 26.169 1.00 38.81 ? 231 HIS A CG 1 ATOM 1687 N ND1 . HIS A 1 231 ? -11.681 -0.050 24.941 1.00 39.89 ? 231 HIS A ND1 1 ATOM 1688 C CD2 . HIS A 1 231 ? -10.902 -0.660 26.887 1.00 36.93 ? 231 HIS A CD2 1 ATOM 1689 C CE1 . HIS A 1 231 ? -11.568 -1.365 24.914 1.00 39.71 ? 231 HIS A CE1 1 ATOM 1690 N NE2 . HIS A 1 231 ? -11.095 -1.758 26.084 1.00 40.86 ? 231 HIS A NE2 1 ATOM 1691 N N . CYS A 1 232 ? -9.463 2.006 23.578 1.00 36.81 ? 232 CYS A N 1 ATOM 1692 C CA . CYS A 1 232 ? -9.507 2.108 22.119 1.00 35.06 ? 232 CYS A CA 1 ATOM 1693 C C . CYS A 1 232 ? -10.197 0.900 21.507 1.00 39.56 ? 232 CYS A C 1 ATOM 1694 O O . CYS A 1 232 ? -9.771 -0.240 21.687 1.00 34.74 ? 232 CYS A O 1 ATOM 1695 C CB . CYS A 1 232 ? -8.093 2.284 21.583 1.00 36.30 ? 232 CYS A CB 1 ATOM 1696 S SG . CYS A 1 232 ? -7.892 2.290 19.794 1.00 36.61 ? 232 CYS A SG 1 ATOM 1697 N N . LYS A 1 233 ? -11.282 1.163 20.784 1.00 43.66 ? 233 LYS A N 1 ATOM 1698 C CA . LYS A 1 233 ? -12.076 0.131 20.151 1.00 48.21 ? 233 LYS A CA 1 ATOM 1699 C C . LYS A 1 233 ? -11.278 -0.692 19.148 1.00 44.76 ? 233 LYS A C 1 ATOM 1700 O O . LYS A 1 233 ? -11.360 -1.923 19.158 1.00 50.17 ? 233 LYS A O 1 ATOM 1701 C CB . LYS A 1 233 ? -13.314 0.741 19.471 1.00 48.30 ? 233 LYS A CB 1 ATOM 1702 C CG . LYS A 1 233 ? -14.610 0.524 20.225 1.00 49.87 ? 233 LYS A CG 1 ATOM 1703 C CD . LYS A 1 233 ? -15.742 1.377 19.661 1.00 52.61 ? 233 LYS A CD 1 ATOM 1704 C CE . LYS A 1 233 ? -17.095 0.885 20.155 1.00 52.38 ? 233 LYS A CE 1 ATOM 1705 N NZ . LYS A 1 233 ? -18.226 1.526 19.420 1.00 51.61 ? 233 LYS A NZ 1 ATOM 1706 N N . LYS A 1 234 ? -10.516 -0.037 18.291 1.00 43.69 ? 234 LYS A N 1 ATOM 1707 C CA . LYS A 1 234 ? -9.718 -0.700 17.281 1.00 49.74 ? 234 LYS A CA 1 ATOM 1708 C C . LYS A 1 234 ? -8.635 -1.598 17.848 1.00 46.04 ? 234 LYS A C 1 ATOM 1709 O O . LYS A 1 234 ? -8.393 -2.686 17.309 1.00 50.13 ? 234 LYS A O 1 ATOM 1710 C CB . LYS A 1 234 ? -9.082 0.330 16.330 1.00 50.34 ? 234 LYS A CB 1 ATOM 1711 C CG . LYS A 1 234 ? -8.090 -0.278 15.355 1.00 53.83 ? 234 LYS A CG 1 ATOM 1712 C CD . LYS A 1 234 ? -8.114 0.420 14.007 1.00 54.81 ? 234 LYS A CD 1 ATOM 1713 C CE . LYS A 1 234 ? -8.216 1.929 14.151 1.00 55.79 ? 234 LYS A CE 1 ATOM 1714 N NZ . LYS A 1 234 ? -8.009 2.620 12.842 1.00 54.98 ? 234 LYS A NZ 1 ATOM 1715 N N . LEU A 1 235 ? -7.948 -1.151 18.896 1.00 33.59 ? 235 LEU A N 1 ATOM 1716 C CA . LEU A 1 235 ? -6.869 -1.951 19.466 1.00 33.04 ? 235 LEU A CA 1 ATOM 1717 C C . LEU A 1 235 ? -7.396 -2.900 20.532 1.00 29.03 ? 235 LEU A C 1 ATOM 1718 O O . LEU A 1 235 ? -6.644 -3.698 21.088 1.00 35.45 ? 235 LEU A O 1 ATOM 1719 C CB . LEU A 1 235 ? -5.781 -1.066 20.048 1.00 33.29 ? 235 LEU A CB 1 ATOM 1720 C CG . LEU A 1 235 ? -5.053 -0.083 19.145 1.00 28.52 ? 235 LEU A CG 1 ATOM 1721 C CD1 . LEU A 1 235 ? -3.901 0.578 19.892 1.00 26.58 ? 235 LEU A CD1 1 ATOM 1722 C CD2 . LEU A 1 235 ? -4.530 -0.770 17.893 1.00 32.62 ? 235 LEU A CD2 1 ATOM 1723 N N . SER A 1 236 ? -8.686 -2.791 20.833 1.00 36.52 ? 236 SER A N 1 ATOM 1724 C CA . SER A 1 236 ? -9.294 -3.620 21.870 1.00 35.03 ? 236 SER A CA 1 ATOM 1725 C C . SER A 1 236 ? -8.424 -3.568 23.126 1.00 35.09 ? 236 SER A C 1 ATOM 1726 O O . SER A 1 236 ? -8.174 -4.584 23.770 1.00 40.14 ? 236 SER A O 1 ATOM 1727 C CB . SER A 1 236 ? -9.477 -5.053 21.398 1.00 36.24 ? 236 SER A CB 1 ATOM 1728 O OG . SER A 1 236 ? -10.555 -5.164 20.487 1.00 39.15 ? 236 SER A OG 1 ATOM 1729 N N . SER A 1 237 ? -7.957 -2.363 23.456 1.00 29.40 ? 237 SER A N 1 ATOM 1730 C CA . SER A 1 237 ? -7.097 -2.178 24.605 1.00 26.43 ? 237 SER A CA 1 ATOM 1731 C C . SER A 1 237 ? -7.264 -0.827 25.292 1.00 26.26 ? 237 SER A C 1 ATOM 1732 O O . SER A 1 237 ? -7.691 0.146 24.684 1.00 27.48 ? 237 SER A O 1 ATOM 1733 C CB . SER A 1 237 ? -5.616 -2.227 24.114 1.00 24.36 ? 237 SER A CB 1 ATOM 1734 O OG . SER A 1 237 ? -5.444 -3.349 23.256 1.00 25.81 ? 237 SER A OG 1 ATOM 1735 N N . TRP A 1 238 ? -6.849 -0.785 26.555 1.00 22.12 ? 238 TRP A N 1 ATOM 1736 C CA . TRP A 1 238 ? -6.730 0.478 27.278 1.00 27.70 ? 238 TRP A CA 1 ATOM 1737 C C . TRP A 1 238 ? -5.355 1.046 26.850 1.00 29.64 ? 238 TRP A C 1 ATOM 1738 O O . TRP A 1 238 ? -4.415 0.264 26.678 1.00 27.93 ? 238 TRP A O 1 ATOM 1739 C CB . TRP A 1 238 ? -6.726 0.285 28.784 1.00 26.60 ? 238 TRP A CB 1 ATOM 1740 C CG . TRP A 1 238 ? -8.098 0.181 29.380 1.00 32.69 ? 238 TRP A CG 1 ATOM 1741 C CD1 . TRP A 1 238 ? -8.788 -0.945 29.693 1.00 32.84 ? 238 TRP A CD1 1 ATOM 1742 C CD2 . TRP A 1 238 ? -8.944 1.288 29.733 1.00 31.06 ? 238 TRP A CD2 1 ATOM 1743 N NE1 . TRP A 1 238 ? -10.017 -0.615 30.218 1.00 36.65 ? 238 TRP A NE1 1 ATOM 1744 C CE2 . TRP A 1 238 ? -10.131 0.750 30.253 1.00 33.90 ? 238 TRP A CE2 1 ATOM 1745 C CE3 . TRP A 1 238 ? -8.795 2.677 29.655 1.00 31.39 ? 238 TRP A CE3 1 ATOM 1746 C CZ2 . TRP A 1 238 ? -11.183 1.554 30.700 1.00 32.70 ? 238 TRP A CZ2 1 ATOM 1747 C CZ3 . TRP A 1 238 ? -9.842 3.472 30.099 1.00 32.32 ? 238 TRP A CZ3 1 ATOM 1748 C CH2 . TRP A 1 238 ? -11.014 2.904 30.613 1.00 30.24 ? 238 TRP A CH2 1 ATOM 1749 N N . VAL A 1 239 ? -5.276 2.344 26.684 1.00 27.05 ? 239 VAL A N 1 ATOM 1750 C CA . VAL A 1 239 ? -4.016 2.967 26.266 1.00 22.20 ? 239 VAL A CA 1 ATOM 1751 C C . VAL A 1 239 ? -3.655 4.108 27.201 1.00 21.53 ? 239 VAL A C 1 ATOM 1752 O O . VAL A 1 239 ? -4.386 5.088 27.321 1.00 19.79 ? 239 VAL A O 1 ATOM 1753 C CB . VAL A 1 239 ? -4.130 3.447 24.811 1.00 21.37 ? 239 VAL A CB 1 ATOM 1754 C CG1 . VAL A 1 239 ? -2.800 3.979 24.312 1.00 20.42 ? 239 VAL A CG1 1 ATOM 1755 C CG2 . VAL A 1 239 ? -4.636 2.296 23.940 1.00 23.09 ? 239 VAL A CG2 1 ATOM 1756 N N . LEU A 1 240 ? -2.520 3.974 27.874 1.00 16.74 ? 240 LEU A N 1 ATOM 1757 C CA . LEU A 1 240 ? -2.054 4.940 28.848 1.00 20.35 ? 240 LEU A CA 1 ATOM 1758 C C . LEU A 1 240 ? -0.741 5.594 28.450 1.00 21.32 ? 240 LEU A C 1 ATOM 1759 O O . LEU A 1 240 ? 0.222 4.906 28.087 1.00 19.62 ? 240 LEU A O 1 ATOM 1760 C CB . LEU A 1 240 ? -1.891 4.220 30.201 1.00 19.33 ? 240 LEU A CB 1 ATOM 1761 C CG . LEU A 1 240 ? -1.090 4.915 31.292 1.00 20.76 ? 240 LEU A CG 1 ATOM 1762 C CD1 . LEU A 1 240 ? -1.835 6.128 31.842 1.00 19.05 ? 240 LEU A CD1 1 ATOM 1763 C CD2 . LEU A 1 240 ? -0.780 3.934 32.429 1.00 19.61 ? 240 LEU A CD2 1 ATOM 1764 N N . LEU A 1 241 ? -0.699 6.912 28.520 1.00 20.73 ? 241 LEU A N 1 ATOM 1765 C CA . LEU A 1 241 ? 0.470 7.708 28.216 1.00 21.73 ? 241 LEU A CA 1 ATOM 1766 C C . LEU A 1 241 ? 0.940 8.491 29.439 1.00 20.24 ? 241 LEU A C 1 ATOM 1767 O O . LEU A 1 241 ? 0.186 9.277 30.018 1.00 20.47 ? 241 LEU A O 1 ATOM 1768 C CB . LEU A 1 241 ? 0.181 8.708 27.079 1.00 21.97 ? 241 LEU A CB 1 ATOM 1769 C CG . LEU A 1 241 ? 0.113 8.117 25.667 1.00 25.79 ? 241 LEU A CG 1 ATOM 1770 C CD1 . LEU A 1 241 ? -1.216 7.405 25.445 1.00 27.21 ? 241 LEU A CD1 1 ATOM 1771 C CD2 . LEU A 1 241 ? 0.324 9.196 24.618 1.00 23.30 ? 241 LEU A CD2 1 ATOM 1772 N N . MET A 1 242 ? 2.193 8.298 29.835 1.00 22.70 ? 242 MET A N 1 ATOM 1773 C CA . MET A 1 242 ? 2.754 9.017 30.979 1.00 23.98 ? 242 MET A CA 1 ATOM 1774 C C . MET A 1 242 ? 4.101 9.614 30.590 1.00 24.45 ? 242 MET A C 1 ATOM 1775 O O . MET A 1 242 ? 4.928 8.913 29.998 1.00 20.68 ? 242 MET A O 1 ATOM 1776 C CB . MET A 1 242 ? 2.890 8.117 32.205 1.00 25.10 ? 242 MET A CB 1 ATOM 1777 C CG . MET A 1 242 ? 1.550 7.703 32.807 1.00 26.61 ? 242 MET A CG 1 ATOM 1778 S SD . MET A 1 242 ? 1.711 6.963 34.440 1.00 28.28 ? 242 MET A SD 1 ATOM 1779 C CE . MET A 1 242 ? 2.884 5.659 34.133 1.00 27.92 ? 242 MET A CE 1 ATOM 1780 N N . LYS A 1 243 ? 4.304 10.891 30.899 1.00 22.00 ? 243 LYS A N 1 ATOM 1781 C CA . LYS A 1 243 ? 5.545 11.558 30.537 1.00 27.20 ? 243 LYS A CA 1 ATOM 1782 C C . LYS A 1 243 ? 6.645 11.422 31.576 1.00 23.44 ? 243 LYS A C 1 ATOM 1783 O O . LYS A 1 243 ? 6.410 11.428 32.780 1.00 32.62 ? 243 LYS A O 1 ATOM 1784 C CB . LYS A 1 243 ? 5.294 13.045 30.251 1.00 26.36 ? 243 LYS A CB 1 ATOM 1785 C CG . LYS A 1 243 ? 4.254 13.315 29.173 1.00 28.20 ? 243 LYS A CG 1 ATOM 1786 C CD . LYS A 1 243 ? 4.116 14.822 28.963 1.00 33.49 ? 243 LYS A CD 1 ATOM 1787 C CE . LYS A 1 243 ? 2.920 15.171 28.101 1.00 36.76 ? 243 LYS A CE 1 ATOM 1788 N NZ . LYS A 1 243 ? 2.485 16.586 28.328 1.00 41.78 ? 243 LYS A NZ 1 ATOM 1789 N N . TYR A 1 244 ? 7.876 11.326 31.095 1.00 29.55 ? 244 TYR A N 1 ATOM 1790 C CA . TYR A 1 244 ? 9.059 11.217 31.924 1.00 27.40 ? 244 TYR A CA 1 ATOM 1791 C C . TYR A 1 244 ? 9.785 12.575 31.970 1.00 34.37 ? 244 TYR A C 1 ATOM 1792 O O . TYR A 1 244 ? 9.760 13.287 30.964 1.00 33.86 ? 244 TYR A O 1 ATOM 1793 C CB . TYR A 1 244 ? 10.065 10.244 31.315 1.00 30.14 ? 244 TYR A CB 1 ATOM 1794 C CG . TYR A 1 244 ? 9.784 8.777 31.411 1.00 27.60 ? 244 TYR A CG 1 ATOM 1795 C CD1 . TYR A 1 244 ? 9.788 8.116 32.634 1.00 28.16 ? 244 TYR A CD1 1 ATOM 1796 C CD2 . TYR A 1 244 ? 9.539 8.027 30.263 1.00 29.79 ? 244 TYR A CD2 1 ATOM 1797 C CE1 . TYR A 1 244 ? 9.541 6.756 32.710 1.00 28.47 ? 244 TYR A CE1 1 ATOM 1798 C CE2 . TYR A 1 244 ? 9.289 6.674 30.335 1.00 27.11 ? 244 TYR A CE2 1 ATOM 1799 C CZ . TYR A 1 244 ? 9.294 6.045 31.561 1.00 27.51 ? 244 TYR A CZ 1 ATOM 1800 O OH . TYR A 1 244 ? 9.047 4.691 31.625 1.00 31.30 ? 244 TYR A OH 1 ATOM 1801 N N . LEU A 1 245 ? 10.449 12.856 33.087 1.00 34.95 ? 245 LEU A N 1 ATOM 1802 C CA . LEU A 1 245 ? 11.249 14.097 33.120 1.00 39.82 ? 245 LEU A CA 1 ATOM 1803 C C . LEU A 1 245 ? 12.240 13.972 31.950 1.00 41.63 ? 245 LEU A C 1 ATOM 1804 O O . LEU A 1 245 ? 12.896 12.938 31.819 1.00 43.16 ? 245 LEU A O 1 ATOM 1805 C CB . LEU A 1 245 ? 11.990 14.272 34.423 1.00 39.78 ? 245 LEU A CB 1 ATOM 1806 C CG . LEU A 1 245 ? 11.272 14.982 35.571 1.00 40.07 ? 245 LEU A CG 1 ATOM 1807 C CD1 . LEU A 1 245 ? 10.605 16.257 35.075 1.00 40.95 ? 245 LEU A CD1 1 ATOM 1808 C CD2 . LEU A 1 245 ? 10.270 14.060 36.237 1.00 41.53 ? 245 LEU A CD2 1 ATOM 1809 N N . GLY A 1 246 ? 12.308 14.995 31.124 1.00 44.34 ? 246 GLY A N 1 ATOM 1810 C CA . GLY A 1 246 ? 13.197 14.955 29.955 1.00 44.59 ? 246 GLY A CA 1 ATOM 1811 C C . GLY A 1 246 ? 12.303 14.978 28.708 1.00 46.38 ? 246 GLY A C 1 ATOM 1812 O O . GLY A 1 246 ? 11.183 15.489 28.783 1.00 51.30 ? 246 GLY A O 1 ATOM 1813 N N . ASN A 1 247 ? 12.777 14.418 27.609 1.00 48.24 ? 247 ASN A N 1 ATOM 1814 C CA . ASN A 1 247 ? 11.993 14.430 26.376 1.00 50.06 ? 247 ASN A CA 1 ATOM 1815 C C . ASN A 1 247 ? 11.397 13.087 26.020 1.00 46.46 ? 247 ASN A C 1 ATOM 1816 O O . ASN A 1 247 ? 11.388 12.744 24.828 1.00 46.27 ? 247 ASN A O 1 ATOM 1817 C CB . ASN A 1 247 ? 12.901 14.913 25.224 1.00 51.22 ? 247 ASN A CB 1 ATOM 1818 C CG . ASN A 1 247 ? 14.235 14.188 25.217 1.00 52.72 ? 247 ASN A CG 1 ATOM 1819 O OD1 . ASN A 1 247 ? 15.039 14.332 26.139 1.00 53.61 ? 247 ASN A OD1 1 ATOM 1820 N ND2 . ASN A 1 247 ? 14.479 13.403 24.176 1.00 52.79 ? 247 ASN A ND2 1 ATOM 1821 N N . ALA A 1 248 ? 10.885 12.328 26.992 1.00 38.01 ? 248 ALA A N 1 ATOM 1822 C CA . ALA A 1 248 ? 10.336 11.014 26.690 1.00 35.06 ? 248 ALA A CA 1 ATOM 1823 C C . ALA A 1 248 ? 8.942 10.756 27.238 1.00 32.88 ? 248 ALA A C 1 ATOM 1824 O O . ALA A 1 248 ? 8.513 11.292 28.256 1.00 29.97 ? 248 ALA A O 1 ATOM 1825 C CB . ALA A 1 248 ? 11.293 9.931 27.187 1.00 34.29 ? 248 ALA A CB 1 ATOM 1826 N N . THR A 1 249 ? 8.225 9.874 26.538 1.00 27.58 ? 249 THR A N 1 ATOM 1827 C CA . THR A 1 249 ? 6.873 9.495 26.902 1.00 26.38 ? 249 THR A CA 1 ATOM 1828 C C . THR A 1 249 ? 6.632 7.999 26.781 1.00 21.54 ? 249 THR A C 1 ATOM 1829 O O . THR A 1 249 ? 6.900 7.376 25.750 1.00 25.12 ? 249 THR A O 1 ATOM 1830 C CB . THR A 1 249 ? 5.838 10.251 26.043 1.00 26.30 ? 249 THR A CB 1 ATOM 1831 O OG1 . THR A 1 249 ? 6.007 11.661 26.249 1.00 27.77 ? 249 THR A OG1 1 ATOM 1832 C CG2 . THR A 1 249 ? 4.421 9.864 26.426 1.00 26.82 ? 249 THR A CG2 1 ATOM 1833 N N . ALA A 1 250 ? 6.109 7.405 27.849 1.00 20.32 ? 250 ALA A N 1 ATOM 1834 C CA . ALA A 1 250 ? 5.797 5.983 27.865 1.00 18.74 ? 250 ALA A CA 1 ATOM 1835 C C . ALA A 1 250 ? 4.337 5.745 27.473 1.00 17.70 ? 250 ALA A C 1 ATOM 1836 O O . ALA A 1 250 ? 3.443 6.438 27.944 1.00 19.05 ? 250 ALA A O 1 ATOM 1837 C CB . ALA A 1 250 ? 6.046 5.406 29.256 1.00 18.12 ? 250 ALA A CB 1 ATOM 1838 N N . ILE A 1 251 ? 4.107 4.756 26.617 1.00 17.14 ? 251 ILE A N 1 ATOM 1839 C CA . ILE A 1 251 ? 2.768 4.379 26.205 1.00 16.86 ? 251 ILE A CA 1 ATOM 1840 C C . ILE A 1 251 ? 2.509 2.912 26.564 1.00 21.29 ? 251 ILE A C 1 ATOM 1841 O O . ILE A 1 251 ? 3.202 2.016 26.073 1.00 21.69 ? 251 ILE A O 1 ATOM 1842 C CB . ILE A 1 251 ? 2.531 4.579 24.700 1.00 19.99 ? 251 ILE A CB 1 ATOM 1843 C CG1 . ILE A 1 251 ? 3.104 5.927 24.245 1.00 23.01 ? 251 ILE A CG1 1 ATOM 1844 C CG2 . ILE A 1 251 ? 1.051 4.494 24.378 1.00 20.09 ? 251 ILE A CG2 1 ATOM 1845 C CD1 . ILE A 1 251 ? 2.885 6.218 22.776 1.00 23.29 ? 251 ILE A CD1 1 ATOM 1846 N N . PHE A 1 252 ? 1.516 2.668 27.413 1.00 13.82 ? 252 PHE A N 1 ATOM 1847 C CA . PHE A 1 252 ? 1.168 1.318 27.829 1.00 14.75 ? 252 PHE A CA 1 ATOM 1848 C C . PHE A 1 252 ? -0.125 0.854 27.175 1.00 18.59 ? 252 PHE A C 1 ATOM 1849 O O . PHE A 1 252 ? -1.104 1.613 27.167 1.00 19.46 ? 252 PHE A O 1 ATOM 1850 C CB . PHE A 1 252 ? 1.074 1.254 29.361 1.00 14.44 ? 252 PHE A CB 1 ATOM 1851 C CG . PHE A 1 252 ? 2.328 1.640 30.087 1.00 20.24 ? 252 PHE A CG 1 ATOM 1852 C CD1 . PHE A 1 252 ? 3.277 0.690 30.433 1.00 22.32 ? 252 PHE A CD1 1 ATOM 1853 C CD2 . PHE A 1 252 ? 2.566 2.958 30.441 1.00 17.96 ? 252 PHE A CD2 1 ATOM 1854 C CE1 . PHE A 1 252 ? 4.435 1.045 31.098 1.00 18.76 ? 252 PHE A CE1 1 ATOM 1855 C CE2 . PHE A 1 252 ? 3.715 3.323 31.109 1.00 19.89 ? 252 PHE A CE2 1 ATOM 1856 C CZ . PHE A 1 252 ? 4.647 2.361 31.443 1.00 22.43 ? 252 PHE A CZ 1 ATOM 1857 N N . PHE A 1 253 ? -0.147 -0.321 26.555 1.00 15.03 ? 253 PHE A N 1 ATOM 1858 C CA . PHE A 1 253 ? -1.332 -0.877 25.933 1.00 15.69 ? 253 PHE A CA 1 ATOM 1859 C C . PHE A 1 253 ? -1.796 -2.143 26.680 1.00 26.54 ? 253 PHE A C 1 ATOM 1860 O O . PHE A 1 253 ? -1.094 -3.164 26.672 1.00 24.06 ? 253 PHE A O 1 ATOM 1861 C CB . PHE A 1 253 ? -1.136 -1.279 24.465 1.00 17.60 ? 253 PHE A CB 1 ATOM 1862 C CG . PHE A 1 253 ? -0.518 -0.197 23.614 1.00 19.40 ? 253 PHE A CG 1 ATOM 1863 C CD1 . PHE A 1 253 ? -1.306 0.615 22.827 1.00 24.77 ? 253 PHE A CD1 1 ATOM 1864 C CD2 . PHE A 1 253 ? 0.853 -0.004 23.618 1.00 22.97 ? 253 PHE A CD2 1 ATOM 1865 C CE1 . PHE A 1 253 ? -0.755 1.620 22.055 1.00 22.76 ? 253 PHE A CE1 1 ATOM 1866 C CE2 . PHE A 1 253 ? 1.422 0.990 22.835 1.00 26.82 ? 253 PHE A CE2 1 ATOM 1867 C CZ . PHE A 1 253 ? 0.619 1.799 22.060 1.00 26.59 ? 253 PHE A CZ 1 ATOM 1868 N N . LEU A 1 254 ? -2.966 -2.087 27.288 1.00 23.31 ? 254 LEU A N 1 ATOM 1869 C CA . LEU A 1 254 ? -3.534 -3.218 28.021 1.00 20.80 ? 254 LEU A CA 1 ATOM 1870 C C . LEU A 1 254 ? -4.662 -3.855 27.215 1.00 24.15 ? 254 LEU A C 1 ATOM 1871 O O . LEU A 1 254 ? -5.767 -3.302 27.161 1.00 26.60 ? 254 LEU A O 1 ATOM 1872 C CB . LEU A 1 254 ? -4.135 -2.714 29.349 1.00 24.92 ? 254 LEU A CB 1 ATOM 1873 C CG . LEU A 1 254 ? -4.733 -3.814 30.246 1.00 23.56 ? 254 LEU A CG 1 ATOM 1874 C CD1 . LEU A 1 254 ? -3.609 -4.607 30.894 1.00 22.56 ? 254 LEU A CD1 1 ATOM 1875 C CD2 . LEU A 1 254 ? -5.656 -3.205 31.297 1.00 25.84 ? 254 LEU A CD2 1 ATOM 1876 N N . PRO A 1 255 ? -4.400 -4.981 26.580 1.00 26.29 ? 255 PRO A N 1 ATOM 1877 C CA . PRO A 1 255 ? -5.377 -5.663 25.766 1.00 27.12 ? 255 PRO A CA 1 ATOM 1878 C C . PRO A 1 255 ? -6.530 -6.257 26.556 1.00 27.34 ? 255 PRO A C 1 ATOM 1879 O O . PRO A 1 255 ? -6.352 -6.719 27.680 1.00 27.39 ? 255 PRO A O 1 ATOM 1880 C CB . PRO A 1 255 ? -4.577 -6.779 25.090 1.00 27.78 ? 255 PRO A CB 1 ATOM 1881 C CG . PRO A 1 255 ? -3.434 -7.026 26.011 1.00 27.65 ? 255 PRO A CG 1 ATOM 1882 C CD . PRO A 1 255 ? -3.089 -5.684 26.599 1.00 18.46 ? 255 PRO A CD 1 ATOM 1883 N N . ASP A 1 256 ? -7.716 -6.235 25.954 1.00 32.28 ? 256 ASP A N 1 ATOM 1884 C CA . ASP A 1 256 ? -8.902 -6.816 26.574 1.00 39.85 ? 256 ASP A CA 1 ATOM 1885 C C . ASP A 1 256 ? -8.698 -8.338 26.640 1.00 41.75 ? 256 ASP A C 1 ATOM 1886 O O . ASP A 1 256 ? -7.709 -8.831 26.093 1.00 41.90 ? 256 ASP A O 1 ATOM 1887 C CB . ASP A 1 256 ? -10.154 -6.526 25.756 1.00 39.59 ? 256 ASP A CB 1 ATOM 1888 C CG . ASP A 1 256 ? -10.573 -5.078 25.719 1.00 39.26 ? 256 ASP A CG 1 ATOM 1889 O OD1 . ASP A 1 256 ? -10.283 -4.329 26.675 1.00 39.65 ? 256 ASP A OD1 1 ATOM 1890 O OD2 . ASP A 1 256 ? -11.212 -4.672 24.719 1.00 38.25 ? 256 ASP A OD2 1 ATOM 1891 N N . GLU A 1 257 ? -9.615 -9.038 27.285 1.00 44.12 ? 257 GLU A N 1 ATOM 1892 C CA . GLU A 1 257 ? -9.517 -10.491 27.394 1.00 46.98 ? 257 GLU A CA 1 ATOM 1893 C C . GLU A 1 257 ? -9.310 -11.117 26.014 1.00 41.18 ? 257 GLU A C 1 ATOM 1894 O O . GLU A 1 257 ? -10.135 -10.922 25.120 1.00 39.03 ? 257 GLU A O 1 ATOM 1895 C CB . GLU A 1 257 ? -10.782 -11.081 28.018 1.00 48.02 ? 257 GLU A CB 1 ATOM 1896 C CG . GLU A 1 257 ? -10.813 -11.108 29.533 1.00 52.39 ? 257 GLU A CG 1 ATOM 1897 C CD . GLU A 1 257 ? -11.831 -12.096 30.079 1.00 54.15 ? 257 GLU A CD 1 ATOM 1898 O OE1 . GLU A 1 257 ? -13.038 -11.931 29.802 1.00 54.22 ? 257 GLU A OE1 1 ATOM 1899 O OE2 . GLU A 1 257 ? -11.423 -13.043 30.784 1.00 56.03 ? 257 GLU A OE2 1 ATOM 1900 N N . GLY A 1 258 ? -8.233 -11.867 25.854 1.00 38.90 ? 258 GLY A N 1 ATOM 1901 C CA . GLY A 1 258 ? -7.915 -12.537 24.614 1.00 40.57 ? 258 GLY A CA 1 ATOM 1902 C C . GLY A 1 258 ? -7.648 -11.634 23.433 1.00 43.09 ? 258 GLY A C 1 ATOM 1903 O O . GLY A 1 258 ? -7.872 -12.051 22.281 1.00 40.51 ? 258 GLY A O 1 ATOM 1904 N N . LYS A 1 259 ? -7.143 -10.419 23.650 1.00 38.16 ? 259 LYS A N 1 ATOM 1905 C CA . LYS A 1 259 ? -6.879 -9.519 22.529 1.00 36.61 ? 259 LYS A CA 1 ATOM 1906 C C . LYS A 1 259 ? -5.421 -9.129 22.386 1.00 34.80 ? 259 LYS A C 1 ATOM 1907 O O . LYS A 1 259 ? -5.107 -8.222 21.592 1.00 36.43 ? 259 LYS A O 1 ATOM 1908 C CB . LYS A 1 259 ? -7.746 -8.259 22.639 1.00 38.98 ? 259 LYS A CB 1 ATOM 1909 C CG . LYS A 1 259 ? -9.239 -8.522 22.613 1.00 41.63 ? 259 LYS A CG 1 ATOM 1910 C CD . LYS A 1 259 ? -9.741 -8.766 21.196 1.00 45.27 ? 259 LYS A CD 1 ATOM 1911 C CE . LYS A 1 259 ? -11.206 -9.182 21.208 1.00 45.92 ? 259 LYS A CE 1 ATOM 1912 N NZ . LYS A 1 259 ? -11.748 -9.356 19.834 1.00 47.26 ? 259 LYS A NZ 1 ATOM 1913 N N . LEU A 1 260 ? -4.513 -9.773 23.106 1.00 28.16 ? 260 LEU A N 1 ATOM 1914 C CA . LEU A 1 260 ? -3.099 -9.424 23.001 1.00 32.10 ? 260 LEU A CA 1 ATOM 1915 C C . LEU A 1 260 ? -2.595 -9.512 21.564 1.00 31.40 ? 260 LEU A C 1 ATOM 1916 O O . LEU A 1 260 ? -1.993 -8.566 21.051 1.00 30.22 ? 260 LEU A O 1 ATOM 1917 C CB . LEU A 1 260 ? -2.234 -10.290 23.914 1.00 30.81 ? 