data_1QMU # _entry.id 1QMU # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.279 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 1QMU PDBE EBI-4196 WWPDB D_1290004196 # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 1QMU _pdbx_database_status.deposit_site PDBE _pdbx_database_status.process_site PDBE _pdbx_database_status.SG_entry . _pdbx_database_status.recvd_initial_deposition_date 1999-10-06 _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_sf ? _pdbx_database_status.status_code_mr ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Gomis-Rueth, F.X.' 1 'Coll, M.' 2 'Aviles, F.X.' 3 'Vendrell, J.' 4 'Fricker, L.D.' 5 # _citation.id primary _citation.title 'Crystal Structure of Avian Carboxypeptidase D Domain II : A Prototype for the Regulatory Metallocarboxypeptidase Subfamily' _citation.journal_abbrev 'Embo J.' _citation.journal_volume 18 _citation.page_first 5817 _citation.page_last ? _citation.year 1999 _citation.journal_id_ASTM EMJODG _citation.country UK _citation.journal_id_ISSN 0261-4189 _citation.journal_id_CSD 0897 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 10545093 _citation.pdbx_database_id_DOI 10.1093/EMBOJ/18.21.5817 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Gomis-Rueth, F.X.' 1 primary 'Companys, V.' 2 primary 'Qian, Y.' 3 primary 'Fricker, L.D.' 4 primary 'Vendrell, J.' 5 primary 'Aviles, F.X.' 6 primary 'Coll, M.' 7 # _cell.entry_id 1QMU _cell.length_a 135.540 _cell.length_b 135.540 _cell.length_c 135.540 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 12 _cell.pdbx_unique_axis ? # _symmetry.entry_id 1QMU _symmetry.space_group_name_H-M 'P 21 3' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 198 # 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 'CARBOXYPEPTIDASE GP180 RESIDUES 503-882' 43337.297 1 ? ? YES ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 6 ? ? ? ? 3 non-polymer man ALPHA-D-MANNOSE 180.156 2 ? ? ? ? 4 non-polymer syn 'SULFATE ION' 96.063 3 ? ? ? ? 5 non-polymer syn 'ZINC ION' 65.409 1 ? ? ? ? 6 water nat water 18.015 121 ? ? ? ? # _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 ;QAVQPVDFRHHHFSDMEIFLRRYANEYPSITRLYSVGKSVELRELYVMEISDNPGIHEAGEPEFKYIGNMHGNEVVGREL LLNLIEYLCKNFGTDPEVTDLVQSTRIHIMPSMNPDGYEKSQEGDRGGTVGRNNSNNYDLNRNFPDQFFQVTDPPQPETL AVMSWLKTYPFVLSANLHGGSLVVNYPFDDDEQGIAIYSKSPDDAVFQQLALSYSKENKKMYQGSPCKDLYPTEYFPHGI TNGAQWYNVPGGMQDWNYLNTNCFEVTIELGCVKYPKAEELPKYWEQNRRSLLQFIKQVHRGIWGFVLDATDGRGILNAT ISVADINHPVTTYKDGDYWRLLVQGTYKVTASARGYDPVTKTVEVDSKGGVQVNFTLSRT ; _entity_poly.pdbx_seq_one_letter_code_can ;QAVQPVDFRHHHFSDMEIFLRRYANEYPSITRLYSVGKSVELRELYVMEISDNPGIHEAGEPEFKYIGNMHGNEVVGREL LLNLIEYLCKNFGTDPEVTDLVQSTRIHIMPSMNPDGYEKSQEGDRGGTVGRNNSNNYDLNRNFPDQFFQVTDPPQPETL AVMSWLKTYPFVLSANLHGGSLVVNYPFDDDEQGIAIYSKSPDDAVFQQLALSYSKENKKMYQGSPCKDLYPTEYFPHGI TNGAQWYNVPGGMQDWNYLNTNCFEVTIELGCVKYPKAEELPKYWEQNRRSLLQFIKQVHRGIWGFVLDATDGRGILNAT ISVADINHPVTTYKDGDYWRLLVQGTYKVTASARGYDPVTKTVEVDSKGGVQVNFTLSRT ; _entity_poly.pdbx_strand_id A _entity_poly.pdbx_target_identifier ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 GLN n 1 2 ALA n 1 3 VAL n 1 4 GLN n 1 5 PRO n 1 6 VAL n 1 7 ASP n 1 8 PHE n 1 9 ARG n 1 10 HIS n 1 11 HIS n 1 12 HIS n 1 13 PHE n 1 14 SER n 1 15 ASP n 1 16 MET n 1 17 GLU n 1 18 ILE n 1 19 PHE n 1 20 LEU n 1 21 ARG n 1 22 ARG n 1 23 TYR n 1 24 ALA n 1 25 ASN n 1 26 GLU n 1 27 TYR n 1 28 PRO n 1 29 SER n 1 30 ILE n 1 31 THR n 1 32 ARG n 1 33 LEU n 1 34 TYR n 1 35 SER n 1 36 VAL n 1 37 GLY n 1 38 LYS n 1 39 SER n 1 40 VAL n 1 41 GLU n 1 42 LEU n 1 43 ARG n 1 44 GLU n 1 45 LEU n 1 46 TYR n 1 47 VAL n 1 48 MET n 1 49 GLU n 1 50 ILE n 1 51 SER n 1 52 ASP n 1 53 ASN n 1 54 PRO n 1 55 GLY n 1 56 ILE n 1 57 HIS n 1 58 GLU n 1 59 ALA n 1 60 GLY n 1 61 GLU n 1 62 PRO n 1 63 GLU n 1 64 PHE n 1 65 LYS n 1 66 TYR n 1 67 ILE n 1 68 GLY n 1 69 ASN n 1 70 MET n 1 71 HIS n 1 72 GLY n 1 73 ASN n 1 74 GLU n 1 75 VAL n 1 76 VAL n 1 77 GLY n 1 78 ARG n 1 79 GLU n 1 80 LEU n 1 81 LEU n 1 82 LEU n 1 83 ASN n 1 84 LEU n 1 85 ILE n 1 86 GLU n 1 87 TYR n 1 88 LEU n 1 89 CYS n 1 90 LYS n 1 91 ASN n 1 92 PHE n 1 93 GLY n 1 94 THR n 1 95 ASP n 1 96 PRO n 1 97 GLU n 1 98 VAL n 1 99 THR n 1 100 ASP n 1 101 LEU n 1 102 VAL n 1 103 GLN n 1 104 SER n 1 105 THR n 1 106 ARG n 1 107 ILE n 1 108 HIS n 1 109 ILE n 1 110 MET n 1 111 PRO n 1 112 SER n 1 113 MET n 1 114 ASN n 1 115 PRO n 1 116 ASP n 1 117 GLY n 1 118 TYR n 1 119 GLU n 1 120 LYS n 1 121 SER n 1 122 GLN n 1 123 GLU n 1 124 GLY n 1 125 ASP n 1 126 ARG n 1 127 GLY n 1 128 GLY n 1 129 THR n 1 130 VAL n 1 131 GLY n 1 132 ARG n 1 133 ASN n 1 134 ASN n 1 135 SER n 1 136 ASN n 1 137 ASN n 1 138 TYR n 1 139 ASP n 1 140 LEU n 1 141 ASN n 1 142 ARG n 1 143 ASN n 1 144 PHE n 1 145 PRO n 1 146 ASP n 1 147 GLN n 1 148 PHE n 1 149 PHE n 1 150 GLN n 1 151 VAL n 1 152 THR n 1 153 ASP n 1 154 PRO n 1 155 PRO n 1 156 GLN n 1 157 PRO n 1 158 GLU n 1 159 THR n 1 160 LEU n 1 161 ALA n 1 162 VAL n 1 163 MET n 1 164 SER n 1 165 TRP n 1 166 LEU n 1 167 LYS n 1 168 THR n 1 169 TYR n 1 170 PRO n 1 171 PHE n 1 172 VAL n 1 173 LEU n 1 174 SER n 1 175 ALA n 1 176 ASN n 1 177 LEU n 1 178 HIS n 1 179 GLY n 1 180 GLY n 1 181 SER n 1 182 LEU n 1 183 VAL n 1 184 VAL n 1 185 ASN n 1 186 TYR n 1 187 PRO n 1 188 PHE n 1 189 ASP n 1 190 ASP n 1 191 ASP n 1 192 GLU n 1 193 GLN n 1 194 GLY n 1 195 ILE n 1 196 ALA n 1 197 ILE n 1 198 TYR n 1 199 SER n 1 200 LYS n 1 201 SER n 1 202 PRO n 1 203 ASP n 1 204 ASP n 1 205 ALA n 1 206 VAL n 1 207 PHE n 1 208 GLN n 1 209 GLN n 1 210 LEU n 1 211 ALA n 1 212 LEU n 1 213 SER n 1 214 TYR n 1 215 SER n 1 216 LYS n 1 217 GLU n 1 218 ASN n 1 219 LYS n 1 220 LYS n 1 221 MET n 1 222 TYR n 1 223 GLN n 1 224 GLY n 1 225 SER n 1 226 PRO n 1 227 CYS n 1 228 LYS n 1 229 ASP n 1 230 LEU n 1 231 TYR n 1 232 PRO n 1 233 THR n 1 234 GLU n 1 235 TYR n 1 236 PHE n 1 237 PRO n 1 238 HIS n 1 239 GLY n 1 240 ILE n 1 241 THR n 1 242 ASN n 1 243 GLY n 1 244 ALA n 1 245 GLN n 1 246 TRP n 1 247 TYR n 1 248 ASN n 1 249 VAL n 1 250 PRO n 1 251 GLY n 1 252 GLY n 1 253 MET n 1 254 GLN n 1 255 ASP n 1 256 TRP n 1 257 ASN n 1 258 TYR n 1 259 LEU n 1 260 ASN n 1 261 THR n 1 262 ASN n 1 263 CYS n 1 264 PHE n 1 265 GLU n 1 266 VAL n 1 267 THR n 1 268 ILE n 1 269 GLU n 1 270 LEU n 1 271 GLY n 1 272 CYS n 1 273 VAL n 1 274 LYS n 1 275 TYR n 1 276 PRO n 1 277 LYS n 1 278 ALA n 1 279 GLU n 1 280 GLU n 1 281 LEU n 1 282 PRO n 1 283 LYS n 1 284 TYR n 1 285 TRP n 1 286 GLU n 1 287 GLN n 1 288 ASN n 1 289 ARG n 1 290 ARG n 1 291 SER n 1 292 LEU n 1 293 LEU n 1 294 GLN n 1 295 PHE n 1 296 ILE n 1 297 LYS n 1 298 GLN n 1 299 VAL n 1 300 HIS n 1 301 ARG n 1 302 GLY n 1 303 ILE n 1 304 TRP n 1 305 GLY n 1 306 PHE n 1 307 VAL n 1 308 LEU n 1 309 ASP n 1 310 ALA n 1 311 THR n 1 312 ASP n 1 313 GLY n 1 314 ARG n 1 315 GLY n 1 316 ILE n 1 317 LEU n 1 318 ASN n 1 319 ALA n 1 320 THR n 1 321 ILE n 1 322 SER n 1 323 VAL n 1 324 ALA n 1 325 ASP n 1 326 ILE n 1 327 ASN n 1 328 HIS n 1 329 PRO n 1 330 VAL n 1 331 THR n 1 332 THR n 1 333 TYR n 1 334 LYS n 1 335 ASP n 1 336 GLY n 1 337 ASP n 1 338 TYR n 1 339 TRP n 1 340 ARG n 1 341 LEU n 1 342 LEU n 1 343 VAL n 1 344 GLN n 1 345 GLY n 1 346 THR n 1 347 TYR n 1 348 LYS n 1 349 VAL n 1 350 THR n 1 351 ALA n 1 352 SER n 1 353 ALA n 1 354 ARG n 1 355 GLY n 1 356 TYR n 1 357 ASP n 1 358 PRO n 1 359 VAL n 1 360 THR n 1 361 LYS n 1 362 THR n 1 363 VAL n 1 364 GLU n 1 365 VAL n 1 366 ASP n 1 367 SER n 1 368 LYS n 1 369 GLY n 1 370 GLY n 1 371 VAL n 1 372 GLN n 1 373 VAL n 1 374 ASN n 1 375 PHE n 1 376 THR n 1 377 LEU n 1 378 SER n 1 379 ARG n 1 380 THR 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 'CRESTED DUCK' _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene ? _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain ? _entity_src_gen.gene_src_tissue ? _entity_src_gen.gene_src_tissue_fraction ? _entity_src_gen.gene_src_details ? _entity_src_gen.pdbx_gene_src_fragment ? _entity_src_gen.pdbx_gene_src_scientific_name 'LOPHONETTA SPECULARIOIDES' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 8836 _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 ? _entity_src_gen.pdbx_gene_src_cellular_location ? _entity_src_gen.host_org_common_name ? _entity_src_gen.pdbx_host_org_scientific_name 'PICHIA PASTORIS' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 4922 _entity_src_gen.host_org_genus ? _entity_src_gen.pdbx_host_org_gene ? _entity_src_gen.pdbx_host_org_organ ? _entity_src_gen.host_org_species ? _entity_src_gen.pdbx_host_org_tissue ? _entity_src_gen.pdbx_host_org_tissue_fraction ? _entity_src_gen.pdbx_host_org_strain KM71 _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line ? _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type ? _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name ? _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description 'OBTAINED AFTER CLONING INTO AND OVEREXPRESSION FROM A PICHIA PASTORIS SYSTEM.' # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code Q90240 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ? _struct_ref.pdbx_align_begin ? _struct_ref.pdbx_db_accession Q90240 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 1QMU _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 1 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 380 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession Q90240 _struct_ref_seq.db_align_beg 503 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 882 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 4 _struct_ref_seq.pdbx_auth_seq_align_end 383 # 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 MAN D-saccharide . ALPHA-D-MANNOSE ? 'C6 H12 O6' 180.156 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 SO4 non-polymer . 'SULFATE ION' ? 'O4 S -2' 96.063 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 ZN non-polymer . 'ZINC ION' ? 'Zn 2' 65.409 # _exptl.entry_id 1QMU _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number ? # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 4.6 _exptl_crystal.density_percent_sol 73 _exptl_crystal.description ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method ? _exptl_crystal_grow.temp ? _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 5.20 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details 'pH 5.20' # _diffrn.id 1 _diffrn.ambient_temp 110.0 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector 'IMAGE PLATE' _diffrn_detector.type MARRESEARCH _diffrn_detector.pdbx_collection_date ? _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.8467 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'EMBL/DESY, HAMBURG BEAMLINE X11' _diffrn_source.pdbx_synchrotron_site 'EMBL/DESY, Hamburg' _diffrn_source.pdbx_synchrotron_beamline X11 _diffrn_source.pdbx_wavelength 0.8467 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 1QMU _reflns.observed_criterion_sigma_I ? _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 20.000 _reflns.d_resolution_high 2.700 _reflns.number_obs 22564 _reflns.number_all ? _reflns.percent_possible_obs 98.0 _reflns.pdbx_Rmerge_I_obs 0.07600 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 8.3000 _reflns.B_iso_Wilson_estimate 83.1 _reflns.pdbx_redundancy 12.000 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 2.70 _reflns_shell.d_res_low 2.85 _reflns_shell.percent_possible_all 87.0 _reflns_shell.Rmerge_I_obs 0.60800 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 1.200 _reflns_shell.pdbx_redundancy 6.00 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 1QMU _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 22539 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 0.0 _refine.pdbx_data_cutoff_high_absF 100000 _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 20.0 _refine.ls_d_res_high 2.70 _refine.ls_percent_reflns_obs 98.1 _refine.ls_R_factor_obs 0.198 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.198 _refine.ls_R_factor_R_free 0.236 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 7.0 _refine.ls_number_reflns_R_free ? _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.B_iso_mean ? _refine.aniso_B[1][1] ? _refine.aniso_B[2][2] ? _refine.aniso_B[3][3] ? _refine.aniso_B[1][2] ? _refine.aniso_B[1][3] ? _refine.aniso_B[2][3] ? _refine.solvent_model_details ? _refine.solvent_model_param_ksol 0.298 _refine.solvent_model_param_bsol 31.47 _refine.pdbx_solvent_vdw_probe_radii ? _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii ? _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details ? _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct SIRAS _refine.pdbx_isotropic_thermal_model ? _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_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 3057 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 122 _refine_hist.number_atoms_solvent 121 _refine_hist.number_atoms_total 3300 _refine_hist.d_res_high 2.70 _refine_hist.d_res_low 20.0 # 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 0.011 ? ? ? '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 1.59 ? ? ? 'X-RAY DIFFRACTION' ? c_angle_deg_na ? ? ? ? 'X-RAY DIFFRACTION' ? c_angle_deg_prot ? ? ? ? 'X-RAY DIFFRACTION' ? c_dihedral_angle_d ? ? ? ? 'X-RAY DIFFRACTION' ? c_dihedral_angle_d_na ? ? ? ? 'X-RAY DIFFRACTION' ? c_dihedral_angle_d_prot ? ? ? ? 'X-RAY DIFFRACTION' ? c_improper_angle_d ? ? ? ? 'X-RAY DIFFRACTION' ? c_improper_angle_d_na ? ? ? ? 'X-RAY DIFFRACTION' ? c_improper_angle_d_prot ? ? ? ? 'X-RAY DIFFRACTION' ? c_mcbond_it ? ? ? ? 'X-RAY DIFFRACTION' ? c_mcangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? c_scbond_it ? ? ? ? 'X-RAY DIFFRACTION' ? c_scangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? # _struct.entry_id 1QMU _struct.title 'Duck carboxypeptidase D domain II' _struct.pdbx_descriptor 'CARBOXYPEPTIDASE GP180 RESIDUES 503-882' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 1QMU _struct_keywords.pdbx_keywords CARBOXYPEPTIDASE _struct_keywords.text 'CARBOXYPEPTIDASE, HYDROLASE, ZINC-DEPENDENT PROTEASE' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 2 ? D N N 3 ? E N N 2 ? F N N 2 ? G N N 2 ? H N N 2 ? I N N 3 ? J N N 4 ? K N N 4 ? L N N 4 ? M N N 5 ? N N N 6 ? # _struct_biol.id 1 # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 HIS A 12 ? TYR A 27 ? HIS A 15 TYR A 30 1 ? 16 HELX_P HELX_P2 2 VAL A 75 ? PHE A 92 ? VAL A 78 PHE A 95 1 ? 18 HELX_P HELX_P3 3 ASP A 95 ? THR A 105 ? ASP A 98 THR A 108 1 ? 11 HELX_P HELX_P4 4 ASN A 114 ? LYS A 120 ? ASN A 117 LYS A 123 1 ? 7 HELX_P HELX_P5 5 GLN A 156 ? TYR A 169 ? GLN A 159 TYR A 172 1 ? 14 HELX_P HELX_P6 6 ASP A 203 ? LYS A 216 ? ASP A 206 LYS A 219 1 ? 14 HELX_P HELX_P7 7 ASN A 218 ? GLN A 223 ? ASN A 221 GLN A 226 1 ? 6 HELX_P HELX_P8 8 PHE A 236 ? HIS A 238 ? PHE A 239 HIS A 241 5 ? 3 HELX_P HELX_P9 9 GLY A 243 ? TYR A 247 ? GLY A 246 TYR A 250 1 ? 5 HELX_P HELX_P10 10 GLY A 252 ? THR A 261 ? GLY A 255 THR A 264 1 ? 10 HELX_P HELX_P11 11 GLU A 280 ? GLN A 298 ? GLU A 283 GLN A 301 1 ? 19 HELX_P HELX_P12 12 VAL A 299 ? ARG A 301 ? VAL A 302 ARG A 304 5 ? 3 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 227 SG ? ? ? 1_555 A CYS 272 SG ? ? A CYS 230 A CYS 275 1_555 ? ? ? ? ? ? ? 2.035 ? covale1 covale ? ? A ASN 133 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 136 A NAG 901 1_555 ? ? ? ? ? ? ? 1.445 ? covale2 covale ? ? A ASN 318 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 321 A NAG 911 1_555 ? ? ? ? ? ? ? 1.440 ? covale3 covale ? ? A ASN 374 ND2 ? ? ? 1_555 G NAG . C1 ? ? A ASN 377 A NAG 921 1_555 ? ? ? ? ? ? ? 1.448 ? covale4 covale ? ? B NAG . O4 ? ? ? 1_555 C NAG . C1 ? ? A NAG 901 A NAG 902 1_555 ? ? ? ? ? ? ? 1.376 ? covale5 covale ? ? C NAG . O4 ? ? ? 1_555 D MAN . C1 ? ? A NAG 902 A MAN 903 1_555 ? ? ? ? ? ? ? 1.385 ? covale6 covale ? ? E NAG . O4 ? ? ? 1_555 F NAG . C1 ? ? A NAG 911 A NAG 912 1_555 ? ? ? ? ? ? ? 1.399 ? covale7 covale ? ? G NAG . O4 ? ? ? 1_555 H NAG . C1 ? ? A NAG 921 A NAG 922 1_555 ? ? ? ? ? ? ? 1.395 ? covale8 covale ? ? H NAG . O4 ? ? ? 1_555 I MAN . C1 ? ? A NAG 922 A MAN 923 1_555 ? ? ? ? ? ? ? 1.406 ? metalc1 metalc ? ? M ZN . ZN ? ? ? 1_555 A HIS 178 ND1 ? ? A ZN 999 A HIS 181 1_555 ? ? ? ? ? ? ? 2.073 ? metalc2 metalc ? ? M ZN . ZN ? ? ? 1_555 A GLU 74 OE1 ? ? A ZN 999 A GLU 77 1_555 ? ? ? ? ? ? ? 2.231 ? metalc3 metalc ? ? M ZN . ZN ? ? ? 1_555 A GLU 74 OE2 ? ? A ZN 999 A GLU 77 1_555 ? ? ? ? ? ? ? 2.338 ? metalc4 metalc ? ? M ZN . ZN ? ? ? 1_555 N HOH . O ? ? A ZN 999 A HOH 2121 1_555 ? ? ? ? ? ? ? 2.678 ? metalc5 metalc ? ? M ZN . ZN ? ? ? 1_555 A HIS 71 ND1 ? ? A ZN 999 A HIS 74 1_555 ? ? ? ? ? ? ? 2.007 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? metalc ? ? # _struct_mon_prot_cis.pdbx_id 1 _struct_mon_prot_cis.label_comp_id PRO _struct_mon_prot_cis.label_seq_id 187 _struct_mon_prot_cis.label_asym_id A _struct_mon_prot_cis.label_alt_id . _struct_mon_prot_cis.pdbx_PDB_ins_code ? _struct_mon_prot_cis.auth_comp_id PRO _struct_mon_prot_cis.auth_seq_id 190 _struct_mon_prot_cis.auth_asym_id A _struct_mon_prot_cis.pdbx_label_comp_id_2 PHE _struct_mon_prot_cis.pdbx_label_seq_id_2 188 _struct_mon_prot_cis.pdbx_label_asym_id_2 A _struct_mon_prot_cis.pdbx_PDB_ins_code_2 ? _struct_mon_prot_cis.pdbx_auth_comp_id_2 PHE _struct_mon_prot_cis.pdbx_auth_seq_id_2 191 _struct_mon_prot_cis.pdbx_auth_asym_id_2 A _struct_mon_prot_cis.pdbx_PDB_model_num 1 _struct_mon_prot_cis.pdbx_omega_angle 2.94 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 8 ? B ? 3 ? C ? 2 ? D ? 3 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? anti-parallel A 2 3 ? anti-parallel A 3 4 ? parallel A 4 5 ? parallel A 5 6 ? parallel A 6 7 ? anti-parallel A 7 8 ? parallel B 1 2 ? parallel B 2 3 ? anti-parallel C 1 2 ? parallel D 1 2 ? anti-parallel D 2 3 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 THR A 31 ? SER A 35 ? THR A 34 SER A 38 A 2 TYR A 46 ? ILE A 50 ? TYR A 49 ILE A 53 A 3 THR A 105 ? MET A 110 ? THR A 108 MET A 113 A 4 PRO A 62 ? ILE A 67 ? PRO A 65 ILE A 70 A 5 PHE A 171 ? HIS A 178 ? PHE A 174 HIS A 181 A 6 PHE A 264 ? GLY A 271 ? PHE A 267 GLY A 274 A 7 SER A 181 ? TYR A 186 ? SER A 184 TYR A 189 A 8 ILE A 240 ? ASN A 242 ? ILE A 243 ASN A 245 B 1 GLY A 370 ? GLN A 372 ? GLY A 373 GLN A 375 B 2 GLY A 302 ? PHE A 306 ? GLY A 305 PHE A 309 B 3 ASP A 337 ? ARG A 340 ? ASP A 340 ARG A 343 C 1 VAL A 307 ? ASP A 309 ? VAL A 310 ASP A 312 C 2 PHE A 375 ? LEU A 377 ? PHE A 378 LEU A 380 D 1 THR A 320 ? SER A 322 ? THR A 323 SER A 325 D 2 GLY A 345 ? SER A 352 ? GLY A 348 SER A 355 D 3 VAL A 359 ? VAL A 365 ? VAL A 362 VAL A 368 # 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 ARG A 32 ? O ARG A 35 N GLU A 49 ? N GLU A 52 A 2 3 O MET A 48 ? O MET A 51 N ILE A 109 ? N ILE A 112 A 3 4 O ARG A 106 ? O ARG A 109 N PRO A 62 ? N PRO A 65 A 4 5 O GLU A 63 ? O GLU A 66 N VAL A 172 ? N VAL A 175 A 5 6 O SER A 174 ? O SER A 177 N PHE A 264 ? N PHE A 267 A 6 7 O THR A 267 ? O THR A 270 N ASN A 185 ? N ASN A 188 A 7 8 O VAL A 184 ? O VAL A 187 N THR A 241 ? N THR A 244 B 1 2 O VAL A 371 ? O VAL A 374 N GLY A 302 ? N GLY A 305 B 2 3 O ILE A 303 ? O ILE A 306 N ARG A 340 ? N ARG A 343 C 1 2 O LEU A 308 ? O LEU A 311 N PHE A 375 ? N PHE A 378 D 1 2 O THR A 320 ? O THR A 323 N SER A 352 ? N SER A 355 D 2 3 O GLY A 345 ? O GLY A 348 N VAL A 365 ? N VAL A 368 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE NAG A 901' AC2 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 902' AC3 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE MAN A 903' AC4 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 911' AC5 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG A 912' AC6 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 921' AC7 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 922' AC8 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE MAN A 923' AC9 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE SO4 A 996' BC1 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE SO4 A 997' BC2 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE SO4 A 998' BC3 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ZN A 999' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 8 THR A 129 ? THR A 132 . ? 1_555 ? 2 AC1 8 ASN A 133 ? ASN A 136 . ? 1_555 ? 3 AC1 8 ASN A 137 ? ASN A 140 . ? 1_555 ? 4 AC1 8 TYR A 138 ? TYR A 141 . ? 1_555 ? 5 AC1 8 ASP A 139 ? ASP A 142 . ? 1_555 ? 6 AC1 8 ASP A 153 ? ASP A 156 . ? 1_555 ? 7 AC1 8 ASP A 325 ? ASP A 328 . ? 1_555 ? 8 AC1 8 NAG C . ? NAG A 902 . ? 1_555 ? 9 AC2 2 NAG B . ? NAG A 901 . ? 1_555 ? 10 AC2 2 MAN D . ? MAN A 903 . ? 1_555 ? 11 AC3 2 NAG C . ? NAG A 902 . ? 1_555 ? 12 AC3 2 HOH N . ? HOH A 2112 . ? 1_555 ? 13 AC4 3 ASN A 318 ? ASN A 321 . ? 1_555 ? 14 AC4 3 NAG F . ? NAG A 912 . ? 1_555 ? 15 AC4 3 HOH N . ? HOH A 2092 . ? 1_555 ? 16 AC5 1 NAG E . ? NAG A 911 . ? 1_555 ? 17 AC6 5 PHE A 306 ? PHE A 309 . ? 1_555 ? 18 AC6 5 LEU A 308 ? LEU A 311 . ? 1_555 ? 19 AC6 5 GLN A 372 ? GLN A 375 . ? 1_555 ? 20 AC6 5 ASN A 374 ? ASN A 377 . ? 1_555 ? 21 AC6 5 NAG H . ? NAG A 922 . ? 1_555 ? 22 AC7 2 NAG G . ? NAG A 921 . ? 1_555 ? 23 AC7 2 MAN I . ? MAN A 923 . ? 1_555 ? 24 AC8 2 NAG H . ? NAG A 922 . ? 1_555 ? 25 AC8 2 HOH N . ? HOH A 2116 . ? 1_555 ? 26 AC9 3 LYS A 220 ? LYS A 223 . ? 1_555 ? 27 AC9 3 LYS A 228 ? LYS A 231 . ? 1_555 ? 28 AC9 3 HOH N . ? HOH A 2120 . ? 1_555 ? 29 BC1 2 ARG A 289 ? ARG A 292 . ? 1_555 ? 30 BC1 2 ARG A 290 ? ARG A 293 . ? 1_555 ? 31 BC2 8 HIS A 71 ? HIS A 74 . ? 1_555 ? 32 BC2 8 ARG A 132 ? ARG A 135 . ? 1_555 ? 33 BC2 8 ASN A 141 ? ASN A 144 . ? 1_555 ? 34 BC2 8 ARG A 142 ? ARG A 145 . ? 1_555 ? 35 BC2 8 TYR A 247 ? TYR A 250 . ? 1_555 ? 36 BC2 8 VAL A 249 ? VAL A 252 . ? 1_555 ? 37 BC2 8 ZN M . ? ZN A 999 . ? 1_555 ? 38 BC2 8 HOH N . ? HOH A 2121 . ? 1_555 ? 39 BC3 5 HIS A 71 ? HIS A 74 . ? 1_555 ? 40 BC3 5 GLU A 74 ? GLU A 77 . ? 1_555 ? 41 BC3 5 HIS A 178 ? HIS A 181 . ? 1_555 ? 42 BC3 5 SO4 L . ? SO4 A 998 . ? 1_555 ? 43 BC3 5 HOH N . ? HOH A 2121 . ? 1_555 ? # _database_PDB_matrix.entry_id 1QMU _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 1QMU _atom_sites.fract_transf_matrix[1][1] 0.007378 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.007378 _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] 0.007378 _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 ZN # 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 . GLN A 1 1 ? 23.365 64.284 25.202 1.00 73.50 ? 4 GLN A N 1 ATOM 2 C CA . GLN A 1 1 ? 22.849 65.419 24.384 1.00 75.30 ? 4 GLN A CA 1 ATOM 3 C C . GLN A 1 1 ? 21.417 65.176 23.861 1.00 74.48 ? 4 GLN A C 1 ATOM 4 O O . GLN A 1 1 ? 20.542 66.023 24.059 1.00 75.94 ? 4 GLN A O 1 ATOM 5 C CB . GLN A 1 1 ? 23.806 65.701 23.207 1.00 78.74 ? 4 GLN A CB 1 ATOM 6 C CG . GLN A 1 1 ? 23.512 66.988 22.386 1.00 82.65 ? 4 GLN A CG 1 ATOM 7 C CD . GLN A 1 1 ? 24.054 68.283 23.017 1.00 85.48 ? 4 GLN A CD 1 ATOM 8 O OE1 . GLN A 1 1 ? 23.614 68.703 24.096 1.00 85.90 ? 4 GLN A OE1 1 ATOM 9 N NE2 . GLN A 1 1 ? 25.009 68.922 22.333 1.00 85.56 ? 4 GLN A NE2 1 ATOM 10 N N . ALA A 1 2 ? 21.166 64.038 23.205 1.00 71.62 ? 5 ALA A N 1 ATOM 11 C CA . ALA A 1 2 ? 19.824 63.744 22.679 1.00 68.24 ? 5 ALA A CA 1 ATOM 12 C C . ALA A 1 2 ? 18.784 63.645 23.785 1.00 66.92 ? 5 ALA A C 1 ATOM 13 O O . ALA A 1 2 ? 19.074 63.201 24.894 1.00 66.26 ? 5 ALA A O 1 ATOM 14 C CB . ALA A 1 2 ? 19.831 62.457 21.881 1.00 67.16 ? 5 ALA A CB 1 ATOM 15 N N . VAL A 1 3 ? 17.562 64.039 23.458 1.00 65.17 ? 6 VAL A N 1 ATOM 16 C CA . VAL A 1 3 ? 16.458 64.034 24.412 1.00 65.65 ? 6 VAL A CA 1 ATOM 17 C C . VAL A 1 3 ? 15.803 62.677 24.630 1.00 64.04 ? 6 VAL A C 1 ATOM 18 O O . VAL A 1 3 ? 15.282 62.078 23.693 1.00 64.00 ? 6 VAL A O 1 ATOM 19 C CB . VAL A 1 3 ? 15.347 64.985 23.959 1.00 67.84 ? 6 VAL A CB 1 ATOM 20 C CG1 . VAL A 1 3 ? 14.203 64.939 24.957 1.00 68.34 ? 6 VAL A CG1 1 ATOM 21 C CG2 . VAL A 1 3 ? 15.890 66.398 23.810 1.00 68.52 ? 6 VAL A CG2 1 ATOM 22 N N . GLN A 1 4 ? 15.786 62.210 25.872 1.00 61.83 ? 7 GLN A N 1 ATOM 23 C CA . GLN A 1 4 ? 15.176 60.925 26.153 1.00 61.62 ? 7 GLN A CA 1 ATOM 24 C C . GLN A 1 4 ? 13.687 61.048 26.387 1.00 62.24 ? 7 GLN A C 1 ATOM 25 O O . GLN A 1 4 ? 13.175 62.125 26.680 1.00 63.37 ? 7 GLN A O 1 ATOM 26 C CB . GLN A 1 4 ? 15.817 60.283 27.376 1.00 61.70 ? 7 GLN A CB 1 ATOM 27 C CG . GLN A 1 4 ? 17.267 59.877 27.185 1.00 63.88 ? 7 GLN A CG 1 ATOM 28 C CD . GLN A 1 4 ? 17.452 59.011 25.971 1.00 65.00 ? 7 GLN A CD 1 ATOM 29 O OE1 . GLN A 1 4 ? 16.642 58.122 25.710 1.00 67.26 ? 7 GLN A OE1 1 ATOM 30 N NE2 . GLN A 1 4 ? 18.518 59.257 25.216 1.00 64.49 ? 7 GLN A NE2 1 ATOM 31 N N . PRO A 1 5 ? 12.962 59.934 26.248 1.00 62.96 ? 8 PRO A N 1 ATOM 32 C CA . PRO A 1 5 ? 11.514 59.954 26.459 1.00 64.15 ? 8 PRO A CA 1 ATOM 33 C C . PRO A 1 5 ? 11.205 60.216 27.925 1.00 66.31 ? 8 PRO A C 1 ATOM 34 O O . PRO A 1 5 ? 12.095 60.183 28.779 1.00 65.99 ? 8 PRO A O 1 ATOM 35 C CB . PRO A 1 5 ? 11.078 58.557 26.025 1.00 62.70 ? 8 PRO A CB 1 ATOM 36 C CG . PRO A 1 5 ? 12.107 58.173 25.011 1.00 62.47 ? 8 PRO A CG 1 ATOM 37 C CD . PRO A 1 5 ? 13.388 58.655 25.657 1.00 62.75 ? 8 PRO A CD 1 ATOM 38 N N . VAL A 1 6 ? 9.931 60.455 28.211 1.00 69.02 ? 9 VAL A N 1 ATOM 39 C CA . VAL A 1 6 ? 9.484 60.742 29.570 1.00 70.20 ? 9 VAL A CA 1 ATOM 40 C C . VAL A 1 6 ? 8.184 60.012 29.913 1.00 72.20 ? 9 VAL A C 1 ATOM 41 O O . VAL A 1 6 ? 7.981 59.601 31.061 1.00 70.03 ? 9 VAL A O 1 ATOM 42 C CB . VAL A 1 6 ? 9.274 62.238 29.719 1.00 69.51 ? 9 VAL A CB 1 ATOM 43 C CG1 . VAL A 1 6 ? 10.593 62.937 29.490 1.00 70.79 ? 9 VAL A CG1 1 ATOM 44 C CG2 . VAL A 1 6 ? 8.246 62.731 28.688 1.00 68.18 ? 9 VAL A CG2 1 ATOM 45 N N . ASP A 1 7 ? 7.319 59.859 28.900 1.00 74.75 ? 10 ASP A N 1 ATOM 46 C CA . ASP A 1 7 ? 6.021 59.180 29.035 1.00 76.42 ? 10 ASP A CA 1 ATOM 47 C C . ASP A 1 7 ? 6.269 57.673 29.267 1.00 75.80 ? 10 ASP A C 1 ATOM 48 O O . ASP A 1 7 ? 6.013 56.854 28.366 1.00 77.43 ? 10 ASP A O 1 ATOM 49 C CB . ASP A 1 7 ? 5.160 59.402 27.747 1.00 77.73 ? 10 ASP A CB 1 ATOM 50 C CG . ASP A 1 7 ? 3.610 59.362 28.013 1.00 80.15 ? 10 ASP A CG 1 ATOM 51 O OD1 . ASP A 1 7 ? 3.184 59.231 29.187 1.00 82.74 ? 10 ASP A OD1 1 ATOM 52 O OD2 . ASP A 1 7 ? 2.807 59.474 27.047 1.00 76.94 ? 10 ASP A OD2 1 ATOM 53 N N . PHE A 1 8 ? 6.780 57.318 30.458 1.00 73.02 ? 11 PHE A N 1 ATOM 54 C CA . PHE A 1 8 ? 7.052 55.911 30.810 1.00 70.53 ? 11 PHE A CA 1 ATOM 55 C C . PHE A 1 8 ? 5.904 55.281 31.592 1.00 69.32 ? 11 PHE A C 1 ATOM 56 O O . PHE A 1 8 ? 5.889 55.314 32.817 1.00 70.46 ? 11 PHE A O 1 ATOM 57 C CB . PHE A 1 8 ? 8.335 55.769 31.648 1.00 67.36 ? 11 PHE A CB 1 ATOM 58 C CG . PHE A 1 8 ? 9.604 55.859 30.853 1.00 67.26 ? 11 PHE A CG 1 ATOM 59 C CD1 . PHE A 1 8 ? 9.780 55.095 29.704 1.00 67.97 ? 11 PHE A CD1 1 ATOM 60 C CD2 . PHE A 1 8 ? 10.627 56.722 31.243 1.00 66.95 ? 11 PHE A CD2 1 ATOM 61 C CE1 . PHE A 1 8 ? 10.958 55.193 28.953 1.00 67.23 ? 11 PHE A CE1 1 ATOM 62 C CE2 . PHE A 1 8 ? 11.806 56.827 30.500 1.00 66.73 ? 11 PHE A CE2 1 ATOM 63 C CZ . PHE A 1 8 ? 11.970 56.065 29.358 1.00 66.30 ? 11 PHE A CZ 1 ATOM 64 N N . ARG A 1 9 ? 4.942 54.705 30.891 1.00 67.14 ? 12 ARG A N 1 ATOM 65 C CA . ARG A 1 9 ? 3.839 54.073 31.575 1.00 67.20 ? 12 ARG A CA 1 ATOM 66 C C . ARG A 1 9 ? 3.148 53.139 30.629 1.00 66.25 ? 12 ARG A C 1 ATOM 67 O O . ARG A 1 9 ? 3.375 53.184 29.430 1.00 67.46 ? 12 ARG A O 1 ATOM 68 C CB . ARG A 1 9 ? 2.853 55.116 32.082 1.00 70.48 ? 12 ARG A CB 1 ATOM 69 C CG . ARG A 1 9 ? 2.147 55.917 31.003 1.00 74.64 ? 12 ARG A CG 1 ATOM 70 C CD . ARG A 1 9 ? 1.659 57.256 31.577 1.00 79.52 ? 12 ARG A CD 1 ATOM 71 N NE . ARG A 1 9 ? 0.926 58.051 30.598 1.00 84.78 ? 12 ARG A NE 1 ATOM 72 C CZ . ARG A 1 9 ? -0.327 57.802 30.222 1.00 88.71 ? 12 ARG A CZ 1 ATOM 73 N NH1 . ARG A 1 9 ? -0.987 56.775 30.756 1.00 89.53 ? 12 ARG A NH1 1 ATOM 74 N NH2 . ARG A 1 9 ? -0.918 58.567 29.304 1.00 89.76 ? 12 ARG A NH2 1 ATOM 75 N N . HIS A 1 10 ? 2.317 52.270 31.174 1.00 64.85 ? 13 HIS A N 1 ATOM 76 C CA . HIS A 1 10 ? 1.587 51.341 30.346 1.00 64.16 ? 13 HIS A CA 1 ATOM 77 C C . HIS A 1 10 ? 0.518 52.148 29.637 1.00 64.30 ? 13 HIS A C 1 ATOM 78 O O . HIS A 1 10 ? -0.183 52.927 30.277 1.00 66.17 ? 13 HIS A O 1 ATOM 79 C CB . HIS A 1 10 ? 0.951 50.268 31.215 1.00 63.31 ? 13 HIS A CB 1 ATOM 80 C CG . HIS A 1 10 ? 1.931 49.279 31.766 1.00 61.90 ? 13 HIS A CG 1 ATOM 81 N ND1 . HIS A 1 10 ? 2.720 48.488 30.959 1.00 61.29 ? 13 HIS A ND1 1 ATOM 82 C CD2 . HIS A 1 10 ? 2.215 48.916 33.038 1.00 62.97 ? 13 HIS A CD2 1 ATOM 83 C CE1 . HIS A 1 10 ? 3.443 47.678 31.710 1.00 60.87 ? 13 HIS A CE1 1 ATOM 84 N NE2 . HIS A 1 10 ? 3.155 47.916 32.976 1.00 61.35 ? 13 HIS A NE2 1 ATOM 85 N N . HIS A 1 11 ? 0.411 51.986 28.321 1.00 63.00 ? 14 HIS A N 1 ATOM 86 C CA . HIS A 1 11 ? -0.595 52.712 27.558 1.00 60.92 ? 14 HIS A CA 1 ATOM 87 C C . HIS A 1 11 ? -1.687 51.802 27.017 1.00 61.39 ? 14 HIS A C 1 ATOM 88 O O . HIS A 1 11 ? -1.438 50.977 26.127 1.00 61.06 ? 14 HIS A O 1 ATOM 89 C CB . HIS A 1 11 ? 0.026 53.444 26.371 1.00 59.36 ? 14 HIS A CB 1 ATOM 90 C CG . HIS A 1 11 ? 0.986 54.525 26.753 1.00 58.51 ? 14 HIS A CG 1 ATOM 91 N ND1 . HIS A 1 11 ? 2.234 54.264 27.273 1.00 59.76 ? 14 HIS A ND1 1 ATOM 92 C CD2 . HIS A 1 11 ? 0.891 55.873 26.659 1.00 58.51 ? 14 HIS A CD2 1 ATOM 93 C CE1 . HIS A 1 11 ? 2.871 55.404 27.479 1.00 59.39 ? 14 HIS A CE1 1 ATOM 94 N NE2 . HIS A 1 11 ? 2.077 56.396 27.115 1.00 60.19 ? 14 HIS A NE2 1 ATOM 95 N N . HIS A 1 12 ? -2.895 51.952 27.557 1.00 61.22 ? 15 HIS A N 1 ATOM 96 C CA . HIS A 1 12 ? -4.027 51.171 27.086 1.00 60.90 ? 15 HIS A CA 1 ATOM 97 C C . HIS A 1 12 ? -4.431 51.773 25.771 1.00 59.76 ? 15 HIS A C 1 ATOM 98 O O . HIS A 1 12 ? -4.002 52.876 25.429 1.00 59.22 ? 15 HIS A O 1 ATOM 99 C CB . HIS A 1 12 ? -5.165 51.201 28.094 1.00 62.22 ? 15 HIS A CB 1 ATOM 100 C CG . HIS A 1 12 ? -4.968 50.225 29.209 1.00 65.87 ? 15 HIS A CG 1 ATOM 101 N ND1 . HIS A 1 12 ? -5.310 48.894 29.098 1.00 66.12 ? 15 HIS A ND1 1 ATOM 102 C CD2 . HIS A 1 12 ? -4.340 50.352 30.404 1.00 67.43 ? 15 HIS A CD2 1 ATOM 103 C CE1 . HIS A 1 12 ? -4.898 48.242 30.172 1.00 67.28 ? 15 HIS A CE1 1 ATOM 104 N NE2 . HIS A 1 12 ? -4.304 49.104 30.978 1.00 67.51 ? 15 HIS A NE2 1 ATOM 105 N N . PHE A 1 13 ? -5.249 51.060 25.020 1.00 58.55 ? 16 PHE A N 1 ATOM 106 C CA . PHE A 1 13 ? -5.593 51.564 23.713 1.00 58.22 ? 16 PHE A CA 1 ATOM 107 C C . PHE A 1 13 ? -5.942 53.046 23.658 1.00 58.10 ? 16 PHE A C 1 ATOM 108 O O . PHE A 1 13 ? -5.310 53.805 22.918 1.00 57.27 ? 16 PHE A O 1 ATOM 109 C CB . PHE A 1 13 ? -6.718 50.743 23.080 1.00 59.33 ? 16 PHE A CB 1 ATOM 110 C CG . PHE A 1 13 ? -6.744 50.854 21.584 1.00 60.65 ? 16 PHE A CG 1 ATOM 111 C CD1 . PHE A 1 13 ? -5.781 50.207 20.816 1.00 59.69 ? 16 PHE A CD1 1 ATOM 112 C CD2 . PHE A 1 13 ? -7.658 51.686 20.944 1.00 61.30 ? 16 PHE A CD2 1 ATOM 113 C CE1 . PHE A 1 13 ? -5.719 50.393 19.429 1.00 58.87 ? 16 PHE A CE1 1 ATOM 114 C CE2 . PHE A 1 13 ? -7.603 51.878 19.552 1.00 60.69 ? 16 PHE A CE2 1 ATOM 115 C CZ . PHE A 1 13 ? -6.629 51.230 18.798 1.00 58.42 ? 16 PHE A CZ 1 ATOM 116 N N . SER A 1 14 ? -6.927 53.458 24.446 1.00 58.58 ? 17 SER A N 1 ATOM 117 C CA . SER A 1 14 ? -7.352 54.845 24.440 1.00 59.51 ? 17 SER A CA 1 ATOM 118 C C . SER A 1 14 ? -6.186 55.826 24.449 1.00 60.16 ? 17 SER A C 1 ATOM 119 O O . SER A 1 14 ? -6.113 56.727 23.607 1.00 60.48 ? 17 SER A O 1 ATOM 120 C CB . SER A 1 14 ? -8.256 55.123 25.640 1.00 61.43 ? 17 SER A CB 1 ATOM 121 O OG . SER A 1 14 ? -8.775 56.445 25.571 1.00 62.40 ? 17 SER A OG 1 ATOM 122 N N . ASP A 1 15 ? -5.277 55.642 25.407 1.00 60.11 ? 18 ASP A N 1 ATOM 123 C CA . ASP A 1 15 ? -4.113 56.513 25.565 1.00 58.62 ? 18 ASP A CA 1 ATOM 124 C C . ASP A 1 15 ? -3.056 56.326 24.507 1.00 57.69 ? 18 ASP A C 1 ATOM 125 O O . ASP A 1 15 ? -2.340 57.271 24.172 1.00 57.49 ? 18 ASP A O 1 ATOM 126 C CB . ASP A 1 15 ? -3.509 56.299 26.941 1.00 59.53 ? 18 ASP A CB 1 ATOM 127 C CG . ASP A 1 15 ? -4.493 56.588 28.023 1.00 60.80 ? 18 ASP A CG 1 ATOM 128 O OD1 . ASP A 1 15 ? -4.851 57.781 28.164 1.00 61.30 ? 18 ASP A OD1 1 ATOM 129 O OD2 . ASP A 1 15 ? -4.931 55.629 28.701 1.00 60.81 ? 18 ASP A OD2 1 ATOM 130 N N . MET A 1 16 ? -2.937 55.104 23.997 1.00 56.22 ? 19 MET A N 1 ATOM 131 C CA . MET A 1 16 ? -1.972 54.854 22.959 1.00 54.29 ? 19 MET A CA 1 ATOM 132 C C . MET A 1 16 ? -2.456 55.600 21.731 1.00 54.72 ? 19 MET A C 1 ATOM 133 O O . MET A 1 16 ? -1.661 56.181 20.987 1.00 54.75 ? 19 MET A O 1 ATOM 134 C CB . MET A 1 16 ? -1.886 53.385 22.652 1.00 54.03 ? 19 MET A CB 1 ATOM 135 C CG . MET A 1 16 ? -0.865 53.120 21.584 1.00 54.65 ? 19 MET A CG 1 ATOM 136 S SD . MET A 1 16 ? -1.130 51.503 20.909 1.00 55.42 ? 19 MET A SD 1 ATOM 137 C CE . MET A 1 16 ? -0.203 50.596 22.023 1.00 58.40 ? 19 MET A CE 1 ATOM 138 N N . GLU A 1 17 ? -3.769 55.582 21.515 1.00 54.02 ? 20 GLU A N 1 ATOM 139 C CA . GLU A 1 17 ? -4.335 56.304 20.383 1.00 55.86 ? 20 GLU A CA 1 ATOM 140 C C . GLU A 1 17 ? -3.999 57.780 20.584 1.00 56.71 ? 20 GLU A C 1 ATOM 141 O O . GLU A 1 17 ? -3.445 58.442 19.707 1.00 57.08 ? 20 GLU A O 1 ATOM 142 C CB . GLU A 1 17 ? -5.857 56.123 20.301 1.00 56.35 ? 20 GLU A CB 1 ATOM 143 C CG . GLU A 1 17 ? -6.472 56.884 19.133 1.00 60.67 ? 20 GLU A CG 1 ATOM 144 C CD . GLU A 1 17 ? -7.909 56.481 18.793 1.00 64.57 ? 20 GLU A CD 1 ATOM 145 O OE1 . GLU A 1 17 ? -8.176 55.300 18.463 1.00 65.54 ? 20 GLU A OE1 1 ATOM 146 O OE2 . GLU A 1 17 ? -8.782 57.371 18.831 1.00 69.70 ? 20 GLU A OE2 1 ATOM 147 N N . ILE A 1 18 ? -4.324 58.292 21.759 1.00 57.40 ? 21 ILE A N 1 ATOM 148 C CA . ILE A 1 18 ? -4.039 59.680 22.070 1.00 57.00 ? 21 ILE A CA 1 ATOM 149 C C . ILE A 1 18 ? -2.563 60.001 21.840 1.00 57.12 ? 21 ILE A C 1 ATOM 150 O O . ILE A 1 18 ? -2.243 60.924 21.089 1.00 58.51 ? 21 ILE A O 1 ATOM 151 C CB . ILE A 1 18 ? -4.426 59.982 23.525 1.00 57.36 ? 21 ILE A CB 1 ATOM 152 C CG1 . ILE A 1 18 ? -5.954 59.880 23.663 1.00 55.32 ? 21 ILE A CG1 1 ATOM 153 C CG2 . ILE A 1 18 ? -3.867 61.344 23.951 1.00 55.89 ? 21 ILE A CG2 1 ATOM 154 C CD1 . ILE A 1 18 ? -6.445 60.022 25.086 1.00 55.06 ? 21 ILE A CD1 1 ATOM 155 N N . PHE A 1 19 ? -1.677 59.235 22.486 1.00 56.79 ? 22 PHE A N 1 ATOM 156 C CA . PHE A 1 19 ? -0.219 59.402 22.371 1.00 54.55 ? 22 PHE A CA 1 ATOM 157 C C . PHE A 1 19 ? 0.176 59.484 20.908 1.00 54.08 ? 22 PHE A C 1 ATOM 158 O O . PHE A 1 19 ? 0.833 60.431 20.464 1.00 53.77 ? 22 PHE A O 1 ATOM 159 C CB . PHE A 1 19 ? 0.499 58.206 22.996 1.00 52.71 ? 22 PHE A CB 1 ATOM 160 C CG . PHE A 1 19 ? 2.001 58.267 22.893 1.00 54.16 ? 22 PHE A CG 1 ATOM 161 C CD1 . PHE A 1 19 ? 2.663 57.707 21.811 1.00 56.10 ? 22 PHE A CD1 1 ATOM 162 C CD2 . PHE A 1 19 ? 2.760 58.851 23.896 1.00 56.45 ? 22 PHE A CD2 1 ATOM 163 C CE1 . PHE A 1 19 ? 4.065 57.722 21.729 1.00 55.69 ? 22 PHE A CE1 1 ATOM 164 C CE2 . PHE A 1 19 ? 4.161 58.872 23.827 1.00 55.85 ? 22 PHE A CE2 1 ATOM 165 C CZ . PHE A 1 19 ? 4.811 58.306 22.741 1.00 56.64 ? 22 PHE A CZ 1 ATOM 166 N N . LEU A 1 20 ? -0.231 58.472 20.162 1.00 52.77 ? 23 LEU A N 1 ATOM 167 C CA . LEU A 1 20 ? 0.075 58.425 18.753 1.00 53.36 ? 23 LEU A CA 1 ATOM 168 C C . LEU A 1 20 ? -0.394 59.651 17.988 1.00 55.38 ? 23 LEU A C 1 ATOM 169 O O . LEU A 1 20 ? 0.375 60.239 17.223 1.00 57.14 ? 23 LEU A O 1 ATOM 170 C CB . LEU A 1 20 ? -0.544 57.181 18.127 1.00 50.92 ? 23 LEU A CB 1 ATOM 171 C CG . LEU A 1 20 ? 0.154 55.868 18.441 1.00 48.97 ? 23 LEU A CG 1 ATOM 172 C CD1 . LEU A 1 20 ? -0.722 54.759 17.944 1.00 46.64 ? 23 LEU A CD1 1 ATOM 173 C CD2 . LEU A 1 20 ? 1.542 55.822 17.799 1.00 45.71 ? 23 LEU A CD2 1 ATOM 174 N N . ARG A 1 21 ? -1.653 60.036 18.179 1.00 56.07 ? 24 ARG A N 1 ATOM 175 C CA . ARG A 1 21 ? -2.188 61.179 17.459 1.00 56.18 ? 24 ARG A CA 1 ATOM 176 C C . ARG A 1 21 ? -1.473 62.455 17.857 1.00 56.50 ? 24 ARG A C 1 ATOM 177 O O . ARG A 1 21 ? -1.277 63.329 17.024 1.00 56.76 ? 24 ARG A O 1 ATOM 178 C CB . ARG A 1 21 ? -3.683 61.323 17.709 1.00 58.13 ? 24 ARG A CB 1 ATOM 179 C CG . ARG A 1 21 ? -4.598 60.279 17.051 1.00 62.26 ? 24 ARG A CG 1 ATOM 180 C CD . ARG A 1 21 ? -5.866 60.158 17.910 1.00 66.35 ? 24 ARG A CD 1 ATOM 181 N NE . ARG A 1 21 ? -6.947 59.283 17.440 1.00 67.25 ? 24 ARG A NE 1 ATOM 182 C CZ . ARG A 1 21 ? -7.623 59.447 16.305 1.00 68.52 ? 24 ARG A CZ 1 ATOM 183 N NH1 . ARG A 1 21 ? -7.314 60.456 15.487 1.00 68.69 ? 24 ARG A NH1 1 ATOM 184 N NH2 . ARG A 1 21 ? -8.656 58.647 16.027 1.00 68.58 ? 24 ARG A NH2 1 ATOM 185 N N . ARG A 1 22 ? -1.078 62.574 19.122 1.00 57.33 ? 25 ARG A N 1 ATOM 186 C CA . ARG A 1 22 ? -0.364 63.774 19.560 1.00 59.74 ? 25 ARG A CA 1 ATOM 187 C C . ARG A 1 22 ? 0.899 63.961 18.724 1.00 60.77 ? 25 ARG A C 1 ATOM 188 O O . ARG A 1 22 ? 1.197 65.067 18.261 1.00 62.56 ? 25 ARG A O 1 ATOM 189 C CB . ARG A 1 22 ? 0.007 63.670 21.035 1.00 59.68 ? 25 ARG A CB 1 ATOM 190 C CG . ARG A 1 22 ? 0.960 64.745 21.552 1.00 63.24 ? 25 ARG A CG 1 ATOM 191 C CD . ARG A 1 22 ? 0.879 64.750 23.072 1.00 70.33 ? 25 ARG A CD 1 ATOM 192 N NE . ARG A 1 22 ? 2.093 65.154 23.787 1.00 78.37 ? 25 ARG A NE 1 ATOM 193 C CZ . ARG A 1 22 ? 2.685 66.347 23.693 1.00 83.57 ? 25 ARG A CZ 1 ATOM 194 N NH1 . ARG A 1 22 ? 2.188 67.286 22.892 1.00 86.24 ? 25 ARG A NH1 1 ATOM 195 N NH2 . ARG A 1 22 ? 3.761 66.618 24.436 1.00 86.16 ? 25 ARG A NH2 1 ATOM 196 N N . TYR A 1 23 ? 1.641 62.875 18.521 1.00 60.38 ? 26 TYR A N 1 ATOM 197 C CA . TYR A 1 23 ? 2.857 62.955 17.726 1.00 59.72 ? 26 TYR A CA 1 ATOM 198 C C . TYR A 1 23 ? 2.586 63.107 16.255 1.00 59.41 ? 26 TYR A C 1 ATOM 199 O O . TYR A 1 23 ? 3.365 63.740 15.548 1.00 59.52 ? 26 TYR A O 1 ATOM 200 C CB . TYR A 1 23 ? 3.751 61.749 17.974 1.00 59.86 ? 26 TYR A CB 1 ATOM 201 C CG . TYR A 1 23 ? 4.452 61.876 19.291 1.00 60.80 ? 26 TYR A CG 1 ATOM 202 C CD1 . TYR A 1 23 ? 5.602 62.651 19.407 1.00 60.35 ? 26 TYR A CD1 1 ATOM 203 C CD2 . TYR A 1 23 ? 3.901 61.333 20.447 1.00 61.20 ? 26 TYR A CD2 1 ATOM 204 C CE1 . TYR A 1 23 ? 6.179 62.894 20.639 1.00 63.44 ? 26 TYR A CE1 1 ATOM 205 C CE2 . TYR A 1 23 ? 4.470 61.566 21.686 1.00 62.66 ? 26 TYR A CE2 1 ATOM 206 C CZ . TYR A 1 23 ? 5.606 62.354 21.780 1.00 63.92 ? 26 TYR A CZ 1 ATOM 207 O OH . TYR A 1 23 ? 6.134 62.651 23.024 1.00 68.02 ? 26 TYR A OH 1 ATOM 208 N N . ALA A 1 24 ? 1.487 62.536 15.780 1.00 59.35 ? 27 ALA A N 1 ATOM 209 C CA . ALA A 1 24 ? 1.155 62.683 14.368 1.00 60.08 ? 27 ALA A CA 1 ATOM 210 C C . ALA A 1 24 ? 0.864 64.160 14.119 1.00 61.67 ? 27 ALA A C 1 ATOM 211 O O . ALA A 1 24 ? 1.272 64.711 13.104 1.00 63.82 ? 27 ALA A O 1 ATOM 212 C CB . ALA A 1 24 ? -0.061 61.834 14.005 1.00 57.04 ? 27 ALA A CB 1 ATOM 213 N N . ASN A 1 25 ? 0.186 64.804 15.068 1.00 62.99 ? 28 ASN A N 1 ATOM 214 C CA . ASN A 1 25 ? -0.160 66.215 14.941 1.00 63.00 ? 