data_4JS1 # _entry.id 4JS1 # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.287 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 4JS1 RCSB RCSB078431 WWPDB D_1000078431 # _pdbx_database_related.db_name PDB _pdbx_database_related.db_id 4JS2 _pdbx_database_related.details . _pdbx_database_related.content_type unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4JS1 _pdbx_database_status.recvd_initial_deposition_date 2013-03-22 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site PDBJ _pdbx_database_status.methods_development_category ? _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Kuhn, B.' 1 'Benz, J.' 2 'Greif, M.' 3 'Engel, A.M.' 4 'Sobek, H.' 5 'Rudolph, M.G.' 6 # _citation.id primary _citation.title 'The structure of human alpha-2,6-sialyltransferase reveals the binding mode of complex glycans' _citation.journal_abbrev 'Acta Crystallogr.,Sect.D' _citation.journal_volume 69 _citation.page_first 1826 _citation.page_last 1838 _citation.year 2013 _citation.journal_id_ASTM ABCRE6 _citation.country DK _citation.journal_id_ISSN 0907-4449 _citation.journal_id_CSD 0766 _citation.book_publisher ? _citation.pdbx_database_id_PubMed ? _citation.pdbx_database_id_DOI 10.1107/S0907444913015412 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Kuhn, B.' 1 primary 'Benz, J.' 2 primary 'Greif, M.' 3 primary 'Engel, A.M.' 4 primary 'Sobek, H.' 5 primary 'Rudolph, M.G.' 6 # _cell.entry_id 4JS1 _cell.length_a 65.292 _cell.length_b 65.292 _cell.length_c 162.232 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 120.00 _cell.Z_PDB 6 _cell.pdbx_unique_axis ? _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.entry_id 4JS1 _symmetry.space_group_name_H-M 'P 61' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 169 _symmetry.space_group_name_Hall ? # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer man 'Beta-galactoside alpha-2,6-sialyltransferase 1' 36821.906 1 2.4.99.1 ? 'catalytic domain, UNP RESIDUES 89-406' ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 4 ? ? ? ? 3 non-polymer man BETA-D-MANNOSE 180.156 1 ? ? ? ? 4 non-polymer man ALPHA-D-MANNOSE 180.156 2 ? ? ? ? 5 non-polymer man BETA-D-GALACTOSE 180.156 2 ? ? ? ? 6 non-polymer syn '4-AMINO-1-BETA-D-RIBOFURANOSYL-2(1H)-PYRIMIDINONE' 243.217 1 ? ? ? ? 7 non-polymer syn 'PHOSPHATE ION' 94.971 1 ? ? ? ? 8 water nat water 18.015 41 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name ;Alpha 2,6-ST 1, B-cell antigen CD75, CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase 1, ST6Gal I, ST6GalI, Sialyltransferase 1 ; # _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 ;PEASFQVWNKDSSSKNLIPRLQKIWKNYLSMNKYKVSYKGPGPGIKFSAEALRCHLRDHVNVSMVEVTDFPFNTSEWEGY LPKESIRTKAGPWGRCAVVSSAGSLKSSQLGREIDDHDAVLRFNGAPTANFQQDVGTKTTIRLMNSQLVTTEKRFLKDSL YNEGILIVWDPSVYHSDIPKWYQNPDYNFFNNYKTYRKLHPNQPFYILKPQMPWELWDILQEISPEEIQPNPPSSGMLGI IIMMTLCDQVDIYEFLPSKRKTDVCYYYQKFFDSACTMGAYHPLLYEKNLVKHLNQGTDEDIYLLGKATLPGFRTIHC ; _entity_poly.pdbx_seq_one_letter_code_can ;PEASFQVWNKDSSSKNLIPRLQKIWKNYLSMNKYKVSYKGPGPGIKFSAEALRCHLRDHVNVSMVEVTDFPFNTSEWEGY LPKESIRTKAGPWGRCAVVSSAGSLKSSQLGREIDDHDAVLRFNGAPTANFQQDVGTKTTIRLMNSQLVTTEKRFLKDSL YNEGILIVWDPSVYHSDIPKWYQNPDYNFFNNYKTYRKLHPNQPFYILKPQMPWELWDILQEISPEEIQPNPPSSGMLGI IIMMTLCDQVDIYEFLPSKRKTDVCYYYQKFFDSACTMGAYHPLLYEKNLVKHLNQGTDEDIYLLGKATLPGFRTIHC ; _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 PRO n 1 2 GLU n 1 3 ALA n 1 4 SER n 1 5 PHE n 1 6 GLN n 1 7 VAL n 1 8 TRP n 1 9 ASN n 1 10 LYS n 1 11 ASP n 1 12 SER n 1 13 SER n 1 14 SER n 1 15 LYS n 1 16 ASN n 1 17 LEU n 1 18 ILE n 1 19 PRO n 1 20 ARG n 1 21 LEU n 1 22 GLN n 1 23 LYS n 1 24 ILE n 1 25 TRP n 1 26 LYS n 1 27 ASN n 1 28 TYR n 1 29 LEU n 1 30 SER n 1 31 MET n 1 32 ASN n 1 33 LYS n 1 34 TYR n 1 35 LYS n 1 36 VAL n 1 37 SER n 1 38 TYR n 1 39 LYS n 1 40 GLY n 1 41 PRO n 1 42 GLY n 1 43 PRO n 1 44 GLY n 1 45 ILE n 1 46 LYS n 1 47 PHE n 1 48 SER n 1 49 ALA n 1 50 GLU n 1 51 ALA n 1 52 LEU n 1 53 ARG n 1 54 CYS n 1 55 HIS n 1 56 LEU n 1 57 ARG n 1 58 ASP n 1 59 HIS n 1 60 VAL n 1 61 ASN n 1 62 VAL n 1 63 SER n 1 64 MET n 1 65 VAL n 1 66 GLU n 1 67 VAL n 1 68 THR n 1 69 ASP n 1 70 PHE n 1 71 PRO n 1 72 PHE n 1 73 ASN n 1 74 THR n 1 75 SER n 1 76 GLU n 1 77 TRP n 1 78 GLU n 1 79 GLY n 1 80 TYR n 1 81 LEU n 1 82 PRO n 1 83 LYS n 1 84 GLU n 1 85 SER n 1 86 ILE n 1 87 ARG n 1 88 THR n 1 89 LYS n 1 90 ALA n 1 91 GLY n 1 92 PRO n 1 93 TRP n 1 94 GLY n 1 95 ARG n 1 96 CYS n 1 97 ALA n 1 98 VAL n 1 99 VAL n 1 100 SER n 1 101 SER n 1 102 ALA n 1 103 GLY n 1 104 SER n 1 105 LEU n 1 106 LYS n 1 107 SER n 1 108 SER n 1 109 GLN n 1 110 LEU n 1 111 GLY n 1 112 ARG n 1 113 GLU n 1 114 ILE n 1 115 ASP n 1 116 ASP n 1 117 HIS n 1 118 ASP n 1 119 ALA n 1 120 VAL n 1 121 LEU n 1 122 ARG n 1 123 PHE n 1 124 ASN n 1 125 GLY n 1 126 ALA n 1 127 PRO n 1 128 THR n 1 129 ALA n 1 130 ASN n 1 131 PHE n 1 132 GLN n 1 133 GLN n 1 134 ASP n 1 135 VAL n 1 136 GLY n 1 137 THR n 1 138 LYS n 1 139 THR n 1 140 THR n 1 141 ILE n 1 142 ARG n 1 143 LEU n 1 144 MET n 1 145 ASN n 1 146 SER n 1 147 GLN n 1 148 LEU n 1 149 VAL n 1 150 THR n 1 151 THR n 1 152 GLU n 1 153 LYS n 1 154 ARG n 1 155 PHE n 1 156 LEU n 1 157 LYS n 1 158 ASP n 1 159 SER n 1 160 LEU n 1 161 TYR n 1 162 ASN n 1 163 GLU n 1 164 GLY n 1 165 ILE n 1 166 LEU n 1 167 ILE n 1 168 VAL n 1 169 TRP n 1 170 ASP n 1 171 PRO n 1 172 SER n 1 173 VAL n 1 174 TYR n 1 175 HIS n 1 176 SER n 1 177 ASP n 1 178 ILE n 1 179 PRO n 1 180 LYS n 1 181 TRP n 1 182 TYR n 1 183 GLN n 1 184 ASN n 1 185 PRO n 1 186 ASP n 1 187 TYR n 1 188 ASN n 1 189 PHE n 1 190 PHE n 1 191 ASN n 1 192 ASN n 1 193 TYR n 1 194 LYS n 1 195 THR n 1 196 TYR n 1 197 ARG n 1 198 LYS n 1 199 LEU n 1 200 HIS n 1 201 PRO n 1 202 ASN n 1 203 GLN n 1 204 PRO n 1 205 PHE n 1 206 TYR n 1 207 ILE n 1 208 LEU n 1 209 LYS n 1 210 PRO n 1 211 GLN n 1 212 MET n 1 213 PRO n 1 214 TRP n 1 215 GLU n 1 216 LEU n 1 217 TRP n 1 218 ASP n 1 219 ILE n 1 220 LEU n 1 221 GLN n 1 222 GLU n 1 223 ILE n 1 224 SER n 1 225 PRO n 1 226 GLU n 1 227 GLU n 1 228 ILE n 1 229 GLN n 1 230 PRO n 1 231 ASN n 1 232 PRO n 1 233 PRO n 1 234 SER n 1 235 SER n 1 236 GLY n 1 237 MET n 1 238 LEU n 1 239 GLY n 1 240 ILE n 1 241 ILE n 1 242 ILE n 1 243 MET n 1 244 MET n 1 245 THR n 1 246 LEU n 1 247 CYS n 1 248 ASP n 1 249 GLN n 1 250 VAL n 1 251 ASP n 1 252 ILE n 1 253 TYR n 1 254 GLU n 1 255 PHE n 1 256 LEU n 1 257 PRO n 1 258 SER n 1 259 LYS n 1 260 ARG n 1 261 LYS n 1 262 THR n 1 263 ASP n 1 264 VAL n 1 265 CYS n 1 266 TYR n 1 267 TYR n 1 268 TYR n 1 269 GLN n 1 270 LYS n 1 271 PHE n 1 272 PHE n 1 273 ASP n 1 274 SER n 1 275 ALA n 1 276 CYS n 1 277 THR n 1 278 MET n 1 279 GLY n 1 280 ALA n 1 281 TYR n 1 282 HIS n 1 283 PRO n 1 284 LEU n 1 285 LEU n 1 286 TYR n 1 287 GLU n 1 288 LYS n 1 289 ASN n 1 290 LEU n 1 291 VAL n 1 292 LYS n 1 293 HIS n 1 294 LEU n 1 295 ASN n 1 296 GLN n 1 297 GLY n 1 298 THR n 1 299 ASP n 1 300 GLU n 1 301 ASP n 1 302 ILE n 1 303 TYR n 1 304 LEU n 1 305 LEU n 1 306 GLY n 1 307 LYS n 1 308 ALA n 1 309 THR n 1 310 LEU n 1 311 PRO n 1 312 GLY n 1 313 PHE n 1 314 ARG n 1 315 THR n 1 316 ILE n 1 317 HIS n 1 318 CYS n # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _entity_src_gen.pdbx_seq_type ? _entity_src_gen.pdbx_beg_seq_num ? _entity_src_gen.pdbx_end_seq_num ? _entity_src_gen.gene_src_common_name human _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene 'ST6GAL1, SIAT1' _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 'Homo sapiens' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 9606 _entity_src_gen.pdbx_gene_src_variant ? _entity_src_gen.pdbx_gene_src_cell_line ? _entity_src_gen.pdbx_gene_src_atcc ? _entity_src_gen.pdbx_gene_src_organ ? _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 human _entity_src_gen.pdbx_host_org_scientific_name 'Homo sapiens' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 9606 _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 'HEK 293' _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 SIAT1_HUMAN _struct_ref.pdbx_db_accession P15907 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;PEASFQVWNKDSSSKNLIPRLQKIWKNYLSMNKYKVSYKGPGPGIKFSAEALRCHLRDHVNVSMVEVTDFPFNTSEWEGY LPKESIRTKAGPWGRCAVVSSAGSLKSSQLGREIDDHDAVLRFNGAPTANFQQDVGTKTTIRLMNSQLVTTEKRFLKDSL YNEGILIVWDPSVYHSDIPKWYQNPDYNFFNNYKTYRKLHPNQPFYILKPQMPWELWDILQEISPEEIQPNPPSSGMLGI IIMMTLCDQVDIYEFLPSKRKTDVCYYYQKFFDSACTMGAYHPLLYEKNLVKHLNQGTDEDIYLLGKATLPGFRTIHC ; _struct_ref.pdbx_align_begin 89 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 4JS1 _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 318 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession P15907 _struct_ref_seq.db_align_beg 89 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 406 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 89 _struct_ref_seq.pdbx_auth_seq_align_end 406 # 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 BMA D-saccharide . BETA-D-MANNOSE ? 'C6 H12 O6' 180.156 CTN non-polymer . '4-AMINO-1-BETA-D-RIBOFURANOSYL-2(1H)-PYRIMIDINONE' CYTIDINE 'C9 H13 N3 O5' 243.217 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GAL D-saccharide . BETA-D-GALACTOSE ? 'C6 H12 O6' 180.156 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MAN D-saccharide . ALPHA-D-MANNOSE ? 'C6 H12 O6' 180.156 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PO4 non-polymer . 'PHOSPHATE ION' ? 'O4 P -3' 94.971 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 4JS1 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.71 _exptl_crystal.density_percent_sol 54.63 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, SITTING DROP' _exptl_crystal_grow.temp 294 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 5.8 _exptl_crystal_grow.pdbx_details '0.1M MES/NaOH, pH 5.8, 20% PEG 2000 MME, 0.01M CaCl2, 0.01M MgCl2, VAPOR DIFFUSION, SITTING DROP, temperature 294K' _exptl_crystal_grow.pdbx_pH_range ? # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector PIXEL _diffrn_detector.type 'DECTRIS PILATUS 6M' _diffrn_detector.pdbx_collection_date 2012-11-12 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'SLS BEAMLINE X10SA' _diffrn_source.pdbx_synchrotron_site SLS _diffrn_source.pdbx_synchrotron_beamline X10SA _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 1 # _reflns.entry_id 4JS1 _reflns.observed_criterion_sigma_I 0 _reflns.observed_criterion_sigma_F 0 _reflns.d_resolution_low 46.4 _reflns.d_resolution_high 2.09 _reflns.number_obs 22378 _reflns.number_all ? _reflns.percent_possible_obs 99.4 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 13.5 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 9.9 _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _reflns_shell.d_res_high 2.09 _reflns_shell.d_res_low 2.16 _reflns_shell.percent_possible_all 99.4 _reflns_shell.Rmerge_I_obs ? _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 1.3 _reflns_shell.pdbx_redundancy 10.2 _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all 2292 _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_rejects ? _reflns_shell.pdbx_netI_over_sigmaI_obs ? _reflns_shell.number_possible ? _reflns_shell.Rmerge_F_all ? _reflns_shell.Rmerge_F_obs ? _reflns_shell.Rmerge_I_all ? _reflns_shell.meanI_over_sigI_all ? _reflns_shell.pdbx_Rrim_I_all ? _reflns_shell.pdbx_Rpim_I_all ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 # _refine.entry_id 4JS1 _refine.ls_number_reflns_obs 22159 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 1.35 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 46.387 _refine.ls_d_res_high 2.090 _refine.ls_percent_reflns_obs 95.85 _refine.ls_R_factor_obs 0.1953 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.1934 _refine.ls_R_factor_R_free 0.2282 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.16 _refine.ls_number_reflns_R_free 1143 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.B_iso_mean ? _refine.aniso_B[1][1] ? _refine.aniso_B[2][2] ? _refine.aniso_B[3][3] ? _refine.aniso_B[1][2] ? _refine.aniso_B[1][3] ? _refine.aniso_B[2][3] ? _refine.solvent_model_details 'FLAT BULK SOLVENT MODEL' _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.11 _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii 0.90 _refine.pdbx_ls_cross_valid_method ? _refine.details ? _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct SIRAS _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values ML _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details random _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML 0.24 _refine.pdbx_overall_phase_error 34.08 _refine.overall_SU_B ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_diffrn_id 1 _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 2594 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 133 _refine_hist.number_atoms_solvent 41 _refine_hist.number_atoms_total 2768 _refine_hist.d_res_high 2.090 _refine_hist.d_res_low 46.387 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_restraint_function _refine_ls_restr.pdbx_refine_id f_bond_d 0.009 ? ? 2816 ? 'X-RAY DIFFRACTION' f_angle_d 1.252 ? ? 3835 ? 'X-RAY DIFFRACTION' f_dihedral_angle_d 25.993 ? ? 1087 ? 'X-RAY DIFFRACTION' f_chiral_restr 0.081 ? ? 428 ? 'X-RAY DIFFRACTION' f_plane_restr 0.005 ? ? 472 ? 'X-RAY DIFFRACTION' # loop_ _refine_ls_shell.pdbx_refine_id _refine_ls_shell.pdbx_total_number_of_bins_used _refine_ls_shell.d_res_high _refine_ls_shell.d_res_low _refine_ls_shell.number_reflns_R_work _refine_ls_shell.R_factor_R_work _refine_ls_shell.percent_reflns_obs _refine_ls_shell.R_factor_R_free _refine_ls_shell.R_factor_R_free_error _refine_ls_shell.percent_reflns_R_free _refine_ls_shell.number_reflns_R_free _refine_ls_shell.number_reflns_all _refine_ls_shell.R_factor_all _refine_ls_shell.number_reflns_obs _refine_ls_shell.redundancy_reflns_obs 'X-RAY DIFFRACTION' 8 2.0901 2.1852 2712 0.3319 99.00 0.3733 . . 128 . . 2712 . 'X-RAY DIFFRACTION' 8 2.1852 2.3005 1973 0.3417 72.00 0.4374 . . 104 . . 1973 . 'X-RAY DIFFRACTION' 8 2.3005 2.4446 2707 0.2848 99.00 0.3579 . . 145 . . 2707 . 'X-RAY DIFFRACTION' 8 2.4446 2.6333 2741 0.2750 99.00 0.3203 . . 136 . . 2741 . 'X-RAY DIFFRACTION' 8 2.6333 2.8983 2688 0.2446 99.00 0.2962 . . 161 . . 2688 . 'X-RAY DIFFRACTION' 8 2.8983 3.3176 2751 0.2264 100.00 0.3006 . . 145 . . 2751 . 'X-RAY DIFFRACTION' 8 3.3176 4.1794 2681 0.1783 99.00 0.2185 . . 169 . . 2681 . 'X-RAY DIFFRACTION' 8 4.1794 46.3980 2763 0.1415 100.00 0.1562 . . 155 . . 2763 . # _struct.entry_id 4JS1 _struct.title 'crystal structure of human Beta-galactoside alpha-2,6-sialyltransferase 1 in complex with cytidine and phosphate' _struct.pdbx_descriptor 'Beta-galactoside alpha-2,6-sialyltransferase 1 (E.C.2.4.99.1)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4JS1 _struct_keywords.pdbx_keywords TRANSFERASE _struct_keywords.text 'Rossmann, GT-A, sialyltransferase, glycoprotein, sialylation, endoplasmatic reticulum, golgi, TRANSFERASE' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 2 ? D N N 3 ? E N N 4 ? F N N 2 ? G N N 5 ? H N N 4 ? I N N 2 ? J N N 5 ? K N N 6 ? L N N 7 ? M N N 8 ? # _struct_biol.id 1 _struct_biol.details ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 SER A 13 ? LEU A 17 ? SER A 101 LEU A 105 5 ? 5 HELX_P HELX_P2 2 ILE A 18 ? MET A 31 ? ILE A 106 MET A 119 1 ? 14 HELX_P HELX_P3 3 SER A 48 ? VAL A 60 ? SER A 136 VAL A 148 1 ? 13 HELX_P HELX_P4 4 THR A 74 ? GLU A 78 ? THR A 162 GLU A 166 5 ? 5 HELX_P HELX_P5 5 SER A 85 ? ALA A 90 ? SER A 173 ALA A 178 1 ? 6 HELX_P HELX_P6 6 ALA A 102 ? LYS A 106 ? ALA A 190 LYS A 194 5 ? 5 HELX_P HELX_P7 7 LEU A 110 ? ASP A 115 ? LEU A 198 ASP A 203 1 ? 6 HELX_P HELX_P8 8 PHE A 131 ? GLY A 136 ? PHE A 219 GLY A 224 1 ? 6 HELX_P HELX_P9 9 SER A 146 ? GLU A 152 ? SER A 234 GLU A 240 1 ? 7 HELX_P HELX_P10 10 LYS A 153 ? LYS A 157 ? LYS A 241 LYS A 245 5 ? 5 HELX_P HELX_P11 11 ASP A 158 ? GLU A 163 ? ASP A 246 GLU A 251 5 ? 6 HELX_P HELX_P12 12 ASP A 177 ? ASN A 184 ? ASP A 265 ASN A 272 1 ? 8 HELX_P HELX_P13 13 PHE A 189 ? HIS A 200 ? PHE A 277 HIS A 288 1 ? 12 HELX_P HELX_P14 14 PRO A 210 ? SER A 224 ? PRO A 298 SER A 312 1 ? 15 HELX_P HELX_P15 15 SER A 234 ? LEU A 246 ? SER A 322 LEU A 334 1 ? 13 HELX_P HELX_P16 16 SER A 274 ? GLY A 279 ? SER A 362 GLY A 367 1 ? 6 HELX_P HELX_P17 17 PRO A 283 ? ASN A 295 ? PRO A 371 ASN A 383 1 ? 13 HELX_P HELX_P18 18 THR A 298 ? GLY A 306 ? THR A 386 GLY A 394 1 ? 9 HELX_P HELX_P19 19 PHE A 313 ? ILE A 316 ? PHE A 401 ILE A 404 5 ? 4 # _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 96 SG ? ? ? 1_555 A CYS 247 SG ? ? A CYS 184 A CYS 335 1_555 ? ? ? ? ? ? ? 2.039 ? disulf2 disulf ? ? A CYS 265 SG ? ? ? 1_555 A CYS 276 SG ? ? A CYS 353 A CYS 364 1_555 ? ? ? ? ? ? ? 2.043 ? covale1 covale ? ? D BMA . O3 ? ? ? 1_555 E MAN . C1 ? ? A BMA 503 A MAN 504 1_555 ? ? ? ? ? ? ? 1.437 ? covale2 covale ? ? D BMA . O6 ? ? ? 1_555 H MAN . C1 ? ? A BMA 503 A MAN 507 1_555 ? ? ? ? ? ? ? 1.438 ? covale3 covale ? ? C NAG . O4 ? ? ? 1_555 D BMA . C1 ? ? A NAG 502 A BMA 503 1_555 ? ? ? ? ? ? ? 1.439 ? covale4 covale ? ? E MAN . O2 ? ? ? 1_555 F NAG . C1 ? ? A MAN 504 A NAG 505 1_555 ? ? ? ? ? ? ? 1.439 ? covale5 covale ? ? B NAG . O4 ? ? ? 1_555 C NAG . C1 ? ? A NAG 501 A NAG 502 1_555 ? ? ? ? ? ? ? 1.439 ? covale6 covale ? ? F NAG . O4 ? ? ? 1_555 G GAL . C1 ? ? A NAG 505 A GAL 506 1_555 ? ? ? ? ? ? ? 1.440 ? covale7 covale ? ? H MAN . O2 ? ? ? 1_555 I NAG . C1 ? ? A MAN 507 A NAG 508 1_555 ? ? ? ? ? ? ? 1.442 ? covale8 covale ? ? A ASN 61 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 149 A NAG 501 1_555 ? ? ? ? ? ? ? 1.443 ? covale9 covale ? ? I NAG . O4 ? ? ? 1_555 J GAL . C1 ? ? A NAG 508 A GAL 509 1_555 ? ? ? ? ? ? ? 1.448 ? # 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 PHE 70 A . ? PHE 158 A PRO 71 A ? PRO 159 A 1 5.26 2 GLY 91 A . ? GLY 179 A PRO 92 A ? PRO 180 A 1 7.24 # _struct_sheet.id A _struct_sheet.type ? _struct_sheet.number_strands 7 _struct_sheet.details ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? parallel A 2 3 ? parallel A 3 4 ? parallel A 4 5 ? parallel A 5 6 ? parallel A 6 7 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 PHE A 205 ? ILE A 207 ? PHE A 293 ILE A 295 A 2 ILE A 165 ? TRP A 169 ? ILE A 253 TRP A 257 A 3 ILE A 141 ? ASN A 145 ? ILE A 229 ASN A 233 A 4 ALA A 119 ? PHE A 123 ? ALA A 207 PHE A 211 A 5 TRP A 93 ? VAL A 99 ? TRP A 181 VAL A 187 A 6 CYS A 247 ? TYR A 253 ? CYS A 335 TYR A 341 A 7 LYS A 307 ? PRO A 311 ? LYS A 395 PRO A 399 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 O TYR A 206 ? O TYR A 294 N LEU A 166 ? N LEU A 254 A 2 3 O ILE A 165 ? O ILE A 253 N ARG A 142 ? N ARG A 230 A 3 4 O LEU A 143 ? O LEU A 231 N ARG A 122 ? N ARG A 210 A 4 5 O LEU A 121 ? O LEU A 209 N VAL A 99 ? N VAL A 187 A 5 6 N CYS A 96 ? N CYS A 184 O ASP A 251 ? O ASP A 339 A 6 7 N VAL A 250 ? N VAL A 338 O LEU A 310 ? O LEU A 398 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 15 'BINDING SITE FOR RESIDUE CTN A 510' AC2 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE PO4 A 511' AC3 Software ? ? ? ? 25 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 149 RESIDUES 501 TO 509' # 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 15 SER A 101 ? SER A 189 . ? 1_555 ? 2 AC1 15 ALA A 102 ? ALA A 190 . ? 1_555 ? 3 AC1 15 PHE A 123 ? PHE A 211 . ? 1_555 ? 4 AC1 15 SER A 234 ? SER A 322 . ? 1_555 ? 5 AC1 15 SER A 235 ? SER A 323 . ? 1_555 ? 6 AC1 15 GLY A 236 ? GLY A 324 . ? 1_555 ? 7 AC1 15 PHE A 255 ? PHE A 343 . ? 1_555 ? 8 AC1 15 CYS A 265 ? CYS A 353 . ? 1_555 ? 9 AC1 15 CYS A 276 ? CYS A 364 . ? 1_555 ? 10 AC1 15 THR A 277 ? THR A 365 . ? 1_555 ? 11 AC1 15 LYS A 288 ? LYS A 376 . ? 1_555 ? 12 AC1 15 PO4 L . ? PO4 A 511 . ? 1_555 ? 13 AC1 15 HOH M . ? HOH A 607 . ? 1_555 ? 14 AC1 15 HOH M . ? HOH A 623 . ? 1_555 ? 15 AC1 15 HOH M . ? HOH A 634 . ? 1_555 ? 16 AC2 7 ASN A 124 ? ASN A 212 . ? 1_555 ? 17 AC2 7 ASN A 145 ? ASN A 233 . ? 1_555 ? 18 AC2 7 SER A 234 ? SER A 322 . ? 1_555 ? 19 AC2 7 SER A 235 ? SER A 323 . ? 1_555 ? 20 AC2 7 HIS A 282 ? HIS A 370 . ? 1_555 ? 21 AC2 7 GAL G . ? GAL A 506 . ? 6_665 ? 22 AC2 7 CTN K . ? CTN A 510 . ? 1_555 ? 23 AC3 25 ARG A 20 ? ARG A 108 . ? 5_454 ? 24 AC3 25 ILE A 24 ? ILE A 112 . ? 5_454 ? 25 AC3 25 TYR A 28 ? TYR A 116 . ? 5_454 ? 26 AC3 25 HIS A 59 ? HIS A 147 . ? 1_555 ? 27 AC3 25 ASN A 61 ? ASN A 149 . ? 1_555 ? 28 AC3 25 ARG A 112 ? ARG A 200 . ? 3_564 ? 29 AC3 25 ASN A 145 ? ASN A 233 . ? 5_454 ? 30 AC3 25 GLN A 147 ? GLN A 235 . ? 5_454 ? 31 AC3 25 ARG A 154 ? ARG A 242 . ? 5_454 ? 32 AC3 25 PRO A 171 ? PRO A 259 . ? 5_454 ? 33 AC3 25 ASP A 186 ? ASP A 274 . ? 5_454 ? 34 AC3 25 TYR A 187 ? TYR A 275 . ? 5_454 ? 35 AC3 25 TYR A 268 ? TYR A 356 . ? 5_454 ? 36 AC3 25 GLN A 269 ? GLN A 357 . ? 5_454 ? 37 AC3 25 LYS A 270 ? LYS A 358 . ? 5_454 ? 38 AC3 25 PHE A 271 ? PHE A 359 . ? 5_454 ? 39 AC3 25 PHE A 272 ? PHE A 360 . ? 5_454 ? 40 AC3 25 ASP A 273 ? ASP A 361 . ? 5_454 ? 41 AC3 25 ALA A 275 ? ALA A 363 . ? 5_454 ? 42 AC3 25 ALA A 280 ? ALA A 368 . ? 5_454 ? 43 AC3 25 TYR A 281 ? TYR A 369 . ? 5_454 ? 44 AC3 25 HIS A 282 ? HIS A 370 . ? 5_454 ? 45 AC3 25 PO4 L . ? PO4 A 511 . ? 5_454 ? 46 AC3 25 HOH M . ? HOH A 608 . ? 5_454 ? 47 AC3 25 HOH M . ? HOH A 612 . ? 5_454 ? # _database_PDB_matrix.entry_id 4JS1 _database_PDB_matrix.origx[1][1] 1.000000 _database_PDB_matrix.origx[1][2] 0.000000 _database_PDB_matrix.origx[1][3] 0.000000 _database_PDB_matrix.origx[2][1] 0.000000 _database_PDB_matrix.origx[2][2] 1.000000 _database_PDB_matrix.origx[2][3] 0.000000 _database_PDB_matrix.origx[3][1] 0.000000 _database_PDB_matrix.origx[3][2] 0.000000 _database_PDB_matrix.origx[3][3] 1.000000 _database_PDB_matrix.origx_vector[1] 0.00000 _database_PDB_matrix.origx_vector[2] 0.00000 _database_PDB_matrix.origx_vector[3] 0.00000 # _atom_sites.entry_id 4JS1 _atom_sites.fract_transf_matrix[1][1] 0.015316 _atom_sites.fract_transf_matrix[1][2] 0.008843 _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] 0.017685 _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] 0.006164 _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 P 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 . PRO A 1 1 ? -18.044 40.681 65.686 1.00 172.52 ? 89 PRO A N 1 ATOM 2 C CA . PRO A 1 1 ? -18.620 41.288 64.485 1.00 168.62 ? 89 PRO A CA 1 ATOM 3 C C . PRO A 1 1 ? -17.661 41.222 63.289 1.00 162.86 ? 89 PRO A C 1 ATOM 4 O O . PRO A 1 1 ? -16.553 40.703 63.402 1.00 157.37 ? 89 PRO A O 1 ATOM 5 C CB . PRO A 1 1 ? -18.860 42.737 64.916 1.00 163.05 ? 89 PRO A CB 1 ATOM 6 C CG . PRO A 1 1 ? -17.830 42.990 65.944 1.00 163.74 ? 89 PRO A CG 1 ATOM 7 C CD . PRO A 1 1 ? -17.636 41.695 66.672 1.00 171.85 ? 89 PRO A CD 1 ATOM 8 N N . GLU A 1 2 ? -18.087 41.735 62.144 1.00 152.13 ? 90 GLU A N 1 ATOM 9 C CA . GLU A 1 2 ? -17.232 41.692 60.964 1.00 144.67 ? 90 GLU A CA 1 ATOM 10 C C . GLU A 1 2 ? -16.566 43.034 60.687 1.00 136.64 ? 90 GLU A C 1 ATOM 11 O O . GLU A 1 2 ? -17.194 44.089 60.763 1.00 135.11 ? 90 GLU A O 1 ATOM 12 C CB . GLU A 1 2 ? -17.996 41.146 59.754 1.00 144.11 ? 90 GLU A CB 1 ATOM 13 C CG . GLU A 1 2 ? -18.329 39.660 59.906 1.00 163.80 ? 90 GLU A CG 1 ATOM 14 C CD . GLU A 1 2 ? -19.359 39.163 58.911 1.00 165.36 ? 90 GLU A CD 1 ATOM 15 O OE1 . GLU A 1 2 ? -19.528 39.818 57.861 1.00 159.78 ? 90 GLU A OE1 1 ATOM 16 O OE2 . GLU A 1 2 ? -19.999 38.119 59.181 1.00 161.27 ? 90 GLU A OE2 1 ATOM 17 N N . ALA A 1 3 ? -15.274 42.971 60.389 1.00 132.16 ? 91 ALA A N 1 ATOM 18 C CA . ALA A 1 3 ? -14.440 44.154 60.221 1.00 125.40 ? 91 ALA A CA 1 ATOM 19 C C . ALA A 1 3 ? -14.817 44.976 58.995 1.00 129.59 ? 91 ALA A C 1 ATOM 20 O O . ALA A 1 3 ? -15.176 44.426 57.957 1.00 117.51 ? 91 ALA A O 1 ATOM 21 C CB . ALA A 1 3 ? -12.979 43.752 60.148 1.00 123.17 ? 91 ALA A CB 1 ATOM 22 N N . SER A 1 4 ? -14.741 46.295 59.136 1.00 115.36 ? 92 SER A N 1 ATOM 23 C CA . SER A 1 4 ? -15.010 47.201 58.032 1.00 109.49 ? 92 SER A CA 1 ATOM 24 C C . SER A 1 4 ? -13.735 47.907 57.618 1.00 103.23 ? 92 SER A C 1 ATOM 25 O O . SER A 1 4 ? -13.082 48.566 58.421 1.00 103.19 ? 92 SER A O 1 ATOM 26 C CB . SER A 1 4 ? -16.069 48.233 58.404 1.00 117.92 ? 92 SER A CB 1 ATOM 27 O OG . SER A 1 4 ? -15.475 49.387 58.975 1.00 119.01 ? 92 SER A OG 1 ATOM 28 N N . PHE A 1 5 ? -13.389 47.752 56.345 1.00 98.37 ? 93 PHE A N 1 ATOM 29 C CA . PHE A 1 5 ? -12.206 48.374 55.775 1.00 99.07 ? 93 PHE A CA 1 ATOM 30 C C . PHE A 1 5 ? -12.372 48.433 54.266 1.00 92.53 ? 93 PHE A C 1 ATOM 31 O O . PHE A 1 5 ? -13.266 47.795 53.712 1.00 91.96 ? 93 PHE A O 1 ATOM 32 C CB . PHE A 1 5 ? -10.960 47.568 56.118 1.00 93.26 ? 93 PHE A CB 1 ATOM 33 C CG . PHE A 1 5 ? -11.030 46.133 55.678 1.00 95.38 ? 93 PHE A CG 1 ATOM 34 C CD1 . PHE A 1 5 ? -11.686 45.185 56.452 1.00 101.90 ? 93 PHE A CD1 1 ATOM 35 C CD2 . PHE A 1 5 ? -10.444 45.729 54.493 1.00 91.35 ? 93 PHE A CD2 1 ATOM 36 C CE1 . PHE A 1 5 ? -11.755 43.874 56.053 1.00 104.46 ? 93 PHE A CE1 1 ATOM 37 C CE2 . PHE A 1 5 ? -10.512 44.419 54.091 1.00 93.67 ? 93 PHE A CE2 1 ATOM 38 C CZ . PHE A 1 5 ? -11.167 43.487 54.879 1.00 100.33 ? 93 PHE A CZ 1 ATOM 39 N N . GLN A 1 6 ? -11.500 49.179 53.597 1.00 95.78 ? 94 GLN A N 1 ATOM 40 C CA . GLN A 1 6 ? -11.641 49.353 52.157 1.00 98.05 ? 94 GLN A CA 1 ATOM 41 C C . GLN A 1 6 ? -10.531 48.700 51.333 1.00 97.86 ? 94 GLN A C 1 ATOM 42 O O . GLN A 1 6 ? -9.347 48.945 51.559 1.00 73.33 ? 94 GLN A O 1 ATOM 43 C CB . GLN A 1 6 ? -11.776 50.835 51.805 1.00 101.81 ? 94 GLN A CB 1 ATOM 44 C CG . GLN A 1 6 ? -12.952 51.517 52.501 1.00 113.73 ? 94 GLN A CG 1 ATOM 45 C CD . GLN A 1 6 ? -13.725 52.442 51.576 1.00 118.28 ? 94 GLN A CD 1 ATOM 46 O OE1 . GLN A 1 6 ? -13.442 52.520 50.379 1.00 120.17 ? 94 GLN A OE1 1 ATOM 47 N NE2 . GLN A 1 6 ? -14.709 53.147 52.129 1.00 121.10 ? 94 GLN A NE2 1 ATOM 48 N N . VAL A 1 7 ? -10.940 47.841 50.403 1.00 74.83 ? 95 VAL A N 1 ATOM 49 C CA . VAL A 1 7 ? -10.050 47.308 49.367 1.00 76.45 ? 95 VAL A CA 1 ATOM 50 C C . VAL A 1 7 ? -10.626 47.708 48.023 1.00 72.36 ? 95 VAL A C 1 ATOM 51 O O . VAL A 1 7 ? -11.776 48.149 47.967 1.00 72.61 ? 95 VAL A O 1 ATOM 52 C CB . VAL A 1 7 ? -9.917 45.773 49.441 1.00 78.07 ? 95 VAL A CB 1 ATOM 53 C CG1 . VAL A 1 7 ? -9.272 45.370 50.750 1.00 78.49 ? 95 VAL A CG1 1 ATOM 54 C CG2 . VAL A 1 7 ? -11.275 45.100 49.269 1.00 81.69 ? 95 VAL A CG2 1 ATOM 55 N N . TRP A 1 8 ? -9.835 47.569 46.955 1.00 68.60 ? 96 TRP A N 1 ATOM 56 C CA . TRP A 1 8 ? -10.259 47.987 45.624 1.00 67.08 ? 96 TRP A CA 1 ATOM 57 C C . TRP A 1 8 ? -11.704 47.609 45.293 1.00 72.47 ? 96 TRP A C 1 ATOM 58 O O . TRP A 1 8 ? -12.164 46.485 45.542 1.00 71.28 ? 96 TRP A O 1 ATOM 59 C CB . TRP A 1 8 ? -9.305 47.469 44.543 1.00 69.39 ? 96 TRP A CB 1 ATOM 60 C CG . TRP A 1 8 ? -9.543 48.103 43.200 1.00 69.09 ? 96 TRP A CG 1 ATOM 61 C CD1 . TRP A 1 8 ? -10.452 47.713 42.269 1.00 70.97 ? 96 TRP A CD1 1 ATOM 62 C CD2 . TRP A 1 8 ? -8.882 49.255 42.656 1.00 69.09 ? 96 TRP A CD2 1 ATOM 63 N NE1 . TRP A 1 8 ? -10.403 48.539 41.179 1.00 72.15 ? 96 TRP A NE1 1 ATOM 64 C CE2 . TRP A 1 8 ? -9.444 49.495 41.387 1.00 69.94 ? 96 TRP A CE2 1 ATOM 65 C CE3 . TRP A 1 8 ? -7.868 50.102 43.117 1.00 68.40 ? 96 TRP A CE3 1 ATOM 66 C CZ2 . TRP A 1 8 ? -9.022 50.540 40.565 1.00 63.20 ? 96 TRP A CZ2 1 ATOM 67 C CZ3 . TRP A 1 8 ? -7.454 51.145 42.304 1.00 66.27 ? 96 TRP A CZ3 1 ATOM 68 C CH2 . TRP A 1 8 ? -8.030 51.354 41.036 1.00 61.83 ? 96 TRP A CH2 1 ATOM 69 N N . ASN A 1 9 ? -12.419 48.592 44.765 1.00 78.02 ? 97 ASN A N 1 ATOM 70 C CA . ASN A 1 9 ? -13.799 48.432 44.343 1.00 79.90 ? 97 ASN A CA 1 ATOM 71 C C . ASN A 1 9 ? -13.834 47.972 42.882 1.00 78.06 ? 97 ASN A C 1 ATOM 72 O O . ASN A 1 9 ? -13.467 48.726 41.994 1.00 69.49 ? 97 ASN A O 1 ATOM 73 C CB . ASN A 1 9 ? -14.516 49.774 44.514 1.00 79.38 ? 97 ASN A CB 1 ATOM 74 C CG . ASN A 1 9 ? -15.844 49.840 43.786 1.00 83.93 ? 97 ASN A CG 1 ATOM 75 O OD1 . ASN A 1 9 ? -16.522 48.827 43.604 1.00 89.67 ? 97 ASN A OD1 1 ATOM 76 N ND2 . ASN A 1 9 ? -16.228 51.048 43.372 1.00 81.90 ? 97 ASN A ND2 1 ATOM 77 N N . LYS A 1 10 ? -14.289 46.741 42.653 1.00 86.88 ? 98 LYS A N 1 ATOM 78 C CA . LYS A 1 10 ? -14.352 46.118 41.320 1.00 82.55 ? 98 LYS A CA 1 ATOM 79 C C . LYS A 1 10 ? -15.116 46.915 40.271 1.00 76.50 ? 98 LYS A C 1 ATOM 80 O O . LYS A 1 10 ? -14.950 46.694 39.078 1.00 80.12 ? 98 LYS A O 1 ATOM 81 C CB . LYS A 1 10 ? -15.035 44.755 41.426 1.00 90.04 ? 98 LYS A CB 1 ATOM 82 C CG . LYS A 1 10 ? -14.112 43.567 41.504 1.00 91.35 ? 98 LYS A CG 1 ATOM 83 C CD . LYS A 1 10 ? -14.927 42.275 41.639 1.00 98.61 ? 98 LYS A CD 1 ATOM 84 C CE . LYS A 1 10 ? -15.740 42.238 42.916 1.00 102.29 ? 98 LYS A CE 1 ATOM 85 N NZ . LYS A 1 10 ? -16.397 40.911 43.104 1.00 107.03 ? 98 LYS A NZ 1 ATOM 86 N N . ASP A 1 11 ? -15.993 47.807 40.708 1.00 78.20 ? 99 ASP A N 1 ATOM 87 C CA . ASP A 1 11 ? -16.819 48.548 39.767 1.00 78.37 ? 99 ASP A CA 1 ATOM 88 C C . ASP A 1 11 ? -16.398 50.002 39.678 1.00 72.24 ? 99 ASP A C 1 ATOM 89 O O . ASP A 1 11 ? -17.222 50.908 39.526 1.00 75.84 ? 99 ASP A O 1 ATOM 90 C CB . ASP A 1 11 ? -18.297 48.409 40.126 1.00 87.02 ? 99 ASP A CB 1 ATOM 91 C CG . ASP A 1 11 ? -18.903 47.133 39.571 1.00 99.27 ? 99 ASP A CG 1 ATOM 92 O OD1 . ASP A 1 11 ? -18.599 46.804 38.396 1.00 106.95 ? 99 ASP A OD1 1 ATOM 93 O OD2 . ASP A 1 11 ? -19.665 46.456 40.301 1.00 95.10 ? 99 ASP A OD2 1 ATOM 94 N N . SER A 1 12 ? -15.099 50.222 39.788 1.00 70.05 ? 100 SER A N 1 ATOM 95 C CA . SER A 1 12 ? -14.569 51.564 39.665 1.00 74.67 ? 100 SER A CA 1 ATOM 96 C C . SER A 1 12 ? -14.793 52.074 38.251 1.00 73.84 ? 100 SER A C 1 ATOM 97 O O . SER A 1 12 ? -14.616 51.334 37.277 1.00 70.04 ? 100 SER A O 1 ATOM 98 C CB . SER A 1 12 ? -13.087 51.585 40.032 1.00 68.75 ? 100 SER A CB 1 ATOM 99 O OG . SER A 1 12 ? -12.924 51.194 41.389 1.00 69.68 ? 100 SER A OG 1 ATOM 100 N N . SER A 1 13 ? -15.219 53.331 38.149 1.00 76.72 ? 101 SER A N 1 ATOM 101 C CA . SER A 1 13 ? -15.432 53.986 36.862 1.00 80.59 ? 101 SER A CA 1 ATOM 102 C C . SER A 1 13 ? -14.768 55.341 36.936 1.00 73.64 ? 101 SER A C 1 ATOM 103 O O . SER A 1 13 ? -14.231 55.715 37.976 1.00 68.62 ? 101 SER A O 1 ATOM 104 C CB . SER A 1 13 ? -16.927 54.187 36.586 1.00 89.12 ? 101 SER A CB 1 ATOM 105 O OG . SER A 1 13 ? -17.705 53.105 37.071 1.00 96.03 ? 101 SER A OG 1 ATOM 106 N N . SER A 1 14 ? -14.821 56.085 35.842 1.00 70.60 ? 102 SER A N 1 ATOM 107 C CA . SER A 1 14 ? -14.324 57.453 35.833 1.00 71.21 ? 102 SER A CA 1 ATOM 108 C C . SER A 1 14 ? -15.068 58.339 36.841 1.00 76.26 ? 102 SER A C 1 ATOM 109 O O . SER A 1 14 ? -14.502 59.283 37.399 1.00 72.01 ? 102 SER A O 1 ATOM 110 C CB . SER A 1 14 ? -14.447 58.038 34.423 1.00 75.25 ? 102 SER A CB 1 ATOM 111 O OG . SER A 1 14 ? -15.781 57.950 33.940 1.00 79.85 ? 102 SER A OG 1 ATOM 112 N N . LYS A 1 15 ? -16.337 58.042 37.087 1.00 80.21 ? 103 LYS A N 1 ATOM 113 C CA . LYS A 1 15 ? -17.106 58.881 38.006 1.00 86.65 ? 103 LYS A CA 1 ATOM 114 C C . LYS A 1 15 ? -16.662 58.754 39.467 1.00 84.54 ? 103 LYS A C 1 ATOM 115 O O . LYS A 1 15 ? -17.025 59.577 40.304 1.00 82.79 ? 103 LYS A O 1 ATOM 116 C CB . LYS A 1 15 ? -18.611 58.670 37.835 1.00 96.70 ? 103 LYS A CB 1 ATOM 117 C CG . LYS A 1 15 ? -19.097 59.167 36.479 1.00 109.73 ? 103 LYS A CG 1 ATOM 118 C CD . LYS A 1 15 ? -20.518 59.702 36.529 1.00 121.02 ? 103 LYS A CD 1 ATOM 119 C CE . LYS A 1 15 ? -20.883 60.371 35.207 1.00 125.19 ? 103 LYS A CE 1 ATOM 120 N NZ . LYS A 1 15 ? -22.319 60.765 35.153 1.00 132.92 ? 103 LYS A NZ 1 ATOM 121 N N . ASN A 1 16 ? -15.849 57.740 39.757 1.00 80.64 ? 104 ASN A N 1 ATOM 122 C CA . ASN A 1 16 ? -15.236 57.596 41.077 1.00 73.13 ? 104 ASN A CA 1 ATOM 123 C C . ASN A 1 16 ? -13.949 58.404 41.213 1.00 70.12 ? 104 ASN A C 1 ATOM 124 O O . ASN A 1 16 ? -13.491 58.662 42.323 1.00 72.52 ? 104 ASN A O 1 ATOM 125 C CB . ASN A 1 16 ? -14.944 56.124 41.385 1.00 62.73 ? 104 ASN A CB 1 ATOM 126 C CG . ASN A 1 16 ? -16.178 55.254 41.294 1.00 69.28 ? 104 ASN A CG 1 ATOM 127 O OD1 . ASN A 1 16 ? -16.255 54.345 40.469 1.00 76.74 ? 104 ASN A OD1 1 ATOM 128 N ND2 . ASN A 1 16 ? -17.155 55.532 42.133 1.00 73.89 ? 104 ASN A ND2 1 ATOM 129 N N . LEU A 1 17 ? -13.367 58.796 40.084 1.00 58.00 ? 105 LEU A N 1 ATOM 130 C CA . LEU A 1 17 ? -12.055 59.445 40.059 1.00 59.18 ? 105 LEU A CA 1 ATOM 131 C C . LEU A 1 17 ? -12.100 60.902 40.500 1.00 66.46 ? 105 LEU A C 1 ATOM 132 O O . LEU A 1 17 ? -13.146 61.554 40.407 1.00 65.13 ? 105 LEU A O 1 ATOM 133 C CB . LEU A 1 17 ? -11.479 59.409 38.638 1.00 58.80 ? 105 LEU A CB 1 ATOM 134 C CG . LEU A 1 17 ? -10.990 58.108 38.005 1.00 58.12 ? 105 LEU A CG 1 ATOM 135 C CD1 . LEU A 1 17 ? -10.646 58.369 36.542 1.00 54.81 ? 105 LEU A CD1 1 ATOM 136 C CD2 . LEU A 1 17 ? -9.772 57.569 38.736 1.00 59.50 ? 105 LEU A CD2 1 ATOM 137 N N . ILE A 1 18 ? -10.951 61.395 40.975 1.00 67.31 ? 106 ILE A N 1 ATOM 138 C CA . ILE A 1 18 ? -10.697 62.826 41.172 1.00 71.77 ? 106 ILE A CA 1 ATOM 139 C C . ILE A 1 18 ? -10.960 63.555 39.854 1.00 73.35 ? 106 ILE A C 1 ATOM 140 O O . ILE A 1 18 ? -10.524 63.084 38.807 1.00 60.89 ? 106 ILE A O 1 ATOM 141 C CB . ILE A 1 18 ? -9.196 63.061 41.475 1.00 82.89 ? 106 ILE A CB 1 ATOM 142 C CG1 . ILE A 1 18 ? -8.760 62.339 42.743 1.00 94.73 ? 106 ILE A CG1 1 ATOM 143 C CG2 . ILE A 1 18 ? -8.884 64.536 41.601 1.00 92.88 ? 106 ILE A CG2 1 ATOM 144 C CD1 . ILE A 1 18 ? -7.270 62.460 43.005 1.00 96.55 ? 106 ILE A CD1 1 ATOM 145 N N . PRO A 1 19 ? -11.648 64.711 39.894 1.00 80.30 ? 107 PRO A N 1 ATOM 146 C CA . PRO A 1 19 ? -11.883 65.506 38.679 1.00 81.13 ? 107 PRO A CA 1 ATOM 147 C C . PRO A 1 19 ? -10.618 65.753 37.852 1.00 80.28 ? 107 PRO A C 1 ATOM 148 O O . PRO A 1 19 ? -10.681 65.825 36.624 1.00 82.82 ? 107 PRO A O 1 ATOM 149 C CB . PRO A 1 19 ? -12.428 66.829 39.226 1.00 86.19 ? 107 PRO A CB 1 ATOM 150 C CG . PRO A 1 19 ? -12.143 66.799 40.716 1.00 87.51 ? 107 PRO A CG 1 ATOM 151 C CD . PRO A 1 19 ? -12.221 65.361 41.081 1.00 84.70 ? 107 PRO A CD 1 ATOM 152 N N . ARG A 1 20 ? -9.479 65.866 38.521 1.00 73.23 ? 108 ARG A N 1 ATOM 153 C CA . ARG A 1 20 ? -8.215 66.039 37.829 1.00 63.60 ? 108 ARG A CA 1 ATOM 154 C C . ARG A 1 20 ? -7.940 64.893 36.868 1.00 66.27 ? 108 ARG A C 1 ATOM 155 O O . ARG A 1 20 ? -7.633 65.128 35.705 1.00 70.59 ? 108 ARG A O 1 ATOM 156 C CB . ARG A 1 20 ? -7.075 66.141 38.836 1.00 63.71 ? 108 ARG A CB 1 ATOM 157 C CG . ARG A 1 20 ? -5.739 66.508 38.228 1.00 59.40 ? 108 ARG A CG 1 ATOM 158 C CD . ARG A 1 20 ? -4.598 66.193 39.185 1.00 62.47 ? 108 ARG A CD 1 ATOM 159 N NE . ARG A 1 20 ? -3.407 65.862 38.425 1.00 72.59 ? 108 ARG A NE 1 ATOM 160 C CZ . ARG A 1 20 ? -2.646 64.796 38.626 1.00 70.31 ? 108 ARG A CZ 1 ATOM 161 N NH1 . ARG A 1 20 ? -2.917 63.953 39.607 1.00 60.78 ? 108 ARG A NH1 1 ATOM 162 N NH2 . ARG A 1 20 ? -1.600 64.583 37.839 1.00 72.81 ? 108 ARG A NH2 1 ATOM 163 N N . LEU A 1 21 ? -8.055 63.657 37.354 1.00 58.40 ? 109 LEU A N 1 ATOM 164 C CA . LEU A 1 21 ? -7.789 62.479 36.537 1.00 57.44 ? 109 LEU A CA 1 ATOM 165 C C . LEU A 1 21 ? -8.955 62.184 35.599 1.00 60.54 ? 109 LEU A C 1 ATOM 166 O O . LEU A 1 21 ? -8.787 61.545 34.559 1.00 58.00 ? 109 LEU A O 1 ATOM 167 C CB . LEU A 1 21 ? -7.493 61.249 37.398 1.00 53.11 ? 109 LEU A CB 1 ATOM 168 C CG . LEU A 1 21 ? -6.422 61.330 38.477 1.00 56.35 ? 109 LEU A CG 1 ATOM 169 C CD1 . LEU A 1 21 ? -6.588 60.153 39.416 1.00 66.23 ? 109 LEU A CD1 1 ATOM 170 C CD2 . LEU A 1 21 ? -5.051 61.314 37.880 1.00 58.89 ? 109 LEU A CD2 1 ATOM 171 N N . GLN A 1 22 ? -10.140 62.643 35.974 1.00 63.01 ? 110 GLN A N 1 ATOM 172 C CA . GLN A 1 22 ? -11.273 62.552 35.074 1.00 67.75 ? 110 GLN A CA 1 ATOM 173 C C . GLN A 1 22 ? -11.013 63.300 33.758 1.00 66.39 ? 110 GLN A C 1 ATOM 174 O O . GLN A 1 22 ? -11.329 62.783 32.697 1.00 58.25 ? 110 GLN A O 1 ATOM 175 C CB . GLN A 1 22 ? -12.533 63.085 35.738 1.00 74.79 ? 110 GLN A CB 1 ATOM 176 C CG . GLN A 1 22 ? -13.495 62.023 36.230 1.00 77.39 ? 110 GLN A CG 1 ATOM 177 C CD . GLN A 1 22 ? -14.635 62.618 37.048 1.00 86.32 ? 110 GLN A CD 1 ATOM 178 O OE1 . GLN A 1 22 ? -14.677 63.826 37.286 1.00 85.24 ? 110 GLN A OE1 1 ATOM 179 N NE2 . GLN A 1 22 ? -15.563 61.769 37.484 1.00 91.71 ? 110 GLN A NE2 1 ATOM 180 N N . LYS A 1 23 ? -10.460 64.512 33.822 1.00 68.69 ? 111 LYS A N 1 ATOM 181 C CA . LYS A 1 23 ? -10.204 65.304 32.610 1.00 73.18 ? 111 LYS A CA 1 ATOM 182 C C . LYS A 1 23 ? -9.137 64.646 31.744 1.00 72.91 ? 111 LYS A C 1 ATOM 183 O O . LYS A 1 23 ? -9.244 64.606 30.519 1.00 75.66 ? 111 LYS A O 1 ATOM 184 C CB . LYS A 1 23 ? -9.801 66.742 32.957 1.00 76.62 ? 111 LYS A CB 1 ATOM 185 C CG . LYS A 1 23 ? -10.889 67.519 33.687 1.00 90.82 ? 111 LYS A CG 1 ATOM 186 C CD . LYS A 1 23 ? -10.425 68.900 34.135 1.00 96.03 ? 111 LYS A CD 1 ATOM 187 C CE . LYS A 1 23 ? -11.412 69.488 35.139 1.00 105.23 ? 111 LYS A CE 1 ATOM 188 N NZ . LYS A 1 23 ? -11.169 70.931 35.450 1.00 111.63 ? 111 LYS A NZ 1 ATOM 189 N N . ILE A 1 24 ? -8.122 64.104 32.400 1.00 67.28 ? 112 ILE A N 1 ATOM 190 C CA . ILE A 1 24 ? -7.064 63.364 31.732 1.00 63.20 ? 112 ILE A CA 1 ATOM 191 C C . ILE A 1 24 ? -7.575 62.138 30.971 1.00 61.12 ? 112 ILE A C 1 ATOM 192 O O . ILE A 1 24 ? -7.224 61.940 29.813 1.00 58.56 ? 112 ILE A O 1 ATOM 193 C CB . ILE A 1 24 ? -6.022 62.962 32.765 1.00 54.90 ? 112 ILE A CB 1 ATOM 194 C CG1 . ILE A 1 24 ? -5.358 64.226 33.312 1.00 57.30 ? 112 ILE A CG1 1 ATOM 195 C CG2 . ILE A 1 24 ? -5.004 62.014 32.183 1.00 49.89 ? 112 ILE A CG2 1 ATOM 196 C CD1 . ILE A 1 24 ? -4.248 63.941 34.280 1.00 59.15 ? 112 ILE A CD1 1 ATOM 197 N N . TRP A 1 25 ? -8.384 61.315 31.637 1.00 57.64 ? 113 TRP A N 1 ATOM 198 C CA . TRP A 1 25 ? -9.091 60.190 31.001 1.00 56.41 ? 113 TRP A CA 1 ATOM 199 C C . TRP A 1 25 ? -9.873 60.668 29.772 1.00 59.69 ? 113 TRP A C 1 ATOM 200 O O . TRP A 1 25 ? -9.707 60.133 28.663 1.00 55.85 ? 113 TRP A O 1 ATOM 201 C CB . TRP A 1 25 ? -10.028 59.507 32.031 1.00 64.10 ? 113 TRP A CB 1 ATOM 202 C CG . TRP A 1 25 ? -11.098 58.579 31.454 1.00 60.88 ? 113 TRP A CG 1 ATOM 203 C CD1 . TRP A 1 25 ? -10.914 57.317 30.962 1.00 58.36 ? 113 TRP A CD1 1 ATOM 204 C CD2 . TRP A 1 25 ? -12.509 58.842 31.351 1.00 62.72 ? 113 TRP A CD2 1 ATOM 205 N NE1 . TRP A 1 25 ? -12.115 56.783 30.550 1.00 58.97 ? 113 TRP A NE1 1 ATOM 206 C CE2 . TRP A 1 25 ? -13.108 57.701 30.776 1.00 62.25 ? 113 TRP A CE2 1 ATOM 207 C CE3 . TRP A 1 25 ? -13.319 59.932 31.681 1.00 72.78 ? 113 TRP A CE3 1 ATOM 208 C CZ2 . TRP A 1 25 ? -14.482 57.624 30.518 1.00 68.94 ? 113 TRP A CZ2 1 ATOM 209 C CZ3 . TRP A 1 25 ? -14.691 59.853 31.422 1.00 76.28 ? 113 TRP A CZ3 1 ATOM 210 C CH2 . TRP A 1 25 ? -15.253 58.709 30.847 1.00 71.70 ? 113 TRP A CH2 1 ATOM 211 N N . LYS A 1 26 ? -10.699 61.694 29.977 1.00 65.63 ? 114 LYS A N 1 ATOM 212 C CA . LYS A 1 26 ? -11.467 62.312 28.897 1.00 73.59 ? 114 LYS A CA 1 ATOM 213 C C . LYS A 1 26 ? -10.584 62.724 27.721 1.00 74.17 ? 114 LYS A C 1 ATOM 214 O O . LYS A 1 26 ? -10.929 62.475 26.567 1.00 74.61 ? 114 LYS A O 1 ATOM 215 C CB . LYS A 1 26 ? -12.260 63.520 29.410 1.00 80.39 ? 114 LYS A CB 1 ATOM 216 C CG . LYS A 1 26 ? -13.572 63.155 30.097 1.00 95.09 ? 114 LYS A CG 1 ATOM 217 C CD . LYS A 1 26 ? -13.968 64.177 31.182 1.00 104.63 ? 114 LYS A CD 1 ATOM 218 C CE . LYS A 1 26 ? -14.902 63.563 32.243 1.00 102.11 ? 114 LYS A CE 1 ATOM 219 N NZ . LYS A 1 26 ? -14.815 64.254 33.561 1.00 96.99 ? 114 LYS A NZ 1 ATOM 220 N N . ASN A 1 27 ? -9.442 63.340 28.016 1.00 76.92 ? 115 ASN A N 1 ATOM 221 C CA . ASN A 1 27 ? -8.558 63.835 26.961 1.00 77.69 ? 115 ASN A CA 1 ATOM 222 C C . ASN A 1 27 ? -7.837 62.746 26.186 1.00 68.56 ? 115 ASN A C 1 ATOM 223 O O . ASN A 1 27 ? -7.562 62.923 25.006 1.00 70.96 ? 115 ASN A O 1 ATOM 224 C CB . ASN A 1 27 ? -7.563 64.863 27.499 1.00 82.00 ? 115 ASN A CB 1 ATOM 225 C CG . ASN A 1 27 ? -8.247 66.131 27.964 1.00 99.93 ? 115 ASN A CG 1 ATOM 226 O OD1 . ASN A 1 27 ? -9.253 66.553 27.386 1.00 104.48 ? 115 ASN A OD1 1 ATOM 227 N ND2 . ASN A 1 27 ? -7.716 66.744 29.017 1.00 104.82 ? 115 ASN A ND2 1 ATOM 228 N N . TYR A 1 28 ? -7.532 61.623 26.833 1.00 52.40 ? 116 TYR A N 1 ATOM 229 C CA . TYR A 1 28 ? -6.909 60.521 26.108 1.00 51.33 ? 116 TYR A CA 1 ATOM 230 C C . TYR A 1 28 ? -7.912 59.832 25.195 1.00 60.43 ? 116 TYR A C 1 ATOM 231 O O . TYR A 1 28 ? -7.545 59.284 24.146 1.00 64.18 ? 116 TYR A O 1 ATOM 232 C CB . TYR A 1 28 ? -6.305 59.504 27.062 1.00 52.79 ? 116 TYR A CB 1 ATOM 233 C CG . TYR A 1 28 ? -4.912 59.872 27.520 1.00 56.62 ? 116 TYR A CG 1 ATOM 234 C CD1 . TYR A 1 28 ? -3.876 60.021 26.603 1.00 55.96 ? 116 TYR A CD1 1 ATOM 235 C CD2 . TYR A 1 28 ? -4.622 60.033 28.870 1.00 51.53 ? 116 TYR A CD2 1 ATOM 236 C CE1 . TYR A 1 28 ? -2.597 60.348 27.022 1.00 55.91 ? 116 TYR A CE1 1 ATOM 237 C CE2 . TYR A 1 28 ? -3.345 60.363 29.292 1.00 47.46 ? 116 TYR A CE2 1 ATOM 238 C CZ . TYR A 1 28 ? -2.345 60.519 28.374 1.00 52.23 ? 116 TYR A CZ 1 ATOM 239 O OH . TYR A 1 28 ? -1.078 60.835 28.804 1.00 55.36 ? 116 TYR A OH 1 ATOM 240 N N . LEU A 1 29 ? -9.178 59.863 25.603 1.00 55.60 ? 117 LEU A N 1 ATOM 241 C CA . LEU A 1 29 ? -10.265 59.364 24.792 1.00 57.37 ? 117 LEU A CA 1 ATOM 242 C C . LEU A 1 29 ? -10.273 60.158 23.502 1.00 67.28 ? 117 LEU A C 1 ATOM 243 O O . LEU A 1 29 ? -10.477 59.603 22.423 1.00 73.03 ? 117 LEU A O 1 ATOM 244 C CB . LEU A 1 29 ? -11.591 59.560 25.518 1.00 53.29 ? 117 LEU A CB 1 ATOM 245 C CG . LEU A 1 29 ? -12.239 58.282 26.049 1.00 68.35 ? 117 LEU A CG 1 ATOM 246 C CD1 . LEU A 1 29 ? -11.220 57.440 26.793 1.00 74.43 ? 117 LEU A CD1 1 ATOM 247 C CD2 . LEU A 1 29 ? -13.418 58.601 26.954 1.00 69.13 ? 117 LEU A CD2 1 ATOM 248 N N . SER A 1 30 ? -10.026 61.460 23.631 1.00 67.11 ? 118 SER A N 1 ATOM 249 C CA . SER A 1 30 ? -10.151 62.390 22.524 1.00 68.76 ? 118 SER A CA 1 ATOM 250 C C . SER A 1 30 ? -8.999 62.268 21.547 1.00 72.70 ? 118 SER A C 1 ATOM 251 O O . SER A 1 30 ? -9.214 62.055 20.352 1.00 78.60 ? 118 SER A O 1 ATOM 252 C CB . SER A 1 30 ? -10.222 63.816 23.040 1.00 71.69 ? 118 SER A CB 1 ATOM 253 O OG . SER A 1 30 ? -11.066 64.590 22.213 1.00 80.00 ? 118 SER A OG 1 ATOM 254 N N . MET A 1 31 ? -7.773 62.428 22.034 1.00 72.31 ? 119 MET A N 1 ATOM 255 C CA . MET A 1 31 ? -6.637 62.191 21.162 1.00 78.36 ? 119 MET A CA 1 ATOM 256 C C . MET A 1 31 ? -6.431 60.691 21.062 1.00 82.08 ? 119 MET A C 1 ATOM 257 O O . MET A 1 31 ? -5.658 60.100 21.812 1.00 88.65 ? 119 MET A O 1 ATOM 258 C CB . MET A 1 31 ? -5.370 62.933 21.609 1.00 78.04 ? 119 MET A CB 1 ATOM 259 C CG . MET A 1 31 ? -5.025 62.837 23.067 1.00 76.92 ? 119 MET A CG 1 ATOM 260 S SD . MET A 1 31 ? -3.272 63.134 23.327 1.00 143.54 ? 119 MET A SD 1 ATOM 261 C CE . MET A 1 31 ? -2.591 61.508 22.989 1.00 67.46 ? 119 MET A CE 1 ATOM 262 N N . ASN A 1 32 ? -7.162 60.076 20.142 1.00 81.27 ? 120 ASN A N 1 ATOM 263 C CA . ASN A 1 32 ? -7.102 58.640 19.956 1.00 76.49 ? 120 ASN A CA 1 ATOM 264 C C . ASN A 1 32 ? -5.804 58.280 19.265 1.00 73.13 ? 120 ASN A C 1 ATOM 265 O O . ASN A 1 32 ? -5.800 57.951 18.076 1.00 67.13 ? 120 ASN A O 1 ATOM 266 C CB . ASN A 1 32 ? -8.276 58.177 19.101 1.00 83.90 ? 120 ASN A CB 1 ATOM 267 C CG . ASN A 1 32 ? -8.833 56.854 19.565 1.00 92.90 ? 120 ASN A CG 1 ATOM 268 O OD1 . ASN A 1 32 ? -8.312 55.796 19.215 1.00 88.16 ? 120 ASN A OD1 1 ATOM 269 N ND2 . ASN A 1 32 ? -9.895 56.904 20.374 1.00 102.42 ? 120 ASN A ND2 1 ATOM 270 N N . LYS A 1 33 ? -4.706 58.345 20.016 1.00 63.26 ? 121 LYS A N 1 ATOM 271 C CA . LYS A 1 33 ? -3.358 58.266 19.434 1.00 67.06 ? 121 LYS A CA 1 ATOM 272 C C . LYS A 1 33 ? -3.142 57.031 18.562 1.00 59.20 ? 121 LYS A C 1 ATOM 273 O O . LYS A 1 33 ? -2.516 57.095 17.499 1.00 57.96 ? 121 LYS A O 1 ATOM 274 C CB . LYS A 1 33 ? -2.298 58.299 20.550 1.00 66.79 ? 121 LYS A CB 1 ATOM 275 C CG . LYS A 1 33 ? -0.877 58.507 20.037 1.00 62.32 ? 121 LYS A CG 1 ATOM 276 C CD . LYS A 1 33 ? 0.142 58.568 21.177 1.00 64.31 ? 121 LYS A CD 1 ATOM 277 C CE . LYS A 1 33 ? 1.542 58.848 20.631 1.00 66.00 ? 121 LYS A CE 1 ATOM 278 N NZ . LYS A 1 33 ? 2.613 57.970 21.199 1.00 58.06 ? 121 LYS A NZ 1 ATOM 279 N N . TYR A 1 34 ? -3.664 55.902 19.020 1.00 53.12 ? 122 TYR A N 1 ATOM 280 C CA . TYR A 1 34 ? -3.397 54.637 18.366 1.00 48.14 ? 122 TYR A CA 1 ATOM 281 C C . TYR A 1 34 ? -4.514 54.251 17.409 1.00 47.41 ? 122 TYR A C 1 ATOM 282 O O . TYR A 1 34 ? -4.542 53.132 16.900 1.00 50.11 ? 122 TYR A O 1 ATOM 283 C CB . TYR A 1 34 ? -3.114 53.571 19.423 1.00 42.39 ? 122 TYR A CB 1 ATOM 284 C CG . TYR A 1 34 ? -1.941 53.989 20.261 1.00 47.68 ? 122 TYR A CG 1 ATOM 285 C CD1 . TYR A 1 34 ? -0.642 54.008 19.737 1.00 46.68 ? 122 TYR A CD1 1 ATOM 286 C CD2 . TYR A 1 34 ? -2.126 54.421 21.572 1.00 44.45 ? 122 TYR A CD2 1 ATOM 287 C CE1 . TYR A 1 34 ? 0.436 54.423 20.535 1.00 52.10 ? 122 TYR A CE1 1 ATOM 288 C CE2 . TYR A 1 34 ? -1.077 54.828 22.340 1.00 45.33 ? 122 TYR A CE2 1 ATOM 289 C CZ . TYR A 1 34 ? 0.191 54.830 21.849 1.00 47.32 ? 122 TYR A CZ 1 ATOM 290 O OH . TYR A 1 34 ? 1.202 55.270 22.690 1.00 49.70 ? 122 TYR A OH 1 ATOM 291 N N . LYS A 1 35 ? -5.415 55.199 17.160 1.00 49.63 ? 123 LYS A N 1 ATOM 292 C CA . LYS A 1 35 ? -6.416 55.054 16.115 1.00 60.88 ? 123 LYS A CA 1 ATOM 293 C C . LYS A 1 35 ? -7.254 53.833 16.432 1.00 58.04 ? 123 LYS A C 1 ATOM 294 O O . LYS A 1 35 ? -7.482 52.974 15.592 1.00 60.99 ? 123 LYS A O 1 ATOM 295 C CB . LYS A 1 35 ? -5.754 54.920 14.733 1.00 69.59 ? 123 LYS A CB 1 ATOM 296 C CG . LYS A 1 35 ? -5.049 56.181 14.227 1.00 78.10 ? 123 LYS A CG 1 ATOM 297 C CD . LYS A 1 35 ? -4.251 55.876 12.963 1.00 86.24 ? 123 LYS A CD 1 ATOM 298 C CE . LYS A 1 35 ? -3.418 57.062 12.469 1.00 92.79 ? 123 LYS A CE 1 ATOM 299 N NZ . LYS A 1 35 ? -2.312 56.621 11.552 1.00 90.28 ? 123 LYS A NZ 1 ATOM 300 N N . VAL A 1 36 ? -7.684 53.754 17.677 1.00 58.43 ? 124 VAL A N 1 ATOM 301 C CA . VAL A 1 36 ? -8.533 52.675 18.128 1.00 45.44 ? 124 VAL A CA 1 ATOM 302 C C . VAL A 1 36 ? -9.953 52.934 17.677 1.00 61.86 ? 124 VAL A C 1 ATOM 303 O O . VAL A 1 36 ? -10.450 54.058 17.770 1.00 66.83 ? 124 VAL A O 1 ATOM 304 C CB . VAL A 1 36 ? -8.486 52.595 19.647 1.00 58.65 ? 124 VAL A CB 1 ATOM 305 C CG1 . VAL A 1 36 ? -9.382 51.472 20.166 1.00 63.80 ? 124 VAL A CG1 1 ATOM 306 C CG2 . VAL A 1 36 ? -7.042 52.414 20.089 1.00 47.34 ? 124 VAL A CG2 1 ATOM 307 N N . SER A 1 37 ? -10.594 51.893 17.157 1.00 65.95 ? 125 SER A N 1 ATOM 308 C CA . SER A 1 37 ? -12.040 51.877 16.995 1.00 74.44 ? 125 SER A CA 1 ATOM 309 C C . SER A 1 37 ? -12.539 50.553 17.542 1.00 74.47 ? 125 SER A C 1 ATOM 310 O O . SER A 1 37 ? -12.465 49.531 16.867 1.00 74.06 ? 125 SER A O 1 ATOM 311 C CB . SER A 1 37 ? -12.434 52.036 15.529 1.00 81.38 ? 125 SER A CB 1 ATOM 312 O OG . SER A 1 37 ? -12.254 53.377 15.109 1.00 85.14 ? 125 SER A OG 1 ATOM 313 N N . TYR A 1 38 ? -13.008 50.550 18.781 1.00 69.93 ? 126 TYR A N 1 ATOM 314 C CA . TYR A 1 38 ? -13.461 49.296 19.351 1.00 74.64 ? 126 TYR A CA 1 ATOM 315 C C . TYR A 1 38 ? -14.694 48.777 18.605 1.00 83.28 ? 126 TYR A C 1 ATOM 316 O O . TYR A 1 38 ? -15.759 49.400 18.625 1.00 83.18 ? 126 TYR A O 1 ATOM 317 C CB . TYR A 1 38 ? -13.749 49.418 20.848 1.00 67.74 ? 126 TYR A CB 1 ATOM 318 C CG . TYR A 1 38 ? -14.190 48.108 21.448 1.00 65.80 ? 126 TYR A CG 1 ATOM 319 C CD1 . TYR A 1 38 ? -13.300 47.059 21.587 1.00 68.48 ? 126 TYR A CD1 1 ATOM 320 C CD2 . TYR A 1 38 ? -15.498 47.913 21.862 1.00 74.78 ? 126 TYR A CD2 1 ATOM 321 C CE1 . TYR A 1 38 ? -13.699 45.847 22.128 1.00 72.78 ? 126 TYR A CE1 1 ATOM 322 C CE2 . TYR A 1 38 ? -15.905 46.708 22.415 1.00 77.80 ? 126 TYR A CE2 1 ATOM 323 C CZ . TYR A 1 38 ? -14.995 45.680 22.544 1.00 73.37 ? 126 TYR A CZ 1 ATOM 324 O OH . TYR A 1 38 ? -15.390 44.474 23.077 1.00 76.50 ? 126 TYR A OH 1 ATOM 325 N N . LYS A 1 39 ? -14.542 47.629 17.952 1.00 89.16 ? 127 LYS A N 1 ATOM 326 C CA . LYS A 1 39 ? -15.638 47.029 17.197 1.00 98.20 ? 127 LYS A CA 1 ATOM 327 C C . LYS A 1 39 ? -16.103 45.701 17.799 1.00 98.51 ? 127 LYS A C 1 ATOM 328 O O . LYS A 1 39 ? -16.800 44.922 17.144 1.00 107.82 ? 127 LYS A O 1 ATOM 329 C CB . LYS A 1 39 ? -15.224 46.827 15.738 1.00 100.94 ? 127 LYS A CB 1 ATOM 330 C CG . LYS A 1 39 ? -15.908 47.768 14.761 1.00 109.47 ? 127 LYS A CG 1 ATOM 331 C CD . LYS A 1 39 ? -15.862 49.217 15.223 1.00 110.86 ? 127 LYS A CD 1 ATOM 332 C CE . LYS A 1 39 ? -16.082 50.173 14.050 1.00 111.34 ? 127 LYS A CE 1 ATOM 333 N NZ . LYS A 1 39 ? -14.856 50.313 13.213 1.00 103.21 ? 127 LYS A NZ 1 ATOM 334 N N . GLY A 1 40 ? -15.720 45.453 19.046 1.00 89.16 ? 128 GLY A N 1 ATOM 335 C CA . GLY A 1 40 ? -16.068 44.221 19.732 1.00 84.46 ? 128 GLY A CA 1 ATOM 336 C C . GLY A 1 40 ? -17.395 44.271 20.465 1.00 82.86 ? 128 GLY A C 1 ATOM 337 O O . GLY A 1 40 ? -18.048 45.318 20.498 1.00 83.68 ? 128 GLY A O 1 ATOM 338 N N . PRO A 1 41 ? -17.792 43.131 21.062 1.00 82.72 ? 129 PRO A N 1 ATOM 339 C CA . PRO A 1 41 ? -19.102 42.822 21.651 1.00 98.75 ? 129 PRO A CA 1 ATOM 340 C C . PRO A 1 41 ? -19.844 43.986 22.325 1.00 112.22 ? 129 PRO A C 1 ATOM 341 O O . PRO A 1 41 ? -21.077 43.955 22.370 1.00 121.69 ? 129 PRO A O 1 ATOM 342 C CB . PRO A 1 41 ? -18.765 41.719 22.655 1.00 94.11 ? 129 PRO A CB 1 ATOM 343 C CG . PRO A 1 41 ? -17.687 40.957 21.954 1.00 82.64 ? 129 PRO A CG 1 ATOM 344 C CD . PRO A 1 41 ? -16.852 42.008 21.252 1.00 75.31 ? 129 PRO A CD 1 ATOM 345 N N . GLY A 1 42 ? -19.130 44.989 22.825 1.00 108.61 ? 130 GLY A N 1 ATOM 346 C CA . GLY A 1 42 ? -19.790 46.197 23.285 1.00 111.78 ? 130 GLY A CA 1 ATOM 347 C C . GLY A 1 42 ? -19.590 46.462 24.757 1.00 118.50 ? 130 GLY A C 1 ATOM 348 O O . GLY A 1 42 ? -19.616 45.532 25.560 1.00 122.59 ? 130 GLY A O 1 ATOM 349 N N . PRO A 1 43 ? -19.405 47.743 25.115 1.00 122.36 ? 131 PRO A N 1 ATOM 350 C CA . PRO A 1 43 ? -19.031 48.202 26.462 1.00 119.83 ? 131 PRO A CA 1 ATOM 351 C C . PRO A 1 43 ? -19.931 47.644 27.562 1.00 121.96 ? 131 PRO A C 1 ATOM 352 O O . PRO A 1 43 ? -21.116 47.973 27.625 1.00 126.55 ? 131 PRO A O 1 ATOM 353 C CB . PRO A 1 43 ? -19.187 49.724 26.369 1.00 121.39 ? 131 PRO A CB 1 ATOM 354 C CG . PRO A 1 43 ? -18.994 50.031 24.914 1.00 123.87 ? 131 PRO A CG 1 ATOM 355 C CD . PRO A 1 43 ? -19.581 48.864 24.174 1.00 125.73 ? 131 PRO A CD 1 ATOM 356 N N . GLY A 1 44 ? -19.364 46.799 28.415 1.00 116.69 ? 132 GLY A N 1 ATOM 357 C CA . GLY A 1 44 ? -20.096 46.253 29.542 1.00 115.36 ? 132 GLY A CA 1 ATOM 358 C C . GLY A 1 44 ? -20.567 44.831 29.320 1.00 113.32 ? 132 GLY A C 1 ATOM 359 O O . GLY A 1 44 ? -21.585 44.606 28.672 1.00 121.15 ? 132 GLY A O 1 ATOM 360 N N . ILE A 1 45 ? -19.820 43.873 29.859 1.00 103.34 ? 133 ILE A N 1 ATOM 361 C CA . ILE A 1 45 ? -20.195 42.463 29.800 1.00 102.85 ? 133 ILE A CA 1 ATOM 362 C C . ILE A 1 45 ? -19.728 41.716 31.052 1.00 104.50 ? 133 ILE A C 1 ATOM 363 O O . ILE A 1 45 ? -18.606 41.918 31.523 1.00 100.11 ? 133 ILE A O 1 ATOM 364 C CB . ILE A 1 45 ? -19.658 41.783 28.523 1.00 94.93 ? 133 ILE A CB 1 ATOM 365 C CG1 . ILE A 1 45 ? -20.682 41.915 27.397 1.00 95.05 ? 133 ILE A CG1 1 ATOM 366 C CG2 . ILE A 1 45 ? -19.354 40.310 28.769 1.00 93.72 ? 133 ILE A CG2 1 ATOM 367 C CD1 . ILE A 1 45 ? -20.147 41.516 26.061 1.00 98.93 ? 133 ILE A CD1 1 ATOM 368 N N . LYS A 1 46 ? -20.596 40.862 31.591 1.00 103.99 ? 134 LYS A N 1 ATOM 369 C CA . LYS A 1 46 ? -20.267 40.109 32.794 1.00 104.40 ? 134 LYS A CA 1 ATOM 370 C C . LYS A 1 46 ? -19.763 38.685 32.533 1.00 106.46 ? 134 LYS A C 1 ATOM 371 O O . LYS A 1 46 ? -20.351 37.932 31.761 1.00 97.85 ? 134 LYS A O 1 ATOM 372 C CB . LYS A 1 46 ? -21.458 40.084 33.749 1.00 106.79 ? 134 LYS A CB 1 ATOM 373 C CG . LYS A 1 46 ? -21.732 41.418 34.431 1.00 106.07 ? 134 LYS A CG 1 ATOM 374 C CD . LYS A 1 46 ? -22.647 41.223 35.638 1.00 114.86 ? 134 LYS A CD 1 ATOM 375 C CE . LYS A 1 46 ? -23.004 42.539 36.320 1.00 117.35 ? 134 LYS A CE 1 ATOM 376 N NZ . LYS A 1 46 ? -24.063 42.348 37.369 1.00 129.71 ? 134 LYS A NZ 1 ATOM 377 N N . PHE A 1 47 ? -18.666 38.344 33.207 1.00 104.99 ? 135 PHE A N 1 ATOM 378 C CA . PHE A 1 47 ? -18.053 37.019 33.173 1.00 106.76 ? 135 PHE A CA 1 ATOM 379 C C . PHE A 1 47 ? -17.867 36.498 34.600 1.00 109.29 ? 135 PHE A C 1 ATOM 380 O O . PHE A 1 47 ? -17.551 37.276 35.507 1.00 106.52 ? 135 PHE A O 1 ATOM 381 C CB . PHE A 1 47 ? -16.660 37.109 32.543 1.00 100.80 ? 135 PHE A CB 1 ATOM 382 C CG . PHE A 1 47 ? -16.634 36.898 31.056 1.00 98.46 ? 135 PHE A CG 1 ATOM 383 C CD1 . PHE A 1 47 ? -16.762 37.969 30.187 1.00 91.89 ? 135 PHE A CD1 1 ATOM 384 C CD2 . PHE A 1 47 ? -16.445 35.627 30.530 1.00 105.70 ? 135 PHE A CD2 1 ATOM 385 C CE1 . PHE A 1 47 ? -16.722 37.770 28.820 1.00 96.41 ? 135 PHE A CE1 1 ATOM 386 C CE2 . PHE A 1 47 ? -16.411 35.420 29.171 1.00 88.48 ? 135 PHE A CE2 1 ATOM 387 C CZ . PHE A 1 47 ? -16.548 36.493 28.312 1.00 101.54 ? 135 PHE A CZ 1 ATOM 388 N N . SER A 1 48 ? -18.038 35.192 34.802 1.00 110.83 ? 136 SER A N 1 ATOM 389 C CA . SER A 1 48 ? -17.588 34.566 36.044 1.00 113.13 ? 136 SER A CA 1 ATOM 390 C C . SER A 1 48 ? -16.062 34.562 36.025 1.00 113.60 ? 136 SER A C 1 ATOM 391 O O . SER A 1 48 ? -15.465 34.565 34.950 1.00 115.58 ? 136 SER A O 1 ATOM 392 C CB . SER A 1 48 ? -18.103 33.133 36.144 1.00 119.45 ? 136 SER A CB 1 ATOM 393 O OG . SER A 1 48 ? -17.667 32.365 35.034 1.00 117.95 ? 136 SER A OG 1 ATOM 394 N N . ALA A 1 49 ? -15.428 34.557 37.196 1.00 113.00 ? 137 ALA A N 1 ATOM 395 C CA . ALA A 1 49 ? -13.967 34.520 37.260 1.00 112.52 ? 137 ALA A CA 1 ATOM 396 C C . ALA A 1 49 ? -13.411 33.278 36.552 1.00 123.73 ? 137 ALA A C 1 ATOM 397 O O . ALA A 1 49 ? -12.381 33.343 35.884 1.00 124.41 ? 137 ALA A O 1 ATOM 398 C CB . ALA A 1 49 ? -13.477 34.587 38.704 1.00 93.78 ? 137 ALA A CB 1 ATOM 399 N N . GLU A 1 50 ? -14.104 32.152 36.686 1.00 128.75 ? 138 GLU A N 1 ATOM 400 C CA . GLU A 1 50 ? -13.706 30.942 35.985 1.00 124.67 ? 138 GLU A CA 1 ATOM 401 C C . GLU A 1 50 ? -13.757 31.144 34.469 1.00 120.12 ? 138 GLU A C 1 ATOM 402 O O . GLU A 1 50 ? -12.803 30.809 33.769 1.00 120.02 ? 138 GLU A O 1 ATOM 403 C CB . GLU A 1 50 ? -14.583 29.756 36.396 1.00 134.34 ? 138 GLU A CB 1 ATOM 404 C CG . GLU A 1 50 ? -14.370 29.258 37.821 1.00 139.95 ? 138 GLU A CG 1 ATOM 405 C CD . GLU A 1 50 ? -14.847 27.821 38.010 1.00 152.96 ? 138 GLU A CD 1 ATOM 406 O OE1 . GLU A 1 50 ? -14.888 27.068 37.009 1.00 156.20 ? 138 GLU A OE1 1 ATOM 407 O OE2 . GLU A 1 50 ? -15.180 27.443 39.155 1.00 157.26 ? 138 GLU A OE2 1 ATOM 408 N N . ALA A 1 51 ? -14.860 31.700 33.968 1.00 118.62 ? 139 ALA A N 1 ATOM 409 C CA . ALA A 1 51 ? -15.035 31.905 32.525 1.00 100.28 ? 139 ALA A CA 1 ATOM 410 C C . ALA A 1 51 ? -14.122 32.993 31.959 1.00 114.15 ? 139 ALA A C 1 ATOM 411 O O . ALA A 1 51 ? -13.626 32.877 30.838 1.00 118.08 ? 139 ALA A O 1 ATOM 412 C CB . ALA A 1 51 ? -16.491 32.216 32.188 1.00 103.74 ? 139 ALA A CB 1 ATOM 413 N N . LEU A 1 52 ? -13.914 34.055 32.727 1.00 106.26 ? 140 LEU A N 1 ATOM 414 C CA . LEU A 1 52 ? -13.109 35.171 32.262 1.00 95.26 ? 140 LEU A CA 1 ATOM 415 C C . LEU A 1 52 ? -11.654 34.762 32.255 1.00 91.05 ? 140 LEU A C 1 ATOM 416 O O . LEU A 1 52 ? -10.897 35.158 31.371 1.00 83.94 ? 140 LEU A O 1 ATOM 417 C CB . LEU A 1 52 ? -13.317 36.392 33.153 1.00 92.24 ? 140 LEU A CB 1 ATOM 418 C CG . LEU A 1 52 ? -12.449 37.637 32.966 1.00 86.52 ? 140 LEU A CG 1 ATOM 419 C CD1 . LEU A 1 52 ? -12.484 38.168 31.535 1.00 78.80 ? 140 LEU A CD1 1 ATOM 420 C CD2 . LEU A 1 52 ? -12.919 38.699 33.949 1.00 84.92 ? 140 LEU A CD2 1 ATOM 421 N N . ARG A 1 53 ? -11.256 33.961 33.238 1.00 92.11 ? 141 ARG A N 1 ATOM 422 C CA . ARG A 1 53 ? -9.885 33.470 33.252 1.00 95.94 ? 141 ARG A CA 1 ATOM 423 C C . ARG A 1 53 ? -9.619 32.640 32.004 1.00 92.84 ? 141 ARG A C 1 ATOM 424 O O . ARG A 1 53 ? -8.516 32.671 31.442 1.00 85.99 ? 141 ARG A O 1 ATOM 425 C CB . ARG A 1 53 ? -9.588 32.666 34.519 1.00 107.47 ? 141 ARG A CB 1 ATOM 426 C CG . ARG A 1 53 ? -9.163 33.541 35.695 1.00 107.36 ? 141 ARG A CG 1 ATOM 427 C CD . ARG A 1 53 ? -8.587 32.728 36.840 1.00 112.98 ? 141 ARG A CD 1 ATOM 428 N NE . ARG A 1 53 ? -9.587 31.943 37.565 1.00 117.85 ? 141 ARG A NE 1 ATOM 429 C CZ . ARG A 1 53 ? -10.229 32.366 38.653 1.00 114.72 ? 141 ARG A CZ 1 ATOM 430 N NH1 . ARG A 1 53 ? -9.991 33.576 39.150 1.00 100.55 ? 141 ARG A NH1 1 ATOM 431 N NH2 . ARG A 1 53 ? -11.116 31.578 39.244 1.00 124.26 ? 141 ARG A NH2 1 ATOM 432 N N . CYS A 1 54 ? -10.653 31.924 31.569 1.00 98.44 ? 142 CYS A N 1 ATOM 433 C CA . CYS A 1 54 ? -10.577 31.023 30.424 1.00 95.77 ? 142 CYS A CA 1 ATOM 434 C C . CYS A 1 54 ? -10.778 31.803 29.107 1.00 91.80 ? 142 CYS A C 1 ATOM 435 O O . CYS A 1 54 ? -10.198 31.462 28.080 1.00 91.72 ? 142 CYS A O 1 ATOM 436 C CB . CYS A 1 54 ? -11.495 29.789 30.659 1.00 96.45 ? 142 CYS A CB 1 ATOM 437 S SG . CYS A 1 54 ? -12.770 29.275 29.456 1.00 113.37 ? 142 CYS A SG 1 ATOM 438 N N . HIS A 1 55 ? -11.527 32.900 29.166 1.00 86.84 ? 143 HIS A N 1 ATOM 439 C CA . HIS A 1 55 ? -11.641 33.816 28.037 1.00 84.28 ? 143 HIS A CA 1 ATOM 440 C C . HIS A 1 55 ? -10.345 34.628 27.858 1.00 84.23 ? 143 HIS A C 1 ATOM 441 O O . HIS A 1 55 ? -10.078 35.176 26.777 1.00 79.75 ? 143 HIS A O 1 ATOM 442 C CB . HIS A 1 55 ? -12.862 34.734 28.215 1.00 83.77 ? 143 HIS A CB 1 ATOM 443 C CG . HIS A 1 55 ? -12.945 35.850 27.216 1.00 74.28 ? 143 HIS A CG 1 ATOM 444 N ND1 . HIS A 1 55 ? -12.841 35.644 25.855 1.00 85.53 ? 143 HIS A ND1 1 ATOM 445 C CD2 . HIS A 1 55 ? -13.125 37.181 27.381 1.00 72.86 ? 143 HIS A CD2 1 ATOM 446 C CE1 . HIS A 1 55 ? -12.941 36.804 25.226 1.00 75.81 ? 143 HIS A CE1 1 ATOM 447 N NE2 . HIS A 1 55 ? -13.109 37.754 26.129 1.00 77.23 ? 143 HIS A NE2 1 ATOM 448 N N . LEU A 1 56 ? -9.525 34.672 28.904 1.00 73.87 ? 144 LEU A N 1 ATOM 449 C CA . LEU A 1 56 ? -8.253 35.390 28.874 1.00 64.70 ? 144 LEU A CA 1 ATOM 450 C C . LEU A 1 56 ? -7.116 34.503 28.347 1.00 68.70 ? 144 LEU A C 1 ATOM 451 O O . LEU A 1 56 ? -6.215 34.958 27.624 1.00 68.55 ? 144 LEU A O 1 ATOM 452 C CB . LEU A 1 56 ? -7.921 35.851 30.283 1.00 76.37 ? 144 LEU A CB 1 ATOM 453 C CG . LEU A 1 56 ? -7.114 37.109 30.517 1.00 78.49 ? 144 LEU A CG 1 ATOM 454 C CD1 . LEU A 1 56 ? -7.609 38.221 29.612 1.00 82.70 ? 144 LEU A CD1 1 ATOM 455 C CD2 . LEU A 1 56 ? -7.276 37.496 31.985 1.00 80.31 ? 144 LEU A CD2 1 ATOM 456 N N . ARG A 1 57 ? -7.144 33.243 28.753 1.00 72.97 ? 145 ARG A N 1 ATOM 457 C CA . ARG A 1 57 ? -6.192 32.246 28.287 1.00 80.08 ? 145 ARG A CA 1 ATOM 458 C C . ARG A 1 57 ? -6.343 32.064 26.782 1.00 82.77 ? 145 ARG A C 1 ATOM 459 O O . ARG A 1 57 ? -5.349 31.985 26.065 1.00 72.66 ? 145 ARG A O 1 ATOM 460 C CB . ARG A 1 57 ? -6.447 30.900 28.976 1.00 78.17 ? 145 ARG A CB 1 ATOM 461 C CG . ARG A 1 57 ? -5.600 29.750 28.445 1.00 81.08 ? 145 ARG A CG 1 ATOM 462 C CD . ARG A 1 57 ? -6.193 28.392 28.821 1.00 92.59 ? 145 ARG A CD 1 ATOM 463 N NE . ARG A 1 57 ? -7.518 28.191 28.234 1.00 100.15 ? 145 ARG A NE 1 ATOM 464 C CZ . ARG A 1 57 ? -8.233 27.075 28.347 1.00 111.80 ? 145 ARG A CZ 1 ATOM 465 N NH1 . ARG A 1 57 ? -7.757 26.045 29.033 1.00 121.47 ? 145 ARG A NH1 1 ATOM 466 N NH2 . ARG A 1 57 ? -9.429 26.987 27.775 1.00 112.14 ? 145 ARG A NH2 1 ATOM 467 N N . ASP A 1 58 ? -7.594 32.014 26.329 1.00 73.65 ? 146 ASP A N 1 ATOM 468 C CA . ASP A 1 58 ? -7.911 31.725 24.942 1.00 81.98 ? 146 ASP A CA 1 ATOM 469 C C . ASP A 1 58 ? -7.776 32.914 23.959 1.00 80.39 ? 146 ASP A C 1 ATOM 470 O O . ASP A 1 58 ? -7.457 32.708 22.796 1.00 82.41 ? 146 ASP A O 1 ATOM 471 C CB . ASP A 1 58 ? -9.302 31.070 24.853 1.00 80.78 ? 146 ASP A CB 1 ATOM 472 C CG . ASP A 1 58 ? -9.345 29.696 25.524 1.00 86.58 ? 146 ASP A CG 1 ATOM 473 O OD1 . ASP A 1 58 ? -8.278 29.052 25.604 1.00 92.24 ? 146 ASP A OD1 1 ATOM 474 O OD2 . ASP A 1 58 ? -10.432 29.258 25.981 1.00 95.10 ? 146 ASP A OD2 1 ATOM 475 N N . HIS A 1 59 ? -7.994 34.143 24.416 1.00 74.97 ? 147 HIS A N 1 ATOM 476 C CA . HIS A 1 59 ? -8.055 35.298 23.506 1.00 69.51 ? 147 HIS A CA 1 ATOM 477 C C . HIS A 1 59 ? -6.882 36.276 23.622 1.00 63.40 ? 147 HIS A C 1 ATOM 478 O O . HIS A 1 59 ? -6.936 37.410 23.112 1.00 56.87 ? 147 HIS A O 1 ATOM 479 C CB . HIS A 1 59 ? -9.383 36.053 23.692 1.00 75.47 ? 147 HIS A CB 1 ATOM 480 C CG . HIS A 1 59 ? -10.579 35.316 23.168 1.00 83.92 ? 147 HIS A CG 1 ATOM 481 N ND1 . HIS A 1 59 ? -11.065 34.168 23.758 1.00 97.88 ? 