260 LEU A CB 1 ATOM 1918 C CG . LEU A 1 260 ? -0.718 -10.136 23.687 1.00 32.42 ? 260 LEU A CG 1 ATOM 1919 C CD1 . LEU A 1 260 ? -0.298 -8.693 23.880 1.00 31.12 ? 260 LEU A CD1 1 ATOM 1920 C CD2 . LEU A 1 260 ? 0.060 -11.062 24.605 1.00 32.76 ? 260 LEU A CD2 1 ATOM 1921 N N . GLN A 1 261 ? -2.829 -10.647 20.917 1.00 32.40 ? 261 GLN A N 1 ATOM 1922 C CA . GLN A 1 261 ? -2.397 -10.860 19.544 1.00 38.69 ? 261 GLN A CA 1 ATOM 1923 C C . GLN A 1 261 ? -3.005 -9.824 18.605 1.00 37.96 ? 261 GLN A C 1 ATOM 1924 O O . GLN A 1 261 ? -2.330 -9.312 17.715 1.00 35.85 ? 261 GLN A O 1 ATOM 1925 C CB . GLN A 1 261 ? -2.764 -12.270 19.069 1.00 40.52 ? 261 GLN A CB 1 ATOM 1926 C CG . GLN A 1 261 ? -2.192 -12.607 17.695 1.00 43.10 ? 261 GLN A CG 1 ATOM 1927 C CD . GLN A 1 261 ? -0.685 -12.778 17.747 1.00 44.55 ? 261 GLN A CD 1 ATOM 1928 O OE1 . GLN A 1 261 ? -0.184 -13.688 18.411 1.00 46.58 ? 261 GLN A OE1 1 ATOM 1929 N NE2 . GLN A 1 261 ? 0.038 -11.908 17.055 1.00 43.84 ? 261 GLN A NE2 1 ATOM 1930 N N . HIS A 1 262 ? -4.285 -9.527 18.810 1.00 36.53 ? 262 HIS A N 1 ATOM 1931 C CA . HIS A 1 262 ? -4.971 -8.531 17.983 1.00 37.61 ? 262 HIS A CA 1 ATOM 1932 C C . HIS A 1 262 ? -4.266 -7.179 18.126 1.00 37.68 ? 262 HIS A C 1 ATOM 1933 O O . HIS A 1 262 ? -3.965 -6.491 17.154 1.00 32.82 ? 262 HIS A O 1 ATOM 1934 C CB . HIS A 1 262 ? -6.429 -8.417 18.419 1.00 38.85 ? 262 HIS A CB 1 ATOM 1935 C CG . HIS A 1 262 ? -7.193 -7.332 17.732 1.00 41.39 ? 262 HIS A CG 1 ATOM 1936 N ND1 . HIS A 1 262 ? -7.642 -7.441 16.438 1.00 41.41 ? 262 HIS A ND1 1 ATOM 1937 C CD2 . HIS A 1 262 ? -7.587 -6.107 18.167 1.00 41.94 ? 262 HIS A CD2 1 ATOM 1938 C CE1 . HIS A 1 262 ? -8.282 -6.336 16.098 1.00 41.59 ? 262 HIS A CE1 1 ATOM 1939 N NE2 . HIS A 1 262 ? -8.262 -5.511 17.128 1.00 41.78 ? 262 HIS A NE2 1 ATOM 1940 N N . LEU A 1 263 ? -3.990 -6.830 19.373 1.00 34.61 ? 263 LEU A N 1 ATOM 1941 C CA . LEU A 1 263 ? -3.309 -5.592 19.730 1.00 31.41 ? 263 LEU A CA 1 ATOM 1942 C C . LEU A 1 263 ? -1.964 -5.487 19.014 1.00 30.88 ? 263 LEU A C 1 ATOM 1943 O O . LEU A 1 263 ? -1.604 -4.441 18.475 1.00 28.68 ? 263 LEU A O 1 ATOM 1944 C CB . LEU A 1 263 ? -3.090 -5.583 21.243 1.00 30.21 ? 263 LEU A CB 1 ATOM 1945 C CG . LEU A 1 263 ? -2.628 -4.313 21.932 1.00 30.32 ? 263 LEU A CG 1 ATOM 1946 C CD1 . LEU A 1 263 ? -1.628 -4.634 23.040 1.00 29.26 ? 263 LEU A CD1 1 ATOM 1947 C CD2 . LEU A 1 263 ? -2.066 -3.286 20.980 1.00 29.21 ? 263 LEU A CD2 1 ATOM 1948 N N . GLU A 1 264 ? -1.215 -6.589 19.017 1.00 31.18 ? 264 GLU A N 1 ATOM 1949 C CA . GLU A 1 264 ? 0.091 -6.611 18.371 1.00 33.32 ? 264 GLU A CA 1 ATOM 1950 C C . GLU A 1 264 ? -0.017 -6.401 16.866 1.00 34.38 ? 264 GLU A C 1 ATOM 1951 O O . GLU A 1 264 ? 0.764 -5.635 16.294 1.00 32.01 ? 264 GLU A O 1 ATOM 1952 C CB . GLU A 1 264 ? 0.838 -7.906 18.693 1.00 32.09 ? 264 GLU A CB 1 ATOM 1953 C CG . GLU A 1 264 ? 1.216 -8.044 20.162 1.00 32.47 ? 264 GLU A CG 1 ATOM 1954 C CD . GLU A 1 264 ? 1.870 -9.368 20.492 1.00 34.35 ? 264 GLU A CD 1 ATOM 1955 O OE1 . GLU A 1 264 ? 1.495 -10.387 19.877 1.00 34.51 ? 264 GLU A OE1 1 ATOM 1956 O OE2 . GLU A 1 264 ? 2.762 -9.401 21.370 1.00 34.30 ? 264 GLU A OE2 1 ATOM 1957 N N . ASN A 1 265 ? -0.978 -7.051 16.225 1.00 35.91 ? 265 ASN A N 1 ATOM 1958 C CA . ASN A 1 265 ? -1.175 -6.952 14.793 1.00 38.28 ? 265 ASN A CA 1 ATOM 1959 C C . ASN A 1 265 ? -1.667 -5.579 14.346 1.00 37.97 ? 265 ASN A C 1 ATOM 1960 O O . ASN A 1 265 ? -1.222 -5.062 13.320 1.00 38.84 ? 265 ASN A O 1 ATOM 1961 C CB . ASN A 1 265 ? -2.207 -7.987 14.312 1.00 38.18 ? 265 ASN A CB 1 ATOM 1962 C CG . ASN A 1 265 ? -1.839 -9.417 14.595 1.00 39.25 ? 265 ASN A CG 1 ATOM 1963 O OD1 . ASN A 1 265 ? -0.704 -9.739 14.955 1.00 38.92 ? 265 ASN A OD1 1 ATOM 1964 N ND2 . ASN A 1 265 ? -2.815 -10.313 14.436 1.00 37.47 ? 265 ASN A ND2 1 ATOM 1965 N N . GLU A 1 266 ? -2.593 -4.999 15.098 1.00 38.21 ? 266 GLU A N 1 ATOM 1966 C CA . GLU A 1 266 ? -3.185 -3.722 14.771 1.00 40.03 ? 266 GLU A CA 1 ATOM 1967 C C . GLU A 1 266 ? -2.347 -2.494 15.023 1.00 36.38 ? 266 GLU A C 1 ATOM 1968 O O . GLU A 1 266 ? -2.715 -1.424 14.507 1.00 37.94 ? 266 GLU A O 1 ATOM 1969 C CB . GLU A 1 266 ? -4.545 -3.578 15.486 1.00 41.77 ? 266 GLU A CB 1 ATOM 1970 C CG . GLU A 1 266 ? -5.523 -4.686 15.116 1.00 45.76 ? 266 GLU A CG 1 ATOM 1971 C CD . GLU A 1 266 ? -5.912 -4.647 13.652 1.00 48.36 ? 266 GLU A CD 1 ATOM 1972 O OE1 . GLU A 1 266 ? -6.349 -3.574 13.182 1.00 51.06 ? 266 GLU A OE1 1 ATOM 1973 O OE2 . GLU A 1 266 ? -5.783 -5.683 12.968 1.00 49.02 ? 266 GLU A OE2 1 ATOM 1974 N N . LEU A 1 267 ? -1.256 -2.565 15.781 1.00 33.11 ? 267 LEU A N 1 ATOM 1975 C CA . LEU A 1 267 ? -0.451 -1.377 16.030 1.00 31.84 ? 267 LEU A CA 1 ATOM 1976 C C . LEU A 1 267 ? 0.155 -0.837 14.734 1.00 34.91 ? 267 LEU A C 1 ATOM 1977 O O . LEU A 1 267 ? 0.564 -1.610 13.875 1.00 40.87 ? 267 LEU A O 1 ATOM 1978 C CB . LEU A 1 267 ? 0.661 -1.603 17.034 1.00 30.97 ? 267 LEU A CB 1 ATOM 1979 C CG . LEU A 1 267 ? 0.342 -1.563 18.528 1.00 28.45 ? 267 LEU A CG 1 ATOM 1980 C CD1 . LEU A 1 267 ? 1.598 -1.856 19.336 1.00 27.78 ? 267 LEU A CD1 1 ATOM 1981 C CD2 . LEU A 1 267 ? -0.221 -0.203 18.928 1.00 28.55 ? 267 LEU A CD2 1 ATOM 1982 N N . THR A 1 268 ? 0.249 0.478 14.642 1.00 29.93 ? 268 THR A N 1 ATOM 1983 C CA . THR A 1 268 ? 0.829 1.145 13.483 1.00 36.07 ? 268 THR A CA 1 ATOM 1984 C C . THR A 1 268 ? 1.371 2.513 13.900 1.00 28.47 ? 268 THR A C 1 ATOM 1985 O O . THR A 1 268 ? 0.930 3.066 14.918 1.00 28.84 ? 268 THR A O 1 ATOM 1986 C CB . THR A 1 268 ? -0.152 1.357 12.313 1.00 35.33 ? 268 THR A CB 1 ATOM 1987 O OG1 . THR A 1 268 ? -1.162 2.299 12.677 1.00 34.73 ? 268 THR A OG1 1 ATOM 1988 C CG2 . THR A 1 268 ? -0.818 0.070 11.880 1.00 36.36 ? 268 THR A CG2 1 ATOM 1989 N N . HIS A 1 269 ? 2.298 3.055 13.127 1.00 28.78 ? 269 HIS A N 1 ATOM 1990 C CA . HIS A 1 269 ? 2.856 4.364 13.436 1.00 30.18 ? 269 HIS A CA 1 ATOM 1991 C C . HIS A 1 269 ? 1.799 5.459 13.425 1.00 30.85 ? 269 HIS A C 1 ATOM 1992 O O . HIS A 1 269 ? 1.857 6.374 14.258 1.00 32.13 ? 269 HIS A O 1 ATOM 1993 C CB . HIS A 1 269 ? 3.998 4.720 12.478 1.00 31.00 ? 269 HIS A CB 1 ATOM 1994 C CG . HIS A 1 269 ? 4.662 6.021 12.820 1.00 30.54 ? 269 HIS A CG 1 ATOM 1995 N ND1 . HIS A 1 269 ? 4.924 6.996 11.880 1.00 32.48 ? 269 HIS A ND1 1 ATOM 1996 C CD2 . HIS A 1 269 ? 5.108 6.507 14.002 1.00 30.48 ? 269 HIS A CD2 1 ATOM 1997 C CE1 . HIS A 1 269 ? 5.507 8.024 12.466 1.00 31.75 ? 269 HIS A CE1 1 ATOM 1998 N NE2 . HIS A 1 269 ? 5.631 7.753 13.756 1.00 33.27 ? 269 HIS A NE2 1 ATOM 1999 N N . ASP A 1 270 ? 0.842 5.400 12.500 1.00 34.42 ? 270 ASP A N 1 ATOM 2000 C CA . ASP A 1 270 ? -0.195 6.433 12.450 1.00 38.34 ? 270 ASP A CA 1 ATOM 2001 C C . ASP A 1 270 ? -1.047 6.415 13.719 1.00 32.54 ? 270 ASP A C 1 ATOM 2002 O O . ASP A 1 270 ? -1.397 7.465 14.252 1.00 35.38 ? 270 ASP A O 1 ATOM 2003 C CB . ASP A 1 270 ? -1.091 6.297 11.223 1.00 39.39 ? 270 ASP A CB 1 ATOM 2004 C CG . ASP A 1 270 ? -2.054 7.467 11.100 1.00 42.82 ? 270 ASP A CG 1 ATOM 2005 O OD1 . ASP A 1 270 ? -1.590 8.630 11.103 1.00 43.22 ? 270 ASP A OD1 1 ATOM 2006 O OD2 . ASP A 1 270 ? -3.275 7.229 11.001 1.00 45.80 ? 270 ASP A OD2 1 ATOM 2007 N N . ILE A 1 271 ? -1.381 5.222 14.188 1.00 32.75 ? 271 ILE A N 1 ATOM 2008 C CA . ILE A 1 271 ? -2.186 5.087 15.404 1.00 34.84 ? 271 ILE A CA 1 ATOM 2009 C C . ILE A 1 271 ? -1.452 5.655 16.608 1.00 31.74 ? 271 ILE A C 1 ATOM 2010 O O . ILE A 1 271 ? -2.048 6.324 17.457 1.00 35.69 ? 271 ILE A O 1 ATOM 2011 C CB . ILE A 1 271 ? -2.578 3.621 15.633 1.00 37.21 ? 271 ILE A CB 1 ATOM 2012 C CG1 . ILE A 1 271 ? -3.795 3.262 14.765 1.00 38.86 ? 271 ILE A CG1 1 ATOM 2013 C CG2 . ILE A 1 271 ? -2.864 3.352 17.100 1.00 36.70 ? 271 ILE A CG2 1 ATOM 2014 C CD1 . ILE A 1 271 ? -4.023 1.761 14.641 1.00 36.58 ? 271 ILE A CD1 1 ATOM 2015 N N . ILE A 1 272 ? -0.146 5.430 16.684 1.00 30.16 ? 272 ILE A N 1 ATOM 2016 C CA . ILE A 1 272 ? 0.673 5.927 17.783 1.00 29.66 ? 272 ILE A CA 1 ATOM 2017 C C . ILE A 1 272 ? 0.825 7.436 17.747 1.00 29.56 ? 272 ILE A C 1 ATOM 2018 O O . ILE A 1 272 ? 0.744 8.115 18.783 1.00 27.63 ? 272 ILE A O 1 ATOM 2019 C CB . ILE A 1 272 ? 2.041 5.220 17.810 1.00 30.72 ? 272 ILE A CB 1 ATOM 2020 C CG1 . ILE A 1 272 ? 1.900 3.827 18.439 1.00 30.47 ? 272 ILE A CG1 1 ATOM 2021 C CG2 . ILE A 1 272 ? 3.055 6.049 18.583 1.00 30.96 ? 272 ILE A CG2 1 ATOM 2022 C CD1 . ILE A 1 272 ? 2.699 2.743 17.737 1.00 32.59 ? 272 ILE A CD1 1 ATOM 2023 N N . THR A 1 273 ? 1.006 7.997 16.560 1.00 28.82 ? 273 THR A N 1 ATOM 2024 C CA . THR A 1 273 ? 1.137 9.445 16.389 1.00 31.10 ? 273 THR A CA 1 ATOM 2025 C C . THR A 1 273 ? -0.114 10.150 16.911 1.00 28.87 ? 273 THR A C 1 ATOM 2026 O O . THR A 1 273 ? -0.053 11.177 17.579 1.00 32.94 ? 273 THR A O 1 ATOM 2027 C CB . THR A 1 273 ? 1.316 9.777 14.892 1.00 31.55 ? 273 THR A CB 1 ATOM 2028 O OG1 . THR A 1 273 ? 2.533 9.170 14.440 1.00 35.12 ? 273 THR A OG1 1 ATOM 2029 C CG2 . THR A 1 273 ? 1.358 11.273 14.659 1.00 31.53 ? 273 THR A CG2 1 ATOM 2030 N N . LYS A 1 274 ? -1.256 9.557 16.609 1.00 31.22 ? 274 LYS A N 1 ATOM 2031 C CA . LYS A 1 274 ? -2.555 10.070 17.038 1.00 35.19 ? 274 LYS A CA 1 ATOM 2032 C C . LYS A 1 274 ? -2.650 10.110 18.555 1.00 35.08 ? 274 LYS A C 1 ATOM 2033 O O . LYS A 1 274 ? -3.112 11.092 19.143 1.00 32.83 ? 274 LYS A O 1 ATOM 2034 C CB . LYS A 1 274 ? -3.649 9.183 16.445 1.00 36.12 ? 274 LYS A CB 1 ATOM 2035 C CG . LYS A 1 274 ? -5.058 9.466 16.897 1.00 39.20 ? 274 LYS A CG 1 ATOM 2036 C CD . LYS A 1 274 ? -6.062 8.597 16.137 1.00 39.28 ? 274 LYS A CD 1 ATOM 2037 C CE . LYS A 1 274 ? -7.479 8.887 16.612 1.00 40.85 ? 274 LYS A CE 1 ATOM 2038 N NZ . LYS A 1 274 ? -8.492 8.134 15.823 1.00 42.76 ? 274 LYS A NZ 1 ATOM 2039 N N . PHE A 1 275 ? -2.194 9.035 19.203 1.00 30.07 ? 275 PHE A N 1 ATOM 2040 C CA . PHE A 1 275 ? -2.229 8.972 20.660 1.00 30.84 ? 275 PHE A CA 1 ATOM 2041 C C . PHE A 1 275 ? -1.385 10.095 21.256 1.00 31.60 ? 275 PHE A C 1 ATOM 2042 O O . PHE A 1 275 ? -1.804 10.773 22.188 1.00 31.09 ? 275 PHE A O 1 ATOM 2043 C CB . PHE A 1 275 ? -1.735 7.624 21.174 1.00 30.38 ? 275 PHE A CB 1 ATOM 2044 C CG . PHE A 1 275 ? -2.722 6.501 21.040 1.00 30.34 ? 275 PHE A CG 1 ATOM 2045 C CD1 . PHE A 1 275 ? -3.992 6.606 21.577 1.00 30.69 ? 275 PHE A CD1 1 ATOM 2046 C CD2 . PHE A 1 275 ? -2.374 5.335 20.377 1.00 30.89 ? 275 PHE A CD2 1 ATOM 2047 C CE1 . PHE A 1 275 ? -4.902 5.573 21.457 1.00 31.25 ? 275 PHE A CE1 1 ATOM 2048 C CE2 . PHE A 1 275 ? -3.279 4.298 20.252 1.00 31.60 ? 275 PHE A CE2 1 ATOM 2049 C CZ . PHE A 1 275 ? -4.544 4.418 20.792 1.00 31.65 ? 275 PHE A CZ 1 ATOM 2050 N N . LEU A 1 276 ? -0.191 10.285 20.699 1.00 31.49 ? 276 LEU A N 1 ATOM 2051 C CA . LEU A 1 276 ? 0.716 11.314 21.185 1.00 31.26 ? 276 LEU A CA 1 ATOM 2052 C C . LEU A 1 276 ? 0.161 12.717 20.993 1.00 32.81 ? 276 LEU A C 1 ATOM 2053 O O . LEU A 1 276 ? 0.554 13.632 21.721 1.00 33.24 ? 276 LEU A O 1 ATOM 2054 C CB . LEU A 1 276 ? 2.084 11.188 20.505 1.00 30.36 ? 276 LEU A CB 1 ATOM 2055 C CG . LEU A 1 276 ? 2.847 9.891 20.809 1.00 30.28 ? 276 LEU A CG 1 ATOM 2056 C CD1 . LEU A 1 276 ? 4.015 9.723 19.849 1.00 29.44 ? 276 LEU A CD1 1 ATOM 2057 C CD2 . LEU A 1 276 ? 3.322 9.887 22.256 1.00 29.06 ? 276 LEU A CD2 1 ATOM 2058 N N . GLU A 1 277 ? -0.747 12.891 20.039 1.00 33.66 ? 277 GLU A N 1 ATOM 2059 C CA . GLU A 1 277 ? -1.339 14.202 19.790 1.00 39.54 ? 277 GLU A CA 1 ATOM 2060 C C . GLU A 1 277 ? -2.398 14.531 20.836 1.00 40.31 ? 277 GLU A C 1 ATOM 2061 O O . GLU A 1 277 ? -2.594 15.697 21.182 1.00 39.67 ? 277 GLU A O 1 ATOM 2062 C CB . GLU A 1 277 ? -1.911 14.277 18.371 1.00 39.15 ? 277 GLU A CB 1 ATOM 2063 C CG . GLU A 1 277 ? -0.898 13.941 17.291 1.00 41.55 ? 277 GLU A CG 1 ATOM 2064 C CD . GLU A 1 277 ? -1.381 14.086 15.870 1.00 41.94 ? 277 GLU A CD 1 ATOM 2065 O OE1 . GLU A 1 277 ? -2.549 13.765 15.567 1.00 42.53 ? 277 GLU A OE1 1 ATOM 2066 O OE2 . GLU A 1 277 ? -0.577 14.529 15.008 1.00 42.13 ? 277 GLU A OE2 1 ATOM 2067 N N . ASN A 1 278 ? -3.071 13.511 21.357 1.00 38.06 ? 278 ASN A N 1 ATOM 2068 C CA . ASN A 1 278 ? -4.111 13.698 22.364 1.00 39.64 ? 278 ASN A CA 1 ATOM 2069 C C . ASN A 1 278 ? -3.532 14.098 23.713 1.00 38.64 ? 278 ASN A C 1 ATOM 2070 O O . ASN A 1 278 ? -2.585 13.484 24.210 1.00 41.47 ? 278 ASN A O 1 ATOM 2071 C CB . ASN A 1 278 ? -4.967 12.437 22.499 1.00 39.13 ? 278 ASN A CB 1 ATOM 2072 C CG . ASN A 1 278 ? -5.915 12.473 23.678 1.00 42.02 ? 278 ASN A CG 1 ATOM 2073 O OD1 . ASN A 1 278 ? -5.730 11.758 24.669 1.00 40.42 ? 278 ASN A OD1 1 ATOM 2074 N ND2 . ASN A 1 278 ? -6.950 13.302 23.602 1.00 42.19 ? 278 ASN A ND2 1 ATOM 2075 N N . GLU A 1 279 ? -4.104 15.137 24.318 1.00 39.19 ? 279 GLU A N 1 ATOM 2076 C CA . GLU A 1 279 ? -3.636 15.617 25.609 1.00 43.98 ? 279 GLU A CA 1 ATOM 2077 C C . GLU A 1 279 ? -4.731 15.553 26.668 1.00 39.27 ? 279 GLU A C 1 ATOM 2078 O O . GLU A 1 279 ? -4.533 16.049 27.778 1.00 46.00 ? 279 GLU A O 1 ATOM 2079 C CB . GLU A 1 279 ? -3.147 17.064 25.504 1.00 45.60 ? 279 GLU A CB 1 ATOM 2080 C CG . GLU A 1 279 ? -2.014 17.253 24.514 1.00 51.12 ? 279 GLU A CG 1 ATOM 2081 C CD . GLU A 1 279 ? -0.671 16.870 25.103 1.00 55.35 ? 279 GLU A CD 1 ATOM 2082 O OE1 . GLU A 1 279 ? -0.459 15.670 25.381 1.00 56.51 ? 279 GLU A OE1 1 ATOM 2083 O OE2 . GLU A 1 279 ? 0.169 17.777 25.281 1.00 57.55 ? 279 GLU A OE2 1 ATOM 2084 N N . ASP A 1 280 ? -5.869 14.970 26.315 1.00 35.53 ? 280 ASP A N 1 ATOM 2085 C CA . ASP A 1 280 ? -6.981 14.877 27.251 1.00 35.94 ? 280 ASP A CA 1 ATOM 2086 C C . ASP A 1 280 ? -6.650 13.971 28.426 1.00 35.18 ? 280 ASP A C 1 ATOM 2087 O O . ASP A 1 280 ? -5.934 12.977 28.295 1.00 30.71 ? 280 ASP A O 1 ATOM 2088 C CB . ASP A 1 280 ? -8.249 14.394 26.540 1.00 38.45 ? 280 ASP A CB 1 ATOM 2089 C CG . ASP A 1 280 ? -8.736 15.433 25.539 1.00 41.49 ? 280 ASP A CG 1 ATOM 2090 O OD1 . ASP A 1 280 ? -8.611 16.636 25.847 1.00 42.94 ? 280 ASP A OD1 1 ATOM 2091 O OD2 . ASP A 1 280 ? -9.226 15.044 24.465 1.00 43.51 ? 280 ASP A OD2 1 ATOM 2092 N N . ARG A 1 281 ? -7.181 14.339 29.587 1.00 30.94 ? 281 ARG A N 1 ATOM 2093 C CA . ARG A 1 281 ? -6.982 13.571 30.806 1.00 29.44 ? 281 ARG A CA 1 ATOM 2094 C C . ARG A 1 281 ? -8.338 13.304 31.468 1.00 30.40 ? 281 ARG A C 1 ATOM 2095 O O . ARG A 1 281 ? -9.273 14.089 31.331 1.00 23.31 ? 281 ARG A O 1 ATOM 2096 C CB . ARG A 1 281 ? -6.080 14.304 31.789 1.00 30.09 ? 281 ARG A CB 1 ATOM 2097 C CG . ARG A 1 281 ? -4.599 14.293 31.470 1.00 29.31 ? 281 ARG A CG 1 ATOM 2098 C CD . ARG A 1 281 ? -3.829 15.186 32.442 1.00 29.46 ? 281 ARG A CD 1 ATOM 2099 N NE . ARG A 1 281 ? -2.445 15.353 32.029 1.00 29.71 ? 281 ARG A NE 1 ATOM 2100 C CZ . ARG A 1 281 ? -1.466 14.481 32.247 1.00 29.21 ? 281 ARG A CZ 1 ATOM 2101 N NH1 . ARG A 1 281 ? -1.695 13.346 32.897 1.00 25.19 ? 281 ARG A NH1 1 ATOM 2102 N NH2 . ARG A 1 281 ? -0.244 14.765 31.809 1.00 27.08 ? 281 ARG A NH2 1 ATOM 2103 N N . ARG A 1 282 ? -8.418 12.191 32.174 1.00 31.54 ? 282 ARG A N 1 ATOM 2104 C CA . ARG A 1 282 ? -9.633 11.815 32.888 1.00 30.31 ? 282 ARG A CA 1 ATOM 2105 C C . ARG A 1 282 ? -9.208 11.111 34.177 1.00 32.22 ? 282 ARG A C 1 ATOM 2106 O O . ARG A 1 282 ? -8.077 10.616 34.244 1.00 23.60 ? 282 ARG A O 1 ATOM 2107 C CB . ARG A 1 282 ? -10.594 11.011 32.062 1.00 33.23 ? 282 ARG A CB 1 ATOM 2108 C CG . ARG A 1 282 ? -10.255 9.558 31.762 1.00 36.22 ? 282 ARG A CG 1 ATOM 2109 C CD . ARG A 1 282 ? -11.485 8.690 31.983 1.00 39.61 ? 282 ARG A CD 1 ATOM 2110 N NE . ARG A 1 282 ? -11.610 7.557 31.106 1.00 42.55 ? 282 ARG A NE 1 ATOM 2111 C CZ . ARG A 1 282 ? -11.462 7.534 29.789 1.00 42.02 ? 282 ARG A CZ 1 ATOM 2112 N NH1 . ARG A 1 282 ? -11.153 8.634 29.121 1.00 42.65 ? 282 ARG A NH1 1 ATOM 2113 N NH2 . ARG A 1 282 ? -11.619 6.395 29.126 1.00 42.25 ? 282 ARG A NH2 1 ATOM 2114 N N . SER A 1 283 ? -10.079 11.119 35.183 1.00 26.24 ? 283 SER A N 1 ATOM 2115 C CA . SER A 1 283 ? -9.725 10.483 36.446 1.00 27.64 ? 283 SER A CA 1 ATOM 2116 C C . SER A 1 283 ? -9.762 8.962 36.281 1.00 25.88 ? 283 SER A C 1 ATOM 2117 O O . SER A 1 283 ? -10.542 8.434 35.500 1.00 25.40 ? 283 SER A O 1 ATOM 2118 C CB . SER A 1 283 ? -10.635 10.909 37.587 1.00 28.57 ? 283 SER A CB 1 ATOM 2119 O OG . SER A 1 283 ? -11.953 10.433 37.406 1.00 31.78 ? 283 SER A OG 1 ATOM 2120 N N . ALA A 1 284 ? -8.874 8.302 37.007 1.00 25.05 ? 284 ALA A N 1 ATOM 2121 C CA . ALA A 1 284 ? -8.789 6.856 37.002 1.00 24.73 ? 284 ALA A CA 1 ATOM 2122 C C . ALA A 1 284 ? -7.955 6.374 38.189 1.00 22.29 ? 284 ALA A C 1 ATOM 2123 O O . ALA A 1 284 ? -7.097 7.109 38.668 1.00 22.19 ? 284 ALA A O 1 ATOM 2124 C CB . ALA A 1 284 ? -8.141 6.373 35.702 1.00 21.03 ? 284 ALA A CB 1 ATOM 2125 N N . SER A 1 285 ? -8.230 5.162 38.644 1.00 21.32 ? 285 SER A N 1 ATOM 2126 C CA . SER A 1 285 ? -7.408 4.547 39.687 1.00 23.03 ? 285 SER A CA 1 ATOM 2127 C C . SER A 1 285 ? -6.486 3.570 38.926 1.00 23.23 ? 285 SER A C 1 ATOM 2128 O O . SER A 1 285 ? -6.965 2.518 38.516 1.00 24.75 ? 285 SER A O 1 ATOM 2129 C CB . SER A 1 285 ? -8.209 3.770 40.717 1.00 23.52 ? 285 SER A CB 1 ATOM 2130 O OG . SER A 1 285 ? -8.826 4.639 41.641 1.00 29.12 ? 285 SER A OG 1 ATOM 2131 N N . LEU A 1 286 ? -5.245 3.974 38.750 1.00 23.05 ? 286 LEU A N 1 ATOM 2132 C CA . LEU A 1 286 ? -4.290 3.183 38.004 1.00 23.42 ? 286 LEU A CA 1 ATOM 2133 C C . LEU A 1 286 ? -3.401 2.309 38.881 1.00 20.59 ? 286 LEU A C 1 ATOM 2134 O O . LEU A 1 286 ? -2.800 2.747 39.843 1.00 18.89 ? 286 LEU A O 1 ATOM 2135 C CB . LEU A 1 286 ? -3.402 4.114 37.152 1.00 21.31 ? 286 LEU A CB 1 ATOM 2136 C CG . LEU A 1 286 ? -2.180 3.461 36.492 1.00 21.25 ? 286 LEU A CG 1 ATOM 2137 C CD1 . LEU A 1 286 ? -2.607 2.496 35.391 1.00 18.37 ? 286 LEU A CD1 1 ATOM 2138 C CD2 . LEU A 1 286 ? -1.253 4.536 35.927 1.00 21.53 ? 286 LEU A CD2 1 ATOM 2139 N N . HIS A 1 287 ? -3.288 1.053 38.468 1.00 18.66 ? 287 HIS A N 1 ATOM 2140 C CA . HIS A 1 287 ? -2.417 0.083 39.141 1.00 24.13 ? 287 HIS A CA 1 ATOM 2141 C C . HIS A 1 287 ? -1.335 -0.312 38.121 1.00 21.06 ? 287 HIS A C 1 ATOM 2142 O O . HIS A 1 287 ? -1.670 -0.832 37.067 1.00 20.75 ? 287 HIS A O 1 ATOM 2143 C CB . HIS A 1 287 ? -3.247 -1.111 39.568 1.00 24.00 ? 287 HIS A CB 1 ATOM 2144 C CG . HIS A 1 287 ? -4.249 -0.866 40.653 1.00 27.68 ? 287 HIS A CG 1 ATOM 2145 N ND1 . HIS A 1 287 ? -5.228 0.104 40.589 1.00 30.05 ? 287 HIS A ND1 1 ATOM 2146 C CD2 . HIS A 1 287 ? -4.424 -1.495 41.840 1.00 26.30 ? 287 HIS A CD2 1 ATOM 2147 C CE1 . HIS A 1 287 ? -5.959 0.074 41.688 1.00 27.84 ? 287 HIS A CE1 1 ATOM 2148 N NE2 . HIS A 1 287 ? -5.493 -0.883 42.466 1.00 31.07 ? 