28 ASN A CA 1 ATOM 215 C C . ASN A 1 25 ? 0.973 67.181 15.231 1.00 63.23 ? 28 ASN A C 1 ATOM 216 O O . ASN A 1 25 ? 1.122 68.172 14.531 1.00 63.61 ? 28 ASN A O 1 ATOM 217 C CB . ASN A 1 25 ? -1.359 66.548 15.826 1.00 63.57 ? 28 ASN A CB 1 ATOM 218 C CG . ASN A 1 25 ? -2.636 65.899 15.328 1.00 65.89 ? 28 ASN A CG 1 ATOM 219 O OD1 . ASN A 1 25 ? -2.815 65.712 14.127 1.00 65.74 ? 28 ASN A OD1 1 ATOM 220 N ND2 . ASN A 1 25 ? -3.534 65.563 16.242 1.00 65.71 ? 28 ASN A ND2 1 ATOM 221 N N . GLU A 1 26 ? 1.773 66.904 16.251 1.00 62.88 ? 29 GLU A N 1 ATOM 222 C CA . GLU A 1 26 ? 2.878 67.793 16.582 1.00 64.33 ? 29 GLU A CA 1 ATOM 223 C C . GLU A 1 26 ? 4.023 67.830 15.555 1.00 65.76 ? 29 GLU A C 1 ATOM 224 O O . GLU A 1 26 ? 4.743 68.832 15.451 1.00 66.24 ? 29 GLU A O 1 ATOM 225 C CB . GLU A 1 26 ? 3.445 67.430 17.952 1.00 64.02 ? 29 GLU A CB 1 ATOM 226 C CG . GLU A 1 26 ? 2.812 68.172 19.091 1.00 65.79 ? 29 GLU A CG 1 ATOM 227 C CD . GLU A 1 26 ? 3.849 68.683 20.068 1.00 67.43 ? 29 GLU A CD 1 ATOM 228 O OE1 . GLU A 1 26 ? 4.290 67.891 20.929 1.00 66.27 ? 29 GLU A OE1 1 ATOM 229 O OE2 . GLU A 1 26 ? 4.236 69.873 19.960 1.00 70.16 ? 29 GLU A OE2 1 ATOM 230 N N . TYR A 1 27 ? 4.198 66.744 14.804 1.00 66.71 ? 30 TYR A N 1 ATOM 231 C CA . TYR A 1 27 ? 5.276 66.673 13.816 1.00 66.26 ? 30 TYR A CA 1 ATOM 232 C C . TYR A 1 27 ? 4.738 66.100 12.528 1.00 66.62 ? 30 TYR A C 1 ATOM 233 O O . TYR A 1 27 ? 5.171 65.045 12.076 1.00 67.09 ? 30 TYR A O 1 ATOM 234 C CB . TYR A 1 27 ? 6.400 65.772 14.309 1.00 63.29 ? 30 TYR A CB 1 ATOM 235 C CG . TYR A 1 27 ? 6.808 66.013 15.738 1.00 62.20 ? 30 TYR A CG 1 ATOM 236 C CD1 . TYR A 1 27 ? 6.069 65.491 16.798 1.00 60.10 ? 30 TYR A CD1 1 ATOM 237 C CD2 . TYR A 1 27 ? 7.953 66.749 16.032 1.00 64.04 ? 30 TYR A CD2 1 ATOM 238 C CE1 . TYR A 1 27 ? 6.469 65.693 18.120 1.00 59.93 ? 30 TYR A CE1 1 ATOM 239 C CE2 . TYR A 1 27 ? 8.363 66.961 17.349 1.00 62.87 ? 30 TYR A CE2 1 ATOM 240 C CZ . TYR A 1 27 ? 7.623 66.432 18.385 1.00 60.99 ? 30 TYR A CZ 1 ATOM 241 O OH . TYR A 1 27 ? 8.055 66.641 19.675 1.00 59.58 ? 30 TYR A OH 1 ATOM 242 N N . PRO A 1 28 ? 3.793 66.808 11.908 1.00 66.98 ? 31 PRO A N 1 ATOM 243 C CA . PRO A 1 28 ? 3.137 66.421 10.655 1.00 67.62 ? 31 PRO A CA 1 ATOM 244 C C . PRO A 1 28 ? 4.084 66.320 9.467 1.00 67.94 ? 31 PRO A C 1 ATOM 245 O O . PRO A 1 28 ? 3.775 65.666 8.464 1.00 67.61 ? 31 PRO A O 1 ATOM 246 C CB . PRO A 1 28 ? 2.108 67.525 10.463 1.00 67.04 ? 31 PRO A CB 1 ATOM 247 C CG . PRO A 1 28 ? 2.847 68.721 10.981 1.00 67.41 ? 31 PRO A CG 1 ATOM 248 C CD . PRO A 1 28 ? 3.469 68.200 12.261 1.00 67.01 ? 31 PRO A CD 1 ATOM 249 N N . SER A 1 29 ? 5.231 66.977 9.583 1.00 66.85 ? 32 SER A N 1 ATOM 250 C CA . SER A 1 29 ? 6.203 66.974 8.508 1.00 66.34 ? 32 SER A CA 1 ATOM 251 C C . SER A 1 29 ? 7.066 65.711 8.509 1.00 66.67 ? 32 SER A C 1 ATOM 252 O O . SER A 1 29 ? 7.712 65.392 7.515 1.00 67.77 ? 32 SER A O 1 ATOM 253 C CB . SER A 1 29 ? 7.095 68.204 8.636 1.00 65.35 ? 32 SER A CB 1 ATOM 254 O OG . SER A 1 29 ? 7.789 68.168 9.873 1.00 62.95 ? 32 SER A OG 1 ATOM 255 N N . ILE A 1 30 ? 7.064 64.981 9.617 1.00 66.33 ? 33 ILE A N 1 ATOM 256 C CA . ILE A 1 30 ? 7.884 63.781 9.730 1.00 65.08 ? 33 ILE A CA 1 ATOM 257 C C . ILE A 1 30 ? 7.091 62.514 9.918 1.00 64.66 ? 33 ILE A C 1 ATOM 258 O O . ILE A 1 30 ? 7.610 61.408 9.764 1.00 65.84 ? 33 ILE A O 1 ATOM 259 C CB . ILE A 1 30 ? 8.824 63.908 10.920 1.00 64.70 ? 33 ILE A CB 1 ATOM 260 C CG1 . ILE A 1 30 ? 9.703 65.116 10.711 1.00 68.06 ? 33 ILE A CG1 1 ATOM 261 C CG2 . ILE A 1 30 ? 9.683 62.693 11.049 1.00 67.31 ? 33 ILE A CG2 1 ATOM 262 C CD1 . ILE A 1 30 ? 10.237 65.198 9.302 1.00 68.73 ? 33 ILE A CD1 1 ATOM 263 N N . THR A 1 31 ? 5.818 62.671 10.225 1.00 62.87 ? 34 THR A N 1 ATOM 264 C CA . THR A 1 31 ? 5.012 61.513 10.509 1.00 62.08 ? 34 THR A CA 1 ATOM 265 C C . THR A 1 31 ? 3.762 61.348 9.700 1.00 61.63 ? 34 THR A C 1 ATOM 266 O O . THR A 1 31 ? 3.212 62.302 9.153 1.00 63.95 ? 34 THR A O 1 ATOM 267 C CB . THR A 1 31 ? 4.551 61.542 11.956 1.00 62.22 ? 34 THR A CB 1 ATOM 268 O OG1 . THR A 1 31 ? 3.683 62.673 12.133 1.00 61.49 ? 34 THR A OG1 1 ATOM 269 C CG2 . THR A 1 31 ? 5.734 61.652 12.901 1.00 61.02 ? 34 THR A CG2 1 ATOM 270 N N . ARG A 1 32 ? 3.297 60.110 9.672 1.00 58.68 ? 35 ARG A N 1 ATOM 271 C CA . ARG A 1 32 ? 2.068 59.787 9.005 1.00 56.71 ? 35 ARG A CA 1 ATOM 272 C C . ARG A 1 32 ? 1.498 58.612 9.731 1.00 56.50 ? 35 ARG A C 1 ATOM 273 O O . ARG A 1 32 ? 2.027 57.505 9.677 1.00 58.00 ? 35 ARG A O 1 ATOM 274 C CB . ARG A 1 32 ? 2.288 59.412 7.564 1.00 56.18 ? 35 ARG A CB 1 ATOM 275 C CG . ARG A 1 32 ? 1.002 59.032 6.899 1.00 54.23 ? 35 ARG A CG 1 ATOM 276 C CD . ARG A 1 32 ? 1.297 58.018 5.861 1.00 54.87 ? 35 ARG A CD 1 ATOM 277 N NE . ARG A 1 32 ? 0.094 57.313 5.476 1.00 55.87 ? 35 ARG A NE 1 ATOM 278 C CZ . ARG A 1 32 ? 0.107 56.095 4.961 1.00 57.86 ? 35 ARG A CZ 1 ATOM 279 N NH1 . ARG A 1 32 ? 1.267 55.459 4.792 1.00 57.85 ? 35 ARG A NH1 1 ATOM 280 N NH2 . ARG A 1 32 ? -1.040 55.515 4.629 1.00 59.90 ? 35 ARG A NH2 1 ATOM 281 N N . LEU A 1 33 ? 0.410 58.869 10.428 1.00 55.61 ? 36 LEU A N 1 ATOM 282 C CA . LEU A 1 33 ? -0.253 57.849 11.191 1.00 54.61 ? 36 LEU A CA 1 ATOM 283 C C . LEU A 1 33 ? -1.410 57.269 10.382 1.00 54.79 ? 36 LEU A C 1 ATOM 284 O O . LEU A 1 33 ? -2.215 58.010 9.795 1.00 53.91 ? 36 LEU A O 1 ATOM 285 C CB . LEU A 1 33 ? -0.751 58.464 12.499 1.00 54.45 ? 36 LEU A CB 1 ATOM 286 C CG . LEU A 1 33 ? -1.602 57.599 13.423 1.00 54.43 ? 36 LEU A CG 1 ATOM 287 C CD1 . LEU A 1 33 ? -0.809 56.383 13.852 1.00 51.58 ? 36 LEU A CD1 1 ATOM 288 C CD2 . LEU A 1 33 ? -2.023 58.422 14.628 1.00 53.35 ? 36 LEU A CD2 1 ATOM 289 N N . TYR A 1 34 ? -1.479 55.939 10.348 1.00 54.46 ? 37 TYR A N 1 ATOM 290 C CA . TYR A 1 34 ? -2.542 55.240 9.632 1.00 53.73 ? 37 TYR A CA 1 ATOM 291 C C . TYR A 1 34 ? -2.893 53.915 10.282 1.00 53.59 ? 37 TYR A C 1 ATOM 292 O O . TYR A 1 34 ? -2.193 53.429 11.170 1.00 52.30 ? 37 TYR A O 1 ATOM 293 C CB . TYR A 1 34 ? -2.143 54.992 8.179 1.00 53.89 ? 37 TYR A CB 1 ATOM 294 C CG . TYR A 1 34 ? -0.863 54.189 7.986 1.00 53.38 ? 37 TYR A CG 1 ATOM 295 C CD1 . TYR A 1 34 ? 0.396 54.757 8.197 1.00 52.90 ? 37 TYR A CD1 1 ATOM 296 C CD2 . TYR A 1 34 ? -0.918 52.863 7.570 1.00 52.80 ? 37 TYR A CD2 1 ATOM 297 C CE1 . TYR A 1 34 ? 1.554 54.016 7.994 1.00 53.74 ? 37 TYR A CE1 1 ATOM 298 C CE2 . TYR A 1 34 ? 0.226 52.126 7.366 1.00 52.63 ? 37 TYR A CE2 1 ATOM 299 C CZ . TYR A 1 34 ? 1.450 52.698 7.575 1.00 53.63 ? 37 TYR A CZ 1 ATOM 300 O OH . TYR A 1 34 ? 2.561 51.927 7.347 1.00 57.82 ? 37 TYR A OH 1 ATOM 301 N N . SER A 1 35 ? -4.005 53.349 9.841 1.00 54.98 ? 38 SER A N 1 ATOM 302 C CA . SER A 1 35 ? -4.466 52.065 10.346 1.00 55.47 ? 38 SER A CA 1 ATOM 303 C C . SER A 1 35 ? -4.292 51.101 9.189 1.00 56.39 ? 38 SER A C 1 ATOM 304 O O . SER A 1 35 ? -4.180 51.518 8.035 1.00 57.48 ? 38 SER A O 1 ATOM 305 C CB . SER A 1 35 ? -5.940 52.130 10.760 1.00 55.19 ? 38 SER A CB 1 ATOM 306 O OG . SER A 1 35 ? -6.416 50.853 11.163 1.00 55.52 ? 38 SER A OG 1 ATOM 307 N N . VAL A 1 36 ? -4.293 49.814 9.497 1.00 56.71 ? 39 VAL A N 1 ATOM 308 C CA . VAL A 1 36 ? -4.081 48.802 8.481 1.00 55.02 ? 39 VAL A CA 1 ATOM 309 C C . VAL A 1 36 ? -5.262 47.823 8.469 1.00 54.15 ? 39 VAL A C 1 ATOM 310 O O . VAL A 1 36 ? -5.335 46.904 7.649 1.00 52.65 ? 39 VAL A O 1 ATOM 311 C CB . VAL A 1 36 ? -2.719 48.101 8.779 1.00 54.69 ? 39 VAL A CB 1 ATOM 312 C CG1 . VAL A 1 36 ? -2.911 46.877 9.647 1.00 53.88 ? 39 VAL A CG1 1 ATOM 313 C CG2 . VAL A 1 36 ? -2.018 47.779 7.506 1.00 57.26 ? 39 VAL A CG2 1 ATOM 314 N N . GLY A 1 37 ? -6.198 48.070 9.384 1.00 54.08 ? 40 GLY A N 1 ATOM 315 C CA . GLY A 1 37 ? -7.378 47.237 9.526 1.00 53.27 ? 40 GLY A CA 1 ATOM 316 C C . GLY A 1 37 ? -7.862 47.392 10.954 1.00 52.23 ? 40 GLY A C 1 ATOM 317 O O . GLY A 1 37 ? -7.452 48.333 11.630 1.00 51.60 ? 40 GLY A O 1 ATOM 318 N N . LYS A 1 38 ? -8.721 46.487 11.420 1.00 51.35 ? 41 LYS A N 1 ATOM 319 C CA . LYS A 1 38 ? -9.234 46.549 12.789 1.00 50.73 ? 41 LYS A CA 1 ATOM 320 C C . LYS A 1 38 ? -9.187 45.194 13.472 1.00 50.33 ? 41 LYS A C 1 ATOM 321 O O . LYS A 1 38 ? -9.475 44.173 12.859 1.00 51.49 ? 41 LYS A O 1 ATOM 322 C CB . LYS A 1 38 ? -10.693 47.024 12.831 1.00 50.45 ? 41 LYS A CB 1 ATOM 323 C CG . LYS A 1 38 ? -10.980 48.355 12.169 1.00 52.18 ? 41 LYS A CG 1 ATOM 324 C CD . LYS A 1 38 ? -12.244 48.987 12.757 1.00 51.98 ? 41 LYS A CD 1 ATOM 325 C CE . LYS A 1 38 ? -12.767 50.114 11.876 1.00 52.57 ? 41 LYS A CE 1 ATOM 326 N NZ . LYS A 1 38 ? -11.671 50.988 11.350 1.00 55.03 ? 41 LYS A NZ 1 ATOM 327 N N . SER A 1 39 ? -8.851 45.197 14.755 1.00 50.05 ? 42 SER A N 1 ATOM 328 C CA . SER A 1 39 ? -8.804 43.973 15.535 1.00 49.48 ? 42 SER A CA 1 ATOM 329 C C . SER A 1 39 ? -10.198 43.373 15.514 1.00 49.24 ? 42 SER A C 1 ATOM 330 O O . SER A 1 39 ? -11.148 44.004 15.071 1.00 51.22 ? 42 SER A O 1 ATOM 331 C CB . SER A 1 39 ? -8.421 44.287 16.979 1.00 51.16 ? 42 SER A CB 1 ATOM 332 O OG . SER A 1 39 ? -9.434 45.057 17.611 1.00 52.51 ? 42 SER A OG 1 ATOM 333 N N . VAL A 1 40 ? -10.326 42.149 15.994 1.00 49.13 ? 43 VAL A N 1 ATOM 334 C CA . VAL A 1 40 ? -11.625 41.510 16.024 1.00 50.52 ? 43 VAL A CA 1 ATOM 335 C C . VAL A 1 40 ? -12.595 42.437 16.736 1.00 52.43 ? 43 VAL A C 1 ATOM 336 O O . VAL A 1 40 ? -13.737 42.602 16.303 1.00 53.16 ? 43 VAL A O 1 ATOM 337 C CB . VAL A 1 40 ? -11.568 40.160 16.777 1.00 51.23 ? 43 VAL A CB 1 ATOM 338 C CG1 . VAL A 1 40 ? -12.956 39.778 17.286 1.00 50.59 ? 43 VAL A CG1 1 ATOM 339 C CG2 . VAL A 1 40 ? -11.027 39.070 15.851 1.00 50.00 ? 43 VAL A CG2 1 ATOM 340 N N . GLU A 1 41 ? -12.130 43.056 17.820 1.00 53.04 ? 44 GLU A N 1 ATOM 341 C CA . GLU A 1 41 ? -12.977 43.958 18.592 1.00 52.83 ? 44 GLU A CA 1 ATOM 342 C C . GLU A 1 41 ? -12.931 45.384 18.067 1.00 52.21 ? 44 GLU A C 1 ATOM 343 O O . GLU A 1 41 ? -13.090 46.350 18.804 1.00 52.41 ? 44 GLU A O 1 ATOM 344 C CB . GLU A 1 41 ? -12.592 43.913 20.065 1.00 53.93 ? 44 GLU A CB 1 ATOM 345 C CG . GLU A 1 41 ? -12.420 42.497 20.556 1.00 55.83 ? 44 GLU A CG 1 ATOM 346 C CD . GLU A 1 41 ? -12.175 42.406 22.043 1.00 58.26 ? 44 GLU A CD 1 ATOM 347 O OE1 . GLU A 1 41 ? -11.346 43.187 22.581 1.00 59.73 ? 44 GLU A OE1 1 ATOM 348 O OE2 . GLU A 1 41 ? -12.812 41.535 22.667 1.00 59.34 ? 44 GLU A OE2 1 ATOM 349 N N . LEU A 1 42 ? -12.684 45.498 16.775 1.00 51.71 ? 45 LEU A N 1 ATOM 350 C CA . LEU A 1 42 ? -12.691 46.782 16.093 1.00 51.41 ? 45 LEU A CA 1 ATOM 351 C C . LEU A 1 42 ? -11.741 47.867 16.544 1.00 52.56 ? 45 LEU A C 1 ATOM 352 O O . LEU A 1 42 ? -12.061 49.048 16.394 1.00 54.12 ? 45 LEU A O 1 ATOM 353 C CB . LEU A 1 42 ? -14.110 47.342 16.109 1.00 48.69 ? 45 LEU A CB 1 ATOM 354 C CG . LEU A 1 42 ? -15.209 46.290 15.931 1.00 45.93 ? 45 LEU A CG 1 ATOM 355 C CD1 . LEU A 1 42 ? -16.510 46.983 15.762 1.00 47.78 ? 45 LEU A CD1 1 ATOM 356 C CD2 . LEU A 1 42 ? -14.946 45.423 14.725 1.00 41.89 ? 45 LEU A CD2 1 ATOM 357 N N . ARG A 1 43 ? -10.590 47.486 17.097 1.00 53.17 ? 46 ARG A N 1 ATOM 358 C CA . ARG A 1 43 ? -9.583 48.471 17.508 1.00 54.12 ? 46 ARG A CA 1 ATOM 359 C C . ARG A 1 43 ? -8.608 48.653 16.346 1.00 54.55 ? 46 ARG A C 1 ATOM 360 O O . ARG A 1 43 ? -8.102 47.681 15.797 1.00 55.51 ? 46 ARG A O 1 ATOM 361 C CB . ARG A 1 43 ? -8.825 47.988 18.740 1.00 54.16 ? 46 ARG A CB 1 ATOM 362 C CG . ARG A 1 43 ? -9.672 47.898 20.000 1.00 54.68 ? 46 ARG A CG 1 ATOM 363 C CD . ARG A 1 43 ? -8.888 47.297 21.146 1.00 52.91 ? 46 ARG A CD 1 ATOM 364 N NE . ARG A 1 43 ? -9.745 46.475 21.989 1.00 51.26 ? 46 ARG A NE 1 ATOM 365 C CZ . ARG A 1 43 ? -10.419 46.944 23.024 1.00 53.96 ? 46 ARG A CZ 1 ATOM 366 N NH1 . ARG A 1 43 ? -10.311 48.229 23.351 1.00 55.75 ? 46 ARG A NH1 1 ATOM 367 N NH2 . ARG A 1 43 ? -11.181 46.126 23.737 1.00 56.16 ? 46 ARG A NH2 1 ATOM 368 N N . GLU A 1 44 ? -8.346 49.893 15.968 1.00 54.56 ? 47 GLU A N 1 ATOM 369 C CA . GLU A 1 44 ? -7.449 50.152 14.852 1.00 54.47 ? 47 GLU A CA 1 ATOM 370 C C . GLU A 1 44 ? -6.073 49.535 15.022 1.00 54.66 ? 47 GLU A C 1 ATOM 371 O O . GLU A 1 44 ? -5.530 49.481 16.114 1.00 57.25 ? 47 GLU A O 1 ATOM 372 C CB . GLU A 1 44 ? -7.313 51.656 14.655 1.00 55.84 ? 47 GLU A CB 1 ATOM 373 C CG . GLU A 1 44 ? -8.648 52.335 14.463 1.00 60.25 ? 47 GLU A CG 1 ATOM 374 C CD . GLU A 1 44 ? -9.139 52.227 13.036 1.00 62.60 ? 47 GLU A CD 1 ATOM 375 O OE1 . GLU A 1 44 ? -9.002 51.141 12.427 1.00 63.61 ? 47 GLU A OE1 1 ATOM 376 O OE2 . GLU A 1 44 ? -9.669 53.236 12.521 1.00 65.56 ? 47 GLU A OE2 1 ATOM 377 N N . LEU A 1 45 ? -5.515 49.051 13.928 1.00 54.21 ? 48 LEU A N 1 ATOM 378 C CA . LEU A 1 45 ? -4.191 48.477 13.961 1.00 54.51 ? 48 LEU A CA 1 ATOM 379 C C . LEU A 1 45 ? -3.263 49.573 13.473 1.00 55.37 ? 48 LEU A C 1 ATOM 380 O O . LEU A 1 45 ? -2.802 49.545 12.336 1.00 57.99 ? 48 LEU A O 1 ATOM 381 C CB . LEU A 1 45 ? -4.143 47.272 13.044 1.00 54.12 ? 48 LEU A CB 1 ATOM 382 C CG . LEU A 1 45 ? -4.235 45.953 13.808 1.00 55.69 ? 48 LEU A CG 1 ATOM 383 C CD1 . LEU A 1 45 ? -5.245 46.052 14.925 1.00 55.16 ? 48 LEU A CD1 1 ATOM 384 C CD2 . LEU A 1 45 ? -4.602 44.849 12.847 1.00 57.80 ? 48 LEU A CD2 1 ATOM 385 N N . TYR A 1 46 ? -2.998 50.542 14.346 1.00 54.41 ? 49 TYR A N 1 ATOM 386 C CA . TYR A 1 46 ? -2.166 51.698 14.015 1.00 52.95 ? 49 TYR A CA 1 ATOM 387 C C . TYR A 1 46 ? -0.709 51.467 13.684 1.00 52.84 ? 49 TYR A C 1 ATOM 388 O O . TYR A 1 46 ? -0.070 50.567 14.222 1.00 55.12 ? 49 TYR A O 1 ATOM 389 C CB . TYR A 1 46 ? -2.228 52.725 15.142 1.00 53.25 ? 49 TYR A CB 1 ATOM 390 C CG . TYR A 1 46 ? -3.548 53.434 15.248 1.00 56.31 ? 49 TYR A CG 1 ATOM 391 C CD1 . TYR A 1 46 ? -4.102 54.079 14.144 1.00 57.78 ? 49 TYR A CD1 1 ATOM 392 C CD2 . TYR A 1 46 ? -4.260 53.448 16.447 1.00 58.48 ? 49 TYR A CD2 1 ATOM 393 C CE1 . TYR A 1 46 ? -5.348 54.723 14.226 1.00 59.62 ? 49 TYR A CE1 1 ATOM 394 C CE2 . TYR A 1 46 ? -5.506 54.087 16.544 1.00 60.88 ? 49 TYR A CE2 1 ATOM 395 C CZ . TYR A 1 46 ? -6.046 54.722 15.427 1.00 60.98 ? 49 TYR A CZ 1 ATOM 396 O OH . TYR A 1 46 ? -7.285 55.330 15.499 1.00 62.67 ? 49 TYR A OH 1 ATOM 397 N N . VAL A 1 47 ? -0.190 52.318 12.803 1.00 51.02 ? 50 VAL A N 1 ATOM 398 C CA . VAL A 1 47 ? 1.204 52.279 12.387 1.00 49.75 ? 50 VAL A CA 1 ATOM 399 C C . VAL A 1 47 ? 1.656 53.724 12.262 1.00 51.35 ? 50 VAL A C 1 ATOM 400 O O . VAL A 1 47 ? 0.924 54.572 11.760 1.00 52.41 ? 50 VAL A O 1 ATOM 401 C CB . VAL A 1 47 ? 1.389 51.627 11.007 1.00 47.25 ? 50 VAL A CB 1 ATOM 402 C CG1 . VAL A 1 47 ? 2.865 51.573 10.662 1.00 44.71 ? 50 VAL A CG1 1 ATOM 403 C CG2 . VAL A 1 47 ? 0.766 50.261 10.985 1.00 44.91 ? 50 VAL A CG2 1 ATOM 404 N N . MET A 1 48 ? 2.863 54.009 12.713 1.00 51.79 ? 51 MET A N 1 ATOM 405 C CA . MET A 1 48 ? 3.375 55.353 12.620 1.00 53.13 ? 51 MET A CA 1 ATOM 406 C C . MET A 1 48 ? 4.519 55.366 11.659 1.00 54.32 ? 51 MET A C 1 ATOM 407 O O . MET A 1 48 ? 5.571 54.789 11.916 1.00 56.45 ? 51 MET A O 1 ATOM 408 C CB . MET A 1 48 ? 3.866 55.844 13.968 1.00 54.62 ? 51 MET A CB 1 ATOM 409 C CG . MET A 1 48 ? 2.967 56.874 14.610 1.00 60.24 ? 51 MET A CG 1 ATOM 410 S SD . MET A 1 48 ? 3.321 58.550 14.092 1.00 61.12 ? 51 MET A SD 1 ATOM 411 C CE . MET A 1 48 ? 2.663 58.519 12.504 1.00 60.29 ? 51 MET A CE 1 ATOM 412 N N . GLU A 1 49 ? 4.307 56.017 10.533 1.00 54.49 ? 52 GLU A N 1 ATOM 413 C CA . GLU A 1 49 ? 5.351 56.131 9.548 1.00 52.79 ? 52 GLU A CA 1 ATOM 414 C C . GLU A 1 49 ? 6.201 57.329 9.981 1.00 54.04 ? 52 GLU A C 1 ATOM 415 O O . GLU A 1 49 ? 5.663 58.374 10.345 1.00 55.06 ? 52 GLU A O 1 ATOM 416 C CB . GLU A 1 49 ? 4.724 56.390 8.192 1.00 51.49 ? 52 GLU A CB 1 ATOM 417 C CG . GLU A 1 49 ? 5.695 56.306 7.060 1.00 52.17 ? 52 GLU A CG 1 ATOM 418 C CD . GLU A 1 49 ? 5.131 56.862 5.771 1.00 52.65 ? 52 GLU A CD 1 ATOM 419 O OE1 . GLU A 1 49 ? 3.970 56.526 5.402 1.00 51.24 ? 52 GLU A OE1 1 ATOM 420 O OE2 . GLU A 1 49 ? 5.871 57.635 5.126 1.00 53.70 ? 52 GLU A OE2 1 ATOM 421 N N . ILE A 1 50 ? 7.518 57.178 9.971 1.00 53.57 ? 53 ILE A N 1 ATOM 422 C CA . ILE A 1 50 ? 8.400 58.270 10.347 1.00 53.22 ? 53 ILE A CA 1 ATOM 423 C C . ILE A 1 50 ? 9.460 58.374 9.280 1.00 56.75 ? 53 ILE A C 1 ATOM 424 O O . ILE A 1 50 ? 10.369 57.564 9.219 1.00 57.17 ? 53 ILE A O 1 ATOM 425 C CB . ILE A 1 50 ? 9.088 58.019 11.694 1.00 50.13 ? 53 ILE A CB 1 ATOM 426 C CG1 . ILE A 1 50 ? 8.045 57.934 12.806 1.00 47.49 ? 53 ILE A CG1 1 ATOM 427 C CG2 . ILE A 1 50 ? 10.103 59.116 11.972 1.00 46.35 ? 53 ILE A CG2 1 ATOM 428 C CD1 . ILE A 1 50 ? 8.668 57.691 14.152 1.00 44.61 ? 53 ILE A CD1 1 ATOM 429 N N . SER A 1 51 ? 9.316 59.372 8.427 1.00 61.01 ? 54 SER A N 1 ATOM 430 C CA . SER A 1 51 ? 10.243 59.622 7.335 1.00 65.66 ? 54 SER A CA 1 ATOM 431 C C . SER A 1 51 ? 10.238 61.120 7.165 1.00 69.00 ? 54 SER A C 1 ATOM 432 O O . SER A 1 51 ? 9.297 61.780 7.597 1.00 70.91 ? 54 SER A O 1 ATOM 433 C CB . SER A 1 51 ? 9.744 58.978 6.029 1.00 66.01 ? 54 SER A CB 1 ATOM 434 O OG . SER A 1 51 ? 10.520 59.388 4.900 1.00 64.59 ? 54 SER A OG 1 ATOM 435 N N . ASP A 1 52 ? 11.283 61.663 6.549 1.00 71.92 ? 55 ASP A N 1 ATOM 436 C CA . ASP A 1 52 ? 11.335 63.099 6.308 1.00 74.10 ? 55 ASP A CA 1 ATOM 437 C C . ASP A 1 52 ? 10.503 63.339 5.064 1.00 75.09 ? 55 ASP A C 1 ATOM 438 O O . ASP A 1 52 ? 10.505 64.426 4.505 1.00 77.58 ? 55 ASP A O 1 ATOM 439 C CB . ASP A 1 52 ? 12.771 63.574 6.083 1.00 74.83 ? 55 ASP A CB 1 ATOM 440 C CG . ASP A 1 52 ? 13.437 62.884 4.912 1.00 78.87 ? 55 ASP A CG 1 ATOM 441 O OD1 . ASP A 1 52 ? 13.151 61.681 4.665 1.00 80.63 ? 55 ASP A OD1 1 ATOM 442 O OD2 . ASP A 1 52 ? 14.264 63.546 4.249 1.00 80.15 ? 55 ASP A OD2 1 ATOM 443 N N . ASN A 1 53 ? 9.795 62.298 4.640 1.00 74.90 ? 56 ASN A N 1 ATOM 444 C CA . ASN A 1 53 ? 8.925 62.365 3.476 1.00 75.06 ? 56 ASN A CA 1 ATOM 445 C C . ASN A 1 53 ? 7.792 61.380 3.704 1.00 74.53 ? 56 ASN A C 1 ATOM 446 O O . ASN A 1 53 ? 7.587 60.437 2.935 1.00 75.31 ? 56 ASN A O 1 ATOM 447 C CB . ASN A 1 53 ? 9.703 62.003 2.224 1.00 77.15 ? 56 ASN A CB 1 ATOM 448 C CG . ASN A 1 53 ? 9.947 63.199 1.336 1.00 78.40 ? 56 ASN A CG 1 ATOM 449 O OD1 . ASN A 1 53 ? 9.007 63.768 0.768 1.00 80.31 ? 56 ASN A OD1 1 ATOM 450 N ND2 . ASN A 1 53 ? 11.210 63.598 1.213 1.00 77.37 ? 56 ASN A ND2 1 ATOM 451 N N . PRO A 1 54 ? 7.023 61.604 4.774 1.00 73.00 ? 57 PRO A N 1 ATOM 452 C CA . PRO A 1 54 ? 5.901 60.749 5.145 1.00 71.74 ? 57 PRO A CA 1 ATOM 453 C C . PRO A 1 54 ? 4.876 60.517 4.054 1.00 70.71 ? 57 PRO A C 1 ATOM 454 O O . PRO A 1 54 ? 4.415 61.455 3.423 1.00 71.38 ? 57 PRO A O 1 ATOM 455 C CB . PRO A 1 54 ? 5.318 61.468 6.360 1.00 70.84 ? 57 PRO A CB 1 ATOM 456 C CG . PRO A 1 54 ? 5.602 62.891 6.059 1.00 71.15 ? 57 PRO A CG 1 ATOM 457 C CD . PRO A 1 54 ? 7.017 62.839 5.578 1.00 71.83 ? 57 PRO A CD 1 ATOM 458 N N . GLY A 1 55 ? 4.531 59.253 3.839 1.00 69.89 ? 58 GLY A N 1 ATOM 459 C CA . GLY A 1 55 ? 3.529 58.913 2.852 1.00 70.30 ? 58 GLY A CA 1 ATOM 460 C C . GLY A 1 55 ? 4.047 58.407 1.528 1.00 71.53 ? 58 GLY A C 1 ATOM 461 O O . GLY A 1 55 ? 3.328 57.723 0.807 1.00 71.73 ? 58 GLY A O 1 ATOM 462 N N . ILE A 1 56 ? 5.286 58.732 1.190 1.00 73.29 ? 59 ILE A N 1 ATOM 463 C CA . ILE A 1 56 ? 5.821 58.285 -0.085 1.00 74.46 ? 59 ILE A CA 1 ATOM 464 C C . ILE A 1 56 ? 7.076 57.451 -0.008 1.00 74.93 ? 59 ILE A C 1 ATOM 465 O O . ILE A 1 56 ? 7.992 57.696 0.805 1.00 73.57 ? 59 ILE A O 1 ATOM 466 C CB . ILE A 1 56 ? 6.145 59.459 -1.028 1.00 75.09 ? 59 ILE A CB 1 ATOM 467 C CG1 . ILE A 1 56 ? 7.114 60.424 -0.340 1.00 77.09 ? 59 ILE A CG1 1 ATOM 468 C CG2 . ILE A 1 56 ? 4.872 60.143 -1.452 1.00 74.11 ? 59 ILE A CG2 1 ATOM 469 C CD1 . ILE A 1 56 ? 8.057 61.148 -1.293 1.00 79.57 ? 59 ILE A CD1 1 ATOM 470 N N . HIS A 1 57 ? 7.112 56.459 -0.886 1.00 75.19 ? 60 HIS A N 1 ATOM 471 C CA . HIS A 1 57 ? 8.266 55.599 -0.968 1.00 75.26 ? 60 HIS A CA 1 ATOM 472 C C . HIS A 1 57 ? 9.157 56.217 -2.009 1.00 74.61 ? 60 HIS A C 1 ATOM 473 O O . HIS A 1 57 ? 8.812 56.219 -3.187 1.00 75.56 ? 60 HIS A O 1 ATOM 474 C CB . HIS A 1 57 ? 7.896 54.189 -1.432 1.00 75.15 ? 60 HIS A CB 1 ATOM 475 C CG . HIS A 1 57 ? 9.059 53.436 -1.992 1.00 74.76 ? 60 HIS A CG 1 ATOM 476 N ND1 . HIS A 1 57 ? 10.203 53.187 -1.262 1.00 74.26 ? 60 HIS A ND1 1 ATOM 477 C CD2 . HIS A 1 57 ? 9.300 52.971 -3.238 1.00 74.39 ? 60 HIS A CD2 1 ATOM 478 C CE1 . HIS A 1 57 ? 11.099 52.605 -2.036 1.00 73.31 ? 60 HIS A CE1 1 ATOM 479 N NE2 . HIS A 1 57 ? 10.575 52.462 -3.242 1.00 74.68 ? 60 HIS A NE2 1 ATOM 480 N N . GLU A 1 58 ? 10.281 56.779 -1.601 1.00 73.66 ? 61 GLU A N 1 ATOM 481 C CA . GLU A 1 58 ? 11.138 57.297 -2.630 1.00 74.39 ? 61 GLU A CA 1 ATOM 482 C C . GLU A 1 58 ? 12.150 56.231 -3.022 1.00 75.15 ? 61 GLU A C 1 ATOM 483 O O . GLU A 1 58 ? 12.584 55.414 -2.200 1.00 74.91 ? 61 GLU A O 1 ATOM 484 C CB . GLU A 1 58 ? 11.800 58.600 -2.221 1.00 73.99 ? 61 GLU A CB 1 ATOM 485 C CG . GLU A 1 58 ? 12.189 58.731 -0.799 1.00 77.60 ? 61 GLU A CG 1 ATOM 486 C CD . GLU A 1 58 ? 11.990 60.162 -0.341 1.00 79.51 ? 61 GLU A CD 1 ATOM 487 O OE1 . GLU A 1 58 ? 11.191 60.868 -1.004 1.00 77.58 ? 61 GLU A OE1 1 ATOM 488 O OE2 . GLU A 1 58 ? 12.612 60.573 0.670 1.00 81.12 ? 61 GLU A OE2 1 ATOM 489 N N . ALA A 1 59 ? 12.472 56.235 -4.312 1.00 75.46 ? 62 ALA A N 1 ATOM 490 C CA . ALA A 1 59 ? 13.379 55.285 -4.933 1.00 74.25 ? 62 ALA A CA 1 ATOM 491 C C . ALA A 1 59 ? 14.758 55.181 -4.307 1.00 74.02 ? 62 ALA A C 1 ATOM 492 O O . ALA A 1 59 ? 15.497 56.167 -4.225 1.00 72.54 ? 62 ALA A O 1 ATOM 493 C CB . ALA A 1 59 ? 13.502 55.613 -6.406 1.00 73.66 ? 62 ALA A CB 1 ATOM 494 N N . GLY A 1 60 ? 15.103 53.966 -3.888 1.00 73.42 ? 63 GLY A N 1 ATOM 495 C CA . GLY A 1 60 ? 16.397 53.734 -3.281 1.00 73.97 ? 63 GLY A CA 1 ATOM 496 C C . GLY A 1 60 ? 16.382 53.931 -1.776 1.00 74.51 ? 63 GLY A C 1 ATOM 497 O O . GLY A 1 60 ? 17.411 53.720 -1.111 1.00 76.32 ? 63 GLY A O 1 ATOM 498 N N . GLU A 1 61 ? 15.232 54.359 -1.241 1.00 73.59 ? 64 GLU A N 1 ATOM 499 C CA . GLU A 1 61 ? 15.070 54.568 0.202 1.00 69.78 ? 64 GLU A CA 1 ATOM 500 C C . GLU A 1 61 ? 14.461 53.267 0.712 1.00 66.08 ? 64 GLU A C 1 ATOM 501 O O . GLU A 1 61 ? 13.352 52.889 0.314 1.00 64.89 ? 64 GLU A O 1 ATOM 502 C CB . GLU A 1 61 ? 14.135 55.748 0.497 1.00 70.44 ? 64 GLU A CB 1 ATOM 503 C CG . GLU A 1 61 ? 14.345 56.349 1.882 1.00 73.91 ? 64 GLU A CG 1 ATOM 504 C CD . GLU A 1 61 ? 13.182 57.222 2.332 1.00 77.48 ? 64 GLU A CD 1 ATOM 505 O OE1 . GLU A 1 61 ? 12.018 56.860 2.017 1.00 78.01 ? 64 GLU A OE1 1 ATOM 506 O OE2 . GLU A 1 61 ? 13.429 58.251 3.012 1.00 78.52 ? 64 GLU A OE2 1 ATOM 507 N N . PRO A 1 62 ? 15.198 52.557 1.584 1.00 62.54 ? 65 PRO A N 1 ATOM 508 C CA . PRO A 1 62 ? 14.810 51.283 2.185 1.00 60.54 ? 65 PRO A CA 1 ATOM 509 C C . PRO A 1 62 ? 13.637 51.440 3.128 1.00 60.22 ? 65 PRO A C 1 ATOM 510 O O . PRO A 1 62 ? 13.581 52.390 3.919 1.00 59.66 ? 65 PRO A O 1 ATOM 511 C CB . PRO A 1 62 ? 16.065 50.857 2.939 1.00 59.33 ? 65 PRO A CB 1 ATOM 512 C CG . PRO A 1 62 ? 17.172 51.713 2.360 1.00 59.09 ? 65 PRO A CG 1 ATOM 513 C CD . PRO A 1 62 ? 16.482 53.007 2.141 1.00 60.94 ? 65 PRO A CD 1 ATOM 514 N N . GLU A 1 63 ? 12.702 50.502 3.053 1.00 59.54 ? 66 GLU A N 1 ATOM 515 C CA . GLU A 1 63 ? 11.533 50.536 3.926 1.00 57.81 ? 66 GLU A CA 1 ATOM 516 C C . GLU A 1 63 ? 11.711 49.575 5.105 1.00 55.81 ? 66 GLU A C 1 ATOM 517 O O . GLU A 1 63 ? 11.945 48.383 4.922 1.00 55.68 ? 66 GLU A O 1 ATOM 518 C CB . GLU A 1 63 ? 10.290 50.173 3.127 1.00 58.52 ? 66 GLU A CB 1 ATOM 519 C CG . GLU A 1 63 ? 10.031 51.102 1.962 1.00 57.68 ? 66 GLU A CG 1 ATOM 520 C CD . GLU A 1 63 ? 8.787 51.937 2.155 1.00 59.27 ? 66 GLU A CD 1 ATOM 521 O OE1 . GLU A 1 63 ? 8.088 51.774 3.175 1.00 60.24 ? 66 GLU A OE1 1 ATOM 522 O OE2 . GLU A 1 63 ? 8.502 52.761 1.274 1.00 62.65 ? 66 GLU A OE2 1 ATOM 523 N N . PHE A 1 64 ? 11.575 50.110 6.312 1.00 53.66 ? 67 PHE A N 1 ATOM 524 C CA . PHE A 1 64 ? 11.755 49.350 7.542 1.00 51.21 ? 67 PHE A CA 1 ATOM 525 C C . PHE A 1 64 ? 10.520 49.306 8.438 1.00 50.89 ? 67 PHE A C 1 ATOM 526 O O . PHE A 1 64 ? 9.746 50.265 8.497 1.00 52.17 ? 67 PHE A O 1 ATOM 527 C CB . PHE A 1 64 ? 12.897 49.969 8.327 1.00 50.30 ? 67 PHE A CB 1 ATOM 528 C CG . PHE A 1 64 ? 13.150 49.309 9.622 1.00 50.51 ? 67 PHE A CG 1 ATOM 529 C CD1 . PHE A 1 64 ? 12.385 49.629 10.734 1.00 50.43 ? 67 PHE A CD1 1 ATOM 530 C CD2 . PHE A 1 64 ? 14.170 48.378 9.747 1.00 52.80 ? 67 PHE A CD2 1 ATOM 531 C CE1 . PHE A 1 64 ? 12.630 49.039 11.960 1.00 50.73 ? 67 PHE A CE1 1 ATOM 532 C CE2 . PHE A 1 64 ? 14.433 47.776 10.973 1.00 53.13 ? 67 PHE A CE2 1 ATOM 533 C CZ . PHE A 1 64 ? 13.659 48.111 12.086 1.00 52.19 ? 67 PHE A CZ 1 ATOM 534 N N . LYS A 1 65 ? 10.347 48.211 9.169 1.00 49.45 ? 68 LYS A N 1 ATOM 535 C CA . LYS A 1 65 ? 9.197 48.113 10.053 1.00 47.25 ? 68 LYS A CA 1 ATOM 536 C C . LYS A 1 65 ? 9.475 47.378 11.345 1.00 47.00 ? 68 LYS A C 1 ATOM 537 O O . LYS A 1 65 ? 10.223 46.391 11.370 1.00 48.73 ? 68 LYS A O 1 ATOM 538 C CB . LYS A 1 65 ? 8.034 47.433 9.332 1.00 46.48 ? 68 LYS A CB 1 ATOM 539 C CG . LYS A 1 65 ? 8.109 45.918 9.229 1.00 44.59 ? 68 LYS A CG 1 ATOM 540 C CD . LYS A 1 65 ? 7.150 45.405 8.143 1.00 45.14 ? 68 LYS A CD 1 ATOM 541 C CE . LYS A 1 65 ? 6.793 43.942 8.314 1.00 43.98 ? 68 LYS A CE 1 ATOM 542 N NZ . LYS A 1 65 ? 7.968 43.058 8.513 1.00 47.75 ? 68 LYS A NZ 1 ATOM 543 N N . TYR A 1 66 ? 8.874 47.881 12.421 1.00 46.69 ? 69 TYR A N 1 ATOM 544 C CA . TYR A 1 66 ? 8.970 47.281 13.758 1.00 46.95 ? 69 TYR A CA 1 ATOM 545 C C . TYR A 1 66 ? 7.546 46.941 14.166 1.00 47.08 ? 69 TYR A C 1 ATOM 546 O O . TYR A 1 66 ? 6.643 47.769 14.017 1.00 48.59 ? 69 TYR A O 1 ATOM 547 C CB . TYR A 1 66 ? 9.482 48.268 14.802 1.00 46.31 ? 69 TYR A CB 1 ATOM 548 C CG . TYR A 1 66 ? 10.944 48.211 15.123 1.00 45.36 ? 69 TYR A CG 1 ATOM 549 C CD1 . TYR A 1 66 ? 11.580 47.006 15.406 1.00 46.82 ? 69 TYR A CD1 1 ATOM 550 C CD2 . TYR A 1 66 ? 11.681 49.376 15.221 1.00 47.03 ? 69 TYR A CD2 1 ATOM 551 C CE1 . TYR A 1 66 ? 12.935 46.975 15.787 1.00 47.62 ? 69 TYR A CE1 1 ATOM 552 C CE2 . TYR A 1 66 ? 13.023 49.361 15.601 1.00 49.04 ? 69 TYR A CE2 1 ATOM 553 C CZ . TYR A 1 66 ? 13.645 48.165 15.883 1.00 47.76 ? 69 TYR A CZ 1 ATOM 554 O OH . TYR A 1 66 ? 14.968 48.181 16.273 1.00 46.75 ? 69 TYR A OH 1 ATOM 555 N N . ILE A 1 67 ? 7.331 45.745 14.689 1.00 46.14 ? 70 ILE A N 1 ATOM 556 C CA . ILE A 1 67 ? 5.995 45.382 15.131 1.00 46.03 ? 70 ILE A CA 1 ATOM 557 C C . ILE A 1 67 ? 6.039 44.871 16.566 1.00 47.52 ? 70 ILE A C 1 ATOM 558 O O . ILE A 1 67 ? 6.927 44.089 16.930 1.00 48.84 ? 70 ILE A O 1 ATOM 559 C CB . ILE A 1 67 ? 5.415 44.316 14.233 1.00 45.04 ? 70 ILE A CB 1 ATOM 560 C CG1 . ILE A 1 67 ? 5.467 44.802 12.791 1.00 42.30 ? 70 ILE A CG1 1 ATOM 561 C CG2 . ILE A 1 67 ? 4.000 44.005 14.661 1.00 42.84 ? 70 ILE A CG2 1 ATOM 562 C CD1 . ILE A 1 67 ? 5.145 43.736 11.788 1.00 47.58 ? 70 ILE A CD1 1 ATOM 563 N N . GLY A 1 68 ? 5.097 45.314 17.390 1.00 46.77 ? 71 GLY A N 1 ATOM 564 C CA . GLY A 1 68 ? 5.109 44.850 18.761 1.00 47.12 ? 71 GLY A CA 1 ATOM 565 C C . GLY A 1 68 ? 3.768 44.410 19.299 1.00 48.72 ? 71 GLY A C 1 ATOM 566 O O . GLY A 1 68 ? 2.732 44.676 18.690 1.00 48.28 ? 71 GLY A O 1 ATOM 567 N N . ASN A 1 69 ? 3.801 43.707 20.430 1.00 50.58 ? 72 ASN A N 1 ATOM 568 C CA . ASN A 1 69 ? 2.590 43.267 21.118 1.00 51.88 ? 72 ASN A CA 1 ATOM 569 C C . ASN A 1 69 ? 1.672 42.337 20.308 1.00 51.66 ? 72 ASN A C 1 ATOM 570 O O . ASN A 1 69 ? 0.453 42.471 20.320 1.00 52.74 ? 72 ASN A O 1 ATOM 571 C CB . ASN A 1 69 ? 1.817 44.513 21.567 1.00 53.33 ? 72 ASN A CB 1 ATOM 572 C CG . ASN A 1 69 ? 0.834 44.234 22.675 1.00 52.90 ? 72 ASN A CG 1 ATOM 573 O OD1 . ASN A 1 69 ? -0.066 45.030 22.934 1.00 53.96 ? 72 ASN A OD1 1 ATOM 574 N ND2 . ASN A 1 69 ? 1.006 43.108 23.347 1.00 54.49 ? 72 ASN A ND2 1 ATOM 575 N N . MET A 1 70 ? 2.268 41.391 19.601 1.00 52.73 ? 73 MET A N 1 ATOM 576 C CA . MET A 1 70 ? 1.524 40.414 18.810 1.00 51.67 ? 73 MET A CA 1 ATOM 577 C C . MET A 1 70 ? 0.742 39.547 19.806 1.00 52.64 ? 73 MET A C 1 ATOM 578 O O . MET A 1 70 ? -0.400 39.128 19.556 1.00 52.11 ? 73 MET A O 1 ATOM 579 C CB . MET A 1 70 ? 2.535 39.569 18.072 1.00 50.88 ? 73 MET A CB 1 ATOM 580 C CG . MET A 1 70 ? 1.989 38.713 16.993 1.00 54.46 ? 73 MET A CG 1 ATOM 581 S SD . MET A 1 70 ? 3.323 37.709 16.392 1.00 53.70 ? 73 MET A SD 1 ATOM 582 C CE . MET A 1 70 ? 4.721 38.706 16.912 1.00 49.05 ? 73 MET A CE 1 ATOM 583 N N . HIS A 1 71 ? 1.409 39.269 20.930 1.00 52.67 ? 74 HIS A N 1 ATOM 584 C CA . HIS A 1 71 ? 0.860 38.499 22.046 1.00 50.65 ? 74 HIS A CA 1 ATOM 585 C C . HIS A 1 71 ? 0.422 39.558 23.032 1.00 50.02 ? 74 HIS A C 1 ATOM 586 O O . HIS A 1 71 ? 1.256 40.291 23.555 1.00 50.16 ? 74 HIS A O 1 ATOM 587 C CB . HIS A 1 71 ? 1.942 37.639 22.698 1.00 49.33 ? 74 HIS A CB 1 ATOM 588 C CG . HIS A 1 71 ? 2.347 36.457 21.879 1.00 47.03 ? 74 HIS A CG 1 ATOM 589 N ND1 . HIS A 1 71 ? 3.663 36.076 21.768 1.00 45.44 ? 74 HIS A ND1 1 ATOM 590 C CD2 . HIS A 1 71 ? 1.568 35.624 21.142 1.00 44.33 ? 74 HIS A CD2 1 ATOM 591 C CE1 . HIS A 1 71 ? 3.660 35.029 20.967 1.00 45.99 ? 74 HIS A CE1 1 ATOM 592 N NE2 . HIS A 1 71 ? 2.411 34.716 20.560 1.00 44.36 ? 74 HIS A NE2 1 ATOM 593 N N . GLY A 1 72 ? -0.883 39.628 23.279 1.00 49.27 ? 75 GLY A N 1 ATOM 594 C CA . GLY A 1 72 ? -1.453 40.623 24.170 1.00 46.47 ? 75 GLY A CA 1 ATOM 595 C C . GLY A 1 72 ? -0.744 40.926 25.469 1.00 46.38 ? 75 GLY A C 1 ATOM 596 O O . GLY A 1 72 ? -0.517 42.092 25.776 1.00 45.79 ? 75 GLY A O 1 ATOM 597 N N . ASN A 1 73 ? -0.387 39.898 26.231 1.00 47.93 ? 76 ASN A N 1 ATOM 598 C CA . ASN A 1 73 ? 0.261 40.120 27.520 1.00 50.72 ? 76 ASN A CA 1 ATOM 599 C C . ASN A 1 73 ? 1.760 40.424 27.515 1.00 51.27 ? 76 ASN A C 1 ATOM 600 O O . ASN A 1 73 ? 2.342 40.693 28.565 1.00 50.99 ? 76 ASN A O 1 ATOM 601 C CB . ASN A 1 73 ? -0.053 38.954 28.469 1.00 52.57 ? 76 ASN A CB 1 ATOM 602 C CG . ASN A 1 73 ? 0.488 37.619 27.985 1.00 54.74 ? 76 ASN A CG 1 ATOM 603 O OD1 . ASN A 1 73 ? 0.699 37.391 26.788 1.00 57.29 ? 76 ASN A OD1 1 ATOM 604 N ND2 . ASN A 1 73 ? 0.690 36.710 28.926 1.00 55.74 ? 76 ASN A ND2 1 ATOM 605 N N . GLU A 1 74 ? 2.382 40.392 26.338 1.00 51.67 ? 77 GLU A N 1 ATOM 606 C CA . GLU A 1 74 ? 3.804 40.708 26.200 1.00 50.28 ? 77 GLU A CA 1 ATOM 607 C C . GLU A 1 74 ? 3.813 42.198 25.856 1.00 51.21 ? 77 GLU A C 1 ATOM 608 O O . GLU A 1 74 ? 3.734 42.605 24.701 1.00 53.34 ? 77 GLU A O 1 ATOM 609 C CB . GLU A 1 74 ? 4.413 39.847 25.102 1.00 46.03 ? 77 GLU A CB 1 ATOM 610 C CG . GLU A 1 74 ? 4.184 38.385 25.371 1.00 45.15 ? 77 GLU A CG 1 ATOM 611 C CD . GLU A 1 74 ? 4.785 37.485 24.329 1.00 45.21 ? 77 GLU A CD 1 ATOM 612 O OE1 . GLU A 1 74 ? 5.371 37.982 23.337 1.00 44.14 ? 77 GLU A OE1 1 ATOM 613 O OE2 . GLU A 1 74 ? 4.663 36.259 24.515 1.00 47.22 ? 77 GLU A OE2 1 ATOM 614 N N . VAL A 1 75 ? 3.916 42.994 26.909 1.00 50.60 ? 78 VAL A N 1 ATOM 615 C CA . VAL A 1 75 ? 3.838 44.444 26.858 1.00 49.51 ? 78 VAL A CA 1 ATOM 616 C C . VAL A 1 75 ? 5.069 45.299 26.577 1.00 50.26 ? 78 VAL A C 1 ATOM 617 O O . VAL A 1 75 ? 4.957 46.380 25.984 1.00 48.19 ? 78 VAL A O 1 ATOM 618 C CB . VAL A 1 75 ? 3.219 44.916 28.189 1.00 49.78 ? 78 VAL A CB 1 ATOM 619 C CG1 . VAL A 1 75 ? 3.194 46.439 28.282 1.00 50.78 ? 78 VAL A CG1 1 ATOM 620 C CG2 . VAL A 1 75 ? 1.826 44.327 28.314 1.00 48.13 ? 78 VAL A CG2 1 ATOM 621 N N . VAL A 1 76 ? 6.235 44.838 27.016 1.00 50.87 ? 79 VAL A N 1 ATOM 622 C CA . VAL A 1 76 ? 7.438 45.634 26.852 1.00 50.24 ? 79 VAL A CA 1 ATOM 623 C C . VAL A 1 76 ? 7.573 46.193 25.442 1.00 51.38 ? 79 VAL A C 1 ATOM 624 O O . VAL A 1 76 ? 7.862 47.377 25.267 1.00 50.71 ? 79 VAL A O 1 ATOM 625 C CB . VAL A 1 76 ? 8.685 44.825 27.242 1.00 50.20 ? 79 VAL A CB 1 ATOM 626 C CG1 . VAL A 1 76 ? 9.878 45.743 27.368 1.00 51.19 ? 79 VAL A CG1 1 ATOM 627 C CG2 . VAL A 1 76 ? 8.447 44.110 28.558 1.00 48.72 ? 79 VAL A CG2 1 ATOM 628 N N . GLY A 1 77 ? 7.334 45.359 24.434 1.00 52.56 ? 80 GLY A N 1 ATOM 629 C CA . GLY A 1 77 ? 7.442 45.835 23.063 1.00 52.91 ? 80 GLY A CA 1 ATOM 630 C C . GLY A 1 77 ? 6.615 47.084 22.791 1.00 52.13 ? 80 GLY A C 1 ATOM 631 O O . GLY A 1 77 ? 7.133 48.126 22.401 1.00 53.86 ? 80 GLY A O 1 ATOM 632 N N . ARG A 1 78 ? 5.313 46.963 22.989 1.00 51.11 ? 81 ARG A N 1 ATOM 633 C CA . ARG A 1 78 ? 4.372 48.054 22.796 1.00 50.37 ? 81 ARG A CA 1 ATOM 634 C C . ARG A 1 78 ? 4.944 49.366 23.318 1.00 50.31 ? 81 ARG A C 1 ATOM 635 O O . ARG A 1 78 ? 5.062 50.344 22.583 1.00 51.26 ? 81 ARG A O 1 ATOM 636 C CB . ARG A 1 78 ? 3.090 47.703 23.550 1.00 51.17 ? 81 ARG A CB 1 ATOM 637 C CG . ARG A 1 78 ? 1.937 48.675 23.490 1.00 49.03 ? 81 ARG A CG 1 ATOM 638 C CD . ARG A 1 78 ? 0.849 48.157 24.432 1.00 49.40 ? 81 ARG A CD 1 ATOM 639 N NE . ARG A 1 78 ? -0.379 48.955 24.477 1.00 51.47 ? 81 ARG A NE 1 ATOM 640 C CZ . ARG A 1 78 ? -1.500 48.661 23.819 1.00 50.52 ? 81 ARG A CZ 1 ATOM 641 N NH1 . ARG A 1 78 ? -1.564 47.584 23.049 1.00 49.41 ? 81 ARG A NH1 1 ATOM 642 N NH2 . ARG A 1 78 ? -2.564 49.438 23.942 1.00 49.02 ? 81 ARG A NH2 1 ATOM 643 N N . GLU A 1 79 ? 5.327 49.380 24.586 1.00 49.90 ? 82 GLU A N 1 ATOM 644 C CA . GLU A 1 79 ? 5.838 50.600 25.192 1.00 50.59 ? 82 GLU A CA 1 ATOM 645 C C . GLU A 1 79 ? 7.135 51.112 24.588 1.00 52.13 ? 82 GLU A C 1 ATOM 646 O O . GLU A 1 79 ? 7.300 52.318 24.363 1.00 53.02 ? 82 GLU A O 1 ATOM 647 C CB . GLU A 1 79 ? 6.002 50.390 26.693 1.00 49.35 ? 82 GLU A CB 1 ATOM 648 C CG . GLU A 1 79 ? 4.738 49.868 27.334 1.00 48.72 ? 82 GLU A CG 1 ATOM 649 C CD . GLU A 1 79 ? 3.567 50.822 27.140 1.00 49.53 ? 82 GLU A CD 1 ATOM 650 O OE1 . GLU A 1 79 ? 3.823 52.003 26.776 1.00 44.95 ? 82 GLU A OE1 1 ATOM 651 O OE2 . GLU A 1 79 ? 2.403 50.381 27.358 1.00 50.84 ? 82 GLU A OE2 1 ATOM 652 N N . LEU A 1 80 ? 8.061 50.204 24.321 1.00 52.32 ? 83 LEU A N 1 ATOM 653 C CA . LEU A 1 80 ? 9.329 50.608 23.749 1.00 51.19 ? 83 LEU A CA 1 ATOM 654 C C . LEU A 1 80 ? 9.127 51.292 22.415 1.00 51.05 ? 83 LEU A C 1 ATOM 655 O O . LEU A 1 80 ? 9.781 52.293 22.123 1.00 52.65 ? 83 LEU A O 1 ATOM 656 C CB . LEU A 1 80 ? 10.245 49.402 23.580 1.00 51.18 ? 83 LEU A CB 1 ATOM 657 C CG . LEU A 1 80 ? 10.955 48.908 24.840 1.00 50.23 ? 83 LEU A CG 1 ATOM 658 C CD1 . LEU A 1 80 ? 11.658 47.618 24.532 1.00 53.03 ? 83 LEU A CD1 1 ATOM 659 C CD2 . LEU A 1 80 ? 11.956 49.935 25.325 1.00 50.53 ? 83 LEU A CD2 1 ATOM 660 N N . LEU A 1 81 ? 8.214 50.767 21.605 1.00 49.73 ? 84 LEU A N 1 ATOM 661 C CA . LEU A 1 81 ? 7.969 51.359 20.295 1.00 48.81 ? 84 LEU A CA 1 ATOM 662 C C . LEU A 1 81 ? 7.375 52.750 20.425 1.00 48.80 ? 84 LEU A C 1 ATOM 663 O O . LEU A 1 81 ? 7.639 53.621 19.592 1.00 48.28 ? 84 LEU A O 1 ATOM 664 C CB . LEU A 1 81 ? 7.076 50.445 19.449 1.00 48.02 ? 84 LEU A CB 1 ATOM 665 C CG . LEU A 1 81 ? 7.796 49.196 18.915 1.00 45.16 ? 84 LEU A CG 1 ATOM 666 C CD1 . LEU A 1 81 ? 6.834 48.305 18.153 1.00 43.91 ? 84 LEU A CD1 1 ATOM 667 C CD2 . LEU A 1 81 ? 8.940 49.623 18.012 1.00 44.85 ? 84 LEU A CD2 1 ATOM 668 N N . LEU A 1 82 ? 6.585 52.964 21.475 1.00 49.17 ? 85 LEU A N 1 ATOM 669 C CA . LEU A 1 82 ? 6.009 54.286 21.717 1.00 49.01 ? 85 LEU A CA 1 ATOM 670 C C . LEU A 1 82 ? 7.182 55.181 22.115 1.00 49.37 ? 85 LEU A C 1 ATOM 671 O O . LEU A 1 82 ? 7.371 56.266 21.558 1.00 48.89 ? 85 LEU A O 1 ATOM 672 C CB . LEU A 1 82 ? 4.971 54.234 22.845 1.00 47.99 ? 85 LEU A CB 1 ATOM 673 C CG . LEU A 1 82 ? 3.688 53.426 22.587 1.00 46.97 ? 85 LEU A CG 1 ATOM 674 C CD1 . LEU A 1 82 ? 2.868 53.350 23.861 1.00 47.09 ? 85 LEU A CD1 1 ATOM 675 C CD2 . LEU A 1 82 ? 2.877 54.074 21.484 1.00 47.33 ? 85 LEU A CD2 1 ATOM 676 N N . ASN A 1 83 ? 7.980 54.708 23.068 1.00 49.93 ? 86 ASN A N 1 ATOM 677 C CA . ASN A 1 83 ? 9.145 55.459 23.506 1.00 52.20 ? 86 ASN A CA 1 ATOM 678 C C . ASN A 1 83 ? 9.941 55.878 22.272 1.00 53.21 ? 86 ASN A C 1 ATOM 679 O O . ASN A 1 83 ? 10.437 57.004 22.192 1.00 55.51 ? 86 ASN A O 1 ATOM 680 C CB . ASN A 1 83 ? 10.025 54.596 24.413 1.00 53.53 ? 86 ASN A CB 1 ATOM 681 C CG . ASN A 1 83 ? 9.351 54.254 25.736 1.00 59.42 ? 86 ASN A CG 1 ATOM 682 O OD1 . ASN A 1 83 ? 9.839 53.410 26.498 1.00 60.35 ? 86 ASN A OD1 1 ATOM 683 N ND2 . ASN A 1 83 ? 8.230 54.915 26.021 1.00 61.86 ? 86 ASN A ND2 1 ATOM 684 N N . LEU A 1 84 ? 10.049 54.968 21.306 1.00 52.31 ? 87 LEU A N 1 ATOM 685 C CA . LEU A 1 84 ? 10.794 55.217 20.074 1.00 50.27 ? 87 LEU A CA 1 ATOM 686 C C . LEU A 1 84 ? 10.138 56.283 19.214 1.00 50.57 ? 87 LEU A C 1 ATOM 687 O O . LEU A 1 84 ? 10.810 57.206 18.754 1.00 50.41 ? 87 LEU A O 1 ATOM 688 C CB . LEU A 1 84 ? 10.921 53.924 19.276 1.00 49.88 ? 87 LEU A CB 1 ATOM 689 C CG . LEU A 1 84 ? 11.685 53.978 17.954 1.00 47.87 ? 87 LEU A CG 1 ATOM 690 C CD1 . LEU A 1 84 ? 13.082 54.509 18.163 1.00 45.61 ? 87 LEU A CD1 1 ATOM 691 C CD2 . LEU A 1 84 ? 11.748 52.593 17.377 1.00 48.26 ? 87 LEU A CD2 1 ATOM 692 N N . ILE A 1 85 ? 8.836 56.142 18.970 1.00 49.85 ? 88 ILE A N 1 ATOM 693 C CA . ILE A 1 85 ? 8.123 57.141 18.193 1.00 50.57 ? 88 ILE A CA 1 ATOM 694 C C . ILE A 1 85 ? 8.537 58.478 18.810 1.00 52.56 ? 88 ILE A C 1 ATOM 695 O O . ILE A 1 85 ? 9.032 59.355 18.118 1.00 54.79 ? 88 ILE A O 1 ATOM 696 C CB . ILE A 1 85 ? 6.594 57.021 18.344 1.00 50.23 ? 88 ILE A CB 1 ATOM 697 C CG1 . ILE A 1 85 ? 6.091 55.638 17.888 1.00 49.13 ? 88 ILE A CG1 1 ATOM 698 C CG2 . ILE A 1 85 ? 5.926 58.151 17.593 1.00 47.68 ? 88 ILE A CG2 1 ATOM 699 C CD1 . ILE A 1 85 ? 6.030 55.422 16.420 1.00 49.91 ? 88 ILE A CD1 1 ATOM 700 N N . GLU A 1 86 ? 8.355 58.618 20.123 1.00 53.75 ? 89 GLU A N 1 ATOM 701 C CA . GLU A 1 86 ? 8.726 59.857 20.822 1.00 55.04 ? 89 GLU A CA 1 ATOM 702 C C . GLU A 1 86 ? 10.167 60.232 20.500 1.00 54.93 ? 89 GLU A C 1 ATOM 703 O O . GLU A 1 86 ? 10.428 61.190 19.774 1.00 55.69 ? 89 GLU A O 1 ATOM 704 C CB . GLU A 1 86 ? 8.577 59.706 22.355 1.00 56.47 ? 89 GLU A CB 1 ATOM 705 C CG . GLU A 1 86 ? 8.672 61.042 23.143 1.00 61.31 ? 89 GLU A CG 1 ATOM 706 C CD . GLU A 1 86 ? 8.421 60.922 24.668 1.00 64.05 ? 89 GLU A CD 1 ATOM 707 O OE1 . GLU A 1 86 ? 7.547 60.131 25.096 1.00 66.65 ? 89 GLU A OE1 1 ATOM 708 O OE2 . GLU A 1 86 ? 9.085 61.644 25.447 1.00 62.69 ? 89 GLU A OE2 1 ATOM 709 N N . TYR A 1 87 ? 11.100 59.456 21.037 1.00 54.27 ? 90 TYR A N 1 ATOM 710 C CA . TYR A 1 87 ? 12.519 59.707 20.840 1.00 53.23 ? 90 TYR A CA 1 ATOM 711 C C . TYR A 1 87 ? 12.879 60.182 19.433 1.00 53.31 ? 90 TYR A C 1 ATOM 712 O O . TYR A 1 87 ? 13.675 61.110 19.274 1.00 52.03 ? 90 TYR A O 1 ATOM 713 C CB . TYR A 1 87 ? 13.325 58.453 21.181 1.00 51.52 ? 90 TYR A CB 1 ATOM 714 C CG . TYR A 1 87 ? 14.815 58.655 21.065 1.00 51.96 ? 90 TYR A CG 1 ATOM 715 C CD1 . TYR A 1 87 ? 15.571 59.093 22.145 1.00 51.54 ? 90 TYR A CD1 1 ATOM 716 C CD2 . TYR A 1 87 ? 15.469 58.403 19.865 1.00 53.95 ? 90 TYR A CD2 1 ATOM 717 C CE1 . TYR A 1 87 ? 16.955 59.271 22.030 1.00 54.46 ? 90 TYR A CE1 1 ATOM 718 C CE2 . TYR A 1 87 ? 16.843 58.576 19.732 1.00 55.72 ? 90 TYR A CE2 1 ATOM 719 C CZ . TYR A 1 87 ? 