data_4ZV7 # _entry.id 4ZV7 # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.284 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 4ZV7 WWPDB D_1000209973 # loop_ _pdbx_database_related.db_name _pdbx_database_related.details _pdbx_database_related.db_id _pdbx_database_related.content_type PDB . 1TCA unspecified PDB . 1TCB unspecified PDB . 1TCC unspecified PDB . 3W9B unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.entry_id 4ZV7 _pdbx_database_status.recvd_initial_deposition_date 2015-05-18 _pdbx_database_status.SG_entry N _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site PDBE _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? _pdbx_database_status.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Strzelczyk, P.' 1 'Blaszczyk, J.' 2 'Bujacz, G.' 3 # _citation.abstract ? _citation.abstract_id_CAS ? _citation.book_id_ISBN ? _citation.book_publisher ? _citation.book_publisher_city ? _citation.book_title ? _citation.coordinate_linkage ? _citation.country PL _citation.database_id_Medline ? _citation.details ? _citation.id primary _citation.journal_abbrev 'Acta Biochim.Pol.' _citation.journal_id_ASTM ABPLAF _citation.journal_id_CSD 1139 _citation.journal_id_ISSN 0001-527X _citation.journal_full ? _citation.journal_issue ? _citation.journal_volume 63 _citation.language ? _citation.page_first 103 _citation.page_last 109 _citation.title 'Crystal and molecular structure of hexagonal form of lipase B from Candida antarctica.' _citation.year 2016 _citation.database_id_CSD ? _citation.pdbx_database_id_DOI 10.18388/abp.2015_1065 _citation.pdbx_database_id_PubMed 26716135 _citation.unpublished_flag ? # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Strzelczyk, P.' 1 primary 'Bujacz, G.D.' 2 primary 'Kiebasinski, P.' 3 primary 'Baszczyk, J.' 4 # _cell.angle_alpha 90.00 _cell.angle_alpha_esd ? _cell.angle_beta 90.00 _cell.angle_beta_esd ? _cell.angle_gamma 120.00 _cell.angle_gamma_esd ? _cell.entry_id 4ZV7 _cell.details ? _cell.formula_units_Z ? _cell.length_a 89.034 _cell.length_a_esd ? _cell.length_b 89.034 _cell.length_b_esd ? _cell.length_c 137.257 _cell.length_c_esd ? _cell.volume ? _cell.volume_esd ? _cell.Z_PDB 12 _cell.reciprocal_angle_alpha ? _cell.reciprocal_angle_beta ? _cell.reciprocal_angle_gamma ? _cell.reciprocal_angle_alpha_esd ? _cell.reciprocal_angle_beta_esd ? _cell.reciprocal_angle_gamma_esd ? _cell.reciprocal_length_a ? _cell.reciprocal_length_b ? _cell.reciprocal_length_c ? _cell.reciprocal_length_a_esd ? _cell.reciprocal_length_b_esd ? _cell.reciprocal_length_c_esd ? _cell.pdbx_unique_axis ? # _symmetry.entry_id 4ZV7 _symmetry.cell_setting ? _symmetry.Int_Tables_number 182 _symmetry.space_group_name_Hall ? _symmetry.space_group_name_H-M 'P 63 2 2' _symmetry.pdbx_full_space_group_name_H-M ? # 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 'Lipase B' 33040.238 1 3.1.1.3 ? 'UNP residues 26-342' ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 2 ? ? ? ? 3 water nat water 18.015 332 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name CALB # _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 ;LPSGSDPAFSQPKSVLDAGLTCQGASPSSVSKPILLVPGTGTTGPQSFDSNWIPLSTQLGYTPCWISPPPFMLNDTQVNT EYMVNAITALYAGSGNNKLPVLTWSQGGLVAQWGLTFFPSIRSKVDRLMAFAPDYKGTVLAGPLDALAVSAPSVWQQTTG SALTTALRNAGGLTQIVPTTNLYSATDEIVQPQVSNSPLDSSYLFNGKNVQAQAVCGPLFVIDHAGSLTSQFSYVVGRSA LRSTTGQARSADYGITDCNPLPANDLTPEQKVAAAALLAPAAAAIVAGPKQNCEPDLMPYARPFAVGKRTCSGIVTP ; _entity_poly.pdbx_seq_one_letter_code_can ;LPSGSDPAFSQPKSVLDAGLTCQGASPSSVSKPILLVPGTGTTGPQSFDSNWIPLSTQLGYTPCWISPPPFMLNDTQVNT EYMVNAITALYAGSGNNKLPVLTWSQGGLVAQWGLTFFPSIRSKVDRLMAFAPDYKGTVLAGPLDALAVSAPSVWQQTTG SALTTALRNAGGLTQIVPTTNLYSATDEIVQPQVSNSPLDSSYLFNGKNVQAQAVCGPLFVIDHAGSLTSQFSYVVGRSA LRSTTGQARSADYGITDCNPLPANDLTPEQKVAAAALLAPAAAAIVAGPKQNCEPDLMPYARPFAVGKRTCSGIVTP ; _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 LEU n 1 2 PRO n 1 3 SER n 1 4 GLY n 1 5 SER n 1 6 ASP n 1 7 PRO n 1 8 ALA n 1 9 PHE n 1 10 SER n 1 11 GLN n 1 12 PRO n 1 13 LYS n 1 14 SER n 1 15 VAL n 1 16 LEU n 1 17 ASP n 1 18 ALA n 1 19 GLY n 1 20 LEU n 1 21 THR n 1 22 CYS n 1 23 GLN n 1 24 GLY n 1 25 ALA n 1 26 SER n 1 27 PRO n 1 28 SER n 1 29 SER n 1 30 VAL n 1 31 SER n 1 32 LYS n 1 33 PRO n 1 34 ILE n 1 35 LEU n 1 36 LEU n 1 37 VAL n 1 38 PRO n 1 39 GLY n 1 40 THR n 1 41 GLY n 1 42 THR n 1 43 THR n 1 44 GLY n 1 45 PRO n 1 46 GLN n 1 47 SER n 1 48 PHE n 1 49 ASP n 1 50 SER n 1 51 ASN n 1 52 TRP n 1 53 ILE n 1 54 PRO n 1 55 LEU n 1 56 SER n 1 57 THR n 1 58 GLN n 1 59 LEU n 1 60 GLY n 1 61 TYR n 1 62 THR n 1 63 PRO n 1 64 CYS n 1 65 TRP n 1 66 ILE n 1 67 SER n 1 68 PRO n 1 69 PRO n 1 70 PRO n 1 71 PHE n 1 72 MET n 1 73 LEU n 1 74 ASN n 1 75 ASP n 1 76 THR n 1 77 GLN n 1 78 VAL n 1 79 ASN n 1 80 THR n 1 81 GLU n 1 82 TYR n 1 83 MET n 1 84 VAL n 1 85 ASN n 1 86 ALA n 1 87 ILE n 1 88 THR n 1 89 ALA n 1 90 LEU n 1 91 TYR n 1 92 ALA n 1 93 GLY n 1 94 SER n 1 95 GLY n 1 96 ASN n 1 97 ASN n 1 98 LYS n 1 99 LEU n 1 100 PRO n 1 101 VAL n 1 102 LEU n 1 103 THR n 1 104 TRP n 1 105 SER n 1 106 GLN n 1 107 GLY n 1 108 GLY n 1 109 LEU n 1 110 VAL n 1 111 ALA n 1 112 GLN n 1 113 TRP n 1 114 GLY n 1 115 LEU n 1 116 THR n 1 117 PHE n 1 118 PHE n 1 119 PRO n 1 120 SER n 1 121 ILE n 1 122 ARG n 1 123 SER n 1 124 LYS n 1 125 VAL n 1 126 ASP n 1 127 ARG n 1 128 LEU n 1 129 MET n 1 130 ALA n 1 131 PHE n 1 132 ALA n 1 133 PRO n 1 134 ASP n 1 135 TYR n 1 136 LYS n 1 137 GLY n 1 138 THR n 1 139 VAL n 1 140 LEU n 1 141 ALA n 1 142 GLY n 1 143 PRO n 1 144 LEU n 1 145 ASP n 1 146 ALA n 1 147 LEU n 1 148 ALA n 1 149 VAL n 1 150 SER n 1 151 ALA n 1 152 PRO n 1 153 SER n 1 154 VAL n 1 155 TRP n 1 156 GLN n 1 157 GLN n 1 158 THR n 1 159 THR n 1 160 GLY n 1 161 SER n 1 162 ALA n 1 163 LEU n 1 164 THR n 1 165 THR n 1 166 ALA n 1 167 LEU n 1 168 ARG n 1 169 ASN n 1 170 ALA n 1 171 GLY n 1 172 GLY n 1 173 LEU n 1 174 THR n 1 175 GLN n 1 176 ILE n 1 177 VAL n 1 178 PRO n 1 179 THR n 1 180 THR n 1 181 ASN n 1 182 LEU n 1 183 TYR n 1 184 SER n 1 185 ALA n 1 186 THR n 1 187 ASP n 1 188 GLU n 1 189 ILE n 1 190 VAL n 1 191 GLN n 1 192 PRO n 1 193 GLN n 1 194 VAL n 1 195 SER n 1 196 ASN n 1 197 SER n 1 198 PRO n 1 199 LEU n 1 200 ASP n 1 201 SER n 1 202 SER n 1 203 TYR n 1 204 LEU n 1 205 PHE n 1 206 ASN n 1 207 GLY n 1 208 LYS n 1 209 ASN n 1 210 VAL n 1 211 GLN n 1 212 ALA n 1 213 GLN n 1 214 ALA n 1 215 VAL n 1 216 CYS n 1 217 GLY n 1 218 PRO n 1 219 LEU n 1 220 PHE n 1 221 VAL n 1 222 ILE n 1 223 ASP n 1 224 HIS n 1 225 ALA n 1 226 GLY n 1 227 SER n 1 228 LEU n 1 229 THR n 1 230 SER n 1 231 GLN n 1 232 PHE n 1 233 SER n 1 234 TYR n 1 235 VAL n 1 236 VAL n 1 237 GLY n 1 238 ARG n 1 239 SER n 1 240 ALA n 1 241 LEU n 1 242 ARG n 1 243 SER n 1 244 THR n 1 245 THR n 1 246 GLY n 1 247 GLN n 1 248 ALA n 1 249 ARG n 1 250 SER n 1 251 ALA n 1 252 ASP n 1 253 TYR n 1 254 GLY n 1 255 ILE n 1 256 THR n 1 257 ASP n 1 258 CYS n 1 259 ASN n 1 260 PRO n 1 261 LEU n 1 262 PRO n 1 263 ALA n 1 264 ASN n 1 265 ASP n 1 266 LEU n 1 267 THR n 1 268 PRO n 1 269 GLU n 1 270 GLN n 1 271 LYS n 1 272 VAL n 1 273 ALA n 1 274 ALA n 1 275 ALA n 1 276 ALA n 1 277 LEU n 1 278 LEU n 1 279 ALA n 1 280 PRO n 1 281 ALA n 1 282 ALA n 1 283 ALA n 1 284 ALA n 1 285 ILE n 1 286 VAL n 1 287 ALA n 1 288 GLY n 1 289 PRO n 1 290 LYS n 1 291 GLN n 1 292 ASN n 1 293 CYS n 1 294 GLU n 1 295 PRO n 1 296 ASP n 1 297 LEU n 1 298 MET n 1 299 PRO n 1 300 TYR n 1 301 ALA n 1 302 ARG n 1 303 PRO n 1 304 PHE n 1 305 ALA n 1 306 VAL n 1 307 GLY n 1 308 LYS n 1 309 ARG n 1 310 THR n 1 311 CYS n 1 312 SER n 1 313 GLY n 1 314 ILE n 1 315 VAL n 1 316 THR n 1 317 PRO 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 'Biological sequence' _entity_src_gen.pdbx_beg_seq_num 1 _entity_src_gen.pdbx_end_seq_num 317 _entity_src_gen.gene_src_common_name Yeast _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 'Candida antarctica' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 34362 _entity_src_gen.pdbx_gene_src_variant ? _entity_src_gen.pdbx_gene_src_cell_line ? _entity_src_gen.pdbx_gene_src_atcc ? _entity_src_gen.pdbx_gene_src_organ ? _entity_src_gen.pdbx_gene_src_organelle ? _entity_src_gen.pdbx_gene_src_cell ? _entity_src_gen.pdbx_gene_src_cellular_location ? _entity_src_gen.host_org_common_name ? _entity_src_gen.pdbx_host_org_scientific_name 'Aspergillus oryzae' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 5062 _entity_src_gen.host_org_genus ? _entity_src_gen.pdbx_host_org_gene ? _entity_src_gen.pdbx_host_org_organ ? _entity_src_gen.host_org_species ? _entity_src_gen.pdbx_host_org_tissue ? _entity_src_gen.pdbx_host_org_tissue_fraction ? _entity_src_gen.pdbx_host_org_strain ? _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line ? _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type ? _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name ? _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code LIPB_CANAR _struct_ref.pdbx_db_accession P41365 _struct_ref.pdbx_db_isoform ? _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;LPSGSDPAFSQPKSVLDAGLTCQGASPSSVSKPILLVPGTGTTGPQSFDSNWIPLSTQLGYTPCWISPPPFMLNDTQVNT EYMVNAITALYAGSGNNKLPVLTWSQGGLVAQWGLTFFPSIRSKVDRLMAFAPDYKGTVLAGPLDALAVSAPSVWQQTTG SALTTALRNAGGLTQIVPTTNLYSATDEIVQPQVSNSPLDSSYLFNGKNVQAQAVCGPLFVIDHAGSLTSQFSYVVGRSA LRSTTGQARSADYGITDCNPLPANDLTPEQKVAAAALLAPAAAAIVAGPKQNCEPDLMPYARPFAVGKRTCSGIVTP ; _struct_ref.pdbx_align_begin 26 # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 4ZV7 _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 317 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession P41365 _struct_ref_seq.db_align_beg 26 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 342 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 1 _struct_ref_seq.pdbx_auth_seq_align_end 317 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.absorpt_coefficient_mu ? _exptl.absorpt_correction_T_max ? _exptl.absorpt_correction_T_min ? _exptl.absorpt_correction_type ? _exptl.absorpt_process_details ? _exptl.entry_id 4ZV7 _exptl.crystals_number ? _exptl.details ? _exptl.method 'X-RAY DIFFRACTION' _exptl.method_details ? # _exptl_crystal.colour ? _exptl_crystal.density_diffrn ? _exptl_crystal.density_Matthews 2.38 _exptl_crystal.density_method ? _exptl_crystal.density_percent_sol 48.24 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.id 1 _exptl_crystal.preparation ? _exptl_crystal.size_max ? _exptl_crystal.size_mid ? _exptl_crystal.size_min ? _exptl_crystal.size_rad ? _exptl_crystal.colour_lustre ? _exptl_crystal.colour_modifier ? _exptl_crystal.colour_primary ? _exptl_crystal.density_meas ? _exptl_crystal.density_meas_esd ? _exptl_crystal.density_meas_gt ? _exptl_crystal.density_meas_lt ? _exptl_crystal.density_meas_temp ? _exptl_crystal.density_meas_temp_esd ? _exptl_crystal.density_meas_temp_gt ? _exptl_crystal.density_meas_temp_lt ? _exptl_crystal.pdbx_crystal_image_url ? _exptl_crystal.pdbx_crystal_image_format ? _exptl_crystal.pdbx_mosaicity ? _exptl_crystal.pdbx_mosaicity_esd ? # _exptl_crystal_grow.apparatus ? _exptl_crystal_grow.atmosphere ? _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.details ? _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.method_ref ? _exptl_crystal_grow.pH 5.5 _exptl_crystal_grow.pressure ? _exptl_crystal_grow.pressure_esd ? _exptl_crystal_grow.seeding ? _exptl_crystal_grow.seeding_ref ? _exptl_crystal_grow.temp 294.15 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.temp_esd ? _exptl_crystal_grow.time ? _exptl_crystal_grow.pdbx_details '24% polyethylene glycol 3350, 0.1M citric acid, and 0.1M sodium acetate' _exptl_crystal_grow.pdbx_pH_range ? # _diffrn.ambient_environment ? _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.ambient_temp_esd ? _diffrn.crystal_id 1 _diffrn.crystal_support ? _diffrn.crystal_treatment ? _diffrn.details ? _diffrn.id 1 _diffrn.ambient_pressure ? _diffrn.ambient_pressure_esd ? _diffrn.ambient_pressure_gt ? _diffrn.ambient_pressure_lt ? _diffrn.ambient_temp_gt ? _diffrn.ambient_temp_lt ? # _diffrn_detector.details ? _diffrn_detector.detector CCD _diffrn_detector.diffrn_id 1 _diffrn_detector.type 'OXFORD TITAN CCD' _diffrn_detector.area_resol_mean ? _diffrn_detector.dtime ? _diffrn_detector.pdbx_frames_total ? _diffrn_detector.pdbx_collection_time_total ? _diffrn_detector.pdbx_collection_date 2015-03-29 # _diffrn_radiation.collimation ? _diffrn_radiation.diffrn_id 1 _diffrn_radiation.filter_edge ? _diffrn_radiation.inhomogeneity ? _diffrn_radiation.monochromator ? _diffrn_radiation.polarisn_norm ? _diffrn_radiation.polarisn_ratio ? _diffrn_radiation.probe ? _diffrn_radiation.type ? _diffrn_radiation.xray_symbol ? _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.pdbx_wavelength_list ? _diffrn_radiation.pdbx_wavelength ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_analyzer ? _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.54 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.current ? _diffrn_source.details ? _diffrn_source.diffrn_id 1 _diffrn_source.power ? _diffrn_source.size ? _diffrn_source.source 'ROTATING ANODE' _diffrn_source.target ? _diffrn_source.type RIGAKU _diffrn_source.voltage ? _diffrn_source.take-off_angle ? _diffrn_source.pdbx_wavelength_list 1.54 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_synchrotron_beamline ? _diffrn_source.pdbx_synchrotron_site ? # _reflns.B_iso_Wilson_estimate ? _reflns.entry_id 4ZV7 _reflns.data_reduction_details ? _reflns.data_reduction_method ? _reflns.d_resolution_high 2.00 _reflns.d_resolution_low 77.11 _reflns.details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.number_all ? _reflns.number_obs 22034 _reflns.observed_criterion ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.observed_criterion_I_max ? _reflns.observed_criterion_I_min ? _reflns.observed_criterion_sigma_F ? _reflns.observed_criterion_sigma_I ? _reflns.percent_possible_obs 98.1 _reflns.R_free_details ? _reflns.Rmerge_F_all ? _reflns.Rmerge_F_obs ? _reflns.Friedel_coverage ? _reflns.number_gt ? _reflns.threshold_expression ? _reflns.pdbx_redundancy 8.8 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rmerge_I_all ? _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_av_sigmaI ? _reflns.pdbx_netI_over_sigmaI 24.58 _reflns.pdbx_res_netI_over_av_sigmaI_2 ? _reflns.pdbx_res_netI_over_sigmaI_2 ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_d_res_high_opt ? _reflns.pdbx_d_res_low_opt ? _reflns.pdbx_d_res_opt_method ? _reflns.phase_calculation_details ? _reflns.pdbx_Rrim_I_all ? _reflns.pdbx_Rpim_I_all ? _reflns.pdbx_d_opt ? _reflns.pdbx_number_measured_all ? _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.pdbx_CC_half ? _reflns.pdbx_R_split ? # _refine.aniso_B[1][1] 0.32 _refine.aniso_B[1][2] 0.16 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][2] 0.32 _refine.aniso_B[2][3] 0.00 _refine.aniso_B[3][3] -1.04 _refine.B_iso_max ? _refine.B_iso_mean 22.891 _refine.B_iso_min ? _refine.correlation_coeff_Fo_to_Fc 0.966 _refine.correlation_coeff_Fo_to_Fc_free 0.940 _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' _refine.diff_density_max ? _refine.diff_density_max_esd ? _refine.diff_density_min ? _refine.diff_density_min_esd ? _refine.diff_density_rms ? _refine.diff_density_rms_esd ? _refine.entry_id 4ZV7 _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.ls_abs_structure_details ? _refine.ls_abs_structure_Flack ? _refine.ls_abs_structure_Flack_esd ? _refine.ls_abs_structure_Rogers ? _refine.ls_abs_structure_Rogers_esd ? _refine.ls_d_res_high 2.00 _refine.ls_d_res_low 77.11 _refine.ls_extinction_coef ? _refine.ls_extinction_coef_esd ? _refine.ls_extinction_expression ? _refine.ls_extinction_method ? _refine.ls_goodness_of_fit_all ? _refine.ls_goodness_of_fit_all_esd ? _refine.ls_goodness_of_fit_obs ? _refine.ls_goodness_of_fit_obs_esd ? _refine.ls_hydrogen_treatment ? _refine.ls_matrix_type ? _refine.ls_number_constraints ? _refine.ls_number_parameters ? _refine.ls_number_reflns_all ? _refine.ls_number_reflns_obs 20971 _refine.ls_number_reflns_R_free 1032 _refine.ls_number_reflns_R_work ? _refine.ls_number_restraints ? _refine.ls_percent_reflns_obs 98.08 _refine.ls_percent_reflns_R_free 4.7 _refine.ls_R_factor_all ? _refine.ls_R_factor_obs 0.14654 _refine.ls_R_factor_R_free 0.19276 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_R_factor_R_work 0.14413 _refine.ls_R_Fsqd_factor_obs ? _refine.ls_R_I_factor_obs ? _refine.ls_redundancy_reflns_all ? _refine.ls_redundancy_reflns_obs ? _refine.ls_restrained_S_all ? _refine.ls_restrained_S_obs ? _refine.ls_shift_over_esd_max ? _refine.ls_shift_over_esd_mean ? _refine.ls_structure_factor_coef ? _refine.ls_weighting_details ? _refine.ls_weighting_scheme ? _refine.ls_wR_factor_all ? _refine.ls_wR_factor_obs ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.occupancy_max ? _refine.occupancy_min ? _refine.solvent_model_details 'BABINET MODEL WITH MASK' _refine.solvent_model_param_bsol ? _refine.solvent_model_param_ksol ? _refine.ls_R_factor_gt ? _refine.ls_goodness_of_fit_gt ? _refine.ls_goodness_of_fit_ref ? _refine.ls_shift_over_su_max ? _refine.ls_shift_over_su_max_lt ? _refine.ls_shift_over_su_mean ? _refine.ls_shift_over_su_mean_lt ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F ? _refine.pdbx_ls_sigma_Fsqd ? _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_starting_model 3W9B _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_overall_ESU_R 0.153 _refine.pdbx_overall_ESU_R_Free 0.142 _refine.pdbx_solvent_vdw_probe_radii 1.20 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_real_space_R ? _refine.pdbx_density_correlation ? _refine.pdbx_pd_number_of_powder_patterns ? _refine.pdbx_pd_number_of_points ? _refine.pdbx_pd_meas_number_of_points ? _refine.pdbx_pd_proc_ls_prof_R_factor ? _refine.pdbx_pd_proc_ls_prof_wR_factor ? _refine.pdbx_pd_Marquardt_correlation_coeff ? _refine.pdbx_pd_Fsqrd_R_factor ? _refine.pdbx_pd_ls_matrix_band_width ? _refine.pdbx_overall_phase_error ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_diffrn_id 1 _refine.overall_SU_B 6.698 _refine.overall_SU_ML 0.097 _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_average_fsc_overall ? _refine.pdbx_average_fsc_work ? _refine.pdbx_average_fsc_free ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id 1 _refine_hist.pdbx_number_atoms_protein 2324 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 28 _refine_hist.number_atoms_solvent 332 _refine_hist.number_atoms_total 2684 _refine_hist.d_res_high 2.00 _refine_hist.d_res_low 77.11 # loop_ _refine_ls_restr.pdbx_refine_id _refine_ls_restr.criterion _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.number _refine_ls_restr.rejects _refine_ls_restr.type _refine_ls_restr.weight _refine_ls_restr.pdbx_restraint_function 'X-RAY DIFFRACTION' ? 0.020 0.020 2449 ? r_bond_refined_d ? ? 'X-RAY DIFFRACTION' ? 0.002 0.020 2289 ? r_bond_other_d ? ? 'X-RAY DIFFRACTION' ? 1.964 1.983 3371 ? r_angle_refined_deg ? ? 'X-RAY DIFFRACTION' ? 1.136 3.000 5296 ? r_angle_other_deg ? ? 'X-RAY DIFFRACTION' ? 6.744 5.000 324 ? r_dihedral_angle_1_deg ? ? 'X-RAY DIFFRACTION' ? 34.756 24.706 85 ? r_dihedral_angle_2_deg ? ? 'X-RAY DIFFRACTION' ? 13.024 15.000 348 ? r_dihedral_angle_3_deg ? ? 'X-RAY DIFFRACTION' ? 17.036 15.000 10 ? r_dihedral_angle_4_deg ? ? 'X-RAY DIFFRACTION' ? 0.119 0.200 397 ? r_chiral_restr ? ? 'X-RAY DIFFRACTION' ? 0.010 0.021 2805 ? r_gen_planes_refined ? ? 'X-RAY DIFFRACTION' ? 0.002 0.020 517 ? r_gen_planes_other ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_nbd_refined ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_nbd_other ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_nbtor_refined ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_nbtor_other ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_xyhbond_nbd_refined ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_xyhbond_nbd_other ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_metal_ion_refined ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_metal_ion_other ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_symmetry_vdw_refined ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_symmetry_vdw_other ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_symmetry_hbond_refined ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_symmetry_hbond_other ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_symmetry_metal_ion_refined ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_symmetry_metal_ion_other ? ? 'X-RAY DIFFRACTION' ? 1.000 1.743 1281 ? r_mcbond_it ? ? 'X-RAY DIFFRACTION' ? 0.990 1.741 1280 ? r_mcbond_other ? ? 'X-RAY DIFFRACTION' ? 1.537 2.607 1604 ? r_mcangle_it ? ? 'X-RAY DIFFRACTION' ? 1.541 2.608 1605 ? r_mcangle_other ? ? 'X-RAY DIFFRACTION' ? 1.395 1.910 1168 ? r_scbond_it ? ? 'X-RAY DIFFRACTION' ? 1.395 1.913 1169 ? r_scbond_other ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_scangle_it ? ? 'X-RAY DIFFRACTION' ? 2.132 2.817 1766 ? r_scangle_other ? ? 'X-RAY DIFFRACTION' ? 5.510 16.203 3035 ? r_long_range_B_refined ? ? 'X-RAY DIFFRACTION' ? 5.509 16.217 3036 ? r_long_range_B_other ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_rigid_bond_restr ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_sphericity_free ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_sphericity_bonded ? ? # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.d_res_high 2.000 _refine_ls_shell.d_res_low 2.052 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.number_reflns_R_free 64 _refine_ls_shell.number_reflns_R_work 1418 _refine_ls_shell.percent_reflns_obs 91.48 _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.R_factor_obs ? _refine_ls_shell.R_factor_R_free 0.248 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.R_factor_R_work 0.175 _refine_ls_shell.redundancy_reflns_all ? _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.wR_factor_all ? _refine_ls_shell.wR_factor_obs ? _refine_ls_shell.wR_factor_R_free ? _refine_ls_shell.wR_factor_R_work ? _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.pdbx_phase_error ? _refine_ls_shell.pdbx_fsc_work ? _refine_ls_shell.pdbx_fsc_free ? # _struct.entry_id 4ZV7 _struct.title 'Crystal structure of hexagonal form of lipase B from Candida antarctica' _struct.pdbx_descriptor 'Uncharacterized protein' _struct.pdbx_model_details ? _struct.pdbx_formula_weight ? _struct.pdbx_formula_weight_method ? _struct.pdbx_model_type_details ? _struct.pdbx_CASP_flag ? # _struct_keywords.entry_id 4ZV7 _struct_keywords.text 'CAL-B, hexagonal form, hydrolase' _struct_keywords.pdbx_keywords HYDROLASE # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 2 ? D N N 3 ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 AA1 PRO A 12 ? GLY A 19 ? PRO A 12 GLY A 19 1 ? 8 HELX_P HELX_P2 AA2 THR A 43 ? ASP A 49 ? THR A 43 ASP A 49 1 ? 7 HELX_P HELX_P3 AA3 ASN A 51 ? LEU A 59 ? ASN A 51 LEU A 59 1 ? 9 HELX_P HELX_P4 AA4 ASP A 75 ? SER A 94 ? ASP A 75 SER A 94 1 ? 20 HELX_P HELX_P5 AA5 SER A 105 ? PHE A 118 ? SER A 105 PHE A 118 1 ? 14 HELX_P HELX_P6 AA6 PRO A 119 ? ARG A 122 ? PRO A 119 ARG A 122 5 ? 4 HELX_P HELX_P7 AA7 THR A 138 ? LEU A 140 ? THR A 138 LEU A 140 5 ? 3 HELX_P HELX_P8 AA8 ALA A 141 ? LEU A 147 ? ALA A 141 LEU A 147 1 ? 7 HELX_P HELX_P9 AA9 ALA A 151 ? GLN A 157 ? ALA A 151 GLN A 157 1 ? 7 HELX_P HELX_P10 AB1 SER A 161 ? ALA A 170 ? SER A 161 ALA A 170 1 ? 10 HELX_P HELX_P11 AB2 ALA A 212 ? GLY A 217 ? ALA A 212 GLY A 217 1 ? 6 HELX_P HELX_P12 AB3 ALA A 225 ? SER A 230 ? ALA A 225 SER A 230 1 ? 6 HELX_P HELX_P13 AB4 SER A 230 ? SER A 243 ? SER A 230 SER A 243 1 ? 14 HELX_P HELX_P14 AB5 ARG A 249 ? TYR A 253 ? ARG A 249 TYR A 253 5 ? 5 HELX_P HELX_P15 AB6 GLY A 254 ? CYS A 258 ? GLY A 254 CYS A 258 5 ? 5 HELX_P HELX_P16 AB7 THR A 267 ? ALA A 276 ? THR A 267 ALA A 276 1 ? 10 HELX_P HELX_P17 AB8 LEU A 277 ? GLY A 288 ? LEU A 277 GLY A 288 1 ? 12 HELX_P HELX_P18 AB9 MET A 298 ? ALA A 305 ? MET A 298 ALA A 305 5 ? 8 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 22 SG ? ? ? 1_555 A CYS 64 SG ? ? A CYS 22 A CYS 64 1_555 ? ? ? ? ? ? ? 2.095 ? disulf2 disulf ? ? A CYS 216 SG ? ? ? 1_555 A CYS 258 SG ? ? A CYS 216 A CYS 258 1_555 ? ? ? ? ? ? ? 2.044 ? disulf3 disulf ? ? A CYS 293 SG ? ? ? 1_555 A CYS 311 SG ? ? A CYS 293 A CYS 311 1_555 ? ? ? ? ? ? ? 2.036 ? covale1 covale one ? A ASN 74 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 74 A NAG 800 1_555 ? ? ? ? ? ? ? 1.428 ? covale2 covale both ? B NAG . O4 ? ? ? 1_555 C NAG . C1 ? ? A NAG 800 A NAG 801 1_555 ? ? ? ? ? ? ? 1.436 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 PRO 69 A . ? PRO 69 A PRO 70 A ? PRO 70 A 1 -11.53 2 GLN 191 A . ? GLN 191 A PRO 192 A ? PRO 192 A 1 5.84 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA1 ? 7 ? AA2 ? 2 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense AA1 1 2 ? anti-parallel AA1 2 3 ? parallel AA1 3 4 ? parallel AA1 4 5 ? parallel AA1 5 6 ? parallel AA1 6 7 ? parallel AA2 1 2 ? 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 AA1 1 LEU A 20 ? CYS A 22 ? LEU A 20 CYS A 22 AA1 2 THR A 62 ? ILE A 66 ? THR A 62 ILE A 66 AA1 3 PRO A 33 ? VAL A 37 ? PRO A 33 VAL A 37 AA1 4 LEU A 99 ? TRP A 104 ? LEU A 99 TRP A 104 AA1 5 VAL A 125 ? PHE A 131 ? VAL A 125 PHE A 131 AA1 6 THR A 179 ? TYR A 183 ? THR A 179 TYR A 183 AA1 7 LYS A 208 ? GLN A 211 ? LYS A 208 GLN A 211 AA2 1 ARG A 309 ? THR A 310 ? ARG A 309 THR A 310 AA2 2 GLY A 313 ? ILE A 314 ? GLY A 313 ILE A 314 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id AA1 1 2 N THR A 21 ? N THR A 21 O TRP A 65 ? O TRP A 65 AA1 2 3 O CYS A 64 ? O CYS A 64 N ILE A 34 ? N ILE A 34 AA1 3 4 N LEU A 35 ? N LEU A 35 O LEU A 102 ? O LEU A 102 AA1 4 5 N THR A 103 ? N THR A 103 O MET A 129 ? O MET A 129 AA1 5 6 N ALA A 130 ? N ALA A 130 O THR A 180 ? O THR A 180 AA1 6 7 N ASN A 181 ? N ASN A 181 O VAL A 210 ? O VAL A 210 AA2 1 2 N THR A 310 ? N THR A 310 O GLY A 313 ? O GLY A 313 # _struct_site.id AC1 _struct_site.pdbx_evidence_code Software _struct_site.pdbx_auth_asym_id A _struct_site.pdbx_auth_comp_id ASN _struct_site.pdbx_auth_seq_id 74 _struct_site.pdbx_auth_ins_code ? _struct_site.pdbx_num_residues 5 _struct_site.details 'binding site for Poly-Saccharide residues NAG A 800 through NAG A 801 bound to ASN A 74' # 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 5 PRO A 70 ? PRO A 70 . ? 1_555 ? 2 AC1 5 ASN A 74 ? ASN A 74 . ? 1_555 ? 3 AC1 5 HOH D . ? HOH A 958 . ? 1_555 ? 4 AC1 5 HOH D . ? HOH A 1015 . ? 1_555 ? 5 AC1 5 HOH D . ? HOH A 1053 . ? 1_555 ? # _atom_sites.entry_id 4ZV7 _atom_sites.fract_transf_matrix[1][1] 0.011232 _atom_sites.fract_transf_matrix[1][2] 0.006485 _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] 0.012969 _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] 0.007286 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . LEU A 1 1 ? 13.429 2.109 3.201 1.00 29.55 ? 1 LEU A N 1 ATOM 2 C CA . LEU A 1 1 ? 13.825 3.498 3.283 1.00 29.24 ? 1 LEU A CA 1 ATOM 3 C C . LEU A 1 1 ? 12.941 4.318 2.390 1.00 26.24 ? 1 LEU A C 1 ATOM 4 O O . LEU A 1 1 ? 12.609 3.889 1.258 1.00 25.62 ? 1 LEU A O 1 ATOM 5 C CB . LEU A 1 1 ? 15.281 3.727 2.808 1.00 31.57 ? 1 LEU A CB 1 ATOM 6 C CG . LEU A 1 1 ? 16.407 3.116 3.581 1.00 33.56 ? 1 LEU A CG 1 ATOM 7 C CD1 . LEU A 1 1 ? 17.730 3.439 2.842 1.00 33.13 ? 1 LEU A CD1 1 ATOM 8 C CD2 . LEU A 1 1 ? 16.354 3.658 5.025 1.00 32.68 ? 1 LEU A CD2 1 ATOM 9 N N . PRO A 1 2 ? 12.648 5.534 2.841 1.00 24.02 ? 2 PRO A N 1 ATOM 10 C CA . PRO A 1 2 ? 12.095 6.487 1.934 1.00 23.90 ? 2 PRO A CA 1 ATOM 11 C C . PRO A 1 2 ? 12.952 6.592 0.689 1.00 23.71 ? 2 PRO A C 1 ATOM 12 O O . PRO A 1 2 ? 14.197 6.579 0.716 1.00 22.76 ? 2 PRO A O 1 ATOM 13 C CB . PRO A 1 2 ? 12.137 7.801 2.729 1.00 23.33 ? 2 PRO A CB 1 ATOM 14 C CG . PRO A 1 2 ? 11.975 7.321 4.128 1.00 22.50 ? 2 PRO A CG 1 ATOM 15 C CD . PRO A 1 2 ? 12.806 6.101 4.187 1.00 23.17 ? 2 PRO A CD 1 ATOM 16 N N . SER A 1 3 ? 12.246 6.767 -0.407 1.00 25.62 ? 3 SER A N 1 ATOM 17 C CA . SER A 1 3 ? 12.884 7.090 -1.643 1.00 27.21 ? 3 SER A CA 1 ATOM 18 C C . SER A 1 3 ? 12.097 8.329 -2.042 1.00 27.96 ? 3 SER A C 1 ATOM 19 O O . SER A 1 3 ? 11.242 8.828 -1.330 1.00 31.08 ? 3 SER A O 1 ATOM 20 C CB . SER A 1 3 ? 12.810 5.901 -2.604 1.00 29.05 ? 3 SER A CB 1 ATOM 21 O OG . SER A 1 3 ? 11.461 5.540 -2.744 1.00 30.98 ? 3 SER A OG 1 ATOM 22 N N . GLY A 1 4 ? 12.332 8.848 -3.183 1.00 28.14 ? 4 GLY A N 1 ATOM 23 C CA . GLY A 1 4 ? 11.576 10.076 -3.492 1.00 25.40 ? 4 GLY A CA 1 ATOM 24 C C . GLY A 1 4 ? 12.400 11.306 -3.168 1.00 21.95 ? 4 GLY A C 1 ATOM 25 O O . GLY A 1 4 ? 13.636 11.236 -3.037 1.00 20.43 ? 4 GLY A O 1 ATOM 26 N N . SER A 1 5 ? 11.682 12.440 -3.117 1.00 21.55 ? 5 SER A N 1 ATOM 27 C CA . SER A 1 5 ? 12.306 13.775 -3.031 1.00 19.90 ? 5 SER A CA 1 ATOM 28 C C . SER A 1 5 ? 12.698 14.048 -1.606 1.00 19.73 ? 5 SER A C 1 ATOM 29 O O . SER A 1 5 ? 12.117 13.517 -0.668 1.00 18.31 ? 5 SER A O 1 ATOM 30 C CB . SER A 1 5 ? 11.378 14.870 -3.543 1.00 20.84 ? 5 SER A CB 1 ATOM 31 O OG . SER A 1 5 ? 11.406 14.985 -4.926 1.00 19.07 ? 5 SER A OG 1 ATOM 32 N N . ASP A 1 6 ? 13.743 14.840 -1.426 1.00 20.61 ? 6 ASP A N 1 ATOM 33 C CA . ASP A 1 6 ? 14.004 15.420 -0.117 1.00 19.97 ? 6 ASP A CA 1 ATOM 34 C C . ASP A 1 6 ? 12.768 16.311 0.245 1.00 19.90 ? 6 ASP A C 1 ATOM 35 O O . ASP A 1 6 ? 12.246 17.068 -0.604 1.00 19.10 ? 6 ASP A O 1 ATOM 36 C CB . ASP A 1 6 ? 15.238 16.326 -0.127 1.00 20.50 ? 6 ASP A CB 1 ATOM 37 C CG . ASP A 1 6 ? 16.531 15.598 -0.192 1.00 20.30 ? 6 ASP A CG 1 ATOM 38 O OD1 . ASP A 1 6 ? 16.558 14.389 -0.423 1.00 19.83 ? 6 ASP A OD1 1 ATOM 39 O OD2 . ASP A 1 6 ? 17.571 16.295 0.002 1.00 20.65 ? 6 ASP A OD2 1 ATOM 40 N N . PRO A 1 7 ? 12.292 16.206 1.493 1.00 18.16 ? 7 PRO A N 1 ATOM 41 C CA . PRO A 1 7 ? 11.341 17.205 1.983 1.00 17.89 ? 7 PRO A CA 1 ATOM 42 C C . PRO A 1 7 ? 11.939 18.604 1.973 1.00 17.07 ? 7 PRO A C 1 ATOM 43 O O . PRO A 1 7 ? 13.164 18.734 2.240 1.00 18.33 ? 7 PRO A O 1 ATOM 44 C CB . PRO A 1 7 ? 11.084 16.783 3.432 1.00 17.93 ? 7 PRO A CB 1 ATOM 45 C CG . PRO A 1 7 ? 11.730 15.487 3.621 1.00 18.28 ? 7 PRO A CG 1 ATOM 46 C CD . PRO A 1 7 ? 12.709 15.246 2.514 1.00 18.27 ? 7 PRO A CD 1 ATOM 47 N N . ALA A 1 8 ? 11.129 19.635 1.738 1.00 17.48 ? 8 ALA A N 1 ATOM 48 C CA . ALA A 1 8 ? 11.550 21.014 1.917 1.00 18.01 ? 8 ALA A CA 1 ATOM 49 C C . ALA A 1 8 ? 11.959 21.240 3.377 1.00 17.87 ? 8 ALA A C 1 ATOM 50 O O . ALA A 1 8 ? 11.473 20.544 4.291 1.00 17.43 ? 8 ALA A O 1 ATOM 51 C CB . ALA A 1 8 ? 10.428 21.994 1.584 1.00 18.60 ? 8 ALA A CB 1 ATOM 52 N N . PHE A 1 9 ? 12.868 22.180 3.589 1.00 17.87 ? 9 PHE A N 1 ATOM 53 C CA . PHE A 1 9 ? 13.249 22.592 4.899 1.00 18.85 ? 9 PHE A CA 1 ATOM 54 C C . PHE A 1 9 ? 12.183 23.542 5.447 1.00 19.64 ? 9 PHE A C 1 ATOM 55 O O . PHE A 1 9 ? 11.605 24.260 4.709 1.00 21.44 ? 9 PHE A O 1 ATOM 56 C CB . PHE A 1 9 ? 14.564 23.299 4.896 1.00 18.59 ? 9 PHE A CB 1 ATOM 57 C CG . PHE A 1 9 ? 15.714 22.451 4.469 1.00 18.25 ? 9 PHE A CG 1 ATOM 58 C CD1 . PHE A 1 9 ? 15.919 21.191 4.976 1.00 18.34 ? 9 PHE A CD1 1 ATOM 59 C CD2 . PHE A 1 9 ? 16.653 22.968 3.587 1.00 18.80 ? 9 PHE A CD2 1 ATOM 60 C CE1 . PHE A 1 9 ? 17.025 20.413 4.579 1.00 18.44 ? 9 PHE A CE1 1 ATOM 61 C CE2 . PHE A 1 9 ? 17.763 22.212 3.199 1.00 19.25 ? 9 PHE A CE2 1 ATOM 62 C CZ . PHE A 1 9 ? 17.957 20.953 3.688 1.00 18.27 ? 9 PHE A CZ 1 ATOM 63 N N . SER A 1 10 ? 11.936 23.507 6.739 1.00 20.80 ? 10 SER A N 1 ATOM 64 C CA . SER A 1 10 ? 11.043 24.483 7.437 1.00 21.07 ? 10 SER A CA 1 ATOM 65 C C . SER A 1 10 ? 11.785 25.808 7.712 1.00 23.30 ? 10 SER A C 1 ATOM 66 O O . SER A 1 10 ? 11.168 26.799 7.953 1.00 23.78 ? 10 SER A O 1 ATOM 67 C CB . SER A 1 10 ? 10.641 23.817 8.724 1.00 20.92 ? 10 SER A CB 1 ATOM 68 O OG . SER A 1 10 ? 11.701 23.730 9.711 1.00 20.52 ? 10 SER A OG 1 ATOM 69 N N . GLN A 1 11 ? 13.116 25.811 7.685 1.00 23.05 ? 11 GLN A N 1 ATOM 70 C CA . GLN A 1 11 ? 13.912 27.065 7.906 1.00 23.76 ? 11 GLN A CA 1 ATOM 71 C C . GLN A 1 11 ? 14.425 27.533 6.579 1.00 23.47 ? 11 GLN A C 1 ATOM 72 O O . GLN A 1 11 ? 14.745 26.691 5.752 1.00 22.20 ? 11 GLN A O 1 ATOM 73 C CB . GLN A 1 11 ? 15.228 26.752 8.660 1.00 24.84 ? 11 GLN A CB 1 ATOM 74 C CG . GLN A 1 11 ? 15.037 26.116 9.989 1.00 26.82 ? 11 GLN A CG 1 ATOM 75 C CD . GLN A 1 11 ? 14.328 27.029 10.914 1.00 29.29 ? 11 GLN A CD 1 ATOM 76 O OE1 . GLN A 1 11 ? 14.761 28.149 11.131 1.00 29.18 ? 11 GLN A OE1 1 ATOM 77 N NE2 . GLN A 1 11 ? 13.173 26.589 11.396 1.00 32.33 ? 11 GLN A NE2 1 ATOM 78 N N . PRO A 1 12 ? 14.687 28.823 6.439 1.00 24.28 ? 12 PRO A N 1 ATOM 79 C CA . PRO A 1 12 ? 15.397 29.327 5.262 1.00 25.18 ? 12 PRO A CA 1 ATOM 80 C C . PRO A 1 12 ? 16.854 28.845 5.190 1.00 26.37 ? 12 PRO A C 1 ATOM 81 O O . PRO A 1 12 ? 17.539 28.624 6.215 1.00 24.93 ? 12 PRO A O 1 ATOM 82 C CB . PRO A 1 12 ? 15.382 30.854 5.435 1.00 26.89 ? 12 PRO A CB 1 ATOM 83 C CG . PRO A 1 12 ? 14.583 31.142 6.657 1.00 26.91 ? 12 PRO A CG 1 ATOM 84 C CD . PRO A 1 12 ? 14.218 29.883 7.342 1.00 24.84 ? 12 PRO A CD 1 ATOM 85 N N . LYS A 1 13 ? 17.339 28.668 3.977 1.00 28.01 ? 13 LYS A N 1 ATOM 86 C CA . LYS A 1 13 ? 18.735 28.253 3.767 1.00 30.88 ? 13 LYS A CA 1 ATOM 87 C C . LYS A 1 13 ? 19.690 29.320 4.299 1.00 29.11 ? 13 LYS A C 1 ATOM 88 O O . LYS A 1 13 ? 20.743 28.966 4.820 1.00 28.02 ? 13 LYS A O 1 ATOM 89 C CB . LYS A 1 13 ? 19.020 27.944 2.299 1.00 35.49 ? 13 LYS A CB 1 ATOM 90 C CG . LYS A 1 13 ? 20.427 27.457 1.938 1.00 37.62 ? 13 LYS A CG 1 ATOM 91 C CD . LYS A 1 13 ? 20.770 27.634 0.457 1.00 39.55 ? 13 LYS A CD 1 ATOM 92 C CE . LYS A 1 13 ? 22.276 27.856 0.183 1.00 39.80 ? 13 LYS A CE 1 ATOM 93 N NZ . LYS A 1 13 ? 23.045 26.617 0.494 1.00 43.08 ? 13 LYS A NZ 1 ATOM 94 N N . SER A 1 14 ? 19.316 30.600 4.267 1.00 28.40 ? 14 SER A N 1 ATOM 95 C CA . SER A 1 14 ? 20.189 31.597 4.924 1.00 27.80 ? 14 SER A CA 1 ATOM 96 C C . SER A 1 14 ? 20.432 31.278 6.426 1.00 25.76 ? 14 SER A C 1 ATOM 97 O O . SER A 1 14 ? 21.554 31.418 6.972 1.00 25.75 ? 14 SER A O 1 ATOM 98 C CB . SER A 1 14 ? 19.620 32.992 4.758 1.00 28.84 ? 14 SER A CB 1 ATOM 99 O OG . SER A 1 14 ? 18.429 33.137 5.511 1.00 31.11 ? 14 SER A OG 1 ATOM 100 N N . VAL A 1 15 ? 19.379 30.850 7.095 1.00 23.41 ? 15 VAL A N 1 ATOM 101 C CA . VAL A 1 15 ? 19.451 30.489 8.507 1.00 23.30 ? 15 VAL A CA 1 ATOM 102 C C . VAL A 1 15 ? 20.262 29.225 8.692 1.00 21.95 ? 15 VAL A C 1 ATOM 103 O O . VAL A 1 15 ? 21.100 29.114 9.595 1.00 22.24 ? 15 VAL A O 1 ATOM 104 C CB . VAL A 1 15 ? 18.010 30.336 9.104 1.00 23.13 ? 15 VAL A CB 1 ATOM 105 C CG1 . VAL A 1 15 ? 18.026 29.733 10.511 1.00 23.74 ? 15 VAL A CG1 1 ATOM 106 C CG2 . VAL A 1 15 ? 17.272 31.676 9.086 1.00 24.23 ? 15 VAL A CG2 1 ATOM 107 N N . LEU A 1 16 ? 19.951 28.223 7.873 1.00 20.77 ? 16 LEU A N 1 ATOM 108 C CA . LEU A 1 16 ? 20.759 26.974 7.856 1.00 19.84 ? 16 LEU A CA 1 ATOM 109 C C . LEU A 1 16 ? 22.260 27.146 7.587 1.00 20.44 ? 16 LEU A C 1 ATOM 110 O O . LEU A 1 16 ? 23.129 26.564 8.308 1.00 17.64 ? 16 LEU A O 1 ATOM 111 C CB . LEU A 1 16 ? 20.149 25.993 6.838 1.00 19.25 ? 16 LEU A CB 1 ATOM 112 C CG . LEU A 1 16 ? 18.722 25.518 7.195 1.00 18.83 ? 16 LEU A CG 1 ATOM 113 C CD1 . LEU A 1 16 ? 18.187 24.507 6.178 1.00 18.85 ? 16 LEU A CD1 1 ATOM 114 C CD2 . LEU A 1 16 ? 18.661 24.926 8.582 1.00 18.78 ? 16 LEU A CD2 1 ATOM 115 N N . ASP A 1 17 ? 22.571 27.951 6.566 1.00 21.27 ? 17 ASP A N 1 ATOM 116 C CA . ASP A 1 17 ? 23.961 28.267 6.256 1.00 24.26 ? 17 ASP A CA 1 ATOM 117 C C . ASP A 1 17 ? 24.702 28.960 7.408 1.00 24.09 ? 17 ASP A C 1 ATOM 118 O O . ASP A 1 17 ? 25.871 28.723 7.578 1.00 24.35 ? 17 ASP A O 1 ATOM 119 C CB . ASP A 1 17 ? 24.079 29.172 5.016 1.00 25.30 ? 17 ASP A CB 1 ATOM 120 C CG . ASP A 1 17 ? 23.800 28.442 3.715 1.00 25.80 ? 17 ASP A CG 1 ATOM 121 O OD1 . ASP A 1 17 ? 24.016 27.187 3.601 1.00 27.69 ? 17 ASP A OD1 1 ATOM 122 O OD2 . ASP A 1 17 ? 23.446 29.173 2.780 1.00 25.83 ? 17 ASP A OD2 1 ATOM 123 N N . ALA A 1 18 ? 24.014 29.851 8.128 1.00 25.46 ? 18 ALA A N 1 ATOM 124 C CA . ALA A 1 18 ? 24.570 30.551 9.279 1.00 25.48 ? 18 ALA A CA 1 ATOM 125 C C . ALA A 1 18 ? 24.929 29.631 10.439 1.00 25.36 ? 18 ALA A C 1 ATOM 126 O O . ALA A 1 18 ? 25.681 30.037 11.317 1.00 24.73 ? 18 ALA A O 1 ATOM 127 C CB . ALA A 1 18 ? 23.632 31.642 9.778 1.00 27.04 ? 18 ALA A CB 1 ATOM 128 N N . GLY A 1 19 ? 24.358 28.422 10.476 1.00 22.84 ? 19 GLY A N 1 ATOM 129 C CA . GLY A 1 19 ? 24.651 27.428 11.491 1.00 21.78 ? 19 GLY A CA 1 ATOM 130 C C . GLY A 1 19 ? 25.827 26.530 11.200 1.00 19.73 ? 19 GLY A C 1 ATOM 131 O O . GLY A 1 19 ? 26.175 25.694 12.050 1.00 21.93 ? 19 GLY A O 1 ATOM 132 N N . LEU A 1 20 ? 26.453 26.700 10.042 1.00 19.72 ? 20 LEU A N 1 ATOM 133 C CA . LEU A 1 20 ? 27.499 25.857 9.525 1.00 19.21 ? 20 LEU A CA 1 ATOM 134 C C . LEU A 1 20 ? 28.764 26.655 9.333 1.00 21.88 ? 20 LEU A C 1 ATOM 135 O O . LEU A 1 20 ? 28.739 27.796 8.753 1.00 22.59 ? 20 LEU A O 1 ATOM 136 C CB . LEU A 1 20 ? 27.140 25.344 8.135 1.00 19.05 ? 20 LEU A CB 1 ATOM 137 C CG . LEU A 1 20 ? 28.240 24.629 7.332 1.00 18.79 ? 20 LEU A CG 1 ATOM 138 C CD1 . LEU A 1 20 ? 28.810 23.358 7.964 1.00 18.71 ? 20 LEU A CD1 1 ATOM 139 C CD2 . LEU A 1 20 ? 27.751 24.356 5.922 1.00 19.05 ? 20 LEU A CD2 1 ATOM 140 N N . THR A 1 21 ? 29.856 26.072 9.785 1.00 22.12 ? 21 THR A N 1 ATOM 141 C CA . THR A 1 21 ? 31.184 26.619 9.498 1.00 24.25 ? 21 THR A CA 1 ATOM 142 C C . THR A 1 21 ? 32.251 25.608 9.449 1.00 21.81 ? 21 THR A C 1 ATOM 143 O O . THR A 1 21 ? 32.098 24.535 9.987 1.00 20.57 ? 21 THR A O 1 ATOM 144 C CB . THR A 1 21 ? 31.669 27.588 10.596 1.00 27.07 ? 21 THR A CB 1 ATOM 145 O OG1 . THR A 1 21 ? 31.707 26.930 11.882 1.00 27.14 ? 21 THR A OG1 1 ATOM 146 C CG2 . THR A 1 21 ? 30.832 28.858 10.558 1.00 29.17 ? 21 THR A CG2 1 ATOM 147 N N . CYS A 1 22 ? 33.334 26.025 8.835 1.00 21.46 ? 22 CYS A N 1 ATOM 148 C CA . CYS A 1 22 ? 34.559 25.240 8.691 1.00 21.56 ? 22 CYS A CA 1 ATOM 149 C C . CYS A 1 22 ? 35.719 26.005 9.299 1.00 20.83 ? 22 CYS A C 1 ATOM 150 O O . CYS A 1 22 ? 35.726 27.268 9.271 1.00 19.79 ? 22 CYS A O 1 ATOM 151 C CB . CYS A 1 22 ? 34.848 24.962 7.221 1.00 22.33 ? 22 CYS A CB 1 ATOM 152 S SG . CYS A 1 22 ? 33.555 23.909 6.505 1.00 22.89 ? 22 CYS A SG 1 ATOM 153 N N . GLN A 1 23 ? 36.664 25.249 9.830 1.00 19.76 ? 23 GLN A N 1 ATOM 154 C CA . GLN A 1 23 ? 37.816 25.853 10.489 1.00 21.01 ? 23 GLN A CA 1 ATOM 155 C C . GLN A 1 23 ? 38.736 26.405 9.419 1.00 21.63 ? 23 GLN A C 1 ATOM 156 O O . GLN A 1 23 ? 39.427 25.644 8.701 1.00 19.91 ? 23 GLN A O 1 ATOM 157 C CB . GLN A 1 23 ? 38.565 24.815 11.248 1.00 21.63 ? 23 GLN A CB 1 ATOM 158 C CG . GLN A 1 23 ? 39.784 25.240 12.038 1.00 22.52 ? 23 GLN A CG 1 ATOM 159 C CD . GLN A 1 23 ? 40.414 24.005 12.627 1.00 23.36 ? 23 GLN A CD 1 ATOM 160 O OE1 . GLN A 1 23 ? 41.179 23.266 11.941 1.00 27.16 ? 23 GLN A OE1 1 ATOM 161 N NE2 . GLN A 1 23 ? 40.074 23.715 13.853 1.00 23.16 ? 23 GLN A NE2 1 ATOM 162 N N . GLY A 1 24 ? 38.714 27.712 9.257 1.00 22.37 ? 24 GLY A N 1 ATOM 163 C CA . GLY A 1 24 ? 39.694 28.354 8.356 1.00 23.75 ? 24 GLY A CA 1 ATOM 164 C C . GLY A 1 24 ? 39.274 28.235 6.889 1.00 23.92 ? 24 GLY A C 1 ATOM 165 O O . GLY A 1 24 ? 40.083 28.448 5.987 1.00 25.84 ? 24 GLY A O 1 ATOM 166 N N . ALA A 1 25 ? 38.001 27.941 6.652 1.00 23.46 ? 25 ALA A N 1 ATOM 167 C CA . ALA A 1 25 ? 37.427 27.909 5.274 1.00 24.31 ? 25 ALA A CA 1 ATOM 168 C C . ALA A 1 25 ? 35.949 28.162 5.171 1.00 24.50 ? 25 ALA A C 1 ATOM 169 O O . ALA A 1 25 ? 35.176 28.026 6.122 1.00 22.12 ? 25 ALA A O 1 ATOM 170 C CB . ALA A 1 25 ? 37.784 26.625 4.593 1.00 24.93 ? 25 ALA A CB 1 ATOM 171 N N . SER A 1 26 ? 35.558 28.600 3.967 1.00 25.40 ? 26 SER A N 1 ATOM 172 C CA . SER A 1 26 ? 34.191 28.623 3.570 1.00 25.01 ? 26 SER A CA 1 ATOM 173 C C . SER A 1 26 ? 33.758 27.180 3.160 1.00 24.77 ? 26 SER A C 1 ATOM 174 O O . SER A 1 26 ? 34.525 26.461 2.489 1.00 22.58 ? 26 SER A O 1 ATOM 175 C CB . SER A 1 26 ? 34.006 29.585 2.355 1.00 26.29 ? 26 SER A CB 1 ATOM 176 O OG . SER A 1 26 ? 32.653 29.557 1.911 1.00 28.91 ? 26 SER A OG 1 ATOM 177 N N . PRO A 1 27 ? 32.516 26.788 3.500 1.00 24.76 ? 27 PRO A N 1 ATOM 178 C CA . PRO A 1 27 ? 31.925 25.529 3.021 1.00 24.99 ? 27 PRO A CA 1 ATOM 179 C C . PRO A 1 27 ? 31.858 25.436 1.468 1.00 24.34 ? 27 PRO A C 1 ATOM 180 O O . PRO A 1 27 ? 31.910 24.347 0.946 1.00 24.50 ? 27 PRO A O 1 ATOM 181 C CB . PRO A 1 27 ? 30.542 25.512 3.680 1.00 24.96 ? 27 PRO A CB 1 ATOM 182 C CG . PRO A 1 27 ? 30.746 26.349 4.902 1.00 25.15 ? 27 PRO A CG 1 ATOM 183 C CD . PRO A 1 27 ? 31.672 27.426 4.535 1.00 24.98 ? 27 PRO A CD 1 ATOM 184 N N A SER A 1 28 ? 31.783 26.577 0.778 0.50 24.72 ? 28 SER A N 1 ATOM 185 N N B SER A 1 28 ? 31.791 26.579 0.773 0.50 25.16 ? 28 SER A N 1 ATOM 186 C CA A SER A 1 28 ? 31.777 26.628 -0.673 0.50 24.21 ? 28 SER A CA 1 ATOM 187 C CA B SER A 1 28 ? 31.807 26.637 -0.688 0.50 24.91 ? 28 SER A CA 1 ATOM 188 C C A SER A 1 28 ? 33.142 26.349 -1.303 0.50 24.55 ? 28 SER A C 1 ATOM 189 C C B SER A 1 28 ? 33.147 26.297 -1.300 0.50 24.94 ? 28 SER A C 1 ATOM 190 O O A SER A 1 28 ? 33.213 26.157 -2.503 0.50 23.39 ? 28 SER A O 1 ATOM 191 O O B SER A 1 28 ? 33.213 26.035 -2.488 0.50 23.74 ? 28 SER A O 1 ATOM 192 C CB A SER A 1 28 ? 31.268 27.980 -1.170 0.50 24.34 ? 28 SER A CB 1 ATOM 193 C CB B SER A 1 28 ? 31.447 28.026 -1.195 0.50 25.49 ? 28 SER A CB 1 ATOM 194 O OG A SER A 1 28 ? 32.209 28.999 -0.895 0.50 24.70 ? 28 SER A OG 1 ATOM 195 O OG B SER A 1 28 ? 30.510 28.625 -0.353 0.50 26.35 ? 28 SER A OG 1 ATOM 196 N N . SER A 1 29 ? 34.224 26.328 -0.523 1.00 24.61 ? 29 SER A N 1 ATOM 197 C CA . SER A 1 29 ? 35.544 25.967 -1.070 1.00 24.33 ? 29 SER A CA 1 ATOM 198 C C . SER A 1 29 ? 36.438 25.379 -0.001 1.00 25.04 ? 29 SER A C 1 ATOM 199 O O . SER A 1 29 ? 37.068 26.099 0.746 1.00 26.07 ? 29 SER A O 1 ATOM 200 C CB . SER A 1 29 ? 36.182 27.210 -1.687 1.00 24.86 ? 29 SER A CB 1 ATOM 201 O OG . SER A 1 29 ? 37.418 26.849 -2.278 1.00 25.71 ? 29 SER A OG 1 ATOM 202 N N . VAL A 1 30 ? 36.468 24.064 0.103 1.00 24.97 ? 30 VAL A N 1 ATOM 203 C CA . VAL A 1 30 ? 37.009 23.456 1.321 1.00 26.50 ? 30 VAL A CA 1 ATOM 204 C C . VAL A 1 30 ? 37.614 22.130 0.919 1.00 26.79 ? 30 VAL A C 1 ATOM 205 O O . VAL A 1 30 ? 37.028 21.388 0.145 1.00 24.32 ? 30 VAL A O 1 ATOM 206 C CB . VAL A 1 30 ? 35.952 23.286 2.485 1.00 26.14 ? 30 VAL A CB 1 ATOM 207 C CG1 . VAL A 1 30 ? 34.750 22.453 2.065 1.00 26.20 ? 30 VAL A CG1 1 ATOM 208 C CG2 . VAL A 1 30 ? 36.586 22.654 3.737 1.00 27.34 ? 30 VAL A CG2 1 ATOM 209 N N . SER A 1 31 ? 38.800 21.859 1.444 1.00 29.41 ? 31 SER A N 1 ATOM 210 C CA . SER A 1 31 ? 39.448 20.628 1.102 1.00 30.92 ? 31 SER A CA 1 ATOM 211 C C . SER A 1 31 ? 39.350 19.582 2.270 1.00 28.58 ? 31 SER A C 1 ATOM 212 O O . SER A 1 31 ? 39.621 19.897 3.432 1.00 29.49 ? 31 SER A O 1 ATOM 213 C CB . SER A 1 31 ? 40.870 20.930 0.634 1.00 34.39 ? 31 SER A CB 1 ATOM 214 O OG . SER A 1 31 ? 41.778 20.813 1.705 1.00 35.23 ? 31 SER A OG 1 ATOM 215 N N . LYS A 1 32 ? 38.971 18.359 1.924 1.00 27.12 ? 32 LYS A N 1 ATOM 216 C CA . LYS A 1 32 ? 38.804 17.228 2.863 1.00 29.28 ? 32 LYS A CA 1 ATOM 217 C C . LYS A 1 32 ? 37.956 17.584 4.100 1.00 25.93 ? 32 LYS A C 1 ATOM 218 O O . LYS A 1 32 ? 38.428 17.452 5.289 1.00 23.98 ? 32 LYS A O 1 ATOM 219 C CB . LYS A 1 32 ? 40.130 16.578 3.279 1.00 32.55 ? 32 LYS A CB 1 ATOM 220 C CG . LYS A 1 32 ? 40.897 15.992 2.129 1.00 37.79 ? 32 LYS A CG 1 ATOM 221 C CD . LYS A 1 32 ? 41.593 14.675 2.492 1.00 43.44 ? 32 LYS A CD 1 ATOM 222 C CE . LYS A 1 32 ? 42.639 14.364 1.397 1.00 46.72 ? 32 LYS A CE 1 ATOM 223 N NZ . LYS A 1 32 ? 43.101 12.934 1.259 1.00 49.86 ? 32 LYS A NZ 1 ATOM 224 N N . PRO A 1 33 ? 36.733 18.112 3.829 1.00 22.77 ? 33 PRO A N 1 ATOM 225 C CA . PRO A 1 33 ? 35.928 18.409 5.002 1.00 21.84 ? 33 PRO A CA 1 ATOM 226 C C . PRO A 1 33 ? 35.495 17.155 5.759 1.00 20.75 ? 33 PRO A C 1 ATOM 227 O O . PRO A 1 33 ? 35.297 16.096 5.134 1.00 20.48 ? 33 PRO A O 1 ATOM 228 C CB . PRO A 1 33 ? 34.696 19.132 4.446 1.00 22.03 ? 33 PRO A CB 1 ATOM 229 C CG . PRO A 1 33 ? 34.620 18.708 3.037 1.00 22.44 ? 33 PRO A CG 1 ATOM 230 C CD . PRO A 1 33 ? 36.017 18.419 2.581 1.00 22.57 ? 33 PRO A CD 1 ATOM 231 N N . ILE A 1 34 ? 35.250 17.330 7.063 1.00 19.64 ? 34 ILE A N 1 ATOM 232 C CA . ILE A 1 34 ? 34.528 16.361 7.866 1.00 19.44 ? 34 ILE A CA 1 ATOM 233 C C . ILE A 1 34 ? 33.493 17.115 8.670 1.00 19.62 ? 34 ILE A C 1 ATOM 234 O O . ILE A 1 34 ? 33.775 18.135 9.342 1.00 19.22 ? 34 ILE A O 1 ATOM 235 C CB . ILE A 1 34 ? 35.461 15.546 8.797 1.00 19.83 ? 34 ILE A CB 1 ATOM 236 C CG1 . ILE A 1 34 ? 34.685 14.476 9.601 1.00 19.75 ? 34 ILE A CG1 1 ATOM 237 C CG2 . ILE A 1 34 ? 36.303 16.482 9.672 1.00 19.95 ? 34 ILE A CG2 1 ATOM 238 C CD1 . ILE A 1 34 ? 35.583 13.558 10.429 1.00 19.59 ? 34 ILE A CD1 1 ATOM 239 N N . LEU A 1 35 ? 32.269 16.624 8.591 1.00 19.19 ? 35 LEU A N 1 ATOM 240 C CA . LEU A 1 35 ? 31.191 17.302 9.266 1.00 18.43 ? 35 LEU A CA 1 ATOM 241 C C . LEU A 1 35 ? 31.037 16.656 10.623 1.00 17.77 ? 35 LEU A C 1 ATOM 242 O O . LEU A 1 35 ? 30.776 15.440 10.699 1.00 16.18 ? 35 LEU A O 1 ATOM 243 C CB . LEU A 1 35 ? 29.877 17.224 8.470 1.00 18.13 ? 35 LEU A CB 1 ATOM 244 C CG . LEU A 1 35 ? 28.705 17.961 9.078 1.00 18.51 ? 35 LEU A CG 1 ATOM 245 C CD1 . LEU A 1 35 ? 28.987 19.466 9.279 1.00 19.01 ? 35 LEU A CD1 1 ATOM 246 C CD2 . LEU A 1 35 ? 27.394 17.743 8.297 1.00 19.06 ? 35 LEU A CD2 1 ATOM 247 N N . LEU A 1 36 ? 31.081 17.526 11.640 1.00 17.20 ? 36 LEU A N 1 ATOM 248 C CA . LEU A 1 36 ? 30.854 17.135 12.997 1.00 17.41 ? 36 LEU A CA 1 ATOM 249 C C . LEU A 1 36 ? 29.501 17.617 13.445 1.00 16.99 ? 36 LEU A C 1 ATOM 250 O O . LEU A 1 36 ? 29.145 18.805 13.288 1.00 16.14 ? 36 LEU A O 1 ATOM 251 C CB . LEU A 1 36 ? 31.971 17.612 13.909 1.00 18.23 ? 36 LEU A CB 1 ATOM 252 C CG . LEU A 1 36 ? 33.413 17.498 13.372 1.00 18.15 ? 36 LEU A CG 1 ATOM 253 C CD1 . LEU A 1 36 ? 34.337 18.244 14.280 1.00 18.61 ? 36 LEU A CD1 1 ATOM 254 C CD2 . LEU A 1 36 ? 33.896 16.075 13.263 1.00 19.04 ? 36 LEU A CD2 1 ATOM 255 N N . VAL A 1 37 ? 28.770 16.694 14.058 1.00 16.26 ? 37 VAL A N 1 ATOM 256 C CA . VAL A 1 37 ? 27.390 16.983 14.554 1.00 17.18 ? 37 VAL A CA 1 ATOM 257 C C . VAL A 1 37 ? 27.375 16.776 16.070 1.00 15.48 ? 37 VAL A C 1 ATOM 258 O O . VAL A 1 37 ? 27.588 15.653 16.534 1.00 14.97 ? 37 VAL A O 1 ATOM 259 C CB . VAL A 1 37 ? 26.299 16.110 13.877 1.00 17.11 ? 37 VAL A CB 1 ATOM 260 C CG1 . VAL A 1 37 ? 24.926 16.652 14.233 1.00 17.93 ? 37 VAL A CG1 1 ATOM 261 C CG2 . VAL A 1 37 ? 26.561 16.058 12.388 1.00 18.58 ? 37 VAL A CG2 1 ATOM 262 N N . PRO A 1 38 ? 27.146 17.871 16.830 1.00 15.52 ? 38 PRO A N 1 ATOM 263 C CA . PRO A 1 38 ? 27.269 17.873 18.268 1.00 16.36 ? 38 PRO A CA 1 ATOM 264 C C . PRO A 1 38 ? 26.091 17.258 19.057 1.00 16.62 ? 38 PRO A C 1 ATOM 265 O O . PRO A 1 38 ? 25.060 16.872 18.501 1.00 17.19 ? 38 PRO A O 1 ATOM 266 C CB . PRO A 1 38 ? 27.390 19.398 18.597 1.00 16.54 ? 38 PRO A CB 1 ATOM 267 C CG . PRO A 1 38 ? 26.589 20.085 17.525 1.00 16.13 ? 38 PRO A CG 1 ATOM 268 C CD . PRO A 1 38 ? 26.725 19.196 16.316 1.00 16.38 ? 38 PRO A CD 1 ATOM 269 N N . GLY A 1 39 ? 26.324 17.122 20.357 1.00 16.41 ? 39 GLY A N 1 ATOM 270 C CA . GLY A 1 39 ? 25.475 16.433 21.288 1.00 16.68 ? 39 GLY A CA 1 ATOM 271 C C . GLY A 1 39 ? 24.526 17.452 21.899 1.00 17.24 ? 39 GLY A C 1 ATOM 272 O O . GLY A 1 39 ? 24.575 18.681 21.657 1.00 17.97 ? 39 GLY A O 1 ATOM 273 N N . THR A 1 40 ? 23.564 16.911 22.568 1.00 16.50 ? 40 THR A N 1 ATOM 274 C CA . THR A 1 40 ? 22.529 17.703 23.218 1.00 16.65 ? 40 THR A CA 1 ATOM 275 C C . THR A 1 40 ? 23.158 18.668 24.265 1.00 17.33 ? 40 THR A C 1 ATOM 276 O O . THR A 1 40 ? 24.040 18.276 25.074 1.00 17.33 ? 40 THR A O 1 ATOM 277 C CB . THR A 1 40 ? 21.498 16.755 23.918 1.00 15.80 ? 40 THR A CB 1 ATOM 278 O OG1 . THR A 1 40 ? 21.022 15.812 22.966 1.00 15.08 ? 40 THR A OG1 1 ATOM 279 C CG2 . THR A 1 40 ? 20.311 17.540 24.471 1.00 16.04 ? 40 THR A CG2 1 ATOM 280 N N . GLY A 1 41 ? 22.690 19.905 24.265 1.00 17.58 ? 41 GLY A N 1 ATOM 281 C CA . GLY A 1 41 ? 23.156 20.884 25.226 1.00 18.63 ? 41 GLY A CA 1 ATOM 282 C C . GLY A 1 41 ? 24.451 21.569 24.816 1.00 19.13 ? 41 GLY A C 1 ATOM 283 O O . GLY A 1 41 ? 25.097 22.171 25.663 1.00 20.61 ? 41 GLY A O 1 ATOM 284 N N . THR A 1 42 ? 24.837 21.486 23.537 1.00 19.02 ? 42 THR A N 1 ATOM 285 C CA . THR A 1 42 ? 26.145 22.029 23.035 1.00 19.16 ? 42 THR A CA 1 ATOM 286 C C . THR A 1 42 ? 26.024 22.645 21.651 1.00 19.34 ? 42 THR A C 1 ATOM 287 O O . THR A 1 42 ? 25.039 22.395 20.917 1.00 19.46 ? 42 THR A O 1 ATOM 288 C CB . THR A 1 42 ? 27.225 20.954 22.952 1.00 19.51 ? 42 THR A CB 1 ATOM 289 O OG1 . THR A 1 42 ? 26.912 19.982 21.909 1.00 18.78 ? 42 THR A OG1 1 ATOM 290 C CG2 . THR A 1 42 ? 27.412 20.209 24.357 1.00 19.95 ? 42 THR A CG2 1 ATOM 291 N N . THR A 1 43 ? 27.018 23.466 21.312 1.00 18.51 ? 43 THR A N 1 ATOM 292 C CA . THR A 1 43 ? 27.327 23.832 19.951 1.00 18.53 ? 43 THR A CA 1 ATOM 293 C C . THR A 1 43 ? 28.462 22.886 19.407 1.00 19.36 ? 43 THR A C 1 ATOM 294 O O . THR A 1 43 ? 29.088 22.115 20.186 1.00 19.12 ? 43 THR A O 1 ATOM 295 C CB . THR A 1 43 ? 27.842 25.297 19.918 1.00 18.58 ? 43 THR A CB 1 ATOM 296 O OG1 . THR A 1 43 ? 29.108 25.341 20.585 1.00 17.85 ? 43 THR A OG1 1 ATOM 297 C CG2 . THR A 1 43 ? 26.835 26.309 20.586 1.00 19.23 ? 43 THR A CG2 1 ATOM 298 N N . GLY A 1 44 ? 28.763 22.981 18.102 1.00 19.57 ? 44 GLY A N 1 ATOM 299 C CA . GLY A 1 44 ? 29.897 22.237 17.530 1.00 19.52 ? 44 GLY A CA 1 ATOM 300 C C . GLY A 1 44 ? 31.176 22.370 18.400 1.00 19.80 ? 44 GLY A C 1 ATOM 301 O O . GLY A 1 44 ? 31.726 21.382 18.864 1.00 18.69 ? 44 GLY A O 1 ATOM 302 N N . PRO A 1 45 ? 31.644 23.623 18.614 1.00 20.81 ? 45 PRO A N 1 ATOM 303 C CA . PRO A 1 45 ? 32.912 23.828 19.346 1.00 20.93 ? 45 PRO A CA 1 ATOM 304 C C . PRO A 1 45 ? 32.839 23.298 20.760 1.00 20.99 ? 45 PRO A C 1 ATOM 305 O O . PRO A 1 45 ? 33.801 22.712 21.257 1.00 19.11 ? 45 PRO A O 1 ATOM 306 C CB . PRO A 1 45 ? 33.092 25.361 19.326 1.00 21.35 ? 45 PRO A CB 1 ATOM 307 C CG . PRO A 1 45 ? 32.359 25.814 18.123 1.00 21.23 ? 45 PRO A CG 1 ATOM 308 C CD . PRO A 1 45 ? 31.211 24.844 17.908 1.00 21.29 ? 45 PRO A CD 1 ATOM 309 N N . GLN A 1 46 ? 31.696 23.487 21.422 1.00 20.84 ? 46 GLN A N 1 ATOM 310 C CA . GLN A 1 46 ? 31.562 22.945 22.760 1.00 21.31 ? 46 GLN A CA 1 ATOM 311 C C . GLN A 1 46 ? 31.663 21.436 22.855 1.00 20.16 ? 46 GLN A C 1 ATOM 312 O O . GLN A 1 46 ? 32.218 20.912 23.827 1.00 19.80 ? 46 GLN A O 1 ATOM 313 C CB . GLN A 1 46 ? 30.305 23.424 23.425 1.00 23.94 ? 46 GLN A CB 1 ATOM 314 C CG . GLN A 1 46 ? 30.279 24.934 23.568 1.00 27.61 ? 46 GLN A CG 1 ATOM 315 C CD . GLN A 1 46 ? 28.945 25.480 24.109 1.00 30.96 ? 46 GLN A CD 1 ATOM 316 O OE1 . GLN A 1 46 ? 27.918 24.741 24.188 1.00 29.60 ? 46 GLN A OE1 1 ATOM 317 N NE2 . GLN A 1 46 ? 28.955 26.787 24.511 1.00 32.15 ? 46 GLN A NE2 1 ATOM 318 N N . SER A 1 47 ? 31.090 20.709 21.889 1.00 18.81 ? 47 SER A N 1 ATOM 319 C CA . SER A 1 47 ? 31.152 19.222 21.926 1.00 18.89 ? 47 SER A CA 1 ATOM 320 C C . SER A 1 47 ? 32.558 18.814 21.564 1.00 18.72 ? 47 SER A C 1 ATOM 321 O O . SER A 1 47 ? 33.110 17.871 22.184 1.00 18.89 ? 47 SER A O 1 ATOM 322 C CB . SER A 1 47 ? 30.179 18.544 20.917 1.00 18.10 ? 47 SER A CB 1 ATOM 323 O OG . SER A 1 47 ? 28.863 18.378 21.435 1.00 17.60 ? 47 SER A OG 1 ATOM 324 N N . PHE A 1 48 ? 33.149 19.526 20.584 1.00 19.32 ? 48 PHE A N 1 ATOM 325 C CA . PHE A 1 48 ? 34.373 19.019 19.911 1.00 19.93 ? 48 PHE A CA 1 ATOM 326 C C . PHE A 1 48 ? 35.734 19.680 20.031 1.00 21.08 ? 48 PHE A C 1 ATOM 327 O O . PHE A 1 48 ? 36.757 19.071 19.629 1.00 20.10 ? 48 PHE A O 1 ATOM 328 C CB . PHE A 1 48 ? 34.064 18.886 18.434 1.00 20.76 ? 48 PHE A CB 1 ATOM 329 C CG . PHE A 1 48 ? 32.857 18.014 18.118 1.00 20.62 ? 48 PHE A CG 1 ATOM 330 C CD1 . PHE A 1 48 ? 32.849 16.692 18.474 1.00 20.99 ? 48 PHE A CD1 1 ATOM 331 C CD2 . PHE A 1 48 ? 31.750 18.528 17.462 1.00 20.53 ? 48 PHE A CD2 1 ATOM 332 C CE1 . PHE A 1 48 ? 31.797 15.874 18.113 1.00 21.37 ? 48 PHE A CE1 1 ATOM 333 C CE2 . PHE A 1 48 ? 30.651 17.732 17.167 1.00 20.54 ? 48 PHE A CE2 1 ATOM 334 C CZ . PHE A 1 48 ? 30.672 16.411 17.491 1.00 20.65 ? 48 PHE A CZ 1 ATOM 335 N N . ASP A 1 49 ? 35.799 20.892 20.571 1.00 22.05 ? 49 ASP A N 1 ATOM 336 C CA . ASP A 1 49 ? 37.037 21.597 20.682 1.00 22.13 ? 49 ASP A CA 1 ATOM 337 C C . ASP A 1 49 ? 38.055 20.815 21.547 1.00 23.32 ? 49 ASP A C 1 ATOM 338 O O . ASP A 1 49 ? 39.324 20.935 21.340 1.00 23.34 ? 49 ASP A O 1 ATOM 339 C CB . ASP A 1 49 ? 36.807 22.923 21.424 1.00 22.89 ? 49 ASP A CB 1 ATOM 340 C CG . ASP A 1 49 ? 36.382 24.051 20.564 1.00 23.13 ? 49 ASP A CG 1 ATOM 341 O OD1 . ASP A 1 49 ? 36.464 23.952 19.323 1.00 21.82 ? 49 ASP A OD1 1 ATOM 342 O OD2 . ASP A 1 49 ? 35.984 25.102 21.166 1.00 22.70 ? 49 ASP A OD2 1 ATOM 343 N N . SER A 1 50 ? 37.552 20.042 22.527 1.00 21.47 ? 50 SER A N 1 ATOM 344 C CA . SER A 1 50 ? 38.406 19.237 23.390 1.00 21.19 ? 50 SER A CA 1 ATOM 345 C C . SER A 1 50 ? 38.833 17.880 22.778 1.00 21.88 ? 50 SER A C 1 ATOM 346 O O . SER A 1 50 ? 39.540 17.069 23.449 1.00 22.26 ? 50 SER A O 1 ATOM 347 C CB . SER A 1 50 ? 37.709 18.957 24.747 1.00 20.81 ? 50 SER A CB 1 ATOM 348 O OG . SER A 1 50 ? 36.494 18.197 24.638 1.00 19.21 ? 50 SER A OG 1 ATOM 349 N N . ASN A 1 51 ? 38.378 17.581 21.572 1.00 21.42 ? 51 ASN A N 1 ATOM 350 C CA . ASN A 1 51 ? 38.528 16.210 21.037 1.00 21.77 ? 51 ASN A CA 1 ATOM 351 C C . ASN A 1 51 ? 38.618 16.226 19.509 1.00 20.62 ? 51 ASN A C 1 ATOM 352 O O . ASN A 1 51 ? 39.742 16.428 18.943 1.00 19.57 ? 51 ASN A O 1 ATOM 353 C CB . ASN A 1 51 ? 37.441 15.203 21.612 1.00 20.99 ? 51 ASN A CB 1 ATOM 354 C CG . ASN A 1 51 ? 36.031 15.753 21.552 1.00 21.93 ? 51 ASN A CG 1 ATOM 355 O OD1 . ASN A 1 51 ? 35.388 15.729 20.509 1.00 21.42 ? 51 ASN A OD1 1 ATOM 356 N ND2 . ASN A 1 51 ? 35.542 16.290 22.693 1.00 23.11 ? 51 ASN A ND2 1 ATOM 357 N N . TRP A 1 52 ? 37.504 16.038 18.823 1.00 19.07 ? 52 TRP A N 1 ATOM 358 C CA . TRP A 1 52 ? 37.597 15.727 17.406 1.00 19.06 ? 52 TRP A CA 1 ATOM 359 C C . TRP A 1 52 ? 37.897 16.898 16.452 1.00 19.53 ? 52 TRP A C 1 ATOM 360 O O . TRP A 1 52 ? 38.293 16.690 15.300 1.00 18.85 ? 52 TRP A O 1 ATOM 361 C CB . TRP A 1 52 ? 36.402 14.924 16.972 1.00 18.34 ? 52 TRP A CB 1 ATOM 362 C CG . TRP A 1 52 ? 36.547 13.493 17.508 1.00 17.00 ? 52 TRP A CG 1 ATOM 363 C CD1 . TRP A 1 52 ? 35.996 13.000 18.638 1.00 16.68 ? 52 TRP A CD1 1 ATOM 364 C CD2 . TRP A 1 52 ? 37.372 12.467 16.972 1.00 16.74 ? 52 TRP A CD2 1 ATOM 365 N NE1 . TRP A 1 52 ? 36.408 11.695 18.836 1.00 17.27 ? 52 TRP A NE1 1 ATOM 366 C CE2 . TRP A 1 52 ? 37.239 11.341 17.815 1.00 17.09 ? 52 TRP A CE2 1 ATOM 367 C CE3 . TRP A 1 52 ? 38.238 12.380 15.858 1.00 17.93 ? 52 TRP A CE3 1 ATOM 368 C CZ2 . TRP A 1 52 ? 37.914 10.156 17.589 1.00 17.60 ? 52 TRP A CZ2 1 ATOM 369 C CZ3 . TRP A 1 52 ? 38.889 11.183 15.619 1.00 17.72 ? 52 TRP A CZ3 1 ATOM 370 C CH2 . TRP A 1 52 ? 38.743 10.099 16.491 1.00 17.90 ? 52 TRP A CH2 1 ATOM 371 N N . ILE A 1 53 ? 37.759 18.122 16.915 1.00 19.47 ? 53 ILE A N 1 ATOM 372 C CA . ILE A 1 53 ? 38.197 19.274 16.089 1.00 19.80 ? 53 ILE A CA 1 ATOM 373 C C . ILE A 1 53 ? 39.727 19.161 15.963 1.00 20.14 ? 53 ILE A C 1 ATOM 374 O O . ILE A 1 53 ? 40.203 19.010 14.847 1.00 21.40 ? 53 ILE A O 1 ATOM 375 C CB . ILE A 1 53 ? 37.629 20.672 16.564 1.00 19.59 ? 53 ILE A CB 1 ATOM 376 C CG1 . ILE A 1 53 ? 36.144 20.761 16.212 1.00 18.78 ? 53 ILE A CG1 1 ATOM 377 C CG2 . ILE A 1 53 ? 38.364 21.850 15.869 1.00 19.34 ? 53 ILE A CG2 1 ATOM 378 C CD1 . ILE A 1 53 ? 35.403 21.886 16.971 1.00 20.07 ? 53 ILE A CD1 1 ATOM 379 N N . PRO A 1 54 ? 40.490 19.191 17.076 1.00 21.77 ? 54 PRO A N 1 ATOM 380 C CA . PRO A 1 54 ? 41.982 19.100 16.897 1.00 21.88 ? 54 PRO A CA 1 ATOM 381 C C . PRO A 1 54 ? 42.426 17.720 16.440 1.00 23.16 ? 54 PRO A C 1 ATOM 382 O O . PRO A 1 54 ? 43.319 17.609 15.571 1.00 22.32 ? 54 PRO A O 1 ATOM 383 C CB . PRO A 1 54 ? 42.553 19.502 18.259 1.00 21.14 ? 54 PRO A CB 1 ATOM 384 C CG . PRO A 1 54 ? 41.377 19.391 19.221 1.00 20.71 ? 54 PRO A CG 1 ATOM 385 C CD . PRO A 1 54 ? 40.135 19.654 18.435 1.00 20.56 ? 54 PRO A CD 1 ATOM 386 N N . LEU A 1 55 ? 41.756 16.660 16.929 1.00 22.71 ? 55 LEU A N 1 ATOM 387 C CA . LEU A 1 55 ? 42.060 15.300 16.398 1.00 23.77 ? 55 LEU A CA 1 ATOM 388 C C . LEU A 1 55 ? 41.844 15.063 14.915 1.00 23.99 ? 55 LEU A C 1 ATOM 389 O O . LEU A 1 55 ? 42.728 14.434 14.193 1.00 23.46 ? 55 LEU A O 1 ATOM 390 C CB . LEU A 1 55 ? 41.337 14.176 17.156 1.00 23.12 ? 55 LEU A CB 1 ATOM 391 C CG . LEU A 1 55 ? 41.786 14.062 18.614 1.00 24.71 ? 55 LEU A CG 1 ATOM 392 C CD1 . LEU A 1 55 ? 40.845 13.061 19.313 1.00 25.21 ? 55 LEU A CD1 1 ATOM 393 C CD2 . LEU A 1 55 ? 43.283 13.729 18.823 1.00 25.90 ? 55 LEU A CD2 1 ATOM 394 N N . SER A 1 56 ? 40.700 15.539 14.431 1.00 22.37 ? 56 SER A N 1 ATOM 395 C CA . SER A 1 56 ? 40.433 15.407 13.007 1.00 22.13 ? 56 SER A CA 1 ATOM 396 C C . SER A 1 56 ? 