287 HIS A NE2 1 ATOM 2149 N N . LEU A 1 288 ? -0.087 0.027 38.401 1.00 24.24 ? 288 LEU A N 1 ATOM 2150 C CA . LEU A 1 288 ? 1.002 -0.241 37.467 1.00 27.09 ? 288 LEU A CA 1 ATOM 2151 C C . LEU A 1 288 ? 2.149 -0.911 38.215 1.00 24.42 ? 288 LEU A C 1 ATOM 2152 O O . LEU A 1 288 ? 2.608 -0.411 39.237 1.00 21.02 ? 288 LEU A O 1 ATOM 2153 C CB . LEU A 1 288 ? 1.505 1.053 36.808 1.00 23.32 ? 288 LEU A CB 1 ATOM 2154 C CG . LEU A 1 288 ? 2.628 0.912 35.773 1.00 27.63 ? 288 LEU A CG 1 ATOM 2155 C CD1 . LEU A 1 288 ? 2.075 0.390 34.443 1.00 25.55 ? 288 LEU A CD1 1 ATOM 2156 C CD2 . LEU A 1 288 ? 3.336 2.240 35.548 1.00 22.46 ? 288 LEU A CD2 1 ATOM 2157 N N . PRO A 1 289 ? 2.605 -2.036 37.694 1.00 25.84 ? 289 PRO A N 1 ATOM 2158 C CA . PRO A 1 289 ? 3.648 -2.812 38.324 1.00 29.75 ? 289 PRO A CA 1 ATOM 2159 C C . PRO A 1 289 ? 4.984 -2.117 38.413 1.00 27.31 ? 289 PRO A C 1 ATOM 2160 O O . PRO A 1 289 ? 5.447 -1.445 37.491 1.00 32.45 ? 289 PRO A O 1 ATOM 2161 C CB . PRO A 1 289 ? 3.725 -4.085 37.484 1.00 29.83 ? 289 PRO A CB 1 ATOM 2162 C CG . PRO A 1 289 ? 3.185 -3.672 36.150 1.00 34.91 ? 289 PRO A CG 1 ATOM 2163 C CD . PRO A 1 289 ? 2.071 -2.700 36.482 1.00 28.83 ? 289 PRO A CD 1 ATOM 2164 N N . LYS A 1 290 ? 5.637 -2.296 39.550 1.00 27.67 ? 290 LYS A N 1 ATOM 2165 C CA . LYS A 1 290 ? 6.980 -1.767 39.801 1.00 33.63 ? 290 LYS A CA 1 ATOM 2166 C C . LYS A 1 290 ? 7.944 -2.888 39.385 1.00 42.51 ? 290 LYS A C 1 ATOM 2167 O O . LYS A 1 290 ? 8.036 -3.876 40.119 1.00 43.19 ? 290 LYS A O 1 ATOM 2168 C CB . LYS A 1 290 ? 7.164 -1.472 41.284 1.00 36.91 ? 290 LYS A CB 1 ATOM 2169 C CG . LYS A 1 290 ? 8.587 -1.208 41.729 1.00 38.81 ? 290 LYS A CG 1 ATOM 2170 C CD . LYS A 1 290 ? 8.641 -0.862 43.219 1.00 36.31 ? 290 LYS A CD 1 ATOM 2171 C CE . LYS A 1 290 ? 10.072 -0.650 43.677 1.00 37.17 ? 290 LYS A CE 1 ATOM 2172 N NZ . LYS A 1 290 ? 10.148 0.171 44.922 1.00 43.48 ? 290 LYS A NZ 1 ATOM 2173 N N . LEU A 1 291 ? 8.594 -2.747 38.230 1.00 41.26 ? 291 LEU A N 1 ATOM 2174 C CA . LEU A 1 291 ? 9.475 -3.824 37.814 1.00 44.21 ? 291 LEU A CA 1 ATOM 2175 C C . LEU A 1 291 ? 10.780 -3.414 37.174 1.00 42.46 ? 291 LEU A C 1 ATOM 2176 O O . LEU A 1 291 ? 11.147 -2.266 36.948 1.00 29.23 ? 291 LEU A O 1 ATOM 2177 C CB . LEU A 1 291 ? 8.707 -4.775 36.872 1.00 46.05 ? 291 LEU A CB 1 ATOM 2178 C CG . LEU A 1 291 ? 8.361 -4.191 35.498 1.00 46.96 ? 291 LEU A CG 1 ATOM 2179 C CD1 . LEU A 1 291 ? 7.048 -4.762 34.990 1.00 46.04 ? 291 LEU A CD1 1 ATOM 2180 C CD2 . LEU A 1 291 ? 8.318 -2.676 35.567 1.00 49.05 ? 291 LEU A CD2 1 ATOM 2181 N N . SER A 1 292 ? 11.540 -4.469 36.874 1.00 42.19 ? 292 SER A N 1 ATOM 2182 C CA . SER A 1 292 ? 12.840 -4.364 36.236 1.00 46.22 ? 292 SER A CA 1 ATOM 2183 C C . SER A 1 292 ? 12.983 -5.563 35.292 1.00 45.42 ? 292 SER A C 1 ATOM 2184 O O . SER A 1 292 ? 13.028 -6.703 35.745 1.00 44.67 ? 292 SER A O 1 ATOM 2185 C CB . SER A 1 292 ? 13.967 -4.349 37.257 1.00 47.25 ? 292 SER A CB 1 ATOM 2186 O OG . SER A 1 292 ? 15.194 -3.960 36.653 1.00 51.41 ? 292 SER A OG 1 ATOM 2187 N N . ILE A 1 293 ? 12.956 -5.279 34.000 1.00 45.76 ? 293 ILE A N 1 ATOM 2188 C CA . ILE A 1 293 ? 13.075 -6.330 33.001 1.00 42.26 ? 293 ILE A CA 1 ATOM 2189 C C . ILE A 1 293 ? 14.295 -6.052 32.121 1.00 40.24 ? 293 ILE A C 1 ATOM 2190 O O . ILE A 1 293 ? 14.801 -4.934 32.086 1.00 35.51 ? 293 ILE A O 1 ATOM 2191 C CB . ILE A 1 293 ? 11.831 -6.459 32.119 1.00 43.80 ? 293 ILE A CB 1 ATOM 2192 C CG1 . ILE A 1 293 ? 11.581 -5.171 31.325 1.00 43.00 ? 293 ILE A CG1 1 ATOM 2193 C CG2 . ILE A 1 293 ? 10.604 -6.818 32.944 1.00 43.50 ? 293 ILE A CG2 1 ATOM 2194 C CD1 . ILE A 1 293 ? 10.533 -5.344 30.239 1.00 43.73 ? 293 ILE A CD1 1 ATOM 2195 N N . THR A 1 294 ? 14.746 -7.090 31.437 1.00 40.82 ? 294 THR A N 1 ATOM 2196 C CA . THR A 1 294 ? 15.896 -6.973 30.555 1.00 41.92 ? 294 THR A CA 1 ATOM 2197 C C . THR A 1 294 ? 15.647 -7.759 29.268 1.00 39.76 ? 294 THR A C 1 ATOM 2198 O O . THR A 1 294 ? 14.862 -8.701 29.249 1.00 40.60 ? 294 THR A O 1 ATOM 2199 C CB . THR A 1 294 ? 17.177 -7.517 31.214 1.00 42.11 ? 294 THR A CB 1 ATOM 2200 O OG1 . THR A 1 294 ? 17.037 -8.934 31.394 1.00 43.25 ? 294 THR A OG1 1 ATOM 2201 C CG2 . THR A 1 294 ? 17.402 -6.860 32.565 1.00 43.75 ? 294 THR A CG2 1 ATOM 2202 N N . GLY A 1 295 ? 16.321 -7.339 28.213 1.00 36.02 ? 295 GLY A N 1 ATOM 2203 C CA . GLY A 1 295 ? 16.224 -8.015 26.918 1.00 31.19 ? 295 GLY A CA 1 ATOM 2204 C C . GLY A 1 295 ? 17.666 -8.168 26.396 1.00 26.27 ? 295 GLY A C 1 ATOM 2205 O O . GLY A 1 295 ? 18.379 -7.170 26.330 1.00 29.49 ? 295 GLY A O 1 ATOM 2206 N N . THR A 1 296 ? 18.054 -9.388 26.088 1.00 27.98 ? 296 THR A N 1 ATOM 2207 C CA . THR A 1 296 ? 19.399 -9.651 25.570 1.00 33.86 ? 296 THR A CA 1 ATOM 2208 C C . THR A 1 296 ? 19.248 -10.403 24.245 1.00 32.04 ? 296 THR A C 1 ATOM 2209 O O . THR A 1 296 ? 18.649 -11.480 24.227 1.00 34.24 ? 296 THR A O 1 ATOM 2210 C CB . THR A 1 296 ? 20.262 -10.469 26.534 1.00 34.36 ? 296 THR A CB 1 ATOM 2211 O OG1 . THR A 1 296 ? 20.348 -9.811 27.806 1.00 34.60 ? 296 THR A OG1 1 ATOM 2212 C CG2 . THR A 1 296 ? 21.675 -10.643 25.986 1.00 33.20 ? 296 THR A CG2 1 ATOM 2213 N N . TYR A 1 297 ? 19.752 -9.825 23.160 1.00 31.22 ? 297 TYR A N 1 ATOM 2214 C CA . TYR A 1 297 ? 19.597 -10.454 21.865 1.00 32.37 ? 297 TYR A CA 1 ATOM 2215 C C . TYR A 1 297 ? 20.863 -10.602 21.048 1.00 29.76 ? 297 TYR A C 1 ATOM 2216 O O . TYR A 1 297 ? 21.778 -9.789 21.085 1.00 24.41 ? 297 TYR A O 1 ATOM 2217 C CB . TYR A 1 297 ? 18.568 -9.627 21.034 1.00 31.53 ? 297 TYR A CB 1 ATOM 2218 C CG . TYR A 1 297 ? 17.278 -9.468 21.818 1.00 31.23 ? 297 TYR A CG 1 ATOM 2219 C CD1 . TYR A 1 297 ? 16.304 -10.453 21.778 1.00 29.65 ? 297 TYR A CD1 1 ATOM 2220 C CD2 . TYR A 1 297 ? 17.056 -8.343 22.598 1.00 28.84 ? 297 TYR A CD2 1 ATOM 2221 C CE1 . TYR A 1 297 ? 15.130 -10.322 22.495 1.00 30.24 ? 297 TYR A CE1 1 ATOM 2222 C CE2 . TYR A 1 297 ? 15.884 -8.201 23.317 1.00 29.00 ? 297 TYR A CE2 1 ATOM 2223 C CZ . TYR A 1 297 ? 14.928 -9.191 23.262 1.00 29.66 ? 297 TYR A CZ 1 ATOM 2224 O OH . TYR A 1 297 ? 13.759 -9.055 23.977 1.00 28.32 ? 297 TYR A OH 1 ATOM 2225 N N . ASP A 1 298 ? 20.876 -11.689 20.274 1.00 30.61 ? 298 ASP A N 1 ATOM 2226 C CA . ASP A 1 298 ? 21.995 -11.954 19.355 1.00 30.28 ? 298 ASP A CA 1 ATOM 2227 C C . ASP A 1 298 ? 21.567 -11.325 18.021 1.00 24.77 ? 298 ASP A C 1 ATOM 2228 O O . ASP A 1 298 ? 20.696 -11.874 17.349 1.00 29.37 ? 298 ASP A O 1 ATOM 2229 C CB . ASP A 1 298 ? 22.229 -13.448 19.207 1.00 31.39 ? 298 ASP A CB 1 ATOM 2230 C CG . ASP A 1 298 ? 23.229 -13.798 18.117 1.00 30.67 ? 298 ASP A CG 1 ATOM 2231 O OD1 . ASP A 1 298 ? 23.781 -12.886 17.476 1.00 26.77 ? 298 ASP A OD1 1 ATOM 2232 O OD2 . ASP A 1 298 ? 23.462 -15.005 17.904 1.00 32.64 ? 298 ASP A OD2 1 ATOM 2233 N N . LEU A 1 299 ? 22.096 -10.152 17.715 1.00 18.07 ? 299 LEU A N 1 ATOM 2234 C CA . LEU A 1 299 ? 21.734 -9.410 16.527 1.00 21.61 ? 299 LEU A CA 1 ATOM 2235 C C . LEU A 1 299 ? 22.044 -10.135 15.230 1.00 24.63 ? 299 LEU A C 1 ATOM 2236 O O . LEU A 1 299 ? 21.371 -9.887 14.215 1.00 27.41 ? 299 LEU A O 1 ATOM 2237 C CB . LEU A 1 299 ? 22.381 -8.018 16.537 1.00 20.98 ? 299 LEU A CB 1 ATOM 2238 C CG . LEU A 1 299 ? 21.955 -7.103 17.697 1.00 22.83 ? 299 LEU A CG 1 ATOM 2239 C CD1 . LEU A 1 299 ? 22.771 -5.821 17.705 1.00 22.73 ? 299 LEU A CD1 1 ATOM 2240 C CD2 . LEU A 1 299 ? 20.469 -6.786 17.616 1.00 21.27 ? 299 LEU A CD2 1 ATOM 2241 N N . LYS A 1 300 ? 23.037 -11.017 15.224 1.00 27.80 ? 300 LYS A N 1 ATOM 2242 C CA . LYS A 1 300 ? 23.356 -11.747 13.986 1.00 28.57 ? 300 LYS A CA 1 ATOM 2243 C C . LYS A 1 300 ? 22.153 -12.612 13.605 1.00 29.73 ? 300 LYS A C 1 ATOM 2244 O O . LYS A 1 300 ? 21.748 -12.686 12.453 1.00 33.26 ? 300 LYS A O 1 ATOM 2245 C CB . LYS A 1 300 ? 24.591 -12.620 14.152 1.00 32.19 ? 300 LYS A CB 1 ATOM 2246 C CG . LYS A 1 300 ? 24.881 -13.517 12.951 1.00 34.93 ? 300 LYS A CG 1 ATOM 2247 C CD . LYS A 1 300 ? 26.153 -14.321 13.156 1.00 37.44 ? 300 LYS A CD 1 ATOM 2248 C CE . LYS A 1 300 ? 26.538 -15.073 11.888 1.00 39.78 ? 300 LYS A CE 1 ATOM 2249 N NZ . LYS A 1 300 ? 27.717 -15.959 12.109 1.00 41.22 ? 300 LYS A NZ 1 ATOM 2250 N N . SER A 1 301 ? 21.584 -13.248 14.624 1.00 26.19 ? 301 SER A N 1 ATOM 2251 C CA . SER A 1 301 ? 20.428 -14.110 14.468 1.00 27.59 ? 301 SER A CA 1 ATOM 2252 C C . SER A 1 301 ? 19.164 -13.310 14.180 1.00 30.18 ? 301 SER A C 1 ATOM 2253 O O . SER A 1 301 ? 18.460 -13.558 13.206 1.00 27.85 ? 301 SER A O 1 ATOM 2254 C CB . SER A 1 301 ? 20.238 -14.935 15.752 1.00 29.37 ? 301 SER A CB 1 ATOM 2255 O OG . SER A 1 301 ? 19.007 -15.634 15.734 1.00 31.18 ? 301 SER A OG 1 ATOM 2256 N N . VAL A 1 302 ? 18.878 -12.331 15.038 1.00 30.70 ? 302 VAL A N 1 ATOM 2257 C CA . VAL A 1 302 ? 17.683 -11.516 14.903 1.00 28.13 ? 302 VAL A CA 1 ATOM 2258 C C . VAL A 1 302 ? 17.656 -10.671 13.649 1.00 26.89 ? 302 VAL A C 1 ATOM 2259 O O . VAL A 1 302 ? 16.660 -10.696 12.913 1.00 22.21 ? 302 VAL A O 1 ATOM 2260 C CB . VAL A 1 302 ? 17.477 -10.626 16.151 1.00 28.87 ? 302 VAL A CB 1 ATOM 2261 C CG1 . VAL A 1 302 ? 16.398 -9.590 15.891 1.00 29.70 ? 302 VAL A CG1 1 ATOM 2262 C CG2 . VAL A 1 302 ? 17.102 -11.505 17.340 1.00 32.25 ? 302 VAL A CG2 1 ATOM 2263 N N . LEU A 1 303 ? 18.719 -9.916 13.376 1.00 23.35 ? 303 LEU A N 1 ATOM 2264 C CA . LEU A 1 303 ? 18.747 -9.080 12.173 1.00 24.64 ? 303 LEU A CA 1 ATOM 2265 C C . LEU A 1 303 ? 18.887 -9.965 10.934 1.00 24.20 ? 303 LEU A C 1 ATOM 2266 O O . LEU A 1 303 ? 18.603 -9.544 9.813 1.00 20.05 ? 303 LEU A O 1 ATOM 2267 C CB . LEU A 1 303 ? 19.860 -8.048 12.240 1.00 24.89 ? 303 LEU A CB 1 ATOM 2268 C CG . LEU A 1 303 ? 19.870 -7.124 13.462 1.00 26.67 ? 303 LEU A CG 1 ATOM 2269 C CD1 . LEU A 1 303 ? 21.042 -6.161 13.391 1.00 28.81 ? 303 LEU A CD1 1 ATOM 2270 C CD2 . LEU A 1 303 ? 18.550 -6.371 13.566 1.00 27.35 ? 303 LEU A CD2 1 ATOM 2271 N N . GLY A 1 304 ? 19.330 -11.193 11.165 1.00 27.62 ? 304 GLY A N 1 ATOM 2272 C CA . GLY A 1 304 ? 19.468 -12.156 10.058 1.00 30.72 ? 304 GLY A CA 1 ATOM 2273 C C . GLY A 1 304 ? 18.060 -12.414 9.501 1.00 34.04 ? 304 GLY A C 1 ATOM 2274 O O . GLY A 1 304 ? 17.846 -12.407 8.297 1.00 34.91 ? 304 GLY A O 1 ATOM 2275 N N . GLN A 1 305 ? 17.111 -12.604 10.414 1.00 34.36 ? 305 GLN A N 1 ATOM 2276 C CA . GLN A 1 305 ? 15.725 -12.845 10.032 1.00 35.84 ? 305 GLN A CA 1 ATOM 2277 C C . GLN A 1 305 ? 15.099 -11.624 9.376 1.00 39.37 ? 305 GLN A C 1 ATOM 2278 O O . GLN A 1 305 ? 14.014 -11.705 8.796 1.00 43.07 ? 305 GLN A O 1 ATOM 2279 C CB . GLN A 1 305 ? 14.907 -13.295 11.243 1.00 38.53 ? 305 GLN A CB 1 ATOM 2280 C CG . GLN A 1 305 ? 15.426 -14.572 11.889 1.00 40.58 ? 305 GLN A CG 1 ATOM 2281 C CD . GLN A 1 305 ? 15.471 -15.726 10.910 1.00 43.36 ? 305 GLN A CD 1 ATOM 2282 O OE1 . GLN A 1 305 ? 14.441 -16.295 10.547 1.00 45.01 ? 305 GLN A OE1 1 ATOM 2283 N NE2 . GLN A 1 305 ? 16.672 -16.084 10.468 1.00 45.72 ? 305 GLN A NE2 1 ATOM 2284 N N . LEU A 1 306 ? 15.782 -10.484 9.440 1.00 36.67 ? 306 LEU A N 1 ATOM 2285 C CA . LEU A 1 306 ? 15.294 -9.264 8.809 1.00 34.24 ? 306 LEU A CA 1 ATOM 2286 C C . LEU A 1 306 ? 16.013 -8.994 7.494 1.00 33.26 ? 306 LEU A C 1 ATOM 2287 O O . LEU A 1 306 ? 15.847 -7.937 6.888 1.00 34.29 ? 306 LEU A O 1 ATOM 2288 C CB . LEU A 1 306 ? 15.427 -8.068 9.752 1.00 33.48 ? 306 LEU A CB 1 ATOM 2289 C CG . LEU A 1 306 ? 14.510 -8.096 10.982 1.00 34.45 ? 306 LEU A CG 1 ATOM 2290 C CD1 . LEU A 1 306 ? 14.721 -6.862 11.842 1.00 32.21 ? 306 LEU A CD1 1 ATOM 2291 C CD2 . LEU A 1 306 ? 13.059 -8.236 10.550 1.00 34.53 ? 306 LEU A CD2 1 ATOM 2292 N N . GLY A 1 307 ? 16.827 -9.950 7.045 1.00 33.93 ? 307 GLY A N 1 ATOM 2293 C CA . GLY A 1 307 ? 17.558 -9.842 5.811 1.00 34.48 ? 307 GLY A CA 1 ATOM 2294 C C . GLY A 1 307 ? 18.967 -9.307 5.902 1.00 32.70 ? 307 GLY A C 1 ATOM 2295 O O . GLY A 1 307 ? 19.607 -9.103 4.856 1.00 37.73 ? 307 GLY A O 1 ATOM 2296 N N . ILE A 1 308 ? 19.488 -9.056 7.095 1.00 31.88 ? 308 ILE A N 1 ATOM 2297 C CA . ILE A 1 308 ? 20.860 -8.539 7.227 1.00 32.82 ? 308 ILE A CA 1 ATOM 2298 C C . ILE A 1 308 ? 21.810 -9.705 7.449 1.00 31.76 ? 308 ILE A C 1 ATOM 2299 O O . ILE A 1 308 ? 22.029 -10.096 8.594 1.00 34.58 ? 308 ILE A O 1 ATOM 2300 C CB . ILE A 1 308 ? 20.966 -7.534 8.381 1.00 31.73 ? 308 ILE A CB 1 ATOM 2301 C CG1 . ILE A 1 308 ? 19.940 -6.409 8.184 1.00 30.98 ? 308 ILE A CG1 1 ATOM 2302 C CG2 . ILE A 1 308 ? 22.369 -6.939 8.468 1.00 30.64 ? 308 ILE A CG2 1 ATOM 2303 C CD1 . ILE A 1 308 ? 20.003 -5.335 9.244 1.00 28.89 ? 308 ILE A CD1 1 ATOM 2304 N N . THR A 1 309 ? 22.332 -10.291 6.360 1.00 30.02 ? 309 THR A N 1 ATOM 2305 C CA . THR A 1 309 ? 23.191 -11.454 6.517 1.00 29.93 ? 309 THR A CA 1 ATOM 2306 C C . THR A 1 309 ? 24.603 -11.321 6.002 1.00 30.76 ? 309 THR A C 1 ATOM 2307 O O . THR A 1 309 ? 25.516 -11.926 6.598 1.00 34.20 ? 309 THR A O 1 ATOM 2308 C CB . THR A 1 309 ? 22.518 -12.710 5.918 1.00 32.62 ? 309 THR A CB 1 ATOM 2309 O OG1 . THR A 1 309 ? 22.649 -12.720 4.499 1.00 34.02 ? 309 THR A OG1 1 ATOM 2310 C CG2 . THR A 1 309 ? 21.030 -12.724 6.270 1.00 31.00 ? 309 THR A CG2 1 ATOM 2311 N N . LYS A 1 310 ? 24.861 -10.569 4.946 1.00 33.18 ? 310 LYS A N 1 ATOM 2312 C CA . LYS A 1 310 ? 26.190 -10.438 4.379 1.00 35.26 ? 310 LYS A CA 1 ATOM 2313 C C . LYS A 1 310 ? 27.242 -9.830 5.271 1.00 35.54 ? 310 LYS A C 1 ATOM 2314 O O . LYS A 1 310 ? 28.397 -10.300 5.263 1.00 30.78 ? 310 LYS A O 1 ATOM 2315 C CB . LYS A 1 310 ? 26.140 -9.713 3.022 1.00 33.62 ? 310 LYS A CB 1 ATOM 2316 C CG . LYS A 1 310 ? 25.921 -10.687 1.869 1.00 36.10 ? 310 LYS A CG 1 ATOM 2317 C CD . LYS A 1 310 ? 26.083 -10.017 0.515 1.00 39.20 ? 310 LYS A CD 1 ATOM 2318 C CE . LYS A 1 310 ? 25.981 -11.042 -0.609 1.00 40.72 ? 310 LYS A CE 1 ATOM 2319 N NZ . LYS A 1 310 ? 26.029 -10.399 -1.950 1.00 43.69 ? 310 LYS A NZ 1 ATOM 2320 N N . VAL A 1 311 ? 26.910 -8.797 6.038 1.00 31.37 ? 311 VAL A N 1 ATOM 2321 C CA . VAL A 1 311 ? 27.889 -8.171 6.921 1.00 28.32 ? 311 VAL A CA 1 ATOM 2322 C C . VAL A 1 311 ? 28.412 -9.173 7.941 1.00 30.54 ? 311 VAL A C 1 ATOM 2323 O O . VAL A 1 311 ? 29.505 -9.009 8.487 1.00 32.12 ? 311 VAL A O 1 ATOM 2324 C CB . VAL A 1 311 ? 27.329 -6.927 7.617 1.00 30.73 ? 311 VAL A CB 1 ATOM 2325 C CG1 . VAL A 1 311 ? 26.432 -7.298 8.788 1.00 29.44 ? 311 VAL A CG1 1 ATOM 2326 C CG2 . VAL A 1 311 ? 28.456 -6.004 8.060 1.00 30.63 ? 311 VAL A CG2 1 ATOM 2327 N N . PHE A 1 312 ? 27.653 -10.238 8.177 1.00 27.41 ? 312 PHE A N 1 ATOM 2328 C CA . PHE A 1 312 ? 28.025 -11.270 9.122 1.00 26.77 ? 312 PHE A CA 1 ATOM 2329 C C . PHE A 1 312 ? 28.656 -12.488 8.450 1.00 27.72 ? 312 PHE A C 1 ATOM 2330 O O . PHE A 1 312 ? 28.927 -13.484 9.137 1.00 29.80 ? 312 PHE A O 1 ATOM 2331 C CB . PHE A 1 312 ? 26.798 -11.751 9.914 1.00 26.92 ? 312 PHE A CB 1 ATOM 2332 C CG . PHE A 1 312 ? 26.105 -10.680 10.707 1.00 27.35 ? 312 PHE A CG 1 ATOM 2333 C CD1 . PHE A 1 312 ? 26.692 -10.151 11.843 1.00 26.88 ? 312 PHE A CD1 1 ATOM 2334 C CD2 . PHE A 1 312 ? 24.861 -10.210 10.320 1.00 28.00 ? 312 PHE A CD2 1 ATOM 2335 C CE1 . PHE A 1 312 ? 26.052 -9.168 12.579 1.00 27.48 ? 312 PHE A CE1 1 ATOM 2336 C CE2 . PHE A 1 312 ? 24.213 -9.228 11.052 1.00 26.74 ? 312 PHE A CE2 1 ATOM 2337 C CZ . PHE A 1 312 ? 24.814 -8.710 12.180 1.00 27.41 ? 312 PHE A CZ 1 ATOM 2338 N N . SER A 1 313 ? 28.865 -12.435 7.144 1.00 28.71 ? 313 SER A N 1 ATOM 2339 C CA . SER A 1 313 ? 29.418 -13.565 6.416 1.00 34.83 ? 313 SER A CA 1 ATOM 2340 C C . SER A 1 313 ? 30.749 -13.292 5.737 1.00 30.78 ? 313 SER A C 1 ATOM 2341 O O . SER A 1 313 ? 31.203 -12.161 5.596 1.00 33.18 ? 313 SER A O 1 ATOM 2342 C CB . SER A 1 313 ? 28.409 -14.023 5.338 1.00 34.56 ? 313 SER A CB 1 ATOM 2343 O OG . SER A 1 313 ? 28.553 -13.200 4.182 1.00 37.02 ? 313 SER A OG 1 ATOM 2344 N N . ASN A 1 314 ? 31.384 -14.377 5.277 1.00 35.44 ? 314 ASN A N 1 ATOM 2345 C CA . ASN A 1 314 ? 32.668 -14.299 4.599 1.00 34.15 ? 314 ASN A CA 1 ATOM 2346 C C . ASN A 1 314 ? 32.645 -13.402 3.378 1.00 36.20 ? 314 ASN A C 1 ATOM 2347 O O . ASN A 1 314 ? 33.693 -12.906 2.943 1.00 41.99 ? 314 ASN A O 1 ATOM 2348 C CB . ASN A 1 314 ? 33.151 -15.707 4.218 1.00 33.37 ? 314 ASN A CB 1 ATOM 2349 C CG . ASN A 1 314 ? 33.395 -16.558 5.445 1.00 32.68 ? 314 ASN A CG 1 ATOM 2350 O OD1 . ASN A 1 314 ? 33.848 -16.051 6.479 1.00 36.76 ? 314 ASN A OD1 1 ATOM 2351 N ND2 . ASN A 1 314 ? 33.095 -17.841 5.370 1.00 32.56 ? 314 ASN A ND2 1 ATOM 2352 N N . GLY A 1 315 ? 31.467 -13.161 2.809 1.00 39.03 ? 315 GLY A N 1 ATOM 2353 C CA . GLY A 1 315 ? 31.377 -12.298 1.629 1.00 39.00 ? 315 GLY A CA 1 ATOM 2354 C C . GLY A 1 315 ? 31.258 -10.831 1.999 1.00 40.12 ? 315 GLY A C 1 ATOM 2355 O O . GLY A 1 315 ? 31.095 -9.970 1.125 1.00 36.91 ? 315 GLY A O 1 ATOM 2356 N N . ALA A 1 316 ? 31.334 -10.514 3.291 1.00 36.46 ? 316 ALA A N 1 ATOM 2357 C CA . ALA A 1 316 ? 31.178 -9.148 3.749 1.00 38.75 ? 316 ALA A CA 1 ATOM 2358 C C . ALA A 1 316 ? 32.115 -8.156 3.081 1.00 39.55 ? 316 ALA A C 1 ATOM 2359 O O . ALA A 1 316 ? 33.335 -8.331 3.052 1.00 38.07 ? 316 ALA A O 1 ATOM 2360 C CB . ALA A 1 316 ? 31.345 -9.062 5.266 1.00 40.91 ? 316 ALA A CB 1 ATOM 2361 N N . ASP A 1 317 ? 31.527 -7.080 2.559 1.00 34.81 ? 317 ASP A N 1 ATOM 2362 C CA . ASP A 1 317 ? 32.331 -6.024 1.943 1.00 36.51 ? 317 ASP A CA 1 ATOM 2363 C C . ASP A 1 317 ? 32.502 -4.910 2.985 1.00 36.05 ? 317 ASP A C 1 ATOM 2364 O O . ASP A 1 317 ? 31.698 -3.988 3.050 1.00 34.33 ? 317 ASP A O 1 ATOM 2365 C CB . ASP A 1 317 ? 31.709 -5.479 0.672 1.00 37.11 ? 317 ASP A CB 1 ATOM 2366 C CG . ASP A 1 317 ? 32.653 -4.556 -0.083 1.00 39.00 ? 317 ASP A CG 1 ATOM 2367 O OD1 . ASP A 1 317 ? 33.479 -3.883 0.569 1.00 39.10 ? 317 ASP A OD1 1 ATOM 2368 O OD2 . ASP A 1 317 ? 32.564 -4.509 -1.326 1.00 39.80 ? 317 ASP A OD2 1 ATOM 2369 N N . LEU A 1 318 ? 33.517 -5.070 3.826 1.00 34.36 ? 318 LEU A N 1 ATOM 2370 C CA . LEU A 1 318 ? 33.791 -4.088 4.876 1.00 34.42 ? 318 LEU A CA 1 ATOM 2371 C C . LEU A 1 318 ? 35.049 -3.299 4.525 1.00 36.44 ? 318 LEU A C 1 ATOM 2372 O O . LEU A 1 318 ? 35.830 -2.911 5.385 1.00 33.15 ? 318 LEU A O 1 ATOM 2373 C CB . LEU A 1 318 ? 33.930 -4.790 6.226 1.00 34.03 ? 318 LEU A CB 1 ATOM 2374 C CG . LEU A 1 318 ? 32.608 -5.116 6.934 1.00 33.42 ? 318 LEU A CG 1 ATOM 2375 C CD1 . LEU A 1 318 ? 32.724 -6.381 7.759 1.00 32.76 ? 318 LEU A CD1 1 ATOM 2376 C CD2 . LEU A 1 318 ? 32.181 -3.941 7.809 1.00 32.10 ? 318 LEU A CD2 1 ATOM 2377 N N . SER A 1 319 ? 35.204 -3.064 3.223 1.00 31.09 ? 319 SER A N 1 ATOM 2378 C CA . SER A 1 319 ? 36.341 -2.354 2.679 1.00 36.99 ? 319 SER A CA 1 ATOM 2379 C C . SER A 1 319 ? 