data_4OPB # _entry.id 4OPB # _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 4OPB RCSB RCSB084780 WWPDB D_1000084780 # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4OPB _pdbx_database_status.recvd_initial_deposition_date 2014-02-05 _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 'Lo Leggio, L.' 1 'Frandsen, K.H.' 2 'Davies, G.J.' 3 'Dupree, P.' 4 'Walton, P.' 5 'Henrissat, B.' 6 'Stringer, M.' 7 'Tovborg, M.' 8 'De Maria, L.' 9 'Johansen, K.S.' 10 # _citation.id primary _citation.title 'Structure and boosting activity of a starch-degrading lytic polysaccharide monooxygenase.' _citation.journal_abbrev 'Nat Commun' _citation.journal_volume 6 _citation.page_first 5961 _citation.page_last 5961 _citation.year 2015 _citation.journal_id_ASTM ? _citation.country UK _citation.journal_id_ISSN 2041-1723 _citation.journal_id_CSD ? _citation.book_publisher ? _citation.pdbx_database_id_PubMed 25608804 _citation.pdbx_database_id_DOI 10.1038/ncomms6961 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Lo Leggio, L.' 1 primary 'Simmons, T.J.' 2 primary 'Poulsen, J.C.' 3 primary 'Frandsen, K.E.' 4 primary 'Hemsworth, G.R.' 5 primary 'Stringer, M.A.' 6 primary 'von Freiesleben, P.' 7 primary 'Tovborg, M.' 8 primary 'Johansen, K.S.' 9 primary 'De Maria, L.' 10 primary 'Harris, P.V.' 11 primary 'Soong, C.L.' 12 primary 'Dupree, P.' 13 primary 'Tryfona, T.' 14 primary 'Lenfant, N.' 15 primary 'Henrissat, B.' 16 primary 'Davies, G.J.' 17 primary 'Walton, P.H.' 18 # _cell.entry_id 4OPB _cell.length_a 46.560 _cell.length_b 61.600 _cell.length_c 73.160 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 4 _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 4OPB _symmetry.space_group_name_H-M 'P 21 21 21' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 19 _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 'Predicted protein' 25691.057 1 ? ? 'UNP RESIDUES 47-279' ? 2 non-polymer syn 'COPPER (II) ION' 63.546 1 ? ? ? ? 3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 1 ? ? ? ? 4 non-polymer syn 'ZINC ION' 65.409 4 ? ? ? ? 5 non-polymer syn 'ISOPROPYL ALCOHOL' 60.095 2 ? ? ? ? 6 non-polymer syn GLYCEROL 92.094 7 ? ? ? ? 7 non-polymer syn 'ACETATE ION' 59.044 2 ? ? ? ? 8 water nat water 18.015 212 ? ? ? ? # _entity_poly.entity_id 1 _entity_poly.type 'polypeptide(L)' _entity_poly.nstd_linkage no _entity_poly.nstd_monomer yes _entity_poly.pdbx_seq_one_letter_code ;(HIC)GYMYIPSSRTRLGHEAGIDSCPECAILEPVSSWPDLDAAPVGRSGPCGYNARDSIDYNQPTTNWGSDAVQSYSPG EEIEVQWCVDHNGDHGGMFTYRICQDQSIVDKFLDPSYLPTNDEKQAAEDCFDAGLLPCTDVSGQECGYSADCTEGEACW RNDWFTCNGFEASDRPKCQGVDNAELNSCYTSIAGGYTVTKKVKLPEYTSNHTLISFKWNSFQTGQIYLSCADIAIQ ; _entity_poly.pdbx_seq_one_letter_code_can ;HGYMYIPSSRTRLGHEAGIDSCPECAILEPVSSWPDLDAAPVGRSGPCGYNARDSIDYNQPTTNWGSDAVQSYSPGEEIE VQWCVDHNGDHGGMFTYRICQDQSIVDKFLDPSYLPTNDEKQAAEDCFDAGLLPCTDVSGQECGYSADCTEGEACWRNDW FTCNGFEASDRPKCQGVDNAELNSCYTSIAGGYTVTKKVKLPEYTSNHTLISFKWNSFQTGQIYLSCADIAIQ ; _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 HIC n 1 2 GLY n 1 3 TYR n 1 4 MET n 1 5 TYR n 1 6 ILE n 1 7 PRO n 1 8 SER n 1 9 SER n 1 10 ARG n 1 11 THR n 1 12 ARG n 1 13 LEU n 1 14 GLY n 1 15 HIS n 1 16 GLU n 1 17 ALA n 1 18 GLY n 1 19 ILE n 1 20 ASP n 1 21 SER n 1 22 CYS n 1 23 PRO n 1 24 GLU n 1 25 CYS n 1 26 ALA n 1 27 ILE n 1 28 LEU n 1 29 GLU n 1 30 PRO n 1 31 VAL n 1 32 SER n 1 33 SER n 1 34 TRP n 1 35 PRO n 1 36 ASP n 1 37 LEU n 1 38 ASP n 1 39 ALA n 1 40 ALA n 1 41 PRO n 1 42 VAL n 1 43 GLY n 1 44 ARG n 1 45 SER n 1 46 GLY n 1 47 PRO n 1 48 CYS n 1 49 GLY n 1 50 TYR n 1 51 ASN n 1 52 ALA n 1 53 ARG n 1 54 ASP n 1 55 SER n 1 56 ILE n 1 57 ASP n 1 58 TYR n 1 59 ASN n 1 60 GLN n 1 61 PRO n 1 62 THR n 1 63 THR n 1 64 ASN n 1 65 TRP n 1 66 GLY n 1 67 SER n 1 68 ASP n 1 69 ALA n 1 70 VAL n 1 71 GLN n 1 72 SER n 1 73 TYR n 1 74 SER n 1 75 PRO n 1 76 GLY n 1 77 GLU n 1 78 GLU n 1 79 ILE n 1 80 GLU n 1 81 VAL n 1 82 GLN n 1 83 TRP n 1 84 CYS n 1 85 VAL n 1 86 ASP n 1 87 HIS n 1 88 ASN n 1 89 GLY n 1 90 ASP n 1 91 HIS n 1 92 GLY n 1 93 GLY n 1 94 MET n 1 95 PHE n 1 96 THR n 1 97 TYR n 1 98 ARG n 1 99 ILE n 1 100 CYS n 1 101 GLN n 1 102 ASP n 1 103 GLN n 1 104 SER n 1 105 ILE n 1 106 VAL n 1 107 ASP n 1 108 LYS n 1 109 PHE n 1 110 LEU n 1 111 ASP n 1 112 PRO n 1 113 SER n 1 114 TYR n 1 115 LEU n 1 116 PRO n 1 117 THR n 1 118 ASN n 1 119 ASP n 1 120 GLU n 1 121 LYS n 1 122 GLN n 1 123 ALA n 1 124 ALA n 1 125 GLU n 1 126 ASP n 1 127 CYS n 1 128 PHE n 1 129 ASP n 1 130 ALA n 1 131 GLY n 1 132 LEU n 1 133 LEU n 1 134 PRO n 1 135 CYS n 1 136 THR n 1 137 ASP n 1 138 VAL n 1 139 SER n 1 140 GLY n 1 141 GLN n 1 142 GLU n 1 143 CYS n 1 144 GLY n 1 145 TYR n 1 146 SER n 1 147 ALA n 1 148 ASP n 1 149 CYS n 1 150 THR n 1 151 GLU n 1 152 GLY n 1 153 GLU n 1 154 ALA n 1 155 CYS n 1 156 TRP n 1 157 ARG n 1 158 ASN n 1 159 ASP n 1 160 TRP n 1 161 PHE n 1 162 THR n 1 163 CYS n 1 164 ASN n 1 165 GLY n 1 166 PHE n 1 167 GLU n 1 168 ALA n 1 169 SER n 1 170 ASP n 1 171 ARG n 1 172 PRO n 1 173 LYS n 1 174 CYS n 1 175 GLN n 1 176 GLY n 1 177 VAL n 1 178 ASP n 1 179 ASN n 1 180 ALA n 1 181 GLU n 1 182 LEU n 1 183 ASN n 1 184 SER n 1 185 CYS n 1 186 TYR n 1 187 THR n 1 188 SER n 1 189 ILE n 1 190 ALA n 1 191 GLY n 1 192 GLY n 1 193 TYR n 1 194 THR n 1 195 VAL n 1 196 THR n 1 197 LYS n 1 198 LYS n 1 199 VAL n 1 200 LYS n 1 201 LEU n 1 202 PRO n 1 203 GLU n 1 204 TYR n 1 205 THR n 1 206 SER n 1 207 ASN n 1 208 HIS n 1 209 THR n 1 210 LEU n 1 211 ILE n 1 212 SER n 1 213 PHE n 1 214 LYS n 1 215 TRP n 1 216 ASN n 1 217 SER n 1 218 PHE n 1 219 GLN n 1 220 THR n 1 221 GLY n 1 222 GLN n 1 223 ILE n 1 224 TYR n 1 225 LEU n 1 226 SER n 1 227 CYS n 1 228 ALA n 1 229 ASP n 1 230 ILE n 1 231 ALA n 1 232 ILE n 1 233 GLN 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 'Yellow koji mold' _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene AO090701000246 _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain 'ATCC 42149 / RIB 40' _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 'Aspergillus oryzae' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 510516 _entity_src_gen.pdbx_gene_src_variant ? _entity_src_gen.pdbx_gene_src_cell_line ? _entity_src_gen.pdbx_gene_src_atcc ? _entity_src_gen.pdbx_gene_src_organ ? _entity_src_gen.pdbx_gene_src_organelle ? _entity_src_gen.pdbx_gene_src_cell ? _entity_src_gen.pdbx_gene_src_cellular_location ? _entity_src_gen.host_org_common_name ? _entity_src_gen.pdbx_host_org_scientific_name 'Aspergillus oryzae' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 5062 _entity_src_gen.host_org_genus ? _entity_src_gen.pdbx_host_org_gene ? _entity_src_gen.pdbx_host_org_organ ? _entity_src_gen.host_org_species ? _entity_src_gen.pdbx_host_org_tissue ? _entity_src_gen.pdbx_host_org_tissue_fraction ? _entity_src_gen.pdbx_host_org_strain ? _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line ? _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type ? _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name ? _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code Q2U8Y3_ASPOR _struct_ref.pdbx_db_accession Q2U8Y3 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;HGYMYIPSSRTRLGHEAGIDSCPECAILEPVSSWPDLDAAPVGRSGPCGYNARDSIDYNQPTTNWGSDAVQSYSPGEEIE VQWCVDHNGDHGGMFTYRICQDQSIVDKFLDPSYLPTNDEKQAAEDCFDAGLLPCTDVSGQECGYSADCTEGEACWRNDW FTCNGFEASDRPKCQGVDNAELNSCYTSIAGGYTVTKKVKLPEYTSNHTLISFKWNSFQTGQIYLSCADIAIQ ; _struct_ref.pdbx_align_begin 47 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 4OPB _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 233 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession Q2U8Y3 _struct_ref_seq.db_align_beg 47 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 279 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 1 _struct_ref_seq.pdbx_auth_seq_align_end 233 # 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 ACT non-polymer . 'ACETATE ION' ? 'C2 H3 O2 -1' 59.044 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 CU non-polymer . 'COPPER (II) ION' ? 'Cu 2' 63.546 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 GOL non-polymer . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3' 92.094 HIC 'L-peptide linking' n 4-METHYL-HISTIDINE ? 'C7 H11 N3 O2' 169.181 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 IPA non-polymer . 'ISOPROPYL ALCOHOL' 2-PROPANOL 'C3 H8 O' 60.095 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 ZN non-polymer . 'ZINC ION' ? 'Zn 2' 65.409 # _exptl.entry_id 4OPB _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.04 _exptl_crystal.density_percent_sol 39.76 _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 298 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 4.6 _exptl_crystal_grow.pdbx_details ;0.14M calcium chloride, 0.07M sodium acetate pH 4.6, 14 %v/v isopropanol, 30% v/v glycerol, VAPOR DIFFUSION, SITTING DROP, temperature 298K ; _exptl_crystal_grow.pdbx_pH_range ? # loop_ _diffrn.id _diffrn.ambient_temp _diffrn.ambient_temp_details _diffrn.crystal_id 1 100 ? 1 2 100 ? 1 # loop_ _diffrn_detector.diffrn_id _diffrn_detector.detector _diffrn_detector.type _diffrn_detector.pdbx_collection_date _diffrn_detector.details 1 CCD 'MAR CCD 165 mm' 2013-05-08 ? 2 ? ? 2013-05-08 ? # loop_ _diffrn_radiation.diffrn_id _diffrn_radiation.wavelength_id _diffrn_radiation.pdbx_monochromatic_or_laue_m_l _diffrn_radiation.monochromator _diffrn_radiation.pdbx_diffrn_protocol _diffrn_radiation.pdbx_scattering_type 1 1 M 'Bent Si (111) crystal, horizontally focusing' 'SINGLE WAVELENGTH' x-ray 2 1 M ? 'SINGLE WAVELENGTH' x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.037 _diffrn_radiation_wavelength.wt 1.0 # loop_ _diffrn_source.diffrn_id _diffrn_source.source _diffrn_source.type _diffrn_source.pdbx_synchrotron_site _diffrn_source.pdbx_synchrotron_beamline _diffrn_source.pdbx_wavelength _diffrn_source.pdbx_wavelength_list 1 SYNCHROTRON 'MAX II BEAMLINE I911-2' 'MAX II' I911-2 ? 1.037 2 SYNCHROTRON 'ESRF BEAMLINE ID23-1' ESRF ID23-1 ? ? # _reflns.entry_id 4OPB _reflns.observed_criterion_sigma_I 0 _reflns.observed_criterion_sigma_F 0 _reflns.d_resolution_low 30 _reflns.d_resolution_high 1.5 _reflns.number_obs 32929 _reflns.number_all 32929 _reflns.percent_possible_obs 99.2 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI ? _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy ? _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 1.50 _reflns_shell.d_res_low 1.59 _reflns_shell.percent_possible_all 98.7 _reflns_shell.Rmerge_I_obs ? _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs ? _reflns_shell.pdbx_redundancy ? _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all ? _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 4OPB _refine.ls_number_reflns_obs 32929 _refine.ls_number_reflns_all 32929 _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 0 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 30 _refine.ls_d_res_high 1.50 _refine.ls_percent_reflns_obs 99.16 _refine.ls_R_factor_obs 0.12107 _refine.ls_R_factor_all 0.12107 _refine.ls_R_factor_R_work 0.11932 _refine.ls_R_factor_R_free 0.16997 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 3.4 _refine.ls_number_reflns_R_free 1165 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.977 _refine.correlation_coeff_Fo_to_Fc_free 0.962 _refine.B_iso_mean 15.027 _refine.aniso_B[1][1] 2.34 _refine.aniso_B[2][2] -2.18 _refine.aniso_B[3][3] -0.16 _refine.aniso_B[1][2] -0.00 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details MASK _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.20 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details ;(1) HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. (2) AUTHORS ATATE THAT THE LOOP CONSISTING OF RES 165-171 IS DISORDERED (POOR DENSITY) AND WAS MODELLED IN TWO CONFORMATIONS ; _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct SAD _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.069 _refine.pdbx_overall_ESU_R_Free 0.066 _refine.overall_SU_ML 0.050 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 2.846 _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 1799 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 77 _refine_hist.number_atoms_solvent 212 _refine_hist.number_atoms_total 2088 _refine_hist.d_res_high 1.50 _refine_hist.d_res_low 30 # 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 r_bond_refined_d 0.019 0.020 ? 1981 ? 'X-RAY DIFFRACTION' r_bond_other_d 0.002 0.020 ? 1707 ? 'X-RAY DIFFRACTION' r_angle_refined_deg 1.993 1.967 ? 2692 ? 'X-RAY DIFFRACTION' r_angle_other_deg 0.987 3.000 ? 3949 ? 'X-RAY DIFFRACTION' r_dihedral_angle_1_deg 12.158 5.000 ? 242 ? 'X-RAY DIFFRACTION' r_dihedral_angle_2_deg 33.274 25.208 ? 96 ? 'X-RAY DIFFRACTION' r_dihedral_angle_3_deg 12.005 15.000 ? 280 ? 'X-RAY DIFFRACTION' r_dihedral_angle_4_deg 19.075 15.000 ? 8 ? 'X-RAY DIFFRACTION' r_chiral_restr 0.130 0.200 ? 281 ? 'X-RAY DIFFRACTION' r_gen_planes_refined 0.010 0.021 ? 2287 ? 'X-RAY DIFFRACTION' r_gen_planes_other 0.001 0.020 ? 446 ? 'X-RAY DIFFRACTION' r_nbd_refined ? ? ? ? ? 'X-RAY DIFFRACTION' r_nbd_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_nbtor_refined ? ? ? ? ? 'X-RAY DIFFRACTION' r_nbtor_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_xyhbond_nbd_refined ? ? ? ? ? 'X-RAY DIFFRACTION' r_xyhbond_nbd_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_metal_ion_refined ? ? ? ? ? 'X-RAY DIFFRACTION' r_metal_ion_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_symmetry_vdw_refined ? ? ? ? ? 'X-RAY DIFFRACTION' r_symmetry_vdw_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_symmetry_hbond_refined ? ? ? ? ? 'X-RAY DIFFRACTION' r_symmetry_hbond_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_symmetry_metal_ion_refined ? ? ? ? ? 'X-RAY DIFFRACTION' r_symmetry_metal_ion_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_mcbond_it 3.494 2.455 ? 967 ? 'X-RAY DIFFRACTION' r_mcbond_other 3.492 83.714 ? 964 ? 'X-RAY DIFFRACTION' r_mcangle_it 4.170 . ? 1208 ? 'X-RAY DIFFRACTION' r_mcangle_other 4.168 . ? 1209 ? 'X-RAY DIFFRACTION' r_scbond_it 7.118 1.521 ? 1014 ? 'X-RAY DIFFRACTION' r_scbond_other 7.115 1.524 ? 1015 ? 'X-RAY DIFFRACTION' r_scangle_it ? ? ? ? ? 'X-RAY DIFFRACTION' r_scangle_other 8.805 2.156 ? 1485 ? 'X-RAY DIFFRACTION' r_long_range_B_refined 4.984 . ? 2400 ? 'X-RAY DIFFRACTION' r_long_range_B_other 4.987 . ? 2400 ? 'X-RAY DIFFRACTION' r_rigid_bond_restr 5.269 3.000 ? 1920 ? 'X-RAY DIFFRACTION' r_sphericity_free ? ? ? ? ? 'X-RAY DIFFRACTION' r_sphericity_bonded 19.439 5.000 ? 1868 ? 'X-RAY DIFFRACTION' # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 1.500 _refine_ls_shell.d_res_low 1.539 _refine_ls_shell.number_reflns_R_work 2329 _refine_ls_shell.R_factor_R_work 0.199 _refine_ls_shell.percent_reflns_obs 96.94 _refine_ls_shell.R_factor_R_free 0.251 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 79 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.redundancy_reflns_obs ? # _struct.entry_id 4OPB _struct.title 'AA13 Lytic polysaccharide monooxygenase from Aspergillus oryzae' _struct.pdbx_descriptor 'Predicted protein' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4OPB _struct_keywords.pdbx_keywords 'METAL BINDING PROTEIN' _struct_keywords.text 'METAL BINDING PROTEIN' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 4 ? E N N 4 ? F N N 4 ? G N N 4 ? H N N 5 ? I N N 6 ? J N N 6 ? K N N 5 ? L N N 6 ? M N N 6 ? N N N 7 ? O N N 6 ? P N N 6 ? Q N N 6 ? R N N 7 ? S 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 9 ? ALA A 17 ? SER A 9 ALA A 17 1 ? 9 HELX_P HELX_P2 2 CYS A 22 ? ALA A 26 ? CYS A 22 ALA A 26 5 ? 5 HELX_P HELX_P3 3 ASP A 102 ? ASP A 107 ? ASP A 102 ASP A 107 1 ? 6 HELX_P HELX_P4 4 LYS A 108 ? LEU A 110 ? LYS A 108 LEU A 110 5 ? 3 HELX_P HELX_P5 5 THR A 117 ? GLY A 131 ? THR A 117 GLY A 131 1 ? 15 HELX_P HELX_P6 6 PRO A 134 ? VAL A 138 ? PRO A 134 VAL A 138 5 ? 5 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 22 SG ? ? ? 1_555 A CYS 25 SG ? ? A CYS 22 A CYS 25 1_555 ? ? ? ? ? ? ? 1.997 ? disulf2 disulf ? ? A CYS 48 SG ? ? ? 1_555 A CYS 227 SG ? ? A CYS 48 A CYS 227 1_555 ? ? ? ? ? ? ? 2.106 ? disulf3 disulf ? ? A CYS 84 SG ? ? ? 1_555 A CYS 185 SG ? ? A CYS 84 A CYS 185 1_555 ? ? ? ? ? ? ? 2.043 ? disulf4 disulf ? ? A CYS 100 SG ? ? ? 1_555 A CYS 127 SG ? ? A CYS 100 A CYS 127 1_555 ? ? ? ? ? ? ? 2.129 ? disulf5 disulf ? ? A CYS 135 SG ? ? ? 1_555 A CYS 143 SG ? ? A CYS 135 A CYS 143 1_555 ? ? ? ? ? ? ? 2.043 ? disulf6 disulf ? ? A CYS 149 SG ? ? ? 1_555 A CYS 155 SG ? ? A CYS 149 A CYS 155 1_555 ? ? ? ? ? ? ? 2.067 ? disulf7 disulf ? ? A CYS 163 SG ? ? ? 1_555 A CYS 174 SG ? ? A CYS 163 A CYS 174 1_555 ? ? ? ? ? ? ? 2.068 ? covale1 covale ? ? A HIC 1 C ? ? ? 1_555 A GLY 2 N ? ? A HIC 1 A GLY 2 1_555 ? ? ? ? ? ? ? 1.308 ? covale2 covale ? ? A ASN 207 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 207 A NAG 302 1_555 ? ? ? ? ? ? ? 1.430 ? metalc1 metalc ? ? A HIC 1 ND1 ? ? ? 1_555 B CU . CU ? ? A HIC 1 A CU 301 1_555 ? ? ? ? ? ? ? 1.870 ? metalc2 metalc ? ? G ZN . ZN ? ? ? 1_555 S HOH . O B ? A ZN 306 A HOH 578 1_555 ? ? ? ? ? ? ? 1.923 ? metalc3 metalc ? ? A HIS 91 NE2 ? ? ? 1_555 B CU . CU ? ? A HIS 91 A CU 301 1_555 ? ? ? ? ? ? ? 1.980 ? metalc4 metalc ? ? D ZN . ZN ? ? ? 1_555 S HOH . O ? ? A ZN 303 A HOH 451 1_555 ? ? ? ? ? ? ? 1.982 ? metalc5 metalc ? ? A ASP 38 OD1 ? ? ? 1_555 F ZN . ZN ? ? A ASP 38 A ZN 305 1_555 ? ? ? ? ? ? ? 1.982 ? metalc6 metalc ? ? A GLU 142 OE1 ? ? ? 1_555 G ZN . ZN ? ? A GLU 142 A ZN 306 1_555 ? ? ? ? ? ? ? 2.007 ? metalc7 metalc ? ? A ASP 36 OD1 ? ? ? 1_555 F ZN . ZN ? ? A ASP 36 A ZN 305 1_555 ? ? ? ? ? ? ? 2.009 ? metalc8 metalc ? ? A GLU 125 OE2 ? ? ? 1_555 D ZN . ZN ? ? A GLU 125 A ZN 303 1_555 ? ? ? ? ? ? ? 2.024 ? metalc9 metalc ? ? A ASP 129 OD2 ? ? ? 1_555 D ZN . ZN ? ? A ASP 129 A ZN 303 1_555 ? ? ? ? ? ? ? 2.129 ? metalc10 metalc ? ? F ZN . ZN ? ? ? 1_555 S HOH . O ? ? A ZN 305 A HOH 458 1_555 ? ? ? ? ? ? ? 2.138 ? metalc11 metalc ? ? G ZN . ZN ? ? ? 1_555 S HOH . O ? ? A ZN 306 A HOH 579 1_555 ? ? ? ? ? ? ? 2.188 ? metalc12 metalc ? ? A HIC 1 N ? ? ? 1_555 B CU . CU ? ? A HIC 1 A CU 301 1_555 ? ? ? ? ? ? ? 2.214 ? metalc13 metalc ? ? D ZN . ZN ? ? ? 1_555 S HOH . O ? ? A ZN 303 A HOH 603 1_555 ? ? ? ? ? ? ? 2.240 ? metalc14 metalc ? ? A HIS 15 NE2 ? ? ? 1_555 E ZN . ZN ? ? A HIS 15 A ZN 304 1_555 ? ? ? ? ? ? ? 2.251 ? metalc15 metalc ? ? E ZN . ZN ? ? ? 1_555 S HOH . O ? ? A ZN 304 A HOH 404 1_555 ? ? ? ? ? ? ? 2.280 ? metalc16 metalc ? ? A ASP 129 OD1 ? ? ? 1_555 D ZN . ZN ? ? A ASP 129 A ZN 303 1_555 ? ? ? ? ? ? ? 2.348 ? metalc17 metalc ? ? A TYR 224 OH ? ? ? 1_555 B CU . CU ? ? A TYR 224 A CU 301 1_555 ? ? ? ? ? ? ? 2.534 ? metalc18 metalc ? ? A ASP 36 OD2 ? ? ? 1_555 F ZN . ZN ? ? A ASP 36 A ZN 305 1_555 ? ? ? ? ? ? ? 2.687 ? metalc19 metalc ? ? A GLU 142 OE2 ? ? ? 1_555 G ZN . ZN ? ? A GLU 142 A ZN 306 1_555 ? ? ? ? ? ? ? 2.695 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? metalc ? ? # 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 ILE 6 A . ? ILE 6 A PRO 7 A ? PRO 7 A 1 -15.74 2 GLU 29 A . ? GLU 29 A PRO 30 A ? PRO 30 A 1 -14.05 3 TRP 34 A . ? TRP 34 A PRO 35 A ? PRO 35 A 1 -0.48 4 GLU 167 A . ? GLU 167 A ALA 168 A ? ALA 168 A 1 21.81 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 3 ? B ? 2 ? C ? 5 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? anti-parallel A 2 3 ? anti-parallel B 1 2 ? anti-parallel C 1 2 ? parallel C 2 3 ? anti-parallel C 3 4 ? anti-parallel C 4 5 ? 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 GLY A 2 ? ILE A 6 ? GLY A 2 ILE A 6 A 2 GLU A 78 ? ASP A 86 ? GLU A 78 ASP A 86 A 3 GLY A 192 ? LYS A 200 ? GLY A 192 LYS A 200 B 1 TYR A 50 ? ASN A 51 ? TYR A 50 ASN A 51 B 2 ILE A 56 ? ASP A 57 ? ILE A 56 ASP A 57 C 1 GLN A 71 ? TYR A 73 ? GLN A 71 TYR A 73 C 2 ILE A 223 ? ILE A 232 ? ILE A 223 ILE A 232 C 3 SER A 206 ? SER A 217 ? SER A 206 SER A 217 C 4 GLY A 93 ? ARG A 98 ? GLY A 93 ARG A 98 C 5 PHE A 161 ? THR A 162 ? PHE A 161 THR A 162 # 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 N TYR A 3 ? N TYR A 3 O CYS A 84 ? O CYS A 84 A 2 3 N ILE A 79 ? N ILE A 79 O VAL A 199 ? O VAL A 199 B 1 2 N ASN A 51 ? N ASN A 51 O ILE A 56 ? O ILE A 56 C 1 2 N TYR A 73 ? N TYR A 73 O ALA A 231 ? O ALA A 231 C 2 3 O ILE A 230 ? O ILE A 230 N THR A 209 ? N THR A 209 C 3 4 O ASN A 216 ? O ASN A 216 N MET A 94 ? N MET A 94 C 4 5 N PHE A 95 ? N PHE A 95 O PHE A 161 ? O PHE A 161 # 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 ? ? ? ? 3 'BINDING SITE FOR RESIDUE CU A 301' AC2 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE NAG A 302' AC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN A 303' AC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN A 304' AC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN A 305' AC6 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN A 306' AC7 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE IPA A 307' AC8 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE GOL A 308' AC9 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE GOL A 309' BC1 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE IPA A 310' BC2 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE GOL A 311' BC3 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE GOL A 312' BC4 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE ACT A 313' BC5 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE GOL A 314' BC6 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE GOL A 315' BC7 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE GOL A 316' BC8 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ACT A 317' # 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 3 HIC A 1 ? HIC A 1 . ? 1_555 ? 2 AC1 3 HIS A 91 ? HIS A 91 . ? 1_555 ? 3 AC1 3 TYR A 224 ? TYR A 224 . ? 1_555 ? 4 AC2 10 TYR A 145 ? TYR A 145 . ? 4_556 ? 5 AC2 10 ASN A 158 ? ASN A 158 . ? 4_556 ? 6 AC2 10 TYR A 193 ? TYR A 193 . ? 2_764 ? 7 AC2 10 THR A 205 ? THR A 205 . ? 1_555 ? 8 AC2 10 ASN A 207 ? ASN A 207 . ? 1_555 ? 9 AC2 10 HOH S . ? HOH A 489 . ? 2_764 ? 10 AC2 10 HOH S . ? HOH A 493 . ? 1_555 ? 11 AC2 10 HOH S . ? HOH A 495 . ? 4_556 ? 12 AC2 10 HOH S . ? HOH A 496 . ? 4_556 ? 13 AC2 10 HOH S . ? HOH A 567 . ? 4_556 ? 14 AC3 4 GLU A 125 ? GLU A 125 . ? 1_555 ? 15 AC3 4 ASP A 129 ? ASP A 129 . ? 1_555 ? 16 AC3 4 HOH S . ? HOH A 451 . ? 1_555 ? 17 AC3 4 HOH S . ? HOH A 603 . ? 1_555 ? 18 AC4 4 HIS A 15 ? HIS A 15 . ? 1_555 ? 19 AC4 4 GLU A 29 ? GLU A 29 . ? 4_566 ? 20 AC4 4 HOH S . ? HOH A 404 . ? 1_555 ? 21 AC4 4 HOH S . ? HOH A 471 . ? 4_566 ? 22 AC5 4 ASP A 36 ? ASP A 36 . ? 1_555 ? 23 AC5 4 ASP A 38 ? ASP A 38 . ? 1_555 ? 24 AC5 4 GLU A 203 ? GLU A 203 . ? 4_456 ? 25 AC5 4 HOH S . ? HOH A 458 . ? 1_555 ? 26 AC6 4 HIS A 87 ? HIS A 87 . ? 3_746 ? 27 AC6 4 GLU A 142 ? GLU A 142 . ? 1_555 ? 28 AC6 4 HOH S . ? HOH A 578 . ? 1_555 ? 29 AC6 4 HOH S . ? HOH A 579 . ? 1_555 ? 30 AC7 4 GLU A 29 ? GLU A 29 . ? 1_555 ? 31 AC7 4 PRO A 30 ? PRO A 30 . ? 1_555 ? 32 AC7 4 HOH S . ? HOH A 606 . ? 1_555 ? 33 AC7 4 HOH S . ? HOH A 612 . ? 1_555 ? 34 AC8 6 GLN A 71 ? GLN A 71 . ? 1_555 ? 35 AC8 6 SER A 72 ? SER A 72 . ? 1_555 ? 36 AC8 6 TYR A 73 ? TYR A 73 . ? 1_555 ? 37 AC8 6 SER A 74 ? SER A 74 . ? 1_555 ? 38 AC8 6 GLU A 77 ? GLU A 77 . ? 1_555 ? 39 AC8 6 ACT R . ? ACT A 317 . ? 1_555 ? 40 AC9 8 TRP A 34 ? TRP A 34 . ? 2_664 ? 41 AC9 8 PRO A 35 ? PRO A 35 . ? 2_664 ? 42 AC9 8 TYR A 114 ? TYR A 114 . ? 1_555 ? 43 AC9 8 THR A 117 ? THR A 117 . ? 1_555 ? 44 AC9 8 ASP A 148 ? ASP A 148 . ? 2_664 ? 45 AC9 8 GLU A 153 ? GLU A 153 . ? 2_664 ? 46 AC9 8 HOH S . ? HOH A 468 . ? 1_555 ? 47 AC9 8 HOH S . ? HOH A 470 . ? 1_555 ? 48 BC1 4 HIC A 1 ? HIC A 1 . ? 1_555 ? 49 BC1 4 CYS A 25 ? CYS A 25 . ? 1_555 ? 50 BC1 4 ARG A 53 ? ARG A 53 . ? 1_555 ? 51 BC1 4 HOH S . ? HOH A 604 . ? 1_555 ? 52 BC2 9 GLN A 101 ? GLN A 101 . ? 1_555 ? 53 BC2 9 GLN A 103 ? GLN A 103 . ? 1_555 ? 54 BC2 9 GLU A 151 ? GLU A 151 . ? 4_556 ? 55 BC2 9 GLY A 152 ? GLY A 152 . ? 4_556 ? 56 BC2 9 TRP A 156 ? TRP A 156 . ? 4_556 ? 57 BC2 9 TYR A 204 ? TYR A 204 . ? 1_555 ? 58 BC2 9 HOH S . ? HOH A 428 . ? 1_555 ? 59 BC2 9 HOH S . ? HOH A 526 . ? 1_555 ? 60 BC2 9 HOH S . ? HOH A 527 . ? 1_555 ? 61 BC3 7 ASP A 119 ? ASP A 119 . ? 2_665 ? 62 BC3 7 ASP A 148 ? ASP A 148 . ? 1_555 ? 63 BC3 7 PHE A 166 ? PHE A 166 . ? 1_555 ? 64 BC3 7 GLU A 167 ? GLU A 167 . ? 1_555 ? 65 BC3 7 PHE A 218 ? PHE A 218 . ? 1_555 ? 66 BC3 7 HOH S . ? HOH A 469 . ? 2_665 ? 67 BC3 7 HOH S . ? HOH A 537 . ? 2_665 ? 68 BC4 8 GLY A 144 ? GLY A 144 . ? 1_555 ? 69 BC4 8 TYR A 145 ? TYR A 145 . ? 1_555 ? 70 BC4 8 THR A 162 ? THR A 162 . ? 1_555 ? 71 BC4 8 CYS A 163 ? CYS A 163 . ? 1_555 ? 72 BC4 8 ASN A 164 ? ASN A 164 . ? 1_555 ? 73 BC4 8 GOL O . ? GOL A 314 . ? 1_555 ? 74 BC4 8 GOL P . ? GOL A 315 . ? 1_555 ? 75 BC4 8 HOH S . ? HOH A 434 . ? 1_555 ? 76 BC5 7 ASN A 118 ? ASN A 118 . ? 2_665 ? 77 BC5 7 TYR A 145 ? TYR A 145 . ? 1_555 ? 78 BC5 7 SER A 146 ? SER A 146 . ? 1_555 ? 79 BC5 7 ALA A 147 ? ALA A 147 . ? 1_555 ? 80 BC5 7 ACT N . ? ACT A 313 . ? 1_555 ? 81 BC5 7 HOH S . ? HOH A 414 . ? 1_555 ? 82 BC5 7 HOH S . ? HOH A 574 . ? 1_555 ? 83 BC6 8 GLY A 144 ? GLY A 144 . ? 1_555 ? 84 BC6 8 THR A 162 ? THR A 162 . ? 1_555 ? 85 BC6 8 ASN A 164 ? ASN A 164 . ? 1_555 ? 86 BC6 8 LYS A 197 ? LYS A 197 . ? 1_555 ? 87 BC6 8 ACT N . ? ACT A 313 . ? 1_555 ? 88 BC6 8 HOH S . ? HOH A 409 . ? 1_555 ? 89 BC6 8 HOH S . ? HOH A 416 . ? 1_555 ? 90 BC6 8 HOH S . ? HOH A 545 . ? 1_555 ? 91 BC7 6 ILE A 27 ? ILE A 27 . ? 1_555 ? 92 BC7 6 LEU A 28 ? LEU A 28 . ? 1_555 ? 93 BC7 6 GLU A 29 ? GLU A 29 . ? 1_555 ? 94 BC7 6 SER A 45 ? SER A 45 . ? 1_555 ? 95 BC7 6 HOH S . ? HOH A 596 . ? 1_555 ? 96 BC7 6 HOH S . ? HOH A 606 . ? 1_555 ? 97 BC8 4 SER A 74 ? SER A 74 . ? 1_555 ? 98 BC8 4 GLU A 77 ? GLU A 77 . ? 1_555 ? 99 BC8 4 ALA A 130 ? ALA A 130 . ? 4_556 ? 100 BC8 4 GOL I . ? GOL A 308 . ? 1_555 ? # _database_PDB_matrix.entry_id 4OPB _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 4OPB _atom_sites.fract_transf_matrix[1][1] 0.021478 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] -0.000000 _atom_sites.fract_transf_matrix[2][2] 0.016234 _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] 0.013669 _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 CU N O S ZN # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num HETATM 1 N N . HIC A 1 1 ? 42.811 41.160 41.331 1.00 10.18 ? 1 HIC A N 1 HETATM 2 C CA . HIC A 1 1 ? 44.006 41.597 40.511 1.00 8.69 ? 1 HIC A CA 1 HETATM 3 C C . HIC A 1 1 ? 45.175 40.711 40.945 1.00 8.68 ? 1 HIC A C 1 HETATM 4 O O . HIC A 1 1 ? 45.625 40.780 42.090 1.00 9.22 ? 1 HIC A O 1 HETATM 5 C CB . HIC A 1 1 ? 44.277 43.091 40.728 1.00 11.23 ? 1 HIC A CB 1 HETATM 6 C CG . HIC A 1 1 ? 43.302 43.944 39.986 1.00 9.55 ? 1 HIC A CG 1 HETATM 7 N ND1 . HIC A 1 1 ? 41.937 43.830 40.187 1.00 9.93 ? 1 HIC A ND1 1 HETATM 8 C CD2 . HIC A 1 1 ? 43.564 44.889 39.046 1.00 8.53 ? 1 HIC A CD2 1 HETATM 9 C CE1 . HIC A 1 1 ? 41.386 44.715 39.339 1.00 10.69 ? 1 HIC A CE1 1 HETATM 10 N NE2 . HIC A 1 1 ? 42.386 45.341 38.651 1.00 10.71 ? 1 HIC A NE2 1 HETATM 11 C CZ . HIC A 1 1 ? 42.152 46.361 37.596 1.00 12.01 ? 1 HIC A CZ 1 ATOM 12 N N . GLY A 1 2 ? 45.645 39.891 40.041 1.00 7.55 ? 2 GLY A N 1 ATOM 13 C CA . GLY A 1 2 ? 46.749 38.964 40.320 1.00 7.16 ? 2 GLY A CA 1 ATOM 14 C C . GLY A 1 2 ? 47.197 38.325 39.018 1.00 6.47 ? 2 GLY A C 1 ATOM 15 O O . GLY A 1 2 ? 46.516 38.420 37.973 1.00 8.85 ? 2 GLY A O 1 ATOM 16 N N . TYR A 1 3 ? 48.356 37.641 39.069 1.00 7.86 ? 3 TYR A N 1 ATOM 17 C CA . TYR A 1 3 ? 48.897 36.964 37.933 1.00 7.19 ? 3 TYR A CA 1 ATOM 18 C C . TYR A 1 3 ? 49.948 35.969 38.410 1.00 6.83 ? 3 TYR A C 1 ATOM 19 O O . TYR A 1 3 ? 50.453 36.060 39.519 1.00 8.12 ? 3 TYR A O 1 ATOM 20 C CB . TYR A 1 3 ? 49.519 37.974 36.939 1.00 7.12 ? 3 TYR A CB 1 ATOM 21 C CG . TYR A 1 3 ? 50.743 38.688 37.439 1.00 8.83 ? 3 TYR A CG 1 ATOM 22 C CD1 . TYR A 1 3 ? 50.646 39.729 38.385 1.00 9.27 ? 3 TYR A CD1 1 ATOM 23 C CD2 . TYR A 1 3 ? 51.990 38.340 37.017 1.00 9.90 ? 3 TYR A CD2 1 ATOM 24 C CE1 . TYR A 1 3 ? 51.742 40.375 38.846 1.00 9.32 ? 3 TYR A CE1 1 ATOM 25 C CE2 . TYR A 1 3 ? 53.101 39.044 37.437 1.00 9.95 ? 3 TYR A CE2 1 ATOM 26 C CZ . TYR A 1 3 ? 52.992 40.046 38.354 1.00 9.38 ? 3 TYR A CZ 1 ATOM 27 O OH . TYR A 1 3 ? 54.115 40.706 38.829 1.00 12.02 ? 3 TYR A OH 1 ATOM 28 N N . MET A 1 4 ? 50.268 35.034 37.549 1.00 6.84 ? 4 MET A N 1 ATOM 29 C CA . MET A 1 4 ? 51.238 33.964 37.855 1.00 7.04 ? 4 MET A CA 1 ATOM 30 C C . MET A 1 4 ? 52.681 34.507 37.866 1.00 7.87 ? 4 MET A C 1 ATOM 31 O O . MET A 1 4 ? 53.100 35.234 36.960 1.00 9.52 ? 4 MET A O 1 ATOM 32 C CB . MET A 1 4 ? 51.115 32.849 36.857 1.00 7.74 ? 4 MET A CB 1 ATOM 33 C CG . MET A 1 4 ? 52.119 31.729 37.032 1.00 8.53 ? 4 MET A CG 1 ATOM 34 S SD . MET A 1 4 ? 51.839 30.383 35.912 1.00 9.78 ? 4 MET A SD 1 ATOM 35 C CE . MET A 1 4 ? 53.160 29.327 36.508 1.00 11.24 ? 4 MET A CE 1 ATOM 36 N N . TYR A 1 5 ? 53.398 34.151 38.929 1.00 7.70 ? 5 TYR A N 1 ATOM 37 C CA . TYR A 1 5 ? 54.729 34.709 39.210 1.00 7.94 ? 5 TYR A CA 1 ATOM 38 C C . TYR A 1 5 ? 55.854 33.709 39.036 1.00 9.62 ? 5 TYR A C 1 ATOM 39 O O . TYR A 1 5 ? 56.890 34.079 38.505 1.00 9.43 ? 5 TYR A O 1 ATOM 40 C CB . TYR A 1 5 ? 54.728 35.315 40.645 1.00 10.00 ? 5 TYR A CB 1 ATOM 41 C CG . TYR A 1 5 ? 55.662 36.455 40.814 1.00 11.61 ? 5 TYR A CG 1 ATOM 42 C CD1 . TYR A 1 5 ? 55.426 37.641 40.150 1.00 11.54 ? 5 TYR A CD1 1 ATOM 43 C CD2 . TYR A 1 5 ? 56.779 36.362 41.643 1.00 11.89 ? 5 TYR A CD2 1 ATOM 44 C CE1 . TYR A 1 5 ? 56.274 38.708 40.301 1.00 11.66 ? 5 TYR A CE1 1 ATOM 45 C CE2 . TYR A 1 5 ? 57.663 37.450 41.794 1.00 14.36 ? 5 TYR A CE2 1 ATOM 46 C CZ . TYR A 1 5 ? 57.368 38.627 41.107 1.00 13.88 ? 5 TYR A CZ 1 ATOM 47 O OH . TYR A 1 5 ? 58.111 39.770 41.218 1.00 17.98 ? 5 TYR A OH 1 ATOM 48 N N . ILE A 1 6 ? 55.685 32.480 39.466 1.00 9.01 ? 6 ILE A N 1 ATOM 49 C CA . ILE A 1 6 ? 56.750 31.451 39.390 1.00 8.80 ? 6 ILE A CA 1 ATOM 50 C C . ILE A 1 6 ? 56.109 30.136 38.945 1.00 8.72 ? 6 ILE A C 1 ATOM 51 O O . ILE A 1 6 ? 55.138 29.702 39.582 1.00 9.38 ? 6 ILE A O 1 ATOM 52 C CB . ILE A 1 6 ? 57.463 31.180 40.749 1.00 10.22 ? 6 ILE A CB 1 ATOM 53 C CG1 . ILE A 1 6 ? 58.138 32.475 41.318 1.00 13.33 ? 6 ILE A CG1 1 ATOM 54 C CG2 . ILE A 1 6 ? 58.445 29.978 40.591 1.00 13.09 ? 6 ILE A CG2 1 ATOM 55 C CD1 . ILE A 1 6 ? 58.736 32.373 42.708 1.00 16.03 ? 6 ILE A CD1 1 ATOM 56 N N . PRO A 1 7 ? 56.700 29.467 37.937 1.00 10.94 ? 7 PRO A N 1 ATOM 57 C CA . PRO A 1 7 ? 57.685 29.989 37.014 1.00 10.04 ? 7 PRO A CA 1 ATOM 58 C C . PRO A 1 7 ? 57.211 31.263 36.340 1.00 10.22 ? 7 PRO A C 1 ATOM 59 O O . PRO A 1 7 ? 55.971 31.504 36.250 1.00 9.34 ? 7 PRO A O 1 ATOM 60 C CB . PRO A 1 7 ? 57.867 28.850 35.971 1.00 10.05 ? 7 PRO A CB 1 ATOM 61 C CG . PRO A 1 7 ? 56.611 28.059 36.087 1.00 10.59 ? 7 PRO A CG 1 ATOM 62 C CD . PRO A 1 7 ? 56.239 28.116 37.528 1.00 11.75 ? 7 PRO A CD 1 ATOM 63 N N . SER A 1 8 ? 58.166 32.109 35.904 1.00 9.73 ? 8 SER A N 1 ATOM 64 C CA . SER A 1 8 ? 57.754 33.389 35.328 1.00 9.81 ? 8 SER A CA 1 ATOM 65 C C . SER A 1 8 ? 56.776 33.246 34.153 1.00 7.87 ? 8 SER A C 1 ATOM 66 O O . SER A 1 8 ? 57.100 32.626 33.141 1.00 10.41 ? 8 SER A O 1 ATOM 67 C CB . SER A 1 8 ? 58.920 34.258 34.901 1.00 10.81 ? 8 SER A CB 1 ATOM 68 O OG . SER A 1 8 ? 59.787 34.513 35.988 1.00 16.28 ? 8 SER A OG 1 ATOM 69 N N . SER A 1 9 ? 55.598 33.845 34.308 1.00 8.00 ? 9 SER A N 1 ATOM 70 C CA . SER A 1 9 ? 54.613 33.808 33.276 1.00 7.55 ? 9 SER A CA 1 ATOM 71 C C . SER A 1 9 ? 54.888 34.798 32.146 1.00 7.64 ? 9 SER A C 1 ATOM 72 O O . SER A 1 9 ? 55.685 35.715 32.283 1.00 7.71 ? 9 SER A O 1 ATOM 73 C CB . SER A 1 9 ? 53.211 34.079 33.889 1.00 8.08 ? 9 SER A CB 1 ATOM 74 O OG . SER A 1 9 ? 53.121 35.403 34.329 1.00 9.71 ? 9 SER A OG 1 ATOM 75 N N . ARG A 1 10 ? 54.178 34.628 31.028 1.00 6.50 ? 10 ARG A N 1 ATOM 76 C CA . ARG A 1 10 ? 54.188 35.610 29.969 1.00 8.27 ? 10 ARG A CA 1 ATOM 77 C C . ARG A 1 10 ? 53.827 36.993 30.497 1.00 7.28 ? 10 ARG A C 1 ATOM 78 O O . ARG A 1 10 ? 54.439 37.971 30.077 1.00 7.92 ? 10 ARG A O 1 ATOM 79 C CB . ARG A 1 10 ? 53.297 35.211 28.811 1.00 7.95 ? 10 ARG A CB 1 ATOM 80 C CG . ARG A 1 10 ? 53.768 33.928 28.156 1.00 7.66 ? 10 ARG A CG 1 ATOM 81 C CD . ARG A 1 10 ? 52.872 33.504 27.028 1.00 8.88 ? 10 ARG A CD 1 ATOM 82 N NE . ARG A 1 10 ? 53.430 32.410 26.288 1.00 8.68 ? 10 ARG A NE 1 ATOM 83 C CZ . ARG A 1 10 ? 52.991 31.921 25.145 1.00 8.11 ? 10 ARG A CZ 1 ATOM 84 N NH1 . ARG A 1 10 ? 51.927 32.423 24.546 1.00 9.69 ? 10 ARG A NH1 1 ATOM 85 N NH2 . ARG A 1 10 ? 53.638 30.926 24.567 1.00 7.99 ? 10 ARG A NH2 1 ATOM 86 N N . THR A 1 11 ? 52.883 37.074 31.446 1.00 8.30 ? 11 THR A N 1 ATOM 87 C CA . THR A 1 11 ? 52.477 38.371 32.001 1.00 8.55 ? 11 THR A CA 1 ATOM 88 C C . THR A 1 11 ? 53.618 39.012 32.823 1.00 8.74 ? 11 THR A C 1 ATOM 89 O O . THR A 1 11 ? 53.864 40.211 32.691 1.00 9.01 ? 11 THR A O 1 ATOM 90 C CB . THR A 1 11 ? 51.289 38.183 32.905 1.00 7.91 ? 11 THR A CB 1 ATOM 91 O OG1 . THR A 1 11 ? 50.294 37.468 32.168 1.00 9.20 ? 11 THR A OG1 1 ATOM 92 C CG2 . THR A 1 11 ? 50.702 39.510 33.403 1.00 9.96 ? 11 THR A CG2 1 ATOM 93 N N . ARG A 1 12 ? 54.354 38.199 33.605 1.00 8.41 ? 12 ARG A N 1 ATOM 94 C CA . ARG A 1 12 ? 55.490 38.713 34.345 1.00 7.77 ? 12 ARG A CA 1 ATOM 95 C C . ARG A 1 12 ? 56.571 39.199 33.413 1.00 8.51 ? 12 ARG A C 1 ATOM 96 O O . ARG A 1 12 ? 57.112 40.288 33.584 1.00 10.96 ? 12 ARG A O 1 ATOM 97 C CB . ARG A 1 12 ? 56.041 37.671 35.274 1.00 8.33 ? 12 ARG A CB 1 ATOM 98 C CG . ARG A 1 12 ? 57.250 38.109 36.068 1.00 9.24 ? 12 ARG A CG 1 ATOM 99 C CD . ARG A 1 12 ? 57.691 37.095 37.082 1.00 9.90 ? 12 ARG A CD 1 ATOM 100 N NE . ARG A 1 12 ? 58.913 37.583 37.721 1.00 12.19 ? 12 ARG A NE 1 ATOM 101 C CZ . ARG A 1 12 ? 59.527 36.952 38.693 1.00 13.22 ? 12 ARG A CZ 1 ATOM 102 N NH1 . ARG A 1 12 ? 59.098 35.783 39.109 1.00 14.14 ? 12 ARG A NH1 1 ATOM 103 N NH2 . ARG A 1 12 ? 60.657 37.478 39.221 1.00 18.03 ? 12 ARG A NH2 1 ATOM 104 N N . LEU A 1 13 ? 56.799 38.417 32.365 1.00 8.52 ? 13 LEU A N 1 ATOM 105 C CA . LEU A 1 13 ? 57.820 38.819 31.399 1.00 9.98 ? 13 LEU A CA 1 ATOM 106 C C . LEU A 1 13 ? 57.413 40.094 30.616 1.00 9.59 ? 13 LEU A C 1 ATOM 107 O O . LEU A 1 13 ? 58.223 40.932 30.335 1.00 9.55 ? 13 LEU A O 1 ATOM 108 C CB . LEU A 1 13 ? 58.114 37.690 30.420 1.00 11.52 ? 13 LEU A CB 1 ATOM 109 C CG . LEU A 1 13 ? 58.817 36.460 31.020 1.00 13.47 ? 13 LEU A CG 1 ATOM 110 C CD1 . LEU A 1 13 ? 59.105 35.482 29.903 1.00 16.78 ? 13 LEU A CD1 1 ATOM 111 C CD2 . LEU A 1 13 ? 60.073 36.802 31.765 1.00 22.11 ? 13 LEU A CD2 1 ATOM 112 N N . GLY A 1 14 ? 56.128 40.262 30.359 1.00 8.77 ? 14 GLY A N 1 ATOM 113 C CA . GLY A 1 14 ? 55.649 41.436 29.696 1.00 10.16 ? 14 GLY A CA 1 ATOM 114 C C . GLY A 1 14 ? 55.833 42.686 30.535 1.00 10.67 ? 14 GLY A C 1 ATOM 115 O O . GLY A 1 14 ? 56.201 43.736 30.012 1.00 11.30 ? 14 GLY A O 1 ATOM 116 N N . HIS A 1 15 ? 55.598 42.588 31.845 1.00 8.02 ? 15 HIS A N 1 ATOM 117 C CA . HIS A 1 15 ? 55.910 43.696 32.706 1.00 9.36 ? 15 HIS A CA 1 ATOM 118 C C . HIS A 1 15 ? 57.460 43.967 32.701 1.00 9.47 ? 15 HIS A C 1 ATOM 119 O O . HIS A 1 15 ? 57.923 45.109 32.583 1.00 12.46 ? 15 HIS A O 1 ATOM 120 C CB . HIS A 1 15 ? 55.488 43.443 34.132 1.00 11.70 ? 15 HIS A CB 1 ATOM 121 C CG . HIS A 1 15 ? 56.049 44.466 35.032 1.00 11.98 ? 15 HIS A CG 1 ATOM 122 N ND1 . HIS A 1 15 ? 55.719 45.811 34.903 1.00 16.42 ? 15 HIS A ND1 1 ATOM 123 C CD2 . HIS A 1 15 ? 57.039 44.395 35.942 1.00 18.43 ? 15 HIS A CD2 1 ATOM 124 C CE1 . HIS A 1 15 ? 56.476 46.512 35.723 1.00 17.72 ? 15 HIS A CE1 1 ATOM 125 N NE2 . HIS A 1 15 ? 57.261 45.671 36.386 1.00 22.94 ? 15 HIS A NE2 1 ATOM 126 N N . GLU A 1 16 ? 58.214 42.903 32.902 1.00 11.30 ? 16 GLU A N 1 ATOM 127 C CA . GLU A 1 16 ? 59.666 43.043 32.991 1.00 11.79 ? 16 GLU A CA 1 ATOM 128 C C . GLU A 1 16 ? 60.284 43.627 31.721 1.00 12.30 ? 16 GLU A C 1 ATOM 129 O O . GLU A 1 16 ? 61.357 44.260 31.761 1.00 15.59 ? 16 GLU A O 1 ATOM 130 C CB . GLU A 1 16 ? 60.324 41.718 33.456 1.00 14.94 ? 16 GLU A CB 1 ATOM 131 C CG . GLU A 1 16 ? 59.983 41.460 34.929 1.00 17.98 ? 16 GLU A CG 1 ATOM 132 C CD . GLU A 1 16 ? 60.384 40.118 35.451 1.00 20.48 ? 16 GLU A CD 1 ATOM 133 O OE1 . GLU A 1 16 ? 60.759 39.220 34.663 1.00 19.74 ? 16 GLU A OE1 1 ATOM 134 O OE2 . GLU A 1 16 ? 60.296 39.944 36.696 1.00 20.98 ? 16 GLU A OE2 1 ATOM 135 N N . ALA A 1 17 ? 59.621 43.409 30.602 1.00 12.52 ? 17 ALA A N 1 ATOM 136 C CA . ALA A 1 17 ? 60.020 43.942 29.282 1.00 12.93 ? 17 ALA A CA 1 ATOM 137 C C . ALA A 1 17 ? 59.539 45.371 28.991 1.00 15.52 ? 17 ALA A C 1 ATOM 138 O O . ALA A 1 17 ? 59.882 45.941 27.917 1.00 18.82 ? 17 ALA A O 1 ATOM 139 C CB . ALA A 1 17 ? 59.540 43.022 28.150 1.00 13.14 ? 17 ALA A CB 1 ATOM 140 N N . GLY A 1 18 ? 58.761 45.963 29.903 1.00 15.53 ? 18 GLY A N 1 ATOM 141 C CA . GLY A 1 18 ? 58.347 47.344 29.727 1.00 14.31 ? 18 GLY A CA 1 ATOM 142 C C . GLY A 1 18 ? 57.105 47.464 28.895 1.00 14.49 ? 18 GLY A C 1 ATOM 143 O O . GLY A 1 18 ? 56.743 48.578 28.519 1.00 18.58 ? 18 GLY A O 1 ATOM 144 N N . ILE A 1 19 ? 56.431 46.329 28.634 1.00 11.84 ? 19 ILE A N 1 ATOM 145 C CA . ILE A 1 19 ? 55.215 46.342 27.822 1.00 12.99 ? 19 ILE A CA 1 ATOM 146 C C . ILE A 1 19 ? 53.956 46.471 28.603 1.00 11.47 ? 19 ILE A C 1 ATOM 147 O O . ILE A 1 19 ? 52.991 47.148 28.156 1.00 14.87 ? 19 ILE A O 1 ATOM 148 C CB . ILE A 1 19 ? 55.107 45.048 26.948 1.00 12.91 ? 19 ILE A CB 1 ATOM 149 C CG1 . ILE A 1 19 ? 56.405 44.843 26.211 1.00 15.43 ? 19 ILE A CG1 1 ATOM 150 C CG2 . ILE A 1 19 ? 53.997 45.161 25.962 1.00 19.04 ? 19 ILE A CG2 1 ATOM 151 C CD1 . ILE A 1 19 ? 56.855 45.972 25.311 1.00 21.27 ? 19 ILE A CD1 1 ATOM 152 N N . ASP A 1 20 ? 53.942 45.800 29.769 1.00 12.47 ? 20 ASP A N 1 ATOM 153 C CA . ASP A 1 20 ? 52.703 45.700 30.552 1.00 12.62 ? 20 ASP A CA 1 ATOM 154 C C . ASP A 1 20 ? 52.864 46.519 31.824 1.00 14.00 ? 20 ASP A C 1 ATOM 155 O O . ASP A 1 20 ? 53.626 46.143 32.733 1.00 12.97 ? 20 ASP A O 1 ATOM 156 C CB . ASP A 1 20 ? 52.442 44.221 30.861 1.00 15.45 ? 20 ASP A CB 1 ATOM 157 C CG . ASP A 1 20 ? 51.058 43.951 31.450 1.00 13.87 ? 20 ASP A CG 1 ATOM 158 O OD1 . ASP A 1 20 ? 50.505 44.919 32.061 1.00 12.21 ? 20 ASP A OD1 1 ATOM 159 O OD2 . ASP A 1 20 ? 50.557 42.771 31.344 1.00 14.53 ? 20 ASP A OD2 1 ATOM 160 N N . SER A 1 21 ? 52.101 47.644 31.886 1.00 12.81 ? 21 SER A N 1 ATOM 161 C CA . SER A 1 21 ? 52.098 48.541 33.022 1.00 13.79 ? 21 SER A CA 1 ATOM 162 C C . SER A 1 21 ? 51.397 48.043 34.248 1.00 11.53 ? 21 SER A C 1 ATOM 163 O O . SER A 1 21 ? 51.552 48.627 35.315 1.00 14.81 ? 21 SER A O 1 ATOM 164 C CB . SER A 1 21 ? 51.443 49.853 32.649 1.00 15.63 ? 21 SER A CB 1 ATOM 165 O OG . SER A 1 21 ? 50.079 49.739 32.376 1.00 17.15 ? 21 SER A OG 1 ATOM 166 N N . CYS A 1 22 ? 50.615 47.003 34.104 1.00 10.36 ? 22 CYS A N 1 ATOM 167 C CA . CYS A 1 22 ? 49.760 46.516 35.186 1.00 9.77 ? 22 CYS A CA 1 ATOM 168 C C . CYS A 1 22 ? 49.552 45.032 34.965 1.00 9.00 ? 22 CYS A C 1 ATOM 169 O O . CYS A 1 22 ? 48.480 44.624 34.496 1.00 10.68 ? 22 CYS A O 1 ATOM 170 C CB . CYS A 1 22 ? 48.443 47.294 35.186 1.00 12.24 ? 22 CYS A CB 1 ATOM 171 S SG . CYS A 1 22 ? 47.459 46.740 36.603 1.00 12.09 ? 22 CYS A SG 1 ATOM 172 N N . PRO A 1 23 ? 50.579 44.212 35.287 1.00 8.82 ? 23 PRO A N 1 ATOM 173 C CA . PRO A 1 23 ? 50.444 42.803 34.996 1.00 10.30 ? 23 PRO A CA 1 ATOM 174 C C . PRO A 1 23 ? 49.220 42.152 35.696 1.00 7.51 ? 23 PRO A C 1 ATOM 175 O O . PRO A 1 23 ? 48.630 41.212 35.165 1.00 12.21 ? 23 PRO A O 1 ATOM 176 C CB . PRO A 1 23 ? 51.732 42.217 35.515 1.00 11.63 ? 23 PRO A CB 1 ATOM 177 C CG . PRO A 1 23 ? 52.326 43.230 36.484 1.00 11.08 ? 23 PRO A CG 1 ATOM 178 C CD . PRO A 1 23 ? 51.870 44.537 35.893 1.00 10.84 ? 23 PRO A CD 1 ATOM 179 N N . GLU A 1 24 ? 48.865 42.689 36.878 1.00 7.75 ? 24 GLU A N 1 ATOM 180 C CA . GLU A 1 24 ? 47.755 42.200 37.693 1.00 7.08 ? 24 GLU A CA 1 ATOM 181 C C . GLU A 1 24 ? 46.411 42.583 37.123 1.00 9.07 ? 24 GLU A C 1 ATOM 182 O O . GLU A 1 24 ? 45.350 42.081 37.623 1.00 10.07 ? 24 GLU A O 1 ATOM 183 C CB . GLU A 1 24 ? 47.865 42.681 39.110 1.00 10.20 ? 24 GLU A CB 1 ATOM 184 C CG . GLU A 1 24 ? 47.654 44.181 39.391 1.00 10.65 ? 24 GLU A CG 1 ATOM 185 C CD . GLU A 1 24 ? 48.863 45.100 39.214 1.00 10.66 ? 24 GLU A CD 1 ATOM 186 O OE1 . GLU A 1 24 ? 49.914 44.678 38.675 1.00 10.71 ? 24 GLU A OE1 1 ATOM 187 O OE2 . GLU A 1 24 ? 48.715 46.268 39.603 1.00 10.97 ? 24 GLU A OE2 1 ATOM 188 N N . CYS A 1 25 ? 46.427 43.412 36.085 1.00 11.34 ? 25 CYS A N 1 ATOM 189 C CA . CYS A 1 25 ? 45.200 43.937 35.445 1.00 12.31 ? 25 CYS A CA 1 ATOM 190 C C . CYS A 1 25 ? 44.619 43.048 34.329 1.00 10.17 ? 25 CYS A C 1 ATOM 191 O O . CYS A 1 25 ? 43.661 43.430 33.706 1.00 14.09 ? 25 CYS A O 1 ATOM 192 C CB . CYS A 1 25 ? 45.472 45.337 34.829 1.00 13.19 ? 25 CYS A CB 1 ATOM 193 S SG . CYS A 1 25 ? 45.571 46.740 35.951 1.00 14.41 ? 25 CYS A SG 1 ATOM 194 N N . ALA A 1 26 ? 45.245 41.914 34.012 1.00 13.27 ? 26 ALA A N 1 ATOM 195 C CA . ALA A 1 26 ? 44.764 41.022 32.965 1.00 10.49 ? 26 ALA A CA 1 ATOM 196 C C . ALA A 1 26 ? 43.573 40.229 33.496 1.00 9.19 ? 26 ALA A C 1 ATOM 197 O O . ALA A 1 26 ? 43.740 39.286 34.299 1.00 11.74 ? 26 ALA A O 1 ATOM 198 C CB . ALA A 1 26 ? 45.825 40.081 32.488 1.00 13.18 ? 26 ALA A CB 1 ATOM 199 N N . ILE A 1 27 ? 42.372 40.615 33.011 1.00 10.58 ? 27 ILE A N 1 ATOM 200 C CA . ILE A 1 27 ? 41.121 40.152 33.632 1.00 12.68 ? 27 ILE A CA 1 ATOM 201 C C . ILE A 1 27 ? 40.144 39.711 32.574 1.00 10.80 ? 27 ILE A C 1 ATOM 202 O O . ILE A 1 27 ? 40.017 40.343 31.523 1.00 12.33 ? 27 ILE A O 1 ATOM 203 C CB . ILE A 1 27 ? 40.446 41.220 34.499 1.00 12.53 ? 27 ILE A CB 1 ATOM 204 C CG1 . ILE A 1 27 ? 41.411 41.858 35.472 1.00 16.85 ? 27 ILE A CG1 1 ATOM 205 C CG2 . ILE A 1 27 ? 39.253 40.631 35.297 1.00 20.41 ? 27 ILE A CG2 1 ATOM 206 C CD1 . ILE A 1 27 ? 40.867 42.953 36.395 1.00 19.92 ? 27 ILE A CD1 1 ATOM 207 N N . LEU A 1 28 ? 39.507 38.569 32.871 1.00 9.59 ? 28 LEU A N 1 ATOM 208 C CA . LEU A 1 28 ? 38.338 38.052 32.151 1.00 11.14 ? 28 LEU A CA 1 ATOM 209 C C . LEU A 1 28 ? 37.112 38.503 32.983 1.00 10.56 ? 28 LEU A C 1 ATOM 210 O O . LEU A 1 28 ? 36.892 38.025 34.094 1.00 9.54 ? 28 LEU A O 1 ATOM 211 C CB . LEU A 1 28 ? 38.396 36.554 32.010 1.00 11.01 ? 28 LEU A CB 1 ATOM 212 C CG . LEU A 1 28 ? 37.121 35.900 31.483 1.00 11.37 ? 28 LEU A CG 1 ATOM 213 C CD1 . LEU A 1 28 ? 36.738 36.401 30.123 1.00 14.44 ? 28 LEU A CD1 1 ATOM 214 C CD2 . LEU A 1 28 ? 37.283 34.385 31.462 1.00 14.83 ? 28 LEU A CD2 1 ATOM 215 N N . GLU A 1 29 ? 36.309 39.382 32.390 1.00 11.09 ? 29 GLU A N 1 ATOM 216 C CA . GLU A 1 29 ? 35.169 39.940 33.087 1.00 12.14 ? 29 GLU A CA 1 ATOM 217 C C . GLU A 1 29 ? 34.240 40.550 32.065 1.00 12.98 ? 29 GLU A C 1 ATOM 218 O O . GLU A 1 29 ? 34.652 40.988 31.006 1.00 15.79 ? 29 GLU A O 1 ATOM 219 C CB . GLU A 1 29 ? 35.571 41.006 34.109 1.00 16.06 ? 29 GLU A CB 1 ATOM 220 C CG . GLU A 1 29 ? 35.883 42.395 33.611 1.00 27.67 ? 29 GLU A CG 1 ATOM 221 C CD . GLU A 1 29 ? 35.772 43.510 34.725 1.00 45.15 ? 29 GLU A CD 1 ATOM 222 O OE1 . GLU A 1 29 ? 35.637 43.241 35.899 1.00 40.08 ? 29 GLU A OE1 1 ATOM 223 O OE2 . GLU A 1 29 ? 35.721 44.718 34.432 1.00 38.76 ? 29 GLU A OE2 1 ATOM 224 N N . PRO A 1 30 ? 32.988 40.678 32.416 1.00 13.41 ? 30 PRO A N 1 ATOM 225 C CA . PRO A 1 30 ? 32.314 40.056 33.555 1.00 13.87 ? 30 PRO A CA 1 ATOM 226 C C . PRO A 1 30 ? 31.978 38.599 33.231 1.00 11.26 ? 30 PRO A C 1 ATOM 227 O O . PRO A 1 30 ? 31.538 38.288 32.111 1.00 13.09 ? 30 PRO A O 1 ATOM 228 C CB . PRO A 1 30 ? 31.031 40.862 33.664 1.00 17.45 ? 30 PRO A CB 1 ATOM 229 C CG . PRO A 1 30 ? 30.729 41.203 32.250 1.00 18.26 ? 30 PRO A CG 1 ATOM 230 C CD . PRO A 1 30 ? 32.027 41.367 31.524 1.00 14.22 ? 30 PRO A CD 1 ATOM 231 N N . VAL A 1 31 ? 32.108 37.742 34.234 1.00 11.15 ? 31 VAL A N 1 ATOM 232 C CA . VAL A 1 31 ? 31.830 36.314 34.098 1.00 11.23 ? 31 VAL A CA 1 ATOM 233 C C . VAL A 1 31 ? 31.256 35.800 35.439 1.00 12.84 ? 31 VAL A C 1 ATOM 234 O O . VAL A 1 31 ? 31.482 36.398 36.491 1.00 14.19 ? 31 VAL A O 1 ATOM 235 C CB . VAL A 1 31 ? 33.055 35.521 33.668 1.00 12.55 ? 31 VAL A CB 1 ATOM 236 C CG1 . VAL A 1 31 ? 33.480 35.908 32.240 1.00 14.19 ? 31 VAL A CG1 1 ATOM 237 C CG2 . VAL A 1 31 ? 34.178 35.654 34.689 1.00 13.33 ? 31 VAL A CG2 1 ATOM 238 N N . SER A 1 32 ? 30.503 34.699 35.376 1.00 12.45 ? 32 SER A N 1 ATOM 239 C CA . SER A 1 32 ? 30.162 33.982 36.567 1.00 13.60 ? 32 SER A CA 1 ATOM 240 C C . SER A 1 32 ? 31.335 33.136 36.953 1.00 12.78 ? 32 SER A C 1 ATOM 241 O O . SER A 1 32 ? 31.503 32.073 36.401 1.00 13.68 ? 32 SER A O 1 ATOM 242 C CB . SER A 1 32 ? 28.941 33.069 36.359 1.00 15.06 ? 32 SER A CB 1 ATOM 243 O OG . SER A 1 32 ? 28.610 32.469 37.591 1.00 18.65 ? 32 SER A OG 1 ATOM 244 N N . SER A 1 33 ? 32.139 33.602 37.898 1.00 10.55 ? 33 SER A N 1 ATOM 245 C CA . SER A 1 33 ? 33.320 32.850 38.372 1.00 9.28 ? 33 SER A CA 1 ATOM 246 C C . SER A 1 33 ? 33.001 31.943 39.554 1.00 9.02 ? 33 SER A C 1 ATOM 247 O O . SER A 1 33 ? 33.794 31.102 39.906 1.00 10.44 ? 33 SER A O 1 ATOM 248 C CB . SER A 1 33 ? 34.414 33.846 38.798 1.00 8.73 ? 33 SER A CB 1 ATOM 249 O OG . SER A 1 33 ? 33.892 34.793 39.721 1.00 10.97 ? 33 SER A OG 1 ATOM 250 N N . TRP A 1 34 ? 31.826 32.111 40.158 1.00 10.66 ? 34 TRP A N 1 ATOM 251 C CA . TRP A 1 34 ? 31.483 31.409 41.396 1.00 11.96 ? 34 TRP A CA 1 ATOM 252 C C . TRP A 1 34 ? 29.989 31.093 41.361 1.00 13.38 ? 34 TRP A C 1 ATOM 253 O O . TRP A 1 34 ? 29.224 31.953 40.947 1.00 13.29 ? 34 TRP A O 1 ATOM 254 C CB . TRP A 1 34 ? 31.749 32.304 42.580 1.00 13.44 ? 34 TRP A CB 1 ATOM 255 C CG . TRP A 1 34 ? 31.866 31.580 43.851 1.00 11.27 ? 34 TRP A CG 1 ATOM 256 C CD1 . TRP A 1 34 ? 30.890 31.340 44.777 1.00 11.73 ? 34 TRP A CD1 1 ATOM 257 C CD2 . TRP A 1 34 ? 33.086 30.978 44.371 1.00 10.68 ? 34 TRP A CD2 1 ATOM 258 N NE1 . TRP A 1 34 ? 