147 HIS A ND1 1 ATOM 482 C CD2 . HIS A 1 59 ? -11.392 35.568 22.114 1.00 81.55 ? 147 HIS A CD2 1 ATOM 483 C CE1 . HIS A 1 59 ? -12.115 33.735 23.081 1.00 99.22 ? 147 HIS A CE1 1 ATOM 484 N NE2 . HIS A 1 59 ? -12.335 34.568 22.079 1.00 93.85 ? 147 HIS A NE2 1 ATOM 485 N N . VAL A 1 60 ? -5.830 35.873 24.327 1.00 69.02 ? 148 VAL A N 1 ATOM 486 C CA . VAL A 1 60 ? -4.625 36.698 24.397 1.00 62.35 ? 148 VAL A CA 1 ATOM 487 C C . VAL A 1 60 ? -3.461 35.802 24.008 1.00 67.20 ? 148 VAL A C 1 ATOM 488 O O . VAL A 1 60 ? -3.279 34.718 24.580 1.00 68.15 ? 148 VAL A O 1 ATOM 489 C CB . VAL A 1 60 ? -4.416 37.311 25.798 1.00 62.73 ? 148 VAL A CB 1 ATOM 490 C CG1 . VAL A 1 60 ? -3.253 38.299 25.787 1.00 49.76 ? 148 VAL A CG1 1 ATOM 491 C CG2 . VAL A 1 60 ? -5.674 38.040 26.249 1.00 58.47 ? 148 VAL A CG2 1 ATOM 492 N N . ASN A 1 61 ? -2.709 36.215 22.992 1.00 55.59 ? 149 ASN A N 1 ATOM 493 C CA . ASN A 1 61 ? -1.592 35.410 22.545 1.00 58.39 ? 149 ASN A CA 1 ATOM 494 C C . ASN A 1 61 ? -0.316 35.993 23.115 1.00 62.75 ? 149 ASN A C 1 ATOM 495 O O . ASN A 1 61 ? 0.252 36.934 22.568 1.00 62.00 ? 149 ASN A O 1 ATOM 496 C CB . ASN A 1 61 ? -1.525 35.337 21.010 1.00 55.80 ? 149 ASN A CB 1 ATOM 497 C CG . ASN A 1 61 ? -2.322 34.177 20.442 1.00 59.12 ? 149 ASN A CG 1 ATOM 498 O OD1 . ASN A 1 61 ? -2.510 33.159 21.100 1.00 68.76 ? 149 ASN A OD1 1 ATOM 499 N ND2 . ASN A 1 61 ? -2.779 34.317 19.217 1.00 68.86 ? 149 ASN A ND2 1 ATOM 500 N N . VAL A 1 62 ? 0.121 35.435 24.233 1.00 60.57 ? 150 VAL A N 1 ATOM 501 C CA . VAL A 1 62 ? 1.402 35.799 24.801 1.00 59.36 ? 150 VAL A CA 1 ATOM 502 C C . VAL A 1 62 ? 2.474 35.158 23.948 1.00 59.52 ? 150 VAL A C 1 ATOM 503 O O . VAL A 1 62 ? 2.783 33.970 24.108 1.00 58.43 ? 150 VAL A O 1 ATOM 504 C CB . VAL A 1 62 ? 1.537 35.260 26.231 1.00 63.50 ? 150 VAL A CB 1 ATOM 505 C CG1 . VAL A 1 62 ? 2.613 36.034 26.959 1.00 56.42 ? 150 VAL A CG1 1 ATOM 506 C CG2 . VAL A 1 62 ? 0.223 35.405 26.955 1.00 61.69 ? 150 VAL A CG2 1 ATOM 507 N N . SER A 1 63 ? 3.005 35.912 22.992 1.00 58.90 ? 151 SER A N 1 ATOM 508 C CA . SER A 1 63 ? 4.056 35.373 22.149 1.00 61.30 ? 151 SER A CA 1 ATOM 509 C C . SER A 1 63 ? 5.039 36.472 21.780 1.00 58.78 ? 151 SER A C 1 ATOM 510 O O . SER A 1 63 ? 4.700 37.660 21.811 1.00 55.16 ? 151 SER A O 1 ATOM 511 C CB . SER A 1 63 ? 3.482 34.665 20.919 1.00 80.01 ? 151 SER A CB 1 ATOM 512 O OG . SER A 1 63 ? 2.535 35.478 20.255 1.00 88.20 ? 151 SER A OG 1 ATOM 513 N N . MET A 1 64 ? 6.265 36.066 21.467 1.00 57.52 ? 152 MET A N 1 ATOM 514 C CA . MET A 1 64 ? 7.367 36.999 21.266 1.00 50.53 ? 152 MET A CA 1 ATOM 515 C C . MET A 1 64 ? 7.741 36.975 19.806 1.00 50.21 ? 152 MET A C 1 ATOM 516 O O . MET A 1 64 ? 7.550 35.965 19.128 1.00 56.21 ? 152 MET A O 1 ATOM 517 C CB . MET A 1 64 ? 8.583 36.547 22.075 1.00 56.11 ? 152 MET A CB 1 ATOM 518 C CG . MET A 1 64 ? 8.322 36.387 23.567 1.00 58.29 ? 152 MET A CG 1 ATOM 519 S SD . MET A 1 64 ? 7.907 37.918 24.403 1.00 58.04 ? 152 MET A SD 1 ATOM 520 C CE . MET A 1 64 ? 7.143 37.243 25.879 1.00 54.44 ? 152 MET A CE 1 ATOM 521 N N . VAL A 1 65 ? 8.284 38.081 19.320 1.00 51.18 ? 153 VAL A N 1 ATOM 522 C CA . VAL A 1 65 ? 8.740 38.124 17.940 1.00 53.28 ? 153 VAL A CA 1 ATOM 523 C C . VAL A 1 65 ? 9.798 37.062 17.698 1.00 55.68 ? 153 VAL A C 1 ATOM 524 O O . VAL A 1 65 ? 10.792 36.982 18.420 1.00 56.91 ? 153 VAL A O 1 ATOM 525 C CB . VAL A 1 65 ? 9.313 39.504 17.593 1.00 53.07 ? 153 VAL A CB 1 ATOM 526 C CG1 . VAL A 1 65 ? 9.898 39.483 16.192 1.00 53.24 ? 153 VAL A CG1 1 ATOM 527 C CG2 . VAL A 1 65 ? 8.228 40.575 17.736 1.00 41.99 ? 153 VAL A CG2 1 ATOM 528 N N . GLU A 1 66 ? 9.575 36.238 16.672 1.00 55.19 ? 154 GLU A N 1 ATOM 529 C CA . GLU A 1 66 ? 10.488 35.175 16.328 1.00 58.90 ? 154 GLU A CA 1 ATOM 530 C C . GLU A 1 66 ? 11.119 35.426 14.958 1.00 64.02 ? 154 GLU A C 1 ATOM 531 O O . GLU A 1 66 ? 10.613 36.213 14.145 1.00 62.13 ? 154 GLU A O 1 ATOM 532 C CB . GLU A 1 66 ? 9.764 33.826 16.340 1.00 70.76 ? 154 GLU A CB 1 ATOM 533 C CG . GLU A 1 66 ? 9.440 33.313 17.738 1.00 82.45 ? 154 GLU A CG 1 ATOM 534 C CD . GLU A 1 66 ? 8.651 32.013 17.720 1.00 95.15 ? 154 GLU A CD 1 ATOM 535 O OE1 . GLU A 1 66 ? 7.678 31.914 16.938 1.00 97.63 ? 154 GLU A OE1 1 ATOM 536 O OE2 . GLU A 1 66 ? 9.007 31.088 18.482 1.00 102.35 ? 154 GLU A OE2 1 ATOM 537 N N . VAL A 1 67 ? 12.222 34.737 14.704 1.00 60.14 ? 155 VAL A N 1 ATOM 538 C CA . VAL A 1 67 ? 13.014 34.970 13.503 1.00 61.57 ? 155 VAL A CA 1 ATOM 539 C C . VAL A 1 67 ? 12.274 34.535 12.217 1.00 70.06 ? 155 VAL A C 1 ATOM 540 O O . VAL A 1 67 ? 12.779 34.705 11.111 1.00 68.17 ? 155 VAL A O 1 ATOM 541 C CB . VAL A 1 67 ? 14.414 34.313 13.635 1.00 65.80 ? 155 VAL A CB 1 ATOM 542 C CG1 . VAL A 1 67 ? 14.341 32.827 13.313 1.00 69.58 ? 155 VAL A CG1 1 ATOM 543 C CG2 . VAL A 1 67 ? 15.450 35.026 12.765 1.00 78.23 ? 155 VAL A CG2 1 ATOM 544 N N . THR A 1 68 ? 11.065 33.999 12.376 1.00 70.28 ? 156 THR A N 1 ATOM 545 C CA . THR A 1 68 ? 10.214 33.632 11.244 1.00 69.17 ? 156 THR A CA 1 ATOM 546 C C . THR A 1 68 ? 9.278 34.783 10.849 1.00 73.19 ? 156 THR A C 1 ATOM 547 O O . THR A 1 68 ? 8.731 34.795 9.748 1.00 85.92 ? 156 THR A O 1 ATOM 548 C CB . THR A 1 68 ? 9.353 32.382 11.559 1.00 66.12 ? 156 THR A CB 1 ATOM 549 O OG1 . THR A 1 68 ? 8.765 32.535 12.865 1.00 78.61 ? 156 THR A OG1 1 ATOM 550 C CG2 . THR A 1 68 ? 10.195 31.100 11.514 1.00 68.88 ? 156 THR A CG2 1 ATOM 551 N N . ASP A 1 69 ? 9.097 35.747 11.742 1.00 55.63 ? 157 ASP A N 1 ATOM 552 C CA . ASP A 1 69 ? 8.206 36.887 11.491 1.00 62.62 ? 157 ASP A CA 1 ATOM 553 C C . ASP A 1 69 ? 8.906 38.022 10.737 1.00 57.38 ? 157 ASP A C 1 ATOM 554 O O . ASP A 1 69 ? 9.798 38.706 11.271 1.00 51.53 ? 157 ASP A O 1 ATOM 555 C CB . ASP A 1 69 ? 7.631 37.483 12.792 1.00 60.79 ? 157 ASP A CB 1 ATOM 556 C CG . ASP A 1 69 ? 7.074 36.430 13.758 1.00 71.57 ? 157 ASP A CG 1 ATOM 557 O OD1 . ASP A 1 69 ? 6.011 35.835 13.471 1.00 79.23 ? 157 ASP A OD1 1 ATOM 558 O OD2 . ASP A 1 69 ? 7.679 36.238 14.836 1.00 63.35 ? 157 ASP A OD2 1 ATOM 559 N N . PHE A 1 70 ? 8.452 38.254 9.517 1.00 53.00 ? 158 PHE A N 1 ATOM 560 C CA . PHE A 1 70 ? 8.994 39.303 8.665 1.00 53.23 ? 158 PHE A CA 1 ATOM 561 C C . PHE A 1 70 ? 8.804 40.647 9.323 1.00 50.53 ? 158 PHE A C 1 ATOM 562 O O . PHE A 1 70 ? 7.719 40.932 9.806 1.00 48.61 ? 158 PHE A O 1 ATOM 563 C CB . PHE A 1 70 ? 8.258 39.313 7.321 1.00 55.80 ? 158 PHE A CB 1 ATOM 564 C CG . PHE A 1 70 ? 8.680 40.443 6.413 1.00 58.71 ? 158 PHE A CG 1 ATOM 565 C CD1 . PHE A 1 70 ? 9.686 40.263 5.486 1.00 61.66 ? 158 PHE A CD1 1 ATOM 566 C CD2 . PHE A 1 70 ? 8.087 41.695 6.509 1.00 55.18 ? 158 PHE A CD2 1 ATOM 567 C CE1 . PHE A 1 70 ? 10.098 41.308 4.661 1.00 62.17 ? 158 PHE A CE1 1 ATOM 568 C CE2 . PHE A 1 70 ? 8.492 42.734 5.690 1.00 57.58 ? 158 PHE A CE2 1 ATOM 569 C CZ . PHE A 1 70 ? 9.494 42.542 4.761 1.00 58.03 ? 158 PHE A CZ 1 ATOM 570 N N . PRO A 1 71 ? 9.825 41.523 9.279 1.00 51.56 ? 159 PRO A N 1 ATOM 571 C CA . PRO A 1 71 ? 11.118 41.435 8.587 1.00 56.67 ? 159 PRO A CA 1 ATOM 572 C C . PRO A 1 71 ? 12.281 40.943 9.463 1.00 57.75 ? 159 PRO A C 1 ATOM 573 O O . PRO A 1 71 ? 13.454 41.196 9.158 1.00 57.18 ? 159 PRO A O 1 ATOM 574 C CB . PRO A 1 71 ? 11.380 42.885 8.214 1.00 53.71 ? 159 PRO A CB 1 ATOM 575 C CG . PRO A 1 71 ? 10.830 43.655 9.420 1.00 50.62 ? 159 PRO A CG 1 ATOM 576 C CD . PRO A 1 71 ? 9.620 42.855 9.887 1.00 51.07 ? 159 PRO A CD 1 ATOM 577 N N . PHE A 1 72 ? 11.962 40.241 10.539 1.00 56.59 ? 160 PHE A N 1 ATOM 578 C CA . PHE A 1 72 ? 12.984 39.727 11.438 1.00 54.76 ? 160 PHE A CA 1 ATOM 579 C C . PHE A 1 72 ? 13.630 38.464 10.883 1.00 61.33 ? 160 PHE A C 1 ATOM 580 O O . PHE A 1 72 ? 14.460 37.845 11.552 1.00 62.62 ? 160 PHE A O 1 ATOM 581 C CB . PHE A 1 72 ? 12.375 39.480 12.818 1.00 52.65 ? 160 PHE A CB 1 ATOM 582 C CG . PHE A 1 72 ? 11.910 40.734 13.497 1.00 55.52 ? 160 PHE A CG 1 ATOM 583 C CD1 . PHE A 1 72 ? 10.620 41.210 13.302 1.00 47.27 ? 160 PHE A CD1 1 ATOM 584 C CD2 . PHE A 1 72 ? 12.758 41.440 14.337 1.00 51.95 ? 160 PHE A CD2 1 ATOM 585 C CE1 . PHE A 1 72 ? 10.188 42.359 13.907 1.00 44.93 ? 160 PHE A CE1 1 ATOM 586 C CE2 . PHE A 1 72 ? 12.334 42.593 14.935 1.00 48.95 ? 160 PHE A CE2 1 ATOM 587 C CZ . PHE A 1 72 ? 11.045 43.054 14.741 1.00 51.29 ? 160 PHE A CZ 1 ATOM 588 N N . ASN A 1 73 ? 13.234 38.074 9.669 1.00 59.46 ? 161 ASN A N 1 ATOM 589 C CA . ASN A 1 73 ? 13.920 37.020 8.924 1.00 67.33 ? 161 ASN A CA 1 ATOM 590 C C . ASN A 1 73 ? 14.946 37.584 7.934 1.00 71.95 ? 161 ASN A C 1 ATOM 591 O O . ASN A 1 73 ? 15.501 36.847 7.129 1.00 69.15 ? 161 ASN A O 1 ATOM 592 C CB . ASN A 1 73 ? 12.916 36.140 8.148 1.00 69.89 ? 161 ASN A CB 1 ATOM 593 C CG . ASN A 1 73 ? 12.091 36.943 7.135 1.00 70.75 ? 161 ASN A CG 1 ATOM 594 O OD1 . ASN A 1 73 ? 11.946 38.158 7.269 1.00 73.91 ? 161 ASN A OD1 1 ATOM 595 N ND2 . ASN A 1 73 ? 11.543 36.263 6.128 1.00 73.43 ? 161 ASN A ND2 1 ATOM 596 N N . THR A 1 74 ? 15.191 38.890 7.973 1.00 69.87 ? 162 THR A N 1 ATOM 597 C CA . THR A 1 74 ? 16.103 39.489 6.993 1.00 74.39 ? 162 THR A CA 1 ATOM 598 C C . THR A 1 74 ? 17.533 39.530 7.511 1.00 75.86 ? 162 THR A C 1 ATOM 599 O O . THR A 1 74 ? 17.775 39.376 8.708 1.00 69.31 ? 162 THR A O 1 ATOM 600 C CB . THR A 1 74 ? 15.672 40.909 6.595 1.00 73.18 ? 162 THR A CB 1 ATOM 601 O OG1 . THR A 1 74 ? 15.628 41.734 7.767 1.00 63.15 ? 162 THR A OG1 1 ATOM 602 C CG2 . THR A 1 74 ? 14.293 40.881 5.916 1.00 64.46 ? 162 THR A CG2 1 ATOM 603 N N . SER A 1 75 ? 18.468 39.769 6.598 1.00 73.76 ? 163 SER A N 1 ATOM 604 C CA . SER A 1 75 ? 19.883 39.652 6.914 1.00 91.51 ? 163 SER A CA 1 ATOM 605 C C . SER A 1 75 ? 20.326 40.546 8.077 1.00 76.66 ? 163 SER A C 1 ATOM 606 O O . SER A 1 75 ? 21.159 40.146 8.882 1.00 93.89 ? 163 SER A O 1 ATOM 607 C CB . SER A 1 75 ? 20.731 39.939 5.676 1.00 92.05 ? 163 SER A CB 1 ATOM 608 O OG . SER A 1 75 ? 20.720 41.320 5.388 1.00 94.97 ? 163 SER A OG 1 ATOM 609 N N . GLU A 1 76 ? 19.771 41.748 8.167 1.00 73.92 ? 164 GLU A N 1 ATOM 610 C CA . GLU A 1 76 ? 20.210 42.686 9.190 1.00 83.49 ? 164 GLU A CA 1 ATOM 611 C C . GLU A 1 76 ? 19.847 42.200 10.592 1.00 83.06 ? 164 GLU A C 1 ATOM 612 O O . GLU A 1 76 ? 20.493 42.580 11.574 1.00 89.22 ? 164 GLU A O 1 ATOM 613 C CB . GLU A 1 76 ? 19.630 44.080 8.944 1.00 82.56 ? 164 GLU A CB 1 ATOM 614 C CG . GLU A 1 76 ? 18.120 44.154 9.041 1.00 81.44 ? 164 GLU A CG 1 ATOM 615 C CD . GLU A 1 76 ? 17.620 45.568 9.301 1.00 85.32 ? 164 GLU A CD 1 ATOM 616 O OE1 . GLU A 1 76 ? 16.550 45.934 8.762 1.00 88.18 ? 164 GLU A OE1 1 ATOM 617 O OE2 . GLU A 1 76 ? 18.290 46.310 10.053 1.00 87.19 ? 164 GLU A OE2 1 ATOM 618 N N . TRP A 1 77 ? 18.828 41.346 10.675 1.00 76.62 ? 165 TRP A N 1 ATOM 619 C CA . TRP A 1 77 ? 18.352 40.834 11.966 1.00 70.98 ? 165 TRP A CA 1 ATOM 620 C C . TRP A 1 77 ? 18.888 39.460 12.298 1.00 73.58 ? 165 TRP A C 1 ATOM 621 O O . TRP A 1 77 ? 18.414 38.818 13.239 1.00 79.09 ? 165 TRP A O 1 ATOM 622 C CB . TRP A 1 77 ? 16.835 40.780 11.998 1.00 61.68 ? 165 TRP A CB 1 ATOM 623 C CG . TRP A 1 77 ? 16.275 42.088 12.234 1.00 68.34 ? 165 TRP A CG 1 ATOM 624 C CD1 . TRP A 1 77 ? 15.752 42.941 11.311 1.00 71.76 ? 165 TRP A CD1 1 ATOM 625 C CD2 . TRP A 1 77 ? 16.195 42.753 13.494 1.00 62.35 ? 165 TRP A CD2 1 ATOM 626 N NE1 . TRP A 1 77 ? 15.330 44.099 11.930 1.00 75.05 ? 165 TRP A NE1 1 ATOM 627 C CE2 . TRP A 1 77 ? 15.600 44.007 13.268 1.00 54.92 ? 165 TRP A CE2 1 ATOM 628 C CE3 . TRP A 1 77 ? 16.574 42.406 14.794 1.00 60.80 ? 165 TRP A CE3 1 ATOM 629 C CZ2 . TRP A 1 77 ? 15.364 44.916 14.297 1.00 64.34 ? 165 TRP A CZ2 1 ATOM 630 C CZ3 . TRP A 1 77 ? 16.340 43.304 15.813 1.00 60.95 ? 165 TRP A CZ3 1 ATOM 631 C CH2 . TRP A 1 77 ? 15.738 44.544 15.560 1.00 53.09 ? 165 TRP A CH2 1 ATOM 632 N N . GLU A 1 78 ? 19.870 39.013 11.525 1.00 75.88 ? 166 GLU A N 1 ATOM 633 C CA . GLU A 1 78 ? 20.435 37.693 11.715 1.00 76.64 ? 166 GLU A CA 1 ATOM 634 C C . GLU A 1 78 ? 21.083 37.567 13.091 1.00 85.06 ? 166 GLU A C 1 ATOM 635 O O . GLU A 1 78 ? 21.900 38.406 13.486 1.00 85.03 ? 166 GLU A O 1 ATOM 636 C CB . GLU A 1 78 ? 21.435 37.379 10.592 1.00 81.40 ? 166 GLU A CB 1 ATOM 637 C CG . GLU A 1 78 ? 21.833 35.921 10.498 1.00 85.32 ? 166 GLU A CG 1 ATOM 638 C CD . GLU A 1 78 ? 22.958 35.549 11.457 1.00 101.81 ? 166 GLU A CD 1 ATOM 639 O OE1 . GLU A 1 78 ? 23.898 36.357 11.621 1.00 105.13 ? 166 GLU A OE1 1 ATOM 640 O OE2 . GLU A 1 78 ? 22.901 34.449 12.049 1.00 101.95 ? 166 GLU A OE2 1 ATOM 641 N N . GLY A 1 79 ? 20.682 36.534 13.830 1.00 82.47 ? 167 GLY A N 1 ATOM 642 C CA . GLY A 1 79 ? 21.332 36.185 15.083 1.00 83.08 ? 167 GLY A CA 1 ATOM 643 C C . GLY A 1 79 ? 20.981 37.118 16.222 1.00 85.87 ? 167 GLY A C 1 ATOM 644 O O . GLY A 1 79 ? 21.554 37.034 17.317 1.00 84.82 ? 167 GLY A O 1 ATOM 645 N N . TYR A 1 80 ? 20.027 38.007 15.971 1.00 83.14 ? 168 TYR A N 1 ATOM 646 C CA . TYR A 1 80 ? 19.677 39.015 16.950 1.00 70.74 ? 168 TYR A CA 1 ATOM 647 C C . TYR A 1 80 ? 18.629 38.545 17.955 1.00 74.21 ? 168 TYR A C 1 ATOM 648 O O . TYR A 1 80 ? 18.732 38.858 19.139 1.00 69.68 ? 168 TYR A O 1 ATOM 649 C CB . TYR A 1 80 ? 19.259 40.330 16.274 1.00 68.86 ? 168 TYR A CB 1 ATOM 650 C CG . TYR A 1 80 ? 20.417 41.280 16.064 1.00 76.61 ? 168 TYR A CG 1 ATOM 651 C CD1 . TYR A 1 80 ? 21.136 41.767 17.153 1.00 83.76 ? 168 TYR A CD1 1 ATOM 652 C CD2 . TYR A 1 80 ? 20.799 41.691 14.788 1.00 77.53 ? 168 TYR A CD2 1 ATOM 653 C CE1 . TYR A 1 80 ? 22.205 42.628 16.982 1.00 82.30 ? 168 TYR A CE1 1 ATOM 654 C CE2 . TYR A 1 80 ? 21.872 42.559 14.606 1.00 82.22 ? 168 TYR A CE2 1 ATOM 655 C CZ . TYR A 1 80 ? 22.566 43.023 15.716 1.00 85.63 ? 168 TYR A CZ 1 ATOM 656 O OH . TYR A 1 80 ? 23.628 43.882 15.574 1.00 88.05 ? 168 TYR A OH 1 ATOM 657 N N . LEU A 1 81 ? 17.630 37.792 17.497 1.00 73.09 ? 169 LEU A N 1 ATOM 658 C CA . LEU A 1 81 ? 16.585 37.311 18.398 1.00 73.23 ? 169 LEU A CA 1 ATOM 659 C C . LEU A 1 81 ? 17.085 36.050 19.087 1.00 80.57 ? 169 LEU A C 1 ATOM 660 O O . LEU A 1 81 ? 17.961 35.368 18.562 1.00 78.94 ? 169 LEU A O 1 ATOM 661 C CB . LEU A 1 81 ? 15.293 37.022 17.637 1.00 70.82 ? 169 LEU A CB 1 ATOM 662 C CG . LEU A 1 81 ? 14.747 38.129 16.736 1.00 57.35 ? 169 LEU A CG 1 ATOM 663 C CD1 . LEU A 1 81 ? 13.379 37.730 16.266 1.00 55.61 ? 169 LEU A CD1 1 ATOM 664 C CD2 . LEU A 1 81 ? 14.666 39.462 17.466 1.00 56.76 ? 169 LEU A CD2 1 ATOM 665 N N . PRO A 1 82 ? 16.558 35.751 20.283 1.00 81.88 ? 170 PRO A N 1 ATOM 666 C CA . PRO A 1 82 ? 16.975 34.539 21.001 1.00 84.92 ? 170 PRO A CA 1 ATOM 667 C C . PRO A 1 82 ? 16.619 33.275 20.223 1.00 84.78 ? 170 PRO A C 1 ATOM 668 O O . PRO A 1 82 ? 15.540 33.206 19.616 1.00 79.94 ? 170 PRO A O 1 ATOM 669 C CB . PRO A 1 82 ? 16.168 34.609 22.305 1.00 85.94 ? 170 PRO A CB 1 ATOM 670 C CG . PRO A 1 82 ? 15.871 36.070 22.489 1.00 78.68 ? 170 PRO A CG 1 ATOM 671 C CD . PRO A 1 82 ? 15.674 36.604 21.095 1.00 76.43 ? 170 PRO A CD 1 ATOM 672 N N . LYS A 1 83 ? 17.530 32.302 20.234 1.00 89.52 ? 171 LYS A N 1 ATOM 673 C CA . LYS A 1 83 ? 17.346 31.048 19.514 1.00 95.61 ? 171 LYS A CA 1 ATOM 674 C C . LYS A 1 83 ? 16.156 30.270 20.062 1.00 96.75 ? 171 LYS A C 1 ATOM 675 O O . LYS A 1 83 ? 15.368 29.704 19.297 1.00 98.80 ? 171 LYS A O 1 ATOM 676 C CB . LYS A 1 83 ? 18.606 30.179 19.609 1.00 103.89 ? 171 LYS A CB 1 ATOM 677 C CG . LYS A 1 83 ? 19.851 30.737 18.923 1.00 105.88 ? 171 LYS A CG 1 ATOM 678 C CD . LYS A 1 83 ? 20.022 30.148 17.534 1.00 109.75 ? 171 LYS A CD 1 ATOM 679 C CE . LYS A 1 83 ? 21.424 30.393 16.988 1.00 116.30 ? 171 LYS A CE 1 ATOM 680 N NZ . LYS A 1 83 ? 21.715 29.569 15.764 1.00 118.24 ? 171 LYS A NZ 1 ATOM 681 N N . GLU A 1 84 ? 16.031 30.244 21.387 1.00 90.23 ? 172 GLU A N 1 ATOM 682 C CA . GLU A 1 84 ? 15.012 29.427 22.039 1.00 92.23 ? 172 GLU A CA 1 ATOM 683 C C . GLU A 1 84 ? 13.766 30.225 22.398 1.00 79.83 ? 172 GLU A C 1 ATOM 684 O O . GLU A 1 84 ? 13.817 31.440 22.555 1.00 74.18 ? 172 GLU A O 1 ATOM 685 C CB . GLU A 1 84 ? 15.563 28.760 23.302 1.00 107.81 ? 172 GLU A CB 1 ATOM 686 C CG . GLU A 1 84 ? 16.731 27.816 23.078 1.00 124.02 ? 172 GLU A CG 1 ATOM 687 C CD . GLU A 1 84 ? 18.030 28.551 22.832 1.00 132.98 ? 172 GLU A CD 1 ATOM 688 O OE1 . GLU A 1 84 ? 18.128 29.734 23.231 1.00 130.63 ? 172 GLU A OE1 1 ATOM 689 O OE2 . GLU A 1 84 ? 18.942 27.948 22.225 1.00 140.09 ? 172 GLU A OE2 1 ATOM 690 N N . SER A 1 85 ? 12.646 29.520 22.522 1.00 79.73 ? 173 SER A N 1 ATOM 691 C CA . SER A 1 85 ? 11.391 30.129 22.918 1.00 74.52 ? 173 SER A CA 1 ATOM 692 C C . SER A 1 85 ? 11.534 30.598 24.355 1.00 84.33 ? 173 SER A C 1 ATOM 693 O O . SER A 1 85 ? 12.291 30.008 25.128 1.00 89.14 ? 173 SER A O 1 ATOM 694 C CB . SER A 1 85 ? 10.253 29.116 22.812 1.00 86.77 ? 173 SER A CB 1 ATOM 695 O OG . SER A 1 85 ? 9.008 29.731 23.089 1.00 98.06 ? 173 SER A OG 1 ATOM 696 N N . ILE A 1 86 ? 10.821 31.661 24.719 1.00 75.10 ? 174 ILE A N 1 ATOM 697 C CA . ILE A 1 86 ? 10.895 32.152 26.082 1.00 70.51 ? 174 ILE A CA 1 ATOM 698 C C . ILE A 1 86 ? 10.413 31.065 27.039 1.00 80.84 ? 174 ILE A C 1 ATOM 699 O O . ILE A 1 86 ? 11.036 30.803 28.068 1.00 81.54 ? 174 ILE A O 1 ATOM 700 C CB . ILE A 1 86 ? 10.109 33.436 26.263 1.00 67.40 ? 174 ILE A CB 1 ATOM 701 C CG1 . ILE A 1 86 ? 10.020 33.770 27.752 1.00 71.99 ? 174 ILE A CG1 1 ATOM 702 C CG2 . ILE A 1 86 ? 8.730 33.324 25.600 1.00 62.61 ? 174 ILE A CG2 1 ATOM 703 C CD1 . ILE A 1 86 ? 9.405 35.092 28.022 1.00 67.39 ? 174 ILE A CD1 1 ATOM 704 N N . ARG A 1 87 ? 9.342 30.386 26.642 1.00 85.53 ? 175 ARG A N 1 ATOM 705 C CA . ARG A 1 87 ? 8.842 29.214 27.346 1.00 85.12 ? 175 ARG A CA 1 ATOM 706 C C . ARG A 1 87 ? 9.895 28.134 27.560 1.00 86.57 ? 175 ARG A C 1 ATOM 707 O O . ARG A 1 87 ? 9.786 27.341 28.484 1.00 93.01 ? 175 ARG A O 1 ATOM 708 C CB . ARG A 1 87 ? 7.644 28.649 26.592 1.00 80.53 ? 175 ARG A CB 1 ATOM 709 C CG . ARG A 1 87 ? 6.474 29.621 26.590 1.00 80.27 ? 175 ARG A CG 1 ATOM 710 C CD . ARG A 1 87 ? 5.533 29.283 25.476 1.00 83.32 ? 175 ARG A CD 1 ATOM 711 N NE . ARG A 1 87 ? 4.129 29.441 25.837 1.00 81.81 ? 175 ARG A NE 1 ATOM 712 C CZ . ARG A 1 87 ? 3.391 30.517 25.579 1.00 75.41 ? 175 ARG A CZ 1 ATOM 713 N NH1 . ARG A 1 87 ? 3.909 31.586 24.966 1.00 66.98 ? 175 ARG A NH1 1 ATOM 714 N NH2 . ARG A 1 87 ? 2.119 30.517 25.935 1.00 78.33 ? 175 ARG A NH2 1 ATOM 715 N N . THR A 1 88 ? 10.913 28.103 26.708 1.00 94.54 ? 176 THR A N 1 ATOM 716 C CA . THR A 1 88 ? 12.023 27.167 26.879 1.00 100.44 ? 176 THR A CA 1 ATOM 717 C C . THR A 1 88 ? 12.979 27.739 27.912 1.00 104.40 ? 176 THR A C 1 ATOM 718 O O . THR A 1 88 ? 13.486 27.025 28.774 1.00 113.58 ? 176 THR A O 1 ATOM 719 C CB . THR A 1 88 ? 12.799 26.948 25.557 1.00 97.82 ? 176 THR A CB 1 ATOM 720 O OG1 . THR A 1 88 ? 11.938 26.355 24.574 1.00 100.60 ? 176 THR A OG1 1 ATOM 721 C CG2 . THR A 1 88 ? 14.015 26.060 25.771 1.00 99.87 ? 176 THR A CG2 1 ATOM 722 N N . LYS A 1 89 ? 13.201 29.047 27.822 1.00 99.25 ? 177 LYS A N 1 ATOM 723 C CA . LYS A 1 89 ? 14.181 29.727 28.654 1.00 103.23 ? 177 LYS A CA 1 ATOM 724 C C . LYS A 1 89 ? 13.627 30.006 30.050 1.00 106.08 ? 177 LYS A C 1 ATOM 725 O O . LYS A 1 89 ? 14.386 30.122 31.015 1.00 110.37 ? 177 LYS A O 1 ATOM 726 C CB . LYS A 1 89 ? 14.607 31.040 27.987 1.00 102.20 ? 177 LYS A CB 1 ATOM 727 C CG . LYS A 1 89 ? 16.108 31.187 27.720 1.00 110.56 ? 177 LYS A CG 1 ATOM 728 C CD . LYS A 1 89 ? 16.601 30.321 26.561 1.00 116.47 ? 177 LYS A CD 1 ATOM 729 C CE . LYS A 1 89 ? 18.069 30.604 26.241 1.00 119.25 ? 177 LYS A CE 1 ATOM 730 N NZ . LYS A 1 89 ? 18.252 31.927 25.561 1.00 114.57 ? 177 LYS A NZ 1 ATOM 731 N N . ALA A 1 90 ? 12.302 30.094 30.154 1.00 102.46 ? 178 ALA A N 1 ATOM 732 C CA . ALA A 1 90 ? 11.650 30.528 31.392 1.00 98.64 ? 178 ALA A CA 1 ATOM 733 C C . ALA A 1 90 ? 10.711 29.489 32.016 1.00 103.95 ? 178 ALA A C 1 ATOM 734 O O . ALA A 1 90 ? 9.596 29.280 31.536 1.00 104.71 ? 178 ALA A O 1 ATOM 735 C CB . ALA A 1 90 ? 10.901 31.825 31.152 1.00 86.20 ? 178 ALA A CB 1 ATOM 736 N N . GLY A 1 91 ? 11.158 28.866 33.102 1.00 106.67 ? 179 GLY A N 1 ATOM 737 C CA . GLY A 1 91 ? 10.353 27.877 33.794 1.00 107.30 ? 179 GLY A CA 1 ATOM 738 C C . GLY A 1 91 ? 10.007 26.718 32.874 1.00 112.84 ? 179 GLY A C 1 ATOM 739 O O . GLY A 1 91 ? 10.852 26.317 32.075 1.00 117.61 ? 179 GLY A O 1 ATOM 740 N N . PRO A 1 92 ? 8.758 26.204 32.939 1.00 110.50 ? 180 PRO A N 1 ATOM 741 C CA . PRO A 1 92 ? 7.596 26.697 33.690 1.00 105.62 ? 180 PRO A CA 1 ATOM 742 C C . PRO A 1 92 ? 7.805 26.601 35.196 1.00 111.61 ? 180 PRO A C 1 ATOM 743 O O . PRO A 1 92 ? 8.436 25.659 35.676 1.00 121.76 ? 180 PRO A O 1 ATOM 744 C CB . PRO A 1 92 ? 6.463 25.745 33.265 1.00 105.43 ? 180 PRO A CB 1 ATOM 745 C CG . PRO A 1 92 ? 6.975 25.011 32.076 1.00 109.24 ? 180 PRO A CG 1 ATOM 746 C CD . PRO A 1 92 ? 8.451 24.927 32.277 1.00 113.92 ? 180 PRO A CD 1 ATOM 747 N N . TRP A 1 93 ? 7.280 27.580 35.921 1.00 105.40 ? 181 TRP A N 1 ATOM 748 C CA . TRP A 1 93 ? 7.578 27.751 37.336 1.00 108.35 ? 181 TRP A CA 1 ATOM 749 C C . TRP A 1 93 ? 6.363 27.510 38.215 1.00 111.48 ? 181 TRP A C 1 ATOM 750 O O . TRP A 1 93 ? 5.229 27.553 37.742 1.00 103.83 ? 181 TRP A O 1 ATOM 751 C CB . TRP A 1 93 ? 8.072 29.167 37.587 1.00 103.04 ? 181 TRP A CB 1 ATOM 752 C CG . TRP A 1 93 ? 9.431 29.467 37.049 1.00 103.21 ? 181 TRP A CG 1 ATOM 753 C CD1 . TRP A 1 93 ? 10.593 28.790 37.314 1.00 111.15 ? 181 TRP A CD1 1 ATOM 754 C CD2 . TRP A 1 93 ? 9.788 30.559 36.193 1.00 98.42 ? 181 TRP A CD2 1 ATOM 755 N NE1 . TRP A 1 93 ? 11.646 29.386 36.656 1.00 110.31 ? 181 TRP A NE1 1 ATOM 756 C CE2 . TRP A 1 93 ? 11.178 30.474 35.963 1.00 100.48 ? 181 TRP A CE2 1 ATOM 757 C CE3 . TRP A 1 93 ? 9.066 31.598 35.591 1.00 92.30 ? 181 TRP A CE3 1 ATOM 758 C CZ2 . TRP A 1 93 ? 11.857 31.390 35.159 1.00 91.03 ? 181 TRP A CZ2 1 ATOM 759 C CZ3 . TRP A 1 93 ? 9.742 32.506 34.792 1.00 88.57 ? 181 TRP A CZ3 1 ATOM 760 C CH2 . TRP A 1 93 ? 11.124 32.396 34.587 1.00 89.98 ? 181 TRP A CH2 1 ATOM 761 N N . GLY A 1 94 ? 6.615 27.298 39.505 1.00 116.16 ? 182 GLY A N 1 ATOM 762 C CA . GLY A 1 94 ? 5.567 26.996 40.466 1.00 121.24 ? 182 GLY A CA 1 ATOM 763 C C . GLY A 1 94 ? 5.018 28.190 41.230 1.00 114.33 ? 182 GLY A C 1 ATOM 764 O O . GLY A 1 94 ? 3.858 28.558 41.060 1.00 109.99 ? 182 GLY A O 1 ATOM 765 N N . ARG A 1 95 ? 5.833 28.780 42.098 1.00 114.70 ? 183 ARG A N 1 ATOM 766 C CA . ARG A 1 95 ? 5.429 30.001 42.793 1.00 106.32 ? 183 ARG A CA 1 ATOM 767 C C . ARG A 1 95 ? 6.047 31.178 42.071 1.00 115.03 ? 183 ARG A C 1 ATOM 768 O O . ARG A 1 95 ? 7.256 31.209 41.853 1.00 119.50 ? 183 ARG A O 1 ATOM 769 C CB . ARG A 1 95 ? 5.888 29.994 44.259 1.00 111.56 ? 183 ARG A CB 1 ATOM 770 C CG . ARG A 1 95 ? 5.037 29.152 45.212 1.00 118.17 ? 183 ARG A CG 1 ATOM 771 C CD . ARG A 1 95 ? 5.468 29.365 46.673 1.00 122.69 ? 183 ARG A CD 1 ATOM 772 N NE . ARG A 1 95 ? 5.724 30.778 46.955 1.00 116.86 ? 183 ARG A NE 1 ATOM 773 C CZ . ARG A 1 95 ? 6.316 31.237 48.053 1.00 138.09 ? 183 ARG A CZ 1 ATOM 774 N NH1 . ARG A 1 95 ? 6.717 30.392 49.000 1.00 151.52 ? 183 ARG A NH1 1 ATOM 775 N NH2 . ARG A 1 95 ? 6.508 32.543 48.208 1.00 126.10 ? 183 ARG A NH2 1 ATOM 776 N N . CYS A 1 96 ? 5.221 32.138 41.676 1.00 108.25 ? 184 CYS A N 1 ATOM 777 C CA . CYS A 1 96 ? 5.738 33.332 41.030 1.00 86.50 ? 184 CYS A CA 1 ATOM 778 C C . CYS A 1 96 ? 5.129 34.584 41.613 1.00 82.48 ? 184 CYS A C 1 ATOM 779 O O . CYS A 1 96 ? 3.948 34.625 41.951 1.00 82.25 ? 184 CYS A O 1 ATOM 780 C CB . CYS A 1 96 ? 5.454 33.322 39.531 1.00 82.28 ? 184 CYS A CB 1 ATOM 781 S SG . CYS A 1 96 ? 5.924 31.827 38.683 1.00 118.04 ? 184 CYS A SG 1 ATOM 782 N N . ALA A 1 97 ? 5.937 35.628 41.674 1.00 79.53 ? 185 ALA A N 1 ATOM 783 C CA . ALA A 1 97 ? 5.455 36.910 42.147 1.00 79.56 ? 185 ALA A CA 1 ATOM 784 C C . ALA A 1 97 ? 5.602 37.974 41.073 1.00 80.19 ? 185 ALA A C 1 ATOM 785 O O . ALA A 1 97 ? 6.542 37.949 40.275 1.00 83.06 ? 185 ALA A O 1 ATOM 786 C CB . ALA A 1 97 ? 6.197 37.314 43.402 1.00 79.45 ? 185 ALA A CB 1 ATOM 787 N N . VAL A 1 98 ? 4.638 38.887 41.043 1.00 69.96 ? 186 VAL A N 1 ATOM 788 C CA . VAL A 1 98 ? 4.754 40.097 40.273 1.00 65.05 ? 186 VAL A CA 1 ATOM 789 C C . VAL A 1 98 ? 4.887 41.285 41.216 1.00 68.21 ? 186 VAL A C 1 ATOM 790 O O . VAL A 1 98 ? 3.993 41.552 42.011 1.00 72.40 ? 186 VAL A O 1 ATOM 791 C CB . VAL A 1 98 ? 3.542 40.298 39.352 1.00 68.62 ? 186 VAL A CB 1 ATOM 792 C CG1 . VAL A 1 98 ? 3.519 41.708 38.848 1.00 68.49 ? 186 VAL A CG1 1 ATOM 793 C CG2 . VAL A 1 98 ? 3.589 39.302 38.192 1.00 63.51 ? 186 VAL A CG2 1 ATOM 794 N N . VAL A 1 99 ? 6.014 41.986 41.116 1.00 71.03 ? 187 VAL A N 1 ATOM 795 C CA . VAL A 1 99 ? 6.291 43.183 41.906 1.00 67.31 ? 187 VAL A CA 1 ATOM 796 C C . VAL A 1 99 ? 5.935 44.461 41.142 1.00 67.32 ? 187 VAL A C 1 ATOM 797 O O . VAL A 1 99 ? 6.607 44.842 40.162 1.00 59.73 ? 187 VAL A O 1 ATOM 798 C CB . VAL A 1 99 ? 7.789 43.245 42.310 1.00 76.25 ? 187 VAL A CB 1 ATOM 799 C CG1 . VAL A 1 99 ? 8.138 44.596 42.941 1.00 76.85 ? 187 VAL A CG1 1 ATOM 800 C CG2 . VAL A 1 99 ? 8.161 42.089 43.247 1.00 79.42 ? 187 VAL A CG2 1 ATOM 801 N N . SER A 1 100 ? 4.878 45.131 41.581 1.00 61.44 ? 188 SER A N 1 ATOM 802 C CA . SER A 1 100 ? 4.486 46.374 40.937 1.00 61.71 ? 188 SER A CA 1 ATOM 803 C C . SER A 1 100 ? 5.518 47.383 41.381 1.00 48.65 ? 188 SER A C 1 ATOM 804 O O . SER A 1 100 ? 6.308 47.086 42.258 1.00 57.76 ? 188 SER A O 1 ATOM 805 C CB . SER A 1 100 ? 3.072 46.773 41.357 1.00 65.06 ? 188 SER A CB 1 ATOM 806 O OG . SER A 1 100 ? 3.040 48.055 41.945 1.00 67.74 ? 188 SER A OG 1 ATOM 807 N N . SER A 1 101 ? 5.550 48.568 40.798 1.00 52.25 ? 189 SER A N 1 ATOM 808 C CA . SER A 1 101 ? 6.577 49.528 41.227 1.00 50.85 ? 189 SER A CA 1 ATOM 809 C C . SER A 1 101 ? 6.078 50.598 42.182 1.00 47.63 ? 189 SER A C 1 ATOM 810 O O . SER A 1 101 ? 6.807 51.538 42.488 1.00 60.81 ? 189 SER A O 1 ATOM 811 C CB . SER A 1 101 ? 7.219 50.200 40.018 1.00 49.14 ? 189 SER A CB 1 ATOM 812 O OG . SER A 1 101 ? 7.827 49.221 39.192 1.00 58.28 ? 189 SER A OG 1 ATOM 813 N N . ALA A 1 102 ? 4.842 50.448 42.650 1.00 49.05 ? 190 ALA A N 1 ATOM 814 C CA . ALA A 1 102 ? 4.176 51.434 43.524 1.00 51.15 ? 190 ALA A CA 1 ATOM 815 C C . ALA A 1 102 ? 5.001 51.923 44.730 1.00 55.50 ? 190 ALA A C 1 ATOM 816 O O . ALA A 1 102 ? 5.791 51.176 45.298 1.00 60.54 ? 190 ALA A O 1 ATOM 817 C CB . ALA A 1 102 ? 2.841 50.870 44.009 1.00 49.61 ? 190 ALA A CB 1 ATOM 818 N N . GLY A 1 103 ? 4.791 53.181 45.115 1.00 60.05 ? 191 GLY A N 1 ATOM 819 C CA . GLY A 1 103 ? 5.382 53.736 46.325 1.00 61.64 ? 191 GLY A CA 1 ATOM 820 C C . GLY A 1 103 ? 4.874 53.017 47.556 1.00 67.02 ? 191 GLY A C 1 ATOM 821 O O . GLY A 1 103 ? 5.515 53.011 48.607 1.00 66.89 ? 191 GLY A O 1 ATOM 822 N N . SER A 1 104 ? 3.716 52.380 47.423 1.00 67.74 ? 192 SER A N 1 ATOM 823 C CA . SER A 1 104 ? 3.098 51.710 48.565 1.00 60.71 ? 192 SER A CA 1 ATOM 824 C C . SER A 1 104 ? 3.906 50.515 49.051 1.00 64.59 ? 192 SER A C 1 ATOM 825 O O . SER A 1 104 ? 3.603 49.944 50.089 1.00 65.51 ? 192 SER A O 1 ATOM 826 C CB . SER A 1 104 ? 1.685 51.255 48.216 1.00 58.55 ? 192 SER A CB 1 ATOM 827 O OG . SER A 1 104 ? 1.700 50.487 47.022 1.00 72.45 ? 192 SER A OG 1 ATOM 828 N N . LEU A 1 105 ? 4.917 50.105 48.298 1.00 63.90 ? 193 LEU A N 1 ATOM 829 C CA . LEU A 1 105 ? 5.750 49.021 48.786 1.00 65.25 ? 193 LEU A CA 1 ATOM 830 C C . LEU A 1 105 ? 6.670 49.455 49.901 1.00 69.48 ? 193 LEU A C 1 ATOM 831 O O . LEU A 1 105 ? 7.188 48.607 50.602 1.00 73.84 ? 193 LEU A O 1 ATOM 832 C CB . LEU A 1 105 ? 6.594 48.412 47.681 1.00 64.26 ? 193 LEU A CB 1 ATOM 833 C CG . LEU A 1 105 ? 5.781 47.473 46.811 1.00 68.42 ? 193 LEU A CG 1 ATOM 834 C CD1 . LEU A 1 105 ? 6.139 47.721 45.378 1.00 58.32 ? 193 LEU A CD1 1 ATOM 835 C CD2 . LEU A 1 105 ? 6.064 46.056 47.208 1.00 77.91 ? 193 LEU A CD2 1 ATOM 836 N N . LYS A 1 106 ? 6.909 50.759 50.018 1.00 72.18 ? 194 LYS A N 1 ATOM 837 C CA . LYS A 1 106 ? 7.865 51.274 51.006 1.00 74.97 ? 194 LYS A CA 1 ATOM 838 C C . LYS A 1 106 ? 7.475 50.840 52.400 1.00 80.71 ? 194 LYS A C 1 ATOM 839 O O . LYS A 1 106 ? 6.337 51.035 52.809 1.00 81.31 ? 194 LYS A O 1 ATOM 840 C CB . LYS A 1 106 ? 7.977 52.800 50.954 1.00 71.69 ? 194 LYS A CB 1 ATOM 841 C CG . LYS A 1 106 ? 9.024 53.351 51.916 1.00 77.94 ? 194 LYS A CG 1 ATOM 842 C CD . LYS A 1 106 ? 8.933 54.859 52.095 1.00 76.20 ? 194 LYS A CD 1 ATOM 843 C CE . LYS A 1 106 ? 10.206 55.389 52.733 1.00 88.72 ? 194 LYS A CE 1 ATOM 844 N NZ . LYS A 1 106 ? 9.935 56.449 53.750 1.00 93.90 ? 194 LYS A NZ 1 ATOM 845 N N . SER A 1 107 ? 8.425 50.235 53.109 1.00 86.13 ? 195 SER A N 1 ATOM 846 C CA . SER A 1 107 ? 8.248 49.764 54.494 1.00 89.22 ? 195 SER A CA 1 ATOM 847 C C . SER A 1 107 ? 7.141 48.715 54.629 1.00 87.88 ? 195 SER A C 1 ATOM 848 O O . SER A 1 107 ? 6.488 48.623 55.662 1.00 90.32 ? 195 SER A O 1 ATOM 849 C CB . SER A 1 107 ? 8.027 50.930 55.470 1.00 89.05 ? 195 SER A CB 1 ATOM 850 O OG . SER A 1 107 ? 6.715 51.449 55.368 1.00 85.33 ? 195 SER A OG 1 ATOM 851 N N . SER A 1 108 ? 6.937 47.934 53.569 1.00 84.63 ? 196 SER A N 1 ATOM 852 C CA . SER A 1 108 ? 5.977 46.832 53.591 1.00 87.67 ? 196 SER A CA 1 ATOM 853 C C . SER A 1 108 ? 6.585 45.524 54.091 1.00 90.97 ? 196 SER A C 1 ATOM 854 O O . SER A 1 108 ? 5.855 44.594 54.414 1.00 130.55 ? 196 SER A O 1 ATOM 855 C CB . SER A 1 108 ? 5.406 46.599 52.189 1.00 79.80 ? 196 SER A CB 1 ATOM 856 O OG . SER A 1 108 ? 6.415 46.109 51.327 1.00 80.33 ? 196 SER A OG 1 ATOM 857 N N . GLN A 1 109 ? 7.913 45.447 54.121 1.00 93.77 ? 197 GLN A N 1 ATOM 858 C CA . GLN A 1 109 ? 8.632 44.241 54.571 1.00 100.00 ? 197 GLN A CA 1 ATOM 859 C C . GLN A 1 109 ? 8.287 42.946 53.799 1.00 101.71 ? 197 GLN A C 1 ATOM 860 O O . GLN A 1 109 ? 8.271 41.850 54.362 1.00 105.16 ? 197 GLN A O 1 ATOM 861 C CB . GLN A 1 109 ? 8.468 44.041 56.092 1.00 108.71 ? 197 GLN A CB 1 ATOM 862 C CG . GLN A 1 109 ? 8.897 45.248 56.927 1.00 107.65 ? 197 GLN A CG 1 ATOM 863 C CD . GLN A 1 109 ? 8.653 45.057 58.422 1.00 128.38 ? 197 GLN A CD 1 ATOM 864 O OE1 . GLN A 1 109 ? 8.690 43.936 58.939 1.00 119.48 ? 197 GLN A OE1 1 ATOM 865 N NE2 . GLN A 1 109 ? 8.400 46.157 59.120 1.00 113.73 ? 197 GLN A NE2 1 ATOM 866 N N . LEU A 1 110 ? 8.032 43.079 52.497 1.00 94.54 ? 198 LEU A N 1 ATOM 867 C CA . LEU A 1 110 ? 7.681 41.927 51.660 1.00 93.33 ? 198 LEU A CA 1 ATOM 868 C C . LEU A 1 110 ? 8.911 41.176 51.146 1.00 98.02 ? 198 LEU A C 1 ATOM 869 O O . LEU A 1 110 ? 8.808 40.034 50.690 1.00 101.42 ? 198 LEU A O 1 ATOM 870 C CB . LEU A 1 110 ? 6.788 42.377 50.495 1.00 86.30 ? 198 LEU A CB 1 ATOM 871 C CG . LEU A 1 110 ? 5.436 42.931 50.959 1.00 84.34 ? 198 LEU A CG 1 ATOM 872 C CD1 . LEU A 1 110 ? 4.655 43.584 49.843 1.00 77.80 ? 198 LEU A CD1 1 ATOM 873 C CD2 . LEU A 1 110 ? 4.615 41.828 51.596 1.00 89.39 ? 198 LEU A CD2 1 ATOM 874 N N . GLY A 1 111 ? 10.071 41.821 51.252 1.00 102.44 ? 199 GLY A N 1 ATOM 875 C CA . GLY A 1 111 ? 11.326 41.329 50.699 1.00 108.16 ? 199 GLY A CA 1 ATOM 876 C C . GLY A 1 111 ? 11.685 39.859 50.846 1.00 118.16 ? 199 GLY A C 1 ATOM 877 O O . GLY A 1 111 ? 12.227 39.260 49.924 1.00 122.14 ? 199 GLY A O 1 ATOM 878 N N . ARG A 1 112 ? 11.400 39.272 52.000 1.00 125.00 ? 200 ARG A N 1 ATOM 879 C CA . ARG A 1 112 ? 11.690 37.860 52.202 1.00 134.62 ? 200 ARG A CA 1 ATOM 880 C C . ARG A 1 112 ? 10.612 37.004 51.544 1.00 137.23 ? 200 ARG A C 1 ATOM 881 O O . ARG A 1 112 ? 10.909 35.959 50.964 1.00 143.54 ? 200 ARG A O 1 ATOM 882 C CB . ARG A 1 112 ? 11.799 37.522 53.696 1.00 139.79 ? 200 ARG A CB 1 ATOM 883 C CG . ARG A 1 112 ? 12.938 36.570 54.051 1.00 147.32 ? 200 ARG A CG 1 ATOM 884 C CD . ARG A 1 112 ? 12.752 36.008 55.457 1.00 156.57 ? 200 ARG A CD 1 ATOM 885 N NE . ARG A 1 112 ? 13.960 36.078 56.278 1.00 163.59 ? 200 ARG A NE 1 ATOM 886 C CZ . ARG A 1 112 ? 14.018 36.664 57.472 1.00 166.10 ? 200 ARG A CZ 1 ATOM 887 N NH1 . ARG A 1 112 ? 12.938 37.239 57.983 1.00 149.48 ? 200 ARG A NH1 1 ATOM 888 N NH2 . ARG A 1 112 ? 15.155 36.677 58.157 1.00 159.81 ? 200 ARG A NH2 1 ATOM 889 N N . GLU A 1 113 ? 9.362 37.449 51.633 1.00 111.55 ? 201 GLU A N 1 ATOM 890 C CA . GLU A 1 113 ? 8.248 36.669 51.115 1.00 110.29 ? 201 GLU A CA 1 ATOM 891 C C . GLU A 1 113 ? 8.308 36.592 49.594 1.00 117.37 ? 201 GLU A C 1 ATOM 892 O O . GLU A 1 113 ? 8.106 35.524 49.000 1.00 123.22 ? 201 GLU A O 1 ATOM 893 C CB . GLU A 1 113 ? 6.914 37.261 51.552 1.00 107.37 ? 201 GLU A CB 1 ATOM 894 C CG . GLU A 1 113 ? 5.762 36.870 50.641 1.00 117.86 ? 201 GLU A CG 1 ATOM 895 C CD . GLU A 1 113 ? 4.410 37.013 51.297 1.00 117.68 ? 201 GLU A CD 1 ATOM 896 O OE1 . GLU A 1 113 ? 4.367 37.177 52.536 1.00 119.29 ? 201 GLU A OE1 1 ATOM 897 O OE2 . GLU A 1 113 ? 3.391 36.947 50.577 1.00 100.50 ? 201 GLU A OE2 1 ATOM 898 N N . ILE A 1 114 ? 8.591 37.735 48.975 1.00 108.47 ? 202 ILE A N 1 ATOM 899 C CA . ILE A 1 114 ? 8.749 37.822 47.523 1.00 102.64 ? 202 ILE A CA 1 ATOM 900 C C . ILE A 1 114 ? 9.904 36.938 47.049 1.00 104.39 ? 202 ILE A C 1 ATOM 901 O O . ILE A 1 114 ? 9.823 36.331 45.986 1.00 101.62 ? 202 ILE A O 1 ATOM 902 C CB . ILE A 1 114 ? 8.970 39.290 47.076 1.00 96.76 ? 202 ILE A CB 1 ATOM 903 C CG1 . ILE A 1 114 ? 7.722 40.130 47.359 1.00 89.61 ? 202 ILE A CG1 1 ATOM 904 C CG2 . ILE A 1 114 ? 9.321 39.378 45.599 1.00 87.74 ? 202 ILE A CG2 1 ATOM 905 C CD1 . ILE A 1 114 ? 7.864 41.590 46.953 1.00 79.97 ? 202 ILE A CD1 1 ATOM 906 N N . ASP A 1 115 ? 10.961 36.849 47.862 1.00 103.18 ? 203 ASP A N 1 ATOM 907 C CA . ASP A 1 115 ? 12.128 36.013 47.565 1.00 114.09 ? 203 ASP A CA 1 ATOM 908 C C . ASP A 1 115 ? 11.827 34.522 47.628 1.00 124.72 ? 203 ASP A C 1 ATOM 909 O O . ASP A 1 115 ? 12.618 33.699 47.156 1.00 129.54 ? 203 ASP A O 1 ATOM 910 C CB . ASP A 1 115 ? 13.289 36.314 48.519 1.00 116.93 ? 203 ASP A CB 1 ATOM 911 C CG . ASP A 1 115 ? 14.008 37.598 48.180 1.00 118.91 ? 203 ASP A CG 1 ATOM 912 O OD1 . ASP A 1 115 ? 13.685 38.204 47.140 1.00 103.02 ? 203 ASP A OD1 1 ATOM 913 O OD2 . ASP A 1 115 ? 14.898 38.003 48.956 1.00 127.79 ? 203 ASP A OD2 1 ATOM 914 N N . ASP A 1 116 ? 10.694 34.168 48.222 1.00 125.95 ? 204 ASP A N 1 ATOM 915 C CA . ASP A 1 116 ? 10.381 32.760 48.410 1.00 135.78 ? 204 ASP A CA 1 ATOM 916 C C . ASP A 1 116 ? 9.601 32.148 47.238 1.00 133.64 ? 204 ASP A C 1 ATOM 917 O O . ASP A 1 116 ? 9.185 30.990 47.288 1.00 142.36 ? 204 ASP A O 1 ATOM 918 C CB . ASP A 1 116 ? 9.718 32.532 49.772 1.00 138.41 ? 204 ASP A CB 1 ATOM 919 C CG . ASP A 1 116 ? 10.725 32.590 50.914 1.00 143.47 ? 204 ASP A CG 1 ATOM 920 O OD1 . ASP A 1 116 ? 11.799 31.961 50.773 1.00 149.71 ? 204 ASP A OD1 1 ATOM 921 O OD2 . ASP A 1 116 ? 10.462 33.270 51.935 1.00 138.53 ? 204 ASP A OD2 1 ATOM 922 N N . HIS A 1 117 ? 9.443 32.922 46.170 1.00 124.88 ? 205 HIS A N 1 ATOM 923 C CA . HIS A 1 117 ? 8.876 32.406 44.924 1.00 118.23 ? 205 HIS A CA 1 ATOM 924 C C . HIS A 1 117 ? 9.989 31.904 43.999 1.00 107.99 ? 205 HIS A C 1 ATOM 925 O O . HIS A 1 117 ? 11.092 32.447 44.003 1.00 127.04 ? 205 HIS A O 1 ATOM 926 C CB . HIS A 1 117 ? 8.043 33.485 44.225 1.00 98.41 ? 205 HIS A CB 1 ATOM 927 C CG . HIS A 1 117 ? 6.912 34.018 45.055 1.00 139.23 ? 205 HIS A CG 1 ATOM 928 N ND1 . HIS A 1 117 ? 7.101 34.912 46.090 1.00 97.18 ? 205 HIS A ND1 1 ATOM 929 C CD2 . HIS A 1 117 ? 5.579 33.791 44.994 1.00 96.24 ? 205 HIS A CD2 1 ATOM 930 C CE1 . HIS A 1 117 ? 5.933 35.212 46.628 1.00 96.17 ? 205 HIS A CE1 1 ATOM 931 N NE2 . HIS A 1 117 ? 4.994 34.539 45.987 1.00 95.71 ? 205 HIS A NE2 1 ATOM 932 N N . ASP A 1 118 ? 9.698 30.863 43.219 1.00 109.63 ? 206 ASP A N 1 ATOM 933 C CA . ASP A 1 118 ? 10.653 30.325 42.241 1.00 110.85 ? 206 ASP A CA 1 ATOM 934 C C . ASP A 1 118 ? 11.078 31.366 41.198 1.00 103.76 ? 206 ASP A C 1 ATOM 935 O O . ASP A 1 118 ? 12.156 31.259 40.614 1.00 110.41 ? 206 ASP A O 1 ATOM 936 C CB . ASP A 1 118 ? 10.087 29.087 41.524 1.00 113.42 ? 206 ASP A CB 1 ATOM 937 C CG . ASP A 1 118 ? 9.927 27.878 42.448 1.00 126.80 ? 206 ASP A CG 1 ATOM 938 O OD1 . ASP A 1 118 ? 10.938 27.382 43.003 1.00 131.69 ? 206 ASP A OD1 1 ATOM 939 O OD2 . ASP A 1 118 ? 8.780 27.402 42.593 1.00 126.15 ? 206 ASP A OD2 1 ATOM 940 N N . ALA A 1 119 ? 10.239 32.373 40.970 1.00 97.03 ? 207 ALA A N 1 ATOM 941 C CA . ALA A 1 119 ? 10.541 33.387 39.962 1.00 90.63 ? 207 ALA A CA 1 ATOM 942 C C . ALA A 1 119 ? 9.842 34.708 40.227 1.00 92.93 ? 207 ALA A C 1 ATOM 943 O O . ALA A 1 119 ? 8.664 34.747 40.599 1.00 85.77 ? 207 ALA A O 1 ATOM 944 C CB . ALA A 1 119 ? 10.185 32.884 38.589 1.00 88.29 ? 207 ALA A CB 1 ATOM 945 N N . VAL A 1 120 ? 10.575 35.794 40.008 1.00 96.17 ? 208 VAL A N 1 ATOM 946 C CA . VAL A 1 120 ? 10.071 37.127 40.294 1.00 91.12 ? 208 VAL A CA 1 ATOM 947 C C . VAL A 1 120 ? 10.147 38.071 39.098 1.00 82.56 ? 208 VAL A C 1 ATOM 948 O O . VAL A 1 120 ? 11.196 38.193 38.468 1.00 82.68 ? 208 VAL A O 1 ATOM 949 C CB . VAL A 1 120 ? 10.829 37.749 41.472 1.00 79.75 ? 208 VAL A CB 1 ATOM 950 C CG1 . VAL A 1 120 ? 10.461 39.207 41.617 1.00 74.92 ? 208 VAL A CG1 1 ATOM 951 C CG2 . VAL A 1 120 ? 10.514 36.983 42.727 1.00 85.12 ? 208 VAL A CG2 1 ATOM 952 N N . LEU A 1 121 ? 9.029 38.752 38.828 1.00 73.74 ? 209 LEU A N 1 ATOM 953 C CA . LEU A 1 121 ? 8.895 39.731 37.748 1.00 67.18 ? 209 LEU A CA 1 ATOM 954 C C . LEU A 1 121 ? 8.863 41.204 38.190 1.00 67.21 ? 209 LEU A C 1 ATOM 955 O O . LEU A 1 121 ? 8.028 41.609 39.002 1.00 75.79 ? 209 LEU A O 1 ATOM 956 C CB . LEU A 1 121 ? 7.626 39.449 36.940 1.00 66.92 ? 209 LEU A CB 1 ATOM 957 C CG . LEU A 1 121 ? 7.327 40.482 35.832 1.00 68.31 ? 209 LEU A CG 1 ATOM 958 C CD1 . LEU A 1 121 ? 8.269 40.339 34.684 1.00 69.72 ? 209 LEU A CD1 1 ATOM 959 C CD2 . LEU A 1 121 ? 5.896 40.396 35.341 1.00 54.43 ? 209 LEU A CD2 1 ATOM 960 N N . ARG A 1 122 ? 9.752 42.012 37.619 1.00 69.29 ? 210 ARG A N 1 ATOM 961 C CA . ARG A 1 122 ? 9.841 43.426 37.968 1.00 64.13 ? 210 ARG A CA 1 ATOM 962 C C . ARG A 1 122 ? 9.710 44.260 36.697 1.00 63.84 ? 210 ARG A C 1 ATOM 963 O O . ARG A 1 122 ? 9.685 43.711 35.594 1.00 60.94 ? 210 ARG A O 1 ATOM 964 C CB . ARG A 1 122 ? 11.156 43.696 38.696 1.00 66.20 ? 210 ARG A CB 1 ATOM 965 C CG . ARG A 1 122 ? 11.356 42.749 39.864 1.00 76.51 ? 210 ARG A CG 1 ATOM 966 C CD . ARG A 1 122 ? 12.545 43.081 40.724 1.00 87.38 ? 210 ARG A CD 1 ATOM 967 N NE . ARG A 1 122 ? 12.466 42.341 41.981 1.00 100.39 ? 210 ARG A NE 1 ATOM 968 C CZ . ARG A 1 122 ? 13.233 42.564 43.042 1.00 103.57 ? 210 ARG A CZ 1 ATOM 969 N NH1 . ARG A 1 122 ? 13.078 41.826 44.128 1.00 100.86 ? 210 ARG A NH1 1 ATOM 970 N NH2 . ARG A 1 122 ? 14.155 43.517 43.019 1.00 108.56 ? 210 ARG A NH2 1 ATOM 971 N N . PHE A 1 123 ? 9.607 45.579 36.832 1.00 57.50 ? 211 PHE A N 1 ATOM 972 C CA . PHE A 1 123 ? 9.302 46.401 35.665 1.00 53.98 ? 211 PHE A CA 1 ATOM 973 C C . PHE A 1 123 ? 10.293 47.513 35.405 1.00 58.41 ? 211 PHE A C 1 ATOM 974 O O . PHE A 1 123 ? 10.815 48.117 36.339 1.00 50.62 ? 211 PHE A O 1 ATOM 975 C CB . PHE A 1 123 ? 7.907 47.011 35.804 1.00 49.67 ? 211 PHE A CB 1 ATOM 976 C CG . PHE A 1 123 ? 6.831 45.989 35.906 1.00 54.98 ? 211 PHE A CG 1 ATOM 977 C CD1 . PHE A 1 123 ? 6.393 45.317 34.780 1.00 50.58 ? 211 PHE A CD1 1 ATOM 978 C CD2 . PHE A 1 123 ? 6.266 45.683 37.128 1.00 53.41 ? 211 PHE A CD2 1 ATOM 979 C CE1 . PHE A 1 123 ? 5.400 44.365 34.866 1.00 49.45 ? 211 PHE A CE1 1 ATOM 980 C CE2 . PHE A 1 123 ? 5.272 44.726 37.222 1.00 52.82 ? 211 PHE A CE2 1 ATOM 981 C CZ . PHE A 1 123 ? 4.841 44.066 36.087 1.00 54.95 ? 211 PHE A CZ 1 ATOM 982 N N . ASN A 1 124 ? 10.523 47.799 34.123 1.00 54.26 ? 212 ASN A N 1 ATOM 983 C CA . ASN A 1 124 ? 11.328 48.952 33.755 1.00 54.58 ? 212 ASN A CA 1 ATOM 984 C C . ASN A 1 124 ? 12.613 49.052 34.579 1.00 56.77 ? 212 ASN A C 1 ATOM 985 O O . ASN A 1 124 ? 13.403 48.111 34.610 1.00 65.94 ? 212 ASN A O 1 ATOM 986 C CB . ASN A 1 124 ? 10.486 50.213 33.897 1.00 49.41 ? 212 ASN A CB 1 ATOM 987 C CG . ASN A 1 124 ? 9.272 50.184 33.008 1.00 53.49 ? 212 ASN A CG 1 ATOM 988 O OD1 . ASN A 1 124 ? 9.357 49.796 31.846 1.00 50.68 ? 212 ASN A OD1 1 ATOM 989 N ND2 . ASN A 1 124 ? 8.128 50.589 33.544 1.00 55.09 ? 212 ASN A ND2 1 ATOM 990 N N . GLY A 1 125 ? 12.798 50.162 35.286 1.00 60.29 ? 213 GLY A N 1 ATOM 991 C CA . GLY A 1 125 ? 14.045 50.393 35.992 1.00 59.73 ? 213 GLY A CA 1 ATOM 992 C C . GLY A 1 125 ? 13.950 50.201 37.492 1.00 67.36 ? 213 GLY A C 1 ATOM 993 O O . GLY A 1 125 ? 14.748 50.762 38.254 1.00 75.75 ? 213 GLY A O 1 ATOM 994 N N . ALA A 1 126 ? 12.971 49.413 37.923 1.00 65.56 ? 214 ALA A N 1 ATOM 995 C CA . ALA A 1 126 ? 12.741 49.211 39.349 1.00 67.64 ? 214 ALA A CA 1 ATOM 996 C C . ALA A 1 126 ? 13.922 48.460 39.932 1.00 71.61 ? 214 ALA A C 1 ATOM 997 O O . ALA A 1 126 ? 14.173 47.326 39.551 1.00 71.54 ? 214 ALA A O 1 ATOM 998 C CB . ALA A 1 126 ? 11.445 48.443 39.572 1.00 65.56 ? 214 ALA A CB 1 ATOM 999 N N . PRO A 1 127 ? 14.663 49.107 40.841 1.00 70.84 ? 215 PRO A N 1 ATOM 1000 C CA . PRO A 1 127 ? 15.934 48.623 41.390 1.00 74.41 ? 215 PRO A CA 1 ATOM 1001 C C . PRO A 1 127 ? 15.816 47.733 42.623 1.00 80.55 ? 215 PRO A C 1 ATOM 1002 O O . PRO A 1 127 ? 14.801 47.748 43.330 1.00 76.27 ? 215 PRO A O 1 ATOM 1003 C CB . PRO A 1 127 ? 16.650 49.924 41.782 1.00 78.63 ? 215 PRO A CB 1 ATOM 1004 C CG . PRO A 1 127 ? 15.538 50.808 42.212 1.00 70.11 ? 215 PRO A CG 1 ATOM 1005 C CD . PRO A 1 127 ? 14.359 50.467 41.312 1.00 74.04 ? 215 PRO A CD 1 ATOM 1006 N N . THR A 1 128 ? 16.891 46.985 42.871 1.00 89.83 ? 216 THR A N 1 ATOM 1007 C CA . THR A 1 128 ? 17.008 46.070 43.998 1.00 94.17 ? 216 THR A CA 1 ATOM 1008 C C . THR A 1 128 ? 17.834 46.689 45.125 1.00 96.99 ? 216 THR A C 1 ATOM 1009 O O . THR A 1 128 ? 17.489 46.559 46.302 1.00 102.90 ? 216 THR A O 1 ATOM 1010 C CB . THR A 1 128 ? 17.671 44.754 43.553 1.00 99.42 ? 216 THR A CB 1 ATOM 1011 O OG1 . THR A 1 128 ? 16.718 43.965 42.837 1.00 93.79 ? 216 THR A OG1 1 ATOM 1012 C CG2 . THR A 1 128 ? 18.175 43.962 44.748 1.00 113.90 ? 216 THR A CG2 1 ATOM 1013 N N . ALA A 1 129 ? 18.923 47.357 44.753 1.00 97.14 ? 217 ALA A N 1 ATOM 1014 C CA . ALA A 1 129 ? 19.808 48.019 45.709 1.00 106.90 ? 217 ALA A CA 1 ATOM 1015 C C . ALA A 1 129 ? 19.036 48.969 46.618 1.00 109.58 ? 217 ALA A C 1 ATOM 1016 O O . ALA A 1 129 ? 18.224 49.758 46.134 1.00 106.33 ? 217 ALA A O 1 ATOM 1017 C CB . ALA A 1 129 ? 20.902 48.774 44.969 1.00 104.31 ? 217 ALA A CB 1 ATOM 1018 N N . ASN A 1 130 ? 19.293 48.866 47.924 1.00 116.24 ? 218 ASN A N 1 ATOM 1019 C CA . ASN A 1 130 ? 18.692 49.715 48.966 1.00 113.79 ? 218 ASN A CA 1 ATOM 1020 C C . ASN A 1 130 ? 17.253 49.366 49.352 1.00 111.38 ? 218 ASN A C 1 ATOM 1021 O O . ASN A 1 130 ? 16.678 49.992 50.255 1.00 115.93 ? 218 ASN A O 1 ATOM 1022 C CB . ASN A 1 130 ? 18.774 51.209 48.612 1.00 114.23 ? 218 ASN A CB 1 ATOM 1023 C CG . ASN A 1 130 ? 20.162 51.639 48.179 1.00 121.66 ? 218 ASN A CG 1 ATOM 1024 O OD1 . ASN A 1 130 ? 21.160 51.326 48.833 1.00 129.41 ? 218 ASN A OD1 1 ATOM 1025 N ND2 . ASN A 1 130 ? 20.232 52.364 47.067 1.00 116.98 ? 218 ASN A ND2 1 ATOM 1026 N N . PHE A 1 131 ? 16.678 48.369 48.684 1.00 94.29 ? 219 PHE A N 1 ATOM 1027 C CA . PHE A 1 131 ? 15.257 48.067 48.836 1.00 90.14 ? 219 PHE A CA 1 ATOM 1028 C C . PHE A 1 131 ? 15.000 46.593 49.091 1.00 92.46 ? 219 PHE A C 1 ATOM 1029 O O . PHE A 1 131 ? 13.850 46.162 49.122 1.00 89.63 ? 219 PHE A O 1 ATOM 1030 C CB . PHE A 1 131 ? 14.466 48.514 47.592 1.00 83.01 ? 219 PHE A CB 1 ATOM 1031 C CG . PHE A 1 131 ? 14.557 49.986 47.318 1.00 87.45 ? 219 PHE A CG 1 ATOM 1032 C CD1 . PHE A 1 131 ? 13.821 50.891 48.066 1.00 79.79 ? 219 PHE A CD1 1 ATOM 1033 C CD2 . PHE A 1 131 ? 15.383 50.466 46.321 1.00 83.88 ? 219 PHE A CD2 1 ATOM 1034 C CE1 . PHE A 1 131 ? 13.908 52.248 47.829 1.00 92.40 ? 219 PHE A CE1 1 ATOM 1035 C CE2 . PHE A 1 131 ? 15.477 51.824 46.076 1.00 89.96 ? 219 PHE A CE2 1 ATOM 1036 C CZ . PHE A 1 131 ? 14.735 52.716 46.832 1.00 91.54 ? 219 PHE A CZ 1 ATOM 1037 N N . GLN A 1 132 ? 16.066 45.824 49.266 1.00 98.13 ? 220 GLN A N 1 ATOM 1038 C CA . GLN A 1 132 ? 15.937 44.379 49.421 1.00 106.37 ? 220 GLN A CA 1 ATOM 1039 C C . GLN A 1 132 ? 14.837 43.954 50.398 1.00 106.74 ? 220 GLN A C 1 ATOM 1040 O O . GLN A 1 132 ? 14.047 43.064 50.092 1.00 100.36 ? 220 GLN A O 1 ATOM 1041 C CB . GLN A 1 132 ? 17.275 43.742 49.819 1.00 115.04 ? 220 GLN A CB 1 ATOM 1042 C CG . GLN A 1 132 ? 18.262 43.539 48.670 1.00 109.07 ? 220 GLN A CG 1 ATOM 1043 C CD . GLN A 1 132 ? 19.354 44.591 48.642 1.00 115.43 ? 220 GLN A CD 1 ATOM 1044 O OE1 . GLN A 1 132 ? 19.077 45.791 48.714 1.00 109.67 ? 220 GLN A OE1 1 ATOM 1045 N NE2 . GLN A 1 132 ? 20.605 44.146 48.545 1.00 117.10 ? 220 GLN A NE2 1 ATOM 1046 N N . GLN A 1 133 ? 14.768 44.603 51.560 1.00 108.73 ? 221 GLN A N 1 ATOM 1047 C CA . GLN A 1 133 ? 13.827 44.166 52.591 1.00 109.28 ? 221 GLN A CA 1 ATOM 1048 C C . GLN A 1 133 ? 12.364 44.481 52.292 1.00 101.70 ? 221 GLN A C 1 ATOM 1049 O O . GLN A 1 133 ? 11.469 43.801 52.791 1.00 103.18 ? 221 GLN A O 1 ATOM 1050 C CB . GLN A 1 133 ? 14.233 44.654 53.981 1.00 117.72 ? 221 GLN A CB 1 ATOM 1051 C CG . GLN A 1 133 ? 14.203 46.147 54.221 1.00 109.38 ? 221 GLN A CG 1 ATOM 1052 C CD . GLN A 1 133 ? 14.700 46.467 55.628 1.00 127.60 ? 221 GLN A CD 1 ATOM 1053 O OE1 . GLN A 1 133 ? 15.410 45.660 56.236 1.00 131.81 ? 221 GLN A OE1 1 ATOM 1054 N NE2 . GLN A 1 133 ? 14.321 47.630 56.156 1.00 114.64 ? 221 GLN A NE2 1 ATOM 1055 N N . ASP A 1 134 ? 12.127 45.501 51.477 1.00 94.01 ? 222 ASP A N 1 ATOM 1056 C CA . ASP A 1 134 ? 10.779 45.802 51.001 1.00 93.46 ? 222 ASP A CA 1 ATOM 1057 C C . ASP A 1 134 ? 10.390 45.081 49.699 1.00 89.83 ? 222 ASP A C 1 ATOM 1058 O O . ASP A 1 134 ? 9.225 44.739 49.516 1.00 84.47 ? 222 ASP A O 1 ATOM 1059 C CB . ASP A 1 134 ? 10.601 47.311 50.796 1.00 84.04 ? 222 ASP A CB 1 ATOM 1060 C CG . ASP A 1 134 ? 10.557 48.078 52.110 1.00 90.63 ? 222 ASP A CG 1 ATOM 1061 O OD1 . ASP A 1 134 ? 10.302 47.437 53.152 1.00 93.33 ? 222 ASP A OD1 1 ATOM 1062 O OD2 . ASP A 1 134 ? 10.758 49.315 52.093 1.00 85.69 ? 222 ASP A OD2 1 ATOM 1063 N N . VAL A 1 135 ? 11.360 44.842 48.816 1.00 93.37 ? 223 VAL A N 1 ATOM 1064 C CA . VAL A 1 135 ? 11.072 44.477 47.407 1.00 92.97 ? 223 VAL A CA 1 ATOM 1065 C C . VAL A 1 135 ? 11.551 43.069 47.016 1.00 94.39 ? 223 VAL A C 1 ATOM 1066 O O . VAL A 1 135 ? 11.025 42.461 46.070 1.00 83.80 ? 223 VAL A O 1 ATOM 1067 C CB . VAL A 1 135 ? 11.697 45.514 46.444 1.00 76.29 ? 223 VAL A CB 1 ATOM 1068 C CG1 . VAL A 1 135 ? 11.300 45.254 45.006 1.00 138.43 ? 223 VAL A CG1 1 ATOM 1069 C CG2 . VAL A 1 135 ? 11.279 46.911 46.850 1.00 73.95 ? 223 VAL A CG2 1 ATOM 1070 N N . GLY A 1 136 ? 12.532 42.550 47.760 1.00 89.16 ? 224 GLY A N 1 ATOM 1071 C CA . GLY A 1 136 ? 13.210 41.313 47.409 1.00 93.15 ? 224 GLY A CA 1 ATOM 1072 C C . GLY A 1 136 ? 14.588 41.575 46.813 1.00 101.60 ? 224 GLY A C 1 ATOM 1073 O O . GLY A 1 136 ? 14.957 42.733 46.595 1.00 94.02 ? 224 GLY A O 1 ATOM 1074 N N . THR A 1 137 ? 15.348 40.509 46.547 1.00 107.09 ? 225 THR A N 1 ATOM 1075 C CA . THR A 1 137 ? 16.679 40.631 45.936 1.00 110.36 ? 225 THR A CA 1 ATOM 1076 C C . THR A 1 137 ? 16.757 39.997 44.532 1.00 104.47 ? 225 THR A C 1 ATOM 1077 O O . THR A 1 137 ? 17.666 40.296 43.753 1.00 108.01 ? 225 THR A O 1 ATOM 1078 C CB . THR A 1 137 ? 17.775 40.009 46.835 1.00 123.26 ? 225 THR A CB 1 ATOM 1079 O OG1 . THR A 1 137 ? 17.550 40.387 48.199 1.00 130.85 ? 225 THR A OG1 1 ATOM 1080 C CG2 . THR A 1 137 ? 19.169 40.468 46.407 1.00 112.57 ? 225 THR A CG2 1 ATOM 1081 N N . LYS A 1 138 ? 15.799 39.137 44.204 1.00 96.92 ? 226 LYS A N 1 ATOM 1082 C CA . LYS A 1 138 ? 15.884 38.372 42.962 1.00 95.69 ? 226 LYS A CA 1 ATOM 1083 C C . LYS A 1 138 ? 15.088 38.971 41.797 1.00 111.06 ? 226 LYS A C 1 ATOM 1084 O O . LYS A 1 138 ? 13.974 39.463 41.964 1.00 83.82 ? 226 LYS A O 1 ATOM 1085 C CB . LYS A 1 138 ? 15.490 36.912 43.211 1.00 99.88 ? 226 LYS A CB 1 ATOM 1086 C CG . LYS A 1 138 ? 15.946 35.947 42.126 1.00 133.73 ? 226 LYS A CG 1 ATOM 1087 C CD . LYS A 1 138 ? 15.932 34.500 42.611 1.00 141.61 ? 226 LYS A CD 1 ATOM 1088 C CE . LYS A 1 138 ? 16.321 33.529 41.491 1.00 142.17 ? 226 LYS A CE 1 ATOM 1089 N NZ . LYS A 1 138 ? 16.529 32.130 41.978 1.00 147.99 ? 226 LYS A NZ 1 ATOM 1090 N N . THR A 1 139 ? 15.683 38.926 40.609 1.00 114.21 ? 227 THR A N 1 ATOM 1091 C CA . THR A 1 139 ? 15.018 39.347 39.377 1.00 103.11 ? 227 THR A CA 1 ATOM 1092 C C . THR A 1 139 ? 15.175 38.215 38.376 1.00 97.34 ? 227 THR A C 1 ATOM 1093 O O . THR A 1 139 ? 16.289 37.945 37.939 1.00 89.93 ? 227 THR A O 1 ATOM 1094 C CB . THR A 1 139 ? 15.683 40.606 38.772 1.00 103.71 ? 227 THR A CB 1 ATOM 1095 O OG1 . THR A 1 139 ? 15.789 41.630 39.770 1.00 117.20 ? 227 THR A OG1 1 ATOM 1096 C CG2 . THR A 1 139 ? 14.886 41.126 37.583 1.00 88.03 ? 227 THR A CG2 1 ATOM 1097 N N . THR A 1 140 ? 14.085 37.529 38.037 1.00 79.62 ? 228 THR A N 1 ATOM 1098 C CA . THR A 1 140 ? 14.167 36.484 37.016 1.00 90.65 ? 228 THR A CA 1 ATOM 1099 C C . THR A 1 140 ? 13.684 37.011 35.667 1.00 80.08 ? 228 THR A C 1 ATOM 1100 O O . THR A 1 140 ? 14.349 36.801 34.663 1.00 82.46 ? 228 THR A O 1 ATOM 1101 C CB . THR A 1 140 ? 13.443 35.162 37.400 1.00 103.41 ? 228 THR A CB 1 ATOM 1102 O OG1 . THR A 1 140 ? 12.354 35.437 38.287 1.00 101.84 ? 228 THR A OG1 1 ATOM 1103 C CG2 . THR A 1 140 ? 14.411 34.204 38.088 1.00 118.58 ? 228 THR A CG2 1 ATOM 1104 N N . ILE A 1 141 ? 12.545 37.703 35.655 1.00 73.38 ? 229 ILE A N 1 ATOM 1105 C CA . ILE A 1 141 ? 12.064 38.367 34.439 1.00 69.90 ? 229 ILE A CA 1 ATOM 1106 C C . ILE A 1 141 ? 11.827 39.849 34.670 1.00 67.54 ? 229 ILE A C 1 ATOM 1107 O O . ILE A 1 141 ? 11.217 40.240 35.653 1.00 82.27 ? 229 ILE A O 1 ATOM 1108 C CB . ILE A 1 141 ? 10.766 37.760 33.907 1.00 75.48 ? 229 ILE A CB 1 ATOM 1109 C CG1 . ILE A 1 141 ? 10.937 36.278 33.588 1.00 84.31 ? 229 ILE A CG1 1 ATOM 1110 C CG2 . ILE A 1 141 ? 10.364 38.459 32.626 1.00 75.01 ? 229 ILE A CG2 1 ATOM 1111 C CD1 . ILE A 1 141 ? 9.692 35.663 32.970 1.00 65.29 ? 229 ILE A CD1 1 ATOM 1112 N N . ARG A 1 142 ? 12.321 40.679 33.765 1.00 63.34 ? 230 ARG A N 1 ATOM 1113 C CA . ARG A 1 142 ? 12.035 42.100 33.816 1.00 58.83 ? 230 ARG A CA 1 ATOM 1114 C C . ARG A 1 142 ? 11.330 42.561 32.528 1.00 62.83 ? 230 ARG A C 1 ATOM 1115 O O . ARG A 1 142 ? 11.895 42.465 31.445 1.00 59.27 ? 230 ARG A O 1 ATOM 1116 C CB . ARG A 1 142 ? 13.330 42.883 34.048 1.00 61.45 ? 230 ARG A CB 1 ATOM 1117 C CG . ARG A 1 142 ? 13.149 44.402 34.009 1.00 58.38 ? 230 ARG A CG 1 ATOM 1118 C CD . ARG A 1 142 ? 14.459 45.116 34.294 1.00 65.73 ? 230 ARG A CD 1 ATOM 1119 N NE . ARG A 1 142 ? 15.068 44.688 35.556 1.00 74.17 ? 230 ARG A NE 1 ATOM 1120 C CZ . ARG A 1 142 ? 14.879 45.294 36.727 1.00 77.23 ? 230 ARG A CZ 1 ATOM 1121 N NH1 . ARG A 1 142 ? 14.071 46.349 36.814 1.00 64.46 ? 230 ARG A NH1 1 ATOM 1122 N NH2 . ARG A 1 142 ? 15.480 44.831 37.817 1.00 83.58 ? 230 ARG A NH2 1 ATOM 1123 N N . LEU A 1 143 ? 10.091 43.044 32.647 1.00 66.96 ? 231 LEU A N 1 ATOM 1124 C CA . LEU A 1 143 ? 9.341 43.584 31.500 1.00 55.37 ? 231 LEU A CA 1 ATOM 1125 C C . LEU A 1 143 ? 9.507 45.097 31.418 1.00 55.42 ? 231 LEU A C 1 ATOM 1126 O O . LEU A 1 143 ? 9.221 45.805 32.385 1.00 55.04 ? 231 LEU A O 1 ATOM 1127 C CB . LEU A 1 143 ? 7.836 43.261 31.608 1.00 49.43 ? 231 LEU A CB 1 ATOM 1128 C CG . LEU A 1 143 ? 7.020 43.903 30.472 1.00 46.17 ? 231 LEU A CG 1 ATOM 1129 C CD1 . LEU A 1 143 ? 7.351 43.216 29.127 1.00 48.33 ? 231 LEU A CD1 1 ATOM 1130 C CD2 . LEU A 1 143 ? 5.519 43.887 30.694 1.00 44.69 ? 231 LEU A CD2 1 ATOM 1131 N N . MET A 1 144 ? 9.939 45.597 30.255 1.00 53.24 ? 232 MET A N 1 ATOM 1132 C CA . MET A 1 144 ? 10.214 47.027 30.091 1.00 46.63 ? 232 MET A CA 1 ATOM 1133 C C . MET A 1 144 ? 9.475 47.595 28.907 1.00 48.69 ? 232 MET A C 1 ATOM 1134 O O . MET A 1 144 ? 9.225 46.881 27.936 1.00 45.69 ? 232 MET A O 1 ATOM 1135 C CB . MET A 1 144 ? 11.708 47.250 29.858 1.00 43.48 ? 232 MET A CB 1 ATOM 1136 C CG . MET A 1 144 ? 12.574 46.361 30.719 1.00 54.76 ? 232 MET A CG 1 ATOM 1137 S SD . MET A 1 144 ? 14.309 46.433 30.295 1.00 64.88 ? 232 MET A SD 1 ATOM 1138 C CE . MET A 1 144 ? 14.283 45.891 28.584 1.00 76.69 ? 232 MET A CE 1 ATOM 1139 N N . ASN A 1 145 ? 9.131 48.880 28.974 1.00 47.85 ? 233 ASN A N 1 ATOM 1140 C CA . ASN A 1 145 ? 8.527 49.520 27.819 1.00 51.71 ? 233 ASN A CA 1 ATOM 1141 C C . ASN A 1 145 ? 9.595 50.030 26.864 1.00 48.39 ? 233 ASN A C 1 ATOM 1142 O O . ASN A 1 145 ? 10.756 50.199 27.248 1.00 44.08 ? 233 ASN A O 1 ATOM 1143 C CB . ASN A 1 145 ? 7.550 50.620 28.215 1.00 44.58 ? 233 ASN A CB 1 ATOM 1144 C CG . ASN A 1 145 ? 8.202 51.740 28.991 1.00 51.89 ? 233 ASN A CG 1 ATOM 1145 O OD1 . ASN A 1 145 ? 9.095 52.420 28.499 1.00 52.36 ? 233 ASN A OD1 1 ATOM 1146 N ND2 . ASN A 1 145 ? 7.721 51.967 30.206 1.00 48.74 ? 233 ASN A ND2 1 ATOM 1147 N N . SER A 1 146 ? 9.205 50.271 25.619 1.00 45.90 ? 234 SER A N 1 ATOM 1148 C CA . SER A 1 146 ? 10.166 50.623 24.577 1.00 45.35 ? 234 SER A CA 1 ATOM 1149 C C . SER A 1 146 ? 10.753 52.012 24.783 1.00 46.51 ? 234 SER A C 1 ATOM 1150 O O . SER A 1 146 ? 11.822 52.334 24.245 1.00 51.18 ? 234 SER A O 1 ATOM 1151 C CB . SER A 1 146 ? 9.501 50.547 23.196 1.00 42.23 ? 234 SER A CB 1 ATOM 1152 O OG . SER A 1 146 ? 8.351 51.385 23.150 1.00 41.19 ? 234 SER A OG 1 ATOM 1153 N N . GLN A 1 147 ? 10.051 52.846 25.543 1.00 47.47 ? 235 GLN A N 1 ATOM 1154 C CA . GLN A 1 147 ? 10.511 54.208 25.768 1.00 55.36 ? 235 GLN A CA 1 ATOM 1155 C C . GLN A 1 147 ? 11.796 54.189 26.562 1.00 53.98 ? 235 GLN A C 1 ATOM 1156 O O . GLN A 1 147 ? 12.712 54.963 26.300 1.00 65.23 ? 235 GLN A O 1 ATOM 1157 C CB . GLN A 1 147 ? 9.461 55.006 26.537 1.00 65.58 ? 235 GLN A CB 1 ATOM 1158 C CG . GLN A 1 147 ? 9.920 56.389 26.996 1.00 68.12 ? 235 GLN A CG 1 ATOM 1159 C CD . GLN A 1 147 ? 8.880 57.064 27.863 1.00 79.23 ? 235 GLN A CD 1 ATOM 1160 O OE1 . GLN A 1 147 ? 8.725 56.723 29.037 1.00 89.80 ? 235 GLN A OE1 1 ATOM 1161 N NE2 . GLN A 1 147 ? 8.143 58.012 27.287 1.00 78.74 ? 235 GLN A NE2 1 ATOM 1162 N N . LEU A 1 148 ? 11.847 53.291 27.538 1.00 51.22 ? 236 LEU A N 1 ATOM 1163 C CA . LEU A 1 148 ? 13.001 53.154 28.407 1.00 52.01 ? 236 LEU A CA 1 ATOM 1164 C C . LEU A 1 148 ? 14.202 52.652 27.608 1.00 61.53 ? 236 LEU A C 1 ATOM 1165 O O . LEU A 1 148 ? 15.315 53.138 27.775 1.00 65.72 ? 236 LEU A O 1 ATOM 1166 C CB . LEU A 1 148 ? 12.664 52.198 29.550 1.00 53.93 ? 236 LEU A CB 1 ATOM 1167 C CG . LEU A 1 148 ? 13.723 51.893 30.612 1.00 63.37 ? 236 LEU A CG 1 ATOM 1168 C CD1 . LEU A 1 148 ? 13.034 51.552 31.898 1.00 64.30 ? 236 LEU A CD1 1 ATOM 1169 C CD2 . LEU A 1 148 ? 14.617 50.736 30.195 1.00 69.58 ? 236 LEU A CD2 1 ATOM 1170 N N . VAL A 1 149 ? 13.972 51.677 26.734 1.00 64.02 ? 237 VAL A N 1 ATOM 1171 C CA . VAL A 1 149 ? 15.048 51.125 25.919 1.00 61.68 ? 237 VAL A CA 1 ATOM 1172 C C . VAL A 1 149 ? 15.527 52.146 24.898 1.00 54.76 ? 237 VAL A C 1 ATOM 1173 O O . VAL A 1 149 ? 16.719 52.271 24.639 1.00 61.09 ? 237 VAL A O 1 ATOM 1174 C CB . VAL A 1 149 ? 14.604 49.835 25.224 1.00 61.39 ? 237 VAL A CB 1 ATOM 1175 C CG1 . VAL A 1 149 ? 15.673 49.345 24.223 1.00 53.03 ? 237 VAL A CG1 1 ATOM 1176 C CG2 . VAL A 1 149 ? 14.307 48.779 26.279 1.00 59.84 ? 237 VAL A CG2 1 ATOM 1177 N N . THR A 1 150 ? 14.599 52.909 24.348 1.00 48.31 ? 238 THR A N 1 ATOM 1178 C CA . THR A 1 150 ? 14.972 53.965 23.425 1.00 56.42 ? 238 THR A CA 1 ATOM 1179 C C . THR A 1 150 ? 15.670 55.160 24.084 1.00 60.78 ? 238 THR A C 1 ATOM 1180 O O . THR A 1 150 ? 16.702 55.618 23.609 1.00 67.13 ? 238 THR A O 1 ATOM 1181 C CB . THR A 1 150 ? 13.750 54.472 22.656 1.00 57.67 ? 238 THR A CB 1 ATOM 1182 O OG1 . THR A 1 150 ? 13.046 53.357 22.099 1.00 64.65 ? 238 THR A OG1 1 ATOM 1183 C CG2 . THR A 1 150 ? 14.174 55.431 21.551 1.00 58.67 ? 238 THR A CG2 1 ATOM 1184 N N . THR A 1 151 ? 15.113 55.676 25.173 1.00 68.20 ? 239 THR A N 1 ATOM 1185 C CA . THR A 1 151 ? 15.586 56.963 25.693 1.00 68.64 ? 239 THR A CA 1 ATOM 1186 C C . THR A 1 151 ? 16.347 56.945 27.029 1.00 70.48 ? 239 THR A C 1 ATOM 1187 O O . THR A 1 151 ? 17.112 57.865 27.300 1.00 72.64 ? 239 THR A O 1 ATOM 1188 C CB . THR A 1 151 ? 14.439 57.991 25.773 1.00 65.94 ? 239 THR A CB 1 ATOM 1189 O OG1 . THR A 1 151 ? 13.566 57.650 26.857 1.00 65.28 ? 239 THR A OG1 1 ATOM 1190 C CG2 . THR A 1 151 ? 13.643 58.005 24.459 1.00 61.65 ? 239 THR A CG2 1 ATOM 1191 N N . GLU A 1 152 ? 16.160 55.919 27.857 1.00 70.19 ? 240 GLU A N 1 ATOM 1192 C CA . GLU A 1 152 ? 16.898 55.850 29.123 1.00 67.16 ? 240 GLU A CA 1 ATOM 1193 C C . GLU A 1 152 ? 18.345 55.400 28.948 1.00 78.85 ? 240 GLU A C 1 ATOM 1194 O O . GLU A 1 152 ? 18.628 54.202 28.882 1.00 82.90 ? 240 GLU A O 1 ATOM 1195 C CB . GLU A 1 152 ? 16.190 54.954 30.149 1.00 71.80 ? 240 GLU A CB 1 ATOM 1196 C CG . GLU A 1 152 ? 16.767 55.044 31.561 1.00 77.03 ? 240 GLU A CG 1 ATOM 1197 C CD . GLU A 1 152 ? 17.116 56.469 31.945 1.00 82.32 ? 240 GLU A CD 1 ATOM 1198 O OE1 . GLU A 1 152 ? 18.327 56.806 31.998 1.00 83.96 ? 240 GLU A OE1 1 ATOM 1199 O OE2 . GLU A 1 152 ? 16.174 57.255 32.177 1.00 82.21 ? 240 GLU A OE2 1 ATOM 1200 N N . LYS A 1 153 ? 19.258 56.371 28.904 1.00 85.50 ? 241 LYS A N 1 ATOM 1201 C CA . LYS A 1 153 ? 20.678 56.107 28.672 1.00 87.81 ? 241 LYS A CA 1 ATOM 1202 C C . LYS A 1 153 ? 21.245 55.120 29.684 1.00 81.73 ? 241 LYS A C 1 ATOM 1203 O O . LYS A 1 153 ? 22.231 54.431 29.420 1.00 80.21 ? 241 LYS A O 1 ATOM 1204 C CB . LYS A 1 153 ? 21.477 57.415 28.707 1.00 100.62 ? 241 LYS A CB 1 ATOM 1205 C CG . LYS A 1 153 ? 20.864 58.531 27.868 1.00 106.58 ? 241 LYS A CG 1 ATOM 1206 C CD . LYS A 1 153 ? 21.422 59.893 28.255 1.00 116.45 ? 241 LYS A CD 1 ATOM 1207 C CE . LYS A 1 153 ? 20.443 61.010 27.913 1.00 116.99 ? 241 LYS A CE 1 ATOM 1208 N NZ . LYS A 1 153 ? 20.845 62.304 28.536 1.00 123.54 ? 241 LYS A NZ 1 ATOM 1209 N N . ARG A 1 154 ? 20.614 55.055 30.846 1.00 85.48 ? 242 ARG A N 1 ATOM 1210 C CA . ARG A 1 154 ? 21.037 54.117 31.870 1.00 92.21 ? 242 ARG A CA 1 ATOM 1211 C C . ARG A 1 154 ? 20.782 52.667 31.459 1.00 84.08 ? 242 ARG A C 1 ATOM 1212 O O . ARG A 1 154 ? 21.380 51.751 32.022 1.00 86.75 ? 242 ARG A O 1 ATOM 1213 C CB . ARG A 1 154 ? 20.351 54.421 33.203 1.00 95.18 ? 242 ARG A CB 1 ATOM 1214 C CG . ARG A 1 154 ? 20.959 55.588 33.958 1.00 103.56 ? 242 ARG A CG 1 ATOM 1215 C CD . ARG A 1 154 ? 20.431 55.636 35.378 1.00 105.90 ? 242 ARG A CD 1 ATOM 1216 N NE . ARG A 1 154 ? 18.975 55.747 35.415 1.00 105.38 ? 242 ARG A NE 1 ATOM 1217 C CZ . ARG A 1 154 ? 18.264 55.840 36.533 1.00 110.16 ? 242 ARG A CZ 1 ATOM 1218 N NH1 . ARG A 1 154 ? 16.943 55.939 36.473 1.00 107.63 ? 242 ARG A NH1 1 ATOM 1219 N NH2 . ARG A 1 154 ? 18.875 55.833 37.714 1.00 115.28 ? 242 ARG A NH2 1 ATOM 1220 N N . PHE A 1 155 ? 19.903 52.450 30.485 1.00 81.57 ? 243 PHE A N 1 ATOM 1221 C CA . PHE A 1 155 ? 19.579 51.074 30.102 1.00 81.28 ? 243 PHE A CA 1 ATOM 1222 C C . PHE A 1 155 ? 20.767 50.289 29.555 1.00 81.44 ? 243 PHE A C 1 ATOM 1223 O O . PHE A 1 155 ? 20.926 49.096 29.827 1.00 85.65 ? 243 PHE A O 1 ATOM 1224 C CB . PHE A 1 155 ? 18.448 50.989 29.092 1.00 74.42 ? 243 PHE A CB 1 ATOM 1225 C CG . PHE A 1 155 ? 18.228 49.596 28.596 1.00 76.24 ? 243 PHE A CG 1 ATOM 1226 C CD1 . PHE A 1 155 ? 17.845 48.593 29.471 1.00 75.20 ? 243 PHE A CD1 1 ATOM 1227 C CD2 . PHE A 1 155 ? 18.445 49.267 27.267 1.00 76.42 ? 243 PHE A CD2 1 ATOM 1228 C CE1 . PHE A 1 155 ? 17.665 47.291 29.024 1.00 71.74 ? 243 PHE A CE1 1 ATOM 1229 C CE2 . PHE A 1 155 ? 18.258 47.965 26.816 1.00 67.51 ? 243 PHE A CE2 1 ATOM 1230 C CZ . PHE A 1 155 ? 17.870 46.982 27.694 1.00 66.70 ? 243 PHE A CZ 1 ATOM 1231 N N . LEU A 1 156 ? 21.600 50.957 28.773 1.00 81.37 ? 244 LEU A N 1 ATOM 1232 C CA . LEU A 1 156 ? 22.788 50.310 28.247 1.00 83.44 ? 244 LEU A CA 1 ATOM 1233 C C . LEU A 1 156 ? 23.935 50.233 29.268 1.00 91.96 ? 244 LEU A C 1 ATOM 1234 O O . LEU A 1 156 ? 24.964 49.603 28.996 1.00 92.02 ? 244 LEU A O 1 ATOM 1235 C CB . LEU A 1 156 ? 23.245 51.015 26.968 1.00 90.65 ? 244 LEU A CB 1 ATOM 1236 C CG . LEU A 1 156 ? 22.198 51.093 25.850 1.00 86.75 ? 244 LEU A CG 1 ATOM 1237 C CD1 . LEU A 1 156 ? 22.813 51.646 24.575 1.00 93.13 ? 244 LEU A CD1 1 ATOM 1238 C CD2 . LEU A 1 156 ? 21.575 49.731 25.594 1.00 79.88 ? 244 LEU A CD2 1 ATOM 1239 N N . LYS A 1 157 ? 23.754 50.845 30.444 1.00 99.45 ? 245 LYS A N 1 ATOM 1240 C CA . LYS A 1 157 ? 24.850 50.981 31.425 1.00 107.24 ? 245 LYS A CA 1 ATOM 1241 C C . LYS A 1 157 ? 