41.379 16.327 12.154 1.00 22.06 ? 56 SER A C 1 ATOM 397 O O . SER A 1 56 ? 41.834 15.934 11.082 1.00 22.40 ? 56 SER A O 1 ATOM 398 C CB . SER A 1 56 ? 38.967 15.611 12.713 1.00 21.53 ? 56 SER A CB 1 ATOM 399 O OG . SER A 1 56 ? 38.693 16.994 12.664 1.00 22.22 ? 56 SER A OG 1 ATOM 400 N N . THR A 1 57 ? 41.693 17.516 12.631 1.00 22.15 ? 57 THR A N 1 ATOM 401 C CA . THR A 1 57 ? 42.694 18.398 11.963 1.00 23.11 ? 57 THR A CA 1 ATOM 402 C C . THR A 1 57 ? 44.075 17.660 11.861 1.00 24.98 ? 57 THR A C 1 ATOM 403 O O . THR A 1 57 ? 44.725 17.604 10.806 1.00 22.44 ? 57 THR A O 1 ATOM 404 C CB . THR A 1 57 ? 42.905 19.682 12.800 1.00 22.19 ? 57 THR A CB 1 ATOM 405 O OG1 . THR A 1 57 ? 41.674 20.407 12.959 1.00 23.37 ? 57 THR A OG1 1 ATOM 406 C CG2 . THR A 1 57 ? 43.960 20.597 12.201 1.00 22.96 ? 57 THR A CG2 1 ATOM 407 N N . GLN A 1 58 ? 44.466 17.030 12.991 1.00 26.35 ? 58 GLN A N 1 ATOM 408 C CA . GLN A 1 58 ? 45.727 16.304 13.085 1.00 28.64 ? 58 GLN A CA 1 ATOM 409 C C . GLN A 1 58 ? 45.762 15.048 12.219 1.00 29.63 ? 58 GLN A C 1 ATOM 410 O O . GLN A 1 58 ? 46.855 14.540 11.984 1.00 32.32 ? 58 GLN A O 1 ATOM 411 C CB . GLN A 1 58 ? 46.071 16.048 14.578 1.00 28.79 ? 58 GLN A CB 1 ATOM 412 C CG . GLN A 1 58 ? 46.417 17.376 15.213 1.00 31.13 ? 58 GLN A CG 1 ATOM 413 C CD . GLN A 1 58 ? 47.092 17.297 16.578 1.00 34.00 ? 58 GLN A CD 1 ATOM 414 O OE1 . GLN A 1 58 ? 46.771 16.388 17.402 1.00 31.08 ? 58 GLN A OE1 1 ATOM 415 N NE2 . GLN A 1 58 ? 48.006 18.302 16.855 1.00 34.74 ? 58 GLN A NE2 1 ATOM 416 N N . LEU A 1 59 ? 44.575 14.597 11.726 1.00 29.26 ? 59 LEU A N 1 ATOM 417 C CA . LEU A 1 59 ? 44.426 13.498 10.766 1.00 27.90 ? 59 LEU A CA 1 ATOM 418 C C . LEU A 1 59 ? 44.328 13.983 9.306 1.00 29.33 ? 59 LEU A C 1 ATOM 419 O O . LEU A 1 59 ? 44.156 13.151 8.406 1.00 28.51 ? 59 LEU A O 1 ATOM 420 C CB . LEU A 1 59 ? 43.178 12.644 11.103 1.00 27.77 ? 59 LEU A CB 1 ATOM 421 C CG . LEU A 1 59 ? 43.358 11.743 12.331 1.00 27.42 ? 59 LEU A CG 1 ATOM 422 C CD1 . LEU A 1 59 ? 42.022 11.165 12.798 1.00 27.48 ? 59 LEU A CD1 1 ATOM 423 C CD2 . LEU A 1 59 ? 44.372 10.645 12.063 1.00 27.47 ? 59 LEU A CD2 1 ATOM 424 N N . GLY A 1 60 ? 44.438 15.297 9.089 1.00 26.33 ? 60 GLY A N 1 ATOM 425 C CA . GLY A 1 60 ? 44.527 15.836 7.739 1.00 27.80 ? 60 GLY A CA 1 ATOM 426 C C . GLY A 1 60 ? 43.234 16.397 7.151 1.00 27.06 ? 60 GLY A C 1 ATOM 427 O O . GLY A 1 60 ? 43.205 16.765 5.968 1.00 27.49 ? 60 GLY A O 1 ATOM 428 N N . TYR A 1 61 ? 42.162 16.466 7.954 1.00 24.39 ? 61 TYR A N 1 ATOM 429 C CA . TYR A 1 61 ? 40.843 17.064 7.501 1.00 23.24 ? 61 TYR A CA 1 ATOM 430 C C . TYR A 1 61 ? 40.675 18.538 7.797 1.00 20.56 ? 61 TYR A C 1 ATOM 431 O O . TYR A 1 61 ? 41.324 19.094 8.654 1.00 20.56 ? 61 TYR A O 1 ATOM 432 C CB . TYR A 1 61 ? 39.655 16.349 8.220 1.00 23.29 ? 61 TYR A CB 1 ATOM 433 C CG . TYR A 1 61 ? 39.609 14.907 7.921 1.00 23.95 ? 61 TYR A CG 1 ATOM 434 C CD1 . TYR A 1 61 ? 38.863 14.434 6.846 1.00 24.30 ? 61 TYR A CD1 1 ATOM 435 C CD2 . TYR A 1 61 ? 40.343 13.987 8.714 1.00 25.51 ? 61 TYR A CD2 1 ATOM 436 C CE1 . TYR A 1 61 ? 38.823 13.071 6.568 1.00 25.43 ? 61 TYR A CE1 1 ATOM 437 C CE2 . TYR A 1 61 ? 40.312 12.622 8.442 1.00 26.47 ? 61 TYR A CE2 1 ATOM 438 C CZ . TYR A 1 61 ? 39.578 12.186 7.371 1.00 26.41 ? 61 TYR A CZ 1 ATOM 439 O OH . TYR A 1 61 ? 39.545 10.864 7.111 1.00 29.63 ? 61 TYR A OH 1 ATOM 440 N N . THR A 1 62 ? 39.707 19.147 7.155 1.00 19.83 ? 62 THR A N 1 ATOM 441 C CA . THR A 1 62 ? 39.199 20.411 7.644 1.00 19.67 ? 62 THR A CA 1 ATOM 442 C C . THR A 1 62 ? 37.891 20.113 8.424 1.00 19.68 ? 62 THR A C 1 ATOM 443 O O . THR A 1 62 ? 36.879 19.732 7.807 1.00 19.46 ? 62 THR A O 1 ATOM 444 C CB . THR A 1 62 ? 38.914 21.463 6.526 1.00 19.94 ? 62 THR A CB 1 ATOM 445 O OG1 . THR A 1 62 ? 40.072 21.657 5.695 1.00 20.44 ? 62 THR A OG1 1 ATOM 446 C CG2 . THR A 1 62 ? 38.521 22.839 7.124 1.00 19.32 ? 62 THR A CG2 1 ATOM 447 N N . PRO A 1 63 ? 37.897 20.370 9.741 1.00 19.46 ? 63 PRO A N 1 ATOM 448 C CA . PRO A 1 63 ? 36.706 20.172 10.541 1.00 19.66 ? 63 PRO A CA 1 ATOM 449 C C . PRO A 1 63 ? 35.680 21.272 10.291 1.00 19.95 ? 63 PRO A C 1 ATOM 450 O O . PRO A 1 63 ? 36.043 22.462 10.168 1.00 20.12 ? 63 PRO A O 1 ATOM 451 C CB . PRO A 1 63 ? 37.241 20.196 11.985 1.00 19.29 ? 63 PRO A CB 1 ATOM 452 C CG . PRO A 1 63 ? 38.516 20.964 11.971 1.00 19.78 ? 63 PRO A CG 1 ATOM 453 C CD . PRO A 1 63 ? 39.088 20.711 10.584 1.00 20.19 ? 63 PRO A CD 1 ATOM 454 N N . CYS A 1 64 ? 34.477 20.829 9.975 1.00 20.52 ? 64 CYS A N 1 ATOM 455 C CA . CYS A 1 64 ? 33.312 21.673 9.834 1.00 19.91 ? 64 CYS A CA 1 ATOM 456 C C . CYS A 1 64 ? 32.304 21.133 10.822 1.00 19.36 ? 64 CYS A C 1 ATOM 457 O O . CYS A 1 64 ? 32.358 19.967 11.207 1.00 18.98 ? 64 CYS A O 1 ATOM 458 C CB . CYS A 1 64 ? 32.759 21.618 8.427 1.00 21.12 ? 64 CYS A CB 1 ATOM 459 S SG . CYS A 1 64 ? 34.031 21.982 7.176 1.00 23.00 ? 64 CYS A SG 1 ATOM 460 N N . TRP A 1 65 ? 31.384 21.975 11.224 1.00 18.85 ? 65 TRP A N 1 ATOM 461 C CA . TRP A 1 65 ? 30.380 21.603 12.180 1.00 19.12 ? 65 TRP A CA 1 ATOM 462 C C . TRP A 1 65 ? 29.165 22.496 11.999 1.00 18.81 ? 65 TRP A C 1 ATOM 463 O O . TRP A 1 65 ? 29.207 23.558 11.362 1.00 19.71 ? 65 TRP A O 1 ATOM 464 C CB . TRP A 1 65 ? 30.903 21.684 13.636 1.00 19.90 ? 65 TRP A CB 1 ATOM 465 C CG . TRP A 1 65 ? 31.509 23.033 13.961 1.00 21.31 ? 65 TRP A CG 1 ATOM 466 C CD1 . TRP A 1 65 ? 30.856 24.165 14.412 1.00 22.36 ? 65 TRP A CD1 1 ATOM 467 C CD2 . TRP A 1 65 ? 32.892 23.400 13.801 1.00 22.87 ? 65 TRP A CD2 1 ATOM 468 N NE1 . TRP A 1 65 ? 31.763 25.205 14.548 1.00 22.51 ? 65 TRP A NE1 1 ATOM 469 C CE2 . TRP A 1 65 ? 33.016 24.752 14.198 1.00 23.82 ? 65 TRP A CE2 1 ATOM 470 C CE3 . TRP A 1 65 ? 34.053 22.696 13.367 1.00 23.03 ? 65 TRP A CE3 1 ATOM 471 C CZ2 . TRP A 1 65 ? 34.252 25.428 14.155 1.00 25.66 ? 65 TRP A CZ2 1 ATOM 472 C CZ3 . TRP A 1 65 ? 35.251 23.357 13.289 1.00 24.03 ? 65 TRP A CZ3 1 ATOM 473 C CH2 . TRP A 1 65 ? 35.351 24.725 13.676 1.00 25.60 ? 65 TRP A CH2 1 ATOM 474 N N . ILE A 1 66 ? 28.079 22.016 12.565 1.00 18.85 ? 66 ILE A N 1 ATOM 475 C CA . ILE A 1 66 ? 26.859 22.770 12.697 1.00 18.41 ? 66 ILE A CA 1 ATOM 476 C C . ILE A 1 66 ? 26.587 23.044 14.174 1.00 17.50 ? 66 ILE A C 1 ATOM 477 O O . ILE A 1 66 ? 26.887 22.229 15.063 1.00 16.89 ? 66 ILE A O 1 ATOM 478 C CB . ILE A 1 66 ? 25.624 22.049 12.044 1.00 19.02 ? 66 ILE A CB 1 ATOM 479 C CG1 . ILE A 1 66 ? 25.485 20.574 12.502 1.00 19.55 ? 66 ILE A CG1 1 ATOM 480 C CG2 . ILE A 1 66 ? 25.670 22.083 10.570 1.00 19.57 ? 66 ILE A CG2 1 ATOM 481 C CD1 . ILE A 1 66 ? 24.120 19.979 12.166 1.00 19.91 ? 66 ILE A CD1 1 ATOM 482 N N . SER A 1 67 ? 25.886 24.147 14.437 1.00 17.78 ? 67 SER A N 1 ATOM 483 C CA . SER A 1 67 ? 25.504 24.539 15.786 1.00 18.29 ? 67 SER A CA 1 ATOM 484 C C . SER A 1 67 ? 24.022 24.907 15.878 1.00 18.70 ? 67 SER A C 1 ATOM 485 O O . SER A 1 67 ? 23.705 26.064 16.038 1.00 19.04 ? 67 SER A O 1 ATOM 486 C CB . SER A 1 67 ? 26.423 25.684 16.315 1.00 18.72 ? 67 SER A CB 1 ATOM 487 O OG . SER A 1 67 ? 27.722 25.184 16.395 1.00 18.42 ? 67 SER A OG 1 ATOM 488 N N . PRO A 1 68 ? 23.111 23.930 15.628 1.00 18.44 ? 68 PRO A N 1 ATOM 489 C CA . PRO A 1 68 ? 21.711 24.291 15.619 1.00 18.29 ? 68 PRO A CA 1 ATOM 490 C C . PRO A 1 68 ? 21.314 24.905 16.956 1.00 18.46 ? 68 PRO A C 1 ATOM 491 O O . PRO A 1 68 ? 21.619 24.310 18.020 1.00 18.52 ? 68 PRO A O 1 ATOM 492 C CB . PRO A 1 68 ? 20.986 23.001 15.373 1.00 18.00 ? 68 PRO A CB 1 ATOM 493 C CG . PRO A 1 68 ? 22.018 22.121 14.715 1.00 18.05 ? 68 PRO A CG 1 ATOM 494 C CD . PRO A 1 68 ? 23.303 22.495 15.362 1.00 18.86 ? 68 PRO A CD 1 ATOM 495 N N . PRO A 1 69 ? 20.630 26.055 16.905 1.00 19.12 ? 69 PRO A N 1 ATOM 496 C CA . PRO A 1 69 ? 20.334 26.726 18.146 1.00 19.65 ? 69 PRO A CA 1 ATOM 497 C C . PRO A 1 69 ? 18.972 26.273 18.746 1.00 20.60 ? 69 PRO A C 1 ATOM 498 O O . PRO A 1 69 ? 18.131 25.681 18.030 1.00 19.76 ? 69 PRO A O 1 ATOM 499 C CB . PRO A 1 69 ? 20.313 28.212 17.735 1.00 20.12 ? 69 PRO A CB 1 ATOM 500 C CG . PRO A 1 69 ? 19.798 28.191 16.313 1.00 20.08 ? 69 PRO A CG 1 ATOM 501 C CD . PRO A 1 69 ? 20.229 26.885 15.719 1.00 19.81 ? 69 PRO A CD 1 ATOM 502 N N . PRO A 1 70 ? 18.786 26.432 20.063 1.00 20.60 ? 70 PRO A N 1 ATOM 503 C CA . PRO A 1 70 ? 19.825 26.771 21.023 1.00 20.67 ? 70 PRO A CA 1 ATOM 504 C C . PRO A 1 70 ? 20.453 25.489 21.544 1.00 20.14 ? 70 PRO A C 1 ATOM 505 O O . PRO A 1 70 ? 19.760 24.698 22.104 1.00 18.96 ? 70 PRO A O 1 ATOM 506 C CB . PRO A 1 70 ? 19.013 27.434 22.145 1.00 21.63 ? 70 PRO A CB 1 ATOM 507 C CG . PRO A 1 70 ? 17.616 26.866 22.034 1.00 21.55 ? 70 PRO A CG 1 ATOM 508 C CD . PRO A 1 70 ? 17.503 26.157 20.709 1.00 20.78 ? 70 PRO A CD 1 ATOM 509 N N . PHE A 1 71 ? 21.745 25.306 21.356 1.00 19.52 ? 71 PHE A N 1 ATOM 510 C CA . PHE A 1 71 ? 22.487 24.200 21.958 1.00 20.24 ? 71 PHE A CA 1 ATOM 511 C C . PHE A 1 71 ? 21.917 22.785 21.675 1.00 19.12 ? 71 PHE A C 1 ATOM 512 O O . PHE A 1 71 ? 21.907 21.943 22.550 1.00 18.64 ? 71 PHE A O 1 ATOM 513 C CB . PHE A 1 71 ? 22.613 24.472 23.497 1.00 20.97 ? 71 PHE A CB 1 ATOM 514 C CG . PHE A 1 71 ? 23.219 25.831 23.806 1.00 22.66 ? 71 PHE A CG 1 ATOM 515 C CD1 . PHE A 1 71 ? 24.600 26.043 23.645 1.00 24.10 ? 71 PHE A CD1 1 ATOM 516 C CD2 . PHE A 1 71 ? 22.425 26.910 24.235 1.00 23.58 ? 71 PHE A CD2 1 ATOM 517 C CE1 . PHE A 1 71 ? 25.183 27.288 23.882 1.00 25.12 ? 71 PHE A CE1 1 ATOM 518 C CE2 . PHE A 1 71 ? 22.995 28.140 24.444 1.00 24.21 ? 71 PHE A CE2 1 ATOM 519 C CZ . PHE A 1 71 ? 24.378 28.329 24.270 1.00 24.85 ? 71 PHE A CZ 1 ATOM 520 N N . MET A 1 72 ? 21.361 22.559 20.473 1.00 18.36 ? 72 MET A N 1 ATOM 521 C CA . MET A 1 72 ? 20.789 21.276 20.134 1.00 17.91 ? 72 MET A CA 1 ATOM 522 C C . MET A 1 72 ? 19.574 20.838 21.007 1.00 17.27 ? 72 MET A C 1 ATOM 523 O O . MET A 1 72 ? 19.218 19.632 21.066 1.00 17.11 ? 72 MET A O 1 ATOM 524 C CB . MET A 1 72 ? 21.905 20.171 20.106 1.00 17.50 ? 72 MET A CB 1 ATOM 525 C CG . MET A 1 72 ? 22.957 20.363 18.966 1.00 17.35 ? 72 MET A CG 1 ATOM 526 S SD . MET A 1 72 ? 22.272 19.806 17.386 1.00 17.68 ? 72 MET A SD 1 ATOM 527 C CE . MET A 1 72 ? 22.084 18.072 17.699 1.00 17.85 ? 72 MET A CE 1 ATOM 528 N N . LEU A 1 73 ? 18.939 21.810 21.658 1.00 17.13 ? 73 LEU A N 1 ATOM 529 C CA . LEU A 1 73 ? 17.762 21.581 22.486 1.00 17.24 ? 73 LEU A CA 1 ATOM 530 C C . LEU A 1 73 ? 16.417 21.649 21.711 1.00 16.69 ? 73 LEU A C 1 ATOM 531 O O . LEU A 1 73 ? 15.410 21.218 22.218 1.00 16.62 ? 73 LEU A O 1 ATOM 532 C CB . LEU A 1 73 ? 17.742 22.663 23.590 1.00 18.32 ? 73 LEU A CB 1 ATOM 533 C CG . LEU A 1 73 ? 18.959 22.561 24.537 1.00 18.84 ? 73 LEU A CG 1 ATOM 534 C CD1 . LEU A 1 73 ? 18.862 23.581 25.673 1.00 19.34 ? 73 LEU A CD1 1 ATOM 535 C CD2 . LEU A 1 73 ? 19.095 21.163 25.117 1.00 19.34 ? 73 LEU A CD2 1 ATOM 536 N N . ASN A 1 74 ? 16.410 22.310 20.554 1.00 17.42 ? 74 ASN A N 1 ATOM 537 C CA . ASN A 1 74 ? 15.222 22.444 19.721 1.00 18.28 ? 74 ASN A CA 1 ATOM 538 C C . ASN A 1 74 ? 15.023 21.202 18.835 1.00 17.55 ? 74 ASN A C 1 ATOM 539 O O . ASN A 1 74 ? 15.897 20.321 18.808 1.00 16.36 ? 74 ASN A O 1 ATOM 540 C CB . ASN A 1 74 ? 15.203 23.751 18.966 1.00 20.05 ? 74 ASN A CB 1 ATOM 541 C CG . ASN A 1 74 ? 14.363 24.829 19.696 1.00 22.37 ? 74 ASN A CG 1 ATOM 542 O OD1 . ASN A 1 74 ? 13.963 24.674 20.855 1.00 20.21 ? 74 ASN A OD1 1 ATOM 543 N ND2 . ASN A 1 74 ? 14.137 25.928 18.996 1.00 25.12 ? 74 ASN A ND2 1 ATOM 544 N N . ASP A 1 75 ? 13.824 21.123 18.268 1.00 17.40 ? 75 ASP A N 1 ATOM 545 C CA . ASP A 1 75 ? 13.318 20.017 17.430 1.00 16.74 ? 75 ASP A CA 1 ATOM 546 C C . ASP A 1 75 ? 14.502 19.367 16.672 1.00 17.18 ? 75 ASP A C 1 ATOM 547 O O . ASP A 1 75 ? 15.167 20.014 15.844 1.00 15.35 ? 75 ASP A O 1 ATOM 548 C CB . ASP A 1 75 ? 12.282 20.649 16.491 1.00 16.47 ? 75 ASP A CB 1 ATOM 549 C CG . ASP A 1 75 ? 11.612 19.698 15.561 1.00 16.04 ? 75 ASP A CG 1 ATOM 550 O OD1 . ASP A 1 75 ? 11.968 18.527 15.506 1.00 15.88 ? 75 ASP A OD1 1 ATOM 551 O OD2 . ASP A 1 75 ? 10.685 20.150 14.841 1.00 16.08 ? 75 ASP A OD2 1 ATOM 552 N N . THR A 1 76 ? 14.711 18.077 16.956 1.00 16.26 ? 76 THR A N 1 ATOM 553 C CA . THR A 1 76 ? 15.674 17.226 16.241 1.00 16.92 ? 76 THR A CA 1 ATOM 554 C C . THR A 1 76 ? 15.505 17.233 14.754 1.00 16.05 ? 76 THR A C 1 ATOM 555 O O . THR A 1 76 ? 16.500 17.220 14.004 1.00 15.24 ? 76 THR A O 1 ATOM 556 C CB . THR A 1 76 ? 15.641 15.776 16.827 1.00 17.15 ? 76 THR A CB 1 ATOM 557 O OG1 . THR A 1 76 ? 16.048 15.791 18.231 1.00 17.73 ? 76 THR A OG1 1 ATOM 558 C CG2 . THR A 1 76 ? 16.552 14.818 16.076 1.00 17.49 ? 76 THR A CG2 1 ATOM 559 N N . GLN A 1 77 ? 14.259 17.374 14.278 1.00 16.75 ? 77 GLN A N 1 ATOM 560 C CA . GLN A 1 77 ? 14.005 17.436 12.839 1.00 16.66 ? 77 GLN A CA 1 ATOM 561 C C . GLN A 1 77 ? 14.611 18.735 12.213 1.00 17.56 ? 77 GLN A C 1 ATOM 562 O O . GLN A 1 77 ? 15.045 18.724 11.048 1.00 17.23 ? 77 GLN A O 1 ATOM 563 C CB . GLN A 1 77 ? 12.523 17.359 12.533 1.00 16.41 ? 77 GLN A CB 1 ATOM 564 C CG . GLN A 1 77 ? 11.905 16.047 13.096 1.00 17.10 ? 77 GLN A CG 1 ATOM 565 C CD . GLN A 1 77 ? 10.399 16.055 13.039 1.00 16.53 ? 77 GLN A CD 1 ATOM 566 O OE1 . GLN A 1 77 ? 9.789 15.348 12.239 1.00 17.41 ? 77 GLN A OE1 1 ATOM 567 N NE2 . GLN A 1 77 ? 9.791 16.874 13.894 1.00 16.65 ? 77 GLN A NE2 1 ATOM 568 N N . VAL A 1 78 ? 14.560 19.820 12.966 1.00 17.00 ? 78 VAL A N 1 ATOM 569 C CA . VAL A 1 78 ? 15.140 21.104 12.541 1.00 17.09 ? 78 VAL A CA 1 ATOM 570 C C . VAL A 1 78 ? 16.660 20.971 12.639 1.00 16.99 ? 78 VAL A C 1 ATOM 571 O O . VAL A 1 78 ? 17.394 21.389 11.722 1.00 16.14 ? 78 VAL A O 1 ATOM 572 C CB . VAL A 1 78 ? 14.619 22.333 13.329 1.00 17.13 ? 78 VAL A CB 1 ATOM 573 C CG1 . VAL A 1 78 ? 15.412 23.597 12.960 1.00 17.99 ? 78 VAL A CG1 1 ATOM 574 C CG2 . VAL A 1 78 ? 13.117 22.545 13.120 1.00 17.45 ? 78 VAL A CG2 1 ATOM 575 N N . ASN A 1 79 ? 17.159 20.333 13.717 1.00 16.50 ? 79 ASN A N 1 ATOM 576 C CA . ASN A 1 79 ? 18.613 20.129 13.816 1.00 16.22 ? 79 ASN A CA 1 ATOM 577 C C . ASN A 1 79 ? 19.156 19.367 12.626 1.00 15.48 ? 79 ASN A C 1 ATOM 578 O O . ASN A 1 79 ? 20.263 19.648 12.082 1.00 14.75 ? 79 ASN A O 1 ATOM 579 C CB . ASN A 1 79 ? 18.942 19.381 15.142 1.00 16.28 ? 79 ASN A CB 1 ATOM 580 C CG . ASN A 1 79 ? 18.469 20.151 16.372 1.00 16.54 ? 79 ASN A CG 1 ATOM 581 O OD1 . ASN A 1 79 ? 18.162 21.383 16.335 1.00 17.07 ? 79 ASN A OD1 1 ATOM 582 N ND2 . ASN A 1 79 ? 18.409 19.434 17.481 1.00 15.91 ? 79 ASN A ND2 1 ATOM 583 N N . THR A 1 80 ? 18.350 18.412 12.152 1.00 15.44 ? 80 THR A N 1 ATOM 584 C CA . THR A 1 80 ? 18.735 17.628 10.989 1.00 16.04 ? 80 THR A CA 1 ATOM 585 C C . THR A 1 80 ? 18.752 18.512 9.708 1.00 16.62 ? 80 THR A C 1 ATOM 586 O O . THR A 1 80 ? 19.581 18.301 8.846 1.00 16.03 ? 80 THR A O 1 ATOM 587 C CB . THR A 1 80 ? 17.831 16.435 10.772 1.00 15.76 ? 80 THR A CB 1 ATOM 588 O OG1 . THR A 1 80 ? 17.826 15.674 11.956 1.00 15.83 ? 80 THR A OG1 1 ATOM 589 C CG2 . THR A 1 80 ? 18.346 15.542 9.633 1.00 15.96 ? 80 THR A CG2 1 ATOM 590 N N . GLU A 1 81 ? 17.874 19.509 9.607 1.00 16.82 ? 81 GLU A N 1 ATOM 591 C CA . GLU A 1 81 ? 17.920 20.413 8.436 1.00 16.90 ? 81 GLU A CA 1 ATOM 592 C C . GLU A 1 81 ? 19.296 21.039 8.297 1.00 17.38 ? 81 GLU A C 1 ATOM 593 O O . GLU A 1 81 ? 19.864 21.102 7.206 1.00 16.72 ? 81 GLU A O 1 ATOM 594 C CB . GLU A 1 81 ? 16.889 21.533 8.554 1.00 18.06 ? 81 GLU A CB 1 ATOM 595 C CG . GLU A 1 81 ? 15.449 21.005 8.563 1.00 18.00 ? 81 GLU A CG 1 ATOM 596 C CD . GLU A 1 81 ? 14.386 22.084 8.637 1.00 18.68 ? 81 GLU A CD 1 ATOM 597 O OE1 . GLU A 1 81 ? 14.598 23.236 8.165 1.00 20.30 ? 81 GLU A OE1 1 ATOM 598 O OE2 . GLU A 1 81 ? 13.332 21.814 9.280 1.00 18.98 ? 81 GLU A OE2 1 ATOM 599 N N . TYR A 1 82 ? 19.853 21.493 9.433 1.00 17.49 ? 82 TYR A N 1 ATOM 600 C CA . TYR A 1 82 ? 21.219 22.010 9.409 1.00 16.86 ? 82 TYR A CA 1 ATOM 601 C C . TYR A 1 82 ? 22.227 20.982 8.840 1.00 16.39 ? 82 TYR A C 1 ATOM 602 O O . TYR A 1 82 ? 23.084 21.299 8.006 1.00 15.68 ? 82 TYR A O 1 ATOM 603 C CB . TYR A 1 82 ? 21.646 22.439 10.837 1.00 17.27 ? 82 TYR A CB 1 ATOM 604 C CG . TYR A 1 82 ? 21.050 23.751 11.301 1.00 17.43 ? 82 TYR A CG 1 ATOM 605 C CD1 . TYR A 1 82 ? 19.845 23.764 12.037 1.00 18.27 ? 82 TYR A CD1 1 ATOM 606 C CD2 . TYR A 1 82 ? 21.654 24.993 10.997 1.00 17.79 ? 82 TYR A CD2 1 ATOM 607 C CE1 . TYR A 1 82 ? 19.256 24.980 12.487 1.00 17.56 ? 82 TYR A CE1 1 ATOM 608 C CE2 . TYR A 1 82 ? 21.088 26.213 11.474 1.00 18.37 ? 82 TYR A CE2 1 ATOM 609 C CZ . TYR A 1 82 ? 19.893 26.175 12.205 1.00 18.39 ? 82 TYR A CZ 1 ATOM 610 O OH . TYR A 1 82 ? 19.304 27.318 12.662 1.00 19.07 ? 82 TYR A OH 1 ATOM 611 N N . MET A 1 83 ? 22.116 19.763 9.299 1.00 16.29 ? 83 MET A N 1 ATOM 612 C CA . MET A 1 83 ? 22.994 18.740 8.860 1.00 17.74 ? 83 MET A CA 1 ATOM 613 C C . MET A 1 83 ? 22.907 18.409 7.352 1.00 17.53 ? 83 MET A C 1 ATOM 614 O O . MET A 1 83 ? 23.927 18.371 6.662 1.00 16.23 ? 83 MET A O 1 ATOM 615 C CB . MET A 1 83 ? 22.812 17.498 9.697 1.00 20.31 ? 83 MET A CB 1 ATOM 616 C CG . MET A 1 83 ? 23.996 16.631 9.399 1.00 23.52 ? 83 MET A CG 1 ATOM 617 S SD . MET A 1 83 ? 23.563 14.962 9.117 1.00 35.36 ? 83 MET A SD 1 ATOM 618 C CE . MET A 1 83 ? 22.500 15.030 7.808 1.00 24.82 ? 83 MET A CE 1 ATOM 619 N N . VAL A 1 84 ? 21.700 18.202 6.871 1.00 16.30 ? 84 VAL A N 1 ATOM 620 C CA . VAL A 1 84 ? 21.430 17.908 5.423 1.00 16.98 ? 84 VAL A CA 1 ATOM 621 C C . VAL A 1 84 ? 21.947 19.043 4.536 1.00 17.57 ? 84 VAL A C 1 ATOM 622 O O . VAL A 1 84 ? 22.695 18.822 3.612 1.00 17.11 ? 84 VAL A O 1 ATOM 623 C CB . VAL A 1 84 ? 19.911 17.632 5.227 1.00 16.34 ? 84 VAL A CB 1 ATOM 624 C CG1 . VAL A 1 84 ? 19.502 17.499 3.755 1.00 17.13 ? 84 VAL A CG1 1 ATOM 625 C CG2 . VAL A 1 84 ? 19.496 16.417 6.018 1.00 16.69 ? 84 VAL A CG2 1 ATOM 626 N N . ASN A 1 85 ? 21.501 20.272 4.809 1.00 18.23 ? 85 ASN A N 1 ATOM 627 C CA . ASN A 1 85 ? 22.048 21.471 4.133 1.00 18.18 ? 85 ASN A CA 1 ATOM 628 C C . ASN A 1 85 ? 23.603 21.515 4.114 1.00 18.74 ? 85 ASN A C 1 ATOM 629 O O . ASN A 1 85 ? 24.232 21.826 3.075 1.00 18.79 ? 85 ASN A O 1 ATOM 630 C CB . ASN A 1 85 ? 21.491 22.754 4.776 1.00 17.72 ? 85 ASN A CB 1 ATOM 631 C CG . ASN A 1 85 ? 21.981 24.018 4.057 1.00 19.09 ? 85 ASN A CG 1 ATOM 632 O OD1 . ASN A 1 85 ? 21.603 24.263 2.912 1.00 19.33 ? 85 ASN A OD1 1 ATOM 633 N ND2 . ASN A 1 85 ? 22.823 24.824 4.736 1.00 18.54 ? 85 ASN A ND2 1 ATOM 634 N N . ALA A 1 86 ? 24.210 21.153 5.245 1.00 19.04 ? 86 ALA A N 1 ATOM 635 C CA . ALA A 1 86 ? 25.641 21.112 5.351 1.00 19.31 ? 86 ALA A CA 1 ATOM 636 C C . ALA A 1 86 ? 26.286 20.131 4.449 1.00 19.11 ? 86 ALA A C 1 ATOM 637 O O . ALA A 1 86 ? 27.256 20.492 3.759 1.00 19.00 ? 86 ALA A O 1 ATOM 638 C CB . ALA A 1 86 ? 26.102 20.973 6.798 1.00 18.89 ? 86 ALA A CB 1 ATOM 639 N N . ILE A 1 87 ? 25.747 18.915 4.409 1.00 19.34 ? 87 ILE A N 1 ATOM 640 C CA . ILE A 1 87 ? 26.250 17.875 3.503 1.00 20.19 ? 87 ILE A CA 1 ATOM 641 C C . ILE A 1 87 ? 26.148 18.312 2.009 1.00 21.45 ? 87 ILE A C 1 ATOM 642 O O . ILE A 1 87 ? 27.140 18.229 1.258 1.00 22.50 ? 87 ILE A O 1 ATOM 643 C CB . ILE A 1 87 ? 25.537 16.534 3.697 1.00 20.25 ? 87 ILE A CB 1 ATOM 644 C CG1 . ILE A 1 87 ? 25.758 15.992 5.120 1.00 20.10 ? 87 ILE A CG1 1 ATOM 645 C CG2 . ILE A 1 87 ? 25.972 15.586 2.584 1.00 19.84 ? 87 ILE A CG2 1 ATOM 646 C CD1 . ILE A 1 87 ? 27.209 15.755 5.378 1.00 21.48 ? 87 ILE A CD1 1 ATOM 647 N N . THR A 1 88 ? 24.991 18.854 1.615 1.00 21.23 ? 88 THR A N 1 ATOM 648 C CA . THR A 1 88 ? 24.845 19.417 0.266 1.00 20.03 ? 88 THR A CA 1 ATOM 649 C C . THR A 1 88 ? 25.940 20.500 -0.029 1.00 20.52 ? 88 THR A C 1 ATOM 650 O O . THR A 1 88 ? 26.673 20.400 -1.009 1.00 20.01 ? 88 THR A O 1 ATOM 651 C CB . THR A 1 88 ? 23.452 20.013 0.145 1.00 19.90 ? 88 THR A CB 1 ATOM 652 O OG1 . THR A 1 88 ? 22.511 19.023 0.499 1.00 19.04 ? 88 THR A OG1 1 ATOM 653 C CG2 . THR A 1 88 ? 23.155 20.614 -1.252 1.00 20.07 ? 88 THR A CG2 1 ATOM 654 N N . ALA A 1 89 ? 26.087 21.487 0.859 1.00 19.94 ? 89 ALA A N 1 ATOM 655 C CA . ALA A 1 89 ? 27.101 22.524 0.690 1.00 19.82 ? 89 ALA A CA 1 ATOM 656 C C . ALA A 1 89 ? 28.560 22.008 0.636 1.00 19.88 ? 89 ALA A C 1 ATOM 657 O O . ALA A 1 89 ? 29.331 22.450 -0.183 1.00 20.09 ? 89 ALA A O 1 ATOM 658 C CB . ALA A 1 89 ? 26.970 23.553 1.791 1.00 19.53 ? 89 ALA A CB 1 ATOM 659 N N . LEU A 1 90 ? 28.912 21.085 1.512 1.00 19.09 ? 90 LEU A N 1 ATOM 660 C CA . LEU A 1 90 ? 30.302 20.615 1.640 1.00 20.72 ? 90 LEU A CA 1 ATOM 661 C C . LEU A 1 90 ? 30.707 19.616 0.585 1.00 21.56 ? 90 LEU A C 1 ATOM 662 O O . LEU A 1 90 ? 31.893 19.581 0.171 1.00 22.47 ? 90 LEU A O 1 ATOM 663 C CB . LEU A 1 90 ? 30.544 20.018 3.028 1.00 20.66 ? 90 LEU A CB 1 ATOM 664 C CG . LEU A 1 90 ? 30.454 21.008 4.186 1.00 20.35 ? 90 LEU A CG 1 ATOM 665 C CD1 . LEU A 1 90 ? 30.310 20.207 5.513 1.00 20.15 ? 90 LEU A CD1 1 ATOM 666 C CD2 . LEU A 1 90 ? 31.664 21.927 4.167 1.00 20.86 ? 90 LEU A CD2 1 ATOM 667 N N . TYR A 1 91 ? 29.722 18.842 0.122 1.00 21.68 ? 91 TYR A N 1 ATOM 668 C CA . TYR A 1 91 ? 29.920 17.985 -1.069 1.00 22.28 ? 91 TYR A CA 1 ATOM 669 C C . TYR A 1 91 ? 30.313 18.895 -2.268 1.00 23.02 ? 91 TYR A C 1 ATOM 670 O O . TYR A 1 91 ? 31.354 18.669 -2.908 1.00 22.02 ? 91 TYR A O 1 ATOM 671 C CB . TYR A 1 91 ? 28.640 17.270 -1.399 1.00 22.05 ? 91 TYR A CB 1 ATOM 672 C CG . TYR A 1 91 ? 28.731 16.290 -2.564 1.00 22.80 ? 91 TYR A CG 1 ATOM 673 C CD1 . TYR A 1 91 ? 29.364 15.049 -2.407 1.00 22.66 ? 91 TYR A CD1 1 ATOM 674 C CD2 . TYR A 1 91 ? 28.156 16.584 -3.758 1.00 24.01 ? 91 TYR A CD2 1 ATOM 675 C CE1 . TYR A 1 91 ? 29.430 14.141 -3.429 1.00 23.61 ? 91 TYR A CE1 1 ATOM 676 C CE2 . TYR A 1 91 ? 28.218 15.696 -4.798 1.00 25.28 ? 91 TYR A CE2 1 ATOM 677 C CZ . TYR A 1 91 ? 28.827 14.466 -4.599 1.00 25.51 ? 91 TYR A CZ 1 ATOM 678 O OH . TYR A 1 91 ? 28.881 13.606 -5.637 1.00 28.59 ? 91 TYR A OH 1 ATOM 679 N N . ALA A 1 92 ? 29.492 19.920 -2.499 1.00 22.45 ? 92 ALA A N 1 ATOM 680 C CA . ALA A 1 92 ? 29.776 20.872 -3.589 1.00 24.24 ? 92 ALA A CA 1 ATOM 681 C C . ALA A 1 92 ? 31.079 21.615 -3.387 1.00 24.33 ? 92 ALA A C 1 ATOM 682 O O . ALA A 1 92 ? 31.949 21.680 -4.299 1.00 25.67 ? 92 ALA A O 1 ATOM 683 C CB . ALA A 1 92 ? 28.642 21.849 -3.724 1.00 24.87 ? 92 ALA A CB 1 ATOM 684 N N . GLY A 1 93 ? 31.263 22.128 -2.179 1.00 23.78 ? 93 GLY A N 1 ATOM 685 C CA . GLY A 1 93 ? 32.477 22.854 -1.839 1.00 22.60 ? 93 GLY A CA 1 ATOM 686 C C . GLY A 1 93 ? 33.778 22.091 -1.825 1.00 23.33 ? 93 GLY A C 1 ATOM 687 O O . GLY A 1 93 ? 34.836 22.699 -1.823 1.00 21.99 ? 93 GLY A O 1 ATOM 688 N N . SER A 1 94 ? 33.718 20.767 -1.817 1.00 23.64 ? 94 SER A N 1 ATOM 689 C CA . SER A 1 94 ? 34.943 19.976 -1.856 1.00 24.93 ? 94 SER A CA 1 ATOM 690 C C . SER A 1 94 ? 35.120 19.362 -3.245 1.00 26.89 ? 94 SER A C 1 ATOM 691 O O . SER A 1 94 ? 35.861 18.410 -3.384 1.00 27.43 ? 94 SER A O 1 ATOM 692 C CB . SER A 1 94 ? 34.875 18.886 -0.765 1.00 24.71 ? 94 SER A CB 1 ATOM 693 O OG . SER A 1 94 ? 33.747 18.052 -0.905 1.00 24.49 ? 94 SER A OG 1 ATOM 694 N N . GLY A 1 95 ? 34.419 19.902 -4.255 1.00 27.78 ? 95 GLY A N 1 ATOM 695 C CA . GLY A 1 95 ? 34.521 19.408 -5.630 1.00 28.51 ? 95 GLY A CA 1 ATOM 696 C C . GLY A 1 95 ? 33.637 18.217 -5.952 1.00 27.87 ? 95 GLY A C 1 ATOM 697 O O . GLY A 1 95 ? 33.984 17.343 -6.715 1.00 27.20 ? 95 GLY A O 1 ATOM 698 N N . ASN A 1 96 ? 32.457 18.181 -5.393 1.00 27.43 ? 96 ASN A N 1 ATOM 699 C CA . ASN A 1 96 ? 31.605 17.000 -5.502 1.00 27.09 ? 96 ASN A CA 1 ATOM 700 C C . ASN A 1 96 ? 32.326 15.743 -5.058 1.00 26.60 ? 96 ASN A C 1 ATOM 701 O O . ASN A 1 96 ? 32.365 14.758 -5.745 1.00 28.41 ? 96 ASN A O 1 ATOM 702 C CB . ASN A 1 96 ? 31.026 16.869 -6.886 1.00 27.73 ? 96 ASN A CB 1 ATOM 703 C CG . ASN A 1 96 ? 30.102 18.005 -7.225 1.00 29.92 ? 96 ASN A CG 1 ATOM 704 O OD1 . ASN A 1 96 ? 29.614 18.749 -6.374 1.00 29.95 ? 96 ASN A OD1 1 ATOM 705 N ND2 . ASN A 1 96 ? 29.838 18.142 -8.479 1.00 31.88 ? 96 ASN A ND2 1 ATOM 706 N N . ASN A 1 97 ? 32.939 15.792 -3.890 1.00 25.75 ? 97 ASN A N 1 ATOM 707 C CA . ASN A 1 97 ? 33.506 14.613 -3.304 1.00 25.57 ? 97 ASN A CA 1 ATOM 708 C C . ASN A 1 97 ? 32.690 14.252 -2.024 1.00 25.30 ? 97 ASN A C 1 ATOM 709 O O . ASN A 1 97 ? 32.360 15.115 -1.199 1.00 23.19 ? 97 ASN A O 1 ATOM 710 C CB . ASN A 1 97 ? 34.976 14.875 -2.995 1.00 26.23 ? 97 ASN A CB 1 ATOM 711 C CG . ASN A 1 97 ? 35.797 14.927 -4.237 1.00 27.54 ? 97 ASN A CG 1 ATOM 712 O OD1 . ASN A 1 97 ? 35.995 13.925 -4.850 1.00 28.47 ? 97 ASN A OD1 1 ATOM 713 N ND2 . ASN A 1 97 ? 36.164 16.089 -4.662 1.00 26.84 ? 97 ASN A ND2 1 ATOM 714 N N . LYS A 1 98 ? 32.438 12.975 -1.835 1.00 25.44 ? 98 LYS A N 1 ATOM 715 C CA . LYS A 1 98 ? 31.808 12.495 -0.609 1.00 26.13 ? 98 LYS A CA 1 ATOM 716 C C . LYS A 1 98 ? 32.659 12.850 0.624 1.00 25.55 ? 98 LYS A C 1 ATOM 717 O O . LYS A 1 98 ? 33.862 12.976 0.520 1.00 25.62 ? 98 LYS A O 1 ATOM 718 C CB . LYS A 1 98 ? 31.616 10.970 -0.681 1.00 27.21 ? 98 LYS A CB 1 ATOM 719 C CG . LYS A 1 98 ? 30.672 10.465 -1.754 1.00 27.03 ? 98 LYS A CG 1 ATOM 720 C CD . LYS A 1 98 ? 30.581 8.946 -1.595 1.00 30.42 ? 98 LYS A CD 1 ATOM 721 C CE . LYS A 1 98 ? 29.561 8.344 -2.537 1.00 33.54 ? 98 LYS A CE 1 ATOM 722 N NZ . LYS A 1 98 ? 29.189 6.908 -2.219 1.00 34.95 ? 98 LYS A NZ 1 ATOM 723 N N . LEU A 1 99 ? 32.019 13.062 1.775 1.00 23.80 ? 99 LEU A N 1 ATOM 724 C CA . LEU A 1 99 ? 32.718 13.436 2.985 1.00 22.50 ? 99 LEU A CA 1 ATOM 725 C C . LEU A 1 99 ? 32.288 12.553 4.179 1.00 21.67 ? 99 LEU A C 1 ATOM 726 O O . LEU A 1 99 ? 31.183 12.062 4.185 1.00 19.56 ? 99 LEU A O 1 ATOM 727 C CB . LEU A 1 99 ? 32.522 14.904 3.304 1.00 21.78 ? 99 LEU A CB 1 ATOM 728 C CG . LEU A 1 99 ? 31.107 15.463 3.473 1.00 21.37 ? 99 LEU A CG 1 ATOM 729 C CD1 . LEU A 1 99 ? 31.086 16.409 4.688 1.00 21.69 ? 99 LEU A CD1 1 ATOM 730 C CD2 . LEU A 1 99 ? 30.655 16.180 2.183 1.00 21.66 ? 99 LEU A CD2 1 ATOM 731 N N . PRO A 1 100 ? 33.205 12.304 5.133 1.00 20.67 ? 100 PRO A N 1 ATOM 732 C CA . PRO A 1 100 ? 32.812 11.618 6.377 1.00 20.20 ? 100 PRO A CA 1 ATOM 733 C C . PRO A 1 100 ? 31.963 12.553 7.301 1.00 19.49 ? 100 PRO A C 1 ATOM 734 O O . PRO A 1 100 ? 32.128 13.779 7.296 1.00 18.26 ? 100 PRO A O 1 ATOM 735 C CB . PRO A 1 100 ? 34.136 11.240 7.014 1.00 21.06 ? 100 PRO A CB 1 ATOM 736 C CG . PRO A 1 100 ? 35.104 12.246 6.513 1.00 21.02 ? 100 PRO A CG 1 ATOM 737 C CD . PRO A 1 100 ? 34.577 12.785 5.194 1.00 21.37 ? 100 PRO A CD 1 ATOM 738 N N . VAL A 1 101 ? 31.089 11.919 8.099 1.00 19.58 ? 101 VAL A N 1 ATOM 739 C CA . VAL A 1 101 ? 30.388 12.572 9.206 1.00 18.18 ? 101 VAL A CA 1 ATOM 740 C C . VAL A 1 101 ? 30.744 11.901 10.514 1.00 18.77 ? 101 VAL A C 1 ATOM 741 O O . VAL A 1 101 ? 30.775 10.667 10.564 1.00 18.33 ? 101 VAL A O 1 ATOM 742 C CB . VAL A 1 101 ? 28.872 12.486 9.007 1.00 17.75 ? 101 VAL A CB 1 ATOM 743 C CG1 . VAL A 1 101 ? 28.095 13.149 10.145 1.00 17.24 ? 101 VAL A CG1 1 ATOM 744 C CG2 . VAL A 1 101 ? 28.509 13.085 7.692 1.00 18.20 ? 101 VAL A CG2 1 ATOM 745 N N . LEU A 1 102 ? 31.109 12.709 11.550 1.00 18.17 ? 102 LEU A N 1 ATOM 746 C CA . LEU A 1 102 ? 31.459 12.180 12.862 1.00 18.72 ? 102 LEU A CA 1 ATOM 747 C C . LEU A 1 102 ? 30.587 12.880 13.937 1.00 18.40 ? 102 LEU A C 1 ATOM 748 O O . LEU A 1 102 ? 30.386 14.088 13.876 1.00 16.88 ? 102 LEU A O 1 ATOM 749 C CB . LEU A 1 102 ? 32.951 12.373 13.138 1.00 18.86 ? 102 LEU A CB 1 ATOM 750 C CG . LEU A 1 102 ? 33.619 11.806 14.391 1.00 19.62 ? 102 LEU A CG 1 ATOM 751 C CD1 . LEU A 1 102 ? 35.105 11.550 14.153 1.00 19.97 ? 102 LEU A CD1 1 ATOM 752 C CD2 . LEU A 1 102 ? 33.467 12.740 15.632 1.00 19.46 ? 102 LEU A CD2 1 ATOM 753 N N . THR A 1 103 ? 30.063 12.100 14.876 1.00 17.98 ? 103 THR A N 1 ATOM 754 C CA . THR A 1 103 ? 28.986 12.620 15.730 1.00 17.74 ? 103 THR A CA 1 ATOM 755 C C . THR A 1 103 ? 29.086 12.200 17.177 1.00 17.41 ? 103 THR A C 1 ATOM 756 O O . THR A 1 103 ? 29.735 11.243 17.498 1.00 15.87 ? 103 THR A O 1 ATOM 757 C CB . THR A 1 103 ? 27.580 12.234 15.212 1.00 17.71 ? 103 THR A CB 1 ATOM 758 O OG1 . THR A 1 103 ? 27.354 10.844 15.373 1.00 17.24 ? 103 THR A OG1 1 ATOM 759 C CG2 . THR A 1 103 ? 27.428 12.571 13.761 1.00 18.56 ? 103 THR A CG2 1 ATOM 760 N N . TRP A 1 104 ? 28.414 12.987 18.047 1.00 17.02 ? 104 TRP A N 1 ATOM 761 C CA . TRP A 1 104 ? 28.259 12.589 19.391 1.00 16.87 ? 104 TRP A CA 1 ATOM 762 C C . TRP A 1 104 ? 26.801 12.658 19.822 1.00 15.81 ? 104 TRP A C 1 ATOM 763 O O . TRP A 1 104 ? 26.136 13.689 19.598 1.00 15.95 ? 104 TRP A O 1 ATOM 764 C CB . TRP A 1 104 ? 29.123 13.506 20.289 1.00 16.82 ? 104 TRP A CB 1 ATOM 765 C CG . TRP A 1 104 ? 29.104 13.113 21.810 1.00 17.23 ? 104 TRP A CG 1 ATOM 766 C CD1 . TRP A 1 104 ? 29.235 11.841 22.353 1.00 17.53 ? 104 TRP A CD1 1 ATOM 767 C CD2 . TRP A 1 104 ? 29.023 14.003 22.935 1.00 17.35 ? 104 TRP A CD2 1 ATOM 768 N NE1 . TRP A 1 104 ? 29.260 11.906 23.720 1.00 17.12 ? 104 TRP A NE1 1 ATOM 769 C CE2 . TRP A 1 104 ? 29.073 13.209 24.104 1.00 17.42 ? 104 TRP A CE2 1 ATOM 770 C CE3 . TRP A 1 104 ? 28.890 15.398 23.059 1.00 18.78 ? 104 TRP A CE3 1 ATOM 771 C CZ2 . TRP A 1 104 ? 29.033 13.763 25.407 1.00 18.83 ? 104 TRP A CZ2 1 ATOM 772 C CZ3 . TRP A 1 104 ? 28.815 15.961 24.344 1.00 19.43 ? 104 TRP A CZ3 1 ATOM 773 C CH2 . TRP A 1 104 ? 28.856 15.148 25.507 1.00 19.35 ? 104 TRP A CH2 1 ATOM 774 N N . SER A 1 105 ? 26.391 11.632 20.552 1.00 15.96 ? 105 SER A N 1 ATOM 775 C CA . SER A 1 105 ? 25.109 11.517 21.198 1.00 16.15 ? 105 SER A CA 1 ATOM 776 C C . SER A 1 105 ? 24.015 11.836 20.129 1.00 15.63 ? 105 SER A C 1 ATOM 777 O O . SER A 1 105 ? 23.993 11.163 19.106 1.00 17.05 ? 105 SER A O 1 ATOM 778 C CB . SER A 1 105 ? 25.100 12.470 22.418 1.00 17.23 ? 105 SER A CB 1 ATOM 779 O OG . SER A 1 105 ? 24.046 12.168 23.305 1.00 18.08 ? 105 SER A OG 1 ATOM 780 N N . GLN A 1 106 ? 23.178 12.832 20.364 1.00 15.03 ? 106 GLN A N 1 ATOM 781 C CA . GLN A 1 106 ? 22.144 13.302 19.427 1.00 15.02 ? 106 GLN A CA 1 ATOM 782 C C . GLN A 1 106 ? 22.596 13.486 18.018 1.00 14.55 ? 106 GLN A C 1 ATOM 783 O O . GLN A 1 106 ? 21.799 13.304 17.079 1.00 14.66 ? 106 GLN A O 1 ATOM 784 C CB . GLN A 1 106 ? 21.423 14.540 19.887 1.00 15.13 ? 106 GLN A CB 1 ATOM 785 C CG . GLN A 1 106 ? 20.145 14.829 19.072 1.00 15.32 ? 106 GLN A CG 1 ATOM 786 C CD . GLN A 1 106 ? 19.562 16.258 19.194 1.00 16.25 ? 106 GLN A CD 1 ATOM 787 O OE1 . GLN A 1 106 ? 18.773 16.673 18.373 1.00 15.96 ? 106 GLN A OE1 1 ATOM 788 N NE2 . GLN A 1 106 ? 19.911 16.970 20.251 1.00 16.65 ? 106 GLN A NE2 1 ATOM 789 N N . GLY A 1 107 ? 23.837 13.889 17.852 1.00 14.85 ? 107 GLY A N 1 ATOM 790 C CA . GLY A 1 107 ? 24.379 14.136 16.532 1.00 15.61 ? 107 GLY A CA 1 ATOM 791 C C . GLY A 1 107 ? 24.264 12.927 15.610 1.00 15.31 ? 107 GLY A C 1 ATOM 792 O O . GLY A 1 107 ? 24.063 13.099 14.445 1.00 16.08 ? 107 GLY A O 1 ATOM 793 N N . GLY A 1 108 ? 24.406 11.740 16.138 1.00 15.07 ? 108 GLY A N 1 ATOM 794 C CA . GLY A 1 108 ? 24.300 10.469 15.365 1.00 15.32 ? 108 GLY A CA 1 ATOM 795 C C . GLY A 1 108 ? 22.831 10.167 14.977 1.00 15.36 ? 108 GLY A C 1 ATOM 796 O O . GLY A 1 108 ? 22.588 9.811 13.860 1.00 16.82 ? 108 GLY A O 1 ATOM 797 N N . LEU A 1 109 ? 21.882 10.413 15.895 1.00 14.96 ? 109 LEU A N 1 ATOM 798 C CA . LEU A 1 109 ? 20.455 10.325 15.644 1.00 14.58 ? 109 LEU A CA 1 ATOM 799 C C . LEU A 1 109 ? 20.127 11.325 14.567 1.00 14.54 ? 109 LEU A C 1 ATOM 800 O O . LEU A 1 109 ? 19.388 11.021 13.659 1.00 14.59 ? 109 LEU A O 1 ATOM 801 C CB . LEU A 1 109 ? 19.651 10.710 16.897 1.00 14.56 ? 109 LEU A CB 1 ATOM 802 C CG . LEU A 1 109 ? 18.118 10.825 16.784 1.00 14.55 ? 109 LEU A CG 1 ATOM 803 C CD1 . LEU A 1 109 ? 17.533 9.494 16.303 1.00 15.04 ? 109 LEU A CD1 1 ATOM 804 C CD2 . LEU A 1 109 ? 17.511 11.203 18.108 1.00 14.89 ? 109 LEU A CD2 1 ATOM 805 N N . VAL A 1 110 ? 20.692 12.525 14.658 1.00 15.01 ? 110 VAL A N 1 ATOM 806 C CA . VAL A 1 110 ? 20.542 13.526 13.576 1.00 15.44 ? 110 VAL A CA 1 ATOM 807 C C . VAL A 1 110 ? 21.059 13.007 12.224 1.00 15.80 ? 110 VAL A C 1 ATOM 808 O O . VAL A 1 110 ? 20.391 13.107 11.230 1.00 15.01 ? 110 VAL A O 1 ATOM 809 C CB . VAL A 1 110 ? 21.123 14.914 14.008 1.00 15.08 ? 110 VAL A CB 1 ATOM 810 C CG1 . VAL A 1 110 ? 21.369 15.835 12.845 1.00 15.36 ? 110 VAL A CG1 1 ATOM 811 C CG2 . VAL A 1 110 ? 20.161 15.598 15.017 1.00 15.01 ? 110 VAL A CG2 1 ATOM 812 N N . ALA A 1 111 ? 22.281 12.526 12.173 1.00 16.01 ? 111 ALA A N 1 ATOM 813 C CA . ALA A 1 111 ? 22.792 12.038 10.925 1.00 17.08 ? 111 ALA A CA 1 ATOM 814 C C . ALA A 1 111 ? 21.944 10.932 10.311 1.00 17.69 ? 111 ALA A C 1 ATOM 815 O O . ALA A 1 111 ? 21.649 10.938 9.122 1.00 18.61 ? 111 ALA A O 1 ATOM 816 C CB . ALA A 1 111 ? 24.208 11.561 11.107 1.00 17.46 ? 111 ALA A CB 1 ATOM 817 N N . GLN A 1 112 ? 21.547 9.996 11.143 1.00 18.10 ? 112 GLN A N 1 ATOM 818 C CA . GLN A 1 112 ? 20.741 8.902 10.698 1.00 18.09 ? 112 GLN A CA 1 ATOM 819 C C . GLN A 1 112 ? 19.306 9.339 10.275 1.00 17.99 ? 112 GLN A C 1 ATOM 820 O O . GLN A 1 112 ? 18.761 8.784 9.301 1.00 17.22 ? 112 GLN A O 1 ATOM 821 C CB . GLN A 1 112 ? 20.774 7.832 11.770 1.00 18.53 ? 112 GLN A CB 1 ATOM 822 C CG . GLN A 1 112 ? 20.401 6.449 11.320 1.00 19.94 ? 112 GLN A CG 1 ATOM 823 C CD . GLN A 1 112 ? 21.141 5.770 10.174 1.00 19.83 ? 112 GLN A CD 1 ATOM 824 O OE1 . GLN A 1 112 ? 22.108 6.250 9.605 1.00 21.00 ? 112 GLN A OE1 1 ATOM 825 N NE2 . GLN A 1 112 ? 20.643 4.558 9.838 1.00 20.17 ? 112 GLN A NE2 1 ATOM 826 N N . TRP A 1 113 ? 18.706 10.332 10.950 1.00 17.13 ? 113 TRP A N 1 ATOM 827 C CA . TRP A 1 113 ? 17.419 10.911 10.500 1.00 17.00 ? 113 TRP A CA 1 ATOM 828 C C . TRP A 1 113 ? 17.550 11.580 9.116 1.00 16.96 ? 113 TRP A C 1 ATOM 829 O O . TRP A 1 113 ? 16.708 11.422 8.194 1.00 16.98 ? 113 TRP A O 1 ATOM 830 C CB . TRP A 1 113 ? 16.952 11.989 11.525 1.00 17.08 ? 113 TRP A CB 1 ATOM 831 C CG . TRP A 1 113 ? 15.585 12.537 11.286 1.00 16.22 ? 113 TRP A CG 1 ATOM 832 C CD1 . TRP A 1 113 ? 15.246 13.649 10.545 1.00 16.15 ? 113 TRP A CD1 1 ATOM 833 C CD2 . TRP A 1 113 ? 14.372 11.996 11.775 1.00 15.97 ? 113 TRP A CD2 1 ATOM 834 N NE1 . TRP A 1 113 ? 13.836 13.835 10.559 1.00 15.46 ? 113 TRP A NE1 1 ATOM 835 C CE2 . TRP A 1 113 ? 13.294 12.803 11.278 1.00 15.57 ? 113 TRP A CE2 1 ATOM 836 C CE3 . TRP A 1 113 ? 14.058 10.867 12.523 1.00 15.36 ? 113 TRP A CE3 1 ATOM 837 C CZ2 . TRP A 1 113 ? 11.954 12.531 11.586 1.00 14.90 ? 113 TRP A CZ2 1 ATOM 838 C CZ3 . TRP A 1 113 ? 12.679 10.607 12.796 1.00 15.04 ? 113 TRP A CZ3 1 ATOM 839 C CH2 . TRP A 1 113 ? 11.676 11.434 12.319 1.00 15.10 ? 113 TRP A CH2 1 ATOM 840 N N . GLY A 1 114 ? 18.639 12.321 8.966 1.00 16.62 ? 114 GLY A N 1 ATOM 841 C CA . GLY A 1 114 ? 19.006 12.892 7.681 1.00 16.61 ? 114 GLY A CA 1 ATOM 842 C C . GLY A 1 114 ? 19.083 11.875 6.547 1.00 17.32 ? 114 GLY A C 1 ATOM 843 O O . GLY A 1 114 ? 18.427 12.027 5.500 1.00 17.81 ? 114 GLY A O 1 ATOM 844 N N . LEU A 1 115 ? 19.870 10.824 6.763 1.00 17.22 ? 115 LEU A N 1 ATOM 845 C CA . LEU A 1 115 ? 20.106 9.793 5.716 1.00 17.17 ? 115 LEU A CA 1 ATOM 846 C C . LEU A 1 115 ? 18.807 9.068 5.403 1.00 16.66 ? 115 LEU A C 1 ATOM 847 O O . LEU A 1 115 ? 18.619 8.565 4.322 1.00 17.62 ? 115 LEU A O 1 ATOM 848 C CB . LEU A 1 115 ? 21.172 8.821 6.233 1.00 16.75 ? 115 LEU A CB 1 ATOM 849 C CG . LEU A 1 115 ? 22.590 9.378 6.218 1.00 17.03 ? 115 LEU A CG 1 ATOM 850 C CD1 . LEU A 1 115 ? 23.543 8.526 7.068 1.00 17.11 ? 115 LEU A CD1 1 ATOM 851 C CD2 . LEU A 1 115 ? 23.108 9.506 4.793 1.00 18.04 ? 115 LEU A CD2 1 ATOM 852 N N . THR A 1 116 ? 17.933 8.974 6.393 1.00 16.36 ? 116 THR A N 1 ATOM 853 C CA . THR A 1 116 ? 16.707 8.206 6.300 1.00 16.38 ? 116 THR A CA 1 ATOM 854 C C . THR A 1 116 ? 15.678 9.035 5.486 1.00 16.56 ? 116 THR A C 1 ATOM 855 O O . THR A 1 116 ? 15.047 8.519 4.478 1.00 16.70 ? 116 THR A O 1 ATOM 856 C CB . THR A 1 116 ? 16.190 7.770 7.696 1.00 15.98 ? 116 THR A CB 1 ATOM 857 O OG1 . THR A 1 116 ? 17.118 6.874 8.322 1.00 15.98 ? 116 THR A OG1 1 ATOM 858 C CG2 . THR A 1 116 ? 14.815 7.131 7.565 1.00 15.80 ? 116 THR A CG2 1 ATOM 859 N N . PHE A 1 117 ? 15.526 10.309 5.815 1.00 16.42 ? 117 PHE A N 1 ATOM 860 C CA . PHE A 1 117 ? 14.398 11.056 5.238 1.00 16.24 ? 117 PHE A CA 1 ATOM 861 C C . PHE A 1 117 ? 14.772 12.053 4.153 1.00 17.04 ? 117 PHE A C 1 ATOM 862 O O . PHE A 1 117 ? 13.857 12.590 3.493 1.00 17.19 ? 117 PHE A O 1 ATOM 863 C CB . PHE A 1 117 ? 13.598 11.713 6.366 1.00 16.85 ? 117 PHE A CB 1 ATOM 864 C CG . PHE A 1 117 ? 12.867 10.744 7.269 1.00 17.03 ? 117 PHE A CG 1 ATOM 865 C CD1 . PHE A 1 117 ? 11.712 10.095 6.842 1.00 18.13 ? 117 PHE A CD1 1 ATOM 866 C CD2 . PHE A 1 117 ? 13.296 10.518 8.566 1.00 17.37 ? 117 PHE A CD2 1 ATOM 867 C CE1 . PHE A 1 117 ? 11.003 9.238 7.685 1.00 17.53 ? 117 PHE A CE1 1 ATOM 868 C CE2 . PHE A 1 117 ? 12.631 9.617 9.383 1.00 17.17 ? 117 PHE A CE2 1 ATOM 869 C CZ . PHE A 1 117 ? 11.487 8.984 8.947 1.00 17.18 ? 117 PHE A CZ 1 ATOM 870 N N . PHE A 1 118 ? 16.079 12.257 3.895 1.00 16.90 ? 118 PHE A N 1 ATOM 871 C CA . PHE A 1 118 ? 16.592 13.156 2.835 1.00 17.48 ? 118 PHE A CA 1 ATOM 872 C C . PHE A 1 118 ? 17.521 12.363 1.902 1.00 17.42 ? 118 PHE A C 1 ATOM 873 O O . PHE A 1 118 ? 18.784 12.410 2.064 1.00 19.20 ? 118 PHE A O 1 ATOM 874 C CB . PHE A 1 118 ? 17.327 14.389 3.434 1.00 17.52 ? 118 PHE A CB 1 ATOM 875 C CG . PHE A 1 118 ? 16.448 15.217 4.308 1.00 17.42 ? 118 PHE A CG 1 ATOM 876 C CD1 . PHE A 1 118 ? 16.083 14.769 5.615 1.00 17.16 ? 118 PHE A CD1 1 ATOM 877 C CD2 . PHE A 1 118 ? 15.917 16.410 3.853 1.00 17.29 ? 118 PHE A CD2 1 ATOM 878 C CE1 . PHE A 1 118 ? 15.267 15.541 6.414 1.00 16.71 ? 118 PHE A CE1 1 ATOM 879 C CE2 . PHE A 1 118 ? 15.104 17.187 4.690 1.00 16.98 ? 118 PHE A CE2 1 ATOM 880 C CZ . PHE A 1 118 ? 14.758 16.725 5.947 1.00 16.98 ? 118 PHE A CZ 1 ATOM 881 N N . PRO A 1 119 ? 16.939 11.569 0.968 1.00 17.26 ? 119 PRO A N 1 ATOM 882 C CA . PRO A 1 119 ? 17.757 10.690 0.173 1.00 17.25 ? 119 PRO A CA 1 ATOM 883 C C . PRO A 1 119 ? 18.914 11.288 -0.607 1.00 18.32 ? 119 PRO A C 1 ATOM 884 O O . PRO A 1 119 ? 19.873 10.566 -0.857 1.00 17.88 ? 119 PRO A O 1 ATOM 885 C CB . PRO A 1 119 ? 16.749 10.053 -0.807 1.00 17.93 ? 119 PRO A CB 1 ATOM 886 C CG . PRO A 1 119 ? 15.445 10.117 -0.133 1.00 17.88 ? 119 PRO A CG 1 ATOM 887 C CD . PRO A 1 119 ? 15.491 11.394 0.646 1.00 17.74 ? 119 PRO A CD 1 ATOM 888 N N . SER A 1 120 ? 18.819 12.590 -0.981 1.00 18.44 ? 120 SER A N 1 ATOM 889 C CA . SER A 1 120 ? 19.829 13.230 -1.798 1.00 19.28 ? 120 SER A CA 1 ATOM 890 C C . SER A 1 120 ? 21.193 13.124 -1.152 1.00 19.17 ? 120 SER A C 1 ATOM 891 O O . SER A 1 120 ? 22.224 13.180 -1.860 1.00 20.53 ? 120 SER A O 1 ATOM 892 C CB . SER A 1 120 ? 19.477 14.686 -2.051 1.00 20.24 ? 120 SER A CB 1 ATOM 893 O OG . SER A 1 120 ? 19.714 15.438 -0.908 1.00 19.22 ? 120 SER A OG 1 ATOM 894 N N . ILE A 1 121 ? 21.231 12.996 0.164 1.00 18.79 ? 121 ILE A N 1 ATOM 895 C CA . ILE A 1 121 ? 22.529 12.926 0.886 1.00 19.50 ? 121 ILE A CA 1 ATOM 896 C C . ILE A 1 121 ? 23.215 11.558 1.024 1.00 19.53 ? 121 ILE A C 1 ATOM 897 O O . ILE A 1 121 ? 24.397 11.521 1.318 1.00 19.89 ? 121 ILE A O 1 ATOM 898 C CB . ILE A 1 121 ? 22.568 13.677 2.271 1.00 18.97 ? 121 ILE A CB 1 ATOM 899 C CG1 . ILE A 1 121 ? 21.623 13.006 3.319 1.00 18.95 ? 121 ILE A CG1 1 ATOM 900 C CG2 . ILE A 1 121 ? 22.423 15.183 2.010 1.00 19.44 ? 121 ILE A CG2 1 ATOM 901 C CD1 . ILE A 1 121 ? 22.002 13.329 4.762 1.00 19.01 ? 121 ILE A CD1 1 ATOM 902 N N . ARG A 1 122 ? 22.536 10.472 0.709 1.00 20.85 ? 122 ARG A N 1 ATOM 903 C CA . ARG A 1 122 ? 23.081 9.156 0.857 1.00 21.36 ? 122 ARG A CA 1 ATOM 904 C C . ARG A 1 122 ? 24.286 8.926 -0.029 1.00 24.26 ? 122 ARG A C 1 ATOM 905 O O . ARG A 1 122 ? 25.151 8.081 0.313 1.00 24.45 ? 122 ARG A O 1 ATOM 906 C CB . ARG A 1 122 ? 22.015 8.080 0.497 1.00 22.23 ? 122 ARG A CB 1 ATOM 907 C CG . ARG A 1 122 ? 20.838 8.102 1.442 1.00 21.62 ? 122 ARG A CG 1 ATOM 908 C CD . ARG A 1 122 ? 19.739 7.235 0.944 1.00 21.87 ? 122 ARG A CD 1 ATOM 909 N NE . ARG A 1 122 ? 18.570 7.380 1.830 1.00 21.20 ? 122 ARG A NE 1 ATOM 910 C CZ . ARG A 1 122 ? 17.351 6.978 1.540 1.00 21.87 ? 122 ARG A CZ 1 ATOM 911 N NH1 . ARG A 1 122 ? 17.095 6.393 0.358 1.00 23.34 ? 122 ARG A NH1 1 ATOM 912 N NH2 . ARG A 1 122 ? 16.347 7.195 2.371 1.00 21.86 ? 122 ARG A NH2 1 ATOM 913 N N . SER A 1 123 ? 24.306 9.622 -1.194 1.00 24.83 ? 123 SER A N 1 ATOM 914 C CA . SER A 1 123 ? 25.382 9.579 -2.147 1.00 25.51 ? 123 SER A CA 1 ATOM 915 C C . SER A 1 123 ? 26.452 10.644 -1.902 1.00 26.10 ? 123 SER A C 1 ATOM 916 O O . SER A 1 123 ? 27.387 10.736 -2.677 1.00 26.74 ? 123 SER A O 1 ATOM 917 C CB . SER A 1 123 ? 24.808 9.746 -3.554 1.00 28.14 ? 123 SER A CB 1 ATOM 918 O OG . SER A 1 123 ? 24.181 11.013 -3.683 1.00 28.40 ? 123 SER A OG 1 ATOM 919 N N . LYS A 1 124 ? 26.341 11.439 -0.839 1.00 22.81 ? 124 LYS A N 1 ATOM 920 C CA . LYS A 1 124 ? 27.278 12.533 -0.559 1.00 22.31 ? 124 LYS A CA 1 ATOM 921 C C . LYS A 1 124 ? 28.052 12.324 0.729 1.00 22.35 ? 124 LYS A C 1 ATOM 922 O O . LYS A 1 124 ? 29.056 13.009 0.948 1.00 21.13 ? 124 LYS A O 1 ATOM 923 C CB . LYS A 1 124 ? 26.484 13.863 -0.469 1.00 22.20 ? 124 LYS A CB 1 ATOM 924 C CG . LYS A 1 124 ? 25.612 14.049 -1.677 1.00 21.43 ? 124 LYS A CG 1 ATOM 925 C CD . LYS A 1 124 ? 25.203 15.448 -1.914 1.00 21.55 ? 124 LYS A CD 1 ATOM 926 C CE . LYS A 1 124 ? 24.458 15.501 -3.219 1.00 21.28 ? 124 LYS A CE 1 ATOM 927 N NZ . LYS A 1 124 ? 23.863 16.848 -3.280 1.00 21.24 ? 124 LYS A NZ 1 ATOM 928 N N . VAL A 1 125 ? 27.591 11.354 1.561 1.00 22.50 ? 125 VAL A N 1 ATOM 929 C CA . VAL A 1 125 ? 28.231 10.950 2.781 1.00 22.23 ? 125 VAL A CA 1 ATOM 930 C C . VAL A 1 125 ? 28.969 9.640 2.520 1.00 23.59 ? 125 VAL A C 1 ATOM 931 O O . VAL A 1 125 ? 28.369 8.622 2.160 1.00 23.15 ? 125 VAL A O 1 ATOM 932 C CB . VAL A 1 125 ? 27.234 10.695 3.941 1.00 22.25 ? 125 VAL A CB 1 ATOM 933 C CG1 . VAL A 1 125 ? 27.987 10.215 5.207 1.00 21.94 ? 125 VAL A CG1 1 ATOM 934 C CG2 . VAL A 1 125 ? 26.435 11.931 4.259 1.00 21.51 ? 125 VAL A CG2 1 ATOM 935 N N . ASP A 1 126 ? 30.268 9.723 2.780 1.00 24.32 ? 126 ASP A N 1 ATOM 936 C CA . ASP A 1 126 ? 31.259 8.654 2.662 1.00 26.22 ? 126 ASP A CA 1 ATOM 937 C C . ASP A 1 126 ? 31.051 7.530 3.705 1.00 25.16 ? 126 ASP A C 1 ATOM 938 O O . ASP A 1 126 ? 31.135 6.331 3.433 1.00 24.70 ? 126 ASP A O 1 ATOM 939 C CB . ASP A 1 126 ? 32.634 9.304 2.986 1.00 28.39 ? 126 ASP A CB 1 ATOM 940 C CG . ASP A 1 126 ? 33.714 8.631 2.331 1.00 31.72 ? 126 ASP A CG 1 ATOM 941 O OD1 . ASP A 1 126 ? 33.424 8.029 1.303 1.00 34.91 ? 126 ASP A OD1 1 ATOM 942 O OD2 . ASP A 1 126 ? 34.862 8.723 2.796 1.00 34.89 ? 126 ASP A OD2 1 ATOM 943 N N . ARG A 1 127 ? 30.848 7.966 4.942 1.00 22.84 ? 127 ARG A N 1 ATOM 944 C CA . ARG A 1 127 ? 30.847 7.085 6.114 1.00 22.17 ? 127 ARG A CA 1 ATOM 945 C C . ARG A 1 127 ? 30.377 7.908 7.309 1.00 20.39 ? 127 ARG A C 1 ATOM 946 O O . ARG A 1 127 ? 30.406 9.134 7.259 1.00 18.91 ? 127 ARG A O 1 ATOM 947 C CB . ARG A 1 127 ? 32.282 6.589 6.403 1.00 23.70 ? 127 ARG A CB 1 ATOM 948 C CG . ARG A 1 127 ? 33.241 7.658 6.843 1.00 23.94 ? 127 ARG A CG 1 ATOM 949 C CD . ARG A 1 127 ? 34.671 7.204 6.833 1.00 24.37 ? 127 ARG A CD 1 ATOM 950 N NE . ARG A 1 127 ? 35.110 7.107 5.459 1.00 26.08 ? 127 ARG A NE 1 ATOM 951 C CZ . ARG A 1 127 ? 36.045 6.298 4.974 1.00 26.73 ? 127 ARG A CZ 1 ATOM 952 N NH1 . ARG A 1 127 ? 36.696 5.380 5.717 1.00 26.80 ? 127 ARG A NH1 1 ATOM 953 N NH2 . ARG A 1 127 ? 36.287 6.383 3.691 1.00 26.91 ? 127 ARG A NH2 1 ATOM 954 N N . LEU A 1 128 ? 29.941 7.212 8.349 1.00 19.51 ? 128 LEU A N 1 ATOM 955 C CA . LEU A 1 128 ? 29.423 7.831 9.597 1.00 18.88 ? 128 LEU A CA 1 ATOM 956 C C . LEU A 1 128 ? 30.233 7.190 10.718 1.00 18.43 ? 128 LEU A C 1 ATOM 957 O O . LEU A 1 128 ? 30.407 5.920 10.742 1.00 19.20 ? 128 LEU A O 1 ATOM 958 C CB . LEU A 1 128 ? 27.895 7.554 9.721 1.00 18.22 ? 128 LEU A CB 1 ATOM 959 C CG . LEU A 1 128 ? 27.225 8.024 11.039 1.00 18.69 ? 128 LEU A CG 1 ATOM 960 C CD1 . LEU A 1 128 ? 27.439 9.454 11.351 1.00 17.64 ? 128 LEU A CD1 1 ATOM 961 C CD2 . LEU A 1 128 ? 25.735 7.657 11.073 1.00 19.22 ? 128 LEU A CD2 1 ATOM 962 N N . MET A 1 129 ? 30.823 8.046 11.569 1.00 18.14 ? 129 MET A N 1 ATOM 963 C CA . MET A 1 129 ? 31.578 7.614 12.754 1.00 18.65 ? 129 MET A CA 1 ATOM 964 C C . MET A 1 129 ? 30.823 8.270 13.917 1.00 19.00 ? 129 MET A C 1 ATOM 965 O O . MET A 1 129 ? 30.980 9.512 14.175 1.00 17.19 ? 129 MET A O 1 ATOM 966 C CB . MET A 1 129 ? 33.031 8.094 12.671 1.00 19.92 ? 129 MET A CB 1 ATOM 967 C CG . MET A 1 129 ? 33.915 7.722 13.884 1.00 19.68 ? 129 MET A CG 1 ATOM 968 S SD . MET A 1 129 ? 33.925 5.953 14.315 1.00 20.32 ? 129 MET A SD 1 ATOM 969 C CE . MET A 1 129 ? 32.769 5.906 15.687 1.00 19.38 ? 129 MET A CE 1 ATOM 970 N N . ALA A 1 130 ? 29.978 7.446 14.570 1.00 17.70 ? 130 ALA A N 1 ATOM 971 C CA . ALA A 1 130 ? 29.101 7.869 15.659 1.00 18.54 ? 130 ALA A CA 1 ATOM 972 C C . ALA A 1 130 ? 29.599 7.366 17.036 1.00 18.25 ? 130 ALA A C 1 ATOM 973 O O . ALA A 1 130 ? 29.784 6.180 17.262 1.00 17.31 ? 130 ALA A O 1 ATOM 974 C CB . ALA A 1 130 ? 27.644 7.400 15.418 1.00 18.62 ? 130 ALA A CB 1 ATOM 975 N N . PHE A 1 131 ? 29.725 8.318 17.951 1.00 17.30 ? 131 PHE A N 1 ATOM 976 C CA . PHE A 1 131 ? 30.100 8.088 19.316 1.00 17.27 ? 131 PHE A CA 1 ATOM 977 C C . PHE A 1 131 ? 28.877 8.230 20.216 1.00 16.95 ? 131 PHE A C 1 ATOM 978 O O . PHE A 1 131 ? 28.218 9.290 20.223 1.00 17.09 ? 131 PHE A O 1 ATOM 979 C CB . PHE A 1 131 ? 31.243 9.016 19.736 1.00 17.42 ? 131 PHE A CB 1 ATOM 980 C CG . PHE A 1 131 ? 32.540 8.809 18.941 1.00 17.78 ? 131 PHE A CG 1 ATOM 981 C CD1 . PHE A 1 131 ? 33.431 7.832 19.281 1.00 17.89 ? 131 PHE A CD1 1 ATOM 982 C CD2 . PHE A 1 131 ? 32.886 9.651 17.893 1.00 18.00 ? 131 PHE A CD2 1 ATOM 983 C CE1 . PHE A 1 131 ? 34.609 7.633 18.542 1.00 18.54 ? 131 PHE A CE1 1 ATOM 984 C CE2 . PHE A 1 131 ? 34.051 9.478 17.188 1.00 17.49 ? 131 PHE A CE2 1 ATOM 985 C CZ . PHE A 1 131 ? 34.914 8.473 17.504 1.00 16.90 ? 131 PHE A CZ 1 ATOM 986 N N . ALA A 1 132 ? 28.553 7.146 20.974 1.00 16.77 ? 132 ALA A N 1 ATOM 987 C CA . ALA A 1 132 ? 27.385 7.116 21.857 1.00 16.12 ? 132 ALA A CA 1 ATOM 988 C C . ALA A 1 132 ? 26.097 7.606 21.194 1.00 16.21 ? 132 ALA A C 1 ATOM 989 O O . ALA A 1 132 ? 25.303 8.345 21.813 1.00 15.98 ? 132 ALA A O 1 ATOM 990 C CB . ALA A 1 132 ? 27.635 7.836 23.198 1.00 16.11 ? 132 ALA A CB 1 ATOM 991 N N . PRO A 1 133 ? 25.848 7.133 19.957 1.00 16.12 ? 133 PRO A N 1 ATOM 992 C CA . PRO A 1 133 ? 24.640 7.571 19.264 1.00 15.64 ? 133 PRO A CA 1 ATOM 993 C C . PRO A 1 133 ? 23.404 6.980 19.914 1.00 15.70 ? 133 PRO A C 1 ATOM 994 O O . PRO A 1 133 ? 23.420 5.824 20.375 1.00 16.54 ? 133 PRO A O 1 ATOM 995 C CB . PRO A 1 133 ? 24.854 7.026 17.843 1.00 15.67 ? 133 PRO A CB 1 ATOM 996 C CG . PRO A 1 133 ? 25.626 5.750 18.067 1.00 15.93 ? 133 PRO A CG 1 ATOM 997 C CD . PRO A 1 133 ? 26.606 6.173 19.135 1.00 16.19 ? 133 PRO A CD 1 ATOM 998 N N . ASP A 1 134 ? 22.326 7.752 19.942 1.00 15.41 ? 134 ASP A N 1 ATOM 999 C CA . ASP A 1 134 ? 21.092 7.338 20.606 1.00 15.44 ? 134 ASP A CA 1 ATOM 1000 C C . ASP A 1 134 ? 19.950 7.161 19.574 1.00 15.61 ? 134 ASP A C 1 ATOM 1001 O O . ASP A 1 134 ? 18.905 7.843 19.648 1.00 15.01 ? 134 ASP A O 1 ATOM 1002 C CB . ASP A 1 134 ? 20.677 8.271 21.766 1.00 15.22 ? 134 ASP A CB 1 ATOM 1003 C CG . ASP A 1 134 ? 20.434 9.744 21.356 1.00 15.56 ? 134 ASP A CG 1 ATOM 1004 O OD1 . ASP A 1 134 ? 21.088 10.272 20.391 1.00 15.78 ? 134 ASP A OD1 1 ATOM 1005 O OD2 . ASP A 1 134 ? 19.664 10.410 22.145 1.00 15.95 ? 134 ASP A OD2 1 ATOM 1006 N N . TYR A 1 135 ? 20.138 6.173 18.671 1.00 15.26 ? 135 TYR A N 1 ATOM 1007 C CA . TYR A 1 135 ? 19.189 5.921 17.623 1.00 15.60 ? 135 TYR A CA 1 ATOM 1008 C C . TYR A 1 135 ? 17.817 5.444 18.162 1.00 15.85 ? 135 TYR A C 1 ATOM 1009 O O . TYR A 1 135 ? 16.784 5.799 17.583 1.00 16.10 ? 135 TYR A O 1 ATOM 1010 C CB . TYR A 1 135 ? 19.708 4.948 16.590 1.00 15.52 ? 135 TYR A CB 1 ATOM 1011 C CG . TYR A 1 135 ? 21.044 5.238 16.032 1.00 15.19 ? 135 TYR A CG 1 ATOM 1012 C CD1 . TYR A 1 135 ? 21.238 6.336 15.262 1.00 14.95 ? 135 TYR A CD1 1 ATOM 1013 C CD2 . TYR A 1 135 ? 22.109 4.378 16.281 1.00 15.22 ? 135 TYR A CD2 1 ATOM 1014 C CE1 . TYR A 1 135 ? 22.461 6.552 14.659 1.00 15.83 ? 135 TYR A CE1 1 ATOM 1015 C CE2 . TYR A 1 135 ? 23.339 4.576 15.731 1.00 15.68 ? 135 TYR A CE2 1 ATOM 1016 C CZ . TYR A 1 135 ? 23.518 5.686 14.900 1.00 15.80 ? 135 TYR A CZ 1 ATOM 1017 O OH . TYR A 1 135 ? 24.744 5.932 14.345 1.00 15.70 ? 135 TYR A OH 1 ATOM 1018 N N . LYS A 1 136 ? 17.823 4.729 19.278 1.00 16.09 ? 136 LYS A N 1 ATOM 1019 C CA . LYS A 1 136 ? 16.579 4.300 19.989 1.00 17.79 ? 136 LYS A CA 1 ATOM 1020 C C . LYS A 1 136 ? 16.175 5.313 21.101 1.00 17.77 ? 136 LYS A C 1 ATOM 1021 O O . LYS A 1 136 ? 15.293 5.070 21.881 1.00 18.74 ? 136 LYS A O 1 ATOM 1022 C CB . LYS A 1 136 ? 16.770 2.918 20.596 1.00 18.00 ? 136 LYS A CB 1 ATOM 1023 C CG . LYS A 1 136 ? 17.044 1.830 19.559 1.00 17.94 ? 136 LYS A CG 1 ATOM 1024 C CD . LYS A 1 136 ? 17.030 0.402 20.192 1.00 17.95 ? 136 LYS A CD 1 ATOM 1025 C CE . LYS A 1 136 ? 17.167 -0.705 19.144 1.00 18.03 ? 136 LYS A CE 1 ATOM 1026 N NZ . LYS A 1 136 ? 18.569 -0.571 18.620 1.00 18.28 ? 136 LYS A NZ 1 ATOM 1027 N N . GLY A 1 137 ? 16.820 6.468 21.147 1.00 17.10 ? 137 GLY A N 1 ATOM 1028 C CA . GLY A 1 137 ? 16.622 7.379 22.284 1.00 17.38 ? 137 GLY A CA 1 ATOM 1029 C C . GLY A 1 137 ? 17.238 6.841 23.568 1.00 17.51 ? 137 GLY A C 1 ATOM 1030 O O . GLY A 1 137 ? 18.132 5.961 23.538 1.00 16.16 ? 137 GLY A O 1 ATOM 1031 N N . THR A 1 138 ? 16.793 7.422 24.682 1.00 17.48 ? 138 THR A N 1 ATOM 1032 C CA . THR A 1 138 ? 17.229 6.960 25.977 1.00 18.79 ? 138 THR A CA 1 ATOM 1033 C C . THR A 1 138 ? 16.064 6.819 26.962 1.00 19.37 ? 138 THR A C 1 ATOM 1034 O O . THR A 1 138 ? 15.189 7.652 26.959 1.00 18.15 ? 138 THR A O 1 ATOM 1035 C CB . THR A 1 138 ? 18.341 7.842 26.557 1.00 18.45 ? 138 THR A CB 1 ATOM 1036 O OG1 . THR A 1 138 ? 18.727 7.291 27.801 1.00 18.99 ? 138 THR A OG1 1 ATOM 1037 C CG2 . THR A 1 138 ? 17.928 9.327 26.729 1.00 19.35 ? 138 THR A CG2 1 ATOM 1038 N N . VAL A 1 139 ? 16.105 5.781 27.801 1.00 19.68 ? 139 VAL A N 1 ATOM 1039 C CA . VAL A 1 139 ? 15.106 5.635 28.895 1.00 21.16 ? 139 VAL A CA 1 ATOM 1040 C C . VAL A 1 139 ? 15.264 6.668 30.000 1.00 22.95 ? 139 VAL A C 1 ATOM 1041 O O . VAL A 1 139 ? 14.348 6.918 30.750 1.00 22.46 ? 139 VAL A O 1 ATOM 1042 C CB . VAL A 1 139 ? 15.151 4.259 29.553 1.00 22.48 ? 139 VAL A CB 1 ATOM 1043 C CG1 . VAL A 1 139 ? 14.871 3.126 28.562 1.00 22.21 ? 139 VAL A CG1 1 ATOM 1044 C CG2 . VAL A 1 139 ? 16.461 4.024 30.253 1.00 22.31 ? 139 VAL A CG2 1 ATOM 1045 N N . LEU A 1 140 ? 16.419 7.320 30.074 1.00 23.45 ? 140 LEU A N 1 ATOM 1046 C CA . LEU A 1 140 ? 16.684 8.261 31.163 1.00 24.16 ? 140 LEU A CA 1 ATOM 1047 C C . LEU A 1 140 ? 15.851 9.536 31.010 1.00 23.41 ? 140 LEU A C 1 ATOM 1048 O O . LEU A 1 140 ? 15.641 10.237 31.972 1.00 23.10 ? 140 LEU A O 1 ATOM 1049 C CB . LEU A 1 140 ? 18.235 8.522 31.270 1.00 25.28 ? 140 LEU A CB 1 ATOM 1050 C CG . LEU A 1 140 ? 19.055 7.194 31.275 1.00 26.71 ? 140 LEU A CG 1 ATOM 1051 C CD1 . LEU A 1 140 ? 20.506 7.287 31.601 1.00 28.69 ? 140 LEU A CD1 1 ATOM 1052 C CD2 . LEU A 1 140 ? 18.482 6.108 32.188 1.00 29.53 ? 140 LEU A CD2 1 ATOM 1053 N N . ALA A 1 141 ? 15.364 9.861 29.800 1.00 21.86 ? 141 ALA A N 1 ATOM 1054 C CA . ALA A 1 141 ? 14.579 11.069 29.608 1.00 20.56 ? 141 ALA A CA 1 ATOM 1055 C C . ALA A 1 141 ? 13.096 11.021 30.057 1.00 20.73 ? 141 ALA A C 1 ATOM 1056 O O . ALA A 1 141 ? 12.477 12.080 30.249 1.00 21.20 ? 141 ALA A O 1 ATOM 1057 C CB . ALA A 1 141 ? 14.647 11.474 28.124 1.00 21.50 ? 141 ALA A CB 1 ATOM 1058 N N . GLY A 1 142 ? 12.545 9.819 30.174 1.00 19.89 ? 142 GLY A N 1 ATOM 1059 C CA . GLY A 1 142 ? 11.153 9.605 30.515 1.00 21.30 ? 142 GLY A CA 1 ATOM 1060 C C . GLY A 1 142 ? 10.622 10.395 31.703 1.00 21.59 ? 142 GLY A C 1 ATOM 1061 O O . GLY A 1 142 ? 9.620 11.100 31.572 1.00 22.03 ? 142 GLY A O 1 ATOM 1062 N N . PRO A 1 143 ? 11.295 10.296 32.846 1.00 22.12 ? 143 PRO A N 1 ATOM 1063 C CA . PRO A 1 143 ? 10.818 11.023 34.065 1.00 22.93 ? 143 PRO A CA 1 ATOM 1064 C C . PRO A 1 143 ? 10.810 12.534 33.909 1.00 23.42 ? 143 PRO A C 1 ATOM 1065 O O . PRO A 1 143 ? 9.885 13.205 34.397 1.00 25.22 ? 143 PRO A O 1 ATOM 1066 C CB . PRO A 1 143 ? 11.815 10.556 35.134 1.00 23.38 ? 143 PRO A CB 1 ATOM 1067 C CG . PRO A 1 143 ? 12.315 9.197 34.592 1.00 23.00 ? 143 PRO A CG 1 ATOM 1068 C CD . PRO A 1 143 ? 12.450 9.413 33.143 1.00 21.62 ? 143 PRO A CD 1 ATOM 1069 N N . LEU A 1 144 ? 11.759 13.061 33.156 1.00 22.51 ? 144 LEU A N 1 ATOM 1070 C CA . LEU A 1 144 ? 11.846 14.502 32.908 1.00 23.87 ? 144 LEU A CA 1 ATOM 1071 C C . LEU A 1 144 ? 10.666 14.939 32.074 1.00 23.02 ? 144 LEU A C 1 ATOM 1072 O O . LEU A 1 144 ? 10.021 15.968 32.354 1.00 22.97 ? 144 LEU A O 1 ATOM 1073 C CB . LEU A 1 144 ? 13.131 14.895 32.179 1.00 25.53 ? 144 LEU A CB 1 ATOM 1074 C CG . LEU A 1 144 ? 14.474 14.710 32.855 1.00 26.73 ? 144 LEU A CG 1 ATOM 1075 C CD1 . LEU A 1 144 ? 15.640 15.039 31.900 1.00 27.66 ? 144 LEU A CD1 1 ATOM 1076 C CD2 . LEU A 1 144 ? 14.508 15.628 34.057 1.00 28.08 ? 144 LEU A CD2 1 ATOM 1077 N N . ASP A 1 145 ? 10.358 14.134 31.088 1.00 21.24 ? 145 ASP A N 1 ATOM 1078 C CA . ASP A 1 145 ? 9.224 14.399 30.242 1.00 21.11 ? 145 ASP A CA 1 ATOM 1079 C C . ASP A 1 145 ? 7.944 14.475 31.046 1.00 21.76 ? 145 ASP A C 1 ATOM 1080 O O . ASP A 1 145 ? 7.137 15.381 30.803 1.00 21.77 ? 145 ASP A O 1 ATOM 1081 C CB . ASP A 1 145 ? 9.003 13.292 29.212 1.00 19.70 ? 145 ASP A CB 1 ATOM 1082 C CG . ASP A 1 145 ? 10.122 13.159 28.182 1.00 19.13 ? 145 ASP A CG 1 ATOM 1083 O OD1 . ASP A 1 145 ? 10.986 14.038 28.061 1.00 19.23 ? 145 ASP A OD1 1 ATOM 1084 O OD2 . ASP A 1 145 ? 10.148 12.114 27.496 1.00 17.78 ? 145 ASP A OD2 1 ATOM 1085 N N . ALA A 1 146 ? 7.719 13.471 31.921 1.00 22.93 ? 146 ALA A N 1 ATOM 1086 C CA . ALA A 1 146 ? 6.552 13.354 32.815 1.00 23.08 ? 146 ALA A CA 1 ATOM 1087 C C . ALA A 1 146 ? 6.368 14.589 33.685 1.00 24.17 ? 146 ALA A C 1 ATOM 1088 O O . ALA A 1 146 ? 5.249 14.990 33.962 1.00 24.84 ? 146 ALA A O 1 ATOM 1089 C CB . ALA A 1 146 ? 6.642 12.077 33.660 1.00 23.16 ? 146 ALA A CB 1 ATOM 1090 N N . LEU A 1 147 ? 7.455 15.266 34.026 1.00 23.92 ? 147 LEU A N 1 ATOM 1091 C CA . LEU A 1 147 ? 7.390 16.573 34.737 1.00 24.78 ? 147 LEU A CA 1 ATOM 1092 C C . LEU A 1 147 ? 7.338 17.834 33.902 1.00 24.44 ? 147 LEU A C 1 ATOM 1093 O O . LEU A 1 147 ? 7.356 18.912 34.488 1.00 23.72 ? 147 LEU A O 1 ATOM 1094 C CB . LEU A 1 147 ? 8.609 16.717 35.667 1.00 24.69 ? 147 LEU A CB 1 ATOM 1095 C CG . LEU A 1 147 ? 8.501 15.767 36.887 1.00 27.07 ? 147 LEU A CG 1 ATOM 1096 C CD1 . LEU A 1 147 ? 9.846 15.645 37.605 1.00 26.96 ? 147 LEU A CD1 1 ATOM 1097 C CD2 . LEU A 1 147 ? 7.356 16.212 37.841 1.00 27.40 ? 147 LEU A CD2 1 ATOM 1098 N N . ALA A 1 148 ? 7.297 17.694 32.561 1.00 26.04 ? 148 ALA A N 1 ATOM 1099 C CA . ALA A 1 148 ? 7.244 18.793 31.577 1.00 26.56 ? 148 ALA A CA 1 ATOM 1100 C C . ALA A 1 148 ? 8.416 19.727 31.690 1.00 30.15 ? 148 ALA A C 1 ATOM 1101 O O . ALA A 1 148 ? 8.282 20.952 31.458 1.00 31.99 ? 148 ALA A O 1 ATOM 1102 C CB . ALA A 1 148 ? 5.947 19.564 31.691 1.00 28.10 ? 148 ALA A CB 1 ATOM 1103 N N . VAL A 1 149 ? 9.571 19.190 32.079 1.00 27.84 ? 149 VAL A N 1 ATOM 1104 C CA . VAL A 1 149 ? 10.769 20.008 32.133 1.00 28.83 ? 149 VAL A CA 1 ATOM 1105 C C . VAL A 1 149 ? 11.749 19.640 30.986 1.00 26.17 ? 149 VAL A C 1 ATOM 1106 O O . VAL A 1 149 ? 12.922 20.003 31.041 1.00 25.86 ? 149 VAL A O 1 ATOM 1107 C CB . VAL A 1 149 ? 11.507 19.876 33.514 1.00 30.33 ? 149 VAL A CB 1 ATOM 1108 C CG1 . VAL A 1 149 ? 10.621 20.355 34.668 1.00 32.10 ? 149 VAL A CG1 1 ATOM 1109 C CG2 . VAL A 1 149 ? 12.033 18.459 33.790 1.00 30.33 ? 149 VAL A CG2 1 ATOM 1110 N N . SER A 1 150 ? 11.292 18.856 29.996 1.00 23.80 ? 150 SER A N 1 ATOM 1111 C CA . SER A 1 150 ? 12.202 18.441 28.920 1.00 20.97 ? 150 SER A CA 1 ATOM 1112 C C . SER A 1 150 ? 12.204 19.442 27.765 1.00 20.10 ? 150 SER A C 1 ATOM 1113 O O . SER A 1 150 ? 11.156 19.928 27.325 1.00 19.20 ? 150 SER A O 1 ATOM 1114 C CB . SER A 1 150 ? 11.841 17.061 28.403 1.00 20.61 ? 150 SER A CB 1 ATOM 1115 O OG . SER A 1 150 ? 11.986 16.110 29.416 1.00 20.02 ? 150 SER A OG 1 ATOM 1116 N N . ALA A 1 151 ? 13.411 19.713 27.268 1.00 19.89 ? 151 ALA A N 1 ATOM 1117 C CA . ALA A 1 151 ? 13.573 20.456 26.030 1.00 19.06 ? 151 ALA A CA 1 ATOM 1118 C C . ALA A 1 151 ? 12.877 19.709 24.878 1.00 18.81 ? 151 ALA A C 1 ATOM 1119 O O . ALA A 1 151 ? 12.777 18.472 24.926 1.00 18.31 ? 151 ALA A O 1 ATOM 1120 C CB . ALA A 1 151 ? 15.059 20.583 25.714 1.00 19.20 ? 151 ALA A CB 1 ATOM 1121 N N . PRO A 1 152 ? 12.479 20.419 23.817 1.00 18.49 ? 152 PRO A N 1 ATOM 1122 C CA . PRO A 1 152 ? 12.025 19.697 22.597 1.00 18.94 ? 152 PRO A CA 1 ATOM 1123 C C . PRO A 1 152 ? 12.819 18.438 22.138 1.00 18.55 ? 152 PRO A C 1 ATOM 1124 O O . PRO A 1 152 ? 12.241 17.363 21.962 1.00 17.93 ? 152 PRO A O 1 ATOM 1125 C CB . PRO A 1 152 ? 12.076 20.792 21.507 1.00 19.29 ? 152 PRO A CB 1 ATOM 1126 C CG . PRO A 1 152 ? 