31.420 30.629 45.825 1.00 11.51 ? 34 TRP A NE1 1 ATOM 259 C CE2 . TRP A 1 34 ? 32.757 30.387 45.598 1.00 9.82 ? 34 TRP A CE2 1 ATOM 260 C CE3 . TRP A 1 34 ? 34.426 30.904 43.913 1.00 11.80 ? 34 TRP A CE3 1 ATOM 261 C CZ2 . TRP A 1 34 ? 33.699 29.736 46.368 1.00 12.53 ? 34 TRP A CZ2 1 ATOM 262 C CZ3 . TRP A 1 34 ? 35.327 30.238 44.642 1.00 12.80 ? 34 TRP A CZ3 1 ATOM 263 C CH2 . TRP A 1 34 ? 34.985 29.659 45.885 1.00 11.47 ? 34 TRP A CH2 1 ATOM 264 N N . PRO A 1 35 ? 29.590 29.895 41.807 1.00 13.47 ? 35 PRO A N 1 ATOM 265 C CA . PRO A 1 35 ? 30.359 28.766 42.343 1.00 14.92 ? 35 PRO A CA 1 ATOM 266 C C . PRO A 1 35 ? 30.821 27.728 41.353 1.00 12.07 ? 35 PRO A C 1 ATOM 267 O O . PRO A 1 35 ? 31.518 26.798 41.742 1.00 12.26 ? 35 PRO A O 1 ATOM 268 C CB . PRO A 1 35 ? 29.355 28.098 43.221 1.00 12.11 ? 35 PRO A CB 1 ATOM 269 C CG . PRO A 1 35 ? 27.964 28.405 42.624 1.00 15.53 ? 35 PRO A CG 1 ATOM 270 C CD . PRO A 1 35 ? 28.107 29.667 41.870 1.00 14.59 ? 35 PRO A CD 1 ATOM 271 N N . ASP A 1 36 ? 30.401 27.861 40.080 1.00 10.79 ? 36 ASP A N 1 ATOM 272 C CA . ASP A 1 36 ? 30.705 26.848 39.099 1.00 13.26 ? 36 ASP A CA 1 ATOM 273 C C . ASP A 1 36 ? 31.980 27.275 38.394 1.00 11.82 ? 36 ASP A C 1 ATOM 274 O O . ASP A 1 36 ? 31.991 28.144 37.546 1.00 11.91 ? 36 ASP A O 1 ATOM 275 C CB . ASP A 1 36 ? 29.519 26.582 38.149 1.00 15.02 ? 36 ASP A CB 1 ATOM 276 C CG . ASP A 1 36 ? 29.750 25.352 37.280 1.00 15.81 ? 36 ASP A CG 1 ATOM 277 O OD1 . ASP A 1 36 ? 30.885 25.172 36.853 1.00 19.44 ? 36 ASP A OD1 1 ATOM 278 O OD2 . ASP A 1 36 ? 28.847 24.552 37.039 1.00 28.33 ? 36 ASP A OD2 1 ATOM 279 N N . LEU A 1 37 ? 33.058 26.682 38.848 1.00 12.21 ? 37 LEU A N 1 ATOM 280 C CA . LEU A 1 37 ? 34.404 27.195 38.530 1.00 9.43 ? 37 LEU A CA 1 ATOM 281 C C . LEU A 1 37 ? 34.789 27.068 37.047 1.00 8.50 ? 37 LEU A C 1 ATOM 282 O O . LEU A 1 37 ? 35.679 27.808 36.573 1.00 11.93 ? 37 LEU A O 1 ATOM 283 C CB . LEU A 1 37 ? 35.432 26.477 39.393 1.00 10.77 ? 37 LEU A CB 1 ATOM 284 C CG . LEU A 1 37 ? 35.261 26.615 40.876 1.00 11.23 ? 37 LEU A CG 1 ATOM 285 C CD1 . LEU A 1 37 ? 36.327 25.881 41.632 1.00 9.94 ? 37 LEU A CD1 1 ATOM 286 C CD2 . LEU A 1 37 ? 35.293 28.069 41.321 1.00 12.19 ? 37 LEU A CD2 1 ATOM 287 N N . ASP A 1 38 ? 34.181 26.122 36.319 1.00 11.44 ? 38 ASP A N 1 ATOM 288 C CA . ASP A 1 38 ? 34.616 25.905 34.946 1.00 12.86 ? 38 ASP A CA 1 ATOM 289 C C . ASP A 1 38 ? 33.592 26.312 33.904 1.00 11.33 ? 38 ASP A C 1 ATOM 290 O O . ASP A 1 38 ? 33.784 26.087 32.682 1.00 15.32 ? 38 ASP A O 1 ATOM 291 C CB . ASP A 1 38 ? 35.074 24.405 34.720 1.00 14.69 ? 38 ASP A CB 1 ATOM 292 C CG . ASP A 1 38 ? 33.893 23.457 34.933 1.00 19.82 ? 38 ASP A CG 1 ATOM 293 O OD1 . ASP A 1 38 ? 32.781 23.969 35.143 1.00 16.13 ? 38 ASP A OD1 1 ATOM 294 O OD2 . ASP A 1 38 ? 34.047 22.229 34.886 1.00 28.24 ? 38 ASP A OD2 1 ATOM 295 N N . ALA A 1 39 ? 32.507 26.891 34.410 1.00 10.18 ? 39 ALA A N 1 ATOM 296 C CA . ALA A 1 39 ? 31.425 27.215 33.499 1.00 12.90 ? 39 ALA A CA 1 ATOM 297 C C . ALA A 1 39 ? 31.697 28.364 32.497 1.00 12.35 ? 39 ALA A C 1 ATOM 298 O O . ALA A 1 39 ? 31.233 28.300 31.319 1.00 15.04 ? 39 ALA A O 1 ATOM 299 C CB . ALA A 1 39 ? 30.124 27.471 34.250 1.00 13.72 ? 39 ALA A CB 1 ATOM 300 N N . ALA A 1 40 ? 32.289 29.450 32.973 1.00 10.93 ? 40 ALA A N 1 ATOM 301 C CA . ALA A 1 40 ? 32.402 30.661 32.184 1.00 10.96 ? 40 ALA A CA 1 ATOM 302 C C . ALA A 1 40 ? 33.387 30.455 31.020 1.00 9.46 ? 40 ALA A C 1 ATOM 303 O O . ALA A 1 40 ? 34.483 29.969 31.236 1.00 11.43 ? 40 ALA A O 1 ATOM 304 C CB . ALA A 1 40 ? 32.860 31.789 33.036 1.00 14.26 ? 40 ALA A CB 1 ATOM 305 N N . PRO A 1 41 ? 32.939 30.705 29.754 1.00 9.61 ? 41 PRO A N 1 ATOM 306 C CA . PRO A 1 41 ? 33.901 30.653 28.664 1.00 11.67 ? 41 PRO A CA 1 ATOM 307 C C . PRO A 1 41 ? 35.030 31.617 28.827 1.00 9.38 ? 41 PRO A C 1 ATOM 308 O O . PRO A 1 41 ? 34.855 32.743 29.394 1.00 10.06 ? 41 PRO A O 1 ATOM 309 C CB . PRO A 1 41 ? 33.081 31.055 27.443 1.00 11.23 ? 41 PRO A CB 1 ATOM 310 C CG . PRO A 1 41 ? 31.758 31.472 27.916 1.00 19.49 ? 41 PRO A CG 1 ATOM 311 C CD . PRO A 1 41 ? 31.609 31.183 29.354 1.00 11.49 ? 41 PRO A CD 1 ATOM 312 N N . VAL A 1 42 ? 36.187 31.239 28.283 1.00 9.25 ? 42 VAL A N 1 ATOM 313 C CA . VAL A 1 42 ? 37.326 32.143 28.398 1.00 8.85 ? 42 VAL A CA 1 ATOM 314 C C . VAL A 1 42 ? 37.442 33.265 27.374 1.00 9.35 ? 42 VAL A C 1 ATOM 315 O O . VAL A 1 42 ? 38.285 34.170 27.573 1.00 9.72 ? 42 VAL A O 1 ATOM 316 C CB . VAL A 1 42 ? 38.652 31.346 28.475 1.00 9.51 ? 42 VAL A CB 1 ATOM 317 C CG1 . VAL A 1 42 ? 38.639 30.489 29.746 1.00 12.06 ? 42 VAL A CG1 1 ATOM 318 C CG2 . VAL A 1 42 ? 38.944 30.573 27.213 1.00 14.35 ? 42 VAL A CG2 1 ATOM 319 N N . GLY A 1 43 ? 36.605 33.281 26.340 1.00 11.48 ? 43 GLY A N 1 ATOM 320 C CA . GLY A 1 43 ? 36.598 34.339 25.330 1.00 9.93 ? 43 GLY A CA 1 ATOM 321 C C . GLY A 1 43 ? 37.979 34.722 24.864 1.00 9.24 ? 43 GLY A C 1 ATOM 322 O O . GLY A 1 43 ? 38.798 33.889 24.580 1.00 10.49 ? 43 GLY A O 1 ATOM 323 N N . ARG A 1 44 ? 38.172 36.007 24.733 1.00 10.60 ? 44 ARG A N 1 ATOM 324 C CA . ARG A 1 44 ? 39.456 36.583 24.250 1.00 11.59 ? 44 ARG A CA 1 ATOM 325 C C . ARG A 1 44 ? 40.591 36.299 25.199 1.00 8.29 ? 44 ARG A C 1 ATOM 326 O O . ARG A 1 44 ? 41.790 36.315 24.808 1.00 10.21 ? 44 ARG A O 1 ATOM 327 C CB . ARG A 1 44 ? 39.263 38.095 24.107 1.00 19.02 ? 44 ARG A CB 1 ATOM 328 C CG . ARG A 1 44 ? 40.364 38.781 23.421 1.00 19.60 ? 44 ARG A CG 1 ATOM 329 C CD . ARG A 1 44 ? 40.073 40.243 23.341 1.00 27.49 ? 44 ARG A CD 1 ATOM 330 N NE . ARG A 1 44 ? 40.941 40.830 22.337 1.00 29.76 ? 44 ARG A NE 1 ATOM 331 C CZ . ARG A 1 44 ? 40.883 42.104 21.958 1.00 33.91 ? 44 ARG A CZ 1 ATOM 332 N NH1 . ARG A 1 44 ? 39.962 42.908 22.510 1.00 30.45 ? 44 ARG A NH1 1 ATOM 333 N NH2 . ARG A 1 44 ? 41.745 42.565 21.017 1.00 44.80 ? 44 ARG A NH2 1 ATOM 334 N N . SER A 1 45 ? 40.290 36.102 26.486 1.00 9.32 ? 45 SER A N 1 ATOM 335 C CA . SER A 1 45 ? 41.377 35.931 27.473 1.00 7.18 ? 45 SER A CA 1 ATOM 336 C C . SER A 1 45 ? 42.170 34.673 27.252 1.00 7.16 ? 45 SER A C 1 ATOM 337 O O . SER A 1 45 ? 43.434 34.662 27.348 1.00 9.49 ? 45 SER A O 1 ATOM 338 C CB . SER A 1 45 ? 40.751 35.942 28.872 1.00 8.96 ? 45 SER A CB 1 ATOM 339 O OG . SER A 1 45 ? 40.250 37.204 29.255 1.00 11.91 ? 45 SER A OG 1 ATOM 340 N N . GLY A 1 46 ? 41.480 33.582 26.922 1.00 8.72 ? 46 GLY A N 1 ATOM 341 C CA . GLY A 1 46 ? 42.123 32.340 26.619 1.00 8.69 ? 46 GLY A CA 1 ATOM 342 C C . GLY A 1 46 ? 42.891 31.792 27.857 1.00 8.17 ? 46 GLY A C 1 ATOM 343 O O . GLY A 1 46 ? 42.728 32.247 29.004 1.00 11.04 ? 46 GLY A O 1 ATOM 344 N N . PRO A 1 47 ? 43.732 30.791 27.638 1.00 10.40 ? 47 PRO A N 1 ATOM 345 C CA . PRO A 1 47 ? 44.472 30.207 28.779 1.00 9.25 ? 47 PRO A CA 1 ATOM 346 C C . PRO A 1 47 ? 45.640 31.073 29.253 1.00 11.78 ? 47 PRO A C 1 ATOM 347 O O . PRO A 1 47 ? 46.227 30.808 30.304 1.00 11.94 ? 47 PRO A O 1 ATOM 348 C CB . PRO A 1 47 ? 45.015 28.919 28.178 1.00 10.80 ? 47 PRO A CB 1 ATOM 349 C CG . PRO A 1 47 ? 45.092 29.175 26.659 1.00 15.10 ? 47 PRO A CG 1 ATOM 350 C CD . PRO A 1 47 ? 43.879 30.022 26.390 1.00 11.18 ? 47 PRO A CD 1 ATOM 351 N N . CYS A 1 48 ? 46.066 32.021 28.433 1.00 8.52 ? 48 CYS A N 1 ATOM 352 C CA . CYS A 1 48 ? 47.259 32.845 28.783 1.00 9.05 ? 48 CYS A CA 1 ATOM 353 C C . CYS A 1 48 ? 46.907 34.276 29.261 1.00 10.25 ? 48 CYS A C 1 ATOM 354 O O . CYS A 1 48 ? 47.787 34.997 29.744 1.00 9.50 ? 48 CYS A O 1 ATOM 355 C CB . CYS A 1 48 ? 48.258 32.924 27.600 1.00 11.46 ? 48 CYS A CB 1 ATOM 356 S SG . CYS A 1 48 ? 49.039 31.350 27.240 1.00 13.28 ? 48 CYS A SG 1 ATOM 357 N N . GLY A 1 49 ? 45.660 34.699 29.066 1.00 8.25 ? 49 GLY A N 1 ATOM 358 C CA . GLY A 1 49 ? 45.261 36.029 29.446 1.00 10.28 ? 49 GLY A CA 1 ATOM 359 C C . GLY A 1 49 ? 45.318 37.057 28.314 1.00 7.36 ? 49 GLY A C 1 ATOM 360 O O . GLY A 1 49 ? 46.141 36.972 27.372 1.00 9.63 ? 49 GLY A O 1 ATOM 361 N N . TYR A 1 50 ? 44.417 38.036 28.469 1.00 8.30 ? 50 TYR A N 1 ATOM 362 C CA . TYR A 1 50 ? 44.357 39.252 27.667 1.00 8.32 ? 50 TYR A CA 1 ATOM 363 C C . TYR A 1 50 ? 44.351 40.435 28.675 1.00 8.10 ? 50 TYR A C 1 ATOM 364 O O . TYR A 1 50 ? 43.462 40.501 29.539 1.00 10.47 ? 50 TYR A O 1 ATOM 365 C CB . TYR A 1 50 ? 43.082 39.305 26.773 1.00 8.90 ? 50 TYR A CB 1 ATOM 366 C CG . TYR A 1 50 ? 43.111 40.528 25.903 1.00 10.95 ? 50 TYR A CG 1 ATOM 367 C CD1 . TYR A 1 50 ? 43.726 40.507 24.661 1.00 13.33 ? 50 TYR A CD1 1 ATOM 368 C CD2 . TYR A 1 50 ? 42.540 41.719 26.324 1.00 14.96 ? 50 TYR A CD2 1 ATOM 369 C CE1 . TYR A 1 50 ? 43.784 41.647 23.896 1.00 15.89 ? 50 TYR A CE1 1 ATOM 370 C CE2 . TYR A 1 50 ? 42.605 42.871 25.561 1.00 16.36 ? 50 TYR A CE2 1 ATOM 371 C CZ . TYR A 1 50 ? 43.214 42.835 24.354 1.00 15.26 ? 50 TYR A CZ 1 ATOM 372 O OH . TYR A 1 50 ? 43.242 43.979 23.598 1.00 21.88 ? 50 TYR A OH 1 ATOM 373 N N . ASN A 1 51 ? 45.262 41.381 28.529 1.00 10.39 ? 51 ASN A N 1 ATOM 374 C CA . ASN A 1 51 ? 45.307 42.551 29.393 1.00 10.14 ? 51 ASN A CA 1 ATOM 375 C C . ASN A 1 51 ? 44.765 43.773 28.668 1.00 9.05 ? 51 ASN A C 1 ATOM 376 O O . ASN A 1 51 ? 45.399 44.318 27.720 1.00 12.23 ? 51 ASN A O 1 ATOM 377 C CB . ASN A 1 51 ? 46.729 42.830 29.865 1.00 10.63 ? 51 ASN A CB 1 ATOM 378 C CG . ASN A 1 51 ? 46.757 43.716 31.114 1.00 13.75 ? 51 ASN A CG 1 ATOM 379 O OD1 . ASN A 1 51 ? 45.814 44.483 31.341 1.00 17.66 ? 51 ASN A OD1 1 ATOM 380 N ND2 . ASN A 1 51 ? 47.787 43.556 31.965 1.00 14.89 ? 51 ASN A ND2 1 ATOM 381 N N . ALA A 1 52 ? 43.551 44.139 29.041 1.00 12.46 ? 52 ALA A N 1 ATOM 382 C CA . ALA A 1 52 ? 42.894 45.320 28.482 1.00 14.29 ? 52 ALA A CA 1 ATOM 383 C C . ALA A 1 52 ? 43.595 46.625 28.818 1.00 13.53 ? 52 ALA A C 1 ATOM 384 O O . ALA A 1 52 ? 43.434 47.580 28.092 1.00 19.97 ? 52 ALA A O 1 ATOM 385 C CB . ALA A 1 52 ? 41.414 45.373 28.895 1.00 16.50 ? 52 ALA A CB 1 ATOM 386 N N . ARG A 1 53 ? 44.466 46.656 29.858 1.00 13.47 ? 53 ARG A N 1 ATOM 387 C CA . ARG A 1 53 ? 45.127 47.916 30.245 1.00 15.97 ? 53 ARG A CA 1 ATOM 388 C C . ARG A 1 53 ? 46.019 48.420 29.112 1.00 17.86 ? 53 ARG A C 1 ATOM 389 O O . ARG A 1 53 ? 45.838 49.553 28.649 1.00 19.84 ? 53 ARG A O 1 ATOM 390 C CB . ARG A 1 53 ? 45.875 47.736 31.532 1.00 16.82 ? 53 ARG A CB 1 ATOM 391 C CG . ARG A 1 53 ? 46.577 48.961 32.040 1.00 19.78 ? 53 ARG A CG 1 ATOM 392 C CD . ARG A 1 53 ? 45.660 50.131 32.316 1.00 23.86 ? 53 ARG A CD 1 ATOM 393 N NE . ARG A 1 53 ? 44.574 49.862 33.275 1.00 25.43 ? 53 ARG A NE 1 ATOM 394 C CZ . ARG A 1 53 ? 44.649 50.025 34.602 1.00 27.60 ? 53 ARG A CZ 1 ATOM 395 N NH1 . ARG A 1 53 ? 45.782 50.413 35.173 1.00 28.27 ? 53 ARG A NH1 1 ATOM 396 N NH2 . ARG A 1 53 ? 43.565 49.797 35.365 1.00 28.06 ? 53 ARG A NH2 1 ATOM 397 N N . ASP A 1 54 ? 46.928 47.576 28.636 1.00 18.22 ? 54 ASP A N 1 ATOM 398 C CA . ASP A 1 54 ? 47.733 47.950 27.497 1.00 18.54 ? 54 ASP A CA 1 ATOM 399 C C . ASP A 1 54 ? 47.438 47.177 26.195 1.00 14.66 ? 54 ASP A C 1 ATOM 400 O O . ASP A 1 54 ? 48.298 47.230 25.239 1.00 19.80 ? 54 ASP A O 1 ATOM 401 C CB . ASP A 1 54 ? 49.229 47.824 27.842 1.00 19.43 ? 54 ASP A CB 1 ATOM 402 C CG . ASP A 1 54 ? 49.657 48.777 28.957 1.00 23.98 ? 54 ASP A CG 1 ATOM 403 O OD1 . ASP A 1 54 ? 49.680 49.992 28.646 1.00 26.93 ? 54 ASP A OD1 1 ATOM 404 O OD2 . ASP A 1 54 ? 49.952 48.314 30.131 1.00 19.37 ? 54 ASP A OD2 1 ATOM 405 N N . SER A 1 55 ? 46.280 46.493 26.125 1.00 12.90 ? 55 SER A N 1 ATOM 406 C CA . SER A 1 55 ? 45.844 45.721 24.960 1.00 13.09 ? 55 SER A CA 1 ATOM 407 C C . SER A 1 55 ? 46.857 44.657 24.568 1.00 13.46 ? 55 SER A C 1 ATOM 408 O O . SER A 1 55 ? 47.371 44.676 23.478 1.00 16.84 ? 55 SER A O 1 ATOM 409 C CB . SER A 1 55 ? 45.523 46.647 23.790 1.00 22.03 ? 55 SER A CB 1 ATOM 410 O OG . SER A 1 55 ? 44.602 47.632 24.225 1.00 23.11 ? 55 SER A OG 1 ATOM 411 N N . ILE A 1 56 ? 47.140 43.746 25.493 1.00 10.32 ? 56 ILE A N 1 ATOM 412 C CA . ILE A 1 56 ? 48.169 42.728 25.281 1.00 10.41 ? 56 ILE A CA 1 ATOM 413 C C . ILE A 1 56 ? 47.472 41.359 25.275 1.00 9.59 ? 56 ILE A C 1 ATOM 414 O O . ILE A 1 56 ? 46.838 40.967 26.253 1.00 10.12 ? 56 ILE A O 1 ATOM 415 C CB . ILE A 1 56 ? 49.228 42.723 26.374 1.00 10.52 ? 56 ILE A CB 1 ATOM 416 C CG1 . ILE A 1 56 ? 49.938 44.088 26.491 1.00 10.38 ? 56 ILE A CG1 1 ATOM 417 C CG2 . ILE A 1 56 ? 50.246 41.620 26.083 1.00 13.38 ? 56 ILE A CG2 1 ATOM 418 C CD1 . ILE A 1 56 ? 50.697 44.285 27.810 1.00 14.50 ? 56 ILE A CD1 1 ATOM 419 N N . ASP A 1 57 ? 47.678 40.623 24.182 1.00 9.71 ? 57 ASP A N 1 ATOM 420 C CA . ASP A 1 57 ? 47.173 39.242 24.061 1.00 9.71 ? 57 ASP A CA 1 ATOM 421 C C . ASP A 1 57 ? 48.364 38.289 24.312 1.00 8.34 ? 57 ASP A C 1 ATOM 422 O O . ASP A 1 57 ? 49.242 38.131 23.477 1.00 10.00 ? 57 ASP A O 1 ATOM 423 C CB . ASP A 1 57 ? 46.496 38.970 22.688 1.00 9.78 ? 57 ASP A CB 1 ATOM 424 C CG . ASP A 1 57 ? 45.726 37.672 22.705 1.00 8.60 ? 57 ASP A CG 1 ATOM 425 O OD1 . ASP A 1 57 ? 46.159 36.703 23.428 1.00 10.17 ? 57 ASP A OD1 1 ATOM 426 O OD2 . ASP A 1 57 ? 44.621 37.686 22.074 1.00 11.89 ? 57 ASP A OD2 1 ATOM 427 N N . TYR A 1 58 ? 48.393 37.713 25.544 1.00 7.72 ? 58 TYR A N 1 ATOM 428 C CA . TYR A 1 58 ? 49.494 36.812 25.913 1.00 8.81 ? 58 TYR A CA 1 ATOM 429 C C . TYR A 1 58 ? 49.419 35.434 25.291 1.00 10.30 ? 58 TYR A C 1 ATOM 430 O O . TYR A 1 58 ? 50.290 34.580 25.518 1.00 10.72 ? 58 TYR A O 1 ATOM 431 C CB . TYR A 1 58 ? 49.617 36.724 27.424 1.00 10.14 ? 58 TYR A CB 1 ATOM 432 C CG . TYR A 1 58 ? 50.170 37.962 28.024 1.00 9.54 ? 58 TYR A CG 1 ATOM 433 C CD1 . TYR A 1 58 ? 51.514 38.313 27.797 1.00 10.61 ? 58 TYR A CD1 1 ATOM 434 C CD2 . TYR A 1 58 ? 49.396 38.765 28.846 1.00 11.41 ? 58 TYR A CD2 1 ATOM 435 C CE1 . TYR A 1 58 ? 52.030 39.424 28.316 1.00 11.68 ? 58 TYR A CE1 1 ATOM 436 C CE2 . TYR A 1 58 ? 49.967 39.902 29.445 1.00 13.12 ? 58 TYR A CE2 1 ATOM 437 C CZ . TYR A 1 58 ? 51.285 40.203 29.167 1.00 12.87 ? 58 TYR A CZ 1 ATOM 438 O OH . TYR A 1 58 ? 51.948 41.343 29.671 1.00 12.95 ? 58 TYR A OH 1 ATOM 439 N N . ASN A 1 59 ? 48.351 35.155 24.534 1.00 8.51 ? 59 ASN A N 1 ATOM 440 C CA . ASN A 1 59 ? 48.228 33.897 23.900 1.00 7.78 ? 59 ASN A CA 1 ATOM 441 C C . ASN A 1 59 ? 49.109 33.690 22.669 1.00 10.10 ? 59 ASN A C 1 ATOM 442 O O . ASN A 1 59 ? 49.120 32.615 22.119 1.00 13.67 ? 59 ASN A O 1 ATOM 443 C CB . ASN A 1 59 ? 46.772 33.629 23.511 1.00 7.72 ? 59 ASN A CB 1 ATOM 444 C CG . ASN A 1 59 ? 45.869 33.545 24.744 1.00 9.76 ? 59 ASN A CG 1 ATOM 445 O OD1 . ASN A 1 59 ? 45.847 32.504 25.448 1.00 9.53 ? 59 ASN A OD1 1 ATOM 446 N ND2 . ASN A 1 59 ? 45.150 34.655 25.049 1.00 8.48 ? 59 ASN A ND2 1 ATOM 447 N N . GLN A 1 60 ? 49.789 34.722 22.212 1.00 12.68 ? 60 GLN A N 1 ATOM 448 C CA . GLN A 1 60 ? 50.765 34.502 21.211 1.00 16.22 ? 60 GLN A CA 1 ATOM 449 C C . GLN A 1 60 ? 52.062 35.102 21.622 1.00 17.47 ? 60 GLN A C 1 ATOM 450 O O . GLN A 1 60 ? 52.120 36.177 22.241 1.00 21.30 ? 60 GLN A O 1 ATOM 451 C CB . GLN A 1 60 ? 50.386 34.984 19.853 1.00 23.82 ? 60 GLN A CB 1 ATOM 452 C CG . GLN A 1 60 ? 50.389 36.448 19.688 1.00 23.96 ? 60 GLN A CG 1 ATOM 453 C CD . GLN A 1 60 ? 50.166 37.005 18.258 1.00 26.92 ? 60 GLN A CD 1 ATOM 454 O OE1 . GLN A 1 60 ? 50.552 36.493 17.213 1.00 31.80 ? 60 GLN A OE1 1 ATOM 455 N NE2 . GLN A 1 60 ? 49.570 38.104 18.258 1.00 31.15 ? 60 GLN A NE2 1 ATOM 456 N N . PRO A 1 61 ? 53.129 34.398 21.343 1.00 11.97 ? 61 PRO A N 1 ATOM 457 C CA . PRO A 1 61 ? 54.471 34.946 21.620 1.00 11.16 ? 61 PRO A CA 1 ATOM 458 C C . PRO A 1 61 ? 54.802 36.221 20.895 1.00 10.51 ? 61 PRO A C 1 ATOM 459 O O . PRO A 1 61 ? 54.218 36.505 19.819 1.00 12.95 ? 61 PRO A O 1 ATOM 460 C CB . PRO A 1 61 ? 55.420 33.831 21.111 1.00 15.11 ? 61 PRO A CB 1 ATOM 461 C CG . PRO A 1 61 ? 54.540 32.642 20.993 1.00 17.24 ? 61 PRO A CG 1 ATOM 462 C CD . PRO A 1 61 ? 53.222 33.171 20.558 1.00 15.35 ? 61 PRO A CD 1 ATOM 463 N N . THR A 1 62 ? 55.768 36.947 21.457 1.00 9.52 ? 62 THR A N 1 ATOM 464 C CA . THR A 1 62 ? 56.348 38.138 20.848 1.00 11.66 ? 62 THR A CA 1 ATOM 465 C C . THR A 1 62 ? 57.843 38.032 21.104 1.00 11.74 ? 62 THR A C 1 ATOM 466 O O . THR A 1 62 ? 58.326 37.027 21.635 1.00 15.07 ? 62 THR A O 1 ATOM 467 C CB . THR A 1 62 ? 55.786 39.424 21.508 1.00 12.97 ? 62 THR A CB 1 ATOM 468 O OG1 . THR A 1 62 ? 56.220 39.484 22.874 1.00 13.26 ? 62 THR A OG1 1 ATOM 469 C CG2 . THR A 1 62 ? 54.244 39.501 21.398 1.00 14.20 ? 62 THR A CG2 1 ATOM 470 N N . THR A 1 63 ? 58.605 39.075 20.754 1.00 15.88 ? 63 THR A N 1 ATOM 471 C CA . THR A 1 63 ? 60.019 39.115 21.039 1.00 15.03 ? 63 THR A CA 1 ATOM 472 C C . THR A 1 63 ? 60.242 39.079 22.578 1.00 15.31 ? 63 THR A C 1 ATOM 473 O O . THR A 1 63 ? 61.355 38.728 23.013 1.00 23.35 ? 63 THR A O 1 ATOM 474 C CB . THR A 1 63 ? 60.654 40.355 20.411 1.00 18.56 ? 63 THR A CB 1 ATOM 475 O OG1 . THR A 1 63 ? 60.072 41.568 20.937 1.00 25.74 ? 63 THR A OG1 1 ATOM 476 C CG2 . THR A 1 63 ? 60.495 40.318 18.958 1.00 31.58 ? 63 THR A CG2 1 ATOM 477 N N . ASN A 1 64 ? 59.191 39.376 23.365 1.00 13.63 ? 64 ASN A N 1 ATOM 478 C CA . ASN A 1 64 ? 59.322 39.510 24.831 1.00 14.72 ? 64 ASN A CA 1 ATOM 479 C C . ASN A 1 64 ? 58.830 38.389 25.666 1.00 15.36 ? 64 ASN A C 1 ATOM 480 O O . ASN A 1 64 ? 59.088 38.391 26.889 1.00 14.40 ? 64 ASN A O 1 ATOM 481 C CB . ASN A 1 64 ? 58.719 40.835 25.329 1.00 16.43 ? 64 ASN A CB 1 ATOM 482 C CG . ASN A 1 64 ? 59.461 42.034 24.759 1.00 14.21 ? 64 ASN A CG 1 ATOM 483 O OD1 . ASN A 1 64 ? 60.664 42.117 24.882 1.00 18.01 ? 64 ASN A OD1 1 ATOM 484 N ND2 . ASN A 1 64 ? 58.732 42.906 24.017 1.00 19.63 ? 64 ASN A ND2 1 ATOM 485 N N . TRP A 1 65 ? 58.071 37.462 25.071 1.00 11.27 ? 65 TRP A N 1 ATOM 486 C CA . TRP A 1 65 ? 57.628 36.280 25.772 1.00 12.17 ? 65 TRP A CA 1 ATOM 487 C C . TRP A 1 65 ? 57.224 35.178 24.774 1.00 12.07 ? 65 TRP A C 1 ATOM 488 O O . TRP A 1 65 ? 56.868 35.450 23.621 1.00 13.22 ? 65 TRP A O 1 ATOM 489 C CB . TRP A 1 65 ? 56.460 36.561 26.712 1.00 12.86 ? 65 TRP A CB 1 ATOM 490 C CG . TRP A 1 65 ? 55.235 37.116 25.970 1.00 11.51 ? 65 TRP A CG 1 ATOM 491 C CD1 . TRP A 1 65 ? 54.342 36.431 25.176 1.00 14.19 ? 65 TRP A CD1 1 ATOM 492 C CD2 . TRP A 1 65 ? 54.857 38.494 25.882 1.00 11.87 ? 65 TRP A CD2 1 ATOM 493 N NE1 . TRP A 1 65 ? 53.437 37.312 24.603 1.00 14.50 ? 65 TRP A NE1 1 ATOM 494 C CE2 . TRP A 1 65 ? 53.789 38.588 24.979 1.00 13.71 ? 65 TRP A CE2 1 ATOM 495 C CE3 . TRP A 1 65 ? 55.394 39.679 26.405 1.00 13.01 ? 65 TRP A CE3 1 ATOM 496 C CZ2 . TRP A 1 65 ? 53.185 39.815 24.684 1.00 11.94 ? 65 TRP A CZ2 1 ATOM 497 C CZ3 . TRP A 1 65 ? 54.823 40.899 26.079 1.00 13.21 ? 65 TRP A CZ3 1 ATOM 498 C CH2 . TRP A 1 65 ? 53.686 40.945 25.266 1.00 13.47 ? 65 TRP A CH2 1 ATOM 499 N N . GLY A 1 66 ? 57.264 33.938 25.265 1.00 12.59 ? 66 GLY A N 1 ATOM 500 C CA . GLY A 1 66 ? 56.712 32.780 24.539 1.00 11.86 ? 66 GLY A CA 1 ATOM 501 C C . GLY A 1 66 ? 57.619 32.095 23.558 1.00 12.82 ? 66 GLY A C 1 ATOM 502 O O . GLY A 1 66 ? 57.218 31.081 22.962 1.00 14.26 ? 66 GLY A O 1 ATOM 503 N N . SER A 1 67 ? 58.831 32.591 23.387 1.00 15.73 ? 67 SER A N 1 ATOM 504 C CA . SER A 1 67 ? 59.749 31.972 22.399 1.00 14.51 ? 67 SER A CA 1 ATOM 505 C C . SER A 1 67 ? 60.330 30.657 22.883 1.00 17.28 ? 67 SER A C 1 ATOM 506 O O . SER A 1 67 ? 60.513 29.672 22.111 1.00 21.65 ? 67 SER A O 1 ATOM 507 C CB . SER A 1 67 ? 60.893 32.905 22.021 1.00 27.19 ? 67 SER A CB 1 ATOM 508 O OG . SER A 1 67 ? 60.383 33.944 21.206 1.00 35.05 ? 67 SER A OG 1 ATOM 509 N N . ASP A 1 68 ? 60.649 30.641 24.159 1.00 17.46 ? 68 ASP A N 1 ATOM 510 C CA . ASP A 1 68 ? 61.295 29.489 24.726 1.00 18.47 ? 68 ASP A CA 1 ATOM 511 C C . ASP A 1 68 ? 60.795 29.284 26.135 1.00 16.51 ? 68 ASP A C 1 ATOM 512 O O . ASP A 1 68 ? 60.123 30.163 26.715 1.00 17.11 ? 68 ASP A O 1 ATOM 513 C CB . ASP A 1 68 ? 62.804 29.695 24.753 1.00 27.45 ? 68 ASP A CB 1 ATOM 514 C CG . ASP A 1 68 ? 63.431 29.582 23.358 1.00 33.89 ? 68 ASP A CG 1 ATOM 515 O OD1 . ASP A 1 68 ? 63.573 28.438 22.787 1.00 42.70 ? 68 ASP A OD1 1 ATOM 516 O OD2 . ASP A 1 68 ? 63.769 30.667 22.841 1.00 38.19 ? 68 ASP A OD2 1 ATOM 517 N N . ALA A 1 69 ? 61.109 28.117 26.648 1.00 15.63 ? 69 ALA A N 1 ATOM 518 C CA . ALA A 1 69 ? 60.800 27.787 28.063 1.00 10.54 ? 69 ALA A CA 1 ATOM 519 C C . ALA A 1 69 ? 61.566 28.654 29.023 1.00 11.51 ? 69 ALA A C 1 ATOM 520 O O . ALA A 1 69 ? 62.768 28.839 28.826 1.00 15.97 ? 69 ALA A O 1 ATOM 521 C CB . ALA A 1 69 ? 61.046 26.333 28.357 1.00 13.50 ? 69 ALA A CB 1 ATOM 522 N N . VAL A 1 70 ? 60.898 29.146 30.067 1.00 10.37 ? 70 VAL A N 1 ATOM 523 C CA . VAL A 1 70 ? 61.566 29.941 31.107 1.00 11.78 ? 70 VAL A CA 1 ATOM 524 C C . VAL A 1 70 ? 62.304 29.050 32.159 1.00 11.88 ? 70 VAL A C 1 ATOM 525 O O . VAL A 1 70 ? 63.220 29.510 32.887 1.00 14.31 ? 70 VAL A O 1 ATOM 526 C CB . VAL A 1 70 ? 60.659 30.944 31.835 1.00 15.80 ? 70 VAL A CB 1 ATOM 527 C CG1 . VAL A 1 70 ? 60.088 31.909 30.862 1.00 22.34 ? 70 VAL A CG1 1 ATOM 528 C CG2 . VAL A 1 70 ? 59.598 30.268 32.659 1.00 13.71 ? 70 VAL A CG2 1 ATOM 529 N N . GLN A 1 71 ? 61.870 27.780 32.242 1.00 10.58 ? 71 GLN A N 1 ATOM 530 C CA . GLN A 1 71 ? 62.403 26.862 33.267 1.00 12.48 ? 71 GLN A CA 1 ATOM 531 C C . GLN A 1 71 ? 62.184 25.465 32.740 1.00 12.32 ? 71 GLN A C 1 ATOM 532 O O . GLN A 1 71 ? 61.174 25.224 32.022 1.00 11.37 ? 71 GLN A O 1 ATOM 533 C CB . GLN A 1 71 ? 61.650 27.072 34.603 1.00 15.81 ? 71 GLN A CB 1 ATOM 534 C CG . GLN A 1 71 ? 62.300 26.467 35.811 1.00 22.12 ? 71 GLN A CG 1 ATOM 535 C CD . GLN A 1 71 ? 62.003 27.253 37.112 1.00 33.21 ? 71 GLN A CD 1 ATOM 536 O OE1 . GLN A 1 71 ? 61.555 28.431 37.080 1.00 45.56 ? 71 GLN A OE1 1 ATOM 537 N NE2 . GLN A 1 71 ? 62.233 26.609 38.246 1.00 52.63 ? 71 GLN A NE2 1 ATOM 538 N N . SER A 1 72 ? 63.099 24.562 33.096 1.00 12.58 ? 72 SER A N 1 ATOM 539 C CA . SER A 1 72 ? 63.003 23.176 32.744 1.00 11.50 ? 72 SER A CA 1 ATOM 540 C C . SER A 1 72 ? 62.836 22.369 34.010 1.00 10.12 ? 72 SER A C 1 ATOM 541 O O . SER A 1 72 ? 63.544 22.611 35.006 1.00 14.67 ? 72 SER A O 1 ATOM 542 C CB . SER A 1 72 ? 64.258 22.728 31.982 1.00 17.89 ? 72 SER A CB 1 ATOM 543 O OG . SER A 1 72 ? 64.233 21.325 31.764 1.00 19.26 ? 72 SER A OG 1 ATOM 544 N N . TYR A 1 73 ? 61.942 21.373 33.954 1.00 9.73 ? 73 TYR A N 1 ATOM 545 C CA . TYR A 1 73 ? 61.674 20.499 35.045 1.00 10.22 ? 73 TYR A CA 1 ATOM 546 C C . TYR A 1 73 ? 61.701 19.058 34.584 1.00 11.01 ? 73 TYR A C 1 ATOM 547 O O . TYR A 1 73 ? 61.811 18.789 33.390 1.00 13.83 ? 73 TYR A O 1 ATOM 548 C CB . TYR A 1 73 ? 60.232 20.766 35.546 1.00 10.86 ? 73 TYR A CB 1 ATOM 549 C CG . TYR A 1 73 ? 59.984 22.192 35.992 1.00 8.98 ? 73 TYR A CG 1 ATOM 550 C CD1 . TYR A 1 73 ? 60.429 22.652 37.225 1.00 9.95 ? 73 TYR A CD1 1 ATOM 551 C CD2 . TYR A 1 73 ? 59.252 23.068 35.209 1.00 12.77 ? 73 TYR A CD2 1 ATOM 552 C CE1 . TYR A 1 73 ? 60.138 23.955 37.671 1.00 11.44 ? 73 TYR A CE1 1 ATOM 553 C CE2 . TYR A 1 73 ? 59.000 24.364 35.601 1.00 13.98 ? 73 TYR A CE2 1 ATOM 554 C CZ . TYR A 1 73 ? 59.386 24.797 36.858 1.00 11.95 ? 73 TYR A CZ 1 ATOM 555 O OH . TYR A 1 73 ? 59.105 26.047 37.304 1.00 13.81 ? 73 TYR A OH 1 ATOM 556 N N . SER A 1 74 ? 61.616 18.129 35.545 1.00 9.98 ? 74 SER A N 1 ATOM 557 C CA . SER A 1 74 ? 61.661 16.716 35.223 1.00 10.30 ? 74 SER A CA 1 ATOM 558 C C . SER A 1 74 ? 60.226 16.154 35.224 1.00 8.99 ? 74 SER A C 1 ATOM 559 O O . SER A 1 74 ? 59.351 16.651 35.918 1.00 9.03 ? 74 SER A O 1 ATOM 560 C CB . SER A 1 74 ? 62.437 16.055 36.304 1.00 14.94 ? 74 SER A CB 1 ATOM 561 O OG . SER A 1 74 ? 63.809 16.474 36.297 1.00 21.64 ? 74 SER A OG 1 ATOM 562 N N . PRO A 1 75 ? 59.988 15.063 34.486 1.00 9.80 ? 75 PRO A N 1 ATOM 563 C CA . PRO A 1 75 ? 58.718 14.353 34.536 1.00 9.58 ? 75 PRO A CA 1 ATOM 564 C C . PRO A 1 75 ? 58.320 14.016 35.965 1.00 9.81 ? 75 PRO A C 1 ATOM 565 O O . PRO A 1 75 ? 59.165 13.435 36.724 1.00 12.59 ? 75 PRO A O 1 ATOM 566 C CB . PRO A 1 75 ? 59.011 13.079 33.744 1.00 11.09 ? 75 PRO A CB 1 ATOM 567 C CG . PRO A 1 75 ? 59.993 13.552 32.669 1.00 13.26 ? 75 PRO A CG 1 ATOM 568 C CD . PRO A 1 75 ? 60.888 14.467 33.484 1.00 13.30 ? 75 PRO A CD 1 ATOM 569 N N . GLY A 1 76 ? 57.058 14.291 36.314 1.00 9.52 ? 76 GLY A N 1 ATOM 570 C CA . GLY A 1 76 ? 56.593 13.920 37.621 1.00 10.64 ? 76 GLY A CA 1 ATOM 571 C C . GLY A 1 76 ? 57.190 14.751 38.763 1.00 9.31 ? 76 GLY A C 1 ATOM 572 O O . GLY A 1 76 ? 56.844 14.492 39.921 1.00 11.96 ? 76 GLY A O 1 ATOM 573 N N . GLU A 1 77 ? 57.970 15.800 38.460 1.00 9.42 ? 77 GLU A N 1 ATOM 574 C CA . GLU A 1 77 ? 58.544 16.680 39.517 1.00 9.72 ? 77 GLU A CA 1 ATOM 575 C C . GLU A 1 77 ? 57.472 17.426 40.281 1.00 8.92 ? 77 GLU A C 1 ATOM 576 O O . GLU A 1 77 ? 56.491 17.868 39.694 1.00 10.64 ? 77 GLU A O 1 ATOM 577 C CB . GLU A 1 77 ? 59.531 17.686 38.917 1.00 9.55 ? 77 GLU A CB 1 ATOM 578 C CG . GLU A 1 77 ? 60.425 18.318 39.934 1.00 12.49 ? 77 GLU A CG 1 ATOM 579 C CD . GLU A 1 77 ? 61.522 19.248 39.364 1.00 13.99 ? 77 GLU A CD 1 ATOM 580 O OE1 . GLU A 1 77 ? 61.823 19.166 38.174 1.00 15.37 ? 77 GLU A OE1 1 ATOM 581 O OE2 . GLU A 1 77 ? 62.086 20.060 40.174 1.00 16.59 ? 77 GLU A OE2 1 ATOM 582 N N . GLU A 1 78 ? 57.647 17.490 41.610 1.00 9.48 ? 78 GLU A N 1 ATOM 583 C CA . GLU A 1 78 ? 56.800 18.370 42.438 1.00 10.90 ? 78 GLU A CA 1 ATOM 584 C C . GLU A 1 78 ? 57.435 19.709 42.485 1.00 11.79 ? 78 GLU A C 1 ATOM 585 O O . GLU A 1 78 ? 58.598 19.832 42.938 1.00 13.61 ? 78 GLU A O 1 ATOM 586 C CB . GLU A 1 78 ? 56.618 17.811 43.857 1.00 13.19 ? 78 GLU A CB 1 ATOM 587 C CG . GLU A 1 78 ? 55.841 16.515 43.835 1.00 16.27 ? 78 GLU A CG 1 ATOM 588 C CD . GLU A 1 78 ? 55.674 15.909 45.218 1.00 19.01 ? 78 GLU A CD 1 ATOM 589 O OE1 . GLU A 1 78 ? 56.298 16.420 46.187 1.00 26.83 ? 78 GLU A OE1 1 ATOM 590 O OE2 . GLU A 1 78 ? 54.921 14.945 45.328 1.00 31.03 ? 78 GLU A OE2 1 ATOM 591 N N . ILE A 1 79 ? 56.787 20.679 41.849 1.00 10.54 ? 79 ILE A N 1 ATOM 592 C CA . ILE A 1 79 ? 57.410 21.987 41.639 1.00 10.18 ? 79 ILE A CA 1 ATOM 593 C C . ILE A 1 79 ? 56.662 23.061 42.422 1.00 10.07 ? 79 ILE A C 1 ATOM 594 O O . ILE A 1 79 ? 55.428 22.971 42.658 1.00 9.99 ? 79 ILE A O 1 ATOM 595 C CB . ILE A 1 79 ? 57.488 22.358 40.145 1.00 9.67 ? 79 ILE A CB 1 ATOM 596 C CG1 . ILE A 1 79 ? 56.077 22.620 39.579 1.00 10.07 ? 79 ILE A CG1 1 ATOM 597 C CG2 . ILE A 1 79 ? 58.246 21.261 39.364 1.00 13.19 ? 79 ILE A CG2 1 ATOM 598 C CD1 . ILE A 1 79 ? 56.061 23.322 38.267 1.00 13.85 ? 79 ILE A CD1 1 ATOM 599 N N . GLU A 1 80 ? 57.396 24.094 42.773 1.00 10.08 ? 80 GLU A N 1 ATOM 600 C CA . GLU A 1 80 ? 56.820 25.293 43.334 1.00 9.56 ? 80 GLU A CA 1 ATOM 601 C C . GLU A 1 80 ? 56.120 26.111 42.229 1.00 8.64 ? 80 GLU A C 1 ATOM 602 O O . GLU A 1 80 ? 56.712 26.354 41.175 1.00 10.85 ? 80 GLU A O 1 ATOM 603 C CB . GLU A 1 80 ? 57.856 26.170 44.050 1.00 14.05 ? 80 GLU A CB 1 ATOM 604 C CG . GLU A 1 80 ? 57.247 27.451 44.592 1.00 20.22 ? 80 GLU A CG 1 ATOM 605 C CD . GLU A 1 80 ? 58.303 28.405 45.103 1.00 36.97 ? 80 GLU A CD 1 ATOM 606 O OE1 . GLU A 1 80 ? 58.037 29.627 45.162 1.00 28.75 ? 80 GLU A OE1 1 ATOM 607 O OE2 . GLU A 1 80 ? 59.368 27.916 45.414 1.00 62.54 ? 80 GLU A OE2 1 ATOM 608 N N . VAL A 1 81 ? 54.864 26.523 42.496 1.00 9.38 ? 81 VAL A N 1 ATOM 609 C CA . VAL A 1 81 ? 54.127 27.451 41.638 1.00 9.36 ? 81 VAL A CA 1 ATOM 610 C C . VAL A 1 81 ? 53.616 28.571 42.528 1.00 7.17 ? 81 VAL A C 1 ATOM 611 O O . VAL A 1 81 ? 53.100 28.320 43.619 1.00 10.12 ? 81 VAL A O 1 ATOM 612 C CB . VAL A 1 81 ? 52.994 26.750 40.877 1.00 8.75 ? 81 VAL A CB 1 ATOM 613 C CG1 . VAL A 1 81 ? 53.584 25.961 39.705 1.00 9.69 ? 81 VAL A CG1 1 ATOM 614 C CG2 . VAL A 1 81 ? 52.155 25.888 41.807 1.00 10.15 ? 81 VAL A CG2 1 ATOM 615 N N . GLN A 1 82 ? 53.817 29.802 42.078 1.00 7.74 ? 82 GLN A N 1 ATOM 616 C CA . GLN A 1 82 ? 53.460 30.997 42.843 1.00 8.04 ? 82 GLN A CA 1 ATOM 617 C C . GLN A 1 82 ? 52.741 32.008 42.007 1.00 6.00 ? 82 GLN A C 1 ATOM 618 O O . GLN A 1 82 ? 53.062 32.186 40.870 1.00 7.94 ? 82 GLN A O 1 ATOM 619 C CB . GLN A 1 82 ? 54.731 31.644 43.368 1.00 10.35 ? 82 GLN A CB 1 ATOM 620 C CG . GLN A 1 82 ? 54.517 32.755 44.374 1.00 10.90 ? 82 GLN A CG 1 ATOM 621 C CD . GLN A 1 82 ? 55.876 33.294 44.821 1.00 9.89 ? 82 GLN A CD 1 ATOM 622 O OE1 . GLN A 1 82 ? 56.479 34.134 44.160 1.00 12.09 ? 82 GLN A OE1 1 ATOM 623 N NE2 . GLN A 1 82 ? 56.342 32.801 45.968 1.00 12.14 ? 82 GLN A NE2 1 ATOM 624 N N . TRP A 1 83 ? 51.661 32.592 42.569 1.00 7.63 ? 83 TRP A N 1 ATOM 625 C CA . TRP A 1 83 ? 51.060 33.736 41.955 1.00 7.28 ? 83 TRP A CA 1 ATOM 626 C C . TRP A 1 83 ? 51.117 34.924 42.904 1.00 7.00 ? 83 TRP A C 1 ATOM 627 O O . TRP A 1 83 ? 51.464 34.762 44.078 1.00 7.81 ? 83 TRP A O 1 ATOM 628 C CB . TRP A 1 83 ? 49.661 33.430 41.417 1.00 8.16 ? 83 TRP A CB 1 ATOM 629 C CG . TRP A 1 83 ? 48.619 33.112 42.392 1.00 8.08 ? 83 TRP A CG 1 ATOM 630 C CD1 . TRP A 1 83 ? 48.362 31.916 42.927 1.00 8.59 ? 83 TRP A CD1 1 ATOM 631 C CD2 . TRP A 1 83 ? 47.542 33.999 42.829 1.00 7.25 ? 83 TRP A CD2 1 ATOM 632 N NE1 . TRP A 1 83 ? 47.204 31.986 43.726 1.00 7.67 ? 83 TRP A NE1 1 ATOM 633 C CE2 . TRP A 1 83 ? 46.718 33.252 43.687 1.00 6.72 ? 83 TRP A CE2 1 ATOM 634 C CE3 . TRP A 1 83 ? 47.243 35.343 42.602 1.00 7.53 ? 83 TRP A CE3 1 ATOM 635 C CZ2 . TRP A 1 83 ? 45.554 33.814 44.289 1.00 9.10 ? 83 TRP A CZ2 1 ATOM 636 C CZ3 . TRP A 1 83 ? 46.121 35.899 43.175 1.00 7.75 ? 83 TRP A CZ3 1 ATOM 637 C CH2 . TRP A 1 83 ? 45.272 35.119 44.003 1.00 8.72 ? 83 TRP A CH2 1 ATOM 638 N N . CYS A 1 84 ? 50.850 36.100 42.349 1.00 7.69 ? 84 CYS A N 1 ATOM 639 C CA . CYS A 1 84 ? 50.981 37.359 43.036 1.00 8.73 ? 84 CYS A CA 1 ATOM 640 C C . CYS A 1 84 ? 49.605 38.040 43.065 1.00 7.40 ? 84 CYS A C 1 ATOM 641 O O . CYS A 1 84 ? 49.035 38.239 42.020 1.00 8.81 ? 84 CYS A O 1 ATOM 642 C CB . CYS A 1 84 ? 51.949 38.262 42.307 1.00 9.92 ? 84 CYS A CB 1 ATOM 643 S SG . CYS A 1 84 ? 52.510 39.659 43.269 1.00 11.64 ? 84 CYS A SG 1 ATOM 644 N N . VAL A 1 85 ? 49.144 38.422 44.248 1.00 6.94 ? 85 VAL A N 1 ATOM 645 C CA . VAL A 1 85 ? 47.863 39.155 44.428 1.00 6.45 ? 85 VAL A CA 1 ATOM 646 C C . VAL A 1 85 ? 48.159 40.594 44.871 1.00 7.43 ? 85 VAL A C 1 ATOM 647 O O . VAL A 1 85 ? 48.967 40.812 45.812 1.00 9.69 ? 85 VAL A O 1 ATOM 648 C CB . VAL A 1 85 ? 46.911 38.405 45.431 1.00 6.77 ? 85 VAL A CB 1 ATOM 649 C CG1 . VAL A 1 85 ? 47.434 38.310 46.845 1.00 7.99 ? 85 VAL A CG1 1 ATOM 650 C CG2 . VAL A 1 85 ? 45.478 38.950 45.382 1.00 9.63 ? 85 VAL A CG2 1 ATOM 651 N N . ASP A 1 86 ? 47.499 41.552 44.246 1.00 8.37 ? 86 ASP A N 1 ATOM 652 C CA . ASP A 1 86 ? 47.659 42.921 44.668 1.00 9.23 ? 86 ASP A CA 1 ATOM 653 C C . ASP A 1 86 ? 46.925 43.178 45.984 1.00 7.91 ? 86 ASP A C 1 ATOM 654 O O . ASP A 1 86 ? 45.840 42.717 46.227 1.00 9.65 ? 86 ASP A O 1 ATOM 655 C CB . ASP A 1 86 ? 47.091 43.834 43.576 1.00 8.38 ? 86 ASP A CB 1 ATOM 656 C CG . ASP A 1 86 ? 47.265 45.298 43.902 1.00 9.26 ? 86 ASP A CG 1 ATOM 657 O OD1 . ASP A 1 86 ? 48.402 45.801 43.703 1.00 12.25 ? 86 ASP A OD1 1 ATOM 658 O OD2 . ASP A 1 86 ? 46.245 45.914 44.345 1.00 10.62 ? 86 ASP A OD2 1 ATOM 659 N N . HIS A 1 87 ? 47.519 44.017 46.794 1.00 10.05 ? 87 HIS A N 1 ATOM 660 C CA . HIS A 1 87 ? 47.046 44.408 48.126 1.00 10.62 ? 87 HIS A CA 1 ATOM 661 C C . HIS A 1 87 ? 45.615 44.915 48.056 1.00 9.62 ? 87 HIS A C 1 ATOM 662 O O . HIS A 1 87 ? 44.829 44.674 48.972 1.00 11.06 ? 87 HIS A O 1 ATOM 663 C CB . HIS A 1 87 ? 47.977 45.502 48.682 1.00 10.79 ? 87 HIS A CB 1 ATOM 664 C CG . HIS A 1 87 ? 47.464 46.145 49.931 1.00 11.51 ? 87 HIS A CG 1 ATOM 665 N ND1 . HIS A 1 87 ? 46.423 47.054 49.923 1.00 11.89 ? 87 HIS A ND1 1 ATOM 666 C CD2 . HIS A 1 87 ? 47.818 45.979 51.226 1.00 15.37 ? 87 HIS A CD2 1 ATOM 667 C CE1 . HIS A 1 87 ? 46.194 47.455 51.166 1.00 16.72 ? 87 HIS A CE1 1 ATOM 668 N NE2 . HIS A 1 87 ? 47.042 46.837 51.966 1.00 15.11 ? 87 HIS A NE2 1 ATOM 669 N N . ASN A 1 88 ? 45.257 45.628 46.978 1.00 9.34 ? 88 ASN A N 1 ATOM 670 C CA . ASN A 1 88 ? 43.938 46.221 46.854 1.00 9.56 ? 88 ASN A CA 1 ATOM 671 C C . ASN A 1 88 ? 42.958 45.353 46.069 1.00 11.44 ? 88 ASN A C 1 ATOM 672 O O . ASN A 1 88 ? 41.802 45.740 45.847 1.00 13.74 ? 88 ASN A O 1 ATOM 673 C CB . ASN A 1 88 ? 44.022 47.590 46.178 1.00 11.14 ? 88 ASN A CB 1 ATOM 674 C CG . ASN A 1 88 ? 44.501 48.695 47.066 1.00 11.58 ? 88 ASN A CG 1 ATOM 675 O OD1 . ASN A 1 88 ? 44.979 48.507 48.200 1.00 13.07 ? 88 ASN A OD1 1 ATOM 676 N ND2 . ASN A 1 88 ? 44.463 49.897 46.512 1.00 15.81 ? 88 ASN A ND2 1 ATOM 677 N N . GLY A 1 89 ? 43.417 44.181 45.650 1.00 10.42 ? 89 GLY A N 1 ATOM 678 C CA . GLY A 1 89 ? 42.546 43.306 44.797 1.00 9.70 ? 89 GLY A CA 1 ATOM 679 C C . GLY A 1 89 ? 42.521 41.824 45.219 1.00 9.00 ? 89 GLY A C 1 ATOM 680 O O . GLY A 1 89 ? 42.550 40.934 44.394 1.00 9.25 ? 89 GLY A O 1 ATOM 681 N N . ASP A 1 90 ? 42.520 41.607 46.533 1.00 8.35 ? 90 ASP A N 1 ATOM 682 C CA . ASP A 1 90 ? 42.507 40.292 47.059 1.00 9.38 ? 90 ASP A CA 1 ATOM 683 C C . ASP A 1 90 ? 41.029 39.858 47.178 1.00 8.31 ? 90 ASP A C 1 ATOM 684 O O . ASP A 1 90 ? 40.385 40.095 48.163 1.00 10.18 ? 90 ASP A O 1 ATOM 685 C CB . ASP A 1 90 ? 43.238 40.232 48.363 1.00 12.27 ? 90 ASP A CB 1 ATOM 686 C CG . ASP A 1 90 ? 43.358 38.815 48.933 1.00 10.17 ? 90 ASP A CG 1 ATOM 687 O OD1 . ASP A 1 90 ? 42.750 37.869 48.338 1.00 9.37 ? 90 ASP A OD1 1 ATOM 688 O OD2 . ASP A 1 90 ? 44.137 38.660 49.927 1.00 11.44 ? 90 ASP A OD2 1 ATOM 689 N N . HIS A 1 91 ? 40.527 39.204 46.133 1.00 9.44 ? 91 HIS A N 1 ATOM 690 C CA . HIS A 1 91 ? 39.099 38.824 46.029 1.00 8.64 ? 91 HIS A CA 1 ATOM 691 C C . HIS A 1 91 ? 38.737 37.469 46.608 1.00 9.83 ? 91 HIS A C 1 ATOM 692 O O . HIS A 1 91 ? 37.573 37.053 46.498 1.00 9.26 ? 91 HIS A O 1 ATOM 693 C CB . HIS A 1 91 ? 38.725 38.812 44.546 1.00 11.44 ? 91 HIS A CB 1 ATOM 694 C CG . HIS A 1 91 ? 39.090 40.068 43.848 1.00 7.50 ? 91 HIS A CG 1 ATOM 695 N ND1 . HIS A 1 91 ? 38.685 41.302 44.307 1.00 10.66 ? 91 HIS A ND1 1 ATOM 696 C CD2 . HIS A 1 91 ? 39.858 40.307 42.738 1.00 9.66 ? 91 HIS A CD2 1 ATOM 697 C CE1 . HIS A 1 91 ? 39.226 42.253 43.547 1.00 11.22 ? 91 HIS A CE1 1 ATOM 698 N NE2 . HIS A 1 91 ? 39.917 41.680 42.582 1.00 9.29 ? 91 HIS A NE2 1 ATOM 699 N N . GLY A 1 92 ? 39.684 36.766 47.219 1.00 9.12 ? 92 GLY A N 1 ATOM 700 C CA . GLY A 1 92 ? 39.425 35.430 47.672 1.00 8.62 ? 92 GLY A CA 1 ATOM 701 C C . GLY A 1 92 ? 39.127 34.540 46.475 1.00 7.61 ? 92 GLY A C 1 ATOM 702 O O . GLY A 1 92 ? 39.395 34.887 45.274 1.00 9.02 ? 92 GLY A O 1 ATOM 703 N N . GLY A 1 93 ? 38.572 33.364 46.773 1.00 8.16 ? 93 GLY A N 1 ATOM 704 C CA . GLY A 1 93 ? 38.274 32.402 45.758 1.00 8.60 ? 93 GLY A CA 1 ATOM 705 C C . GLY A 1 93 ? 39.193 31.213 45.673 1.00 7.77 ? 93 GLY A C 1 ATOM 706 O O . GLY A 1 93 ? 39.679 30.762 46.657 1.00 8.72 ? 93 GLY A O 1 ATOM 707 N N . MET A 1 94 ? 39.300 30.652 44.459 1.00 8.48 ? 94 MET A N 1 ATOM 708 C CA . MET A 1 94 ? 40.000 29.392 44.207 1.00 6.34 ? 94 MET A CA 1 ATOM 709 C C . MET A 1 94 ? 40.789 29.475 42.949 1.00 6.15 ? 94 MET A C 1 ATOM 710 O O . MET A 1 94 ? 40.480 30.248 42.062 1.00 8.39 ? 94 MET A O 1 ATOM 711 C CB . MET A 1 94 ? 38.975 28.251 44.129 1.00 6.93 ? 94 MET A CB 1 ATOM 712 C CG . MET A 1 94 ? 38.295 27.908 45.461 1.00 9.73 ? 94 MET A CG 1 ATOM 713 S SD . MET A 1 94 ? 36.933 26.729 45.349 1.00 9.45 ? 94 MET A SD 1 ATOM 714 C CE . MET A 1 94 ? 37.926 25.309 44.927 1.00 9.21 ? 94 MET A CE 1 ATOM 715 N N . PHE A 1 95 ? 41.898 28.727 42.926 1.00 7.26 ? 95 PHE A N 1 ATOM 716 C CA . PHE A 1 95 ? 42.807 28.807 41.794 1.00 6.56 ? 95 PHE A CA 1 ATOM 717 C C . PHE A 1 95 ? 43.376 27.438 41.496 1.00 7.44 ? 95 PHE A C 1 ATOM 718 O O . PHE A 1 95 ? 43.354 26.516 42.322 1.00 8.89 ? 95 PHE A O 1 ATOM 719 C CB . PHE A 1 95 ? 43.906 29.831 42.029 1.00 6.25 ? 95 PHE A CB 1 ATOM 720 C CG . PHE A 1 95 ? 44.770 29.554 43.234 1.00 7.20 ? 95 PHE A CG 1 ATOM 721 C CD1 . PHE A 1 95 ? 44.389 29.954 44.495 1.00 8.49 ? 95 PHE A CD1 1 ATOM 722 C CD2 . PHE A 1 95 ? 45.957 28.844 43.097 1.00 7.67 ? 95 PHE A CD2 1 ATOM 723 C CE1 . PHE A 1 95 ? 45.147 29.672 45.588 1.00 7.36 ? 95 PHE A CE1 1 ATOM 724 C CE2 . PHE A 1 95 ? 46.779 28.629 44.188 1.00 8.13 ? 95 PHE A CE2 1 ATOM 725 C CZ . PHE A 1 95 ? 46.375 29.024 45.453 1.00 9.16 ? 95 PHE A CZ 1 ATOM 726 N N . THR A 1 96 ? 43.936 27.325 40.297 1.00 7.58 ? 96 THR A N 1 ATOM 727 C CA . THR A 1 96 ? 44.486 26.074 39.808 1.00 8.36 ? 96 THR A CA 1 ATOM 728 C C . THR A 1 96 ? 45.498 26.316 38.743 1.00 5.94 ? 96 THR A C 1 ATOM 729 O O . THR A 1 96 ? 45.631 27.389 38.201 1.00 7.56 ? 96 THR A O 1 ATOM 730 C CB . THR A 1 96 ? 43.346 25.142 39.257 1.00 9.74 ? 96 THR A CB 1 ATOM 731 O OG1 . THR A 1 96 ? 43.828 23.855 38.898 1.00 12.57 ? 96 THR A OG1 1 ATOM 732 C CG2 . THR A 1 96 ? 42.569 25.807 38.114 1.00 10.79 ? 96 THR A CG2 1 ATOM 733 N N . TYR A 1 97 ? 46.273 25.267 38.511 1.00 5.91 ? 97 TYR A N 1 ATOM 734 C CA . TYR A 1 97 ? 47.304 25.226 37.469 1.00 6.77 ? 97 TYR A CA 1 ATOM 735 C C . TYR A 1 97 ? 47.077 23.985 36.626 1.00 7.24 ? 97 TYR A C 1 ATOM 736 O O . TYR A 1 97 ? 46.662 22.947 37.144 1.00 7.95 ? 97 TYR A O 1 ATOM 737 C CB . TYR A 1 97 ? 48.680 25.176 38.086 1.00 7.50 ? 97 TYR A CB 1 ATOM 738 C CG . TYR A 1 97 ? 49.099 26.373 38.904 1.00 7.27 ? 97 TYR A CG 1 ATOM 739 C CD1 . TYR A 1 97 ? 48.850 26.466 40.256 1.00 7.90 ? 97 TYR A CD1 1 ATOM 740 C CD2 . TYR A 1 97 ? 49.732 27.437 38.306 1.00 7.97 ? 97 TYR A CD2 1 ATOM 741 C CE1 . TYR A 1 97 ? 49.194 27.564 40.987 1.00 8.18 ? 97 TYR A CE1 1 ATOM 742 C CE2 . TYR A 1 97 ? 50.111 28.548 39.038 1.00 8.50 ? 97 TYR A CE2 1 ATOM 743 C CZ . TYR A 1 97 ? 49.852 28.619 40.388 1.00 7.83 ? 97 TYR A CZ 1 ATOM 744 O OH . TYR A 1 97 ? 50.277 29.732 41.089 1.00 9.15 ? 97 TYR A OH 1 ATOM 745 N N . ARG A 1 98 ? 47.256 24.136 35.314 1.00 6.57 ? 98 ARG A N 1 ATOM 746 C CA . ARG A 1 98 ? 46.922 23.132 34.303 1.00 6.98 ? 98 ARG A CA 1 ATOM 747 C C . ARG A 1 98 ? 47.983 23.033 33.226 1.00 6.67 ? 98 ARG A C 1 ATOM 748 O O . ARG A 1 98 ? 48.617 24.001 32.882 1.00 7.47 ? 98 ARG A O 1 ATOM 749 C CB . ARG A 1 98 ? 45.575 23.424 33.616 1.00 8.29 ? 98 ARG A CB 1 ATOM 750 C CG . ARG A 1 98 ? 44.379 23.754 34.559 1.00 7.68 ? 98 ARG A CG 1 ATOM 751 C CD . ARG A 1 98 ? 44.167 25.198 34.962 1.00 8.86 ? 98 ARG A CD 1 ATOM 752 N NE . ARG A 1 98 ? 44.257 26.169 33.866 1.00 8.99 ? 98 ARG A NE 1 ATOM 753 C CZ . ARG A 1 98 ? 43.216 26.515 33.116 1.00 9.63 ? 98 ARG A CZ 1 ATOM 754 N NH1 . ARG A 1 98 ? 42.015 25.896 33.272 1.00 10.54 ? 98 ARG A NH1 1 ATOM 755 N NH2 . ARG A 1 98 ? 43.358 27.474 32.210 1.00 10.18 ? 98 ARG A NH2 1 ATOM 756 N N . ILE A 1 99 ? 48.182 21.816 32.723 1.00 6.03 ? 99 ILE A N 1 ATOM 757 C CA . ILE A 1 99 ? 48.997 21.570 31.528 1.00 7.48 ? 99 ILE A CA 1 ATOM 758 C C . ILE A 1 99 ? 48.188 20.795 30.510 1.00 7.78 ? 99 ILE A C 1 ATOM 759 O O . ILE A 1 99 ? 47.689 19.681 30.782 1.00 10.59 ? 99 ILE A O 1 ATOM 760 C CB . ILE A 1 99 ? 50.266 20.800 31.851 1.00 9.73 ? 99 ILE A CB 1 ATOM 761 C CG1 . ILE A 1 99 ? 51.124 21.641 32.796 1.00 7.98 ? 99 ILE A CG1 1 ATOM 762 C CG2 . ILE A 1 99 ? 51.044 20.490 30.575 1.00 9.81 ? 99 ILE A CG2 1 ATOM 763 C CD1 . ILE A 1 99 ? 52.400 21.026 33.387 1.00 9.77 ? 99 ILE A CD1 1 ATOM 764 N N . CYS A 1 100 ? 47.989 21.411 29.353 1.00 8.25 ? 100 CYS A N 1 ATOM 765 C CA . CYS A 1 100 ? 47.309 20.754 28.232 1.00 7.66 ? 100 CYS A CA 1 ATOM 766 C C . CYS A 1 100 ? 48.284 19.729 27.598 1.00 8.54 ? 100 CYS A C 1 ATOM 767 O O . CYS A 1 100 ? 49.429 20.046 27.234 1.00 9.62 ? 100 CYS A O 1 ATOM 768 C CB . CYS A 1 100 ? 46.903 21.785 27.179 1.00 8.93 ? 100 CYS A CB 1 ATOM 769 S SG . CYS A 1 100 ? 46.408 21.160 25.559 1.00 12.06 ? 100 CYS A SG 1 ATOM 770 N N . GLN A 1 101 ? 47.801 18.476 27.530 1.00 11.51 ? 101 GLN A N 1 ATOM 771 C CA . GLN A 1 101 ? 48.673 17.314 27.107 1.00 11.80 ? 101 GLN A CA 1 ATOM 772 C C . GLN A 1 101 ? 48.649 17.086 25.610 1.00 15.03 ? 101 GLN A C 1 ATOM 773 O O . GLN A 1 101 ? 49.285 16.157 25.144 1.00 17.21 ? 101 GLN A O 1 ATOM 774 C CB . GLN A 1 101 ? 48.237 16.073 27.913 1.00 14.58 ? 101 GLN A CB 1 ATOM 775 C CG . GLN A 1 101 ? 48.322 16.345 29.422 1.00 14.82 ? 101 GLN A CG 1 ATOM 776 C CD . GLN A 1 101 ? 48.268 15.075 30.283 1.00 16.86 ? 101 GLN A CD 1 ATOM 777 O OE1 . GLN A 1 101 ? 48.139 13.961 29.752 1.00 23.75 ? 101 GLN A OE1 1 ATOM 778 N NE2 . GLN A 1 101 ? 48.386 15.228 31.598 1.00 18.14 ? 101 GLN A NE2 1 ATOM 779 N N . ASP A 1 102 ? 47.995 17.974 24.861 1.00 12.60 ? 102 ASP A N 1 ATOM 780 C CA . ASP A 1 102 ? 47.876 17.812 23.394 1.00 10.45 ? 102 ASP A CA 1 ATOM 781 C C . ASP A 1 102 ? 48.812 18.863 22.778 1.00 10.47 ? 102 ASP A C 1 ATOM 782 O O . ASP A 1 102 ? 48.486 20.038 22.686 1.00 13.09 ? 102 ASP A O 1 ATOM 783 C CB . ASP A 1 102 ? 46.443 17.991 22.924 1.00 13.68 ? 102 ASP A CB 1 ATOM 784 C CG . ASP A 1 102 ? 46.278 17.801 21.416 1.00 14.47 ? 102 ASP A CG 1 ATOM 785 O OD1 . ASP A 1 102 ? 47.304 17.877 20.658 1.00 20.16 ? 102 ASP A OD1 1 ATOM 786 O OD2 . ASP A 1 102 ? 45.108 17.650 20.956 1.00 20.74 ? 102 ASP A OD2 1 ATOM 787 N N . GLN A 1 103 ? 50.008 18.416 22.396 1.00 13.42 ? 103 GLN A N 1 ATOM 788 C CA . GLN A 1 103 ? 51.057 19.342 21.909 1.00 14.59 ? 103 GLN A CA 1 ATOM 789 C C . GLN A 1 103 ? 50.552 20.117 20.657 1.00 11.63 ? 103 GLN A C 1 ATOM 790 O O . GLN A 1 103 ? 50.928 21.262 20.393 1.00 15.45 ? 103 GLN A O 1 ATOM 791 C CB . GLN A 1 103 ? 52.377 18.587 21.594 1.00 16.53 ? 103 GLN A CB 1 ATOM 792 C CG . GLN A 1 103 ? 53.529 19.529 21.285 1.00 16.93 ? 103 GLN A CG 1 ATOM 793 C CD . GLN A 1 103 ? 54.048 20.267 22.491 1.00 18.86 ? 103 GLN A CD 1 ATOM 794 O OE1 . GLN A 1 103 ? 54.417 19.650 23.512 1.00 18.27 ? 103 GLN A OE1 1 ATOM 795 N NE2 . GLN A 1 103 ? 54.154 21.586 22.371 1.00 16.90 ? 103 GLN A NE2 1 ATOM 796 N N . SER A 1 104 ? 49.705 19.475 19.855 1.00 15.67 ? 104 SER A N 1 ATOM 797 C CA . SER A 1 104 ? 49.124 20.159 18.663 1.00 15.31 ? 104 SER A CA 1 ATOM 798 C C . SER A 1 104 ? 48.262 21.385 18.999 1.00 16.52 ? 104 SER A C 1 ATOM 799 O O . SER A 1 104 ? 48.299 22.366 18.251 1.00 17.82 ? 104 SER A O 1 ATOM 800 C CB . SER A 1 104 ? 48.373 19.219 17.730 1.00 18.22 ? 104 SER A CB 1 ATOM 801 O OG . SER A 1 104 ? 47.089 18.946 18.215 1.00 25.35 ? 104 SER A OG 1 ATOM 802 N N . ILE A 1 105 ? 47.533 21.332 20.129 1.00 13.38 ? 105 ILE A N 1 ATOM 803 C CA . ILE A 1 105 ? 46.792 22.500 20.650 1.00 11.69 ? 105 ILE A CA 1 ATOM 804 C C . ILE A 1 105 ? 47.767 23.539 21.226 1.00 11.29 ? 105 ILE A C 1 ATOM 805 O O . ILE A 1 105 ? 47.700 24.724 20.844 1.00 13.65 ? 105 ILE A O 1 ATOM 806 C CB . ILE A 1 105 ? 45.776 22.059 21.701 1.00 13.00 ? 105 ILE A CB 1 ATOM 807 C CG1 . ILE A 1 105 ? 44.757 21.167 21.042 1.00 16.32 ? 105 ILE A CG1 1 ATOM 808 C CG2 . ILE A 1 105 ? 45.141 23.247 22.304 1.00 16.87 ? 105 ILE A CG2 1 ATOM 809 C CD1 . ILE A 1 105 ? 43.588 20.757 21.908 1.00 23.25 ? 105 ILE A CD1 1 ATOM 810 N N . VAL A 1 106 ? 48.748 23.062 22.030 1.00 10.19 ? 106 VAL A N 1 ATOM 811 C CA . VAL A 1 106 ? 49.678 23.944 22.694 1.00 10.05 ? 106 VAL A CA 1 ATOM 812 C C . VAL A 1 106 ? 50.455 24.726 21.620 1.00 9.13 ? 106 VAL A C 1 ATOM 813 O O . VAL A 1 106 ? 50.727 25.937 21.754 1.00 9.72 ? 106 VAL A O 1 ATOM 814 C CB . VAL A 1 106 ? 50.682 23.173 23.582 1.00 11.72 ? 106 VAL A CB 1 ATOM 815 C CG1 . VAL A 1 106 ? 51.756 24.080 24.146 1.00 12.64 ? 106 VAL A CG1 1 ATOM 816 C CG2 . VAL A 1 106 ? 49.969 22.442 24.736 1.00 12.47 ? 106 VAL A CG2 1 ATOM 817 N N . ASP A 1 107 ? 50.807 24.043 20.532 1.00 10.15 ? 107 ASP A N 1 ATOM 818 C CA . ASP A 1 107 ? 51.633 24.667 19.525 1.00 10.61 ? 107 ASP A CA 1 ATOM 819 C C . ASP A 1 107 ? 50.964 25.919 18.866 1.00 9.64 ? 107 ASP A C 1 ATOM 820 O O . ASP A 1 107 ? 51.673 26.817 18.346 1.00 13.10 ? 107 ASP A O 1 ATOM 821 C CB . ASP A 1 107 ? 51.911 23.674 18.414 1.00 15.87 ? 107 ASP A CB 1 ATOM 822 C CG . ASP A 1 107 ? 53.033 22.715 18.740 1.00 16.02 ? 107 ASP A CG 1 ATOM 823 O OD1 . ASP A 1 107 ? 53.752 22.904 19.753 1.00 17.34 ? 107 ASP A OD1 1 ATOM 824 O OD2 . ASP A 1 107 ? 53.176 21.762 17.907 1.00 19.43 ? 107 ASP A OD2 1 ATOM 825 N N . LYS A 1 108 ? 49.623 26.003 18.887 1.00 12.44 ? 108 LYS A N 1 ATOM 826 C CA . LYS A 1 108 ? 48.926 27.198 18.377 1.00 11.24 ? 108 LYS A CA 1 ATOM 827 C C . LYS A 1 108 ? 49.203 28.465 19.204 1.00 9.22 ? 108 LYS A C 1 ATOM 828 O O . LYS A 1 108 ? 48.892 29.568 18.740 1.00 11.90 ? 108 LYS A O 1 ATOM 829 C CB . LYS A 1 108 ? 47.411 26.960 18.353 1.00 12.29 ? 108 LYS A CB 1 ATOM 830 C CG . LYS A 1 108 ? 46.971 25.768 17.494 1.00 14.42 ? 108 LYS A CG 1 ATOM 831 C CD . LYS A 1 108 ? 45.490 25.565 17.420 1.00 22.72 ? 108 LYS A CD 1 ATOM 832 C CE . LYS A 1 108 ? 45.191 24.387 16.477 1.00 36.28 ? 108 LYS A CE 1 ATOM 833 N NZ . LYS A 1 108 ? 43.966 24.550 15.670 1.00 42.16 ? 108 LYS A NZ 1 ATOM 834 N N . PHE A 1 109 ? 49.802 28.283 20.405 1.00 8.80 ? 109 PHE A N 1 ATOM 835 C CA . PHE A 1 109 ? 50.131 29.375 21.337 1.00 8.84 ? 109 PHE A CA 1 ATOM 836 C C . PHE A 1 109 ? 51.634 29.666 21.398 1.00 8.26 ? 109 PHE A C 1 ATOM 837 O O . PHE A 1 109 ? 52.072 30.555 22.163 1.00 9.71 ? 109 PHE A O 1 ATOM 838 C CB . PHE A 1 109 ? 49.609 29.027 22.709 1.00 9.09 ? 109 PHE A CB 1 ATOM 839 C CG . PHE A 1 109 ? 48.114 28.871 22.744 1.00 8.30 ? 109 PHE A CG 1 ATOM 840 C CD1 . PHE A 1 109 ? 47.516 27.736 22.299 1.00 11.09 ? 109 PHE A CD1 1 ATOM 841 C CD2 . PHE A 1 109 ? 47.309 29.893 23.221 1.00 8.59 ? 109 PHE A CD2 1 ATOM 842 C CE1 . PHE A 1 109 ? 46.109 27.640 22.258 1.00 11.64 ? 109 PHE A CE1 1 ATOM 843 C CE2 . PHE A 1 109 ? 45.908 29.817 23.202 1.00 10.09 ? 109 PHE A CE2 1 ATOM 844 C CZ . PHE A 1 109 ? 45.312 28.679 22.694 1.00 11.75 ? 109 PHE A CZ 1 ATOM 845 N N . LEU A 1 110 ? 52.396 28.972 20.554 1.00 9.27 ? 110 LEU A N 1 ATOM 846 C CA . LEU A 1 110 ? 53.859 29.049 20.579 1.00 11.00 ? 110 LEU A CA 1 ATOM 847 C C . LEU A 1 110 ? 54.415 29.648 19.291 1.00 10.62 ? 110 LEU A C 1 ATOM 848 O O . LEU A 1 110 ? 55.661 29.547 19.078 1.00 12.51 ? 110 LEU A O 1 ATOM 849 C CB . LEU A 1 110 ? 54.452 27.672 20.770 1.00 11.58 ? 110 LEU A CB 1 ATOM 850 C CG . LEU A 1 110 ? 54.037 26.841 21.992 1.00 12.24 ? 110 LEU A CG 1 ATOM 851 C CD1 . LEU A 1 110 ? 54.852 25.544 22.099 1.00 14.88 ? 110 LEU A CD1 1 ATOM 852 C CD2 . LEU A 1 110 ? 54.113 27.615 23.302 1.00 13.91 ? 