17.588 59.006 20.812 1.00 56.64 ? 90 TYR A CZ 1 ATOM 720 O OH . TYR A 1 87 ? 18.960 59.139 20.665 1.00 58.02 ? 90 TYR A OH 1 ATOM 721 N N . LEU A 1 88 ? 12.293 59.553 18.419 1.00 54.67 ? 91 LEU A N 1 ATOM 722 C CA . LEU A 1 88 ? 12.590 59.921 17.034 1.00 57.22 ? 91 LEU A CA 1 ATOM 723 C C . LEU A 1 88 ? 12.043 61.292 16.687 1.00 58.76 ? 91 LEU A C 1 ATOM 724 O O . LEU A 1 88 ? 12.783 62.160 16.211 1.00 61.41 ? 91 LEU A O 1 ATOM 725 C CB . LEU A 1 88 ? 12.027 58.880 16.063 1.00 55.51 ? 91 LEU A CB 1 ATOM 726 C CG . LEU A 1 88 ? 12.745 57.527 16.090 1.00 53.54 ? 91 LEU A CG 1 ATOM 727 C CD1 . LEU A 1 88 ? 12.036 56.574 15.155 1.00 52.93 ? 91 LEU A CD1 1 ATOM 728 C CD2 . LEU A 1 88 ? 14.201 57.699 15.691 1.00 49.52 ? 91 LEU A CD2 1 ATOM 729 N N . CYS A 1 89 ? 10.750 61.487 16.928 1.00 58.06 ? 92 CYS A N 1 ATOM 730 C CA . CYS A 1 89 ? 10.109 62.762 16.656 1.00 56.45 ? 92 CYS A CA 1 ATOM 731 C C . CYS A 1 89 ? 10.762 63.883 17.434 1.00 57.30 ? 92 CYS A C 1 ATOM 732 O O . CYS A 1 89 ? 10.985 64.962 16.905 1.00 59.13 ? 92 CYS A O 1 ATOM 733 C CB . CYS A 1 89 ? 8.639 62.707 17.028 1.00 54.44 ? 92 CYS A CB 1 ATOM 734 S SG . CYS A 1 89 ? 7.684 61.661 15.932 1.00 55.99 ? 92 CYS A SG 1 ATOM 735 N N . LYS A 1 90 ? 11.090 63.637 18.690 1.00 56.95 ? 93 LYS A N 1 ATOM 736 C CA . LYS A 1 90 ? 11.689 64.695 19.473 1.00 57.65 ? 93 LYS A CA 1 ATOM 737 C C . LYS A 1 90 ? 13.103 65.096 19.083 1.00 57.84 ? 93 LYS A C 1 ATOM 738 O O . LYS A 1 90 ? 13.439 66.276 19.112 1.00 59.78 ? 93 LYS A O 1 ATOM 739 C CB . LYS A 1 90 ? 11.613 64.345 20.959 1.00 58.13 ? 93 LYS A CB 1 ATOM 740 C CG . LYS A 1 90 ? 10.178 64.383 21.470 1.00 61.70 ? 93 LYS A CG 1 ATOM 741 C CD . LYS A 1 90 ? 10.090 64.403 22.989 1.00 63.50 ? 93 LYS A CD 1 ATOM 742 C CE . LYS A 1 90 ? 8.641 64.610 23.444 1.00 66.55 ? 93 LYS A CE 1 ATOM 743 N NZ . LYS A 1 90 ? 8.456 64.630 24.928 1.00 67.44 ? 93 LYS A NZ 1 ATOM 744 N N . ASN A 1 91 ? 13.937 64.145 18.695 1.00 58.18 ? 94 ASN A N 1 ATOM 745 C CA . ASN A 1 91 ? 15.297 64.510 18.341 1.00 58.29 ? 94 ASN A CA 1 ATOM 746 C C . ASN A 1 91 ? 15.518 64.820 16.875 1.00 58.95 ? 94 ASN A C 1 ATOM 747 O O . ASN A 1 91 ? 16.609 65.227 16.512 1.00 59.73 ? 94 ASN A O 1 ATOM 748 C CB . ASN A 1 91 ? 16.263 63.415 18.765 1.00 58.30 ? 94 ASN A CB 1 ATOM 749 C CG . ASN A 1 91 ? 16.384 63.296 20.265 1.00 60.52 ? 94 ASN A CG 1 ATOM 750 O OD1 . ASN A 1 91 ? 17.259 63.915 20.886 1.00 60.59 ? 94 ASN A OD1 1 ATOM 751 N ND2 . ASN A 1 91 ? 15.500 62.497 20.865 1.00 60.32 ? 94 ASN A ND2 1 ATOM 752 N N . PHE A 1 92 ? 14.517 64.635 16.020 1.00 60.17 ? 95 PHE A N 1 ATOM 753 C CA . PHE A 1 92 ? 14.728 64.930 14.601 1.00 63.62 ? 95 PHE A CA 1 ATOM 754 C C . PHE A 1 92 ? 15.068 66.398 14.395 1.00 64.82 ? 95 PHE A C 1 ATOM 755 O O . PHE A 1 92 ? 14.293 67.266 14.769 1.00 65.42 ? 95 PHE A O 1 ATOM 756 C CB . PHE A 1 92 ? 13.492 64.604 13.771 1.00 65.74 ? 95 PHE A CB 1 ATOM 757 C CG . PHE A 1 92 ? 13.696 64.788 12.277 1.00 70.15 ? 95 PHE A CG 1 ATOM 758 C CD1 . PHE A 1 92 ? 14.504 63.912 11.549 1.00 71.18 ? 95 PHE A CD1 1 ATOM 759 C CD2 . PHE A 1 92 ? 13.070 65.829 11.591 1.00 71.21 ? 95 PHE A CD2 1 ATOM 760 C CE1 . PHE A 1 92 ? 14.675 64.072 10.163 1.00 70.76 ? 95 PHE A CE1 1 ATOM 761 C CE2 . PHE A 1 92 ? 13.238 65.994 10.208 1.00 70.24 ? 95 PHE A CE2 1 ATOM 762 C CZ . PHE A 1 92 ? 14.037 65.115 9.498 1.00 70.86 ? 95 PHE A CZ 1 ATOM 763 N N . GLY A 1 93 ? 16.214 66.674 13.778 1.00 66.50 ? 96 GLY A N 1 ATOM 764 C CA . GLY A 1 93 ? 16.631 68.053 13.560 1.00 68.83 ? 96 GLY A CA 1 ATOM 765 C C . GLY A 1 93 ? 17.666 68.477 14.596 1.00 70.12 ? 96 GLY A C 1 ATOM 766 O O . GLY A 1 93 ? 18.720 69.010 14.273 1.00 71.39 ? 96 GLY A O 1 ATOM 767 N N . THR A 1 94 ? 17.348 68.220 15.856 1.00 71.19 ? 97 THR A N 1 ATOM 768 C CA . THR A 1 94 ? 18.205 68.536 16.987 1.00 71.31 ? 97 THR A CA 1 ATOM 769 C C . THR A 1 94 ? 19.381 67.570 17.046 1.00 71.73 ? 97 THR A C 1 ATOM 770 O O . THR A 1 94 ? 20.534 67.973 17.175 1.00 72.97 ? 97 THR A O 1 ATOM 771 C CB . THR A 1 94 ? 17.407 68.388 18.288 1.00 72.13 ? 97 THR A CB 1 ATOM 772 O OG1 . THR A 1 94 ? 16.265 69.252 18.240 1.00 73.85 ? 97 THR A OG1 1 ATOM 773 C CG2 . THR A 1 94 ? 18.272 68.710 19.501 1.00 73.74 ? 97 THR A CG2 1 ATOM 774 N N . ASP A 1 95 ? 19.071 66.282 16.964 1.00 71.89 ? 98 ASP A N 1 ATOM 775 C CA . ASP A 1 95 ? 20.080 65.233 17.029 1.00 70.55 ? 98 ASP A CA 1 ATOM 776 C C . ASP A 1 95 ? 20.518 64.762 15.650 1.00 69.61 ? 98 ASP A C 1 ATOM 777 O O . ASP A 1 95 ? 19.695 64.451 14.791 1.00 68.61 ? 98 ASP A O 1 ATOM 778 C CB . ASP A 1 95 ? 19.542 64.042 17.826 1.00 71.16 ? 98 ASP A CB 1 ATOM 779 C CG . ASP A 1 95 ? 20.541 62.903 17.933 1.00 72.02 ? 98 ASP A CG 1 ATOM 780 O OD1 . ASP A 1 95 ? 21.570 63.066 18.634 1.00 70.92 ? 98 ASP A OD1 1 ATOM 781 O OD2 . ASP A 1 95 ? 20.287 61.845 17.313 1.00 72.40 ? 98 ASP A OD2 1 ATOM 782 N N . PRO A 1 96 ? 21.835 64.704 15.428 1.00 69.39 ? 99 PRO A N 1 ATOM 783 C CA . PRO A 1 96 ? 22.406 64.267 14.152 1.00 67.51 ? 99 PRO A CA 1 ATOM 784 C C . PRO A 1 96 ? 22.058 62.826 13.762 1.00 64.67 ? 99 PRO A C 1 ATOM 785 O O . PRO A 1 96 ? 21.665 62.570 12.620 1.00 63.33 ? 99 PRO A O 1 ATOM 786 C CB . PRO A 1 96 ? 23.908 64.479 14.359 1.00 69.37 ? 99 PRO A CB 1 ATOM 787 C CG . PRO A 1 96 ? 24.083 64.350 15.866 1.00 69.79 ? 99 PRO A CG 1 ATOM 788 C CD . PRO A 1 96 ? 22.893 65.130 16.363 1.00 70.28 ? 99 PRO A CD 1 ATOM 789 N N . GLU A 1 97 ? 22.200 61.893 14.703 1.00 61.59 ? 100 GLU A N 1 ATOM 790 C CA . GLU A 1 97 ? 21.897 60.486 14.429 1.00 59.93 ? 100 GLU A CA 1 ATOM 791 C C . GLU A 1 97 ? 20.454 60.277 13.974 1.00 58.40 ? 100 GLU A C 1 ATOM 792 O O . GLU A 1 97 ? 20.206 59.670 12.926 1.00 58.32 ? 100 GLU A O 1 ATOM 793 C CB . GLU A 1 97 ? 22.156 59.617 15.675 1.00 61.51 ? 100 GLU A CB 1 ATOM 794 C CG . GLU A 1 97 ? 21.897 58.104 15.467 1.00 61.32 ? 100 GLU A CG 1 ATOM 795 C CD . GLU A 1 97 ? 22.226 57.233 16.686 1.00 60.40 ? 100 GLU A CD 1 ATOM 796 O OE1 . GLU A 1 97 ? 22.299 57.762 17.818 1.00 62.94 ? 100 GLU A OE1 1 ATOM 797 O OE2 . GLU A 1 97 ? 22.401 56.010 16.507 1.00 56.98 ? 100 GLU A OE2 1 ATOM 798 N N . VAL A 1 98 ? 19.512 60.777 14.773 1.00 56.05 ? 101 VAL A N 1 ATOM 799 C CA . VAL A 1 98 ? 18.090 60.635 14.482 1.00 54.37 ? 101 VAL A CA 1 ATOM 800 C C . VAL A 1 98 ? 17.715 61.256 13.156 1.00 55.83 ? 101 VAL A C 1 ATOM 801 O O . VAL A 1 98 ? 17.001 60.656 12.355 1.00 55.44 ? 101 VAL A O 1 ATOM 802 C CB . VAL A 1 98 ? 17.234 61.269 15.599 1.00 52.21 ? 101 VAL A CB 1 ATOM 803 C CG1 . VAL A 1 98 ? 15.761 61.307 15.194 1.00 50.38 ? 101 VAL A CG1 1 ATOM 804 C CG2 . VAL A 1 98 ? 17.415 60.468 16.886 1.00 51.16 ? 101 VAL A CG2 1 ATOM 805 N N . THR A 1 99 ? 18.206 62.466 12.932 1.00 59.80 ? 102 THR A N 1 ATOM 806 C CA . THR A 1 99 ? 17.931 63.196 11.699 1.00 63.33 ? 102 THR A CA 1 ATOM 807 C C . THR A 1 99 ? 18.403 62.401 10.493 1.00 64.46 ? 102 THR A C 1 ATOM 808 O O . THR A 1 99 ? 17.704 62.279 9.483 1.00 63.40 ? 102 THR A O 1 ATOM 809 C CB . THR A 1 99 ? 18.656 64.547 11.683 1.00 64.01 ? 102 THR A CB 1 ATOM 810 O OG1 . THR A 1 99 ? 18.349 65.269 12.882 1.00 65.12 ? 102 THR A OG1 1 ATOM 811 C CG2 . THR A 1 99 ? 18.216 65.358 10.479 1.00 63.93 ? 102 THR A CG2 1 ATOM 812 N N . ASP A 1 100 ? 19.606 61.865 10.605 1.00 66.78 ? 103 ASP A N 1 ATOM 813 C CA . ASP A 1 100 ? 20.161 61.081 9.533 1.00 69.24 ? 103 ASP A CA 1 ATOM 814 C C . ASP A 1 100 ? 19.274 59.870 9.250 1.00 68.43 ? 103 ASP A C 1 ATOM 815 O O . ASP A 1 100 ? 18.940 59.586 8.100 1.00 68.98 ? 103 ASP A O 1 ATOM 816 C CB . ASP A 1 100 ? 21.561 60.632 9.913 1.00 75.80 ? 103 ASP A CB 1 ATOM 817 C CG . ASP A 1 100 ? 22.225 59.848 8.810 1.00 83.80 ? 103 ASP A CG 1 ATOM 818 O OD1 . ASP A 1 100 ? 22.355 60.415 7.698 1.00 87.32 ? 103 ASP A OD1 1 ATOM 819 O OD2 . ASP A 1 100 ? 22.608 58.672 9.047 1.00 88.92 ? 103 ASP A OD2 1 ATOM 820 N N . LEU A 1 101 ? 18.890 59.167 10.308 1.00 67.01 ? 104 LEU A N 1 ATOM 821 C CA . LEU A 1 101 ? 18.040 57.988 10.193 1.00 66.28 ? 104 LEU A CA 1 ATOM 822 C C . LEU A 1 101 ? 16.696 58.243 9.529 1.00 65.83 ? 104 LEU A C 1 ATOM 823 O O . LEU A 1 101 ? 16.284 57.512 8.627 1.00 65.35 ? 104 LEU A O 1 ATOM 824 C CB . LEU A 1 101 ? 17.764 57.414 11.578 1.00 68.21 ? 104 LEU A CB 1 ATOM 825 C CG . LEU A 1 101 ? 18.446 56.122 12.005 1.00 69.13 ? 104 LEU A CG 1 ATOM 826 C CD1 . LEU A 1 101 ? 17.895 55.693 13.347 1.00 68.48 ? 104 LEU A CD1 1 ATOM 827 C CD2 . LEU A 1 101 ? 18.192 55.051 10.964 1.00 70.28 ? 104 LEU A CD2 1 ATOM 828 N N . VAL A 1 102 ? 16.000 59.266 10.005 1.00 65.10 ? 105 VAL A N 1 ATOM 829 C CA . VAL A 1 102 ? 14.691 59.583 9.477 1.00 65.52 ? 105 VAL A CA 1 ATOM 830 C C . VAL A 1 102 ? 14.766 60.045 8.042 1.00 68.22 ? 105 VAL A C 1 ATOM 831 O O . VAL A 1 102 ? 13.808 59.895 7.281 1.00 71.01 ? 105 VAL A O 1 ATOM 832 C CB . VAL A 1 102 ? 14.012 60.654 10.321 1.00 64.63 ? 105 VAL A CB 1 ATOM 833 C CG1 . VAL A 1 102 ? 12.615 60.961 9.771 1.00 63.95 ? 105 VAL A CG1 1 ATOM 834 C CG2 . VAL A 1 102 ? 13.933 60.173 11.754 1.00 62.76 ? 105 VAL A CG2 1 ATOM 835 N N . GLN A 1 103 ? 15.902 60.602 7.652 1.00 68.23 ? 106 GLN A N 1 ATOM 836 C CA . GLN A 1 103 ? 16.037 61.059 6.276 1.00 68.79 ? 106 GLN A CA 1 ATOM 837 C C . GLN A 1 103 ? 16.331 59.921 5.285 1.00 67.94 ? 106 GLN A C 1 ATOM 838 O O . GLN A 1 103 ? 15.670 59.798 4.243 1.00 68.07 ? 106 GLN A O 1 ATOM 839 C CB . GLN A 1 103 ? 17.107 62.144 6.211 1.00 70.27 ? 106 GLN A CB 1 ATOM 840 C CG . GLN A 1 103 ? 16.598 63.456 6.786 1.00 70.79 ? 106 GLN A CG 1 ATOM 841 C CD . GLN A 1 103 ? 17.637 64.567 6.832 1.00 71.66 ? 106 GLN A CD 1 ATOM 842 O OE1 . GLN A 1 103 ? 17.277 65.735 6.954 1.00 73.03 ? 106 GLN A OE1 1 ATOM 843 N NE2 . GLN A 1 103 ? 18.923 64.213 6.751 1.00 70.36 ? 106 GLN A NE2 1 ATOM 844 N N . SER A 1 104 ? 17.296 59.076 5.638 1.00 65.61 ? 107 SER A N 1 ATOM 845 C CA . SER A 1 104 ? 17.709 57.940 4.816 1.00 63.81 ? 107 SER A CA 1 ATOM 846 C C . SER A 1 104 ? 16.775 56.712 4.783 1.00 61.74 ? 107 SER A C 1 ATOM 847 O O . SER A 1 104 ? 16.847 55.900 3.849 1.00 61.81 ? 107 SER A O 1 ATOM 848 C CB . SER A 1 104 ? 19.090 57.492 5.278 1.00 64.46 ? 107 SER A CB 1 ATOM 849 O OG . SER A 1 104 ? 19.134 57.392 6.694 1.00 66.11 ? 107 SER A OG 1 ATOM 850 N N . THR A 1 105 ? 15.901 56.592 5.784 1.00 58.31 ? 108 THR A N 1 ATOM 851 C CA . THR A 1 105 ? 14.994 55.450 5.905 1.00 54.21 ? 108 THR A CA 1 ATOM 852 C C . THR A 1 105 ? 13.530 55.813 6.045 1.00 52.89 ? 108 THR A C 1 ATOM 853 O O . THR A 1 105 ? 13.198 56.868 6.566 1.00 54.26 ? 108 THR A O 1 ATOM 854 C CB . THR A 1 105 ? 15.316 54.655 7.157 1.00 53.08 ? 108 THR A CB 1 ATOM 855 O OG1 . THR A 1 105 ? 16.733 54.538 7.294 1.00 53.84 ? 108 THR A OG1 1 ATOM 856 C CG2 . THR A 1 105 ? 14.676 53.292 7.094 1.00 53.56 ? 108 THR A CG2 1 ATOM 857 N N . ARG A 1 106 ? 12.648 54.928 5.600 1.00 51.01 ? 109 ARG A N 1 ATOM 858 C CA . ARG A 1 106 ? 11.225 55.177 5.767 1.00 49.68 ? 109 ARG A CA 1 ATOM 859 C C . ARG A 1 106 ? 10.795 54.166 6.842 1.00 49.62 ? 109 ARG A C 1 ATOM 860 O O . ARG A 1 106 ? 10.509 53.011 6.548 1.00 50.13 ? 109 ARG A O 1 ATOM 861 C CB . ARG A 1 106 ? 10.463 54.947 4.462 1.00 48.28 ? 109 ARG A CB 1 ATOM 862 C CG . ARG A 1 106 ? 9.056 55.489 4.509 1.00 45.90 ? 109 ARG A CG 1 ATOM 863 C CD . ARG A 1 106 ? 8.290 55.165 3.249 1.00 47.99 ? 109 ARG A CD 1 ATOM 864 N NE . ARG A 1 106 ? 6.866 55.413 3.463 1.00 51.02 ? 109 ARG A NE 1 ATOM 865 C CZ . ARG A 1 106 ? 5.879 55.056 2.637 1.00 51.93 ? 109 ARG A CZ 1 ATOM 866 N NH1 . ARG A 1 106 ? 6.142 54.419 1.500 1.00 53.85 ? 109 ARG A NH1 1 ATOM 867 N NH2 . ARG A 1 106 ? 4.610 55.319 2.962 1.00 50.55 ? 109 ARG A NH2 1 ATOM 868 N N . ILE A 1 107 ? 10.765 54.615 8.092 1.00 48.48 ? 110 ILE A N 1 ATOM 869 C CA . ILE A 1 107 ? 10.433 53.768 9.228 1.00 46.86 ? 110 ILE A CA 1 ATOM 870 C C . ILE A 1 107 ? 8.944 53.643 9.530 1.00 48.86 ? 110 ILE A C 1 ATOM 871 O O . ILE A 1 107 ? 8.246 54.645 9.588 1.00 51.99 ? 110 ILE A O 1 ATOM 872 C CB . ILE A 1 107 ? 11.158 54.314 10.437 1.00 43.76 ? 110 ILE A CB 1 ATOM 873 C CG1 . ILE A 1 107 ? 12.634 54.474 10.064 1.00 39.30 ? 110 ILE A CG1 1 ATOM 874 C CG2 . ILE A 1 107 ? 10.941 53.417 11.637 1.00 42.11 ? 110 ILE A CG2 1 ATOM 875 C CD1 . ILE A 1 107 ? 13.467 55.132 11.116 1.00 36.88 ? 110 ILE A CD1 1 ATOM 876 N N . HIS A 1 108 ? 8.463 52.417 9.725 1.00 48.09 ? 111 HIS A N 1 ATOM 877 C CA . HIS A 1 108 ? 7.048 52.176 10.015 1.00 48.61 ? 111 HIS A CA 1 ATOM 878 C C . HIS A 1 108 ? 6.958 51.447 11.319 1.00 48.66 ? 111 HIS A C 1 ATOM 879 O O . HIS A 1 108 ? 7.478 50.339 11.435 1.00 49.87 ? 111 HIS A O 1 ATOM 880 C CB . HIS A 1 108 ? 6.402 51.263 8.986 1.00 49.38 ? 111 HIS A CB 1 ATOM 881 C CG . HIS A 1 108 ? 6.345 51.826 7.601 1.00 52.34 ? 111 HIS A CG 1 ATOM 882 N ND1 . HIS A 1 108 ? 5.168 52.248 7.020 1.00 51.80 ? 111 HIS A ND1 1 ATOM 883 C CD2 . HIS A 1 108 ? 7.302 51.962 6.653 1.00 52.81 ? 111 HIS A CD2 1 ATOM 884 C CE1 . HIS A 1 108 ? 5.400 52.612 5.773 1.00 52.02 ? 111 HIS A CE1 1 ATOM 885 N NE2 . HIS A 1 108 ? 6.687 52.449 5.525 1.00 53.77 ? 111 HIS A NE2 1 ATOM 886 N N . ILE A 1 109 ? 6.254 52.026 12.282 1.00 48.26 ? 112 ILE A N 1 ATOM 887 C CA . ILE A 1 109 ? 6.135 51.399 13.590 1.00 46.77 ? 112 ILE A CA 1 ATOM 888 C C . ILE A 1 109 ? 4.704 51.052 14.005 1.00 47.23 ? 112 ILE A C 1 ATOM 889 O O . ILE A 1 109 ? 3.824 51.903 14.014 1.00 48.90 ? 112 ILE A O 1 ATOM 890 C CB . ILE A 1 109 ? 6.764 52.305 14.657 1.00 44.44 ? 112 ILE A CB 1 ATOM 891 C CG1 . ILE A 1 109 ? 8.213 52.602 14.285 1.00 42.69 ? 112 ILE A CG1 1 ATOM 892 C CG2 . ILE A 1 109 ? 6.723 51.638 15.995 1.00 45.21 ? 112 ILE A CG2 1 ATOM 893 C CD1 . ILE A 1 109 ? 8.854 53.633 15.162 1.00 43.58 ? 112 ILE A CD1 1 ATOM 894 N N . MET A 1 110 ? 4.473 49.785 14.325 1.00 47.06 ? 113 MET A N 1 ATOM 895 C CA . MET A 1 110 ? 3.163 49.335 14.778 1.00 46.53 ? 113 MET A CA 1 ATOM 896 C C . MET A 1 110 ? 3.369 48.831 16.217 1.00 49.88 ? 113 MET A C 1 ATOM 897 O O . MET A 1 110 ? 3.889 47.728 16.433 1.00 50.14 ? 113 MET A O 1 ATOM 898 C CB . MET A 1 110 ? 2.656 48.208 13.897 1.00 42.58 ? 113 MET A CB 1 ATOM 899 C CG . MET A 1 110 ? 1.324 47.718 14.355 1.00 42.44 ? 113 MET A CG 1 ATOM 900 S SD . MET A 1 110 ? 0.852 46.188 13.609 1.00 45.38 ? 113 MET A SD 1 ATOM 901 C CE . MET A 1 110 ? -0.055 46.753 12.209 1.00 44.81 ? 113 MET A CE 1 ATOM 902 N N . PRO A 1 111 ? 2.956 49.632 17.224 1.00 51.70 ? 114 PRO A N 1 ATOM 903 C CA . PRO A 1 111 ? 3.100 49.305 18.648 1.00 50.56 ? 114 PRO A CA 1 ATOM 904 C C . PRO A 1 111 ? 2.287 48.145 19.165 1.00 49.59 ? 114 PRO A C 1 ATOM 905 O O . PRO A 1 111 ? 2.618 47.579 20.210 1.00 51.01 ? 114 PRO A O 1 ATOM 906 C CB . PRO A 1 111 ? 2.722 50.605 19.358 1.00 51.01 ? 114 PRO A CB 1 ATOM 907 C CG . PRO A 1 111 ? 2.854 51.647 18.313 1.00 52.87 ? 114 PRO A CG 1 ATOM 908 C CD . PRO A 1 111 ? 2.327 50.951 17.083 1.00 52.29 ? 114 PRO A CD 1 ATOM 909 N N . SER A 1 112 ? 1.213 47.797 18.470 1.00 47.23 ? 115 SER A N 1 ATOM 910 C CA . SER A 1 112 ? 0.416 46.686 18.933 1.00 46.73 ? 115 SER A CA 1 ATOM 911 C C . SER A 1 112 ? -0.364 46.014 17.838 1.00 48.63 ? 115 SER A C 1 ATOM 912 O O . SER A 1 112 ? -1.305 46.589 17.292 1.00 50.66 ? 115 SER A O 1 ATOM 913 C CB . SER A 1 112 ? -0.545 47.133 20.015 1.00 44.73 ? 115 SER A CB 1 ATOM 914 O OG . SER A 1 112 ? -1.391 46.058 20.376 1.00 45.63 ? 115 SER A OG 1 ATOM 915 N N . MET A 1 113 ? 0.032 44.785 17.528 1.00 48.75 ? 116 MET A N 1 ATOM 916 C CA . MET A 1 113 ? -0.632 44.006 16.502 1.00 49.60 ? 116 MET A CA 1 ATOM 917 C C . MET A 1 113 ? -1.847 43.292 17.086 1.00 52.21 ? 116 MET A C 1 ATOM 918 O O . MET A 1 113 ? -2.753 42.875 16.351 1.00 54.22 ? 116 MET A O 1 ATOM 919 C CB . MET A 1 113 ? 0.321 42.978 15.911 1.00 45.97 ? 116 MET A CB 1 ATOM 920 C CG . MET A 1 113 ? -0.366 42.070 14.946 1.00 43.32 ? 116 MET A CG 1 ATOM 921 S SD . MET A 1 113 ? 0.740 40.948 14.130 1.00 44.31 ? 116 MET A SD 1 ATOM 922 C CE . MET A 1 113 ? -0.511 39.776 13.404 1.00 39.68 ? 116 MET A CE 1 ATOM 923 N N . ASN A 1 114 ? -1.856 43.138 18.407 1.00 52.77 ? 117 ASN A N 1 ATOM 924 C CA . ASN A 1 114 ? -2.972 42.492 19.080 1.00 53.70 ? 117 ASN A CA 1 ATOM 925 C C . ASN A 1 114 ? -3.494 43.321 20.253 1.00 55.98 ? 117 ASN A C 1 ATOM 926 O O . ASN A 1 114 ? -3.325 42.955 21.422 1.00 56.21 ? 117 ASN A O 1 ATOM 927 C CB . ASN A 1 114 ? -2.575 41.119 19.580 1.00 51.53 ? 117 ASN A CB 1 ATOM 928 C CG . ASN A 1 114 ? -3.675 40.488 20.366 1.00 51.99 ? 117 ASN A CG 1 ATOM 929 O OD1 . ASN A 1 114 ? -4.839 40.863 20.192 1.00 54.34 ? 117 ASN A OD1 1 ATOM 930 N ND2 . ASN A 1 114 ? -3.341 39.537 21.231 1.00 49.96 ? 117 ASN A ND2 1 ATOM 931 N N . PRO A 1 115 ? -4.144 44.457 19.952 1.00 56.64 ? 118 PRO A N 1 ATOM 932 C CA . PRO A 1 115 ? -4.685 45.337 20.988 1.00 55.47 ? 118 PRO A CA 1 ATOM 933 C C . PRO A 1 115 ? -5.819 44.756 21.816 1.00 56.22 ? 118 PRO A C 1 ATOM 934 O O . PRO A 1 115 ? -5.974 45.127 22.976 1.00 57.45 ? 118 PRO A O 1 ATOM 935 C CB . PRO A 1 115 ? -5.106 46.579 20.199 1.00 53.53 ? 118 PRO A CB 1 ATOM 936 C CG . PRO A 1 115 ? -5.438 46.046 18.854 1.00 52.25 ? 118 PRO A CG 1 ATOM 937 C CD . PRO A 1 115 ? -4.328 45.051 18.615 1.00 55.87 ? 118 PRO A CD 1 ATOM 938 N N . ASP A 1 116 ? -6.614 43.859 21.235 1.00 56.89 ? 119 ASP A N 1 ATOM 939 C CA . ASP A 1 116 ? -7.719 43.258 21.977 1.00 55.42 ? 119 ASP A CA 1 ATOM 940 C C . ASP A 1 116 ? -7.127 42.444 23.107 1.00 54.20 ? 119 ASP A C 1 ATOM 941 O O . ASP A 1 116 ? -7.590 42.507 24.250 1.00 54.97 ? 119 ASP A O 1 ATOM 942 C CB . ASP A 1 116 ? -8.549 42.307 21.104 1.00 55.62 ? 119 ASP A CB 1 ATOM 943 C CG . ASP A 1 116 ? -9.187 42.995 19.927 1.00 56.41 ? 119 ASP A CG 1 ATOM 944 O OD1 . ASP A 1 116 ? -9.614 44.152 20.091 1.00 58.74 ? 119 ASP A OD1 1 ATOM 945 O OD2 . ASP A 1 116 ? -9.278 42.366 18.849 1.00 57.33 ? 119 ASP A OD2 1 ATOM 946 N N . GLY A 1 117 ? -6.097 41.677 22.763 1.00 52.29 ? 120 GLY A N 1 ATOM 947 C CA . GLY A 1 117 ? -5.448 40.819 23.730 1.00 50.73 ? 120 GLY A CA 1 ATOM 948 C C . GLY A 1 117 ? -4.880 41.607 24.875 1.00 50.40 ? 120 GLY A C 1 ATOM 949 O O . GLY A 1 117 ? -5.005 41.224 26.035 1.00 50.22 ? 120 GLY A O 1 ATOM 950 N N . TYR A 1 118 ? -4.243 42.714 24.541 1.00 50.97 ? 121 TYR A N 1 ATOM 951 C CA . TYR A 1 118 ? -3.652 43.560 25.552 1.00 53.36 ? 121 TYR A CA 1 ATOM 952 C C . TYR A 1 118 ? -4.665 43.909 26.637 1.00 55.30 ? 121 TYR A C 1 ATOM 953 O O . TYR A 1 118 ? -4.413 43.700 27.825 1.00 57.30 ? 121 TYR A O 1 ATOM 954 C CB . TYR A 1 118 ? -3.156 44.851 24.922 1.00 53.21 ? 121 TYR A CB 1 ATOM 955 C CG . TYR A 1 118 ? -2.517 45.799 25.904 1.00 53.09 ? 121 TYR A CG 1 ATOM 956 C CD1 . TYR A 1 118 ? -1.201 45.619 26.305 1.00 53.89 ? 121 TYR A CD1 1 ATOM 957 C CD2 . TYR A 1 118 ? -3.218 46.889 26.414 1.00 53.36 ? 121 TYR A CD2 1 ATOM 958 C CE1 . TYR A 1 118 ? -0.586 46.506 27.187 1.00 55.11 ? 121 TYR A CE1 1 ATOM 959 C CE2 . TYR A 1 118 ? -2.611 47.786 27.303 1.00 53.37 ? 121 TYR A CE2 1 ATOM 960 C CZ . TYR A 1 118 ? -1.291 47.587 27.678 1.00 53.47 ? 121 TYR A CZ 1 ATOM 961 O OH . TYR A 1 118 ? -0.642 48.473 28.505 1.00 52.91 ? 121 TYR A OH 1 ATOM 962 N N . GLU A 1 119 ? -5.811 44.444 26.224 1.00 56.23 ? 122 GLU A N 1 ATOM 963 C CA . GLU A 1 119 ? -6.844 44.862 27.169 1.00 54.84 ? 122 GLU A CA 1 ATOM 964 C C . GLU A 1 119 ? -7.281 43.780 28.153 1.00 54.79 ? 122 GLU A C 1 ATOM 965 O O . GLU A 1 119 ? -7.743 44.093 29.240 1.00 55.41 ? 122 GLU A O 1 ATOM 966 C CB . GLU A 1 119 ? -8.063 45.406 26.422 1.00 52.44 ? 122 GLU A CB 1 ATOM 967 C CG . GLU A 1 119 ? -7.770 46.624 25.556 1.00 54.50 ? 122 GLU A CG 1 ATOM 968 C CD . GLU A 1 119 ? -7.055 47.751 26.304 1.00 56.75 ? 122 GLU A CD 1 ATOM 969 O OE1 . GLU A 1 119 ? -7.393 47.972 27.484 1.00 58.73 ? 122 GLU A OE1 1 ATOM 970 O OE2 . GLU A 1 119 ? -6.169 48.423 25.712 1.00 55.35 ? 122 GLU A OE2 1 ATOM 971 N N . LYS A 1 120 ? -7.124 42.514 27.792 1.00 55.62 ? 123 LYS A N 1 ATOM 972 C CA . LYS A 1 120 ? -7.534 41.451 28.696 1.00 57.91 ? 123 LYS A CA 1 ATOM 973 C C . LYS A 1 120 ? -6.367 40.973 29.532 1.00 59.83 ? 123 LYS A C 1 ATOM 974 O O . LYS A 1 120 ? -6.468 39.948 30.201 1.00 61.50 ? 123 LYS A O 1 ATOM 975 C CB . LYS A 1 120 ? -8.079 40.249 27.925 1.00 56.46 ? 123 LYS A CB 1 ATOM 976 C CG . LYS A 1 120 ? -8.899 40.588 26.719 1.00 59.56 ? 123 LYS A CG 1 ATOM 977 C CD . LYS A 1 120 ? -9.457 39.325 26.074 1.00 63.83 ? 123 LYS A CD 1 ATOM 978 C CE . LYS A 1 120 ? -9.979 39.616 24.670 1.00 66.40 ? 123 LYS A CE 1 ATOM 979 N NZ . LYS A 1 120 ? -10.695 40.933 24.608 1.00 69.32 ? 123 LYS A NZ 1 ATOM 980 N N . SER A 1 121 ? -5.261 41.702 29.508 1.00 62.14 ? 124 SER A N 1 ATOM 981 C CA . SER A 1 121 ? -4.084 41.261 30.254 1.00 64.63 ? 124 SER A CA 1 ATOM 982 C C . SER A 1 121 ? -3.939 41.845 31.663 1.00 66.01 ? 124 SER A C 1 ATOM 983 O O . SER A 1 121 ? -4.511 42.887 31.983 1.00 66.31 ? 124 SER A O 1 ATOM 984 C CB . SER A 1 121 ? -2.831 41.530 29.419 1.00 63.35 ? 124 SER A CB 1 ATOM 985 O OG . SER A 1 121 ? -2.988 40.988 28.115 1.00 61.05 ? 124 SER A OG 1 ATOM 986 N N . GLN A 1 122 ? -3.162 41.159 32.497 1.00 67.10 ? 125 GLN A N 1 ATOM 987 C CA . GLN A 1 122 ? -2.959 41.573 33.883 1.00 68.25 ? 125 GLN A CA 1 ATOM 988 C C . GLN A 1 122 ? -1.554 42.105 34.181 1.00 67.87 ? 125 GLN A C 1 ATOM 989 O O . GLN A 1 122 ? -0.575 41.360 34.045 1.00 67.66 ? 125 GLN A O 1 ATOM 990 C CB . GLN A 1 122 ? -3.250 40.381 34.808 1.00 71.07 ? 125 GLN A CB 1 ATOM 991 C CG . GLN A 1 122 ? -4.700 39.898 34.780 1.00 75.63 ? 125 GLN A CG 1 ATOM 992 C CD . GLN A 1 122 ? -5.697 41.000 35.179 1.00 79.49 ? 125 GLN A CD 1 ATOM 993 O OE1 . GLN A 1 122 ? -6.547 41.421 34.370 1.00 80.36 ? 125 GLN A OE1 1 ATOM 994 N NE2 . GLN A 1 122 ? -5.593 41.475 36.429 1.00 78.58 ? 125 GLN A NE2 1 ATOM 995 N N . GLU A 1 123 ? -1.441 43.371 34.601 1.00 67.56 ? 126 GLU A N 1 ATOM 996 C CA . GLU A 1 123 ? -0.119 43.931 34.914 1.00 67.19 ? 126 GLU A CA 1 ATOM 997 C C . GLU A 1 123 ? 0.508 42.969 35.919 1.00 69.00 ? 126 GLU A C 1 ATOM 998 O O . GLU A 1 123 ? -0.210 42.289 36.661 1.00 70.63 ? 126 GLU A O 1 ATOM 999 C CB . GLU A 1 123 ? -0.229 45.357 35.498 1.00 64.52 ? 126 GLU A CB 1 ATOM 1000 C CG . GLU A 1 123 ? 1.117 46.024 35.857 1.00 62.55 ? 126 GLU A CG 1 ATOM 1001 C CD . GLU A 1 123 ? 1.009 47.543 36.124 1.00 66.04 ? 126 GLU A CD 1 ATOM 1002 O OE1 . GLU A 1 123 ? 0.028 48.163 35.656 1.00 68.10 ? 126 GLU A OE1 1 ATOM 1003 O OE2 . GLU A 1 123 ? 1.908 48.128 36.789 1.00 63.34 ? 126 GLU A OE2 1 ATOM 1004 N N . GLY A 1 124 ? 1.836 42.877 35.918 1.00 70.09 ? 127 GLY A N 1 ATOM 1005 C CA . GLY A 1 124 ? 2.512 41.969 36.832 1.00 70.05 ? 127 GLY A CA 1 ATOM 1006 C C . GLY A 1 124 ? 2.627 40.538 36.325 1.00 69.99 ? 127 GLY A C 1 ATOM 1007 O O . GLY A 1 124 ? 3.420 39.750 36.845 1.00 70.41 ? 127 GLY A O 1 ATOM 1008 N N . ASP A 1 125 ? 1.827 40.188 35.322 1.00 71.00 ? 128 ASP A N 1 ATOM 1009 C CA . ASP A 1 125 ? 1.868 38.848 34.738 1.00 72.94 ? 128 ASP A CA 1 ATOM 1010 C C . ASP A 1 125 ? 3.299 38.567 34.234 1.00 72.36 ? 128 ASP A C 1 ATOM 1011 O O . ASP A 1 125 ? 3.846 39.309 33.419 1.00 70.91 ? 128 ASP A O 1 ATOM 1012 C CB . ASP A 1 125 ? 0.856 38.768 33.586 1.00 74.91 ? 128 ASP A CB 1 ATOM 1013 C CG . ASP A 1 125 ? 0.611 37.343 33.107 1.00 78.00 ? 128 ASP A CG 1 ATOM 1014 O OD1 . ASP A 1 125 ? 1.291 36.415 33.611 1.00 79.86 ? 128 ASP A OD1 1 ATOM 1015 O OD2 . ASP A 1 125 ? -0.267 37.161 32.224 1.00 78.79 ? 128 ASP A OD2 1 ATOM 1016 N N . ARG A 1 126 ? 3.911 37.500 34.721 1.00 73.07 ? 129 ARG A N 1 ATOM 1017 C CA . ARG A 1 126 ? 5.271 37.189 34.314 1.00 75.34 ? 129 ARG A CA 1 ATOM 1018 C C . ARG A 1 126 ? 5.388 36.114 33.236 1.00 75.80 ? 129 ARG A C 1 ATOM 1019 O O . ARG A 1 126 ? 6.130 36.291 32.260 1.00 77.03 ? 129 ARG A O 1 ATOM 1020 C CB . ARG A 1 126 ? 6.080 36.766 35.528 1.00 77.26 ? 129 ARG A CB 1 ATOM 1021 C CG . ARG A 1 126 ? 5.357 35.749 36.408 1.00 81.93 ? 129 ARG A CG 1 ATOM 1022 C CD . ARG A 1 126 ? 6.354 35.084 37.322 1.00 84.02 ? 129 ARG A CD 1 ATOM 1023 N NE . ARG A 1 126 ? 7.389 36.040 37.704 1.00 85.68 ? 129 ARG A NE 1 ATOM 1024 C CZ . ARG A 1 126 ? 8.515 35.710 38.323 1.00 86.68 ? 129 ARG A CZ 1 ATOM 1025 N NH1 . ARG A 1 126 ? 8.748 34.437 38.632 1.00 85.93 ? 129 ARG A NH1 1 ATOM 1026 N NH2 . ARG A 1 126 ? 9.407 36.650 38.623 1.00 87.37 ? 129 ARG A NH2 1 ATOM 1027 N N . GLY A 1 127 ? 4.676 34.999 33.416 1.00 74.78 ? 130 GLY A N 1 ATOM 1028 C CA . GLY A 1 127 ? 4.738 33.919 32.442 1.00 71.92 ? 130 GLY A CA 1 ATOM 1029 C C . GLY A 1 127 ? 3.376 33.433 31.987 1.00 70.17 ? 130 GLY A C 1 ATOM 1030 O O . GLY A 1 127 ? 3.296 32.520 31.168 1.00 69.14 ? 130 GLY A O 1 ATOM 1031 N N . GLY A 1 128 ? 2.314 34.058 32.506 1.00 68.97 ? 131 GLY A N 1 ATOM 1032 C CA . GLY A 1 128 ? 0.937 33.686 32.181 1.00 67.13 ? 131 GLY A CA 1 ATOM 1033 C C . GLY A 1 128 ? 0.538 33.731 30.721 1.00 65.90 ? 131 GLY A C 1 ATOM 1034 O O . GLY A 1 128 ? 1.390 33.920 29.860 1.00 65.75 ? 131 GLY A O 1 ATOM 1035 N N . THR A 1 129 ? -0.747 33.550 30.424 1.00 65.39 ? 132 THR A N 1 ATOM 1036 C CA . THR A 1 129 ? -1.180 33.585 29.022 1.00 66.76 ? 132 THR A CA 1 ATOM 1037 C C . THR A 1 129 ? -2.456 34.357 28.794 1.00 65.97 ? 132 THR A C 1 ATOM 1038 O O . THR A 1 129 ? -2.934 34.474 27.664 1.00 67.18 ? 132 THR A O 1 ATOM 1039 C CB . THR A 1 129 ? -1.435 32.196 28.436 1.00 67.59 ? 132 THR A CB 1 ATOM 1040 O OG1 . THR A 1 129 ? -2.520 31.580 29.142 1.00 69.55 ? 132 THR A OG1 1 ATOM 1041 C CG2 . THR A 1 129 ? -0.185 31.345 28.505 1.00 67.77 ? 132 THR A CG2 1 ATOM 1042 N N . VAL A 1 130 ? -3.024 34.871 29.867 1.00 64.82 ? 133 VAL A N 1 ATOM 1043 C CA . VAL A 1 130 ? -4.245 35.636 29.740 1.00 62.96 ? 133 VAL A CA 1 ATOM 1044 C C . VAL A 1 130 ? -4.038 36.888 28.885 1.00 61.88 ? 133 VAL A C 1 ATOM 1045 O O . VAL A 1 130 ? -3.309 37.808 29.277 1.00 62.37 ? 133 VAL A O 1 ATOM 1046 C CB . VAL A 1 130 ? -4.747 36.035 31.114 1.00 62.04 ? 133 VAL A CB 1 ATOM 1047 C CG1 . VAL A 1 130 ? -6.039 36.809 30.974 1.00 59.76 ? 133 VAL A CG1 1 ATOM 1048 C CG2 . VAL A 1 130 ? -4.902 34.781 31.977 1.00 59.55 ? 133 VAL A CG2 1 ATOM 1049 N N . GLY A 1 131 ? -4.680 36.912 27.717 1.00 60.18 ? 134 GLY A N 1 ATOM 1050 C CA . GLY A 1 131 ? -4.565 38.051 26.824 1.00 58.37 ? 134 GLY A CA 1 ATOM 1051 C C . GLY A 1 131 ? -3.547 37.823 25.722 1.00 58.06 ? 134 GLY A C 1 ATOM 1052 O O . GLY A 1 131 ? -3.367 38.668 24.849 1.00 58.19 ? 134 GLY A O 1 ATOM 1053 N N . ARG A 1 132 ? -2.870 36.681 25.764 1.00 56.10 ? 135 ARG A N 1 ATOM 1054 C CA . ARG A 1 132 ? -1.876 36.360 24.756 1.00 54.74 ? 135 ARG A CA 1 ATOM 1055 C C . ARG A 1 132 ? -2.560 36.212 23.409 1.00 56.82 ? 135 ARG A C 1 ATOM 1056 O O . ARG A 1 132 ? -2.212 36.891 22.439 1.00 59.34 ? 135 ARG A O 1 ATOM 1057 C CB . ARG A 1 132 ? -1.173 35.056 25.107 1.00 52.98 ? 135 ARG A CB 1 ATOM 1058 C CG . ARG A 1 132 ? -0.357 34.477 23.969 1.00 51.84 ? 135 ARG A CG 1 ATOM 1059 C CD . ARG A 1 132 ? 0.170 33.125 24.351 1.00 51.70 ? 135 ARG A CD 1 ATOM 1060 N NE . ARG A 1 132 ? 0.883 32.429 23.282 1.00 54.52 ? 135 ARG A NE 1 ATOM 1061 C CZ . ARG A 1 132 ? 2.162 32.618 22.970 1.00 54.44 ? 135 ARG A CZ 1 ATOM 1062 N NH1 . ARG A 1 132 ? 2.892 33.506 23.642 1.00 54.32 ? 135 ARG A NH1 1 ATOM 1063 N NH2 . ARG A 1 132 ? 2.725 31.883 22.011 1.00 54.79 ? 135 ARG A NH2 1 ATOM 1064 N N . ASN A 1 133 ? -3.536 35.315 23.342 1.00 57.79 ? 136 ASN A N 1 ATOM 1065 C CA . ASN A 1 133 ? -4.258 35.101 22.099 1.00 57.18 ? 136 ASN A CA 1 ATOM 1066 C C . ASN A 1 133 ? -5.086 36.307 21.686 1.00 57.70 ? 136 ASN A C 1 ATOM 1067 O O . ASN A 1 133 ? -5.155 37.300 22.420 1.00 57.65 ? 136 ASN A O 1 ATOM 1068 C CB . ASN A 1 133 ? -5.140 33.869 22.222 1.00 55.96 ? 136 ASN A CB 1 ATOM 1069 C CG . ASN A 1 133 ? -4.356 32.602 22.027 1.00 53.96 ? 136 ASN A CG 1 ATOM 1070 O OD1 . ASN A 1 133 ? -3.250 32.649 21.499 1.00 55.51 ? 136 ASN A OD1 1 ATOM 1071 N ND2 . ASN A 1 133 ? -4.905 31.463 22.420 1.00 51.14 ? 136 ASN A ND2 1 ATOM 1072 N N . ASN A 1 134 ? -5.696 36.233 20.502 1.00 57.74 ? 137 ASN A N 1 ATOM 1073 C CA . ASN A 1 134 ? -6.516 37.342 20.018 1.00 57.90 ? 137 ASN A CA 1 ATOM 1074 C C . ASN A 1 134 ? -7.933 37.172 20.567 1.00 59.08 ? 137 ASN A C 1 ATOM 1075 O O . ASN A 1 134 ? -8.195 36.241 21.341 1.00 60.63 ? 137 ASN A O 1 ATOM 1076 C CB . ASN A 1 134 ? -6.483 37.425 18.477 1.00 54.21 ? 137 ASN A CB 1 ATOM 1077 C CG . ASN A 1 134 ? -7.562 36.613 17.815 1.00 52.42 ? 137 ASN A CG 1 ATOM 1078 O OD1 . ASN A 1 134 ? -7.954 35.557 18.303 1.00 52.01 ? 137 ASN A OD1 1 ATOM 1079 N ND2 . ASN A 1 134 ? -8.040 37.097 16.674 1.00 52.31 ? 137 ASN A ND2 1 ATOM 1080 N N . SER A 1 135 ? -8.838 38.070 20.190 1.00 59.36 ? 138 SER A N 1 ATOM 1081 C CA . SER A 1 135 ? -10.202 38.025 20.707 1.00 59.19 ? 138 SER A CA 1 ATOM 1082 C C . SER A 1 135 ? -10.967 36.702 20.500 1.00 59.45 ? 138 SER A C 1 ATOM 1083 O O . SER A 1 135 ? -11.832 36.357 21.314 1.00 60.05 ? 138 SER A O 1 ATOM 1084 C CB . SER A 1 135 ? -10.998 39.192 20.126 1.00 59.65 ? 138 SER A CB 1 ATOM 1085 O OG . SER A 1 135 ? -12.112 39.485 20.946 1.00 60.93 ? 138 SER A OG 1 ATOM 1086 N N . ASN A 1 136 ? -10.644 35.974 19.424 1.00 58.39 ? 139 ASN A N 1 ATOM 1087 C CA . ASN A 1 136 ? -11.290 34.699 19.102 1.00 56.29 ? 139 ASN A CA 1 ATOM 1088 C C . ASN A 1 136 ? -10.471 33.574 19.660 1.00 55.77 ? 139 ASN A C 1 ATOM 1089 O O . ASN A 1 136 ? -10.790 32.405 19.466 1.00 56.81 ? 139 ASN A O 1 ATOM 1090 C CB . ASN A 1 136 ? -11.412 34.500 17.592 1.00 57.68 ? 139 ASN A CB 1 ATOM 1091 C CG . ASN A 1 136 ? -12.331 35.510 16.948 1.00 59.98 ? 139 ASN A CG 1 ATOM 1092 O OD1 . ASN A 1 136 ? -13.456 35.710 17.406 1.00 63.37 ? 139 ASN A OD1 1 ATOM 1093 N ND2 . ASN A 1 136 ? -11.861 36.157 15.882 1.00 58.65 ? 139 ASN A ND2 1 ATOM 1094 N N . ASN A 1 137 ? -9.396 33.943 20.335 1.00 54.74 ? 140 ASN A N 1 ATOM 1095 C CA . ASN A 1 137 ? -8.500 32.995 20.972 1.00 55.25 ? 140 ASN A CA 1 ATOM 1096 C C . ASN A 1 137 ? -7.647 32.102 20.078 1.00 55.18 ? 140 ASN A C 1 ATOM 1097 O O . ASN A 1 137 ? -7.677 30.871 20.178 1.00 54.41 ? 140 ASN A O 1 ATOM 1098 C CB . ASN A 1 137 ? -9.261 32.118 21.954 1.00 56.44 ? 140 ASN A CB 1 ATOM 1099 C CG . ASN A 1 137 ? -8.335 31.400 22.899 1.00 56.49 ? 140 ASN A CG 1 ATOM 1100 O OD1 . ASN A 1 137 ? -7.492 32.028 23.541 1.00 57.55 ? 140 ASN A OD1 1 ATOM 1101 N ND2 . ASN A 1 137 ? -8.478 30.085 22.994 1.00 57.42 ? 140 ASN A ND2 1 ATOM 1102 N N . TYR A 1 138 ? -6.882 32.744 19.207 1.00 53.75 ? 141 TYR A N 1 ATOM 1103 C CA . TYR A 1 138 ? -5.961 32.051 18.343 1.00 52.55 ? 141 TYR A CA 1 ATOM 1104 C C . TYR A 1 138 ? -4.649 32.768 18.567 1.00 52.12 ? 141 TYR A C 1 ATOM 1105 O O . TYR A 1 138 ? -4.641 33.951 18.902 1.00 52.01 ? 141 TYR A O 1 ATOM 1106 C CB . TYR A 1 138 ? -6.392 32.154 16.891 1.00 54.63 ? 141 TYR A CB 1 ATOM 1107 C CG . TYR A 1 138 ? -7.552 31.245 16.575 1.00 57.97 ? 141 TYR A CG 1 ATOM 1108 C CD1 . TYR A 1 138 ? -7.335 29.912 16.263 1.00 58.90 ? 141 TYR A CD1 1 ATOM 1109 C CD2 . TYR A 1 138 ? -8.870 31.708 16.608 1.00 58.44 ? 141 TYR A CD2 1 ATOM 1110 C CE1 . TYR A 1 138 ? -8.393 29.047 15.987 1.00 61.00 ? 141 TYR A CE1 1 ATOM 1111 C CE2 . TYR A 1 138 ? -9.948 30.850 16.331 1.00 59.48 ? 141 TYR A CE2 1 ATOM 1112 C CZ . TYR A 1 138 ? -9.701 29.514 16.020 1.00 61.62 ? 141 TYR A CZ 1 ATOM 1113 O OH . TYR A 1 138 ? -10.742 28.632 15.744 1.00 62.92 ? 141 TYR A OH 1 ATOM 1114 N N . ASP A 1 139 ? -3.547 32.041 18.417 1.00 52.07 ? 142 ASP A N 1 ATOM 1115 C CA . ASP A 1 139 ? -2.209 32.595 18.605 1.00 51.22 ? 142 ASP A CA 1 ATOM 1116 C C . ASP A 1 139 ? -1.817 33.284 17.303 1.00 50.43 ? 142 ASP A C 1 ATOM 1117 O O . ASP A 1 139 ? -1.476 32.614 16.326 1.00 51.17 ? 142 ASP A O 1 ATOM 1118 C CB . ASP A 1 139 ? -1.233 31.457 18.906 1.00 52.18 ? 142 ASP A CB 1 ATOM 1119 C CG . ASP A 1 139 ? 0.057 31.937 19.539 1.00 52.15 ? 142 ASP A CG 1 ATOM 1120 O OD1 . ASP A 1 139 ? 0.596 32.982 19.097 1.00 49.75 ? 142 ASP A OD1 1 ATOM 1121 O OD2 . ASP A 1 139 ? 0.535 31.248 20.475 1.00 53.02 ? 142 ASP A OD2 1 ATOM 1122 N N . LEU A 1 140 ? -1.861 34.613 17.279 1.00 48.88 ? 143 LEU A N 1 ATOM 1123 C CA . LEU A 1 140 ? -1.528 35.322 16.049 1.00 46.74 ? 143 LEU A CA 1 ATOM 1124 C C . LEU A 1 140 ? -0.159 34.958 15.505 1.00 47.78 ? 143 LEU A C 1 ATOM 1125 O O . LEU A 1 140 ? 0.134 35.228 14.342 1.00 47.44 ? 143 LEU A O 1 ATOM 1126 C CB . LEU A 1 140 ? -1.631 36.836 16.237 1.00 43.69 ? 143 LEU A CB 1 ATOM 1127 C CG . LEU A 1 140 ? -3.027 37.396 16.528 1.00 41.60 ? 143 LEU A CG 1 ATOM 1128 C CD1 . LEU A 1 140 ? -2.966 38.917 16.457 1.00 36.80 ? 143 LEU A CD1 1 ATOM 1129 C CD2 . LEU A 1 140 ? -4.052 36.850 15.521 1.00 39.64 ? 143 LEU A CD2 1 ATOM 1130 N N . ASN A 1 141 ? 0.682 34.339 16.332 1.00 49.49 ? 144 ASN A N 1 ATOM 1131 C CA . ASN A 1 141 ? 2.011 33.937 15.865 1.00 48.24 ? 144 ASN A CA 1 ATOM 1132 C C . ASN A 1 141 ? 2.092 32.450 15.511 1.00 47.57 ? 144 ASN A C 1 ATOM 1133 O O . ASN A 1 141 ? 3.175 31.859 15.494 1.00 49.03 ? 144 ASN A O 1 ATOM 1134 C CB . ASN A 1 141 ? 3.079 34.282 16.891 1.00 47.57 ? 144 ASN A CB 1 ATOM 1135 C CG . ASN A 1 141 ? 4.466 34.298 16.284 1.00 48.14 ? 144 ASN A CG 1 ATOM 1136 O OD1 . ASN A 1 141 ? 4.673 34.803 15.163 1.00 47.89 ? 144 ASN A OD1 1 ATOM 1137 N ND2 . ASN A 1 141 ? 5.433 33.762 17.019 1.00 47.44 ? 144 ASN A ND2 1 ATOM 1138 N N . ARG A 1 142 ? 0.925 31.864 15.248 1.00 46.04 ? 145 ARG A N 1 ATOM 1139 C CA . ARG A 1 142 ? 0.772 30.479 14.825 1.00 45.27 ? 145 ARG A CA 1 ATOM 1140 C C . ARG A 1 142 ? -0.279 30.582 13.734 1.00 48.38 ? 145 ARG A C 1 ATOM 1141 O O . ARG A 1 142 ? -0.673 29.587 13.139 1.00 50.44 ? 145 ARG A O 1 ATOM 1142 C CB . ARG A 1 142 ? 0.187 29.619 15.928 1.00 41.93 ? 145 ARG A CB 1 ATOM 1143 C CG . ARG A 1 142 ? 1.009 29.525 17.143 1.00 42.44 ? 145 ARG A CG 1 ATOM 1144 C CD . ARG A 1 142 ? 2.116 28.493 17.031 1.00 42.75 ? 145 ARG A CD 1 ATOM 1145 N NE . ARG A 1 142 ? 2.845 28.476 18.297 1.00 43.10 ? 145 ARG A NE 1 ATOM 1146 C CZ . ARG A 1 142 ? 3.589 29.491 18.736 1.00 44.77 ? 145 ARG A CZ 1 ATOM 1147 N NH1 . ARG A 1 142 ? 3.762 30.576 17.986 1.00 49.18 ? 145 ARG A NH1 1 ATOM 1148 N NH2 . ARG A 1 142 ? 4.193 29.410 19.908 1.00 45.64 ? 145 ARG A NH2 1 ATOM 1149 N N . ASN A 1 143 ? -0.730 31.803 13.473 1.00 50.49 ? 146 ASN A N 1 ATOM 1150 C CA . ASN A 1 143 ? -1.788 32.017 12.501 1.00 51.16 ? 146 ASN A CA 1 ATOM 1151 C C . ASN A 1 143 ? -1.367 32.201 11.059 1.00 51.67 ? 146 ASN A C 1 ATOM 1152 O O . ASN A 1 143 ? -2.224 32.262 10.184 1.00 53.72 ? 146 ASN A O 1 ATOM 1153 C CB . ASN A 1 143 ? -2.634 33.217 12.915 1.00 51.29 ? 146 ASN A CB 1 ATOM 1154 C CG . ASN A 1 143 ? -4.074 33.083 12.479 1.00 51.84 ? 146 ASN A CG 1 ATOM 1155 O OD1 . ASN A 1 143 ? -4.681 34.035 12.001 1.00 55.37 ? 146 ASN A OD1 1 ATOM 1156 N ND2 . ASN A 1 143 ? -4.634 31.897 12.660 1.00 50.49 ? 146 ASN A ND2 1 ATOM 1157 N N . PHE A 1 144 ? -0.073 32.294 10.792 1.00 51.43 ? 147 PHE A N 1 ATOM 1158 C CA . PHE A 1 144 ? 0.380 32.491 9.416 1.00 51.58 ? 147 PHE A CA 1 ATOM 1159 C C . PHE A 1 144 ? 0.607 31.194 8.658 1.00 53.35 ? 147 PHE A C 1 ATOM 1160 O O . PHE A 1 144 ? 0.801 30.143 9.263 1.00 53.56 ? 147 PHE A O 1 ATOM 1161 C CB . PHE A 1 144 ? 1.681 33.297 9.393 1.00 50.41 ? 147 PHE A CB 1 ATOM 1162 C CG . PHE A 1 144 ? 1.507 34.731 9.763 1.00 50.24 ? 147 PHE A CG 1 ATOM 1163 C CD1 . PHE A 1 144 ? 1.163 35.094 11.057 1.00 51.10 ? 147 PHE A CD1 1 ATOM 1164 C CD2 . PHE A 1 144 ? 1.682 35.722 8.819 1.00 49.93 ? 147 PHE A CD2 1 ATOM 1165 C CE1 . PHE A 1 144 ? 0.997 36.427 11.408 1.00 49.88 ? 147 PHE A CE1 1 ATOM 1166 C CE2 . PHE A 1 144 ? 1.517 37.058 9.165 1.00 51.89 ? 147 PHE A CE2 1 ATOM 1167 C CZ . PHE A 1 144 ? 1.174 37.408 10.464 1.00 50.21 ? 147 PHE A CZ 1 ATOM 1168 N N . PRO A 1 145 ? 0.579 31.248 7.313 1.00 55.17 ? 148 PRO A N 1 ATOM 1169 C CA . PRO A 1 145 ? 0.803 30.035 6.527 1.00 55.47 ? 148 PRO A CA 1 ATOM 1170 C C . PRO A 1 145 ? 2.250 29.628 6.760 1.00 56.27 ? 148 PRO A C 1 ATOM 1171 O O . PRO A 1 145 ? 3.177 30.437 6.577 1.00 57.21 ? 148 PRO A O 1 ATOM 1172 C CB . PRO A 1 145 ? 0.560 30.498 5.097 1.00 54.17 ? 148 PRO A CB 1 ATOM 1173 C CG . PRO A 1 145 ? -0.417 31.592 5.260 1.00 54.63 ? 148 PRO A CG 1 ATOM 1174 C CD . PRO A 1 145 ? 0.142 32.345 6.435 1.00 55.89 ? 148 PRO A CD 1 ATOM 1175 N N . ASP A 1 146 ? 2.436 28.379 7.175 1.00 56.70 ? 149 ASP A N 1 ATOM 1176 C CA . ASP A 1 146 ? 3.761 27.855 7.474 1.00 55.42 ? 149 ASP A CA 1 ATOM 1177 C C . ASP A 1 146 ? 4.300 27.115 6.270 1.00 54.96 ? 149 ASP A C 1 ATOM 1178 O O . ASP A 1 146 ? 3.520 26.615 5.452 1.00 55.69 ? 149 ASP A O 1 ATOM 1179 C CB . ASP A 1 146 ? 3.673 26.904 8.652 1.00 53.90 ? 149 ASP A CB 1 ATOM 1180 C CG . ASP A 1 146 ? 4.999 26.622 9.248 1.00 52.22 ? 149 ASP A CG 1 ATOM 1181 O OD1 . ASP A 1 146 ? 5.467 27.452 10.053 1.00 51.66 ? 149 ASP A OD1 1 ATOM 1182 O OD2 . ASP A 1 146 ? 5.579 25.578 8.898 1.00 53.82 ? 149 ASP A OD2 1 ATOM 1183 N N . GLN A 1 147 ? 5.623 27.038 6.151 1.00 54.10 ? 150 GLN A N 1 ATOM 1184 C CA . GLN A 1 147 ? 6.203 26.342 5.007 1.00 52.79 ? 150 GLN A CA 1 ATOM 1185 C C . GLN A 1 147 ? 6.211 24.830 5.185 1.00 54.29 ? 150 GLN A C 1 ATOM 1186 O O . GLN A 1 147 ? 6.214 24.096 4.204 1.00 56.56 ? 150 GLN A O 1 ATOM 1187 C CB . GLN A 1 147 ? 7.626 26.817 4.737 1.00 49.93 ? 150 GLN A CB 1 ATOM 1188 C CG . GLN A 1 147 ? 8.602 26.366 5.769 1.00 48.68 ? 150 GLN A CG 1 ATOM 1189 C CD . GLN A 1 147 ? 10.018 26.791 5.469 1.00 49.86 ? 150 GLN A CD 1 ATOM 1190 O OE1 . GLN A 1 147 ? 10.611 26.382 4.459 1.00 51.42 ? 150 GLN A OE1 1 ATOM 1191 N NE2 . GLN A 1 147 ? 10.584 27.615 6.353 1.00 50.11 ? 150 GLN A NE2 1 ATOM 1192 N N . PHE A 1 148 ? 6.200 24.353 6.424 1.00 56.17 ? 151 PHE A N 1 ATOM 1193 C CA . PHE A 1 148 ? 6.225 22.913 6.657 1.00 58.40 ? 151 PHE A CA 1 ATOM 1194 C C . PHE A 1 148 ? 4.892 22.383 7.117 1.00 62.82 ? 151 PHE A C 1 ATOM 1195 O O . PHE A 1 148 ? 4.272 21.578 6.430 1.00 64.74 ? 151 PHE A O 1 ATOM 1196 C CB . PHE A 1 148 ? 7.276 22.569 7.697 1.00 55.15 ? 151 PHE A CB 1 ATOM 1197 C CG . PHE A 1 148 ? 8.666 22.972 7.311 1.00 51.37 ? 151 PHE A CG 1 ATOM 1198 C CD1 . PHE A 1 148 ? 9.273 22.425 6.187 1.00 49.35 ? 151 PHE A CD1 1 ATOM 1199 C CD2 . PHE A 1 148 ? 9.383 23.874 8.092 1.00 50.05 ? 151 PHE A CD2 1 ATOM 1200 C CE1 . PHE A 1 148 ? 10.580 22.766 5.845 1.00 46.78 ? 151 PHE A CE1 1 ATOM 1201 C CE2 . PHE A 1 148 ? 10.684 24.223 7.760 1.00 49.86 ? 151 PHE A CE2 1 ATOM 1202 C CZ . PHE A 1 148 ? 11.286 23.664 6.629 1.00 48.65 ? 151 PHE A CZ 1 ATOM 1203 N N . PHE A 1 149 ? 4.473 22.821 8.300 1.00 69.25 ? 152 PHE A N 1 ATOM 1204 C CA . PHE A 1 149 ? 3.192 22.430 8.890 1.00 74.49 ? 152 PHE A CA 1 ATOM 1205 C C . PHE A 1 149 ? 2.109 23.152 8.094 1.00 74.13 ? 152 PHE A C 1 ATOM 1206 O O . PHE A 1 149 ? 2.358 24.205 7.500 1.00 74.57 ? 152 PHE A O 1 ATOM 1207 C CB . PHE A 1 149 ? 3.141 22.884 10.369 1.00 81.62 ? 152 PHE A CB 1 ATOM 1208 C CG . PHE A 1 149 ? 1.854 22.516 11.110 1.00 89.08 ? 