11.861 22.088 22.238 1.00 20.55 ? 152 PRO A CG 1 ATOM 1127 C CD . PRO A 1 152 ? 12.601 21.878 23.568 1.00 19.73 ? 152 PRO A CD 1 ATOM 1128 N N . SER A 1 153 ? 14.134 18.561 21.958 1.00 18.25 ? 153 SER A N 1 ATOM 1129 C CA . SER A 1 153 ? 14.928 17.378 21.515 1.00 17.26 ? 153 SER A CA 1 ATOM 1130 C C . SER A 1 153 ? 15.063 16.283 22.585 1.00 16.71 ? 153 SER A C 1 ATOM 1131 O O . SER A 1 153 ? 15.351 15.130 22.249 1.00 16.57 ? 153 SER A O 1 ATOM 1132 C CB . SER A 1 153 ? 16.281 17.784 20.991 1.00 16.82 ? 153 SER A CB 1 ATOM 1133 O OG . SER A 1 153 ? 17.119 18.093 22.064 1.00 15.85 ? 153 SER A OG 1 ATOM 1134 N N . VAL A 1 154 ? 14.871 16.604 23.857 1.00 17.16 ? 154 VAL A N 1 ATOM 1135 C CA . VAL A 1 154 ? 14.957 15.600 24.941 1.00 18.15 ? 154 VAL A CA 1 ATOM 1136 C C . VAL A 1 154 ? 13.717 14.701 24.931 1.00 17.73 ? 154 VAL A C 1 ATOM 1137 O O . VAL A 1 154 ? 13.839 13.504 25.073 1.00 16.88 ? 154 VAL A O 1 ATOM 1138 C CB . VAL A 1 154 ? 15.185 16.265 26.332 1.00 19.61 ? 154 VAL A CB 1 ATOM 1139 C CG1 . VAL A 1 154 ? 15.091 15.277 27.518 1.00 20.20 ? 154 VAL A CG1 1 ATOM 1140 C CG2 . VAL A 1 154 ? 16.527 16.974 26.333 1.00 19.90 ? 154 VAL A CG2 1 ATOM 1141 N N . TRP A 1 155 ? 12.533 15.297 24.779 1.00 16.76 ? 155 TRP A N 1 ATOM 1142 C CA . TRP A 1 155 ? 11.343 14.563 24.416 1.00 17.29 ? 155 TRP A CA 1 ATOM 1143 C C . TRP A 1 155 ? 11.589 13.614 23.239 1.00 16.30 ? 155 TRP A C 1 ATOM 1144 O O . TRP A 1 155 ? 11.279 12.430 23.286 1.00 16.11 ? 155 TRP A O 1 ATOM 1145 C CB . TRP A 1 155 ? 10.209 15.551 24.004 1.00 17.41 ? 155 TRP A CB 1 ATOM 1146 C CG . TRP A 1 155 ? 9.449 16.102 25.117 1.00 18.21 ? 155 TRP A CG 1 ATOM 1147 C CD1 . TRP A 1 155 ? 9.658 17.313 25.725 1.00 18.62 ? 155 TRP A CD1 1 ATOM 1148 C CD2 . TRP A 1 155 ? 8.367 15.474 25.814 1.00 18.21 ? 155 TRP A CD2 1 ATOM 1149 N NE1 . TRP A 1 155 ? 8.735 17.483 26.753 1.00 19.06 ? 155 TRP A NE1 1 ATOM 1150 C CE2 . TRP A 1 155 ? 7.923 16.383 26.810 1.00 18.60 ? 155 TRP A CE2 1 ATOM 1151 C CE3 . TRP A 1 155 ? 7.700 14.243 25.676 1.00 18.84 ? 155 TRP A CE3 1 ATOM 1152 C CZ2 . TRP A 1 155 ? 6.841 16.094 27.690 1.00 19.79 ? 155 TRP A CZ2 1 ATOM 1153 C CZ3 . TRP A 1 155 ? 6.622 13.928 26.544 1.00 19.19 ? 155 TRP A CZ3 1 ATOM 1154 C CH2 . TRP A 1 155 ? 6.175 14.893 27.529 1.00 20.01 ? 155 TRP A CH2 1 ATOM 1155 N N . GLN A 1 156 ? 12.127 14.174 22.156 1.00 15.42 ? 156 GLN A N 1 ATOM 1156 C CA . GLN A 1 156 ? 12.366 13.339 20.951 1.00 15.10 ? 156 GLN A CA 1 ATOM 1157 C C . GLN A 1 156 ? 13.349 12.187 21.093 1.00 15.09 ? 156 GLN A C 1 ATOM 1158 O O . GLN A 1 156 ? 13.221 11.117 20.415 1.00 14.81 ? 156 GLN A O 1 ATOM 1159 C CB . GLN A 1 156 ? 12.730 14.239 19.779 1.00 14.75 ? 156 GLN A CB 1 ATOM 1160 C CG . GLN A 1 156 ? 11.601 15.158 19.420 1.00 15.28 ? 156 GLN A CG 1 ATOM 1161 C CD . GLN A 1 156 ? 12.019 16.213 18.431 1.00 15.46 ? 156 GLN A CD 1 ATOM 1162 O OE1 . GLN A 1 156 ? 12.880 16.963 18.713 1.00 15.26 ? 156 GLN A OE1 1 ATOM 1163 N NE2 . GLN A 1 156 ? 11.372 16.277 17.292 1.00 16.14 ? 156 GLN A NE2 1 ATOM 1164 N N . GLN A 1 157 ? 14.328 12.374 22.007 1.00 14.88 ? 157 GLN A N 1 ATOM 1165 C CA . GLN A 1 157 ? 15.359 11.404 22.313 1.00 14.82 ? 157 GLN A CA 1 ATOM 1166 C C . GLN A 1 157 ? 14.934 10.449 23.439 1.00 15.63 ? 157 GLN A C 1 ATOM 1167 O O . GLN A 1 157 ? 15.748 9.726 23.968 1.00 14.62 ? 157 GLN A O 1 ATOM 1168 C CB . GLN A 1 157 ? 16.629 12.165 22.707 1.00 14.92 ? 157 GLN A CB 1 ATOM 1169 C CG . GLN A 1 157 ? 17.341 12.828 21.550 1.00 15.24 ? 157 GLN A CG 1 ATOM 1170 C CD . GLN A 1 157 ? 18.493 13.592 22.010 1.00 15.58 ? 157 GLN A CD 1 ATOM 1171 O OE1 . GLN A 1 157 ? 18.399 14.844 22.316 1.00 16.88 ? 157 GLN A OE1 1 ATOM 1172 N NE2 . GLN A 1 157 ? 19.592 12.914 22.115 1.00 15.17 ? 157 GLN A NE2 1 ATOM 1173 N N . THR A 1 158 ? 13.663 10.541 23.878 1.00 16.27 ? 158 THR A N 1 ATOM 1174 C CA . THR A 1 158 ? 13.081 9.604 24.790 1.00 17.16 ? 158 THR A CA 1 ATOM 1175 C C . THR A 1 158 ? 12.731 8.252 24.153 1.00 17.49 ? 158 THR A C 1 ATOM 1176 O O . THR A 1 158 ? 12.018 8.200 23.195 1.00 17.97 ? 158 THR A O 1 ATOM 1177 C CB . THR A 1 158 ? 11.821 10.201 25.459 1.00 17.23 ? 158 THR A CB 1 ATOM 1178 O OG1 . THR A 1 158 ? 12.205 11.389 26.155 1.00 16.30 ? 158 THR A OG1 1 ATOM 1179 C CG2 . THR A 1 158 ? 11.217 9.224 26.481 1.00 17.69 ? 158 THR A CG2 1 ATOM 1180 N N . THR A 1 159 ? 13.187 7.144 24.744 1.00 17.69 ? 159 THR A N 1 ATOM 1181 C CA A THR A 1 159 ? 12.737 5.827 24.322 0.50 18.19 ? 159 THR A CA 1 ATOM 1182 C CA B THR A 1 159 ? 12.760 5.843 24.233 0.50 18.76 ? 159 THR A CA 1 ATOM 1183 C C . THR A 1 159 ? 11.211 5.799 24.097 1.00 18.76 ? 159 THR A C 1 ATOM 1184 O O . THR A 1 159 ? 10.454 6.276 24.932 1.00 18.14 ? 159 THR A O 1 ATOM 1185 C CB A THR A 1 159 ? 13.219 4.775 25.333 0.50 18.28 ? 159 THR A CB 1 ATOM 1186 C CB B THR A 1 159 ? 13.344 4.678 25.059 0.50 19.46 ? 159 THR A CB 1 ATOM 1187 O OG1 A THR A 1 159 ? 14.636 4.606 25.141 0.50 17.33 ? 159 THR A OG1 1 ATOM 1188 O OG1 B THR A 1 159 ? 13.053 3.400 24.414 0.50 21.09 ? 159 THR A OG1 1 ATOM 1189 C CG2 A THR A 1 159 ? 12.463 3.383 25.113 0.50 18.75 ? 159 THR A CG2 1 ATOM 1190 C CG2 B THR A 1 159 ? 12.757 4.699 26.396 0.50 19.18 ? 159 THR A CG2 1 ATOM 1191 N N . GLY A 1 160 ? 10.748 5.269 22.975 1.00 19.69 ? 160 GLY A N 1 ATOM 1192 C CA . GLY A 1 160 ? 9.311 5.255 22.695 1.00 19.83 ? 160 GLY A CA 1 ATOM 1193 C C . GLY A 1 160 ? 8.742 6.478 22.043 1.00 19.72 ? 160 GLY A C 1 ATOM 1194 O O . GLY A 1 160 ? 7.541 6.513 21.750 1.00 19.95 ? 160 GLY A O 1 ATOM 1195 N N . SER A 1 161 ? 9.587 7.463 21.729 1.00 18.37 ? 161 SER A N 1 ATOM 1196 C CA . SER A 1 161 ? 9.110 8.768 21.281 1.00 17.65 ? 161 SER A CA 1 ATOM 1197 C C . SER A 1 161 ? 8.514 8.601 19.892 1.00 17.58 ? 161 SER A C 1 ATOM 1198 O O . SER A 1 161 ? 8.740 7.561 19.218 1.00 18.74 ? 161 SER A O 1 ATOM 1199 C CB . SER A 1 161 ? 10.250 9.791 21.274 1.00 16.54 ? 161 SER A CB 1 ATOM 1200 O OG . SER A 1 161 ? 11.268 9.361 20.333 1.00 15.88 ? 161 SER A OG 1 ATOM 1201 N N . ALA A 1 162 ? 7.722 9.603 19.490 1.00 17.05 ? 162 ALA A N 1 ATOM 1202 C CA . ALA A 1 162 ? 7.213 9.674 18.110 1.00 16.50 ? 162 ALA A CA 1 ATOM 1203 C C . ALA A 1 162 ? 8.381 9.676 17.099 1.00 15.84 ? 162 ALA A C 1 ATOM 1204 O O . ALA A 1 162 ? 8.398 8.893 16.129 1.00 14.70 ? 162 ALA A O 1 ATOM 1205 C CB . ALA A 1 162 ? 6.270 10.866 17.925 1.00 16.87 ? 162 ALA A CB 1 ATOM 1206 N N . LEU A 1 163 ? 9.419 10.405 17.434 1.00 15.73 ? 163 LEU A N 1 ATOM 1207 C CA . LEU A 1 163 ? 10.584 10.533 16.567 1.00 15.00 ? 163 LEU A CA 1 ATOM 1208 C C . LEU A 1 163 ? 11.381 9.222 16.414 1.00 14.90 ? 163 LEU A C 1 ATOM 1209 O O . LEU A 1 163 ? 11.672 8.838 15.288 1.00 15.14 ? 163 LEU A O 1 ATOM 1210 C CB . LEU A 1 163 ? 11.504 11.677 17.081 1.00 14.92 ? 163 LEU A CB 1 ATOM 1211 C CG . LEU A 1 163 ? 12.643 11.885 16.066 1.00 14.52 ? 163 LEU A CG 1 ATOM 1212 C CD1 . LEU A 1 163 ? 12.547 13.241 15.390 1.00 15.19 ? 163 LEU A CD1 1 ATOM 1213 C CD2 . LEU A 1 163 ? 13.979 11.706 16.816 1.00 14.90 ? 163 LEU A CD2 1 ATOM 1214 N N . THR A 1 164 ? 11.737 8.535 17.522 1.00 15.19 ? 164 THR A N 1 ATOM 1215 C CA . THR A 1 164 ? 12.420 7.248 17.453 1.00 15.59 ? 164 THR A CA 1 ATOM 1216 C C . THR A 1 164 ? 11.587 6.154 16.796 1.00 15.93 ? 164 THR A C 1 ATOM 1217 O O . THR A 1 164 ? 12.135 5.325 16.074 1.00 16.61 ? 164 THR A O 1 ATOM 1218 C CB . THR A 1 164 ? 12.977 6.822 18.807 1.00 15.46 ? 164 THR A CB 1 ATOM 1219 O OG1 . THR A 1 164 ? 11.967 6.858 19.791 1.00 16.15 ? 164 THR A OG1 1 ATOM 1220 C CG2 . THR A 1 164 ? 14.081 7.832 19.234 1.00 15.92 ? 164 THR A CG2 1 ATOM 1221 N N . THR A 1 165 ? 10.275 6.194 16.989 1.00 16.07 ? 165 THR A N 1 ATOM 1222 C CA . THR A 1 165 ? 9.369 5.298 16.287 1.00 16.99 ? 165 THR A CA 1 ATOM 1223 C C . THR A 1 165 ? 9.457 5.502 14.765 1.00 16.85 ? 165 THR A C 1 ATOM 1224 O O . THR A 1 165 ? 9.624 4.546 13.988 1.00 17.82 ? 165 THR A O 1 ATOM 1225 C CB . THR A 1 165 ? 7.915 5.493 16.797 1.00 17.51 ? 165 THR A CB 1 ATOM 1226 O OG1 . THR A 1 165 ? 7.898 5.257 18.204 1.00 17.48 ? 165 THR A OG1 1 ATOM 1227 C CG2 . THR A 1 165 ? 6.874 4.585 16.107 1.00 17.68 ? 165 THR A CG2 1 ATOM 1228 N N . ALA A 1 166 ? 9.299 6.757 14.364 1.00 16.52 ? 166 ALA A N 1 ATOM 1229 C CA . ALA A 1 166 ? 9.321 7.106 12.976 1.00 16.14 ? 166 ALA A CA 1 ATOM 1230 C C . ALA A 1 166 ? 10.624 6.637 12.339 1.00 16.34 ? 166 ALA A C 1 ATOM 1231 O O . ALA A 1 166 ? 10.606 6.082 11.181 1.00 15.46 ? 166 ALA A O 1 ATOM 1232 C CB . ALA A 1 166 ? 9.103 8.602 12.797 1.00 15.83 ? 166 ALA A CB 1 ATOM 1233 N N . LEU A 1 167 ? 11.745 6.936 13.007 1.00 15.50 ? 167 LEU A N 1 ATOM 1234 C CA . LEU A 1 167 ? 13.084 6.508 12.453 1.00 16.10 ? 167 LEU A CA 1 ATOM 1235 C C . LEU A 1 167 ? 13.143 5.005 12.198 1.00 16.87 ? 167 LEU A C 1 ATOM 1236 O O . LEU A 1 167 ? 13.514 4.539 11.088 1.00 16.88 ? 167 LEU A O 1 ATOM 1237 C CB . LEU A 1 167 ? 14.226 6.921 13.410 1.00 15.62 ? 167 LEU A CB 1 ATOM 1238 C CG . LEU A 1 167 ? 15.600 6.487 13.017 1.00 15.78 ? 167 LEU A CG 1 ATOM 1239 C CD1 . LEU A 1 167 ? 15.971 7.193 11.712 1.00 16.09 ? 167 LEU A CD1 1 ATOM 1240 C CD2 . LEU A 1 167 ? 16.640 6.736 14.100 1.00 16.28 ? 167 LEU A CD2 1 ATOM 1241 N N . ARG A 1 168 ? 12.740 4.220 13.194 1.00 17.36 ? 168 ARG A N 1 ATOM 1242 C CA . ARG A 1 168 ? 12.893 2.764 13.052 1.00 18.01 ? 168 ARG A CA 1 ATOM 1243 C C . ARG A 1 168 ? 11.887 2.194 11.977 1.00 18.54 ? 168 ARG A C 1 ATOM 1244 O O . ARG A 1 168 ? 12.213 1.320 11.190 1.00 18.06 ? 168 ARG A O 1 ATOM 1245 C CB . ARG A 1 168 ? 12.793 2.064 14.411 1.00 18.73 ? 168 ARG A CB 1 ATOM 1246 C CG . ARG A 1 168 ? 11.426 1.800 14.943 1.00 20.02 ? 168 ARG A CG 1 ATOM 1247 C CD . ARG A 1 168 ? 11.409 0.815 16.119 1.00 20.54 ? 168 ARG A CD 1 ATOM 1248 N NE . ARG A 1 168 ? 10.056 0.913 16.636 1.00 20.93 ? 168 ARG A NE 1 ATOM 1249 C CZ . ARG A 1 168 ? 9.672 1.659 17.647 1.00 22.72 ? 168 ARG A CZ 1 ATOM 1250 N NH1 . ARG A 1 168 ? 10.543 2.273 18.452 1.00 23.40 ? 168 ARG A NH1 1 ATOM 1251 N NH2 . ARG A 1 168 ? 8.380 1.660 17.967 1.00 24.30 ? 168 ARG A NH2 1 ATOM 1252 N N . ASN A 1 169 ? 10.668 2.726 11.978 1.00 18.39 ? 169 ASN A N 1 ATOM 1253 C CA . ASN A 1 169 ? 9.675 2.297 11.007 1.00 18.28 ? 169 ASN A CA 1 ATOM 1254 C C . ASN A 1 169 ? 9.985 2.680 9.571 1.00 18.95 ? 169 ASN A C 1 ATOM 1255 O O . ASN A 1 169 ? 9.515 2.010 8.691 1.00 18.80 ? 169 ASN A O 1 ATOM 1256 C CB . ASN A 1 169 ? 8.290 2.746 11.424 1.00 17.72 ? 169 ASN A CB 1 ATOM 1257 C CG . ASN A 1 169 ? 7.727 1.887 12.542 1.00 18.61 ? 169 ASN A CG 1 ATOM 1258 O OD1 . ASN A 1 169 ? 8.126 0.752 12.708 1.00 17.61 ? 169 ASN A OD1 1 ATOM 1259 N ND2 . ASN A 1 169 ? 6.776 2.438 13.305 1.00 18.10 ? 169 ASN A ND2 1 ATOM 1260 N N . ALA A 1 170 ? 10.814 3.692 9.327 1.00 18.39 ? 170 ALA A N 1 ATOM 1261 C CA . ALA A 1 170 ? 11.259 4.047 8.009 1.00 18.32 ? 170 ALA A CA 1 ATOM 1262 C C . ALA A 1 170 ? 12.527 3.327 7.576 1.00 18.89 ? 170 ALA A C 1 ATOM 1263 O O . ALA A 1 170 ? 13.008 3.576 6.493 1.00 20.08 ? 170 ALA A O 1 ATOM 1264 C CB . ALA A 1 170 ? 11.537 5.547 7.964 1.00 18.46 ? 170 ALA A CB 1 ATOM 1265 N N . GLY A 1 171 ? 13.090 2.467 8.417 1.00 19.02 ? 171 GLY A N 1 ATOM 1266 C CA . GLY A 1 171 ? 14.273 1.653 8.079 1.00 18.97 ? 171 GLY A CA 1 ATOM 1267 C C . GLY A 1 171 ? 15.551 2.166 8.657 1.00 18.76 ? 171 GLY A C 1 ATOM 1268 O O . GLY A 1 171 ? 16.581 1.584 8.390 1.00 20.23 ? 171 GLY A O 1 ATOM 1269 N N . GLY A 1 172 ? 15.461 3.166 9.526 1.00 18.85 ? 172 GLY A N 1 ATOM 1270 C CA . GLY A 1 172 ? 16.570 3.914 10.047 1.00 18.44 ? 172 GLY A CA 1 ATOM 1271 C C . GLY A 1 172 ? 17.469 3.207 11.036 1.00 17.38 ? 172 GLY A C 1 ATOM 1272 O O . GLY A 1 172 ? 18.514 3.767 11.424 1.00 17.27 ? 172 GLY A O 1 ATOM 1273 N N . LEU A 1 173 ? 17.030 2.035 11.512 1.00 17.38 ? 173 LEU A N 1 ATOM 1274 C CA . LEU A 1 173 ? 17.901 1.221 12.391 1.00 17.60 ? 173 LEU A CA 1 ATOM 1275 C C . LEU A 1 173 ? 18.860 0.250 11.688 1.00 17.84 ? 173 LEU A C 1 ATOM 1276 O O . LEU A 1 173 ? 19.573 -0.506 12.365 1.00 17.97 ? 173 LEU A O 1 ATOM 1277 C CB . LEU A 1 173 ? 17.157 0.540 13.568 1.00 17.99 ? 173 LEU A CB 1 ATOM 1278 C CG . LEU A 1 173 ? 16.356 1.465 14.510 1.00 18.42 ? 173 LEU A CG 1 ATOM 1279 C CD1 . LEU A 1 173 ? 15.857 0.653 15.668 1.00 19.45 ? 173 LEU A CD1 1 ATOM 1280 C CD2 . LEU A 1 173 ? 17.211 2.597 15.005 1.00 18.38 ? 173 LEU A CD2 1 ATOM 1281 N N . THR A 1 174 ? 18.928 0.340 10.372 1.00 17.79 ? 174 THR A N 1 ATOM 1282 C CA . THR A 1 174 ? 19.856 -0.352 9.545 1.00 18.22 ? 174 THR A CA 1 ATOM 1283 C C . THR A 1 174 ? 20.799 0.717 8.965 1.00 18.89 ? 174 THR A C 1 ATOM 1284 O O . THR A 1 174 ? 20.347 1.761 8.507 1.00 18.28 ? 174 THR A O 1 ATOM 1285 C CB . THR A 1 174 ? 19.082 -1.100 8.408 1.00 18.36 ? 174 THR A CB 1 ATOM 1286 O OG1 . THR A 1 174 ? 18.389 -2.185 9.013 1.00 17.35 ? 174 THR A OG1 1 ATOM 1287 C CG2 . THR A 1 174 ? 20.008 -1.708 7.416 1.00 19.08 ? 174 THR A CG2 1 ATOM 1288 N N . GLN A 1 175 ? 22.105 0.453 8.945 1.00 20.32 ? 175 GLN A N 1 ATOM 1289 C CA . GLN A 1 175 ? 23.018 1.478 8.411 1.00 21.05 ? 175 GLN A CA 1 ATOM 1290 C C . GLN A 1 175 ? 22.658 1.749 6.945 1.00 21.21 ? 175 GLN A C 1 ATOM 1291 O O . GLN A 1 175 ? 22.101 0.864 6.232 1.00 21.28 ? 175 GLN A O 1 ATOM 1292 C CB . GLN A 1 175 ? 24.492 1.099 8.526 1.00 21.39 ? 175 GLN A CB 1 ATOM 1293 C CG . GLN A 1 175 ? 24.995 0.214 7.416 1.00 22.55 ? 175 GLN A CG 1 ATOM 1294 C CD . GLN A 1 175 ? 26.507 0.048 7.461 1.00 23.43 ? 175 GLN A CD 1 ATOM 1295 O OE1 . GLN A 1 175 ? 27.206 0.509 8.378 1.00 22.19 ? 175 GLN A OE1 1 ATOM 1296 N NE2 . GLN A 1 175 ? 27.024 -0.604 6.433 1.00 23.75 ? 175 GLN A NE2 1 ATOM 1297 N N . ILE A 1 176 ? 22.878 2.978 6.553 1.00 20.15 ? 176 ILE A N 1 ATOM 1298 C CA . ILE A 1 176 ? 22.493 3.488 5.210 1.00 20.63 ? 176 ILE A CA 1 ATOM 1299 C C . ILE A 1 176 ? 23.770 3.852 4.417 1.00 20.96 ? 176 ILE A C 1 ATOM 1300 O O . ILE A 1 176 ? 23.845 3.631 3.239 1.00 21.08 ? 176 ILE A O 1 ATOM 1301 C CB . ILE A 1 176 ? 21.584 4.733 5.363 1.00 21.09 ? 176 ILE A CB 1 ATOM 1302 C CG1 . ILE A 1 176 ? 20.260 4.297 6.014 1.00 21.06 ? 176 ILE A CG1 1 ATOM 1303 C CG2 . ILE A 1 176 ? 21.368 5.417 4.019 1.00 20.66 ? 176 ILE A CG2 1 ATOM 1304 C CD1 . ILE A 1 176 ? 19.318 5.419 6.407 1.00 20.56 ? 176 ILE A CD1 1 ATOM 1305 N N . VAL A 1 177 ? 24.782 4.347 5.097 1.00 20.21 ? 177 VAL A N 1 ATOM 1306 C CA . VAL A 1 177 ? 26.154 4.406 4.561 1.00 20.56 ? 177 VAL A CA 1 ATOM 1307 C C . VAL A 1 177 ? 27.007 3.600 5.512 1.00 20.97 ? 177 VAL A C 1 ATOM 1308 O O . VAL A 1 177 ? 26.531 3.297 6.607 1.00 20.73 ? 177 VAL A O 1 ATOM 1309 C CB . VAL A 1 177 ? 26.624 5.886 4.517 1.00 19.40 ? 177 VAL A CB 1 ATOM 1310 C CG1 . VAL A 1 177 ? 25.662 6.734 3.736 1.00 19.05 ? 177 VAL A CG1 1 ATOM 1311 C CG2 . VAL A 1 177 ? 26.786 6.447 5.922 1.00 19.38 ? 177 VAL A CG2 1 ATOM 1312 N N . PRO A 1 178 ? 28.284 3.259 5.128 1.00 22.17 ? 178 PRO A N 1 ATOM 1313 C CA . PRO A 1 178 ? 29.146 2.511 6.052 1.00 21.46 ? 178 PRO A CA 1 ATOM 1314 C C . PRO A 1 178 ? 29.270 3.282 7.397 1.00 20.34 ? 178 PRO A C 1 ATOM 1315 O O . PRO A 1 178 ? 29.693 4.438 7.423 1.00 19.70 ? 178 PRO A O 1 ATOM 1316 C CB . PRO A 1 178 ? 30.499 2.476 5.330 1.00 22.22 ? 178 PRO A CB 1 ATOM 1317 C CG . PRO A 1 178 ? 30.191 2.638 3.853 1.00 22.69 ? 178 PRO A CG 1 ATOM 1318 C CD . PRO A 1 178 ? 28.977 3.554 3.843 1.00 23.10 ? 178 PRO A CD 1 ATOM 1319 N N . THR A 1 179 ? 28.820 2.646 8.465 1.00 20.43 ? 179 THR A N 1 ATOM 1320 C CA . THR A 1 179 ? 28.715 3.268 9.806 1.00 19.99 ? 179 THR A CA 1 ATOM 1321 C C . THR A 1 179 ? 29.446 2.455 10.869 1.00 20.27 ? 179 THR A C 1 ATOM 1322 O O . THR A 1 179 ? 29.380 1.206 10.891 1.00 20.87 ? 179 THR A O 1 ATOM 1323 C CB . THR A 1 179 ? 27.241 3.448 10.185 1.00 19.06 ? 179 THR A CB 1 ATOM 1324 O OG1 . THR A 1 179 ? 26.673 4.305 9.220 1.00 18.23 ? 179 THR A OG1 1 ATOM 1325 C CG2 . THR A 1 179 ? 27.054 4.092 11.543 1.00 18.24 ? 179 THR A CG2 1 ATOM 1326 N N . THR A 1 180 ? 30.175 3.187 11.713 1.00 19.15 ? 180 THR A N 1 ATOM 1327 C CA . THR A 1 180 ? 30.803 2.653 12.911 1.00 18.34 ? 180 THR A CA 1 ATOM 1328 C C . THR A 1 180 ? 30.124 3.386 14.122 1.00 17.53 ? 180 THR A C 1 ATOM 1329 O O . THR A 1 180 ? 30.032 4.631 14.148 1.00 17.00 ? 180 THR A O 1 ATOM 1330 C CB . THR A 1 180 ? 32.334 2.907 12.886 1.00 18.37 ? 180 THR A CB 1 ATOM 1331 O OG1 . THR A 1 180 ? 32.925 2.375 11.680 1.00 19.09 ? 180 THR A OG1 1 ATOM 1332 C CG2 . THR A 1 180 ? 33.076 2.298 14.152 1.00 18.36 ? 180 THR A CG2 1 ATOM 1333 N N . ASN A 1 181 ? 29.680 2.597 15.089 1.00 16.61 ? 181 ASN A N 1 ATOM 1334 C CA . ASN A 1 181 ? 29.125 3.024 16.335 1.00 16.74 ? 181 ASN A CA 1 ATOM 1335 C C . ASN A 1 181 ? 30.021 2.635 17.498 1.00 17.39 ? 181 ASN A C 1 ATOM 1336 O O . ASN A 1 181 ? 30.142 1.449 17.795 1.00 18.16 ? 181 ASN A O 1 ATOM 1337 C CB . ASN A 1 181 ? 27.738 2.415 16.491 1.00 16.75 ? 181 ASN A CB 1 ATOM 1338 C CG . ASN A 1 181 ? 26.807 2.851 15.362 1.00 16.83 ? 181 ASN A CG 1 ATOM 1339 O OD1 . ASN A 1 181 ? 26.644 4.034 15.102 1.00 16.21 ? 181 ASN A OD1 1 ATOM 1340 N ND2 . ASN A 1 181 ? 26.234 1.869 14.646 1.00 17.73 ? 181 ASN A ND2 1 ATOM 1341 N N . LEU A 1 182 ? 30.633 3.622 18.162 1.00 16.65 ? 182 LEU A N 1 ATOM 1342 C CA . LEU A 1 182 ? 31.493 3.368 19.368 1.00 17.71 ? 182 LEU A CA 1 ATOM 1343 C C . LEU A 1 182 ? 30.656 3.818 20.581 1.00 17.99 ? 182 LEU A C 1 ATOM 1344 O O . LEU A 1 182 ? 30.203 4.981 20.653 1.00 18.90 ? 182 LEU A O 1 ATOM 1345 C CB . LEU A 1 182 ? 32.841 4.133 19.304 1.00 17.35 ? 182 LEU A CB 1 ATOM 1346 C CG . LEU A 1 182 ? 33.967 3.937 20.335 1.00 17.64 ? 182 LEU A CG 1 ATOM 1347 C CD1 . LEU A 1 182 ? 33.520 4.380 21.717 1.00 18.56 ? 182 LEU A CD1 1 ATOM 1348 C CD2 . LEU A 1 182 ? 34.441 2.495 20.351 1.00 18.90 ? 182 LEU A CD2 1 ATOM 1349 N N . TYR A 1 183 ? 30.445 2.899 21.526 1.00 18.53 ? 183 TYR A N 1 ATOM 1350 C CA . TYR A 1 183 ? 29.605 3.189 22.675 1.00 17.92 ? 183 TYR A CA 1 ATOM 1351 C C . TYR A 1 183 ? 30.019 2.342 23.847 1.00 17.97 ? 183 TYR A C 1 ATOM 1352 O O . TYR A 1 183 ? 30.913 1.511 23.753 1.00 17.90 ? 183 TYR A O 1 ATOM 1353 C CB . TYR A 1 183 ? 28.130 3.023 22.291 1.00 17.74 ? 183 TYR A CB 1 ATOM 1354 C CG . TYR A 1 183 ? 27.653 1.554 21.959 1.00 18.43 ? 183 TYR A CG 1 ATOM 1355 C CD1 . TYR A 1 183 ? 27.907 0.972 20.727 1.00 18.55 ? 183 TYR A CD1 1 ATOM 1356 C CD2 . TYR A 1 183 ? 26.897 0.820 22.887 1.00 17.89 ? 183 TYR A CD2 1 ATOM 1357 C CE1 . TYR A 1 183 ? 27.422 -0.278 20.423 1.00 19.61 ? 183 TYR A CE1 1 ATOM 1358 C CE2 . TYR A 1 183 ? 26.419 -0.429 22.590 1.00 18.93 ? 183 TYR A CE2 1 ATOM 1359 C CZ . TYR A 1 183 ? 26.681 -0.995 21.369 1.00 19.56 ? 183 TYR A CZ 1 ATOM 1360 O OH . TYR A 1 183 ? 26.167 -2.255 21.088 1.00 20.51 ? 183 TYR A OH 1 ATOM 1361 N N . SER A 1 184 ? 29.376 2.580 24.973 1.00 17.60 ? 184 SER A N 1 ATOM 1362 C CA . SER A 1 184 ? 29.754 1.935 26.200 1.00 17.82 ? 184 SER A CA 1 ATOM 1363 C C . SER A 1 184 ? 28.548 1.545 26.972 1.00 18.03 ? 184 SER A C 1 ATOM 1364 O O . SER A 1 184 ? 27.540 2.281 27.069 1.00 17.27 ? 184 SER A O 1 ATOM 1365 C CB . SER A 1 184 ? 30.585 2.959 27.045 1.00 18.37 ? 184 SER A CB 1 ATOM 1366 O OG . SER A 1 184 ? 31.112 2.415 28.270 1.00 18.09 ? 184 SER A OG 1 ATOM 1367 N N . ALA A 1 185 ? 28.669 0.416 27.662 1.00 18.17 ? 185 ALA A N 1 ATOM 1368 C CA . ALA A 1 185 ? 27.613 -0.041 28.580 1.00 17.82 ? 185 ALA A CA 1 ATOM 1369 C C . ALA A 1 185 ? 27.419 0.881 29.759 1.00 17.23 ? 185 ALA A C 1 ATOM 1370 O O . ALA A 1 185 ? 26.369 0.875 30.367 1.00 16.52 ? 185 ALA A O 1 ATOM 1371 C CB . ALA A 1 185 ? 27.910 -1.438 29.105 1.00 17.70 ? 185 ALA A CB 1 ATOM 1372 N N . THR A 1 186 ? 28.495 1.535 30.165 1.00 17.15 ? 186 THR A N 1 ATOM 1373 C CA . THR A 1 186 ? 28.528 2.334 31.346 1.00 18.48 ? 186 THR A CA 1 ATOM 1374 C C . THR A 1 186 ? 28.283 3.796 31.002 1.00 19.64 ? 186 THR A C 1 ATOM 1375 O O . THR A 1 186 ? 29.055 4.663 31.403 1.00 22.27 ? 186 THR A O 1 ATOM 1376 C CB . THR A 1 186 ? 29.895 2.197 32.049 1.00 19.07 ? 186 THR A CB 1 ATOM 1377 O OG1 . THR A 1 186 ? 30.917 2.627 31.164 1.00 19.10 ? 186 THR A OG1 1 ATOM 1378 C CG2 . THR A 1 186 ? 30.187 0.729 32.479 1.00 19.35 ? 186 THR A CG2 1 ATOM 1379 N N . ASP A 1 187 ? 27.279 4.021 30.170 1.00 18.72 ? 187 ASP A N 1 ATOM 1380 C CA . ASP A 1 187 ? 26.797 5.311 29.759 1.00 18.24 ? 187 ASP A CA 1 ATOM 1381 C C . ASP A 1 187 ? 25.678 5.755 30.709 1.00 18.96 ? 187 ASP A C 1 ATOM 1382 O O . ASP A 1 187 ? 24.633 5.087 30.816 1.00 19.46 ? 187 ASP A O 1 ATOM 1383 C CB . ASP A 1 187 ? 26.358 5.202 28.286 1.00 17.05 ? 187 ASP A CB 1 ATOM 1384 C CG . ASP A 1 187 ? 26.127 6.555 27.661 1.00 17.30 ? 187 ASP A CG 1 ATOM 1385 O OD1 . ASP A 1 187 ? 25.534 7.437 28.351 1.00 16.11 ? 187 ASP A OD1 1 ATOM 1386 O OD2 . ASP A 1 187 ? 26.616 6.761 26.508 1.00 17.19 ? 187 ASP A OD2 1 ATOM 1387 N N . GLU A 1 188 ? 25.844 6.922 31.360 1.00 18.79 ? 188 GLU A N 1 ATOM 1388 C CA . GLU A 1 188 ? 24.866 7.421 32.308 1.00 19.10 ? 188 GLU A CA 1 ATOM 1389 C C . GLU A 1 188 ? 23.810 8.286 31.655 1.00 18.92 ? 188 GLU A C 1 ATOM 1390 O O . GLU A 1 188 ? 22.914 8.758 32.353 1.00 18.37 ? 188 GLU A O 1 ATOM 1391 C CB . GLU A 1 188 ? 25.556 8.206 33.460 1.00 20.06 ? 188 GLU A CB 1 ATOM 1392 C CG . GLU A 1 188 ? 26.169 9.563 33.086 1.00 20.15 ? 188 GLU A CG 1 ATOM 1393 C CD . GLU A 1 188 ? 27.572 9.506 32.488 1.00 20.53 ? 188 GLU A CD 1 ATOM 1394 O OE1 . GLU A 1 188 ? 27.747 9.017 31.360 1.00 18.80 ? 188 GLU A OE1 1 ATOM 1395 O OE2 . GLU A 1 188 ? 28.498 9.951 33.188 1.00 22.24 ? 188 GLU A OE2 1 ATOM 1396 N N . ILE A 1 189 ? 23.917 8.531 30.332 1.00 18.20 ? 189 ILE A N 1 ATOM 1397 C CA . ILE A 1 189 ? 22.955 9.375 29.581 1.00 17.80 ? 189 ILE A CA 1 ATOM 1398 C C . ILE A 1 189 ? 22.032 8.603 28.636 1.00 17.58 ? 189 ILE A C 1 ATOM 1399 O O . ILE A 1 189 ? 20.776 8.838 28.621 1.00 18.88 ? 189 ILE A O 1 ATOM 1400 C CB . ILE A 1 189 ? 23.689 10.488 28.797 1.00 17.45 ? 189 ILE A CB 1 ATOM 1401 C CG1 . ILE A 1 189 ? 24.564 11.294 29.753 1.00 18.22 ? 189 ILE A CG1 1 ATOM 1402 C CG2 . ILE A 1 189 ? 22.701 11.418 28.072 1.00 17.97 ? 189 ILE A CG2 1 ATOM 1403 C CD1 . ILE A 1 189 ? 23.874 12.001 30.934 1.00 18.30 ? 189 ILE A CD1 1 ATOM 1404 N N . VAL A 1 190 ? 22.642 7.678 27.899 1.00 16.63 ? 190 VAL A N 1 ATOM 1405 C CA . VAL A 1 190 ? 22.033 6.798 26.938 1.00 16.37 ? 190 VAL A CA 1 ATOM 1406 C C . VAL A 1 190 ? 22.034 5.396 27.420 1.00 17.27 ? 190 VAL A C 1 ATOM 1407 O O . VAL A 1 190 ? 23.131 4.783 27.586 1.00 16.62 ? 190 VAL A O 1 ATOM 1408 C CB . VAL A 1 190 ? 22.795 6.830 25.604 1.00 16.32 ? 190 VAL A CB 1 ATOM 1409 C CG1 . VAL A 1 190 ? 22.143 5.904 24.590 1.00 16.97 ? 190 VAL A CG1 1 ATOM 1410 C CG2 . VAL A 1 190 ? 22.772 8.276 25.080 1.00 16.84 ? 190 VAL A CG2 1 ATOM 1411 N N . GLN A 1 191 ? 20.805 4.882 27.612 1.00 17.21 ? 191 GLN A N 1 ATOM 1412 C CA . GLN A 1 191 ? 20.553 3.503 27.943 1.00 17.47 ? 191 GLN A CA 1 ATOM 1413 C C . GLN A 1 191 ? 19.216 3.130 27.205 1.00 17.62 ? 191 GLN A C 1 ATOM 1414 O O . GLN A 1 191 ? 18.389 4.018 26.993 1.00 17.66 ? 191 GLN A O 1 ATOM 1415 C CB . GLN A 1 191 ? 20.404 3.340 29.461 1.00 17.77 ? 191 GLN A CB 1 ATOM 1416 C CG . GLN A 1 191 ? 21.713 3.412 30.221 1.00 18.06 ? 191 GLN A CG 1 ATOM 1417 C CD . GLN A 1 191 ? 22.626 2.221 29.943 1.00 17.47 ? 191 GLN A CD 1 ATOM 1418 O OE1 . GLN A 1 191 ? 22.193 1.154 29.481 1.00 16.27 ? 191 GLN A OE1 1 ATOM 1419 N NE2 . GLN A 1 191 ? 23.886 2.435 30.139 1.00 17.59 ? 191 GLN A NE2 1 ATOM 1420 N N . PRO A 1 192 ? 19.006 1.849 26.816 1.00 16.42 ? 192 PRO A N 1 ATOM 1421 C CA . PRO A 1 192 ? 19.922 0.730 27.158 1.00 16.63 ? 192 PRO A CA 1 ATOM 1422 C C . PRO A 1 192 ? 21.145 0.594 26.196 1.00 16.38 ? 192 PRO A C 1 ATOM 1423 O O . PRO A 1 192 ? 21.004 0.672 24.955 1.00 16.26 ? 192 PRO A O 1 ATOM 1424 C CB . PRO A 1 192 ? 18.983 -0.523 27.121 1.00 17.04 ? 192 PRO A CB 1 ATOM 1425 C CG . PRO A 1 192 ? 17.972 -0.134 26.053 1.00 16.48 ? 192 PRO A CG 1 ATOM 1426 C CD . PRO A 1 192 ? 17.751 1.366 26.186 1.00 16.14 ? 192 PRO A CD 1 ATOM 1427 N N . GLN A 1 193 ? 22.311 0.297 26.777 1.00 16.74 ? 193 GLN A N 1 ATOM 1428 C CA . GLN A 1 193 ? 23.605 0.071 26.065 1.00 17.35 ? 193 GLN A CA 1 ATOM 1429 C C . GLN A 1 193 ? 24.387 -1.175 26.497 1.00 17.44 ? 193 GLN A C 1 ATOM 1430 O O . GLN A 1 193 ? 25.477 -1.396 26.031 1.00 17.16 ? 193 GLN A O 1 ATOM 1431 C CB . GLN A 1 193 ? 24.516 1.274 26.290 1.00 16.99 ? 193 GLN A CB 1 ATOM 1432 C CG . GLN A 1 193 ? 23.943 2.562 25.701 1.00 17.23 ? 193 GLN A CG 1 ATOM 1433 C CD . GLN A 1 193 ? 24.118 2.681 24.199 1.00 17.53 ? 193 GLN A CD 1 ATOM 1434 O OE1 . GLN A 1 193 ? 23.599 1.872 23.391 1.00 16.84 ? 193 GLN A OE1 1 ATOM 1435 N NE2 . GLN A 1 193 ? 24.866 3.752 23.792 1.00 17.45 ? 193 GLN A NE2 1 ATOM 1436 N N . VAL A 1 194 ? 23.795 -1.977 27.369 1.00 19.16 ? 194 VAL A N 1 ATOM 1437 C CA . VAL A 1 194 ? 24.461 -3.070 28.083 1.00 20.56 ? 194 VAL A CA 1 ATOM 1438 C C . VAL A 1 194 ? 24.464 -4.432 27.340 1.00 22.33 ? 194 VAL A C 1 ATOM 1439 O O . VAL A 1 194 ? 25.134 -5.368 27.795 1.00 23.61 ? 194 VAL A O 1 ATOM 1440 C CB . VAL A 1 194 ? 23.797 -3.293 29.495 1.00 20.68 ? 194 VAL A CB 1 ATOM 1441 C CG1 . VAL A 1 194 ? 23.969 -2.049 30.361 1.00 20.90 ? 194 VAL A CG1 1 ATOM 1442 C CG2 . VAL A 1 194 ? 22.291 -3.638 29.417 1.00 20.88 ? 194 VAL A CG2 1 ATOM 1443 N N . SER A 1 195 ? 23.732 -4.602 26.244 1.00 22.07 ? 195 SER A N 1 ATOM 1444 C CA . SER A 1 195 ? 23.541 -6.005 25.685 1.00 21.84 ? 195 SER A CA 1 ATOM 1445 C C . SER A 1 195 ? 24.628 -6.458 24.715 1.00 21.30 ? 195 SER A C 1 ATOM 1446 O O . SER A 1 195 ? 24.762 -7.673 24.433 1.00 22.17 ? 195 SER A O 1 ATOM 1447 C CB . SER A 1 195 ? 22.195 -6.094 25.017 1.00 22.16 ? 195 SER A CB 1 ATOM 1448 O OG . SER A 1 195 ? 21.288 -5.744 26.012 1.00 23.26 ? 195 SER A OG 1 ATOM 1449 N N . ASN A 1 196 ? 25.389 -5.523 24.188 1.00 19.88 ? 196 ASN A N 1 ATOM 1450 C CA . ASN A 1 196 ? 26.251 -5.793 23.065 1.00 20.02 ? 196 ASN A CA 1 ATOM 1451 C C . ASN A 1 196 ? 25.430 -6.523 21.926 1.00 20.97 ? 196 ASN A C 1 ATOM 1452 O O . ASN A 1 196 ? 25.787 -7.625 21.451 1.00 20.97 ? 196 ASN A O 1 ATOM 1453 C CB . ASN A 1 196 ? 27.520 -6.628 23.529 1.00 21.18 ? 196 ASN A CB 1 ATOM 1454 C CG . ASN A 1 196 ? 28.583 -6.810 22.406 1.00 22.07 ? 196 ASN A CG 1 ATOM 1455 O OD1 . ASN A 1 196 ? 29.157 -7.937 22.228 1.00 24.22 ? 196 ASN A OD1 1 ATOM 1456 N ND2 . ASN A 1 196 ? 28.813 -5.771 21.619 1.00 21.18 ? 196 ASN A ND2 1 ATOM 1457 N N . SER A 1 197 ? 24.330 -5.917 21.536 1.00 19.27 ? 197 SER A N 1 ATOM 1458 C CA . SER A 1 197 ? 23.338 -6.593 20.697 1.00 19.63 ? 197 SER A CA 1 ATOM 1459 C C . SER A 1 197 ? 22.437 -5.536 20.061 1.00 19.79 ? 197 SER A C 1 ATOM 1460 O O . SER A 1 197 ? 22.512 -4.351 20.428 1.00 18.58 ? 197 SER A O 1 ATOM 1461 C CB . SER A 1 197 ? 22.539 -7.599 21.507 1.00 19.64 ? 197 SER A CB 1 ATOM 1462 O OG . SER A 1 197 ? 21.358 -7.057 22.010 1.00 19.36 ? 197 SER A OG 1 ATOM 1463 N N . PRO A 1 198 ? 21.598 -5.956 19.129 1.00 19.47 ? 198 PRO A N 1 ATOM 1464 C CA . PRO A 1 198 ? 20.615 -5.049 18.586 1.00 20.44 ? 198 PRO A CA 1 ATOM 1465 C C . PRO A 1 198 ? 19.734 -4.285 19.585 1.00 19.88 ? 198 PRO A C 1 ATOM 1466 O O . PRO A 1 198 ? 19.155 -3.296 19.210 1.00 20.66 ? 198 PRO A O 1 ATOM 1467 C CB . PRO A 1 198 ? 19.697 -6.014 17.750 1.00 20.57 ? 198 PRO A CB 1 ATOM 1468 C CG . PRO A 1 198 ? 20.610 -7.099 17.313 1.00 20.95 ? 198 PRO A CG 1 ATOM 1469 C CD . PRO A 1 198 ? 21.489 -7.307 18.534 1.00 20.83 ? 198 PRO A CD 1 ATOM 1470 N N . LEU A 1 199 ? 19.620 -4.738 20.830 1.00 20.41 ? 199 LEU A N 1 ATOM 1471 C CA . LEU A 1 199 ? 18.885 -3.961 21.835 1.00 20.06 ? 199 LEU A CA 1 ATOM 1472 C C . LEU A 1 199 ? 19.535 -2.600 22.148 1.00 19.33 ? 199 LEU A C 1 ATOM 1473 O O . LEU A 1 199 ? 18.857 -1.673 22.649 1.00 18.96 ? 199 LEU A O 1 ATOM 1474 C CB . LEU A 1 199 ? 18.667 -4.744 23.104 1.00 20.17 ? 199 LEU A CB 1 ATOM 1475 C CG . LEU A 1 199 ? 17.895 -6.071 22.920 1.00 21.59 ? 199 LEU A CG 1 ATOM 1476 C CD1 . LEU A 1 199 ? 17.804 -6.843 24.230 1.00 22.25 ? 199 LEU A CD1 1 ATOM 1477 C CD2 . LEU A 1 199 ? 16.518 -5.856 22.349 1.00 22.02 ? 199 LEU A CD2 1 ATOM 1478 N N . ASP A 1 200 ? 20.826 -2.448 21.887 1.00 18.55 ? 200 ASP A N 1 ATOM 1479 C CA . ASP A 1 200 ? 21.492 -1.255 22.352 1.00 17.65 ? 200 ASP A CA 1 ATOM 1480 C C . ASP A 1 200 ? 21.095 -0.053 21.511 1.00 17.13 ? 200 ASP A C 1 ATOM 1481 O O . ASP A 1 200 ? 20.916 -0.149 20.306 1.00 16.08 ? 200 ASP A O 1 ATOM 1482 C CB . ASP A 1 200 ? 22.990 -1.408 22.343 1.00 18.26 ? 200 ASP A CB 1 ATOM 1483 C CG . ASP A 1 200 ? 23.487 -2.564 23.258 1.00 18.61 ? 200 ASP A CG 1 ATOM 1484 O OD1 . ASP A 1 200 ? 22.843 -2.804 24.300 1.00 18.72 ? 200 ASP A OD1 1 ATOM 1485 O OD2 . ASP A 1 200 ? 24.515 -3.178 22.895 1.00 18.54 ? 200 ASP A OD2 1 ATOM 1486 N N . SER A 1 201 ? 21.042 1.110 22.144 1.00 16.65 ? 201 SER A N 1 ATOM 1487 C CA . SER A 1 201 ? 20.575 2.269 21.479 1.00 16.27 ? 201 SER A CA 1 ATOM 1488 C C . SER A 1 201 ? 21.504 2.710 20.340 1.00 15.68 ? 201 SER A C 1 ATOM 1489 O O . SER A 1 201 ? 21.018 3.189 19.307 1.00 15.41 ? 201 SER A O 1 ATOM 1490 C CB . SER A 1 201 ? 20.258 3.388 22.486 1.00 16.15 ? 201 SER A CB 1 ATOM 1491 O OG . SER A 1 201 ? 19.720 4.523 21.759 1.00 15.56 ? 201 SER A OG 1 ATOM 1492 N N . SER A 1 202 ? 22.810 2.439 20.478 1.00 15.81 ? 202 SER A N 1 ATOM 1493 C CA . SER A 1 202 ? 23.836 2.772 19.475 1.00 15.95 ? 202 SER A CA 1 ATOM 1494 C C . SER A 1 202 ? 23.950 1.770 18.351 1.00 17.48 ? 202 SER A C 1 ATOM 1495 O O . SER A 1 202 ? 24.721 1.991 17.411 1.00 18.10 ? 202 SER A O 1 ATOM 1496 C CB . SER A 1 202 ? 25.248 2.963 20.179 1.00 16.01 ? 202 SER A CB 1 ATOM 1497 O OG . SER A 1 202 ? 25.249 4.139 21.048 1.00 14.87 ? 202 SER A OG 1 ATOM 1498 N N . TYR A 1 203 ? 23.219 0.641 18.400 1.00 18.68 ? 203 TYR A N 1 ATOM 1499 C CA . TYR A 1 203 ? 23.383 -0.400 17.368 1.00 18.81 ? 203 TYR A CA 1 ATOM 1500 C C . TYR A 1 203 ? 22.616 -0.088 16.092 1.00 19.16 ? 203 TYR A C 1 ATOM 1501 O O . TYR A 1 203 ? 21.415 0.210 16.115 1.00 19.87 ? 203 TYR A O 1 ATOM 1502 C CB . TYR A 1 203 ? 22.903 -1.751 17.929 1.00 20.30 ? 203 TYR A CB 1 ATOM 1503 C CG . TYR A 1 203 ? 23.223 -3.012 17.147 1.00 20.61 ? 203 TYR A CG 1 ATOM 1504 C CD1 . TYR A 1 203 ? 22.485 -3.379 16.035 1.00 21.24 ? 203 TYR A CD1 1 ATOM 1505 C CD2 . TYR A 1 203 ? 24.220 -3.844 17.574 1.00 22.55 ? 203 TYR A CD2 1 ATOM 1506 C CE1 . TYR A 1 203 ? 22.755 -4.574 15.345 1.00 23.40 ? 203 TYR A CE1 1 ATOM 1507 C CE2 . TYR A 1 203 ? 24.522 -5.023 16.901 1.00 24.28 ? 203 TYR A CE2 1 ATOM 1508 C CZ . TYR A 1 203 ? 23.749 -5.389 15.807 1.00 24.64 ? 203 TYR A CZ 1 ATOM 1509 O OH . TYR A 1 203 ? 24.075 -6.545 15.160 1.00 28.82 ? 203 TYR A OH 1 ATOM 1510 N N . LEU A 1 204 ? 23.292 -0.265 14.967 1.00 19.62 ? 204 LEU A N 1 ATOM 1511 C CA . LEU A 1 204 ? 22.632 -0.326 13.636 1.00 18.95 ? 204 LEU A CA 1 ATOM 1512 C C . LEU A 1 204 ? 22.940 -1.671 12.985 1.00 19.50 ? 204 LEU A C 1 ATOM 1513 O O . LEU A 1 204 ? 24.092 -2.185 13.054 1.00 18.23 ? 204 LEU A O 1 ATOM 1514 C CB . LEU A 1 204 ? 23.159 0.771 12.736 1.00 19.40 ? 204 LEU A CB 1 ATOM 1515 C CG . LEU A 1 204 ? 22.872 2.225 13.174 1.00 19.69 ? 204 LEU A CG 1 ATOM 1516 C CD1 . LEU A 1 204 ? 23.534 3.151 12.182 1.00 20.45 ? 204 LEU A CD1 1 ATOM 1517 C CD2 . LEU A 1 204 ? 21.373 2.552 13.187 1.00 18.98 ? 204 LEU A CD2 1 ATOM 1518 N N . PHE A 1 205 ? 21.917 -2.229 12.319 1.00 19.76 ? 205 PHE A N 1 ATOM 1519 C CA . PHE A 1 205 ? 22.085 -3.486 11.582 1.00 20.32 ? 205 PHE A CA 1 ATOM 1520 C C . PHE A 1 205 ? 23.023 -3.229 10.403 1.00 21.72 ? 205 PHE A C 1 ATOM 1521 O O . PHE A 1 205 ? 22.912 -2.199 9.687 1.00 21.20 ? 205 PHE A O 1 ATOM 1522 C CB . PHE A 1 205 ? 20.765 -4.038 11.104 1.00 20.47 ? 205 PHE A CB 1 ATOM 1523 C CG . PHE A 1 205 ? 19.837 -4.459 12.218 1.00 21.44 ? 205 PHE A CG 1 ATOM 1524 C CD1 . PHE A 1 205 ? 20.045 -5.650 12.950 1.00 21.76 ? 205 PHE A CD1 1 ATOM 1525 C CD2 . PHE A 1 205 ? 18.703 -3.723 12.493 1.00 21.92 ? 205 PHE A CD2 1 ATOM 1526 C CE1 . PHE A 1 205 ? 19.116 -6.041 13.945 1.00 21.59 ? 205 PHE A CE1 1 ATOM 1527 C CE2 . PHE A 1 205 ? 17.812 -4.088 13.492 1.00 21.95 ? 205 PHE A CE2 1 ATOM 1528 C CZ . PHE A 1 205 ? 18.037 -5.254 14.225 1.00 22.07 ? 205 PHE A CZ 1 ATOM 1529 N N . ASN A 1 206 ? 24.012 -4.137 10.282 1.00 22.91 ? 206 ASN A N 1 ATOM 1530 C CA . ASN A 1 206 ? 25.135 -4.091 9.306 1.00 22.91 ? 206 ASN A CA 1 ATOM 1531 C C . ASN A 1 206 ? 26.213 -3.059 9.601 1.00 22.04 ? 206 ASN A C 1 ATOM 1532 O O . ASN A 1 206 ? 27.203 -2.953 8.836 1.00 20.08 ? 206 ASN A O 1 ATOM 1533 C CB . ASN A 1 206 ? 24.647 -3.900 7.861 1.00 25.09 ? 206 ASN A CB 1 ATOM 1534 C CG . ASN A 1 206 ? 23.644 -4.957 7.403 1.00 26.39 ? 206 ASN A CG 1 ATOM 1535 O OD1 . ASN A 1 206 ? 23.828 -6.107 7.605 1.00 29.10 ? 206 ASN A OD1 1 ATOM 1536 N ND2 . ASN A 1 206 ? 22.544 -4.527 6.823 1.00 29.47 ? 206 ASN A ND2 1 ATOM 1537 N N . GLY A 1 207 ? 26.083 -2.301 10.698 1.00 20.08 ? 207 GLY A N 1 ATOM 1538 C CA . GLY A 1 207 ? 27.133 -1.411 11.136 1.00 19.85 ? 207 GLY A CA 1 ATOM 1539 C C . GLY A 1 207 ? 28.229 -2.176 11.866 1.00 19.95 ? 207 GLY A C 1 ATOM 1540 O O . GLY A 1 207 ? 28.103 -3.397 12.252 1.00 19.92 ? 207 GLY A O 1 ATOM 1541 N N . LYS A 1 208 ? 29.311 -1.460 12.034 1.00 20.28 ? 208 LYS A N 1 ATOM 1542 C CA . LYS A 1 208 ? 30.424 -1.894 12.901 1.00 20.61 ? 208 LYS A CA 1 ATOM 1543 C C . LYS A 1 208 ? 30.125 -1.376 14.290 1.00 19.71 ? 208 LYS A C 1 ATOM 1544 O O . LYS A 1 208 ? 30.366 -0.217 14.602 1.00 19.33 ? 208 LYS A O 1 ATOM 1545 C CB . LYS A 1 208 ? 31.735 -1.365 12.354 1.00 21.80 ? 208 LYS A CB 1 ATOM 1546 C CG . LYS A 1 208 ? 32.977 -1.809 13.115 1.00 23.28 ? 208 LYS A CG 1 ATOM 1547 C CD . LYS A 1 208 ? 33.150 -3.302 13.050 1.00 25.30 ? 208 LYS A CD 1 ATOM 1548 C CE . LYS A 1 208 ? 34.526 -3.641 13.642 1.00 27.60 ? 208 LYS A CE 1 ATOM 1549 N NZ . LYS A 1 208 ? 34.566 -5.025 14.151 1.00 29.07 ? 208 LYS A NZ 1 ATOM 1550 N N . ASN A 1 209 ? 29.523 -2.220 15.107 1.00 19.01 ? 209 ASN A N 1 ATOM 1551 C CA . ASN A 1 209 ? 29.028 -1.832 16.393 1.00 20.23 ? 209 ASN A CA 1 ATOM 1552 C C . ASN A 1 209 ? 30.048 -2.289 17.401 1.00 20.33 ? 209 ASN A C 1 ATOM 1553 O O . ASN A 1 209 ? 30.248 -3.513 17.592 1.00 22.57 ? 209 ASN A O 1 ATOM 1554 C CB . ASN A 1 209 ? 27.623 -2.427 16.660 1.00 20.17 ? 209 ASN A CB 1 ATOM 1555 C CG . ASN A 1 209 ? 26.599 -2.019 15.593 1.00 20.55 ? 209 ASN A CG 1 ATOM 1556 O OD1 . ASN A 1 209 ? 26.307 -0.840 15.438 1.00 20.69 ? 209 ASN A OD1 1 ATOM 1557 N ND2 . ASN A 1 209 ? 26.029 -3.006 14.875 1.00 21.22 ? 209 ASN A ND2 1 ATOM 1558 N N . VAL A 1 210 ? 30.674 -1.309 18.029 1.00 19.13 ? 210 VAL A N 1 ATOM 1559 C CA . VAL A 1 210 ? 31.720 -1.511 18.947 1.00 20.05 ? 210 VAL A CA 1 ATOM 1560 C C . VAL A 1 210 ? 31.300 -0.981 20.337 1.00 20.86 ? 210 VAL A C 1 ATOM 1561 O O . VAL A 1 210 ? 31.459 0.210 20.637 1.00 20.03 ? 210 VAL A O 1 ATOM 1562 C CB . VAL A 1 210 ? 33.007 -0.798 18.523 1.00 19.96 ? 210 VAL A CB 1 ATOM 1563 C CG1 . VAL A 1 210 ? 34.108 -1.241 19.446 1.00 19.86 ? 210 VAL A CG1 1 ATOM 1564 C CG2 . VAL A 1 210 ? 33.330 -1.073 17.057 1.00 20.49 ? 210 VAL A CG2 1 ATOM 1565 N N . GLN A 1 211 ? 30.727 -1.890 21.146 1.00 21.46 ? 211 GLN A N 1 ATOM 1566 C CA . GLN A 1 211 ? 30.639 -1.698 22.590 1.00 22.16 ? 211 GLN A CA 1 ATOM 1567 C C . GLN A 1 211 ? 32.029 -1.943 23.221 1.00 21.56 ? 211 GLN A C 1 ATOM 1568 O O . GLN A 1 211 ? 32.652 -3.018 23.033 1.00 21.13 ? 211 GLN A O 1 ATOM 1569 C CB . GLN A 1 211 ? 29.645 -2.668 23.188 1.00 22.81 ? 211 GLN A CB 1 ATOM 1570 C CG . GLN A 1 211 ? 29.195 -2.255 24.558 1.00 22.10 ? 211 GLN A CG 1 ATOM 1571 C CD . GLN A 1 211 ? 28.797 -3.505 25.353 1.00 24.22 ? 211 GLN A CD 1 ATOM 1572 O OE1 . GLN A 1 211 ? 29.563 -4.483 25.421 1.00 22.27 ? 211 GLN A OE1 1 ATOM 1573 N NE2 . GLN A 1 211 ? 27.586 -3.492 25.915 1.00 23.48 ? 211 GLN A NE2 1 ATOM 1574 N N . ALA A 1 212 ? 32.503 -0.934 23.929 1.00 21.44 ? 212 ALA A N 1 ATOM 1575 C CA . ALA A 1 212 ? 33.887 -0.887 24.364 1.00 21.52 ? 212 ALA A CA 1 ATOM 1576 C C . ALA A 1 212 ? 34.226 -2.084 25.264 1.00 21.61 ? 212 ALA A C 1 ATOM 1577 O O . ALA A 1 212 ? 35.320 -2.629 25.108 1.00 23.07 ? 212 ALA A O 1 ATOM 1578 C CB . ALA A 1 212 ? 34.142 0.400 25.081 1.00 21.88 ? 212 ALA A CB 1 ATOM 1579 N N . GLN A 1 213 ? 33.278 -2.528 26.083 1.00 20.62 ? 213 GLN A N 1 ATOM 1580 C CA . GLN A 1 213 ? 33.448 -3.655 27.017 1.00 21.55 ? 213 GLN A CA 1 ATOM 1581 C C . GLN A 1 213 ? 33.541 -5.002 26.285 1.00 23.41 ? 213 GLN A C 1 ATOM 1582 O O . GLN A 1 213 ? 34.165 -5.951 26.836 1.00 23.23 ? 213 GLN A O 1 ATOM 1583 C CB . GLN A 1 213 ? 32.302 -3.768 28.008 1.00 20.67 ? 213 GLN A CB 1 ATOM 1584 C CG . GLN A 1 213 ? 32.188 -2.615 29.026 1.00 20.58 ? 213 GLN A CG 1 ATOM 1585 C CD . GLN A 1 213 ? 31.712 -1.297 28.417 1.00 20.14 ? 213 GLN A CD 1 ATOM 1586 O OE1 . GLN A 1 213 ? 31.025 -1.265 27.377 1.00 18.62 ? 213 GLN A OE1 1 ATOM 1587 N NE2 . GLN A 1 213 ? 32.131 -0.179 29.029 1.00 20.76 ? 213 GLN A NE2 1 ATOM 1588 N N . ALA A 1 214 ? 32.896 -5.102 25.111 1.00 23.15 ? 214 ALA A N 1 ATOM 1589 C CA . ALA A 1 214 ? 33.025 -6.292 24.256 1.00 24.79 ? 214 ALA A CA 1 ATOM 1590 C C . ALA A 1 214 ? 34.464 -6.466 23.779 1.00 26.00 ? 214 ALA A C 1 ATOM 1591 O O . ALA A 1 214 ? 34.887 -7.594 23.560 1.00 26.41 ? 214 ALA A O 1 ATOM 1592 C CB . ALA A 1 214 ? 32.115 -6.189 23.057 1.00 24.50 ? 214 ALA A CB 1 ATOM 1593 N N . VAL A 1 215 ? 35.222 -5.368 23.613 1.00 25.32 ? 215 VAL A N 1 ATOM 1594 C CA . VAL A 1 215 ? 36.641 -5.411 23.226 1.00 26.10 ? 215 VAL A CA 1 ATOM 1595 C C . VAL A 1 215 ? 37.548 -5.309 24.465 1.00 26.36 ? 215 VAL A C 1 ATOM 1596 O O . VAL A 1 215 ? 38.605 -5.946 24.505 1.00 26.69 ? 215 VAL A O 1 ATOM 1597 C CB . VAL A 1 215 ? 36.982 -4.213 22.238 1.00 26.61 ? 215 VAL A CB 1 ATOM 1598 C CG1 . VAL A 1 215 ? 38.463 -4.102 21.939 1.00 27.51 ? 215 VAL A CG1 1 ATOM 1599 C CG2 . VAL A 1 215 ? 36.140 -4.293 20.959 1.00 26.55 ? 215 VAL A CG2 1 ATOM 1600 N N . CYS A 1 216 ? 37.160 -4.532 25.490 1.00 25.38 ? 216 CYS A N 1 ATOM 1601 C CA . CYS A 1 216 ? 38.096 -4.205 26.579 1.00 26.57 ? 216 CYS A CA 1 ATOM 1602 C C . CYS A 1 216 ? 37.829 -4.949 27.880 1.00 28.68 ? 216 CYS A C 1 ATOM 1603 O O . CYS A 1 216 ? 38.644 -4.904 28.844 1.00 31.55 ? 216 CYS A O 1 ATOM 1604 C CB . CYS A 1 216 ? 38.136 -2.692 26.830 1.00 25.99 ? 216 CYS A CB 1 ATOM 1605 S SG . CYS A 1 216 ? 38.753 -1.760 25.422 1.00 25.89 ? 216 CYS A SG 1 ATOM 1606 N N . GLY A 1 217 ? 36.702 -5.632 27.929 1.00 27.61 ? 217 GLY A N 1 ATOM 1607 C CA . GLY A 1 217 ? 36.361 -6.482 29.050 1.00 27.64 ? 217 GLY A CA 1 ATOM 1608 C C . GLY A 1 217 ? 35.335 -5.757 29.872 1.00 27.97 ? 217 GLY A C 1 ATOM 1609 O O . GLY A 1 217 ? 35.129 -4.523 29.701 1.00 25.57 ? 217 GLY A O 1 ATOM 1610 N N . PRO A 1 218 ? 34.677 -6.522 30.751 1.00 29.55 ? 218 PRO A N 1 ATOM 1611 C CA . PRO A 1 218 ? 33.516 -6.039 31.473 1.00 31.34 ? 218 PRO A CA 1 ATOM 1612 C C . PRO A 1 218 ? 33.860 -5.037 32.538 1.00 30.34 ? 218 PRO A C 1 ATOM 1613 O O . PRO A 1 218 ? 32.975 -4.388 33.011 1.00 30.92 ? 218 PRO A O 1 ATOM 1614 C CB . PRO A 1 218 ? 32.923 -7.326 32.106 1.00 32.78 ? 218 PRO A CB 1 ATOM 1615 C CG . PRO A 1 218 ? 34.072 -8.317 32.135 1.00 32.30 ? 218 PRO A CG 1 ATOM 1616 C CD . PRO A 1 218 ? 34.883 -7.984 30.932 1.00 32.14 ? 218 PRO A CD 1 ATOM 1617 N N . LEU A 1 219 ? 35.108 -4.886 32.945 1.00 31.03 ? 219 LEU A N 1 ATOM 1618 C CA . LEU A 1 219 ? 35.431 -3.804 33.895 1.00 31.69 ? 219 LEU A CA 1 ATOM 1619 C C . LEU A 1 219 ? 35.963 -2.544 33.243 1.00 29.53 ? 219 LEU A C 1 ATOM 1620 O O . LEU A 1 219 ? 36.469 -1.656 33.938 1.00 29.46 ? 219 LEU A O 1 ATOM 1621 C CB . LEU A 1 219 ? 36.472 -4.265 34.889 1.00 35.42 ? 219 LEU A CB 1 ATOM 1622 C CG . LEU A 1 219 ? 36.163 -5.608 35.565 1.00 37.03 ? 219 LEU A CG 1 ATOM 1623 C CD1 . LEU A 1 219 ? 37.438 -5.990 36.313 1.00 39.26 ? 219 LEU A CD1 1 ATOM 1624 C CD2 . LEU A 1 219 ? 34.895 -5.512 36.432 1.00 37.05 ? 219 LEU A CD2 1 ATOM 1625 N N . PHE A 1 220 ? 35.928 -2.464 31.922 1.00 26.52 ? 220 PHE A N 1 ATOM 1626 C CA . PHE A 1 220 ? 36.364 -1.213 31.267 1.00 25.72 ? 220 PHE A CA 1 ATOM 1627 C C . PHE A 1 220 ? 35.225 -0.201 31.391 1.00 25.17 ? 220 PHE A C 1 ATOM 1628 O O . PHE A 1 220 ? 34.028 -0.510 31.175 1.00 23.86 ? 220 PHE A O 1 ATOM 1629 C CB . PHE A 1 220 ? 36.698 -1.501 29.806 1.00 25.58 ? 220 PHE A CB 1 ATOM 1630 C CG . PHE A 1 220 ? 37.258 -0.348 29.061 1.00 24.99 ? 220 PHE A CG 1 ATOM 1631 C CD1 . PHE A 1 220 ? 38.552 0.061 29.272 1.00 25.09 ? 220 PHE A CD1 1 ATOM 1632 C CD2 . PHE A 1 220 ? 36.507 0.299 28.097 1.00 23.93 ? 220 PHE A CD2 1 ATOM 1633 C CE1 . PHE A 1 220 ? 39.099 1.130 28.564 1.00 24.54 ? 220 PHE A CE1 1 ATOM 1634 C CE2 . PHE A 1 220 ? 37.070 1.352 27.377 1.00 24.97 ? 220 PHE A CE2 1 ATOM 1635 C CZ . PHE A 1 220 ? 38.362 1.775 27.623 1.00 23.90 ? 220 PHE A CZ 1 ATOM 1636 N N . VAL A 1 221 ? 35.599 1.036 31.738 1.00 25.61 ? 221 VAL A N 1 ATOM 1637 C CA . VAL A 1 221 ? 34.627 2.057 31.966 1.00 24.42 ? 221 VAL A CA 1 ATOM 1638 C C . VAL A 1 221 ? 35.054 3.302 31.220 1.00 23.72 ? 221 VAL A C 1 ATOM 1639 O O . VAL A 1 221 ? 36.156 3.861 31.434 1.00 22.80 ? 221 VAL A O 1 ATOM 1640 C CB . VAL A 1 221 ? 34.480 2.377 33.445 1.00 24.75 ? 221 VAL A CB 1 ATOM 1641 C CG1 . VAL A 1 221 ? 33.544 3.580 33.620 1.00 24.11 ? 221 VAL A CG1 1 ATOM 1642 C CG2 . VAL A 1 221 ? 34.017 1.132 34.225 1.00 26.05 ? 221 VAL A CG2 1 ATOM 1643 N N . ILE A 1 222 ? 34.191 3.681 30.304 1.00 21.44 ? 222 ILE A N 1 ATOM 1644 C CA . ILE A 1 222 ? 34.149 5.042 29.757 1.00 21.29 ? 222 ILE A CA 1 ATOM 1645 C C . ILE A 1 222 ? 32.671 5.448 29.775 1.00 20.69 ? 222 ILE A C 1 ATOM 1646 O O . ILE A 1 222 ? 31.750 4.609 29.497 1.00 20.50 ? 222 ILE A O 1 ATOM 1647 C CB . ILE A 1 222 ? 34.772 5.136 28.378 1.00 20.60 ? 222 ILE A CB 1 ATOM 1648 C CG1 . ILE A 1 222 ? 34.038 4.220 27.411 1.00 21.89 ? 222 ILE A CG1 1 ATOM 1649 C CG2 . ILE A 1 222 ? 36.277 4.753 28.428 1.00 20.34 ? 222 ILE A CG2 1 ATOM 1650 C CD1 . ILE A 1 222 ? 34.536 4.307 26.002 1.00 22.36 ? 222 ILE A CD1 1 ATOM 1651 N N . ASP A 1 223 ? 32.412 6.719 30.124 1.00 19.01 ? 223 ASP A N 1 ATOM 1652 C CA . ASP A 1 223 ? 31.030 7.125 30.305 1.00 18.41 ? 223 ASP A CA 1 ATOM 1653 C C . ASP A 1 223 ? 30.488 7.725 28.987 1.00 18.10 ? 223 ASP A C 1 ATOM 1654 O O . ASP A 1 223 ? 31.076 7.511 27.907 1.00 18.46 ? 223 ASP A O 1 ATOM 1655 C CB . ASP A 1 223 ? 30.856 7.988 31.617 1.00 17.71 ? 223 ASP A CB 1 ATOM 1656 C CG . ASP A 1 223 ? 31.163 9.521 31.432 1.00 17.51 ? 223 ASP A CG 1 ATOM 1657 O OD1 . ASP A 1 223 ? 31.998 9.868 30.566 1.00 18.30 ? 223 ASP A OD1 1 ATOM 1658 O OD2 . ASP A 1 223 ? 30.642 10.361 32.215 1.00 17.14 ? 223 ASP A OD2 1 ATOM 1659 N N . HIS A 1 224 ? 29.423 8.510 29.077 1.00 17.16 ? 224 HIS A N 1 ATOM 1660 C CA . HIS A 1 224 ? 28.866 9.125 27.891 1.00 17.90 ? 224 HIS A CA 1 ATOM 1661 C C . HIS A 1 224 ? 29.878 10.035 27.179 1.00 17.96 ? 224 HIS A C 1 ATOM 1662 O O . HIS A 1 224 ? 29.898 10.078 25.956 1.00 18.72 ? 224 HIS A O 1 ATOM 1663 C CB . HIS A 1 224 ? 27.610 9.915 28.263 1.00 18.53 ? 224 HIS A CB 1 ATOM 1664 C CG . HIS A 1 224 ? 26.824 10.381 27.071 1.00 18.70 ? 224 HIS A CG 1 ATOM 1665 N ND1 . HIS A 1 224 ? 26.299 9.516 26.122 1.00 18.75 ? 224 HIS A ND1 1 ATOM 1666 C CD2 . HIS A 1 224 ? 26.450 11.616 26.691 1.00 19.16 ? 224 HIS A CD2 1 ATOM 1667 C CE1 . HIS A 1 224 ? 25.686 10.214 25.188 1.00 19.16 ? 224 HIS A CE1 1 ATOM 1668 N NE2 . HIS A 1 224 ? 25.772 11.494 25.503 1.00 18.89 ? 224 HIS A NE2 1 ATOM 1669 N N . ALA A 1 225 ? 30.630 10.824 27.961 1.00 17.51 ? 225 ALA A N 1 ATOM 1670 C CA . ALA A 1 225 ? 31.668 11.760 27.381 1.00 17.26 ? 225 ALA A CA 1 ATOM 1671 C C . ALA A 1 225 ? 32.914 10.998 26.982 1.00 16.66 ? 225 ALA A C 1 ATOM 1672 O O . ALA A 1 225 ? 33.452 11.241 25.891 1.00 15.45 ? 225 ALA A O 1 ATOM 1673 C CB . ALA A 1 225 ? 31.978 12.875 28.335 1.00 17.95 ? 225 ALA A CB 1 ATOM 1674 N N . GLY A 1 226 ? 33.346 10.053 27.824 1.00 16.04 ? 226 GLY A N 1 ATOM 1675 C CA . GLY A 1 226 ? 34.520 9.268 27.491 1.00 16.97 ? 226 GLY A CA 1 ATOM 1676 C C . GLY A 1 226 ? 34.425 8.409 26.215 1.00 16.40 ? 226 GLY A C 1 ATOM 1677 O O . GLY A 1 226 ? 35.446 8.130 25.590 1.00 17.30 ? 226 GLY A O 1 ATOM 1678 N N . SER A 1 227 ? 33.191 8.027 25.874 1.00 16.96 ? 227 SER A N 1 ATOM 1679 C CA . SER A 1 227 ? 32.780 7.378 24.602 1.00 17.11 ? 227 SER A CA 1 ATOM 1680 C C . SER A 1 227 ? 33.265 8.179 23.383 1.00 17.41 ? 227 SER A C 1 ATOM 1681 O O . SER A 1 227 ? 33.730 7.604 22.329 1.00 17.26 ? 227 SER A O 1 ATOM 1682 C CB . SER A 1 227 ? 31.260 7.205 24.593 1.00 17.28 ? 227 SER A CB 1 ATOM 1683 O OG . SER A 1 227 ? 30.782 6.143 25.498 1.00 17.68 ? 227 SER A OG 1 ATOM 1684 N N . LEU A 1 228 ? 33.218 9.508 23.532 1.00 16.70 ? 228 LEU A N 1 ATOM 1685 C CA . LEU A 1 228 ? 33.692 10.436 22.492 1.00 16.77 ? 228 LEU A CA 1 ATOM 1686 C C . LEU A 1 228 ? 35.200 10.645 22.579 1.00 17.07 ? 228 LEU A C 1 ATOM 1687 O O . LEU A 1 228 ? 35.866 10.715 21.536 1.00 17.75 ? 228 LEU A O 1 ATOM 1688 C CB . LEU A 1 228 ? 32.987 11.798 22.633 1.00 16.97 ? 228 LEU A CB 1 ATOM 1689 C CG . LEU A 1 228 ? 33.311 12.932 21.634 1.00 16.34 ? 228 LEU A CG 1 ATOM 1690 C CD1 . LEU A 1 228 ? 33.042 12.437 20.246 1.00 16.33 ? 228 LEU A CD1 1 ATOM 1691 C CD2 . LEU A 1 228 ? 32.466 14.137 21.943 1.00 16.89 ? 228 LEU A CD2 1 ATOM 1692 N N . THR A 1 229 ? 35.688 10.804 23.818 1.00 17.20 ? 229 THR A N 1 ATOM 1693 C CA . THR A 1 229 ? 36.986 11.456 24.079 1.00 17.78 ? 229 THR A CA 1 ATOM 1694 C C . THR A 1 229 ? 38.197 10.531 24.387 1.00 18.45 ? 229 THR A C 1 ATOM 1695 O O . THR A 1 229 ? 39.363 10.973 24.285 1.00 18.88 ? 229 THR A O 1 ATOM 1696 C CB . THR A 1 229 ? 36.905 12.482 25.220 1.00 17.21 ? 229 THR A CB 1 ATOM 1697 O OG1 . THR A 1 229 ? 36.769 11.821 26.481 1.00 17.12 ? 229 THR A OG1 1 ATOM 1698 C CG2 . THR A 1 229 ? 35.827 13.521 25.009 1.00 17.38 ? 229 THR A CG2 1 ATOM 1699 N N . SER A 1 230 ? 37.931 9.275 24.781 1.00 19.11 ? 230 SER A N 1 ATOM 1700 C CA . SER A 1 230 ? 38.997 8.393 25.204 1.00 18.71 ? 230 SER A CA 1 ATOM 1701 C C . SER A 1 230 ? 40.038 8.054 24.134 1.00 19.14 ? 230 SER A C 1 ATOM 1702 O O . SER A 1 230 ? 39.759 8.088 22.932 1.00 18.78 ? 230 SER A O 1 ATOM 1703 C CB . SER A 1 230 ? 38.436 7.064 25.755 1.00 18.64 ? 230 SER A CB 1 ATOM 1704 O OG . SER A 1 230 ? 37.961 6.189 24.750 1.00 19.19 ? 230 SER A OG 1 ATOM 1705 N N . GLN A 1 231 ? 41.194 7.589 24.596 1.00 19.98 ? 231 GLN A N 1 ATOM 1706 C CA . GLN A 1 231 ? 42.223 7.006 23.669 1.00 21.78 ? 231 GLN A CA 1 ATOM 1707 C C . GLN A 1 231 ? 41.659 5.792 22.883 1.00 20.22 ? 231 GLN A C 1 ATOM 1708 O O . GLN A 1 231 ? 41.861 5.750 21.703 1.00 22.04 ? 231 GLN A O 1 ATOM 1709 C CB . GLN A 1 231 ? 43.526 6.643 24.413 1.00 21.67 ? 231 GLN A CB 1 ATOM 1710 C CG . GLN A 1 231 ? 44.554 5.950 23.555 1.00 22.68 ? 231 GLN A CG 1 ATOM 1711 C CD . GLN A 1 231 ? 45.098 6.804 22.465 1.00 23.62 ? 231 GLN A CD 1 ATOM 1712 O OE1 . GLN A 1 231 ? 45.008 8.039 22.505 1.00 24.43 ? 231 GLN A OE1 1 ATOM 1713 N NE2 . GLN A 1 231 ? 45.664 6.147 21.436 1.00 23.83 ? 231 GLN A NE2 1 ATOM 1714 N N . PHE A 1 232 ? 40.941 4.867 23.516 1.00 19.83 ? 232 PHE A N 1 ATOM 1715 C CA . PHE A 1 232 ? 40.314 3.739 22.832 1.00 19.71 ? 232 PHE A CA 1 ATOM 1716 C C . PHE A 1 232 ? 39.367 4.252 21.773 1.00 19.52 ? 232 PHE A C 1 ATOM 1717 O O . PHE A 1 232 ? 39.360 3.771 20.622 1.00 19.61 ? 232 PHE A O 1 ATOM 1718 C CB . PHE A 1 232 ? 39.520 2.865 23.799 1.00 20.96 ? 232 PHE A CB 1 ATOM 1719 C CG . PHE A 1 232 ? 38.781 1.716 23.129 1.00 21.24 ? 232 PHE A CG 1 ATOM 1720 C CD1 . PHE A 1 232 ? 39.482 0.648 22.584 1.00 21.61 ? 232 PHE A CD1 1 ATOM 1721 C CD2 . PHE A 1 232 ? 37.386 1.695 23.086 1.00 21.97 ? 232 PHE A CD2 1 ATOM 1722 C CE1 . PHE A 1 232 ? 38.784 -0.386 21.932 1.00 22.57 ? 232 PHE A CE1 1 ATOM 1723 C CE2 . PHE A 1 232 ? 36.684 0.661 22.471 1.00 21.82 ? 232 PHE A CE2 1 ATOM 1724 C CZ . PHE A 1 232 ? 37.389 -0.385 21.898 1.00 23.03 ? 232 PHE A CZ 1 ATOM 1725 N N . SER A 1 233 ? 38.586 5.267 22.124 1.00 18.95 ? 233 SER A N 1 ATOM 1726 C CA . SER A 1 233 ? 37.654 5.872 21.129 1.00 18.79 ? 233 SER A CA 1 ATOM 1727 C C . SER A 1 233 ? 38.360 6.496 19.923 1.00 19.14 ? 233 SER A C 1 ATOM 1728 O O . SER A 1 233 ? 37.914 6.360 18.791 1.00 18.96 ? 233 SER A O 1 ATOM 1729 C CB . SER A 1 233 ? 36.809 6.922 21.827 1.00 18.53 ? 233 SER A CB 1 ATOM 1730 O OG . SER A 1 233 ? 36.143 6.325 22.920 1.00 16.89 ? 233 SER A OG 1 ATOM 1731 N N . TYR A 1 234 ? 39.478 7.158 20.183 1.00 19.78 ? 234 TYR A N 1 ATOM 1732 C CA . TYR A 1 234 ? 40.309 7.740 19.134 1.00 19.31 ? 234 TYR A CA 1 ATOM 1733 C C . TYR A 1 234 ? 40.854 6.657 18.164 1.00 20.07 ? 234 TYR A C 1 ATOM 1734 O O . TYR A 1 234 ? 40.840 6.839 16.946 1.00 20.83 ? 234 TYR A O 1 ATOM 1735 C CB . TYR A 1 234 ? 41.440 8.518 19.763 1.00 20.14 ? 234 TYR A CB 1 ATOM 1736 C CG . TYR A 1 234 ? 42.458 8.903 18.723 1.00 22.11 ? 234 TYR A CG 1 ATOM 1737 C CD1 . TYR A 1 234 ? 42.194 9.949 17.836 1.00 22.61 ? 234 TYR A CD1 1 ATOM 1738 C CD2 . TYR A 1 234 ? 43.635 8.211 18.574 1.00 23.32 ? 234 TYR A CD2 1 ATOM 1739 C CE1 . TYR A 1 234 ? 43.087 10.289 16.822 1.00 24.17 ? 234 TYR A CE1 1 ATOM 1740 C CE2 . TYR A 1 234 ? 44.538 8.558 17.582 1.00 24.71 ? 234 TYR A CE2 1 ATOM 1741 C CZ . TYR A 1 234 ? 44.235 9.604 16.712 1.00 25.13 ? 234 TYR A CZ 1 ATOM 1742 O OH . TYR A 1 234 ? 45.125 9.995 15.759 1.00 29.14 ? 234 TYR A OH 1 ATOM 1743 N N . VAL A 1 235 ? 41.314 5.534 18.704 1.00 19.50 ? 235 VAL A N 1 ATOM 1744 C CA . VAL A 1 235 ? 41.898 4.474 17.914 1.00 19.97 ? 235 VAL A CA 1 ATOM 1745 C C . VAL A 1 235 ? 40.842 3.915 16.963 1.00 20.04 ? 235 VAL A C 1 ATOM 1746 O O . VAL A 1 235 ? 41.085 3.714 15.750 1.00 19.81 ? 235 VAL A O 1 ATOM 1747 C CB . VAL A 1 235 ? 42.533 3.337 18.796 1.00 20.67 ? 235 VAL A CB 1 ATOM 1748 C CG1 . VAL A 1 235 ? 42.986 2.178 17.913 1.00 21.60 ? 235 VAL A CG1 1 ATOM 1749 C CG2 . VAL A 1 235 ? 43.699 3.869 19.607 1.00 20.41 ? 235 VAL A CG2 1 ATOM 1750 N N . VAL A 1 236 ? 39.652 3.682 17.510 1.00 20.06 ? 236 VAL A N 1 ATOM 1751 C CA . VAL A 1 236 ? 38.510 3.202 16.717 1.00 20.50 ? 236 VAL A CA 1 ATOM 1752 C C . VAL A 1 236 ? 38.060 4.214 15.679 1.00 20.15 ? 236 VAL A C 1 ATOM 1753 O O . VAL A 1 236 ? 37.875 3.895 14.510 1.00 20.13 ? 236 VAL A O 1 ATOM 1754 C CB . VAL A 1 236 ? 37.352 2.721 17.620 1.00 20.02 ? 236 VAL A CB 1 ATOM 1755 C CG1 . VAL A 1 236 ? 36.124 2.338 16.798 1.00 20.03 ? 236 VAL A CG1 1 ATOM 1756 C CG2 . VAL A 1 236 ? 37.828 1.567 18.526 1.00 20.53 ? 236 VAL A CG2 1 ATOM 1757 N N . GLY A 1 237 ? 37.957 5.457 16.073 1.00 21.25 ? 237 GLY A N 1 ATOM 1758 C CA . GLY A 1 237 ? 37.611 6.548 15.157 1.00 22.24 ? 237 GLY A CA 1 ATOM 1759 C C . GLY A 1 237 ? 38.569 6.746 13.999 1.00 21.74 ? 237 GLY A C 1 ATOM 1760 O O . GLY A 1 237 ? 38.144 6.964 12.889 1.00 21.02 ? 237 GLY A O 1 ATOM 1761 N N . ARG A 1 238 ? 39.848 6.762 14.317 1.00 23.49 ? 238 ARG A N 1 ATOM 1762 C CA . ARG A 1 238 ? 40.950 6.811 13.344 1.00 24.44 ? 238 ARG A CA 1 ATOM 1763 C C . ARG A 1 238 ? 40.838 5.662 12.365 1.00 24.25 ? 238 ARG A C 1 ATOM 1764 O O . ARG A 1 238 ? 40.989 5.847 11.184 1.00 24.30 ? 238 ARG A O 1 ATOM 1765 C CB . ARG A 1 238 ? 42.321 6.765 14.059 1.00 26.17 ? 238 ARG A CB 1 ATOM 1766 C CG . ARG A 1 238 ? 43.555 6.843 13.140 1.00 29.40 ? 238 ARG A CG 1 ATOM 1767 C CD . ARG A 1 238 ? 44.891 7.062 13.885 1.00 32.38 ? 238 ARG A CD 1 ATOM 1768 N NE . ARG A 1 238 ? 45.102 5.937 14.769 1.00 35.24 ? 238 ARG A NE 1 ATOM 1769 C CZ . ARG A 1 238 ? 46.110 5.734 15.641 1.00 38.66 ? 238 ARG A CZ 1 ATOM 1770 N NH1 . ARG A 1 238 ? 47.101 6.612 15.863 1.00 37.98 ? 238 ARG A NH1 1 ATOM 1771 N NH2 . ARG A 1 238 ? 46.112 4.579 16.306 1.00 41.84 ? 238 ARG A NH2 1 ATOM 1772 N N . SER A 1 239 ? 40.592 4.459 12.875 1.00 23.43 ? 239 SER A N 1 ATOM 1773 C CA . SER A 1 239 ? 40.433 3.285 12.037 1.00 22.58 ? 239 SER A CA 1 ATOM 1774 C C . SER A 1 239 ? 39.286 3.518 11.054 1.00 23.04 ? 239 SER A C 1 ATOM 1775 O O . SER A 1 239 ? 39.507 3.395 9.839 1.00 23.06 ? 239 SER A O 1 ATOM 1776 C CB . SER A 1 239 ? 40.262 2.015 12.849 1.00 22.27 ? 239 SER A CB 1 ATOM 1777 O OG . SER A 1 239 ? 39.996 0.952 12.003 1.00 20.94 ? 239 SER A OG 1 ATOM 1778 N N . ALA A 1 240 ? 38.110 3.920 11.553 1.00 20.74 ? 240 ALA A N 1 ATOM 1779 C CA . ALA A 1 240 ? 36.954 4.154 10.734 1.00 21.13 ? 240 ALA A CA 1 ATOM 1780 C C . ALA A 1 240 ? 37.227 5.216 9.678 1.00 20.82 ? 240 ALA A C 1 ATOM 1781 O O . ALA A 1 240 ? 36.794 5.062 8.550 1.00 21.31 ? 240 ALA A O 1 ATOM 1782 C CB . ALA A 1 240 ? 35.768 4.606 11.578 1.00 20.75 ? 240 ALA A CB 1 ATOM 1783 N N . LEU A 1 241 ? 37.889 6.315 10.049 1.00 20.81 ? 241 LEU A N 1 ATOM 1784 C CA . LEU A 1 241 ? 38.171 7.390 9.080 1.00 22.22 ? 241 LEU A CA 1 ATOM 1785 C C . LEU A 1 241 ? 39.162 6.966 7.964 1.00 25.51 ? 241 LEU A C 1 ATOM 1786 O O . LEU A 1 241 ? 39.025 7.415 6.866 1.00 25.96 ? 241 LEU A O 1 ATOM 1787 C CB . LEU A 1 241 ? 38.651 8.657 9.771 1.00 20.84 ? 241 LEU A CB 1 ATOM 1788 C CG . LEU A 1 241 ? 37.598 9.278 10.741 1.00 20.76 ? 241 LEU A CG 1 ATOM 1789 C CD1 . LEU A 1 241 ? 38.216 10.525 11.402 1.00 20.60 ? 241 LEU A CD1 1 ATOM 1790 C CD2 . LEU A 1 241 ? 36.326 9.620 9.993 1.00 20.50 ? 241 LEU A CD2 1 ATOM 1791 N N . ARG A 1 242 ? 40.123 6.114 8.299 1.00 28.26 ? 242 ARG A N 1 ATOM 1792 C CA A ARG A 1 242 ? 41.145 5.623 7.359 0.50 29.54 ? 242 ARG A CA 1 ATOM 1793 C CA B ARG A 1 242 ? 41.140 5.603 7.359 0.50 30.00 ? 242 ARG A CA 1 ATOM 1794 C C . ARG A 1 242 ? 40.673 4.419 6.518 1.00 29.99 ? 242 ARG A C 1 ATOM 1795 O O . ARG A 1 242 ? 41.213 4.157 5.495 1.00 29.90 ? 242 ARG A O 1 ATOM 1796 C CB A ARG A 1 242 ? 42.408 5.211 8.147 0.50 30.56 ? 242 ARG A CB 1 ATOM 1797 C CB B ARG A 1 242 ? 42.386 5.137 8.131 0.50 31.48 ? 242 ARG A CB 1 ATOM 1798 C CG A ARG A 1 242 ? 43.059 6.337 8.957 0.50 30.80 ? 242 ARG A CG 1 ATOM 1799 C CG B ARG A 1 242 ? 43.512 6.150 8.146 0.50 33.06 ? 242 ARG A CG 1 ATOM 1800 C CD A ARG A 1 242 ? 44.373 5.941 9.631 0.50 31.95 ? 242 ARG A CD 1 ATOM 1801 C CD B ARG A 1 242 ? 43.237 7.349 9.005 0.50 33.25 ? 242 ARG A CD 1 ATOM 1802 N NE A ARG A 1 242 ? 45.506 6.533 8.905 0.50 33.97 ? 242 ARG A NE 1 ATOM 1803 N NE B ARG A 1 242 ? 44.074 8.476 8.614 0.50 34.31 ? 242 ARG A NE 1 ATOM 1804 C CZ A ARG A 1 242 ? 46.299 5.866 8.073 0.50 33.93 ? 242 ARG A CZ 1 ATOM 1805 C CZ B ARG A 1 242 ? 43.645 9.563 7.964 0.50 33.33 ? 242 ARG A CZ 1 ATOM 1806 N NH1 A ARG A 1 242 ? 47.295 6.477 7.445 0.50 34.23 ? 242 ARG A NH1 1 ATOM 1807 N NH1 B ARG A 1 242 ? 44.509 10.506 7.699 0.50 32.63 ? 242 ARG A NH1 1 ATOM 1808 N NH2 A ARG A 1 242 ? 46.091 4.589 7.880 0.50 34.88 ? 242 ARG A NH2 1 ATOM 1809 N NH2 B ARG A 1 242 ? 42.377 9.705 7.580 0.50 31.78 ? 242 ARG A NH2 1 ATOM 1810 N N . SER A 1 243 ? 39.700 3.653 6.989 1.00 29.66 ? 243 SER A N 1 ATOM 1811 C CA . SER A 1 243 ? 39.369 2.331 6.389 1.00 30.28 ? 243 SER A CA 1 ATOM 1812 C C . SER A 1 243 ? 38.818 2.394 4.994 1.00 30.48 ? 243 SER A C 1 ATOM 1813 O O . SER A 1 243 ? 37.839 3.131 4.761 1.00 29.66 ? 243 SER A O 1 ATOM 1814 C CB . SER A 1 243 ? 38.304 1.653 7.225 1.00 29.55 ? 243 SER A CB 1 ATOM 1815 O OG . SER A 1 243 ? 37.794 0.487 6.618 1.00 28.86 ? 243 SER A OG 1 ATOM 1816 N N . THR A 1 244 ? 39.367 1.575 4.088 1.00 29.10 ? 244 THR A N 1 ATOM 1817 C CA . THR A 1 244 ? 38.828 1.457 2.716 1.00 30.07 ? 244 THR A CA 1 ATOM 1818 C C . THR A 1 244 ? 37.420 0.798 2.649 1.00 30.21 ? 244 THR A C 1 ATOM 1819 O O . THR A 1 244 ? 36.792 0.797 1.588 1.00 30.58 ? 244 THR A O 1 ATOM 1820 C CB . THR A 1 244 ? 39.803 0.690 1.737 1.00 31.91 ? 244 THR A CB 1 ATOM 1821 O OG1 . THR A 1 244 ? 40.060 -0.622 2.226 1.00 34.04 ? 244 THR A OG1 1 ATOM 1822 C CG2 . THR A 1 244 ? 41.169 1.376 1.570 1.00 31.11 ? 244 THR A CG2 1 ATOM 1823 N N . THR A 1 245 ? 36.930 0.204 3.739 1.00 29.64 ? 245 THR A N 1 ATOM 1824 C CA . THR A 1 245 ? 35.541 -0.276 3.810 1.00 29.35 ? 245 THR A CA 1 ATOM 1825 C C . THR A 1 245 ? 34.555 0.778 4.316 1.00 29.19 ? 245 THR A C 1 ATOM 1826 O O . THR A 1 245 ? 33.346 0.566 4.265 1.00 28.41 ? 245 THR A O 1 ATOM 1827 C CB . THR A 1 245 ? 35.414 -1.496 4.740 1.00 29.05 ? 245 THR A CB 1 ATOM 1828 O OG1 . THR A 1 245 ? 35.715 -1.098 6.100 1.00 27.59 ? 245 THR A OG1 1 ATOM 1829 C CG2 . THR A 1 245 ? 36.333 -2.698 4.214 1.00 30.21 ? 245 THR A CG2 1 ATOM 1830 N N . GLY A 1 246 ? 35.051 1.919 4.808 1.00 28.84 ? 246 GLY A N 1 ATOM 1831 C CA . GLY A 1 246 ? 34.162 2.886 5.426 1.00 27.76 ? 246 GLY A CA 1 ATOM 1832 C C . GLY A 1 246 ? 33.773 2.601 6.850 1.00 26.86 ? 246 GLY A C 1 ATOM 1833 O O . GLY A 1 246 ? 33.207 3.482 7.491 1.00 25.88 ? 246 GLY A O 1 ATOM 1834 N N . GLN A 1 247 ? 34.193 1.443 7.399 1.00 24.55 ? 247 GLN A N 1 ATOM 1835 C CA . GLN A 1 247 ? 33.978 1.114 8.810 1.00 23.46 ? 247 GLN A CA 1 ATOM 1836 C C . GLN A 1 247 ? 35.278 0.839 9.540 1.00 23.09 ? 247 GLN A C 1 ATOM 1837 O O . GLN A 1 247 ? 36.291 0.520 8.903 1.00 22.98 ? 247 GLN A O 1 ATOM 1838 C CB . GLN A 1 247 ? 33.069 -0.124 8.910 1.00 23.85 ? 247 GLN A CB 1 ATOM 1839 C CG . GLN A 1 247 ? 31.717 -0.024 8.194 1.00 22.94 ? 247 GLN A CG 1 ATOM 1840 C CD . GLN A 1 247 ? 30.918 -1.285 8.454 1.00 24.89 ? 247 GLN A CD 1 ATOM 1841 O OE1 . GLN A 1 247 ? 31.521 -2.366 8.606 1.00 27.16 ? 247 GLN A OE1 1 ATOM 1842 N NE2 . GLN A 1 247 ? 