24.663 50.247 32.760 1.00 102.90 ? 245 LYS A C 1 ATOM 1242 O O . LYS A 1 157 ? 25.576 49.568 33.239 1.00 105.06 ? 245 LYS A O 1 ATOM 1243 C CB . LYS A 1 157 ? 25.114 52.461 31.742 1.00 114.96 ? 245 LYS A CB 1 ATOM 1244 C CG . LYS A 1 157 ? 25.576 53.324 30.577 1.00 121.98 ? 245 LYS A CG 1 ATOM 1245 C CD . LYS A 1 157 ? 25.620 54.794 31.002 1.00 129.35 ? 245 LYS A CD 1 ATOM 1246 C CE . LYS A 1 157 ? 25.900 55.724 29.826 1.00 135.12 ? 245 LYS A CE 1 ATOM 1247 N NZ . LYS A 1 157 ? 25.764 57.165 30.202 1.00 137.18 ? 245 LYS A NZ 1 ATOM 1248 N N . ASP A 1 158 ? 23.501 50.416 33.382 1.00 99.32 ? 246 ASP A N 1 ATOM 1249 C CA . ASP A 1 158 ? 23.307 49.948 34.757 1.00 104.76 ? 246 ASP A CA 1 ATOM 1250 C C . ASP A 1 158 ? 23.291 48.428 34.871 1.00 103.49 ? 246 ASP A C 1 ATOM 1251 O O . ASP A 1 158 ? 22.568 47.744 34.152 1.00 101.10 ? 246 ASP A O 1 ATOM 1252 C CB . ASP A 1 158 ? 22.053 50.567 35.389 1.00 103.15 ? 246 ASP A CB 1 ATOM 1253 C CG . ASP A 1 158 ? 22.310 51.960 35.944 1.00 114.00 ? 246 ASP A CG 1 ATOM 1254 O OD1 . ASP A 1 158 ? 23.454 52.456 35.797 1.00 120.67 ? 246 ASP A OD1 1 ATOM 1255 O OD2 . ASP A 1 158 ? 21.374 52.559 36.523 1.00 114.22 ? 246 ASP A OD2 1 ATOM 1256 N N . SER A 1 159 ? 24.096 47.914 35.793 1.00 106.59 ? 247 SER A N 1 ATOM 1257 C CA . SER A 1 159 ? 24.272 46.479 35.967 1.00 106.31 ? 247 SER A CA 1 ATOM 1258 C C . SER A 1 159 ? 22.987 45.737 36.340 1.00 102.20 ? 247 SER A C 1 ATOM 1259 O O . SER A 1 159 ? 22.940 44.512 36.278 1.00 104.32 ? 247 SER A O 1 ATOM 1260 C CB . SER A 1 159 ? 25.344 46.206 37.029 1.00 111.75 ? 247 SER A CB 1 ATOM 1261 O OG . SER A 1 159 ? 24.931 46.685 38.299 1.00 107.81 ? 247 SER A OG 1 ATOM 1262 N N . LEU A 1 160 ? 21.949 46.465 36.729 1.00 100.74 ? 248 LEU A N 1 ATOM 1263 C CA . LEU A 1 160 ? 20.720 45.819 37.177 1.00 102.36 ? 248 LEU A CA 1 ATOM 1264 C C . LEU A 1 160 ? 19.953 45.100 36.065 1.00 97.31 ? 248 LEU A C 1 ATOM 1265 O O . LEU A 1 160 ? 19.415 44.009 36.266 1.00 103.72 ? 248 LEU A O 1 ATOM 1266 C CB . LEU A 1 160 ? 19.796 46.826 37.833 1.00 105.79 ? 248 LEU A CB 1 ATOM 1267 C CG . LEU A 1 160 ? 18.478 46.148 38.192 1.00 108.87 ? 248 LEU A CG 1 ATOM 1268 C CD1 . LEU A 1 160 ? 18.704 45.014 39.207 1.00 115.52 ? 248 LEU A CD1 1 ATOM 1269 C CD2 . LEU A 1 160 ? 17.483 47.165 38.683 1.00 105.65 ? 248 LEU A CD2 1 ATOM 1270 N N . TYR A 1 161 ? 19.888 45.718 34.897 1.00 83.83 ? 249 TYR A N 1 ATOM 1271 C CA . TYR A 1 161 ? 19.169 45.118 33.787 1.00 80.15 ? 249 TYR A CA 1 ATOM 1272 C C . TYR A 1 161 ? 19.790 43.775 33.373 1.00 83.63 ? 249 TYR A C 1 ATOM 1273 O O . TYR A 1 161 ? 19.141 42.934 32.752 1.00 82.19 ? 249 TYR A O 1 ATOM 1274 C CB . TYR A 1 161 ? 19.147 46.094 32.620 1.00 68.78 ? 249 TYR A CB 1 ATOM 1275 C CG . TYR A 1 161 ? 18.393 47.377 32.912 1.00 69.19 ? 249 TYR A CG 1 ATOM 1276 C CD1 . TYR A 1 161 ? 17.012 47.450 32.732 1.00 60.95 ? 249 TYR A CD1 1 ATOM 1277 C CD2 . TYR A 1 161 ? 19.056 48.514 33.360 1.00 72.86 ? 249 TYR A CD2 1 ATOM 1278 C CE1 . TYR A 1 161 ? 16.307 48.617 32.987 1.00 57.82 ? 249 TYR A CE1 1 ATOM 1279 C CE2 . TYR A 1 161 ? 18.360 49.690 33.617 1.00 69.56 ? 249 TYR A CE2 1 ATOM 1280 C CZ . TYR A 1 161 ? 16.986 49.732 33.427 1.00 65.17 ? 249 TYR A CZ 1 ATOM 1281 O OH . TYR A 1 161 ? 16.286 50.890 33.676 1.00 75.30 ? 249 TYR A OH 1 ATOM 1282 N N . ASN A 1 162 ? 21.048 43.570 33.742 1.00 85.46 ? 250 ASN A N 1 ATOM 1283 C CA . ASN A 1 162 ? 21.794 42.386 33.327 1.00 90.71 ? 250 ASN A CA 1 ATOM 1284 C C . ASN A 1 162 ? 21.425 41.111 34.074 1.00 93.52 ? 250 ASN A C 1 ATOM 1285 O O . ASN A 1 162 ? 22.080 40.080 33.915 1.00 95.04 ? 250 ASN A O 1 ATOM 1286 C CB . ASN A 1 162 ? 23.297 42.641 33.455 1.00 96.42 ? 250 ASN A CB 1 ATOM 1287 C CG . ASN A 1 162 ? 23.688 44.005 32.935 1.00 100.36 ? 250 ASN A CG 1 ATOM 1288 O OD1 . ASN A 1 162 ? 22.887 44.673 32.267 1.00 90.84 ? 250 ASN A OD1 1 ATOM 1289 N ND2 . ASN A 1 162 ? 24.911 44.438 33.240 1.00 109.43 ? 250 ASN A ND2 1 ATOM 1290 N N . GLU A 1 163 ? 20.371 41.184 34.876 1.00 92.72 ? 251 GLU A N 1 ATOM 1291 C CA . GLU A 1 163 ? 19.887 40.020 35.601 1.00 97.91 ? 251 GLU A CA 1 ATOM 1292 C C . GLU A 1 163 ? 18.622 39.454 34.973 1.00 90.03 ? 251 GLU A C 1 ATOM 1293 O O . GLU A 1 163 ? 17.682 40.194 34.687 1.00 86.84 ? 251 GLU A O 1 ATOM 1294 C CB . GLU A 1 163 ? 19.600 40.386 37.056 1.00 106.15 ? 251 GLU A CB 1 ATOM 1295 C CG . GLU A 1 163 ? 20.834 40.734 37.855 1.00 117.12 ? 251 GLU A CG 1 ATOM 1296 C CD . GLU A 1 163 ? 20.585 40.656 39.340 1.00 124.09 ? 251 GLU A CD 1 ATOM 1297 O OE1 . GLU A 1 163 ? 19.411 40.463 39.729 1.00 120.79 ? 251 GLU A OE1 1 ATOM 1298 O OE2 . GLU A 1 163 ? 21.560 40.783 40.114 1.00 132.20 ? 251 GLU A OE2 1 ATOM 1299 N N . GLY A 1 164 ? 18.603 38.141 34.773 1.00 89.36 ? 252 GLY A N 1 ATOM 1300 C CA . GLY A 1 164 ? 17.403 37.454 34.328 1.00 92.41 ? 252 GLY A CA 1 ATOM 1301 C C . GLY A 1 164 ? 17.017 37.623 32.863 1.00 90.18 ? 252 GLY A C 1 ATOM 1302 O O . GLY A 1 164 ? 17.839 37.998 32.016 1.00 83.48 ? 252 GLY A O 1 ATOM 1303 N N . ILE A 1 165 ? 15.751 37.335 32.566 1.00 83.72 ? 253 ILE A N 1 ATOM 1304 C CA . ILE A 1 165 ? 15.223 37.443 31.210 1.00 75.71 ? 253 ILE A CA 1 ATOM 1305 C C . ILE A 1 165 ? 14.582 38.803 31.012 1.00 70.56 ? 253 ILE A C 1 ATOM 1306 O O . ILE A 1 165 ? 13.801 39.263 31.846 1.00 65.46 ? 253 ILE A O 1 ATOM 1307 C CB . ILE A 1 165 ? 14.171 36.361 30.946 1.00 75.71 ? 253 ILE A CB 1 ATOM 1308 C CG1 . ILE A 1 165 ? 14.815 34.978 31.009 1.00 83.31 ? 253 ILE A CG1 1 ATOM 1309 C CG2 . ILE A 1 165 ? 13.510 36.580 29.603 1.00 65.05 ? 253 ILE A CG2 1 ATOM 1310 C CD1 . ILE A 1 165 ? 13.848 33.876 31.351 1.00 80.92 ? 253 ILE A CD1 1 ATOM 1311 N N . LEU A 1 166 ? 14.926 39.464 29.919 1.00 63.64 ? 254 LEU A N 1 ATOM 1312 C CA . LEU A 1 166 ? 14.323 40.754 29.630 1.00 57.28 ? 254 LEU A CA 1 ATOM 1313 C C . LEU A 1 166 ? 13.288 40.616 28.544 1.00 64.83 ? 254 LEU A C 1 ATOM 1314 O O . LEU A 1 166 ? 13.373 39.723 27.697 1.00 69.08 ? 254 LEU A O 1 ATOM 1315 C CB . LEU A 1 166 ? 15.380 41.760 29.195 1.00 66.93 ? 254 LEU A CB 1 ATOM 1316 C CG . LEU A 1 166 ? 16.577 41.889 30.132 1.00 71.62 ? 254 LEU A CG 1 ATOM 1317 C CD1 . LEU A 1 166 ? 17.646 42.778 29.508 1.00 69.84 ? 254 LEU A CD1 1 ATOM 1318 C CD2 . LEU A 1 166 ? 16.137 42.416 31.508 1.00 64.83 ? 254 LEU A CD2 1 ATOM 1319 N N . ILE A 1 167 ? 12.317 41.519 28.566 1.00 59.55 ? 255 ILE A N 1 ATOM 1320 C CA . ILE A 1 167 ? 11.318 41.632 27.518 1.00 51.05 ? 255 ILE A CA 1 ATOM 1321 C C . ILE A 1 167 ? 11.073 43.115 27.321 1.00 48.21 ? 255 ILE A C 1 ATOM 1322 O O . ILE A 1 167 ? 10.958 43.839 28.287 1.00 52.25 ? 255 ILE A O 1 ATOM 1323 C CB . ILE A 1 167 ? 9.980 40.991 27.937 1.00 54.23 ? 255 ILE A CB 1 ATOM 1324 C CG1 . ILE A 1 167 ? 10.160 39.517 28.277 1.00 56.96 ? 255 ILE A CG1 1 ATOM 1325 C CG2 . ILE A 1 167 ? 8.953 41.139 26.829 1.00 51.63 ? 255 ILE A CG2 1 ATOM 1326 C CD1 . ILE A 1 167 ? 9.115 38.998 29.247 1.00 60.83 ? 255 ILE A CD1 1 ATOM 1327 N N . VAL A 1 168 ? 11.048 43.568 26.074 1.00 47.28 ? 256 VAL A N 1 ATOM 1328 C CA . VAL A 1 168 ? 10.636 44.925 25.744 1.00 43.80 ? 256 VAL A CA 1 ATOM 1329 C C . VAL A 1 168 ? 9.312 44.875 24.973 1.00 48.12 ? 256 VAL A C 1 ATOM 1330 O O . VAL A 1 168 ? 9.061 43.937 24.224 1.00 54.31 ? 256 VAL A O 1 ATOM 1331 C CB . VAL A 1 168 ? 11.707 45.653 24.900 1.00 42.80 ? 256 VAL A CB 1 ATOM 1332 C CG1 . VAL A 1 168 ? 11.954 44.905 23.605 1.00 42.66 ? 256 VAL A CG1 1 ATOM 1333 C CG2 . VAL A 1 168 ? 11.285 47.092 24.624 1.00 43.19 ? 256 VAL A CG2 1 ATOM 1334 N N . TRP A 1 169 ? 8.449 45.865 25.181 1.00 44.80 ? 257 TRP A N 1 ATOM 1335 C CA . TRP A 1 169 ? 7.216 45.965 24.411 1.00 40.50 ? 257 TRP A CA 1 ATOM 1336 C C . TRP A 1 169 ? 6.990 47.404 24.029 1.00 37.47 ? 257 TRP A C 1 ATOM 1337 O O . TRP A 1 169 ? 7.496 48.326 24.658 1.00 48.01 ? 257 TRP A O 1 ATOM 1338 C CB . TRP A 1 169 ? 6.002 45.427 25.186 1.00 48.90 ? 257 TRP A CB 1 ATOM 1339 C CG . TRP A 1 169 ? 5.548 46.326 26.285 1.00 49.52 ? 257 TRP A CG 1 ATOM 1340 C CD1 . TRP A 1 169 ? 6.090 46.429 27.543 1.00 45.97 ? 257 TRP A CD1 1 ATOM 1341 C CD2 . TRP A 1 169 ? 4.463 47.259 26.240 1.00 45.73 ? 257 TRP A CD2 1 ATOM 1342 N NE1 . TRP A 1 169 ? 5.416 47.366 28.266 1.00 46.04 ? 257 TRP A NE1 1 ATOM 1343 C CE2 . TRP A 1 169 ? 4.412 47.894 27.502 1.00 48.57 ? 257 TRP A CE2 1 ATOM 1344 C CE3 . TRP A 1 169 ? 3.530 47.620 25.257 1.00 42.95 ? 257 TRP A CE3 1 ATOM 1345 C CZ2 . TRP A 1 169 ? 3.460 48.858 27.820 1.00 48.94 ? 257 TRP A CZ2 1 ATOM 1346 C CZ3 . TRP A 1 169 ? 2.585 48.582 25.569 1.00 42.68 ? 257 TRP A CZ3 1 ATOM 1347 C CH2 . TRP A 1 169 ? 2.561 49.198 26.837 1.00 51.21 ? 257 TRP A CH2 1 ATOM 1348 N N . ASP A 1 170 ? 6.186 47.571 22.993 1.00 35.78 ? 258 ASP A N 1 ATOM 1349 C CA . ASP A 1 170 ? 6.019 48.835 22.306 1.00 46.09 ? 258 ASP A CA 1 ATOM 1350 C C . ASP A 1 170 ? 4.568 48.891 21.870 1.00 40.87 ? 258 ASP A C 1 ATOM 1351 O O . ASP A 1 170 ? 4.042 47.906 21.380 1.00 39.32 ? 258 ASP A O 1 ATOM 1352 C CB . ASP A 1 170 ? 6.932 48.856 21.082 1.00 43.52 ? 258 ASP A CB 1 ATOM 1353 C CG . ASP A 1 170 ? 6.826 50.134 20.288 1.00 42.29 ? 258 ASP A CG 1 ATOM 1354 O OD1 . ASP A 1 170 ? 7.300 51.183 20.785 1.00 44.63 ? 258 ASP A OD1 1 ATOM 1355 O OD2 . ASP A 1 170 ? 6.301 50.077 19.143 1.00 51.83 ? 258 ASP A OD2 1 ATOM 1356 N N . PRO A 1 171 ? 3.895 50.014 22.127 1.00 38.71 ? 259 PRO A N 1 ATOM 1357 C CA . PRO A 1 171 ? 2.513 50.237 21.717 1.00 37.63 ? 259 PRO A CA 1 ATOM 1358 C C . PRO A 1 171 ? 2.476 50.440 20.187 1.00 40.01 ? 259 PRO A C 1 ATOM 1359 O O . PRO A 1 171 ? 3.187 51.294 19.687 1.00 44.39 ? 259 PRO A O 1 ATOM 1360 C CB . PRO A 1 171 ? 2.171 51.558 22.407 1.00 32.54 ? 259 PRO A CB 1 ATOM 1361 C CG . PRO A 1 171 ? 3.227 51.759 23.451 1.00 45.29 ? 259 PRO A CG 1 ATOM 1362 C CD . PRO A 1 171 ? 4.435 51.148 22.891 1.00 47.06 ? 259 PRO A CD 1 ATOM 1363 N N . SER A 1 172 ? 1.672 49.668 19.468 1.00 42.01 ? 260 SER A N 1 ATOM 1364 C CA . SER A 1 172 ? 1.512 49.838 18.025 1.00 47.44 ? 260 SER A CA 1 ATOM 1365 C C . SER A 1 172 ? 0.184 50.524 17.706 1.00 43.51 ? 260 SER A C 1 ATOM 1366 O O . SER A 1 172 ? -0.668 50.678 18.581 1.00 46.46 ? 260 SER A O 1 ATOM 1367 C CB . SER A 1 172 ? 1.505 48.465 17.361 1.00 54.78 ? 260 SER A CB 1 ATOM 1368 O OG . SER A 1 172 ? 0.390 47.701 17.812 1.00 55.32 ? 260 SER A OG 1 ATOM 1369 N N . VAL A 1 173 ? -0.001 50.926 16.458 1.00 44.86 ? 261 VAL A N 1 ATOM 1370 C CA . VAL A 1 173 ? -1.331 51.284 15.973 1.00 41.76 ? 261 VAL A CA 1 ATOM 1371 C C . VAL A 1 173 ? -2.295 50.114 16.238 1.00 45.67 ? 261 VAL A C 1 ATOM 1372 O O . VAL A 1 173 ? -1.922 48.953 16.125 1.00 50.55 ? 261 VAL A O 1 ATOM 1373 C CB . VAL A 1 173 ? -1.309 51.635 14.476 1.00 46.41 ? 261 VAL A CB 1 ATOM 1374 C CG1 . VAL A 1 173 ? -2.655 52.165 14.022 1.00 49.94 ? 261 VAL A CG1 1 ATOM 1375 C CG2 . VAL A 1 173 ? -0.239 52.684 14.189 1.00 44.91 ? 261 VAL A CG2 1 ATOM 1376 N N . TYR A 1 174 ? -3.526 50.427 16.617 1.00 47.92 ? 262 TYR A N 1 ATOM 1377 C CA . TYR A 1 174 ? -4.496 49.413 16.989 1.00 45.26 ? 262 TYR A CA 1 ATOM 1378 C C . TYR A 1 174 ? -4.672 48.413 15.858 1.00 50.98 ? 262 TYR A C 1 ATOM 1379 O O . TYR A 1 174 ? -4.760 48.820 14.714 1.00 45.51 ? 262 TYR A O 1 ATOM 1380 C CB . TYR A 1 174 ? -5.822 50.095 17.270 1.00 48.64 ? 262 TYR A CB 1 ATOM 1381 C CG . TYR A 1 174 ? -6.919 49.189 17.761 1.00 46.82 ? 262 TYR A CG 1 ATOM 1382 C CD1 . TYR A 1 174 ? -6.808 48.541 18.970 1.00 52.98 ? 262 TYR A CD1 1 ATOM 1383 C CD2 . TYR A 1 174 ? -8.071 48.994 17.018 1.00 51.95 ? 262 TYR A CD2 1 ATOM 1384 C CE1 . TYR A 1 174 ? -7.827 47.718 19.448 1.00 55.55 ? 262 TYR A CE1 1 ATOM 1385 C CE2 . TYR A 1 174 ? -9.091 48.170 17.476 1.00 57.04 ? 262 TYR A CE2 1 ATOM 1386 C CZ . TYR A 1 174 ? -8.965 47.534 18.696 1.00 57.04 ? 262 TYR A CZ 1 ATOM 1387 O OH . TYR A 1 174 ? -9.977 46.716 19.189 1.00 60.81 ? 262 TYR A OH 1 ATOM 1388 N N . HIS A 1 175 ? -4.731 47.116 16.180 1.00 53.42 ? 263 HIS A N 1 ATOM 1389 C CA . HIS A 1 175 ? -4.862 46.035 15.167 1.00 57.62 ? 263 HIS A CA 1 ATOM 1390 C C . HIS A 1 175 ? -3.803 46.019 14.050 1.00 59.48 ? 263 HIS A C 1 ATOM 1391 O O . HIS A 1 175 ? -4.058 45.531 12.953 1.00 61.39 ? 263 HIS A O 1 ATOM 1392 C CB . HIS A 1 175 ? -6.273 45.962 14.572 1.00 62.59 ? 263 HIS A CB 1 ATOM 1393 C CG . HIS A 1 175 ? -7.297 45.428 15.528 1.00 71.19 ? 263 HIS A CG 1 ATOM 1394 N ND1 . HIS A 1 175 ? -8.546 45.000 15.125 1.00 74.38 ? 263 HIS A ND1 1 ATOM 1395 C CD2 . HIS A 1 175 ? -7.255 45.261 16.875 1.00 64.47 ? 263 HIS A CD2 1 ATOM 1396 C CE1 . HIS A 1 175 ? -9.228 44.591 16.184 1.00 79.31 ? 263 HIS A CE1 1 ATOM 1397 N NE2 . HIS A 1 175 ? -8.468 44.740 17.257 1.00 68.37 ? 263 HIS A NE2 1 ATOM 1398 N N . SER A 1 176 ? -2.612 46.531 14.336 1.00 52.70 ? 264 SER A N 1 ATOM 1399 C CA . SER A 1 176 ? -1.544 46.568 13.339 1.00 52.18 ? 264 SER A CA 1 ATOM 1400 C C . SER A 1 176 ? -0.747 45.265 13.407 1.00 54.95 ? 264 SER A C 1 ATOM 1401 O O . SER A 1 176 ? -0.461 44.774 14.488 1.00 56.98 ? 264 SER A O 1 ATOM 1402 C CB . SER A 1 176 ? -0.624 47.748 13.651 1.00 51.27 ? 264 SER A CB 1 ATOM 1403 O OG . SER A 1 176 ? 0.490 47.797 12.785 1.00 65.83 ? 264 SER A OG 1 ATOM 1404 N N . ASP A 1 177 ? -0.370 44.715 12.256 1.00 60.87 ? 265 ASP A N 1 ATOM 1405 C CA . ASP A 1 177 ? 0.452 43.507 12.230 1.00 51.72 ? 265 ASP A CA 1 ATOM 1406 C C . ASP A 1 177 ? 1.926 43.876 12.311 1.00 50.23 ? 265 ASP A C 1 ATOM 1407 O O . ASP A 1 177 ? 2.284 45.065 12.342 1.00 45.15 ? 265 ASP A O 1 ATOM 1408 C CB . ASP A 1 177 ? 0.153 42.643 11.000 1.00 57.22 ? 265 ASP A CB 1 ATOM 1409 C CG . ASP A 1 177 ? 0.518 43.335 9.699 1.00 76.71 ? 265 ASP A CG 1 ATOM 1410 O OD1 . ASP A 1 177 ? 0.452 44.579 9.653 1.00 83.08 ? 265 ASP A OD1 1 ATOM 1411 O OD2 . ASP A 1 177 ? 0.868 42.639 8.720 1.00 87.46 ? 265 ASP A OD2 1 ATOM 1412 N N . ILE A 1 178 ? 2.785 42.865 12.365 1.00 51.51 ? 266 ILE A N 1 ATOM 1413 C CA . ILE A 1 178 ? 4.185 43.121 12.679 1.00 46.75 ? 266 ILE A CA 1 ATOM 1414 C C . ILE A 1 178 ? 4.874 44.068 11.656 1.00 52.46 ? 266 ILE A C 1 ATOM 1415 O O . ILE A 1 178 ? 5.512 45.056 12.044 1.00 51.43 ? 266 ILE A O 1 ATOM 1416 C CB . ILE A 1 178 ? 4.947 41.793 12.930 1.00 50.53 ? 266 ILE A CB 1 ATOM 1417 C CG1 . ILE A 1 178 ? 4.565 41.268 14.325 1.00 43.98 ? 266 ILE A CG1 1 ATOM 1418 C CG2 . ILE A 1 178 ? 6.464 42.006 12.843 1.00 49.44 ? 266 ILE A CG2 1 ATOM 1419 C CD1 . ILE A 1 178 ? 4.889 39.791 14.601 1.00 42.99 ? 266 ILE A CD1 1 ATOM 1420 N N . PRO A 1 179 ? 4.698 43.816 10.355 1.00 51.50 ? 267 PRO A N 1 ATOM 1421 C CA . PRO A 1 179 ? 5.427 44.698 9.427 1.00 59.16 ? 267 PRO A CA 1 ATOM 1422 C C . PRO A 1 179 ? 4.986 46.159 9.487 1.00 45.02 ? 267 PRO A C 1 ATOM 1423 O O . PRO A 1 179 ? 5.826 47.055 9.385 1.00 48.38 ? 267 PRO A O 1 ATOM 1424 C CB . PRO A 1 179 ? 5.073 44.128 8.063 1.00 48.07 ? 267 PRO A CB 1 ATOM 1425 C CG . PRO A 1 179 ? 4.698 42.743 8.319 1.00 54.99 ? 267 PRO A CG 1 ATOM 1426 C CD . PRO A 1 179 ? 4.040 42.709 9.634 1.00 52.08 ? 267 PRO A CD 1 ATOM 1427 N N . LYS A 1 180 ? 3.689 46.398 9.641 1.00 49.87 ? 268 LYS A N 1 ATOM 1428 C CA . LYS A 1 180 ? 3.211 47.766 9.728 1.00 58.72 ? 268 LYS A CA 1 ATOM 1429 C C . LYS A 1 180 ? 3.771 48.364 11.002 1.00 57.64 ? 268 LYS A C 1 ATOM 1430 O O . LYS A 1 180 ? 4.201 49.514 11.006 1.00 60.91 ? 268 LYS A O 1 ATOM 1431 C CB . LYS A 1 180 ? 1.679 47.846 9.748 1.00 64.01 ? 268 LYS A CB 1 ATOM 1432 C CG . LYS A 1 180 ? 0.988 47.366 8.468 1.00 82.18 ? 268 LYS A CG 1 ATOM 1433 C CD . LYS A 1 180 ? 1.569 47.994 7.210 1.00 96.50 ? 268 LYS A CD 1 ATOM 1434 C CE . LYS A 1 180 ? 1.276 49.485 7.107 1.00 106.64 ? 268 LYS A CE 1 ATOM 1435 N NZ . LYS A 1 180 ? 1.830 50.061 5.842 1.00 115.72 ? 268 LYS A NZ 1 ATOM 1436 N N . TRP A 1 181 ? 3.779 47.579 12.077 1.00 52.26 ? 269 TRP A N 1 ATOM 1437 C CA . TRP A 1 181 ? 4.261 48.086 13.363 1.00 42.23 ? 269 TRP A CA 1 ATOM 1438 C C . TRP A 1 181 ? 5.736 48.420 13.283 1.00 48.40 ? 269 TRP A C 1 ATOM 1439 O O . TRP A 1 181 ? 6.166 49.472 13.760 1.00 50.06 ? 269 TRP A O 1 ATOM 1440 C CB . TRP A 1 181 ? 3.985 47.070 14.470 1.00 47.55 ? 269 TRP A CB 1 ATOM 1441 C CG . TRP A 1 181 ? 4.853 47.195 15.666 1.00 46.15 ? 269 TRP A CG 1 ATOM 1442 C CD1 . TRP A 1 181 ? 4.808 48.168 16.619 1.00 42.10 ? 269 TRP A CD1 1 ATOM 1443 C CD2 . TRP A 1 181 ? 5.873 46.279 16.070 1.00 48.46 ? 269 TRP A CD2 1 ATOM 1444 N NE1 . TRP A 1 181 ? 5.752 47.916 17.608 1.00 43.03 ? 269 TRP A NE1 1 ATOM 1445 C CE2 . TRP A 1 181 ? 6.416 46.760 17.282 1.00 49.21 ? 269 TRP A CE2 1 ATOM 1446 C CE3 . TRP A 1 181 ? 6.373 45.093 15.530 1.00 47.84 ? 269 TRP A CE3 1 ATOM 1447 C CZ2 . TRP A 1 181 ? 7.443 46.099 17.952 1.00 51.53 ? 269 TRP A CZ2 1 ATOM 1448 C CZ3 . TRP A 1 181 ? 7.394 44.441 16.187 1.00 51.16 ? 269 TRP A CZ3 1 ATOM 1449 C CH2 . TRP A 1 181 ? 7.916 44.941 17.394 1.00 46.88 ? 269 TRP A CH2 1 ATOM 1450 N N . TYR A 1 182 ? 6.499 47.546 12.632 1.00 50.86 ? 270 TYR A N 1 ATOM 1451 C CA . TYR A 1 182 ? 7.943 47.710 12.524 1.00 47.44 ? 270 TYR A CA 1 ATOM 1452 C C . TYR A 1 182 ? 8.277 49.029 11.834 1.00 56.61 ? 270 TYR A C 1 ATOM 1453 O O . TYR A 1 182 ? 9.221 49.717 12.211 1.00 64.37 ? 270 TYR A O 1 ATOM 1454 C CB . TYR A 1 182 ? 8.544 46.514 11.774 1.00 45.09 ? 270 TYR A CB 1 ATOM 1455 C CG . TYR A 1 182 ? 10.050 46.570 11.594 1.00 51.66 ? 270 TYR A CG 1 ATOM 1456 C CD1 . TYR A 1 182 ? 10.897 45.991 12.528 1.00 52.34 ? 270 TYR A CD1 1 ATOM 1457 C CD2 . TYR A 1 182 ? 10.628 47.204 10.493 1.00 56.76 ? 270 TYR A CD2 1 ATOM 1458 C CE1 . TYR A 1 182 ? 12.274 46.031 12.376 1.00 56.30 ? 270 TYR A CE1 1 ATOM 1459 C CE2 . TYR A 1 182 ? 12.014 47.251 10.333 1.00 55.11 ? 270 TYR A CE2 1 ATOM 1460 C CZ . TYR A 1 182 ? 12.828 46.663 11.297 1.00 58.51 ? 270 TYR A CZ 1 ATOM 1461 O OH . TYR A 1 182 ? 14.203 46.687 11.194 1.00 57.21 ? 270 TYR A OH 1 ATOM 1462 N N . GLN A 1 183 ? 7.484 49.386 10.830 1.00 56.44 ? 271 GLN A N 1 ATOM 1463 C CA . GLN A 1 183 ? 7.680 50.635 10.105 1.00 60.78 ? 271 GLN A CA 1 ATOM 1464 C C . GLN A 1 183 ? 7.318 51.859 10.949 1.00 63.68 ? 271 GLN A C 1 ATOM 1465 O O . GLN A 1 183 ? 7.870 52.937 10.756 1.00 70.86 ? 271 GLN A O 1 ATOM 1466 C CB . GLN A 1 183 ? 6.847 50.610 8.824 1.00 72.80 ? 271 GLN A CB 1 ATOM 1467 C CG . GLN A 1 183 ? 7.062 51.782 7.904 1.00 87.43 ? 271 GLN A CG 1 ATOM 1468 C CD . GLN A 1 183 ? 6.234 51.672 6.638 1.00 95.69 ? 271 GLN A CD 1 ATOM 1469 O OE1 . GLN A 1 183 ? 5.003 51.562 6.688 1.00 92.26 ? 271 GLN A OE1 1 ATOM 1470 N NE2 . GLN A 1 183 ? 6.909 51.686 5.493 1.00 105.86 ? 271 GLN A NE2 1 ATOM 1471 N N . ASN A 1 184 ? 6.404 51.672 11.898 1.00 56.87 ? 272 ASN A N 1 ATOM 1472 C CA . ASN A 1 184 ? 5.875 52.762 12.723 1.00 57.24 ? 272 ASN A CA 1 ATOM 1473 C C . ASN A 1 184 ? 5.759 52.401 14.220 1.00 56.09 ? 272 ASN A C 1 ATOM 1474 O O . ASN A 1 184 ? 4.652 52.303 14.775 1.00 52.57 ? 272 ASN A O 1 ATOM 1475 C CB . ASN A 1 184 ? 4.512 53.200 12.182 1.00 63.72 ? 272 ASN A CB 1 ATOM 1476 C CG . ASN A 1 184 ? 3.926 54.388 12.935 1.00 69.43 ? 272 ASN A CG 1 ATOM 1477 O OD1 . ASN A 1 184 ? 4.641 55.329 13.306 1.00 75.25 ? 272 ASN A OD1 1 ATOM 1478 N ND2 . ASN A 1 184 ? 2.609 54.348 13.160 1.00 57.59 ? 272 ASN A ND2 1 ATOM 1479 N N . PRO A 1 185 ? 6.905 52.184 14.875 1.00 51.03 ? 273 PRO A N 1 ATOM 1480 C CA . PRO A 1 185 ? 6.895 51.832 16.294 1.00 53.58 ? 273 PRO A CA 1 ATOM 1481 C C . PRO A 1 185 ? 6.655 53.098 17.139 1.00 53.37 ? 273 PRO A C 1 ATOM 1482 O O . PRO A 1 185 ? 6.954 54.202 16.680 1.00 55.92 ? 273 PRO A O 1 ATOM 1483 C CB . PRO A 1 185 ? 8.299 51.272 16.496 1.00 49.01 ? 273 PRO A CB 1 ATOM 1484 C CG . PRO A 1 185 ? 9.137 52.028 15.540 1.00 52.05 ? 273 PRO A CG 1 ATOM 1485 C CD . PRO A 1 185 ? 8.277 52.277 14.335 1.00 56.85 ? 273 PRO A CD 1 ATOM 1486 N N . ASP A 1 186 ? 6.100 52.958 18.336 1.00 50.23 ? 274 ASP A N 1 ATOM 1487 C CA . ASP A 1 186 ? 5.878 54.136 19.171 1.00 44.18 ? 274 ASP A CA 1 ATOM 1488 C C . ASP A 1 186 ? 7.212 54.730 19.576 1.00 43.74 ? 274 ASP A C 1 ATOM 1489 O O . ASP A 1 186 ? 7.435 55.921 19.410 1.00 51.79 ? 274 ASP A O 1 ATOM 1490 C CB . ASP A 1 186 ? 5.023 53.806 20.388 1.00 50.35 ? 274 ASP A CB 1 ATOM 1491 C CG . ASP A 1 186 ? 4.361 55.033 20.972 1.00 54.29 ? 274 ASP A CG 1 ATOM 1492 O OD1 . ASP A 1 186 ? 4.449 56.104 20.341 1.00 70.60 ? 274 ASP A OD1 1 ATOM 1493 O OD2 . ASP A 1 186 ? 3.736 54.934 22.043 1.00 53.70 ? 274 ASP A OD2 1 ATOM 1494 N N . TYR A 1 187 ? 8.110 53.901 20.106 1.00 44.10 ? 275 TYR A N 1 ATOM 1495 C CA . TYR A 1 187 ? 9.513 54.308 20.208 1.00 50.23 ? 275 TYR A CA 1 ATOM 1496 C C . TYR A 1 187 ? 10.400 53.430 19.338 1.00 54.38 ? 275 TYR A C 1 ATOM 1497 O O . TYR A 1 187 ? 10.162 52.233 19.198 1.00 61.41 ? 275 TYR A O 1 ATOM 1498 C CB . TYR A 1 187 ? 9.987 54.322 21.667 1.00 62.49 ? 275 TYR A CB 1 ATOM 1499 C CG . TYR A 1 187 ? 9.494 55.537 22.419 1.00 65.66 ? 275 TYR A CG 1 ATOM 1500 C CD1 . TYR A 1 187 ? 8.185 55.607 22.888 1.00 67.76 ? 275 TYR A CD1 1 ATOM 1501 C CD2 . TYR A 1 187 ? 10.326 56.624 22.631 1.00 67.00 ? 275 TYR A CD2 1 ATOM 1502 C CE1 . TYR A 1 187 ? 7.723 56.725 23.557 1.00 66.82 ? 275 TYR A CE1 1 ATOM 1503 C CE2 . TYR A 1 187 ? 9.876 57.742 23.297 1.00 71.76 ? 275 TYR A CE2 1 ATOM 1504 C CZ . TYR A 1 187 ? 8.575 57.789 23.758 1.00 68.93 ? 275 TYR A CZ 1 ATOM 1505 O OH . TYR A 1 187 ? 8.141 58.913 24.425 1.00 69.59 ? 275 TYR A OH 1 ATOM 1506 N N . ASN A 1 188 ? 11.416 54.031 18.733 1.00 53.93 ? 276 ASN A N 1 ATOM 1507 C CA . ASN A 1 188 ? 12.332 53.276 17.895 1.00 55.85 ? 276 ASN A CA 1 ATOM 1508 C C . ASN A 1 188 ? 13.472 52.653 18.701 1.00 55.55 ? 276 ASN A C 1 ATOM 1509 O O . ASN A 1 188 ? 14.595 53.164 18.748 1.00 61.82 ? 276 ASN A O 1 ATOM 1510 C CB . ASN A 1 188 ? 12.859 54.138 16.748 1.00 59.75 ? 276 ASN A CB 1 ATOM 1511 C CG . ASN A 1 188 ? 13.577 53.324 15.697 1.00 60.64 ? 276 ASN A CG 1 ATOM 1512 O OD1 . ASN A 1 188 ? 13.638 52.101 15.783 1.00 62.63 ? 276 ASN A OD1 1 ATOM 1513 N ND2 . ASN A 1 188 ? 14.130 54.000 14.696 1.00 65.29 ? 276 ASN A ND2 1 ATOM 1514 N N . PHE A 1 189 ? 13.165 51.516 19.308 1.00 56.59 ? 277 PHE A N 1 ATOM 1515 C CA . PHE A 1 189 ? 14.064 50.880 20.248 1.00 61.81 ? 277 PHE A CA 1 ATOM 1516 C C . PHE A 1 189 ? 14.978 49.881 19.554 1.00 62.85 ? 277 PHE A C 1 ATOM 1517 O O . PHE A 1 189 ? 15.961 49.430 20.150 1.00 70.59 ? 277 PHE A O 1 ATOM 1518 C CB . PHE A 1 189 ? 13.256 50.178 21.341 1.00 52.14 ? 277 PHE A CB 1 ATOM 1519 C CG . PHE A 1 189 ? 12.441 49.034 20.832 1.00 50.31 ? 277 PHE A CG 1 ATOM 1520 C CD1 . PHE A 1 189 ? 11.206 49.251 20.257 1.00 46.89 ? 277 PHE A CD1 1 ATOM 1521 C CD2 . PHE A 1 189 ? 12.915 47.739 20.918 1.00 53.22 ? 277 PHE A CD2 1 ATOM 1522 C CE1 . PHE A 1 189 ? 10.455 48.206 19.783 1.00 43.81 ? 277 PHE A CE1 1 ATOM 1523 C CE2 . PHE A 1 189 ? 12.161 46.678 20.445 1.00 46.89 ? 277 PHE A CE2 1 ATOM 1524 C CZ . PHE A 1 189 ? 10.932 46.915 19.877 1.00 42.68 ? 277 PHE A CZ 1 ATOM 1525 N N . PHE A 1 190 ? 14.669 49.548 18.300 1.00 59.02 ? 278 PHE A N 1 ATOM 1526 C CA . PHE A 1 190 ? 15.446 48.540 17.558 1.00 60.00 ? 278 PHE A CA 1 ATOM 1527 C C . PHE A 1 190 ? 16.950 48.752 17.598 1.00 54.70 ? 278 PHE A C 1 ATOM 1528 O O . PHE A 1 190 ? 17.700 47.796 17.804 1.00 61.39 ? 278 PHE A O 1 ATOM 1529 C CB . PHE A 1 190 ? 14.942 48.383 16.111 1.00 50.23 ? 278 PHE A CB 1 ATOM 1530 C CG . PHE A 1 190 ? 13.505 47.975 16.036 1.00 47.21 ? 278 PHE A CG 1 ATOM 1531 C CD1 . PHE A 1 190 ? 13.106 46.731 16.485 1.00 51.37 ? 278 PHE A CD1 1 ATOM 1532 C CD2 . PHE A 1 190 ? 12.548 48.849 15.571 1.00 47.99 ? 278 PHE A CD2 1 ATOM 1533 C CE1 . PHE A 1 190 ? 11.776 46.360 16.449 1.00 48.79 ? 278 PHE A CE1 1 ATOM 1534 C CE2 . PHE A 1 190 ? 11.219 48.489 15.522 1.00 44.53 ? 278 PHE A CE2 1 ATOM 1535 C CZ . PHE A 1 190 ? 10.826 47.246 15.967 1.00 46.29 ? 278 PHE A CZ 1 ATOM 1536 N N . ASN A 1 191 ? 17.402 49.990 17.429 1.00 67.20 ? 279 ASN A N 1 ATOM 1537 C CA . ASN A 1 191 ? 18.841 50.264 17.514 1.00 75.92 ? 279 ASN A CA 1 ATOM 1538 C C . ASN A 1 191 ? 19.469 49.854 18.844 1.00 74.50 ? 279 ASN A C 1 ATOM 1539 O O . ASN A 1 191 ? 20.543 49.248 18.883 1.00 78.24 ? 279 ASN A O 1 ATOM 1540 C CB . ASN A 1 191 ? 19.128 51.742 17.264 1.00 84.45 ? 279 ASN A CB 1 ATOM 1541 C CG . ASN A 1 191 ? 19.130 52.087 15.805 1.00 89.99 ? 279 ASN A CG 1 ATOM 1542 O OD1 . ASN A 1 191 ? 19.898 51.520 15.022 1.00 89.65 ? 279 ASN A OD1 1 ATOM 1543 N ND2 . ASN A 1 191 ? 18.251 53.009 15.416 1.00 93.56 ? 279 ASN A ND2 1 ATOM 1544 N N . ASN A 1 192 ? 18.789 50.197 19.931 1.00 72.53 ? 280 ASN A N 1 ATOM 1545 C CA . ASN A 1 192 ? 19.329 49.975 21.265 1.00 79.42 ? 280 ASN A CA 1 ATOM 1546 C C . ASN A 1 192 ? 19.182 48.513 21.683 1.00 69.10 ? 280 ASN A C 1 ATOM 1547 O O . ASN A 1 192 ? 20.071 47.951 22.315 1.00 73.20 ? 280 ASN A O 1 ATOM 1548 C CB . ASN A 1 192 ? 18.675 50.931 22.273 1.00 87.12 ? 280 ASN A CB 1 ATOM 1549 C CG . ASN A 1 192 ? 18.675 52.377 21.788 1.00 97.99 ? 280 ASN A CG 1 ATOM 1550 O OD1 . ASN A 1 192 ? 18.026 52.708 20.792 1.00 106.68 ? 280 ASN A OD1 1 ATOM 1551 N ND2 . ASN A 1 192 ? 19.392 53.241 22.490 1.00 97.98 ? 280 ASN A ND2 1 ATOM 1552 N N . TYR A 1 193 ? 18.063 47.899 21.318 1.00 61.10 ? 281 TYR A N 1 ATOM 1553 C CA . TYR A 1 193 ? 17.906 46.454 21.484 1.00 65.21 ? 281 TYR A CA 1 ATOM 1554 C C . TYR A 1 193 ? 19.084 45.705 20.839 1.00 70.85 ? 281 TYR A C 1 ATOM 1555 O O . TYR A 1 193 ? 19.682 44.817 21.451 1.00 77.79 ? 281 TYR A O 1 ATOM 1556 C CB . TYR A 1 193 ? 16.556 45.975 20.917 1.00 57.59 ? 281 TYR A CB 1 ATOM 1557 C CG . TYR A 1 193 ? 16.367 44.463 20.920 1.00 56.61 ? 281 TYR A CG 1 ATOM 1558 C CD1 . TYR A 1 193 ? 16.917 43.669 19.915 1.00 55.14 ? 281 TYR A CD1 1 ATOM 1559 C CD2 . TYR A 1 193 ? 15.630 43.833 21.923 1.00 51.37 ? 281 TYR A CD2 1 ATOM 1560 C CE1 . TYR A 1 193 ? 16.758 42.294 19.916 1.00 63.48 ? 281 TYR A CE1 1 ATOM 1561 C CE2 . TYR A 1 193 ? 15.465 42.444 21.931 1.00 52.40 ? 281 TYR A CE2 1 ATOM 1562 C CZ . TYR A 1 193 ? 16.026 41.685 20.919 1.00 60.26 ? 281 TYR A CZ 1 ATOM 1563 O OH . TYR A 1 193 ? 15.879 40.311 20.895 1.00 63.06 ? 281 TYR A OH 1 ATOM 1564 N N . LYS A 1 194 ? 19.423 46.071 19.608 1.00 69.16 ? 282 LYS A N 1 ATOM 1565 C CA . LYS A 1 194 ? 20.554 45.464 18.940 1.00 70.49 ? 282 LYS A CA 1 ATOM 1566 C C . LYS A 1 194 ? 21.822 45.735 19.719 1.00 82.72 ? 282 LYS A C 1 ATOM 1567 O O . LYS A 1 194 ? 22.642 44.840 19.924 1.00 93.04 ? 282 LYS A O 1 ATOM 1568 C CB . LYS A 1 194 ? 20.725 46.039 17.536 1.00 71.95 ? 282 LYS A CB 1 ATOM 1569 C CG . LYS A 1 194 ? 19.659 45.624 16.543 1.00 68.73 ? 282 LYS A CG 1 ATOM 1570 C CD . LYS A 1 194 ? 20.010 46.127 15.172 1.00 75.40 ? 282 LYS A CD 1 ATOM 1571 C CE . LYS A 1 194 ? 18.809 46.077 14.262 1.00 76.37 ? 282 LYS A CE 1 ATOM 1572 N NZ . LYS A 1 194 ? 19.216 46.343 12.857 1.00 74.73 ? 282 LYS A NZ 1 ATOM 1573 N N . THR A 1 195 ? 21.987 46.981 20.143 1.00 77.21 ? 283 THR A N 1 ATOM 1574 C CA . THR A 1 195 ? 23.231 47.392 20.783 1.00 83.07 ? 283 THR A CA 1 ATOM 1575 C C . THR A 1 195 ? 23.432 46.657 22.102 1.00 81.10 ? 283 THR A C 1 ATOM 1576 O O . THR A 1 195 ? 24.536 46.238 22.426 1.00 86.87 ? 283 THR A O 1 ATOM 1577 C CB . THR A 1 195 ? 23.268 48.912 20.991 1.00 87.57 ? 283 THR A CB 1 ATOM 1578 O OG1 . THR A 1 195 ? 23.289 49.557 19.709 1.00 93.17 ? 283 THR A OG1 1 ATOM 1579 C CG2 . THR A 1 195 ? 24.508 49.317 21.789 1.00 88.08 ? 283 THR A CG2 1 ATOM 1580 N N . TYR A 1 196 ? 22.344 46.483 22.845 1.00 80.71 ? 284 TYR A N 1 ATOM 1581 C CA . TYR A 1 196 ? 22.361 45.677 24.062 1.00 79.48 ? 284 TYR A CA 1 ATOM 1582 C C . TYR A 1 196 ? 22.729 44.232 23.726 1.00 81.67 ? 284 TYR A C 1 ATOM 1583 O O . TYR A 1 196 ? 23.615 43.631 24.332 1.00 84.62 ? 284 TYR A O 1 ATOM 1584 C CB . TYR A 1 196 ? 20.985 45.717 24.735 1.00 75.58 ? 284 TYR A CB 1 ATOM 1585 C CG . TYR A 1 196 ? 21.000 45.229 26.151 1.00 80.45 ? 284 TYR A CG 1 ATOM 1586 C CD1 . TYR A 1 196 ? 21.219 46.115 27.204 1.00 81.58 ? 284 TYR A CD1 1 ATOM 1587 C CD2 . TYR A 1 196 ? 20.813 43.885 26.450 1.00 80.03 ? 284 TYR A CD2 1 ATOM 1588 C CE1 . TYR A 1 196 ? 21.244 45.680 28.515 1.00 83.62 ? 284 TYR A CE1 1 ATOM 1589 C CE2 . TYR A 1 196 ? 20.834 43.438 27.771 1.00 83.58 ? 284 TYR A CE2 1 ATOM 1590 C CZ . TYR A 1 196 ? 21.055 44.343 28.798 1.00 82.56 ? 284 TYR A CZ 1 ATOM 1591 O OH . TYR A 1 196 ? 21.086 43.921 30.113 1.00 75.89 ? 284 TYR A OH 1 ATOM 1592 N N . ARG A 1 197 ? 22.040 43.684 22.737 1.00 82.25 ? 285 ARG A N 1 ATOM 1593 C CA . ARG A 1 197 ? 22.253 42.306 22.315 1.00 83.35 ? 285 ARG A CA 1 ATOM 1594 C C . ARG A 1 197 ? 23.730 41.986 22.082 1.00 85.78 ? 285 ARG A C 1 ATOM 1595 O O . ARG A 1 197 ? 24.216 40.905 22.454 1.00 88.70 ? 285 ARG A O 1 ATOM 1596 C CB . ARG A 1 197 ? 21.436 42.051 21.060 1.00 85.11 ? 285 ARG A CB 1 ATOM 1597 C CG . ARG A 1 197 ? 20.701 40.746 21.068 1.00 86.51 ? 285 ARG A CG 1 ATOM 1598 C CD . ARG A 1 197 ? 19.685 40.639 22.185 1.00 78.62 ? 285 ARG A CD 1 ATOM 1599 N NE . ARG A 1 197 ? 19.204 39.263 22.203 1.00 89.49 ? 285 ARG A NE 1 ATOM 1600 C CZ . ARG A 1 197 ? 19.878 38.247 22.733 1.00 101.57 ? 285 ARG A CZ 1 ATOM 1601 N NH1 . ARG A 1 197 ? 21.046 38.461 23.316 1.00 111.03 ? 285 ARG A NH1 1 ATOM 1602 N NH2 . ARG A 1 197 ? 19.383 37.018 22.687 1.00 106.20 ? 285 ARG A NH2 1 ATOM 1603 N N . LYS A 1 198 ? 24.450 42.942 21.496 1.00 90.36 ? 286 LYS A N 1 ATOM 1604 C CA . LYS A 1 198 ? 25.898 42.825 21.304 1.00 96.28 ? 286 LYS A CA 1 ATOM 1605 C C . LYS A 1 198 ? 26.616 42.747 22.653 1.00 99.37 ? 286 LYS A C 1 ATOM 1606 O O . LYS A 1 198 ? 27.545 41.957 22.829 1.00 101.57 ? 286 LYS A O 1 ATOM 1607 C CB . LYS A 1 198 ? 26.446 44.023 20.514 1.00 102.65 ? 286 LYS A CB 1 ATOM 1608 C CG . LYS A 1 198 ? 25.986 44.134 19.062 1.00 109.63 ? 286 LYS A CG 1 ATOM 1609 C CD . LYS A 1 198 ? 26.131 45.577 18.552 1.00 114.88 ? 286 LYS A CD 1 ATOM 1610 C CE . LYS A 1 198 ? 25.339 45.811 17.261 1.00 111.01 ? 286 LYS A CE 1 ATOM 1611 N NZ . LYS A 1 198 ? 24.930 47.237 17.058 1.00 105.80 ? 286 LYS A NZ 1 ATOM 1612 N N . LEU A 1 199 ? 26.182 43.579 23.599 1.00 99.33 ? 287 LEU A N 1 ATOM 1613 C CA . LEU A 1 199 ? 26.813 43.656 24.915 1.00 100.24 ? 287 LEU A CA 1 ATOM 1614 C C . LEU A 1 199 ? 26.561 42.420 25.766 1.00 102.30 ? 287 LEU A C 1 ATOM 1615 O O . LEU A 1 199 ? 27.444 41.970 26.494 1.00 108.74 ? 287 LEU A O 1 ATOM 1616 C CB . LEU A 1 199 ? 26.306 44.877 25.671 1.00 94.76 ? 287 LEU A CB 1 ATOM 1617 C CG . LEU A 1 199 ? 26.713 46.261 25.179 1.00 95.48 ? 287 LEU A CG 1 ATOM 1618 C CD1 . LEU A 1 199 ? 25.924 47.330 25.938 1.00 90.51 ? 287 LEU A CD1 1 ATOM 1619 C CD2 . LEU A 1 199 ? 28.205 46.454 25.362 1.00 102.21 ? 287 LEU A CD2 1 ATOM 1620 N N . HIS A 1 200 ? 25.349 41.882 25.692 1.00 94.39 ? 288 HIS A N 1 ATOM 1621 C CA . HIS A 1 200 ? 25.003 40.721 26.504 1.00 97.58 ? 288 HIS A CA 1 ATOM 1622 C C . HIS A 1 200 ? 24.350 39.584 25.712 1.00 99.35 ? 288 HIS A C 1 ATOM 1623 O O . HIS A 1 200 ? 23.175 39.290 25.921 1.00 86.47 ? 288 HIS A O 1 ATOM 1624 C CB . HIS A 1 200 ? 24.086 41.150 27.646 1.00 94.95 ? 288 HIS A CB 1 ATOM 1625 C CG . HIS A 1 200 ? 24.598 42.326 28.423 1.00 103.42 ? 288 HIS A CG 1 ATOM 1626 N ND1 . HIS A 1 200 ? 25.503 42.201 29.455 1.00 106.88 ? 288 HIS A ND1 1 ATOM 1627 C CD2 . HIS A 1 200 ? 24.323 43.649 28.322 1.00 98.37 ? 288 HIS A CD2 1 ATOM 1628 C CE1 . HIS A 1 200 ? 25.766 43.396 29.954 1.00 105.19 ? 288 HIS A CE1 1 ATOM 1629 N NE2 . HIS A 1 200 ? 25.064 44.292 29.284 1.00 99.66 ? 288 HIS A NE2 1 ATOM 1630 N N . PRO A 1 201 ? 25.124 38.920 24.829 1.00 102.19 ? 289 PRO A N 1 ATOM 1631 C CA . PRO A 1 201 ? 24.621 37.855 23.950 1.00 101.88 ? 289 PRO A CA 1 ATOM 1632 C C . PRO A 1 201 ? 23.989 36.716 24.740 1.00 100.70 ? 289 PRO A C 1 ATOM 1633 O O . PRO A 1 201 ? 23.022 36.098 24.288 1.00 91.11 ? 289 PRO A O 1 ATOM 1634 C CB . PRO A 1 201 ? 25.890 37.338 23.259 1.00 106.30 ? 289 PRO A CB 1 ATOM 1635 C CG . PRO A 1 201 ? 26.918 38.393 23.456 1.00 103.13 ? 289 PRO A CG 1 ATOM 1636 C CD . PRO A 1 201 ? 26.588 39.048 24.753 1.00 109.30 ? 289 PRO A CD 1 ATOM 1637 N N . ASN A 1 202 ? 24.542 36.461 25.921 1.00 102.75 ? 290 ASN A N 1 ATOM 1638 C CA . ASN A 1 202 ? 24.100 35.368 26.780 1.00 108.85 ? 290 ASN A CA 1 ATOM 1639 C C . ASN A 1 202 ? 22.734 35.554 27.447 1.00 104.33 ? 290 ASN A C 1 ATOM 1640 O O . ASN A 1 202 ? 22.057 34.570 27.737 1.00 95.49 ? 290 ASN A O 1 ATOM 1641 C CB . ASN A 1 202 ? 25.153 35.068 27.853 1.00 116.67 ? 290 ASN A CB 1 ATOM 1642 C CG . ASN A 1 202 ? 25.641 33.633 27.802 1.00 122.63 ? 290 ASN A CG 1 ATOM 1643 O OD1 . ASN A 1 202 ? 25.579 32.988 26.754 1.00 123.26 ? 290 ASN A OD1 1 ATOM 1644 N ND2 . ASN A 1 202 ? 26.129 33.125 28.934 1.00 125.33 ? 290 ASN A ND2 1 ATOM 1645 N N . GLN A 1 203 ? 22.318 36.789 27.710 1.00 104.34 ? 291 GLN A N 1 ATOM 1646 C CA . GLN A 1 203 ? 21.064 36.953 28.451 1.00 102.72 ? 291 GLN A CA 1 ATOM 1647 C C . GLN A 1 203 ? 19.829 37.112 27.566 1.00 97.98 ? 291 GLN A C 1 ATOM 1648 O O . GLN A 1 203 ? 19.755 37.998 26.700 1.00 76.52 ? 291 GLN A O 1 ATOM 1649 C CB . GLN A 1 203 ? 21.147 38.010 29.570 1.00 106.99 ? 291 GLN A CB 1 ATOM 1650 C CG . GLN A 1 203 ? 20.829 39.439 29.169 1.00 101.77 ? 291 GLN A CG 1 ATOM 1651 C CD . GLN A 1 203 ? 20.273 40.268 30.321 1.00 95.87 ? 291 GLN A CD 1 ATOM 1652 O OE1 . GLN A 1 203 ? 20.643 41.430 30.494 1.00 102.13 ? 291 GLN A OE1 1 ATOM 1653 N NE2 . GLN A 1 203 ? 19.356 39.685 31.094 1.00 85.58 ? 291 GLN A NE2 1 ATOM 1654 N N . PRO A 1 204 ? 18.852 36.223 27.781 1.00 95.70 ? 292 PRO A N 1 ATOM 1655 C CA . PRO A 1 204 ? 17.665 36.166 26.930 1.00 84.70 ? 292 PRO A CA 1 ATOM 1656 C C . PRO A 1 204 ? 16.919 37.490 26.973 1.00 77.37 ? 292 PRO A C 1 ATOM 1657 O O . PRO A 1 204 ? 16.630 38.016 28.051 1.00 80.14 ? 292 PRO A O 1 ATOM 1658 C CB . PRO A 1 204 ? 16.840 35.032 27.552 1.00 87.15 ? 292 PRO A CB 1 ATOM 1659 C CG . PRO A 1 204 ? 17.834 34.218 28.338 1.00 93.11 ? 292 PRO A CG 1 ATOM 1660 C CD . PRO A 1 204 ? 18.818 35.216 28.857 1.00 94.63 ? 292 PRO A CD 1 ATOM 1661 N N . PHE A 1 205 ? 16.632 38.030 25.793 1.00 74.82 ? 293 PHE A N 1 ATOM 1662 C CA . PHE A 1 205 ? 16.000 39.335 25.651 1.00 65.91 ? 293 PHE A CA 1 ATOM 1663 C C . PHE A 1 205 ? 14.995 39.232 24.517 1.00 67.25 ? 293 PHE A C 1 ATOM 1664 O O . PHE A 1 205 ? 15.367 39.112 23.355 1.00 75.69 ? 293 PHE A O 1 ATOM 1665 C CB . PHE A 1 205 ? 17.059 40.386 25.328 1.00 61.55 ? 293 PHE A CB 1 ATOM 1666 C CG . PHE A 1 205 ? 16.569 41.801 25.387 1.00 57.83 ? 293 PHE A CG 1 ATOM 1667 C CD1 . PHE A 1 205 ? 15.232 42.092 25.599 1.00 53.74 ? 293 PHE A CD1 1 ATOM 1668 C CD2 . PHE A 1 205 ? 17.461 42.850 25.238 1.00 59.03 ? 293 PHE A CD2 1 ATOM 1669 C CE1 . PHE A 1 205 ? 14.793 43.396 25.659 1.00 50.87 ? 293 PHE A CE1 1 ATOM 1670 C CE2 . PHE A 1 205 ? 17.029 44.162 25.303 1.00 56.24 ? 293 PHE A CE2 1 ATOM 1671 C CZ . PHE A 1 205 ? 15.695 44.435 25.514 1.00 56.02 ? 293 PHE A CZ 1 ATOM 1672 N N . TYR A 1 206 ? 13.718 39.288 24.860 1.00 63.21 ? 294 TYR A N 1 ATOM 1673 C CA . TYR A 1 206 ? 12.665 39.069 23.888 1.00 60.08 ? 294 TYR A CA 1 ATOM 1674 C C . TYR A 1 206 ? 11.927 40.370 23.575 1.00 59.90 ? 294 TYR A C 1 ATOM 1675 O O . TYR A 1 206 ? 11.990 41.332 24.334 1.00 61.36 ? 294 TYR A O 1 ATOM 1676 C CB . TYR A 1 206 ? 11.686 38.019 24.416 1.00 52.42 ? 294 TYR A CB 1 ATOM 1677 C CG . TYR A 1 206 ? 12.309 36.669 24.647 1.00 57.01 ? 294 TYR A CG 1 ATOM 1678 C CD1 . TYR A 1 206 ? 12.979 36.380 25.829 1.00 71.95 ? 294 TYR A CD1 1 ATOM 1679 C CD2 . TYR A 1 206 ? 12.214 35.674 23.689 1.00 58.76 ? 294 TYR A CD2 1 ATOM 1680 C CE1 . TYR A 1 206 ? 13.554 35.137 26.038 1.00 82.16 ? 294 TYR A CE1 1 ATOM 1681 C CE2 . TYR A 1 206 ? 12.777 34.436 23.885 1.00 78.91 ? 294 TYR A CE2 1 ATOM 1682 C CZ . TYR A 1 206 ? 13.452 34.167 25.059 1.00 83.80 ? 294 TYR A CZ 1 ATOM 1683 O OH . TYR A 1 206 ? 14.018 32.915 25.239 1.00 86.36 ? 294 TYR A OH 1 ATOM 1684 N N . ILE A 1 207 ? 11.237 40.389 22.440 1.00 54.41 ? 295 ILE A N 1 ATOM 1685 C CA . ILE A 1 207 ? 10.375 41.496 22.068 1.00 45.36 ? 295 ILE A CA 1 ATOM 1686 C C . ILE A 1 207 ? 8.960 40.947 22.071 1.00 44.48 ? 295 ILE A C 1 ATOM 1687 O O . ILE A 1 207 ? 8.684 39.941 21.427 1.00 52.56 ? 295 ILE A O 1 ATOM 1688 C CB . ILE A 1 207 ? 10.688 41.990 20.625 1.00 49.58 ? 295 ILE A CB 1 ATOM 1689 C CG1 . ILE A 1 207 ? 12.143 42.433 20.505 1.00 45.16 ? 295 ILE A CG1 1 ATOM 1690 C CG2 . ILE A 1 207 ? 9.764 43.140 20.216 1.00 46.46 ? 295 ILE A CG2 1 ATOM 1691 C CD1 . ILE A 1 207 ? 12.507 42.856 19.103 1.00 57.46 ? 295 ILE A CD1 1 ATOM 1692 N N . LEU A 1 208 ? 8.068 41.592 22.805 1.00 41.88 ? 296 LEU A N 1 ATOM 1693 C CA . LEU A 1 208 ? 6.669 41.198 22.794 1.00 46.17 ? 296 LEU A CA 1 ATOM 1694 C C . LEU A 1 208 ? 6.032 41.489 21.429 1.00 45.17 ? 296 LEU A C 1 ATOM 1695 O O . LEU A 1 208 ? 6.280 42.548 20.841 1.00 44.31 ? 296 LEU A O 1 ATOM 1696 C CB . LEU A 1 208 ? 5.940 41.975 23.893 1.00 39.58 ? 296 LEU A CB 1 ATOM 1697 C CG . LEU A 1 208 ? 4.491 41.570 24.164 1.00 41.14 ? 296 LEU A CG 1 ATOM 1698 C CD1 . LEU A 1 208 ? 4.447 40.112 24.567 1.00 50.73 ? 296 LEU A CD1 1 ATOM 1699 C CD2 . LEU A 1 208 ? 3.877 42.493 25.259 1.00 39.44 ? 296 LEU A CD2 1 ATOM 1700 N N . LYS A 1 209 ? 5.227 40.571 20.905 1.00 50.77 ? 297 LYS A N 1 ATOM 1701 C CA . LYS A 1 209 ? 4.479 40.880 19.681 1.00 49.08 ? 297 LYS A CA 1 ATOM 1702 C C . LYS A 1 209 ? 3.539 42.067 19.963 1.00 49.52 ? 297 LYS A C 1 ATOM 1703 O O . LYS A 1 209 ? 2.943 42.146 21.039 1.00 45.02 ? 297 LYS A O 1 ATOM 1704 C CB . LYS A 1 209 ? 3.698 39.664 19.173 1.00 40.16 ? 297 LYS A CB 1 ATOM 1705 C CG . LYS A 1 209 ? 4.558 38.567 18.574 1.00 48.56 ? 297 LYS A CG 1 ATOM 1706 C CD . LYS A 1 209 ? 3.796 37.678 17.596 1.00 53.87 ? 297 LYS A CD 1 ATOM 1707 C CE . LYS A 1 209 ? 4.340 36.256 17.645 1.00 64.72 ? 297 LYS A CE 1 ATOM 1708 N NZ . LYS A 1 209 ? 4.796 35.734 16.341 1.00 64.86 ? 297 LYS A NZ 1 ATOM 1709 N N . PRO A 1 210 ? 3.409 42.992 19.000 1.00 51.97 ? 298 PRO A N 1 ATOM 1710 C CA . PRO A 1 210 ? 2.604 44.214 19.130 1.00 45.47 ? 298 PRO A CA 1 ATOM 1711 C C . PRO A 1 210 ? 1.125 43.911 19.287 1.00 45.19 ? 298 PRO A C 1 ATOM 1712 O O . PRO A 1 210 ? 0.392 44.709 19.864 1.00 47.50 ? 298 PRO A O 1 ATOM 1713 C CB . PRO A 1 210 ? 2.846 44.932 17.791 1.00 42.91 ? 298 PRO A CB 1 ATOM 1714 C CG . PRO A 1 210 ? 3.290 43.879 16.875 1.00 46.66 ? 298 PRO A CG 1 ATOM 1715 C CD . PRO A 1 210 ? 4.095 42.939 17.696 1.00 53.05 ? 298 PRO A CD 1 ATOM 1716 N N . GLN A 1 211 ? 0.697 42.756 18.799 1.00 41.52 ? 299 GLN A N 1 ATOM 1717 C CA . GLN A 1 211 ? -0.704 42.372 18.915 1.00 45.63 ? 299 GLN A CA 1 ATOM 1718 C C . GLN A 1 211 ? -1.130 42.073 20.353 1.00 53.03 ? 299 GLN A C 1 ATOM 1719 O O . GLN A 1 211 ? -2.299 42.242 20.704 1.00 50.38 ? 299 GLN A O 1 ATOM 1720 C CB . GLN A 1 211 ? -1.018 41.153 18.051 1.00 42.27 ? 299 GLN A CB 1 ATOM 1721 C CG . GLN A 1 211 ? -0.908 41.369 16.543 1.00 50.33 ? 299 GLN A CG 1 ATOM 1722 C CD . GLN A 1 211 ? 0.434 40.944 16.044 1.00 54.15 ? 299 GLN A CD 1 ATOM 1723 O OE1 . GLN A 1 211 ? 1.414 40.978 16.789 1.00 47.87 ? 299 GLN A OE1 1 ATOM 1724 N NE2 . GLN A 1 211 ? 0.507 40.542 14.783 1.00 52.77 ? 299 GLN A NE2 1 ATOM 1725 N N . MET A 1 212 ? -0.201 41.622 21.193 1.00 51.17 ? 300 MET A N 1 ATOM 1726 C CA . MET A 1 212 ? -0.597 41.170 22.530 1.00 48.10 ? 300 MET A CA 1 ATOM 1727 C C . MET A 1 212 ? -1.281 42.252 23.393 1.00 50.35 ? 300 MET A C 1 ATOM 1728 O O . MET A 1 212 ? -2.341 41.999 23.971 1.00 46.20 ? 300 MET A O 1 ATOM 1729 C CB . MET A 1 212 ? 0.565 40.469 23.254 1.00 48.13 ? 300 MET A CB 1 ATOM 1730 C CG . MET A 1 212 ? 0.186 39.743 24.544 1.00 52.79 ? 300 MET A CG 1 ATOM 1731 S SD . MET A 1 212 ? 0.315 40.856 25.936 1.00 64.58 ? 300 MET A SD 1 ATOM 1732 C CE . MET A 1 212 ? 0.736 39.698 27.242 1.00 56.94 ? 300 MET A CE 1 ATOM 1733 N N . PRO A 1 213 ? -0.702 43.456 23.486 1.00 48.61 ? 301 PRO A N 1 ATOM 1734 C CA . PRO A 1 213 ? -1.356 44.430 24.376 1.00 45.23 ? 301 PRO A CA 1 ATOM 1735 C C . PRO A 1 213 ? -2.778 44.795 23.941 1.00 49.45 ? 301 PRO A C 1 ATOM 1736 O O . PRO A 1 213 ? -3.606 45.104 24.801 1.00 49.54 ? 301 PRO A O 1 ATOM 1737 C CB . PRO A 1 213 ? -0.471 45.666 24.249 1.00 43.82 ? 301 PRO A CB 1 ATOM 1738 C CG . PRO A 1 213 ? 0.849 45.159 23.718 1.00 38.59 ? 301 PRO A CG 1 ATOM 1739 C CD . PRO A 1 213 ? 0.576 43.947 22.949 1.00 45.74 ? 301 PRO A CD 1 ATOM 1740 N N . TRP A 1 214 ? -3.063 44.768 22.639 1.00 44.41 ? 302 TRP A N 1 ATOM 1741 C CA . TRP A 1 214 ? -4.395 45.165 22.179 1.00 47.26 ? 302 TRP A CA 1 ATOM 1742 C C . TRP A 1 214 ? -5.374 44.023 22.343 1.00 47.27 ? 302 TRP A C 1 ATOM 1743 O O . TRP A 1 214 ? -6.569 44.236 22.530 1.00 47.26 ? 302 TRP A O 1 ATOM 1744 C CB . TRP A 1 214 ? -4.386 45.692 20.731 1.00 42.95 ? 302 TRP A CB 1 ATOM 1745 C CG . TRP A 1 214 ? -3.661 47.012 20.603 1.00 36.23 ? 302 TRP A CG 1 ATOM 1746 C CD1 . TRP A 1 214 ? -2.522 47.247 19.918 1.00 41.58 ? 302 TRP A CD1 1 ATOM 1747 C CD2 . TRP A 1 214 ? -4.018 48.260 21.229 1.00 43.99 ? 302 TRP A CD2 1 ATOM 1748 N NE1 . TRP A 1 214 ? -2.145 48.567 20.053 1.00 38.87 ? 302 TRP A NE1 1 ATOM 1749 C CE2 . TRP A 1 214 ? -3.054 49.208 20.851 1.00 42.21 ? 302 TRP A CE2 1 ATOM 1750 C CE3 . TRP A 1 214 ? -5.058 48.662 22.069 1.00 43.67 ? 302 TRP A CE3 1 ATOM 1751 C CZ2 . TRP A 1 214 ? -3.092 50.535 21.291 1.00 43.66 ? 302 TRP A CZ2 1 ATOM 1752 C CZ3 . TRP A 1 214 ? -5.100 49.988 22.498 1.00 46.00 ? 302 TRP A CZ3 1 ATOM 1753 C CH2 . TRP A 1 214 ? -4.123 50.903 22.112 1.00 39.95 ? 302 TRP A CH2 1 ATOM 1754 N N . GLU A 1 215 ? -4.875 42.794 22.292 1.00 44.82 ? 303 GLU A N 1 ATOM 1755 C CA . GLU A 1 215 ? -5.753 41.664 22.527 1.00 46.92 ? 303 GLU A CA 1 ATOM 1756 C C . GLU A 1 215 ? -6.223 41.741 23.979 1.00 48.90 ? 303 GLU A C 1 ATOM 1757 O O . GLU A 1 215 ? -7.357 41.417 24.296 1.00 58.60 ? 303 GLU A O 1 ATOM 1758 C CB . GLU A 1 215 ? -5.048 40.338 22.220 1.00 50.30 ? 303 GLU A CB 1 ATOM 1759 C CG . GLU A 1 215 ? -4.795 40.084 20.728 1.00 54.14 ? 303 GLU A CG 1 ATOM 1760 C CD . GLU A 1 215 ? -3.726 39.016 20.494 1.00 64.39 ? 303 GLU A CD 1 ATOM 1761 O OE1 . GLU A 1 215 ? -3.348 38.346 21.479 1.00 59.13 ? 303 GLU A OE1 1 ATOM 1762 O OE2 . GLU A 1 215 ? -3.267 38.842 19.330 1.00 73.13 ? 303 GLU A OE2 1 ATOM 1763 N N . LEU A 1 216 ? -5.358 42.199 24.864 1.00 51.48 ? 304 LEU A N 1 ATOM 1764 C CA . LEU A 1 216 ? -5.752 42.304 26.256 1.00 52.12 ? 304 LEU A CA 1 ATOM 1765 C C . LEU A 1 216 ? -6.693 43.503 26.432 1.00 55.66 ? 304 LEU A C 1 ATOM 1766 O O . LEU A 1 216 ? -7.669 43.428 27.169 1.00 60.11 ? 304 LEU A O 1 ATOM 1767 C CB . LEU A 1 216 ? -4.515 42.406 27.134 1.00 47.54 ? 304 LEU A CB 1 ATOM 1768 C CG . LEU A 1 216 ? -4.778 42.596 28.626 1.00 55.14 ? 304 LEU A CG 1 ATOM 1769 C CD1 . LEU A 1 216 ? -5.601 41.447 29.179 1.00 59.38 ? 304 LEU A CD1 1 ATOM 1770 C CD2 . LEU A 1 216 ? -3.463 42.691 29.353 1.00 42.56 ? 304 LEU A CD2 1 ATOM 1771 N N . TRP A 1 217 ? -6.423 44.581 25.694 1.00 52.67 ? 305 TRP A N 1 ATOM 1772 C CA . TRP A 1 217 ? -7.257 45.785 25.743 1.00 45.72 ? 305 TRP A CA 1 ATOM 1773 C C . TRP A 1 217 ? -8.682 45.523 25.324 1.00 48.12 ? 305 TRP A C 1 ATOM 1774 O O . TRP A 1 217 ? -9.609 46.076 25.898 1.00 55.74 ? 305 TRP A O 1 ATOM 1775 C CB . TRP A 1 217 ? -6.686 46.855 24.834 1.00 41.61 ? 305 TRP A CB 1 ATOM 1776 C CG . TRP A 1 217 ? -7.339 48.190 24.991 1.00 44.20 ? 305 TRP A CG 1 ATOM 1777 C CD1 . TRP A 1 217 ? -6.944 49.203 25.830 1.00 35.55 ? 305 TRP A CD1 1 ATOM 1778 C CD2 . TRP A 1 217 ? -8.473 48.689 24.267 1.00 48.62 ? 305 TRP A CD2 1 ATOM 1779 N NE1 . TRP A 1 217 ? -7.771 50.290 25.676 1.00 48.60 ? 305 TRP A NE1 1 ATOM 1780 C CE2 . TRP A 1 217 ? -8.714 50.003 24.723 1.00 50.24 ? 305 TRP A CE2 1 ATOM 1781 C CE3 . TRP A 1 217 ? -9.296 48.160 23.267 1.00 51.07 ? 305 TRP A CE3 1 ATOM 1782 C CZ2 . TRP A 1 217 ? -9.759 50.785 24.225 1.00 46.95 ? 305 TRP A CZ2 1 ATOM 1783 C CZ3 . TRP A 1 217 ? -10.336 48.934 22.781 1.00 50.68 ? 305 TRP A CZ3 1 ATOM 1784 C CH2 . TRP A 1 217 ? -10.556 50.231 23.258 1.00 53.71 ? 305 TRP A CH2 1 ATOM 1785 N N . ASP A 1 218 ? -8.862 44.681 24.316 1.00 57.41 ? 306 ASP A N 1 ATOM 1786 C CA . ASP A 1 218 ? -10.198 44.409 23.813 1.00 57.71 ? 306 ASP A CA 1 ATOM 1787 C C . ASP A 1 218 ? -11.063 43.879 24.945 1.00 62.40 ? 306 ASP A C 1 ATOM 1788 O O . ASP A 1 218 ? -12.231 44.251 25.080 1.00 67.66 ? 306 ASP A O 1 ATOM 1789 C CB . ASP A 1 218 ? -10.168 43.399 22.659 1.00 60.84 ? 306 ASP A CB 1 ATOM 1790 C CG . ASP A 1 218 ? -9.717 44.019 21.360 1.00 64.28 ? 306 ASP A CG 1 ATOM 1791 O OD1 . ASP A 1 218 ? -9.707 45.261 21.290 1.00 59.93 ? 306 ASP A OD1 1 ATOM 1792 O OD2 . ASP A 1 218 ? -9.374 43.276 20.409 1.00 72.78 ? 306 ASP A OD2 1 ATOM 1793 N N . ILE A 1 219 ? -10.481 43.005 25.757 1.00 58.61 ? 307 ILE A N 1 ATOM 1794 C CA . ILE A 1 219 ? -11.231 42.341 26.818 1.00 66.95 ? 307 ILE A CA 1 ATOM 1795 C C . ILE A 1 219 ? -11.585 43.362 27.897 1.00 64.80 ? 307 ILE A C 1 ATOM 1796 O O . ILE A 1 219 ? -12.713 43.398 28.380 1.00 74.77 ? 307 ILE A O 1 ATOM 1797 C CB . ILE A 1 219 ? -10.438 41.136 27.383 1.00 64.24 ? 307 ILE A CB 1 ATOM 1798 C CG1 . ILE A 1 219 ? -9.973 40.244 26.227 1.00 60.34 ? 307 ILE A CG1 1 ATOM 1799 C CG2 . ILE A 1 219 ? -11.255 40.368 28.389 1.00 77.07 ? 307 ILE A CG2 1 ATOM 1800 C CD1 . ILE A 1 219 ? -9.699 38.806 26.608 1.00 61.13 ? 307 ILE A CD1 1 ATOM 1801 N N . LEU A 1 220 ? -10.619 44.215 28.227 1.00 60.46 ? 308 LEU A N 1 ATOM 1802 C CA . LEU A 1 220 ? -10.828 45.318 29.148 1.00 55.84 ? 308 LEU A CA 1 ATOM 1803 C C . LEU A 1 220 ? -12.014 46.181 28.735 1.00 61.24 ? 308 LEU A C 1 ATOM 1804 O O . LEU A 1 220 ? -12.999 46.272 29.473 1.00 62.17 ? 308 LEU A O 1 ATOM 1805 C CB . LEU A 1 220 ? -9.562 46.153 29.269 1.00 51.56 ? 308 LEU A CB 1 ATOM 1806 C CG . LEU A 1 220 ? -8.392 45.404 29.915 1.00 50.43 ? 308 LEU A CG 1 ATOM 1807 C CD1 . LEU A 1 220 ? -7.117 46.231 29.823 1.00 41.14 ? 308 LEU A CD1 1 ATOM 1808 C CD2 . LEU A 1 220 ? -8.709 45.058 31.398 1.00 56.95 ? 308 LEU A CD2 1 ATOM 1809 N N . GLN A 1 221 ? -11.936 46.772 27.545 1.00 65.97 ? 309 GLN A N 1 ATOM 1810 C CA . GLN A 1 221 ? -13.020 47.594 27.010 1.00 63.06 ? 309 GLN A CA 1 ATOM 1811 C C . GLN A 1 221 ? -14.333 46.856 26.995 1.00 67.62 ? 309 GLN A C 1 ATOM 1812 O O . GLN A 1 221 ? -15.397 47.428 27.270 1.00 73.32 ? 309 GLN A O 1 ATOM 1813 C CB . GLN A 1 221 ? -12.715 48.033 25.585 1.00 63.83 ? 309 GLN A CB 1 ATOM 1814 C CG . GLN A 1 221 ? -13.820 48.905 25.018 1.00 63.94 ? 309 GLN A CG 1 ATOM 1815 C CD . GLN A 1 221 ? -13.948 50.183 25.805 1.00 66.83 ? 309 GLN A CD 1 ATOM 1816 O OE1 . GLN A 1 221 ? -13.131 51.088 25.646 1.00 64.06 ? 309 GLN A OE1 1 ATOM 1817 N NE2 . GLN A 1 221 ? -14.945 50.251 26.699 1.00 69.47 ? 309 GLN A NE2 1 ATOM 1818 N N . GLU A 1 222 ? -14.265 45.572 26.676 1.00 66.73 ? 310 GLU A N 1 ATOM 1819 C CA . GLU A 1 222 ? -15.468 44.755 26.663 1.00 77.57 ? 310 GLU A CA 1 ATOM 1820 C C . GLU A 1 222 ? -16.049 44.589 28.071 1.00 74.68 ? 310 GLU A C 1 ATOM 1821 O O . GLU A 1 222 ? -17.262 44.550 28.249 1.00 75.93 ? 310 GLU A O 1 ATOM 1822 C CB . GLU A 1 222 ? -15.190 43.386 26.046 1.00 76.17 ? 310 GLU A CB 1 ATOM 1823 C CG . GLU A 1 222 ? -16.449 42.565 25.840 1.00 83.89 ? 310 GLU A CG 1 ATOM 1824 C CD . GLU A 1 222 ? -16.164 41.109 25.547 1.00 92.38 ? 310 GLU A CD 1 ATOM 1825 O OE1 . GLU A 1 222 ? -15.030 40.647 25.810 1.00 93.77 ? 310 GLU A OE1 1 ATOM 1826 O OE2 . GLU A 1 222 ? -17.082 40.426 25.052 1.00 98.67 ? 310 GLU A OE2 1 ATOM 1827 N N . ILE A 1 223 ? -15.180 44.493 29.068 1.00 72.31 ? 311 ILE A N 1 ATOM 1828 C CA . ILE A 1 223 ? -15.625 44.329 30.444 1.00 83.11 ? 311 ILE A CA 1 ATOM 1829 C C . ILE A 1 223 ? -16.220 45.613 31.023 1.00 89.23 ? 311 ILE A C 1 ATOM 1830 O O . ILE A 1 223 ? -17.248 45.597 31.705 1.00 93.73 ? 311 ILE A O 1 ATOM 1831 C CB . ILE A 1 223 ? -14.452 43.936 31.350 1.00 82.27 ? 311 ILE A CB 1 ATOM 1832 C CG1 . ILE A 1 223 ? -14.096 42.468 31.168 1.00 82.90 ? 311 ILE A CG1 1 ATOM 1833 C CG2 . ILE A 1 223 ? -14.803 44.166 32.810 1.00 95.45 ? 311 ILE A CG2 1 ATOM 1834 C CD1 . ILE A 1 223 ? -12.952 42.050 32.071 1.00 80.87 ? 311 ILE A CD1 1 ATOM 1835 N N . SER A 1 224 ? -15.553 46.730 30.760 1.00 86.90 ? 312 SER A N 1 ATOM 1836 C CA . SER A 1 224 ? -15.834 47.961 31.485 1.00 77.48 ? 312 SER A CA 1 ATOM 1837 C C . SER A 1 224 ? -17.161 48.599 31.078 1.00 85.53 ? 312 SER A C 1 ATOM 1838 O O . SER A 1 224 ? -17.594 48.464 29.935 1.00 89.04 ? 312 SER A O 1 ATOM 1839 C CB . SER A 1 224 ? -14.667 48.922 31.325 1.00 66.16 ? 312 SER A CB 1 ATOM 1840 O OG . SER A 1 224 ? -13.451 48.250 31.649 1.00 57.93 ? 312 SER A OG 1 ATOM 1841 N N . PRO A 1 225 ? -17.821 49.287 32.025 1.00 92.62 ? 313 PRO A N 1 ATOM 1842 C CA . PRO A 1 225 ? -19.151 49.825 31.738 1.00 96.34 ? 313 PRO A CA 1 ATOM 1843 C C . PRO A 1 225 ? -19.066 51.078 30.881 1.00 96.46 ? 313 PRO A C 1 ATOM 1844 O O . PRO A 1 225 ? -20.093 51.668 30.558 1.00 110.30 ? 313 PRO A O 1 ATOM 1845 C CB . PRO A 1 225 ? -19.672 50.185 33.128 1.00 93.99 ? 313 PRO A CB 1 ATOM 1846 C CG . PRO A 1 225 ? -18.443 50.589 33.870 1.00 90.10 ? 313 PRO A CG 1 ATOM 1847 C CD . PRO A 1 225 ? -17.346 49.685 33.366 1.00 86.93 ? 313 PRO A CD 1 ATOM 1848 N N . GLU A 1 226 ? -17.855 51.481 30.519 1.00 86.19 ? 314 GLU A N 1 ATOM 1849 C CA . GLU A 1 226 ? -17.675 52.702 29.750 1.00 80.83 ? 314 GLU A CA 1 ATOM 1850 C C . GLU A 1 226 ? -16.385 52.665 28.942 1.00 73.45 ? 314 GLU A C 1 ATOM 1851 O O . GLU A 1 226 ? -15.550 51.774 29.113 1.00 69.44 ? 314 GLU A O 1 ATOM 1852 C CB . GLU A 1 226 ? -17.643 53.901 30.693 1.00 77.20 ? 314 GLU A CB 1 ATOM 1853 C CG . GLU A 1 226 ? -16.310 54.062 31.384 1.00 72.10 ? 314 GLU A CG 1 ATOM 1854 C CD . GLU A 1 226 ? -16.361 55.043 32.536 1.00 77.41 ? 314 GLU A CD 1 ATOM 1855 O OE1 . GLU A 1 226 ? -17.290 55.885 32.572 1.00 74.90 ? 314 GLU A OE1 1 ATOM 1856 O OE2 . GLU A 1 226 ? -15.470 54.964 33.412 1.00 78.37 ? 314 GLU A OE2 1 ATOM 1857 N N . GLU A 1 227 ? -16.218 53.650 28.067 1.00 73.37 ? 315 GLU A N 1 ATOM 1858 C CA . GLU A 1 227 ? -15.009 53.747 27.268 1.00 73.27 ? 315 GLU A CA 1 ATOM 1859 C C . GLU A 1 227 ? -13.796 53.952 28.153 1.00 68.33 ? 315 GLU A C 1 ATOM 1860 O O . GLU A 1 227 ? -13.786 54.838 29.011 1.00 69.31 ? 315 GLU A O 1 ATOM 1861 C CB . GLU A 1 227 ? -15.106 54.908 26.288 1.00 83.83 ? 315 GLU A CB 1 ATOM 1862 C CG . GLU A 1 227 ? -16.227 54.777 25.298 1.00 101.71 ? 315 GLU A CG 1 ATOM 1863 C CD . GLU A 1 227 ? -16.286 55.954 24.347 1.00 115.68 ? 315 GLU A CD 1 ATOM 1864 O OE1 . GLU A 1 227 ? -16.338 57.109 24.832 1.00 117.52 ? 315 GLU A OE1 1 ATOM 1865 O OE2 . GLU A 1 227 ? -16.271 55.722 23.117 1.00 122.67 ? 315 GLU A OE2 1 ATOM 1866 N N . ILE A 1 228 ? -12.773 53.136 27.926 1.00 57.37 ? 316 ILE A N 1 ATOM 1867 C CA . ILE A 1 228 ? -11.532 53.232 28.660 1.00 55.98 ? 316 ILE A CA 1 ATOM 1868 C C . ILE A 1 228 ? -10.501 53.938 27.783 1.00 55.67 ? 316 ILE A C 1 ATOM 1869 O O . ILE A 1 228 ? -10.695 54.052 26.571 1.00 56.97 ? 316 ILE A O 1 ATOM 1870 C CB . ILE A 1 228 ? -11.033 51.833 29.032 1.00 58.66 ? 316 ILE A CB 1 ATOM 1871 C CG1 . ILE A 1 228 ? -10.532 51.103 27.791 1.00 50.72 ? 316 ILE A CG1 1 ATOM 1872 C CG2 . ILE A 1 228 ? -12.154 51.022 29.643 1.00 61.16 ? 316 ILE A CG2 1 ATOM 1873 C CD1 . ILE A 1 228 ? -10.245 49.591 28.024 1.00 43.60 ? 316 ILE A CD1 1 ATOM 1874 N N . GLN A 1 229 ? -9.426 54.438 28.395 1.00 47.24 ? 317 GLN A N 1 ATOM 1875 C CA . GLN A 1 229 ? -8.339 55.038 27.642 1.00 46.61 ? 317 GLN A CA 1 ATOM 1876 C C . GLN A 1 229 ? -7.955 54.135 26.488 1.00 48.77 ? 317 GLN A C 1 ATOM 1877 O O . GLN A 1 229 ? -7.703 52.946 26.691 1.00 47.60 ? 317 GLN A O 1 ATOM 1878 C CB . GLN A 1 229 ? -7.106 55.219 28.520 1.00 46.90 ? 317 GLN A CB 1 ATOM 1879 C CG . GLN A 1 229 ? -7.224 56.327 29.554 1.00 48.73 ? 317 GLN A CG 1 ATOM 1880 C CD . GLN A 1 229 ? -7.705 55.822 30.878 1.00 50.81 ? 317 GLN A CD 1 ATOM 1881 O OE1 . GLN A 1 229 ? -8.533 54.911 30.951 1.00 47.56 ? 317 GLN A OE1 1 ATOM 1882 N NE2 . GLN A 1 229 ? -7.183 56.409 31.952 1.00 49.89 ? 317 GLN A NE2 1 ATOM 1883 N N . PRO A 1 230 ? -7.919 54.693 25.270 1.00 48.72 ? 318 PRO A N 1 ATOM 1884 C CA . PRO A 1 230 ? -7.549 53.922 24.087 1.00 45.54 ? 318 PRO A CA 1 ATOM 1885 C C . PRO A 1 230 ? -6.037 53.815 23.976 1.00 47.40 ? 318 PRO A C 1 ATOM 1886 O O . PRO A 1 230 ? -5.463 54.029 22.938 1.00 50.96 ? 318 PRO A O 1 ATOM 1887 C CB . PRO A 1 230 ? -8.099 54.768 22.944 1.00 52.69 ? 318 PRO A CB 1 ATOM 1888 C CG . PRO A 1 230 ? -8.074 56.157 23.471 1.00 52.47 ? 318 PRO A CG 1 ATOM 1889 C CD . PRO A 1 230 ? -8.440 56.023 24.917 1.00 42.20 ? 318 PRO A CD 1 ATOM 1890 N N . ASN A 1 231 ? -5.397 53.495 25.080 1.00 49.32 ? 319 ASN A N 1 ATOM 1891 C CA . ASN A 1 231 ? -3.972 53.283 25.087 1.00 43.65 ? 319 ASN A CA 1 ATOM 1892 C C . ASN A 1 231 ? -3.771 51.891 25.650 1.00 46.71 ? 319 ASN A C 1 ATOM 1893 O O . ASN A 1 231 ? -4.602 51.416 26.400 1.00 44.57 ? 319 ASN A O 1 ATOM 1894 C CB . ASN A 1 231 ? -3.325 54.336 25.972 1.00 43.23 ? 319 ASN A CB 1 ATOM 1895 C CG . ASN A 1 231 ? -3.653 55.745 25.517 1.00 50.64 ? 319 ASN A CG 1 ATOM 1896 O OD1 . ASN A 1 231 ? -3.612 56.044 24.321 1.00 48.91 ? 319 ASN A OD1 1 ATOM 1897 N ND2 . ASN A 1 231 ? -3.994 56.614 26.465 1.00 49.28 ? 319 ASN A ND2 1 ATOM 1898 N N . PRO A 1 232 ? -2.700 51.201 25.238 1.00 44.78 ? 320 PRO A N 1 ATOM 1899 C CA . PRO A 1 232 ? -2.492 49.831 25.722 1.00 48.92 ? 320 PRO A CA 1 ATOM 1900 C C . PRO A 1 232 ? -2.461 49.706 27.264 1.00 43.85 ? 320 PRO A C 1 ATOM 1901 O O . PRO A 1 232 ? -2.233 50.694 28.001 1.00 43.04 ? 320 PRO A O 1 ATOM 1902 C CB . PRO A 1 232 ? -1.142 49.451 25.101 1.00 39.14 ? 320 PRO A CB 1 ATOM 1903 C CG . PRO A 1 232 ? -0.487 50.752 24.759 1.00 36.01 ? 320 PRO A CG 1 ATOM 1904 C CD . PRO A 1 232 ? -1.601 51.671 24.387 1.00 35.74 ? 320 PRO A CD 1 ATOM 1905 N N . PRO A 1 233 ? -2.720 48.492 27.765 1.00 43.79 ? 321 PRO A N 1 ATOM 1906 C CA . PRO A 1 233 ? -2.616 48.223 29.195 1.00 46.49 ? 321 PRO A CA 1 ATOM 1907 C C . PRO A 1 233 ? -1.214 48.538 29.729 1.00 50.28 ? 321 PRO A C 1 ATOM 1908 O O . PRO A 1 233 ? -0.261 48.594 28.936 1.00 46.64 ? 321 PRO A O 1 ATOM 1909 C CB . PRO A 1 233 ? -2.886 46.717 29.281 1.00 46.76 ? 321 PRO A CB 1 ATOM 1910 C CG . PRO A 1 233 ? -3.644 46.388 28.019 1.00 45.23 ? 321 PRO A CG 1 ATOM 1911 C CD . PRO A 1 233 ? -3.200 47.324 27.003 1.00 43.07 ? 321 PRO A CD 1 ATOM 1912 N N . SER A 1 234 ? -1.100 48.732 31.047 1.00 41.74 ? 322 SER A N 1 ATOM 1913 C CA . SER A 1 234 ? 0.171 49.077 31.681 1.00 43.63 ? 322 SER A CA 1 ATOM 1914 C C . SER A 1 234 ? 1.120 47.884 31.630 1.00 39.23 ? 322 SER A C 1 ATOM 1915 O O . SER A 1 234 ? 0.685 46.748 31.474 1.00 38.66 ? 322 SER A O 1 ATOM 1916 C CB . SER A 1 234 ? -0.065 49.563 33.135 1.00 40.51 ? 322 SER A CB 1 ATOM 1917 O OG . SER A 1 234 ? -0.357 48.479 33.992 1.00 45.39 ? 322 SER A OG 1 ATOM 1918 N N . SER A 1 235 ? 2.423 48.110 31.756 1.00 38.93 ? 323 SER A N 1 ATOM 1919 C CA . SER A 1 235 ? 3.342 46.963 31.831 1.00 38.67 ? 323 SER A CA 1 ATOM 1920 C C . SER A 1 235 ? 2.890 45.982 32.918 1.00 37.72 ? 323 SER A C 1 ATOM 1921 O O . SER A 1 235 ? 3.014 44.764 32.785 1.00 44.81 ? 323 SER A O 1 ATOM 1922 C CB . SER A 1 235 ? 4.771 47.445 32.126 1.00 42.51 ? 323 SER A CB 1 ATOM 1923 O OG . SER A 1 235 ? 5.266 48.293 31.083 1.00 44.96 ? 323 SER A OG 1 ATOM 1924 N N . GLY A 1 236 ? 2.342 46.515 34.001 1.00 52.96 ? 324 GLY A N 1 ATOM 1925 C CA . GLY A 1 236 ? 1.887 45.664 35.086 1.00 44.91 ? 324 GLY A CA 1 ATOM 1926 C C . GLY A 1 236 ? 0.830 44.650 34.683 1.00 43.02 ? 324 GLY A C 1 ATOM 1927 O O . GLY A 1 236 ? 0.921 43.476 35.048 1.00 50.66 ? 324 GLY A O 1 ATOM 1928 N N . MET A 1 237 ? -0.182 45.073 33.938 1.00 50.08 ? 325 MET A N 1 ATOM 1929 C CA . MET A 1 237 ? -1.198 44.109 33.518 1.00 50.76 ? 325 MET A CA 1 ATOM 1930 C C . MET A 1 237 ? -0.624 43.070 32.542 1.00 50.81 ? 325 MET A C 1 ATOM 1931 O O . MET A 1 237 ? -0.927 41.876 32.647 1.00 52.50 ? 325 MET A O 1 ATOM 1932 C CB . MET A 1 237 ? -2.389 44.814 32.869 1.00 49.29 ? 325 MET A CB 1 ATOM 1933 C CG . MET A 1 237 ? -3.577 43.871 32.684 1.00 54.62 ? 325 MET A CG 1 ATOM 1934 S SD . MET A 1 237 ? -4.179 43.365 34.289 1.00 60.13 ? 325 MET A SD 1 ATOM 1935 C CE . MET A 1 237 ? -4.482 41.622 34.059 1.00 55.33 ? 325 MET A CE 1 ATOM 1936 N N . LEU A 1 238 ? 0.196 43.517 31.594 1.00 48.64 ? 326 LEU A N 1 ATOM 1937 C CA . LEU A 1 238 ? 0.801 42.584 30.621 1.00 44.79 ? 326 LEU A CA 1 ATOM 1938 C C . LEU A 1 238 ? 1.692 41.612 31.368 1.00 48.94 ? 326 LEU A C 1 ATOM 1939 O O . LEU A 1 238 ? 1.716 40.421 31.072 1.00 49.87 ? 326 LEU A O 1 ATOM 1940 C CB . LEU A 1 238 ? 1.644 43.318 29.581 1.00 39.36 ? 326 LEU A CB 1 ATOM 1941 C CG . LEU A 1 238 ? 1.103 44.530 28.826 1.00 37.80 ? 326 LEU A CG 1 ATOM 1942 C CD1 . LEU A 1 238 ? 2.274 45.312 28.248 1.00 36.50 ? 326 LEU A CD1 1 ATOM 1943 C CD2 . LEU A 1 238 ? 0.161 44.116 27.700 1.00 49.02 ? 326 LEU A CD2 1 ATOM 1944 N N . GLY A 1 239 ? 2.384 42.125 32.385 1.00 50.86 ? 327 GLY A N 1 ATOM 1945 C CA . GLY A 1 239 ? 3.245 41.286 33.186 1.00 49.36 ? 327 GLY A CA 1 ATOM 1946 C C . GLY A 1 239 ? 2.453 40.238 33.948 1.00 59.50 ? 327 GLY A C 1 ATOM 1947 O O . GLY A 1 239 ? 2.903 39.087 34.083 1.00 59.04 ? 327 GLY A O 1 ATOM 1948 N N . ILE A 1 240 ? 1.278 40.617 34.450 1.00 63.57 ? 328 ILE A N 1 ATOM 1949 C CA . ILE A 1 240 ? 0.411 39.641 35.110 1.00 66.92 ? 328 ILE A CA 1 ATOM 1950 C C . ILE A 1 240 ? 0.048 38.534 34.117 1.00 71.57 ? 328 ILE A C 1 ATOM 1951 O O . ILE A 1 240 ? 0.241 37.351 34.400 1.00 75.03 ? 328 ILE A O 1 ATOM 1952 C CB . ILE A 1 240 ? -0.851 40.302 35.742 1.00 54.94 ? 328 ILE A CB 1 ATOM 1953 C CG1 . ILE A 1 240 ? -0.500 40.984 37.070 1.00 52.27 ? 328 ILE A CG1 1 ATOM 1954 C CG2 . ILE A 1 240 ? -1.919 39.275 36.037 1.00 53.07 ? 328 ILE A CG2 1 ATOM 1955 C CD1 . ILE A 1 240 ? -1.172 42.336 37.207 1.00 49.43 ? 328 ILE A CD1 1 ATOM 1956 N N . ILE A 1 241 ? -0.440 38.919 32.941 1.00 64.95 ? 329 ILE A N 1 ATOM 1957 C CA . ILE A 1 241 ? -0.821 37.936 31.927 1.00 63.37 ? 329 ILE A CA 1 ATOM 1958 C C . ILE A 1 241 ? 0.359 37.042 31.542 1.00 54.94 ? 329 ILE A C 1 ATOM 1959 O O . ILE A 1 241 ? 0.202 35.849 31.327 1.00 55.68 ? 329 ILE A O 1 ATOM 1960 C CB . ILE A 1 241 ? -1.395 38.608 30.658 1.00 60.40 ? 329 ILE A CB 1 ATOM 1961 C CG1 . ILE A 1 241 ? -2.560 39.524 31.032 1.00 58.75 ? 329 ILE A CG1 1 ATOM 1962 C CG2 . ILE A 1 241 ? -1.894 37.562 29.697 1.00 61.07 ? 329 ILE A CG2 1 ATOM 1963 C CD1 . ILE A 1 241 ? -3.802 38.754 31.466 1.00 56.64 ? 329 ILE A CD1 1 ATOM 1964 N N . ILE A 1 242 ? 1.544 37.632 31.455 1.00 60.66 ? 330 ILE A N 1 ATOM 1965 C CA . ILE A 1 242 ? 2.716 36.858 31.080 1.00 60.99 ? 330 ILE A CA 1 ATOM 1966 C C . ILE A 1 242 ? 2.987 35.796 32.123 1.00 71.29 ? 330 ILE A C 1 ATOM 1967 O O . ILE A 1 242 ? 3.023 34.610 31.816 1.00 74.90 ? 330 ILE A O 1 ATOM 1968 C CB . ILE A 1 242 ? 3.963 37.751 30.927 1.00 57.73 ? 330 ILE A CB 1 ATOM 1969 C CG1 . ILE A 1 242 ? 3.828 38.652 29.698 1.00 60.63 ? 330 ILE A CG1 1 ATOM 1970 C CG2 . ILE A 1 242 ? 5.198 36.871 30.825 1.00 58.79 ? 330 ILE A CG2 1 ATOM 1971 C CD1 . ILE A 1 242 ? 4.949 39.653 29.523 1.00 55.40 ? 330 ILE A CD1 1 ATOM 1972 N N . MET A 1 243 ? 3.147 36.219 33.373 1.00 69.88 ? 331 MET A N 1 ATOM 1973 C CA . MET A 1 243 ? 3.434 35.268 34.443 1.00 62.60 ? 331 MET A CA 1 ATOM 1974 C C . MET A 1 243 ? 2.352 34.214 34.554 1.00 66.20 ? 331 MET A C 1 ATOM 1975 O O . MET A 1 243 ? 2.636 33.075 34.870 1.00 73.31 ? 331 MET A O 1 ATOM 1976 C CB . MET A 1 243 ? 3.624 35.998 35.776 1.00 68.96 ? 331 MET A CB 1 ATOM 1977 C CG . MET A 1 243 ? 4.787 36.951 35.704 1.00 69.38 ? 331 MET A CG 1 ATOM 1978 S SD . MET A 1 243 ? 6.223 36.121 34.992 1.00 73.49 ? 331 MET A SD 1 ATOM 1979 C CE . MET A 1 243 ? 6.740 35.140 36.403 1.00 72.60 ? 331 MET A CE 1 ATOM 1980 N N . MET A 1 244 ? 1.109 34.581 34.276 1.00 76.38 ? 332 MET A N 1 ATOM 1981 C CA . MET A 1 244 ? 0.051 33.577 34.221 1.00 72.78 ? 332 MET A CA 1 ATOM 1982 C C . MET A 1 244 ? 0.329 32.522 33.147 1.00 70.28 ? 332 MET A C 1 ATOM 1983 O O . MET A 1 244 ? -0.000 31.345 33.328 1.00 79.89 ? 332 MET A O 1 ATOM 1984 C CB . MET A 1 244 ? -1.307 34.238 34.004 1.00 69.98 ? 332 MET A CB 1 ATOM 1985 C CG . MET A 1 244 ? -1.926 34.678 35.313 1.00 66.79 ? 332 MET A CG 1 ATOM 1986 S SD . MET A 1 244 ? -3.300 35.821 35.122 1.00 72.37 ? 332 MET A SD 1 ATOM 1987 C CE . MET A 1 244 ? -4.654 34.675 34.889 1.00 82.05 ? 