152 PHE A CG 1 ATOM 1209 C CD1 . PHE A 1 149 ? 1.580 21.189 11.472 1.00 92.61 ? 152 PHE A CD1 1 ATOM 1210 C CD2 . PHE A 1 149 ? 0.932 23.503 11.474 1.00 91.90 ? 152 PHE A CD2 1 ATOM 1211 C CE1 . PHE A 1 149 ? 0.410 20.849 12.190 1.00 93.19 ? 152 PHE A CE1 1 ATOM 1212 C CE2 . PHE A 1 149 ? -0.241 23.175 12.190 1.00 93.21 ? 152 PHE A CE2 1 ATOM 1213 C CZ . PHE A 1 149 ? -0.498 21.845 12.546 1.00 94.17 ? 152 PHE A CZ 1 ATOM 1214 N N . GLN A 1 150 ? 0.909 22.595 8.062 1.00 73.92 ? 153 GLN A N 1 ATOM 1215 C CA . GLN A 1 150 ? -0.160 23.266 7.349 1.00 73.43 ? 153 GLN A CA 1 ATOM 1216 C C . GLN A 1 150 ? -1.150 23.806 8.386 1.00 71.10 ? 153 GLN A C 1 ATOM 1217 O O . GLN A 1 150 ? -1.889 23.061 9.035 1.00 69.20 ? 153 GLN A O 1 ATOM 1218 C CB . GLN A 1 150 ? -0.807 22.302 6.361 1.00 78.22 ? 153 GLN A CB 1 ATOM 1219 C CG . GLN A 1 150 ? -2.030 21.568 6.844 1.00 83.77 ? 153 GLN A CG 1 ATOM 1220 C CD . GLN A 1 150 ? -3.294 22.130 6.216 1.00 88.04 ? 153 GLN A CD 1 ATOM 1221 O OE1 . GLN A 1 150 ? -4.368 21.523 6.318 1.00 90.95 ? 153 GLN A OE1 1 ATOM 1222 N NE2 . GLN A 1 150 ? -3.175 23.299 5.558 1.00 85.35 ? 153 GLN A NE2 1 ATOM 1223 N N . VAL A 1 151 ? -1.118 25.125 8.552 1.00 68.85 ? 154 VAL A N 1 ATOM 1224 C CA . VAL A 1 151 ? -1.953 25.822 9.523 1.00 65.70 ? 154 VAL A CA 1 ATOM 1225 C C . VAL A 1 151 ? -3.456 25.568 9.387 1.00 64.98 ? 154 VAL A C 1 ATOM 1226 O O . VAL A 1 151 ? -4.003 25.492 8.291 1.00 64.62 ? 154 VAL A O 1 ATOM 1227 C CB . VAL A 1 151 ? -1.648 27.347 9.488 1.00 62.60 ? 154 VAL A CB 1 ATOM 1228 C CG1 . VAL A 1 151 ? -2.426 28.072 10.569 1.00 61.58 ? 154 VAL A CG1 1 ATOM 1229 C CG2 . VAL A 1 151 ? -0.156 27.573 9.686 1.00 60.04 ? 154 VAL A CG2 1 ATOM 1230 N N . THR A 1 152 ? -4.113 25.459 10.533 1.00 65.29 ? 155 THR A N 1 ATOM 1231 C CA . THR A 1 152 ? -5.534 25.177 10.601 1.00 64.53 ? 155 THR A CA 1 ATOM 1232 C C . THR A 1 152 ? -6.392 26.253 11.245 1.00 64.87 ? 155 THR A C 1 ATOM 1233 O O . THR A 1 152 ? -7.576 26.406 10.926 1.00 64.89 ? 155 THR A O 1 ATOM 1234 C CB . THR A 1 152 ? -5.726 23.885 11.349 1.00 64.29 ? 155 THR A CB 1 ATOM 1235 O OG1 . THR A 1 152 ? -5.747 22.823 10.390 1.00 61.77 ? 155 THR A OG1 1 ATOM 1236 C CG2 . THR A 1 152 ? -7.008 23.927 12.227 1.00 65.46 ? 155 THR A CG2 1 ATOM 1237 N N . ASP A 1 153 ? -5.809 26.966 12.192 1.00 63.64 ? 156 ASP A N 1 ATOM 1238 C CA . ASP A 1 153 ? -6.544 28.022 12.828 1.00 62.17 ? 156 ASP A CA 1 ATOM 1239 C C . ASP A 1 153 ? -6.975 28.953 11.692 1.00 61.82 ? 156 ASP A C 1 ATOM 1240 O O . ASP A 1 153 ? -6.195 29.277 10.782 1.00 63.85 ? 156 ASP A O 1 ATOM 1241 C CB . ASP A 1 153 ? -5.652 28.764 13.827 1.00 62.81 ? 156 ASP A CB 1 ATOM 1242 C CG . ASP A 1 153 ? -5.044 27.837 14.875 1.00 64.17 ? 156 ASP A CG 1 ATOM 1243 O OD1 . ASP A 1 153 ? -5.529 26.687 15.012 1.00 64.02 ? 156 ASP A OD1 1 ATOM 1244 O OD2 . ASP A 1 153 ? -4.084 28.267 15.564 1.00 63.77 ? 156 ASP A OD2 1 ATOM 1245 N N . PRO A 1 154 ? -8.236 29.377 11.716 1.00 59.28 ? 157 PRO A N 1 ATOM 1246 C CA . PRO A 1 154 ? -8.775 30.268 10.696 1.00 57.57 ? 157 PRO A CA 1 ATOM 1247 C C . PRO A 1 154 ? -7.991 31.547 10.713 1.00 57.52 ? 157 PRO A C 1 ATOM 1248 O O . PRO A 1 154 ? -7.541 32.002 11.760 1.00 57.62 ? 157 PRO A O 1 ATOM 1249 C CB . PRO A 1 154 ? -10.191 30.523 11.169 1.00 56.79 ? 157 PRO A CB 1 ATOM 1250 C CG . PRO A 1 154 ? -10.497 29.320 11.993 1.00 60.28 ? 157 PRO A CG 1 ATOM 1251 C CD . PRO A 1 154 ? -9.237 29.096 12.745 1.00 58.53 ? 157 PRO A CD 1 ATOM 1252 N N . PRO A 1 155 ? -7.798 32.145 9.548 1.00 57.98 ? 158 PRO A N 1 ATOM 1253 C CA . PRO A 1 155 ? -7.057 33.405 9.460 1.00 57.56 ? 158 PRO A CA 1 ATOM 1254 C C . PRO A 1 155 ? -7.776 34.511 10.239 1.00 57.17 ? 158 PRO A C 1 ATOM 1255 O O . PRO A 1 155 ? -8.959 34.776 10.008 1.00 57.66 ? 158 PRO A O 1 ATOM 1256 C CB . PRO A 1 155 ? -7.038 33.676 7.967 1.00 57.22 ? 158 PRO A CB 1 ATOM 1257 C CG . PRO A 1 155 ? -6.927 32.279 7.408 1.00 58.75 ? 158 PRO A CG 1 ATOM 1258 C CD . PRO A 1 155 ? -7.936 31.514 8.226 1.00 57.93 ? 158 PRO A CD 1 ATOM 1259 N N . GLN A 1 156 ? -7.059 35.146 11.161 1.00 55.82 ? 159 GLN A N 1 ATOM 1260 C CA . GLN A 1 156 ? -7.623 36.221 11.966 1.00 53.56 ? 159 GLN A CA 1 ATOM 1261 C C . GLN A 1 156 ? -7.456 37.569 11.274 1.00 53.07 ? 159 GLN A C 1 ATOM 1262 O O . GLN A 1 156 ? -6.537 37.758 10.461 1.00 54.03 ? 159 GLN A O 1 ATOM 1263 C CB . GLN A 1 156 ? -6.948 36.244 13.332 1.00 52.74 ? 159 GLN A CB 1 ATOM 1264 C CG . GLN A 1 156 ? -7.140 34.944 14.047 1.00 54.08 ? 159 GLN A CG 1 ATOM 1265 C CD . GLN A 1 156 ? -8.598 34.538 14.032 1.00 55.35 ? 159 GLN A CD 1 ATOM 1266 O OE1 . GLN A 1 156 ? -9.446 35.212 14.619 1.00 55.39 ? 159 GLN A OE1 1 ATOM 1267 N NE2 . GLN A 1 156 ? -8.903 33.446 13.341 1.00 56.04 ? 159 GLN A NE2 1 ATOM 1268 N N . PRO A 1 157 ? -8.346 38.530 11.583 1.00 50.80 ? 160 PRO A N 1 ATOM 1269 C CA . PRO A 1 157 ? -8.289 39.867 10.983 1.00 48.80 ? 160 PRO A CA 1 ATOM 1270 C C . PRO A 1 157 ? -6.970 40.598 11.211 1.00 49.61 ? 160 PRO A C 1 ATOM 1271 O O . PRO A 1 157 ? -6.493 41.325 10.332 1.00 50.54 ? 160 PRO A O 1 ATOM 1272 C CB . PRO A 1 157 ? -9.478 40.580 11.618 1.00 46.94 ? 160 PRO A CB 1 ATOM 1273 C CG . PRO A 1 157 ? -9.693 39.842 12.886 1.00 46.26 ? 160 PRO A CG 1 ATOM 1274 C CD . PRO A 1 157 ? -9.488 38.419 12.501 1.00 47.86 ? 160 PRO A CD 1 ATOM 1275 N N . GLU A 1 158 ? -6.377 40.415 12.387 1.00 49.10 ? 161 GLU A N 1 ATOM 1276 C CA . GLU A 1 158 ? -5.115 41.067 12.663 1.00 46.91 ? 161 GLU A CA 1 ATOM 1277 C C . GLU A 1 158 ? -4.054 40.454 11.754 1.00 47.18 ? 161 GLU A C 1 ATOM 1278 O O . GLU A 1 158 ? -3.176 41.150 11.245 1.00 48.17 ? 161 GLU A O 1 ATOM 1279 C CB . GLU A 1 158 ? -4.741 40.898 14.132 1.00 47.73 ? 161 GLU A CB 1 ATOM 1280 C CG . GLU A 1 158 ? -5.682 41.620 15.078 1.00 47.77 ? 161 GLU A CG 1 ATOM 1281 C CD . GLU A 1 158 ? -6.731 40.699 15.655 1.00 49.45 ? 161 GLU A CD 1 ATOM 1282 O OE1 . GLU A 1 158 ? -7.079 39.717 14.949 1.00 48.72 ? 161 GLU A OE1 1 ATOM 1283 O OE2 . GLU A 1 158 ? -7.199 40.963 16.804 1.00 49.20 ? 161 GLU A OE2 1 ATOM 1284 N N . THR A 1 159 ? -4.151 39.149 11.534 1.00 46.38 ? 162 THR A N 1 ATOM 1285 C CA . THR A 1 159 ? -3.202 38.456 10.670 1.00 46.34 ? 162 THR A CA 1 ATOM 1286 C C . THR A 1 159 ? -3.370 38.986 9.247 1.00 45.72 ? 162 THR A C 1 ATOM 1287 O O . THR A 1 159 ? -2.449 39.560 8.669 1.00 45.23 ? 162 THR A O 1 ATOM 1288 C CB . THR A 1 159 ? -3.459 36.944 10.647 1.00 46.98 ? 162 THR A CB 1 ATOM 1289 O OG1 . THR A 1 159 ? -3.659 36.459 11.980 1.00 48.73 ? 162 THR A OG1 1 ATOM 1290 C CG2 . THR A 1 159 ? -2.280 36.235 10.055 1.00 47.69 ? 162 THR A CG2 1 ATOM 1291 N N . LEU A 1 160 ? -4.562 38.801 8.691 1.00 45.92 ? 163 LEU A N 1 ATOM 1292 C CA . LEU A 1 160 ? -4.877 39.270 7.335 1.00 45.56 ? 163 LEU A CA 1 ATOM 1293 C C . LEU A 1 160 ? -4.476 40.737 7.118 1.00 45.86 ? 163 LEU A C 1 ATOM 1294 O O . LEU A 1 160 ? -3.845 41.091 6.115 1.00 45.95 ? 163 LEU A O 1 ATOM 1295 C CB . LEU A 1 160 ? -6.380 39.111 7.079 1.00 45.92 ? 163 LEU A CB 1 ATOM 1296 C CG . LEU A 1 160 ? -6.972 37.697 7.233 1.00 45.53 ? 163 LEU A CG 1 ATOM 1297 C CD1 . LEU A 1 160 ? -8.505 37.752 7.323 1.00 46.95 ? 163 LEU A CD1 1 ATOM 1298 C CD2 . LEU A 1 160 ? -6.540 36.848 6.074 1.00 41.09 ? 163 LEU A CD2 1 ATOM 1299 N N . ALA A 1 161 ? -4.859 41.586 8.065 1.00 45.37 ? 164 ALA A N 1 ATOM 1300 C CA . ALA A 1 161 ? -4.540 43.001 7.997 1.00 44.26 ? 164 ALA A CA 1 ATOM 1301 C C . ALA A 1 161 ? -3.055 43.177 7.742 1.00 44.62 ? 164 ALA A C 1 ATOM 1302 O O . ALA A 1 161 ? -2.652 43.883 6.815 1.00 43.70 ? 164 ALA A O 1 ATOM 1303 C CB . ALA A 1 161 ? -4.925 43.677 9.306 1.00 42.25 ? 164 ALA A CB 1 ATOM 1304 N N . VAL A 1 162 ? -2.256 42.509 8.571 1.00 45.75 ? 165 VAL A N 1 ATOM 1305 C CA . VAL A 1 162 ? -0.793 42.563 8.507 1.00 46.84 ? 165 VAL A CA 1 ATOM 1306 C C . VAL A 1 162 ? -0.178 41.923 7.266 1.00 48.42 ? 165 VAL A C 1 ATOM 1307 O O . VAL A 1 162 ? 0.817 42.416 6.728 1.00 48.77 ? 165 VAL A O 1 ATOM 1308 C CB . VAL A 1 162 ? -0.169 41.885 9.731 1.00 45.87 ? 165 VAL A CB 1 ATOM 1309 C CG1 . VAL A 1 162 ? 1.318 41.925 9.631 1.00 44.30 ? 165 VAL A CG1 1 ATOM 1310 C CG2 . VAL A 1 162 ? -0.628 42.568 10.987 1.00 45.84 ? 165 VAL A CG2 1 ATOM 1311 N N . MET A 1 163 ? -0.741 40.808 6.825 1.00 49.70 ? 166 MET A N 1 ATOM 1312 C CA . MET A 1 163 ? -0.205 40.168 5.638 1.00 51.44 ? 166 MET A CA 1 ATOM 1313 C C . MET A 1 163 ? -0.297 41.168 4.492 1.00 53.52 ? 166 MET A C 1 ATOM 1314 O O . MET A 1 163 ? 0.697 41.447 3.801 1.00 54.59 ? 166 MET A O 1 ATOM 1315 C CB . MET A 1 163 ? -1.006 38.918 5.300 1.00 49.12 ? 166 MET A CB 1 ATOM 1316 C CG . MET A 1 163 ? -0.822 37.796 6.283 1.00 50.69 ? 166 MET A CG 1 ATOM 1317 S SD . MET A 1 163 ? -1.472 36.226 5.663 1.00 53.58 ? 166 MET A SD 1 ATOM 1318 C CE . MET A 1 163 ? -3.107 36.263 6.347 1.00 58.04 ? 166 MET A CE 1 ATOM 1319 N N . SER A 1 164 ? -1.502 41.708 4.311 1.00 54.27 ? 167 SER A N 1 ATOM 1320 C CA . SER A 1 164 ? -1.770 42.691 3.274 1.00 55.06 ? 167 SER A CA 1 ATOM 1321 C C . SER A 1 164 ? -0.719 43.805 3.373 1.00 55.72 ? 167 SER A C 1 ATOM 1322 O O . SER A 1 164 ? -0.053 44.152 2.393 1.00 56.22 ? 167 SER A O 1 ATOM 1323 C CB . SER A 1 164 ? -3.171 43.260 3.479 1.00 55.95 ? 167 SER A CB 1 ATOM 1324 O OG . SER A 1 164 ? -3.661 43.844 2.289 1.00 59.57 ? 167 SER A OG 1 ATOM 1325 N N . TRP A 1 165 ? -0.566 44.345 4.577 1.00 55.72 ? 168 TRP A N 1 ATOM 1326 C CA . TRP A 1 165 ? 0.401 45.403 4.835 1.00 54.94 ? 168 TRP A CA 1 ATOM 1327 C C . TRP A 1 165 ? 1.811 45.002 4.391 1.00 55.91 ? 168 TRP A C 1 ATOM 1328 O O . TRP A 1 165 ? 2.534 45.815 3.823 1.00 55.84 ? 168 TRP A O 1 ATOM 1329 C CB . TRP A 1 165 ? 0.368 45.751 6.332 1.00 53.99 ? 168 TRP A CB 1 ATOM 1330 C CG . TRP A 1 165 ? 1.374 46.795 6.845 1.00 51.95 ? 168 TRP A CG 1 ATOM 1331 C CD1 . TRP A 1 165 ? 1.679 48.012 6.285 1.00 50.27 ? 168 TRP A CD1 1 ATOM 1332 C CD2 . TRP A 1 165 ? 2.136 46.720 8.068 1.00 50.85 ? 168 TRP A CD2 1 ATOM 1333 N NE1 . TRP A 1 165 ? 2.574 48.695 7.082 1.00 49.25 ? 168 TRP A NE1 1 ATOM 1334 C CE2 . TRP A 1 165 ? 2.873 47.926 8.179 1.00 51.19 ? 168 TRP A CE2 1 ATOM 1335 C CE3 . TRP A 1 165 ? 2.266 45.746 9.080 1.00 50.39 ? 168 TRP A CE3 1 ATOM 1336 C CZ2 . TRP A 1 165 ? 3.733 48.185 9.265 1.00 53.36 ? 168 TRP A CZ2 1 ATOM 1337 C CZ3 . TRP A 1 165 ? 3.120 46.004 10.159 1.00 51.02 ? 168 TRP A CZ3 1 ATOM 1338 C CH2 . TRP A 1 165 ? 3.843 47.216 10.240 1.00 52.75 ? 168 TRP A CH2 1 ATOM 1339 N N . LEU A 1 166 ? 2.207 43.756 4.625 1.00 58.10 ? 169 LEU A N 1 ATOM 1340 C CA . LEU A 1 166 ? 3.555 43.333 4.237 1.00 60.28 ? 169 LEU A CA 1 ATOM 1341 C C . LEU A 1 166 ? 3.731 43.325 2.718 1.00 60.80 ? 169 LEU A C 1 ATOM 1342 O O . LEU A 1 166 ? 4.855 43.371 2.198 1.00 59.72 ? 169 LEU A O 1 ATOM 1343 C CB . LEU A 1 166 ? 3.871 41.949 4.825 1.00 61.00 ? 169 LEU A CB 1 ATOM 1344 C CG . LEU A 1 166 ? 3.777 41.803 6.352 1.00 60.93 ? 169 LEU A CG 1 ATOM 1345 C CD1 . LEU A 1 166 ? 4.642 40.636 6.787 1.00 61.62 ? 169 LEU A CD1 1 ATOM 1346 C CD2 . LEU A 1 166 ? 4.254 43.070 7.049 1.00 59.46 ? 169 LEU A CD2 1 ATOM 1347 N N . LYS A 1 167 ? 2.605 43.281 2.018 1.00 61.42 ? 170 LYS A N 1 ATOM 1348 C CA . LYS A 1 167 ? 2.598 43.277 0.563 1.00 64.50 ? 170 LYS A CA 1 ATOM 1349 C C . LYS A 1 167 ? 2.565 44.705 0.007 1.00 63.36 ? 170 LYS A C 1 ATOM 1350 O O . LYS A 1 167 ? 3.129 44.996 -1.055 1.00 63.88 ? 170 LYS A O 1 ATOM 1351 C CB . LYS A 1 167 ? 1.368 42.524 0.070 1.00 68.50 ? 170 LYS A CB 1 ATOM 1352 C CG . LYS A 1 167 ? 1.319 41.050 0.452 1.00 73.67 ? 170 LYS A CG 1 ATOM 1353 C CD . LYS A 1 167 ? 2.198 40.208 -0.476 1.00 79.44 ? 170 LYS A CD 1 ATOM 1354 C CE . LYS A 1 167 ? 1.846 38.722 -0.363 1.00 84.24 ? 170 LYS A CE 1 ATOM 1355 N NZ . LYS A 1 167 ? 2.564 37.864 -1.355 1.00 87.26 ? 170 LYS A NZ 1 ATOM 1356 N N . THR A 1 168 ? 1.893 45.585 0.744 1.00 61.32 ? 171 THR A N 1 ATOM 1357 C CA . THR A 1 168 ? 1.738 46.988 0.385 1.00 58.44 ? 171 THR A CA 1 ATOM 1358 C C . THR A 1 168 ? 3.028 47.817 0.257 1.00 57.58 ? 171 THR A C 1 ATOM 1359 O O . THR A 1 168 ? 3.090 48.726 -0.565 1.00 58.53 ? 171 THR A O 1 ATOM 1360 C CB . THR A 1 168 ? 0.826 47.680 1.398 1.00 57.53 ? 171 THR A CB 1 ATOM 1361 O OG1 . THR A 1 168 ? -0.395 46.942 1.518 1.00 57.10 ? 171 THR A OG1 1 ATOM 1362 C CG2 . THR A 1 168 ? 0.513 49.090 0.955 1.00 57.99 ? 171 THR A CG2 1 ATOM 1363 N N . TYR A 1 169 ? 4.048 47.523 1.059 1.00 56.19 ? 172 TYR A N 1 ATOM 1364 C CA . TYR A 1 169 ? 5.297 48.281 0.998 1.00 57.43 ? 172 TYR A CA 1 ATOM 1365 C C . TYR A 1 169 ? 6.510 47.354 0.795 1.00 59.27 ? 172 TYR A C 1 ATOM 1366 O O . TYR A 1 169 ? 6.442 46.172 1.132 1.00 61.73 ? 172 TYR A O 1 ATOM 1367 C CB . TYR A 1 169 ? 5.479 49.112 2.286 1.00 57.32 ? 172 TYR A CB 1 ATOM 1368 C CG . TYR A 1 169 ? 4.449 50.223 2.516 1.00 58.16 ? 172 TYR A CG 1 ATOM 1369 C CD1 . TYR A 1 169 ? 4.544 51.432 1.833 1.00 58.39 ? 172 TYR A CD1 1 ATOM 1370 C CD2 . TYR A 1 169 ? 3.365 50.055 3.393 1.00 57.24 ? 172 TYR A CD2 1 ATOM 1371 C CE1 . TYR A 1 169 ? 3.589 52.447 2.001 1.00 57.55 ? 172 TYR A CE1 1 ATOM 1372 C CE2 . TYR A 1 169 ? 2.405 51.075 3.568 1.00 55.41 ? 172 TYR A CE2 1 ATOM 1373 C CZ . TYR A 1 169 ? 2.528 52.264 2.858 1.00 56.22 ? 172 TYR A CZ 1 ATOM 1374 O OH . TYR A 1 169 ? 1.581 53.262 2.942 1.00 56.37 ? 172 TYR A OH 1 ATOM 1375 N N . PRO A 1 170 ? 7.631 47.881 0.233 1.00 59.91 ? 173 PRO A N 1 ATOM 1376 C CA . PRO A 1 170 ? 8.913 47.201 -0.062 1.00 58.97 ? 173 PRO A CA 1 ATOM 1377 C C . PRO A 1 170 ? 9.769 46.972 1.171 1.00 57.58 ? 173 PRO A C 1 ATOM 1378 O O . PRO A 1 170 ? 10.970 47.270 1.146 1.00 59.00 ? 173 PRO A O 1 ATOM 1379 C CB . PRO A 1 170 ? 9.642 48.172 -1.000 1.00 58.48 ? 173 PRO A CB 1 ATOM 1380 C CG . PRO A 1 170 ? 8.591 49.075 -1.487 1.00 61.28 ? 173 PRO A CG 1 ATOM 1381 C CD . PRO A 1 170 ? 7.669 49.246 -0.312 1.00 60.68 ? 173 PRO A CD 1 ATOM 1382 N N . PHE A 1 171 ? 9.167 46.465 2.241 1.00 55.91 ? 174 PHE A N 1 ATOM 1383 C CA . PHE A 1 171 ? 9.906 46.240 3.468 1.00 53.74 ? 174 PHE A CA 1 ATOM 1384 C C . PHE A 1 171 ? 11.153 45.430 3.242 1.00 53.25 ? 174 PHE A C 1 ATOM 1385 O O . PHE A 1 171 ? 11.122 44.371 2.623 1.00 53.78 ? 174 PHE A O 1 ATOM 1386 C CB . PHE A 1 171 ? 9.015 45.575 4.495 1.00 52.50 ? 174 PHE A CB 1 ATOM 1387 C CG . PHE A 1 171 ? 7.978 46.491 5.040 1.00 51.43 ? 174 PHE A CG 1 ATOM 1388 C CD1 . PHE A 1 171 ? 8.353 47.600 5.794 1.00 51.59 ? 174 PHE A CD1 1 ATOM 1389 C CD2 . PHE A 1 171 ? 6.629 46.276 4.777 1.00 51.35 ? 174 PHE A CD2 1 ATOM 1390 C CE1 . PHE A 1 171 ? 7.399 48.491 6.282 1.00 51.35 ? 174 PHE A CE1 1 ATOM 1391 C CE2 . PHE A 1 171 ? 5.661 47.160 5.259 1.00 50.36 ? 174 PHE A CE2 1 ATOM 1392 C CZ . PHE A 1 171 ? 6.049 48.272 6.014 1.00 50.47 ? 174 PHE A CZ 1 ATOM 1393 N N . VAL A 1 172 ? 12.250 45.965 3.755 1.00 52.29 ? 175 VAL A N 1 ATOM 1394 C CA . VAL A 1 172 ? 13.558 45.360 3.634 1.00 53.54 ? 175 VAL A CA 1 ATOM 1395 C C . VAL A 1 172 ? 13.957 44.602 4.907 1.00 54.87 ? 175 VAL A C 1 ATOM 1396 O O . VAL A 1 172 ? 14.297 43.422 4.842 1.00 56.84 ? 175 VAL A O 1 ATOM 1397 C CB . VAL A 1 172 ? 14.601 46.451 3.311 1.00 53.22 ? 175 VAL A CB 1 ATOM 1398 C CG1 . VAL A 1 172 ? 16.016 45.893 3.441 1.00 51.74 ? 175 VAL A CG1 1 ATOM 1399 C CG2 . VAL A 1 172 ? 14.348 46.998 1.901 1.00 50.27 ? 175 VAL A CG2 1 ATOM 1400 N N . LEU A 1 173 ? 13.916 45.283 6.053 1.00 52.87 ? 176 LEU A N 1 ATOM 1401 C CA . LEU A 1 173 ? 14.253 44.688 7.349 1.00 48.90 ? 176 LEU A CA 1 ATOM 1402 C C . LEU A 1 173 ? 13.071 44.881 8.307 1.00 49.27 ? 176 LEU A C 1 ATOM 1403 O O . LEU A 1 173 ? 12.301 45.828 8.176 1.00 50.69 ? 176 LEU A O 1 ATOM 1404 C CB . LEU A 1 173 ? 15.492 45.367 7.922 1.00 44.33 ? 176 LEU A CB 1 ATOM 1405 C CG . LEU A 1 173 ? 16.126 44.740 9.158 1.00 43.03 ? 176 LEU A CG 1 ATOM 1406 C CD1 . LEU A 1 173 ? 16.332 43.256 8.933 1.00 41.53 ? 176 LEU A CD1 1 ATOM 1407 C CD2 . LEU A 1 173 ? 17.450 45.418 9.445 1.00 41.32 ? 176 LEU A CD2 1 ATOM 1408 N N . SER A 1 174 ? 12.921 43.994 9.274 1.00 48.77 ? 177 SER A N 1 ATOM 1409 C CA . SER A 1 174 ? 11.813 44.114 10.212 1.00 46.92 ? 177 SER A CA 1 ATOM 1410 C C . SER A 1 174 ? 12.119 43.333 11.471 1.00 47.45 ? 177 SER A C 1 ATOM 1411 O O . SER A 1 174 ? 13.018 42.502 11.478 1.00 47.46 ? 177 SER A O 1 ATOM 1412 C CB . SER A 1 174 ? 10.547 43.563 9.580 1.00 46.14 ? 177 SER A CB 1 ATOM 1413 O OG . SER A 1 174 ? 9.654 43.099 10.576 1.00 45.36 ? 177 SER A OG 1 ATOM 1414 N N . ALA A 1 175 ? 11.386 43.606 12.543 1.00 48.27 ? 178 ALA A N 1 ATOM 1415 C CA . ALA A 1 175 ? 11.586 42.874 13.798 1.00 47.97 ? 178 ALA A CA 1 ATOM 1416 C C . ALA A 1 175 ? 10.295 42.965 14.547 1.00 47.42 ? 178 ALA A C 1 ATOM 1417 O O . ALA A 1 175 ? 9.766 44.062 14.706 1.00 49.05 ? 178 ALA A O 1 ATOM 1418 C CB . ALA A 1 175 ? 12.689 43.494 14.631 1.00 47.21 ? 178 ALA A CB 1 ATOM 1419 N N . ASN A 1 176 ? 9.754 41.830 14.972 1.00 46.11 ? 179 ASN A N 1 ATOM 1420 C CA . ASN A 1 176 ? 8.525 41.885 15.731 1.00 45.86 ? 179 ASN A CA 1 ATOM 1421 C C . ASN A 1 176 ? 8.936 41.548 17.163 1.00 45.61 ? 179 ASN A C 1 ATOM 1422 O O . ASN A 1 176 ? 9.783 40.680 17.399 1.00 45.58 ? 179 ASN A O 1 ATOM 1423 C CB . ASN A 1 176 ? 7.434 40.969 15.109 1.00 47.03 ? 179 ASN A CB 1 ATOM 1424 C CG . ASN A 1 176 ? 7.540 39.511 15.514 1.00 47.85 ? 179 ASN A CG 1 ATOM 1425 O OD1 . ASN A 1 176 ? 7.521 39.192 16.696 1.00 52.02 ? 179 ASN A OD1 1 ATOM 1426 N ND2 . ASN A 1 176 ? 7.615 38.615 14.529 1.00 47.43 ? 179 ASN A ND2 1 ATOM 1427 N N . LEU A 1 177 ? 8.369 42.282 18.116 1.00 44.93 ? 180 LEU A N 1 ATOM 1428 C CA . LEU A 1 177 ? 8.743 42.130 19.512 1.00 43.97 ? 180 LEU A CA 1 ATOM 1429 C C . LEU A 1 177 ? 7.891 41.249 20.399 1.00 45.76 ? 180 LEU A C 1 ATOM 1430 O O . LEU A 1 177 ? 6.666 41.136 20.221 1.00 46.92 ? 180 LEU A O 1 ATOM 1431 C CB . LEU A 1 177 ? 8.864 43.513 20.137 1.00 41.42 ? 180 LEU A CB 1 ATOM 1432 C CG . LEU A 1 177 ? 9.570 44.505 19.202 1.00 40.81 ? 180 LEU A CG 1 ATOM 1433 C CD1 . LEU A 1 177 ? 9.648 45.829 19.896 1.00 40.14 ? 180 LEU A CD1 1 ATOM 1434 C CD2 . LEU A 1 177 ? 10.972 44.019 18.804 1.00 38.55 ? 180 LEU A CD2 1 ATOM 1435 N N . HIS A 1 178 ? 8.571 40.650 21.376 1.00 47.52 ? 181 HIS A N 1 ATOM 1436 C CA . HIS A 1 178 ? 7.965 39.744 22.337 1.00 47.22 ? 181 HIS A CA 1 ATOM 1437 C C . HIS A 1 178 ? 8.479 39.872 23.760 1.00 47.66 ? 181 HIS A C 1 ATOM 1438 O O . HIS A 1 178 ? 9.326 40.712 24.066 1.00 48.46 ? 181 HIS A O 1 ATOM 1439 C CB . HIS A 1 178 ? 8.188 38.319 21.885 1.00 47.15 ? 181 HIS A CB 1 ATOM 1440 C CG . HIS A 1 178 ? 7.356 37.935 20.713 1.00 47.30 ? 181 HIS A CG 1 ATOM 1441 N ND1 . HIS A 1 178 ? 6.161 37.271 20.870 1.00 47.50 ? 181 HIS A ND1 1 ATOM 1442 C CD2 . HIS A 1 178 ? 7.578 38.169 19.400 1.00 44.14 ? 181 HIS A CD2 1 ATOM 1443 C CE1 . HIS A 1 178 ? 5.685 37.111 19.651 1.00 47.17 ? 181 HIS A CE1 1 ATOM 1444 N NE2 . HIS A 1 178 ? 6.508 37.640 18.726 1.00 45.74 ? 181 HIS A NE2 1 ATOM 1445 N N . GLY A 1 179 ? 7.940 39.000 24.608 1.00 47.22 ? 182 GLY A N 1 ATOM 1446 C CA . GLY A 1 179 ? 8.289 38.940 26.011 1.00 46.09 ? 182 GLY A CA 1 ATOM 1447 C C . GLY A 1 179 ? 8.095 37.510 26.481 1.00 46.60 ? 182 GLY A C 1 ATOM 1448 O O . GLY A 1 179 ? 7.216 36.785 26.016 1.00 48.15 ? 182 GLY A O 1 ATOM 1449 N N . GLY A 1 180 ? 8.919 37.095 27.423 1.00 46.73 ? 183 GLY A N 1 ATOM 1450 C CA . GLY A 1 180 ? 8.835 35.736 27.907 1.00 46.50 ? 183 GLY A CA 1 ATOM 1451 C C . GLY A 1 180 ? 10.241 35.175 27.900 1.00 46.33 ? 183 GLY A C 1 ATOM 1452 O O . GLY A 1 180 ? 10.496 34.079 28.387 1.00 47.66 ? 183 GLY A O 1 ATOM 1453 N N . SER A 1 181 ? 11.163 35.940 27.330 1.00 45.39 ? 184 SER A N 1 ATOM 1454 C CA . SER A 1 181 ? 12.551 35.537 27.277 1.00 44.47 ? 184 SER A CA 1 ATOM 1455 C C . SER A 1 181 ? 13.395 36.709 26.865 1.00 44.61 ? 184 SER A C 1 ATOM 1456 O O . SER A 1 181 ? 12.874 37.784 26.589 1.00 47.20 ? 184 SER A O 1 ATOM 1457 C CB . SER A 1 181 ? 12.755 34.414 26.287 1.00 44.86 ? 184 SER A CB 1 ATOM 1458 O OG . SER A 1 181 ? 14.017 33.827 26.527 1.00 49.16 ? 184 SER A OG 1 ATOM 1459 N N . LEU A 1 182 ? 14.704 36.504 26.813 1.00 44.69 ? 185 LEU A N 1 ATOM 1460 C CA . LEU A 1 182 ? 15.608 37.582 26.438 1.00 43.83 ? 185 LEU A CA 1 ATOM 1461 C C . LEU A 1 182 ? 16.588 37.070 25.400 1.00 45.28 ? 185 LEU A C 1 ATOM 1462 O O . LEU A 1 182 ? 17.636 36.515 25.734 1.00 47.02 ? 185 LEU A O 1 ATOM 1463 C CB . LEU A 1 182 ? 16.350 38.066 27.670 1.00 41.92 ? 185 LEU A CB 1 ATOM 1464 C CG . LEU A 1 182 ? 17.058 39.379 27.436 1.00 40.93 ? 185 LEU A CG 1 ATOM 1465 C CD1 . LEU A 1 182 ? 16.025 40.480 27.223 1.00 39.45 ? 185 LEU A CD1 1 ATOM 1466 C CD2 . LEU A 1 182 ? 17.948 39.672 28.620 1.00 38.84 ? 185 LEU A CD2 1 ATOM 1467 N N . VAL A 1 183 ? 16.238 37.251 24.134 1.00 45.52 ? 186 VAL A N 1 ATOM 1468 C CA . VAL A 1 183 ? 17.073 36.775 23.047 1.00 44.33 ? 186 VAL A CA 1 ATOM 1469 C C . VAL A 1 183 ? 16.461 37.223 21.753 1.00 44.93 ? 186 VAL A C 1 ATOM 1470 O O . VAL A 1 183 ? 15.271 37.488 21.687 1.00 46.33 ? 186 VAL A O 1 ATOM 1471 C CB . VAL A 1 183 ? 17.112 35.223 22.999 1.00 42.29 ? 186 VAL A CB 1 ATOM 1472 C CG1 . VAL A 1 183 ? 15.746 34.680 22.620 1.00 38.30 ? 186 VAL A CG1 1 ATOM 1473 C CG2 . VAL A 1 183 ? 18.144 34.748 21.986 1.00 42.36 ? 186 VAL A CG2 1 ATOM 1474 N N . VAL A 1 184 ? 17.280 37.337 20.723 1.00 45.03 ? 187 VAL A N 1 ATOM 1475 C CA . VAL A 1 184 ? 16.737 37.662 19.427 1.00 43.53 ? 187 VAL A CA 1 ATOM 1476 C C . VAL A 1 184 ? 16.832 36.334 18.643 1.00 44.70 ? 187 VAL A C 1 ATOM 1477 O O . VAL A 1 184 ? 17.893 35.707 18.463 1.00 42.97 ? 187 VAL A O 1 ATOM 1478 C CB . VAL A 1 184 ? 17.433 38.891 18.771 1.00 39.12 ? 187 VAL A CB 1 ATOM 1479 C CG1 . VAL A 1 184 ? 18.756 39.143 19.396 1.00 38.49 ? 187 VAL A CG1 1 ATOM 1480 C CG2 . VAL A 1 184 ? 17.551 38.692 17.313 1.00 35.28 ? 187 VAL A CG2 1 ATOM 1481 N N . ASN A 1 185 ? 15.633 35.894 18.289 1.00 45.64 ? 188 ASN A N 1 ATOM 1482 C CA . ASN A 1 185 ? 15.321 34.653 17.602 1.00 45.70 ? 188 ASN A CA 1 ATOM 1483 C C . ASN A 1 185 ? 15.265 34.871 16.091 1.00 46.38 ? 188 ASN A C 1 ATOM 1484 O O . ASN A 1 185 ? 14.616 35.803 15.612 1.00 48.90 ? 188 ASN A O 1 ATOM 1485 C CB . ASN A 1 185 ? 13.972 34.194 18.210 1.00 45.24 ? 188 ASN A CB 1 ATOM 1486 C CG . ASN A 1 185 ? 13.233 33.163 17.386 1.00 46.59 ? 188 ASN A CG 1 ATOM 1487 O OD1 . ASN A 1 185 ? 12.569 32.292 17.947 1.00 47.87 ? 188 ASN A OD1 1 ATOM 1488 N ND2 . ASN A 1 185 ? 13.299 33.271 16.065 1.00 47.24 ? 188 ASN A ND2 1 ATOM 1489 N N . TYR A 1 186 ? 15.954 34.029 15.331 1.00 45.91 ? 189 TYR A N 1 ATOM 1490 C CA . TYR A 1 186 ? 15.923 34.178 13.878 1.00 46.94 ? 189 TYR A CA 1 ATOM 1491 C C . TYR A 1 186 ? 15.537 32.879 13.154 1.00 46.74 ? 189 TYR A C 1 ATOM 1492 O O . TYR A 1 186 ? 15.538 31.796 13.738 1.00 46.48 ? 189 TYR A O 1 ATOM 1493 C CB . TYR A 1 186 ? 17.261 34.713 13.359 1.00 45.98 ? 189 TYR A CB 1 ATOM 1494 C CG . TYR A 1 186 ? 18.433 33.813 13.632 1.00 49.44 ? 189 TYR A CG 1 ATOM 1495 C CD1 . TYR A 1 186 ? 19.154 33.908 14.828 1.00 50.12 ? 189 TYR A CD1 1 ATOM 1496 C CD2 . TYR A 1 186 ? 18.788 32.815 12.716 1.00 50.48 ? 189 TYR A CD2 1 ATOM 1497 C CE1 . TYR A 1 186 ? 20.195 33.023 15.107 1.00 52.07 ? 189 TYR A CE1 1 ATOM 1498 C CE2 . TYR A 1 186 ? 19.824 31.923 12.983 1.00 51.02 ? 189 TYR A CE2 1 ATOM 1499 C CZ . TYR A 1 186 ? 20.519 32.030 14.177 1.00 52.57 ? 189 TYR A CZ 1 ATOM 1500 O OH . TYR A 1 186 ? 21.518 31.120 14.437 1.00 53.72 ? 189 TYR A OH 1 ATOM 1501 N N . PRO A 1 187 ? 15.190 32.981 11.867 1.00 47.33 ? 190 PRO A N 1 ATOM 1502 C CA . PRO A 1 187 ? 14.774 31.869 10.997 1.00 47.90 ? 190 PRO A CA 1 ATOM 1503 C C . PRO A 1 187 ? 15.737 30.684 10.765 1.00 48.34 ? 190 PRO A C 1 ATOM 1504 O O . PRO A 1 187 ? 16.967 30.846 10.723 1.00 47.96 ? 190 PRO A O 1 ATOM 1505 C CB . PRO A 1 187 ? 14.421 32.581 9.687 1.00 47.79 ? 190 PRO A CB 1 ATOM 1506 C CG . PRO A 1 187 ? 14.010 33.958 10.139 1.00 47.87 ? 190 PRO A CG 1 ATOM 1507 C CD . PRO A 1 187 ? 15.069 34.265 11.157 1.00 47.68 ? 190 PRO A CD 1 ATOM 1508 N N . PHE A 1 188 ? 15.173 29.488 10.583 1.00 48.96 ? 191 PHE A N 1 ATOM 1509 C CA . PHE A 1 188 ? 13.726 29.263 10.531 1.00 49.17 ? 191 PHE A CA 1 ATOM 1510 C C . PHE A 1 188 ? 13.170 28.957 11.919 1.00 50.96 ? 191 PHE A C 1 ATOM 1511 O O . PHE A 1 188 ? 13.914 28.532 12.814 1.00 51.79 ? 191 PHE A O 1 ATOM 1512 C CB . PHE A 1 188 ? 13.409 28.094 9.607 1.00 46.56 ? 191 PHE A CB 1 ATOM 1513 C CG . PHE A 1 188 ? 13.550 28.414 8.156 1.00 46.64 ? 191 PHE A CG 1 ATOM 1514 C CD1 . PHE A 1 188 ? 12.813 29.450 7.581 1.00 46.34 ? 191 PHE A CD1 1 ATOM 1515 C CD2 . PHE A 1 188 ? 14.386 27.660 7.348 1.00 45.71 ? 191 PHE A CD2 1 ATOM 1516 C CE1 . PHE A 1 188 ? 12.906 29.730 6.211 1.00 45.73 ? 191 PHE A CE1 1 ATOM 1517 C CE2 . PHE A 1 188 ? 14.486 27.932 5.984 1.00 46.78 ? 191 PHE A CE2 1 ATOM 1518 C CZ . PHE A 1 188 ? 13.740 28.972 5.413 1.00 45.85 ? 191 PHE A CZ 1 ATOM 1519 N N . ASP A 1 189 ? 11.859 29.158 12.084 1.00 51.01 ? 192 ASP A N 1 ATOM 1520 C CA . ASP A 1 189 ? 11.187 28.927 13.363 1.00 49.82 ? 192 ASP A CA 1 ATOM 1521 C C . ASP A 1 189 ? 10.757 27.493 13.571 1.00 50.49 ? 192 ASP A C 1 ATOM 1522 O O . ASP A 1 189 ? 10.417 27.102 14.690 1.00 50.50 ? 192 ASP A O 1 ATOM 1523 C CB . ASP A 1 189 ? 9.947 29.806 13.502 1.00 49.86 ? 192 ASP A CB 1 ATOM 1524 C CG . ASP A 1 189 ? 10.224 31.108 14.225 1.00 51.44 ? 192 ASP A CG 1 ATOM 1525 O OD1 . ASP A 1 189 ? 11.099 31.127 15.119 1.00 51.28 ? 192 ASP A OD1 1 ATOM 1526 O OD2 . ASP A 1 189 ? 9.546 32.114 13.911 1.00 54.76 ? 192 ASP A OD2 1 ATOM 1527 N N . ASP A 1 190 ? 10.737 26.716 12.497 1.00 49.97 ? 193 ASP A N 1 ATOM 1528 C CA . ASP A 1 190 ? 10.334 25.332 12.604 1.00 49.69 ? 193 ASP A CA 1 ATOM 1529 C C . ASP A 1 190 ? 11.054 24.487 11.571 1.00 51.18 ? 193 ASP A C 1 ATOM 1530 O O . ASP A 1 190 ? 11.912 24.973 10.842 1.00 50.73 ? 193 ASP A O 1 ATOM 1531 C CB . ASP A 1 190 ? 8.811 25.215 12.463 1.00 49.23 ? 193 ASP A CB 1 ATOM 1532 C CG . ASP A 1 190 ? 8.299 25.608 11.076 1.00 50.95 ? 193 ASP A CG 1 ATOM 1533 O OD1 . ASP A 1 190 ? 9.025 26.270 10.299 1.00 51.56 ? 193 ASP A OD1 1 ATOM 1534 O OD2 . ASP A 1 190 ? 7.141 25.253 10.769 1.00 48.82 ? 193 ASP A OD2 1 ATOM 1535 N N . ASP A 1 191 ? 10.705 23.213 11.517 1.00 52.70 ? 194 ASP A N 1 ATOM 1536 C CA . ASP A 1 191 ? 11.339 22.299 10.591 1.00 53.61 ? 194 ASP A CA 1 ATOM 1537 C C . ASP A 1 191 ? 10.388 21.191 10.191 1.00 54.37 ? 194 ASP A C 1 ATOM 1538 O O . ASP A 1 191 ? 9.389 20.938 10.852 1.00 55.76 ? 194 ASP A O 1 ATOM 1539 C CB . ASP A 1 191 ? 12.576 21.708 11.248 1.00 53.25 ? 194 ASP A CB 1 ATOM 1540 C CG . ASP A 1 191 ? 12.321 21.288 12.672 1.00 53.59 ? 194 ASP A CG 1 ATOM 1541 O OD1 . ASP A 1 191 ? 11.658 20.251 12.883 1.00 52.85 ? 194 ASP A OD1 1 ATOM 1542 O OD2 . ASP A 1 191 ? 12.768 22.012 13.587 1.00 54.44 ? 194 ASP A OD2 1 ATOM 1543 N N . GLU A 1 192 ? 10.714 20.525 9.100 1.00 54.54 ? 195 GLU A N 1 ATOM 1544 C CA . GLU A 1 192 ? 9.902 19.440 8.576 1.00 53.99 ? 195 GLU A CA 1 ATOM 1545 C C . GLU A 1 192 ? 9.496 18.440 9.655 1.00 51.45 ? 195 GLU A C 1 ATOM 1546 O O . GLU A 1 192 ? 8.417 17.866 9.606 1.00 49.88 ? 195 GLU A O 1 ATOM 1547 C CB . GLU A 1 192 ? 10.700 18.749 7.492 1.00 60.03 ? 195 GLU A CB 1 ATOM 1548 C CG . GLU A 1 192 ? 10.016 17.639 6.765 1.00 70.80 ? 195 GLU A CG 1 ATOM 1549 C CD . GLU A 1 192 ? 11.048 16.751 6.060 1.00 79.99 ? 195 GLU A CD 1 ATOM 1550 O OE1 . GLU A 1 192 ? 11.948 17.306 5.371 1.00 82.78 ? 195 GLU A OE1 1 ATOM 1551 O OE2 . GLU A 1 192 ? 10.967 15.501 6.200 1.00 83.92 ? 195 GLU A OE2 1 ATOM 1552 N N . GLN A 1 193 ? 10.360 18.245 10.639 1.00 49.55 ? 196 GLN A N 1 ATOM 1553 C CA . GLN A 1 193 ? 10.091 17.302 11.713 1.00 48.44 ? 196 GLN A CA 1 ATOM 1554 C C . GLN A 1 193 ? 9.318 17.898 12.894 1.00 47.43 ? 196 GLN A C 1 ATOM 1555 O O . GLN A 1 193 ? 8.802 17.169 13.742 1.00 48.03 ? 196 GLN A O 1 ATOM 1556 C CB . GLN A 1 193 ? 11.416 16.705 12.203 1.00 50.32 ? 196 GLN A CB 1 ATOM 1557 C CG . GLN A 1 193 ? 12.196 15.928 11.138 1.00 52.02 ? 196 GLN A CG 1 ATOM 1558 C CD . GLN A 1 193 ? 13.034 16.807 10.203 1.00 54.61 ? 196 GLN A CD 1 ATOM 1559 O OE1 . GLN A 1 193 ? 13.751 16.293 9.330 1.00 57.18 ? 196 GLN A OE1 1 ATOM 1560 N NE2 . GLN A 1 193 ? 12.957 18.127 10.382 1.00 54.43 ? 196 GLN A NE2 1 ATOM 1561 N N . GLY A 1 194 ? 9.254 19.223 12.955 1.00 46.51 ? 197 GLY A N 1 ATOM 1562 C CA . GLY A 1 194 ? 8.533 19.884 14.028 1.00 46.65 ? 197 GLY A CA 1 ATOM 1563 C C . GLY A 1 194 ? 9.141 19.663 15.394 1.00 47.43 ? 197 GLY A C 1 ATOM 1564 O O . GLY A 1 194 ? 8.436 19.437 16.379 1.00 47.51 ? 197 GLY A O 1 ATOM 1565 N N . ILE A 1 195 ? 10.462 19.743 15.462 1.00 46.90 ? 198 ILE A N 1 ATOM 1566 C CA . ILE A 1 195 ? 11.149 19.530 16.717 1.00 45.07 ? 198 ILE A CA 1 ATOM 1567 C C . ILE A 1 195 ? 12.135 20.661 16.967 1.00 46.30 ? 198 ILE A C 1 ATOM 1568 O O . ILE A 1 195 ? 12.382 21.479 16.077 1.00 46.71 ? 198 ILE A O 1 ATOM 1569 C CB . ILE A 1 195 ? 11.877 18.165 16.703 1.00 43.06 ? 198 ILE A CB 1 ATOM 1570 C CG1 . ILE A 1 195 ? 12.695 18.010 15.415 1.00 40.68 ? 198 ILE A CG1 1 ATOM 1571 C CG2 . ILE A 1 195 ? 10.871 17.053 16.774 1.00 40.46 ? 198 ILE A CG2 1 ATOM 1572 C CD1 . ILE A 1 195 ? 13.559 16.761 15.375 1.00 34.85 ? 198 ILE A CD1 1 ATOM 1573 N N . ALA A 1 196 ? 12.681 20.716 18.180 1.00 45.35 ? 199 ALA A N 1 ATOM 1574 C CA . ALA A 1 196 ? 13.632 21.754 18.535 1.00 44.19 ? 199 ALA A CA 1 ATOM 1575 C C . ALA A 1 196 ? 15.010 21.350 18.068 1.00 46.19 ? 199 ALA A C 1 ATOM 1576 O O . ALA A 1 196 ? 15.784 20.734 18.817 1.00 47.68 ? 199 ALA A O 1 ATOM 1577 C CB . ALA A 1 196 ? 13.641 21.974 20.026 1.00 43.28 ? 199 ALA A CB 1 ATOM 1578 N N . ILE A 1 197 ? 15.296 21.683 16.813 1.00 46.16 ? 200 ILE A N 1 ATOM 1579 C CA . ILE A 1 197 ? 16.588 21.413 16.184 1.00 45.65 ? 200 ILE A CA 1 ATOM 1580 C C . ILE A 1 197 ? 16.921 22.639 15.333 1.00 46.77 ? 200 ILE A C 1 ATOM 1581 O O . ILE A 1 197 ? 16.026 23.396 14.940 1.00 47.31 ? 200 ILE A O 1 ATOM 1582 C CB . ILE A 1 197 ? 16.559 20.134 15.281 1.00 44.13 ? 200 ILE A CB 1 ATOM 1583 C CG1 . ILE A 1 197 ? 15.530 20.283 14.163 1.00 44.31 ? 200 ILE A CG1 1 ATOM 1584 C CG2 . ILE A 1 197 ? 16.222 18.911 16.114 1.00 42.51 ? 200 ILE A CG2 1 ATOM 1585 C CD1 . ILE A 1 197 ? 15.434 19.083 13.244 1.00 43.19 ? 200 ILE A CD1 1 ATOM 1586 N N . TYR A 1 198 ? 18.199 22.863 15.064 1.00 47.73 ? 201 TYR A N 1 ATOM 1587 C CA . TYR A 1 198 ? 18.570 24.019 14.261 1.00 48.80 ? 201 TYR A CA 1 ATOM 1588 C C . TYR A 1 198 ? 17.959 23.884 12.869 1.00 50.06 ? 201 TYR A C 1 ATOM 1589 O O . TYR A 1 198 ? 18.183 22.881 12.198 1.00 52.10 ? 201 TYR A O 1 ATOM 1590 C CB . TYR A 1 198 ? 20.088 24.108 14.126 1.00 48.36 ? 201 TYR A CB 1 ATOM 1591 C CG . TYR A 1 198 ? 20.580 25.462 13.648 1.00 48.64 ? 201 TYR A CG 1 ATOM 1592 C CD1 . TYR A 1 198 ? 20.623 25.778 12.288 1.00 48.55 ? 201 TYR A CD1 1 ATOM 1593 C CD2 . TYR A 1 198 ? 20.980 26.436 14.560 1.00 46.43 ? 201 TYR A CD2 1 ATOM 1594 C CE1 . TYR A 1 198 ? 21.048 27.037 11.848 1.00 47.31 ? 201 TYR A CE1 1 ATOM 1595 C CE2 . TYR A 1 198 ? 21.410 27.690 14.136 1.00 48.01 ? 201 TYR A CE2 1 ATOM 1596 C CZ . TYR A 1 198 ? 21.441 27.993 12.781 1.00 47.74 ? 201 TYR A CZ 1 ATOM 1597 O OH . TYR A 1 198 ? 21.843 29.258 12.379 1.00 48.99 ? 201 TYR A OH 1 ATOM 1598 N N . SER A 1 199 ? 17.191 24.876 12.429 1.00 50.24 ? 202 SER A N 1 ATOM 1599 C CA . SER A 1 199 ? 16.599 24.811 11.096 1.00 50.94 ? 202 SER A CA 1 ATOM 1600 C C . SER A 1 199 ? 17.160 25.957 10.258 1.00 51.38 ? 202 SER A C 1 ATOM 1601 O O . SER A 1 199 ? 16.622 27.062 10.275 1.00 52.91 ? 202 SER A O 1 ATOM 1602 C CB . SER A 1 199 ? 15.083 24.919 11.195 1.00 50.25 ? 202 SER A CB 1 ATOM 1603 O OG . SER A 1 199 ? 14.506 24.860 9.906 1.00 52.46 ? 202 SER A OG 1 ATOM 1604 N N . LYS A 1 200 ? 18.226 25.690 9.509 1.00 51.78 ? 203 LYS A N 1 ATOM 1605 C CA . LYS A 1 200 ? 18.885 26.740 8.729 1.00 53.60 ? 203 LYS A CA 1 ATOM 1606 C C . LYS A 1 200 ? 18.233 27.276 7.463 1.00 53.94 ? 203 LYS A C 1 ATOM 1607 O O . LYS A 1 200 ? 17.785 26.539 6.588 1.00 52.97 ? 203 LYS A O 1 ATOM 1608 C CB . LYS A 1 200 ? 20.336 26.335 8.412 1.00 54.55 ? 203 LYS A CB 1 ATOM 1609 C CG . LYS A 1 200 ? 21.060 27.287 7.472 1.00 56.85 ? 203 LYS A CG 1 ATOM 1610 C CD . LYS A 1 200 ? 22.478 26.826 7.119 1.00 58.52 ? 203 LYS A CD 1 ATOM 1611 C CE . LYS A 1 200 ? 23.472 27.042 8.262 1.00 61.65 ? 203 LYS A CE 1 ATOM 1612 N NZ . LYS A 1 200 ? 24.883 27.122 7.738 1.00 64.40 ? 203 LYS A NZ 1 ATOM 1613 N N . SER A 1 201 ? 18.218 28.601 7.392 1.00 56.76 ? 204 SER A N 1 ATOM 1614 C CA . SER A 1 201 ? 17.667 29.363 6.274 1.00 56.19 ? 204 SER A CA 1 ATOM 1615 C C . SER A 1 201 ? 18.809 29.656 5.314 1.00 56.53 ? 204 SER A C 1 ATOM 1616 O O . SER A 1 201 ? 19.978 29.663 5.709 1.00 57.93 ? 204 SER A O 1 ATOM 1617 C CB . SER A 1 201 ? 17.140 30.694 6.788 1.00 55.10 ? 204 SER A CB 1 ATOM 1618 O OG . SER A 1 201 ? 18.149 31.313 7.589 1.00 53.74 ? 204 SER A OG 1 ATOM 1619 N N . PRO A 1 202 ? 18.489 29.906 4.043 1.00 55.14 ? 205 PRO A N 1 ATOM 1620 C CA . PRO A 1 202 ? 19.495 30.213 3.028 1.00 55.25 ? 205 PRO A CA 1 ATOM 1621 C C . PRO A 1 202 ? 20.313 31.415 3.472 1.00 57.43 ? 205 PRO A C 1 ATOM 1622 O O . PRO A 1 202 ? 21.513 31.519 3.186 1.00 59.30 ? 205 PRO A O 1 ATOM 1623 C CB . PRO A 1 202 ? 18.654 30.532 1.811 1.00 53.23 ? 205 PRO A CB 1 ATOM 1624 C CG . PRO A 1 202 ? 17.518 29.580 1.968 1.00 53.52 ? 205 PRO A CG 1 ATOM 1625 C CD . PRO A 1 202 ? 17.169 29.715 3.428 1.00 53.70 ? 205 PRO A CD 1 ATOM 1626 N N . ASP A 1 203 ? 19.654 32.320 4.190 1.00 57.27 ? 206 ASP A N 1 ATOM 1627 C CA . ASP A 1 203 ? 20.305 33.523 4.666 1.00 55.77 ? 206 ASP A CA 1 ATOM 1628 C C . ASP A 1 203 ? 20.802 33.463 6.080 1.00 55.96 ? 206 ASP A C 1 ATOM 1629 O O . ASP A 1 203 ? 20.971 34.496 6.725 1.00 57.23 ? 206 ASP A O 1 ATOM 1630 C CB . ASP A 1 203 ? 19.363 34.688 4.513 1.00 55.33 ? 206 ASP A CB 1 ATOM 1631 C CG . ASP A 1 203 ? 19.393 35.237 3.135 1.00 56.72 ? 206 ASP A CG 1 ATOM 1632 O OD1 . ASP A 1 203 ? 20.430 35.852 2.800 1.00 57.74 ? 206 ASP A OD1 1 ATOM 1633 O OD2 . ASP A 1 203 ? 18.412 35.029 2.387 1.00 57.12 ? 206 ASP A OD2 1 ATOM 1634 N N . ASP A 1 204 ? 21.054 32.252 6.557 1.00 55.83 ? 207 ASP A N 1 ATOM 1635 C CA . ASP A 1 204 ? 21.526 32.051 7.912 1.00 56.08 ? 207 ASP A CA 1 ATOM 1636 C C . ASP A 1 204 ? 22.576 33.056 8.378 1.00 56.95 ? 207 ASP A C 1 ATOM 1637 O O . ASP A 1 204 ? 22.454 33.663 9.448 1.00 57.74 ? 207 ASP A O 1 ATOM 1638 C CB . ASP A 1 204 ? 22.099 30.659 8.057 1.00 56.08 ? 207 ASP A CB 1 ATOM 1639 C CG . ASP A 1 204 ? 22.359 30.312 9.487 1.00 58.18 ? 207 ASP A CG 1 ATOM 1640 O OD1 . ASP A 1 204 ? 21.367 30.271 10.244 1.00 58.75 ? 207 ASP A OD1 1 ATOM 1641 O OD2 . ASP A 1 204 ? 23.538 30.097 9.850 1.00 58.88 ? 207 ASP A OD2 1 ATOM 1642 N N . ALA A 1 205 ? 23.615 33.235 7.578 1.00 58.13 ? 208 ALA A N 1 ATOM 1643 C CA . ALA A 1 205 ? 24.690 34.152 7.945 1.00 57.35 ? 208 ALA A CA 1 ATOM 1644 C C . ALA A 1 205 ? 24.234 35.576 8.233 1.00 56.63 ? 208 ALA A C 1 ATOM 1645 O O . ALA A 1 205 ? 24.558 36.145 9.281 1.00 57.23 ? 208 ALA A O 1 ATOM 1646 C CB . ALA A 1 205 ? 25.737 34.163 6.862 1.00 58.69 ? 208 ALA A CB 1 ATOM 1647 N N . VAL A 1 206 ? 23.494 36.153 7.294 1.00 55.01 ? 209 VAL A N 1 ATOM 1648 C CA . VAL A 1 206 ? 23.002 37.514 7.444 1.00 53.98 ? 209 VAL A CA 1 ATOM 1649 C C . VAL A 1 206 ? 22.153 37.608 8.699 1.00 53.17 ? 209 VAL A C 1 ATOM 1650 O O . VAL A 1 206 ? 22.327 38.517 9.510 1.00 54.46 ? 209 VAL A O 1 ATOM 1651 C CB . VAL A 1 206 ? 22.159 37.910 6.244 1.00 54.18 ? 209 VAL A CB 1 ATOM 1652 C CG1 . VAL A 1 206 ? 21.968 39.395 6.232 1.00 53.29 ? 209 VAL A CG1 1 ATOM 1653 C CG2 . VAL A 1 206 ? 22.838 37.417 4.957 1.00 58.41 ? 209 VAL A CG2 1 ATOM 1654 N N . PHE A 1 207 ? 21.234 36.662 8.862 1.00 50.99 ? 210 PHE A N 1 ATOM 1655 C CA . PHE A 1 207 ? 20.388 36.647 10.039 1.00 48.92 ? 210 PHE A CA 1 ATOM 1656 C C . PHE A 1 207 ? 21.201 36.647 11.308 1.00 50.72 ? 210 PHE A C 1 ATOM 1657 O O . PHE A 1 207 ? 20.910 37.412 12.222 1.00 52.82 ? 210 PHE A O 1 ATOM 1658 C CB . PHE A 1 207 ? 19.480 35.438 10.035 1.00 46.14 ? 210 PHE A CB 1 ATOM 1659 C CG . PHE A 1 207 ? 18.256 35.626 9.213 1.00 46.16 ? 210 PHE A CG 1 ATOM 1660 C CD1 . PHE A 1 207 ? 17.416 36.709 9.446 1.00 47.05 ? 210 PHE A CD1 1 ATOM 1661 C CD2 . PHE A 1 207 ? 17.938 34.738 8.197 1.00 45.73 ? 210 PHE A CD2 1 ATOM 1662 C CE1 . PHE A 1 207 ? 16.276 36.907 8.676 1.00 46.80 ? 210 PHE A CE1 1 ATOM 1663 C CE2 . PHE A 1 207 ? 16.796 34.927 7.420 1.00 46.91 ? 210 PHE A CE2 1 ATOM 1664 C CZ . PHE A 1 207 ? 15.964 36.015 7.661 1.00 46.89 ? 210 PHE A CZ 1 ATOM 1665 N N . GLN A 1 208 ? 22.216 35.799 11.399 1.00 51.57 ? 211 GLN A N 1 ATOM 1666 C CA . GLN A 1 208 ? 23.005 35.816 12.623 1.00 53.13 ? 211 GLN A CA 1 ATOM 1667 C C . GLN A 1 208 ? 23.575 37.212 12.845 1.00 54.36 ? 211 GLN A C 1 ATOM 1668 O O . GLN A 1 208 ? 23.591 37.709 13.971 1.00 54.77 ? 211 GLN A O 1 ATOM 1669 C CB . GLN A 1 208 ? 24.141 34.810 12.567 1.00 53.59 ? 211 GLN A CB 1 ATOM 1670 C CG . GLN A 1 208 ? 23.689 33.385 12.638 1.00 55.32 ? 211 GLN A CG 1 ATOM 1671 C CD . GLN A 1 208 ? 24.864 32.432 12.739 1.00 57.93 ? 211 GLN A CD 1 ATOM 1672 O OE1 . GLN A 1 208 ? 25.678 32.526 13.672 1.00 56.75 ? 211 GLN A OE1 1 ATOM 1673 N NE2 . GLN A 1 208 ? 24.967 31.504 11.775 1.00 56.82 ? 211 GLN A NE2 1 ATOM 1674 N N . GLN A 1 209 ? 24.028 37.851 11.766 1.00 55.10 ? 212 GLN A N 1 ATOM 1675 C CA . GLN A 1 209 ? 24.595 39.194 11.861 1.00 55.64 ? 212 GLN A CA 1 ATOM 1676 C C . GLN A 1 209 ? 23.551 40.193 12.338 1.00 53.38 ? 212 GLN A C 1 ATOM 1677 O O . GLN A 1 209 ? 23.804 41.022 13.208 1.00 51.48 ? 212 GLN A O 1 ATOM 1678 C CB . GLN A 1 209 ? 25.154 39.624 10.502 1.00 60.32 ? 212 GLN A CB 1 ATOM 1679 C CG . GLN A 1 209 ? 26.548 40.210 10.611 1.00 66.45 ? 212 GLN A CG 1 ATOM 1680 C CD . GLN A 1 209 ? 27.391 39.451 11.646 1.00 72.42 ? 212 GLN A CD 1 ATOM 1681 O OE1 . GLN A 1 209 ? 27.708 38.262 11.475 1.00 73.99 ? 212 GLN A OE1 1 ATOM 1682 N NE2 . GLN A 1 209 ? 27.741 40.137 12.737 1.00 74.57 ? 212 GLN A NE2 1 ATOM 1683 N N . LEU A 1 210 ? 22.368 40.100 11.761 1.00 52.02 ? 213 LEU A N 1 ATOM 1684 C CA . LEU A 1 210 ? 21.288 40.977 12.136 1.00 51.75 ? 213 LEU A CA 1 ATOM 1685 C C . LEU A 1 210 ? 20.897 40.812 13.610 1.00 52.95 ? 213 LEU A C 1 ATOM 1686 O O . LEU A 1 210 ? 20.810 41.792 14.367 1.00 53.70 ? 213 LEU A O 1 ATOM 1687 C CB . LEU A 1 210 ? 20.091 40.691 11.241 1.00 50.96 ? 213 LEU A CB 1 ATOM 1688 C CG . LEU A 1 210 ? 20.269 41.094 9.775 1.00 51.29 ? 213 LEU A CG 1 ATOM 1689 C CD1 . LEU A 1 210 ? 19.069 40.640 8.969 1.00 49.63 ? 213 LEU A CD1 1 ATOM 1690 C CD2 . LEU A 1 210 ? 20.431 42.612 9.672 1.00 50.08 ? 213 LEU A CD2 1 ATOM 1691 N N . ALA A 1 211 ? 20.661 39.568 14.018 1.00 51.15 ? 214 ALA A N 1 ATOM 1692 C CA . ALA A 1 211 ? 20.262 39.297 15.384 1.00 48.24 ? 214 ALA A CA 1 ATOM 1693 C C . ALA A 1 211 ? 21.310 39.824 16.356 1.00 48.12 ? 