29.602 -1.178 8.606 1.00 23.10 ? 247 GLN A NE2 1 ATOM 1843 N N . ALA A 1 248 ? 35.286 0.899 10.872 1.00 20.66 ? 248 ALA A N 1 ATOM 1844 C CA . ALA A 1 248 ? 36.485 0.581 11.586 1.00 22.25 ? 248 ALA A CA 1 ATOM 1845 C C . ALA A 1 248 ? 36.726 -0.912 11.367 1.00 24.77 ? 248 ALA A C 1 ATOM 1846 O O . ALA A 1 248 ? 35.782 -1.659 11.175 1.00 22.71 ? 248 ALA A O 1 ATOM 1847 C CB . ALA A 1 248 ? 36.366 0.821 13.060 1.00 22.44 ? 248 ALA A CB 1 ATOM 1848 N N . ARG A 1 249 ? 37.973 -1.305 11.559 1.00 28.76 ? 249 ARG A N 1 ATOM 1849 C CA . ARG A 1 249 ? 38.445 -2.670 11.376 1.00 31.54 ? 249 ARG A CA 1 ATOM 1850 C C . ARG A 1 249 ? 39.068 -3.241 12.660 1.00 29.54 ? 249 ARG A C 1 ATOM 1851 O O . ARG A 1 249 ? 39.948 -2.670 13.271 1.00 26.80 ? 249 ARG A O 1 ATOM 1852 C CB . ARG A 1 249 ? 39.437 -2.655 10.208 1.00 36.83 ? 249 ARG A CB 1 ATOM 1853 C CG . ARG A 1 249 ? 38.834 -2.204 8.861 1.00 40.13 ? 249 ARG A CG 1 ATOM 1854 C CD . ARG A 1 249 ? 37.608 -3.048 8.422 1.00 45.55 ? 249 ARG A CD 1 ATOM 1855 N NE . ARG A 1 249 ? 37.892 -4.439 7.914 1.00 49.22 ? 249 ARG A NE 1 ATOM 1856 C CZ . ARG A 1 249 ? 37.552 -5.615 8.493 1.00 51.19 ? 249 ARG A CZ 1 ATOM 1857 N NH1 . ARG A 1 249 ? 36.952 -5.705 9.685 1.00 51.87 ? 249 ARG A NH1 1 ATOM 1858 N NH2 . ARG A 1 249 ? 37.862 -6.766 7.870 1.00 56.23 ? 249 ARG A NH2 1 ATOM 1859 N N . SER A 1 250 ? 38.546 -4.373 13.075 1.00 30.87 ? 250 SER A N 1 ATOM 1860 C CA . SER A 1 250 ? 39.045 -5.095 14.216 1.00 31.40 ? 250 SER A CA 1 ATOM 1861 C C . SER A 1 250 ? 40.537 -5.320 14.135 1.00 31.49 ? 250 SER A C 1 ATOM 1862 O O . SER A 1 250 ? 41.181 -5.430 15.142 1.00 29.93 ? 250 SER A O 1 ATOM 1863 C CB . SER A 1 250 ? 38.350 -6.435 14.315 1.00 33.10 ? 250 SER A CB 1 ATOM 1864 O OG . SER A 1 250 ? 37.019 -6.191 14.679 1.00 34.33 ? 250 SER A OG 1 ATOM 1865 N N . ALA A 1 251 ? 41.097 -5.326 12.936 1.00 31.73 ? 251 ALA A N 1 ATOM 1866 C CA . ALA A 1 251 ? 42.508 -5.504 12.833 1.00 32.13 ? 251 ALA A CA 1 ATOM 1867 C C . ALA A 1 251 ? 43.269 -4.320 13.364 1.00 32.33 ? 251 ALA A C 1 ATOM 1868 O O . ALA A 1 251 ? 44.442 -4.476 13.627 1.00 30.62 ? 251 ALA A O 1 ATOM 1869 C CB . ALA A 1 251 ? 42.893 -5.788 11.391 1.00 33.64 ? 251 ALA A CB 1 ATOM 1870 N N . ASP A 1 252 ? 42.620 -3.143 13.518 1.00 31.02 ? 252 ASP A N 1 ATOM 1871 C CA . ASP A 1 252 ? 43.262 -1.885 13.798 1.00 30.12 ? 252 ASP A CA 1 ATOM 1872 C C . ASP A 1 252 ? 43.358 -1.604 15.270 1.00 30.34 ? 252 ASP A C 1 ATOM 1873 O O . ASP A 1 252 ? 44.099 -0.706 15.703 1.00 31.08 ? 252 ASP A O 1 ATOM 1874 C CB . ASP A 1 252 ? 42.502 -0.716 13.089 1.00 31.97 ? 252 ASP A CB 1 ATOM 1875 C CG . ASP A 1 252 ? 42.627 -0.767 11.568 1.00 32.29 ? 252 ASP A CG 1 ATOM 1876 O OD1 . ASP A 1 252 ? 43.553 -1.464 11.129 1.00 35.11 ? 252 ASP A OD1 1 ATOM 1877 O OD2 . ASP A 1 252 ? 41.842 -0.165 10.780 1.00 29.07 ? 252 ASP A OD2 1 ATOM 1878 N N . TYR A 1 253 ? 42.623 -2.348 16.076 1.00 31.67 ? 253 TYR A N 1 ATOM 1879 C CA . TYR A 1 253 ? 42.604 -2.094 17.520 1.00 32.44 ? 253 TYR A CA 1 ATOM 1880 C C . TYR A 1 253 ? 42.414 -3.370 18.295 1.00 34.45 ? 253 TYR A C 1 ATOM 1881 O O . TYR A 1 253 ? 41.806 -4.325 17.808 1.00 34.12 ? 253 TYR A O 1 ATOM 1882 C CB . TYR A 1 253 ? 41.466 -1.120 17.908 1.00 32.58 ? 253 TYR A CB 1 ATOM 1883 C CG . TYR A 1 253 ? 40.088 -1.534 17.430 1.00 31.14 ? 253 TYR A CG 1 ATOM 1884 C CD1 . TYR A 1 253 ? 39.289 -2.341 18.212 1.00 30.61 ? 253 TYR A CD1 1 ATOM 1885 C CD2 . TYR A 1 253 ? 39.578 -1.077 16.175 1.00 31.06 ? 253 TYR A CD2 1 ATOM 1886 C CE1 . TYR A 1 253 ? 38.032 -2.734 17.795 1.00 30.10 ? 253 TYR A CE1 1 ATOM 1887 C CE2 . TYR A 1 253 ? 38.305 -1.442 15.763 1.00 30.16 ? 253 TYR A CE2 1 ATOM 1888 C CZ . TYR A 1 253 ? 37.540 -2.272 16.574 1.00 29.95 ? 253 TYR A CZ 1 ATOM 1889 O OH . TYR A 1 253 ? 36.267 -2.648 16.189 1.00 31.61 ? 253 TYR A OH 1 ATOM 1890 N N . GLY A 1 254 ? 42.923 -3.331 19.514 1.00 36.05 ? 254 GLY A N 1 ATOM 1891 C CA . GLY A 1 254 ? 42.918 -4.468 20.421 1.00 36.42 ? 254 GLY A CA 1 ATOM 1892 C C . GLY A 1 254 ? 43.082 -3.985 21.827 1.00 35.84 ? 254 GLY A C 1 ATOM 1893 O O . GLY A 1 254 ? 43.093 -2.763 22.106 1.00 32.63 ? 254 GLY A O 1 ATOM 1894 N N . ILE A 1 255 ? 43.196 -4.988 22.683 1.00 34.83 ? 255 ILE A N 1 ATOM 1895 C CA . ILE A 1 255 ? 43.440 -4.888 24.099 1.00 35.26 ? 255 ILE A CA 1 ATOM 1896 C C . ILE A 1 255 ? 44.390 -3.781 24.529 1.00 31.29 ? 255 ILE A C 1 ATOM 1897 O O . ILE A 1 255 ? 44.077 -3.014 25.447 1.00 29.50 ? 255 ILE A O 1 ATOM 1898 C CB . ILE A 1 255 ? 43.900 -6.310 24.543 1.00 40.80 ? 255 ILE A CB 1 ATOM 1899 C CG1 . ILE A 1 255 ? 42.657 -7.092 24.977 1.00 43.17 ? 255 ILE A CG1 1 ATOM 1900 C CG2 . ILE A 1 255 ? 45.023 -6.336 25.583 1.00 41.25 ? 255 ILE A CG2 1 ATOM 1901 C CD1 . ILE A 1 255 ? 42.781 -8.601 24.728 1.00 47.04 ? 255 ILE A CD1 1 ATOM 1902 N N . THR A 1 256 ? 45.507 -3.645 23.845 1.00 29.97 ? 256 THR A N 1 ATOM 1903 C CA . THR A 1 256 ? 46.473 -2.602 24.177 1.00 30.05 ? 256 THR A CA 1 ATOM 1904 C C . THR A 1 256 ? 46.000 -1.173 23.907 1.00 28.99 ? 256 THR A C 1 ATOM 1905 O O . THR A 1 256 ? 46.630 -0.233 24.381 1.00 28.60 ? 256 THR A O 1 ATOM 1906 C CB . THR A 1 256 ? 47.821 -2.760 23.464 1.00 31.71 ? 256 THR A CB 1 ATOM 1907 O OG1 . THR A 1 256 ? 47.620 -2.767 22.047 1.00 34.12 ? 256 THR A OG1 1 ATOM 1908 C CG2 . THR A 1 256 ? 48.513 -4.052 23.884 1.00 33.68 ? 256 THR A CG2 1 ATOM 1909 N N . ASP A 1 257 ? 44.886 -0.985 23.216 1.00 28.24 ? 257 ASP A N 1 ATOM 1910 C CA . ASP A 1 257 ? 44.303 0.386 23.017 1.00 26.52 ? 257 ASP A CA 1 ATOM 1911 C C . ASP A 1 257 ? 43.236 0.705 24.043 1.00 24.34 ? 257 ASP A C 1 ATOM 1912 O O . ASP A 1 257 ? 42.566 1.768 23.963 1.00 24.77 ? 257 ASP A O 1 ATOM 1913 C CB . ASP A 1 257 ? 43.698 0.471 21.619 1.00 26.05 ? 257 ASP A CB 1 ATOM 1914 C CG . ASP A 1 257 ? 44.691 0.117 20.561 1.00 26.84 ? 257 ASP A CG 1 ATOM 1915 O OD1 . ASP A 1 257 ? 45.644 0.906 20.458 1.00 25.44 ? 257 ASP A OD1 1 ATOM 1916 O OD2 . ASP A 1 257 ? 44.511 -0.943 19.878 1.00 26.89 ? 257 ASP A OD2 1 ATOM 1917 N N . CYS A 1 258 ? 43.029 -0.201 25.006 1.00 24.00 ? 258 CYS A N 1 ATOM 1918 C CA . CYS A 1 258 ? 41.956 -0.045 25.944 1.00 23.52 ? 258 CYS A CA 1 ATOM 1919 C C . CYS A 1 258 ? 42.408 0.919 27.069 1.00 23.50 ? 258 CYS A C 1 ATOM 1920 O O . CYS A 1 258 ? 42.453 0.534 28.236 1.00 23.99 ? 258 CYS A O 1 ATOM 1921 C CB . CYS A 1 258 ? 41.498 -1.385 26.484 1.00 25.15 ? 258 CYS A CB 1 ATOM 1922 S SG . CYS A 1 258 ? 40.692 -2.374 25.223 1.00 26.50 ? 258 CYS A SG 1 ATOM 1923 N N . ASN A 1 259 ? 42.655 2.178 26.708 1.00 22.17 ? 259 ASN A N 1 ATOM 1924 C CA . ASN A 1 259 ? 42.985 3.243 27.631 1.00 22.57 ? 259 ASN A CA 1 ATOM 1925 C C . ASN A 1 259 ? 41.742 4.154 27.792 1.00 23.19 ? 259 ASN A C 1 ATOM 1926 O O . ASN A 1 259 ? 41.328 4.820 26.834 1.00 21.90 ? 259 ASN A O 1 ATOM 1927 C CB . ASN A 1 259 ? 44.169 4.012 27.056 1.00 23.09 ? 259 ASN A CB 1 ATOM 1928 C CG . ASN A 1 259 ? 44.569 5.204 27.873 1.00 23.72 ? 259 ASN A CG 1 ATOM 1929 O OD1 . ASN A 1 259 ? 43.928 5.558 28.819 1.00 24.59 ? 259 ASN A OD1 1 ATOM 1930 N ND2 . ASN A 1 259 ? 45.666 5.834 27.496 1.00 24.60 ? 259 ASN A ND2 1 ATOM 1931 N N . PRO A 1 260 ? 41.155 4.218 28.989 1.00 22.65 ? 260 PRO A N 1 ATOM 1932 C CA . PRO A 1 260 ? 39.935 5.015 29.077 1.00 22.74 ? 260 PRO A CA 1 ATOM 1933 C C . PRO A 1 260 ? 40.206 6.496 29.270 1.00 23.64 ? 260 PRO A C 1 ATOM 1934 O O . PRO A 1 260 ? 39.262 7.214 29.284 1.00 24.92 ? 260 PRO A O 1 ATOM 1935 C CB . PRO A 1 260 ? 39.274 4.499 30.322 1.00 22.23 ? 260 PRO A CB 1 ATOM 1936 C CG . PRO A 1 260 ? 40.418 4.133 31.210 1.00 23.01 ? 260 PRO A CG 1 ATOM 1937 C CD . PRO A 1 260 ? 41.510 3.622 30.290 1.00 23.50 ? 260 PRO A CD 1 ATOM 1938 N N . LEU A 1 261 ? 41.471 6.921 29.411 1.00 23.99 ? 261 LEU A N 1 ATOM 1939 C CA . LEU A 1 261 ? 41.762 8.361 29.603 1.00 25.35 ? 261 LEU A CA 1 ATOM 1940 C C . LEU A 1 261 ? 41.566 9.152 28.304 1.00 23.70 ? 261 LEU A C 1 ATOM 1941 O O . LEU A 1 261 ? 41.587 8.578 27.226 1.00 20.22 ? 261 LEU A O 1 ATOM 1942 C CB . LEU A 1 261 ? 43.162 8.530 30.176 1.00 26.20 ? 261 LEU A CB 1 ATOM 1943 C CG . LEU A 1 261 ? 43.285 7.936 31.584 1.00 27.40 ? 261 LEU A CG 1 ATOM 1944 C CD1 . LEU A 1 261 ? 44.661 8.285 32.120 1.00 29.88 ? 261 LEU A CD1 1 ATOM 1945 C CD2 . LEU A 1 261 ? 42.214 8.400 32.548 1.00 30.01 ? 261 LEU A CD2 1 ATOM 1946 N N . PRO A 1 262 ? 41.367 10.475 28.396 1.00 22.70 ? 262 PRO A N 1 ATOM 1947 C CA . PRO A 1 262 ? 41.298 11.226 27.133 1.00 21.75 ? 262 PRO A CA 1 ATOM 1948 C C . PRO A 1 262 ? 42.500 10.940 26.175 1.00 22.84 ? 262 PRO A C 1 ATOM 1949 O O . PRO A 1 262 ? 43.659 10.684 26.658 1.00 22.83 ? 262 PRO A O 1 ATOM 1950 C CB . PRO A 1 262 ? 41.276 12.689 27.597 1.00 22.46 ? 262 PRO A CB 1 ATOM 1951 C CG . PRO A 1 262 ? 40.760 12.666 29.010 1.00 22.77 ? 262 PRO A CG 1 ATOM 1952 C CD . PRO A 1 262 ? 41.325 11.359 29.590 1.00 23.12 ? 262 PRO A CD 1 ATOM 1953 N N . ALA A 1 263 ? 42.226 10.986 24.871 1.00 21.84 ? 263 ALA A N 1 ATOM 1954 C CA . ALA A 1 263 ? 43.180 10.709 23.764 1.00 22.72 ? 263 ALA A CA 1 ATOM 1955 C C . ALA A 1 263 ? 44.533 11.336 24.009 1.00 24.22 ? 263 ALA A C 1 ATOM 1956 O O . ALA A 1 263 ? 44.630 12.542 24.376 1.00 23.57 ? 263 ALA A O 1 ATOM 1957 C CB . ALA A 1 263 ? 42.621 11.155 22.431 1.00 22.86 ? 263 ALA A CB 1 ATOM 1958 N N . ASN A 1 264 ? 45.554 10.482 23.896 1.00 25.37 ? 264 ASN A N 1 ATOM 1959 C CA . ASN A 1 264 ? 46.937 10.824 24.235 1.00 26.94 ? 264 ASN A CA 1 ATOM 1960 C C . ASN A 1 264 ? 47.417 12.100 23.552 1.00 27.49 ? 264 ASN A C 1 ATOM 1961 O O . ASN A 1 264 ? 48.092 12.893 24.172 1.00 26.91 ? 264 ASN A O 1 ATOM 1962 C CB . ASN A 1 264 ? 47.920 9.745 23.786 1.00 27.35 ? 264 ASN A CB 1 ATOM 1963 C CG . ASN A 1 264 ? 47.776 8.438 24.493 1.00 28.01 ? 264 ASN A CG 1 ATOM 1964 O OD1 . ASN A 1 264 ? 47.215 8.320 25.573 1.00 29.84 ? 264 ASN A OD1 1 ATOM 1965 N ND2 . ASN A 1 264 ? 48.323 7.429 23.870 1.00 29.71 ? 264 ASN A ND2 1 ATOM 1966 N N . ASP A 1 265 ? 47.042 12.280 22.300 1.00 29.15 ? 265 ASP A N 1 ATOM 1967 C CA . ASP A 1 265 ? 47.536 13.442 21.517 1.00 33.04 ? 265 ASP A CA 1 ATOM 1968 C C . ASP A 1 265 ? 47.005 14.807 22.007 1.00 34.13 ? 265 ASP A C 1 ATOM 1969 O O . ASP A 1 265 ? 47.614 15.840 21.786 1.00 35.65 ? 265 ASP A O 1 ATOM 1970 C CB . ASP A 1 265 ? 47.217 13.242 20.028 1.00 33.89 ? 265 ASP A CB 1 ATOM 1971 C CG . ASP A 1 265 ? 48.100 12.184 19.384 1.00 36.68 ? 265 ASP A CG 1 ATOM 1972 O OD1 . ASP A 1 265 ? 47.603 11.348 18.567 1.00 38.52 ? 265 ASP A OD1 1 ATOM 1973 O OD2 . ASP A 1 265 ? 49.290 12.153 19.774 1.00 37.91 ? 265 ASP A OD2 1 ATOM 1974 N N . LEU A 1 266 ? 45.918 14.790 22.767 1.00 30.45 ? 266 LEU A N 1 ATOM 1975 C CA . LEU A 1 266 ? 45.334 16.022 23.213 1.00 28.68 ? 266 LEU A CA 1 ATOM 1976 C C . LEU A 1 266 ? 46.216 16.776 24.205 1.00 29.37 ? 266 LEU A C 1 ATOM 1977 O O . LEU A 1 266 ? 46.953 16.174 24.972 1.00 28.96 ? 266 LEU A O 1 ATOM 1978 C CB . LEU A 1 266 ? 43.960 15.699 23.859 1.00 27.50 ? 266 LEU A CB 1 ATOM 1979 C CG . LEU A 1 266 ? 42.857 15.114 22.967 1.00 25.89 ? 266 LEU A CG 1 ATOM 1980 C CD1 . LEU A 1 266 ? 41.677 14.734 23.852 1.00 25.47 ? 266 LEU A CD1 1 ATOM 1981 C CD2 . LEU A 1 266 ? 42.356 16.054 21.897 1.00 26.98 ? 266 LEU A CD2 1 ATOM 1982 N N . THR A 1 267 ? 46.105 18.113 24.226 1.00 29.36 ? 267 THR A N 1 ATOM 1983 C CA . THR A 1 267 ? 46.932 18.929 25.136 1.00 29.93 ? 267 THR A CA 1 ATOM 1984 C C . THR A 1 267 ? 46.412 18.729 26.555 1.00 30.57 ? 267 THR A C 1 ATOM 1985 O O . THR A 1 267 ? 45.322 18.243 26.722 1.00 30.27 ? 267 THR A O 1 ATOM 1986 C CB . THR A 1 267 ? 46.862 20.431 24.753 1.00 28.62 ? 267 THR A CB 1 ATOM 1987 O OG1 . THR A 1 267 ? 45.504 20.895 24.925 1.00 24.73 ? 267 THR A OG1 1 ATOM 1988 C CG2 . THR A 1 267 ? 47.277 20.601 23.281 1.00 28.15 ? 267 THR A CG2 1 ATOM 1989 N N . PRO A 1 268 ? 47.226 19.040 27.578 1.00 33.49 ? 268 PRO A N 1 ATOM 1990 C CA . PRO A 1 268 ? 46.783 18.949 28.936 1.00 33.45 ? 268 PRO A CA 1 ATOM 1991 C C . PRO A 1 268 ? 45.432 19.664 29.145 1.00 35.75 ? 268 PRO A C 1 ATOM 1992 O O . PRO A 1 268 ? 44.530 19.123 29.841 1.00 33.86 ? 268 PRO A O 1 ATOM 1993 C CB . PRO A 1 268 ? 47.920 19.678 29.691 1.00 34.87 ? 268 PRO A CB 1 ATOM 1994 C CG . PRO A 1 268 ? 49.137 19.335 28.927 1.00 33.42 ? 268 PRO A CG 1 ATOM 1995 C CD . PRO A 1 268 ? 48.687 19.378 27.507 1.00 33.05 ? 268 PRO A CD 1 ATOM 1996 N N . GLU A 1 269 ? 45.270 20.837 28.526 1.00 34.17 ? 269 GLU A N 1 ATOM 1997 C CA . GLU A 1 269 ? 43.994 21.556 28.677 1.00 34.59 ? 269 GLU A CA 1 ATOM 1998 C C . GLU A 1 269 ? 42.820 20.968 27.974 1.00 29.55 ? 269 GLU A C 1 ATOM 1999 O O . GLU A 1 269 ? 41.697 21.026 28.493 1.00 27.46 ? 269 GLU A O 1 ATOM 2000 C CB . GLU A 1 269 ? 44.088 23.021 28.279 1.00 37.40 ? 269 GLU A CB 1 ATOM 2001 C CG . GLU A 1 269 ? 44.779 23.849 29.358 1.00 41.73 ? 269 GLU A CG 1 ATOM 2002 C CD . GLU A 1 269 ? 44.705 23.307 30.810 1.00 44.75 ? 269 GLU A CD 1 ATOM 2003 O OE1 . GLU A 1 269 ? 43.618 23.207 31.503 1.00 42.08 ? 269 GLU A OE1 1 ATOM 2004 O OE2 . GLU A 1 269 ? 45.828 23.031 31.272 1.00 46.29 ? 269 GLU A OE2 1 ATOM 2005 N N . GLN A 1 270 ? 43.064 20.408 26.801 1.00 26.84 ? 270 GLN A N 1 ATOM 2006 C CA . GLN A 1 270 ? 42.014 19.690 26.120 1.00 25.37 ? 270 GLN A CA 1 ATOM 2007 C C . GLN A 1 270 ? 41.595 18.476 26.901 1.00 24.88 ? 270 GLN A C 1 ATOM 2008 O O . GLN A 1 270 ? 40.450 18.118 26.879 1.00 22.42 ? 270 GLN A O 1 ATOM 2009 C CB . GLN A 1 270 ? 42.412 19.324 24.712 1.00 24.61 ? 270 GLN A CB 1 ATOM 2010 C CG . GLN A 1 270 ? 42.488 20.546 23.778 1.00 24.45 ? 270 GLN A CG 1 ATOM 2011 C CD . GLN A 1 270 ? 43.364 20.289 22.544 1.00 24.99 ? 270 GLN A CD 1 ATOM 2012 O OE1 . GLN A 1 270 ? 44.029 19.258 22.409 1.00 23.37 ? 270 GLN A OE1 1 ATOM 2013 N NE2 . GLN A 1 270 ? 43.335 21.238 21.627 1.00 23.96 ? 270 GLN A NE2 1 ATOM 2014 N N . LYS A 1 271 ? 42.535 17.852 27.606 1.00 27.36 ? 271 LYS A N 1 ATOM 2015 C CA . LYS A 1 271 ? 42.241 16.619 28.365 1.00 27.89 ? 271 LYS A CA 1 ATOM 2016 C C . LYS A 1 271 ? 41.368 16.937 29.610 1.00 27.88 ? 271 LYS A C 1 ATOM 2017 O O . LYS A 1 271 ? 40.443 16.185 29.989 1.00 26.16 ? 271 LYS A O 1 ATOM 2018 C CB . LYS A 1 271 ? 43.525 15.912 28.728 1.00 28.45 ? 271 LYS A CB 1 ATOM 2019 C CG . LYS A 1 271 ? 44.267 15.186 27.622 1.00 28.90 ? 271 LYS A CG 1 ATOM 2020 C CD . LYS A 1 271 ? 45.235 14.271 28.321 1.00 29.62 ? 271 LYS A CD 1 ATOM 2021 C CE . LYS A 1 271 ? 46.003 13.281 27.490 1.00 32.61 ? 271 LYS A CE 1 ATOM 2022 N NZ . LYS A 1 271 ? 47.141 13.897 26.796 1.00 35.45 ? 271 LYS A NZ 1 ATOM 2023 N N . VAL A 1 272 ? 41.634 18.100 30.196 1.00 27.00 ? 272 VAL A N 1 ATOM 2024 C CA . VAL A 1 272 ? 40.885 18.558 31.314 1.00 27.29 ? 272 VAL A CA 1 ATOM 2025 C C . VAL A 1 272 ? 39.466 18.902 30.829 1.00 25.05 ? 272 VAL A C 1 ATOM 2026 O O . VAL A 1 272 ? 38.487 18.498 31.449 1.00 26.59 ? 272 VAL A O 1 ATOM 2027 C CB . VAL A 1 272 ? 41.584 19.794 31.988 1.00 29.24 ? 272 VAL A CB 1 ATOM 2028 C CG1 . VAL A 1 272 ? 40.671 20.476 32.989 1.00 29.53 ? 272 VAL A CG1 1 ATOM 2029 C CG2 . VAL A 1 272 ? 42.897 19.398 32.633 1.00 29.71 ? 272 VAL A CG2 1 ATOM 2030 N N . ALA A 1 273 ? 39.346 19.639 29.731 1.00 23.43 ? 273 ALA A N 1 ATOM 2031 C CA . ALA A 1 273 ? 38.040 19.979 29.170 1.00 22.36 ? 273 ALA A CA 1 ATOM 2032 C C . ALA A 1 273 ? 37.273 18.719 28.729 1.00 21.69 ? 273 ALA A C 1 ATOM 2033 O O . ALA A 1 273 ? 36.020 18.638 28.872 1.00 20.66 ? 273 ALA A O 1 ATOM 2034 C CB . ALA A 1 273 ? 38.173 20.953 28.023 1.00 23.46 ? 273 ALA A CB 1 ATOM 2035 N N . ALA A 1 274 ? 37.980 17.751 28.148 1.00 20.64 ? 274 ALA A N 1 ATOM 2036 C CA . ALA A 1 274 ? 37.326 16.521 27.716 1.00 20.73 ? 274 ALA A CA 1 ATOM 2037 C C . ALA A 1 274 ? 36.714 15.798 28.891 1.00 21.04 ? 274 ALA A C 1 ATOM 2038 O O . ALA A 1 274 ? 35.600 15.241 28.772 1.00 20.10 ? 274 ALA A O 1 ATOM 2039 C CB . ALA A 1 274 ? 38.295 15.605 26.964 1.00 20.41 ? 274 ALA A CB 1 ATOM 2040 N N . ALA A 1 275 ? 37.464 15.720 29.996 1.00 22.17 ? 275 ALA A N 1 ATOM 2041 C CA . ALA A 1 275 ? 36.997 14.963 31.159 1.00 22.41 ? 275 ALA A CA 1 ATOM 2042 C C . ALA A 1 275 ? 35.767 15.658 31.812 1.00 23.30 ? 275 ALA A C 1 ATOM 2043 O O . ALA A 1 275 ? 34.962 15.003 32.395 1.00 22.86 ? 275 ALA A O 1 ATOM 2044 C CB . ALA A 1 275 ? 38.094 14.803 32.187 1.00 23.10 ? 275 ALA A CB 1 ATOM 2045 N N . ALA A 1 276 ? 35.649 16.993 31.673 1.00 22.61 ? 276 ALA A N 1 ATOM 2046 C CA . ALA A 1 276 ? 34.562 17.798 32.200 1.00 22.81 ? 276 ALA A CA 1 ATOM 2047 C C . ALA A 1 276 ? 33.355 18.010 31.223 1.00 21.77 ? 276 ALA A C 1 ATOM 2048 O O . ALA A 1 276 ? 32.351 18.673 31.550 1.00 20.35 ? 276 ALA A O 1 ATOM 2049 C CB . ALA A 1 276 ? 35.124 19.136 32.595 1.00 22.70 ? 276 ALA A CB 1 ATOM 2050 N N . LEU A 1 277 ? 33.427 17.377 30.063 1.00 22.33 ? 277 LEU A N 1 ATOM 2051 C CA . LEU A 1 277 ? 32.456 17.647 28.948 1.00 22.85 ? 277 LEU A CA 1 ATOM 2052 C C . LEU A 1 277 ? 30.962 17.586 29.307 1.00 21.95 ? 277 LEU A C 1 ATOM 2053 O O . LEU A 1 277 ? 30.178 18.326 28.784 1.00 21.37 ? 277 LEU A O 1 ATOM 2054 C CB . LEU A 1 277 ? 32.730 16.659 27.811 1.00 23.32 ? 277 LEU A CB 1 ATOM 2055 C CG . LEU A 1 277 ? 32.167 17.009 26.485 1.00 23.65 ? 277 LEU A CG 1 ATOM 2056 C CD1 . LEU A 1 277 ? 32.849 18.302 25.974 1.00 24.02 ? 277 LEU A CD1 1 ATOM 2057 C CD2 . LEU A 1 277 ? 32.434 15.785 25.578 1.00 23.12 ? 277 LEU A CD2 1 ATOM 2058 N N . LEU A 1 278 ? 30.572 16.658 30.150 1.00 22.33 ? 278 LEU A N 1 ATOM 2059 C CA . LEU A 1 278 ? 29.144 16.524 30.501 1.00 22.85 ? 278 LEU A CA 1 ATOM 2060 C C . LEU A 1 278 ? 28.587 17.666 31.339 1.00 21.69 ? 278 LEU A C 1 ATOM 2061 O O . LEU A 1 278 ? 27.364 18.009 31.284 1.00 21.53 ? 278 LEU A O 1 ATOM 2062 C CB . LEU A 1 278 ? 28.913 15.258 31.280 1.00 24.55 ? 278 LEU A CB 1 ATOM 2063 C CG . LEU A 1 278 ? 29.006 13.914 30.547 1.00 26.29 ? 278 LEU A CG 1 ATOM 2064 C CD1 . LEU A 1 278 ? 28.383 12.852 31.446 1.00 26.26 ? 278 LEU A CD1 1 ATOM 2065 C CD2 . LEU A 1 278 ? 28.227 13.941 29.213 1.00 26.22 ? 278 LEU A CD2 1 ATOM 2066 N N . ALA A 1 279 ? 29.466 18.301 32.098 1.00 21.01 ? 279 ALA A N 1 ATOM 2067 C CA . ALA A 1 279 ? 28.987 19.369 33.019 1.00 21.12 ? 279 ALA A CA 1 ATOM 2068 C C . ALA A 1 279 ? 28.383 20.565 32.302 1.00 21.40 ? 279 ALA A C 1 ATOM 2069 O O . ALA A 1 279 ? 27.243 20.931 32.603 1.00 22.14 ? 279 ALA A O 1 ATOM 2070 C CB . ALA A 1 279 ? 30.142 19.811 33.954 1.00 21.41 ? 279 ALA A CB 1 ATOM 2071 N N . PRO A 1 280 ? 29.099 21.167 31.310 1.00 20.93 ? 280 PRO A N 1 ATOM 2072 C CA . PRO A 1 280 ? 28.470 22.320 30.652 1.00 21.01 ? 280 PRO A CA 1 ATOM 2073 C C . PRO A 1 280 ? 27.214 21.959 29.839 1.00 21.11 ? 280 PRO A C 1 ATOM 2074 O O . PRO A 1 280 ? 26.301 22.750 29.711 1.00 20.78 ? 280 PRO A O 1 ATOM 2075 C CB . PRO A 1 280 ? 29.573 22.885 29.719 1.00 22.03 ? 280 PRO A CB 1 ATOM 2076 C CG . PRO A 1 280 ? 30.792 22.099 29.956 1.00 22.44 ? 280 PRO A CG 1 ATOM 2077 C CD . PRO A 1 280 ? 30.515 20.974 30.916 1.00 22.09 ? 280 PRO A CD 1 ATOM 2078 N N . ALA A 1 281 ? 27.199 20.759 29.271 1.00 19.88 ? 281 ALA A N 1 ATOM 2079 C CA . ALA A 1 281 ? 26.057 20.317 28.477 1.00 20.95 ? 281 ALA A CA 1 ATOM 2080 C C . ALA A 1 281 ? 24.791 20.111 29.396 1.00 21.98 ? 281 ALA A C 1 ATOM 2081 O O . ALA A 1 281 ? 23.688 20.563 29.046 1.00 22.66 ? 281 ALA A O 1 ATOM 2082 C CB . ALA A 1 281 ? 26.379 19.028 27.730 1.00 19.19 ? 281 ALA A CB 1 ATOM 2083 N N . ALA A 1 282 ? 24.961 19.444 30.540 1.00 24.18 ? 282 ALA A N 1 ATOM 2084 C CA . ALA A 1 282 ? 23.838 19.367 31.526 1.00 26.20 ? 282 ALA A CA 1 ATOM 2085 C C . ALA A 1 282 ? 23.364 20.795 31.956 1.00 28.83 ? 282 ALA A C 1 ATOM 2086 O O . ALA A 1 282 ? 22.187 21.124 31.929 1.00 32.92 ? 282 ALA A O 1 ATOM 2087 C CB . ALA A 1 282 ? 24.256 18.534 32.704 1.00 28.10 ? 282 ALA A CB 1 ATOM 2088 N N . ALA A 1 283 ? 24.275 21.707 32.197 1.00 29.90 ? 283 ALA A N 1 ATOM 2089 C CA . ALA A 1 283 ? 23.899 23.080 32.502 1.00 31.60 ? 283 ALA A CA 1 ATOM 2090 C C . ALA A 1 283 ? 23.152 23.811 31.420 1.00 33.10 ? 283 ALA A C 1 ATOM 2091 O O . ALA A 1 283 ? 22.315 24.688 31.710 1.00 34.26 ? 283 ALA A O 1 ATOM 2092 C CB . ALA A 1 283 ? 25.145 23.916 32.831 1.00 32.33 ? 283 ALA A CB 1 ATOM 2093 N N . ALA A 1 284 ? 23.504 23.557 30.170 1.00 30.68 ? 284 ALA A N 1 ATOM 2094 C CA . ALA A 1 284 ? 22.806 24.212 29.052 1.00 28.77 ? 284 ALA A CA 1 ATOM 2095 C C . ALA A 1 284 ? 21.396 23.660 28.932 1.00 28.34 ? 284 ALA A C 1 ATOM 2096 O O . ALA A 1 284 ? 20.438 24.452 28.645 1.00 28.62 ? 284 ALA A O 1 ATOM 2097 C CB . ALA A 1 284 ? 23.577 24.028 27.755 1.00 28.55 ? 284 ALA A CB 1 ATOM 2098 N N . ILE A 1 285 ? 21.265 22.360 29.203 1.00 26.19 ? 285 ILE A N 1 ATOM 2099 C CA . ILE A 1 285 ? 19.953 21.663 29.183 1.00 28.17 ? 285 ILE A CA 1 ATOM 2100 C C . ILE A 1 285 ? 18.946 22.328 30.161 1.00 31.25 ? 285 ILE A C 1 ATOM 2101 O O . ILE A 1 285 ? 17.903 22.919 29.780 1.00 32.66 ? 285 ILE A O 1 ATOM 2102 C CB . ILE A 1 285 ? 20.112 20.124 29.375 1.00 26.77 ? 285 ILE A CB 1 ATOM 2103 C CG1 . ILE A 1 285 ? 20.728 19.497 28.127 1.00 26.15 ? 285 ILE A CG1 1 ATOM 2104 C CG2 . ILE A 1 285 ? 18.797 19.386 29.603 1.00 28.83 ? 285 ILE A CG2 1 ATOM 2105 C CD1 . ILE A 1 285 ? 21.402 18.151 28.343 1.00 26.40 ? 285 ILE A CD1 1 ATOM 2106 N N . VAL A 1 286 ? 19.311 22.269 31.422 1.00 31.35 ? 286 VAL A N 1 ATOM 2107 C CA . VAL A 1 286 ? 18.662 23.029 32.505 1.00 30.02 ? 286 VAL A CA 1 ATOM 2108 C C . VAL A 1 286 ? 18.293 24.507 32.176 1.00 28.11 ? 286 VAL A C 1 ATOM 2109 O O . VAL A 1 286 ? 17.213 24.969 32.573 1.00 29.71 ? 286 VAL A O 1 ATOM 2110 C CB . VAL A 1 286 ? 19.603 22.764 33.732 1.00 32.19 ? 286 VAL A CB 1 ATOM 2111 C CG1 . VAL A 1 286 ? 19.778 23.914 34.721 1.00 33.35 ? 286 VAL A CG1 1 ATOM 2112 C CG2 . VAL A 1 286 ? 19.291 21.406 34.322 1.00 30.57 ? 286 VAL A CG2 1 ATOM 2113 N N . ALA A 1 287 ? 19.123 25.259 31.459 1.00 26.55 ? 287 ALA A N 1 ATOM 2114 C CA . ALA A 1 287 ? 18.823 26.676 31.205 1.00 28.06 ? 287 ALA A CA 1 ATOM 2115 C C . ALA A 1 287 ? 17.962 26.925 29.985 1.00 27.24 ? 287 ALA A C 1 ATOM 2116 O O . ALA A 1 287 ? 17.564 28.030 29.769 1.00 27.71 ? 287 ALA A O 1 ATOM 2117 C CB . ALA A 1 287 ? 20.118 27.478 31.094 1.00 28.73 ? 287 ALA A CB 1 ATOM 2118 N N . GLY A 1 288 ? 17.690 25.912 29.171 1.00 25.10 ? 288 GLY A N 1 ATOM 2119 C CA . GLY A 1 288 ? 17.110 26.096 27.798 1.00 25.02 ? 288 GLY A CA 1 ATOM 2120 C C . GLY A 1 288 ? 15.592 25.977 27.782 1.00 23.97 ? 288 GLY A C 1 ATOM 2121 O O . GLY A 1 288 ? 14.972 25.920 28.819 1.00 24.24 ? 288 GLY A O 1 ATOM 2122 N N . PRO A 1 289 ? 14.987 25.881 26.592 1.00 24.37 ? 289 PRO A N 1 ATOM 2123 C CA . PRO A 1 289 ? 13.541 25.786 26.493 1.00 24.93 ? 289 PRO A CA 1 ATOM 2124 C C . PRO A 1 289 ? 13.081 24.461 27.087 1.00 24.36 ? 289 PRO A C 1 ATOM 2125 O O . PRO A 1 289 ? 13.843 23.485 27.106 1.00 23.24 ? 289 PRO A O 1 ATOM 2126 C CB . PRO A 1 289 ? 13.259 25.838 24.985 1.00 25.64 ? 289 PRO A CB 1 ATOM 2127 C CG . PRO A 1 289 ? 14.529 25.420 24.344 1.00 27.05 ? 289 PRO A CG 1 ATOM 2128 C CD . PRO A 1 289 ? 15.671 25.694 25.305 1.00 25.49 ? 289 PRO A CD 1 ATOM 2129 N N . LYS A 1 290 ? 11.864 24.452 27.605 1.00 23.20 ? 290 LYS A N 1 ATOM 2130 C CA . LYS A 1 290 ? 11.261 23.276 28.146 1.00 23.98 ? 290 LYS A CA 1 ATOM 2131 C C . LYS A 1 290 ? 9.789 23.278 27.823 1.00 23.48 ? 290 LYS A C 1 ATOM 2132 O O . LYS A 1 290 ? 9.198 24.360 27.763 1.00 22.89 ? 290 LYS A O 1 ATOM 2133 C CB . LYS A 1 290 ? 11.388 23.276 29.646 1.00 26.61 ? 290 LYS A CB 1 ATOM 2134 C CG . LYS A 1 290 ? 12.817 23.275 30.184 1.00 29.18 ? 290 LYS A CG 1 ATOM 2135 C CD . LYS A 1 290 ? 12.758 23.658 31.659 1.00 32.28 ? 290 LYS A CD 1 ATOM 2136 C CE . LYS A 1 290 ? 14.101 23.419 32.333 1.00 33.58 ? 290 LYS A CE 1 ATOM 2137 N NZ . LYS A 1 290 ? 14.871 24.641 32.340 1.00 34.08 ? 290 LYS A NZ 1 ATOM 2138 N N . GLN A 1 291 ? 9.226 22.091 27.572 1.00 21.85 ? 291 GLN A N 1 ATOM 2139 C CA . GLN A 1 291 ? 7.800 21.988 27.232 1.00 22.04 ? 291 GLN A CA 1 ATOM 2140 C C . GLN A 1 291 ? 7.149 20.700 27.712 1.00 21.16 ? 291 GLN A C 1 ATOM 2141 O O . GLN A 1 291 ? 7.810 19.803 28.238 1.00 19.16 ? 291 GLN A O 1 ATOM 2142 C CB . GLN A 1 291 ? 7.551 22.225 25.735 1.00 21.82 ? 291 GLN A CB 1 ATOM 2143 C CG . GLN A 1 291 ? 8.330 21.252 24.840 1.00 21.10 ? 291 GLN A CG 1 ATOM 2144 C CD . GLN A 1 291 ? 8.158 21.636 23.395 1.00 21.59 ? 291 GLN A CD 1 ATOM 2145 O OE1 . GLN A 1 291 ? 8.420 22.803 23.007 1.00 22.53 ? 291 GLN A OE1 1 ATOM 2146 N NE2 . GLN A 1 291 ? 7.612 20.729 22.613 1.00 20.49 ? 291 GLN A NE2 1 ATOM 2147 N N . ASN A 1 292 ? 5.810 20.649 27.556 1.00 20.94 ? 292 ASN A N 1 ATOM 2148 C CA . ASN A 1 292 ? 5.027 19.552 28.135 1.00 20.88 ? 292 ASN A CA 1 ATOM 2149 C C . ASN A 1 292 ? 4.613 18.465 27.170 1.00 20.06 ? 292 ASN A C 1 ATOM 2150 O O . ASN A 1 292 ? 3.818 17.595 27.551 1.00 19.81 ? 292 ASN A O 1 ATOM 2151 C CB . ASN A 1 292 ? 3.837 20.097 28.951 1.00 22.42 ? 292 ASN A CB 1 ATOM 2152 C CG . ASN A 1 292 ? 2.751 20.619 28.111 1.00 23.69 ? 292 ASN A CG 1 ATOM 2153 O OD1 . ASN A 1 292 ? 2.803 20.608 26.887 1.00 24.44 ? 292 ASN A OD1 1 ATOM 2154 N ND2 . ASN A 1 292 ? 1.715 21.090 28.774 1.00 24.80 ? 292 ASN A ND2 1 ATOM 2155 N N . CYS A 1 293 ? 5.258 18.424 25.997 1.00 18.72 ? 293 CYS A N 1 ATOM 2156 C CA . CYS A 1 293 ? 4.864 17.533 24.963 1.00 19.75 ? 293 CYS A CA 1 ATOM 2157 C C . CYS A 1 293 ? 5.989 17.428 23.927 1.00 19.06 ? 293 CYS A C 1 ATOM 2158 O O . CYS A 1 293 ? 6.769 18.372 23.760 1.00 20.01 ? 293 CYS A O 1 ATOM 2159 C CB . CYS A 1 293 ? 3.543 18.012 24.236 1.00 19.85 ? 293 CYS A CB 1 ATOM 2160 S SG . CYS A 1 293 ? 3.655 19.760 23.685 1.00 21.54 ? 293 CYS A SG 1 ATOM 2161 N N . GLU A 1 294 ? 6.036 16.294 23.230 1.00 18.49 ? 294 GLU A N 1 ATOM 2162 C CA . GLU A 1 294 ? 6.975 16.095 22.157 1.00 17.59 ? 294 GLU A CA 1 ATOM 2163 C C . GLU A 1 294 ? 6.551 16.910 20.946 1.00 18.58 ? 294 GLU A C 1 ATOM 2164 O O . GLU A 1 294 ? 5.366 16.814 20.475 1.00 18.49 ? 294 GLU A O 1 ATOM 2165 C CB . GLU A 1 294 ? 7.034 14.620 21.756 1.00 17.70 ? 294 GLU A CB 1 ATOM 2166 C CG . GLU A 1 294 ? 8.184 14.322 20.791 1.00 17.10 ? 294 GLU A CG 1 ATOM 2167 C CD . GLU A 1 294 ? 8.195 12.904 20.296 1.00 16.94 ? 294 GLU A CD 1 ATOM 2168 O OE1 . GLU A 1 294 ? 7.610 12.027 20.985 1.00 16.90 ? 294 GLU A OE1 1 ATOM 2169 O OE2 . GLU A 1 294 ? 8.799 12.643 19.212 1.00 15.95 ? 294 GLU A OE2 1 ATOM 2170 N N . PRO A 1 295 ? 7.502 17.681 20.362 1.00 19.10 ? 295 PRO A N 1 ATOM 2171 C CA . PRO A 1 295 ? 7.243 18.372 19.106 1.00 18.42 ? 295 PRO A CA 1 ATOM 2172 C C . PRO A 1 295 ? 6.589 17.456 18.085 1.00 17.79 ? 295 PRO A C 1 ATOM 2173 O O . PRO A 1 295 ? 6.950 16.261 17.997 1.00 17.85 ? 295 PRO A O 1 ATOM 2174 C CB . PRO A 1 295 ? 8.640 18.745 18.621 1.00 18.65 ? 295 PRO A CB 1 ATOM 2175 C CG . PRO A 1 295 ? 9.465 18.827 19.839 1.00 19.21 ? 295 PRO A CG 1 ATOM 2176 C CD . PRO A 1 295 ? 8.930 17.766 20.719 1.00 19.36 ? 295 PRO A CD 1 ATOM 2177 N N . ASP A 1 296 ? 5.674 18.026 17.290 1.00 18.06 ? 296 ASP A N 1 ATOM 2178 C CA . ASP A 1 296 ? 5.067 17.312 16.205 1.00 17.61 ? 296 ASP A CA 1 ATOM 2179 C C . ASP A 1 296 ? 6.095 16.776 15.241 1.00 16.93 ? 296 ASP A C 1 ATOM 2180 O O . ASP A 1 296 ? 7.123 17.423 14.993 1.00 17.02 ? 296 ASP A O 1 ATOM 2181 C CB . ASP A 1 296 ? 4.068 18.193 15.461 1.00 18.29 ? 296 ASP A CB 1 ATOM 2182 C CG . ASP A 1 296 ? 2.859 18.490 16.281 1.00 18.34 ? 296 ASP A CG 1 ATOM 2183 O OD1 . ASP A 1 296 ? 2.580 17.799 17.253 1.00 18.70 ? 296 ASP A OD1 1 ATOM 2184 O OD2 . ASP A 1 296 ? 2.151 19.412 15.937 1.00 19.34 ? 296 ASP A OD2 1 ATOM 2185 N N . LEU A 1 297 ? 5.784 15.622 14.685 1.00 17.11 ? 297 LEU A N 1 ATOM 2186 C CA . LEU A 1 297 ? 6.472 15.179 13.528 1.00 17.85 ? 297 LEU A CA 1 ATOM 2187 C C . LEU A 1 297 ? 6.120 16.055 12.307 1.00 19.21 ? 297 LEU A C 1 ATOM 2188 O O . LEU A 1 297 ? 4.932 16.505 12.121 1.00 20.75 ? 297 LEU A O 1 ATOM 2189 C CB . LEU A 1 297 ? 6.191 13.739 13.211 1.00 17.46 ? 297 LEU A CB 1 ATOM 2190 C CG . LEU A 1 297 ? 6.692 12.731 14.238 1.00 16.92 ? 297 LEU A CG 1 ATOM 2191 C CD1 . LEU A 1 297 ? 6.092 11.389 13.898 1.00 17.32 ? 297 LEU A CD1 1 ATOM 2192 C CD2 . LEU A 1 297 ? 8.193 12.621 14.230 1.00 17.19 ? 297 LEU A CD2 1 ATOM 2193 N N . MET A 1 298 ? 7.148 16.284 11.495 1.00 19.61 ? 298 MET A N 1 ATOM 2194 C CA . MET A 1 298 ? 6.966 16.949 10.263 1.00 21.36 ? 298 MET A CA 1 ATOM 2195 C C . MET A 1 298 ? 6.247 16.010 9.348 1.00 21.09 ? 298 MET A C 1 ATOM 2196 O O . MET A 1 298 ? 6.323 14.822 9.560 1.00 20.04 ? 298 MET A O 1 ATOM 2197 C CB . MET A 1 298 ? 8.282 17.490 9.713 1.00 23.31 ? 298 MET A CB 1 ATOM 2198 C CG . MET A 1 298 ? 8.617 18.759 10.469 1.00 26.13 ? 298 MET A CG 1 ATOM 2199 S SD . MET A 1 298 ? 10.016 19.481 9.741 1.00 32.24 ? 298 MET A SD 1 ATOM 2200 C CE . MET A 1 298 ? 10.538 20.504 11.102 1.00 28.86 ? 298 MET A CE 1 ATOM 2201 N N . PRO A 1 299 ? 5.468 16.551 8.382 1.00 21.27 ? 299 PRO A N 1 ATOM 2202 C CA . PRO A 1 299 ? 4.584 15.728 7.574 1.00 21.52 ? 299 PRO A CA 1 ATOM 2203 C C . PRO A 1 299 ? 5.206 14.497 6.937 1.00 20.60 ? 299 PRO A C 1 ATOM 2204 O O . PRO A 1 299 ? 4.595 13.422 6.950 1.00 22.29 ? 299 PRO A O 1 ATOM 2205 C CB . PRO A 1 299 ? 4.079 16.721 6.508 1.00 22.08 ? 299 PRO A CB 1 ATOM 2206 C CG . PRO A 1 299 ? 4.063 18.021 7.209 1.00 22.14 ? 299 PRO A CG 1 ATOM 2207 C CD . PRO A 1 299 ? 5.275 17.994 8.085 1.00 22.20 ? 299 PRO A CD 1 ATOM 2208 N N . TYR A 1 300 ? 6.446 14.610 6.498 1.00 19.82 ? 300 TYR A N 1 ATOM 2209 C CA . TYR A 1 300 ? 7.203 13.490 5.884 1.00 19.49 ? 300 TYR A CA 1 ATOM 2210 C C . TYR A 1 300 ? 7.410 12.261 6.798 1.00 19.80 ? 300 TYR A C 1 ATOM 2211 O O . TYR A 1 300 ? 7.612 11.127 6.327 1.00 19.00 ? 300 TYR A O 1 ATOM 2212 C CB . TYR A 1 300 ? 8.553 13.980 5.305 1.00 17.76 ? 300 TYR A CB 1 ATOM 2213 C CG . TYR A 1 300 ? 9.575 14.487 6.326 1.00 16.81 ? 300 TYR A CG 1 ATOM 2214 C CD1 . TYR A 1 300 ? 10.399 13.586 7.027 1.00 17.00 ? 300 TYR A CD1 1 ATOM 2215 C CD2 . TYR A 1 300 ? 9.766 15.833 6.531 1.00 16.37 ? 300 TYR A CD2 1 ATOM 2216 C CE1 . TYR A 1 300 ? 11.359 14.004 7.921 1.00 16.68 ? 300 TYR A CE1 1 ATOM 2217 C CE2 . TYR A 1 300 ? 10.755 16.302 7.410 1.00 16.58 ? 300 TYR A CE2 1 ATOM 2218 C CZ . TYR A 1 300 ? 11.534 15.376 8.127 1.00 16.67 ? 300 TYR A CZ 1 ATOM 2219 O OH . TYR A 1 300 ? 12.497 15.795 9.020 1.00 17.11 ? 300 TYR A OH 1 ATOM 2220 N N . ALA A 1 301 ? 7.350 12.471 8.116 1.00 19.40 ? 301 ALA A N 1 ATOM 2221 C CA . ALA A 1 301 ? 7.639 11.376 9.041 1.00 19.22 ? 301 ALA A CA 1 ATOM 2222 C C . ALA A 1 301 ? 6.395 10.750 9.682 1.00 20.34 ? 301 ALA A C 1 ATOM 2223 O O . ALA A 1 301 ? 6.493 9.644 10.250 1.00 19.20 ? 301 ALA A O 1 ATOM 2224 C CB . ALA A 1 301 ? 8.630 11.909 10.121 1.00 18.76 ? 301 ALA A CB 1 ATOM 2225 N N . ARG A 1 302 ? 5.240 11.443 9.585 1.00 20.80 ? 302 ARG A N 1 ATOM 2226 C CA . ARG A 1 302 ? 3.997 11.005 10.264 1.00 20.85 ? 302 ARG A CA 1 ATOM 2227 C C . ARG A 1 302 ? 3.534 9.613 9.890 1.00 21.27 ? 302 ARG A C 1 ATOM 2228 O O . ARG A 1 302 ? 3.151 8.889 10.778 1.00 19.89 ? 302 ARG A O 1 ATOM 2229 C CB . ARG A 1 302 ? 2.870 12.021 10.013 1.00 22.16 ? 302 ARG A CB 1 ATOM 2230 C CG . ARG A 1 302 ? 3.085 13.328 10.750 1.00 22.07 ? 302 ARG A CG 1 ATOM 2231 C CD . ARG A 1 302 ? 1.987 14.385 10.525 1.00 24.52 ? 302 ARG A CD 1 ATOM 2232 N NE . ARG A 1 302 ? 2.582 15.659 10.942 1.00 25.75 ? 302 ARG A NE 1 ATOM 2233 C CZ . ARG A 1 302 ? 2.219 16.899 10.608 1.00 27.52 ? 302 ARG A CZ 1 ATOM 2234 N NH1 . ARG A 1 302 ? 1.149 17.142 9.861 1.00 28.55 ? 302 ARG A NH1 1 ATOM 2235 N NH2 . ARG A 1 302 ? 2.984 17.937 11.027 1.00 27.32 ? 302 ARG A NH2 1 ATOM 2236 N N . PRO A 1 303 ? 3.599 9.191 8.588 1.00 20.88 ? 303 PRO A N 1 ATOM 2237 C CA . PRO A 1 303 ? 3.166 7.821 8.271 1.00 21.55 ? 303 PRO A CA 1 ATOM 2238 C C . PRO A 1 303 ? 3.879 6.780 9.032 1.00 19.73 ? 303 PRO A C 1 ATOM 2239 O O . PRO A 1 303 ? 3.401 5.656 9.131 1.00 19.20 ? 303 PRO A O 1 ATOM 2240 C CB . PRO A 1 303 ? 3.434 7.692 6.754 1.00 22.66 ? 303 PRO A CB 1 ATOM 2241 C CG . PRO A 1 303 ? 3.536 9.115 6.256 1.00 21.89 ? 303 PRO A CG 1 ATOM 2242 C CD . PRO A 1 303 ? 4.098 9.887 7.387 1.00 22.02 ? 303 PRO A CD 1 ATOM 2243 N N . PHE A 1 304 ? 5.025 7.115 9.625 1.00 20.10 ? 304 PHE A N 1 ATOM 2244 C CA . PHE A 1 304 ? 5.895 6.063 10.273 1.00 19.10 ? 304 PHE A CA 1 ATOM 2245 C C . PHE A 1 304 ? 5.719 5.924 11.802 1.00 18.74 ? 304 PHE A C 1 ATOM 2246 O O . PHE A 1 304 ? 6.393 5.103 12.459 1.00 19.59 ? 304 PHE A O 1 ATOM 2247 C CB . PHE A 1 304 ? 7.360 6.285 9.875 1.00 19.00 ? 304 PHE A CB 1 ATOM 2248 C CG . PHE A 1 304 ? 7.604 6.243 8.404 1.00 18.63 ? 304 PHE A CG 1 ATOM 2249 C CD1 . PHE A 1 304 ? 7.708 5.023 7.719 1.00 19.13 ? 304 PHE A CD1 1 ATOM 2250 C CD2 . PHE A 1 304 ? 7.686 7.443 7.668 1.00 18.86 ? 304 PHE A CD2 1 ATOM 2251 C CE1 . PHE A 1 304 ? 7.875 5.033 6.343 1.00 19.09 ? 304 PHE A CE1 1 ATOM 2252 C CE2 . PHE A 1 304 ? 7.910 7.432 6.310 1.00 18.63 ? 304 PHE A CE2 1 ATOM 2253 C CZ . PHE A 1 304 ? 8.031 6.238 5.646 1.00 19.20 ? 304 PHE A CZ 1 ATOM 2254 N N . ALA A 1 305 ? 4.823 6.706 12.378 1.00 18.10 ? 305 ALA A N 1 ATOM 2255 C CA . ALA A 1 305 ? 4.617 6.721 13.797 1.00 17.84 ? 305 ALA A CA 1 ATOM 2256 C C . ALA A 1 305 ? 3.142 6.924 14.136 1.00 18.43 ? 305 ALA A C 1 ATOM 2257 O O . ALA A 1 305 ? 2.818 7.519 15.182 1.00 17.86 ? 305 ALA A O 1 ATOM 2258 C CB . ALA A 1 305 ? 5.443 7.805 14.443 1.00 17.51 ? 305 ALA A CB 1 ATOM 2259 N N . VAL A 1 306 ? 2.284 6.368 13.290 1.00 19.30 ? 306 VAL A N 1 ATOM 2260 C CA . VAL A 1 306 ? 0.854 6.387 13.521 1.00 20.61 ? 306 VAL A CA 1 ATOM 2261 C C . VAL A 1 306 ? 0.551 5.895 14.937 1.00 19.81 ? 306 VAL A C 1 ATOM 2262 O O . VAL A 1 306 ? 1.037 4.886 15.325 1.00 19.99 ? 306 VAL A O 1 ATOM 2263 C CB . VAL A 1 306 ? 0.073 5.626 12.400 1.00 21.41 ? 306 VAL A CB 1 ATOM 2264 C CG1 . VAL A 1 306 ? -1.404 5.553 12.772 1.00 22.24 ? 306 VAL A CG1 1 ATOM 2265 C CG2 . VAL A 1 306 ? 0.243 6.418 11.105 1.00 21.21 ? 306 VAL A CG2 1 ATOM 2266 N N . GLY A 1 307 ? -0.236 6.650 15.715 1.00 19.77 ? 307 GLY A N 1 ATOM 2267 C CA . GLY A 1 307 ? -0.556 6.219 17.062 1.00 19.32 ? 307 GLY A CA 1 ATOM 2268 C C . GLY A 1 307 ? 0.286 6.786 18.194 1.00 19.78 ? 307 GLY A C 1 ATOM 2269 O O . GLY A 1 307 ? -0.145 6.720 19.323 1.00 19.30 ? 307 GLY A O 1 ATOM 2270 N N . LYS A 1 308 ? 1.427 7.424 17.934 1.00 19.73 ? 308 LYS A N 1 ATOM 2271 C CA . LYS A 1 308 ? 2.180 8.055 19.019 1.00 21.11 ? 308 LYS A CA 1 ATOM 2272 C C . LYS A 1 308 ? 1.633 9.429 19.286 1.00 21.67 ? 308 LYS A C 1 ATOM 2273 O O . LYS A 1 308 ? 0.891 9.954 18.469 1.00 21.14 ? 308 LYS A O 1 ATOM 2274 C CB . LYS A 1 308 ? 3.697 8.169 18.685 1.00 22.07 ? 308 LYS A CB 1 ATOM 2275 C CG . LYS A 1 308 ? 4.312 6.946 18.117 1.00 23.56 ? 308 LYS A CG 1 ATOM 2276 C CD . LYS A 1 308 ? 3.868 5.736 18.874 1.00 26.65 ? 308 LYS A CD 1 ATOM 2277 C CE . LYS A 1 308 ? 4.764 5.437 19.997 1.00 28.70 ? 308 LYS A CE 1 ATOM 2278 N NZ . LYS A 1 308 ? 4.559 3.954 20.189 1.00 31.64 ? 308 LYS A NZ 1 ATOM 2279 N N A ARG A 1 309 ? 1.988 10.029 20.422 0.50 21.70 ? 309 ARG A N 1 ATOM 2280 N N B ARG A 1 309 ? 2.085 10.026 20.388 0.50 22.00 ? 309 ARG A N 1 ATOM 2281 C CA A ARG A 1 309 ? 1.374 11.301 20.843 0.50 22.30 ? 309 ARG A CA 1 ATOM 2282 C CA B ARG A 1 309 ? 1.530 11.264 20.931 0.50 22.98 ? 309 ARG A CA 1 ATOM 2283 C C A ARG A 1 309 ? 2.393 12.441 20.868 0.50 21.37 ? 309 ARG A C 1 ATOM 2284 C C B ARG A 1 309 ? 2.527 12.405 20.704 0.50 21.56 ? 309 ARG A C 1 ATOM 2285 O O A ARG A 1 309 ? 3.417 12.352 21.569 0.50 20.87 ? 309 ARG A O 1 ATOM 2286 O O B ARG A 1 309 ? 3.719 12.258 20.970 0.50 20.54 ? 309 ARG A O 1 ATOM 2287 C CB A ARG A 1 309 ? 0.714 11.213 22.229 0.50 23.51 ? 309 ARG A CB 1 ATOM 2288 C CB B ARG A 1 309 ? 1.232 11.093 22.435 0.50 24.95 ? 309 ARG A CB 1 ATOM 2289 C CG A ARG A 1 309 ? 0.302 12.615 22.731 0.50 24.88 ? 309 ARG A CG 1 ATOM 2290 C CG B ARG A 1 309 ? 0.660 12.343 23.127 0.50 27.52 ? 309 ARG A CG 1 ATOM 2291 C CD A ARG A 1 309 ? -0.333 12.595 24.111 0.50 26.04 ? 309 ARG A CD 1 ATOM 2292 C CD B ARG A 1 309 ? 0.125 12.088 24.544 0.50 29.43 ? 309 ARG A CD 1 ATOM 2293 N NE A ARG A 1 309 ? -1.504 11.745 24.075 0.50 27.91 ? 309 ARG A NE 1 ATOM 2294 N NE B ARG A 1 309 ? -1.301 11.782 24.523 0.50 32.15 ? 309 ARG A NE 1 ATOM 2295 C CZ A ARG A 1 309 ? -2.650 12.079 23.507 0.50 28.07 ? 309 ARG A CZ 1 ATOM 2296 C CZ B ARG A 1 309 ? -1.825 10.563 24.647 0.50 33.60 ? 309 ARG A CZ 1 ATOM 2297 N NH1 A ARG A 1 309 ? -2.798 13.257 22.938 0.50 27.20 ? 309 ARG A NH1 1 ATOM 2298 N NH1 B ARG A 1 309 ? -1.054 9.504 24.841 0.50 33.25 ? 309 ARG A NH1 1 ATOM 2299 N NH2 A ARG A 1 309 ? -3.638 11.208 23.516 0.50 29.85 ? 309 ARG A NH2 1 ATOM 2300 N NH2 B ARG A 1 309 ? -3.139 10.406 24.594 0.50 33.70 ? 309 ARG A NH2 1 ATOM 2301 N N . THR A 1 310 ? 2.063 13.532 20.165 1.00 20.71 ? 310 THR A N 1 ATOM 2302 C CA . THR A 1 310 ? 2.885 14.764 20.156 1.00 19.76 ? 310 THR A CA 1 ATOM 2303 C C . THR A 1 310 ? 2.061 15.929 20.656 1.00 20.29 ? 310 THR A C 1 ATOM 2304 O O . THR A 1 310 ? 0.870 15.737 20.993 1.00 20.44 ? 310 THR A O 1 ATOM 2305 C CB . THR A 1 310 ? 3.501 15.013 18.760 1.00 19.92 ? 310 THR A CB 1 ATOM 2306 O OG1 . THR A 1 310 ? 2.486 15.225 17.790 1.00 19.81 ? 310 THR A OG1 1 ATOM 2307 C CG2 . THR A 1 310 ? 4.399 13.828 18.354 1.00 18.99 ? 310 THR A CG2 1 ATOM 2308 N N . CYS A 1 311 ? 2.649 17.148 20.700 1.00 20.28 ? 311 CYS A N 1 ATOM 2309 C CA . CYS A 1 311 ? 1.902 18.385 21.026 1.00 20.23 ? 311 CYS A CA 1 ATOM 2310 C C . CYS A 1 311 ? 0.497 18.520 20.362 1.00 20.90 ? 311 CYS A C 1 ATOM 2311 O O . CYS A 1 311 ? -0.421 18.832 21.055 1.00 20.47 ? 311 CYS A O 1 ATOM 2312 C CB . CYS A 1 311 ? 2.750 19.613 20.731 1.00 20.67 ? 311 CYS A CB 1 ATOM 2313 S SG . CYS A 1 311 ? 4.239 19.631 21.739 1.00 21.06 ? 311 CYS A SG 1 ATOM 2314 N N . SER A 1 312 ? 0.297 18.194 19.087 1.00 20.82 ? 312 SER A N 1 ATOM 2315 C CA . SER A 1 312 ? -1.020 18.332 18.469 1.00 21.30 ? 312 SER A CA 1 ATOM 2316 C C . SER A 1 312 ? -1.941 17.147 18.633 1.00 22.75 ? 312 SER A C 1 ATOM 2317 O O . SER A 1 312 ? -3.059 17.185 18.104 1.00 25.33 ? 312 SER A O 1 ATOM 2318 C CB . SER A 1 312 ? -0.895 18.737 17.015 1.00 21.11 ? 312 SER A CB 1 ATOM 2319 O OG . SER A 1 312 ? -0.231 19.961 16.962 1.00 20.04 ? 312 SER A OG 1 ATOM 2320 N N . GLY A 1 313 ? -1.483 16.110 19.347 1.00 21.61 ? 313 GLY A N 1 ATOM 2321 C CA . GLY A 1 313 ? -2.239 14.939 19.672 1.00 21.66 ? 313 GLY A CA 1 ATOM 2322 C C . GLY A 1 313 ? -1.667 13.689 19.066 1.00 21.31 ? 313 GLY A C 1 ATOM 2323 O O . GLY A 1 313 ? -0.455 13.579 18.831 1.00 20.00 ? 313 GLY A O 1 ATOM 2324 N N . ILE A 1 314 ? -2.548 12.773 18.705 1.00 21.54 ? 314 ILE A N 1 ATOM 2325 C CA . ILE A 1 314 ? -2.081 11.441 18.261 1.00 21.03 ? 314 ILE A CA 1 ATOM 2326 C C . ILE A 1 314 ? -1.769 11.495 16.754 1.00 20.43 ? 314 ILE A C 1 ATOM 2327 O O . ILE A 1 314 ? -2.573 11.953 15.946 1.00 20.95 ? 314 ILE A O 1 ATOM 2328 C CB . ILE A 1 314 ? -3.114 10.336 18.590 1.00 21.88 ? 314 ILE A CB 1 ATOM 2329 C CG1 . ILE A 1 314 ? -3.327 10.284 20.083 1.00 22.36 ? 314 ILE A CG1 1 ATOM 2330 C CG2 . ILE A 1 314 ? -2.610 8.998 18.033 1.00 20.93 ? 314 ILE A CG2 1 ATOM 2331 C CD1 . ILE A 1 314 ? -4.437 9.392 20.544 1.00 23.67 ? 314 ILE A CD1 1 ATOM 2332 N N . VAL A 1 315 ? -0.608 11.014 16.369 1.00 19.54 ? 315 VAL A N 1 ATOM 2333 C CA . VAL A 1 315 ? -0.169 10.997 14.951 1.00 20.02 ? 315 VAL A CA 1 ATOM 2334 C C . VAL A 1 315 ? -1.081 10.115 14.063 1.00 19.94 ? 315 VAL A C 1 ATOM 2335 O O . VAL A 1 315 ? -1.359 8.940 14.415 1.00 19.53 ? 315 VAL A O 1 ATOM 2336 C CB . VAL A 1 315 ? 1.292 10.478 14.832 1.00 20.45 ? 315 VAL A CB 1 ATOM 2337 C CG1 . VAL A 1 315 ? 1.753 10.387 13.362 1.00 21.34 ? 315 VAL A CG1 1 ATOM 2338 C CG2 . VAL A 1 315 ? 2.259 11.302 15.707 1.00 20.57 ? 315 VAL A CG2 1 ATOM 2339 N N . THR A 1 316 ? -1.604 10.725 12.981 1.00 20.53 ? 316 THR A N 1 ATOM 2340 C CA . THR A 1 316 ? -2.380 10.032 11.955 1.00 22.15 ? 316 THR A CA 1 ATOM 2341 C C . THR A 1 316 ? -1.573 9.907 10.614 1.00 23.54 ? 316 THR A C 1 ATOM 2342 O O . THR A 1 316 ? -0.594 10.631 10.439 1.00 23.15 ? 316 THR A O 1 ATOM 2343 C CB . THR A 1 316 ? -3.737 10.709 11.774 1.00 21.46 ? 316 THR A CB 1 ATOM 2344 O OG1 . THR A 1 316 ? -3.536 12.016 11.225 1.00 23.19 ? 316 THR A OG1 1 ATOM 2345 C CG2 . THR A 1 316 ? -4.390 10.914 13.102 1.00 22.76 ? 316 THR A CG2 1 ATOM 2346 N N . PRO A 1 317 ? -1.973 8.969 9.701 1.00 26.02 ? 317 PRO A N 1 ATOM 2347 C CA . PRO A 1 317 ? -1.269 8.731 8.441 1.00 29.27 ? 317 PRO A CA 1 ATOM 2348 C C . PRO A 1 317 ? -0.904 10.029 7.698 1.00 33.67 ? 317 PRO A C 1 ATOM 2349 O O . PRO A 1 317 ? 0.283 10.189 7.300 1.00 35.92 ? 317 PRO A O 1 ATOM 2350 C CB . PRO A 1 317 ? -2.252 7.839 7.648 1.00 29.50 ? 317 PRO A CB 1 ATOM 2351 C CG . PRO A 1 317 ? -2.903 7.001 8.725 1.00 29.26 ? 317 PRO A CG 1 ATOM 2352 C CD . PRO A 1 317 ? -3.049 7.977 9.903 1.00 28.39 ? 317 PRO A CD 1 ATOM 2353 O OXT . PRO A 1 317 ? -1.727 10.999 7.643 1.00 33.25 ? 317 PRO A OXT 1 HETATM 2354 C C1 . NAG B 2 . ? 13.278 27.002 19.381 1.00 26.24 ? 800 NAG A C1 1 HETATM 2355 C C2 . NAG B 2 . ? 13.647 28.298 18.683 1.00 29.38 ? 800 NAG A C2 1 HETATM 2356 C C3 . NAG B 2 . ? 12.501 29.314 18.778 1.00 32.04 ? 800 NAG A C3 1 HETATM 2357 C C4 . NAG B 2 . ? 11.181 28.700 18.335 1.00 32.78 ? 800 NAG A C4 1 HETATM 2358 C C5 . NAG B 2 . ? 10.906 27.379 19.028 1.00 32.36 ? 800 NAG A C5 1 HETATM 2359 C C6 . NAG B 2 . ? 9.617 26.712 18.513 1.00 30.72 ? 800 NAG A C6 1 HETATM 2360 C C7 . NAG B 2 . ? 15.943 29.152 18.713 1.00 31.23 ? 800 NAG A C7 1 HETATM 2361 C C8 . NAG B 2 . ? 17.037 29.657 19.603 1.00 31.55 ? 800 NAG A C8 1 HETATM 2362 N N2 . NAG B 2 . ? 14.827 28.796 19.344 1.00 30.82 ? 800 NAG A N2 1 HETATM 2363 O O3 . NAG B 2 . ? 12.824 30.462 17.981 1.00 31.42 ? 800 NAG A O3 1 HETATM 2364 O O4 . NAG B 2 . ? 10.117 29.584 18.686 1.00 40.74 ? 800 NAG A O4 1 HETATM 2365 O O5 . NAG B 2 . ? 12.053 26.557 18.806 1.00 26.82 ? 800 NAG A O5 1 HETATM 2366 O O6 . NAG B 2 . ? 9.762 26.287 17.156 1.00 31.25 ? 800 NAG A O6 1 HETATM 2367 O O7 . NAG B 2 . ? 16.087 29.094 17.509 1.00 35.20 ? 800 NAG A O7 1 HETATM 2368 C C1 . NAG C 2 . ? 9.492 30.106 17.503 1.00 49.87 ? 801 NAG A C1 1 HETATM 2369 C C2 . NAG C 2 . ? 8.270 30.939 17.874 1.00 54.68 ? 801 NAG A C2 1 HETATM 2370 C C3 . NAG C 2 . ? 7.688 31.633 16.631 1.00 61.02 ? 801 NAG A C3 1 HETATM 2371 C C4 . NAG C 2 . ? 8.795 32.356 15.869 1.00 64.68 ? 801 NAG A C4 1 HETATM 2372 C C5 . NAG C 2 . ? 9.844 31.309 15.475 1.00 67.74 ? 801 NAG A C5 1 HETATM 2373 C C6 . NAG C 2 . ? 10.935 31.792 14.512 1.00 71.44 ? 801 NAG A C6 1 HETATM 2374 C C7 . NAG C 2 . ? 7.280 29.599 19.747 1.00 55.98 ? 801 NAG A C7 1 HETATM 2375 C C8 . NAG C 2 . ? 8.171 30.157 20.840 1.00 55.27 ? 801 NAG A C8 1 HETATM 2376 N N2 . NAG C 2 . ? 7.344 29.991 18.463 1.00 55.96 ? 801 NAG A N2 1 HETATM 2377 O O3 . NAG C 2 . ? 6.655 32.573 16.949 1.00 63.50 ? 801 NAG A O3 1 HETATM 2378 O O4 . NAG C 2 . ? 8.250 33.036 14.733 1.00 69.35 ? 801 NAG A O4 1 HETATM 2379 O O5 . NAG C 2 . ? 10.421 30.849 16.706 1.00 58.83 ? 801 NAG A O5 1 HETATM 2380 O O6 . NAG C 2 . ? 11.874 32.642 15.179 1.00 79.09 ? 801 NAG A O6 1 HETATM 2381 O O7 . NAG C 2 . ? 6.447 28.760 20.022 1.00 59.12 ? 801 NAG A O7 1 HETATM 2382 O O . HOH D 3 . ? 30.339 27.584 13.117 1.00 34.73 ? 901 HOH A O 1 HETATM 2383 O O . HOH D 3 . ? 50.416 12.197 21.436 1.00 38.18 ? 902 HOH A O 1 HETATM 2384 O O . HOH D 3 . ? 36.406 -5.702 11.867 1.00 46.02 ? 903 HOH A O 1 HETATM 2385 O O . HOH D 3 . ? 30.111 28.933 1.860 1.00 39.07 ? 904 HOH A O 1 HETATM 2386 O O . HOH D 3 . ? 6.011 4.424 21.995 1.00 43.07 ? 905 HOH A O 1 HETATM 2387 O O . HOH D 3 . ? 22.870 14.226 23.095 1.00 36.53 ? 906 HOH A O 1 HETATM 2388 O O . HOH D 3 . ? 17.048 27.411 13.440 1.00 28.92 ? 907 HOH A O 1 HETATM 2389 O O . HOH D 3 . ? 46.001 8.605 10.050 1.00 44.17 ? 908 HOH A O 1 HETATM 2390 O O . HOH D 3 . ? 36.643 10.153 3.703 1.00 24.49 ? 909 HOH A O 1 HETATM 2391 O O . HOH D 3 . ? 38.787 25.480 14.989 1.00 29.47 ? 910 HOH A O 1 HETATM 2392 O O . HOH D 3 . ? 47.139 14.057 16.659 1.00 21.81 ? 911 HOH A O 1 HETATM 2393 O O . HOH D 3 . ? -4.951 13.792 21.838 1.00 34.93 ? 912 HOH A O 1 HETATM 2394 O O . HOH D 3 . ? 20.930 -3.100 25.865 1.00 16.79 ? 913 HOH A O 1 HETATM 2395 O O . HOH D 3 . ? 1.362 9.133 25.317 1.00 61.68 ? 914 HOH A O 1 HETATM 2396 O O . HOH D 3 . ? 35.913 27.169 19.768 1.00 28.04 ? 915 HOH A O 1 HETATM 2397 O O . HOH D 3 . ? 29.015 24.605 -1.418 1.00 21.54 ? 916 HOH A O 1 HETATM 2398 O O . HOH D 3 . ? 32.345 -1.965 32.897 1.00 43.91 ? 917 HOH A O 1 HETATM 2399 O O . HOH D 3 . ? 35.108 -4.400 17.577 1.00 39.17 ? 918 HOH A O 1 HETATM 2400 O O . HOH D 3 . ? 7.162 22.987 30.486 1.00 38.30 ? 919 HOH A O 1 HETATM 2401 O O . HOH D 3 . ? 26.357 24.781 26.166 1.00 59.18 ? 920 HOH A O 1 HETATM 2402 O O . HOH D 3 . ? 15.835 22.443 28.399 1.00 32.23 ? 921 HOH A O 1 HETATM 2403 O O . HOH D 3 . ? 27.466 7.083 0.040 1.00 26.96 ? 922 HOH A O 1 HETATM 2404 O O . HOH D 3 . ? 26.760 25.244 29.829 1.00 34.26 ? 923 HOH A O 1 HETATM 2405 O O . HOH D 3 . ? 28.800 29.603 6.957 1.00 42.30 ? 924 HOH A O 1 HETATM 2406 O O . HOH D 3 . ? 38.192 17.999 33.932 1.00 24.34 ? 925 HOH A O 1 HETATM 2407 O O . HOH D 3 . ? 13.342 18.199 8.818 1.00 14.94 ? 926 HOH A O 1 HETATM 2408 O O . HOH D 3 . ? 37.454 9.693 6.218 1.00 25.69 ? 927 HOH A O 1 HETATM 2409 O O . HOH D 3 . ? 29.770 -6.694 26.708 1.00 29.61 ? 928 HOH A O 1 HETATM 2410 O O . HOH D 3 . ? -2.654 7.830 23.718 1.00 45.16 ? 929 HOH A O 1 HETATM 2411 O O . HOH D 3 . ? 11.887 6.178 30.582 1.00 32.39 ? 930 HOH A O 1 HETATM 2412 O O . HOH D 3 . ? 33.285 28.870 7.666 1.00 22.32 ? 931 HOH A O 1 HETATM 2413 O O . HOH D 3 . ? 20.277 20.137 1.166 1.00 19.14 ? 932 HOH A O 1 HETATM 2414 O O . HOH D 3 . ? -1.948 12.872 5.863 1.00 40.16 ? 933 HOH A O 1 HETATM 2415 O O . HOH D 3 . ? 22.937 31.717 2.744 1.00 43.22 ? 934 HOH A O 1 HETATM 2416 O O . HOH D 3 . ? 35.587 11.565 -0.811 1.00 32.81 ? 935 HOH A O 1 HETATM 2417 O O . HOH D 3 . ? 34.603 -3.090 7.341 1.00 49.56 ? 936 HOH A O 1 HETATM 2418 O O . HOH D 3 . ? 19.749 1.649 17.497 1.00 17.55 ? 937 HOH A O 1 HETATM 2419 O O . HOH D 3 . ? 10.349 24.140 11.893 1.00 36.90 ? 938 HOH A O 1 HETATM 2420 O O . HOH D 3 . ? 21.889 13.285 -4.436 1.00 42.85 ? 939 HOH A O 1 HETATM 2421 O O . HOH D 3 . ? 29.032 27.355 16.978 1.00 24.92 ? 940 HOH A O 1 HETATM 2422 O O . HOH D 3 . ? 26.858 -5.626 11.696 1.00 27.23 ? 941 HOH A O 1 HETATM 2423 O O . HOH D 3 . ? 20.511 -9.008 23.540 1.00 25.86 ? 942 HOH A O 1 HETATM 2424 O O . HOH D 3 . ? 38.912 17.774 -0.632 1.00 39.51 ? 943 HOH A O 1 HETATM 2425 O O . HOH D 3 . ? 10.185 24.239 24.313 1.00 24.76 ? 944 HOH A O 1 HETATM 2426 O O . HOH D 3 . ? -5.133 15.853 17.204 1.00 32.45 ? 945 HOH A O 1 HETATM 2427 O O . HOH D 3 . ? 31.197 31.151 3.405 1.00 54.46 ? 946 HOH A O 1 HETATM 2428 O O . HOH D 3 . ? -4.047 11.871 8.519 1.00 28.63 ? 947 HOH A O 1 HETATM 2429 O O . HOH D 3 . ? 35.160 12.672 28.426 1.00 22.66 ? 948 HOH A O 1 HETATM 2430 O O . HOH D 3 . ? 10.410 4.487 19.866 1.00 37.82 ? 949 HOH A O 1 HETATM 2431 O O . HOH D 3 . ? 27.931 4.941 25.135 1.00 25.41 ? 950 HOH A O 1 HETATM 2432 O O . HOH D 3 . ? 21.888 10.129 -2.735 1.00 35.98 ? 951 HOH A O 1 HETATM 2433 O O . HOH D 3 . ? 13.563 23.742 1.585 1.00 29.00 ? 952 HOH A O 1 HETATM 2434 O O . HOH D 3 . ? 10.166 22.731 14.751 1.00 20.85 ? 953 HOH A O 1 HETATM 2435 O O . HOH D 3 . ? 44.843 23.391 24.403 1.00 42.97 ? 954 HOH A O 1 HETATM 2436 O O . HOH D 3 . ? 16.005 -1.870 10.092 1.00 27.83 ? 955 HOH A O 1 HETATM 2437 O O . HOH D 3 . ? 7.989 19.907 14.793 1.00 19.52 ? 956 HOH A O 1 HETATM 2438 O O . HOH D 3 . ? 26.628 26.882 3.304 1.00 37.66 ? 957 HOH A O 1 HETATM 2439 O O . HOH D 3 . ? 15.141 27.734 15.445 1.00 38.80 ? 958 HOH A O 1 HETATM 2440 O O . HOH D 3 . ? 30.740 -4.758 20.107 1.00 17.09 ? 959 HOH A O 1 HETATM 2441 O O . HOH D 3 . ? 14.334 26.441 3.145 1.00 28.46 ? 960 HOH A O 1 HETATM 2442 O O . HOH D 3 . ? 21.696 12.201 24.534 1.00 44.53 ? 961 HOH A O 1 HETATM 2443 O O . HOH D 3 . ? 20.485 22.997 0.866 1.00 23.37 ? 962 HOH A O 1 HETATM 2444 O O . HOH D 3 . ? 0.738 11.989 5.401 1.00 37.57 ? 963 HOH A O 1 HETATM 2445 O O . HOH D 3 . ? 24.021 4.901 8.342 1.00 16.52 ? 964 HOH A O 1 HETATM 2446 O O . HOH D 3 . ? 9.385 1.317 6.120 1.00 33.47 ? 965 HOH A O 1 HETATM 2447 O O . HOH D 3 . ? 34.409 20.758 29.021 1.00 25.29 ? 966 HOH A O 1 HETATM 2448 O O . HOH D 3 . ? 32.023 -1.595 5.101 1.00 41.60 ? 967 HOH A O 1 HETATM 2449 O O . HOH D 3 . ? 45.163 16.910 31.195 1.00 42.08 ? 968 HOH A O 1 HETATM 2450 O O . HOH D 3 . ? 39.636 -7.725 22.793 1.00 36.14 ? 969 HOH A O 1 HETATM 2451 O O . HOH D 3 . ? 3.382 3.653 14.928 1.00 33.85 ? 970 HOH A O 1 HETATM 2452 O O . HOH D 3 . ? 15.044 16.141 -3.383 1.00 25.33 ? 971 HOH A O 1 HETATM 2453 O O . HOH D 3 . ? 31.682 12.648 33.176 1.00 21.71 ? 972 HOH A O 1 HETATM 2454 O O . HOH D 3 . ? 32.569 4.521 9.889 1.00 20.71 ? 973 HOH A O 1 HETATM 2455 O O . HOH D 3 . ? 27.177 -4.372 19.770 1.00 22.14 ? 974 HOH A O 1 HETATM 2456 O O . HOH D 3 . ? 41.489 23.195 9.267 1.00 41.42 ? 975 HOH A O 1 HETATM 2457 O O . HOH D 3 . ? -0.256 15.405 23.420 1.00 29.40 ? 976 HOH A O 1 HETATM 2458 O O . HOH D 3 . ? 34.231 30.768 -1.132 1.00 50.44 ? 977 HOH A O 1 HETATM 2459 O O . HOH D 3 . ? 39.644 -5.824 18.402 1.00 41.92 ? 978 HOH A O 1 HETATM 2460 O O . HOH D 3 . ? -0.060 20.513 23.133 1.00 29.44 ? 979 HOH A O 1 HETATM 2461 O O . HOH D 3 . ? 21.211 29.560 12.254 1.00 27.17 ? 980 HOH A O 1 HETATM 2462 O O . HOH D 3 . ? 42.472 22.325 6.745 1.00 28.75 ? 981 HOH A O 1 HETATM 2463 O O . HOH D 3 . ? 16.263 -1.702 23.430 1.00 21.60 ? 982 HOH A O 1 HETATM 2464 O O . HOH D 3 . ? 34.936 24.817 23.649 1.00 30.49 ? 983 HOH A O 1 HETATM 2465 O O . HOH D 3 . ? 37.097 2.052 -0.795 1.00 37.68 ? 984 HOH A O 1 HETATM 2466 O O . HOH D 3 . ? 15.814 12.829 -2.743 1.00 22.11 ? 985 HOH A O 1 HETATM 2467 O O . HOH D 3 . ? 12.663 17.392 -4.938 1.00 41.74 ? 986 HOH A O 1 HETATM 2468 O O . HOH D 3 . ? 37.428 -5.996 17.357 1.00 49.08 ? 987 HOH A O 1 HETATM 2469 O O . HOH D 3 . ? 38.282 10.215 28.067 1.00 21.19 ? 988 HOH A O 1 HETATM 2470 O O . HOH D 3 . ? 43.530 3.563 14.563 1.00 25.25 ? 989 HOH A O 1 HETATM 2471 O O . HOH D 3 . ? 23.751 24.075 7.388 1.00 21.78 ? 990 HOH A O 1 HETATM 2472 O O . HOH D 3 . ? 11.775 10.867 0.399 1.00 25.74 ? 991 HOH A O 1 HETATM 2473 O O . HOH D 3 . ? 17.740 18.948 0.615 1.00 23.61 ? 992 HOH A O 1 HETATM 2474 O O . HOH D 3 . ? 8.295 -0.620 15.061 1.00 17.61 ? 993 HOH A O 1 HETATM 2475 O O . HOH D 3 . ? 18.450 22.930 18.566 1.00 15.71 ? 994 HOH A O 1 HETATM 2476 O O . HOH D 3 . ? 32.333 21.794 26.412 1.00 30.11 ? 995 HOH A O 1 HETATM 2477 O O . HOH D 3 . ? 15.486 20.071 1.690 1.00 17.65 ? 996 HOH A O 1 HETATM 2478 O O . HOH D 3 . ? 14.534 4.198 16.756 1.00 15.95 ? 997 HOH A O 1 HETATM 2479 O O . HOH D 3 . ? 24.321 23.884 18.731 1.00 20.05 ? 998 HOH A O 1 HETATM 2480 O O . HOH D 3 . ? 45.554 18.926 20.156 1.00 35.35 ? 999 HOH A O 1 HETATM 2481 O O . HOH D 3 . ? 5.546 8.245 22.485 1.00 36.33 ? 1000 HOH A O 1 HETATM 2482 O O . HOH D 3 . ? 37.377 -6.299 32.329 1.00 32.85 ? 1001 HOH A O 1 HETATM 2483 O O . HOH D 3 . ? 41.558 -1.410 29.954 1.00 42.63 ? 1002 HOH A O 1 HETATM 2484 O O . HOH D 3 . ? 0.498 19.829 25.612 1.00 24.99 ? 1003 HOH A O 1 HETATM 2485 O O . HOH D 3 . ? 13.048 3.767 20.980 1.00 23.97 ? 1004 HOH A O 1 HETATM 2486 O O . HOH D 3 . ? 49.656 7.542 21.470 1.00 39.74 ? 1005 HOH A O 1 HETATM 2487 O O . HOH D 3 . ? 14.051 0.054 4.916 1.00 29.15 ? 1006 HOH A O 1 HETATM 2488 O O . HOH D 3 . ? 11.317 11.704 2.926 1.00 20.29 ? 1007 HOH A O 1 HETATM 2489 O O . HOH D 3 . ? 8.940 14.517 17.201 1.00 11.12 ? 1008 HOH A O 1 HETATM 2490 O O . HOH D 3 . ? 17.156 24.684 15.656 1.00 35.17 ? 1009 HOH A O 1 HETATM 2491 O O . HOH D 3 . ? 21.854 17.122 -1.413 1.00 17.78 ? 1010 HOH A O 1 HETATM 2492 O O . HOH D 3 . ? 29.476 -0.966 5.215 1.00 39.03 ? 1011 HOH A O 1 HETATM 2493 O O . HOH D 3 . ? 17.978 -4.605 7.736 1.00 45.48 ? 1012 HOH A O 1 HETATM 2494 O O . HOH D 3 . ? 34.790 15.884 0.463 1.00 25.45 ? 1013 HOH A O 1 HETATM 2495 O O . HOH D 3 . ? 29.816 -4.886 14.417 1.00 21.88 ? 1014 HOH A O 1 HETATM 2496 O O . HOH D 3 . ? 11.746 24.587 16.221 1.00 28.57 ? 1015 HOH A O 1 HETATM 2497 O O . HOH D 3 . ? 1.023 5.235 7.763 1.00 35.99 ? 1016 HOH A O 1 HETATM 2498 O O . HOH D 3 . ? 14.800 0.303 11.210 1.00 15.79 ? 1017 HOH A O 1 HETATM 2499 O O . HOH D 3 . ? 19.776 -1.692 14.917 1.00 36.23 ? 1018 HOH A O 1 HETATM 2500 O O . HOH D 3 . ? 6.401 0.581 16.336 1.00 29.35 ? 1019 HOH A O 1 HETATM 2501 O O . HOH D 3 . ? 41.754 1.862 8.874 1.00 31.59 ? 1020 HOH A O 1 HETATM 2502 O O . HOH D 3 . ? 35.043 20.441 23.857 1.00 20.15 ? 1021 HOH A O 1 HETATM 2503 O O . HOH D 3 . ? 8.940 12.393 -2.636 1.00 26.54 ? 1022 HOH A O 1 HETATM 2504 O O . HOH D 3 . ? 47.094 22.647 27.450 1.00 35.83 ? 1023 HOH A O 1 HETATM 2505 O O . HOH D 3 . ? 22.458 16.309 -5.625 1.00 44.31 ? 1024 HOH A O 1 HETATM 2506 O O . HOH D 3 . ? 35.490 8.893 -0.356 1.00 37.05 ? 1025 HOH A O 1 HETATM 2507 O O . HOH D 3 . ? 8.830 11.972 36.668 1.00 22.80 ? 1026 HOH A O 1 HETATM 2508 O O . HOH D 3 . ? -0.429 22.183 18.641 1.00 39.81 ? 1027 HOH A O 1 HETATM 2509 O O . HOH D 3 . ? 39.797 -6.215 10.629 1.00 32.09 ? 1028 HOH A O 1 HETATM 2510 O O . HOH D 3 . ? 36.149 14.937 2.739 1.00 22.66 ? 1029 HOH A O 1 HETATM 2511 O O . HOH D 3 . ? 16.294 -0.220 6.272 1.00 24.37 ? 1030 HOH A O 1 HETATM 2512 O O . HOH D 3 . ? 20.653 26.890 27.289 1.00 35.30 ? 1031 HOH A O 1 HETATM 2513 O O . HOH D 3 . ? 26.954 19.407 -5.797 1.00 34.60 ? 1032 HOH A O 1 HETATM 2514 O O . HOH D 3 . ? 25.662 19.086 -3.267 1.00 17.92 ? 1033 HOH A O 1 HETATM 2515 O O . HOH D 3 . ? 0.689 19.395 8.259 1.00 43.36 ? 1034 HOH A O 1 HETATM 2516 O O . HOH D 3 . ? 37.166 28.813 1.678 1.00 25.02 ? 1035 HOH A O 1 HETATM 2517 O O . HOH D 3 . ? 28.432 26.721 13.364 1.00 30.62 ? 1036 HOH A O 1 HETATM 2518 O O . HOH D 3 . ? 49.535 15.468 24.109 1.00 49.26 ? 1037 HOH A O 1 HETATM 2519 O O . HOH D 3 . ? 11.568 25.703 21.911 1.00 29.09 ? 1038 HOH A O 1 HETATM 2520 O O . HOH D 3 . ? 10.562 3.553 -0.644 1.00 49.96 ? 1039 HOH A O 1 HETATM 2521 O O . HOH D 3 . ? 34.327 -6.077 10.631 1.00 50.40 ? 1040 HOH A O 1 HETATM 2522 O O . HOH D 3 . ? 23.128 27.543 20.326 1.00 31.87 ? 1041 HOH A O 1 HETATM 2523 O O . HOH D 3 . ? 5.095 20.715 17.937 1.00 25.04 ? 1042 HOH A O 1 HETATM 2524 O O . HOH D 3 . ? 8.606 11.574 23.628 1.00 33.96 ? 1043 HOH A O 1 HETATM 2525 O O . HOH D 3 . ? 42.070 22.444 15.401 1.00 26.32 ? 1044 HOH A O 1 HETATM 2526 O O . HOH D 3 . ? 26.521 10.045 17.966 1.00 16.44 ? 1045 HOH A O 1 HETATM 2527 O O . HOH D 3 . ? 9.533 24.153 20.770 1.00 37.17 ? 1046 HOH A O 1 HETATM 2528 O O . HOH D 3 . ? 3.182 14.532 15.061 1.00 18.93 ? 1047 HOH A O 1 HETATM 2529 O O . HOH D 3 . ? 38.608 10.150 21.015 1.00 35.36 ? 1048 HOH A O 1 HETATM 2530 O O . HOH D 3 . ? 28.394 22.911 26.323 1.00 50.51 ? 1049 HOH A O 1 HETATM 2531 O O . HOH D 3 . ? 17.363 31.427 2.358 1.00 32.71 ? 1050 HOH A O 1 HETATM 2532 O O . HOH D 3 . ? 34.456 12.261 33.009 1.00 32.07 ? 1051 HOH A O 1 HETATM 2533 O O . HOH D 3 . ? 19.763 0.952 4.589 1.00 40.06 ? 1052 HOH A O 1 HETATM 2534 O O . HOH D 3 . ? 14.334 29.045 22.152 1.00 40.23 ? 1053 HOH A O 1 HETATM 2535 O O . HOH D 3 . ? 2.885 4.099 11.478 1.00 25.06 ? 1054 HOH A O 1 HETATM 2536 O O . HOH D 3 . ? 9.267 6.897 -0.573 1.00 43.07 ? 1055 HOH A O 1 HETATM 2537 O O . HOH D 3 . ? 22.778 -1.813 5.466 1.00 28.42 ? 1056 HOH A O 1 HETATM 2538 O O . HOH D 3 . ? 6.004 20.419 36.516 1.00 58.39 ? 1057 HOH A O 1 HETATM 2539 O O . HOH D 3 . ? 47.008 11.733 12.561 1.00 44.25 ? 1058 HOH A O 1 HETATM 2540 O O . HOH D 3 . ? 40.453 23.135 29.997 1.00 32.81 ? 1059 HOH A O 1 HETATM 2541 O O . HOH D 3 . ? 6.822 21.703 20.027 1.00 21.22 ? 1060 HOH A O 1 HETATM 2542 O O . HOH D 3 . ? 45.746 10.169 20.720 1.00 23.02 ? 1061 HOH A O 1 HETATM 2543 O O . HOH D 3 . ? 31.435 27.981 15.225 1.00 20.56 ? 1062 HOH A O 1 HETATM 2544 O O . HOH D 3 . ? 15.536 18.913 29.035 1.00 33.59 ? 1063 HOH A O 1 HETATM 2545 O O . HOH D 3 . ? 29.756 20.371 26.793 1.00 24.27 ? 1064 HOH A O 1 HETATM 2546 O O . HOH D 3 . ? -0.697 13.332 9.425 1.00 45.41 ? 1065 HOH A O 1 HETATM 2547 O O . HOH D 3 . ? 1.296 18.047 13.538 1.00 44.92 ? 1066 HOH A O 1 HETATM 2548 O O . HOH D 3 . ? 38.262 1.526 32.747 1.00 28.53 ? 1067 HOH A O 1 HETATM 2549 O O . HOH D 3 . ? 43.870 14.196 4.824 1.00 46.98 ? 1068 HOH A O 1 HETATM 2550 O O . HOH D 3 . ? 40.495 5.046 2.838 1.00 41.00 ? 1069 HOH A O 1 HETATM 2551 O O . HOH D 3 . ? 24.200 -6.292 12.273 1.00 32.39 ? 1070 HOH A O 1 HETATM 2552 O O . HOH D 3 . ? 22.799 27.086 33.274 1.00 34.16 ? 1071 HOH A O 1 HETATM 2553 O O . HOH D 3 . ? 32.249 14.582 31.425 1.00 21.62 ? 1072 HOH A O 1 HETATM 2554 O O . HOH D 3 . ? 4.576 23.239 27.052 1.00 22.89 ? 1073 HOH A O 1 HETATM 2555 O O . HOH D 3 . ? 24.048 28.069 18.130 1.00 34.02 ? 1074 HOH A O 1 HETATM 2556 O O . HOH D 3 . ? 34.732 8.348 30.825 1.00 18.20 ? 1075 HOH A O 1 HETATM 2557 O O . HOH D 3 . ? 27.475 28.755 26.086 1.00 32.66 ? 1076 HOH A O 1 HETATM 2558 O O . HOH D 3 . ? 28.131 -10.219 23.748 1.00 40.68 ? 1077 HOH A O 1 HETATM 2559 O O . HOH D 3 . ? 42.398 19.060 4.331 1.00 33.82 ? 1078 HOH A O 1 HETATM 2560 O O . HOH D 3 . ? 