36.455 -0.932 3.198 1.00 39.55 ? 319 SER A C 1 ATOM 2380 O O . SER A 1 319 ? 37.479 -0.270 2.995 1.00 41.58 ? 319 SER A O 1 ATOM 2381 C CB . SER A 1 319 ? 36.272 -2.360 1.146 1.00 35.85 ? 319 SER A CB 1 ATOM 2382 O OG . SER A 1 319 ? 35.123 -1.655 0.693 1.00 38.56 ? 319 SER A OG 1 ATOM 2383 N N . GLY A 1 320 ? 35.414 -0.453 3.874 1.00 40.03 ? 320 GLY A N 1 ATOM 2384 C CA . GLY A 1 320 ? 35.460 0.913 4.427 1.00 32.62 ? 320 GLY A CA 1 ATOM 2385 C C . GLY A 1 320 ? 36.081 0.834 5.831 1.00 24.36 ? 320 GLY A C 1 ATOM 2386 O O . GLY A 1 320 ? 36.453 1.845 6.407 1.00 35.32 ? 320 GLY A O 1 ATOM 2387 N N . VAL A 1 321 ? 36.151 -0.391 6.355 1.00 33.28 ? 321 VAL A N 1 ATOM 2388 C CA . VAL A 1 321 ? 36.728 -0.608 7.681 1.00 35.13 ? 321 VAL A CA 1 ATOM 2389 C C . VAL A 1 321 ? 38.219 -0.943 7.568 1.00 35.60 ? 321 VAL A C 1 ATOM 2390 O O . VAL A 1 321 ? 39.075 -0.341 8.197 1.00 34.04 ? 321 VAL A O 1 ATOM 2391 C CB . VAL A 1 321 ? 36.044 -1.786 8.406 1.00 32.69 ? 321 VAL A CB 1 ATOM 2392 C CG1 . VAL A 1 321 ? 36.650 -1.987 9.788 1.00 31.87 ? 321 VAL A CG1 1 ATOM 2393 C CG2 . VAL A 1 321 ? 34.549 -1.553 8.502 1.00 32.66 ? 321 VAL A CG2 1 ATOM 2394 N N . THR A 1 322 ? 38.484 -1.969 6.775 1.00 42.33 ? 322 THR A N 1 ATOM 2395 C CA . THR A 1 322 ? 39.846 -2.450 6.530 1.00 44.49 ? 322 THR A CA 1 ATOM 2396 C C . THR A 1 322 ? 39.983 -2.607 5.015 1.00 44.95 ? 322 THR A C 1 ATOM 2397 O O . THR A 1 322 ? 39.123 -3.206 4.366 1.00 45.44 ? 322 THR A O 1 ATOM 2398 C CB . THR A 1 322 ? 40.155 -3.742 7.274 1.00 44.81 ? 322 THR A CB 1 ATOM 2399 O OG1 . THR A 1 322 ? 41.570 -3.825 7.525 1.00 46.04 ? 322 THR A OG1 1 ATOM 2400 C CG2 . THR A 1 322 ? 39.714 -4.967 6.491 1.00 44.80 ? 322 THR A CG2 1 ATOM 2401 N N . GLU A 1 323 ? 41.001 -1.993 4.450 1.00 46.35 ? 323 GLU A N 1 ATOM 2402 C CA . GLU A 1 323 ? 41.227 -1.950 3.029 1.00 51.65 ? 323 GLU A CA 1 ATOM 2403 C C . GLU A 1 323 ? 41.769 -3.178 2.353 1.00 51.72 ? 323 GLU A C 1 ATOM 2404 O O . GLU A 1 323 ? 41.396 -3.415 1.185 1.00 53.92 ? 323 GLU A O 1 ATOM 2405 C CB . GLU A 1 323 ? 42.161 -0.751 2.730 1.00 52.32 ? 323 GLU A CB 1 ATOM 2406 C CG . GLU A 1 323 ? 41.913 -0.131 1.365 1.00 54.96 ? 323 GLU A CG 1 ATOM 2407 C CD . GLU A 1 323 ? 42.319 1.332 1.333 1.00 56.63 ? 323 GLU A CD 1 ATOM 2408 O OE1 . GLU A 1 323 ? 41.806 2.097 2.179 1.00 56.45 ? 323 GLU A OE1 1 ATOM 2409 O OE2 . GLU A 1 323 ? 43.139 1.712 0.476 1.00 57.61 ? 323 GLU A OE2 1 ATOM 2410 N N . GLU A 1 324 ? 42.647 -3.957 2.974 1.00 49.96 ? 324 GLU A N 1 ATOM 2411 C CA . GLU A 1 324 ? 43.253 -5.086 2.292 1.00 49.82 ? 324 GLU A CA 1 ATOM 2412 C C . GLU A 1 324 ? 42.928 -6.464 2.808 1.00 45.19 ? 324 GLU A C 1 ATOM 2413 O O . GLU A 1 324 ? 43.032 -7.429 2.023 1.00 40.61 ? 324 GLU A O 1 ATOM 2414 C CB . GLU A 1 324 ? 44.791 -4.909 2.291 1.00 52.03 ? 324 GLU A CB 1 ATOM 2415 C CG . GLU A 1 324 ? 45.258 -3.687 1.524 1.00 55.47 ? 324 GLU A CG 1 ATOM 2416 C CD . GLU A 1 324 ? 44.852 -3.714 0.065 1.00 57.83 ? 324 GLU A CD 1 ATOM 2417 O OE1 . GLU A 1 324 ? 43.659 -3.483 -0.225 1.00 59.61 ? 324 GLU A OE1 1 ATOM 2418 O OE2 . GLU A 1 324 ? 45.721 -3.963 -0.798 1.00 58.71 ? 324 GLU A OE2 1 ATOM 2419 N N . ALA A 1 325 ? 42.579 -6.629 4.073 1.00 36.26 ? 325 ALA A N 1 ATOM 2420 C CA . ALA A 1 325 ? 42.300 -7.951 4.613 1.00 38.22 ? 325 ALA A CA 1 ATOM 2421 C C . ALA A 1 325 ? 40.820 -8.281 4.720 1.00 38.37 ? 325 ALA A C 1 ATOM 2422 O O . ALA A 1 325 ? 39.980 -7.415 4.947 1.00 41.59 ? 325 ALA A O 1 ATOM 2423 C CB . ALA A 1 325 ? 42.964 -8.089 5.984 1.00 35.81 ? 325 ALA A CB 1 ATOM 2424 N N . PRO A 1 326 ? 40.497 -9.561 4.563 1.00 36.20 ? 326 PRO A N 1 ATOM 2425 C CA . PRO A 1 326 ? 39.135 -10.049 4.677 1.00 36.17 ? 326 PRO A CA 1 ATOM 2426 C C . PRO A 1 326 ? 38.580 -9.679 6.056 1.00 36.27 ? 326 PRO A C 1 ATOM 2427 O O . PRO A 1 326 ? 39.342 -9.618 7.023 1.00 29.46 ? 326 PRO A O 1 ATOM 2428 C CB . PRO A 1 326 ? 39.260 -11.559 4.553 1.00 32.28 ? 326 PRO A CB 1 ATOM 2429 C CG . PRO A 1 326 ? 40.569 -11.793 3.888 1.00 37.81 ? 326 PRO A CG 1 ATOM 2430 C CD . PRO A 1 326 ? 41.461 -10.657 4.303 1.00 37.21 ? 326 PRO A CD 1 ATOM 2431 N N . LEU A 1 327 ? 37.280 -9.435 6.130 1.00 33.54 ? 327 LEU A N 1 ATOM 2432 C CA . LEU A 1 327 ? 36.668 -9.058 7.401 1.00 33.20 ? 327 LEU A CA 1 ATOM 2433 C C . LEU A 1 327 ? 35.167 -9.313 7.395 1.00 32.07 ? 327 LEU A C 1 ATOM 2434 O O . LEU A 1 327 ? 34.509 -9.253 6.364 1.00 34.26 ? 327 LEU A O 1 ATOM 2435 C CB . LEU A 1 327 ? 36.941 -7.572 7.677 1.00 30.51 ? 327 LEU A CB 1 ATOM 2436 C CG . LEU A 1 327 ? 36.464 -7.029 9.025 1.00 30.17 ? 327 LEU A CG 1 ATOM 2437 C CD1 . LEU A 1 327 ? 37.105 -7.801 10.167 1.00 30.98 ? 327 LEU A CD1 1 ATOM 2438 C CD2 . LEU A 1 327 ? 36.764 -5.539 9.146 1.00 28.84 ? 327 LEU A CD2 1 ATOM 2439 N N . LYS A 1 328 ? 34.628 -9.591 8.573 1.00 32.22 ? 328 LYS A N 1 ATOM 2440 C CA . LYS A 1 328 ? 33.207 -9.816 8.764 1.00 35.70 ? 328 LYS A CA 1 ATOM 2441 C C . LYS A 1 328 ? 32.873 -9.610 10.249 1.00 30.66 ? 328 LYS A C 1 ATOM 2442 O O . LYS A 1 328 ? 33.771 -9.697 11.081 1.00 22.78 ? 328 LYS A O 1 ATOM 2443 C CB . LYS A 1 328 ? 32.777 -11.217 8.342 1.00 32.45 ? 328 LYS A CB 1 ATOM 2444 C CG . LYS A 1 328 ? 33.239 -12.300 9.303 1.00 37.32 ? 328 LYS A CG 1 ATOM 2445 C CD . LYS A 1 328 ? 32.655 -13.658 8.941 1.00 37.44 ? 328 LYS A CD 1 ATOM 2446 C CE . LYS A 1 328 ? 33.399 -14.771 9.668 1.00 39.09 ? 328 LYS A CE 1 ATOM 2447 N NZ . LYS A 1 328 ? 32.903 -16.114 9.254 1.00 42.81 ? 328 LYS A NZ 1 ATOM 2448 N N . LEU A 1 329 ? 31.609 -9.339 10.533 1.00 29.15 ? 329 LEU A N 1 ATOM 2449 C CA . LEU A 1 329 ? 31.203 -9.154 11.947 1.00 27.26 ? 329 LEU A CA 1 ATOM 2450 C C . LEU A 1 329 ? 30.730 -10.505 12.471 1.00 27.51 ? 329 LEU A C 1 ATOM 2451 O O . LEU A 1 329 ? 29.693 -11.010 12.036 1.00 31.87 ? 329 LEU A O 1 ATOM 2452 C CB . LEU A 1 329 ? 30.142 -8.086 12.032 1.00 26.49 ? 329 LEU A CB 1 ATOM 2453 C CG . LEU A 1 329 ? 29.644 -7.606 13.387 1.00 25.78 ? 329 LEU A CG 1 ATOM 2454 C CD1 . LEU A 1 329 ? 30.780 -7.045 14.234 1.00 22.03 ? 329 LEU A CD1 1 ATOM 2455 C CD2 . LEU A 1 329 ? 28.557 -6.543 13.185 1.00 22.69 ? 329 LEU A CD2 1 ATOM 2456 N N . SER A 1 330 ? 31.513 -11.127 13.348 1.00 26.97 ? 330 SER A N 1 ATOM 2457 C CA . SER A 1 330 ? 31.166 -12.451 13.852 1.00 32.88 ? 330 SER A CA 1 ATOM 2458 C C . SER A 1 330 ? 30.349 -12.400 15.130 1.00 32.27 ? 330 SER A C 1 ATOM 2459 O O . SER A 1 330 ? 29.740 -13.406 15.503 1.00 37.28 ? 330 SER A O 1 ATOM 2460 C CB . SER A 1 330 ? 32.434 -13.282 14.085 1.00 33.05 ? 330 SER A CB 1 ATOM 2461 O OG . SER A 1 330 ? 33.513 -12.422 14.417 1.00 38.94 ? 330 SER A OG 1 ATOM 2462 N N . LYS A 1 331 ? 30.346 -11.251 15.795 1.00 28.17 ? 331 LYS A N 1 ATOM 2463 C CA . LYS A 1 331 ? 29.601 -11.103 17.037 1.00 35.75 ? 331 LYS A CA 1 ATOM 2464 C C . LYS A 1 331 ? 28.898 -9.748 17.109 1.00 32.23 ? 331 LYS A C 1 ATOM 2465 O O . LYS A 1 331 ? 29.493 -8.719 16.815 1.00 31.72 ? 331 LYS A O 1 ATOM 2466 C CB . LYS A 1 331 ? 30.532 -11.233 18.250 1.00 35.71 ? 331 LYS A CB 1 ATOM 2467 C CG . LYS A 1 331 ? 29.782 -11.540 19.545 1.00 37.81 ? 331 LYS A CG 1 ATOM 2468 C CD . LYS A 1 331 ? 29.449 -13.023 19.615 1.00 38.44 ? 331 LYS A CD 1 ATOM 2469 C CE . LYS A 1 331 ? 28.531 -13.340 20.777 1.00 39.67 ? 331 LYS A CE 1 ATOM 2470 N NZ . LYS A 1 331 ? 28.855 -12.536 21.985 1.00 42.71 ? 331 LYS A NZ 1 ATOM 2471 N N . ALA A 1 332 ? 27.636 -9.779 17.513 1.00 29.29 ? 332 ALA A N 1 ATOM 2472 C CA . ALA A 1 332 ? 26.844 -8.554 17.641 1.00 31.04 ? 332 ALA A CA 1 ATOM 2473 C C . ALA A 1 332 ? 25.770 -8.797 18.705 1.00 28.91 ? 332 ALA A C 1 ATOM 2474 O O . ALA A 1 332 ? 24.884 -9.629 18.526 1.00 27.04 ? 332 ALA A O 1 ATOM 2475 C CB . ALA A 1 332 ? 26.248 -8.136 16.319 1.00 29.34 ? 332 ALA A CB 1 ATOM 2476 N N . VAL A 1 333 ? 25.899 -8.094 19.825 1.00 32.09 ? 333 VAL A N 1 ATOM 2477 C CA . VAL A 1 333 ? 24.965 -8.278 20.931 1.00 32.81 ? 333 VAL A CA 1 ATOM 2478 C C . VAL A 1 333 ? 24.321 -6.968 21.369 1.00 29.46 ? 333 VAL A C 1 ATOM 2479 O O . VAL A 1 333 ? 24.929 -5.910 21.332 1.00 25.88 ? 333 VAL A O 1 ATOM 2480 C CB . VAL A 1 333 ? 25.692 -8.888 22.152 1.00 32.33 ? 333 VAL A CB 1 ATOM 2481 C CG1 . VAL A 1 333 ? 24.693 -9.349 23.201 1.00 33.89 ? 333 VAL A CG1 1 ATOM 2482 C CG2 . VAL A 1 333 ? 26.598 -10.024 21.713 1.00 33.70 ? 333 VAL A CG2 1 ATOM 2483 N N . HIS A 1 334 ? 23.074 -7.076 21.803 1.00 32.72 ? 334 HIS A N 1 ATOM 2484 C CA . HIS A 1 334 ? 22.309 -5.937 22.285 1.00 28.57 ? 334 HIS A CA 1 ATOM 2485 C C . HIS A 1 334 ? 21.632 -6.314 23.607 1.00 26.06 ? 334 HIS A C 1 ATOM 2486 O O . HIS A 1 334 ? 21.017 -7.372 23.710 1.00 26.11 ? 334 HIS A O 1 ATOM 2487 C CB . HIS A 1 334 ? 21.258 -5.501 21.275 1.00 30.45 ? 334 HIS A CB 1 ATOM 2488 C CG . HIS A 1 334 ? 20.265 -4.493 21.757 1.00 30.10 ? 334 HIS A CG 1 ATOM 2489 N ND1 . HIS A 1 334 ? 20.596 -3.199 22.075 1.00 29.24 ? 334 HIS A ND1 1 ATOM 2490 C CD2 . HIS A 1 334 ? 18.929 -4.597 21.973 1.00 30.82 ? 334 HIS A CD2 1 ATOM 2491 C CE1 . HIS A 1 334 ? 19.516 -2.544 22.461 1.00 29.34 ? 334 HIS A CE1 1 ATOM 2492 N NE2 . HIS A 1 334 ? 18.489 -3.367 22.412 1.00 29.57 ? 334 HIS A NE2 1 ATOM 2493 N N . LYS A 1 335 ? 21.767 -5.440 24.589 1.00 28.42 ? 335 LYS A N 1 ATOM 2494 C CA . LYS A 1 335 ? 21.151 -5.626 25.886 1.00 31.73 ? 335 LYS A CA 1 ATOM 2495 C C . LYS A 1 335 ? 20.442 -4.326 26.296 1.00 28.29 ? 335 LYS A C 1 ATOM 2496 O O . LYS A 1 335 ? 21.051 -3.264 26.297 1.00 26.74 ? 335 LYS A O 1 ATOM 2497 C CB . LYS A 1 335 ? 22.145 -6.030 26.977 1.00 33.48 ? 335 LYS A CB 1 ATOM 2498 C CG . LYS A 1 335 ? 21.428 -6.288 28.308 1.00 36.43 ? 335 LYS A CG 1 ATOM 2499 C CD . LYS A 1 335 ? 22.273 -7.121 29.255 1.00 38.43 ? 335 LYS A CD 1 ATOM 2500 C CE . LYS A 1 335 ? 21.421 -7.618 30.419 1.00 41.62 ? 335 LYS A CE 1 ATOM 2501 N NZ . LYS A 1 335 ? 22.250 -8.110 31.552 1.00 42.87 ? 335 LYS A NZ 1 ATOM 2502 N N . ALA A 1 336 ? 19.163 -4.443 26.607 1.00 28.32 ? 336 ALA A N 1 ATOM 2503 C CA . ALA A 1 336 ? 18.355 -3.298 27.011 1.00 24.81 ? 336 ALA A CA 1 ATOM 2504 C C . ALA A 1 336 ? 17.825 -3.532 28.425 1.00 27.73 ? 336 ALA A C 1 ATOM 2505 O O . ALA A 1 336 ? 17.231 -4.578 28.692 1.00 27.56 ? 336 ALA A O 1 ATOM 2506 C CB . ALA A 1 336 ? 17.201 -3.082 26.038 1.00 22.21 ? 336 ALA A CB 1 ATOM 2507 N N . VAL A 1 337 ? 18.063 -2.570 29.312 1.00 29.24 ? 337 VAL A N 1 ATOM 2508 C CA . VAL A 1 337 ? 17.598 -2.728 30.693 1.00 30.87 ? 337 VAL A CA 1 ATOM 2509 C C . VAL A 1 337 ? 16.646 -1.594 31.060 1.00 27.45 ? 337 VAL A C 1 ATOM 2510 O O . VAL A 1 337 ? 16.940 -0.419 30.856 1.00 28.29 ? 337 VAL A O 1 ATOM 2511 C CB . VAL A 1 337 ? 18.751 -2.797 31.694 1.00 32.12 ? 337 VAL A CB 1 ATOM 2512 C CG1 . VAL A 1 337 ? 18.242 -2.933 33.130 1.00 31.63 ? 337 VAL A CG1 1 ATOM 2513 C CG2 . VAL A 1 337 ? 19.664 -3.980 31.360 1.00 29.97 ? 337 VAL A CG2 1 ATOM 2514 N N . LEU A 1 338 ? 15.490 -1.980 31.586 1.00 28.18 ? 338 LEU A N 1 ATOM 2515 C CA . LEU A 1 338 ? 14.472 -1.042 31.990 1.00 34.49 ? 338 LEU A CA 1 ATOM 2516 C C . LEU A 1 338 ? 14.045 -1.244 33.444 1.00 33.84 ? 338 LEU A C 1 ATOM 2517 O O . LEU A 1 338 ? 13.745 -2.362 33.859 1.00 33.82 ? 338 LEU A O 1 ATOM 2518 C CB . LEU A 1 338 ? 13.235 -1.192 31.084 1.00 37.37 ? 338 LEU A CB 1 ATOM 2519 C CG . LEU A 1 338 ? 11.959 -0.513 31.614 1.00 37.28 ? 338 LEU A CG 1 ATOM 2520 C CD1 . LEU A 1 338 ? 12.038 0.986 31.419 1.00 34.87 ? 338 LEU A CD1 1 ATOM 2521 C CD2 . LEU A 1 338 ? 10.737 -1.109 30.942 1.00 36.95 ? 338 LEU A CD2 1 ATOM 2522 N N . THR A 1 339 ? 14.014 -0.148 34.190 1.00 29.98 ? 339 THR A N 1 ATOM 2523 C CA . THR A 1 339 ? 13.560 -0.152 35.570 1.00 35.37 ? 339 THR A CA 1 ATOM 2524 C C . THR A 1 339 ? 12.369 0.818 35.697 1.00 33.28 ? 339 THR A C 1 ATOM 2525 O O . THR A 1 339 ? 12.495 1.982 35.332 1.00 30.90 ? 339 THR A O 1 ATOM 2526 C CB . THR A 1 339 ? 14.633 0.302 36.575 1.00 34.46 ? 339 THR A CB 1 ATOM 2527 O OG1 . THR A 1 339 ? 15.641 -0.707 36.697 1.00 39.44 ? 339 THR A OG1 1 ATOM 2528 C CG2 . THR A 1 339 ? 14.012 0.539 37.946 1.00 35.79 ? 339 THR A CG2 1 ATOM 2529 N N . ILE A 1 340 ? 11.248 0.332 36.198 1.00 34.34 ? 340 ILE A N 1 ATOM 2530 C CA . ILE A 1 340 ? 10.072 1.185 36.385 1.00 34.83 ? 340 ILE A CA 1 ATOM 2531 C C . ILE A 1 340 ? 9.686 1.195 37.867 1.00 33.70 ? 340 ILE A C 1 ATOM 2532 O O . ILE A 1 340 ? 9.436 0.117 38.418 1.00 24.90 ? 340 ILE A O 1 ATOM 2533 C CB . ILE A 1 340 ? 8.858 0.693 35.585 1.00 35.73 ? 340 ILE A CB 1 ATOM 2534 C CG1 . ILE A 1 340 ? 8.992 1.032 34.094 1.00 37.54 ? 340 ILE A CG1 1 ATOM 2535 C CG2 . ILE A 1 340 ? 7.580 1.295 36.160 1.00 34.60 ? 340 ILE A CG2 1 ATOM 2536 C CD1 . ILE A 1 340 ? 9.189 2.519 33.835 1.00 37.92 ? 340 ILE A CD1 1 ATOM 2537 N N . ASP A 1 341 ? 9.638 2.372 38.473 1.00 32.91 ? 341 ASP A N 1 ATOM 2538 C CA . ASP A 1 341 ? 9.258 2.469 39.888 1.00 32.45 ? 341 ASP A CA 1 ATOM 2539 C C . ASP A 1 341 ? 8.495 3.763 40.154 1.00 31.75 ? 341 ASP A C 1 ATOM 2540 O O . ASP A 1 341 ? 8.172 4.509 39.223 1.00 26.22 ? 341 ASP A O 1 ATOM 2541 C CB . ASP A 1 341 ? 10.482 2.324 40.783 1.00 35.04 ? 341 ASP A CB 1 ATOM 2542 C CG . ASP A 1 341 ? 11.476 3.454 40.592 1.00 35.45 ? 341 ASP A CG 1 ATOM 2543 O OD1 . ASP A 1 341 ? 11.124 4.427 39.895 1.00 36.68 ? 341 ASP A OD1 1 ATOM 2544 O OD2 . ASP A 1 341 ? 12.593 3.365 41.134 1.00 37.93 ? 341 ASP A OD2 1 ATOM 2545 N N . GLU A 1 342 ? 8.159 4.036 41.399 1.00 31.47 ? 342 GLU A N 1 ATOM 2546 C CA . GLU A 1 342 ? 7.383 5.173 41.830 1.00 29.75 ? 342 GLU A CA 1 ATOM 2547 C C . GLU A 1 342 ? 7.934 6.523 41.384 1.00 34.22 ? 342 GLU A C 1 ATOM 2548 O O . GLU A 1 342 ? 7.208 7.399 40.921 1.00 28.16 ? 342 GLU A O 1 ATOM 2549 C CB . GLU A 1 342 ? 7.273 5.194 43.366 1.00 30.76 ? 342 GLU A CB 1 ATOM 2550 C CG . GLU A 1 342 ? 6.557 4.004 43.963 1.00 28.79 ? 342 GLU A CG 1 ATOM 2551 C CD . GLU A 1 342 ? 7.436 2.798 44.200 1.00 31.12 ? 342 GLU A CD 1 ATOM 2552 O OE1 . GLU A 1 342 ? 8.620 2.789 43.798 1.00 29.63 ? 342 GLU A OE1 1 ATOM 2553 O OE2 . GLU A 1 342 ? 6.925 1.824 44.807 1.00 30.27 ? 342 GLU A OE2 1 ATOM 2554 N N . LYS A 1 343 ? 9.217 6.701 41.598 1.00 35.32 ? 343 LYS A N 1 ATOM 2555 C CA . LYS A 1 343 ? 9.960 7.901 41.282 1.00 44.21 ? 343 LYS A CA 1 ATOM 2556 C C . LYS A 1 343 ? 11.339 7.449 40.777 1.00 52.45 ? 343 LYS A C 1 ATOM 2557 O O . LYS A 1 343 ? 11.892 6.497 41.334 1.00 59.58 ? 343 LYS A O 1 ATOM 2558 C CB . LYS A 1 343 ? 10.143 8.798 42.504 1.00 43.95 ? 343 LYS A CB 1 ATOM 2559 C CG . LYS A 1 343 ? 8.937 9.614 42.911 1.00 45.23 ? 343 LYS A CG 1 ATOM 2560 C CD . LYS A 1 343 ? 9.173 10.396 44.189 1.00 46.19 ? 343 LYS A CD 1 ATOM 2561 C CE . LYS A 1 343 ? 10.454 11.212 44.131 1.00 48.18 ? 343 LYS A CE 1 ATOM 2562 N NZ . LYS A 1 343 ? 10.508 12.225 45.227 1.00 49.28 ? 343 LYS A NZ 1 ATOM 2563 N N . GLY A 1 344 ? 11.843 8.105 39.748 1.00 58.65 ? 344 GLY A N 1 ATOM 2564 C CA . GLY A 1 344 ? 13.147 7.717 39.206 1.00 67.77 ? 344 GLY A CA 1 ATOM 2565 C C . GLY A 1 344 ? 14.273 8.087 40.161 1.00 71.61 ? 344 GLY A C 1 ATOM 2566 O O . GLY A 1 344 ? 15.391 7.587 40.029 1.00 74.42 ? 344 GLY A O 1 ATOM 2567 N N . THR A 1 345 ? 13.978 8.960 41.122 1.00 75.99 ? 345 THR A N 1 ATOM 2568 C CA . THR A 1 345 ? 14.986 9.409 42.069 1.00 78.83 ? 345 THR A CA 1 ATOM 2569 C C . THR A 1 345 ? 14.421 9.711 43.449 1.00 80.26 ? 345 THR A C 1 ATOM 2570 O O . THR A 1 345 ? 13.216 9.851 43.634 1.00 84.38 ? 345 THR A O 1 ATOM 2571 C CB . THR A 1 345 ? 15.673 10.698 41.549 1.00 79.35 ? 345 THR A CB 1 ATOM 2572 O OG1 . THR A 1 345 ? 16.674 11.103 42.489 1.00 80.23 ? 345 THR A OG1 1 ATOM 2573 C CG2 . THR A 1 345 ? 14.643 11.806 41.395 1.00 79.32 ? 345 THR A CG2 1 ATOM 2574 N N . GLU A 1 346 ? 15.325 9.834 44.419 1.00 80.85 ? 346 GLU A N 1 ATOM 2575 C CA . GLU A 1 346 ? 14.942 10.154 45.791 1.00 80.98 ? 346 GLU A CA 1 ATOM 2576 C C . GLU A 1 346 ? 14.787 11.671 45.933 1.00 79.87 ? 346 GLU A C 1 ATOM 2577 O O . GLU A 1 346 ? 14.405 12.179 46.980 1.00 78.77 ? 346 GLU A O 1 ATOM 2578 C CB . GLU A 1 346 ? 15.987 9.645 46.779 1.00 81.47 ? 346 GLU A CB 1 ATOM 2579 C CG . GLU A 1 346 ? 16.222 8.145 46.734 1.00 82.28 ? 346 GLU A CG 1 ATOM 2580 C CD . GLU A 1 346 ? 17.372 7.713 47.624 1.00 82.99 ? 346 GLU A CD 1 ATOM 2581 O OE1 . GLU A 1 346 ? 18.524 8.101 47.332 1.00 83.32 ? 346 GLU A OE1 1 ATOM 2582 O OE2 . GLU A 1 346 ? 17.126 6.990 48.611 1.00 83.49 ? 346 GLU A OE2 1 ATOM 2583 N N . ALA A 1 347 ? 15.100 12.375 44.848 1.00 78.27 ? 347 ALA A N 1 ATOM 2584 C CA . ALA A 1 347 ? 15.004 13.828 44.819 1.00 77.38 ? 347 ALA A CA 1 ATOM 2585 C C . ALA A 1 347 ? 13.554 14.275 44.645 1.00 78.15 ? 347 ALA A C 1 ATOM 2586 O O . ALA A 1 347 ? 13.032 14.284 43.530 1.00 81.42 ? 347 ALA A O 1 ATOM 2587 C CB . ALA A 1 347 ? 15.858 14.398 43.696 1.00 76.34 ? 347 ALA A CB 1 ATOM 2588 N N . ALA A 1 348 ? 12.918 14.642 45.750 1.00 76.50 ? 348 ALA A N 1 ATOM 2589 C CA . ALA A 1 348 ? 11.530 15.090 45.722 1.00 77.18 ? 348 ALA A CA 1 ATOM 2590 C C . ALA A 1 348 ? 11.297 16.099 44.601 1.00 75.83 ? 348 ALA A C 1 ATOM 2591 O O . ALA A 1 348 ? 12.023 17.084 44.473 1.00 74.71 ? 348 ALA A O 1 ATOM 2592 C CB . ALA A 1 348 ? 11.150 15.693 47.067 1.00 76.40 ? 348 ALA A CB 1 ATOM 2593 N N . GLY A 1 349 ? 10.276 15.849 43.787 1.00 77.00 ? 349 GLY A N 1 ATOM 2594 C CA . GLY A 1 349 ? 9.948 16.728 42.673 1.00 77.28 ? 349 GLY A CA 1 ATOM 2595 C C . GLY A 1 349 ? 9.009 17.848 43.107 1.00 77.02 ? 349 GLY A C 1 ATOM 2596 O O . GLY A 1 349 ? 8.297 17.728 44.105 1.00 78.45 ? 349 GLY A O 1 ATOM 2597 N N . ALA A 1 350 ? 9.019 18.941 42.348 1.00 73.29 ? 350 ALA A N 1 ATOM 2598 C CA . ALA A 1 350 ? 8.145 20.075 42.668 1.00 70.55 ? 350 ALA A CA 1 ATOM 2599 C C . ALA A 1 350 ? 6.706 19.573 42.782 1.00 65.66 ? 350 ALA A C 1 ATOM 2600 O O . ALA A 1 350 ? 6.291 18.668 42.057 1.00 61.31 ? 350 ALA A O 1 ATOM 2601 C CB . ALA A 1 350 ? 8.272 21.153 41.613 1.00 71.61 ? 350 ALA A CB 1 ATOM 2602 N N . MET A 1 351 ? 5.953 20.144 43.705 1.00 60.33 ? 351 MET A N 1 ATOM 2603 C CA . MET A 1 351 ? 4.578 19.755 43.947 1.00 55.77 ? 351 MET A CA 1 ATOM 2604 C C . MET A 1 351 ? 3.596 20.354 42.956 1.00 51.41 ? 351 MET A C 1 ATOM 2605 O O . MET A 1 351 ? 3.806 21.409 42.364 1.00 55.62 ? 351 MET A O 1 ATOM 2606 C CB . MET A 1 351 ? 4.180 20.123 45.390 1.00 58.94 ? 351 MET A CB 1 ATOM 2607 C CG . MET A 1 351 ? 5.083 19.467 46.431 1.00 61.88 ? 351 MET A CG 1 ATOM 2608 S SD . MET A 1 351 ? 4.415 19.538 48.101 1.00 64.31 ? 351 MET A SD 1 ATOM 2609 C CE . MET A 1 351 ? 4.133 21.308 48.268 1.00 64.71 ? 351 MET A CE 1 ATOM 2610 N N . PHE A 1 352 ? 2.488 19.650 42.761 1.00 40.28 ? 352 PHE A N 1 ATOM 2611 C CA . PHE A 1 352 ? 