332 MET A CE 1 ATOM 1988 N N . THR A 1 245 ? 0.968 32.922 32.047 1.00 67.24 ? 333 THR A N 1 ATOM 1989 C CA . THR A 1 245 ? 1.294 31.944 31.002 1.00 69.01 ? 333 THR A CA 1 ATOM 1990 C C . THR A 1 245 ? 2.445 31.014 31.398 1.00 75.61 ? 333 THR A C 1 ATOM 1991 O O . THR A 1 245 ? 2.649 29.983 30.765 1.00 81.52 ? 333 THR A O 1 ATOM 1992 C CB . THR A 1 245 ? 1.640 32.600 29.643 1.00 64.59 ? 333 THR A CB 1 ATOM 1993 O OG1 . THR A 1 245 ? 1.187 33.948 29.622 1.00 62.84 ? 333 THR A OG1 1 ATOM 1994 C CG2 . THR A 1 245 ? 0.946 31.870 28.509 1.00 81.96 ? 333 THR A CG2 1 ATOM 1995 N N . LEU A 1 246 ? 3.189 31.370 32.443 1.00 73.73 ? 334 LEU A N 1 ATOM 1996 C CA . LEU A 1 246 ? 4.418 30.661 32.809 1.00 77.82 ? 334 LEU A CA 1 ATOM 1997 C C . LEU A 1 246 ? 4.411 30.074 34.219 1.00 88.64 ? 334 LEU A C 1 ATOM 1998 O O . LEU A 1 246 ? 5.378 29.440 34.639 1.00 89.62 ? 334 LEU A O 1 ATOM 1999 C CB . LEU A 1 246 ? 5.607 31.620 32.717 1.00 82.10 ? 334 LEU A CB 1 ATOM 2000 C CG . LEU A 1 246 ? 6.288 31.973 31.389 1.00 84.34 ? 334 LEU A CG 1 ATOM 2001 C CD1 . LEU A 1 246 ? 5.411 31.758 30.176 1.00 81.99 ? 334 LEU A CD1 1 ATOM 2002 C CD2 . LEU A 1 246 ? 6.741 33.402 31.448 1.00 78.27 ? 334 LEU A CD2 1 ATOM 2003 N N . CYS A 1 247 ? 3.344 30.307 34.970 1.00 93.06 ? 335 CYS A N 1 ATOM 2004 C CA . CYS A 1 247 ? 3.344 29.936 36.379 1.00 94.71 ? 335 CYS A CA 1 ATOM 2005 C C . CYS A 1 247 ? 2.065 29.220 36.761 1.00 91.79 ? 335 CYS A C 1 ATOM 2006 O O . CYS A 1 247 ? 1.036 29.386 36.118 1.00 90.00 ? 335 CYS A O 1 ATOM 2007 C CB . CYS A 1 247 ? 3.475 31.179 37.254 1.00 91.79 ? 335 CYS A CB 1 ATOM 2008 S SG . CYS A 1 247 ? 4.918 32.223 36.954 1.00 96.44 ? 335 CYS A SG 1 ATOM 2009 N N . ASP A 1 248 ? 2.122 28.435 37.826 1.00 102.74 ? 336 ASP A N 1 ATOM 2010 C CA . ASP A 1 248 ? 0.905 27.857 38.367 1.00 106.91 ? 336 ASP A CA 1 ATOM 2011 C C . ASP A 1 248 ? 0.180 28.893 39.211 1.00 104.95 ? 336 ASP A C 1 ATOM 2012 O O . ASP A 1 248 ? -1.047 28.996 39.167 1.00 99.29 ? 336 ASP A O 1 ATOM 2013 C CB . ASP A 1 248 ? 1.223 26.609 39.184 1.00 111.20 ? 336 ASP A CB 1 ATOM 2014 C CG . ASP A 1 248 ? 1.886 25.535 38.355 1.00 134.83 ? 336 ASP A CG 1 ATOM 2015 O OD1 . ASP A 1 248 ? 1.893 25.668 37.105 1.00 130.72 ? 336 ASP A OD1 1 ATOM 2016 O OD2 . ASP A 1 248 ? 2.396 24.558 38.945 1.00 142.12 ? 336 ASP A OD2 1 ATOM 2017 N N . GLN A 1 249 ? 0.956 29.684 39.946 1.00 106.88 ? 337 GLN A N 1 ATOM 2018 C CA . GLN A 1 249 ? 0.411 30.604 40.931 1.00 101.28 ? 337 GLN A CA 1 ATOM 2019 C C . GLN A 1 249 ? 1.076 31.968 40.812 1.00 94.97 ? 337 GLN A C 1 ATOM 2020 O O . GLN A 1 249 ? 2.300 32.086 40.902 1.00 89.12 ? 337 GLN A O 1 ATOM 2021 C CB . GLN A 1 249 ? 0.637 30.038 42.334 1.00 107.96 ? 337 GLN A CB 1 ATOM 2022 C CG . GLN A 1 249 ? -0.500 30.294 43.308 1.00 109.81 ? 337 GLN A CG 1 ATOM 2023 C CD . GLN A 1 249 ? -0.156 29.844 44.715 1.00 124.95 ? 337 GLN A CD 1 ATOM 2024 O OE1 . GLN A 1 249 ? 0.094 30.668 45.594 1.00 109.53 ? 337 GLN A OE1 1 ATOM 2025 N NE2 . GLN A 1 249 ? -0.129 28.531 44.933 1.00 137.38 ? 337 GLN A NE2 1 ATOM 2026 N N . VAL A 1 250 ? 0.277 33.006 40.601 1.00 84.10 ? 338 VAL A N 1 ATOM 2027 C CA . VAL A 1 250 ? 0.837 34.351 40.630 1.00 78.65 ? 338 VAL A CA 1 ATOM 2028 C C . VAL A 1 250 ? 0.331 35.202 41.789 1.00 83.90 ? 338 VAL A C 1 ATOM 2029 O O . VAL A 1 250 ? -0.864 35.455 41.960 1.00 77.88 ? 338 VAL A O 1 ATOM 2030 C CB . VAL A 1 250 ? 0.722 35.102 39.281 1.00 86.09 ? 338 VAL A CB 1 ATOM 2031 C CG1 . VAL A 1 250 ? 1.256 34.230 38.161 1.00 93.25 ? 338 VAL A CG1 1 ATOM 2032 C CG2 . VAL A 1 250 ? -0.707 35.530 38.997 1.00 82.09 ? 338 VAL A CG2 1 ATOM 2033 N N . ASP A 1 251 ? 1.278 35.618 42.609 1.00 90.39 ? 339 ASP A N 1 ATOM 2034 C CA . ASP A 1 251 ? 0.973 36.516 43.698 1.00 91.44 ? 339 ASP A CA 1 ATOM 2035 C C . ASP A 1 251 ? 1.409 37.866 43.191 1.00 85.42 ? 339 ASP A C 1 ATOM 2036 O O . ASP A 1 251 ? 2.552 38.023 42.757 1.00 83.27 ? 339 ASP A O 1 ATOM 2037 C CB . ASP A 1 251 ? 1.744 36.114 44.952 1.00 83.89 ? 339 ASP A CB 1 ATOM 2038 C CG . ASP A 1 251 ? 1.326 34.757 45.471 1.00 90.73 ? 339 ASP A CG 1 ATOM 2039 O OD1 . ASP A 1 251 ? 0.136 34.421 45.297 1.00 91.40 ? 339 ASP A OD1 1 ATOM 2040 O OD2 . ASP A 1 251 ? 2.176 34.031 46.040 1.00 95.91 ? 339 ASP A OD2 1 ATOM 2041 N N . ILE A 1 252 ? 0.491 38.826 43.203 1.00 77.15 ? 340 ILE A N 1 ATOM 2042 C CA . ILE A 1 252 ? 0.804 40.147 42.691 1.00 71.69 ? 340 ILE A CA 1 ATOM 2043 C C . ILE A 1 252 ? 0.627 41.221 43.786 1.00 71.77 ? 340 ILE A C 1 ATOM 2044 O O . ILE A 1 252 ? -0.431 41.364 44.409 1.00 79.55 ? 340 ILE A O 1 ATOM 2045 C CB . ILE A 1 252 ? 0.032 40.443 41.383 1.00 68.48 ? 340 ILE A CB 1 ATOM 2046 C CG1 . ILE A 1 252 ? -1.409 40.795 41.683 1.00 74.10 ? 340 ILE A CG1 1 ATOM 2047 C CG2 . ILE A 1 252 ? 0.010 39.197 40.474 1.00 61.33 ? 340 ILE A CG2 1 ATOM 2048 C CD1 . ILE A 1 252 ? -1.889 41.934 40.928 1.00 59.04 ? 340 ILE A CD1 1 ATOM 2049 N N . TYR A 1 253 ? 1.695 41.979 43.997 1.00 66.05 ? 341 TYR A N 1 ATOM 2050 C CA . TYR A 1 253 ? 1.837 42.866 45.128 1.00 70.02 ? 341 TYR A CA 1 ATOM 2051 C C . TYR A 1 253 ? 1.726 44.339 44.757 1.00 68.75 ? 341 TYR A C 1 ATOM 2052 O O . TYR A 1 253 ? 2.261 44.778 43.739 1.00 66.23 ? 341 TYR A O 1 ATOM 2053 C CB . TYR A 1 253 ? 3.181 42.577 45.782 1.00 76.63 ? 341 TYR A CB 1 ATOM 2054 C CG . TYR A 1 253 ? 3.288 41.151 46.287 1.00 82.74 ? 341 TYR A CG 1 ATOM 2055 C CD1 . TYR A 1 253 ? 3.670 40.111 45.441 1.00 83.74 ? 341 TYR A CD1 1 ATOM 2056 C CD2 . TYR A 1 253 ? 2.995 40.839 47.616 1.00 82.68 ? 341 TYR A CD2 1 ATOM 2057 C CE1 . TYR A 1 253 ? 3.759 38.800 45.906 1.00 85.77 ? 341 TYR A CE1 1 ATOM 2058 C CE2 . TYR A 1 253 ? 3.088 39.540 48.093 1.00 82.30 ? 341 TYR A CE2 1 ATOM 2059 C CZ . TYR A 1 253 ? 3.468 38.520 47.245 1.00 93.53 ? 341 TYR A CZ 1 ATOM 2060 O OH . TYR A 1 253 ? 3.552 37.228 47.735 1.00 89.59 ? 341 TYR A OH 1 ATOM 2061 N N . GLU A 1 254 ? 1.017 45.084 45.602 1.00 69.83 ? 342 GLU A N 1 ATOM 2062 C CA . GLU A 1 254 ? 0.727 46.512 45.424 1.00 64.47 ? 342 GLU A CA 1 ATOM 2063 C C . GLU A 1 254 ? 0.319 46.934 44.013 1.00 58.05 ? 342 GLU A C 1 ATOM 2064 O O . GLU A 1 254 ? 0.613 48.044 43.568 1.00 53.80 ? 342 GLU A O 1 ATOM 2065 C CB . GLU A 1 254 ? 1.862 47.381 45.958 1.00 65.31 ? 342 GLU A CB 1 ATOM 2066 C CG . GLU A 1 254 ? 2.247 47.065 47.413 1.00 76.03 ? 342 GLU A CG 1 ATOM 2067 C CD . GLU A 1 254 ? 1.236 47.560 48.467 1.00 71.84 ? 342 GLU A CD 1 ATOM 2068 O OE1 . GLU A 1 254 ? 0.316 48.335 48.139 1.00 69.82 ? 342 GLU A OE1 1 ATOM 2069 O OE2 . GLU A 1 254 ? 1.374 47.167 49.641 1.00 72.01 ? 342 GLU A OE2 1 ATOM 2070 N N . PHE A 1 255 ? -0.373 46.049 43.309 1.00 53.71 ? 343 PHE A N 1 ATOM 2071 C CA . PHE A 1 255 ? -1.056 46.466 42.086 1.00 52.10 ? 343 PHE A CA 1 ATOM 2072 C C . PHE A 1 255 ? -2.388 46.965 42.639 1.00 56.33 ? 343 PHE A C 1 ATOM 2073 O O . PHE A 1 255 ? -2.657 48.171 42.652 1.00 55.75 ? 343 PHE A O 1 ATOM 2074 C CB . PHE A 1 255 ? -1.247 45.274 41.162 1.00 48.03 ? 343 PHE A CB 1 ATOM 2075 C CG . PHE A 1 255 ? -1.724 45.637 39.796 1.00 52.10 ? 343 PHE A CG 1 ATOM 2076 C CD1 . PHE A 1 255 ? -0.961 46.456 38.984 1.00 50.81 ? 343 PHE A CD1 1 ATOM 2077 C CD2 . PHE A 1 255 ? -2.927 45.149 39.316 1.00 48.07 ? 343 PHE A CD2 1 ATOM 2078 C CE1 . PHE A 1 255 ? -1.385 46.796 37.701 1.00 57.15 ? 343 PHE A CE1 1 ATOM 2079 C CE2 . PHE A 1 255 ? -3.371 45.487 38.043 1.00 55.48 ? 343 PHE A CE2 1 ATOM 2080 C CZ . PHE A 1 255 ? -2.588 46.303 37.221 1.00 51.76 ? 343 PHE A CZ 1 ATOM 2081 N N . LEU A 1 256 ? -3.196 46.038 43.154 1.00 54.20 ? 344 LEU A N 1 ATOM 2082 C CA . LEU A 1 256 ? -4.285 46.442 44.041 1.00 62.82 ? 344 LEU A CA 1 ATOM 2083 C C . LEU A 1 256 ? -3.611 46.971 45.293 1.00 54.71 ? 344 LEU A C 1 ATOM 2084 O O . LEU A 1 256 ? -2.813 46.265 45.909 1.00 57.41 ? 344 LEU A O 1 ATOM 2085 C CB . LEU A 1 256 ? -5.206 45.277 44.396 1.00 59.40 ? 344 LEU A CB 1 ATOM 2086 C CG . LEU A 1 256 ? -5.815 44.507 43.226 1.00 60.37 ? 344 LEU A CG 1 ATOM 2087 C CD1 . LEU A 1 256 ? -6.941 43.626 43.714 1.00 66.07 ? 344 LEU A CD1 1 ATOM 2088 C CD2 . LEU A 1 256 ? -6.277 45.446 42.125 1.00 60.75 ? 344 LEU A CD2 1 ATOM 2089 N N . PRO A 1 257 ? -3.900 48.228 45.650 1.00 56.84 ? 345 PRO A N 1 ATOM 2090 C CA . PRO A 1 257 ? -3.177 48.893 46.733 1.00 71.01 ? 345 PRO A CA 1 ATOM 2091 C C . PRO A 1 257 ? -3.581 48.369 48.097 1.00 69.97 ? 345 PRO A C 1 ATOM 2092 O O . PRO A 1 257 ? -4.726 47.972 48.292 1.00 65.60 ? 345 PRO A O 1 ATOM 2093 C CB . PRO A 1 257 ? -3.578 50.368 46.583 1.00 71.06 ? 345 PRO A CB 1 ATOM 2094 C CG . PRO A 1 257 ? -4.842 50.360 45.836 1.00 65.24 ? 345 PRO A CG 1 ATOM 2095 C CD . PRO A 1 257 ? -4.827 49.140 44.959 1.00 56.22 ? 345 PRO A CD 1 ATOM 2096 N N . SER A 1 258 ? -2.623 48.348 49.015 1.00 61.50 ? 346 SER A N 1 ATOM 2097 C CA . SER A 1 258 ? -2.887 47.990 50.390 1.00 66.12 ? 346 SER A CA 1 ATOM 2098 C C . SER A 1 258 ? -3.275 49.241 51.150 1.00 66.87 ? 346 SER A C 1 ATOM 2099 O O . SER A 1 258 ? -3.628 50.258 50.551 1.00 63.13 ? 346 SER A O 1 ATOM 2100 C CB . SER A 1 258 ? -1.643 47.350 51.024 1.00 73.56 ? 346 SER A CB 1 ATOM 2101 O OG . SER A 1 258 ? -0.536 48.244 51.081 1.00 67.81 ? 346 SER A OG 1 ATOM 2102 N N . LYS A 1 259 ? -3.178 49.163 52.473 1.00 70.46 ? 347 LYS A N 1 ATOM 2103 C CA . LYS A 1 259 ? -3.472 50.288 53.347 1.00 75.79 ? 347 LYS A CA 1 ATOM 2104 C C . LYS A 1 259 ? -2.371 51.311 53.235 1.00 73.97 ? 347 LYS A C 1 ATOM 2105 O O . LYS A 1 259 ? -2.511 52.431 53.701 1.00 75.91 ? 347 LYS A O 1 ATOM 2106 C CB . LYS A 1 259 ? -3.594 49.829 54.801 1.00 77.02 ? 347 LYS A CB 1 ATOM 2107 C CG . LYS A 1 259 ? -2.412 49.025 55.301 1.00 80.06 ? 347 LYS A CG 1 ATOM 2108 C CD . LYS A 1 259 ? -2.345 48.997 56.832 1.00 88.84 ? 347 LYS A CD 1 ATOM 2109 C CE . LYS A 1 259 ? -1.378 47.918 57.307 1.00 94.96 ? 347 LYS A CE 1 ATOM 2110 N NZ . LYS A 1 259 ? -0.257 47.721 56.333 1.00 87.76 ? 347 LYS A NZ 1 ATOM 2111 N N . ARG A 1 260 ? -1.269 50.922 52.605 1.00 73.00 ? 348 ARG A N 1 ATOM 2112 C CA . ARG A 1 260 ? -0.169 51.851 52.395 1.00 76.97 ? 348 ARG A CA 1 ATOM 2113 C C . ARG A 1 260 ? -0.336 52.695 51.125 1.00 72.56 ? 348 ARG A C 1 ATOM 2114 O O . ARG A 1 260 ? 0.578 53.438 50.761 1.00 65.69 ? 348 ARG A O 1 ATOM 2115 C CB . ARG A 1 260 ? 1.160 51.106 52.372 1.00 68.33 ? 348 ARG A CB 1 ATOM 2116 C CG . ARG A 1 260 ? 1.492 50.437 53.675 1.00 73.71 ? 348 ARG A CG 1 ATOM 2117 C CD . ARG A 1 260 ? 2.773 49.660 53.577 1.00 75.72 ? 348 ARG A CD 1 ATOM 2118 N NE . ARG A 1 260 ? 2.682 48.599 52.572 1.00 87.50 ? 348 ARG A NE 1 ATOM 2119 C CZ . ARG A 1 260 ? 2.200 47.386 52.818 1.00 88.10 ? 348 ARG A CZ 1 ATOM 2120 N NH1 . ARG A 1 260 ? 2.152 46.485 51.858 1.00 82.04 ? 348 ARG A NH1 1 ATOM 2121 N NH2 . ARG A 1 260 ? 1.773 47.077 54.034 1.00 97.78 ? 348 ARG A NH2 1 ATOM 2122 N N . LYS A 1 261 ? -1.499 52.571 50.476 1.00 60.03 ? 349 LYS A N 1 ATOM 2123 C CA . LYS A 1 261 ? -1.880 53.404 49.335 1.00 62.86 ? 349 LYS A CA 1 ATOM 2124 C C . LYS A 1 261 ? -1.348 54.819 49.490 1.00 63.96 ? 349 LYS A C 1 ATOM 2125 O O . LYS A 1 261 ? -1.597 55.460 50.499 1.00 65.75 ? 349 LYS A O 1 ATOM 2126 C CB . LYS A 1 261 ? -3.404 53.484 49.206 1.00 62.00 ? 349 LYS A CB 1 ATOM 2127 C CG . LYS A 1 261 ? -3.861 54.110 47.859 1.00 77.04 ? 349 LYS A CG 1 ATOM 2128 C CD . LYS A 1 261 ? -5.351 53.938 47.644 1.00 75.73 ? 349 LYS A CD 1 ATOM 2129 C CE . LYS A 1 261 ? -5.804 54.555 46.352 1.00 84.63 ? 349 LYS A CE 1 ATOM 2130 N NZ . LYS A 1 261 ? -7.140 54.015 45.989 1.00 93.22 ? 349 LYS A NZ 1 ATOM 2131 N N . THR A 1 262 ? -0.583 55.298 48.518 1.00 53.57 ? 350 THR A N 1 ATOM 2132 C CA . THR A 1 262 ? -0.004 56.626 48.676 1.00 66.62 ? 350 THR A CA 1 ATOM 2133 C C . THR A 1 262 ? 0.148 57.342 47.345 1.00 62.23 ? 350 THR A C 1 ATOM 2134 O O . THR A 1 262 ? 0.167 56.714 46.289 1.00 58.30 ? 350 THR A O 1 ATOM 2135 C CB . THR A 1 262 ? 1.351 56.576 49.418 1.00 56.64 ? 350 THR A CB 1 ATOM 2136 O OG1 . THR A 1 262 ? 2.007 57.845 49.312 1.00 62.69 ? 350 THR A OG1 1 ATOM 2137 C CG2 . THR A 1 262 ? 2.242 55.510 48.836 1.00 56.02 ? 350 THR A CG2 1 ATOM 2138 N N . ASP A 1 263 ? 0.246 58.663 47.382 1.00 60.18 ? 351 ASP A N 1 ATOM 2139 C CA . ASP A 1 263 ? 0.466 59.387 46.136 1.00 53.96 ? 351 ASP A CA 1 ATOM 2140 C C . ASP A 1 263 ? 1.863 59.161 45.581 1.00 55.98 ? 351 ASP A C 1 ATOM 2141 O O . ASP A 1 263 ? 2.055 59.223 44.363 1.00 54.84 ? 351 ASP A O 1 ATOM 2142 C CB . ASP A 1 263 ? 0.172 60.869 46.306 1.00 55.24 ? 351 ASP A CB 1 ATOM 2143 C CG . ASP A 1 263 ? -1.316 61.159 46.351 1.00 58.79 ? 351 ASP A CG 1 ATOM 2144 O OD1 . ASP A 1 263 ? -2.132 60.244 46.091 1.00 61.51 ? 351 ASP A OD1 1 ATOM 2145 O OD2 . ASP A 1 263 ? -1.668 62.314 46.628 1.00 61.84 ? 351 ASP A OD2 1 ATOM 2146 N N . VAL A 1 264 ? 2.835 58.890 46.451 1.00 58.84 ? 352 VAL A N 1 ATOM 2147 C CA . VAL A 1 264 ? 4.195 58.590 45.983 1.00 61.92 ? 352 VAL A CA 1 ATOM 2148 C C . VAL A 1 264 ? 4.168 57.560 44.878 1.00 56.21 ? 352 VAL A C 1 ATOM 2149 O O . VAL A 1 264 ? 3.849 56.388 45.097 1.00 62.19 ? 352 VAL A O 1 ATOM 2150 C CB . VAL A 1 264 ? 5.099 58.039 47.077 1.00 69.72 ? 352 VAL A CB 1 ATOM 2151 C CG1 . VAL A 1 264 ? 6.537 57.948 46.554 1.00 56.66 ? 352 VAL A CG1 1 ATOM 2152 C CG2 . VAL A 1 264 ? 4.989 58.892 48.343 1.00 58.73 ? 352 VAL A CG2 1 ATOM 2153 N N . CYS A 1 265 ? 4.505 58.006 43.674 1.00 53.52 ? 353 CYS A N 1 ATOM 2154 C CA . CYS A 1 265 ? 4.313 57.196 42.487 1.00 45.05 ? 353 CYS A CA 1 ATOM 2155 C C . CYS A 1 265 ? 5.105 55.881 42.498 1.00 51.04 ? 353 CYS A C 1 ATOM 2156 O O . CYS A 1 265 ? 4.562 54.814 42.170 1.00 50.89 ? 353 CYS A O 1 ATOM 2157 C CB . CYS A 1 265 ? 4.637 58.023 41.234 1.00 44.01 ? 353 CYS A CB 1 ATOM 2158 S SG . CYS A 1 265 ? 4.583 57.019 39.739 1.00 67.98 ? 353 CYS A SG 1 ATOM 2159 N N . TYR A 1 266 ? 6.384 55.950 42.858 1.00 53.35 ? 354 TYR A N 1 ATOM 2160 C CA . TYR A 1 266 ? 7.246 54.756 42.850 1.00 57.53 ? 354 TYR A CA 1 ATOM 2161 C C . TYR A 1 266 ? 7.991 54.588 44.182 1.00 64.26 ? 354 TYR A C 1 ATOM 2162 O O . TYR A 1 266 ? 8.207 55.565 44.905 1.00 64.53 ? 354 TYR A O 1 ATOM 2163 C CB . TYR A 1 266 ? 8.287 54.841 41.741 1.00 56.64 ? 354 TYR A CB 1 ATOM 2164 C CG . TYR A 1 266 ? 7.760 54.853 40.330 1.00 60.04 ? 354 TYR A CG 1 ATOM 2165 C CD1 . TYR A 1 266 ? 6.952 53.830 39.851 1.00 60.95 ? 354 TYR A CD1 1 ATOM 2166 C CD2 . TYR A 1 266 ? 8.107 55.875 39.457 1.00 65.40 ? 354 TYR A CD2 1 ATOM 2167 C CE1 . TYR A 1 266 ? 6.484 53.842 38.536 1.00 62.41 ? 354 TYR A CE1 1 ATOM 2168 C CE2 . TYR A 1 266 ? 7.650 55.897 38.152 1.00 64.25 ? 354 TYR A CE2 1 ATOM 2169 C CZ . TYR A 1 266 ? 6.843 54.876 37.695 1.00 67.08 ? 354 TYR A CZ 1 ATOM 2170 O OH . TYR A 1 266 ? 6.387 54.901 36.394 1.00 74.35 ? 354 TYR A OH 1 ATOM 2171 N N . TYR A 1 267 ? 8.406 53.362 44.498 1.00 64.89 ? 355 TYR A N 1 ATOM 2172 C CA . TYR A 1 267 ? 9.147 53.128 45.741 1.00 65.88 ? 355 TYR A CA 1 ATOM 2173 C C . TYR A 1 267 ? 10.582 53.632 45.638 1.00 66.98 ? 355 TYR A C 1 ATOM 2174 O O . TYR A 1 267 ? 11.228 53.882 46.641 1.00 76.67 ? 355 TYR A O 1 ATOM 2175 C CB . TYR A 1 267 ? 9.148 51.643 46.128 1.00 70.21 ? 355 TYR A CB 1 ATOM 2176 C CG . TYR A 1 267 ? 9.977 50.721 45.233 1.00 68.67 ? 355 TYR A CG 1 ATOM 2177 C CD1 . TYR A 1 267 ? 11.327 50.483 45.494 1.00 68.13 ? 355 TYR A CD1 1 ATOM 2178 C CD2 . TYR A 1 267 ? 9.399 50.057 44.177 1.00 63.40 ? 355 TYR A CD2 1 ATOM 2179 C CE1 . TYR A 1 267 ? 12.073 49.631 44.701 1.00 67.53 ? 355 TYR A CE1 1 ATOM 2180 C CE2 . TYR A 1 267 ? 10.136 49.197 43.366 1.00 65.75 ? 355 TYR A CE2 1 ATOM 2181 C CZ . TYR A 1 267 ? 11.472 48.988 43.638 1.00 74.02 ? 355 TYR A CZ 1 ATOM 2182 O OH . TYR A 1 267 ? 12.204 48.143 42.834 1.00 77.13 ? 355 TYR A OH 1 ATOM 2183 N N . TYR A 1 268 ? 11.078 53.757 44.411 1.00 69.95 ? 356 TYR A N 1 ATOM 2184 C CA . TYR A 1 268 ? 12.458 54.164 44.196 1.00 70.02 ? 356 TYR A CA 1 ATOM 2185 C C . TYR A 1 268 ? 12.574 55.609 43.736 1.00 71.90 ? 356 TYR A C 1 ATOM 2186 O O . TYR A 1 268 ? 13.678 56.126 43.572 1.00 75.86 ? 356 TYR A O 1 ATOM 2187 C CB . TYR A 1 268 ? 13.149 53.226 43.204 1.00 71.14 ? 356 TYR A CB 1 ATOM 2188 C CG . TYR A 1 268 ? 12.439 53.028 41.869 1.00 73.97 ? 356 TYR A CG 1 ATOM 2189 C CD1 . TYR A 1 268 ? 11.402 52.114 41.737 1.00 72.00 ? 356 TYR A CD1 1 ATOM 2190 C CD2 . TYR A 1 268 ? 12.846 53.719 40.732 1.00 72.82 ? 356 TYR A CD2 1 ATOM 2191 C CE1 . TYR A 1 268 ? 10.764 51.920 40.522 1.00 69.23 ? 356 TYR A CE1 1 ATOM 2192 C CE2 . TYR A 1 268 ? 12.216 53.535 39.521 1.00 74.53 ? 356 TYR A CE2 1 ATOM 2193 C CZ . TYR A 1 268 ? 11.176 52.633 39.416 1.00 73.79 ? 356 TYR A CZ 1 ATOM 2194 O OH . TYR A 1 268 ? 10.553 52.446 38.191 1.00 72.74 ? 356 TYR A OH 1 ATOM 2195 N N . GLN A 1 269 ? 11.429 56.252 43.522 1.00 72.63 ? 357 GLN A N 1 ATOM 2196 C CA . GLN A 1 269 ? 11.392 57.663 43.169 1.00 75.35 ? 357 GLN A CA 1 ATOM 2197 C C . GLN A 1 269 ? 10.742 58.431 44.313 1.00 78.02 ? 357 GLN A C 1 ATOM 2198 O O . GLN A 1 269 ? 10.096 57.842 45.182 1.00 76.08 ? 357 GLN A O 1 ATOM 2199 C CB . GLN A 1 269 ? 10.623 57.875 41.864 1.00 81.92 ? 357 GLN A CB 1 ATOM 2200 C CG . GLN A 1 269 ? 11.408 58.606 40.759 1.00 85.55 ? 357 GLN A CG 1 ATOM 2201 C CD . GLN A 1 269 ? 11.804 57.718 39.579 1.00 86.38 ? 357 GLN A CD 1 ATOM 2202 O OE1 . GLN A 1 269 ? 12.870 57.101 39.582 1.00 91.89 ? 357 GLN A OE1 1 ATOM 2203 N NE2 . GLN A 1 269 ? 10.949 57.661 38.561 1.00 81.83 ? 357 GLN A NE2 1 ATOM 2204 N N . LYS A 1 270 ? 10.908 59.747 44.318 1.00 77.33 ? 358 LYS A N 1 ATOM 2205 C CA . LYS A 1 270 ? 10.425 60.540 45.431 1.00 81.31 ? 358 LYS A CA 1 ATOM 2206 C C . LYS A 1 270 ? 9.213 61.403 45.094 1.00 76.96 ? 358 LYS A C 1 ATOM 2207 O O . LYS A 1 270 ? 8.684 62.089 45.962 1.00 88.53 ? 358 LYS A O 1 ATOM 2208 C CB . LYS A 1 270 ? 11.552 61.414 45.981 1.00 95.10 ? 358 LYS A CB 1 ATOM 2209 C CG . LYS A 1 270 ? 12.655 60.650 46.700 1.00 104.70 ? 358 LYS A CG 1 ATOM 2210 C CD . LYS A 1 270 ? 13.614 61.625 47.366 1.00 114.19 ? 358 LYS A CD 1 ATOM 2211 C CE . LYS A 1 270 ? 14.699 60.917 48.163 1.00 119.52 ? 358 LYS A CE 1 ATOM 2212 N NZ . LYS A 1 270 ? 15.551 61.900 48.894 1.00 124.39 ? 358 LYS A NZ 1 ATOM 2213 N N . PHE A 1 271 ? 8.764 61.357 43.845 1.00 73.52 ? 359 PHE A N 1 ATOM 2214 C CA . PHE A 1 271 ? 7.744 62.297 43.377 1.00 70.13 ? 359 PHE A CA 1 ATOM 2215 C C . PHE A 1 271 ? 6.328 61.771 43.551 1.00 62.89 ? 359 PHE A C 1 ATOM 2216 O O . PHE A 1 271 ? 6.102 60.571 43.489 1.00 58.44 ? 359 PHE A O 1 ATOM 2217 C CB . PHE A 1 271 ? 8.009 62.743 41.923 1.00 69.65 ? 359 PHE A CB 1 ATOM 2218 C CG . PHE A 1 271 ? 7.629 61.742 40.878 1.00 65.40 ? 359 PHE A CG 1 ATOM 2219 C CD1 . PHE A 1 271 ? 6.347 61.716 40.358 1.00 66.24 ? 359 PHE A CD1 1 ATOM 2220 C CD2 . PHE A 1 271 ? 8.561 60.864 40.365 1.00 62.31 ? 359 PHE A CD2 1 ATOM 2221 C CE1 . PHE A 1 271 ? 5.995 60.805 39.376 1.00 58.72 ? 359 PHE A CE1 1 ATOM 2222 C CE2 . PHE A 1 271 ? 8.211 59.960 39.367 1.00 56.09 ? 359 PHE A CE2 1 ATOM 2223 C CZ . PHE A 1 271 ? 6.928 59.932 38.877 1.00 51.33 ? 359 PHE A CZ 1 ATOM 2224 N N . PHE A 1 272 ? 5.380 62.679 43.772 1.00 65.42 ? 360 PHE A N 1 ATOM 2225 C CA . PHE A 1 272 ? 3.994 62.302 44.046 1.00 61.53 ? 360 PHE A CA 1 ATOM 2226 C C . PHE A 1 272 ? 3.159 62.318 42.779 1.00 59.11 ? 360 PHE A C 1 ATOM 2227 O O . PHE A 1 272 ? 3.254 63.258 42.005 1.00 62.91 ? 360 PHE A O 1 ATOM 2228 C CB . PHE A 1 272 ? 3.353 63.288 45.028 1.00 61.84 ? 360 PHE A CB 1 ATOM 2229 C CG . PHE A 1 272 ? 3.994 63.326 46.379 1.00 71.33 ? 360 PHE A CG 1 ATOM 2230 C CD1 . PHE A 1 272 ? 5.118 64.109 46.612 1.00 80.94 ? 360 PHE A CD1 1 ATOM 2231 C CD2 . PHE A 1 272 ? 3.439 62.627 47.436 1.00 79.85 ? 360 PHE A CD2 1 ATOM 2232 C CE1 . PHE A 1 272 ? 5.690 64.170 47.872 1.00 86.79 ? 360 PHE A CE1 1 ATOM 2233 C CE2 . PHE A 1 272 ? 4.004 62.686 48.698 1.00 82.23 ? 360 PHE A CE2 1 ATOM 2234 C CZ . PHE A 1 272 ? 5.133 63.453 48.912 1.00 85.30 ? 360 PHE A CZ 1 ATOM 2235 N N . ASP A 1 273 ? 2.342 61.282 42.571 1.00 54.63 ? 361 ASP A N 1 ATOM 2236 C CA . ASP A 1 273 ? 1.347 61.277 41.504 1.00 47.07 ? 361 ASP A CA 1 ATOM 2237 C C . ASP A 1 273 ? 0.269 60.184 41.683 1.00 48.67 ? 361 ASP A C 1 ATOM 2238 O O . ASP A 1 273 ? 0.544 58.997 41.567 1.00 51.13 ? 361 ASP A O 1 ATOM 2239 C CB . ASP A 1 273 ? 2.011 61.129 40.132 1.00 49.68 ? 361 ASP A CB 1 ATOM 2240 C CG . ASP A 1 273 ? 1.106 61.589 39.010 1.00 59.88 ? 361 ASP A CG 1 ATOM 2241 O OD1 . ASP A 1 273 ? -0.103 61.781 39.278 1.00 57.36 ? 361 ASP A OD1 1 ATOM 2242 O OD2 . ASP A 1 273 ? 1.586 61.757 37.868 1.00 77.14 ? 361 ASP A OD2 1 ATOM 2243 N N . SER A 1 274 ? -0.960 60.599 41.959 1.00 58.17 ? 362 SER A N 1 ATOM 2244 C CA . SER A 1 274 ? -2.061 59.666 42.159 1.00 58.25 ? 362 SER A CA 1 ATOM 2245 C C . SER A 1 274 ? -2.317 58.841 40.889 1.00 58.11 ? 362 SER A C 1 ATOM 2246 O O . SER A 1 274 ? -2.736 57.678 40.949 1.00 58.58 ? 362 SER A O 1 ATOM 2247 C CB . SER A 1 274 ? -3.312 60.450 42.563 1.00 62.32 ? 362 SER A CB 1 ATOM 2248 O OG . SER A 1 274 ? -4.339 59.603 43.049 1.00 75.09 ? 362 SER A OG 1 ATOM 2249 N N . ALA A 1 275 ? -2.039 59.446 39.742 1.00 55.04 ? 363 ALA A N 1 ATOM 2250 C CA . ALA A 1 275 ? -2.256 58.809 38.448 1.00 46.81 ? 363 ALA A CA 1 ATOM 2251 C C . ALA A 1 275 ? -1.489 57.512 38.287 1.00 50.26 ? 363 ALA A C 1 ATOM 2252 O O . ALA A 1 275 ? -1.934 56.629 37.566 1.00 51.22 ? 363 ALA A O 1 ATOM 2253 C CB . ALA A 1 275 ? -1.885 59.778 37.312 1.00 51.27 ? 363 ALA A CB 1 ATOM 2254 N N . CYS A 1 276 ? -0.344 57.380 38.954 1.00 54.61 ? 364 CYS A N 1 ATOM 2255 C CA . CYS A 1 276 ? 0.402 56.115 38.894 1.00 53.54 ? 364 CYS A CA 1 ATOM 2256 C C . CYS A 1 276 ? -0.367 54.955 39.499 1.00 50.23 ? 364 CYS A C 1 ATOM 2257 O O . CYS A 1 276 ? -0.198 53.822 39.075 1.00 46.44 ? 364 CYS A O 1 ATOM 2258 C CB . CYS A 1 276 ? 1.752 56.233 39.594 1.00 51.94 ? 364 CYS A CB 1 ATOM 2259 S SG . CYS A 1 276 ? 2.813 57.457 38.818 1.00 63.78 ? 364 CYS A SG 1 ATOM 2260 N N . THR A 1 277 ? -1.184 55.235 40.514 1.00 55.30 ? 365 THR A N 1 ATOM 2261 C CA . THR A 1 277 ? -1.976 54.195 41.171 1.00 39.23 ? 365 THR A CA 1 ATOM 2262 C C . THR A 1 277 ? -3.331 54.020 40.463 1.00 51.48 ? 365 THR A C 1 ATOM 2263 O O . THR A 1 277 ? -3.804 52.899 40.272 1.00 52.03 ? 365 THR A O 1 ATOM 2264 C CB . THR A 1 277 ? -2.184 54.508 42.672 1.00 49.06 ? 365 THR A CB 1 ATOM 2265 O OG1 . THR A 1 277 ? -0.913 54.723 43.293 1.00 47.64 ? 365 THR A OG1 1 ATOM 2266 C CG2 . THR A 1 277 ? -2.867 53.340 43.384 1.00 44.85 ? 365 THR A CG2 1 ATOM 2267 N N . MET A 1 278 ? -3.934 55.126 40.038 1.00 52.43 ? 366 MET A N 1 ATOM 2268 C CA . MET A 1 278 ? -5.303 55.104 39.513 1.00 49.12 ? 366 MET A CA 1 ATOM 2269 C C . MET A 1 278 ? -5.400 55.114 37.971 1.00 50.27 ? 366 MET A C 1 ATOM 2270 O O . MET A 1 278 ? -6.416 54.701 37.396 1.00 50.54 ? 366 MET A O 1 ATOM 2271 C CB . MET A 1 278 ? -6.092 56.283 40.112 1.00 45.24 ? 366 MET A CB 1 ATOM 2272 C CG . MET A 1 278 ? -6.039 56.330 41.625 1.00 61.28 ? 366 MET A CG 1 ATOM 2273 S SD . MET A 1 278 ? -6.733 54.857 42.392 1.00 63.78 ? 366 MET A SD 1 ATOM 2274 C CE . MET A 1 278 ? -8.473 55.234 42.248 1.00 77.10 ? 366 MET A CE 1 ATOM 2275 N N . GLY A 1 279 ? -4.347 55.563 37.304 1.00 46.51 ? 367 GLY A N 1 ATOM 2276 C CA . GLY A 1 279 ? -4.326 55.556 35.847 1.00 53.11 ? 367 GLY A CA 1 ATOM 2277 C C . GLY A 1 279 ? -4.445 56.941 35.247 1.00 54.55 ? 367 GLY A C 1 ATOM 2278 O O . GLY A 1 279 ? -5.159 57.799 35.774 1.00 57.76 ? 367 GLY A O 1 ATOM 2279 N N . ALA A 1 280 ? -3.716 57.166 34.159 1.00 41.77 ? 368 ALA A N 1 ATOM 2280 C CA . ALA A 1 280 ? -3.832 58.375 33.357 1.00 44.42 ? 368 ALA A CA 1 ATOM 2281 C C . ALA A 1 280 ? -3.744 57.949 31.883 1.00 42.99 ? 368 ALA A C 1 ATOM 2282 O O . ALA A 1 280 ? -4.759 57.781 31.231 1.00 50.37 ? 368 ALA A O 1 ATOM 2283 C CB . ALA A 1 280 ? -2.744 59.357 33.702 1.00 44.51 ? 368 ALA A CB 1 ATOM 2284 N N . TYR A 1 281 ? -2.530 57.698 31.402 1.00 44.28 ? 369 TYR A N 1 ATOM 2285 C CA . TYR A 1 281 ? -2.318 57.091 30.093 1.00 38.89 ? 369 TYR A CA 1 ATOM 2286 C C . TYR A 1 281 ? -2.899 55.683 30.019 1.00 44.58 ? 369 TYR A C 1 ATOM 2287 O O . TYR A 1 281 ? -3.686 55.403 29.113 1.00 50.58 ? 369 TYR A O 1 ATOM 2288 C CB . TYR A 1 281 ? -0.825 57.132 29.699 1.00 37.92 ? 369 TYR A CB 1 ATOM 2289 C CG . TYR A 1 281 ? -0.421 56.393 28.410 1.00 39.51 ? 369 TYR A CG 1 ATOM 2290 C CD1 . TYR A 1 281 ? -0.092 55.042 28.448 1.00 38.26 ? 369 TYR A CD1 1 ATOM 2291 C CD2 . TYR A 1 281 ? -0.332 57.048 27.178 1.00 46.02 ? 369 TYR A CD2 1 ATOM 2292 C CE1 . TYR A 1 281 ? 0.288 54.348 27.323 1.00 46.35 ? 369 TYR A CE1 1 ATOM 2293 C CE2 . TYR A 1 281 ? 0.081 56.340 26.006 1.00 38.04 ? 369 TYR A CE2 1 ATOM 2294 C CZ . TYR A 1 281 ? 0.377 54.987 26.113 1.00 40.86 ? 369 TYR A CZ 1 ATOM 2295 O OH . TYR A 1 281 ? 0.749 54.222 25.026 1.00 47.87 ? 369 TYR A OH 1 ATOM 2296 N N . HIS A 1 282 ? -2.542 54.788 30.947 1.00 38.07 ? 370 HIS A N 1 ATOM 2297 C CA . HIS A 1 282 ? -3.073 53.426 30.857 1.00 32.56 ? 370 HIS A CA 1 ATOM 2298 C C . HIS A 1 282 ? -4.460 53.325 31.442 1.00 41.84 ? 370 HIS A C 1 ATOM 2299 O O . HIS A 1 282 ? -4.834 54.113 32.316 1.00 50.32 ? 370 HIS A O 1 ATOM 2300 C CB . HIS A 1 282 ? -2.157 52.378 31.516 1.00 35.55 ? 370 HIS A CB 1 ATOM 2301 C CG . HIS A 1 282 ? -0.757 52.365 30.987 1.00 44.48 ? 370 HIS A CG 1 ATOM 2302 N ND1 . HIS A 1 282 ? -0.424 51.819 29.765 1.00 46.69 ? 370 HIS A ND1 1 ATOM 2303 C CD2 . HIS A 1 282 ? 0.401 52.815 31.524 1.00 43.82 ? 370 HIS A CD2 1 ATOM 2304 C CE1 . HIS A 1 282 ? 0.879 51.931 29.577 1.00 42.51 ? 370 HIS A CE1 1 ATOM 2305 N NE2 . HIS A 1 282 ? 1.400 52.547 30.622 1.00 46.71 ? 370 HIS A NE2 1 ATOM 2306 N N . PRO A 1 283 ? -5.233 52.337 30.979 1.00 40.81 ? 371 PRO A N 1 ATOM 2307 C CA . PRO A 1 283 ? -6.522 52.038 31.598 1.00 45.54 ? 371 PRO A CA 1 ATOM 2308 C C . PRO A 1 283 ? -6.344 51.232 32.902 1.00 46.81 ? 371 PRO A C 1 ATOM 2309 O O . PRO A 1 283 ? -7.022 50.231 33.157 1.00 47.00 ? 371 PRO A O 1 ATOM 2310 C CB . PRO A 1 283 ? -7.213 51.201 30.524 1.00 40.05 ? 371 PRO A CB 1 ATOM 2311 C CG . PRO A 1 283 ? -6.098 50.495 29.867 1.00 43.68 ? 371 PRO A CG 1 ATOM 2312 C CD . PRO A 1 283 ? -5.025 51.544 29.749 1.00 41.39 ? 371 PRO A CD 1 ATOM 2313 N N . LEU A 1 284 ? -5.410 51.699 33.721 1.00 51.61 ? 372 LEU A N 1 ATOM 2314 C CA . LEU A 1 284 ? -4.998 51.054 34.953 1.00 54.56 ? 372 LEU A CA 1 ATOM 2315 C C . LEU A 1 284 ? -6.168 50.789 35.872 1.00 45.57 ? 372 LEU A C 1 ATOM 2316 O O . LEU A 1 284 ? -6.221 49.777 36.564 1.00 51.68 ? 372 LEU A O 1 ATOM 2317 C CB . LEU A 1 284 ? -4.005 51.964 35.654 1.00 54.65 ? 372 LEU A CB 1 ATOM 2318 C CG . LEU A 1 284 ? -3.149 51.336 36.734 1.00 49.96 ? 372 LEU A CG 1 ATOM 2319 C CD1 . LEU A 1 284 ? -2.387 50.168 36.174 1.00 41.38 ? 372 LEU A CD1 1 ATOM 2320 C CD2 . LEU A 1 284 ? -2.197 52.376 37.264 1.00 49.58 ? 372 LEU A CD2 1 ATOM 2321 N N . LEU A 1 285 ? -7.133 51.696 35.859 1.00 44.42 ? 373 LEU A N 1 ATOM 2322 C CA . LEU A 1 285 ? -8.271 51.590 36.747 1.00 50.75 ? 373 LEU A CA 1 ATOM 2323 C C . LEU A 1 285 ? -9.061 50.336 36.404 1.00 57.17 ? 373 LEU A C 1 ATOM 2324 O O . LEU A 1 285 ? -9.497 49.602 37.279 1.00 61.77 ? 373 LEU A O 1 ATOM 2325 C CB . LEU A 1 285 ? -9.134 52.841 36.613 1.00 48.10 ? 373 LEU A CB 1 ATOM 2326 C CG . LEU A 1 285 ? -10.364 52.979 37.480 1.00 53.93 ? 373 LEU A CG 1 ATOM 2327 C CD1 . LEU A 1 285 ? -9.930 53.334 38.876 1.00 51.02 ? 373 LEU A CD1 1 ATOM 2328 C CD2 . LEU A 1 285 ? -11.221 54.067 36.898 1.00 59.25 ? 373 LEU A CD2 1 ATOM 2329 N N . TYR A 1 286 ? -9.199 50.058 35.119 1.00 46.38 ? 374 TYR A N 1 ATOM 2330 C CA . TYR A 1 286 ? -10.018 48.929 34.698 1.00 53.00 ? 374 TYR A CA 1 ATOM 2331 C C . TYR A 1 286 ? -9.248 47.616 34.819 1.00 51.17 ? 374 TYR A C 1 ATOM 2332 O O . TYR A 1 286 ? -9.832 46.551 35.022 1.00 53.38 ? 374 TYR A O 1 ATOM 2333 C CB . TYR A 1 286 ? -10.494 49.183 33.259 1.00 57.36 ? 374 TYR A CB 1 ATOM 2334 C CG . TYR A 1 286 ? -11.105 50.562 33.131 1.00 56.08 ? 374 TYR A CG 1 ATOM 2335 C CD1 . TYR A 1 286 ? -12.394 50.820 33.590 1.00 55.60 ? 374 TYR A CD1 1 ATOM 2336 C CD2 . TYR A 1 286 ? -10.380 51.613 32.610 1.00 53.82 ? 374 TYR A CD2 1 ATOM 2337 C CE1 . TYR A 1 286 ? -12.950 52.086 33.491 1.00 52.51 ? 374 TYR A CE1 1 ATOM 2338 C CE2 . TYR A 1 286 ? -10.921 52.890 32.510 1.00 52.36 ? 374 TYR A CE2 1 ATOM 2339 C CZ . TYR A 1 286 ? -12.207 53.118 32.945 1.00 57.67 ? 374 TYR A CZ 1 ATOM 2340 O OH . TYR A 1 286 ? -12.748 54.387 32.848 1.00 69.48 ? 374 TYR A OH 1 ATOM 2341 N N . GLU A 1 287 ? -7.928 47.697 34.686 1.00 54.72 ? 375 GLU A N 1 ATOM 2342 C CA . GLU A 1 287 ? -7.066 46.540 34.903 1.00 49.94 ? 375 GLU A CA 1 ATOM 2343 C C . GLU A 1 287 ? -7.199 46.078 36.352 1.00 52.74 ? 375 GLU A C 1 ATOM 2344 O O . GLU A 1 287 ? -7.240 44.876 36.632 1.00 59.54 ? 375 GLU A O 1 ATOM 2345 C CB . GLU A 1 287 ? -5.605 46.907 34.612 1.00 44.28 ? 375 GLU A CB 1 ATOM 2346 C CG . GLU A 1 287 ? -5.338 47.459 33.209 1.00 52.56 ? 375 GLU A CG 1 ATOM 2347 C CD . GLU A 1 287 ? -3.930 48.054 33.059 1.00 55.48 ? 375 GLU A CD 1 ATOM 2348 O OE1 . GLU A 1 287 ? -3.638 48.682 32.008 1.00 45.34 ? 375 GLU A OE1 1 ATOM 2349 O OE2 . GLU A 1 287 ? -3.106 47.907 33.994 1.00 51.11 ? 375 GLU A OE2 1 ATOM 2350 N N . LYS A 1 288 ? -7.273 47.028 37.279 1.00 55.08 ? 376 LYS A N 1 ATOM 2351 C CA . LYS A 1 288 ? -7.381 46.674 38.684 1.00 54.69 ? 376 LYS A CA 1 ATOM 2352 C C . LYS A 1 288 ? -8.747 46.105 39.049 1.00 56.63 ? 376 LYS A C 1 ATOM 2353 O O . LYS A 1 288 ? -8.827 45.170 39.849 1.00 55.77 ? 376 LYS A O 1 ATOM 2354 C CB . LYS A 1 288 ? -6.947 47.837 39.587 1.00 56.67 ? 376 LYS A CB 1 ATOM 2355 C CG . LYS A 1 288 ? -5.470 48.128 39.394 1.00 45.82 ? 376 LYS A CG 1 ATOM 2356 C CD . LYS A 1 288 ? -4.898 49.131 40.383 1.00 44.85 ? 376 LYS A CD 1 ATOM 2357 C CE . LYS A 1 288 ? -3.489 49.504 39.858 1.00 52.28 ? 376 LYS A CE 1 ATOM 2358 N NZ . LYS A 1 288 ? -2.760 50.403 40.793 1.00 46.83 ? 376 LYS A NZ 1 ATOM 2359 N N . ASN A 1 289 ? -9.810 46.627 38.439 1.00 54.01 ? 377 ASN A N 1 ATOM 2360 C CA . ASN A 1 289 ? -11.121 45.980 38.556 1.00 58.07 ? 377 ASN A CA 1 ATOM 2361 C C . ASN A 1 289 ? -10.998 44.524 38.133 1.00 63.14 ? 377 ASN A C 1 ATOM 2362 O O . ASN A 1 289 ? -11.565 43.603 38.736 1.00 66.51 ? 377 ASN A O 1 ATOM 2363 C CB . ASN A 1 289 ? -12.148 46.662 37.646 1.00 65.48 ? 377 ASN A CB 1 ATOM 2364 C CG . ASN A 1 289 ? -12.389 48.126 38.004 1.00 69.48 ? 377 ASN A CG 1 ATOM 2365 O OD1 . ASN A 1 289 ? -12.030 48.584 39.087 1.00 70.18 ? 377 ASN A OD1 1 ATOM 2366 N ND2 . ASN A 1 289 ? -13.023 48.861 37.090 1.00 66.46 ? 377 ASN A ND2 1 ATOM 2367 N N . LEU A 1 290 ? -10.252 44.317 37.067 1.00 68.31 ? 378 LEU A N 1 ATOM 2368 C CA . LEU A 1 290 ? -10.097 42.986 36.526 1.00 66.62 ? 378 LEU A CA 1 ATOM 2369 C C . LEU A 1 290 ? -9.361 42.089 37.505 1.00 65.23 ? 378 LEU A C 1 ATOM 2370 O O . LEU A 1 290 ? -9.785 40.967 37.786 1.00 61.47 ? 378 LEU A O 1 ATOM 2371 C CB . LEU A 1 290 ? -9.316 43.047 35.218 1.00 62.89 ? 378 LEU A CB 1 ATOM 2372 C CG . LEU A 1 290 ? -8.943 41.661 34.706 1.00 61.05 ? 378 LEU A CG 1 ATOM 2373 C CD1 . LEU A 1 290 ? -10.205 40.911 34.403 1.00 68.00 ? 378 LEU A CD1 1 ATOM 2374 C CD2 . LEU A 1 290 ? -8.082 41.752 33.455 1.00 55.01 ? 378 LEU A CD2 1 ATOM 2375 N N . VAL A 1 291 ? -8.221 42.568 37.978 1.00 56.95 ? 379 VAL A N 1 ATOM 2376 C CA . VAL A 1 291 ? -7.385 41.741 38.828 1.00 59.07 ? 379 VAL A CA 1 ATOM 2377 C C . VAL A 1 291 ? -8.137 41.504 40.127 1.00 65.25 ? 379 VAL A C 1 ATOM 2378 O O . VAL A 1 291 ? -8.131 40.391 40.669 1.00 66.28 ? 379 VAL A O 1 ATOM 2379 C CB . VAL A 1 291 ? -6.026 42.408 39.088 1.00 56.56 ? 379 VAL A CB 1 ATOM 2380 C CG1 . VAL A 1 291 ? -5.326 41.714 40.227 1.00 64.81 ? 379 VAL A CG1 1 ATOM 2381 C CG2 . VAL A 1 291 ? -5.175 42.357 37.806 1.00 53.68 ? 379 VAL A CG2 1 ATOM 2382 N N . LYS A 1 292 ? -8.837 42.532 40.596 1.00 60.37 ? 380 LYS A N 1 ATOM 2383 C CA . LYS A 1 292 ? -9.668 42.366 41.784 1.00 64.62 ? 380 LYS A CA 1 ATOM 2384 C C . LYS A 1 292 ? -10.794 41.399 41.491 1.00 74.10 ? 380 LYS A C 1 ATOM 2385 O O . LYS A 1 292 ? -11.199 40.629 42.365 1.00 79.08 ? 380 LYS A O 1 ATOM 2386 C CB . LYS A 1 292 ? -10.227 43.695 42.303 1.00 76.70 ? 380 LYS A CB 1 ATOM 2387 C CG . LYS A 1 292 ? -10.531 43.680 43.831 1.00 75.49 ? 380 LYS A CG 1 ATOM 2388 C CD . LYS A 1 292 ? -11.882 43.109 44.134 1.00 72.23 ? 380 LYS A CD 1 ATOM 2389 C CE . LYS A 1 292 ? -12.345 43.382 45.577 1.00 79.66 ? 380 LYS A CE 1 ATOM 2390 N NZ . LYS A 1 292 ? -13.669 42.751 45.750 1.00 81.26 ? 380 LYS A NZ 1 ATOM 2391 N N . HIS A 1 293 ? -11.286 41.393 40.259 1.00 71.52 ? 381 HIS A N 1 ATOM 2392 C CA . HIS A 1 293 ? -12.363 40.462 39.960 1.00 82.48 ? 381 HIS A CA 1 ATOM 2393 C C . HIS A 1 293 ? -11.896 39.004 39.931 1.00 85.26 ? 381 HIS A C 1 ATOM 2394 O O . HIS A 1 293 ? -12.606 38.106 40.386 1.00 90.48 ? 381 HIS A O 1 ATOM 2395 C CB . HIS A 1 293 ? -13.089 40.815 38.669 1.00 81.52 ? 381 HIS A CB 1 ATOM 2396 C CG . HIS A 1 293 ? -14.144 39.826 38.311 1.00 90.62 ? 381 HIS A CG 1 ATOM 2397 N ND1 . HIS A 1 293 ? -13.946 38.838 37.371 1.00 96.06 ? 381 HIS A ND1 1 ATOM 2398 C CD2 . HIS A 1 293 ? -15.388 39.630 38.808 1.00 101.08 ? 381 HIS A CD2 1 ATOM 2399 C CE1 . HIS A 1 293 ? -15.034 38.092 37.283 1.00 104.05 ? 381 HIS A CE1 1 ATOM 2400 N NE2 . HIS A 1 293 ? -15.923 38.551 38.147 1.00 108.21 ? 381 HIS A NE2 1 ATOM 2401 N N . LEU A 1 294 ? -10.698 38.776 39.405 1.00 77.39 ? 382 LEU A N 1 ATOM 2402 C CA . LEU A 1 294 ? -10.138 37.428 39.338 1.00 83.07 ? 382 LEU A CA 1 ATOM 2403 C C . LEU A 1 294 ? -9.451 37.005 40.635 1.00 78.54 ? 382 LEU A C 1 ATOM 2404 O O . LEU A 1 294 ? -8.985 35.872 40.745 1.00 90.11 ? 382 LEU A O 1 ATOM 2405 C CB . LEU A 1 294 ? -9.129 37.330 38.188 1.00 74.62 ? 382 LEU A CB 1 ATOM 2406 C CG . LEU A 1 294 ? -9.647 37.725 36.813 1.00 69.34 ? 382 LEU A CG 1 ATOM 2407 C CD1 . LEU A 1 294 ? -8.478 37.853 35.820 1.00 65.03 ? 382 LEU A CD1 1 ATOM 2408 C CD2 . LEU A 1 294 ? -10.684 36.712 36.331 1.00 74.32 ? 382 LEU A CD2 1 ATOM 2409 N N . ASN A 1 295 ? -9.365 37.916 41.602 1.00 85.35 ? 383 ASN A N 1 ATOM 2410 C CA . ASN A 1 295 ? -8.652 37.633 42.843 1.00 90.88 ? 383 ASN A CA 1 ATOM 2411 C C . ASN A 1 295 ? -9.229 36.444 43.623 1.00 99.16 ? 383 ASN A C 1 ATOM 2412 O O . ASN A 1 295 ? -10.430 36.382 43.875 1.00 90.43 ? 383 ASN A O 1 ATOM 2413 C CB . ASN A 1 295 ? -8.593 38.869 43.745 1.00 86.84 ? 383 ASN A CB 1 ATOM 2414 C CG . ASN A 1 295 ? -7.780 38.625 44.998 1.00 90.60 ? 383 ASN A CG 1 ATOM 2415 O OD1 . ASN A 1 295 ? -6.759 37.935 44.963 1.00 81.13 ? 383 ASN A OD1 1 ATOM 2416 N ND2 . ASN A 1 295 ? -8.236 39.177 46.119 1.00 94.40 ? 383 ASN A ND2 1 ATOM 2417 N N . GLN A 1 296 ? -8.356 35.504 43.979 1.00 90.24 ? 384 GLN A N 1 ATOM 2418 C CA . GLN A 1 296 ? -8.745 34.305 44.711 1.00 113.92 ? 384 GLN A CA 1 ATOM 2419 C C . GLN A 1 296 ? -8.402 34.432 46.188 1.00 101.04 ? 384 GLN A C 1 ATOM 2420 O O . GLN A 1 296 ? -8.626 33.504 46.964 1.00 120.64 ? 384 GLN A O 1 ATOM 2421 C CB . GLN A 1 296 ? -8.047 33.068 44.139 1.00 100.63 ? 384 GLN A CB 1 ATOM 2422 C CG . GLN A 1 296 ? -8.715 32.492 42.921 1.00 101.14 ? 384 GLN A CG 1 ATOM 2423 C CD . GLN A 1 296 ? -8.086 31.184 42.488 1.00 110.05 ? 384 GLN A CD 1 ATOM 2424 O OE1 . GLN A 1 296 ? -6.861 31.057 42.412 1.00 104.61 ? 384 GLN A OE1 1 ATOM 2425 N NE2 . GLN A 1 296 ? -8.924 30.196 42.208 1.00 110.70 ? 384 GLN A NE2 1 ATOM 2426 N N . GLY A 1 297 ? -7.841 35.576 46.563 1.00 96.36 ? 385 GLY A N 1 ATOM 2427 C CA . GLY A 1 297 ? -7.463 35.825 47.939 1.00 103.80 ? 385 GLY A CA 1 ATOM 2428 C C . GLY A 1 297 ? -8.551 36.518 48.734 1.00 100.25 ? 385 GLY A C 1 ATOM 2429 O O . GLY A 1 297 ? -9.632 36.806 48.227 1.00 99.35 ? 385 GLY A O 1 ATOM 2430 N N . THR A 1 298 ? -8.260 36.792 49.996 1.00 102.77 ? 386 THR A N 1 ATOM 2431 C CA . THR A 1 298 ? -9.230 37.448 50.868 1.00 107.33 ? 386 THR A CA 1 ATOM 2432 C C . THR A 1 298 ? -9.073 38.953 50.764 1.00 101.86 ? 386 THR A C 1 ATOM 2433 O O . THR A 1 298 ? -8.073 39.445 50.250 1.00 93.11 ? 386 THR A O 1 ATOM 2434 C CB . THR A 1 298 ? -9.019 37.071 52.330 1.00 110.85 ? 386 THR A CB 1 ATOM 2435 O OG1 . THR A 1 298 ? -7.660 37.340 52.689 1.00 109.06 ? 386 THR A OG1 1 ATOM 2436 C CG2 . THR A 1 298 ? -9.325 35.602 52.556 1.00 118.54 ? 386 THR A CG2 1 ATOM 2437 N N . ASP A 1 299 ? -10.052 39.687 51.277 1.00 99.87 ? 387 ASP A N 1 ATOM 2438 C CA . ASP A 1 299 ? -9.951 41.131 51.286 1.00 93.58 ? 387 ASP A CA 1 ATOM 2439 C C . ASP A 1 299 ? -8.912 41.582 52.306 1.00 96.01 ? 387 ASP A C 1 ATOM 2440 O O . ASP A 1 299 ? -8.321 42.652 52.177 1.00 89.08 ? 387 ASP A O 1 ATOM 2441 C CB . ASP A 1 299 ? -11.310 41.766 51.551 1.00 100.21 ? 387 ASP A CB 1 ATOM 2442 C CG . ASP A 1 299 ? -12.179 41.805 50.311 1.00 99.27 ? 387 ASP A CG 1 ATOM 2443 O OD1 . ASP A 1 299 ? -11.640 41.644 49.196 1.00 93.27 ? 387 ASP A OD1 1 ATOM 2444 O OD2 . ASP A 1 299 ? -13.401 42.005 50.446 1.00 108.40 ? 387 ASP A OD2 1 ATOM 2445 N N . GLU A 1 300 ? -8.677 40.751 53.312 1.00 99.70 ? 388 GLU A N 1 ATOM 2446 C CA . GLU A 1 300 ? -7.667 41.048 54.320 1.00 100.94 ? 388 GLU A CA 1 ATOM 2447 C C . GLU A 1 300 ? -6.281 40.998 53.688 1.00 97.33 ? 388 GLU A C 1 ATOM 2448 O O . GLU A 1 300 ? -5.422 41.817 53.990 1.00 94.96 ? 388 GLU A O 1 ATOM 2449 C CB . GLU A 1 300 ? -7.747 40.067 55.501 1.00 114.27 ? 388 GLU A CB 1 ATOM 2450 C CG . GLU A 1 300 ? -8.967 40.234 56.409 1.00 117.89 ? 388 GLU A CG 1 ATOM 2451 C CD . GLU A 1 300 ? -10.202 39.515 55.890 1.00 124.66 ? 388 GLU A CD 1 ATOM 2452 O OE1 . GLU A 1 300 ? -10.076 38.706 54.944 1.00 122.64 ? 388 GLU A OE1 1 ATOM 2453 O OE2 . GLU A 1 300 ? -11.300 39.762 56.436 1.00 127.32 ? 388 GLU A OE2 1 ATOM 2454 N N . ASP A 1 301 ? -6.068 40.020 52.820 1.00 97.43 ? 389 ASP A N 1 ATOM 2455 C CA . ASP A 1 301 ? -4.810 39.922 52.084 1.00 103.02 ? 389 ASP A CA 1 ATOM 2456 C C . ASP A 1 301 ? -4.522 41.181 51.247 1.00 95.95 ? 389 ASP A C 1 ATOM 2457 O O . ASP A 1 301 ? -3.374 41.582 51.084 1.00 91.09 ? 389 ASP A O 1 ATOM 2458 C CB . ASP A 1 301 ? -4.794 38.679 51.195 1.00 95.55 ? 389 ASP A CB 1 ATOM 2459 C CG . ASP A 1 301 ? -4.711 37.392 51.992 1.00 106.12 ? 389 ASP A CG 1 ATOM 2460 O OD1 . ASP A 1 301 ? -4.525 37.472 53.220 1.00 115.04 ? 389 ASP A OD1 1 ATOM 2461 O OD2 . ASP A 1 301 ? -4.817 36.301 51.382 1.00 107.94 ? 389 ASP A OD2 1 ATOM 2462 N N . ILE A 1 302 ? -5.562 41.820 50.732 1.00 83.86 ? 390 ILE A N 1 ATOM 2463 C CA . ILE A 1 302 ? -5.338 43.067 50.023 1.00 77.73 ? 390 ILE A CA 1 ATOM 2464 C C . ILE A 1 302 ? -5.023 44.213 50.995 1.00 78.74 ? 390 ILE A C 1 ATOM 2465 O O . ILE A 1 302 ? -4.083 44.971 50.757 1.00 74.15 ? 390 ILE A O 1 ATOM 2466 C CB . ILE A 1 302 ? -6.517 43.448 49.108 1.00 75.03 ? 390 ILE A CB 1 ATOM 2467 C CG1 . ILE A 1 302 ? -6.853 42.304 48.154 1.00 75.87 ? 390 ILE A CG1 1 ATOM 2468 C CG2 . ILE A 1 302 ? -6.205 44.709 48.342 1.00 69.28 ? 390 ILE A CG2 1 ATOM 2469 C CD1 . ILE A 1 302 ? -8.257 42.401 47.596 1.00 75.89 ? 390 ILE A CD1 1 ATOM 2470 N N . TYR A 1 303 ? -5.780 44.328 52.094 1.00 81.21 ? 391 TYR A N 1 ATOM 2471 C CA . TYR A 1 303 ? -5.613 45.456 53.014 1.00 81.19 ? 391 TYR A CA 1 ATOM 2472 C C . TYR A 1 303 ? -4.214 45.429 53.611 1.00 82.44 ? 391 TYR A C 1 ATOM 2473 O O . TYR A 1 303 ? -3.498 46.418 53.585 1.00 79.70 ? 391 TYR A O 1 ATOM 2474 C CB . TYR A 1 303 ? -6.692 45.437 54.114 1.00 85.88 ? 391 TYR A CB 1 ATOM 2475 C CG . TYR A 1 303 ? -6.709 46.642 55.056 1.00 86.17 ? 391 TYR A CG 1 ATOM 2476 C CD1 . TYR A 1 303 ? -7.287 47.847 54.670 1.00 105.50 ? 391 TYR A CD1 1 ATOM 2477 C CD2 . TYR A 1 303 ? -6.167 46.564 56.336 1.00 90.50 ? 391 TYR A CD2 1 ATOM 2478 C CE1 . TYR A 1 303 ? -7.312 48.947 55.531 1.00 107.72 ? 391 TYR A CE1 1 ATOM 2479 C CE2 . TYR A 1 303 ? -6.187 47.664 57.205 1.00 91.12 ? 391 TYR A CE2 1 ATOM 2480 C CZ . TYR A 1 303 ? -6.762 48.847 56.797 1.00 87.51 ? 391 TYR A CZ 1 ATOM 2481 O OH . TYR A 1 303 ? -6.780 49.935 57.641 1.00 88.46 ? 391 TYR A OH 1 ATOM 2482 N N . LEU A 1 304 ? -3.819 44.266 54.110 1.00 87.70 ? 392 LEU A N 1 ATOM 2483 C CA . LEU A 1 304 ? -2.565 44.118 54.843 1.00 90.56 ? 392 LEU A CA 1 ATOM 2484 C C . LEU A 1 304 ? -1.319 43.912 53.981 1.00 89.63 ? 392 LEU A C 1 ATOM 2485 O O . LEU A 1 304 ? -0.247 44.417 54.315 1.00 87.39 ? 392 LEU A O 1 ATOM 2486 C CB . LEU A 1 304 ? -2.675 42.963 55.841 1.00 97.09 ? 392 LEU A CB 1 ATOM 2487 C CG . LEU A 1 304 ? -3.457 43.202 57.142 1.00 107.77 ? 392 LEU A CG 1 ATOM 2488 C CD1 . LEU A 1 304 ? -3.333 44.645 57.604 1.00 99.15 ? 392 LEU A CD1 1 ATOM 2489 C CD2 . LEU A 1 304 ? -4.918 42.803 57.009 1.00 112.29 ? 392 LEU A CD2 1 ATOM 2490 N N . LEU A 1 305 ? -1.464 43.158 52.890 1.00 86.05 ? 393 LEU A N 1 ATOM 2491 C CA . LEU A 1 305 ? -0.319 42.661 52.132 1.00 84.45 ? 393 LEU A CA 1 ATOM 2492 C C . LEU A 1 305 ? -0.234 43.255 50.720 1.00 84.92 ? 393 LEU A C 1 ATOM 2493 O O . LEU A 1 305 ? 0.791 43.125 50.039 1.00 78.38 ? 393 LEU A O 1 ATOM 2494 C CB . LEU A 1 305 ? -0.389 41.135 52.042 1.00 96.53 ? 393 LEU A CB 1 ATOM 2495 C CG . LEU A 1 305 ? -0.496 40.285 53.312 1.00 104.05 ? 393 LEU A CG 1 ATOM 2496 C CD1 . LEU A 1 305 ? -1.166 38.946 53.011 1.00 99.86 ? 393 LEU A CD1 1 ATOM 2497 C CD2 . LEU A 1 305 ? 0.875 40.060 53.938 1.00 105.58 ? 393 LEU A CD2 1 ATOM 2498 N N . GLY A 1 306 ? -1.316 43.902 50.287 1.00 74.71 ? 394 GLY A N 1 ATOM 2499 C CA . GLY A 1 306 ? -1.415 44.437 48.939 1.00 69.20 ? 394 GLY A CA 1 ATOM 2500 C C . GLY A 1 306 ? -1.379 43.277 47.963 1.00 80.58 ? 394 GLY A C 1 ATOM 2501 O O . GLY A 1 306 ? -1.008 43.434 46.791 1.00 76.97 ? 394 GLY A O 1 ATOM 2502 N N . LYS A 1 307 ? -1.770 42.103 48.453 1.00 77.65 ? 395 LYS A N 1 ATOM 2503 C CA . LYS A 1 307 ? -1.587 40.876 47.711 1.00 78.28 ? 395 LYS A CA 1 ATOM 2504 C C . LYS A 1 307 ? -2.876 40.355 47.103 1.00 85.22 ? 395 LYS A C 1 ATOM 2505 O O . LYS A 1 307 ? -3.863 40.111 47.809 1.00 87.53 ? 395 LYS A O 1 ATOM 2506 C CB . LYS A 1 307 ? -0.953 39.807 48.602 1.00 82.13 ? 395 LYS A CB 1 ATOM 2507 C CG . LYS A 1 307 ? -0.604 38.508 47.891 1.00 88.75 ? 395 LYS A CG 1 ATOM 2508 C CD . LYS A 1 307 ? 0.245 37.614 48.784 1.00 95.52 ? 395 LYS A CD 1 ATOM 2509 C CE . LYS A 1 307 ? -0.426 36.281 49.067 1.00 98.90 ? 395 LYS A CE 1 ATOM 2510 N NZ . LYS A 1 307 ? 0.515 35.350 49.758 1.00 104.87 ? 395 LYS A NZ 1 ATOM 2511 N N . ALA A 1 308 ? -2.846 40.191 45.780 1.00 77.26 ? 396 ALA A N 1 ATOM 2512 C CA . ALA A 1 308 ? -3.893 39.485 45.070 1.00 74.91 ? 396 ALA A CA 1 ATOM 2513 C C . ALA A 1 308 ? -3.320 38.145 44.658 1.00 77.10 ? 396 ALA A C 1 ATOM 2514 O O . ALA A 1 308 ? -2.117 38.016 44.463 1.00 78.87 ? 396 ALA A O 1 ATOM 2515 C CB . ALA A 1 308 ? -4.335 40.273 43.866 1.00 72.69 ? 396 ALA A CB 1 ATOM 2516 N N . THR A 1 309 ? -4.164 37.133 44.556 1.00 80.20 ? 397 THR A N 1 ATOM 2517 C CA . THR A 1 309 ? -3.690 35.854 44.059 1.00 93.43 ? 397 THR A CA 1 ATOM 2518 C C . THR A 1 309 ? -4.522 35.425 42.877 1.00 94.64 ? 397 THR A C 1 ATOM 2519 O O . THR A 1 309 ? -5.733 35.226 42.995 1.00 97.70 ? 397 THR A O 1 ATOM 2520 C CB . THR A 1 309 ? -3.715 34.750 45.130 1.00 99.79 ? 397 THR A CB 1 ATOM 2521 O OG1 . THR A 1 309 ? -2.616 34.945 46.030 1.00 97.64 ? 397 THR A OG1 1 ATOM 2522 C CG2 . THR A 1 309 ? -3.594 33.368 44.481 1.00 94.84 ? 397 THR A CG2 1 ATOM 2523 N N . LEU A 1 310 ? -3.859 35.311 41.732 1.00 94.64 ? 398 LEU A N 1 ATOM 2524 C CA . LEU A 1 310 ? -4.482 34.784 40.528 1.00 88.99 ? 398 LEU A CA 1 ATOM 2525 C C . LEU A 1 310 ? -3.831 33.453 40.142 1.00 88.06 ? 398 LEU A C 1 ATOM 2526 O O . LEU A 1 310 ? -2.615 33.271 40.275 1.00 84.91 ? 398 LEU A O 1 ATOM 2527 C CB . LEU A 1 310 ? -4.391 35.794 39.375 1.00 81.06 ? 398 LEU A CB 1 ATOM 2528 C CG . LEU A 1 310 ? -5.511 36.831 39.218 1.00 76.24 ? 398 LEU A CG 1 ATOM 2529 C CD1 . LEU A 1 310 ? -5.704 37.649 40.491 1.00 81.38 ? 398 LEU A CD1 1 ATOM 2530 C CD2 . LEU A 1 310 ? -5.231 37.761 38.019 1.00 72.17 ? 398 LEU A CD2 1 ATOM 2531 N N . PRO A 1 311 ? -4.643 32.508 39.664 1.00 94.19 ? 399 PRO A N 1 ATOM 2532 C CA . PRO A 1 311 ? -4.062 31.226 39.271 1.00 103.34 ? 399 PRO A CA 1 ATOM 2533 C C . PRO A 1 311 ? -3.483 31.313 37.862 1.00 98.94 ? 399 PRO A C 1 ATOM 2534 O O . PRO A 1 311 ? -3.954 32.117 37.050 1.00 91.35 ? 399 PRO A O 1 ATOM 2535 C CB . PRO A 1 311 ? -5.267 30.289 39.298 1.00 108.02 ? 399 PRO A CB 1 ATOM 2536 C CG . PRO A 1 311 ? -6.409 31.167 38.902 1.00 104.84 ? 399 PRO A CG 1 ATOM 2537 C CD . PRO A 1 311 ? -6.093 32.567 39.405 1.00 87.86 ? 399 PRO A CD 1 ATOM 2538 N N . GLY A 1 312 ? -2.464 30.502 37.585 1.00 99.24 ? 400 GLY A N 1 ATOM 2539 C CA . GLY A 1 312 ? -1.828 30.489 36.281 1.00 85.87 ? 400 GLY A CA 1 ATOM 2540 C C . GLY A 1 312 ? -2.669 29.742 35.271 1.00 87.89 ? 400 GLY A C 1 ATOM 2541 O O . GLY A 1 312 ? -3.483 28.904 35.648 1.00 95.32 ? 400 GLY A O 1 ATOM 2542 N N . PHE A 1 313 ? -2.480 30.054 33.990 1.00 84.95 ? 401 PHE A N 1 ATOM 2543 C CA . PHE A 1 313 ? -3.249 29.421 32.927 1.00 89.06 ? 401 PHE A CA 1 ATOM 2544 C C . PHE A 1 313 ? -3.119 27.904 32.967 1.00 96.54 ? 401 PHE A C 1 ATOM 2545 O O . PHE A 1 313 ? -4.104 27.192 32.768 1.00 99.75 ? 401 PHE A O 1 ATOM 2546 C CB . PHE A 1 313 ? -2.829 29.959 31.552 1.00 81.47 ? 401 PHE A CB 1 ATOM 2547 C CG . PHE A 1 313 ? -3.260 31.389 31.294 1.00 78.47 ? 401 PHE A CG 1 ATOM 2548 C CD1 . PHE A 1 313 ? -4.525 31.827 31.673 1.00 75.11 ? 401 PHE A CD1 1 ATOM 2549 C CD2 . PHE A 1 313 ? -2.397 32.294 30.680 1.00 71.99 ? 401 PHE A CD2 1 ATOM 2550 C CE1 . PHE A 1 313 ? -4.930 33.137 31.443 1.00 70.94 ? 401 PHE A CE1 1 ATOM 2551 C CE2 . PHE A 1 313 ? -2.792 33.615 30.448 1.00 71.45 ? 401 PHE A CE2 1 ATOM 2552 C CZ . PHE A 1 313 ? -4.065 34.039 30.838 1.00 64.46 ? 401 PHE A CZ 1 ATOM 2553 N N . ARG A 1 314 ? -1.914 27.415 33.254 1.00 102.03 ? 402 ARG A N 1 ATOM 2554 C CA . ARG A 1 314 ? -1.630 25.971 33.240 1.00 109.79 ? 402 ARG A CA 1 ATOM 2555 C C . ARG A 1 314 ? -2.582 25.161 34.124 1.00 118.52 ? 402 ARG A C 1 ATOM 2556 O O . ARG A 1 314 ? -2.722 23.945 33.959 1.00 115.43 ? 402 ARG A O 1 ATOM 2557 C CB . ARG A 1 314 ? -0.173 25.706 33.652 1.00 103.14 ? 402 ARG A CB 1 ATOM 2558 C CG . ARG A 1 314 ? 0.244 24.246 33.574 1.00 118.93 ? 402 ARG A CG 1 ATOM 2559 C CD . ARG A 1 314 ? 1.719 24.047 33.859 1.00 127.33 ? 402 ARG A CD 1 ATOM 2560 N NE . ARG A 1 314 ? 2.022 22.645 34.150 1.00 147.46 ? 402 ARG A NE 1 ATOM 2561 C CZ . ARG A 1 314 ? 3.132 22.017 33.764 1.00 156.72 ? 402 ARG A CZ 1 ATOM 2562 N NH1 . ARG A 1 314 ? 4.054 22.667 33.063 1.00 156.33 ? 402 ARG A NH1 1 ATOM 2563 N NH2 . ARG A 1 314 ? 3.320 20.738 34.076 1.00 163.79 ? 402 ARG A NH2 1 ATOM 2564 N N . THR A 1 315 ? -3.255 25.848 35.044 1.00 114.45 ? 403 THR A N 1 ATOM 2565 C CA . THR A 1 315 ? -4.059 25.195 36.075 1.00 126.89 ? 403 THR A CA 1 ATOM 2566 C C . THR A 1 315 ? -5.556 25.535 36.006 1.00 128.93 ? 403 THR A C 1 ATOM 2567 O O . THR A 1 315 ? -6.244 25.518 37.021 1.00 132.12 ? 403 THR A O 1 ATOM 2568 C CB . THR A 1 315 ? -3.536 25.580 37.467 1.00 126.54 ? 403 THR A CB 1 ATOM 2569 O OG1 . THR A 1 315 ? -3.723 26.986 37.672 1.00 108.00 ? 403 THR A OG1 1 ATOM 2570 C CG2 . THR A 1 315 ? -2.053 25.262 37.587 1.00 115.75 ? 403 THR A CG2 1 ATOM 2571 N N . ILE A 1 316 ? -6.058 25.804 34.805 1.00 126.89 ? 404 ILE A N 1 ATOM 2572 C CA . ILE A 1 316 ? -7.394 26.373 34.612 1.00 129.93 ? 404 ILE A CA 1 ATOM 2573 C C . ILE A 1 316 ? -8.444 25.315 34.212 1.00 137.52 ? 404 ILE A C 1 ATOM 2574 O O . ILE A 1 316 ? -8.130 24.128 34.168 1.00 143.06 ? 404 ILE A O 1 ATOM 2575 C CB . ILE A 1 316 ? -7.311 27.474 33.536 1.00 130.44 ? 404 ILE A CB 1 ATOM 2576 C CG1 . ILE A 1 316 ? -8.416 28.512 33.698 1.00 128.46 ? 404 ILE A CG1 1 ATOM 2577 C CG2 . ILE A 1 316 ? -7.293 26.864 32.135 1.00 136.03 ? 404 ILE A CG2 1 ATOM 2578 C CD1 . ILE A 1 316 ? -8.327 29.578 32.663 1.00 121.13 ? 404 ILE A CD1 1 ATOM 2579 N N . HIS A 1 317 ? -9.681 25.738 33.935 1.00 117.15 ? 405 HIS A N 1 ATOM 2580 C CA . HIS A 1 317 ? -10.725 24.824 33.462 1.00 140.22 ? 405 HIS A CA 1 ATOM 2581 C C . HIS A 1 317 ? -10.989 24.917 31.951 1.00 142.45 ? 405 HIS A C 1 ATOM 2582 O O . HIS A 1 317 ? -10.676 25.931 31.319 1.00 142.91 ? 405 HIS A O 1 ATOM 2583 C CB . HIS A 1 317 ? -12.035 25.046 34.224 1.00 127.76 ? 405 HIS A CB 1 ATOM 2584 C CG . HIS A 1 317 ? -12.981 23.880 34.162 1.00 147.79 ? 405 HIS A CG 1 ATOM 2585 N ND1 . HIS A 1 317 ? -12.600 22.631 33.716 1.00 152.67 ? 405 HIS A ND1 1 ATOM 2586 C CD2 . HIS A 1 317 ? -14.291 23.773 34.493 1.00 151.86 ? 405 HIS A CD2 1 ATOM 2587 C CE1 . HIS A 1 317 ? -13.634 21.809 33.767 1.00 160.39 ? 405 HIS A CE1 1 ATOM 2588 N NE2 . HIS A 1 317 ? -14.672 22.477 34.236 1.00 160.43 ? 405 HIS A NE2 1 ATOM 2589 N N . CYS A 1 318 ? -11.562 23.837 31.409 1.00 148.36 ? 406 CYS A N 1 ATOM 2590 C CA . CYS A 1 318 ? -11.967 23.671 30.001 1.00 145.28 ? 406 CYS A CA 1 ATOM 2591 C C . CYS A 1 318 ? -11.386 24.664 28.998 1.00 129.07 ? 406 CYS A C 1 ATOM 2592 O O . CYS A 1 318 ? -10.459 24.336 28.264 1.00 127.20 ? 406 CYS A O 1 ATOM 2593 C CB . CYS A 1 318 ? -13.496 23.644 29.883 1.00 151.35 ? 406 CYS A CB 1 ATOM 2594 S SG . CYS A 1 318 ? -14.306 25.178 30.401 1.00 161.19 ? 406 CYS A SG 1 HETATM 2595 C C1 . NAG B 2 . ? -3.364 33.058 18.824 1.00 85.25 ? 501 NAG A C1 1 HETATM 2596 C C2 . NAG B 2 . ? -4.467 33.709 18.003 1.00 82.57 ? 501 NAG A C2 1 HETATM 2597 C C3 . NAG B 2 . ? -5.283 32.643 17.273 1.00 80.50 ? 501 NAG A C3 1 HETATM 2598 C C4 . NAG B 2 . ? -4.392 31.655 16.532 1.00 79.42 ? 501 NAG A C4 1 HETATM 2599 C C5 . NAG B 2 . ? -3.251 31.156 17.415 1.00 85.18 ? 501 NAG A C5 1 HETATM 2600 C C6 . NAG B 2 . ? -2.229 30.346 16.647 1.00 85.88 ? 501 NAG A C6 1 HETATM 2601 C C7 . NAG B 2 . ? -5.716 35.751 18.568 1.00 94.32 ? 501 NAG A C7 1 HETATM 2602 C C8 . NAG B 2 . ? -6.598 36.422 19.583 1.00 80.17 ? 501 NAG A C8 1 HETATM 2603 N N2 . NAG B 2 . ? -5.327 34.503 18.862 1.00 93.86 ? 501 NAG A N2 1 HETATM 2604 O O3 . NAG B 2 . ? -6.170 33.266 16.350 1.00 73.83 ? 501 NAG A O3 1 HETATM 2605 O O4 . NAG B 2 . ? -5.192 30.540 16.155 1.00 76.66 ? 501 NAG A O4 1 HETATM 2606 O O5 . NAG B 2 . ? -2.549 32.269 17.988 1.00 88.63 ? 501 NAG A O5 1 HETATM 2607 O O6 . NAG B 2 . ? -1.465 31.147 15.753 1.00 81.42 ? 501 NAG A O6 1 HETATM 2608 O O7 . NAG B 2 . ? -5.368 36.310 17.526 1.00 98.31 ? 501 NAG A O7 1 HETATM 2609 C C1 . NAG C 2 . ? -5.404 30.470 14.733 1.00 73.46 ? 502 NAG A C1 1 HETATM 2610 C C2 . NAG C 2 . ? -5.580 29.006 14.403 1.00 75.77 ? 502 NAG A C2 1 HETATM 2611 C C3 . NAG C 2 . ? -5.766 28.826 12.895 1.00 74.77 ? 502 NAG A C3 1 HETATM 2612 C C4 . NAG C 2 . ? -6.864 29.744 12.361 1.00 70.37 ? 502 NAG A C4 1 HETATM 2613 C C5 . NAG C 2 . ? -6.741 31.172 12.907 1.00 76.36 ? 502 NAG A C5 1 HETATM 2614 C C6 . NAG C 2 . ? -7.980 32.000 12.650 1.00 63.89 ? 502 NAG A C6 1 HETATM 2615 C C7 . NAG C 2 . ? -4.539 27.401 15.937 1.00 82.32 ? 502 NAG A C7 1 HETATM 2616 C C8 . NAG C 2 . ? -3.286 26.664 16.298 1.00 86.81 ? 502 NAG A C8 1 HETATM 2617 N N2 . NAG C 2 . ? -4.457 28.221 14.882 1.00 80.05 ? 502 NAG A N2 1 HETATM 2618 O O3 . NAG C 2 . ? -6.081 27.461 12.641 1.00 76.78 ? 502 NAG A O3 1 HETATM 2619 O O4 . NAG C 2 . ? -6.771 29.840 10.941 1.00 69.54 ? 502 NAG A O4 1 HETATM 2620 O O5 . NAG C 2 . ? -6.532 31.177 14.330 1.00 78.94 ? 502 NAG A O5 1 HETATM 2621 O O6 . NAG C 2 . ? -7.687 33.390 12.585 1.00 62.78 ? 502 NAG A O6 1 HETATM 2622 O O7 . NAG C 2 . ? -5.580 27.262 16.571 1.00 80.87 ? 502 NAG A O7 1 HETATM 2623 C C1 . BMA D 3 . ? -7.419 28.783 10.210 1.00 70.00 ? 503 BMA A C1 1 HETATM 2624 C C2 . BMA D 3 . ? -8.035 29.439 8.995 1.00 66.86 ? 503 BMA A C2 1 HETATM 2625 C C3 . BMA D 3 . ? -8.704 28.424 8.085 1.00 67.24 ? 503 BMA A C3 1 HETATM 2626 C C4 . BMA D 3 . ? -7.904 27.126 7.879 1.00 71.37 ? 503 BMA A C4 1 HETATM 2627 C C5 . BMA D 3 . ? -7.211 26.649 9.173 1.00 75.26 ? 503 BMA A C5 1 HETATM 2628 C C6 . BMA D 3 . ? -6.182 25.567 8.886 1.00 83.62 ? 503 BMA A C6 1 HETATM 2629 O O2 . BMA D 3 . ? -7.017 30.045 8.200 1.00 71.92 ? 503 BMA A O2 1 HETATM 2630 O O3 . BMA D 3 . ? -8.951 29.031 6.836 1.00 64.99 ? 503 BMA A O3 1 HETATM 2631 O O4 . BMA D 3 . ? -8.803 26.103 7.463 1.00 71.69 ? 503 BMA A O4 1 HETATM 2632 O O5 . BMA D 3 . ? -6.550 27.753 9.835 1.00 74.16 ? 503 BMA A O5 1 HETATM 2633 O O6 . BMA D 3 . ? -5.488 25.275 10.082 1.00 96.00 ? 503 BMA A O6 1 HETATM 2634 C C1 . MAN E 4 . ? -10.366 29.051 6.584 1.00 62.25 ? 504 MAN A C1 1 HETATM 2635 C C2 . MAN E 4 . ? -10.575 29.293 5.107 1.00 69.15 ? 504 MAN A C2 1 HETATM 2636 C C3 . MAN E 4 . ? -10.216 30.720 4.746 1.00 71.07 ? 504 MAN A C3 1 HETATM 2637 C C4 . MAN E 4 . ? -10.964 31.703 5.669 1.00 67.99 ? 504 MAN A C4 1 HETATM 2638 C C5 . MAN E 4 . ? -10.630 31.360 7.114 1.00 64.41 ? 504 MAN A C5 1 HETATM 2639 C C6 . MAN E 4 . ? -11.355 32.241 8.122 1.00 67.36 ? 504 MAN A C6 1 HETATM 2640 O O2 . MAN E 4 . ? -11.931 29.175 4.761 1.00 58.59 ? 504 MAN A O2 1 HETATM 2641 O O3 . MAN E 4 . ? -10.543 30.970 3.383 1.00 62.16 ? 504 MAN A O3 1 HETATM 2642 O O4 . MAN E 4 . ? -10.533 33.014 5.391 1.00 79.14 ? 504 MAN A O4 1 HETATM 2643 O O5 . MAN E 4 . ? -11.038 30.010 7.348 1.00 59.38 ? 504 MAN A O5 1 HETATM 2644 O O6 . MAN E 4 . ? -11.047 31.801 9.450 1.00 64.20 ? 504 MAN A O6 1 HETATM 2645 C C1 . NAG F 2 . ? -12.026 27.991 3.948 1.00 60.66 ? 505 NAG A C1 1 HETATM 2646 C C2 . NAG F 2 . ? -13.391 27.390 4.178 1.00 59.69 ? 505 NAG A C2 1 HETATM 2647 C C3 . NAG F 2 . ? -13.565 26.129 3.337 1.00 61.92 ? 505 NAG A C3 1 HETATM 2648 C C4 . NAG F 2 . ? -13.264 26.426 1.871 1.00 61.46 ? 505 NAG A C4 1 HETATM 2649 C C5 . NAG F 2 . ? -11.902 27.099 1.739 1.00 73.44 ? 505 NAG A C5 1 HETATM 2650 C C6 . NAG F 2 . ? -11.616 27.560 0.327 1.00 67.92 ? 505 NAG A C6 1 HETATM 2651 C C7 . NAG F 2 . ? -14.543 27.743 6.299 1.00 60.33 ? 505 NAG A C7 1 HETATM 2652 C C8 . NAG F 2 . ? -14.645 27.364 7.753 1.00 58.69 ? 505 NAG A C8 1 HETATM 2653 N N2 . NAG F 2 . ? -13.604 27.112 5.589 1.00 62.14 ? 505 NAG A N2 1 HETATM 2654 O O3 . NAG F 2 . ? -14.905 25.675 3.473 1.00 60.76 ? 505 NAG A O3 1 HETATM 2655 O O4 . NAG F 2 . ? -13.239 25.234 1.094 1.00 63.99 ? 505 NAG A O4 1 HETATM 2656 O O5 . NAG F 2 . ? -11.858 28.269 2.571 1.00 60.01 ? 505 NAG A O5 1 HETATM 2657 O O6 . NAG F 2 . ? -12.420 28.684 -0.012 1.00 62.47 ? 505 NAG A O6 1 HETATM 2658 O O7 . NAG F 2 . ? -15.292 28.573 5.785 1.00 55.85 ? 505 NAG A O7 1 HETATM 2659 C C1 . GAL G 5 . ? -14.514 24.969 0.479 1.00 62.45 ? 506 GAL A C1 1 HETATM 2660 C C2 . GAL G 5 . ? -14.294 24.352 -0.943 1.00 64.03 ? 506 GAL A C2 1 HETATM 2661 C C3 . GAL G 5 . ? -15.597 23.847 -1.537 1.00 63.15 ? 506 GAL A C3 1 HETATM 2662 C C4 . GAL G 5 . ? -16.318 22.951 -0.562 1.00 66.98 ? 506 GAL A C4 1 HETATM 2663 C C5 . GAL G 5 . ? -16.532 23.714 0.742 1.00 68.15 ? 506 GAL A C5 1 HETATM 2664 C C6 . GAL G 5 . ? -17.168 22.907 1.849 1.00 74.20 ? 506 GAL A C6 1 HETATM 2665 O O2 . GAL G 5 . ? -13.699 25.273 -1.883 1.00 62.79 ? 506 GAL A O2 1 HETATM 2666 O O3 . GAL G 5 . ? -15.352 23.034 -2.660 1.00 65.35 ? 506 GAL A O3 1 HETATM 2667 O O4 . GAL G 5 . ? -15.523 21.801 -0.331 1.00 69.56 ? 506 GAL A O4 1 HETATM 2668 O O5 . GAL G 5 . ? -15.277 24.091 1.297 1.00 63.36 ? 506 GAL A O5 1 HETATM 2669 O O6 . GAL G 5 . ? -16.157 22.195 2.524 1.00 90.92 ? 506 GAL A O6 1 HETATM 2670 C C1 . MAN H 4 . ? -4.691 24.089 9.918 1.00 112.66 ? 507 MAN A C1 1 HETATM 2671 C C2 . MAN H 4 . ? -4.686 23.323 11.256 1.00 126.44 ? 507 MAN A C2 1 HETATM 2672 C C3 . MAN H 4 . ? -4.045 24.213 12.334 1.00 127.05 ? 507 MAN A C3 1 HETATM 2673 C C4 . MAN H 4 . ? -2.678 24.772 11.863 1.00 147.72 ? 507 MAN A C4 1 HETATM 2674 C C5 . MAN H 4 . ? -2.788 25.404 10.437 1.00 121.60 ? 507 MAN A C5 1 HETATM 2675 C C6 . MAN H 4 . ? -1.455 25.805 9.820 1.00 127.68 ? 507 MAN A C6 1 HETATM 2676 O O2 . MAN H 4 . ? -3.898 22.114 11.216 1.00 141.25 ? 507 MAN A O2 1 HETATM 2677 O O3 . MAN H 4 . ? -3.907 23.538 13.588 1.00 128.53 ? 507 MAN A O3 1 HETATM 2678 O O4 . MAN H 4 . ? -2.211 25.740 12.799 1.00 146.62 ? 507 MAN A O4 1 HETATM 2679 O O5 . MAN H 4 . ? -3.406 24.459 9.536 1.00 116.61 ? 507 MAN A O5 1 HETATM 2680 O O6 . MAN H 4 . ? -1.110 27.105 10.299 1.00 128.25 ? 507 MAN A O6 1 HETATM 2681 C C1 . NAG I 2 . ? -4.720 20.980 11.559 1.00 149.77 ? 508 NAG A C1 1 HETATM 2682 C C2 . NAG I 2 . ? -4.478 19.838 10.566 1.00 154.82 ? 508 NAG A C2 1 HETATM 2683 C C3 . NAG I 2 . ? -5.253 18.582 10.986 1.00 161.34 ? 508 NAG A C3 1 HETATM 2684 C C4 . NAG I 2 . ? -5.055 18.249 12.461 1.00 166.70 ? 508 NAG A C4 1 HETATM 2685 C C5 . NAG I 2 . ? -5.278 19.494 13.318 1.00 161.21 ? 508 NAG A C5 1 HETATM 2686 C C6 . NAG I 2 . ? -4.968 19.290 14.783 1.00 164.69 ? 508 NAG A C6 1 HETATM 2687 C C7 . NAG I 2 . ? -4.017 20.760 8.327 1.00 147.80 ? 508 NAG A C7 1 HETATM 2688 C C8 . NAG I 2 . ? -4.610 21.121 7.000 1.00 144.07 ? 508 NAG A C8 1 HETATM 2689 N N2 . NAG I 2 . ? -4.865 20.241 9.224 1.00 149.44 ? 508 NAG A N2 1 HETATM 2690 O O3 . NAG I 2 . ? -4.837 17.479 10.188 1.00 165.07 ? 508 NAG A O3 1 HETATM 2691 O O4 . NAG I 2 . ? -6.014 17.257 12.816 1.00 172.70 ? 508 NAG A O4 1 HETATM 2692 O O5 . NAG I 2 . ? -4.421 20.548 12.864 1.00 155.85 ? 508 NAG A O5 1 HETATM 2693 O O6 . NAG I 2 . ? -6.157 19.255 15.559 1.00 163.31 ? 508 NAG A O6 1 HETATM 2694 O O7 . NAG I 2 . ? -2.823 20.924 8.576 1.00 149.46 ? 508 NAG A O7 1 HETATM 2695 C C1 . GAL J 5 . ? -5.526 16.161 13.626 1.00 179.04 ? 509 GAL A C1 1 HETATM 2696 C C2 . GAL J 5 . ? -6.746 15.613 14.402 1.00 180.57 ? 509 GAL A C2 1 HETATM 2697 C C3 . GAL J 5 . ? -6.333 14.536 15.388 1.00 186.14 ? 509 GAL A C3 1 HETATM 2698 C C4 . GAL J 5 . ? -5.625 13.424 14.620 1.00 190.99 ? 509 GAL A C4 1 HETATM 2699 C C5 . GAL J 5 . ? -4.455 14.036 13.822 1.00 190.14 ? 509 GAL A C5 1 HETATM 2700 C C6 . GAL J 5 . ? -3.688 13.052 12.946 1.00 194.84 ? 509 GAL A C6 1 HETATM 2701 O O2 . GAL J 5 . ? -7.426 16.627 15.132 1.00 178.33 ? 509 GAL A O2 1 HETATM 2702 O O3 . GAL J 5 . ? -7.477 13.961 16.007 1.00 186.11 ? 509 GAL A O3 1 HETATM 2703 O O4 . GAL J 5 . ? -6.550 12.797 13.745 1.00 191.28 ? 509 GAL A O4 1 HETATM 2704 O O5 . GAL J 5 . ? -4.893 15.094 12.930 1.00 183.63 ? 509 GAL A O5 1 HETATM 2705 O O6 . GAL J 5 . ? -3.380 11.874 13.663 1.00 200.28 ? 509 GAL A O6 1 HETATM 2706 O "O5'" . CTN K 6 . ? 5.485 50.694 36.798 1.00 59.65 ? 510 CTN A "O5'" 1 HETATM 2707 C "C5'" . CTN K 6 . ? 5.327 49.288 36.922 1.00 54.52 ? 510 CTN A "C5'" 1 HETATM 2708 C "C4'" . CTN K 6 . ? 3.869 48.912 36.997 1.00 56.98 ? 510 CTN A "C4'" 1 HETATM 2709 O "O4'" . CTN K 6 . ? 3.441 48.961 38.374 1.00 48.02 ? 510 CTN A "O4'" 1 HETATM 2710 C "C1'" . CTN K 6 . ? 2.088 49.359 38.451 1.00 45.25 ? 510 CTN A "C1'" 1 HETATM 2711 N N1 . CTN K 6 . ? 2.003 50.532 39.330 1.00 45.63 ? 510 CTN A N1 1 HETATM 2712 C C6 . CTN K 6 . ? 3.050 51.482 39.333 1.00 48.19 ? 510 CTN A C6 1 HETATM 2713 C C5 . CTN K 6 . ? 3.008 52.461 40.259 1.00 48.91 ? 510 CTN A C5 1 HETATM 2714 C C4 . CTN K 6 . ? 1.896 52.483 41.160 1.00 46.55 ? 510 CTN A C4 1 HETATM 2715 N N3 . CTN K 6 . ? 0.907 51.624 41.125 1.00 43.30 ? 510 CTN A N3 1 HETATM 2716 C C2 . CTN K 6 . ? 0.875 50.652 40.185 1.00 46.41 ? 510 CTN A C2 1 HETATM 2717 O O2 . CTN K 6 . ? -0.089 49.858 40.030 1.00 48.86 ? 510 CTN A O2 1 HETATM 2718 N N4 . CTN K 6 . ? 1.858 53.465 42.137 1.00 49.31 ? 510 CTN A N4 1 HETATM 2719 C "C2'" . CTN K 6 . ? 1.594 49.648 37.033 1.00 48.60 ? 510 CTN A "C2'" 1 HETATM 2720 O "O2'" . CTN K 6 . ? 0.920 48.487 36.564 1.00 45.09 ? 510 CTN A "O2'" 1 HETATM 2721 C "C3'" . CTN K 6 . ? 2.900 49.834 36.270 1.00 51.07 ? 510 CTN A "C3'" 1 HETATM 2722 O "O3'" . CTN K 6 . ? 2.776 49.475 34.919 1.00 48.41 ? 510 CTN A "O3'" 1 HETATM 2723 P P . PO4 L 7 . ? 4.568 51.518 32.370 1.00 63.55 ? 511 PO4 A P 1 HETATM 2724 O O1 . PO4 L 7 . ? 5.663 50.593 31.850 1.00 57.19 -1 511 PO4 A O1 1 HETATM 2725 O O2 . PO4 L 7 . ? 4.252 52.626 31.389 1.00 69.39 -1 511 PO4 A O2 1 HETATM 2726 O O3 . PO4 L 7 . ? 3.308 50.701 32.542 1.00 64.79 ? 511 PO4 A O3 1 HETATM 2727 O O4 . PO4 L 7 . ? 5.004 52.106 33.700 1.00 77.77 ? 511 PO4 A O4 1 HETATM 2728 O O . HOH M 8 . ? 9.121 50.939 37.000 1.00 61.77 ? 601 HOH A O 1 HETATM 2729 O O . HOH M 8 . ? -6.040 55.405 20.697 1.00 54.69 ? 602 HOH A O 1 HETATM 2730 O O . HOH M 8 . ? 2.182 50.546 14.950 1.00 44.16 ? 603 HOH A O 1 HETATM 2731 O O . HOH M 8 . ? 3.007 52.983 17.473 1.00 63.83 ? 604 HOH A O 1 HETATM 2732 O O . HOH M 8 . ? 11.664 38.254 20.544 1.00 47.79 ? 