46.286 3.317 22.000 1.00 29.15 ? 1079 HOH A O 1 HETATM 2561 O O . HOH D 3 . ? 18.204 -2.326 16.298 1.00 27.43 ? 1080 HOH A O 1 HETATM 2562 O O . HOH D 3 . ? 27.278 -5.646 15.163 1.00 32.15 ? 1081 HOH A O 1 HETATM 2563 O O . HOH D 3 . ? -5.369 13.535 19.009 1.00 32.99 ? 1082 HOH A O 1 HETATM 2564 O O . HOH D 3 . ? 34.092 11.090 -3.368 1.00 39.08 ? 1083 HOH A O 1 HETATM 2565 O O . HOH D 3 . ? 25.978 0.446 33.251 1.00 47.80 ? 1084 HOH A O 1 HETATM 2566 O O . HOH D 3 . ? 27.735 28.280 5.346 1.00 40.69 ? 1085 HOH A O 1 HETATM 2567 O O . HOH D 3 . ? 3.665 14.504 23.559 1.00 23.56 ? 1086 HOH A O 1 HETATM 2568 O O . HOH D 3 . ? 13.454 2.660 18.693 1.00 19.16 ? 1087 HOH A O 1 HETATM 2569 O O . HOH D 3 . ? 47.034 2.051 18.110 1.00 42.35 ? 1088 HOH A O 1 HETATM 2570 O O . HOH D 3 . ? 24.730 14.509 24.982 1.00 42.79 ? 1089 HOH A O 1 HETATM 2571 O O . HOH D 3 . ? 32.419 -5.372 16.159 1.00 38.51 ? 1090 HOH A O 1 HETATM 2572 O O . HOH D 3 . ? 41.482 -0.205 5.155 1.00 30.95 ? 1091 HOH A O 1 HETATM 2573 O O . HOH D 3 . ? 47.119 1.974 8.821 1.00 47.30 ? 1092 HOH A O 1 HETATM 2574 O O . HOH D 3 . ? 39.885 23.817 3.651 1.00 24.59 ? 1093 HOH A O 1 HETATM 2575 O O . HOH D 3 . ? 8.143 8.141 25.239 1.00 43.07 ? 1094 HOH A O 1 HETATM 2576 O O . HOH D 3 . ? 44.440 21.132 3.028 1.00 38.78 ? 1095 HOH A O 1 HETATM 2577 O O . HOH D 3 . ? 11.882 23.340 18.772 1.00 23.21 ? 1096 HOH A O 1 HETATM 2578 O O . HOH D 3 . ? 45.082 12.974 15.501 1.00 28.74 ? 1097 HOH A O 1 HETATM 2579 O O . HOH D 3 . ? -0.708 13.546 12.533 1.00 27.60 ? 1098 HOH A O 1 HETATM 2580 O O . HOH D 3 . ? 45.794 10.588 28.756 1.00 40.93 ? 1099 HOH A O 1 HETATM 2581 O O . HOH D 3 . ? 12.341 19.967 7.138 1.00 23.06 ? 1100 HOH A O 1 HETATM 2582 O O . HOH D 3 . ? 9.515 10.119 4.242 1.00 23.28 ? 1101 HOH A O 1 HETATM 2583 O O . HOH D 3 . ? 14.445 25.349 16.060 1.00 30.03 ? 1102 HOH A O 1 HETATM 2584 O O . HOH D 3 . ? 41.052 23.213 22.283 1.00 39.80 ? 1103 HOH A O 1 HETATM 2585 O O . HOH D 3 . ? 39.405 -2.321 33.807 1.00 54.19 ? 1104 HOH A O 1 HETATM 2586 O O . HOH D 3 . ? 41.566 15.134 32.590 1.00 39.60 ? 1105 HOH A O 1 HETATM 2587 O O . HOH D 3 . ? 8.634 9.776 -0.133 1.00 36.08 ? 1106 HOH A O 1 HETATM 2588 O O . HOH D 3 . ? 14.881 3.620 -0.726 1.00 46.57 ? 1107 HOH A O 1 HETATM 2589 O O . HOH D 3 . ? -0.098 15.213 16.208 1.00 29.18 ? 1108 HOH A O 1 HETATM 2590 O O . HOH D 3 . ? 19.196 4.678 -0.995 1.00 34.15 ? 1109 HOH A O 1 HETATM 2591 O O . HOH D 3 . ? 34.766 11.133 30.549 1.00 27.26 ? 1110 HOH A O 1 HETATM 2592 O O . HOH D 3 . ? 10.631 2.944 4.100 1.00 30.91 ? 1111 HOH A O 1 HETATM 2593 O O . HOH D 3 . ? 24.833 -8.483 17.419 1.00 41.18 ? 1112 HOH A O 1 HETATM 2594 O O . HOH D 3 . ? -0.767 2.421 14.921 1.00 28.68 ? 1113 HOH A O 1 HETATM 2595 O O . HOH D 3 . ? 46.999 11.913 6.551 1.00 35.63 ? 1114 HOH A O 1 HETATM 2596 O O . HOH D 3 . ? 47.296 4.418 25.261 1.00 30.98 ? 1115 HOH A O 1 HETATM 2597 O O . HOH D 3 . ? 31.496 -8.558 20.257 1.00 40.88 ? 1116 HOH A O 1 HETATM 2598 O O . HOH D 3 . ? 1.482 13.801 6.904 1.00 42.35 ? 1117 HOH A O 1 HETATM 2599 O O . HOH D 3 . ? 2.923 7.968 22.620 1.00 31.44 ? 1118 HOH A O 1 HETATM 2600 O O . HOH D 3 . ? 4.466 1.250 15.106 1.00 31.95 ? 1119 HOH A O 1 HETATM 2601 O O . HOH D 3 . ? 35.471 13.808 35.291 1.00 33.35 ? 1120 HOH A O 1 HETATM 2602 O O . HOH D 3 . ? 10.919 29.065 5.735 1.00 53.76 ? 1121 HOH A O 1 HETATM 2603 O O . HOH D 3 . ? 15.757 29.314 1.269 1.00 30.09 ? 1122 HOH A O 1 HETATM 2604 O O . HOH D 3 . ? 34.220 14.663 -8.475 1.00 55.50 ? 1123 HOH A O 1 HETATM 2605 O O . HOH D 3 . ? 7.734 22.022 35.212 1.00 46.36 ? 1124 HOH A O 1 HETATM 2606 O O . HOH D 3 . ? 2.288 15.275 25.896 1.00 42.22 ? 1125 HOH A O 1 HETATM 2607 O O . HOH D 3 . ? 48.321 15.662 29.237 1.00 37.49 ? 1126 HOH A O 1 HETATM 2608 O O . HOH D 3 . ? 15.682 9.065 -4.352 1.00 37.88 ? 1127 HOH A O 1 HETATM 2609 O O . HOH D 3 . ? 8.121 2.034 21.233 1.00 39.69 ? 1128 HOH A O 1 HETATM 2610 O O . HOH D 3 . ? 2.949 23.184 24.832 1.00 44.46 ? 1129 HOH A O 1 HETATM 2611 O O . HOH D 3 . ? 45.889 -3.923 18.097 1.00 46.46 ? 1130 HOH A O 1 HETATM 2612 O O . HOH D 3 . ? 13.094 0.949 22.137 1.00 30.97 ? 1131 HOH A O 1 HETATM 2613 O O . HOH D 3 . ? 39.145 -4.369 32.111 1.00 51.13 ? 1132 HOH A O 1 HETATM 2614 O O . HOH D 3 . ? 10.923 5.640 28.199 1.00 32.65 ? 1133 HOH A O 1 HETATM 2615 O O . HOH D 3 . ? 25.942 1.123 2.301 1.00 47.23 ? 1134 HOH A O 1 HETATM 2616 O O . HOH D 3 . ? 0.849 15.348 13.856 1.00 32.58 ? 1135 HOH A O 1 HETATM 2617 O O . HOH D 3 . ? 10.064 1.935 22.779 1.00 52.21 ? 1136 HOH A O 1 HETATM 2618 O O . HOH D 3 . ? 5.987 5.410 24.604 1.00 46.18 ? 1137 HOH A O 1 HETATM 2619 O O . HOH D 3 . ? 44.107 1.757 7.648 1.00 43.57 ? 1138 HOH A O 1 HETATM 2620 O O . HOH D 3 . ? 15.306 0.773 24.005 1.00 25.79 ? 1139 HOH A O 1 HETATM 2621 O O . HOH D 3 . ? 8.576 7.456 -3.380 1.00 32.61 ? 1140 HOH A O 1 HETATM 2622 O O . HOH D 3 . ? 40.260 7.790 3.588 1.00 49.81 ? 1141 HOH A O 1 HETATM 2623 O O . HOH D 3 . ? 41.389 -7.357 20.761 1.00 41.47 ? 1142 HOH A O 1 HETATM 2624 O O . HOH D 3 . ? 49.127 22.017 32.101 1.00 37.45 ? 1143 HOH A O 1 HETATM 2625 O O . HOH D 3 . ? 25.127 17.161 -6.612 1.00 42.77 ? 1144 HOH A O 1 HETATM 2626 O O . HOH D 3 . ? 27.812 -6.142 17.808 1.00 28.58 ? 1145 HOH A O 1 HETATM 2627 O O . HOH D 3 . ? 38.797 22.467 24.879 1.00 29.01 ? 1146 HOH A O 1 HETATM 2628 O O . HOH D 3 . ? 34.288 -7.999 20.012 1.00 35.56 ? 1147 HOH A O 1 HETATM 2629 O O . HOH D 3 . ? 26.825 -1.321 33.252 1.00 31.82 ? 1148 HOH A O 1 HETATM 2630 O O . HOH D 3 . ? 38.429 22.625 -2.999 1.00 44.01 ? 1149 HOH A O 1 HETATM 2631 O O . HOH D 3 . ? 5.593 25.106 23.421 1.00 47.73 ? 1150 HOH A O 1 HETATM 2632 O O . HOH D 3 . ? -2.634 15.204 9.635 1.00 42.14 ? 1151 HOH A O 1 HETATM 2633 O O . HOH D 3 . ? 44.502 24.355 13.180 1.00 49.81 ? 1152 HOH A O 1 HETATM 2634 O O . HOH D 3 . ? 1.044 3.812 21.370 1.00 49.39 ? 1153 HOH A O 1 HETATM 2635 O O . HOH D 3 . ? 22.007 23.815 -1.714 1.00 33.71 ? 1154 HOH A O 1 HETATM 2636 O O . HOH D 3 . ? 26.333 6.883 -4.603 1.00 40.81 ? 1155 HOH A O 1 HETATM 2637 O O . HOH D 3 . ? 38.683 -8.677 27.082 1.00 41.66 ? 1156 HOH A O 1 HETATM 2638 O O . HOH D 3 . ? 46.403 0.051 28.107 1.00 40.65 ? 1157 HOH A O 1 HETATM 2639 O O . HOH D 3 . ? 1.154 23.929 26.303 1.00 47.95 ? 1158 HOH A O 1 HETATM 2640 O O . HOH D 3 . ? 33.080 -5.391 19.283 1.00 27.13 ? 1159 HOH A O 1 HETATM 2641 O O . HOH D 3 . ? -0.939 17.928 12.952 1.00 37.35 ? 1160 HOH A O 1 HETATM 2642 O O . HOH D 3 . ? 37.884 21.288 -5.177 1.00 60.07 ? 1161 HOH A O 1 HETATM 2643 O O . HOH D 3 . ? 31.002 -5.920 12.035 1.00 32.22 ? 1162 HOH A O 1 HETATM 2644 O O . HOH D 3 . ? -4.875 14.707 25.843 1.00 41.23 ? 1163 HOH A O 1 HETATM 2645 O O . HOH D 3 . ? 6.902 20.413 12.563 1.00 42.29 ? 1164 HOH A O 1 HETATM 2646 O O . HOH D 3 . ? 19.798 -6.570 8.615 1.00 47.73 ? 1165 HOH A O 1 HETATM 2647 O O . HOH D 3 . ? 15.871 6.982 -3.262 1.00 38.70 ? 1166 HOH A O 1 HETATM 2648 O O . HOH D 3 . ? 14.745 -2.210 7.697 1.00 29.01 ? 1167 HOH A O 1 HETATM 2649 O O . HOH D 3 . ? 36.226 22.547 25.169 1.00 27.29 ? 1168 HOH A O 1 HETATM 2650 O O . HOH D 3 . ? 4.549 23.045 23.188 1.00 51.03 ? 1169 HOH A O 1 HETATM 2651 O O . HOH D 3 . ? 4.899 2.119 9.700 1.00 35.66 ? 1170 HOH A O 1 HETATM 2652 O O . HOH D 3 . ? 42.199 25.972 3.872 1.00 50.04 ? 1171 HOH A O 1 HETATM 2653 O O . HOH D 3 . ? 40.180 24.144 -1.906 1.00 46.06 ? 1172 HOH A O 1 HETATM 2654 O O . HOH D 3 . ? 39.531 -8.617 29.583 1.00 53.74 ? 1173 HOH A O 1 HETATM 2655 O O . HOH D 3 . ? 43.771 16.548 -0.036 1.00 45.64 ? 1174 HOH A O 1 HETATM 2656 O O . HOH D 3 . ? 44.119 2.943 11.452 1.00 42.81 ? 1175 HOH A O 1 HETATM 2657 O O . HOH D 3 . ? 15.530 21.390 34.422 1.00 37.21 ? 1176 HOH A O 1 HETATM 2658 O O . HOH D 3 . ? 13.723 0.038 19.046 1.00 25.04 ? 1177 HOH A O 1 HETATM 2659 O O . HOH D 3 . ? 19.646 12.706 26.044 1.00 32.28 ? 1178 HOH A O 1 HETATM 2660 O O . HOH D 3 . ? 29.572 -10.797 19.534 1.00 53.24 ? 1179 HOH A O 1 HETATM 2661 O O . HOH D 3 . ? 42.446 23.493 -1.154 1.00 55.56 ? 1180 HOH A O 1 HETATM 2662 O O . HOH D 3 . ? 45.218 22.866 18.509 1.00 56.26 ? 1181 HOH A O 1 HETATM 2663 O O . HOH D 3 . ? 37.410 15.585 -0.498 1.00 27.92 ? 1182 HOH A O 1 HETATM 2664 O O . HOH D 3 . ? 20.130 18.803 -3.080 1.00 37.00 ? 1183 HOH A O 1 HETATM 2665 O O . HOH D 3 . ? 2.808 22.475 18.508 1.00 35.63 ? 1184 HOH A O 1 HETATM 2666 O O . HOH D 3 . ? 14.207 0.043 26.476 1.00 37.97 ? 1185 HOH A O 1 HETATM 2667 O O . HOH D 3 . ? 8.705 25.590 2.095 1.00 47.82 ? 1186 HOH A O 1 HETATM 2668 O O . HOH D 3 . ? 34.005 -4.815 5.374 1.00 48.19 ? 1187 HOH A O 1 HETATM 2669 O O . HOH D 3 . ? 27.096 4.233 0.700 1.00 37.68 ? 1188 HOH A O 1 HETATM 2670 O O . HOH D 3 . ? 19.572 16.593 -4.930 1.00 44.84 ? 1189 HOH A O 1 HETATM 2671 O O . HOH D 3 . ? 11.852 28.381 22.600 1.00 27.24 ? 1190 HOH A O 1 HETATM 2672 O O . HOH D 3 . ? 21.710 6.804 -2.956 1.00 42.29 ? 1191 HOH A O 1 HETATM 2673 O O . HOH D 3 . ? 40.642 0.298 32.049 1.00 33.49 ? 1192 HOH A O 1 HETATM 2674 O O . HOH D 3 . ? 33.377 -8.539 16.220 1.00 43.36 ? 1193 HOH A O 1 HETATM 2675 O O . HOH D 3 . ? 40.663 16.629 34.593 1.00 32.47 ? 1194 HOH A O 1 HETATM 2676 O O . HOH D 3 . ? 15.406 22.413 0.164 1.00 43.64 ? 1195 HOH A O 1 HETATM 2677 O O . HOH D 3 . ? 17.572 -3.802 26.841 1.00 40.10 ? 1196 HOH A O 1 HETATM 2678 O O . HOH D 3 . ? 17.187 -6.151 10.065 1.00 46.96 ? 1197 HOH A O 1 HETATM 2679 O O . HOH D 3 . ? 3.252 11.024 25.678 1.00 50.53 ? 1198 HOH A O 1 HETATM 2680 O O . HOH D 3 . ? 8.471 9.295 35.995 1.00 36.41 ? 1199 HOH A O 1 HETATM 2681 O O . HOH D 3 . ? 25.308 14.996 28.066 1.00 37.93 ? 1200 HOH A O 1 HETATM 2682 O O . HOH D 3 . ? 20.107 30.667 20.064 1.00 45.85 ? 1201 HOH A O 1 HETATM 2683 O O . HOH D 3 . ? 6.587 12.864 37.675 1.00 37.79 ? 1202 HOH A O 1 HETATM 2684 O O . HOH D 3 . ? 18.136 -5.008 29.073 1.00 49.83 ? 1203 HOH A O 1 HETATM 2685 O O . HOH D 3 . ? 34.626 22.469 31.004 1.00 31.58 ? 1204 HOH A O 1 HETATM 2686 O O . HOH D 3 . ? 37.610 12.655 2.919 1.00 23.60 ? 1205 HOH A O 1 HETATM 2687 O O . HOH D 3 . ? 17.928 24.271 0.370 1.00 26.96 ? 1206 HOH A O 1 HETATM 2688 O O . HOH D 3 . ? 36.852 22.292 33.165 1.00 43.67 ? 1207 HOH A O 1 HETATM 2689 O O . HOH D 3 . ? 42.362 23.527 17.908 1.00 45.40 ? 1208 HOH A O 1 HETATM 2690 O O . HOH D 3 . ? 16.367 14.277 -5.022 1.00 40.26 ? 1209 HOH A O 1 HETATM 2691 O O . HOH D 3 . ? -0.067 16.898 25.385 1.00 40.10 ? 1210 HOH A O 1 HETATM 2692 O O . HOH D 3 . ? 18.611 12.789 28.535 1.00 37.97 ? 1211 HOH A O 1 HETATM 2693 O O . HOH D 3 . ? 21.971 29.830 21.707 1.00 49.12 ? 1212 HOH A O 1 HETATM 2694 O O . HOH D 3 . ? -0.755 19.034 6.177 1.00 46.25 ? 1213 HOH A O 1 HETATM 2695 O O . HOH D 3 . ? 19.480 28.381 25.603 1.00 44.29 ? 1214 HOH A O 1 HETATM 2696 O O . HOH D 3 . ? 43.970 15.535 33.228 1.00 38.51 ? 1215 HOH A O 1 HETATM 2697 O O . HOH D 3 . ? 19.933 32.066 12.968 1.00 46.98 ? 1216 HOH A O 1 HETATM 2698 O O . HOH D 3 . ? 45.086 11.827 30.978 1.00 44.83 ? 1217 HOH A O 1 HETATM 2699 O O . HOH D 3 . ? 23.354 15.021 28.382 1.00 43.06 ? 1218 HOH A O 1 HETATM 2700 O O . HOH D 3 . ? 47.963 -2.275 28.401 1.00 45.02 ? 1219 HOH A O 1 HETATM 2701 O O . HOH D 3 . ? 50.898 4.289 17.425 1.00 41.77 ? 1220 HOH A O 1 HETATM 2702 O O . HOH D 3 . ? 2.360 13.054 27.430 1.00 46.11 ? 1221 HOH A O 1 HETATM 2703 O O . HOH D 3 . ? 7.339 22.920 11.470 1.00 44.46 ? 1222 HOH A O 1 HETATM 2704 O O . HOH D 3 . ? 38.920 11.045 32.562 1.00 43.03 ? 1223 HOH A O 1 HETATM 2705 O O . HOH D 3 . ? 48.153 10.671 30.438 1.00 54.07 ? 1224 HOH A O 1 HETATM 2706 O O . HOH D 3 . ? 41.219 12.416 33.154 1.00 33.23 ? 1225 HOH A O 1 HETATM 2707 O O . HOH D 3 . ? 4.794 21.557 7.732 1.00 42.05 ? 1226 HOH A O 1 HETATM 2708 O O . HOH D 3 . ? 21.934 21.852 -3.738 1.00 48.20 ? 1227 HOH A O 1 HETATM 2709 O O . HOH D 3 . ? 50.951 16.246 29.890 1.00 43.61 ? 1228 HOH A O 1 HETATM 2710 O O . HOH D 3 . ? 39.769 13.922 34.894 1.00 42.92 ? 1229 HOH A O 1 HETATM 2711 O O . HOH D 3 . ? 19.884 13.987 30.505 1.00 45.69 ? 1230 HOH A O 1 HETATM 2712 O O . HOH D 3 . ? 42.886 10.634 34.719 1.00 45.57 ? 1231 HOH A O 1 HETATM 2713 O O . HOH D 3 . ? 41.386 9.085 35.926 1.00 49.26 ? 1232 HOH A O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . LEU A 1 ? 0.4610 0.3195 0.3420 -0.0121 -0.0053 -0.0044 1 LEU A N 2 C CA . LEU A 1 ? 0.4519 0.3193 0.3395 -0.0108 -0.0022 -0.0043 1 LEU A CA 3 C C . LEU A 1 ? 0.4138 0.2820 0.3011 -0.0131 -0.0038 -0.0037 1 LEU A C 4 O O . LEU A 1 ? 0.4112 0.2718 0.2905 -0.0138 -0.0057 -0.0042 1 LEU A O 5 C CB . LEU A 1 ? 0.4824 0.3492 0.3679 -0.0063 0.0017 -0.0057 1 LEU A CB 6 C CG . LEU A 1 ? 0.5073 0.3740 0.3936 -0.0031 0.0041 -0.0062 1 LEU A CG 7 C CD1 . LEU A 1 ? 0.5028 0.3693 0.3865 0.0011 0.0079 -0.0072 1 LEU A CD1 8 C CD2 . LEU A 1 ? 0.4896 0.3659 0.3859 -0.0041 0.0048 -0.0050 1 LEU A CD2 9 N N . PRO A 2 ? 0.3799 0.2572 0.2756 -0.0138 -0.0031 -0.0028 2 PRO A N 10 C CA . PRO A 2 ? 0.3776 0.2564 0.2739 -0.0152 -0.0040 -0.0022 2 PRO A CA 11 C C . PRO A 2 ? 0.3789 0.2530 0.2687 -0.0128 -0.0022 -0.0031 2 PRO A C 12 O O . PRO A 2 ? 0.3670 0.2415 0.2562 -0.0093 0.0010 -0.0040 2 PRO A O 13 C CB . PRO A 2 ? 0.3635 0.2526 0.2704 -0.0148 -0.0026 -0.0018 2 PRO A CB 14 C CG . PRO A 2 ? 0.3502 0.2431 0.2615 -0.0152 -0.0028 -0.0017 2 PRO A CG 15 C CD . PRO A 2 ? 0.3629 0.2494 0.2680 -0.0134 -0.0017 -0.0024 2 PRO A CD 16 N N . SER A 3 ? 0.4057 0.2765 0.2911 -0.0148 -0.0043 -0.0026 3 SER A N 17 C CA . SER A 3 ? 0.4285 0.2968 0.3086 -0.0131 -0.0027 -0.0030 3 SER A CA 18 C C . SER A 3 ? 0.4343 0.3081 0.3199 -0.0156 -0.0042 -0.0012 3 SER A C 19 O O . SER A 3 ? 0.4698 0.3484 0.3626 -0.0179 -0.0059 -0.0001 3 SER A O 20 C CB . SER A 3 ? 0.4591 0.3171 0.3272 -0.0129 -0.0042 -0.0044 3 SER A CB 21 O OG . SER A 3 ? 0.4853 0.3398 0.3517 -0.0170 -0.0085 -0.0036 3 SER A OG 22 N N . GLY A 4 ? 0.4379 0.3110 0.3202 -0.0153 -0.0038 -0.0006 4 GLY A N 23 C CA . GLY A 4 ? 0.3992 0.2777 0.2878 -0.0178 -0.0054 0.0013 4 GLY A CA 24 C C . GLY A 4 ? 0.3501 0.2364 0.2473 -0.0159 -0.0030 0.0022 4 GLY A C 25 O O . GLY A 4 ? 0.3308 0.2180 0.2274 -0.0127 0.0001 0.0016 4 GLY A O 26 N N . SER A 5 ? 0.3406 0.2322 0.2457 -0.0180 -0.0048 0.0038 5 SER A N 27 C CA . SER A 5 ? 0.3147 0.2130 0.2281 -0.0169 -0.0036 0.0051 5 SER A CA 28 C C . SER A 5 ? 0.3083 0.2115 0.2297 -0.0152 -0.0023 0.0039 5 SER A C 29 O O . SER A 5 ? 0.2898 0.1932 0.2127 -0.0158 -0.0031 0.0027 5 SER A O 30 C CB . SER A 5 ? 0.3238 0.2252 0.2426 -0.0196 -0.0065 0.0071 5 SER A CB 31 O OG . SER A 5 ? 0.3043 0.2032 0.2172 -0.0206 -0.0071 0.0088 5 SER A OG 32 N N . ASP A 6 ? 0.3163 0.2239 0.2429 -0.0132 -0.0004 0.0045 6 ASP A N 33 C CA . ASP A 6 ? 0.3033 0.2164 0.2389 -0.0120 0.0000 0.0036 6 ASP A CA 34 C C . ASP A 6 ? 0.2986 0.2154 0.2419 -0.0141 -0.0031 0.0037 6 ASP A C 35 O O . ASP A 6 ? 0.2878 0.2050 0.2327 -0.0158 -0.0051 0.0054 6 ASP A O 36 C CB . ASP A 6 ? 0.3070 0.2242 0.2477 -0.0101 0.0017 0.0048 6 ASP A CB 37 C CG . ASP A 6 ? 0.3067 0.2223 0.2423 -0.0074 0.0051 0.0046 6 ASP A CG 38 O OD1 . ASP A 6 ? 0.3052 0.2158 0.2324 -0.0068 0.0062 0.0036 6 ASP A OD1 39 O OD2 . ASP A 6 ? 0.3080 0.2277 0.2486 -0.0059 0.0065 0.0058 6 ASP A OD2 40 N N . PRO A 7 ? 0.2740 0.1939 0.2219 -0.0139 -0.0035 0.0020 7 PRO A N 41 C CA . PRO A 7 ? 0.2661 0.1909 0.2225 -0.0148 -0.0060 0.0017 7 PRO A CA 42 C C . PRO A 7 ? 0.2518 0.1805 0.2162 -0.0137 -0.0064 0.0023 7 PRO A C 43 O O . PRO A 7 ? 0.2672 0.1966 0.2325 -0.0118 -0.0043 0.0021 7 PRO A O 44 C CB . PRO A 7 ? 0.2644 0.1928 0.2238 -0.0139 -0.0054 -0.0003 7 PRO A CB 45 C CG . PRO A 7 ? 0.2726 0.1972 0.2248 -0.0132 -0.0032 -0.0007 7 PRO A CG 46 C CD . PRO A 7 ? 0.2761 0.1958 0.2221 -0.0125 -0.0016 0.0003 7 PRO A CD 47 N N . ALA A 8 ? 0.2541 0.1851 0.2247 -0.0148 -0.0092 0.0029 8 ALA A N 48 C CA . ALA A 8 ? 0.2567 0.1913 0.2362 -0.0138 -0.0104 0.0031 8 ALA A CA 49 C C . ALA A 8 ? 0.2516 0.1903 0.2368 -0.0115 -0.0096 0.0003 8 ALA A C 50 O O . ALA A 8 ? 0.2460 0.1862 0.2300 -0.0110 -0.0089 -0.0017 8 ALA A O 51 C CB . ALA A 8 ? 0.2615 0.1979 0.2472 -0.0152 -0.0139 0.0039 8 ALA A CB 52 N N . PHE A 9 ? 0.2492 0.1897 0.2401 -0.0101 -0.0099 0.0004 9 PHE A N 53 C CA . PHE A 9 ? 0.2583 0.2026 0.2552 -0.0080 -0.0098 -0.0022 9 PHE A CA 54 C C . PHE A 9 ? 0.2645 0.2122 0.2692 -0.0076 -0.0129 -0.0042 9 PHE A C 55 O O . PHE A 9 ? 0.2865 0.2336 0.2942 -0.0087 -0.0154 -0.0028 9 PHE A O 56 C CB . PHE A 9 ? 0.2536 0.1984 0.2541 -0.0069 -0.0096 -0.0011 9 PHE A CB 57 C CG . PHE A 9 ? 0.2522 0.1948 0.2461 -0.0067 -0.0063 0.0006 9 PHE A CG 58 C CD1 . PHE A 9 ? 0.2558 0.1974 0.2433 -0.0059 -0.0034 -0.0005 9 PHE A CD1 59 C CD2 . PHE A 9 ? 0.2592 0.2012 0.2537 -0.0070 -0.0062 0.0039 9 PHE A CD2 60 C CE1 . PHE A 9 ? 0.2598 0.1993 0.2414 -0.0051 -0.0004 0.0009 9 PHE A CE1 61 C CE2 . PHE A 9 ? 0.2673 0.2081 0.2559 -0.0063 -0.0030 0.0056 9 PHE A CE2 62 C CZ . PHE A 9 ? 0.2575 0.1969 0.2397 -0.0052 -0.0001 0.0040 9 PHE A CZ 63 N N . SER A 10 ? 0.2770 0.2286 0.2847 -0.0058 -0.0126 -0.0075 10 SER A N 64 C CA . SER A 10 ? 0.2763 0.2321 0.2919 -0.0045 -0.0154 -0.0102 10 SER A CA 65 C C . SER A 10 ? 0.3018 0.2581 0.3253 -0.0029 -0.0176 -0.0112 10 SER A C 66 O O . SER A 10 ? 0.3049 0.2631 0.3352 -0.0018 -0.0205 -0.0129 10 SER A O 67 C CB . SER A 10 ? 0.2732 0.2335 0.2879 -0.0030 -0.0138 -0.0132 10 SER A CB 68 O OG . SER A 10 ? 0.2675 0.2294 0.2828 -0.0012 -0.0122 -0.0151 10 SER A OG 69 N N . GLN A 11 ? 0.2994 0.2541 0.3220 -0.0027 -0.0164 -0.0100 11 GLN A N 70 C CA . GLN A 11 ? 0.3059 0.2607 0.3360 -0.0016 -0.0190 -0.0104 11 GLN A CA 71 C C . GLN A 11 ? 0.3031 0.2547 0.3337 -0.0036 -0.0202 -0.0059 11 GLN A C 72 O O . GLN A 11 ? 0.2901 0.2396 0.3136 -0.0051 -0.0176 -0.0030 11 GLN A O 73 C CB . GLN A 11 ? 0.3198 0.2753 0.3487 -0.0004 -0.0169 -0.0110 11 GLN A CB 74 C CG . GLN A 11 ? 0.3442 0.3032 0.3715 0.0013 -0.0151 -0.0147 11 GLN A CG 75 C CD . GLN A 11 ? 0.3720 0.3344 0.4062 0.0033 -0.0179 -0.0189 11 GLN A CD 76 O OE1 . GLN A 11 ? 0.3686 0.3306 0.4093 0.0043 -0.0209 -0.0200 11 GLN A OE1 77 N NE2 . GLN A 11 ? 0.4099 0.3755 0.4427 0.0040 -0.0173 -0.0212 11 GLN A NE2 78 N N . PRO A 12 ? 0.3109 0.2621 0.3494 -0.0036 -0.0239 -0.0052 12 PRO A N 79 C CA . PRO A 12 ? 0.3227 0.2717 0.3622 -0.0056 -0.0251 -0.0003 12 PRO A CA 80 C C . PRO A 12 ? 0.3389 0.2880 0.3749 -0.0057 -0.0222 0.0020 12 PRO A C 81 O O . PRO A 12 ? 0.3201 0.2706 0.3564 -0.0041 -0.0209 -0.0001 12 PRO A O 82 C CB . PRO A 12 ? 0.3409 0.2897 0.3909 -0.0052 -0.0303 -0.0007 12 PRO A CB 83 C CG . PRO A 12 ? 0.3393 0.2900 0.3932 -0.0025 -0.0316 -0.0064 12 PRO A CG 84 C CD . PRO A 12 ? 0.3148 0.2675 0.3615 -0.0015 -0.0274 -0.0091 12 PRO A CD 85 N N . LYS A 13 ? 0.3612 0.3092 0.3938 -0.0076 -0.0212 0.0067 13 LYS A N 86 C CA . LYS A 13 ? 0.3984 0.3470 0.4278 -0.0076 -0.0185 0.0096 13 LYS A CA 87 C C . LYS A 13 ? 0.3727 0.3228 0.4105 -0.0072 -0.0213 0.0105 13 LYS A C 88 O O . LYS A 13 ? 0.3588 0.3103 0.3955 -0.0063 -0.0192 0.0107 13 LYS A O 89 C CB . LYS A 13 ? 0.4587 0.4067 0.4829 -0.0095 -0.0170 0.0146 13 LYS A CB 90 C CG . LYS A 13 ? 0.4864 0.4360 0.5068 -0.0091 -0.0138 0.0179 13 LYS A CG 91 C CD . LYS A 13 ? 0.5113 0.4617 0.5295 -0.0110 -0.0137 0.0234 13 LYS A CD 92 C CE . LYS A 13 ? 0.5128 0.4666 0.5326 -0.0109 -0.0124 0.0278 13 LYS A CE 93 N NZ . LYS A 13 ? 0.5568 0.5110 0.5690 -0.0087 -0.0074 0.0267 13 LYS A NZ 94 N N . SER A 14 ? 0.3609 0.3105 0.4073 -0.0079 -0.0263 0.0106 14 SER A N 95 C CA . SER A 14 ? 0.3504 0.3007 0.4050 -0.0075 -0.0295 0.0108 14 SER A CA 96 C C . SER A 14 ? 0.3244 0.2755 0.3789 -0.0049 -0.0284 0.0057 14 SER A C 97 O O . SER A 14 ? 0.3231 0.2755 0.3797 -0.0045 -0.0284 0.0064 14 SER A O 98 C CB . SER A 14 ? 0.3611 0.3098 0.4249 -0.0082 -0.0356 0.0110 14 SER A CB 99 O OG . SER A 14 ? 0.3895 0.3373 0.4550 -0.0064 -0.0370 0.0053 14 SER A OG 100 N N . VAL A 15 ? 0.2953 0.2465 0.3475 -0.0034 -0.0275 0.0007 15 VAL A N 101 C CA . VAL A 15 ? 0.2935 0.2465 0.3452 -0.0010 -0.0263 -0.0041 15 VAL A CA 102 C C . VAL A 15 ? 0.2785 0.2327 0.3226 -0.0008 -0.0212 -0.0030 15 VAL A C 103 O O . VAL A 15 ? 0.2814 0.2371 0.3263 0.0002 -0.0204 -0.0042 15 VAL A O 104 C CB . VAL A 15 ? 0.2913 0.2450 0.3424 0.0005 -0.0265 -0.0091 15 VAL A CB 105 C CG1 . VAL A 15 ? 0.2988 0.2555 0.3477 0.0027 -0.0244 -0.0137 15 VAL A CG1 106 C CG2 . VAL A 15 ? 0.3027 0.2554 0.3622 0.0010 -0.0319 -0.0108 15 VAL A CG2 107 N N . LEU A 16 ? 0.2663 0.2197 0.3030 -0.0017 -0.0178 -0.0011 16 LEU A N 108 C CA . LEU A 16 ? 0.2569 0.2107 0.2861 -0.0014 -0.0130 0.0003 16 LEU A CA 109 C C . LEU A 16 ? 0.2637 0.2185 0.2943 -0.0017 -0.0122 0.0043 16 LEU A C 110 O O . LEU A 16 ? 0.2283 0.1847 0.2571 -0.0005 -0.0098 0.0038 16 LEU A O 111 C CB . LEU A 16 ? 0.2528 0.2047 0.2740 -0.0023 -0.0103 0.0018 16 LEU A CB 112 C CG . LEU A 16 ? 0.2483 0.1998 0.2670 -0.0021 -0.0103 -0.0016 16 LEU A CG 113 C CD1 . LEU A 16 ? 0.2522 0.2011 0.2626 -0.0034 -0.0081 0.0000 16 LEU A CD1 114 C CD2 . LEU A 16 ? 0.2473 0.2010 0.2651 -0.0004 -0.0088 -0.0055 16 LEU A CD2 115 N N . ASP A 17 ? 0.2731 0.2277 0.3073 -0.0033 -0.0144 0.0085 17 ASP A N 116 C CA . ASP A 17 ? 0.3095 0.2660 0.3461 -0.0039 -0.0143 0.0131 17 ASP A CA 117 C C . ASP A 17 ? 0.3046 0.2625 0.3481 -0.0032 -0.0167 0.0117 17 ASP A C 118 O O . ASP A 17 ? 0.3072 0.2672 0.3506 -0.0029 -0.0151 0.0142 17 ASP A O 119 C CB . ASP A 17 ? 0.3214 0.2780 0.3619 -0.0061 -0.0170 0.0182 17 ASP A CB 120 C CG . ASP A 17 ? 0.3303 0.2865 0.3632 -0.0070 -0.0140 0.0210 17 ASP A CG 121 O OD1 . ASP A 17 ? 0.3572 0.3133 0.3816 -0.0057 -0.0093 0.0205 17 ASP A OD1 122 O OD2 . ASP A 17 ? 0.3299 0.2858 0.3657 -0.0089 -0.0167 0.0240 17 ASP A OD2 123 N N . ALA A 18 ? 0.3203 0.2769 0.3698 -0.0028 -0.0210 0.0079 18 ALA A N 124 C CA . ALA A 18 ? 0.3182 0.2756 0.3740 -0.0020 -0.0240 0.0056 18 ALA A CA 125 C C . ALA A 18 ? 0.3176 0.2767 0.3692 -0.0001 -0.0206 0.0024 18 ALA A C 126 O O . ALA A 18 ? 0.3079 0.2681 0.3635 0.0002 -0.0223 0.0015 18 ALA A O 127 C CB . ALA A 18 ? 0.3365 0.2919 0.3988 -0.0014 -0.0291 0.0015 18 ALA A CB 128 N N . GLY A 19 ? 0.2881 0.2475 0.3320 0.0006 -0.0163 0.0005 19 GLY A N 129 C CA . GLY A 19 ? 0.2755 0.2368 0.3152 0.0022 -0.0130 -0.0019 19 GLY A CA 130 C C . GLY A 19 ? 0.2506 0.2131 0.2859 0.0021 -0.0089 0.0019 19 GLY A C 131 O O . GLY A 19 ? 0.2790 0.2430 0.3111 0.0033 -0.0063 0.0003 19 GLY A O 132 N N . LEU A 20 ? 0.2505 0.2128 0.2858 0.0010 -0.0085 0.0070 20 LEU A N 133 C CA . LEU A 20 ? 0.2450 0.2088 0.2759 0.0013 -0.0044 0.0110 20 LEU A CA 134 C C . LEU A 20 ? 0.2760 0.2423 0.3130 0.0004 -0.0062 0.0157 20 LEU A C 135 O O . LEU A 20 ? 0.2830 0.2491 0.3259 -0.0012 -0.0101 0.0182 20 LEU A O 136 C CB . LEU A 20 ? 0.2454 0.2077 0.2705 0.0008 -0.0021 0.0136 20 LEU A CB 137 C CG . LEU A 20 ? 0.2430 0.2071 0.2636 0.0014 0.0017 0.0182 20 LEU A CG 138 C CD1 . LEU A 20 ? 0.2437 0.2082 0.2588 0.0035 0.0060 0.0169 20 LEU A CD1 139 C CD2 . LEU A 20 ? 0.2486 0.2111 0.2638 0.0008 0.0030 0.0203 20 LEU A CD2 140 N N . THR A 21 ? 0.2785 0.2474 0.3144 0.0013 -0.0035 0.0173 21 THR A N 141 C CA . THR A 21 ? 0.3027 0.2750 0.3435 0.0005 -0.0043 0.0228 21 THR A CA 142 C C . THR A 21 ? 0.2722 0.2474 0.3088 0.0020 0.0003 0.0256 21 THR A C 143 O O . THR A 21 ? 0.2587 0.2331 0.2898 0.0037 0.0036 0.0226 21 THR A O 144 C CB . THR A 21 ? 0.3355 0.3086 0.3843 -0.0001 -0.0088 0.0218 21 THR A CB 145 O OG1 . THR A 21 ? 0.3369 0.3104 0.3836 0.0013 -0.0072 0.0176 21 THR A OG1 146 C CG2 . THR A 21 ? 0.3610 0.3314 0.4158 -0.0015 -0.0144 0.0199 21 THR A CG2 147 N N . CYS A 22 ? 0.2653 0.2443 0.3055 0.0012 0.0002 0.0315 22 CYS A N 148 C CA . CYS A 22 ? 0.2661 0.2491 0.3038 0.0027 0.0044 0.0353 22 CYS A CA 149 C C . CYS A 22 ? 0.2529 0.2398 0.2987 0.0015 0.0018 0.0389 22 CYS A C 150 O O . CYS A 22 ? 0.2372 0.2242 0.2905 -0.0007 -0.0033 0.0406 22 CYS A O 151 C CB . CYS A 22 ? 0.2763 0.2616 0.3103 0.0030 0.0074 0.0400 22 CYS A CB 152 S SG . CYS A 22 ? 0.2887 0.2688 0.3120 0.0044 0.0106 0.0358 22 CYS A SG 153 N N . GLN A 23 ? 0.2387 0.2287 0.2832 0.0031 0.0049 0.0401 23 GLN A N 154 C CA . GLN A 23 ? 0.2507 0.2447 0.3026 0.0021 0.0026 0.0436 23 GLN A CA 155 C C . GLN A 23 ? 0.2555 0.2547 0.3114 0.0009 0.0023 0.0514 23 GLN A C 156 O O . GLN A 23 ? 0.2336 0.2370 0.2857 0.0027 0.0071 0.0552 23 GLN A O 157 C CB . GLN A 23 ? 0.2588 0.2550 0.3080 0.0042 0.0064 0.0433 23 GLN A CB 158 C CG . GLN A 23 ? 0.2664 0.2669 0.3223 0.0032 0.0045 0.0468 23 GLN A CG 159 C CD . GLN A 23 ? 0.2777 0.2802 0.3295 0.0057 0.0091 0.0464 23 GLN A CD 160 O OE1 . GLN A 23 ? 0.3255 0.3318 0.3746 0.0077 0.0136 0.0505 23 GLN A OE1 161 N NE2 . GLN A 23 ? 0.2761 0.2764 0.3272 0.0060 0.0083 0.0416 23 GLN A NE2 162 N N . GLY A 24 ? 0.2623 0.2616 0.3258 -0.0019 -0.0031 0.0537 24 GLY A N 163 C CA . GLY A 24 ? 0.2761 0.2814 0.3448 -0.0037 -0.0042 0.0621 24 GLY A CA 164 C C . GLY A 24 ? 0.2792 0.2856 0.3438 -0.0035 -0.0019 0.0647 24 GLY A C 165 O O . GLY A 24 ? 0.3007 0.3135 0.3674 -0.0042 -0.0010 0.0718 24 GLY A O 166 N N . ALA A 25 ? 0.2771 0.2779 0.3361 -0.0029 -0.0013 0.0593 25 ALA A N 167 C CA . ALA A 25 ? 0.2892 0.2902 0.3440 -0.0031 0.0000 0.0612 25 ALA A CA 168 C C . ALA A 25 ? 0.2945 0.2889 0.3473 -0.0039 -0.0023 0.0559 25 ALA A C 169 O O . ALA A 25 ? 0.2664 0.2556 0.3182 -0.0033 -0.0035 0.0495 25 ALA A O 170 C CB . ALA A 25 ? 0.2991 0.3028 0.3450 0.0000 0.0068 0.0621 25 ALA A CB 171 N N . SER A 26 ? 0.3058 0.3009 0.3583 -0.0054 -0.0032 0.0591 26 SER A N 172 C CA . SER A 26 ? 0.3038 0.2936 0.3526 -0.0058 -0.0043 0.0550 26 SER A CA 173 C C . SER A 26 ? 0.3052 0.2933 0.3425 -0.0029 0.0017 0.0517 26 SER A C 174 O O . SER A 26 ? 0.2777 0.2700 0.3102 -0.0012 0.0062 0.0550 26 SER A O 175 C CB . SER A 26 ? 0.3181 0.3100 0.3708 -0.0086 -0.0074 0.0604 26 SER A CB 176 O OG . SER A 26 ? 0.3542 0.3411 0.4031 -0.0090 -0.0083 0.0566 26 SER A OG 177 N N . PRO A 27 ? 0.3086 0.2906 0.3416 -0.0024 0.0016 0.0454 27 PRO A N 178 C CA . PRO A 27 ? 0.3160 0.2952 0.3383 -0.0003 0.0061 0.0424 27 PRO A CA 179 C C . PRO A 27 ? 0.3086 0.2898 0.3262 -0.0007 0.0078 0.0463 27 PRO A C 180 O O . PRO A 27 ? 0.3138 0.2944 0.3225 0.0014 0.0122 0.0455 27 PRO A O 181 C CB . PRO A 27 ? 0.3179 0.2911 0.3393 -0.0007 0.0039 0.0361 27 PRO A CB 182 C CG . PRO A 27 ? 0.3173 0.2907 0.3473 -0.0015 0.0001 0.0346 27 PRO A CG 183 C CD . PRO A 27 ? 0.3112 0.2888 0.3490 -0.0033 -0.0027 0.0405 27 PRO A CD 184 N N A SER A 28 ? 0.3108 0.2942 0.3343 -0.0035 0.0040 0.0506 28 SER A N 185 N N B SER A 28 ? 0.3162 0.2997 0.3398 -0.0035 0.0040 0.0506 28 SER A N 186 C CA A SER A 28 ? 0.3044 0.2908 0.3244 -0.0043 0.0051 0.0550 28 SER A CA 187 C CA B SER A 28 ? 0.3132 0.2998 0.3332 -0.0043 0.0051 0.0551 28 SER A CA 188 C C A SER A 28 ? 0.3067 0.3007 0.3254 -0.0029 0.0087 0.0609 28 SER A C 189 C C B SER A 28 ? 0.3117 0.3057 0.3301 -0.0028 0.0089 0.0607 28 SER A C 190 O O A SER A 28 ? 0.2926 0.2897 0.3064 -0.0028 0.0107 0.0641 28 SER A O 191 O O B SER A 28 ? 0.2973 0.2942 0.3102 -0.0025 0.0112 0.0637 28 SER A O 192 C CB A SER A 28 ? 0.3035 0.2902 0.3311 -0.0079 -0.0004 0.0581 28 SER A CB 193 C CB B SER A 28 ? 0.3175 0.3052 0.3457 -0.0079 -0.0003 0.0589 28 SER A CB 194 O OG A SER A 28 ? 0.3031 0.2945 0.3407 -0.0097 -0.0037 0.0632 28 SER A OG 195 O OG B SER A 28 ? 0.3285 0.3107 0.3617 -0.0092 -0.0047 0.0544 28 SER A OG 196 N N . SER A 29 ? 0.3048 0.3023 0.3278 -0.0019 0.0095 0.0624 29 SER A N 197 C CA . SER A 29 ? 0.2990 0.3045 0.3207 -0.0001 0.0135 0.0680 29 SER A CA 198 C C . SER A 29 ? 0.3074 0.3139 0.3300 0.0022 0.0159 0.0668 29 SER A C 199 O O . SER A 29 ? 0.3167 0.3257 0.3480 0.0007 0.0129 0.0691 29 SER A O 200 C CB . SER A 29 ? 0.3004 0.3130 0.3309 -0.0033 0.0100 0.0760 29 SER A CB 201 O OG . SER A 29 ? 0.3088 0.3301 0.3378 -0.0015 0.0140 0.0817 29 SER A OG 202 N N . VAL A 30 ? 0.3102 0.3145 0.3240 0.0058 0.0208 0.0630 30 VAL A N 203 C CA . VAL A 30 ? 0.3296 0.3329 0.3442 0.0078 0.0224 0.0603 30 VAL A CA 204 C C . VAL A 30 ? 0.3356 0.3406 0.3416 0.0122 0.0286 0.0600 30 VAL A C 205 O O . VAL A 30 ? 0.3083 0.3102 0.3054 0.0138 0.0311 0.0575 30 VAL A O 206 C CB . VAL A 30 ? 0.3279 0.3230 0.3422 0.0072 0.0201 0.0531 30 VAL A CB 207 C CG1 . VAL A 30 ? 0.3340 0.3225 0.3390 0.0083 0.0217 0.0479 30 VAL A CG1 208 C CG2 . VAL A 30 ? 0.3428 0.3378 0.3581 0.0092 0.0218 0.0509 30 VAL A CG2 209 N N . SER A 31 ? 0.3661 0.3761 0.3750 0.0140 0.0307 0.0626 31 SER A N 210 C CA . SER A 31 ? 0.3871 0.3989 0.3886 0.0185 0.0364 0.0624 31 SER A CA 211 C C . SER A 31 ? 0.3603 0.3665 0.3588 0.0208 0.0381 0.0569 31 SER A C 212 O O . SER A 31 ? 0.3698 0.3760 0.3747 0.0195 0.0359 0.0565 31 SER A O 213 C CB . SER A 31 ? 0.4260 0.4486 0.4320 0.0195 0.0385 0.0700 31 SER A CB 214 O OG . SER A 31 ? 0.4339 0.4592 0.4453 0.0203 0.0388 0.0711 31 SER A OG 215 N N . LYS A 32 ? 0.3467 0.3481 0.3353 0.0240 0.0416 0.0528 32 LYS A N 216 C CA . LYS A 32 ? 0.3774 0.3730 0.3620 0.0263 0.0433 0.0477 32 LYS A CA 217 C C . LYS A 32 ? 0.3352 0.3257 0.3240 0.0232 0.0392 0.0437 32 LYS A C 218 O O . LYS A 32 ? 0.3088 0.3001 0.3020 0.0233 0.0388 0.0432 32 LYS A O 219 C CB . LYS A 32 ? 0.4168 0.4173 0.4026 0.0297 0.0468 0.0502 32 LYS A CB 220 C CG . LYS A 32 ? 0.4834 0.4887 0.4637 0.0338 0.0514 0.0530 32 LYS A CG 221 C CD . LYS A 32 ? 0.5566 0.5610 0.5326 0.0387 0.0556 0.0514 32 LYS A CD 222 C CE . LYS A 32 ? 0.5967 0.6087 0.5695 0.0430 0.0601 0.0555 32 LYS A CE 223 N NZ . LYS A 32 ? 0.6397 0.6495 0.6050 0.0489 0.0647 0.0529 32 LYS A NZ 224 N N . PRO A 33 ? 0.2970 0.2830 0.2850 0.0204 0.0361 0.0412 33 PRO A N 225 C CA . PRO A 33 ? 0.2854 0.2672 0.2771 0.0181 0.0326 0.0373 33 PRO A CA 226 C C . PRO A 33 ? 0.2753 0.2517 0.2613 0.0199 0.0343 0.0323 33 PRO A C 227 O O . PRO A 33 ? 0.2758 0.2487 0.2534 0.0223 0.0372 0.0307 33 PRO A O 228 C CB . PRO A 33 ? 0.2890 0.2675 0.2805 0.0153 0.0293 0.0357 33 PRO A CB 229 C CG . PRO A 33 ? 0.2966 0.2750 0.2809 0.0167 0.0318 0.0371 33 PRO A CG 230 C CD . PRO A 33 ? 0.2962 0.2809 0.2802 0.0194 0.0355 0.0417 33 PRO A CD 231 N N . ILE A 34 ? 0.2601 0.2356 0.2506 0.0185 0.0321 0.0299 34 ILE A N 232 C CA . ILE A 34 ? 0.2607 0.2311 0.2469 0.0191 0.0324 0.0251 34 ILE A CA 233 C C . ILE A 34 ? 0.2621 0.2309 0.2525 0.0162 0.0283 0.0220 34 ILE A C 234 O O . ILE A 34 ? 0.2533 0.2254 0.2514 0.0145 0.0256 0.0229 34 ILE A O 235 C CB . ILE A 34 ? 0.2648 0.2369 0.2516 0.0212 0.0347 0.0255 34 ILE A CB 236 C CG1 . ILE A 34 ? 0.2671 0.2340 0.2493 0.0216 0.0349 0.0211 34 ILE A CG1 237 C CG2 . ILE A 34 ? 0.2614 0.2392 0.2574 0.0199 0.0328 0.0281 34 ILE A CG2 238 C CD1 . ILE A 34 ? 0.2645 0.2328 0.2468 0.0238 0.0372 0.0217 34 ILE A CD1 239 N N . LEU A 35 ? 0.2600 0.2236 0.2453 0.0156 0.0278 0.0183 35 LEU A N 240 C CA . LEU A 35 ? 0.2495 0.2121 0.2384 0.0132 0.0242 0.0152 35 LEU A CA 241 C C . LEU A 35 ? 0.2413 0.2037 0.2303 0.0135 0.0242 0.0123 35 LEU A C 242 O O . LEU A 35 ? 0.2241 0.1833 0.2070 0.0147 0.0263 0.0108 35 LEU A O 243 C CB . LEU A 35 ? 0.2488 0.2069 0.2329 0.0121 0.0231 0.0132 35 LEU A CB 244 C CG . LEU A 35 ? 0.2525 0.2101 0.2405 0.0099 0.0195 0.0101 35 LEU A CG 245 C CD1 . LEU A 35 ? 0.2547 0.2158 0.2515 0.0084 0.0162 0.0115 35 LEU A CD1 246 C CD2 . LEU A 35 ? 0.2626 0.2158 0.2455 0.0088 0.0186 0.0084 35 LEU A CD2 247 N N . LEU A 36 ? 0.2307 0.1962 0.2266 0.0122 0.0215 0.0114 36 LEU A N 248 C CA . LEU A 36 ? 0.2327 0.1992 0.2296 0.0121 0.0210 0.0087 36 LEU A CA 249 C C . LEU A 36 ? 0.2273 0.1929 0.2253 0.0105 0.0181 0.0048 36 LEU A C 250 O O . LEU A 36 ? 0.2147 0.1811 0.2174 0.0093 0.0151 0.0044 36 LEU A O 251 C CB . LEU A 36 ? 0.2394 0.2105 0.2424 0.0123 0.0204 0.0102 36 LEU A CB 252 C CG . LEU A 36 ? 0.2373 0.2108 0.2413 0.0136 0.0227 0.0149 36 LEU A CG 253 C CD1 . LEU A 36 ? 0.2392 0.2173 0.2504 0.0130 0.0209 0.0164 36 LEU A CD1 254 C CD2 . LEU A 36 ? 0.2509 0.2231 0.2491 0.0159 0.0267 0.0158 36 LEU A CD2 255 N N . VAL A 37 ? 0.2197 0.1841 0.2138 0.0106 0.0188 0.0023 37 VAL A N 256 C CA . VAL A 37 ? 0.2311 0.1956 0.2259 0.0093 0.0164 -0.0012 37 VAL A CA 257 C C . VAL A 37 ? 0.2075 0.1759 0.2045 0.0094 0.0159 -0.0034 37 VAL A C 258 O O . VAL A 37 ? 0.2023 0.1707 0.1958 0.0099 0.0179 -0.0030 37 VAL A O 259 C CB . VAL A 37 ? 0.2339 0.1941 0.2221 0.0089 0.0172 -0.0021 37 VAL A CB 260 C CG1 . VAL A 37 ? 0.2433 0.2046 0.2334 0.0076 0.0145 -0.0051 37 VAL A CG1 261 C CG2 . VAL A 37 ? 0.2549 0.2113 0.2395 0.0092 0.0184 0.0003 37 VAL A CG2 262 N N . PRO A 38 ? 0.2051 0.1768 0.2077 0.0089 0.0130 -0.0056 38 PRO A N 263 C CA . PRO A 38 ? 0.2134 0.1897 0.2185 0.0091 0.0123 -0.0076 38 PRO A CA 264 C C . PRO A 38 ? 0.2168 0.1952 0.2195 0.0087 0.0122 -0.0106 38 PRO A C 265 O O . PRO A 38 ? 0.2259 0.2020 0.2252 0.0081 0.0123 -0.0111 38 PRO A O 266 C CB . PRO A 38 ? 0.2127 0.1910 0.2247 0.0089 0.0087 -0.0093 38 PRO A CB 267 C CG . PRO A 38 ? 0.2083 0.1835 0.2208 0.0084 0.0072 -0.0096 38 PRO A CG 268 C CD . PRO A 38 ? 0.2146 0.1859 0.2216 0.0083 0.0101 -0.0064 38 PRO A CD 269 N N . GLY A 39 ? 0.2120 0.1951 0.2162 0.0089 0.0119 -0.0119 39 GLY A N 270 C CA . GLY A 39 ? 0.2149 0.2017 0.2171 0.0085 0.0121 -0.0138 39 GLY A CA 271 C C . GLY A 39 ? 0.2195 0.2103 0.2252 0.0087 0.0094 -0.0178 39 GLY A C 272 O O . GLY A 39 ? 0.2276 0.2177 0.2375 0.0092 0.0071 -0.0194 39 GLY A O 273 N N . THR A 40 ? 0.2094 0.2041 0.2133 0.0084 0.0096 -0.0194 40 THR A N 274 C CA . THR A 40 ? 0.2088 0.2083 0.2153 0.0090 0.0075 -0.0234 40 THR A CA 275 C C . THR A 40 ? 0.2146 0.2183 0.2255 0.0102 0.0056 -0.0262 40 THR A C 276 O O . THR A 40 ? 0.2137 0.2200 0.2245 0.0101 0.0064 -0.0253 40 THR A O 277 C CB . THR A 40 ? 0.1973 0.2020 0.2009 0.0083 0.0084 -0.0237 40 THR A CB 278 O OG1 . THR A 40 ? 0.1912 0.1912 0.1905 0.0070 0.0097 -0.0209 40 THR A OG1 279 C CG2 . THR A 40 ? 0.1976 0.2080 0.2037 0.0093 0.0065 -0.0277 40 THR A CG2 280 N N . GLY A 41 ? 0.2163 0.2204 0.2311 0.0113 0.0029 -0.0296 41 GLY A N 281 C CA . GLY A 41 ? 0.2272 0.2346 0.2459 0.0126 0.0004 -0.0329 41 GLY A CA 282 C C . GLY A 41 ? 0.2339 0.2368 0.2559 0.0124 -0.0008 -0.0311 41 GLY A C 283 O O . GLY A 41 ? 0.2511 0.2561 0.2757 0.0130 -0.0028 -0.0329 41 GLY A O 284 N N . THR A 42 ? 0.2347 0.2316 0.2562 0.0114 0.0000 -0.0274 42 THR A N 285 C CA . THR A 42 ? 0.2367 0.2300 0.2613 0.0109 -0.0010 -0.0245 42 THR A CA 286 C C . THR A 42 ? 0.2402 0.2282 0.2665 0.0104 -0.0020 -0.0225 42 THR A C 287 O O . THR A 42 ? 0.2431 0.2292 0.2670 0.0102 -0.0012 -0.0226 42 THR A O 288 C CB . THR A 42 ? 0.2422 0.2352 0.2640 0.0102 0.0022 -0.0201 42 THR A CB 289 O OG1 . THR A 42 ? 0.2356 0.2252 0.2527 0.0097 0.0051 -0.0172 42 THR A OG1 290 C CG2 . THR A 42 ? 0.2464 0.2451 0.2665 0.0104 0.0033 -0.0213 42 THR A CG2 291 N N . THR A 43 ? 0.2290 0.2147 0.2594 0.0100 -0.0040 -0.0205 43 THR A N 292 C CA . THR A 43 ? 0.2303 0.2118 0.2620 0.0091 -0.0042 -0.0168 43 THR A CA 293 C C . THR A 43 ? 0.2419 0.2228 0.2707 0.0085 -0.0006 -0.0116 43 THR A C 294 O O . THR A 43 ? 0.2386 0.2221 0.2656 0.0089 0.0013 -0.0110 43 THR A O 295 C CB . THR A 43 ? 0.2290 0.2091 0.2678 0.0087 -0.0089 -0.0169 43 THR A CB 296 O OG1 . THR A 43 ? 0.2184 0.2003 0.2593 0.0084 -0.0093 -0.0152 43 THR A OG1 297 C CG2 . THR A 43 ? 0.2359 0.2164 0.2780 0.0099 -0.0129 -0.0227 43 THR A CG2 298 N N . GLY A 44 ? 0.2457 0.2235 0.2742 0.0079 0.0000 -0.0077 44 GLY A N 299 C CA . GLY A 44 ? 0.2458 0.2235 0.2721 0.0079 0.0033 -0.0029 44 GLY A CA 300 C C . GLY A 44 ? 0.2472 0.2281 0.2770 0.0079 0.0028 -0.0013 44 GLY A C 301 O O . GLY A 44 ? 0.2335 0.2161 0.2604 0.0086 0.0057 -0.0002 44 GLY A O 302 N N . PRO A 45 ? 0.2576 0.2390 0.2940 0.0071 -0.0011 -0.0011 45 PRO A N 303 C CA . PRO A 45 ? 0.2569 0.2411 0.2970 0.0068 -0.0021 0.0009 45 PRO A CA 304 C C . PRO A 45 ? 0.2573 0.2444 0.2958 0.0075 -0.0016 -0.0024 45 PRO A C 305 O O . PRO A 45 ? 0.2326 0.2223 0.2709 0.0075 0.0000 -0.0001 45 PRO A O 306 C CB . PRO A 45 ? 0.2603 0.2434 0.3075 0.0056 -0.0076 0.0008 45 PRO A CB 307 C CG . PRO A 45 ? 0.2597 0.2397 0.3071 0.0052 -0.0083 0.0014 45 PRO A CG 308 C CD . PRO A 45 ? 0.2631 0.2420 0.3038 0.0063 -0.0049 -0.0012 45 PRO A CD 309 N N . GLN A 46 ? 0.2556 0.2429 0.2931 0.0080 -0.0031 -0.0078 46 GLN A N 310 C CA . GLN A 46 ? 0.2610 0.2521 0.2966 0.0086 -0.0025 -0.0109 46 GLN A CA 311 C C . GLN A 46 ? 0.2477 0.2402 0.2778 0.0090 0.0020 -0.0091 46 GLN A C 312 O O . GLN A 46 ? 0.2422 0.2382 0.2718 0.0090 0.0029 -0.0089 46 GLN A O 313 C CB . GLN A 46 ? 0.2940 0.2860 0.3295 0.0094 -0.0048 -0.0169 46 GLN A CB 314 C CG . GLN A 46 ? 0.3391 0.3295 0.3804 0.0094 -0.0101 -0.0194 46 GLN A CG 315 C CD . GLN A 46 ? 0.3811 0.3724 0.4225 0.0107 -0.0123 -0.0257 46 GLN A CD 316 O OE1 . GLN A 46 ? 0.3648 0.3579 0.4019 0.0115 -0.0098 -0.0275 46 GLN A OE1 317 N NE2 . GLN A 46 ? 0.3950 0.3851 0.4414 0.0112 -0.0174 -0.0289 46 GLN A NE2 318 N N . SER A 47 ? 0.2330 0.2227 0.2588 0.0092 0.0048 -0.0078 47 SER A N 319 C CA . SER A 47 ? 0.2357 0.2258 0.2560 0.0096 0.0089 -0.0061 47 SER A CA 320 C C . SER A 47 ? 0.2333 0.2234 0.2543 0.0099 0.0109 -0.0013 47 SER A C 321 O O . SER A 47 ? 0.2354 0.2276 0.2547 0.0102 0.0130 0.0000 47 SER A O 322 C CB . SER A 47 ? 0.2287 0.2150 0.2439 0.0098 0.0109 -0.0061 47 SER A CB 323 O OG . SER A 47 ? 0.2225 0.2101 0.2358 0.0096 0.0102 -0.0099 47 SER A OG 324 N N . PHE A 48 ? 0.2407 0.2289 0.2645 0.0097 0.0102 0.0015 48 PHE A N 325 C CA . PHE A 48 ? 0.2484 0.2367 0.2719 0.0103 0.0130 0.0067 48 PHE A CA 326 C C . PHE A 48 ? 0.2601 0.2513 0.2893 0.0099 0.0117 0.0105 48 PHE A C 327 O O . PHE A 48 ? 0.2474 0.2399 0.2762 0.0108 0.0146 0.0149 48 PHE A O 328 C CB . PHE A 48 ? 0.2611 0.2458 0.2816 0.0108 0.0147 0.0085 48 PHE A CB 329 C CG . PHE A 48 ? 0.2626 0.2440 0.2767 0.0112 0.0164 0.0058 48 PHE A CG 330 C CD1 . PHE A 48 ? 0.2690 0.2501 0.2784 0.0121 0.0192 0.0057 48 PHE A CD1 331 C CD2 . PHE A 48 ? 0.2627 0.2413 0.2759 0.0105 0.0148 0.0037 48 PHE A CD2 332 C CE1 . PHE A 48 ? 0.2768 0.2545 0.2805 0.0123 0.0204 0.0039 48 PHE A CE1 333 C CE2 . PHE A 48 ? 0.2657 0.2415 0.2732 0.0107 0.0161 0.0017 48 PHE A CE2 334 C CZ . PHE A 48 ? 0.2689 0.2440 0.2716 0.0114 0.0187 0.0018 48 PHE A CZ 335 N N . ASP A 49 ? 0.2702 0.2625 0.3049 0.0086 0.0074 0.0091 49 ASP A N 336 C CA . ASP A 49 ? 0.2685 0.2632 0.3091 0.0077 0.0055 0.0129 49 ASP A CA 337 C C . ASP A 49 ? 0.2822 0.2807 0.3229 0.0081 0.0074 0.0151 49 ASP A C 338 O O . ASP A 49 ? 0.2804 0.2815 0.3247 0.0079 0.0077 0.0203 49 ASP A O 339 C CB . ASP A 49 ? 0.2763 0.2710 0.3222 0.0063 0.0000 0.0098 49 ASP A CB 340 C CG . ASP A 49 ? 0.2793 0.2710 0.3284 0.0054 -0.0032 0.0098 49 ASP A CG 341 O OD1 . ASP A 49 ? 0.2634 0.2539 0.3116 0.0055 -0.0014 0.0134 49 ASP A OD1 342 O OD2 . ASP A 49 ? 0.2729 0.2636 0.3259 0.0047 -0.0081 0.0062 49 ASP A OD2 343 N N . SER A 50 ? 0.2596 0.2591 0.2968 0.0086 0.0085 0.0117 50 SER A N 344 C CA . SER A 50 ? 0.2549 0.2579 0.2920 0.0089 0.0102 0.0137 50 SER A CA 345 C C . SER A 50 ? 0.2653 0.2678 0.2982 0.0107 0.0152 0.0171 50 SER A C 346 O O . SER A 50 ? 0.2691 0.2744 0.3019 0.0111 0.0169 0.0190 50 SER A O 347 C CB . SER A 50 ? 0.2501 0.2550 0.2853 0.0086 0.0091 0.0090 50 SER A CB 348 O OG . SER A 50 ? 0.2323 0.2354 0.2621 0.0093 0.0110 0.0058 50 SER A OG 349 N N . ASN A 51 ? 0.2618 0.2608 0.2912 0.0117 0.0174 0.0176 51 ASN A N 350 C CA . ASN A 51 ? 0.2685 0.2659 0.2927 0.0137 0.0218 0.0194 51 ASN A CA 351 C C . ASN A 51 ? 0.2555 0.2503 0.2777 0.0149 0.0239 0.0217 51 ASN A C 352 O O . ASN A 51 ? 0.2403 0.2377 0.2654 0.0157 0.0250 0.0264 51 ASN A O 353 C CB . ASN A 51 ? 0.2610 0.2565 0.2798 0.0139 0.0228 0.0155 51 ASN A CB 354 C CG . ASN A 51 ? 0.2742 0.2674 0.2915 0.0128 0.0206 0.0110 51 ASN A CG 355 O OD1 . ASN A 51 ? 0.2700 0.2593 0.2842 0.0132 0.0213 0.0105 51 ASN A OD1 356 N ND2 . ASN A 51 ? 0.2876 0.2834 0.3071 0.0115 0.0177 0.0076 51 ASN A ND2 357 N N . TRP A 52 ? 0.2388 0.2293 0.2564 0.0151 0.0243 0.0190 52 TRP A N 358 C CA . TRP A 52 ? 0.2407 0.2286 0.2547 0.0167 0.0269 0.0212 52 TRP A CA 359 C C . TRP A 52 ? 0.2450 0.2341 0.2628 0.0159 0.0254 0.0238 52 TRP A C 360 O O . TRP A 52 ? 0.2372 0.2260 0.2527 0.0173 0.0278 0.0267 52 TRP A O 361 C CB . TRP A 52 ? 0.2356 0.2184 0.2426 0.0172 0.0280 0.0179 52 TRP A CB 362 C CG . TRP A 52 ? 0.2203 0.2020 0.2234 0.0187 0.0305 0.0176 52 TRP A CG 363 C CD1 . TRP A 52 ? 0.2164 0.1985 0.2189 0.0178 0.0296 0.0151 52 TRP A CD1 364 C CD2 . TRP A 52 ? 0.2184 0.1992 0.2183 0.0214 0.0341 0.0203 52 TRP A CD2 365 N NE1 . TRP A 52 ? 0.2253 0.2062 0.2246 0.0194 0.0321 0.0162 52 TRP A NE1 366 C CE2 . TRP A 52 ? 0.2239 0.2036 0.2215 0.0219 0.0348 0.0192 52 TRP A CE2 367 C CE3 . TRP A 52 ? 0.2337 0.2149 0.2327 0.0238 0.0367 0.0237 52 TRP A CE3 368 C CZ2 . TRP A 52 ? 0.2320 0.2101 0.2265 0.0246 0.0378 0.0210 52 TRP A CZ2 369 C CZ3 . TRP A 52 ? 0.2325 0.2125 0.2279 0.0268 0.0400 0.0252 52 TRP A CZ3 370 C CH2 . TRP A 52 ? 0.2361 0.2142 0.2295 0.0273 0.0404 0.0238 52 TRP A CH2 371 N N . ILE A 53 ? 0.2419 0.2324 0.2652 0.0137 0.0214 0.0230 53 ILE A N 372 C CA . ILE A 53 ? 0.2440 0.2360 0.2721 0.0126 0.0194 0.0263 53 ILE A CA 373 C C . ILE A 53 ? 0.2456 0.2426 0.2771 0.0135 0.0212 0.0321 53 ILE A C 374 O O . ILE A 53 ? 0.2615 0.2597 0.2917 0.0147 0.0236 0.0359 53 ILE A O 375 C CB . ILE A 53 ? 0.2397 0.2312 0.2734 0.0101 0.0139 0.0239 53 ILE A CB 376 C CG1 . ILE A 53 ? 0.2321 0.2192 0.2621 0.0098 0.0130 0.0194 53 ILE A CG1 377 C CG2 . ILE A 53 ? 0.2337 0.2274 0.2737 0.0086 0.0113 0.0286 53 ILE A CG2 378 C CD1 . ILE A 53 ? 0.2473 0.2335 0.2817 0.0081 0.0080 0.0154 53 ILE A CD1 379 N N . PRO A 54 ? 0.2637 0.2640 0.2992 0.0130 0.0201 0.0330 54 PRO A N 380 C CA . PRO A 54 ? 0.2621 0.2677 0.3014 0.0138 0.0218 0.0392 54 PRO A CA 381 C C . PRO A 54 ? 0.2800 0.2860 0.3139 0.0171 0.0273 0.0408 54 PRO A C 382 O O . PRO A 54 ? 0.2680 0.2774 0.3026 0.0186 0.0298 0.0457 54 PRO A O 383 C CB . PRO A 54 ? 0.2500 0.2584 0.2947 0.0121 0.0188 0.0392 54 PRO A CB 384 C CG . PRO A 54 ? 0.2467 0.2515 0.2885 0.0114 0.0170 0.0326 54 PRO A CG 385 C CD . PRO A 54 ? 0.2475 0.2477 0.2859 0.0112 0.0164 0.0293 54 PRO A CD 386 N N . LEU A 55 ? 0.2774 0.2798 0.3056 0.0183 0.0290 0.0367 55 LEU A N 387 C CA . LEU A 55 ? 0.2931 0.2943 0.3156 0.0217 0.0338 0.0377 55 LEU A CA 388 C C . LEU A 55 ? 0.2982 0.2973 0.3159 0.0237 0.0364 0.0385 55 LEU A C 389 O O . LEU A 55 ? 0.2913 0.2927 0.3071 0.0267 0.0402 0.0420 55 LEU A O 390 C CB . LEU A 55 ? 0.2878 0.2851 0.3053 0.0224 0.0347 0.0335 55 LEU A CB 391 C CG . LEU A 55 ? 0.3057 0.3061 0.3271 0.0212 0.0333 0.0335 55 LEU A CG 392 C CD1 . LEU A 55 ? 0.3148 0.3115 0.3313 0.0213 0.0336 0.0293 55 LEU A CD1 393 C CD2 . LEU A 55 ? 0.3177 0.3233 0.3430 0.0228 0.0353 0.0387 55 LEU A CD2 394 N N . SER A 56 ? 0.2798 0.2749 0.2950 0.0221 0.0346 0.0354 56 SER A N 395 C CA . SER A 56 ? 0.2791 0.2722 0.2895 0.0236 0.0366 0.0361 56 SER A CA 396 C C . SER A 56 ? 0.2747 0.2736 0.2899 0.0234 0.0366 0.0418 56 SER A C 397 O O . SER A 56 ? 0.2796 0.2801 0.2915 0.0259 0.0399 0.0444 56 SER A O 398 C CB . SER A 56 ? 0.2747 0.2621 0.2812 0.0220 0.0347 0.0316 56 SER A CB 399 O OG . SER A 56 ? 0.2810 0.2700 0.2931 0.0191 0.0309 0.0322 56 SER A OG 400 N N . THR A 57 ? 0.2720 0.2744 0.2949 0.0205 0.0329 0.0438 57 THR A N 401 C CA . THR A 57 ? 0.2801 0.2889 0.3089 0.0198 0.0324 0.0501 57 THR A CA 402 C C . THR A 57 ? 0.3017 0.3163 0.3311 0.0229 0.0365 0.0549 57 THR A C 403 O O . THR A 57 ? 0.2683 0.2873 0.2969 0.0247 0.0392 0.0592 57 THR A O 404 C CB . THR A 57 ? 0.2649 0.2758 0.3024 0.0162 0.0270 0.0512 57 THR A CB 405 O OG1 . THR A 57 ? 0.2814 0.2872 0.3190 0.0138 0.0231 0.0467 57 THR A OG1 406 C CG2 . THR A 57 ? 0.2701 0.2877 0.3145 0.0149 0.0258 0.0583 57 THR A CG2 407 N N . GLN A 58 ? 0.3186 0.3334 0.3489 0.0236 0.0370 0.0538 58 GLN A N 408 C CA . GLN A 58 ? 0.3455 0.3656 0.3769 0.0265 0.0406 0.0579 58 GLN A CA 409 C C . GLN A 58 ? 0.3613 0.3796 0.3848 0.0311 0.0458 0.0572 58 GLN A C 410 O O . GLN A 58 ? 0.3933 0.4168 0.4178 0.0341 0.0491 0.0612 58 GLN A O 411 C CB . GLN A 58 ? 0.3461 0.3666 0.3810 0.0255 0.0391 0.0570 58 GLN A CB 412 C CG . GLN A 58 ? 0.3717 0.3957 0.4151 0.0215 0.0342 0.0593 58 GLN A CG 413 C CD . GLN A 58 ? 0.4056 0.4323 0.4537 0.0205 0.0326 0.0601 58 GLN A CD 414 O OE1 . GLN A 58 ? 0.3708 0.3946 0.4155 0.0214 0.0337 0.0565 58 GLN A OE1 415 N NE2 . GLN A 58 ? 0.4104 0.4427 0.4667 0.0180 0.0294 0.0651 58 GLN A NE2 416 N N . LEU A 59 ? 0.3615 0.3727 0.3776 0.0316 0.0462 0.0521 59 LEU A N 417 C CA . LEU A 59 ? 0.3480 0.3560 0.3557 0.0357 0.0504 0.0507 59 LEU A CA 418 C C . LEU A 59 ? 0.3664 0.3762 0.3715 0.0363 0.0515 0.0527 59 LEU A C 419 O O . LEU A 59 ? 0.3595 0.3666 0.3570 0.0397 0.0547 0.0511 59 LEU A O 420 C CB . LEU A 59 ? 0.3518 0.3507 0.3525 0.0357 0.0499 0.0442 59 LEU A CB 421 C CG . LEU A 59 ? 0.3478 0.3450 0.3489 0.0364 0.0502 0.0425 59 LEU A CG 422 C CD1 . LEU A 59 ? 0.3529 0.3422 0.3489 0.0351 0.0486 0.0368 59 LEU A CD1 423 C CD2 . LEU A 59 ? 0.3486 0.3475 0.3474 0.0412 0.0545 0.0447 59 LEU A CD2 424 N N . GLY A 60 ? 0.3249 0.3391 0.3362 0.0330 0.0485 0.0560 60 GLY A N 425 C CA . GLY A 60 ? 0.3428 0.3605 0.3530 0.0332 0.0494 0.0593 60 GLY A CA 426 C C . GLY A 60 ? 0.3362 0.3486 0.3433 0.0306 0.0468 0.0561 60 GLY A C 427 O O . GLY A 60 ? 0.3414 0.3563 0.3467 0.0308 0.0475 0.0585 60 GLY A O 428 N N . TYR A 61 ? 0.3048 0.3104 0.3114 0.0282 0.0437 0.0509 61 TYR A N 429 C CA . TYR A 61 ? 0.2926 0.2931 0.2972 0.0255 0.0407 0.0477 61 TYR A CA 430 C C . TYR A 61 ? 0.2553 0.2578 0.2682 0.0212 0.0356 0.0495 61 TYR A C 431 O O . TYR A 61 ? 0.2516 0.2576 0.2718 0.0197 0.0335 0.0516 61 TYR A O 432 C CB . TYR A 61 ? 0.2976 0.2899 0.2972 0.0252 0.0398 0.0410 61 TYR A CB 433 C CG . TYR A 61 ? 0.3101 0.2985 0.3011 0.0289 0.0438 0.0387 61 TYR A CG 434 C CD1 . TYR A 61 ? 0.3188 0.3026 0.3018 0.0301 0.0450 0.0365 61 TYR A CD1 435 C CD2 . TYR A 61 ? 0.3297 0.3188 0.3207 0.0313 0.0460 0.0386 61 TYR A CD2 436 C CE1 . TYR A 61 ? 0.3373 0.3166 0.3121 0.0336 0.0482 0.0340 61 TYR A CE1 437 C CE2 . TYR A 61 ? 0.3458 0.3306 0.3291 0.0350 0.0492 0.0364 61 TYR A CE2 438 C CZ . TYR A 61 ? 0.3494 0.3293 0.3247 0.0362 0.0503 0.0340 61 TYR A CZ 439 O OH . TYR A 61 ? 0.3944 0.3692 0.3621 0.0397 0.0529 0.0316 61 TYR A OH 440 N N . THR A 62 ? 0.2474 0.2469 0.2591 0.0192 0.0333 0.0481 62 THR A N 441 C CA . THR A 62 ? 0.2432 0.2419 0.2620 0.0153 0.0279 0.0476 62 THR A CA 442 C C . THR A 62 ? 0.2468 0.2383 0.2625 0.0146 0.0262 0.0407 62 THR A C 443 O O . THR A 62 ? 0.2476 0.2345 0.2571 0.0149 0.0269 0.0377 62 THR A O 444 C CB . THR A 62 ? 0.2453 0.2457 0.2666 0.0131 0.0255 0.0509 62 THR A CB 445 O OG1 . THR A 62 ? 0.2483 0.2563 0.2717 0.0138 0.0275 0.0577 62 THR A OG1 446 C CG2 . THR A 62 ? 0.2348 0.2343 0.2646 0.0093 0.0193 0.0506 62 THR A CG2 447 N N . PRO A 63 ? 0.2427 0.2338 0.2629 0.0135 0.0237 0.0385 63 PRO A N 448 C CA . PRO A 63 ? 0.2476 0.2335 0.2657 0.0128 0.0220 0.0324 63 PRO A CA 449 C C . PRO A 63 ? 0.2512 0.2347 0.2722 0.0102 0.0177 0.0306 63 PRO A C 450 O O . PRO A 63 ? 0.2501 0.2361 0.2782 0.0082 0.0143 0.0335 63 PRO A O 451 C CB . PRO A 63 ? 0.2408 0.2287 0.2634 0.0125 0.0208 0.0314 63 PRO A CB 452 C CG . PRO A 63 ? 0.2427 0.2362 0.2724 0.0117 0.0196 0.0369 63 PRO A CG 453 C CD . PRO A 63 ? 0.2479 0.2441 0.2749 0.0131 0.0228 0.0417 63 PRO A CD 454 N N . CYS A 64 ? 0.2619 0.2407 0.2772 0.0104 0.0182 0.0268 64 CYS A N 455 C CA . CYS A 64 ? 0.2544 0.2303 0.2716 0.0083 0.0145 0.0243 64 CYS A CA 456 C C . CYS A 64 ? 0.2494 0.2222 0.2638 0.0086 0.0141 0.0186 64 CYS A C 457 O O . CYS A 64 ? 0.2466 0.2185 0.2559 0.0102 0.0172 0.0171 64 CYS A O 458 C CB . CYS A 64 ? 0.2719 0.2459 0.2846 0.0081 0.0154 0.0256 64 CYS A CB 459 S SG . CYS A 64 ? 0.2934 0.2727 0.3078 0.0083 0.0170 0.0329 64 CYS A SG 460 N N . TRP A 65 ? 0.2422 0.2136 0.2603 0.0071 0.0103 0.0155 65 TRP A N 461 C CA . TRP A 65 ? 0.2468 0.2165 0.2630 0.0073 0.0097 0.0104 65 TRP A CA 462 C C . TRP A 65 ? 0.2427 0.2104 0.2614 0.0060 0.0061 0.0078 65 TRP A C 463 O O . TRP A 65 ? 0.2526 0.2203 0.2759 0.0048 0.0033 0.0098 65 TRP A O 464 C CB . TRP A 65 ? 0.2545 0.2271 0.2745 0.0076 0.0087 0.0087 65 TRP A CB 465 C CG . TRP A 65 ? 0.2688 0.2434 0.2971 0.0065 0.0047 0.0099 65 TRP A CG 466 C CD1 . TRP A 65 ? 0.2807 0.2546 0.3141 0.0055 0.0001 0.0070 65 TRP A CD1 467 C CD2 . TRP A 65 ? 0.2863 0.2639 0.3187 0.0061 0.0046 0.0148 65 TRP A CD2 468 N NE1 . TRP A 65 ? 0.2798 0.2553 0.3202 0.0045 -0.0030 0.0096 65 TRP A NE1 469 C CE2 . TRP A 65 ? 0.2956 0.2736 0.3356 0.0046 -0.0004 0.0146 65 TRP A CE2 470 C CE3 . TRP A 65 ? 0.2881 0.2681 0.3186 0.0071 0.0083 0.0193 65 TRP A CE3 471 C CZ2 . TRP A 65 ? 0.3159 0.2968 0.3619 0.0036 -0.0022 0.0192 65 TRP A CZ2 472 C CZ3 . TRP A 65 ? 0.2977 0.2813 0.3340 0.0064 0.0070 0.0240 65 TRP A CZ3 473 C CH2 . TRP A 65 ? 0.3148 0.2988 0.3590 0.0044 0.0016 0.0242 65 TRP A CH2 474 N N . ILE A 66 ? 0.2447 0.2111 0.2604 0.0062 0.0062 0.0035 66 ILE A N 475 C CA . ILE A 66 ? 0.2385 0.2039 0.2568 0.0055 0.0029 0.0003 66 ILE A CA 476 C C . ILE A 66 ? 0.2252 0.1930 0.2468 0.0061 0.0011 -0.0038 66 ILE A C 477 O O . ILE A 66 ? 0.2176 0.1873 0.2368 0.0069 0.0031 -0.0049 66 ILE A O 478 C CB . ILE A 66 ? 0.2493 0.2118 0.2615 0.0052 0.0042 -0.0009 66 ILE A CB 479 C CG1 . ILE A 66 ? 0.2584 0.2205 0.2638 0.0061 0.0077 -0.0021 66 ILE A CG1 480 C CG2 . ILE A 66 ? 0.2579 0.2180 0.2675 0.0045 0.0049 0.0024 66 ILE A CG2 481 C CD1 . ILE A 66 ? 0.2654 0.2250 0.2660 0.0055 0.0079 -0.0040 66 ILE A CD1 482 N N . SER A 67 ? 0.2269 0.1947 0.2536 0.0058 -0.0027 -0.0065 67 SER A N 483 C CA . SER A 67 ? 0.2316 0.2020 0.2614 0.0067 -0.0049 -0.0111 67 SER A CA 484 C C . SER A 67 ? 0.2366 0.2067 0.2669 0.0071 -0.0068 -0.0150 67 SER A C 485 O O . SER A 67 ? 0.2392 0.2090 0.2751 0.0073 -0.0106 -0.0171 67 SER A O 486 C CB . SER A 67 ? 0.2343 0.2055 0.2711 0.0066 -0.0085 -0.0110 67 SER A CB 487 O OG . SER A 67 ? 0.2304 0.2029 0.2663 0.0064 -0.0063 -0.0075 67 SER A OG 488 N N . PRO A 68 ? 0.2353 0.2052 0.2599 0.0070 -0.0042 -0.0156 68 PRO A N 489 C CA . PRO A 68 ? 0.2330 0.2032 0.2585 0.0072 -0.0060 -0.0186 68 PRO A CA 490 C C . PRO A 68 ? 0.2325 0.2067 0.2620 0.0089 -0.0083 -0.0234 68 PRO A C 491 O O . PRO A 68 ? 0.2327 0.2104 0.2604 0.0096 -0.0067 -0.0250 68 PRO A O 492 C CB . PRO A 68 ? 0.2316 0.2017 0.2503 0.0067 -0.0028 -0.0180 68 PRO A CB 493 C CG . PRO A 68 ? 0.2347 0.2022 0.2488 0.0060 0.0001 -0.0140 68 PRO A CG 494 C CD . PRO A 68 ? 0.2432 0.2124 0.2607 0.0067 0.0000 -0.0134 68 PRO A CD 495 N N . PRO A 69 ? 0.2392 0.2130 0.2739 0.0095 -0.0119 -0.0259 69 PRO A N 496 C CA . PRO A 69 ? 0.2436 0.2208 0.2820 0.0116 -0.0143 -0.0310 69 PRO A CA 497 C C . PRO A 69 ? 0.2548 0.2366 0.2910 0.0128 -0.0133 -0.0345 69 PRO A C 498 O O . PRO A 69 ? 0.2455 0.2267 0.2786 0.0118 -0.0117 -0.0328 69 PRO A O 499 C CB . PRO A 69 ? 0.2482 0.2223 0.2938 0.0119 -0.0192 -0.0318 69 PRO A CB 500 C CG . PRO A 69 ? 0.2491 0.2197 0.2939 0.0102 -0.0190 -0.0283 69 PRO A CG 501 C CD . PRO A 69 ? 0.2483 0.2182 0.2862 0.0086 -0.0145 -0.0242 69 PRO A CD 502 N N . PRO A 70 ? 0.2528 0.2397 0.2901 0.0149 -0.0139 -0.0389 70 PRO A N 503 C CA . PRO A 70 ? 0.2526 0.2408 0.2918 0.0157 -0.0150 -0.0405 70 PRO A CA 504 C C . PRO A 70 ? 0.2468 0.2378 0.2807 0.0148 -0.0111 -0.0384 70 PRO A C 505 O O . PRO A 70 ? 0.2314 0.2270 0.2619 0.0151 -0.0090 -0.0396 70 PRO A O 506 C CB . PRO A 70 ? 0.2623 0.2555 0.3040 0.0186 -0.0172 -0.0467 70 PRO A CB 507 C CG . PRO A 70 ? 0.2608 0.2578 0.3000 0.0191 -0.0153 -0.0475 70 PRO A CG 508 C CD . PRO A 70 ? 0.2535 0.2461 0.2897 0.0164 -0.0132 -0.0422 70 PRO A CD 509 N N . PHE A 71 ? 0.2398 0.2282 0.2735 0.0136 -0.0104 -0.0352 71 PHE A N 510 C CA . PHE A 71 ? 0.2494 0.2404 0.2790 0.0130 -0.0072 -0.0333 71 PHE A CA 511 C C . PHE A 71 ? 0.2369 0.2289 0.2605 0.0120 -0.0034 -0.0311 71 PHE A C 512 O O . PHE A 71 ? 0.2303 0.2267 0.2511 0.0121 -0.0015 -0.0315 71 PHE A O 513 C CB . PHE A 71 ? 0.2563 0.2530 0.2873 0.0146 -0.0085 -0.0376 71 PHE A CB 514 C CG . PHE A 71 ? 0.2764 0.2713 0.3132 0.0155 -0.0128 -0.0400 71 PHE A CG 515 C CD1 . PHE A 71 ? 0.2950 0.2870 0.3337 0.0143 -0.0136 -0.0368 71 PHE A CD1 516 C CD2 . PHE A 71 ? 0.2865 0.2824 0.3269 0.0176 -0.0164 -0.0452 71 PHE A CD2 517 C CE1 . PHE A 71 ? 0.3068 0.2966 0.3510 0.0147 -0.0181 -0.0384 71 PHE A CE1 518 C CE2 . PHE A 71 ? 0.2937 0.2867 0.3393 0.0183 -0.0209 -0.0473 71 PHE A CE2 519 C CZ . PHE A 71 ? 0.3022 0.2921 0.3497 0.0166 -0.0219 -0.0437 71 PHE A CZ 520 N N . MET A 72 ? 0.2292 0.2172 0.2509 0.0110 -0.0027 -0.0288 72 MET A N 521 C CA . MET A 72 ? 0.2254 0.2133 0.2414 0.0099 0.0002 -0.0268 72 MET A CA 522 C C . MET A 72 ? 0.2158 0.2097 0.2304 0.0104 0.0005 -0.0295 72 MET A C 523 O O . MET A 72 ? 0.2150 0.2100 0.2251 0.0093 0.0028 -0.0277 72 MET A O 524 C CB . MET A 72 ? 0.2221 0.2085 0.2342 0.0091 0.0032 -0.0233 72 MET A CB 525 C CG . MET A 72 ? 0.2220 0.2029 0.2342 0.0086 0.0036 -0.0196 72 MET A CG 526 S SD . MET A 72 ? 0.2297 0.2049 0.2372 0.0074 0.0049 -0.0170 72 MET A SD 527 C CE . MET A 72 ? 0.2339 0.2094 0.2346 0.0068 0.0081 -0.0158 72 MET A CE 528 N N . LEU A 73 ? 0.2113 0.2092 0.2300 0.0120 -0.0018 -0.0337 73 LEU A N 529 C CA . LEU A 73 ? 0.2106 0.2155 0.2289 0.0129 -0.0017 -0.0364 73 LEU A CA 530 C C . LEU A 73 ? 0.2038 0.2081 0.2220 0.0126 -0.0022 -0.0362 73 LEU A C 531 O O . LEU A 73 ? 0.2014 0.2115 0.2185 0.0128 -0.0016 -0.0371 73 LEU A O 532 C CB . LEU A 73 ? 0.2212 0.2310 0.2439 0.0155 -0.0041 -0.0414 73 LEU A CB 533 C CG . LEU A 73 ? 0.2271 0.2387 0.2497 0.0158 -0.0038 -0.0418 73 LEU A CG 534 C CD1 . LEU A 73 ? 0.2307 0.2472 0.2569 0.0185 -0.0064 -0.0474 73 LEU A CD1 535 C CD2 . LEU A 73 ? 0.2337 0.2493 0.2516 0.0145 -0.0006 -0.0394 73 LEU A CD2 536 N N . ASN A 74 ? 0.2146 0.2127 0.2346 0.0121 -0.0037 -0.0351 74 ASN A N 537 C CA . ASN A 74 ? 0.2257 0.2227 0.2460 0.0115 -0.0045 -0.0346 74 ASN A CA 538 C C . ASN A 74 ? 0.2197 0.2130 0.2341 0.0089 -0.0023 -0.0303 74 ASN A C 539 O O . ASN A 74 ? 0.2067 0.1977 0.2171 0.0078 -0.0002 -0.0279 74 ASN A O 540 C CB . ASN A 74 ? 0.2479 0.2406 0.2732 0.0122 -0.0076 -0.0355 74 ASN A CB 541 C CG . ASN A 74 ? 0.2738 0.2714 0.3046 0.0150 -0.0103 -0.0404 74 ASN A CG 542 O OD1 . ASN A 74 ? 0.2442 0.2488 0.2749 0.0168 -0.0097 -0.0435 74 ASN A OD1 543 N ND2 . ASN A 74 ? 0.3084 0.3021 0.3438 0.0156 -0.0133 -0.0411 74 ASN A ND2 544 N N . ASP A 75 ? 0.2178 0.2114 0.2318 0.0081 -0.0029 -0.0297 75 ASP A N 545 C CA . ASP A 75 ? 0.2124 0.2027 0.2209 0.0056 -0.0016 -0.0261 75 ASP A CA 546 C C . ASP A 75 ? 0.2219 0.2051 0.2259 0.0042 0.0000 -0.0230 75 ASP A C 547 O O . ASP A 75 ? 0.1998 0.1781 0.2051 0.0043 -0.0006 -0.0221 75 ASP A O 548 C CB . ASP A 75 ? 0.2089 0.1974 0.2194 0.0050 -0.0036 -0.0259 75 ASP A CB 549 C CG . ASP A 75 ? 0.2063 0.1913 0.2117 0.0024 -0.0030 -0.0225 75 ASP A CG 550 O OD1 . ASP A 75 ? 0.2068 0.1896 0.2067 0.0009 -0.0012 -0.0203 75 ASP A OD1 551 O OD2 . ASP A 75 ? 0.2066 0.1908 0.2136 0.0017 -0.0047 -0.0221 75 ASP A OD2 552 N N . THR A 76 ? 0.2119 0.1951 0.2109 0.0031 0.0021 -0.0212 76 THR A N 553 C CA . THR A 76 ? 0.2241 0.2008 0.2179 0.0022 0.0039 -0.0183 76 THR A CA 554 C C . THR A 76 ? 0.2163 0.1861 0.2073 0.0009 0.0035 -0.0162 76 THR A C 555 O O . THR A 76 ? 0.2083 0.1732 0.1974 0.0011 0.0045 -0.0145 76 THR A O 556 C CB . THR A 76 ? 0.2282 0.2060 0.2173 0.0011 0.0055 -0.0168 76 THR A CB 557 O OG1 . THR A 76 ? 0.2325 0.2169 0.2242 0.0023 0.0061 -0.0185 76 THR A OG1 558 C CG2 . THR A 76 ? 0.2368 0.2074 0.2202 0.0005 0.0073 -0.0141 76 THR A CG2 559 N N . GLN A 77 ? 0.2250 0.1950 0.2161 -0.0001 0.0019 -0.0161 77 GLN A N 560 C CA . GLN A 77 ? 0.2270 0.1908 0.2153 -0.0015 0.0012 -0.0141 77 GLN A CA 561 C C . GLN A 77 ? 0.2375 0.1995 0.2302 -0.0006 0.0001 -0.0143 77 GLN A C 562 O O . GLN A 77 ? 0.2359 0.1927 0.2258 -0.0014 0.0004 -0.0120 77 GLN A O 563 C CB . GLN A 77 ? 0.2234 0.1885 0.2115 -0.0031 -0.0004 -0.0138 77 GLN A CB 564 C CG . GLN A 77 ? 0.2329 0.1997 0.2169 -0.0045 0.0002 -0.0129 77 GLN A CG 565 C CD . GLN A 77 ? 0.2242 0.1943 0.2093 -0.0059 -0.0016 -0.0125 77 GLN A CD 566 O OE1 . GLN A 77 ? 0.2383 0.2042 0.2188 -0.0082 -0.0023 -0.0103 77 GLN A OE1 567 N NE2 . GLN A 77 ? 0.2211 0.1990 0.2124 -0.0044 -0.0025 -0.0148 77 GLN A NE2 568 N N . VAL A 78 ? 0.2266 0.1932 0.2261 0.0009 -0.0013 -0.0168 78 VAL A N 569 C CA . VAL A 78 ? 0.2264 0.1916 0.2312 0.0017 -0.0031 -0.0169 78 VAL A CA 570 C C . VAL A 78 ? 0.2260 0.1896 0.2299 0.0023 -0.0014 -0.0157 78 VAL A C 571 O O . VAL A 78 ? 0.2162 0.1763 0.2205 0.0019 -0.0016 -0.0134 78 VAL A O 572 C CB . VAL A 78 ? 0.2228 0.1926 0.2352 0.0034 -0.0058 -0.0204 78 VAL A CB 573 C CG1 . VAL A 78 ? 0.2326 0.2003 0.2506 0.0040 -0.0080 -0.0202 78 VAL A CG1 574 C CG2 . VAL A 78 ? 0.2257 0.1976 0.2397 0.0030 -0.0075 -0.0212 78 VAL A CG2 575 N N . ASN A 79 ? 0.2192 0.1857 0.2220 0.0032 0.0002 -0.0168 79 ASN A N 576 C CA . ASN A 79 ? 0.2163 0.1815 0.2183 0.0038 0.0019 -0.0153 79 ASN A CA 577 C C . ASN A 79 ? 0.2107 0.1706 0.2068 0.0029 0.0039 -0.0119 79 ASN A C 578 O O . ASN A 79 ? 0.2019 0.1600 0.1985 0.0032 0.0046 -0.0097 79 ASN A O 579 C CB . ASN A 79 ? 0.2161 0.1853 0.2170 0.0046 0.0035 -0.0167 79 ASN A CB 580 C CG . ASN A 79 ? 0.2155 0.1908 0.2218 0.0059 0.0016 -0.0205 79 ASN A CG 581 O OD1 . ASN A 79 ? 0.2203 0.1963 0.2320 0.0066 -0.0010 -0.0223 79 ASN A OD1 582 N ND2 . ASN A 79 ? 