1.429 20.087 41.866 1.00 41.98 ? 352 PHE A CA 1 ATOM 2612 C C . PHE A 1 352 ? 0.108 19.533 42.394 1.00 34.12 ? 352 PHE A C 1 ATOM 2613 O O . PHE A 1 352 ? 0.107 18.634 43.240 1.00 40.54 ? 352 PHE A O 1 ATOM 2614 C CB . PHE A 1 352 ? 1.670 19.685 40.414 1.00 40.21 ? 352 PHE A CB 1 ATOM 2615 C CG . PHE A 1 352 ? 1.788 18.205 40.195 1.00 43.66 ? 352 PHE A CG 1 ATOM 2616 C CD1 . PHE A 1 352 ? 0.658 17.432 39.967 1.00 43.50 ? 352 PHE A CD1 1 ATOM 2617 C CD2 . PHE A 1 352 ? 3.028 17.584 40.221 1.00 43.60 ? 352 PHE A CD2 1 ATOM 2618 C CE1 . PHE A 1 352 ? 0.761 16.069 39.771 1.00 42.94 ? 352 PHE A CE1 1 ATOM 2619 C CE2 . PHE A 1 352 ? 3.134 16.219 40.023 1.00 43.52 ? 352 PHE A CE2 1 ATOM 2620 C CZ . PHE A 1 352 ? 2.000 15.463 39.798 1.00 42.96 ? 352 PHE A CZ 1 ATOM 2621 N N . LEU A 1 353 ? -0.986 20.073 41.918 1.00 35.40 ? 353 LEU A N 1 ATOM 2622 C CA . LEU A 1 353 ? -2.317 19.651 42.357 1.00 34.00 ? 353 LEU A CA 1 ATOM 2623 C C . LEU A 1 353 ? -3.184 19.326 41.150 1.00 32.95 ? 353 LEU A C 1 ATOM 2624 O O . LEU A 1 353 ? -3.252 20.162 40.244 1.00 29.60 ? 353 LEU A O 1 ATOM 2625 C CB . LEU A 1 353 ? -2.948 20.824 43.136 1.00 33.26 ? 353 LEU A CB 1 ATOM 2626 C CG . LEU A 1 353 ? -2.201 21.276 44.391 1.00 37.00 ? 353 LEU A CG 1 ATOM 2627 C CD1 . LEU A 1 353 ? -2.956 22.426 45.076 1.00 34.13 ? 353 LEU A CD1 1 ATOM 2628 C CD2 . LEU A 1 353 ? -2.021 20.137 45.386 1.00 36.47 ? 353 LEU A CD2 1 ATOM 2629 N N . GLU A 1 354 ? -3.781 18.137 41.105 1.00 26.00 ? 354 GLU A N 1 ATOM 2630 C CA . GLU A 1 354 ? -4.675 17.807 40.003 1.00 29.23 ? 354 GLU A CA 1 ATOM 2631 C C . GLU A 1 354 ? -6.118 17.888 40.522 1.00 31.03 ? 354 GLU A C 1 ATOM 2632 O O . GLU A 1 354 ? -6.373 17.495 41.664 1.00 34.53 ? 354 GLU A O 1 ATOM 2633 C CB . GLU A 1 354 ? -4.428 16.430 39.412 1.00 31.17 ? 354 GLU A CB 1 ATOM 2634 C CG . GLU A 1 354 ? -3.007 16.102 39.027 1.00 32.53 ? 354 GLU A CG 1 ATOM 2635 C CD . GLU A 1 354 ? -2.834 14.719 38.427 1.00 31.89 ? 354 GLU A CD 1 ATOM 2636 O OE1 . GLU A 1 354 ? -3.483 13.760 38.890 1.00 30.00 ? 354 GLU A OE1 1 ATOM 2637 O OE2 . GLU A 1 354 ? -2.034 14.584 37.475 1.00 31.67 ? 354 GLU A OE2 1 ATOM 2638 N N . ALA A 1 355 ? -7.024 18.377 39.695 1.00 34.47 ? 355 ALA A N 1 ATOM 2639 C CA . ALA A 1 355 ? -8.427 18.487 40.092 1.00 37.79 ? 355 ALA A CA 1 ATOM 2640 C C . ALA A 1 355 ? -9.177 17.213 39.708 1.00 35.48 ? 355 ALA A C 1 ATOM 2641 O O . ALA A 1 355 ? -9.566 17.021 38.556 1.00 34.48 ? 355 ALA A O 1 ATOM 2642 C CB . ALA A 1 355 ? -9.062 19.708 39.446 1.00 36.70 ? 355 ALA A CB 1 ATOM 2643 N N . ILE A 1 356 ? -9.383 16.342 40.688 1.00 40.53 ? 356 ILE A N 1 ATOM 2644 C CA . ILE A 1 356 ? -10.071 15.075 40.459 1.00 41.28 ? 356 ILE A CA 1 ATOM 2645 C C . ILE A 1 356 ? -11.547 15.165 40.809 1.00 43.69 ? 356 ILE A C 1 ATOM 2646 O O . ILE A 1 356 ? -11.922 15.540 41.922 1.00 40.99 ? 356 ILE A O 1 ATOM 2647 C CB . ILE A 1 356 ? -9.400 13.950 41.269 1.00 42.37 ? 356 ILE A CB 1 ATOM 2648 C CG1 . ILE A 1 356 ? -7.905 13.876 40.922 1.00 41.27 ? 356 ILE A CG1 1 ATOM 2649 C CG2 . ILE A 1 356 ? -10.076 12.616 41.007 1.00 43.00 ? 356 ILE A CG2 1 ATOM 2650 C CD1 . ILE A 1 356 ? -7.077 13.174 41.979 1.00 42.61 ? 356 ILE A CD1 1 ATOM 2651 N N . PRO A 1 357 ? -12.403 14.827 39.855 1.00 43.92 ? 357 PRO A N 1 ATOM 2652 C CA . PRO A 1 357 ? -13.840 14.859 40.020 1.00 44.25 ? 357 PRO A CA 1 ATOM 2653 C C . PRO A 1 357 ? -14.322 13.849 41.050 1.00 46.29 ? 357 PRO A C 1 ATOM 2654 O O . PRO A 1 357 ? -13.616 12.898 41.384 1.00 44.67 ? 357 PRO A O 1 ATOM 2655 C CB . PRO A 1 357 ? -14.398 14.552 38.642 1.00 43.89 ? 357 PRO A CB 1 ATOM 2656 C CG . PRO A 1 357 ? -13.259 14.709 37.699 1.00 47.84 ? 357 PRO A CG 1 ATOM 2657 C CD . PRO A 1 357 ? -12.019 14.378 38.490 1.00 45.85 ? 357 PRO A CD 1 ATOM 2658 N N . MET A 1 358 ? -15.534 14.056 41.553 1.00 47.58 ? 358 MET A N 1 ATOM 2659 C CA . MET A 1 358 ? -16.123 13.190 42.555 1.00 49.23 ? 358 MET A CA 1 ATOM 2660 C C . MET A 1 358 ? -16.831 11.978 41.985 1.00 47.57 ? 358 MET A C 1 ATOM 2661 O O . MET A 1 358 ? -17.417 11.196 42.748 1.00 56.55 ? 358 MET A O 1 ATOM 2662 C CB . MET A 1 358 ? -17.074 14.003 43.452 1.00 49.12 ? 358 MET A CB 1 ATOM 2663 C CG . MET A 1 358 ? -17.968 14.967 42.696 1.00 50.23 ? 358 MET A CG 1 ATOM 2664 S SD . MET A 1 358 ? -18.836 16.130 43.773 1.00 51.94 ? 358 MET A SD 1 ATOM 2665 C CE . MET A 1 358 ? -19.737 14.995 44.834 1.00 49.33 ? 358 MET A CE 1 ATOM 2666 N N . SER A 1 359 ? -16.796 11.780 40.671 1.00 50.03 ? 359 SER A N 1 ATOM 2667 C CA . SER A 1 359 ? -17.456 10.622 40.069 1.00 46.57 ? 359 SER A CA 1 ATOM 2668 C C . SER A 1 359 ? -16.588 9.376 40.206 1.00 41.48 ? 359 SER A C 1 ATOM 2669 O O . SER A 1 359 ? -15.392 9.471 40.479 1.00 35.36 ? 359 SER A O 1 ATOM 2670 C CB . SER A 1 359 ? -17.817 10.875 38.615 1.00 47.47 ? 359 SER A CB 1 ATOM 2671 O OG . SER A 1 359 ? -16.728 10.605 37.754 1.00 50.82 ? 359 SER A OG 1 ATOM 2672 N N . ILE A 1 360 ? -17.203 8.205 40.037 1.00 34.80 ? 360 ILE A N 1 ATOM 2673 C CA . ILE A 1 360 ? -16.476 6.949 40.156 1.00 35.28 ? 360 ILE A CA 1 ATOM 2674 C C . ILE A 1 360 ? -15.461 6.806 39.023 1.00 34.12 ? 360 ILE A C 1 ATOM 2675 O O . ILE A 1 360 ? -15.832 6.716 37.855 1.00 30.01 ? 360 ILE A O 1 ATOM 2676 C CB . ILE A 1 360 ? -17.407 5.727 40.143 1.00 34.78 ? 360 ILE A CB 1 ATOM 2677 C CG1 . ILE A 1 360 ? -18.066 5.514 41.501 1.00 33.15 ? 360 ILE A CG1 1 ATOM 2678 C CG2 . ILE A 1 360 ? -16.644 4.484 39.700 1.00 34.50 ? 360 ILE A CG2 1 ATOM 2679 C CD1 . ILE A 1 360 ? -17.104 5.280 42.644 1.00 34.42 ? 360 ILE A CD1 1 ATOM 2680 N N . PRO A 1 361 ? -14.189 6.787 39.380 1.00 36.22 ? 361 PRO A N 1 ATOM 2681 C CA . PRO A 1 361 ? -13.112 6.645 38.416 1.00 32.64 ? 361 PRO A CA 1 ATOM 2682 C C . PRO A 1 361 ? -12.913 5.188 38.038 1.00 34.16 ? 361 PRO A C 1 ATOM 2683 O O . PRO A 1 361 ? -13.007 4.291 38.879 1.00 29.86 ? 361 PRO A O 1 ATOM 2684 C CB . PRO A 1 361 ? -11.905 7.172 39.183 1.00 34.72 ? 361 PRO A CB 1 ATOM 2685 C CG . PRO A 1 361 ? -12.196 6.864 40.609 1.00 35.65 ? 361 PRO A CG 1 ATOM 2686 C CD . PRO A 1 361 ? -13.683 6.890 40.769 1.00 33.90 ? 361 PRO A CD 1 ATOM 2687 N N . PRO A 1 362 ? -12.631 4.936 36.771 1.00 33.69 ? 362 PRO A N 1 ATOM 2688 C CA . PRO A 1 362 ? -12.396 3.575 36.308 1.00 34.29 ? 362 PRO A CA 1 ATOM 2689 C C . PRO A 1 362 ? -11.136 3.020 36.950 1.00 27.27 ? 362 PRO A C 1 ATOM 2690 O O . PRO A 1 362 ? -10.161 3.750 37.160 1.00 28.55 ? 362 PRO A O 1 ATOM 2691 C CB . PRO A 1 362 ? -12.249 3.725 34.804 1.00 32.79 ? 362 PRO A CB 1 ATOM 2692 C CG . PRO A 1 362 ? -11.819 5.134 34.593 1.00 31.11 ? 362 PRO A CG 1 ATOM 2693 C CD . PRO A 1 362 ? -12.474 5.934 35.694 1.00 36.45 ? 362 PRO A CD 1 ATOM 2694 N N . GLU A 1 363 ? -11.150 1.745 37.294 1.00 28.11 ? 363 GLU A N 1 ATOM 2695 C CA . GLU A 1 363 ? -9.987 1.061 37.842 1.00 24.04 ? 363 GLU A CA 1 ATOM 2696 C C . GLU A 1 363 ? -9.249 0.413 36.657 1.00 29.19 ? 363 GLU A C 1 ATOM 2697 O O . GLU A 1 363 ? -9.779 -0.528 36.074 1.00 35.46 ? 363 GLU A O 1 ATOM 2698 C CB . GLU A 1 363 ? -10.398 -0.021 38.834 1.00 32.24 ? 363 GLU A CB 1 ATOM 2699 C CG . GLU A 1 363 ? -9.311 -0.512 39.760 1.00 34.41 ? 363 GLU A CG 1 ATOM 2700 C CD . GLU A 1 363 ? -9.825 -1.466 40.829 1.00 40.67 ? 363 GLU A CD 1 ATOM 2701 O OE1 . GLU A 1 363 ? -10.215 -2.596 40.458 1.00 44.85 ? 363 GLU A OE1 1 ATOM 2702 O OE2 . GLU A 1 363 ? -9.847 -1.108 42.023 1.00 35.75 ? 363 GLU A OE2 1 ATOM 2703 N N . VAL A 1 364 ? -8.080 0.935 36.311 1.00 29.87 ? 364 VAL A N 1 ATOM 2704 C CA . VAL A 1 364 ? -7.338 0.346 35.176 1.00 27.18 ? 364 VAL A CA 1 ATOM 2705 C C . VAL A 1 364 ? -6.088 -0.315 35.723 1.00 20.77 ? 364 VAL A C 1 ATOM 2706 O O . VAL A 1 364 ? -5.205 0.343 36.256 1.00 24.79 ? 364 VAL A O 1 ATOM 2707 C CB . VAL A 1 364 ? -7.017 1.388 34.106 1.00 29.28 ? 364 VAL A CB 1 ATOM 2708 C CG1 . VAL A 1 364 ? -6.410 0.741 32.858 1.00 25.77 ? 364 VAL A CG1 1 ATOM 2709 C CG2 . VAL A 1 364 ? -8.299 2.129 33.710 1.00 28.02 ? 364 VAL A CG2 1 ATOM 2710 N N . LYS A 1 365 ? -6.063 -1.655 35.686 1.00 22.97 ? 365 LYS A N 1 ATOM 2711 C CA . LYS A 1 365 ? -4.960 -2.389 36.269 1.00 20.98 ? 365 LYS A CA 1 ATOM 2712 C C . LYS A 1 365 ? -4.098 -3.102 35.233 1.00 23.93 ? 365 LYS A C 1 ATOM 2713 O O . LYS A 1 365 ? -4.604 -3.868 34.415 1.00 22.54 ? 365 LYS A O 1 ATOM 2714 C CB . LYS A 1 365 ? -5.506 -3.470 37.233 1.00 26.37 ? 365 LYS A CB 1 ATOM 2715 C CG . LYS A 1 365 ? -6.308 -2.937 38.412 1.00 30.15 ? 365 LYS A CG 1 ATOM 2716 C CD . LYS A 1 365 ? -6.612 -4.093 39.381 1.00 32.29 ? 365 LYS A CD 1 ATOM 2717 C CE . LYS A 1 365 ? -7.245 -3.572 40.660 1.00 35.24 ? 365 LYS A CE 1 ATOM 2718 N NZ . LYS A 1 365 ? -7.290 -4.614 41.727 1.00 35.51 ? 365 LYS A NZ 1 ATOM 2719 N N . PHE A 1 366 ? -2.793 -2.871 35.323 1.00 24.39 ? 366 PHE A N 1 ATOM 2720 C CA . PHE A 1 366 ? -1.872 -3.561 34.398 1.00 26.07 ? 366 PHE A CA 1 ATOM 2721 C C . PHE A 1 366 ? -1.437 -4.848 35.102 1.00 25.94 ? 366 PHE A C 1 ATOM 2722 O O . PHE A 1 366 ? -0.300 -5.007 35.513 1.00 22.37 ? 366 PHE A O 1 ATOM 2723 C CB . PHE A 1 366 ? -0.711 -2.646 34.033 1.00 22.79 ? 366 PHE A CB 1 ATOM 2724 C CG . PHE A 1 366 ? -1.135 -1.587 33.045 1.00 26.22 ? 366 PHE A CG 1 ATOM 2725 C CD1 . PHE A 1 366 ? -1.882 -0.498 33.453 1.00 26.18 ? 366 PHE A CD1 1 ATOM 2726 C CD2 . PHE A 1 366 ? -0.781 -1.701 31.706 1.00 25.34 ? 366 PHE A CD2 1 ATOM 2727 C CE1 . PHE A 1 366 ? -2.273 0.470 32.546 1.00 25.38 ? 366 PHE A CE1 1 ATOM 2728 C CE2 . PHE A 1 366 ? -1.174 -0.734 30.800 1.00 29.81 ? 366 PHE A CE2 1 ATOM 2729 C CZ . PHE A 1 366 ? -1.920 0.353 31.217 1.00 28.25 ? 366 PHE A CZ 1 ATOM 2730 N N . ASN A 1 367 ? -2.428 -5.726 35.292 1.00 27.16 ? 367 ASN A N 1 ATOM 2731 C CA . ASN A 1 367 ? -2.242 -6.978 35.995 1.00 27.30 ? 367 ASN A CA 1 ATOM 2732 C C . ASN A 1 367 ? -2.417 -8.202 35.106 1.00 30.40 ? 367 ASN A C 1 ATOM 2733 O O . ASN A 1 367 ? -2.975 -9.218 35.531 1.00 25.02 ? 367 ASN A O 1 ATOM 2734 C CB . ASN A 1 367 ? -3.188 -7.075 37.201 1.00 26.08 ? 367 ASN A CB 1 ATOM 2735 C CG . ASN A 1 367 ? -4.644 -7.089 36.822 1.00 27.04 ? 367 ASN A CG 1 ATOM 2736 O OD1 . ASN A 1 367 ? -5.019 -6.990 35.654 1.00 28.32 ? 367 ASN A OD1 1 ATOM 2737 N ND2 . ASN A 1 367 ? -5.518 -7.213 37.824 1.00 28.93 ? 367 ASN A ND2 1 ATOM 2738 N N . LYS A 1 368 ? -1.925 -8.110 33.889 1.00 25.54 ? 368 LYS A N 1 ATOM 2739 C CA . LYS A 1 368 ? -1.944 -9.160 32.882 1.00 27.72 ? 368 LYS A CA 1 ATOM 2740 C C . LYS A 1 368 ? -1.026 -8.702 31.737 1.00 29.73 ? 368 LYS A C 1 ATOM 2741 O O . LYS A 1 368 ? -0.704 -7.511 31.673 1.00 26.84 ? 368 LYS A O 1 ATOM 2742 C CB . LYS A 1 368 ? -3.335 -9.475 32.378 1.00 27.06 ? 368 LYS A CB 1 ATOM 2743 C CG . LYS A 1 368 ? -4.031 -8.357 31.634 1.00 28.39 ? 368 LYS A CG 1 ATOM 2744 C CD . LYS A 1 368 ? -5.485 -8.701 31.323 1.00 29.42 ? 368 LYS A CD 1 ATOM 2745 C CE . LYS A 1 368 ? -6.156 -7.546 30.602 1.00 30.49 ? 368 LYS A CE 1 ATOM 2746 N NZ . LYS A 1 368 ? -7.427 -7.922 29.952 1.00 29.62 ? 368 LYS A NZ 1 ATOM 2747 N N . PRO A 1 369 ? -0.597 -9.609 30.886 1.00 27.65 ? 369 PRO A N 1 ATOM 2748 C CA . PRO A 1 369 ? 0.293 -9.281 29.789 1.00 27.30 ? 369 PRO A CA 1 ATOM 2749 C C . PRO A 1 369 ? -0.070 -7.993 29.081 1.00 18.75 ? 369 PRO A C 1 ATOM 2750 O O . PRO A 1 369 ? -1.216 -7.750 28.703 1.00 20.25 ? 369 PRO A O 1 ATOM 2751 C CB . PRO A 1 369 ? 0.238 -10.513 28.896 1.00 24.98 ? 369 PRO A CB 1 ATOM 2752 C CG . PRO A 1 369 ? -0.024 -11.633 29.864 1.00 28.93 ? 369 PRO A CG 1 ATOM 2753 C CD . PRO A 1 369 ? -0.935 -11.051 30.918 1.00 24.81 ? 369 PRO A CD 1 ATOM 2754 N N . PHE A 1 370 ? 0.922 -7.117 28.929 1.00 20.48 ? 370 PHE A N 1 ATOM 2755 C CA . PHE A 1 370 ? 0.705 -5.830 28.263 1.00 20.45 ? 370 PHE A CA 1 ATOM 2756 C C . PHE A 1 370 ? 1.921 -5.416 27.447 1.00 21.77 ? 370 PHE A C 1 ATOM 2757 O O . PHE A 1 370 ? 3.039 -5.875 27.680 1.00 24.39 ? 370 PHE A O 1 ATOM 2758 C CB . PHE A 1 370 ? 0.345 -4.753 29.289 1.00 19.99 ? 370 PHE A CB 1 ATOM 2759 C CG . PHE A 1 370 ? 1.444 -4.401 30.247 1.00 20.78 ? 370 PHE A CG 1 ATOM 2760 C CD1 . PHE A 1 370 ? 2.408 -3.474 29.923 1.00 19.36 ? 370 PHE A CD1 1 ATOM 2761 C CD2 . PHE A 1 370 ? 1.495 -5.003 31.503 1.00 20.69 ? 370 PHE A CD2 1 ATOM 2762 C CE1 . PHE A 1 370 ? 3.420 -3.145 30.809 1.00 19.14 ? 370 PHE A CE1 1 ATOM 2763 C CE2 . PHE A 1 370 ? 2.499 -4.683 32.394 1.00 20.93 ? 370 PHE A CE2 1 ATOM 2764 C CZ . PHE A 1 370 ? 3.464 -3.754 32.050 1.00 23.52 ? 370 PHE A CZ 1 ATOM 2765 N N . VAL A 1 371 ? 1.696 -4.536 26.488 1.00 19.51 ? 371 VAL A N 1 ATOM 2766 C CA . VAL A 1 371 ? 2.737 -4.041 25.590 1.00 24.71 ? 371 VAL A CA 1 ATOM 2767 C C . VAL A 1 371 ? 3.092 -2.593 25.866 1.00 21.59 ? 371 VAL A C 1 ATOM 2768 O O . VAL A 1 371 ? 2.249 -1.834 26.366 1.00 23.84 ? 371 VAL A O 1 ATOM 2769 C CB . VAL A 1 371 ? 2.218 -4.144 24.131 1.00 23.68 ? 371 VAL A CB 1 ATOM 2770 C CG1 . VAL A 1 371 ? 3.192 -3.523 23.149 1.00 26.36 ? 371 VAL A CG1 1 ATOM 2771 C CG2 . VAL A 1 371 ? 1.927 -5.594 23.792 1.00 25.10 ? 371 VAL A CG2 1 ATOM 2772 N N . PHE A 1 372 ? 4.324 -2.183 25.562 1.00 22.80 ? 372 PHE A N 1 ATOM 2773 C CA . PHE A 1 372 ? 4.692 -0.796 25.795 1.00 24.54 ? 372 PHE A CA 1 ATOM 2774 C C . PHE A 1 372 ? 5.735 -0.257 24.824 1.00 24.41 ? 372 PHE A C 1 ATOM 2775 O O . PHE A 1 372 ? 6.473 -0.966 24.145 1.00 14.76 ? 372 PHE A O 1 ATOM 2776 C CB . PHE A 1 372 ? 5.101 -0.574 27.232 1.00 26.14 ? 372 PHE A CB 1 ATOM 2777 C CG . PHE A 1 372 ? 6.450 -1.121 27.579 1.00 28.13 ? 372 PHE A CG 1 ATOM 2778 C CD1 . PHE A 1 372 ? 6.569 -2.354 28.191 1.00 30.91 ? 372 PHE A CD1 1 ATOM 2779 C CD2 . PHE A 1 372 ? 7.592 -0.391 27.299 1.00 31.79 ? 372 PHE A CD2 1 ATOM 2780 C CE1 . PHE A 1 372 ? 7.810 -2.863 28.513 1.00 31.96 ? 372 PHE A CE1 1 ATOM 2781 C CE2 . PHE A 1 372 ? 8.838 -0.896 27.617 1.00 34.55 ? 372 PHE A CE2 1 ATOM 2782 C CZ . PHE A 1 372 ? 8.938 -2.131 28.229 1.00 34.85 ? 372 PHE A CZ 1 ATOM 2783 N N . LEU A 1 373 ? 5.795 1.063 24.784 1.00 18.65 ? 373 LEU A N 1 ATOM 2784 C CA . LEU A 1 373 ? 6.701 1.790 23.886 1.00 26.63 ? 373 LEU A CA 1 ATOM 2785 C C . LEU A 1 373 ? 7.117 3.095 24.534 1.00 28.66 ? 373 LEU A C 1 ATOM 2786 O O . LEU A 1 373 ? 6.280 3.741 25.189 1.00 27.59 ? 373 LEU A O 1 ATOM 2787 C CB . LEU A 1 373 ? 5.892 2.048 22.616 1.00 32.59 ? 373 LEU A CB 1 ATOM 2788 C CG . LEU A 1 373 ? 6.521 2.099 21.248 1.00 39.39 ? 373 LEU A CG 1 ATOM 2789 C CD1 . LEU A 1 373 ? 7.830 1.350 21.154 1.00 36.11 ? 373 LEU A CD1 1 ATOM 2790 C CD2 . LEU A 1 373 ? 5.548 1.544 20.197 1.00 41.85 ? 373 LEU A CD2 1 ATOM 2791 N N . MET A 1 374 ? 8.379 3.476 24.406 1.00 19.98 ? 374 MET A N 1 ATOM 2792 C CA . MET A 1 374 ? 8.817 4.759 24.964 1.00 25.07 ? 374 MET A CA 1 ATOM 2793 C C . MET A 1 374 ? 9.209 5.610 23.740 1.00 25.02 ? 374 MET A C 1 ATOM 2794 O O . MET A 1 374 ? 9.972 5.125 22.910 1.00 16.75 ? 374 MET A O 1 ATOM 2795 C CB . MET A 1 374 ? 9.915 4.687 25.978 1.00 26.87 ? 374 MET A CB 1 ATOM 2796 C CG . MET A 1 374 ? 9.460 4.249 27.376 1.00 33.96 ? 374 MET A CG 1 ATOM 2797 S SD . MET A 1 374 ? 9.596 2.483 27.588 1.00 40.57 ? 374 MET A SD 1 ATOM 2798 C CE . MET A 1 374 ? 8.671 2.185 29.094 1.00 35.71 ? 374 MET A CE 1 ATOM 2799 N N . ILE A 1 375 ? 8.631 6.786 23.648 1.00 27.01 ? 375 ILE A N 1 ATOM 2800 C CA . ILE A 1 375 ? 8.864 7.679 22.524 1.00 22.15 ? 375 ILE A CA 1 ATOM 2801 C C . ILE A 1 375 ? 9.614 8.943 22.921 1.00 30.89 ? 375 ILE A C 1 ATOM 2802 O O . ILE A 1 375 ? 9.320 9.536 23.960 1.00 34.02 ? 375 ILE A O 1 ATOM 2803 C CB . ILE A 1 375 ? 7.498 8.145 21.948 1.00 24.71 ? 375 ILE A CB 1 ATOM 2804 C CG1 . ILE A 1 375 ? 6.607 6.954 21.626 1.00 25.66 ? 375 ILE A CG1 1 ATOM 2805 C CG2 . ILE A 1 375 ? 7.713 9.043 20.741 1.00 23.11 ? 375 ILE A CG2 1 ATOM 2806 C CD1 . ILE A 1 375 ? 7.127 6.043 20.541 1.00 24.68 ? 375 ILE A CD1 1 ATOM 2807 N N . GLU A 1 376 ? 10.547 9.359 22.072 1.00 30.21 ? 376 GLU A N 1 ATOM 2808 C CA . GLU A 1 376 ? 11.292 10.607 22.332 1.00 30.81 ? 376 GLU A CA 1 ATOM 2809 C C . GLU A 1 376 ? 10.403 11.732 21.799 1.00 24.85 ? 376 GLU A C 1 ATOM 2810 O O . GLU A 1 376 ? 9.923 11.638 20.670 1.00 29.62 ? 376 GLU A O 1 ATOM 2811 C CB . GLU A 1 376 ? 12.649 10.572 21.663 1.00 33.36 ? 376 GLU A CB 1 ATOM 2812 C CG . GLU A 1 376 ? 13.636 11.614 22.170 1.00 35.32 ? 376 GLU A CG 1 ATOM 2813 C CD . GLU A 1 376 ? 13.451 12.953 21.481 1.00 35.25 ? 376 GLU A CD 1 ATOM 2814 O OE1 . GLU A 1 376 ? 13.308 12.959 20.240 1.00 36.77 ? 376 GLU A OE1 1 ATOM 2815 O OE2 . GLU A 1 376 ? 13.446 13.984 22.180 1.00 36.29 ? 376 GLU A OE2 1 ATOM 2816 N N . GLN A 1 377 ? 10.082 12.710 22.627 1.00 25.00 ? 377 GLN A N 1 ATOM 2817 C CA . GLN A 1 377 ? 9.142 13.753 22.297 1.00 29.29 ? 377 GLN A CA 1 ATOM 2818 C C . GLN A 1 377 ? 9.479 14.617 21.106 1.00 32.68 ? 377 GLN A C 1 ATOM 2819 O O . GLN A 1 377 ? 8.577 14.917 20.305 1.00 32.94 ? 377 GLN A O 1 ATOM 2820 C CB . GLN A 1 377 ? 8.845 14.609 23.545 1.00 31.33 ? 377 GLN A CB 1 ATOM 2821 C CG . GLN A 1 377 ? 7.948 13.862 24.542 1.00 32.94 ? 377 GLN A CG 1 ATOM 2822 C CD . GLN A 1 377 ? 7.886 14.559 25.886 1.00 33.52 ? 377 GLN A CD 1 ATOM 2823 O OE1 . GLN A 1 377 ? 8.164 15.753 25.984 1.00 35.59 ? 377 GLN A OE1 1 ATOM 2824 N NE2 . GLN A 1 377 ? 7.521 13.823 26.930 1.00 34.25 ? 377 GLN A NE2 1 ATOM 2825 N N . ASN A 1 378 ? 10.722 15.043 20.944 1.00 38.04 ? 378 ASN A N 1 ATOM 2826 C CA . ASN A 1 378 ? 11.079 15.902 19.811 1.00 43.59 ? 378 ASN A CA 1 ATOM 2827 C C . ASN A 1 378 ? 10.950 15.188 18.476 1.00 42.62 ? 378 ASN A C 1 ATOM 2828 O O . ASN A 1 378 ? 10.120 15.546 17.637 1.00 42.20 ? 378 ASN A O 1 ATOM 2829 C CB . ASN A 1 378 ? 12.501 16.438 19.999 1.00 42.92 ? 378 ASN A CB 1 ATOM 2830 C CG . ASN A 1 378 ? 12.590 17.362 21.200 1.00 46.77 ? 378 ASN A CG 1 ATOM 2831 O OD1 . ASN A 1 378 ? 11.796 18.302 21.317 1.00 47.56 ? 378 ASN A OD1 1 ATOM 2832 N ND2 . ASN A 1 378 ? 13.539 17.102 22.084 1.00 44.79 ? 378 ASN A ND2 1 ATOM 2833 N N . THR A 1 379 ? 11.769 14.164 18.272 1.00 41.88 ? 379 THR A N 1 ATOM 2834 C CA . THR A 1 379 ? 11.788 13.396 17.041 1.00 41.49 ? 379 THR A CA 1 ATOM 2835 C C . THR A 1 379 ? 10.647 12.397 16.934 1.00 40.58 ? 379 THR A C 1 ATOM 2836 O O . THR A 1 379 ? 10.258 12.011 15.827 1.00 41.78 ? 379 THR A O 1 ATOM 2837 C CB . THR A 1 379 ? 13.119 12.610 16.925 1.00 41.72 ? 379 THR A CB 1 ATOM 2838 O OG1 . THR A 1 379 ? 13.173 11.647 17.992 1.00 41.29 ? 379 THR A OG1 1 ATOM 2839 C CG2 . THR A 1 379 ? 14.299 13.555 17.043 1.00 40.35 ? 379 THR A CG2 1 ATOM 2840 N N . LYS A 1 380 ? 10.129 11.950 18.072 1.00 37.50 ? 380 LYS A N 1 ATOM 2841 C CA . LYS A 1 380 ? 9.046 10.968 18.078 1.00 35.28 ? 