605 HOH A O 1 HETATM 2733 O O . HOH M 8 . ? -0.982 45.108 17.172 1.00 53.36 ? 606 HOH A O 1 HETATM 2734 O O . HOH M 8 . ? -0.535 50.495 43.056 1.00 46.05 ? 607 HOH A O 1 HETATM 2735 O O . HOH M 8 . ? 7.184 52.568 25.136 1.00 48.65 ? 608 HOH A O 1 HETATM 2736 O O . HOH M 8 . ? -4.665 58.142 23.204 1.00 54.72 ? 609 HOH A O 1 HETATM 2737 O O . HOH M 8 . ? -2.182 43.808 44.277 1.00 49.30 ? 610 HOH A O 1 HETATM 2738 O O . HOH M 8 . ? 13.697 33.040 16.771 1.00 58.60 ? 611 HOH A O 1 HETATM 2739 O O . HOH M 8 . ? -1.489 55.173 33.492 1.00 44.37 ? 612 HOH A O 1 HETATM 2740 O O . HOH M 8 . ? -7.155 54.028 34.453 1.00 65.37 ? 613 HOH A O 1 HETATM 2741 O O . HOH M 8 . ? 5.509 39.278 10.157 1.00 58.72 ? 614 HOH A O 1 HETATM 2742 O O . HOH M 8 . ? 1.973 54.012 45.246 1.00 65.94 ? 615 HOH A O 1 HETATM 2743 O O . HOH M 8 . ? -0.804 51.163 45.625 1.00 50.06 ? 616 HOH A O 1 HETATM 2744 O O . HOH M 8 . ? 14.976 44.022 7.591 1.00 63.82 ? 617 HOH A O 1 HETATM 2745 O O . HOH M 8 . ? 1.821 39.915 12.002 1.00 50.99 ? 618 HOH A O 1 HETATM 2746 O O . HOH M 8 . ? 8.815 46.495 39.607 1.00 51.71 ? 619 HOH A O 1 HETATM 2747 O O . HOH M 8 . ? -0.580 60.142 49.445 1.00 63.70 ? 620 HOH A O 1 HETATM 2748 O O . HOH M 8 . ? -0.285 32.683 24.994 1.00 59.32 ? 621 HOH A O 1 HETATM 2749 O O . HOH M 8 . ? 0.855 56.809 43.273 1.00 54.04 ? 622 HOH A O 1 HETATM 2750 O O . HOH M 8 . ? 1.776 53.081 37.073 1.00 63.19 ? 623 HOH A O 1 HETATM 2751 O O . HOH M 8 . ? -3.186 32.073 24.140 1.00 52.79 ? 624 HOH A O 1 HETATM 2752 O O . HOH M 8 . ? 5.663 45.195 21.379 1.00 63.22 ? 625 HOH A O 1 HETATM 2753 O O . HOH M 8 . ? 7.769 32.824 22.282 1.00 65.02 ? 626 HOH A O 1 HETATM 2754 O O . HOH M 8 . ? 1.618 50.544 12.197 1.00 53.67 ? 627 HOH A O 1 HETATM 2755 O O . HOH M 8 . ? 20.055 34.323 24.234 1.00 70.73 ? 628 HOH A O 1 HETATM 2756 O O . HOH M 8 . ? -5.185 38.150 48.143 1.00 62.23 ? 629 HOH A O 1 HETATM 2757 O O . HOH M 8 . ? 1.478 46.906 21.151 1.00 51.40 ? 630 HOH A O 1 HETATM 2758 O O . HOH M 8 . ? 15.105 47.992 8.960 1.00 58.59 ? 631 HOH A O 1 HETATM 2759 O O . HOH M 8 . ? 5.390 60.057 25.015 1.00 67.91 ? 632 HOH A O 1 HETATM 2760 O O . HOH M 8 . ? -7.401 48.106 47.092 1.00 55.00 ? 633 HOH A O 1 HETATM 2761 O O . HOH M 8 . ? 7.585 51.630 35.591 1.00 70.26 ? 634 HOH A O 1 HETATM 2762 O O . HOH M 8 . ? -8.553 51.339 47.037 1.00 64.63 ? 635 HOH A O 1 HETATM 2763 O O . HOH M 8 . ? -3.279 44.796 17.367 1.00 54.05 ? 636 HOH A O 1 HETATM 2764 O O . HOH M 8 . ? -1.736 36.855 18.171 1.00 65.92 ? 637 HOH A O 1 HETATM 2765 O O . HOH M 8 . ? -4.133 42.826 18.475 1.00 55.71 ? 638 HOH A O 1 HETATM 2766 O O . HOH M 8 . ? 12.221 52.960 35.338 1.00 60.59 ? 639 HOH A O 1 HETATM 2767 O O . HOH M 8 . ? 16.409 52.727 37.873 1.00 55.75 ? 640 HOH A O 1 HETATM 2768 O O . HOH M 8 . ? 17.420 39.734 3.591 1.00 61.45 ? 641 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 . PRO A 1 ? 3.3853 1.8575 1.3123 -0.4624 0.9017 0.0277 89 PRO A N 2 C CA . PRO A 1 ? 3.2367 1.8508 1.3193 -0.4888 0.8941 -0.0020 89 PRO A CA 3 C C . PRO A 1 ? 3.1488 1.7587 1.2803 -0.4574 0.8416 0.0051 89 PRO A C 4 O O . PRO A 1 ? 3.1434 1.6444 1.1916 -0.4147 0.8113 0.0312 89 PRO A O 5 C CB . PRO A 1 ? 3.0966 1.8485 1.2501 -0.4628 0.8810 -0.0178 89 PRO A CB 6 C CG . PRO A 1 ? 3.1615 1.8457 1.2142 -0.4020 0.8511 0.0072 89 PRO A CG 7 C CD . PRO A 1 ? 3.3695 1.8864 1.2736 -0.4121 0.8788 0.0335 89 PRO A CD 8 N N . GLU A 2 ? 2.9288 1.6583 1.1932 -0.4763 0.8311 -0.0190 90 GLU A N 9 C CA . GLU A 2 ? 2.8172 1.5487 1.1308 -0.4500 0.7846 -0.0135 90 GLU A CA 10 C C . GLU A 2 ? 2.6560 1.4891 1.0464 -0.3965 0.7335 -0.0154 90 GLU A C 11 O O . GLU A 2 ? 2.5703 1.5240 1.0394 -0.3991 0.7386 -0.0363 90 GLU A O 12 C CB . GLU A 2 ? 2.7706 1.5419 1.1629 -0.5055 0.8044 -0.0366 90 GLU A CB 13 C CG . GLU A 2 ? 3.0957 1.7345 1.3934 -0.5519 0.8474 -0.0337 90 GLU A CG 14 C CD . GLU A 2 ? 3.0717 1.7653 1.4460 -0.6190 0.8779 -0.0665 90 GLU A CD 15 O OE1 . GLU A 2 ? 2.9189 1.7365 1.4156 -0.6184 0.8533 -0.0851 90 GLU A OE1 16 O OE2 . GLU A 2 ? 3.0688 1.6810 1.3776 -0.6724 0.9269 -0.0753 90 GLU A OE2 17 N N . ALA A 3 ? 2.6268 1.4061 0.9887 -0.3466 0.6855 0.0044 91 ALA A N 18 C CA . ALA A 3 ? 2.4997 1.3517 0.9133 -0.2935 0.6354 0.0037 91 ALA A CA 19 C C . ALA A 3 ? 2.4644 1.4441 1.0155 -0.3047 0.6227 -0.0188 91 ALA A C 20 O O . ALA A 3 ? 2.2914 1.2815 0.8919 -0.3372 0.6311 -0.0256 91 ALA A O 21 C CB . ALA A 3 ? 2.5222 1.2857 0.8721 -0.2415 0.5895 0.0274 91 ALA A CB 22 N N . SER A 4 ? 2.2339 1.3079 0.8414 -0.2761 0.6029 -0.0321 92 SER A N 23 C CA . SER A 4 ? 2.0805 1.2701 0.8096 -0.2761 0.5881 -0.0526 92 SER A CA 24 C C . SER A 4 ? 1.9944 1.1889 0.7391 -0.2249 0.5347 -0.0461 92 SER A C 25 O O . SER A 4 ? 2.0092 1.1962 0.7154 -0.1865 0.5131 -0.0450 92 SER A O 26 C CB . SER A 4 ? 2.1298 1.4302 0.9205 -0.2847 0.6121 -0.0799 92 SER A CB 27 O OG . SER A 4 ? 2.1354 1.4646 0.9218 -0.2375 0.5849 -0.0856 92 SER A OG 28 N N . PHE A 5 ? 1.9090 1.1183 0.7105 -0.2266 0.5143 -0.0444 93 PHE A N 29 C CA . PHE A 5 ? 1.9073 1.1252 0.7318 -0.1842 0.4663 -0.0403 93 PHE A CA 30 C C . PHE A 5 ? 1.7755 1.0492 0.6908 -0.1993 0.4589 -0.0473 93 PHE A C 31 O O . PHE A 5 ? 1.7518 1.0430 0.6991 -0.2407 0.4868 -0.0532 93 PHE A O 32 C CB . PHE A 5 ? 1.8993 1.0102 0.6338 -0.1544 0.4385 -0.0157 93 PHE A CB 33 C CG . PHE A 5 ? 1.9662 0.9957 0.6621 -0.1796 0.4535 -0.0006 93 PHE A CG 34 C CD1 . PHE A 5 ? 2.0968 1.0555 0.7195 -0.2083 0.4922 0.0060 93 PHE A CD1 35 C CD2 . PHE A 5 ? 1.9075 0.9272 0.6361 -0.1753 0.4310 0.0046 93 PHE A CD2 36 C CE1 . PHE A 5 ? 2.1709 1.0457 0.7522 -0.2323 0.5082 0.0152 93 PHE A CE1 37 C CE2 . PHE A 5 ? 1.9757 0.9176 0.6657 -0.1972 0.4454 0.0137 93 PHE A CE2 38 C CZ . PHE A 5 ? 2.1105 0.9766 0.7250 -0.2257 0.4843 0.0181 93 PHE A CZ 39 N N . GLN A 6 ? 1.7944 1.0959 0.7489 -0.1671 0.4214 -0.0487 94 GLN A N 40 C CA . GLN A 6 ? 1.7758 1.1345 0.8150 -0.1778 0.4139 -0.0555 94 GLN A CA 41 C C . GLN A 6 ? 1.7968 1.1007 0.8206 -0.1639 0.3832 -0.0381 94 GLN A C 42 O O . GLN A 6 ? 1.5092 0.7781 0.4988 -0.1263 0.3493 -0.0298 94 GLN A O 43 C CB . GLN A 6 ? 1.7691 1.2175 0.8819 -0.1572 0.4034 -0.0762 94 GLN A CB 44 C CG . GLN A 6 ? 1.8898 1.4034 1.0279 -0.1666 0.4341 -0.0977 94 GLN A CG 45 C CD . GLN A 6 ? 1.8798 1.4973 1.1171 -0.1658 0.4401 -0.1203 94 GLN A CD 46 O OE1 . GLN A 6 ? 1.8801 1.5197 1.1660 -0.1627 0.4238 -0.1186 94 GLN A OE1 47 N NE2 . GLN A 6 ? 1.8843 1.5670 1.1501 -0.1647 0.4634 -0.1423 94 GLN A NE2 48 N N . VAL A 7 ? 1.4977 0.7986 0.5471 -0.1948 0.3955 -0.0361 95 VAL A N 49 C CA . VAL A 7 ? 1.5272 0.7964 0.5813 -0.1843 0.3692 -0.0249 95 VAL A CA 50 C C . VAL A 7 ? 1.4141 0.7714 0.5637 -0.2034 0.3722 -0.0385 95 VAL A C 51 O O . VAL A 7 ? 1.3741 0.8072 0.5774 -0.2266 0.3970 -0.0563 95 VAL A O 52 C CB . VAL A 7 ? 1.6034 0.7744 0.5885 -0.2003 0.3797 -0.0118 95 VAL A CB 53 C CG1 . VAL A 7 ? 1.6729 0.7527 0.5566 -0.1731 0.3742 0.0032 95 VAL A CG1 54 C CG2 . VAL A 7 ? 1.6375 0.8246 0.6418 -0.2547 0.4219 -0.0253 95 VAL A CG2 55 N N . TRP A 8 ? 1.3611 0.7137 0.5316 -0.1906 0.3466 -0.0316 96 TRP A N 56 C CA . TRP A 8 ? 1.2858 0.7207 0.5421 -0.2029 0.3456 -0.0428 96 TRP A CA 57 C C . TRP A 8 ? 1.3188 0.8128 0.6220 -0.2474 0.3790 -0.0604 96 TRP A C 58 O O . TRP A 8 ? 1.3312 0.7788 0.5983 -0.2795 0.4002 -0.0613 96 TRP A O 59 C CB . TRP A 8 ? 1.3245 0.7300 0.5819 -0.1924 0.3202 -0.0315 96 TRP A CB 60 C CG . TRP A 8 ? 1.2651 0.7550 0.6050 -0.1957 0.3141 -0.0406 96 TRP A CG 61 C CD1 . TRP A 8 ? 1.2526 0.7984 0.6457 -0.2277 0.3297 -0.0525 96 TRP A CD1 62 C CD2 . TRP A 8 ? 1.2409 0.7685 0.6156 -0.1651 0.2918 -0.0408 96 TRP A CD2 63 N NE1 . TRP A 8 ? 1.2218 0.8400 0.6798 -0.2153 0.3175 -0.0575 96 TRP A NE1 64 C CE2 . TRP A 8 ? 1.2032 0.8055 0.6486 -0.1777 0.2963 -0.0495 96 TRP A CE2 65 C CE3 . TRP A 8 ? 1.2479 0.7524 0.5986 -0.1290 0.2688 -0.0377 96 TRP A CE3 66 C CZ2 . TRP A 8 ? 1.0805 0.7328 0.5880 -0.1492 0.2698 -0.0504 96 TRP A CZ2 67 C CZ3 . TRP A 8 ? 1.1804 0.7371 0.6003 -0.1067 0.2439 -0.0422 96 TRP A CZ3 68 C CH2 . TRP A 8 ? 1.0755 0.7011 0.5726 -0.1154 0.2440 -0.0458 96 TRP A CH2 69 N N . ASN A 9 ? 1.3283 0.9259 0.7102 -0.2466 0.3837 -0.0776 97 ASN A N 70 C CA . ASN A 9 ? 1.3034 0.9857 0.7466 -0.2818 0.4095 -0.1003 97 ASN A CA 71 C C . ASN A 9 ? 1.2522 0.9703 0.7433 -0.2963 0.3998 -0.1047 97 ASN A C 72 O O . ASN A 9 ? 1.1126 0.8785 0.6493 -0.2715 0.3798 -0.1038 97 ASN A O 73 C CB . ASN A 9 ? 1.2440 1.0251 0.7472 -0.2622 0.4159 -0.1189 97 ASN A CB 74 C CG . ASN A 9 ? 1.2351 1.1322 0.8216 -0.2847 0.4321 -0.1459 97 ASN A CG 75 O OD1 . ASN A 9 ? 1.3046 1.2075 0.8950 -0.3273 0.4496 -0.1563 97 ASN A OD1 76 N ND2 . ASN A 9 ? 1.1568 1.1464 0.8086 -0.2535 0.4258 -0.1607 97 ASN A ND2 77 N N . LYS A 10 ? 1.3779 1.0692 0.8539 -0.3371 0.4157 -0.1117 98 LYS A N 78 C CA . LYS A 10 ? 1.3027 1.0195 0.8141 -0.3562 0.4084 -0.1195 98 LYS A CA 79 C C . LYS A 10 ? 1.1480 1.0010 0.7577 -0.3535 0.4034 -0.1406 98 LYS A C 80 O O . LYS A 10 ? 1.1731 1.0558 0.8152 -0.3562 0.3893 -0.1437 98 LYS A O 81 C CB . LYS A 10 ? 1.4217 1.0978 0.9019 -0.4069 0.4351 -0.1347 98 LYS A CB 82 C CG . LYS A 10 ? 1.5111 1.0548 0.9051 -0.4089 0.4311 -0.1174 98 LYS A CG 83 C CD . LYS A 10 ? 1.6289 1.1305 0.9873 -0.4616 0.4645 -0.1380 98 LYS A CD 84 C CE . LYS A 10 ? 1.6894 1.1786 1.0185 -0.4843 0.4970 -0.1460 98 LYS A CE 85 N NZ . LYS A 10 ? 1.7875 1.2139 1.0651 -0.5363 0.5327 -0.1649 98 LYS A NZ 86 N N . ASP A 11 ? 1.1257 1.0642 0.7812 -0.3458 0.4150 -0.1572 99 ASP A N 87 C CA . ASP A 11 ? 1.0521 1.1261 0.7996 -0.3358 0.4093 -0.1806 99 ASP A CA 88 C C . ASP A 11 ? 0.9531 1.0643 0.7272 -0.2809 0.3921 -0.1731 99 ASP A C 89 O O . ASP A 11 ? 0.9436 1.1581 0.7799 -0.2590 0.3937 -0.1934 99 ASP A O 90 C CB . ASP A 11 ? 1.1184 1.2791 0.9088 -0.3661 0.4347 -0.2138 99 ASP A CB 91 C CG . ASP A 11 ? 1.2696 1.4369 1.0652 -0.4204 0.4470 -0.2349 99 ASP A CG 92 O OD1 . ASP A 11 ? 1.3549 1.5374 1.1713 -0.4224 0.4291 -0.2361 99 ASP A OD1 93 O OD2 . ASP A 11 ? 1.2282 1.3822 1.0030 -0.4618 0.4761 -0.2521 99 ASP A OD2 94 N N . SER A 12 ? 0.9719 0.9945 0.6951 -0.2565 0.3754 -0.1463 100 SER A N 95 C CA . SER A 12 ? 1.0205 1.0584 0.7583 -0.2082 0.3609 -0.1416 100 SER A CA 96 C C . SER A 12 ? 0.9569 1.0792 0.7696 -0.1838 0.3354 -0.1468 100 SER A C 97 O O . SER A 12 ? 0.9038 1.0310 0.7263 -0.2019 0.3260 -0.1435 100 SER A O 98 C CB . SER A 12 ? 1.0050 0.9287 0.6783 -0.1883 0.3381 -0.1131 100 SER A CB 99 O OG . SER A 12 ? 1.0642 0.9154 0.6682 -0.2001 0.3536 -0.1078 100 SER A OG 100 N N . SER A 13 ? 0.9566 1.1413 0.8171 -0.1395 0.3237 -0.1551 101 SER A N 101 C CA . SER A 13 ? 0.9616 1.2176 0.8827 -0.1034 0.2960 -0.1560 101 SER A CA 102 C C . SER A 13 ? 0.8895 1.1023 0.8063 -0.0486 0.2722 -0.1389 101 SER A C 103 O O . SER A 13 ? 0.8628 1.0059 0.7387 -0.0432 0.2774 -0.1326 101 SER A O 104 C CB . SER A 13 ? 1.0019 1.3949 0.9893 -0.1001 0.3098 -0.1905 101 SER A CB 105 O OG . SER A 13 ? 1.0773 1.5078 1.0635 -0.1595 0.3470 -0.2154 101 SER A OG 106 N N . SER A 14 ? 0.8257 1.0769 0.7798 -0.0086 0.2475 -0.1330 102 SER A N 107 C CA . SER A 14 ? 0.8502 1.0571 0.7984 0.0425 0.2301 -0.1188 102 SER A CA 108 C C . SER A 14 ? 0.9047 1.1336 0.8592 0.0684 0.2464 -0.1380 102 SER A C 109 O O . SER A 14 ? 0.8826 1.0425 0.8112 0.0942 0.2422 -0.1303 102 SER A O 110 C CB . SER A 14 ? 0.8782 1.1239 0.8572 0.0822 0.2056 -0.1089 102 SER A CB 111 O OG . SER A 14 ? 0.8793 1.2465 0.9081 0.0947 0.2087 -0.1336 102 SER A OG 112 N N . LYS A 15 ? 0.9098 1.2381 0.8998 0.0598 0.2668 -0.1671 103 LYS A N 113 C CA . LYS A 15 ? 0.9773 1.3379 0.9772 0.0879 0.2838 -0.1891 103 LYS A CA 114 C C . LYS A 15 ? 0.9933 1.2781 0.9405 0.0619 0.3056 -0.1903 103 LYS A C 115 O O . LYS A 15 ? 0.9727 1.2580 0.9152 0.0883 0.3173 -0.2051 103 LYS A O 116 C CB . LYS A 15 ? 1.0360 1.5414 1.0966 0.0892 0.2999 -0.2252 103 LYS A CB 117 C CG . LYS A 15 ? 1.1588 1.7431 1.2674 0.1378 0.2720 -0.2267 103 LYS A CG 118 C CD . LYS A 15 ? 1.2373 1.9572 1.4039 0.1769 0.2799 -0.2645 103 LYS A CD 119 C CE . LYS A 15 ? 1.2589 2.0402 1.4577 0.2417 0.2459 -0.2611 103 LYS A CE 120 N NZ . LYS A 15 ? 1.2997 2.1993 1.5515 0.2729 0.2395 -0.2913 103 LYS A NZ 121 N N . ASN A 16 ? 0.9819 1.1981 0.8841 0.0152 0.3094 -0.1749 104 ASN A N 122 C CA . ASN A 16 ? 0.9358 1.0681 0.7748 -0.0033 0.3231 -0.1713 104 ASN A CA 123 C C . ASN A 16 ? 0.9406 0.9768 0.7467 0.0234 0.2971 -0.1520 104 ASN A C 124 O O . ASN A 16 ? 1.0059 0.9835 0.7662 0.0230 0.3031 -0.1550 104 ASN A O 125 C CB . ASN A 16 ? 0.8316 0.9261 0.6259 -0.0594 0.3389 -0.1636 104 ASN A CB 126 C CG . ASN A 16 ? 0.8761 1.0575 0.6987 -0.0986 0.3711 -0.1863 104 ASN A CG 127 O OD1 . ASN A 16 ? 0.9589 1.1610 0.7959 -0.1284 0.3700 -0.1838 104 ASN A OD1 128 N ND2 . ASN A 16 ? 0.9131 1.1479 0.7466 -0.1004 0.3990 -0.2107 104 ASN A ND2 129 N N . LEU A 17 ? 0.7843 0.8071 0.6123 0.0443 0.2697 -0.1346 105 LEU A N 130 C CA . LEU A 17 ? 0.8371 0.7728 0.6386 0.0587 0.2475 -0.1179 105 LEU A CA 131 C C . LEU A 17 ? 0.9384 0.8472 0.7394 0.0984 0.2469 -0.1276 105 LEU A C 132 O O . LEU A 17 ? 0.8940 0.8562 0.7246 0.1294 0.2560 -0.1415 105 LEU A O 133 C CB . LEU A 17 ? 0.8261 0.7582 0.6499 0.0650 0.2243 -0.0969 105 LEU A CB 134 C CG . LEU A 17 ? 0.8195 0.7512 0.6376 0.0304 0.2171 -0.0836 105 LEU A CG 135 C CD1 . LEU A 17 ? 0.7651 0.7069 0.6105 0.0468 0.1967 -0.0669 105 LEU A CD1 136 C CD2 . LEU A 17 ? 0.8789 0.7344 0.6473 0.0086 0.2112 -0.0760 105 LEU A CD2 137 N N . ILE A 18 ? 0.9874 0.8151 0.7547 0.0980 0.2359 -0.1232 106 ILE A N 138 C CA . ILE A 18 ? 1.0619 0.8408 0.8244 0.1305 0.2326 -0.1303 106 ILE A CA 139 C C . ILE A 18 ? 1.0683 0.8563 0.8624 0.1637 0.2232 -0.1164 106 ILE A C 140 O O . ILE A 18 ? 0.9047 0.6978 0.7112 0.1532 0.2099 -0.0964 106 ILE A O 141 C CB . ILE A 18 ? 1.2396 0.9384 0.9714 0.1139 0.2175 -0.1265 106 ILE A CB 142 C CG1 . ILE A 18 ? 1.4089 1.0917 1.0986 0.0878 0.2203 -0.1380 106 ILE A CG1 143 C CG2 . ILE A 18 ? 1.3883 1.0273 1.1135 0.1390 0.2175 -0.1361 106 ILE A CG2 144 C CD1 . ILE A 18 ? 1.4592 1.0843 1.1251 0.0734 0.2009 -0.1391 106 ILE A CD1 145 N N . PRO A 19 ? 1.1556 0.9397 0.9557 0.2075 0.2301 -0.1265 107 PRO A N 146 C CA . PRO A 19 ? 1.1640 0.9404 0.9783 0.2483 0.2211 -0.1107 107 PRO A CA 147 C C . PRO A 19 ? 1.1842 0.8843 0.9818 0.2347 0.2077 -0.0864 107 PRO A C 148 O O . PRO A 19 ? 1.2104 0.9191 1.0175 0.2517 0.1983 -0.0657 107 PRO A O 149 C CB . PRO A 19 ? 1.2444 0.9854 1.0450 0.2951 0.2321 -0.1275 107 PRO A CB 150 C CG . PRO A 19 ? 1.2779 0.9924 1.0545 0.2701 0.2447 -0.1516 107 PRO A CG 151 C CD . PRO A 19 ? 1.2176 0.9968 1.0038 0.2259 0.2472 -0.1532 107 PRO A CD 152 N N . ARG A 20 ? 1.1255 0.7586 0.8983 0.2037 0.2072 -0.0915 108 ARG A N 153 C CA . ARG A 20 ? 1.0270 0.5997 0.7899 0.1829 0.1979 -0.0748 108 ARG A CA 154 C C . ARG A 20 ? 1.0381 0.6591 0.8205 0.1610 0.1855 -0.0549 108 ARG A C 155 O O . ARG A 20 ? 1.0978 0.7019 0.8825 0.1684 0.1802 -0.0341 108 ARG A O 156 C CB . ARG A 20 ? 1.0525 0.5737 0.7945 0.1492 0.1971 -0.0924 108 ARG A CB 157 C CG . ARG A 20 ? 1.0190 0.4822 0.7559 0.1255 0.1916 -0.0838 108 ARG A CG 158 C CD . ARG A 20 ? 1.0652 0.5156 0.7929 0.0884 0.1840 -0.1054 108 ARG A CD 159 N NE . ARG A 20 ? 1.1911 0.6363 0.9308 0.0600 0.1743 -0.0955 108 ARG A NE 160 C CZ . ARG A 20 ? 1.1477 0.6303 0.8936 0.0354 0.1589 -0.0989 108 ARG A CZ 161 N NH1 . ARG A 20 ? 1.0205 0.5363 0.7526 0.0343 0.1521 -0.1093 108 ARG A NH1 162 N NH2 . ARG A 20 ? 1.1740 0.6572 0.9351 0.0140 0.1519 -0.0918 108 ARG A NH2 163 N N . LEU A 21 ? 0.9186 0.5924 0.7082 0.1346 0.1829 -0.0614 109 LEU A N 164 C CA . LEU A 21 ? 0.8887 0.6017 0.6920 0.1120 0.1726 -0.0464 109 LEU A CA 165 C C . LEU A 21 ? 0.8953 0.6794 0.7256 0.1325 0.1727 -0.0392 109 LEU A C 166 O O . LEU A 21 ? 0.8505 0.6606 0.6928 0.1238 0.1632 -0.0248 109 LEU A O 167 C CB . LEU A 21 ? 0.8335 0.5612 0.6231 0.0783 0.1720 -0.0553 109 LEU A CB 168 C CG . LEU A 21 ? 0.9017 0.5777 0.6615 0.0613 0.1677 -0.0673 109 LEU A CG 169 C CD1 . LEU A 21 ? 1.0301 0.7224 0.7639 0.0415 0.1714 -0.0746 109 LEU A CD1 170 C CD2 . LEU A 21 ? 0.9436 0.5887 0.7053 0.0466 0.1529 -0.0590 109 LEU A CD2 171 N N . GLN A 22 ? 0.9099 0.7328 0.7514 0.1610 0.1827 -0.0529 110 GLN A N 172 C CA . GLN A 22 ? 0.9337 0.8352 0.8052 0.1883 0.1799 -0.0517 110 GLN A CA 173 C C . GLN A 22 ? 0.9279 0.8005 0.7939 0.2211 0.1674 -0.0283 110 GLN A C 174 O O . GLN A 22 ? 0.8013 0.7279 0.6842 0.2254 0.1570 -0.0191 110 GLN A O 175 C CB . GLN A 22 ? 1.0012 0.9528 0.8877 0.2208 0.1925 -0.0745 110 GLN A CB 176 C CG . GLN A 22 ? 0.9935 1.0400 0.9072 0.1953 0.2052 -0.0966 110 GLN A CG 177 C CD . GLN A 22 ? 1.0848 1.1812 1.0137 0.2249 0.2217 -0.1236 110 GLN A CD 178 O OE1 . GLN A 22 ? 1.0904 1.1425 1.0056 0.2680 0.2219 -0.1254 110 GLN A OE1 179 N NE2 . GLN A 22 ? 1.1143 1.3007 1.0697 0.2003 0.2386 -0.1467 110 GLN A NE2 180 N N . LYS A 23 ? 0.9963 0.7801 0.8333 0.2427 0.1704 -0.0196 111 LYS A N 181 C CA . LYS A 23 ? 1.0756 0.8124 0.8924 0.2739 0.1642 0.0056 111 LYS A CA 182 C C . LYS A 23 ? 1.0787 0.7995 0.8919 0.2379 0.1562 0.0250 111 LYS A C 183 O O . LYS A 23 ? 1.1096 0.8463 0.9190 0.2555 0.1477 0.0441 111 LYS A O 184 C CB . LYS A 23 ? 1.1684 0.7962 0.9468 0.2972 0.1757 0.0087 111 LYS A CB 185 C CG . LYS A 23 ? 1.3456 0.9827 1.1226 0.3439 0.1835 -0.0102 111 LYS A CG 186 C CD . LYS A 23 ? 1.4669 0.9819 1.2001 0.3614 0.1976 -0.0112 111 LYS A CD 187 C CE . LYS A 23 ? 1.5778 1.1076 1.3128 0.3996 0.2068 -0.0377 111 LYS A CE 188 N NZ . LYS A 23 ? 1.7165 1.1219 1.4031 0.4286 0.2212 -0.0398 111 LYS A NZ 189 N N . ILE A 24 ? 1.0161 0.7111 0.8290 0.1908 0.1582 0.0179 112 ILE A N 190 C CA . ILE A 24 ? 0.9658 0.6555 0.7801 0.1559 0.1510 0.0301 112 ILE A CA 191 C C . ILE A 24 ? 0.9043 0.6770 0.7412 0.1487 0.1403 0.0335 112 ILE A C 192 O O . ILE A 24 ? 0.8715 0.6482 0.7053 0.1488 0.1337 0.0506 112 ILE A O 193 C CB . ILE A 24 ? 0.8711 0.5324 0.6825 0.1156 0.1521 0.0153 112 ILE A CB 194 C CG1 . ILE A 24 ? 0.9360 0.5146 0.7264 0.1166 0.1623 0.0090 112 ILE A CG1 195 C CG2 . ILE A 24 ? 0.8021 0.4740 0.6196 0.0837 0.1430 0.0226 112 ILE A CG2 196 C CD1 . ILE A 24 ? 0.9669 0.5252 0.7554 0.0800 0.1597 -0.0098 112 ILE A CD1 197 N N . TRP A 25 ? 0.8329 0.6681 0.6889 0.1390 0.1415 0.0154 113 TRP A N 198 C CA . TRP A 25 ? 0.7821 0.7000 0.6612 0.1295 0.1354 0.0114 113 TRP A CA 199 C C . TRP A 25 ? 0.8058 0.7682 0.6939 0.1702 0.1264 0.0211 113 TRP A C 200 O O . TRP A 25 ? 0.7476 0.7364 0.6382 0.1656 0.1162 0.0313 113 TRP A O 201 C CB . TRP A 25 ? 0.8562 0.8283 0.7511 0.1138 0.1462 -0.0131 113 TRP A CB 202 C CG . TRP A 25 ? 0.7729 0.8421 0.6981 0.1057 0.1455 -0.0261 113 TRP A CG 203 C CD1 . TRP A 25 ? 0.7318 0.8250 0.6608 0.0702 0.1428 -0.0277 113 TRP A CD1 204 C CD2 . TRP A 25 ? 0.7558 0.9142 0.7131 0.1322 0.1485 -0.0445 113 TRP A CD2 205 N NE1 . TRP A 25 ? 0.6964 0.8860 0.6581 0.0671 0.1452 -0.0472 113 TRP A NE1 206 C CE2 . TRP A 25 ? 0.7144 0.9534 0.6975 0.1054 0.1477 -0.0588 113 TRP A CE2 207 C CE3 . TRP A 25 ? 0.8725 1.0532 0.8398 0.1778 0.1516 -0.0533 113 TRP A CE3 208 C CZ2 . TRP A 25 ? 0.7471 1.1002 0.7720 0.1194 0.1492 -0.0844 113 TRP A CZ2 209 C CZ3 . TRP A 25 ? 0.8653 1.1600 0.8731 0.1987 0.1518 -0.0768 113 TRP A CZ3 210 C CH2 . TRP A 25 ? 0.7667 1.1518 0.8058 0.1678 0.1502 -0.0934 113 TRP A CH2 211 N N . LYS A 26 ? 0.8790 0.8476 0.7671 0.2144 0.1293 0.0171 114 LYS A N 212 C CA . LYS A 26 ? 0.9682 0.9727 0.8551 0.2669 0.1183 0.0268 114 LYS A CA 213 C C . LYS A 26 ? 1.0086 0.9492 0.8602 0.2765 0.1117 0.0578 114 LYS A C 214 O O . LYS A 26 ? 0.9982 0.9870 0.8497 0.2956 0.0984 0.0666 114 LYS A O 215 C CB . LYS A 26 ? 1.0607 1.0534 0.9405 0.3200 0.1235 0.0201 114 LYS A CB 216 C CG . LYS A 26 ? 1.1970 1.2963 1.1197 0.3286 0.1271 -0.0128 114 LYS A CG 217 C CD . LYS A 26 ? 1.3326 1.3965 1.2465 0.3596 0.1403 -0.0257 114 LYS A CD 218 C CE . LYS A 26 ? 1.2567 1.4116 1.2112 0.3404 0.1535 -0.0615 114 LYS A CE 219 N NZ . LYS A 26 ? 1.2172 1.3137 1.1544 0.3441 0.1710 -0.0737 114 LYS A NZ 220 N N . ASN A 27 ? 1.0883 0.9247 0.9097 0.2605 0.1225 0.0717 115 ASN A N 221 C CA . ASN A 27 ? 1.1334 0.9009 0.9175 0.2644 0.1237 0.1002 115 ASN A CA 222 C C . ASN A 27 ? 1.0046 0.8019 0.7983 0.2265 0.1169 0.1059 115 ASN A C 223 O O . ASN A 27 ? 1.0486 0.8308 0.8168 0.2397 0.1139 0.1274 115 ASN A O 224 C CB . ASN A 27 ? 1.2372 0.8889 0.9897 0.2525 0.1415 0.1075 115 ASN A CB 225 C CG . ASN A 27 ? 1.4897 1.0900 1.2171 0.2999 0.1497 0.1069 115 ASN A CG 226 O OD1 . ASN A 27 ? 1.5431 1.1690 1.2578 0.3556 0.1418 0.1150 115 ASN A OD1 227 N ND2 . ASN A 27 ? 1.5778 1.1081 1.2967 0.2814 0.1642 0.0946 115 ASN A ND2 228 N N . TYR A 28 ? 0.7779 0.6117 0.6013 0.1826 0.1153 0.0874 116 TYR A N 229 C CA . TYR A 28 ? 0.7525 0.6144 0.5833 0.1513 0.1085 0.0899 116 TYR A CA 230 C C . TYR A 28 ? 0.8332 0.7841 0.6789 0.1669 0.0950 0.0855 116 TYR A C 231 O O . TYR A 28 ? 0.8769 0.8453 0.7162 0.1589 0.0882 0.0938 116 TYR A O 232 C CB . TYR A 28 ? 0.7646 0.6290 0.6123 0.1068 0.1103 0.0722 116 TYR A CB 233 C CG . TYR A 28 ? 0.8411 0.6342 0.6762 0.0841 0.1175 0.0753 116 TYR A CG 234 C CD1 . TYR A 28 ? 0.8464 0.6101 0.6696 0.0745 0.1198 0.0898 116 TYR A CD1 235 C CD2 . TYR A 28 ? 0.7860 0.5497 0.6223 0.0705 0.1225 0.0600 116 TYR A CD2 236 C CE1 . TYR A 28 ? 0.8633 0.5775 0.6835 0.0499 0.1273 0.0859 116 TYR A CE1 237 C CE2 . TYR A 28 ? 0.7534 0.4665 0.5834 0.0493 0.1264 0.0564 116 TYR A CE2 238 C CZ . TYR A 28 ? 0.8221 0.5146 0.6479 0.0380 0.1290 0.0677 116 TYR A CZ 239 O OH . TYR A 28 ? 0.8728 0.5301 0.7005 0.0134 0.1339 0.0576 116 TYR A OH 240 N N . LEU A 29 ? 0.7437 0.7573 0.6114 0.1882 0.0917 0.0685 117 LEU A N 241 C CA . LEU A 29 ? 0.7263 0.8391 0.6142 0.2064 0.0781 0.0572 117 LEU A CA 242 C C . LEU A 29 ? 0.8676 0.9669 0.7219 0.2528 0.0675 0.0821 117 LEU A C 243 O O . LEU A 29 ? 0.9220 1.0765 0.7762 0.2568 0.0543 0.0821 117 LEU A O 244 C CB . LEU A 29 ? 0.6411 0.8237 0.5598 0.2277 0.0792 0.0328 117 LEU A CB 245 C CG . LEU A 29 ? 0.7910 1.0556 0.7504 0.1845 0.0842 0.0002 117 LEU A CG 246 C CD1 . LEU A 29 ? 0.8929 1.0937 0.8414 0.1292 0.0966 0.0010 117 LEU A CD1 247 C CD2 . LEU A 29 ? 0.7705 1.0961 0.7600 0.2006 0.0924 -0.0252 117 LEU A CD2 248 N N . SER A 30 ? 0.9048 0.9219 0.7234 0.2870 0.0750 0.1031 118 SER A N 249 C CA . SER A 30 ? 0.9522 0.9372 0.7232 0.3401 0.0686 0.1303 118 SER A CA 250 C C . SER A 30 ? 1.0332 0.9613 0.7678 0.3188 0.0736 0.1554 118 SER A C 251 O O . SER A 30 ? 1.1021 1.0676 0.8168 0.3401 0.0608 0.1656 118 SER A O 252 C CB . SER A 30 ? 1.0309 0.9265 0.7663 0.3802 0.0804 0.1443 118 SER A CB 253 O OG . SER A 30 ? 1.1446 1.0507 0.8443 0.4518 0.0678 0.1588 118 SER A OG 254 N N . MET A 31 ? 1.0594 0.9032 0.7850 0.2780 0.0923 0.1628 119 MET A N 255 C CA . MET A 31 ? 1.1569 0.9624 0.8580 0.2509 0.0998 0.1803 119 MET A CA 256 C C . MET A 31 ? 1.1649 1.0471 0.9068 0.2100 0.0896 0.1594 119 MET A C 257 O O . MET A 31 ? 1.2438 1.1139 1.0105 0.1663 0.0963 0.1458 119 MET A O 258 C CB . MET A 31 ? 1.1955 0.8943 0.8754 0.2215 0.1244 0.1913 119 MET A CB 259 C CG . MET A 31 ? 1.1741 0.8590 0.8895 0.1889 0.1306 0.1681 119 MET A CG 260 S SD . MET A 31 ? 2.0462 1.6522 1.7554 0.1369 0.1530 0.1690 119 MET A SD 261 C CE . MET A 31 ? 1.0449 0.7274 0.7909 0.0981 0.1408 0.1546 119 MET A CE 262 N N . ASN A 32 ? 1.1272 1.0882 0.8726 0.2275 0.0724 0.1549 120 ASN A N 263 C CA . ASN A 32 ? 1.0328 1.0625 0.8109 0.1909 0.0636 0.1328 120 ASN A CA 264 C C . ASN A 32 ? 1.0101 1.0002 0.7684 0.1629 0.0721 0.1448 120 ASN A C 265 O O . ASN A 32 ? 0.9307 0.9507 0.6693 0.1718 0.0648 0.1509 120 ASN A O 266 C CB . ASN A 32 ? 1.0909 1.2196 0.8773 0.2172 0.0430 0.1200 120 ASN A CB 267 C CG . ASN A 32 ? 1.1622 1.3701 0.9974 0.1806 0.0372 0.0839 120 ASN A CG 268 O OD1 . ASN A 32 ? 1.0968 1.3155 0.9373 0.1448 0.0372 0.0738 120 ASN A OD1 269 N ND2 . ASN A 32 ? 1.2547 1.5141 1.1228 0.1881 0.0353 0.0629 120 ASN A ND2 270 N N . LYS A 33 ? 0.9027 0.8331 0.6675 0.1304 0.0870 0.1449 121 LYS A N 271 C CA . LYS A 33 ? 0.9697 0.8602 0.7181 0.1065 0.0993 0.1554 121 LYS A CA 272 C C . LYS A 33 ? 0.8502 0.7946 0.6046 0.0911 0.0903 0.1448 121 LYS A C 273 O O . LYS A 33 ? 0.8469 0.7811 0.5743 0.0914 0.0968 0.1582 121 LYS A O 274 C CB . LYS A 33 ? 0.9743 0.8201 0.7433 0.0725 0.1112 0.1451 121 LYS A CB 275 C CG . LYS A 33 ? 0.9344 0.7420 0.6916 0.0491 0.1278 0.1528 121 LYS A CG 276 C CD . LYS A 33 ? 0.9603 0.7400 0.7433 0.0186 0.1356 0.1362 121 LYS A CD 277 C CE . LYS A 33 ? 0.9909 0.7472 0.7697 -0.0067 0.1545 0.1385 121 LYS A CE 278 N NZ . LYS A 33 ? 0.8684 0.6544 0.6830 -0.0338 0.1496 0.1123 121 LYS A NZ 279 N N . TYR A 34 ? 0.7455 0.7420 0.5310 0.0759 0.0782 0.1196 122 TYR A N 280 C CA . TYR A 34 ? 0.6678 0.7029 0.4583 0.0564 0.0718 0.1044 122 TYR A CA 281 C C . TYR A 34 ? 0.6367 0.7422 0.4223 0.0745 0.0566 0.0966 122 TYR A C 282 O O . TYR A 34 ? 0.6564 0.8002 0.4473 0.0573 0.0502 0.0778 122 TYR A O 283 C CB . TYR A 34 ? 0.5879 0.6189 0.4039 0.0251 0.0716 0.0812 122 TYR A CB 284 C CG . TYR A 34 ? 0.6730 0.6466 0.4922 0.0128 0.0822 0.0862 122 TYR A CG 285 C CD1 . TYR A 34 ? 0.6695 0.6224 0.4818 0.0034 0.0902 0.0912 122 TYR A CD1 286 C CD2 . TYR A 34 ? 0.6370 0.5843 0.4676 0.0107 0.0848 0.0827 122 TYR A CD2 287 C CE1 . TYR A 34 ? 0.7475 0.6623 0.5699 -0.0094 0.0988 0.0892 122 TYR A CE1 288 C CE2 . TYR A 34 ? 0.6614 0.5650 0.4958 -0.0002 0.0920 0.0825 122 TYR A CE2 289 C CZ . TYR A 34 ? 0.6913 0.5821 0.5245 -0.0108 0.0980 0.0842 122 TYR A CZ 290 O OH . TYR A 34 ? 0.7281 0.5885 0.5719 -0.0231 0.1038 0.0774 122 TYR A OH 291 N N . LYS A 35 ? 0.6635 0.7855 0.4367 0.1119 0.0503 0.1091 123 LYS A N 292 C CA . LYS A 35 ? 0.7847 0.9805 0.5480 0.1393 0.0327 0.1030 123 LYS A CA 293 C C . LYS A 35 ? 0.7097 0.9817 0.5140 0.1135 0.0226 0.0648 123 LYS A C 294 O O . LYS A 35 ? 0.7290 1.0549 0.5333 0.1039 0.0128 0.0465 123 LYS A O 295 C CB . LYS A 35 ? 0.9096 1.1012 0.6331 0.1449 0.0327 0.1164 123 LYS A CB 296 C CG . LYS A 35 ? 1.0600 1.1759 0.7316 0.1699 0.0473 0.1555 123 LYS A CG 297 C CD . LYS A 35 ? 1.1773 1.2881 0.8111 0.1647 0.0532 0.1652 123 LYS A CD 298 C CE . LYS A 35 ? 1.3076 1.3329 0.8850 0.1778 0.0765 0.2036 123 LYS A CE 299 N NZ . LYS A 35 ? 1.2869 1.3022 0.8412 0.1550 0.0916 0.2071 123 LYS A NZ 300 N N . VAL A 36 ? 0.7044 0.9751 0.5404 0.0985 0.0282 0.0514 124 VAL A N 301 C CA . VAL A 36 ? 0.5075 0.8402 0.3790 0.0682 0.0259 0.0153 124 VAL A CA 302 C C . VAL A 36 ? 0.6752 1.1090 0.5662 0.0966 0.0100 -0.0024 124 VAL A C 303 O O . VAL A 36 ? 0.7369 1.1787 0.6238 0.1406 0.0045 0.0120 124 VAL A O 304 C CB . VAL A 36 ? 0.6823 0.9737 0.5725 0.0444 0.0407 0.0097 124 VAL A CB 305 C CG1 . VAL A 36 ? 0.7201 1.0647 0.6394 0.0071 0.0455 -0.0268 124 VAL A CG1 306 C CG2 . VAL A 36 ? 0.5757 0.7766 0.4465 0.0245 0.0518 0.0252 124 VAL A CG2 307 N N . SER A 37 ? 0.6943 1.2065 0.6050 0.0731 0.0023 -0.0363 125 SER A N 308 C CA . SER A 37 ? 0.7508 1.3805 0.6972 0.0860 -0.0109 -0.0681 125 SER A CA 309 C C . SER A 37 ? 0.7264 1.3944 0.7085 0.0244 0.0019 -0.1106 125 SER A C 310 O O . SER A 37 ? 0.7147 1.4051 0.6939 -0.0069 -0.0001 -0.1330 125 SER A O 311 C CB . SER A 37 ? 0.8192 1.5239 0.7489 0.1234 -0.0361 -0.0718 125 SER A CB 312 O OG . SER A 37 ? 0.8910 1.5623 0.7818 0.1866 -0.0458 -0.0329 125 SER A OG 313 N N . TYR A 38 ? 0.6608 1.3261 0.6699 0.0042 0.0186 -0.1218 126 TYR A N 314 C CA . TYR A 38 ? 0.7064 1.3912 0.7385 -0.0591 0.0375 -0.1595 126 TYR A CA 315 C C . TYR A 38 ? 0.7563 1.5794 0.8284 -0.0719 0.0268 -0.2073 126 TYR A C 316 O O . TYR A 38 ? 0.7078 1.6347 0.8180 -0.0435 0.0166 -0.2251 126 TYR A O 317 C CB . TYR A 38 ? 0.6245 1.2783 0.6709 -0.0787 0.0609 -0.1615 126 TYR A CB 318 C CG . TYR A 38 ? 0.5954 1.2524 0.6525 -0.1476 0.0865 -0.1971 126 TYR A CG 319 C CD1 . TYR A 38 ? 0.6756 1.2333 0.6929 -0.1876 0.1005 -0.1921 126 TYR A CD1 320 C CD2 . TYR A 38 ? 0.6604 1.4173 0.7638 -0.1723 0.0990 -0.2372 126 TYR A CD2 321 C CE1 . TYR A 38 ? 0.7372 1.2777 0.7504 -0.2507 0.1277 -0.2223 126 TYR A CE1 322 C CE2 . TYR A 38 ? 0.7003 1.4493 0.8065 -0.2427 0.1291 -0.2701 126 TYR A CE2 323 C CZ . TYR A 38 ? 0.7002 1.3318 0.7558 -0.2815 0.1440 -0.2603 126 TYR A CZ 324 O OH . TYR A 38 ? 0.7524 1.3568 0.7974 -0.3510 0.1773 -0.2904 126 TYR A OH 325 N N . LYS A 39 ? 0.8321 1.6597 0.8959 -0.1136 0.0287 -0.2315 127 LYS A N 326 C CA . LYS A 39 ? 0.8898 1.8498 0.9914 -0.1343 0.0189 -0.2837 127 LYS A CA 327 C C . LYS A 39 ? 0.8876 1.8480 1.0075 -0.2162 0.0497 -0.3279 127 LYS A C 328 O O . LYS A 39 ? 0.9678 2.0163 1.1124 -0.2516 0.0475 -0.3763 127 LYS A O 329 C CB . LYS A 39 ? 0.9269 1.9068 1.0015 -0.1145 -0.0056 -0.2834 127 LYS A CB 330 C CG . LYS A 39 ? 0.9922 2.0885 1.0788 -0.0488 -0.0407 -0.2855 127 LYS A CG 331 C CD . LYS A 39 ? 1.0208 2.0920 1.0994 0.0165 -0.0481 -0.2427 127 LYS A CD 332 C CE . LYS A 39 ? 1.0148 2.1461 1.0694 0.0933 -0.0830 -0.2263 127 LYS A CE 333 N NZ . LYS A 39 ? 0.9664 2.0001 0.9552 0.1115 -0.0872 -0.1849 127 LYS A NZ 334 N N . GLY A 40 ? 0.8089 1.6674 0.9114 -0.2467 0.0795 -0.3121 128 GLY A N 335 C CA . GLY A 40 ? 0.7601 1.5874 0.8615 -0.3240 0.1150 -0.3457 128 GLY A CA 336 C C . GLY A 40 ? 0.6878 1.6166 0.8439 -0.3542 0.1348 -0.3846 128 GLY A C 337 O O . GLY A 40 ? 0.6512 1.6788 0.8496 -0.3076 0.1180 -0.3851 128 GLY A O 338 N N . PRO A 41 ? 0.7062 1.5899 0.8470 -0.4245 0.1713 -0.4142 129 PRO A N 339 C CA . PRO A 41 ? 0.8867 1.8201 1.0454 -0.4539 0.1931 -0.4531 129 PRO A CA 340 C C . PRO A 41 ? 1.0149 2.0305 1.2184 -0.4152 0.1853 -0.4507 129 PRO A C 341 O O . PRO A 41 ? 1.0927 2.2025 1.3285 -0.4243 0.1887 -0.4914 129 PRO A O 342 C CB . PRO A 41 ? 0.8989 1.6818 0.9949 -0.5119 0.2355 -0.4479 129 PRO A CB 343 C CG . PRO A 41 ? 0.7992 1.4911 0.8496 -0.5232 0.2331 -0.4336 129 PRO A CG 344 C CD . PRO A 41 ? 0.6840 1.4178 0.7598 -0.4681 0.1939 -0.4022 129 PRO A CD 345 N N . GLY A 42 ? 0.9802 1.9623 1.1841 -0.3711 0.1775 -0.4062 130 GLY A N 346 C CA . GLY A 42 ? 0.9801 2.0425 1.2246 -0.3211 0.1665 -0.4027 130 GLY A CA 347 C C . GLY A 42 ? 1.1010 2.0771 1.3243 -0.3300 0.1948 -0.3795 130 GLY A C 348 O O . GLY A 42 ? 1.1939 2.0832 1.3807 -0.3870 0.2262 -0.3868 130 GLY A O 349 N N . PRO A 43 ? 1.1390 2.1329 1.3774 -0.2693 0.1840 -0.3518 131 PRO A N 350 C CA . PRO A 43 ? 1.1444 2.0523 1.3565 -0.2649 0.2073 -0.3248 131 PRO A CA 351 C C . PRO A 43 ? 1.1752 2.0728 1.3859 -0.3137 0.2359 -0.3510 131 PRO A C 352 O O . PRO A 43 ? 1.1825 2.1865 1.4393 -0.3053 0.2315 -0.3833 131 PRO A O 353 C CB . PRO A 43 ? 1.1356 2.1016 1.3749 -0.1835 0.1822 -0.3082 131 PRO A CB 354 C CG . PRO A 43 ? 1.1498 2.1612 1.3956 -0.1387 0.1422 -0.3009 131 PRO A CG 355 C CD . PRO A 43 ? 1.1358 2.2316 1.4099 -0.1936 0.1466 -0.3460 131 PRO A CD 356 N N . GLY A 44 ? 1.1716 1.9387 1.3235 -0.3610 0.2646 -0.3368 132 GLY A N 357 C CA . GLY A 44 ? 1.1697 1.9075 1.3058 -0.4054 0.2953 -0.3558 132 GLY A CA 358 C C . GLY A 44 ? 1.1589 1.8740 1.2727 -0.4718 0.3141 -0.3895 132 GLY A C 359 O O . GLY A 44 ? 1.2066 2.0320 1.3644 -0.4870 0.3088 -0.4331 132 GLY A O 360 N N . ILE A 45 ? 1.1066 1.6746 1.1453 -0.5071 0.3363 -0.3708 133 ILE A N 361 C CA . ILE A 45 ? 1.1306 1.6479 1.1294 -0.5683 0.3617 -0.4003 133 ILE A CA 362 C C . ILE A 45 ? 1.2331 1.5916 1.1457 -0.5954 0.3936 -0.3789 133 ILE A C 363 O O . ILE A 45 ? 1.2285 1.4823 1.0932 -0.5680 0.3878 -0.3353 133 ILE A O 364 C CB . ILE A 45 ? 1.0381 1.5432 1.0256 -0.5761 0.3480 -0.4057 133 ILE A CB 365 C CG1 . ILE A 45 ? 0.9623 1.6285 1.0207 -0.5775 0.3310 -0.4521 133 ILE A CG1 366 C CG2 . ILE A 45 ? 1.0952 1.4650 1.0006 -0.6251 0.3790 -0.4102 133 ILE A CG2 367 C CD1 . ILE A 45 ? 1.0081 1.6851 1.0656 -0.5730 0.3113 -0.4553 133 ILE A CD1 368 N N . LYS A 46 ? 1.2398 1.5824 1.1290 -0.6467 0.4272 -0.4109 134 LYS A N 369 C CA . LYS A 46 ? 1.3240 1.5182 1.1247 -0.6709 0.4593 -0.3933 134 LYS A CA 370 C C . LYS A 46 ? 1.4195 1.4877 1.1378 -0.7030 0.4787 -0.3945 134 LYS A C 371 O O . LYS A 46 ? 1.2940 1.4017 1.0221 -0.7400 0.4908 -0.4321 134 LYS A O 372 C CB . LYS A 46 ? 1.3364 1.5722 1.1488 -0.7053 0.4902 -0.4225 134 LYS A CB 373 C CG . LYS A 46 ? 1.2845 1.5967 1.1491 -0.6672 0.4786 -0.4097 134 LYS A CG 374 C CD . LYS A 46 ? 1.4021 1.7104 1.2514 -0.7028 0.5155 -0.4291 134 LYS A CD 375 C CE . LYS A 46 ? 1.3887 1.7796 1.2904 -0.6643 0.5070 -0.4206 134 LYS A CE 376 N NZ . LYS A 46 ? 1.5390 1.9515 1.4377 -0.7032 0.5441 -0.4477 134 LYS A NZ 377 N N . PHE A 47 ? 1.4787 1.3972 1.1133 -0.6840 0.4816 -0.3536 135 PHE A N 378 C CA . PHE A 47 ? 1.5792 1.3574 1.1198 -0.7018 0.5007 -0.3468 135 PHE A CA 379 C C . PHE A 47 ? 1.6866 1.3306 1.1353 -0.7086 0.5290 -0.3281 135 PHE A C 380 O O . PHE A 47 ? 1.6578 1.2860 1.1034 -0.6777 0.5192 -0.3011 135 PHE A O 381 C CB . PHE A 47 ? 1.5307 1.2502 1.0490 -0.6561 0.4692 -0.3104 135 PHE A CB 382 C CG . PHE A 47 ? 1.4642 1.2517 1.0252 -0.6618 0.4540 -0.3292 135 PHE A CG 383 C CD1 . PHE A 47 ? 1.3054 1.2276 0.9582 -0.6389 0.4216 -0.3342 135 PHE A CD1 384 C CD2 . PHE A 47 ? 1.5991 1.3132 1.1039 -0.6870 0.4727 -0.3402 135 PHE A CD2 385 C CE1 . PHE A 47 ? 1.3298 1.3153 1.0180 -0.6424 0.4064 -0.3517 135 PHE A CE1 386 C CE2 . PHE A 47 ? 1.3471 1.1243 0.8904 -0.6921 0.4593 -0.3575 135 PHE A CE2 387 C CZ . PHE A 47 ? 1.4363 1.3505 1.0713 -0.6701 0.4252 -0.3640 135 PHE A CZ 388 N N . SER A 48 ? 1.7656 1.3107 1.1349 -0.7470 0.5649 -0.3418 136 SER A N 389 C CA . SER A 48 ? 1.8813 1.2738 1.1431 -0.7435 0.5881 -0.3174 136 SER A CA 390 C C . SER A 48 ? 1.9386 1.2321 1.1457 -0.6844 0.5580 -0.2720 136 SER A C 391 O O . SER A 48 ? 1.9475 1.2644 1.1795 -0.6647 0.5335 -0.2670 136 SER A O 392 C CB . SER A 48 ? 2.0159 1.3220 1.2005 -0.7977 0.6356 -0.3430 136 SER A CB 393 O OG . SER A 48 ? 2.0110 1.2918 1.1788 -0.8002 0.6322 -0.3480 136 SER A OG 394 N N . ALA A 49 ? 1.9904 1.1791 1.1239 -0.6551 0.5590 -0.2410 137 ALA A N 395 C CA . ALA A 49 ? 2.0325 1.1315 1.1110 -0.5959 0.5294 -0.2018 137 ALA A CA 396 C C . ALA A 49 ? 2.2261 1.2371 1.2377 -0.5978 0.5374 -0.2018 137 ALA A C 397 O O . ALA A 49 ? 2.2382 1.2378 1.2509 -0.5572 0.5068 -0.1822 137 ALA A O 398 C CB . ALA A 49 ? 1.8534 0.8544 0.8554 -0.5667 0.5322 -0.1745 137 ALA A CB 399 N N . GLU A 50 ? 2.3294 1.2795 1.2830 -0.6464 0.5805 -0.2245 138 GLU A N 400 C CA . GLU A 50 ? 2.3254 1.1950 1.2165 -0.6539 0.5935 -0.2268 138 GLU A CA 401 C C . GLU A 50 ? 2.2034 1.1797 1.1809 -0.6617 0.5739 -0.2431 138 GLU A C 402 O O . GLU A 50 ? 2.2215 1.1598 1.1790 -0.6300 0.5538 -0.2253 138 GLU A O 403 C CB . GLU A 50 ? 2.4985 1.2897 1.3160 -0.7132 0.6490 -0.2524 138 GLU A CB 404 C CG . GLU A 50 ? 2.6550 1.3048 1.3578 -0.7033 0.6726 -0.2330 138 GLU A CG 405 C CD . GLU A 50 ? 2.8934 1.4244 1.4941 -0.7520 0.7267 -0.2504 138 GLU A CD 406 O OE1 . GLU A 50 ? 2.9371 1.4628 1.5349 -0.7748 0.7378 -0.2658 138 GLU A OE1 407 O OE2 . GLU A 50 ? 3.0047 1.4446 1.5260 -0.7686 0.7597 -0.2486 138 GLU A OE2 408 N N . ALA A 51 ? 2.1068 1.2198 1.1802 -0.7014 0.5785 -0.2775 139 ALA A N 409 C CA . ALA A 51 ? 1.8096 1.0340 0.9664 -0.7111 0.5608 -0.2977 139 ALA A CA 410 C C . ALA A 51 ? 1.9452 1.2299 1.1622 -0.6560 0.5108 -0.2710 139 ALA A C 411 O O . ALA A 51 ? 1.9786 1.2880 1.2200 -0.6445 0.4921 -0.2697 139 ALA A O 412 C CB . ALA A 51 ? 1.7793 1.1420 1.0204 -0.7636 0.5772 -0.3454 139 ALA A CB 413 N N . LEU A 52 ? 1.8294 1.1374 1.0705 -0.6245 0.4910 -0.2507 140 LEU A N 414 C CA . LEU A 52 ? 1.6518 1.0177 0.9501 -0.5768 0.4478 -0.2271 140 LEU A CA 415 C C . LEU A 52 ? 1.6582 0.9139 0.8873 -0.5296 0.4294 -0.1921 140 LEU A C 416 O O . LEU A 52 ? 1.5462 0.8335 0.8095 -0.5014 0.3999 -0.1803 140 LEU A O 417 C CB . LEU A 52 ? 1.5829 0.9996 0.9220 -0.5581 0.4362 -0.2153 140 LEU A CB 418 C CG . LEU A 52 ? 1.4805 0.9407 0.8663 -0.5074 0.3968 -0.1866 140 LEU A CG 419 C CD1 . LEU A 52 ? 1.3191 0.8885 0.7862 -0.5066 0.3747 -0.1979 140 LEU A CD1 420 C CD2 . LEU A 52 ? 1.4321 0.9419 0.8526 -0.4990 0.3965 -0.1806 140 LEU A CD2 421 N N . ARG A 53 ? 1.7472 0.8753 0.8773 -0.5194 0.4463 -0.1769 141 ARG A N 422 C CA . ARG A 53 ? 1.8526 0.8797 0.9128 -0.4704 0.4278 -0.1468 141 ARG A CA 423 C C . ARG A 53 ? 1.8178 0.8351 0.8748 -0.4801 0.4285 -0.1550 141 ARG A C 424 O O . ARG A 53 ? 1.7384 0.7369 0.7919 -0.4387 0.4000 -0.1354 141 ARG A O 425 C CB . ARG A 53 ? 2.0812 0.9734 1.0286 -0.4573 0.4472 -0.1324 141 ARG A CB 426 C CG . ARG A 53 ? 2.0861 0.9679 1.0250 -0.4188 0.4291 -0.1110 141 ARG A CG 427 C CD . ARG A 53 ? 2.2436 0.9863 1.0629 -0.3919 0.4397 -0.0935 141 ARG A CD 428 N NE . ARG A 53 ? 2.3459 1.0261 1.1059 -0.4392 0.4859 -0.1099 141 ARG A NE 429 C CZ . ARG A 53 ? 2.3072 0.9886 1.0628 -0.4546 0.5016 -0.1125 141 ARG A CZ 430 N NH1 . ARG A 53 ? 2.0898 0.8328 0.8977 -0.4256 0.4746 -0.0993 141 ARG A NH1 431 N NH2 . ARG A 53 ? 2.4681 1.0877 1.1656 -0.5008 0.5465 -0.1287 141 ARG A NH2 432 N N . CYS A 54 ? 1.8807 0.9164 0.9432 -0.5363 0.4613 -0.1865 142 CYS A N 433 C CA . CYS A 54 ? 1.8521 0.8766 0.9101 -0.5549 0.4683 -0.1996 142 CYS A CA 434 C C . CYS A 54 ? 1.7195 0.8818 0.8867 -0.5616 0.4431 -0.2160 142 CYS A C 435 O O . CYS A 54 ? 1.7162 0.8762 0.8926 -0.5506 0.4280 -0.2148 142 CYS A O 436 C CB . CYS A 54 ? 1.9011 0.8639 0.8997 -0.6113 0.5178 -0.2258 142 CYS A CB 437 S SG . CYS A 54 ? 2.0619 1.1215 1.1241 -0.6836 0.5445 -0.2776 142 CYS A SG 438 N N . HIS A 55 ? 1.5908 0.8703 0.8382 -0.5736 0.4353 -0.2302 143 HIS A N 439 C CA . HIS A 55 ? 1.4820 0.8926 0.8277 -0.5700 0.4068 -0.2420 143 HIS A CA 440 C C . HIS A 55 ? 1.4822 0.8805 0.8379 -0.5130 0.3674 -0.2074 143 HIS A C 441 O O . HIS A 55 ? 1.3806 0.8536 0.7959 -0.5030 0.3417 -0.2119 143 HIS A O 442 C CB . HIS A 55 ? 1.4062 0.9462 0.8305 -0.5957 0.4102 -0.2681 143 HIS A CB 443 C CG . HIS A 55 ? 1.2086 0.8847 0.7289 -0.5821 0.3774 -0.2760 143 HIS A CG 444 N ND1 . HIS A 55 ? 1.3206 1.0525 0.8766 -0.5870 0.3630 -0.2921 143 HIS A ND1 445 C CD2 . HIS A 55 ? 1.1387 0.9060 0.7238 -0.5618 0.3563 -0.2696 143 HIS A CD2 446 C CE1 . HIS A 55 ? 1.1315 0.9828 0.7660 -0.5694 0.3332 -0.2958 143 HIS A CE1 447 N NE2 . HIS A 55 ? 1.1355 1.0096 0.7893 -0.5537 0.3298 -0.2809 143 HIS A NE2 448 N N . LEU A 56 ? 1.4029 0.7070 0.6969 -0.4755 0.3623 -0.1757 144 LEU A N 449 C CA . LEU A 56 ? 1.2915 0.5783 0.5884 -0.4207 0.3270 -0.1452 144 LEU A CA 450 C C . LEU A 56 ? 1.3881 0.5899 0.6324 -0.3910 0.3155 -0.1320 144 LEU A C 451 O O . LEU A 56 ? 1.3701 0.5918 0.6426 -0.3583 0.2854 -0.1230 144 LEU A O 452 C CB . LEU A 56 ? 1.4688 0.7058 0.7270 -0.3915 0.3245 -0.1221 144 LEU A CB 453 C CG . LEU A 56 ? 1.4742 0.7419 0.7662 -0.3478 0.2925 -0.0989 144 LEU A CG 454 C CD1 . LEU A 56 ? 1.4534 0.8459 0.8428 -0.3630 0.2805 -0.1100 144 LEU A CD1 455 C CD2 . LEU A 56 ? 1.5170 0.7548 0.7796 -0.3365 0.2992 -0.0875 144 LEU A CD2 456 N N . ARG A 57 ? 1.5014 0.6052 0.6660 -0.4005 0.3398 -0.1321 145 ARG A N 457 C CA . ARG A 57 ? 1.6381 0.6567 0.7477 -0.3742 0.3328 -0.1227 145 ARG A CA 458 C C . ARG A 57 ? 1.6329 0.7129 0.7990 -0.3951 0.3260 -0.1457 145 ARG A C 459 O O . ARG A 57 ? 1.5081 0.5749 0.6777 -0.3594 0.3005 -0.1393 145 ARG A O 460 C CB . ARG A 57 ? 1.6853 0.5883 0.6964 -0.3908 0.3673 -0.1232 145 ARG A CB 461 C CG . ARG A 57 ? 1.7728 0.5840 0.7237 -0.3676 0.3641 -0.1172 145 ARG A CG 462 C CD . ARG A 57 ? 1.9812 0.6912 0.8456 -0.4035 0.4068 -0.1274 145 ARG A CD 463 N NE . ARG A 57 ? 2.0398 0.8144 0.9510 -0.4738 0.4371 -0.1625 145 ARG A NE 464 C CZ . ARG A 57 ? 2.2287 0.9367 1.0825 -0.5197 0.4788 -0.1808 145 ARG A CZ 465 N NH1 . ARG A 57 ? 2.4371 1.0011 1.1772 -0.5021 0.4965 -0.1646 145 ARG A NH1 466 N NH2 . ARG A 57 ? 2.1889 0.9752 1.0967 -0.5827 0.5033 -0.2174 145 ARG A NH2 467 N N . ASP A 58 ? 1.4775 0.6318 0.6891 -0.4510 0.3476 -0.1764 146 ASP A N 468 C CA . ASP A 58 ? 1.5455 0.7633 0.8061 -0.4765 0.3440 -0.2049 146 ASP A CA 469 C C . ASP A 58 ? 1.4549 0.7944 0.8051 -0.4628 0.3094 -0.2134 146 ASP A C 470 O O . ASP A 58 ? 1.4633 0.8315 0.8365 -0.4577 0.2935 -0.2281 146 ASP A O 471 C CB . ASP A 58 ? 1.5168 0.7676 0.7848 -0.5411 0.3816 -0.2395 146 ASP A CB 472 C CG . ASP A 58 ? 1.6678 0.7850 0.8367 -0.5578 0.4177 -0.2363 146 ASP A CG 473 O OD1 . ASP A 58 ? 1.7977 0.8069 0.9002 -0.5199 0.4093 -0.2133 146 ASP A OD1 474 O OD2 . ASP A 58 ? 1.7799 0.8992 0.9342 -0.6071 0.4548 -0.2584 146 ASP A OD2 475 N N . HIS A 59 ? 1.3489 0.7560 0.7436 -0.4549 0.2978 -0.2056 147 HIS A N 476 C CA . HIS A 59 ? 1.2131 0.7404 0.6875 -0.4473 0.2688 -0.2176 147 HIS A CA 477 C C . HIS A 59 ? 1.1398 0.6534 0.6156 -0.3950 0.2375 -0.1919 147 HIS A C 478 O O . HIS A 59 ? 0.9995 0.6212 0.5400 -0.3743 0.2136 -0.1893 147 HIS A O 479 C CB . HIS A 59 ? 1.2284 0.8723 0.7668 -0.4819 0.2781 -0.2379 147 HIS A CB 480 C CG . HIS A 59 ? 1.3075 1.0124 0.8687 -0.5306 0.3005 -0.2759 147 HIS A CG 481 N ND1 . HIS A 59 ? 1.5273 1.1575 1.0344 -0.5631 0.3377 -0.2840 147 HIS A ND1 482 C CD2 . HIS A 59 ? 1.2107 1.0475 0.8404 -0.5503 0.2906 -0.3105 147 HIS A CD2 483 C CE1 . HIS A 59 ? 1.5049 1.2160 1.0489 -0.6050 0.3520 -0.3236 147 HIS A CE1 484 N NE2 . HIS A 59 ? 1.3682 1.2091 0.9885 -0.5957 0.3224 -0.3402 147 HIS A NE2 485 N N . VAL A 60 ? 1.2683 0.6726 0.6817 -0.3580 0.2351 -0.1643 148 VAL A N 486 C CA . VAL A 60 ? 1.1833 0.5844 0.6013 -0.3027 0.2053 -0.1423 148 VAL A CA 487 C C . VAL A 60 ? 1.2885 0.6086 0.6561 -0.2686 0.1960 -0.1389 148 VAL A C 488 O O . VAL A 60 ? 1.3521 0.5794 0.6580 -0.2646 0.2104 -0.1288 148 VAL A O 489 C CB . VAL A 60 ? 1.2053 0.5727 0.6054 -0.2819 0.2056 -0.1146 148 VAL A CB 490 C CG1 . VAL A 60 ? 1.0170 0.4248 0.4489 -0.2233 0.1724 -0.0919 148 VAL A CG1 491 C CG2 . VAL A 60 ? 1.1099 0.5547 0.5569 -0.3163 0.2199 -0.1199 148 VAL A CG2 492 N N . ASN A 61 ? 1.1103 0.4885 0.5134 -0.2375 0.1714 -0.1422 149 ASN A N 493 C CA . ASN A 61 ? 1.1832 0.4934 0.5418 -0.2038 0.1630 -0.1459 149 ASN A CA 494 C C . ASN A 61 ? 1.2399 0.5452 0.5992 -0.1446 0.1399 -0.1210 149 ASN A C 495 O O . ASN A 61 ? 1.1798 0.5771 0.5989 -0.1193 0.1194 -0.1143 149 ASN A O 496 C CB . ASN A 61 ? 1.1133 0.4971 0.5097 -0.2067 0.1534 -0.1679 149 ASN A CB 497 C CG . ASN A 61 ? 1.1693 0.5285 0.5486 -0.2490 0.1729 -0.1924 149 ASN A CG 498 O OD1 . ASN A 61 ? 1.3370 0.6077 0.6678 -0.2607 0.1920 -0.1860 149 ASN A OD1 499 N ND2 . ASN A 61 ? 1.2510 0.6954 0.6700 -0.2691 0.1679 -0.2178 149 ASN A ND2 500 N N . VAL A 62 ? 1.2673 0.4720 0.5620 -0.1230 0.1436 -0.1064 150 VAL A N 501 C CA . VAL A 62 ? 1.2610 0.4509 0.5436 -0.0646 0.1205 -0.0923 150 VAL A CA 502 C C . VAL A 62 ? 1.2679 0.4511 0.5424 -0.0262 0.1068 -0.1038 150 VAL A C 503 O O . VAL A 62 ? 1.2972 0.4042 0.5187 -0.0102 0.1107 -0.1009 150 VAL A O 504 C CB . VAL A 62 ? 1.3638 0.4674 0.5815 -0.0467 0.1247 -0.0695 150 VAL A CB 505 C CG1 . VAL A 62 ? 1.2671 0.3866 0.4899 0.0057 0.0983 -0.0588 150 VAL A CG1 506 C CG2 . VAL A 62 ? 1.3460 0.4413 0.5568 -0.0968 0.1502 -0.0629 150 VAL A CG2 507 N N . SER A 63 ? 1.2031 0.4897 0.5452 -0.0129 0.0912 -0.1107 151 SER A N 508 C CA . SER A 63 ? 1.2347 0.5235 0.5712 0.0239 0.0805 -0.1260 151 SER A CA 509 C C . SER A 63 ? 1.1407 0.5422 0.5503 0.0534 0.0602 -0.1219 151 SER A C 510 O O . SER A 63 ? 1.0488 0.5301 0.5169 0.0346 0.0579 -0.1095 151 SER A O 511 C CB . SER A 63 ? 1.4743 0.7609 0.8048 -0.0077 0.0946 -0.1491 151 SER A CB 512 O OG . SER A 63 ? 1.5254 0.9083 0.9177 -0.0504 0.0990 -0.1501 151 SER A OG 513 N N . MET A 64 ? 1.1264 0.5301 0.5292 0.1000 0.0476 -0.1341 152 MET A N 514 C CA . MET A 64 ? 0.9827 0.4874 0.4499 0.1285 0.0315 -0.1349 152 MET A CA 515 C C . MET A 64 ? 0.9451 0.5161 0.4464 0.1269 0.0355 -0.1519 152 MET A C 516 O O . MET A 64 ? 1.0502 0.5733 0.5121 0.1256 0.0437 -0.1680 152 MET A O 517 C CB . MET A 64 ? 1.0739 0.5467 0.5113 0.1884 0.0129 -0.1414 152 MET A CB 518 C CG . MET A 64 ? 1.1469 0.5382 0.5298 0.2000 0.0074 -0.1252 152 MET A CG 519 S SD . MET A 64 ? 1.1015 0.5618 0.5419 0.1713 0.0040 -0.1053 152 MET A SD 520 C CE . MET A 64 ? 1.1314 0.4594 0.4776 0.1712 0.0100 -0.0880 152 MET A CE 521 N N . VAL A 65 ? 0.8997 0.5756 0.4692 0.1254 0.0323 -0.1494 153 VAL A N 522 C CA . VAL A 65 ? 0.8949 0.6368 0.4929 0.1256 0.0386 -0.1642 153 VAL A CA 523 C C . VAL A 65 ? 0.9423 0.6606 0.5125 0.1721 0.0327 -0.1897 153 VAL A C 524 O O . VAL A 65 ? 0.9555 0.6782 0.5285 0.2139 0.0186 -0.1964 153 VAL A O 525 C CB . VAL A 65 ? 0.8341 0.6808 0.5014 0.1178 0.0404 -0.1564 153 VAL A CB 526 C CG1 . VAL A 65 ? 0.8083 0.7184 0.4960 0.1205 0.0503 -0.1720 153 VAL A CG1 527 C CG2 . VAL A 65 ? 0.6812 0.5444 0.3697 0.0777 0.0466 -0.1311 153 VAL A CG2 528 N N . GLU A 66 ? 0.9527 0.6492 0.4951 0.1676 0.0423 -0.2068 154 GLU A N 529 C CA . GLU A 66 ? 1.0199 0.6876 0.5305 0.2131 0.0389 -0.2335 154 GLU A CA 530 C C . GLU A 66 ? 1.0397 0.8018 0.5910 0.2151 0.0473 -0.2516 154 GLU A C 531 O O . GLU A 66 ? 0.9835 0.8090 0.5681 0.1763 0.0581 -0.2423 154 GLU A O 532 C CB . GLU A 66 ? 1.2392 0.7810 0.6684 0.2091 0.0461 -0.2434 154 GLU A CB 533 C CG . GLU A 66 ? 1.4409 0.8751 0.8165 0.2182 0.0406 -0.2266 154 GLU A CG 534 C CD . GLU A 66 ? 1.6567 0.9840 0.9747 0.1951 0.0530 -0.2262 154 GLU A CD 535 O OE1 . GLU A 66 ? 1.6875 1.0165 1.0054 0.1469 0.0683 -0.2357 154 GLU A OE1 536 O OE2 . GLU A 66 ? 1.7910 1.0360 1.0618 0.2252 0.0474 -0.2172 154 GLU A OE2 537 N N . VAL A 67 ? 0.9909 0.7601 0.5340 0.2642 0.0428 -0.2780 155 VAL A N 538 C CA . VAL A 67 ? 0.9633 0.8295 0.5466 0.2716 0.0528 -0.2984 155 VAL A CA 539 C C . VAL A 67 ? 1.0842 0.9379 0.6400 0.2417 0.0685 -0.3083 155 VAL A C 540 O O . VAL A 67 ? 1.0278 0.9557 0.6065 0.2428 0.0799 -0.3239 155 VAL A O 541 C CB . VAL A 67 ? 1.0069 0.8947 0.5986 0.3323 0.0424 -0.3238 155 VAL A CB 542 C CG1 . VAL A 67 ? 1.1042 0.8996 0.6399 0.3502 0.0417 -0.3340 155 VAL A CG1 543 C CG2 . VAL A 67 ? 1.0962 1.1195 0.7567 0.3355 0.0534 -0.3410 155 VAL A CG2 544 N N . THR A 68 ? 1.1330 0.8978 0.6397 0.2122 0.0701 -0.3014 156 THR A N 545 C CA . THR A 68 ? 1.1289 0.8876 0.6115 0.1779 0.0820 -0.3137 156 THR A CA 546 C C . THR A 68 ? 1.1452 0.9716 0.6642 0.1284 0.0862 -0.2894 156 THR A C 547 O O . THR A 68 ? 1.2973 1.1574 0.8100 0.1044 0.0936 -0.2984 156 THR A O 548 C CB . THR A 68 ? 1.1552 0.7879 0.5693 0.1647 0.0843 -0.3252 156 THR A CB 549 O OG1 . THR A 68 ? 1.3397 0.9082 0.7388 0.1526 0.0790 -0.3017 156 THR A OG1 550 C CG2 . THR A 68 ? 1.2154 0.7937 0.6080 0.2030 0.0828 -0.3426 156 THR A CG2 551 N N . ASP A 69 ? 0.9053 0.7506 0.4579 0.1175 0.0804 -0.2600 157 ASP A N 552 C CA . ASP A 69 ? 0.9655 0.8655 0.5480 0.0786 0.0831 -0.2349 157 ASP A CA 553 C C . ASP A 69 ? 0.8519 0.8497 0.4784 0.0804 0.0913 -0.2241 157 ASP A C 554 O O . ASP A 69 ? 0.7541 0.7861 0.4178 0.0947 0.0915 -0.2149 157 ASP A O 555 C CB . ASP A 69 ? 0.9474 0.8192 0.5430 0.0649 0.0759 -0.2084 157 ASP A CB 556 C CG . ASP A 69 ? 1.1354 0.9013 0.6828 0.0633 0.0723 -0.2150 157 ASP A CG 557 O OD1 . ASP A 69 ? 1.2550 0.9833 0.7722 0.0330 0.0779 -0.2252 157 ASP A OD1 558 O OD2 . ASP A 69 ? 1.0493 0.7705 0.5872 0.0905 0.0649 -0.2101 157 ASP A OD2 559 N N . PHE A 70 ? 0.7845 0.8259 0.4032 0.0629 0.0994 -0.2257 158 PHE A N 560 C CA . PHE A 70 ? 0.7527 0.8734 0.3964 0.0604 0.1126 -0.2129 158 PHE A CA 561 C C . PHE A 70 ? 0.7012 0.8409 0.3779 0.0456 0.1133 -0.1783 158 PHE A C 562 O O . PHE A 70 ? 0.6868 0.8013 0.3587 0.0285 0.1042 -0.1616 158 PHE A O 563 C CB . PHE A 70 ? 0.7849 0.9362 0.3991 0.0447 0.1177 -0.2163 158 PHE A CB 564 C CG . PHE A 70 ? 0.7963 1.0147 0.4196 0.0407 0.1345 -0.1969 158 PHE A CG 565 C CD1 . PHE A 70 ? 0.8214 1.0813 0.4400 0.0537 0.1516 -0.2143 158 PHE A CD1 566 C CD2 . PHE A 70 ? 0.7438 0.9776 0.3752 0.0250 0.1359 -0.1612 158 PHE A CD2 567 C CE1 . PHE A 70 ? 0.8102 1.1230 0.4289 0.0458 0.1731 -0.1950 158 PHE A CE1 568 C CE2 . PHE A 70 ? 0.7615 1.0383 0.3881 0.0212 0.1555 -0.1406 158 PHE A CE2 569 C CZ . PHE A 70 ? 0.7572 1.0720 0.3757 0.0289 0.1756 -0.1566 158 PHE A CZ 570 N N . PRO A 71 ? 0.6870 0.8747 0.3973 0.0493 0.1267 -0.1697 159 PRO A N 571 C CA . PRO A 71 ? 0.7292 0.9698 0.4542 0.0636 0.1434 -0.1894 159 PRO A CA 572 C C . PRO A 71 ? 0.7307 0.9765 0.4871 0.0916 0.1371 -0.2128 159 PRO A C 573 O O . PRO A 71 ? 0.6917 1.0004 0.4803 0.1002 0.1519 -0.2281 159 PRO A O 574 C CB . PRO A 71 ? 0.6697 0.9560 0.4150 0.0417 0.1645 -0.1631 159 PRO A CB 575 C CG . PRO A 71 ? 0.6352 0.8883 0.4000 0.0294 0.1532 -0.1377 159 PRO A CG 576 C CD . PRO A 71 ? 0.6695 0.8650 0.4060 0.0321 0.1300 -0.1381 159 PRO A CD 577 N N . PHE A 72 ? 0.7407 0.9240 0.4856 0.1068 0.1160 -0.2171 160 PHE A N 578 C CA . PHE A 72 ? 0.7117 0.8935 0.4754 0.1424 0.1046 -0.2380 160 PHE A CA 579 C C . PHE A 72 ? 0.8051 0.9806 0.5447 0.1793 0.1037 -0.2735 160 PHE A C 580 O O . PHE A 72 ? 0.8223 0.9905 0.5666 0.2204 0.0912 -0.2944 160 PHE A O 581 C CB . PHE A 72 ? 0.7158 0.8221 0.4625 0.1473 0.0840 -0.2254 160 PHE A CB 582 C CG . PHE A 72 ? 0.7390 0.8563 0.5142 0.1180 0.0843 -0.1955 160 PHE A CG 583 C CD1 . PHE A 72 ? 0.6486 0.7403 0.4070 0.0851 0.0875 -0.1701 160 PHE A CD1 584 C CD2 . PHE A 72 ? 0.6660 0.8228 0.4852 0.1252 0.0806 -0.1967 160 PHE A CD2 585 C CE1 . PHE A 72 ? 0.6096 0.7070 0.3905 0.0633 0.0883 -0.1442 160 PHE A CE1 586 C CE2 . PHE A 72 ? 0.6195 0.7796 0.4609 0.0978 0.0825 -0.1720 160 PHE A CE2 587 C CZ . PHE A 72 ? 0.6678 0.7932 0.4880 0.0687 0.0867 -0.1445 160 PHE A CZ 588 N N . ASN A 73 ? 0.7910 0.9679 0.5005 0.1688 0.1155 -0.2816 161 ASN A N 589 C CA . ASN A 73 ? 0.8955 1.0784 0.5843 0.2017 0.1200 -0.3180 161 ASN A CA 590 C C . ASN A 73 ? 0.9064 1.1947 0.6327 0.2020 0.1431 -0.3315 161 ASN A C 591 O O . ASN A 73 ? 0.8700 1.1686 0.5888 0.2194 0.1484 -0.3524 161 ASN A O 592 C CB . ASN A 73 ? 0.9683 1.0898 0.5974 0.1895 0.1205 -0.3269 161 ASN A CB 593 C CG . ASN A 73 ? 0.9668 1.1294 0.5920 0.1475 0.1328 -0.3075 161 ASN A CG 594 O OD1 . ASN A 73 ? 0.9830 1.1866 0.6387 0.1241 0.1383 -0.2777 161 ASN A OD1 595 N ND2 . ASN A 73 ? 1.0199 1.1677 0.6023 0.1404 0.1365 -0.3256 161 ASN A ND2 596 N N . THR A 74 ? 0.8444 1.1955 0.6149 0.1735 0.1568 -0.3099 162 THR A N 597 C CA . THR A 74 ? 0.8612 1.3030 0.6623 0.1628 0.1850 -0.3183 162 THR A CA 598 C C . THR A 74 ? 0.8374 1.3445 0.7005 0.1853 0.1845 -0.3413 162 THR A C 599 O O . THR A 74 ? 0.7514 1.2474 0.6346 0.2090 0.1638 -0.3493 162 THR A O 600 C CB . THR A 74 ? 0.8349 1.3038 0.6416 0.1162 0.2072 -0.2834 162 THR A CB 601 O OG1 . THR A 74 ? 0.6991 1.1586 0.5417 0.1023 0.1983 -0.2631 162 THR A OG1 602 C CG2 . THR A 74 ? 0.7619 1.1773 0.5100 0.0973 0.2030 -0.2592 162 THR A CG2 603 N N . SER A 75 ? 0.7777 1.3553 0.6697 0.1769 0.2064 -0.3521 163 SER A N 604 C CA . SER A 75 ? 0.9577 1.6094 0.9099 0.1991 0.2041 -0.3810 163 SER A CA 605 C C . SER A 75 ? 0.7363 1.4314 0.7449 0.1883 0.1993 -0.3804 163 SER A C 606 O O . SER A 75 ? 0.9311 1.6594 0.9767 0.2225 0.1776 -0.4052 163 SER A O 607 C CB . SER A 75 ? 0.9342 1.6566 0.9066 0.1805 0.2341 -0.3906 163 SER A CB 608 O OG . SER A 75 ? 0.9548 1.7091 0.9446 0.1286 0.2639 -0.3668 163 SER A OG 609 N N . GLU A 76 ? 0.7014 1.3941 0.7132 0.1422 0.2179 -0.3522 164 GLU A N 610 C CA . GLU A 76 ? 0.7905 1.5248 0.8571 0.1241 0.2177 -0.3534 164 GLU A CA 611 C C . GLU A 76 ? 0.8005 1.4928 0.8626 0.1607 0.1815 -0.3591 164 GLU A C 612 O O . GLU A 76 ? 0.8470 1.5840 0.9589 0.1658 0.1694 -0.3740 164 GLU A O 613 C CB . GLU A 76 ? 0.7848 1.5067 0.8453 0.0660 0.2477 -0.3180 164 GLU A CB 614 C CG . GLU A 76 ? 0.8224 1.4503 0.8217 0.0582 0.2378 -0.2800 164 GLU A CG 615 C CD . GLU A 76 ? 0.8801 1.4806 0.8813 0.0112 0.2534 -0.2425 164 GLU A CD 616 O OE1 . GLU A 76 ? 0.9538 1.4938 0.9027 -0.0055 0.2584 -0.2058 164 GLU A OE1 617 O OE2 . GLU A 76 ? 0.8732 1.5131 0.9267 -0.0067 0.2596 -0.2523 164 GLU A OE2 618 N N . TRP A 77 ? 0.7717 1.3694 0.7702 0.1833 0.1620 -0.3455 165 TRP A N 619 C CA . TRP A 77 ? 0.7328 1.2546 0.7094 0.2114 0.1260 -0.3377 165 TRP A CA 620 C C . TRP A 77 ? 0.7789 1.2822 0.7346 0.2771 0.1018 -0.3701 165 TRP A C 621 O O . TRP A 77 ? 0.8908 1.3083 0.8060 0.3049 0.0746 -0.3618 165 TRP A O 622 C CB . TRP A 77 ? 0.6704 1.0854 0.5878 0.1884 0.1194 -0.2988 165 TRP A CB 623 C CG . TRP A 77 ? 0.7493 1.1636 0.6838 0.1411 0.1301 -0.2658 165 TRP A CG 624 C CD1 . TRP A 77 ? 0.7932 1.2146 0.7188 0.0998 0.1553 -0.2411 165 TRP A CD1 625 C CD2 . TRP A 77 ? 0.6695 1.0716 0.6277 0.1331 0.1162 -0.2538 165 TRP A CD2 626 N NE1 . TRP A 77 ? 0.8343 1.2416 0.7755 0.0681 0.1584 -0.2134 165 TRP A NE1 627 C CE2 . TRP A 77 ? 0.5748 0.9730 0.5391 0.0856 0.1353 -0.2224 165 TRP A CE2 628 C CE3 . TRP A 77 ? 0.6500 1.0413 0.6188 0.1652 0.0890 -0.2671 165 TRP A CE3 629 C CZ2 . TRP A 77 ? 0.6925 1.0755 0.6768 0.0667 0.1294 -0.2062 165 TRP A CZ2 630 C CZ3 . TRP A 77 ? 0.6483 1.0306 0.6370 0.1448 0.0821 -0.2511 165 TRP A CZ3 631 C CH2 . TRP A 77 ? 0.5470 0.9250 0.5453 0.0948 0.1029 -0.2220 165 TRP A CH2 632 N N . GLU A 78 ? 0.7807 1.3422 0.7601 0.2928 0.1077 -0.3929 166 GLU A N 633 C CA . GLU A 78 ? 0.8077 1.3388 0.7653 0.3501 0.0822 -0.4128 166 GLU A CA 634 C C . GLU A 78 ? 0.9030 1.4468 0.8820 0.3901 0.0494 -0.4235 166 GLU A C 635 O O . GLU A 78 ? 0.8472 1.4903 0.8931 0.3790 0.0494 -0.4376 166 GLU A O 636 C CB . GLU A 78 ? 0.8334 1.4401 0.8194 0.3567 0.0970 -0.4372 166 GLU A CB 637 C CG . GLU A 78 ? 0.9110 1.4709 0.8598 0.4134 0.0765 -0.4551 166 GLU A CG 638 C CD . GLU A 78 ? 1.0946 1.6998 1.0740 0.4651 0.0452 -0.4773 166 GLU A CD 639 O OE1 . GLU A 78 ? 1.0736 1.7959 1.1248 0.4532 0.0477 -0.4951 166 GLU A OE1 640 O OE2 . GLU A 78 ? 1.1417 1.6632 1.0689 0.5156 0.0182 -0.4770 166 GLU A OE2 641 N N . GLY A 79 ? 0.9265 1.3642 0.8429 0.4326 0.0223 -0.4156 167 GLY A N 642 C CA . GLY A 79 ? 0.9341 1.3711 0.8516 0.4812 -0.0130 -0.4238 167 GLY A CA 643 C C . GLY A 79 ? 0.9623 1.4035 0.8969 0.4644 -0.0223 -0.4110 167 GLY A C 644 O O . GLY A 79 ? 0.9418 1.3987 0.8824 0.5003 -0.0523 -0.4190 167 GLY A O 645 N N . TYR A 80 ? 0.9316 1.3586 0.8689 0.4114 0.0024 -0.3917 168 TYR A N 646 C CA . TYR A 80 ? 0.7640 1.2015 0.7224 0.3898 -0.0011 -0.3816 168 TYR A CA 647 C C . TYR A 80 ? 0.8785 1.1797 0.7616 0.3999 -0.0212 -0.3506 168 TYR A C 648 O O . TYR A 80 ? 0.8212 1.1184 0.7080 0.4124 -0.0420 -0.3468 168 TYR A O 649 C CB . TYR A 80 ? 0.7111 1.1930 0.7123 0.3138 0.0314 -0.3610 168 TYR A CB 650 C CG . TYR A 80 ? 0.7327 1.3562 0.8219 0.2940 0.0476 -0.3901 168 TYR A CG 651 C CD1 . TYR A 80 ? 0.7858 1.4733 0.9233 0.3056 0.0289 -0.4106 168 TYR A CD1 652 C CD2 . TYR A 80 ? 0.7098 1.4045 0.8316 0.2608 0.0834 -0.3997 168 TYR A CD2 653 C CE1 . TYR A 80 ? 0.6974 1.5125 0.9171 0.2770 0.0441 -0.4392 168 TYR A CE1 654 C CE2 . TYR A 80 ? 0.7059 1.5148 0.9034 0.2300 0.1001 -0.4212 168 TYR A CE2 655 C CZ . TYR A 80 ? 0.7129 1.5806 0.9602 0.2355 0.0802 -0.4419 168 TYR A CZ 656 O OH . TYR A 80 ? 0.6844 1.6581 1.0029 0.1975 0.0959 -0.4665 168 TYR A OH 657 N N . LEU A 81 ? 0.9233 1.1159 0.7379 0.3917 -0.0136 -0.3309 169 LEU A N 658 C CA . LEU A 81 ? 0.9932 1.0544 0.7347 0.3924 -0.0258 -0.3027 169 LEU A CA 659 C C . LEU A 81 ? 1.1284 1.1200 0.8131 0.4572 -0.0512 -0.3108 169 LEU A C 660 O O . LEU A 81 ? 1.0931 1.1187 0.7874 0.4898 -0.0567 -0.3296 169 LEU A O 661 C CB . LEU A 81 ? 1.0042 0.9853 0.7015 0.3480 -0.0060 -0.2804 169 LEU A CB 662 C CG . LEU A 81 ? 0.7973 0.8402 0.5414 0.2847 0.0176 -0.2642 169 LEU A CG 663 C CD1 . LEU A 81 ? 0.8199 0.7798 0.5132 0.2502 0.0284 -0.2451 169 LEU A CD1 664 C CD2 . LEU A 81 ? 0.7586 0.8471 0.5510 0.2536 0.0167 -0.2457 169 LEU A CD2 665 N N . PRO A 82 ? 1.1966 1.0913 0.8232 0.4692 -0.0670 -0.2889 170 PRO A N 666 C CA . PRO A 82 ? 1.2826 1.0992 0.8447 0.5223 -0.0907 -0.2833 170 PRO A CA 667 C C . PRO A 82 ? 1.3312 1.0555 0.8346 0.5246 -0.0782 -0.2798 170 PRO A C 668 O O . PRO A 82 ? 1.2965 0.9630 0.7780 0.4775 -0.0541 -0.2694 170 PRO A O 669 C CB . PRO A 82 ? 1.3470 1.0676 0.8509 0.5156 -0.0988 -0.2542 170 PRO A CB 670 C CG . PRO A 82 ? 1.2091 1.0055 0.7751 0.4775 -0.0912 -0.2562 170 PRO A CG 671 C CD . PRO A 82 ? 1.1394 1.0041 0.7603 0.4338 -0.0643 -0.2667 170 PRO A CD 672 N N . LYS A 83 ? 1.4022 1.1185 0.8807 0.5786 -0.0953 -0.2916 171 LYS A N 673 C CA . LYS A 83 ? 1.5264 1.1570 0.9492 0.5869 -0.0843 -0.2930 171 LYS A CA 674 C C . LYS A 83 ? 1.6257 1.0953 0.9551 0.5644 -0.0737 -0.2633 171 LYS A C 675 O O . LYS A 83 ? 1.6832 1.0864 0.9844 0.5293 -0.0503 -0.2626 171 LYS A O 676 C CB . LYS A 83 ? 1.6305 1.2801 1.0369 0.6566 -0.1081 -0.3106 171 LYS A CB 677 C CG . LYS A 83 ? 1.5705 1.3833 1.0694 0.6765 -0.1150 -0.3457 171 LYS A CG 678 C CD . LYS A 83 ? 1.6124 1.4365 1.1210 0.6722 -0.0950 -0.3650 171 LYS A CD 679 C CE . LYS A 83 ? 1.6207 1.5939 1.2043 0.7038 -0.1044 -0.4005 171 LYS A CE 680 N NZ . LYS A 83 ? 1.6492 1.6182 1.2253 0.7140 -0.0891 -0.4198 171 LYS A NZ 681 N N . GLU A 84 ? 1.5783 0.9906 0.8595 0.5815 -0.0897 -0.2412 172 GLU A N 682 C CA . GLU A 84 ? 1.6867 0.9460 0.8715 0.5621 -0.0777 -0.2124 172 GLU A CA 683 C C . GLU A 84 ? 1.5346 0.7713 0.7274 0.4989 -0.0599 -0.1927 172 GLU A C 684 O O . GLU A 84 ? 1.4113 0.7380 0.6691 0.4849 -0.0651 -0.1959 172 GLU A O 685 C CB . GLU A 84 ? 1.9329 1.1260 1.0373 0.6194 -0.1023 -0.1979 172 GLU A CB 686 C CG . GLU A 84 ? 2.1464 1.3432 1.2225 0.6876 -0.1217 -0.2156 172 GLU A CG 687 C CD . GLU A 84 ? 2.1753 1.5350 1.3422 0.7273 -0.1476 -0.2464 172 GLU A CD 688 O OE1 . GLU A 84 ? 2.0924 1.5462 1.3248 0.7126 -0.1564 -0.2498 172 GLU A OE1 689 O OE2 . GLU A 84 ? 2.2507 1.6470 1.4253 0.7701 -0.1571 -0.2693 172 GLU A OE2 690 N N . SER A 85 ? 1.5949 0.7133 0.7214 0.4592 -0.0373 -0.1745 173 SER A N 691 C CA . SER A 85 ? 1.5378 0.6291 0.6645 0.3981 -0.0189 -0.1563 173 SER A CA 692 C C . SER A 85 ? 1.6743 0.7543 0.7754 0.4194 -0.0357 -0.1358 173 SER A C 693 O O . SER A 85 ? 1.7662 0.8092 0.8116 0.4741 -0.0555 -0.1300 173 SER A O 694 C CB . SER A 85 ? 1.7553 0.7274 0.8141 0.3529 0.0095 -0.1455 173 SER A CB 695 O OG . SER A 85 ? 1.8970 0.8619 0.9670 0.2900 0.0286 -0.1328 173 SER A OG 696 N N . ILE A 86 ? 1.5345 0.6474 0.6714 0.3788 -0.0289 -0.1268 174 ILE A N 697 C CA . ILE A 86 ? 1.4876 0.5909 0.6004 0.3956 -0.0433 -0.1095 174 ILE A CA 698 C C . ILE A 86 ? 1.7005 0.6701 0.7011 0.3982 -0.0336 -0.0852 174 ILE A C 699 O O . ILE A 86 ? 1.7377 0.6787 0.6816 0.4463 -0.0535 -0.0771 174 ILE A O 700 C CB . ILE A 86 ? 1.4142 0.5665 0.5802 0.3478 -0.0337 -0.1046 174 ILE A CB 701 C CG1 . ILE A 86 ? 1.4968 0.6170 0.6215 0.3606 -0.0444 -0.0854 174 ILE A CG1 702 C CG2 . ILE A 86 ? 1.3658 0.4808 0.5323 0.2776 -0.0007 -0.0998 174 ILE A CG2 703 C CD1 . ILE A 86 ? 1.4032 0.5761 0.5813 0.3227 -0.0386 -0.0829 174 ILE A CD1 704 N N . ARG A 87 ? 1.7973 0.6895 0.7629 0.3468 -0.0018 -0.0780 175 ARG A N 705 C CA . ARG A 87 ? 1.8725 0.6335 0.7282 0.3414 0.0166 -0.0596 175 ARG A CA 706 C C . ARG A 87 ? 1.9349 0.6381 0.7164 0.4096 -0.0009 -0.0613 175 ARG A C 707 O O . ARG A 87 ? 2.0856 0.6853 0.7629 0.4252 0.0060 -0.0450 175 ARG A O 708 C CB . ARG A 87 ? 1.8329 0.5441 0.6828 0.2737 0.0535 -0.0625 175 ARG A CB 709 C CG . ARG A 87 ? 1.7949 0.5542 0.7009 0.2071 0.0718 -0.0597 175 ARG A CG 710 C CD . ARG A 87 ? 1.8235 0.5844 0.7578 0.1476 0.0982 -0.0754 175 ARG A CD 711 N NE . ARG A 87 ? 1.8115 0.5556 0.7413 0.0798 0.1282 -0.0686 175 ARG A NE 712 C CZ . ARG A 87 ? 1.6784 0.5057 0.6811 0.0376 0.1325 -0.0742 175 ARG A CZ 713 N NH1 . ARG A 87 ? 1.5128 0.4391 0.5931 0.0541 0.1105 -0.0848 175 ARG A NH1 714 N NH2 . ARG A 87 ? 1.7227 0.5360 0.7175 -0.0211 0.1609 -0.0712 175 ARG A NH2 715 N N . THR A 88 ? 1.9964 0.7678 0.8278 0.4511 -0.0220 -0.0829 176 THR A N 716 C CA . THR A 88 ? 2.1037 0.8387 0.8737 0.5233 -0.0432 -0.0884 176 THR A CA 717 C C . THR A 88 ? 2.1356 0.9283 0.9030 0.5820 -0.0793 -0.0886 176 THR A C 718 O O . THR A 88 ? 2.3054 1.0311 0.9790 0.6331 -0.0928 -0.0817 176 THR A O 719 C CB . THR A 88 ? 2.0276 0.8299 0.8593 0.5467 -0.0518 -0.1165 176 THR A CB 720 O OG1 . THR A 88 ? 2.0815 0.8301 0.9109 0.4942 -0.0196 -0.1215 176 THR A OG1 721 C CG2 . THR A 88 ? 2.0806 0.8595 0.8546 0.6270 -0.0771 -0.1247 176 THR A CG2 722 N N . LYS A 89 ? 1.9952 0.9126 0.8632 0.5732 -0.0938 -0.0996 177 LYS A N 723 C CA . LYS A 89 ? 2.0113 1.0114 0.8997 0.6249 -0.1299 -0.1093 177 LYS A CA 724 C C . LYS A 89 ? 2.0879 1.0306 0.9120 0.6160 -0.1285 -0.0877 177 LYS A C 725 O O . LYS A 89 ? 2.1459 1.1102 0.9374 0.6678 -0.1568 -0.0940 177 LYS A O 726 C CB . LYS A 89 ? 1.9017 1.0572 0.9241 0.6130 -0.1408 -0.1328 177 LYS A CB 727 C CG . LYS A 89 ? 1.9488 1.2249 1.0270 0.6740 -0.1742 -0.1656 177 LYS A CG 728 C CD . LYS A 89 ? 2.0206 1.2991 1.1058 0.6927 -0.1693 -0.1818 177 LYS A CD 729 C CE . LYS A 89 ? 1.9844 1.4055 1.1409 0.7451 -0.1990 -0.2185 177 LYS A CE 730 N NZ . LYS A 89 ? 