0.2066 0.1863 0.2115 0.0062 0.0029 -0.0216 79 ASN A ND2 583 N N . THR A 80 ? 0.2129 0.1703 0.2033 0.0018 0.0047 -0.0113 80 THR A N 584 C CA . THR A 80 ? 0.2245 0.1765 0.2084 0.0012 0.0065 -0.0086 80 THR A CA 585 C C . THR A 80 ? 0.2322 0.1816 0.2173 0.0005 0.0052 -0.0068 80 THR A C 586 O O . THR A 80 ? 0.2269 0.1734 0.2088 0.0007 0.0067 -0.0045 80 THR A O 587 C CB . THR A 80 ? 0.2239 0.1732 0.2014 0.0000 0.0069 -0.0085 80 THR A CB 588 O OG1 . THR A 80 ? 0.2241 0.1763 0.2011 0.0003 0.0078 -0.0096 80 THR A OG1 589 C CG2 . THR A 80 ? 0.2312 0.1741 0.2011 -0.0001 0.0087 -0.0063 80 THR A CG2 590 N N . GLU A 81 ? 0.2327 0.1836 0.2226 -0.0001 0.0024 -0.0078 81 GLU A N 591 C CA . GLU A 81 ? 0.2337 0.1826 0.2256 -0.0010 0.0008 -0.0057 81 GLU A CA 592 C C . GLU A 81 ? 0.2385 0.1881 0.2337 -0.0001 0.0012 -0.0038 81 GLU A C 593 O O . GLU A 81 ? 0.2316 0.1791 0.2246 -0.0006 0.0019 -0.0008 81 GLU A O 594 C CB . GLU A 81 ? 0.2456 0.1966 0.2440 -0.0014 -0.0026 -0.0072 81 GLU A CB 595 C CG . GLU A 81 ? 0.2456 0.1967 0.2415 -0.0025 -0.0032 -0.0084 81 GLU A CG 596 C CD . GLU A 81 ? 0.2513 0.2048 0.2537 -0.0026 -0.0065 -0.0098 81 GLU A CD 597 O OE1 . GLU A 81 ? 0.2701 0.2232 0.2779 -0.0026 -0.0087 -0.0090 81 GLU A OE1 598 O OE2 . GLU A 81 ? 0.2539 0.2103 0.2567 -0.0025 -0.0070 -0.0117 81 GLU A OE2 599 N N . TYR A 82 ? 0.2369 0.1899 0.2373 0.0010 0.0007 -0.0055 82 TYR A N 600 C CA . TYR A 82 ? 0.2277 0.1816 0.2313 0.0017 0.0010 -0.0034 82 TYR A CA 601 C C . TYR A 82 ? 0.2243 0.1766 0.2216 0.0022 0.0047 -0.0006 82 TYR A C 602 O O . TYR A 82 ? 0.2153 0.1673 0.2129 0.0021 0.0052 0.0026 82 TYR A O 603 C CB . TYR A 82 ? 0.2297 0.1874 0.2388 0.0029 0.0000 -0.0060 82 TYR A CB 604 C CG . TYR A 82 ? 0.2287 0.1880 0.2453 0.0030 -0.0039 -0.0084 82 TYR A CG 605 C CD1 . TYR A 82 ? 0.2385 0.1996 0.2560 0.0035 -0.0051 -0.0123 82 TYR A CD1 606 C CD2 . TYR A 82 ? 0.2312 0.1903 0.2544 0.0026 -0.0069 -0.0068 82 TYR A CD2 607 C CE1 . TYR A 82 ? 0.2267 0.1894 0.2511 0.0042 -0.0088 -0.0151 82 TYR A CE1 608 C CE2 . TYR A 82 ? 0.2359 0.1957 0.2662 0.0030 -0.0111 -0.0096 82 TYR A CE2 609 C CZ . TYR A 82 ? 0.2354 0.1970 0.2661 0.0040 -0.0119 -0.0139 82 TYR A CZ 610 O OH . TYR A 82 ? 0.2416 0.2039 0.2789 0.0050 -0.0158 -0.0170 82 TYR A OH 611 N N . MET A 83 ? 0.2252 0.1766 0.2170 0.0028 0.0071 -0.0019 83 MET A N 612 C CA . MET A 83 ? 0.2462 0.1957 0.2319 0.0038 0.0104 0.0000 83 MET A CA 613 C C . MET A 83 ? 0.2469 0.1926 0.2266 0.0033 0.0114 0.0023 83 MET A C 614 O O . MET A 83 ? 0.2308 0.1767 0.2091 0.0042 0.0132 0.0051 83 MET A O 615 C CB . MET A 83 ? 0.2804 0.2293 0.2618 0.0045 0.0122 -0.0018 83 MET A CB 616 C CG . MET A 83 ? 0.3230 0.2705 0.3000 0.0061 0.0154 0.0002 83 MET A CG 617 S SD . MET A 83 ? 0.4778 0.4201 0.4454 0.0064 0.0173 -0.0004 83 MET A SD 618 C CE . MET A 83 ? 0.3472 0.2852 0.3103 0.0049 0.0160 -0.0002 83 MET A CE 619 N N . VAL A 84 ? 0.2332 0.1761 0.2097 0.0020 0.0101 0.0013 84 VAL A N 620 C CA . VAL A 84 ? 0.2452 0.1843 0.2156 0.0012 0.0106 0.0031 84 VAL A CA 621 C C . VAL A 84 ? 0.2507 0.1918 0.2251 0.0007 0.0095 0.0061 84 VAL A C 622 O O . VAL A 84 ? 0.2462 0.1868 0.2168 0.0014 0.0114 0.0087 84 VAL A O 623 C CB . VAL A 84 ? 0.2388 0.1752 0.2065 -0.0005 0.0086 0.0014 84 VAL A CB 624 C CG1 . VAL A 84 ? 0.2520 0.1847 0.2139 -0.0017 0.0083 0.0032 84 VAL A CG1 625 C CG2 . VAL A 84 ? 0.2453 0.1800 0.2087 -0.0002 0.0096 -0.0006 84 VAL A CG2 626 N N . ASN A 85 ? 0.2556 0.1991 0.2379 -0.0004 0.0063 0.0059 85 ASN A N 627 C CA . ASN A 85 ? 0.2523 0.1981 0.2401 -0.0012 0.0046 0.0092 85 ASN A CA 628 C C . ASN A 85 ? 0.2582 0.2067 0.2472 0.0001 0.0067 0.0120 85 ASN A C 629 O O . ASN A 85 ? 0.2585 0.2083 0.2469 -0.0002 0.0072 0.0159 85 ASN A O 630 C CB . ASN A 85 ? 0.2427 0.1904 0.2399 -0.0021 0.0005 0.0078 85 ASN A CB 631 C CG . ASN A 85 ? 0.2574 0.2069 0.2609 -0.0033 -0.0019 0.0115 85 ASN A CG 632 O OD1 . ASN A 85 ? 0.2614 0.2098 0.2632 -0.0048 -0.0028 0.0140 85 ASN A OD1 633 N ND2 . ASN A 85 ? 0.2471 0.1993 0.2578 -0.0029 -0.0034 0.0121 85 ASN A ND2 634 N N . ALA A 86 ? 0.2609 0.2109 0.2514 0.0016 0.0080 0.0104 86 ALA A N 635 C CA . ALA A 86 ? 0.2630 0.2159 0.2548 0.0029 0.0100 0.0131 86 ALA A CA 636 C C . ALA A 86 ? 0.2633 0.2153 0.2473 0.0043 0.0138 0.0152 86 ALA A C 637 O O . ALA A 86 ? 0.2606 0.2156 0.2458 0.0047 0.0148 0.0192 86 ALA A O 638 C CB . ALA A 86 ? 0.2558 0.2106 0.2511 0.0040 0.0103 0.0109 86 ALA A CB 639 N N . ILE A 87 ? 0.2702 0.2181 0.2463 0.0052 0.0158 0.0127 87 ILE A N 640 C CA . ILE A 87 ? 0.2845 0.2304 0.2520 0.0070 0.0193 0.0139 87 ILE A CA 641 C C . ILE A 87 ? 0.3013 0.2473 0.2661 0.0061 0.0190 0.0168 87 ILE A C 642 O O . ILE A 87 ? 0.3145 0.2631 0.2773 0.0076 0.0213 0.0199 87 ILE A O 643 C CB . ILE A 87 ? 0.2897 0.2302 0.2494 0.0077 0.0204 0.0106 87 ILE A CB 644 C CG1 . ILE A 87 ? 0.2870 0.2280 0.2488 0.0086 0.0211 0.0084 87 ILE A CG1 645 C CG2 . ILE A 87 ? 0.2886 0.2260 0.2390 0.0097 0.0234 0.0115 87 ILE A CG2 646 C CD1 . ILE A 87 ? 0.3030 0.2471 0.2659 0.0110 0.0238 0.0104 87 ILE A CD1 647 N N . THR A 88 ? 0.2988 0.2430 0.2646 0.0037 0.0160 0.0161 88 THR A N 648 C CA . THR A 88 ? 0.2839 0.2288 0.2483 0.0024 0.0151 0.0192 88 THR A CA 649 C C . THR A 88 ? 0.2857 0.2368 0.2571 0.0021 0.0147 0.0239 88 THR A C 650 O O . THR A 88 ? 0.2795 0.2332 0.2475 0.0030 0.0168 0.0272 88 THR A O 651 C CB . THR A 88 ? 0.2822 0.2250 0.2489 -0.0003 0.0114 0.0179 88 THR A CB 652 O OG1 . THR A 88 ? 0.2749 0.2127 0.2358 -0.0002 0.0116 0.0141 88 THR A OG1 653 C CG2 . THR A 88 ? 0.2845 0.2278 0.2499 -0.0022 0.0100 0.0212 88 THR A CG2 654 N N . ALA A 89 ? 0.2743 0.2280 0.2553 0.0011 0.0120 0.0242 89 ALA A N 655 C CA . ALA A 89 ? 0.2683 0.2276 0.2569 0.0004 0.0109 0.0288 89 ALA A CA 656 C C . ALA A 89 ? 0.2683 0.2316 0.2551 0.0028 0.0148 0.0316 89 ALA A C 657 O O . ALA A 89 ? 0.2691 0.2370 0.2572 0.0026 0.0153 0.0364 89 ALA A O 658 C CB . ALA A 89 ? 0.2611 0.2212 0.2596 -0.0007 0.0070 0.0276 89 ALA A CB 659 N N . LEU A 90 ? 0.2597 0.2216 0.2437 0.0051 0.0173 0.0288 90 LEU A N 660 C CA . LEU A 90 ? 0.2793 0.2452 0.2628 0.0076 0.0208 0.0312 90 LEU A CA 661 C C . LEU A 90 ? 0.2930 0.2588 0.2671 0.0101 0.0249 0.0323 90 LEU A C 662 O O . LEU A 90 ? 0.3026 0.2739 0.2771 0.0118 0.0275 0.0363 90 LEU A O 663 C CB . LEU A 90 ? 0.2785 0.2431 0.2631 0.0090 0.0216 0.0280 90 LEU A CB 664 C CG . LEU A 90 ? 0.2710 0.2371 0.2651 0.0072 0.0179 0.0271 90 LEU A CG 665 C CD1 . LEU A 90 ? 0.2696 0.2334 0.2624 0.0084 0.0188 0.0228 90 LEU A CD1 666 C CD2 . LEU A 90 ? 0.2729 0.2450 0.2747 0.0066 0.0169 0.0321 90 LEU A CD2 667 N N . TYR A 91 ? 0.2992 0.2592 0.2651 0.0103 0.0255 0.0289 91 TYR A N 668 C CA . TYR A 91 ? 0.3104 0.2694 0.2665 0.0125 0.0287 0.0295 91 TYR A CA 669 C C . TYR A 91 ? 0.3172 0.2821 0.2752 0.0113 0.0283 0.0348 91 TYR A C 670 O O . TYR A 91 ? 0.3037 0.2736 0.2593 0.0137 0.0315 0.0380 91 TYR A O 671 C CB . TYR A 91 ? 0.3126 0.2641 0.2608 0.0119 0.0279 0.0254 91 TYR A CB 672 C CG . TYR A 91 ? 0.3266 0.2757 0.2637 0.0143 0.0308 0.0249 91 TYR A CG 673 C CD1 . TYR A 91 ? 0.3278 0.2745 0.2583 0.0181 0.0344 0.0229 91 TYR A CD1 674 C CD2 . TYR A 91 ? 0.3436 0.2922 0.2765 0.0128 0.0298 0.0261 91 TYR A CD2 675 C CE1 . TYR A 91 ? 0.3444 0.2881 0.2644 0.0207 0.0367 0.0217 91 TYR A CE1 676 C CE2 . TYR A 91 ? 0.3640 0.3101 0.2862 0.0151 0.0322 0.0252 91 TYR A CE2 677 C CZ . TYR A 91 ? 0.3700 0.3133 0.2857 0.0191 0.0356 0.0227 91 TYR A CZ 678 O OH . TYR A 91 ? 0.4137 0.3541 0.3185 0.0218 0.0377 0.0213 91 TYR A OH 679 N N . ALA A 92 ? 0.3084 0.2732 0.2712 0.0078 0.0243 0.0357 92 ALA A N 680 C CA . ALA A 92 ? 0.3283 0.2987 0.2939 0.0060 0.0231 0.0412 92 ALA A CA 681 C C . ALA A 92 ? 0.3240 0.3024 0.2978 0.0061 0.0234 0.0465 92 ALA A C 682 O O . ALA A 92 ? 0.3393 0.3242 0.3116 0.0071 0.0256 0.0512 92 ALA A O 683 C CB . ALA A 92 ? 0.3354 0.3037 0.3059 0.0021 0.0183 0.0412 92 ALA A CB 684 N N . GLY A 93 ? 0.3142 0.2927 0.2964 0.0052 0.0211 0.0457 93 GLY A N 685 C CA . GLY A 93 ? 0.2941 0.2795 0.2848 0.0049 0.0207 0.0506 93 GLY A CA 686 C C . GLY A 93 ? 0.3027 0.2929 0.2906 0.0084 0.0254 0.0526 93 GLY A C 687 O O . GLY A 93 ? 0.2812 0.2785 0.2755 0.0080 0.0252 0.0579 93 GLY A O 688 N N . SER A 94 ? 0.3110 0.2974 0.2896 0.0118 0.0294 0.0487 94 SER A N 689 C CA . SER A 94 ? 0.3270 0.3177 0.3025 0.0157 0.0340 0.0504 94 SER A CA 690 C C . SER A 94 ? 0.3541 0.3470 0.3204 0.0182 0.0377 0.0518 94 SER A C 691 O O . SER A 94 ? 0.3623 0.3567 0.3230 0.0223 0.0420 0.0513 94 SER A O 692 C CB . SER A 94 ? 0.3272 0.3123 0.2994 0.0181 0.0358 0.0451 94 SER A CB 693 O OG . SER A 94 ? 0.3299 0.3067 0.2938 0.0185 0.0360 0.0396 94 SER A OG 694 N N . GLY A 95 ? 0.3660 0.3589 0.3304 0.0158 0.0358 0.0532 95 GLY A N 695 C CA . GLY A 95 ? 0.3775 0.3728 0.3327 0.0179 0.0388 0.0544 95 GLY A CA 696 C C . GLY A 95 ? 0.3763 0.3628 0.3197 0.0199 0.0404 0.0482 95 GLY A C 697 O O . GLY A 95 ? 0.3707 0.3576 0.3050 0.0236 0.0441 0.0473 95 GLY A O 698 N N . ASN A 96 ? 0.3735 0.3517 0.3169 0.0176 0.0372 0.0437 96 ASN A N 699 C CA . ASN A 96 ? 0.3756 0.3448 0.3087 0.0192 0.0381 0.0378 96 ASN A CA 700 C C . ASN A 96 ? 0.3719 0.3389 0.2995 0.0239 0.0421 0.0350 96 ASN A C 701 O O . ASN A 96 ? 0.3991 0.3632 0.3168 0.0271 0.0447 0.0327 96 ASN A O 702 C CB . ASN A 96 ? 0.3870 0.3551 0.3116 0.0188 0.0382 0.0379 96 ASN A CB 703 C CG . ASN A 96 ? 0.4129 0.3813 0.3426 0.0139 0.0338 0.0400 96 ASN A CG 704 O OD1 . ASN A 96 ? 0.4107 0.3779 0.3491 0.0109 0.0303 0.0398 96 ASN A OD1 705 N ND2 . ASN A 96 ? 0.4389 0.4091 0.3632 0.0132 0.0338 0.0419 96 ASN A ND2 706 N N . ASN A 97 ? 0.3582 0.3270 0.2929 0.0244 0.0423 0.0352 97 ASN A N 707 C CA . ASN A 97 ? 0.3583 0.3242 0.2889 0.0284 0.0454 0.0324 97 ASN A CA 708 C C . ASN A 97 ? 0.3566 0.3153 0.2893 0.0267 0.0430 0.0279 97 ASN A C 709 O O . ASN A 97 ? 0.3267 0.2865 0.2679 0.0234 0.0399 0.0285 97 ASN A O 710 C CB . ASN A 97 ? 0.3616 0.3364 0.2984 0.0306 0.0480 0.0369 97 ASN A CB 711 C CG . ASN A 97 ? 0.3770 0.3591 0.3101 0.0332 0.0512 0.0408 97 ASN A CG 712 O OD1 . ASN A 97 ? 0.3926 0.3726 0.3164 0.0373 0.0544 0.0386 97 ASN A OD1 713 N ND2 . ASN A 97 ? 0.3632 0.3534 0.3030 0.0307 0.0500 0.0464 97 ASN A ND2 714 N N . LYS A 98 ? 0.3633 0.3149 0.2883 0.0292 0.0444 0.0236 98 LYS A N 715 C CA . LYS A 98 ? 0.3734 0.3193 0.3001 0.0280 0.0426 0.0200 98 LYS A CA 716 C C . LYS A 98 ? 0.3612 0.3122 0.2972 0.0281 0.0428 0.0218 98 LYS A C 717 O O . LYS A 98 ? 0.3592 0.3163 0.2977 0.0304 0.0454 0.0251 98 LYS A O 718 C CB . LYS A 98 ? 0.3929 0.3309 0.3099 0.0311 0.0442 0.0158 98 LYS A CB 719 C CG . LYS A 98 ? 0.3961 0.3274 0.3032 0.0309 0.0433 0.0133 98 LYS A CG 720 C CD . LYS A 98 ? 0.4447 0.3677 0.3435 0.0339 0.0442 0.0092 98 LYS A CD 721 C CE . LYS A 98 ? 0.4901 0.4051 0.3789 0.0334 0.0427 0.0062 98 LYS A CE 722 N NZ . LYS A 98 ? 0.5136 0.4188 0.3953 0.0351 0.0420 0.0020 98 LYS A NZ 723 N N . LEU A 99 ? 0.3381 0.2870 0.2791 0.0255 0.0401 0.0198 99 LEU A N 724 C CA . LEU A 99 ? 0.3174 0.2707 0.2668 0.0252 0.0398 0.0211 99 LEU A CA 725 C C . LEU A 99 ? 0.3087 0.2572 0.2572 0.0253 0.0393 0.0174 99 LEU A C 726 O O . LEU A 99 ? 0.2855 0.2280 0.2296 0.0240 0.0377 0.0142 99 LEU A O 727 C CB . LEU A 99 ? 0.3037 0.2615 0.2623 0.0216 0.0365 0.0232 99 LEU A CB 728 C CG . LEU A 99 ? 0.2993 0.2534 0.2593 0.0181 0.0327 0.0206 99 LEU A CG 729 C CD1 . LEU A 99 ? 0.2991 0.2563 0.2687 0.0159 0.0297 0.0205 99 LEU A CD1 730 C CD2 . LEU A 99 ? 0.3032 0.2579 0.2618 0.0165 0.0315 0.0225 99 LEU A CD2 731 N N . PRO A 100 ? 0.2936 0.2452 0.2463 0.0267 0.0406 0.0183 100 PRO A N 732 C CA . PRO A 100 ? 0.2885 0.2370 0.2418 0.0262 0.0396 0.0155 100 PRO A CA 733 C C . PRO A 100 ? 0.2770 0.2267 0.2368 0.0224 0.0359 0.0142 100 PRO A C 734 O O . PRO A 100 ? 0.2577 0.2120 0.2240 0.0206 0.0342 0.0161 100 PRO A O 735 C CB . PRO A 100 ? 0.2970 0.2495 0.2534 0.0288 0.0421 0.0176 100 PRO A CB 736 C CG . PRO A 100 ? 0.2924 0.2520 0.2539 0.0291 0.0429 0.0219 100 PRO A CG 737 C CD . PRO A 100 ? 0.2982 0.2571 0.2564 0.0282 0.0424 0.0225 100 PRO A CD 738 N N . VAL A 101 ? 0.2799 0.2258 0.2380 0.0213 0.0345 0.0110 101 VAL A N 739 C CA . VAL A 101 ? 0.2595 0.2075 0.2235 0.0185 0.0315 0.0094 101 VAL A CA 740 C C . VAL A 101 ? 0.2661 0.2152 0.2319 0.0190 0.0320 0.0087 101 VAL A C 741 O O . VAL A 101 ? 0.2635 0.2088 0.2241 0.0205 0.0335 0.0079 101 VAL A O 742 C CB . VAL A 101 ? 0.2567 0.2003 0.2174 0.0163 0.0292 0.0066 101 VAL A CB 743 C CG1 . VAL A 101 ? 0.2474 0.1937 0.2139 0.0138 0.0263 0.0047 101 VAL A CG1 744 C CG2 . VAL A 101 ? 0.2635 0.2058 0.2221 0.0156 0.0287 0.0075 101 VAL A CG2 745 N N . LEU A 102 ? 0.2541 0.2086 0.2275 0.0179 0.0306 0.0091 102 LEU A N 746 C CA . LEU A 102 ? 0.2596 0.2162 0.2352 0.0181 0.0308 0.0086 102 LEU A CA 747 C C . LEU A 102 ? 0.2531 0.2124 0.2333 0.0156 0.0277 0.0061 102 LEU A C 748 O O . LEU A 102 ? 0.2316 0.1932 0.2164 0.0143 0.0256 0.0059 102 LEU A O 749 C CB . LEU A 102 ? 0.2584 0.2196 0.2383 0.0197 0.0325 0.0118 102 LEU A CB 750 C CG . LEU A 102 ? 0.2663 0.2303 0.2487 0.0202 0.0331 0.0122 102 LEU A CG 751 C CD1 . LEU A 102 ? 0.2694 0.2361 0.2531 0.0228 0.0358 0.0159 102 LEU A CD1 752 C CD2 . LEU A 102 ? 0.2605 0.2292 0.2496 0.0180 0.0302 0.0111 102 LEU A CD2 753 N N . THR A 103 ? 0.2484 0.2074 0.2272 0.0150 0.0273 0.0043 103 THR A N 754 C CA . THR A 103 ? 0.2437 0.2051 0.2252 0.0129 0.0246 0.0016 103 THR A CA 755 C C . THR A 103 ? 0.2375 0.2028 0.2211 0.0124 0.0243 0.0009 103 THR A C 756 O O . THR A 103 ? 0.2187 0.1835 0.2005 0.0135 0.0260 0.0023 103 THR A O 757 C CB . THR A 103 ? 0.2462 0.2035 0.2230 0.0116 0.0236 -0.0002 103 THR A CB 758 O OG1 . THR A 103 ? 0.2430 0.1971 0.2147 0.0119 0.0246 -0.0001 103 THR A OG1 759 C CG2 . THR A 103 ? 0.2593 0.2126 0.2333 0.0119 0.0239 0.0005 103 THR A CG2 760 N N . TRP A 104 ? 0.2298 0.1993 0.2174 0.0110 0.0219 -0.0014 104 TRP A N 761 C CA . TRP A 104 ? 0.2261 0.1999 0.2150 0.0104 0.0214 -0.0024 104 TRP A CA 762 C C . TRP A 104 ? 0.2123 0.1877 0.2005 0.0089 0.0195 -0.0052 104 TRP A C 763 O O . TRP A 104 ? 0.2130 0.1892 0.2036 0.0085 0.0177 -0.0072 104 TRP A O 764 C CB . TRP A 104 ? 0.2216 0.2007 0.2165 0.0106 0.0204 -0.0025 104 TRP A CB 765 C CG . TRP A 104 ? 0.2246 0.2092 0.2209 0.0100 0.0199 -0.0035 104 TRP A CG 766 C CD1 . TRP A 104 ? 0.2291 0.2142 0.2227 0.0099 0.0213 -0.0021 104 TRP A CD1 767 C CD2 . TRP A 104 ? 0.2226 0.2131 0.2233 0.0095 0.0177 -0.0059 104 TRP A CD2 768 N NE1 . TRP A 104 ? 0.2209 0.2123 0.2170 0.0091 0.0202 -0.0030 104 TRP A NE1 769 C CE2 . TRP A 104 ? 0.2222 0.2171 0.2223 0.0090 0.0181 -0.0057 104 TRP A CE2 770 C CE3 . TRP A 104 ? 0.2387 0.2310 0.2438 0.0095 0.0152 -0.0083 104 TRP A CE3 771 C CZ2 . TRP A 104 ? 0.2368 0.2383 0.2401 0.0086 0.0164 -0.0079 104 TRP A CZ2 772 C CZ3 . TRP A 104 ? 0.2439 0.2420 0.2521 0.0093 0.0132 -0.0110 104 TRP A CZ3 773 C CH2 . TRP A 104 ? 0.2418 0.2447 0.2488 0.0088 0.0139 -0.0109 104 TRP A CH2 774 N N . SER A 105 ? 0.2144 0.1913 0.2004 0.0082 0.0198 -0.0051 105 SER A N 775 C CA . SER A 105 ? 0.2158 0.1961 0.2015 0.0068 0.0183 -0.0070 105 SER A CA 776 C C . SER A 105 ? 0.2113 0.1877 0.1949 0.0061 0.0174 -0.0080 105 SER A C 777 O O . SER A 105 ? 0.2329 0.2029 0.2120 0.0062 0.0183 -0.0065 105 SER A O 778 C CB . SER A 105 ? 0.2253 0.2133 0.2161 0.0068 0.0169 -0.0093 105 SER A CB 779 O OG . SER A 105 ? 0.2343 0.2276 0.2248 0.0057 0.0159 -0.0107 105 SER A OG 780 N N . GLN A 106 ? 0.2014 0.1815 0.1882 0.0058 0.0155 -0.0106 106 GLN A N 781 C CA . GLN A 106 ? 0.2025 0.1797 0.1884 0.0052 0.0143 -0.0115 106 GLN A CA 782 C C . GLN A 106 ? 0.1995 0.1699 0.1833 0.0056 0.0150 -0.0100 106 GLN A C 783 O O . GLN A 106 ? 0.2033 0.1697 0.1839 0.0048 0.0145 -0.0098 106 GLN A O 784 C CB . GLN A 106 ? 0.2007 0.1828 0.1914 0.0054 0.0122 -0.0146 106 GLN A CB 785 C CG . GLN A 106 ? 0.2040 0.1842 0.1938 0.0045 0.0109 -0.0153 106 GLN A CG 786 C CD . GLN A 106 ? 0.2130 0.1964 0.2081 0.0053 0.0086 -0.0183 106 GLN A CD 787 O OE1 . GLN A 106 ? 0.2100 0.1910 0.2051 0.0048 0.0075 -0.0185 106 GLN A OE1 788 N NE2 . GLN A 106 ? 0.2149 0.2035 0.2142 0.0065 0.0077 -0.0206 106 GLN A NE2 789 N N . GLY A 107 ? 0.2029 0.1726 0.1886 0.0068 0.0159 -0.0089 107 GLY A N 790 C CA . GLY A 107 ? 0.2146 0.1793 0.1989 0.0074 0.0167 -0.0071 107 GLY A CA 791 C C . GLY A 107 ? 0.2152 0.1738 0.1924 0.0074 0.0184 -0.0055 107 GLY A C 792 O O . GLY A 107 ? 0.2272 0.1818 0.2019 0.0074 0.0184 -0.0049 107 GLY A O 793 N N . GLY A 108 ? 0.2134 0.1714 0.1876 0.0075 0.0195 -0.0049 108 GLY A N 794 C CA . GLY A 108 ? 0.2211 0.1725 0.1883 0.0077 0.0206 -0.0037 108 GLY A CA 795 C C . GLY A 108 ? 0.2235 0.1724 0.1875 0.0057 0.0187 -0.0046 108 GLY A C 796 O O . GLY A 108 ? 0.2456 0.1886 0.2047 0.0057 0.0189 -0.0042 108 GLY A O 797 N N . LEU A 109 ? 0.2158 0.1698 0.1828 0.0042 0.0170 -0.0059 109 LEU A N 798 C CA . LEU A 109 ? 0.2117 0.1651 0.1771 0.0022 0.0151 -0.0066 109 LEU A CA 799 C C . LEU A 109 ? 0.2116 0.1630 0.1777 0.0022 0.0143 -0.0072 109 LEU A C 800 O O . LEU A 109 ? 0.2151 0.1618 0.1771 0.0010 0.0135 -0.0068 109 LEU A O 801 C CB . LEU A 109 ? 0.2071 0.1687 0.1772 0.0012 0.0137 -0.0080 109 LEU A CB 802 C CG . LEU A 109 ? 0.2064 0.1697 0.1764 -0.0006 0.0116 -0.0086 109 LEU A CG 803 C CD1 . LEU A 109 ? 0.2164 0.1743 0.1805 -0.0024 0.0110 -0.0066 109 LEU A CD1 804 C CD2 . LEU A 109 ? 0.2061 0.1787 0.1808 -0.0009 0.0108 -0.0100 109 LEU A CD2 805 N N . VAL A 110 ? 0.2149 0.1694 0.1860 0.0033 0.0143 -0.0079 110 VAL A N 806 C CA . VAL A 110 ? 0.2206 0.1730 0.1929 0.0032 0.0135 -0.0079 110 VAL A CA 807 C C . VAL A 110 ? 0.2294 0.1751 0.1959 0.0037 0.0149 -0.0060 110 VAL A C 808 O O . VAL A 110 ? 0.2214 0.1636 0.1851 0.0027 0.0140 -0.0057 110 VAL A O 809 C CB . VAL A 110 ? 0.2120 0.1690 0.1916 0.0042 0.0127 -0.0088 110 VAL A CB 810 C CG1 . VAL A 110 ? 0.2160 0.1705 0.1968 0.0042 0.0120 -0.0077 110 VAL A CG1 811 C CG2 . VAL A 110 ? 0.2076 0.1704 0.1921 0.0037 0.0105 -0.0115 110 VAL A CG2 812 N N . ALA A 111 ? 0.2331 0.1774 0.1979 0.0054 0.0171 -0.0047 111 ALA A N 813 C CA . ALA A 111 ? 0.2503 0.1890 0.2094 0.0064 0.0187 -0.0032 111 ALA A CA 814 C C . ALA A 111 ? 0.2627 0.1952 0.2143 0.0055 0.0182 -0.0035 111 ALA A C 815 O O . ALA A 111 ? 0.2771 0.2053 0.2244 0.0052 0.0179 -0.0031 111 ALA A O 816 C CB . ALA A 111 ? 0.2553 0.1942 0.2139 0.0087 0.0213 -0.0018 111 ALA A CB 817 N N . GLN A 112 ? 0.2683 0.2006 0.2186 0.0048 0.0177 -0.0040 112 GLN A N 818 C CA . GLN A 112 ? 0.2724 0.1987 0.2162 0.0035 0.0167 -0.0040 112 GLN A CA 819 C C . GLN A 112 ? 0.2711 0.1973 0.2149 0.0009 0.0140 -0.0046 112 GLN A C 820 O O . GLN A 112 ? 0.2655 0.1855 0.2032 0.0000 0.0131 -0.0043 112 GLN A O 821 C CB . GLN A 112 ? 0.2779 0.2047 0.2213 0.0033 0.0166 -0.0038 112 GLN A CB 822 C CG . GLN A 112 ? 0.3007 0.2198 0.2368 0.0027 0.0157 -0.0034 112 GLN A CG 823 C CD . GLN A 112 ? 0.3044 0.2155 0.2335 0.0050 0.0171 -0.0034 112 GLN A CD 824 O OE1 . GLN A 112 ? 0.3190 0.2304 0.2481 0.0074 0.0194 -0.0032 112 GLN A OE1 825 N NE2 . GLN A 112 ? 0.3132 0.2170 0.2360 0.0042 0.0155 -0.0034 112 GLN A NE2 826 N N . TRP A 113 ? 0.2559 0.1886 0.2063 0.0000 0.0128 -0.0053 113 TRP A N 827 C CA . TRP A 113 ? 0.2537 0.1871 0.2051 -0.0021 0.0104 -0.0057 113 TRP A CA 828 C C . TRP A 113 ? 0.2550 0.1847 0.2045 -0.0019 0.0104 -0.0051 113 TRP A C 829 O O . TRP A 113 ? 0.2579 0.1836 0.2035 -0.0035 0.0089 -0.0047 113 TRP A O 830 C CB . TRP A 113 ? 0.2492 0.1909 0.2087 -0.0023 0.0093 -0.0070 113 TRP A CB 831 C CG . TRP A 113 ? 0.2372 0.1806 0.1985 -0.0041 0.0069 -0.0074 113 TRP A CG 832 C CD1 . TRP A 113 ? 0.2352 0.1788 0.1994 -0.0043 0.0057 -0.0076 113 TRP A CD1 833 C CD2 . TRP A 113 ? 0.2333 0.1791 0.1944 -0.0061 0.0053 -0.0073 113 TRP A CD2 834 N NE1 . TRP A 113 ? 0.2252 0.1711 0.1909 -0.0061 0.0035 -0.0078 113 TRP A NE1 835 C CE2 . TRP A 113 ? 0.2269 0.1742 0.1905 -0.0072 0.0033 -0.0075 113 TRP A CE2 836 C CE3 . TRP A 113 ? 0.2259 0.1727 0.1847 -0.0071 0.0052 -0.0065 113 TRP A CE3 837 C CZ2 . TRP A 113 ? 0.2171 0.1676 0.1813 -0.0092 0.0014 -0.0070 113 TRP A CZ2 838 C CZ3 . TRP A 113 ? 0.2206 0.1706 0.1801 -0.0094 0.0030 -0.0058 113 TRP A CZ3 839 C CH2 . TRP A 113 ? 0.2198 0.1717 0.1819 -0.0103 0.0013 -0.0061 113 TRP A CH2 840 N N . GLY A 114 ? 0.2491 0.1805 0.2016 0.0000 0.0119 -0.0048 114 GLY A N 841 C CA . GLY A 114 ? 0.2505 0.1793 0.2012 0.0003 0.0122 -0.0036 114 GLY A CA 842 C C . GLY A 114 ? 0.2649 0.1864 0.2065 0.0005 0.0131 -0.0029 114 GLY A C 843 O O . GLY A 114 ? 0.2733 0.1917 0.2116 -0.0007 0.0118 -0.0025 114 GLY A O 844 N N . LEU A 115 ? 0.2660 0.1848 0.2034 0.0023 0.0150 -0.0030 115 LEU A N 845 C CA . LEU A 115 ? 0.2709 0.1823 0.1991 0.0033 0.0160 -0.0029 115 LEU A CA 846 C C . LEU A 115 ? 0.2679 0.1741 0.1910 0.0008 0.0133 -0.0035 115 LEU A C 847 O O . LEU A 115 ? 0.2844 0.1845 0.2003 0.0008 0.0129 -0.0036 115 LEU A O 848 C CB . LEU A 115 ? 0.2668 0.1767 0.1928 0.0059 0.0183 -0.0030 115 LEU A CB 849 C CG . LEU A 115 ? 0.2680 0.1819 0.1972 0.0086 0.0212 -0.0018 115 LEU A CG 850 C CD1 . LEU A 115 ? 0.2688 0.1829 0.1982 0.0109 0.0231 -0.0018 115 LEU A CD1 851 C CD2 . LEU A 115 ? 0.2832 0.1945 0.2074 0.0103 0.0226 -0.0009 115 LEU A CD2 852 N N . THR A 116 ? 0.2618 0.1708 0.1887 -0.0011 0.0115 -0.0039 116 THR A N 853 C CA . THR A 116 ? 0.2647 0.1698 0.1877 -0.0038 0.0087 -0.0039 116 THR A CA 854 C C . THR A 116 ? 0.2666 0.1721 0.1903 -0.0060 0.0066 -0.0035 116 THR A C 855 O O . THR A 116 ? 0.2728 0.1719 0.1897 -0.0075 0.0049 -0.0033 116 THR A O 856 C CB . THR A 116 ? 0.2570 0.1661 0.1840 -0.0051 0.0077 -0.0039 116 THR A CB 857 O OG1 . THR A 116 ? 0.2579 0.1656 0.1834 -0.0033 0.0093 -0.0039 116 THR A OG1 858 C CG2 . THR A 116 ? 0.2565 0.1629 0.1806 -0.0084 0.0044 -0.0033 116 THR A CG2 859 N N . PHE A 117 ? 0.2600 0.1723 0.1913 -0.0063 0.0064 -0.0035 117 PHE A N 860 C CA . PHE A 117 ? 0.2568 0.1701 0.1899 -0.0086 0.0040 -0.0030 117 PHE A CA 861 C C . PHE A 117 ? 0.2668 0.1800 0.2005 -0.0081 0.0043 -0.0022 117 PHE A C 862 O O . PHE A 117 ? 0.2685 0.1815 0.2028 -0.0101 0.0022 -0.0015 117 PHE A O 863 C CB . PHE A 117 ? 0.2593 0.1801 0.2006 -0.0096 0.0026 -0.0035 117 PHE A CB 864 C CG . PHE A 117 ? 0.2616 0.1833 0.2021 -0.0110 0.0015 -0.0035 117 PHE A CG 865 C CD1 . PHE A 117 ? 0.2779 0.1964 0.2145 -0.0138 -0.0009 -0.0024 117 PHE A CD1 866 C CD2 . PHE A 117 ? 0.2630 0.1896 0.2071 -0.0099 0.0027 -0.0041 117 PHE A CD2 867 C CE1 . PHE A 117 ? 0.2697 0.1898 0.2062 -0.0155 -0.0023 -0.0017 117 PHE A CE1 868 C CE2 . PHE A 117 ? 0.2603 0.1883 0.2038 -0.0115 0.0016 -0.0035 117 PHE A CE2 869 C CZ . PHE A 117 ? 0.2625 0.1876 0.2025 -0.0143 -0.0009 -0.0022 117 PHE A CZ 870 N N . PHE A 118 ? 0.2651 0.1784 0.1984 -0.0056 0.0069 -0.0019 118 PHE A N 871 C CA . PHE A 118 ? 0.2722 0.1859 0.2059 -0.0051 0.0074 -0.0005 118 PHE A CA 872 C C . PHE A 118 ? 0.2759 0.1846 0.2012 -0.0031 0.0097 -0.0001 118 PHE A C 873 O O . PHE A 118 ? 0.2975 0.2081 0.2237 -0.0005 0.0124 0.0003 118 PHE A O 874 C CB . PHE A 118 ? 0.2675 0.1878 0.2104 -0.0039 0.0080 0.0000 118 PHE A CB 875 C CG . PHE A 118 ? 0.2619 0.1870 0.2128 -0.0052 0.0057 -0.0010 118 PHE A CG 876 C CD1 . PHE A 118 ? 0.2570 0.1847 0.2103 -0.0051 0.0056 -0.0027 118 PHE A CD1 877 C CD2 . PHE A 118 ? 0.2577 0.1851 0.2138 -0.0064 0.0035 -0.0002 118 PHE A CD2 878 C CE1 . PHE A 118 ? 0.2472 0.1799 0.2075 -0.0058 0.0036 -0.0039 118 PHE A CE1 879 C CE2 . PHE A 118 ? 0.2498 0.1817 0.2134 -0.0071 0.0014 -0.0015 118 PHE A CE2 880 C CZ . PHE A 118 ? 0.2484 0.1830 0.2137 -0.0066 0.0015 -0.0034 118 PHE A CZ 881 N N . PRO A 119 ? 0.2789 0.1812 0.1957 -0.0042 0.0087 -0.0003 119 PRO A N 882 C CA . PRO A 119 ? 0.2834 0.1805 0.1914 -0.0018 0.0108 -0.0006 119 PRO A CA 883 C C . PRO A 119 ? 0.2960 0.1960 0.2038 0.0004 0.0134 0.0008 119 PRO A C 884 O O . PRO A 119 ? 0.2930 0.1907 0.1954 0.0034 0.0160 0.0003 119 PRO A O 885 C CB . PRO A 119 ? 0.2971 0.1874 0.1967 -0.0039 0.0084 -0.0011 119 PRO A CB 886 C CG . PRO A 119 ? 0.2948 0.1859 0.1985 -0.0071 0.0053 -0.0012 119 PRO A CG 887 C CD . PRO A 119 ? 0.2866 0.1860 0.2012 -0.0074 0.0054 -0.0004 119 PRO A CD 888 N N . SER A 120 ? 0.2939 0.1989 0.2076 -0.0009 0.0125 0.0028 120 SER A N 889 C CA . SER A 120 ? 0.3033 0.2118 0.2172 0.0006 0.0145 0.0051 120 SER A CA 890 C C . SER A 120 ? 0.2998 0.2117 0.2165 0.0037 0.0176 0.0054 120 SER A C 891 O O . SER A 120 ? 0.3173 0.2312 0.2315 0.0060 0.0202 0.0071 120 SER A O 892 C CB . SER A 120 ? 0.3111 0.2248 0.2329 -0.0016 0.0124 0.0074 120 SER A CB 893 O OG . SER A 120 ? 0.2933 0.2119 0.2249 -0.0016 0.0120 0.0075 120 SER A OG 894 N N . ILE A 121 ? 0.2928 0.2061 0.2147 0.0039 0.0176 0.0041 121 ILE A N 895 C CA . ILE A 121 ? 0.2995 0.2164 0.2248 0.0067 0.0203 0.0047 121 ILE A CA 896 C C . ILE A 121 ? 0.3035 0.2164 0.2220 0.0097 0.0229 0.0032 121 ILE A C 897 O O . ILE A 121 ? 0.3064 0.2224 0.2268 0.0123 0.0255 0.0043 121 ILE A O 898 C CB . ILE A 121 ? 0.2877 0.2099 0.2232 0.0059 0.0193 0.0045 121 ILE A CB 899 C CG1 . ILE A 121 ? 0.2882 0.2080 0.2237 0.0046 0.0177 0.0018 121 ILE A CG1 900 C CG2 . ILE A 121 ? 0.2895 0.2165 0.2326 0.0041 0.0173 0.0065 121 ILE A CG2 901 C CD1 . ILE A 121 ? 0.2847 0.2095 0.2279 0.0050 0.0178 0.0012 121 ILE A CD1 902 N N . ARG A 122 ? 0.3252 0.2310 0.2357 0.0095 0.0221 0.0012 122 ARG A N 903 C CA . ARG A 122 ? 0.3354 0.2363 0.2396 0.0123 0.0239 -0.0003 122 ARG A CA 904 C C . ARG A 122 ? 0.3736 0.2749 0.2730 0.0161 0.0273 0.0005 122 ARG A C 905 O O . ARG A 122 ? 0.3773 0.2772 0.2745 0.0194 0.0296 -0.0001 122 ARG A O 906 C CB . ARG A 122 ? 0.3521 0.2443 0.2480 0.0110 0.0216 -0.0025 122 ARG A CB 907 C CG . ARG A 122 ? 0.3429 0.2351 0.2432 0.0074 0.0184 -0.0031 122 ARG A CG 908 C CD . ARG A 122 ? 0.3511 0.2355 0.2440 0.0055 0.0156 -0.0045 122 ARG A CD 909 N NE . ARG A 122 ? 0.3404 0.2265 0.2384 0.0019 0.0127 -0.0044 122 ARG A NE 910 C CZ . ARG A 122 ? 0.3515 0.2332 0.2460 -0.0009 0.0095 -0.0047 122 ARG A CZ 911 N NH1 . ARG A 122 ? 0.3757 0.2501 0.2610 -0.0010 0.0084 -0.0054 122 ARG A NH1 912 N NH2 . ARG A 122 ? 0.3486 0.2335 0.2485 -0.0039 0.0071 -0.0042 122 ARG A NH2 913 N N . SER A 123 ? 0.3807 0.2841 0.2782 0.0158 0.0275 0.0021 123 SER A N 914 C CA . SER A 123 ? 0.3901 0.2957 0.2834 0.0192 0.0307 0.0034 123 SER A CA 915 C C . SER A 123 ? 0.3915 0.3066 0.2935 0.0200 0.0326 0.0070 123 SER A C 916 O O . SER A 123 ? 0.3992 0.3179 0.2988 0.0226 0.0353 0.0089 123 SER A O 917 C CB . SER A 123 ? 0.4264 0.3298 0.3127 0.0182 0.0297 0.0036 123 SER A CB 918 O OG . SER A 123 ? 0.4260 0.3339 0.3191 0.0144 0.0273 0.0059 123 SER A OG 919 N N . LYS A 124 ? 0.3452 0.2644 0.2569 0.0178 0.0311 0.0079 124 LYS A N 920 C CA . LYS A 124 ? 0.3330 0.2607 0.2537 0.0179 0.0320 0.0114 124 LYS A CA 921 C C . LYS A 124 ? 0.3309 0.2610 0.2571 0.0193 0.0332 0.0113 124 LYS A C 922 O O . LYS A 124 ? 0.3111 0.2479 0.2436 0.0201 0.0345 0.0142 124 LYS A O 923 C CB . LYS A 124 ? 0.3282 0.2589 0.2564 0.0138 0.0285 0.0127 124 LYS A CB 924 C CG . LYS A 124 ? 0.3211 0.2491 0.2441 0.0120 0.0269 0.0129 124 LYS A CG 925 C CD . LYS A 124 ? 0.3187 0.2510 0.2491 0.0089 0.0242 0.0155 124 LYS A CD 926 C CE . LYS A 124 ? 0.3181 0.2480 0.2424 0.0073 0.0230 0.0161 124 LYS A CE 927 N NZ . LYS A 124 ? 0.3137 0.2469 0.2462 0.0039 0.0196 0.0182 124 LYS A NZ 928 N N . VAL A 125 ? 0.3353 0.2603 0.2591 0.0195 0.0327 0.0082 125 VAL A N 929 C CA . VAL A 125 ? 0.3300 0.2566 0.2578 0.0208 0.0338 0.0078 125 VAL A CA 930 C C . VAL A 125 ? 0.3509 0.2737 0.2715 0.0248 0.0368 0.0069 125 VAL A C 931 O O . VAL A 125 ? 0.3505 0.2659 0.2632 0.0254 0.0363 0.0043 125 VAL A O 932 C CB . VAL A 125 ? 0.3303 0.2543 0.2606 0.0183 0.0312 0.0053 125 VAL A CB 933 C CG1 . VAL A 125 ? 0.3244 0.2505 0.2584 0.0198 0.0324 0.0052 125 VAL A CG1 934 C CG2 . VAL A 125 ? 0.3176 0.2450 0.2548 0.0149 0.0282 0.0056 125 VAL A CG2 935 N N . ASP A 126 ? 0.3573 0.2853 0.2813 0.0275 0.0395 0.0091 126 ASP A N 936 C CA . ASP A 126 ? 0.3834 0.3099 0.3028 0.0320 0.0427 0.0089 126 ASP A CA 937 C C . ASP A 126 ? 0.3721 0.2934 0.2903 0.0324 0.0421 0.0064 126 ASP A C 938 O O . ASP A 126 ? 0.3708 0.2858 0.2818 0.0352 0.0431 0.0044 126 ASP A O 939 C CB . ASP A 126 ? 0.4055 0.3409 0.3322 0.0336 0.0451 0.0127 126 ASP A CB 940 C CG . ASP A 126 ? 0.4488 0.3854 0.3710 0.0384 0.0488 0.0137 126 ASP A CG 941 O OD1 . ASP A 126 ? 0.4937 0.4255 0.4071 0.0403 0.0496 0.0119 126 ASP A OD1 942 O OD2 . ASP A 126 ? 0.4853 0.4277 0.4124 0.0404 0.0510 0.0163 126 ASP A OD2 943 N N . ARG A 127 ? 0.3391 0.2635 0.2649 0.0298 0.0404 0.0067 127 ARG A N 944 C CA . ARG A 127 ? 0.3311 0.2532 0.2579 0.0300 0.0399 0.0054 127 ARG A CA 945 C C . ARG A 127 ? 0.3043 0.2309 0.2393 0.0264 0.0376 0.0057 127 ARG A C 946 O O . ARG A 127 ? 0.2819 0.2138 0.2225 0.0247 0.0368 0.0071 127 ARG A O 947 C CB . ARG A 127 ? 0.3491 0.2740 0.2773 0.0340 0.0432 0.0071 127 ARG A CB 948 C CG . ARG A 127 ? 0.3461 0.2802 0.2830 0.0338 0.0442 0.0105 127 ARG A CG 949 C CD . ARG A 127 ? 0.3503 0.2877 0.2878 0.0379 0.0477 0.0127 127 ARG A CD 950 N NE . ARG A 127 ? 0.3739 0.3111 0.3057 0.0411 0.0502 0.0134 127 ARG A NE 951 C CZ . ARG A 127 ? 0.3835 0.3204 0.3113 0.0459 0.0534 0.0138 127 ARG A CZ 952 N NH1 . ARG A 127 ? 0.3847 0.3205 0.3132 0.0485 0.0547 0.0137 127 ARG A NH1 953 N NH2 . ARG A 127 ? 0.3873 0.3250 0.3099 0.0483 0.0554 0.0143 127 ARG A NH2 954 N N . LEU A 128 ? 0.2937 0.2183 0.2293 0.0253 0.0362 0.0043 128 LEU A N 955 C CA . LEU A 128 ? 0.2818 0.2109 0.2245 0.0222 0.0340 0.0040 128 LEU A CA 956 C C . LEU A 128 ? 0.2745 0.2057 0.2200 0.0234 0.0350 0.0048 128 LEU A C 957 O O . LEU A 128 ? 0.2875 0.2137 0.2283 0.0253 0.0358 0.0043 128 LEU A O 958 C CB . LEU A 128 ? 0.2757 0.2007 0.2156 0.0191 0.0310 0.0018 128 LEU A CB 959 C CG . LEU A 128 ? 0.2780 0.2078 0.2242 0.0162 0.0288 0.0011 128 LEU A CG 960 C CD1 . LEU A 128 ? 0.2601 0.1965 0.2136 0.0153 0.0282 0.0017 128 LEU A CD1 961 C CD2 . LEU A 128 ? 0.2869 0.2132 0.2301 0.0135 0.0261 -0.0005 128 LEU A CD2 962 N N . MET A 129 ? 0.2658 0.2041 0.2190 0.0228 0.0350 0.0062 129 MET A N 963 C CA . MET A 129 ? 0.2699 0.2115 0.2269 0.0234 0.0357 0.0072 129 MET A CA 964 C C . MET A 129 ? 0.2712 0.2170 0.2334 0.0202 0.0330 0.0060 129 MET A C 965 O O . MET A 129 ? 0.2447 0.1957 0.2127 0.0190 0.0321 0.0064 129 MET A O 966 C CB . MET A 129 ? 0.2829 0.2296 0.2441 0.0257 0.0380 0.0101 129 MET A CB 967 C CG . MET A 129 ? 0.2771 0.2278 0.2427 0.0263 0.0387 0.0116 129 MET A CG 968 S SD . MET A 129 ? 0.2887 0.2338 0.2494 0.0280 0.0394 0.0110 129 MET A SD 969 C CE . MET A 129 ? 0.2755 0.2221 0.2387 0.0240 0.0361 0.0092 129 MET A CE 970 N N . ALA A 130 ? 0.2562 0.1998 0.2163 0.0187 0.0316 0.0046 130 ALA A N 971 C CA . ALA A 130 ? 0.2643 0.2120 0.2282 0.0158 0.0292 0.0032 130 ALA A CA 972 C C . ALA A 130 ? 0.2581 0.2100 0.2253 0.0157 0.0292 0.0041 130 ALA A C 973 O O . ALA A 130 ? 0.2481 0.1971 0.2125 0.0164 0.0298 0.0049 130 ALA A O 974 C CB . ALA A 130 ? 0.2680 0.2116 0.2276 0.0138 0.0272 0.0015 130 ALA A CB 975 N N . PHE A 131 ? 0.2418 0.2005 0.2149 0.0145 0.0282 0.0037 131 PHE A N 976 C CA . PHE A 131 ? 0.2384 0.2024 0.2152 0.0139 0.0279 0.0043 131 PHE A CA 977 C C . PHE A 131 ? 0.2328 0.2004 0.2106 0.0114 0.0255 0.0023 131 PHE A C 978 O O . PHE A 131 ? 0.2330 0.2032 0.2131 0.0104 0.0241 0.0003 131 PHE A O 979 C CB . PHE A 131 ? 0.2367 0.2059 0.2192 0.0147 0.0283 0.0055 131 PHE A CB 980 C CG . PHE A 131 ? 0.2421 0.2092 0.2241 0.0173 0.0309 0.0082 131 PHE A CG 981 C CD1 . PHE A 131 ? 0.2437 0.2106 0.2253 0.0189 0.0326 0.0103 131 PHE A CD1 982 C CD2 . PHE A 131 ? 0.2450 0.2113 0.2276 0.0182 0.0315 0.0088 131 PHE A CD2 983 C CE1 . PHE A 131 ? 0.2525 0.2182 0.2337 0.0217 0.0351 0.0129 131 PHE A CE1 984 C CE2 . PHE A 131 ? 0.2387 0.2045 0.2211 0.0207 0.0339 0.0116 131 PHE A CE2 985 C CZ . PHE A 131 ? 0.2316 0.1973 0.2132 0.0226 0.0359 0.0135 131 PHE A CZ 986 N N . ALA A 132 ? 0.2309 0.1990 0.2071 0.0104 0.0251 0.0030 132 ALA A N 987 C CA . ALA A 132 ? 0.2209 0.1934 0.1978 0.0080 0.0231 0.0017 132 ALA A CA 988 C C . ALA A 132 ? 0.2233 0.1941 0.1985 0.0068 0.0217 -0.0003 132 ALA A C 989 O O . ALA A 132 ? 0.2175 0.1940 0.1955 0.0056 0.0202 -0.0022 132 ALA A O 990 C CB . ALA A 132 ? 0.2160 0.1975 0.1983 0.0073 0.0224 0.0009 132 ALA A CB 991 N N . PRO A 133 ? 0.2262 0.1893 0.1967 0.0073 0.0221 0.0000 133 PRO A N 992 C CA . PRO A 133 ? 0.2214 0.1826 0.1901 0.0060 0.0207 -0.0015 133 PRO A CA 993 C C . PRO A 133 ? 0.2216 0.1853 0.1895 0.0036 0.0188 -0.0016 133 PRO A C 994 O O . PRO A 133 ? 0.2331 0.1959 0.1991 0.0028 0.0185 0.0001 133 PRO A O 995 C CB . PRO A 133 ? 0.2266 0.1788 0.1898 0.0072 0.0216 -0.0008 133 PRO A CB 996 C CG . PRO A 133 ? 0.2319 0.1808 0.1925 0.0083 0.0227 0.0010 133 PRO A CG 997 C CD . PRO A 133 ? 0.2310 0.1868 0.1971 0.0091 0.0237 0.0017 133 PRO A CD 998 N N . ASP A 134 ? 0.2161 0.1833 0.1857 0.0024 0.0173 -0.0033 134 ASP A N 999 C CA . ASP A 134 ? 0.2152 0.1867 0.1847 0.0001 0.0155 -0.0031 134 ASP A CA 1000 C C . ASP A 134 ? 0.2202 0.1865 0.1861 -0.0013 0.0141 -0.0032 134 ASP A C 1001 O O . ASP A 134 ? 0.2105 0.1811 0.1785 -0.0022 0.0128 -0.0045 134 ASP A O 1002 C CB . ASP A 134 ? 0.2072 0.1890 0.1821 -0.0001 0.0149 -0.0050 134 ASP A CB 1003 C CG . ASP A 134 ? 0.2099 0.1931 0.1879 0.0009 0.0144 -0.0079 134 ASP A CG 1004 O OD1 . ASP A 134 ? 0.2147 0.1924 0.1923 0.0022 0.0151 -0.0082 134 ASP A OD1 1005 O OD2 . ASP A 134 ? 0.2112 0.2021 0.1926 0.0007 0.0133 -0.0098 134 ASP A OD2 1006 N N . TYR A 135 ? 0.2205 0.1780 0.1811 -0.0013 0.0142 -0.0017 135 TYR A N 1007 C CA . TYR A 135 ? 0.2282 0.1798 0.1846 -0.0026 0.0127 -0.0016 135 TYR A CA 1008 C C . TYR A 135 ? 0.2300 0.1853 0.1866 -0.0057 0.0103 -0.0005 135 TYR A C 1009 O O . TYR A 135 ? 0.2336 0.1884 0.1896 -0.0070 0.0088 -0.0010 135 TYR A O 1010 C CB . TYR A 135 ? 0.2328 0.1739 0.1829 -0.0018 0.0132 -0.0007 135 TYR A CB 1011 C CG . TYR A 135 ? 0.2299 0.1678 0.1793 0.0012 0.0157 -0.0012 135 TYR A CG 1012 C CD1 . TYR A 135 ? 0.2265 0.1643 0.1769 0.0023 0.0166 -0.0024 135 TYR A CD1 1013 C CD2 . TYR A 135 ? 0.2316 0.1668 0.1796 0.0029 0.0171 0.0000 135 TYR A CD2 1014 C CE1 . TYR A 135 ? 0.2388 0.1740 0.1884 0.0050 0.0189 -0.0023 135 TYR A CE1 1015 C CE2 . TYR A 135 ? 0.2385 0.1712 0.1859 0.0059 0.0195 -0.0001 135 TYR A CE2 1016 C CZ . TYR A 135 ? 0.2396 0.1726 0.1878 0.0069 0.0205 -0.0011 135 TYR A CZ 1017 O OH . TYR A 135 ? 0.2389 0.1706 0.1868 0.0097 0.0229 -0.0007 135 TYR A OH 1018 N N . LYS A 136 ? 0.2310 0.1911 0.1891 -0.0068 0.0098 0.0011 136 LYS A N 1019 C CA . LYS A 136 ? 0.2500 0.2162 0.2094 -0.0098 0.0076 0.0028 136 LYS A CA 1020 C C . LYS A 136 ? 0.2436 0.2223 0.2090 -0.0096 0.0080 0.0013 136 LYS A C 1021 O O . LYS A 136 ? 0.2528 0.2390 0.2200 -0.0115 0.0067 0.0027 136 LYS A O 1022 C CB . LYS A 136 ? 0.2536 0.2186 0.2114 -0.0114 0.0066 0.0059 136 LYS A CB 1023 C CG . LYS A 136 ? 0.2592 0.2115 0.2109 -0.0115 0.0056 0.0070 136 LYS A CG 1024 C CD . LYS A 136 ? 0.2601 0.2111 0.2108 -0.0135 0.0036 0.0105 136 LYS A CD 1025 C CE . LYS A 136 ? 0.2677 0.2052 0.2120 -0.0136 0.0019 0.0113 136 LYS A CE 1026 N NZ . LYS A 136 ? 0.2734 0.2051 0.2159 -0.0096 0.0048 0.0093 136 LYS A NZ 1027 N N . GLY A 137 ? 0.2335 0.2144 0.2017 -0.0071 0.0096 -0.0014 137 GLY A N 1028 C CA . GLY A 137 ? 0.2316 0.2237 0.2051 -0.0064 0.0099 -0.0033 137 GLY A CA 1029 C C . GLY A 137 ? 0.2306 0.2289 0.2058 -0.0065 0.0105 -0.0020 137 GLY A C 1030 O O . GLY A 137 ? 0.2159 0.2092 0.1889 -0.0065 0.0111 0.0000 137 GLY A O 1031 N N . THR A 138 ? 0.2252 0.2346 0.2042 -0.0064 0.0103 -0.0034 138 THR A N 1032 C CA . THR A 138 ? 0.2388 0.2556 0.2193 -0.0068 0.0107 -0.0021 138 THR A CA 1033 C C . THR A 138 ? 0.2417 0.2702 0.2241 -0.0085 0.0096 -0.0012 138 THR A C 1034 O O . THR A 138 ? 0.2239 0.2574 0.2082 -0.0078 0.0092 -0.0035 138 THR A O 1035 C CB . THR A 138 ? 0.2326 0.2523 0.2161 -0.0043 0.0120 -0.0047 138 THR A CB 1036 O OG1 . THR A 138 ? 0.2366 0.2636 0.2212 -0.0051 0.0122 -0.0031 138 THR A OG1 1037 C CG2 . THR A 138 ? 0.2411 0.2660 0.2279 -0.0024 0.0117 -0.0091 138 THR A CG2 1038 N N . VAL A 139 ? 0.2442 0.2772 0.2263 -0.0105 0.0091 0.0022 139 VAL A N 1039 C CA . VAL A 139 ? 0.2578 0.3040 0.2421 -0.0121 0.0083 0.0036 139 VAL A CA 1040 C C . VAL A 139 ? 0.2756 0.3330 0.2633 -0.0098 0.0093 0.0001 139 VAL A C 1041 O O . VAL A 139 ? 0.2650 0.3337 0.2544 -0.0100 0.0090 -0.0002 139 VAL A O 1042 C CB . VAL A 139 ? 0.2739 0.3227 0.2575 -0.0151 0.0073 0.0088 139 VAL A CB 1043 C CG1 . VAL A 139 ? 0.2752 0.3132 0.2553 -0.0176 0.0055 0.0125 139 VAL A CG1 1044 C CG2 . VAL A 139 ? 0.2715 0.3206 0.2556 -0.0143 0.0084 0.0092 139 VAL A CG2 1045 N N . LEU A 140 ? 0.2827 0.3369 0.2711 -0.0074 0.0105 -0.0027 140 LEU A N 1046 C CA . LEU A 140 ? 0.2876 0.3515 0.2787 -0.0053 0.0111 -0.0062 140 LEU A CA 1047 C C . LEU A 140 ? 0.2762 0.3438 0.2693 -0.0030 0.0107 -0.0109 140 LEU A C 1048 O O . LEU A 140 ? 0.2683 0.3459 0.2634 -0.0014 0.0108 -0.0139 140 LEU A O 1049 C CB . LEU A 140 ? 0.3033 0.3621 0.2948 -0.0038 0.0120 -0.0073 140 LEU A CB 1050 C CG . LEU A 140 ? 0.3237 0.3776 0.3133 -0.0058 0.0123 -0.0025 140 LEU A CG 1051 C CD1 . LEU A 140 ? 0.3493 0.4008 0.3398 -0.0047 0.0132 -0.0027 140 LEU A CD1 1052 C CD2 . LEU A 140 ? 0.3568 0.4190 0.3462 -0.0086 0.0115 0.0015 140 LEU A CD2 1053 N N . ALA A 141 ? 0.2594 0.3192 0.2519 -0.0028 0.0103 -0.0116 141 ALA A N 1054 C CA . ALA A 141 ? 0.2411 0.3039 0.2359 -0.0006 0.0098 -0.0158 141 ALA A CA 1055 C C . ALA A 141 ? 0.2393 0.3128 0.2353 -0.0011 0.0092 -0.0153 141 ALA A C 1056 O O . ALA A 141 ? 0.2426 0.3215 0.2411 0.0013 0.0088 -0.0194 141 ALA A O 1057 C CB . ALA A 141 ? 0.2574 0.3081 0.2514 -0.0002 0.0094 -0.0164 141 ALA A CB 1058 N N . GLY A 142 ? 0.2283 0.3045 0.2226 -0.0043 0.0088 -0.0104 142 GLY A N 1059 C CA . GLY A 142 ? 0.2425 0.3288 0.2379 -0.0055 0.0081 -0.0087 142 GLY A CA 1060 C C . GLY A 142 ? 0.2402 0.3413 0.2385 -0.0029 0.0087 -0.0120 142 GLY A C 1061 O O . GLY A 142 ? 0.2435 0.3497 0.2438 -0.0013 0.0083 -0.0142 142 GLY A O 1062 N N . PRO A 143 ? 0.2445 0.3527 0.2429 -0.0023 0.0094 -0.0126 143 PRO A N 1063 C CA . PRO A 143 ? 0.2491 0.3723 0.2496 0.0003 0.0099 -0.0161 143 PRO A CA 1064 C C . PRO A 143 ? 0.2551 0.3770 0.2576 0.0048 0.0098 -0.0231 143 PRO A C 1065 O O . PRO A 143 ? 0.2738 0.4061 0.2783 0.0073 0.0098 -0.0261 143 PRO A O 1066 C CB . PRO A 143 ? 0.2537 0.3813 0.2532 -0.0003 0.0105 -0.0151 143 PRO A CB 1067 C CG . PRO A 143 ? 0.2526 0.3713 0.2500 -0.0044 0.0102 -0.0088 143 PRO A CG 1068 C CD . PRO A 143 ? 0.2403 0.3442 0.2369 -0.0043 0.0097 -0.0095 143 PRO A CD 1069 N N . LEU A 144 ? 0.2479 0.3570 0.2502 0.0057 0.0095 -0.0254 144 LEU A N 1070 C CA . LEU A 144 ? 0.2654 0.3715 0.2700 0.0096 0.0088 -0.0316 144 LEU A CA 1071 C C . LEU A 144 ? 0.2544 0.3596 0.2606 0.0103 0.0081 -0.0322 144 LEU A C 1072 O O . LEU A 144 ? 0.2509 0.3619 0.2597 0.0138 0.0076 -0.0369 144 LEU A O 1073 C CB . LEU A 144 ? 0.2909 0.3835 0.2952 0.0099 0.0084 -0.0328 144 LEU A CB 1074 C CG . LEU A 144 ? 0.3068 0.3984 0.3102 0.0097 0.0088 -0.0327 144 LEU A CG 1075 C CD1 . LEU A 144 ? 0.3232 0.4011 0.3266 0.0096 0.0084 -0.0328 144 LEU A CD1 1076 C CD2 . LEU A 144 ? 0.3202 0.4214 0.3251 0.0129 0.0083 -0.0381 144 LEU A CD2 1077 N N . ASP A 145 ? 0.2346 0.3328 0.2393 0.0071 0.0080 -0.0276 145 ASP A N 1078 C CA . ASP A 145 ? 0.2329 0.3300 0.2389 0.0071 0.0072 -0.0272 145 ASP A CA 1079 C C . ASP A 145 ? 0.2355 0.3477 0.2436 0.0082 0.0074 -0.0274 145 ASP A C 1080 O O . ASP A 145 ? 0.2338 0.3486 0.2447 0.0108 0.0067 -0.0306 145 ASP A O 1081 C CB . ASP A 145 ? 0.2187 0.3076 0.2220 0.0029 0.0068 -0.0214 145 ASP A CB 1082 C CG . ASP A 145 ? 0.2173 0.2910 0.2183 0.0019 0.0068 -0.0208 145 ASP A CG 1083 O OD1 . ASP A 145 ? 0.2199 0.2886 0.2220 0.0043 0.0068 -0.0245 145 ASP A OD1 1084 O OD2 . ASP A 145 ? 0.2036 0.2705 0.2015 -0.0012 0.0066 -0.0163 145 ASP A OD2 1085 N N . ALA A 146 ? 0.2475 0.3694 0.2543 0.0060 0.0081 -0.0235 146 ALA A N 1086 C CA . ALA A 146 ? 0.2433 0.3817 0.2518 0.0065 0.0085 -0.0226 146 ALA A CA 1087 C C . ALA A 146 ? 0.2530 0.4012 0.2640 0.0118 0.0090 -0.0293 146 ALA A C 1088 O O . ALA A 146 ? 0.2572 0.4159 0.2705 0.0139 0.0091 -0.0305 146 ALA A O 1089 C CB . ALA A 146 ? 0.2423 0.3887 0.2489 0.0030 0.0090 -0.0170 146 ALA A CB 1090 N N . LEU A 147 ? 0.2515 0.3951 0.2620 0.0143 0.0090 -0.0341 147 LEU A N 1091 C CA . LEU A 147 ? 0.2596 0.4096 0.2722 0.0197 0.0088 -0.0415 147 LEU A CA 1092 C C . LEU A 147 ? 0.2575 0.3983 0.2728 0.0229 0.0073 -0.0466 147 LEU A C 1093 O O . LEU A 147 ? 0.2465 0.3913 0.2635 0.0275 0.0067 -0.0530 147 LEU A O 1094 C CB . LEU A 147 ? 0.2589 0.4094 0.2698 0.0207 0.0090 -0.0443 147 LEU A CB 1095 C CG . LEU A 147 ? 0.2850 0.4495 0.2940 0.0189 0.0104 -0.0408 147 LEU A CG 1096 C CD1 . LEU A 147 ? 0.2849 0.4475 0.2919 0.0185 0.0105 -0.0418 147 LEU A CD1 1097 C CD2 . LEU A 147 ? 0.2827 0.4649 0.2932 0.0225 0.0111 -0.0437 147 LEU A CD2 1098 N N . ALA A 148 ? 0.2818 0.4104 0.2972 0.0206 0.0065 -0.0438 148 ALA A N 1099 C CA . ALA A 148 ? 0.2907 0.4095 0.3089 0.0227 0.0049 -0.0474 148 ALA A CA 1100 C C . ALA A 148 ? 0.3385 0.4497 0.3573 0.0251 0.0037 -0.0523 148 ALA A C 1101 O O . ALA A 148 ? 0.3617 0.4699 0.3837 0.0287 0.0020 -0.0574 148 ALA A O 1102 C CB . ALA A 148 ? 0.3062 0.4336 0.3279 0.0263 0.0044 -0.0504 148 ALA A CB 1103 N N . VAL A 149 ? 0.3111 0.4193 0.3273 0.0233 0.0044 -0.0509 149 VAL A N 1104 C CA . VAL A 149 ? 0.3259 0.4264 0.3427 0.0249 0.0031 -0.0547 149 VAL A CA 1105 C C . VAL A 149 ? 0.2975 0.3837 0.3131 0.0217 0.0030 -0.0509 149 VAL A C 1106 O O . VAL A 149 ? 0.2955 0.3756 0.3112 0.0220 0.0022 -0.0522 149 VAL A O 1107 C CB . VAL A 149 ? 0.3431 0.4511 0.3582 0.0258 0.0037 -0.0566 149 VAL A CB 1108 C CG1 . VAL A 149 ? 0.3603 0.4828 0.3763 0.0297 0.0038 -0.0612 149 VAL A CG1 1109 C CG2 . VAL A 149 ? 0.3437 0.4532 0.3554 0.0217 0.0055 -0.0506 149 VAL A CG2 1110 N N . SER A 150 ? 0.2695 0.3510 0.2837 0.0186 0.0037 -0.0459 150 SER A N 1111 C CA . SER A 150 ? 0.2385 0.3073 0.2509 0.0159 0.0038 -0.0424 150 SER A CA 1112 C C . SER A 150 ? 0.2297 0.2891 0.2446 0.0169 0.0020 -0.0441 150 SER A C 1113 O O . SER A 150 ? 0.2172 0.2779 0.2343 0.0180 0.0011 -0.0452 150 SER A O 1114 C CB . SER A 150 ? 0.2355 0.3028 0.2445 0.0121 0.0051 -0.0364 150 SER A CB 1115 O OG . SER A 150 ? 0.2262 0.3012 0.2331 0.0107 0.0064 -0.0342 150 SER A OG 1116 N N . ALA A 151 ? 0.2302 0.2803 0.2451 0.0165 0.0016 -0.0438 151 ALA A N 1117 C CA . ALA A 151 ? 0.2223 0.2627 0.2391 0.0165 0.0001 -0.0438 151 ALA A CA 1118 C C . ALA A 151 ? 0.2213 0.2573 0.2357 0.0138 0.0008 -0.0395 151 ALA A C 1119 O O . ALA A 151 ? 0.2160 0.2531 0.2266 0.0114 0.0025 -0.0358 151 ALA A O 1120 C CB . ALA A 151 ? 0.2268 0.2593 0.2434 0.0158 0.0000 -0.0428 151 ALA A CB 1121 N N . PRO A 152 ? 0.2186 0.2488 0.2351 0.0140 -0.0007 -0.0398 152 PRO A N 1122 C CA . PRO A 152 ? 0.2271 0.2516 0.2407 0.0112 -0.0001 -0.0355 152 PRO A CA 1123 C C . PRO A 152 ? 0.2260 0.2446 0.2342 0.0083 0.0017 -0.0311 152 PRO A C 1124 O O . PRO A 152 ? 0.2190 0.2383 0.2237 0.0061 0.0025 -0.0279 152 PRO A O 1125 C CB . PRO A 152 ? 0.2329 0.2502 0.2497 0.0118 -0.0022 -0.0364 152 PRO A CB 1126 C CG . PRO A 152 ? 0.2456 0.2674 0.2678 0.0153 -0.0042 -0.0415 152 PRO A CG 1127 C CD . PRO A 152 ? 0.2335 0.2608 0.2550 0.0165 -0.0032 -0.0435 152 PRO A CD 1128 N N . SER A 153 ? 0.2242 0.2372 0.2319 0.0084 0.0021 -0.0307 153 SER A N 1129 C CA . SER A 153 ? 0.2152 0.2226 0.2179 0.0063 0.0040 -0.0268 153 SER A CA 1130 C C . SER A 153 ? 0.2071 0.2202 0.2074 0.0055 0.0055 -0.0255 153 SER A C 1131 O O . SER A 153 ? 0.2081 0.2173 0.2041 0.0036 0.0067 -0.0221 153 SER A O 1132 C CB . SER A 153 ? 0.2117 0.2125 0.2148 0.0067 0.0042 -0.0262 153 SER A CB 1133 O OG . SER A 153 ? 0.1973 0.2021 0.2027 0.0081 0.0043 -0.0281 153 SER A OG 1134 N N . VAL A 154 ? 0.2090 0.2311 0.2118 0.0070 0.0053 -0.0282 154 VAL A N 1135 C CA . VAL A 154 ? 0.2200 0.2486 0.2209 0.0060 0.0066 -0.0267 154 VAL A CA 1136 C C . VAL A 154 ? 0.2140 0.2467 0.2129 0.0040 0.0066 -0.0241 154 VAL A C 1137 O O . VAL A 154 ? 0.2044 0.2367 0.2000 0.0019 0.0075 -0.0206 154 VAL A O 1138 C CB . VAL A 154 ? 0.2345 0.2720 0.2383 0.0083 0.0062 -0.0304 154 VAL A CB 1139 C CG1 . VAL A 154 ? 0.2397 0.2860 0.2418 0.0072 0.0074 -0.0287 154 VAL A CG1 1140 C CG2 . VAL A 154 ? 0.2392 0.2720 0.2447 0.0096 0.0059 -0.0320 154 VAL A CG2 1141 N N . TRP A 155 ? 0.1996 0.2362 0.2007 0.0047 0.0055 -0.0257 155 TRP A N 1142 C CA . TRP A 155 ? 0.2063 0.2448 0.2058 0.0025 0.0052 -0.0227 155 TRP A CA 1143 C C . TRP A 155 ? 0.1989 0.2266 0.1938 -0.0002 0.0053 -0.0188 155 TRP A C 1144 O O . TRP A 155 ? 0.1973 0.2253 0.1892 -0.0028 0.0054 -0.0151 155 TRP A O 1145 C CB . TRP A 155 ? 0.2058 0.2468 0.2087 0.0039 0.0038 -0.0250 155 TRP A CB 1146 C CG . TRP A 155 ? 0.2107 0.2640 0.2171 0.0062 0.0036 -0.0279 155 TRP A CG 1147 C CD1 . TRP A 155 ? 0.2134 0.2705 0.2236 0.0099 0.0031 -0.0330 155 TRP A CD1 1148 C CD2 . TRP A 155 ? 0.2071 0.2712 0.2137 0.0053 0.0039 -0.0260 155 TRP A CD2 1149 N NE1 . TRP A 155 ? 0.2140 0.2838 0.2263 0.0117 0.0032 -0.0348 155 TRP A NE1 1150 C CE2 . TRP A 155 ? 0.2072 0.2820 0.2175 0.0088 0.0038 -0.0303 155 TRP A CE2 1151 C CE3 . TRP A 155 ? 0.2153 0.2811 0.2192 0.0017 0.0039 -0.0208 155 TRP A CE3 1152 C CZ2 . TRP A 155 ? 0.2173 0.3057 0.2288 0.0091 0.0042 -0.0296 155 TRP A CZ2 1153 C CZ3 . TRP A 155 ? 0.2149 0.2939 0.2203 0.0014 0.0040 -0.0195 155 TRP A CZ3 1154 C CH2 . TRP A 155 ? 0.2200 0.3108 0.2294 0.0053 0.0043 -0.0239 155 TRP A CH2 1155 N N . GLN A 156 ? 0.1909 0.2094 0.1855 0.0003 0.0050 -0.0195 156 GLN A N 1156 C CA . GLN A 156 ? 0.1919 0.2001 0.1817 -0.0018 0.0051 -0.0162 156 GLN A CA 1157 C C . GLN A 156 ? 0.1945 0.1985 0.1803 -0.0029 0.0064 -0.0137 156 GLN A C 1158 O O . GLN A 156 ? 0.1945 0.1923 0.1757 -0.0051 0.0063 -0.0107 156 GLN A O 1159 C CB . GLN A 156 ? 0.1898 0.1903 0.1802 -0.0009 0.0047 -0.0174 156 GLN A CB 1160 C CG . GLN A 156 ? 0.1945 0.1976 0.1883 -0.0004 0.0030 -0.0189 156 GLN A CG 1161 C CD . GLN A 156 ? 0.1983 0.1951 0.1940 0.0006 0.0022 -0.0202 156 GLN A CD 1162 O OE1 . GLN A 156 ? 0.1949 0.1915 0.1933 0.0024 0.0023 -0.0222 156 GLN A OE1 1163 N NE2 . GLN A 156 ? 0.2089 0.2009 0.2033 -0.0007 0.0011 -0.0187 156 GLN A NE2 1164 N N . GLN A 157 ? 0.1900 0.1975 0.1776 -0.0014 0.0075 -0.0150 157 GLN A N 1165 C CA . GLN A 157 ? 0.1912 0.1959 0.1760 -0.0019 0.0088 -0.0129 157 GLN A CA 1166 C C . GLN A 157 ? 0.1989 0.2113 0.1834 -0.0035 0.0088 -0.0109 157 GLN A C 1167 O O . GLN A 157 ? 0.1866 0.1988 0.1699 -0.0038 0.0096 -0.0093 157 GLN A O 1168 C CB . GLN A 157 ? 0.1915 0.1964 0.1789 0.0002 0.0098 -0.0150 157 GLN A CB 1169 C CG . GLN A 157 ? 0.1983 0.1949 0.1856 0.0013 0.0100 -0.0155 157 GLN A CG 1170 C CD . GLN A 157 ? 0.2012 0.1989 0.1916 0.0031 0.0104 -0.0171 157 GLN A CD 1171 O OE1 . GLN A 157 ? 0.2151 0.2163 0.2099 0.0046 0.0092 -0.0202 157 GLN A OE1 1172 N NE2 . GLN A 157 ? 0.1975 0.1925 0.1861 0.0032 0.0118 -0.0151 157 GLN A NE2 1173 N N . THR A 158 ? 0.2039 0.2241 0.1900 -0.0043 0.0077 -0.0110 158 THR A N 1174 C CA . THR A 158 ? 0.2127 0.2406 0.1985 -0.0063 0.0074 -0.0083 158 THR A CA 1175 C C . THR A 158 ? 0.2204 0.2419 0.2020 -0.0095 0.0063 -0.0038 158 THR A C 1176 O O . THR A 158 ? 0.2287 0.2452 0.2086 -0.0106 0.0052 -0.0031 158 THR A O 1177 C CB . THR A 158 ? 0.2085 0.2481 0.1978 -0.0059 0.0066 -0.0097 158 THR A CB 1178 O OG1 . THR A 158 ? 0.1937 0.2389 0.1865 -0.0027 0.0073 -0.0142 158 THR A OG1 1179 C CG2 . THR A 158 ? 0.2111 0.2604 0.2003 -0.0081 0.0063 -0.0062 158 THR A CG2 1180 N N . THR A 159 ? 0.2233 0.2453 0.2033 -0.0111 0.0064 -0.0008 159 THR A N 1181 C CA A THR A 159 ? 0.2326 0.2495 0.2091 -0.0143 0.0048 0.0034 159 THR A CA 1182 C CA B THR A 159 ? 0.2400 0.2561 0.2163 -0.0142 0.0048 0.0033 159 THR A CA 1183 C C . THR A 159 ? 0.2381 0.2592 0.2152 -0.0164 0.0028 0.0049 159 THR A C 1184 O O . THR A 159 ? 0.2251 0.2582 0.2059 -0.0162 0.0028 0.0045 159 THR A O 1185 C CB A THR A 159 ? 0.2324 0.2531 0.2089 -0.0158 0.0046 0.0066 159 THR A CB 1186 C CB B THR A 159 ? 0.2487 0.2662 0.2242 -0.0157 0.0046 0.0066 159 THR A CB 1187 O OG1 A THR A 159 ? 0.2235 0.2365 0.1983 -0.0140 0.0061 0.0058 159 THR A OG1 1188 O OG1 B THR A 159 ? 0.2735 0.2827 0.2451 -0.0186 0.0025 0.0105 159 THR A OG1 1189 C CG2 A THR A 159 ? 0.2403 0.2579 0.2141 -0.0197 0.0020 0.0116 159 THR A CG2 1190 C CG2 B THR A 159 ? 0.2392 0.2709 0.2183 -0.0166 0.0044 0.0078 159 THR A CG2 1191 N N . GLY A 160 ? 0.2542 0.2661 0.2278 -0.0183 0.0012 0.0067 160 GLY A N 1192 C CA . GLY A 160 ? 0.2544 0.2701 0.2287 -0.0206 -0.0007 0.0085 160 GLY A CA 1193 C C . GLY A 160 ? 0.2522 0.2684 0.2284 -0.0188 -0.0005 0.0054 160 GLY A C 1194 O O . GLY A 160 ? 0.2538 0.2731 0.2309 -0.0206 -0.0022 0.0069 160 GLY A O 1195 N N . SER A 161 ? 0.2361 0.2488 0.2131 -0.0156 0.0012 0.0014 161 SER A N 1196 C CA . SER A 161 ? 0.2254 0.2397 0.2053 -0.0136 0.0013 -0.0017 161 SER A CA 1197 C C . SER A 161 ? 0.2286 0.2338 0.2053 -0.0154 -0.0002 -0.0004 161 SER A C 1198 O O . SER A 161 ? 0.2480 0.2441 0.2196 -0.0175 -0.0011 0.0020 161 SER A O 1199 C CB . SER A 161 ? 0.2116 0.2236 0.1932 -0.0102 0.0031 -0.0058 161 SER A CB 1200 O OG . SER A 161 ? 0.2087 0.2086 0.1859 -0.0103 0.0037 -0.0052 161 SER A OG 1201 N N . ALA A 162 ? 0.2200 0.2280 0.1997 -0.0146 -0.0008 -0.0021 162 ALA A N 1202 C CA . ALA A 162 ? 0.2167 0.2163 0.1938 -0.0160 -0.0024 -0.0012 162 ALA A CA 1203 C C . ALA A 162 ? 0.2138 0.2012 0.1867 -0.0150 -0.0015 -0.0023 162 ALA A C 1204 O O . ALA A 162 ? 0.2044 0.1824 0.1718 -0.0170 -0.0025 -0.0004 162 ALA A O 1205 C CB . ALA A 162 ? 0.2180 0.2231 0.1999 -0.0148 -0.0031 -0.0030 162 ALA A CB 1206 N N . LEU A 163 ? 0.2115 0.1995 0.1865 -0.0121 0.0003 -0.0052 163 LEU A N 1207 C CA . LEU A 163 ? 0.2064 0.1849 0.1784 -0.0109 0.0015 -0.0060 163 LEU A CA 1208 C C . LEU A 163 ? 0.2095 0.1809 0.1758 -0.0118 0.0021 -0.0040 163 LEU A C 1209 O O . LEU A 163 ? 0.2173 0.1792 0.1786 -0.0123 0.0019 -0.0033 163 LEU A O 1210 C CB . LEU A 163 ? 0.2027 0.1846 0.1793 -0.0077 0.0030 -0.0092 163 LEU A CB 1211 C CG . LEU A 163 ? 0.2016 0.1744 0.1754 -0.0066 0.0041 -0.0095 163 LEU A CG 1212 C CD1 . LEU A 163 ? 0.2092 0.1813 0.1865 -0.0054 0.0034 -0.0113 163 LEU A CD1 1213 C CD2 . LEU A 163 ? 0.2060 0.1796 0.1803 -0.0049 0.0061 -0.0100 163 LEU A CD2 1214 N N . THR A 164 ? 0.2114 0.1873 0.1783 -0.0119 0.0028 -0.0031 164 THR A N 1215 C CA . THR A 164 ? 0.2203 0.1896 0.1823 -0.0128 0.0030 -0.0011 164 THR A CA 1216 C C . THR A 164 ? 0.2282 0.1915 0.1854 -0.0159 0.0005 0.0016 164 THR A C 1217 O O . THR A 164 ? 0.2419 0.1954 0.1936 -0.0160 0.0004 0.0024 164 THR A O 1218 C CB . THR A 164 ? 0.2157 0.1916 0.1800 -0.0124 0.0040 -0.0005 164 THR A CB 1219 O OG1 . THR A 164 ? 0.2197 0.2062 0.1877 -0.0138 0.0029 0.0003 164 THR A OG1 1220 C CG2 . THR A 164 ? 0.2193 0.1982 0.1872 -0.0092 0.0063 -0.0033 164 THR A CG2 1221 N N . THR A 165 ? 0.2275 0.1964 0.1866 -0.0181 -0.0013 0.0030 165 THR A N 1222 C CA . THR A 165 ? 0.2424 0.2057 0.1974 -0.0214 -0.0042 0.0058 165 THR A CA 1223 C C . THR A 165 ? 0.2458 0.1983 0.1960 -0.0212 -0.0047 0.0048 165 THR A C 1224 O O . THR A 165 ? 0.2634 0.2059 0.2074 -0.0223 -0.0060 0.0059 165 THR A O 1225 C CB . THR A 165 ? 0.2442 0.2174 0.2033 -0.0237 -0.0061 0.0077 165 THR A CB 1226 O OG1 . THR A 165 ? 0.2391 0.2227 0.2021 -0.0239 -0.0055 0.0088 165 THR A OG1 1227 C CG2 . THR A 165 ? 0.2494 0.2175 0.2048 -0.0277 -0.0096 0.0112 165 THR A CG2 1228 N N . ALA A 166 ? 0.2398 0.1948 0.1930 -0.0196 -0.0038 0.0026 166 ALA A N 1229 C CA . ALA A 166 ? 0.2389 0.1857 0.1885 -0.0195 -0.0042 0.0018 166 ALA A CA 1230 C C . ALA A 166 ? 0.2464 0.1837 0.1905 -0.0176 -0.0026 0.0009 166 ALA A C 1231 O O . ALA A 166 ? 0.2407 0.1684 0.1783 -0.0185 -0.0037 0.0014 166 ALA A O 1232 C CB . ALA A 166 ? 0.2316 0.1834 0.1864 -0.0179 -0.0035 -0.0002 166 ALA A CB 1233 N N . LEU A 167 ? 0.2339 0.1742 0.1806 -0.0149 0.0000 -0.0004 167 LEU A N 1234 C CA . LEU A 167 ? 0.2457 0.1780 0.1878 -0.0127 0.0018 -0.0011 167 LEU A CA 1235 C C . LEU A 167 ? 0.2603 0.1845 0.1959 -0.0140 0.0005 0.0004 167 LEU A C 1236 O O . LEU A 167 ? 0.2658 0.1805 0.1949 -0.0133 0.0004 0.0000 167 LEU A O 1237 C CB . LEU A 167 ? 0.2363 0.1740 0.1828 -0.0101 0.0045 -0.0022 167 LEU A CB 1238 C CG . LEU A 167 ? 0.2416 0.1731 0.1845 -0.0077 0.0066 -0.0025 167 LEU A CG 1239 C CD1 . LEU A 167 ? 0.2480 0.1747 0.1886 -0.0063 0.0075 -0.0034 167 LEU A CD1 1240 C CD2 . LEU A 167 ? 0.2446 0.1819 0.1920 -0.0057 0.0088 -0.0030 167 LEU A CD2 1241 N N . ARG A 168 ? 0.2649 0.1927 0.2019 -0.0158 -0.0007 0.0022 168 ARG A N 1242 C CA . ARG A 168 ? 0.2776 0.1974 0.2090 -0.0169 -0.0023 0.0038 168 ARG A CA 1243 C C . ARG A 168 ? 0.2890 0.2007 0.2146 -0.0196 -0.0058 0.0049 168 ARG A C 1244 O O . ARG A 168 ? 0.2886 0.1898 0.2075 -0.0193 -0.0068 0.0047 168 ARG A O 1245 C CB . ARG A 168 ? 0.2836 0.2095 0.2184 -0.0183 -0.0031 0.0060 168 ARG A CB 1246 C CG . ARG A 168 ? 0.2971 0.2290 0.2344 -0.0221 -0.0061 0.0087 168 ARG A CG 1247 C CD . ARG A 168 ? 0.3017 0.2377 0.2409 -0.0239 -0.0074 0.0117 168 ARG A CD 1248 N NE . ARG A 168 ? 0.3025 0.2473 0.2454 -0.0272 -0.0096 0.0141 168 ARG A NE 1249 C CZ . ARG A 168 ? 0.3187 0.2765 0.2678 -0.0270 -0.0084 0.0142 168 ARG A CZ 1250 N NH1 . ARG A 168 ? 0.3241 0.2881 0.2768 -0.0242 -0.0054 0.0121 168 ARG A NH1 1251 N NH2 . ARG A 168 ? 0.3353 0.3005 0.2872 -0.0300 -0.0106 0.0167 168 ARG A NH2 1252 N N . ASN A 169 ? 0.2843 0.2014 0.2129 -0.0221 -0.0076 0.0059 169 ASN A N 1253 C CA . ASN A 169 ? 0.2867 0.1972 0.2106 -0.0250 -0.0109 0.0071 169 ASN A CA 1254 C C . ASN A 169 ? 0.2997 0.2019 0.2181 -0.0236 -0.0104 0.0050 169 ASN A C 1255 O O . ASN A 169 ? 0.3027 0.1964 0.2150 -0.0254 -0.0131 0.0057 169 ASN A O 1256 C CB . ASN A 169 ? 0.2749 0.1943 0.2039 -0.0280 -0.0130 0.0091 169 ASN A CB 1257 C CG . ASN A 169 ? 0.2834 0.2083 0.2150 -0.0308 -0.0150 0.0124 169 ASN A CG 1258 O OD1 . ASN A 169 ? 0.2739 0.1929 0.2021 -0.0315 -0.0163 0.0136 169 ASN A OD1 1259 N ND2 . ASN A 169 ? 0.2710 0.2076 0.2090 -0.0323 -0.0155 0.0139 169 ASN A ND2 1260 N N . ALA A 170 ? 0.2913 0.1956 0.2116 -0.0204 -0.0071 0.0028 170 ALA A N 1261 C CA . ALA A 170 ? 0.2945 0.1918 0.2098 -0.0188 -0.0062 0.0012 170 ALA A CA 1262 C C . ALA A 170 ? 0.3064 0.1957 0.2157 -0.0158 -0.0043 -0.0001 170 ALA A C 1263 O O . ALA A 170 ? 0.3246 0.2089 0.2294 -0.0141 -0.0032 -0.0014 170 ALA A O 1264 C CB . ALA A 170 ? 0.2920 0.1963 0.2131 -0.0170 -0.0038 0.0000 170 ALA A CB 1265 N N . GLY A 171 ? 0.3081 0.1969 0.2175 -0.0150 -0.0039 0.0002 171 GLY A N 1266 C CA . GLY A 171 ? 0.3118 0.1929 0.2158 -0.0120 -0.0024 -0.0009 171 GLY A CA 1267 C C . GLY A 171 ? 0.3061 0.1924 0.2143 -0.0085 0.0015 -0.0017 171 GLY A C 1268 O O . GLY A 171 ? 0.3277 0.2088 0.2321 -0.0055 0.0032 -0.0026 171 GLY A O 1269 N N . GLY A 172 ? 0.3012 0.1977 0.2173 -0.0088 0.0027 -0.0014 172 GLY A N 1270 C CA . GLY A 172 ? 0.2924 0.1948 0.2134 -0.0059 0.0061 -0.0021 172 GLY A CA 1271 C C . GLY A 172 ? 0.2780 0.1817 0.2006 -0.0044 0.0074 -0.0016 172 GLY A C 1272 O O . GLY A 172 ? 0.2739 0.1819 0.2001 -0.0019 0.0102 -0.0021 172 GLY A O 1273 N N . LEU A 173 ? 0.2796 0.1803 0.2002 -0.0062 0.0051 -0.0003 173 LEU A N 1274 C CA . LEU A 173 ? 0.2820 0.1829 0.2036 -0.0049 0.0060 0.0005 173 LEU A CA 1275 C C . LEU A 173 ? 0.2905 0.1814 0.2057 -0.0020 0.0068 -0.0001 173 LEU A C 1276 O O . LEU A 173 ? 0.2922 0.1824 0.2081 -0.0008 0.0073 0.0007 173 LEU A O 1277 C CB . LEU A 173 ? 0.2845 0.1897 0.2092 -0.0081 0.0035 0.0028 173 LEU A CB 1278 C CG . LEU A 173 ? 0.2836 0.2006 0.2153 -0.0102 0.0032 0.0034 173 LEU A CG 1279 C CD1 . LEU A 173 ? 0.2943 0.2159 0.2285 -0.0128 0.0012 0.0061 173 LEU A CD1 1280 C CD2 . LEU A 173 ? 0.2789 0.2033 0.2159 -0.0076 0.0065 0.0019 173 LEU A CD2 1281 N N . THR A 174 ? 0.2942 0.1782 0.2035 -0.0006 0.0072 -0.0017 174 THR A N 1282 C CA . THR A 174 ? 0.3046 0.1801 0.2075 0.0029 0.0085 -0.0029 174 THR A CA 1283 C C . THR A 174 ? 0.3114 0.1906 0.2155 0.0061 0.0124 -0.0040 174 THR A C 1284 O O . THR A 174 ? 0.3020 0.1848 0.2077 0.0050 0.0126 -0.0043 174 THR A O 1285 C CB . THR A 174 ? 0.3128 0.1776 0.2071 0.0018 0.0054 -0.0039 174 THR A CB 1286 O OG1 . THR A 174 ? 0.3014 0.1624 0.1950 -0.0010 0.0016 -0.0025 174 THR A OG1 1287 C CG2 . THR A 174 ? 0.3273 0.1833 0.2142 0.0060 0.0069 -0.0059 174 THR A CG2 1288 N N . GLN A 175 ? 0.3300 0.2083 0.2335 0.0100 0.0153 -0.0043 175 GLN A N 1289 C CA . GLN A 175 ? 0.3372 0.2199 0.2424 0.0128 0.0188 -0.0046 175 GLN A CA 1290 C C . GLN A 175 ? 0.3431 0.2209 0.2419 0.0132 0.0186 -0.0059 175 GLN A C 1291 O O . GLN A 175 ? 0.3494 0.2183 0.2406 0.0128 0.0164 -0.0071 175 GLN A O 1292 C CB . GLN A 175 ? 0.3415 0.2243 0.2468 0.0172 0.0220 -0.0044 175 GLN A CB 1293 C CG . GLN A 175 ? 0.3620 0.2358 0.2587 0.0208 0.0229 -0.0059 175 GLN A CG 1294 C CD . GLN A 175 ? 0.3723 0.2481 0.2699 0.0255 0.0266 -0.0055 175 GLN A CD 1295 O OE1 . GLN A 175 ? 0.3515 0.2349 0.2564 0.0259 0.0283 -0.0038 175 GLN A OE1 1296 N NE2 . GLN A 175 ? 0.3810 0.2501 0.2712 0.0294 0.0278 -0.0071 175 GLN A NE2 1297 N N . ILE A 176 ? 0.3266 0.2102 0.2286 0.0134 0.0203 -0.0055 176 ILE A N 1298 C CA . ILE A 176 ? 0.3352 0.2163 0.2324 0.0132 0.0201 -0.0061 176 ILE A CA 1299 C C . ILE A 176 ? 0.3393 0.2220 0.2350 0.0173 0.0238 -0.0059 176 ILE A C 1300 O O . ILE A 176 ? 