380 LYS A CA 1 ATOM 2842 C C . LYS A 1 380 ? 9.566 9.582 17.716 1.00 33.14 ? 380 LYS A C 1 ATOM 2843 O O . LYS A 1 380 ? 8.831 8.697 17.289 1.00 29.24 ? 380 LYS A O 1 ATOM 2844 C CB . LYS A 1 380 ? 7.925 11.419 17.135 1.00 37.60 ? 380 LYS A CB 1 ATOM 2845 C CG . LYS A 1 380 ? 7.344 12.772 17.545 1.00 39.63 ? 380 LYS A CG 1 ATOM 2846 C CD . LYS A 1 380 ? 6.156 13.178 16.702 1.00 40.38 ? 380 LYS A CD 1 ATOM 2847 C CE . LYS A 1 380 ? 5.252 14.149 17.460 1.00 40.57 ? 380 LYS A CE 1 ATOM 2848 N NZ . LYS A 1 380 ? 6.042 15.151 18.228 1.00 42.00 ? 380 LYS A NZ 1 ATOM 2849 N N . SER A 1 381 ? 10.865 9.386 17.911 1.00 31.93 ? 381 SER A N 1 ATOM 2850 C CA . SER A 1 381 ? 11.527 8.118 17.647 1.00 32.79 ? 381 SER A CA 1 ATOM 2851 C C . SER A 1 381 ? 11.208 7.111 18.756 1.00 29.55 ? 381 SER A C 1 ATOM 2852 O O . SER A 1 381 ? 11.160 7.493 19.927 1.00 22.39 ? 381 SER A O 1 ATOM 2853 C CB . SER A 1 381 ? 13.051 8.327 17.635 1.00 33.85 ? 381 SER A CB 1 ATOM 2854 O OG . SER A 1 381 ? 13.417 9.338 16.715 1.00 38.76 ? 381 SER A OG 1 ATOM 2855 N N . PRO A 1 382 ? 11.036 5.859 18.384 1.00 25.87 ? 382 PRO A N 1 ATOM 2856 C CA . PRO A 1 382 ? 10.750 4.797 19.339 1.00 27.68 ? 382 PRO A CA 1 ATOM 2857 C C . PRO A 1 382 ? 12.012 4.366 20.070 1.00 26.63 ? 382 PRO A C 1 ATOM 2858 O O . PRO A 1 382 ? 12.758 3.506 19.599 1.00 29.06 ? 382 PRO A O 1 ATOM 2859 C CB . PRO A 1 382 ? 10.183 3.687 18.479 1.00 28.34 ? 382 PRO A CB 1 ATOM 2860 C CG . PRO A 1 382 ? 10.775 3.891 17.128 1.00 29.95 ? 382 PRO A CG 1 ATOM 2861 C CD . PRO A 1 382 ? 11.090 5.352 16.997 1.00 28.71 ? 382 PRO A CD 1 ATOM 2862 N N . LEU A 1 383 ? 12.268 4.992 21.210 1.00 26.72 ? 383 LEU A N 1 ATOM 2863 C CA . LEU A 1 383 ? 13.428 4.719 22.031 1.00 31.05 ? 383 LEU A CA 1 ATOM 2864 C C . LEU A 1 383 ? 13.438 3.282 22.556 1.00 28.19 ? 383 LEU A C 1 ATOM 2865 O O . LEU A 1 383 ? 14.493 2.662 22.635 1.00 26.88 ? 383 LEU A O 1 ATOM 2866 C CB . LEU A 1 383 ? 13.489 5.663 23.236 1.00 30.69 ? 383 LEU A CB 1 ATOM 2867 C CG . LEU A 1 383 ? 14.071 7.053 23.022 1.00 35.04 ? 383 LEU A CG 1 ATOM 2868 C CD1 . LEU A 1 383 ? 13.826 7.934 24.242 1.00 35.77 ? 383 LEU A CD1 1 ATOM 2869 C CD2 . LEU A 1 383 ? 15.565 6.970 22.727 1.00 36.44 ? 383 LEU A CD2 1 ATOM 2870 N N . PHE A 1 384 ? 12.274 2.790 22.955 1.00 24.15 ? 384 PHE A N 1 ATOM 2871 C CA . PHE A 1 384 ? 12.141 1.443 23.468 1.00 21.68 ? 384 PHE A CA 1 ATOM 2872 C C . PHE A 1 384 ? 10.806 0.825 23.057 1.00 25.53 ? 384 PHE A C 1 ATOM 2873 O O . PHE A 1 384 ? 9.806 1.511 22.829 1.00 19.01 ? 384 PHE A O 1 ATOM 2874 C CB . PHE A 1 384 ? 12.246 1.363 24.993 1.00 25.74 ? 384 PHE A CB 1 ATOM 2875 C CG . PHE A 1 384 ? 13.537 1.854 25.567 1.00 30.32 ? 384 PHE A CG 1 ATOM 2876 C CD1 . PHE A 1 384 ? 14.701 1.112 25.417 1.00 31.76 ? 384 PHE A CD1 1 ATOM 2877 C CD2 . PHE A 1 384 ? 13.597 3.055 26.255 1.00 30.69 ? 384 PHE A CD2 1 ATOM 2878 C CE1 . PHE A 1 384 ? 15.893 1.564 25.943 1.00 32.23 ? 384 PHE A CE1 1 ATOM 2879 C CE2 . PHE A 1 384 ? 14.791 3.510 26.779 1.00 31.70 ? 384 PHE A CE2 1 ATOM 2880 C CZ . PHE A 1 384 ? 15.941 2.761 26.619 1.00 32.15 ? 384 PHE A CZ 1 ATOM 2881 N N . MET A 1 385 ? 10.799 -0.498 23.012 1.00 22.70 ? 385 MET A N 1 ATOM 2882 C CA . MET A 1 385 ? 9.572 -1.238 22.748 1.00 23.67 ? 385 MET A CA 1 ATOM 2883 C C . MET A 1 385 ? 9.653 -2.556 23.517 1.00 29.31 ? 385 MET A C 1 ATOM 2884 O O . MET A 1 385 ? 10.745 -3.120 23.601 1.00 25.05 ? 385 MET A O 1 ATOM 2885 C CB . MET A 1 385 ? 9.295 -1.458 21.276 1.00 25.56 ? 385 MET A CB 1 ATOM 2886 C CG . MET A 1 385 ? 7.896 -1.976 21.013 1.00 23.56 ? 385 MET A CG 1 ATOM 2887 S SD . MET A 1 385 ? 7.414 -2.117 19.314 1.00 23.51 ? 385 MET A SD 1 ATOM 2888 C CE . MET A 1 385 ? 5.712 -2.680 19.464 1.00 21.98 ? 385 MET A CE 1 ATOM 2889 N N . GLY A 1 386 ? 8.534 -3.009 24.090 1.00 29.08 ? 386 GLY A N 1 ATOM 2890 C CA . GLY A 1 386 ? 8.588 -4.246 24.849 1.00 24.77 ? 386 GLY A CA 1 ATOM 2891 C C . GLY A 1 386 ? 7.251 -4.878 25.144 1.00 23.14 ? 386 GLY A C 1 ATOM 2892 O O . GLY A 1 386 ? 6.187 -4.442 24.723 1.00 20.30 ? 386 GLY A O 1 ATOM 2893 N N . LYS A 1 387 ? 7.317 -6.001 25.873 1.00 23.23 ? 387 LYS A N 1 ATOM 2894 C CA . LYS A 1 387 ? 6.133 -6.720 26.290 1.00 24.25 ? 387 LYS A CA 1 ATOM 2895 C C . LYS A 1 387 ? 6.403 -7.356 27.657 1.00 29.17 ? 387 LYS A C 1 ATOM 2896 O O . LYS A 1 387 ? 7.440 -7.999 27.830 1.00 30.76 ? 387 LYS A O 1 ATOM 2897 C CB . LYS A 1 387 ? 5.685 -7.802 25.302 1.00 23.89 ? 387 LYS A CB 1 ATOM 2898 C CG . LYS A 1 387 ? 4.259 -8.248 25.565 1.00 24.38 ? 387 LYS A CG 1 ATOM 2899 C CD . LYS A 1 387 ? 3.868 -9.592 25.085 1.00 23.78 ? 387 LYS A CD 1 ATOM 2900 C CE . LYS A 1 387 ? 4.738 -10.187 24.001 1.00 26.42 ? 387 LYS A CE 1 ATOM 2901 N NZ . LYS A 1 387 ? 4.018 -11.292 23.289 1.00 26.37 ? 387 LYS A NZ 1 ATOM 2902 N N . VAL A 1 388 ? 5.495 -7.128 28.593 1.00 25.81 ? 388 VAL A N 1 ATOM 2903 C CA . VAL A 1 388 ? 5.645 -7.719 29.922 1.00 27.33 ? 388 VAL A CA 1 ATOM 2904 C C . VAL A 1 388 ? 4.663 -8.887 30.027 1.00 29.26 ? 388 VAL A C 1 ATOM 2905 O O . VAL A 1 388 ? 3.453 -8.694 29.989 1.00 31.17 ? 388 VAL A O 1 ATOM 2906 C CB . VAL A 1 388 ? 5.417 -6.725 31.063 1.00 28.59 ? 388 VAL A CB 1 ATOM 2907 C CG1 . VAL A 1 388 ? 5.525 -7.432 32.412 1.00 30.80 ? 388 VAL A CG1 1 ATOM 2908 C CG2 . VAL A 1 388 ? 6.427 -5.587 30.997 1.00 29.66 ? 388 VAL A CG2 1 ATOM 2909 N N . VAL A 1 389 ? 5.212 -10.095 30.084 1.00 33.55 ? 389 VAL A N 1 ATOM 2910 C CA . VAL A 1 389 ? 4.411 -11.308 30.182 1.00 33.39 ? 389 VAL A CA 1 ATOM 2911 C C . VAL A 1 389 ? 4.266 -11.728 31.645 1.00 31.77 ? 389 VAL A C 1 ATOM 2912 O O . VAL A 1 389 ? 3.242 -12.258 32.061 1.00 33.13 ? 389 VAL A O 1 ATOM 2913 C CB . VAL A 1 389 ? 5.054 -12.460 29.385 1.00 35.32 ? 389 VAL A CB 1 ATOM 2914 C CG1 . VAL A 1 389 ? 4.280 -13.748 29.593 1.00 34.69 ? 389 VAL A CG1 1 ATOM 2915 C CG2 . VAL A 1 389 ? 5.120 -12.098 27.909 1.00 34.99 ? 389 VAL A CG2 1 ATOM 2916 N N . ASN A 1 390 ? 5.311 -11.476 32.417 1.00 32.99 ? 390 ASN A N 1 ATOM 2917 C CA . ASN A 1 390 ? 5.340 -11.781 33.845 1.00 35.16 ? 390 ASN A CA 1 ATOM 2918 C C . ASN A 1 390 ? 6.408 -10.916 34.513 1.00 31.70 ? 390 ASN A C 1 ATOM 2919 O O . ASN A 1 390 ? 7.602 -11.095 34.281 1.00 28.59 ? 390 ASN A O 1 ATOM 2920 C CB . ASN A 1 390 ? 5.592 -13.258 34.100 1.00 37.18 ? 390 ASN A CB 1 ATOM 2921 C CG . ASN A 1 390 ? 5.578 -13.645 35.564 1.00 37.56 ? 390 ASN A CG 1 ATOM 2922 O OD1 . ASN A 1 390 ? 5.312 -12.831 36.452 1.00 36.98 ? 390 ASN A OD1 1 ATOM 2923 N ND2 . ASN A 1 390 ? 5.869 -14.915 35.836 1.00 37.07 ? 390 ASN A ND2 1 ATOM 2924 N N . PRO A 1 391 ? 5.971 -9.956 35.315 1.00 33.81 ? 391 PRO A N 1 ATOM 2925 C CA . PRO A 1 391 ? 6.858 -9.034 35.989 1.00 38.02 ? 391 PRO A CA 1 ATOM 2926 C C . PRO A 1 391 ? 7.979 -9.723 36.741 1.00 43.20 ? 391 PRO A C 1 ATOM 2927 O O . PRO A 1 391 ? 9.146 -9.346 36.623 1.00 45.59 ? 391 PRO A O 1 ATOM 2928 C CB . PRO A 1 391 ? 5.944 -8.266 36.937 1.00 36.46 ? 391 PRO A CB 1 ATOM 2929 C CG . PRO A 1 391 ? 4.588 -8.376 36.343 1.00 38.86 ? 391 PRO A CG 1 ATOM 2930 C CD . PRO A 1 391 ? 4.544 -9.687 35.613 1.00 37.38 ? 391 PRO A CD 1 ATOM 2931 N N . THR A 1 392 ? 7.631 -10.741 37.525 1.00 47.49 ? 392 THR A N 1 ATOM 2932 C CA . THR A 1 392 ? 8.610 -11.472 38.311 1.00 51.31 ? 392 THR A CA 1 ATOM 2933 C C . THR A 1 392 ? 9.394 -12.481 37.489 1.00 55.26 ? 392 THR A C 1 ATOM 2934 O O . THR A 1 392 ? 9.781 -13.538 37.991 1.00 55.01 ? 392 THR A O 1 ATOM 2935 C CB . THR A 1 392 ? 7.983 -12.142 39.541 1.00 50.50 ? 392 THR A CB 1 ATOM 2936 O OG1 . THR A 1 392 ? 6.686 -12.661 39.222 1.00 50.58 ? 392 THR A OG1 1 ATOM 2937 C CG2 . THR A 1 392 ? 7.844 -11.136 40.678 1.00 50.53 ? 392 THR A CG2 1 ATOM 2938 N N . GLN A 1 393 ? 9.651 -12.148 36.230 1.00 60.48 ? 393 GLN A N 1 ATOM 2939 C CA . GLN A 1 393 ? 10.432 -12.990 35.337 1.00 63.71 ? 393 GLN A CA 1 ATOM 2940 C C . GLN A 1 393 ? 11.708 -12.237 34.934 1.00 65.41 ? 393 GLN A C 1 ATOM 2941 O O . GLN A 1 393 ? 11.615 -11.215 34.252 1.00 67.67 ? 393 GLN A O 1 ATOM 2942 C CB . GLN A 1 393 ? 9.663 -13.349 34.062 1.00 64.53 ? 393 GLN A CB 1 ATOM 2943 C CG . GLN A 1 393 ? 10.441 -14.269 33.133 1.00 65.14 ? 393 GLN A CG 1 ATOM 2944 C CD . GLN A 1 393 ? 10.451 -13.817 31.690 1.00 65.13 ? 393 GLN A CD 1 ATOM 2945 O OE1 . GLN A 1 393 ? 11.266 -12.978 31.293 1.00 64.17 ? 393 GLN A OE1 1 ATOM 2946 N NE2 . GLN A 1 393 ? 9.553 -14.371 30.881 1.00 64.59 ? 393 GLN A NE2 1 ATOM 2947 N N . LYS A 1 394 ? 12.859 -12.733 35.361 1.00 66.66 ? 394 LYS A N 1 ATOM 2948 C CA . LYS A 1 394 ? 14.120 -12.063 35.027 1.00 67.35 ? 394 LYS A CA 1 ATOM 2949 C C . LYS A 1 394 ? 15.316 -12.878 35.486 1.00 67.96 ? 394 LYS A C 1 ATOM 2950 O O . LYS A 1 394 ? 16.011 -12.454 36.432 1.00 70.79 ? 394 LYS A O 1 ATOM 2951 C CB . LYS A 1 394 ? 14.132 -10.666 35.649 1.00 67.40 ? 394 LYS A CB 1 ATOM 2952 C CG . LYS A 1 394 ? 15.374 -9.846 35.366 1.00 66.91 ? 394 LYS A CG 1 ATOM 2953 C CD . LYS A 1 394 ? 15.196 -8.401 35.816 1.00 66.28 ? 394 LYS A CD 1 ATOM 2954 C CE . LYS A 1 394 ? 16.508 -7.640 35.741 1.00 66.53 ? 394 LYS A CE 1 ATOM 2955 N NZ . LYS A 1 394 ? 16.325 -6.175 35.921 1.00 65.75 ? 394 LYS A NZ 1 ATOM 2956 O OXT . LYS A 1 394 ? 15.590 -13.908 34.764 1.00 65.78 ? 394 LYS A OXT 1 HETATM 2957 O O . HOH B 2 . ? 11.076 7.704 5.387 1.00 31.24 ? 2001 HOH A O 1 HETATM 2958 O O . HOH B 2 . ? 2.942 1.621 10.898 1.00 33.99 ? 2002 HOH A O 1 HETATM 2959 O O . HOH B 2 . ? 7.005 -3.220 9.986 1.00 34.31 ? 2003 HOH A O 1 HETATM 2960 O O . HOH B 2 . ? 6.052 3.749 9.674 1.00 37.15 ? 2004 HOH A O 1 HETATM 2961 O O . HOH B 2 . ? 5.494 -5.349 10.929 1.00 39.91 ? 2005 HOH A O 1 HETATM 2962 O O . HOH B 2 . ? 2.627 -13.387 24.878 1.00 39.11 ? 2006 HOH A O 1 HETATM 2963 O O . HOH B 2 . ? 22.605 6.351 21.090 1.00 54.57 ? 2007 HOH A O 1 HETATM 2964 O O . HOH B 2 . ? 26.752 7.799 23.735 1.00 71.96 ? 2008 HOH A O 1 HETATM 2965 O O . HOH B 2 . ? 23.237 2.801 19.128 1.00 43.17 ? 2009 HOH A O 1 HETATM 2966 O O . HOH B 2 . ? 29.141 2.711 1.270 1.00 45.09 ? 2010 HOH A O 1 HETATM 2967 O O . HOH B 2 . ? 28.164 3.793 2.966 1.00 51.30 ? 2011 HOH A O 1 HETATM 2968 O O . HOH B 2 . ? 25.317 5.645 21.682 1.00 46.98 ? 2012 HOH A O 1 HETATM 2969 O O . HOH B 2 . ? 24.656 -7.301 5.174 1.00 29.06 ? 2013 HOH A O 1 HETATM 2970 O O . HOH B 2 . ? 17.935 -6.291 4.083 1.00 36.57 ? 2014 HOH A O 1 HETATM 2971 O O . HOH B 2 . ? 16.175 -0.754 -0.410 1.00 42.26 ? 2015 HOH A O 1 HETATM 2972 O O . HOH B 2 . ? 15.184 2.880 10.947 1.00 34.56 ? 2016 HOH A O 1 HETATM 2973 O O . HOH B 2 . ? 12.274 4.395 3.082 1.00 34.48 ? 2017 HOH A O 1 HETATM 2974 O O . HOH B 2 . ? 15.526 5.931 -7.142 1.00 38.34 ? 2018 HOH A O 1 HETATM 2975 O O . HOH B 2 . ? 19.373 5.982 -1.280 1.00 36.72 ? 2019 HOH A O 1 HETATM 2976 O O . HOH B 2 . ? 22.733 10.873 -0.430 1.00 36.29 ? 2020 HOH A O 1 HETATM 2977 O O . HOH B 2 . ? 18.287 14.483 0.142 1.00 61.17 ? 2021 HOH A O 1 HETATM 2978 O O . HOH B 2 . ? 9.739 13.017 41.325 1.00 49.66 ? 2022 HOH A O 1 HETATM 2979 O O . HOH B 2 . ? 25.454 4.766 4.270 1.00 51.26 ? 2023 HOH A O 1 HETATM 2980 O O . HOH B 2 . ? 1.781 12.389 26.661 1.00 42.10 ? 2024 HOH A O 1 HETATM 2981 O O . HOH B 2 . ? 18.169 14.236 28.247 1.00 55.18 ? 2025 HOH A O 1 HETATM 2982 O O . HOH B 2 . ? 29.196 4.823 22.502 1.00 55.90 ? 2026 HOH A O 1 HETATM 2983 O O . HOH B 2 . ? 43.469 -10.185 16.770 1.00 29.77 ? 2027 HOH A O 1 HETATM 2984 O O . HOH B 2 . ? 33.492 5.073 6.821 1.00 43.78 ? 2028 HOH A O 1 HETATM 2985 O O . HOH B 2 . ? 25.848 5.094 18.926 1.00 62.15 ? 2029 HOH A O 1 HETATM 2986 O O . HOH B 2 . ? 40.463 2.432 17.292 1.00 55.61 ? 2030 HOH A O 1 HETATM 2987 O O . HOH B 2 . ? 42.060 0.544 21.078 1.00 45.95 ? 2031 HOH A O 1 HETATM 2988 O O . HOH B 2 . ? 42.772 -15.434 28.955 1.00 32.53 ? 2032 HOH A O 1 HETATM 2989 O O . HOH B 2 . ? 41.873 -17.415 25.960 1.00 37.39 ? 2033 HOH A O 1 HETATM 2990 O O . HOH B 2 . ? 37.071 -14.102 29.971 1.00 42.06 ? 2034 HOH A O 1 HETATM 2991 O O . HOH B 2 . ? -2.702 -12.120 27.254 1.00 30.87 ? 2035 HOH A O 1 HETATM 2992 O O . HOH B 2 . ? 6.688 4.671 16.580 1.00 40.25 ? 2036 HOH A O 1 HETATM 2993 O O . HOH B 2 . ? 29.442 -6.651 31.014 1.00 31.29 ? 2037 HOH A O 1 HETATM 2994 O O . HOH B 2 . ? 34.187 -7.071 37.252 1.00 47.23 ? 2038 HOH A O 1 HETATM 2995 O O . HOH B 2 . ? 29.147 -5.379 39.672 1.00 52.80 ? 2039 HOH A O 1 HETATM 2996 O O . HOH B 2 . ? 31.610 -16.046 32.669 1.00 43.17 ? 2040 HOH A O 1 HETATM 2997 O O . HOH B 2 . ? 27.431 -14.435 23.988 1.00 33.44 ? 2041 HOH A O 1 HETATM 2998 O O . HOH B 2 . ? 33.995 -18.153 24.157 1.00 52.33 ? 2042 HOH A O 1 HETATM 2999 O O . HOH B 2 . ? 33.096 -15.955 12.863 1.00 42.57 ? 2043 HOH A O 1 HETATM 3000 O O . HOH B 2 . ? 9.664 11.138 39.844 1.00 39.41 ? 2044 HOH A O 1 HETATM 3001 O O . HOH B 2 . ? 1.837 8.363 38.521 1.00 32.06 ? 2045 HOH A O 1 HETATM 3002 O O . HOH B 2 . ? 2.123 9.333 35.845 1.00 46.46 ? 2046 HOH A O 1 HETATM 3003 O O . HOH B 2 . ? -0.567 8.888 45.130 1.00 47.14 ? 2047 HOH A O 1 HETATM 3004 O O . HOH B 2 . ? 2.681 11.196 48.222 1.00 63.10 ? 2048 HOH A O 1 HETATM 3005 O O . HOH B 2 . ? 0.681 6.822 44.521 1.00 32.18 ? 2049 HOH A O 1 HETATM 3006 O O . HOH B 2 . ? 7.080 8.151 47.645 1.00 41.17 ? 2050 HOH A O 1 HETATM 3007 O O . HOH B 2 . ? 3.618 9.571 50.741 1.00 40.88 ? 2051 HOH A O 1 HETATM 3008 O O . HOH B 2 . ? -2.202 7.835 49.529 1.00 38.94 ? 2052 HOH A O 1 HETATM 3009 O O . HOH B 2 . ? -2.564 2.737 49.449 1.00 43.35 ? 2053 HOH A O 1 HETATM 3010 O O . HOH B 2 . ? 2.428 3.261 44.520 1.00 22.24 ? 2054 HOH A O 1 HETATM 3011 O O . HOH B 2 . ? -5.221 -1.163 49.756 1.00 33.15 ? 2055 HOH A O 1 HETATM 3012 O O . HOH B 2 . ? 2.859 -10.567 47.964 1.00 42.64 ? 2056 HOH A O 1 HETATM 3013 O O . HOH B 2 . ? 2.370 -5.604 50.352 1.00 50.84 ? 2057 HOH A O 1 HETATM 3014 O O . HOH B 2 . ? -4.167 -13.430 31.689 1.00 33.50 ? 2058 HOH A O 1 HETATM 3015 O O . HOH B 2 . ? -6.055 -15.302 35.991 1.00 33.78 ? 2059 HOH A O 1 HETATM 3016 O O . HOH B 2 . ? 1.766 -14.833 30.936 1.00 32.68 ? 2060 HOH A O 1 HETATM 3017 O O . HOH B 2 . ? 5.436 -13.256 41.663 1.00 40.39 ? 2061 HOH A O 1 HETATM 3018 O O . HOH B 2 . ? -2.608 11.581 42.873 1.00 40.51 ? 2062 HOH A O 1 HETATM 3019 O O . HOH B 2 . ? -9.334 10.036 24.381 1.00 38.70 ? 2063 HOH A O 1 HETATM 3020 O O . HOH B 2 . ? 0.846 12.114 29.324 1.00 32.47 ? 2064 HOH A O 1 HETATM 3021 O O . HOH B 2 . ? -1.301 9.858 32.195 1.00 19.69 ? 2065 HOH A O 1 HETATM 3022 O O . HOH B 2 . ? 2.165 12.533 32.409 1.00 15.31 ? 2066 HOH A O 1 HETATM 3023 O O . HOH B 2 . ? 1.264 17.054 30.609 1.00 33.96 ? 2067 HOH A O 1 HETATM 3024 O O . HOH B 2 . ? 4.347 11.212 34.470 1.00 24.93 ? 2068 HOH A O 1 HETATM 3025 O O . HOH B 2 . ? 8.513 14.953 29.628 1.00 38.75 ? 2069 HOH A O 1 HETATM 3026 O O . HOH B 2 . ? 13.458 10.615 33.230 1.00 35.83 ? 2070 HOH A O 1 HETATM 3027 O O . HOH B 2 . ? 3.905 13.102 25.136 1.00 40.72 ? 2071 HOH A O 1 HETATM 3028 O O . HOH B 2 . ? -11.476 -7.195 28.821 1.00 47.44 ? 2072 HOH A O 1 HETATM 3029 O O . HOH B 2 . ? -6.877 -12.055 27.643 1.00 39.89 ? 2073 HOH A O 1 HETATM 3030 O O . HOH B 2 . ? -5.900 -11.841 20.064 1.00 40.01 ? 2074 HOH A O 1 HETATM 3031 O O . HOH B 2 . ? -4.416 -12.464 25.406 1.00 41.77 ? 2075 HOH A O 1 HETATM 3032 O O . HOH B 2 . ? 1.505 -8.634 14.788 1.00 35.56 ? 2076 HOH A O 1 HETATM 3033 O O . HOH B 2 . ? -3.283 3.051 11.081 1.00 41.11 ? 2077 HOH A O 1 HETATM 3034 O O . HOH B 2 . ? 1.058 3.964 10.098 1.00 32.68 ? 2078 HOH A O 1 HETATM 3035 O O . HOH B 2 . ? -3.886 9.870 23.919 1.00 34.10 ? 2079 HOH A O 1 HETATM 3036 O O . HOH B 2 . ? -0.627 14.230 28.220 1.00 43.44 ? 2080 HOH A O 1 HETATM 3037 O O . HOH B 2 . ? 0.322 11.234 34.409 1.00 22.06 ? 2081 HOH A O 1 HETATM 3038 O O . HOH B 2 . ? -12.798 8.848 34.322 1.00 36.55 ? 2082 HOH A O 1 HETATM 3039 O O . HOH B 2 . ? -13.512 10.682 39.302 1.00 39.88 ? 2083 HOH A O 1 HETATM 3040 O O . HOH B 2 . ? -12.608 12.728 34.760 1.00 27.82 ? 2084 HOH A O 1 HETATM 3041 O O . HOH B 2 . ? 16.248 -11.405 26.505 1.00 52.50 ? 2085 HOH A O 1 HETATM 3042 O O . HOH B 2 . ? 18.722 -13.702 20.230 1.00 31.27 ? 2086 HOH A O 1 HETATM 3043 O O . HOH B 2 . ? 26.316 -12.462 17.590 1.00 33.00 ? 2087 HOH A O 1 HETATM 3044 O O . HOH B 2 . ? 29.822 -14.473 11.620 1.00 40.64 ? 2088 HOH A O 1 HETATM 3045 O O . HOH B 2 . ? 22.668 -12.732 10.067 1.00 28.05 ? 2089 HOH A O 1 HETATM 3046 O O . HOH B 2 . ? 36.141 -11.971 2.239 1.00 31.54 ? 2090 HOH A O 1 HETATM 3047 O O . HOH B 2 . ? 36.123 -6.155 3.226 1.00 39.88 ? 2091 HOH A O 1 HETATM 3048 O O . HOH B 2 . ? 35.944 4.545 5.377 1.00 34.48 ? 2092 HOH A O 1 HETATM 3049 O O . HOH B 2 . ? 35.939 -9.207 3.707 1.00 26.28 ? 2093 HOH A O 1 HETATM 3050 O O . HOH B 2 . ? 20.035 -9.792 33.171 1.00 45.36 ? 2094 HOH A O 1 HETATM 3051 O O . HOH B 2 . ? 9.714 4.770 36.519 1.00 33.83 ? 2095 HOH A O 1 HETATM 3052 O O . HOH B 2 . ? 3.741 23.929 43.991 1.00 54.57 ? 2096 HOH A O 1 HETATM 3053 O O . HOH B 2 . ? 2.251 16.595 43.901 1.00 71.42 ? 2097 HOH A O 1 HETATM 3054 O O . HOH B 2 . ? -1.560 12.215 36.460 1.00 28.06 ? 2098 HOH A O 1 HETATM 3055 O O . HOH B 2 . ? -13.081 17.350 43.964 1.00 27.36 ? 2099 HOH A O 1 HETATM 3056 O O . HOH B 2 . ? -18.753 8.893 42.727 1.00 27.89 ? 2100 HOH A O 1 HETATM 3057 O O . HOH B 2 . ? -13.673 -0.123 37.025 1.00 46.41 ? 2101 HOH A O 1 HETATM 3058 O O . HOH B 2 . ? -8.989 -5.809 30.162 1.00 31.50 ? 2102 HOH A O 1 HETATM 3059 O O . HOH B 2 . ? -3.440 -9.638 28.146 1.00 31.41 ? 2103 HOH A O 1 HETATM 3060 O O . HOH B 2 . ? 8.274 18.348 24.522 1.00 47.99 ? 2104 HOH A O 1 HETATM 3061 O O . HOH B 2 . ? 6.282 7.879 16.999 1.00 53.92 ? 2105 HOH A O 1 HETATM 3062 O O . HOH B 2 . ? 13.642 10.464 14.421 1.00 59.95 ? 