1.8338 1.4009 1.1186 0.7102 -0.1935 -0.2406 177 LYS A NZ 731 N N . ALA A 90 ? 2.0710 0.9456 0.8763 0.5500 -0.0945 -0.0665 178 ALA A N 732 C CA . ALA A 90 ? 2.0511 0.8857 0.8111 0.5307 -0.0874 -0.0488 178 ALA A CA 733 C C . ALA A 90 ? 2.2071 0.8943 0.8483 0.5046 -0.0541 -0.0267 178 ALA A C 734 O O . ALA A 90 ? 2.2302 0.8732 0.8750 0.4405 -0.0186 -0.0175 178 ALA A O 735 C CB . ALA A 90 ? 1.8380 0.7454 0.6917 0.4737 -0.0764 -0.0475 178 ALA A CB 736 N N . GLY A 91 ? 2.2999 0.9164 0.8366 0.5537 -0.0642 -0.0224 179 GLY A N 737 C CA . GLY A 91 ? 2.3963 0.8690 0.8115 0.5337 -0.0303 -0.0046 179 GLY A CA 738 C C . GLY A 91 ? 2.5058 0.8970 0.8847 0.5127 -0.0042 -0.0013 179 GLY A C 739 O O . GLY A 91 ? 2.5503 0.9680 0.9504 0.5521 -0.0237 -0.0136 179 GLY A O 740 N N . PRO A 92 ? 2.5223 0.8224 0.8537 0.4483 0.0409 0.0111 180 PRO A N 741 C CA . PRO A 92 ? 2.4687 0.7514 0.7929 0.3894 0.0704 0.0210 180 PRO A CA 742 C C . PRO A 92 ? 2.5981 0.8183 0.8245 0.4276 0.0661 0.0277 180 PRO A C 743 O O . PRO A 92 ? 2.7915 0.9228 0.9121 0.4826 0.0597 0.0296 180 PRO A O 744 C CB . PRO A 92 ? 2.5133 0.7009 0.7917 0.3256 0.1191 0.0251 180 PRO A CB 745 C CG . PRO A 92 ? 2.5601 0.7384 0.8520 0.3421 0.1127 0.0162 180 PRO A CG 746 C CD . PRO A 92 ? 2.6192 0.8185 0.8905 0.4325 0.0681 0.0121 180 PRO A CD 747 N N . TRP A 93 ? 2.4926 0.7581 0.7541 0.4008 0.0697 0.0293 181 TRP A N 748 C CA . TRP A 93 ? 2.5643 0.7959 0.7567 0.4411 0.0592 0.0303 181 TRP A CA 749 C C . TRP A 93 ? 2.6556 0.7982 0.7819 0.3902 0.1037 0.0391 181 TRP A C 750 O O . TRP A 93 ? 2.5460 0.6899 0.7091 0.3166 0.1392 0.0411 181 TRP A O 751 C CB . TRP A 93 ? 2.4217 0.7821 0.7113 0.4588 0.0239 0.0207 181 TRP A CB 752 C CG . TRP A 93 ? 2.3745 0.8273 0.7199 0.5206 -0.0234 0.0062 181 TRP A CG 753 C CD1 . TRP A 93 ? 2.5035 0.9335 0.7860 0.5983 -0.0521 -0.0033 181 TRP A CD1 754 C CD2 . TRP A 93 ? 2.2243 0.8134 0.7017 0.5117 -0.0471 -0.0043 181 TRP A CD2 755 N NE1 . TRP A 93 ? 2.4207 0.9750 0.7956 0.6354 -0.0920 -0.0219 181 TRP A NE1 756 C CE2 . TRP A 93 ? 2.2247 0.8745 0.7187 0.5826 -0.0885 -0.0223 181 TRP A CE2 757 C CE3 . TRP A 93 ? 2.0867 0.7521 0.6683 0.4519 -0.0361 -0.0020 181 TRP A CE3 758 C CZ2 . TRP A 93 ? 2.0197 0.8051 0.6340 0.5915 -0.1165 -0.0393 181 TRP A CZ2 759 C CZ3 . TRP A 93 ? 1.9618 0.7492 0.6543 0.4640 -0.0643 -0.0157 181 TRP A CZ3 760 C CH2 . TRP A 93 ? 1.9540 0.8012 0.6638 0.5317 -0.1029 -0.0348 181 TRP A CH2 761 N N . GLY A 94 ? 2.7689 0.8421 0.8027 0.4310 0.1010 0.0410 182 GLY A N 762 C CA . GLY A 94 ? 2.8900 0.8678 0.8490 0.3913 0.1431 0.0482 182 GLY A CA 763 C C . GLY A 94 ? 2.7600 0.8032 0.7808 0.3641 0.1437 0.0459 182 GLY A C 764 O O . GLY A 94 ? 2.6813 0.7463 0.7516 0.2918 0.1757 0.0462 182 GLY A O 765 N N . ARG A 95 ? 2.7551 0.8303 0.7728 0.4227 0.1086 0.0419 183 ARG A N 766 C CA . ARG A 95 ? 2.6033 0.7480 0.6883 0.4023 0.1040 0.0399 183 ARG A CA 767 C C . ARG A 95 ? 2.6211 0.9131 0.8364 0.4115 0.0654 0.0300 183 ARG A C 768 O O . ARG A 95 ? 2.6591 0.9960 0.8854 0.4732 0.0256 0.0204 183 ARG A O 769 C CB . ARG A 95 ? 2.7147 0.8046 0.7193 0.4580 0.0906 0.0415 183 ARG A CB 770 C CG . ARG A 95 ? 2.8858 0.8339 0.7700 0.4369 0.1346 0.0534 183 ARG A CG 771 C CD . ARG A 95 ? 2.9772 0.8879 0.7965 0.4914 0.1181 0.0567 183 ARG A CD 772 N NE . ARG A 95 ? 2.8247 0.8627 0.7528 0.4972 0.0860 0.0505 183 ARG A NE 773 C CZ . ARG A 95 ? 3.0964 1.1469 1.0033 0.5501 0.0585 0.0497 183 ARG A CZ 774 N NH1 . ARG A 95 ? 3.3461 1.2876 1.1233 0.6055 0.0584 0.0550 183 ARG A NH1 775 N NH2 . ARG A 95 ? 2.8696 1.0405 0.8812 0.5484 0.0313 0.0438 183 ARG A NH2 776 N N . CYS A 96 ? 2.4770 0.8456 0.7902 0.3509 0.0779 0.0304 184 CYS A N 777 C CA . CYS A 96 ? 2.1186 0.6181 0.5501 0.3562 0.0451 0.0223 184 CYS A CA 778 C C . CYS A 96 ? 2.0263 0.5844 0.5231 0.3247 0.0480 0.0236 184 CYS A C 779 O O . CYS A 96 ? 2.0363 0.5629 0.5261 0.2705 0.0839 0.0303 184 CYS A O 780 C CB . CYS A 96 ? 2.0249 0.5748 0.5268 0.3155 0.0533 0.0225 184 CYS A CB 781 S SG . CYS A 96 ? 2.5239 1.0025 0.9585 0.3373 0.0574 0.0245 184 CYS A SG 782 N N . ALA A 97 ? 1.9349 0.5860 0.5008 0.3574 0.0101 0.0155 185 ALA A N 783 C CA . ALA A 97 ? 1.8920 0.6063 0.5245 0.3301 0.0091 0.0182 185 ALA A CA 784 C C . ALA A 97 ? 1.8259 0.6504 0.5706 0.3100 -0.0064 0.0135 185 ALA A C 785 O O . ALA A 97 ? 1.8356 0.7078 0.6127 0.3420 -0.0333 0.0036 185 ALA A O 786 C CB . ALA A 97 ? 1.8959 0.6195 0.5035 0.3835 -0.0199 0.0144 185 ALA A CB 787 N N . VAL A 98 ? 1.6645 0.5286 0.4651 0.2569 0.0125 0.0201 186 VAL A N 788 C CA . VAL A 98 ? 1.5363 0.5019 0.4333 0.2404 -0.0022 0.0176 186 VAL A CA 789 C C . VAL A 98 ? 1.5482 0.5708 0.4725 0.2478 -0.0190 0.0154 186 VAL A C 790 O O . VAL A 98 ? 1.6145 0.6144 0.5220 0.2189 0.0040 0.0225 186 VAL A O 791 C CB . VAL A 98 ? 1.5607 0.5422 0.5045 0.1733 0.0324 0.0236 186 VAL A CB 792 C CG1 . VAL A 98 ? 1.4984 0.5779 0.5262 0.1553 0.0218 0.0224 186 VAL A CG1 793 C CG2 . VAL A 98 ? 1.5072 0.4625 0.4433 0.1661 0.0416 0.0217 186 VAL A CG2 794 N N . VAL A 99 ? 1.5416 0.6472 0.5101 0.2844 -0.0585 0.0003 187 VAL A N 795 C CA . VAL A 99 ? 1.4585 0.6373 0.4617 0.2891 -0.0776 -0.0125 187 VAL A CA 796 C C . VAL A 99 ? 1.4026 0.6669 0.4885 0.2452 -0.0714 -0.0243 187 VAL A C 797 O O . VAL A 99 ? 1.2495 0.5957 0.4241 0.2435 -0.0851 -0.0407 187 VAL A O 798 C CB . VAL A 99 ? 1.5488 0.7862 0.5623 0.3507 -0.1240 -0.0359 187 VAL A CB 799 C CG1 . VAL A 99 ? 1.5072 0.8386 0.5741 0.3460 -0.1438 -0.0593 187 VAL A CG1 800 C CG2 . VAL A 99 ? 1.6470 0.7992 0.5713 0.4016 -0.1300 -0.0295 187 VAL A CG2 801 N N . SER A 100 ? 1.3269 0.5872 0.4203 0.2053 -0.0453 -0.0177 188 SER A N 802 C CA . SER A 100 ? 1.2650 0.6119 0.4680 0.1639 -0.0350 -0.0284 188 SER A CA 803 C C . SER A 100 ? 1.0580 0.4826 0.3077 0.1844 -0.0665 -0.0561 188 SER A C 804 O O . SER A 100 ? 1.1954 0.6089 0.3902 0.2269 -0.0937 -0.0662 188 SER A O 805 C CB . SER A 100 ? 1.3190 0.6410 0.5120 0.1235 0.0004 -0.0167 188 SER A CB 806 O OG . SER A 100 ? 1.3216 0.6965 0.5559 0.1168 -0.0045 -0.0325 188 SER A OG 807 N N . SER A 101 ? 1.0459 0.5473 0.3920 0.1557 -0.0635 -0.0704 189 SER A N 808 C CA . SER A 101 ? 0.9894 0.5625 0.3802 0.1680 -0.0902 -0.1020 189 SER A CA 809 C C . SER A 101 ? 0.9471 0.5248 0.3380 0.1517 -0.0828 -0.1122 189 SER A C 810 O O . SER A 101 ? 1.0797 0.7161 0.5146 0.1512 -0.0996 -0.1419 189 SER A O 811 C CB . SER A 101 ? 0.9079 0.5595 0.3996 0.1482 -0.0924 -0.1171 189 SER A CB 812 O OG . SER A 101 ? 1.0222 0.6784 0.5140 0.1684 -0.1021 -0.1134 189 SER A OG 813 N N . ALA A 102 ? 1.0009 0.5192 0.3435 0.1364 -0.0558 -0.0912 190 ALA A N 814 C CA . ALA A 102 ? 1.0287 0.5464 0.3684 0.1206 -0.0428 -0.0996 190 ALA A CA 815 C C . ALA A 102 ? 1.0860 0.6244 0.3984 0.1459 -0.0709 -0.1284 190 ALA A C 816 O O . ALA A 102 ? 1.1732 0.7000 0.4272 0.1849 -0.0981 -0.1337 190 ALA A O 817 C CB . ALA A 102 ? 1.0541 0.5034 0.3274 0.1082 -0.0109 -0.0748 190 ALA A CB 818 N N . GLY A 103 ? 1.1211 0.6885 0.4721 0.1263 -0.0646 -0.1485 191 GLY A N 819 C CA . GLY A 103 ? 1.1443 0.7304 0.4675 0.1439 -0.0871 -0.1796 191 GLY A CA 820 C C . GLY A 103 ? 1.2682 0.7928 0.4854 0.1677 -0.0841 -0.1646 191 GLY A C 821 O O . GLY A 103 ? 1.2689 0.8126 0.4599 0.1927 -0.1077 -0.1787 191 GLY A O 822 N N . SER A 104 ? 1.3104 0.7745 0.4888 0.1540 -0.0509 -0.1307 192 SER A N 823 C CA . SER A 104 ? 1.2647 0.6754 0.3668 0.1638 -0.0371 -0.1090 192 SER A CA 824 C C . SER A 104 ? 1.3434 0.7243 0.3865 0.2048 -0.0615 -0.0958 192 SER A C 825 O O . SER A 104 ? 1.3950 0.7257 0.3684 0.2190 -0.0543 -0.0805 192 SER A O 826 C CB . SER A 104 ? 1.2591 0.6206 0.3447 0.1327 0.0071 -0.0805 192 SER A CB 827 O OG . SER A 104 ? 1.4353 0.7819 0.5355 0.1256 0.0119 -0.0641 192 SER A OG 828 N N . LEU A 105 ? 1.3173 0.7247 0.3859 0.2260 -0.0884 -0.1019 193 LEU A N 829 C CA . LEU A 105 ? 1.3613 0.7422 0.3758 0.2737 -0.1134 -0.0932 193 LEU A CA 830 C C . LEU A 105 ? 1.4014 0.8305 0.4080 0.3070 -0.1474 -0.1198 193 LEU A C 831 O O . LEU A 105 ? 1.4871 0.8843 0.4341 0.3508 -0.1646 -0.1116 193 LEU A O 832 C CB . LEU A 105 ? 1.3317 0.7330 0.3769 0.2924 -0.1327 -0.0949 193 LEU A CB 833 C CG . LEU A 105 ? 1.4167 0.7451 0.4379 0.2730 -0.1015 -0.0628 193 LEU A CG 834 C CD1 . LEU A 105 ? 1.2482 0.6279 0.3400 0.2584 -0.1070 -0.0739 193 LEU A CD1 835 C CD2 . LEU A 105 ? 1.5896 0.8382 0.5324 0.3128 -0.1055 -0.0426 193 LEU A CD2 836 N N . LYS A 106 ? 1.3903 0.8944 0.4578 0.2870 -0.1568 -0.1544 194 LYS A N 837 C CA . LYS A 106 ? 1.4030 0.9689 0.4766 0.3124 -0.1904 -0.1877 194 LYS A CA 838 C C . LYS A 106 ? 1.5245 1.0336 0.5084 0.3357 -0.1861 -0.1715 194 LYS A C 839 O O . LYS A 106 ? 1.5601 1.0191 0.5104 0.3093 -0.1531 -0.1550 194 LYS A O 840 C CB . LYS A 106 ? 1.3124 0.9504 0.4612 0.2758 -0.1913 -0.2284 194 LYS A CB 841 C CG . LYS A 106 ? 1.3625 1.0728 0.5261 0.2955 -0.2254 -0.2683 194 LYS A CG 842 C CD . LYS A 106 ? 1.3062 1.0625 0.5266 0.2539 -0.2179 -0.3072 194 LYS A CD 843 C CE . LYS A 106 ? 1.4225 1.2682 0.6802 0.2663 -0.2538 -0.3536 194 LYS A CE 844 N NZ . LYS A 106 ? 1.4881 1.3411 0.7385 0.2455 -0.2477 -0.3805 194 LYS A NZ 845 N N . SER A 107 ? 1.6024 1.1215 0.5485 0.3870 -0.2186 -0.1776 195 SER A N 846 C CA . SER A 107 ? 1.6906 1.1555 0.5437 0.4183 -0.2198 -0.1647 195 SER A CA 847 C C . SER A 107 ? 1.7432 1.0853 0.5105 0.4136 -0.1814 -0.1176 195 SER A C 848 O O . SER A 107 ? 1.8145 1.1040 0.5133 0.4127 -0.1635 -0.1047 195 SER A O 849 C CB . SER A 107 ? 1.6721 1.1788 0.5325 0.3982 -0.2197 -0.1915 195 SER A CB 850 O OG . SER A 107 ? 1.6374 1.1064 0.4984 0.3496 -0.1777 -0.1784 195 SER A OG 851 N N . SER A 108 ? 1.7145 1.0131 0.4880 0.4069 -0.1668 -0.0951 196 SER A N 852 C CA . SER A 108 ? 1.8172 0.9986 0.5151 0.3981 -0.1290 -0.0557 196 SER A CA 853 C C . SER A 108 ? 1.9132 1.0190 0.5242 0.4554 -0.1425 -0.0414 196 SER A C 854 O O . SER A 108 ? 2.4772 1.4748 1.0082 0.4511 -0.1108 -0.0136 196 SER A O 855 C CB . SER A 108 ? 1.7070 0.8737 0.4515 0.3593 -0.1039 -0.0417 196 SER A CB 856 O OG . SER A 108 ? 1.6956 0.8870 0.4694 0.3898 -0.1313 -0.0489 196 SER A OG 857 N N . GLN A 109 ? 1.9237 1.0872 0.5521 0.5080 -0.1871 -0.0640 197 GLN A N 858 C CA . GLN A 109 ? 2.0511 1.1502 0.5984 0.5737 -0.2041 -0.0568 197 GLN A CA 859 C C . GLN A 109 ? 2.1240 1.1159 0.6246 0.5748 -0.1778 -0.0305 197 GLN A C 860 O O . GLN A 109 ? 2.2369 1.1230 0.6358 0.6099 -0.1683 -0.0145 197 GLN A O 861 C CB . GLN A 109 ? 2.2126 1.2558 0.6621 0.6017 -0.2031 -0.0494 197 GLN A CB 862 C CG . GLN A 109 ? 2.1516 1.2993 0.6393 0.6050 -0.2314 -0.0803 197 GLN A CG 863 C CD . GLN A 109 ? 2.4672 1.5573 0.8532 0.6304 -0.2281 -0.0714 197 GLN A CD 864 O OE1 . GLN A 109 ? 2.4228 1.4106 0.7064 0.6720 -0.2221 -0.0502 197 GLN A OE1 865 N NE2 . GLN A 109 ? 2.2535 1.4050 0.6628 0.6052 -0.2305 -0.0894 197 GLN A NE2 866 N N . LEU A 110 ? 2.0007 1.0188 0.5725 0.5362 -0.1657 -0.0290 198 LEU A N 867 C CA . LEU A 110 ? 2.0277 0.9539 0.5646 0.5295 -0.1398 -0.0096 198 LEU A CA 868 C C . LEU A 110 ? 2.0845 1.0214 0.6184 0.5899 -0.1713 -0.0243 198 LEU A C 869 O O . LEU A 110 ? 2.1765 1.0224 0.6547 0.6003 -0.1537 -0.0127 198 LEU A O 870 C CB . LEU A 110 ? 1.9067 0.8556 0.5166 0.4609 -0.1109 -0.0020 198 LEU A CB 871 C CG . LEU A 110 ? 1.8907 0.8181 0.4956 0.4023 -0.0722 0.0117 198 LEU A CG 872 C CD1 . LEU A 110 ? 1.7647 0.7389 0.4526 0.3415 -0.0497 0.0125 198 LEU A CD1 873 C CD2 . LEU A 110 ? 2.0321 0.8296 0.5346 0.3946 -0.0343 0.0342 198 LEU A CD2 874 N N . GLY A 111 ? 2.0822 1.1344 0.6756 0.6282 -0.2162 -0.0544 199 GLY A N 875 C CA . GLY A 111 ? 2.1316 1.2305 0.7475 0.6841 -0.2492 -0.0773 199 GLY A CA 876 C C . GLY A 111 ? 2.3289 1.3195 0.8411 0.7410 -0.2463 -0.0699 199 GLY A C 877 O O . GLY A 111 ? 2.3731 1.3681 0.8997 0.7617 -0.2527 -0.0792 199 GLY A O 878 N N . ARG A 112 ? 2.4854 1.3768 0.8872 0.7671 -0.2359 -0.0551 200 ARG A N 879 C CA . ARG A 112 ? 2.6849 1.4587 0.9714 0.8205 -0.2297 -0.0485 200 ARG A CA 880 C C . ARG A 112 ? 2.7769 1.4255 1.0116 0.7704 -0.1799 -0.0215 200 ARG A C 881 O O . ARG A 112 ? 2.8947 1.4797 1.0794 0.7951 -0.1741 -0.0231 200 ARG A O 882 C CB . ARG A 112 ? 2.8088 1.5162 0.9863 0.8689 -0.2360 -0.0427 200 ARG A CB 883 C CG . ARG A 112 ? 2.9405 1.6182 1.0388 0.9613 -0.2646 -0.0596 200 ARG A CG 884 C CD . ARG A 112 ? 3.1401 1.7075 1.1013 1.0017 -0.2578 -0.0439 200 ARG A CD 885 N NE . ARG A 112 ? 3.2136 1.8471 1.1549 1.0869 -0.3058 -0.0714 200 ARG A NE 886 C CZ . ARG A 112 ? 3.2419 1.9064 1.1627 1.1047 -0.3226 -0.0743 200 ARG A CZ 887 N NH1 . ARG A 112 ? 3.0430 1.6772 0.9595 1.0428 -0.2944 -0.0506 200 ARG A NH1 888 N NH2 . ARG A 112 ? 3.1454 1.8767 1.0499 1.1846 -0.3674 -0.1034 200 ARG A NH2 889 N N . GLU A 113 ? 2.4571 1.0770 0.7042 0.6989 -0.1436 -0.0005 201 GLU A N 890 C CA . GLU A 113 ? 2.4928 1.0033 0.6944 0.6447 -0.0934 0.0204 201 GLU A CA 891 C C . GLU A 113 ? 2.5432 1.0963 0.8201 0.6171 -0.0906 0.0130 201 GLU A C 892 O O . GLU A 113 ? 2.6637 1.1325 0.8857 0.6113 -0.0678 0.0178 201 GLU A O 893 C CB . GLU A 113 ? 2.4578 0.9516 0.6701 0.5743 -0.0565 0.0383 201 GLU A CB 894 C CG . GLU A 113 ? 2.6021 1.0475 0.8284 0.5019 -0.0096 0.0495 201 GLU A CG 895 C CD . GLU A 113 ? 2.6259 1.0211 0.8243 0.4426 0.0345 0.0655 201 GLU A CD 896 O OE1 . GLU A 113 ? 2.6744 1.0424 0.8156 0.4626 0.0327 0.0720 201 GLU A OE1 897 O OE2 . GLU A 113 ? 2.3990 0.7868 0.6327 0.3767 0.0709 0.0694 201 GLU A OE2 898 N N . ILE A 114 ? 2.3466 1.0305 0.7443 0.5993 -0.1134 0.0008 202 ILE A N 899 C CA . ILE A 114 ? 2.2276 0.9676 0.7046 0.5769 -0.1156 -0.0072 202 ILE A CA 900 C C . ILE A 114 ? 2.2608 0.9964 0.7092 0.6400 -0.1405 -0.0244 202 ILE A C 901 O O . ILE A 114 ? 2.2327 0.9449 0.6834 0.6249 -0.1274 -0.0239 202 ILE A O 902 C CB . ILE A 114 ? 2.0628 0.9466 0.6672 0.5532 -0.1388 -0.0192 202 ILE A CB 903 C CG1 . ILE A 114 ? 1.9628 0.8490 0.5929 0.4860 -0.1092 -0.0032 202 ILE A CG1 904 C CG2 . ILE A 114 ? 1.9018 0.8480 0.5837 0.5408 -0.1463 -0.0291 202 ILE A CG2 905 C CD1 . ILE A 114 ? 1.7604 0.7773 0.5010 0.4592 -0.1277 -0.0165 202 ILE A CD1 906 N N . ASP A 115 ? 2.2471 1.0081 0.6651 0.7113 -0.1760 -0.0411 203 ASP A N 907 C CA . ASP A 115 ? 2.3955 1.1596 0.7800 0.7805 -0.2020 -0.0617 203 ASP A CA 908 C C . ASP A 115 ? 2.6263 1.2364 0.8763 0.7962 -0.1742 -0.0468 203 ASP A C 909 O O . ASP A 115 ? 2.7039 1.3010 0.9172 0.8435 -0.1882 -0.0600 203 ASP A O 910 C CB . ASP A 115 ? 2.4074 1.2440 0.7916 0.8536 -0.2461 -0.0867 203 ASP A CB 911 C CG . ASP A 115 ? 2.3272 1.3393 0.8515 0.8497 -0.2810 -0.1148 203 ASP A CG 912 O OD1 . ASP A 115 ? 2.0757 1.1470 0.6915 0.7967 -0.2724 -0.1135 203 ASP A OD1 913 O OD2 . ASP A 115 ? 2.4072 1.4998 0.9486 0.8982 -0.3161 -0.1399 203 ASP A OD2 914 N N . ASP A 116 ? 2.7052 1.2009 0.8796 0.7559 -0.1341 -0.0210 204 ASP A N 915 C CA . ASP A 116 ? 2.9262 1.2690 0.9639 0.7681 -0.1049 -0.0073 204 ASP A CA 916 C C . ASP A 116 ? 2.9153 1.2081 0.9543 0.7070 -0.0676 0.0031 204 ASP A C 917 O O . ASP A 116 ? 3.1046 1.2693 1.0350 0.7023 -0.0367 0.0153 204 ASP A O 918 C CB . ASP A 116 ? 3.0277 1.2658 0.9656 0.7668 -0.0816 0.0113 204 ASP A CB 919 C CG . ASP A 116 ? 3.1037 1.3558 0.9917 0.8513 -0.1203 0.0001 204 ASP A CG 920 O OD1 . ASP A 116 ? 3.1955 1.4490 1.0437 0.9223 -0.1485 -0.0167 204 ASP A OD1 921 O OD2 . ASP A 116 ? 3.0351 1.3038 0.9244 0.8482 -0.1239 0.0064 204 ASP A OD2 922 N N . HIS A 117 ? 2.7296 1.1257 0.8897 0.6622 -0.0715 -0.0026 205 HIS A N 923 C CA . HIS A 117 ? 2.6477 1.0217 0.8230 0.6112 -0.0443 0.0036 205 HIS A CA 924 C C . HIS A 117 ? 2.5015 0.9150 0.6866 0.6594 -0.0734 -0.0115 205 HIS A C 925 O O . HIS A 117 ? 2.6911 1.2042 0.9315 0.7114 -0.1162 -0.0322 205 HIS A O 926 C CB . HIS A 117 ? 2.3283 0.7880 0.6227 0.5372 -0.0309 0.0071 205 HIS A CB 927 C CG . HIS A 117 ? 2.8542 1.2879 1.1478 0.4872 -0.0020 0.0204 205 HIS A CG 928 N ND1 . HIS A 117 ? 2.3006 0.7771 0.6145 0.5070 -0.0213 0.0197 205 HIS A ND1 929 C CD2 . HIS A 117 ? 2.3332 0.7116 0.6118 0.4175 0.0446 0.0327 205 HIS A CD2 930 C CE1 . HIS A 117 ? 2.3005 0.7452 0.6085 0.4526 0.0123 0.0332 205 HIS A CE1 931 N NE2 . HIS A 117 ? 2.3202 0.7074 0.6089 0.3981 0.0528 0.0395 205 HIS A NE2 932 N N . ASP A 118 ? 2.5639 0.9040 0.6975 0.6411 -0.0498 -0.0027 206 ASP A N 933 C CA . ASP A 118 ? 2.5651 0.9386 0.7081 0.6809 -0.0740 -0.0136 206 ASP A CA 934 C C . ASP A 118 ? 2.3767 0.9019 0.6638 0.6664 -0.0999 -0.0275 206 ASP A C 935 O O . ASP A 118 ? 2.4281 1.0205 0.7464 0.7137 -0.1325 -0.0448 206 ASP A O 936 C CB . ASP A 118 ? 2.6572 0.9235 0.7288 0.6512 -0.0391 0.0022 206 ASP A CB 937 C CG . ASP A 118 ? 2.9324 1.0394 0.8460 0.6796 -0.0166 0.0132 206 ASP A CG 938 O OD1 . ASP A 118 ? 3.0285 1.1065 0.8686 0.7600 -0.0442 0.0044 206 ASP A OD1 939 O OD2 . ASP A 118 ? 2.9737 0.9844 0.8350 0.6214 0.0301 0.0290 206 ASP A OD2 940 N N . ALA A 119 ? 2.2448 0.8241 0.6179 0.6024 -0.0848 -0.0212 207 ALA A N 941 C CA . ALA A 119 ? 2.0767 0.7875 0.5792 0.5847 -0.1047 -0.0318 207 ALA A CA 942 C C . ALA A 119 ? 2.0593 0.8299 0.6417 0.5373 -0.0979 -0.0283 207 ALA A C 943 O O . ALA A 119 ? 1.9960 0.7077 0.5552 0.4843 -0.0627 -0.0118 207 ALA A O 944 C CB . ALA A 119 ? 2.0411 0.7453 0.5683 0.5470 -0.0871 -0.0224 207 ALA A CB 945 N N . VAL A 120 ? 2.0270 0.9199 0.7069 0.5554 -0.1309 -0.0460 208 VAL A N 946 C CA . VAL A 120 ? 1.9169 0.8722 0.6729 0.5188 -0.1300 -0.0430 208 VAL A CA 947 C C . VAL A 120 ? 1.7367 0.7956 0.6045 0.4904 -0.1390 -0.0484 208 VAL A C 948 O O . VAL A 120 ? 1.6933 0.8350 0.6133 0.5262 -0.1684 -0.0693 208 VAL A O 949 C CB . VAL A 120 ? 1.7524 0.7596 0.5183 0.5656 -0.1617 -0.0580 208 VAL A CB 950 C CG1 . VAL A 120 ? 1.6331 0.7262 0.4872 0.5271 -0.1665 -0.0560 208 VAL A CG1 951 C CG2 . VAL A 120 ? 1.8947 0.7912 0.5484 0.5853 -0.1477 -0.0471 208 VAL A CG2 952 N N . LEU A 121 ? 1.6135 0.6711 0.5172 0.4267 -0.1126 -0.0313 209 LEU A N 953 C CA . LEU A 121 ? 1.4709 0.6132 0.4684 0.3934 -0.1157 -0.0313 209 LEU A CA 954 C C . LEU A 121 ? 1.4136 0.6556 0.4843 0.3691 -0.1256 -0.0414 209 LEU A C 955 O O . LEU A 121 ? 1.5434 0.7512 0.5849 0.3418 -0.1089 -0.0283 209 LEU A O 956 C CB . LEU A 121 ? 1.4851 0.5738 0.4836 0.3297 -0.0736 -0.0122 209 LEU A CB 957 C CG . LEU A 121 ? 1.4227 0.6239 0.5487 0.2779 -0.0638 -0.0221 209 LEU A CG 958 C CD1 . LEU A 121 ? 1.3971 0.6670 0.5850 0.2979 -0.0796 -0.0411 209 LEU A CD1 959 C CD2 . LEU A 121 ? 1.2581 0.4216 0.3884 0.2137 -0.0236 -0.0068 209 LEU A CD2 960 N N . ARG A 122 ? 1.3623 0.7323 0.5383 0.3718 -0.1463 -0.0691 210 ARG A N 961 C CA . ARG A 122 ? 1.2384 0.7049 0.4935 0.3443 -0.1523 -0.0858 210 ARG A CA 962 C C . ARG A 122 ? 1.1687 0.7194 0.5374 0.2934 -0.1348 -0.0933 210 ARG A C 963 O O . ARG A 122 ? 1.1277 0.6738 0.5139 0.2863 -0.1238 -0.0888 210 ARG A O 964 C CB . ARG A 122 ? 1.2371 0.7772 0.5011 0.3971 -0.1948 -0.1173 210 ARG A CB 965 C CG . ARG A 122 ? 1.4328 0.8876 0.5867 0.4556 -0.2114 -0.1067 210 ARG A CG 966 C CD . ARG A 122 ? 1.5327 1.0724 0.7151 0.5024 -0.2484 -0.1383 210 ARG A CD 967 N NE . ARG A 122 ? 1.7574 1.2085 0.8484 0.5422 -0.2494 -0.1248 210 ARG A NE 968 C CZ . ARG A 122 ? 1.7825 1.2806 0.8720 0.5820 -0.2759 -0.1465 210 ARG A CZ 969 N NH1 . ARG A 122 ? 1.8110 1.2162 0.8052 0.6170 -0.2727 -0.1329 210 ARG A NH1 970 N NH2 . ARG A 122 ? 1.7681 1.4065 0.9500 0.5837 -0.3032 -0.1849 210 ARG A NH2 971 N N . PHE A 123 ? 1.0422 0.6618 0.4805 0.2587 -0.1308 -0.1043 211 PHE A N 972 C CA . PHE A 123 ? 0.9492 0.6253 0.4764 0.2100 -0.1091 -0.1041 211 PHE A CA 973 C C . PHE A 123 ? 0.9396 0.7235 0.5562 0.1999 -0.1203 -0.1344 211 PHE A C 974 O O . PHE A 123 ? 0.8268 0.6464 0.4501 0.2103 -0.1382 -0.1558 211 PHE A O 975 C CB . PHE A 123 ? 0.9075 0.5465 0.4331 0.1651 -0.0802 -0.0826 211 PHE A CB 976 C CG . PHE A 123 ? 1.0311 0.5757 0.4824 0.1601 -0.0609 -0.0566 211 PHE A CG 977 C CD1 . PHE A 123 ? 0.9799 0.5056 0.4365 0.1441 -0.0443 -0.0456 211 PHE A CD1 978 C CD2 . PHE A 123 ? 1.0607 0.5350 0.4337 0.1683 -0.0571 -0.0458 211 PHE A CD2 979 C CE1 . PHE A 123 ? 1.0161 0.4563 0.4065 0.1319 -0.0234 -0.0271 211 PHE A CE1 980 C CE2 . PHE A 123 ? 1.1066 0.4908 0.4094 0.1559 -0.0332 -0.0242 211 PHE A CE2 981 C CZ . PHE A 123 ? 1.1353 0.5033 0.4493 0.1356 -0.0161 -0.0164 211 PHE A CZ 982 N N . ASN A 124 ? 0.8486 0.6823 0.5308 0.1759 -0.1068 -0.1376 212 ASN A N 983 C CA . ASN A 124 ? 0.7937 0.7198 0.5603 0.1522 -0.1062 -0.1638 212 ASN A CA 984 C C . ASN A 124 ? 0.7933 0.7882 0.5754 0.1841 -0.1380 -0.2028 212 ASN A C 985 O O . ASN A 124 ? 0.9097 0.9235 0.6722 0.2303 -0.1612 -0.2167 212 ASN A O 986 C CB . ASN A 124 ? 0.7244 0.6382 0.5149 0.1073 -0.0839 -0.1531 212 ASN A CB 987 C CG . ASN A 124 ? 0.7938 0.6606 0.5781 0.0805 -0.0560 -0.1199 212 ASN A CG 988 O OD1 . ASN A 124 ? 0.7475 0.6278 0.5502 0.0755 -0.0468 -0.1132 212 ASN A OD1 989 N ND2 . ASN A 124 ? 0.8387 0.6569 0.5975 0.0649 -0.0431 -0.1019 212 ASN A ND2 990 N N . GLY A 125 ? 0.8155 0.8469 0.6285 0.1630 -0.1406 -0.2229 213 GLY A N 991 C CA . GLY A 125 ? 0.7704 0.8873 0.6118 0.1859 -0.1706 -0.2680 213 GLY A CA 992 C C . GLY A 125 ? 0.8995 0.9853 0.6746 0.2213 -0.1975 -0.2740 213 GLY A C 993 O O . GLY A 125 ? 0.9734 1.1301 0.7746 0.2282 -0.2199 -0.3136 213 GLY A O 994 N N . ALA A 126 ? 0.9409 0.9222 0.6279 0.2413 -0.1937 -0.2368 214 ALA A N 995 C CA . ALA A 126 ? 1.0088 0.9439 0.6173 0.2730 -0.2132 -0.2358 214 ALA A CA 996 C C . ALA A 126 ? 1.0542 1.0340 0.6328 0.3392 -0.2565 -0.2639 214 ALA A C 997 O O . ALA A 126 ? 1.0764 1.0266 0.6152 0.3807 -0.2658 -0.2525 214 ALA A O 998 C CB . ALA A 126 ? 1.0539 0.8646 0.5724 0.2750 -0.1929 -0.1897 214 ALA A CB 999 N N . PRO A 127 ? 1.0130 1.0674 0.6111 0.3514 -0.2840 -0.3039 215 PRO A N 1000 C CA . PRO A 127 ? 1.0298 1.1590 0.6386 0.4082 -0.3197 -0.3330 215 PRO A CA 1001 C C . PRO A 127 ? 1.1659 1.2177 0.6769 0.4665 -0.3347 -0.3099 215 PRO A C 1002 O O . PRO A 127 ? 1.1670 1.1240 0.6070 0.4554 -0.3202 -0.2791 215 PRO A O 1003 C CB . PRO A 127 ? 1.0151 1.2594 0.7130 0.3739 -0.3264 -0.3814 215 PRO A CB 1004 C CG . PRO A 127 ? 0.9372 1.1166 0.6102 0.3259 -0.3045 -0.3665 215 PRO A CG 1005 C CD . PRO A 127 ? 1.0309 1.1109 0.6714 0.3007 -0.2710 -0.3203 215 PRO A CD 1006 N N . THR A 128 ? 1.2690 1.3652 0.7789 0.5287 -0.3607 -0.3288 216 THR A N 1007 C CA . THR A 128 ? 1.3778 1.4053 0.7949 0.5934 -0.3758 -0.3148 216 THR A CA 1008 C C . THR A 128 ? 1.3739 1.4913 0.8199 0.6128 -0.4011 -0.3540 216 THR A C 1009 O O . THR A 128 ? 1.4933 1.5501 0.8662 0.6344 -0.4059 -0.3399 216 THR A O 1010 C CB . THR A 128 ? 1.4633 1.4682 0.8459 0.6579 -0.3860 -0.3146 216 THR A CB 1011 O OG1 . THR A 128 ? 1.4540 1.3359 0.7737 0.6468 -0.3607 -0.2706 216 THR A OG1 1012 C CG2 . THR A 128 ? 1.6870 1.6525 0.9884 0.7310 -0.4060 -0.3190 216 THR A CG2 1013 N N . ALA A 129 ? 1.2916 1.5548 0.8445 0.6023 -0.4144 -0.4049 217 ALA A N 1014 C CA . ALA A 129 ? 1.3666 1.7334 0.9618 0.6138 -0.4366 -0.4506 217 ALA A CA 1015 C C . ALA A 129 ? 1.4180 1.7524 0.9933 0.5710 -0.4292 -0.4428 217 ALA A C 1016 O O . ALA A 129 ? 1.3767 1.6862 0.9771 0.5047 -0.4044 -0.4307 217 ALA A O 1017 C CB . ALA A 129 ? 1.2383 1.7623 0.9628 0.5834 -0.4383 -0.5059 217 ALA A CB 1018 N N . ASN A 130 ? 1.5196 1.8517 1.0452 0.6122 -0.4498 -0.4517 218 ASN A N 1019 C CA . ASN A 130 ? 1.5049 1.8136 1.0049 0.5815 -0.4465 -0.4503 218 ASN A CA 1020 C C . ASN A 130 ? 1.5603 1.7164 0.9552 0.5718 -0.4238 -0.3933 218 ASN A C 1021 O O . ASN A 130 ? 1.6377 1.7660 1.0012 0.5500 -0.4183 -0.3902 218 ASN A O 1022 C CB . ASN A 130 ? 1.4475 1.8429 1.0499 0.5033 -0.4334 -0.4865 218 ASN A CB 1023 C CG . ASN A 130 ? 1.4534 2.0019 1.1672 0.4990 -0.4465 -0.5452 218 ASN A CG 1024 O OD1 . ASN A 130 ? 1.5250 2.1474 1.2445 0.5509 -0.4740 -0.5778 218 ASN A OD1 1025 N ND2 . ASN A 130 ? 1.3488 1.9456 1.1504 0.4361 -0.4237 -0.5609 218 ASN A ND2 1026 N N . PHE A 131 ? 1.3941 1.4534 0.7352 0.5861 -0.4080 -0.3513 219 PHE A N 1027 C CA . PHE A 131 ? 1.4163 1.3372 0.6716 0.5638 -0.3776 -0.2997 219 PHE A CA 1028 C C . PHE A 131 ? 1.5216 1.3228 0.6687 0.6190 -0.3736 -0.2612 219 PHE A C 1029 O O . PHE A 131 ? 1.5491 1.2315 0.6250 0.5995 -0.3435 -0.2187 219 PHE A O 1030 C CB . PHE A 131 ? 1.3165 1.2206 0.6168 0.5002 -0.3474 -0.2848 219 PHE A CB 1031 C CG . PHE A 131 ? 1.3116 1.3053 0.7056 0.4400 -0.3424 -0.3204 219 PHE A CG 1032 C CD1 . PHE A 131 ? 1.2276 1.1976 0.6063 0.4037 -0.3284 -0.3212 219 PHE A CD1 1033 C CD2 . PHE A 131 ? 1.1982 1.2950 0.6937 0.4185 -0.3481 -0.3552 219 PHE A CD2 1034 C CE1 . PHE A 131 ? 1.3382 1.3753 0.7972 0.3489 -0.3203 -0.3561 219 PHE A CE1 1035 C CE2 . PHE A 131 ? 1.2249 1.3903 0.8027 0.3588 -0.3377 -0.3892 219 PHE A CE2 1036 C CZ . PHE A 131 ? 1.2637 1.3936 0.8210 0.3248 -0.3239 -0.3894 219 PHE A CZ 1037 N N . GLN A 132 ? 1.5877 1.4186 0.7222 0.6859 -0.4004 -0.2798 220 GLN A N 1038 C CA . GLN A 132 ? 1.7678 1.4776 0.7961 0.7409 -0.3946 -0.2496 220 GLN A CA 1039 C C . GLN A 132 ? 1.8579 1.4273 0.7706 0.7381 -0.3709 -0.2083 220 GLN A C 1040 O O . GLN A 132 ? 1.8428 1.2869 0.6836 0.7323 -0.3417 -0.1712 220 GLN A O 1041 C CB . GLN A 132 ? 1.8634 1.6271 0.8804 0.8216 -0.4290 -0.2831 220 GLN A CB 1042 C CG . GLN A 132 ? 1.7300 1.5870 0.8270 0.8381 -0.4418 -0.3143 220 GLN A CG 1043 C CD . GLN A 132 ? 1.7095 1.7480 0.9282 0.8291 -0.4679 -0.3714 220 GLN A CD 1044 O OE1 . GLN A 132 ? 1.5933 1.6941 0.8793 0.7685 -0.4631 -0.3827 220 GLN A OE1 1045 N NE2 . GLN A 132 ? 1.6940 1.8167 0.9387 0.8870 -0.4924 -0.4116 220 GLN A NE2 1046 N N . GLN A 133 ? 1.8808 1.4730 0.7773 0.7373 -0.3805 -0.2175 221 GLN A N 1047 C CA . GLN A 133 ? 1.9675 1.4335 0.7510 0.7399 -0.3586 -0.1822 221 GLN A CA 1048 C C . GLN A 133 ? 1.8998 1.2918 0.6727 0.6678 -0.3147 -0.1476 221 GLN A C 1049 O O . GLN A 133 ? 1.9912 1.2593 0.6698 0.6639 -0.2853 -0.1133 221 GLN A O 1050 C CB . GLN A 133 ? 2.0688 1.5775 0.8265 0.7686 -0.3830 -0.2030 221 GLN A CB 1051 C CG . GLN A 133 ? 1.8988 1.5164 0.7406 0.7185 -0.3907 -0.2319 221 GLN A CG 1052 C CD . GLN A 133 ? 2.1287 1.7845 0.9350 0.7553 -0.4174 -0.2550 221 GLN A CD 1053 O OE1 . GLN A 133 ? 2.2077 1.8471 0.9535 0.8264 -0.4403 -0.2603 221 GLN A OE1 1054 N NE2 . GLN A 133 ? 1.9383 1.6410 0.7763 0.7092 -0.4137 -0.2706 221 GLN A NE2 1055 N N . ASP A 134 ? 1.7448 1.2135 0.6135 0.6105 -0.3082 -0.1597 222 ASP A N 1056 C CA . ASP A 134 ? 1.7572 1.1677 0.6260 0.5449 -0.2664 -0.1317 222 ASP A CA 1057 C C . ASP A 134 ? 1.7262 1.0848 0.6022 0.5272 -0.2441 -0.1095 222 ASP A C 1058 O O . ASP A 134 ? 1.7014 0.9707 0.5372 0.4905 -0.2054 -0.0784 222 ASP A O 1059 C CB . ASP A 134 ? 1.5765 1.0824 0.5345 0.4912 -0.2658 -0.1573 222 ASP A CB 1060 C CG . ASP A 134 ? 1.6577 1.1893 0.5964 0.4912 -0.2742 -0.1739 222 ASP A CG 1061 O OD1 . ASP A 134 ? 1.7474 1.2048 0.5941 0.5217 -0.2706 -0.1548 222 ASP A OD1 1062 O OD2 . ASP A 134 ? 1.5413 1.1611 0.5532 0.4589 -0.2819 -0.2073 222 ASP A OD2 1063 N N . VAL A 135 ? 1.7332 1.1526 0.6620 0.5522 -0.2671 -0.1284 223 VAL A N 1064 C CA . VAL A 135 ? 1.7235 1.1253 0.6837 0.5265 -0.2494 -0.1159 223 VAL A CA 1065 C C . VAL A 135 ? 1.7816 1.1168 0.6880 0.5761 -0.2528 -0.1071 223 VAL A C 1066 O O . VAL A 135 ? 1.6711 0.9464 0.5664 0.5547 -0.2287 -0.0879 223 VAL A O 1067 C CB . VAL A 135 ? 1.4288 0.9627 0.5070 0.5005 -0.2663 -0.1488 223 VAL A CB 1068 C CG1 . VAL A 135 ? 2.2114 1.7288 1.3195 0.4698 -0.2464 -0.1353 223 VAL A CG1 1069 C CG2 . VAL A 135 ? 1.3651 0.9548 0.4900 0.4527 -0.2606 -0.1646 223 VAL A CG2 1070 N N . GLY A 136 ? 1.7250 1.0689 0.5938 0.6426 -0.2813 -0.1243 224 GLY A N 1071 C CA . GLY A 136 ? 1.8066 1.1046 0.6280 0.6984 -0.2892 -0.1278 224 GLY A CA 1072 C C . GLY A 136 ? 1.8390 1.2732 0.7483 0.7340 -0.3261 -0.1695 224 GLY A C 1073 O O . GLY A 136 ? 1.6664 1.2280 0.6779 0.7061 -0.3418 -0.1950 224 GLY A O 1074 N N . THR A 137 ? 1.9306 1.3396 0.7989 0.7920 -0.3369 -0.1806 225 THR A N 1075 C CA . THR A 137 ? 1.9008 1.4417 0.8506 0.8281 -0.3680 -0.2240 225 THR A CA 1076 C C . THR A 137 ? 1.8251 1.3525 0.7917 0.8222 -0.3563 -0.2220 225 THR A C 1077 O O . THR A 137 ? 1.7998 1.4485 0.8558 0.8306 -0.3743 -0.2559 225 THR A O 1078 C CB . THR A 137 ? 2.0764 1.6338 0.9730 0.9119 -0.3978 -0.2522 225 THR A CB 1079 O OG1 . THR A 137 ? 2.1930 1.7318 1.0467 0.9210 -0.4050 -0.2469 225 THR A OG1 1080 C CG2 . THR A 137 ? 1.8477 1.5782 0.8512 0.9392 -0.4304 -0.3066 225 THR A CG2 1081 N N . LYS A 138 ? 1.8051 1.1899 0.6874 0.8031 -0.3240 -0.1852 226 LYS A N 1082 C CA . LYS A 138 ? 1.7998 1.1586 0.6776 0.8023 -0.3132 -0.1839 226 LYS A CA 1083 C C . LYS A 138 ? 1.9640 1.3420 0.9138 0.7317 -0.2916 -0.1670 226 LYS A C 1084 O O . LYS A 138 ? 1.6358 0.9667 0.5821 0.6773 -0.2677 -0.1391 226 LYS A O 1085 C CB . LYS A 138 ? 1.9541 1.1513 0.6895 0.8269 -0.2922 -0.1614 226 LYS A CB 1086 C CG . LYS A 138 ? 2.3956 1.5768 1.1088 0.8464 -0.2920 -0.1685 226 LYS A CG 1087 C CD . LYS A 138 ? 2.5915 1.6318 1.1572 0.8891 -0.2820 -0.1555 226 LYS A CD 1088 C CE . LYS A 138 ? 2.6130 1.6344 1.1543 0.9033 -0.2816 -0.1578 226 LYS A CE 1089 N NZ . LYS A 138 ? 2.7769 1.6717 1.1743 0.9563 -0.2780 -0.1497 226 LYS A NZ 1090 N N . THR A 139 ? 1.9580 1.4100 0.9713 0.7345 -0.3001 -0.1857 227 THR A N 1091 C CA . THR A 139 ? 1.7928 1.2595 0.8653 0.6768 -0.2811 -0.1707 227 THR A CA 1092 C C . THR A 139 ? 1.7501 1.1671 0.7813 0.6912 -0.2726 -0.1677 227 THR A C 1093 O O . THR A 139 ? 1.6188 1.1154 0.6826 0.7321 -0.2954 -0.1981 227 THR A O 1094 C CB . THR A 139 ? 1.6979 1.3342 0.9083 0.6571 -0.3014 -0.2013 227 THR A CB 1095 O OG1 . THR A 139 ? 1.8351 1.5357 1.0824 0.6449 -0.3142 -0.2136 227 THR A OG1 1096 C CG2 . THR A 139 ? 1.4808 1.1252 0.7387 0.5948 -0.2809 -0.1838 227 THR A CG2 1097 N N . THR A 140 ? 1.5901 0.8837 0.5513 0.6543 -0.2392 -0.1328 228 THR A N 1098 C CA . THR A 140 ? 1.7536 1.0061 0.6845 0.6575 -0.2302 -0.1253 228 THR A CA 1099 C C . THR A 140 ? 1.5746 0.8731 0.5949 0.6060 -0.2151 -0.1166 228 THR A C 1100 O O . THR A 140 ? 1.5661 0.9270 0.6400 0.6201 -0.2239 -0.1321 228 THR A O 1101 C CB . THR A 140 ? 2.0121 1.1052 0.8118 0.6532 -0.2020 -0.0974 228 THR A CB 1102 O OG1 . THR A 140 ? 2.0313 1.0496 0.7886 0.6144 -0.1760 -0.0769 228 THR A OG1 1103 C CG2 . THR A 140 ? 2.2439 1.3030 0.9588 0.7268 -0.2233 -0.1130 228 THR A CG2 1104 N N . ILE A 141 ? 1.4927 0.7629 0.5326 0.5480 -0.1899 -0.0953 229 ILE A N 1105 C CA . ILE A 141 ? 1.4019 0.7190 0.5351 0.4994 -0.1706 -0.0956 229 ILE A CA 1106 C C . ILE A 141 ? 1.3097 0.7246 0.5319 0.4531 -0.1685 -0.1028 229 ILE A C 1107 O O . ILE A 141 ? 1.5211 0.8982 0.7067 0.4378 -0.1639 -0.0886 229 ILE A O 1108 C CB . ILE A 141 ? 1.5186 0.7368 0.6125 0.4418 -0.1291 -0.0674 229 ILE A CB 1109 C CG1 . ILE A 141 ? 1.6801 0.8231 0.7002 0.4613 -0.1233 -0.0596 229 ILE A CG1 1110 C CG2 . ILE A 141 ? 1.4557 0.7450 0.6493 0.3890 -0.1092 -0.0764 229 ILE A CG2 1111 C CD1 . ILE A 141 ? 1.4750 0.5369 0.4688 0.4011 -0.0823 -0.0397 229 ILE A CD1 1112 N N . ARG A 142 ? 1.1768 0.7168 0.5131 0.4276 -0.1690 -0.1246 230 ARG A N 1113 C CA . ARG A 142 ? 1.0640 0.6870 0.4841 0.3743 -0.1600 -0.1290 230 ARG A CA 1114 C C . ARG A 142 ? 1.0842 0.7330 0.5700 0.3127 -0.1280 -0.1194 230 ARG A C 1115 O O . ARG A 142 ? 1.0033 0.7089 0.5397 0.3132 -0.1262 -0.1333 230 ARG A O 1116 C CB . ARG A 142 ? 1.0294 0.7817 0.5236 0.3967 -0.1887 -0.1666 230 ARG A CB 1117 C CG . ARG A 142 ? 0.9345 0.7674 0.5161 0.3390 -0.1763 -0.1749 230 ARG A CG 1118 C CD . ARG A 142 ? 0.9623 0.9208 0.6143 0.3556 -0.2021 -0.2180 230 ARG A CD 1119 N NE . ARG A 142 ? 1.0897 1.0443 0.6840 0.4168 -0.2394 -0.2338 230 ARG A NE 1120 C CZ . ARG A 142 ? 1.1372 1.0872 0.7098 0.4143 -0.2506 -0.2373 230 ARG A CZ 1121 N NH1 . ARG A 142 ? 0.9671 0.9105 0.5715 0.3538 -0.2257 -0.2260 230 ARG A NH1 1122 N NH2 . ARG A 142 ? 1.2382 1.1867 0.7509 0.4769 -0.2873 -0.2522 230 ARG A NH2 1123 N N . LEU A 143 ? 1.1510 0.7607 0.6325 0.2635 -0.1032 -0.0967 231 LEU A N 1124 C CA . LEU A 143 ? 0.9753 0.6138 0.5147 0.2101 -0.0762 -0.0873 231 LEU A CA 1125 C C . LEU A 143 ? 0.9188 0.6457 0.5411 0.1790 -0.0734 -0.0961 231 LEU A C 1126 O O . LEU A 143 ? 0.9167 0.6398 0.5349 0.1705 -0.0758 -0.0943 231 LEU A O 1127 C CB . LEU A 143 ? 0.9436 0.4989 0.4356 0.1755 -0.0503 -0.0614 231 LEU A CB 1128 C CG . LEU A 143 ? 0.8683 0.4653 0.4206 0.1268 -0.0273 -0.0539 231 LEU A CG 1129 C CD1 . LEU A 143 ? 0.8861 0.4977 0.4524 0.1299 -0.0236 -0.0606 231 LEU A CD1 1130 C CD2 . LEU A 143 ? 0.8749 0.4225 0.4008 0.0901 -0.0038 -0.0357 231 LEU A CD2 1131 N N . MET A 144 ? 0.8447 0.6426 0.5356 0.1604 -0.0653 -0.1054 232 MET A N 1132 C CA . MET A 144 ? 0.7127 0.5833 0.4756 0.1297 -0.0584 -0.1144 232 MET A CA 1133 C C . MET A 144 ? 0.7248 0.6044 0.5207 0.0895 -0.0319 -0.0974 232 MET A C 1134 O O . MET A 144 ? 0.6945 0.5616 0.4799 0.0891 -0.0236 -0.0899 232 MET A O 1135 C CB . MET A 144 ? 0.6252 0.5855 0.4414 0.1463 -0.0726 -0.1475 232 MET A CB 1136 C CG . MET A 144 ? 0.7798 0.7413 0.5594 0.2017 -0.1041 -0.1677 232 MET A CG 1137 S SD . MET A 144 ? 0.8436 0.9291 0.6926 0.2262 -0.1212 -0.2131 232 MET A SD 1138 C CE . MET A 144 ? 0.9839 1.0776 0.8524 0.2142 -0.0979 -0.2052 232 MET A CE 1139 N N . ASN A 145 ? 0.6963 0.5945 0.5271 0.0586 -0.0191 -0.0922 233 ASN A N 1140 C CA . ASN A 145 ? 0.7331 0.6411 0.5903 0.0280 0.0041 -0.0756 233 ASN A CA 1141 C C . ASN A 145 ? 0.6524 0.6256 0.5606 0.0173 0.0123 -0.0903 233 ASN A C 1142 O O . ASN A 145 ? 0.5719 0.5938 0.5092 0.0252 0.0019 -0.1171 233 ASN A O 1143 C CB . ASN A 145 ? 0.6497 0.5343 0.5099 0.0050 0.0169 -0.0598 233 ASN A CB 1144 C CG . ASN A 145 ? 0.7249 0.6324 0.6141 -0.0041 0.0147 -0.0764 233 ASN A CG 1145 O OD1 . ASN A 145 ? 0.7021 0.6542 0.6332 -0.0187 0.0220 -0.0905 233 ASN A OD1 1146 N ND2 . ASN A 145 ? 0.7034 0.5794 0.5690 0.0005 0.0078 -0.0766 233 ASN A ND2 1147 N N . SER A 146 ? 0.6159 0.5945 0.5335 -0.0010 0.0316 -0.0748 234 SER A N 1148 C CA . SER A 146 ? 0.5777 0.6119 0.5335 -0.0131 0.0450 -0.0862 234 SER A CA 1149 C C . SER A 146 ? 0.5702 0.6314 0.5654 -0.0411 0.0592 -0.0958 234 SER A C 1150 O O . SER A 146 ? 0.5984 0.7148 0.6314 -0.0548 0.0707 -0.1153 234 SER A O 1151 C CB . SER A 146 ? 0.5454 0.5705 0.4885 -0.0238 0.0626 -0.0643 234 SER A CB 1152 O OG . SER A 146 ? 0.5494 0.5368 0.4786 -0.0394 0.0739 -0.0384 234 SER A OG 1153 N N . GLN A 147 ? 0.5989 0.6201 0.5846 -0.0524 0.0617 -0.0845 235 GLN A N 1154 C CA . GLN A 147 ? 0.6860 0.7160 0.7014 -0.0823 0.0783 -0.0941 235 GLN A CA 1155 C C . GLN A 147 ? 0.6366 0.7256 0.6889 -0.0813 0.0642 -0.1348 235 GLN A C 1156 O O . GLN A 147 ? 0.7513 0.8829 0.8444 -0.1102 0.0810 -0.1562 235 GLN A O 1157 C CB . GLN A 147 ? 0.8426 0.8137 0.8355 -0.0875 0.0809 -0.0772 235 GLN A CB 1158 C CG . GLN A 147 ? 0.8688 0.8346 0.8850 -0.1172 0.0965 -0.0915 235 GLN A CG 1159 C CD . GLN A 147 ? 1.0376 0.9446 1.0282 -0.1147 0.0962 -0.0784 235 GLN A CD 1160 O OE1 . GLN A 147 ? 1.1758 1.0800 1.1562 -0.0989 0.0755 -0.0906 235 GLN A OE1 1161 N NE2 . GLN A 147 ? 1.0532 0.9109 1.0275 -0.1260 0.1194 -0.0533 235 GLN A NE2 1162 N N . LEU A 148 ? 0.6068 0.6981 0.6411 -0.0476 0.0340 -0.1465 236 LEU A N 1163 C CA . LEU A 148 ? 0.5871 0.7397 0.6492 -0.0345 0.0123 -0.1868 236 LEU A CA 1164 C C . LEU A 148 ? 0.6676 0.9008 0.7696 -0.0284 0.0124 -0.2129 236 LEU A C 1165 O O . LEU A 148 ? 0.6779 0.9876 0.8317 -0.0430 0.0130 -0.2509 236 LEU A O 1166 C CB . LEU A 148 ? 0.6380 0.7587 0.6524 0.0084 -0.0196 -0.1859 236 LEU A CB 1167 C CG . LEU A 148 ? 0.7354 0.9121 0.7602 0.0378 -0.0510 -0.2250 236 LEU A CG 1168 C CD1 . LEU A 148 ? 0.7874 0.9032 0.7525 0.0639 -0.0711 -0.2143 236 LEU A CD1 1169 C CD2 . LEU A 148 ? 0.7959 1.0224 0.8252 0.0772 -0.0690 -0.2429 236 LEU A CD2 1170 N N . VAL A 149 ? 0.7105 0.9316 0.7905 -0.0082 0.0131 -0.1964 237 VAL A N 1171 C CA . VAL A 149 ? 0.6446 0.9405 0.7586 0.0022 0.0146 -0.2210 237 VAL A CA 1172 C C . VAL A 149 ? 0.5278 0.8654 0.6876 -0.0466 0.0514 -0.2263 237 VAL A C 1173 O O . VAL A 149 ? 0.5608 0.9870 0.7732 -0.0559 0.0575 -0.2627 237 VAL A O 1174 C CB . VAL A 149 ? 0.6667 0.9274 0.7382 0.0345 0.0084 -0.2025 237 VAL A CB 1175 C CG1 . VAL A 149 ? 0.5234 0.8613 0.6302 0.0437 0.0152 -0.2276 237 VAL A CG1 1176 C CG2 . VAL A 149 ? 0.6801 0.8936 0.6999 0.0817 -0.0242 -0.2010 237 VAL A CG2 1177 N N . THR A 150 ? 0.4748 0.7486 0.6122 -0.0774 0.0774 -0.1910 238 THR A N 1178 C CA . THR A 150 ? 0.5633 0.8533 0.7269 -0.1242 0.1165 -0.1899 238 THR A CA 1179 C C . THR A 150 ? 0.5950 0.9134 0.8008 -0.1636 0.1298 -0.2184 238 THR A C 1180 O O . THR A 150 ? 0.6385 1.0218 0.8902 -0.1963 0.1534 -0.2465 238 THR A O 1181 C CB . THR A 150 ? 0.6227 0.8290 0.7395 -0.1379 0.1384 -0.1423 238 THR A CB 1182 O OG1 . THR A 150 ? 0.7305 0.9155 0.8105 -0.1054 0.1247 -0.1214 238 THR A OG1 1183 C CG2 . THR A 150 ? 0.6304 0.8416 0.7574 -0.1804 0.1812 -0.1364 238 THR A CG2 1184 N N . THR A 151 ? 0.7097 0.9812 0.9003 -0.1642 0.1174 -0.2144 239 THR A N 1185 C CA . THR A 151 ? 0.7030 0.9807 0.9244 -0.2090 0.1363 -0.2379 239 THR A CA 1186 C C . THR A 151 ? 0.6931 1.0343 0.9508 -0.2014 0.1072 -0.2857 239 THR A C 1187 O O . THR A 151 ? 0.6928 1.0736 0.9936 -0.2438 0.1238 -0.3211 239 THR A O 1188 C CB . THR A 151 ? 0.7191 0.8897 0.8968 -0.2276 0.1558 -0.2007 239 THR A CB 1189 O OG1 . THR A 151 ? 0.7350 0.8642 0.8810 -0.1938 0.1249 -0.1899 239 THR A OG1 1190 C CG2 . THR A 151 ? 0.6976 0.8109 0.8340 -0.2270 0.1795 -0.1540 239 THR A CG2 1191 N N . GLU A 152 ? 0.6935 1.0431 0.9303 -0.1493 0.0655 -0.2887 240 GLU A N 1192 C CA . GLU A 152 ? 0.6255 1.0383 0.8878 -0.1336 0.0337 -0.3339 240 GLU A CA 1193 C C . GLU A 152 ? 0.7101 1.2517 1.0342 -0.1256 0.0225 -0.3851 240 GLU A C 1194 O O . GLU A 152 ? 0.7531 1.3293 1.0674 -0.0738 -0.0046 -0.3890 240 GLU A O 1195 C CB . GLU A 152 ? 0.7191 1.0849 0.9241 -0.0784 -0.0052 -0.3175 240 GLU A CB 1196 C CG . GLU A 152 ? 0.7663 1.1797 0.9809 -0.0607 -0.0382 -0.3585 240 GLU A CG 1197 C CD . GLU A 152 ? 0.8127 1.2461 1.0691 -0.1160 -0.0186 -0.3887 240 GLU A CD 1198 O OE1 . GLU A 152 ? 0.7771 1.3149 1.0981 -0.1371 -0.0195 -0.4413 240 GLU A OE1 1199 O OE2 . GLU A 152 ? 0.8508 1.1965 1.0763 -0.1392 -0.0007 -0.3625 240 GLU A OE2 1200 N N . LYS A 153 ? 0.7498 1.3621 1.1369 -0.1770 0.0444 -0.4274 241 LYS A N 1201 C CA . LYS A 153 ? 0.7076 1.4613 1.1675 -0.1792 0.0401 -0.4838 241 LYS A CA 1202 C C . LYS A 153 ? 0.6035 1.4338 1.0679 -0.1121 -0.0158 -0.5183 241 LYS A C 1203 O O . LYS A 153 ? 0.5337 1.4732 1.0406 -0.0835 -0.0309 -0.5547 241 LYS A O 1204 C CB . LYS A 153 ? 0.8284 1.6410 1.3536 -0.2537 0.0734 -0.5293 241 LYS A CB 1205 C CG . LYS A 153 ? 0.9452 1.6562 1.4482 -0.3184 0.1299 -0.4923 241 LYS A CG 1206 C CD . LYS A 153 ? 1.0654 1.7713 1.5880 -0.3767 0.1592 -0.5221 241 LYS A CD 1207 C CE . LYS A 153 ? 1.1376 1.6998 1.6078 -0.4195 0.2001 -0.4763 241 LYS A CE 1208 N NZ . LYS A 153 ? 1.2299 1.7641 1.7001 -0.4603 0.2206 -0.5007 241 LYS A NZ 1209 N N . ARG A 154 ? 0.6872 1.4583 1.1025 -0.0834 -0.0460 -0.5067 242 ARG A N 1210 C CA . ARG A 154 ? 0.7613 1.5827 1.1594 -0.0133 -0.0997 -0.5318 242 ARG A CA 1211 C C . ARG A 154 ? 0.6873 1.4738 1.0337 0.0537 -0.1197 -0.5009 242 ARG A C 1212 O O . ARG A 154 ? 0.7070 1.5468 1.0422 0.1186 -0.1610 -0.5251 242 ARG A O 1213 C CB . ARG A 154 ? 0.8389 1.5926 1.1848 -0.0012 -0.1224 -0.5229 242 ARG A CB 1214 C CG . ARG A 154 ? 0.9046 1.7262 1.3039 -0.0466 -0.1211 -0.5756 242 ARG A CG 1215 C CD . ARG A 154 ? 0.9699 1.7420 1.3119 -0.0173 -0.1534 -0.5738 242 ARG A CD 1216 N NE . ARG A 154 ? 1.0378 1.6601 1.3059 -0.0222 -0.1355 -0.5108 242 ARG A NE 1217 C CZ . ARG A 154 ? 1.1401 1.6964 1.3491 -0.0034 -0.1529 -0.4985 242 ARG A CZ 1218 N NH1 . ARG A 154 ? 1.1684 1.6018 1.3193 -0.0100 -0.1330 -0.4446 242 ARG A NH1 1219 N NH2 . ARG A 154 ? 1.1840 1.8042 1.3919 0.0232 -0.1905 -0.5426 242 ARG A NH2 1220 N N . PHE A 155 ? 0.6977 1.3932 1.0085 0.0407 -0.0914 -0.4495 243 PHE A N 1221 C CA . PHE A 155 ? 0.7275 1.3770 0.9836 0.0986 -0.1074 -0.4215 243 PHE A CA 1222 C C . PHE A 155 ? 0.6792 1.4373 0.9778 0.1355 -0.1203 -0.4596 243 PHE A C 1223 O O . PHE A 155 ? 0.7500 1.4987 1.0056 0.2048 -0.1527 -0.4598 243 PHE A O 1224 C CB . PHE A 155 ? 0.6881 1.2349 0.9046 0.0751 -0.0752 -0.3666 243 PHE A CB 1225 C CG . PHE A 155 ? 0.7402 1.2483 0.9082 0.1261 -0.0876 -0.3466 243 PHE A CG 1226 C CD1 . PHE A 155 ? 0.7720 1.2163 0.8688 0.1830 -0.1202 -0.3338 243 PHE A CD1 1227 C CD2 . PHE A 155 ? 0.7282 1.2595 0.9161 0.1176 -0.0652 -0.3427 243 PHE A CD2 1228 C CE1 . PHE A 155 ? 0.7612 1.1574 0.8070 0.2279 -0.1286 -0.3177 243 PHE A CE1 1229 C CE2 . PHE A 155 ? 0.6442 1.1356 0.7851 0.1642 -0.0761 -0.3286 243 PHE A CE2 1230 C CZ . PHE A 155 ? 0.6811 1.1019 0.7512 0.2181 -0.1072 -0.3166 243 PHE A CZ 1231 N N . LEU A 156 ? 0.6185 1.4756 0.9976 0.0897 -0.0924 -0.4923 244 LEU A N 1232 C CA . LEU A 156 ? 0.5868 1.5658 1.0177 0.1212 -0.1013 -0.5356 244 LEU A CA 1233 C C . LEU A 156 ? 0.6356 1.7448 1.1136 0.1589 -0.1422 -0.5995 244 LEU A C 1234 O O . LEU A 156 ? 0.6106 1.7867 1.0991 0.1951 -0.1496 -0.6295 244 LEU A O 1235 C CB . LEU A 156 ? 0.6361 1.6753 1.1330 0.0553 -0.0509 -0.5474 244 LEU A CB 1236 C CG . LEU A 156 ? 0.6406 1.5651 1.0903 0.0235 -0.0123 -0.4879 244 LEU A CG 1237 C CD1 . LEU A 156 ? 0.6804 1.6716 1.1865 -0.0311 0.0357 -0.5028 244 LEU A CD1 1238 C CD2 . LEU A 156 ? 0.6034 1.4504 0.9813 0.0867 -0.0337 -0.4536 244 LEU A CD2 1239 N N . LYS A 157 ? 0.7402 1.8327 1.2058 0.1499 -0.1598 -0.6075 245 LYS A N 1240 C CA . LYS A 157 ? 0.8085 1.9770 1.2892 0.1739 -0.1795 -0.6555 245 LYS A CA 1241 C C . LYS A 157 ? 0.7923 1.9168 1.2005 0.2512 -0.2286 -0.6491 245 LYS A C 1242 O O . LYS A 157 ? 0.8063 1.9833 1.2023 0.3121 -0.2536 -0.6790 245 LYS A O 1243 C CB . LYS A 157 ? 0.8774 2.0792 1.4113 0.0956 -0.1498 -0.6811 245 LYS A CB 1244 C CG . LYS A 157 ? 0.9325 2.1743 1.5280 0.0166 -0.0954 -0.6941 245 LYS A CG 1245 C CD . LYS A 157 ? 1.0185 2.2530 1.6430 -0.0583 -0.0653 -0.7099 245 LYS A CD 1246 C CE . LYS A 157 ? 1.0796 2.3136 1.7409 -0.1398 -0.0053 -0.7106 245 LYS A CE 1247 N NZ . LYS A 157 ? 1.1165 2.3085 1.7873 -0.2110 0.0273 -0.7164 245 LYS A NZ 1248 N N . ASP A 158 ? 0.7995 1.8222 1.1520 0.2470 -0.2398 -0.6110 246 ASP A N 1249 C CA . ASP A 158 ? 0.9104 1.8810 1.1889 0.3072 -0.2775 -0.6028 246 ASP A CA 1250 C C . ASP A 158 ? 0.9406 1.8543 1.1375 0.3973 -0.3067 -0.5815 246 ASP A C 1251 O O . ASP A 158 ? 0.9505 1.7873 1.1037 0.4093 -0.3036 -0.5440 246 ASP A O 1252 C CB . ASP A 158 ? 0.9416 1.8075 1.1700 0.2737 -0.2761 -0.5682 246 ASP A CB 1253 C CG . ASP A 158 ? 1.0441 1.9578 1.3294 0.2114 -0.2593 -0.5985 246 ASP A CG 1254 O OD1 . ASP A 158 ? 1.0648 2.0919 1.4283 0.1898 -0.2466 -0.6455 246 ASP A OD1 1255 O OD2 . ASP A 158 ? 1.0870 1.9196 1.3333 0.1834 -0.2557 -0.5771 246 ASP A OD2 1256 N N . SER A 159 ? 0.9779 1.9234 1.1488 0.4599 -0.3333 -0.6070 247 SER A N 1257 C CA . SER A 159 ? 1.0219 1.9093 1.1079 0.5471 -0.3575 -0.5942 247 SER A CA 1258 C C . SER A 159 ? 1.0636 1.7840 1.0354 0.5765 -0.3658 -0.5326 247 SER A C 1259 O O . SER A 159 ? 1.1439 1.7855 1.0342 0.6372 -0.3763 -0.5137 247 SER A O 1260 C CB . SER A 159 ? 1.0742 2.0243 1.1474 0.6055 -0.3843 -0.6360 247 SER A CB 1261 O OG . SER A 159 ? 1.0468 1.9606 1.0889 0.6060 -0.3971 -0.6269 247 SER A OG 1262 N N . LEU A 160 ? 1.0713 1.7288 1.0274 0.5296 -0.3576 -0.5030 248 LEU A N 1263 C CA . LEU A 160 ? 1.1840 1.6805 1.0248 0.5500 -0.3601 -0.4469 248 LEU A CA 1264 C C . LEU A 160 ? 1.1623 1.5731 0.9618 0.5463 -0.3454 -0.4095 248 LEU A C 1265 O O . LEU A 160 ? 1.3194 1.6050 1.0166 0.5901 -0.3481 -0.3735 248 LEU A O 1266 C CB . LEU A 160 ? 1.2457 1.6982 1.0757 0.4955 -0.3505 -0.4295 248 LEU A CB 1267 C CG . LEU A 160 ? 1.3806 1.6656 1.0905 0.5078 -0.3436 -0.3722 248 LEU A CG 1268 C CD1 . LEU A 160 ? 1.5201 1.7323 1.1366 0.5858 -0.3632 -0.3590 248 LEU A CD1 1269 C CD2 . LEU A 160 ? 1.3581 1.5986 1.0575 0.4496 -0.3270 -0.3572 248 LEU A CD2 1270 N N . TYR A 161 ? 0.9479 1.4099 0.8273 0.4852 -0.3165 -0.4141 249 TYR A N 1271 C CA . TYR A 161 ? 0.9384 1.3138 0.7932 0.4680 -0.2848 -0.3747 249 TYR A CA 1272 C C . TYR A 161 ? 0.9966 1.3667 0.8143 0.5416 -0.3041 -0.3823 249 TYR A C 1273 O O . TYR A 161 ? 1.0317 1.2985 0.7928 0.5477 -0.2867 -0.3483 249 TYR A O 1274 C CB . TYR A 161 ? 0.7414 1.1796 0.6925 0.3907 -0.2453 -0.3798 249 TYR A CB 1275 C CG . TYR A 161 ? 0.7461 1.1623 0.7204 0.3206 -0.2214 -0.3656 249 TYR A CG 1276 C CD1 . TYR A 161 ? 0.6978 0.9950 0.6228 0.2867 -0.1945 -0.3156 249 TYR A CD1 1277 C CD2 . TYR A 161 ? 0.7357 1.2515 0.7813 0.2886 -0.2249 -0.4055 249 TYR A CD2 1278 C CE1 . TYR A 161 ? 0.6593 0.9348 0.6027 0.2303 -0.1733 -0.3033 249 TYR A CE1 1279 C CE2 . TYR A 161 ? 0.6999 1.1831 0.7600 0.2274 -0.2013 -0.3929 249 TYR A CE2 1280 C CZ . TYR A 161 ? 0.7024 1.0641 0.7097 0.2023 -0.1764 -0.3406 249 TYR A CZ 1281 O OH . TYR A 161 ? 0.8380 1.1664 0.8569 0.1495 -0.1539 -0.3290 249 TYR A OH 1282 N N . ASN A 162 ? 0.9742 1.4515 0.8215 0.5956 -0.3362 -0.4293 250 ASN A N 1283 C CA . ASN A 162 ? 1.0550 1.5254 0.8662 0.6523 -0.3429 -0.4417 250 ASN A CA 1284 C C . ASN A 162 ? 1.1887 1.5073 0.8573 0.7126 -0.3563 -0.4110 250 ASN A C 1285 O O . ASN A 162 ? 1.2294 1.5328 0.8489 0.7613 -0.3677 -0.4214 250 ASN A O 1286 C CB . ASN A 162 ? 1.0542 1.6745 0.9349 0.6673 -0.3553 -0.5024 250 ASN A CB 1287 C CG . ASN A 162 ? 1.0131 1.7738 1.0262 0.5952 -0.3352 -0.5350 250 ASN A CG 1288 O OD1 . ASN A 162 ? 0.8817 1.6324 0.9372 0.5367 -0.3118 -0.5123 250 ASN A OD1 1289 N ND2 . ASN A 162 ? 1.0651 1.9530 1.1396 0.5961 -0.3416 -0.5893 250 ASN A ND2 1290 N N . GLU A 163 ? 1.2401 1.4442 0.8386 0.7041 -0.3526 -0.3727 251 GLU A N 1291 C CA . GLU A 163 ? 1.4057 1.4514 0.8633 0.7469 -0.3547 -0.3405 251 GLU A CA 1292 C C . GLU A 163 ? 1.3742 1.2795 0.7670 0.7182 -0.3284 -0.2894 251 GLU A C 1293 O O . GLU A 163 ? 1.3283 1.2167 0.7545 0.6677 -0.3107 -0.2665 251 GLU A O 1294 C CB . GLU A 163 ? 1.5375 1.5436 0.9522 0.7556 -0.3625 -0.3335 251 GLU A CB 1295 C CG . GLU A 163 ? 1.6224 1.7472 1.0806 0.7929 -0.3885 -0.3822 251 GLU A CG 1296 C CD . GLU A 163 ? 1.7597 1.8142 1.1410 0.8208 -0.3980 -0.3702 251 GLU A CD 1297 O OE1 . GLU A 163 ? 1.7882 1.7088 1.0925 0.8010 -0.3807 -0.3243 251 GLU A OE1 1298 O OE2 . GLU A 163 ? 1.8300 1.9657 1.2273 0.8612 -0.4212 -0.4081 251 GLU A OE2 1299 N N . GLY A 164 ? 1.4300 1.2354 0.7298 0.7484 -0.3249 -0.2724 252 GLY A N 1300 C CA . GLY A 164 ? 1.5404 1.2017 0.7691 0.7172 -0.2952 -0.2254 252 GLY A CA 1301 C C . GLY A 164 ? 1.4790 1.1649 0.7824 0.6736 -0.2706 -0.2184 252 GLY A C 1302 O O . GLY A 164 ? 1.3207 1.1306 0.7204 0.6761 -0.2761 -0.2502 252 GLY A O 1303 N N . ILE A 165 ? 1.4512 1.0202 0.7096 0.6289 -0.2376 -0.1813 253 ILE A N 1304 C CA . ILE A 165 ? 1.3288 0.9042 0.6436 0.5820 -0.2067 -0.1779 253 ILE A CA 1305 C C . ILE A 165 ? 1.2179 0.8512 0.6119 0.5186 -0.1869 -0.1786 253 ILE A C 1306 O O . ILE A 165 ? 1.1774 0.7658 0.5440 0.4899 -0.1804 -0.1578 253 ILE A O 1307 C CB . ILE A 165 ? 1.4068 0.8366 0.6331 0.5556 -0.1785 -0.1430 253 ILE A CB 1308 C CG1 . ILE A 165 ? 1.5483 0.9217 0.6955 0.6065 -0.1918 -0.1423 253 ILE A CG1 1309 C CG2 . ILE A 165 ? 1.2494 0.6907 0.5316 0.5018 -0.1469 -0.1436 253 ILE A CG2 1310 C CD1 . ILE A 165 ? 1.6091 0.8248 0.6409 0.5885 -0.1675 -0.1094 253 ILE A CD1 1311 N N . LEU A 166 ? 1.0599 0.8033 0.5548 0.4838 -0.1755 -0.1962 254 LEU A N 1312 C CA . LEU A 166 ? 0.9355 0.7362 0.5048 0.4107 -0.1538 -0.1876 254 LEU A CA 1313 C C . LEU A 166 ? 1.0462 0.8009 0.6162 0.3594 -0.1205 -0.1659 254 LEU A C 1314 O O . LEU A 166 ? 1.1170 0.8423 0.6653 0.3742 -0.1138 -0.1696 254 LEU A O 1315 C CB . LEU A 166 ? 0.9709 0.9235 0.6486 0.3997 -0.1596 -0.2209 254 LEU A CB 1316 C CG . LEU A 166 ? 0.9988 1.0294 0.6932 0.4517 -0.1957 -0.2549 254 LEU A CG 1317 C CD1 . LEU A 166 ? 0.8862 1.0733 0.6942 0.4322 -0.1941 -0.2939 254 LEU A CD1 1318 C CD2 . LEU A 166 ? 0.9363 0.9311 0.5958 0.4476 -0.2081 -0.2437 254 LEU A CD2 1319 N N . ILE A 167 ? 0.9715 0.7247 0.5665 0.3018 -0.1008 -0.1463 255 ILE A N 1320 C CA . ILE A 167 ? 0.8647 0.6007 0.4743 0.2514 -0.0721 -0.1292 255 ILE A CA 1321 C C . ILE A 167 ? 0.7794 0.5895 0.4630 0.2043 -0.0601 -0.1250 255 ILE A C 1322 O O . ILE A 167 ? 0.8271 0.6422 0.5161 0.1976 -0.0663 -0.1220 255 ILE A O 1323 C CB . ILE A 167 ? 0.9688 0.5889 0.5026 0.2326 -0.0574 -0.1034 255 ILE A CB 1324 C CG1 . ILE A 167 ? 1.0681 0.5863 0.5100 0.2773 -0.0649 -0.1041 255 ILE A CG1 1325 C CG2 . ILE A 167 ? 0.9275 0.5498 0.4844 0.1822 -0.0314 -0.0922 255 ILE A CG2 1326 C CD1 . ILE A 167 ? 1.1852 0.5852 0.5410 0.2660 -0.0534 -0.0815 255 ILE A CD1 1327 N N . VAL A 168 ? 0.7330 0.5962 0.4673 0.1748 -0.0428 -0.1258 256 VAL A N 1328 C CA . VAL A 168 ? 0.6560 0.5647 0.4435 0.1299 -0.0262 -0.1156 256 VAL A CA 1329 C C . VAL A 168 ? 0.7294 0.5989 0.5002 0.0972 -0.0060 -0.0921 256 VAL A C 1330 O O . VAL A 168 ? 0.8255 0.6686 0.5694 0.1018 -0.0013 -0.0924 256 VAL A O 1331 C CB . VAL A 168 ? 0.5884 0.5930 0.4446 0.1207 -0.0194 -0.1348 256 VAL A CB 1332 C CG1 . VAL A 168 ? 0.5820 0.6015 0.4373 0.1276 -0.0105 -0.1408 256 VAL A CG1 1333 C CG2 . VAL A 168 ? 0.5714 0.6016 0.4679 0.0758 0.0005 -0.1213 256 VAL A CG2 1334 N N . TRP A 169 ? 0.6831 0.5506 0.4684 0.0666 0.0048 -0.0749 257 TRP A N 1335 C CA . TRP A 169 ? 0.6361 0.4879 0.4150 0.0393 0.0212 -0.0567 257 TRP A CA 1336 C C . TRP A 169 ? 0.5702 0.4623 0.3911 0.0150 0.0336 -0.0454 257 TRP A C 1337 O O . TRP A 169 ? 0.6889 0.5998 0.5353 0.0121 0.0319 -0.0492 257 TRP A O 1338 C CB . TRP A 169 ? 0.7798 0.5656 0.5124 0.0321 0.0230 -0.0455 257 TRP A CB 1339 C CG . TRP A 169 ? 0.7888 0.5661 0.5264 0.0235 0.0230 -0.0367 257 TRP A CG 1340 C CD1 . TRP A 169 ? 0.7542 0.5146 0.4778 0.0411 0.0102 -0.0431 257 TRP A CD1 1341 C CD2 . TRP A 169 ? 0.7316 0.5190 0.4870 -0.0005 0.0352 -0.0224 257 TRP A CD2 1342 N NE1 . TRP A 169 ? 0.7534 0.5105 0.4853 0.0258 0.0157 -0.0342 257 TRP A NE1 1343 C CE2 . TRP A 169 ? 0.7738 0.5460 0.5258 0.0017 0.0314 -0.0214 257 TRP A CE2 1344 C CE3 . TRP A 169 ? 0.6833 0.4939 0.4545 -0.0189 0.0473 -0.0121 257 TRP A CE3 1345 C CZ2 . TRP A 169 ? 0.7730 0.5484 0.5379 -0.0139 0.0412 -0.0107 257 TRP A CZ2 1346 C CZ3 . TRP A 169 ? 0.6733 0.4907 0.4574 -0.0304 0.0547 -0.0009 257 TRP A CZ3 1347 C CH2 . TRP A 169 ? 0.7886 0.5868 0.5704 -0.0280 0.0527 -0.0003 257 TRP A CH2 1348 N N . ASP A 170 ? 0.5458 0.4458 0.3677 -0.0012 0.0459 -0.0326 258 ASP A N 1349 C CA . ASP A 170 ? 0.6574 0.5875 0.5063 -0.0177 0.0596 -0.0191 258 ASP A CA 1350 C C . ASP A 170 ? 0.6005 0.5194 0.4331 -0.0270 0.0647 -0.0030 258 ASP A C 1351 O O . ASP A 170 ? 0.5896 0.5029 0.4016 -0.0270 0.0625 -0.0075 258 ASP A O 1352 C CB . ASP A 170 ? 0.6053 0.5773 0.4711 -0.0184 0.0686 -0.0254 258 ASP A CB 1353 C CG . ASP A 170 ? 0.5794 0.5686 0.4587 -0.0349 0.0870 -0.0084 258 ASP A CG 1354 O OD1 . ASP A 170 ? 0.6018 0.5920 0.5020 -0.0454 0.0947 -0.0075 258 ASP A OD1 1355 O OD2 . ASP A 170 ? 0.7026 0.7005 0.5662 -0.0368 0.0945 0.0030 258 ASP A OD2 1356 N N . PRO A 171 ? 0.5713 0.4872 0.4123 -0.0338 0.0709 0.0121 259 PRO A N 1357 C CA . PRO A 171 ? 0.5591 0.4796 0.3910 -0.0367 0.0738 0.0248 259 PRO A CA 1358 C C . PRO A 171 ? 0.5800 0.5313 0.4089 -0.0351 0.0801 0.0334 259 PRO A C 1359 O O . PRO A 171 ? 0.6315 0.5879 0.4673 -0.0355 0.0903 0.0425 259 PRO A O 1360 C CB . PRO A 171 ? 0.4957 0.4029 0.3379 -0.0363 0.0790 0.0370 259 PRO A CB 1361 C CG . PRO A 171 ? 0.6593 0.5491 0.5123 -0.0381 0.0764 0.0262 259 PRO A CG 1362 C CD . PRO A 171 ? 0.6729 0.5822 0.5329 -0.0370 0.0746 0.0139 259 PRO A CD 1363 N N . SER A 172 ? 0.6035 0.5737 0.4189 -0.0356 0.0759 0.0288 260 SER A N 1364 C CA . SER A 172 ? 0.6648 0.6674 0.4701 -0.0307 0.0792 0.0359 260 SER A CA 1365 C C . SER A 172 ? 0.6097 0.6336 0.4097 -0.0218 0.0762 0.0487 260 SER A C 1366 O O . SER A 172 ? 0.6454 0.6653 0.4544 -0.0224 0.0724 0.0472 260 SER A O 1367 C CB . SER A 172 ? 0.7574 0.7743 0.5498 -0.0353 0.0739 0.0160 260 SER A CB 1368 O OG . SER A 172 ? 0.7663 0.7817 0.5540 -0.0451 0.0673 0.0031 260 SER A OG 1369 N N . VAL A 173 ? 0.6240 0.6736 0.4067 -0.0101 0.0777 0.0600 261 VAL A N 1370 C CA . VAL A 173 ? 0.5757 0.6613 0.3497 0.0058 0.0687 0.0654 261 VAL A CA 1371 C C . VAL A 173 ? 0.6095 0.7293 0.3963 -0.0082 0.0576 0.0378 261 VAL A C 1372 O O . VAL A 173 ? 0.6732 0.7895 0.4578 -0.0257 0.0573 0.0179 261 VAL A O 1373 C CB . VAL A 173 ? 0.6371 0.7469 0.3794 0.0234 0.0693 0.0785 261 VAL A CB 1374 C CG1 . VAL A 173 ? 0.6722 0.8229 0.4026 0.0501 0.0562 0.0851 261 VAL A CG1 1375 C CG2 . VAL A 173 ? 0.6391 0.7045 0.3626 0.0277 0.0883 0.1042 261 VAL A CG2 1376 N N . TYR A 174 ? 0.6237 0.7741 0.4229 -0.0014 0.0509 0.0345 262 TYR A N 1377 C CA . TYR A 174 ? 0.5733 0.7577 0.3885 -0.0226 0.0462 0.0056 262 TYR A CA 1378 C C . TYR A 174 ? 0.6358 0.8609 0.4404 -0.0330 0.0396 -0.0162 262 TYR A C 1379 O O . TYR A 174 ? 0.5592 0.8212 0.3487 -0.0119 0.0317 -0.0087 262 TYR A O 1380 C CB . TYR A 174 ? 0.5934 0.8277 0.4270 -0.0075 0.0399 0.0038 262 TYR A CB 1381 C CG . TYR A 174 ? 0.5480 0.8263 0.4049 -0.0350 0.0403 -0.0290 262 TYR A CG 1382 C CD1 . TYR A 174 ? 0.6399 0.8720 0.5013 -0.0650 0.0534 -0.0390 262 TYR A CD1 1383 C CD2 . TYR A 174 ? 0.5782 0.9460 0.4497 -0.0318 0.0287 -0.0517 262 TYR A CD2 1384 C CE1 . TYR A 174 ? 0.6562 0.9209 0.5335 -0.0969 0.0607 -0.0691 262 TYR A CE1 1385 C CE2 . TYR A 174 ? 0.6183 1.0331 0.5160 -0.0652 0.0336 -0.0870 262 TYR A CE2 1386 C CZ . TYR A 174 ? 0.6366 0.9948 0.5357 -0.1005 0.0524 -0.0946 262 TYR A CZ 1387 O OH . TYR A 174 ? 0.6652 1.0608 0.5846 -0.1403 0.0643 -0.1294 262 TYR A OH 1388 N N . HIS A 175 ? 0.6708 0.8825 0.4764 -0.0649 0.0440 -0.0432 263 HIS A N 1389 C CA . HIS A 175 ? 0.7187 0.9589 0.5117 -0.0804 0.0401 -0.0701 263 HIS A CA 1390 C C . HIS A 175 ? 0.7535 0.9850 0.5214 -0.0646 0.0385 -0.0608 263 HIS A C 1391 O O . HIS A 175 ? 0.7677 1.0418 0.5229 -0.0660 0.0316 -0.0786 263 HIS A O 1392 C CB . HIS A 175 ? 0.7461 1.0767 0.5552 -0.0844 0.0289 -0.0943 263 HIS A CB 1393 C CG . HIS A 175 ? 0.8418 1.1872 0.6757 -0.1170 0.0367 -0.1198 263 HIS A CG 1394 N ND1 . HIS A 175 ? 0.8465 1.2775 0.7022 -0.1359 0.0310 -0.1557 263 HIS A ND1 1395 C CD2 . HIS A 175 ? 0.7741 1.0628 0.6127 -0.1359 0.0517 -0.1164 263 HIS A CD2 1396 C CE1 . HIS A 175 ? 0.9044 1.3296 0.7795 -0.1692 0.0459 -0.1734 263 HIS A CE1 1397 N NE2 . HIS A 175 ? 0.8008 1.1356 0.6614 -0.1683 0.0587 -0.1480 263 HIS A NE2 1398 N N . SER A 176 ? 0.6864 0.8679 0.4481 -0.0520 0.0462 -0.0369 264 SER A N 1399 C CA . SER A 176 ? 0.6881 0.8652 0.4294 -0.0399 0.0498 -0.0293 264 SER A CA 1400 C C . SER A 176 ? 0.7385 0.8791 0.4703 -0.0550 0.0549 -0.0523 264 SER A C 1401 O O . SER A 176 ? 0.7787 0.8705 0.5157 -0.0649 0.0587 -0.0577 264 SER A O 1402 C CB . SER A 176 ? 0.6858 0.8323 0.4301 -0.0245 0.0593 0.0018 264 SER A CB 1403 O OG . SER A 176 ? 0.8764 1.0200 0.6046 -0.0183 0.0685 0.0072 264 SER A OG 1404 N N . ASP A 177 ? 0.8137 0.9737 0.5254 -0.0524 0.0549 -0.0656 265 ASP A N 1405 C CA . ASP A 177 ? 0.7152 0.8370 0.4131 -0.0593 0.0600 -0.0883 265 ASP A CA 1406 C C . ASP A 177 ? 0.7018 0.8029 0.4038 -0.0426 0.0688 -0.0746 265 ASP A C 1407 O O . ASP A 177 ? 0.6292 0.7428 0.3436 -0.0329 0.0738 -0.0485 265 ASP A O 1408 C CB . ASP A 177 ? 0.7825 0.9348 0.4569 -0.0656 0.0568 -0.1160 265 ASP A CB 1409 C CG . ASP A 177 ? 1.0179 1.2189 0.6777 -0.0464 0.0573 -0.1033 265 ASP A CG 1410 O OD1 . ASP A 177 ? 1.0906 1.3102 0.7558 -0.0320 0.0580 -0.0725 265 ASP A OD1 1411 O OD2 . ASP A 177 ? 1.1575 1.3716 0.7942 -0.0452 0.0591 -0.1238 265 ASP A OD2 1412 N N . ILE A 178 ? 0.7321 0.8014 0.4236 -0.0393 0.0720 -0.0945 266 ILE A N 1413 C CA . ILE A 178 ? 0.6709 0.7297 0.3758 -0.0231 0.0786 -0.0887 266 ILE A CA 1414 C C . ILE A 178 ? 0.7252 0.8321 0.4359 -0.0156 0.0901 -0.0743 266 ILE A C 1415 O O . ILE A 178 ? 0.7031 0.8153 0.4355 -0.0135 0.0982 -0.0562 266 ILE A O 1416 C CB . ILE A 178 ? 0.7381 0.7550 0.4267 -0.0123 0.0775 -0.1154 266 ILE A CB 1417 C CG1 . ILE A 178 ? 0.6794 0.6320 0.3596 -0.0163 0.0711 -0.1169 266 ILE A CG1 1418 C CG2 . ILE A 178 ? 0.7116 0.7486 0.4183 0.0091 0.0836 -0.1183 266 ILE A CG2 1419 C CD1 . ILE A 178 ? 0.7017 0.5873 0.3443 -0.0066 0.0700 -0.1420 266 ILE A CD1 1420 N N . PRO A 179 ? 0.7103 0.8495 0.3971 -0.0146 0.0931 -0.0825 267 PRO A N 1421 C CA . PRO A 179 ? 0.7968 0.9715 0.4795 -0.0087 0.1092 -0.0668 267 PRO A CA 1422 C C . PRO A 179 ? 0.6159 0.7950 0.2997 -0.0108 0.1143 -0.0313 267 PRO A C 1423 O O . PRO A 179 ? 0.6553 0.8370 0.3460 -0.0122 0.1326 -0.0148 267 PRO A O 1424 C CB . PRO A 179 ? 0.6581 0.8632 0.3050 -0.0059 0.1085 -0.0818 267 PRO A CB 1425 C CG . PRO A 179 ? 0.7559 0.9371 0.3963 -0.0102 0.0962 -0.1144 267 PRO A CG 1426 C CD . PRO A 179 ? 0.7253 0.8687 0.3846 -0.0197 0.0858 -0.1093 267 PRO A CD 1427 N N . LYS A 180 ? 0.6797 0.8593 0.3557 -0.0112 0.1003 -0.0221 268 LYS A N 1428 C CA . LYS A 180 ? 0.7946 0.9707 0.4657 -0.0054 0.1036 0.0110 268 LYS A CA 1429 C C . LYS A 180 ? 0.7816 0.9224 0.4860 -0.0125 0.1102 0.0212 268 LYS A C 1430 O O . LYS A 180 ? 0.8284 0.9548 0.5309 -0.0128 0.1258 0.0448 268 LYS A O 1431 C CB . LYS A 180 ? 0.8580 1.0528 0.5214 0.0007 0.0844 0.0130 268 LYS A CB 1432 C CG . LYS A 180 ? 1.0832 1.3256 0.7138 0.0090 0.0738 -0.0002 268 LYS A CG 1433 C CD . LYS A 180 ? 1.2750 1.5283 0.8631 0.0237 0.0877 0.0191 268 LYS A CD 1434 C CE . LYS A 180 ? 1.4175 1.6533 0.9809 0.0428 0.0941 0.0597 268 LYS A CE 1435 N NZ . LYS A 180 ? 1.5516 1.7859 1.0594 0.0554 0.1121 0.0807 268 LYS A NZ 1436 N N . TRP A 181 ? 0.7117 0.8334 0.4405 -0.0188 0.0998 0.0025 269 TRP A N 1437 C CA . TRP A 181 ? 0.5849 0.6771 0.3424 -0.0232 0.1022 0.0087 269 TRP A CA 1438 C C . TRP A 181 ? 0.6554 0.7542 0.4293 -0.0260 0.1185 0.0060 269 TRP A C 1439 O O . TRP A 181 ? 0.6749 0.7626 0.4646 -0.0329 0.1296 0.0198 269 TRP A O 1440 C CB . TRP A 181 ? 0.6578 0.7238 0.4250 -0.0261 0.0882 -0.0105 269 TRP A CB 1441 C CG . TRP A 181 ? 0.6406 0.6822 0.4305 -0.0250 0.0882 -0.0139 269 TRP A CG 1442 C CD1 . TRP A 181 ? 0.5888 0.6147 0.3961 -0.0283 0.0894 0.0000 269 TRP A CD1 1443 C CD2 . TRP A 181 ? 0.6714 0.7035 0.4663 -0.0160 0.0842 -0.0358 269 TRP A CD2 1444 N NE1 . TRP A 181 ? 0.5994 0.6121 0.4236 -0.0242 0.0853 -0.0132 269 TRP A NE1 1445 C CE2 . TRP A 181 ? 0.6785 0.6962 0.4949 -0.0137 0.0810 -0.0345 269 TRP A CE2 1446 C CE3 . TRP A 181 ? 0.6680 0.7015 0.4481 -0.0057 0.0820 -0.0581 269 TRP A CE3 1447 C CZ2 . TRP A 181 ? 0.7075 0.7194 0.5311 0.0021 0.0731 -0.0543 269 TRP A CZ2 1448 C CZ3 . TRP A 181 ? 0.7125 0.7331 0.4984 0.0118 0.0759 -0.0764 269 TRP A CZ3 1449 C CH2 . TRP A 181 ? 0.6537 0.6666 0.4611 0.0172 0.0701 -0.0741 269 TRP A CH2 1450 N N . TYR A 182 ? 0.6803 0.8009 0.4511 -0.0218 0.1219 -0.0149 270 TYR A N 1451 C CA . TYR A 182 ? 0.6217 0.7656 0.4152 -0.0239 0.1377 -0.0259 270 TYR A CA 1452 C C . TYR A 182 ? 0.7366 0.8906 0.5238 -0.0375 0.1636 -0.0030 270 TYR A C 1453 O O . TYR A 182 ? 0.8229 0.9850 0.6380 -0.0506 0.1797 -0.0048 270 TYR A O 1454 C CB . TYR A 182 ? 0.5864 0.7555 0.3715 -0.0123 0.1375 -0.0534 270 TYR A CB 1455 C CG . TYR A 182 ? 0.6462 0.8564 0.4603 -0.0112 0.1540 -0.0716 270 TYR A CG 1456 C CD1 . TYR A 182 ? 0.6420 0.8592 0.4873 0.0030 0.1430 -0.0965 270 TYR A CD1 1457 C CD2 . TYR A 182 ? 0.7009 0.9465 0.5091 -0.0230 0.1813 -0.0657 270 TYR A CD2 1458 C CE1 . TYR A 182 ? 0.6624 0.9345 0.5423 0.0064 0.1563 -0.1194 270 TYR A CE1 1459 C CE2 . TYR A 182 ? 0.6523 0.9477 0.4938 -0.0264 0.2001 -0.0876 270 TYR A CE2 1460 C CZ . TYR A 182 ? 0.6752 0.9902 0.5579 -0.0112 0.1859 -0.1167 270 TYR A CZ 1461 O OH . TYR A 182 ? 0.6230 1.0035 0.5473 -0.0114 0.2016 -0.1448 270 TYR A OH 1462 N N . GLN A 183 ? 0.7491 0.9001 0.4953 -0.0346 0.1682 0.0176 271 GLN A N 1463 C CA . GLN A 183 ? 0.8158 0.9573 0.5361 -0.0438 0.1948 0.0451 271 GLN A CA 1464 C C . GLN A 183 ? 0.8656 0.9630 0.5910 -0.0509 0.1990 0.0691 271 GLN A C 1465 O O . GLN A 183 ? 0.9669 1.0427 0.6828 -0.0665 0.2267 0.0857 271 GLN A O 1466 C CB . GLN A 183 ? 0.9847 1.1325 0.6491 -0.0295 0.1932 0.0607 271 GLN A CB 1467 C CG . GLN A 183 ? 1.1923 1.3198 0.8100 -0.0334 0.2227 0.0919 271 GLN A CG 1468 C CD . GLN A 183 ? 1.3139 1.4526 0.8692 -0.0117 0.2161 0.1054 271 GLN A CD 1469 O OE1 . GLN A 183 ? 1.2746 1.4156 0.8154 0.0085 0.1892 0.1108 271 GLN A OE1 1470 N NE2 . GLN A 183 ? 1.4500 1.6035 0.9687 -0.0155 0.2406 0.1076 271 GLN A NE2 1471 N N . ASN A 184 ? 0.7806 0.8614 0.5188 -0.0415 0.1742 0.0688 272 ASN A N 1472 C CA . ASN A 184 ? 0.7987 0.8376 0.5386 -0.0427 0.1749 0.0892 272 ASN A CA 1473 C C . ASN A 184 ? 0.7733 0.8042 0.5535 -0.0450 0.1563 0.0726 272 ASN A C 1474 O O . ASN A 184 ? 