110 LEU A CD2 1 ATOM 853 N N . ASP A 1 111 ? 53.570 30.261 18.436 1.00 10.11 ? 111 ASP A N 1 ATOM 854 C CA . ASP A 1 111 ? 54.020 30.776 17.121 1.00 11.91 ? 111 ASP A CA 1 ATOM 855 C C . ASP A 1 111 ? 53.841 32.299 17.072 1.00 12.10 ? 111 ASP A C 1 ATOM 856 O O . ASP A 1 111 ? 52.695 32.785 17.085 1.00 12.50 ? 111 ASP A O 1 ATOM 857 C CB . ASP A 1 111 ? 53.220 30.106 15.990 1.00 15.11 ? 111 ASP A CB 1 ATOM 858 C CG . ASP A 1 111 ? 53.631 30.540 14.611 1.00 20.65 ? 111 ASP A CG 1 ATOM 859 O OD1 . ASP A 1 111 ? 54.399 31.512 14.444 1.00 19.43 ? 111 ASP A OD1 1 ATOM 860 O OD2 . ASP A 1 111 ? 53.123 29.881 13.693 1.00 25.01 ? 111 ASP A OD2 1 ATOM 861 N N . PRO A 1 112 ? 54.961 33.059 17.048 1.00 12.95 ? 112 PRO A N 1 ATOM 862 C CA . PRO A 1 112 ? 54.810 34.537 17.042 1.00 13.68 ? 112 PRO A CA 1 ATOM 863 C C . PRO A 1 112 ? 54.045 35.118 15.847 1.00 13.50 ? 112 PRO A C 1 ATOM 864 O O . PRO A 1 112 ? 53.562 36.241 15.917 1.00 16.86 ? 112 PRO A O 1 ATOM 865 C CB . PRO A 1 112 ? 56.251 35.040 17.121 1.00 16.84 ? 112 PRO A CB 1 ATOM 866 C CG . PRO A 1 112 ? 57.096 33.902 16.647 1.00 20.75 ? 112 PRO A CG 1 ATOM 867 C CD . PRO A 1 112 ? 56.369 32.633 17.012 1.00 15.13 ? 112 PRO A CD 1 ATOM 868 N N . SER A 1 113 ? 53.970 34.355 14.766 1.00 13.65 ? 113 SER A N 1 ATOM 869 C CA . SER A 1 113 ? 53.292 34.799 13.561 1.00 15.74 ? 113 SER A CA 1 ATOM 870 C C . SER A 1 113 ? 51.770 34.431 13.562 1.00 16.53 ? 113 SER A C 1 ATOM 871 O O . SER A 1 113 ? 51.105 34.748 12.594 1.00 22.56 ? 113 SER A O 1 ATOM 872 C CB . SER A 1 113 ? 53.980 34.257 12.303 1.00 23.89 ? 113 SER A CB 1 ATOM 873 O OG . SER A 1 113 ? 53.444 33.014 12.002 1.00 28.74 ? 113 SER A OG 1 ATOM 874 N N . TYR A 1 114 ? 51.247 33.798 14.655 1.00 12.44 ? 114 TYR A N 1 ATOM 875 C CA . TYR A 1 114 ? 49.873 33.301 14.708 1.00 13.42 ? 114 TYR A CA 1 ATOM 876 C C . TYR A 1 114 ? 49.182 33.718 15.989 1.00 12.91 ? 114 TYR A C 1 ATOM 877 O O . TYR A 1 114 ? 49.677 33.479 17.077 1.00 12.06 ? 114 TYR A O 1 ATOM 878 C CB . TYR A 1 114 ? 49.869 31.757 14.604 1.00 15.52 ? 114 TYR A CB 1 ATOM 879 C CG . TYR A 1 114 ? 48.475 31.234 14.496 1.00 14.39 ? 114 TYR A CG 1 ATOM 880 C CD1 . TYR A 1 114 ? 47.711 31.504 13.358 1.00 16.38 ? 114 TYR A CD1 1 ATOM 881 C CD2 . TYR A 1 114 ? 47.849 30.546 15.565 1.00 16.01 ? 114 TYR A CD2 1 ATOM 882 C CE1 . TYR A 1 114 ? 46.380 31.085 13.246 1.00 16.94 ? 114 TYR A CE1 1 ATOM 883 C CE2 . TYR A 1 114 ? 46.520 30.121 15.428 1.00 14.85 ? 114 TYR A CE2 1 ATOM 884 C CZ . TYR A 1 114 ? 45.804 30.409 14.274 1.00 14.73 ? 114 TYR A CZ 1 ATOM 885 O OH . TYR A 1 114 ? 44.506 30.031 14.169 1.00 18.22 ? 114 TYR A OH 1 ATOM 886 N N . LEU A 1 115 ? 47.967 34.222 15.834 1.00 13.16 ? 115 LEU A N 1 ATOM 887 C CA . LEU A 1 115 ? 47.144 34.572 16.949 1.00 12.62 ? 115 LEU A CA 1 ATOM 888 C C . LEU A 1 115 ? 45.955 33.584 17.006 1.00 9.46 ? 115 LEU A C 1 ATOM 889 O O . LEU A 1 115 ? 45.106 33.541 16.037 1.00 13.36 ? 115 LEU A O 1 ATOM 890 C CB . LEU A 1 115 ? 46.648 36.005 16.772 1.00 15.76 ? 115 LEU A CB 1 ATOM 891 C CG . LEU A 1 115 ? 45.692 36.415 17.890 1.00 18.17 ? 115 LEU A CG 1 ATOM 892 C CD1 . LEU A 1 115 ? 46.418 36.471 19.241 1.00 22.12 ? 115 LEU A CD1 1 ATOM 893 C CD2 . LEU A 1 115 ? 45.008 37.722 17.568 1.00 20.90 ? 115 LEU A CD2 1 ATOM 894 N N . PRO A 1 116 ? 45.880 32.749 18.081 1.00 10.04 ? 116 PRO A N 1 ATOM 895 C CA . PRO A 1 116 ? 44.755 31.829 18.153 1.00 11.60 ? 116 PRO A CA 1 ATOM 896 C C . PRO A 1 116 ? 43.387 32.529 18.197 1.00 9.07 ? 116 PRO A C 1 ATOM 897 O O . PRO A 1 116 ? 43.223 33.618 18.716 1.00 9.48 ? 116 PRO A O 1 ATOM 898 C CB . PRO A 1 116 ? 44.990 31.053 19.421 1.00 13.15 ? 116 PRO A CB 1 ATOM 899 C CG . PRO A 1 116 ? 46.401 31.349 19.860 1.00 17.89 ? 116 PRO A CG 1 ATOM 900 C CD . PRO A 1 116 ? 46.860 32.566 19.168 1.00 13.92 ? 116 PRO A CD 1 ATOM 901 N N . THR A 1 117 ? 42.420 31.892 17.536 1.00 10.03 ? 117 THR A N 1 ATOM 902 C CA . THR A 1 117 ? 41.062 32.387 17.510 1.00 9.86 ? 117 THR A CA 1 ATOM 903 C C . THR A 1 117 ? 40.411 32.183 18.854 1.00 9.18 ? 117 THR A C 1 ATOM 904 O O . THR A 1 117 ? 40.874 31.414 19.659 1.00 9.36 ? 117 THR A O 1 ATOM 905 C CB . THR A 1 117 ? 40.248 31.655 16.438 1.00 10.62 ? 117 THR A CB 1 ATOM 906 O OG1 . THR A 1 117 ? 40.070 30.290 16.830 1.00 10.40 ? 117 THR A OG1 1 ATOM 907 C CG2 . THR A 1 117 ? 40.866 31.740 15.107 1.00 7.96 ? 117 THR A CG2 1 ATOM 908 N N . ASN A 1 118 ? 39.267 32.839 19.110 1.00 9.79 ? 118 ASN A N 1 ATOM 909 C CA . ASN A 1 118 ? 38.553 32.545 20.327 1.00 9.81 ? 118 ASN A CA 1 ATOM 910 C C . ASN A 1 118 ? 38.121 31.084 20.445 1.00 10.15 ? 118 ASN A C 1 ATOM 911 O O . ASN A 1 118 ? 38.093 30.556 21.582 1.00 11.53 ? 118 ASN A O 1 ATOM 912 C CB . ASN A 1 118 ? 37.351 33.443 20.461 1.00 11.66 ? 118 ASN A CB 1 ATOM 913 C CG . ASN A 1 118 ? 37.723 34.832 20.972 1.00 13.78 ? 118 ASN A CG 1 ATOM 914 O OD1 . ASN A 1 118 ? 38.870 35.199 21.064 1.00 15.04 ? 118 ASN A OD1 1 ATOM 915 N ND2 . ASN A 1 118 ? 36.740 35.583 21.253 1.00 22.55 ? 118 ASN A ND2 1 ATOM 916 N N . ASP A 1 119 ? 37.762 30.438 19.308 1.00 8.72 ? 119 ASP A N 1 ATOM 917 C CA . ASP A 1 119 ? 37.430 29.016 19.343 1.00 10.41 ? 119 ASP A CA 1 ATOM 918 C C . ASP A 1 119 ? 38.652 28.213 19.800 1.00 8.69 ? 119 ASP A C 1 ATOM 919 O O . ASP A 1 119 ? 38.517 27.302 20.605 1.00 9.99 ? 119 ASP A O 1 ATOM 920 C CB . ASP A 1 119 ? 36.966 28.520 17.949 1.00 12.53 ? 119 ASP A CB 1 ATOM 921 C CG . ASP A 1 119 ? 35.620 28.027 17.897 1.00 17.86 ? 119 ASP A CG 1 ATOM 922 O OD1 . ASP A 1 119 ? 34.955 27.971 18.914 1.00 21.93 ? 119 ASP A OD1 1 ATOM 923 O OD2 . ASP A 1 119 ? 35.207 27.611 16.812 1.00 27.66 ? 119 ASP A OD2 1 ATOM 924 N N . GLU A 1 120 ? 39.827 28.518 19.237 1.00 8.86 ? 120 GLU A N 1 ATOM 925 C CA . GLU A 1 120 ? 41.057 27.838 19.623 1.00 10.15 ? 120 GLU A CA 1 ATOM 926 C C . GLU A 1 120 ? 41.392 28.049 21.079 1.00 10.63 ? 120 GLU A C 1 ATOM 927 O O . GLU A 1 120 ? 41.876 27.129 21.772 1.00 11.02 ? 120 GLU A O 1 ATOM 928 C CB . GLU A 1 120 ? 42.216 28.253 18.685 1.00 10.50 ? 120 GLU A CB 1 ATOM 929 C CG . GLU A 1 120 ? 42.067 27.586 17.343 1.00 11.87 ? 120 GLU A CG 1 ATOM 930 C CD . GLU A 1 120 ? 42.942 28.159 16.258 1.00 14.31 ? 120 GLU A CD 1 ATOM 931 O OE1 . GLU A 1 120 ? 43.445 29.310 16.406 1.00 12.43 ? 120 GLU A OE1 1 ATOM 932 O OE2 . GLU A 1 120 ? 43.099 27.453 15.235 1.00 15.87 ? 120 GLU A OE2 1 ATOM 933 N N . LYS A 1 121 ? 41.200 29.280 21.540 1.00 9.04 ? 121 LYS A N 1 ATOM 934 C CA . LYS A 1 121 ? 41.386 29.563 22.971 1.00 8.56 ? 121 LYS A CA 1 ATOM 935 C C . LYS A 1 121 ? 40.474 28.705 23.865 1.00 8.02 ? 121 LYS A C 1 ATOM 936 O O . LYS A 1 121 ? 40.945 28.220 24.891 1.00 10.54 ? 121 LYS A O 1 ATOM 937 C CB . LYS A 1 121 ? 41.159 31.070 23.228 1.00 8.83 ? 121 LYS A CB 1 ATOM 938 C CG . LYS A 1 121 ? 42.297 31.945 22.680 1.00 10.45 ? 121 LYS A CG 1 ATOM 939 C CD . LYS A 1 121 ? 41.999 33.447 22.773 1.00 11.06 ? 121 LYS A CD 1 ATOM 940 C CE . LYS A 1 121 ? 43.153 34.297 22.288 1.00 11.01 ? 121 LYS A CE 1 ATOM 941 N NZ . LYS A 1 121 ? 42.714 35.733 22.252 1.00 11.79 ? 121 LYS A NZ 1 ATOM 942 N N . GLN A 1 122 ? 39.194 28.496 23.496 1.00 10.17 ? 122 GLN A N 1 ATOM 943 C CA . GLN A 1 122 ? 38.317 27.674 24.262 1.00 9.48 ? 122 GLN A CA 1 ATOM 944 C C . GLN A 1 122 ? 38.651 26.185 24.156 1.00 9.30 ? 122 GLN A C 1 ATOM 945 O O . GLN A 1 122 ? 38.646 25.455 25.165 1.00 9.78 ? 122 GLN A O 1 ATOM 946 C CB . GLN A 1 122 ? 36.912 28.007 23.880 1.00 10.10 ? 122 GLN A CB 1 ATOM 947 C CG . GLN A 1 122 ? 35.908 27.310 24.803 1.00 10.61 ? 122 GLN A CG 1 ATOM 948 C CD . GLN A 1 122 ? 35.966 27.807 26.266 1.00 11.01 ? 122 GLN A CD 1 ATOM 949 O OE1 . GLN A 1 122 ? 35.802 28.991 26.570 1.00 13.99 ? 122 GLN A OE1 1 ATOM 950 N NE2 . GLN A 1 122 ? 36.172 26.888 27.168 1.00 13.81 ? 122 GLN A NE2 1 ATOM 951 N N . ALA A 1 123 ? 39.023 25.724 22.963 1.00 9.97 ? 123 ALA A N 1 ATOM 952 C CA . ALA A 1 123 ? 39.493 24.382 22.827 1.00 10.17 ? 123 ALA A CA 1 ATOM 953 C C . ALA A 1 123 ? 40.725 24.090 23.723 1.00 10.23 ? 123 ALA A C 1 ATOM 954 O O . ALA A 1 123 ? 40.840 23.025 24.376 1.00 11.84 ? 123 ALA A O 1 ATOM 955 C CB . ALA A 1 123 ? 39.869 24.136 21.375 1.00 12.81 ? 123 ALA A CB 1 ATOM 956 N N . ALA A 1 124 ? 41.625 25.061 23.757 1.00 9.25 ? 124 ALA A N 1 ATOM 957 C CA . ALA A 1 124 ? 42.770 24.948 24.620 1.00 10.72 ? 124 ALA A CA 1 ATOM 958 C C . ALA A 1 124 ? 42.342 24.906 26.105 1.00 7.92 ? 124 ALA A C 1 ATOM 959 O O . ALA A 1 124 ? 42.851 24.068 26.831 1.00 10.68 ? 124 ALA A O 1 ATOM 960 C CB . ALA A 1 124 ? 43.758 26.099 24.381 1.00 10.79 ? 124 ALA A CB 1 ATOM 961 N N . GLU A 1 125 ? 41.413 25.791 26.529 1.00 7.99 ? 125 GLU A N 1 ATOM 962 C CA . GLU A 1 125 ? 40.939 25.800 27.890 1.00 8.84 ? 125 GLU A CA 1 ATOM 963 C C . GLU A 1 125 ? 40.409 24.418 28.261 1.00 9.08 ? 125 GLU A C 1 ATOM 964 O O . GLU A 1 125 ? 40.723 23.878 29.334 1.00 8.55 ? 125 GLU A O 1 ATOM 965 C CB . GLU A 1 125 ? 39.827 26.820 28.038 1.00 10.04 ? 125 GLU A CB 1 ATOM 966 C CG . GLU A 1 125 ? 39.141 26.805 29.429 1.00 9.22 ? 125 GLU A CG 1 ATOM 967 C CD . GLU A 1 125 ? 40.074 27.156 30.607 1.00 10.88 ? 125 GLU A CD 1 ATOM 968 O OE1 . GLU A 1 125 ? 41.227 27.672 30.367 1.00 12.32 ? 125 GLU A OE1 1 ATOM 969 O OE2 . GLU A 1 125 ? 39.697 26.831 31.772 1.00 10.45 ? 125 GLU A OE2 1 ATOM 970 N N . ASP A 1 126 ? 39.652 23.818 27.343 1.00 9.64 ? 126 ASP A N 1 ATOM 971 C CA . ASP A 1 126 ? 39.126 22.477 27.625 1.00 10.52 ? 126 ASP A CA 1 ATOM 972 C C . ASP A 1 126 ? 40.241 21.441 27.782 1.00 8.19 ? 126 ASP A C 1 ATOM 973 O O . ASP A 1 126 ? 40.139 20.516 28.627 1.00 12.41 ? 126 ASP A O 1 ATOM 974 C CB . ASP A 1 126 ? 38.148 22.062 26.545 1.00 12.04 ? 126 ASP A CB 1 ATOM 975 C CG . ASP A 1 126 ? 36.905 22.950 26.484 1.00 14.92 ? 126 ASP A CG 1 ATOM 976 O OD1 . ASP A 1 126 ? 36.633 23.792 27.369 1.00 15.64 ? 126 ASP A OD1 1 ATOM 977 O OD2 . ASP A 1 126 ? 36.218 22.790 25.445 1.00 23.60 ? 126 ASP A OD2 1 ATOM 978 N N . CYS A 1 127 ? 41.285 21.549 26.961 1.00 9.50 ? 127 CYS A N 1 ATOM 979 C CA . CYS A 1 127 ? 42.448 20.669 27.101 1.00 9.08 ? 127 CYS A CA 1 ATOM 980 C C . CYS A 1 127 ? 43.196 20.923 28.443 1.00 8.63 ? 127 CYS A C 1 ATOM 981 O O . CYS A 1 127 ? 43.576 19.982 29.105 1.00 9.36 ? 127 CYS A O 1 ATOM 982 C CB . CYS A 1 127 ? 43.326 20.845 25.887 1.00 12.98 ? 127 CYS A CB 1 ATOM 983 S SG . CYS A 1 127 ? 44.799 19.810 25.910 1.00 14.98 ? 127 CYS A SG 1 ATOM 984 N N . PHE A 1 128 ? 43.375 22.191 28.821 1.00 7.50 ? 128 PHE A N 1 ATOM 985 C CA . PHE A 1 128 ? 43.971 22.516 30.088 1.00 8.27 ? 128 PHE A CA 1 ATOM 986 C C . PHE A 1 128 ? 43.139 21.905 31.221 1.00 9.15 ? 128 PHE A C 1 ATOM 987 O O . PHE A 1 128 ? 43.720 21.320 32.138 1.00 9.74 ? 128 PHE A O 1 ATOM 988 C CB . PHE A 1 128 ? 44.128 24.021 30.246 1.00 8.19 ? 128 PHE A CB 1 ATOM 989 C CG . PHE A 1 128 ? 45.342 24.590 29.552 1.00 7.81 ? 128 PHE A CG 1 ATOM 990 C CD1 . PHE A 1 128 ? 46.585 24.371 30.070 1.00 7.32 ? 128 PHE A CD1 1 ATOM 991 C CD2 . PHE A 1 128 ? 45.245 25.295 28.392 1.00 11.22 ? 128 PHE A CD2 1 ATOM 992 C CE1 . PHE A 1 128 ? 47.741 24.882 29.410 1.00 9.12 ? 128 PHE A CE1 1 ATOM 993 C CE2 . PHE A 1 128 ? 46.364 25.809 27.754 1.00 12.18 ? 128 PHE A CE2 1 ATOM 994 C CZ . PHE A 1 128 ? 47.627 25.604 28.266 1.00 8.87 ? 128 PHE A CZ 1 ATOM 995 N N . ASP A 1 129 ? 41.811 21.973 31.123 1.00 9.14 ? 129 ASP A N 1 ATOM 996 C CA . ASP A 1 129 ? 40.983 21.421 32.152 1.00 9.83 ? 129 ASP A CA 1 ATOM 997 C C . ASP A 1 129 ? 41.191 19.922 32.308 1.00 9.55 ? 129 ASP A C 1 ATOM 998 O O . ASP A 1 129 ? 41.198 19.427 33.432 1.00 10.77 ? 129 ASP A O 1 ATOM 999 C CB . ASP A 1 129 ? 39.506 21.715 31.874 1.00 12.22 ? 129 ASP A CB 1 ATOM 1000 C CG . ASP A 1 129 ? 39.164 23.190 32.083 1.00 12.11 ? 129 ASP A CG 1 ATOM 1001 O OD1 . ASP A 1 129 ? 39.937 23.907 32.710 1.00 16.64 ? 129 ASP A OD1 1 ATOM 1002 O OD2 . ASP A 1 129 ? 38.076 23.619 31.596 1.00 19.96 ? 129 ASP A OD2 1 ATOM 1003 N N . ALA A 1 130 ? 41.353 19.216 31.184 1.00 9.90 ? 130 ALA A N 1 ATOM 1004 C CA . ALA A 1 130 ? 41.569 17.794 31.219 1.00 10.66 ? 130 ALA A CA 1 ATOM 1005 C C . ALA A 1 130 ? 42.954 17.512 31.848 1.00 11.41 ? 130 ALA A C 1 ATOM 1006 O O . ALA A 1 130 ? 43.175 16.408 32.314 1.00 15.97 ? 130 ALA A O 1 ATOM 1007 C CB . ALA A 1 130 ? 41.443 17.168 29.807 1.00 17.22 ? 130 ALA A CB 1 ATOM 1008 N N . GLY A 1 131 ? 43.857 18.501 31.857 1.00 7.95 ? 131 GLY A N 1 ATOM 1009 C CA . GLY A 1 131 ? 45.183 18.340 32.363 1.00 9.83 ? 131 GLY A CA 1 ATOM 1010 C C . GLY A 1 131 ? 45.444 19.125 33.662 1.00 8.52 ? 131 GLY A C 1 ATOM 1011 O O . GLY A 1 131 ? 46.587 19.570 33.928 1.00 8.37 ? 131 GLY A O 1 ATOM 1012 N N . LEU A 1 132 ? 44.400 19.375 34.429 1.00 8.48 ? 132 LEU A N 1 ATOM 1013 C CA . LEU A 1 132 ? 44.553 20.074 35.687 1.00 8.20 ? 132 LEU A CA 1 ATOM 1014 C C . LEU A 1 132 ? 45.472 19.287 36.612 1.00 8.68 ? 132 LEU A C 1 ATOM 1015 O O . LEU A 1 132 ? 45.434 18.053 36.659 1.00 9.80 ? 132 LEU A O 1 ATOM 1016 C CB . LEU A 1 132 ? 43.154 20.275 36.284 1.00 9.57 ? 132 LEU A CB 1 ATOM 1017 C CG . LEU A 1 132 ? 42.983 21.041 37.578 1.00 10.55 ? 132 LEU A CG 1 ATOM 1018 C CD1 . LEU A 1 132 ? 41.606 21.658 37.645 1.00 13.93 ? 132 LEU A CD1 1 ATOM 1019 C CD2 . LEU A 1 132 ? 43.176 20.196 38.830 1.00 12.66 ? 132 LEU A CD2 1 ATOM 1020 N N . LEU A 1 133 ? 46.333 20.040 37.307 1.00 7.35 ? 133 LEU A N 1 ATOM 1021 C CA . LEU A 1 133 ? 47.297 19.504 38.252 1.00 6.66 ? 133 LEU A CA 1 ATOM 1022 C C . LEU A 1 133 ? 46.734 19.555 39.682 1.00 7.24 ? 133 LEU A C 1 ATOM 1023 O O . LEU A 1 133 ? 46.713 20.609 40.308 1.00 10.08 ? 133 LEU A O 1 ATOM 1024 C CB . LEU A 1 133 ? 48.618 20.282 38.136 1.00 8.91 ? 133 LEU A CB 1 ATOM 1025 C CG . LEU A 1 133 ? 49.162 20.380 36.719 1.00 7.92 ? 133 LEU A CG 1 ATOM 1026 C CD1 . LEU A 1 133 ? 50.394 21.273 36.746 1.00 9.62 ? 133 LEU A CD1 1 ATOM 1027 C CD2 . LEU A 1 133 ? 49.471 19.043 36.087 1.00 11.08 ? 133 LEU A CD2 1 ATOM 1028 N N . PRO A 1 134 ? 46.197 18.443 40.153 1.00 8.56 ? 134 PRO A N 1 ATOM 1029 C CA . PRO A 1 134 ? 45.540 18.502 41.454 1.00 8.58 ? 134 PRO A CA 1 ATOM 1030 C C . PRO A 1 134 ? 46.405 18.787 42.668 1.00 7.12 ? 134 PRO A C 1 ATOM 1031 O O . PRO A 1 134 ? 47.527 18.281 42.814 1.00 9.56 ? 134 PRO A O 1 ATOM 1032 C CB . PRO A 1 134 ? 44.877 17.110 41.615 1.00 11.03 ? 134 PRO A CB 1 ATOM 1033 C CG . PRO A 1 134 ? 44.804 16.602 40.221 1.00 12.31 ? 134 PRO A CG 1 ATOM 1034 C CD . PRO A 1 134 ? 46.082 17.103 39.579 1.00 10.17 ? 134 PRO A CD 1 ATOM 1035 N N . CYS A 1 135 ? 45.848 19.611 43.569 1.00 8.03 ? 135 CYS A N 1 ATOM 1036 C CA . CYS A 1 135 ? 46.535 19.942 44.834 1.00 8.08 ? 135 CYS A CA 1 ATOM 1037 C C . CYS A 1 135 ? 46.951 18.640 45.544 1.00 8.24 ? 135 CYS A C 1 ATOM 1038 O O . CYS A 1 135 ? 48.023 18.515 46.102 1.00 9.28 ? 135 CYS A O 1 ATOM 1039 C CB . CYS A 1 135 ? 45.574 20.746 45.689 1.00 9.49 ? 135 CYS A CB 1 ATOM 1040 S SG . CYS A 1 135 ? 46.170 21.160 47.324 1.00 10.27 ? 135 CYS A SG 1 ATOM 1041 N N . THR A 1 136 ? 46.065 17.664 45.487 1.00 8.55 ? 136 THR A N 1 ATOM 1042 C CA . THR A 1 136 ? 46.201 16.422 46.240 1.00 8.39 ? 136 THR A CA 1 ATOM 1043 C C . THR A 1 136 ? 47.144 15.409 45.580 1.00 12.61 ? 136 THR A C 1 ATOM 1044 O O . THR A 1 136 ? 47.416 14.307 46.150 1.00 13.09 ? 136 THR A O 1 ATOM 1045 C CB . THR A 1 136 ? 44.803 15.780 46.426 1.00 10.96 ? 136 THR A CB 1 ATOM 1046 O OG1 . THR A 1 136 ? 44.130 15.696 45.154 1.00 11.66 ? 136 THR A OG1 1 ATOM 1047 C CG2 . THR A 1 136 ? 43.923 16.555 47.388 1.00 9.87 ? 136 THR A CG2 1 ATOM 1048 N N . ASP A 1 137 ? 47.735 15.763 44.433 1.00 10.23 ? 137 ASP A N 1 ATOM 1049 C CA . ASP A 1 137 ? 48.798 14.883 43.891 1.00 9.49 ? 137 ASP A CA 1 ATOM 1050 C C . ASP A 1 137 ? 50.162 15.054 44.504 1.00 11.35 ? 137 ASP A C 1 ATOM 1051 O O . ASP A 1 137 ? 51.070 14.251 44.198 1.00 15.11 ? 137 ASP A O 1 ATOM 1052 C CB . ASP A 1 137 ? 48.976 15.086 42.376 1.00 12.60 ? 137 ASP A CB 1 ATOM 1053 C CG . ASP A 1 137 ? 48.116 14.252 41.560 1.00 21.55 ? 137 ASP A CG 1 ATOM 1054 O OD1 . ASP A 1 137 ? 47.153 13.613 42.053 1.00 25.61 ? 137 ASP A OD1 1 ATOM 1055 O OD2 . ASP A 1 137 ? 48.395 14.287 40.347 1.00 25.67 ? 137 ASP A OD2 1 ATOM 1056 N N . VAL A 1 138 ? 50.294 16.056 45.377 1.00 11.38 ? 138 VAL A N 1 ATOM 1057 C CA . VAL A 1 138 ? 51.547 16.361 46.052 1.00 12.79 ? 138 VAL A CA 1 ATOM 1058 C C . VAL A 1 138 ? 51.499 15.755 47.407 1.00 13.87 ? 138 VAL A C 1 ATOM 1059 O O . VAL A 1 138 ? 50.660 16.090 48.187 1.00 14.30 ? 138 VAL A O 1 ATOM 1060 C CB . VAL A 1 138 ? 51.808 17.899 46.092 1.00 10.54 ? 138 VAL A CB 1 ATOM 1061 C CG1 . VAL A 1 138 ? 53.016 18.247 46.964 1.00 12.76 ? 138 VAL A CG1 1 ATOM 1062 C CG2 . VAL A 1 138 ? 52.020 18.386 44.656 1.00 14.56 ? 138 VAL A CG2 1 ATOM 1063 N N . SER A 1 139 ? 52.504 14.909 47.687 1.00 21.54 ? 139 SER A N 1 ATOM 1064 C CA . SER A 1 139 ? 52.642 14.228 48.944 1.00 21.12 ? 139 SER A CA 1 ATOM 1065 C C . SER A 1 139 ? 52.751 15.255 50.074 1.00 18.09 ? 139 SER A C 1 ATOM 1066 O O . SER A 1 139 ? 53.540 16.194 49.977 1.00 23.67 ? 139 SER A O 1 ATOM 1067 C CB . SER A 1 139 ? 53.920 13.370 48.928 1.00 30.66 ? 139 SER A CB 1 ATOM 1068 O OG . SER A 1 139 ? 53.891 12.520 50.014 1.00 33.71 ? 139 SER A OG 1 ATOM 1069 N N . GLY A 1 140 ? 51.896 15.143 51.086 1.00 21.12 ? 140 GLY A N 1 ATOM 1070 C CA . GLY A 1 140 ? 51.961 16.051 52.262 1.00 24.07 ? 140 GLY A CA 1 ATOM 1071 C C . GLY A 1 140 ? 51.299 17.416 52.130 1.00 19.93 ? 140 GLY A C 1 ATOM 1072 O O . GLY A 1 140 ? 51.215 18.190 53.092 1.00 23.31 ? 140 GLY A O 1 ATOM 1073 N N . GLN A 1 141 ? 50.839 17.761 50.955 1.00 14.20 ? 141 GLN A N 1 ATOM 1074 C CA . GLN A 1 141 ? 50.181 19.072 50.806 1.00 12.19 ? 141 GLN A CA 1 ATOM 1075 C C . GLN A 1 141 ? 48.755 18.949 51.301 1.00 14.40 ? 141 GLN A C 1 ATOM 1076 O O . GLN A 1 141 ? 48.008 17.994 50.923 1.00 13.32 ? 141 GLN A O 1 ATOM 1077 C CB . GLN A 1 141 ? 50.208 19.541 49.328 1.00 11.57 ? 141 GLN A CB 1 ATOM 1078 C CG . GLN A 1 141 ? 49.650 20.905 49.056 1.00 10.33 ? 141 GLN A CG 1 ATOM 1079 C CD . GLN A 1 141 ? 50.102 21.498 47.742 1.00 8.88 ? 141 GLN A CD 1 ATOM 1080 O OE1 . GLN A 1 141 ? 50.860 22.529 47.700 1.00 10.02 ? 141 GLN A OE1 1 ATOM 1081 N NE2 . GLN A 1 141 ? 49.789 20.797 46.631 1.00 8.14 ? 141 GLN A NE2 1 ATOM 1082 N N . GLU A 1 142 ? 48.361 19.939 52.109 1.00 12.76 ? 142 GLU A N 1 ATOM 1083 C CA . GLU A 1 142 ? 47.030 19.991 52.636 1.00 11.02 ? 142 GLU A CA 1 ATOM 1084 C C . GLU A 1 142 ? 46.094 20.784 51.761 1.00 11.78 ? 142 GLU A C 1 ATOM 1085 O O . GLU A 1 142 ? 46.381 21.944 51.489 1.00 15.24 ? 142 GLU A O 1 ATOM 1086 C CB . GLU A 1 142 ? 47.040 20.573 54.031 1.00 12.43 ? 142 GLU A CB 1 ATOM 1087 C CG . GLU A 1 142 ? 47.938 19.820 55.038 1.00 16.53 ? 142 GLU A CG 1 ATOM 1088 C CD . GLU A 1 142 ? 47.437 18.408 55.363 1.00 19.26 ? 142 GLU A CD 1 ATOM 1089 O OE1 . GLU A 1 142 ? 46.245 18.152 55.265 1.00 21.91 ? 142 GLU A OE1 1 ATOM 1090 O OE2 . GLU A 1 142 ? 48.279 17.558 55.750 1.00 30.54 ? 142 GLU A OE2 1 ATOM 1091 N N . CYS A 1 143 ? 45.037 20.140 51.255 1.00 10.07 ? 143 CYS A N 1 ATOM 1092 C CA . CYS A 1 143 ? 44.159 20.662 50.234 1.00 10.95 ? 143 CYS A CA 1 ATOM 1093 C C . CYS A 1 143 ? 42.771 20.834 50.816 1.00 8.15 ? 143 CYS A C 1 ATOM 1094 O O . CYS A 1 143 ? 41.939 19.925 50.763 1.00 11.99 ? 143 CYS A O 1 ATOM 1095 C CB . CYS A 1 143 ? 44.152 19.727 49.036 1.00 10.23 ? 143 CYS A CB 1 ATOM 1096 S SG . CYS A 1 143 ? 45.836 19.469 48.420 1.00 11.10 ? 143 CYS A SG 1 ATOM 1097 N N . GLY A 1 144 ? 42.513 22.026 51.362 1.00 10.24 ? 144 GLY A N 1 ATOM 1098 C CA . GLY A 1 144 ? 41.245 22.324 52.048 1.00 10.74 ? 144 GLY A CA 1 ATOM 1099 C C . GLY A 1 144 ? 40.147 22.647 51.051 1.00 9.01 ? 144 GLY A C 1 ATOM 1100 O O . GLY A 1 144 ? 40.382 22.880 49.831 1.00 10.13 ? 144 GLY A O 1 ATOM 1101 N N . TYR A 1 145 ? 38.912 22.701 51.596 1.00 9.13 ? 145 TYR A N 1 ATOM 1102 C CA . TYR A 1 145 ? 37.729 23.173 50.905 1.00 11.70 ? 145 TYR A CA 1 ATOM 1103 C C . TYR A 1 145 ? 37.463 24.649 51.264 1.00 10.31 ? 145 TYR A C 1 ATOM 1104 O O . TYR A 1 145 ? 37.846 25.137 52.351 1.00 12.14 ? 145 TYR A O 1 ATOM 1105 C CB . TYR A 1 145 ? 36.559 22.266 51.225 1.00 9.81 ? 145 TYR A CB 1 ATOM 1106 C CG . TYR A 1 145 ? 36.663 20.872 50.627 1.00 8.92 ? 145 TYR A CG 1 ATOM 1107 C CD1 . TYR A 1 145 ? 36.154 20.628 49.347 1.00 9.03 ? 145 TYR A CD1 1 ATOM 1108 C CD2 . TYR A 1 145 ? 37.372 19.845 51.271 1.00 13.24 ? 145 TYR A CD2 1 ATOM 1109 C CE1 . TYR A 1 145 ? 36.225 19.367 48.769 1.00 9.11 ? 145 TYR A CE1 1 ATOM 1110 C CE2 . TYR A 1 145 ? 37.476 18.600 50.704 1.00 13.05 ? 145 TYR A CE2 1 ATOM 1111 C CZ . TYR A 1 145 ? 36.908 18.342 49.451 1.00 11.86 ? 145 TYR A CZ 1 ATOM 1112 O OH . TYR A 1 145 ? 37.014 17.046 48.910 1.00 12.64 ? 145 TYR A OH 1 ATOM 1113 N N . SER A 1 146 ? 36.814 25.360 50.344 1.00 9.13 ? 146 SER A N 1 ATOM 1114 C CA . SER A 1 146 ? 36.607 26.787 50.528 1.00 7.95 ? 146 SER A CA 1 ATOM 1115 C C . SER A 1 146 ? 35.571 27.147 51.590 1.00 9.28 ? 146 SER A C 1 ATOM 1116 O O . SER A 1 146 ? 34.460 26.564 51.598 1.00 11.10 ? 146 SER A O 1 ATOM 1117 C CB . SER A 1 146 ? 36.101 27.368 49.213 1.00 9.16 ? 146 SER A CB 1 ATOM 1118 O OG . SER A 1 146 ? 35.635 28.730 49.315 1.00 10.01 ? 146 SER A OG 1 ATOM 1119 N N . ALA A 1 147 ? 35.906 28.155 52.386 1.00 10.14 ? 147 ALA A N 1 ATOM 1120 C CA . ALA A 1 147 ? 34.966 28.720 53.358 1.00 10.50 ? 147 ALA A CA 1 ATOM 1121 C C . ALA A 1 147 ? 33.820 29.461 52.712 1.00 9.69 ? 147 ALA A C 1 ATOM 1122 O O . ALA A 1 147 ? 32.850 29.832 53.406 1.00 11.37 ? 147 ALA A O 1 ATOM 1123 C CB . ALA A 1 147 ? 35.742 29.627 54.336 1.00 13.94 ? 147 ALA A CB 1 ATOM 1124 N N . ASP A 1 148 ? 33.910 29.705 51.413 1.00 9.96 ? 148 ASP A N 1 ATOM 1125 C CA . ASP A 1 148 ? 32.908 30.438 50.637 1.00 9.98 ? 148 ASP A CA 1 ATOM 1126 C C . ASP A 1 148 ? 32.058 29.493 49.751 1.00 11.22 ? 148 ASP A C 1 ATOM 1127 O O . ASP A 1 148 ? 31.311 29.959 48.858 1.00 10.94 ? 148 ASP A O 1 ATOM 1128 C CB . ASP A 1 148 ? 33.642 31.485 49.811 1.00 9.82 ? 148 ASP A CB 1 ATOM 1129 C CG . ASP A 1 148 ? 34.202 32.563 50.675 1.00 11.54 ? 148 ASP A CG 1 ATOM 1130 O OD1 . ASP A 1 148 ? 33.311 33.148 51.429 1.00 12.79 ? 148 ASP A OD1 1 ATOM 1131 O OD2 . ASP A 1 148 ? 35.422 32.844 50.567 1.00 16.13 ? 148 ASP A OD2 1 ATOM 1132 N N . CYS A 1 149 ? 32.115 28.186 50.073 1.00 9.41 ? 149 CYS A N 1 ATOM 1133 C CA . CYS A 1 149 ? 31.424 27.097 49.337 1.00 11.50 ? 149 CYS A CA 1 ATOM 1134 C C . CYS A 1 149 ? 30.724 26.212 50.374 1.00 11.54 ? 149 CYS A C 1 ATOM 1135 O O . CYS A 1 149 ? 31.104 26.235 51.538 1.00 14.78 ? 149 CYS A O 1 ATOM 1136 C CB . CYS A 1 149 ? 32.482 26.235 48.581 1.00 11.22 ? 149 CYS A CB 1 ATOM 1137 S SG . CYS A 1 149 ? 31.749 25.201 47.320 1.00 12.65 ? 149 CYS A SG 1 ATOM 1138 N N . THR A 1 150 ? 29.704 25.452 49.937 1.00 12.85 ? 150 THR A N 1 ATOM 1139 C CA . THR A 1 150 ? 29.144 24.399 50.780 1.00 15.25 ? 150 THR A CA 1 ATOM 1140 C C . THR A 1 150 ? 29.167 23.052 50.068 1.00 17.26 ? 150 THR A C 1 ATOM 1141 O O . THR A 1 150 ? 29.313 22.953 48.833 1.00 14.22 ? 150 THR A O 1 ATOM 1142 C CB . THR A 1 150 ? 27.675 24.713 51.247 1.00 16.73 ? 150 THR A CB 1 ATOM 1143 O OG1 . THR A 1 150 ? 26.789 24.824 50.111 1.00 20.89 ? 150 THR A OG1 1 ATOM 1144 C CG2 . THR A 1 150 ? 27.595 25.992 52.060 1.00 20.98 ? 150 THR A CG2 1 ATOM 1145 N N . GLU A 1 151 ? 28.979 22.017 50.865 1.00 16.10 ? 151 GLU A N 1 ATOM 1146 C CA . GLU A 1 151 ? 29.206 20.654 50.409 1.00 17.42 ? 151 GLU A CA 1 ATOM 1147 C C . GLU A 1 151 ? 28.348 20.333 49.176 1.00 16.15 ? 151 GLU A C 1 ATOM 1148 O O . GLU A 1 151 ? 27.106 20.621 49.115 1.00 22.85 ? 151 GLU A O 1 ATOM 1149 C CB . GLU A 1 151 ? 29.061 19.677 51.603 1.00 23.62 ? 151 GLU A CB 1 ATOM 1150 C CG . GLU A 1 151 ? 29.539 18.273 51.313 1.00 40.30 ? 151 GLU A CG 1 ATOM 1151 C CD . GLU A 1 151 ? 29.387 17.335 52.494 1.00 55.89 ? 151 GLU A CD 1 ATOM 1152 O OE1 . GLU A 1 151 ? 29.044 17.849 53.599 1.00 51.05 ? 151 GLU A OE1 1 ATOM 1153 O OE2 . GLU A 1 151 ? 29.601 16.092 52.308 1.00 60.97 ? 151 GLU A OE2 1 ATOM 1154 N N . GLY A 1 152 ? 29.016 19.717 48.168 1.00 17.00 ? 152 GLY A N 1 ATOM 1155 C CA . GLY A 1 152 ? 28.388 19.284 46.927 1.00 18.65 ? 152 GLY A CA 1 ATOM 1156 C C . GLY A 1 152 ? 28.165 20.322 45.828 1.00 15.03 ? 152 GLY A C 1 ATOM 1157 O O . GLY A 1 152 ? 27.785 19.959 44.695 1.00 21.21 ? 152 GLY A O 1 ATOM 1158 N N . GLU A 1 153 ? 28.381 21.616 46.143 1.00 18.99 ? 153 GLU A N 1 ATOM 1159 C CA . GLU A 1 153 ? 28.352 22.674 45.108 1.00 17.14 ? 153 GLU A CA 1 ATOM 1160 C C . GLU A 1 153 ? 29.498 22.456 44.174 1.00 12.83 ? 153 GLU A C 1 ATOM 1161 O O . GLU A 1 153 ? 30.446 21.744 44.504 1.00 12.61 ? 153 GLU A O 1 ATOM 1162 C CB . GLU A 1 153 ? 28.458 24.046 45.721 1.00 15.59 ? 153 GLU A CB 1 ATOM 1163 C CG . GLU A 1 153 ? 27.260 24.426 46.542 1.00 20.09 ? 153 GLU A CG 1 ATOM 1164 C CD . GLU A 1 153 ? 27.295 25.890 46.910 1.00 27.92 ? 153 GLU A CD 1 ATOM 1165 O OE1 . GLU A 1 153 ? 28.330 26.446 47.285 1.00 24.70 ? 153 GLU A OE1 1 ATOM 1166 O OE2 . GLU A 1 153 ? 26.242 26.502 46.887 1.00 27.97 ? 153 GLU A OE2 1 ATOM 1167 N N . ALA A 1 154 ? 29.480 23.108 43.025 1.00 11.91 ? 154 ALA A N 1 ATOM 1168 C CA . ALA A 1 154 ? 30.523 22.919 42.027 1.00 10.81 ? 154 ALA A CA 1 ATOM 1169 C C . ALA A 1 154 ? 31.850 23.479 42.449 1.00 11.56 ? 154 ALA A C 1 ATOM 1170 O O . ALA A 1 154 ? 32.867 23.210 41.842 1.00 15.66 ? 154 ALA A O 1 ATOM 1171 C CB . ALA A 1 154 ? 30.065 23.529 40.737 1.00 11.61 ? 154 ALA A CB 1 ATOM 1172 N N . CYS A 1 155 ? 31.873 24.294 43.480 1.00 10.20 ? 155 CYS A N 1 ATOM 1173 C CA . CYS A 1 155 ? 33.117 24.813 44.046 1.00 10.00 ? 155 CYS A CA 1 ATOM 1174 C C . CYS A 1 155 ? 33.716 23.885 45.137 1.00 8.98 ? 155 CYS A C 1 ATOM 1175 O O . CYS A 1 155 ? 34.826 24.193 45.685 1.00 11.93 ? 155 CYS A O 1 ATOM 1176 C CB . CYS A 1 155 ? 32.920 26.208 44.676 1.00 10.22 ? 155 CYS A CB 1 ATOM 1177 S SG . CYS A 1 155 ? 31.450 26.420 45.678 1.00 12.31 ? 155 CYS A SG 1 ATOM 1178 N N . TRP A 1 156 ? 33.000 22.791 45.451 1.00 10.65 ? 156 TRP A N 1 ATOM 1179 C CA . TRP A 1 156 ? 33.369 21.921 46.541 1.00 9.63 ? 156 TRP A CA 1 ATOM 1180 C C . TRP A 1 156 ? 34.329 20.828 46.015 1.00 8.97 ? 156 TRP A C 1 ATOM 1181 O O . TRP A 1 156 ? 33.991 19.663 45.917 1.00 9.76 ? 156 TRP A O 1 ATOM 1182 C CB . TRP A 1 156 ? 32.132 21.279 47.184 1.00 12.41 ? 156 TRP A CB 1 ATOM 1183 C CG . TRP A 1 156 ? 32.466 20.682 48.537 1.00 11.55 ? 156 TRP A CG 1 ATOM 1184 C CD1 . TRP A 1 156 ? 32.664 19.356 48.829 1.00 14.46 ? 156 TRP A CD1 1 ATOM 1185 C CD2 . TRP A 1 156 ? 32.658 21.390 49.784 1.00 15.21 ? 156 TRP A CD2 1 ATOM 1186 N NE1 . TRP A 1 156 ? 32.975 19.197 50.164 1.00 16.88 ? 156 TRP A NE1 1 ATOM 1187 C CE2 . TRP A 1 156 ? 32.958 20.419 50.776 1.00 18.89 ? 156 TRP A CE2 1 ATOM 1188 C CE3 . TRP A 1 156 ? 32.631 22.740 50.148 1.00 13.06 ? 156 TRP A CE3 1 ATOM 1189 C CZ2 . TRP A 1 156 ? 33.178 20.760 52.106 1.00 19.24 ? 156 TRP A CZ2 1 ATOM 1190 C CZ3 . TRP A 1 156 ? 32.843 23.088 51.479 1.00 12.91 ? 156 TRP A CZ3 1 ATOM 1191 C CH2 . TRP A 1 156 ? 33.124 22.107 52.434 1.00 20.11 ? 156 TRP A CH2 1 ATOM 1192 N N . ARG A 1 157 ? 35.538 21.229 45.710 1.00 9.24 ? 157 ARG A N 1 ATOM 1193 C CA . ARG A 1 157 ? 36.541 20.398 45.045 1.00 8.56 ? 157 ARG A CA 1 ATOM 1194 C C . ARG A 1 157 ? 37.934 20.822 45.483 1.00 9.33 ? 157 ARG A C 1 ATOM 1195 O O . ARG A 1 157 ? 38.263 22.021 45.489 1.00 12.26 ? 157 ARG A O 1 ATOM 1196 C CB . ARG A 1 157 ? 36.368 20.450 43.517 1.00 10.62 ? 157 ARG A CB 1 ATOM 1197 C CG . ARG A 1 157 ? 36.415 21.829 42.921 1.00 9.87 ? 157 ARG A CG 1 ATOM 1198 C CD . ARG A 1 157 ? 35.959 21.824 41.458 1.00 10.79 ? 157 ARG A CD 1 ATOM 1199 N NE . ARG A 1 157 ? 36.939 21.103 40.653 1.00 11.44 ? 157 ARG A NE 1 ATOM 1200 C CZ . ARG A 1 157 ? 36.911 21.019 39.327 1.00 9.48 ? 157 ARG A CZ 1 ATOM 1201 N NH1 . ARG A 1 157 ? 37.932 20.404 38.689 1.00 13.23 ? 157 ARG A NH1 1 ATOM 1202 N NH2 . ARG A 1 157 ? 35.929 21.635 38.645 1.00 11.46 ? 157 ARG A NH2 1 ATOM 1203 N N . ASN A 1 158 ? 38.753 19.852 45.883 1.00 8.35 ? 158 ASN A N 1 ATOM 1204 C CA . ASN A 1 158 ? 40.114 20.158 46.392 1.00 8.76 ? 158 ASN A CA 1 ATOM 1205 C C . ASN A 1 158 ? 41.217 19.656 45.472 1.00 7.98 ? 158 ASN A C 1 ATOM 1206 O O . ASN A 1 158 ? 42.378 19.582 45.910 1.00 10.94 ? 158 ASN A O 1 ATOM 1207 C CB . ASN A 1 158 ? 40.286 19.690 47.807 1.00 9.25 ? 158 ASN A CB 1 ATOM 1208 C CG . ASN A 1 158 ? 40.479 18.212 47.905 1.00 8.88 ? 158 ASN A CG 1 ATOM 1209 O OD1 . ASN A 1 158 ? 40.143 17.446 46.978 1.00 9.12 ? 158 ASN A OD1 1 ATOM 1210 N ND2 . ASN A 1 158 ? 40.963 17.765 49.051 1.00 9.93 ? 158 ASN A ND2 1 ATOM 1211 N N . ASP A 1 159 ? 40.865 19.401 44.191 1.00 7.75 ? 159 ASP A N 1 ATOM 1212 C CA . ASP A 1 159 ? 41.874 19.400 43.122 1.00 8.93 ? 159 ASP A CA 1 ATOM 1213 C C . ASP A 1 159 ? 42.358 20.821 42.901 1.00 8.70 ? 159 ASP A C 1 ATOM 1214 O O . ASP A 1 159 ? 43.545 21.059 42.779 1.00 9.56 ? 159 ASP A O 1 ATOM 1215 C CB . ASP A 1 159 ? 41.374 18.714 41.811 1.00 9.09 ? 159 ASP A CB 1 ATOM 1216 C CG . ASP A 1 159 ? 40.038 19.235 41.290 1.00 7.35 ? 159 ASP A CG 1 ATOM 1217 O OD1 . ASP A 1 159 ? 39.283 19.999 41.971 1.00 9.45 ? 159 ASP A OD1 1 ATOM 1218 O OD2 . ASP A 1 159 ? 39.761 18.867 40.125 1.00 11.44 ? 159 ASP A OD2 1 ATOM 1219 N N . TRP A 1 160 ? 41.444 21.793 42.791 1.00 8.58 ? 160 TRP A N 1 ATOM 1220 C CA . TRP A 1 160 ? 41.732 23.199 42.884 1.00 8.44 ? 160 TRP A CA 1 ATOM 1221 C C . TRP A 1 160 ? 42.278 23.539 44.305 1.00 8.85 ? 160 TRP A C 1 ATOM 1222 O O . TRP A 1 160 ? 41.988 22.852 45.300 1.00 9.37 ? 160 TRP A O 1 ATOM 1223 C CB . TRP A 1 160 ? 40.486 24.086 42.640 1.00 9.59 ? 160 TRP A CB 1 ATOM 1224 C CG . TRP A 1 160 ? 40.011 24.148 41.236 1.00 8.25 ? 160 TRP A CG 1 ATOM 1225 C CD1 . TRP A 1 160 ? 39.603 23.113 40.443 1.00 7.79 ? 160 TRP A CD1 1 ATOM 1226 C CD2 . TRP A 1 160 ? 39.785 25.327 40.496 1.00 6.65 ? 160 TRP A CD2 1 ATOM 1227 N NE1 . TRP A 1 160 ? 39.184 23.571 39.211 1.00 8.17 ? 160 TRP A NE1 1 ATOM 1228 C CE2 . TRP A 1 160 ? 39.269 24.935 39.209 1.00 7.16 ? 160 TRP A CE2 1 ATOM 1229 C CE3 . TRP A 1 160 ? 39.986 26.687 40.753 1.00 8.26 ? 160 TRP A CE3 1 ATOM 1230 C CZ2 . TRP A 1 160 ? 38.990 25.887 38.224 1.00 9.34 ? 160 TRP A CZ2 1 ATOM 1231 C CZ3 . TRP A 1 160 ? 39.718 27.608 39.775 1.00 9.00 ? 160 TRP A CZ3 1 ATOM 1232 C CH2 . TRP A 1 160 ? 39.196 27.235 38.570 1.00 9.26 ? 160 TRP A CH2 1 ATOM 1233 N N . PHE A 1 161 ? 43.061 24.624 44.344 1.00 7.62 ? 161 PHE A N 1 ATOM 1234 C CA . PHE A 1 161 ? 43.479 25.211 45.564 1.00 8.28 ? 161 PHE A CA 1 ATOM 1235 C C . PHE A 1 161 ? 42.485 26.270 45.995 1.00 7.33 ? 161 PHE A C 1 ATOM 1236 O O . PHE A 1 161 ? 41.744 26.831 45.169 1.00 7.61 ? 161 PHE A O 1 ATOM 1237 C CB . PHE A 1 161 ? 44.849 25.917 45.363 1.00 7.78 ? 161 PHE A CB 1 ATOM 1238 C CG . PHE A 1 161 ? 45.958 25.009 44.920 1.00 8.94 ? 161 PHE A CG 1 ATOM 1239 C CD1 . PHE A 1 161 ? 46.692 24.298 45.841 1.00 9.02 ? 161 PHE A CD1 1 ATOM 1240 C CD2 . PHE A 1 161 ? 46.284 24.883 43.598 1.00 9.31 ? 161 PHE A CD2 1 ATOM 1241 C CE1 . PHE A 1 161 ? 47.670 23.437 45.440 1.00 7.87 ? 161 PHE A CE1 1 ATOM 1242 C CE2 . PHE A 1 161 ? 47.307 24.047 43.200 1.00 9.43 ? 161 PHE A CE2 1 ATOM 1243 C CZ . PHE A 1 161 ? 47.991 23.324 44.122 1.00 8.17 ? 161 PHE A CZ 1 ATOM 1244 N N . THR A 1 162 ? 42.410 26.512 47.320 1.00 7.53 ? 162 THR A N 1 ATOM 1245 C CA . THR A 1 162 ? 41.570 27.591 47.819 1.00 7.75 ? 162 THR A CA 1 ATOM 1246 C C . THR A 1 162 ? 42.338 28.689 48.576 1.00 7.59 ? 162 THR A C 1 ATOM 1247 O O . THR A 1 162 ? 43.316 28.457 49.277 1.00 10.06 ? 162 THR A O 1 ATOM 1248 C CB . THR A 1 162 ? 40.399 27.043 48.679 1.00 11.28 ? 162 THR A CB 1 ATOM 1249 O OG1 . THR A 1 162 ? 39.436 28.106 48.931 1.00 10.86 ? 162 THR A OG1 1 ATOM 1250 C CG2 . THR A 1 162 ? 40.886 26.418 49.965 1.00 12.98 ? 162 THR A CG2 1 ATOM 1251 N N . CYS A 1 163 ? 41.884 29.923 48.411 1.00 7.84 ? 163 CYS A N 1 ATOM 1252 C CA . CYS A 1 163 ? 42.252 31.020 49.306 1.00 9.79 ? 163 CYS A CA 1 ATOM 1253 C C . CYS A 1 163 ? 41.496 30.814 50.597 1.00 9.53 ? 163 CYS A C 1 ATOM 1254 O O . CYS A 1 163 ? 40.574 30.016 50.654 1.00 10.08 ? 163 CYS A O 1 ATOM 1255 C CB . CYS A 1 163 ? 41.894 32.357 48.635 1.00 9.64 ? 163 CYS A CB 1 ATOM 1256 S SG . CYS A 1 163 ? 42.892 32.595 47.112 1.00 10.31 ? 163 CYS A SG 1 ATOM 1257 N N . ASN A 1 164 ? 41.910 31.523 51.622 1.00 9.31 ? 164 ASN A N 1 ATOM 1258 C CA . ASN A 1 164 ? 41.243 31.525 52.867 1.00 8.12 ? 164 ASN A CA 1 ATOM 1259 C C . ASN A 1 164 ? 39.917 32.319 52.789 1.00 10.98 ? 164 ASN A C 1 ATOM 1260 O O . ASN A 1 164 ? 39.705 33.031 51.803 1.00 9.56 ? 164 ASN A O 1 ATOM 1261 C CB . ASN A 1 164 ? 42.172 32.032 53.939 1.00 8.98 ? 164 ASN A CB 1 ATOM 1262 C CG . ASN A 1 164 ? 43.222 31.020 54.313 1.00 9.97 ? 164 ASN A CG 1 ATOM 1263 O OD1 . ASN A 1 164 ? 43.168 29.831 53.914 1.00 14.42 ? 164 ASN A OD1 1 ATOM 1264 N ND2 . ASN A 1 164 ? 44.214 31.471 55.011 1.00 13.25 ? 164 ASN A ND2 1 ATOM 1265 N N A GLY A 1 165 ? 39.071 32.177 53.810 0.50 10.57 ? 165 GLY A N 1 ATOM 1266 N N B GLY A 1 165 ? 39.050 32.258 53.791 0.50 9.85 ? 165 GLY A N 1 ATOM 1267 C CA A GLY A 1 165 ? 37.755 32.787 53.822 0.50 12.29 ? 165 GLY A CA 1 ATOM 1268 C CA B GLY A 1 165 ? 37.797 33.014 53.715 0.50 11.72 ? 165 GLY A CA 1 ATOM 1269 C C A GLY A 1 165 ? 37.857 34.278 53.622 0.50 13.35 ? 165 GLY A C 1 ATOM 1270 C C B GLY A 1 165 ? 37.974 34.509 53.939 0.50 13.87 ? 165 GLY A C 1 ATOM 1271 O O A GLY A 1 165 ? 38.732 34.920 54.216 0.50 15.67 ? 165 GLY A O 1 ATOM 1272 O O B GLY A 1 165 ? 38.982 34.923 54.472 0.50 15.08 ? 165 GLY A O 1 ATOM 1273 N N A PHE A 1 166 ? 36.953 34.797 52.764 0.50 16.19 ? 166 PHE A N 1 ATOM 1274 N N B PHE A 1 166 ? 36.993 35.314 53.511 0.50 19.48 ? 166 PHE A N 1 ATOM 1275 C CA A PHE A 1 166 ? 36.937 36.224 52.356 0.50 12.87 ? 166 PHE A CA 1 ATOM 1276 C CA B PHE A 1 166 ? 36.915 36.756 53.869 0.50 22.80 ? 166 PHE A CA 1 ATOM 1277 C C A PHE A 1 166 ? 36.802 37.078 53.667 0.50 14.97 ? 166 PHE A C 1 ATOM 1278 C C B PHE A 1 166 ? 36.864 36.934 55.400 0.50 29.88 ? 166 PHE A C 1 ATOM 1279 O O A PHE A 1 166 ? 37.018 38.280 53.680 0.50 20.11 ? 166 PHE A O 1 ATOM 1280 O O B PHE A 1 166 ? 37.273 37.992 55.862 0.50 62.42 ? 166 PHE A O 1 ATOM 1281 C CB A PHE A 1 166 ? 35.903 36.491 51.218 0.50 14.30 ? 166 PHE A CB 1 ATOM 1282 C CB B PHE A 1 166 ? 35.699 37.474 53.209 0.50 27.57 ? 166 PHE A CB 1 ATOM 1283 C CG A PHE A 1 166 ? 35.946 37.897 50.679 0.50 12.99 ? 166 PHE A CG 1 ATOM 1284 C CG B PHE A 1 166 ? 36.003 38.161 51.874 0.50 27.74 ? 166 PHE A CG 1 ATOM 1285 C CD1 A PHE A 1 166 ? 36.919 38.282 49.757 0.50 14.81 ? 166 PHE A CD1 1 ATOM 1286 C CD1 B PHE A 1 166 ? 36.542 37.463 50.813 0.50 36.37 ? 166 PHE A CD1 1 ATOM 1287 C CD2 A PHE A 1 166 ? 34.995 38.831 51.056 0.50 19.53 ? 166 PHE A CD2 1 ATOM 1288 C CD2 B PHE A 1 166 ? 35.663 39.501 51.662 0.50 30.37 ? 166 PHE A CD2 1 ATOM 1289 C CE1 A PHE A 1 166 ? 36.968 39.593 49.244 0.50 13.21 ? 166 PHE A CE1 1 ATOM 1290 C CE1 B PHE A 1 166 ? 36.797 38.099 49.599 0.50 45.77 ? 166 PHE A CE1 1 ATOM 1291 C CE2 A PHE A 1 166 ? 35.033 40.114 50.557 0.50 22.79 ? 166 PHE A CE2 1 ATOM 1292 C CE2 B PHE A 1 166 ? 35.904 40.129 50.455 0.50 26.10 ? 166 PHE A CE2 1 ATOM 1293 C CZ A PHE A 1 166 ? 36.020 40.491 49.651 0.50 17.96 ? 166 PHE A CZ 1 ATOM 1294 C CZ B PHE A 1 166 ? 36.481 39.442 49.421 0.50 41.19 ? 166 PHE A CZ 1 ATOM 1295 N N A GLU A 1 167 ? 36.439 36.414 54.761 0.30 23.82 ? 167 GLU A N 1 ATOM 1296 N N B GLU A 1 167 ? 36.387 35.947 56.191 0.70 29.18 ? 167 GLU A N 1 ATOM 1297 C CA A GLU A 1 167 ? 37.128 36.662 56.071 0.50 30.85 ? 167 GLU A CA 1 ATOM 1298 C CA B GLU A 1 167 ? 36.512 36.097 57.674 0.50 26.04 ? 167 GLU A CA 1 ATOM 1299 C C A GLU A 1 167 ? 36.428 36.281 57.398 0.50 27.77 ? 167 GLU A C 1 ATOM 1300 C C B GLU A 1 167 ? 37.369 35.123 58.552 0.50 34.69 ? 167 GLU A C 1 ATOM 1301 O O A GLU A 1 167 ? 35.383 36.764 57.734 0.50 37.44 ? 167 GLU A O 1 ATOM 1302 O O B GLU A 1 167 ? 37.300 35.263 59.796 0.50 26.52 ? 167 GLU A O 1 ATOM 1303 C CB A GLU A 1 167 ? 37.712 38.050 56.160 0.50 24.82 ? 167 GLU A CB 1 ATOM 1304 C CB B GLU A 1 167 ? 35.124 35.869 58.294 0.50 20.35 ? 167 GLU A CB 1 ATOM 1305 C CG A GLU A 1 167 ? 36.795 39.212 56.226 0.50 33.95 ? 167 GLU A CG 1 ATOM 1306 C CG B GLU A 1 167 ? 33.949 36.594 57.691 0.50 24.53 ? 167 GLU A CG 1 ATOM 1307 C CD A GLU A 1 167 ? 37.610 40.404 55.848 0.50 39.30 ? 167 GLU A CD 1 ATOM 1308 C CD B GLU A 1 167 ? 33.723 37.948 58.321 0.50 28.24 ? 167 GLU A CD 1 ATOM 1309 O OE1 A GLU A 1 167 ? 38.342 40.248 54.851 0.50 31.67 ? 167 GLU A OE1 1 ATOM 1310 O OE1 B GLU A 1 167 ? 33.467 38.906 57.564 0.50 40.08 ? 167 GLU A OE1 1 ATOM 1311 O OE2 A GLU A 1 167 ? 37.569 41.419 56.573 0.50 45.36 ? 167 GLU A OE2 1 ATOM 1312 O OE2 B GLU A 1 167 ? 33.798 38.059 59.562 0.50 38.33 ? 167 GLU A OE2 1 ATOM 1313 N N A ALA A 1 168 ? 37.123 35.482 58.188 0.50 39.16 ? 168 ALA A N 1 ATOM 1314 N N B ALA A 1 168 ? 38.275 34.289 58.017 0.50 29.28 ? 168 ALA A N 1 ATOM 1315 C CA A ALA A 1 168 ? 38.550 35.403 58.053 0.50 32.52 ? 168 ALA A CA 1 ATOM 1316 C CA B ALA A 1 168 ? 39.701 34.212 58.465 0.50 32.83 ? 168 ALA A CA 1 ATOM 1317 C C A ALA A 1 168 ? 39.066 34.004 58.372 0.50 24.89 ? 168 ALA A C 1 ATOM 1318 C C B ALA A 1 168 ? 40.254 35.113 59.570 0.50 38.37 ? 168 ALA A C 1 ATOM 1319 O O A ALA A 1 168 ? 38.430 33.268 59.155 0.50 35.64 ? 168 ALA A O 1 ATOM 1320 O O B ALA A 1 168 ? 40.584 36.292 59.366 0.50 43.90 ? 168 ALA A O 1 ATOM 1321 C CB A ALA A 1 168 ? 39.150 36.444 58.995 0.50 23.64 ? 168 ALA A CB 1 ATOM 1322 C CB B ALA A 1 168 ? 40.689 34.003 57.334 0.50 42.09 ? 168 ALA A CB 1 ATOM 1323 N N A SER A 1 169 ? 40.195 33.610 57.778 0.50 45.17 ? 169 SER A N 1 ATOM 1324 N N B SER A 1 169 ? 40.292 34.483 60.747 0.50 40.73 ? 169 SER A N 1 ATOM 1325 C CA A SER A 1 169 ? 40.916 32.440 58.293 0.50 42.69 ? 169 SER A CA 1 ATOM 1326 C CA B SER A 1 169 ? 40.742 35.084 61.962 0.50 44.81 ? 169 SER A CA 1 ATOM 1327 C C A SER A 1 169 ? 42.266 32.811 58.798 0.50 44.16 ? 169 SER A C 1 ATOM 1328 C C B SER A 1 169 ? 41.316 36.388 61.593 0.50 42.62 ? 169 SER A C 1 ATOM 1329 O O A SER A 1 169 ? 43.164 31.968 58.837 0.50 48.56 ? 169 SER A O 1 ATOM 1330 O O B SER A 1 169 ? 40.699 37.430 61.767 0.50 44.89 ? 169 SER A O 1 ATOM 1331 C CB A SER A 1 169 ? 41.064 31.301 57.302 0.50 38.55 ? 169 SER A CB 1 ATOM 1332 C CB B SER A 1 169 ? 41.876 34.235 62.491 0.50 47.34 ? 169 SER A CB 1 ATOM 1333 O OG A SER A 1 169 ? 41.743 30.200 57.886 0.50 34.75 ? 169 SER A OG 1 ATOM 1334 O OG B SER A 1 169 ? 42.665 33.855 61.373 0.50 40.56 ? 169 SER A OG 1 ATOM 1335 N N A ASP A 1 170 ? 42.412 34.079 59.161 0.50 32.53 ? 170 ASP A N 1 ATOM 1336 N N B ASP A 1 170 ? 42.456 36.234 60.930 0.50 53.82 ? 170 ASP A N 1 ATOM 1337 C CA A ASP A 1 170 ? 43.278 34.413 60.318 0.50 50.29 ? 170 ASP A CA 1 ATOM 1338 C CA B ASP A 1 170 ? 43.559 37.182 60.887 0.50 47.55 ? 170 ASP A CA 1 ATOM 1339 C C A ASP A 1 170 ? 44.255 35.411 59.820 0.50 44.95 ? 170 ASP A C 1 ATOM 1340 C C B ASP A 1 170 ? 44.441 36.756 59.732 0.50 38.34 ? 170 ASP A C 1 ATOM 1341 O O A ASP A 1 170 ? 45.095 36.002 60.524 0.50 66.14 ? 170 ASP A O 1 ATOM 1342 O O B ASP A 1 170 ? 45.509 37.345 59.503 0.50 43.19 ? 170 ASP A O 1 ATOM 1343 C CB A ASP A 1 170 ? 44.066 33.185 60.784 0.50 41.77 ? 170 ASP A CB 1 ATOM 1344 C CB B ASP A 1 170 ? 44.368 37.122 62.179 0.50 55.36 ? 170 ASP A CB 1 ATOM 1345 C CG A ASP A 1 170 ? 44.785 33.418 62.087 0.50 45.46 ? 170 ASP A CG 1 ATOM 1346 C CG B ASP A 1 170 ? 44.529 35.700 62.707 0.50 79.55 ? 170 ASP A CG 1 ATOM 1347 O OD1 A ASP A 1 170 ? 44.791 34.576 62.579 0.50 52.04 ? 170 ASP A OD1 1 ATOM 1348 O OD1 B ASP A 1 170 ? 44.932 34.797 61.932 0.50 88.83 ? 170 ASP A OD1 1 ATOM 1349 O OD2 A ASP A 1 170 ? 45.349 32.433 62.617 0.50 52.05 ? 170 ASP A OD2 1 ATOM 1350 O OD2 B ASP A 1 170 ? 44.253 35.493 63.910 0.50 94.18 ? 170 ASP A OD2 1 ATOM 1351 N N A ARG A 1 171 ? 43.946 35.676 58.585 0.50 30.34 ? 171 ARG A N 1 ATOM 1352 N N B ARG A 1 171 ? 44.001 35.707 59.024 0.50 27.82 ? 171 ARG A N 1 ATOM 1353 C CA A ARG A 1 171 ? 44.799 35.443 57.478 0.50 24.44 ? 171 ARG A CA 1 ATOM 1354 C CA B ARG A 1 171 ? 44.625 35.331 57.740 0.50 17.69 ? 171 ARG A CA 1 ATOM 1355 C C A ARG A 1 171 ? 43.733 35.262 56.414 0.50 16.91 ? 171 ARG A C 1 ATOM 1356 C C B ARG A 1 171 ? 43.642 35.210 56.556 0.50 15.00 ? 171 ARG A C 1 ATOM 1357 O O A ARG A 1 171 ? 43.641 34.230 55.773 0.50 14.91 ? 171 ARG A O 1 ATOM 1358 O O B ARG A 1 171 ? 43.616 34.203 55.876 0.50 15.54 ? 171 ARG A O 1 ATOM 1359 C CB A ARG A 1 171 ? 45.559 34.132 57.686 0.50 21.83 ? 171 ARG A CB 1 ATOM 1360 C CB B ARG A 1 171 ? 45.424 34.031 57.893 0.50 17.91 ? 171 ARG A CB 1 ATOM 1361 C CG A ARG A 1 171 ? 46.636 34.190 58.764 0.50 27.61 ? 171 ARG A CG 1 ATOM 1362 C CG B ARG A 1 171 ? 46.606 34.146 58.854 0.50 25.48 ? 171 ARG A CG 1 ATOM 1363 C CD A ARG A 1 171 ? 47.338 32.857 58.975 0.50 26.84 ? 171 ARG A CD 1 ATOM 1364 C CD B ARG A 1 171 ? 47.367 32.844 59.061 0.50 24.90 ? 171 ARG A CD 1 ATOM 1365 N NE A ARG A 1 171 ? 47.939 32.350 57.746 0.50 23.03 ? 171 ARG A NE 1 ATOM 1366 N NE B ARG A 1 171 ? 47.944 32.337 57.821 0.50 22.04 ? 171 ARG A NE 1 ATOM 1367 C CZ A ARG A 1 171 ? 49.106 31.705 57.689 0.50 16.15 ? 171 ARG A CZ 1 ATOM 1368 C CZ B ARG A 1 171 ? 49.130 31.726 57.732 0.50 17.22 ? 171 ARG A CZ 1 ATOM 1369 N NH1 A ARG A 1 171 ? 49.584 31.270 56.540 0.50 20.30 ? 171 ARG A NH1 1 ATOM 1370 N NH1 B ARG A 1 171 ? 49.858 31.542 58.813 0.50 25.38 ? 171 ARG A NH1 1 ATOM 1371 N NH2 A ARG A 1 171 ? 49.784 31.487 58.794 0.50 23.74 ? 171 ARG A NH2 1 ATOM 1372 N NH2 B ARG A 1 171 ? 49.579 31.291 56.571 0.50 21.97 ? 171 ARG A NH2 1 ATOM 1373 N N . PRO A 1 172 ? 42.859 36.259 56.287 1.00 19.32 ? 172 PRO A N 1 ATOM 1374 C CA . PRO A 1 172 ? 41.793 36.118 55.325 1.00 16.82 ? 172 PRO A CA 1 ATOM 1375 C C . PRO A 1 172 ? 42.297 36.108 53.878 1.00 13.06 ? 172 PRO A C 1 ATOM 1376 O O . PRO A 1 172 ? 43.377 36.616 53.538 1.00 15.28 ? 172 PRO A O 1 ATOM 1377 C CB . PRO A 1 172 ? 40.919 37.337 55.585 1.00 26.42 ? 172 PRO A CB 1 ATOM 1378 C CG . PRO A 1 172 ? 41.809 38.338 56.146 1.00 33.99 ? 172 PRO A CG 1 ATOM 1379 C CD . PRO A 1 172 ? 42.744 37.553 57.021 1.00 28.26 ? 172 PRO A CD 1 ATOM 1380 N N . LYS A 1 173 ? 41.439 35.551 53.045 1.00 12.25 ? 173 LYS A N 1 ATOM 1381 C CA . LYS A 1 173 ? 41.523 35.685 51.605 1.00 11.30 ? 173 LYS A CA 1 ATOM 1382 C C . LYS A 1 173 ? 42.779 35.077 51.030 1.00 9.51 ? 173 LYS A C 1 ATOM 1383 O O . LYS A 1 173 ? 43.332 34.121 51.592 1.00 12.00 ? 173 LYS A O 1 ATOM 1384 C CB . LYS A 1 173 ? 41.360 37.138 51.208 1.00 12.49 ? 173 LYS A CB 1 ATOM 1385 C CG . LYS A 1 173 ? 40.113 37.651 51.843 1.00 18.95 ? 173 LYS A CG 1 ATOM 1386 C CD . LYS A 1 173 ? 39.529 38.766 51.110 1.00 21.67 ? 173 LYS A CD 1 ATOM 1387 C CE . LYS A 1 173 ? 40.276 39.987 51.497 1.00 21.33 ? 173 LYS A CE 1 ATOM 1388 N NZ . LYS A 1 173 ? 39.297 41.115 51.496 1.00 45.60 ? 173 LYS A NZ 1 ATOM 1389 N N . CYS A 1 174 ? 43.170 35.549 49.850 1.00 8.83 ? 174 CYS A N 1 ATOM 1390 C CA . CYS A 1 174 ? 44.376 34.968 49.204 1.00 9.00 ? 174 CYS A CA 1 ATOM 1391 C C . CYS A 1 174 ? 45.694 35.277 49.909 1.00 9.40 ? 174 CYS A C 1 ATOM 1392 O O . CYS A 1 174 ? 46.569 34.400 49.951 1.00 9.87 ? 174 CYS A O 1 ATOM 1393 C CB . CYS A 1 174 ? 44.423 35.273 47.681 1.00 9.76 ? 174 CYS A CB 1 ATOM 1394 S SG . CYS A 1 174 ? 42.907 34.646 46.844 1.00 10.59 ? 174 CYS A SG 1 ATOM 1395 N N . GLN A 1 175 ? 45.799 36.487 50.463 1.00 9.23 ? 175 GLN A N 1 ATOM 1396 C CA . GLN A 1 175 ? 47.048 36.910 51.075 1.00 9.96 ? 175 GLN A CA 1 ATOM 1397 C C . GLN A 1 175 ? 47.309 35.995 52.284 1.00 9.44 ? 175 GLN A C 1 ATOM 1398 O O . GLN A 1 175 ? 48.428 35.791 52.647 1.00 10.25 ? 175 GLN A O 1 ATOM 1399 C CB . GLN A 1 175 ? 46.961 38.343 51.506 1.00 9.90 ? 175 GLN A CB 1 ATOM 1400 C CG . GLN A 1 175 ? 48.188 38.900 52.165 1.00 11.99 ? 175 GLN A CG 1 ATOM 1401 C CD . GLN A 1 175 ? 48.324 38.631 53.652 1.00 11.49 ? 175 GLN A CD 1 ATOM 1402 O OE1 . GLN A 1 175 ? 47.360 38.399 54.358 1.00 14.74 ? 175 GLN A OE1 1 ATOM 1403 N NE2 . GLN A 1 175 ? 49.546 38.671 54.119 1.00 13.73 ? 175 GLN A NE2 1 ATOM 1404 N N . GLY A 1 176 ? 46.237 35.522 52.946 1.00 10.95 ? 176 GLY A N 1 ATOM 1405 C CA . GLY A 1 176 ? 46.396 34.719 54.186 1.00 13.42 ? 176 GLY A CA 1 ATOM 1406 C C . GLY A 1 176 ? 47.069 33.373 53.954 1.00 11.52 ? 176 GLY A C 1 ATOM 1407 O O . GLY A 1 176 ? 47.550 32.719 54.889 1.00 12.92 ? 176 GLY A O 1 ATOM 1408 N N . VAL A 1 177 ? 47.051 32.912 52.709 1.00 10.65 ? 177 VAL A N 1 ATOM 1409 C CA . VAL A 1 177 ? 47.617 31.572 52.424 1.00 10.45 ? 177 VAL A CA 1 ATOM 1410 C C . VAL A 1 177 ? 49.083 31.466 52.807 1.00 9.22 ? 177 VAL A C 1 ATOM 1411 O O . VAL A 1 177 ? 49.484 30.614 53.658 1.00 12.07 ? 177 VAL A O 1 ATOM 1412 C CB . VAL A 1 177 ? 47.312 31.173 50.954 1.00 11.01 ? 177 VAL A CB 1 ATOM 1413 C CG1 . VAL A 1 177 ? 47.985 29.884 50.557 1.00 14.73 ? 177 VAL A CG1 1 ATOM 1414 C CG2 . VAL A 1 177 ? 45.823 31.147 50.684 1.00 10.61 ? 177 VAL A CG2 1 ATOM 1415 N N . ASP A 1 178 ? 49.913 32.336 52.235 1.00 10.77 ? 178 ASP A N 1 ATOM 1416 C CA . ASP A 1 178 ? 51.368 32.450 52.610 1.00 11.85 ? 178 ASP A CA 1 ATOM 1417 C C . ASP A 1 178 ? 51.553 33.379 53.803 1.00 11.27 ? 178 ASP A C 1 ATOM 1418 O O . ASP A 1 178 ? 52.534 33.205 54.551 1.00 11.54 ? 178 ASP A O 1 ATOM 1419 C CB . ASP A 1 178 ? 52.212 33.108 51.465 1.00 11.01 ? 178 ASP A CB 1 ATOM 1420 C CG . ASP A 1 178 ? 52.388 32.255 50.226 1.00 9.88 ? 178 ASP A CG 1 ATOM 1421 O OD1 . ASP A 1 178 ? 51.732 31.198 50.071 1.00 10.66 ? 178 ASP A OD1 1 ATOM 1422 O OD2 . ASP A 1 178 ? 53.196 32.696 49.374 1.00 12.17 ? 178 ASP A OD2 1 ATOM 1423 N N . ASN A 1 179 ? 50.605 34.315 53.997 1.00 12.17 ? 179 ASN A N 1 ATOM 1424 C CA . ASN A 1 179 ? 50.782 35.351 54.998 1.00 12.55 ? 179 ASN A CA 1 ATOM 1425 C C . ASN A 1 179 ? 52.165 36.016 54.856 1.00 10.26 ? 179 ASN A C 1 ATOM 1426 O O . ASN A 1 179 ? 52.910 36.238 55.852 1.00 16.17 ? 179 ASN A O 1 ATOM 1427 C CB . ASN A 1 179 ? 50.584 34.752 56.365 1.00 14.46 ? 179 ASN A CB 1 ATOM 1428 C CG . ASN A 1 179 ? 50.369 35.808 57.446 1.00 19.64 ? 179 ASN A CG 1 ATOM 1429 O OD1 . ASN A 1 179 ? 