2106 HOH A O 1 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 MET 1 1 ? ? ? A . n A 1 2 ASP 2 2 ? ? ? A . n A 1 3 PRO 3 3 ? ? ? A . n A 1 4 GLN 4 4 ? ? ? A . n A 1 5 GLY 5 5 ? ? ? A . n A 1 6 ASP 6 6 ? ? ? A . n A 1 7 ALA 7 7 ? ? ? A . n A 1 8 ALA 8 8 ? ? ? A . n A 1 9 GLN 9 9 ? ? ? A . n A 1 10 LYS 10 10 ? ? ? A . n A 1 11 THR 11 11 ? ? ? A . n A 1 12 ASP 12 12 ? ? ? A . n A 1 13 THR 13 13 ? ? ? A . n A 1 14 SER 14 14 ? ? ? A . n A 1 15 HIS 15 15 ? ? ? A . n A 1 16 HIS 16 16 ? ? ? A . n A 1 17 ASP 17 17 ? ? ? A . n A 1 18 GLN 18 18 ? ? ? A . n A 1 19 ASP 19 19 ? ? ? A . n A 1 20 HIS 20 20 ? ? ? A . n A 1 21 PRO 21 21 ? ? ? A . n A 1 22 THR 22 22 ? ? ? A . n A 1 23 PHE 23 23 23 PHE PHE A . n A 1 24 ASN 24 24 24 ASN ASN A . n A 1 25 LYS 25 25 25 LYS LYS A . n A 1 26 ILE 26 26 26 ILE ILE A . n A 1 27 THR 27 27 27 THR THR A . n A 1 28 PRO 28 28 28 PRO PRO A . n A 1 29 ASN 29 29 29 ASN ASN A . n A 1 30 LEU 30 30 30 LEU LEU A . n A 1 31 ALA 31 31 31 ALA ALA A . n A 1 32 GLU 32 32 32 GLU GLU A . n A 1 33 PHE 33 33 33 PHE PHE A . n A 1 34 ALA 34 34 34 ALA ALA A . n A 1 35 PHE 35 35 35 PHE PHE A . n A 1 36 SER 36 36 36 SER SER A . n A 1 37 LEU 37 37 37 LEU LEU A . n A 1 38 TYR 38 38 38 TYR TYR A . n A 1 39 ARG 39 39 39 ARG ARG A . n A 1 40 GLN 40 40 40 GLN GLN A . n A 1 41 LEU 41 41 41 LEU LEU A . n A 1 42 ALA 42 42 42 ALA ALA A . n A 1 43 HIS 43 43 43 HIS HIS A . n A 1 44 GLN 44 44 44 GLN GLN A . n A 1 45 SER 45 45 45 SER SER A . n A 1 46 ASN 46 46 46 ASN ASN A . n A 1 47 SER 47 47 47 SER SER A . n A 1 48 THR 48 48 48 THR THR A . n A 1 49 ASN 49 49 49 ASN ASN A . n A 1 50 ILE 50 50 50 ILE ILE A . n A 1 51 PHE 51 51 51 PHE PHE A . n A 1 52 PHE 52 52 52 PHE PHE A . n A 1 53 SER 53 53 53 SER SER A . n A 1 54 PRO 54 54 54 PRO PRO A . n A 1 55 VAL 55 55 55 VAL VAL A . n A 1 56 SER 56 56 56 SER SER A . n A 1 57 ILE 57 57 57 ILE ILE A . n A 1 58 ALA 58 58 58 ALA ALA A . n A 1 59 THR 59 59 59 THR THR A . n A 1 60 ALA 60 60 60 ALA ALA A . n A 1 61 PHE 61 61 61 PHE PHE A . n A 1 62 ALA 62 62 62 ALA ALA A . n A 1 63 MET 63 63 63 MET MET A . n A 1 64 LEU 64 64 64 LEU LEU A . n A 1 65 SER 65 65 65 SER SER A . n A 1 66 LEU 66 66 66 LEU LEU A . n A 1 67 GLY 67 67 67 GLY GLY A . n A 1 68 THR 68 68 68 THR THR A . n A 1 69 LYS 69 69 69 LYS LYS A . n A 1 70 ALA 70 70 70 ALA ALA A . n A 1 71 ASP 71 71 71 ASP ASP A . n A 1 72 THR 72 72 72 THR THR A . n A 1 73 HIS 73 73 73 HIS HIS A . n A 1 74 ASP 74 74 74 ASP ASP A . n A 1 75 GLU 75 75 75 GLU GLU A . n A 1 76 ILE 76 76 76 ILE ILE A . n A 1 77 LEU 77 77 77 LEU LEU A . n A 1 78 GLU 78 78 78 GLU GLU A . n A 1 79 GLY 79 79 79 GLY GLY A . n A 1 80 LEU 80 80 80 LEU LEU A . n A 1 81 ASN 81 81 81 ASN ASN A . n A 1 82 PHE 82 82 82 PHE PHE A . n A 1 83 ASN 83 83 83 ASN ASN A . n A 1 84 LEU 84 84 84 LEU LEU A . n A 1 85 THR 85 85 85 THR THR A . n A 1 86 GLU 86 86 86 GLU GLU A . n A 1 87 ILE 87 87 87 ILE ILE A . n A 1 88 PRO 88 88 88 PRO PRO A . n A 1 89 GLU 89 89 89 GLU GLU A . n A 1 90 ALA 90 90 90 ALA ALA A . n A 1 91 GLN 91 91 91 GLN GLN A . n A 1 92 ILE 92 92 92 ILE ILE A . n A 1 93 HIS 93 93 93 HIS HIS A . n A 1 94 GLU 94 94 94 GLU GLU A . n A 1 95 GLY 95 95 95 GLY GLY A . n A 1 96 PHE 96 96 96 PHE PHE A . n A 1 97 GLN 97 97 97 GLN GLN A . n A 1 98 GLU 98 98 98 GLU GLU A . n A 1 99 LEU 99 99 99 LEU LEU A . n A 1 100 LEU 100 100 100 LEU LEU A . n A 1 101 ARG 101 101 101 ARG ARG A . n A 1 102 THR 102 102 102 THR THR A . n A 1 103 LEU 103 103 103 LEU LEU A . n A 1 104 ASN 104 104 104 ASN ASN A . n A 1 105 GLN 105 105 105 GLN GLN A . n A 1 106 PRO 106 106 106 PRO PRO A . n A 1 107 ASP 107 107 107 ASP ASP A . n A 1 108 SER 108 108 108 SER SER A . n A 1 109 GLN 109 109 109 GLN GLN A . n A 1 110 LEU 110 110 110 LEU LEU A . n A 1 111 GLN 111 111 111 GLN GLN A . n A 1 112 LEU 112 112 112 LEU LEU A . n A 1 113 THR 113 113 113 THR THR A . n A 1 114 THR 114 114 114 THR THR A . n A 1 115 GLY 115 115 115 GLY GLY A . n A 1 116 ASN 116 116 116 ASN ASN A . n A 1 117 GLY 117 117 117 GLY GLY A . n A 1 118 LEU 118 118 118 LEU LEU A . n A 1 119 PHE 119 119 119 PHE PHE A . n A 1 120 LEU 120 120 120 LEU LEU A . n A 1 121 SER 121 121 121 SER SER A . n A 1 122 GLU 122 122 122 GLU GLU A . n A 1 123 GLY 123 123 123 GLY GLY A . n A 1 124 LEU 124 124 124 LEU LEU A . n A 1 125 LYS 125 125 125 LYS LYS A . n A 1 126 LEU 126 126 126 LEU LEU A . n A 1 127 VAL 127 127 127 VAL VAL A . n A 1 128 ASP 128 128 128 ASP ASP A . n A 1 129 LYS 129 129 129 LYS LYS A . n A 1 130 PHE 130 130 130 PHE PHE A . n A 1 131 LEU 131 131 131 LEU LEU A . n A 1 132 GLU 132 132 132 GLU GLU A . n A 1 133 ASP 133 133 133 ASP ASP A . n A 1 134 VAL 134 134 134 VAL VAL A . n A 1 135 LYS 135 135 135 LYS LYS A . n A 1 136 LYS 136 136 136 LYS LYS A . n A 1 137 LEU 137 137 137 LEU LEU A . n A 1 138 TYR 138 138 138 TYR TYR A . n A 1 139 HIS 139 139 139 HIS HIS A . n A 1 140 SER 140 140 140 SER SER A . n A 1 141 GLU 141 141 141 GLU GLU A . n A 1 142 ALA 142 142 142 ALA ALA A . n A 1 143 PHE 143 143 143 PHE PHE A . n A 1 144 THR 144 144 144 THR THR A . n A 1 145 VAL 145 145 145 VAL VAL A . n A 1 146 ASN 146 146 146 ASN ASN A . n A 1 147 PHE 147 147 147 PHE PHE A . n A 1 148 GLY 148 148 148 GLY GLY A . n A 1 149 ASP 149 149 149 ASP ASP A . n A 1 150 THR 150 150 150 THR THR A . n A 1 151 GLU 151 151 151 GLU GLU A . n A 1 152 GLU 152 152 152 GLU GLU A . n A 1 153 ALA 153 153 153 ALA ALA A . n A 1 154 LYS 154 154 154 LYS LYS A . n A 1 155 LYS 155 155 155 LYS LYS A . n A 1 156 GLN 156 156 156 GLN GLN A . n A 1 157 ILE 157 157 157 ILE ILE A . n A 1 158 ASN 158 158 158 ASN ASN A . n A 1 159 ASP 159 159 159 ASP ASP A . n A 1 160 TYR 160 160 160 TYR TYR A . n A 1 161 VAL 161 161 161 VAL VAL A . n A 1 162 GLU 162 162 162 GLU GLU A . n A 1 163 LYS 163 163 163 LYS LYS A . n A 1 164 GLY 164 164 164 GLY GLY A . n A 1 165 THR 165 165 165 THR THR A . n A 1 166 GLN 166 166 166 GLN GLN A . n A 1 167 GLY 167 167 167 GLY GLY A . n A 1 168 LYS 168 168 168 LYS LYS A . n A 1 169 ILE 169 169 169 ILE ILE A . n A 1 170 VAL 170 170 170 VAL VAL A . n A 1 171 ASP 171 171 171 ASP ASP A . n A 1 172 LEU 172 172 172 LEU LEU A . n A 1 173 VAL 173 173 173 VAL VAL A . n A 1 174 LYS 174 174 174 LYS LYS A . n A 1 175 GLU 175 175 175 GLU GLU A . n A 1 176 LEU 176 176 176 LEU LEU A . n A 1 177 ASP 177 177 177 ASP ASP A . n A 1 178 ARG 178 178 178 ARG ARG A . n A 1 179 ASP 179 179 179 ASP ASP A . n A 1 180 THR 180 180 180 THR THR A . n A 1 181 VAL 181 181 181 VAL VAL A . n A 1 182 PHE 182 182 182 PHE PHE A . n A 1 183 ALA 183 183 183 ALA ALA A . n A 1 184 LEU 184 184 184 LEU LEU A . n A 1 185 VAL 185 185 185 VAL VAL A . n A 1 186 ASN 186 186 186 ASN ASN A . n A 1 187 TYR 187 187 187 TYR TYR A . n A 1 188 ILE 188 188 188 ILE ILE A . n A 1 189 PHE 189 189 189 PHE PHE A . n A 1 190 PHE 190 190 190 PHE PHE A . n A 1 191 LYS 191 191 191 LYS LYS A . n A 1 192 GLY 192 192 192 GLY GLY A . n A 1 193 LYS 193 193 193 LYS LYS A . n A 1 194 TRP 194 194 194 TRP TRP A . n A 1 195 GLU 195 195 195 GLU GLU A . n A 1 196 ARG 196 196 196 ARG ARG A . n A 1 197 PRO 197 197 197 PRO PRO A . n A 1 198 PHE 198 198 198 PHE PHE A . n A 1 199 GLU 199 199 199 GLU GLU A . n A 1 200 VAL 200 200 200 VAL VAL A . n A 1 201 LYS 201 201 201 LYS LYS A . n A 1 202 ASP 202 202 202 ASP ASP A . n A 1 203 THR 203 203 203 THR THR A . n A 1 204 GLU 204 204 204 GLU GLU A . n A 1 205 GLU 205 205 205 GLU GLU A . n A 1 206 GLU 206 206 206 GLU GLU A . n A 1 207 ASP 207 207 207 ASP ASP A . n A 1 208 PHE 208 208 208 PHE PHE A . n A 1 209 HIS 209 209 209 HIS HIS A . n A 1 210 VAL 210 210 210 VAL VAL A . n A 1 211 ASP 211 211 211 ASP ASP A . n A 1 212 GLN 212 212 212 GLN GLN A . n A 1 213 VAL 213 213 213 VAL VAL A . n A 1 214 THR 214 214 214 THR THR A . n A 1 215 THR 215 215 215 THR THR A . n A 1 216 VAL 216 216 216 VAL VAL A . n A 1 217 LYS 217 217 217 LYS LYS A . n A 1 218 VAL 218 218 218 VAL VAL A . n A 1 219 PRO 219 219 219 PRO PRO A . n A 1 220 MET 220 220 220 MET MET A . n A 1 221 MET 221 221 221 MET MET A . n A 1 222 LYS 222 222 222 LYS LYS A . n A 1 223 ARG 223 223 223 ARG ARG A . n A 1 224 LEU 224 224 224 LEU LEU A . n A 1 225 GLY 225 225 225 GLY GLY A . n A 1 226 MET 226 226 226 MET MET A . n A 1 227 PHE 227 227 227 PHE PHE A . n A 1 228 ASN 228 228 228 ASN ASN A . n A 1 229 ILE 229 229 229 ILE ILE A . n A 1 230 GLN 230 230 230 GLN GLN A . n A 1 231 HIS 231 231 231 HIS HIS A . n A 1 232 CYS 232 232 232 CYS CYS A . n A 1 233 LYS 233 233 233 LYS LYS A . n A 1 234 LYS 234 234 234 LYS LYS A . n A 1 235 LEU 235 235 235 LEU LEU A . n A 1 236 SER 236 236 236 SER SER A . n A 1 237 SER 237 237 237 SER SER A . n A 1 238 TRP 238 238 238 TRP TRP A . n A 1 239 VAL 239 239 239 VAL VAL A . n A 1 240 LEU 240 240 240 LEU LEU A . n A 1 241 LEU 241 241 241 LEU LEU A . n A 1 242 MET 242 242 242 MET MET A . n A 1 243 LYS 243 243 243 LYS LYS A . n A 1 244 TYR 244 244 244 TYR TYR A . n A 1 245 LEU 245 245 245 LEU LEU A . n A 1 246 GLY 246 246 246 GLY GLY A . n A 1 247 ASN 247 247 247 ASN ASN A . n A 1 248 ALA 248 248 248 ALA ALA A . n A 1 249 THR 249 249 249 THR THR A . n A 1 250 ALA 250 250 250 ALA ALA A . n A 1 251 ILE 251 251 251 ILE ILE A . n A 1 252 PHE 252 252 252 PHE PHE A . n A 1 253 PHE 253 253 253 PHE PHE A . n A 1 254 LEU 254 254 254 LEU LEU A . n A 1 255 PRO 255 255 255 PRO PRO A . n A 1 256 ASP 256 256 256 ASP ASP A . n A 1 257 GLU 257 257 257 GLU GLU A . n A 1 258 GLY 258 258 258 GLY GLY A . n A 1 259 LYS 259 259 259 LYS LYS A . n A 1 260 LEU 260 260 260 LEU LEU A . n A 1 261 GLN 261 261 261 GLN GLN A . n A 1 262 HIS 262 262 262 HIS HIS A . n A 1 263 LEU 263 263 263 LEU LEU A . n A 1 264 GLU 264 264 264 GLU GLU A . n A 1 265 ASN 265 265 265 ASN ASN A . n A 1 266 GLU 266 266 266 GLU GLU A . n A 1 267 LEU 267 267 267 LEU LEU A . n A 1 268 THR 268 268 268 THR THR A . n A 1 269 HIS 269 269 269 HIS HIS A . n A 1 270 ASP 270 270 270 ASP ASP A . n A 1 271 ILE 271 271 271 ILE ILE A . n A 1 272 ILE 272 272 272 ILE ILE A . n A 1 273 THR 273 273 273 THR THR A . n A 1 274 LYS 274 274 274 LYS LYS A . n A 1 275 PHE 275 275 275 PHE PHE A . n A 1 276 LEU 276 276 276 LEU LEU A . n A 1 277 GLU 277 277 277 GLU GLU A . n A 1 278 ASN 278 278 278 ASN ASN A . n A 1 279 GLU 279 279 279 GLU GLU A . n A 1 280 ASP 280 280 280 ASP ASP A . n A 1 281 ARG 281 281 281 ARG ARG A . n A 1 282 ARG 282 282 282 ARG ARG A . n A 1 283 SER 283 283 283 SER SER A . n A 1 284 ALA 284 284 284 ALA ALA A . n A 1 285 SER 285 285 285 SER SER A . n A 1 286 LEU 286 286 286 LEU LEU A . n A 1 287 HIS 287 287 287 HIS HIS A . n A 1 288 LEU 288 288 288 LEU LEU A . n A 1 289 PRO 289 289 289 PRO PRO A . n A 1 290 LYS 290 290 290 LYS LYS A . n A 1 291 LEU 291 291 291 LEU LEU A . n A 1 292 SER 292 292 292 SER SER A . n A 1 293 ILE 293 293 293 ILE ILE A . n A 1 294 THR 294 294 294 THR THR A . n A 1 295 GLY 295 295 295 GLY GLY A . n A 1 296 THR 296 296 296 THR THR A . n A 1 297 TYR 297 297 297 TYR TYR A . n A 1 298 ASP 298 298 298 ASP ASP A . n A 1 299 LEU 299 299 299 LEU LEU A . n A 1 300 LYS 300 300 300 LYS LYS A . n A 1 301 SER 301 301 301 SER SER A . n A 1 302 VAL 302 302 302 VAL VAL A . n A 1 303 LEU 303 303 303 LEU LEU A . n A 1 304 GLY 304 304 304 GLY GLY A . n A 1 305 GLN 305 305 305 GLN GLN A . n A 1 306 LEU 306 306 306 LEU LEU A . n A 1 307 GLY 307 307 307 GLY GLY A . n A 1 308 ILE 308 308 308 ILE ILE A . n A 1 309 THR 309 309 309 THR THR A . n A 1 310 LYS 310 310 310 LYS LYS A . n A 1 311 VAL 311 311 311 VAL VAL A . n A 1 312 PHE 312 312 312 PHE PHE A . n A 1 313 SER 313 313 313 SER SER A . n A 1 314 ASN 314 314 314 ASN ASN A . n A 1 315 GLY 315 315 315 GLY GLY A . n A 1 316 ALA 316 316 316 ALA ALA A . n A 1 317 ASP 317 317 317 ASP ASP A . n A 1 318 LEU 318 318 318 LEU LEU A . n A 1 319 SER 319 319 319 SER SER A . n A 1 320 GLY 320 320 320 GLY GLY A . n A 1 321 VAL 321 321 321 VAL VAL A . n A 1 322 THR 322 322 322 THR THR A . n A 1 323 GLU 323 323 323 GLU GLU A . n A 1 324 GLU 324 324 324 GLU GLU A . n A 1 325 ALA 325 325 325 ALA ALA A . n A 1 326 PRO 326 326 326 PRO PRO A . n A 1 327 LEU 327 327 327 LEU LEU A . n A 1 328 LYS 328 328 328 LYS LYS A . n A 1 329 LEU 329 329 329 LEU LEU A . n A 1 330 SER 330 330 330 SER SER A . n A 1 331 LYS 331 331 331 LYS LYS A . n A 1 332 ALA 332 332 332 ALA ALA A . n A 1 333 VAL 333 333 333 VAL VAL A . n A 1 334 HIS 334 334 334 HIS HIS A . n A 1 335 LYS 335 335 335 LYS LYS A . n A 1 336 ALA 336 336 336 ALA ALA A . n A 1 337 VAL 337 337 337 VAL VAL A . n A 1 338 LEU 338 338 338 LEU LEU A . n A 1 339 THR 339 339 339 THR THR A . n A 1 340 ILE 340 340 340 ILE ILE A . n A 1 341 ASP 341 341 341 ASP ASP A . n A 1 342 GLU 342 342 342 GLU GLU A . n A 1 343 LYS 343 343 343 LYS LYS A . n A 1 344 GLY 344 344 344 GLY GLY A . n A 1 345 THR 345 345 345 THR THR A . n A 1 346 GLU 346 346 346 GLU GLU A . n A 1 347 ALA 347 347 347 ALA ALA A . n A 1 348 ALA 348 348 348 ALA ALA A . n A 1 349 GLY 349 349 349 GLY GLY A . n A 1 350 ALA 350 350 350 ALA ALA A . n A 1 351 MET 351 351 351 MET MET A . n A 1 352 PHE 352 352 352 PHE PHE A . n A 1 353 LEU 353 353 353 LEU LEU A . n A 1 354 GLU 354 354 354 GLU GLU A . n A 1 355 ALA 355 355 355 ALA ALA A . n A 1 356 ILE 356 356 356 ILE ILE A . n A 1 357 PRO 357 357 357 PRO PRO A . n A 1 358 MET 358 358 358 MET MET A . n A 1 359 SER 359 359 359 SER SER A . n A 1 360 ILE 360 360 360 ILE ILE A . n A 1 361 PRO 361 361 361 PRO PRO A . n A 1 362 PRO 362 362 362 PRO PRO A . n A 1 363 GLU 363 363 363 GLU GLU A . n A 1 364 VAL 364 364 364 VAL VAL A . n A 1 365 LYS 365 365 365 LYS LYS A . n A 1 366 PHE 366 366 366 PHE PHE A . n A 1 367 ASN 367 367 367 ASN ASN A . n A 1 368 LYS 368 368 368 LYS LYS A . n A 1 369 PRO 369 369 369 PRO PRO A . n A 1 370 PHE 370 370 370 PHE PHE A . n A 1 371 VAL 371 371 371 VAL VAL A . n A 1 372 PHE 372 372 372 PHE PHE A . n A 1 373 LEU 373 373 373 LEU LEU A . n A 1 374 MET 374 374 374 MET MET A . n A 1 375 ILE 375 375 375 ILE ILE A . n A 1 376 GLU 376 376 376 GLU GLU A . n A 1 377 GLN 377 377 377 GLN GLN A . n A 1 378 ASN 378 378 378 ASN ASN A . n A 1 379 THR 379 379 379 THR THR A . n A 1 380 LYS 380 380 380 LYS LYS A . n A 1 381 SER 381 381 381 SER SER A . n A 1 382 PRO 382 382 382 PRO PRO A . n A 1 383 LEU 383 383 383 LEU LEU A . n A 1 384 PHE 384 384 384 PHE PHE A . n A 1 385 MET 385 385 385 MET MET A . n A 1 386 GLY 386 386 386 GLY GLY A . n A 1 387 LYS 387 387 387 LYS LYS A . n A 1 388 VAL 388 388 388 VAL VAL A . n A 1 389 VAL 389 389 389 VAL VAL A . n A 1 390 ASN 390 390 390 ASN ASN A . n A 1 391 PRO 391 391 391 PRO PRO A . n A 1 392 THR 392 392 392 THR THR A . n A 1 393 GLN 393 393 393 GLN GLN A . n A 1 394 LYS 394 394 394 LYS LYS A . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code B 2 HOH 1 2001 2001 HOH HOH A . B 2 HOH 2 2002 2002 HOH HOH A . B 2 HOH 3 2003 2003 HOH HOH A . B 2 HOH 4 2004 2004 HOH HOH A . B 2 HOH 5 2005 2005 HOH HOH A . B 2 HOH 6 2006 2006 HOH HOH A . B 2 HOH 7 2007 2007 HOH HOH A . B 2 HOH 8 2008 2008 HOH HOH A . B 2 HOH 9 2009 2009 HOH HOH A . B 2 HOH 10 2010 2010 HOH HOH A . B 2 HOH 11 2011 2011 HOH HOH A . B 2 HOH 12 2012 2012 HOH HOH A . B 2 HOH 13 2013 2013 HOH HOH A . B 2 HOH 14 2014 2014 HOH HOH A . B 2 HOH 15 2015 2015 HOH HOH A . B 2 HOH 16 2016 2016 HOH HOH A . B 2 HOH 17 2017 2017 HOH HOH A . B 2 HOH 18 2018 2018 HOH HOH A . B 2 HOH 19 2019 2019 HOH HOH A . B 2 HOH 20 2020 2020 HOH HOH A . B 2 HOH 21 2021 2021 HOH HOH A . B 2 HOH 22 2022 2022 HOH HOH A . B 2 HOH 23 2023 2023 HOH HOH A . B 2 HOH 24 2024 2024 HOH HOH A . B 2 HOH 25 2025 2025 HOH HOH A . B 2 HOH 26 2026 2026 HOH HOH A . B 2 HOH 27 2027 2027 HOH HOH A . B 2 HOH 28 2028 2028 HOH HOH A . B 2 HOH 29 2029 2029 HOH HOH A . B 2 HOH 30 2030 2030 HOH HOH A . B 2 HOH 31 2031 2031 HOH HOH A . B 2 HOH 32 2032 2032 HOH HOH A . B 2 HOH 33 2033 2033 HOH HOH A . B 2 HOH 34 2034 2034 HOH HOH A . B 2 HOH 35 2035 2035 HOH HOH A . B 2 HOH 36 2036 2036 HOH HOH A . B 2 HOH 37 2037 2037 HOH HOH A . B 2 HOH 38 2038 2038 HOH HOH A . B 2 HOH 39 2039 2039 HOH HOH A . B 2 HOH 40 2040 2040 HOH HOH A . B 2 HOH 41 2041 2041 HOH HOH A . B 2 HOH 42 2042 2042 HOH HOH A . B 2 HOH 43 2043 2043 HOH HOH A . B 2 HOH 44 2044 2044 HOH HOH A . B 2 HOH 45 2045 2045 HOH HOH A . B 2 HOH 46 2046 2046 HOH HOH A . B 2 HOH 47 2047 2047 HOH HOH A . B 2 HOH 48 2048 2048 HOH HOH A . B 2 HOH 49 2049 2049 HOH HOH A . B 2 HOH 50 2050 2050 HOH HOH A . B 2 HOH 51 2051 2051 HOH HOH A . B 2 HOH 52 2052 2052 HOH HOH A . B 2 HOH 53 2053 2053 HOH HOH A . B 2 HOH 54 2054 2054 HOH HOH A . B 2 HOH 55 2055 2055 HOH HOH A . B 2 HOH 56 2056 2056 HOH HOH A . B 2 HOH 57 2057 2057 HOH HOH A . B 2 HOH 58 2058 2058 HOH HOH A . B 2 HOH 59 2059 2059 HOH HOH A . B 2 HOH 60 2060 2060 HOH HOH A . B 2 HOH 61 2061 2061 HOH HOH A . B 2 HOH 62 2062 2062 HOH HOH A . B 2 HOH 63 2063 2063 HOH HOH A . B 2 HOH 64 2064 2064 HOH HOH A . B 2 HOH 65 2065 2065 HOH HOH A . B 2 HOH 66 2066 2066 HOH HOH A . B 2 HOH 67 2067 2067 HOH HOH A . B 2 HOH 68 2068 2068 HOH HOH A . B 2 HOH 69 2069 2069 HOH HOH A . B 2 HOH 70 2070 2070 HOH HOH A . B 2 HOH 71 2071 2071 HOH HOH A . B 2 HOH 72 2072 2072 HOH HOH A . B 2 HOH 73 2073 2073 HOH HOH A . B 2 HOH 74 2074 2074 HOH HOH A . B 2 HOH 75 2075 2075 HOH HOH A . B 2 HOH 76 2076 2076 HOH HOH A . B 2 HOH 77 2077 2077 HOH HOH A . B 2 HOH 78 2078 2078 HOH HOH A . B 2 HOH 79 2079 2079 HOH HOH A . B 2 HOH 80 2080 2080 HOH HOH A . B 2 HOH 81 2081 2081 HOH HOH A . B 2 HOH 82 2082 2082 HOH HOH A . B 2 HOH 83 2083 2083 HOH HOH A . B 2 HOH 84 2084 2084 HOH HOH A . B 2 HOH 85 2085 2085 HOH HOH A . B 2 HOH 86 2086 2086 HOH HOH A . B 2 HOH 87 2087 2087 HOH HOH A . B 2 HOH 88 2088 2088 HOH HOH A . B 2 HOH 89 2089 2089 HOH HOH A . B 2 HOH 90 2090 2090 HOH HOH A . B 2 HOH 91 2091 2091 HOH HOH A . B 2 HOH 92 2092 2092 HOH HOH A . B 2 HOH 93 2093 2093 HOH HOH A . B 2 HOH 94 2094 2094 HOH HOH A . B 2 HOH 95 2095 2095 HOH HOH A . B 2 HOH 96 2096 2096 HOH HOH A . B 2 HOH 97 2097 2097 HOH HOH A . B 2 HOH 98 2098 2098 HOH HOH A . B 2 HOH 99 2099 2099 HOH HOH A . B 2 HOH 100 2100 2100 HOH HOH A . B 2 HOH 101 2101 2101 HOH HOH A . B 2 HOH 102 2102 2102 HOH HOH A . B 2 HOH 103 2103 2103 HOH HOH A . B 2 HOH 104 2104 2104 HOH HOH A . B 2 HOH 105 2105 2105 HOH HOH A . B 2 HOH 106 2106 2106 HOH HOH A . # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details software_defined_assembly _pdbx_struct_assembly.method_details PQS _pdbx_struct_assembly.oligomeric_details monomeric _pdbx_struct_assembly.oligomeric_count 1 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B # _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 1999-09-27 2 'Structure model' 1 1 2011-05-08 3 'Structure model' 1 2 2011-07-13 4 'Structure model' 1 3 2019-05-22 5 'Structure model' 1 4 2019-10-09 6 'Structure model' 1 5 2023-12-13 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? _pdbx_audit_revision_details.details ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Version format compliance' 2 3 'Structure model' 'Version format compliance' 3 4 'Structure model' 'Data collection' 4 4 'Structure model' Other 5 4 'Structure model' 'Refinement description' 6 5 'Structure model' 'Data collection' 7 5 'Structure model' 'Database references' 8 5 'Structure model' Other 9 6 'Structure model' 'Data collection' 10 6 'Structure model' 'Database references' 11 6 'Structure model' 'Refinement description' # 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 4 'Structure model' pdbx_database_proc 2 4 'Structure model' pdbx_database_status 3 4 'Structure model' refine 4 5 'Structure model' citation 5 5 'Structure model' citation_author 6 5 'Structure model' pdbx_database_status 7 6 'Structure model' chem_comp_atom 8 6 'Structure model' chem_comp_bond 9 6 'Structure model' database_2 10 6 'Structure model' pdbx_initial_refinement_model # 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 4 'Structure model' '_pdbx_database_status.recvd_author_approval' 2 4 'Structure model' '_refine.pdbx_ls_cross_valid_method' 3 5 'Structure model' '_citation.page_last' 4 5 'Structure model' '_citation.pdbx_database_id_DOI' 5 5 'Structure model' '_citation.title' 6 5 'Structure model' '_citation_author.name' 7 5 'Structure model' '_pdbx_database_status.status_code_sf' 8 6 'Structure model' '_database_2.pdbx_DOI' 9 6 'Structure model' '_database_2.pdbx_database_accession' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal CNS refinement 0.5 ? 