0.7337 0.7530 0.5109 -0.0342 0.1385 0.0769 272 ASN A O 1475 C CB . ASN A 184 ? 0.8991 0.9251 0.5968 -0.0209 0.1653 0.1139 272 ASN A CB 1476 C CG . ASN A 184 ? 0.9887 0.9678 0.6815 -0.0152 0.1675 0.1356 272 ASN A CG 1477 O OD1 . ASN A 184 ? 1.0741 1.0144 0.7706 -0.0312 0.1895 0.1446 272 ASN A OD1 1478 N ND2 . ASN A 184 ? 0.8391 0.8243 0.5246 0.0065 0.1459 0.1406 272 ASN A ND2 1479 N N . PRO A 185 ? 0.6935 0.7358 0.5098 -0.0577 0.1606 0.0513 273 PRO A N 1480 C CA . PRO A 185 ? 0.7194 0.7519 0.5643 -0.0560 0.1426 0.0358 273 PRO A CA 1481 C C . PRO A 185 ? 0.7270 0.7228 0.5781 -0.0648 0.1494 0.0502 273 PRO A C 1482 O O . PRO A 185 ? 0.7686 0.7464 0.6096 -0.0774 0.1726 0.0657 273 PRO A O 1483 C CB . PRO A 185 ? 0.6393 0.7067 0.5162 -0.0603 0.1446 0.0072 273 PRO A CB 1484 C CG . PRO A 185 ? 0.6706 0.7579 0.5491 -0.0780 0.1739 0.0116 273 PRO A CG 1485 C CD . PRO A 185 ? 0.7522 0.8239 0.5841 -0.0728 0.1827 0.0385 273 PRO A CD 1486 N N . ASP A 186 ? 0.6902 0.6676 0.5508 -0.0590 0.1324 0.0455 274 ASP A N 1487 C CA . ASP A 186 ? 0.6240 0.5657 0.4891 -0.0658 0.1388 0.0554 274 ASP A CA 1488 C C . ASP A 186 ? 0.6064 0.5549 0.5006 -0.0872 0.1530 0.0393 274 ASP A C 1489 O O . ASP A 186 ? 0.7193 0.6399 0.6083 -0.1037 0.1754 0.0504 274 ASP A O 1490 C CB . ASP A 186 ? 0.7066 0.6321 0.5741 -0.0556 0.1193 0.0509 274 ASP A CB 1491 C CG . ASP A 186 ? 0.7716 0.6586 0.6325 -0.0551 0.1260 0.0659 274 ASP A CG 1492 O OD1 . ASP A 186 ? 0.9909 0.8543 0.8375 -0.0595 0.1450 0.0831 274 ASP A OD1 1493 O OD2 . ASP A 186 ? 0.7673 0.6416 0.6312 -0.0491 0.1143 0.0609 274 ASP A OD2 1494 N N . TYR A 187 ? 0.5891 0.5744 0.5120 -0.0864 0.1407 0.0109 275 TYR A N 1495 C CA . TYR A 187 ? 0.6436 0.6630 0.6021 -0.1069 0.1543 -0.0123 275 TYR A CA 1496 C C . TYR A 187 ? 0.6733 0.7477 0.6450 -0.1031 0.1571 -0.0294 275 TYR A C 1497 O O . TYR A 187 ? 0.7626 0.8478 0.7228 -0.0793 0.1382 -0.0347 275 TYR A O 1498 C CB . TYR A 187 ? 0.7863 0.8150 0.7730 -0.1062 0.1372 -0.0375 275 TYR A CB 1499 C CG . TYR A 187 ? 0.8441 0.8250 0.8257 -0.1204 0.1452 -0.0276 275 TYR A CG 1500 C CD1 . TYR A 187 ? 0.8963 0.8299 0.8484 -0.1045 0.1347 -0.0065 275 TYR A CD1 1501 C CD2 . TYR A 187 ? 0.8518 0.8357 0.8581 -0.1517 0.1659 -0.0423 275 TYR A CD2 1502 C CE1 . TYR A 187 ? 0.9016 0.7902 0.8469 -0.1131 0.1427 0.0010 275 TYR A CE1 1503 C CE2 . TYR A 187 ? 0.9332 0.8637 0.9295 -0.1644 0.1750 -0.0351 275 TYR A CE2 1504 C CZ . TYR A 187 ? 0.9241 0.8060 0.8888 -0.1419 0.1625 -0.0127 275 TYR A CZ 1505 O OH . TYR A 187 ? 0.9541 0.7822 0.9077 -0.1506 0.1721 -0.0078 275 TYR A OH 1506 N N . ASN A 188 ? 0.6499 0.7559 0.6431 -0.1285 0.1838 -0.0397 276 ASN A N 1507 C CA . ASN A 188 ? 0.6484 0.8154 0.6581 -0.1254 0.1902 -0.0598 276 ASN A CA 1508 C C . ASN A 188 ? 0.6065 0.8390 0.6654 -0.1153 0.1728 -0.1024 276 ASN A C 1509 O O . ASN A 188 ? 0.6530 0.9403 0.7558 -0.1391 0.1896 -0.1294 276 ASN A O 1510 C CB . ASN A 188 ? 0.6969 0.8716 0.7015 -0.1578 0.2315 -0.0511 276 ASN A CB 1511 C CG . ASN A 188 ? 0.6863 0.9203 0.6974 -0.1518 0.2407 -0.0671 276 ASN A CG 1512 O OD1 . ASN A 188 ? 0.6996 0.9632 0.7167 -0.1204 0.2149 -0.0840 276 ASN A OD1 1513 N ND2 . ASN A 188 ? 0.7436 0.9890 0.7481 -0.1818 0.2802 -0.0620 276 ASN A ND2 1514 N N . PHE A 189 ? 0.6252 0.8520 0.6731 -0.0787 0.1397 -0.1096 277 PHE A N 1515 C CA . PHE A 189 ? 0.6651 0.9391 0.7444 -0.0559 0.1156 -0.1455 277 PHE A CA 1516 C C . PHE A 189 ? 0.6522 0.9886 0.7472 -0.0332 0.1132 -0.1719 277 PHE A C 1517 O O . PHE A 189 ? 0.7199 1.1147 0.8477 -0.0109 0.0958 -0.2074 277 PHE A O 1518 C CB . PHE A 189 ? 0.5721 0.7914 0.6174 -0.0252 0.0836 -0.1370 277 PHE A CB 1519 C CG . PHE A 189 ? 0.5787 0.7553 0.5777 -0.0016 0.0742 -0.1211 277 PHE A CG 1520 C CD1 . PHE A 189 ? 0.5628 0.6901 0.5286 -0.0152 0.0845 -0.0894 277 PHE A CD1 1521 C CD2 . PHE A 189 ? 0.6163 0.8025 0.6032 0.0353 0.0552 -0.1410 277 PHE A CD2 1522 C CE1 . PHE A 189 ? 0.5470 0.6428 0.4747 0.0002 0.0769 -0.0812 277 PHE A CE1 1523 C CE2 . PHE A 189 ? 0.5676 0.7056 0.5084 0.0513 0.0500 -0.1297 277 PHE A CE2 1524 C CZ . PHE A 189 ? 0.5369 0.6336 0.4512 0.0301 0.0614 -0.1016 277 PHE A CZ 1525 N N . PHE A 190 ? 0.6146 0.9428 0.6851 -0.0354 0.1293 -0.1571 278 PHE A N 1526 C CA . PHE A 190 ? 0.6065 0.9878 0.6853 -0.0111 0.1286 -0.1821 278 PHE A CA 1527 C C . PHE A 190 ? 0.4847 0.9670 0.6266 -0.0155 0.1377 -0.2243 278 PHE A C 1528 O O . PHE A 190 ? 0.5481 1.0785 0.7061 0.0238 0.1179 -0.2562 278 PHE A O 1529 C CB . PHE A 190 ? 0.4998 0.8647 0.5441 -0.0207 0.1502 -0.1618 278 PHE A CB 1530 C CG . PHE A 190 ? 0.5065 0.7919 0.4954 -0.0120 0.1370 -0.1306 278 PHE A CG 1531 C CD1 . PHE A 190 ? 0.5802 0.8302 0.5415 0.0216 0.1101 -0.1376 278 PHE A CD1 1532 C CD2 . PHE A 190 ? 0.5384 0.7838 0.5011 -0.0368 0.1522 -0.0964 278 PHE A CD2 1533 C CE1 . PHE A 190 ? 0.5843 0.7691 0.5004 0.0219 0.1013 -0.1146 278 PHE A CE1 1534 C CE2 . PHE A 190 ? 0.5272 0.7172 0.4476 -0.0287 0.1389 -0.0739 278 PHE A CE2 1535 C CZ . PHE A 190 ? 0.5646 0.7285 0.4657 -0.0035 0.1147 -0.0848 278 PHE A CZ 1536 N N . ASN A 191 ? 0.6206 1.1353 0.7972 -0.0623 0.1680 -0.2271 279 ASN A N 1537 C CA . ASN A 191 ? 0.6716 1.2954 0.9175 -0.0754 0.1799 -0.2738 279 ASN A CA 1538 C C . ASN A 191 ? 0.6252 1.2979 0.9074 -0.0417 0.1420 -0.3104 279 ASN A C 1539 O O . ASN A 191 ? 0.6270 1.3939 0.9518 -0.0140 0.1311 -0.3538 279 ASN A O 1540 C CB . ASN A 191 ? 0.7681 1.4013 1.0392 -0.1399 0.2221 -0.2707 279 ASN A CB 1541 C CG . ASN A 191 ? 0.8478 1.4750 1.0965 -0.1706 0.2662 -0.2520 279 ASN A CG 1542 O OD1 . ASN A 191 ? 0.8124 1.5122 1.0817 -0.1627 0.2787 -0.2766 279 ASN A OD1 1543 N ND2 . ASN A 191 ? 0.9388 1.4773 1.1389 -0.2011 0.2897 -0.2080 279 ASN A ND2 1544 N N . ASN A 192 ? 0.6276 1.2386 0.8898 -0.0405 0.1215 -0.2939 280 ASN A N 1545 C CA . ASN A 192 ? 0.6928 1.3441 0.9809 -0.0111 0.0861 -0.3260 280 ASN A CA 1546 C C . ASN A 192 ? 0.5843 1.2099 0.8315 0.0584 0.0462 -0.3277 280 ASN A C 1547 O O . ASN A 192 ? 0.6056 1.2984 0.8774 0.1004 0.0185 -0.3657 280 ASN A O 1548 C CB . ASN A 192 ? 0.8134 1.4064 1.0906 -0.0373 0.0821 -0.3091 280 ASN A CB 1549 C CG . ASN A 192 ? 0.9452 1.5328 1.2451 -0.1053 0.1257 -0.3008 280 ASN A CG 1550 O OD1 . ASN A 192 ? 1.0850 1.6162 1.3521 -0.1287 0.1547 -0.2649 280 ASN A OD1 1551 N ND2 . ASN A 192 ? 0.9104 1.5517 1.2606 -0.1362 0.1305 -0.3346 280 ASN A ND2 1552 N N . TYR A 193 ? 0.5375 1.0648 0.7191 0.0712 0.0443 -0.2883 281 TYR A N 1553 C CA . TYR A 193 ? 0.6192 1.1061 0.7523 0.1303 0.0161 -0.2888 281 TYR A CA 1554 C C . TYR A 193 ? 0.6510 1.2257 0.8155 0.1642 0.0143 -0.3277 281 TYR A C 1555 O O . TYR A 193 ? 0.7350 1.3294 0.8915 0.2220 -0.0166 -0.3530 281 TYR A O 1556 C CB . TYR A 193 ? 0.5800 0.9611 0.6470 0.1245 0.0239 -0.2467 281 TYR A CB 1557 C CG . TYR A 193 ? 0.6046 0.9308 0.6154 0.1762 0.0033 -0.2482 281 TYR A CG 1558 C CD1 . TYR A 193 ? 0.5751 0.9332 0.5867 0.1983 0.0097 -0.2665 281 TYR A CD1 1559 C CD2 . TYR A 193 ? 0.5886 0.8235 0.5398 0.2009 -0.0190 -0.2317 281 TYR A CD2 1560 C CE1 . TYR A 193 ? 0.7207 1.0162 0.6749 0.2453 -0.0068 -0.2697 281 TYR A CE1 1561 C CE2 . TYR A 193 ? 0.6444 0.8123 0.5344 0.2449 -0.0330 -0.2327 281 TYR A CE2 1562 C CZ . TYR A 193 ? 0.7344 0.9296 0.6257 0.2672 -0.0272 -0.2519 281 TYR A CZ 1563 O OH . TYR A 193 ? 0.8177 0.9354 0.6430 0.3105 -0.0385 -0.2548 281 TYR A OH 1564 N N . LYS A 194 ? 0.6018 1.2282 0.7976 0.1318 0.0480 -0.3328 282 LYS A N 1565 C CA . LYS A 194 ? 0.5751 1.2960 0.8071 0.1594 0.0516 -0.3727 282 LYS A CA 1566 C C . LYS A 194 ? 0.6672 1.5065 0.9693 0.1748 0.0360 -0.4227 282 LYS A C 1567 O O . LYS A 194 ? 0.7745 1.6722 1.0886 0.2341 0.0113 -0.4587 282 LYS A O 1568 C CB . LYS A 194 ? 0.5721 1.3340 0.8275 0.1112 0.0969 -0.3695 282 LYS A CB 1569 C CG . LYS A 194 ? 0.5831 1.2552 0.7733 0.1048 0.1104 -0.3308 282 LYS A CG 1570 C CD . LYS A 194 ? 0.6445 1.3673 0.8530 0.0661 0.1534 -0.3325 282 LYS A CD 1571 C CE . LYS A 194 ? 0.7081 1.3423 0.8513 0.0494 0.1672 -0.2893 282 LYS A CE 1572 N NZ . LYS A 194 ? 0.6700 1.3520 0.8173 0.0235 0.2067 -0.2930 282 LYS A NZ 1573 N N . THR A 195 ? 0.5699 1.4463 0.9176 0.1226 0.0505 -0.4278 283 THR A N 1574 C CA . THR A 195 ? 0.5740 1.5819 1.0003 0.1238 0.0410 -0.4827 283 THR A CA 1575 C C . THR A 195 ? 0.5551 1.5633 0.9629 0.1929 -0.0128 -0.5006 283 THR A C 1576 O O . THR A 195 ? 0.5916 1.6831 1.0260 0.2287 -0.0387 -0.5416 283 THR A O 1577 C CB . THR A 195 ? 0.6092 1.6384 1.0796 0.0467 0.0706 -0.4841 283 THR A CB 1578 O OG1 . THR A 195 ? 0.6733 1.7098 1.1570 -0.0121 0.1233 -0.4720 283 THR A OG1 1579 C CG2 . THR A 195 ? 0.5581 1.6973 1.0911 0.0426 0.0529 -0.5387 283 THR A CG2 1580 N N . TYR A 196 ? 0.6160 1.4985 0.9523 0.2054 -0.0324 -0.4591 284 TYR A N 1581 C CA . TYR A 196 ? 0.6254 1.4764 0.9178 0.2743 -0.0807 -0.4653 284 TYR A CA 1582 C C . TYR A 196 ? 0.6678 1.5121 0.9231 0.3499 -0.1013 -0.4765 284 TYR A C 1583 O O . TYR A 196 ? 0.6881 1.5839 0.9433 0.4069 -0.1371 -0.5081 284 TYR A O 1584 C CB . TYR A 196 ? 0.6511 1.3554 0.8651 0.2652 -0.0872 -0.4134 284 TYR A CB 1585 C CG . TYR A 196 ? 0.7385 1.4106 0.9076 0.3208 -0.1307 -0.4186 284 TYR A CG 1586 C CD1 . TYR A 196 ? 0.7291 1.4430 0.9277 0.3035 -0.1439 -0.4358 284 TYR A CD1 1587 C CD2 . TYR A 196 ? 0.7856 1.3796 0.8756 0.3911 -0.1573 -0.4073 284 TYR A CD2 1588 C CE1 . TYR A 196 ? 0.7805 1.4660 0.9305 0.3571 -0.1845 -0.4406 284 TYR A CE1 1589 C CE2 . TYR A 196 ? 0.8622 1.4163 0.8972 0.4453 -0.1957 -0.4089 284 TYR A CE2 1590 C CZ . TYR A 196 ? 0.8224 1.4268 0.8879 0.4293 -0.2102 -0.4254 284 TYR A CZ 1591 O OH . TYR A 196 ? 0.7706 1.3375 0.7753 0.4850 -0.2489 -0.4272 284 TYR A OH 1592 N N . ARG A 197 ? 0.7171 1.4809 0.9271 0.3432 -0.0803 -0.4454 285 ARG A N 1593 C CA . ARG A 197 ? 0.7562 1.4903 0.9205 0.4092 -0.0942 -0.4529 285 ARG A CA 1594 C C . ARG A 197 ? 0.7336 1.5816 0.9440 0.4326 -0.1101 -0.4939 285 ARG A C 1595 O O . ARG A 197 ? 0.7943 1.6183 0.9578 0.4960 -0.1444 -0.5017 285 ARG A O 1596 C CB . ARG A 197 ? 0.8142 1.4753 0.9444 0.3763 -0.0614 -0.4213 285 ARG A CB 1597 C CG . ARG A 197 ? 0.9081 1.4364 0.9424 0.4215 -0.0753 -0.3978 285 ARG A CG 1598 C CD . ARG A 197 ? 0.8722 1.2781 0.8370 0.4234 -0.0928 -0.3619 285 ARG A CD 1599 N NE . ARG A 197 ? 1.0814 1.3655 0.9535 0.4709 -0.1038 -0.3486 285 ARG A NE 1600 C CZ . ARG A 197 ? 1.2549 1.5171 1.0870 0.5349 -0.1345 -0.3588 285 ARG A CZ 1601 N NH1 . ARG A 197 ? 1.3253 1.6907 1.2026 0.5652 -0.1607 -0.3879 285 ARG A NH1 1602 N NH2 . ARG A 197 ? 1.3855 1.5208 1.1290 0.5600 -0.1389 -0.3367 285 ARG A NH2 1603 N N . LYS A 198 ? 0.7250 1.6892 1.0190 0.3783 -0.0835 -0.5198 286 LYS A N 1604 C CA . LYS A 198 ? 0.7448 1.8266 1.0870 0.3891 -0.0942 -0.5652 286 LYS A CA 1605 C C . LYS A 198 ? 0.7697 1.8950 1.1107 0.4306 -0.1386 -0.5955 286 LYS A C 1606 O O . LYS A 198 ? 0.7883 1.9549 1.1158 0.4840 -0.1679 -0.6240 286 LYS A O 1607 C CB . LYS A 198 ? 0.7660 1.9457 1.1887 0.3100 -0.0511 -0.5847 286 LYS A CB 1608 C CG . LYS A 198 ? 0.8641 2.0168 1.2846 0.2685 -0.0053 -0.5602 286 LYS A CG 1609 C CD . LYS A 198 ? 0.8958 2.0973 1.3717 0.1802 0.0413 -0.5619 286 LYS A CD 1610 C CE . LYS A 198 ? 0.8747 2.0179 1.3252 0.1388 0.0866 -0.5242 286 LYS A CE 1611 N NZ . LYS A 198 ? 0.8078 1.9357 1.2764 0.0594 0.1281 -0.5040 286 LYS A NZ 1612 N N . LEU A 199 ? 0.7690 1.8850 1.1202 0.4070 -0.1430 -0.5905 287 LEU A N 1613 C CA . LEU A 199 ? 0.7679 1.9256 1.1152 0.4399 -0.1815 -0.6208 287 LEU A CA 1614 C C . LEU A 199 ? 0.8584 1.9210 1.1076 0.5252 -0.2260 -0.6037 287 LEU A C 1615 O O . LEU A 199 ? 0.9331 2.0372 1.1615 0.5759 -0.2600 -0.6355 287 LEU A O 1616 C CB . LEU A 199 ? 0.6871 1.8476 1.0658 0.3894 -0.1718 -0.6168 287 LEU A CB 1617 C CG . LEU A 199 ? 0.6379 1.8859 1.1040 0.3009 -0.1302 -0.6392 287 LEU A CG 1618 C CD1 . LEU A 199 ? 0.5823 1.7961 1.0606 0.2558 -0.1217 -0.6233 287 LEU A CD1 1619 C CD2 . LEU A 199 ? 0.6659 2.0384 1.1792 0.3009 -0.1384 -0.6995 287 LEU A CD2 1620 N N . HIS A 200 ? 0.8261 1.7535 1.0068 0.5393 -0.2225 -0.5538 288 HIS A N 1621 C CA . HIS A 200 ? 0.9423 1.7516 1.0138 0.6105 -0.2576 -0.5302 288 HIS A CA 1622 C C . HIS A 200 ? 1.0276 1.7181 1.0291 0.6334 -0.2475 -0.4939 288 HIS A C 1623 O O . HIS A 200 ? 0.9315 1.4887 0.8652 0.6319 -0.2405 -0.4515 288 HIS A O 1624 C CB . HIS A 200 ? 0.9489 1.6797 0.9791 0.6072 -0.2676 -0.5042 288 HIS A CB 1625 C CG . HIS A 200 ? 0.9983 1.8351 1.0963 0.5776 -0.2737 -0.5385 288 HIS A CG 1626 N ND1 . HIS A 200 ? 1.0309 1.9177 1.1122 0.6192 -0.3063 -0.5737 288 HIS A ND1 1627 C CD2 . HIS A 200 ? 0.8877 1.7838 1.0662 0.5082 -0.2479 -0.5441 288 HIS A CD2 1628 C CE1 . HIS A 200 ? 0.9576 1.9301 1.1089 0.5748 -0.2996 -0.6006 288 HIS A CE1 1629 N NE2 . HIS A 200 ? 0.8667 1.8435 1.0766 0.5048 -0.2653 -0.5821 288 HIS A NE2 1630 N N . PRO A 201 ? 1.0442 1.7800 1.0585 0.6533 -0.2458 -0.5134 289 PRO A N 1631 C CA . PRO A 201 ? 1.0931 1.7282 1.0497 0.6703 -0.2329 -0.4864 289 PRO A CA 1632 C C . PRO A 201 ? 1.1729 1.6477 1.0057 0.7220 -0.2556 -0.4519 289 PRO A C 1633 O O . PRO A 201 ? 1.1129 1.4628 0.8863 0.7135 -0.2370 -0.4169 289 PRO A O 1634 C CB . PRO A 201 ? 1.1052 1.8382 1.0955 0.6990 -0.2404 -0.5249 289 PRO A CB 1635 C CG . PRO A 201 ? 0.9788 1.8750 1.0647 0.6720 -0.2424 -0.5711 289 PRO A CG 1636 C CD . PRO A 201 ? 1.0655 1.9473 1.1402 0.6676 -0.2598 -0.5666 289 PRO A CD 1637 N N . ASN A 202 ? 1.2123 1.6899 1.0017 0.7709 -0.2924 -0.4641 290 ASN A N 1638 C CA . ASN A 202 ? 1.3828 1.7099 1.0432 0.8218 -0.3129 -0.4337 290 ASN A CA 1639 C C . ASN A 202 ? 1.3902 1.5848 0.9891 0.7941 -0.3012 -0.3882 290 ASN A C 1640 O O . ASN A 202 ? 1.3645 1.4081 0.8557 0.8134 -0.2997 -0.3536 290 ASN A O 1641 C CB . ASN A 202 ? 1.4785 1.8520 1.1026 0.8848 -0.3533 -0.4646 290 ASN A CB 1642 C CG . ASN A 202 ? 1.6075 1.9113 1.1405 0.9534 -0.3712 -0.4642 290 ASN A CG 1643 O OD1 . ASN A 202 ? 1.6255 1.8999 1.1581 0.9527 -0.3552 -0.4568 290 ASN A OD1 1644 N ND2 . ASN A 202 ? 1.6788 1.9528 1.1302 1.0146 -0.4027 -0.4739 290 ASN A ND2 1645 N N . GLN A 203 ? 1.3519 1.5979 1.0145 0.7468 -0.2905 -0.3889 291 GLN A N 1646 C CA . GLN A 203 ? 1.3939 1.5160 0.9932 0.7252 -0.2818 -0.3484 291 GLN A CA 1647 C C . GLN A 203 ? 1.3574 1.4039 0.9617 0.6686 -0.2416 -0.3179 291 GLN A C 1648 O O . GLN A 203 ? 1.0282 1.1576 0.7215 0.6224 -0.2169 -0.3314 291 GLN A O 1649 C CB . GLN A 203 ? 1.4184 1.5991 1.0476 0.7176 -0.2977 -0.3612 291 GLN A CB 1650 C CG . GLN A 203 ? 1.2861 1.5568 1.0240 0.6553 -0.2741 -0.3716 291 GLN A CG 1651 C CD . GLN A 203 ? 1.2207 1.4721 0.9500 0.6419 -0.2819 -0.3627 291 GLN A CD 1652 O OE1 . GLN A 203 ? 1.2308 1.5990 1.0506 0.6115 -0.2821 -0.3900 291 GLN A OE1 1653 N NE2 . GLN A 203 ? 1.1770 1.2783 0.7964 0.6559 -0.2847 -0.3232 291 GLN A NE2 1654 N N . PRO A 204 ? 1.4162 1.3026 0.9172 0.6684 -0.2317 -0.2791 292 PRO A N 1655 C CA . PRO A 204 ? 1.3069 1.1133 0.7980 0.6149 -0.1941 -0.2545 292 PRO A CA 1656 C C . PRO A 204 ? 1.1849 1.0244 0.7304 0.5595 -0.1747 -0.2514 292 PRO A C 1657 O O . PRO A 204 ? 1.2319 1.0532 0.7599 0.5583 -0.1850 -0.2428 292 PRO A O 1658 C CB . PRO A 204 ? 1.4362 1.0727 0.8024 0.6235 -0.1909 -0.2176 292 PRO A CB 1659 C CG . PRO A 204 ? 1.5343 1.1632 0.8403 0.6929 -0.2248 -0.2265 292 PRO A CG 1660 C CD . PRO A 204 ? 1.4799 1.2534 0.8620 0.7141 -0.2523 -0.2594 292 PRO A CD 1661 N N . PHE A 205 ? 1.1155 1.0053 0.7222 0.5115 -0.1465 -0.2578 293 PHE A N 1662 C CA . PHE A 205 ? 0.9655 0.9039 0.6349 0.4368 -0.1266 -0.2425 293 PHE A CA 1663 C C . PHE A 205 ? 0.9993 0.8928 0.6628 0.3851 -0.0949 -0.2221 293 PHE A C 1664 O O . PHE A 205 ? 1.0775 1.0226 0.7758 0.3797 -0.0822 -0.2368 293 PHE A O 1665 C CB . PHE A 205 ? 0.8225 0.9180 0.5980 0.4240 -0.1282 -0.2736 293 PHE A CB 1666 C CG . PHE A 205 ? 0.7428 0.8799 0.5745 0.3560 -0.1104 -0.2602 293 PHE A CG 1667 C CD1 . PHE A 205 ? 0.7325 0.7821 0.5274 0.3138 -0.0953 -0.2231 293 PHE A CD1 1668 C CD2 . PHE A 205 ? 0.6860 0.9501 0.6068 0.3344 -0.1071 -0.2876 293 PHE A CD2 1669 C CE1 . PHE A 205 ? 0.6696 0.7519 0.5111 0.2592 -0.0798 -0.2115 293 PHE A CE1 1670 C CE2 . PHE A 205 ? 0.6289 0.9156 0.5922 0.2734 -0.0885 -0.2753 293 PHE A CE2 1671 C CZ . PHE A 205 ? 0.6714 0.8644 0.5928 0.2398 -0.0762 -0.2362 293 PHE A CZ 1672 N N . TYR A 206 ? 0.9924 0.7970 0.6124 0.3475 -0.0821 -0.1909 294 TYR A N 1673 C CA . TYR A 206 ? 0.9722 0.7319 0.5785 0.3030 -0.0561 -0.1747 294 TYR A CA 1674 C C . TYR A 206 ? 0.9341 0.7448 0.5972 0.2412 -0.0385 -0.1576 294 TYR A C 1675 O O . TYR A 206 ? 0.9306 0.7760 0.6246 0.2296 -0.0441 -0.1527 294 TYR A O 1676 C CB . TYR A 206 ? 0.9541 0.5730 0.4645 0.3055 -0.0513 -0.1565 294 TYR A CB 1677 C CG . TYR A 206 ? 1.0630 0.6040 0.4992 0.3678 -0.0645 -0.1694 294 TYR A CG 1678 C CD1 . TYR A 206 ? 1.2747 0.7886 0.6703 0.4224 -0.0898 -0.1708 294 TYR A CD1 1679 C CD2 . TYR A 206 ? 1.1118 0.6053 0.5155 0.3725 -0.0526 -0.1784 294 TYR A CD2 1680 C CE1 . TYR A 206 ? 1.4418 0.9006 0.7794 0.4688 -0.1038 -0.1683 294 TYR A CE1 1681 C CE2 . TYR A 206 ? 1.4037 0.8395 0.7552 0.4159 -0.0643 -0.1774 294 TYR A CE2 1682 C CZ . TYR A 206 ? 1.4839 0.9009 0.7993 0.4651 -0.0900 -0.1711 294 TYR A CZ 1683 O OH . TYR A 206 ? 1.5584 0.9137 0.8091 0.5117 -0.1022 -0.1695 294 TYR A OH 1684 N N . ILE A 207 ? 0.8607 0.6737 0.5328 0.2055 -0.0181 -0.1503 295 ILE A N 1685 C CA . ILE A 207 ? 0.7232 0.5678 0.4324 0.1544 -0.0019 -0.1311 295 ILE A CA 1686 C C . ILE A 207 ? 0.7555 0.5197 0.4148 0.1289 0.0085 -0.1145 295 ILE A C 1687 O O . ILE A 207 ? 0.8841 0.6063 0.5068 0.1310 0.0144 -0.1219 295 ILE A O 1688 C CB . ILE A 207 ? 0.7353 0.6568 0.4917 0.1353 0.0136 -0.1373 295 ILE A CB 1689 C CG1 . ILE A 207 ? 0.6327 0.6414 0.4416 0.1549 0.0094 -0.1600 295 ILE A CG1 1690 C CG2 . ILE A 207 ? 0.6800 0.6233 0.4621 0.0905 0.0292 -0.1145 295 ILE A CG2 1691 C CD1 . ILE A 207 ? 0.7533 0.8308 0.5992 0.1354 0.0295 -0.1660 295 ILE A CD1 1692 N N . LEU A 208 ? 0.7288 0.4746 0.3878 0.1035 0.0120 -0.0960 296 LEU A N 1693 C CA . LEU A 208 ? 0.8134 0.5033 0.4376 0.0729 0.0247 -0.0844 296 LEU A CA 1694 C C . LEU A 208 ? 0.7754 0.5130 0.4277 0.0433 0.0375 -0.0836 296 LEU A C 1695 O O . LEU A 208 ? 0.7249 0.5330 0.4258 0.0354 0.0400 -0.0781 296 LEU A O 1696 C CB . LEU A 208 ? 0.7331 0.4107 0.3602 0.0555 0.0260 -0.0677 296 LEU A CB 1697 C CG . LEU A 208 ? 0.7819 0.4067 0.3747 0.0237 0.0405 -0.0593 296 LEU A CG 1698 C CD1 . LEU A 208 ? 0.9610 0.4876 0.4790 0.0345 0.0439 -0.0663 296 LEU A CD1 1699 C CD2 . LEU A 208 ? 0.7562 0.3832 0.3594 0.0106 0.0423 -0.0450 296 LEU A CD2 1700 N N . LYS A 209 ? 0.8710 0.5690 0.4889 0.0267 0.0464 -0.0904 297 LYS A N 1701 C CA . LYS A 209 ? 0.8246 0.5742 0.4659 -0.0004 0.0552 -0.0912 297 LYS A CA 1702 C C . LYS A 209 ? 0.8067 0.5947 0.4803 -0.0234 0.0584 -0.0726 297 LYS A C 1703 O O . LYS A 209 ? 0.7655 0.5181 0.4269 -0.0324 0.0598 -0.0650 297 LYS A O 1704 C CB . LYS A 209 ? 0.7411 0.4441 0.3407 -0.0191 0.0639 -0.1079 297 LYS A CB 1705 C CG . LYS A 209 ? 0.8690 0.5391 0.4370 0.0045 0.0628 -0.1285 297 LYS A CG 1706 C CD . LYS A 209 ? 0.9501 0.6043 0.4925 -0.0209 0.0729 -0.1491 297 LYS A CD 1707 C CE . LYS A 209 ? 1.1383 0.7008 0.6200 -0.0007 0.0759 -0.1692 297 LYS A CE 1708 N NZ . LYS A 209 ? 1.1327 0.7201 0.6114 0.0088 0.0773 -0.1922 297 LYS A NZ 1709 N N . PRO A 210 ? 0.8035 0.6593 0.5119 -0.0297 0.0605 -0.0650 298 PRO A N 1710 C CA . PRO A 210 ? 0.7002 0.5918 0.4358 -0.0421 0.0626 -0.0467 298 PRO A CA 1711 C C . PRO A 210 ? 0.7014 0.5885 0.4271 -0.0653 0.0661 -0.0503 298 PRO A C 1712 O O . PRO A 210 ? 0.7208 0.6213 0.4626 -0.0715 0.0672 -0.0387 298 PRO A O 1713 C CB . PRO A 210 ? 0.6421 0.5921 0.3962 -0.0387 0.0656 -0.0402 298 PRO A CB 1714 C CG . PRO A 210 ? 0.6958 0.6463 0.4308 -0.0346 0.0662 -0.0594 298 PRO A CG 1715 C CD . PRO A 210 ? 0.8004 0.6981 0.5172 -0.0209 0.0623 -0.0727 298 PRO A CD 1716 N N . GLN A 211 ? 0.6690 0.5391 0.3694 -0.0791 0.0694 -0.0701 299 GLN A N 1717 C CA . GLN A 211 ? 0.7211 0.5961 0.4167 -0.1086 0.0757 -0.0814 299 GLN A CA 1718 C C . GLN A 211 ? 0.8407 0.6569 0.5173 -0.1217 0.0840 -0.0794 299 GLN A C 1719 O O . GLN A 211 ? 0.7963 0.6339 0.4839 -0.1450 0.0913 -0.0833 299 GLN A O 1720 C CB . GLN A 211 ? 0.6898 0.5556 0.3605 -0.1269 0.0802 -0.1086 299 GLN A CB 1721 C CG . GLN A 211 ? 0.7654 0.6978 0.4491 -0.1191 0.0732 -0.1151 299 GLN A CG 1722 C CD . GLN A 211 ? 0.8277 0.7352 0.4945 -0.0958 0.0716 -0.1179 299 GLN A CD 1723 O OE1 . GLN A 211 ? 0.7635 0.6298 0.4256 -0.0759 0.0707 -0.1079 299 GLN A OE1 1724 N NE2 . GLN A 211 ? 0.8024 0.7417 0.4608 -0.0959 0.0705 -0.1344 299 GLN A NE2 1725 N N . MET A 212 ? 0.8508 0.5968 0.4965 -0.1050 0.0832 -0.0748 300 MET A N 1726 C CA . MET A 212 ? 0.8469 0.5234 0.4572 -0.1166 0.0931 -0.0727 300 MET A CA 1727 C C . MET A 212 ? 0.8558 0.5632 0.4939 -0.1229 0.0953 -0.0587 300 MET A C 1728 O O . MET A 212 ? 0.8112 0.5056 0.4385 -0.1510 0.1100 -0.0645 300 MET A O 1729 C CB . MET A 212 ? 0.8908 0.4849 0.4532 -0.0877 0.0881 -0.0699 300 MET A CB 1730 C CG . MET A 212 ? 1.0013 0.5012 0.5033 -0.0975 0.1010 -0.0673 300 MET A CG 1731 S SD . MET A 212 ? 1.1437 0.6519 0.6582 -0.0822 0.0942 -0.0471 300 MET A SD 1732 C CE . MET A 212 ? 1.1233 0.4994 0.5409 -0.0649 0.0997 -0.0428 300 MET A CE 1733 N N . PRO A 213 ? 0.8089 0.5563 0.4819 -0.0995 0.0837 -0.0429 301 PRO A N 1734 C CA . PRO A 213 ? 0.7537 0.5187 0.4461 -0.1035 0.0870 -0.0322 301 PRO A CA 1735 C C . PRO A 213 ? 0.7773 0.6030 0.4985 -0.1253 0.0947 -0.0383 301 PRO A C 1736 O O . PRO A 213 ? 0.7763 0.6046 0.5012 -0.1369 0.1039 -0.0380 301 PRO A O 1737 C CB . PRO A 213 ? 0.7139 0.5118 0.4391 -0.0783 0.0753 -0.0182 301 PRO A CB 1738 C CG . PRO A 213 ? 0.6551 0.4399 0.3713 -0.0604 0.0667 -0.0226 301 PRO A CG 1739 C CD . PRO A 213 ? 0.7587 0.5285 0.4506 -0.0717 0.0710 -0.0369 301 PRO A CD 1740 N N . TRP A 214 ? 0.6888 0.5689 0.4296 -0.1281 0.0902 -0.0459 302 TRP A N 1741 C CA . TRP A 214 ? 0.6905 0.6436 0.4615 -0.1410 0.0924 -0.0549 302 TRP A CA 1742 C C . TRP A 214 ? 0.6974 0.6445 0.4543 -0.1802 0.1075 -0.0810 302 TRP A C 1743 O O . TRP A 214 ? 0.6714 0.6716 0.4526 -0.1978 0.1148 -0.0936 302 TRP A O 1744 C CB . TRP A 214 ? 0.6067 0.6263 0.3991 -0.1242 0.0797 -0.0526 302 TRP A CB 1745 C CG . TRP A 214 ? 0.5153 0.5407 0.3206 -0.0922 0.0719 -0.0261 302 TRP A CG 1746 C CD1 . TRP A 214 ? 0.5885 0.6034 0.3877 -0.0759 0.0674 -0.0149 302 TRP A CD1 1747 C CD2 . TRP A 214 ? 0.6039 0.6404 0.4273 -0.0767 0.0720 -0.0102 302 TRP A CD2 1748 N NE1 . TRP A 214 ? 0.5500 0.5656 0.3612 -0.0560 0.0668 0.0071 302 TRP A NE1 1749 C CE2 . TRP A 214 ? 0.5852 0.6094 0.4092 -0.0544 0.0686 0.0106 302 TRP A CE2 1750 C CE3 . TRP A 214 ? 0.5889 0.6435 0.4269 -0.0804 0.0769 -0.0139 302 TRP A CE3 1751 C CZ2 . TRP A 214 ? 0.6024 0.6204 0.4362 -0.0368 0.0701 0.0283 302 TRP A CZ2 1752 C CZ3 . TRP A 214 ? 0.6144 0.6691 0.4644 -0.0571 0.0759 0.0037 302 TRP A CZ3 1753 C CH2 . TRP A 214 ? 0.5472 0.5781 0.3927 -0.0360 0.0726 0.0247 302 TRP A CH2 1754 N N . GLU A 215 ? 0.7020 0.5826 0.4182 -0.1948 0.1144 -0.0919 303 GLU A N 1755 C CA . GLU A 215 ? 0.7449 0.5996 0.4381 -0.2389 0.1350 -0.1174 303 GLU A CA 1756 C C . GLU A 215 ? 0.7893 0.6025 0.4663 -0.2538 0.1527 -0.1112 303 GLU A C 1757 O O . GLU A 215 ? 0.9028 0.7377 0.5860 -0.2923 0.1725 -0.1309 303 GLU A O 1758 C CB . GLU A 215 ? 0.8335 0.6038 0.4739 -0.2471 0.1408 -0.1284 303 GLU A CB 1759 C CG . GLU A 215 ? 0.8625 0.6786 0.5158 -0.2413 0.1282 -0.1430 303 GLU A CG 1760 C CD . GLU A 215 ? 1.0395 0.7664 0.6407 -0.2305 0.1293 -0.1472 303 GLU A CD 1761 O OE1 . GLU A 215 ? 1.0237 0.6493 0.5735 -0.2308 0.1409 -0.1413 303 GLU A OE1 1762 O OE2 . GLU A 215 ? 1.1384 0.8948 0.7452 -0.2182 0.1187 -0.1567 303 GLU A OE2 1763 N N . LEU A 216 ? 0.8459 0.6068 0.5035 -0.2245 0.1465 -0.0867 304 LEU A N 1764 C CA . LEU A 216 ? 0.8750 0.5951 0.5104 -0.2350 0.1626 -0.0802 304 LEU A CA 1765 C C . LEU A 216 ? 0.8705 0.6819 0.5623 -0.2337 0.1620 -0.0802 304 LEU A C 1766 O O . LEU A 216 ? 0.9237 0.7445 0.6157 -0.2610 0.1828 -0.0907 304 LEU A O 1767 C CB . LEU A 216 ? 0.8562 0.4988 0.4513 -0.2008 0.1525 -0.0581 304 LEU A CB 1768 C CG . LEU A 216 ? 0.9783 0.5750 0.5419 -0.2043 0.1660 -0.0490 304 LEU A CG 1769 C CD1 . LEU A 216 ? 1.0716 0.6032 0.5813 -0.2478 0.1982 -0.0613 304 LEU A CD1 1770 C CD2 . LEU A 216 ? 0.8525 0.3862 0.3785 -0.1649 0.1494 -0.0316 304 LEU A CD2 1771 N N . TRP A 217 ? 0.7959 0.6731 0.5324 -0.2018 0.1404 -0.0699 305 TRP A N 1772 C CA . TRP A 217 ? 0.6650 0.6226 0.4495 -0.1897 0.1370 -0.0684 305 TRP A CA 1773 C C . TRP A 217 ? 0.6575 0.6969 0.4740 -0.2182 0.1474 -0.0960 305 TRP A C 1774 O O . TRP A 217 ? 0.7291 0.8170 0.5717 -0.2215 0.1563 -0.1035 305 TRP A O 1775 C CB . TRP A 217 ? 0.5905 0.5878 0.4027 -0.1513 0.1148 -0.0516 305 TRP A CB 1776 C CG . TRP A 217 ? 0.5931 0.6462 0.4401 -0.1281 0.1106 -0.0444 305 TRP A CG 1777 C CD1 . TRP A 217 ? 0.4935 0.5174 0.3400 -0.1060 0.1094 -0.0272 305 TRP A CD1 1778 C CD2 . TRP A 217 ? 0.6057 0.7520 0.4897 -0.1194 0.1053 -0.0559 305 TRP A CD2 1779 N NE1 . TRP A 217 ? 0.6288 0.7115 0.5061 -0.0838 0.1061 -0.0258 305 TRP A NE1 1780 C CE2 . TRP A 217 ? 0.6158 0.7768 0.5163 -0.0880 0.1021 -0.0424 305 TRP A CE2 1781 C CE3 . TRP A 217 ? 0.6050 0.8266 0.5087 -0.1323 0.1014 -0.0789 305 TRP A CE3 1782 C CZ2 . TRP A 217 ? 0.5355 0.7802 0.4680 -0.0634 0.0945 -0.0489 305 TRP A CZ2 1783 C CZ3 . TRP A 217 ? 0.5565 0.8728 0.4963 -0.1096 0.0918 -0.0876 305 TRP A CZ3 1784 C CH2 . TRP A 217 ? 0.5877 0.9131 0.5400 -0.0724 0.0881 -0.0713 305 TRP A CH2 1785 N N . ASP A 218 ? 0.7675 0.8296 0.5844 -0.2385 0.1462 -0.1154 306 ASP A N 1786 C CA . ASP A 218 ? 0.7276 0.8839 0.5812 -0.2677 0.1535 -0.1490 306 ASP A CA 1787 C C . ASP A 218 ? 0.7945 0.9361 0.6404 -0.3119 0.1850 -0.1676 306 ASP A C 1788 O O . ASP A 218 ? 0.8154 1.0497 0.7058 -0.3237 0.1926 -0.1893 306 ASP A O 1789 C CB . ASP A 218 ? 0.7662 0.9338 0.6118 -0.2906 0.1503 -0.1720 306 ASP A CB 1790 C CG . ASP A 218 ? 0.7865 1.0062 0.6495 -0.2503 0.1214 -0.1615 306 ASP A CG 1791 O OD1 . ASP A 218 ? 0.7100 0.9707 0.5965 -0.2091 0.1060 -0.1405 306 ASP A OD1 1792 O OD2 . ASP A 218 ? 0.9015 1.1151 0.7488 -0.2596 0.1160 -0.1741 306 ASP A OD2 1793 N N . ILE A 219 ? 0.8053 0.8305 0.5910 -0.3339 0.2043 -0.1596 307 ILE A N 1794 C CA . ILE A 219 ? 0.9314 0.9205 0.6919 -0.3819 0.2407 -0.1752 307 ILE A CA 1795 C C . ILE A 219 ? 0.8905 0.9034 0.6682 -0.3634 0.2456 -0.1627 307 ILE A C 1796 O O . ILE A 219 ? 0.9888 1.0600 0.7920 -0.3941 0.2689 -0.1856 307 ILE A O 1797 C CB . ILE A 219 ? 0.9758 0.8153 0.6499 -0.4017 0.2591 -0.1650 307 ILE A CB 1798 C CG1 . ILE A 219 ? 0.9398 0.7551 0.5980 -0.4097 0.2502 -0.1771 307 ILE A CG1 1799 C CG2 . ILE A 219 ? 1.1667 0.9582 0.8033 -0.4479 0.2964 -0.1812 307 ILE A CG2 1800 C CD1 . ILE A 219 ? 1.0220 0.7031 0.5975 -0.4453 0.2780 -0.1828 307 ILE A CD1 1801 N N . LEU A 220 ? 0.8516 0.8267 0.6190 -0.3140 0.2241 -0.1302 308 LEU A N 1802 C CA . LEU A 220 ? 0.7808 0.7764 0.5646 -0.2893 0.2242 -0.1184 308 LEU A CA 1803 C C . LEU A 220 ? 0.7815 0.9087 0.6366 -0.2813 0.2205 -0.1380 308 LEU A C 1804 O O . LEU A 220 ? 0.7740 0.9428 0.6453 -0.3026 0.2436 -0.1560 308 LEU A O 1805 C CB . LEU A 220 ? 0.7466 0.6949 0.5177 -0.2394 0.1980 -0.0866 308 LEU A CB 1806 C CG . LEU A 220 ? 0.7954 0.6239 0.4970 -0.2382 0.1993 -0.0697 308 LEU A CG 1807 C CD1 . LEU A 220 ? 0.6841 0.4911 0.3880 -0.1924 0.1714 -0.0467 308 LEU A CD1 1808 C CD2 . LEU A 220 ? 0.9158 0.6809 0.5670 -0.2584 0.2261 -0.0691 308 LEU A CD2 1809 N N . GLN A 221 ? 0.8065 0.9999 0.7001 -0.2493 0.1928 -0.1358 309 GLN A N 1810 C CA . GLN A 221 ? 0.7070 1.0268 0.6624 -0.2295 0.1832 -0.1536 309 GLN A CA 1811 C C . GLN A 221 ? 0.7257 1.1307 0.7130 -0.2777 0.2055 -0.1966 309 GLN A C 1812 O O . GLN A 221 ? 0.7503 1.2517 0.7839 -0.2717 0.2114 -0.2174 309 GLN A O 1813 C CB . GLN A 221 ? 0.6951 1.0607 0.6693 -0.1934 0.1519 -0.1457 309 GLN A CB 1814 C CG . GLN A 221 ? 0.6361 1.1289 0.6644 -0.1619 0.1380 -0.1622 309 GLN A CG 1815 C CD . GLN A 221 ? 0.6708 1.1606 0.7077 -0.1202 0.1367 -0.1453 309 GLN A CD 1816 O OE1 . GLN A 221 ? 0.6598 1.0966 0.6775 -0.0782 0.1211 -0.1131 309 GLN A OE1 1817 N NE2 . GLN A 221 ? 0.6783 1.2196 0.7415 -0.1352 0.1568 -0.1688 309 GLN A NE2 1818 N N . GLU A 222 ? 0.7337 1.1047 0.6970 -0.3267 0.2195 -0.2135 310 GLU A N 1819 C CA . GLU A 222 ? 0.8372 1.2819 0.8283 -0.3852 0.2463 -0.2595 310 GLU A CA 1820 C C . GLU A 222 ? 0.8172 1.2282 0.7921 -0.4153 0.2795 -0.2666 310 GLU A C 1821 O O . GLU A 222 ? 0.7927 1.2860 0.8063 -0.4336 0.2870 -0.3005 310 GLU A O 1822 C CB . GLU A 222 ? 0.8485 1.2398 0.8057 -0.4334 0.2566 -0.2758 310 GLU A CB 1823 C CG . GLU A 222 ? 0.9165 1.3740 0.8971 -0.4830 0.2719 -0.3265 310 GLU A CG 1824 C CD . GLU A 222 ? 1.0755 1.4367 0.9978 -0.5275 0.2887 -0.3401 310 GLU A CD 1825 O OE1 . GLU A 222 ? 1.1593 1.3867 1.0168 -0.5245 0.2936 -0.3092 310 GLU A OE1 1826 O OE2 . GLU A 222 ? 1.1306 1.5500 1.0684 -0.5609 0.2980 -0.3827 310 GLU A OE2 1827 N N . ILE A 223 ? 0.8515 1.1332 0.7625 -0.4111 0.2910 -0.2340 311 ILE A N 1828 C CA . ILE A 223 ? 1.0155 1.2449 0.8973 -0.4284 0.3142 -0.2350 311 ILE A CA 1829 C C . ILE A 223 ? 1.0493 1.3624 0.9787 -0.3954 0.3123 -0.2352 311 ILE A C 1830 O O . ILE A 223 ? 1.0860 1.4410 1.0342 -0.4144 0.3290 -0.2581 311 ILE A O 1831 C CB . ILE A 223 ? 1.0861 1.1577 0.8820 -0.4215 0.3203 -0.1992 311 ILE A CB 1832 C CG1 . ILE A 223 ? 1.1492 1.1184 0.8824 -0.4557 0.3310 -0.2044 311 ILE A CG1 1833 C CG2 . ILE A 223 ? 1.2742 1.3080 1.0446 -0.4226 0.3387 -0.1941 311 ILE A CG2 1834 C CD1 . ILE A 223 ? 1.2026 1.0220 0.8482 -0.4379 0.3322 -0.1711 311 ILE A CD1 1835 N N . SER A 224 ? 1.0088 1.3410 0.9520 -0.3446 0.2939 -0.2112 312 SER A N 1836 C CA . SER A 224 ? 0.8702 1.2376 0.8359 -0.3039 0.2908 -0.2044 312 SER A CA 1837 C C . SER A 224 ? 0.8931 1.4179 0.9386 -0.2902 0.2879 -0.2386 312 SER A C 1838 O O . SER A 224 ? 0.8932 1.5077 0.9822 -0.2881 0.2710 -0.2583 312 SER A O 1839 C CB . SER A 224 ? 0.7537 1.0589 0.7013 -0.2441 0.2567 -0.1658 312 SER A CB 1840 O OG . SER A 224 ? 0.7145 0.8915 0.5951 -0.2552 0.2564 -0.1406 312 SER A OG 1841 N N . PRO A 225 ? 0.9671 1.5229 1.0291 -0.2752 0.2989 -0.2461 313 PRO A N 1842 C CA . PRO A 225 ? 0.9429 1.6408 1.0769 -0.2571 0.2912 -0.2798 313 PRO A CA 1843 C C . PRO A 225 ? 0.9049 1.6813 1.0789 -0.1851 0.2615 -0.2730 313 PRO A C 1844 O O . PRO A 225 ? 1.0237 1.9150 1.2524 -0.1533 0.2473 -0.2970 313 PRO A O 1845 C CB . PRO A 225 ? 0.9207 1.6039 1.0465 -0.2599 0.3142 -0.2843 313 PRO A CB 1846 C CG . PRO A 225 ? 0.9326 1.4943 0.9966 -0.2413 0.3199 -0.2465 313 PRO A CG 1847 C CD . PRO A 225 ? 0.9411 1.4067 0.9551 -0.2670 0.3153 -0.2248 313 PRO A CD 1848 N N . GLU A 226 ? 0.8217 1.4986 0.9545 -0.1510 0.2366 -0.2318 314 GLU A N 1849 C CA . GLU A 226 ? 0.7413 1.4409 0.8891 -0.0782 0.2012 -0.2130 314 GLU A CA 1850 C C . GLU A 226 ? 0.6927 1.2985 0.7997 -0.0647 0.1769 -0.1762 314 GLU A C 1851 O O . GLU A 226 ? 0.6842 1.2030 0.7514 -0.1050 0.1856 -0.1641 314 GLU A O 1852 C CB . GLU A 226 ? 0.7097 1.3751 0.8484 -0.0343 0.2043 -0.1999 314 GLU A CB 1853 C CG . GLU A 226 ? 0.7152 1.2321 0.7924 -0.0368 0.2058 -0.1634 314 GLU A CG 1854 C CD . GLU A 226 ? 0.7976 1.2805 0.8631 -0.0092 0.2164 -0.1598 314 GLU A CD 1855 O OE1 . GLU A 226 ? 0.7267 1.2897 0.8294 0.0307 0.2151 -0.1772 314 GLU A OE1 1856 O OE2 . GLU A 226 ? 0.8607 1.2390 0.8783 -0.0247 0.2249 -0.1420 314 GLU A OE2 1857 N N . GLU A 227 ? 0.6848 1.3057 0.7972 -0.0056 0.1481 -0.1584 315 GLU A N 1858 C CA . GLU A 227 ? 0.7236 1.2619 0.7985 0.0087 0.1284 -0.1242 315 GLU A CA 1859 C C . GLU A 227 ? 0.7196 1.1278 0.7488 0.0014 0.1368 -0.0956 315 GLU A C 1860 O O . GLU A 227 ? 0.7450 1.1211 0.7675 0.0247 0.1428 -0.0887 315 GLU A O 1861 C CB . GLU A 227 ? 0.8468 1.4133 0.9252 0.0758 0.1018 -0.1078 315 GLU A CB 1862 C CG . GLU A 227 ? 1.0147 1.7161 1.1338 0.0949 0.0857 -0.1355 315 GLU A CG 1863 C CD . GLU A 227 ? 1.1919 1.9057 1.2977 0.1698 0.0587 -0.1142 315 GLU A CD 1864 O OE1 . GLU A 227 ? 1.2318 1.9083 1.3252 0.2167 0.0590 -0.0988 315 GLU A OE1 1865 O OE2 . GLU A 227 ? 1.2691 2.0220 1.3696 0.1827 0.0383 -0.1125 315 GLU A OE2 1866 N N . ILE A 228 ? 0.6144 0.9529 0.6125 -0.0286 0.1358 -0.0823 316 ILE A N 1867 C CA . ILE A 228 ? 0.6473 0.8751 0.6045 -0.0341 0.1391 -0.0592 316 ILE A CA 1868 C C . ILE A 228 ? 0.6628 0.8468 0.6055 -0.0029 0.1195 -0.0317 316 ILE A C 1869 O O . ILE A 228 ? 0.6606 0.8893 0.6146 0.0152 0.1054 -0.0287 316 ILE A O 1870 C CB . ILE A 228 ? 0.7077 0.8853 0.6356 -0.0830 0.1514 -0.0643 316 ILE A CB 1871 C CG1 . ILE A 228 ? 0.6079 0.7876 0.5317 -0.0923 0.1383 -0.0611 316 ILE A CG1 1872 C CG2 . ILE A 228 ? 0.7204 0.9439 0.6593 -0.1222 0.1759 -0.0932 316 ILE A CG2 1873 C CD1 . ILE A 228 ? 0.5437 0.6768 0.4362 -0.1394 0.1522 -0.0712 316 ILE A CD1 1874 N N . GLN A 229 ? 0.5927 0.6931 0.5091 0.0025 0.1199 -0.0137 317 GLN A N 1875 C CA . GLN A 229 ? 0.6048 0.6593 0.5068 0.0210 0.1078 0.0093 317 GLN A CA 1876 C C . GLN A 229 ? 0.6275 0.6988 0.5269 0.0068 0.0992 0.0111 317 GLN A C 1877 O O . GLN A 229 ? 0.6193 0.6794 0.5097 -0.0255 0.1034 0.0010 317 GLN A O 1878 C CB . GLN A 229 ? 0.6434 0.6168 0.5217 0.0110 0.1109 0.0177 317 GLN A CB 1879 C CG . GLN A 229 ? 0.6778 0.6209 0.5527 0.0282 0.1178 0.0173 317 GLN A CG 1880 C CD . GLN A 229 ? 0.7065 0.6494 0.5748 0.0098 0.1298 0.0005 317 GLN A CD 1881 O OE1 . GLN A 229 ? 0.6482 0.6348 0.5238 -0.0095 0.1376 -0.0130 317 GLN A OE1 1882 N NE2 . GLN A 229 ? 0.7176 0.6094 0.5687 0.0127 0.1336 -0.0006 317 GLN A NE2 1883 N N . PRO A 230 ? 0.6196 0.7115 0.5199 0.0329 0.0883 0.0242 318 PRO A N 1884 C CA . PRO A 230 ? 0.5750 0.6856 0.4698 0.0228 0.0799 0.0252 318 PRO A CA 1885 C C . PRO A 230 ? 0.6281 0.6712 0.5019 0.0122 0.0808 0.0397 318 PRO A C 1886 O O . PRO A 230 ? 0.6781 0.7169 0.5412 0.0222 0.0761 0.0529 318 PRO A O 1887 C CB . PRO A 230 ? 0.6513 0.8045 0.5460 0.0623 0.0688 0.0362 318 PRO A CB 1888 C CG . PRO A 230 ? 0.6660 0.7760 0.5514 0.0937 0.0733 0.0528 318 PRO A CG 1889 C CD . PRO A 230 ? 0.5330 0.6366 0.4340 0.0769 0.0839 0.0364 318 PRO A CD 1890 N N . ASN A 231 ? 0.6706 0.6658 0.5374 -0.0066 0.0871 0.0355 319 ASN A N 1891 C CA . ASN A 231 ? 0.6195 0.5662 0.4729 -0.0158 0.0860 0.0418 319 ASN A CA 1892 C C . ASN A 231 ? 0.6674 0.5989 0.5085 -0.0404 0.0869 0.0268 319 ASN A C 1893 O O . ASN A 231 ? 0.6393 0.5766 0.4777 -0.0528 0.0936 0.0153 319 ASN A O 1894 C CB . ASN A 231 ? 0.6304 0.5306 0.4814 -0.0083 0.0902 0.0488 319 ASN A CB 1895 C CG . ASN A 231 ? 0.7250 0.6215 0.5774 0.0167 0.0937 0.0640 319 ASN A CG 1896 O OD1 . ASN A 231 ? 0.7011 0.6097 0.5476 0.0291 0.0921 0.0770 319 ASN A OD1 1897 N ND2 . ASN A 231 ? 0.7154 0.5888 0.5682 0.0267 0.0993 0.0626 319 ASN A ND2 1898 N N . PRO A 232 ? 0.6536 0.5643 0.4833 -0.0465 0.0823 0.0263 320 PRO A N 1899 C CA . PRO A 232 ? 0.7235 0.6055 0.5298 -0.0634 0.0832 0.0135 320 PRO A CA 1900 C C . PRO A 232 ? 0.6809 0.5186 0.4666 -0.0676 0.0877 0.0099 320 PRO A C 1901 O O . PRO A 232 ? 0.6718 0.4992 0.4645 -0.0570 0.0870 0.0150 320 PRO A O 1902 C CB . PRO A 232 ? 0.6066 0.4737 0.4067 -0.0574 0.0757 0.0146 320 PRO A CB 1903 C CG . PRO A 232 ? 0.5565 0.4344 0.3773 -0.0441 0.0745 0.0269 320 PRO A CG 1904 C CD . PRO A 232 ? 0.5390 0.4462 0.3727 -0.0372 0.0787 0.0364 320 PRO A CD 1905 N N . PRO A 233 ? 0.7018 0.5069 0.4552 -0.0838 0.0941 0.0005 321 PRO A N 1906 C CA . PRO A 233 ? 0.7652 0.5178 0.4833 -0.0857 0.0992 -0.0008 321 PRO A CA 1907 C C . PRO A 233 ? 0.8267 0.5491 0.5344 -0.0636 0.0844 0.0029 321 PRO A C 1908 O O . PRO A 233 ? 0.7705 0.5071 0.4944 -0.0527 0.0733 0.0035 321 PRO A O 1909 C CB . PRO A 233 ? 0.7983 0.5065 0.4719 -0.1055 0.1096 -0.0089 321 PRO A CB 1910 C CG . PRO A 233 ? 0.7533 0.5118 0.4535 -0.1230 0.1141 -0.0176 321 PRO A CG 1911 C CD . PRO A 233 ? 0.6945 0.5053 0.4365 -0.1031 0.0997 -0.0102 321 PRO A CD 1912 N N . SER A 234 ? 0.7386 0.4269 0.4205 -0.0580 0.0847 0.0022 322 SER A N 1913 C CA . SER A 234 ? 0.7704 0.4422 0.4450 -0.0369 0.0684 -0.0005 322 SER A CA 1914 C C . SER A 234 ? 0.7391 0.3751 0.3764 -0.0230 0.0570 -0.0043 322 SER A C 1915 O O . SER A 234 ? 0.7568 0.3557 0.3565 -0.0315 0.0656 -0.0031 322 SER A O 1916 C CB . SER A 234 ? 0.7472 0.3942 0.3976 -0.0332 0.0710 -0.0028 322 SER A CB 1917 O OG . SER A 234 ? 0.8493 0.4393 0.4360 -0.0353 0.0780 -0.0019 322 SER A OG 1918 N N . SER A 235 ? 0.7286 0.3756 0.3750 -0.0012 0.0384 -0.0119 323 SER A N 1919 C CA . SER A 235 ? 0.7495 0.3637 0.3560 0.0223 0.0247 -0.0178 323 SER A CA 1920 C C . SER A 235 ? 0.7904 0.3253 0.3175 0.0284 0.0299 -0.0124 323 SER A C 1921 O O . SER A 235 ? 0.9153 0.3960 0.3913 0.0380 0.0308 -0.0108 323 SER A O 1922 C CB . SER A 235 ? 0.7788 0.4284 0.4079 0.0478 0.0022 -0.0327 323 SER A CB 1923 O OG . SER A 235 ? 0.7658 0.4806 0.4619 0.0370 0.0033 -0.0380 323 SER A OG 1924 N N . GLY A 236 ? 0.9942 0.5144 0.5038 0.0225 0.0361 -0.0094 324 GLY A N 1925 C CA . GLY A 236 ? 0.9466 0.3869 0.3730 0.0257 0.0457 -0.0025 324 GLY A CA 1926 C C . GLY A 236 ? 0.9502 0.3425 0.3420 -0.0034 0.0725 0.0051 324 GLY A C 1927 O O . GLY A 236 ? 1.1007 0.4097 0.4147 0.0048 0.0781 0.0101 324 GLY A O 1928 N N . MET A 237 ? 1.0055 0.4470 0.4501 -0.0371 0.0897 0.0040 325 MET A N 1929 C CA . MET A 237 ? 1.0331 0.4427 0.4527 -0.0706 0.1155 0.0038 325 MET A CA 1930 C C . MET A 237 ? 1.0483 0.4302 0.4518 -0.0640 0.1094 0.0004 325 MET A C 1931 O O . MET A 237 ? 1.1174 0.4209 0.4563 -0.0772 0.1263 0.0005 325 MET A O 1932 C CB . MET A 237 ? 0.9665 0.4535 0.4529 -0.1025 0.1304 -0.0019 325 MET A CB 1933 C CG . MET A 237 ? 1.0493 0.5141 0.5120 -0.1443 0.1603 -0.0093 325 MET A CG 1934 S SD . MET A 237 ? 1.1743 0.5555 0.5549 -0.1614 0.1885 -0.0046 325 MET A SD 1935 C CE . MET A 237 ? 1.1626 0.4601 0.4796 -0.1881 0.2099 -0.0133 325 MET A CE 1936 N N . LEU A 238 ? 0.9832 0.4239 0.4411 -0.0454 0.0887 -0.0038 326 LEU A N 1937 C CA . LEU A 238 ? 0.9444 0.3667 0.3906 -0.0356 0.0825 -0.0098 326 LEU A CA 1938 C C . LEU A 238 ? 1.0529 0.3867 0.4198 -0.0006 0.0728 -0.0076 326 LEU A C 1939 O O . LEU A 238 ? 1.1061 0.3699 0.4189 0.0001 0.0810 -0.0100 326 LEU A O 1940 C CB . LEU A 238 ? 0.8257 0.3291 0.3408 -0.0195 0.0637 -0.0148 326 LEU A CB 1941 C CG . LEU A 238 ? 0.7523 0.3422 0.3415 -0.0382 0.0667 -0.0131 326 LEU A CG 1942 C CD1 . LEU A 238 ? 0.7020 0.3468 0.3381 -0.0168 0.0497 -0.0153 326 LEU A CD1 1943 C CD2 . LEU A 238 ? 0.8815 0.4954 0.4857 -0.0661 0.0801 -0.0180 326 LEU A CD2 1944 N N . GLY A 239 ? 1.0818 0.4145 0.4360 0.0301 0.0554 -0.0043 327 GLY A N 1945 C CA . GLY A 239 ? 1.1155 0.3702 0.3897 0.0732 0.0413 -0.0022 327 GLY A CA 1946 C C . GLY A 239 ? 1.3174 0.4527 0.4906 0.0595 0.0666 0.0097 327 GLY A C 1947 O O . GLY A 239 ? 1.3640 0.4176 0.4618 0.0855 0.0650 0.0120 327 GLY A O 1948 N N . ILE A 240 ? 1.3692 0.5031 0.5430 0.0181 0.0921 0.0155 328 ILE A N 1949 C CA . ILE A 240 ? 1.4592 0.5197 0.5637 -0.0065 0.1219 0.0168 328 ILE A CA 1950 C C . ILE A 240 ? 1.5304 0.5648 0.6241 -0.0309 0.1394 0.0095 328 ILE A C 1951 O O . ILE A 240 ? 1.6243 0.5828 0.6437 -0.0187 0.1470 0.0100 328 ILE A O 1952 C CB . ILE A 240 ? 1.2887 0.3803 0.4187 -0.0487 0.1468 0.0154 328 ILE A CB 1953 C CG1 . ILE A 240 ? 1.2652 0.3495 0.3713 -0.0210 0.1342 0.0219 328 ILE A CG1 1954 C CG2 . ILE A 240 ? 1.2959 0.3375 0.3832 -0.0866 0.1817 0.0070 328 ILE A CG2 1955 C CD1 . ILE A 240 ? 1.1819 0.3439 0.3525 -0.0443 0.1402 0.0223 328 ILE A CD1 1956 N N . ILE A 241 ? 1.4029 0.4979 0.5668 -0.0634 0.1452 0.0019 329 ILE A N 1957 C CA . ILE A 241 ? 1.3894 0.4690 0.5493 -0.0897 0.1609 -0.0090 329 ILE A CA 1958 C C . ILE A 241 ? 1.3134 0.3428 0.4314 -0.0456 0.1422 -0.0073 329 ILE A C 1959 O O . ILE A 241 ? 1.3589 0.3300 0.4267 -0.0543 0.1576 -0.0101 329 ILE A O 1960 C CB . ILE A 241 ? 1.2961 0.4578 0.5408 -0.1246 0.1633 -0.0222 329 ILE A CB 1961 C CG1 . ILE A 241 ? 1.2371 0.4653 0.5297 -0.1616 0.1793 -0.0233 329 ILE A CG1 1962 C CG2 . ILE A 241 ? 1.3112 0.4604 0.5489 -0.1556 0.1805 -0.0378 329 ILE A CG2 1963 C CD1 . ILE A 241 ? 1.2282 0.4329 0.4911 -0.2067 0.2140 -0.0349 329 ILE A CD1 1964 N N . ILE A 242 ? 1.3693 0.4254 0.5101 0.0028 0.1095 -0.0058 330 ILE A N 1965 C CA . ILE A 242 ? 1.3928 0.4198 0.5047 0.0506 0.0891 -0.0087 330 ILE A CA 1966 C C . ILE A 242 ? 1.5872 0.5227 0.5986 0.0777 0.0922 0.0027 330 ILE A C 1967 O O . ILE A 242 ? 1.6706 0.5450 0.6304 0.0794 0.1029 0.0019 330 ILE A O 1968 C CB . ILE A 242 ? 1.3148 0.4041 0.4748 0.0998 0.0539 -0.0172 330 ILE A CB 1969 C CG1 . ILE A 242 ? 1.2761 0.4848 0.5426 0.0732 0.0517 -0.0286 330 ILE A CG1 1970 C CG2 . ILE A 242 ? 1.3495 0.4122 0.4720 0.1569 0.0318 -0.0211 330 ILE A CG2 1971 C CD1 . ILE A 242 ? 1.1521 0.4627 0.4902 0.1050 0.0237 -0.0355 330 ILE A CD1 1972 N N . MET A 243 ? 1.5851 0.5069 0.5631 0.0984 0.0843 0.0107 331 MET A N 1973 C CA . MET A 243 ? 1.5572 0.3898 0.4313 0.1289 0.0865 0.0168 331 MET A CA 1974 C C . MET A 243 ? 1.6484 0.4043 0.4625 0.0837 0.1276 0.0176 331 MET A C 1975 O O . MET A 243 ? 1.7966 0.4654 0.5234 0.1052 0.1341 0.0204 331 MET A O 1976 C CB . MET A 243 ? 1.6433 0.4794 0.4976 0.1522 0.0741 0.0196 331 MET A CB 1977 C CG . MET A 243 ? 1.6063 0.5161 0.5137 0.1999 0.0325 0.0147 331 MET A CG 1978 S SD . MET A 243 ? 1.6628 0.5733 0.5562 0.2626 0.0012 0.0061 331 MET A SD 1979 C CE . MET A 243 ? 1.7245 0.5417 0.4922 0.3151 -0.0058 0.0074 331 MET A CE 1980 N N . MET A 244 ? 1.7506 0.5403 0.6111 0.0215 0.1559 0.0125 332 MET A N 1981 C CA . MET A 244 ? 1.7396 0.4703 0.5554 -0.0267 0.1960 0.0067 332 MET A CA 1982 C C . MET A 244 ? 1.7254 0.4210 0.5239 -0.0267 0.1997 0.0030 332 MET A C 1983 O O . MET A 244 ? 1.9028 0.5095 0.6233 -0.0400 0.2257 0.0018 332 MET A O 1984 C CB . MET A 244 ? 1.6593 0.4563 0.5433 -0.0907 0.2214 -0.0044 332 MET A CB 1985 C CG . MET A 244 ? 1.6299 0.4151 0.4926 -0.1018 0.2352 -0.0038 332 MET A CG 1986 S SD . MET A 244 ? 1.6320 0.5230 0.5946 -0.1601 0.2524 -0.0170 332 MET A SD 1987 C CE . MET A 244 ? 1.7765 0.6316 0.7094 -0.2248 0.3000 -0.0370 332 MET A CE 1988 N N . THR A 245 ? 1.6430 0.4017 0.5103 -0.0103 0.1748 -0.0007 333 THR A N 1989 C CA . THR A 245 ? 1.6796 0.4072 0.5352 -0.0064 0.1761 -0.0076 333 THR A CA 1990 C C . THR A 245 ? 1.8188 0.4646 0.5893 0.0563 0.1590 0.0008 333 THR A C 1991 O O . THR A 245 ? 1.9227 0.5159 0.6586 0.0611 0.1657 -0.0039 333 THR A O 1992 C CB . THR A 245 ? 1.5608 0.3794 0.5139 -0.0062 0.1561 -0.0204 333 THR A CB 1993 O OG1 . THR A 245 ? 1.4831 0.3905 0.5139 -0.0285 0.1514 -0.0228 333 THR A OG1 1994 C CG2 . THR A 245 ? 1.7772 0.5917 0.7454 -0.0512 0.1784 -0.0373 333 THR A CG2 1995 N N . LEU A 246 ? 1.8097 0.4465 0.5453 0.1059 0.1363 0.0105 334 LEU A N 1996 C CA . LEU A 246 ? 1.9035 0.4853 0.5681 0.1762 0.1116 0.0146 334 LEU A CA 1997 C C . LEU A 246 ? 2.1108 0.5960 0.6611 0.1989 0.1213 0.0236 334 LEU A C 1998 O O . LEU A 246 ? 2.1647 0.5974 0.6431 0.2603 0.1016 0.0257 334 LEU A O 1999 C CB . LEU A 246 ? 1.9060 0.5788 0.6347 0.2304 0.0667 0.0099 334 LEU A CB 2000 C CG . LEU A 246 ? 1.8763 0.6325 0.6957 0.2445 0.0452 -0.0040 334 LEU A CG 2001 C CD1 . LEU A 246 ? 1.8279 0.5942 0.6933 0.1862 0.0717 -0.0122 334 LEU A CD1 2002 C CD2 . LEU A 246 ? 1.7352 0.5977 0.6411 0.2581 0.0194 -0.0105 334 LEU A CD2 2003 N N . CYS A 247 ? 2.1793 0.6438 0.7128 0.1530 0.1508 0.0259 335 CYS A N 2004 C CA . CYS A 247 ? 2.2620 0.6416 0.6949 0.1760 0.1592 0.0313 335 CYS A CA 2005 C C . CYS A 247 ? 2.2726 0.5693 0.6458 0.1170 0.2099 0.0307 335 CYS A C 2006 O O . CYS A 247 ? 2.2171 0.5535 0.6492 0.0524 0.2361 0.0233 335 CYS A O 2007 C CB . CYS A 247 ? 2.1894 0.6342 0.6642 0.1904 0.1392 0.0307 335 CYS A CB 2008 S SG . CYS A 247 ? 2.1854 0.7404 0.7384 0.2538 0.0815 0.0258 335 CYS A SG 2009 N N . ASP A 248 ? 2.4881 0.6717 0.7440 0.1397 0.2242 0.0359 336 ASP A N 2010 C CA . ASP A 248 ? 2.5870 0.6911 0.7839 0.0834 0.2743 0.0334 336 ASP A CA 2011 C C . ASP A 248 ? 2.5294 0.6861 0.7721 0.0551 0.2816 0.0300 336 ASP A C 2012 O O . ASP A 248 ? 2.4426 0.6145 0.7153 -0.0116 0.3173 0.0210 336 ASP A O 2013 C CB . ASP A 248 ? 2.7428 0.6936 0.7886 0.1183 0.2902 0.0410 336 ASP A CB 2014 C CG . ASP A 248 ? 3.0788 0.9693 1.0746 0.1460 0.2853 0.0442 336 ASP A CG 2015 O OD1 . ASP A 248 ? 2.9744 0.9371 1.0550 0.1248 0.2775 0.0388 336 ASP A OD1 2016 O OD2 . ASP A 248 ? 3.2538 1.0219 1.1242 0.1906 0.2894 0.0516 336 ASP A OD2 2017 N N . GLN A 249 ? 2.5386 0.7300 0.7922 0.1068 0.2464 0.0349 337 GLN A N 2018 C CA . GLN A 249 ? 2.4480 0.6713 0.7290 0.0910 0.2508 0.0341 337 GLN A CA 2019 C C . GLN A 249 ? 2.2952 0.6375 0.6757 0.1196 0.2078 0.0336 337 GLN A C 2020 O O . GLN A 249 ? 2.2205 0.5751 0.5906 0.1839 0.1689 0.0356 337 GLN A O 2021 C CB . GLN A 249 ? 2.6110 0.7198 0.7711 0.1279 0.2581 0.0416 337 GLN A CB 2022 C CG . GLN A 249 ? 2.6479 0.7305 0.7939 0.0814 0.2929 0.0411 337 GLN A CG 2023 C CD . GLN A 249 ? 2.9158 0.8885 0.9433 0.1254 0.2954 0.0511 337 GLN A CD 2024 O OE1 . GLN A 249 ? 2.7042 0.7094 0.7482 0.1517 0.2750 0.0557 337 GLN A OE1 2025 N NE2 . GLN A 249 ? 3.1593 0.9980 1.0624 0.1350 0.3206 0.0553 337 GLN A NE2 2026 N N . VAL A 250 ? 2.0956 0.5277 0.5723 0.0728 0.2150 0.0290 338 VAL A N 2027 C CA . VAL A 250 ? 1.9649 0.4972 0.5260 0.0970 0.1789 0.0296 338 VAL A CA 2028 C C . VAL A 250 ? 2.0230 0.5698 0.5951 0.0872 0.1840 0.0323 338 VAL A C 2029 O O . VAL A 250 ? 1.9333 0.4942 0.5317 0.0323 0.2153 0.0294 338 VAL A O 2030 C CB . VAL A 250 ? 1.9858 0.6258 0.6592 0.0697 0.1693 0.0249 338 VAL A CB 2031 C CG1 . VAL A 250 ? 2.0865 0.7095 0.7471 0.0814 0.1638 0.0241 338 VAL A CG1 2032 C CG2 . VAL A 250 ? 1.8997 0.5856 0.6337 -0.0009 0.2024 0.0185 338 VAL A CG2 2033 N N . ASP A 251 ? 2.1122 0.6590 0.6630 0.1436 0.1518 0.0366 339 ASP A N 2034 C CA . ASP A 251 ? 2.1138 0.6828 0.6776 0.1417 0.1503 0.0411 339 ASP A CA 2035 C C . ASP A 251 ? 1.9638 0.6498 0.6319 0.1481 0.1195 0.0386 339 ASP A C 2036 O O . ASP A 251 ? 1.9185 0.6396 0.6058 0.1934 0.0834 0.0348 339 ASP A O 2037 C CB . ASP A 251 ? 2.0735 0.5699 0.5439 0.2012 0.1337 0.0466 339 ASP A CB 2038 C CG . ASP A 251 ? 2.2426 0.6089 0.5958 0.1965 0.1671 0.0509 339 ASP A CG 2039 O OD1 . ASP A 251 ? 2.2604 0.6006 0.6117 0.1345 0.2092 0.0498 339 ASP A OD1 2040 O OD2 . ASP A 251 ? 2.3630 0.6552 0.6258 0.2547 0.1519 0.0537 339 ASP A OD2 2041 N N . ILE A 252 ? 1.8163 0.5646 0.5506 0.1025 0.1349 0.0392 340 ILE A N 2042 C CA . ILE A 252 ? 1.6812 0.5349 0.5076 0.1035 0.1110 0.0373 340 ILE A CA 2043 C C . ILE A 252 ? 1.6666 0.5560 0.5045 0.1064 0.1056 0.0400 340 ILE A C 2044 O O . ILE A 252 ? 1.7715 0.6497 0.6014 0.0709 0.1354 0.0421 340 ILE A O 2045 C CB . ILE A 252 ? 1.5944 0.5085 0.4991 0.0529 0.1288 0.0329 340 ILE A CB 2046 C CG1 . ILE A 252 ? 1.6502 0.5844 0.5810 -0.0019 0.1648 0.0308 340 ILE A CG1 2047 C CG2 . ILE A 252 ? 1.5290 0.3955 0.4056 0.0436 0.1414 0.0290 340 ILE A CG2 2048 C CD1 . ILE A 252 ? 1.3956 0.4283 0.4193 -0.0293 0.1657 0.0272 340 ILE A CD1 2049 N N . TYR A 253 ? 1.5703 0.5106 0.4286 0.1490 0.0668 0.0366 341 TYR A N 2050 C CA . TYR A 253 ? 1.6121 0.5823 0.4658 0.1646 0.0537 0.0345 341 TYR A CA 2051 C C . TYR A 253 ? 1.5348 0.6063 0.4712 0.1449 0.0456 0.0243 341 TYR A C 2052 O O . TYR A 253 ? 1.4646 0.5944 0.4572 0.1474 0.0281 0.0159 341 TYR A O 2053 C CB . TYR A 253 ? 1.7149 0.6725 0.5242 0.2305 0.0140 0.0294 341 TYR A CB 2054 C CG . TYR A 253 ? 1.8615 0.7083 0.5739 0.2565 0.0240 0.0373 341 TYR A CG 2055 C CD1 . TYR A 253 ? 1.8959 0.6990 0.5867 0.2701 0.0240 0.0361 341 TYR A CD1 2056 C CD2 . TYR A 253 ? 1.9082 0.6902 0.5430 0.2676 0.0356 0.0444 341 TYR A CD2 2057 C CE1 . TYR A 253 ? 1.9908 0.6861 0.5819 0.2940 0.0360 0.0400 341 TYR A CE1 2058 C CE2 . TYR A 253 ? 1.9733 0.6453 0.5083 0.2920 0.0473 0.0507 341 TYR A CE2 2059 C CZ . TYR A 253 ? 2.1386 0.7653 0.6497 0.3053 0.0480 0.0478 341 TYR A CZ 2060 O OH . TYR A 253 ? 2.1641 0.6748 0.5650 0.3302 0.0620 0.0524 341 TYR A OH 2061 N N . GLU A 254 ? 1.5425 0.6304 0.4804 0.1257 0.0608 0.0223 342 GLU A N 2062 C CA . GLU A 254 ? 1.4249 0.5952 0.4296 0.1055 0.0607 0.0083 342 GLU A CA 2063 C C . GLU A 254 ? 1.3034 0.5227 0.3793 0.0738 0.0723 0.0047 342 GLU A C 2064 O O . GLU A 254 ? 1.2078 0.4938 0.3428 0.0725 0.0595 -0.0119 342 GLU A O 2065 C CB . GLU A 254 ? 1.4139 0.6364 0.4311 0.1423 0.0210 -0.0118 342 GLU A CB 2066 C CG . GLU A 254 ? 1.5852 0.7704 0.5333 0.1762 0.0078 -0.0102 342 GLU A CG 2067 C CD . GLU A 254 ? 1.5437 0.7172 0.4687 0.1538 0.0346 -0.0088 342 GLU A CD 2068 O OE1 . GLU A 254 ? 1.4913 0.6988 0.4626 0.1164 0.0596 -0.0141 342 GLU A OE1 2069 O OE2 . GLU A 254 ? 1.5823 0.7133 0.4407 0.1770 0.0308 -0.0038 342 GLU A OE2 2070 N N . PHE A 255 ? 1.2596 0.4466 0.3344 0.0467 0.0973 0.0166 343 PHE A N 2071 C CA . PHE A 255 ? 1.1996 0.4384 0.3417 0.0114 0.1147 0.0139 343 PHE A CA 2072 C C . PHE A 255 ? 1.2414 0.4994 0.3995 -0.0220 0.1475 0.0109 343 PHE A C 2073 O O . PHE A 255 ? 1.1994 0.5156 0.4035 -0.0262 0.1487 -0.0003 343 PHE A O 2074 C CB . PHE A 255 ? 1.1612 0.3653 0.2985 -0.0042 0.1260 0.0220 343 PHE A CB 2075 C CG . PHE A 255 ? 1.1666 0.4337 0.3794 -0.0325 0.1350 0.0183 343 PHE A CG 2076 C CD1 . PHE A 255 ? 1.0984 0.4396 0.3925 -0.0162 0.1071 0.0097 343 PHE A CD1 2077 C CD2 . PHE A 255 ? 1.1078 0.3796 0.3391 -0.0747 0.1666 0.0171 343 PHE A CD2 2078 C CE1 . PHE A 255 ? 1.1310 0.5359 0.5045 -0.0373 0.1118 0.0065 343 PHE A CE1 2079 C CE2 . PHE A 255 ? 1.1531 0.4944 0.4604 -0.0960 0.1704 0.0115 343 PHE A CE2 2080 C CZ . PHE A 255 ? 1.0603 0.4669 0.4395 -0.0739 0.1409 0.0076 343 PHE A CZ 2081 N N . LEU A 256 ? 1.2430 0.4519 0.3643 -0.0435 0.1737 0.0167 344 LEU A N 2082 C CA . LEU A 256 ? 1.3480 0.5700 0.4688 -0.0663 0.2012 0.0118 344 LEU A CA 2083 C C . LEU A 256 ? 1.2664 0.4702 0.3422 -0.0320 0.1823 0.0114 344 LEU A C 2084 O O . LEU A 256 ? 1.3425 0.4847 0.3542 -0.0026 0.1652 0.0195 344 LEU A O 2085 C CB . LEU A 256 ? 1.3352 0.5038 0.4179 -0.0977 0.2334 0.0141 344 LEU A CB 2086 C CG . LEU A 256 ? 1.3331 0.5115 0.4492 -0.1325 0.2503 0.0090 344 LEU A CG 2087 C CD1 . LEU A 256 ? 1.4276 0.5695 0.5133 -0.1719 0.2875 0.0025 344 LEU A CD1 2088 C CD2 . LEU A 256 ? 1.2740 0.5523 0.4819 -0.1483 0.2504 -0.0002 344 LEU A CD2 2089 N N . PRO A 257 ? 1.2637 0.5231 0.3730 -0.0321 0.1839 -0.0010 345 PRO A N 2090 C CA . PRO A 257 ? 1.4548 0.7112 0.5320 0.0004 0.1613 -0.0085 345 PRO A CA 2091 C C . PRO A 257 ? 1.4818 0.6864 0.4904 0.0014 0.1767 -0.0014 345 PRO A C 2092 O O . PRO A 257 ? 1.4315 0.6252 0.4358 -0.0315 0.2125 0.0020 345 PRO A O 2093 C CB . PRO A 257 ? 1.4124 0.7377 0.5497 -0.0066 0.1661 -0.0285 345 PRO A CB 2094 C CG . PRO A 257 ? 1.3113 0.6706 0.4970 -0.0426 0.2001 -0.0279 345 PRO A CG 2095 C CD . PRO A 257 ? 1.2073 0.5390 0.3897 -0.0575 0.2035 -0.0129 345 PRO A CD 2096 N N . SER A 258 ? 1.4010 0.5785 0.3571 0.0392 0.1490 -0.0015 346 SER A N 2097 C CA . SER A 258 ? 1.4995 0.6289 0.3838 0.0465 0.1602 0.0044 346 SER A CA 2098 C C . SER A 258 ? 1.4852 0.6664 0.3890 0.0440 0.1648 -0.0138 346 SER A C 2099 O O . SER A 258 ? 1.3940 0.6379 0.3667 0.0295 0.1694 -0.0295 346 SER A O 2100 C CB . SER A 258 ? 1.6328 0.7128 0.4493 0.0946 0.1257 0.0110 346 SER A CB 2101 O OG . SER A 258 ? 1.5312 0.6691 0.3761 0.1275 0.0841 -0.0077 346 SER A OG 2102 N N . LYS A 259 ? 1.5627 0.7132 0.4013 0.0616 0.1632 -0.0130 347 LYS A N 2103 C CA . LYS A 259 ? 1.6134 0.8067 0.4594 0.0633 0.1661 -0.0327 347 LYS A CA 2104 C C . LYS A 259 ? 1.5606 0.8063 0.4434 0.0909 0.1250 -0.0567 347 LYS A C 2105 O O . LYS A 259 ? 1.5631 0.8514 0.4698 0.0907 0.1240 -0.0804 347 LYS A O 2106 C CB . LYS A 259 ? 1.6751 0.8179 0.4335 0.0760 0.1743 -0.0250 347 LYS A CB 2107 C CG . LYS A 259 ? 1.7548 0.8443 0.4429 0.1190 0.1407 -0.0137 347 LYS A CG 2108 C CD . LYS A 259 ? 1.9029 0.9625 0.5100 0.1407 0.1395 -0.0141 347 LYS A CD 2109 C CE . LYS A 259 ? 2.0312 1.0207 0.5560 0.1845 0.1142 0.0022 347 LYS A CE 2110 N NZ . LYS A 259 ? 1.9204 0.9301 0.4840 0.2109 0.0759 -0.0009 347 LYS A NZ 2111 N N . ARG A 260 ? 1.5466 0.7904 0.4368 0.1133 0.0918 -0.0541 348 ARG A N 2112 C CA . ARG A 260 ? 1.5625 0.8642 0.4979 0.1337 0.0530 -0.0819 348 ARG A CA 2113 C C . ARG A 260 ? 1.4623 0.8108 0.4837 0.1108 0.0579 -0.0956 348 ARG A C 2114 O O . ARG A 260 ? 1.3456 0.7380 0.4124 0.1206 0.0294 -0.1203 348 ARG A O 2115 C CB . ARG A 260 ? 1.4652 0.7571 0.3740 0.1720 0.0132 -0.0788 348 ARG A CB 2116 C CG . ARG A 260 ? 1.5763 0.8249 0.3996 0.2042 0.0024 -0.0700 348 ARG A CG 2117 C CD . ARG A 260 ? 1.6114 0.8531 0.4124 0.2483 -0.0365 -0.0680 348 ARG A CD 2118 N NE . ARG A 260 ? 1.7778 0.9715 0.5751 0.2449 -0.0258 -0.0435 348 ARG A NE 2119 C CZ . ARG A 260 ? 1.8395 0.9423 0.5657 0.2473 -0.0029 -0.0153 348 ARG A CZ 2120 N NH1 . ARG A 260 ? 1.7757 0.8376 0.5039 0.2415 0.0066 0.0005 348 ARG A NH1 2121 N NH2 . ARG A 260 ? 2.0049 1.0548 0.6555 0.2541 0.0119 -0.0056 348 ARG A NH2 2122 N N . LYS A 261 ? 1.2988 0.6392 0.3430 0.0796 0.0949 -0.0819 349 LYS A N 2123 C CA . LYS A 261 ? 1.2961 0.6763 0.4160 0.0594 0.1057 -0.0932 349 LYS A CA 2124 C C . LYS A 261 ? 1.2827 0.7025 0.4449 0.0676 0.0877 -0.1266 349 LYS A C 2125 O O . LYS A 261 ? 1.3084 0.7344 0.4554 0.0714 0.0920 -0.1421 349 LYS A O 2126 C CB . LYS A 261 ? 1.2775 0.6639 0.4144 0.0300 0.1499 -0.0861 349 LYS A CB 2127 C CG . LYS A 261 ? 1.4296 0.8551 0.6426 0.0138 0.1619 -0.0919 349 LYS A CG 2128 C CD . LYS A 261 ? 1.4003 0.8449 0.6321 -0.0128 0.2033 -0.0856 349 LYS A CD 2129 C CE . LYS A 261 ? 1.4605 0.9643 0.7906 -0.0211 0.2053 -0.0871 349 LYS A CE 2130 N NZ . LYS A 261 ? 1.5557 1.0856 0.9006 -0.0476 0.2411 -0.0815 349 LYS A NZ 2131 N N . THR A 262 ? 1.1218 0.5701 0.3437 0.0677 0.0676 -0.1381 350 THR A N 2132 C CA . THR A 262 ? 1.2587 0.7421 0.5305 0.0688 0.0518 -0.1702 350 THR A CA 2133 C C . THR A 262 ? 1.1594 0.6775 0.5275 0.0520 0.0524 -0.1705 350 THR A C 2134 O O . THR A 262 ? 1.0980 0.6230 0.4943 0.0458 0.0533 -0.1490 350 THR A O 2135 C CB . THR A 262 ? 1.1403 0.6337 0.3782 0.0921 0.0125 -0.1948 350 THR A CB 2136 O OG1 . THR A 262 ? 1.1824 0.7153 0.4843 0.0828 -0.0009 -0.2294 350 THR A OG1 2137 C CG2 . THR A 262 ? 1.1339 0.6307 0.3640 0.1075 -0.0119 -0.1811 350 THR A CG2 2138 N N . ASP A 263 ? 1.1138 0.6467 0.5262 0.0446 0.0539 -0.1949 351 ASP A N 2139 C CA . ASP A 263 ? 1.0023 0.5547 0.4931 0.0295 0.0565 -0.1934 351 ASP A CA 2140 C C . ASP A 263 ? 1.0090 0.5890 0.5291 0.0272 0.0288 -0.2024 351 ASP A C 2141 O O . ASP A 263 ? 0.9725 0.5669 0.5444 0.0156 0.0320 -0.1896 351 ASP A O 2142 C CB . ASP A 263 ? 1.0118 0.5551 0.5320 0.0223 0.0701 -0.2156 351 ASP A CB 2143 C CG . ASP A 263 ? 1.0626 0.5922 0.5790 0.0268 0.1009 -0.2027 351 ASP A CG 2144 O OD1 . ASP A 263 ? 1.0991 0.6355 0.6026 0.0284 0.1136 -0.1773 351 ASP A OD1 2145 O OD2 . ASP A 263 ? 1.1024 0.6167 0.6305 0.0286 0.1133 -0.2209 351 ASP A OD2 2146 N N . VAL A 264 ? 1.0519 0.6453 0.5385 0.0404 0.0013 -0.2260 352 VAL A N 2147 C CA . VAL A 264 ? 1.0668 0.7020 0.5838 0.0424 -0.0270 -0.2399 352 VAL A CA 2148 C C . VAL A 264 ? 0.9896 0.6269 0.5194 0.0453 -0.0254 -0.2072 352 VAL A C 2149 O O . VAL A 264 ? 1.0924 0.7042 0.5665 0.0639 -0.0275 -0.1848 352 VAL A O 2150 C CB . VAL A 264 ? 1.1770 0.8310 0.6411 0.0697 -0.0609 -0.2634 352 VAL A CB 2151 C CG1 . VAL A 264 ? 0.9742 0.6910 0.4875 0.0709 -0.0898 -0.2876 352 VAL A CG1 2152 C CG2 . VAL A 264 ? 1.0502 0.6979 0.4834 0.0706 -0.0630 -0.2956 352 VAL A CG2 2153 N N . CYS A 265 ? 0.9248 0.5860 0.5228 0.0254 -0.0192 -0.2052 353 CYS A N 2154 C CA . CYS A 265 ? 0.8114 0.4737 0.4268 0.0243 -0.0125 -0.1747 353 CYS A CA 2155 C C . CYS A 265 ? 0.8930 0.5682 0.4782 0.0486 -0.0375 -0.1714 353 CYS A C 2156 O O . CYS A 265 ? 0.9118 0.5579 0.4637 0.0576 -0.0308 -0.1433 353 CYS A O 2157 C CB . CYS A 265 ? 0.7669 0.4514 0.4541 -0.0005 -0.0011 -0.1756 353 CYS A CB 2158 S SG . CYS A 265 ? 1.0599 0.7553 0.7678 -0.0003 0.0032 -0.1439 353 CYS A SG 2159 N N . TYR A 266 ? 0.9037 0.6232 0.5003 0.0600 -0.0658 -0.2027 354 TYR A N 2160 C CA . TYR A 266 ? 0.9597 0.6972 0.5291 0.0923 -0.0933 -0.2036 354 TYR A CA 2161 C C . TYR A 266 ? 1.0559 0.8103 0.5756 0.1250 -0.1259 -0.2324 354 TYR A C 2162 O O . TYR A 266 ? 1.0469 0.8249 0.5800 0.1143 -0.1311 -0.2633 354 TYR A O 2163 C CB . TYR A 266 ? 0.9033 0.7035 0.5452 0.0828 -0.1015 -0.2177 354 TYR A CB 2164 C CG . TYR A 266 ? 0.9359 0.7258 0.6197 0.0581 -0.0750 -0.1902 354 TYR A CG 2165 C CD1 . TYR A 266 ? 0.9746 0.7191 0.6220 0.0671 -0.0638 -0.1548 354 TYR A CD1 2166 C CD2 . TYR A 266 ? 0.9685 0.7926 0.7238 0.0247 -0.0605 -0.2013 354 TYR A CD2 2167 C CE1 . TYR A 266 ? 0.9807 0.7244 0.6661 0.0463 -0.0427 -0.1333 354 TYR A CE1 2168 C CE2 . TYR A 266 ? 0.9473 0.7615 0.7324 0.0067 -0.0380 -0.1753 354 TYR A CE2 2169 C CZ . TYR A 266 ? 1.0057 0.7853 0.7576 0.0194 -0.0315 -0.1426 354 TYR A CZ 2170 O OH . TYR A 266 ? 1.0892 0.8664 0.8693 0.0033 -0.0120 -0.1202 354 TYR A OH 2171 N N . TYR A 267 ? 1.0891 0.8291 0.5473 0.1675 -0.1488 -0.2240 355 TYR A N 2172 C CA . TYR A 267 ? 1.1151 0.8722 0.5160 0.2086 -0.1843 -0.2501 355 TYR A CA 2173 C C . TYR A 267 ? 1.0704 0.9332 0.5412 0.2136 -0.2162 -0.2992 355 TYR A C 2174 O O . TYR A 267 ? 1.1787 1.0856 0.6488 0.2294 -0.2377 -0.3229 355 TYR A O 2175 C CB . TYR A 267 ? 1.2167 0.9185 0.5324 0.2552 -0.1947 -0.2183 355 TYR A CB 2176 C CG . TYR A 267 ? 1.1837 0.9092 0.5161 0.2825 -0.2123 -0.2159 355 TYR A CG 2177 C CD1 . TYR A 267 ? 1.1427 0.9442 0.5018 0.3208 -0.2488 -0.2434 355 TYR A CD1 2178 C CD2 . TYR A 267 ? 1.1368 0.8118 0.4604 0.2714 -0.1907 -0.1867 355 TYR A CD2 2179 C CE1 . TYR A 267 ? 1.1220 0.9471 0.4966 0.3504 -0.2634 -0.2433 355 TYR A CE1 2180 C CE2 . TYR A 267 ? 1.1565 0.8495 0.4920 0.2978 -0.2052 -0.1856 355 TYR A CE2 2181 C CZ . TYR A 267 ? 1.2291 0.9960 0.5874 0.3396 -0.2422 -0.2146 355 TYR A CZ 2182 O OH . TYR A 267 ? 1.2570 1.0451 0.6285 0.3697 -0.2557 -0.2163 355 TYR A OH 2183 N N . TYR A 268 ? 1.0644 0.9763 0.6171 0.1919 -0.2095 -0.3040 356 TYR A N 2184 C CA . TYR A 268 ? 1.0042 1.0255 0.6306 0.1911 -0.2346 -0.3531 356 TYR A CA 2185 C C . TYR A 268 ? 0.9846 1.0468 0.7006 0.1295 -0.2109 -0.3794 356 TYR A C 2186 O O . TYR A 268 ? 0.9808 1.1359 0.7655 0.1144 -0.2240 -0.4257 356 TYR A O 2187 C CB . TYR A 268 ? 0.9984 1.0550 0.6497 0.2142 -0.2449 -0.3470 356 TYR A CB 2188 C CG . TYR A 268 ? 1.0406 1.0516 0.7185 0.1841 -0.2086 -0.3066 356 TYR A CG 2189 C CD1 . TYR A 268 ? 1.0709 0.9861 0.6788 0.1981 -0.1932 -0.2586 356 TYR A CD1 2190 C CD2 . TYR A 268 ? 0.9771 1.0430 0.7465 0.1415 -0.1895 -0.3190 356 TYR A CD2 2191 C CE1 . TYR A 268 ? 1.0376 0.9218 0.6709 0.1717 -0.1635 -0.2273 356 TYR A CE1 2192 C CE2 . TYR A 268 ? 1.0058 1.0334 0.7926 0.1190 -0.1595 -0.2834 356 TYR A CE2 2193 C CZ . TYR A 268 ? 1.0469 0.9887 0.7681 0.1353 -0.1488 -0.2391 356 TYR A CZ 2194 O OH . TYR A 268 ? 1.0364 0.9503 0.7771 0.1130 -0.1216 -0.2086 356 TYR A OH 2195 N N . GLN A 269 ? 1.0184 1.0099 0.7311 0.0944 -0.1745 -0.3512 357 GLN A N 2196 C CA . GLN A 269 ? 1.0278 1.0299 0.8053 0.0403 -0.1484 -0.3707 357 GLN A CA 2197 C C . GLN A 269 ? 1.0887 1.0486 0.8270 0.0338 -0.1434 -0.3816 357 GLN A C 2198 O O . GLN A 269 ? 1.1050 1.0189 0.7667 0.0662 -0.1518 -0.3633 357 GLN A O 2199 C CB . GLN A 269 ? 1.1168 1.0724 0.9234 0.0105 -0.1103 -0.3306 357 GLN A CB 2200 C CG . GLN A 269 ? 1.1189 1.1236 1.0079 -0.0310 -0.0937 -0.3495 357 GLN A CG 2201 C CD . GLN A 269 ? 1.1116 1.1458 1.0248 -0.0214 -0.0938 -0.3307 357 GLN A CD 2202 O OE1 . GLN A 269 ? 1.1502 1.2580 1.0831 -0.0008 -0.1198 -0.3568 357 GLN A OE1 2203 N NE2 . GLN A 269 ? 1.0720 1.0536 0.9835 -0.0334 -0.0660 -0.2881 357 GLN A NE2 2204 N N . LYS A 270 ? 1.0610 1.0306 0.8465 -0.0091 -0.1267 -0.4120 358 LYS A N 2205 C CA . LYS A 270 ? 1.1340 1.0698 0.8855 -0.0149 -0.1235 -0.4313 358 LYS A CA 2206 C C . LYS A 270 ? 1.1070 0.9604 0.8566 -0.0410 -0.0823 -0.4037 358 LYS A C 2207 O O . LYS A 270 ? 1.2755 1.0928 0.9954 -0.0443 -0.0750 -0.4173 358 LYS A O 2208 C CB . LYS A 270 ? 1.2707 1.2760 1.0665 -0.0394 -0.1381 -0.4921 358 LYS A CB 2209 C CG . LYS A 270 ? 1.3659 1.4559 1.1564 -0.0027 -0.1799 -0.5108 358 LYS A CG 2210 C CD . LYS A 270 ? 1.4494 1.6034 1.2860 -0.0293 -0.1870 -0.5583 358 LYS A CD 2211 C CE . LYS A 270 ? 1.4870 1.7324 1.3219 0.0125 -0.2289 -0.5804 358 LYS A CE 2212 N NZ . LYS A 270 ? 1.5130 1.8223 1.3911 -0.0136 -0.2349 -0.6301 358 LYS A NZ 2213 N N . PHE A 271 ? 1.0633 0.8892 0.8410 -0.0548 -0.0569 -0.3664 359 PHE A N 2214 C CA . PHE A 271 ? 1.0415 0.7984 0.8247 -0.0764 -0.0198 -0.3445 359 PHE A CA 2215 C C . PHE A 271 ? 