0.3446 0.2227 0.2332 0.0189 0.0243 -0.0068 176 ILE A O 1301 C CB . ILE A 176 ? 0.3369 0.2242 0.2401 0.0097 0.0186 -0.0053 176 ILE A CB 1302 C CG1 . ILE A 176 ? 0.3366 0.2226 0.2406 0.0059 0.0150 -0.0054 176 ILE A CG1 1303 C CG2 . ILE A 176 ? 0.3330 0.2192 0.2327 0.0096 0.0187 -0.0054 176 ILE A CG2 1304 C CD1 . ILE A 176 ? 0.3259 0.2187 0.2365 0.0028 0.0134 -0.0048 176 ILE A CD1 1305 N N . VAL A 177 ? 0.3254 0.2150 0.2275 0.0190 0.0263 -0.0045 177 VAL A N 1306 C CA . VAL A 177 ? 0.3295 0.2210 0.2305 0.0233 0.0300 -0.0038 177 VAL A CA 1307 C C . VAL A 177 ? 0.3340 0.2256 0.2369 0.0256 0.0314 -0.0036 177 VAL A C 1308 O O . VAL A 177 ? 0.3296 0.2216 0.2362 0.0233 0.0295 -0.0035 177 VAL A O 1309 C CB . VAL A 177 ? 0.3094 0.2099 0.2175 0.0228 0.0314 -0.0017 177 VAL A CB 1310 C CG1 . VAL A 177 ? 0.3051 0.2059 0.2127 0.0199 0.0295 -0.0016 177 VAL A CG1 1311 C CG2 . VAL A 177 ? 0.3037 0.2110 0.2213 0.0212 0.0311 -0.0006 177 VAL A CG2 1312 N N . PRO A 178 ? 0.3497 0.2417 0.2507 0.0302 0.0347 -0.0031 178 PRO A N 1313 C CA . PRO A 178 ? 0.3398 0.2323 0.2433 0.0325 0.0360 -0.0026 178 PRO A CA 1314 C C . PRO A 178 ? 0.3194 0.2202 0.2330 0.0299 0.0357 -0.0006 178 PRO A C 1315 O O . PRO A 178 ? 0.3070 0.2152 0.2262 0.0295 0.0369 0.0010 178 PRO A O 1316 C CB . PRO A 178 ? 0.3492 0.2439 0.2509 0.0376 0.0400 -0.0017 178 PRO A CB 1317 C CG . PRO A 178 ? 0.3589 0.2502 0.2530 0.0386 0.0403 -0.0029 178 PRO A CG 1318 C CD . PRO A 178 ? 0.3626 0.2555 0.2593 0.0335 0.0374 -0.0028 178 PRO A CD 1319 N N . THR A 179 ? 0.3204 0.2198 0.2360 0.0280 0.0337 -0.0009 179 THR A N 1320 C CA . THR A 179 ? 0.3095 0.2163 0.2335 0.0253 0.0328 0.0003 179 THR A CA 1321 C C . THR A 179 ? 0.3119 0.2196 0.2386 0.0266 0.0334 0.0013 179 THR A C 1322 O O . THR A 179 ? 0.3231 0.2242 0.2454 0.0277 0.0326 0.0007 179 THR A O 1323 C CB . THR A 179 ? 0.2977 0.2040 0.2224 0.0209 0.0293 -0.0006 179 THR A CB 1324 O OG1 . THR A 179 ? 0.2877 0.1939 0.2108 0.0198 0.0288 -0.0012 179 THR A OG1 1325 C CG2 . THR A 179 ? 0.2820 0.1962 0.2147 0.0183 0.0284 0.0001 179 THR A CG2 1326 N N . THR A 180 ? 0.2925 0.2084 0.2266 0.0265 0.0346 0.0031 180 THR A N 1327 C CA . THR A 180 ? 0.2798 0.1986 0.2181 0.0268 0.0349 0.0045 180 THR A CA 1328 C C . THR A 180 ? 0.2652 0.1908 0.2099 0.0228 0.0328 0.0046 180 THR A C 1329 O O . THR A 180 ? 0.2554 0.1864 0.2042 0.0216 0.0327 0.0046 180 THR A O 1330 C CB . THR A 180 ? 0.2776 0.2009 0.2192 0.0303 0.0382 0.0065 180 THR A CB 1331 O OG1 . THR A 180 ? 0.2903 0.2087 0.2260 0.0344 0.0404 0.0062 180 THR A OG1 1332 C CG2 . THR A 180 ? 0.2749 0.2014 0.2211 0.0308 0.0384 0.0083 180 THR A CG2 1333 N N . ASN A 181 ? 0.2535 0.1786 0.1988 0.0211 0.0310 0.0049 181 ASN A N 1334 C CA . ASN A 181 ? 0.2512 0.1830 0.2017 0.0179 0.0292 0.0051 181 ASN A CA 1335 C C . ASN A 181 ? 0.2565 0.1928 0.2115 0.0184 0.0299 0.0070 181 ASN A C 1336 O O . ASN A 181 ? 0.2681 0.2007 0.2211 0.0189 0.0294 0.0080 181 ASN A O 1337 C CB . ASN A 181 ? 0.2534 0.1820 0.2010 0.0149 0.0262 0.0042 181 ASN A CB 1338 C CG . ASN A 181 ? 0.2571 0.1815 0.2006 0.0140 0.0253 0.0025 181 ASN A CG 1339 O OD1 . ASN A 181 ? 0.2471 0.1755 0.1932 0.0135 0.0256 0.0017 181 ASN A OD1 1340 N ND2 . ASN A 181 ? 0.2735 0.1895 0.2106 0.0139 0.0239 0.0020 181 ASN A ND2 1341 N N . LEU A 182 ? 0.2424 0.1866 0.2034 0.0182 0.0307 0.0077 182 LEU A N 1342 C CA . LEU A 182 ? 0.2525 0.2020 0.2182 0.0184 0.0311 0.0097 182 LEU A CA 1343 C C . LEU A 182 ? 0.2526 0.2089 0.2220 0.0149 0.0288 0.0090 182 LEU A C 1344 O O . LEU A 182 ? 0.2619 0.2223 0.2338 0.0137 0.0281 0.0073 182 LEU A O 1345 C CB . LEU A 182 ? 0.2451 0.1989 0.2150 0.0206 0.0333 0.0112 182 LEU A CB 1346 C CG . LEU A 182 ? 0.2454 0.2045 0.2202 0.0213 0.0342 0.0137 182 LEU A CG 1347 C CD1 . LEU A 182 ? 0.2533 0.2195 0.2324 0.0181 0.0321 0.0133 182 LEU A CD1 1348 C CD2 . LEU A 182 ? 0.2638 0.2182 0.2360 0.0232 0.0350 0.0153 182 LEU A CD2 1349 N N . TYR A 183 ? 0.2588 0.2163 0.2286 0.0135 0.0276 0.0102 183 TYR A N 1350 C CA . TYR A 183 ? 0.2478 0.2124 0.2204 0.0104 0.0256 0.0098 183 TYR A CA 1351 C C . TYR A 183 ? 0.2466 0.2148 0.2214 0.0095 0.0251 0.0122 183 TYR A C 1352 O O . TYR A 183 ? 0.2470 0.2117 0.2213 0.0113 0.0261 0.0143 183 TYR A O 1353 C CB . TYR A 183 ? 0.2476 0.2094 0.2167 0.0083 0.0237 0.0083 183 TYR A CB 1354 C CG . TYR A 183 ? 0.2604 0.2148 0.2248 0.0076 0.0224 0.0097 183 TYR A CG 1355 C CD1 . TYR A 183 ? 0.2669 0.2117 0.2262 0.0098 0.0231 0.0094 183 TYR A CD1 1356 C CD2 . TYR A 183 ? 0.2524 0.2099 0.2174 0.0047 0.0201 0.0113 183 TYR A CD2 1357 C CE1 . TYR A 183 ? 0.2842 0.2217 0.2392 0.0092 0.0213 0.0103 183 TYR A CE1 1358 C CE2 . TYR A 183 ? 0.2691 0.2197 0.2302 0.0038 0.0183 0.0127 183 TYR A CE2 1359 C CZ . TYR A 183 ? 0.2823 0.2224 0.2384 0.0060 0.0187 0.0121 183 TYR A CZ 1360 O OH . TYR A 183 ? 0.2982 0.2307 0.2503 0.0050 0.0163 0.0133 183 TYR A OH 1361 N N . SER A 184 ? 0.2384 0.2142 0.2158 0.0069 0.0235 0.0121 184 SER A N 1362 C CA . SER A 184 ? 0.2385 0.2196 0.2186 0.0057 0.0229 0.0146 184 SER A CA 1363 C C . SER A 184 ? 0.2397 0.2254 0.2196 0.0025 0.0206 0.0150 184 SER A C 1364 O O . SER A 184 ? 0.2288 0.2185 0.2088 0.0011 0.0197 0.0128 184 SER A O 1365 C CB . SER A 184 ? 0.2411 0.2304 0.2262 0.0061 0.0236 0.0142 184 SER A CB 1366 O OG . SER A 184 ? 0.2347 0.2299 0.2227 0.0050 0.0231 0.0168 184 SER A OG 1367 N N . ALA A 185 ? 0.2412 0.2276 0.2214 0.0012 0.0195 0.0182 185 ALA A N 1368 C CA . ALA A 185 ? 0.2344 0.2272 0.2153 -0.0022 0.0172 0.0196 185 ALA A CA 1369 C C . ALA A 185 ? 0.2217 0.2266 0.2062 -0.0034 0.0171 0.0185 185 ALA A C 1370 O O . ALA A 185 ? 0.2105 0.2219 0.1953 -0.0058 0.0156 0.0186 185 ALA A O 1371 C CB . ALA A 185 ? 0.2333 0.2245 0.2144 -0.0034 0.0159 0.0239 185 ALA A CB 1372 N N . THR A 186 ? 0.2187 0.2269 0.2061 -0.0019 0.0185 0.0179 186 THR A N 1373 C CA . THR A 186 ? 0.2308 0.2498 0.2214 -0.0028 0.0182 0.0169 186 THR A CA 1374 C C . THR A 186 ? 0.2447 0.2652 0.2360 -0.0014 0.0187 0.0124 186 THR A C 1375 O O . THR A 186 ? 0.2760 0.3001 0.2700 -0.0004 0.0192 0.0110 186 THR A O 1376 C CB . THR A 186 ? 0.2363 0.2581 0.2300 -0.0021 0.0189 0.0191 186 THR A CB 1377 O OG1 . THR A 186 ? 0.2388 0.2541 0.2328 0.0006 0.0207 0.0183 186 THR A OG1 1378 C CG2 . THR A 186 ? 0.2403 0.2609 0.2340 -0.0034 0.0182 0.0238 186 THR A CG2 1379 N N . ASP A 187 ? 0.2353 0.2520 0.2241 -0.0015 0.0183 0.0104 187 ASP A N 1380 C CA . ASP A 187 ? 0.2287 0.2462 0.2180 -0.0005 0.0183 0.0064 187 ASP A CA 1381 C C . ASP A 187 ? 0.2341 0.2615 0.2245 -0.0020 0.0169 0.0045 187 ASP A C 1382 O O . ASP A 187 ? 0.2404 0.2697 0.2291 -0.0039 0.0160 0.0059 187 ASP A O 1383 C CB . ASP A 187 ? 0.2180 0.2257 0.2040 0.0002 0.0187 0.0058 187 ASP A CB 1384 C CG . ASP A 187 ? 0.2212 0.2280 0.2081 0.0015 0.0187 0.0021 187 ASP A CG 1385 O OD1 . ASP A 187 ? 0.2029 0.2171 0.1920 0.0011 0.0178 -0.0004 187 ASP A OD1 1386 O OD2 . ASP A 187 ? 0.2228 0.2219 0.2084 0.0031 0.0198 0.0019 187 ASP A OD2 1387 N N . GLU A 188 ? 0.2290 0.2628 0.2220 -0.0011 0.0167 0.0013 188 GLU A N 1388 C CA . GLU A 188 ? 0.2292 0.2732 0.2231 -0.0018 0.0156 -0.0009 188 GLU A CA 1389 C C . GLU A 188 ? 0.2275 0.2704 0.2210 -0.0010 0.0150 -0.0044 188 GLU A C 1390 O O . GLU A 188 ? 0.2174 0.2688 0.2117 -0.0011 0.0142 -0.0067 188 GLU A O 1391 C CB . GLU A 188 ? 0.2378 0.2896 0.2345 -0.0011 0.0152 -0.0029 188 GLU A CB 1392 C CG . GLU A 188 ? 0.2393 0.2879 0.2380 0.0010 0.0149 -0.0066 188 GLU A CG 1393 C CD . GLU A 188 ? 0.2463 0.2875 0.2460 0.0018 0.0158 -0.0046 188 GLU A CD 1394 O OE1 . GLU A 188 ? 0.2278 0.2605 0.2259 0.0022 0.0169 -0.0026 188 GLU A OE1 1395 O OE2 . GLU A 188 ? 0.2662 0.3106 0.2681 0.0022 0.0154 -0.0048 188 GLU A OE2 1396 N N . ILE A 189 ? 0.2219 0.2551 0.2143 0.0000 0.0155 -0.0049 189 ILE A N 1397 C CA . ILE A 189 ? 0.2175 0.2488 0.2098 0.0007 0.0149 -0.0080 189 ILE A CA 1398 C C . ILE A 189 ? 0.2176 0.2434 0.2068 -0.0006 0.0147 -0.0061 189 ILE A C 1399 O O . ILE A 189 ? 0.2329 0.2625 0.2220 -0.0012 0.0138 -0.0074 189 ILE A O 1400 C CB . ILE A 189 ? 0.2145 0.2399 0.2085 0.0027 0.0150 -0.0103 189 ILE A CB 1401 C CG1 . ILE A 189 ? 0.2214 0.2520 0.2186 0.0037 0.0145 -0.0122 189 ILE A CG1 1402 C CG2 . ILE A 189 ? 0.2215 0.2453 0.2159 0.0034 0.0140 -0.0134 189 ILE A CG2 1403 C CD1 . ILE A 189 ? 0.2184 0.2591 0.2174 0.0041 0.0131 -0.0158 189 ILE A CD1 1404 N N . VAL A 190 ? 0.2091 0.2266 0.1958 -0.0009 0.0155 -0.0031 190 VAL A N 1405 C CA . VAL A 190 ? 0.2096 0.2199 0.1925 -0.0021 0.0152 -0.0011 190 VAL A CA 1406 C C . VAL A 190 ? 0.2214 0.2320 0.2027 -0.0040 0.0148 0.0027 190 VAL A C 1407 O O . VAL A 190 ? 0.2141 0.2219 0.1954 -0.0035 0.0156 0.0047 190 VAL A O 1408 C CB . VAL A 190 ? 0.2132 0.2127 0.1940 -0.0005 0.0163 -0.0010 190 VAL A CB 1409 C CG1 . VAL A 190 ? 0.2256 0.2171 0.2019 -0.0016 0.0157 0.0006 190 VAL A CG1 1410 C CG2 . VAL A 190 ? 0.2192 0.2184 0.2021 0.0010 0.0164 -0.0044 190 VAL A CG2 1411 N N . GLN A 191 ? 0.2197 0.2337 0.2002 -0.0063 0.0133 0.0040 191 GLN A N 1412 C CA . GLN A 191 ? 0.2237 0.2374 0.2026 -0.0087 0.0121 0.0081 191 GLN A CA 1413 C C . GLN A 191 ? 0.2274 0.2380 0.2038 -0.0107 0.0103 0.0090 191 GLN A C 1414 O O . GLN A 191 ? 0.2265 0.2404 0.2038 -0.0104 0.0101 0.0065 191 GLN A O 1415 C CB . GLN A 191 ? 0.2224 0.2485 0.2042 -0.0102 0.0116 0.0096 191 GLN A CB 1416 C CG . GLN A 191 ? 0.2245 0.2531 0.2083 -0.0090 0.0128 0.0098 191 GLN A CG 1417 C CD . GLN A 191 ? 0.2202 0.2408 0.2026 -0.0093 0.0128 0.0134 191 GLN A CD 1418 O OE1 . GLN A 191 ? 0.2078 0.2226 0.1877 -0.0109 0.0114 0.0162 191 GLN A OE1 1419 N NE2 . GLN A 191 ? 0.2216 0.2411 0.2054 -0.0074 0.0142 0.0131 191 GLN A NE2 1420 N N . PRO A 192 ? 0.2154 0.2194 0.1889 -0.0127 0.0087 0.0124 192 PRO A N 1421 C CA . PRO A 192 ? 0.2195 0.2199 0.1924 -0.0131 0.0085 0.0156 192 PRO A CA 1422 C C . PRO A 192 ? 0.2209 0.2098 0.1914 -0.0102 0.0101 0.0145 192 PRO A C 1423 O O . PRO A 192 ? 0.2237 0.2034 0.1907 -0.0091 0.0102 0.0130 192 PRO A O 1424 C CB . PRO A 192 ? 0.2260 0.2243 0.1971 -0.0166 0.0054 0.0197 192 PRO A CB 1425 C CG . PRO A 192 ? 0.2213 0.2149 0.1898 -0.0170 0.0046 0.0179 192 PRO A CG 1426 C CD . PRO A 192 ? 0.2137 0.2146 0.1848 -0.0151 0.0065 0.0139 192 PRO A CD 1427 N N . GLN A 193 ? 0.2248 0.2144 0.1969 -0.0090 0.0113 0.0157 193 GLN A N 1428 C CA . GLN A 193 ? 0.2360 0.2166 0.2065 -0.0060 0.0130 0.0154 193 GLN A CA 1429 C C . GLN A 193 ? 0.2380 0.2158 0.2087 -0.0062 0.0125 0.0189 193 GLN A C 1430 O O . GLN A 193 ? 0.2368 0.2084 0.2066 -0.0035 0.0140 0.0188 193 GLN A O 1431 C CB . GLN A 193 ? 0.2289 0.2140 0.2025 -0.0036 0.0154 0.0129 193 GLN A CB 1432 C CG . GLN A 193 ? 0.2316 0.2177 0.2052 -0.0028 0.0160 0.0093 193 GLN A CG 1433 C CD . GLN A 193 ? 0.2401 0.2159 0.2101 -0.0010 0.0168 0.0079 193 GLN A CD 1434 O OE1 . GLN A 193 ? 0.2353 0.2034 0.2011 -0.0016 0.0157 0.0087 193 GLN A OE1 1435 N NE2 . GLN A 193 ? 0.2386 0.2142 0.2102 0.0013 0.0186 0.0058 193 GLN A NE2 1436 N N . VAL A 194 ? 0.2578 0.2403 0.2296 -0.0093 0.0101 0.0221 194 VAL A N 1437 C CA . VAL A 194 ? 0.2751 0.2576 0.2485 -0.0100 0.0092 0.0260 194 VAL A CA 1438 C C . VAL A 194 ? 0.3027 0.2731 0.2725 -0.0102 0.0070 0.0281 194 VAL A C 1439 O O . VAL A 194 ? 0.3191 0.2876 0.2902 -0.0102 0.0062 0.0312 194 VAL A O 1440 C CB . VAL A 194 ? 0.2713 0.2662 0.2482 -0.0137 0.0073 0.0291 194 VAL A CB 1441 C CG1 . VAL A 194 ? 0.2690 0.2758 0.2493 -0.0131 0.0093 0.0267 194 VAL A CG1 1442 C CG2 . VAL A 194 ? 0.2737 0.2703 0.2492 -0.0172 0.0045 0.0305 194 VAL A CG2 1443 N N . SER A 195 ? 0.3037 0.2655 0.2691 -0.0103 0.0059 0.0267 195 SER A N 1444 C CA . SER A 195 ? 0.3057 0.2563 0.2676 -0.0111 0.0028 0.0290 195 SER A CA 1445 C C . SER A 195 ? 0.3040 0.2425 0.2625 -0.0069 0.0042 0.0274 195 SER A C 1446 O O . SER A 195 ? 0.3190 0.2482 0.2752 -0.0068 0.0017 0.0292 195 SER A O 1447 C CB . SER A 195 ? 0.3120 0.2590 0.2706 -0.0136 0.0002 0.0286 195 SER A CB 1448 O OG . SER A 195 ? 0.3206 0.2800 0.2829 -0.0171 -0.0008 0.0305 195 SER A OG 1449 N N . ASN A 196 ? 0.2862 0.2246 0.2443 -0.0033 0.0078 0.0242 196 ASN A N 1450 C CA . ASN A 196 ? 0.2929 0.2207 0.2471 0.0008 0.0095 0.0222 196 ASN A CA 1451 C C . ASN A 196 ? 0.3110 0.2268 0.2587 0.0004 0.0068 0.0212 196 ASN A C 1452 O O . ASN A 196 ? 0.3156 0.2211 0.2600 0.0020 0.0052 0.0216 196 ASN A O 1453 C CB . ASN A 196 ? 0.3076 0.2333 0.2639 0.0032 0.0101 0.0245 196 ASN A CB 1454 C CG . ASN A 196 ? 0.3232 0.2395 0.2758 0.0085 0.0126 0.0223 196 ASN A CG 1455 O OD1 . ASN A 196 ? 0.3536 0.2620 0.3047 0.0106 0.0115 0.0234 196 ASN A OD1 1456 N ND2 . ASN A 196 ? 0.3122 0.2292 0.2634 0.0108 0.0156 0.0193 196 ASN A ND2 1457 N N . SER A 197 ? 0.2895 0.2068 0.2356 -0.0017 0.0059 0.0198 197 SER A N 1458 C CA . SER A 197 ? 0.2989 0.2069 0.2397 -0.0035 0.0025 0.0195 197 SER A CA 1459 C C . SER A 197 ? 0.3007 0.2111 0.2399 -0.0045 0.0031 0.0171 197 SER A C 1460 O O . SER A 197 ? 0.2811 0.2008 0.2240 -0.0042 0.0057 0.0159 197 SER A O 1461 C CB . SER A 197 ? 0.2981 0.2072 0.2406 -0.0079 -0.0018 0.0236 197 SER A CB 1462 O OG . SER A 197 ? 0.2908 0.2089 0.2357 -0.0119 -0.0031 0.0247 197 SER A OG 1463 N N . PRO A 198 ? 0.3012 0.2031 0.2352 -0.0057 0.0005 0.0163 198 PRO A N 1464 C CA . PRO A 198 ? 0.3131 0.2175 0.2461 -0.0073 0.0005 0.0147 198 PRO A CA 1465 C C . PRO A 198 ? 0.2997 0.2172 0.2383 -0.0107 0.0001 0.0161 198 PRO A C 1466 O O . PRO A 198 ? 0.3083 0.2293 0.2472 -0.0110 0.0010 0.0142 198 PRO A O 1467 C CB . PRO A 198 ? 0.3202 0.2137 0.2473 -0.0094 -0.0038 0.0152 198 PRO A CB 1468 C CG . PRO A 198 ? 0.3302 0.2124 0.2532 -0.0065 -0.0043 0.0148 198 PRO A CG 1469 C CD . PRO A 198 ? 0.3244 0.2135 0.2532 -0.0058 -0.0029 0.0170 198 PRO A CD 1470 N N . LEU A 199 ? 0.3024 0.2273 0.2455 -0.0130 -0.0011 0.0193 199 LEU A N 1471 C CA . LEU A 199 ? 0.2917 0.2304 0.2401 -0.0156 -0.0009 0.0203 199 LEU A CA 1472 C C . LEU A 199 ? 0.2787 0.2253 0.2305 -0.0128 0.0030 0.0174 199 LEU A C 1473 O O . LEU A 199 ? 0.2695 0.2260 0.2247 -0.0140 0.0034 0.0167 199 LEU A O 1474 C CB . LEU A 199 ? 0.2895 0.2351 0.2416 -0.0186 -0.0031 0.0246 199 LEU A CB 1475 C CG . LEU A 199 ? 0.3106 0.2494 0.2602 -0.0221 -0.0079 0.0283 199 LEU A CG 1476 C CD1 . LEU A 199 ? 0.3149 0.2614 0.2689 -0.0252 -0.0101 0.0332 199 LEU A CD1 1477 C CD2 . LEU A 199 ? 0.3167 0.2553 0.2645 -0.0249 -0.0102 0.0284 199 LEU A CD2 1478 N N . ASP A 200 ? 0.2702 0.2131 0.2216 -0.0092 0.0057 0.0159 200 ASP A N 1479 C CA . ASP A 200 ? 0.2547 0.2056 0.2102 -0.0072 0.0088 0.0139 200 ASP A CA 1480 C C . ASP A 200 ? 0.2485 0.1992 0.2031 -0.0062 0.0100 0.0107 200 ASP A C 1481 O O . ASP A 200 ? 0.2395 0.1816 0.1897 -0.0054 0.0098 0.0095 200 ASP A O 1482 C CB . ASP A 200 ? 0.2633 0.2112 0.2192 -0.0039 0.0112 0.0138 200 ASP A CB 1483 C CG . ASP A 200 ? 0.2670 0.2156 0.2244 -0.0048 0.0100 0.0172 200 ASP A CG 1484 O OD1 . ASP A 200 ? 0.2649 0.2212 0.2252 -0.0079 0.0082 0.0196 200 ASP A OD1 1485 O OD2 . ASP A 200 ? 0.2689 0.2106 0.2248 -0.0021 0.0110 0.0176 200 ASP A OD2 1486 N N . SER A 201 ? 0.2377 0.1980 0.1968 -0.0059 0.0113 0.0091 201 SER A N 1487 C CA . SER A 201 ? 0.2326 0.1936 0.1919 -0.0053 0.0119 0.0064 201 SER A CA 1488 C C . SER A 201 ? 0.2284 0.1819 0.1853 -0.0022 0.0140 0.0046 201 SER A C 1489 O O . SER A 201 ? 0.2272 0.1765 0.1818 -0.0020 0.0138 0.0031 201 SER A O 1490 C CB . SER A 201 ? 0.2254 0.1982 0.1901 -0.0056 0.0123 0.0049 201 SER A CB 1491 O OG . SER A 201 ? 0.2177 0.1904 0.1829 -0.0049 0.0124 0.0022 201 SER A OG 1492 N N . SER A 202 ? 0.2304 0.1823 0.1878 0.0000 0.0158 0.0052 202 SER A N 1493 C CA . SER A 202 ? 0.2347 0.1808 0.1903 0.0032 0.0181 0.0041 202 SER A CA 1494 C C . SER A 202 ? 0.2599 0.1950 0.2090 0.0043 0.0179 0.0045 202 SER A C 1495 O O . SER A 202 ? 0.2701 0.2006 0.2170 0.0071 0.0199 0.0036 202 SER A O 1496 C CB . SER A 202 ? 0.2328 0.1830 0.1923 0.0053 0.0203 0.0049 202 SER A CB 1497 O OG . SER A 202 ? 0.2134 0.1731 0.1784 0.0047 0.0205 0.0039 202 SER A OG 1498 N N . TYR A 203 ? 0.2776 0.2083 0.2236 0.0023 0.0154 0.0058 203 TYR A N 1499 C CA . TYR A 203 ? 0.2853 0.2046 0.2248 0.0037 0.0148 0.0057 203 TYR A CA 1500 C C . TYR A 203 ? 0.2933 0.2067 0.2279 0.0033 0.0140 0.0040 203 TYR A C 1501 O O . TYR A 203 ? 0.3014 0.2171 0.2364 0.0003 0.0119 0.0039 203 TYR A O 1502 C CB . TYR A 203 ? 0.3056 0.2217 0.2438 0.0014 0.0118 0.0081 203 TYR A CB 1503 C CG . TYR A 203 ? 0.3156 0.2196 0.2476 0.0030 0.0106 0.0081 203 TYR A CG 1504 C CD1 . TYR A 203 ? 0.3286 0.2237 0.2544 0.0025 0.0086 0.0069 203 TYR A CD1 1505 C CD2 . TYR A 203 ? 0.3407 0.2424 0.2734 0.0051 0.0112 0.0095 203 TYR A CD2 1506 C CE1 . TYR A 203 ? 0.3619 0.2453 0.2817 0.0041 0.0071 0.0065 203 TYR A CE1 1507 C CE2 . TYR A 203 ? 0.3682 0.2586 0.2955 0.0070 0.0099 0.0092 203 TYR A CE2 1508 C CZ . TYR A 203 ? 0.3780 0.2592 0.2987 0.0065 0.0077 0.0076 203 TYR A CZ 1509 O OH . TYR A 203 ? 0.4368 0.3063 0.3518 0.0087 0.0061 0.0069 203 TYR A OH 1510 N N . LEU A 204 ? 0.3033 0.2091 0.2330 0.0064 0.0155 0.0027 204 LEU A N 1511 C CA . LEU A 204 ? 0.2994 0.1975 0.2228 0.0063 0.0144 0.0012 204 LEU A CA 1512 C C . LEU A 204 ? 0.3125 0.1994 0.2290 0.0081 0.0133 0.0009 204 LEU A C 1513 O O . LEU A 204 ? 0.2973 0.1820 0.2133 0.0115 0.0153 0.0010 204 LEU A O 1514 C CB . LEU A 204 ? 0.3049 0.2041 0.2279 0.0086 0.0171 -0.0003 204 LEU A CB 1515 C CG . LEU A 204 ? 0.3032 0.2121 0.2327 0.0072 0.0178 -0.0004 204 LEU A CG 1516 C CD1 . LEU A 204 ? 0.3130 0.2219 0.2419 0.0096 0.0202 -0.0014 204 LEU A CD1 1517 C CD2 . LEU A 204 ? 0.2936 0.2041 0.2235 0.0035 0.0150 -0.0007 204 LEU A CD2 1518 N N . PHE A 205 ? 0.3200 0.1995 0.2310 0.0060 0.0101 0.0004 205 PHE A N 1519 C CA . PHE A 205 ? 0.3335 0.2011 0.2372 0.0077 0.0085 -0.0004 205 PHE A CA 1520 C C . PHE A 205 ? 0.3544 0.2177 0.2531 0.0124 0.0117 -0.0028 205 PHE A C 1521 O O . PHE A 205 ? 0.3470 0.2132 0.2453 0.0126 0.0134 -0.0038 205 PHE A O 1522 C CB . PHE A 205 ? 0.3393 0.2002 0.2383 0.0041 0.0040 -0.0003 205 PHE A CB 1523 C CG . PHE A 205 ? 0.3486 0.2137 0.2520 -0.0005 0.0005 0.0025 205 PHE A CG 1524 C CD1 . PHE A 205 ? 0.3536 0.2153 0.2576 -0.0010 -0.0016 0.0045 205 PHE A CD1 1525 C CD2 . PHE A 205 ? 0.3513 0.2233 0.2581 -0.0043 -0.0007 0.0035 205 PHE A CD2 1526 C CE1 . PHE A 205 ? 0.3486 0.2149 0.2567 -0.0057 -0.0051 0.0078 205 PHE A CE1 1527 C CE2 . PHE A 205 ? 0.3487 0.2257 0.2595 -0.0085 -0.0037 0.0065 205 PHE A CE2 1528 C CZ . PHE A 205 ? 0.3508 0.2252 0.2623 -0.0093 -0.0059 0.0088 205 PHE A CZ 1529 N N . ASN A 206 ? 0.3723 0.2298 0.2681 0.0162 0.0127 -0.0033 206 ASN A N 1530 C CA . ASN A 206 ? 0.3749 0.2291 0.2664 0.0217 0.0162 -0.0053 206 ASN A CA 1531 C C . ASN A 206 ? 0.3585 0.2226 0.2560 0.0240 0.0207 -0.0044 206 ASN A C 1532 O O . ASN A 206 ? 0.3349 0.1982 0.2297 0.0285 0.0240 -0.0054 206 ASN A O 1533 C CB . ASN A 206 ? 0.4071 0.2552 0.2908 0.0223 0.0158 -0.0077 206 ASN A CB 1534 C CG . ASN A 206 ? 0.4296 0.2665 0.3063 0.0202 0.0110 -0.0089 206 ASN A CG 1535 O OD1 . ASN A 206 ? 0.4673 0.2968 0.3414 0.0213 0.0090 -0.0092 206 ASN A OD1 1536 N ND2 . ASN A 206 ? 0.4699 0.3057 0.3441 0.0168 0.0088 -0.0093 206 ASN A ND2 1537 N N . GLY A 207 ? 0.3278 0.2017 0.2334 0.0213 0.0210 -0.0024 207 GLY A N 1538 C CA . GLY A 207 ? 0.3198 0.2027 0.2316 0.0232 0.0246 -0.0013 207 GLY A CA 1539 C C . GLY A 207 ? 0.3201 0.2034 0.2343 0.0259 0.0260 0.0000 207 GLY A C 1540 O O . GLY A 207 ? 0.3224 0.1996 0.2347 0.0258 0.0237 0.0003 207 GLY A O 1541 N N . LYS A 208 ? 0.3205 0.2107 0.2392 0.0282 0.0293 0.0010 208 LYS A N 1542 C CA . LYS A 208 ? 0.3221 0.2156 0.2452 0.0304 0.0309 0.0029 208 LYS A CA 1543 C C . LYS A 208 ? 0.3054 0.2074 0.2361 0.0265 0.0297 0.0047 208 LYS A C 1544 O O . LYS A 208 ? 0.2961 0.2062 0.2319 0.0257 0.0311 0.0053 208 LYS A O 1545 C CB . LYS A 208 ? 0.3356 0.2327 0.2598 0.0347 0.0350 0.0034 208 LYS A CB 1546 C CG . LYS A 208 ? 0.3518 0.2522 0.2804 0.0374 0.0369 0.0056 208 LYS A CG 1547 C CD . LYS A 208 ? 0.3818 0.2734 0.3060 0.0399 0.0359 0.0050 208 LYS A CD 1548 C CE . LYS A 208 ? 0.4081 0.3036 0.3369 0.0433 0.0383 0.0073 208 LYS A CE 1549 N NZ . LYS A 208 ? 0.4293 0.3181 0.3570 0.0442 0.0362 0.0076 208 LYS A NZ 1550 N N . ASN A 209 ? 0.2970 0.1971 0.2282 0.0240 0.0269 0.0055 209 ASN A N 1551 C CA . ASN A 209 ? 0.3077 0.2158 0.2450 0.0201 0.0253 0.0070 209 ASN A CA 1552 C C . ASN A 209 ? 0.3061 0.2180 0.2480 0.0213 0.0263 0.0093 209 ASN A C 1553 O O . ASN A 209 ? 0.3370 0.2434 0.2771 0.0222 0.0250 0.0103 209 ASN A O 1554 C CB . ASN A 209 ? 0.3087 0.2138 0.2439 0.0160 0.0214 0.0070 209 ASN A CB 1555 C CG . ASN A 209 ? 0.3165 0.2173 0.2468 0.0148 0.0202 0.0049 209 ASN A CG 1556 O OD1 . ASN A 209 ? 0.3158 0.2220 0.2483 0.0139 0.0212 0.0040 209 ASN A OD1 1557 N ND2 . ASN A 209 ? 0.3304 0.2212 0.2543 0.0146 0.0178 0.0041 209 ASN A ND2 1558 N N . VAL A 210 ? 0.2859 0.2070 0.2337 0.0213 0.0282 0.0102 210 VAL A N 1559 C CA . VAL A 210 ? 0.2944 0.2203 0.2470 0.0224 0.0294 0.0125 210 VAL A CA 1560 C C . VAL A 210 ? 0.2995 0.2349 0.2580 0.0185 0.0279 0.0136 210 VAL A C 1561 O O . VAL A 210 ? 0.2853 0.2279 0.2477 0.0179 0.0288 0.0131 210 VAL A O 1562 C CB . VAL A 210 ? 0.2914 0.2205 0.2462 0.0259 0.0329 0.0130 210 VAL A CB 1563 C CG1 . VAL A 210 ? 0.2873 0.2204 0.2468 0.0272 0.0338 0.0157 210 VAL A CG1 1564 C CG2 . VAL A 210 ? 0.3026 0.2242 0.2514 0.0298 0.0347 0.0115 210 VAL A CG2 1565 N N . GLN A 211 ? 0.3071 0.2422 0.2658 0.0160 0.0253 0.0151 211 GLN A N 1566 C CA . GLN A 211 ? 0.3111 0.2554 0.2753 0.0132 0.0242 0.0169 211 GLN A CA 1567 C C . GLN A 211 ? 0.3010 0.2486 0.2693 0.0152 0.0259 0.0193 211 GLN A C 1568 O O . GLN A 211 ? 0.2979 0.2398 0.2648 0.0174 0.0261 0.0208 211 GLN A O 1569 C CB . GLN A 211 ? 0.3200 0.2633 0.2832 0.0098 0.0209 0.0184 211 GLN A CB 1570 C CG . GLN A 211 ? 0.3057 0.2600 0.2737 0.0064 0.0197 0.0196 211 GLN A CG 1571 C CD . GLN A 211 ? 0.3325 0.2867 0.3010 0.0038 0.0169 0.0229 211 GLN A CD 1572 O OE1 . GLN A 211 ? 0.3092 0.2589 0.2778 0.0052 0.0167 0.0250 211 GLN A OE1 1573 N NE2 . GLN A 211 ? 0.3213 0.2805 0.2903 0.0000 0.0145 0.0234 211 GLN A NE2 1574 N N . ALA A 212 ? 0.2949 0.2514 0.2681 0.0147 0.0270 0.0195 212 ALA A N 1575 C CA . ALA A 212 ? 0.2934 0.2535 0.2706 0.0168 0.0289 0.0216 212 ALA A CA 1576 C C . ALA A 212 ? 0.2938 0.2542 0.2728 0.0161 0.0276 0.0248 212 ALA A C 1577 O O . ALA A 212 ? 0.3128 0.2708 0.2927 0.0191 0.0291 0.0266 212 ALA A O 1578 C CB . ALA A 212 ? 0.2932 0.2626 0.2752 0.0155 0.0293 0.0212 212 ALA A CB 1579 N N . GLN A 213 ? 0.2804 0.2434 0.2596 0.0125 0.0249 0.0256 213 GLN A N 1580 C CA . GLN A 213 ? 0.2911 0.2552 0.2723 0.0111 0.0231 0.0291 213 GLN A CA 1581 C C . GLN A 213 ? 0.3196 0.2726 0.2971 0.0131 0.0222 0.0300 213 GLN A C 1582 O O . GLN A 213 ? 0.3169 0.2691 0.2967 0.0136 0.0214 0.0332 213 GLN A O 1583 C CB . GLN A 213 ? 0.2776 0.2479 0.2598 0.0065 0.0202 0.0300 213 GLN A CB 1584 C CG . GLN A 213 ? 0.2711 0.2534 0.2572 0.0044 0.0205 0.0293 213 GLN A CG 1585 C CD . GLN A 213 ? 0.2656 0.2490 0.2504 0.0049 0.0217 0.0252 213 GLN A CD 1586 O OE1 . GLN A 213 ? 0.2499 0.2266 0.2307 0.0054 0.0216 0.0231 213 GLN A OE1 1587 N NE2 . GLN A 213 ? 0.2696 0.2610 0.2579 0.0048 0.0225 0.0241 213 GLN A NE2 1588 N N . ALA A 214 ? 0.3210 0.2655 0.2930 0.0142 0.0220 0.0274 214 ALA A N 1589 C CA . ALA A 214 ? 0.3471 0.2799 0.3148 0.0168 0.0212 0.0273 214 ALA A CA 1590 C C . ALA A 214 ? 0.3632 0.2932 0.3315 0.0219 0.0242 0.0276 214 ALA A C 1591 O O . ALA A 214 ? 0.3713 0.2939 0.3381 0.0243 0.0234 0.0287 214 ALA A O 1592 C CB . ALA A 214 ? 0.3481 0.2732 0.3095 0.0170 0.0206 0.0241 214 ALA A CB 1593 N N . VAL A 215 ? 0.3518 0.2876 0.3224 0.0238 0.0275 0.0269 215 VAL A N 1594 C CA . VAL A 215 ? 0.3614 0.2967 0.3335 0.0285 0.0306 0.0278 215 VAL A CA 1595 C C . VAL A 215 ? 0.3593 0.3035 0.3384 0.0277 0.0310 0.0313 215 VAL A C 1596 O O . VAL A 215 ? 0.3633 0.3061 0.3444 0.0309 0.0322 0.0335 215 VAL A O 1597 C CB . VAL A 215 ? 0.3678 0.3047 0.3386 0.0309 0.0338 0.0255 215 VAL A CB 1598 C CG1 . VAL A 215 ? 0.3776 0.3166 0.3510 0.0354 0.0372 0.0271 215 VAL A CG1 1599 C CG2 . VAL A 215 ? 0.3722 0.3005 0.3358 0.0318 0.0335 0.0221 215 VAL A CG2 1600 N N . CYS A 216 ? 0.3426 0.2959 0.3255 0.0236 0.0300 0.0320 216 CYS A N 1601 C CA . CYS A 216 ? 0.3526 0.3150 0.3418 0.0230 0.0306 0.0349 216 CYS A CA 1602 C C . CYS A 216 ? 0.3770 0.3434 0.3692 0.0195 0.0278 0.0379 216 CYS A C 1603 O O . CYS A 216 ? 0.4093 0.3827 0.4067 0.0189 0.0280 0.0409 216 CYS A O 1604 C CB . CYS A 216 ? 0.3416 0.3123 0.3335 0.0214 0.0317 0.0336 216 CYS A CB 1605 S SG . CYS A 216 ? 0.3418 0.3099 0.3320 0.0254 0.0349 0.0315 216 CYS A SG 1606 N N . GLY A 217 ? 0.3658 0.3282 0.3550 0.0170 0.0251 0.0376 217 GLY A N 1607 C CA . GLY A 217 ? 0.3643 0.3299 0.3560 0.0136 0.0221 0.0409 217 GLY A CA 1608 C C . GLY A 217 ? 0.3653 0.3397 0.3578 0.0091 0.0206 0.0402 217 GLY A C 1609 O O . GLY A 217 ? 0.3335 0.3121 0.3257 0.0089 0.0220 0.0372 217 GLY A O 1610 N N . PRO A 218 ? 0.3840 0.3611 0.3775 0.0054 0.0175 0.0430 218 PRO A N 1611 C CA . PRO A 218 ? 0.4039 0.3891 0.3976 0.0011 0.0158 0.0425 218 PRO A CA 1612 C C . PRO A 218 ? 0.3859 0.3833 0.3834 -0.0002 0.0167 0.0425 218 PRO A C 1613 O O . PRO A 218 ? 0.3910 0.3955 0.3883 -0.0027 0.0160 0.0409 218 PRO A O 1614 C CB . PRO A 218 ? 0.4221 0.4069 0.4164 -0.0020 0.0121 0.0466 218 PRO A CB 1615 C CG . PRO A 218 ? 0.4170 0.3965 0.4135 0.0002 0.0120 0.0498 218 PRO A CG 1616 C CD . PRO A 218 ? 0.4184 0.3899 0.4126 0.0053 0.0152 0.0467 218 PRO A CD 1617 N N . LEU A 219 ? 0.3923 0.3929 0.3935 0.0013 0.0182 0.0441 219 LEU A N 1618 C CA . LEU A 219 ? 0.3959 0.4076 0.4004 0.0000 0.0188 0.0435 219 LEU A CA 1619 C C . LEU A 219 ? 0.3688 0.3799 0.3731 0.0027 0.0213 0.0400 219 LEU A C 1620 O O . LEU A 219 ? 0.3644 0.3831 0.3716 0.0021 0.0217 0.0395 219 LEU A O 1621 C CB . LEU A 219 ? 0.4398 0.4568 0.4488 -0.0004 0.0185 0.0477 219 LEU A CB 1622 C CG . LEU A 219 ? 0.4598 0.4772 0.4699 -0.0030 0.0158 0.0523 219 LEU A CG 1623 C CD1 . LEU A 219 ? 0.4852 0.5064 0.5001 -0.0025 0.0160 0.0564 219 LEU A CD1 1624 C CD2 . LEU A 219 ? 0.4574 0.4833 0.4668 -0.0074 0.0135 0.0524 219 LEU A CD2 1625 N N . PHE A 220 ? 0.3347 0.3368 0.3358 0.0055 0.0228 0.0377 220 PHE A N 1626 C CA . PHE A 220 ? 0.3246 0.3266 0.3259 0.0076 0.0249 0.0347 220 PHE A CA 1627 C C . PHE A 220 ? 0.3167 0.3229 0.3166 0.0055 0.0239 0.0310 220 PHE A C 1628 O O . PHE A 220 ? 0.3019 0.3059 0.2986 0.0040 0.0227 0.0297 220 PHE A O 1629 C CB . PHE A 220 ? 0.3272 0.3190 0.3254 0.0114 0.0268 0.0338 220 PHE A CB 1630 C CG . PHE A 220 ? 0.3197 0.3114 0.3184 0.0136 0.0289 0.0318 220 PHE A CG 1631 C CD1 . PHE A 220 ? 0.3183 0.3137 0.3211 0.0152 0.0304 0.0337 220 PHE A CD1 1632 C CD2 . PHE A 220 ? 0.3087 0.2965 0.3039 0.0140 0.0293 0.0283 220 PHE A CD2 1633 C CE1 . PHE A 220 ? 0.3109 0.3066 0.3147 0.0170 0.0321 0.0325 220 PHE A CE1 1634 C CE2 . PHE A 220 ? 0.3215 0.3094 0.3177 0.0160 0.0310 0.0270 220 PHE A CE2 1635 C CZ . PHE A 220 ? 0.3052 0.2972 0.3057 0.0173 0.0323 0.0292 220 PHE A CZ 1636 N N . VAL A 221 ? 0.3195 0.3316 0.3219 0.0055 0.0244 0.0292 221 VAL A N 1637 C CA . VAL A 221 ? 0.3031 0.3197 0.3048 0.0039 0.0234 0.0255 221 VAL A CA 1638 C C . VAL A 221 ? 0.2947 0.3095 0.2971 0.0058 0.0245 0.0229 221 VAL A C 1639 O O . VAL A 221 ? 0.2810 0.2983 0.2869 0.0068 0.0251 0.0238 221 VAL A O 1640 C CB . VAL A 221 ? 0.3029 0.3302 0.3072 0.0013 0.0217 0.0257 221 VAL A CB 1641 C CG1 . VAL A 221 ? 0.2935 0.3253 0.2971 0.0005 0.0208 0.0211 221 VAL A CG1 1642 C CG2 . VAL A 221 ? 0.3185 0.3486 0.3223 -0.0009 0.0204 0.0290 221 VAL A CG2 1643 N N . ILE A 222 ? 0.2683 0.2785 0.2677 0.0063 0.0246 0.0200 222 ILE A N 1644 C CA . ILE A 222 ? 0.2662 0.2762 0.2663 0.0072 0.0247 0.0168 222 ILE A CA 1645 C C . ILE A 222 ? 0.2589 0.2703 0.2569 0.0056 0.0233 0.0134 222 ILE A C 1646 O O . ILE A 222 ? 0.2585 0.2669 0.2532 0.0047 0.0229 0.0137 222 ILE A O 1647 C CB . ILE A 222 ? 0.2604 0.2629 0.2594 0.0098 0.0267 0.0173 222 ILE A CB 1648 C CG1 . ILE A 222 ? 0.2810 0.2757 0.2751 0.0105 0.0272 0.0171 222 ILE A CG1 1649 C CG2 . ILE A 222 ? 0.2561 0.2587 0.2579 0.0116 0.0283 0.0209 222 ILE A CG2 1650 C CD1 . ILE A 222 ? 0.2900 0.2776 0.2820 0.0133 0.0292 0.0172 222 ILE A CD1 1651 N N . ASP A 223 ? 0.2354 0.2515 0.2354 0.0052 0.0222 0.0103 223 ASP A N 1652 C CA . ASP A 223 ? 0.2273 0.2462 0.2258 0.0040 0.0208 0.0071 223 ASP A CA 1653 C C . ASP A 223 ? 0.2262 0.2385 0.2229 0.0051 0.0211 0.0048 223 ASP A C 1654 O O . ASP A 223 ? 0.2334 0.2387 0.2290 0.0067 0.0226 0.0062 223 ASP A O 1655 C CB . ASP A 223 ? 0.2144 0.2430 0.2156 0.0030 0.0191 0.0046 223 ASP A CB 1656 C CG . ASP A 223 ? 0.2109 0.2397 0.2147 0.0042 0.0182 0.0012 223 ASP A CG 1657 O OD1 . ASP A 223 ? 0.2223 0.2456 0.2273 0.0055 0.0190 0.0022 223 ASP A OD1 1658 O OD2 . ASP A 223 ? 0.2038 0.2387 0.2088 0.0039 0.0165 -0.0021 223 ASP A OD2 1659 N N . HIS A 224 ? 0.2133 0.2284 0.2100 0.0046 0.0198 0.0014 224 HIS A N 1660 C CA . HIS A 224 ? 0.2251 0.2346 0.2205 0.0054 0.0198 -0.0005 224 HIS A CA 1661 C C . HIS A 224 ? 0.2262 0.2322 0.2239 0.0070 0.0203 -0.0006 224 HIS A C 1662 O O . HIS A 224 ? 0.2385 0.2381 0.2345 0.0079 0.0211 -0.0001 224 HIS A O 1663 C CB . HIS A 224 ? 0.2312 0.2455 0.2271 0.0047 0.0181 -0.0042 224 HIS A CB 1664 C CG . HIS A 224 ? 0.2358 0.2446 0.2301 0.0052 0.0179 -0.0058 224 HIS A CG 1665 N ND1 . HIS A 224 ? 0.2398 0.2423 0.2302 0.0047 0.0186 -0.0042 224 HIS A ND1 1666 C CD2 . HIS A 224 ? 0.2410 0.2495 0.2373 0.0059 0.0167 -0.0089 224 HIS A CD2 1667 C CE1 . HIS A 224 ? 0.2463 0.2452 0.2362 0.0051 0.0181 -0.0061 224 HIS A CE1 1668 N NE2 . HIS A 224 ? 0.2405 0.2430 0.2341 0.0058 0.0169 -0.0088 224 HIS A NE2 1669 N N . ALA A 225 ? 0.2177 0.2284 0.2192 0.0072 0.0193 -0.0012 225 ALA A N 1670 C CA . ALA A 225 ? 0.2142 0.2225 0.2188 0.0083 0.0193 -0.0007 225 ALA A CA 1671 C C . ALA A 225 ? 0.2075 0.2130 0.2122 0.0093 0.0214 0.0035 225 ALA A C 1672 O O . ALA A 225 ? 0.1938 0.1946 0.1985 0.0105 0.0225 0.0049 225 ALA A O 1673 C CB . ALA A 225 ? 0.2198 0.2336 0.2286 0.0080 0.0170 -0.0029 225 ALA A CB 1674 N N . GLY A 226 ? 0.1988 0.2071 0.2033 0.0088 0.0221 0.0057 226 GLY A N 1675 C CA . GLY A 226 ? 0.2114 0.2173 0.2161 0.0101 0.0242 0.0097 226 GLY A CA 1676 C C . GLY A 226 ? 0.2080 0.2063 0.2086 0.0116 0.0263 0.0111 226 GLY A C 1677 O O . GLY A 226 ? 0.2202 0.2159 0.2212 0.0135 0.0282 0.0138 226 GLY A O 1678 N N . SER A 227 ? 0.2174 0.2128 0.2141 0.0109 0.0259 0.0092 227 SER A N 1679 C CA . SER A 227 ? 0.2234 0.2111 0.2154 0.0120 0.0271 0.0094 227 SER A CA 1680 C C . SER A 227 ? 0.2283 0.2125 0.2205 0.0137 0.0282 0.0094 227 SER A C 1681 O O . SER A 227 ? 0.2293 0.2080 0.2185 0.0158 0.0302 0.0110 227 SER A O 1682 C CB . SER A 227 ? 0.2269 0.2137 0.2158 0.0103 0.0256 0.0070 227 SER A CB 1683 O OG . SER A 227 ? 0.2316 0.2205 0.2193 0.0087 0.0249 0.0081 227 SER A OG 1684 N N . LEU A 228 ? 0.2170 0.2047 0.2129 0.0130 0.0267 0.0078 228 LEU A N 1685 C CA . LEU A 228 ? 0.2181 0.2037 0.2153 0.0141 0.0271 0.0082 228 LEU A CA 1686 C C . LEU A 228 ? 0.2197 0.2079 0.2208 0.0153 0.0282 0.0115 228 LEU A C 1687 O O . LEU A 228 ? 0.2293 0.2151 0.2300 0.0170 0.0299 0.0136 228 LEU A O 1688 C CB . LEU A 228 ? 0.2189 0.2067 0.2189 0.0127 0.0245 0.0052 228 LEU A CB 1689 C CG . LEU A 228 ? 0.2106 0.1969 0.2130 0.0132 0.0239 0.0056 228 LEU A CG 1690 C CD1 . LEU A 228 ? 0.2141 0.1946 0.2117 0.0143 0.0258 0.0065 228 LEU A CD1 1691 C CD2 . LEU A 228 ? 0.2161 0.2042 0.2213 0.0118 0.0209 0.0022 228 LEU A CD2 1692 N N . THR A 229 ? 0.2183 0.2120 0.2232 0.0143 0.0271 0.0119 229 THR A N 1693 C CA . THR A 229 ? 0.2227 0.2201 0.2328 0.0146 0.0269 0.0145 229 THR A CA 1694 C C . THR A 229 ? 0.2302 0.2292 0.2413 0.0159 0.0290 0.0185 229 THR A C 1695 O O . THR A 229 ? 0.2335 0.2350 0.2487 0.0166 0.0294 0.0216 229 THR A O 1696 C CB . THR A 229 ? 0.2122 0.2148 0.2267 0.0127 0.0237 0.0125 229 THR A CB 1697 O OG1 . THR A 229 ? 0.2099 0.2163 0.2240 0.0117 0.0233 0.0120 229 THR A OG1 1698 C CG2 . THR A 229 ? 0.2147 0.2163 0.2292 0.0117 0.0213 0.0085 229 THR A CG2 1699 N N . SER A 230 ? 0.2401 0.2378 0.2480 0.0162 0.0301 0.0188 230 SER A N 1700 C CA . SER A 230 ? 0.2340 0.2334 0.2434 0.0174 0.0317 0.0224 230 SER A CA 1701 C C . SER A 230 ? 0.2404 0.2373 0.2496 0.0205 0.0346 0.0257 230 SER A C 1702 O O . SER A 230 ? 0.2384 0.2308 0.2444 0.0220 0.0359 0.0250 230 SER A O 1703 C CB . SER A 230 ? 0.2348 0.2326 0.2408 0.0171 0.0319 0.0222 230 SER A CB 1704 O OG . SER A 230 ? 0.2458 0.2366 0.2466 0.0188 0.0335 0.0217 230 SER A OG 1705 N N . GLN A 231 ? 0.2489 0.2489 0.2612 0.0216 0.0357 0.0293 231 GLN A N 1706 C CA . GLN A 231 ? 0.2724 0.2707 0.2843 0.0252 0.0390 0.0327 231 GLN A CA 1707 C C . GLN A 231 ? 0.2572 0.2482 0.2626 0.0275 0.0408 0.0313 231 GLN A C 1708 O O . GLN A 231 ? 0.2821 0.2700 0.2850 0.0301 0.0428 0.0316 231 GLN A O 1709 C CB . GLN A 231 ? 0.2677 0.2711 0.2846 0.0260 0.0397 0.0369 231 GLN A CB 1710 C CG . GLN A 231 ? 0.2809 0.2831 0.2975 0.0301 0.0431 0.0403 231 GLN A CG 1711 C CD . GLN A 231 ? 0.2919 0.2955 0.3097 0.0316 0.0445 0.0418 231 GLN A CD 1712 O OE1 . GLN A 231 ? 0.3003 0.3068 0.3211 0.0292 0.0425 0.0416 231 GLN A OE1 1713 N NE2 . GLN A 231 ? 0.2961 0.2976 0.3116 0.0357 0.0479 0.0435 231 GLN A NE2 1714 N N . PHE A 232 ? 0.2540 0.2425 0.2569 0.0265 0.0398 0.0299 232 PHE A N 1715 C CA . PHE A 232 ? 0.2571 0.2379 0.2538 0.0282 0.0406 0.0285 232 PHE A CA 1716 C C . PHE A 232 ? 0.2576 0.2340 0.2499 0.0280 0.0404 0.0254 232 PHE A C 1717 O O . PHE A 232 ? 0.2622 0.2329 0.2499 0.0308 0.0422 0.0249 232 PHE A O 1718 C CB . PHE A 232 ? 0.2737 0.2536 0.2691 0.0259 0.0386 0.0276 232 PHE A CB 1719 C CG . PHE A 232 ? 0.2821 0.2535 0.2713 0.0272 0.0386 0.0262 232 PHE A CG 1720 C CD1 . PHE A 232 ? 0.2892 0.2555 0.2763 0.0309 0.0405 0.0277 232 PHE A CD1 1721 C CD2 . PHE A 232 ? 0.2936 0.2620 0.2791 0.0246 0.0366 0.0233 232 PHE A CD2 1722 C CE1 . PHE A 232 ? 0.3063 0.2639 0.2873 0.0320 0.0400 0.0260 232 PHE A CE1 1723 C CE2 . PHE A 232 ? 0.2962 0.2565 0.2761 0.0254 0.0361 0.0222 232 PHE A CE2 1724 C CZ . PHE A 232 ? 0.3143 0.2688 0.2918 0.0290 0.0376 0.0234 232 PHE A CZ 1725 N N . SER A 233 ? 0.2490 0.2282 0.2427 0.0249 0.0383 0.0232 233 SER A N 1726 C CA . SER A 233 ? 0.2493 0.2248 0.2396 0.0245 0.0378 0.0205 233 SER A CA 1727 C C . SER A 233 ? 0.2538 0.2289 0.2442 0.0268 0.0398 0.0218 233 SER A C 1728 O O . SER A 233 ? 0.2548 0.2249 0.2404 0.0281 0.0407 0.0205 233 SER A O 1729 C CB . SER A 233 ? 0.2439 0.2233 0.2367 0.0211 0.0350 0.0181 233 SER A CB 1730 O OG . SER A 233 ? 0.2227 0.2035 0.2152 0.0191 0.0334 0.0171 233 SER A OG 1731 N N . TYR A 234 ? 0.2582 0.2390 0.2541 0.0272 0.0403 0.0246 234 TYR A N 1732 C CA . TYR A 234 ? 0.2515 0.2336 0.2485 0.0293 0.0422 0.0269 234 TYR A CA 1733 C C . TYR A 234 ? 0.2640 0.2422 0.2564 0.0335 0.0456 0.0282 234 TYR A C 1734 O O . TYR A 234 ? 0.2754 0.2514 0.2646 0.0354 0.0471 0.0281 234 TYR A O 1735 C CB . TYR A 234 ? 0.2571 0.2465 0.2614 0.0286 0.0418 0.0303 234 TYR A CB 1736 C CG . TYR A 234 ? 0.2807 0.2725 0.2866 0.0311 0.0441 0.0339 234 TYR A CG 1737 C CD1 . TYR A 234 ? 0.2869 0.2790 0.2932 0.0302 0.0434 0.0337 234 TYR A CD1 1738 C CD2 . TYR A 234 ? 0.2949 0.2890 0.3019 0.0343 0.0470 0.0374 234 TYR A CD2 1739 C CE1 . TYR A 234 ? 0.3052 0.3003 0.3127 0.0323 0.0456 0.0374 234 TYR A CE1 1740 C CE2 . TYR A 234 ? 0.3110 0.3083 0.3193 0.0367 0.0493 0.0409 234 TYR A CE2 1741 C CZ . TYR A 234 ? 0.3161 0.3140 0.3245 0.0356 0.0486 0.0409 234 TYR A CZ 1742 O OH . TYR A 234 ? 0.3649 0.3671 0.3750 0.0376 0.0507 0.0448 234 TYR A OH 1743 N N . VAL A 235 ? 0.2571 0.2343 0.2492 0.0352 0.0467 0.0293 235 VAL A N 1744 C CA . VAL A 235 ? 0.2657 0.2392 0.2538 0.0397 0.0496 0.0302 235 VAL A CA 1745 C C . VAL A 235 ? 0.2720 0.2371 0.2521 0.0406 0.0496 0.0266 235 VAL A C 1746 O O . VAL A 235 ? 0.2715 0.2338 0.2473 0.0439 0.0519 0.0265 235 VAL A O 1747 C CB . VAL A 235 ? 0.2741 0.2476 0.2638 0.0412 0.0501 0.0320 235 VAL A CB 1748 C CG1 . VAL A 235 ? 0.2892 0.2574 0.2741 0.0463 0.0529 0.0320 235 VAL A CG1 1749 C CG2 . VAL A 235 ? 0.2654 0.2473 0.2628 0.0407 0.0504 0.0360 235 VAL A CG2 1750 N N . VAL A 236 ? 0.2741 0.2356 0.2521 0.0375 0.0469 0.0238 236 VAL A N 1751 C CA . VAL A 236 ? 0.2848 0.2384 0.2556 0.0374 0.0461 0.0205 236 VAL A CA 1752 C C . VAL A 236 ? 0.2810 0.2345 0.2500 0.0368 0.0462 0.0194 236 VAL A C 1753 O O . VAL A 236 ? 0.2844 0.2329 0.2475 0.0390 0.0474 0.0182 236 VAL A O 1754 C CB . VAL A 236 ? 0.2799 0.2309 0.2497 0.0339 0.0430 0.0186 236 VAL A CB 1755 C CG1 . VAL A 236 ? 0.2849 0.2282 0.2478 0.0332 0.0417 0.0155 236 VAL A CG1 1756 C CG2 . VAL A 236 ? 0.2861 0.2365 0.2572 0.0347 0.0428 0.0202 236 VAL A CG2 1757 N N . GLY A 237 ? 0.2913 0.2506 0.2655 0.0339 0.0448 0.0198 237 GLY A N 1758 C CA . GLY A 237 ? 0.3037 0.2637 0.2775 0.0330 0.0445 0.0193 237 GLY A CA 1759 C C . GLY A 237 ? 0.2971 0.2587 0.2701 0.0364 0.0474 0.0217 237 GLY A C 1760 O O . GLY A 237 ? 0.2903 0.2491 0.2590 0.0369 0.0479 0.0207 237 GLY A O 1761 N N . ARG A 238 ? 0.3160 0.2829 0.2935 0.0383 0.0492 0.0251 238 ARG A N 1762 C CA . ARG A 238 ? 0.3270 0.2970 0.3043 0.0420 0.0525 0.0281 238 ARG A CA 1763 C C . ARG A 238 ? 0.3296 0.2931 0.2987 0.0460 0.0548 0.0263 238 ARG A C 1764 O O . ARG A 238 ? 0.3313 0.2948 0.2969 0.0481 0.0566 0.0267 238 ARG A O 1765 C CB . ARG A 238 ? 0.3445 0.3213 0.3282 0.0434 0.0539 0.0322 238 ARG A CB 1766 C CG . ARG A 238 ? 0.3836 0.3653 0.3682 0.0474 0.0575 0.0361 238 ARG A CG 1767 C CD . ARG A 238 ? 0.4159 0.4058 0.4083 0.0480 0.0583 0.0408 238 ARG A CD 1768 N NE . ARG A 238 ? 0.4531 0.4405 0.4453 0.0493 0.0587 0.0402 238 ARG A NE 1769 C CZ . ARG A 238 ? 0.4928 0.4853 0.4908 0.0499 0.0592 0.0436 238 ARG A CZ 1770 N NH1 . ARG A 238 ? 0.4789 0.4800 0.4842 0.0490 0.0593 0.0482 238 ARG A NH1 1771 N NH2 . ARG A 238 ? 0.5347 0.5236 0.5313 0.0513 0.0593 0.0425 238 ARG A NH2 1772 N N . SER A 239 ? 0.3221 0.2800 0.2880 0.0471 0.0545 0.0244 239 SER A N 1773 C CA . SER A 239 ? 0.3166 0.2669 0.2744 0.0509 0.0560 0.0222 239 SER A CA 1774 C C . SER A 239 ? 0.3263 0.2711 0.2777 0.0496 0.0548 0.0191 239 SER A C 1775 O O . SER A 239 ? 0.3289 0.2721 0.2750 0.0528 0.0570 0.0187 239 SER A O 1776 C CB . SER A 239 ? 0.3150 0.2598 0.2713 0.0515 0.0550 0.0208 239 SER A CB 1777 O OG . SER A 239 ? 0.3037 0.2400 0.2519 0.0549 0.0557 0.0182 239 SER A OG 1778 N N . ALA A 240 ? 0.2977 0.2406 0.2496 0.0449 0.0515 0.0171 240 ALA A N 1779 C CA . ALA A 240 ? 0.3061 0.2441 0.2527 0.0432 0.0500 0.0144 240 ALA A CA 1780 C C . ALA A 240 ? 0.3006 0.2428 0.2475 0.0436 0.0513 0.0159 240 ALA A C 1781 O O . ALA A 240 ? 0.3104 0.2485 0.2508 0.0447 0.0518 0.0143 240 ALA A O 1782 C CB . ALA A 240 ? 0.3005 0.2381 0.2496 0.0381 0.0464 0.0128 240 ALA A CB 1783 N N . LEU A 241 ? 0.2952 0.2457 0.2497 0.0422 0.0515 0.0190 241 LEU A N 1784 C CA . LEU A 241 ? 0.3110 0.2663 0.2668 0.0421 0.0523 0.0212 241 LEU A CA 1785 C C . LEU A 241 ? 0.3534 0.3103 0.3053 0.0471 0.0562 0.0230 241 LEU A C 1786 O O . LEU A 241 ? 0.3599 0.3176 0.3088 0.0475 0.0569 0.0235 241 LEU A O 1787 C CB . LEU A 241 ? 0.2876 0.2509 0.2529 0.0393 0.0509 0.0242 241 LEU A CB 1788 C CG . LEU A 241 ? 0.2858 0.2481 0.2547 0.0347 0.0470 0.0220 241 LEU A CG 1789 C CD1 . LEU A 241 ? 0.2781 0.2481 0.2563 0.0324 0.0455 0.0249 241 LEU A CD1 1790 C CD2 . LEU A 241 ? 0.2854 0.2432 0.2501 0.0326 0.0451 0.0194 241 LEU A CD2 1791 N N . ARG A 242 ? 0.3878 0.3457 0.3400 0.0508 0.0586 0.0241 242 ARG A N 1792 C CA A ARG A 242 ? 0.4044 0.3646 0.3532 0.0563 0.0627 0.0258 242 ARG A CA 1793 C CA B ARG A 242 ? 0.4103 0.3704 0.3590 0.0564 0.0627 0.0257 242 ARG A CA 1794 C C . ARG A 242 ? 0.4167 0.3677 0.3549 0.0599 0.0637 0.0217 242 ARG A C 1795 O O . ARG A 242 ? 0.4167 0.3689 0.3504 0.0642 0.0666 0.0221 242 ARG A O 1796 C CB A ARG A 242 ? 0.4138 0.3790 0.3680 0.0590 0.0647 0.0288 242 ARG A CB 1797 C CB B ARG A 242 ? 0.4258 0.3905 0.3796 0.0592 0.0647 0.0286 242 ARG A CB 1798 C CG A ARG A 242 ? 0.4103 0.3848 0.3749 0.0558 0.0637 0.0332 242 ARG A CG 1799 C CG B ARG A 242 ? 0.4395 0.4154 0.4012 0.0590 0.0662 0.0341 242 ARG A CG 1800 C CD A ARG A 242 ? 0.4213 0.4014 0.3912 0.0586 0.0658 0.0367 242 ARG A CD 1801 C CD B ARG A 242 ? 0.4378 0.4178 0.4075 0.0534 0.0628 0.0358 242 ARG A CD 1802 N NE A ARG A 242 ? 0.4427 0.4321 0.4159 0.0610 0.0687 0.0416 242 ARG A NE 1803 N NE B ARG A 242 ? 0.4460 0.4355 0.4219 0.0527 0.0634 0.0409 242 ARG A NE 1804 C CZ A ARG A 242 ? 0.4427 0.4341 0.4122 0.0667 0.0727 0.0427 242 ARG A CZ 1805 C CZ B ARG A 242 ? 0.4326 0.4242 0.4095 0.0499 0.0619 0.0419 242 ARG A CZ 1806 N NH1 A ARG A 242 ? 0.4421 0.4433 0.4152 0.0685 0.0752 0.0477 242 ARG A NH1 1807 N NH1 B ARG A 242 ? 0.4186 0.4192 0.4018 0.0493 0.0622 0.0471 242 ARG A NH1 1808 N NH2 A ARG A 242 ? 0.4597 0.4435 0.4221 0.0707 0.0740 0.0389 242 ARG A NH2 1809 N NH2 B ARG A 242 ? 0.4167 0.4019 0.3888 0.0476 0.0597 0.0380 242 ARG A NH2 1810 N N . SER A 243 ? 0.4168 0.3590 0.3512 0.0584 0.0611 0.0179 243 SER A N 1811 C CA . SER A 243 ? 0.4310 0.3635 0.3560 0.0620 0.0615 0.0141 243 SER A CA 1812 C C . SER A 243 ? 0.4375 0.3664 0.3542 0.0631 0.0619 0.0119 243 SER A C 1813 O O . SER A 243 ? 0.4275 0.3554 0.3437 0.0588 0.0595 0.0111 243 SER A O 1814 C CB . SER A 243 ? 0.4249 0.3492 0.3485 0.0588 0.0579 0.0111 243 SER A CB 1815 O OG . SER A 243 ? 0.4226 0.3367 0.3371 0.0613 0.0572 0.0074 243 SER A OG 1816 N N . THR A 244 ? 0.4233 0.3494 0.3329 0.0689 0.0647 0.0104 244 THR A N 1817 C CA . THR A 244 ? 0.4402 0.3617 0.3402 0.0704 0.0650 0.0077 244 THR A CA 1818 C C . THR A 244 ? 0.4484 0.3579 0.3415 0.0678 0.0610 0.0031 244 THR A C 1819 O O . THR A 244 ? 0.4570 0.3623 0.3425 0.0679 0.0604 0.0009 244 THR A O 1820 C CB . THR A 244 ? 0.4658 0.3874 0.3591 0.0781 0.0691 0.0069 244 THR A CB 1821 O OG1 . THR A 244 ? 0.4960 0.4103 0.3869 0.0817 0.0689 0.0043 244 THR A OG1 1822 C CG2 . THR A 244 ? 0.4492 0.3839 0.3487 0.0809 0.0732 0.0118 244 THR A CG2 1823 N N . THR A 245 ? 0.4421 0.3462 0.3376 0.0653 0.0582 0.0020 245 THR A N 1824 C CA . THR A 245 ? 0.4434 0.3377 0.3341 0.0617 0.0539 -0.0012 245 THR A CA 1825 C C . THR A 245 ? 0.4384 0.3360 0.3344 0.0551 0.0511 0.0000 245 THR A C 1826 O O . THR A 245 ? 0.4320 0.3230 0.3244 0.0517 0.0477 -0.0022 245 THR A O 1827 C CB . THR A 245 ? 0.4421 0.3291 0.3326 0.0621 0.0518 -0.0027 245 THR A CB 1828 O OG1 . THR A 245 ? 0.4180 0.3116 0.3185 0.0593 0.0515 0.0003 245 THR A OG1 1829 C CG2 . THR A 245 ? 0.4604 0.3422 0.3450 0.0693 0.0542 -0.0045 245 THR A CG2 1830 N N . GLY A 246 ? 0.4278 0.3355 0.3325 0.0532 0.0522 0.0033 246 GLY A N 1831 C CA . GLY A 246 ? 0.4111 0.3218 0.3215 0.0474 0.0494 0.0041 246 GLY A CA 1832 C C . GLY A 246 ? 0.3982 0.3083 0.3138 0.0444 0.0470 0.0040 246 GLY A C 1833 O O . GLY A 246 ? 0.3825 0.2968 0.3039 0.0402 0.0450 0.0048 246 GLY A O 1834 N N . GLN A 247 ? 0.3707 0.2769 0.2851 0.0468 0.0473 0.0035 247 GLN A N 1835 C CA . GLN A 247 ? 0.3549 0.2616 0.2746 0.0442 0.0452 0.0040 247 GLN A CA 1836 C C . GLN A 247 ? 0.3469 0.2585 0.2718 0.0471 0.0476 0.0065 247 GLN A C 1837 O O . GLN A 247 ? 0.3460 0.2581 0.2688 0.0519 0.0507 0.0071 247 GLN A O 1838 C CB . GLN A 247 ? 0.3652 0.2618 0.2790 0.0434 0.0423 0.0015 247 GLN A CB 1839 C CG . GLN A 247 ? 0.3575 0.2484 0.2657 0.0405 0.0395 -0.0007 247 GLN A CG 1840 C CD . GLN A 247 ? 0.3868 0.2683 0.2903 0.0394 0.0362 -0.0025 247 GLN A CD 1841 O OE1 . GLN A 247 ? 0.4179 0.2946 0.3193 0.0426 0.0366 -0.0029 247 GLN A OE1 1842 N NE2 . GLN A 247 ? 0.3651 0.2443 0.2679 0.0348 0.0327 -0.0033 247 GLN A NE2 1843 N N . ALA A 248 ? 0.3126 0.2280 0.2441 0.0444 0.0462 0.0079 248 ALA A N 1844 C CA . ALA A 248 ? 0.3297 0.2494 0.2660 0.0469 0.0481 0.0104 248 ALA A CA 1845 C C . ALA A 248 ? 0.3663 0.2777 0.2971 0.0507 0.0483 0.0090 248 ALA A C 1846 O O . ALA A 248 ? 0.3448 0.2479 0.2701 0.0496 0.0458 0.0065 248 ALA A O 1847 C CB . ALA A 248 ? 0.3280 0.2527 0.2715 0.0432 0.0462 0.0119 248 ALA A CB 1848 N N . ARG A 249 ? 0.4150 0.3293 0.3484 0.0547 0.0509 0.0110 249 ARG A N 1849 C CA . ARG A 249 ? 0.4539 0.3611 0.3831 0.0593 0.0515 0.0100 249 ARG A CA 1850 C C . ARG A 249 ? 0.4257 0.3354 0.3612 0.0592 0.0510 0.0125 249 ARG A C 1851 O O . ARG A 249 ? 0.3857 0.3042 0.3282 0.0592 0.0528 0.0157 249 ARG A O 1852 C CB . ARG A 249 ? 0.5216 0.4302 0.4474 0.0653 0.0556 0.0100 249 ARG A CB 1853 C CG . ARG A 249 ? 0.5666 0.4725 0.4854 0.0657 0.0560 0.0075 249 ARG A CG 1854 C CD . ARG A 249 ? 0.6422 0.5360 0.5525 0.0645 0.0526 0.0034 249 ARG A CD 1855 N NE . ARG A 249 ? 0.6942 0.5784 0.5975 0.0698 0.0528 0.0007 249 ARG A NE 1856 C CZ . ARG A 249 ? 0.7224 0.5981 0.6242 0.0697 0.0497 -0.0005 249 ARG A CZ 1857 N NH1 . ARG A 249 ? 0.7292 0.6052 0.6362 0.0646 0.0465 0.0009 249 ARG A NH1 1858 N NH2 . ARG A 249 ? 0.7915 0.6582 0.6866 0.0751 0.0498 -0.0032 249 ARG A NH2 1859 N N . SER A 250 ? 0.4459 0.3478 0.3789 0.0586 0.0482 0.0112 250 SER A N 1860 C CA . SER A 250 ? 0.4506 0.3535 0.3888 0.0586 0.0473 0.0135 250 SER A CA 1861 C C . SER A 250 ? 0.4495 0.3563 0.3906 0.0641 0.0509 0.0157 250 SER A C 1862 O O . SER A 250 ? 0.4258 0.3377 0.3735 0.0636 0.0510 0.0188 250 SER A O 1863 C CB . SER A 250 ? 0.4774 0.3692 0.4109 0.0584 0.0437 0.0117 250 SER A CB 1864 O OG . SER A 250 ? 0.4936 0.3842 0.4264 0.0526 0.0402 0.0109 250 SER A OG 1865 N N . ALA A 251 ? 0.4545 0.3600 0.3910 0.0693 0.0540 0.0144 251 ALA A N 1866 C CA . ALA A 251 ? 0.4569 0.3673 0.3965 0.0748 0.0577 0.0167 251 ALA A CA 1867 C C . ALA A 251 ? 0.4524 0.3755 0.4003 0.0729 0.0598 0.0208 251 ALA A C 1868 O O . ALA A 251 ? 0.4274 0.3559 0.3800 0.0763 0.0622 0.0238 251 ALA A O 1869 C CB . ALA A 251 ? 0.4797 0.3863 0.4119 0.0810 0.0607 0.0141 251 ALA A CB 1870 N N . ASP A 252 ? 0.4335 0.3614 0.3836 0.0677 0.0586 0.0211 252 ASP A N 1871 C CA . ASP A 252 ? 0.4161 0.3550 0.3731 0.0660 0.0602 0.0246 252 ASP A CA 1872 C C . ASP A 252 ? 0.4145 0.3589 0.3793 0.0617 0.0582 0.0272 252 ASP A C 1873 O O . ASP A 252 ? 0.4185 0.3721 0.3901 0.0605 0.0592 0.0305 252 ASP A O 1874 C CB . ASP A 252 ? 0.4397 0.3802 0.3946 0.0629 0.0598 0.0232 252 ASP A CB 1875 C CG . ASP A 252 ? 0.4470 0.3849 0.3950 0.0672 0.0624 0.0215 252 ASP A CG 1876 O OD1 . ASP A 252 ? 0.4833 0.4210 0.4297 0.0729 0.0652 0.0222 252 ASP A OD1 1877 O OD2 . ASP A 252 ? 0.4081 0.3443 0.3520 0.0654 0.0617 0.0196 252 ASP A OD2 1878 N N . TYR A 253 ? 0.4333 0.3725 0.3974 0.0591 0.0551 0.0259 253 TYR A N 1879 C CA . TYR A 253 ? 0.4389 0.3837 0.4099 0.0547 0.0530 0.0282 253 TYR A CA 1880 C C . TYR A 253 ? 0.4661 0.4057 0.4368 0.0545 0.0508 0.0283 253 TYR A C 1881 O O . TYR A 253 ? 0.4672 0.3974 0.4318 0.0559 0.0496 0.0257 253 TYR A O 1882 C CB . TYR A 253 ? 0.4397 0.3866 0.4113 0.0489 0.0503 0.0266 253 TYR A CB 1883 C CG . TYR A 253 ? 0.4267 0.3650 0.3914 0.0472 0.0480 0.0229 253 TYR A CG 1884 C CD1 . TYR A 253 ? 0.4216 0.3559 0.3855 0.0445 0.0449 0.0222 253 TYR A CD1 1885 C CD2 . TYR A 253 ? 0.4287 0.3636 0.3879 0.0481 0.0488 0.0204 253 TYR A CD2 1886 C CE1 . TYR A 253 ? 0.4195 0.3465 0.3776 0.0427 0.0425 0.0193 253 TYR A CE1 1887 C CE2 . TYR A 253 ? 0.4218 0.3491 0.3750 0.0462 0.0464 0.0172 253 TYR A CE2 1888 C CZ . TYR A 253 ? 0.4206 0.3440 0.3734 0.0435 0.0433 0.0167 253 TYR A CZ 1889 O OH . TYR A 253 ? 0.4459 0.3621 0.3930 0.0414 0.0406 0.0140 253 TYR A OH 1890 N N . GLY A 254 ? 0.4821 0.4280 0.4595 0.0525 0.0501 0.0315 254 GLY A N 1891 C CA . GLY A 254 ? 0.4872 0.4302 0.4662 0.0520 0.0480 0.0328 254 GLY A CA 1892 C C . GLY A 254 ? 0.4746 0.4263 0.4606 0.0476 0.0465 0.0357 254 GLY A C 1893 O O . GLY A 254 ? 0.4304 0.3894 0.4197 0.0449 0.0467 0.0361 254 GLY A O 1894 N N . ILE A 255 ? 0.4616 0.4119 0.4498 0.0471 0.0447 0.0376 255 ILE A N 1895 C CA . ILE A 255 ? 0.4624 0.4202 0.4569 0.0435 0.0430 0.0408 255 ILE A CA 1896 C C . ILE A 255 ? 0.4067 0.3748 0.4074 0.0429 0.0448 0.0433 255 ILE A C 1897 O O . ILE A 255 ? 0.3807 0.3554 0.3845 0.0384 0.0431 0.0438 255 ILE A O 1898 C CB . ILE A 255 ? 0.5335 0.4872 0.5293 0.0455 0.0420 0.0432 255 ILE A CB 1899 C CG1 . ILE A 255 ? 0.5663 0.5144 0.5592 0.0418 0.0381 0.0420 255 ILE A CG1 1900 C CG2 . ILE A 255 ? 0.5339 0.4957 0.5374 0.0453 0.0425 0.0478 255 ILE A CG2 1901 C CD1 . ILE A 255 ? 0.6193 0.5578 0.6100 0.0450 0.0368 0.0425 255 ILE A CD1 1902 N N . THR A 256 ? 0.3890 0.3586 0.3911 0.0474 0.0480 0.0449 256 THR A N 1903 C CA . THR A 256 ? 0.3847 0.3639 0.3929 0.0469 0.0494 0.0478 256 THR A CA 1904 C C . THR A 256 ? 0.3702 0.3531 0.3781 0.0440 0.0491 0.0460 256 THR A C 1905 O O . THR A 256 ? 0.3608 0.3516 0.3741 0.0424 0.0491 0.0482 256 THR A O 1906 C CB . THR A 256 ? 0.4044 0.3856 0.4147 0.0524 0.0530 0.0505 256 THR A CB 1907 O OG1 . THR A 256 ? 0.4388 0.4144 0.4431 0.0562 0.0553 0.0478 256 THR A OG1 1908 C CG2 . THR A 256 ? 0.4293 0.4084 0.4417 0.0555 0.0533 0.0531 256 THR A CG2 1909 N N . ASP A 257 ? 0.3645 0.3419 0.3667 0.0431 0.0484 0.0420 257 ASP A N 1910 C CA . ASP A 257 ? 0.3416 0.3222 0.3438 0.0401 0.0476 0.0400 257 ASP A CA 1911 C C . ASP A 257 ? 0.3132 0.2954 0.3159 0.0349 0.0442 0.0381 257 ASP A C 1912 O O . ASP A 257 ? 0.3182 0.3022 0.3206 0.0324 0.0431 0.0359 257 ASP A O 1913 C CB . ASP A 257 ? 0.3399 0.3141 0.3358 0.0422 0.0489 0.0369 257 ASP A CB 1914 C CG . ASP A 257 ? 0.3507 0.3236 0.3453 0.0476 0.0524 0.0384 257 ASP A CG 1915 O OD1 . ASP A 257 ? 0.3291 0.3090 0.3284 0.0484 0.0540 0.0412 257 ASP A OD1 1916 O OD2 . ASP A 257 ? 0.3558 0.3210 0.3449 0.0511 0.0533 0.0367 257 ASP A OD2 1917 N N . CYS A 258 ? 0.3089 0.2908 0.3122 0.0335 0.0425 0.0391 258 CYS A N 1918 C CA . CYS A 258 ? 0.3022 0.2860 0.3053 0.0289 0.0395 0.0374 258 CYS A CA 1919 C C . CYS A 258 ? 0.2968 0.2901 0.3058 0.0260 0.0384 0.0389 258 CYS A C 1920 O O . CYS A 258 ? 0.3008 0.2982 0.3124 0.0237 0.0367 0.0406 258 CYS A O 1921 C CB . CYS A 258 ? 0.3247 0.3047 0.3262 0.0282 0.0379 0.0382 258 CYS A CB 1922 S SG . CYS A 258 ? 0.3483 0.3164 0.3421 0.0306 0.0381 0.0355 258 CYS A SG 1923 N N . ASN A 259 ? 0.2783 0.2748 0.2890 0.0258 0.0388 0.0382 259 ASN A N 1924 C CA . ASN A 259 ? 0.2791 0.2835 0.2948 0.0231 0.0372 0.0388 259 ASN A CA 1925 C C . ASN A 259 ? 0.2874 0.2923 0.3012 0.0201 0.0350 0.0345 259 ASN A C 1926 O O . ASN A 259 ? 0.2728 0.2746 0.2844 0.0207 0.0355 0.0323 259 ASN A O 1927 C CB . ASN A 259 ? 0.2835 0.2906 0.3030 0.0250 0.0389 0.0412 259 ASN A CB 1928 C CG . ASN A 259 ? 0.2874 0.3017 0.3120 0.0223 0.0369 0.0418 259 ASN A CG 1929 O OD1 . ASN A 259 ? 0.2974 0.3146 0.3223 0.0192 0.0343 0.0398 259 ASN A OD1 1930 N ND2 . ASN A 259 ? 0.2962 0.3136 0.3249 0.0235 0.0378 0.0448 259 ASN A ND2 1931 N N . PRO A 260 ? 0.2788 0.2882 0.2934 0.0169 0.0326 0.0334 260 PRO A N 1932 C CA . PRO A 260 ? 0.2805 0.2904 0.2931 0.0147 0.0308 0.0292 260 PRO A CA 1933 C C . PRO A 260 ? 0.2892 0.3035 0.3052 0.0137 0.0294 0.0278 260 PRO A C 1934 O O . PRO A 260 ? 0.3058 0.3203 0.3205 0.0123 0.0279 0.0243 260 PRO A O 1935 C CB . PRO A 260 ? 0.2727 0.2868 0.2850 0.0120 0.0289 0.0289 260 PRO A CB 1936 C CG . PRO A 260 ? 0.2796 0.2986 0.2960 0.0118 0.0289 0.0328 260 PRO A CG 1937 C CD . PRO A 260 ? 0.2869 0.3015 0.3042 0.0152 0.0315 0.0359 260 PRO A CD 1938 N N . LEU A 261 ? 0.2910 0.3086 0.3116 0.0143 0.0298 0.0308 261 LEU A N 1939 C CA . LEU A 261 ? 0.3060 0.3271 0.3301 0.0130 0.0278 0.0297 261 LEU A CA 1940 C C . LEU A 261 ? 0.2867 0.3036 0.3100 0.0143 0.0284 0.0284 261 LEU A C 1941 O O . LEU A 261 ? 0.2451 0.2572 0.2657 0.0166 0.0309 0.0294 261 LEU A O 1942 C CB . LEU A 261 ? 0.3133 0.3394 0.3428 0.0129 0.0276 0.0338 261 LEU A CB 1943 C CG . LEU A 261 ? 0.3263 0.3576 0.3569 0.0111 0.0264 0.0349 261 LEU A CG 1944 C CD1 . LEU A 261 ? 0.3542 0.3905 0.3904 0.0106 0.0257 0.0389 261 LEU A CD1 1945 C CD2 . LEU A 261 ? 0.3588 0.3933 0.3878 0.0085 0.0236 0.0306 261 LEU A CD2 1946 N N . PRO A 262 ? 0.2727 0.2913 0.2983 0.0128 0.0260 0.0262 262 PRO A N 1947 C CA . PRO A 262 ? 0.2620 0.2769 0.2874 0.0139 0.0264 0.0258 262 PRO A CA 1948 C C . PRO A 262 ? 0.2755 0.2897 0.3026 0.0163 0.0292 0.0306 262 PRO A C 1949 O O . PRO A 262 ? 0.2728 0.2909 0.3036 0.0166 0.0298 0.0346 262 PRO A O 1950 C CB . PRO A 262 ? 0.2687 0.2865 0.2981 0.0119 0.0227 0.0239 262 PRO A CB 1951 C CG . PRO A 262 ? 0.2714 0.2931 0.3006 0.0100 0.0205 0.0210 262 PRO A CG 1952 C CD . PRO A 262 ? 0.2753 0.2990 0.3038 0.0104 0.0226 0.0242 262 PRO A CD 1953 N N . ALA A 263 ? 0.2652 0.2750 0.2895 0.0180 0.0309 0.0304 263 ALA A N 1954 C CA . ALA A 263 ? 0.2765 0.2855 0.3012 0.0208 0.0339 0.0344 263 ALA A CA 1955 C C . ALA A 263 ? 0.2914 0.3062 0.3226 0.0205 0.0335 0.0389 263 ALA A C 1956 O O . ALA A 263 ? 0.2808 0.2983 0.3162 0.0181 0.0302 0.0387 263 ALA A O 1957 C CB . ALA A 263 ? 0.2806 0.2856 0.3023 0.0216 0.0347 0.0331 263 ALA A CB 1958 N N . ASN A 264 ? 0.3051 0.3217 0.3372 0.0229 0.0363 0.0430 264 ASN A N 1959 C CA . ASN A 264 ? 0.3206 0.3434 0.3592 0.0229 0.0362 0.0481 264 ASN A CA 1960 C C . ASN A 264 ? 0.3254 0.3508 0.3682 0.0220 0.0349 0.0505 264 ASN A C 1961 O O . ASN A 264 ? 0.3146 0.3445 0.3631 0.0198 0.0322 0.0528 264 ASN A O 1962 C CB . ASN A 264 ? 0.3256 0.3495 0.3641 0.0266 0.0402 0.0522 264 ASN A CB 1963 C CG . ASN A 264 ? 0.3354 0.3574 0.3713 0.0277 0.0413 0.0514 264 ASN A CG 1964 O OD1 . ASN A 264 ? 0.3586 0.3808 0.3943 0.0251 0.0390 0.0491 264 ASN A OD1 1965 N ND2 . ASN A 264 ? 0.3580 0.3786 0.3922 0.0316 0.0448 0.0536 264 ASN A ND2 1966 N N . ASP A 265 ? 0.3484 0.3708 0.3883 0.0235 0.0364 0.0499 265 ASP A N 1967 C CA . ASP A 265 ? 0.3953 0.4206 0.4393 0.0227 0.0353 0.0530 265 ASP A CA 1968 C C . ASP A 265 ? 0.4081 0.4332 0.4554 0.0187 0.0302 0.0506 265 ASP A C 1969 O O . ASP A 265 ? 0.4244 0.4528 0.4771 0.0172 0.0280 0.0539 265 ASP A O 1970 C CB . ASP A 265 ? 0.4086 0.4309 0.4480 0.0253 0.0383 0.0529 265 ASP A CB 1971 C CG . ASP A 265 ? 0.4439 0.4681 0.4817 0.0296 0.0431 0.0565 265 ASP A CG 1972 O OD1 . ASP A 265 ? 0.4710 0.4905 0.5021 0.0325 0.0461 0.0543 265 ASP A OD1 1973 O OD2 . ASP A 265 ? 0.4557 0.4858 0.4988 0.0301 0.0437 0.0613 265 ASP A OD2 1974 N N . LEU A 266 ? 0.3635 0.3852 0.4080 0.0172 0.0281 0.0451 266 LEU A N 1975 C CA . LEU A 266 ? 0.3405 0.3615 0.3874 0.0141 0.0234 0.0421 266 LEU A CA 1976 C C . LEU A 266 ? 0.3455 0.3712 0.3990 0.0118 0.0199 0.0444 266 LEU A C 1977 O O . LEU A 266 ? 0.3387 0.3678 0.3937 0.0120 0.0207 0.0467 266 LEU A O 1978 C CB . LEU A 266 ? 0.3285 0.3458 0.3706 0.0135 0.0225 0.0357 266 LEU A CB 1979 C CG . LEU A 266 ? 0.3120 0.3240 0.3476 0.0151 0.0249 0.0326 266 LEU A CG 1980 C CD1 . LEU A 266 ? 0.3085 0.3186 0.3404 0.0141 0.0237 0.0274 266 LEU A CD1 1981 C CD2 . LEU A 266 ? 0.3266 0.3359 0.3623 0.0146 0.0237 0.0319 266 LEU A CD2 1982 N N . THR A 267 ? 0.3441 0.3696 0.4017 0.0094 0.0154 0.0437 267 THR A N 1983 C CA . THR A 267 ? 0.3480 0.3772 0.4118 0.0069 0.0112 0.0457 267 THR A CA 1984 C C . THR A 267 ? 0.3568 0.3860 0.4187 0.0058 0.0092 0.0409 267 THR A C 1985 O O . THR A 267 ? 0.3557 0.3820 0.4124 0.0066 0.0103 0.0360 267 THR A O 1986 C CB . THR A 267 ? 0.3303 0.3582 0.3987 0.0046 0.0063 0.0459 267 THR A CB 1987 O OG1 . THR A 267 ? 0.2837 0.3068 0.3490 0.0041 0.0040 0.0390 267 THR A OG1 1988 C CG2 . THR A 267 ? 0.3237 0.3523 0.3936 0.0056 0.0085 0.0509 267 THR A CG2 1989 N N . PRO A 268 ? 0.3911 0.4241 0.4573 0.0040 0.0063 0.0426 268 PRO A N 1990 C CA . PRO A 268 ? 0.3909 0.4247 0.4553 0.0028 0.0041 0.0382 268 PRO A CA 1991 C C . PRO A 268 ? 0.4221 0.4520 0.4838 0.0023 0.0012 0.0310 268 PRO A C 1992 O O . PRO A 268 ? 0.3998 0.4296 0.4569 0.0027 0.0020 0.0262 268 PRO A O 1993 C CB . PRO A 268 ? 0.4054 0.4431 0.4761 0.0004 0.0000 0.0415 268 PRO A CB 1994 C CG . PRO A 268 ? 0.3848 0.4257 0.4593 0.0012 0.0028 0.0492 268 PRO A CG 1995 C CD . PRO A 268 ? 0.3818 0.4194 0.4545 0.0029 0.0054 0.0496 268 PRO A CD 1996 N N . GLU A 269 ? 0.4021 0.4292 0.4667 0.0014 -0.0020 0.0304 269 GLU A N 1997 C CA . GLU A 269 ? 0.4095 0.4328 0.4719 0.0012 -0.0048 0.0235 269 GLU A CA 1998 C C . GLU A 269 ? 0.3486 0.3687 0.4055 0.0031 -0.0014 0.0205 269 GLU A C 1999 O O . GLU A 269 ? 0.3236 0.3425 0.3771 0.0034 -0.0024 0.0146 269 GLU A O 2000 C CB . GLU A 269 ? 0.4442 0.4649 0.5116 -0.0002 -0.0100 0.0235 269 GLU A CB 2001 C CG . GLU A 269 ? 0.4971 0.5195 0.5689 -0.0024 -0.0155 0.0232 269 GLU A CG 2002 C CD . GLU A 269 ? 0.5351 0.5609 0.6040 -0.0025 -0.0156 0.0198 269 GLU A CD 2003 O OE1 . GLU A 269 ? 0.5030 0.5283 0.5675 -0.0016 -0.0160 0.0132 269 GLU A OE1 2004 O OE2 . GLU A 269 ? 0.5525 0.5821 0.6242 -0.0036 -0.0157 0.0244 269 GLU A OE2 2005 N N . GLN A 270 ? 0.3149 0.3340 0.3708 0.0043 0.0024 0.0245 270 GLN A N 2006 C CA . GLN A 270 ? 0.2992 0.3151 0.3494 0.0061 0.0058 0.0220 270 GLN A CA 2007 C C . GLN A 270 ? 0.2941 0.3114 0.3396 0.0069 0.0085 0.0200 270 GLN A C 2008 O O . GLN A 270 ? 0.2651 0.2803 0.3061 0.0075 0.0095 0.0160 270 GLN A O 2009 C CB . GLN A 270 ? 0.2903 0.3049 0.3399 0.0074 0.0093 0.0266 270 GLN A CB 2010 C CG . GLN A 270 ? 0.2874 0.3003 0.3410 0.0064 0.0066 0.0281 270 GLN A CG 2011 C CD . GLN A 270 ? 0.2935 0.3077 0.3482 0.0075 0.0097 0.0344 270 GLN A CD 2012 O OE1 . GLN A 270 ? 0.2728 0.2892 0.3257 0.0092 0.0138 0.0377 270 GLN A OE1 2013 N NE2 . GLN A 270 ? 0.2799 0.2929 0.3375 0.0066 0.0077 0.0362 270 GLN A NE2 2014 N N . LYS A 271 ? 0.3239 0.3450 0.3706 0.0068 0.0096 0.0231 271 LYS A N 2015 C CA . LYS A 271 ? 