214 ALA A C 1 ATOM 1694 O O . ALA A 1 211 ? 20.989 40.443 17.374 1.00 49.58 ? 214 ALA A O 1 ATOM 1695 C CB . ALA A 1 211 ? 20.067 37.821 15.571 1.00 46.37 ? 214 ALA A CB 1 ATOM 1696 N N . LEU A 1 212 ? 22.572 39.593 16.035 1.00 47.14 ? 215 LEU A N 1 ATOM 1697 C CA . LEU A 1 212 ? 23.646 40.037 16.902 1.00 47.41 ? 215 LEU A CA 1 ATOM 1698 C C . LEU A 1 212 ? 23.707 41.552 17.007 1.00 48.54 ? 215 LEU A C 1 ATOM 1699 O O . LEU A 1 212 ? 23.956 42.089 18.087 1.00 49.47 ? 215 LEU A O 1 ATOM 1700 C CB . LEU A 1 212 ? 24.975 39.515 16.385 1.00 47.11 ? 215 LEU A CB 1 ATOM 1701 C CG . LEU A 1 212 ? 26.198 40.012 17.142 1.00 48.12 ? 215 LEU A CG 1 ATOM 1702 C CD1 . LEU A 1 212 ? 26.277 39.372 18.522 1.00 47.65 ? 215 LEU A CD1 1 ATOM 1703 C CD2 . LEU A 1 212 ? 27.416 39.666 16.332 1.00 49.47 ? 215 LEU A CD2 1 ATOM 1704 N N . SER A 1 213 ? 23.482 42.243 15.889 1.00 49.10 ? 216 SER A N 1 ATOM 1705 C CA . SER A 1 213 ? 23.524 43.707 15.883 1.00 49.60 ? 216 SER A CA 1 ATOM 1706 C C . SER A 1 213 ? 22.661 44.274 17.027 1.00 51.65 ? 216 SER A C 1 ATOM 1707 O O . SER A 1 213 ? 23.005 45.281 17.669 1.00 53.76 ? 216 SER A O 1 ATOM 1708 C CB . SER A 1 213 ? 23.018 44.242 14.542 1.00 47.74 ? 216 SER A CB 1 ATOM 1709 O OG . SER A 1 213 ? 21.610 44.140 14.455 1.00 47.33 ? 216 SER A OG 1 ATOM 1710 N N . TYR A 1 214 ? 21.538 43.615 17.278 1.00 51.72 ? 217 TYR A N 1 ATOM 1711 C CA . TYR A 1 214 ? 20.648 44.040 18.329 1.00 49.26 ? 217 TYR A CA 1 ATOM 1712 C C . TYR A 1 214 ? 21.090 43.510 19.681 1.00 50.28 ? 217 TYR A C 1 ATOM 1713 O O . TYR A 1 214 ? 21.246 44.289 20.624 1.00 51.87 ? 217 TYR A O 1 ATOM 1714 C CB . TYR A 1 214 ? 19.242 43.552 18.043 1.00 47.76 ? 217 TYR A CB 1 ATOM 1715 C CG . TYR A 1 214 ? 18.220 44.107 18.988 1.00 47.30 ? 217 TYR A CG 1 ATOM 1716 C CD1 . TYR A 1 214 ? 18.092 43.615 20.275 1.00 49.29 ? 217 TYR A CD1 1 ATOM 1717 C CD2 . TYR A 1 214 ? 17.397 45.158 18.602 1.00 48.45 ? 217 TYR A CD2 1 ATOM 1718 C CE1 . TYR A 1 214 ? 17.162 44.163 21.164 1.00 51.22 ? 217 TYR A CE1 1 ATOM 1719 C CE2 . TYR A 1 214 ? 16.466 45.715 19.473 1.00 48.31 ? 217 TYR A CE2 1 ATOM 1720 C CZ . TYR A 1 214 ? 16.348 45.220 20.758 1.00 49.40 ? 217 TYR A CZ 1 ATOM 1721 O OH . TYR A 1 214 ? 15.436 45.796 21.635 1.00 47.13 ? 217 TYR A OH 1 ATOM 1722 N N . SER A 1 215 ? 21.293 42.194 19.787 1.00 49.84 ? 218 SER A N 1 ATOM 1723 C CA . SER A 1 215 ? 21.676 41.596 21.073 1.00 49.74 ? 218 SER A CA 1 ATOM 1724 C C . SER A 1 215 ? 22.993 42.112 21.647 1.00 51.36 ? 218 SER A C 1 ATOM 1725 O O . SER A 1 215 ? 23.166 42.215 22.863 1.00 50.26 ? 218 SER A O 1 ATOM 1726 C CB . SER A 1 215 ? 21.709 40.059 20.979 1.00 47.35 ? 218 SER A CB 1 ATOM 1727 O OG . SER A 1 215 ? 22.755 39.588 20.154 1.00 45.25 ? 218 SER A OG 1 ATOM 1728 N N . LYS A 1 216 ? 23.915 42.460 20.766 1.00 54.52 ? 219 LYS A N 1 ATOM 1729 C CA . LYS A 1 216 ? 25.210 42.945 21.201 1.00 56.53 ? 219 LYS A CA 1 ATOM 1730 C C . LYS A 1 216 ? 25.027 44.192 22.039 1.00 55.92 ? 219 LYS A C 1 ATOM 1731 O O . LYS A 1 216 ? 25.778 44.436 22.968 1.00 54.55 ? 219 LYS A O 1 ATOM 1732 C CB . LYS A 1 216 ? 26.073 43.276 19.987 1.00 60.73 ? 219 LYS A CB 1 ATOM 1733 C CG . LYS A 1 216 ? 27.569 43.064 20.205 1.00 67.66 ? 219 LYS A CG 1 ATOM 1734 C CD . LYS A 1 216 ? 28.411 43.661 19.058 1.00 72.15 ? 219 LYS A CD 1 ATOM 1735 C CE . LYS A 1 216 ? 27.804 43.382 17.671 1.00 73.47 ? 219 LYS A CE 1 ATOM 1736 N NZ . LYS A 1 216 ? 28.630 43.945 16.562 1.00 73.94 ? 219 LYS A NZ 1 ATOM 1737 N N . GLU A 1 217 ? 24.004 44.966 21.703 1.00 56.71 ? 220 GLU A N 1 ATOM 1738 C CA . GLU A 1 217 ? 23.713 46.226 22.373 1.00 56.57 ? 220 GLU A CA 1 ATOM 1739 C C . GLU A 1 217 ? 22.860 46.117 23.624 1.00 55.70 ? 220 GLU A C 1 ATOM 1740 O O . GLU A 1 217 ? 22.786 47.062 24.394 1.00 56.40 ? 220 GLU A O 1 ATOM 1741 C CB . GLU A 1 217 ? 23.024 47.181 21.401 1.00 59.64 ? 220 GLU A CB 1 ATOM 1742 C CG . GLU A 1 217 ? 23.775 47.415 20.109 1.00 61.90 ? 220 GLU A CG 1 ATOM 1743 C CD . GLU A 1 217 ? 25.154 47.985 20.349 1.00 65.33 ? 220 GLU A CD 1 ATOM 1744 O OE1 . GLU A 1 217 ? 25.342 48.697 21.367 1.00 65.73 ? 220 GLU A OE1 1 ATOM 1745 O OE2 . GLU A 1 217 ? 26.042 47.726 19.506 1.00 67.51 ? 220 GLU A OE2 1 ATOM 1746 N N . ASN A 1 218 ? 22.168 45.003 23.815 1.00 53.69 ? 221 ASN A N 1 ATOM 1747 C CA . ASN A 1 218 ? 21.374 44.858 25.023 1.00 51.91 ? 221 ASN A CA 1 ATOM 1748 C C . ASN A 1 218 ? 22.262 44.019 25.907 1.00 53.68 ? 221 ASN A C 1 ATOM 1749 O O . ASN A 1 218 ? 22.337 42.803 25.745 1.00 53.61 ? 221 ASN A O 1 ATOM 1750 C CB . ASN A 1 218 ? 20.091 44.115 24.739 1.00 50.56 ? 221 ASN A CB 1 ATOM 1751 C CG . ASN A 1 218 ? 19.315 43.839 25.987 1.00 51.13 ? 221 ASN A CG 1 ATOM 1752 O OD1 . ASN A 1 218 ? 19.896 43.466 27.008 1.00 52.02 ? 221 ASN A OD1 1 ATOM 1753 N ND2 . ASN A 1 218 ? 17.993 44.008 25.925 1.00 51.45 ? 221 ASN A ND2 1 ATOM 1754 N N . LYS A 1 219 ? 22.937 44.667 26.845 1.00 56.44 ? 222 LYS A N 1 ATOM 1755 C CA . LYS A 1 219 ? 23.887 43.971 27.697 1.00 59.06 ? 222 LYS A CA 1 ATOM 1756 C C . LYS A 1 219 ? 23.491 42.628 28.285 1.00 58.20 ? 222 LYS A C 1 ATOM 1757 O O . LYS A 1 219 ? 24.114 41.614 27.976 1.00 58.59 ? 222 LYS A O 1 ATOM 1758 C CB . LYS A 1 219 ? 24.359 44.888 28.820 1.00 63.81 ? 222 LYS A CB 1 ATOM 1759 C CG . LYS A 1 219 ? 25.483 44.277 29.658 1.00 71.06 ? 222 LYS A CG 1 ATOM 1760 C CD . LYS A 1 219 ? 25.961 45.249 30.741 1.00 78.07 ? 222 LYS A CD 1 ATOM 1761 C CE . LYS A 1 219 ? 27.068 44.655 31.632 1.00 81.51 ? 222 LYS A CE 1 ATOM 1762 N NZ . LYS A 1 219 ? 27.492 45.600 32.732 1.00 83.92 ? 222 LYS A NZ 1 ATOM 1763 N N . LYS A 1 220 ? 22.468 42.613 29.133 1.00 57.54 ? 223 LYS A N 1 ATOM 1764 C CA . LYS A 1 220 ? 22.051 41.370 29.775 1.00 56.32 ? 223 LYS A CA 1 ATOM 1765 C C . LYS A 1 220 ? 21.618 40.267 28.810 1.00 54.62 ? 223 LYS A C 1 ATOM 1766 O O . LYS A 1 220 ? 21.669 39.083 29.147 1.00 52.72 ? 223 LYS A O 1 ATOM 1767 C CB . LYS A 1 220 ? 20.934 41.643 30.793 1.00 58.08 ? 223 LYS A CB 1 ATOM 1768 C CG . LYS A 1 220 ? 20.391 40.367 31.456 1.00 63.78 ? 223 LYS A CG 1 ATOM 1769 C CD . LYS A 1 220 ? 19.331 40.631 32.553 1.00 67.51 ? 223 LYS A CD 1 ATOM 1770 C CE . LYS A 1 220 ? 18.799 39.293 33.140 1.00 69.14 ? 223 LYS A CE 1 ATOM 1771 N NZ . LYS A 1 220 ? 17.924 39.427 34.357 1.00 70.18 ? 223 LYS A NZ 1 ATOM 1772 N N . MET A 1 221 ? 21.184 40.661 27.620 1.00 53.69 ? 224 MET A N 1 ATOM 1773 C CA . MET A 1 221 ? 20.747 39.706 26.617 1.00 53.67 ? 224 MET A CA 1 ATOM 1774 C C . MET A 1 221 ? 21.978 39.059 26.026 1.00 54.50 ? 224 MET A C 1 ATOM 1775 O O . MET A 1 221 ? 22.040 37.837 25.882 1.00 55.06 ? 224 MET A O 1 ATOM 1776 C CB . MET A 1 221 ? 19.980 40.410 25.499 1.00 53.16 ? 224 MET A CB 1 ATOM 1777 C CG . MET A 1 221 ? 19.419 39.464 24.449 1.00 51.47 ? 224 MET A CG 1 ATOM 1778 S SD . MET A 1 221 ? 18.721 40.324 23.044 1.00 51.51 ? 224 MET A SD 1 ATOM 1779 C CE . MET A 1 221 ? 17.377 41.200 23.791 1.00 47.04 ? 224 MET A CE 1 ATOM 1780 N N . TYR A 1 222 ? 22.947 39.907 25.683 1.00 55.03 ? 225 TYR A N 1 ATOM 1781 C CA . TYR A 1 222 ? 24.200 39.478 25.085 1.00 55.17 ? 225 TYR A CA 1 ATOM 1782 C C . TYR A 1 222 ? 24.877 38.439 25.938 1.00 56.89 ? 225 TYR A C 1 ATOM 1783 O O . TYR A 1 222 ? 25.602 37.581 25.425 1.00 58.73 ? 225 TYR A O 1 ATOM 1784 C CB . TYR A 1 222 ? 25.151 40.654 24.919 1.00 55.05 ? 225 TYR A CB 1 ATOM 1785 C CG . TYR A 1 222 ? 26.387 40.301 24.122 1.00 55.64 ? 225 TYR A CG 1 ATOM 1786 C CD1 . TYR A 1 222 ? 26.301 40.031 22.753 1.00 55.98 ? 225 TYR A CD1 1 ATOM 1787 C CD2 . TYR A 1 222 ? 27.648 40.228 24.734 1.00 57.53 ? 225 TYR A CD2 1 ATOM 1788 C CE1 . TYR A 1 222 ? 27.449 39.700 21.998 1.00 56.94 ? 225 TYR A CE1 1 ATOM 1789 C CE2 . TYR A 1 222 ? 28.810 39.890 23.992 1.00 57.01 ? 225 TYR A CE2 1 ATOM 1790 C CZ . TYR A 1 222 ? 28.701 39.634 22.624 1.00 57.70 ? 225 TYR A CZ 1 ATOM 1791 O OH . TYR A 1 222 ? 29.830 39.346 21.876 1.00 55.95 ? 225 TYR A OH 1 ATOM 1792 N N . GLN A 1 223 ? 24.648 38.523 27.244 1.00 58.50 ? 226 GLN A N 1 ATOM 1793 C CA . GLN A 1 223 ? 25.240 37.577 28.187 1.00 60.24 ? 226 GLN A CA 1 ATOM 1794 C C . GLN A 1 223 ? 24.764 36.153 27.968 1.00 58.62 ? 226 GLN A C 1 ATOM 1795 O O . GLN A 1 223 ? 25.424 35.215 28.388 1.00 60.49 ? 226 GLN A O 1 ATOM 1796 C CB . GLN A 1 223 ? 24.933 37.990 29.624 1.00 64.51 ? 226 GLN A CB 1 ATOM 1797 C CG . GLN A 1 223 ? 26.152 38.428 30.429 1.00 72.65 ? 226 GLN A CG 1 ATOM 1798 C CD . GLN A 1 223 ? 27.079 39.360 29.646 1.00 79.95 ? 226 GLN A CD 1 ATOM 1799 O OE1 . GLN A 1 223 ? 28.105 38.918 29.094 1.00 82.11 ? 226 GLN A OE1 1 ATOM 1800 N NE2 . GLN A 1 223 ? 26.719 40.654 29.581 1.00 81.89 ? 226 GLN A NE2 1 ATOM 1801 N N . GLY A 1 224 ? 23.608 35.988 27.334 1.00 56.48 ? 227 GLY A N 1 ATOM 1802 C CA . GLY A 1 224 ? 23.112 34.652 27.073 1.00 55.89 ? 227 GLY A CA 1 ATOM 1803 C C . GLY A 1 224 ? 22.179 34.039 28.102 1.00 56.89 ? 227 GLY A C 1 ATOM 1804 O O . GLY A 1 224 ? 21.510 33.060 27.776 1.00 57.64 ? 227 GLY A O 1 ATOM 1805 N N . SER A 1 225 ? 22.135 34.569 29.328 1.00 56.17 ? 228 SER A N 1 ATOM 1806 C CA . SER A 1 225 ? 21.237 34.034 30.357 1.00 57.00 ? 228 SER A CA 1 ATOM 1807 C C . SER A 1 225 ? 20.023 34.935 30.553 1.00 58.76 ? 228 SER A C 1 ATOM 1808 O O . SER A 1 225 ? 20.130 35.963 31.211 1.00 60.87 ? 228 SER A O 1 ATOM 1809 C CB . SER A 1 225 ? 21.961 33.911 31.693 1.00 57.05 ? 228 SER A CB 1 ATOM 1810 O OG . SER A 1 225 ? 22.704 32.711 31.790 1.00 59.38 ? 228 SER A OG 1 ATOM 1811 N N . PRO A 1 226 ? 18.849 34.557 30.003 1.00 59.26 ? 229 PRO A N 1 ATOM 1812 C CA . PRO A 1 226 ? 17.618 35.353 30.124 1.00 59.93 ? 229 PRO A CA 1 ATOM 1813 C C . PRO A 1 226 ? 17.146 35.634 31.560 1.00 62.44 ? 229 PRO A C 1 ATOM 1814 O O . PRO A 1 226 ? 16.833 36.781 31.911 1.00 63.63 ? 229 PRO A O 1 ATOM 1815 C CB . PRO A 1 226 ? 16.600 34.533 29.330 1.00 57.81 ? 229 PRO A CB 1 ATOM 1816 C CG . PRO A 1 226 ? 17.433 33.872 28.300 1.00 56.27 ? 229 PRO A CG 1 ATOM 1817 C CD . PRO A 1 226 ? 18.616 33.403 29.119 1.00 57.37 ? 229 PRO A CD 1 ATOM 1818 N N . CYS A 1 227 ? 17.078 34.589 32.379 1.00 62.40 ? 230 CYS A N 1 ATOM 1819 C CA . CYS A 1 227 ? 16.652 34.729 33.768 1.00 61.53 ? 230 CYS A CA 1 ATOM 1820 C C . CYS A 1 227 ? 16.963 33.409 34.432 1.00 60.05 ? 230 CYS A C 1 ATOM 1821 O O . CYS A 1 227 ? 16.153 32.512 34.421 1.00 59.92 ? 230 CYS A O 1 ATOM 1822 C CB . CYS A 1 227 ? 15.156 35.050 33.833 1.00 60.68 ? 230 CYS A CB 1 ATOM 1823 S SG . CYS A 1 227 ? 14.096 34.074 32.712 1.00 60.99 ? 230 CYS A SG 1 ATOM 1824 N N . LYS A 1 228 ? 18.158 33.300 35.000 1.00 59.96 ? 231 LYS A N 1 ATOM 1825 C CA . LYS A 1 228 ? 18.611 32.060 35.618 1.00 59.62 ? 231 LYS A CA 1 ATOM 1826 C C . LYS A 1 228 ? 17.691 31.338 36.591 1.00 58.89 ? 231 LYS A C 1 ATOM 1827 O O . LYS A 1 228 ? 17.709 30.120 36.645 1.00 57.46 ? 231 LYS A O 1 ATOM 1828 C CB . LYS A 1 228 ? 19.968 32.275 36.292 1.00 62.44 ? 231 LYS A CB 1 ATOM 1829 C CG . LYS A 1 228 ? 19.974 33.336 37.363 1.00 68.61 ? 231 LYS A CG 1 ATOM 1830 C CD . LYS A 1 228 ? 21.325 33.437 38.036 1.00 71.54 ? 231 LYS A CD 1 ATOM 1831 C CE . LYS A 1 228 ? 21.516 34.830 38.617 1.00 76.15 ? 231 LYS A CE 1 ATOM 1832 N NZ . LYS A 1 228 ? 22.868 35.011 39.228 1.00 78.35 ? 231 LYS A NZ 1 ATOM 1833 N N . ASP A 1 229 ? 16.880 32.063 37.353 1.00 60.58 ? 232 ASP A N 1 ATOM 1834 C CA . ASP A 1 229 ? 16.003 31.416 38.337 1.00 59.72 ? 232 ASP A CA 1 ATOM 1835 C C . ASP A 1 229 ? 14.598 31.030 37.843 1.00 58.28 ? 232 ASP A C 1 ATOM 1836 O O . ASP A 1 229 ? 13.893 30.264 38.487 1.00 59.40 ? 232 ASP A O 1 ATOM 1837 C CB . ASP A 1 229 ? 15.923 32.289 39.597 1.00 62.60 ? 232 ASP A CB 1 ATOM 1838 C CG . ASP A 1 229 ? 17.297 32.472 40.281 1.00 68.39 ? 232 ASP A CG 1 ATOM 1839 O OD1 . ASP A 1 229 ? 17.971 31.445 40.579 1.00 69.59 ? 232 ASP A OD1 1 ATOM 1840 O OD2 . ASP A 1 229 ? 17.705 33.642 40.527 1.00 71.29 ? 232 ASP A OD2 1 ATOM 1841 N N . LEU A 1 230 ? 14.208 31.566 36.693 1.00 56.76 ? 233 LEU A N 1 ATOM 1842 C CA . LEU A 1 230 ? 12.926 31.281 36.044 1.00 55.09 ? 233 LEU A CA 1 ATOM 1843 C C . LEU A 1 230 ? 13.413 30.740 34.706 1.00 57.20 ? 233 LEU A C 1 ATOM 1844 O O . LEU A 1 230 ? 14.207 31.394 34.043 1.00 61.86 ? 233 LEU A O 1 ATOM 1845 C CB . LEU A 1 230 ? 12.183 32.586 35.821 1.00 50.71 ? 233 LEU A CB 1 ATOM 1846 C CG . LEU A 1 230 ? 10.858 32.541 35.092 1.00 51.05 ? 233 LEU A CG 1 ATOM 1847 C CD1 . LEU A 1 230 ? 9.831 31.831 35.947 1.00 51.49 ? 233 LEU A CD1 1 ATOM 1848 C CD2 . LEU A 1 230 ? 10.419 33.954 34.813 1.00 50.51 ? 233 LEU A CD2 1 ATOM 1849 N N . TYR A 1 231 ? 12.976 29.571 34.272 1.00 56.16 ? 234 TYR A N 1 ATOM 1850 C CA . TYR A 1 231 ? 13.507 29.050 32.996 1.00 55.72 ? 234 TYR A CA 1 ATOM 1851 C C . TYR A 1 231 ? 15.050 28.953 33.084 1.00 54.97 ? 234 TYR A C 1 ATOM 1852 O O . TYR A 1 231 ? 15.772 29.577 32.300 1.00 53.24 ? 234 TYR A O 1 ATOM 1853 C CB . TYR A 1 231 ? 13.179 29.967 31.799 1.00 52.62 ? 234 TYR A CB 1 ATOM 1854 C CG . TYR A 1 231 ? 11.810 30.593 31.752 1.00 52.30 ? 234 TYR A CG 1 ATOM 1855 C CD1 . TYR A 1 231 ? 10.670 29.908 32.144 1.00 53.92 ? 234 TYR A CD1 1 ATOM 1856 C CD2 . TYR A 1 231 ? 11.668 31.891 31.306 1.00 54.51 ? 234 TYR A CD2 1 ATOM 1857 C CE1 . TYR A 1 231 ? 9.408 30.516 32.093 1.00 55.04 ? 234 TYR A CE1 1 ATOM 1858 C CE2 . TYR A 1 231 ? 10.431 32.511 31.251 1.00 57.26 ? 234 TYR A CE2 1 ATOM 1859 C CZ . TYR A 1 231 ? 9.295 31.828 31.644 1.00 56.50 ? 234 TYR A CZ 1 ATOM 1860 O OH . TYR A 1 231 ? 8.077 32.501 31.567 1.00 56.82 ? 234 TYR A OH 1 ATOM 1861 N N . PRO A 1 232 ? 15.571 28.177 34.046 1.00 55.74 ? 235 PRO A N 1 ATOM 1862 C CA . PRO A 1 232 ? 17.024 28.020 34.208 1.00 56.09 ? 235 PRO A CA 1 ATOM 1863 C C . PRO A 1 232 ? 17.721 27.167 33.138 1.00 55.62 ? 235 PRO A C 1 ATOM 1864 O O . PRO A 1 232 ? 18.945 27.035 33.137 1.00 55.68 ? 235 PRO A O 1 ATOM 1865 C CB . PRO A 1 232 ? 17.145 27.397 35.599 1.00 56.37 ? 235 PRO A CB 1 ATOM 1866 C CG . PRO A 1 232 ? 15.894 26.582 35.707 1.00 56.89 ? 235 PRO A CG 1 ATOM 1867 C CD . PRO A 1 232 ? 14.852 27.529 35.159 1.00 55.42 ? 235 PRO A CD 1 ATOM 1868 N N . THR A 1 233 ? 16.944 26.600 32.228 1.00 55.70 ? 236 THR A N 1 ATOM 1869 C CA . THR A 1 233 ? 17.498 25.749 31.189 1.00 56.02 ? 236 THR A CA 1 ATOM 1870 C C . THR A 1 233 ? 17.923 26.525 29.945 1.00 55.58 ? 236 THR A C 1 ATOM 1871 O O . THR A 1 233 ? 18.570 25.986 29.048 1.00 55.83 ? 236 THR A O 1 ATOM 1872 C CB . THR A 1 233 ? 16.466 24.702 30.753 1.00 56.55 ? 236 THR A CB 1 ATOM 1873 O OG1 . THR A 1 233 ? 17.103 23.742 29.899 1.00 60.67 ? 236 THR A OG1 1 ATOM 1874 C CG2 . THR A 1 233 ? 15.313 25.373 29.995 1.00 54.08 ? 236 THR A CG2 1 ATOM 1875 N N . GLU A 1 234 ? 17.556 27.795 29.893 1.00 55.16 ? 237 GLU A N 1 ATOM 1876 C CA . GLU A 1 234 ? 17.870 28.622 28.740 1.00 53.65 ? 237 GLU A CA 1 ATOM 1877 C C . GLU A 1 234 ? 19.253 29.263 28.734 1.00 53.52 ? 237 GLU A C 1 ATOM 1878 O O . GLU A 1 234 ? 19.640 29.944 29.687 1.00 54.17 ? 237 GLU A O 1 ATOM 1879 C CB . GLU A 1 234 ? 16.804 29.712 28.611 1.00 53.93 ? 237 GLU A CB 1 ATOM 1880 C CG . GLU A 1 234 ? 15.422 29.171 28.293 1.00 53.85 ? 237 GLU A CG 1 ATOM 1881 C CD . GLU A 1 234 ? 14.360 30.250 28.179 1.00 54.12 ? 237 GLU A CD 1 ATOM 1882 O OE1 . GLU A 1 234 ? 14.697 31.451 28.110 1.00 55.66 ? 237 GLU A OE1 1 ATOM 1883 O OE2 . GLU A 1 234 ? 13.170 29.886 28.148 1.00 54.46 ? 237 GLU A OE2 1 ATOM 1884 N N . TYR A 1 235 ? 20.000 29.025 27.658 1.00 52.98 ? 238 TYR A N 1 ATOM 1885 C CA . TYR A 1 235 ? 21.321 29.625 27.486 1.00 52.80 ? 238 TYR A CA 1 ATOM 1886 C C . TYR A 1 235 ? 21.513 29.931 26.004 1.00 52.20 ? 238 TYR A C 1 ATOM 1887 O O . TYR A 1 235 ? 21.567 29.034 25.165 1.00 50.85 ? 238 TYR A O 1 ATOM 1888 C CB . TYR A 1 235 ? 22.445 28.710 28.003 1.00 54.83 ? 238 TYR A CB 1 ATOM 1889 C CG . TYR A 1 235 ? 23.845 29.284 27.772 1.00 59.16 ? 238 TYR A CG 1 ATOM 1890 C CD1 . TYR A 1 235 ? 24.175 30.581 28.179 1.00 59.65 ? 238 TYR A CD1 1 ATOM 1891 C CD2 . TYR A 1 235 ? 24.811 28.561 27.065 1.00 60.38 ? 238 TYR A CD2 1 ATOM 1892 C CE1 . TYR A 1 235 ? 25.426 31.144 27.872 1.00 61.25 ? 238 TYR A CE1 1 ATOM 1893 C CE2 . TYR A 1 235 ? 26.065 29.119 26.754 1.00 61.27 ? 238 TYR A CE2 1 ATOM 1894 C CZ . TYR A 1 235 ? 26.363 30.408 27.154 1.00 63.00 ? 238 TYR A CZ 1 ATOM 1895 O OH . TYR A 1 235 ? 27.585 30.961 26.810 1.00 65.42 ? 238 TYR A OH 1 ATOM 1896 N N . PHE A 1 236 ? 21.584 31.218 25.690 1.00 53.19 ? 239 PHE A N 1 ATOM 1897 C CA . PHE A 1 236 ? 21.756 31.668 24.319 1.00 53.30 ? 239 PHE A CA 1 ATOM 1898 C C . PHE A 1 236 ? 23.083 32.391 24.133 1.00 52.53 ? 239 PHE A C 1 ATOM 1899 O O . PHE A 1 236 ? 23.256 33.527 24.585 1.00 50.46 ? 239 PHE A O 1 ATOM 1900 C CB . PHE A 1 236 ? 20.621 32.617 23.911 1.00 53.64 ? 239 PHE A CB 1 ATOM 1901 C CG . PHE A 1 236 ? 19.249 32.021 24.045 1.00 53.70 ? 239 PHE A CG 1 ATOM 1902 C CD1 . PHE A 1 236 ? 18.896 30.884 23.325 1.00 53.88 ? 239 PHE A CD1 1 ATOM 1903 C CD2 . PHE A 1 236 ? 18.317 32.587 24.912 1.00 51.70 ? 239 PHE A CD2 1 ATOM 1904 C CE1 . PHE A 1 236 ? 17.637 30.318 23.471 1.00 53.00 ? 239 PHE A CE1 1 ATOM 1905 C CE2 . PHE A 1 236 ? 17.062 32.032 25.065 1.00 49.54 ? 239 PHE A CE2 1 ATOM 1906 C CZ . PHE A 1 236 ? 16.720 30.894 24.345 1.00 51.60 ? 239 PHE A CZ 1 ATOM 1907 N N . PRO A 1 237 ? 24.043 31.732 23.469 1.00 52.71 ? 240 PRO A N 1 ATOM 1908 C CA . PRO A 1 237 ? 25.350 32.339 23.224 1.00 52.85 ? 240 PRO A CA 1 ATOM 1909 C C . PRO A 1 237 ? 25.173 33.707 22.559 1.00 53.76 ? 240 PRO A C 1 ATOM 1910 O O . PRO A 1 237 ? 24.615 33.800 21.462 1.00 55.51 ? 240 PRO A O 1 ATOM 1911 C CB . PRO A 1 237 ? 26.020 31.331 22.294 1.00 51.40 ? 240 PRO A CB 1 ATOM 1912 C CG . PRO A 1 237 ? 25.494 30.038 22.788 1.00 50.65 ? 240 PRO A CG 1 ATOM 1913 C CD . PRO A 1 237 ? 24.018 30.338 22.990 1.00 51.82 ? 240 PRO A CD 1 ATOM 1914 N N . HIS A 1 238 ? 25.615 34.763 23.236 1.00 52.61 ? 241 HIS A N 1 ATOM 1915 C CA . HIS A 1 238 ? 25.536 36.115 22.688 1.00 53.45 ? 241 HIS A CA 1 ATOM 1916 C C . HIS A 1 238 ? 24.118 36.656 22.418 1.00 54.29 ? 241 HIS A C 1 ATOM 1917 O O . HIS A 1 238 ? 23.917 37.575 21.603 1.00 55.44 ? 241 HIS A O 1 ATOM 1918 C CB . HIS A 1 238 ? 26.401 36.183 21.425 1.00 52.42 ? 241 HIS A CB 1 ATOM 1919 C CG . HIS A 1 238 ? 27.794 35.672 21.635 1.00 50.84 ? 241 HIS A CG 1 ATOM 1920 N ND1 . HIS A 1 238 ? 28.324 34.629 20.906 1.00 50.41 ? 241 HIS A ND1 1 ATOM 1921 C CD2 . HIS A 1 238 ? 28.742 36.013 22.543 1.00 51.86 ? 241 HIS A CD2 1 ATOM 1922 C CE1 . HIS A 1 238 ? 29.533 34.347 21.360 1.00 51.31 ? 241 HIS A CE1 1 ATOM 1923 N NE2 . HIS A 1 238 ? 29.811 35.171 22.354 1.00 51.06 ? 241 HIS A NE2 1 ATOM 1924 N N . GLY A 1 239 ? 23.142 36.074 23.113 1.00 52.71 ? 242 GLY A N 1 ATOM 1925 C CA . GLY A 1 239 ? 21.766 36.520 23.013 1.00 50.30 ? 242 GLY A CA 1 ATOM 1926 C C . GLY A 1 239 ? 20.990 36.373 21.723 1.00 50.23 ? 242 GLY A C 1 ATOM 1927 O O . GLY A 1 239 ? 20.091 37.169 21.478 1.00 52.22 ? 242 GLY A O 1 ATOM 1928 N N . ILE A 1 240 ? 21.316 35.388 20.895 1.00 48.67 ? 243 ILE A N 1 ATOM 1929 C CA . ILE A 1 240 ? 20.569 35.190 19.662 1.00 46.33 ? 243 ILE A CA 1 ATOM 1930 C C . ILE A 1 240 ? 20.309 33.701 19.547 1.00 47.13 ? 243 ILE A C 1 ATOM 1931 O O . ILE A 1 240 ? 21.075 32.904 20.089 1.00 48.87 ? 243 ILE A O 1 ATOM 1932 C CB . ILE A 1 240 ? 21.360 35.656 18.399 1.00 44.41 ? 243 ILE A CB 1 ATOM 1933 C CG1 . ILE A 1 240 ? 22.518 34.705 18.111 1.00 43.52 ? 243 ILE A CG1 1 ATOM 1934 C CG2 . ILE A 1 240 ? 21.900 37.065 18.593 1.00 41.99 ? 243 ILE A CG2 1 ATOM 1935 C CD1 . ILE A 1 240 ? 22.970 34.735 16.656 1.00 40.21 ? 243 ILE A CD1 1 ATOM 1936 N N . THR A 1 241 ? 19.239 33.311 18.862 1.00 45.96 ? 244 THR A N 1 ATOM 1937 C CA . THR A 1 241 ? 18.969 31.888 18.703 1.00 46.06 ? 244 THR A CA 1 ATOM 1938 C C . THR A 1 241 ? 18.185 31.620 17.452 1.00 47.12 ? 244 THR A C 1 ATOM 1939 O O . THR A 1 241 ? 17.346 32.442 17.069 1.00 49.50 ? 244 THR A O 1 ATOM 1940 C CB . THR A 1 241 ? 18.140 31.292 19.872 1.00 46.12 ? 244 THR A CB 1 ATOM 1941 O OG1 . THR A 1 241 ? 17.981 29.884 19.663 1.00 46.45 ? 244 THR A OG1 1 ATOM 1942 C CG2 . THR A 1 241 ? 16.748 31.914 19.933 1.00 44.31 ? 244 THR A CG2 1 ATOM 1943 N N . ASN A 1 242 ? 18.475 30.493 16.800 1.00 46.32 ? 245 ASN A N 1 ATOM 1944 C CA . ASN A 1 242 ? 17.709 30.097 15.623 1.00 45.91 ? 245 ASN A CA 1 ATOM 1945 C C . ASN A 1 242 ? 16.377 29.746 16.278 1.00 46.57 ? 245 ASN A C 1 ATOM 1946 O O . ASN A 1 242 ? 16.360 29.113 17.338 1.00 46.90 ? 245 ASN A O 1 ATOM 1947 C CB . ASN A 1 242 ? 18.308 28.847 14.956 1.00 45.96 ? 245 ASN A CB 1 ATOM 1948 C CG . ASN A 1 242 ? 17.310 28.118 14.020 1.00 48.46 ? 245 ASN A CG 1 ATOM 1949 O OD1 . ASN A 1 242 ? 16.931 26.965 14.263 1.00 48.33 ? 245 ASN A OD1 1 ATOM 1950 N ND2 . ASN A 1 242 ? 16.892 28.791 12.947 1.00 49.34 ? 245 ASN A ND2 1 ATOM 1951 N N . GLY A 1 243 ? 15.271 30.166 15.674 1.00 45.21 ? 246 GLY A N 1 ATOM 1952 C CA . GLY A 1 243 ? 13.974 29.889 16.260 1.00 45.09 ? 246 GLY A CA 1 ATOM 1953 C C . GLY A 1 243 ? 13.695 28.424 16.523 1.00 46.95 ? 246 GLY A C 1 ATOM 1954 O O . GLY A 1 243 ? 13.497 28.012 17.663 1.00 47.31 ? 246 GLY A O 1 ATOM 1955 N N . ALA A 1 244 ? 13.682 27.636 15.454 1.00 48.70 ? 247 ALA A N 1 ATOM 1956 C CA . ALA A 1 244 ? 13.406 26.209 15.533 1.00 48.41 ? 247 ALA A CA 1 ATOM 1957 C C . ALA A 1 244 ? 14.246 25.488 16.568 1.00 48.52 ? 247 ALA A C 1 ATOM 1958 O O . ALA A 1 244 ? 13.754 24.622 17.291 1.00 50.89 ? 247 ALA A O 1 ATOM 1959 C CB . ALA A 1 244 ? 13.616 25.567 14.168 1.00 48.24 ? 247 ALA A CB 1 ATOM 1960 N N . GLN A 1 245 ? 15.519 25.828 16.650 1.00 47.44 ? 248 GLN A N 1 ATOM 1961 C CA . GLN A 1 245 ? 16.344 25.137 17.605 1.00 46.52 ? 248 GLN A CA 1 ATOM 1962 C C . GLN A 1 245 ? 15.950 25.418 19.026 1.00 45.94 ? 248 GLN A C 1 ATOM 1963 O O . GLN A 1 245 ? 16.175 24.594 19.902 1.00 47.64 ? 248 GLN A O 1 ATOM 1964 C CB . GLN A 1 245 ? 17.783 25.504 17.445 1.00 46.54 ? 248 GLN A CB 1 ATOM 1965 C CG . GLN A 1 245 ? 18.623 24.627 18.296 1.00 52.39 ? 248 GLN A CG 1 ATOM 1966 C CD . GLN A 1 245 ? 19.987 25.192 18.481 1.00 57.34 ? 248 GLN A CD 1 ATOM 1967 O OE1 . GLN A 1 245 ? 20.930 24.465 18.792 1.00 61.56 ? 248 GLN A OE1 1 ATOM 1968 N NE2 . GLN A 1 245 ? 20.112 26.511 18.303 1.00 59.94 ? 248 GLN A NE2 1 ATOM 1969 N N . TRP A 1 246 ? 15.384 26.592 19.270 1.00 46.11 ? 249 TRP A N 1 ATOM 1970 C CA . TRP A 1 246 ? 14.951 26.943 20.625 1.00 46.36 ? 249 TRP A CA 1 ATOM 1971 C C . TRP A 1 246 ? 13.713 26.088 20.887 1.00 48.32 ? 249 TRP A C 1 ATOM 1972 O O . TRP A 1 246 ? 13.640 25.360 21.886 1.00 50.65 ? 249 TRP A O 1 ATOM 1973 C CB . TRP A 1 246 ? 14.652 28.434 20.699 1.00 43.87 ? 249 TRP A CB 1 ATOM 1974 C CG . TRP A 1 246 ? 14.110 28.866 21.985 1.00 42.87 ? 249 TRP A CG 1 ATOM 1975 C CD1 . TRP A 1 246 ? 14.157 28.190 23.170 1.00 44.22 ? 249 TRP A CD1 1 ATOM 1976 C CD2 . TRP A 1 246 ? 13.402 30.078 22.238 1.00 42.11 ? 249 TRP A CD2 1 ATOM 1977 N NE1 . TRP A 1 246 ? 13.512 28.910 24.154 1.00 42.57 ? 249 TRP A NE1 1 ATOM 1978 C CE2 . TRP A 1 246 ? 13.041 30.076 23.605 1.00 41.13 ? 249 TRP A CE2 1 ATOM 1979 C CE3 . TRP A 1 246 ? 13.036 31.172 21.441 1.00 42.38 ? 249 TRP A CE3 1 ATOM 1980 C CZ2 . TRP A 1 246 ? 12.330 31.128 24.195 1.00 41.02 ? 249 TRP A CZ2 1 ATOM 1981 C CZ3 . TRP A 1 246 ? 12.327 32.223 22.030 1.00 43.13 ? 249 TRP A CZ3 1 ATOM 1982 C CH2 . TRP A 1 246 ? 11.984 32.191 23.395 1.00 40.87 ? 249 TRP A CH2 1 ATOM 1983 N N . TYR A 1 247 ? 12.751 26.180 19.972 1.00 48.20 ? 250 TYR A N 1 ATOM 1984 C CA . TYR A 1 247 ? 11.555 25.352 19.996 1.00 49.92 ? 250 TYR A CA 1 ATOM 1985 C C . TYR A 1 247 ? 10.749 25.592 18.733 1.00 50.70 ? 250 TYR A C 1 ATOM 1986 O O . TYR A 1 247 ? 10.667 26.710 18.243 1.00 52.95 ? 250 TYR A O 1 ATOM 1987 C CB . TYR A 1 247 ? 10.727 25.544 21.271 1.00 51.21 ? 250 TYR A CB 1 ATOM 1988 C CG . TYR A 1 247 ? 10.012 26.847 21.448 1.00 51.72 ? 250 TYR A CG 1 ATOM 1989 C CD1 . TYR A 1 247 ? 8.836 27.113 20.769 1.00 52.16 ? 250 TYR A CD1 1 ATOM 1990 C CD2 . TYR A 1 247 ? 10.494 27.803 22.343 1.00 53.54 ? 250 TYR A CD2 1 ATOM 1991 C CE1 . TYR A 1 247 ? 8.148 28.308 20.976 1.00 54.71 ? 250 TYR A CE1 1 ATOM 1992 C CE2 . TYR A 1 247 ? 9.816 29.001 22.563 1.00 54.47 ? 250 TYR A CE2 1 ATOM 1993 C CZ . TYR A 1 247 ? 8.639 29.254 21.878 1.00 55.16 ? 250 TYR A CZ 1 ATOM 1994 O OH . TYR A 1 247 ? 7.940 30.437 22.105 1.00 55.04 ? 250 TYR A OH 1 ATOM 1995 N N . ASN A 1 248 ? 10.194 24.513 18.191 1.00 49.30 ? 251 ASN A N 1 ATOM 1996 C CA . ASN A 1 248 ? 9.447 24.551 16.946 1.00 47.86 ? 251 ASN A CA 1 ATOM 1997 C C . ASN A 1 248 ? 8.209 25.453 16.975 1.00 49.39 ? 251 ASN A C 1 ATOM 1998 O O . ASN A 1 248 ? 7.323 25.280 17.813 1.00 50.59 ? 251 ASN A O 1 ATOM 1999 C CB . ASN A 1 248 ? 9.063 23.122 16.572 1.00 45.37 ? 251 ASN A CB 1 ATOM 2000 C CG . ASN A 1 248 ? 8.583 23.003 15.158 1.00 45.25 ? 251 ASN A CG 1 ATOM 2001 O OD1 . ASN A 1 248 ? 9.377 22.959 14.215 1.00 45.07 ? 251 ASN A OD1 1 ATOM 2002 N ND2 . ASN A 1 248 ? 7.267 22.960 14.992 1.00 44.89 ? 251 ASN A ND2 1 ATOM 2003 N N . VAL A 1 249 ? 8.162 26.428 16.067 1.00 49.57 ? 252 VAL A N 1 ATOM 2004 C CA . VAL A 1 249 ? 7.016 27.338 15.971 1.00 48.39 ? 252 VAL A CA 1 ATOM 2005 C C . VAL A 1 249 ? 6.438 27.329 14.574 1.00 49.51 ? 252 VAL A C 1 ATOM 2006 O O . VAL A 1 249 ? 6.983 27.916 13.632 1.00 50.49 ? 252 VAL A O 1 ATOM 2007 C CB . VAL A 1 249 ? 7.364 28.802 16.286 1.00 47.03 ? 252 VAL A CB 1 ATOM 2008 C CG1 . VAL A 1 249 ? 6.132 29.688 16.068 1.00 42.38 ? 252 VAL A CG1 1 ATOM 2009 C CG2 . VAL A 1 249 ? 7.834 28.924 17.710 1.00 47.42 ? 252 VAL A CG2 1 ATOM 2010 N N . PRO A 1 250 ? 5.317 26.652 14.413 1.00 49.27 ? 253 PRO A N 1 ATOM 2011 C CA . PRO A 1 250 ? 4.763 26.647 13.067 1.00 49.95 ? 253 PRO A CA 1 ATOM 2012 C C . PRO A 1 250 ? 3.698 27.729 12.955 1.00 51.03 ? 253 PRO A C 1 ATOM 2013 O O . PRO A 1 250 ? 2.953 27.968 13.903 1.00 51.77 ? 253 PRO A O 1 ATOM 2014 C CB . PRO A 1 250 ? 4.204 25.239 12.950 1.00 49.03 ? 253 PRO A CB 1 ATOM 2015 C CG . PRO A 1 250 ? 3.678 24.997 14.344 1.00 48.59 ? 253 PRO A CG 1 ATOM 2016 C CD . PRO A 1 250 ? 4.739 25.590 15.250 1.00 48.62 ? 253 PRO A CD 1 ATOM 2017 N N . GLY A 1 251 ? 3.647 28.401 11.809 1.00 51.83 ? 254 GLY A N 1 ATOM 2018 C CA . GLY A 1 251 ? 2.643 29.429 11.604 1.00 51.22 ? 254 GLY A CA 1 ATOM 2019 C C . GLY A 1 251 ? 3.038 30.832 12.010 1.00 50.75 ? 254 GLY A C 1 ATOM 2020 O O . GLY A 1 251 ? 2.219 31.745 11.955 1.00 52.22 ? 254 GLY A O 1 ATOM 2021 N N . GLY A 1 252 ? 4.289 31.019 12.403 1.00 48.89 ? 255 GLY A N 1 ATOM 2022 C CA . GLY A 1 252 ? 4.710 32.340 12.813 1.00 49.10 ? 255 GLY A CA 1 ATOM 2023 C C . GLY A 1 252 ? 4.745 33.394 11.719 1.00 50.94 ? 255 GLY A C 1 ATOM 2024 O O . GLY A 1 252 ? 4.778 33.082 10.523 1.00 51.75 ? 255 GLY A O 1 ATOM 2025 N N . MET A 1 253 ? 4.740 34.653 12.148 1.00 51.36 ? 256 MET A N 1 ATOM 2026 C CA . MET A 1 253 ? 4.789 35.785 11.246 1.00 50.94 ? 256 MET A CA 1 ATOM 2027 C C . MET A 1 253 ? 6.203 35.989 10.734 1.00 50.98 ? 256 MET A C 1 ATOM 2028 O O . MET A 1 253 ? 6.397 36.393 9.594 1.00 49.82 ? 256 MET A O 1 ATOM 2029 C CB . MET A 1 253 ? 4.330 37.042 11.976 1.00 53.17 ? 256 MET A CB 1 ATOM 2030 C CG . MET A 1 253 ? 4.622 38.352 11.247 1.00 52.88 ? 256 MET A CG 1 ATOM 2031 S SD . MET A 1 253 ? 3.825 39.763 12.067 1.00 54.49 ? 256 MET A SD 1 ATOM 2032 C CE . MET A 1 253 ? 5.019 40.137 13.298 1.00 50.89 ? 256 MET A CE 1 ATOM 2033 N N . GLN A 1 254 ? 7.188 35.711 11.586 1.00 51.37 ? 257 GLN A N 1 ATOM 2034 C CA . GLN A 1 254 ? 8.600 35.876 11.233 1.00 49.47 ? 257 GLN A CA 1 ATOM 2035 C C . GLN A 1 254 ? 9.042 35.191 9.945 1.00 48.97 ? 257 GLN A C 1 ATOM 2036 O O . GLN A 1 254 ? 9.662 35.807 9.070 1.00 48.82 ? 257 GLN A O 1 ATOM 2037 C CB . GLN A 1 254 ? 9.493 35.373 12.359 1.00 47.83 ? 257 GLN A CB 1 ATOM 2038 C CG . GLN A 1 254 ? 10.925 35.176 11.902 1.00 48.26 ? 257 GLN A CG 1 ATOM 2039 C CD . GLN A 1 254 ? 11.817 34.567 12.961 1.00 47.79 ? 257 GLN A CD 1 ATOM 2040 O OE1 . GLN A 1 254 ? 12.091 35.176 14.000 1.00 44.08 ? 257 GLN A OE1 1 ATOM 2041 N NE2 . GLN A 1 254 ? 12.284 33.355 12.698 1.00 47.82 ? 257 GLN A NE2 1 ATOM 2042 N N . ASP A 1 255 ? 8.767 33.902 9.843 1.00 48.52 ? 258 ASP A N 1 ATOM 2043 C CA . ASP A 1 255 ? 9.160 33.180 8.646 1.00 48.44 ? 258 ASP A CA 1 ATOM 2044 C C . ASP A 1 255 ? 8.263 33.551 7.458 1.00 48.28 ? 258 ASP A C 1 ATOM 2045 O O . ASP A 1 255 ? 8.681 33.529 6.298 1.00 47.90 ? 258 ASP A O 1 ATOM 2046 C CB . ASP A 1 255 ? 9.117 31.670 8.911 1.00 47.50 ? 258 ASP A CB 1 ATOM 2047 C CG . ASP A 1 255 ? 10.363 31.161 9.641 1.00 47.81 ? 258 ASP A CG 1 ATOM 2048 O OD1 . ASP A 1 255 ? 11.170 31.995 10.121 1.00 46.23 ? 258 ASP A OD1 1 ATOM 2049 O OD2 . ASP A 1 255 ? 10.525 29.918 9.731 1.00 47.30 ? 258 ASP A OD2 1 ATOM 2050 N N . TRP A 1 256 ? 7.024 33.911 7.740 1.00 48.89 ? 259 TRP A N 1 ATOM 2051 C CA . TRP A 1 256 ? 6.146 34.254 6.648 1.00 49.12 ? 259 TRP A CA 1 ATOM 2052 C C . TRP A 1 256 ? 6.775 35.397 5.868 1.00 49.91 ? 259 TRP A C 1 ATOM 2053 O O . TRP A 1 256 ? 6.922 35.310 4.661 1.00 50.70 ? 259 TRP A O 1 ATOM 2054 C CB . TRP A 1 256 ? 4.782 34.657 7.169 1.00 49.89 ? 259 TRP A CB 1 ATOM 2055 C CG . TRP A 1 256 ? 3.784 34.715 6.081 1.00 52.14 ? 259 TRP A CG 1 ATOM 2056 C CD1 . TRP A 1 256 ? 3.079 33.667 5.557 1.00 52.46 ? 259 TRP A CD1 1 ATOM 2057 C CD2 . TRP A 1 256 ? 3.404 35.874 5.327 1.00 53.51 ? 259 TRP A CD2 1 ATOM 2058 N NE1 . TRP A 1 256 ? 2.280 34.101 4.520 1.00 52.28 ? 259 TRP A NE1 1 ATOM 2059 C CE2 . TRP A 1 256 ? 2.461 35.452 4.358 1.00 53.81 ? 259 TRP A CE2 1 ATOM 2060 C CE3 . TRP A 1 256 ? 3.770 37.231 5.374 1.00 53.65 ? 259 TRP A CE3 1 ATOM 2061 C CZ2 . TRP A 1 256 ? 1.874 36.342 3.441 1.00 53.18 ? 259 TRP A CZ2 1 ATOM 2062 C CZ3 . TRP A 1 256 ? 3.185 38.120 4.461 1.00 54.00 ? 259 TRP A CZ3 1 ATOM 2063 C CH2 . TRP A 1 256 ? 2.247 37.667 3.508 1.00 53.92 ? 259 TRP A CH2 1 ATOM 2064 N N . ASN A 1 257 ? 7.149 36.464 6.562 1.00 51.27 ? 260 ASN A N 1 ATOM 2065 C CA . ASN A 1 257 ? 7.790 37.611 5.930 1.00 51.80 ? 260 ASN A CA 1 ATOM 2066 C C . ASN A 1 257 ? 8.774 37.122 4.878 1.00 53.74 ? 260 ASN A C 1 ATOM 2067 O O . ASN A 1 257 ? 8.560 37.285 3.682 1.00 56.65 ? 260 ASN A O 1 ATOM 2068 C CB . ASN A 1 257 ? 8.580 38.404 6.966 1.00 52.35 ? 260 ASN A CB 1 ATOM 2069 C CG . ASN A 1 257 ? 7.748 39.427 7.687 1.00 52.11 ? 260 ASN A CG 1 ATOM 2070 O OD1 . ASN A 1 257 ? 7.731 40.592 7.305 1.00 53.11 ? 260 ASN A OD1 1 ATOM 2071 N ND2 . ASN A 1 257 ? 7.054 39.004 8.746 1.00 52.17 ? 260 ASN A ND2 1 ATOM 2072 N N . TYR A 1 258 ? 9.856 36.520 5.357 1.00 54.18 ? 261 TYR A N 1 ATOM 2073 C CA . TYR A 1 258 ? 10.941 35.996 4.535 1.00 53.83 ? 261 TYR A CA 1 ATOM 2074 C C . TYR A 1 258 ? 10.480 35.259 3.300 1.00 54.14 ? 261 TYR A C 1 ATOM 2075 O O . TYR A 1 258 ? 10.849 35.611 2.174 1.00 56.01 ? 261 TYR A O 1 ATOM 2076 C CB . TYR A 1 258 ? 11.785 35.046 5.370 1.00 54.88 ? 261 TYR A CB 1 ATOM 2077 C CG . TYR A 1 258 ? 13.058 34.584 4.703 1.00 57.55 ? 261 TYR A CG 1 ATOM 2078 C CD1 . TYR A 1 258 ? 14.137 35.453 4.544 1.00 58.34 ? 261 TYR A CD1 1 ATOM 2079 C CD2 . TYR A 1 258 ? 13.215 33.261 4.279 1.00 58.20 ? 261 TYR A CD2 1 ATOM 2080 C CE1 . TYR A 1 258 ? 15.358 35.015 3.984 1.00 57.68 ? 261 TYR A CE1 1 ATOM 2081 C CE2 . TYR A 1 258 ? 14.434 32.816 3.713 1.00 58.20 ? 261 TYR A CE2 1 ATOM 2082 C CZ . TYR A 1 258 ? 15.500 33.700 3.573 1.00 56.99 ? 261 TYR A CZ 1 ATOM 2083 O OH . TYR A 1 258 ? 16.711 33.282 3.046 1.00 56.78 ? 261 TYR A OH 1 ATOM 2084 N N . LEU A 1 259 ? 9.672 34.231 3.533 1.00 53.57 ? 262 LEU A N 1 ATOM 2085 C CA . LEU A 1 259 ? 9.160 33.377 2.472 1.00 54.34 ? 262 LEU A CA 1 ATOM 2086 C C . LEU A 1 259 ? 8.136 33.967 1.516 1.00 55.23 ? 262 LEU A C 1 ATOM 2087 O O . LEU A 1 259 ? 7.868 33.369 0.484 1.00 57.10 ? 262 LEU A O 1 ATOM 2088 C CB . LEU A 1 259 ? 8.558 32.107 3.067 1.00 53.77 ? 262 LEU A CB 1 ATOM 2089 C CG . LEU A 1 259 ? 9.418 31.220 3.967 1.00 53.00 ? 262 LEU A CG 1 ATOM 2090 C CD1 . LEU A 1 259 ? 8.564 30.060 4.458 1.00 53.49 ? 262 LEU A CD1 1 ATOM 2091 C CD2 . LEU A 1 259 ? 10.629 30.716 3.219 1.00 50.26 ? 262 LEU A CD2 1 ATOM 2092 N N . ASN A 1 260 ? 7.537 35.108 1.830 1.00 56.19 ? 263 ASN A N 1 ATOM 2093 C CA . ASN A 1 260 ? 6.541 35.657 0.910 1.00 57.07 ? 263 ASN A CA 1 ATOM 2094 C C . ASN A 1 260 ? 6.766 37.101 0.473 1.00 57.97 ? 263 ASN A C 1 ATOM 2095 O O . ASN A 1 260 ? 6.004 37.630 -0.339 1.00 60.41 ? 263 ASN A O 1 ATOM 2096 C CB . ASN A 1 260 ? 5.147 35.526 1.506 1.00 57.67 ? 263 ASN A CB 1 ATOM 2097 C CG . ASN A 1 260 ? 4.832 34.121 1.918 1.00 60.80 ? 263 ASN A CG 1 ATOM 2098 O OD1 . ASN A 1 260 ? 5.602 33.502 2.638 1.00 63.05 ? 263 ASN A OD1 1 ATOM 2099 N ND2 . ASN A 1 260 ? 3.693 33.606 1.472 1.00 63.10 ? 263 ASN A ND2 1 ATOM 2100 N N . THR A 1 261 ? 7.798 37.742 1.009 1.00 56.05 ? 264 THR A N 1 ATOM 2101 C CA . THR A 1 261 ? 8.105 39.106 0.631 1.00 55.03 ? 264 THR A CA 1 ATOM 2102 C C . THR A 1 261 ? 9.616 39.180 0.611 1.00 55.44 ? 264 THR A C 1 ATOM 2103 O O . THR A 1 261 ? 10.286 38.157 0.788 1.00 56.46 ? 264 THR A O 1 ATOM 2104 C CB . THR A 1 261 ? 7.531 40.122 1.652 1.00 56.32 ? 264 THR A CB 1 ATOM 2105 O OG1 . THR A 1 261 ? 8.230 40.018 2.897 1.00 59.21 ? 264 THR A OG1 1 ATOM 2106 C CG2 . THR A 1 261 ? 6.069 39.849 1.896 1.00 53.99 ? 264 THR A CG2 1 ATOM 2107 N N . ASN A 1 262 ? 10.158 40.372 0.388 1.00 56.11 ? 265 ASN A N 1 ATOM 2108 C CA . ASN A 1 262 ? 11.609 40.539 0.361 1.00 57.08 ? 265 ASN A CA 1 ATOM 2109 C C . ASN A 1 262 ? 12.079 40.831 1.763 1.00 57.01 ? 265 ASN A C 1 ATOM 2110 O O . ASN A 1 262 ? 13.274 40.755 2.075 1.00 56.61 ? 265 ASN A O 1 ATOM 2111 C CB . ASN A 1 262 ? 12.002 41.706 -0.540 1.00 57.99 ? 265 ASN A CB 1 ATOM 2112 C CG . ASN A 1 262 ? 11.592 41.486 -1.960 1.00 59.63 ? 265 ASN A CG 1 ATOM 2113 O OD1 . ASN A 1 262 ? 12.037 40.536 -2.595 1.00 63.76 ? 265 ASN A OD1 1 ATOM 2114 N ND2 . ASN A 1 262 ? 10.726 42.350 -2.471 1.00 61.81 ? 265 ASN A ND2 1 ATOM 2115 N N . CYS A 1 263 ? 11.118 41.175 2.611 1.00 56.15 ? 266 CYS A N 1 ATOM 2116 C CA . CYS A 1 263 ? 11.442 41.514 3.976 1.00 54.92 ? 266 CYS A CA 1 ATOM 2117 C C . CYS A 1 263 ? 12.091 40.373 4.739 1.00 54.50 ? 266 CYS A C 1 ATOM 2118 O O . CYS A 1 263 ? 11.752 39.202 4.563 1.00 56.58 ? 266 CYS A O 1 ATOM 2119 C CB . CYS A 1 263 ? 10.205 41.995 4.728 1.00 53.13 ? 266 CYS A CB 1 ATOM 2120 S SG . CYS A 1 263 ? 10.698 42.815 6.250 1.00 53.85 ? 266 CYS A SG 1 ATOM 2121 N N . PHE A 1 264 ? 13.054 40.742 5.570 1.00 53.86 ? 267 PHE A N 1 ATOM 2122 C CA . PHE A 1 264 ? 13.783 39.807 6.415 1.00 52.43 ? 267 PHE A CA 1 ATOM 2123 C C . PHE A 1 264 ? 13.382 40.214 7.836 1.00 52.04 ? 267 PHE A C 1 ATOM 2124 O O . PHE A 1 264 ? 13.665 41.347 8.254 1.00 53.03 ? 267 PHE A O 1 ATOM 2125 C CB . PHE A 1 264 ? 15.309 39.982 6.269 1.00 52.08 ? 267 PHE A CB 1 ATOM 2126 C CG . PHE A 1 264 ? 15.927 39.282 5.071 1.00 50.60 ? 267 PHE A CG 1 ATOM 2127 C CD1 . PHE A 1 264 ? 15.198 39.057 3.902 1.00 50.78 ? 267 PHE A CD1 1 ATOM 2128 C CD2 . PHE A 1 264 ? 17.268 38.869 5.125 1.00 48.85 ? 267 PHE A CD2 1 ATOM 2129 C CE1 . PHE A 1 264 ? 15.793 38.436 2.810 1.00 50.37 ? 267 PHE A CE1 1 ATOM 2130 C CE2 . PHE A 1 264 ? 17.869 38.250 4.053 1.00 49.04 ? 267 PHE A CE2 1 ATOM 2131 C CZ . PHE A 1 264 ? 17.133 38.030 2.886 1.00 50.19 ? 267 PHE A CZ 1 ATOM 2132 N N . GLU A 1 265 ? 12.734 39.304 8.571 1.00 51.84 ? 268 GLU A N 1 ATOM 2133 C CA . GLU A 1 265 ? 12.296 39.600 9.932 1.00 51.15 ? 268 GLU A CA 1 ATOM 2134 C C . GLU A 1 265 ? 12.845 38.670 10.998 1.00 50.91 ? 268 GLU A C 1 ATOM 2135 O O . GLU A 1 265 ? 12.991 37.458 10.798 1.00 51.67 ? 268 GLU A O 1 ATOM 2136 C CB . GLU A 1 265 ? 10.768 39.613 10.020 1.00 50.57 ? 268 GLU A CB 1 ATOM 2137 C CG . GLU A 1 265 ? 10.242 39.972 11.388 1.00 50.35 ? 268 GLU A CG 1 ATOM 2138 C CD . GLU A 1 265 ? 8.764 40.128 11.367 1.00 52.05 ? 268 GLU A CD 1 ATOM 2139 O OE1 . GLU A 1 265 ? 8.292 41.122 10.778 1.00 54.24 ? 268 GLU A OE1 1 ATOM 2140 O OE2 . GLU A 1 265 ? 8.072 39.252 11.917 1.00 52.15 ? 268 GLU A OE2 1 ATOM 2141 N N . VAL A 1 266 ? 13.119 39.283 12.142 1.00 49.66 ? 269 VAL A N 1 ATOM 2142 C CA . VAL A 1 266 ? 13.652 38.628 13.309 1.00 47.51 ? 269 VAL A CA 1 ATOM 2143 C C . VAL A 1 266 ? 12.693 38.841 14.472 1.00 46.59 ? 269 VAL A C 1 ATOM 2144 O O . VAL A 1 266 ? 12.024 39.870 14.546 1.00 47.84 ? 269 VAL A O 1 ATOM 2145 C CB . VAL A 1 266 ? 15.006 39.227 13.650 1.00 47.47 ? 269 VAL A CB 1 ATOM 2146 C CG1 . VAL A 1 266 ? 15.208 39.244 15.143 1.00 49.71 ? 269 VAL A CG1 1 ATOM 2147 C CG2 . VAL A 1 266 ? 16.092 38.430 12.968 1.00 47.21 ? 269 VAL A CG2 1 ATOM 2148 N N . THR A 1 267 ? 12.635 37.870 15.376 1.00 44.09 ? 270 THR A N 1 ATOM 2149 C CA . THR A 1 267 ? 11.762 37.942 16.537 1.00 42.13 ? 270 THR A CA 1 ATOM 2150 C C . THR A 1 267 ? 12.582 38.299 17.774 1.00 42.34 ? 270 THR A C 1 ATOM 2151 O O . THR A 1 267 ? 13.519 37.588 18.135 1.00 42.69 ? 270 THR A O 1 ATOM 2152 C CB . THR A 1 267 ? 11.068 36.605 16.755 1.00 40.70 ? 270 THR A CB 1 ATOM 2153 O OG1 . THR A 1 267 ? 10.344 36.241 15.570 1.00 44.62 ? 270 THR A OG1 1 ATOM 2154 C CG2 . THR A 1 267 ? 10.110 36.707 17.878 1.00 39.53 ? 270 THR A CG2 1 ATOM 2155 N N . ILE A 1 268 ? 12.226 39.389 18.440 1.00 41.38 ? 271 ILE A N 1 ATOM 2156 C CA . ILE A 1 268 ? 12.992 39.820 19.595 1.00 40.02 ? 271 ILE A CA 1 ATOM 2157 C C . ILE A 1 268 ? 12.301 39.673 20.935 1.00 43.21 ? 271 ILE A C 1 ATOM 2158 O O . ILE A 1 268 ? 11.275 40.310 21.175 1.00 45.65 ? 271 ILE A O 1 ATOM 2159 C CB . ILE A 1 268 ? 13.382 41.275 19.451 1.00 36.93 ? 271 ILE A CB 1 ATOM 2160 C CG1 . ILE A 1 268 ? 14.165 41.468 18.159 1.00 38.69 ? 271 ILE A CG1 1 ATOM 2161 C CG2 . ILE A 1 268 ? 14.220 41.698 20.627 1.00 34.74 ? 271 ILE A CG2 1 ATOM 2162 C CD1 . ILE A 1 268 ? 14.675 42.885 17.969 1.00 38.75 ? 271 ILE A CD1 1 ATOM 2163 N N . GLU A 1 269 ? 12.879 38.856 21.814 1.00 43.62 ? 272 GLU A N 1 ATOM 2164 C CA . GLU A 1 269 ? 12.328 38.642 23.148 1.00 43.63 ? 272 GLU A CA 1 ATOM 2165 C C . GLU A 1 269 ? 13.025 39.599 24.097 1.00 44.07 ? 272 GLU A C 1 ATOM 2166 O O . GLU A 1 269 ? 14.192 39.420 24.433 1.00 46.17 ? 272 GLU A O 1 ATOM 2167 C CB . GLU A 1 269 ? 12.547 37.195 23.584 1.00 43.95 ? 272 GLU A CB 1 ATOM 2168 C CG . GLU A 1 269 ? 11.701 36.189 22.814 1.00 45.18 ? 272 GLU A CG 1 ATOM 2169 C CD . GLU A 1 269 ? 10.265 36.179 23.283 1.00 47.78 ? 272 GLU A CD 1 ATOM 2170 O OE1 . GLU A 1 269 ? 9.961 36.950 24.224 1.00 47.34 ? 272 GLU A OE1 1 ATOM 2171 O OE2 . GLU A 1 269 ? 9.440 35.410 22.727 1.00 48.92 ? 272 GLU A OE2 1 ATOM 2172 N N . LEU A 1 270 ? 12.285 40.610 24.537 1.00 44.56 ? 273 LEU A N 1 ATOM 2173 C CA . LEU A 1 270 ? 12.803 41.657 25.403 1.00 44.28 ? 273 LEU A CA 1 ATOM 2174 C C . LEU A 1 270 ? 12.941 41.395 26.898 1.00 46.89 ? 273 LEU A C 1 ATOM 2175 O O . LEU A 1 270 ? 13.355 42.289 27.628 1.00 48.53 ? 273 LEU A O 1 ATOM 2176 C CB . LEU A 1 270 ? 11.963 42.913 25.191 1.00 41.69 ? 