0.9846 0.6882 0.7168 -0.0500 -0.0082 -0.3021 359 PHE A C 2216 O O . PHE A 271 ? 0.9356 0.6460 0.6389 -0.0250 -0.0196 -0.2765 359 PHE A O 2217 C CB . PHE A 271 ? 1.0182 0.7722 0.8559 -0.1069 0.0039 -0.3307 359 PHE A CB 2218 C CG . PHE A 271 ? 0.9637 0.7193 0.8020 -0.0906 0.0066 -0.2862 359 PHE A CG 2219 C CD1 . PHE A 271 ? 0.9989 0.7008 0.8172 -0.0812 0.0280 -0.2442 359 PHE A CD1 2220 C CD2 . PHE A 271 ? 0.8967 0.7124 0.7586 -0.0846 -0.0119 -0.2903 359 PHE A CD2 2221 C CE1 . PHE A 271 ? 0.9012 0.6088 0.7213 -0.0697 0.0301 -0.2084 359 PHE A CE1 2222 C CE2 . PHE A 271 ? 0.8194 0.6320 0.6798 -0.0714 -0.0079 -0.2522 359 PHE A CE2 2223 C CZ . PHE A 271 ? 0.7843 0.5423 0.6234 -0.0661 0.0130 -0.2120 359 PHE A CZ 2224 N N . PHE A 272 ? 1.0382 0.6885 0.7589 -0.0564 0.0162 -0.2976 360 PHE A N 2225 C CA . PHE A 272 ? 1.0157 0.6282 0.6942 -0.0341 0.0298 -0.2661 360 PHE A CA 2226 C C . PHE A 272 ? 0.9841 0.5754 0.6864 -0.0364 0.0531 -0.2272 360 PHE A C 2227 O O . PHE A 272 ? 1.0277 0.5989 0.7637 -0.0539 0.0696 -0.2272 360 PHE A O 2228 C CB . PHE A 272 ? 1.0406 0.6154 0.6936 -0.0331 0.0432 -0.2865 360 PHE A CB 2229 C CG . PHE A 272 ? 1.1655 0.7591 0.7855 -0.0279 0.0209 -0.3263 360 PHE A CG 2230 C CD1 . PHE A 272 ? 1.2700 0.8865 0.9189 -0.0509 0.0094 -0.3714 360 PHE A CD1 2231 C CD2 . PHE A 272 ? 1.2966 0.8844 0.8531 -0.0021 0.0139 -0.3212 360 PHE A CD2 2232 C CE1 . PHE A 272 ? 1.3457 0.9881 0.9637 -0.0441 -0.0141 -0.4129 360 PHE A CE1 2233 C CE2 . PHE A 272 ? 1.3347 0.9384 0.8513 0.0073 -0.0079 -0.3576 360 PHE A CE2 2234 C CZ . PHE A 272 ? 1.3522 0.9875 0.9012 -0.0118 -0.0244 -0.4045 360 PHE A CZ 2235 N N . ASP A 273 ? 0.9340 0.5273 0.6142 -0.0194 0.0553 -0.1956 361 ASP A N 2236 C CA . ASP A 273 ? 0.8360 0.4181 0.5343 -0.0175 0.0757 -0.1629 361 ASP A CA 2237 C C . ASP A 273 ? 0.8655 0.4517 0.5319 -0.0032 0.0813 -0.1394 361 ASP A C 2238 O O . ASP A 273 ? 0.8978 0.4975 0.5474 -0.0003 0.0697 -0.1283 361 ASP A O 2239 C CB . ASP A 273 ? 0.8496 0.4496 0.5884 -0.0298 0.0738 -0.1493 361 ASP A CB 2240 C CG . ASP A 273 ? 0.9779 0.5613 0.7360 -0.0275 0.0947 -0.1224 361 ASP A CG 2241 O OD1 . ASP A 273 ? 0.9552 0.5256 0.6986 -0.0126 0.1076 -0.1134 361 ASP A OD1 2242 O OD2 . ASP A 273 ? 1.1859 0.7734 0.9717 -0.0381 0.0982 -0.1116 361 ASP A OD2 2243 N N . SER A 274 ? 0.9930 0.5665 0.6507 0.0048 0.1012 -0.1344 362 SER A N 2244 C CA . SER A 274 ? 0.9991 0.5824 0.6317 0.0106 0.1129 -0.1181 362 SER A CA 2245 C C . SER A 274 ? 0.9818 0.5877 0.6385 0.0054 0.1142 -0.0926 362 SER A C 2246 O O . SER A 274 ? 0.9939 0.6058 0.6261 0.0015 0.1177 -0.0811 362 SER A O 2247 C CB . SER A 274 ? 1.0513 0.6319 0.6845 0.0206 0.1356 -0.1233 362 SER A CB 2248 O OG . SER A 274 ? 1.2174 0.8127 0.8231 0.0204 0.1507 -0.1166 362 SER A OG 2249 N N . ALA A 275 ? 0.9267 0.5391 0.6255 0.0037 0.1132 -0.0850 363 ALA A N 2250 C CA . ALA A 275 ? 0.8067 0.4430 0.5289 0.0004 0.1136 -0.0633 363 ALA A CA 2251 C C . ALA A 275 ? 0.8535 0.4959 0.5603 -0.0074 0.0988 -0.0581 363 ALA A C 2252 O O . ALA A 275 ? 0.8594 0.5178 0.5688 -0.0115 0.1020 -0.0434 363 ALA A O 2253 C CB . ALA A 275 ? 0.8527 0.4845 0.6108 0.0011 0.1151 -0.0563 363 ALA A CB 2254 N N . CYS A 276 ? 0.9180 0.5495 0.6074 -0.0072 0.0818 -0.0729 364 CYS A N 2255 C CA . CYS A 276 ? 0.9113 0.5447 0.5781 -0.0049 0.0658 -0.0694 364 CYS A CA 2256 C C . CYS A 276 ? 0.8943 0.5058 0.5083 -0.0026 0.0735 -0.0593 364 CYS A C 2257 O O . CYS A 276 ? 0.8550 0.4589 0.4507 -0.0027 0.0695 -0.0484 364 CYS A O 2258 C CB . CYS A 276 ? 0.8932 0.5297 0.5506 0.0021 0.0429 -0.0919 364 CYS A CB 2259 S SG . CYS A 276 ? 1.0132 0.6765 0.7335 -0.0122 0.0389 -0.1083 364 CYS A SG 2260 N N . THR A 277 ? 0.9733 0.5695 0.5584 -0.0020 0.0874 -0.0645 365 THR A N 2261 C CA . THR A 277 ? 0.7974 0.3670 0.3262 -0.0063 0.1025 -0.0559 365 THR A CA 2262 C C . THR A 277 ? 0.9354 0.5294 0.4911 -0.0229 0.1278 -0.0456 365 THR A C 2263 O O . THR A 277 ? 0.9552 0.5368 0.4850 -0.0365 0.1397 -0.0358 365 THR A O 2264 C CB . THR A 277 ? 0.9471 0.4918 0.4251 0.0010 0.1079 -0.0687 365 THR A CB 2265 O OG1 . THR A 277 ? 0.9390 0.4741 0.3970 0.0180 0.0805 -0.0835 365 THR A OG1 2266 C CG2 . THR A 277 ? 0.9312 0.4360 0.3369 -0.0062 0.1270 -0.0578 365 THR A CG2 2267 N N . MET A 278 ? 0.9190 0.5478 0.5254 -0.0207 0.1356 -0.0499 366 MET A N 2268 C CA . MET A 278 ? 0.8547 0.5224 0.4893 -0.0295 0.1572 -0.0467 366 MET A CA 2269 C C . MET A 278 ? 0.8401 0.5450 0.5250 -0.0302 0.1513 -0.0363 366 MET A C 2270 O O . MET A 278 ? 0.8239 0.5681 0.5283 -0.0400 0.1643 -0.0350 366 MET A O 2271 C CB . MET A 278 ? 0.7947 0.4795 0.4447 -0.0174 0.1704 -0.0597 366 MET A CB 2272 C CG . MET A 278 ? 1.0264 0.6778 0.6242 -0.0161 0.1774 -0.0721 366 MET A CG 2273 S SD . MET A 278 ? 1.0848 0.7181 0.6207 -0.0399 0.2013 -0.0680 366 MET A SD 2274 C CE . MET A 278 ? 1.2164 0.9176 0.7955 -0.0480 0.2335 -0.0794 366 MET A CE 2275 N N . GLY A 279 ? 0.7886 0.4855 0.4932 -0.0216 0.1328 -0.0315 367 GLY A N 2276 C CA . GLY A 279 ? 0.8502 0.5760 0.5919 -0.0212 0.1275 -0.0201 367 GLY A CA 2277 C C . GLY A 279 ? 0.8537 0.5897 0.6292 -0.0042 0.1277 -0.0173 367 GLY A C 2278 O O . GLY A 279 ? 0.8925 0.6303 0.6717 0.0085 0.1376 -0.0243 367 GLY A O 2279 N N . ALA A 280 ? 0.6858 0.4217 0.4796 -0.0026 0.1186 -0.0071 368 ALA A N 2280 C CA . ALA A 280 ? 0.7135 0.4467 0.5275 0.0135 0.1217 0.0015 368 ALA A CA 2281 C C . ALA A 280 ? 0.6820 0.4413 0.5104 0.0131 0.1167 0.0168 368 ALA A C 2282 O O . ALA A 280 ? 0.7586 0.5575 0.5978 0.0233 0.1189 0.0221 368 ALA A O 2283 C CB . ALA A 280 ? 0.7308 0.4189 0.5416 0.0110 0.1204 -0.0046 368 ALA A CB 2284 N N . TYR A 281 ? 0.7025 0.4482 0.5316 0.0010 0.1094 0.0200 369 TYR A N 2285 C CA . TYR A 281 ? 0.6232 0.3937 0.4606 -0.0023 0.1048 0.0315 369 TYR A CA 2286 C C . TYR A 281 ? 0.6863 0.4886 0.5190 -0.0116 0.1013 0.0274 369 TYR A C 2287 O O . TYR A 281 ? 0.7467 0.5863 0.5888 -0.0074 0.1019 0.0327 369 TYR A O 2288 C CB . TYR A 281 ? 0.6152 0.3691 0.4565 -0.0144 0.1006 0.0308 369 TYR A CB 2289 C CG . TYR A 281 ? 0.6251 0.4044 0.4719 -0.0189 0.0967 0.0393 369 TYR A CG 2290 C CD1 . TYR A 281 ? 0.6062 0.4003 0.4471 -0.0270 0.0874 0.0315 369 TYR A CD1 2291 C CD2 . TYR A 281 ? 0.7062 0.4865 0.5559 -0.0134 0.1036 0.0550 369 TYR A CD2 2292 C CE1 . TYR A 281 ? 0.7007 0.5159 0.5447 -0.0300 0.0843 0.0356 369 TYR A CE1 2293 C CE2 . TYR A 281 ? 0.5962 0.4019 0.4474 -0.0177 0.1008 0.0606 369 TYR A CE2 2294 C CZ . TYR A 281 ? 0.6251 0.4508 0.4765 -0.0263 0.0907 0.0489 369 TYR A CZ 2295 O OH . TYR A 281 ? 0.7063 0.5554 0.5573 -0.0292 0.0880 0.0506 369 TYR A OH 2296 N N . HIS A 282 ? 0.6160 0.4010 0.4293 -0.0238 0.0983 0.0171 370 HIS A N 2297 C CA . HIS A 282 ? 0.5468 0.3444 0.3460 -0.0368 0.1000 0.0136 370 HIS A CA 2298 C C . HIS A 282 ? 0.6583 0.4759 0.4557 -0.0420 0.1135 0.0068 370 HIS A C 2299 O O . HIS A 282 ? 0.7681 0.5790 0.5650 -0.0339 0.1197 0.0026 370 HIS A O 2300 C CB . HIS A 282 ? 0.6085 0.3679 0.3744 -0.0438 0.0931 0.0079 370 HIS A CB 2301 C CG . HIS A 282 ? 0.7210 0.4751 0.4941 -0.0376 0.0796 0.0085 370 HIS A CG 2302 N ND1 . HIS A 282 ? 0.7393 0.5120 0.5227 -0.0397 0.0761 0.0123 370 HIS A ND1 2303 C CD2 . HIS A 282 ? 0.7167 0.4574 0.4907 -0.0306 0.0697 0.0012 370 HIS A CD2 2304 C CE1 . HIS A 282 ? 0.6841 0.4556 0.4754 -0.0338 0.0663 0.0084 370 HIS A CE1 2305 N NE2 . HIS A 282 ? 0.7433 0.4994 0.5321 -0.0293 0.0619 0.0004 370 HIS A NE2 2306 N N . PRO A 283 ? 0.6360 0.4813 0.4333 -0.0582 0.1199 0.0017 371 PRO A N 2307 C CA . PRO A 283 ? 0.6877 0.5584 0.4844 -0.0723 0.1372 -0.0106 371 PRO A CA 2308 C C . PRO A 283 ? 0.7387 0.5530 0.4869 -0.0899 0.1485 -0.0152 371 PRO A C 2309 O O . PRO A 283 ? 0.7492 0.5598 0.4768 -0.1167 0.1657 -0.0239 371 PRO A O 2310 C CB . PRO A 283 ? 0.5965 0.5155 0.4098 -0.0893 0.1398 -0.0182 371 PRO A CB 2311 C CG . PRO A 283 ? 0.6605 0.5434 0.4557 -0.0922 0.1279 -0.0105 371 PRO A CG 2312 C CD . PRO A 283 ? 0.6356 0.4988 0.4384 -0.0660 0.1135 0.0035 371 PRO A CD 2313 N N . LEU A 284 ? 0.8221 0.5904 0.5483 -0.0752 0.1398 -0.0103 372 LEU A N 2314 C CA . LEU A 284 ? 0.8982 0.6064 0.5682 -0.0808 0.1441 -0.0117 372 LEU A CA 2315 C C . LEU A 284 ? 0.7916 0.5002 0.4397 -0.0993 0.1700 -0.0202 372 LEU A C 2316 O O . LEU A 284 ? 0.9045 0.5625 0.4965 -0.1161 0.1833 -0.0200 372 LEU A O 2317 C CB . LEU A 284 ? 0.9091 0.5937 0.5736 -0.0586 0.1287 -0.0116 372 LEU A CB 2318 C CG . LEU A 284 ? 0.8892 0.5151 0.4939 -0.0524 0.1211 -0.0127 372 LEU A CG 2319 C CD1 . LEU A 284 ? 0.7978 0.3962 0.3783 -0.0518 0.1105 -0.0070 372 LEU A CD1 2320 C CD2 . LEU A 284 ? 0.8817 0.5059 0.4963 -0.0331 0.1036 -0.0197 372 LEU A CD2 2321 N N . LEU A 285 ? 0.7447 0.5092 0.4337 -0.0952 0.1794 -0.0281 373 LEU A N 2322 C CA . LEU A 285 ? 0.8237 0.6036 0.5010 -0.1120 0.2064 -0.0405 373 LEU A CA 2323 C C . LEU A 285 ? 0.9038 0.6964 0.5719 -0.1498 0.2279 -0.0482 373 LEU A C 2324 O O . LEU A 285 ? 0.9891 0.7472 0.6109 -0.1762 0.2536 -0.0532 373 LEU A O 2325 C CB . LEU A 285 ? 0.7494 0.5978 0.4803 -0.0925 0.2092 -0.0502 373 LEU A CB 2326 C CG . LEU A 285 ? 0.8101 0.6955 0.5434 -0.1033 0.2371 -0.0680 373 LEU A CG 2327 C CD1 . LEU A 285 ? 0.8090 0.6360 0.4936 -0.0955 0.2423 -0.0677 373 LEU A CD1 2328 C CD2 . LEU A 285 ? 0.8298 0.7962 0.6253 -0.0767 0.2339 -0.0781 373 LEU A CD2 2329 N N . TYR A 286 ? 0.7400 0.5759 0.4464 -0.1549 0.2189 -0.0498 374 TYR A N 2330 C CA . TYR A 286 ? 0.8168 0.6744 0.5225 -0.1953 0.2397 -0.0638 374 TYR A CA 2331 C C . TYR A 286 ? 0.8472 0.6111 0.4860 -0.2149 0.2436 -0.0545 374 TYR A C 2332 O O . TYR A 286 ? 0.8947 0.6329 0.5007 -0.2553 0.2712 -0.0645 374 TYR A O 2333 C CB . TYR A 286 ? 0.8208 0.7673 0.5915 -0.1896 0.2260 -0.0726 374 TYR A CB 2334 C CG . TYR A 286 ? 0.7608 0.7844 0.5856 -0.1561 0.2176 -0.0772 374 TYR A CG 2335 C CD1 . TYR A 286 ? 0.7210 0.8162 0.5754 -0.1654 0.2386 -0.0995 374 TYR A CD1 2336 C CD2 . TYR A 286 ? 0.7283 0.7471 0.5695 -0.1146 0.1917 -0.0602 374 TYR A CD2 2337 C CE1 . TYR A 286 ? 0.6454 0.8058 0.5439 -0.1264 0.2298 -0.1043 374 TYR A CE1 2338 C CE2 . TYR A 286 ? 0.6805 0.7505 0.5585 -0.0797 0.1857 -0.0622 374 TYR A CE2 2339 C CZ . TYR A 286 ? 0.7150 0.8552 0.6208 -0.0818 0.2029 -0.0839 374 TYR A CZ 2340 O OH . TYR A 286 ? 0.8384 1.0253 0.7762 -0.0391 0.1959 -0.0866 374 TYR A OH 2341 N N . GLU A 287 ? 0.9168 0.6285 0.5340 -0.1859 0.2173 -0.0371 375 GLU A N 2342 C CA . GLU A 287 ? 0.9105 0.5285 0.4583 -0.1903 0.2163 -0.0276 375 GLU A CA 2343 C C . GLU A 287 ? 0.9969 0.5385 0.4683 -0.2009 0.2386 -0.0238 375 GLU A C 2344 O O . GLU A 287 ? 1.1230 0.5970 0.5424 -0.2180 0.2499 -0.0246 375 GLU A O 2345 C CB . GLU A 287 ? 0.8460 0.4421 0.3944 -0.1510 0.1822 -0.0145 375 GLU A CB 2346 C CG . GLU A 287 ? 0.9068 0.5691 0.5211 -0.1385 0.1622 -0.0148 375 GLU A CG 2347 C CD . GLU A 287 ? 0.9445 0.5964 0.5670 -0.1045 0.1343 -0.0055 375 GLU A CD 2348 O OE1 . GLU A 287 ? 0.7839 0.4838 0.4548 -0.0937 0.1212 -0.0034 375 GLU A OE1 2349 O OE2 . GLU A 287 ? 0.9215 0.5200 0.5005 -0.0886 0.1263 -0.0018 375 GLU A OE2 2350 N N . LYS A 288 ? 1.0211 0.5763 0.4956 -0.1839 0.2377 -0.0230 376 LYS A N 2351 C CA . LYS A 288 ? 1.0600 0.5506 0.4676 -0.1872 0.2529 -0.0203 376 LYS A CA 2352 C C . LYS A 288 ? 1.0762 0.5844 0.4912 -0.2269 0.2845 -0.0356 376 LYS A C 2353 O O . LYS A 288 ? 1.1093 0.5449 0.4648 -0.2385 0.2966 -0.0342 376 LYS A O 2354 C CB . LYS A 288 ? 1.0867 0.5809 0.4856 -0.1568 0.2424 -0.0175 376 LYS A CB 2355 C CG . LYS A 288 ? 0.9570 0.4298 0.3544 -0.1177 0.2029 -0.0087 376 LYS A CG 2356 C CD . LYS A 288 ? 0.9484 0.4192 0.3367 -0.0889 0.1869 -0.0118 376 LYS A CD 2357 C CE . LYS A 288 ? 1.0310 0.5099 0.4454 -0.0584 0.1487 -0.0105 376 LYS A CE 2358 N NZ . LYS A 288 ? 0.9657 0.4430 0.3708 -0.0333 0.1302 -0.0190 376 LYS A NZ 2359 N N . ASN A 289 ? 0.9873 0.5923 0.4725 -0.2465 0.2980 -0.0523 377 ASN A N 2360 C CA . ASN A 289 ? 1.0224 0.6594 0.5246 -0.2889 0.3263 -0.0731 377 ASN A CA 2361 C C . ASN A 289 ? 1.1215 0.6929 0.5845 -0.3152 0.3315 -0.0757 377 ASN A C 2362 O O . ASN A 289 ? 1.1935 0.7175 0.6160 -0.3453 0.3550 -0.0854 377 ASN A O 2363 C CB . ASN A 289 ? 1.0435 0.8093 0.6351 -0.2997 0.3319 -0.0944 377 ASN A CB 2364 C CG . ASN A 289 ? 1.0593 0.8914 0.6891 -0.2694 0.3305 -0.0969 377 ASN A CG 2365 O OD1 . ASN A 289 ? 1.0964 0.8828 0.6873 -0.2509 0.3315 -0.0877 377 ASN A OD1 2366 N ND2 . ASN A 289 ? 0.9602 0.9009 0.6638 -0.2613 0.3280 -0.1126 377 ASN A ND2 2367 N N . LEU A 290 ? 1.1862 0.7517 0.6574 -0.3037 0.3117 -0.0687 378 LEU A N 2368 C CA . LEU A 290 ? 1.1968 0.7028 0.6315 -0.3246 0.3163 -0.0742 378 LEU A CA 2369 C C . LEU A 290 ? 1.2538 0.6324 0.5924 -0.3108 0.3180 -0.0607 378 LEU A C 2370 O O . LEU A 290 ? 1.2431 0.5607 0.5319 -0.3382 0.3406 -0.0713 378 LEU A O 2371 C CB . LEU A 290 ? 1.1348 0.6599 0.5948 -0.3086 0.2929 -0.0676 378 LEU A CB 2372 C CG . LEU A 290 ? 1.1534 0.6026 0.5635 -0.3217 0.2960 -0.0719 378 LEU A CG 2373 C CD1 . LEU A 290 ? 1.2264 0.7057 0.6515 -0.3732 0.3241 -0.1017 378 LEU A CD1 2374 C CD2 . LEU A 290 ? 1.0642 0.5294 0.4963 -0.3033 0.2726 -0.0642 378 LEU A CD2 2375 N N . VAL A 291 ? 1.1718 0.5112 0.4810 -0.2661 0.2937 -0.0392 379 VAL A N 2376 C CA . VAL A 291 ? 1.2667 0.4932 0.4846 -0.2422 0.2890 -0.0268 379 VAL A CA 2377 C C . VAL A 291 ? 1.3724 0.5604 0.5465 -0.2603 0.3156 -0.0306 379 VAL A C 2378 O O . VAL A 291 ? 1.4421 0.5375 0.5388 -0.2672 0.3316 -0.0309 379 VAL A O 2379 C CB . VAL A 291 ? 1.2449 0.4560 0.4483 -0.1894 0.2545 -0.0081 379 VAL A CB 2380 C CG1 . VAL A 291 ? 1.4143 0.5235 0.5249 -0.1606 0.2498 0.0018 379 VAL A CG1 2381 C CG2 . VAL A 291 ? 1.1933 0.4225 0.4237 -0.1726 0.2310 -0.0044 379 VAL A CG2 2382 N N . LYS A 292 ? 1.2714 0.5304 0.4921 -0.2687 0.3236 -0.0348 380 LYS A N 2383 C CA . LYS A 292 ? 1.3446 0.5794 0.5311 -0.2902 0.3521 -0.0404 380 LYS A CA 2384 C C . LYS A 292 ? 1.4653 0.6985 0.6518 -0.3433 0.3860 -0.0622 380 LYS A C 2385 O O . LYS A 292 ? 1.5738 0.7356 0.6952 -0.3633 0.4124 -0.0654 380 LYS A O 2386 C CB . LYS A 292 ? 1.4519 0.7714 0.6909 -0.2866 0.3552 -0.0439 380 LYS A CB 2387 C CG . LYS A 292 ? 1.4721 0.7437 0.6524 -0.2873 0.3741 -0.0402 380 LYS A CG 2388 C CD . LYS A 292 ? 1.4258 0.7102 0.6085 -0.3379 0.4141 -0.0595 380 LYS A CD 2389 C CE . LYS A 292 ? 1.5397 0.8049 0.6822 -0.3405 0.4353 -0.0580 380 LYS A CE 2390 N NZ . LYS A 292 ? 1.5527 0.8341 0.7008 -0.3949 0.4763 -0.0801 380 LYS A NZ 2391 N N . HIS A 293 ? 1.3851 0.6935 0.6390 -0.3671 0.3862 -0.0790 381 HIS A N 2392 C CA . HIS A 293 ? 1.5221 0.8353 0.7765 -0.4202 0.4182 -0.1056 381 HIS A CA 2393 C C . HIS A 293 ? 1.6285 0.8191 0.7921 -0.4274 0.4289 -0.1041 381 HIS A C 2394 O O . HIS A 293 ? 1.7277 0.8670 0.8431 -0.4654 0.4632 -0.1192 381 HIS A O 2395 C CB . HIS A 293 ? 1.4375 0.8724 0.7873 -0.4440 0.4153 -0.1289 381 HIS A CB 2396 C CG . HIS A 293 ? 1.5494 0.9944 0.8993 -0.4994 0.4461 -0.1615 381 HIS A CG 2397 N ND1 . HIS A 293 ? 1.6368 1.0473 0.9657 -0.5158 0.4478 -0.1720 381 HIS A ND1 2398 C CD2 . HIS A 293 ? 1.6654 1.1473 1.0278 -0.5434 0.4787 -0.1881 381 HIS A CD2 2399 C CE1 . HIS A 293 ? 1.7325 1.1593 1.0614 -0.5688 0.4803 -0.2050 381 HIS A CE1 2400 N NE2 . HIS A 293 ? 1.7633 1.2345 1.1136 -0.5873 0.4993 -0.2159 381 HIS A NE2 2401 N N . LEU A 294 ? 1.5534 0.6967 0.6904 -0.3895 0.4015 -0.0868 382 LEU A N 2402 C CA . LEU A 294 ? 1.6939 0.7218 0.7407 -0.3857 0.4094 -0.0839 382 LEU A CA 2403 C C . LEU A 294 ? 1.7097 0.6201 0.6544 -0.3530 0.4104 -0.0637 382 LEU A C 2404 O O . LEU A 294 ? 1.9207 0.7255 0.7774 -0.3440 0.4190 -0.0597 382 LEU A O 2405 C CB . LEU A 294 ? 1.5801 0.6134 0.6417 -0.3558 0.3795 -0.0755 382 LEU A CB 2406 C CG . LEU A 294 ? 1.4454 0.5886 0.6007 -0.3815 0.3745 -0.0930 382 LEU A CG 2407 C CD1 . LEU A 294 ? 1.3848 0.5322 0.5540 -0.3440 0.3414 -0.0788 382 LEU A CD1 2408 C CD2 . LEU A 294 ? 1.5114 0.6535 0.6590 -0.4373 0.4089 -0.1225 382 LEU A CD2 2409 N N . ASN A 295 ? 1.7869 0.7162 0.7399 -0.3322 0.4013 -0.0512 383 ASN A N 2410 C CA . ASN A 295 ? 1.9220 0.7499 0.7812 -0.2954 0.3973 -0.0320 383 ASN A CA 2411 C C . ASN A 295 ? 2.0947 0.8153 0.8577 -0.3241 0.4376 -0.0378 383 ASN A C 2412 O O . ASN A 295 ? 1.9699 0.7160 0.7499 -0.3753 0.4725 -0.0548 383 ASN A O 2413 C CB . ASN A 295 ? 1.8449 0.7217 0.7327 -0.2739 0.3839 -0.0208 383 ASN A CB 2414 C CG . ASN A 295 ? 1.9567 0.7366 0.7490 -0.2310 0.3748 -0.0018 383 ASN A CG 2415 O OD1 . ASN A 295 ? 1.8839 0.5867 0.6119 -0.1924 0.3568 0.0082 383 ASN A OD1 2416 N ND2 . ASN A 295 ? 2.0066 0.7932 0.7868 -0.2350 0.3871 0.0021 383 ASN A ND2 2417 N N . GLN A 296 ? 2.0554 0.6574 0.7159 -0.2898 0.4332 -0.0248 384 GLN A N 2418 C CA . GLN A 296 ? 2.4329 0.9121 0.9835 -0.3103 0.4718 -0.0270 384 GLN A CA 2419 C C . GLN A 296 ? 2.3199 0.7266 0.7925 -0.2774 0.4711 -0.0081 384 GLN A C 2420 O O . GLN A 296 ? 2.6410 0.9336 1.0091 -0.2867 0.5021 -0.0055 384 GLN A O 2421 C CB . GLN A 296 ? 2.3222 0.7060 0.7954 -0.2917 0.4717 -0.0250 384 GLN A CB 2422 C CG . GLN A 296 ? 2.3049 0.7214 0.8164 -0.3418 0.4931 -0.0474 384 GLN A CG 2423 C CD . GLN A 296 ? 2.4847 0.7928 0.9040 -0.3254 0.4996 -0.0438 384 GLN A CD 2424 O OE1 . GLN A 296 ? 2.4406 0.7109 0.8232 -0.2649 0.4665 -0.0261 384 GLN A OE1 2425 N NE2 . GLN A 296 ? 2.5222 0.7815 0.9025 -0.3796 0.5435 -0.0623 384 GLN A NE2 2426 N N . GLY A 297 ? 2.2241 0.6945 0.7428 -0.2386 0.4365 0.0049 385 GLY A N 2427 C CA . GLY A 297 ? 2.3580 0.7756 0.8103 -0.2036 0.4308 0.0222 385 GLY A CA 2428 C C . GLY A 297 ? 2.2866 0.7535 0.7689 -0.2422 0.4576 0.0176 385 GLY A C 2429 O O . GLY A 297 ? 2.2234 0.7700 0.7814 -0.2958 0.4807 -0.0010 385 GLY A O 2430 N N . THR A 298 ? 2.3525 0.7777 0.7748 -0.2123 0.4537 0.0332 386 THR A N 2431 C CA . THR A 298 ? 2.3896 0.8583 0.8301 -0.2439 0.4798 0.0300 386 THR A CA 2432 C C . THR A 298 ? 2.2450 0.8413 0.7839 -0.2259 0.4496 0.0300 386 THR A C 2433 O O . THR A 298 ? 2.1113 0.7423 0.6843 -0.1835 0.4077 0.0362 386 THR A O 2434 C CB . THR A 298 ? 2.5083 0.8724 0.8311 -0.2199 0.4917 0.0470 386 THR A CB 2435 O OG1 . THR A 298 ? 2.5056 0.8460 0.7922 -0.1474 0.4452 0.0646 386 THR A OG1 2436 C CG2 . THR A 298 ? 2.6881 0.9148 0.9011 -0.2428 0.5306 0.0465 386 THR A CG2 2437 N N . ASP A 299 ? 2.1831 0.8481 0.7633 -0.2573 0.4726 0.0215 387 ASP A N 2438 C CA . ASP A 299 ? 2.0391 0.8167 0.7000 -0.2385 0.4486 0.0197 387 ASP A CA 2439 C C . ASP A 299 ? 2.1016 0.8438 0.7027 -0.1809 0.4183 0.0371 387 ASP A C 2440 O O . ASP A 299 ? 1.9732 0.7866 0.6249 -0.1496 0.3852 0.0368 387 ASP A O 2441 C CB . ASP A 299 ? 2.0748 0.9388 0.7940 -0.2839 0.4828 0.0021 387 ASP A CB 2442 C CG . ASP A 299 ? 2.0013 0.9530 0.8177 -0.3279 0.4960 -0.0200 387 ASP A CG 2443 O OD1 . ASP A 299 ? 1.9097 0.8728 0.7614 -0.3181 0.4724 -0.0201 387 ASP A OD1 2444 O OD2 . ASP A 299 ? 2.0818 1.0969 0.9401 -0.3706 0.5292 -0.0391 387 ASP A OD2 2445 N N . GLU A 300 ? 2.2225 0.8536 0.7119 -0.1662 0.4296 0.0503 388 GLU A N 2446 C CA . GLU A 300 ? 2.2725 0.8670 0.6959 -0.1080 0.3991 0.0653 388 GLU A CA 2447 C C . GLU A 300 ? 2.2272 0.8152 0.6557 -0.0550 0.3499 0.0712 388 GLU A C 2448 O O . GLU A 300 ? 2.1783 0.8099 0.6198 -0.0111 0.3118 0.0727 388 GLU A O 2449 C CB . GLU A 300 ? 2.5266 0.9953 0.8200 -0.1018 0.4239 0.0788 388 GLU A CB 2450 C CG . GLU A 300 ? 2.5764 1.0515 0.8513 -0.1458 0.4700 0.0743 388 GLU A CG 2451 C CD . GLU A 300 ? 2.6597 1.1235 0.9535 -0.2151 0.5199 0.0606 388 GLU A CD 2452 O OE1 . GLU A 300 ? 2.6450 1.0715 0.9431 -0.2273 0.5209 0.0565 388 GLU A OE1 2453 O OE2 . GLU A 300 ? 2.6787 1.1757 0.9832 -0.2576 0.5584 0.0510 388 GLU A OE2 2454 N N . ASP A 301 ? 2.2498 0.7858 0.6664 -0.0599 0.3518 0.0712 389 ASP A N 2455 C CA . ASP A 301 ? 2.3155 0.8539 0.7448 -0.0128 0.3082 0.0737 389 ASP A CA 2456 C C . ASP A 301 ? 2.1457 0.8100 0.6899 -0.0097 0.2787 0.0646 389 ASP A C 2457 O O . ASP A 301 ? 2.0713 0.7619 0.6280 0.0377 0.2363 0.0659 389 ASP A O 2458 C CB . ASP A 301 ? 2.2528 0.7223 0.6553 -0.0258 0.3212 0.0711 389 ASP A CB 2459 C CG . ASP A 301 ? 2.4779 0.8057 0.7485 -0.0117 0.3421 0.0807 389 ASP A CG 2460 O OD1 . ASP A 301 ? 2.6293 0.9128 0.8288 0.0156 0.3406 0.0918 389 ASP A OD1 2461 O OD2 . ASP A 301 ? 2.5365 0.7951 0.7694 -0.0267 0.3603 0.0765 389 ASP A OD2 2462 N N . ILE A 302 ? 1.9385 0.6828 0.5649 -0.0587 0.3015 0.0533 390 ILE A N 2463 C CA . ILE A 302 ? 1.7917 0.6462 0.5155 -0.0539 0.2774 0.0448 390 ILE A CA 2464 C C . ILE A 302 ? 1.7899 0.6885 0.5133 -0.0266 0.2595 0.0429 390 ILE A C 2465 O O . ILE A 302 ? 1.7057 0.6512 0.4606 0.0073 0.2221 0.0389 390 ILE A O 2466 C CB . ILE A 302 ? 1.7015 0.6345 0.5148 -0.1072 0.3045 0.0310 390 ILE A CB 2467 C CG1 . ILE A 302 ? 1.7247 0.6202 0.5377 -0.1369 0.3217 0.0278 390 ILE A CG1 2468 C CG2 . ILE A 302 ? 1.5657 0.5990 0.4675 -0.0963 0.2798 0.0232 390 ILE A CG2 2469 C CD1 . ILE A 302 ? 1.6811 0.6416 0.5607 -0.1949 0.3567 0.0110 390 ILE A CD1 2470 N N . TYR A 303 ? 1.8386 0.7229 0.5241 -0.0418 0.2861 0.0428 391 TYR A N 2471 C CA . TYR A 303 ? 1.8219 0.7541 0.5089 -0.0205 0.2729 0.0361 391 TYR A CA 2472 C C . TYR A 303 ? 1.8673 0.7670 0.4982 0.0383 0.2294 0.0418 391 TYR A C 2473 O O . TYR A 303 ? 1.7987 0.7618 0.4677 0.0645 0.1963 0.0298 391 TYR A O 2474 C CB . TYR A 303 ? 1.8998 0.8162 0.5470 -0.0472 0.3123 0.0350 391 TYR A CB 2475 C CG . TYR A 303 ? 1.8832 0.8555 0.5354 -0.0307 0.3047 0.0231 391 TYR A CG 2476 C CD1 . TYR A 303 ? 2.0666 1.1367 0.8051 -0.0469 0.3105 0.0032 391 TYR A CD1 2477 C CD2 . TYR A 303 ? 1.9820 0.9075 0.5493 0.0031 0.2923 0.0293 391 TYR A CD2 2478 C CE1 . TYR A 303 ? 2.0790 1.1947 0.8191 -0.0310 0.3050 -0.0124 391 TYR A CE1 2479 C CE2 . TYR A 303 ? 1.9711 0.9495 0.5418 0.0170 0.2852 0.0140 391 TYR A CE2 2480 C CZ . TYR A 303 ? 1.8655 0.9367 0.5228 -0.0011 0.2923 -0.0079 391 TYR A CZ 2481 O OH . TYR A 303 ? 1.8612 0.9794 0.5203 0.0133 0.2862 -0.0274 391 TYR A OH 2482 N N . LEU A 304 ? 1.9967 0.7983 0.5373 0.0596 0.2294 0.0568 392 LEU A N 2483 C CA . LEU A 304 ? 2.0649 0.8339 0.5419 0.1205 0.1897 0.0611 392 LEU A CA 2484 C C . LEU A 304 ? 2.0408 0.8225 0.5424 0.1596 0.1474 0.0588 392 LEU A C 2485 O O . LEU A 304 ? 1.9987 0.8198 0.5021 0.2053 0.1052 0.0497 392 LEU A O 2486 C CB . LEU A 304 ? 2.2263 0.8783 0.5845 0.1339 0.2088 0.0775 392 LEU A CB 2487 C CG . LEU A 304 ? 2.3858 1.0193 0.6895 0.1189 0.2372 0.0802 392 LEU A CG 2488 C CD1 . LEU A 304 ? 2.2256 0.9610 0.5805 0.1277 0.2169 0.0632 392 LEU A CD1 2489 C CD2 . LEU A 304 ? 2.4488 1.0591 0.7584 0.0538 0.2943 0.0820 392 LEU A CD2 2490 N N . LEU A 305 ? 1.9980 0.7517 0.5197 0.1408 0.1591 0.0634 393 LEU A N 2491 C CA . LEU A 305 ? 1.9792 0.7245 0.5051 0.1801 0.1249 0.0627 393 LEU A CA 2492 C C . LEU A 305 ? 1.9232 0.7510 0.5523 0.1593 0.1149 0.0530 393 LEU A C 2493 O O . LEU A 305 ? 1.8270 0.6744 0.4768 0.1919 0.0823 0.0485 393 LEU A O 2494 C CB . LEU A 305 ? 2.1977 0.8271 0.6429 0.1845 0.1448 0.0740 393 LEU A CB 2495 C CG . LEU A 305 ? 2.3694 0.8901 0.6940 0.2049 0.1609 0.0858 393 LEU A CG 2496 C CD1 . LEU A 305 ? 2.3727 0.7860 0.6357 0.1750 0.2019 0.0923 393 LEU A CD1 2497 C CD2 . LEU A 305 ? 2.4155 0.9146 0.6813 0.2823 0.1163 0.0860 393 LEU A CD2 2498 N N . GLY A 306 ? 1.7561 0.6344 0.4482 0.1070 0.1434 0.0486 394 GLY A N 2499 C CA . GLY A 306 ? 1.6322 0.5817 0.4153 0.0835 0.1404 0.0408 394 GLY A CA 2500 C C . GLY A 306 ? 1.7960 0.6958 0.5700 0.0749 0.1489 0.0465 394 GLY A C 2501 O O . GLY A 306 ? 1.7169 0.6599 0.5478 0.0735 0.1350 0.0421 394 GLY A O 2502 N N . LYS A 307 ? 1.8160 0.6212 0.5129 0.0685 0.1734 0.0542 395 LYS A N 2503 C CA . LYS A 307 ? 1.8559 0.5970 0.5216 0.0687 0.1799 0.0556 395 LYS A CA 2504 C C . LYS A 307 ? 1.9404 0.6714 0.6261 0.0062 0.2235 0.0504 395 LYS A C 2505 O O . LYS A 307 ? 1.9915 0.6894 0.6449 -0.0271 0.2583 0.0505 395 LYS A O 2506 C CB . LYS A 307 ? 1.9783 0.6111 0.5314 0.1125 0.1745 0.0635 395 LYS A CB 2507 C CG . LYS A 307 ? 2.1023 0.6611 0.6088 0.1228 0.1788 0.0623 395 LYS A CG 2508 C CD . LYS A 307 ? 2.2584 0.7185 0.6523 0.1817 0.1653 0.0688 395 LYS A CD 2509 C CE . LYS A 307 ? 2.3755 0.7119 0.6704 0.1595 0.2073 0.0728 395 LYS A CE 2510 N NZ . LYS A 307 ? 2.5231 0.7588 0.7028 0.2248 0.1920 0.0787 395 LYS A NZ 2511 N N . ALA A 308 ? 1.8099 0.5758 0.5500 -0.0096 0.2207 0.0436 396 ALA A N 2512 C CA . ALA A 308 ? 1.7793 0.5344 0.5324 -0.0631 0.2566 0.0344 396 ALA A CA 2513 C C . ALA A 308 ? 1.8592 0.5268 0.5432 -0.0451 0.2561 0.0345 396 ALA A C 2514 O O . ALA A 308 ? 1.8928 0.5466 0.5575 0.0058 0.2228 0.0392 396 ALA A O 2515 C CB . ALA A 308 ? 1.6796 0.5415 0.5406 -0.0933 0.2548 0.0252 396 ALA A CB 2516 N N . THR A 309 ? 1.9321 0.5407 0.5743 -0.0854 0.2938 0.0274 397 THR A N 2517 C CA . THR A 309 ? 2.1498 0.6761 0.7240 -0.0720 0.2974 0.0259 397 THR A CA 2518 C C . THR A 309 ? 2.1393 0.6975 0.7590 -0.1262 0.3222 0.0108 397 THR A C 2519 O O . THR A 309 ? 2.1749 0.7354 0.8019 -0.1815 0.3596 -0.0007 397 THR A O 2520 C CB . THR A 309 ? 2.3182 0.7100 0.7635 -0.0605 0.3206 0.0322 397 THR A CB 2521 O OG1 . THR A 309 ? 2.3200 0.6770 0.7129 0.0062 0.2881 0.0455 397 THR A OG1 2522 C CG2 . THR A 309 ? 2.3065 0.6138 0.6832 -0.0648 0.3377 0.0275 397 THR A CG2 2523 N N . LEU A 310 ? 2.1177 0.7076 0.7706 -0.1098 0.3004 0.0093 398 LEU A N 2524 C CA . LEU A 310 ? 2.0264 0.6412 0.7135 -0.1541 0.3202 -0.0044 398 LEU A CA 2525 C C . LEU A 310 ? 2.0745 0.5952 0.6763 -0.1327 0.3229 -0.0016 398 LEU A C 2526 O O . LEU A 310 ? 2.0610 0.5452 0.6200 -0.0734 0.2928 0.0102 398 LEU A O 2527 C CB . LEU A 310 ? 1.8469 0.5839 0.6493 -0.1596 0.2967 -0.0081 398 LEU A CB 2528 C CG . LEU A 310 ? 1.7198 0.5601 0.6170 -0.2043 0.3086 -0.0188 398 LEU A CG 2529 C CD1 . LEU A 310 ? 1.7833 0.6307 0.6779 -0.1951 0.3081 -0.0112 398 LEU A CD1 2530 C CD2 . LEU A 310 ? 1.6005 0.5457 0.5959 -0.1999 0.2832 -0.0194 398 LEU A CD2 2531 N N . PRO A 311 ? 2.1732 0.6564 0.7492 -0.1804 0.3593 -0.0140 399 PRO A N 2532 C CA . PRO A 311 ? 2.3487 0.7375 0.8401 -0.1618 0.3647 -0.0101 399 PRO A CA 2533 C C . PRO A 311 ? 2.2502 0.7036 0.8054 -0.1509 0.3400 -0.0105 399 PRO A C 2534 O O . PRO A 311 ? 2.0833 0.6451 0.7425 -0.1807 0.3347 -0.0198 399 PRO A O 2535 C CB . PRO A 311 ? 2.4417 0.7731 0.8893 -0.2257 0.4170 -0.0259 399 PRO A CB 2536 C CG . PRO A 311 ? 2.3249 0.7753 0.8831 -0.2818 0.4286 -0.0445 399 PRO A CG 2537 C CD . PRO A 311 ? 2.0606 0.5916 0.6860 -0.2522 0.3960 -0.0345 399 PRO A CD 2538 N N . GLY A 312 ? 2.2975 0.6839 0.7893 -0.1061 0.3247 -0.0004 400 GLY A N 2539 C CA . GLY A 312 ? 2.0936 0.5304 0.6385 -0.0919 0.3012 0.0004 400 GLY A CA 2540 C C . GLY A 312 ? 2.1158 0.5488 0.6748 -0.1488 0.3329 -0.0139 400 GLY A C 2541 O O . GLY A 312 ? 2.2553 0.6151 0.7514 -0.1879 0.3732 -0.0223 400 GLY A O 2542 N N . PHE A 313 ? 2.0249 0.5364 0.6664 -0.1549 0.3159 -0.0188 401 PHE A N 2543 C CA . PHE A 313 ? 2.0652 0.5869 0.7318 -0.2082 0.3420 -0.0364 401 PHE A CA 2544 C C . PHE A 313 ? 2.2387 0.6315 0.7981 -0.2077 0.3664 -0.0356 401 PHE A C 2545 O O . PHE A 313 ? 2.2964 0.6584 0.8354 -0.2645 0.4062 -0.0525 401 PHE A O 2546 C CB . PHE A 313 ? 1.9063 0.5207 0.6687 -0.2019 0.3138 -0.0411 401 PHE A CB 2547 C CG . PHE A 313 ? 1.7903 0.5310 0.6603 -0.2190 0.2998 -0.0471 401 PHE A CG 2548 C CD1 . PHE A 313 ? 1.7211 0.5094 0.6234 -0.2703 0.3256 -0.0615 401 PHE A CD1 2549 C CD2 . PHE A 313 ? 1.6630 0.4728 0.5995 -0.1826 0.2617 -0.0405 401 PHE A CD2 2550 C CE1 . PHE A 313 ? 1.5994 0.5002 0.5960 -0.2824 0.3125 -0.0671 401 PHE A CE1 2551 C CE2 . PHE A 313 ? 1.5911 0.5061 0.6175 -0.1978 0.2510 -0.0454 401 PHE A CE2 2552 C CZ . PHE A 313 ? 1.4781 0.4377 0.5333 -0.2465 0.2758 -0.0574 401 PHE A CZ 2553 N N . ARG A 314 ? 2.3570 0.6745 0.8454 -0.1431 0.3432 -0.0180 402 ARG A N 2554 C CA . ARG A 314 ? 2.5349 0.7218 0.9148 -0.1317 0.3621 -0.0151 402 ARG A CA 2555 C C . ARG A 314 ? 2.7114 0.7954 0.9964 -0.1743 0.4121 -0.0206 402 ARG A C 2556 O O . ARG A 314 ? 2.7351 0.7131 0.9378 -0.1889 0.4409 -0.0241 402 ARG A O 2557 C CB . ARG A 314 ? 2.4921 0.6208 0.8058 -0.0459 0.3258 0.0037 402 ARG A CB 2558 C CG . ARG A 314 ? 2.7755 0.7682 0.9753 -0.0236 0.3404 0.0076 402 ARG A CG 2559 C CD . ARG A 314 ? 2.9116 0.8678 1.0586 0.0668 0.2992 0.0217 402 ARG A CD 2560 N NE . ARG A 314 ? 3.2626 1.0667 1.2736 0.0927 0.3177 0.0277 402 ARG A NE 2561 C CZ . ARG A 314 ? 3.4076 1.1695 1.3776 0.1564 0.2915 0.0319 402 ARG A CZ 2562 N NH1 . ARG A 314 ? 3.3378 1.2044 1.3976 0.1987 0.2462 0.0287 402 ARG A NH1 2563 N NH2 . ARG A 314 ? 3.5906 1.2043 1.4282 0.1786 0.3118 0.0375 402 ARG A NH2 2564 N N . THR A 315 ? 2.6456 0.7596 0.9434 -0.1962 0.4240 -0.0232 403 THR A N 2565 C CA . THR A 315 ? 2.8677 0.8818 1.0718 -0.2294 0.4692 -0.0281 403 THR A CA 2566 C C . THR A 315 ? 2.8496 0.9315 1.1175 -0.3111 0.5062 -0.0534 403 THR A C 2567 O O . THR A 315 ? 2.9178 0.9595 1.1426 -0.3360 0.5348 -0.0584 403 THR A O 2568 C CB . THR A 315 ? 2.8984 0.8677 1.0420 -0.1787 0.4537 -0.0116 403 THR A CB 2569 O OG1 . THR A 315 ? 2.5871 0.6814 0.8351 -0.1809 0.4304 -0.0137 403 THR A OG1 2570 C CG2 . THR A 315 ? 2.8011 0.7145 0.8826 -0.0938 0.4147 0.0085 403 THR A CG2 2571 N N . ILE A 316 ? 2.7564 0.9403 1.1245 -0.3516 0.5059 -0.0715 404 ILE A N 2572 C CA . ILE A 316 ? 2.7323 1.0182 1.1861 -0.4198 0.5294 -0.0989 404 ILE A CA 2573 C C . ILE A 316 ? 2.8525 1.0970 1.2758 -0.4910 0.5808 -0.1270 404 ILE A C 2574 O O . ILE A 316 ? 2.9958 1.1176 1.3223 -0.4878 0.6009 -0.1223 404 ILE A O 2575 C CB . ILE A 316 ? 2.6428 1.0813 1.2321 -0.4170 0.4935 -0.1044 404 ILE A CB 2576 C CG1 . ILE A 316 ? 2.5473 1.1053 1.2285 -0.4591 0.5009 -0.1246 404 ILE A CG1 2577 C CG2 . ILE A 316 ? 2.6970 1.1543 1.3173 -0.4375 0.4950 -0.1178 404 ILE A CG2 2578 C CD1 . ILE A 316 ? 2.3681 1.0644 1.1700 -0.4534 0.4671 -0.1291 404 ILE A CD1 2579 N N . HIS A 317 ? 2.5337 0.8801 1.0374 -0.5540 0.6022 -0.1581 405 HIS A N 2580 C CA . HIS A 317 ? 2.8351 1.1663 1.3264 -0.6262 0.6498 -0.1918 405 HIS A CA 2581 C C . HIS A 317 ? 2.7937 1.2350 1.3839 -0.6530 0.6386 -0.2148 405 HIS A C 2582 O O . HIS A 317 ? 2.7284 1.2854 1.4162 -0.6275 0.5977 -0.2102 405 HIS A O 2583 C CB . HIS A 317 ? 2.6615 1.0271 1.1656 -0.6846 0.6877 -0.2191 405 HIS A CB 2584 C CG . HIS A 317 ? 2.9558 1.2565 1.4031 -0.7553 0.7460 -0.2507 405 HIS A CG 2585 N ND1 . HIS A 317 ? 3.0845 1.2686 1.4478 -0.7606 0.7665 -0.2483 405 HIS A ND1 2586 C CD2 . HIS A 317 ? 2.9906 1.3264 1.4529 -0.8252 0.7894 -0.2877 405 HIS A CD2 2587 C CE1 . HIS A 317 ? 3.2067 1.3536 1.5338 -0.8330 0.8217 -0.2821 405 HIS A CE1 2588 N NE2 . HIS A 317 ? 3.1560 1.3966 1.5432 -0.8739 0.8368 -0.3075 405 HIS A NE2 2589 N N . CYS A 318 ? 2.8936 1.2914 1.4519 -0.7053 0.6767 -0.2408 406 CYS A N 2590 C CA . CYS A 318 ? 2.7982 1.2859 1.4361 -0.7417 0.6753 -0.2707 406 CYS A CA 2591 C C . CYS A 318 ? 2.5157 1.1268 1.2617 -0.7035 0.6217 -0.2629 406 CYS A C 2592 O O . CYS A 318 ? 2.5067 1.0826 1.2438 -0.6685 0.5974 -0.2485 406 CYS A O 2593 C CB . CYS A 318 ? 2.8283 1.4043 1.5179 -0.8219 0.7146 -0.3194 406 CYS A CB 2594 S SG . CYS A 318 ? 2.8644 1.6004 1.6596 -0.8275 0.6984 -0.3318 406 CYS A SG 2595 C C1 . NAG B . ? 0.7441 1.5253 0.9697 -0.4088 0.0194 -0.2642 501 NAG A C1 2596 C C2 . NAG B . ? 0.7270 1.4795 0.9310 -0.4242 0.0829 -0.2426 501 NAG A C2 2597 C C3 . NAG B . ? 0.7444 1.4084 0.9056 -0.3976 0.0337 -0.2138 501 NAG A C3 2598 C C4 . NAG B . ? 0.7264 1.3795 0.9116 -0.3348 -0.0191 -0.2453 501 NAG A C4 2599 C C5 . NAG B . ? 0.7793 1.4677 0.9895 -0.3228 -0.0733 -0.2675 501 NAG A C5 2600 C C6 . NAG B . ? 0.7765 1.4673 1.0192 -0.2593 -0.1142 -0.3046 501 NAG A C6 2601 C C7 . NAG B . ? 0.9445 1.5873 1.0521 -0.4237 0.1691 -0.1916 501 NAG A C7 2602 C C8 . NAG B . ? 0.8072 1.3814 0.8576 -0.4304 0.1685 -0.1534 501 NAG A C8 2603 N N2 . NAG B . ? 0.9080 1.6074 1.0507 -0.4498 0.1147 -0.1996 501 NAG A N2 2604 O O3 . NAG B . ? 0.6698 1.3171 0.8183 -0.4040 0.0957 -0.2006 501 NAG A O3 2605 O O4 . NAG B . ? 0.7366 1.3013 0.8748 -0.3181 -0.0772 -0.2134 501 NAG A O4 2606 O O5 . NAG B . ? 0.7798 1.5558 1.0319 -0.3487 -0.0187 -0.2950 501 NAG A O5 2607 O O6 . NAG B . ? 0.6807 1.4353 0.9778 -0.2345 -0.0512 -0.3501 501 NAG A O6 2608 O O7 . NAG B . ? 0.9900 1.6275 1.1179 -0.3888 0.2009 -0.2142 501 NAG A O7 2609 C C1 . NAG C . ? 0.7014 1.2448 0.8450 -0.2812 -0.0536 -0.2255 502 NAG A C1 2610 C C2 . NAG C . ? 0.7668 1.2321 0.8802 -0.2454 -0.1369 -0.2127 502 NAG A C2 2611 C C3 . NAG C . ? 0.7608 1.2017 0.8785 -0.2034 -0.1188 -0.2273 502 NAG A C3 2612 C C4 . NAG C . ? 0.7123 1.1505 0.8109 -0.2324 -0.0471 -0.2052 502 NAG A C4 2613 C C5 . NAG C . ? 0.7553 1.2670 0.8792 -0.2736 0.0313 -0.2113 502 NAG A C5 2614 C C6 . NAG C . ? 0.6110 1.1108 0.7058 -0.3105 0.0942 -0.1784 502 NAG A C6 2615 C C7 . NAG C . ? 0.8594 1.3019 0.9667 -0.2289 -0.2682 -0.2109 502 NAG A C7 2616 C C8 . NAG C . ? 0.8991 1.3635 1.0359 -0.1919 -0.3254 -0.2395 502 NAG A C8 2617 N N2 . NAG C . ? 0.8091 1.2873 0.9453 -0.2154 -0.1993 -0.2363 502 NAG A N2 2618 O O3 . NAG C . ? 0.8243 1.1855 0.9076 -0.1763 -0.1959 -0.2110 502 NAG A O3 2619 O O4 . NAG C . ? 0.6949 1.1359 0.8116 -0.1909 -0.0152 -0.2293 502 NAG A O4 2620 O O5 . NAG C . ? 0.7848 1.3118 0.9027 -0.3102 0.0038 -0.1986 502 NAG A O5 2621 O O6 . NAG C . ? 0.5603 1.1334 0.6916 -0.3289 0.1828 -0.1983 502 NAG A O6 2622 O O7 . NAG C . ? 0.8726 1.2681 0.9322 -0.2685 -0.2829 -0.1659 502 NAG A O7 2623 C C1 . BMA D . ? 0.7386 1.1026 0.8185 -0.1649 -0.0643 -0.2124 503 BMA A C1 2624 C C2 . BMA D . ? 0.6970 1.0668 0.7765 -0.1562 0.0013 -0.2138 503 BMA A C2 2625 C C3 . BMA D . ? 0.7381 1.0343 0.7823 -0.1273 -0.0422 -0.2007 503 BMA A C3 2626 C C4 . BMA D . ? 0.7998 1.0608 0.8512 -0.0788 -0.1213 -0.2237 503 BMA A C4 2627 C C5 . BMA D . ? 0.8457 1.1108 0.9031 -0.0902 -0.1765 -0.2232 503 BMA A C5 2628 C C6 . BMA D . ? 0.9504 1.1990 1.0278 -0.0361 -0.2405 -0.2544 503 BMA A C6 2629 O O2 . BMA D . ? 0.7213 1.1553 0.8560 -0.1196 0.0496 -0.2617 503 BMA A O2 2630 O O3 . BMA D . ? 0.6991 1.0153 0.7550 -0.1069 0.0191 -0.2140 503 BMA A O3 2631 O O4 . BMA D . ? 0.8474 1.0254 0.8511 -0.0711 -0.1722 -0.1972 503 BMA A O4 2632 O O5 . BMA D . ? 0.7918 1.1378 0.8881 -0.1137 -0.1243 -0.2404 503 BMA A O5 2633 O O6 . BMA D . ? 1.0985 1.3631 1.1859 -0.0467 -0.2826 -0.2554 503 BMA A O6 2634 C C1 . MAN E . ? 0.6962 0.9659 0.7032 -0.1335 0.0303 -0.1719 504 MAN A C1 2635 C C2 . MAN E . ? 0.7788 1.0552 0.7934 -0.0982 0.0728 -0.1881 504 MAN A C2 2636 C C3 . MAN E . ? 0.7630 1.1188 0.8186 -0.1014 0.1681 -0.2090 504 MAN A C3 2637 C C4 . MAN E . ? 0.7229 1.0987 0.7619 -0.1628 0.2168 -0.1739 504 MAN A C4 2638 C C5 . MAN E . ? 0.6815 1.0504 0.7155 -0.1938 0.1673 -0.1634 504 MAN A C5 2639 C C6 . MAN E . ? 0.7201 1.1043 0.7349 -0.2556 0.2081 -0.1280 504 MAN A C6 2640 O O2 . MAN E . ? 0.6768 0.9061 0.6434 -0.1183 0.0765 -0.1490 504 MAN A O2 2641 O O3 . MAN E . ? 0.6480 1.0082 0.7057 -0.0709 0.2100 -0.2185 504 MAN A O3 2642 O O4 . MAN E . ? 0.8368 1.2587 0.9117 -0.1566 0.2854 -0.1853 504 MAN A O4 2643 O O5 . MAN E . ? 0.6567 0.9490 0.6503 -0.1881 0.0792 -0.1418 504 MAN A O5 2644 O O6 . MAN E . ? 0.6861 1.0600 0.6933 -0.2813 0.1545 -0.1180 504 MAN A O6 2645 C C1 . NAG F . ? 0.7285 0.8999 0.6766 -0.0782 0.0174 -0.1561 505 NAG A C1 2646 C C2 . NAG F . ? 0.7595 0.8604 0.6479 -0.1096 -0.0191 -0.1079 505 NAG A C2 2647 C C3 . NAG F . ? 0.8167 0.8531 0.6830 -0.0709 -0.0812 -0.1145 505 NAG A C3 2648 C C4 . NAG F . ? 0.7925 0.8590 0.6836 -0.0240 -0.0388 -0.1483 505 NAG A C4 2649 C C5 . NAG F . ? 0.9001 1.0392 0.8512 0.0045 0.0008 -0.1938 505 NAG A C5 2650 C C6 . NAG F . ? 0.8089 0.9850 0.7866 0.0480 0.0533 -0.2256 505 NAG A C6 2651 C C7 . NAG F . ? 0.7921 0.8687 0.6313 -0.2058 -0.0300 -0.0375 505 NAG A C7 2652 C C8 . NAG F . ? 0.7871 0.8374 0.6053 -0.2449 -0.0779 -0.0099 505 NAG A C8 2653 N N2 . NAG F . ? 0.8064 0.8822 0.6726 -0.1525 -0.0599 -0.0779 505 NAG A N2 2654 O O3 . NAG F . ? 0.8405 0.8159 0.6523 -0.1024 -0.1068 -0.0697 505 NAG A O3 2655 O O4 . NAG F . ? 0.8483 0.8588 0.7241 0.0163 -0.0981 -0.1614 505 NAG A O4 2656 O O5 . NAG F . ? 0.7058 0.9005 0.6739 -0.0366 0.0585 -0.1835 505 NAG A O5 2657 O O6 . NAG F . ? 0.7306 0.9412 0.7017 0.0233 0.1318 -0.2059 505 NAG A O6 2658 O O7 . NAG F . ? 0.7312 0.8284 0.5623 -0.2208 0.0331 -0.0229 505 NAG A O7 2659 C C1 . GAL G . ? 0.8583 0.8249 0.6896 0.0054 -0.0999 -0.1326 506 GAL A C1 2660 C C2 . GAL G . ? 0.8825 0.8319 0.7183 0.0614 -0.1138 -0.1641 506 GAL A C2 2661 C C3 . GAL G . ? 0.9058 0.8013 0.6922 0.0513 -0.1308 -0.1355 506 GAL A C3 2662 C C4 . GAL G . ? 0.9929 0.8166 0.7353 0.0141 -0.1987 -0.0974 506 GAL A C4 2663 C C5 . GAL G . ? 0.9998 0.8487 0.7408 -0.0389 -0.1742 -0.0668 506 GAL A C5 2664 C C6 . GAL G . ? 1.1121 0.8949 0.8123 -0.0778 -0.2386 -0.0280 506 GAL A C6 2665 O O2 . GAL G . ? 0.8302 0.8485 0.7070 0.0935 -0.0434 -0.1976 506 GAL A O2 2666 O O3 . GAL G . ? 0.9432 0.8106 0.7293 0.1008 -0.1615 -0.1641 506 GAL A O3 2667 O O4 . GAL G . ? 1.0385 0.8182 0.7863 0.0426 -0.2725 -0.1183 506 GAL A O4 2668 O O5 . GAL G . ? 0.9084 0.8048 0.6943 -0.0271 -0.1644 -0.0952 506 GAL A O5 2669 O O6 . GAL G . ? 1.3236 1.0898 1.0412 -0.0612 -0.2946 -0.0465 506 GAL A O6 2670 C C1 . MAN H . ? 1.3168 1.5514 1.4125 0.0015 -0.3530 -0.2754 507 MAN A C1 2671 C C2 . MAN H . ? 1.5108 1.7125 1.5810 -0.0197 -0.4221 -0.2484 507 MAN A C2 2672 C C3 . MAN H . ? 1.4822 1.7622 1.5830 -0.0507 -0.3928 -0.2570 507 MAN A C3 2673 C C4 . MAN H . ? 1.6946 2.0573 1.8608 -0.0145 -0.3574 -0.3117 507 MAN A C4 2674 C C5 . MAN H . ? 1.3508 1.7320 1.5374 0.0091 -0.2929 -0.3355 507 MAN A C5 2675 C C6 . MAN H . ? 1.3828 1.8359 1.6327 0.0517 -0.2631 -0.3898 507 MAN A C6 2676 O O2 . MAN H . ? 1.7069 1.8768 1.7833 0.0266 -0.4945 -0.2647 507 MAN A O2 2677 O O3 . MAN H . ? 1.5143 1.7734 1.5960 -0.0667 -0.4557 -0.2355 507 MAN A O3 2678 O O4 . MAN H . ? 1.6463 2.0845 1.8402 -0.0492 -0.3199 -0.3196 507 MAN A O4 2679 O O5 . MAN H . ? 1.3249 1.6278 1.4780 0.0378 -0.3295 -0.3239 507 MAN A O5 2680 O O6 . MAN H . ? 1.3511 1.8865 1.6354 0.0192 -0.1956 -0.4033 507 MAN A O6 2681 C C1 . NAG I . ? 1.8635 1.9413 1.8859 0.0186 -0.5617 -0.2258 508 NAG A C1 2682 C C2 . NAG I . ? 1.9482 1.9683 1.9660 0.0742 -0.6092 -0.2428 508 NAG A C2 2683 C C3 . NAG I . ? 2.0817 2.0036 2.0450 0.0669 -0.6832 -0.2038 508 NAG A C3 2684 C C4 . NAG I . ? 2.1544 2.0737 2.1059 0.0415 -0.7283 -0.1798 508 NAG A C4 2685 C C5 . NAG I . ? 2.0607 2.0449 2.0198 -0.0119 -0.6738 -0.1667 508 NAG A C5 2686 C C6 . NAG I . ? 2.1031 2.0986 2.0559 -0.0361 -0.7124 -0.1477 508 NAG A C6 2687 C C7 . NAG I . ? 1.8227 1.9006 1.8925 0.1281 -0.5190 -0.3022 508 NAG A C7 2688 C C8 . NAG I . ? 1.7797 1.8493 1.8450 0.1412 -0.4723 -0.3098 508 NAG A C8 2689 N N2 . NAG I . ? 1.8783 1.8988 1.9008 0.0911 -0.5611 -0.2579 508 NAG A N2 2690 O O3 . NAG I . ? 2.1452 2.0176 2.1090 0.1209 -0.7314 -0.2236 508 NAG A O3 2691 O O4 . NAG I . ? 2.2796 2.1062 2.1761 0.0257 -0.7843 -0.1378 508 NAG A O4 2692 O O5 . NAG I . ? 1.9446 2.0189 1.9580 0.0014 -0.6108 -0.2086 508 NAG A O5 2693 O O6 . NAG I . ? 2.1178 2.0666 2.0207 -0.0875 -0.7224 -0.0973 508 NAG A O6 2694 O O7 . NAG I . ? 1.8098 1.9449 1.9240 0.1505 -0.5187 -0.3344 508 NAG A O7 2695 C C1 . GAL J . ? 2.3743 2.1644 2.2638 0.0415 -0.8329 -0.1244 509 GAL A C1 2696 C C2 . GAL J . ? 2.4350 2.1527 2.2730 0.0004 -0.8399 -0.0686 509 GAL A C2 2697 C C3 . GAL J . ? 2.5205 2.2016 2.3504 0.0105 -0.8805 -0.0518 509 GAL A C3 2698 C C4 . GAL J . ? 2.5927 2.2310 2.4331 0.0672 -0.9194 -0.0773 509 GAL A C4 2699 C C5 . GAL J . ? 2.5405 2.2533 2.4306 0.1071 -0.9094 -0.1301 509 GAL A C5 2700 C C6 . GAL J . ? 2.6068 2.2848 2.5115 0.1671 -0.9423 -0.1604 509 GAL A C6 2701 O O2 . GAL J . ? 2.3989 2.1518 2.2250 -0.0545 -0.8024 -0.0435 509 GAL A O2 2702 O O3 . GAL J . ? 2.5586 2.1681 2.3448 -0.0225 -0.8866 -0.0054 509 GAL A O3 2703 O O4 . GAL J . ? 2.6326 2.1924 2.4426 0.0717 -0.9258 -0.0661 509 GAL A O4 2704 O O5 . GAL J . ? 2.4430 2.1925 2.3416 0.0966 -0.8692 -0.1465 509 GAL A O5 2705 O O6 . GAL J . ? 2.6976 2.3240 2.5881 0.1791 -0.9834 -0.1439 509 GAL A O6 2706 O "O5'" . CTN K . ? 0.9947 0.6636 0.6082 0.0672 -0.0294 -0.0745 510 CTN A "O5'" 2707 C "C5'" . CTN K . ? 0.9692 0.5850 0.5175 0.0868 -0.0319 -0.0615 510 CTN A "C5'" 2708 C "C4'" . CTN K . ? 1.0298 0.5928 0.5423 0.0651 -0.0046 -0.0397 510 CTN A "C4'" 2709 O "O4'" . CTN K . ? 0.9495 0.4709 0.4040 0.0715 -0.0018 -0.0389 510 CTN A "O4'" 2710 C "C1'" . CTN K . ? 0.9156 0.4277 0.3759 0.0419 0.0263 -0.0287 510 CTN A "C1'" 2711 N N1 . CTN K . ? 0.9093 0.4413 0.3831 0.0410 0.0251 -0.0409 510 CTN A N1 2712 C C6 . CTN K . ? 0.9101 0.4900 0.4308 0.0497 0.0043 -0.0611 510 CTN A C6 2713 C C5 . CTN K . ? 0.9164 0.5039 0.4382 0.0491 0.0029 -0.0760 510 CTN A C5 2714 C C4 . CTN K . ? 0.9141 0.4642 0.3903 0.0431 0.0226 -0.0687 510 CTN A C4 2715 N N3 . CTN K . ? 0.8984 0.4110 0.3358 0.0334 0.0441 -0.0495 510 CTN A N3 2716 C C2 . CTN K . ? 0.9412 0.4434 0.3786 0.0288 0.0473 -0.0354 510 CTN A C2 2717 O O2 . CTN K . ? 0.9927 0.4631 0.4006 0.0119 0.0707 -0.0212 510 CTN A O2 2718 N N4 . CTN K . ? 0.9484 0.5041 0.4212 0.0446 0.0214 -0.0862 510 CTN A N4 2719 C "C2'" . CTN K . ? 0.9220 0.4755 0.4490 0.0180 0.0393 -0.0226 510 CTN A "C2'" 2720 O "O2'" . CTN K . ? 0.9002 0.4179 0.3950 0.0060 0.0548 -0.0103 510 CTN A "O2'" 2721 C "C3'" . CTN K . ? 0.9250 0.5202 0.4952 0.0320 0.0174 -0.0329 510 CTN A "C3'" 2722 O "O3'" . CTN K . ? 0.8743 0.4887 0.4763 0.0208 0.0241 -0.0254 510 CTN A "O3'" 2723 P P . PO4 L . ? 0.9695 0.7175 0.7278 0.0043 0.0178 -0.0407 511 PO4 A P 2724 O O1 . PO4 L . ? 0.8827 0.6491 0.6410 0.0207 0.0035 -0.0505 511 PO4 A O1 2725 O O2 . PO4 L . ? 1.0205 0.7928 0.8232 -0.0150 0.0338 -0.0323 511 PO4 A O2 2726 O O3 . PO4 L . ? 1.0123 0.7200 0.7292 0.0011 0.0284 -0.0253 511 PO4 A O3 2727 O O4 . PO4 L . ? 1.1541 0.8980 0.9030 0.0118 0.0070 -0.0571 511 PO4 A O4 # 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 PRO 1 89 89 PRO PRO A . n A 1 2 GLU 2 90 90 GLU GLU A . n A 1 3 ALA 3 91 91 ALA ALA A . n A 1 4 SER 4 92 92 SER SER A . n A 1 5 PHE 5 93 93 PHE PHE A . n A 1 6 GLN 6 94 94 GLN GLN A . n A 1 7 VAL 7 95 95 VAL VAL A . n A 1 8 TRP 8 96 96 TRP TRP A . n A 1 9 ASN 9 97 97 ASN ASN A . n A 1 10 LYS 10 98 98 LYS LYS A . n A 1 11 ASP 11 99 99 ASP ASP A . n A 1 12 SER 12 100 100 SER SER A . n A 1 13 SER 13 101 101 SER SER A . n A 1 14 SER 14 102 102 SER SER A . n A 1 15 LYS 15 103 103 LYS LYS A . n A 1 16 ASN 16 104 104 ASN ASN A . n A 1 17 LEU 17 105 105 LEU LEU A . n A 1 18 ILE 18 106 106 ILE ILE A . n A 1 19 PRO 19 107 107 PRO PRO A . n A 1 20 ARG 20 108 108 ARG ARG A . n A 1 21 LEU 21 109 109 LEU LEU A . n A 1 22 GLN 22 110 110 GLN GLN A . n A 1 23 LYS 23 111 111 LYS LYS A . n A 1 24 ILE 24 112 112 ILE ILE A . n A 1 25 TRP 25 113 113 TRP TRP A . n A 1 26 LYS 26 114 114 LYS LYS A . n A 1 27 ASN 27 115 115 ASN ASN A . n A 1 28 TYR 28 116 116 TYR TYR A . n A 1 29 LEU 29 117 117 LEU LEU A . n A 1 30 SER 30 118 118 SER SER A . n A 1 31 MET 31 119 119 MET MET A . n A 1 32 ASN 32 120 120 ASN ASN A . n A 1 33 LYS 33 121 121 LYS LYS A . n A 1 34 TYR 34 122 122 TYR TYR A . n A 1 35 LYS 35 123 123 LYS LYS A . n A 1 36 VAL 36 124 124 VAL VAL A . n A 1 37 SER 37 125 125 SER SER A . n A 1 38 TYR 38 126 126 TYR TYR A . n A 1 39 LYS 39 127 127 LYS LYS A . n A 1 40 GLY 40 128 128 GLY GLY A . n A 1 41 PRO 41 129 129 PRO PRO A . n A 1 42 GLY 42 130 130 GLY GLY A . n A 1 43 PRO 43 131 131 PRO PRO A . n A 1 44 GLY 44 132 132 GLY GLY A . n A 1 45 ILE 45 133 133 ILE ILE A . n A 1 46 LYS 46 134 134 LYS LYS A . n A 1 47 PHE 47 135 135 PHE PHE A . n A 1 48 SER 48 136 136 SER SER A . n A 1 49 ALA 49 137 137 ALA ALA A . n A 1 50 GLU 50 138 138 GLU GLU A . n A 1 51 ALA 51 139 139 ALA ALA A . n A 1 52 LEU 52 140 140 LEU LEU A . n A 1 53 ARG 53 141 141 ARG ARG A . n A 1 54 CYS 54 142 142 CYS CYS A . n A 1 55 HIS 55 143 143 HIS HIS A . n A 1 56 LEU 56 144 144 LEU LEU A . n A 1 57 ARG 57 145 145 ARG ARG A . n A 1 58 ASP 58 146 146 ASP ASP A . n A 1 59 HIS 59 147 147 HIS HIS A . n A 1 60 VAL 60 148 148 VAL VAL A . n A 1 61 ASN 61 149 149 ASN ASN A . n A 1 62 VAL 62 150 150 VAL VAL A . n A 1 63 SER 63 151 151 SER SER A . n A 1 64 MET 64 152 152 MET MET A . n A 1 65 VAL 65 153 153 VAL VAL A . n A 1 66 GLU 66 154 154 GLU GLU A . n A 1 67 VAL 67 155 155 VAL VAL A . n A 1 68 THR 68 156 156 THR THR A . n A 1 69 ASP 69 157 157 ASP ASP A . n A 1 70 PHE 70 158 158 PHE PHE A . n A 1 71 PRO 71 159 159 PRO PRO A . n A 1 72 PHE 72 160 160 PHE PHE A . n A 1 73 ASN 73 161 161 ASN ASN A . n A 1 74 THR 74 162 162 THR THR A . n A 1 75 SER 75 163 163 SER SER A . n A 1 76 GLU 76 164 164 GLU GLU A . n A 1 77 TRP 77 165 165 TRP TRP A . n A 1 78 GLU 78 166 166 GLU GLU A . n A 1 79 GLY 79 167 167 GLY GLY A . n A 1 80 TYR 80 168 168 TYR TYR A . n A 1 81 LEU 81 169 169 LEU LEU A . n A 1 82 PRO 82 170 170 PRO PRO A . n A 1 83 LYS 83 171 171 LYS LYS A . n A 1 84 GLU 84 172 172 GLU GLU A . n A 1 85 SER 85 173 173 SER SER A . n A 1 86 ILE 86 174 174 ILE ILE A . n A 1 87 ARG 87 175 175 ARG ARG A . n A 1 88 THR 88 176 176 THR THR A . n A 1 89 LYS 89 177 177 LYS LYS A . n A 1 90 ALA 90 178 178 ALA ALA A . n A 1 91 GLY 91 179 179 GLY GLY A . n A 1 92 PRO 92 180 180 PRO PRO A . n A 1 93 TRP 93 181 181 TRP TRP A . n A 1 94 GLY 94 182 182 GLY GLY A . n A 1 95 ARG 95 183 183 ARG ARG A . n A 1 96 CYS 96 184 184 CYS CYS A . n A 1 97 ALA 97 185 185 ALA ALA A . n A 1 98 VAL 98 186 186 VAL VAL A . n A 1 99 VAL 99 187 187 VAL VAL A . n A 1 100 SER 100 188 188 SER SER A . n A 1 101 SER 101 189 189 SER SER A . n A 1 102 ALA 102 190 190 ALA ALA A . n A 1 103 GLY 103 191 191 GLY GLY A . n A 1 104 SER 104 192 192 SER SER A . n A 1 105 LEU 105 193 193 LEU LEU A . n A 1 106 LYS 106 194 194 LYS LYS A . n A 1 107 SER 107 195 195 SER SER A . n A 1 108 SER 108 196 196 SER SER A . n A 1 109 GLN 109 197 197 GLN GLN A . n A 1 110 LEU 110 198 198 LEU LEU A . n A 1 111 GLY 111 199 199 GLY GLY A . n A 1 112 ARG 112 200 200 ARG ARG A . n A 1 113 GLU 113 201 201 GLU GLU A . n A 1 114 ILE 114 202 202 ILE ILE A . n A 1 115 ASP 115 203 203 ASP ASP A . n A 1 116 ASP 116 204 204 ASP ASP A . n A 1 117 HIS 117 205 205 HIS HIS A . n A 1 118 ASP 118 206 206 ASP ASP A . n A 1 119 ALA 119 207 207 ALA ALA A . n A 1 120 VAL 120 208 208 VAL VAL A . n A 1 121 LEU 121 209 209 LEU LEU A . n A 1 122 ARG 122 210 210 ARG ARG A . n A 1 123 PHE 123 211 211 PHE PHE A . n A 1 124 ASN 124 212 212 ASN ASN A . n A 1 125 GLY 125 213 213 GLY GLY A . n A 1 126 ALA 126 214 214 ALA ALA A . n A 1 127 PRO 127 215 215 PRO PRO A . n A 1 128 THR 128 216 216 THR THR A . n A 1 129 ALA 129 217 217 ALA ALA A . n A 1 130 ASN 130 218 218 ASN ASN A . n A 1 131 PHE 131 219 219 PHE PHE A . n A 1 132 GLN 132 220 220 GLN GLN A . n A 1 133 GLN 133 221 221 GLN GLN A . n A 1 134 ASP 134 222 222 ASP ASP A . n A 1 135 VAL 135 223 223 VAL VAL A . n A 1 136 GLY 136 224 224 GLY GLY A . n A 1 137 THR 137 225 225 THR THR A . n A 1 138 LYS 138 226 226 LYS LYS A . n A 1 139 THR 139 227 227 THR THR A . n A 1 140 THR 140 228 228 THR THR A . n A 1 141 ILE 141 229 229 ILE ILE A . n A 1 142 ARG 142 230 230 ARG ARG A . n A 1 143 LEU 143 231 231 LEU LEU A . n A 1 144 MET 144 232 232 MET MET A . n A 1 145 ASN 145 233 233 ASN ASN A . n A 1 146 SER 146 234 234 SER SER A . n A 1 147 GLN 147 235 235 GLN GLN A . n A 1 148 LEU 148 236 236 LEU LEU A . n A 1 149 VAL 149 237 237 VAL VAL A . n A 1 150 THR 150 238 238 THR THR A . n A 1 151 THR 151 239 239 THR THR A . n A 1 152 GLU 152 240 240 GLU GLU A . n A 1 153 LYS 153 241 241 LYS LYS A . n A 1 154 ARG 154 242 242 ARG ARG A . n A 1 155 PHE 155 243 243 PHE PHE A . n A 1 156 LEU 156 244 244 LEU LEU A . n A 1 157 LYS 157 245 245 LYS LYS A . n A 1 158 ASP 158 246 246 ASP ASP A . n A 1 159 SER 159 247 247 SER SER A . n A 1 160 LEU 160 248 248 LEU LEU A . n A 1 161 TYR 161 249 249 TYR TYR A . n A 1 162 ASN 162 250 250 ASN ASN A . n A 1 163 GLU 163 251 251 GLU GLU A . n A 1 164 GLY 164 252 252 GLY GLY A . n A 1 165 ILE 165 253 253 ILE ILE A . n A 1 166 LEU 166 254 254 LEU LEU A . n A 1 167 ILE 167 255 255 ILE ILE A . n A 1 168 VAL 168 256 256 VAL VAL A . n A 1 169 TRP 169 257 257 TRP TRP A . n A 1 170 ASP 170 258 258 ASP ASP A . n A 1 171 PRO 171 259 259 PRO PRO A . n A 1 172 SER 172 260 260 SER SER A . n A 1 173 VAL 173 261 261 VAL VAL A . n A 1 174 TYR 174 262 262 TYR TYR A . n A 1 175 HIS 175 263 263 HIS HIS A . n A 1 176 SER 176 264 264 SER SER A . n A 1 177 ASP 177 265 265 ASP ASP A . n A 1 178 ILE 178 266 266 ILE ILE A . n A 1 179 PRO 179 267 267 PRO PRO A . n A 1 180 LYS 180 268 268 LYS LYS A . n A 1 181 TRP 181 269 269 TRP TRP A . n A 1 182 TYR 182 270 270 TYR TYR A . n A 1 183 GLN 183 271 271 GLN GLN A . n A 1 184 ASN 184 272 272 ASN ASN A . n A 1 185 PRO 185 273 273 PRO PRO A . n A 1 186 ASP 186 274 274 ASP ASP A . n A 1 187 TYR 187 275 275 TYR TYR A . n A 1 188 ASN 188 276 276 ASN ASN A . n A 1 189 PHE 189 277 277 PHE PHE A . n A 1 190 PHE 190 278 278 PHE PHE A . n A 1 191 ASN 191 279 279 ASN ASN A . n A 1 192 ASN 192 280 280 ASN ASN A . n A 1 193 TYR 193 281 281 TYR TYR A . n A 1 194 LYS 194 282 282 LYS LYS A . n A 1 195 THR 195 283 283 THR THR A . n A 1 196 TYR 196 284 284 TYR TYR A . n A 1 197 ARG 197 285 285 ARG ARG A . n A 1 198 LYS 198 286 286 LYS LYS A . n A 1 199 LEU 199 287 287 LEU LEU A . n A 1 200 HIS 200 288 288 HIS HIS A . n A 1 201 PRO 201 289 289 PRO PRO A . n A 1 202 ASN 202 290 290 ASN ASN A . n A 1 203 GLN 203 291 291 GLN GLN A . n A 1 204 PRO 204 292 292 PRO PRO A . n A 1 205 PHE 205 293 293 PHE PHE A . n A 1 206 TYR 206 294 294 TYR TYR A . n A 1 207 ILE 207 295 295 ILE ILE A . n A 1 208 LEU 208 296 296 LEU LEU A . n A 1 209 LYS 209 297 297 LYS LYS A . n A 1 210 PRO 210 298 298 PRO PRO A . n A 1 211 GLN 211 299 299 GLN GLN A . n A 1 212 MET 212 300 300 MET MET A . n A 1 213 PRO 213 301 301 PRO PRO A . n A 1 214 TRP 214 302 302 TRP TRP A . n A 1 215 GLU 215 303 303 GLU GLU A . n A 1 216 LEU 216 304 304 LEU LEU A . n A 1 217 TRP 217 305 305 TRP TRP A . n A 1 218 ASP 218 306 306 ASP ASP A . n A 1 219 ILE 219 307 307 ILE ILE A . n A 1 220 LEU 220 308 308 LEU LEU A . n A 1 221 GLN 221 309 309 GLN GLN A . n A 1 222 GLU 222 310 310 GLU GLU A . n A 1 223 ILE 223 311 311 ILE ILE A . n A 1 224 SER 224 312 312 SER SER A . n A 1 225 PRO 225 313 313 PRO PRO A . n A 1 226 GLU 226 314 314 GLU GLU A . n A 1 227 GLU 227 315 315 GLU GLU A . n A 1 228 ILE 228 316 316 ILE ILE A . n A 1 229 GLN 229 317 317 GLN GLN A . n A 1 230 PRO 230 318 318 PRO PRO A . n A 1 231 ASN 231 319 319 ASN ASN A . n A 1 232 PRO 232 320 320 PRO PRO A . n A 1 233 PRO 233 321 321 PRO PRO A . n A 1 234 SER 234 322 322 SER SER A . n A 1 235 SER 235 323 323 SER SER A . n A 1 236 GLY 236 324 324 GLY GLY A . n A 1 237 MET 237 325 325 MET MET A . n A 1 238 LEU 238 326 326 LEU LEU A . n A 1 239 GLY 239 327 327 GLY GLY A . n A 1 240 ILE 240 328 328 ILE ILE A . n A 1 241 ILE 241 329 329 ILE ILE A . n A 1 242 ILE 242 330 330 ILE ILE A . n A 1 243 MET 243 331 331 MET MET A . n A 1 244 MET 244 332 332 MET MET A . n A 1 245 THR 245 333 333 THR THR A . n A 1 246 LEU 246 334 334 LEU LEU A . n A 1 247 CYS 247 335 335 CYS CYS A . n A 1 248 ASP 248 336 336 ASP ASP A . n A 1 249 GLN 249 337 337 GLN GLN A . n A 1 250 VAL 250 338 338 VAL VAL A . n A 1 251 ASP 251 339 339 ASP ASP A . n A 1 252 ILE 252 340 340 ILE ILE A . n A 1 253 TYR 253 341 341 TYR TYR A . n A 1 254 GLU 254 342 342 GLU GLU A . n A 1 255 PHE 255 343 343 PHE PHE A . n A 1 256 LEU 256 344 344 LEU LEU A . n A 1 257 PRO 257 345 345 PRO PRO A . n A 1 258 SER 258 346 346 SER SER A . n A 1 259 LYS 259 347 347 LYS LYS A . n A 1 260 ARG 260 348 348 ARG ARG A . n A 1 261 LYS 261 349 349 LYS LYS A . n A 1 262 THR 262 350 350 THR THR A . n A 1 263 ASP 263 351 351 ASP ASP A . n A 1 264 VAL 264 352 352 VAL VAL A . n A 1 265 CYS 265 353 353 CYS CYS A . n A 1 266 TYR 266 354 354 TYR TYR A . n A 1 267 TYR 267 355 355 TYR TYR A . n A 1 268 TYR 268 356 356 TYR TYR A . n A 1 269 GLN 269 357 357 GLN GLN A . n A 1 270 LYS 270 358 358 LYS LYS A . n A 1 271 PHE 271 359 359 PHE PHE A . n A 1 272 PHE 272 360 360 PHE PHE A . n A 1 273 ASP 273 361 361 ASP ASP A . n A 1 274 SER 274 362 362 SER SER A . n A 1 275 ALA 275 363 363 ALA ALA A . n A 1 276 CYS 276 364 364 CYS CYS A . n A 1 277 THR 277 365 365 THR THR A . n A 1 278 MET 278 366 366 MET MET A . n A 1 279 GLY 279 367 367 GLY GLY A . n A 1 280 ALA 280 368 368 ALA ALA A . n A 1 281 TYR 281 369 369 TYR TYR A . n A 1 282 HIS 282 370 370 HIS HIS A . n A 1 283 PRO 283 371 371 PRO PRO A . n A 1 284 LEU 284 372 372 LEU LEU A . n A 1 285 LEU 285 373 373 LEU LEU A . n A 1 286 TYR 286 374 374 TYR TYR A . n A 1 287 GLU 287 375 375 GLU GLU A . n A 1 288 LYS 288 376 376 LYS LYS A . n A 1 289 ASN 289 377 377 ASN ASN A . n A 1 290 LEU 290 378 378 LEU LEU A . n A 1 291 VAL 291 379 379 VAL VAL A . n A 1 292 LYS 292 380 380 LYS LYS A . n A 1 293 HIS 293 381 381 HIS HIS A . n A 1 294 LEU 294 382 382 LEU LEU A . n A 1 295 ASN 295 383 383 ASN ASN A . n A 1 296 GLN 296 384 384 GLN GLN A . n A 1 297 GLY 297 385 385 GLY GLY A . n A 1 298 THR 298 386 386 THR THR A . n A 1 299 ASP 299 387 387 ASP ASP A . n A 1 300 GLU 300 388 388 GLU GLU A . n A 1 301 ASP 301 389 389 ASP ASP A . n A 1 302 ILE 302 390 390 ILE ILE A . n A 1 303 TYR 303 391 391 TYR TYR A . n A 1 304 LEU 304 392 392 LEU LEU A . n A 1 305 LEU 305 393 393 LEU LEU A . n A 1 306 GLY 306 394 394 GLY GLY A . n A 1 307 LYS 307 395 395 LYS LYS A . n A 1 308 ALA 308 396 396 ALA ALA A . n A 1 309 THR 309 397 397 THR THR A . n A 1 310 LEU 310 398 398 LEU LEU A . n A 1 311 PRO 311 399 399 PRO PRO A . n A 1 312 GLY 312 400 400 GLY GLY A . n A 1 313 PHE 313 401 401 PHE PHE A . n A 1 314 ARG 314 402 402 ARG ARG A . n A 1 315 THR 315 403 403 THR THR A . n A 1 316 ILE 316 404 404 ILE ILE A . n A 1 317 HIS 317 405 405 HIS HIS A . n A 1 318 CYS 318 406 406 CYS CYS 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 1 501 450 NAG NAG A . C 2 NAG 2 502 451 NAG NAG A . D 3 BMA 3 503 452 BMA BMA A . E 4 MAN 4 504 453 MAN MAN A . F 2 NAG 5 505 454 NAG NAG A . G 5 GAL 6 506 455 GAL GAL A . H 4 MAN 7 507 456 MAN MAN A . I 2 NAG 8 508 457 NAG NAG A . J 5 GAL 9 509 458 GAL GAL A . K 6 CTN 1 510 500 CTN C A . L 7 PO4 1 511 501 PO4 PO4 A . M 8 HOH 1 601 1 HOH HOH A . M 8 HOH 2 602 2 HOH HOH A . M 8 HOH 3 603 3 HOH HOH A . M 8 HOH 4 604 4 HOH HOH A . M 8 HOH 5 605 5 HOH HOH A . M 8 HOH 6 606 6 HOH HOH A . M 8 HOH 7 607 7 HOH HOH A . M 8 HOH 8 608 8 HOH HOH A . M 8 HOH 9 609 9 HOH HOH A . M 8 HOH 10 610 10 HOH HOH A . M 8 HOH 11 611 11 HOH HOH A . M 8 HOH 12 612 13 HOH HOH A . M 8 HOH 13 613 14 HOH HOH A . M 8 HOH 14 614 15 HOH HOH A . M 8 HOH 15 615 16 HOH HOH A . M 8 HOH 16 616 17 HOH HOH A . M 8 HOH 17 617 18 HOH HOH A . M 8 HOH 18 618 19 HOH HOH A . M 8 HOH 19 619 20 HOH HOH A . M 8 HOH 20 620 21 HOH HOH A . M 8 HOH 21 621 22 HOH HOH A . M 8 HOH 22 622 23 HOH HOH A . M 8 HOH 23 623 24 HOH HOH A . M 8 HOH 24 624 25 HOH HOH A . M 8 HOH 25 625 26 HOH HOH A . M 8 HOH 26 626 27 HOH HOH A . M 8 HOH 27 627 28 HOH HOH A . M 8 HOH 28 628 29 HOH HOH A . M 8 HOH 29 629 30 HOH HOH A . M 8 HOH 30 630 32 HOH HOH A . M 8 HOH 31 631 33 HOH HOH A . M 8 HOH 32 632 34 HOH HOH A . M 8 HOH 33 633 35 HOH HOH A . M 8 HOH 34 634 36 HOH HOH A . M 8 HOH 35 635 37 HOH HOH A . M 8 HOH 36 636 38 HOH HOH A . M 8 HOH 37 637 39 HOH HOH A . M 8 HOH 38 638 40 HOH HOH A . M 8 HOH 39 639 41 HOH HOH A . M 8 HOH 40 640 42 HOH HOH A . M 8 HOH 41 641 43 HOH HOH A . # _pdbx_struct_mod_residue.id 1 _pdbx_struct_mod_residue.label_asym_id A _pdbx_struct_mod_residue.label_comp_id ASN _pdbx_struct_mod_residue.label_seq_id 61 _pdbx_struct_mod_residue.auth_asym_id A _pdbx_struct_mod_residue.auth_comp_id ASN _pdbx_struct_mod_residue.auth_seq_id 149 _pdbx_struct_mod_residue.PDB_ins_code ? _pdbx_struct_mod_residue.parent_comp_id ASN _pdbx_struct_mod_residue.details 'GLYCOSYLATION SITE' # _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,E,F,G,H,I,J,K,L,M # _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 2013-07-31 2 'Structure model' 1 1 2013-08-28 3 'Structure model' 1 2 2017-11-15 # _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' 'Refinement description' # _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 software # loop_ _pdbx_refine_tls.pdbx_refine_id _pdbx_refine_tls.id _pdbx_refine_tls.details _pdbx_refine_tls.method _pdbx_refine_tls.origin_x _pdbx_refine_tls.origin_y _pdbx_refine_tls.origin_z _pdbx_refine_tls.T[1][1] _pdbx_refine_tls.T[2][2] _pdbx_refine_tls.T[3][3] _pdbx_refine_tls.T[1][2] _pdbx_refine_tls.T[1][3] _pdbx_refine_tls.T[2][3] _pdbx_refine_tls.L[1][1] _pdbx_refine_tls.L[2][2] _pdbx_refine_tls.L[3][3] _pdbx_refine_tls.L[1][2] _pdbx_refine_tls.L[1][3] _pdbx_refine_tls.L[2][3] _pdbx_refine_tls.S[1][1] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[2][2] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] _pdbx_refine_tls.S[3][3] 'X-RAY DIFFRACTION' 1 ? refined 2.3395 44.8877 32.6420 0.8266 0.3110 0.3112 0.0185 0.0431 -0.0073 3.6997 4.0448 8.6045 -1.0168 -1.6255 3.1222 -0.2335 -0.0938 -0.1270 1.0391 0.2734 -0.0865 1.4709 0.2644 -0.0626 'X-RAY DIFFRACTION' 2 ? refined -7.8249 25.7520 9.7658 0.9100 1.1090 0.9239 -0.1058 -0.2386 -0.1895 1.2595 0.4733 1.2789 -0.3638 -1.0275 -0.0903 1.6800 -0.3088 -0.9208 0.2395 0.0680 -1.0318 1.4399 1.0577 -1.2164 # loop_ _pdbx_refine_tls_group.pdbx_refine_id _pdbx_refine_tls_group.id _pdbx_refine_tls_group.refine_tls_id _pdbx_refine_tls_group.beg_auth_asym_id _pdbx_refine_tls_group.beg_auth_seq_id _pdbx_refine_tls_group.end_auth_asym_id _pdbx_refine_tls_group.end_auth_seq_id _pdbx_refine_tls_group.selection_details _pdbx_refine_tls_group.beg_label_asym_id _pdbx_refine_tls_group.beg_label_seq_id _pdbx_refine_tls_group.end_label_asym_id _pdbx_refine_tls_group.end_label_seq_id _pdbx_refine_tls_group.selection 'X-RAY DIFFRACTION' 1 1 A 89 A 406 'CHAIN A AND (RESID 89:406 )' ? ? ? ? ? 'X-RAY DIFFRACTION' 2 2 A 501 A 509 'CHAIN A AND (RESID 501:509 )' ? ? ? ? ? # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal SHARP phasing . ? 1 PHENIX refinement '(phenix.refine: dev_1327)' ? 2 XDS 'data reduction' . ? 3 SADABS 'data scaling' . ? 4 # _pdbx_validate_close_contact.id 1 _pdbx_validate_close_contact.PDB_model_num 1 _pdbx_validate_close_contact.auth_atom_id_1 ND2 _pdbx_validate_close_contact.auth_asym_id_1 A _pdbx_validate_close_contact.auth_comp_id_1 ASN _pdbx_validate_close_contact.auth_seq_id_1 149 _pdbx_validate_close_contact.PDB_ins_code_1 ? _pdbx_validate_close_contact.label_alt_id_1 ? _pdbx_validate_close_contact.auth_atom_id_2 C2 _pdbx_validate_close_contact.auth_asym_id_2 A _pdbx_validate_close_contact.auth_comp_id_2 NAG _pdbx_validate_close_contact.auth_seq_id_2 501 _pdbx_validate_close_contact.PDB_ins_code_2 ? _pdbx_validate_close_contact.label_alt_id_2 ? _pdbx_validate_close_contact.dist 2.17 # _pdbx_validate_rmsd_angle.id 1 _pdbx_validate_rmsd_angle.PDB_model_num 1 _pdbx_validate_rmsd_angle.auth_atom_id_1 CA _pdbx_validate_rmsd_angle.auth_asym_id_1 A _pdbx_validate_rmsd_angle.auth_comp_id_1 CYS _pdbx_validate_rmsd_angle.auth_seq_id_1 142 _pdbx_validate_rmsd_angle.PDB_ins_code_1 ? _pdbx_validate_rmsd_angle.label_alt_id_1 ? _pdbx_validate_rmsd_angle.auth_atom_id_2 CB _pdbx_validate_rmsd_angle.auth_asym_id_2 A _pdbx_validate_rmsd_angle.auth_comp_id_2 CYS _pdbx_validate_rmsd_angle.auth_seq_id_2 142 _pdbx_validate_rmsd_angle.PDB_ins_code_2 ? _pdbx_validate_rmsd_angle.label_alt_id_2 ? _pdbx_validate_rmsd_angle.auth_atom_id_3 SG _pdbx_validate_rmsd_angle.auth_asym_id_3 A _pdbx_validate_rmsd_angle.auth_comp_id_3 CYS _pdbx_validate_rmsd_angle.auth_seq_id_3 142 _pdbx_validate_rmsd_angle.PDB_ins_code_3 ? _pdbx_validate_rmsd_angle.label_alt_id_3 ? _pdbx_validate_rmsd_angle.angle_value 122.38 _pdbx_validate_rmsd_angle.angle_target_value 114.20 _pdbx_validate_rmsd_angle.angle_deviation 8.18 _pdbx_validate_rmsd_angle.angle_standard_deviation 1.10 _pdbx_validate_rmsd_angle.linker_flag 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 PRO A 129 ? ? -34.20 -26.95 2 1 ASN A 212 ? ? 46.02 -121.59 3 1 ASN A 218 ? ? 77.39 -2.14 4 1 PRO A 318 ? ? -81.46 46.30 5 1 LYS A 349 ? ? -34.85 123.82 6 1 ASP A 361 ? ? -163.94 111.57 7 1 ALA A 368 ? ? -139.59 -78.99 8 1 PRO A 371 ? ? -78.43 46.38 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 BETA-D-MANNOSE BMA 4 ALPHA-D-MANNOSE MAN 5 BETA-D-GALACTOSE GAL 6 '4-AMINO-1-BETA-D-RIBOFURANOSYL-2(1H)-PYRIMIDINONE' CTN 7 'PHOSPHATE ION' PO4 8 water HOH #