49.724 36.850 57.201 1.00 21.22 ? 179 ASN A OD1 1 ATOM 1430 N ND2 . ASN A 1 179 ? 50.867 35.529 58.671 1.00 24.85 ? 179 ASN A ND2 1 ATOM 1431 N N . ALA A 1 180 ? 52.478 36.323 53.594 1.00 11.81 ? 180 ALA A N 1 ATOM 1432 C CA . ALA A 1 180 ? 53.734 36.927 53.253 1.00 12.14 ? 180 ALA A CA 1 ATOM 1433 C C . ALA A 1 180 ? 53.700 38.460 53.437 1.00 12.26 ? 180 ALA A C 1 ATOM 1434 O O . ALA A 1 180 ? 52.648 39.048 53.655 1.00 13.72 ? 180 ALA A O 1 ATOM 1435 C CB . ALA A 1 180 ? 54.113 36.564 51.817 1.00 15.07 ? 180 ALA A CB 1 ATOM 1436 N N . GLU A 1 181 ? 54.862 39.091 53.321 1.00 15.28 ? 181 GLU A N 1 ATOM 1437 C CA . GLU A 1 181 ? 54.950 40.521 53.459 1.00 15.39 ? 181 GLU A CA 1 ATOM 1438 C C . GLU A 1 181 ? 54.579 41.240 52.150 1.00 12.41 ? 181 GLU A C 1 ATOM 1439 O O . GLU A 1 181 ? 54.649 40.678 51.034 1.00 12.55 ? 181 GLU A O 1 ATOM 1440 C CB . GLU A 1 181 ? 56.329 40.930 53.966 1.00 19.34 ? 181 GLU A CB 1 ATOM 1441 C CG . GLU A 1 181 ? 57.444 40.985 52.963 1.00 28.52 ? 181 GLU A CG 1 ATOM 1442 C CD . GLU A 1 181 ? 58.843 41.029 53.617 1.00 47.91 ? 181 GLU A CD 1 ATOM 1443 O OE1 . GLU A 1 181 ? 59.085 41.971 54.413 1.00 192.56 ? 181 GLU A OE1 1 ATOM 1444 O OE2 . GLU A 1 181 ? 59.662 40.137 53.333 1.00 78.53 ? 181 GLU A OE2 1 ATOM 1445 N N . LEU A 1 182 ? 54.123 42.466 52.305 1.00 11.31 ? 182 LEU A N 1 ATOM 1446 C CA . LEU A 1 182 ? 53.798 43.323 51.159 1.00 13.53 ? 182 LEU A CA 1 ATOM 1447 C C . LEU A 1 182 ? 55.068 43.473 50.320 1.00 11.84 ? 182 LEU A C 1 ATOM 1448 O O . LEU A 1 182 ? 56.142 43.639 50.873 1.00 12.92 ? 182 LEU A O 1 ATOM 1449 C CB . LEU A 1 182 ? 53.322 44.683 51.586 1.00 12.84 ? 182 LEU A CB 1 ATOM 1450 C CG . LEU A 1 182 ? 52.839 45.576 50.455 1.00 13.54 ? 182 LEU A CG 1 ATOM 1451 C CD1 . LEU A 1 182 ? 51.641 44.998 49.760 1.00 12.85 ? 182 LEU A CD1 1 ATOM 1452 C CD2 . LEU A 1 182 ? 52.414 46.886 51.100 1.00 21.50 ? 182 LEU A CD2 1 ATOM 1453 N N . ASN A 1 183 ? 54.901 43.484 48.994 1.00 13.43 ? 183 ASN A N 1 ATOM 1454 C CA . ASN A 1 183 ? 55.969 43.571 48.021 1.00 11.45 ? 183 ASN A CA 1 ATOM 1455 C C . ASN A 1 183 ? 56.864 42.340 48.013 1.00 12.21 ? 183 ASN A C 1 ATOM 1456 O O . ASN A 1 183 ? 58.031 42.388 47.577 1.00 16.30 ? 183 ASN A O 1 ATOM 1457 C CB . ASN A 1 183 ? 56.774 44.837 48.211 1.00 14.23 ? 183 ASN A CB 1 ATOM 1458 C CG . ASN A 1 183 ? 55.934 46.089 48.111 1.00 19.17 ? 183 ASN A CG 1 ATOM 1459 O OD1 . ASN A 1 183 ? 55.129 46.227 47.190 1.00 28.28 ? 183 ASN A OD1 1 ATOM 1460 N ND2 . ASN A 1 183 ? 56.095 47.003 49.088 1.00 28.26 ? 183 ASN A ND2 1 ATOM 1461 N N . SER A 1 184 ? 56.303 41.213 48.407 1.00 10.89 ? 184 SER A N 1 ATOM 1462 C CA . SER A 1 184 ? 56.976 39.921 48.206 1.00 12.50 ? 184 SER A CA 1 ATOM 1463 C C . SER A 1 184 ? 56.981 39.482 46.726 1.00 11.79 ? 184 SER A C 1 ATOM 1464 O O . SER A 1 184 ? 57.686 38.560 46.315 1.00 13.40 ? 184 SER A O 1 ATOM 1465 C CB . SER A 1 184 ? 56.367 38.874 49.127 1.00 12.00 ? 184 SER A CB 1 ATOM 1466 O OG . SER A 1 184 ? 54.958 38.823 49.057 1.00 12.17 ? 184 SER A OG 1 ATOM 1467 N N . CYS A 1 185 ? 56.129 40.169 45.971 1.00 12.13 ? 185 CYS A N 1 ATOM 1468 C CA . CYS A 1 185 ? 56.072 40.065 44.544 1.00 11.91 ? 185 CYS A CA 1 ATOM 1469 C C . CYS A 1 185 ? 55.494 41.327 43.958 1.00 9.93 ? 185 CYS A C 1 ATOM 1470 O O . CYS A 1 185 ? 54.847 42.071 44.667 1.00 13.45 ? 185 CYS A O 1 ATOM 1471 C CB . CYS A 1 185 ? 55.296 38.837 44.137 1.00 11.01 ? 185 CYS A CB 1 ATOM 1472 S SG . CYS A 1 185 ? 53.619 38.752 44.725 1.00 12.44 ? 185 CYS A SG 1 ATOM 1473 N N . TYR A 1 186 ? 55.761 41.576 42.669 1.00 10.47 ? 186 TYR A N 1 ATOM 1474 C CA . TYR A 1 186 ? 55.429 42.863 42.072 1.00 9.45 ? 186 TYR A CA 1 ATOM 1475 C C . TYR A 1 186 ? 53.967 42.938 41.652 1.00 9.82 ? 186 TYR A C 1 ATOM 1476 O O . TYR A 1 186 ? 53.500 42.144 40.851 1.00 10.51 ? 186 TYR A O 1 ATOM 1477 C CB . TYR A 1 186 ? 56.293 43.169 40.869 1.00 12.63 ? 186 TYR A CB 1 ATOM 1478 C CG . TYR A 1 186 ? 55.957 44.526 40.268 1.00 12.95 ? 186 TYR A CG 1 ATOM 1479 C CD1 . TYR A 1 186 ? 56.447 45.694 40.840 1.00 16.12 ? 186 TYR A CD1 1 ATOM 1480 C CD2 . TYR A 1 186 ? 55.131 44.640 39.170 1.00 12.05 ? 186 TYR A CD2 1 ATOM 1481 C CE1 . TYR A 1 186 ? 56.083 46.920 40.387 1.00 15.44 ? 186 TYR A CE1 1 ATOM 1482 C CE2 . TYR A 1 186 ? 54.759 45.882 38.655 1.00 15.59 ? 186 TYR A CE2 1 ATOM 1483 C CZ . TYR A 1 186 ? 55.223 47.023 39.258 1.00 14.41 ? 186 TYR A CZ 1 ATOM 1484 O OH . TYR A 1 186 ? 54.870 48.249 38.746 1.00 18.56 ? 186 TYR A OH 1 ATOM 1485 N N . THR A 1 187 ? 53.300 43.985 42.115 1.00 9.75 ? 187 THR A N 1 ATOM 1486 C CA . THR A 1 187 ? 52.087 44.467 41.479 1.00 11.62 ? 187 THR A CA 1 ATOM 1487 C C . THR A 1 187 ? 52.181 46.003 41.376 1.00 10.09 ? 187 THR A C 1 ATOM 1488 O O . THR A 1 187 ? 52.865 46.666 42.167 1.00 12.46 ? 187 THR A O 1 ATOM 1489 C CB . THR A 1 187 ? 50.771 44.044 42.183 1.00 12.18 ? 187 THR A CB 1 ATOM 1490 O OG1 . THR A 1 187 ? 50.732 44.623 43.459 1.00 12.90 ? 187 THR A OG1 1 ATOM 1491 C CG2 . THR A 1 187 ? 50.629 42.521 42.279 1.00 12.72 ? 187 THR A CG2 1 ATOM 1492 N N . SER A 1 188 ? 51.473 46.551 40.385 1.00 10.68 ? 188 SER A N 1 ATOM 1493 C CA . SER A 1 188 ? 51.602 47.968 40.120 1.00 9.34 ? 188 SER A CA 1 ATOM 1494 C C . SER A 1 188 ? 50.682 48.854 40.957 1.00 11.62 ? 188 SER A C 1 ATOM 1495 O O . SER A 1 188 ? 50.979 50.035 41.156 1.00 14.58 ? 188 SER A O 1 ATOM 1496 C CB . SER A 1 188 ? 51.355 48.269 38.653 1.00 10.02 ? 188 SER A CB 1 ATOM 1497 O OG . SER A 1 188 ? 49.976 48.135 38.255 1.00 11.55 ? 188 SER A OG 1 ATOM 1498 N N . ILE A 1 189 ? 49.533 48.347 41.393 1.00 11.14 ? 189 ILE A N 1 ATOM 1499 C CA . ILE A 1 189 ? 48.565 49.209 42.023 1.00 12.38 ? 189 ILE A CA 1 ATOM 1500 C C . ILE A 1 189 ? 48.886 49.520 43.504 1.00 11.37 ? 189 ILE A C 1 ATOM 1501 O O . ILE A 1 189 ? 48.986 50.680 43.883 1.00 12.35 ? 189 ILE A O 1 ATOM 1502 C CB . ILE A 1 189 ? 47.174 48.609 41.842 1.00 9.99 ? 189 ILE A CB 1 ATOM 1503 C CG1 . ILE A 1 189 ? 46.762 48.679 40.359 1.00 10.29 ? 189 ILE A CG1 1 ATOM 1504 C CG2 . ILE A 1 189 ? 46.161 49.313 42.731 1.00 12.10 ? 189 ILE A CG2 1 ATOM 1505 C CD1 . ILE A 1 189 ? 45.589 47.778 39.992 1.00 12.34 ? 189 ILE A CD1 1 ATOM 1506 N N . ALA A 1 190 ? 49.060 48.487 44.311 1.00 9.41 ? 190 ALA A N 1 ATOM 1507 C CA . ALA A 1 190 ? 49.281 48.692 45.722 1.00 11.27 ? 190 ALA A CA 1 ATOM 1508 C C . ALA A 1 190 ? 50.328 47.782 46.324 1.00 9.84 ? 190 ALA A C 1 ATOM 1509 O O . ALA A 1 190 ? 50.526 47.814 47.533 1.00 11.53 ? 190 ALA A O 1 ATOM 1510 C CB . ALA A 1 190 ? 47.944 48.551 46.473 1.00 11.67 ? 190 ALA A CB 1 ATOM 1511 N N . GLY A 1 191 ? 51.004 47.020 45.491 1.00 11.15 ? 191 GLY A N 1 ATOM 1512 C CA . GLY A 1 191 ? 52.108 46.107 45.914 1.00 10.26 ? 191 GLY A CA 1 ATOM 1513 C C . GLY A 1 191 ? 51.561 44.695 46.105 1.00 10.20 ? 191 GLY A C 1 ATOM 1514 O O . GLY A 1 191 ? 50.386 44.528 46.424 1.00 9.96 ? 191 GLY A O 1 ATOM 1515 N N . GLY A 1 192 ? 52.398 43.674 45.909 1.00 9.71 ? 192 GLY A N 1 ATOM 1516 C CA . GLY A 1 192 ? 51.948 42.318 45.797 1.00 10.98 ? 192 GLY A CA 1 ATOM 1517 C C . GLY A 1 192 ? 52.296 41.432 46.976 1.00 9.95 ? 192 GLY A C 1 ATOM 1518 O O . GLY A 1 192 ? 53.255 41.671 47.725 1.00 9.58 ? 192 GLY A O 1 ATOM 1519 N N . TYR A 1 193 ? 51.460 40.395 47.116 1.00 8.87 ? 193 TYR A N 1 ATOM 1520 C CA . TYR A 1 193 ? 51.691 39.322 48.061 1.00 9.62 ? 193 TYR A CA 1 ATOM 1521 C C . TYR A 1 193 ? 51.786 38.005 47.328 1.00 8.73 ? 193 TYR A C 1 ATOM 1522 O O . TYR A 1 193 ? 50.966 37.725 46.442 1.00 7.28 ? 193 TYR A O 1 ATOM 1523 C CB . TYR A 1 193 ? 50.478 39.250 49.019 1.00 8.97 ? 193 TYR A CB 1 ATOM 1524 C CG . TYR A 1 193 ? 50.313 40.425 50.015 1.00 8.43 ? 193 TYR A CG 1 ATOM 1525 C CD1 . TYR A 1 193 ? 51.086 40.520 51.198 1.00 11.39 ? 193 TYR A CD1 1 ATOM 1526 C CD2 . TYR A 1 193 ? 49.328 41.381 49.809 1.00 10.40 ? 193 TYR A CD2 1 ATOM 1527 C CE1 . TYR A 1 193 ? 50.858 41.540 52.078 1.00 11.89 ? 193 TYR A CE1 1 ATOM 1528 C CE2 . TYR A 1 193 ? 49.113 42.377 50.692 1.00 10.73 ? 193 TYR A CE2 1 ATOM 1529 C CZ . TYR A 1 193 ? 49.862 42.472 51.816 1.00 10.41 ? 193 TYR A CZ 1 ATOM 1530 O OH . TYR A 1 193 ? 49.605 43.474 52.679 1.00 13.62 ? 193 TYR A OH 1 ATOM 1531 N N . THR A 1 194 ? 52.712 37.149 47.722 1.00 8.70 ? 194 THR A N 1 ATOM 1532 C CA . THR A 1 194 ? 52.842 35.814 47.130 1.00 8.25 ? 194 THR A CA 1 ATOM 1533 C C . THR A 1 194 ? 51.697 34.902 47.614 1.00 8.23 ? 194 THR A C 1 ATOM 1534 O O . THR A 1 194 ? 51.215 34.998 48.733 1.00 9.94 ? 194 THR A O 1 ATOM 1535 C CB . THR A 1 194 ? 54.198 35.175 47.420 1.00 10.26 ? 194 THR A CB 1 ATOM 1536 O OG1 . THR A 1 194 ? 54.402 35.054 48.840 1.00 11.65 ? 194 THR A OG1 1 ATOM 1537 C CG2 . THR A 1 194 ? 55.298 36.009 46.780 1.00 12.20 ? 194 THR A CG2 1 ATOM 1538 N N . VAL A 1 195 ? 51.418 33.928 46.748 1.00 8.99 ? 195 VAL A N 1 ATOM 1539 C CA . VAL A 1 195 ? 50.488 32.858 47.002 1.00 7.72 ? 195 VAL A CA 1 ATOM 1540 C C . VAL A 1 195 ? 51.169 31.626 46.408 1.00 7.02 ? 195 VAL A C 1 ATOM 1541 O O . VAL A 1 195 ? 51.224 31.475 45.184 1.00 8.27 ? 195 VAL A O 1 ATOM 1542 C CB . VAL A 1 195 ? 49.090 33.082 46.427 1.00 7.93 ? 195 VAL A CB 1 ATOM 1543 C CG1 . VAL A 1 195 ? 48.153 32.029 46.996 1.00 10.51 ? 195 VAL A CG1 1 ATOM 1544 C CG2 . VAL A 1 195 ? 48.554 34.477 46.690 1.00 8.00 ? 195 VAL A CG2 1 ATOM 1545 N N . THR A 1 196 ? 51.641 30.741 47.306 1.00 7.52 ? 196 THR A N 1 ATOM 1546 C CA . THR A 1 196 ? 52.615 29.690 46.893 1.00 8.51 ? 196 THR A CA 1 ATOM 1547 C C . THR A 1 196 ? 52.093 28.272 47.211 1.00 7.34 ? 196 THR A C 1 ATOM 1548 O O . THR A 1 196 ? 51.551 28.052 48.327 1.00 9.12 ? 196 THR A O 1 ATOM 1549 C CB . THR A 1 196 ? 53.939 29.903 47.600 1.00 9.51 ? 196 THR A CB 1 ATOM 1550 O OG1 . THR A 1 196 ? 54.336 31.285 47.498 1.00 12.52 ? 196 THR A OG1 1 ATOM 1551 C CG2 . THR A 1 196 ? 55.038 29.000 46.993 1.00 11.72 ? 196 THR A CG2 1 ATOM 1552 N N . LYS A 1 197 ? 52.187 27.385 46.220 1.00 8.35 ? 197 LYS A N 1 ATOM 1553 C CA . LYS A 1 197 ? 51.776 25.998 46.323 1.00 7.57 ? 197 LYS A CA 1 ATOM 1554 C C . LYS A 1 197 ? 52.777 25.107 45.580 1.00 7.61 ? 197 LYS A C 1 ATOM 1555 O O . LYS A 1 197 ? 53.771 25.613 44.998 1.00 9.39 ? 197 LYS A O 1 ATOM 1556 C CB . LYS A 1 197 ? 50.358 25.804 45.797 1.00 7.65 ? 197 LYS A CB 1 ATOM 1557 C CG . LYS A 1 197 ? 49.271 26.571 46.516 1.00 9.24 ? 197 LYS A CG 1 ATOM 1558 C CD . LYS A 1 197 ? 49.030 26.062 47.906 1.00 8.20 ? 197 LYS A CD 1 ATOM 1559 C CE . LYS A 1 197 ? 47.841 26.696 48.565 1.00 9.27 ? 197 LYS A CE 1 ATOM 1560 N NZ . LYS A 1 197 ? 47.742 26.249 49.993 1.00 9.83 ? 197 LYS A NZ 1 ATOM 1561 N N . LYS A 1 198 ? 52.519 23.787 45.610 1.00 8.53 ? 198 LYS A N 1 ATOM 1562 C CA . LYS A 1 198 ? 53.208 22.829 44.795 1.00 8.72 ? 198 LYS A CA 1 ATOM 1563 C C . LYS A 1 198 ? 52.254 22.111 43.886 1.00 7.93 ? 198 LYS A C 1 ATOM 1564 O O . LYS A 1 198 ? 51.090 21.871 44.251 1.00 8.24 ? 198 LYS A O 1 ATOM 1565 C CB . LYS A 1 198 ? 54.006 21.814 45.637 1.00 10.25 ? 198 LYS A CB 1 ATOM 1566 C CG . LYS A 1 198 ? 55.178 22.411 46.359 1.00 16.68 ? 198 LYS A CG 1 ATOM 1567 C CD . LYS A 1 198 ? 56.032 21.376 47.080 1.00 22.60 ? 198 LYS A CD 1 ATOM 1568 C CE . LYS A 1 198 ? 57.229 22.034 47.766 1.00 35.60 ? 198 LYS A CE 1 ATOM 1569 N NZ . LYS A 1 198 ? 58.090 21.001 48.407 1.00 78.58 ? 198 LYS A NZ 1 ATOM 1570 N N . VAL A 1 199 ? 52.717 21.760 42.726 1.00 8.83 ? 199 VAL A N 1 ATOM 1571 C CA . VAL A 1 199 ? 51.979 20.875 41.826 1.00 8.44 ? 199 VAL A CA 1 ATOM 1572 C C . VAL A 1 199 ? 52.948 19.766 41.333 1.00 9.03 ? 199 VAL A C 1 ATOM 1573 O O . VAL A 1 199 ? 54.174 19.946 41.276 1.00 8.60 ? 199 VAL A O 1 ATOM 1574 C CB . VAL A 1 199 ? 51.353 21.612 40.648 1.00 8.01 ? 199 VAL A CB 1 ATOM 1575 C CG1 . VAL A 1 199 ? 50.181 22.481 41.121 1.00 9.85 ? 199 VAL A CG1 1 ATOM 1576 C CG2 . VAL A 1 199 ? 52.331 22.375 39.807 1.00 8.96 ? 199 VAL A CG2 1 ATOM 1577 N N . LYS A 1 200 ? 52.354 18.644 40.954 1.00 9.05 ? 200 LYS A N 1 ATOM 1578 C CA . LYS A 1 200 ? 53.090 17.548 40.401 1.00 9.12 ? 200 LYS A CA 1 ATOM 1579 C C . LYS A 1 200 ? 52.936 17.513 38.866 1.00 10.75 ? 200 LYS A C 1 ATOM 1580 O O . LYS A 1 200 ? 51.836 17.418 38.352 1.00 10.41 ? 200 LYS A O 1 ATOM 1581 C CB . LYS A 1 200 ? 52.657 16.197 41.009 1.00 10.42 ? 200 LYS A CB 1 ATOM 1582 C CG . LYS A 1 200 ? 53.575 15.066 40.550 1.00 12.21 ? 200 LYS A CG 1 ATOM 1583 C CD . LYS A 1 200 ? 53.086 13.802 41.249 1.00 18.45 ? 200 LYS A CD 1 ATOM 1584 C CE . LYS A 1 200 ? 53.795 12.584 40.692 1.00 24.97 ? 200 LYS A CE 1 ATOM 1585 N NZ . LYS A 1 200 ? 55.175 12.647 41.117 1.00 25.29 ? 200 LYS A NZ 1 ATOM 1586 N N . LEU A 1 201 ? 54.062 17.592 38.147 1.00 8.29 ? 201 LEU A N 1 ATOM 1587 C CA . LEU A 1 201 ? 53.995 17.610 36.699 1.00 9.04 ? 201 LEU A CA 1 ATOM 1588 C C . LEU A 1 201 ? 53.625 16.226 36.171 1.00 8.56 ? 201 LEU A C 1 ATOM 1589 O O . LEU A 1 201 ? 53.910 15.181 36.787 1.00 10.29 ? 201 LEU A O 1 ATOM 1590 C CB . LEU A 1 201 ? 55.352 18.059 36.144 1.00 8.64 ? 201 LEU A CB 1 ATOM 1591 C CG . LEU A 1 201 ? 55.741 19.442 36.468 1.00 8.79 ? 201 LEU A CG 1 ATOM 1592 C CD1 . LEU A 1 201 ? 57.132 19.745 35.925 1.00 10.10 ? 201 LEU A CD1 1 ATOM 1593 C CD2 . LEU A 1 201 ? 54.721 20.460 36.062 1.00 11.83 ? 201 LEU A CD2 1 ATOM 1594 N N . PRO A 1 202 ? 53.129 16.187 34.935 1.00 9.25 ? 202 PRO A N 1 ATOM 1595 C CA . PRO A 1 202 ? 52.927 14.888 34.292 1.00 10.12 ? 202 PRO A CA 1 ATOM 1596 C C . PRO A 1 202 ? 54.215 14.194 33.943 1.00 9.65 ? 202 PRO A C 1 ATOM 1597 O O . PRO A 1 202 ? 55.289 14.782 34.067 1.00 9.35 ? 202 PRO A O 1 ATOM 1598 C CB . PRO A 1 202 ? 52.120 15.229 33.078 1.00 11.71 ? 202 PRO A CB 1 ATOM 1599 C CG . PRO A 1 202 ? 52.337 16.697 32.822 1.00 13.56 ? 202 PRO A CG 1 ATOM 1600 C CD . PRO A 1 202 ? 52.730 17.322 34.098 1.00 10.36 ? 202 PRO A CD 1 ATOM 1601 N N . GLU A 1 203 ? 54.099 12.957 33.496 1.00 11.11 ? 203 GLU A N 1 ATOM 1602 C CA . GLU A 1 203 ? 55.259 12.076 33.341 1.00 10.08 ? 203 GLU A CA 1 ATOM 1603 C C . GLU A 1 203 ? 55.858 11.922 31.935 1.00 15.99 ? 203 GLU A C 1 ATOM 1604 O O . GLU A 1 203 ? 56.864 11.203 31.703 1.00 21.09 ? 203 GLU A O 1 ATOM 1605 C CB . GLU A 1 203 ? 54.954 10.729 33.918 1.00 12.01 ? 203 GLU A CB 1 ATOM 1606 C CG . GLU A 1 203 ? 54.769 10.770 35.417 1.00 14.20 ? 203 GLU A CG 1 ATOM 1607 C CD . GLU A 1 203 ? 54.596 9.422 36.047 1.00 15.61 ? 203 GLU A CD 1 ATOM 1608 O OE1 . GLU A 1 203 ? 55.072 8.406 35.522 1.00 16.53 ? 203 GLU A OE1 1 ATOM 1609 O OE2 . GLU A 1 203 ? 53.967 9.379 37.140 1.00 22.01 ? 203 GLU A OE2 1 ATOM 1610 N N . TYR A 1 204 ? 55.385 12.694 31.017 1.00 10.34 ? 204 TYR A N 1 ATOM 1611 C CA . TYR A 1 204 ? 55.985 12.711 29.674 1.00 9.80 ? 204 TYR A CA 1 ATOM 1612 C C . TYR A 1 204 ? 56.957 13.889 29.551 1.00 10.59 ? 204 TYR A C 1 ATOM 1613 O O . TYR A 1 204 ? 56.945 14.809 30.364 1.00 11.75 ? 204 TYR A O 1 ATOM 1614 C CB . TYR A 1 204 ? 54.868 12.811 28.618 1.00 13.66 ? 204 TYR A CB 1 ATOM 1615 C CG . TYR A 1 204 ? 54.019 14.032 28.743 1.00 11.37 ? 204 TYR A CG 1 ATOM 1616 C CD1 . TYR A 1 204 ? 54.429 15.297 28.252 1.00 12.08 ? 204 TYR A CD1 1 ATOM 1617 C CD2 . TYR A 1 204 ? 52.790 13.945 29.309 1.00 10.54 ? 204 TYR A CD2 1 ATOM 1618 C CE1 . TYR A 1 204 ? 53.619 16.437 28.395 1.00 11.18 ? 204 TYR A CE1 1 ATOM 1619 C CE2 . TYR A 1 204 ? 51.973 15.056 29.426 1.00 12.34 ? 204 TYR A CE2 1 ATOM 1620 C CZ . TYR A 1 204 ? 52.366 16.302 28.946 1.00 11.24 ? 204 TYR A CZ 1 ATOM 1621 O OH . TYR A 1 204 ? 51.610 17.428 29.129 1.00 13.40 ? 204 TYR A OH 1 ATOM 1622 N N . THR A 1 205 ? 57.851 13.836 28.573 1.00 10.45 ? 205 THR A N 1 ATOM 1623 C CA . THR A 1 205 ? 58.715 14.967 28.255 1.00 11.05 ? 205 THR A CA 1 ATOM 1624 C C . THR A 1 205 ? 58.166 15.769 27.100 1.00 9.03 ? 205 THR A C 1 ATOM 1625 O O . THR A 1 205 ? 57.511 15.228 26.200 1.00 12.34 ? 205 THR A O 1 ATOM 1626 C CB . THR A 1 205 ? 60.162 14.490 27.974 1.00 9.91 ? 205 THR A CB 1 ATOM 1627 O OG1 . THR A 1 205 ? 60.147 13.412 27.014 1.00 10.25 ? 205 THR A OG1 1 ATOM 1628 C CG2 . THR A 1 205 ? 60.827 14.029 29.274 1.00 10.23 ? 205 THR A CG2 1 ATOM 1629 N N . SER A 1 206 ? 58.507 17.074 27.122 1.00 10.20 ? 206 SER A N 1 ATOM 1630 C CA . SER A 1 206 ? 58.268 18.031 26.057 1.00 9.63 ? 206 SER A CA 1 ATOM 1631 C C . SER A 1 206 ? 59.236 19.182 26.147 1.00 8.30 ? 206 SER A C 1 ATOM 1632 O O . SER A 1 206 ? 59.499 19.707 27.250 1.00 9.93 ? 206 SER A O 1 ATOM 1633 C CB . SER A 1 206 ? 56.861 18.630 26.212 1.00 12.36 ? 206 SER A CB 1 ATOM 1634 O OG . SER A 1 206 ? 56.716 19.723 25.269 1.00 15.65 ? 206 SER A OG 1 ATOM 1635 N N . ASN A 1 207 ? 59.828 19.559 24.992 1.00 9.69 ? 207 ASN A N 1 ATOM 1636 C CA . ASN A 1 207 ? 60.776 20.672 24.961 1.00 10.69 ? 207 ASN A CA 1 ATOM 1637 C C . ASN A 1 207 ? 60.143 22.053 25.215 1.00 9.29 ? 207 ASN A C 1 ATOM 1638 O O . ASN A 1 207 ? 60.804 22.985 25.588 1.00 10.52 ? 207 ASN A O 1 ATOM 1639 C CB . ASN A 1 207 ? 61.541 20.684 23.650 1.00 13.66 ? 207 ASN A CB 1 ATOM 1640 C CG . ASN A 1 207 ? 62.765 19.803 23.665 1.00 11.54 ? 207 ASN A CG 1 ATOM 1641 O OD1 . ASN A 1 207 ? 63.409 19.621 24.669 1.00 11.74 ? 207 ASN A OD1 1 ATOM 1642 N ND2 . ASN A 1 207 ? 63.070 19.241 22.513 1.00 12.09 ? 207 ASN A ND2 1 ATOM 1643 N N . HIS A 1 208 ? 58.823 22.151 24.986 1.00 8.69 ? 208 HIS A N 1 ATOM 1644 C CA . HIS A 1 208 ? 58.156 23.397 25.164 1.00 8.91 ? 208 HIS A CA 1 ATOM 1645 C C . HIS A 1 208 ? 56.639 23.196 25.275 1.00 9.10 ? 208 HIS A C 1 ATOM 1646 O O . HIS A 1 208 ? 55.965 22.856 24.318 1.00 9.24 ? 208 HIS A O 1 ATOM 1647 C CB . HIS A 1 208 ? 58.457 24.331 23.984 1.00 11.05 ? 208 HIS A CB 1 ATOM 1648 C CG . HIS A 1 208 ? 58.055 25.762 24.200 1.00 9.52 ? 208 HIS A CG 1 ATOM 1649 N ND1 . HIS A 1 208 ? 58.463 26.765 23.362 1.00 11.62 ? 208 HIS A ND1 1 ATOM 1650 C CD2 . HIS A 1 208 ? 57.285 26.356 25.138 1.00 12.05 ? 208 HIS A CD2 1 ATOM 1651 C CE1 . HIS A 1 208 ? 57.972 27.921 23.779 1.00 11.30 ? 208 HIS A CE1 1 ATOM 1652 N NE2 . HIS A 1 208 ? 57.230 27.699 24.833 1.00 10.35 ? 208 HIS A NE2 1 ATOM 1653 N N . THR A 1 209 ? 56.153 23.393 26.463 1.00 9.51 ? 209 THR A N 1 ATOM 1654 C CA . THR A 1 209 ? 54.732 23.379 26.718 1.00 8.26 ? 209 THR A CA 1 ATOM 1655 C C . THR A 1 209 ? 54.381 24.571 27.664 1.00 9.07 ? 209 THR A C 1 ATOM 1656 O O . THR A 1 209 ? 55.164 25.484 27.886 1.00 8.89 ? 209 THR A O 1 ATOM 1657 C CB . THR A 1 209 ? 54.293 22.004 27.233 1.00 9.00 ? 209 THR A CB 1 ATOM 1658 O OG1 . THR A 1 209 ? 52.841 21.954 27.242 1.00 9.92 ? 209 THR A OG1 1 ATOM 1659 C CG2 . THR A 1 209 ? 54.897 21.660 28.641 1.00 11.47 ? 209 THR A CG2 1 ATOM 1660 N N . LEU A 1 210 ? 53.115 24.601 28.120 1.00 9.07 ? 210 LEU A N 1 ATOM 1661 C CA . LEU A 1 210 ? 52.554 25.660 28.889 1.00 7.44 ? 210 LEU A CA 1 ATOM 1662 C C . LEU A 1 210 ? 51.966 25.155 30.188 1.00 7.14 ? 210 LEU A C 1 ATOM 1663 O O . LEU A 1 210 ? 51.312 24.072 30.224 1.00 8.76 ? 210 LEU A O 1 ATOM 1664 C CB . LEU A 1 210 ? 51.489 26.440 28.135 1.00 7.28 ? 210 LEU A CB 1 ATOM 1665 C CG . LEU A 1 210 ? 51.923 27.146 26.880 1.00 7.95 ? 210 LEU A CG 1 ATOM 1666 C CD1 . LEU A 1 210 ? 50.744 27.691 26.163 1.00 9.97 ? 210 LEU A CD1 1 ATOM 1667 C CD2 . LEU A 1 210 ? 52.789 28.337 27.209 1.00 11.42 ? 210 LEU A CD2 1 ATOM 1668 N N A ILE A 1 211 ? 52.219 25.868 31.313 0.50 6.74 ? 211 ILE A N 1 ATOM 1669 N N B ILE A 1 211 ? 52.094 25.993 31.181 0.50 7.28 ? 211 ILE A N 1 ATOM 1670 C CA A ILE A 1 211 ? 51.353 25.818 32.549 0.50 6.67 ? 211 ILE A CA 1 ATOM 1671 C CA B ILE A 1 211 ? 51.287 25.812 32.335 0.50 8.41 ? 211 ILE A CA 1 ATOM 1672 C C A ILE A 1 211 ? 50.401 27.028 32.369 0.50 6.47 ? 211 ILE A C 1 ATOM 1673 C C B ILE A 1 211 ? 50.413 27.045 32.501 0.50 7.77 ? 211 ILE A C 1 ATOM 1674 O O A ILE A 1 211 ? 50.817 28.152 32.114 0.50 5.79 ? 211 ILE A O 1 ATOM 1675 O O B ILE A 1 211 ? 50.891 28.173 32.653 0.50 8.87 ? 211 ILE A O 1 ATOM 1676 C CB A ILE A 1 211 ? 52.111 25.945 33.924 0.50 7.04 ? 211 ILE A CB 1 ATOM 1677 C CB B ILE A 1 211 ? 52.204 25.427 33.454 0.50 8.39 ? 211 ILE A CB 1 ATOM 1678 C CG1 A ILE A 1 211 ? 53.123 24.787 34.117 0.70 10.62 ? 211 ILE A CG1 1 ATOM 1679 C CG1 B ILE A 1 211 ? 51.429 25.155 34.752 0.30 6.61 ? 211 ILE A CG1 1 ATOM 1680 C CG2 A ILE A 1 211 ? 51.128 26.029 35.105 0.70 9.58 ? 211 ILE A CG2 1 ATOM 1681 C CG2 B ILE A 1 211 ? 53.396 26.387 33.598 0.30 5.40 ? 211 ILE A CG2 1 ATOM 1682 C CD1 A ILE A 1 211 ? 54.068 25.052 35.264 0.70 12.75 ? 211 ILE A CD1 1 ATOM 1683 C CD1 B ILE A 1 211 ? 52.272 24.776 35.954 0.30 6.14 ? 211 ILE A CD1 1 ATOM 1684 N N . SER A 1 212 ? 49.093 26.800 32.506 1.00 7.86 ? 212 SER A N 1 ATOM 1685 C CA . SER A 1 212 ? 48.132 27.867 32.595 1.00 7.30 ? 212 SER A CA 1 ATOM 1686 C C . SER A 1 212 ? 47.570 27.934 34.036 1.00 7.10 ? 212 SER A C 1 ATOM 1687 O O . SER A 1 212 ? 47.041 26.934 34.576 1.00 8.39 ? 212 SER A O 1 ATOM 1688 C CB . SER A 1 212 ? 46.960 27.639 31.620 1.00 9.02 ? 212 SER A CB 1 ATOM 1689 O OG . SER A 1 212 ? 45.884 28.559 31.869 1.00 8.57 ? 212 SER A OG 1 ATOM 1690 N N . PHE A 1 213 ? 47.666 29.125 34.602 1.00 7.50 ? 213 PHE A N 1 ATOM 1691 C CA . PHE A 1 213 ? 47.131 29.520 35.920 1.00 7.19 ? 213 PHE A CA 1 ATOM 1692 C C . PHE A 1 213 ? 45.731 30.101 35.704 1.00 6.77 ? 213 PHE A C 1 ATOM 1693 O O . PHE A 1 213 ? 45.561 30.954 34.832 1.00 7.32 ? 213 PHE A O 1 ATOM 1694 C CB . PHE A 1 213 ? 48.021 30.596 36.486 1.00 7.49 ? 213 PHE A CB 1 ATOM 1695 C CG . PHE A 1 213 ? 47.458 31.345 37.652 1.00 8.29 ? 213 PHE A CG 1 ATOM 1696 C CD1 . PHE A 1 213 ? 47.302 30.744 38.907 1.00 9.04 ? 213 PHE A CD1 1 ATOM 1697 C CD2 . PHE A 1 213 ? 47.140 32.674 37.524 1.00 10.94 ? 213 PHE A CD2 1 ATOM 1698 C CE1 . PHE A 1 213 ? 46.820 31.476 39.988 1.00 9.62 ? 213 PHE A CE1 1 ATOM 1699 C CE2 . PHE A 1 213 ? 46.606 33.385 38.610 1.00 11.52 ? 213 PHE A CE2 1 ATOM 1700 C CZ . PHE A 1 213 ? 46.468 32.784 39.840 1.00 10.74 ? 213 PHE A CZ 1 ATOM 1701 N N . LYS A 1 214 ? 44.808 29.684 36.560 1.00 6.41 ? 214 LYS A N 1 ATOM 1702 C CA . LYS A 1 214 ? 43.408 30.199 36.507 1.00 6.57 ? 214 LYS A CA 1 ATOM 1703 C C . LYS A 1 214 ? 42.963 30.433 37.931 1.00 6.92 ? 214 LYS A C 1 ATOM 1704 O O . LYS A 1 214 ? 42.974 29.513 38.740 1.00 8.42 ? 214 LYS A O 1 ATOM 1705 C CB . LYS A 1 214 ? 42.472 29.236 35.794 1.00 8.15 ? 214 LYS A CB 1 ATOM 1706 C CG . LYS A 1 214 ? 41.067 29.740 35.624 1.00 8.53 ? 214 LYS A CG 1 ATOM 1707 C CD . LYS A 1 214 ? 40.342 28.778 34.731 1.00 8.18 ? 214 LYS A CD 1 ATOM 1708 C CE . LYS A 1 214 ? 38.963 29.201 34.221 1.00 9.89 ? 214 LYS A CE 1 ATOM 1709 N NZ . LYS A 1 214 ? 37.880 28.928 35.183 1.00 8.69 ? 214 LYS A NZ 1 ATOM 1710 N N . TRP A 1 215 ? 42.538 31.674 38.184 1.00 6.64 ? 215 TRP A N 1 ATOM 1711 C CA . TRP A 1 215 ? 42.033 32.117 39.489 1.00 6.12 ? 215 TRP A CA 1 ATOM 1712 C C . TRP A 1 215 ? 40.603 32.652 39.275 1.00 6.39 ? 215 TRP A C 1 ATOM 1713 O O . TRP A 1 215 ? 40.386 33.585 38.568 1.00 6.45 ? 215 TRP A O 1 ATOM 1714 C CB . TRP A 1 215 ? 42.934 33.197 40.092 1.00 7.35 ? 215 TRP A CB 1 ATOM 1715 C CG . TRP A 1 215 ? 42.356 33.889 41.336 1.00 7.90 ? 215 TRP A CG 1 ATOM 1716 C CD1 . TRP A 1 215 ? 41.522 33.353 42.296 1.00 8.09 ? 215 TRP A CD1 1 ATOM 1717 C CD2 . TRP A 1 215 ? 42.593 35.255 41.753 1.00 6.88 ? 215 TRP A CD2 1 ATOM 1718 N NE1 . TRP A 1 215 ? 41.261 34.273 43.246 1.00 8.47 ? 215 TRP A NE1 1 ATOM 1719 C CE2 . TRP A 1 215 ? 41.856 35.456 42.946 1.00 6.93 ? 215 TRP A CE2 1 ATOM 1720 C CE3 . TRP A 1 215 ? 43.323 36.333 41.217 1.00 7.42 ? 215 TRP A CE3 1 ATOM 1721 C CZ2 . TRP A 1 215 ? 41.844 36.649 43.617 1.00 8.63 ? 215 TRP A CZ2 1 ATOM 1722 C CZ3 . TRP A 1 215 ? 43.344 37.543 41.914 1.00 8.11 ? 215 TRP A CZ3 1 ATOM 1723 C CH2 . TRP A 1 215 ? 42.584 37.709 43.082 1.00 8.69 ? 215 TRP A CH2 1 ATOM 1724 N N . ASN A 1 216 ? 39.699 31.935 39.938 1.00 6.85 ? 216 ASN A N 1 ATOM 1725 C CA . ASN A 1 216 ? 38.284 32.300 39.945 1.00 7.40 ? 216 ASN A CA 1 ATOM 1726 C C . ASN A 1 216 ? 37.996 33.089 41.226 1.00 7.62 ? 216 ASN A C 1 ATOM 1727 O O . ASN A 1 216 ? 38.094 32.586 42.344 1.00 8.37 ? 216 ASN A O 1 ATOM 1728 C CB . ASN A 1 216 ? 37.416 31.048 39.901 1.00 7.98 ? 216 ASN A CB 1 ATOM 1729 C CG . ASN A 1 216 ? 37.190 30.541 38.533 1.00 7.45 ? 216 ASN A CG 1 ATOM 1730 O OD1 . ASN A 1 216 ? 38.115 30.311 37.764 1.00 8.07 ? 216 ASN A OD1 1 ATOM 1731 N ND2 . ASN A 1 216 ? 35.911 30.341 38.164 1.00 9.89 ? 216 ASN A ND2 1 ATOM 1732 N N . SER A 1 217 ? 37.698 34.374 41.046 1.00 8.64 ? 217 SER A N 1 ATOM 1733 C CA . SER A 1 217 ? 37.350 35.255 42.135 1.00 9.13 ? 217 SER A CA 1 ATOM 1734 C C . SER A 1 217 ? 36.038 34.853 42.787 1.00 7.49 ? 217 SER A C 1 ATOM 1735 O O . SER A 1 217 ? 35.046 34.498 42.114 1.00 10.37 ? 217 SER A O 1 ATOM 1736 C CB . SER A 1 217 ? 37.188 36.662 41.581 1.00 10.44 ? 217 SER A CB 1 ATOM 1737 O OG . SER A 1 217 ? 36.889 37.587 42.605 1.00 11.18 ? 217 SER A OG 1 ATOM 1738 N N . PHE A 1 218 ? 36.058 34.982 44.113 1.00 7.59 ? 218 PHE A N 1 ATOM 1739 C CA . PHE A 1 218 ? 34.818 34.909 44.926 1.00 8.90 ? 218 PHE A CA 1 ATOM 1740 C C . PHE A 1 218 ? 34.116 36.245 45.057 1.00 8.72 ? 218 PHE A C 1 ATOM 1741 O O . PHE A 1 218 ? 32.895 36.294 44.820 1.00 10.51 ? 218 PHE A O 1 ATOM 1742 C CB . PHE A 1 218 ? 35.064 34.321 46.307 1.00 8.83 ? 218 PHE A CB 1 ATOM 1743 C CG . PHE A 1 218 ? 33.891 34.445 47.224 1.00 10.08 ? 218 PHE A CG 1 ATOM 1744 C CD1 . PHE A 1 218 ? 32.731 33.745 46.931 1.00 10.30 ? 218 PHE A CD1 1 ATOM 1745 C CD2 . PHE A 1 218 ? 33.904 35.343 48.282 1.00 11.96 ? 218 PHE A CD2 1 ATOM 1746 C CE1 . PHE A 1 218 ? 31.589 33.937 47.706 1.00 13.94 ? 218 PHE A CE1 1 ATOM 1747 C CE2 . PHE A 1 218 ? 32.741 35.532 49.070 1.00 13.44 ? 218 PHE A CE2 1 ATOM 1748 C CZ . PHE A 1 218 ? 31.618 34.813 48.774 1.00 15.90 ? 218 PHE A CZ 1 ATOM 1749 N N . GLN A 1 219 ? 34.817 37.319 45.458 1.00 10.22 ? 219 GLN A N 1 ATOM 1750 C CA . GLN A 1 219 ? 34.186 38.650 45.731 1.00 10.93 ? 219 GLN A CA 1 ATOM 1751 C C . GLN A 1 219 ? 33.615 39.289 44.501 1.00 10.58 ? 219 GLN A C 1 ATOM 1752 O O . GLN A 1 219 ? 32.634 40.024 44.583 1.00 14.50 ? 219 GLN A O 1 ATOM 1753 C CB . GLN A 1 219 ? 35.245 39.602 46.304 1.00 16.56 ? 219 GLN A CB 1 ATOM 1754 C CG . GLN A 1 219 ? 34.736 41.028 46.485 1.00 21.37 ? 219 GLN A CG 1 ATOM 1755 C CD . GLN A 1 219 ? 35.829 42.057 46.799 1.00 21.60 ? 219 GLN A CD 1 ATOM 1756 O OE1 . GLN A 1 219 ? 37.030 41.858 46.464 1.00 19.06 ? 219 GLN A OE1 1 ATOM 1757 N NE2 . GLN A 1 219 ? 35.382 43.233 47.359 1.00 33.30 ? 219 GLN A NE2 1 ATOM 1758 N N . THR A 1 220 ? 34.196 38.976 43.348 1.00 9.90 ? 220 THR A N 1 ATOM 1759 C CA . THR A 1 220 ? 33.846 39.585 42.063 1.00 10.69 ? 220 THR A CA 1 ATOM 1760 C C . THR A 1 220 ? 33.593 38.505 40.987 1.00 10.91 ? 220 THR A C 1 ATOM 1761 O O . THR A 1 220 ? 34.072 37.369 41.086 1.00 12.26 ? 220 THR A O 1 ATOM 1762 C CB . THR A 1 220 ? 35.009 40.517 41.581 1.00 9.56 ? 220 THR A CB 1 ATOM 1763 O OG1 . THR A 1 220 ? 36.188 39.808 41.354 1.00 11.09 ? 220 THR A OG1 1 ATOM 1764 C CG2 . THR A 1 220 ? 35.307 41.588 42.642 1.00 11.44 ? 220 THR A CG2 1 ATOM 1765 N N . GLY A 1 221 ? 32.955 38.901 39.908 1.00 10.36 ? 221 GLY A N 1 ATOM 1766 C CA . GLY A 1 221 ? 32.685 38.028 38.763 1.00 11.39 ? 221 GLY A CA 1 ATOM 1767 C C . GLY A 1 221 ? 33.778 38.245 37.753 1.00 10.06 ? 221 GLY A C 1 ATOM 1768 O O . GLY A 1 221 ? 33.602 38.925 36.699 1.00 10.33 ? 221 GLY A O 1 ATOM 1769 N N . GLN A 1 222 ? 34.915 37.647 38.135 1.00 9.81 ? 222 GLN A N 1 ATOM 1770 C CA . GLN A 1 222 ? 36.178 37.847 37.421 1.00 8.42 ? 222 GLN A CA 1 ATOM 1771 C C . GLN A 1 222 ? 37.016 36.562 37.476 1.00 9.73 ? 222 GLN A C 1 ATOM 1772 O O . GLN A 1 222 ? 36.982 35.858 38.496 1.00 8.75 ? 222 GLN A O 1 ATOM 1773 C CB . GLN A 1 222 ? 36.983 38.976 38.011 1.00 9.68 ? 222 GLN A CB 1 ATOM 1774 C CG . GLN A 1 222 ? 36.380 40.373 37.927 1.00 8.56 ? 222 GLN A CG 1 ATOM 1775 C CD . GLN A 1 222 ? 37.235 41.397 38.665 1.00 11.30 ? 222 GLN A CD 1 ATOM 1776 O OE1 . GLN A 1 222 ? 37.752 41.162 39.791 1.00 11.83 ? 222 GLN A OE1 1 ATOM 1777 N NE2 . GLN A 1 222 ? 37.409 42.559 38.030 1.00 19.12 ? 222 GLN A NE2 1 ATOM 1778 N N . ILE A 1 223 ? 37.761 36.325 36.392 1.00 7.18 ? 223 ILE A N 1 ATOM 1779 C CA . ILE A 1 223 ? 38.756 35.257 36.327 1.00 7.94 ? 223 ILE A CA 1 ATOM 1780 C C . ILE A 1 223 ? 40.080 35.873 35.825 1.00 8.03 ? 223 ILE A C 1 ATOM 1781 O O . ILE A 1 223 ? 40.109 36.717 34.942 1.00 9.42 ? 223 ILE A O 1 ATOM 1782 C CB . ILE A 1 223 ? 38.270 34.108 35.398 1.00 9.21 ? 223 ILE A CB 1 ATOM 1783 C CG1 . ILE A 1 223 ? 36.969 33.497 35.954 1.00 8.07 ? 223 ILE A CG1 1 ATOM 1784 C CG2 . ILE A 1 223 ? 39.338 33.054 35.146 1.00 11.57 ? 223 ILE A CG2 1 ATOM 1785 C CD1 . ILE A 1 223 ? 36.277 32.508 35.040 1.00 9.49 ? 223 ILE A CD1 1 ATOM 1786 N N . TYR A 1 224 ? 41.133 35.391 36.461 1.00 8.06 ? 224 TYR A N 1 ATOM 1787 C CA . TYR A 1 224 ? 42.498 35.836 36.167 1.00 7.65 ? 224 TYR A CA 1 ATOM 1788 C C . TYR A 1 224 ? 43.238 34.642 35.588 1.00 7.26 ? 224 TYR A C 1 ATOM 1789 O O . TYR A 1 224 ? 43.397 33.611 36.277 1.00 8.26 ? 224 TYR A O 1 ATOM 1790 C CB . TYR A 1 224 ? 43.173 36.370 37.442 1.00 9.19 ? 224 TYR A CB 1 ATOM 1791 C CG . TYR A 1 224 ? 42.420 37.615 37.987 1.00 9.32 ? 224 TYR A CG 1 ATOM 1792 C CD1 . TYR A 1 224 ? 41.266 37.486 38.789 1.00 9.17 ? 224 TYR A CD1 1 ATOM 1793 C CD2 . TYR A 1 224 ? 42.832 38.878 37.666 1.00 8.72 ? 224 TYR A CD2 1 ATOM 1794 C CE1 . TYR A 1 224 ? 40.583 38.625 39.236 1.00 10.10 ? 224 TYR A CE1 1 ATOM 1795 C CE2 . TYR A 1 224 ? 42.189 39.999 38.116 1.00 9.67 ? 224 TYR A CE2 1 ATOM 1796 C CZ . TYR A 1 224 ? 41.003 39.873 38.871 1.00 9.92 ? 224 TYR A CZ 1 ATOM 1797 O OH . TYR A 1 224 ? 40.377 40.999 39.323 1.00 11.54 ? 224 TYR A OH 1 ATOM 1798 N N . LEU A 1 225 ? 43.705 34.793 34.361 1.00 7.88 ? 225 LEU A N 1 ATOM 1799 C CA . LEU A 1 225 ? 44.437 33.741 33.631 1.00 7.77 ? 225 LEU A CA 1 ATOM 1800 C C . LEU A 1 225 ? 45.818 34.223 33.256 1.00 7.65 ? 225 LEU A C 1 ATOM 1801 O O . LEU A 1 225 ? 45.976 35.363 32.783 1.00 8.18 ? 225 LEU A O 1 ATOM 1802 C CB . LEU A 1 225 ? 43.669 33.373 32.340 1.00 8.79 ? 225 LEU A CB 1 ATOM 1803 C CG . LEU A 1 225 ? 42.347 32.658 32.646 1.00 9.28 ? 225 LEU A CG 1 ATOM 1804 C CD1 . LEU A 1 225 ? 41.157 33.220 31.809 1.00 11.55 ? 225 LEU A CD1 1 ATOM 1805 C CD2 . LEU A 1 225 ? 42.482 31.176 32.464 1.00 10.43 ? 225 LEU A CD2 1 ATOM 1806 N N . SER A 1 226 ? 46.817 33.327 33.417 1.00 7.39 ? 226 SER A N 1 ATOM 1807 C CA . SER A 1 226 ? 48.213 33.581 32.932 1.00 7.83 ? 226 SER A CA 1 ATOM 1808 C C . SER A 1 226 ? 48.751 32.271 32.445 1.00 7.75 ? 226 SER A C 1 ATOM 1809 O O . SER A 1 226 ? 48.253 31.190 32.829 1.00 9.05 ? 226 SER A O 1 ATOM 1810 C CB . SER A 1 226 ? 49.133 33.926 34.110 1.00 9.07 ? 226 SER A CB 1 ATOM 1811 O OG . SER A 1 226 ? 48.670 34.846 35.000 1.00 10.00 ? 226 SER A OG 1 ATOM 1812 N N . CYS A 1 227 ? 49.840 32.311 31.693 1.00 6.94 ? 227 CYS A N 1 ATOM 1813 C CA . CYS A 1 227 ? 50.522 31.048 31.400 1.00 8.60 ? 227 CYS A CA 1 ATOM 1814 C C . CYS A 1 227 ? 52.037 31.271 31.374 1.00 7.69 ? 227 CYS A C 1 ATOM 1815 O O . CYS A 1 227 ? 52.504 32.371 31.175 1.00 8.90 ? 227 CYS A O 1 ATOM 1816 C CB . CYS A 1 227 ? 50.048 30.459 30.059 1.00 13.72 ? 227 CYS A CB 1 ATOM 1817 S SG . CYS A 1 227 ? 50.617 31.373 28.635 1.00 13.39 ? 227 CYS A SG 1 ATOM 1818 N N . ALA A 1 228 ? 52.724 30.171 31.614 1.00 8.30 ? 228 ALA A N 1 ATOM 1819 C CA . ALA A 1 228 ? 54.225 30.145 31.620 1.00 8.01 ? 228 ALA A CA 1 ATOM 1820 C C . ALA A 1 228 ? 54.660 29.091 30.660 1.00 7.64 ? 228 ALA A C 1 ATOM 1821 O O . ALA A 1 228 ? 54.137 27.957 30.675 1.00 8.45 ? 228 ALA A O 1 ATOM 1822 C CB . ALA A 1 228 ? 54.743 29.831 33.013 1.00 9.26 ? 228 ALA A CB 1 ATOM 1823 N N . ASP A 1 229 ? 55.705 29.438 29.887 1.00 8.03 ? 229 ASP A N 1 ATOM 1824 C CA . ASP A 1 229 ? 56.348 28.489 29.011 1.00 7.74 ? 229 ASP A CA 1 ATOM 1825 C C . ASP A 1 229 ? 57.359 27.651 29.795 1.00 7.02 ? 229 ASP A C 1 ATOM 1826 O O . ASP A 1 229 ? 58.263 28.266 30.418 1.00 8.66 ? 229 ASP A O 1 ATOM 1827 C CB . ASP A 1 229 ? 57.107 29.286 27.924 1.00 7.70 ? 229 ASP A CB 1 ATOM 1828 C CG . ASP A 1 229 ? 56.155 30.088 27.028 1.00 7.33 ? 229 ASP A CG 1 ATOM 1829 O OD1 . ASP A 1 229 ? 55.794 31.224 27.404 1.00 8.82 ? 229 ASP A OD1 1 ATOM 1830 O OD2 . ASP A 1 229 ? 55.765 29.533 25.953 1.00 9.91 ? 229 ASP A OD2 1 ATOM 1831 N N . ILE A 1 230 ? 57.224 26.345 29.746 1.00 7.90 ? 230 ILE A N 1 ATOM 1832 C CA . ILE A 1 230 ? 58.081 25.414 30.492 1.00 8.55 ? 230 ILE A CA 1 ATOM 1833 C C . ILE A 1 230 ? 58.522 24.278 29.591 1.00 7.77 ? 230 ILE A C 1 ATOM 1834 O O . ILE A 1 230 ? 58.030 24.093 28.487 1.00 9.12 ? 230 ILE A O 1 ATOM 1835 C CB . ILE A 1 230 ? 57.428 24.870 31.766 1.00 9.38 ? 230 ILE A CB 1 ATOM 1836 C CG1 . ILE A 1 230 ? 56.251 23.978 31.447 1.00 10.96 ? 230 ILE A CG1 1 ATOM 1837 C CG2 . ILE A 1 230 ? 57.019 26.033 32.652 1.00 10.14 ? 230 ILE A CG2 1 ATOM 1838 C CD1 . ILE A 1 230 ? 55.802 23.029 32.548 1.00 14.66 ? 230 ILE A CD1 1 ATOM 1839 N N . ALA A 1 231 ? 59.556 23.602 30.051 1.00 8.54 ? 231 ALA A N 1 ATOM 1840 C CA . ALA A 1 231 ? 59.959 22.382 29.450 1.00 8.63 ? 231 ALA A CA 1 ATOM 1841 C C . ALA A 1 231 ? 59.919 21.276 30.519 1.00 9.59 ? 231 ALA A C 1 ATOM 1842 O O . ALA A 1 231 ? 60.207 21.520 31.716 1.00 10.36 ? 231 ALA A O 1 ATOM 1843 C CB . ALA A 1 231 ? 61.355 22.514 28.873 1.00 10.39 ? 231 ALA A CB 1 ATOM 1844 N N . ILE A 1 232 ? 59.671 20.043 30.056 1.00 10.37 ? 232 ILE A N 1 ATOM 1845 C CA . ILE A 1 232 ? 59.740 18.888 30.899 1.00 9.74 ? 232 ILE A CA 1 ATOM 1846 C C . ILE A 1 232 ? 60.717 17.946 30.198 1.00 9.75 ? 232 ILE A C 1 ATOM 1847 O O . ILE A 1 232 ? 60.451 17.447 29.128 1.00 11.62 ? 232 ILE A O 1 ATOM 1848 C CB . ILE A 1 232 ? 58.349 18.210 31.114 1.00 11.09 ? 232 ILE A CB 1 ATOM 1849 C CG1 . ILE A 1 232 ? 57.252 19.254 31.564 1.00 11.69 ? 232 ILE A CG1 1 ATOM 1850 C CG2 . ILE A 1 232 ? 58.493 17.061 32.120 1.00 10.52 ? 232 ILE A CG2 1 ATOM 1851 C CD1 . ILE A 1 232 ? 55.879 18.719 31.748 1.00 12.63 ? 232 ILE A CD1 1 ATOM 1852 N N . GLN A 1 233 ? 61.895 17.761 30.813 1.00 10.76 ? 233 GLN A N 1 ATOM 1853 C CA . GLN A 1 233 ? 63.026 17.130 30.162 1.00 10.49 ? 233 GLN A CA 1 ATOM 1854 C C . GLN A 1 233 ? 63.730 16.160 31.071 1.00 11.49 ? 233 GLN A C 1 ATOM 1855 O O . GLN A 1 233 ? 63.633 16.266 32.265 1.00 14.67 ? 233 GLN A O 1 ATOM 1856 C CB . GLN A 1 233 ? 64.034 18.192 29.699 1.00 14.06 ? 233 GLN A CB 1 ATOM 1857 C CG . GLN A 1 233 ? 63.451 19.162 28.681 1.00 12.14 ? 233 GLN A CG 1 ATOM 1858 C CD . GLN A 1 233 ? 64.394 20.336 28.385 1.00 12.10 ? 233 GLN A CD 1 ATOM 1859 O OE1 . GLN A 1 233 ? 64.891 20.993 29.263 1.00 16.91 ? 233 GLN A OE1 1 ATOM 1860 N NE2 . GLN A 1 233 ? 64.546 20.632 27.137 1.00 15.36 ? 233 GLN A NE2 1 ATOM 1861 O OXT . GLN A 1 233 ? 64.492 15.305 30.573 1.00 16.19 ? 233 GLN A OXT 1 HETATM 1862 CU CU . CU B 2 . ? 41.075 42.529 41.218 1.00 10.62 2 301 CU A CU 1 HETATM 1863 C C1 . NAG C 3 . ? 64.254 18.467 22.304 1.00 10.79 ? 302 NAG A C1 1 HETATM 1864 C C2 . NAG C 3 . ? 64.234 16.945 22.518 1.00 10.29 ? 302 NAG A C2 1 HETATM 1865 C C3 . NAG C 3 . ? 65.596 16.363 22.231 1.00 11.98 ? 302 NAG A C3 1 HETATM 1866 C C4 . NAG C 3 . ? 66.092 16.857 20.903 1.00 12.97 ? 302 NAG A C4 1 HETATM 1867 C C5 . NAG C 3 . ? 66.086 18.403 20.763 1.00 14.24 ? 302 NAG A C5 1 HETATM 1868 C C6 . NAG C 3 . ? 66.467 18.841 19.331 1.00 14.45 ? 302 NAG A C6 1 HETATM 1869 C C7 . NAG C 3 . ? 62.474 16.223 24.203 1.00 10.87 ? 302 NAG A C7 1 HETATM 1870 C C8 . NAG C 3 . ? 61.780 15.714 23.085 1.00 7.63 ? 302 NAG A C8 1 HETATM 1871 N N2 . NAG C 3 . ? 63.663 16.755 23.839 1.00 9.90 ? 302 NAG A N2 1 HETATM 1872 O O3 . NAG C 3 . ? 65.418 14.964 22.239 1.00 14.56 ? 302 NAG A O3 1 HETATM 1873 O O4 . NAG C 3 . ? 67.412 16.375 20.701 1.00 15.61 ? 302 NAG A O4 1 HETATM 1874 O O5 . NAG C 3 . ? 64.758 18.839 21.036 1.00 14.00 ? 302 NAG A O5 1 HETATM 1875 O O6 . NAG C 3 . ? 65.499 18.317 18.381 1.00 15.85 ? 302 NAG A O6 1 HETATM 1876 O O7 . NAG C 3 . ? 62.010 16.153 25.475 1.00 18.15 ? 302 NAG A O7 1 HETATM 1877 ZN ZN . ZN D 4 . ? 38.284 25.555 32.458 0.85 10.64 ? 303 ZN A ZN 1 HETATM 1878 ZN ZN . ZN E 4 . ? 59.160 46.318 37.406 0.60 16.69 ? 304 ZN A ZN 1 HETATM 1879 ZN ZN . ZN F 4 . ? 30.951 23.499 35.742 0.95 15.46 ? 305 ZN A ZN 1 HETATM 1880 ZN ZN . ZN G 4 . ? 45.927 16.242 55.792 0.80 25.66 ? 306 ZN A ZN 1 HETATM 1881 C C1 . IPA H 5 . ? 34.087 39.479 27.910 1.00 33.66 ? 307 IPA A C1 1 HETATM 1882 C C2 . IPA H 5 . ? 33.834 38.116 28.527 1.00 36.70 ? 307 IPA A C2 1 HETATM 1883 C C3 . IPA H 5 . ? 32.431 38.065 29.093 1.00 39.20 ? 307 IPA A C3 1 HETATM 1884 O O2 . IPA H 5 . ? 34.001 37.033 27.580 1.00 38.56 ? 307 IPA A O2 1 HETATM 1885 C C1 . GOL I 6 . ? 64.565 20.407 38.970 1.00 46.44 ? 308 GOL A C1 1 HETATM 1886 O O1 . GOL I 6 . ? 64.397 19.817 37.659 1.00 45.78 ? 308 GOL A O1 1 HETATM 1887 C C2 . GOL I 6 . ? 64.499 21.939 38.986 1.00 47.69 ? 308 GOL A C2 1 HETATM 1888 O O2 . GOL I 6 . ? 63.664 22.513 40.008 1.00 47.58 ? 308 GOL A O2 1 HETATM 1889 C C3 . GOL I 6 . ? 63.980 22.409 37.640 1.00 41.99 ? 308 GOL A C3 1 HETATM 1890 O O3 . GOL I 6 . ? 63.708 23.811 37.676 1.00 34.59 ? 308 GOL A O3 1 HETATM 1891 C C1 . GOL J 6 . ? 41.174 30.444 11.445 1.00 27.92 ? 309 GOL A C1 1 HETATM 1892 O O1 . GOL J 6 . ? 41.677 29.176 10.915 1.00 38.62 ? 309 GOL A O1 1 HETATM 1893 C C2 . GOL J 6 . ? 42.060 31.521 10.858 1.00 32.80 ? 309 GOL A C2 1 HETATM 1894 O O2 . GOL J 6 . ? 41.241 32.492 10.114 1.00 33.12 ? 309 GOL A O2 1 HETATM 1895 C C3 . GOL J 6 . ? 42.807 32.155 12.041 1.00 31.64 ? 309 GOL A C3 1 HETATM 1896 O O3 . GOL J 6 . ? 43.952 32.924 11.579 1.00 33.68 ? 309 GOL A O3 1 HETATM 1897 C C1 . IPA K 5 . ? 42.403 45.842 32.436 1.00 39.93 ? 310 IPA A C1 1 HETATM 1898 C C2 . IPA K 5 . ? 41.569 47.082 32.803 1.00 40.11 ? 310 IPA A C2 1 HETATM 1899 C C3 . IPA K 5 . ? 41.312 47.211 34.305 1.00 38.92 ? 310 IPA A C3 1 HETATM 1900 O O2 . IPA K 5 . ? 42.221 48.303 32.362 1.00 37.78 ? 310 IPA A O2 1 HETATM 1901 C C1 . GOL L 6 . ? 54.200 15.727 24.119 1.00 40.62 ? 311 GOL A C1 1 HETATM 1902 O O1 . GOL L 6 . ? 54.320 14.276 24.120 1.00 43.49 ? 311 GOL A O1 1 HETATM 1903 C C2 . GOL L 6 . ? 52.729 15.911 24.376 1.00 35.39 ? 311 GOL A C2 1 HETATM 1904 O O2 . GOL L 6 . ? 52.446 14.814 25.226 1.00 47.06 ? 311 GOL A O2 1 HETATM 1905 C C3 . GOL L 6 . ? 52.209 17.164 25.065 1.00 31.86 ? 311 GOL A C3 1 HETATM 1906 O O3 . GOL L 6 . ? 53.158 18.194 25.311 1.00 22.59 ? 311 GOL A O3 1 HETATM 1907 C C1 . GOL M 6 . ? 30.499 36.886 53.438 1.00 34.50 ? 312 GOL A C1 1 HETATM 1908 O O1 . GOL M 6 . ? 30.431 36.040 52.235 1.00 33.06 ? 312 GOL A O1 1 HETATM 1909 C C2 . GOL M 6 . ? 31.937 36.694 53.835 1.00 33.86 ? 312 GOL A C2 1 HETATM 1910 O O2 . GOL M 6 . ? 32.651 36.381 52.611 1.00 36.88 ? 312 GOL A O2 1 HETATM 1911 C C3 . GOL M 6 . ? 32.498 37.876 54.621 1.00 34.02 ? 312 GOL A C3 1 HETATM 1912 O O3 . GOL M 6 . ? 33.554 37.272 55.381 1.00 42.72 ? 312 GOL A O3 1 HETATM 1913 C C . ACT N 7 . ? 40.590 26.690 54.122 1.00 47.91 ? 313 ACT A C 1 HETATM 1914 O O . ACT N 7 . ? 40.683 27.793 53.558 1.00 46.02 ? 313 ACT A O 1 HETATM 1915 O OXT . ACT N 7 . ? 40.606 25.546 53.527 1.00 33.66 ? 313 ACT A OXT 1 HETATM 1916 C CH3 . ACT N 7 . ? 40.439 26.862 55.608 1.00 51.36 ? 313 ACT A CH3 1 HETATM 1917 C C1 . GOL O 6 . ? 34.816 24.550 54.664 1.00 28.56 ? 314 GOL A C1 1 HETATM 1918 O O1 . GOL O 6 . ? 33.827 25.475 54.183 1.00 23.58 ? 314 GOL A O1 1 HETATM 1919 C C2 . GOL O 6 . ? 36.026 25.403 55.120 1.00 29.92 ? 314 GOL A C2 1 HETATM 1920 O O2 . GOL O 6 . ? 35.649 26.438 56.116 1.00 34.93 ? 314 GOL A O2 1 HETATM 1921 C C3 . GOL O 6 . ? 37.035 24.454 55.712 1.00 34.86 ? 314 GOL A C3 1 HETATM 1922 O O3 . GOL O 6 . ? 37.971 25.227 56.508 1.00 41.00 ? 314 GOL A O3 1 HETATM 1923 C C1 . GOL P 6 . ? 44.608 25.201 52.202 1.00 26.95 ? 315 GOL A C1 1 HETATM 1924 O O1 . GOL P 6 . ? 43.471 24.632 51.595 1.00 24.53 ? 315 GOL A O1 1 HETATM 1925 C C2 . GOL P 6 . ? 44.600 26.787 52.146 1.00 25.53 ? 315 GOL A C2 1 HETATM 1926 O O2 . GOL P 6 . ? 45.162 27.161 50.877 1.00 15.40 ? 315 GOL A O2 1 HETATM 1927 C C3 . GOL P 6 . ? 45.397 27.621 53.202 1.00 23.65 ? 315 GOL A C3 1 HETATM 1928 O O3 . GOL P 6 . ? 46.742 27.051 53.121 1.00 31.74 ? 315 GOL A O3 1 HETATM 1929 C C1 . GOL Q 6 . ? 37.795 41.628 29.567 1.00 39.01 ? 316 GOL A C1 1 HETATM 1930 O O1 . GOL Q 6 . ? 37.410 40.341 29.924 1.00 31.56 ? 316 GOL A O1 1 HETATM 1931 C C2 . GOL Q 6 . ? 38.142 41.442 28.112 1.00 42.27 ? 316 GOL A C2 1 HETATM 1932 O O2 . GOL Q 6 . ? 38.679 42.730 27.779 1.00 48.75 ? 316 GOL A O2 1 HETATM 1933 C C3 . GOL Q 6 . ? 39.126 40.241 27.881 1.00 37.03 ? 316 GOL A C3 1 HETATM 1934 O O3 . GOL Q 6 . ? 38.511 38.896 27.884 1.00 29.64 ? 316 GOL A O3 1 HETATM 1935 C C . ACT R 7 . ? 64.537 17.300 39.882 1.00 47.14 ? 317 ACT A C 1 HETATM 1936 O O . ACT R 7 . ? 64.748 17.963 40.930 1.00 53.76 ? 317 ACT A O 1 HETATM 1937 O OXT . ACT R 7 . ? 64.924 17.708 38.768 1.00 49.31 ? 317 ACT A OXT 1 HETATM 1938 C CH3 . ACT R 7 . ? 63.784 16.006 39.922 1.00 43.01 ? 317 ACT A CH3 1 HETATM 1939 O O . HOH S 8 . ? 37.930 32.940 49.593 1.00 11.83 ? 401 HOH A O 1 HETATM 1940 O O . HOH S 8 . ? 37.672 30.299 48.580 1.00 13.72 ? 402 HOH A O 1 HETATM 1941 O O . HOH S 8 . ? 43.886 45.783 42.962 1.00 19.18 ? 403 HOH A O 1 HETATM 1942 O O . HOH S 8 . ? 59.582 44.433 38.617 1.00 20.15 ? 404 HOH A O 1 HETATM 1943 O O . HOH S 8 . ? 58.557 41.349 38.400 1.00 21.70 ? 405 HOH A O 1 HETATM 1944 O O . HOH S 8 . ? 56.147 41.488 37.059 1.00 18.67 ? 406 HOH A O 1 HETATM 1945 O O . HOH S 8 . ? 54.146 48.661 36.426 1.00 23.63 ? 407 HOH A O 1 HETATM 1946 O O . HOH S 8 . ? 50.441 29.185 43.740 1.00 8.72 ? 408 HOH A O 1 HETATM 1947 O O . HOH S 8 . ? 44.230 24.683 48.843 1.00 10.74 ? 409 HOH A O 1 HETATM 1948 O O . HOH S 8 . ? 46.800 23.665 49.465 1.00 14.54 ? 410 HOH A O 1 HETATM 1949 O O . HOH S 8 . ? 42.554 22.617 48.088 1.00 9.70 ? 411 HOH A O 1 HETATM 1950 O O . HOH S 8 . ? 39.047 23.808 47.509 1.00 12.01 ? 412 HOH A O 1 HETATM 1951 O O . HOH S 8 . ? 36.294 23.979 47.921 1.00 11.48 ? 413 HOH A O 1 HETATM 1952 O O . HOH S 8 . ? 31.455 26.519 54.128 1.00 16.13 ? 414 HOH A O 1 HETATM 1953 O O . HOH S 8 . ? 38.772 21.798 54.406 1.00 18.25 ? 415 HOH A O 1 HETATM 1954 O O . HOH S 8 . ? 48.025 28.505 54.556 1.00 23.08 ? 416 HOH A O 1 HETATM 1955 O O . HOH S 8 . ? 46.102 29.565 56.356 1.00 23.81 ? 417 HOH A O 1 HETATM 1956 O O . HOH S 8 . ? 52.023 28.807 51.326 1.00 27.88 ? 418 HOH A O 1 HETATM 1957 O O . HOH S 8 . ? 50.814 36.448 51.252 1.00 11.22 ? 419 HOH A O 1 HETATM 1958 O O . HOH S 8 . ? 49.234 34.034 50.171 1.00 10.01 ? 420 HOH A O 1 HETATM 1959 O O . HOH S 8 . ? 58.581 35.688 44.889 1.00 26.54 ? 421 HOH A O 1 HETATM 1960 O O . HOH S 8 . ? 42.374 38.135 30.602 1.00 10.13 ? 422 HOH A O 1 HETATM 1961 O O . HOH S 8 . ? 43.753 37.087 32.719 1.00 18.94 ? 423 HOH A O 1 HETATM 1962 O O . HOH S 8 . ? 47.868 37.164 33.618 1.00 12.34 ? 424 HOH A O 1 HETATM 1963 O O . HOH S 8 . ? 46.060 38.025 35.309 1.00 19.83 ? 425 HOH A O 1 HETATM 1964 O O . HOH S 8 . ? 50.286 35.028 30.742 1.00 8.59 ? 426 HOH A O 1 HETATM 1965 O O . HOH S 8 . ? 50.004 23.051 28.068 1.00 11.02 ? 427 HOH A O 1 HETATM 1966 O O . HOH S 8 . ? 52.000 19.299 27.372 1.00 11.90 ? 428 HOH A O 1 HETATM 1967 O O . HOH S 8 . ? 45.212 17.730 28.598 1.00 12.36 ? 429 HOH A O 1 HETATM 1968 O O . HOH S 8 . ? 48.635 17.655 32.748 1.00 15.20 ? 430 HOH A O 1 HETATM 1969 O O . HOH S 8 . ? 49.349 16.531 38.871 1.00 13.80 ? 431 HOH A O 1 HETATM 1970 O O . HOH S 8 . ? 49.563 18.314 40.950 1.00 10.92 ? 432 HOH A O 1 HETATM 1971 O O . HOH S 8 . ? 45.107 22.693 40.997 1.00 13.39 ? 433 HOH A O 1 HETATM 1972 O O . HOH S 8 . ? 38.549 29.115 52.411 1.00 19.94 ? 434 HOH A O 1 HETATM 1973 O O . HOH S 8 . ? 39.332 30.481 56.044 1.00 21.15 ? 435 HOH A O 1 HETATM 1974 O O . HOH S 8 . ? 59.751 16.021 43.001 1.00 19.68 ? 436 HOH A O 1 HETATM 1975 O O . HOH S 8 . ? 60.323 24.060 42.059 1.00 16.72 ? 437 HOH A O 1 HETATM 1976 O O . HOH S 8 . ? 59.136 26.242 40.133 1.00 14.24 ? 438 HOH A O 1 HETATM 1977 O O . HOH S 8 . ? 60.971 31.392 36.345 1.00 20.56 ? 439 HOH A O 1 HETATM 1978 O O . HOH S 8 . ? 61.387 36.637 35.455 1.00 20.16 ? 440 HOH A O 1 HETATM 1979 O O . HOH S 8 . ? 60.939 40.244 30.212 1.00 20.17 ? 441 HOH A O 1 HETATM 1980 O O . HOH S 8 . ? 61.384 38.736 28.083 1.00 23.81 ? 442 HOH A O 1 HETATM 1981 O O . HOH S 8 . ? 56.533 32.157 30.503 1.00 10.03 ? 443 HOH A O 1 HETATM 1982 O O . HOH S 8 . ? 57.508 33.175 28.040 1.00 11.54 ? 444 HOH A O 1 HETATM 1983 O O . HOH S 8 . ? 60.167 32.672 27.664 1.00 23.88 ? 445 HOH A O 1 HETATM 1984 O O . HOH S 8 . ? 37.461 31.649 23.799 1.00 14.59 ? 446 HOH A O 1 HETATM 1985 O O . HOH S 8 . ? 35.215 31.034 24.925 1.00 13.61 ? 447 HOH A O 1 HETATM 1986 O O . HOH S 8 . ? 39.828 20.625 23.408 1.00 23.58 ? 448 HOH A O 1 HETATM 1987 O O . HOH S 8 . ? 32.948 26.994 29.352 1.00 26.90 ? 449 HOH A O 1 HETATM 1988 O O . HOH S 8 . ? 35.691 27.859 29.988 1.00 14.56 ? 450 HOH A O 1 HETATM 1989 O O . HOH S 8 . ? 36.512 26.138 31.789 1.00 17.35 ? 451 HOH A O 1 HETATM 1990 O O . HOH S 8 . ? 35.497 29.304 33.880 1.00 12.01 ? 452 HOH A O 1 HETATM 1991 O O . HOH S 8 . ? 33.259 29.961 35.814 1.00 11.46 ? 453 HOH A O 1 HETATM 1992 O O . HOH S 8 . ? 35.997 23.365 29.896 1.00 26.60 ? 454 HOH A O 1 HETATM 1993 O O . HOH S 8 . ? 36.401 21.156 35.621 1.00 23.42 ? 455 HOH A O 1 HETATM 1994 O O . HOH S 8 . ? 38.565 22.943 36.319 1.00 16.59 ? 456 HOH A O 1 HETATM 1995 O O . HOH S 8 . ? 33.669 23.440 39.215 1.00 15.40 ? 457 HOH A O 1 HETATM 1996 O O . HOH S 8 . ? 29.803 23.606 33.942 1.00 14.36 ? 458 HOH A O 1 HETATM 1997 O O . HOH S 8 . ? 48.611 45.997 30.311 1.00 22.53 ? 459 HOH A O 1 HETATM 1998 O O . HOH S 8 . ? 42.097 42.927 31.190 1.00 16.64 ? 460 HOH A O 1 HETATM 1999 O O . HOH S 8 . ? 56.129 42.508 23.054 1.00 20.11 ? 461 HOH A O 1 HETATM 2000 O O . HOH S 8 . ? 54.280 38.138 17.696 1.00 21.09 ? 462 HOH A O 1 HETATM 2001 O O . HOH S 8 . ? 47.230 35.104 13.078 1.00 23.93 ? 463 HOH A O 1 HETATM 2002 O O . HOH S 8 . ? 50.708 39.307 21.555 1.00 22.92 ? 464 HOH A O 1 HETATM 2003 O O . HOH S 8 . ? 49.088 41.733 21.911 1.00 23.46 ? 465 HOH A O 1 HETATM 2004 O O . HOH S 8 . ? 43.324 39.577 20.820 1.00 22.67 ? 