273 LEU A CB 1 ATOM 2177 C CG . LEU A 1 270 ? 11.957 43.359 23.725 1.00 41.92 ? 273 LEU A CG 1 ATOM 2178 C CD1 . LEU A 1 270 ? 10.882 44.390 23.482 1.00 39.57 ? 273 LEU A CD1 1 ATOM 2179 C CD2 . LEU A 1 270 ? 13.318 43.916 23.376 1.00 42.80 ? 273 LEU A CD2 1 ATOM 2180 N N . GLY A 1 271 ? 12.610 40.197 27.368 1.00 48.19 ? 274 GLY A N 1 ATOM 2181 C CA . GLY A 1 271 ? 12.737 39.918 28.793 1.00 50.17 ? 274 GLY A CA 1 ATOM 2182 C C . GLY A 1 271 ? 11.776 38.847 29.276 1.00 52.55 ? 274 GLY A C 1 ATOM 2183 O O . GLY A 1 271 ? 10.665 38.744 28.750 1.00 53.84 ? 274 GLY A O 1 ATOM 2184 N N . CYS A 1 272 ? 12.178 38.063 30.279 1.00 52.40 ? 275 CYS A N 1 ATOM 2185 C CA . CYS A 1 272 ? 11.330 36.984 30.788 1.00 52.30 ? 275 CYS A CA 1 ATOM 2186 C C . CYS A 1 272 ? 10.000 37.423 31.366 1.00 52.50 ? 275 CYS A C 1 ATOM 2187 O O . CYS A 1 272 ? 9.028 36.658 31.318 1.00 55.07 ? 275 CYS A O 1 ATOM 2188 C CB . CYS A 1 272 ? 12.056 36.172 31.849 1.00 53.24 ? 275 CYS A CB 1 ATOM 2189 S SG . CYS A 1 272 ? 13.528 35.333 31.218 1.00 60.51 ? 275 CYS A SG 1 ATOM 2190 N N . VAL A 1 273 ? 9.947 38.627 31.930 1.00 51.15 ? 276 VAL A N 1 ATOM 2191 C CA . VAL A 1 273 ? 8.699 39.116 32.513 1.00 49.87 ? 276 VAL A CA 1 ATOM 2192 C C . VAL A 1 273 ? 7.822 39.795 31.475 1.00 49.63 ? 276 VAL A C 1 ATOM 2193 O O . VAL A 1 273 ? 8.027 40.967 31.129 1.00 48.17 ? 276 VAL A O 1 ATOM 2194 C CB . VAL A 1 273 ? 8.960 40.091 33.655 1.00 49.00 ? 276 VAL A CB 1 ATOM 2195 C CG1 . VAL A 1 273 ? 7.640 40.628 34.197 1.00 46.70 ? 276 VAL A CG1 1 ATOM 2196 C CG2 . VAL A 1 273 ? 9.707 39.382 34.741 1.00 47.42 ? 276 VAL A CG2 1 ATOM 2197 N N . LYS A 1 274 ? 6.832 39.045 30.999 1.00 48.77 ? 277 LYS A N 1 ATOM 2198 C CA . LYS A 1 274 ? 5.910 39.517 29.975 1.00 48.57 ? 277 LYS A CA 1 ATOM 2199 C C . LYS A 1 274 ? 5.262 40.884 30.213 1.00 49.50 ? 277 LYS A C 1 ATOM 2200 O O . LYS A 1 274 ? 5.345 41.774 29.350 1.00 51.34 ? 277 LYS A O 1 ATOM 2201 C CB . LYS A 1 274 ? 4.829 38.458 29.752 1.00 45.30 ? 277 LYS A CB 1 ATOM 2202 C CG . LYS A 1 274 ? 5.359 37.161 29.141 1.00 45.08 ? 277 LYS A CG 1 ATOM 2203 C CD . LYS A 1 274 ? 4.256 36.110 28.952 1.00 45.44 ? 277 LYS A CD 1 ATOM 2204 C CE . LYS A 1 274 ? 4.743 34.921 28.102 1.00 49.07 ? 277 LYS A CE 1 ATOM 2205 N NZ . LYS A 1 274 ? 3.744 33.799 27.920 1.00 49.68 ? 277 LYS A NZ 1 ATOM 2206 N N . TYR A 1 275 ? 4.639 41.050 31.382 1.00 50.37 ? 278 TYR A N 1 ATOM 2207 C CA . TYR A 1 275 ? 3.930 42.286 31.744 1.00 51.62 ? 278 TYR A CA 1 ATOM 2208 C C . TYR A 1 275 ? 4.474 42.870 33.056 1.00 52.30 ? 278 TYR A C 1 ATOM 2209 O O . TYR A 1 275 ? 3.820 42.856 34.088 1.00 51.62 ? 278 TYR A O 1 ATOM 2210 C CB . TYR A 1 275 ? 2.429 41.961 31.869 1.00 50.35 ? 278 TYR A CB 1 ATOM 2211 C CG . TYR A 1 275 ? 1.464 43.119 31.747 1.00 48.39 ? 278 TYR A CG 1 ATOM 2212 C CD1 . TYR A 1 275 ? 1.809 44.409 32.157 1.00 49.99 ? 278 TYR A CD1 1 ATOM 2213 C CD2 . TYR A 1 275 ? 0.191 42.913 31.222 1.00 48.24 ? 278 TYR A CD2 1 ATOM 2214 C CE1 . TYR A 1 275 ? 0.899 45.480 32.042 1.00 51.12 ? 278 TYR A CE1 1 ATOM 2215 C CE2 . TYR A 1 275 ? -0.730 43.968 31.096 1.00 50.33 ? 278 TYR A CE2 1 ATOM 2216 C CZ . TYR A 1 275 ? -0.374 45.254 31.504 1.00 51.97 ? 278 TYR A CZ 1 ATOM 2217 O OH . TYR A 1 275 ? -1.284 46.301 31.353 1.00 51.04 ? 278 TYR A OH 1 ATOM 2218 N N . PRO A 1 276 ? 5.685 43.407 33.025 1.00 54.58 ? 279 PRO A N 1 ATOM 2219 C CA . PRO A 1 276 ? 6.246 43.972 34.252 1.00 56.96 ? 279 PRO A CA 1 ATOM 2220 C C . PRO A 1 276 ? 5.475 45.189 34.739 1.00 58.91 ? 279 PRO A C 1 ATOM 2221 O O . PRO A 1 276 ? 4.719 45.787 33.972 1.00 57.48 ? 279 PRO A O 1 ATOM 2222 C CB . PRO A 1 276 ? 7.672 44.321 33.840 1.00 57.52 ? 279 PRO A CB 1 ATOM 2223 C CG . PRO A 1 276 ? 7.508 44.703 32.405 1.00 56.47 ? 279 PRO A CG 1 ATOM 2224 C CD . PRO A 1 276 ? 6.562 43.651 31.868 1.00 55.36 ? 279 PRO A CD 1 ATOM 2225 N N . LYS A 1 277 ? 5.665 45.546 36.013 1.00 61.13 ? 280 LYS A N 1 ATOM 2226 C CA . LYS A 1 277 ? 5.010 46.723 36.590 1.00 63.42 ? 280 LYS A CA 1 ATOM 2227 C C . LYS A 1 277 ? 5.529 47.994 35.910 1.00 62.37 ? 280 LYS A C 1 ATOM 2228 O O . LYS A 1 277 ? 6.708 48.101 35.586 1.00 62.16 ? 280 LYS A O 1 ATOM 2229 C CB . LYS A 1 277 ? 5.268 46.802 38.096 1.00 65.48 ? 280 LYS A CB 1 ATOM 2230 C CG . LYS A 1 277 ? 4.265 46.022 38.935 1.00 73.43 ? 280 LYS A CG 1 ATOM 2231 C CD . LYS A 1 277 ? 4.520 46.222 40.439 1.00 77.13 ? 280 LYS A CD 1 ATOM 2232 C CE . LYS A 1 277 ? 3.377 45.677 41.315 1.00 78.37 ? 280 LYS A CE 1 ATOM 2233 N NZ . LYS A 1 277 ? 3.561 46.025 42.765 1.00 77.38 ? 280 LYS A NZ 1 ATOM 2234 N N . ALA A 1 278 ? 4.648 48.963 35.706 1.00 62.56 ? 281 ALA A N 1 ATOM 2235 C CA . ALA A 1 278 ? 5.015 50.210 35.035 1.00 63.14 ? 281 ALA A CA 1 ATOM 2236 C C . ALA A 1 278 ? 6.313 50.880 35.495 1.00 64.18 ? 281 ALA A C 1 ATOM 2237 O O . ALA A 1 278 ? 6.948 51.619 34.737 1.00 63.74 ? 281 ALA A O 1 ATOM 2238 C CB . ALA A 1 278 ? 3.866 51.192 35.148 1.00 61.89 ? 281 ALA A CB 1 ATOM 2239 N N . GLU A 1 279 ? 6.711 50.622 36.733 1.00 66.76 ? 282 GLU A N 1 ATOM 2240 C CA . GLU A 1 279 ? 7.911 51.241 37.278 1.00 68.97 ? 282 GLU A CA 1 ATOM 2241 C C . GLU A 1 279 ? 9.173 50.783 36.572 1.00 67.54 ? 282 GLU A C 1 ATOM 2242 O O . GLU A 1 279 ? 10.107 51.560 36.411 1.00 68.58 ? 282 GLU A O 1 ATOM 2243 C CB . GLU A 1 279 ? 8.017 50.950 38.775 1.00 73.03 ? 282 GLU A CB 1 ATOM 2244 C CG . GLU A 1 279 ? 8.423 49.528 39.089 1.00 81.14 ? 282 GLU A CG 1 ATOM 2245 C CD . GLU A 1 279 ? 8.273 49.184 40.560 1.00 85.83 ? 282 GLU A CD 1 ATOM 2246 O OE1 . GLU A 1 279 ? 8.367 50.109 41.403 1.00 88.05 ? 282 GLU A OE1 1 ATOM 2247 O OE2 . GLU A 1 279 ? 8.075 47.982 40.871 1.00 88.68 ? 282 GLU A OE2 1 ATOM 2248 N N . GLU A 1 280 ? 9.198 49.525 36.150 1.00 65.76 ? 283 GLU A N 1 ATOM 2249 C CA . GLU A 1 280 ? 10.356 48.974 35.459 1.00 64.08 ? 283 GLU A CA 1 ATOM 2250 C C . GLU A 1 280 ? 10.532 49.537 34.039 1.00 63.76 ? 283 GLU A C 1 ATOM 2251 O O . GLU A 1 280 ? 11.652 49.571 33.512 1.00 63.12 ? 283 GLU A O 1 ATOM 2252 C CB . GLU A 1 280 ? 10.228 47.457 35.365 1.00 63.75 ? 283 GLU A CB 1 ATOM 2253 C CG . GLU A 1 280 ? 10.036 46.749 36.679 1.00 66.22 ? 283 GLU A CG 1 ATOM 2254 C CD . GLU A 1 280 ? 11.090 47.126 37.688 1.00 70.44 ? 283 GLU A CD 1 ATOM 2255 O OE1 . GLU A 1 280 ? 12.247 47.393 37.276 1.00 72.45 ? 283 GLU A OE1 1 ATOM 2256 O OE2 . GLU A 1 280 ? 10.761 47.142 38.896 1.00 71.36 ? 283 GLU A OE2 1 ATOM 2257 N N . LEU A 1 281 ? 9.430 49.980 33.427 1.00 62.07 ? 284 LEU A N 1 ATOM 2258 C CA . LEU A 1 281 ? 9.447 50.502 32.056 1.00 58.49 ? 284 LEU A CA 1 ATOM 2259 C C . LEU A 1 281 ? 10.663 51.325 31.635 1.00 57.53 ? 284 LEU A C 1 ATOM 2260 O O . LEU A 1 281 ? 11.323 50.997 30.654 1.00 56.86 ? 284 LEU A O 1 ATOM 2261 C CB . LEU A 1 281 ? 8.175 51.304 31.773 1.00 53.67 ? 284 LEU A CB 1 ATOM 2262 C CG . LEU A 1 281 ? 6.894 50.477 31.708 1.00 49.99 ? 284 LEU A CG 1 ATOM 2263 C CD1 . LEU A 1 281 ? 5.777 51.350 31.190 1.00 48.65 ? 284 LEU A CD1 1 ATOM 2264 C CD2 . LEU A 1 281 ? 7.078 49.295 30.785 1.00 50.28 ? 284 LEU A CD2 1 ATOM 2265 N N . PRO A 1 282 ? 10.973 52.407 32.360 1.00 57.23 ? 285 PRO A N 1 ATOM 2266 C CA . PRO A 1 282 ? 12.141 53.174 31.933 1.00 55.51 ? 285 PRO A CA 1 ATOM 2267 C C . PRO A 1 282 ? 13.419 52.349 31.800 1.00 55.91 ? 285 PRO A C 1 ATOM 2268 O O . PRO A 1 282 ? 14.204 52.578 30.880 1.00 56.97 ? 285 PRO A O 1 ATOM 2269 C CB . PRO A 1 282 ? 12.237 54.276 32.991 1.00 54.15 ? 285 PRO A CB 1 ATOM 2270 C CG . PRO A 1 282 ? 11.554 53.692 34.186 1.00 55.18 ? 285 PRO A CG 1 ATOM 2271 C CD . PRO A 1 282 ? 10.374 52.989 33.573 1.00 56.91 ? 285 PRO A CD 1 ATOM 2272 N N . LYS A 1 283 ? 13.620 51.380 32.690 1.00 56.15 ? 286 LYS A N 1 ATOM 2273 C CA . LYS A 1 283 ? 14.826 50.555 32.648 1.00 56.25 ? 286 LYS A CA 1 ATOM 2274 C C . LYS A 1 283 ? 14.878 49.751 31.363 1.00 54.32 ? 286 LYS A C 1 ATOM 2275 O O . LYS A 1 283 ? 15.934 49.552 30.791 1.00 54.77 ? 286 LYS A O 1 ATOM 2276 C CB . LYS A 1 283 ? 14.869 49.614 33.845 1.00 60.02 ? 286 LYS A CB 1 ATOM 2277 C CG . LYS A 1 283 ? 16.186 48.863 34.000 1.00 67.98 ? 286 LYS A CG 1 ATOM 2278 C CD . LYS A 1 283 ? 16.053 47.689 35.003 1.00 74.63 ? 286 LYS A CD 1 ATOM 2279 C CE . LYS A 1 283 ? 17.393 46.956 35.264 1.00 77.25 ? 286 LYS A CE 1 ATOM 2280 N NZ . LYS A 1 283 ? 17.259 45.713 36.107 1.00 76.78 ? 286 LYS A NZ 1 ATOM 2281 N N . TYR A 1 284 ? 13.727 49.289 30.906 1.00 53.12 ? 287 TYR A N 1 ATOM 2282 C CA . TYR A 1 284 ? 13.651 48.524 29.676 1.00 50.94 ? 287 TYR A CA 1 ATOM 2283 C C . TYR A 1 284 ? 14.057 49.363 28.481 1.00 52.67 ? 287 TYR A C 1 ATOM 2284 O O . TYR A 1 284 ? 14.616 48.852 27.527 1.00 54.77 ? 287 TYR A O 1 ATOM 2285 C CB . TYR A 1 284 ? 12.234 48.028 29.474 1.00 48.83 ? 287 TYR A CB 1 ATOM 2286 C CG . TYR A 1 284 ? 11.980 46.713 30.136 1.00 49.82 ? 287 TYR A CG 1 ATOM 2287 C CD1 . TYR A 1 284 ? 12.449 45.539 29.566 1.00 48.49 ? 287 TYR A CD1 1 ATOM 2288 C CD2 . TYR A 1 284 ? 11.292 46.638 31.349 1.00 48.60 ? 287 TYR A CD2 1 ATOM 2289 C CE1 . TYR A 1 284 ? 12.247 44.316 30.174 1.00 49.45 ? 287 TYR A CE1 1 ATOM 2290 C CE2 . TYR A 1 284 ? 11.086 45.406 31.976 1.00 49.36 ? 287 TYR A CE2 1 ATOM 2291 C CZ . TYR A 1 284 ? 11.571 44.249 31.379 1.00 50.19 ? 287 TYR A CZ 1 ATOM 2292 O OH . TYR A 1 284 ? 11.411 43.018 31.986 1.00 51.93 ? 287 TYR A OH 1 ATOM 2293 N N . TRP A 1 285 ? 13.762 50.654 28.528 1.00 53.33 ? 288 TRP A N 1 ATOM 2294 C CA . TRP A 1 285 ? 14.102 51.547 27.432 1.00 54.11 ? 288 TRP A CA 1 ATOM 2295 C C . TRP A 1 285 ? 15.578 51.846 27.450 1.00 55.77 ? 288 TRP A C 1 ATOM 2296 O O . TRP A 1 285 ? 16.241 51.872 26.415 1.00 55.30 ? 288 TRP A O 1 ATOM 2297 C CB . TRP A 1 285 ? 13.313 52.850 27.545 1.00 53.12 ? 288 TRP A CB 1 ATOM 2298 C CG . TRP A 1 285 ? 13.906 53.988 26.772 1.00 53.35 ? 288 TRP A CG 1 ATOM 2299 C CD1 . TRP A 1 285 ? 14.634 55.024 27.277 1.00 53.02 ? 288 TRP A CD1 1 ATOM 2300 C CD2 . TRP A 1 285 ? 13.804 54.222 25.359 1.00 53.52 ? 288 TRP A CD2 1 ATOM 2301 N NE1 . TRP A 1 285 ? 14.987 55.896 26.273 1.00 52.36 ? 288 TRP A NE1 1 ATOM 2302 C CE2 . TRP A 1 285 ? 14.492 55.427 25.085 1.00 52.81 ? 288 TRP A CE2 1 ATOM 2303 C CE3 . TRP A 1 285 ? 13.197 53.532 24.297 1.00 53.68 ? 288 TRP A CE3 1 ATOM 2304 C CZ2 . TRP A 1 285 ? 14.590 55.961 23.789 1.00 53.52 ? 288 TRP A CZ2 1 ATOM 2305 C CZ3 . TRP A 1 285 ? 13.294 54.065 23.001 1.00 52.84 ? 288 TRP A CZ3 1 ATOM 2306 C CH2 . TRP A 1 285 ? 13.986 55.269 22.764 1.00 52.77 ? 288 TRP A CH2 1 ATOM 2307 N N . GLU A 1 286 ? 16.098 52.078 28.638 1.00 58.20 ? 289 GLU A N 1 ATOM 2308 C CA . GLU A 1 286 ? 17.505 52.377 28.755 1.00 61.11 ? 289 GLU A CA 1 ATOM 2309 C C . GLU A 1 286 ? 18.342 51.206 28.268 1.00 60.12 ? 289 GLU A C 1 ATOM 2310 O O . GLU A 1 286 ? 19.445 51.396 27.762 1.00 59.71 ? 289 GLU A O 1 ATOM 2311 C CB . GLU A 1 286 ? 17.870 52.696 30.202 1.00 65.55 ? 289 GLU A CB 1 ATOM 2312 C CG . GLU A 1 286 ? 19.336 53.083 30.376 1.00 75.67 ? 289 GLU A CG 1 ATOM 2313 C CD . GLU A 1 286 ? 19.717 54.402 29.673 1.00 81.74 ? 289 GLU A CD 1 ATOM 2314 O OE1 . GLU A 1 286 ? 18.820 55.256 29.436 1.00 83.14 ? 289 GLU A OE1 1 ATOM 2315 O OE2 . GLU A 1 286 ? 20.927 54.589 29.374 1.00 84.54 ? 289 GLU A OE2 1 ATOM 2316 N N . GLN A 1 287 ? 17.812 49.998 28.405 1.00 59.60 ? 290 GLN A N 1 ATOM 2317 C CA . GLN A 1 287 ? 18.542 48.809 28.004 1.00 59.47 ? 290 GLN A CA 1 ATOM 2318 C C . GLN A 1 287 ? 18.380 48.437 26.554 1.00 57.70 ? 290 GLN A C 1 ATOM 2319 O O . GLN A 1 287 ? 19.173 47.672 26.022 1.00 57.96 ? 290 GLN A O 1 ATOM 2320 C CB . GLN A 1 287 ? 18.090 47.626 28.825 1.00 64.10 ? 290 GLN A CB 1 ATOM 2321 C CG . GLN A 1 287 ? 18.312 47.764 30.299 1.00 74.27 ? 290 GLN A CG 1 ATOM 2322 C CD . GLN A 1 287 ? 17.530 46.717 31.078 1.00 80.40 ? 290 GLN A CD 1 ATOM 2323 O OE1 . GLN A 1 287 ? 17.712 46.562 32.290 1.00 85.42 ? 290 GLN A OE1 1 ATOM 2324 N NE2 . GLN A 1 287 ? 16.643 45.995 30.382 1.00 81.76 ? 290 GLN A NE2 1 ATOM 2325 N N . ASN A 1 288 ? 17.351 48.957 25.906 1.00 55.50 ? 291 ASN A N 1 ATOM 2326 C CA . ASN A 1 288 ? 17.127 48.602 24.522 1.00 52.41 ? 291 ASN A CA 1 ATOM 2327 C C . ASN A 1 288 ? 17.296 49.732 23.544 1.00 52.58 ? 291 ASN A C 1 ATOM 2328 O O . ASN A 1 288 ? 17.444 49.481 22.356 1.00 55.07 ? 291 ASN A O 1 ATOM 2329 C CB . ASN A 1 288 ? 15.739 47.988 24.366 1.00 49.76 ? 291 ASN A CB 1 ATOM 2330 C CG . ASN A 1 288 ? 15.666 46.596 24.937 1.00 50.89 ? 291 ASN A CG 1 ATOM 2331 O OD1 . ASN A 1 288 ? 15.955 45.623 24.246 1.00 50.06 ? 291 ASN A OD1 1 ATOM 2332 N ND2 . ASN A 1 288 ? 15.303 46.488 26.216 1.00 49.37 ? 291 ASN A ND2 1 ATOM 2333 N N . ARG A 1 289 ? 17.293 50.971 24.024 1.00 51.72 ? 292 ARG A N 1 ATOM 2334 C CA . ARG A 1 289 ? 17.437 52.105 23.116 1.00 50.71 ? 292 ARG A CA 1 ATOM 2335 C C . ARG A 1 289 ? 18.559 51.963 22.081 1.00 50.13 ? 292 ARG A C 1 ATOM 2336 O O . ARG A 1 289 ? 18.320 52.048 20.877 1.00 48.21 ? 292 ARG A O 1 ATOM 2337 C CB . ARG A 1 289 ? 17.634 53.409 23.893 1.00 50.05 ? 292 ARG A CB 1 ATOM 2338 C CG . ARG A 1 289 ? 18.161 54.541 23.008 1.00 49.71 ? 292 ARG A CG 1 ATOM 2339 C CD . ARG A 1 289 ? 17.952 55.884 23.639 1.00 54.55 ? 292 ARG A CD 1 ATOM 2340 N NE . ARG A 1 289 ? 18.217 55.828 25.068 1.00 58.96 ? 292 ARG A NE 1 ATOM 2341 C CZ . ARG A 1 289 ? 19.428 55.724 25.588 1.00 60.36 ? 292 ARG A CZ 1 ATOM 2342 N NH1 . ARG A 1 289 ? 20.478 55.673 24.788 1.00 63.10 ? 292 ARG A NH1 1 ATOM 2343 N NH2 . ARG A 1 289 ? 19.589 55.669 26.900 1.00 61.50 ? 292 ARG A NH2 1 ATOM 2344 N N . ARG A 1 290 ? 19.788 51.756 22.527 1.00 49.85 ? 293 ARG A N 1 ATOM 2345 C CA . ARG A 1 290 ? 20.849 51.629 21.553 1.00 50.14 ? 293 ARG A CA 1 ATOM 2346 C C . ARG A 1 290 ? 20.569 50.437 20.633 1.00 50.76 ? 293 ARG A C 1 ATOM 2347 O O . ARG A 1 290 ? 20.838 50.502 19.434 1.00 51.50 ? 293 ARG A O 1 ATOM 2348 C CB . ARG A 1 290 ? 22.195 51.497 22.262 1.00 51.03 ? 293 ARG A CB 1 ATOM 2349 C CG . ARG A 1 290 ? 23.417 51.455 21.342 1.00 51.20 ? 293 ARG A CG 1 ATOM 2350 C CD . ARG A 1 290 ? 23.296 52.359 20.111 1.00 52.22 ? 293 ARG A CD 1 ATOM 2351 N NE . ARG A 1 290 ? 23.045 53.762 20.419 1.00 54.31 ? 293 ARG A NE 1 ATOM 2352 C CZ . ARG A 1 290 ? 22.842 54.699 19.495 1.00 54.62 ? 293 ARG A CZ 1 ATOM 2353 N NH1 . ARG A 1 290 ? 22.872 54.375 18.204 1.00 52.87 ? 293 ARG A NH1 1 ATOM 2354 N NH2 . ARG A 1 290 ? 22.581 55.951 19.863 1.00 52.44 ? 293 ARG A NH2 1 ATOM 2355 N N . SER A 1 291 ? 20.015 49.356 21.181 1.00 49.50 ? 294 SER A N 1 ATOM 2356 C CA . SER A 1 291 ? 19.685 48.185 20.368 1.00 46.64 ? 294 SER A CA 1 ATOM 2357 C C . SER A 1 291 ? 18.706 48.540 19.246 1.00 47.30 ? 294 SER A C 1 ATOM 2358 O O . SER A 1 291 ? 18.989 48.324 18.066 1.00 48.06 ? 294 SER A O 1 ATOM 2359 C CB . SER A 1 291 ? 19.067 47.090 21.228 1.00 43.78 ? 294 SER A CB 1 ATOM 2360 O OG . SER A 1 291 ? 20.004 46.608 22.164 1.00 43.00 ? 294 SER A OG 1 ATOM 2361 N N . LEU A 1 292 ? 17.551 49.085 19.616 1.00 47.89 ? 295 LEU A N 1 ATOM 2362 C CA . LEU A 1 292 ? 16.545 49.445 18.627 1.00 47.12 ? 295 LEU A CA 1 ATOM 2363 C C . LEU A 1 292 ? 17.154 50.305 17.536 1.00 47.45 ? 295 LEU A C 1 ATOM 2364 O O . LEU A 1 292 ? 16.825 50.174 16.355 1.00 46.54 ? 295 LEU A O 1 ATOM 2365 C CB . LEU A 1 292 ? 15.385 50.232 19.259 1.00 47.14 ? 295 LEU A CB 1 ATOM 2366 C CG . LEU A 1 292 ? 14.219 49.686 20.097 1.00 45.21 ? 295 LEU A CG 1 ATOM 2367 C CD1 . LEU A 1 292 ? 13.805 48.322 19.569 1.00 44.44 ? 295 LEU A CD1 1 ATOM 2368 C CD2 . LEU A 1 292 ? 14.609 49.626 21.556 1.00 44.50 ? 295 LEU A CD2 1 ATOM 2369 N N . LEU A 1 293 ? 18.034 51.204 17.944 1.00 48.72 ? 296 LEU A N 1 ATOM 2370 C CA . LEU A 1 293 ? 18.673 52.113 17.003 1.00 49.76 ? 296 LEU A CA 1 ATOM 2371 C C . LEU A 1 293 ? 19.598 51.362 16.074 1.00 51.24 ? 296 LEU A C 1 ATOM 2372 O O . LEU A 1 293 ? 19.418 51.373 14.854 1.00 52.37 ? 296 LEU A O 1 ATOM 2373 C CB . LEU A 1 293 ? 19.472 53.180 17.764 1.00 48.50 ? 296 LEU A CB 1 ATOM 2374 C CG . LEU A 1 293 ? 18.894 54.593 17.976 1.00 45.86 ? 296 LEU A CG 1 ATOM 2375 C CD1 . LEU A 1 293 ? 17.480 54.676 17.431 1.00 44.03 ? 296 LEU A CD1 1 ATOM 2376 C CD2 . LEU A 1 293 ? 18.952 54.959 19.451 1.00 42.26 ? 296 LEU A CD2 1 ATOM 2377 N N . GLN A 1 294 ? 20.589 50.707 16.668 1.00 52.79 ? 297 GLN A N 1 ATOM 2378 C CA . GLN A 1 294 ? 21.563 49.957 15.904 1.00 54.12 ? 297 GLN A CA 1 ATOM 2379 C C . GLN A 1 294 ? 20.887 48.985 14.963 1.00 53.91 ? 297 GLN A C 1 ATOM 2380 O O . GLN A 1 294 ? 21.327 48.795 13.838 1.00 56.61 ? 297 GLN A O 1 ATOM 2381 C CB . GLN A 1 294 ? 22.519 49.207 16.836 1.00 55.03 ? 297 GLN A CB 1 ATOM 2382 C CG . GLN A 1 294 ? 23.535 50.112 17.500 1.00 58.69 ? 297 GLN A CG 1 ATOM 2383 C CD . GLN A 1 294 ? 24.303 50.950 16.488 1.00 63.16 ? 297 GLN A CD 1 ATOM 2384 O OE1 . GLN A 1 294 ? 24.374 52.182 16.596 1.00 66.20 ? 297 GLN A OE1 1 ATOM 2385 N NE2 . GLN A 1 294 ? 24.884 50.284 15.496 1.00 64.99 ? 297 GLN A NE2 1 ATOM 2386 N N . PHE A 1 295 ? 19.803 48.373 15.404 1.00 51.98 ? 298 PHE A N 1 ATOM 2387 C CA . PHE A 1 295 ? 19.151 47.425 14.534 1.00 50.80 ? 298 PHE A CA 1 ATOM 2388 C C . PHE A 1 295 ? 18.650 48.077 13.242 1.00 52.21 ? 298 PHE A C 1 ATOM 2389 O O . PHE A 1 295 ? 18.947 47.606 12.150 1.00 53.32 ? 298 PHE A O 1 ATOM 2390 C CB . PHE A 1 295 ? 17.999 46.748 15.259 1.00 49.37 ? 298 PHE A CB 1 ATOM 2391 C CG . PHE A 1 295 ? 17.351 45.672 14.453 1.00 49.39 ? 298 PHE A CG 1 ATOM 2392 C CD1 . PHE A 1 295 ? 17.995 44.460 14.255 1.00 49.53 ? 298 PHE A CD1 1 ATOM 2393 C CD2 . PHE A 1 295 ? 16.111 45.883 13.854 1.00 49.67 ? 298 PHE A CD2 1 ATOM 2394 C CE1 . PHE A 1 295 ? 17.413 43.470 13.467 1.00 50.17 ? 298 PHE A CE1 1 ATOM 2395 C CE2 . PHE A 1 295 ? 15.521 44.901 13.062 1.00 50.32 ? 298 PHE A CE2 1 ATOM 2396 C CZ . PHE A 1 295 ? 16.171 43.694 12.867 1.00 49.32 ? 298 PHE A CZ 1 ATOM 2397 N N . ILE A 1 296 ? 17.897 49.161 13.348 1.00 52.98 ? 299 ILE A N 1 ATOM 2398 C CA . ILE A 1 296 ? 17.389 49.817 12.149 1.00 53.22 ? 299 ILE A CA 1 ATOM 2399 C C . ILE A 1 296 ? 18.469 50.102 11.098 1.00 55.33 ? 299 ILE A C 1 ATOM 2400 O O . ILE A 1 296 ? 18.237 49.947 9.896 1.00 55.55 ? 299 ILE A O 1 ATOM 2401 C CB . ILE A 1 296 ? 16.738 51.141 12.488 1.00 50.59 ? 299 ILE A CB 1 ATOM 2402 C CG1 . ILE A 1 296 ? 15.575 50.917 13.441 1.00 49.56 ? 299 ILE A CG1 1 ATOM 2403 C CG2 . ILE A 1 296 ? 16.251 51.797 11.224 1.00 49.68 ? 299 ILE A CG2 1 ATOM 2404 C CD1 . ILE A 1 296 ? 14.999 52.194 13.958 1.00 48.76 ? 299 ILE A CD1 1 ATOM 2405 N N . LYS A 1 297 ? 19.644 50.532 11.553 1.00 55.91 ? 300 LYS A N 1 ATOM 2406 C CA . LYS A 1 297 ? 20.733 50.851 10.644 1.00 56.30 ? 300 LYS A CA 1 ATOM 2407 C C . LYS A 1 297 ? 21.088 49.686 9.711 1.00 58.41 ? 300 LYS A C 1 ATOM 2408 O O . LYS A 1 297 ? 21.506 49.905 8.573 1.00 60.10 ? 300 LYS A O 1 ATOM 2409 C CB . LYS A 1 297 ? 21.966 51.280 11.445 1.00 55.65 ? 300 LYS A CB 1 ATOM 2410 C CG . LYS A 1 297 ? 21.768 52.492 12.369 1.00 57.80 ? 300 LYS A CG 1 ATOM 2411 C CD . LYS A 1 297 ? 23.075 52.822 13.138 1.00 60.72 ? 300 LYS A CD 1 ATOM 2412 C CE . LYS A 1 297 ? 22.959 54.055 14.064 1.00 60.63 ? 300 LYS A CE 1 ATOM 2413 N NZ . LYS A 1 297 ? 24.282 54.448 14.686 1.00 63.89 ? 300 LYS A NZ 1 ATOM 2414 N N . GLN A 1 298 ? 20.919 48.452 10.184 1.00 59.25 ? 301 GLN A N 1 ATOM 2415 C CA . GLN A 1 298 ? 21.233 47.265 9.382 1.00 60.24 ? 301 GLN A CA 1 ATOM 2416 C C . GLN A 1 298 ? 20.503 47.253 8.059 1.00 61.80 ? 301 GLN A C 1 ATOM 2417 O O . GLN A 1 298 ? 20.908 46.558 7.129 1.00 64.04 ? 301 GLN A O 1 ATOM 2418 C CB . GLN A 1 298 ? 20.839 45.989 10.115 1.00 59.80 ? 301 GLN A CB 1 ATOM 2419 C CG . GLN A 1 298 ? 21.525 45.782 11.430 1.00 60.11 ? 301 GLN A CG 1 ATOM 2420 C CD . GLN A 1 298 ? 22.974 45.466 11.262 1.00 61.42 ? 301 GLN A CD 1 ATOM 2421 O OE1 . GLN A 1 298 ? 23.820 46.140 11.838 1.00 62.80 ? 301 GLN A OE1 1 ATOM 2422 N NE2 . GLN A 1 298 ? 23.281 44.429 10.469 1.00 60.37 ? 301 GLN A NE2 1 ATOM 2423 N N . VAL A 1 299 ? 19.409 48.001 7.990 1.00 62.87 ? 302 VAL A N 1 ATOM 2424 C CA . VAL A 1 299 ? 18.594 48.063 6.790 1.00 64.37 ? 302 VAL A CA 1 ATOM 2425 C C . VAL A 1 299 ? 19.394 48.657 5.641 1.00 67.26 ? 302 VAL A C 1 ATOM 2426 O O . VAL A 1 299 ? 19.038 48.503 4.472 1.00 67.21 ? 302 VAL A O 1 ATOM 2427 C CB . VAL A 1 299 ? 17.341 48.922 7.034 1.00 62.58 ? 302 VAL A CB 1 ATOM 2428 C CG1 . VAL A 1 299 ? 17.722 50.381 7.066 1.00 62.75 ? 302 VAL A CG1 1 ATOM 2429 C CG2 . VAL A 1 299 ? 16.307 48.657 5.971 1.00 63.05 ? 302 VAL A CG2 1 ATOM 2430 N N . HIS A 1 300 ? 20.487 49.330 5.982 1.00 70.97 ? 303 HIS A N 1 ATOM 2431 C CA . HIS A 1 300 ? 21.336 49.956 4.975 1.00 75.06 ? 303 HIS A CA 1 ATOM 2432 C C . HIS A 1 300 ? 22.486 49.089 4.469 1.00 77.72 ? 303 HIS A C 1 ATOM 2433 O O . HIS A 1 300 ? 22.950 49.269 3.335 1.00 80.78 ? 303 HIS A O 1 ATOM 2434 C CB . HIS A 1 300 ? 21.876 51.286 5.508 1.00 72.88 ? 303 HIS A CB 1 ATOM 2435 C CG . HIS A 1 300 ? 20.826 52.341 5.615 1.00 71.51 ? 303 HIS A CG 1 ATOM 2436 N ND1 . HIS A 1 300 ? 20.041 52.708 4.542 1.00 71.32 ? 303 HIS A ND1 1 ATOM 2437 C CD2 . HIS A 1 300 ? 20.377 53.052 6.674 1.00 71.29 ? 303 HIS A CD2 1 ATOM 2438 C CE1 . HIS A 1 300 ? 19.147 53.596 4.940 1.00 71.48 ? 303 HIS A CE1 1 ATOM 2439 N NE2 . HIS A 1 300 ? 19.329 53.821 6.229 1.00 71.59 ? 303 HIS A NE2 1 ATOM 2440 N N . ARG A 1 301 ? 22.931 48.147 5.299 1.00 78.32 ? 304 ARG A N 1 ATOM 2441 C CA . ARG A 1 301 ? 24.028 47.257 4.942 1.00 77.52 ? 304 ARG A CA 1 ATOM 2442 C C . ARG A 1 301 ? 23.733 46.301 3.794 1.00 76.47 ? 304 ARG A C 1 ATOM 2443 O O . ARG A 1 301 ? 22.577 46.056 3.443 1.00 75.38 ? 304 ARG A O 1 ATOM 2444 C CB . ARG A 1 301 ? 24.471 46.468 6.165 1.00 79.30 ? 304 ARG A CB 1 ATOM 2445 C CG . ARG A 1 301 ? 25.028 47.345 7.263 1.00 81.73 ? 304 ARG A CG 1 ATOM 2446 C CD . ARG A 1 301 ? 25.978 46.561 8.136 1.00 85.07 ? 304 ARG A CD 1 ATOM 2447 N NE . ARG A 1 301 ? 26.485 47.377 9.229 1.00 89.25 ? 304 ARG A NE 1 ATOM 2448 C CZ . ARG A 1 301 ? 27.444 47.000 10.072 1.00 91.65 ? 304 ARG A CZ 1 ATOM 2449 N NH1 . ARG A 1 301 ? 28.019 45.799 9.948 1.00 90.80 ? 304 ARG A NH1 1 ATOM 2450 N NH2 . ARG A 1 301 ? 27.821 47.825 11.050 1.00 92.17 ? 304 ARG A NH2 1 ATOM 2451 N N . GLY A 1 302 ? 24.802 45.765 3.214 1.00 75.35 ? 305 GLY A N 1 ATOM 2452 C CA . GLY A 1 302 ? 24.659 44.857 2.099 1.00 74.15 ? 305 GLY A CA 1 ATOM 2453 C C . GLY A 1 302 ? 24.803 45.569 0.762 1.00 73.87 ? 305 GLY A C 1 ATOM 2454 O O . GLY A 1 302 ? 25.729 46.352 0.569 1.00 74.30 ? 305 GLY A O 1 ATOM 2455 N N . ILE A 1 303 ? 23.859 45.312 -0.143 1.00 73.34 ? 306 ILE A N 1 ATOM 2456 C CA . ILE A 1 303 ? 23.841 45.860 -1.500 1.00 70.69 ? 306 ILE A CA 1 ATOM 2457 C C . ILE A 1 303 ? 22.477 46.407 -1.883 1.00 69.72 ? 306 ILE A C 1 ATOM 2458 O O . ILE A 1 303 ? 21.444 45.902 -1.439 1.00 68.29 ? 306 ILE A O 1 ATOM 2459 C CB . ILE A 1 303 ? 24.175 44.755 -2.520 1.00 71.60 ? 306 ILE A CB 1 ATOM 2460 C CG1 . ILE A 1 303 ? 25.675 44.550 -2.576 1.00 72.64 ? 306 ILE A CG1 1 ATOM 2461 C CG2 . ILE A 1 303 ? 23.604 45.078 -3.892 1.00 69.64 ? 306 ILE A CG2 1 ATOM 2462 C CD1 . ILE A 1 303 ? 26.044 43.343 -3.384 1.00 77.41 ? 306 ILE A CD1 1 ATOM 2463 N N . TRP A 1 304 ? 22.484 47.415 -2.749 1.00 69.81 ? 307 TRP A N 1 ATOM 2464 C CA . TRP A 1 304 ? 21.251 48.034 -3.229 1.00 68.31 ? 307 TRP A CA 1 ATOM 2465 C C . TRP A 1 304 ? 21.517 48.817 -4.512 1.00 66.19 ? 307 TRP A C 1 ATOM 2466 O O . TRP A 1 304 ? 22.660 49.149 -4.839 1.00 65.06 ? 307 TRP A O 1 ATOM 2467 C CB . TRP A 1 304 ? 20.686 48.974 -2.170 1.00 69.29 ? 307 TRP A CB 1 ATOM 2468 C CG . TRP A 1 304 ? 21.599 50.124 -1.882 1.00 70.33 ? 307 TRP A CG 1 ATOM 2469 C CD1 . TRP A 1 304 ? 22.784 50.104 -1.174 1.00 69.05 ? 307 TRP A CD1 1 ATOM 2470 C CD2 . TRP A 1 304 ? 21.431 51.460 -2.346 1.00 70.57 ? 307 TRP A CD2 1 ATOM 2471 N NE1 . TRP A 1 304 ? 23.359 51.356 -1.179 1.00 69.40 ? 307 TRP A NE1 1 ATOM 2472 C CE2 . TRP A 1 304 ? 22.551 52.207 -1.891 1.00 70.11 ? 307 TRP A CE2 1 ATOM 2473 C CE3 . TRP A 1 304 ? 20.439 52.107 -3.108 1.00 69.27 ? 307 TRP A CE3 1 ATOM 2474 C CZ2 . TRP A 1 304 ? 22.702 53.566 -2.174 1.00 69.24 ? 307 TRP A CZ2 1 ATOM 2475 C CZ3 . TRP A 1 304 ? 20.588 53.455 -3.387 1.00 69.18 ? 307 TRP A CZ3 1 ATOM 2476 C CH2 . TRP A 1 304 ? 21.714 54.172 -2.921 1.00 70.52 ? 307 TRP A CH2 1 ATOM 2477 N N . GLY A 1 305 ? 20.451 49.126 -5.230 1.00 63.41 ? 308 GLY A N 1 ATOM 2478 C CA . GLY A 1 305 ? 20.618 49.842 -6.467 1.00 63.47 ? 308 GLY A CA 1 ATOM 2479 C C . GLY A 1 305 ? 19.359 49.740 -7.290 1.00 65.70 ? 308 GLY A C 1 ATOM 2480 O O . GLY A 1 305 ? 18.264 49.534 -6.747 1.00 66.98 ? 308 GLY A O 1 ATOM 2481 N N . PHE A 1 306 ? 19.513 49.878 -8.606 1.00 66.94 ? 309 PHE A N 1 ATOM 2482 C CA . PHE A 1 306 ? 18.374 49.831 -9.516 1.00 66.60 ? 309 PHE A CA 1 ATOM 2483 C C . PHE A 1 306 ? 18.623 48.945 -10.714 1.00 67.47 ? 309 PHE A C 1 ATOM 2484 O O . PHE A 1 306 ? 19.763 48.737 -11.140 1.00 66.27 ? 309 PHE A O 1 ATOM 2485 C CB . PHE A 1 306 ? 18.029 51.221 -10.071 1.00 65.57 ? 309 PHE A CB 1 ATOM 2486 C CG . PHE A 1 306 ? 17.791 52.272 -9.025 1.00 62.53 ? 309 PHE A CG 1 ATOM 2487 C CD1 . PHE A 1 306 ? 18.854 52.793 -8.283 1.00 60.52 ? 309 PHE A CD1 1 ATOM 2488 C CD2 . PHE A 1 306 ? 16.502 52.748 -8.789 1.00 59.76 ? 309 PHE A CD2 1 ATOM 2489 C CE1 . PHE A 1 306 ? 18.637 53.764 -7.325 1.00 57.31 ? 309 PHE A CE1 1 ATOM 2490 C CE2 . PHE A 1 306 ? 16.276 53.714 -7.837 1.00 55.95 ? 309 PHE A CE2 1 ATOM 2491 C CZ . PHE A 1 306 ? 17.343 54.225 -7.101 1.00 56.65 ? 309 PHE A CZ 1 ATOM 2492 N N . VAL A 1 307 ? 17.511 48.465 -11.259 1.00 69.02 ? 310 VAL A N 1 ATOM 2493 C CA . VAL A 1 307 ? 17.475 47.617 -12.436 1.00 70.67 ? 310 VAL A CA 1 ATOM 2494 C C . VAL A 1 307 ? 16.805 48.484 -13.504 1.00 72.04 ? 310 VAL A C 1 ATOM 2495 O O . VAL A 1 307 ? 15.579 48.522 -13.652 1.00 69.87 ? 310 VAL A O 1 ATOM 2496 C CB . VAL A 1 307 ? 16.657 46.329 -12.168 1.00 70.50 ? 310 VAL A CB 1 ATOM 2497 C CG1 . VAL A 1 307 ? 16.382 45.603 -13.470 1.00 70.85 ? 310 VAL A CG1 1 ATOM 2498 C CG2 . VAL A 1 307 ? 17.425 45.421 -11.205 1.00 68.48 ? 310 VAL A CG2 1 ATOM 2499 N N . LEU A 1 308 ? 17.657 49.203 -14.221 1.00 74.56 ? 311 LEU A N 1 ATOM 2500 C CA . LEU A 1 308 ? 17.259 50.123 -15.271 1.00 76.10 ? 311 LEU A CA 1 ATOM 2501 C C . LEU A 1 308 ? 17.096 49.412 -16.610 1.00 77.73 ? 311 LEU A C 1 ATOM 2502 O O . LEU A 1 308 ? 17.920 48.581 -16.992 1.00 79.15 ? 311 LEU A O 1 ATOM 2503 C CB . LEU A 1 308 ? 18.334 51.203 -15.406 1.00 74.54 ? 311 LEU A CB 1 ATOM 2504 C CG . LEU A 1 308 ? 18.864 51.739 -14.073 1.00 74.17 ? 311 LEU A CG 1 ATOM 2505 C CD1 . LEU A 1 308 ? 20.269 52.295 -14.233 1.00 72.34 ? 311 LEU A CD1 1 ATOM 2506 C CD2 . LEU A 1 308 ? 17.905 52.786 -13.541 1.00 74.03 ? 311 LEU A CD2 1 ATOM 2507 N N . ASP A 1 309 ? 16.023 49.738 -17.316 1.00 79.13 ? 312 ASP A N 1 ATOM 2508 C CA . ASP A 1 309 ? 15.772 49.178 -18.635 1.00 80.83 ? 312 ASP A CA 1 ATOM 2509 C C . ASP A 1 309 ? 16.673 49.982 -19.586 1.00 82.12 ? 312 ASP A C 1 ATOM 2510 O O . ASP A 1 309 ? 16.480 51.184 -19.750 1.00 82.25 ? 312 ASP A O 1 ATOM 2511 C CB . ASP A 1 309 ? 14.292 49.358 -18.988 1.00 80.08 ? 312 ASP A CB 1 ATOM 2512 C CG . ASP A 1 309 ? 14.024 49.250 -20.471 1.00 80.97 ? 312 ASP A CG 1 ATOM 2513 O OD1 . ASP A 1 309 ? 14.985 49.133 -21.251 1.00 81.98 ? 312 ASP A OD1 1 ATOM 2514 O OD2 . ASP A 1 309 ? 12.844 49.287 -20.864 1.00 80.42 ? 312 ASP A OD2 1 ATOM 2515 N N . ALA A 1 310 ? 17.654 49.314 -20.197 1.00 83.21 ? 313 ALA A N 1 ATOM 2516 C CA . ALA A 1 310 ? 18.614 49.950 -21.106 1.00 84.33 ? 313 ALA A CA 1 ATOM 2517 C C . ALA A 1 310 ? 18.039 50.850 -22.206 1.00 86.71 ? 313 ALA A C 1 ATOM 2518 O O . ALA A 1 310 ? 18.654 51.873 -22.518 1.00 86.99 ? 313 ALA A O 1 ATOM 2519 C CB . ALA A 1 310 ? 19.520 48.892 -21.726 1.00 81.38 ? 313 ALA A CB 1 ATOM 2520 N N . THR A 1 311 ? 16.894 50.491 -22.806 1.00 88.40 ? 314 THR A N 1 ATOM 2521 C CA . THR A 1 311 ? 16.304 51.349 -23.851 1.00 89.68 ? 314 THR A CA 1 ATOM 2522 C C . THR A 1 311 ? 15.610 52.594 -23.256 1.00 92.87 ? 314 THR A C 1 ATOM 2523 O O . THR A 1 311 ? 15.813 53.703 -23.757 1.00 94.92 ? 314 THR A O 1 ATOM 2524 C CB . THR A 1 311 ? 15.294 50.585 -24.805 1.00 86.91 ? 314 THR A CB 1 ATOM 2525 O OG1 . THR A 1 311 ? 14.058 50.300 -24.135 1.00 84.42 ? 314 THR A OG1 1 ATOM 2526 C CG2 . THR A 1 311 ? 15.910 49.296 -25.291 1.00 86.10 ? 314 THR A CG2 1 ATOM 2527 N N . ASP A 1 312 ? 14.812 52.422 -22.193 1.00 93.55 ? 315 ASP A N 1 ATOM 2528 C CA . ASP A 1 312 ? 14.126 53.553 -21.538 1.00 92.43 ? 315 ASP A CA 1 ATOM 2529 C C . ASP A 1 312 ? 15.108 54.364 -20.737 1.00 92.94 ? 315 ASP A C 1 ATOM 2530 O O . ASP A 1 312 ? 15.119 55.593 -20.795 1.00 92.57 ? 315 ASP A O 1 ATOM 2531 C CB . ASP A 1 312 ? 13.071 53.081 -20.549 1.00 91.83 ? 315 ASP A CB 1 ATOM 2532 C CG . ASP A 1 312 ? 11.857 52.542 -21.222 1.00 93.40 ? 315 ASP A CG 1 ATOM 2533 O OD1 . ASP A 1 312 ? 11.308 53.254 -22.086 1.00 94.43 ? 315 ASP A OD1 1 ATOM 2534 O OD2 . ASP A 1 312 ? 11.445 51.412 -20.884 1.00 95.70 ? 315 ASP A OD2 1 ATOM 2535 N N . GLY A 1 313 ? 15.916 53.639 -19.968 1.00 93.64 ? 316 GLY A N 1 ATOM 2536 C CA . GLY A 1 313 ? 16.903 54.245 -19.100 1.00 94.13 ? 316 GLY A CA 1 ATOM 2537 C C . GLY A 1 313 ? 16.268 54.347 -17.725 1.00 93.69 ? 316 GLY A C 1 ATOM 2538 O O . GLY A 1 313 ? 16.819 54.975 -16.813 1.00 93.64 ? 316 GLY A O 1 ATOM 2539 N N . ARG A 1 314 ? 15.101 53.716 -17.580 1.00 93.08 ? 317 ARG A N 1 ATOM 2540 C CA . ARG A 1 314 ? 14.370 53.754 -16.318 1.00 92.39 ? 317 ARG A CA 1 ATOM 2541 C C . ARG A 1 314 ? 14.108 52.397 -15.667 1.00 90.51 ? 317 ARG A C 1 ATOM 2542 O O . ARG A 1 314 ? 14.137 51.351 -16.320 1.00 91.35 ? 317 ARG A O 1 ATOM 2543 C CB . ARG A 1 314 ? 13.048 54.493 -16.510 1.00 93.07 ? 317 ARG A CB 1 ATOM 2544 C CG . ARG A 1 314 ? 12.104 53.817 -17.445 1.00 92.33 ? 317 ARG A CG 1 ATOM 2545 C CD . ARG A 1 314 ? 10.996 54.762 -17.781 1.00 94.79 ? 317 ARG A CD 1 ATOM 2546 N NE . ARG A 1 314 ? 9.817 54.032 -18.220 1.00 97.92 ? 317 ARG A NE 1 ATOM 2547 C CZ . ARG A 1 314 ? 8.744 54.599 -18.761 1.00 97.92 ? 317 ARG A CZ 1 ATOM 2548 N NH1 . ARG A 1 314 ? 8.702 55.922 -18.937 1.00 97.92 ? 317 ARG A NH1 1 ATOM 2549 N NH2 . ARG A 1 314 ? 7.712 53.837 -19.120 1.00 97.92 ? 317 ARG A NH2 1 ATOM 2550 N N . GLY A 1 315 ? 13.836 52.447 -14.367 1.00 87.14 ? 318 GLY A N 1 ATOM 2551 C CA . GLY A 1 315 ? 13.595 51.253 -13.583 1.00 81.07 ? 318 GLY A CA 1 ATOM 2552 C C . GLY A 1 315 ? 12.597 50.232 -14.076 1.00 76.45 ? 318 GLY A C 1 ATOM 2553 O O . GLY A 1 315 ? 11.511 50.547 -14.574 1.00 73.84 ? 318 GLY A O 1 ATOM 2554 N N . ILE A 1 316 ? 12.995 48.978 -13.916 1.00 73.28 ? 319 ILE A N 1 ATOM 2555 C CA . ILE A 1 316 ? 12.173 47.851 -14.294 1.00 70.06 ? 319 ILE A CA 1 ATOM 2556 C C . ILE A 1 316 ? 11.504 47.404 -12.997 1.00 68.72 ? 319 ILE A C 1 ATOM 2557 O O . ILE A 1 316 ? 12.112 47.410 -11.921 1.00 66.03 ? 319 ILE A O 1 ATOM 2558 C CB . ILE A 1 316 ? 13.042 46.709 -14.878 1.00 70.30 ? 319 ILE A CB 1 ATOM 2559 C CG1 . ILE A 1 316 ? 13.885 47.249 -16.042 1.00 69.98 ? 319 ILE A CG1 1 ATOM 2560 C CG2 . ILE A 1 316 ? 12.150 45.557 -15.343 1.00 69.60 ? 319 ILE A CG2 1 ATOM 2561 C CD1 . ILE A 1 316 ? 14.958 46.306 -16.538 1.00 68.20 ? 319 ILE A CD1 1 ATOM 2562 N N . LEU A 1 317 ? 10.240 47.035 -13.097 1.00 68.27 ? 320 LEU A N 1 ATOM 2563 C CA . LEU A 1 317 ? 9.507 46.611 -11.926 1.00 69.00 ? 320 LEU A CA 1 ATOM 2564 C C . LEU A 1 317 ? 9.391 45.107 -11.767 1.00 69.63 ? 320 LEU A C 1 ATOM 2565 O O . LEU A 1 317 ? 8.893 44.416 -12.653 1.00 71.64 ? 320 LEU A O 1 ATOM 2566 C CB . LEU A 1 317 ? 8.097 47.189 -11.946 1.00 67.42 ? 320 LEU A CB 1 ATOM 2567 C CG . LEU A 1 317 ? 7.208 46.565 -10.869 1.00 66.80 ? 320 LEU A CG 1 ATOM 2568 C CD1 . LEU A 1 317 ? 7.500 47.213 -9.518 1.00 65.45 ? 320 LEU A CD1 1 ATOM 2569 C CD2 . LEU A 1 317 ? 5.755 46.734 -11.249 1.00 66.47 ? 320 LEU A CD2 1 ATOM 2570 N N . ASN A 1 318 ? 9.826 44.613 -10.615 1.00 68.55 ? 321 ASN A N 1 ATOM 2571 C CA . ASN A 1 318 ? 9.730 43.199 -10.297 1.00 67.04 ? 321 ASN A CA 1 ATOM 2572 C C . ASN A 1 318 ? 10.798 42.384 -10.989 1.00 66.50 ? 321 ASN A C 1 ATOM 2573 O O . ASN A 1 318 ? 10.575 41.243 -11.397 1.00 66.77 ? 321 ASN A O 1 ATOM 2574 C CB . ASN A 1 318 ? 8.332 42.672 -10.641 1.00 66.09 ? 321 ASN A CB 1 ATOM 2575 C CG . ASN A 1 318 ? 7.996 41.370 -9.928 1.00 66.57 ? 321 ASN A CG 1 ATOM 2576 O OD1 . ASN A 1 318 ? 8.093 41.252 -8.709 1.00 69.51 ? 321 ASN A OD1 1 ATOM 2577 N ND2 . ASN A 1 318 ? 7.572 40.391 -10.703 1.00 66.44 ? 321 ASN A ND2 1 ATOM 2578 N N . ALA A 1 319 ? 11.965 42.994 -11.131 1.00 66.01 ? 322 ALA A N 1 ATOM 2579 C CA . ALA A 1 319 ? 13.099 42.305 -11.709 1.00 66.35 ? 322 ALA A CA 1 ATOM 2580 C C . ALA A 1 319 ? 13.552 41.412 -10.547 1.00 65.76 ? 322 ALA A C 1 ATOM 2581 O O . ALA A 1 319 ? 13.074 41.590 -9.428 1.00 66.90 ? 322 ALA A O 1 ATOM 2582 C CB . ALA A 1 319 ? 14.187 43.309 -12.062 1.00 66.23 ? 322 ALA A CB 1 ATOM 2583 N N . THR A 1 320 ? 14.452 40.461 -10.791 1.00 63.34 ? 323 THR A N 1 ATOM 2584 C CA . THR A 1 320 ? 14.930 39.593 -9.718 1.00 59.95 ? 323 THR A CA 1 ATOM 2585 C C . THR A 1 320 ? 16.408 39.725 -9.448 1.00 59.79 ? 323 THR A C 1 ATOM 2586 O O . THR A 1 320 ? 17.221 39.652 -10.360 1.00 60.40 ? 323 THR A O 1 ATOM 2587 C CB . THR A 1 320 ? 14.725 38.123 -10.026 1.00 58.81 ? 323 THR A CB 1 ATOM 2588 O OG1 . THR A 1 320 ? 13.339 37.798 -9.939 1.00 59.87 ? 323 THR A OG1 1 ATOM 2589 C CG2 . THR A 1 320 ? 15.513 37.280 -9.049 1.00 56.54 ? 323 THR A CG2 1 ATOM 2590 N N . ILE A 1 321 ? 16.766 39.894 -8.190 1.00 58.93 ? 324 ILE A N 1 ATOM 2591 C CA . ILE A 1 321 ? 18.167 39.962 -7.850 1.00 58.98 ? 324 ILE A CA 1 ATOM 2592 C C . ILE A 1 321 ? 18.533 38.626 -7.207 1.00 61.08 ? 324 ILE A C 1 ATOM 2593 O O . ILE A 1 321 ? 18.013 38.268 -6.143 1.00 61.90 ? 324 ILE A O 1 ATOM 2594 C CB . ILE A 1 321 ? 18.444 41.097 -6.885 1.00 57.08 ? 324 ILE A CB 1 ATOM 2595 C CG1 . ILE A 1 321 ? 18.200 42.428 -7.595 1.00 57.62 ? 324 ILE A CG1 1 ATOM 2596 C CG2 . ILE A 1 321 ? 19.875 41.005 -6.374 1.00 54.23 ? 324 ILE A CG2 1 ATOM 2597 C CD1 . ILE A 1 321 ? 19.230 42.778 -8.654 1.00 59.70 ? 324 ILE A CD1 1 ATOM 2598 N N . SER A 1 322 ? 19.415 37.881 -7.869 1.00 61.59 ? 325 SER A N 1 ATOM 2599 C CA . SER A 1 322 ? 19.844 36.583 -7.366 1.00 61.68 ? 325 SER A CA 1 ATOM 2600 C C . SER A 1 322 ? 21.294 36.653 -6.916 1.00 63.00 ? 325 SER A C 1 ATOM 2601 O O . SER A 1 322 ? 22.115 37.291 -7.575 1.00 64.96 ? 325 SER A O 1 ATOM 2602 C CB . SER A 1 322 ? 19.679 35.538 -8.457 1.00 59.87 ? 325 SER A CB 1 ATOM 2603 O OG . SER A 1 322 ? 18.363 35.592 -8.968 1.00 58.80 ? 325 SER A OG 1 ATOM 2604 N N . VAL A 1 323 ? 21.617 36.009 -5.796 1.00 62.96 ? 326 VAL A N 1 ATOM 2605 C CA . VAL A 1 323 ? 22.984 36.058 -5.319 1.00 62.24 ? 326 VAL A CA 1 ATOM 2606 C C . VAL A 1 323 ? 23.726 34.743 -5.348 1.00 64.45 ? 326 VAL A C 1 ATOM 2607 O O . VAL A 1 323 ? 23.134 33.663 -5.200 1.00 63.19 ? 326 VAL A O 1 ATOM 2608 C CB . VAL A 1 323 ? 23.067 36.651 -3.897 1.00 60.22 ? 326 VAL A CB 1 ATOM 2609 C CG1 . VAL A 1 323 ? 24.499 36.572 -3.350 1.00 57.19 ? 326 VAL A CG1 1 ATOM 2610 C CG2 . VAL A 1 323 ? 22.636 38.096 -3.944 1.00 59.96 ? 326 VAL A CG2 1 ATOM 2611 N N . ALA A 1 324 ? 25.039 34.896 -5.555 1.00 67.37 ? 327 ALA A N 1 ATOM 2612 C CA . ALA A 1 324 ? 26.032 33.837 -5.620 1.00 68.23 ? 327 ALA A CA 1 ATOM 2613 C C . ALA A 1 324 ? 25.408 32.508 -5.257 1.00 70.20 ? 327 ALA A C 1 ATOM 2614 O O . ALA A 1 324 ? 24.623 31.954 -6.026 1.00 71.82 ? 327 ALA A O 1 ATOM 2615 C CB . ALA A 1 324 ? 27.217 34.169 -4.668 1.00 66.13 ? 327 ALA A CB 1 ATOM 2616 N N . ASP A 1 325 ? 25.731 32.002 -4.076 1.00 70.64 ? 328 ASP A N 1 ATOM 2617 C CA . ASP A 1 325 ? 25.188 30.720 -3.674 1.00 71.07 ? 328 ASP A CA 1 ATOM 2618 C C . ASP A 1 325 ? 24.121 30.813 -2.602 1.00 69.16 ? 328 ASP A C 1 ATOM 2619 O O . ASP A 1 325 ? 24.034 29.940 -1.743 1.00 68.66 ? 328 ASP A O 1 ATOM 2620 C CB . ASP A 1 325 ? 26.313 29.792 -3.198 1.00 75.26 ? 328 ASP A CB 1 ATOM 2621 C CG . ASP A 1 325 ? 27.054 29.124 -4.356 1.00 80.90 ? 328 ASP A CG 1 ATOM 2622 O OD1 . ASP A 1 325 ? 26.456 28.273 -5.069 1.00 80.52 ? 328 ASP A OD1 1 ATOM 2623 O OD2 . ASP A 1 325 ? 28.244 29.458 -4.555 1.00 85.12 ? 328 ASP A OD2 1 ATOM 2624 N N . ILE A 1 326 ? 23.307 31.862 -2.641 1.00 67.29 ? 329 ILE A N 1 ATOM 2625 C CA . ILE A 1 326 ? 22.247 31.991 -1.647 1.00 66.88 ? 329 ILE A CA 1 ATOM 2626 C C . ILE A 1 326 ? 20.922 31.820 -2.347 1.00 68.16 ? 329 ILE A C 1 ATOM 2627 O O . ILE A 1 326 ? 20.567 32.616 -3.228 1.00 68.05 ? 329 ILE A O 1 ATOM 2628 C CB . ILE A 1 326 ? 22.249 33.354 -0.960 1.00 65.01 ? 329 ILE A CB 1 ATOM 2629 C CG1 . ILE A 1 326 ? 23.636 33.649 -0.394 1.00 63.93 ? 329 ILE A CG1 1 ATOM 2630 C CG2 . ILE A 1 326 ? 21.215 33.352 0.153 1.00 65.36 ? 329 ILE A CG2 1 ATOM 2631 C CD1 . ILE A 1 326 ? 23.812 35.058 0.107 1.00 61.98 ? 329 ILE A CD1 1 ATOM 2632 N N . ASN A 1 327 ? 20.189 30.786 -1.950 1.00 70.18 ? 330 ASN A N 1 ATOM 2633 C CA . ASN A 1 327 ? 18.917 30.510 -2.584 1.00 74.32 ? 330 ASN A CA 1 ATOM 2634 C C . ASN A 1 327 ? 17.712 31.266 -2.019 1.00 74.67 ? 330 ASN A C 1 ATOM 2635 O O . ASN A 1 327 ? 16.763 30.671 -1.487 1.00 76.35 ? 330 ASN A O 1 ATOM 2636 C CB . ASN A 1 327 ? 18.626 29.011 -2.570 1.00 79.59 ? 330 ASN A CB 1 ATOM 2637 C CG . ASN A 1 327 ? 17.416 28.644 -3.438 1.00 85.66 ? 330 ASN A CG 1 ATOM 2638 O OD1 . ASN A 1 327 ? 16.832 27.560 -3.284 1.00 89.12 ? 330 ASN A OD1 1 ATOM 2639 N ND2 . ASN A 1 327 ? 17.040 29.546 -4.362 1.00 86.77 ? 330 ASN A ND2 1 ATOM 2640 N N . HIS A 1 328 ? 17.750 32.585 -2.131 1.00 72.94 ? 331 HIS A N 1 ATOM 2641 C CA . HIS A 1 328 ? 16.638 33.393 -1.676 1.00 68.76 ? 331 HIS A CA 1 ATOM 2642 C C . HIS A 1 328 ? 16.728 34.681 -2.462 1.00 67.01 ? 331 HIS A C 1 ATOM 2643 O O . HIS A 1 328 ? 17.346 35.651 -2.038 1.00 66.51 ? 331 HIS A O 1 ATOM 2644 C CB . HIS A 1 328 ? 16.689 33.656 -0.164 1.00 65.94 ? 331 HIS A CB 1 ATOM 2645 C CG . HIS A 1 328 ? 15.468 34.347 0.349 1.00 64.36 ? 331 HIS A CG 1 ATOM 2646 N ND1 . HIS A 1 328 ? 15.494 35.624 0.871 1.00 65.13 ? 331 HIS A ND1 1 ATOM 2647 C CD2 . HIS A 1 328 ? 14.165 33.984 0.317 1.00 63.08 ? 331 HIS A CD2 1 ATOM 2648 C CE1 . HIS A 1 328 ? 14.259 36.021 1.132 1.00 63.57 ? 331 HIS A CE1 1 ATOM 2649 N NE2 . HIS A 1 328 ? 13.433 35.044 0.803 1.00 64.03 ? 331 HIS A NE2 1 ATOM 2650 N N . PRO A 1 329 ? 16.150 34.678 -3.659 1.00 65.69 ? 332 PRO A N 1 ATOM 2651 C CA . PRO A 1 329 ? 16.138 35.837 -4.546 1.00 66.80 ? 332 PRO A CA 1 ATOM 2652 C C . PRO A 1 329 ? 15.326 37.012 -3.988 1.00 67.55 ? 332 PRO A C 1 ATOM 2653 O O . PRO A 1 329 ? 14.513 36.859 -3.074 1.00 69.10 ? 332 PRO A O 1 ATOM 2654 C CB . PRO A 1 329 ? 15.538 35.273 -5.825 1.00 65.82 ? 332 PRO A CB 1 ATOM 2655 C CG . PRO A 1 329 ? 14.656 34.175 -5.319 1.00 64.73 ? 332 PRO A CG 1 ATOM 2656 C CD . PRO A 1 329 ? 15.542 33.516 -4.316 1.00 63.88 ? 332 PRO A CD 1 ATOM 2657 N N . VAL A 1 330 ? 15.553 38.184 -4.565 1.00 67.07 ? 