1 MOSFLM 'data reduction' . ? 2 SCALA 'data scaling' . ? 3 CNS phasing 0.5 ? 4 # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 ALA A 70 ? ? 50.98 -141.27 2 1 PRO A 106 ? ? -49.31 -91.16 3 1 ASP A 107 ? ? -46.97 -14.45 4 1 GLN A 111 ? ? 64.40 61.11 5 1 HIS A 139 ? ? 34.80 54.53 6 1 ASN A 247 ? ? -106.72 40.53 7 1 THR A 392 ? ? -78.89 34.09 # 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 MET 1 ? A MET 1 2 1 Y 1 A ASP 2 ? A ASP 2 3 1 Y 1 A PRO 3 ? A PRO 3 4 1 Y 1 A GLN 4 ? A GLN 4 5 1 Y 1 A GLY 5 ? A GLY 5 6 1 Y 1 A ASP 6 ? A ASP 6 7 1 Y 1 A ALA 7 ? A ALA 7 8 1 Y 1 A ALA 8 ? A ALA 8 9 1 Y 1 A GLN 9 ? A GLN 9 10 1 Y 1 A LYS 10 ? A LYS 10 11 1 Y 1 A THR 11 ? A THR 11 12 1 Y 1 A ASP 12 ? A ASP 12 13 1 Y 1 A THR 13 ? A THR 13 14 1 Y 1 A SER 14 ? A SER 14 15 1 Y 1 A HIS 15 ? A HIS 15 16 1 Y 1 A HIS 16 ? A HIS 16 17 1 Y 1 A ASP 17 ? A ASP 17 18 1 Y 1 A GLN 18 ? A GLN 18 19 1 Y 1 A ASP 19 ? A ASP 19 20 1 Y 1 A HIS 20 ? A HIS 20 21 1 Y 1 A PRO 21 ? A PRO 21 22 1 Y 1 A THR 22 ? A THR 22 # loop_ _chem_comp_atom.comp_id _chem_comp_atom.atom_id _chem_comp_atom.type_symbol _chem_comp_atom.pdbx_aromatic_flag _chem_comp_atom.pdbx_stereo_config _chem_comp_atom.pdbx_ordinal ALA N N N N 1 ALA CA C N S 2 ALA C C N N 3 ALA O O N N 4 ALA CB C N N 5 ALA OXT O N N 6 ALA H H N N 7 ALA H2 H N N 8 ALA HA H N N 9 ALA HB1 H N N 10 ALA HB2 H N N 11 ALA HB3 H N N 12 ALA HXT H N N 13 ARG N N N N 14 ARG CA C N S 15 ARG C C N N 16 ARG O O N N 17 ARG CB C N N 18 ARG CG C N N 19 ARG CD C N N 20 ARG NE N N N 21 ARG CZ C N N 22 ARG NH1 N N N 23 ARG NH2 N N N 24 ARG OXT O N N 25 ARG H H N N 26 ARG H2 H N N 27 ARG HA H N N 28 ARG HB2 H N N 29 ARG HB3 H N N 30 ARG HG2 H N N 31 ARG HG3 H N N 32 ARG HD2 H N N 33 ARG HD3 H N N 34 ARG HE H N N 35 ARG HH11 H N N 36 ARG HH12 H N N 37 ARG HH21 H N N 38 ARG HH22 H N N 39 ARG HXT H N N 40 ASN N N N N 41 ASN CA C N S 42 ASN C C N N 43 ASN O O N N 44 ASN CB C N N 45 ASN CG C N N 46 ASN OD1 O N N 47 ASN ND2 N N N 48 ASN OXT O N N 49 ASN H H N N 50 ASN H2 H N N 51 ASN HA H N N 52 ASN HB2 H N N 53 ASN HB3 H N N 54 ASN HD21 H N N 55 ASN HD22 H N N 56 ASN HXT H N N 57 ASP N N N N 58 ASP CA C N S 59 ASP C C N N 60 ASP O O N N 61 ASP CB C N N 62 ASP CG C N N 63 ASP OD1 O N N 64 ASP OD2 O N N 65 ASP OXT O N N 66 ASP H H N N 67 ASP H2 H N N 68 ASP HA H N N 69 ASP HB2 H N N 70 ASP HB3 H N N 71 ASP HD2 H N N 72 ASP HXT H N N 73 CYS N N N N 74 CYS CA C N R 75 CYS C C N N 76 CYS O O N N 77 CYS CB C N N 78 CYS SG S N N 79 CYS OXT O N N 80 CYS H H N N 81 CYS H2 H N N 82 CYS HA H N N 83 CYS HB2 H N N 84 CYS HB3 H N N 85 CYS HG H N N 86 CYS HXT H N N 87 GLN N N N N 88 GLN CA C N S 89 GLN C C N N 90 GLN O O N N 91 GLN CB C N N 92 GLN CG C N N 93 GLN CD C N N 94 GLN OE1 O N N 95 GLN NE2 N N N 96 GLN OXT O N N 97 GLN H H N N 98 GLN H2 H N N 99 GLN HA H N N 100 GLN HB2 H N N 101 GLN HB3 H N N 102 GLN HG2 H N N 103 GLN HG3 H N N 104 GLN HE21 H N N 105 GLN HE22 H N N 106 GLN HXT H N N 107 GLU N N N N 108 GLU CA C N S 109 GLU C C N N 110 GLU O O N N 111 GLU CB C N N 112 GLU CG C N N 113 GLU CD C N N 114 GLU OE1 O N N 115 GLU OE2 O N N 116 GLU OXT O N N 117 GLU H H N N 118 GLU H2 H N N 119 GLU HA H N N 120 GLU HB2 H N N 121 GLU HB3 H N N 122 GLU HG2 H N N 123 GLU HG3 H N N 124 GLU HE2 H N N 125 GLU HXT H N N 126 GLY N N N N 127 GLY CA C N N 128 GLY C C N N 129 GLY O O N N 130 GLY OXT O N N 131 GLY H H N N 132 GLY H2 H N N 133 GLY HA2 H N N 134 GLY HA3 H N N 135 GLY HXT H N N 136 HIS N N N N 137 HIS CA C N S 138 HIS C C N N 139 HIS O O N N 140 HIS CB C N N 141 HIS CG C Y N 142 HIS ND1 N Y N 143 HIS CD2 C Y N 144 HIS CE1 C Y N 145 HIS NE2 N Y N 146 HIS OXT O N N 147 HIS H H N N 148 HIS H2 H N N 149 HIS HA H N N 150 HIS HB2 H N N 151 HIS HB3 H N N 152 HIS HD1 H N N 153 HIS HD2 H N N 154 HIS HE1 H N N 155 HIS HE2 H N N 156 HIS HXT H N N 157 HOH O O N N 158 HOH H1 H N N 159 HOH H2 H N N 160 ILE N N N N 161 ILE CA C N S 162 ILE C C N N 163 ILE O O N N 164 ILE CB C N S 165 ILE CG1 C N N 166 ILE CG2 C N N 167 ILE CD1 C N N 168 ILE OXT O N N 169 ILE H H N N 170 ILE H2 H N N 171 ILE HA H N N 172 ILE HB H N N 173 ILE HG12 H N N 174 ILE HG13 H N N 175 ILE HG21 H N N 176 ILE HG22 H N N 177 ILE HG23 H N N 178 ILE HD11 H N N 179 ILE HD12 H N N 180 ILE HD13 H N N 181 ILE HXT H N N 182 LEU N N N N 183 LEU CA C N S 184 LEU C C N N 185 LEU O O N N 186 LEU CB C N N 187 LEU CG C N N 188 LEU CD1 C N N 189 LEU CD2 C N N 190 LEU OXT O N N 191 LEU H H N N 192 LEU H2 H N N 193 LEU HA H N N 194 LEU HB2 H N N 195 LEU HB3 H N N 196 LEU HG H N N 197 LEU HD11 H N N 198 LEU HD12 H N N 199 LEU HD13 H N N 200 LEU HD21 H N N 201 LEU HD22 H N N 202 LEU HD23 H N N 203 LEU HXT H N N 204 LYS N N N N 205 LYS CA C N S 206 LYS C C N N 207 LYS O O N N 208 LYS CB C N N 209 LYS CG C N N 210 LYS CD C N N 211 LYS CE C N N 212 LYS NZ N N N 213 LYS OXT O N N 214 LYS H H N N 215 LYS H2 H N N 216 LYS HA H N N 217 LYS HB2 H N N 218 LYS HB3 H N N 219 LYS HG2 H N N 220 LYS HG3 H N N 221 LYS HD2 H N N 222 LYS HD3 H N N 223 LYS HE2 H N N 224 LYS HE3 H N N 225 LYS HZ1 H N N 226 LYS HZ2 H N N 227 LYS HZ3 H N N 228 LYS HXT H N N 229 MET N N N N 230 MET CA C N S 231 MET C C N N 232 MET O O N N 233 MET CB C N N 234 MET CG C N N 235 MET SD S N N 236 MET CE C N N 237 MET OXT O N N 238 MET H H N N 239 MET H2 H N N 240 MET HA H N N 241 MET HB2 H N N 242 MET HB3 H N N 243 MET HG2 H N N 244 MET HG3 H N N 245 MET HE1 H N N 246 MET HE2 H N N 247 MET HE3 H N N 248 MET HXT H N N 249 PHE N N N N 250 PHE CA C N S 251 PHE C C N N 252 PHE O O N N 253 PHE CB C N N 254 PHE CG C Y N 255 PHE CD1 C Y N 256 PHE CD2 C Y N 257 PHE CE1 C Y N 258 PHE CE2 C Y N 259 PHE CZ C Y N 260 PHE OXT O N N 261 PHE H H N N 262 PHE H2 H N N 263 PHE HA H N N 264 PHE HB2 H N N 265 PHE HB3 H N N 266 PHE HD1 H N N 267 PHE HD2 H N N 268 PHE HE1 H N N 269 PHE HE2 H N N 270 PHE HZ H N N 271 PHE HXT H N N 272 PRO N N N N 273 PRO CA C N S 274 PRO C C N N 275 PRO O O N N 276 PRO CB C N N 277 PRO CG C N N 278 PRO CD C N N 279 PRO OXT O N N 280 PRO H H N N 281 PRO HA H N N 282 PRO HB2 H N N 283 PRO HB3 H N N 284 PRO HG2 H N N 285 PRO HG3 H N N 286 PRO HD2 H N N 287 PRO HD3 H N N 288 PRO HXT H N N 289 SER N N N N 290 SER CA C N S 291 SER C C N N 292 SER O O N N 293 SER CB C N N 294 SER OG O N N 295 SER OXT O N N 296 SER H H N N 297 SER H2 H N N 298 SER HA H N N 299 SER HB2 H N N 300 SER HB3 H N N 301 SER HG H N N 302 SER HXT H N N 303 THR N N N N 304 THR CA C N S 305 THR C C N N 306 THR O O N N 307 THR CB C N R 308 THR OG1 O N N 309 THR CG2 C N N 310 THR OXT O N N 311 THR H H N N 312 THR H2 H N N 313 THR HA H N N 314 THR HB H N N 315 THR HG1 H N N 316 THR HG21 H N N 317 THR HG22 H N N 318 THR HG23 H N N 319 THR HXT H N N 320 TRP N N N N 321 TRP CA C N S 322 TRP C C N N 323 TRP O O N N 324 TRP CB C N N 325 TRP CG C Y N 326 TRP CD1 C Y N 327 TRP CD2 C Y N 328 TRP NE1 N Y N 329 TRP CE2 C Y N 330 TRP CE3 C Y N 331 TRP CZ2 C Y N 332 TRP CZ3 C Y N 333 TRP CH2 C Y N 334 TRP OXT O N N 335 TRP H H N N 336 TRP H2 H N N 337 TRP HA H N N 338 TRP HB2 H N N 339 TRP HB3 H N N 340 TRP HD1 H N N 341 TRP HE1 H N N 342 TRP HE3 H N N 343 TRP HZ2 H N N 344 TRP HZ3 H N N 345 TRP HH2 H N N 346 TRP HXT H N N 347 TYR N N N N 348 TYR CA C N S 349 TYR C C N N 350 TYR O O N N 351 TYR CB C N N 352 TYR CG C Y N 353 TYR CD1 C Y N 354 TYR CD2 C Y N 355 TYR CE1 C Y N 356 TYR CE2 C Y N 357 TYR CZ C Y N 358 TYR OH O N N 359 TYR OXT O N N 360 TYR H H N N 361 TYR H2 H N N 362 TYR HA H N N 363 TYR HB2 H N N 364 TYR HB3 H N N 365 TYR HD1 H N N 366 TYR HD2 H N N 367 TYR HE1 H N N 368 TYR HE2 H N N 369 TYR HH H N N 370 TYR HXT H N N 371 VAL N N N N 372 VAL CA C N S 373 VAL C C N N 374 VAL O O N N 375 VAL CB C N N 376 VAL CG1 C N N 377 VAL CG2 C N N 378 VAL OXT O N N 379 VAL H H N N 380 VAL H2 H N N 381 VAL HA H N N 382 VAL HB H N N 383 VAL HG11 H N N 384 VAL HG12 H N N 385 VAL HG13 H N N 386 VAL HG21 H N N 387 VAL HG22 H N N 388 VAL HG23 H N N 389 VAL HXT H N N 390 # loop_ _chem_comp_bond.comp_id _chem_comp_bond.atom_id_1 _chem_comp_bond.atom_id_2 _chem_comp_bond.value_order _chem_comp_bond.pdbx_aromatic_flag _chem_comp_bond.pdbx_stereo_config _chem_comp_bond.pdbx_ordinal ALA N CA sing N N 1 ALA N H sing N N 2 ALA N H2 sing N N 3 ALA CA C sing N N 4 ALA CA CB sing N N 5 ALA CA HA sing N N 6 ALA C O doub N N 7 ALA C OXT sing N N 8 ALA CB HB1 sing N N 9 ALA CB HB2 sing N N 10 ALA CB HB3 sing N N 11 ALA OXT HXT sing N N 12 ARG N CA sing N N 13 ARG N H sing N N 14 ARG N H2 sing N N 15 ARG CA C sing N N 16 ARG CA CB sing N N 17 ARG CA HA sing N N 18 ARG C O doub N N 19 ARG C OXT sing N N 20 ARG CB CG sing N N 21 ARG CB HB2 sing N N 22 ARG CB HB3 sing N N 23 ARG CG CD sing N N 24 ARG CG HG2 sing N N 25 ARG CG HG3 sing N N 26 ARG CD NE sing N N 27 ARG CD HD2 sing N N 28 ARG CD HD3 sing N N 29 ARG NE CZ sing N N 30 ARG NE HE sing N N 31 ARG CZ NH1 sing N N 32 ARG CZ NH2 doub N N 33 ARG NH1 HH11 sing N N 34 ARG NH1 HH12 sing N N 35 ARG NH2 HH21 sing N N 36 ARG NH2 HH22 sing N N 37 ARG OXT HXT sing N N 38 ASN N CA sing N N 39 ASN N H sing N N 40 ASN N H2 sing N N 41 ASN CA C sing N N 42 ASN CA CB sing N N 43 ASN CA HA sing N N 44 ASN C O doub N N 45 ASN C OXT sing N N 46 ASN CB CG sing N N 47 ASN CB HB2 sing N N 48 ASN CB HB3 sing N N 49 ASN CG OD1 doub N N 50 ASN CG ND2 sing N N 51 ASN ND2 HD21 sing N N 52 ASN ND2 HD22 sing N N 53 ASN OXT HXT sing N N 54 ASP N CA sing N N 55 ASP N H sing N N 56 ASP N H2 sing N N 57 ASP CA C sing N N 58 ASP CA CB sing N N 59 ASP CA HA sing N N 60 ASP C O doub N N 61 ASP C OXT sing N N 62 ASP CB CG sing N N 63 ASP CB HB2 sing N N 64 ASP CB HB3 sing N N 65 ASP CG OD1 doub N N 66 ASP CG OD2 sing N N 67 ASP OD2 HD2 sing N N 68 ASP OXT HXT sing N N 69 CYS N CA sing N N 70 CYS N H sing N N 71 CYS N H2 sing N N 72 CYS CA C sing N N 73 CYS CA CB sing N N 74 CYS CA HA sing N N 75 CYS C O doub N N 76 CYS C OXT sing N N 77 CYS CB SG sing N N 78 CYS CB HB2 sing N N 79 CYS CB HB3 sing N N 80 CYS SG HG sing N N 81 CYS OXT HXT sing N N 82 GLN N CA sing N N 83 GLN N H sing N N 84 GLN N H2 sing N N 85 GLN CA C sing N N 86 GLN CA CB sing N N 87 GLN CA HA sing N N 88 GLN C O doub N N 89 GLN C OXT sing N N 90 GLN CB CG sing N N 91 GLN CB HB2 sing N N 92 GLN CB HB3 sing N N 93 GLN CG CD sing N N 94 GLN CG HG2 sing N N 95 GLN CG HG3 sing N N 96 GLN CD OE1 doub N N 97 GLN CD NE2 sing N N 98 GLN NE2 HE21 sing N N 99 GLN NE2 HE22 sing N N 100 GLN OXT HXT sing N N 101 GLU N CA sing N N 102 GLU N H sing N N 103 GLU N H2 sing N N 104 GLU CA C sing N N 105 GLU CA CB sing N N 106 GLU CA HA sing N N 107 GLU C O doub N N 108 GLU C OXT sing N N 109 GLU CB CG sing N N 110 GLU CB HB2 sing N N 111 GLU CB HB3 sing N N 112 GLU CG CD sing N N 113 GLU CG HG2 sing N N 114 GLU CG HG3 sing N N 115 GLU CD OE1 doub N N 116 GLU CD OE2 sing N N 117 GLU OE2 HE2 sing N N 118 GLU OXT HXT sing N N 119 GLY N CA sing N N 120 GLY N H sing N N 121 GLY N H2 sing N N 122 GLY CA C sing N N 123 GLY CA HA2 sing N N 124 GLY CA HA3 sing N N 125 GLY C O doub N N 126 GLY C OXT sing N N 127 GLY OXT HXT sing N N 128 HIS N CA sing N N 129 HIS N H sing N N 130 HIS N H2 sing N N 131 HIS CA C sing N N 132 HIS CA CB sing N N 133 HIS CA HA sing N N 134 HIS C O doub N N 135 HIS C OXT sing N N 136 HIS CB CG sing N N 137 HIS CB HB2 sing N N 138 HIS CB HB3 sing N N 139 HIS CG ND1 sing Y N 140 HIS CG CD2 doub Y N 141 HIS ND1 CE1 doub Y N 142 HIS ND1 HD1 sing N N 143 HIS CD2 NE2 sing Y N 144 HIS CD2 HD2 sing N N 145 HIS CE1 NE2 sing Y N 146 HIS CE1 HE1 sing N N 147 HIS NE2 HE2 sing N N 148 HIS OXT HXT sing N N 149 HOH O H1 sing N N 150 HOH O H2 sing N N 151 ILE N CA sing N N 152 ILE N H sing N N 153 ILE N H2 sing N N 154 ILE CA C sing N N 155 ILE CA CB sing N N 156 ILE CA HA sing N N 157 ILE C O doub N N 158 ILE C OXT sing N N 159 ILE CB CG1 sing N N 160 ILE CB CG2 sing N N 161 ILE CB HB sing N N 162 ILE CG1 CD1 sing N N 163 ILE CG1 HG12 sing N N 164 ILE CG1 HG13 sing N N 165 ILE CG2 HG21 sing N N 166 ILE CG2 HG22 sing N N 167 ILE CG2 HG23 sing N N 168 ILE CD1 HD11 sing N N 169 ILE CD1 HD12 sing N N 170 ILE CD1 HD13 sing N N 171 ILE OXT HXT sing N N 172 LEU N CA sing N N 173 LEU N H sing N N 174 LEU N H2 sing N N 175 LEU CA C sing N N 176 LEU CA CB sing N N 177 LEU CA HA sing N N 178 LEU C O doub N N 179 LEU C OXT sing N N 180 LEU CB CG sing N N 181 LEU CB HB2 sing N N 182 LEU CB HB3 sing N N 183 LEU CG CD1 sing N N 184 LEU CG CD2 sing N N 185 LEU CG HG sing N N 186 LEU CD1 HD11 sing N N 187 LEU CD1 HD12 sing N N 188 LEU CD1 HD13 sing N N 189 LEU CD2 HD21 sing N N 190 LEU CD2 HD22 sing N N 191 LEU CD2 HD23 sing N N 192 LEU OXT HXT sing N N 193 LYS N CA sing N N 194 LYS N H sing N N 195 LYS N H2 sing N N 196 LYS CA C sing N N 197 LYS CA CB sing N N 198 LYS CA HA sing N N 199 LYS C O doub N N 200 LYS C OXT sing N N 201 LYS CB CG sing N N 202 LYS CB HB2 sing N N 203 LYS CB HB3 sing N N 204 LYS CG CD sing N N 205 LYS CG HG2 sing N N 206 LYS CG HG3 sing N N 207 LYS CD CE sing N N 208 LYS CD HD2 sing N N 209 LYS CD HD3 sing N N 210 LYS CE NZ sing N N 211 LYS CE HE2 sing N N 212 LYS CE HE3 sing N N 213 LYS NZ HZ1 sing N N 214 LYS NZ HZ2 sing N N 215 LYS NZ HZ3 sing N N 216 LYS OXT HXT sing N N 217 MET N CA sing N N 218 MET N H sing N N 219 MET N H2 sing N N 220 MET CA C sing N N 221 MET CA CB sing N N 222 MET CA HA sing N N 223 MET C O doub N N 224 MET C OXT sing N N 225 MET CB CG sing N N 226 MET CB HB2 sing N N 227 MET CB HB3 sing N N 228 MET CG SD sing N N 229 MET CG HG2 sing N N 230 MET CG HG3 sing N N 231 MET SD CE sing N N 232 MET CE HE1 sing N N 233 MET CE HE2 sing N N 234 MET CE HE3 sing N N 235 MET OXT HXT sing N N 236 PHE N CA sing N N 237 PHE N H sing N N 238 PHE N H2 sing N N 239 PHE CA C sing N N 240 PHE CA CB sing N N 241 PHE CA HA sing N N 242 PHE C O doub N N 243 PHE C OXT sing N N 244 PHE CB CG sing N N 245 PHE CB HB2 sing N N 246 PHE CB HB3 sing N N 247 PHE CG CD1 doub Y N 248 PHE CG CD2 sing Y N 249 PHE CD1 CE1 sing Y N 250 PHE CD1 HD1 sing N N 251 PHE CD2 CE2 doub Y N 252 PHE CD2 HD2 sing N N 253 PHE CE1 CZ doub Y N 254 PHE CE1 HE1 sing N N 255 PHE CE2 CZ sing Y N 256 PHE CE2 HE2 sing N N 257 PHE CZ HZ sing N N 258 PHE OXT HXT sing N N 259 PRO N CA sing N N 260 PRO N CD sing N N 261 PRO N H sing N N 262 PRO CA C sing N N 263 PRO CA CB sing N N 264 PRO CA HA sing N N 265 PRO C O doub N N 266 PRO C OXT sing N N 267 PRO CB CG sing N N 268 PRO CB HB2 sing N N 269 PRO CB HB3 sing N N 270 PRO CG CD sing N N 271 PRO CG HG2 sing N N 272 PRO CG HG3 sing N N 273 PRO CD HD2 sing N N 274 PRO CD HD3 sing N N 275 PRO OXT HXT sing N N 276 SER N CA sing N N 277 SER N H sing N N 278 SER N H2 sing N N 279 SER CA C sing N N 280 SER CA CB sing N N 281 SER CA HA sing N N 282 SER C O doub N N 283 SER C OXT sing N N 284 SER CB OG sing N N 285 SER CB HB2 sing N N 286 SER CB HB3 sing N N 287 SER OG HG sing N N 288 SER OXT HXT sing N N 289 THR N CA sing N N 290 THR N H sing N N 291 THR N H2 sing N N 292 THR CA C sing N N 293 THR CA CB sing N N 294 THR CA HA sing N N 295 THR C O doub N N 296 THR C OXT sing N N 297 THR CB OG1 sing N N 298 THR CB CG2 sing N N 299 THR CB HB sing N N 300 THR OG1 HG1 sing N N 301 THR CG2 HG21 sing N N 302 THR CG2 HG22 sing N N 303 THR CG2 HG23 sing N N 304 THR OXT HXT sing N N 305 TRP N CA sing N N 306 TRP N H sing N N 307 TRP N H2 sing N N 308 TRP CA C sing N N 309 TRP CA CB sing N N 310 TRP CA HA sing N N 311 TRP C O doub N N 312 TRP C OXT sing N N 313 TRP CB CG sing N N 314 TRP CB HB2 sing N N 315 TRP CB HB3 sing N N 316 TRP CG CD1 doub Y N 317 TRP CG CD2 sing Y N 318 TRP CD1 NE1 sing Y N 319 TRP CD1 HD1 sing N N 320 TRP CD2 CE2 doub Y N 321 TRP CD2 CE3 sing Y N 322 TRP NE1 CE2 sing Y N 323 TRP NE1 HE1 sing N N 324 TRP CE2 CZ2 sing Y N 325 TRP CE3 CZ3 doub Y N 326 TRP CE3 HE3 sing N N 327 TRP CZ2 CH2 doub Y N 328 TRP CZ2 HZ2 sing N N 329 TRP CZ3 CH2 sing Y N 330 TRP CZ3 HZ3 sing N N 331 TRP CH2 HH2 sing N N 332 TRP OXT HXT sing N N 333 TYR N CA sing N N 334 TYR N H sing N N 335 TYR N H2 sing N N 336 TYR CA C sing N N 337 TYR CA CB sing N N 338 TYR CA HA sing N N 339 TYR C O doub N N 340 TYR C OXT sing N N 341 TYR CB CG sing N N 342 TYR CB HB2 sing N N 343 TYR CB HB3 sing N N 344 TYR CG CD1 doub Y N 345 TYR CG CD2 sing Y N 346 TYR CD1 CE1 sing Y N 347 TYR CD1 HD1 sing N N 348 TYR CD2 CE2 doub Y N 349 TYR CD2 HD2 sing N N 350 TYR CE1 CZ doub Y N 351 TYR CE1 HE1 sing N N 352 TYR CE2 CZ sing Y N 353 TYR CE2 HE2 sing N N 354 TYR CZ OH sing N N 355 TYR OH HH sing N N 356 TYR OXT HXT sing N N 357 VAL N CA sing N N 358 VAL N H sing N N 359 VAL N H2 sing N N 360 VAL CA C sing N N 361 VAL CA CB sing N N 362 VAL CA HA sing N N 363 VAL C O doub N N 364 VAL C OXT sing N N 365 VAL CB CG1 sing N N 366 VAL CB CG2 sing N N 367 VAL CB HB sing N N 368 VAL CG1 HG11 sing N N 369 VAL CG1 HG12 sing N N 370 VAL CG1 HG13 sing N N 371 VAL CG2 HG21 sing N N 372 VAL CG2 HG22 sing N N 373 VAL CG2 HG23 sing N N 374 VAL OXT HXT sing N N 375 # _pdbx_entity_nonpoly.entity_id 2 _pdbx_entity_nonpoly.name water _pdbx_entity_nonpoly.comp_id HOH # _pdbx_initial_refinement_model.id 1 _pdbx_initial_refinement_model.entity_id_list ? _pdbx_initial_refinement_model.type 'experimental model' _pdbx_initial_refinement_model.source_name PDB _pdbx_initial_refinement_model.accession_code 1PSI _pdbx_initial_refinement_model.details 'THERMOSTABLE VARIANT ALPHA1-ANTITRYPSIN (PDB ENTRY 1PSI)' # If you find results from this site helpful for your research, please cite one of our papers:
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