466 HOH A O 1 HETATM 2005 O O . HOH S 8 . ? 41.418 35.563 19.776 1.00 16.36 ? 467 HOH A O 1 HETATM 2006 O O . HOH S 8 . ? 41.265 28.315 13.154 1.00 21.17 ? 468 HOH A O 1 HETATM 2007 O O . HOH S 8 . ? 39.246 28.552 15.014 1.00 13.64 ? 469 HOH A O 1 HETATM 2008 O O . HOH S 8 . ? 44.660 34.454 13.753 1.00 23.10 ? 470 HOH A O 1 HETATM 2009 O O . HOH S 8 . ? 37.807 45.747 37.257 1.00 18.31 ? 471 HOH A O 1 HETATM 2010 O O . HOH S 8 . ? 57.868 29.567 20.637 1.00 20.16 ? 472 HOH A O 1 HETATM 2011 O O . HOH S 8 . ? 59.934 28.746 19.761 1.00 12.70 ? 473 HOH A O 1 HETATM 2012 O O . HOH S 8 . ? 59.637 26.503 20.822 1.00 25.06 ? 474 HOH A O 1 HETATM 2013 O O . HOH S 8 . ? 62.116 28.011 20.437 1.00 26.65 ? 475 HOH A O 1 HETATM 2014 O O . HOH S 8 . ? 63.344 23.954 25.668 1.00 28.87 ? 476 HOH A O 1 HETATM 2015 O O . HOH S 8 . ? 62.632 26.462 24.870 1.00 34.17 ? 477 HOH A O 1 HETATM 2016 O O . HOH S 8 . ? 46.711 43.420 53.567 1.00 30.83 ? 478 HOH A O 1 HETATM 2017 O O . HOH S 8 . ? 44.154 40.718 51.704 1.00 19.76 ? 479 HOH A O 1 HETATM 2018 O O . HOH S 8 . ? 45.433 42.968 51.283 1.00 32.27 ? 480 HOH A O 1 HETATM 2019 O O . HOH S 8 . ? 44.660 38.793 54.338 1.00 29.36 ? 481 HOH A O 1 HETATM 2020 O O . HOH S 8 . ? 47.112 37.282 56.767 1.00 26.53 ? 482 HOH A O 1 HETATM 2021 O O . HOH S 8 . ? 42.245 43.579 48.766 1.00 15.91 ? 483 HOH A O 1 HETATM 2022 O O . HOH S 8 . ? 41.842 42.566 51.383 1.00 33.34 ? 484 HOH A O 1 HETATM 2023 O O . HOH S 8 . ? 56.846 35.092 49.867 1.00 21.49 ? 485 HOH A O 1 HETATM 2024 O O . HOH S 8 . ? 55.038 45.225 44.671 1.00 16.22 ? 486 HOH A O 1 HETATM 2025 O O . HOH S 8 . ? 57.772 44.371 44.679 1.00 37.20 ? 487 HOH A O 1 HETATM 2026 O O . HOH S 8 . ? 54.590 48.163 43.587 1.00 26.47 ? 488 HOH A O 1 HETATM 2027 O O . HOH S 8 . ? 53.700 43.439 55.063 1.00 17.90 ? 489 HOH A O 1 HETATM 2028 O O . HOH S 8 . ? 41.092 24.009 35.369 1.00 30.02 ? 490 HOH A O 1 HETATM 2029 O O . HOH S 8 . ? 64.470 14.141 33.889 1.00 18.18 ? 491 HOH A O 1 HETATM 2030 O O . HOH S 8 . ? 64.728 15.088 27.910 1.00 12.66 ? 492 HOH A O 1 HETATM 2031 O O . HOH S 8 . ? 65.165 17.368 26.192 1.00 14.80 ? 493 HOH A O 1 HETATM 2032 O O . HOH S 8 . ? 47.960 15.827 49.213 1.00 23.33 ? 494 HOH A O 1 HETATM 2033 O O . HOH S 8 . ? 45.868 14.101 50.052 1.00 30.20 ? 495 HOH A O 1 HETATM 2034 O O . HOH S 8 . ? 44.629 17.289 51.428 1.00 32.25 ? 496 HOH A O 1 HETATM 2035 O O . HOH S 8 . ? 50.241 22.172 52.707 1.00 34.56 ? 497 HOH A O 1 HETATM 2036 O O . HOH S 8 . ? 62.353 39.372 32.577 1.00 41.41 ? 498 HOH A O 1 HETATM 2037 O O . HOH S 8 . ? 30.432 34.969 40.118 1.00 18.86 ? 499 HOH A O 1 HETATM 2038 O O . HOH S 8 . ? 51.895 23.887 49.658 1.00 22.56 ? 500 HOH A O 1 HETATM 2039 O O . HOH S 8 . ? 54.390 25.309 49.089 1.00 37.80 ? 501 HOH A O 1 HETATM 2040 O O . HOH S 8 . ? 31.859 36.023 42.081 1.00 21.31 ? 502 HOH A O 1 HETATM 2041 O O . HOH S 8 . ? 30.453 40.426 44.661 1.00 17.92 ? 503 HOH A O 1 HETATM 2042 O O . HOH S 8 . ? 60.972 35.104 41.406 1.00 25.70 ? 504 HOH A O 1 HETATM 2043 O O . HOH S 8 . ? 63.600 36.444 36.742 1.00 40.97 ? 505 HOH A O 1 HETATM 2044 O O . HOH S 8 . ? 44.069 16.154 26.339 1.00 37.05 ? 506 HOH A O 1 HETATM 2045 O O . HOH S 8 . ? 41.945 17.946 24.913 1.00 38.61 ? 507 HOH A O 1 HETATM 2046 O O . HOH S 8 . ? 42.974 16.958 22.455 1.00 31.20 ? 508 HOH A O 1 HETATM 2047 O O . HOH S 8 . ? 48.932 22.794 15.594 1.00 28.44 ? 509 HOH A O 1 HETATM 2048 O O . HOH S 8 . ? 50.936 31.376 18.764 1.00 11.77 ? 510 HOH A O 1 HETATM 2049 O O . HOH S 8 . ? 53.922 26.490 16.743 1.00 25.08 ? 511 HOH A O 1 HETATM 2050 O O . HOH S 8 . ? 50.983 27.910 14.206 1.00 38.48 ? 512 HOH A O 1 HETATM 2051 O O . HOH S 8 . ? 54.974 31.006 12.053 1.00 25.56 ? 513 HOH A O 1 HETATM 2052 O O . HOH S 8 . ? 59.494 36.588 17.563 1.00 40.60 ? 514 HOH A O 1 HETATM 2053 O O . HOH S 8 . ? 57.363 42.559 20.360 1.00 33.84 ? 515 HOH A O 1 HETATM 2054 O O . HOH S 8 . ? 57.607 40.757 18.447 1.00 35.72 ? 516 HOH A O 1 HETATM 2055 O O . HOH S 8 . ? 42.816 50.385 44.002 1.00 26.83 ? 517 HOH A O 1 HETATM 2056 O O . HOH S 8 . ? 40.058 47.441 46.606 1.00 39.00 ? 518 HOH A O 1 HETATM 2057 O O . HOH S 8 . ? 44.567 50.264 50.616 1.00 39.75 ? 519 HOH A O 1 HETATM 2058 O O . HOH S 8 . ? 34.121 24.068 25.237 1.00 33.94 ? 520 HOH A O 1 HETATM 2059 O O . HOH S 8 . ? 29.863 33.616 32.501 1.00 12.73 ? 521 HOH A O 1 HETATM 2060 O O . HOH S 8 . ? 28.768 30.908 32.600 1.00 29.69 ? 522 HOH A O 1 HETATM 2061 O O . HOH S 8 . ? 30.630 34.617 30.134 1.00 28.14 ? 523 HOH A O 1 HETATM 2062 O O . HOH S 8 . ? 29.611 29.903 38.136 1.00 19.54 ? 524 HOH A O 1 HETATM 2063 O O . HOH S 8 . ? 38.121 18.917 36.026 1.00 28.90 ? 525 HOH A O 1 HETATM 2064 O O . HOH S 8 . ? 50.790 15.554 22.222 1.00 24.96 ? 526 HOH A O 1 HETATM 2065 O O . HOH S 8 . ? 56.648 14.907 23.642 1.00 28.84 ? 527 HOH A O 1 HETATM 2066 O O . HOH S 8 . ? 59.269 18.187 22.544 1.00 23.93 ? 528 HOH A O 1 HETATM 2067 O O . HOH S 8 . ? 61.443 20.037 20.238 1.00 21.37 ? 529 HOH A O 1 HETATM 2068 O O . HOH S 8 . ? 64.893 19.104 33.339 1.00 28.00 ? 530 HOH A O 1 HETATM 2069 O O . HOH S 8 . ? 66.049 14.271 36.236 1.00 29.26 ? 531 HOH A O 1 HETATM 2070 O O . HOH S 8 . ? 44.841 13.730 43.522 1.00 22.16 ? 532 HOH A O 1 HETATM 2071 O O . HOH S 8 . ? 48.415 15.397 36.503 1.00 37.83 ? 533 HOH A O 1 HETATM 2072 O O . HOH S 8 . ? 46.899 16.377 34.812 1.00 31.27 ? 534 HOH A O 1 HETATM 2073 O O . HOH S 8 . ? 51.507 11.703 33.445 1.00 21.20 ? 535 HOH A O 1 HETATM 2074 O O . HOH S 8 . ? 52.072 13.178 37.333 1.00 24.60 ? 536 HOH A O 1 HETATM 2075 O O . HOH S 8 . ? 41.784 23.675 17.797 1.00 36.70 ? 537 HOH A O 1 HETATM 2076 O O . HOH S 8 . ? 55.949 16.448 48.874 1.00 30.56 ? 538 HOH A O 1 HETATM 2077 O O . HOH S 8 . ? 48.798 50.490 37.544 1.00 25.34 ? 539 HOH A O 1 HETATM 2078 O O . HOH S 8 . ? 48.335 51.126 34.153 1.00 28.72 ? 540 HOH A O 1 HETATM 2079 O O . HOH S 8 . ? 51.660 51.870 29.827 1.00 36.78 ? 541 HOH A O 1 HETATM 2080 O O . HOH S 8 . ? 52.802 48.728 25.755 1.00 37.68 ? 542 HOH A O 1 HETATM 2081 O O . HOH S 8 . ? 55.598 49.360 24.852 1.00 35.70 ? 543 HOH A O 1 HETATM 2082 O O . HOH S 8 . ? 50.260 27.569 50.789 1.00 30.10 ? 544 HOH A O 1 HETATM 2083 O O . HOH S 8 . ? 47.087 24.266 53.065 1.00 41.31 ? 545 HOH A O 1 HETATM 2084 O O . HOH S 8 . ? 27.009 24.712 42.267 1.00 19.66 ? 546 HOH A O 1 HETATM 2085 O O . HOH S 8 . ? 28.548 22.548 53.676 1.00 28.44 ? 547 HOH A O 1 HETATM 2086 O O . HOH S 8 . ? 29.333 23.631 55.834 1.00 42.44 ? 548 HOH A O 1 HETATM 2087 O O . HOH S 8 . ? 26.601 20.477 54.314 1.00 29.81 ? 549 HOH A O 1 HETATM 2088 O O . HOH S 8 . ? 50.017 49.711 49.341 1.00 27.24 ? 550 HOH A O 1 HETATM 2089 O O . HOH S 8 . ? 50.160 52.418 47.931 1.00 42.50 ? 551 HOH A O 1 HETATM 2090 O O . HOH S 8 . ? 26.617 32.365 40.615 1.00 39.86 ? 552 HOH A O 1 HETATM 2091 O O . HOH S 8 . ? 32.742 20.076 34.418 1.00 32.38 ? 553 HOH A O 1 HETATM 2092 O O . HOH S 8 . ? 45.292 15.418 30.178 1.00 29.38 ? 554 HOH A O 1 HETATM 2093 O O . HOH S 8 . ? 48.045 12.506 27.168 1.00 41.68 ? 555 HOH A O 1 HETATM 2094 O O . HOH S 8 . ? 51.010 10.830 31.618 1.00 43.43 ? 556 HOH A O 1 HETATM 2095 O O . HOH S 8 . ? 61.089 21.166 42.317 1.00 33.83 ? 557 HOH A O 1 HETATM 2096 O O . HOH S 8 . ? 44.120 12.292 47.996 1.00 32.26 ? 558 HOH A O 1 HETATM 2097 O O . HOH S 8 . ? 44.925 11.635 45.375 1.00 45.02 ? 559 HOH A O 1 HETATM 2098 O O . HOH S 8 . ? 60.400 39.456 42.814 1.00 31.08 ? 560 HOH A O 1 HETATM 2099 O O . HOH S 8 . ? 33.315 23.593 30.769 1.00 40.68 ? 561 HOH A O 1 HETATM 2100 O O . HOH S 8 . ? 38.011 19.047 29.279 1.00 30.93 ? 562 HOH A O 1 HETATM 2101 O O . HOH S 8 . ? 65.494 25.530 34.220 1.00 25.66 ? 563 HOH A O 1 HETATM 2102 O O . HOH S 8 . ? 64.857 24.430 28.468 1.00 41.92 ? 564 HOH A O 1 HETATM 2103 O O . HOH S 8 . ? 65.066 26.278 30.254 1.00 43.92 ? 565 HOH A O 1 HETATM 2104 O O . HOH S 8 . ? 66.974 18.504 34.092 1.00 41.45 ? 566 HOH A O 1 HETATM 2105 O O . HOH S 8 . ? 40.455 17.029 52.996 1.00 33.69 ? 567 HOH A O 1 HETATM 2106 O O . HOH S 8 . ? 49.360 32.506 61.713 1.00 41.72 ? 568 HOH A O 1 HETATM 2107 O O . HOH S 8 . ? 52.465 30.701 56.869 1.00 36.53 ? 569 HOH A O 1 HETATM 2108 O O . HOH S 8 . ? 55.449 33.643 54.142 1.00 30.57 ? 570 HOH A O 1 HETATM 2109 O O . HOH S 8 . ? 57.391 44.745 53.037 1.00 37.06 ? 571 HOH A O 1 HETATM 2110 O O . HOH S 8 . ? 57.681 19.813 21.334 1.00 45.11 ? 572 HOH A O 1 HETATM 2111 O O . HOH S 8 . ? 57.425 14.228 21.456 1.00 39.95 ? 573 HOH A O 1 HETATM 2112 O O . HOH S 8 . ? 35.709 27.491 58.652 1.00 40.58 ? 574 HOH A O 1 HETATM 2113 O O . HOH S 8 . ? 25.489 22.700 49.439 1.00 30.61 ? 575 HOH A O 1 HETATM 2114 O O . HOH S 8 . ? 58.780 33.919 47.485 1.00 31.89 ? 576 HOH A O 1 HETATM 2115 O O . HOH S 8 . ? 43.492 50.555 38.435 1.00 39.71 ? 577 HOH A O 1 HETATM 2116 O O B HOH S 8 . ? 47.187 14.952 55.124 0.50 19.53 ? 578 HOH A O 1 HETATM 2117 O O . HOH S 8 . ? 43.830 15.819 55.334 1.00 15.79 ? 579 HOH A O 1 HETATM 2118 O O . HOH S 8 . ? 56.909 32.449 12.543 1.00 34.40 ? 580 HOH A O 1 HETATM 2119 O O . HOH S 8 . ? 50.324 24.878 51.455 1.00 35.75 ? 581 HOH A O 1 HETATM 2120 O O . HOH S 8 . ? 35.951 31.516 57.568 1.00 34.96 ? 582 HOH A O 1 HETATM 2121 O O . HOH S 8 . ? 36.716 31.881 59.759 1.00 38.70 ? 583 HOH A O 1 HETATM 2122 O O . HOH S 8 . ? 62.129 33.720 28.505 1.00 40.54 ? 584 HOH A O 1 HETATM 2123 O O . HOH S 8 . ? 30.343 39.259 42.521 1.00 42.73 ? 585 HOH A O 1 HETATM 2124 O O . HOH S 8 . ? 42.866 50.997 28.903 1.00 41.08 ? 586 HOH A O 1 HETATM 2125 O O . HOH S 8 . ? 45.233 49.727 25.883 1.00 35.34 ? 587 HOH A O 1 HETATM 2126 O O . HOH S 8 . ? 41.851 46.804 25.159 1.00 42.22 ? 588 HOH A O 1 HETATM 2127 O O . HOH S 8 . ? 48.014 15.911 18.889 1.00 40.27 ? 589 HOH A O 1 HETATM 2128 O O . HOH S 8 . ? 39.361 47.921 38.900 1.00 32.70 ? 590 HOH A O 1 HETATM 2129 O O . HOH S 8 . ? 37.741 44.500 40.924 1.00 38.49 ? 591 HOH A O 1 HETATM 2130 O O . HOH S 8 . ? 39.108 45.417 42.204 1.00 30.28 ? 592 HOH A O 1 HETATM 2131 O O . HOH S 8 . ? 41.861 47.962 41.477 1.00 40.42 ? 593 HOH A O 1 HETATM 2132 O O . HOH S 8 . ? 39.060 43.705 47.532 1.00 45.23 ? 594 HOH A O 1 HETATM 2133 O O . HOH S 8 . ? 59.301 47.190 33.869 1.00 35.16 ? 595 HOH A O 1 HETATM 2134 O O . HOH S 8 . ? 38.908 42.860 24.885 1.00 37.66 ? 596 HOH A O 1 HETATM 2135 O O . HOH S 8 . ? 46.189 51.290 37.915 1.00 35.85 ? 597 HOH A O 1 HETATM 2136 O O . HOH S 8 . ? 36.938 41.541 52.709 1.00 35.73 ? 598 HOH A O 1 HETATM 2137 O O . HOH S 8 . ? 62.231 22.988 21.058 1.00 40.12 ? 599 HOH A O 1 HETATM 2138 O O . HOH S 8 . ? 61.482 26.114 22.526 1.00 34.10 ? 600 HOH A O 1 HETATM 2139 O O . HOH S 8 . ? 59.634 31.143 18.271 1.00 45.96 ? 601 HOH A O 1 HETATM 2140 O O . HOH S 8 . ? 63.989 13.534 38.046 1.00 27.59 ? 602 HOH A O 1 HETATM 2141 O O . HOH S 8 . ? 38.141 25.802 34.680 1.00 10.31 ? 603 HOH A O 1 HETATM 2142 O O . HOH S 8 . ? 39.906 44.179 32.005 1.00 32.59 ? 604 HOH A O 1 HETATM 2143 O O . HOH S 8 . ? 57.337 37.746 52.865 1.00 25.67 ? 605 HOH A O 1 HETATM 2144 O O A HOH S 8 . ? 36.186 37.961 26.247 1.00 27.60 ? 606 HOH A O 1 HETATM 2145 O O . HOH S 8 . ? 31.334 42.281 43.382 1.00 33.57 ? 607 HOH A O 1 HETATM 2146 O O . HOH S 8 . ? 31.845 41.793 40.141 1.00 20.13 ? 608 HOH A O 1 HETATM 2147 O O . HOH S 8 . ? 37.719 34.550 63.220 1.00 42.23 ? 609 HOH A O 1 HETATM 2148 O O . HOH S 8 . ? 33.569 36.730 23.406 1.00 41.98 ? 610 HOH A O 1 HETATM 2149 O O . HOH S 8 . ? 32.975 34.407 25.718 1.00 41.95 ? 611 HOH A O 1 HETATM 2150 O O . HOH S 8 . ? 33.412 34.888 28.604 1.00 29.64 ? 612 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 . HIC A 1 ? 0.0295 0.2223 0.1349 0.0287 0.0006 0.0160 1 HIC A N 2 C CA . HIC A 1 ? 0.0290 0.1756 0.1256 0.0227 -0.0056 -0.0034 1 HIC A CA 3 C C . HIC A 1 ? 0.0618 0.1456 0.1221 0.0338 -0.0117 -0.0044 1 HIC A C 4 O O . HIC A 1 ? 0.0364 0.2131 0.1005 0.0325 0.0217 0.0083 1 HIC A O 5 C CB . HIC A 1 ? 0.0265 0.1915 0.2084 -0.0075 0.0115 0.0223 1 HIC A CB 6 C CG . HIC A 1 ? 0.0265 0.1816 0.1546 -0.0091 0.0099 -0.0050 1 HIC A CG 7 N ND1 . HIC A 1 ? 0.0282 0.1640 0.1850 0.0071 0.0211 0.0305 1 HIC A ND1 8 C CD2 . HIC A 1 ? 0.0270 0.1944 0.1025 -0.0158 0.0053 -0.0124 1 HIC A CD2 9 C CE1 . HIC A 1 ? 0.0468 0.1824 0.1769 0.0077 0.0199 0.0380 1 HIC A CE1 10 N NE2 . HIC A 1 ? 0.0326 0.1930 0.1810 0.0115 0.0301 0.0072 1 HIC A NE2 11 C CZ . HIC A 1 ? 0.0715 0.2617 0.1228 0.0302 0.0611 0.0270 1 HIC A CZ 12 N N . GLY A 2 ? 0.0257 0.1735 0.0877 0.0072 0.0013 0.0036 2 GLY A N 13 C CA . GLY A 2 ? 0.0254 0.1560 0.0904 0.0030 -0.0003 -0.0063 2 GLY A CA 14 C C . GLY A 2 ? 0.0267 0.1585 0.0604 -0.0014 0.0064 0.0223 2 GLY A C 15 O O . GLY A 2 ? 0.0286 0.2168 0.0906 0.0147 -0.0114 0.0064 2 GLY A O 16 N N . TYR A 3 ? 0.0261 0.1945 0.0780 0.0093 -0.0046 -0.0201 3 TYR A N 17 C CA . TYR A 3 ? 0.0296 0.1736 0.0701 -0.0091 0.0000 -0.0011 3 TYR A CA 18 C C . TYR A 3 ? 0.0264 0.1624 0.0704 -0.0030 0.0072 -0.0108 3 TYR A C 19 O O . TYR A 3 ? 0.0346 0.1916 0.0822 0.0087 -0.0074 -0.0104 3 TYR A O 20 C CB . TYR A 3 ? 0.0299 0.1502 0.0903 -0.0015 -0.0007 -0.0023 3 TYR A CB 21 C CG . TYR A 3 ? 0.0261 0.1739 0.1351 -0.0030 -0.0091 -0.0043 3 TYR A CG 22 C CD1 . TYR A 3 ? 0.0255 0.1828 0.1439 0.0051 0.0016 -0.0061 3 TYR A CD1 23 C CD2 . TYR A 3 ? 0.0611 0.1805 0.1344 0.0272 0.0146 -0.0136 3 TYR A CD2 24 C CE1 . TYR A 3 ? 0.0446 0.1914 0.1178 -0.0236 0.0218 -0.0094 3 TYR A CE1 25 C CE2 . TYR A 3 ? 0.0528 0.2102 0.1148 0.0153 0.0139 -0.0021 3 TYR A CE2 26 C CZ . TYR A 3 ? 0.0358 0.2009 0.1194 0.0014 -0.0013 -0.0024 3 TYR A CZ 27 O OH . TYR A 3 ? 0.0369 0.2585 0.1611 -0.0226 0.0132 -0.0354 3 TYR A OH 28 N N . MET A 4 ? 0.0349 0.1611 0.0638 0.0018 -0.0189 -0.0167 4 MET A N 29 C CA . MET A 4 ? 0.0359 0.1284 0.1032 0.0039 0.0249 -0.0346 4 MET A CA 30 C C . MET A 4 ? 0.0357 0.1671 0.0959 -0.0012 -0.0259 -0.0269 4 MET A C 31 O O . MET A 4 ? 0.0306 0.2060 0.1250 0.0002 -0.0228 -0.0179 4 MET A O 32 C CB . MET A 4 ? 0.0338 0.1414 0.1188 0.0083 -0.0275 -0.0479 4 MET A CB 33 C CG . MET A 4 ? 0.0354 0.1809 0.1076 0.0309 0.0160 -0.0096 4 MET A CG 34 S SD . MET A 4 ? 0.0257 0.1941 0.1517 -0.0007 0.0069 -0.0249 4 MET A SD 35 C CE . MET A 4 ? 0.0505 0.1833 0.1930 -0.0055 0.0018 0.0158 4 MET A CE 36 N N . TYR A 5 ? 0.0290 0.2035 0.0598 -0.0208 0.0070 -0.0028 5 TYR A N 37 C CA . TYR A 5 ? 0.0375 0.1579 0.1060 -0.0047 -0.0215 -0.0283 5 TYR A CA 38 C C . TYR A 5 ? 0.0514 0.2176 0.0963 0.0233 0.0320 -0.0034 5 TYR A C 39 O O . TYR A 5 ? 0.0279 0.2255 0.1047 0.0146 0.0109 -0.0023 5 TYR A O 40 C CB . TYR A 5 ? 0.0520 0.2057 0.1219 0.0497 -0.0180 -0.0504 5 TYR A CB 41 C CG . TYR A 5 ? 0.1010 0.2279 0.1121 -0.0007 -0.0146 -0.0486 5 TYR A CG 42 C CD1 . TYR A 5 ? 0.0756 0.2201 0.1428 -0.0299 0.0013 -0.0364 5 TYR A CD1 43 C CD2 . TYR A 5 ? 0.0822 0.2089 0.1606 0.0171 -0.0128 -0.0326 5 TYR A CD2 44 C CE1 . TYR A 5 ? 0.0955 0.1923 0.1550 -0.0181 -0.0295 0.0313 5 TYR A CE1 45 C CE2 . TYR A 5 ? 0.0344 0.2767 0.2345 -0.0192 -0.0322 -0.0744 5 TYR A CE2 46 C CZ . TYR A 5 ? 0.0451 0.3005 0.1816 -0.0513 -0.0252 -0.0589 5 TYR A CZ 47 O OH . TYR A 5 ? 0.0914 0.3225 0.2691 -0.0434 0.0098 -0.0249 5 TYR A OH 48 N N . ILE A 6 ? 0.0269 0.2049 0.1103 0.0087 0.0093 -0.0111 6 ILE A N 49 C CA . ILE A 6 ? 0.0426 0.1846 0.1069 0.0164 -0.0103 0.0009 6 ILE A CA 50 C C . ILE A 6 ? 0.0444 0.1819 0.1049 0.0087 0.0034 0.0130 6 ILE A C 51 O O . ILE A 6 ? 0.0589 0.2018 0.0955 0.0165 0.0294 0.0034 6 ILE A O 52 C CB . ILE A 6 ? 0.0354 0.2488 0.1041 0.0475 0.0047 0.0164 6 ILE A CB 53 C CG1 . ILE A 6 ? 0.0470 0.2909 0.1686 0.0027 -0.0541 0.0401 6 ILE A CG1 54 C CG2 . ILE A 6 ? 0.0671 0.3166 0.1135 0.0909 -0.0185 -0.0091 6 ILE A CG2 55 C CD1 . ILE A 6 ? 0.0924 0.3537 0.1630 0.0682 -0.0472 0.0000 6 ILE A CD1 56 N N . PRO A 7 ? 0.0661 0.2285 0.1208 0.0145 0.0145 -0.0042 7 PRO A N 57 C CA . PRO A 7 ? 0.0585 0.2036 0.1193 0.0110 0.0075 -0.0007 7 PRO A CA 58 C C . PRO A 7 ? 0.0572 0.1941 0.1370 0.0143 0.0589 0.0047 7 PRO A C 59 O O . PRO A 7 ? 0.0623 0.1811 0.1116 0.0223 0.0283 -0.0051 7 PRO A O 60 C CB . PRO A 7 ? 0.0758 0.2108 0.0950 0.0311 0.0581 0.0146 7 PRO A CB 61 C CG . PRO A 7 ? 0.0488 0.2412 0.1123 0.0325 -0.0059 -0.0289 7 PRO A CG 62 C CD . PRO A 7 ? 0.0903 0.2271 0.1290 0.0416 0.0258 -0.0123 7 PRO A CD 63 N N . SER A 8 ? 0.0260 0.1816 0.1619 -0.0025 0.0098 0.0066 8 SER A N 64 C CA . SER A 8 ? 0.0599 0.2103 0.1024 -0.0002 -0.0205 0.0086 8 SER A CA 65 C C . SER A 8 ? 0.0271 0.1884 0.0835 -0.0112 0.0076 0.0004 8 SER A C 66 O O . SER A 8 ? 0.0371 0.2567 0.1017 0.0070 0.0283 -0.0261 8 SER A O 67 C CB . SER A 8 ? 0.0310 0.2319 0.1475 0.0128 0.0214 -0.0392 8 SER A CB 68 O OG . SER A 8 ? 0.0944 0.3205 0.2036 -0.0025 -0.0320 -0.0148 8 SER A OG 69 N N . SER A 9 ? 0.0328 0.1754 0.0957 0.0061 -0.0197 0.0354 9 SER A N 70 C CA . SER A 9 ? 0.0286 0.2002 0.0579 0.0231 0.0031 0.0032 9 SER A CA 71 C C . SER A 9 ? 0.0522 0.1934 0.0446 -0.0102 0.0060 -0.0172 9 SER A C 72 O O . SER A 9 ? 0.0275 0.1772 0.0880 0.0021 -0.0112 0.0180 9 SER A O 73 C CB . SER A 9 ? 0.0308 0.1953 0.0808 0.0188 0.0153 0.0156 9 SER A CB 74 O OG . SER A 9 ? 0.0353 0.1945 0.1390 0.0268 0.0247 -0.0049 9 SER A OG 75 N N . ARG A 10 ? 0.0294 0.1644 0.0532 -0.0224 0.0056 -0.0118 10 ARG A N 76 C CA . ARG A 10 ? 0.0488 0.1852 0.0801 0.0029 -0.0073 0.0005 10 ARG A CA 77 C C . ARG A 10 ? 0.0254 0.1811 0.0699 -0.0032 0.0001 -0.0008 10 ARG A C 78 O O . ARG A 10 ? 0.0271 0.1846 0.0891 -0.0152 -0.0052 0.0023 10 ARG A O 79 C CB . ARG A 10 ? 0.0303 0.2015 0.0702 -0.0117 0.0105 -0.0005 10 ARG A CB 80 C CG . ARG A 10 ? 0.0262 0.1945 0.0700 0.0121 0.0030 0.0166 10 ARG A CG 81 C CD . ARG A 10 ? 0.0337 0.2434 0.0601 0.0328 0.0089 -0.0128 10 ARG A CD 82 N NE . ARG A 10 ? 0.0297 0.2277 0.0722 0.0296 0.0008 -0.0050 10 ARG A NE 83 C CZ . ARG A 10 ? 0.0551 0.2133 0.0398 0.0407 0.0192 0.0094 10 ARG A CZ 84 N NH1 . ARG A 10 ? 0.0375 0.1896 0.1408 0.0029 -0.0374 -0.0192 10 ARG A NH1 85 N NH2 . ARG A 10 ? 0.0274 0.1907 0.0854 0.0184 -0.0058 -0.0317 10 ARG A NH2 86 N N . THR A 11 ? 0.0421 0.1654 0.1076 -0.0102 0.0301 0.0035 11 THR A N 87 C CA . THR A 11 ? 0.0296 0.1832 0.1119 -0.0121 0.0176 -0.0092 11 THR A CA 88 C C . THR A 11 ? 0.0466 0.1738 0.1115 0.0125 -0.0057 -0.0246 11 THR A C 89 O O . THR A 11 ? 0.0286 0.1978 0.1156 0.0227 -0.0062 -0.0047 11 THR A O 90 C CB . THR A 11 ? 0.0343 0.1923 0.0739 -0.0387 0.0016 -0.0085 11 THR A CB 91 O OG1 . THR A 11 ? 0.0306 0.2035 0.1151 -0.0141 -0.0141 -0.0478 11 THR A OG1 92 C CG2 . THR A 11 ? 0.0907 0.1760 0.1115 -0.0454 0.0207 0.0076 11 THR A CG2 93 N N . ARG A 12 ? 0.0412 0.1642 0.1139 -0.0081 -0.0056 -0.0146 12 ARG A N 94 C CA . ARG A 12 ? 0.0282 0.2024 0.0645 0.0080 0.0086 -0.0228 12 ARG A CA 95 C C . ARG A 12 ? 0.0336 0.2125 0.0772 -0.0185 0.0012 -0.0147 12 ARG A C 96 O O . ARG A 12 ? 0.0429 0.2200 0.1534 -0.0144 -0.0207 -0.0172 12 ARG A O 97 C CB . ARG A 12 ? 0.0291 0.1711 0.1161 -0.0042 -0.0182 -0.0038 12 ARG A CB 98 C CG . ARG A 12 ? 0.0362 0.2085 0.1065 -0.0443 -0.0030 -0.0021 12 ARG A CG 99 C CD . ARG A 12 ? 0.0462 0.2055 0.1242 -0.0603 0.0034 0.0152 12 ARG A CD 100 N NE . ARG A 12 ? 0.0598 0.2205 0.1829 -0.0726 -0.0124 0.0047 12 ARG A NE 101 C CZ . ARG A 12 ? 0.0406 0.2912 0.1705 -0.0260 -0.0411 -0.0169 12 ARG A CZ 102 N NH1 . ARG A 12 ? 0.0705 0.3404 0.1263 -0.0607 -0.0652 0.0481 12 ARG A NH1 103 N NH2 . ARG A 12 ? 0.0926 0.2709 0.3214 -0.0569 -0.1391 0.0769 12 ARG A NH2 104 N N . LEU A 13 ? 0.0276 0.2034 0.0926 -0.0200 0.0020 -0.0307 13 LEU A N 105 C CA . LEU A 13 ? 0.0580 0.2285 0.0927 0.0061 0.0268 -0.0225 13 LEU A CA 106 C C . LEU A 13 ? 0.0480 0.1810 0.1350 -0.0387 0.0239 -0.0031 13 LEU A C 107 O O . LEU A 13 ? 0.0411 0.1977 0.1238 -0.0520 0.0056 -0.0080 13 LEU A O 108 C CB . LEU A 13 ? 0.0808 0.1832 0.1734 -0.0299 0.0902 -0.0344 13 LEU A CB 109 C CG . LEU A 13 ? 0.0446 0.2195 0.2475 0.0019 0.0645 -0.0306 13 LEU A CG 110 C CD1 . LEU A 13 ? 0.1397 0.2630 0.2349 0.0203 -0.0713 -0.0755 13 LEU A CD1 111 C CD2 . LEU A 13 ? 0.0981 0.3286 0.4132 -0.0345 -0.0029 -0.0607 13 LEU A CD2 112 N N . GLY A 14 ? 0.0550 0.1633 0.1149 0.0023 0.0233 -0.0230 14 GLY A N 113 C CA . GLY A 14 ? 0.0546 0.2001 0.1313 0.0009 0.0034 0.0000 14 GLY A CA 114 C C . GLY A 14 ? 0.0770 0.2128 0.1153 -0.0189 0.0085 0.0009 14 GLY A C 115 O O . GLY A 14 ? 0.0735 0.2189 0.1370 -0.0031 0.0115 0.0196 14 GLY A O 116 N N . HIS A 15 ? 0.0365 0.1373 0.1309 0.0067 0.0309 -0.0009 15 HIS A N 117 C CA . HIS A 15 ? 0.0446 0.1386 0.1725 -0.0241 0.0481 -0.0125 15 HIS A CA 118 C C . HIS A 15 ? 0.0332 0.1902 0.1363 -0.0015 0.0190 -0.0165 15 HIS A C 119 O O . HIS A 15 ? 0.0744 0.2066 0.1921 -0.0360 0.0204 -0.0105 15 HIS A O 120 C CB . HIS A 15 ? 0.0457 0.2317 0.1672 -0.0272 0.0438 -0.0085 15 HIS A CB 121 C CG . HIS A 15 ? 0.0737 0.2379 0.1433 -0.0252 0.0168 -0.0039 15 HIS A CG 122 N ND1 . HIS A 15 ? 0.1749 0.2540 0.1949 -0.0622 0.0653 -0.0656 15 HIS A ND1 123 C CD2 . HIS A 15 ? 0.2118 0.3410 0.1474 0.0500 -0.0530 0.0261 15 HIS A CD2 124 C CE1 . HIS A 15 ? 0.2357 0.3170 0.1203 0.0147 -0.0261 -0.0315 15 HIS A CE1 125 N NE2 . HIS A 15 ? 0.1718 0.4504 0.2493 0.0386 -0.1129 -0.0623 15 HIS A NE2 126 N N . GLU A 16 ? 0.0294 0.1802 0.2195 -0.0017 0.0281 -0.0218 16 GLU A N 127 C CA . GLU A 16 ? 0.0406 0.2469 0.1602 -0.0477 0.0241 0.0088 16 GLU A CA 128 C C . GLU A 16 ? 0.0467 0.2303 0.1903 -0.0545 0.0214 0.0425 16 GLU A C 129 O O . GLU A 16 ? 0.0593 0.3311 0.2018 -0.0973 0.0113 0.0161 16 GLU A O 130 C CB . GLU A 16 ? 0.1155 0.2310 0.2210 -0.0754 -0.0420 -0.0038 16 GLU A CB 131 C CG . GLU A 16 ? 0.1823 0.3204 0.1802 -0.0264 -0.0949 -0.0251 16 GLU A CG 132 C CD . GLU A 16 ? 0.1625 0.3373 0.2783 -0.0027 -0.0941 -0.0266 16 GLU A CD 133 O OE1 . GLU A 16 ? 0.1384 0.3412 0.2702 0.0047 0.0436 -0.0043 16 GLU A OE1 134 O OE2 . GLU A 16 ? 0.1352 0.3436 0.3180 -0.0501 -0.1212 0.0681 16 GLU A OE2 135 N N . ALA A 17 ? 0.0405 0.2242 0.2108 -0.0404 0.0333 0.0125 17 ALA A N 136 C CA . ALA A 17 ? 0.0695 0.2491 0.1723 -0.0685 0.0404 -0.0031 17 ALA A CA 137 C C . ALA A 17 ? 0.1154 0.2360 0.2381 -0.1075 0.0313 0.0077 17 ALA A C 138 O O . ALA A 17 ? 0.1724 0.3042 0.2384 -0.0455 0.1036 0.0196 17 ALA A O 139 C CB . ALA A 17 ? 0.1552 0.1560 0.1880 -0.0244 0.0296 0.0126 17 ALA A CB 140 N N . GLY A 18 ? 0.1670 0.2110 0.2120 -0.0700 0.0052 0.0238 18 GLY A N 141 C CA . GLY A 18 ? 0.1203 0.2400 0.1831 -0.0487 -0.0137 -0.0308 18 GLY A CA 142 C C . GLY A 18 ? 0.1439 0.2063 0.2002 -0.0403 -0.0366 0.0299 18 GLY A C 143 O O . GLY A 18 ? 0.2328 0.2221 0.2507 -0.0088 -0.0518 0.0326 18 GLY A O 144 N N . ILE A 19 ? 0.0860 0.2259 0.1376 -0.0234 0.0153 -0.0065 19 ILE A N 145 C CA . ILE A 19 ? 0.1035 0.2600 0.1299 -0.0197 0.0107 0.0268 19 ILE A CA 146 C C . ILE A 19 ? 0.0772 0.2332 0.1251 -0.0147 -0.0188 -0.0001 19 ILE A C 147 O O . ILE A 19 ? 0.0741 0.2571 0.2337 0.0033 -0.0361 0.0122 19 ILE A O 148 C CB . ILE A 19 ? 0.0659 0.2458 0.1786 -0.0047 0.0338 0.0037 19 ILE A CB 149 C CG1 . ILE A 19 ? 0.0820 0.2866 0.2174 -0.0183 0.0483 -0.0567 19 ILE A CG1 150 C CG2 . ILE A 19 ? 0.1289 0.4152 0.1794 -0.1237 0.0003 -0.0334 19 ILE A CG2 151 C CD1 . ILE A 19 ? 0.2517 0.3732 0.1831 -0.0862 0.1112 -0.0536 19 ILE A CD1 152 N N . ASP A 20 ? 0.0655 0.2674 0.1407 0.0193 0.0157 0.0200 20 ASP A N 153 C CA . ASP A 20 ? 0.0389 0.2388 0.2018 0.0390 0.0260 -0.0382 20 ASP A CA 154 C C . ASP A 20 ? 0.0779 0.2848 0.1692 0.0440 0.0224 -0.0066 20 ASP A C 155 O O . ASP A 20 ? 0.0604 0.2383 0.1939 -0.0023 -0.0005 -0.0104 20 ASP A O 156 C CB . ASP A 20 ? 0.0544 0.2823 0.2500 0.0304 -0.0030 0.0089 20 ASP A CB 157 C CG . ASP A 20 ? 0.1098 0.2701 0.1470 0.0242 0.0245 0.0014 20 ASP A CG 158 O OD1 . ASP A 20 ? 0.0259 0.2577 0.1803 0.0122 -0.0003 -0.0185 20 ASP A OD1 159 O OD2 . ASP A 20 ? 0.0569 0.2928 0.2024 0.0053 0.0298 0.0208 20 ASP A OD2 160 N N . SER A 21 ? 0.0698 0.2283 0.1884 0.0033 0.0120 -0.0044 21 SER A N 161 C CA . SER A 21 ? 0.1463 0.2285 0.1491 -0.0414 0.0416 0.0063 21 SER A CA 162 C C . SER A 21 ? 0.0763 0.2024 0.1591 -0.0388 0.0193 0.0121 21 SER A C 163 O O . SER A 21 ? 0.1428 0.2245 0.1951 -0.0784 0.0279 -0.0264 21 SER A O 164 C CB . SER A 21 ? 0.1470 0.2267 0.2201 -0.0486 0.0741 0.0176 21 SER A CB 165 O OG . SER A 21 ? 0.1529 0.2600 0.2386 0.0446 0.0107 0.0104 21 SER A OG 166 N N . CYS A 22 ? 0.0463 0.1622 0.1849 -0.0016 0.0443 0.0040 22 CYS A N 167 C CA . CYS A 22 ? 0.0558 0.1911 0.1241 -0.0121 -0.0047 0.0144 22 CYS A CA 168 C C . CYS A 22 ? 0.0305 0.1870 0.1243 0.0213 0.0137 -0.0127 22 CYS A C 169 O O . CYS A 22 ? 0.0658 0.1849 0.1550 -0.0149 0.0064 -0.0135 22 CYS A O 170 C CB . CYS A 22 ? 0.0750 0.2145 0.1754 0.0054 0.0183 0.0125 22 CYS A CB 171 S SG . CYS A 22 ? 0.0523 0.2666 0.1404 -0.0009 0.0150 -0.0011 22 CYS A SG 172 N N . PRO A 23 ? 0.0486 0.1682 0.1183 0.0008 -0.0298 0.0130 23 PRO A N 173 C CA . PRO A 23 ? 0.0709 0.1896 0.1309 -0.0116 0.0068 0.0041 23 PRO A CA 174 C C . PRO A 23 ? 0.0331 0.1444 0.1077 0.0162 -0.0058 -0.0079 23 PRO A C 175 O O . PRO A 23 ? 0.1247 0.2088 0.1305 -0.0652 0.0431 -0.0362 23 PRO A O 176 C CB . PRO A 23 ? 0.0513 0.2153 0.1751 -0.0099 0.0106 -0.0148 23 PRO A CB 177 C CG . PRO A 23 ? 0.0293 0.2220 0.1694 -0.0281 0.0000 0.0052 23 PRO A CG 178 C CD . PRO A 23 ? 0.0294 0.2411 0.1414 -0.0139 0.0016 -0.0240 23 PRO A CD 179 N N . GLU A 24 ? 0.0345 0.1717 0.0881 -0.0276 -0.0120 -0.0183 24 GLU A N 180 C CA . GLU A 24 ? 0.0320 0.1255 0.1114 0.0256 0.0079 0.0155 24 GLU A CA 181 C C . GLU A 24 ? 0.0258 0.2025 0.1163 0.0037 -0.0063 0.0132 24 GLU A C 182 O O . GLU A 24 ? 0.0494 0.1877 0.1454 -0.0101 0.0205 0.0052 24 GLU A O 183 C CB . GLU A 24 ? 0.0900 0.1970 0.1004 -0.0325 0.0542 0.0114 24 GLU A CB 184 C CG . GLU A 24 ? 0.0538 0.2092 0.1416 -0.0293 0.0192 -0.0310 24 GLU A CG 185 C CD . GLU A 24 ? 0.0277 0.2171 0.1599 -0.0062 0.0175 -0.0052 24 GLU A CD 186 O OE1 . GLU A 24 ? 0.0289 0.2158 0.1620 -0.0180 0.0193 -0.0373 24 GLU A OE1 187 O OE2 . GLU A 24 ? 0.0659 0.2350 0.1159 0.0059 0.0001 -0.0180 24 GLU A OE2 188 N N . CYS A 25 ? 0.0307 0.2278 0.1722 -0.0150 0.0225 0.0303 25 CYS A N 189 C CA . CYS A 25 ? 0.0317 0.2485 0.1873 -0.0296 -0.0176 -0.0025 25 CYS A CA 190 C C . CYS A 25 ? 0.0301 0.1989 0.1571 0.0057 -0.0241 0.0147 25 CYS A C 191 O O . CYS A 25 ? 0.0588 0.2551 0.2215 0.0412 -0.0507 0.0197 25 CYS A O 192 C CB . CYS A 25 ? 0.0552 0.2251 0.2208 -0.0165 -0.0376 0.0090 25 CYS A CB 193 S SG . CYS A 25 ? 0.0644 0.2907 0.1924 0.0039 -0.0056 0.0473 25 CYS A SG 194 N N . ALA A 26 ? 0.0388 0.2420 0.2232 0.0057 0.0262 -0.0150 26 ALA A N 195 C CA . ALA A 26 ? 0.0408 0.2280 0.1295 -0.0106 0.0395 0.0000 26 ALA A CA 196 C C . ALA A 26 ? 0.0286 0.1926 0.1278 0.0032 0.0087 0.0329 26 ALA A C 197 O O . ALA A 26 ? 0.1061 0.2089 0.1310 0.0068 0.0137 0.0457 26 ALA A O 198 C CB . ALA A 26 ? 0.0957 0.3043 0.1007 0.0199 0.0245 -0.0410 26 ALA A CB 199 N N . ILE A 27 ? 0.0258 0.2417 0.1341 -0.0004 0.0073 0.0447 27 ILE A N 200 C CA . ILE A 27 ? 0.0283 0.2997 0.1536 -0.0224 0.0084 0.0437 27 ILE A CA 201 C C . ILE A 27 ? 0.0526 0.2505 0.1073 -0.0410 0.0316 0.0386 27 ILE A C 202 O O . ILE A 27 ? 0.1054 0.2135 0.1494 -0.0230 -0.0001 0.0373 27 ILE A O 203 C CB . ILE A 27 ? 0.0256 0.3276 0.1226 -0.0029 -0.0054 0.0422 27 ILE A CB 204 C CG1 . ILE A 27 ? 0.1346 0.3448 0.1607 -0.0802 -0.0286 0.0663 27 ILE A CG1 205 C CG2 . ILE A 27 ? 0.0946 0.3500 0.3307 -0.0741 0.1357 -0.1107 27 ILE A CG2 206 C CD1 . ILE A 27 ? 0.1645 0.4039 0.1884 -0.0616 -0.0417 0.0370 27 ILE A CD1 207 N N . LEU A 28 ? 0.0327 0.2387 0.0930 -0.0225 -0.0221 0.0520 28 LEU A N 208 C CA . LEU A 28 ? 0.0286 0.2594 0.1350 -0.0250 -0.0094 0.0119 28 LEU A CA 209 C C . LEU A 28 ? 0.0278 0.2303 0.1429 0.0105 -0.0119 0.0510 28 LEU A C 210 O O . LEU A 28 ? 0.0275 0.2188 0.1160 -0.0093 -0.0131 0.0123 28 LEU A O 211 C CB . LEU A 28 ? 0.0349 0.2632 0.1200 -0.0463 -0.0065 -0.0052 28 LEU A CB 212 C CG . LEU A 28 ? 0.0306 0.2822 0.1193 -0.0287 -0.0094 -0.0369 28 LEU A CG 213 C CD1 . LEU A 28 ? 0.0544 0.3624 0.1318 -0.0386 -0.0477 -0.0268 28 LEU A CD1 214 C CD2 . LEU A 28 ? 0.1239 0.3153 0.1241 -0.0457 -0.0536 -0.0529 28 LEU A CD2 215 N N . GLU A 29 ? 0.0327 0.2282 0.1604 0.0026 -0.0292 0.0525 29 GLU A N 216 C CA . GLU A 29 ? 0.0473 0.2110 0.2028 -0.0022 -0.0306 0.0208 29 GLU A CA 217 C C . GLU A 29 ? 0.0604 0.2411 0.1916 0.0062 -0.0445 0.0081 29 GLU A C 218 O O . GLU A 29 ? 0.1055 0.2850 0.2095 0.0781 -0.0475 0.0318 29 GLU A O 219 C CB . GLU A 29 ? 0.1398 0.2021 0.2681 -0.0331 -0.0219 -0.0178 29 GLU A CB 220 C CG . GLU A 29 ? 0.5253 0.2789 0.2472 -0.1297 -0.1642 0.0660 29 GLU A CG 221 C CD . GLU A 29 ? 0.8088 0.6498 0.2567 -0.0503 -0.3328 -0.1233 29 GLU A CD 222 O OE1 . GLU A 29 ? 0.9904 0.2237 0.3085 -0.0051 -0.3507 -0.0366 29 GLU A OE1 223 O OE2 . GLU A 29 ? 0.3675 0.7927 0.3122 0.1224 0.0898 -0.1926 29 GLU A OE2 224 N N . PRO A 30 ? 0.0523 0.2049 0.2521 0.0224 -0.0643 0.0321 30 PRO A N 225 C CA . PRO A 30 ? 0.0320 0.2383 0.2566 -0.0092 -0.0033 0.0084 30 PRO A CA 226 C C . PRO A 30 ? 0.0426 0.2201 0.1650 0.0571 -0.0102 -0.0034 30 PRO A C 227 O O . PRO A 30 ? 0.0790 0.2523 0.1661 0.0245 0.0057 -0.0125 30 PRO A O 228 C CB . PRO A 30 ? 0.0974 0.2404 0.3250 0.0425 -0.0512 -0.0345 30 PRO A CB 229 C CG . PRO A 30 ? 0.0741 0.3077 0.3119 0.1173 0.0089 0.0264 30 PRO A CG 230 C CD . PRO A 30 ? 0.0768 0.2663 0.1971 0.0426 -0.0310 0.0775 30 PRO A CD 231 N N . VAL A 31 ? 0.0427 0.2112 0.1697 0.0192 -0.0076 0.0028 31 VAL A N 232 C CA . VAL A 31 ? 0.0262 0.2191 0.1814 0.0132 -0.0009 -0.0081 31 VAL A CA 233 C C . VAL A 31 ? 0.0392 0.2481 0.2004 0.0174 0.0434 -0.0355 31 VAL A C 234 O O . VAL A 31 ? 0.0926 0.2573 0.1889 -0.0072 0.0293 0.0054 31 VAL A O 235 C CB . VAL A 31 ? 0.0366 0.2297 0.2104 0.0422 -0.0232 -0.0076 31 VAL A CB 236 C CG1 . VAL A 31 ? 0.0291 0.2891 0.2208 0.0315 -0.0070 -0.0524 31 VAL A CG1 237 C CG2 . VAL A 31 ? 0.1012 0.2558 0.1494 0.0403 -0.0327 0.0283 31 VAL A CG2 238 N N . SER A 32 ? 0.0360 0.2393 0.1975 0.0321 -0.0338 -0.0146 32 SER A N 239 C CA . SER A 32 ? 0.0391 0.2534 0.2241 0.0055 -0.0316 0.0047 32 SER A CA 240 C C . SER A 32 ? 0.0317 0.2437 0.2099 0.0064 -0.0078 0.0017 32 SER A C 241 O O . SER A 32 ? 0.0553 0.2782 0.1862 0.0331 0.0000 0.0022 32 SER A O 242 C CB . SER A 32 ? 0.0333 0.2515 0.2872 0.0094 -0.0402 0.0647 32 SER A CB 243 O OG . SER A 32 ? 0.0715 0.3573 0.2795 -0.0218 0.0071 0.0969 32 SER A OG 244 N N . SER A 33 ? 0.0340 0.1717 0.1950 0.0301 -0.0135 0.0005 33 SER A N 245 C CA . SER A 33 ? 0.0342 0.1293 0.1887 0.0004 -0.0269 0.0142 33 SER A CA 246 C C . SER A 33 ? 0.0288 0.1573 0.1567 -0.0143 -0.0067 -0.0068 33 SER A C 247 O O . SER A 33 ? 0.0335 0.2113 0.1516 0.0172 0.0007 -0.0094 33 SER A O 248 C CB . SER A 33 ? 0.0268 0.1333 0.1714 0.0000 -0.0149 0.0093 33 SER A CB 249 O OG . SER A 33 ? 0.0306 0.1989 0.1870 0.0289 0.0059 -0.0171 33 SER A OG 250 N N . TRP A 34 ? 0.0271 0.2228 0.1549 0.0062 -0.0144 -0.0005 34 TRP A N 251 C CA . TRP A 34 ? 0.0390 0.2425 0.1729 -0.0180 -0.0443 0.0297 34 TRP A CA 252 C C . TRP A 34 ? 0.0285 0.2602 0.2195 -0.0052 0.0238 0.0267 34 TRP A C 253 O O . TRP A 34 ? 0.0256 0.2574 0.2218 0.0061 0.0056 0.0273 34 TRP A O 254 C CB . TRP A 34 ? 0.0283 0.3424 0.1397 -0.0235 -0.0121 0.0021 34 TRP A CB 255 C CG . TRP A 34 ? 0.0329 0.2524 0.1428 -0.0352 -0.0162 0.0013 34 TRP A CG 256 C CD1 . TRP A 34 ? 0.0264 0.2836 0.1356 0.0148 -0.0052 0.0086 34 TRP A CD1 257 C CD2 . TRP A 34 ? 0.0278 0.2640 0.1138 -0.0236 -0.0037 0.0005 34 TRP A CD2 258 N NE1 . TRP A 34 ? 0.0319 0.2786 0.1265 -0.0060 0.0253 0.0082 34 TRP A NE1 259 C CE2 . TRP A 34 ? 0.0257 0.2243 0.1229 -0.0087 0.0028 -0.0170 34 TRP A CE2 260 C CE3 . TRP A 34 ? 0.0292 0.2595 0.1594 -0.0300 0.0024 -0.0423 34 TRP A CE3 261 C CZ2 . TRP A 34 ? 0.0487 0.2746 0.1524 0.0041 -0.0173 -0.0252 34 TRP A CZ2 262 C CZ3 . TRP A 34 ? 0.0276 0.2726 0.1860 -0.0237 0.0011 -0.0376 34 TRP A CZ3 263 C CH2 . TRP A 34 ? 0.0423 0.2357 0.1576 -0.0001 -0.0178 -0.0265 34 TRP A CH2 264 N N . PRO A 35 ? 0.0361 0.2655 0.2101 0.0068 0.0446 0.0141 35 PRO A N 265 C CA . PRO A 35 ? 0.0955 0.3033 0.1678 -0.0222 0.0401 0.0376 35 PRO A CA 266 C C . PRO A 35 ? 0.0520 0.2657 0.1407 -0.0220 0.0107 0.0529 35 PRO A C 267 O O . PRO A 35 ? 0.0555 0.2617 0.1485 -0.0168 -0.0006 0.0037 35 PRO A O 268 C CB . PRO A 35 ? 0.0481 0.2752 0.1365 0.0332 0.0483 0.0284 35 PRO A CB 269 C CG . PRO A 35 ? 0.0266 0.2871 0.2762 0.0102 0.0145 -0.0119 35 PRO A CG 270 C CD . PRO A 35 ? 0.0316 0.3019 0.2209 -0.0024 0.0262 -0.0092 35 PRO A CD 271 N N . ASP A 36 ? 0.0439 0.2369 0.1291 -0.0110 0.0083 0.0149 36 ASP A N 272 C CA . ASP A 36 ? 0.0373 0.2783 0.1881 -0.0383 0.0053 -0.0394 36 ASP A CA 273 C C . ASP A 36 ? 0.0380 0.2590 0.1519 -0.0108 -0.0077 0.0220 36 ASP A C 274 O O . ASP A 36 ? 0.0257 0.2618 0.1648 -0.0099 0.0010 0.0225 36 ASP A O 275 C CB . ASP A 36 ? 0.0633 0.3115 0.1955 -0.1042 -0.0123 0.0434 36 ASP A CB 276 C CG . ASP A 36 ? 0.0841 0.3246 0.1918 -0.0582 -0.0957 0.0445 36 ASP A CG 277 O OD1 . ASP A 36 ? 0.1948 0.2617 0.2822 0.0423 -0.0378 -0.0458 36 ASP A OD1 278 O OD2 . ASP A 36 ? 0.1337 0.5845 0.3583 -0.2172 0.0268 -0.0840 36 ASP A OD2 279 N N . LEU A 37 ? 0.0279 0.2114 0.2246 -0.0219 -0.0014 0.0331 37 LEU A N 280 C CA . LEU A 37 ? 0.0316 0.2260 0.1005 -0.0326 -0.0095 0.0050 37 LEU A CA 281 C C . LEU A 37 ? 0.0268 0.1968 0.0990 -0.0152 -0.0059 0.0241 37 LEU A C 282 O O . LEU A 37 ? 0.0618 0.2320 0.1592 -0.0541 0.0046 0.0264 37 LEU A O 283 C CB . LEU A 37 ? 0.0274 0.2316 0.1501 -0.0205 -0.0014 0.0333 37 LEU A CB 284 C CG . LEU A 37 ? 0.0314 0.2298 0.1655 -0.0017 0.0292 0.0097 37 LEU A CG 285 C CD1 . LEU A 37 ? 0.0355 0.2087 0.1334 -0.0290 0.0136 -0.0103 37 LEU A CD1 286 C CD2 . LEU A 37 ? 0.0957 0.2347 0.1327 -0.0111 0.0265 0.0484 37 LEU A CD2 287 N N . ASP A 38 ? 0.0269 0.2223 0.1854 -0.0178 0.0019 -0.0262 38 ASP A N 288 C CA . ASP A 38 ? 0.0270 0.2746 0.1870 -0.0188 -0.0039 -0.0417 38 ASP A CA 289 C C . ASP A 38 ? 0.0514 0.2131 0.1660 -0.0354 0.0009 -0.0408 38 ASP A C 290 O O . ASP A 38 ? 0.1334 0.3046 0.1437 -0.0265 0.0365 0.0034 38 ASP A O 291 C CB . ASP A 38 ? 0.0901 0.2717 0.1963 -0.0390 0.0716 -0.0643 38 ASP A CB 292 C CG . ASP A 38 ? 0.1185 0.2615 0.3730 -0.0511 0.0735 -0.0340 38 ASP A CG 293 O OD1 . ASP A 38 ? 0.0514 0.2911 0.2704 -0.0827 0.0000 -0.0048 38 ASP A OD1 294 O OD2 . ASP A 38 ? 0.2853 0.2803 0.5071 0.0054 0.0619 -0.0865 38 ASP A OD2 295 N N . ALA A 39 ? 0.0318 0.1942 0.1605 -0.0169 -0.0086 0.0249 39 ALA A N 296 C CA . ALA A 39 ? 0.0418 0.2208 0.2273 -0.0394 -0.0486 0.0391 39 ALA A CA 297 C C . ALA A 39 ? 0.0338 0.2545 0.1807 -0.0273 -0.0328 0.0418 39 ALA A C 298 O O . ALA A 39 ? 0.0937 0.2723 0.2054 -0.0817 -0.0581 0.0115 39 ALA A O 299 C CB . ALA A 39 ? 0.0468 0.2739 0.2002 -0.0211 -0.0449 0.0465 39 ALA A CB 300 N N . ALA A 40 ? 0.0478 0.2308 0.1364 -0.0018 -0.0415 0.0361 40 ALA A N 301 C CA . ALA A 40 ? 0.0919 0.2180 0.1063 0.0125 -0.0182 0.0152 40 ALA A CA 302 C C . ALA A 40 ? 0.0309 0.1970 0.1315 -0.0008 -0.0244 0.0112 40 ALA A C 303 O O . ALA A 40 ? 0.0319 0.2225 0.1798 0.0233 -0.0100 -0.0007 40 ALA A O 304 C CB . ALA A 40 ? 0.0275 0.2037 0.3106 -0.0098 -0.0198 -0.0275 40 ALA A CB 305 N N . PRO A 41 ? 0.0279 0.2251 0.1120 0.0108 -0.0136 -0.0063 41 PRO A N 306 C CA . PRO A 41 ? 0.0575 0.2815 0.1042 -0.0201 -0.0089 0.0014 41 PRO A CA 307 C C . PRO A 41 ? 0.0452 0.2117 0.0992 0.0151 -0.0032 -0.0108 41 PRO A C 308 O O . PRO A 41 ? 0.0529 0.2316 0.0976 -0.0303 0.0176 -0.0355 41 PRO A O 309 C CB . PRO A 41 ? 0.0430 0.2557 0.1278 -0.0311 -0.0338 -0.0224 41 PRO A CB 310 C CG . PRO A 41 ? 0.0796 0.5219 0.1388 0.0679 -0.0079 0.0427 41 PRO A CG 311 C CD . PRO A 41 ? 0.0356 0.2701 0.1305 0.0290 -0.0106 0.0202 41 PRO A CD 312 N N . VAL A 42 ? 0.0278 0.2320 0.0914 -0.0224 0.0028 0.0004 42 VAL A N 313 C CA . VAL A 42 ? 0.0304 0.2004 0.1055 -0.0135 -0.0187 0.0118 42 VAL A CA 314 C C . VAL A 42 ? 0.0388 0.1925 0.1240 -0.0204 -0.0344 0.0131 42 VAL A C 315 O O . VAL A 42 ? 0.0311 0.1960 0.1418 -0.0283 -0.0121 0.0033 42 VAL A O 316 C CB . VAL A 42 ? 0.0361 0.2021 0.1231 -0.0152 -0.0324 0.0382 42 VAL A CB 317 C CG1 . VAL A 42 ? 0.0612 0.2491 0.1477 0.0122 -0.0407 0.0523 42 VAL A CG1 318 C CG2 . VAL A 42 ? 0.0852 0.2217 0.2382 -0.0566 -0.0148 0.0061 42 VAL A CG2 319 N N . GLY A 43 ? 0.0541 0.2717 0.1103 -0.0172 -0.0344 0.0275 43 GLY A N 320 C CA . GLY A 43 ? 0.0417 0.2243 0.1113 -0.0066 -0.0094 -0.0068 43 GLY A CA 321 C C . GLY A 43 ? 0.0439 0.2314 0.0758 -0.0067 -0.0305 0.0199 43 GLY A C 322 O O . GLY A 43 ? 0.0352 0.2189 0.1441 -0.0081 -0.0059 0.0120 43 GLY A O 323 N N . ARG A 44 ? 0.0529 0.2027 0.1468 -0.0001 -0.0567 0.0304 44 ARG A N 324 C CA . ARG A 44 ? 0.0343 0.2610 0.1447 0.0266 -0.0254 0.0115 44 ARG A CA 325 C C . ARG A 44 ? 0.0392 0.1735 0.1021 0.0048 -0.0150 0.0126 44 ARG A C 326 O O . ARG A 44 ? 0.0475 0.2348 0.1053 -0.0212 -0.0077 0.0238 44 ARG A O 327 C CB . ARG A 44 ? 0.1103 0.2918 0.3206 0.0182 -0.0893 0.1455 44 ARG A CB 328 C CG . ARG A 44 ? 0.1767 0.3193 0.2486 -0.0364 -0.1393 0.1109 44 ARG A CG 329 C CD . ARG A 44 ? 0.1144 0.2874 0.6424 -0.0403 -0.1781 0.2786 44 ARG A CD 330 N NE . ARG A 44 ? 0.3118 0.3375 0.4815 -0.0785 -0.1539 0.1184 44 ARG A NE 331 C CZ . ARG A 44 ? 0.2893 0.3607 0.6383 0.1101 0.0195 0.2127 44 ARG A CZ 332 N NH1 . ARG A 44 ? 0.0700 0.3124 0.7745 -0.0017 -0.0728 0.0448 44 ARG A NH1 333 N NH2 . ARG A 44 ? 0.2359 0.6686 0.7974 -0.1124 -0.0190 0.2999 44 ARG A NH2 334 N N . SER A 45 ? 0.0417 0.2253 0.0870 -0.0009 -0.0311 -0.0203 45 SER A N 335 C CA . SER A 45 ? 0.0369 0.1651 0.0706 -0.0287 -0.0199 0.0220 45 SER A CA 336 C C . SER A 45 ? 0.0380 0.1770 0.0568 -0.0184 -0.0197 0.0183 45 SER A C 337 O O . SER A 45 ? 0.0339 0.2215 0.1048 -0.0367 0.0106 0.0062 45 SER A O 338 C CB . SER A 45 ? 0.0572 0.2247 0.0584 -0.0473 -0.0287 0.0323 45 SER A CB 339 O OG . SER A 45 ? 0.0269 0.2745 0.1509 -0.0089 -0.0137 0.0247 45 SER A OG 340 N N . GLY A 46 ? 0.0291 0.1824 0.1197 0.0015 -0.0190 -0.0142 46 GLY A N 341 C CA . GLY A 46 ? 0.0406 0.1636 0.1259 -0.0048 -0.0392 0.0057 46 GLY A CA 342 C C . GLY A 46 ? 0.0352 0.1778 0.0973 -0.0292 -0.0090 0.0323 46 GLY A C 343 O O . GLY A 46 ? 0.1053 0.2076 0.1066 0.0243 -0.0208 0.0165 46 GLY A O 344 N N . PRO A 47 ? 0.0663 0.2152 0.1136 0.0063 -0.0300 0.0364 47 PRO A N 345 C CA . PRO A 47 ? 0.0366 0.1972 0.1176 0.0263 -0.0221 0.0214 47 PRO A CA 346 C C . PRO A 47 ? 0.0784 0.2002 0.1689 0.0090 -0.0356 0.0138 47 PRO A C 347 O O . PRO A 47 ? 0.1229 0.1941 0.1368 -0.0102 -0.0158 0.0371 47 PRO A O 348 C CB . PRO A 47 ? 0.0937 0.1714 0.1450 0.0296 -0.0794 0.0210 47 PRO A CB 349 C CG . PRO A 47 ? 0.1526 0.2743 0.1466 0.0128 -0.0740 -0.0027 47 PRO A CG 350 C CD . PRO A 47 ? 0.0696 0.2170 0.1382 -0.0413 -0.0156 0.0191 47 PRO A CD 351 N N . CYS A 48 ? 0.0295 0.2213 0.0729 0.0038 -0.0140 -0.0028 48 CYS A N 352 C CA . CYS A 48 ? 0.0442 0.2046 0.0951 -0.0030 -0.0262 0.0027 48 CYS A CA 353 C C . CYS A 48 ? 0.0411 0.2096 0.1384 0.0002 -0.0178 -0.0090 48 CYS A C 354 O O . CYS A 48 ? 0.0438 0.2033 0.1138 0.0030 -0.0011 -0.0174 48 CYS A O 355 C CB . CYS A 48 ? 0.0845 0.2400 0.1108 0.0388 -0.0048 0.0153 48 CYS A CB 356 S SG . CYS A 48 ? 0.1185 0.2677 0.1182 0.0338 -0.0049 -0.0039 48 CYS A SG 357 N N . GLY A 49 ? 0.0401 0.1860 0.0871 -0.0217 -0.0280 0.0073 49 GLY A N 358 C CA . GLY A 49 ? 0.0588 0.1996 0.1322 0.0140 -0.0036 0.0274 49 GLY A CA 359 C C . GLY A 49 ? 0.0423 0.1469 0.0903 0.0180 0.0071 -0.0174 49 GLY A C 360 O O . GLY A 49 ? 0.0591 0.2178 0.0889 0.0180 0.0167 0.0215 49 GLY A O 361 N N . TYR A 50 ? 0.0374 0.1502 0.1277 0.0186 -0.0132 -0.0032 50 TYR A N 362 C CA . TYR A 50 ? 0.0295 0.1891 0.0973 -0.0102 -0.0164 0.0068 50 TYR A CA 363 C C . TYR A 50 ? 0.0282 0.1879 0.0917 0.0122 -0.0114 0.0008 50 TYR A C 364 O O . TYR A 50 ? 0.0582 0.2019 0.1377 -0.0090 0.0287 -0.0157 50 TYR A O 365 C CB . TYR A 50 ? 0.0421 0.1821 0.1139 -0.0105 -0.0356 -0.0215 50 TYR A CB 366 C CG . TYR A 50 ? 0.0305 0.2386 0.1469 -0.0180 -0.0231 0.0256 50 TYR A CG 367 C CD1 . TYR A 50 ? 0.0800 0.2619 0.1645 -0.0007 -0.0032 0.0343 50 TYR A CD1 368 C CD2 . TYR A 50 ? 0.1873 0.2206 0.1602 0.0088 -0.0865 -0.0101 50 TYR A CD2 369 C CE1 . TYR A 50 ? 0.0580 0.3534 0.1920 -0.0064 0.0233 0.0896 50 TYR A CE1 370 C CE2 . TYR A 50 ? 0.1888 0.2899 0.1428 0.0365 -0.0637 0.0342 50 TYR A CE2 371 C CZ . TYR A 50 ? 0.1251 0.2413 0.2132 -0.0470 -0.0479 0.0739 50 TYR A CZ 372 O OH . TYR A 50 ? 0.2155 0.3072 0.3085 -0.0098 -0.0827 0.1623 50 TYR A OH 373 N N . ASN A 51 ? 0.0895 0.1878 0.1174 -0.0263 -0.0345 -0.0155 51 ASN A N 374 C CA . ASN A 51 ? 0.0813 0.1714 0.1324 -0.0294 -0.0140 -0.0073 51 ASN A CA 375 C C . ASN A 51 ? 0.0282 0.1881 0.1274 -0.0217 -0.0030 0.0074 51 ASN A C 376 O O . ASN A 51 ? 0.0564 0.2308 0.1774 -0.0115 0.0422 0.0269 51 ASN A O 377 C CB . ASN A 51 ? 0.0697 0.1768 0.1574 -0.0263 -0.0022 -0.0045 51 ASN A CB 378 C CG . ASN A 51 ? 0.1767 0.1972 0.1483 0.0341 -0.0252 -0.0010 51 ASN A CG 379 O OD1 . ASN A 51 ? 0.1022 0.2844 0.2843 0.0384 -0.0578 -0.0720 51 ASN A OD1 380 N ND2 . ASN A 51 ? 0.1463 0.2866 0.1328 0.0184 -0.0012 0.0052 51 ASN A ND2 381 N N . ALA A 52 ? 0.0315 0.2257 0.2162 0.0084 -0.0086 0.0003 52 ALA A N 382 C CA . ALA A 52 ? 0.0833 0.2071 0.2525 0.0018 0.0024 0.0127 52 ALA A CA 383 C C . ALA A 52 ? 0.0417 0.1950 0.2774 0.0210 -0.0549 0.0278 52 ALA A C 384 O O . ALA A 52 ? 0.1504 0.2653 0.3427 0.0644 -0.0592 0.0835 52 ALA A O 385 C CB . ALA A 52 ? 0.0601 0.3037 0.2630 -0.0214 -0.0334 0.0173 52 ALA A CB 386 N N . ARG A 53 ? 0.0423 0.2096 0.2597 -0.0044 -0.0301 -0.0113 53 ARG A N 387 C CA . ARG A 53 ? 0.1022 0.1962 0.3083 -0.0255 -0.0067 0.0220 53 ARG A CA 388 C C . ARG A 53 ? 0.0675 0.2296 0.3813 -0.0375 0.0127 0.0335 53 ARG A C 389 O O . ARG A 53 ? 0.1618 0.2591 0.3329 0.0524 0.0864 0.0412 53 ARG A O 390 C CB . ARG A 53 ? 0.1407 0.2716 0.2265 -0.0322 0.0185 0.0047 53 ARG A CB 391 C CG . ARG A 53 ? 0.0941 0.3133 0.3438 -0.0174 0.0037 -0.0140 53 ARG A CG 392 C CD . ARG A 53 ? 0.2596 0.2917 0.3552 0.0170 0.0234 -0.0783 53 ARG A CD 393 N NE . ARG A 53 ? 0.2627 0.3991 0.3044 -0.0040 0.0009 -0.0572 53 ARG A NE 394 C CZ . ARG A 53 ? 0.2517 0.4511 0.3457 0.0358 -0.1080 0.0096 53 ARG A CZ 395 N NH1 . ARG A 53 ? 0.3132 0.3196 0.4413 0.0972 -0.2110 -0.0803 53 ARG A NH1 396 N NH2 . ARG A 53 ? 0.2506 0.3640 0.4512 0.1404 -0.0218 -0.0171 53 ARG A NH2 397 N N . ASP A 54 ? 0.1995 0.2123 0.2802 -0.0062 0.0310 0.0193 54 ASP A N 398 C CA . ASP A 54 ? 0.1696 0.2671 0.2676 0.0227 0.0040 0.0549 54 ASP A CA 399 C C . ASP A 54 ? 0.0275 0.2334 0.2959 0.0072 0.0230 -0.0005 54 ASP A C 400 O O . ASP A 54 ? 0.1831 0.3227 0.2463 -0.0533 0.0647 0.0131 54 ASP A O 401 C CB . ASP A 54 ? 0.1502 0.2713 0.3164 -0.0290 0.0175 0.0737 54 ASP A CB 402 C CG . ASP A 54 ? 0.3472 0.2489 0.3150 -0.0053 -0.1554 0.1094 54 ASP A CG 403 O OD1 . ASP A 54 ? 0.4738 0.2925 0.2569 -0.0958 -0.1410 0.1094 54 ASP A OD1 404 O OD2 . ASP A 54 ? 0.2430 0.2940 0.1987 -0.0036 -0.0664 0.0017 54 ASP A OD2 405 N N . SER A 55 ? 0.0757 0.2210 0.1934 -0.0236 0.0107 0.0413 55 SER A N 406 C CA . SER A 55 ? 0.0925 0.2081 0.1967 0.0256 0.0177 0.0063 55 SER A CA 407 C C . SER A 55 ? 0.0856 0.2176 0.2079 0.0211 0.0774 0.0591 55 SER A C 408 O O . SER A 55 ? 0.1955 0.2657 0.1784 0.0731 0.0546 0.1136 55 SER A O 409 C CB . SER A 55 ? 0.2700 0.2638 0.3031 0.0626 0.0181 0.0856 55 SER A CB 410 O OG . SER A 55 ? 0.3135 0.3181 0.2462 0.0488 0.0058 0.0445 55 SER A OG 411 N N . ILE A 56 ? 0.0282 0.1941 0.1698 0.0218 0.0063 0.0157 56 ILE A N 412 C CA . ILE A 56 ? 0.0282 0.1952 0.1718 0.0068 -0.0197 -0.0014 56 ILE A CA 413 C C . ILE A 56 ? 0.0303 0.2149 0.1192 -0.0274 -0.0116 0.0107 56 ILE A C 414 O O . ILE A 56 ? 0.0569 0.2167 0.1109 -0.0321 -0.0190 0.0326 56 ILE A O 415 C CB . ILE A 56 ? 0.0385 0.1970 0.1642 -0.0380 -0.0265 0.0035 56 ILE A CB 416 C CG1 . ILE A 56 ? 0.0365 0.1804 0.1773 -0.0218 -0.0396 0.0405 56 ILE A CG1 417 C CG2 . ILE A 56 ? 0.0355 0.2248 0.2478 -0.0224 -0.0452 0.0427 56 ILE A CG2 418 C CD1 . ILE A 56 ? 0.0696 0.2587 0.2224 0.0164 -0.0804 -0.0032 56 ILE A CD1 419 N N . ASP A 57 ? 0.0347 0.2023 0.1316 -0.0065 -0.0276 -0.0009 57 ASP A N 420 C CA . ASP A 57 ? 0.0709 0.1809 0.1170 0.0095 -0.0047 0.0209 57 ASP A CA 421 C C . ASP A 57 ? 0.0451 0.1894 0.0823 0.0104 0.0236 0.0124 57 ASP A C 422 O O . ASP A 57 ? 0.0394 0.2110 0.1296 0.0051 0.0375 -0.0149 57 ASP A O 423 C CB . ASP A 57 ? 0.0274 0.1979 0.1462 -0.0157 -0.0097 0.0103 57 ASP A CB 424 C CG . ASP A 57 ? 0.0331 0.1826 0.1111 -0.0025 -0.0258 0.0181 57 ASP A CG 425 O OD1 . ASP A 57 ? 0.0283 0.2100 0.1480 -0.0035 -0.0191 0.0364 57 ASP A OD1 426 O OD2 . ASP A 57 ? 0.0455 0.2360 0.1701 -0.0213 -0.0538 0.0406 57 ASP A OD2 427 N N . TYR A 58 ? 0.0294 0.1785 0.0851 -0.0066 -0.0154 0.0106 58 TYR A N 428 C CA . TYR A 58 ? 0.0328 0.2008 0.1009 0.0114 -0.0222 -0.0021 58 TYR A CA 429 C C . TYR A 58 ? 0.0529 0.2094 0.1289 0.0138 -0.0314 -0.0109 58 TYR A C 430 O O . TYR A 58 ? 0.0320 0.2092 0.1658 0.0113 -0.0303 -0.0306 58 TYR A O 431 C CB . TYR A 58 ? 0.0617 0.2215 0.1018 0.0209 0.0147 -0.0172 58 TYR A CB 432 C CG . TYR A 58 ? 0.0319 0.2288 0.1017 0.0075 -0.0213 0.0143 58 TYR A CG 433 C CD1 . TYR A 58 ? 0.0384 0.2459 0.1188 -0.0068 -0.0232 -0.0130 58 TYR A CD1 434 C CD2 . TYR A 58 ? 0.1072 0.2472 0.0791 0.0019 -0.0139 0.0041 58 TYR A CD2 435 C CE1 . TYR A 58 ? 0.0542 0.2386 0.1509 0.0075 -0.0599 -0.0326 58 TYR A CE1 436 C CE2 . TYR A 58 ? 0.1405 0.2160 0.1417 -0.0048 -0.0330 0.0261 58 TYR A CE2 437 C CZ . TYR A 58 ? 0.1358 0.1877 0.1652 0.0039 0.0191 0.0030 58 TYR A CZ 438 O OH . TYR A 58 ? 0.0608 0.2460 0.1851 -0.0128 0.0348 -0.0098 58 TYR A OH 439 N N . ASN A 59 ? 0.0288 0.1728 0.1216 -0.0226 -0.0021 0.0068 59 ASN A N 440 C CA . ASN A 59 ? 0.0428 0.1944 0.0582 -0.0259 -0.0228 0.0140 59 ASN A CA 441 C C . ASN A 59 ? 0.0694 0.2316 0.0826 -0.0270 -0.0065 -0.0240 59 ASN A C 442 O O . ASN A 59 ? 0.1393 0.2366 0.1435 0.0264 0.0342 -0.0258 59 ASN A O 443 C CB . ASN A 59 ? 0.0296 0.1486 0.1151 -0.0225 -0.0042 0.0028 59 ASN A CB 444 C CG . ASN A 59 ? 0.0383 0.2091 0.1232 0.0005 0.0000 0.0274 59 ASN A CG 445 O OD1 . ASN A 59 ? 0.0591 0.2130 0.0899 -0.0088 -0.0466 0.0197 59 ASN A OD1 446 N ND2 . ASN A 59 ? 