333 VAL A N 1 ATOM 2658 C CA . VAL A 1 330 ? 14.880 39.408 -4.159 1.00 65.02 ? 333 VAL A CA 1 ATOM 2659 C C . VAL A 1 330 ? 14.321 40.117 -5.396 1.00 64.89 ? 333 VAL A C 1 ATOM 2660 O O . VAL A 1 330 ? 14.914 40.047 -6.468 1.00 66.76 ? 333 VAL A O 1 ATOM 2661 C CB . VAL A 1 330 ? 15.883 40.311 -3.428 1.00 63.17 ? 333 VAL A CB 1 ATOM 2662 C CG1 . VAL A 1 330 ? 15.412 41.740 -3.433 1.00 63.15 ? 333 VAL A CG1 1 ATOM 2663 C CG2 . VAL A 1 330 ? 16.065 39.804 -2.009 1.00 61.64 ? 333 VAL A CG2 1 ATOM 2664 N N . THR A 1 331 ? 13.178 40.782 -5.249 1.00 64.08 ? 334 THR A N 1 ATOM 2665 C CA . THR A 1 331 ? 12.540 41.504 -6.347 1.00 63.74 ? 334 THR A CA 1 ATOM 2666 C C . THR A 1 331 ? 12.738 43.046 -6.208 1.00 65.07 ? 334 THR A C 1 ATOM 2667 O O . THR A 1 331 ? 13.227 43.507 -5.175 1.00 64.24 ? 334 THR A O 1 ATOM 2668 C CB . THR A 1 331 ? 11.039 41.099 -6.418 1.00 63.08 ? 334 THR A CB 1 ATOM 2669 O OG1 . THR A 1 331 ? 10.308 42.096 -7.123 1.00 69.67 ? 334 THR A OG1 1 ATOM 2670 C CG2 . THR A 1 331 ? 10.431 40.941 -5.034 1.00 64.23 ? 334 THR A CG2 1 ATOM 2671 N N . THR A 1 332 ? 12.408 43.829 -7.249 1.00 67.63 ? 335 THR A N 1 ATOM 2672 C CA . THR A 1 332 ? 12.560 45.313 -7.233 1.00 69.06 ? 335 THR A CA 1 ATOM 2673 C C . THR A 1 332 ? 11.232 46.056 -7.141 1.00 69.43 ? 335 THR A C 1 ATOM 2674 O O . THR A 1 332 ? 10.201 45.539 -7.582 1.00 68.90 ? 335 THR A O 1 ATOM 2675 C CB . THR A 1 332 ? 13.227 45.870 -8.517 1.00 70.01 ? 335 THR A CB 1 ATOM 2676 O OG1 . THR A 1 332 ? 12.509 45.401 -9.669 1.00 71.43 ? 335 THR A OG1 1 ATOM 2677 C CG2 . THR A 1 332 ? 14.688 45.470 -8.598 1.00 69.57 ? 335 THR A CG2 1 ATOM 2678 N N . TYR A 1 333 ? 11.239 47.276 -6.605 1.00 70.24 ? 336 TYR A N 1 ATOM 2679 C CA . TYR A 1 333 ? 9.969 47.989 -6.521 1.00 73.62 ? 336 TYR A CA 1 ATOM 2680 C C . TYR A 1 333 ? 9.625 48.734 -7.823 1.00 76.09 ? 336 TYR A C 1 ATOM 2681 O O . TYR A 1 333 ? 10.224 48.477 -8.869 1.00 76.73 ? 336 TYR A O 1 ATOM 2682 C CB . TYR A 1 333 ? 9.931 48.961 -5.324 1.00 70.90 ? 336 TYR A CB 1 ATOM 2683 C CG . TYR A 1 333 ? 8.494 49.249 -4.887 1.00 70.30 ? 336 TYR A CG 1 ATOM 2684 C CD1 . TYR A 1 333 ? 7.490 48.276 -5.046 1.00 70.50 ? 336 TYR A CD1 1 ATOM 2685 C CD2 . TYR A 1 333 ? 8.118 50.490 -4.369 1.00 68.87 ? 336 TYR A CD2 1 ATOM 2686 C CE1 . TYR A 1 333 ? 6.134 48.531 -4.704 1.00 70.00 ? 336 TYR A CE1 1 ATOM 2687 C CE2 . TYR A 1 333 ? 6.762 50.762 -4.021 1.00 69.60 ? 336 TYR A CE2 1 ATOM 2688 C CZ . TYR A 1 333 ? 5.773 49.774 -4.196 1.00 69.98 ? 336 TYR A CZ 1 ATOM 2689 O OH . TYR A 1 333 ? 4.437 50.013 -3.894 1.00 65.84 ? 336 TYR A OH 1 ATOM 2690 N N . LYS A 1 334 ? 8.651 49.645 -7.741 1.00 79.16 ? 337 LYS A N 1 ATOM 2691 C CA . LYS A 1 334 ? 8.161 50.457 -8.869 1.00 79.86 ? 337 LYS A CA 1 ATOM 2692 C C . LYS A 1 334 ? 9.223 51.300 -9.614 1.00 80.14 ? 337 LYS A C 1 ATOM 2693 O O . LYS A 1 334 ? 9.099 51.528 -10.827 1.00 79.36 ? 337 LYS A O 1 ATOM 2694 C CB . LYS A 1 334 ? 6.996 51.354 -8.380 1.00 80.69 ? 337 LYS A CB 1 ATOM 2695 C CG . LYS A 1 334 ? 5.630 50.613 -8.249 1.00 83.30 ? 337 LYS A CG 1 ATOM 2696 C CD . LYS A 1 334 ? 4.720 51.075 -7.074 1.00 84.02 ? 337 LYS A CD 1 ATOM 2697 C CE . LYS A 1 334 ? 3.932 52.356 -7.343 1.00 83.96 ? 337 LYS A CE 1 ATOM 2698 N NZ . LYS A 1 334 ? 3.131 52.785 -6.151 1.00 84.30 ? 337 LYS A NZ 1 ATOM 2699 N N . ASP A 1 335 ? 10.256 51.755 -8.899 1.00 79.79 ? 338 ASP A N 1 ATOM 2700 C CA . ASP A 1 335 ? 11.338 52.543 -9.504 1.00 78.47 ? 338 ASP A CA 1 ATOM 2701 C C . ASP A 1 335 ? 12.510 51.625 -9.831 1.00 75.98 ? 338 ASP A C 1 ATOM 2702 O O . ASP A 1 335 ? 13.635 52.091 -10.052 1.00 74.02 ? 338 ASP A O 1 ATOM 2703 C CB . ASP A 1 335 ? 11.853 53.625 -8.545 1.00 81.72 ? 338 ASP A CB 1 ATOM 2704 C CG . ASP A 1 335 ? 10.766 54.583 -8.083 1.00 84.47 ? 338 ASP A CG 1 ATOM 2705 O OD1 . ASP A 1 335 ? 10.052 55.153 -8.947 1.00 86.32 ? 338 ASP A OD1 1 ATOM 2706 O OD2 . ASP A 1 335 ? 10.640 54.774 -6.848 1.00 83.84 ? 338 ASP A OD2 1 ATOM 2707 N N . GLY A 1 336 ? 12.245 50.321 -9.830 1.00 73.87 ? 339 GLY A N 1 ATOM 2708 C CA . GLY A 1 336 ? 13.280 49.350 -10.117 1.00 71.88 ? 339 GLY A CA 1 ATOM 2709 C C . GLY A 1 336 ? 14.357 49.310 -9.050 1.00 70.67 ? 339 GLY A C 1 ATOM 2710 O O . GLY A 1 336 ? 15.406 48.712 -9.255 1.00 71.13 ? 339 GLY A O 1 ATOM 2711 N N . ASP A 1 337 ? 14.117 49.954 -7.913 1.00 69.07 ? 340 ASP A N 1 ATOM 2712 C CA . ASP A 1 337 ? 15.104 49.936 -6.841 1.00 65.54 ? 340 ASP A CA 1 ATOM 2713 C C . ASP A 1 337 ? 15.016 48.600 -6.117 1.00 64.65 ? 340 ASP A C 1 ATOM 2714 O O . ASP A 1 337 ? 13.939 47.984 -6.062 1.00 63.59 ? 340 ASP A O 1 ATOM 2715 C CB . ASP A 1 337 ? 14.875 51.094 -5.860 1.00 65.08 ? 340 ASP A CB 1 ATOM 2716 C CG . ASP A 1 337 ? 13.397 51.314 -5.520 1.00 66.27 ? 340 ASP A CG 1 ATOM 2717 O OD1 . ASP A 1 337 ? 12.510 50.598 -6.046 1.00 63.73 ? 340 ASP A OD1 1 ATOM 2718 O OD2 . ASP A 1 337 ? 13.128 52.228 -4.711 1.00 66.66 ? 340 ASP A OD2 1 ATOM 2719 N N . TYR A 1 338 ? 16.158 48.142 -5.601 1.00 62.36 ? 341 TYR A N 1 ATOM 2720 C CA . TYR A 1 338 ? 16.234 46.879 -4.864 1.00 61.59 ? 341 TYR A CA 1 ATOM 2721 C C . TYR A 1 338 ? 17.188 47.034 -3.690 1.00 61.11 ? 341 TYR A C 1 ATOM 2722 O O . TYR A 1 338 ? 18.069 47.905 -3.692 1.00 60.96 ? 341 TYR A O 1 ATOM 2723 C CB . TYR A 1 338 ? 16.743 45.719 -5.751 1.00 61.32 ? 341 TYR A CB 1 ATOM 2724 C CG . TYR A 1 338 ? 18.255 45.706 -5.982 1.00 60.87 ? 341 TYR A CG 1 ATOM 2725 C CD1 . TYR A 1 338 ? 19.124 45.089 -5.066 1.00 61.40 ? 341 TYR A CD1 1 ATOM 2726 C CD2 . TYR A 1 338 ? 18.822 46.366 -7.077 1.00 60.34 ? 341 TYR A CD2 1 ATOM 2727 C CE1 . TYR A 1 338 ? 20.523 45.143 -5.232 1.00 59.53 ? 341 TYR A CE1 1 ATOM 2728 C CE2 . TYR A 1 338 ? 20.215 46.421 -7.252 1.00 58.75 ? 341 TYR A CE2 1 ATOM 2729 C CZ . TYR A 1 338 ? 21.056 45.815 -6.326 1.00 58.84 ? 341 TYR A CZ 1 ATOM 2730 O OH . TYR A 1 338 ? 22.422 45.931 -6.481 1.00 57.27 ? 341 TYR A OH 1 ATOM 2731 N N . TRP A 1 339 ? 17.010 46.182 -2.688 1.00 59.81 ? 342 TRP A N 1 ATOM 2732 C CA . TRP A 1 339 ? 17.874 46.198 -1.515 1.00 57.88 ? 342 TRP A CA 1 ATOM 2733 C C . TRP A 1 339 ? 18.085 44.752 -1.170 1.00 57.24 ? 342 TRP A C 1 ATOM 2734 O O . TRP A 1 339 ? 17.116 43.994 -1.090 1.00 57.99 ? 342 TRP A O 1 ATOM 2735 C CB . TRP A 1 339 ? 17.195 46.884 -0.342 1.00 56.93 ? 342 TRP A CB 1 ATOM 2736 C CG . TRP A 1 339 ? 16.742 48.219 -0.662 1.00 53.65 ? 342 TRP A CG 1 ATOM 2737 C CD1 . TRP A 1 339 ? 17.405 49.391 -0.431 1.00 53.40 ? 342 TRP A CD1 1 ATOM 2738 C CD2 . TRP A 1 339 ? 15.517 48.557 -1.313 1.00 52.09 ? 342 TRP A CD2 1 ATOM 2739 N NE1 . TRP A 1 339 ? 16.658 50.446 -0.904 1.00 54.24 ? 342 TRP A NE1 1 ATOM 2740 C CE2 . TRP A 1 339 ? 15.492 49.962 -1.451 1.00 52.00 ? 342 TRP A CE2 1 ATOM 2741 C CE3 . TRP A 1 339 ? 14.430 47.808 -1.794 1.00 52.38 ? 342 TRP A CE3 1 ATOM 2742 C CZ2 . TRP A 1 339 ? 14.416 50.643 -2.050 1.00 51.54 ? 342 TRP A CZ2 1 ATOM 2743 C CZ3 . TRP A 1 339 ? 13.357 48.484 -2.390 1.00 51.54 ? 342 TRP A CZ3 1 ATOM 2744 C CH2 . TRP A 1 339 ? 13.362 49.889 -2.511 1.00 50.77 ? 342 TRP A CH2 1 ATOM 2745 N N . ARG A 1 340 ? 19.342 44.381 -0.957 1.00 56.07 ? 343 ARG A N 1 ATOM 2746 C CA . ARG A 1 340 ? 19.695 43.008 -0.638 1.00 55.76 ? 343 ARG A CA 1 ATOM 2747 C C . ARG A 1 340 ? 20.680 42.973 0.525 1.00 54.18 ? 343 ARG A C 1 ATOM 2748 O O . ARG A 1 340 ? 21.798 43.468 0.429 1.00 52.58 ? 343 ARG A O 1 ATOM 2749 C CB . ARG A 1 340 ? 20.300 42.349 -1.878 1.00 57.65 ? 343 ARG A CB 1 ATOM 2750 C CG . ARG A 1 340 ? 20.898 40.970 -1.648 1.00 59.22 ? 343 ARG A CG 1 ATOM 2751 C CD . ARG A 1 340 ? 19.843 39.899 -1.484 1.00 57.88 ? 343 ARG A CD 1 ATOM 2752 N NE . ARG A 1 340 ? 20.149 39.106 -0.305 1.00 59.44 ? 343 ARG A NE 1 ATOM 2753 C CZ . ARG A 1 340 ? 19.713 37.872 -0.108 1.00 60.98 ? 343 ARG A CZ 1 ATOM 2754 N NH1 . ARG A 1 340 ? 18.950 37.287 -1.021 1.00 61.51 ? 343 ARG A NH1 1 ATOM 2755 N NH2 . ARG A 1 340 ? 20.037 37.233 1.004 1.00 60.61 ? 343 ARG A NH2 1 ATOM 2756 N N . LEU A 1 341 ? 20.261 42.377 1.628 1.00 53.34 ? 344 LEU A N 1 ATOM 2757 C CA . LEU A 1 341 ? 21.110 42.324 2.796 1.00 53.82 ? 344 LEU A CA 1 ATOM 2758 C C . LEU A 1 341 ? 22.100 41.197 2.685 1.00 53.99 ? 344 LEU A C 1 ATOM 2759 O O . LEU A 1 341 ? 21.744 40.077 2.316 1.00 53.10 ? 344 LEU A O 1 ATOM 2760 C CB . LEU A 1 341 ? 20.242 42.176 4.044 1.00 56.62 ? 344 LEU A CB 1 ATOM 2761 C CG . LEU A 1 341 ? 19.287 43.368 4.239 1.00 56.49 ? 344 LEU A CG 1 ATOM 2762 C CD1 . LEU A 1 341 ? 18.225 43.001 5.237 1.00 56.57 ? 344 LEU A CD1 1 ATOM 2763 C CD2 . LEU A 1 341 ? 20.069 44.622 4.686 1.00 55.28 ? 344 LEU A CD2 1 ATOM 2764 N N . LEU A 1 342 ? 23.351 41.513 3.002 1.00 54.58 ? 345 LEU A N 1 ATOM 2765 C CA . LEU A 1 342 ? 24.428 40.548 2.927 1.00 55.82 ? 345 LEU A CA 1 ATOM 2766 C C . LEU A 1 342 ? 25.502 40.906 3.896 1.00 56.61 ? 345 LEU A C 1 ATOM 2767 O O . LEU A 1 342 ? 25.564 42.020 4.419 1.00 55.68 ? 345 LEU A O 1 ATOM 2768 C CB . LEU A 1 342 ? 25.058 40.525 1.537 1.00 57.87 ? 345 LEU A CB 1 ATOM 2769 C CG . LEU A 1 342 ? 24.154 40.169 0.358 1.00 59.89 ? 345 LEU A CG 1 ATOM 2770 C CD1 . LEU A 1 342 ? 24.910 40.342 -0.938 1.00 58.79 ? 345 LEU A CD1 1 ATOM 2771 C CD2 . LEU A 1 342 ? 23.669 38.746 0.506 1.00 62.18 ? 345 LEU A CD2 1 ATOM 2772 N N . VAL A 1 343 ? 26.383 39.943 4.082 1.00 58.97 ? 346 VAL A N 1 ATOM 2773 C CA . VAL A 1 343 ? 27.502 40.070 4.983 1.00 62.93 ? 346 VAL A CA 1 ATOM 2774 C C . VAL A 1 343 ? 28.796 40.405 4.235 1.00 66.08 ? 346 VAL A C 1 ATOM 2775 O O . VAL A 1 343 ? 28.911 40.196 3.026 1.00 67.91 ? 346 VAL A O 1 ATOM 2776 C CB . VAL A 1 343 ? 27.694 38.753 5.748 1.00 61.63 ? 346 VAL A CB 1 ATOM 2777 C CG1 . VAL A 1 343 ? 28.842 38.879 6.742 1.00 63.75 ? 346 VAL A CG1 1 ATOM 2778 C CG2 . VAL A 1 343 ? 26.402 38.387 6.446 1.00 60.58 ? 346 VAL A CG2 1 ATOM 2779 N N . GLN A 1 344 ? 29.765 40.936 4.966 1.00 68.22 ? 347 GLN A N 1 ATOM 2780 C CA . GLN A 1 344 ? 31.048 41.262 4.386 1.00 70.27 ? 347 GLN A CA 1 ATOM 2781 C C . GLN A 1 344 ? 31.553 39.991 3.685 1.00 71.51 ? 347 GLN A C 1 ATOM 2782 O O . GLN A 1 344 ? 31.677 38.936 4.316 1.00 73.38 ? 347 GLN A O 1 ATOM 2783 C CB . GLN A 1 344 ? 31.999 41.669 5.505 1.00 73.26 ? 347 GLN A CB 1 ATOM 2784 C CG . GLN A 1 344 ? 33.394 42.090 5.066 1.00 79.83 ? 347 GLN A CG 1 ATOM 2785 C CD . GLN A 1 344 ? 34.472 41.645 6.061 1.00 84.95 ? 347 GLN A CD 1 ATOM 2786 O OE1 . GLN A 1 344 ? 34.790 40.450 6.141 1.00 89.33 ? 347 GLN A OE1 1 ATOM 2787 N NE2 . GLN A 1 344 ? 35.028 42.595 6.829 1.00 84.03 ? 347 GLN A NE2 1 ATOM 2788 N N . GLY A 1 345 ? 31.825 40.104 2.384 1.00 71.75 ? 348 GLY A N 1 ATOM 2789 C CA . GLY A 1 345 ? 32.318 38.990 1.581 1.00 70.66 ? 348 GLY A CA 1 ATOM 2790 C C . GLY A 1 345 ? 32.114 39.325 0.109 1.00 70.65 ? 348 GLY A C 1 ATOM 2791 O O . GLY A 1 345 ? 31.473 40.329 -0.190 1.00 70.96 ? 348 GLY A O 1 ATOM 2792 N N . THR A 1 346 ? 32.628 38.507 -0.811 1.00 70.87 ? 349 THR A N 1 ATOM 2793 C CA . THR A 1 346 ? 32.464 38.780 -2.250 1.00 70.53 ? 349 THR A CA 1 ATOM 2794 C C . THR A 1 346 ? 31.357 37.931 -2.902 1.00 69.66 ? 349 THR A C 1 ATOM 2795 O O . THR A 1 346 ? 31.364 36.718 -2.757 1.00 71.84 ? 349 THR A O 1 ATOM 2796 C CB . THR A 1 346 ? 33.777 38.519 -3.002 1.00 70.97 ? 349 THR A CB 1 ATOM 2797 O OG1 . THR A 1 346 ? 34.823 39.333 -2.456 1.00 71.41 ? 349 THR A OG1 1 ATOM 2798 C CG2 . THR A 1 346 ? 33.610 38.852 -4.460 1.00 71.17 ? 349 THR A CG2 1 ATOM 2799 N N . TYR A 1 347 ? 30.424 38.545 -3.631 1.00 67.97 ? 350 TYR A N 1 ATOM 2800 C CA . TYR A 1 347 ? 29.330 37.782 -4.247 1.00 67.05 ? 350 TYR A CA 1 ATOM 2801 C C . TYR A 1 347 ? 29.203 37.998 -5.732 1.00 68.01 ? 350 TYR A C 1 ATOM 2802 O O . TYR A 1 347 ? 29.872 38.854 -6.294 1.00 69.66 ? 350 TYR A O 1 ATOM 2803 C CB . TYR A 1 347 ? 27.983 38.161 -3.632 1.00 66.94 ? 350 TYR A CB 1 ATOM 2804 C CG . TYR A 1 347 ? 27.955 38.093 -2.137 1.00 66.24 ? 350 TYR A CG 1 ATOM 2805 C CD1 . TYR A 1 347 ? 27.624 36.907 -1.493 1.00 66.31 ? 350 TYR A CD1 1 ATOM 2806 C CD2 . TYR A 1 347 ? 28.305 39.198 -1.358 1.00 66.39 ? 350 TYR A CD2 1 ATOM 2807 C CE1 . TYR A 1 347 ? 27.647 36.813 -0.102 1.00 67.46 ? 350 TYR A CE1 1 ATOM 2808 C CE2 . TYR A 1 347 ? 28.326 39.116 0.037 1.00 67.52 ? 350 TYR A CE2 1 ATOM 2809 C CZ . TYR A 1 347 ? 27.996 37.915 0.657 1.00 66.57 ? 350 TYR A CZ 1 ATOM 2810 O OH . TYR A 1 347 ? 28.012 37.790 2.027 1.00 66.51 ? 350 TYR A OH 1 ATOM 2811 N N . LYS A 1 348 ? 28.310 37.238 -6.361 1.00 67.55 ? 351 LYS A N 1 ATOM 2812 C CA . LYS A 1 348 ? 28.080 37.378 -7.792 1.00 66.59 ? 351 LYS A CA 1 ATOM 2813 C C . LYS A 1 348 ? 26.600 37.517 -8.084 1.00 64.64 ? 351 LYS A C 1 ATOM 2814 O O . LYS A 1 348 ? 25.886 36.550 -8.353 1.00 64.06 ? 351 LYS A O 1 ATOM 2815 C CB . LYS A 1 348 ? 28.663 36.190 -8.551 1.00 70.61 ? 351 LYS A CB 1 ATOM 2816 C CG . LYS A 1 348 ? 30.185 36.077 -8.420 1.00 75.22 ? 351 LYS A CG 1 ATOM 2817 C CD . LYS A 1 348 ? 30.833 35.539 -9.697 1.00 80.17 ? 351 LYS A CD 1 ATOM 2818 C CE . LYS A 1 348 ? 30.228 34.194 -10.108 1.00 84.97 ? 351 LYS A CE 1 ATOM 2819 N NZ . LYS A 1 348 ? 30.778 33.684 -11.405 1.00 89.85 ? 351 LYS A NZ 1 ATOM 2820 N N . VAL A 1 349 ? 26.155 38.758 -8.054 1.00 62.78 ? 352 VAL A N 1 ATOM 2821 C CA . VAL A 1 349 ? 24.758 39.075 -8.265 1.00 60.81 ? 352 VAL A CA 1 ATOM 2822 C C . VAL A 1 349 ? 24.287 39.104 -9.717 1.00 60.28 ? 352 VAL A C 1 ATOM 2823 O O . VAL A 1 349 ? 24.978 39.589 -10.601 1.00 60.56 ? 352 VAL A O 1 ATOM 2824 C CB . VAL A 1 349 ? 24.467 40.404 -7.616 1.00 59.45 ? 352 VAL A CB 1 ATOM 2825 C CG1 . VAL A 1 349 ? 22.985 40.519 -7.326 1.00 58.84 ? 352 VAL A CG1 1 ATOM 2826 C CG2 . VAL A 1 349 ? 25.328 40.538 -6.356 1.00 55.99 ? 352 VAL A CG2 1 ATOM 2827 N N . THR A 1 350 ? 23.085 38.600 -9.944 1.00 59.22 ? 353 THR A N 1 ATOM 2828 C CA . THR A 1 350 ? 22.526 38.543 -11.279 1.00 59.13 ? 353 THR A CA 1 ATOM 2829 C C . THR A 1 350 ? 21.151 39.152 -11.324 1.00 61.79 ? 353 THR A C 1 ATOM 2830 O O . THR A 1 350 ? 20.230 38.689 -10.646 1.00 60.99 ? 353 THR A O 1 ATOM 2831 C CB . THR A 1 350 ? 22.377 37.085 -11.777 1.00 57.43 ? 353 THR A CB 1 ATOM 2832 O OG1 . THR A 1 350 ? 23.670 36.510 -11.980 1.00 57.13 ? 353 THR A OG1 1 ATOM 2833 C CG2 . THR A 1 350 ? 21.569 37.031 -13.074 1.00 55.05 ? 353 THR A CG2 1 ATOM 2834 N N . ALA A 1 351 ? 21.011 40.179 -12.151 1.00 64.30 ? 354 ALA A N 1 ATOM 2835 C CA . ALA A 1 351 ? 19.726 40.827 -12.321 1.00 66.75 ? 354 ALA A CA 1 ATOM 2836 C C . ALA A 1 351 ? 18.960 40.116 -13.450 1.00 69.60 ? 354 ALA A C 1 ATOM 2837 O O . ALA A 1 351 ? 19.287 40.249 -14.625 1.00 72.30 ? 354 ALA A O 1 ATOM 2838 C CB . ALA A 1 351 ? 19.928 42.290 -12.645 1.00 64.41 ? 354 ALA A CB 1 ATOM 2839 N N . SER A 1 352 ? 17.956 39.337 -13.073 1.00 71.83 ? 355 SER A N 1 ATOM 2840 C CA . SER A 1 352 ? 17.119 38.604 -14.015 1.00 73.12 ? 355 SER A CA 1 ATOM 2841 C C . SER A 1 352 ? 15.965 39.544 -14.301 1.00 75.20 ? 355 SER A C 1 ATOM 2842 O O . SER A 1 352 ? 15.799 40.520 -13.586 1.00 76.49 ? 355 SER A O 1 ATOM 2843 C CB . SER A 1 352 ? 16.593 37.345 -13.334 1.00 73.30 ? 355 SER A CB 1 ATOM 2844 O OG . SER A 1 352 ? 17.404 37.037 -12.200 1.00 74.80 ? 355 SER A OG 1 ATOM 2845 N N . ALA A 1 353 ? 15.165 39.266 -15.324 1.00 77.68 ? 356 ALA A N 1 ATOM 2846 C CA . ALA A 1 353 ? 14.025 40.130 -15.656 1.00 80.19 ? 356 ALA A CA 1 ATOM 2847 C C . ALA A 1 353 ? 13.307 39.648 -16.901 1.00 82.60 ? 356 ALA A C 1 ATOM 2848 O O . ALA A 1 353 ? 13.929 39.414 -17.940 1.00 83.74 ? 356 ALA A O 1 ATOM 2849 C CB . ALA A 1 353 ? 14.482 41.566 -15.862 1.00 78.86 ? 356 ALA A CB 1 ATOM 2850 N N . ARG A 1 354 ? 11.991 39.520 -16.791 1.00 84.67 ? 357 ARG A N 1 ATOM 2851 C CA . ARG A 1 354 ? 11.158 39.052 -17.892 1.00 86.69 ? 357 ARG A CA 1 ATOM 2852 C C . ARG A 1 354 ? 11.142 40.000 -19.097 1.00 87.99 ? 357 ARG A C 1 ATOM 2853 O O . ARG A 1 354 ? 10.752 41.164 -18.983 1.00 89.11 ? 357 ARG A O 1 ATOM 2854 C CB . ARG A 1 354 ? 9.738 38.838 -17.388 1.00 87.27 ? 357 ARG A CB 1 ATOM 2855 C CG . ARG A 1 354 ? 8.810 38.224 -18.391 1.00 89.32 ? 357 ARG A CG 1 ATOM 2856 C CD . ARG A 1 354 ? 7.400 38.178 -17.832 1.00 92.30 ? 357 ARG A CD 1 ATOM 2857 N NE . ARG A 1 354 ? 6.484 37.468 -18.726 1.00 97.22 ? 357 ARG A NE 1 ATOM 2858 C CZ . ARG A 1 354 ? 5.152 37.549 -18.671 1.00 97.92 ? 357 ARG A CZ 1 ATOM 2859 N NH1 . ARG A 1 354 ? 4.562 38.318 -17.757 1.00 97.92 ? 357 ARG A NH1 1 ATOM 2860 N NH2 . ARG A 1 354 ? 4.405 36.865 -19.537 1.00 97.92 ? 357 ARG A NH2 1 ATOM 2861 N N . GLY A 1 355 ? 11.563 39.486 -20.251 1.00 88.03 ? 358 GLY A N 1 ATOM 2862 C CA . GLY A 1 355 ? 11.594 40.292 -21.458 1.00 86.42 ? 358 GLY A CA 1 ATOM 2863 C C . GLY A 1 355 ? 12.918 41.012 -21.596 1.00 84.94 ? 358 GLY A C 1 ATOM 2864 O O . GLY A 1 355 ? 13.082 41.877 -22.458 1.00 84.80 ? 358 GLY A O 1 ATOM 2865 N N . TYR A 1 356 ? 13.863 40.656 -20.733 1.00 83.33 ? 359 TYR A N 1 ATOM 2866 C CA . TYR A 1 356 ? 15.178 41.272 -20.749 1.00 82.64 ? 359 TYR A CA 1 ATOM 2867 C C . TYR A 1 356 ? 16.270 40.236 -20.677 1.00 82.41 ? 359 TYR A C 1 ATOM 2868 O O . TYR A 1 356 ? 16.024 39.056 -20.412 1.00 82.49 ? 359 TYR A O 1 ATOM 2869 C CB . TYR A 1 356 ? 15.354 42.233 -19.571 1.00 82.21 ? 359 TYR A CB 1 ATOM 2870 C CG . TYR A 1 356 ? 14.556 43.506 -19.676 1.00 83.15 ? 359 TYR A CG 1 ATOM 2871 C CD1 . TYR A 1 356 ? 13.159 43.476 -19.710 1.00 83.42 ? 359 TYR A CD1 1 ATOM 2872 C CD2 . TYR A 1 356 ? 15.197 44.746 -19.746 1.00 82.56 ? 359 TYR A CD2 1 ATOM 2873 C CE1 . TYR A 1 356 ? 12.416 44.649 -19.814 1.00 84.75 ? 359 TYR A CE1 1 ATOM 2874 C CE2 . TYR A 1 356 ? 14.465 45.927 -19.848 1.00 83.80 ? 359 TYR A CE2 1 ATOM 2875 C CZ . TYR A 1 356 ? 13.075 45.869 -19.881 1.00 85.51 ? 359 TYR A CZ 1 ATOM 2876 O OH . TYR A 1 356 ? 12.341 47.025 -19.978 1.00 87.34 ? 359 TYR A OH 1 ATOM 2877 N N . ASP A 1 357 ? 17.492 40.701 -20.900 1.00 82.76 ? 360 ASP A N 1 ATOM 2878 C CA . ASP A 1 357 ? 18.647 39.828 -20.863 1.00 83.70 ? 360 ASP A CA 1 ATOM 2879 C C . ASP A 1 357 ? 19.414 40.072 -19.579 1.00 81.88 ? 360 ASP A C 1 ATOM 2880 O O . ASP A 1 357 ? 19.845 41.197 -19.298 1.00 82.07 ? 360 ASP A O 1 ATOM 2881 C CB . ASP A 1 357 ? 19.558 40.074 -22.074 1.00 87.38 ? 360 ASP A CB 1 ATOM 2882 C CG . ASP A 1 357 ? 18.855 39.807 -23.411 1.00 89.92 ? 360 ASP A CG 1 ATOM 2883 O OD1 . ASP A 1 357 ? 17.754 39.198 -23.405 1.00 89.96 ? 360 ASP A OD1 1 ATOM 2884 O OD2 . ASP A 1 357 ? 19.414 40.202 -24.467 1.00 90.40 ? 360 ASP A OD2 1 ATOM 2885 N N . PRO A 1 358 ? 19.594 39.007 -18.783 1.00 79.60 ? 361 PRO A N 1 ATOM 2886 C CA . PRO A 1 358 ? 20.296 39.005 -17.498 1.00 77.64 ? 361 PRO A CA 1 ATOM 2887 C C . PRO A 1 358 ? 21.727 39.510 -17.528 1.00 75.50 ? 361 PRO A C 1 ATOM 2888 O O . PRO A 1 358 ? 22.446 39.308 -18.493 1.00 76.86 ? 361 PRO A O 1 ATOM 2889 C CB . PRO A 1 358 ? 20.209 37.542 -17.062 1.00 77.92 ? 361 PRO A CB 1 ATOM 2890 C CG . PRO A 1 358 ? 20.136 36.805 -18.364 1.00 78.53 ? 361 PRO A CG 1 ATOM 2891 C CD . PRO A 1 358 ? 19.162 37.645 -19.138 1.00 78.65 ? 361 PRO A CD 1 ATOM 2892 N N . VAL A 1 359 ? 22.121 40.176 -16.453 1.00 73.53 ? 362 VAL A N 1 ATOM 2893 C CA . VAL A 1 359 ? 23.468 40.706 -16.295 1.00 71.20 ? 362 VAL A CA 1 ATOM 2894 C C . VAL A 1 359 ? 23.977 40.149 -14.981 1.00 70.81 ? 362 VAL A C 1 ATOM 2895 O O . VAL A 1 359 ? 23.200 39.902 -14.057 1.00 73.02 ? 362 VAL A O 1 ATOM 2896 C CB . VAL A 1 359 ? 23.471 42.244 -16.188 1.00 69.90 ? 362 VAL A CB 1 ATOM 2897 C CG1 . VAL A 1 359 ? 24.863 42.753 -15.830 1.00 65.26 ? 362 VAL A CG1 1 ATOM 2898 C CG2 . VAL A 1 359 ? 22.992 42.844 -17.485 1.00 70.41 ? 362 VAL A CG2 1 ATOM 2899 N N . THR A 1 360 ? 25.277 39.957 -14.876 1.00 68.20 ? 363 THR A N 1 ATOM 2900 C CA . THR A 1 360 ? 25.806 39.426 -13.645 1.00 66.35 ? 363 THR A CA 1 ATOM 2901 C C . THR A 1 360 ? 27.050 40.189 -13.276 1.00 67.86 ? 363 THR A C 1 ATOM 2902 O O . THR A 1 360 ? 28.024 40.151 -14.003 1.00 71.78 ? 363 THR A O 1 ATOM 2903 C CB . THR A 1 360 ? 26.166 37.949 -13.805 1.00 63.76 ? 363 THR A CB 1 ATOM 2904 O OG1 . THR A 1 360 ? 25.037 37.243 -14.331 1.00 61.42 ? 363 THR A OG1 1 ATOM 2905 C CG2 . THR A 1 360 ? 26.560 37.351 -12.464 1.00 61.66 ? 363 THR A CG2 1 ATOM 2906 N N . LYS A 1 361 ? 27.040 40.897 -12.161 1.00 68.05 ? 364 LYS A N 1 ATOM 2907 C CA . LYS A 1 361 ? 28.244 41.610 -11.793 1.00 68.40 ? 364 LYS A CA 1 ATOM 2908 C C . LYS A 1 361 ? 28.811 40.975 -10.547 1.00 67.91 ? 364 LYS A C 1 ATOM 2909 O O . LYS A 1 361 ? 28.086 40.356 -9.770 1.00 68.79 ? 364 LYS A O 1 ATOM 2910 C CB . LYS A 1 361 ? 27.958 43.087 -11.506 1.00 69.33 ? 364 LYS A CB 1 ATOM 2911 C CG . LYS A 1 361 ? 27.159 43.857 -12.567 1.00 71.11 ? 364 LYS A CG 1 ATOM 2912 C CD . LYS A 1 361 ? 27.247 45.386 -12.314 1.00 73.75 ? 364 LYS A CD 1 ATOM 2913 C CE . LYS A 1 361 ? 26.432 46.230 -13.319 1.00 76.20 ? 364 LYS A CE 1 ATOM 2914 N NZ . LYS A 1 361 ? 26.658 47.716 -13.207 1.00 76.30 ? 364 LYS A NZ 1 ATOM 2915 N N . THR A 1 362 ? 30.116 41.103 -10.368 1.00 67.02 ? 365 THR A N 1 ATOM 2916 C CA . THR A 1 362 ? 30.748 40.587 -9.170 1.00 66.50 ? 365 THR A CA 1 ATOM 2917 C C . THR A 1 362 ? 30.753 41.784 -8.243 1.00 67.69 ? 365 THR A C 1 ATOM 2918 O O . THR A 1 362 ? 31.236 42.855 -8.612 1.00 67.81 ? 365 THR A O 1 ATOM 2919 C CB . THR A 1 362 ? 32.211 40.145 -9.404 1.00 66.25 ? 365 THR A CB 1 ATOM 2920 O OG1 . THR A 1 362 ? 32.246 38.766 -9.798 1.00 66.02 ? 365 THR A OG1 1 ATOM 2921 C CG2 . THR A 1 362 ? 33.039 40.340 -8.135 1.00 62.75 ? 365 THR A CG2 1 ATOM 2922 N N . VAL A 1 363 ? 30.201 41.613 -7.049 1.00 68.49 ? 366 VAL A N 1 ATOM 2923 C CA . VAL A 1 363 ? 30.161 42.710 -6.099 1.00 68.76 ? 366 VAL A CA 1 ATOM 2924 C C . VAL A 1 363 ? 30.955 42.397 -4.861 1.00 69.46 ? 366 VAL A C 1 ATOM 2925 O O . VAL A 1 363 ? 31.141 41.236 -4.498 1.00 67.54 ? 366 VAL A O 1 ATOM 2926 C CB . VAL A 1 363 ? 28.749 43.017 -5.638 1.00 68.73 ? 366 VAL A CB 1 ATOM 2927 C CG1 . VAL A 1 363 ? 28.728 44.408 -5.024 1.00 68.91 ? 366 VAL A CG1 1 ATOM 2928 C CG2 . VAL A 1 363 ? 27.766 42.878 -6.799 1.00 68.71 ? 366 VAL A CG2 1 ATOM 2929 N N . GLU A 1 364 ? 31.414 43.444 -4.199 1.00 72.20 ? 367 GLU A N 1 ATOM 2930 C CA . GLU A 1 364 ? 32.175 43.241 -2.996 1.00 76.72 ? 367 GLU A CA 1 ATOM 2931 C C . GLU A 1 364 ? 31.593 44.029 -1.816 1.00 78.88 ? 367 GLU A C 1 ATOM 2932 O O . GLU A 1 364 ? 31.680 45.258 -1.760 1.00 79.75 ? 367 GLU A O 1 ATOM 2933 C CB . GLU A 1 364 ? 33.628 43.606 -3.254 1.00 78.48 ? 367 GLU A CB 1 ATOM 2934 C CG . GLU A 1 364 ? 34.559 43.100 -2.181 1.00 86.05 ? 367 GLU A CG 1 ATOM 2935 C CD . GLU A 1 364 ? 35.993 42.984 -2.660 1.00 90.36 ? 367 GLU A CD 1 ATOM 2936 O OE1 . GLU A 1 364 ? 36.236 42.172 -3.592 1.00 91.02 ? 367 GLU A OE1 1 ATOM 2937 O OE2 . GLU A 1 364 ? 36.867 43.700 -2.102 1.00 92.44 ? 367 GLU A OE2 1 ATOM 2938 N N . VAL A 1 365 ? 30.965 43.298 -0.895 1.00 81.00 ? 368 VAL A N 1 ATOM 2939 C CA . VAL A 1 365 ? 30.364 43.870 0.306 1.00 82.49 ? 368 VAL A CA 1 ATOM 2940 C C . VAL A 1 365 ? 31.418 43.761 1.389 1.00 84.69 ? 368 VAL A C 1 ATOM 2941 O O . VAL A 1 365 ? 32.074 42.729 1.524 1.00 84.34 ? 368 VAL A O 1 ATOM 2942 C CB . VAL A 1 365 ? 29.118 43.072 0.772 1.00 80.92 ? 368 VAL A CB 1 ATOM 2943 C CG1 . VAL A 1 365 ? 28.525 43.708 2.013 1.00 81.06 ? 368 VAL A CG1 1 ATOM 2944 C CG2 . VAL A 1 365 ? 28.083 43.020 -0.327 1.00 79.83 ? 368 VAL A CG2 1 ATOM 2945 N N . ASP A 1 366 ? 31.596 44.820 2.159 1.00 88.09 ? 369 ASP A N 1 ATOM 2946 C CA . ASP A 1 366 ? 32.590 44.781 3.216 1.00 91.93 ? 369 ASP A CA 1 ATOM 2947 C C . ASP A 1 366 ? 31.978 44.931 4.594 1.00 93.89 ? 369 ASP A C 1 ATOM 2948 O O . ASP A 1 366 ? 30.757 44.854 4.777 1.00 94.34 ? 369 ASP A O 1 ATOM 2949 C CB . ASP A 1 366 ? 33.621 45.872 3.002 1.00 91.95 ? 369 ASP A CB 1 ATOM 2950 C CG . ASP A 1 366 ? 32.995 47.133 2.516 1.00 94.74 ? 369 ASP A CG 1 ATOM 2951 O OD1 . ASP A 1 366 ? 32.003 47.582 3.132 1.00 95.84 ? 369 ASP A OD1 1 ATOM 2952 O OD2 . ASP A 1 366 ? 33.488 47.669 1.509 1.00 96.93 ? 369 ASP A OD2 1 ATOM 2953 N N . SER A 1 367 ? 32.859 45.155 5.560 1.00 95.70 ? 370 SER A N 1 ATOM 2954 C CA . SER A 1 367 ? 32.491 45.302 6.959 1.00 97.55 ? 370 SER A CA 1 ATOM 2955 C C . SER A 1 367 ? 31.438 46.371 7.250 1.00 97.92 ? 370 SER A C 1 ATOM 2956 O O . SER A 1 367 ? 30.428 46.100 7.915 1.00 97.92 ? 370 SER A O 1 ATOM 2957 C CB . SER A 1 367 ? 33.753 45.591 7.783 1.00 97.92 ? 370 SER A CB 1 ATOM 2958 O OG . SER A 1 367 ? 34.426 46.746 7.298 1.00 97.92 ? 370 SER A OG 1 ATOM 2959 N N . LYS A 1 368 ? 31.680 47.580 6.750 1.00 97.92 ? 371 LYS A N 1 ATOM 2960 C CA . LYS A 1 368 ? 30.781 48.703 6.984 1.00 97.92 ? 371 LYS A CA 1 ATOM 2961 C C . LYS A 1 368 ? 29.548 48.753 6.076 1.00 97.44 ? 371 LYS A C 1 ATOM 2962 O O . LYS A 1 368 ? 29.061 47.723 5.599 1.00 97.92 ? 371 LYS A O 1 ATOM 2963 C CB . LYS A 1 368 ? 31.574 50.015 6.883 1.00 97.92 ? 371 LYS A CB 1 ATOM 2964 C CG . LYS A 1 368 ? 32.800 50.071 7.814 1.00 97.92 ? 371 LYS A CG 1 ATOM 2965 C CD . LYS A 1 368 ? 33.561 51.404 7.709 1.00 97.92 ? 371 LYS A CD 1 ATOM 2966 C CE . LYS A 1 368 ? 34.812 51.429 8.607 1.00 97.92 ? 371 LYS A CE 1 ATOM 2967 N NZ . LYS A 1 368 ? 35.589 52.711 8.503 1.00 97.92 ? 371 LYS A NZ 1 ATOM 2968 N N . GLY A 1 369 ? 29.056 49.967 5.857 1.00 95.87 ? 372 GLY A N 1 ATOM 2969 C CA . GLY A 1 369 ? 27.874 50.201 5.044 1.00 93.54 ? 372 GLY A CA 1 ATOM 2970 C C . GLY A 1 369 ? 27.564 49.335 3.833 1.00 91.61 ? 372 GLY A C 1 ATOM 2971 O O . GLY A 1 369 ? 28.144 48.263 3.610 1.00 91.33 ? 372 GLY A O 1 ATOM 2972 N N . GLY A 1 370 ? 26.617 49.831 3.040 1.00 89.10 ? 373 GLY A N 1 ATOM 2973 C CA . GLY A 1 370 ? 26.185 49.127 1.852 1.00 85.27 ? 373 GLY A CA 1 ATOM 2974 C C . GLY A 1 370 ? 26.784 49.668 0.576 1.00 82.62 ? 373 GLY A C 1 ATOM 2975 O O . GLY A 1 370 ? 27.170 50.831 0.491 1.00 82.80 ? 373 GLY A O 1 ATOM 2976 N N . VAL A 1 371 ? 26.848 48.801 -0.426 1.00 80.01 ? 374 VAL A N 1 ATOM 2977 C CA . VAL A 1 371 ? 27.403 49.136 -1.724 1.00 75.30 ? 374 VAL A CA 1 ATOM 2978 C C . VAL A 1 371 ? 26.303 49.340 -2.742 1.00 72.83 ? 374 VAL A C 1 ATOM 2979 O O . VAL A 1 371 ? 25.368 48.548 -2.846 1.00 70.10 ? 374 VAL A O 1 ATOM 2980 C CB . VAL A 1 371 ? 28.307 48.011 -2.236 1.00 75.72 ? 374 VAL A CB 1 ATOM 2981 C CG1 . VAL A 1 371 ? 28.822 48.356 -3.610 1.00 76.59 ? 374 VAL A CG1 1 ATOM 2982 C CG2 . VAL A 1 371 ? 29.453 47.779 -1.270 1.00 75.26 ? 374 VAL A CG2 1 ATOM 2983 N N . GLN A 1 372 ? 26.423 50.406 -3.511 1.00 72.70 ? 375 GLN A N 1 ATOM 2984 C CA . GLN A 1 372 ? 25.418 50.661 -4.512 1.00 73.63 ? 375 GLN A CA 1 ATOM 2985 C C . GLN A 1 372 ? 25.795 49.991 -5.819 1.00 73.44 ? 375 GLN A C 1 ATOM 2986 O O . GLN A 1 372 ? 26.926 50.123 -6.289 1.00 73.89 ? 375 GLN A O 1 ATOM 2987 C CB . GLN A 1 372 ? 25.257 52.153 -4.749 1.00 75.02 ? 375 GLN A CB 1 ATOM 2988 C CG . GLN A 1 372 ? 24.060 52.441 -5.633 1.00 78.27 ? 375 GLN A CG 1 ATOM 2989 C CD . GLN A 1 372 ? 23.972 53.885 -6.062 1.00 79.81 ? 375 GLN A CD 1 ATOM 2990 O OE1 . GLN A 1 372 ? 22.957 54.313 -6.627 1.00 81.98 ? 375 GLN A OE1 1 ATOM 2991 N NE2 . GLN A 1 372 ? 25.038 54.651 -5.809 1.00 79.80 ? 375 GLN A NE2 1 ATOM 2992 N N . VAL A 1 373 ? 24.839 49.281 -6.410 1.00 71.73 ? 376 VAL A N 1 ATOM 2993 C CA . VAL A 1 373 ? 25.077 48.603 -7.668 1.00 69.56 ? 376 VAL A CA 1 ATOM 2994 C C . VAL A 1 373 ? 23.868 48.618 -8.573 1.00 68.28 ? 376 VAL A C 1 ATOM 2995 O O . VAL A 1 373 ? 22.796 48.125 -8.217 1.00 65.31 ? 376 VAL A O 1 ATOM 2996 C CB . VAL A 1 373 ? 25.501 47.166 -7.438 1.00 70.78 ? 376 VAL A CB 1 ATOM 2997 C CG1 . VAL A 1 373 ? 25.235 46.355 -8.672 1.00 73.76 ? 376 VAL A CG1 1 ATOM 2998 C CG2 . VAL A 1 373 ? 26.979 47.123 -7.110 1.00 71.78 ? 376 VAL A CG2 1 ATOM 2999 N N . ASN A 1 374 ? 24.061 49.183 -9.758 1.00 69.25 ? 377 ASN A N 1 ATOM 3000 C CA . ASN A 1 374 ? 22.993 49.283 -10.737 1.00 70.76 ? 377 ASN A CA 1 ATOM 3001 C C . ASN A 1 374 ? 23.162 48.263 -11.855 1.00 71.57 ? 377 ASN A C 1 ATOM 3002 O O . ASN A 1 374 ? 24.279 47.935 -12.240 1.00 70.75 ? 377 ASN A O 1 ATOM 3003 C CB . ASN A 1 374 ? 22.932 50.711 -11.303 1.00 72.38 ? 377 ASN A CB 1 ATOM 3004 C CG . ASN A 1 374 ? 22.132 51.659 -10.408 1.00 74.60 ? 377 ASN A CG 1 ATOM 3005 O OD1 . ASN A 1 374 ? 21.050 51.293 -9.950 1.00 77.65 ? 377 ASN A OD1 1 ATOM 3006 N ND2 . ASN A 1 374 ? 22.634 52.870 -10.168 1.00 71.75 ? 377 ASN A ND2 1 ATOM 3007 N N . PHE A 1 375 ? 22.036 47.751 -12.347 1.00 73.28 ? 378 PHE A N 1 ATOM 3008 C CA . PHE A 1 375 ? 22.012 46.760 -13.423 1.00 75.58 ? 378 PHE A CA 1 ATOM 3009 C C . PHE A 1 375 ? 21.177 47.283 -14.578 1.00 77.39 ? 378 PHE A C 1 ATOM 3010 O O . PHE A 1 375 ? 19.956 47.410 -14.449 1.00 78.40 ? 378 PHE A O 1 ATOM 3011 C CB . PHE A 1 375 ? 21.369 45.445 -12.965 1.00 75.87 ? 378 PHE A CB 1 ATOM 3012 C CG . PHE A 1 375 ? 22.203 44.651 -12.008 1.00 78.07 ? 378 PHE A CG 1 ATOM 3013 C CD1 . PHE A 1 375 ? 22.371 45.070 -10.694 1.00 79.47 ? 378 PHE A CD1 1 ATOM 3014 C CD2 . PHE A 1 375 ? 22.815 43.473 -12.420 1.00 77.96 ? 378 PHE A CD2 1 ATOM 3015 C CE1 . PHE A 1 375 ? 23.133 44.326 -9.808 1.00 78.77 ? 378 PHE A CE1 1 ATOM 3016 C CE2 . PHE A 1 375 ? 23.581 42.720 -11.541 1.00 78.51 ? 378 PHE A CE2 1 ATOM 3017 C CZ . PHE A 1 375 ? 23.741 43.148 -10.231 1.00 79.04 ? 378 PHE A CZ 1 ATOM 3018 N N . THR A 1 376 ? 21.820 47.578 -15.706 1.00 78.65 ? 379 THR A N 1 ATOM 3019 C CA . THR A 1 376 ? 21.094 48.068 -16.876 1.00 76.62 ? 379 THR A CA 1 ATOM 3020 C C . THR A 1 376 ? 20.826 46.867 -17.785 1.00 76.58 ? 379 THR A C 1 ATOM 3021 O O . THR A 1 376 ? 21.746 46.202 -18.232 1.00 76.60 ? 379 THR A O 1 ATOM 3022 C CB . THR A 1 376 ? 21.913 49.129 -17.609 1.00 75.08 ? 379 THR A CB 1 ATOM 3023 O OG1 . THR A 1 376 ? 22.725 49.840 -16.659 1.00 71.29 ? 379 THR A OG1 1 ATOM 3024 C CG2 . THR A 1 376 ? 20.975 50.108 -18.304 1.00 72.87 ? 379 THR A CG2 1 ATOM 3025 N N . LEU A 1 377 ? 19.560 46.581 -18.045 1.00 77.15 ? 380 LEU A N 1 ATOM 3026 C CA . LEU A 1 377 ? 19.214 45.425 -18.860 1.00 78.90 ? 380 LEU A CA 1 ATOM 3027 C C . LEU A 1 377 ? 18.617 45.740 -20.209 1.00 81.08 ? 380 LEU A C 1 ATOM 3028 O O . LEU A 1 377 ? 17.714 46.570 -20.325 1.00 80.78 ? 380 LEU A O 1 ATOM 3029 C CB . LEU A 1 377 ? 18.224 44.530 -18.120 1.00 77.53 ? 380 LEU A CB 1 ATOM 3030 C CG . LEU A 1 377 ? 18.603 44.061 -16.727 1.00 75.09 ? 380 LEU A CG 1 ATOM 3031 C CD1 . LEU A 1 377 ? 17.489 43.188 -16.205 1.00 74.08 ? 380 LEU A CD1 1 ATOM 3032 C CD2 . LEU A 1 377 ? 19.910 43.307 -16.771 1.00 74.42 ? 380 LEU A CD2 1 ATOM 3033 N N . SER A 1 378 ? 19.104 45.031 -21.221 1.00 84.05 ? 381 SER A N 1 ATOM 3034 C CA . SER A 1 378 ? 18.628 45.194 -22.586 1.00 86.42 ? 381 SER A CA 1 ATOM 3035 C C . SER A 1 378 ? 17.432 44.279 -22.780 1.00 88.14 ? 381 SER A C 1 ATOM 3036 O O . SER A 1 378 ? 17.241 43.325 -22.016 1.00 89.70 ? 381 SER A O 1 ATOM 3037 C CB . SER A 1 378 ? 19.726 44.807 -23.565 1.00 86.41 ? 381 SER A CB 1 ATOM 3038 O OG . SER A 1 378 ? 20.946 45.415 -23.198 1.00 85.41 ? 381 SER A OG 1 ATOM 3039 N N . ARG A 1 379 ? 16.635 44.560 -23.804 1.00 89.01 ? 382 ARG A N 1 ATOM 3040 C CA . ARG A 1 379 ? 15.454 43.756 -24.085 1.00 90.86 ? 382 ARG A CA 1 ATOM 3041 C C . ARG A 1 379 ? 15.763 42.546 -24.969 1.00 92.26 ? 382 ARG A C 1 ATOM 3042 O O . ARG A 1 379 ? 16.913 42.111 -25.070 1.00 91.51 ? 382 ARG A O 1 ATOM 3043 C CB . ARG A 1 379 ? 14.405 44.629 -24.751 1.00 91.03 ? 382 ARG A CB 1 ATOM 3044 C CG . ARG A 1 379 ? 14.102 45.864 -23.960 1.00 92.66 ? 382 ARG A CG 1 ATOM 3045 C CD . ARG A 1 379 ? 13.050 46.679 -24.651 1.00 95.42 ? 382 ARG A CD 1 ATOM 3046 N NE . ARG A 1 379 ? 12.298 47.481 -23.697 1.00 97.67 ? 382 ARG A NE 1 ATOM 3047 C CZ . ARG A 1 379 ? 11.265 48.246 -24.024 1.00 97.92 ? 382 ARG A CZ 1 ATOM 3048 N NH1 . ARG A 1 379 ? 10.864 48.315 -25.285 1.00 97.92 ? 382 ARG A NH1 1 ATOM 3049 N NH2 . ARG A 1 379 ? 10.624 48.928 -23.086 1.00 97.92 ? 382 ARG A NH2 1 ATOM 3050 N N . THR A 1 380 ? 14.729 42.002 -25.607 1.00 94.19 ? 383 THR A N 1 ATOM 3051 C CA . THR A 1 380 ? 14.913 40.845 -26.479 1.00 95.65 ? 383 THR A CA 1 ATOM 3052 C C . THR A 1 380 ? 13.927 40.790 -27.667 1.00 96.23 ? 383 THR A C 1 ATOM 3053 O O . THR A 1 380 ? 12.938 41.564 -27.661 1.00 95.98 ? 383 THR A O 1 ATOM 3054 C CB . THR A 1 380 ? 14.826 39.528 -25.657 1.00 95.45 ? 383 THR A CB 1 ATOM 3055 O OG1 . THR A 1 380 ? 14.574 39.823 -24.273 1.00 93.97 ? 383 THR A OG1 1 ATOM 3056 C CG2 . THR A 1 380 ? 16.136 38.768 -25.765 1.00 94.99 ? 383 THR A CG2 1 ATOM 3057 O OXT . THR A 1 380 ? 14.161 39.977 -28.599 1.00 95.40 ? 383 THR A OXT 1 HETATM 3058 C C1 . NAG B 2 . ? -4.244 30.228 22.067 0.92 48.80 ? 901 NAG A C1 1 HETATM 3059 C C2 . NAG B 2 . ? -4.636 29.148 23.053 0.92 47.68 ? 901 NAG A C2 1 HETATM 3060 C C3 . NAG B 2 . ? -4.081 27.804 22.676 0.92 46.49 ? 901 NAG A C3 1 HETATM 3061 C C4 . NAG B 2 . ? -4.258 27.489 21.200 0.92 48.86 ? 901 NAG A C4 1 HETATM 3062 C C5 . NAG B 2 . ? -3.891 28.672 20.310 0.92 49.65 ? 901 NAG A C5 1 HETATM 3063 C C6 . NAG B 2 . ? -4.289 28.412 18.867 0.92 50.98 ? 901 NAG A C6 1 HETATM 3064 C C7 . NAG B 2 . ? -4.993 29.547 25.381 0.92 50.54 ? 901 NAG A C7 1 HETATM 3065 C C8 . NAG B 2 . ? -4.425 29.899 26.743 0.92 49.84 ? 901 NAG A C8 1 HETATM 3066 N N2 . NAG B 2 . ? -4.141 29.483 24.365 0.92 49.60 ? 901 NAG A N2 1 HETATM 3067 O O3 . NAG B 2 . ? -4.769 26.825 23.428 0.92 45.72 ? 901 NAG A O3 1 HETATM 3068 O O4 . NAG B 2 . ? -3.400 26.391 20.872 0.92 53.13 ? 901 NAG A O4 1 HETATM 3069 O O5 . NAG B 2 . ? -4.594 29.849 20.738 0.92 49.11 ? 901 NAG A O5 1 HETATM 3070 O O6 . NAG B 2 . ? -3.666 29.325 17.976 0.92 52.98 ? 901 NAG A O6 1 HETATM 3071 O O7 . NAG B 2 . ? -6.203 29.343 25.254 0.92 50.32 ? 901 NAG A O7 1 HETATM 3072 C C1 . NAG C 2 . ? -4.015 25.221 20.488 0.92 56.10 ? 902 NAG A C1 1 HETATM 3073 C C2 . NAG C 2 . ? -3.022 24.331 19.751 0.92 56.95 ? 902 NAG A C2 1 HETATM 3074 C C3 . NAG C 2 . ? -3.707 23.041 19.349 0.92 60.47 ? 902 NAG A C3 1 HETATM 3075 C C4 . NAG C 2 . ? -4.410 22.389 20.552 0.92 63.67 ? 902 NAG A C4 1 HETATM 3076 C C5 . NAG C 2 . ? -5.259 23.405 21.330 0.92 62.96 ? 902 NAG A C5 1 HETATM 3077 C C6 . NAG C 2 . ? -5.791 22.849 22.629 0.92 64.24 ? 902 NAG A C6 1 HETATM 3078 C C7 . NAG C 2 . ? -1.347 25.593 18.577 0.92 58.37 ? 902 NAG A C7 1 HETATM 3079 C C8 . NAG C 2 . ? -0.946 26.327 17.311 0.92 60.16 ? 902 NAG A C8 1 HETATM 3080 N N2 . NAG C 2 . ? -2.547 25.023 18.574 0.92 56.98 ? 902 NAG A N2 1 HETATM 3081 O O3 . NAG C 2 . ? -2.732 22.155 18.822 0.92 62.01 ? 902 NAG A O3 1 HETATM 3082 O O4 . NAG C 2 . ? -5.269 21.334 20.087 0.92 70.68 ? 902 NAG A O4 1 HETATM 3083 O O5 . NAG C 2 . ? -4.474 24.561 21.661 0.92 58.52 ? 902 NAG A O5 1 HETATM 3084 O O6 . NAG C 2 . ? -4.873 21.923 23.191 0.92 67.69 ? 902 NAG A O6 1 HETATM 3085 O O7 . NAG C 2 . ? -0.564 25.535 19.534 0.92 61.12 ? 902 NAG A O7 1 HETATM 3086 C C1 . MAN D 3 . ? -5.185 20.134 20.773 0.92 76.62 ? 903 MAN A C1 1 HETATM 3087 C C2 . MAN D 3 . ? -6.453 19.309 20.507 0.92 78.91 ? 903 MAN A C2 1 HETATM 3088 C C3 . MAN D 3 . ? -6.316 17.907 21.118 0.92 79.56 ? 903 MAN A C3 1 HETATM 3089 C C4 . MAN D 3 . ? -5.005 17.244 20.657 0.92 79.68 ? 903 MAN A C4 1 HETATM 3090 C C5 . MAN D 3 . ? -3.824 18.171 20.971 0.92 80.30 ? 903 MAN A C5 1 HETATM 3091 C C6 . MAN D 3 . ? -2.436 17.639 20.581 0.92 81.37 ? 903 MAN A C6 1 HETATM 3092 O O2 . MAN D 3 . ? -6.690 19.222 19.105 0.92 79.23 ? 903 MAN A O2 1 HETATM 3093 O O3 . MAN D 3 . ? -7.437 17.107 20.753 0.92 80.78 ? 903 MAN A O3 1 HETATM 3094 O O4 . MAN D 3 . ? -4.830 16.017 21.338 0.92 80.62 ? 903 MAN A O4 1 HETATM 3095 O O5 . MAN D 3 . ? -4.016 19.436 20.306 0.92 79.94 ? 903 MAN A O5 1 HETATM 3096 O O6 . MAN D 3 . ? -2.355 17.267 19.207 0.92 79.51 ? 903 MAN A O6 1 HETATM 3097 C C1 . NAG E 2 . ? 7.091 39.163 -10.124 0.67 65.44 ? 911 NAG A C1 1 HETATM 3098 C C2 . NAG E 2 . ? 5.637 39.009 -10.624 0.67 66.27 ? 911 NAG A C2 1 HETATM 3099 C C3 . NAG E 2 . ? 5.184 37.582 -10.940 0.67 67.49 ? 911 NAG A C3 1 HETATM 3100 C C4 . NAG E 2 . ? 6.308 36.827 -11.629 0.67 67.89 ? 911 NAG A C4 1 HETATM 3101 C C5 . NAG E 2 . ? 7.461 36.807 -10.634 0.67 66.56 ? 911 NAG A C5 1 HETATM 3102 C C6 . NAG E 2 . ? 8.611 35.910 -11.044 0.67 66.27 ? 911 NAG A C6 1 HETATM 3103 C C7 . NAG E 2 . ? 4.692 39.152 -8.393 0.67 67.18 ? 911 NAG A C7 1 HETATM 3104 C C8 . NAG E 2 . ? 3.713 39.825 -7.438 0.67 63.29 ? 911 NAG A C8 1 HETATM 3105 N N2 . NAG E 2 . ? 4.730 39.598 -9.650 0.67 66.50 ? 911 NAG A N2 1 HETATM 3106 O O3 . NAG E 2 . ? 4.047 37.630 -11.789 0.67 66.99 ? 911 NAG A O3 1 HETATM 3107 O O4 . NAG E 2 . ? 5.883 35.494 -12.038 0.67 70.45 ? 911 NAG A O4 1 HETATM 3108 O O5 . NAG E 2 . ? 8.004 38.128 -10.539 0.67 66.09 ? 911 NAG A O5 1 HETATM 3109 O O6 . NAG E 2 . ? 9.804 36.663 -11.226 0.67 66.75 ? 911 NAG A O6 1 HETATM 3110 O O7 . NAG E 2 . ? 5.407 38.231 -7.986 0.67 68.55 ? 911 NAG A O7 1 HETATM 3111 C C1 . NAG F 2 . ? 5.682 34.478 -11.098 0.67 73.81 ? 912 NAG A C1 1 HETATM 3112 C C2 . NAG F 2 . ? 6.910 33.542 -11.080 0.67 73.20 ? 912 NAG A C2 1 HETATM 3113 C C3 . NAG F 2 . ? 6.880 32.566 -9.896 0.67 73.88 ? 912 NAG A C3 1 HETATM 3114 C C4 . NAG F 2 . ? 6.541 33.282 -8.583 0.67 75.50 ? 912 NAG A C4 1 HETATM 3115 C C5 . NAG F 2 . ? 5.266 34.114 -8.752 0.67 76.37 ? 912 NAG A C5 1 HETATM 3116 C C6 . NAG F 2 . ? 4.898 34.891 -7.496 0.67 77.08 ? 912 NAG A C6 1 HETATM 3117 C C7 . NAG F 2 . ? 5.951 32.083 -12.762 0.67 70.44 ? 912 NAG A C7 1 HETATM 3118 C C8 . NAG F 2 . ? 6.129 31.305 -14.061 0.67 67.34 ? 912 NAG A C8 1 HETATM 3119 N N2 . NAG F 2 . ? 6.995 32.783 -12.319 0.67 71.58 ? 912 NAG A N2 1 HETATM 3120 O O3 . NAG F 2 . ? 8.153 31.952 -9.778 0.67 72.20 ? 912 NAG A O3 1 HETATM 3121 O O4 . NAG F 2 . ? 6.354 32.326 -7.550 0.67 75.40 ? 912 NAG A O4 1 HETATM 3122 O O5 . NAG F 2 . ? 5.453 35.081 -9.805 0.67 75.82 ? 912 NAG A O5 1 HETATM 3123 O O6 . NAG F 2 . ? 4.464 34.019 -6.459 0.67 77.27 ? 912 NAG A O6 1 HETATM 3124 O O7 . NAG F 2 . ? 4.868 32.049 -12.174 0.67 69.78 ? 912 NAG A O7 1 HETATM 3125 C C1 . NAG G 2 . ? 22.467 53.922 -11.149 0.74 66.06 ? 921 NAG A C1 1 HETATM 3126 C C2 . NAG G 2 . ? 23.219 55.222 -10.796 0.74 62.41 ? 921 NAG A C2 1 HETATM 3127 C C3 . NAG G 2 . ? 22.494 56.018 -9.735 0.74 58.80 ? 921 NAG A C3 1 HETATM 3128 C C4 . NAG G 2 . ? 21.179 56.364 -10.385 0.74 60.44 ? 921 NAG A C4 1 HETATM 3129 C C5 . NAG G 2 . ? 20.393 55.068 -10.531 0.74 61.25 ? 921 NAG A C5 1 HETATM 3130 C C6 . NAG G 2 . ? 18.991 55.280 -11.078 0.74 60.11 ? 921 NAG A C6 1 HETATM 3131 C C7 . NAG G 2 . ? 25.128 54.154 -9.690 0.74 65.02 ? 921 NAG A C7 1 HETATM 3132 C C8 . NAG G 2 . ? 26.643 54.142 -9.520 0.74 63.31 ? 921 NAG A C8 1 HETATM 3133 N N2 . NAG G 2 . ? 24.638 55.073 -10.511 0.74 63.31 ? 921 NAG A N2 1 HETATM 3134 O O3 . NAG G 2 . ? 23.227 57.193 -9.447 0.74 55.83 ? 921 NAG A O3 1 HETATM 3135 O O4 . NAG G 2 . ? 20.455 57.348 -9.620 0.74 66.55 ? 921 NAG A O4 1 HETATM 3136 O O5 . NAG G 2 . ? 21.069 54.173 -11.452 0.74 64.50 ? 921 NAG A O5 1 HETATM 3137 O O6 . NAG G 2 . ? 18.829 56.586 -11.606 0.74 56.88 ? 