0.3313 0.3541 0.3740 0.0074 0.0121 0.0221 271 LYS A CA 2016 C C . LYS A 271 ? 0.3311 0.3559 0.3724 0.0061 0.0091 0.0166 271 LYS A C 2017 O O . LYS A 271 ? 0.3107 0.3357 0.3476 0.0065 0.0106 0.0137 271 LYS A O 2018 C CB . LYS A 271 ? 0.3364 0.3630 0.3815 0.0076 0.0138 0.0274 271 LYS A CB 2019 C CG . LYS A 271 ? 0.3424 0.3680 0.3874 0.0098 0.0179 0.0324 271 LYS A CG 2020 C CD . LYS A 271 ? 0.3498 0.3793 0.3962 0.0102 0.0195 0.0363 271 LYS A CD 2021 C CE . LYS A 271 ? 0.3878 0.4171 0.4338 0.0129 0.0239 0.0410 271 LYS A CE 2022 N NZ . LYS A 271 ? 0.4214 0.4531 0.4724 0.0134 0.0241 0.0461 271 LYS A NZ 2023 N N . VAL A 272 ? 0.3181 0.3443 0.3632 0.0047 0.0048 0.0150 272 VAL A N 2024 C CA . VAL A 272 ? 0.3215 0.3497 0.3655 0.0039 0.0018 0.0095 272 VAL A CA 2025 C C . VAL A 272 ? 0.2953 0.3201 0.3362 0.0048 0.0015 0.0044 272 VAL A C 2026 O O . VAL A 272 ? 0.3154 0.3420 0.3526 0.0051 0.0020 0.0006 272 VAL A O 2027 C CB . VAL A 272 ? 0.3441 0.3737 0.3930 0.0023 -0.0033 0.0089 272 VAL A CB 2028 C CG1 . VAL A 272 ? 0.3479 0.3787 0.3951 0.0021 -0.0068 0.0020 272 VAL A CG1 2029 C CG2 . VAL A 272 ? 0.3477 0.3815 0.3993 0.0012 -0.0032 0.0137 272 VAL A CG2 2030 N N . ALA A 273 ? 0.2756 0.2961 0.3183 0.0051 0.0007 0.0048 273 ALA A N 2031 C CA . ALA A 273 ? 0.2640 0.2811 0.3043 0.0059 0.0004 0.0005 273 ALA A CA 2032 C C . ALA A 273 ? 0.2576 0.2738 0.2925 0.0069 0.0048 0.0007 273 ALA A C 2033 O O . ALA A 273 ? 0.2457 0.2617 0.2774 0.0074 0.0048 -0.0034 273 ALA A O 2034 C CB . ALA A 273 ? 0.2784 0.2911 0.3219 0.0057 -0.0012 0.0019 273 ALA A CB 2035 N N . ALA A 274 ? 0.2449 0.2604 0.2787 0.0075 0.0084 0.0056 274 ALA A N 2036 C CA . ALA A 274 ? 0.2483 0.2621 0.2770 0.0084 0.0121 0.0059 274 ALA A CA 2037 C C . ALA A 274 ? 0.2520 0.2696 0.2779 0.0080 0.0123 0.0035 274 ALA A C 2038 O O . ALA A 274 ? 0.2417 0.2583 0.2636 0.0082 0.0134 0.0013 274 ALA A O 2039 C CB . ALA A 274 ? 0.2450 0.2573 0.2731 0.0095 0.0156 0.0112 274 ALA A CB 2040 N N . ALA A 275 ? 0.2639 0.2863 0.2919 0.0072 0.0113 0.0045 275 ALA A N 2041 C CA . ALA A 275 ? 0.2662 0.2933 0.2917 0.0065 0.0116 0.0031 275 ALA A CA 2042 C C . ALA A 275 ? 0.2771 0.3068 0.3014 0.0063 0.0091 -0.0028 275 ALA A C 2043 O O . ALA A 275 ? 0.2714 0.3043 0.2926 0.0060 0.0099 -0.0042 275 ALA A O 2044 C CB . ALA A 275 ? 0.2724 0.3044 0.3006 0.0056 0.0108 0.0056 275 ALA A CB 2045 N N . ALA A 276 ? 0.2679 0.2962 0.2948 0.0064 0.0060 -0.0059 276 ALA A N 2046 C CA . ALA A 276 ? 0.2700 0.3002 0.2962 0.0068 0.0034 -0.0118 276 ALA A CA 2047 C C . ALA A 276 ? 0.2588 0.2849 0.2832 0.0077 0.0040 -0.0141 276 ALA A C 2048 O O . ALA A 276 ? 0.2405 0.2681 0.2645 0.0084 0.0021 -0.0191 276 ALA A O 2049 C CB . ALA A 276 ? 0.2673 0.2975 0.2976 0.0066 -0.0006 -0.0139 276 ALA A CB 2050 N N . LEU A 277 ? 0.2680 0.2894 0.2911 0.0079 0.0067 -0.0107 277 LEU A N 2051 C CA . LEU A 277 ? 0.2766 0.2933 0.2983 0.0085 0.0070 -0.0121 277 LEU A CA 2052 C C . LEU A 277 ? 0.2653 0.2844 0.2843 0.0089 0.0067 -0.0164 277 LEU A C 2053 O O . LEU A 277 ? 0.2585 0.2754 0.2781 0.0094 0.0053 -0.0191 277 LEU A O 2054 C CB . LEU A 277 ? 0.2848 0.2969 0.3040 0.0087 0.0104 -0.0078 277 LEU A CB 2055 C CG . LEU A 277 ? 0.2911 0.2977 0.3095 0.0092 0.0107 -0.0079 277 LEU A CG 2056 C CD1 . LEU A 277 ? 0.2949 0.2994 0.3181 0.0091 0.0082 -0.0074 277 LEU A CD1 2057 C CD2 . LEU A 277 ? 0.2869 0.2898 0.3016 0.0096 0.0143 -0.0040 277 LEU A CD2 2058 N N . LEU A 278 ? 0.2694 0.2934 0.2856 0.0084 0.0080 -0.0164 278 LEU A N 2059 C CA . LEU A 278 ? 0.2756 0.3031 0.2894 0.0086 0.0079 -0.0198 278 LEU A CA 2060 C C . LEU A 278 ? 0.2587 0.2909 0.2745 0.0096 0.0049 -0.0253 278 LEU A C 2061 O O . LEU A 278 ? 0.2564 0.2901 0.2714 0.0105 0.0043 -0.0287 278 LEU A O 2062 C CB . LEU A 278 ? 0.2964 0.3291 0.3073 0.0077 0.0098 -0.0179 278 LEU A CB 2063 C CG . LEU A 278 ? 0.3208 0.3493 0.3288 0.0069 0.0125 -0.0134 278 LEU A CG 2064 C CD1 . LEU A 278 ? 0.3192 0.3538 0.3247 0.0057 0.0133 -0.0125 278 LEU A CD1 2065 C CD2 . LEU A 278 ? 0.3226 0.3447 0.3288 0.0072 0.0132 -0.0135 278 LEU A CD2 2066 N N . ALA A 279 ? 0.2486 0.2828 0.2669 0.0097 0.0029 -0.0263 279 ALA A N 2067 C CA . ALA A 279 ? 0.2480 0.2866 0.2676 0.0110 -0.0002 -0.0321 279 ALA A CA 2068 C C . ALA A 279 ? 0.2524 0.2864 0.2744 0.0124 -0.0026 -0.0357 279 ALA A C 2069 O O . ALA A 279 ? 0.2609 0.2982 0.2821 0.0139 -0.0034 -0.0401 279 ALA A O 2070 C CB . ALA A 279 ? 0.2502 0.2911 0.2719 0.0106 -0.0024 -0.0324 279 ALA A CB 2071 N N . PRO A 280 ? 0.2477 0.2746 0.2728 0.0120 -0.0038 -0.0336 280 PRO A N 2072 C CA . PRO A 280 ? 0.2493 0.2719 0.2770 0.0132 -0.0065 -0.0368 280 PRO A CA 2073 C C . PRO A 280 ? 0.2517 0.2731 0.2771 0.0136 -0.0046 -0.0371 280 PRO A C 2074 O O . PRO A 280 ? 0.2472 0.2682 0.2740 0.0151 -0.0066 -0.0411 280 PRO A O 2075 C CB . PRO A 280 ? 0.2632 0.2792 0.2946 0.0122 -0.0079 -0.0332 280 PRO A CB 2076 C CG . PRO A 280 ? 0.2681 0.2852 0.2990 0.0108 -0.0059 -0.0285 280 PRO A CG 2077 C CD . PRO A 280 ? 0.2630 0.2864 0.2899 0.0107 -0.0033 -0.0286 280 PRO A CD 2078 N N . ALA A 281 ? 0.2376 0.2580 0.2598 0.0124 -0.0010 -0.0328 281 ALA A N 2079 C CA . ALA A 281 ? 0.2525 0.2713 0.2723 0.0124 0.0006 -0.0325 281 ALA A CA 2080 C C . ALA A 281 ? 0.2637 0.2899 0.2816 0.0134 0.0007 -0.0363 281 ALA A C 2081 O O . ALA A 281 ? 0.2720 0.2983 0.2904 0.0143 -0.0001 -0.0389 281 ALA A O 2082 C CB . ALA A 281 ? 0.2323 0.2480 0.2486 0.0110 0.0040 -0.0273 281 ALA A CB 2083 N N . ALA A 282 ? 0.2898 0.3228 0.3059 0.0130 0.0017 -0.0362 282 ALA A N 2084 C CA . ALA A 282 ? 0.3130 0.3547 0.3277 0.0140 0.0016 -0.0398 282 ALA A CA 2085 C C . ALA A 282 ? 0.3447 0.3883 0.3624 0.0166 -0.0016 -0.0461 282 ALA A C 2086 O O . ALA A 282 ? 0.3955 0.4420 0.4133 0.0181 -0.0020 -0.0491 282 ALA A O 2087 C CB . ALA A 282 ? 0.3353 0.3842 0.3481 0.0131 0.0028 -0.0384 282 ALA A CB 2088 N N . ALA A 283 ? 0.3582 0.3990 0.3786 0.0173 -0.0043 -0.0479 283 ALA A N 2089 C CA . ALA A 283 ? 0.3788 0.4196 0.4022 0.0198 -0.0079 -0.0539 283 ALA A CA 2090 C C . ALA A 283 ? 0.3989 0.4341 0.4247 0.0208 -0.0093 -0.0551 283 ALA A C 2091 O O . ALA A 283 ? 0.4123 0.4496 0.4398 0.0233 -0.0115 -0.0604 283 ALA A O 2092 C CB . ALA A 283 ? 0.3882 0.4255 0.4145 0.0198 -0.0111 -0.0548 283 ALA A CB 2093 N N . ALA A 284 ? 0.3704 0.3984 0.3967 0.0189 -0.0082 -0.0505 284 ALA A N 2094 C CA . ALA A 284 ? 0.3472 0.3698 0.3758 0.0195 -0.0095 -0.0510 284 ALA A CA 2095 C C . ALA A 284 ? 0.3412 0.3680 0.3674 0.0200 -0.0075 -0.0517 284 ALA A C 2096 O O . ALA A 284 ? 0.3442 0.3706 0.3726 0.0218 -0.0094 -0.0550 284 ALA A O 2097 C CB . ALA A 284 ? 0.3470 0.3616 0.3762 0.0173 -0.0087 -0.0456 284 ALA A CB 2098 N N . ILE A 285 ? 0.3140 0.3449 0.3360 0.0185 -0.0041 -0.0486 285 ILE A N 2099 C CA . ILE A 285 ? 0.3382 0.3741 0.3577 0.0184 -0.0022 -0.0484 285 ILE A CA 2100 C C . ILE A 285 ? 0.3740 0.4183 0.3948 0.0213 -0.0036 -0.0541 285 ILE A C 2101 O O . ILE A 285 ? 0.3912 0.4358 0.4138 0.0229 -0.0047 -0.0565 285 ILE A O 2102 C CB . ILE A 285 ? 0.3211 0.3597 0.3363 0.0161 0.0010 -0.0437 285 ILE A CB 2103 C CG1 . ILE A 285 ? 0.3167 0.3464 0.3304 0.0139 0.0025 -0.0386 285 ILE A CG1 2104 C CG2 . ILE A 285 ? 0.3457 0.3909 0.3586 0.0157 0.0025 -0.0432 285 ILE A CG2 2105 C CD1 . ILE A 285 ? 0.3209 0.3510 0.3311 0.0119 0.0050 -0.0342 285 ILE A CD1 2106 N N . VAL A 286 ? 0.3734 0.4244 0.3933 0.0222 -0.0037 -0.0563 286 VAL A N 2107 C CA . VAL A 286 ? 0.3535 0.4126 0.3744 0.0255 -0.0054 -0.0624 286 VAL A CA 2108 C C . VAL A 286 ? 0.3293 0.3843 0.3544 0.0285 -0.0090 -0.0677 286 VAL A C 2109 O O . VAL A 286 ? 0.3473 0.4082 0.3732 0.0314 -0.0096 -0.0720 286 VAL A O 2110 C CB . VAL A 286 ? 0.3799 0.4439 0.3991 0.0253 -0.0053 -0.0630 286 VAL A CB 2111 C CG1 . VAL A 286 ? 0.3930 0.4602 0.4138 0.0285 -0.0085 -0.0697 286 VAL A CG1 2112 C CG2 . VAL A 286 ? 0.3578 0.4303 0.3733 0.0234 -0.0020 -0.0594 286 VAL A CG2 2113 N N . ALA A 287 ? 0.3117 0.3570 0.3398 0.0280 -0.0115 -0.0673 287 ALA A N 2114 C CA . ALA A 287 ? 0.3308 0.3719 0.3634 0.0308 -0.0155 -0.0722 287 ALA A CA 2115 C C . ALA A 287 ? 0.3213 0.3577 0.3560 0.0307 -0.0157 -0.0708 287 ALA A C 2116 O O . ALA A 287 ? 0.3269 0.3605 0.3655 0.0330 -0.0190 -0.0746 287 ALA A O 2117 C CB . ALA A 287 ? 0.3409 0.3742 0.3764 0.0302 -0.0189 -0.0723 287 ALA A CB 2118 N N . GLY A 288 ? 0.2953 0.3307 0.3275 0.0279 -0.0125 -0.0654 288 GLY A N 2119 C CA . GLY A 288 ? 0.2959 0.3250 0.3298 0.0270 -0.0129 -0.0629 288 GLY A CA 2120 C C . GLY A 288 ? 0.2807 0.3156 0.3144 0.0284 -0.0120 -0.0645 288 GLY A C 2121 O O . GLY A 288 ? 0.2813 0.3253 0.3143 0.0307 -0.0114 -0.0679 288 GLY A O 2122 N N . PRO A 289 ? 0.2870 0.3175 0.3213 0.0270 -0.0117 -0.0615 289 PRO A N 2123 C CA . PRO A 289 ? 0.2921 0.3280 0.3268 0.0282 -0.0111 -0.0623 289 PRO A CA 2124 C C . PRO A 289 ? 0.2838 0.3279 0.3138 0.0268 -0.0076 -0.0599 289 PRO A C 2125 O O . PRO A 289 ? 0.2713 0.3140 0.2977 0.0240 -0.0055 -0.0560 289 PRO A O 2126 C CB . PRO A 289 ? 0.3034 0.3314 0.3391 0.0260 -0.0116 -0.0585 289 PRO A CB 2127 C CG . PRO A 289 ? 0.3246 0.3449 0.3582 0.0230 -0.0108 -0.0543 289 PRO A CG 2128 C CD . PRO A 289 ? 0.3044 0.3255 0.3384 0.0240 -0.0115 -0.0565 289 PRO A CD 2129 N N . LYS A 290 ? 0.2658 0.3190 0.2964 0.0287 -0.0071 -0.0620 290 LYS A N 2130 C CA . LYS A 290 ? 0.2740 0.3360 0.3011 0.0273 -0.0042 -0.0593 290 LYS A CA 2131 C C . LYS A 290 ? 0.2655 0.3325 0.2940 0.0280 -0.0041 -0.0590 290 LYS A C 2132 O O . LYS A 290 ? 0.2564 0.3242 0.2890 0.0313 -0.0062 -0.0631 290 LYS A O 2133 C CB . LYS A 290 ? 0.3042 0.3763 0.3304 0.0296 -0.0037 -0.0629 290 LYS A CB 2134 C CG . LYS A 290 ? 0.3383 0.4071 0.3632 0.0291 -0.0039 -0.0634 290 LYS A CG 2135 C CD . LYS A 290 ? 0.3741 0.4532 0.3989 0.0324 -0.0043 -0.0686 290 LYS A CD 2136 C CE . LYS A 290 ? 0.3917 0.4694 0.4146 0.0313 -0.0042 -0.0684 290 LYS A CE 2137 N NZ . LYS A 290 ? 0.3994 0.4703 0.4251 0.0334 -0.0075 -0.0727 290 LYS A NZ 2138 N N . GLN A 291 ? 0.2448 0.3148 0.2703 0.0249 -0.0020 -0.0539 291 GLN A N 2139 C CA . GLN A 291 ? 0.2451 0.3204 0.2720 0.0250 -0.0020 -0.0527 291 GLN A CA 2140 C C . GLN A 291 ? 0.2319 0.3162 0.2557 0.0225 0.0001 -0.0484 291 GLN A C 2141 O O . GLN A 291 ? 0.2073 0.2929 0.2276 0.0204 0.0016 -0.0460 291 GLN A O 2142 C CB . GLN A 291 ? 0.2453 0.3104 0.2733 0.0232 -0.0033 -0.0502 291 GLN A CB 2143 C CG . GLN A 291 ? 0.2409 0.2963 0.2645 0.0187 -0.0023 -0.0449 291 GLN A CG 2144 C CD . GLN A 291 ? 0.2499 0.2956 0.2746 0.0174 -0.0037 -0.0431 291 GLN A CD 2145 O OE1 . GLN A 291 ? 0.2622 0.3030 0.2907 0.0194 -0.0058 -0.0461 291 GLN A OE1 2146 N NE2 . GLN A 291 ? 0.2377 0.2811 0.2595 0.0141 -0.0031 -0.0384 291 GLN A NE2 2147 N N . ASN A 292 ? 0.2263 0.3174 0.2519 0.0228 0.0001 -0.0473 292 ASN A N 2148 C CA . ASN A 292 ? 0.2226 0.3244 0.2462 0.0207 0.0017 -0.0433 292 ASN A CA 2149 C C . ASN A 292 ? 0.2147 0.3116 0.2358 0.0158 0.0018 -0.0367 292 ASN A C 2150 O O . ASN A 292 ? 0.2088 0.3145 0.2291 0.0138 0.0026 -0.0329 292 ASN A O 2151 C CB . ASN A 292 ? 0.2361 0.3523 0.2632 0.0245 0.0019 -0.0463 292 ASN A CB 2152 C CG . ASN A 292 ? 0.2513 0.3669 0.2819 0.0253 0.0006 -0.0460 292 ASN A CG 2153 O OD1 . ASN A 292 ? 0.2645 0.3690 0.2949 0.0229 -0.0004 -0.0436 292 ASN A OD1 2154 N ND2 . ASN A 292 ? 0.2599 0.3882 0.2938 0.0289 0.0009 -0.0485 292 ASN A ND2 2155 N N . CYS A 293 ? 0.2030 0.2859 0.2224 0.0137 0.0010 -0.0351 293 CYS A N 2156 C CA . CYS A 293 ? 0.2189 0.2956 0.2357 0.0095 0.0007 -0.0297 293 CYS A CA 2157 C C . CYS A 293 ? 0.2161 0.2780 0.2299 0.0077 0.0004 -0.0287 293 CYS A C 2158 O O . CYS A 293 ? 0.2294 0.2859 0.2450 0.0100 0.0000 -0.0323 293 CYS A O 2159 C CB . CYS A 293 ? 0.2186 0.2971 0.2385 0.0098 -0.0006 -0.0291 293 CYS A CB 2160 S SG . CYS A 293 ? 0.2401 0.3131 0.2651 0.0140 -0.0024 -0.0349 293 CYS A SG 2161 N N . GLU A 294 ? 0.2123 0.2681 0.2218 0.0037 0.0005 -0.0238 294 GLU A N 2162 C CA . GLU A 294 ? 0.2065 0.2489 0.2127 0.0021 0.0004 -0.0226 294 GLU A CA 2163 C C . GLU A 294 ? 0.2207 0.2566 0.2287 0.0024 -0.0010 -0.0231 294 GLU A C 2164 O O . GLU A 294 ? 0.2185 0.2566 0.2272 0.0011 -0.0022 -0.0212 294 GLU A O 2165 C CB . GLU A 294 ? 0.2112 0.2490 0.2120 -0.0018 0.0007 -0.0175 294 GLU A CB 2166 C CG . GLU A 294 ? 0.2093 0.2341 0.2061 -0.0029 0.0011 -0.0165 294 GLU A CG 2167 C CD . GLU A 294 ? 0.2111 0.2301 0.2024 -0.0064 0.0010 -0.0121 294 GLU A CD 2168 O OE1 . GLU A 294 ? 0.2086 0.2340 0.1992 -0.0082 0.0008 -0.0095 294 GLU A OE1 2169 O OE2 . GLU A 294 ? 0.2035 0.2115 0.1909 -0.0074 0.0010 -0.0110 294 GLU A OE2 2170 N N . PRO A 295 ? 0.2297 0.2575 0.2384 0.0036 -0.0014 -0.0252 295 PRO A N 2171 C CA . PRO A 295 ? 0.2231 0.2438 0.2330 0.0033 -0.0029 -0.0250 295 PRO A CA 2172 C C . PRO A 295 ? 0.2180 0.2339 0.2237 -0.0002 -0.0034 -0.0205 295 PRO A C 2173 O O . PRO A 295 ? 0.2217 0.2342 0.2221 -0.0027 -0.0024 -0.0176 295 PRO A O 2174 C CB . PRO A 295 ? 0.2292 0.2411 0.2381 0.0038 -0.0026 -0.0257 295 PRO A CB 2175 C CG . PRO A 295 ? 0.2344 0.2510 0.2443 0.0058 -0.0015 -0.0282 295 PRO A CG 2176 C CD . PRO A 295 ? 0.2345 0.2586 0.2422 0.0047 -0.0003 -0.0266 295 PRO A CD 2177 N N . ASP A 296 ? 0.2210 0.2359 0.2290 -0.0005 -0.0051 -0.0201 296 ASP A N 2178 C CA . ASP A 296 ? 0.2185 0.2280 0.2226 -0.0040 -0.0061 -0.0162 296 ASP A CA 2179 C C . ASP A 296 ? 0.2154 0.2137 0.2139 -0.0058 -0.0055 -0.0144 296 ASP A C 2180 O O . ASP A 296 ? 0.2178 0.2115 0.2170 -0.0042 -0.0050 -0.0162 296 ASP A O 2181 C CB . ASP A 296 ? 0.2255 0.2354 0.2337 -0.0038 -0.0082 -0.0162 296 ASP A CB 2182 C CG . ASP A 296 ? 0.2208 0.2421 0.2339 -0.0023 -0.0087 -0.0171 296 ASP A CG 2183 O OD1 . ASP A 296 ? 0.2230 0.2520 0.2354 -0.0025 -0.0076 -0.0165 296 ASP A OD1 2184 O OD2 . ASP A 296 ? 0.2313 0.2544 0.2491 -0.0010 -0.0102 -0.0182 296 ASP A OD2 2185 N N . LEU A 297 ? 0.2210 0.2150 0.2138 -0.0090 -0.0058 -0.0109 297 LEU A N 2186 C CA . LEU A 297 ? 0.2359 0.2191 0.2230 -0.0105 -0.0057 -0.0093 297 LEU A CA 2187 C C . LEU A 297 ? 0.2541 0.2328 0.2426 -0.0109 -0.0073 -0.0091 297 LEU A C 2188 O O . LEU A 297 ? 0.2712 0.2538 0.2631 -0.0115 -0.0091 -0.0086 297 LEU A O 2189 C CB . LEU A 297 ? 0.2345 0.2135 0.2151 -0.0137 -0.0061 -0.0060 297 LEU A CB 2190 C CG . LEU A 297 ? 0.2275 0.2091 0.2061 -0.0139 -0.0047 -0.0055 297 LEU A CG 2191 C CD1 . LEU A 297 ? 0.2356 0.2135 0.2088 -0.0174 -0.0061 -0.0019 297 LEU A CD1 2192 C CD2 . LEU A 297 ? 0.2337 0.2097 0.2097 -0.0122 -0.0027 -0.0067 297 LEU A CD2 2193 N N . MET A 298 ? 0.2626 0.2337 0.2486 -0.0105 -0.0067 -0.0092 298 MET A N 2194 C CA . MET A 298 ? 0.2863 0.2525 0.2725 -0.0112 -0.0082 -0.0084 298 MET A CA 2195 C C . MET A 298 ? 0.2866 0.2478 0.2666 -0.0145 -0.0093 -0.0054 298 MET A C 2196 O O . MET A 298 ? 0.2757 0.2350 0.2505 -0.0159 -0.0087 -0.0042 298 MET A O 2197 C CB . MET A 298 ? 0.3129 0.2739 0.2986 -0.0099 -0.0071 -0.0090 298 MET A CB 2198 C CG . MET A 298 ? 0.3443 0.3104 0.3378 -0.0070 -0.0074 -0.0118 298 MET A CG 2199 S SD . MET A 298 ? 0.4233 0.3840 0.4173 -0.0061 -0.0069 -0.0116 298 MET A SD 2200 C CE . MET A 298 ? 0.3759 0.3428 0.3777 -0.0028 -0.0071 -0.0153 298 MET A CE 2201 N N . PRO A 299 ? 0.2891 0.2487 0.2702 -0.0159 -0.0114 -0.0041 299 PRO A N 2202 C CA . PRO A 299 ? 0.2952 0.2510 0.2711 -0.0193 -0.0132 -0.0012 299 PRO A CA 2203 C C . PRO A 299 ? 0.2897 0.2368 0.2562 -0.0209 -0.0125 0.0000 299 PRO A C 2204 O O . PRO A 299 ? 0.3131 0.2585 0.2752 -0.0233 -0.0136 0.0018 299 PRO A O 2205 C CB . PRO A 299 ? 0.3021 0.2562 0.2806 -0.0200 -0.0152 -0.0004 299 PRO A CB 2206 C CG . PRO A 299 ? 0.2975 0.2584 0.2851 -0.0171 -0.0152 -0.0028 299 PRO A CG 2207 C CD . PRO A 299 ? 0.2978 0.2596 0.2858 -0.0145 -0.0128 -0.0052 299 PRO A CD 2208 N N . TYR A 300 ? 0.2824 0.2244 0.2461 -0.0194 -0.0107 -0.0008 300 TYR A N 2209 C CA . TYR A 300 ? 0.2840 0.2177 0.2386 -0.0200 -0.0097 -0.0001 300 TYR A CA 2210 C C . TYR A 300 ? 0.2890 0.2227 0.2405 -0.0202 -0.0087 -0.0001 300 TYR A C 2211 O O . TYR A 300 ? 0.2838 0.2104 0.2277 -0.0213 -0.0090 0.0007 300 TYR A O 2212 C CB . TYR A 300 ? 0.2637 0.1938 0.2170 -0.0179 -0.0076 -0.0009 300 TYR A CB 2213 C CG . TYR A 300 ? 0.2485 0.1832 0.2070 -0.0149 -0.0053 -0.0028 300 TYR A CG 2214 C CD1 . TYR A 300 ? 0.2521 0.1859 0.2076 -0.0137 -0.0033 -0.0035 300 TYR A CD1 2215 C CD2 . TYR A 300 ? 0.2388 0.1781 0.2048 -0.0133 -0.0056 -0.0038 300 TYR A CD2 2216 C CE1 . TYR A 300 ? 0.2453 0.1831 0.2051 -0.0112 -0.0014 -0.0049 300 TYR A CE1 2217 C CE2 . TYR A 300 ? 0.2389 0.1817 0.2092 -0.0108 -0.0039 -0.0055 300 TYR A CE2 2218 C CZ . TYR A 300 ? 0.2413 0.1835 0.2084 -0.0098 -0.0017 -0.0060 300 TYR A CZ 2219 O OH . TYR A 300 ? 0.2443 0.1902 0.2156 -0.0075 -0.0002 -0.0075 300 TYR A OH 2220 N N . ALA A 301 ? 0.2793 0.2209 0.2367 -0.0189 -0.0079 -0.0012 301 ALA A N 2221 C CA . ALA A 301 ? 0.2775 0.2199 0.2326 -0.0190 -0.0070 -0.0010 301 ALA A CA 2222 C C . ALA A 301 ? 0.2897 0.2370 0.2461 -0.0215 -0.0091 0.0008 301 ALA A C 2223 O O . ALA A 301 ? 0.2764 0.2231 0.2299 -0.0225 -0.0091 0.0020 301 ALA A O 2224 C CB . ALA A 301 ? 0.2682 0.2161 0.2282 -0.0159 -0.0045 -0.0032 301 ALA A CB 2225 N N . ARG A 302 ? 0.2922 0.2448 0.2531 -0.0225 -0.0108 0.0015 302 ARG A N 2226 C CA . ARG A 302 ? 0.2897 0.2493 0.2531 -0.0247 -0.0126 0.0036 302 ARG A CA 2227 C C . ARG A 302 ? 0.2991 0.2529 0.2561 -0.0283 -0.0148 0.0067 302 ARG A C 2228 O O . ARG A 302 ? 0.2797 0.2384 0.2375 -0.0296 -0.0154 0.0084 302 ARG A O 2229 C CB . ARG A 302 ? 0.3024 0.2678 0.2716 -0.0250 -0.0142 0.0038 302 ARG A CB 2230 C CG . ARG A 302 ? 0.2961 0.2694 0.2730 -0.0213 -0.0127 0.0007 302 ARG A CG 2231 C CD . ARG A 302 ? 0.3232 0.3021 0.3064 -0.0210 -0.0144 0.0007 302 ARG A CD 2232 N NE . ARG A 302 ? 0.3355 0.3179 0.3247 -0.0172 -0.0131 -0.0028 302 ARG A NE 2233 C CZ . ARG A 302 ? 0.3554 0.3398 0.3503 -0.0156 -0.0141 -0.0042 302 ARG A CZ 2234 N NH1 . ARG A 302 ? 0.3679 0.3524 0.3641 -0.0174 -0.0164 -0.0021 302 ARG A NH1 2235 N NH2 . ARG A 302 ? 0.3509 0.3368 0.3503 -0.0122 -0.0132 -0.0076 302 ARG A NH2 2236 N N . PRO A 303 ? 0.3000 0.2432 0.2500 -0.0300 -0.0163 0.0075 303 PRO A N 2237 C CA . PRO A 303 ? 0.3128 0.2496 0.2564 -0.0335 -0.0189 0.0102 303 PRO A CA 2238 C C . PRO A 303 ? 0.2911 0.2262 0.2321 -0.0331 -0.0180 0.0103 303 PRO A C 2239 O O . PRO A 303 ? 0.2865 0.2187 0.2242 -0.0361 -0.0206 0.0130 303 PRO A O 2240 C CB . PRO A 303 ? 0.3331 0.2584 0.2693 -0.0342 -0.0199 0.0098 303 PRO A CB 2241 C CG . PRO A 303 ? 0.3210 0.2490 0.2614 -0.0322 -0.0186 0.0082 303 PRO A CG 2242 C CD . PRO A 303 ? 0.3174 0.2541 0.2650 -0.0290 -0.0158 0.0061 303 PRO A CD 2243 N N . PHE A 304 ? 0.2946 0.2315 0.2374 -0.0297 -0.0148 0.0078 304 PHE A N 2244 C CA . PHE A 304 ? 0.2839 0.2179 0.2237 -0.0291 -0.0138 0.0079 304 PHE A CA 2245 C C . PHE A 304 ? 0.2738 0.2187 0.2195 -0.0291 -0.0131 0.0089 304 PHE A C 2246 O O . PHE A 304 ? 0.2854 0.2292 0.2296 -0.0288 -0.0125 0.0093 304 PHE A O 2247 C CB . PHE A 304 ? 0.2856 0.2136 0.2225 -0.0257 -0.0108 0.0051 304 PHE A CB 2248 C CG . PHE A 304 ? 0.2866 0.2043 0.2168 -0.0257 -0.0113 0.0045 304 PHE A CG 2249 C CD1 . PHE A 304 ? 0.2992 0.2064 0.2211 -0.0270 -0.0131 0.0052 304 PHE A CD1 2250 C CD2 . PHE A 304 ? 0.2885 0.2071 0.2207 -0.0244 -0.0104 0.0031 304 PHE A CD2 2251 C CE1 . PHE A 304 ? 0.3038 0.2023 0.2192 -0.0268 -0.0137 0.0044 304 PHE A CE1 2252 C CE2 . PHE A 304 ? 0.2905 0.2006 0.2164 -0.0244 -0.0108 0.0027 304 PHE A CE2 2253 C CZ . PHE A 304 ? 0.3039 0.2042 0.2212 -0.0255 -0.0122 0.0032 304 PHE A CZ 2254 N N . ALA A 305 ? 0.2600 0.2155 0.2122 -0.0293 -0.0133 0.0093 305 ALA A N 2255 C CA . ALA A 305 ? 0.2509 0.2181 0.2087 -0.0289 -0.0125 0.0098 305 ALA A CA 2256 C C . ALA A 305 ? 0.2536 0.2304 0.2160 -0.0311 -0.0145 0.0123 305 ALA A C 2257 O O . ALA A 305 ? 0.2403 0.2292 0.2089 -0.0296 -0.0133 0.0117 305 ALA A O 2258 C CB . ALA A 305 ? 0.2432 0.2161 0.2057 -0.0249 -0.0093 0.0062 305 ALA A CB 2259 N N . VAL A 306 ? 0.2675 0.2391 0.2266 -0.0346 -0.0177 0.0152 306 VAL A N 2260 C CA . VAL A 306 ? 0.2799 0.2600 0.2429 -0.0372 -0.0200 0.0185 306 VAL A CA 2261 C C . VAL A 306 ? 0.2646 0.2564 0.2317 -0.0379 -0.0198 0.0208 306 VAL A C 2262 O O . VAL A 306 ? 0.2688 0.2575 0.2329 -0.0392 -0.0203 0.0224 306 VAL A O 2263 C CB . VAL A 306 ? 0.2948 0.2661 0.2526 -0.0415 -0.0240 0.0218 306 VAL A CB 2264 C CG1 . VAL A 306 ? 0.3002 0.2817 0.2627 -0.0446 -0.0265 0.0260 306 VAL A CG1 2265 C CG2 . VAL A 306 ? 0.2957 0.2589 0.2510 -0.0403 -0.0238 0.0193 306 VAL A CG2 2266 N N . GLY A 307 ? 0.2571 0.2628 0.2311 -0.0368 -0.0190 0.0209 307 GLY A N 2267 C CA . GLY A 307 ? 0.2460 0.2642 0.2237 -0.0374 -0.0187 0.0233 307 GLY A CA 2268 C C . GLY A 307 ? 0.2482 0.2740 0.2292 -0.0333 -0.0151 0.0197 307 GLY A C 2269 O O . GLY A 307 ? 0.2364 0.2752 0.2215 -0.0332 -0.0146 0.0212 307 GLY A O 2270 N N . LYS A 308 ? 0.2502 0.2694 0.2299 -0.0299 -0.0128 0.0150 308 LYS A N 2271 C CA . LYS A 308 ? 0.2641 0.2908 0.2472 -0.0261 -0.0098 0.0115 308 LYS A CA 2272 C C . LYS A 308 ? 0.2661 0.3020 0.2551 -0.0229 -0.0087 0.0083 308 LYS A C 2273 O O . LYS A 308 ? 0.2596 0.2937 0.2497 -0.0232 -0.0100 0.0084 308 LYS A O 2274 C CB . LYS A 308 ? 0.2809 0.2971 0.2605 -0.0239 -0.0079 0.0082 308 LYS A CB 2275 C CG . LYS A 308 ? 0.3058 0.3103 0.2789 -0.0264 -0.0090 0.0105 308 LYS A CG 2276 C CD . LYS A 308 ? 0.3435 0.3528 0.3163 -0.0296 -0.0106 0.0150 308 LYS A CD 2277 C CE . LYS A 308 ? 0.3675 0.3814 0.3413 -0.0283 -0.0087 0.0145 308 LYS A CE 2278 N NZ . LYS A 308 ? 0.4066 0.4180 0.3775 -0.0323 -0.0113 0.0196 308 LYS A NZ 2279 N N A ARG A 309 ? 0.2621 0.3075 0.2549 -0.0196 -0.0066 0.0053 309 ARG A N 2280 N N B ARG A 309 ? 0.2662 0.3108 0.2587 -0.0195 -0.0065 0.0051 309 ARG A N 2281 C CA A ARG A 309 ? 0.2643 0.3198 0.2631 -0.0160 -0.0058 0.0019 309 ARG A CA 2282 C CA B ARG A 309 ? 0.2731 0.3284 0.2716 -0.0159 -0.0056 0.0017 309 ARG A CA 2283 C C A ARG A 309 ? 0.2533 0.3051 0.2535 -0.0118 -0.0041 -0.0037 309 ARG A C 2284 C C B ARG A 309 ? 0.2566 0.3063 0.2562 -0.0120 -0.0042 -0.0037 309 ARG A C 2285 O O A ARG A 309 ? 0.2471 0.2991 0.2464 -0.0103 -0.0025 -0.0055 309 ARG A O 2286 O O B ARG A 309 ? 0.2459 0.2910 0.2433 -0.0110 -0.0028 -0.0053 309 ARG A O 2287 C CB A ARG A 309 ? 0.2727 0.3448 0.2754 -0.0152 -0.0050 0.0028 309 ARG A CB 2288 C CB B ARG A 309 ? 0.2918 0.3624 0.2935 -0.0149 -0.0044 0.0021 309 ARG A CB 2289 C CG A ARG A 309 ? 0.2850 0.3666 0.2935 -0.0104 -0.0039 -0.0019 309 ARG A CG 2290 C CG B ARG A 309 ? 0.3184 0.4010 0.3259 -0.0105 -0.0033 -0.0018 309 ARG A CG 2291 C CD A ARG A 309 ? 0.2927 0.3917 0.3047 -0.0089 -0.0029 -0.0016 309 ARG A CD 2292 C CD B ARG A 309 ? 0.3361 0.4356 0.3464 -0.0098 -0.0023 -0.0007 309 ARG A CD 2293 N NE A ARG A 309 ? 0.3140 0.4197 0.3265 -0.0127 -0.0044 0.0044 309 ARG A NE 2294 N NE B ARG A 309 ? 0.3666 0.4755 0.3794 -0.0118 -0.0037 0.0035 309 ARG A NE 2295 C CZ A ARG A 309 ? 0.3140 0.4228 0.3294 -0.0132 -0.0058 0.0059 309 ARG A CZ 2296 C CZ B ARG A 309 ? 0.3843 0.4964 0.3956 -0.0164 -0.0050 0.0099 309 ARG A CZ 2297 N NH1 A ARG A 309 ? 0.3032 0.4089 0.3214 -0.0099 -0.0058 0.0018 309 ARG A NH1 2298 N NH1 B ARG A 309 ? 0.3830 0.4897 0.3902 -0.0193 -0.0053 0.0125 309 ARG A NH1 2299 N NH2 A ARG A 309 ? 0.3344 0.4493 0.3502 -0.0171 -0.0074 0.0121 309 ARG A NH2 2300 N NH2 B ARG A 309 ? 0.3817 0.5028 0.3960 -0.0181 -0.0064 0.0138 309 ARG A NH2 2301 N N . THR A 310 ? 0.2448 0.2942 0.2478 -0.0098 -0.0047 -0.0062 310 THR A N 2302 C CA . THR A 310 ? 0.2329 0.2794 0.2384 -0.0059 -0.0038 -0.0115 310 THR A CA 2303 C C . THR A 310 ? 0.2341 0.2906 0.2460 -0.0023 -0.0041 -0.0148 310 THR A C 2304 O O . THR A 310 ? 0.2320 0.2982 0.2462 -0.0029 -0.0046 -0.0127 310 THR A O 2305 C CB . THR A 310 ? 0.2406 0.2730 0.2433 -0.0067 -0.0046 -0.0116 310 THR A CB 2306 O OG1 . THR A 310 ? 0.2395 0.2699 0.2431 -0.0083 -0.0065 -0.0097 310 THR A OG1 2307 C CG2 . THR A 310 ? 0.2340 0.2571 0.2302 -0.0095 -0.0041 -0.0089 310 THR A CG2 2308 N N . CYS A 311 ? 0.2337 0.2881 0.2487 0.0013 -0.0040 -0.0197 311 CYS A N 2309 C CA . CYS A 311 ? 0.2284 0.2903 0.2497 0.0052 -0.0047 -0.0235 311 CYS A CA 2310 C C . CYS A 311 ? 0.2350 0.3000 0.2590 0.0042 -0.0063 -0.0210 311 CYS A C 2311 O O . CYS A 311 ? 0.2245 0.3009 0.2524 0.0063 -0.0062 -0.0220 311 CYS A O 2312 C CB . CYS A 311 ? 0.2354 0.2905 0.2593 0.0083 -0.0054 -0.0281 311 CYS A CB 2313 S SG . CYS A 311 ? 0.2411 0.2956 0.2632 0.0102 -0.0038 -0.0313 311 CYS A SG 2314 N N . SER A 312 ? 0.2379 0.2936 0.2594 0.0008 -0.0077 -0.0176 312 SER A N 2315 C CA . SER A 312 ? 0.2421 0.3008 0.2663 -0.0003 -0.0094 -0.0150 312 SER A CA 2316 C C . SER A 312 ? 0.2591 0.3239 0.2812 -0.0040 -0.0096 -0.0097 312 SER A C 2317 O O . SER A 312 ? 0.2902 0.3577 0.3145 -0.0054 -0.0112 -0.0070 312 SER A O 2318 C CB . SER A 312 ? 0.2440 0.2908 0.2673 -0.0019 -0.0111 -0.0141 312 SER A CB 2319 O OG . SER A 312 ? 0.2304 0.2737 0.2572 0.0016 -0.0114 -0.0187 312 SER A OG 2320 N N . GLY A 313 ? 0.2452 0.3121 0.2635 -0.0057 -0.0083 -0.0079 313 GLY A N 2321 C CA . GLY A 313 ? 0.2443 0.3176 0.2610 -0.0093 -0.0088 -0.0027 313 GLY A CA 2322 C C . GLY A 313 ? 0.2458 0.3082 0.2556 -0.0139 -0.0095 0.0010 313 GLY A C 2323 O O . GLY A 313 ? 0.2337 0.2865 0.2398 -0.0136 -0.0086 -0.0008 313 GLY A O 2324 N N . ILE A 314 ? 0.2490 0.3122 0.2572 -0.0182 -0.0114 0.0064 314 ILE A N 2325 C CA . ILE A 314 ? 0.2479 0.3014 0.2494 -0.0226 -0.0125 0.0101 314 ILE A CA 2326 C C . ILE A 314 ? 0.2469 0.2851 0.2441 -0.0242 -0.0140 0.0101 314 ILE A C 2327 O O . ILE A 314 ? 0.2534 0.2904 0.2522 -0.0250 -0.0157 0.0110 314 ILE A O 2328 C CB . ILE A 314 ? 0.2565 0.3170 0.2579 -0.0269 -0.0145 0.0163 314 ILE A CB 2329 C CG1 . ILE A 314 ? 0.2560 0.3322 0.2613 -0.0252 -0.0128 0.0165 314 ILE A CG1 2330 C CG2 . ILE A 314 ? 0.2508 0.2993 0.2452 -0.0313 -0.0162 0.0198 314 ILE A CG2 2331 C CD1 . ILE A 314 ? 0.2686 0.3551 0.2755 -0.0290 -0.0146 0.0228 314 ILE A CD1 2332 N N . VAL A 315 ? 0.2412 0.2682 0.2328 -0.0247 -0.0134 0.0092 315 VAL A N 2333 C CA . VAL A 315 ? 0.2537 0.2664 0.2403 -0.0259 -0.0144 0.0089 315 VAL A CA 2334 C C . VAL A 315 ? 0.2556 0.2632 0.2385 -0.0307 -0.0177 0.0137 315 VAL A C 2335 O O . VAL A 315 ? 0.2511 0.2594 0.2314 -0.0339 -0.0191 0.0174 315 VAL A O 2336 C CB . VAL A 315 ? 0.2642 0.2671 0.2454 -0.0253 -0.0129 0.0074 315 VAL A CB 2337 C CG1 . VAL A 315 ? 0.2822 0.2710 0.2576 -0.0264 -0.0138 0.0073 315 VAL A CG1 2338 C CG2 . VAL A 315 ? 0.2632 0.2705 0.2478 -0.0210 -0.0100 0.0030 315 VAL A CG2 2339 N N . THR A 316 ? 0.2645 0.2678 0.2476 -0.0313 -0.0192 0.0137 316 THR A N 2340 C CA . THR A 316 ? 0.2886 0.2854 0.2676 -0.0357 -0.0225 0.0177 316 THR A CA 2341 C C . THR A 316 ? 0.3136 0.2952 0.2854 -0.0363 -0.0229 0.0164 316 THR A C 2342 O O . THR A 316 ? 0.3098 0.2880 0.2817 -0.0331 -0.0207 0.0128 316 THR A O 2343 C CB . THR A 316 ? 0.2752 0.2800 0.2599 -0.0363 -0.0242 0.0195 316 THR A CB 2344 O OG1 . THR A 316 ? 0.2965 0.2999 0.2844 -0.0333 -0.0233 0.0161 316 THR A OG1 2345 C CG2 . THR A 316 ? 0.2843 0.3046 0.2759 -0.0348 -0.0232 0.0201 316 THR A CG2 2346 N N . PRO A 317 ? 0.3501 0.3229 0.3156 -0.0404 -0.0260 0.0196 317 PRO A N 2347 C CA . PRO A 317 ? 0.3984 0.3574 0.3562 -0.0409 -0.0265 0.0185 317 PRO A CA 2348 C C . PRO A 317 ? 0.4541 0.4113 0.4139 -0.0383 -0.0251 0.0156 317 PRO A C 2349 O O . PRO A 317 ? 0.4860 0.4364 0.4423 -0.0361 -0.0231 0.0129 317 PRO A O 2350 C CB . PRO A 317 ? 0.4047 0.3583 0.3579 -0.0459 -0.0308 0.0226 317 PRO A CB 2351 C CG . PRO A 317 ? 0.3981 0.3594 0.3539 -0.0481 -0.0321 0.0260 317 PRO A CG 2352 C CD . PRO A 317 ? 0.3793 0.3550 0.3442 -0.0447 -0.0292 0.0245 317 PRO A CD 2353 O OXT . PRO A 317 ? 0.4443 0.4083 0.4104 -0.0379 -0.0258 0.0159 317 PRO A OXT # 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 LEU 1 1 1 LEU LEU A . n A 1 2 PRO 2 2 2 PRO PRO A . n A 1 3 SER 3 3 3 SER SER A . n A 1 4 GLY 4 4 4 GLY GLY A . n A 1 5 SER 5 5 5 SER SER A . n A 1 6 ASP 6 6 6 ASP ASP A . n A 1 7 PRO 7 7 7 PRO PRO A . n A 1 8 ALA 8 8 8 ALA ALA A . n A 1 9 PHE 9 9 9 PHE PHE A . n A 1 10 SER 10 10 10 SER SER A . n A 1 11 GLN 11 11 11 GLN GLN A . n A 1 12 PRO 12 12 12 PRO PRO A . n A 1 13 LYS 13 13 13 LYS LYS A . n A 1 14 SER 14 14 14 SER SER A . n A 1 15 VAL 15 15 15 VAL VAL A . n A 1 16 LEU 16 16 16 LEU LEU A . n A 1 17 ASP 17 17 17 ASP ASP A . n A 1 18 ALA 18 18 18 ALA ALA A . n A 1 19 GLY 19 19 19 GLY GLY A . n A 1 20 LEU 20 20 20 LEU LEU A . n A 1 21 THR 21 21 21 THR THR A . n A 1 22 CYS 22 22 22 CYS CYS A . n A 1 23 GLN 23 23 23 GLN GLN A . n A 1 24 GLY 24 24 24 GLY GLY A . n A 1 25 ALA 25 25 25 ALA ALA A . n A 1 26 SER 26 26 26 SER SER A . n A 1 27 PRO 27 27 27 PRO PRO A . n A 1 28 SER 28 28 28 SER SER A . n A 1 29 SER 29 29 29 SER SER A . n A 1 30 VAL 30 30 30 VAL VAL A . n A 1 31 SER 31 31 31 SER SER A . n A 1 32 LYS 32 32 32 LYS LYS A . n A 1 33 PRO 33 33 33 PRO PRO A . n A 1 34 ILE 34 34 34 ILE ILE A . n A 1 35 LEU 35 35 35 LEU LEU A . n A 1 36 LEU 36 36 36 LEU LEU A . n A 1 37 VAL 37 37 37 VAL VAL A . n A 1 38 PRO 38 38 38 PRO PRO A . n A 1 39 GLY 39 39 39 GLY GLY A . n A 1 40 THR 40 40 40 THR THR A . n A 1 41 GLY 41 41 41 GLY GLY A . n A 1 42 THR 42 42 42 THR THR A . n A 1 43 THR 43 43 43 THR THR A . n A 1 44 GLY 44 44 44 GLY GLY A . n A 1 45 PRO 45 45 45 PRO PRO A . n A 1 46 GLN 46 46 46 GLN GLN A . n A 1 47 SER 47 47 47 SER SER A . n A 1 48 PHE 48 48 48 PHE PHE A . n A 1 49 ASP 49 49 49 ASP ASP A . n A 1 50 SER 50 50 50 SER SER A . n A 1 51 ASN 51 51 51 ASN ASN A . n A 1 52 TRP 52 52 52 TRP TRP A . n A 1 53 ILE 53 53 53 ILE ILE A . n A 1 54 PRO 54 54 54 PRO PRO A . n A 1 55 LEU 55 55 55 LEU LEU A . n A 1 56 SER 56 56 56 SER SER A . n A 1 57 THR 57 57 57 THR THR A . n A 1 58 GLN 58 58 58 GLN GLN A . n A 1 59 LEU 59 59 59 LEU LEU A . n A 1 60 GLY 60 60 60 GLY GLY A . n A 1 61 TYR 61 61 61 TYR TYR A . n A 1 62 THR 62 62 62 THR THR A . n A 1 63 PRO 63 63 63 PRO PRO A . n A 1 64 CYS 64 64 64 CYS CYS A . n A 1 65 TRP 65 65 65 TRP TRP A . n A 1 66 ILE 66 66 66 ILE ILE A . n A 1 67 SER 67 67 67 SER SER A . n A 1 68 PRO 68 68 68 PRO PRO A . n A 1 69 PRO 69 69 69 PRO PRO A . n A 1 70 PRO 70 70 70 PRO PRO A . n A 1 71 PHE 71 71 71 PHE PHE A . n A 1 72 MET 72 72 72 MET MET A . n A 1 73 LEU 73 73 73 LEU LEU A . n A 1 74 ASN 74 74 74 ASN ASN A . n A 1 75 ASP 75 75 75 ASP ASP A . n A 1 76 THR 76 76 76 THR THR A . n A 1 77 GLN 77 77 77 GLN GLN A . n A 1 78 VAL 78 78 78 VAL VAL A . n A 1 79 ASN 79 79 79 ASN ASN A . n A 1 80 THR 80 80 80 THR THR A . n A 1 81 GLU 81 81 81 GLU GLU A . n A 1 82 TYR 82 82 82 TYR TYR A . n A 1 83 MET 83 83 83 MET MET A . n A 1 84 VAL 84 84 84 VAL VAL A . n A 1 85 ASN 85 85 85 ASN ASN A . n A 1 86 ALA 86 86 86 ALA ALA A . n A 1 87 ILE 87 87 87 ILE ILE A . n A 1 88 THR 88 88 88 THR THR A . n A 1 89 ALA 89 89 89 ALA ALA A . n A 1 90 LEU 90 90 90 LEU LEU A . n A 1 91 TYR 91 91 91 TYR TYR A . n A 1 92 ALA 92 92 92 ALA ALA A . n A 1 93 GLY 93 93 93 GLY GLY A . n A 1 94 SER 94 94 94 SER SER A . n A 1 95 GLY 95 95 95 GLY GLY A . n A 1 96 ASN 96 96 96 ASN ASN A . n A 1 97 ASN 97 97 97 ASN ASN A . n A 1 98 LYS 98 98 98 LYS LYS A . n A 1 99 LEU 99 99 99 LEU LEU A . n A 1 100 PRO 100 100 100 PRO PRO A . n A 1 101 VAL 101 101 101 VAL VAL A . n A 1 102 LEU 102 102 102 LEU LEU A . n A 1 103 THR 103 103 103 THR THR A . n A 1 104 TRP 104 104 104 TRP TRP A . n A 1 105 SER 105 105 105 SER SER A . n A 1 106 GLN 106 106 106 GLN GLN A . n A 1 107 GLY 107 107 107 GLY GLY A . n A 1 108 GLY 108 108 108 GLY GLY A . n A 1 109 LEU 109 109 109 LEU LEU A . n A 1 110 VAL 110 110 110 VAL VAL A . n A 1 111 ALA 111 111 111 ALA ALA A . n A 1 112 GLN 112 112 112 GLN GLN A . n A 1 113 TRP 113 113 113 TRP TRP A . n A 1 114 GLY 114 114 114 GLY GLY A . n A 1 115 LEU 115 115 115 LEU LEU A . n A 1 116 THR 116 116 116 THR THR A . n A 1 117 PHE 117 117 117 PHE PHE A . n A 1 118 PHE 118 118 118 PHE PHE A . n A 1 119 PRO 119 119 119 PRO PRO A . n A 1 120 SER 120 120 120 SER SER A . n A 1 121 ILE 121 121 121 ILE ILE A . n A 1 122 ARG 122 122 122 ARG ARG A . n A 1 123 SER 123 123 123 SER SER A . n A 1 124 LYS 124 124 124 LYS LYS A . n A 1 125 VAL 125 125 125 VAL VAL A . n A 1 126 ASP 126 126 126 ASP ASP A . n A 1 127 ARG 127 127 127 ARG ARG A . n A 1 128 LEU 128 128 128 LEU LEU A . n A 1 129 MET 129 129 129 MET MET A . n A 1 130 ALA 130 130 130 ALA ALA A . n A 1 131 PHE 131 131 131 PHE PHE A . n A 1 132 ALA 132 132 132 ALA ALA A . n A 1 133 PRO 133 133 133 PRO PRO A . n A 1 134 ASP 134 134 134 ASP ASP A . n A 1 135 TYR 135 135 135 TYR TYR A . n A 1 136 LYS 136 136 136 LYS LYS A . n A 1 137 GLY 137 137 137 GLY GLY A . n A 1 138 THR 138 138 138 THR THR A . n A 1 139 VAL 139 139 139 VAL VAL A . n A 1 140 LEU 140 140 140 LEU LEU A . n A 1 141 ALA 141 141 141 ALA ALA A . n A 1 142 GLY 142 142 142 GLY GLY A . n A 1 143 PRO 143 143 143 PRO PRO A . n A 1 144 LEU 144 144 144 LEU LEU A . n A 1 145 ASP 145 145 145 ASP ASP A . n A 1 146 ALA 146 146 146 ALA ALA A . n A 1 147 LEU 147 147 147 LEU LEU A . n A 1 148 ALA 148 148 148 ALA ALA A . n A 1 149 VAL 149 149 149 VAL VAL A . n A 1 150 SER 150 150 150 SER SER A . n A 1 151 ALA 151 151 151 ALA ALA A . n A 1 152 PRO 152 152 152 PRO PRO A . n A 1 153 SER 153 153 153 SER SER A . n A 1 154 VAL 154 154 154 VAL VAL A . n A 1 155 TRP 155 155 155 TRP TRP A . n A 1 156 GLN 156 156 156 GLN GLN A . n A 1 157 GLN 157 157 157 GLN GLN A . n A 1 158 THR 158 158 158 THR THR A . n A 1 159 THR 159 159 159 THR THR A . n A 1 160 GLY 160 160 160 GLY GLY A . n A 1 161 SER 161 161 161 SER SER A . n A 1 162 ALA 162 162 162 ALA ALA A . n A 1 163 LEU 163 163 163 LEU LEU A . n A 1 164 THR 164 164 164 THR THR A . n A 1 165 THR 165 165 165 THR THR A . n A 1 166 ALA 166 166 166 ALA ALA A . n A 1 167 LEU 167 167 167 LEU LEU A . n A 1 168 ARG 168 168 168 ARG ARG A . n A 1 169 ASN 169 169 169 ASN ASN A . n A 1 170 ALA 170 170 170 ALA ALA A . n A 1 171 GLY 171 171 171 GLY GLY A . n A 1 172 GLY 172 172 172 GLY GLY A . n A 1 173 LEU 173 173 173 LEU LEU A . n A 1 174 THR 174 174 174 THR THR A . n A 1 175 GLN 175 175 175 GLN GLN A . n A 1 176 ILE 176 176 176 ILE ILE A . n A 1 177 VAL 177 177 177 VAL VAL A . n A 1 178 PRO 178 178 178 PRO PRO A . n A 1 179 THR 179 179 179 THR THR A . n A 1 180 THR 180 180 180 THR THR A . n A 1 181 ASN 181 181 181 ASN ASN A . n A 1 182 LEU 182 182 182 LEU LEU A . n A 1 183 TYR 183 183 183 TYR TYR A . n A 1 184 SER 184 184 184 SER SER A . n A 1 185 ALA 185 185 185 ALA ALA A . n A 1 186 THR 186 186 186 THR THR A . n A 1 187 ASP 187 187 187 ASP ASP A . n A 1 188 GLU 188 188 188 GLU GLU A . n A 1 189 ILE 189 189 189 ILE ILE A . n A 1 190 VAL 190 190 190 VAL VAL A . n A 1 191 GLN 191 191 191 GLN GLN A . n A 1 192 PRO 192 192 192 PRO PRO A . n A 1 193 GLN 193 193 193 GLN GLN A . n A 1 194 VAL 194 194 194 VAL VAL A . n A 1 195 SER 195 195 195 SER SER A . n A 1 196 ASN 196 196 196 ASN ASN A . n A 1 197 SER 197 197 197 SER SER A . n A 1 198 PRO 198 198 198 PRO PRO A . n A 1 199 LEU 199 199 199 LEU LEU A . n A 1 200 ASP 200 200 200 ASP ASP A . n A 1 201 SER 201 201 201 SER SER A . n A 1 202 SER 202 202 202 SER SER A . n A 1 203 TYR 203 203 203 TYR TYR A . n A 1 204 LEU 204 204 204 LEU LEU A . n A 1 205 PHE 205 205 205 PHE PHE A . n A 1 206 ASN 206 206 206 ASN ASN A . n A 1 207 GLY 207 207 207 GLY GLY A . n A 1 208 LYS 208 208 208 LYS LYS A . n A 1 209 ASN 209 209 209 ASN ASN A . n A 1 210 VAL 210 210 210 VAL VAL A . n A 1 211 GLN 211 211 211 GLN GLN A . n A 1 212 ALA 212 212 212 ALA ALA A . n A 1 213 GLN 213 213 213 GLN GLN A . n A 1 214 ALA 214 214 214 ALA ALA A . n A 1 215 VAL 215 215 215 VAL VAL A . n A 1 216 CYS 216 216 216 CYS CYS A . n A 1 217 GLY 217 217 217 GLY GLY A . n A 1 218 PRO 218 218 218 PRO PRO A . n A 1 219 LEU 219 219 219 LEU LEU A . n A 1 220 PHE 220 220 220 PHE PHE A . n A 1 221 VAL 221 221 221 VAL VAL A . n A 1 222 ILE 222 222 222 ILE ILE A . n A 1 223 ASP 223 223 223 ASP ASP A . n A 1 224 HIS 224 224 224 HIS HIS A . n A 1 225 ALA 225 225 225 ALA ALA A . n A 1 226 GLY 226 226 226 GLY GLY A . n A 1 227 SER 227 227 227 SER SER A . n A 1 228 LEU 228 228 228 LEU LEU A . n A 1 229 THR 229 229 229 THR THR A . n A 1 230 SER 230 230 230 SER SER A . n A 1 231 GLN 231 231 231 GLN GLN A . n A 1 232 PHE 232 232 232 PHE PHE A . n A 1 233 SER 233 233 233 SER SER A . n A 1 234 TYR 234 234 234 TYR TYR A . n A 1 235 VAL 235 235 235 VAL VAL A . n A 1 236 VAL 236 236 236 VAL VAL A . n A 1 237 GLY 237 237 237 GLY GLY A . n A 1 238 ARG 238 238 238 ARG ARG A . n A 1 239 SER 239 239 239 SER SER A . n A 1 240 ALA 240 240 240 ALA ALA A . n A 1 241 LEU 241 241 241 LEU LEU A . n A 1 242 ARG 242 242 242 ARG ARG A . n A 1 243 SER 243 243 243 SER SER A . n A 1 244 THR 244 244 244 THR THR A . n A 1 245 THR 245 245 245 THR THR A . n A 1 246 GLY 246 246 246 GLY GLY A . n A 1 247 GLN 247 247 247 GLN GLN A . n A 1 248 ALA 248 248 248 ALA ALA A . n A 1 249 ARG 249 249 249 ARG ARG A . n A 1 250 SER 250 250 250 SER SER A . n A 1 251 ALA 251 251 251 ALA ALA A . n A 1 252 ASP 252 252 252 ASP ASP A . n A 1 253 TYR 253 253 253 TYR TYR A . n A 1 254 GLY 254 254 254 GLY GLY A . n A 1 255 ILE 255 255 255 ILE ILE A . n A 1 256 THR 256 256 256 THR THR A . n A 1 257 ASP 257 257 257 ASP ASP A . n A 1 258 CYS 258 258 258 CYS CYS A . n A 1 259 ASN 259 259 259 ASN ASN A . n A 1 260 PRO 260 260 260 PRO PRO A . n A 1 261 LEU 261 261 261 LEU LEU A . n A 1 262 PRO 262 262 262 PRO PRO A . n A 1 263 ALA 263 263 263 ALA ALA A . n A 1 264 ASN 264 264 264 ASN ASN A . n A 1 265 ASP 265 265 265 ASP ASP A . n A 1 266 LEU 266 266 266 LEU LEU A . n A 1 267 THR 267 267 267 THR THR A . n A 1 268 PRO 268 268 268 PRO PRO A . n A 1 269 GLU 269 269 269 GLU GLU A . n A 1 270 GLN 270 270 270 GLN GLN A . n A 1 271 LYS 271 271 271 LYS LYS A . n A 1 272 VAL 272 272 272 VAL VAL A . n A 1 273 ALA 273 273 273 ALA ALA A . n A 1 274 ALA 274 274 274 ALA ALA A . n A 1 275 ALA 275 275 275 ALA ALA A . n A 1 276 ALA 276 276 276 ALA ALA A . n A 1 277 LEU 277 277 277 LEU LEU A . n A 1 278 LEU 278 278 278 LEU LEU A . n A 1 279 ALA 279 279 279 ALA ALA A . n A 1 280 PRO 280 280 280 PRO PRO A . n A 1 281 ALA 281 281 281 ALA ALA A . n A 1 282 ALA 282 282 282 ALA ALA A . n A 1 283 ALA 283 283 283 ALA ALA A . n A 1 284 ALA 284 284 284 ALA ALA A . n A 1 285 ILE 285 285 285 ILE ILE A . n A 1 286 VAL 286 286 286 VAL VAL A . n A 1 287 ALA 287 287 287 ALA ALA A . n A 1 288 GLY 288 288 288 GLY GLY A . n A 1 289 PRO 289 289 289 PRO PRO A . n A 1 290 LYS 290 290 290 LYS LYS A . n A 1 291 GLN 291 291 291 GLN GLN A . n A 1 292 ASN 292 292 292 ASN ASN A . n A 1 293 CYS 293 293 293 CYS CYS A . n A 1 294 GLU 294 294 294 GLU GLU A . n A 1 295 PRO 295 295 295 PRO PRO A . n A 1 296 ASP 296 296 296 ASP ASP A . n A 1 297 LEU 297 297 297 LEU LEU A . n A 1 298 MET 298 298 298 MET MET A . n A 1 299 PRO 299 299 299 PRO PRO A . n A 1 300 TYR 300 300 300 TYR TYR A . n A 1 301 ALA 301 301 301 ALA ALA A . n A 1 302 ARG 302 302 302 ARG ARG A . n A 1 303 PRO 303 303 303 PRO PRO A . n A 1 304 PHE 304 304 304 PHE PHE A . n A 1 305 ALA 305 305 305 ALA ALA A . n A 1 306 VAL 306 306 306 VAL VAL A . n A 1 307 GLY 307 307 307 GLY GLY A . n A 1 308 LYS 308 308 308 LYS LYS A . n A 1 309 ARG 309 309 309 ARG ARG A . n A 1 310 THR 310 310 310 THR THR A . n A 1 311 CYS 311 311 311 CYS CYS A . n A 1 312 SER 312 312 312 SER SER A . n A 1 313 GLY 313 313 313 GLY GLY A . n A 1 314 ILE 314 314 314 ILE ILE A . n A 1 315 VAL 315 315 315 VAL VAL A . n A 1 316 THR 316 316 316 THR THR A . n A 1 317 PRO 317 317 317 PRO PRO 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 1 800 800 NAG NAG A . C 2 NAG 2 801 801 NAG NAG A . D 3 HOH 1 901 670 HOH HOH A . D 3 HOH 2 902 428 HOH HOH A . D 3 HOH 3 903 504 HOH HOH A . D 3 HOH 4 904 683 HOH HOH A . D 3 HOH 5 905 589 HOH HOH A . D 3 HOH 6 906 548 HOH HOH A . D 3 HOH 7 907 412 HOH HOH A . D 3 HOH 8 908 703 HOH HOH A . D 3 HOH 9 909 427 HOH HOH A . D 3 HOH 10 910 544 HOH HOH A . D 3 HOH 11 911 417 HOH HOH A . D 3 HOH 12 912 579 HOH HOH A . D 3 HOH 13 913 467 HOH HOH A . D 3 HOH 14 914 689 HOH HOH A . D 3 HOH 15 915 571 HOH HOH A . D 3 HOH 16 916 420 HOH HOH A . D 3 HOH 17 917 710 HOH HOH A . D 3 HOH 18 918 488 HOH HOH A . D 3 HOH 19 919 667 HOH HOH A . D 3 HOH 20 920 696 HOH HOH A . D 3 HOH 21 921 559 HOH HOH A . D 3 HOH 22 922 450 HOH HOH A . D 3 HOH 23 923 577 HOH HOH A . D 3 HOH 24 924 680 HOH HOH A . D 3 HOH 25 925 510 HOH HOH A . D 3 HOH 26 926 446 HOH HOH A . D 3 HOH 27 927 426 HOH HOH A . D 3 HOH 28 928 614 HOH HOH A . D 3 HOH 29 929 672 HOH HOH A . D 3 HOH 30 930 558 HOH HOH A . D 3 HOH 31 931 416 HOH HOH A . D 3 HOH 32 932 405 HOH HOH A . D 3 HOH 33 933 725 HOH HOH A . D 3 HOH 34 934 682 HOH HOH A . D 3 HOH 35 935 644 HOH HOH A . D 3 HOH 36 936 606 HOH HOH A . D 3 HOH 37 937 459 HOH HOH A . D 3 HOH 38 938 519 HOH HOH A . D 3 HOH 39 939 641 HOH HOH A . D 3 HOH 40 940 429 HOH HOH A . D 3 HOH 41 941 482 HOH HOH A . D 3 HOH 42 942 526 HOH HOH A . D 3 HOH 43 943 421 HOH HOH A . D 3 HOH 44 944 471 HOH HOH A . D 3 HOH 45 945 537 HOH HOH A . D 3 HOH 46 946 684 HOH HOH A . D 3 HOH 47 947 516 HOH HOH A . D 3 HOH 48 948 496 HOH HOH A . D 3 HOH 49 949 555 HOH HOH A . D 3 HOH 50 950 453 HOH HOH A . D 3 HOH 51 951 552 HOH HOH A . D 3 HOH 52 952 409 HOH HOH A . D 3 HOH 53 953 438 HOH HOH A . D 3 HOH 54 954 575 HOH HOH A . D 3 HOH 55 955 456 HOH HOH A . D 3 HOH 56 956 439 HOH HOH A . D 3 HOH 57 957 681 HOH HOH A . D 3 HOH 58 958 592 HOH HOH A . D 3 HOH 59 959 487 HOH HOH A . D 3 HOH 60 960 520 HOH HOH A . D 3 HOH 61 961 717 HOH HOH A . D 3 HOH 62 962 406 HOH HOH A . D 3 HOH 63 963 668 HOH HOH A . D 3 HOH 64 964 454 HOH HOH A . D 3 HOH 65 965 602 HOH HOH A . D 3 HOH 66 966 433 HOH HOH A . D 3 HOH 67 967 604 HOH HOH A . D 3 HOH 68 968 585 HOH HOH A . D 3 HOH 69 969 612 HOH HOH A . D 3 HOH 70 970 598 HOH HOH A . D 3 HOH 71 971 402 HOH HOH A . D 3 HOH 72 972 498 HOH HOH A . D 3 HOH 73 973 458 HOH HOH A . D 3 HOH 74 974 486 HOH HOH A . D 3 HOH 75 975 708 HOH HOH A . D 3 HOH 76 976 445 HOH HOH A . D 3 HOH 77 977 651 HOH HOH A . D 3 HOH 78 978 619 HOH HOH A . D 3 HOH 79 979 656 HOH HOH A . D 3 HOH 80 980 411 HOH HOH A . D 3 HOH 81 981 419 HOH HOH A . D 3 HOH 82 982 466 HOH HOH A . D 3 HOH 83 983 550 HOH HOH A . D 3 HOH 84 984 618 HOH HOH A . D 3 HOH 85 985 400 HOH HOH A . D 3 HOH 86 986 638 HOH HOH A . D 3 HOH 87 987 718 HOH HOH A . D 3 HOH 88 988 495 HOH HOH A . D 3 HOH 89 989 501 HOH HOH A . D 3 HOH 90 990 414 HOH HOH A . D 3 HOH 91 991 540 HOH HOH A . D 3 HOH 92 992 404 HOH HOH A . D 3 HOH 93 993 478 HOH HOH A . D 3 HOH 94 994 413 HOH HOH A . D 3 HOH 95 995 549 HOH HOH A . D 3 HOH 96 996 403 HOH HOH A . D 3 HOH 97 997 463 HOH HOH A . D 3 HOH 98 998 434 HOH HOH A . D 3 HOH 99 999 587 HOH HOH A . D 3 HOH 100 1000 556 HOH HOH A . D 3 HOH 101 1001 492 HOH HOH A . D 3 HOH 102 1002 563 HOH HOH A . D 3 HOH 103 1003 475 HOH HOH A . D 3 HOH 104 1004 554 HOH HOH A . D 3 HOH 105 1005 586 HOH HOH A . D 3 HOH 106 1006 527 HOH HOH A . D 3 HOH 107 1007 513 HOH HOH A . D 3 HOH 108 1008 443 HOH HOH A . D 3 HOH 109 1009 591 HOH HOH A . D 3 HOH 110 1010 408 HOH HOH A . D 3 HOH 111 1011 603 HOH HOH A . D 3 HOH 112 1012 673 HOH HOH A . D 3 HOH 113 1013 423 HOH HOH A . D 3 HOH 114 1014 701 HOH HOH A . D 3 HOH 115 1015 437 HOH HOH A . D 3 HOH 116 1016 601 HOH HOH A . D 3 HOH 117 1017 455 HOH HOH A . D 3 HOH 118 1018 539 HOH HOH A . D 3 HOH 119 1019 517 HOH HOH A . D 3 HOH 120 1020 502 HOH HOH A . D 3 HOH 121 1021 430 HOH HOH A . D 3 HOH 122 1022 401 HOH HOH A . D 3 HOH 123 1023 574 HOH HOH A . D 3 HOH 124 1024 642 HOH HOH A . D 3 HOH 125 1025 553 HOH HOH A . D 3 HOH 126 1026 468 HOH HOH A . D 3 HOH 127 1027 731 HOH HOH A . D 3 HOH 128 1028 503 HOH HOH A . D 3 HOH 129 1029 424 HOH HOH A . D 3 HOH 130 1030 457 HOH HOH A . D 3 HOH 131 1031 655 HOH HOH A . D 3 HOH 132 1032 448 HOH HOH A . D 3 HOH 133 1033 447 HOH HOH A . D 3 HOH 134 1034 533 HOH HOH A . D 3 HOH 135 1035 546 HOH HOH A . D 3 HOH 136 1036 415 HOH HOH A . D 3 HOH 137 1037 588 HOH HOH A . D 3 HOH 138 1038 472 HOH HOH A . D 3 HOH 139 1039 635 HOH HOH A . D 3 HOH 140 1040 694 HOH HOH A . D 3 HOH 141 1041 435 HOH HOH A . D 3 HOH 142 1042 441 HOH HOH A . D 3 HOH 143 1043 629 HOH HOH A . D 3 HOH 144 1044 545 HOH HOH A . D 3 HOH 145 1045 452 HOH HOH A . D 3 HOH 146 1046 473 HOH HOH A . D 3 HOH 147 1047 442 HOH HOH A . D 3 HOH 148 1048 573 HOH HOH A . D 3 HOH 149 1049 677 HOH HOH A . D 3 HOH 150 1050 640 HOH HOH A . D 3 HOH 151 1051 500 HOH HOH A . D 3 HOH 152 1052 479 HOH HOH A . D 3 HOH 153 1053 522 HOH HOH A . D 3 HOH 154 1054 514 HOH HOH A . D 3 HOH 155 1055 634 HOH HOH A . D 3 HOH 156 1056 528 HOH HOH A . D 3 HOH 157 1057 665 HOH HOH A . D 3 HOH 158 1058 664 HOH HOH A . D 3 HOH 159 1059 511 HOH HOH A . D 3 HOH 160 1060 440 HOH HOH A . D 3 HOH 161 1061 506 HOH HOH A . D 3 HOH 162 1062 508 HOH HOH A . D 3 HOH 163 1063 470 HOH HOH A . D 3 HOH 164 1064 593 HOH HOH A . D 3 HOH 165 1065 515 HOH HOH A . D 3 HOH 166 1066 730 HOH HOH A . D 3 HOH 167 1067 493 HOH HOH A . D 3 HOH 168 1068 643 HOH HOH A . D 3 HOH 169 1069 660 HOH HOH A . D 3 HOH 170 1070 483 HOH HOH A . D 3 HOH 171 1071 627 HOH HOH A . D 3 HOH 172 1072 497 HOH HOH A . D 3 HOH 173 1073 474 HOH HOH A . D 3 HOH 174 1074 543 HOH HOH A . D 3 HOH 175 1075 494 HOH HOH A . D 3 HOH 176 1076 570 HOH HOH A . D 3 HOH 177 1077 608 HOH HOH A . D 3 HOH 178 1078 596 HOH HOH A . D 3 HOH 179 1079 561 HOH HOH A . D 3 HOH 180 1080 538 HOH HOH A . D 3 HOH 181 1081 484 HOH HOH A . D 3 HOH 182 1082 460 HOH HOH A . D 3 HOH 183 1083 449 HOH HOH A . D 3 HOH 184 1084 666 HOH HOH A . D 3 HOH 185 1085 698 HOH HOH A . D 3 HOH 186 1086 444 HOH HOH A . D 3 HOH 187 1087 462 HOH HOH A . D 3 HOH 188 1088 727 HOH HOH A . D 3 HOH 189 1089 676 HOH HOH A . D 3 HOH 190 1090 607 HOH HOH A . D 3 HOH 191 1091 562 HOH HOH A . D 3 HOH 192 1092 729 HOH HOH A . D 3 HOH 193 1093 418 HOH HOH A . D 3 HOH 194 1094 661 HOH HOH A . D 3 HOH 195 1095 649 HOH HOH A . D 3 HOH 196 1096 518 HOH HOH A . D 3 HOH 197 1097 594 HOH HOH A . D 3 HOH 198 1098 535 HOH HOH A . D 3 HOH 199 1099 615 HOH HOH A . D 3 HOH 200 1100 542 HOH HOH A . D 3 HOH 201 1101 512 HOH HOH A . D 3 HOH 202 1102 436 HOH HOH A . D 3 HOH 203 1103 576 HOH HOH A . D 3 HOH 204 1104 581 HOH HOH A . D 3 HOH 205 1105 564 HOH HOH A . D 3 HOH 206 1106 541 HOH HOH A . D 3 HOH 207 1107 646 HOH HOH A . D 3 HOH 208 1108 536 HOH HOH A . D 3 HOH 209 1109 605 HOH HOH A . D 3 HOH 210 1110 499 HOH HOH A . D 3 HOH 211 1111 529 HOH HOH A . D 3 HOH 212 1112 700 HOH HOH A . D 3 HOH 213 1113 600 HOH HOH A . D 3 HOH 214 1114 595 HOH HOH A . D 3 HOH 215 1115 507 HOH HOH A . D 3 HOH 216 1116 657 HOH HOH A . D 3 HOH 217 1117 633 HOH HOH A . D 3 HOH 218 1118 557 HOH HOH A . D 3 HOH 219 1119 599 HOH HOH A . D 3 HOH 220 1120 690 HOH HOH A . D 3 HOH 221 1121 715 HOH HOH A . D 3 HOH 222 1122 639 HOH HOH A . D 3 HOH 223 1123 616 HOH HOH A . D 3 HOH 224 1124 709 HOH HOH A . D 3 HOH 225 1125 628 HOH HOH A . D 3 HOH 226 1126 621 HOH HOH A . D 3 HOH 227 1127 532 HOH HOH A . D 3 HOH 228 1128 477 HOH HOH A . D 3 HOH 229 1129 476 HOH HOH A . D 3 HOH 230 1130 674 HOH HOH A . D 3 HOH 231 1131 464 HOH HOH A . D 3 HOH 232 1132 707 HOH HOH A . D 3 HOH 233 1133 469 HOH HOH A . D 3 HOH 234 1134 530 HOH HOH A . D 3 HOH 235 1135 631 HOH HOH A . D 3 HOH 236 1136 691 HOH HOH A . D 3 HOH 237 1137 659 HOH HOH A . D 3 HOH 238 1138 728 HOH HOH A . D 3 HOH 239 1139 465 HOH HOH A . D 3 HOH 240 1140 636 HOH HOH A . D 3 HOH 241 1141 617 HOH HOH A . D 3 HOH 242 1142 613 HOH HOH A . D 3 HOH 243 1143 572 HOH HOH A . D 3 HOH 244 1144 678 HOH HOH A . D 3 HOH 245 1145 485 HOH HOH A . D 3 HOH 246 1146 432 HOH HOH A . D 3 HOH 247 1147 490 HOH HOH A . D 3 HOH 248 1148 480 HOH HOH A . D 3 HOH 249 1149 547 HOH HOH A . D 3 HOH 250 1150 524 HOH HOH A . D 3 HOH 251 1151 645 HOH HOH A . D 3 HOH 252 1152 626 HOH HOH A . D 3 HOH 253 1153 720 HOH HOH A . D 3 HOH 254 1154 407 HOH HOH A . D 3 HOH 255 1155 451 HOH HOH A . D 3 HOH 256 1156 491 HOH HOH A . D 3 HOH 257 1157 505 HOH HOH A . D 3 HOH 258 1158 525 HOH HOH A . D 3 HOH 259 1159 489 HOH HOH A . D 3 HOH 260 1160 534 HOH HOH A . D 3 HOH 261 1161 679 HOH HOH A . D 3 HOH 262 1162 597 HOH HOH A . D 3 HOH 263 1163 654 HOH HOH A . D 3 HOH 264 1164 697 HOH HOH A . D 3 HOH 265 1165 663 HOH HOH A . D 3 HOH 266 1166 531 HOH HOH A . D 3 HOH 267 1167 653 HOH HOH A . D 3 HOH 268 1168 431 HOH HOH A . D 3 HOH 269 1169 669 HOH HOH A . D 3 HOH 270 1170 637 HOH HOH A . D 3 HOH 271 1171 704 HOH HOH A . D 3 HOH 272 1172 647 HOH HOH A . D 3 HOH 273 1173 582 HOH HOH A . D 3 HOH 274 1174 650 HOH HOH A . D 3 HOH 275 1175 702 HOH HOH A . D 3 HOH 276 1176 481 HOH HOH A . D 3 HOH 277 1177 461 HOH HOH A . D 3 HOH 278 1178 713 HOH HOH A . D 3 HOH 279 1179 609 HOH HOH A . D 3 HOH 280 1180 648 HOH HOH A . D 3 HOH 281 1181 625 HOH HOH A . D 3 HOH 282 1182 422 HOH HOH A . D 3 HOH 283 1183 551 HOH HOH A . D 3 HOH 284 1184 632 HOH HOH A . D 3 HOH 285 1185 560 HOH HOH A . D 3 HOH 286 1186 722 HOH HOH A . D 3 HOH 287 1187 658 HOH HOH A . D 3 HOH 288 1188 590 HOH HOH A . D 3 HOH 289 1189 685 HOH HOH A . D 3 HOH 290 1190 523 HOH HOH A . D 3 HOH 291 1191 706 HOH HOH A . D 3 HOH 292 1192 580 HOH HOH A . D 3 HOH 293 1193 724 HOH HOH A . D 3 HOH 294 1194 509 HOH HOH A . D 3 HOH 295 1195 410 HOH HOH A . D 3 HOH 296 1196 610 HOH HOH A . D 3 HOH 297 1197 662 HOH HOH A . D 3 HOH 298 1198 652 HOH HOH A . D 3 HOH 299 1199 611 HOH HOH A . D 3 HOH 300 1200 714 HOH HOH A . D 3 HOH 301 1201 675 HOH HOH A . D 3 HOH 302 1202 693 HOH HOH A . D 3 HOH 303 1203 723 HOH HOH A . D 3 HOH 304 1204 623 HOH HOH A . D 3 HOH 305 1205 425 HOH HOH A . D 3 HOH 306 1206 521 HOH HOH A . D 3 HOH 307 1207 719 HOH HOH A . D 3 HOH 308 1208 624 HOH HOH A . D 3 HOH 309 1209 686 HOH HOH A . D 3 HOH 310 1210 692 HOH HOH A . D 3 HOH 311 1211 712 HOH HOH A . D 3 HOH 312 1212 705 HOH HOH A . D 3 HOH 313 1213 578 HOH HOH A . D 3 HOH 314 1214 671 HOH HOH A . D 3 HOH 315 1215 569 HOH HOH A . D 3 HOH 316 1216 716 HOH HOH A . D 3 HOH 317 1217 711 HOH HOH A . D 3 HOH 318 1218 695 HOH HOH A . D 3 HOH 319 1219 620 HOH HOH A . D 3 HOH 320 1220 726 HOH HOH A . D 3 HOH 321 1221 630 HOH HOH A . D 3 HOH 322 1222 688 HOH HOH A . D 3 HOH 323 1223 584 HOH HOH A . D 3 HOH 324 1224 568 HOH HOH A . D 3 HOH 325 1225 565 HOH HOH A . D 3 HOH 326 1226 687 HOH HOH A . D 3 HOH 327 1227 699 HOH HOH A . D 3 HOH 328 1228 622 HOH HOH A . D 3 HOH 329 1229 583 HOH HOH A . D 3 HOH 330 1230 721 HOH HOH A . D 3 HOH 331 1231 566 HOH HOH A . D 3 HOH 332 1232 567 HOH HOH A . # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details monomeric _pdbx_struct_assembly.oligomeric_count 1 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D # 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)' 350 ? 1 MORE 4 ? 1 'SSA (A^2)' 12320 ? # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2016-01-13 2 'Structure model' 1 1 2016-03-30 3 'Structure model' 1 2 2017-09-13 # _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' 'Database references' 2 3 'Structure model' 'Data collection' # _pdbx_audit_revision_category.ordinal 1 _pdbx_audit_revision_category.revision_ordinal 3 _pdbx_audit_revision_category.data_content_type 'Structure model' _pdbx_audit_revision_category.category diffrn_source # _pdbx_audit_revision_item.ordinal 1 _pdbx_audit_revision_item.revision_ordinal 3 _pdbx_audit_revision_item.data_content_type 'Structure model' _pdbx_audit_revision_item.item '_diffrn_source.source' # _pdbx_refine_tls.id 1 _pdbx_refine_tls.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine_tls.details ? _pdbx_refine_tls.method refined _pdbx_refine_tls.origin_x 25.1757 _pdbx_refine_tls.origin_y 11.8976 _pdbx_refine_tls.origin_z 16.3273 _pdbx_refine_tls.T[1][1] 0.0489 _pdbx_refine_tls.T[1][1]_esd ? _pdbx_refine_tls.T[1][2] 0.0084 _pdbx_refine_tls.T[1][2]_esd ? _pdbx_refine_tls.T[1][3] 0.0203 _pdbx_refine_tls.T[1][3]_esd ? _pdbx_refine_tls.T[2][2] 0.0081 _pdbx_refine_tls.T[2][2]_esd ? _pdbx_refine_tls.T[2][3] -0.0042 _pdbx_refine_tls.T[2][3]_esd ? _pdbx_refine_tls.T[3][3] 0.0248 _pdbx_refine_tls.T[3][3]_esd ? _pdbx_refine_tls.L[1][1] 0.5089 _pdbx_refine_tls.L[1][1]_esd ? _pdbx_refine_tls.L[1][2] -0.0066 _pdbx_refine_tls.L[1][2]_esd ? _pdbx_refine_tls.L[1][3] 0.2814 _pdbx_refine_tls.L[1][3]_esd ? _pdbx_refine_tls.L[2][2] 0.2068 _pdbx_refine_tls.L[2][2]_esd ? _pdbx_refine_tls.L[2][3] -0.2130 _pdbx_refine_tls.L[2][3]_esd ? _pdbx_refine_tls.L[3][3] 0.3678 _pdbx_refine_tls.L[3][3]_esd ? _pdbx_refine_tls.S[1][1] -0.0121 _pdbx_refine_tls.S[1][1]_esd ? _pdbx_refine_tls.S[1][2] -0.0414 _pdbx_refine_tls.S[1][2]_esd ? _pdbx_refine_tls.S[1][3] 0.0386 _pdbx_refine_tls.S[1][3]_esd ? _pdbx_refine_tls.S[2][1] -0.0734 _pdbx_refine_tls.S[2][1]_esd ? _pdbx_refine_tls.S[2][2] -0.0298 _pdbx_refine_tls.S[2][2]_esd ? _pdbx_refine_tls.S[2][3] -0.0256 _pdbx_refine_tls.S[2][3]_esd ? _pdbx_refine_tls.S[3][1] 0.0683 _pdbx_refine_tls.S[3][1]_esd ? _pdbx_refine_tls.S[3][2] 0.0054 _pdbx_refine_tls.S[3][2]_esd ? _pdbx_refine_tls.S[3][3] 0.0419 _pdbx_refine_tls.S[3][3]_esd ? # _pdbx_refine_tls_group.id 1 _pdbx_refine_tls_group.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine_tls_group.refine_tls_id 1 _pdbx_refine_tls_group.beg_label_asym_id ? _pdbx_refine_tls_group.beg_label_seq_id ? _pdbx_refine_tls_group.beg_auth_asym_id A _pdbx_refine_tls_group.beg_auth_seq_id 1 _pdbx_refine_tls_group.end_label_asym_id ? _pdbx_refine_tls_group.end_label_seq_id ? _pdbx_refine_tls_group.end_auth_asym_id A _pdbx_refine_tls_group.end_auth_seq_id 317 _pdbx_refine_tls_group.selection ? _pdbx_refine_tls_group.selection_details ? # loop_ _software.citation_id _software.classification _software.compiler_name _software.compiler_version _software.contact_author _software.contact_author_email _software.date _software.description _software.dependencies _software.hardware _software.language _software.location _software.mods _software.name _software.os _software.os_version _software.type _software.version _software.pdbx_ordinal ? refinement ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0103 1 ? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? CrysalisPro ? ? ? . 2 ? 'data scaling' ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? . 3 ? phasing ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? . 4 # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 OG1 A THR 21 ? ? O A HOH 901 ? ? 1.96 2 1 O A HOH 1084 ? ? O A HOH 1148 ? ? 1.96 3 1 O A HOH 1200 ? ? O A HOH 1218 ? ? 1.98 4 1 OD2 A ASP 265 ? ? O A HOH 902 ? ? 2.01 5 1 O A HOH 901 ? ? O A HOH 1036 ? ? 2.11 6 1 ND2 A ASN 74 ? ? O5 A NAG 800 ? ? 2.19 7 1 O A HOH 1018 ? ? O A HOH 1080 ? ? 2.19 # _pdbx_validate_symm_contact.id 1 _pdbx_validate_symm_contact.PDB_model_num 1 _pdbx_validate_symm_contact.auth_atom_id_1 O _pdbx_validate_symm_contact.auth_asym_id_1 A _pdbx_validate_symm_contact.auth_comp_id_1 HOH _pdbx_validate_symm_contact.auth_seq_id_1 1127 _pdbx_validate_symm_contact.PDB_ins_code_1 ? _pdbx_validate_symm_contact.label_alt_id_1 ? _pdbx_validate_symm_contact.site_symmetry_1 1_555 _pdbx_validate_symm_contact.auth_atom_id_2 O _pdbx_validate_symm_contact.auth_asym_id_2 A _pdbx_validate_symm_contact.auth_comp_id_2 HOH _pdbx_validate_symm_contact.auth_seq_id_2 1213 _pdbx_validate_symm_contact.PDB_ins_code_2 ? _pdbx_validate_symm_contact.label_alt_id_2 ? _pdbx_validate_symm_contact.site_symmetry_2 7_555 _pdbx_validate_symm_contact.dist 2.18 # loop_ _pdbx_validate_rmsd_angle.id _pdbx_validate_rmsd_angle.PDB_model_num _pdbx_validate_rmsd_angle.auth_atom_id_1 _pdbx_validate_rmsd_angle.auth_asym_id_1 _pdbx_validate_rmsd_angle.auth_comp_id_1 _pdbx_validate_rmsd_angle.auth_seq_id_1 _pdbx_validate_rmsd_angle.PDB_ins_code_1 _pdbx_validate_rmsd_angle.label_alt_id_1 _pdbx_validate_rmsd_angle.auth_atom_id_2 _pdbx_validate_rmsd_angle.auth_asym_id_2 _pdbx_validate_rmsd_angle.auth_comp_id_2 _pdbx_validate_rmsd_angle.auth_seq_id_2 _pdbx_validate_rmsd_angle.PDB_ins_code_2 _pdbx_validate_rmsd_angle.label_alt_id_2 _pdbx_validate_rmsd_angle.auth_atom_id_3 _pdbx_validate_rmsd_angle.auth_asym_id_3 _pdbx_validate_rmsd_angle.auth_comp_id_3 _pdbx_validate_rmsd_angle.auth_seq_id_3 _pdbx_validate_rmsd_angle.PDB_ins_code_3 _pdbx_validate_rmsd_angle.label_alt_id_3 _pdbx_validate_rmsd_angle.angle_value _pdbx_validate_rmsd_angle.angle_target_value _pdbx_validate_rmsd_angle.angle_deviation _pdbx_validate_rmsd_angle.angle_standard_deviation _pdbx_validate_rmsd_angle.linker_flag 1 1 NE A ARG 127 ? ? CZ A ARG 127 ? ? NH1 A ARG 127 ? ? 123.59 120.30 3.29 0.50 N 2 1 NE A ARG 127 ? ? CZ A ARG 127 ? ? NH2 A ARG 127 ? ? 116.66 120.30 -3.64 0.50 N 3 1 NE A ARG 238 ? ? CZ A ARG 238 ? ? NH1 A ARG 238 ? ? 124.08 120.30 3.78 0.50 N 4 1 NE A ARG 238 ? ? CZ A ARG 238 ? ? NH2 A ARG 238 ? ? 117.02 120.30 -3.28 0.50 N 5 1 NE A ARG 249 ? ? CZ A ARG 249 ? ? NH1 A ARG 249 ? ? 123.51 120.30 3.21 0.50 N # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 ASN A 51 ? ? -151.24 -94.67 2 1 ASP A 75 ? ? -30.58 118.57 3 1 SER A 105 ? ? 50.33 -121.66 4 1 ASP A 134 ? ? -114.71 64.54 5 1 THR A 186 ? ? -96.13 45.75 6 1 ASP A 223 ? ? -93.60 -159.48 7 1 ALA A 305 ? ? -144.02 34.39 # 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 1231 ? 6.50 . 2 1 O ? A HOH 1232 ? 6.87 . # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 water HOH #