0.0651 0.1687 0.0882 -0.0101 -0.0083 0.0241 59 ASN A ND2 447 N N . GLN A 60 ? 0.0662 0.2975 0.1181 -0.0436 0.0516 -0.0071 60 GLN A N 448 C CA . GLN A 60 ? 0.1213 0.4074 0.0873 -0.0781 0.0551 -0.0813 60 GLN A CA 449 C C . GLN A 60 ? 0.0850 0.3689 0.2098 -0.0506 0.0338 -0.0644 60 GLN A C 450 O O . GLN A 60 ? 0.0700 0.5105 0.2285 -0.0714 0.0550 -0.1522 60 GLN A O 451 C CB . GLN A 60 ? 0.2801 0.5173 0.1076 -0.2512 0.0274 0.0226 60 GLN A CB 452 C CG . GLN A 60 ? 0.1076 0.3811 0.4216 -0.1366 -0.1020 -0.0172 60 GLN A CG 453 C CD . GLN A 60 ? 0.3472 0.3446 0.3310 -0.0863 0.1806 0.0648 60 GLN A CD 454 O OE1 . GLN A 60 ? 0.1679 0.6316 0.4085 0.0100 -0.1425 -0.1990 60 GLN A OE1 455 N NE2 . GLN A 60 ? 0.4574 0.3536 0.3724 0.0374 0.2059 0.1712 60 GLN A NE2 456 N N . PRO A 61 ? 0.0913 0.2230 0.1403 -0.0808 0.0216 -0.0019 61 PRO A N 457 C CA . PRO A 61 ? 0.0463 0.2658 0.1119 -0.0449 0.0255 0.0272 61 PRO A CA 458 C C . PRO A 61 ? 0.0277 0.2382 0.1334 -0.0225 -0.0005 0.0133 61 PRO A C 459 O O . PRO A 61 ? 0.0907 0.2476 0.1537 -0.0156 -0.0272 0.0288 61 PRO A O 460 C CB . PRO A 61 ? 0.1838 0.2309 0.1594 -0.0229 0.0009 -0.0016 61 PRO A CB 461 C CG . PRO A 61 ? 0.2606 0.2402 0.1539 -0.0523 -0.0425 0.0184 61 PRO A CG 462 C CD . PRO A 61 ? 0.2377 0.2329 0.1126 -0.0738 -0.0129 0.0084 61 PRO A CD 463 N N . THR A 62 ? 0.0499 0.1929 0.1189 -0.0157 -0.0074 0.0094 62 THR A N 464 C CA . THR A 62 ? 0.0740 0.2386 0.1302 -0.0483 0.0064 0.0152 62 THR A CA 465 C C . THR A 62 ? 0.0725 0.2580 0.1153 -0.0315 0.0249 -0.0268 62 THR A C 466 O O . THR A 62 ? 0.0876 0.2857 0.1989 -0.0373 0.0125 0.0132 62 THR A O 467 C CB . THR A 62 ? 0.0807 0.2620 0.1500 -0.0324 -0.0055 0.0123 62 THR A CB 468 O OG1 . THR A 62 ? 0.0834 0.2677 0.1524 -0.0417 0.0033 -0.0371 62 THR A OG1 469 C CG2 . THR A 62 ? 0.0962 0.2552 0.1881 0.0710 -0.0208 0.0163 62 THR A CG2 470 N N . THR A 63 ? 0.0825 0.3131 0.2074 -0.0550 0.0339 0.0077 63 THR A N 471 C CA . THR A 63 ? 0.0799 0.3561 0.1348 -0.0651 0.0409 -0.0278 63 THR A CA 472 C C . THR A 63 ? 0.0605 0.3734 0.1476 -0.0502 0.0308 -0.0419 63 THR A C 473 O O . THR A 63 ? 0.0715 0.5465 0.2691 -0.0184 -0.0064 -0.0717 63 THR A O 474 C CB . THR A 63 ? 0.1367 0.3676 0.2009 -0.0648 0.0188 0.0072 63 THR A CB 475 O OG1 . THR A 63 ? 0.2863 0.3352 0.3563 -0.1199 0.1422 0.0048 63 THR A OG1 476 C CG2 . THR A 63 ? 0.4273 0.5660 0.2065 -0.2528 0.0556 0.0186 63 THR A CG2 477 N N . ASN A 64 ? 0.0839 0.3075 0.1264 -0.0537 0.0510 -0.0082 64 ASN A N 478 C CA . ASN A 64 ? 0.0729 0.3375 0.1488 -0.0685 0.0190 -0.0270 64 ASN A CA 479 C C . ASN A 64 ? 0.1099 0.3360 0.1377 -0.0807 -0.0357 -0.0053 64 ASN A C 480 O O . ASN A 64 ? 0.1154 0.3085 0.1231 -0.0561 0.0041 -0.0067 64 ASN A O 481 C CB . ASN A 64 ? 0.1038 0.3427 0.1777 -0.1023 0.0691 -0.0358 64 ASN A CB 482 C CG . ASN A 64 ? 0.0906 0.2735 0.1758 -0.0826 0.0413 -0.0782 64 ASN A CG 483 O OD1 . ASN A 64 ? 0.1026 0.3471 0.2346 -0.1145 0.0197 -0.0220 64 ASN A OD1 484 N ND2 . ASN A 64 ? 0.2146 0.2805 0.2506 -0.0331 0.0439 -0.0107 64 ASN A ND2 485 N N . TRP A 65 ? 0.0771 0.2711 0.0800 -0.0387 -0.0109 0.0090 65 TRP A N 486 C CA . TRP A 65 ? 0.1070 0.2367 0.1186 -0.0253 -0.0053 0.0212 65 TRP A CA 487 C C . TRP A 65 ? 0.0863 0.2319 0.1404 -0.0099 -0.0031 -0.0015 65 TRP A C 488 O O . TRP A 65 ? 0.0986 0.2332 0.1702 -0.0205 0.0020 0.0486 65 TRP A O 489 C CB . TRP A 65 ? 0.1113 0.2798 0.0972 -0.0217 -0.0026 0.0107 65 TRP A CB 490 C CG . TRP A 65 ? 0.0616 0.2514 0.1243 -0.0246 0.0217 0.0095 65 TRP A CG 491 C CD1 . TRP A 65 ? 0.1275 0.2305 0.1809 -0.0799 0.0588 -0.0123 65 TRP A CD1 492 C CD2 . TRP A 65 ? 0.0472 0.2743 0.1293 -0.0316 0.0350 -0.0111 65 TRP A CD2 493 N NE1 . TRP A 65 ? 0.1211 0.2569 0.1727 -0.0499 0.0900 -0.0489 65 TRP A NE1 494 C CE2 . TRP A 65 ? 0.0889 0.2483 0.1836 -0.0344 -0.0143 -0.0353 65 TRP A CE2 495 C CE3 . TRP A 65 ? 0.0463 0.3125 0.1356 -0.0503 0.0439 -0.0507 65 TRP A CE3 496 C CZ2 . TRP A 65 ? 0.0579 0.2980 0.0978 -0.0082 0.0035 -0.0029 65 TRP A CZ2 497 C CZ3 . TRP A 65 ? 0.0302 0.3232 0.1484 -0.0256 -0.0118 -0.0635 65 TRP A CZ3 498 C CH2 . TRP A 65 ? 0.1087 0.2844 0.1186 -0.0068 -0.0528 0.0021 65 TRP A CH2 499 N N . GLY A 66 ? 0.0854 0.2391 0.1537 0.0271 -0.0068 -0.0089 66 GLY A N 500 C CA . GLY A 66 ? 0.0696 0.2312 0.1496 0.0257 0.0258 0.0123 66 GLY A CA 501 C C . GLY A 66 ? 0.1464 0.2290 0.1116 0.0097 0.0401 0.0022 66 GLY A C 502 O O . GLY A 66 ? 0.1358 0.2261 0.1799 0.0091 -0.0110 0.0087 66 GLY A O 503 N N . SER A 67 ? 0.1580 0.2741 0.1656 -0.0282 0.0483 -0.0112 67 SER A N 504 C CA . SER A 67 ? 0.0865 0.3101 0.1547 -0.0012 0.0423 0.0382 67 SER A CA 505 C C . SER A 67 ? 0.0737 0.3592 0.2235 0.0469 0.0632 0.0433 67 SER A C 506 O O . SER A 67 ? 0.2409 0.3515 0.2302 0.0993 0.0540 0.0536 67 SER A O 507 C CB . SER A 67 ? 0.3049 0.3876 0.3403 -0.1076 0.2121 0.0343 67 SER A CB 508 O OG . SER A 67 ? 0.5387 0.5317 0.2613 -0.1572 0.1418 0.0572 67 SER A OG 509 N N . ASP A 68 ? 0.0897 0.3757 0.1978 0.0538 0.0763 0.0892 68 ASP A N 510 C CA . ASP A 68 ? 0.0615 0.4536 0.1867 0.0511 -0.0164 0.0663 68 ASP A CA 511 C C . ASP A 68 ? 0.0395 0.3735 0.2139 0.0346 0.0321 0.0755 68 ASP A C 512 O O . ASP A 68 ? 0.0872 0.3216 0.2412 0.0434 0.0673 0.0915 68 ASP A O 513 C CB . ASP A 68 ? 0.0785 0.6381 0.3263 -0.0365 0.0846 0.2547 68 ASP A CB 514 C CG . ASP A 68 ? 0.2559 0.7254 0.3063 0.0777 0.0808 0.2896 68 ASP A CG 515 O OD1 . ASP A 68 ? 0.3998 0.8390 0.3833 -0.0623 0.2203 0.1628 68 ASP A OD1 516 O OD2 . ASP A 68 ? 0.0987 0.7494 0.6027 -0.0236 0.0503 0.3581 68 ASP A OD2 517 N N . ALA A 69 ? 0.2069 0.2709 0.1158 0.0533 0.1134 0.0090 69 ALA A N 518 C CA . ALA A 69 ? 0.0565 0.2445 0.0992 0.0506 0.0409 0.0138 69 ALA A CA 519 C C . ALA A 69 ? 0.0493 0.2457 0.1424 0.0296 0.0269 0.0073 69 ALA A C 520 O O . ALA A 69 ? 0.0531 0.3276 0.2262 0.0162 0.0307 -0.0154 69 ALA A O 521 C CB . ALA A 69 ? 0.0486 0.2430 0.2213 0.0315 -0.0064 0.0048 69 ALA A CB 522 N N . VAL A 70 ? 0.0294 0.2106 0.1539 0.0145 0.0182 -0.0148 70 VAL A N 523 C CA . VAL A 70 ? 0.0289 0.2197 0.1989 -0.0171 0.0197 -0.0105 70 VAL A CA 524 C C . VAL A 70 ? 0.0658 0.1985 0.1867 -0.0428 -0.0075 -0.0129 70 VAL A C 525 O O . VAL A 70 ? 0.0613 0.2487 0.2334 -0.0236 -0.0396 -0.0200 70 VAL A O 526 C CB . VAL A 70 ? 0.0938 0.2987 0.2078 0.0387 0.0306 -0.0266 70 VAL A CB 527 C CG1 . VAL A 70 ? 0.2660 0.2971 0.2857 0.0627 0.0825 0.0264 70 VAL A CG1 528 C CG2 . VAL A 70 ? 0.1242 0.2472 0.1494 -0.0128 -0.0028 -0.0425 70 VAL A CG2 529 N N . GLN A 71 ? 0.0311 0.1958 0.1749 -0.0115 0.0263 0.0127 71 GLN A N 530 C CA . GLN A 71 ? 0.0462 0.2319 0.1959 -0.0412 0.0356 0.0459 71 GLN A CA 531 C C . GLN A 71 ? 0.0550 0.2316 0.1812 -0.0033 -0.0272 0.0025 71 GLN A C 532 O O . GLN A 71 ? 0.0256 0.2477 0.1586 0.0002 -0.0068 0.0031 71 GLN A O 533 C CB . GLN A 71 ? 0.0940 0.3012 0.2054 -0.0452 0.0531 -0.0050 71 GLN A CB 534 C CG . GLN A 71 ? 0.1666 0.4217 0.2519 -0.0696 -0.0040 0.0270 71 GLN A CG 535 C CD . GLN A 71 ? 0.6672 0.4030 0.1916 0.0300 -0.1289 0.0317 71 GLN A CD 536 O OE1 . GLN A 71 ? 0.3230 0.3526 1.0553 -0.0551 -0.1675 0.2457 71 GLN A OE1 537 N NE2 . GLN A 71 ? 0.9677 0.5852 0.4468 -0.2706 -0.3887 0.2704 71 GLN A NE2 538 N N . SER A 72 ? 0.0618 0.2513 0.1647 0.0195 0.0128 0.0076 72 SER A N 539 C CA . SER A 72 ? 0.0409 0.2188 0.1770 0.0324 -0.0345 0.0258 72 SER A CA 540 C C . SER A 72 ? 0.0310 0.1928 0.1606 0.0114 -0.0228 0.0019 72 SER A C 541 O O . SER A 72 ? 0.0915 0.2761 0.1897 -0.0461 -0.0662 0.0500 72 SER A O 542 C CB . SER A 72 ? 0.0899 0.2913 0.2985 0.1159 -0.0012 0.0562 72 SER A CB 543 O OG . SER A 72 ? 0.1913 0.2979 0.2423 0.0251 0.0906 0.0417 72 SER A OG 544 N N . TYR A 73 ? 0.0258 0.2306 0.1132 -0.0065 0.0049 0.0041 73 TYR A N 545 C CA . TYR A 73 ? 0.0549 0.2264 0.1069 0.0681 0.0260 0.0089 73 TYR A CA 546 C C . TYR A 73 ? 0.0397 0.2441 0.1346 0.0542 0.0134 0.0240 73 TYR A C 547 O O . TYR A 73 ? 0.1144 0.2933 0.1175 0.0369 -0.0335 -0.0105 73 TYR A O 548 C CB . TYR A 73 ? 0.0369 0.2142 0.1615 0.0150 0.0383 0.0094 73 TYR A CB 549 C CG . TYR A 73 ? 0.0406 0.2411 0.0593 0.0313 0.0141 -0.0275 73 TYR A CG 550 C CD1 . TYR A 73 ? 0.0591 0.2625 0.0563 -0.0010 0.0216 -0.0174 73 TYR A CD1 551 C CD2 . TYR A 73 ? 0.0960 0.2488 0.1404 0.0625 -0.0169 -0.0169 73 TYR A CD2 552 C CE1 . TYR A 73 ? 0.0580 0.2670 0.1097 0.0634 -0.0124 -0.0583 73 TYR A CE1 553 C CE2 . TYR A 73 ? 0.0755 0.2524 0.2030 0.0320 -0.0393 -0.0297 73 TYR A CE2 554 C CZ . TYR A 73 ? 0.0467 0.2021 0.2051 0.0150 -0.0312 -0.0385 73 TYR A CZ 555 O OH . TYR A 73 ? 0.0849 0.2243 0.2156 0.0269 0.0169 -0.0576 73 TYR A OH 556 N N . SER A 74 ? 0.0508 0.2106 0.1174 0.0308 0.0448 0.0097 74 SER A N 557 C CA . SER A 74 ? 0.0421 0.1944 0.1547 -0.0032 0.0461 0.0118 74 SER A CA 558 C C . SER A 74 ? 0.0427 0.2152 0.0838 -0.0057 0.0318 -0.0132 74 SER A C 559 O O . SER A 74 ? 0.0375 0.2026 0.1028 0.0097 0.0138 -0.0254 74 SER A O 560 C CB . SER A 74 ? 0.0812 0.2159 0.2704 0.0198 0.0271 0.0621 74 SER A CB 561 O OG . SER A 74 ? 0.0939 0.4245 0.3038 0.0008 0.0599 0.1000 74 SER A OG 562 N N . PRO A 75 ? 0.0513 0.2026 0.1186 -0.0262 0.0375 -0.0137 75 PRO A N 563 C CA . PRO A 75 ? 0.0262 0.2114 0.1262 -0.0083 0.0066 -0.0201 75 PRO A CA 564 C C . PRO A 75 ? 0.0440 0.1955 0.1332 0.0027 0.0111 -0.0185 75 PRO A C 565 O O . PRO A 75 ? 0.0979 0.2477 0.1325 0.0466 0.0039 -0.0164 75 PRO A O 566 C CB . PRO A 75 ? 0.0594 0.2343 0.1276 -0.0045 0.0002 -0.0250 75 PRO A CB 567 C CG . PRO A 75 ? 0.0721 0.2963 0.1351 -0.0137 0.0110 -0.0139 75 PRO A CG 568 C CD . PRO A 75 ? 0.0855 0.2918 0.1279 0.0262 0.0251 -0.0439 75 PRO A CD 569 N N . GLY A 76 ? 0.0390 0.1844 0.1383 0.0257 -0.0123 0.0021 76 GLY A N 570 C CA . GLY A 76 ? 0.0381 0.2407 0.1255 0.0496 0.0077 -0.0159 76 GLY A CA 571 C C . GLY A 76 ? 0.0318 0.2123 0.1096 0.0348 0.0053 0.0213 76 GLY A C 572 O O . GLY A 76 ? 0.0936 0.2580 0.1026 0.0191 0.0287 0.0022 76 GLY A O 573 N N . GLU A 77 ? 0.0517 0.1797 0.1266 0.0317 0.0057 0.0129 77 GLU A N 574 C CA . GLU A 77 ? 0.0644 0.1896 0.1149 0.0493 0.0068 0.0008 77 GLU A CA 575 C C . GLU A 77 ? 0.0307 0.2126 0.0955 0.0182 -0.0060 -0.0233 77 GLU A C 576 O O . GLU A 77 ? 0.0325 0.2601 0.1116 0.0290 -0.0186 -0.0281 77 GLU A O 577 C CB . GLU A 77 ? 0.0298 0.2227 0.1104 0.0263 0.0073 -0.0142 77 GLU A CB 578 C CG . GLU A 77 ? 0.0858 0.2529 0.1356 0.0346 -0.0310 -0.0112 77 GLU A CG 579 C CD . GLU A 77 ? 0.0706 0.2511 0.2095 0.0150 -0.0337 -0.0272 77 GLU A CD 580 O OE1 . GLU A 77 ? 0.1098 0.2989 0.1753 -0.0184 -0.0609 -0.0018 77 GLU A OE1 581 O OE2 . GLU A 77 ? 0.0833 0.3653 0.1815 -0.0471 0.0212 -0.0646 77 GLU A OE2 582 N N . GLU A 78 ? 0.0295 0.2520 0.0785 0.0186 0.0124 0.0050 78 GLU A N 583 C CA . GLU A 78 ? 0.0545 0.2438 0.1158 0.0195 0.0510 0.0167 78 GLU A CA 584 C C . GLU A 78 ? 0.0319 0.2682 0.1476 -0.0067 -0.0201 0.0171 78 GLU A C 585 O O . GLU A 78 ? 0.0628 0.2768 0.1773 0.0217 -0.0731 0.0047 78 GLU A O 586 C CB . GLU A 78 ? 0.1274 0.2670 0.1064 0.0612 0.0496 0.0187 78 GLU A CB 587 C CG . GLU A 78 ? 0.1244 0.2685 0.2250 0.0784 0.0178 0.0729 78 GLU A CG 588 C CD . GLU A 78 ? 0.1668 0.2701 0.2851 -0.0002 -0.0403 0.1513 78 GLU A CD 589 O OE1 . GLU A 78 ? 0.1294 0.6237 0.2661 0.0075 -0.0779 0.1198 78 GLU A OE1 590 O OE2 . GLU A 78 ? 0.3592 0.3488 0.4707 -0.1204 -0.1302 0.1804 78 GLU A OE2 591 N N . ILE A 79 ? 0.0310 0.2257 0.1437 0.0331 -0.0108 -0.0324 79 ILE A N 592 C CA . ILE A 79 ? 0.0559 0.2333 0.0973 0.0621 -0.0268 -0.0041 79 ILE A CA 593 C C . ILE A 79 ? 0.0307 0.2249 0.1271 0.0229 0.0139 -0.0225 79 ILE A C 594 O O . ILE A 79 ? 0.0317 0.2032 0.1446 0.0161 0.0196 -0.0400 79 ILE A O 595 C CB . ILE A 79 ? 0.0478 0.2161 0.1033 0.0255 0.0016 -0.0041 79 ILE A CB 596 C CG1 . ILE A 79 ? 0.0332 0.2418 0.1073 0.0290 0.0192 0.0080 79 ILE A CG1 597 C CG2 . ILE A 79 ? 0.0871 0.2451 0.1687 0.0546 -0.0235 -0.0351 79 ILE A CG2 598 C CD1 . ILE A 79 ? 0.1619 0.2605 0.1035 0.0692 0.0200 -0.0069 79 ILE A CD1 599 N N . GLU A 80 ? 0.0278 0.2046 0.1505 0.0159 0.0122 0.0038 80 GLU A N 600 C CA . GLU A 80 ? 0.0486 0.2054 0.1091 0.0006 0.0118 -0.0042 80 GLU A CA 601 C C . GLU A 80 ? 0.0257 0.1666 0.1359 0.0022 0.0065 0.0013 80 GLU A C 602 O O . GLU A 80 ? 0.0293 0.2400 0.1429 0.0079 0.0213 0.0161 80 GLU A O 603 C CB . GLU A 80 ? 0.1191 0.2528 0.1616 -0.0359 0.0199 -0.0656 80 GLU A CB 604 C CG . GLU A 80 ? 0.1771 0.2999 0.2910 0.0212 -0.0611 -0.1057 80 GLU A CG 605 C CD . GLU A 80 ? 0.1766 0.3994 0.8283 0.0455 -0.1652 -0.2686 80 GLU A CD 606 O OE1 . GLU A 80 ? 0.3279 0.3560 0.4085 -0.1093 0.0268 0.0417 80 GLU A OE1 607 O OE2 . GLU A 80 ? 0.2334 0.8193 1.3233 0.2282 -0.5045 -0.6504 80 GLU A OE2 608 N N . VAL A 81 ? 0.0284 0.2039 0.1241 0.0228 -0.0012 0.0205 81 VAL A N 609 C CA . VAL A 81 ? 0.0698 0.1584 0.1272 0.0356 0.0140 0.0047 81 VAL A CA 610 C C . VAL A 81 ? 0.0452 0.1758 0.0515 0.0180 -0.0158 -0.0029 81 VAL A C 611 O O . VAL A 81 ? 0.1071 0.2068 0.0705 0.0172 0.0168 -0.0061 81 VAL A O 612 C CB . VAL A 81 ? 0.0408 0.1994 0.0921 0.0471 0.0182 0.0180 81 VAL A CB 613 C CG1 . VAL A 81 ? 0.0750 0.2071 0.0860 0.0163 0.0030 -0.0016 81 VAL A CG1 614 C CG2 . VAL A 81 ? 0.0558 0.2169 0.1127 -0.0016 0.0259 -0.0073 81 VAL A CG2 615 N N . GLN A 82 ? 0.0358 0.1786 0.0793 0.0091 0.0017 0.0017 82 GLN A N 616 C CA . GLN A 82 ? 0.0308 0.1685 0.1060 0.0238 -0.0100 0.0074 82 GLN A CA 617 C C . GLN A 82 ? 0.0254 0.1497 0.0525 0.0029 -0.0015 0.0018 82 GLN A C 618 O O . GLN A 82 ? 0.0285 0.2151 0.0577 0.0121 -0.0086 0.0041 82 GLN A O 619 C CB . GLN A 82 ? 0.0574 0.2322 0.1036 -0.0215 0.0059 -0.0143 82 GLN A CB 620 C CG . GLN A 82 ? 0.0358 0.2118 0.1665 0.0012 -0.0383 -0.0210 82 GLN A CG 621 C CD . GLN A 82 ? 0.0270 0.2251 0.1236 -0.0185 0.0010 -0.0265 82 GLN A CD 622 O OE1 . GLN A 82 ? 0.0660 0.2591 0.1341 -0.0170 0.0005 0.0032 82 GLN A OE1 623 N NE2 . GLN A 82 ? 0.0389 0.2818 0.1404 0.0125 -0.0271 -0.0275 82 GLN A NE2 624 N N . TRP A 83 ? 0.0405 0.1808 0.0683 0.0120 0.0126 -0.0056 83 TRP A N 625 C CA . TRP A 83 ? 0.0269 0.1689 0.0808 -0.0121 -0.0052 -0.0046 83 TRP A CA 626 C C . TRP A 83 ? 0.0264 0.1759 0.0637 -0.0112 0.0033 -0.0046 83 TRP A C 627 O O . TRP A 83 ? 0.0313 0.1898 0.0758 -0.0019 -0.0151 -0.0161 83 TRP A O 628 C CB . TRP A 83 ? 0.0285 0.1843 0.0970 -0.0183 -0.0079 -0.0074 83 TRP A CB 629 C CG . TRP A 83 ? 0.0330 0.1868 0.0872 0.0169 -0.0004 0.0150 83 TRP A CG 630 C CD1 . TRP A 83 ? 0.0255 0.1949 0.1060 0.0037 0.0040 0.0079 83 TRP A CD1 631 C CD2 . TRP A 83 ? 0.0277 0.1722 0.0755 0.0056 -0.0099 0.0140 83 TRP A CD2 632 N NE1 . TRP A 83 ? 0.0292 0.1583 0.1036 -0.0228 0.0042 -0.0156 83 TRP A NE1 633 C CE2 . TRP A 83 ? 0.0260 0.1595 0.0698 0.0032 -0.0054 0.0015 83 TRP A CE2 634 C CE3 . TRP A 83 ? 0.0270 0.1787 0.0801 -0.0075 0.0086 -0.0029 83 TRP A CE3 635 C CZ2 . TRP A 83 ? 0.0398 0.2023 0.1035 0.0110 0.0114 -0.0161 83 TRP A CZ2 636 C CZ3 . TRP A 83 ? 0.0422 0.1758 0.0765 -0.0053 0.0024 -0.0455 83 TRP A CZ3 637 C CH2 . TRP A 83 ? 0.0566 0.1891 0.0855 0.0124 0.0130 -0.0102 83 TRP A CH2 638 N N . CYS A 84 ? 0.0295 0.1783 0.0845 -0.0105 -0.0138 -0.0063 84 CYS A N 639 C CA . CYS A 84 ? 0.0624 0.1859 0.0832 0.0177 0.0077 0.0057 84 CYS A CA 640 C C . CYS A 84 ? 0.0342 0.1750 0.0717 -0.0108 0.0044 -0.0120 84 CYS A C 641 O O . CYS A 84 ? 0.0450 0.1958 0.0937 -0.0073 -0.0061 0.0066 84 CYS A O 642 C CB . CYS A 84 ? 0.0345 0.2116 0.1306 0.0001 -0.0269 0.0171 84 CYS A CB 643 S SG . CYS A 84 ? 0.0504 0.2575 0.1340 -0.0118 -0.0110 -0.0189 84 CYS A SG 644 N N . VAL A 85 ? 0.0284 0.1688 0.0663 0.0195 0.0053 0.0081 85 VAL A N 645 C CA . VAL A 85 ? 0.0267 0.1480 0.0701 0.0115 -0.0041 -0.0053 85 VAL A CA 646 C C . VAL A 85 ? 0.0280 0.1711 0.0831 0.0082 0.0105 -0.0120 85 VAL A C 647 O O . VAL A 85 ? 0.0330 0.1990 0.1359 -0.0078 -0.0277 -0.0128 85 VAL A O 648 C CB . VAL A 85 ? 0.0259 0.1477 0.0834 0.0053 -0.0049 -0.0024 85 VAL A CB 649 C CG1 . VAL A 85 ? 0.0512 0.1839 0.0683 -0.0052 0.0167 -0.0121 85 VAL A CG1 650 C CG2 . VAL A 85 ? 0.0269 0.1818 0.1570 0.0142 -0.0054 0.0064 85 VAL A CG2 651 N N . ASP A 86 ? 0.0524 0.1680 0.0973 0.0198 0.0271 -0.0051 86 ASP A N 652 C CA . ASP A 86 ? 0.0583 0.1900 0.1025 0.0027 0.0312 -0.0111 86 ASP A CA 653 C C . ASP A 86 ? 0.0272 0.1943 0.0789 -0.0164 0.0052 -0.0133 86 ASP A C 654 O O . ASP A 86 ? 0.0375 0.1915 0.1376 -0.0288 0.0106 -0.0257 86 ASP A O 655 C CB . ASP A 86 ? 0.0258 0.1937 0.0988 -0.0068 -0.0037 -0.0150 86 ASP A CB 656 C CG . ASP A 86 ? 0.0629 0.1982 0.0908 0.0147 0.0105 0.0055 86 ASP A CG 657 O OD1 . ASP A 86 ? 0.0754 0.2104 0.1794 -0.0068 0.0098 -0.0130 86 ASP A OD1 658 O OD2 . ASP A 86 ? 0.0642 0.2152 0.1241 0.0149 0.0166 -0.0218 86 ASP A OD2 659 N N . HIS A 87 ? 0.0574 0.2186 0.1055 0.0044 -0.0360 -0.0291 87 HIS A N 660 C CA . HIS A 87 ? 0.0654 0.2233 0.1146 -0.0011 -0.0148 -0.0174 87 HIS A CA 661 C C . HIS A 87 ? 0.0608 0.2184 0.0861 -0.0033 0.0191 -0.0274 87 HIS A C 662 O O . HIS A 87 ? 0.0726 0.2528 0.0947 0.0364 0.0286 -0.0054 87 HIS A O 663 C CB . HIS A 87 ? 0.0326 0.2268 0.1504 0.0198 0.0041 -0.0575 87 HIS A CB 664 C CG . HIS A 87 ? 0.0810 0.2097 0.1465 0.0510 0.0027 -0.0371 87 HIS A CG 665 N ND1 . HIS A 87 ? 0.0721 0.2046 0.1751 0.0393 0.0262 -0.0536 87 HIS A ND1 666 C CD2 . HIS A 87 ? 0.1248 0.3018 0.1570 0.0589 -0.0343 -0.0583 87 HIS A CD2 667 C CE1 . HIS A 87 ? 0.1867 0.3067 0.1417 0.0543 -0.0559 -0.0506 87 HIS A CE1 668 N NE2 . HIS A 87 ? 0.1125 0.3387 0.1227 0.0331 -0.0618 -0.0842 87 HIS A NE2 669 N N . ASN A 88 ? 0.0506 0.2073 0.0969 0.0041 0.0284 -0.0264 88 ASN A N 670 C CA . ASN A 88 ? 0.0286 0.2204 0.1141 -0.0225 0.0096 -0.0139 88 ASN A CA 671 C C . ASN A 88 ? 0.0408 0.2166 0.1771 -0.0045 -0.0216 -0.0286 88 ASN A C 672 O O . ASN A 88 ? 0.0507 0.2275 0.2437 0.0434 0.0333 0.0001 88 ASN A O 673 C CB . ASN A 88 ? 0.0441 0.2055 0.1737 -0.0065 0.0086 -0.0338 88 ASN A CB 674 C CG . ASN A 88 ? 0.0518 0.2159 0.1719 0.0627 -0.0449 -0.0514 88 ASN A CG 675 O OD1 . ASN A 88 ? 0.0888 0.2179 0.1896 0.0252 -0.0522 -0.0420 88 ASN A OD1 676 N ND2 . ASN A 88 ? 0.1496 0.2205 0.2306 0.0670 -0.0230 -0.0442 88 ASN A ND2 677 N N . GLY A 89 ? 0.0729 0.1871 0.1357 0.0013 -0.0467 -0.0020 89 GLY A N 678 C CA . GLY A 89 ? 0.0908 0.2127 0.0648 -0.0138 -0.0044 -0.0185 89 GLY A CA 679 C C . GLY A 89 ? 0.0299 0.2037 0.1080 0.0001 -0.0189 -0.0305 89 GLY A C 680 O O . GLY A 89 ? 0.0297 0.1961 0.1255 0.0058 -0.0209 -0.0313 89 GLY A O 681 N N . ASP A 90 ? 0.0256 0.1951 0.0964 -0.0028 0.0048 -0.0251 90 ASP A N 682 C CA . ASP A 90 ? 0.0302 0.2107 0.1154 -0.0147 0.0189 -0.0072 90 ASP A CA 683 C C . ASP A 90 ? 0.0317 0.1915 0.0923 -0.0195 0.0103 -0.0252 90 ASP A C 684 O O . ASP A 90 ? 0.0359 0.2442 0.1064 -0.0276 0.0254 -0.0298 90 ASP A O 685 C CB . ASP A 90 ? 0.1112 0.2492 0.1056 0.0154 0.0186 -0.0232 90 ASP A CB 686 C CG . ASP A 90 ? 0.0263 0.2392 0.1208 0.0074 -0.0019 -0.0401 90 ASP A CG 687 O OD1 . ASP A 90 ? 0.0345 0.1976 0.1239 0.0070 0.0116 -0.0030 90 ASP A OD1 688 O OD2 . ASP A 90 ? 0.0689 0.2542 0.1113 -0.0018 -0.0165 -0.0130 90 ASP A OD2 689 N N . HIS A 91 ? 0.0401 0.1906 0.1277 -0.0239 -0.0305 -0.0214 91 HIS A N 690 C CA . HIS A 91 ? 0.0296 0.1526 0.1458 -0.0155 0.0201 -0.0284 91 HIS A CA 691 C C . HIS A 91 ? 0.0276 0.1644 0.1814 -0.0137 0.0136 -0.0184 91 HIS A C 692 O O . HIS A 91 ? 0.0334 0.1912 0.1271 -0.0291 0.0074 -0.0137 91 HIS A O 693 C CB . HIS A 91 ? 0.0702 0.2060 0.1584 0.0038 0.0204 -0.0067 91 HIS A CB 694 C CG . HIS A 91 ? 0.0302 0.1913 0.0635 -0.0180 0.0131 -0.0313 91 HIS A CG 695 N ND1 . HIS A 91 ? 0.0384 0.2209 0.1456 0.0105 0.0158 -0.0093 91 HIS A ND1 696 C CD2 . HIS A 91 ? 0.0451 0.2229 0.0990 0.0449 0.0343 0.0411 91 HIS A CD2 697 C CE1 . HIS A 91 ? 0.0541 0.2508 0.1212 0.0331 0.0321 -0.0050 91 HIS A CE1 698 N NE2 . HIS A 91 ? 0.0366 0.2324 0.0836 0.0386 0.0204 0.0295 91 HIS A NE2 699 N N . GLY A 92 ? 0.0301 0.1752 0.1413 -0.0163 0.0187 -0.0018 92 GLY A N 700 C CA . GLY A 92 ? 0.0315 0.2054 0.0904 -0.0229 0.0171 -0.0217 92 GLY A CA 701 C C . GLY A 92 ? 0.0277 0.1790 0.0823 -0.0046 0.0116 -0.0118 92 GLY A C 702 O O . GLY A 92 ? 0.0576 0.2100 0.0750 -0.0076 0.0054 -0.0173 92 GLY A O 703 N N . GLY A 93 ? 0.0272 0.1972 0.0855 0.0047 0.0100 -0.0073 93 GLY A N 704 C CA . GLY A 93 ? 0.0331 0.1864 0.1070 -0.0351 0.0061 -0.0093 93 GLY A CA 705 C C . GLY A 93 ? 0.0265 0.1957 0.0728 -0.0140 -0.0020 0.0129 93 GLY A C 706 O O . GLY A 93 ? 0.0559 0.1864 0.0889 0.0235 -0.0117 0.0061 93 GLY A O 707 N N . MET A 94 ? 0.0315 0.1879 0.1026 -0.0079 0.0211 0.0022 94 MET A N 708 C CA . MET A 94 ? 0.0265 0.1742 0.0401 -0.0123 -0.0004 -0.0138 94 MET A CA 709 C C . MET A 94 ? 0.0258 0.1652 0.0425 -0.0083 -0.0003 -0.0079 94 MET A C 710 O O . MET A 94 ? 0.0288 0.2023 0.0875 0.0220 0.0084 0.0145 94 MET A O 711 C CB . MET A 94 ? 0.0272 0.1675 0.0683 0.0015 0.0087 -0.0126 94 MET A CB 712 C CG . MET A 94 ? 0.0450 0.2499 0.0747 -0.0397 0.0101 -0.0017 94 MET A CG 713 S SD . MET A 94 ? 0.0350 0.2075 0.1163 -0.0077 0.0295 -0.0107 94 MET A SD 714 C CE . MET A 94 ? 0.0265 0.1850 0.1381 -0.0120 0.0050 0.0095 94 MET A CE 715 N N . PHE A 95 ? 0.0366 0.1871 0.0522 0.0142 0.0158 -0.0060 95 PHE A N 716 C CA . PHE A 95 ? 0.0309 0.1677 0.0504 -0.0208 0.0100 -0.0151 95 PHE A CA 717 C C . PHE A 95 ? 0.0288 0.1717 0.0820 -0.0204 0.0087 -0.0186 95 PHE A C 718 O O . PHE A 95 ? 0.0405 0.1909 0.1062 0.0319 0.0236 -0.0159 95 PHE A O 719 C CB . PHE A 95 ? 0.0436 0.1291 0.0646 -0.0087 0.0176 -0.0148 95 PHE A CB 720 C CG . PHE A 95 ? 0.0305 0.1717 0.0712 -0.0113 0.0135 -0.0031 95 PHE A CG 721 C CD1 . PHE A 95 ? 0.0361 0.2118 0.0745 0.0064 0.0016 -0.0153 95 PHE A CD1 722 C CD2 . PHE A 95 ? 0.0399 0.1789 0.0723 -0.0068 0.0092 -0.0455 95 PHE A CD2 723 C CE1 . PHE A 95 ? 0.0278 0.1622 0.0895 -0.0098 0.0014 0.0149 95 PHE A CE1 724 C CE2 . PHE A 95 ? 0.0254 0.1802 0.1031 0.0026 0.0022 -0.0117 95 PHE A CE2 725 C CZ . PHE A 95 ? 0.0253 0.2211 0.1014 0.0004 0.0020 -0.0054 95 PHE A CZ 726 N N . THR A 96 ? 0.0294 0.1848 0.0737 -0.0228 0.0066 -0.0017 96 THR A N 727 C CA . THR A 96 ? 0.0455 0.1732 0.0990 -0.0317 0.0183 -0.0030 96 THR A CA 728 C C . THR A 96 ? 0.0256 0.1249 0.0751 0.0041 0.0029 0.0022 96 THR A C 729 O O . THR A 96 ? 0.0372 0.1475 0.1025 0.0177 0.0295 0.0237 96 THR A O 730 C CB . THR A 96 ? 0.0509 0.1843 0.1347 -0.0415 0.0493 -0.0433 96 THR A CB 731 O OG1 . THR A 96 ? 0.0621 0.2051 0.2102 -0.0393 0.0514 -0.0628 96 THR A OG1 732 C CG2 . THR A 96 ? 0.0334 0.2530 0.1234 -0.0410 0.0191 -0.0650 96 THR A CG2 733 N N . TYR A 97 ? 0.0425 0.1365 0.0453 0.0216 0.0094 0.0128 97 TYR A N 734 C CA . TYR A 97 ? 0.0293 0.1731 0.0547 0.0215 0.0064 0.0098 97 TYR A CA 735 C C . TYR A 97 ? 0.0260 0.1946 0.0541 0.0064 0.0042 0.0099 97 TYR A C 736 O O . TYR A 97 ? 0.0332 0.1830 0.0858 0.0008 0.0141 -0.0072 97 TYR A O 737 C CB . TYR A 97 ? 0.0289 0.1793 0.0768 0.0234 -0.0003 0.0033 97 TYR A CB 738 C CG . TYR A 97 ? 0.0295 0.1860 0.0605 0.0113 -0.0112 -0.0056 97 TYR A CG 739 C CD1 . TYR A 97 ? 0.0295 0.2061 0.0644 0.0273 0.0000 0.0144 97 TYR A CD1 740 C CD2 . TYR A 97 ? 0.0374 0.1993 0.0660 0.0346 -0.0127 0.0086 97 TYR A CD2 741 C CE1 . TYR A 97 ? 0.0332 0.1871 0.0906 0.0337 0.0079 0.0027 97 TYR A CE1 742 C CE2 . TYR A 97 ? 0.0277 0.2063 0.0888 -0.0120 0.0107 -0.0090 97 TYR A CE2 743 C CZ . TYR A 97 ? 0.0341 0.1780 0.0851 0.0332 -0.0080 -0.0098 97 TYR A CZ 744 O OH . TYR A 97 ? 0.0281 0.1972 0.1220 -0.0104 0.0162 -0.0372 97 TYR A OH 745 N N . ARG A 98 ? 0.0262 0.1744 0.0489 0.0053 -0.0026 0.0065 98 ARG A N 746 C CA . ARG A 98 ? 0.0404 0.1641 0.0605 0.0271 0.0051 -0.0096 98 ARG A CA 747 C C . ARG A 98 ? 0.0316 0.1483 0.0732 -0.0027 0.0096 -0.0013 98 ARG A C 748 O O . ARG A 98 ? 0.0259 0.1625 0.0953 -0.0066 0.0050 -0.0017 98 ARG A O 749 C CB . ARG A 98 ? 0.0258 0.1855 0.1036 0.0073 0.0036 0.0003 98 ARG A CB 750 C CG . ARG A 98 ? 0.0264 0.2093 0.0559 -0.0052 -0.0057 0.0107 98 ARG A CG 751 C CD . ARG A 98 ? 0.0368 0.2489 0.0508 0.0345 -0.0129 -0.0025 98 ARG A CD 752 N NE . ARG A 98 ? 0.0257 0.2242 0.0915 0.0077 -0.0030 0.0060 98 ARG A NE 753 C CZ . ARG A 98 ? 0.0298 0.2559 0.0801 0.0250 0.0124 0.0247 98 ARG A CZ 754 N NH1 . ARG A 98 ? 0.0361 0.2108 0.1535 0.0127 0.0060 0.0393 98 ARG A NH1 755 N NH2 . ARG A 98 ? 0.0453 0.2567 0.0848 0.0345 -0.0037 0.0301 98 ARG A NH2 756 N N . ILE A 99 ? 0.0344 0.1470 0.0476 0.0123 0.0013 0.0080 99 ILE A N 757 C CA . ILE A 99 ? 0.0793 0.1368 0.0679 0.0140 0.0250 -0.0141 99 ILE A CA 758 C C . ILE A 99 ? 0.0449 0.1655 0.0849 0.0209 0.0068 -0.0002 99 ILE A C 759 O O . ILE A 99 ? 0.0900 0.1786 0.1335 -0.0051 0.0076 0.0142 99 ILE A O 760 C CB . ILE A 99 ? 0.0429 0.1718 0.1549 0.0088 0.0361 -0.0341 99 ILE A CB 761 C CG1 . ILE A 99 ? 0.0326 0.1774 0.0933 0.0321 0.0049 -0.0043 99 ILE A CG1 762 C CG2 . ILE A 99 ? 0.0294 0.2205 0.1227 0.0273 0.0004 -0.0356 99 ILE A CG2 763 C CD1 . ILE A 99 ? 0.0683 0.1794 0.1233 0.0592 -0.0096 0.0062 99 ILE A CD1 764 N N . CYS A 100 ? 0.0569 0.1888 0.0675 -0.0060 -0.0153 -0.0124 100 CYS A N 765 C CA . CYS A 100 ? 0.0275 0.2358 0.0275 0.0217 -0.0019 -0.0186 100 CYS A CA 766 C C . CYS A 100 ? 0.0375 0.2011 0.0857 0.0048 0.0261 -0.0174 100 CYS A C 767 O O . CYS A 100 ? 0.0310 0.2202 0.1142 -0.0178 0.0153 -0.0298 100 CYS A O 768 C CB . CYS A 100 ? 0.0328 0.2053 0.1011 -0.0024 -0.0239 0.0056 100 CYS A CB 769 S SG . CYS A 100 ? 0.1107 0.2645 0.0829 -0.0060 -0.0092 -0.0091 100 CYS A SG 770 N N . GLN A 101 ? 0.1226 0.1955 0.1190 0.0071 0.0053 -0.0193 101 GLN A N 771 C CA . GLN A 101 ? 0.1236 0.2145 0.1102 -0.0074 0.0385 -0.0453 101 GLN A CA 772 C C . GLN A 101 ? 0.1941 0.2653 0.1115 0.0631 0.0147 -0.0302 101 GLN A C 773 O O . GLN A 101 ? 0.1759 0.2581 0.2199 0.0828 0.0155 -0.0281 101 GLN A O 774 C CB . GLN A 101 ? 0.1027 0.2498 0.2014 0.0123 0.0612 -0.0008 101 GLN A CB 775 C CG . GLN A 101 ? 0.0932 0.2490 0.2206 0.0202 -0.0261 0.0406 101 GLN A CG 776 C CD . GLN A 101 ? 0.2438 0.2701 0.1266 -0.0202 -0.0210 0.0232 101 GLN A CD 777 O OE1 . GLN A 101 ? 0.3645 0.2478 0.2900 0.0177 -0.0560 0.0164 101 GLN A OE1 778 N NE2 . GLN A 101 ? 0.1566 0.3835 0.1491 0.0523 -0.0498 0.0062 101 GLN A NE2 779 N N . ASP A 102 ? 0.1727 0.2206 0.0852 0.0343 -0.0053 -0.0435 102 ASP A N 780 C CA . ASP A 102 ? 0.1081 0.2010 0.0877 -0.0539 0.0211 -0.0534 102 ASP A CA 781 C C . ASP A 102 ? 0.0669 0.1910 0.1396 -0.0228 0.0452 -0.0370 102 ASP A C 782 O O . ASP A 102 ? 0.1346 0.1977 0.1649 -0.0102 0.0215 -0.0071 102 ASP A O 783 C CB . ASP A 102 ? 0.1243 0.2842 0.1110 -0.0036 0.0120 -0.0575 102 ASP A CB 784 C CG . ASP A 102 ? 0.1072 0.3419 0.1006 -0.0182 -0.0019 -0.0044 102 ASP A CG 785 O OD1 . ASP A 102 ? 0.1721 0.4158 0.1779 -0.1075 0.0582 -0.0511 102 ASP A OD1 786 O OD2 . ASP A 102 ? 0.1801 0.3981 0.2096 -0.0764 -0.0890 -0.0447 102 ASP A OD2 787 N N . GLN A 103 ? 0.0790 0.2415 0.1892 0.0237 0.0228 -0.0425 103 GLN A N 788 C CA . GLN A 103 ? 0.0822 0.2785 0.1935 -0.0039 0.0088 -0.0125 103 GLN A CA 789 C C . GLN A 103 ? 0.1484 0.1836 0.1097 -0.0041 0.0689 -0.0553 103 GLN A C 790 O O . GLN A 103 ? 0.1856 0.1813 0.2199 0.0038 0.0142 0.0158 103 GLN A O 791 C CB . GLN A 103 ? 0.1373 0.2749 0.2157 0.0144 0.0292 -0.0449 103 GLN A CB 792 C CG . GLN A 103 ? 0.1840 0.2684 0.1908 -0.0118 0.0315 -0.0020 103 GLN A CG 793 C CD . GLN A 103 ? 0.2061 0.3103 0.1999 -0.0323 -0.0160 0.0373 103 GLN A CD 794 O OE1 . GLN A 103 ? 0.1672 0.4014 0.1256 -0.0332 0.0030 0.0014 103 GLN A OE1 795 N NE2 . GLN A 103 ? 0.1773 0.3022 0.1625 -0.0649 -0.0289 -0.0091 103 GLN A NE2 796 N N . SER A 104 ? 0.2169 0.2276 0.1508 -0.0227 0.0072 -0.0520 104 SER A N 797 C CA . SER A 104 ? 0.1619 0.2389 0.1808 -0.0233 -0.0046 -0.0258 104 SER A CA 798 C C . SER A 104 ? 0.2150 0.2455 0.1671 -0.0148 0.0463 -0.0336 104 SER A C 799 O O . SER A 104 ? 0.2356 0.2730 0.1686 0.0015 0.0472 0.0001 104 SER A O 800 C CB . SER A 104 ? 0.2537 0.2567 0.1817 -0.1035 -0.0496 0.0342 104 SER A CB 801 O OG . SER A 104 ? 0.2849 0.3802 0.2978 -0.1285 -0.0346 -0.0481 104 SER A OG 802 N N . ILE A 105 ? 0.1094 0.2220 0.1768 -0.0136 0.0198 -0.0208 105 ILE A N 803 C CA . ILE A 105 ? 0.0279 0.2650 0.1511 -0.0015 -0.0157 -0.0359 105 ILE A CA 804 C C . ILE A 105 ? 0.0769 0.2404 0.1115 0.0026 -0.0268 -0.0269 105 ILE A C 805 O O . ILE A 105 ? 0.1002 0.2702 0.1482 0.0141 0.0155 -0.0203 105 ILE A O 806 C CB . ILE A 105 ? 0.0987 0.2964 0.0988 -0.0263 -0.0403 -0.0212 105 ILE A CB 807 C CG1 . ILE A 105 ? 0.0523 0.3228 0.2448 -0.0232 -0.0413 -0.0519 105 ILE A CG1 808 C CG2 . ILE A 105 ? 0.1231 0.2980 0.2196 0.0256 -0.0175 -0.0140 105 ILE A CG2 809 C CD1 . ILE A 105 ? 0.2073 0.5457 0.1302 -0.1340 -0.0225 -0.0867 105 ILE A CD1 810 N N . VAL A 106 ? 0.0690 0.1948 0.1231 -0.0068 -0.0150 -0.0022 106 VAL A N 811 C CA . VAL A 106 ? 0.0265 0.2381 0.1171 -0.0038 -0.0103 0.0003 106 VAL A CA 812 C C . VAL A 106 ? 0.0867 0.1926 0.0675 -0.0155 -0.0386 -0.0013 106 VAL A C 813 O O . VAL A 106 ? 0.0394 0.1889 0.1410 -0.0083 -0.0024 -0.0072 106 VAL A O 814 C CB . VAL A 106 ? 0.1265 0.1897 0.1290 0.0161 -0.0392 0.0052 106 VAL A CB 815 C CG1 . VAL A 106 ? 0.1513 0.2193 0.1095 0.0284 -0.0504 -0.0333 106 VAL A CG1 816 C CG2 . VAL A 106 ? 0.0661 0.2347 0.1727 -0.0478 -0.0675 0.0064 106 VAL A CG2 817 N N . ASP A 107 ? 0.0937 0.1936 0.0983 -0.0423 0.0081 -0.0203 107 ASP A N 818 C CA . ASP A 107 ? 0.0320 0.2418 0.1292 -0.0268 -0.0015 0.0102 107 ASP A CA 819 C C . ASP A 107 ? 0.0701 0.2262 0.0698 -0.0263 -0.0394 -0.0196 107 ASP A C 820 O O . ASP A 107 ? 0.1627 0.2629 0.0721 -0.0234 0.0226 0.0216 107 ASP A O 821 C CB . ASP A 107 ? 0.1969 0.2477 0.1582 0.0059 -0.0142 -0.0080 107 ASP A CB 822 C CG . ASP A 107 ? 0.1573 0.2882 0.1630 0.0165 0.0275 -0.0411 107 ASP A CG 823 O OD1 . ASP A 107 ? 0.1226 0.3386 0.1973 -0.0205 0.0156 0.0005 107 ASP A OD1 824 O OD2 . ASP A 107 ? 0.2573 0.3152 0.1654 0.0966 0.0614 -0.0342 107 ASP A OD2 825 N N . LYS A 108 ? 0.0688 0.2528 0.1508 -0.0432 -0.0386 -0.0121 108 LYS A N 826 C CA . LYS A 108 ? 0.0682 0.2681 0.0905 -0.0277 -0.0356 -0.0051 108 LYS A CA 827 C C . LYS A 108 ? 0.0371 0.2113 0.1017 -0.0291 -0.0270 0.0258 108 LYS A C 828 O O . LYS A 108 ? 0.1331 0.2175 0.1013 -0.0190 -0.0197 0.0463 108 LYS A O 829 C CB . LYS A 108 ? 0.0658 0.2980 0.1029 -0.0268 -0.0533 -0.0083 108 LYS A CB 830 C CG . LYS A 108 ? 0.0638 0.3097 0.1742 -0.0537 -0.0203 -0.0088 108 LYS A CG 831 C CD . LYS A 108 ? 0.0571 0.4069 0.3992 -0.0183 -0.0522 -0.1945 108 LYS A CD 832 C CE . LYS A 108 ? 0.4358 0.4510 0.4916 -0.2167 -0.1493 -0.1903 108 LYS A CE 833 N NZ . LYS A 108 ? 0.6170 0.5731 0.4118 -0.0828 -0.1081 -0.2866 108 LYS A NZ 834 N N . PHE A 109 ? 0.0343 0.2047 0.0950 0.0289 -0.0116 0.0103 109 PHE A N 835 C CA . PHE A 109 ? 0.0402 0.2128 0.0829 -0.0157 -0.0285 0.0079 109 PHE A CA 836 C C . PHE A 109 ? 0.0304 0.1855 0.0979 0.0027 0.0106 0.0148 109 PHE A C 837 O O . PHE A 109 ? 0.0268 0.2439 0.0979 -0.0015 -0.0104 -0.0121 109 PHE A O 838 C CB . PHE A 109 ? 0.0295 0.2099 0.1060 0.0054 -0.0093 0.0198 109 PHE A CB 839 C CG . PHE A 109 ? 0.0275 0.1834 0.1044 0.0176 0.0058 0.0141 109 PHE A CG 840 C CD1 . PHE A 109 ? 0.0360 0.2069 0.1781 0.0187 0.0014 -0.0139 109 PHE A CD1 841 C CD2 . PHE A 109 ? 0.0562 0.1932 0.0770 0.0074 0.0382 0.0026 109 PHE A CD2 842 C CE1 . PHE A 109 ? 0.0417 0.2134 0.1868 -0.0191 0.0508 -0.0311 109 PHE A CE1 843 C CE2 . PHE A 109 ? 0.0604 0.2017 0.1212 -0.0246 0.0525 0.0154 109 PHE A CE2 844 C CZ . PHE A 109 ? 0.0776 0.2167 0.1519 0.0217 0.0091 0.0071 109 PHE A CZ 845 N N . LEU A 110 ? 0.0312 0.2304 0.0904 -0.0114 -0.0004 -0.0217 110 LEU A N 846 C CA . LEU A 110 ? 0.0323 0.2467 0.1390 -0.0108 -0.0277 0.0160 110 LEU A CA 847 C C . LEU A 110 ? 0.0268 0.2382 0.1384 0.0177 0.0014 0.0006 110 LEU A C 848 O O . LEU A 110 ? 0.0332 0.2469 0.1950 0.0002 0.0363 0.0218 110 LEU A O 849 C CB . LEU A 110 ? 0.0778 0.2312 0.1309 -0.0537 -0.0648 0.0043 110 LEU A CB 850 C CG . LEU A 110 ? 0.0938 0.2114 0.1598 -0.0269 -0.0341 0.0106 110 LEU A CG 851 C CD1 . LEU A 110 ? 0.1895 0.2064 0.1693 -0.0104 0.0162 -0.0223 110 LEU A CD1 852 C CD2 . LEU A 110 ? 0.1204 0.2545 0.1533 0.0229 0.0135 -0.0043 110 LEU A CD2 853 N N . ASP A 111 ? 0.0283 0.2270 0.1289 -0.0130 0.0122 0.0341 111 ASP A N 854 C CA . ASP A 111 ? 0.0980 0.2693 0.0851 0.0448 0.0049 0.0160 111 ASP A CA 855 C C . ASP A 111 ? 0.0793 0.2445 0.1358 -0.0228 -0.0029 0.0375 111 ASP A C 856 O O . ASP A 111 ? 0.0735 0.2511 0.1502 -0.0184 -0.0117 0.0073 111 ASP A O 857 C CB . ASP A 111 ? 0.2106 0.2740 0.0893 -0.0348 0.0174 0.0075 111 ASP A CB 858 C CG . ASP A 111 ? 0.3317 0.3852 0.0675 -0.0413 -0.0026 0.0227 111 ASP A CG 859 O OD1 . ASP A 111 ? 0.2289 0.4002 0.1091 -0.0359 0.0453 -0.0018 111 ASP A OD1 860 O OD2 . ASP A 111 ? 0.4589 0.3646 0.1266 -0.0874 0.0302 -0.0138 111 ASP A OD2 861 N N . PRO A 112 ? 0.0279 0.2930 0.1709 -0.0072 0.0183 0.0111 112 PRO A N 862 C CA . PRO A 112 ? 0.0634 0.3235 0.1327 -0.0133 0.0067 0.0165 112 PRO A CA 863 C C . PRO A 112 ? 0.0283 0.3374 0.1473 -0.0131 0.0168 0.0100 112 PRO A C 864 O O . PRO A 112 ? 0.1303 0.3213 0.1889 -0.0030 0.0163 0.0460 112 PRO A O 865 C CB . PRO A 112 ? 0.0609 0.3496 0.2293 -0.0137 0.0463 0.0513 112 PRO A CB 866 C CG . PRO A 112 ? 0.0976 0.4040 0.2868 -0.0463 0.0881 -0.0055 112 PRO A CG 867 C CD . PRO A 112 ? 0.0257 0.3602 0.1887 -0.0006 0.0075 0.0462 112 PRO A CD 868 N N . SER A 113 ? 0.0663 0.3450 0.1072 -0.0149 0.0019 0.0061 113 SER A N 869 C CA . SER A 113 ? 0.0874 0.3717 0.1388 -0.0065 -0.0123 0.0215 113 SER A CA 870 C C . SER A 113 ? 0.0952 0.3816 0.1511 -0.0200 0.0479 0.0975 113 SER A C 871 O O . SER A 113 ? 0.1069 0.5350 0.2150 -0.0276 -0.0083 0.1227 113 SER A O 872 C CB . SER A 113 ? 0.3650 0.4986 0.0438 0.0064 -0.0489 -0.0354 113 SER A CB 873 O OG . SER A 113 ? 0.2061 0.6475 0.2383 0.0241 0.0165 -0.1412 113 SER A OG 874 N N . TYR A 114 ? 0.0720 0.3078 0.0928 -0.0544 0.0469 0.0121 114 TYR A N 875 C CA . TYR A 114 ? 0.0531 0.3307 0.1261 -0.0324 0.0177 0.0204 114 TYR A CA 876 C C . TYR A 114 ? 0.0265 0.3599 0.1038 -0.0148 0.0034 0.0641 114 TYR A C 877 O O . TYR A 114 ? 0.0907 0.2983 0.0690 -0.0182 0.0115 0.0353 114 TYR A O 878 C CB . TYR A 114 ? 0.0701 0.3230 0.1964 -0.0514 0.0296 -0.0562 114 TYR A CB 879 C CG . TYR A 114 ? 0.0538 0.3377 0.1551 -0.0374 0.0042 0.0056 114 TYR A CG 880 C CD1 . TYR A 114 ? 0.0756 0.3497 0.1970 -0.0591 -0.0122 0.0809 114 TYR A CD1 881 C CD2 . TYR A 114 ? 0.0564 0.4124 0.1393 -0.0425 -0.0398 0.0385 114 TYR A CD2 882 C CE1 . TYR A 114 ? 0.1131 0.3631 0.1672 -0.1177 -0.0136 0.0519 114 TYR A CE1 883 C CE2 . TYR A 114 ? 0.0530 0.3948 0.1164 -0.0351 -0.0346 0.0127 114 TYR A CE2 884 C CZ . TYR A 114 ? 0.0470 0.3764 0.1360 -0.0511 -0.0275 0.0790 114 TYR A CZ 885 O OH . TYR A 114 ? 0.0787 0.4701 0.1434 -0.1061 -0.0267 -0.0176 114 TYR A OH 886 N N . LEU A 115 ? 0.0394 0.3577 0.1029 0.0128 -0.0094 0.0140 115 LEU A N 887 C CA . LEU A 115 ? 0.0264 0.2901 0.1630 -0.0077 0.0118 -0.0281 115 LEU A CA 888 C C . LEU A 115 ? 0.0283 0.2583 0.0728 0.0069 0.0009 0.0079 115 LEU A C 889 O O . LEU A 115 ? 0.1219 0.2729 0.1128 0.0042 -0.0622 0.0193 115 LEU A O 890 C CB . LEU A 115 ? 0.0697 0.3468 0.1822 0.0029 -0.0830 0.0174 115 LEU A CB 891 C CG . LEU A 115 ? 0.0846 0.2993 0.3062 -0.1112 0.0453 -0.0158 115 LEU A CG 892 C CD1 . LEU A 115 ? 0.2799 0.3471 0.2133 -0.0888 0.0950 -0.0389 115 LEU A CD1 893 C CD2 . LEU A 115 ? 0.0513 0.3789 0.3637 -0.0243 0.0006 -0.1027 115 LEU A CD2 894 N N . PRO A 116 ? 0.0421 0.2538 0.0854 0.0097 -0.0303 0.0163 116 PRO A N 895 C CA . PRO A 116 ? 0.0555 0.2739 0.1113 0.0125 -0.0156 0.0113 116 PRO A CA 896 C C . PRO A 116 ? 0.0543 0.2075 0.0826 -0.0037 -0.0407 0.0020 116 PRO A C 897 O O . PRO A 116 ? 0.0309 0.2188 0.1103 0.0111 -0.0212 -0.0143 116 PRO A O 898 C CB . PRO A 116 ? 0.0354 0.2942 0.1699 0.0013 -0.0363 0.0567 116 PRO A CB 899 C CG . PRO A 116 ? 0.0747 0.3831 0.2216 -0.0890 -0.0566 0.0532 116 PRO A CG 900 C CD . PRO A 116 ? 0.0566 0.3552 0.1171 0.0120 -0.0492 0.0495 116 PRO A CD 901 N N . THR A 117 ? 0.0542 0.2045 0.1222 0.0044 -0.0528 -0.0040 117 THR A N 902 C CA . THR A 117 ? 0.0347 0.2265 0.1132 -0.0065 -0.0286 0.0327 117 THR A CA 903 C C . THR A 117 ? 0.0638 0.1715 0.1134 0.0161 -0.0209 0.0147 117 THR A C 904 O O . THR A 117 ? 0.0434 0.1928 0.1191 -0.0194 -0.0407 0.0255 117 THR A O 905 C CB . THR A 117 ? 0.1023 0.2277 0.0734 0.0056 0.0113 -0.0170 117 THR A CB 906 O OG1 . THR A 117 ? 0.0499 0.2276 0.1176 0.0082 -0.0247 -0.0106 117 THR A OG1 907 C CG2 . THR A 117 ? 0.0270 0.1864 0.0888 0.0120 0.0062 -0.0107 117 THR A CG2 908 N N . ASN A 118 ? 0.0274 0.2550 0.0893 -0.0038 -0.0115 0.0045 118 ASN A N 909 C CA . ASN A 118 ? 0.0281 0.2296 0.1150 0.0062 0.0151 -0.0038 118 ASN A CA 910 C C . ASN A 118 ? 0.0517 0.2278 0.1059 0.0202 0.0401 -0.0300 118 ASN A C 911 O O . ASN A 118 ? 0.0572 0.2417 0.1389 0.0133 -0.0063 -0.0029 118 ASN A O 912 C CB . ASN A 118 ? 0.0621 0.2077 0.1731 0.0193 -0.0184 -0.0065 118 ASN A CB 913 C CG . ASN A 118 ? 0.1047 0.2418 0.1769 0.0240 -0.0165 -0.0517 118 ASN A CG 914 O OD1 . ASN A 118 ? 0.1159 0.2649 0.1905 -0.0131 -0.0271 0.0150 118 ASN A OD1 915 N ND2 . ASN A 118 ? 0.1758 0.3973 0.2838 0.1430 -0.1279 -0.1724 118 ASN A ND2 916 N N . ASP A 119 ? 0.0256 0.2246 0.0810 -0.0074 -0.0027 0.0194 119 ASP A N 917 C CA . ASP A 119 ? 0.0433 0.2332 0.1187 -0.0194 -0.0233 -0.0004 119 ASP A CA 918 C C . ASP A 119 ? 0.0318 0.1991 0.0992 -0.0332 0.0026 0.0068 119 ASP A C 919 O O . ASP A 119 ? 0.0338 0.2239 0.1216 -0.0028 -0.0180 0.0280 119 ASP A O 920 C CB . ASP A 119 ? 0.0666 0.2861 0.1235 -0.0130 -0.0627 0.0195 119 ASP A CB 921 C CG . ASP A 119 ? 0.1478 0.3323 0.1982 -0.1337 -0.0366 0.0775 119 ASP A CG 922 O OD1 . ASP A 119 ? 0.1916 0.4977 0.1438 -0.1691 -0.0810 0.0534 119 ASP A OD1 923 O OD2 . ASP A 119 ? 0.3209 0.4428 0.2869 -0.2190 -0.0390 0.0006 119 ASP A OD2 924 N N . GLU A 120 ? 0.0340 0.2001 0.1025 -0.0384 0.0032 0.0065 120 GLU A N 925 C CA . GLU A 120 ? 0.0746 0.1963 0.1147 -0.0038 0.0076 -0.0104 120 GLU A CA 926 C C . GLU A 120 ? 0.1075 0.1846 0.1118 0.0060 -0.0155 0.0050 120 GLU A C 927 O O . GLU A 120 ? 0.0602 0.2204 0.1381 0.0029 -0.0515 0.0140 120 GLU A O 928 C CB . GLU A 120 ? 0.0254 0.2282 0.1452 0.0037 -0.0032 -0.0193 120 GLU A CB 929 C CG . GLU A 120 ? 0.0520 0.2598 0.1391 0.0159 -0.0262 -0.0178 120 GLU A CG 930 C CD . GLU A 120 ? 0.1185 0.3208 0.1043 -0.0177 -0.0436 0.0030 120 GLU A CD 931 O OE1 . GLU A 120 ? 0.0265 0.2963 0.1494 0.0073 0.0114 0.0170 120 GLU A OE1 932 O OE2 . GLU A 120 ? 0.1626 0.3259 0.1146 0.0153 0.0096 -0.0017 120 GLU A OE2 933 N N . LYS A 121 ? 0.0875 0.1873 0.0687 -0.0235 -0.0158 0.0340 121 LYS A N 934 C CA . LYS A 121 ? 0.0531 0.1972 0.0748 -0.0322 -0.0091 0.0070 121 LYS A CA 935 C C . LYS A 121 ? 0.0283 0.1917 0.0846 -0.0178 -0.0080 0.0007 121 LYS A C 936 O O . LYS A 121 ? 0.0641 0.2133 0.1228 -0.0250 -0.0250 0.0212 121 LYS A O 937 C CB . LYS A 121 ? 0.0291 0.2106 0.0957 -0.0233 -0.0055 -0.0180 121 LYS A CB 938 C CG . LYS A 121 ? 0.0712 0.2217 0.1039 -0.0616 -0.0338 0.0069 121 LYS A CG 939 C CD . LYS A 121 ? 0.0862 0.2316 0.1024 -0.0603 -0.0196 0.0165 121 LYS A CD 940 C CE . LYS A 121 ? 0.0440 0.2785 0.0957 -0.0473 -0.0303 0.0238 121 LYS A CE 941 N NZ . LYS A 121 ? 0.0361 0.2684 0.1435 -0.0170 -0.0347 0.0179 121 LYS A NZ 942 N N . GLN A 122 ? 0.0349 0.2164 0.1349 -0.0296 -0.0240 0.0038 122 GLN A N 943 C CA . GLN A 122 ? 0.0373 0.2333 0.0894 -0.0135 -0.0263 0.0003 122 GLN A CA 944 C C . GLN A 122 ? 0.0345 0.2301 0.0887 -0.0025 -0.0241 0.0058 122 GLN A C 945 O O . GLN A 122 ? 0.0256 0.2614 0.0844 -0.0069 -0.0032 0.0113 122 GLN A O 946 C CB . GLN A 122 ? 0.0267 0.2465 0.1106 -0.0171 -0.0041 0.0217 122 GLN A CB 947 C CG . GLN A 122 ? 0.0274 0.2617 0.1139 -0.0121 0.0104 0.0164 122 GLN A CG 948 C CD . GLN A 122 ? 0.0263 0.2761 0.1156 -0.0162 -0.0011 0.0107 122 GLN A CD 949 O OE1 . GLN A 122 ? 0.0774 0.2879 0.1662 -0.0075 -0.0449 -0.0321 122 GLN A OE1 950 N NE2 . GLN A 122 ? 0.1033 0.2745 0.1468 -0.0303 -0.0300 0.0164 122 GLN A NE2 951 N N . ALA A 123 ? 0.0581 0.2293 0.0912 -0.0180 -0.0323 0.0040 123 ALA A N 952 C CA . ALA A 123 ? 0.0270 0.2204 0.1389 -0.0071 -0.0118 -0.0237 123 ALA A CA 953 C C . ALA A 123 ? 0.0853 0.2052 0.0981 -0.0080 -0.0284 0.0031 123 ALA A C 954 O O . ALA A 123 ? 0.1274 0.2001 0.1222 0.0025 -0.0325 0.0271 123 ALA A O 955 C CB . ALA A 123 ? 0.1181 0.2511 0.1172 -0.0324 -0.0606 -0.0116 123 ALA A CB 956 N N . ALA A 124 ? 0.0322 0.2070 0.1121 0.0064 0.0242 0.0074 124 ALA A N 957 C CA . ALA A 124 ? 0.0562 0.2349 0.1162 -0.0247 0.0006 -0.0015 124 ALA A CA 958 C C . ALA A 124 ? 0.0275 0.1565 0.1168 -0.0043 -0.0030 0.0009 124 ALA A C 959 O O . ALA A 124 ? 0.0891 0.1853 0.1312 -0.0041 -0.0250 0.0388 124 ALA A O 960 C CB . ALA A 124 ? 0.0744 0.1763 0.1592 0.0035 0.0244 -0.0031 124 ALA A CB 961 N N . GLU A 125 ? 0.0264 0.2104 0.0668 0.0130 0.0031 0.0059 125 GLU A N 962 C CA . GLU A 125 ? 0.0335 0.2237 0.0787 0.0058 0.0208 0.0064 125 GLU A CA 963 C C . GLU A 125 ? 0.0783 0.1941 0.0724 0.0245 -0.0037 0.0054 125 GLU A C 964 O O . GLU A 125 ? 0.0265 0.2118 0.0863 0.0046 -0.0074 0.0260 125 GLU A O 965 C CB . GLU A 125 ? 0.0568 0.2020 0.1223 0.0089 -0.0116 0.0124 125 GLU A CB 966 C CG . GLU A 125 ? 0.0380 0.2037 0.1083 0.0079 -0.0216 -0.0061 125 GLU A CG 967 C CD . GLU A 125 ? 0.0460 0.2843 0.0829 0.0322 -0.0206 0.0005 125 GLU A CD 968 O OE1 . GLU A 125 ? 0.0391 0.2821 0.1469 0.0304 -0.0348 0.0029 125 GLU A OE1 969 O OE2 . GLU A 125 ? 0.0376 0.2408 0.1184 -0.0166 0.0321 -0.0001 125 GLU A OE2 970 N N . ASP A 126 ? 0.0326 0.2330 0.1006 -0.0202 0.0191 0.0091 126 ASP A N 971 C CA . ASP A 126 ? 0.0260 0.1965 0.1769 0.0098 -0.0076 -0.0524 126 ASP A CA 972 C C . ASP A 126 ? 0.0426 0.1576 0.1107 -0.0051 0.0068 -0.0303 126 ASP A C 973 O O . ASP A 126 ? 0.0920 0.1931 0.1862 -0.0161 -0.0140 0.0306 126 ASP A O 974 C CB . ASP A 126 ? 0.0305 0.2324 0.1942 -0.0316 -0.0019 -0.0406 126 ASP A CB 975 C CG . ASP A 126 ? 0.0290 0.2564 0.2814 -0.0272 -0.0085 -0.0227 126 ASP A CG 976 O OD1 . ASP A 126 ? 0.1072 0.2922 0.1947 0.0309 0.0116 0.0026 126 ASP A OD1 977 O OD2 . ASP A 126 ? 0.0545 0.4572 0.3849 -0.0116 -0.0955 -0.0420 126 ASP A OD2 978 N N . CYS A 127 ? 0.0383 0.2109 0.1116 0.0084 0.0050 -0.0035 127 CYS A N 979 C CA . CYS A 127 ? 0.0301 0.1917 0.1231 -0.0125 -0.0197 0.0025 127 CYS A CA 980 C C . CYS A 127 ? 0.0254 0.1962 0.1061 0.0013 -0.0021 0.0074 127 CYS A C 981 O O . CYS A 127 ? 0.0621 0.1799 0.1136 0.0104 0.0068 -0.0006 127 CYS A O 982 C CB . CYS A 127 ? 0.0356 0.3394 0.1180 0.0217 -0.0043 -0.0381 127 CYS A CB 983 S SG . CYS A 127 ? 0.0965 0.3418 0.1307 0.0482 -0.0009 0.0042 127 CYS A SG 984 N N . PHE A 128 ? 0.0286 0.1669 0.0894 -0.0020 -0.0144 0.0236 128 PHE A N 985 C CA . PHE A 128 ? 0.0578 0.1856 0.0705 0.0052 0.0069 -0.0123 128 PHE A CA 986 C C . PHE A 128 ? 0.0335 0.2094 0.1046 -0.0284 -0.0189 0.0117 128 PHE A C 987 O O . PHE A 128 ? 0.0332 0.2393 0.0975 -0.0315 -0.0147 0.0217 128 PHE A O 988 C CB . PHE A 128 ? 0.0276 0.1995 0.0838 -0.0175 -0.0074 0.0186 128 PHE A CB 989 C CG . PHE A 128 ? 0.0271 0.1942 0.0751 -0.0058 -0.0096 0.0318 128 PHE A CG 990 C CD1 . PHE A 128 ? 0.0273 0.1727 0.0781 0.0103 -0.0069 0.0165 128 PHE A CD1 991 C CD2 . PHE A 128 ? 0.1147 0.2474 0.0643 0.0023 0.0066 0.0404 128 PHE A CD2 992 C CE1 . PHE A 128 ? 0.0271 0.1981 0.1210 0.0160 0.0081 0.0310 128 PHE A CE1 993 C CE2 . PHE A 128 ? 0.0694 0.2732 0.1199 0.0068 -0.0248 0.0754 128 PHE A CE2 994 C CZ . PHE A 128 ? 0.0318 0.2229 0.0821 0.0096 0.0190 0.0136 128 PHE A CZ 995 N N . ASP A 129 ? 0.0382 0.2234 0.0855 -0.0114 -0.0278 0.0308 129 ASP A N 996 C CA . ASP A 129 ? 0.0303 0.2211 0.1222 -0.0196 -0.0195 0.0267 129 ASP A CA 997 C C . ASP A 129 ? 0.0358 0.2141 0.1128 -0.0027 0.0290 0.0295 129 ASP A C 998 O O . ASP A 129 ? 0.0916 0.2101 0.1074 -0.0065 0.0165 0.0169 129 ASP A O 999 C CB . ASP A 129 ? 0.0257 0.2371 0.2013 -0.0094 -0.0020 0.0188 129 ASP A CB 1000 C CG . ASP A 129 ? 0.0412 0.2182 0.2007 -0.0461 0.0223 0.0274 129 ASP A CG 1001 O OD1 . ASP A 129 ? 0.1529 0.2862 0.1928 -0.0451 0.0446 -0.0469 129 ASP A OD1 1002 O OD2 . ASP A 129 ? 0.0590 0.3554 0.3439 0.0362 0.0664 0.0833 129 ASP A OD2 1003 N N . ALA A 130 ? 0.0283 0.2300 0.1175 -0.0074 0.0077 0.0201 130 ALA A N 1004 C CA . ALA A 130 ? 0.0261 0.2413 0.1374 -0.0062 -0.0088 0.0122 130 ALA A CA 1005 C C . ALA A 130 ? 0.0382 0.1874 0.2077 -0.0271 -0.0423 0.0210 130 ALA A C 1006 O O . ALA A 130 ? 0.0673 0.2351 0.3041 -0.0266 -0.0392 0.0759 130 ALA A O 1007 C CB . ALA A 130 ? 0.2055 0.2868 0.1617 -0.0772 -0.0081 0.0030 130 ALA A CB 1008 N N . GLY A 131 ? 0.0434 0.1618 0.0966 -0.0188 0.0091 0.0157 131 GLY A N 1009 C CA . GLY A 131 ? 0.0497 0.2196 0.1042 0.0092 0.0060 0.0030 131 GLY A CA 1010 C C . GLY A 131 ? 0.0365 0.1984 0.0888 -0.0428 0.0027 0.0141 131 GLY A C 1011 O O . GLY A 131 ? 0.0328 0.1982 0.0868 -0.0357 0.0037 -0.0046 131 GLY A O 1012 N N . LEU A 132 ? 0.0552 0.1836 0.0834 -0.0156 -0.0014 0.0029 132 LEU A N 1013 C CA . LEU A 132 ? 0.0289 0.1876 0.0950 -0.0057 -0.0154 -0.0011 132 LEU A CA 1014 C C . LEU A 132 ? 0.0306 0.1860 0.1129 -0.0087 -0.0061 0.0110 132 LEU A C 1015 O O . LEU A 132 ? 0.0704 0.1731 0.1288 0.0023 0.0106 -0.0002 132 LEU A O 1016 C CB . LEU A 132 ? 0.0345 0.2202 0.1088 0.0288 -0.0138 0.0372 132 LEU A CB 1017 C CG . LEU A 132 ? 0.0313 0.2047 0.1646 0.0292 -0.0005 -0.0148 132 LEU A CG 1018 C CD1 . LEU A 132 ? 0.0311 0.2456 0.2525 0.0358 -0.0058 -0.0426 132 LEU A CD1 1019 C CD2 . LEU A 132 ? 0.0307 0.2552 0.1948 -0.0354 -0.0022 0.0230 132 LEU A CD2 1020 N N . LEU A 133 ? 0.0383 0.1525 0.0886 0.0225 -0.0241 -0.0016 133 LEU A N 1021 C CA . LEU A 133 ? 0.0375 0.1765 0.0389 0.0289 0.0127 0.0239 133 LEU A CA 1022 C C . LEU A 133 ? 0.0525 0.1959 0.0264 0.0261 -0.0009 0.0116 133 LEU A C 1023 O O . LEU A 133 ? 0.0769 0.2181 0.0880 0.0170 -0.0016 -0.0043 133 LEU A O 1024 C CB . LEU A 133 ? 0.0673 0.1970 0.0741 -0.0060 0.0191 -0.0035 133 LEU A CB 1025 C CG . LEU A 133 ? 0.0501 0.1864 0.0641 0.0040 -0.0089 0.0484 133 LEU A CG 1026 C CD1 . LEU A 133 ? 0.0262 0.2067 0.1325 0.0051 -0.0006 -0.0198 133 LEU A CD1 1027 C CD2 . LEU A 133 ? 0.0747 0.2402 0.1058 0.0406 0.0037 0.0135 133 LEU A CD2 1028 N N . PRO A 134 ? 0.0540 0.2015 0.0695 0.0142 0.0126 0.0028 134 PRO A N 1029 C CA . PRO A 134 ? 