921 NAG A O6 1 HETATM 3138 O O7 . NAG G 2 . ? 24.436 53.349 -9.082 0.74 69.23 ? 921 NAG A O7 1 HETATM 3139 C C1 . NAG H 2 . ? 20.471 58.645 -10.134 0.74 71.66 ? 922 NAG A C1 1 HETATM 3140 C C2 . NAG H 2 . ? 19.356 59.486 -9.497 0.74 73.34 ? 922 NAG A C2 1 HETATM 3141 C C3 . NAG H 2 . ? 19.463 60.976 -9.922 0.74 76.03 ? 922 NAG A C3 1 HETATM 3142 C C4 . NAG H 2 . ? 20.902 61.545 -9.826 0.74 77.09 ? 922 NAG A C4 1 HETATM 3143 C C5 . NAG H 2 . ? 21.912 60.540 -10.426 0.74 76.08 ? 922 NAG A C5 1 HETATM 3144 C C6 . NAG H 2 . ? 23.354 60.947 -10.182 0.74 75.24 ? 922 NAG A C6 1 HETATM 3145 C C7 . NAG H 2 . ? 17.571 59.236 -11.114 0.74 73.03 ? 922 NAG A C7 1 HETATM 3146 C C8 . NAG H 2 . ? 16.203 58.663 -11.452 0.74 71.97 ? 922 NAG A C8 1 HETATM 3147 N N2 . NAG H 2 . ? 18.060 58.963 -9.900 0.74 71.94 ? 922 NAG A N2 1 HETATM 3148 O O3 . NAG H 2 . ? 18.597 61.759 -9.110 0.74 76.32 ? 922 NAG A O3 1 HETATM 3149 O O4 . NAG H 2 . ? 21.010 62.819 -10.541 0.74 80.16 ? 922 NAG A O4 1 HETATM 3150 O O5 . NAG H 2 . ? 21.747 59.227 -9.836 0.74 74.39 ? 922 NAG A O5 1 HETATM 3151 O O6 . NAG H 2 . ? 23.720 60.745 -8.823 0.74 73.21 ? 922 NAG A O6 1 HETATM 3152 O O7 . NAG H 2 . ? 18.175 59.915 -11.959 0.74 72.10 ? 922 NAG A O7 1 HETATM 3153 C C1 . MAN I 3 . ? 20.001 63.790 -10.414 0.74 80.92 ? 923 MAN A C1 1 HETATM 3154 C C2 . MAN I 3 . ? 19.738 64.486 -11.766 0.74 80.38 ? 923 MAN A C2 1 HETATM 3155 C C3 . MAN I 3 . ? 20.928 65.371 -12.171 0.74 81.31 ? 923 MAN A C3 1 HETATM 3156 C C4 . MAN I 3 . ? 21.310 66.328 -11.034 0.74 80.89 ? 923 MAN A C4 1 HETATM 3157 C C5 . MAN I 3 . ? 21.534 65.557 -9.734 0.74 80.24 ? 923 MAN A C5 1 HETATM 3158 C C6 . MAN I 3 . ? 21.769 66.513 -8.582 0.74 78.29 ? 923 MAN A C6 1 HETATM 3159 O O2 . MAN I 3 . ? 18.561 65.279 -11.679 0.74 77.29 ? 923 MAN A O2 1 HETATM 3160 O O3 . MAN I 3 . ? 20.594 66.121 -13.333 0.74 81.57 ? 923 MAN A O3 1 HETATM 3161 O O4 . MAN I 3 . ? 22.505 67.018 -11.373 0.74 80.95 ? 923 MAN A O4 1 HETATM 3162 O O5 . MAN I 3 . ? 20.367 64.760 -9.399 0.74 81.58 ? 923 MAN A O5 1 HETATM 3163 O O6 . MAN I 3 . ? 21.949 65.816 -7.360 0.74 76.74 ? 923 MAN A O6 1 HETATM 3164 S S . SO4 J 4 . ? 18.309 37.427 36.952 0.59 66.00 ? 996 SO4 A S 1 HETATM 3165 O O1 . SO4 J 4 . ? 16.934 37.735 36.492 0.59 62.63 ? 996 SO4 A O1 1 HETATM 3166 O O2 . SO4 J 4 . ? 19.035 38.685 37.218 0.59 64.49 ? 996 SO4 A O2 1 HETATM 3167 O O3 . SO4 J 4 . ? 18.249 36.626 38.201 0.59 62.77 ? 996 SO4 A O3 1 HETATM 3168 O O4 . SO4 J 4 . ? 19.034 36.685 35.893 0.59 64.46 ? 996 SO4 A O4 1 HETATM 3169 S S . SO4 K 4 . ? 23.344 55.724 23.677 0.90 67.01 ? 997 SO4 A S 1 HETATM 3170 O O1 . SO4 K 4 . ? 22.187 56.397 23.047 0.90 62.43 ? 997 SO4 A O1 1 HETATM 3171 O O2 . SO4 K 4 . ? 24.461 56.684 23.764 0.90 65.29 ? 997 SO4 A O2 1 HETATM 3172 O O3 . SO4 K 4 . ? 23.022 55.257 25.040 0.90 64.57 ? 997 SO4 A O3 1 HETATM 3173 O O4 . SO4 K 4 . ? 23.750 54.570 22.855 0.90 65.48 ? 997 SO4 A O4 1 HETATM 3174 S S . SO4 L 4 . ? 5.978 32.303 20.343 0.69 55.47 ? 998 SO4 A S 1 HETATM 3175 O O1 . SO4 L 4 . ? 4.897 32.687 19.407 0.69 52.12 ? 998 SO4 A O1 1 HETATM 3176 O O2 . SO4 L 4 . ? 7.163 33.158 20.126 0.69 53.90 ? 998 SO4 A O2 1 HETATM 3177 O O3 . SO4 L 4 . ? 5.550 32.408 21.760 0.69 55.08 ? 998 SO4 A O3 1 HETATM 3178 O O4 . SO4 L 4 . ? 6.327 30.911 20.072 0.69 59.34 ? 998 SO4 A O4 1 HETATM 3179 ZN ZN . ZN M 5 . ? 5.572 35.977 22.379 1.00 51.80 ? 999 ZN A ZN 1 HETATM 3180 O O . HOH N 6 . ? 22.933 72.121 23.490 1.00 67.93 ? 2001 HOH A O 1 HETATM 3181 O O . HOH N 6 . ? 3.491 67.462 27.999 1.00 58.99 ? 2002 HOH A O 1 HETATM 3182 O O . HOH N 6 . ? 1.420 53.046 38.310 1.00 74.57 ? 2003 HOH A O 1 HETATM 3183 O O . HOH N 6 . ? -1.425 59.397 26.373 1.00 46.52 ? 2004 HOH A O 1 HETATM 3184 O O . HOH N 6 . ? 3.374 64.877 28.149 1.00 64.31 ? 2005 HOH A O 1 HETATM 3185 O O . HOH N 6 . ? 0.979 52.506 34.238 1.00 52.71 ? 2006 HOH A O 1 HETATM 3186 O O . HOH N 6 . ? -0.068 65.837 5.208 1.00 70.33 ? 2007 HOH A O 1 HETATM 3187 O O . HOH N 6 . ? -6.119 57.085 11.068 1.00 57.70 ? 2008 HOH A O 1 HETATM 3188 O O . HOH N 6 . ? -8.490 51.633 26.389 1.00 49.29 ? 2009 HOH A O 1 HETATM 3189 O O . HOH N 6 . ? -8.804 56.503 28.681 1.00 49.83 ? 2010 HOH A O 1 HETATM 3190 O O . HOH N 6 . ? -3.229 53.901 29.726 1.00 60.15 ? 2011 HOH A O 1 HETATM 3191 O O . HOH N 6 . ? -7.075 62.103 13.146 1.00 51.60 ? 2012 HOH A O 1 HETATM 3192 O O . HOH N 6 . ? 0.632 62.593 24.867 1.00 42.27 ? 2013 HOH A O 1 HETATM 3193 O O . HOH N 6 . ? 5.423 64.960 26.016 1.00 45.96 ? 2014 HOH A O 1 HETATM 3194 O O . HOH N 6 . ? 8.879 68.812 13.138 1.00 53.76 ? 2015 HOH A O 1 HETATM 3195 O O . HOH N 6 . ? 6.845 69.976 11.722 1.00 50.71 ? 2016 HOH A O 1 HETATM 3196 O O . HOH N 6 . ? 1.209 63.310 6.583 1.00 52.05 ? 2017 HOH A O 1 HETATM 3197 O O . HOH N 6 . ? -3.007 58.774 4.958 1.00 58.09 ? 2018 HOH A O 1 HETATM 3198 O O . HOH N 6 . ? -1.241 61.583 9.880 1.00 60.83 ? 2019 HOH A O 1 HETATM 3199 O O . HOH N 6 . ? -6.159 56.042 8.697 1.00 40.12 ? 2020 HOH A O 1 HETATM 3200 O O . HOH N 6 . ? -10.737 50.525 24.930 1.00 29.03 ? 2021 HOH A O 1 HETATM 3201 O O . HOH N 6 . ? -13.522 31.694 16.110 1.00 38.41 ? 2022 HOH A O 1 HETATM 3202 O O . HOH N 6 . ? -12.735 35.481 12.323 1.00 48.03 ? 2023 HOH A O 1 HETATM 3203 O O . HOH N 6 . ? 4.792 55.651 -2.275 1.00 46.48 ? 2024 HOH A O 1 HETATM 3204 O O . HOH N 6 . ? 18.770 57.040 -3.605 1.00 61.28 ? 2025 HOH A O 1 HETATM 3205 O O . HOH N 6 . ? 20.039 53.999 0.569 1.00 45.22 ? 2026 HOH A O 1 HETATM 3206 O O . HOH N 6 . ? 28.430 24.295 4.540 1.00 43.73 ? 2027 HOH A O 1 HETATM 3207 O O . HOH N 6 . ? 32.286 31.897 28.718 1.00 72.45 ? 2028 HOH A O 1 HETATM 3208 O O . HOH N 6 . ? 10.303 21.939 22.494 1.00 59.79 ? 2029 HOH A O 1 HETATM 3209 O O . HOH N 6 . ? 13.923 71.152 12.392 1.00 63.18 ? 2030 HOH A O 1 HETATM 3210 O O . HOH N 6 . ? 23.730 65.327 20.272 1.00 61.72 ? 2031 HOH A O 1 HETATM 3211 O O . HOH N 6 . ? 15.755 41.395 32.097 1.00 59.64 ? 2032 HOH A O 1 HETATM 3212 O O . HOH N 6 . ? 16.954 69.442 9.293 1.00 47.69 ? 2033 HOH A O 1 HETATM 3213 O O . HOH N 6 . ? -12.814 22.210 23.195 1.00 69.78 ? 2034 HOH A O 1 HETATM 3214 O O . HOH N 6 . ? 1.654 15.656 12.891 1.00 66.10 ? 2035 HOH A O 1 HETATM 3215 O O . HOH N 6 . ? -4.127 45.283 34.376 1.00 55.56 ? 2036 HOH A O 1 HETATM 3216 O O . HOH N 6 . ? 26.659 35.464 -18.048 1.00 62.15 ? 2037 HOH A O 1 HETATM 3217 O O . HOH N 6 . ? 1.097 34.250 36.175 1.00 51.34 ? 2038 HOH A O 1 HETATM 3218 O O . HOH N 6 . ? 2.551 35.806 37.541 1.00 39.77 ? 2039 HOH A O 1 HETATM 3219 O O . HOH N 6 . ? -14.224 37.329 13.913 1.00 44.42 ? 2040 HOH A O 1 HETATM 3220 O O . HOH N 6 . ? -7.253 34.506 25.407 1.00 51.82 ? 2041 HOH A O 1 HETATM 3221 O O . HOH N 6 . ? -10.583 25.885 13.995 1.00 58.47 ? 2042 HOH A O 1 HETATM 3222 O O . HOH N 6 . ? -13.636 29.249 15.323 1.00 50.52 ? 2043 HOH A O 1 HETATM 3223 O O . HOH N 6 . ? -0.085 28.729 21.665 1.00 34.90 ? 2044 HOH A O 1 HETATM 3224 O O . HOH N 6 . ? 3.155 25.271 18.964 1.00 52.19 ? 2045 HOH A O 1 HETATM 3225 O O . HOH N 6 . ? 4.641 29.513 3.145 1.00 45.11 ? 2046 HOH A O 1 HETATM 3226 O O . HOH N 6 . ? 2.144 23.201 3.365 1.00 53.13 ? 2047 HOH A O 1 HETATM 3227 O O . HOH N 6 . ? 0.467 19.201 8.463 1.00 44.19 ? 2048 HOH A O 1 HETATM 3228 O O . HOH N 6 . ? -11.207 36.475 10.297 1.00 46.30 ? 2049 HOH A O 1 HETATM 3229 O O . HOH N 6 . ? 0.746 36.436 -4.279 1.00 74.35 ? 2050 HOH A O 1 HETATM 3230 O O . HOH N 6 . ? 10.790 31.405 27.679 1.00 43.78 ? 2051 HOH A O 1 HETATM 3231 O O . HOH N 6 . ? 13.512 20.098 4.822 1.00 56.74 ? 2052 HOH A O 1 HETATM 3232 O O . HOH N 6 . ? 15.739 16.937 6.525 1.00 55.11 ? 2053 HOH A O 1 HETATM 3233 O O . HOH N 6 . ? 11.617 19.027 20.186 1.00 45.71 ? 2054 HOH A O 1 HETATM 3234 O O . HOH N 6 . ? 20.067 21.502 16.546 1.00 47.98 ? 2055 HOH A O 1 HETATM 3235 O O . HOH N 6 . ? 26.370 29.473 5.651 1.00 63.51 ? 2056 HOH A O 1 HETATM 3236 O O . HOH N 6 . ? 26.885 25.657 8.989 1.00 72.26 ? 2057 HOH A O 1 HETATM 3237 O O . HOH N 6 . ? 24.546 25.621 4.912 1.00 56.82 ? 2058 HOH A O 1 HETATM 3238 O O . HOH N 6 . ? 19.775 26.292 3.170 1.00 70.90 ? 2059 HOH A O 1 HETATM 3239 O O . HOH N 6 . ? 26.399 30.379 8.737 1.00 48.56 ? 2060 HOH A O 1 HETATM 3240 O O . HOH N 6 . ? 14.924 38.705 31.259 1.00 50.49 ? 2061 HOH A O 1 HETATM 3241 O O . HOH N 6 . ? 20.432 36.794 41.320 1.00 70.80 ? 2062 HOH A O 1 HETATM 3242 O O . HOH N 6 . ? 21.095 34.103 42.304 1.00 68.90 ? 2063 HOH A O 1 HETATM 3243 O O . HOH N 6 . ? 18.077 26.537 25.314 1.00 41.85 ? 2064 HOH A O 1 HETATM 3244 O O . HOH N 6 . ? 12.789 26.431 27.059 1.00 39.56 ? 2065 HOH A O 1 HETATM 3245 O O . HOH N 6 . ? 30.308 32.555 25.309 1.00 69.74 ? 2066 HOH A O 1 HETATM 3246 O O . HOH N 6 . ? 27.664 34.947 25.507 1.00 45.72 ? 2067 HOH A O 1 HETATM 3247 O O . HOH N 6 . ? 32.358 34.713 24.232 1.00 45.28 ? 2068 HOH A O 1 HETATM 3248 O O . HOH N 6 . ? 9.577 21.966 19.714 1.00 41.36 ? 2069 HOH A O 1 HETATM 3249 O O . HOH N 6 . ? 8.311 35.747 -2.768 1.00 60.84 ? 2070 HOH A O 1 HETATM 3250 O O . HOH N 6 . ? 6.512 40.792 -2.030 1.00 60.31 ? 2071 HOH A O 1 HETATM 3251 O O . HOH N 6 . ? 5.797 41.370 9.818 1.00 45.70 ? 2072 HOH A O 1 HETATM 3252 O O . HOH N 6 . ? 12.719 48.804 40.730 1.00 56.98 ? 2073 HOH A O 1 HETATM 3253 O O . HOH N 6 . ? 20.354 46.585 35.292 1.00 67.53 ? 2074 HOH A O 1 HETATM 3254 O O . HOH N 6 . ? 11.384 43.531 34.756 1.00 49.28 ? 2075 HOH A O 1 HETATM 3255 O O . HOH N 6 . ? 21.114 57.987 29.124 1.00 59.26 ? 2076 HOH A O 1 HETATM 3256 O O . HOH N 6 . ? 15.768 43.852 31.405 1.00 47.55 ? 2077 HOH A O 1 HETATM 3257 O O . HOH N 6 . ? 15.487 44.192 27.758 1.00 48.18 ? 2078 HOH A O 1 HETATM 3258 O O . HOH N 6 . ? 27.024 53.683 13.489 1.00 43.49 ? 2079 HOH A O 1 HETATM 3259 O O . HOH N 6 . ? 26.332 55.055 17.535 1.00 56.04 ? 2080 HOH A O 1 HETATM 3260 O O . HOH N 6 . ? 26.027 42.657 8.853 1.00 41.65 ? 2081 HOH A O 1 HETATM 3261 O O . HOH N 6 . ? 20.910 52.036 1.651 1.00 43.12 ? 2082 HOH A O 1 HETATM 3262 O O . HOH N 6 . ? 28.700 47.846 13.692 1.00 66.69 ? 2083 HOH A O 1 HETATM 3263 O O . HOH N 6 . ? -10.489 23.166 20.596 1.00 52.87 ? 2084 HOH A O 1 HETATM 3264 O O . HOH N 6 . ? 1.949 19.580 15.552 1.00 63.22 ? 2085 HOH A O 1 HETATM 3265 O O . HOH N 6 . ? -2.355 16.827 12.597 1.00 57.83 ? 2086 HOH A O 1 HETATM 3266 O O . HOH N 6 . ? -4.631 16.372 13.863 1.00 51.16 ? 2087 HOH A O 1 HETATM 3267 O O . HOH N 6 . ? 7.230 56.811 -15.401 1.00 62.17 ? 2088 HOH A O 1 HETATM 3268 O O . HOH N 6 . ? 11.632 58.573 -18.859 1.00 57.20 ? 2089 HOH A O 1 HETATM 3269 O O . HOH N 6 . ? 9.643 53.199 -13.713 1.00 59.87 ? 2090 HOH A O 1 HETATM 3270 O O . HOH N 6 . ? 17.758 67.803 -8.342 1.00 73.80 ? 2091 HOH A O 1 HETATM 3271 O O . HOH N 6 . ? 11.701 38.708 -11.823 1.00 48.75 ? 2092 HOH A O 1 HETATM 3272 O O . HOH N 6 . ? 18.102 32.809 -6.437 1.00 44.25 ? 2093 HOH A O 1 HETATM 3273 O O . HOH N 6 . ? 23.505 29.853 -7.154 1.00 53.28 ? 2094 HOH A O 1 HETATM 3274 O O . HOH N 6 . ? 19.018 26.303 0.094 1.00 47.66 ? 2095 HOH A O 1 HETATM 3275 O O . HOH N 6 . ? 9.820 59.312 -11.513 1.00 60.00 ? 2096 HOH A O 1 HETATM 3276 O O . HOH N 6 . ? 17.733 41.528 2.027 1.00 56.80 ? 2097 HOH A O 1 HETATM 3277 O O . HOH N 6 . ? 24.000 43.742 6.568 1.00 59.42 ? 2098 HOH A O 1 HETATM 3278 O O . HOH N 6 . ? 29.597 42.105 8.014 1.00 52.63 ? 2099 HOH A O 1 HETATM 3279 O O . HOH N 6 . ? 27.877 34.375 2.746 1.00 56.59 ? 2100 HOH A O 1 HETATM 3280 O O . HOH N 6 . ? 23.696 36.847 -16.332 1.00 62.42 ? 2101 HOH A O 1 HETATM 3281 O O . HOH N 6 . ? 27.484 49.878 -15.249 1.00 48.15 ? 2102 HOH A O 1 HETATM 3282 O O . HOH N 6 . ? 32.233 42.270 -12.675 1.00 53.57 ? 2103 HOH A O 1 HETATM 3283 O O . HOH N 6 . ? 30.567 46.709 -7.951 1.00 55.65 ? 2104 HOH A O 1 HETATM 3284 O O . HOH N 6 . ? 36.060 45.993 4.935 1.00 64.09 ? 2105 HOH A O 1 HETATM 3285 O O . HOH N 6 . ? 25.021 49.426 -15.635 1.00 43.21 ? 2106 HOH A O 1 HETATM 3286 O O . HOH N 6 . ? 9.273 45.922 -22.034 1.00 67.66 ? 2107 HOH A O 1 HETATM 3287 O O . HOH N 6 . ? 16.940 41.301 -29.713 1.00 56.05 ? 2108 HOH A O 1 HETATM 3288 O O . HOH N 6 . ? -3.246 22.875 14.751 1.00 49.57 ? 2109 HOH A O 1 HETATM 3289 O O . HOH N 6 . ? 0.630 19.647 19.034 1.00 53.57 ? 2110 HOH A O 1 HETATM 3290 O O . HOH N 6 . ? -6.642 21.762 16.166 1.00 54.66 ? 2111 HOH A O 1 HETATM 3291 O O . HOH N 6 . ? -9.881 17.060 20.915 1.00 49.14 ? 2112 HOH A O 1 HETATM 3292 O O . HOH N 6 . ? -10.074 20.026 19.999 1.00 64.26 ? 2113 HOH A O 1 HETATM 3293 O O . HOH N 6 . ? -2.630 17.924 15.096 1.00 55.76 ? 2114 HOH A O 1 HETATM 3294 O O . HOH N 6 . ? 3.311 30.784 -9.767 1.00 68.34 ? 2115 HOH A O 1 HETATM 3295 O O . HOH N 6 . ? 21.432 67.325 -15.665 1.00 68.72 ? 2116 HOH A O 1 HETATM 3296 O O . HOH N 6 . ? 24.379 67.793 -13.994 1.00 70.48 ? 2117 HOH A O 1 HETATM 3297 O O . HOH N 6 . ? 19.592 67.710 -6.253 1.00 83.81 ? 2118 HOH A O 1 HETATM 3298 O O . HOH N 6 . ? 13.482 37.517 35.967 1.00 58.23 ? 2119 HOH A O 1 HETATM 3299 O O . HOH N 6 . ? 15.773 35.238 37.097 1.00 40.76 ? 2120 HOH A O 1 HETATM 3300 O O . HOH N 6 . ? 6.983 34.080 23.637 1.00 36.90 ? 2121 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 GLN 1 4 4 GLN GLN A . n A 1 2 ALA 2 5 5 ALA ALA A . n A 1 3 VAL 3 6 6 VAL VAL A . n A 1 4 GLN 4 7 7 GLN GLN A . n A 1 5 PRO 5 8 8 PRO PRO A . n A 1 6 VAL 6 9 9 VAL VAL A . n A 1 7 ASP 7 10 10 ASP ASP A . n A 1 8 PHE 8 11 11 PHE PHE A . n A 1 9 ARG 9 12 12 ARG ARG A . n A 1 10 HIS 10 13 13 HIS HIS A . n A 1 11 HIS 11 14 14 HIS HIS A . n A 1 12 HIS 12 15 15 HIS HIS A . n A 1 13 PHE 13 16 16 PHE PHE A . n A 1 14 SER 14 17 17 SER SER A . n A 1 15 ASP 15 18 18 ASP ASP A . n A 1 16 MET 16 19 19 MET MET A . n A 1 17 GLU 17 20 20 GLU GLU A . n A 1 18 ILE 18 21 21 ILE ILE A . n A 1 19 PHE 19 22 22 PHE PHE A . n A 1 20 LEU 20 23 23 LEU LEU A . n A 1 21 ARG 21 24 24 ARG ARG A . n A 1 22 ARG 22 25 25 ARG ARG A . n A 1 23 TYR 23 26 26 TYR TYR A . n A 1 24 ALA 24 27 27 ALA ALA A . n A 1 25 ASN 25 28 28 ASN ASN A . n A 1 26 GLU 26 29 29 GLU GLU A . n A 1 27 TYR 27 30 30 TYR TYR A . n A 1 28 PRO 28 31 31 PRO PRO A . n A 1 29 SER 29 32 32 SER SER A . n A 1 30 ILE 30 33 33 ILE ILE A . n A 1 31 THR 31 34 34 THR THR A . n A 1 32 ARG 32 35 35 ARG ARG A . n A 1 33 LEU 33 36 36 LEU LEU A . n A 1 34 TYR 34 37 37 TYR TYR A . n A 1 35 SER 35 38 38 SER SER A . n A 1 36 VAL 36 39 39 VAL VAL A . n A 1 37 GLY 37 40 40 GLY GLY A . n A 1 38 LYS 38 41 41 LYS LYS A . n A 1 39 SER 39 42 42 SER SER A . n A 1 40 VAL 40 43 43 VAL VAL A . n A 1 41 GLU 41 44 44 GLU GLU A . n A 1 42 LEU 42 45 45 LEU LEU A . n A 1 43 ARG 43 46 46 ARG ARG A . n A 1 44 GLU 44 47 47 GLU GLU A . n A 1 45 LEU 45 48 48 LEU LEU A . n A 1 46 TYR 46 49 49 TYR TYR A . n A 1 47 VAL 47 50 50 VAL VAL A . n A 1 48 MET 48 51 51 MET MET A . n A 1 49 GLU 49 52 52 GLU GLU A . n A 1 50 ILE 50 53 53 ILE ILE A . n A 1 51 SER 51 54 54 SER SER A . n A 1 52 ASP 52 55 55 ASP ASP A . n A 1 53 ASN 53 56 56 ASN ASN A . n A 1 54 PRO 54 57 57 PRO PRO A . n A 1 55 GLY 55 58 58 GLY GLY A . n A 1 56 ILE 56 59 59 ILE ILE A . n A 1 57 HIS 57 60 60 HIS HIS A . n A 1 58 GLU 58 61 61 GLU GLU A . n A 1 59 ALA 59 62 62 ALA ALA A . n A 1 60 GLY 60 63 63 GLY GLY A . n A 1 61 GLU 61 64 64 GLU GLU A . n A 1 62 PRO 62 65 65 PRO PRO A . n A 1 63 GLU 63 66 66 GLU GLU A . n A 1 64 PHE 64 67 67 PHE PHE A . n A 1 65 LYS 65 68 68 LYS LYS A . n A 1 66 TYR 66 69 69 TYR TYR A . n A 1 67 ILE 67 70 70 ILE ILE A . n A 1 68 GLY 68 71 71 GLY GLY A . n A 1 69 ASN 69 72 72 ASN ASN A . n A 1 70 MET 70 73 73 MET MET A . n A 1 71 HIS 71 74 74 HIS HIS A . n A 1 72 GLY 72 75 75 GLY GLY A . n A 1 73 ASN 73 76 76 ASN ASN A . n A 1 74 GLU 74 77 77 GLU GLU A . n A 1 75 VAL 75 78 78 VAL VAL A . n A 1 76 VAL 76 79 79 VAL VAL A . n A 1 77 GLY 77 80 80 GLY GLY A . n A 1 78 ARG 78 81 81 ARG ARG A . n A 1 79 GLU 79 82 82 GLU GLU A . n A 1 80 LEU 80 83 83 LEU LEU A . n A 1 81 LEU 81 84 84 LEU LEU A . n A 1 82 LEU 82 85 85 LEU LEU A . n A 1 83 ASN 83 86 86 ASN ASN A . n A 1 84 LEU 84 87 87 LEU LEU A . n A 1 85 ILE 85 88 88 ILE ILE A . n A 1 86 GLU 86 89 89 GLU GLU A . n A 1 87 TYR 87 90 90 TYR TYR A . n A 1 88 LEU 88 91 91 LEU LEU A . n A 1 89 CYS 89 92 92 CYS CYS A . n A 1 90 LYS 90 93 93 LYS LYS A . n A 1 91 ASN 91 94 94 ASN ASN A . n A 1 92 PHE 92 95 95 PHE PHE A . n A 1 93 GLY 93 96 96 GLY GLY A . n A 1 94 THR 94 97 97 THR THR A . n A 1 95 ASP 95 98 98 ASP ASP A . n A 1 96 PRO 96 99 99 PRO PRO A . n A 1 97 GLU 97 100 100 GLU GLU A . n A 1 98 VAL 98 101 101 VAL VAL A . n A 1 99 THR 99 102 102 THR THR A . n A 1 100 ASP 100 103 103 ASP ASP A . n A 1 101 LEU 101 104 104 LEU LEU A . n A 1 102 VAL 102 105 105 VAL VAL A . n A 1 103 GLN 103 106 106 GLN GLN A . n A 1 104 SER 104 107 107 SER SER A . n A 1 105 THR 105 108 108 THR THR A . n A 1 106 ARG 106 109 109 ARG ARG A . n A 1 107 ILE 107 110 110 ILE ILE A . n A 1 108 HIS 108 111 111 HIS HIS A . n A 1 109 ILE 109 112 112 ILE ILE A . n A 1 110 MET 110 113 113 MET MET A . n A 1 111 PRO 111 114 114 PRO PRO A . n A 1 112 SER 112 115 115 SER SER A . n A 1 113 MET 113 116 116 MET MET A . n A 1 114 ASN 114 117 117 ASN ASN A . n A 1 115 PRO 115 118 118 PRO PRO A . n A 1 116 ASP 116 119 119 ASP ASP A . n A 1 117 GLY 117 120 120 GLY GLY A . n A 1 118 TYR 118 121 121 TYR TYR A . n A 1 119 GLU 119 122 122 GLU GLU A . n A 1 120 LYS 120 123 123 LYS LYS A . n A 1 121 SER 121 124 124 SER SER A . n A 1 122 GLN 122 125 125 GLN GLN A . n A 1 123 GLU 123 126 126 GLU GLU A . n A 1 124 GLY 124 127 127 GLY GLY A . n A 1 125 ASP 125 128 128 ASP ASP A . n A 1 126 ARG 126 129 129 ARG ARG A . n A 1 127 GLY 127 130 130 GLY GLY A . n A 1 128 GLY 128 131 131 GLY GLY A . n A 1 129 THR 129 132 132 THR THR A . n A 1 130 VAL 130 133 133 VAL VAL A . n A 1 131 GLY 131 134 134 GLY GLY A . n A 1 132 ARG 132 135 135 ARG ARG A . n A 1 133 ASN 133 136 136 ASN ASN A . n A 1 134 ASN 134 137 137 ASN ASN A . n A 1 135 SER 135 138 138 SER SER A . n A 1 136 ASN 136 139 139 ASN ASN A . n A 1 137 ASN 137 140 140 ASN ASN A . n A 1 138 TYR 138 141 141 TYR TYR A . n A 1 139 ASP 139 142 142 ASP ASP A . n A 1 140 LEU 140 143 143 LEU LEU A . n A 1 141 ASN 141 144 144 ASN ASN A . n A 1 142 ARG 142 145 145 ARG ARG A . n A 1 143 ASN 143 146 146 ASN ASN A . n A 1 144 PHE 144 147 147 PHE PHE A . n A 1 145 PRO 145 148 148 PRO PRO A . n A 1 146 ASP 146 149 149 ASP ASP A . n A 1 147 GLN 147 150 150 GLN GLN A . n A 1 148 PHE 148 151 151 PHE PHE A . n A 1 149 PHE 149 152 152 PHE PHE A . n A 1 150 GLN 150 153 153 GLN GLN A . n A 1 151 VAL 151 154 154 VAL VAL A . n A 1 152 THR 152 155 155 THR THR A . n A 1 153 ASP 153 156 156 ASP ASP A . n A 1 154 PRO 154 157 157 PRO PRO A . n A 1 155 PRO 155 158 158 PRO PRO A . n A 1 156 GLN 156 159 159 GLN GLN A . n A 1 157 PRO 157 160 160 PRO PRO A . n A 1 158 GLU 158 161 161 GLU GLU A . n A 1 159 THR 159 162 162 THR THR A . n A 1 160 LEU 160 163 163 LEU LEU A . n A 1 161 ALA 161 164 164 ALA ALA A . n A 1 162 VAL 162 165 165 VAL VAL A . n A 1 163 MET 163 166 166 MET MET A . n A 1 164 SER 164 167 167 SER SER A . n A 1 165 TRP 165 168 168 TRP TRP A . n A 1 166 LEU 166 169 169 LEU LEU A . n A 1 167 LYS 167 170 170 LYS LYS A . n A 1 168 THR 168 171 171 THR THR A . n A 1 169 TYR 169 172 172 TYR TYR A . n A 1 170 PRO 170 173 173 PRO PRO A . n A 1 171 PHE 171 174 174 PHE PHE A . n A 1 172 VAL 172 175 175 VAL VAL A . n A 1 173 LEU 173 176 176 LEU LEU A . n A 1 174 SER 174 177 177 SER SER A . n A 1 175 ALA 175 178 178 ALA ALA A . n A 1 176 ASN 176 179 179 ASN ASN A . n A 1 177 LEU 177 180 180 LEU LEU A . n A 1 178 HIS 178 181 181 HIS HIS A . n A 1 179 GLY 179 182 182 GLY GLY A . n A 1 180 GLY 180 183 183 GLY GLY A . n A 1 181 SER 181 184 184 SER SER A . n A 1 182 LEU 182 185 185 LEU LEU A . n A 1 183 VAL 183 186 186 VAL VAL A . n A 1 184 VAL 184 187 187 VAL VAL A . n A 1 185 ASN 185 188 188 ASN ASN A . n A 1 186 TYR 186 189 189 TYR TYR A . n A 1 187 PRO 187 190 190 PRO PRO A . n A 1 188 PHE 188 191 191 PHE PHE A . n A 1 189 ASP 189 192 192 ASP ASP A . n A 1 190 ASP 190 193 193 ASP ASP A . n A 1 191 ASP 191 194 194 ASP ASP A . n A 1 192 GLU 192 195 195 GLU GLU A . n A 1 193 GLN 193 196 196 GLN GLN A . n A 1 194 GLY 194 197 197 GLY GLY A . n A 1 195 ILE 195 198 198 ILE ILE A . n A 1 196 ALA 196 199 199 ALA ALA A . n A 1 197 ILE 197 200 200 ILE ILE A . n A 1 198 TYR 198 201 201 TYR TYR A . n A 1 199 SER 199 202 202 SER SER A . n A 1 200 LYS 200 203 203 LYS LYS A . n A 1 201 SER 201 204 204 SER SER A . n A 1 202 PRO 202 205 205 PRO PRO A . n A 1 203 ASP 203 206 206 ASP ASP A . n A 1 204 ASP 204 207 207 ASP ASP A . n A 1 205 ALA 205 208 208 ALA ALA A . n A 1 206 VAL 206 209 209 VAL VAL A . n A 1 207 PHE 207 210 210 PHE PHE A . n A 1 208 GLN 208 211 211 GLN GLN A . n A 1 209 GLN 209 212 212 GLN GLN A . n A 1 210 LEU 210 213 213 LEU LEU A . n A 1 211 ALA 211 214 214 ALA ALA A . n A 1 212 LEU 212 215 215 LEU LEU A . n A 1 213 SER 213 216 216 SER SER A . n A 1 214 TYR 214 217 217 TYR TYR A . n A 1 215 SER 215 218 218 SER SER A . n A 1 216 LYS 216 219 219 LYS LYS A . n A 1 217 GLU 217 220 220 GLU GLU A . n A 1 218 ASN 218 221 221 ASN ASN A . n A 1 219 LYS 219 222 222 LYS LYS A . n A 1 220 LYS 220 223 223 LYS LYS A . n A 1 221 MET 221 224 224 MET MET A . n A 1 222 TYR 222 225 225 TYR TYR A . n A 1 223 GLN 223 226 226 GLN GLN A . n A 1 224 GLY 224 227 227 GLY GLY A . n A 1 225 SER 225 228 228 SER SER A . n A 1 226 PRO 226 229 229 PRO PRO A . n A 1 227 CYS 227 230 230 CYS CYS A . n A 1 228 LYS 228 231 231 LYS LYS A . n A 1 229 ASP 229 232 232 ASP ASP A . n A 1 230 LEU 230 233 233 LEU LEU A . n A 1 231 TYR 231 234 234 TYR TYR A . n A 1 232 PRO 232 235 235 PRO PRO A . n A 1 233 THR 233 236 236 THR THR A . n A 1 234 GLU 234 237 237 GLU GLU A . n A 1 235 TYR 235 238 238 TYR TYR A . n A 1 236 PHE 236 239 239 PHE PHE A . n A 1 237 PRO 237 240 240 PRO PRO A . n A 1 238 HIS 238 241 241 HIS HIS A . n A 1 239 GLY 239 242 242 GLY GLY A . n A 1 240 ILE 240 243 243 ILE ILE A . n A 1 241 THR 241 244 244 THR THR A . n A 1 242 ASN 242 245 245 ASN ASN A . n A 1 243 GLY 243 246 246 GLY GLY A . n A 1 244 ALA 244 247 247 ALA ALA A . n A 1 245 GLN 245 248 248 GLN GLN A . n A 1 246 TRP 246 249 249 TRP TRP A . n A 1 247 TYR 247 250 250 TYR TYR A . n A 1 248 ASN 248 251 251 ASN ASN A . n A 1 249 VAL 249 252 252 VAL VAL A . n A 1 250 PRO 250 253 253 PRO PRO A . n A 1 251 GLY 251 254 254 GLY GLY A . n A 1 252 GLY 252 255 255 GLY GLY A . n A 1 253 MET 253 256 256 MET MET A . n A 1 254 GLN 254 257 257 GLN GLN A . n A 1 255 ASP 255 258 258 ASP ASP A . n A 1 256 TRP 256 259 259 TRP TRP A . n A 1 257 ASN 257 260 260 ASN ASN A . n A 1 258 TYR 258 261 261 TYR TYR A . n A 1 259 LEU 259 262 262 LEU LEU A . n A 1 260 ASN 260 263 263 ASN ASN A . n A 1 261 THR 261 264 264 THR THR A . n A 1 262 ASN 262 265 265 ASN ASN A . n A 1 263 CYS 263 266 266 CYS CYS A . n A 1 264 PHE 264 267 267 PHE PHE A . n A 1 265 GLU 265 268 268 GLU GLU A . n A 1 266 VAL 266 269 269 VAL VAL A . n A 1 267 THR 267 270 270 THR THR A . n A 1 268 ILE 268 271 271 ILE ILE A . n A 1 269 GLU 269 272 272 GLU GLU A . n A 1 270 LEU 270 273 273 LEU LEU A . n A 1 271 GLY 271 274 274 GLY GLY A . n A 1 272 CYS 272 275 275 CYS CYS A . n A 1 273 VAL 273 276 276 VAL VAL A . n A 1 274 LYS 274 277 277 LYS LYS A . n A 1 275 TYR 275 278 278 TYR TYR A . n A 1 276 PRO 276 279 279 PRO PRO A . n A 1 277 LYS 277 280 280 LYS LYS A . n A 1 278 ALA 278 281 281 ALA ALA A . n A 1 279 GLU 279 282 282 GLU GLU A . n A 1 280 GLU 280 283 283 GLU GLU A . n A 1 281 LEU 281 284 284 LEU LEU A . n A 1 282 PRO 282 285 285 PRO PRO A . n A 1 283 LYS 283 286 286 LYS LYS A . n A 1 284 TYR 284 287 287 TYR TYR A . n A 1 285 TRP 285 288 288 TRP TRP A . n A 1 286 GLU 286 289 289 GLU GLU A . n A 1 287 GLN 287 290 290 GLN GLN A . n A 1 288 ASN 288 291 291 ASN ASN A . n A 1 289 ARG 289 292 292 ARG ARG A . n A 1 290 ARG 290 293 293 ARG ARG A . n A 1 291 SER 291 294 294 SER SER A . n A 1 292 LEU 292 295 295 LEU LEU A . n A 1 293 LEU 293 296 296 LEU LEU A . n A 1 294 GLN 294 297 297 GLN GLN A . n A 1 295 PHE 295 298 298 PHE PHE A . n A 1 296 ILE 296 299 299 ILE ILE A . n A 1 297 LYS 297 300 300 LYS LYS A . n A 1 298 GLN 298 301 301 GLN GLN A . n A 1 299 VAL 299 302 302 VAL VAL A . n A 1 300 HIS 300 303 303 HIS HIS A . n A 1 301 ARG 301 304 304 ARG ARG A . n A 1 302 GLY 302 305 305 GLY GLY A . n A 1 303 ILE 303 306 306 ILE ILE A . n A 1 304 TRP 304 307 307 TRP TRP A . n A 1 305 GLY 305 308 308 GLY GLY A . n A 1 306 PHE 306 309 309 PHE PHE A . n A 1 307 VAL 307 310 310 VAL VAL A . n A 1 308 LEU 308 311 311 LEU LEU A . n A 1 309 ASP 309 312 312 ASP ASP A . n A 1 310 ALA 310 313 313 ALA ALA A . n A 1 311 THR 311 314 314 THR THR A . n A 1 312 ASP 312 315 315 ASP ASP A . n A 1 313 GLY 313 316 316 GLY GLY A . n A 1 314 ARG 314 317 317 ARG ARG A . n A 1 315 GLY 315 318 318 GLY GLY A . n A 1 316 ILE 316 319 319 ILE ILE A . n A 1 317 LEU 317 320 320 LEU LEU A . n A 1 318 ASN 318 321 321 ASN ASN A . n A 1 319 ALA 319 322 322 ALA ALA A . n A 1 320 THR 320 323 323 THR THR A . n A 1 321 ILE 321 324 324 ILE ILE A . n A 1 322 SER 322 325 325 SER SER A . n A 1 323 VAL 323 326 326 VAL VAL A . n A 1 324 ALA 324 327 327 ALA ALA A . n A 1 325 ASP 325 328 328 ASP ASP A . n A 1 326 ILE 326 329 329 ILE ILE A . n A 1 327 ASN 327 330 330 ASN ASN A . n A 1 328 HIS 328 331 331 HIS HIS A . n A 1 329 PRO 329 332 332 PRO PRO A . n A 1 330 VAL 330 333 333 VAL VAL A . n A 1 331 THR 331 334 334 THR THR A . n A 1 332 THR 332 335 335 THR THR A . n A 1 333 TYR 333 336 336 TYR TYR A . n A 1 334 LYS 334 337 337 LYS LYS A . n A 1 335 ASP 335 338 338 ASP ASP A . n A 1 336 GLY 336 339 339 GLY GLY A . n A 1 337 ASP 337 340 340 ASP ASP A . n A 1 338 TYR 338 341 341 TYR TYR A . n A 1 339 TRP 339 342 342 TRP TRP A . n A 1 340 ARG 340 343 343 ARG ARG A . n A 1 341 LEU 341 344 344 LEU LEU A . n A 1 342 LEU 342 345 345 LEU LEU A . n A 1 343 VAL 343 346 346 VAL VAL A . n A 1 344 GLN 344 347 347 GLN GLN A . n A 1 345 GLY 345 348 348 GLY GLY A . n A 1 346 THR 346 349 349 THR THR A . n A 1 347 TYR 347 350 350 TYR TYR A . n A 1 348 LYS 348 351 351 LYS LYS A . n A 1 349 VAL 349 352 352 VAL VAL A . n A 1 350 THR 350 353 353 THR THR A . n A 1 351 ALA 351 354 354 ALA ALA A . n A 1 352 SER 352 355 355 SER SER A . n A 1 353 ALA 353 356 356 ALA ALA A . n A 1 354 ARG 354 357 357 ARG ARG A . n A 1 355 GLY 355 358 358 GLY GLY A . n A 1 356 TYR 356 359 359 TYR TYR A . n A 1 357 ASP 357 360 360 ASP ASP A . n A 1 358 PRO 358 361 361 PRO PRO A . n A 1 359 VAL 359 362 362 VAL VAL A . n A 1 360 THR 360 363 363 THR THR A . n A 1 361 LYS 361 364 364 LYS LYS A . n A 1 362 THR 362 365 365 THR THR A . n A 1 363 VAL 363 366 366 VAL VAL A . n A 1 364 GLU 364 367 367 GLU GLU A . n A 1 365 VAL 365 368 368 VAL VAL A . n A 1 366 ASP 366 369 369 ASP ASP A . n A 1 367 SER 367 370 370 SER SER A . n A 1 368 LYS 368 371 371 LYS LYS A . n A 1 369 GLY 369 372 372 GLY GLY A . n A 1 370 GLY 370 373 373 GLY GLY A . n A 1 371 VAL 371 374 374 VAL VAL A . n A 1 372 GLN 372 375 375 GLN GLN A . n A 1 373 VAL 373 376 376 VAL VAL A . n A 1 374 ASN 374 377 377 ASN ASN A . n A 1 375 PHE 375 378 378 PHE PHE A . n A 1 376 THR 376 379 379 THR THR A . n A 1 377 LEU 377 380 380 LEU LEU A . n A 1 378 SER 378 381 381 SER SER A . n A 1 379 ARG 379 382 382 ARG ARG A . n A 1 380 THR 380 383 383 THR THR A . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code B 2 NAG 1 901 901 NAG NAG A . C 2 NAG 2 902 902 NAG NAG A . D 3 MAN 3 903 903 MAN MAN A . E 2 NAG 1 911 911 NAG NAG A . F 2 NAG 2 912 912 NAG NAG A . G 2 NAG 1 921 921 NAG NAG A . H 2 NAG 2 922 922 NAG NAG A . I 3 MAN 3 923 923 MAN MAN A . J 4 SO4 1 996 996 SO4 SO4 A . K 4 SO4 1 997 997 SO4 SO4 A . L 4 SO4 1 998 998 SO4 SO4 A . M 5 ZN 1 999 999 ZN ZN A . N 6 HOH 1 2001 2001 HOH HOH A . N 6 HOH 2 2002 2002 HOH HOH A . N 6 HOH 3 2003 2003 HOH HOH A . N 6 HOH 4 2004 2004 HOH HOH A . N 6 HOH 5 2005 2005 HOH HOH A . N 6 HOH 6 2006 2006 HOH HOH A . N 6 HOH 7 2007 2007 HOH HOH A . N 6 HOH 8 2008 2008 HOH HOH A . N 6 HOH 9 2009 2009 HOH HOH A . N 6 HOH 10 2010 2010 HOH HOH A . N 6 HOH 11 2011 2011 HOH HOH A . N 6 HOH 12 2012 2012 HOH HOH A . N 6 HOH 13 2013 2013 HOH HOH A . N 6 HOH 14 2014 2014 HOH HOH A . N 6 HOH 15 2015 2015 HOH HOH A . N 6 HOH 16 2016 2016 HOH HOH A . N 6 HOH 17 2017 2017 HOH HOH A . N 6 HOH 18 2018 2018 HOH HOH A . N 6 HOH 19 2019 2019 HOH HOH A . N 6 HOH 20 2020 2020 HOH HOH A . N 6 HOH 21 2021 2021 HOH HOH A . N 6 HOH 22 2022 2022 HOH HOH A . N 6 HOH 23 2023 2023 HOH HOH A . N 6 HOH 24 2024 2024 HOH HOH A . N 6 HOH 25 2025 2025 HOH HOH A . N 6 HOH 26 2026 2026 HOH HOH A . N 6 HOH 27 2027 2027 HOH HOH A . N 6 HOH 28 2028 2028 HOH HOH A . N 6 HOH 29 2029 2029 HOH HOH A . N 6 HOH 30 2030 2030 HOH HOH A . N 6 HOH 31 2031 2031 HOH HOH A . N 6 HOH 32 2032 2032 HOH HOH A . N 6 HOH 33 2033 2033 HOH HOH A . N 6 HOH 34 2034 2034 HOH HOH A . N 6 HOH 35 2035 2035 HOH HOH A . N 6 HOH 36 2036 2036 HOH HOH A . N 6 HOH 37 2037 2037 HOH HOH A . N 6 HOH 38 2038 2038 HOH HOH A . N 6 HOH 39 2039 2039 HOH HOH A . N 6 HOH 40 2040 2040 HOH HOH A . N 6 HOH 41 2041 2041 HOH HOH A . N 6 HOH 42 2042 2042 HOH HOH A . N 6 HOH 43 2043 2043 HOH HOH A . N 6 HOH 44 2044 2044 HOH HOH A . N 6 HOH 45 2045 2045 HOH HOH A . N 6 HOH 46 2046 2046 HOH HOH A . N 6 HOH 47 2047 2047 HOH HOH A . N 6 HOH 48 2048 2048 HOH HOH A . N 6 HOH 49 2049 2049 HOH HOH A . N 6 HOH 50 2050 2050 HOH HOH A . N 6 HOH 51 2051 2051 HOH HOH A . N 6 HOH 52 2052 2052 HOH HOH A . N 6 HOH 53 2053 2053 HOH HOH A . N 6 HOH 54 2054 2054 HOH HOH A . N 6 HOH 55 2055 2055 HOH HOH A . N 6 HOH 56 2056 2056 HOH HOH A . N 6 HOH 57 2057 2057 HOH HOH A . N 6 HOH 58 2058 2058 HOH HOH A . N 6 HOH 59 2059 2059 HOH HOH A . N 6 HOH 60 2060 2060 HOH HOH A . N 6 HOH 61 2061 2061 HOH HOH A . N 6 HOH 62 2062 2062 HOH HOH A . N 6 HOH 63 2063 2063 HOH HOH A . N 6 HOH 64 2064 2064 HOH HOH A . N 6 HOH 65 2065 2065 HOH HOH A . N 6 HOH 66 2066 2066 HOH HOH A . N 6 HOH 67 2067 2067 HOH HOH A . N 6 HOH 68 2068 2068 HOH HOH A . N 6 HOH 69 2069 2069 HOH HOH A . N 6 HOH 70 2070 2070 HOH HOH A . N 6 HOH 71 2071 2071 HOH HOH A . N 6 HOH 72 2072 2072 HOH HOH A . N 6 HOH 73 2073 2073 HOH HOH A . N 6 HOH 74 2074 2074 HOH HOH A . N 6 HOH 75 2075 2075 HOH HOH A . N 6 HOH 76 2076 2076 HOH HOH A . N 6 HOH 77 2077 2077 HOH HOH A . N 6 HOH 78 2078 2078 HOH HOH A . N 6 HOH 79 2079 2079 HOH HOH A . N 6 HOH 80 2080 2080 HOH HOH A . N 6 HOH 81 2081 2081 HOH HOH A . N 6 HOH 82 2082 2082 HOH HOH A . N 6 HOH 83 2083 2083 HOH HOH A . N 6 HOH 84 2084 2084 HOH HOH A . N 6 HOH 85 2085 2085 HOH HOH A . N 6 HOH 86 2086 2086 HOH HOH A . N 6 HOH 87 2087 2087 HOH HOH A . N 6 HOH 88 2088 2088 HOH HOH A . N 6 HOH 89 2089 2089 HOH HOH A . N 6 HOH 90 2090 2090 HOH HOH A . N 6 HOH 91 2091 2091 HOH HOH A . N 6 HOH 92 2092 2092 HOH HOH A . N 6 HOH 93 2093 2093 HOH HOH A . N 6 HOH 94 2094 2094 HOH HOH A . N 6 HOH 95 2095 2095 HOH HOH A . N 6 HOH 96 2096 2096 HOH HOH A . N 6 HOH 97 2097 2097 HOH HOH A . N 6 HOH 98 2098 2098 HOH HOH A . N 6 HOH 99 2099 2099 HOH HOH A . N 6 HOH 100 2100 2100 HOH HOH A . N 6 HOH 101 2101 2101 HOH HOH A . N 6 HOH 102 2102 2102 HOH HOH A . N 6 HOH 103 2103 2103 HOH HOH A . N 6 HOH 104 2104 2104 HOH HOH A . N 6 HOH 105 2105 2105 HOH HOH A . N 6 HOH 106 2106 2106 HOH HOH A . N 6 HOH 107 2107 2107 HOH HOH A . N 6 HOH 108 2108 2108 HOH HOH A . N 6 HOH 109 2109 2109 HOH HOH A . N 6 HOH 110 2110 2110 HOH HOH A . N 6 HOH 111 2111 2111 HOH HOH A . N 6 HOH 112 2112 2112 HOH HOH A . N 6 HOH 113 2113 2113 HOH HOH A . N 6 HOH 114 2114 2114 HOH HOH A . N 6 HOH 115 2115 2115 HOH HOH A . N 6 HOH 116 2116 2116 HOH HOH A . N 6 HOH 117 2117 2117 HOH HOH A . N 6 HOH 118 2118 2118 HOH HOH A . N 6 HOH 119 2119 2119 HOH HOH A . N 6 HOH 120 2120 2120 HOH HOH A . N 6 HOH 121 2121 2121 HOH HOH A . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 133 A ASN 136 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 318 A ASN 321 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 374 A ASN 377 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details software_defined_assembly _pdbx_struct_assembly.method_details PQS _pdbx_struct_assembly.oligomeric_details trimeric _pdbx_struct_assembly.oligomeric_count 3 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1,2,3 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 1 'ABSA (A^2)' 3230 ? 1 MORE -0.3 ? 1 'SSA (A^2)' 55770 ? # loop_ _pdbx_struct_oper_list.id _pdbx_struct_oper_list.type _pdbx_struct_oper_list.name _pdbx_struct_oper_list.symmetry_operation _pdbx_struct_oper_list.matrix[1][1] _pdbx_struct_oper_list.matrix[1][2] _pdbx_struct_oper_list.matrix[1][3] _pdbx_struct_oper_list.vector[1] _pdbx_struct_oper_list.matrix[2][1] _pdbx_struct_oper_list.matrix[2][2] _pdbx_struct_oper_list.matrix[2][3] _pdbx_struct_oper_list.vector[2] _pdbx_struct_oper_list.matrix[3][1] _pdbx_struct_oper_list.matrix[3][2] _pdbx_struct_oper_list.matrix[3][3] _pdbx_struct_oper_list.vector[3] 1 'identity operation' 1_555 x,y,z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 2 'crystal symmetry operation' 8_555 -z,x+1/2,-y+1/2 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 67.7700000000 0.0000000000 -1.0000000000 0.0000000000 67.7700000000 3 'crystal symmetry operation' 11_455 y-1/2,-z+1/2,-x 0.0000000000 1.0000000000 0.0000000000 -67.7700000000 0.0000000000 0.0000000000 -1.0000000000 67.7700000000 -1.0000000000 0.0000000000 0.0000000000 0.0000000000 # loop_ _pdbx_struct_conn_angle.id _pdbx_struct_conn_angle.ptnr1_label_atom_id _pdbx_struct_conn_angle.ptnr1_label_alt_id _pdbx_struct_conn_angle.ptnr1_label_asym_id _pdbx_struct_conn_angle.ptnr1_label_comp_id _pdbx_struct_conn_angle.ptnr1_label_seq_id _pdbx_struct_conn_angle.ptnr1_auth_atom_id _pdbx_struct_conn_angle.ptnr1_auth_asym_id _pdbx_struct_conn_angle.ptnr1_auth_comp_id _pdbx_struct_conn_angle.ptnr1_auth_seq_id _pdbx_struct_conn_angle.ptnr1_PDB_ins_code _pdbx_struct_conn_angle.ptnr1_symmetry _pdbx_struct_conn_angle.ptnr2_label_atom_id _pdbx_struct_conn_angle.ptnr2_label_alt_id _pdbx_struct_conn_angle.ptnr2_label_asym_id _pdbx_struct_conn_angle.ptnr2_label_comp_id _pdbx_struct_conn_angle.ptnr2_label_seq_id _pdbx_struct_conn_angle.ptnr2_auth_atom_id _pdbx_struct_conn_angle.ptnr2_auth_asym_id _pdbx_struct_conn_angle.ptnr2_auth_comp_id _pdbx_struct_conn_angle.ptnr2_auth_seq_id _pdbx_struct_conn_angle.ptnr2_PDB_ins_code _pdbx_struct_conn_angle.ptnr2_symmetry _pdbx_struct_conn_angle.ptnr3_label_atom_id _pdbx_struct_conn_angle.ptnr3_label_alt_id _pdbx_struct_conn_angle.ptnr3_label_asym_id _pdbx_struct_conn_angle.ptnr3_label_comp_id _pdbx_struct_conn_angle.ptnr3_label_seq_id _pdbx_struct_conn_angle.ptnr3_auth_atom_id _pdbx_struct_conn_angle.ptnr3_auth_asym_id _pdbx_struct_conn_angle.ptnr3_auth_comp_id _pdbx_struct_conn_angle.ptnr3_auth_seq_id _pdbx_struct_conn_angle.ptnr3_PDB_ins_code _pdbx_struct_conn_angle.ptnr3_symmetry _pdbx_struct_conn_angle.value _pdbx_struct_conn_angle.value_esd 1 ND1 ? A HIS 178 ? A HIS 181 ? 1_555 ZN ? M ZN . ? A ZN 999 ? 1_555 OE1 ? A GLU 74 ? A GLU 77 ? 1_555 77.1 ? 2 ND1 ? A HIS 178 ? A HIS 181 ? 1_555 ZN ? M ZN . ? A ZN 999 ? 1_555 OE2 ? A GLU 74 ? A GLU 77 ? 1_555 134.4 ? 3 OE1 ? A GLU 74 ? A GLU 77 ? 1_555 ZN ? M ZN . ? A ZN 999 ? 1_555 OE2 ? A GLU 74 ? A GLU 77 ? 1_555 57.6 ? 4 ND1 ? A HIS 178 ? A HIS 181 ? 1_555 ZN ? M ZN . ? A ZN 999 ? 1_555 O ? N HOH . ? A HOH 2121 ? 1_555 129.4 ? 5 OE1 ? A GLU 74 ? A GLU 77 ? 1_555 ZN ? M ZN . ? A ZN 999 ? 1_555 O ? N HOH . ? A HOH 2121 ? 1_555 118.8 ? 6 OE2 ? A GLU 74 ? A GLU 77 ? 1_555 ZN ? M ZN . ? A ZN 999 ? 1_555 O ? N HOH . ? A HOH 2121 ? 1_555 82.0 ? 7 ND1 ? A HIS 178 ? A HIS 181 ? 1_555 ZN ? M ZN . ? A ZN 999 ? 1_555 ND1 ? A HIS 71 ? A HIS 74 ? 1_555 91.0 ? 8 OE1 ? A GLU 74 ? A GLU 77 ? 1_555 ZN ? M ZN . ? A ZN 999 ? 1_555 ND1 ? A HIS 71 ? A HIS 74 ? 1_555 90.0 ? 9 OE2 ? A GLU 74 ? A GLU 77 ? 1_555 ZN ? M ZN . ? A ZN 999 ? 1_555 ND1 ? A HIS 71 ? A HIS 74 ? 1_555 84.4 ? 10 O ? N HOH . ? A HOH 2121 ? 1_555 ZN ? M ZN . ? A ZN 999 ? 1_555 ND1 ? A HIS 71 ? A HIS 74 ? 1_555 132.8 ? # 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 2000-10-13 2 'Structure model' 1 1 2011-05-08 3 'Structure model' 1 2 2011-07-13 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Version format compliance' 2 3 'Structure model' 'Version format compliance' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal CNS refinement 0.4 ? 1 MOSFLM 'data reduction' . ? 2 SCALA 'data scaling' . ? 3 CNS phasing 0.4 ? 4 # _pdbx_validate_close_contact.id 1 _pdbx_validate_close_contact.PDB_model_num 1 _pdbx_validate_close_contact.auth_atom_id_1 ND2 _pdbx_validate_close_contact.auth_asym_id_1 A _pdbx_validate_close_contact.auth_comp_id_1 ASN _pdbx_validate_close_contact.auth_seq_id_1 377 _pdbx_validate_close_contact.PDB_ins_code_1 ? _pdbx_validate_close_contact.label_alt_id_1 ? _pdbx_validate_close_contact.auth_atom_id_2 O7 _pdbx_validate_close_contact.auth_asym_id_2 A _pdbx_validate_close_contact.auth_comp_id_2 NAG _pdbx_validate_close_contact.auth_seq_id_2 921 _pdbx_validate_close_contact.PDB_ins_code_2 ? _pdbx_validate_close_contact.label_alt_id_2 ? _pdbx_validate_close_contact.dist 2.16 # 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 VAL A 9 ? ? -137.45 -34.19 2 1 ASP A 10 ? ? -68.91 70.78 3 1 ASN A 56 ? ? -150.21 60.72 4 1 GLU A 89 ? ? -52.05 -71.10 5 1 PHE A 151 ? ? -106.50 -64.83 6 1 PRO A 173 ? ? -76.08 46.94 7 1 CYS A 230 ? ? -169.10 90.95 8 1 TYR A 250 ? ? -173.38 140.36 9 1 ASN A 321 ? ? 77.80 34.63 10 1 ALA A 327 ? ? -6.66 -107.29 11 1 HIS A 331 ? ? -156.07 85.52 12 1 ALA A 356 ? ? 177.07 129.72 13 1 ASP A 369 ? ? -117.07 -167.83 14 1 LYS A 371 ? ? -81.09 -152.33 # loop_ _pdbx_validate_chiral.id _pdbx_validate_chiral.PDB_model_num _pdbx_validate_chiral.auth_atom_id _pdbx_validate_chiral.label_alt_id _pdbx_validate_chiral.auth_asym_id _pdbx_validate_chiral.auth_comp_id _pdbx_validate_chiral.auth_seq_id _pdbx_validate_chiral.PDB_ins_code _pdbx_validate_chiral.details _pdbx_validate_chiral.omega 1 1 C1 ? A MAN 903 ? 'WRONG HAND' . 2 1 C1 ? A NAG 921 ? 'WRONG HAND' . # loop_ _pdbx_distant_solvent_atoms.id _pdbx_distant_solvent_atoms.PDB_model_num _pdbx_distant_solvent_atoms.auth_atom_id _pdbx_distant_solvent_atoms.label_alt_id _pdbx_distant_solvent_atoms.auth_asym_id _pdbx_distant_solvent_atoms.auth_comp_id _pdbx_distant_solvent_atoms.auth_seq_id _pdbx_distant_solvent_atoms.PDB_ins_code _pdbx_distant_solvent_atoms.neighbor_macromolecule_distance _pdbx_distant_solvent_atoms.neighbor_ligand_distance 1 1 O ? A HOH 2034 ? . 7.80 2 1 O ? A HOH 2035 ? 7.36 . 3 1 O ? A HOH 2085 ? . 6.10 4 1 O ? A HOH 2086 ? . 6.62 5 1 O ? A HOH 2087 ? . 5.88 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 ALPHA-D-MANNOSE MAN 4 'SULFATE ION' SO4 5 'ZINC ION' ZN 6 water HOH #