0.0446 0.2264 0.0546 0.0169 -0.0060 -0.0091 134 PRO A CA 1030 C C . PRO A 134 ? 0.0283 0.2069 0.0350 0.0030 0.0050 0.0204 134 PRO A C 1031 O O . PRO A 134 ? 0.0692 0.2304 0.0637 0.0590 0.0149 0.0201 134 PRO A O 1032 C CB . PRO A 134 ? 0.0313 0.2364 0.1514 0.0091 0.0273 0.0264 134 PRO A CB 1033 C CG . PRO A 134 ? 0.0428 0.2269 0.1978 0.0466 0.0337 -0.0017 134 PRO A CG 1034 C CD . PRO A 134 ? 0.0416 0.2136 0.1309 0.0392 0.0170 -0.0050 134 PRO A CD 1035 N N . CYS A 135 ? 0.0267 0.2086 0.0696 0.0160 -0.0006 -0.0004 135 CYS A N 1036 C CA . CYS A 135 ? 0.0492 0.1807 0.0769 0.0022 0.0019 -0.0263 135 CYS A CA 1037 C C . CYS A 135 ? 0.0254 0.1951 0.0924 0.0037 0.0001 -0.0148 135 CYS A C 1038 O O . CYS A 135 ? 0.0258 0.2099 0.1169 0.0087 -0.0032 0.0037 135 CYS A O 1039 C CB . CYS A 135 ? 0.0501 0.1944 0.1158 0.0289 -0.0005 -0.0216 135 CYS A CB 1040 S SG . CYS A 135 ? 0.0416 0.2288 0.1197 0.0010 -0.0054 -0.0058 135 CYS A SG 1041 N N . THR A 136 ? 0.0697 0.1747 0.0804 -0.0074 -0.0299 -0.0006 136 THR A N 1042 C CA . THR A 136 ? 0.0663 0.1730 0.0792 -0.0215 0.0408 0.0211 136 THR A CA 1043 C C . THR A 136 ? 0.1341 0.1890 0.1557 0.0177 0.0361 0.0145 136 THR A C 1044 O O . THR A 136 ? 0.1201 0.2578 0.1192 0.0004 0.0339 0.0777 136 THR A O 1045 C CB . THR A 136 ? 0.0276 0.2377 0.1510 -0.0063 0.0164 -0.0077 136 THR A CB 1046 O OG1 . THR A 136 ? 0.0815 0.2189 0.1423 -0.0379 -0.0150 0.0087 136 THR A OG1 1047 C CG2 . THR A 136 ? 0.0319 0.2021 0.1411 -0.0049 0.0222 0.0269 136 THR A CG2 1048 N N . ASP A 137 ? 0.0513 0.2126 0.1247 0.0239 -0.0101 0.0174 137 ASP A N 1049 C CA . ASP A 137 ? 0.0628 0.1683 0.1294 0.0142 0.0029 0.0164 137 ASP A CA 1050 C C . ASP A 137 ? 0.0632 0.2000 0.1678 0.0181 -0.0010 0.0062 137 ASP A C 1051 O O . ASP A 137 ? 0.0791 0.2403 0.2547 0.0458 -0.0388 -0.0617 137 ASP A O 1052 C CB . ASP A 137 ? 0.0974 0.2376 0.1437 0.0636 0.0509 0.0125 137 ASP A CB 1053 C CG . ASP A 137 ? 0.2404 0.4111 0.1673 -0.0397 0.0899 -0.0407 137 ASP A CG 1054 O OD1 . ASP A 137 ? 0.1774 0.5131 0.2824 -0.0829 0.0898 -0.0980 137 ASP A OD1 1055 O OD2 . ASP A 137 ? 0.4395 0.3951 0.1406 0.0228 0.0696 -0.0686 137 ASP A OD2 1056 N N . VAL A 138 ? 0.0784 0.2072 0.1464 0.0091 0.0257 0.0046 138 VAL A N 1057 C CA . VAL A 138 ? 0.0776 0.2407 0.1675 0.0337 0.0133 0.0057 138 VAL A CA 1058 C C . VAL A 138 ? 0.0377 0.2754 0.2136 0.0187 -0.0059 0.0594 138 VAL A C 1059 O O . VAL A 138 ? 0.0706 0.3061 0.1665 0.0305 -0.0088 0.0709 138 VAL A O 1060 C CB . VAL A 138 ? 0.0322 0.2252 0.1429 0.0338 -0.0087 0.0177 138 VAL A CB 1061 C CG1 . VAL A 138 ? 0.0430 0.3443 0.0975 0.0245 -0.0138 0.0696 138 VAL A CG1 1062 C CG2 . VAL A 138 ? 0.1007 0.2976 0.1549 -0.0228 0.0285 0.0116 138 VAL A CG2 1063 N N . SER A 139 ? 0.2578 0.2955 0.2650 0.1395 -0.0672 0.0327 139 SER A N 1064 C CA . SER A 139 ? 0.2510 0.3362 0.2153 0.1673 -0.0002 0.0193 139 SER A CA 1065 C C . SER A 139 ? 0.2393 0.3311 0.1169 0.1644 -0.0100 0.0686 139 SER A C 1066 O O . SER A 139 ? 0.2103 0.4800 0.2088 0.0899 -0.0923 -0.0286 139 SER A O 1067 C CB . SER A 139 ? 0.4639 0.4769 0.2238 0.3734 -0.1341 -0.0067 139 SER A CB 1068 O OG . SER A 139 ? 0.4814 0.4261 0.3732 0.2286 -0.1056 0.0249 139 SER A OG 1069 N N . GLY A 140 ? 0.2584 0.3288 0.2151 0.0872 0.0467 0.1198 140 GLY A N 1070 C CA . GLY A 140 ? 0.2850 0.4307 0.1989 0.1240 0.0006 0.0580 140 GLY A CA 1071 C C . GLY A 140 ? 0.2282 0.3323 0.1965 0.0167 -0.0730 0.0442 140 GLY A C 1072 O O . GLY A 140 ? 0.3169 0.4032 0.1655 0.1239 -0.0734 0.0625 140 GLY A O 1073 N N . GLN A 141 ? 0.1354 0.2491 0.1549 0.0331 0.0005 0.0094 141 GLN A N 1074 C CA . GLN A 141 ? 0.0912 0.2326 0.1393 0.0072 0.0101 0.0493 141 GLN A CA 1075 C C . GLN A 141 ? 0.0870 0.2865 0.1736 -0.0306 0.0015 0.0216 141 GLN A C 1076 O O . GLN A 141 ? 0.0567 0.3091 0.1401 -0.0291 -0.0121 0.0300 141 GLN A O 1077 C CB . GLN A 141 ? 0.0487 0.2836 0.1071 0.0131 -0.0041 0.0139 141 GLN A CB 1078 C CG . GLN A 141 ? 0.0678 0.2328 0.0917 0.0047 -0.0049 0.0090 141 GLN A CG 1079 C CD . GLN A 141 ? 0.0257 0.2211 0.0903 -0.0040 -0.0043 -0.0119 141 GLN A CD 1080 O OE1 . GLN A 141 ? 0.0283 0.2215 0.1308 -0.0144 -0.0123 -0.0107 141 GLN A OE1 1081 N NE2 . GLN A 141 ? 0.0491 0.1770 0.0829 -0.0075 -0.0138 0.0048 141 GLN A NE2 1082 N N . GLU A 142 ? 0.0761 0.2934 0.1153 -0.0294 0.0155 0.0855 142 GLU A N 1083 C CA . GLU A 142 ? 0.0731 0.2327 0.1127 -0.0784 0.0192 0.0334 142 GLU A CA 1084 C C . GLU A 142 ? 0.0809 0.2633 0.1032 -0.0435 -0.0053 0.0171 142 GLU A C 1085 O O . GLU A 142 ? 0.1114 0.3404 0.1271 -0.0169 -0.0677 0.0853 142 GLU A O 1086 C CB . GLU A 142 ? 0.0443 0.3234 0.1045 -0.0464 -0.0326 0.0140 142 GLU A CB 1087 C CG . GLU A 142 ? 0.1274 0.4136 0.0868 -0.0855 -0.0638 0.0542 142 GLU A CG 1088 C CD . GLU A 142 ? 0.0896 0.4401 0.2018 -0.0363 0.0892 0.0935 142 GLU A CD 1089 O OE1 . GLU A 142 ? 0.1249 0.4305 0.2768 -0.1067 -0.0065 0.1382 142 GLU A OE1 1090 O OE2 . GLU A 142 ? 0.2089 0.6007 0.3508 0.1055 0.0099 0.1288 142 GLU A OE2 1091 N N . CYS A 143 ? 0.0625 0.2234 0.0966 -0.0154 0.0156 0.0203 143 CYS A N 1092 C CA . CYS A 143 ? 0.0690 0.2388 0.1082 0.0387 0.0234 0.0022 143 CYS A CA 1093 C C . CYS A 143 ? 0.0314 0.2086 0.0695 -0.0283 -0.0097 0.0059 143 CYS A C 1094 O O . CYS A 143 ? 0.0930 0.2042 0.1582 -0.0562 0.0129 -0.0249 143 CYS A O 1095 C CB . CYS A 143 ? 0.0269 0.2425 0.1192 0.0143 -0.0058 -0.0047 143 CYS A CB 1096 S SG . CYS A 143 ? 0.0344 0.2533 0.1337 -0.0008 0.0149 0.0079 143 CYS A SG 1097 N N . GLY A 144 ? 0.0295 0.2133 0.1463 0.0238 -0.0115 0.0041 144 GLY A N 1098 C CA . GLY A 144 ? 0.0585 0.2704 0.0790 0.0263 -0.0044 -0.0177 144 GLY A CA 1099 C C . GLY A 144 ? 0.0293 0.2538 0.0591 0.0038 0.0033 -0.0453 144 GLY A C 1100 O O . GLY A 144 ? 0.0379 0.2761 0.0709 0.0230 0.0153 -0.0216 144 GLY A O 1101 N N . TYR A 145 ? 0.0547 0.2311 0.0608 0.0020 0.0323 0.0000 145 TYR A N 1102 C CA . TYR A 145 ? 0.0281 0.2517 0.1648 -0.0237 0.0077 -0.0125 145 TYR A CA 1103 C C . TYR A 145 ? 0.0417 0.2403 0.1096 -0.0003 0.0366 0.0226 145 TYR A C 1104 O O . TYR A 145 ? 0.0794 0.2641 0.1176 0.0303 0.0010 0.0020 145 TYR A O 1105 C CB . TYR A 145 ? 0.0532 0.2067 0.1128 -0.0098 0.0493 -0.0268 145 TYR A CB 1106 C CG . TYR A 145 ? 0.0276 0.2119 0.0994 -0.0156 0.0102 -0.0227 145 TYR A CG 1107 C CD1 . TYR A 145 ? 0.0345 0.1915 0.1168 0.0110 -0.0275 0.0051 145 TYR A CD1 1108 C CD2 . TYR A 145 ? 0.1057 0.2147 0.1825 0.0395 0.0696 -0.0055 145 TYR A CD2 1109 C CE1 . TYR A 145 ? 0.0299 0.2050 0.1111 0.0151 0.0117 -0.0215 145 TYR A CE1 1110 C CE2 . TYR A 145 ? 0.1331 0.1990 0.1638 0.0501 -0.0238 -0.0024 145 TYR A CE2 1111 C CZ . TYR A 145 ? 0.0507 0.2448 0.1552 0.0423 -0.0036 0.0028 145 TYR A CZ 1112 O OH . TYR A 145 ? 0.0920 0.2386 0.1497 0.0042 -0.0189 0.0196 145 TYR A OH 1113 N N . SER A 146 ? 0.0337 0.1883 0.1249 0.0091 0.0281 0.0034 146 SER A N 1114 C CA . SER A 146 ? 0.0290 0.2009 0.0722 0.0042 0.0128 -0.0051 146 SER A CA 1115 C C . SER A 146 ? 0.0290 0.2179 0.1053 -0.0003 0.0159 -0.0494 146 SER A C 1116 O O . SER A 146 ? 0.0437 0.2357 0.1421 -0.0227 0.0277 -0.0353 146 SER A O 1117 C CB . SER A 146 ? 0.0350 0.2564 0.0566 0.0085 -0.0109 -0.0358 146 SER A CB 1118 O OG . SER A 146 ? 0.0408 0.2394 0.1000 0.0271 0.0280 -0.0136 146 SER A OG 1119 N N . ALA A 147 ? 0.0557 0.2428 0.0865 -0.0319 0.0307 -0.0587 147 ALA A N 1120 C CA . ALA A 147 ? 0.0623 0.2504 0.0861 -0.0025 0.0474 -0.0077 147 ALA A CA 1121 C C . ALA A 147 ? 0.0615 0.2017 0.1048 -0.0018 0.0506 -0.0412 147 ALA A C 1122 O O . ALA A 147 ? 0.0592 0.2568 0.1160 0.0674 0.0256 -0.0322 147 ALA A O 1123 C CB . ALA A 147 ? 0.1211 0.2623 0.1462 -0.0092 0.1021 -0.0630 147 ALA A CB 1124 N N . ASP A 148 ? 0.0387 0.2222 0.1175 0.0048 0.0336 -0.0279 148 ASP A N 1125 C CA . ASP A 148 ? 0.0592 0.2005 0.1193 0.0165 0.0446 -0.0153 148 ASP A CA 1126 C C . ASP A 148 ? 0.0677 0.2450 0.1134 0.0202 0.0411 -0.0444 148 ASP A C 1127 O O . ASP A 148 ? 0.0370 0.2409 0.1377 -0.0159 0.0360 -0.0329 148 ASP A O 1128 C CB . ASP A 148 ? 0.0434 0.2082 0.1214 0.0065 0.0397 -0.0253 148 ASP A CB 1129 C CG . ASP A 148 ? 0.0793 0.1580 0.2012 0.0397 0.0408 -0.0385 148 ASP A CG 1130 O OD1 . ASP A 148 ? 0.0749 0.1862 0.2247 0.0136 0.0547 -0.0685 148 ASP A OD1 1131 O OD2 . ASP A 148 ? 0.0665 0.2879 0.2583 0.0315 -0.0067 0.0095 148 ASP A OD2 1132 N N . CYS A 149 ? 0.0281 0.2348 0.0946 0.0244 -0.0030 -0.0263 149 CYS A N 1133 C CA . CYS A 149 ? 0.0605 0.2280 0.1483 -0.0040 0.0396 -0.0305 149 CYS A CA 1134 C C . CYS A 149 ? 0.0412 0.2126 0.1843 -0.0540 0.0203 -0.0453 149 CYS A C 1135 O O . CYS A 149 ? 0.0956 0.2916 0.1740 -0.0567 0.0497 -0.0380 149 CYS A O 1136 C CB . CYS A 149 ? 0.0367 0.2418 0.1478 -0.0078 0.0374 -0.0279 149 CYS A CB 1137 S SG . CYS A 149 ? 0.0685 0.2743 0.1377 -0.0210 0.0245 -0.0212 149 CYS A SG 1138 N N . THR A 150 ? 0.0456 0.2387 0.2039 -0.0655 0.0220 -0.0546 150 THR A N 1139 C CA . THR A 150 ? 0.0870 0.2678 0.2244 -0.0988 0.0392 -0.0705 150 THR A CA 1140 C C . THR A 150 ? 0.2038 0.2352 0.2166 -0.0792 0.0837 -0.0392 150 THR A C 1141 O O . THR A 150 ? 0.0544 0.2584 0.2274 -0.0403 0.0747 -0.0602 150 THR A O 1142 C CB . THR A 150 ? 0.0681 0.2864 0.2811 -0.0610 0.0100 -0.0746 150 THR A CB 1143 O OG1 . THR A 150 ? 0.0467 0.4664 0.2803 -0.0409 0.0235 -0.1057 150 THR A OG1 1144 C CG2 . THR A 150 ? 0.0850 0.3246 0.3873 -0.0433 -0.0320 -0.1258 150 THR A CG2 1145 N N . GLU A 151 ? 0.0822 0.3101 0.2191 -0.0334 0.0581 -0.0157 151 GLU A N 1146 C CA . GLU A 151 ? 0.1297 0.3267 0.2056 -0.0239 0.0743 -0.0620 151 GLU A CA 1147 C C . GLU A 151 ? 0.1331 0.2880 0.1924 -0.1009 0.1279 -0.0691 151 GLU A C 1148 O O . GLU A 151 ? 0.1499 0.3235 0.3948 -0.1349 0.1200 -0.0670 151 GLU A O 1149 C CB . GLU A 151 ? 0.2114 0.3995 0.2863 -0.0330 0.2203 -0.0471 151 GLU A CB 1150 C CG . GLU A 151 ? 0.5509 0.4157 0.5644 0.0000 0.1034 0.0686 151 GLU A CG 1151 C CD . GLU A 151 ? 0.7891 0.9993 0.3351 -0.1682 0.1737 0.1364 151 GLU A CD 1152 O OE1 . GLU A 151 ? 0.9618 0.7628 0.2148 -0.3114 0.0522 0.1380 151 GLU A OE1 1153 O OE2 . GLU A 151 ? 1.0141 0.8245 0.4780 -0.4112 -0.0884 0.1299 151 GLU A OE2 1154 N N . GLY A 152 ? 0.0885 0.3874 0.1700 -0.0243 0.0720 -0.0738 152 GLY A N 1155 C CA . GLY A 152 ? 0.2389 0.3196 0.1501 -0.1460 0.1019 -0.0366 152 GLY A CA 1156 C C . GLY A 152 ? 0.0772 0.3113 0.1824 -0.0482 0.0735 -0.0602 152 GLY A C 1157 O O . GLY A 152 ? 0.1855 0.3481 0.2721 -0.0750 -0.0554 -0.0964 152 GLY A O 1158 N N . GLU A 153 ? 0.1267 0.3026 0.2921 -0.0676 0.0600 -0.0561 153 GLU A N 1159 C CA . GLU A 153 ? 0.1157 0.3494 0.1861 -0.0552 0.0206 -0.0698 153 GLU A CA 1160 C C . GLU A 153 ? 0.0370 0.2759 0.1743 -0.0172 -0.0173 0.0070 153 GLU A C 1161 O O . GLU A 153 ? 0.0314 0.2782 0.1695 -0.0374 -0.0098 0.0061 153 GLU A O 1162 C CB . GLU A 153 ? 0.0608 0.3135 0.2179 -0.0678 0.0731 -0.0584 153 GLU A CB 1163 C CG . GLU A 153 ? 0.0841 0.4605 0.2186 0.0428 0.0352 -0.1079 153 GLU A CG 1164 C CD . GLU A 153 ? 0.0739 0.4534 0.5334 0.0157 0.1363 -0.1862 153 GLU A CD 1165 O OE1 . GLU A 153 ? 0.1380 0.6030 0.1975 -0.0478 -0.0042 -0.0368 153 GLU A OE1 1166 O OE2 . GLU A 153 ? 0.0589 0.5602 0.4436 0.0327 0.0224 -0.2213 153 GLU A OE2 1167 N N . ALA A 154 ? 0.0293 0.2764 0.1467 0.0050 -0.0220 -0.0362 154 ALA A N 1168 C CA . ALA A 154 ? 0.0519 0.2307 0.1279 -0.0221 -0.0173 -0.0399 154 ALA A CA 1169 C C . ALA A 154 ? 0.0253 0.2292 0.1845 0.0035 -0.0018 -0.0727 154 ALA A C 1170 O O . ALA A 154 ? 0.0441 0.3717 0.1790 0.0509 -0.0124 -0.1084 154 ALA A O 1171 C CB . ALA A 154 ? 0.0376 0.2940 0.1092 0.0320 -0.0198 -0.0585 154 ALA A CB 1172 N N . CYS A 155 ? 0.0364 0.2137 0.1375 0.0043 0.0112 -0.0363 155 CYS A N 1173 C CA . CYS A 155 ? 0.0290 0.2230 0.1277 0.0231 -0.0107 -0.0059 155 CYS A CA 1174 C C . CYS A 155 ? 0.0297 0.2055 0.1059 -0.0142 0.0154 0.0110 155 CYS A C 1175 O O . CYS A 155 ? 0.0356 0.2462 0.1713 -0.0244 0.0007 -0.0352 155 CYS A O 1176 C CB . CYS A 155 ? 0.0289 0.2368 0.1225 -0.0230 -0.0071 -0.0270 155 CYS A CB 1177 S SG . CYS A 155 ? 0.0549 0.2581 0.1546 0.0209 0.0142 -0.0244 155 CYS A SG 1178 N N . TRP A 156 ? 0.0712 0.2027 0.1307 -0.0395 0.0140 -0.0072 156 TRP A N 1179 C CA . TRP A 156 ? 0.0477 0.1957 0.1225 -0.0033 0.0270 -0.0280 156 TRP A CA 1180 C C . TRP A 156 ? 0.0333 0.2062 0.1013 -0.0042 0.0148 -0.0427 156 TRP A C 1181 O O . TRP A 156 ? 0.0499 0.1919 0.1288 0.0080 0.0231 -0.0207 156 TRP A O 1182 C CB . TRP A 156 ? 0.1108 0.2321 0.1283 -0.0083 0.0813 -0.0010 156 TRP A CB 1183 C CG . TRP A 156 ? 0.0363 0.2577 0.1446 -0.0299 0.0299 -0.0064 156 TRP A CG 1184 C CD1 . TRP A 156 ? 0.1193 0.2524 0.1774 -0.0291 0.0495 -0.0385 156 TRP A CD1 1185 C CD2 . TRP A 156 ? 0.1486 0.2912 0.1378 -0.0225 0.0196 -0.0145 156 TRP A CD2 1186 N NE1 . TRP A 156 ? 0.1714 0.2742 0.1954 -0.0492 0.0379 -0.0014 156 TRP A NE1 1187 C CE2 . TRP A 156 ? 0.2264 0.2904 0.2008 -0.0889 0.0263 -0.0089 156 TRP A CE2 1188 C CE3 . TRP A 156 ? 0.1177 0.2775 0.1008 -0.0160 0.0051 -0.0230 156 TRP A CE3 1189 C CZ2 . TRP A 156 ? 0.1332 0.4068 0.1909 -0.0105 0.0001 -0.0111 156 TRP A CZ2 1190 C CZ3 . TRP A 156 ? 0.1004 0.2636 0.1263 -0.0098 -0.0100 -0.0508 156 TRP A CZ3 1191 C CH2 . TRP A 156 ? 0.2215 0.3687 0.1738 -0.0340 0.0007 0.0197 156 TRP A CH2 1192 N N . ARG A 157 ? 0.0397 0.1793 0.1320 -0.0136 0.0078 -0.0218 157 ARG A N 1193 C CA . ARG A 157 ? 0.0264 0.1614 0.1374 -0.0072 -0.0081 -0.0148 157 ARG A CA 1194 C C . ARG A 157 ? 0.0383 0.1960 0.1199 -0.0119 -0.0348 0.0172 157 ARG A C 1195 O O . ARG A 157 ? 0.0325 0.2011 0.2323 0.0187 -0.0180 0.0269 157 ARG A O 1196 C CB . ARG A 157 ? 0.0505 0.2277 0.1251 -0.0076 0.0500 -0.0030 157 ARG A CB 1197 C CG . ARG A 157 ? 0.0480 0.2226 0.1043 -0.0223 -0.0102 -0.0228 157 ARG A CG 1198 C CD . ARG A 157 ? 0.0552 0.2551 0.0994 -0.0423 -0.0026 0.0348 157 ARG A CD 1199 N NE . ARG A 157 ? 0.0866 0.2263 0.1216 -0.0416 0.0080 -0.0041 157 ARG A NE 1200 C CZ . ARG A 157 ? 0.0286 0.2115 0.1199 -0.0157 -0.0119 -0.0203 157 ARG A CZ 1201 N NH1 . ARG A 157 ? 0.0628 0.2831 0.1567 0.0141 0.0163 -0.0271 157 ARG A NH1 1202 N NH2 . ARG A 157 ? 0.0349 0.2872 0.1133 0.0265 -0.0039 -0.0310 157 ARG A NH2 1203 N N . ASN A 158 ? 0.0365 0.1647 0.1160 -0.0063 0.0268 0.0133 158 ASN A N 1204 C CA . ASN A 158 ? 0.0411 0.1861 0.1053 -0.0199 0.0297 0.0197 158 ASN A CA 1205 C C . ASN A 158 ? 0.0371 0.1769 0.0892 -0.0061 0.0148 0.0164 158 ASN A C 1206 O O . ASN A 158 ? 0.0520 0.2272 0.1363 0.0014 -0.0061 0.0164 158 ASN A O 1207 C CB . ASN A 158 ? 0.0262 0.2028 0.1224 -0.0108 0.0032 0.0287 158 ASN A CB 1208 C CG . ASN A 158 ? 0.0506 0.1854 0.1013 -0.0341 0.0015 0.0137 158 ASN A CG 1209 O OD1 . ASN A 158 ? 0.0308 0.1768 0.1385 -0.0133 -0.0021 0.0012 158 ASN A OD1 1210 N ND2 . ASN A 158 ? 0.0726 0.2219 0.0828 -0.0015 0.0148 -0.0077 158 ASN A ND2 1211 N N . ASP A 159 ? 0.0273 0.1750 0.0919 0.0062 0.0112 0.0158 159 ASP A N 1212 C CA . ASP A 159 ? 0.0717 0.1880 0.0795 0.0321 0.0229 0.0423 159 ASP A CA 1213 C C . ASP A 159 ? 0.0321 0.1848 0.1135 0.0112 -0.0041 0.0274 159 ASP A C 1214 O O . ASP A 159 ? 0.0364 0.1969 0.1297 0.0174 0.0318 0.0057 159 ASP A O 1215 C CB . ASP A 159 ? 0.0515 0.1819 0.1119 0.0350 0.0294 0.0182 159 ASP A CB 1216 C CG . ASP A 159 ? 0.0273 0.1413 0.1105 -0.0124 0.0101 -0.0242 159 ASP A CG 1217 O OD1 . ASP A 159 ? 0.0379 0.1832 0.1379 0.0306 0.0255 -0.0090 159 ASP A OD1 1218 O OD2 . ASP A 159 ? 0.0651 0.2536 0.1159 -0.0276 -0.0299 -0.0151 159 ASP A OD2 1219 N N . TRP A 160 ? 0.0253 0.1575 0.1430 -0.0014 -0.0017 -0.0163 160 TRP A N 1220 C CA . TRP A 160 ? 0.0365 0.1579 0.1260 0.0049 0.0317 -0.0232 160 TRP A CA 1221 C C . TRP A 160 ? 0.0368 0.1764 0.1230 -0.0122 0.0312 0.0010 160 TRP A C 1222 O O . TRP A 160 ? 0.0517 0.2048 0.0991 -0.0121 0.0178 -0.0078 160 TRP A O 1223 C CB . TRP A 160 ? 0.0484 0.1999 0.1161 0.0204 0.0087 0.0000 160 TRP A CB 1224 C CG . TRP A 160 ? 0.0412 0.1730 0.0992 0.0167 0.0333 0.0119 160 TRP A CG 1225 C CD1 . TRP A 160 ? 0.0319 0.1484 0.1156 -0.0097 0.0203 0.0246 160 TRP A CD1 1226 C CD2 . TRP A 160 ? 0.0257 0.1579 0.0689 -0.0033 -0.0039 -0.0057 160 TRP A CD2 1227 N NE1 . TRP A 160 ? 0.0375 0.1813 0.0914 -0.0272 0.0235 -0.0079 160 TRP A NE1 1228 C CE2 . TRP A 160 ? 0.0283 0.1723 0.0711 -0.0188 -0.0056 0.0027 160 TRP A CE2 1229 C CE3 . TRP A 160 ? 0.0370 0.1711 0.1056 -0.0204 -0.0250 -0.0103 160 TRP A CE3 1230 C CZ2 . TRP A 160 ? 0.0504 0.1833 0.1211 -0.0446 -0.0408 0.0242 160 TRP A CZ2 1231 C CZ3 . TRP A 160 ? 0.0406 0.1523 0.1488 0.0012 -0.0333 -0.0153 160 TRP A CZ3 1232 C CH2 . TRP A 160 ? 0.0538 0.1752 0.1228 0.0162 -0.0457 0.0322 160 TRP A CH2 1233 N N . PHE A 161 ? 0.0328 0.1586 0.0979 -0.0094 0.0233 -0.0259 161 PHE A N 1234 C CA . PHE A 161 ? 0.0302 0.1764 0.1079 -0.0229 0.0125 -0.0135 161 PHE A CA 1235 C C . PHE A 161 ? 0.0578 0.1740 0.0467 0.0029 0.0150 0.0240 161 PHE A C 1236 O O . PHE A 161 ? 0.0257 0.1928 0.0705 0.0080 -0.0010 0.0000 161 PHE A O 1237 C CB . PHE A 161 ? 0.0299 0.1481 0.1173 -0.0066 0.0176 0.0269 161 PHE A CB 1238 C CG . PHE A 161 ? 0.0390 0.1814 0.1190 0.0101 0.0071 0.0031 161 PHE A CG 1239 C CD1 . PHE A 161 ? 0.0595 0.1816 0.1014 0.0030 0.0117 0.0100 161 PHE A CD1 1240 C CD2 . PHE A 161 ? 0.0416 0.2060 0.1061 0.0284 -0.0145 0.0372 161 PHE A CD2 1241 C CE1 . PHE A 161 ? 0.0279 0.2049 0.0659 -0.0037 -0.0100 -0.0036 161 PHE A CE1 1242 C CE2 . PHE A 161 ? 0.0407 0.2027 0.1145 0.0071 0.0366 0.0360 161 PHE A CE2 1243 C CZ . PHE A 161 ? 0.0570 0.1757 0.0777 0.0081 0.0141 -0.0213 161 PHE A CZ 1244 N N . THR A 162 ? 0.0463 0.1870 0.0527 0.0147 0.0237 0.0082 162 THR A N 1245 C CA . THR A 162 ? 0.0332 0.1940 0.0669 0.0171 0.0161 0.0003 162 THR A CA 1246 C C . THR A 162 ? 0.0302 0.1874 0.0707 0.0122 0.0141 0.0090 162 THR A C 1247 O O . THR A 162 ? 0.0303 0.2317 0.1199 0.0035 -0.0215 -0.0349 162 THR A O 1248 C CB . THR A 162 ? 0.0445 0.2369 0.1469 0.0134 0.0431 0.0309 162 THR A CB 1249 O OG1 . THR A 162 ? 0.0313 0.2571 0.1243 0.0045 0.0239 -0.0090 162 THR A OG1 1250 C CG2 . THR A 162 ? 0.1452 0.2049 0.1430 0.0521 0.1064 0.0414 162 THR A CG2 1251 N N . CYS A 163 ? 0.0270 0.1709 0.0998 0.0000 -0.0113 0.0065 163 CYS A N 1252 C CA . CYS A 163 ? 0.0436 0.1940 0.1342 -0.0297 0.0386 -0.0055 163 CYS A CA 1253 C C . CYS A 163 ? 0.0615 0.2144 0.0859 -0.0023 0.0063 -0.0045 163 CYS A C 1254 O O . CYS A 163 ? 0.0270 0.2275 0.1283 0.0111 0.0094 -0.0172 163 CYS A O 1255 C CB . CYS A 163 ? 0.0309 0.2221 0.1132 -0.0074 0.0215 0.0054 163 CYS A CB 1256 S SG . CYS A 163 ? 0.0586 0.2276 0.1056 0.0031 0.0305 -0.0040 163 CYS A SG 1257 N N . ASN A 164 ? 0.0400 0.2421 0.0713 0.0020 -0.0099 0.0116 164 ASN A N 1258 C CA . ASN A 164 ? 0.0491 0.1919 0.0675 -0.0256 -0.0068 0.0124 164 ASN A CA 1259 C C . ASN A 164 ? 0.0548 0.2616 0.1008 -0.0036 0.0442 0.0091 164 ASN A C 1260 O O . ASN A 164 ? 0.0384 0.2155 0.1090 -0.0371 0.0252 -0.0225 164 ASN A O 1261 C CB . ASN A 164 ? 0.0561 0.2266 0.0585 -0.0085 -0.0127 0.0072 164 ASN A CB 1262 C CG . ASN A 164 ? 0.0648 0.2178 0.0959 0.0075 0.0163 -0.0126 164 ASN A CG 1263 O OD1 . ASN A 164 ? 0.1505 0.2273 0.1698 0.0445 0.0075 -0.0424 164 ASN A OD1 1264 N ND2 . ASN A 164 ? 0.0432 0.2806 0.1796 -0.0077 -0.0092 0.0106 164 ASN A ND2 1265 N N A GLY A 165 ? 0.0526 0.2407 0.1082 -0.0090 0.0466 0.0108 165 GLY A N 1266 N N B GLY A 165 ? 0.0530 0.2136 0.1076 -0.0127 0.0471 -0.0025 165 GLY A N 1267 C CA A GLY A 165 ? 0.0732 0.2804 0.1130 0.0249 0.0564 0.0617 165 GLY A CA 1268 C CA B GLY A 165 ? 0.0765 0.2355 0.1332 0.0167 0.0698 0.0204 165 GLY A CA 1269 C C A GLY A 165 ? 0.0589 0.2840 0.1642 -0.0022 0.0665 0.0384 165 GLY A C 1270 C C B GLY A 165 ? 0.1011 0.2532 0.1726 -0.0254 0.0670 -0.0181 165 GLY A C 1271 O O A GLY A 165 ? 0.1278 0.3167 0.1507 0.0035 0.0741 -0.0508 165 GLY A O 1272 O O B GLY A 165 ? 0.1211 0.2721 0.1797 -0.0526 0.0947 -0.0586 165 GLY A O 1273 N N A PHE A 166 ? 0.0476 0.3387 0.2287 0.0148 0.0626 0.0620 166 PHE A N 1274 N N B PHE A 166 ? 0.1571 0.2587 0.3240 0.0822 0.1644 -0.0279 166 PHE A N 1275 C CA A PHE A 166 ? 0.0821 0.3666 0.0400 -0.0053 -0.0089 0.0681 166 PHE A CA 1276 C CA B PHE A 166 ? 0.2699 0.2801 0.3161 -0.1018 0.1854 -0.1201 166 PHE A CA 1277 C C A PHE A 166 ? 0.1551 0.3354 0.0781 -0.0728 0.0609 0.0432 166 PHE A C 1278 C C B PHE A 166 ? 0.5527 0.2321 0.3505 -0.1601 0.1585 -0.1019 166 PHE A C 1279 O O A PHE A 166 ? 0.2198 0.3396 0.2044 -0.0579 0.0324 0.0216 166 PHE A O 1280 O O B PHE A 166 ? 0.5229 1.0044 0.8440 -0.6921 0.6065 -0.8074 166 PHE A O 1281 C CB A PHE A 166 ? 0.0598 0.3949 0.0886 -0.1110 -0.0356 0.1326 166 PHE A CB 1282 C CB B PHE A 166 ? 0.4509 0.2748 0.3217 0.0943 0.1799 -0.1459 166 PHE A CB 1283 C CG A PHE A 166 ? 0.0410 0.3846 0.0679 0.0316 -0.0135 0.0683 166 PHE A CG 1284 C CG B PHE A 166 ? 0.1483 0.4063 0.4994 0.0345 0.2092 0.0272 166 PHE A CG 1285 C CD1 A PHE A 166 ? 0.0342 0.4559 0.0724 0.0279 -0.0115 0.0687 166 PHE A CD1 1286 C CD1 B PHE A 166 ? 0.4012 0.5068 0.4739 0.1532 0.2196 0.0509 166 PHE A CD1 1287 C CD2 A PHE A 166 ? 0.2493 0.2841 0.2086 0.0773 -0.0377 0.0041 166 PHE A CD2 1288 C CD2 B PHE A 166 ? 0.3732 0.4096 0.3708 0.0391 0.2695 0.0773 166 PHE A CD2 1289 C CE1 A PHE A 166 ? 0.0509 0.3207 0.1302 -0.0001 -0.0424 -0.1007 166 PHE A CE1 1290 C CE1 B PHE A 166 ? 0.6788 0.5971 0.4631 0.1766 0.3986 0.0098 166 PHE A CE1 1291 C CE2 A PHE A 166 ? 0.3113 0.3446 0.2099 -0.0265 0.0063 0.0911 166 PHE A CE2 1292 C CE2 B PHE A 166 ? 0.3106 0.3815 0.2994 0.2727 0.1920 0.0930 166 PHE A CE2 1293 C CZ A PHE A 166 ? 0.1679 0.3283 0.1862 0.1127 -0.0245 0.0470 166 PHE A CZ 1294 C CZ B PHE A 166 ? 0.5323 0.6029 0.4297 0.3266 0.1877 -0.1090 166 PHE A CZ 1295 N N A GLU A 167 ? 0.3761 0.4079 0.1210 -0.0246 0.0584 0.1386 167 GLU A N 1296 N N B GLU A 167 ? 0.4308 0.3354 0.3423 -0.2177 0.3571 -0.1701 167 GLU A N 1297 C CA A GLU A 167 ? 0.4196 0.5504 0.2018 -0.1157 0.0252 -0.0720 167 GLU A CA 1298 C CA B GLU A 167 ? 0.3532 0.3404 0.2958 -0.1800 0.0732 0.1583 167 GLU A CA 1299 C C A GLU A 167 ? 0.2473 0.3938 0.4140 -0.1481 0.0939 0.0537 167 GLU A C 1300 C C B GLU A 167 ? 0.5541 0.5603 0.2035 -0.0452 -0.0096 0.1143 167 GLU A C 1301 O O A GLU A 167 ? 0.0833 0.5595 0.7795 -0.0696 -0.1387 -0.0486 167 GLU A O 1302 O O B GLU A 167 ? 0.3674 0.4020 0.2382 -0.0605 0.0156 -0.1178 167 GLU A O 1303 C CB A GLU A 167 ? 0.2556 0.5415 0.1459 -0.0685 0.1512 0.0575 167 GLU A CB 1304 C CB B GLU A 167 ? 0.3467 0.3851 0.0412 -0.1846 0.0473 0.0204 167 GLU A CB 1305 C CG A GLU A 167 ? 0.5480 0.5300 0.2117 -0.0336 -0.0659 0.0595 167 GLU A CG 1306 C CG B GLU A 167 ? 0.1572 0.6234 0.1513 -0.2808 0.0004 0.0014 167 GLU A CG 1307 C CD A GLU A 167 ? 0.4573 0.5088 0.5271 -0.1069 0.1102 -0.1091 167 GLU A CD 1308 C CD B GLU A 167 ? 0.0463 0.7188 0.3076 -0.1032 0.0026 0.0514 167 GLU A CD 1309 O OE1 A GLU A 167 ? 0.4831 0.2383 0.4818 -0.1020 0.0775 -0.0463 167 GLU A OE1 1310 O OE1 B GLU A 167 ? 0.2291 0.8577 0.4358 -0.2684 -0.0314 0.1946 167 GLU A OE1 1311 O OE2 A GLU A 167 ? 0.8453 0.4372 0.4407 0.0568 -0.1233 -0.0314 167 GLU A OE2 1312 O OE2 B GLU A 167 ? 0.1889 0.9954 0.2720 -0.3275 0.0545 0.1573 167 GLU A OE2 1313 N N A ALA A 168 ? 0.4583 0.3969 0.6324 -0.0488 0.0091 0.0545 168 ALA A N 1314 N N B ALA A 168 ? 0.2200 0.5370 0.3554 -0.1114 -0.0979 0.2813 168 ALA A N 1315 C CA A ALA A 168 ? 0.4226 0.4354 0.3776 -0.1637 -0.0209 0.1365 168 ALA A CA 1316 C CA B ALA A 168 ? 0.1132 0.6626 0.4716 -0.0506 0.0809 0.1069 168 ALA A CA 1317 C C A ALA A 168 ? 0.2571 0.4195 0.2690 -0.2199 0.0907 0.1010 168 ALA A C 1318 C C B ALA A 168 ? 0.0940 0.6878 0.6758 -0.1849 0.0752 0.1034 168 ALA A C 1319 O O A ALA A 168 ? 0.2387 0.6967 0.4186 -0.1811 0.0037 0.4148 168 ALA A O 1320 O O B ALA A 168 ? 0.3747 0.7380 0.5553 -0.3107 -0.4173 0.2539 168 ALA A O 1321 C CB A ALA A 168 ? 0.4339 0.3963 0.0680 0.0553 -0.0023 0.1230 168 ALA A CB 1322 C CB B ALA A 168 ? 0.2178 0.7172 0.6642 -0.1263 0.2459 0.0315 168 ALA A CB 1335 N N A ASP A 170 ? 0.0990 0.8284 0.3082 0.1526 0.1029 0.4477 170 ASP A N 1336 N N B ASP A 170 ? 0.4303 1.5494 0.0648 0.1916 0.0497 -0.1953 170 ASP A N 1337 C CA A ASP A 170 ? 0.3316 0.9493 0.6298 0.0717 -0.2156 0.3759 170 ASP A CA 1338 C CA B ASP A 170 ? 0.5000 1.1375 0.1689 0.1974 -0.2085 -0.2871 170 ASP A CA 1339 C C A ASP A 170 ? 0.4722 0.9368 0.2986 0.1166 -0.0215 0.3415 170 ASP A C 1340 C C B ASP A 170 ? 0.4494 0.7449 0.2622 0.1706 -0.1068 -0.0881 170 ASP A C 1341 O O A ASP A 170 ? 0.7744 1.3594 0.3792 -0.0170 -0.2256 0.2561 170 ASP A O 1342 O O B ASP A 170 ? 0.4803 0.5311 0.6294 0.1072 -0.3510 -0.1650 170 ASP A O 1343 C CB A ASP A 170 ? 0.0368 0.8426 0.7075 -0.0408 0.0516 0.3660 170 ASP A CB 1344 C CB B ASP A 170 ? 0.3424 1.4623 0.2985 0.2263 -0.2410 -0.0358 170 ASP A CB 1345 C CG A ASP A 170 ? 0.1291 0.9722 0.6260 -0.0750 0.0366 0.4511 170 ASP A CG 1346 C CG B ASP A 170 ? 1.0845 1.5833 0.3548 0.2362 -0.1008 0.1156 170 ASP A CG 1347 O OD1 A ASP A 170 ? 0.0253 1.1359 0.8159 -0.0018 -0.0032 0.2646 170 ASP A OD1 1348 O OD1 B ASP A 170 ? 1.5512 1.7765 0.0471 0.2462 0.0872 0.0706 170 ASP A OD1 1349 O OD2 A ASP A 170 ? 0.6345 0.6866 0.6565 -0.1240 -0.0284 0.3317 170 ASP A OD2 1350 O OD2 B ASP A 170 ? 1.4491 1.7575 0.3714 0.5543 0.3484 -0.4933 170 ASP A OD2 1351 N N A ARG A 171 ? 0.3287 0.6428 0.1809 0.1303 -0.1474 -0.1123 171 ARG A N 1352 N N B ARG A 171 ? 0.4210 0.6073 0.0286 0.1993 -0.0335 -0.0013 171 ARG A N 1353 C CA A ARG A 171 ? 0.2701 0.4868 0.1715 0.0617 -0.0922 -0.0102 171 ARG A CA 1354 C CA B ARG A 171 ? 0.1690 0.4041 0.0987 0.0958 -0.0322 -0.0538 171 ARG A CA 1355 C C A ARG A 171 ? 0.2027 0.2953 0.1445 0.0632 -0.0357 -0.0375 171 ARG A C 1356 C C B ARG A 171 ? 0.1753 0.3033 0.0912 0.0624 -0.0247 -0.0452 171 ARG A C 1357 O O A ARG A 171 ? 0.1283 0.3167 0.1215 -0.0065 0.0020 -0.0395 171 ARG A O 1358 O O B ARG A 171 ? 0.1433 0.3172 0.1297 0.0017 -0.0090 -0.0671 171 ARG A O 1359 C CB A ARG A 171 ? 0.2333 0.4872 0.1087 0.0434 -0.0484 0.0376 171 ARG A CB 1360 C CB B ARG A 171 ? 0.1931 0.4212 0.0662 0.0953 -0.0216 0.0223 171 ARG A CB 1361 C CG A ARG A 171 ? 0.2598 0.6245 0.1647 0.1114 -0.0894 0.0146 171 ARG A CG 1362 C CG B ARG A 171 ? 0.2270 0.5822 0.1587 0.1223 -0.0782 0.0035 171 ARG A CG 1363 C CD A ARG A 171 ? 0.2095 0.6288 0.1814 0.1236 0.0221 0.0571 171 ARG A CD 1364 C CD B ARG A 171 ? 0.1832 0.5958 0.1671 0.1339 0.0608 0.0723 171 ARG A CD 1365 N NE A ARG A 171 ? 0.0874 0.5997 0.1878 0.1357 -0.0684 0.0056 171 ARG A NE 1366 N NE B ARG A 171 ? 0.0869 0.5999 0.1506 0.1458 -0.0538 0.0062 171 ARG A NE 1367 C CZ A ARG A 171 ? 0.1049 0.3591 0.1494 0.0884 -0.0235 0.0534 171 ARG A CZ 1368 C CZ B ARG A 171 ? 0.0986 0.3767 0.1787 0.0999 -0.0091 0.0361 171 ARG A CZ 1369 N NH1 A ARG A 171 ? 0.2736 0.3377 0.1598 0.0025 0.0285 0.0452 171 ARG A NH1 1370 N NH1 B ARG A 171 ? 0.2697 0.5231 0.1715 0.0580 -0.0625 0.0539 171 ARG A NH1 1371 N NH2 A ARG A 171 ? 0.2661 0.4671 0.1687 0.0662 -0.0800 0.0980 171 ARG A NH2 1372 N NH2 B ARG A 171 ? 0.2894 0.3754 0.1696 0.0122 0.0275 0.0303 171 ARG A NH2 1373 N N . PRO A 172 ? 0.2502 0.3382 0.1455 0.1140 -0.1151 -0.0872 172 PRO A N 1374 C CA . PRO A 172 ? 0.1828 0.3576 0.0987 0.0769 -0.0598 -0.0838 172 PRO A CA 1375 C C . PRO A 172 ? 0.1444 0.2298 0.1221 0.0286 -0.0324 0.0043 172 PRO A C 1376 O O . PRO A 172 ? 0.1014 0.2853 0.1935 -0.0078 -0.0404 -0.0284 172 PRO A O 1377 C CB . PRO A 172 ? 0.3089 0.3702 0.3245 0.1051 -0.0536 -0.0970 172 PRO A CB 1378 C CG . PRO A 172 ? 0.4018 0.3375 0.5519 0.1020 -0.1399 -0.1350 172 PRO A CG 1379 C CD . PRO A 172 ? 0.5170 0.3757 0.1807 0.0652 -0.1409 -0.1660 172 PRO A CD 1380 N N . LYS A 173 ? 0.1226 0.2378 0.1048 -0.0299 0.0288 -0.0224 173 LYS A N 1381 C CA . LYS A 173 ? 0.0685 0.2654 0.0952 -0.0464 0.0126 -0.0178 173 LYS A CA 1382 C C . LYS A 173 ? 0.0459 0.2299 0.0854 -0.0567 -0.0107 -0.0216 173 LYS A C 1383 O O . LYS A 173 ? 0.0868 0.2660 0.1031 -0.0222 0.0269 0.0072 173 LYS A O 1384 C CB . LYS A 173 ? 0.0699 0.2956 0.1091 0.0325 0.0547 0.0335 173 LYS A CB 1385 C CG . LYS A 173 ? 0.1248 0.3934 0.2017 0.1374 0.0728 0.0611 173 LYS A CG 1386 C CD . LYS A 173 ? 0.2992 0.2978 0.2261 0.1007 0.0832 0.0033 173 LYS A CD 1387 C CE . LYS A 173 ? 0.1112 0.4187 0.2805 0.0286 0.0903 -0.1749 173 LYS A CE 1388 N NZ . LYS A 173 ? 0.0705 0.5746 1.0873 0.1157 0.1216 -0.1206 173 LYS A NZ 1389 N N . CYS A 174 ? 0.0290 0.2121 0.0943 -0.0145 0.0147 -0.0230 174 CYS A N 1390 C CA . CYS A 174 ? 0.0258 0.2050 0.1108 -0.0035 0.0065 -0.0218 174 CYS A CA 1391 C C . CYS A 174 ? 0.0405 0.2225 0.0942 -0.0249 0.0055 -0.0256 174 CYS A C 1392 O O . CYS A 174 ? 0.0558 0.2366 0.0823 -0.0012 0.0192 -0.0255 174 CYS A O 1393 C CB . CYS A 174 ? 0.0260 0.2344 0.1102 -0.0113 0.0023 0.0065 174 CYS A CB 1394 S SG . CYS A 174 ? 0.0259 0.2751 0.1010 -0.0078 0.0060 -0.0166 174 CYS A SG 1395 N N . GLN A 175 ? 0.0266 0.2028 0.1212 -0.0154 0.0016 -0.0119 175 GLN A N 1396 C CA . GLN A 175 ? 0.0560 0.2038 0.1186 -0.0370 -0.0214 0.0047 175 GLN A CA 1397 C C . GLN A 175 ? 0.0384 0.2342 0.0857 -0.0211 -0.0243 -0.0127 175 GLN A C 1398 O O . GLN A 175 ? 0.0529 0.2287 0.1077 -0.0019 -0.0458 -0.0327 175 GLN A O 1399 C CB . GLN A 175 ? 0.0603 0.2273 0.0884 -0.0369 -0.0118 0.0070 175 GLN A CB 1400 C CG . GLN A 175 ? 0.0863 0.2505 0.1186 -0.0176 -0.0385 -0.0500 175 GLN A CG 1401 C CD . GLN A 175 ? 0.1090 0.2220 0.1053 -0.0209 -0.0065 -0.0799 175 GLN A CD 1402 O OE1 . GLN A 175 ? 0.1230 0.2888 0.1480 -0.0002 0.0140 -0.0343 175 GLN A OE1 1403 N NE2 . GLN A 175 ? 0.0987 0.2839 0.1389 -0.0421 -0.0045 -0.0377 175 GLN A NE2 1404 N N . GLY A 176 ? 0.0263 0.2705 0.1191 0.0053 0.0019 -0.0059 176 GLY A N 1405 C CA . GLY A 176 ? 0.0944 0.2573 0.1581 0.0202 0.0277 0.0266 176 GLY A CA 1406 C C . GLY A 176 ? 0.0733 0.2552 0.1091 0.0044 -0.0063 -0.0068 176 GLY A C 1407 O O . GLY A 176 ? 0.0655 0.3003 0.1250 0.0028 -0.0285 -0.0011 176 GLY A O 1408 N N . VAL A 177 ? 0.0680 0.2148 0.1215 0.0008 -0.0092 -0.0288 177 VAL A N 1409 C CA . VAL A 177 ? 0.0286 0.2426 0.1257 -0.0224 -0.0099 -0.0011 177 VAL A CA 1410 C C . VAL A 177 ? 0.0371 0.2009 0.1120 -0.0084 -0.0243 -0.0034 177 VAL A C 1411 O O . VAL A 177 ? 0.0536 0.2457 0.1591 0.0035 -0.0372 0.0269 177 VAL A O 1412 C CB . VAL A 177 ? 0.0746 0.2010 0.1426 -0.0588 -0.0520 -0.0188 177 VAL A CB 1413 C CG1 . VAL A 177 ? 0.1489 0.2338 0.1766 -0.0602 0.0160 -0.0915 177 VAL A CG1 1414 C CG2 . VAL A 177 ? 0.0654 0.2009 0.1367 -0.0406 -0.0334 0.0193 177 VAL A CG2 1415 N N . ASP A 178 ? 0.0615 0.2584 0.0893 -0.0170 -0.0191 0.0180 178 ASP A N 1416 C CA . ASP A 178 ? 0.0771 0.2735 0.0994 0.0432 -0.0567 0.0028 178 ASP A CA 1417 C C . ASP A 178 ? 0.0938 0.2706 0.0635 0.0614 -0.0343 0.0324 178 ASP A C 1418 O O . ASP A 178 ? 0.0511 0.2603 0.1268 0.0485 -0.0381 0.0086 178 ASP A O 1419 C CB . ASP A 178 ? 0.1274 0.2268 0.0638 0.0349 -0.0410 -0.0182 178 ASP A CB 1420 C CG . ASP A 178 ? 0.0876 0.1914 0.0962 0.0016 -0.0292 -0.0210 178 ASP A CG 1421 O OD1 . ASP A 178 ? 0.1055 0.1910 0.1085 -0.0031 -0.0381 -0.0207 178 ASP A OD1 1422 O OD2 . ASP A 178 ? 0.0812 0.2451 0.1361 0.0055 -0.0106 0.0162 178 ASP A OD2 1423 N N . ASN A 179 ? 0.0688 0.2438 0.1494 0.0214 -0.0344 -0.0199 179 ASN A N 1424 C CA . ASN A 179 ? 0.0594 0.2917 0.1256 0.0040 -0.0575 -0.0149 179 ASN A CA 1425 C C . ASN A 179 ? 0.0584 0.2510 0.0803 0.0157 -0.0334 -0.0458 179 ASN A C 1426 O O . ASN A 179 ? 0.1386 0.3424 0.1333 -0.0051 -0.1053 -0.0183 179 ASN A O 1427 C CB . ASN A 179 ? 0.1038 0.3202 0.1253 -0.0088 -0.0632 -0.0151 179 ASN A CB 1428 C CG . ASN A 179 ? 0.2102 0.3932 0.1428 0.0698 -0.0281 -0.0607 179 ASN A CG 1429 O OD1 . ASN A 179 ? 0.2234 0.3918 0.1907 0.0883 -0.0302 -0.0834 179 ASN A OD1 1430 N ND2 . ASN A 179 ? 0.3500 0.4606 0.1333 0.1253 -0.0262 -0.0605 179 ASN A ND2 1431 N N . ALA A 180 ? 0.0705 0.2773 0.1009 0.0384 -0.0067 -0.0275 180 ALA A N 1432 C CA . ALA A 180 ? 0.0846 0.2706 0.1058 0.0093 -0.0396 -0.0076 180 ALA A CA 1433 C C . ALA A 180 ? 0.1000 0.2845 0.0811 0.0074 -0.0027 -0.0337 180 ALA A C 1434 O O . ALA A 180 ? 0.0627 0.2988 0.1598 -0.0109 -0.0636 -0.0425 180 ALA A O 1435 C CB . ALA A 180 ? 0.1372 0.3073 0.1281 -0.0836 -0.0123 -0.0386 180 ALA A CB 1436 N N . GLU A 181 ? 0.1035 0.2787 0.1980 -0.0222 -0.1114 -0.0271 181 GLU A N 1437 C CA . GLU A 181 ? 0.1218 0.2777 0.1849 0.0146 -0.0655 -0.0028 181 GLU A CA 1438 C C . GLU A 181 ? 0.0770 0.2348 0.1596 -0.0493 -0.0653 -0.0292 181 GLU A C 1439 O O . GLU A 181 ? 0.0757 0.2378 0.1632 0.0078 -0.0429 -0.0281 181 GLU A O 1440 C CB . GLU A 181 ? 0.0734 0.3318 0.3293 0.0209 -0.0323 0.0115 181 GLU A CB 1441 C CG . GLU A 181 ? 0.2364 0.4354 0.4117 0.1454 0.0602 -0.0431 181 GLU A CG 1442 C CD . GLU A 181 ? 0.4890 0.5081 0.8231 0.4351 -0.3005 -0.3035 181 GLU A CD 1443 O OE1 . GLU A 181 ? 0.8862 2.4880 3.9420 0.6361 -0.9452 -2.6086 181 GLU A OE1 1444 O OE2 . GLU A 181 ? 0.5211 0.3986 2.0640 0.1994 0.6632 -0.1409 181 GLU A OE2 1445 N N . LEU A 182 ? 0.0744 0.2131 0.1420 -0.0247 -0.0671 -0.0321 182 LEU A N 1446 C CA . LEU A 182 ? 0.1050 0.2397 0.1693 0.0191 -0.0095 -0.0023 182 LEU A CA 1447 C C . LEU A 182 ? 0.0525 0.2533 0.1441 -0.0121 -0.0548 -0.0018 182 LEU A C 1448 O O . LEU A 182 ? 0.0463 0.2811 0.1635 -0.0345 -0.0455 -0.0134 182 LEU A O 1449 C CB . LEU A 182 ? 0.1054 0.2705 0.1119 -0.0110 -0.0408 -0.0368 182 LEU A CB 1450 C CG . LEU A 182 ? 0.1496 0.2568 0.1078 -0.0140 -0.0476 -0.0441 182 LEU A CG 1451 C CD1 . LEU A 182 ? 0.0981 0.2496 0.1402 0.0120 -0.0506 0.0015 182 LEU A CD1 1452 C CD2 . LEU A 182 ? 0.3425 0.3035 0.1707 0.0085 -0.0084 -0.0670 182 LEU A CD2 1453 N N . ASN A 183 ? 0.1190 0.2690 0.1222 -0.0415 -0.0099 -0.0132 183 ASN A N 1454 C CA . ASN A 183 ? 0.0887 0.2345 0.1117 -0.0360 -0.0208 -0.0581 183 ASN A CA 1455 C C . ASN A 183 ? 0.0642 0.2709 0.1285 -0.0464 -0.0531 -0.0038 183 ASN A C 1456 O O . ASN A 183 ? 0.0835 0.3275 0.2081 -0.0249 -0.0185 -0.0110 183 ASN A O 1457 C CB . ASN A 183 ? 0.0442 0.2725 0.2239 -0.0632 -0.0270 0.0148 183 ASN A CB 1458 C CG . ASN A 183 ? 0.1814 0.2900 0.2570 -0.0334 -0.0191 0.0093 183 ASN A CG 1459 O OD1 . ASN A 183 ? 0.1545 0.5545 0.3655 -0.0265 -0.0610 0.0740 183 ASN A OD1 1460 N ND2 . ASN A 183 ? 0.3634 0.3878 0.3222 -0.1010 -0.1147 -0.0530 183 ASN A ND2 1461 N N . SER A 184 ? 0.0568 0.2658 0.0910 -0.0058 -0.0270 0.0358 184 SER A N 1462 C CA . SER A 184 ? 0.0520 0.2672 0.1558 -0.0146 -0.0543 -0.0380 184 SER A CA 1463 C C . SER A 184 ? 0.0393 0.2475 0.1612 -0.0141 -0.0400 -0.0262 184 SER A C 1464 O O . SER A 184 ? 0.0976 0.2303 0.1811 0.0117 -0.0588 -0.0244 184 SER A O 1465 C CB . SER A 184 ? 0.0516 0.2419 0.1625 0.0394 -0.0374 -0.0280 184 SER A CB 1466 O OG . SER A 184 ? 0.0523 0.2536 0.1564 -0.0008 -0.0586 -0.0192 184 SER A OG 1467 N N . CYS A 185 ? 0.0616 0.2340 0.1650 -0.0094 -0.0546 -0.0316 185 CYS A N 1468 C CA . CYS A 185 ? 0.0636 0.2316 0.1572 0.0373 -0.0184 -0.0363 185 CYS A CA 1469 C C . CYS A 185 ? 0.0256 0.2342 0.1173 0.0022 -0.0053 -0.0339 185 CYS A C 1470 O O . CYS A 185 ? 0.1146 0.2640 0.1323 0.0690 0.0371 0.0089 185 CYS A O 1471 C CB . CYS A 185 ? 0.0341 0.2262 0.1580 0.0300 -0.0256 -0.0113 185 CYS A CB 1472 S SG . CYS A 185 ? 0.0403 0.2861 0.1460 -0.0052 -0.0118 0.0047 185 CYS A SG 1473 N N . TYR A 186 ? 0.0506 0.2510 0.0960 -0.0059 -0.0351 -0.0386 186 TYR A N 1474 C CA . TYR A 186 ? 0.0322 0.2384 0.0883 -0.0022 -0.0064 -0.0504 186 TYR A CA 1475 C C . TYR A 186 ? 0.0259 0.2409 0.1063 -0.0070 0.0065 -0.0427 186 TYR A C 1476 O O . TYR A 186 ? 0.0496 0.2407 0.1090 -0.0167 0.0017 -0.0235 186 TYR A O 1477 C CB . TYR A 186 ? 0.0487 0.2997 0.1314 0.0175 0.0238 -0.0276 186 TYR A CB 1478 C CG . TYR A 186 ? 0.0467 0.2879 0.1572 0.0245 0.0258 -0.0395 186 TYR A CG 1479 C CD1 . TYR A 186 ? 0.1425 0.3090 0.1609 -0.0226 -0.1078 -0.0026 186 TYR A CD1 1480 C CD2 . TYR A 186 ? 0.0275 0.2625 0.1677 -0.0220 0.0098 -0.0535 186 TYR A CD2 1481 C CE1 . TYR A 186 ? 0.1185 0.2858 0.1824 -0.0209 -0.0138 0.0167 186 TYR A CE1 1482 C CE2 . TYR A 186 ? 0.1220 0.3014 0.1689 0.0380 0.0209 -0.0074 186 TYR A CE2 1483 C CZ . TYR A 186 ? 0.0433 0.3159 0.1881 0.0000 0.0092 0.0449 186 TYR A CZ 1484 O OH . TYR A 186 ? 0.1176 0.2983 0.2892 0.0152 0.0779 0.0561 186 TYR A OH 1485 N N . THR A 187 ? 0.0273 0.2145 0.1286 -0.0002 0.0064 -0.0240 187 THR A N 1486 C CA . THR A 187 ? 0.0309 0.2376 0.1730 0.0265 0.0143 -0.0302 187 THR A CA 1487 C C . THR A 187 ? 0.0267 0.2193 0.1373 -0.0099 0.0106 -0.0107 187 THR A C 1488 O O . THR A 187 ? 0.0747 0.2682 0.1305 0.0149 -0.0418 -0.0238 187 THR A O 1489 C CB . THR A 187 ? 0.0258 0.3264 0.1102 0.0040 -0.0068 -0.0323 187 THR A CB 1490 O OG1 . THR A 187 ? 0.0414 0.3447 0.1037 0.0169 0.0258 -0.0238 187 THR A OG1 1491 C CG2 . THR A 187 ? 0.0269 0.3045 0.1517 0.0129 0.0121 0.0206 187 THR A CG2 1492 N N . SER A 188 ? 0.0542 0.2224 0.1291 -0.0005 0.0182 0.0066 188 SER A N 1493 C CA . SER A 188 ? 0.0455 0.1973 0.1121 -0.0063 0.0122 0.0051 188 SER A CA 1494 C C . SER A 188 ? 0.0262 0.2324 0.1828 -0.0065 0.0115 -0.0374 188 SER A C 1495 O O . SER A 188 ? 0.0315 0.2377 0.2847 0.0125 0.0307 -0.0549 188 SER A O 1496 C CB . SER A 188 ? 0.0368 0.2133 0.1303 -0.0200 -0.0287 0.0272 188 SER A CB 1497 O OG . SER A 188 ? 0.0306 0.2534 0.1547 0.0040 -0.0259 0.0093 188 SER A OG 1498 N N . ILE A 189 ? 0.0564 0.2105 0.1563 -0.0249 0.0044 -0.0118 189 ILE A N 1499 C CA . ILE A 189 ? 0.0757 0.2532 0.1414 -0.0101 -0.0106 -0.0160 189 ILE A CA 1500 C C . ILE A 189 ? 0.0779 0.2203 0.1336 0.0031 0.0104 -0.0186 189 ILE A C 1501 O O . ILE A 189 ? 0.0872 0.2234 0.1585 0.0163 -0.0181 -0.0386 189 ILE A O 1502 C CB . ILE A 189 ? 0.0324 0.2262 0.1208 0.0370 -0.0014 -0.0364 189 ILE A CB 1503 C CG1 . ILE A 189 ? 0.0313 0.2482 0.1112 0.0208 0.0102 -0.0654 189 ILE A CG1 1504 C CG2 . ILE A 189 ? 0.0439 0.2725 0.1430 0.0345 0.0366 -0.0233 189 ILE A CG2 1505 C CD1 . ILE A 189 ? 0.0254 0.2541 0.1890 0.0045 0.0025 -0.0176 189 ILE A CD1 1506 N N . ALA A 190 ? 0.0318 0.1881 0.1374 -0.0016 -0.0052 -0.0261 190 ALA A N 1507 C CA . ALA A 190 ? 0.0401 0.2398 0.1481 -0.0258 -0.0325 -0.0367 190 ALA A CA 1508 C C . ALA A 190 ? 0.0438 0.2216 0.1084 -0.0290 -0.0255 -0.0446 190 ALA A C 1509 O O . ALA A 190 ? 0.1014 0.2367 0.1000 0.0169 -0.0277 -0.0249 190 ALA A O 1510 C CB . ALA A 190 ? 0.0346 0.2115 0.1973 0.0398 -0.0144 -0.0138 190 ALA A CB 1511 N N . GLY A 191 ? 0.0469 0.2284 0.1481 -0.0195 -0.0134 -0.0363 191 GLY A N 1512 C CA . GLY A 191 ? 0.0344 0.2237 0.1317 -0.0195 -0.0224 -0.0414 191 GLY A CA 1513 C C . GLY A 191 ? 0.0348 0.2482 0.1045 -0.0441 0.0109 -0.0163 191 GLY A C 1514 O O . GLY A 191 ? 0.0354 0.2324 0.1104 -0.0342 0.0228 -0.0214 191 GLY A O 1515 N N . GLY A 192 ? 0.0311 0.2393 0.0983 -0.0337 -0.0072 0.0058 192 GLY A N 1516 C CA . GLY A 192 ? 0.0807 0.2267 0.1095 -0.0024 -0.0009 -0.0191 192 GLY A CA 1517 C C . GLY A 192 ? 0.0431 0.2104 0.1243 -0.0015 -0.0159 -0.0367 192 GLY A C 1518 O O . GLY A 192 ? 0.0378 0.1842 0.1417 -0.0088 -0.0239 -0.0192 192 GLY A O 1519 N N . TYR A 193 ? 0.0267 0.2042 0.1059 -0.0032 -0.0094 -0.0355 193 TYR A N 1520 C CA . TYR A 193 ? 0.0512 0.2495 0.0645 -0.0256 -0.0005 -0.0395 193 TYR A CA 1521 C C . TYR A 193 ? 0.0442 0.2251 0.0624 -0.0100 -0.0235 -0.0183 193 TYR A C 1522 O O . TYR A 193 ? 0.0279 0.1993 0.0491 -0.0134 -0.0023 -0.0355 193 TYR A O 1523 C CB . TYR A 193 ? 0.0324 0.2051 0.1031 0.0012 0.0049 -0.0384 193 TYR A CB 1524 C CG . TYR A 193 ? 0.0271 0.2095 0.0835 0.0160 -0.0073 -0.0332 193 TYR A CG 1525 C CD1 . TYR A 193 ? 0.0488 0.2583 0.1255 -0.0294 -0.0424 -0.0148 193 TYR A CD1 1526 C CD2 . TYR A 193 ? 0.0813 0.2212 0.0924 0.0440 -0.0538 -0.0037 193 TYR A CD2 1527 C CE1 . TYR A 193 ? 0.0490 0.2728 0.1298 -0.0042 -0.0486 -0.0259 193 TYR A CE1 1528 C CE2 . TYR A 193 ? 0.0592 0.2449 0.1034 0.0287 -0.0506 -0.0204 193 TYR A CE2 1529 C CZ . TYR A 193 ? 0.0808 0.2267 0.0880 -0.0086 -0.0404 -0.0454 193 TYR A CZ 1530 O OH . TYR A 193 ? 0.1486 0.2177 0.1511 0.0558 -0.0545 -0.0559 193 TYR A OH 1531 N N . THR A 194 ? 0.0293 0.1966 0.1046 -0.0186 -0.0105 -0.0179 194 THR A N 1532 C CA . THR A 194 ? 0.0295 0.1838 0.1001 -0.0081 -0.0167 -0.0018 194 THR A CA 1533 C C . THR A 194 ? 0.0329 0.1729 0.1068 -0.0062 -0.0245 0.0025 194 THR A C 1534 O O . THR A 194 ? 0.0506 0.2253 0.1015 -0.0100 -0.0423 -0.0157 194 THR A O 1535 C CB . THR A 194 ? 0.0478 0.2194 0.1226 0.0048 -0.0464 0.0048 194 THR A CB 1536 O OG1 . THR A 194 ? 0.0483 0.2669 0.1271 -0.0247 -0.0319 0.0034 194 THR A OG1 1537 C CG2 . THR A 194 ? 0.0953 0.1915 0.1767 -0.0010 -0.0138 -0.0089 194 THR A CG2 1538 N N . VAL A 195 ? 0.0344 0.1897 0.1174 -0.0015 0.0082 -0.0214 195 VAL A N 1539 C CA . VAL A 195 ? 0.0253 0.1957 0.0722 0.0004 0.0004 -0.0029 195 VAL A CA 1540 C C . VAL A 195 ? 0.0356 0.1769 0.0540 -0.0141 -0.0047 0.0116 195 VAL A C 1541 O O . VAL A 195 ? 0.0472 0.2072 0.0597 -0.0169 -0.0214 -0.0204 195 VAL A O 1542 C CB . VAL A 195 ? 0.0265 0.2162 0.0584 0.0054 0.0058 -0.0021 195 VAL A CB 1543 C CG1 . VAL A 195 ? 0.0480 0.2729 0.0784 -0.0217 -0.0120 0.0480 195 VAL A CG1 1544 C CG2 . VAL A 195 ? 0.0364 0.2067 0.0607 0.0016 -0.0197 -0.0013 195 VAL A CG2 1545 N N . THR A 196 ? 0.0257 0.1636 0.0964 0.0001 0.0051 0.0256 196 THR A N 1546 C CA . THR A 196 ? 0.0311 0.1918 0.1002 0.0275 -0.0059 0.0223 196 THR A CA 1547 C C . THR A 196 ? 0.0291 0.1933 0.0563 0.0248 0.0034 0.0094 196 THR A C 1548 O O . THR A 196 ? 0.0640 0.2158 0.0665 0.0056 0.0197 0.0022 196 THR A O 1549 C CB . THR A 196 ? 0.0293 0.2527 0.0791 0.0301 0.0012 0.0093 196 THR A CB 1550 O OG1 . THR A 196 ? 0.0896 0.2209 0.1651 0.0190 -0.0310 -0.0163 196 THR A OG1 1551 C CG2 . THR A 196 ? 0.0365 0.2565 0.1521 0.0097 0.0156 -0.0390 196 THR A CG2 1552 N N . LYS A 197 ? 0.0376 0.1873 0.0920 0.0296 0.0084 0.0027 197 LYS A N 1553 C CA . LYS A 197 ? 0.0370 0.1888 0.0617 0.0138 -0.0053 -0.0138 197 LYS A CA 1554 C C . LYS A 197 ? 0.0264 0.1906 0.0718 0.0138 -0.0005 -0.0036 197 LYS A C 1555 O O . LYS A 197 ? 0.0343 0.1956 0.1267 0.0099 0.0051 0.0229 197 LYS A O 1556 C CB . LYS A 197 ? 0.0473 0.1858 0.0574 0.0224 -0.0220 0.0150 197 LYS A CB 1557 C CG . LYS A 197 ? 0.0294 0.2375 0.0841 0.0119 -0.0124 0.0026 197 LYS A CG 1558 C CD . LYS A 197 ? 0.0297 0.1978 0.0841 0.0000 0.0159 -0.0122 197 LYS A CD 1559 C CE . LYS A 197 ? 0.0541 0.2362 0.0616 0.0074 0.0281 -0.0303 197 LYS A CE 1560 N NZ . LYS A 197 ? 0.0674 0.2442 0.0617 -0.0270 0.0012 -0.0150 197 LYS A NZ 1561 N N . LYS A 198 ? 0.0277 0.2078 0.0884 -0.0025 0.0121 0.0023 198 LYS A N 1562 C CA . LYS A 198 ? 0.0624 0.1890 0.0797 0.0033 -0.0076 -0.0128 198 LYS A CA 1563 C C . LYS A 198 ? 0.0292 0.1910 0.0811 0.0056 0.0030 0.0071 198 LYS A C 1564 O O . LYS A 198 ? 0.0295 0.1844 0.0990 0.0058 0.0161 -0.0208 198 LYS A O 1565 C CB . LYS A 198 ? 0.0616 0.2178 0.1099 0.0076 -0.0286 -0.0177 198 LYS A CB 1566 C CG . LYS A 198 ? 0.1674 0.2777 0.1885 0.0243 -0.1462 -0.0637 198 LYS A CG 1567 C CD . LYS A 198 ? 0.1974 0.3703 0.2909 0.1093 -0.2094 -0.0999 198 LYS A CD 1568 C CE . LYS A 198 ? 0.3098 0.4255 0.6170 0.0567 -0.3608 -0.0845 198 LYS A CE 1569 N NZ . LYS A 198 ? 1.1809 0.6983 1.1063 0.3073 -0.9571 -0.0719 198 LYS A NZ 1570 N N . VAL A 199 ? 0.0324 0.2111 0.0917 0.0146 0.0184 -0.0152 199 VAL A N 1571 C CA . VAL A 199 ? 0.0369 0.1944 0.0893 0.0023 0.0069 0.0263 199 VAL A CA 1572 C C . VAL A 199 ? 0.0466 0.1869 0.1093 -0.0248 0.0369 0.0084 199 VAL A C 1573 O O . VAL A 199 ? 0.0372 0.1940 0.0956 -0.0195 0.0035 0.0032 199 VAL A O 1574 C CB . VAL A 199 ? 0.0299 0.2106 0.0635 0.0030 -0.0132 -0.0070 199 VAL A CB 1575 C CG1 . VAL A 199 ? 0.0511 0.2122 0.1107 0.0177 -0.0062 0.0077 199 VAL A CG1 1576 C CG2 . VAL A 199 ? 0.0687 0.1937 0.0781 0.0118 -0.0009 0.0222 199 VAL A CG2 1577 N N . LYS A 200 ? 0.0426 0.1639 0.1372 0.0036 0.0236 -0.0060 200 LYS A N 1578 C CA . LYS A 200 ? 0.0286 0.2090 0.1087 0.0244 -0.0044 -0.0171 200 LYS A CA 1579 C C . LYS A 200 ? 0.0434 0.2683 0.0965 0.0394 0.0260 -0.0135 200 LYS A C 1580 O O . LYS A 200 ? 0.0629 0.2281 0.1044 0.0422 0.0016 -0.0205 200 LYS A O 1581 C CB . LYS A 200 ? 0.0441 0.2371 0.1145 0.0629 -0.0002 0.0117 200 LYS A CB 1582 C CG . LYS A 200 ? 0.0660 0.1803 0.2175 0.0364 0.0378 0.0113 200 LYS A CG 1583 C CD . LYS A 200 ? 0.1514 0.2589 0.2905 0.0293 0.0697 0.1027 200 LYS A CD 1584 C CE . LYS A 200 ? 0.1292 0.3126 0.5069 0.0426 0.0873 0.0704 200 LYS A CE 1585 N NZ . LYS A 200 ? 0.1829 0.2499 0.5281 0.0466 -0.0140 0.1281 200 LYS A NZ 1586 N N . LEU A 201 ? 0.0356 0.1921 0.0872 0.0360 0.0141 0.0077 201 LEU A N 1587 C CA . LEU A 201 ? 0.0407 0.2028 0.0999 0.0449 0.0180 0.0025 201 LEU A CA 1588 C C . LEU A 201 ? 0.0294 0.2197 0.0761 0.0248 0.0085 0.0120 201 LEU A C 1589 O O . LEU A 201 ? 0.0768 0.2194 0.0945 0.0386 0.0372 0.0166 201 LEU A O 1590 C CB . LEU A 201 ? 0.0423 0.2007 0.0850 0.0416 0.0182 -0.0098 201 LEU A CB 1591 C CG . LEU A 201 ? 0.0265 0.2186 0.0889 0.0102 0.0048 -0.0291 201 LEU A CG 1592 C CD1 . LEU A 201 ? 0.0418 0.2287 0.1130 -0.0074 0.0138 0.0161 201 LEU A CD1 1593 C CD2 . LEU A 201 ? 0.0672 0.2127 0.1696 -0.0028 -0.0372 0.0247 201 LEU A CD2 1594 N N . PRO A 202 ? 0.0375 0.2253 0.0883 0.0400 -0.0050 0.0040 202 PRO A N 1595 C CA . PRO A 202 ? 0.0543 0.2017 0.1283 0.0613 -0.0212 0.0190 202 PRO A CA 1596 C C . PRO A 202 ? 0.0304 0.2494 0.0866 0.0263 -0.0040 -0.0339 202 PRO A C 1597 O O . PRO A 202 ? 0.0447 0.2043 0.1062 0.0213 0.0000 0.0060 202 PRO A O 1598 C CB . PRO A 202 ? 0.0404 0.2701 0.1342 0.0140 -0.0386 0.0131 202 PRO A CB 1599 C CG . PRO A 202 ? 0.1645 0.2749 0.0756 0.0238 -0.0588 0.0508 202 PRO A CG 1600 C CD . PRO A 202 ? 0.0690 0.2706 0.0541 0.0487 -0.0040 0.0329 202 PRO A CD 1601 N N . GLU A 203 ? 0.0811 0.2267 0.1143 0.0346 -0.0073 -0.0017 203 GLU A N 1602 C CA . GLU A 203 ? 0.0614 0.2140 0.1076 0.0202 0.0193 0.0069 203 GLU A CA 1603 C C . GLU A 203 ? 0.2049 0.2920 0.1103 0.0926 0.0508 0.0369 203 GLU A C 1604 O O . GLU A 203 ? 0.1930 0.3198 0.2882 0.0750 0.0435 -0.0205 203 GLU A O 1605 C CB . GLU A 203 ? 0.1219 0.1868 0.1473 0.0652 0.0540 -0.0006 203 GLU A CB 1606 C CG . GLU A 203 ? 0.1195 0.2805 0.1393 0.0308 0.0147 0.0209 203 GLU A CG 1607 C CD . GLU A 203 ? 0.0858 0.2917 0.2155 0.0903 0.0514 0.0601 203 GLU A CD 1608 O OE1 . GLU A 203 ? 0.1499 0.2862 0.1917 0.0276 0.0021 0.0413 203 GLU A OE1 1609 O OE2 . GLU A 203 ? 0.1680 0.3765 0.2916 0.0750 0.1167 0.0939 203 GLU A OE2 1610 N N . TYR A 204 ? 0.0358 0.2246 0.1323 0.0156 0.0326 0.0154 204 TYR A N 1611 C CA . TYR A 204 ? 0.0303 0.2217 0.1202 0.0099 0.0203 -0.0051 204 TYR A CA 1612 C C . TYR A 204 ? 0.0389 0.1972 0.1664 0.0430 0.0238 0.0163 204 TYR A C 1613 O O . TYR A 204 ? 0.0499 0.2426 0.1535 -0.0131 0.0477 0.0067 204 TYR A O 1614 C CB . TYR A 204 ? 0.0953 0.2588 0.1646 0.0099 -0.0309 0.0313 204 TYR A CB 1615 C CG . TYR A 204 ? 0.0324 0.2748 0.1246 0.0155 0.0266 0.0599 204 TYR A CG 1616 C CD1 . TYR A 204 ? 0.0484 0.2570 0.1536 0.0348 0.0307 0.0247 204 TYR A CD1 1617 C CD2 . TYR A 204 ? 0.0401 0.2282 0.1319 0.0160 0.0394 0.0294 204 TYR A CD2 1618 C CE1 . TYR A 204 ? 0.0274 0.2299 0.1673 0.0059 -0.0170 -0.0184 204 TYR A CE1 1619 C CE2 . TYR A 204 ? 0.0567 0.2398 0.1722 0.0292 0.0113 0.0392 204 TYR A CE2 1620 C CZ . TYR A 204 ? 0.0520 0.2326 0.1422 0.0311 0.0008 0.0420 204 TYR A CZ 1621 O OH . TYR A 204 ? 0.1031 0.2210 0.1849 0.0443 -0.0217 -0.0287 204 TYR A OH 1622 N N . THR A 205 ? 0.0385 0.2212 0.1373 0.0288 0.0082 -0.0060 205 THR A N 1623 C CA . THR A 205 ? 0.0510 0.2581 0.1106 0.0038 0.0460 0.0339 205 THR A CA 1624 C C . THR A 205 ? 0.0366 0.1902 0.1161 -0.0046 0.0272 0.0004 205 THR A C 1625 O O . THR A 205 ? 0.0550 0.2439 0.1699 0.0080 -0.0269 -0.0043 205 THR A O 1626 C CB . THR A 205 ? 0.0656 0.1934 0.1173 0.0239 0.0167 0.0019 205 THR A CB 1627 O OG1 . THR A 205 ? 0.0498 0.2104 0.1290 0.0155 0.0037 -0.0241 205 THR A OG1 1628 C CG2 . THR A 205 ? 0.0677 0.1823 0.1385 0.0113 0.0009 0.0175 205 THR A CG2 1629 N N . SER A 206 ? 0.0658 0.1944 0.1274 -0.0211 0.0031 0.0104 206 SER A N 1630 C CA . SER A 206 ? 0.0305 0.2201 0.1150 0.0079 0.0163 0.0086 206 SER A CA 1631 C C . SER A 206 ? 0.0544 0.2163 0.0445 0.0036 -0.0209 0.0250 206 SER A C 1632 O O . SER A 206 ? 0.0530 0.2447 0.0796 -0.0044 -0.0022 -0.0210 206 SER A O 1633 C CB . SER A 206 ? 0.0328 0.3155 0.1212 0.0366 -0.0189 -0.0174 206 SER A CB 1634 O OG . SER A 206 ? 0.1469 0.2288 0.2189 0.0512 -0.0231 -0.0476 206 SER A OG 1635 N N . ASN A 207 ? 0.0516 0.2174 0.0991 0.0148 0.0356 0.0191 207 ASN A N 1636 C CA . ASN A 207 ? 0.0296 0.2158 0.1605 0.0256 -0.0083 0.0173 207 ASN A CA 1637 C C . ASN A 207 ? 0.0267 0.2098 0.1162 0.0121 -0.0079 -0.0052 207 ASN A C 1638 O O . ASN A 207 ? 0.0509 0.2012 0.1474 0.0155 0.0094 -0.0031 207 ASN A O 1639 C CB . ASN A 207 ? 0.0479 0.2681 0.2029 0.0516 0.0438 -0.0074 207 ASN A CB 1640 C CG . ASN A 207 ? 0.0427 0.2470 0.1486 0.0337 0.0018 0.0137 207 ASN A CG 1641 O OD1 . ASN A 207 ? 0.0417 0.2365 0.1678 0.0418 -0.0100 0.0126 207 ASN A OD1 1642 N ND2 . ASN A 207 ? 0.0598 0.2733 0.1262 0.0670 0.0516 0.0475 207 ASN A ND2 1643 N N . HIS A 208 ? 0.0291 0.2073 0.0935 0.0260 -0.0009 0.0123 208 HIS A N 1644 C CA . HIS A 208 ? 0.0296 0.1915 0.1171 0.0263 0.0073 0.0219 208 HIS A CA 1645 C C . HIS A 208 ? 0.0404 0.2333 0.0720 -0.0269 -0.0081 0.0187 208 HIS A C 1646 O O . HIS A 208 ? 0.0274 0.2408 0.0828 0.0104 -0.0101 -0.0112 208 HIS A O 1647 C CB . HIS A 208 ? 0.0649 0.1924 0.1625 0.0281 0.0035 0.0476 208 HIS A CB 1648 C CG . HIS A 208 ? 0.0308 0.2006 0.1302 0.0172 0.0205 0.0148 208 HIS A CG 1649 N ND1 . HIS A 208 ? 0.0880 0.1994 0.1540 -0.0156 0.0432 0.0041 208 HIS A ND1 1650 C CD2 . HIS A 208 ? 0.0813 0.2304 0.1459 0.0520 0.0233 0.0099 208 HIS A CD2 1651 C CE1 . HIS A 208 ? 0.1011 0.2098 0.1182 0.0123 0.0495 0.0243 208 HIS A CE1 1652 N NE2 . HIS A 208 ? 0.0444 0.2143 0.1344 0.0199 0.0427 0.0090 208 HIS A NE2 1653 N N . THR A 209 ? 0.0296 0.2319 0.0997 0.0136 0.0119 0.0039 209 THR A N 1654 C CA . THR A 209 ? 0.0270 0.2031 0.0836 0.0134 -0.0064 -0.0024 209 THR A CA 1655 C C . THR A 209 ? 0.0262 0.2344 0.0840 0.0122 -0.0038 -0.0157 209 THR A C 1656 O O . THR A 209 ? 0.0277 0.2017 0.1080 0.0162 0.0077 -0.0110 209 THR A O 1657 C CB . THR A 209 ? 0.0290 0.2104 0.1023 0.0260 -0.0019 0.0027 209 THR A CB 1658 O OG1 . THR A 209 ? 0.0266 0.1895 0.1606 0.0081 -0.0071 -0.0190 209 THR A OG1 1659 C CG2 . THR A 209 ? 0.0350 0.2517 0.1488 0.0080 -0.0299 0.0574 209 THR A CG2 1660 N N . LEU A 210 ? 0.0258 0.1976 0.1211 -0.0074 0.0049 -0.0266 210 LEU A N 1661 C CA . LEU A 210 ? 0.0406 0.1879 0.0543 0.0071 -0.0210 -0.0068 210 LEU A CA 1662 C C . LEU A 210 ? 0.0289 0.1804 0.0620 0.0217 -0.0055 -0.0085 210 LEU A C 1663 O O . LEU A 210 ? 0.0481 0.1886 0.0960 0.0053 0.0030 -0.0090 210 LEU A O 1664 C CB . LEU A 210 ? 0.0286 0.1951 0.0526 0.0090 -0.0026 0.0070 210 LEU A CB 1665 C CG . LEU A 210 ? 0.0386 0.1993 0.0639 0.0093 -0.0045 0.0226 210 LEU A CG 1666 C CD1 . LEU A 210 ? 0.0464 0.2421 0.0899 0.0008 -0.0356 0.0187 210 LEU A CD1 1667 C CD2 . LEU A 210 ? 0.0375 0.2432 0.1530 -0.0310 0.0282 0.0215 210 LEU A CD2 1668 N N A ILE A 211 ? 0.0314 0.1730 0.0515 0.0285 0.0030 -0.0051 211 ILE A N 1669 N N B ILE A 211 ? 0.0297 0.1584 0.0882 0.0181 0.0082 -0.0181 211 ILE A N 1670 C CA A ILE A 211 ? 0.0376 0.1831 0.0324 0.0138 -0.0082 0.0056 211 ILE A CA 1671 C CA B ILE A 211 ? 0.0708 0.1845 0.0642 -0.0083 0.0008 -0.0117 211 ILE A CA 1672 C C A ILE A 211 ? 0.0381 0.1673 0.0403 0.0050 0.0138 0.0081 211 ILE A C 1673 C C B ILE A 211 ? 0.0454 0.1795 0.0701 -0.0206 0.0276 0.0018 211 ILE A C 1674 O O A ILE A 211 ? 0.0267 0.1672 0.0259 0.0126 0.0008 0.0056 211 ILE A O 1675 O O B ILE A 211 ? 0.0568 0.1634 0.1166 0.0060 0.0515 -0.0215 211 ILE A O 1676 C CB A ILE A 211 ? 0.0511 0.1759 0.0406 0.0139 -0.0169 -0.0107 211 ILE A CB 1677 C CB B ILE A 211 ? 0.0764 0.1793 0.0628 -0.0258 0.0074 0.0112 211 ILE A CB 1678 C CG1 A ILE A 211 ? 0.0430 0.2306 0.1296 0.0346 -0.0263 0.0427 211 ILE A CG1 1679 C CG1 B ILE A 211 ? 0.0446 0.1739 0.0324 0.0024 -0.0109 -0.0127 211 ILE A CG1 1680 C CG2 A ILE A 211 ? 0.0484 0.2126 0.1028 0.0049 0.0176 -0.0061 211 ILE A CG2 1681 C CG2 B ILE A 211 ? 0.0474 0.1299 0.0276 0.0166 -0.0057 -0.0132 211 ILE A CG2 1682 C CD1 A ILE A 211 ? 0.0709 0.3561 0.0575 0.1051 -0.0112 0.0249 211 ILE A CD1 1683 C CD1 B ILE A 211 ? 0.0263 0.1807 0.0261 -0.0111 0.0001 0.0026 211 ILE A CD1 1684 N N . SER A 212 ? 0.0359 0.1796 0.0829 -0.0050 0.0034 0.0142 212 SER A N 1685 C CA . SER A 212 ? 0.0361 0.1599 0.0811 -0.0118 -0.0125 0.0219 212 SER A CA 1686 C C . SER A 212 ? 0.0274 0.1503 0.0921 0.0159 0.0003 0.0221 212 SER A C 1687 O O . SER A 212 ? 0.0289 0.1722 0.1176 0.0084 0.0183 0.0317 212 SER A O 1688 C CB . SER A 212 ? 0.0287 0.2078 0.1061 0.0045 -0.0166 -0.0124 212 SER A CB 1689 O OG . SER A 212 ? 0.0254 0.1911 0.1089 -0.0001 -0.0035 0.0051 212 SER A OG 1690 N N . PHE A 213 ? 0.0318 0.1601 0.0930 -0.0241 0.0095 0.0136 213 PHE A N 1691 C CA . PHE A 213 ? 0.0325 0.1702 0.0701 -0.0086 -0.0179 0.0279 213 PHE A CA 1692 C C . PHE A 213 ? 0.0273 0.1466 0.0831 -0.0132 0.0033 0.0214 213 PHE A C 1693 O O . PHE A 213 ? 0.0359 0.1706 0.0714 -0.0191 0.0146 0.0269 213 PHE A O 1694 C CB . PHE A 213 ? 0.0318 0.1726 0.0801 -0.0026 -0.0046 -0.0050 213 PHE A CB 1695 C CG . PHE A 213 ? 0.0298 0.1847 0.1003 -0.0080 -0.0077 -0.0297 213 PHE A CG 1696 C CD1 . PHE A 213 ? 0.0315 0.2080 0.1037 -0.0149 -0.0188 -0.0099 213 PHE A CD1 1697 C CD2 . PHE A 213 ? 0.0732 0.1968 0.1456 0.0106 -0.0190 -0.0416 213 PHE A CD2 1698 C CE1 . PHE A 213 ? 0.0319 0.2443 0.0893 -0.0263 -0.0143 -0.0052 213 PHE A CE1 1699 C CE2 . PHE A 213 ? 0.0386 0.2058 0.1931 -0.0215 0.0244 -0.0617 213 PHE A CE2 1700 C CZ . PHE A 213 ? 0.0305 0.2401 0.1373 -0.0256 0.0228 -0.0795 213 PHE A CZ 1701 N N . LYS A 214 ? 0.0263 0.1536 0.0633 0.0068 0.0043 0.0309 214 LYS A N 1702 C CA . LYS A 214 ? 0.0313 0.1556 0.0626 0.0070 -0.0123 0.0240 214 LYS A CA 1703 C C . LYS A 214 ? 0.0257 0.1486 0.0886 -0.0061 0.0035 -0.0105 214 LYS A C 1704 O O . LYS A 214 ? 0.0316 0.1907 0.0973 0.0158 0.0202 0.0203 214 LYS A O 1705 C CB . LYS A 214 ? 0.0259 0.1448 0.1387 0.0053 -0.0007 0.0008 214 LYS A CB 1706 C CG . LYS A 214 ? 0.0270 0.1918 0.1051 0.0161 -0.0056 -0.0235 214 LYS A CG 1707 C CD . LYS A 214 ? 0.0392 0.1597 0.1118 0.0129 -0.0102 -0.0053 214 LYS A CD 1708 C CE . LYS A 214 ? 0.0300 0.2095 0.1360 0.0290 0.0021 -0.0117 214 LYS A CE 1709 N NZ . LYS A 214 ? 0.0508 0.1746 0.1047 -0.0026 -0.0137 -0.0230 214 LYS A NZ 1710 N N . TRP A 215 ? 0.0315 0.1469 0.0736 0.0187 -0.0008 0.0104 215 TRP A N 1711 C CA . TRP A 215 ? 0.0365 0.1356 0.0601 0.0102 -0.0194 -0.0068 215 TRP A CA 1712 C C . TRP A 215 ? 0.0362 0.1445 0.0617 0.0190 0.0004 0.0064 215 TRP A C 1713 O O . TRP A 215 ? 0.0274 0.1444 0.0733 -0.0147 -0.0056 0.0172 215 TRP A O 1714 C CB . TRP A 215 ? 0.0435 0.1661 0.0694 -0.0345 0.0235 -0.0124 215 TRP A CB 1715 C CG . TRP A 215 ? 0.0280 0.2096 0.0625 0.0032 0.0096 -0.0117 215 TRP A CG 1716 C CD1 . TRP A 215 ? 0.0255 0.2019 0.0798 -0.0028 0.0030 -0.0037 215 TRP A CD1 1717 C CD2 . TRP A 215 ? 0.0256 0.1824 0.0531 0.0056 0.0015 -0.0078 215 TRP A CD2 1718 N NE1 . TRP A 215 ? 0.0298 0.2016 0.0901 -0.0127 0.0164 -0.0193 215 TRP A NE1 1719 C CE2 . TRP A 215 ? 0.0257 0.1849 0.0525 0.0042 -0.0033 -0.0253 215 TRP A CE2 1720 C CE3 . TRP A 215 ? 0.0286 0.1887 0.0645 0.0058 -0.0110 0.0000 215 TRP A CE3 1721 C CZ2 . TRP A 215 ? 0.0271 0.1838 0.1168 0.0148 0.0029 -0.0360 215 TRP A CZ2 1722 C CZ3 . TRP A 215 ? 0.0290 0.1569 0.1221 -0.0055 0.0184 0.0020 215 TRP A CZ3 1723 C CH2 . TRP A 215 ? 0.0333 0.1738 0.1229 0.0287 0.0118 -0.0174 215 TRP A CH2 1724 N N . ASN A 216 ? 0.0258 0.1531 0.0812 0.0007 -0.0056 -0.0092 216 ASN A N 1725 C CA . ASN A 216 ? 0.0286 0.1779 0.0746 0.0131 0.0097 -0.0084 216 ASN A CA 1726 C C . ASN A 216 ? 0.0315 0.1768 0.0811 -0.0265 0.0124 -0.0192 216 ASN A C 1727 O O . ASN A 216 ? 0.0277 0.1778 0.1125 0.0167 -0.0058 0.0101 216 ASN A O 1728 C CB . ASN A 216 ? 0.0272 0.1816 0.0942 0.0103 0.0056 -0.0431 216 ASN A CB 1729 C CG . ASN A 216 ? 0.0263 0.1785 0.0781 0.0115 -0.0036 -0.0176 216 ASN A CG 1730 O OD1 . ASN A 216 ? 0.0254 0.1965 0.0846 0.0015 0.0019 -0.0283 216 ASN A OD1 1731 N ND2 . ASN A 216 ? 0.0257 0.2506 0.0994 -0.0089 0.0034 -0.0226 216 ASN A ND2 1732 N N . SER A 217 ? 0.0433 0.1887 0.0964 -0.0221 0.0339 -0.0111 217 SER A N 1733 C CA . SER A 217 ? 0.0500 0.1904 0.1064 -0.0332 0.0288 -0.0305 217 SER A CA 1734 C C . SER A 217 ? 0.0309 0.1931 0.0603 0.0061 0.0131 -0.0116 217 SER A C 1735 O O . SER A 217 ? 0.0278 0.2424 0.1237 0.0014 0.0153 -0.0275 217 SER A O 1736 C CB . SER A 217 ? 0.0275 0.1986 0.1706 -0.0138 -0.0057 -0.0152 217 SER A CB 1737 O OG . SER A 217 ? 0.0317 0.2349 0.1582 -0.0129 0.0130 -0.0120 217 SER A OG 1738 N N . PHE A 218 ? 0.0315 0.2011 0.0557 0.0135 0.0122 -0.0037 218 PHE A N 1739 C CA . PHE A 218 ? 0.0384 0.1899 0.1098 -0.0134 0.0324 -0.0078 218 PHE A CA 1740 C C . PHE A 218 ? 0.0257 0.1899 0.1155 0.0036 0.0051 -0.0019 218 PHE A C 1741 O O . PHE A 218 ? 0.0254 0.2409 0.1330 0.0005 0.0036 -0.0168 218 PHE A O 1742 C CB . PHE A 218 ? 0.0358 0.1994 0.1001 -0.0119 0.0271 -0.0032 218 PHE A CB 1743 C CG . PHE A 218 ? 0.0407 0.2206 0.1216 0.0299 0.0320 -0.0013 218 PHE A CG 1744 C CD1 . PHE A 218 ? 0.0358 0.2475 0.1080 0.0289 0.0219 -0.0125 218 PHE A CD1 1745 C CD2 . PHE A 218 ? 0.0569 0.2804 0.1171 0.0408 0.0331 -0.0252 218 PHE A CD2 1746 C CE1 . PHE A 218 ? 0.0824 0.2733 0.1736 0.0273 0.0913 0.0675 218 PHE A CE1 1747 C CE2 . PHE A 218 ? 0.0833 0.3760 0.0510 0.0230 0.0372 -0.0099 218 PHE A CE2 1748 C CZ . PHE A 218 ? 0.0552 0.3580 0.1908 0.0530 0.0398 0.0046 218 PHE A CZ 1749 N N . GLN A 219 ? 0.0373 0.2181 0.1329 -0.0075 0.0358 -0.0321 219 GLN A N 1750 C CA . GLN A 219 ? 0.0280 0.2175 0.1695 0.0087 0.0172 -0.0195 219 GLN A CA 1751 C C . GLN A 219 ? 0.0377 0.2090 0.1551 0.0233 0.0247 -0.0592 219 GLN A C 1752 O O . GLN A 219 ? 0.0772 0.2799 0.1936 0.0875 0.0593 0.0110 219 GLN A O 1753 C CB . GLN A 219 ? 0.0650 0.2901 0.2739 0.0033 0.0278 -0.1500 219 GLN A CB 1754 C CG . GLN A 219 ? 0.1249 0.3520 0.3351 0.0482 -0.0238 -0.0936 219 GLN A CG 1755 C CD . GLN A 219 ? 0.0848 0.4915 0.2444 0.0103 0.0779 -0.0787 219 GLN A CD 1756 O OE1 . GLN A 219 ? 0.0995 0.3788 0.2457 -0.0166 0.1277 -0.0446 219 GLN A OE1 1757 N NE2 . GLN A 219 ? 0.0469 0.6765 0.5417 0.0191 0.0616 -0.2937 219 GLN A NE2 1758 N N . THR A 220 ? 0.0311 0.2287 0.1161 0.0272 0.0127 -0.0097 220 THR A N 1759 C CA . THR A 220 ? 0.0993 0.1898 0.1169 0.0077 0.0129 -0.0026 220 THR A CA 1760 C C . THR A 220 ? 0.0599 0.2026 0.1518 0.0046 -0.0300 -0.0149 220 THR A C 1761 O O . THR A 220 ? 0.0819 0.2018 0.1819 0.0099 0.0309 -0.0295 220 THR A O 1762 C CB . THR A 220 ? 0.0334 0.2178 0.1120 0.0318 -0.0128 0.0167 220 THR A CB 1763 O OG1 . THR A 220 ? 0.0393 0.2515 0.1306 0.0434 -0.0269 -0.0165 220 THR A OG1 1764 C CG2 . THR A 220 ? 0.0307 0.2778 0.1261 0.0320 -0.0121 -0.0033 220 THR A CG2 1765 N N . GLY A 221 ? 0.0360 0.2236 0.1339 0.0429 0.0086 -0.0175 221 GLY A N 1766 C CA . GLY A 221 ? 0.0289 0.2263 0.1773 0.0235 -0.0152 -0.0346 221 GLY A CA 1767 C C . GLY A 221 ? 0.0667 0.1886 0.1269 -0.0037 -0.0378 0.0027 221 GLY A C 1768 O O . GLY A 221 ? 0.0280 0.2164 0.1477 -0.0074 -0.0180 0.0259 221 GLY A O 1769 N N . GLN A 222 ? 0.0257 0.2236 0.1231 -0.0088 0.0019 0.0077 222 GLN A N 1770 C CA . GLN A 222 ? 0.0280 0.1778 0.1139 -0.0202 -0.0028 0.0063 222 GLN A CA 1771 C C . GLN A 222 ? 0.0273 0.1870 0.1554 -0.0007 0.0157 0.0205 222 GLN A C 1772 O O . GLN A 222 ? 0.0256 0.1801 0.1264 0.0066 0.0026 0.0004 222 GLN A O 1773 C CB . GLN A 222 ? 0.0437 0.1668 0.1571 -0.0028 0.0045 -0.0423 222 GLN A CB 1774 C CG . GLN A 222 ? 0.0272 0.1869 0.1110 -0.0014 0.0117 -0.0194 222 GLN A CG 1775 C CD . GLN A 222 ? 0.0423 0.2088 0.1780 -0.0097 -0.0144 -0.0372 222 GLN A CD 1776 O OE1 . GLN A 222 ? 0.0445 0.2506 0.1543 0.0149 -0.0017 -0.0753 222 GLN A OE1 1777 N NE2 . GLN A 222 ? 0.1297 0.2482 0.3484 -0.0007 -0.0562 0.0334 222 GLN A NE2 1778 N N . ILE A 223 ? 0.0299 0.1288 0.1141 -0.0085 -0.0124 0.0158 223 ILE A N 1779 C CA . ILE A 223 ? 0.0276 0.1458 0.1280 -0.0064 0.0122 0.0289 223 ILE A CA 1780 C C . ILE A 223 ? 0.0289 0.1591 0.1171 -0.0131 0.0134 0.0111 223 ILE A C 1781 O O . ILE A 223 ? 0.0340 0.1827 0.1410 -0.0041 -0.0315 0.0311 223 ILE A O 1782 C CB . ILE A 223 ? 0.0448 0.1624 0.1425 -0.0015 0.0098 0.0194 223 ILE A CB 1783 C CG1 . ILE A 223 ? 0.0285 0.1720 0.1061 0.0187 0.0104 0.0174 223 ILE A CG1 1784 C CG2 . ILE A 223 ? 0.0559 0.1806 0.2029 0.0000 0.0224 -0.0254 223 ILE A CG2 1785 C CD1 . ILE A 223 ? 0.0416 0.2362 0.0826 0.0062 -0.0016 0.0206 223 ILE A CD1 1786 N N . TYR A 224 ? 0.0315 0.1705 0.1041 -0.0097 0.0177 0.0324 224 TYR A N 1787 C CA . TYR A 224 ? 0.0354 0.1481 0.1072 -0.0156 0.0245 0.0087 224 TYR A CA 1788 C C . TYR A 224 ? 0.0276 0.1638 0.0845 0.0069 -0.0107 0.0015 224 TYR A C 1789 O O . TYR A 224 ? 0.0331 0.1811 0.0995 0.0222 0.0177 -0.0057 224 TYR A O 1790 C CB . TYR A 224 ? 0.0473 0.1733 0.1284 0.0049 0.0039 0.0007 224 TYR A CB 1791 C CG . TYR A 224 ? 0.0261 0.1982 0.1296 0.0008 0.0087 -0.0211 224 TYR A CG 1792 C CD1 . TYR A 224 ? 0.0269 0.2125 0.1091 -0.0171 0.0000 -0.0064 224 TYR A CD1 1793 C CD2 . TYR A 224 ? 0.0326 0.2149 0.0839 0.0242 -0.0105 0.0241 224 TYR A CD2 1794 C CE1 . TYR A 224 ? 0.0377 0.2346 0.1113 -0.0069 -0.0319 -0.0110 224 TYR A CE1 1795 C CE2 . TYR A 224 ? 0.0287 0.2258 0.1129 0.0152 -0.0153 -0.0217 224 TYR A CE2 1796 C CZ . TYR A 224 ? 0.0421 0.2295 0.1051 0.0349 -0.0038 -0.0088 224 TYR A CZ 1797 O OH . TYR A 224 ? 0.0410 0.2231 0.1741 0.0483 -0.0295 -0.0229 224 TYR A OH 1798 N N . LEU A 225 ? 0.0257 0.1832 0.0902 0.0072 -0.0031 -0.0088 225 LEU A N 1799 C CA . LEU A 225 ? 0.0285 0.1836 0.0829 0.0165 -0.0088 0.0034 225 LEU A CA 1800 C C . LEU A 225 ? 0.0347 0.1574 0.0984 0.0000 -0.0220 0.0103 225 LEU A C 1801 O O . LEU A 225 ? 0.0305 0.1762 0.1039 0.0125 0.0042 0.0137 225 LEU A O 1802 C CB . LEU A 225 ? 0.0354 0.2210 0.0773 0.0039 0.0024 -0.0178 225 LEU A CB 1803 C CG . LEU A 225 ? 0.0272 0.2310 0.0944 0.0157 0.0052 -0.0236 225 LEU A CG 1804 C CD1 . LEU A 225 ? 0.0384 0.3024 0.0977 -0.0004 -0.0299 -0.0335 225 LEU A CD1 1805 C CD2 . LEU A 225 ? 0.0898 0.2352 0.0711 -0.0323 0.0027 0.0053 225 LEU A CD2 1806 N N . SER A 226 ? 0.0277 0.1511 0.1018 -0.0027 0.0123 0.0270 226 SER A N 1807 C CA . SER A 226 ? 0.0275 0.1867 0.0832 -0.0134 0.0067 0.0114 226 SER A CA 1808 C C . SER A 226 ? 0.0311 0.1936 0.0695 0.0224 -0.0058 0.0337 226 SER A C 1809 O O . SER A 226 ? 0.0647 0.1939 0.0853 0.0163 0.0107 0.0022 226 SER A O 1810 C CB . SER A 226 ? 0.0418 0.2280 0.0746 -0.0254 0.0186 -0.0206 226 SER A CB 1811 O OG . SER A 226 ? 0.0276 0.2359 0.1162 -0.0184 0.0115 -0.0495 226 SER A OG 1812 N N . CYS A 227 ? 0.0285 0.1485 0.0866 -0.0027 -0.0058 0.0224 227 CYS A N 1813 C CA . CYS A 227 ? 0.0430 0.1508 0.1327 0.0011 0.0435 0.0030 227 CYS A CA 1814 C C . CYS A 227 ? 0.0404 0.1382 0.1134 -0.0053 0.0010 -0.0154 227 CYS A C 1815 O O . CYS A 227 ? 0.0292 0.1515 0.1574 0.0044 -0.0084 0.0003 227 CYS A O 1816 C CB . CYS A 227 ? 0.1625 0.2324 0.1261 0.0461 0.0892 -0.0300 227 CYS A CB 1817 S SG . CYS A 227 ? 0.0622 0.2908 0.1555 0.0057 0.0333 0.0078 227 CYS A SG 1818 N N . ALA A 228 ? 0.0276 0.1584 0.1291 0.0040 0.0153 0.0116 228 ALA A N 1819 C CA . ALA A 228 ? 0.0303 0.1812 0.0928 -0.0016 0.0183 0.0043 228 ALA A CA 1820 C C . ALA A 228 ? 0.0256 0.1744 0.0900 0.0054 0.0032 0.0125 228 ALA A C 1821 O O . ALA A 228 ? 0.0396 0.1798 0.1016 0.0105 -0.0005 -0.0104 228 ALA A O 1822 C CB . ALA A 228 ? 0.0309 0.1960 0.1248 0.0212 -0.0177 -0.0040 228 ALA A CB 1823 N N . ASP A 229 ? 0.0276 0.1762 0.1013 -0.0173 0.0042 0.0029 229 ASP A N 1824 C CA . ASP A 229 ? 0.0385 0.1578 0.0975 0.0070 -0.0070 0.0227 229 ASP A CA 1825 C C . ASP A 229 ? 0.0279 0.1685 0.0700 0.0178 -0.0045 -0.0026 229 ASP A C 1826 O O . ASP A 229 ? 0.0256 0.1833 0.1199 0.0072 -0.0013 -0.0094 229 ASP A O 1827 C CB . ASP A 229 ? 0.0256 0.1808 0.0860 0.0064 0.0023 0.0154 229 ASP A CB 1828 C CG . ASP A 229 ? 0.0265 0.1749 0.0767 0.0116 0.0047 0.0077 229 ASP A CG 1829 O OD1 . ASP A 229 ? 0.0318 0.1890 0.1143 0.0108 -0.0233 -0.0126 229 ASP A OD1 1830 O OD2 . ASP A 229 ? 0.0870 0.1874 0.1018 -0.0023 0.0221 -0.0271 229 ASP A OD2 1831 N N . ILE A 230 ? 0.0311 0.1662 0.1029 0.0244 -0.0125 -0.0084 230 ILE A N 1832 C CA . ILE A 230 ? 0.0664 0.1807 0.0778 0.0237 -0.0292 -0.0080 230 ILE A CA 1833 C C . ILE A 230 ? 0.0384 0.1783 0.0783 0.0189 -0.0175 0.0011 230 ILE A C 1834 O O . ILE A 230 ? 0.0393 0.2219 0.0851 0.0164 -0.0275 -0.0008 230 ILE A O 1835 C CB . ILE A 230 ? 0.0783 0.1840 0.0940 -0.0037 -0.0289 0.0105 230 ILE A CB 1836 C CG1 . ILE A 230 ? 0.0302 0.2406 0.1453 0.0060 0.0230 -0.0214 230 ILE A CG1 1837 C CG2 . ILE A 230 ? 0.0355 0.2208 0.1288 -0.0168 -0.0315 0.0180 230 ILE A CG2 1838 C CD1 . ILE A 230 ? 0.0954 0.3061 0.1555 0.0195 0.0669 0.0071 230 ILE A CD1 1839 N N . ALA A 231 ? 0.0320 0.1980 0.0945 0.0282 -0.0111 0.0052 231 ALA A N 1840 C CA . ALA A 231 ? 0.0278 0.1815 0.1186 -0.0017 -0.0045 0.0039 231 ALA A CA 1841 C C . ALA A 231 ? 0.0471 0.2079 0.1093 0.0053 -0.0107 0.0121 231 ALA A C 1842 O O . ALA A 231 ? 0.0559 0.2313 0.1064 0.0328 -0.0125 0.0110 231 ALA A O 1843 C CB . ALA A 231 ? 0.0341 0.2018 0.1587 0.0301 0.0183 -0.0206 231 ALA A CB 1844 N N . ILE A 232 ? 0.0658 0.2144 0.1135 0.0226 -0.0416 -0.0156 232 ILE A N 1845 C CA . ILE A 232 ? 0.0557 0.2347 0.0795 0.0243 -0.0049 -0.0049 232 ILE A CA 1846 C C . ILE A 232 ? 0.0258 0.2280 0.1164 0.0093 0.0024 0.0057 232 ILE A C 1847 O O . ILE A 232 ? 0.0588 0.2312 0.1512 0.0088 0.0096 -0.0280 232 ILE A O 1848 C CB . ILE A 232 ? 0.0350 0.2353 0.1510 0.0424 -0.0118 0.0010 232 ILE A CB 1849 C CG1 . ILE A 232 ? 0.0362 0.2320 0.1758 0.0332 0.0323 0.0264 232 ILE A CG1 1850 C CG2 . ILE A 232 ? 0.0537 0.2223 0.1237 0.0160 0.0506 -0.0099 232 ILE A CG2 1851 C CD1 . ILE A 232 ? 0.0510 0.2580 0.1709 -0.0106 0.0087 -0.0216 232 ILE A CD1 1852 N N . GLN A 233 ? 0.0330 0.2371 0.1387 0.0401 -0.0038 -0.0038 233 GLN A N 1853 C CA . GLN A 233 ? 0.0285 0.2314 0.1385 0.0212 0.0107 0.0034 233 GLN A CA 1854 C C . GLN A 233 ? 0.0796 0.2588 0.0981 0.0603 0.0174 0.0055 233 GLN A C 1855 O O . GLN A 233 ? 0.0520 0.3954 0.1100 0.0360 0.0363 -0.0064 233 GLN A O 1856 C CB . GLN A 233 ? 0.0900 0.2579 0.1862 0.0171 0.0724 0.0196 233 GLN A CB 1857 C CG . GLN A 233 ? 0.0783 0.2568 0.1260 -0.0405 0.0194 0.0232 233 GLN A CG 1858 C CD . GLN A 233 ? 0.0522 0.2777 0.1296 -0.0405 0.0428 0.0188 233 GLN A CD 1859 O OE1 . GLN A 233 ? 0.1486 0.2665 0.2275 -0.0316 0.0156 -0.0413 233 GLN A OE1 1860 N NE2 . GLN A 233 ? 0.1041 0.3567 0.1227 -0.0636 0.0303 0.0111 233 GLN A NE2 1861 O OXT . GLN A 233 ? 0.1444 0.2518 0.2188 0.0791 0.0588 0.0105 233 GLN A OXT 1862 CU CU . CU B . ? 0.0309 0.2198 0.1525 0.0147 0.0074 0.0050 301 CU A CU 1863 C C1 . NAG C . ? 0.0373 0.2529 0.1194 0.0521 0.0114 0.0385 302 NAG A C1 1864 C C2 . NAG C . ? 0.0557 0.2173 0.1177 0.0003 0.0523 0.0101 302 NAG A C2 1865 C C3 . NAG C . ? 0.0967 0.2445 0.1139 0.0464 0.0732 0.0237 302 NAG A C3 1866 C C4 . NAG C . ? 0.0673 0.2802 0.1452 0.0819 0.0443 0.0961 302 NAG A C4 1867 C C5 . NAG C . ? 0.0668 0.2941 0.1800 0.0846 0.0411 0.0780 302 NAG A C5 1868 C C6 . NAG C . ? 0.0908 0.2934 0.1647 0.0719 0.0341 0.0728 302 NAG A C6 1869 C C7 . NAG C . ? 0.0896 0.1992 0.1240 0.0068 0.0571 -0.0366 302 NAG A C7 1870 C C8 . NAG C . ? 0.0389 0.1552 0.0956 0.0081 0.0308 0.0122 302 NAG A C8 1871 N N2 . NAG C . ? 0.0713 0.2076 0.0973 0.0224 0.0330 0.0223 302 NAG A N2 1872 O O3 . NAG C . ? 0.1609 0.2494 0.1429 -0.0139 0.0307 0.0215 302 NAG A O3 1873 O O4 . NAG C . ? 0.0458 0.2817 0.2653 0.0460 0.0499 0.0478 302 NAG A O4 1874 O O5 . NAG C . ? 0.0704 0.2888 0.1724 0.0614 0.0786 0.0646 302 NAG A O5 1875 O O6 . NAG C . ? 0.0700 0.3850 0.1469 0.0365 0.0413 0.0916 302 NAG A O6 1876 O O7 . NAG C . ? 0.1873 0.3462 0.1561 0.0002 0.1079 -0.0377 302 NAG A O7 1877 ZN ZN . ZN D . ? 0.0272 0.2405 0.1365 0.0036 -0.0139 0.0026 303 ZN A ZN 1878 ZN ZN . ZN E . ? 0.1628 0.2766 0.1947 0.0041 -0.0256 -0.0420 304 ZN A ZN 1879 ZN ZN . ZN F . ? 0.1191 0.2835 0.1845 -0.0487 -0.0469 0.0258 305 ZN A ZN 1880 ZN ZN . ZN G . ? 0.4043 0.4267 0.1438 -0.1673 -0.0449 0.0517 306 ZN A ZN # 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 HIC 1 1 1 HIC HIC A . n A 1 2 GLY 2 2 2 GLY GLY A . n A 1 3 TYR 3 3 3 TYR TYR A . n A 1 4 MET 4 4 4 MET MET A . n A 1 5 TYR 5 5 5 TYR TYR A . n A 1 6 ILE 6 6 6 ILE ILE A . n A 1 7 PRO 7 7 7 PRO PRO A . n A 1 8 SER 8 8 8 SER SER A . n A 1 9 SER 9 9 9 SER SER A . n A 1 10 ARG 10 10 10 ARG ARG A . n A 1 11 THR 11 11 11 THR THR A . n A 1 12 ARG 12 12 12 ARG ARG A . n A 1 13 LEU 13 13 13 LEU LEU A . n A 1 14 GLY 14 14 14 GLY GLY A . n A 1 15 HIS 15 15 15 HIS HIS A . n A 1 16 GLU 16 16 16 GLU GLU A . n A 1 17 ALA 17 17 17 ALA ALA A . n A 1 18 GLY 18 18 18 GLY GLY A . n A 1 19 ILE 19 19 19 ILE ILE A . n A 1 20 ASP 20 20 20 ASP ASP A . n A 1 21 SER 21 21 21 SER SER A . n A 1 22 CYS 22 22 22 CYS CYS A . n A 1 23 PRO 23 23 23 PRO PRO A . n A 1 24 GLU 24 24 24 GLU GLU A . n A 1 25 CYS 25 25 25 CYS CYS A . n A 1 26 ALA 26 26 26 ALA ALA A . n A 1 27 ILE 27 27 27 ILE ILE A . n A 1 28 LEU 28 28 28 LEU LEU A . n A 1 29 GLU 29 29 29 GLU GLU A . n A 1 30 PRO 30 30 30 PRO PRO A . n A 1 31 VAL 31 31 31 VAL VAL A . n A 1 32 SER 32 32 32 SER SER A . n A 1 33 SER 33 33 33 SER SER A . n A 1 34 TRP 34 34 34 TRP TRP A . n A 1 35 PRO 35 35 35 PRO PRO A . n A 1 36 ASP 36 36 36 ASP ASP A . n A 1 37 LEU 37 37 37 LEU LEU A . n A 1 38 ASP 38 38 38 ASP ASP A . n A 1 39 ALA 39 39 39 ALA ALA A . n A 1 40 ALA 40 40 40 ALA ALA A . n A 1 41 PRO 41 41 41 PRO PRO A . n A 1 42 VAL 42 42 42 VAL VAL A . n A 1 43 GLY 43 43 43 GLY GLY A . n A 1 44 ARG 44 44 44 ARG ARG A . n A 1 45 SER 45 45 45 SER SER A . n A 1 46 GLY 46 46 46 GLY GLY A . n A 1 47 PRO 47 47 47 PRO PRO A . n A 1 48 CYS 48 48 48 CYS CYS A . n A 1 49 GLY 49 49 49 GLY GLY A . n A 1 50 TYR 50 50 50 TYR TYR A . n A 1 51 ASN 51 51 51 ASN ASN A . n A 1 52 ALA 52 52 52 ALA ALA A . n A 1 53 ARG 53 53 53 ARG ARG A . n A 1 54 ASP 54 54 54 ASP ASP A . n A 1 55 SER 55 55 55 SER SER A . n A 1 56 ILE 56 56 56 ILE ILE A . n A 1 57 ASP 57 57 57 ASP ASP A . n A 1 58 TYR 58 58 58 TYR TYR A . n A 1 59 ASN 59 59 59 ASN ASN A . n A 1 60 GLN 60 60 60 GLN GLN A . n A 1 61 PRO 61 61 61 PRO PRO A . n A 1 62 THR 62 62 62 THR THR A . n A 1 63 THR 63 63 63 THR THR A . n A 1 64 ASN 64 64 64 ASN ASN A . n A 1 65 TRP 65 65 65 TRP TRP A . n A 1 66 GLY 66 66 66 GLY GLY A . n A 1 67 SER 67 67 67 SER SER A . n A 1 68 ASP 68 68 68 ASP ASP A . n A 1 69 ALA 69 69 69 ALA ALA A . n A 1 70 VAL 70 70 70 VAL VAL A . n A 1 71 GLN 71 71 71 GLN GLN A . n A 1 72 SER 72 72 72 SER SER A . n A 1 73 TYR 73 73 73 TYR TYR A . n A 1 74 SER 74 74 74 SER SER A . n A 1 75 PRO 75 75 75 PRO PRO A . n A 1 76 GLY 76 76 76 GLY GLY A . n A 1 77 GLU 77 77 77 GLU GLU A . n A 1 78 GLU 78 78 78 GLU GLU A . n A 1 79 ILE 79 79 79 ILE ILE A . n A 1 80 GLU 80 80 80 GLU GLU A . n A 1 81 VAL 81 81 81 VAL VAL A . n A 1 82 GLN 82 82 82 GLN GLN A . n A 1 83 TRP 83 83 83 TRP TRP A . n A 1 84 CYS 84 84 84 CYS CYS A . n A 1 85 VAL 85 85 85 VAL VAL A . n A 1 86 ASP 86 86 86 ASP ASP A . n A 1 87 HIS 87 87 87 HIS HIS A . n A 1 88 ASN 88 88 88 ASN ASN A . n A 1 89 GLY 89 89 89 GLY GLY A . n A 1 90 ASP 90 90 90 ASP ASP A . n A 1 91 HIS 91 91 91 HIS HIS A . n A 1 92 GLY 92 92 92 GLY GLY A . n A 1 93 GLY 93 93 93 GLY GLY A . n A 1 94 MET 94 94 94 MET MET A . n A 1 95 PHE 95 95 95 PHE PHE A . n A 1 96 THR 96 96 96 THR THR A . n A 1 97 TYR 97 97 97 TYR TYR A . n A 1 98 ARG 98 98 98 ARG ARG A . n A 1 99 ILE 99 99 99 ILE ILE A . n A 1 100 CYS 100 100 100 CYS CYS A . n A 1 101 GLN 101 101 101 GLN GLN A . n A 1 102 ASP 102 102 102 ASP ASP A . n A 1 103 GLN 103 103 103 GLN GLN A . n A 1 104 SER 104 104 104 SER SER A . n A 1 105 ILE 105 105 105 ILE ILE A . n A 1 106 VAL 106 106 106 VAL VAL A . n A 1 107 ASP 107 107 107 ASP ASP A . n A 1 108 LYS 108 108 108 LYS LYS A . n A 1 109 PHE 109 109 109 PHE PHE A . n A 1 110 LEU 110 110 110 LEU LEU A . n A 1 111 ASP 111 111 111 ASP ASP A . n A 1 112 PRO 112 112 112 PRO PRO A . n A 1 113 SER 113 113 113 SER SER A . n A 1 114 TYR 114 114 114 TYR TYR A . n A 1 115 LEU 115 115 115 LEU LEU A . n A 1 116 PRO 116 116 116 PRO PRO A . n A 1 117 THR 117 117 117 THR THR A . n A 1 118 ASN 118 118 118 ASN ASN A . n A 1 119 ASP 119 119 119 ASP ASP A . n A 1 120 GLU 120 120 120 GLU GLU A . n A 1 121 LYS 121 121 121 LYS LYS A . n A 1 122 GLN 122 122 122 GLN GLN A . n A 1 123 ALA 123 123 123 ALA ALA A . n A 1 124 ALA 124 124 124 ALA ALA A . n A 1 125 GLU 125 125 125 GLU GLU A . n A 1 126 ASP 126 126 126 ASP ASP A . n A 1 127 CYS 127 127 127 CYS CYS A . n A 1 128 PHE 128 128 128 PHE PHE A . n A 1 129 ASP 129 129 129 ASP ASP A . n A 1 130 ALA 130 130 130 ALA ALA A . n A 1 131 GLY 131 131 131 GLY GLY A . n A 1 132 LEU 132 132 132 LEU LEU A . n A 1 133 LEU 133 133 133 LEU LEU A . n A 1 134 PRO 134 134 134 PRO PRO A . n A 1 135 CYS 135 135 135 CYS CYS A . n A 1 136 THR 136 136 136 THR THR A . n A 1 137 ASP 137 137 137 ASP ASP A . n A 1 138 VAL 138 138 138 VAL VAL A . n A 1 139 SER 139 139 139 SER SER A . n A 1 140 GLY 140 140 140 GLY GLY A . n A 1 141 GLN 141 141 141 GLN GLN A . n A 1 142 GLU 142 142 142 GLU GLU A . n A 1 143 CYS 143 143 143 CYS CYS A . n A 1 144 GLY 144 144 144 GLY GLY A . n A 1 145 TYR 145 145 145 TYR TYR A . n A 1 146 SER 146 146 146 SER SER A . n A 1 147 ALA 147 147 147 ALA ALA A . n A 1 148 ASP 148 148 148 ASP ASP A . n A 1 149 CYS 149 149 149 CYS CYS A . n A 1 150 THR 150 150 150 THR THR A . n A 1 151 GLU 151 151 151 GLU GLU A . n A 1 152 GLY 152 152 152 GLY GLY A . n A 1 153 GLU 153 153 153 GLU GLU A . n A 1 154 ALA 154 154 154 ALA ALA A . n A 1 155 CYS 155 155 155 CYS CYS A . n A 1 156 TRP 156 156 156 TRP TRP A . n A 1 157 ARG 157 157 157 ARG ARG A . n A 1 158 ASN 158 158 158 ASN ASN A . n A 1 159 ASP 159 159 159 ASP ASP A . n A 1 160 TRP 160 160 160 TRP TRP A . n A 1 161 PHE 161 161 161 PHE PHE A . n A 1 162 THR 162 162 162 THR THR A . n A 1 163 CYS 163 163 163 CYS CYS A . n A 1 164 ASN 164 164 164 ASN ASN A . n A 1 165 GLY 165 165 165 GLY GLY A . n A 1 166 PHE 166 166 166 PHE PHE A . n A 1 167 GLU 167 167 167 GLU GLU A . n A 1 168 ALA 168 168 168 ALA ALA A . n A 1 169 SER 169 169 169 SER SER A . n A 1 170 ASP 170 170 170 ASP ASP A . n A 1 171 ARG 171 171 171 ARG ARG A . n A 1 172 PRO 172 172 172 PRO PRO A . n A 1 173 LYS 173 173 173 LYS LYS A . n A 1 174 CYS 174 174 174 CYS CYS A . n A 1 175 GLN 175 175 175 GLN GLN A . n A 1 176 GLY 176 176 176 GLY GLY A . n A 1 177 VAL 177 177 177 VAL VAL A . n A 1 178 ASP 178 178 178 ASP ASP A . n A 1 179 ASN 179 179 179 ASN ASN A . n A 1 180 ALA 180 180 180 ALA ALA A . n A 1 181 GLU 181 181 181 GLU GLU A . n A 1 182 LEU 182 182 182 LEU LEU A . n A 1 183 ASN 183 183 183 ASN ASN A . n A 1 184 SER 184 184 184 SER SER A . n A 1 185 CYS 185 185 185 CYS CYS A . n A 1 186 TYR 186 186 186 TYR TYR A . n A 1 187 THR 187 187 187 THR THR A . n A 1 188 SER 188 188 188 SER SER A . n A 1 189 ILE 189 189 189 ILE ILE A . n A 1 190 ALA 190 190 190 ALA ALA A . n A 1 191 GLY 191 191 191 GLY GLY A . n A 1 192 GLY 192 192 192 GLY GLY A . n A 1 193 TYR 193 193 193 TYR TYR A . n A 1 194 THR 194 194 194 THR THR A . n A 1 195 VAL 195 195 195 VAL VAL A . n A 1 196 THR 196 196 196 THR THR A . n A 1 197 LYS 197 197 197 LYS LYS A . n A 1 198 LYS 198 198 198 LYS LYS A . n A 1 199 VAL 199 199 199 VAL VAL A . n A 1 200 LYS 200 200 200 LYS LYS A . n A 1 201 LEU 201 201 201 LEU LEU A . n A 1 202 PRO 202 202 202 PRO PRO A . n A 1 203 GLU 203 203 203 GLU GLU A . n A 1 204 TYR 204 204 204 TYR TYR A . n A 1 205 THR 205 205 205 THR THR A . n A 1 206 SER 206 206 206 SER SER A . n A 1 207 ASN 207 207 207 ASN ASN A . n A 1 208 HIS 208 208 208 HIS HIS A . n A 1 209 THR 209 209 209 THR THR A . n A 1 210 LEU 210 210 210 LEU LEU A . n A 1 211 ILE 211 211 211 ILE ILE A . n A 1 212 SER 212 212 212 SER SER A . n A 1 213 PHE 213 213 213 PHE PHE A . n A 1 214 LYS 214 214 214 LYS LYS A . n A 1 215 TRP 215 215 215 TRP TRP A . n A 1 216 ASN 216 216 216 ASN ASN A . n A 1 217 SER 217 217 217 SER SER A . n A 1 218 PHE 218 218 218 PHE PHE A . n A 1 219 GLN 219 219 219 GLN GLN A . n A 1 220 THR 220 220 220 THR THR A . n A 1 221 GLY 221 221 221 GLY GLY A . n A 1 222 GLN 222 222 222 GLN GLN A . n A 1 223 ILE 223 223 223 ILE ILE A . n A 1 224 TYR 224 224 224 TYR TYR A . n A 1 225 LEU 225 225 225 LEU LEU A . n A 1 226 SER 226 226 226 SER SER A . n A 1 227 CYS 227 227 227 CYS CYS A . n A 1 228 ALA 228 228 228 ALA ALA A . n A 1 229 ASP 229 229 229 ASP ASP A . n A 1 230 ILE 230 230 230 ILE ILE A . n A 1 231 ALA 231 231 231 ALA ALA A . n A 1 232 ILE 232 232 232 ILE ILE A . n A 1 233 GLN 233 233 233 GLN GLN 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 CU 1 301 301 CU CU A . C 3 NAG 1 302 401 NAG NAG A . D 4 ZN 1 303 1 ZN ZN A . E 4 ZN 1 304 2 ZN ZN A . F 4 ZN 1 305 3 ZN ZN A . G 4 ZN 1 306 4 ZN ZN A . H 5 IPA 1 307 1 IPA IPA A . I 6 GOL 1 308 2 GOL GOL A . J 6 GOL 1 309 3 GOL GOL A . K 5 IPA 1 310 4 IPA IPA A . L 6 GOL 1 311 5 GOL GOL A . M 6 GOL 1 312 6 GOL GOL A . N 7 ACT 1 313 7 ACT ACT A . O 6 GOL 1 314 8 GOL GOL A . P 6 GOL 1 315 9 GOL GOL A . Q 6 GOL 1 316 10 GOL GOL A . R 7 ACT 1 317 11 ACT ACT A . S 8 HOH 1 401 1 HOH HOH A . S 8 HOH 2 402 2 HOH HOH A . S 8 HOH 3 403 3 HOH HOH A . S 8 HOH 4 404 4 HOH HOH A . S 8 HOH 5 405 5 HOH HOH A . S 8 HOH 6 406 6 HOH HOH A . S 8 HOH 7 407 7 HOH HOH A . S 8 HOH 8 408 8 HOH HOH A . S 8 HOH 9 409 9 HOH HOH A . S 8 HOH 10 410 10 HOH HOH A . S 8 HOH 11 411 11 HOH HOH A . S 8 HOH 12 412 12 HOH HOH A . S 8 HOH 13 413 13 HOH HOH A . S 8 HOH 14 414 14 HOH HOH A . S 8 HOH 15 415 15 HOH HOH A . S 8 HOH 16 416 16 HOH HOH A . S 8 HOH 17 417 17 HOH HOH A . S 8 HOH 18 418 18 HOH HOH A . S 8 HOH 19 419 19 HOH HOH A . S 8 HOH 20 420 20 HOH HOH A . S 8 HOH 21 421 21 HOH HOH A . S 8 HOH 22 422 22 HOH HOH A . S 8 HOH 23 423 23 HOH HOH A . S 8 HOH 24 424 24 HOH HOH A . S 8 HOH 25 425 25 HOH HOH A . S 8 HOH 26 426 26 HOH HOH A . S 8 HOH 27 427 27 HOH HOH A . S 8 HOH 28 428 28 HOH HOH A . S 8 HOH 29 429 29 HOH HOH A . S 8 HOH 30 430 30 HOH HOH A . S 8 HOH 31 431 31 HOH HOH A . S 8 HOH 32 432 32 HOH HOH A . S 8 HOH 33 433 33 HOH HOH A . S 8 HOH 34 434 34 HOH HOH A . S 8 HOH 35 435 35 HOH HOH A . S 8 HOH 36 436 36 HOH HOH A . S 8 HOH 37 437 37 HOH HOH A . S 8 HOH 38 438 38 HOH HOH A . S 8 HOH 39 439 39 HOH HOH A . S 8 HOH 40 440 40 HOH HOH A . S 8 HOH 41 441 41 HOH HOH A . S 8 HOH 42 442 42 HOH HOH A . S 8 HOH 43 443 43 HOH HOH A . S 8 HOH 44 444 44 HOH HOH A . S 8 HOH 45 445 45 HOH HOH A . S 8 HOH 46 446 46 HOH HOH A . S 8 HOH 47 447 47 HOH HOH A . S 8 HOH 48 448 48 HOH HOH A . S 8 HOH 49 449 49 HOH HOH A . S 8 HOH 50 450 50 HOH HOH A . S 8 HOH 51 451 51 HOH HOH A . S 8 HOH 52 452 52 HOH HOH A . S 8 HOH 53 453 53 HOH HOH A . S 8 HOH 54 454 54 HOH HOH A . S 8 HOH 55 455 55 HOH HOH A . S 8 HOH 56 456 56 HOH HOH A . S 8 HOH 57 457 57 HOH HOH A . S 8 HOH 58 458 58 HOH HOH A . S 8 HOH 59 459 59 HOH HOH A . S 8 HOH 60 460 60 HOH HOH A . S 8 HOH 61 461 61 HOH HOH A . S 8 HOH 62 462 62 HOH HOH A . S 8 HOH 63 463 63 HOH HOH A . S 8 HOH 64 464 64 HOH HOH A . S 8 HOH 65 465 65 HOH HOH A . S 8 HOH 66 466 66 HOH HOH A . S 8 HOH 67 467 67 HOH HOH A . S 8 HOH 68 468 68 HOH HOH A . S 8 HOH 69 469 69 HOH HOH A . S 8 HOH 70 470 70 HOH HOH A . S 8 HOH 71 471 71 HOH HOH A . S 8 HOH 72 472 72 HOH HOH A . S 8 HOH 73 473 73 HOH HOH A . S 8 HOH 74 474 74 HOH HOH A . S 8 HOH 75 475 75 HOH HOH A . S 8 HOH 76 476 76 HOH HOH A . S 8 HOH 77 477 77 HOH HOH A . S 8 HOH 78 478 78 HOH HOH A . S 8 HOH 79 479 79 HOH HOH A . S 8 HOH 80 480 80 HOH HOH A . S 8 HOH 81 481 81 HOH HOH A . S 8 HOH 82 482 82 HOH HOH A . S 8 HOH 83 483 83 HOH HOH A . S 8 HOH 84 484 84 HOH HOH A . S 8 HOH 85 485 85 HOH HOH A . S 8 HOH 86 486 86 HOH HOH A . S 8 HOH 87 487 87 HOH HOH A . S 8 HOH 88 488 88 HOH HOH A . S 8 HOH 89 489 89 HOH HOH A . S 8 HOH 90 490 90 HOH HOH A . S 8 HOH 91 491 91 HOH HOH A . S 8 HOH 92 492 92 HOH HOH A . S 8 HOH 93 493 93 HOH HOH A . S 8 HOH 94 494 94 HOH HOH A . S 8 HOH 95 495 95 HOH HOH A . S 8 HOH 96 496 96 HOH HOH A . S 8 HOH 97 497 97 HOH HOH A . S 8 HOH 98 498 98 HOH HOH A . S 8 HOH 99 499 99 HOH HOH A . S 8 HOH 100 500 102 HOH HOH A . S 8 HOH 101 501 103 HOH HOH A . S 8 HOH 102 502 105 HOH HOH A . S 8 HOH 103 503 106 HOH HOH A . S 8 HOH 104 504 107 HOH HOH A . S 8 HOH 105 505 108 HOH HOH A . S 8 HOH 106 506 109 HOH HOH A . S 8 HOH 107 507 110 HOH HOH A . S 8 HOH 108 508 111 HOH HOH A . S 8 HOH 109 509 112 HOH HOH A . S 8 HOH 110 510 113 HOH HOH A . S 8 HOH 111 511 114 HOH HOH A . S 8 HOH 112 512 115 HOH HOH A . S 8 HOH 113 513 116 HOH HOH A . S 8 HOH 114 514 117 HOH HOH A . S 8 HOH 115 515 118 HOH HOH A . S 8 HOH 116 516 119 HOH HOH A . S 8 HOH 117 517 120 HOH HOH A . S 8 HOH 118 518 121 HOH HOH A . S 8 HOH 119 519 122 HOH HOH A . S 8 HOH 120 520 123 HOH HOH A . S 8 HOH 121 521 124 HOH HOH A . S 8 HOH 122 522 125 HOH HOH A . S 8 HOH 123 523 126 HOH HOH A . S 8 HOH 124 524 127 HOH HOH A . S 8 HOH 125 525 128 HOH HOH A . S 8 HOH 126 526 129 HOH HOH A . S 8 HOH 127 527 130 HOH HOH A . S 8 HOH 128 528 131 HOH HOH A . S 8 HOH 129 529 132 HOH HOH A . S 8 HOH 130 530 133 HOH HOH A . S 8 HOH 131 531 134 HOH HOH A . S 8 HOH 132 532 135 HOH HOH A . S 8 HOH 133 533 136 HOH HOH A . S 8 HOH 134 534 137 HOH HOH A . S 8 HOH 135 535 138 HOH HOH A . S 8 HOH 136 536 139 HOH HOH A . S 8 HOH 137 537 140 HOH HOH A . S 8 HOH 138 538 141 HOH HOH A . S 8 HOH 139 539 142 HOH HOH A . S 8 HOH 140 540 143 HOH HOH A . S 8 HOH 141 541 144 HOH HOH A . S 8 HOH 142 542 145 HOH HOH A . S 8 HOH 143 543 146 HOH HOH A . S 8 HOH 144 544 147 HOH HOH A . S 8 HOH 145 545 148 HOH HOH A . S 8 HOH 146 546 149 HOH HOH A . S 8 HOH 147 547 150 HOH HOH A . S 8 HOH 148 548 151 HOH HOH A . S 8 HOH 149 549 152 HOH HOH A . S 8 HOH 150 550 153 HOH HOH A . S 8 HOH 151 551 154 HOH HOH A . S 8 HOH 152 552 155 HOH HOH A . S 8 HOH 153 553 156 HOH HOH A . S 8 HOH 154 554 157 HOH HOH A . S 8 HOH 155 555 158 HOH HOH A . S 8 HOH 156 556 159 HOH HOH A . S 8 HOH 157 557 160 HOH HOH A . S 8 HOH 158 558 161 HOH HOH A . S 8 HOH 159 559 162 HOH HOH A . S 8 HOH 160 560 163 HOH HOH A . S 8 HOH 161 561 164 HOH HOH A . S 8 HOH 162 562 165 HOH HOH A . S 8 HOH 163 563 166 HOH HOH A . S 8 HOH 164 564 167 HOH HOH A . S 8 HOH 165 565 168 HOH HOH A . S 8 HOH 166 566 169 HOH HOH A . S 8 HOH 167 567 170 HOH HOH A . S 8 HOH 168 568 171 HOH HOH A . S 8 HOH 169 569 172 HOH HOH A . S 8 HOH 170 570 173 HOH HOH A . S 8 HOH 171 571 174 HOH HOH A . S 8 HOH 172 572 175 HOH HOH A . S 8 HOH 173 573 176 HOH HOH A . S 8 HOH 174 574 177 HOH HOH A . S 8 HOH 175 575 178 HOH HOH A . S 8 HOH 176 576 179 HOH HOH A . S 8 HOH 177 577 180 HOH HOH A . S 8 HOH 178 578 181 HOH HOH A . S 8 HOH 179 579 182 HOH HOH A . S 8 HOH 180 580 183 HOH HOH A . S 8 HOH 181 581 184 HOH HOH A . S 8 HOH 182 582 185 HOH HOH A . S 8 HOH 183 583 186 HOH HOH A . S 8 HOH 184 584 187 HOH HOH A . S 8 HOH 185 585 188 HOH HOH A . S 8 HOH 186 586 189 HOH HOH A . S 8 HOH 187 587 190 HOH HOH A . S 8 HOH 188 588 191 HOH HOH A . S 8 HOH 189 589 192 HOH HOH A . S 8 HOH 190 590 193 HOH HOH A . S 8 HOH 191 591 194 HOH HOH A . S 8 HOH 192 592 195 HOH HOH A . S 8 HOH 193 593 196 HOH HOH A . S 8 HOH 194 594 197 HOH HOH A . S 8 HOH 195 595 198 HOH HOH A . S 8 HOH 196 596 199 HOH HOH A . S 8 HOH 197 597 200 HOH HOH A . S 8 HOH 198 598 201 HOH HOH A . S 8 HOH 199 599 202 HOH HOH A . S 8 HOH 200 600 203 HOH HOH A . S 8 HOH 201 601 204 HOH HOH A . S 8 HOH 202 602 205 HOH HOH A . S 8 HOH 203 603 206 HOH HOH A . S 8 HOH 204 604 207 HOH HOH A . S 8 HOH 205 605 208 HOH HOH A . S 8 HOH 206 606 210 HOH HOH A . S 8 HOH 207 607 211 HOH HOH A . S 8 HOH 208 608 212 HOH HOH A . S 8 HOH 209 609 213 HOH HOH A . S 8 HOH 210 610 215 HOH HOH A . S 8 HOH 211 611 216 HOH HOH A . S 8 HOH 212 612 217 HOH HOH A . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 207 A ASN 207 ? ASN 'GLYCOSYLATION SITE' 2 A HIC 1 A HIC 1 ? HIS 4-METHYL-HISTIDINE # _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,N,O,P,Q,R,S # _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_struct_conn_angle.id _pdbx_struct_conn_angle.ptnr1_label_atom_id _pdbx_struct_conn_angle.ptnr1_label_alt_id _pdbx_struct_conn_angle.ptnr1_label_asym_id _pdbx_struct_conn_angle.ptnr1_label_comp_id _pdbx_struct_conn_angle.ptnr1_label_seq_id _pdbx_struct_conn_angle.ptnr1_auth_atom_id _pdbx_struct_conn_angle.ptnr1_auth_asym_id _pdbx_struct_conn_angle.ptnr1_auth_comp_id _pdbx_struct_conn_angle.ptnr1_auth_seq_id _pdbx_struct_conn_angle.ptnr1_PDB_ins_code _pdbx_struct_conn_angle.ptnr1_symmetry _pdbx_struct_conn_angle.ptnr2_label_atom_id _pdbx_struct_conn_angle.ptnr2_label_alt_id _pdbx_struct_conn_angle.ptnr2_label_asym_id _pdbx_struct_conn_angle.ptnr2_label_comp_id _pdbx_struct_conn_angle.ptnr2_label_seq_id _pdbx_struct_conn_angle.ptnr2_auth_atom_id _pdbx_struct_conn_angle.ptnr2_auth_asym_id _pdbx_struct_conn_angle.ptnr2_auth_comp_id _pdbx_struct_conn_angle.ptnr2_auth_seq_id _pdbx_struct_conn_angle.ptnr2_PDB_ins_code _pdbx_struct_conn_angle.ptnr2_symmetry _pdbx_struct_conn_angle.ptnr3_label_atom_id _pdbx_struct_conn_angle.ptnr3_label_alt_id _pdbx_struct_conn_angle.ptnr3_label_asym_id _pdbx_struct_conn_angle.ptnr3_label_comp_id _pdbx_struct_conn_angle.ptnr3_label_seq_id _pdbx_struct_conn_angle.ptnr3_auth_atom_id _pdbx_struct_conn_angle.ptnr3_auth_asym_id _pdbx_struct_conn_angle.ptnr3_auth_comp_id _pdbx_struct_conn_angle.ptnr3_auth_seq_id _pdbx_struct_conn_angle.ptnr3_PDB_ins_code _pdbx_struct_conn_angle.ptnr3_symmetry _pdbx_struct_conn_angle.value _pdbx_struct_conn_angle.value_esd 1 ND1 ? A HIC 1 ? A HIC 1 ? 1_555 CU ? B CU . ? A CU 301 ? 1_555 NE2 ? A HIS 91 ? A HIS 91 ? 1_555 161.3 ? 2 ND1 ? A HIC 1 ? A HIC 1 ? 1_555 CU ? B CU . ? A CU 301 ? 1_555 N ? A HIC 1 ? A HIC 1 ? 1_555 95.6 ? 3 NE2 ? A HIS 91 ? A HIS 91 ? 1_555 CU ? B CU . ? A CU 301 ? 1_555 N ? A HIC 1 ? A HIC 1 ? 1_555 99.1 ? 4 ND1 ? A HIC 1 ? A HIC 1 ? 1_555 CU ? B CU . ? A CU 301 ? 1_555 OH ? A TYR 224 ? A TYR 224 ? 1_555 97.7 ? 5 NE2 ? A HIS 91 ? A HIS 91 ? 1_555 CU ? B CU . ? A CU 301 ? 1_555 OH ? A TYR 224 ? A TYR 224 ? 1_555 95.5 ? 6 N ? A HIC 1 ? A HIC 1 ? 1_555 CU ? B CU . ? A CU 301 ? 1_555 OH ? A TYR 224 ? A TYR 224 ? 1_555 83.2 ? 7 O B S HOH . ? A HOH 578 ? 1_555 ZN ? G ZN . ? A ZN 306 ? 1_555 OE1 ? A GLU 142 ? A GLU 142 ? 1_555 116.3 ? 8 O B S HOH . ? A HOH 578 ? 1_555 ZN ? G ZN . ? A ZN 306 ? 1_555 O ? S HOH . ? A HOH 579 ? 1_555 115.2 ? 9 OE1 ? A GLU 142 ? A GLU 142 ? 1_555 ZN ? G ZN . ? A ZN 306 ? 1_555 O ? S HOH . ? A HOH 579 ? 1_555 106.3 ? 10 O B S HOH . ? A HOH 578 ? 1_555 ZN ? G ZN . ? A ZN 306 ? 1_555 OE2 ? A GLU 142 ? A GLU 142 ? 1_555 75.5 ? 11 OE1 ? A GLU 142 ? A GLU 142 ? 1_555 ZN ? G ZN . ? A ZN 306 ? 1_555 OE2 ? A GLU 142 ? A GLU 142 ? 1_555 52.6 ? 12 O ? S HOH . ? A HOH 579 ? 1_555 ZN ? G ZN . ? A ZN 306 ? 1_555 OE2 ? A GLU 142 ? A GLU 142 ? 1_555 158.1 ? 13 O ? S HOH . ? A HOH 451 ? 1_555 ZN ? D ZN . ? A ZN 303 ? 1_555 OE2 ? A GLU 125 ? A GLU 125 ? 1_555 108.9 ? 14 O ? S HOH . ? A HOH 451 ? 1_555 ZN ? D ZN . ? A ZN 303 ? 1_555 OD2 ? A ASP 129 ? A ASP 129 ? 1_555 92.5 ? 15 OE2 ? A GLU 125 ? A GLU 125 ? 1_555 ZN ? D ZN . ? A ZN 303 ? 1_555 OD2 ? A ASP 129 ? A ASP 129 ? 1_555 120.3 ? 16 O ? S HOH . ? A HOH 451 ? 1_555 ZN ? D ZN . ? A ZN 303 ? 1_555 O ? S HOH . ? A HOH 603 ? 1_555 104.2 ? 17 OE2 ? A GLU 125 ? A GLU 125 ? 1_555 ZN ? D ZN . ? A ZN 303 ? 1_555 O ? S HOH . ? A HOH 603 ? 1_555 108.1 ? 18 OD2 ? A ASP 129 ? A ASP 129 ? 1_555 ZN ? D ZN . ? A ZN 303 ? 1_555 O ? S HOH . ? A HOH 603 ? 1_555 119.7 ? 19 O ? S HOH . ? A HOH 451 ? 1_555 ZN ? D ZN . ? A ZN 303 ? 1_555 OD1 ? A ASP 129 ? A ASP 129 ? 1_555 150.7 ? 20 OE2 ? A GLU 125 ? A GLU 125 ? 1_555 ZN ? D ZN . ? A ZN 303 ? 1_555 OD1 ? A ASP 129 ? A ASP 129 ? 1_555 89.3 ? 21 OD2 ? A ASP 129 ? A ASP 129 ? 1_555 ZN ? D ZN . ? A ZN 303 ? 1_555 OD1 ? A ASP 129 ? A ASP 129 ? 1_555 58.3 ? 22 O ? S HOH . ? A HOH 603 ? 1_555 ZN ? D ZN . ? A ZN 303 ? 1_555 OD1 ? A ASP 129 ? A ASP 129 ? 1_555 90.9 ? 23 OD1 ? A ASP 38 ? A ASP 38 ? 1_555 ZN ? F ZN . ? A ZN 305 ? 1_555 OD1 ? A ASP 36 ? A ASP 36 ? 1_555 90.0 ? 24 OD1 ? A ASP 38 ? A ASP 38 ? 1_555 ZN ? F ZN . ? A ZN 305 ? 1_555 O ? S HOH . ? A HOH 458 ? 1_555 103.3 ? 25 OD1 ? A ASP 36 ? A ASP 36 ? 1_555 ZN ? F ZN . ? A ZN 305 ? 1_555 O ? S HOH . ? A HOH 458 ? 1_555 114.0 ? 26 OD1 ? A ASP 38 ? A ASP 38 ? 1_555 ZN ? F ZN . ? A ZN 305 ? 1_555 OD2 ? A ASP 36 ? A ASP 36 ? 1_555 140.9 ? 27 OD1 ? A ASP 36 ? A ASP 36 ? 1_555 ZN ? F ZN . ? A ZN 305 ? 1_555 OD2 ? A ASP 36 ? A ASP 36 ? 1_555 51.8 ? 28 O ? S HOH . ? A HOH 458 ? 1_555 ZN ? F ZN . ? A ZN 305 ? 1_555 OD2 ? A ASP 36 ? A ASP 36 ? 1_555 88.1 ? 29 NE2 ? A HIS 15 ? A HIS 15 ? 1_555 ZN ? E ZN . ? A ZN 304 ? 1_555 O ? S HOH . ? A HOH 404 ? 1_555 99.2 ? # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2015-01-28 2 'Structure model' 1 1 2015-03-04 3 'Structure model' 1 2 2017-11-22 # _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 2 'Structure model' 'Experimental preparation' 3 3 'Structure model' 'Data collection' 4 3 'Structure model' 'Refinement description' # loop_ _pdbx_audit_revision_category.ordinal _pdbx_audit_revision_category.revision_ordinal _pdbx_audit_revision_category.data_content_type _pdbx_audit_revision_category.category 1 3 'Structure model' diffrn_source 2 3 'Structure model' software # loop_ _pdbx_audit_revision_item.ordinal _pdbx_audit_revision_item.revision_ordinal _pdbx_audit_revision_item.data_content_type _pdbx_audit_revision_item.item 1 3 'Structure model' '_diffrn_source.pdbx_synchrotron_site' 2 3 'Structure model' '_software.name' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal MAR345 'data collection' . ? 1 PHENIX 'model building' . ? 2 REFMAC refinement 5.8.0049 ? 3 XDS 'data reduction' . ? 4 XSCALE 'data scaling' . ? 5 PHENIX phasing . ? 6 # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 O A HOH 535 ? ? O A HOH 556 ? ? 2.08 2 1 O A HOH 591 ? ? O A HOH 592 ? ? 2.09 # _pdbx_validate_rmsd_angle.id 1 _pdbx_validate_rmsd_angle.PDB_model_num 1 _pdbx_validate_rmsd_angle.auth_atom_id_1 OE1 _pdbx_validate_rmsd_angle.auth_asym_id_1 A _pdbx_validate_rmsd_angle.auth_comp_id_1 GLU _pdbx_validate_rmsd_angle.auth_seq_id_1 29 _pdbx_validate_rmsd_angle.PDB_ins_code_1 ? _pdbx_validate_rmsd_angle.label_alt_id_1 ? _pdbx_validate_rmsd_angle.auth_atom_id_2 CD _pdbx_validate_rmsd_angle.auth_asym_id_2 A _pdbx_validate_rmsd_angle.auth_comp_id_2 GLU _pdbx_validate_rmsd_angle.auth_seq_id_2 29 _pdbx_validate_rmsd_angle.PDB_ins_code_2 ? _pdbx_validate_rmsd_angle.label_alt_id_2 ? _pdbx_validate_rmsd_angle.auth_atom_id_3 OE2 _pdbx_validate_rmsd_angle.auth_asym_id_3 A _pdbx_validate_rmsd_angle.auth_comp_id_3 GLU _pdbx_validate_rmsd_angle.auth_seq_id_3 29 _pdbx_validate_rmsd_angle.PDB_ins_code_3 ? _pdbx_validate_rmsd_angle.label_alt_id_3 ? _pdbx_validate_rmsd_angle.angle_value 116.05 _pdbx_validate_rmsd_angle.angle_target_value 123.30 _pdbx_validate_rmsd_angle.angle_deviation -7.25 _pdbx_validate_rmsd_angle.angle_standard_deviation 1.20 _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 CYS A 22 ? ? -152.62 76.28 2 1 GLU A 167 ? A 159.18 125.16 3 1 ALA A 168 ? B -1.20 98.71 4 1 SER A 169 ? B -8.45 -70.17 5 1 ASP A 170 ? A 125.73 3.44 6 1 ASP A 170 ? B -164.82 2.64 7 1 ARG A 171 ? A 152.99 55.23 8 1 LYS A 173 ? ? 63.31 -156.87 9 1 HIS A 208 ? ? -162.51 108.79 # loop_ _pdbx_validate_peptide_omega.id _pdbx_validate_peptide_omega.PDB_model_num _pdbx_validate_peptide_omega.auth_comp_id_1 _pdbx_validate_peptide_omega.auth_asym_id_1 _pdbx_validate_peptide_omega.auth_seq_id_1 _pdbx_validate_peptide_omega.PDB_ins_code_1 _pdbx_validate_peptide_omega.label_alt_id_1 _pdbx_validate_peptide_omega.auth_comp_id_2 _pdbx_validate_peptide_omega.auth_asym_id_2 _pdbx_validate_peptide_omega.auth_seq_id_2 _pdbx_validate_peptide_omega.PDB_ins_code_2 _pdbx_validate_peptide_omega.label_alt_id_2 _pdbx_validate_peptide_omega.omega 1 1 PHE A 166 ? A GLU A 167 ? A 135.93 2 1 GLU A 167 ? B ALA A 168 ? B 127.17 3 1 SER A 169 ? A ASP A 170 ? A 144.35 4 1 ASP A 170 ? A ARG A 171 ? A -118.80 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 'COPPER (II) ION' CU 3 N-ACETYL-D-GLUCOSAMINE NAG 4 'ZINC ION' ZN 5 'ISOPROPYL ALCOHOL' IPA 6 GLYCEROL GOL 7 'ACETATE ION' ACT 8 water HOH #